data_9JIR
# 
_entry.id   9JIR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9JIR         pdb_00009jir 10.2210/pdb9jir/pdb 
WWPDB D_1300051390 ?            ?                   
# 
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 
1 'Structure model' 1 0 2025-01-22 
2 'Structure model' 1 1 2025-02-05 
# 
_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.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JIR 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-12 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tyokoya3@pha.u-toyama.ac.jp 
_pdbx_contact_author.name_first         Takeshi 
_pdbx_contact_author.name_last          Yokoyama 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5362-8606 
# 
_audit_author.name               'Yokoyama, T.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                1572 
_citation.page_last                 1586 
_citation.title                     'Repurposing of Agrochemicals as ATTRv Amyloidosis Inhibitors.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02221 
_citation.pdbx_database_id_PubMed   39761163 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yokoyama, T.'  1 ? 
primary 'Fujiwara, S.'  2 ? 
primary 'Nishikubo, K.' 3 ? 
primary 'Mizuguchi, M.' 4 ? 
primary 'Nabeshima, Y.' 5 ? 
primary 'Toyooka, N.'   6 ? 
primary 'Okada, T.'     7 ? 
primary 'Nakagawa, Y.'  8 ? 
# 
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 Transthyretin 17342.582 2   ? V30M ? ? 
2 non-polymer syn ioxynil       370.914   3   ? ?    ? ? 
3 water       nat water         18.015    221 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        ATTR,Prealbumin,TBPA 
# 
_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       
;MRGSHHHHHHGSMASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGK
TSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRGSHHHHHHGSMASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAMHVFRKAADDTWEPFASGK
TSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 ioxynil A1L37 
3 water   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ARG n 
1 3   GLY n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  GLY n 
1 12  SER n 
1 13  MET n 
1 14  ALA n 
1 15  SER n 
1 16  HIS n 
1 17  ARG n 
1 18  LEU n 
1 19  LEU n 
1 20  LEU n 
1 21  LEU n 
1 22  CYS n 
1 23  LEU n 
1 24  ALA n 
1 25  GLY n 
1 26  LEU n 
1 27  VAL n 
1 28  PHE n 
1 29  VAL n 
1 30  SER n 
1 31  GLU n 
1 32  ALA n 
1 33  GLY n 
1 34  PRO n 
1 35  THR n 
1 36  GLY n 
1 37  THR n 
1 38  GLY n 
1 39  GLU n 
1 40  SER n 
1 41  LYS n 
1 42  CYS n 
1 43  PRO n 
1 44  LEU n 
1 45  MET n 
1 46  VAL n 
1 47  LYS n 
1 48  VAL n 
1 49  LEU n 
1 50  ASP n 
1 51  ALA n 
1 52  VAL n 
1 53  ARG n 
1 54  GLY n 
1 55  SER n 
1 56  PRO n 
1 57  ALA n 
1 58  ILE n 
1 59  ASN n 
1 60  VAL n 
1 61  ALA n 
1 62  MET n 
1 63  HIS n 
1 64  VAL n 
1 65  PHE n 
1 66  ARG n 
1 67  LYS n 
1 68  ALA n 
1 69  ALA n 
1 70  ASP n 
1 71  ASP n 
1 72  THR n 
1 73  TRP n 
1 74  GLU n 
1 75  PRO n 
1 76  PHE n 
1 77  ALA n 
1 78  SER n 
1 79  GLY n 
1 80  LYS n 
1 81  THR n 
1 82  SER n 
1 83  GLU n 
1 84  SER n 
1 85  GLY n 
1 86  GLU n 
1 87  LEU n 
1 88  HIS n 
1 89  GLY n 
1 90  LEU n 
1 91  THR n 
1 92  THR n 
1 93  GLU n 
1 94  GLU n 
1 95  GLU n 
1 96  PHE n 
1 97  VAL n 
1 98  GLU n 
1 99  GLY n 
1 100 ILE n 
1 101 TYR n 
1 102 LYS n 
1 103 VAL n 
1 104 GLU n 
1 105 ILE n 
1 106 ASP n 
1 107 THR n 
1 108 LYS n 
1 109 SER n 
1 110 TYR n 
1 111 TRP n 
1 112 LYS n 
1 113 ALA n 
1 114 LEU n 
1 115 GLY n 
1 116 ILE n 
1 117 SER n 
1 118 PRO n 
1 119 PHE n 
1 120 HIS n 
1 121 GLU n 
1 122 HIS n 
1 123 ALA n 
1 124 GLU n 
1 125 VAL n 
1 126 VAL n 
1 127 PHE n 
1 128 THR n 
1 129 ALA n 
1 130 ASN n 
1 131 ASP n 
1 132 SER n 
1 133 GLY n 
1 134 PRO n 
1 135 ARG n 
1 136 ARG n 
1 137 TYR n 
1 138 THR n 
1 139 ILE n 
1 140 ALA n 
1 141 ALA n 
1 142 LEU n 
1 143 LEU n 
1 144 SER n 
1 145 PRO n 
1 146 TYR n 
1 147 SER n 
1 148 TYR n 
1 149 SER n 
1 150 THR n 
1 151 THR n 
1 152 ALA n 
1 153 VAL n 
1 154 VAL n 
1 155 THR n 
1 156 ASN n 
1 157 PRO n 
1 158 LYS n 
1 159 GLU 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                   159 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TTR, PALB' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1L37 non-polymer         . ioxynil         '3,5-bis(iodanyl)-4-oxidanyl-benzenecarbonitrile' 'C7 H3 I2 N O'   370.914 
ALA   'L-peptide linking' y ALANINE         ?                                                 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE        ?                                                 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE      ?                                                 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                                                 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE        ?                                                 'C3 H7 N O2 S'   121.158 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                                                 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE         ?                                                 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE       ?                                                 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER           ?                                                 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE      ?                                                 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE         ?                                                 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE          ?                                                 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE      ?                                                 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE   ?                                                 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE         ?                                                 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE          ?                                                 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE       ?                                                 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN      ?                                                 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE        ?                                                 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE          ?                                                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -31 ?   ?   ?   A . n 
A 1 2   ARG 2   -30 ?   ?   ?   A . n 
A 1 3   GLY 3   -29 ?   ?   ?   A . n 
A 1 4   SER 4   -28 ?   ?   ?   A . n 
A 1 5   HIS 5   -27 ?   ?   ?   A . n 
A 1 6   HIS 6   -26 ?   ?   ?   A . n 
A 1 7   HIS 7   -25 ?   ?   ?   A . n 
A 1 8   HIS 8   -24 ?   ?   ?   A . n 
A 1 9   HIS 9   -23 ?   ?   ?   A . n 
A 1 10  HIS 10  -22 ?   ?   ?   A . n 
A 1 11  GLY 11  -21 ?   ?   ?   A . n 
A 1 12  SER 12  -20 ?   ?   ?   A . n 
A 1 13  MET 13  -19 ?   ?   ?   A . n 
A 1 14  ALA 14  -18 ?   ?   ?   A . n 
A 1 15  SER 15  -17 ?   ?   ?   A . n 
A 1 16  HIS 16  -16 ?   ?   ?   A . n 
A 1 17  ARG 17  -15 ?   ?   ?   A . n 
A 1 18  LEU 18  -14 ?   ?   ?   A . n 
A 1 19  LEU 19  -13 ?   ?   ?   A . n 
A 1 20  LEU 20  -12 ?   ?   ?   A . n 
A 1 21  LEU 21  -11 ?   ?   ?   A . n 
A 1 22  CYS 22  -10 ?   ?   ?   A . n 
A 1 23  LEU 23  -9  ?   ?   ?   A . n 
A 1 24  ALA 24  -8  ?   ?   ?   A . n 
A 1 25  GLY 25  -7  ?   ?   ?   A . n 
A 1 26  LEU 26  -6  ?   ?   ?   A . n 
A 1 27  VAL 27  -5  ?   ?   ?   A . n 
A 1 28  PHE 28  -4  ?   ?   ?   A . n 
A 1 29  VAL 29  -3  ?   ?   ?   A . n 
A 1 30  SER 30  -2  ?   ?   ?   A . n 
A 1 31  GLU 31  -1  ?   ?   ?   A . n 
A 1 32  ALA 32  0   ?   ?   ?   A . n 
A 1 33  GLY 33  1   ?   ?   ?   A . n 
A 1 34  PRO 34  2   ?   ?   ?   A . n 
A 1 35  THR 35  3   ?   ?   ?   A . n 
A 1 36  GLY 36  4   ?   ?   ?   A . n 
A 1 37  THR 37  5   ?   ?   ?   A . n 
A 1 38  GLY 38  6   ?   ?   ?   A . n 
A 1 39  GLU 39  7   ?   ?   ?   A . n 
A 1 40  SER 40  8   ?   ?   ?   A . n 
A 1 41  LYS 41  9   ?   ?   ?   A . n 
A 1 42  CYS 42  10  10  CYS CYS A . n 
A 1 43  PRO 43  11  11  PRO PRO A . n 
A 1 44  LEU 44  12  12  LEU LEU A . n 
A 1 45  MET 45  13  13  MET MET A . n 
A 1 46  VAL 46  14  14  VAL VAL A . n 
A 1 47  LYS 47  15  15  LYS LYS A . n 
A 1 48  VAL 48  16  16  VAL VAL A . n 
A 1 49  LEU 49  17  17  LEU LEU A . n 
A 1 50  ASP 50  18  18  ASP ASP A . n 
A 1 51  ALA 51  19  19  ALA ALA A . n 
A 1 52  VAL 52  20  20  VAL VAL A . n 
A 1 53  ARG 53  21  21  ARG ARG A . n 
A 1 54  GLY 54  22  22  GLY GLY A . n 
A 1 55  SER 55  23  23  SER SER A . n 
A 1 56  PRO 56  24  24  PRO PRO A . n 
A 1 57  ALA 57  25  25  ALA ALA A . n 
A 1 58  ILE 58  26  26  ILE ILE A . n 
A 1 59  ASN 59  27  27  ASN ASN A . n 
A 1 60  VAL 60  28  28  VAL VAL A . n 
A 1 61  ALA 61  29  29  ALA ALA A . n 
A 1 62  MET 62  30  30  MET MET A . n 
A 1 63  HIS 63  31  31  HIS HIS A . n 
A 1 64  VAL 64  32  32  VAL VAL A . n 
A 1 65  PHE 65  33  33  PHE PHE A . n 
A 1 66  ARG 66  34  34  ARG ARG A . n 
A 1 67  LYS 67  35  35  LYS LYS A . n 
A 1 68  ALA 68  36  36  ALA ALA A . n 
A 1 69  ALA 69  37  37  ALA ALA A . n 
A 1 70  ASP 70  38  38  ASP ASP A . n 
A 1 71  ASP 71  39  39  ASP ASP A . n 
A 1 72  THR 72  40  40  THR THR A . n 
A 1 73  TRP 73  41  41  TRP TRP A . n 
A 1 74  GLU 74  42  42  GLU GLU A . n 
A 1 75  PRO 75  43  43  PRO PRO A . n 
A 1 76  PHE 76  44  44  PHE PHE A . n 
A 1 77  ALA 77  45  45  ALA ALA A . n 
A 1 78  SER 78  46  46  SER SER A . n 
A 1 79  GLY 79  47  47  GLY GLY A . n 
A 1 80  LYS 80  48  48  LYS LYS A . n 
A 1 81  THR 81  49  49  THR THR A . n 
A 1 82  SER 82  50  50  SER SER A . n 
A 1 83  GLU 83  51  51  GLU GLU A . n 
A 1 84  SER 84  52  52  SER SER A . n 
A 1 85  GLY 85  53  53  GLY GLY A . n 
A 1 86  GLU 86  54  54  GLU GLU A . n 
A 1 87  LEU 87  55  55  LEU LEU A . n 
A 1 88  HIS 88  56  56  HIS HIS A . n 
A 1 89  GLY 89  57  57  GLY GLY A . n 
A 1 90  LEU 90  58  58  LEU LEU A . n 
A 1 91  THR 91  59  59  THR THR A . n 
A 1 92  THR 92  60  60  THR THR A . n 
A 1 93  GLU 93  61  61  GLU GLU A . n 
A 1 94  GLU 94  62  62  GLU GLU A . n 
A 1 95  GLU 95  63  63  GLU GLU A . n 
A 1 96  PHE 96  64  64  PHE PHE A . n 
A 1 97  VAL 97  65  65  VAL VAL A . n 
A 1 98  GLU 98  66  66  GLU GLU A . n 
A 1 99  GLY 99  67  67  GLY GLY A . n 
A 1 100 ILE 100 68  68  ILE ILE A . n 
A 1 101 TYR 101 69  69  TYR TYR A . n 
A 1 102 LYS 102 70  70  LYS LYS A . n 
A 1 103 VAL 103 71  71  VAL VAL A . n 
A 1 104 GLU 104 72  72  GLU GLU A . n 
A 1 105 ILE 105 73  73  ILE ILE A . n 
A 1 106 ASP 106 74  74  ASP ASP A . n 
A 1 107 THR 107 75  75  THR THR A . n 
A 1 108 LYS 108 76  76  LYS LYS A . n 
A 1 109 SER 109 77  77  SER SER A . n 
A 1 110 TYR 110 78  78  TYR TYR A . n 
A 1 111 TRP 111 79  79  TRP TRP A . n 
A 1 112 LYS 112 80  80  LYS LYS A . n 
A 1 113 ALA 113 81  81  ALA ALA A . n 
A 1 114 LEU 114 82  82  LEU LEU A . n 
A 1 115 GLY 115 83  83  GLY GLY A . n 
A 1 116 ILE 116 84  84  ILE ILE A . n 
A 1 117 SER 117 85  85  SER SER A . n 
A 1 118 PRO 118 86  86  PRO PRO A . n 
A 1 119 PHE 119 87  87  PHE PHE A . n 
A 1 120 HIS 120 88  88  HIS HIS A . n 
A 1 121 GLU 121 89  89  GLU GLU A . n 
A 1 122 HIS 122 90  90  HIS HIS A . n 
A 1 123 ALA 123 91  91  ALA ALA A . n 
A 1 124 GLU 124 92  92  GLU GLU A . n 
A 1 125 VAL 125 93  93  VAL VAL A . n 
A 1 126 VAL 126 94  94  VAL VAL A . n 
A 1 127 PHE 127 95  95  PHE PHE A . n 
A 1 128 THR 128 96  96  THR THR A . n 
A 1 129 ALA 129 97  97  ALA ALA A . n 
A 1 130 ASN 130 98  98  ASN ASN A . n 
A 1 131 ASP 131 99  99  ASP ASP A . n 
A 1 132 SER 132 100 100 SER SER A . n 
A 1 133 GLY 133 101 101 GLY GLY A . n 
A 1 134 PRO 134 102 102 PRO PRO A . n 
A 1 135 ARG 135 103 103 ARG ARG A . n 
A 1 136 ARG 136 104 104 ARG ARG A . n 
A 1 137 TYR 137 105 105 TYR TYR A . n 
A 1 138 THR 138 106 106 THR THR A . n 
A 1 139 ILE 139 107 107 ILE ILE A . n 
A 1 140 ALA 140 108 108 ALA ALA A . n 
A 1 141 ALA 141 109 109 ALA ALA A . n 
A 1 142 LEU 142 110 110 LEU LEU A . n 
A 1 143 LEU 143 111 111 LEU LEU A . n 
A 1 144 SER 144 112 112 SER SER A . n 
A 1 145 PRO 145 113 113 PRO PRO A . n 
A 1 146 TYR 146 114 114 TYR TYR A . n 
A 1 147 SER 147 115 115 SER SER A . n 
A 1 148 TYR 148 116 116 TYR TYR A . n 
A 1 149 SER 149 117 117 SER SER A . n 
A 1 150 THR 150 118 118 THR THR A . n 
A 1 151 THR 151 119 119 THR THR A . n 
A 1 152 ALA 152 120 120 ALA ALA A . n 
A 1 153 VAL 153 121 121 VAL VAL A . n 
A 1 154 VAL 154 122 122 VAL VAL A . n 
A 1 155 THR 155 123 123 THR THR A . n 
A 1 156 ASN 156 124 124 ASN ASN A . n 
A 1 157 PRO 157 125 125 PRO PRO A . n 
A 1 158 LYS 158 126 ?   ?   ?   A . n 
A 1 159 GLU 159 127 ?   ?   ?   A . n 
B 1 1   MET 1   -31 ?   ?   ?   B . n 
B 1 2   ARG 2   -30 ?   ?   ?   B . n 
B 1 3   GLY 3   -29 ?   ?   ?   B . n 
B 1 4   SER 4   -28 ?   ?   ?   B . n 
B 1 5   HIS 5   -27 ?   ?   ?   B . n 
B 1 6   HIS 6   -26 ?   ?   ?   B . n 
B 1 7   HIS 7   -25 ?   ?   ?   B . n 
B 1 8   HIS 8   -24 ?   ?   ?   B . n 
B 1 9   HIS 9   -23 ?   ?   ?   B . n 
B 1 10  HIS 10  -22 ?   ?   ?   B . n 
B 1 11  GLY 11  -21 ?   ?   ?   B . n 
B 1 12  SER 12  -20 ?   ?   ?   B . n 
B 1 13  MET 13  -19 ?   ?   ?   B . n 
B 1 14  ALA 14  -18 ?   ?   ?   B . n 
B 1 15  SER 15  -17 ?   ?   ?   B . n 
B 1 16  HIS 16  -16 ?   ?   ?   B . n 
B 1 17  ARG 17  -15 ?   ?   ?   B . n 
B 1 18  LEU 18  -14 ?   ?   ?   B . n 
B 1 19  LEU 19  -13 ?   ?   ?   B . n 
B 1 20  LEU 20  -12 ?   ?   ?   B . n 
B 1 21  LEU 21  -11 ?   ?   ?   B . n 
B 1 22  CYS 22  -10 ?   ?   ?   B . n 
B 1 23  LEU 23  -9  ?   ?   ?   B . n 
B 1 24  ALA 24  -8  ?   ?   ?   B . n 
B 1 25  GLY 25  -7  ?   ?   ?   B . n 
B 1 26  LEU 26  -6  ?   ?   ?   B . n 
B 1 27  VAL 27  -5  ?   ?   ?   B . n 
B 1 28  PHE 28  -4  ?   ?   ?   B . n 
B 1 29  VAL 29  -3  ?   ?   ?   B . n 
B 1 30  SER 30  -2  ?   ?   ?   B . n 
B 1 31  GLU 31  -1  ?   ?   ?   B . n 
B 1 32  ALA 32  0   ?   ?   ?   B . n 
B 1 33  GLY 33  1   ?   ?   ?   B . n 
B 1 34  PRO 34  2   ?   ?   ?   B . n 
B 1 35  THR 35  3   ?   ?   ?   B . n 
B 1 36  GLY 36  4   ?   ?   ?   B . n 
B 1 37  THR 37  5   ?   ?   ?   B . n 
B 1 38  GLY 38  6   ?   ?   ?   B . n 
B 1 39  GLU 39  7   ?   ?   ?   B . n 
B 1 40  SER 40  8   ?   ?   ?   B . n 
B 1 41  LYS 41  9   ?   ?   ?   B . n 
B 1 42  CYS 42  10  10  CYS CYS B . n 
B 1 43  PRO 43  11  11  PRO PRO B . n 
B 1 44  LEU 44  12  12  LEU LEU B . n 
B 1 45  MET 45  13  13  MET MET B . n 
B 1 46  VAL 46  14  14  VAL VAL B . n 
B 1 47  LYS 47  15  15  LYS LYS B . n 
B 1 48  VAL 48  16  16  VAL VAL B . n 
B 1 49  LEU 49  17  17  LEU LEU B . n 
B 1 50  ASP 50  18  18  ASP ASP B . n 
B 1 51  ALA 51  19  19  ALA ALA B . n 
B 1 52  VAL 52  20  20  VAL VAL B . n 
B 1 53  ARG 53  21  21  ARG ARG B . n 
B 1 54  GLY 54  22  22  GLY GLY B . n 
B 1 55  SER 55  23  23  SER SER B . n 
B 1 56  PRO 56  24  24  PRO PRO B . n 
B 1 57  ALA 57  25  25  ALA ALA B . n 
B 1 58  ILE 58  26  26  ILE ILE B . n 
B 1 59  ASN 59  27  27  ASN ASN B . n 
B 1 60  VAL 60  28  28  VAL VAL B . n 
B 1 61  ALA 61  29  29  ALA ALA B . n 
B 1 62  MET 62  30  30  MET MET B . n 
B 1 63  HIS 63  31  31  HIS HIS B . n 
B 1 64  VAL 64  32  32  VAL VAL B . n 
B 1 65  PHE 65  33  33  PHE PHE B . n 
B 1 66  ARG 66  34  34  ARG ARG B . n 
B 1 67  LYS 67  35  35  LYS LYS B . n 
B 1 68  ALA 68  36  36  ALA ALA B . n 
B 1 69  ALA 69  37  37  ALA ALA B . n 
B 1 70  ASP 70  38  38  ASP ASP B . n 
B 1 71  ASP 71  39  39  ASP ASP B . n 
B 1 72  THR 72  40  40  THR THR B . n 
B 1 73  TRP 73  41  41  TRP TRP B . n 
B 1 74  GLU 74  42  42  GLU GLU B . n 
B 1 75  PRO 75  43  43  PRO PRO B . n 
B 1 76  PHE 76  44  44  PHE PHE B . n 
B 1 77  ALA 77  45  45  ALA ALA B . n 
B 1 78  SER 78  46  46  SER SER B . n 
B 1 79  GLY 79  47  47  GLY GLY B . n 
B 1 80  LYS 80  48  48  LYS LYS B . n 
B 1 81  THR 81  49  49  THR THR B . n 
B 1 82  SER 82  50  50  SER SER B . n 
B 1 83  GLU 83  51  51  GLU GLU B . n 
B 1 84  SER 84  52  52  SER SER B . n 
B 1 85  GLY 85  53  53  GLY GLY B . n 
B 1 86  GLU 86  54  54  GLU GLU B . n 
B 1 87  LEU 87  55  55  LEU LEU B . n 
B 1 88  HIS 88  56  56  HIS HIS B . n 
B 1 89  GLY 89  57  57  GLY GLY B . n 
B 1 90  LEU 90  58  58  LEU LEU B . n 
B 1 91  THR 91  59  59  THR THR B . n 
B 1 92  THR 92  60  60  THR THR B . n 
B 1 93  GLU 93  61  61  GLU GLU B . n 
B 1 94  GLU 94  62  62  GLU GLU B . n 
B 1 95  GLU 95  63  63  GLU GLU B . n 
B 1 96  PHE 96  64  64  PHE PHE B . n 
B 1 97  VAL 97  65  65  VAL VAL B . n 
B 1 98  GLU 98  66  66  GLU GLU B . n 
B 1 99  GLY 99  67  67  GLY GLY B . n 
B 1 100 ILE 100 68  68  ILE ILE B . n 
B 1 101 TYR 101 69  69  TYR TYR B . n 
B 1 102 LYS 102 70  70  LYS LYS B . n 
B 1 103 VAL 103 71  71  VAL VAL B . n 
B 1 104 GLU 104 72  72  GLU GLU B . n 
B 1 105 ILE 105 73  73  ILE ILE B . n 
B 1 106 ASP 106 74  74  ASP ASP B . n 
B 1 107 THR 107 75  75  THR THR B . n 
B 1 108 LYS 108 76  76  LYS LYS B . n 
B 1 109 SER 109 77  77  SER SER B . n 
B 1 110 TYR 110 78  78  TYR TYR B . n 
B 1 111 TRP 111 79  79  TRP TRP B . n 
B 1 112 LYS 112 80  80  LYS LYS B . n 
B 1 113 ALA 113 81  81  ALA ALA B . n 
B 1 114 LEU 114 82  82  LEU LEU B . n 
B 1 115 GLY 115 83  83  GLY GLY B . n 
B 1 116 ILE 116 84  84  ILE ILE B . n 
B 1 117 SER 117 85  85  SER SER B . n 
B 1 118 PRO 118 86  86  PRO PRO B . n 
B 1 119 PHE 119 87  87  PHE PHE B . n 
B 1 120 HIS 120 88  88  HIS HIS B . n 
B 1 121 GLU 121 89  89  GLU GLU B . n 
B 1 122 HIS 122 90  90  HIS HIS B . n 
B 1 123 ALA 123 91  91  ALA ALA B . n 
B 1 124 GLU 124 92  92  GLU GLU B . n 
B 1 125 VAL 125 93  93  VAL VAL B . n 
B 1 126 VAL 126 94  94  VAL VAL B . n 
B 1 127 PHE 127 95  95  PHE PHE B . n 
B 1 128 THR 128 96  96  THR THR B . n 
B 1 129 ALA 129 97  97  ALA ALA B . n 
B 1 130 ASN 130 98  98  ASN ASN B . n 
B 1 131 ASP 131 99  99  ASP ASP B . n 
B 1 132 SER 132 100 100 SER SER B . n 
B 1 133 GLY 133 101 101 GLY GLY B . n 
B 1 134 PRO 134 102 102 PRO PRO B . n 
B 1 135 ARG 135 103 103 ARG ARG B . n 
B 1 136 ARG 136 104 104 ARG ARG B . n 
B 1 137 TYR 137 105 105 TYR TYR B . n 
B 1 138 THR 138 106 106 THR THR B . n 
B 1 139 ILE 139 107 107 ILE ILE B . n 
B 1 140 ALA 140 108 108 ALA ALA B . n 
B 1 141 ALA 141 109 109 ALA ALA B . n 
B 1 142 LEU 142 110 110 LEU LEU B . n 
B 1 143 LEU 143 111 111 LEU LEU B . n 
B 1 144 SER 144 112 112 SER SER B . n 
B 1 145 PRO 145 113 113 PRO PRO B . n 
B 1 146 TYR 146 114 114 TYR TYR B . n 
B 1 147 SER 147 115 115 SER SER B . n 
B 1 148 TYR 148 116 116 TYR TYR B . n 
B 1 149 SER 149 117 117 SER SER B . n 
B 1 150 THR 150 118 118 THR THR B . n 
B 1 151 THR 151 119 119 THR THR B . n 
B 1 152 ALA 152 120 120 ALA ALA B . n 
B 1 153 VAL 153 121 121 VAL VAL B . n 
B 1 154 VAL 154 122 122 VAL VAL B . n 
B 1 155 THR 155 123 123 THR THR B . n 
B 1 156 ASN 156 124 124 ASN ASN B . n 
B 1 157 PRO 157 125 125 PRO PRO B . n 
B 1 158 LYS 158 126 ?   ?   ?   B . n 
B 1 159 GLU 159 127 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L37 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L37 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1L37 1   201 201 A1L37 DRG A . 
D 2 A1L37 1   202 202 A1L37 DRG A . 
E 2 A1L37 1   201 201 A1L37 DRG B . 
F 3 HOH   1   301 132 HOH   HOH A . 
F 3 HOH   2   302 13  HOH   HOH A . 
F 3 HOH   3   303 75  HOH   HOH A . 
F 3 HOH   4   304 152 HOH   HOH A . 
F 3 HOH   5   305 120 HOH   HOH A . 
F 3 HOH   6   306 126 HOH   HOH A . 
F 3 HOH   7   307 170 HOH   HOH A . 
F 3 HOH   8   308 19  HOH   HOH A . 
F 3 HOH   9   309 171 HOH   HOH A . 
F 3 HOH   10  310 44  HOH   HOH A . 
F 3 HOH   11  311 28  HOH   HOH A . 
F 3 HOH   12  312 1   HOH   HOH A . 
F 3 HOH   13  313 15  HOH   HOH A . 
F 3 HOH   14  314 196 HOH   HOH A . 
F 3 HOH   15  315 5   HOH   HOH A . 
F 3 HOH   16  316 94  HOH   HOH A . 
F 3 HOH   17  317 96  HOH   HOH A . 
F 3 HOH   18  318 65  HOH   HOH A . 
F 3 HOH   19  319 117 HOH   HOH A . 
F 3 HOH   20  320 66  HOH   HOH A . 
F 3 HOH   21  321 176 HOH   HOH A . 
F 3 HOH   22  322 87  HOH   HOH A . 
F 3 HOH   23  323 27  HOH   HOH A . 
F 3 HOH   24  324 14  HOH   HOH A . 
F 3 HOH   25  325 78  HOH   HOH A . 
F 3 HOH   26  326 213 HOH   HOH A . 
F 3 HOH   27  327 47  HOH   HOH A . 
F 3 HOH   28  328 37  HOH   HOH A . 
F 3 HOH   29  329 225 HOH   HOH A . 
F 3 HOH   30  330 7   HOH   HOH A . 
F 3 HOH   31  331 69  HOH   HOH A . 
F 3 HOH   32  332 173 HOH   HOH A . 
F 3 HOH   33  333 31  HOH   HOH A . 
F 3 HOH   34  334 23  HOH   HOH A . 
F 3 HOH   35  335 45  HOH   HOH A . 
F 3 HOH   36  336 68  HOH   HOH A . 
F 3 HOH   37  337 26  HOH   HOH A . 
F 3 HOH   38  338 62  HOH   HOH A . 
F 3 HOH   39  339 100 HOH   HOH A . 
F 3 HOH   40  340 8   HOH   HOH A . 
F 3 HOH   41  341 3   HOH   HOH A . 
F 3 HOH   42  342 52  HOH   HOH A . 
F 3 HOH   43  343 149 HOH   HOH A . 
F 3 HOH   44  344 84  HOH   HOH A . 
F 3 HOH   45  345 208 HOH   HOH A . 
F 3 HOH   46  346 190 HOH   HOH A . 
F 3 HOH   47  347 72  HOH   HOH A . 
F 3 HOH   48  348 51  HOH   HOH A . 
F 3 HOH   49  349 29  HOH   HOH A . 
F 3 HOH   50  350 39  HOH   HOH A . 
F 3 HOH   51  351 58  HOH   HOH A . 
F 3 HOH   52  352 92  HOH   HOH A . 
F 3 HOH   53  353 162 HOH   HOH A . 
F 3 HOH   54  354 136 HOH   HOH A . 
F 3 HOH   55  355 30  HOH   HOH A . 
F 3 HOH   56  356 46  HOH   HOH A . 
F 3 HOH   57  357 103 HOH   HOH A . 
F 3 HOH   58  358 139 HOH   HOH A . 
F 3 HOH   59  359 70  HOH   HOH A . 
F 3 HOH   60  360 12  HOH   HOH A . 
F 3 HOH   61  361 115 HOH   HOH A . 
F 3 HOH   62  362 21  HOH   HOH A . 
F 3 HOH   63  363 123 HOH   HOH A . 
F 3 HOH   64  364 147 HOH   HOH A . 
F 3 HOH   65  365 124 HOH   HOH A . 
F 3 HOH   66  366 105 HOH   HOH A . 
F 3 HOH   67  367 107 HOH   HOH A . 
F 3 HOH   68  368 168 HOH   HOH A . 
F 3 HOH   69  369 63  HOH   HOH A . 
F 3 HOH   70  370 226 HOH   HOH A . 
F 3 HOH   71  371 181 HOH   HOH A . 
F 3 HOH   72  372 141 HOH   HOH A . 
F 3 HOH   73  373 93  HOH   HOH A . 
F 3 HOH   74  374 211 HOH   HOH A . 
F 3 HOH   75  375 150 HOH   HOH A . 
F 3 HOH   76  376 114 HOH   HOH A . 
F 3 HOH   77  377 193 HOH   HOH A . 
F 3 HOH   78  378 74  HOH   HOH A . 
F 3 HOH   79  379 157 HOH   HOH A . 
F 3 HOH   80  380 166 HOH   HOH A . 
F 3 HOH   81  381 129 HOH   HOH A . 
F 3 HOH   82  382 143 HOH   HOH A . 
F 3 HOH   83  383 145 HOH   HOH A . 
F 3 HOH   84  384 202 HOH   HOH A . 
F 3 HOH   85  385 180 HOH   HOH A . 
F 3 HOH   86  386 111 HOH   HOH A . 
F 3 HOH   87  387 192 HOH   HOH A . 
F 3 HOH   88  388 197 HOH   HOH A . 
F 3 HOH   89  389 49  HOH   HOH A . 
F 3 HOH   90  390 108 HOH   HOH A . 
F 3 HOH   91  391 187 HOH   HOH A . 
F 3 HOH   92  392 198 HOH   HOH A . 
F 3 HOH   93  393 106 HOH   HOH A . 
F 3 HOH   94  394 89  HOH   HOH A . 
F 3 HOH   95  395 222 HOH   HOH A . 
F 3 HOH   96  396 101 HOH   HOH A . 
F 3 HOH   97  397 82  HOH   HOH A . 
F 3 HOH   98  398 183 HOH   HOH A . 
F 3 HOH   99  399 178 HOH   HOH A . 
F 3 HOH   100 400 172 HOH   HOH A . 
F 3 HOH   101 401 185 HOH   HOH A . 
F 3 HOH   102 402 158 HOH   HOH A . 
F 3 HOH   103 403 191 HOH   HOH A . 
F 3 HOH   104 404 165 HOH   HOH A . 
F 3 HOH   105 405 189 HOH   HOH A . 
G 3 HOH   1   301 142 HOH   HOH B . 
G 3 HOH   2   302 128 HOH   HOH B . 
G 3 HOH   3   303 119 HOH   HOH B . 
G 3 HOH   4   304 146 HOH   HOH B . 
G 3 HOH   5   305 217 HOH   HOH B . 
G 3 HOH   6   306 60  HOH   HOH B . 
G 3 HOH   7   307 86  HOH   HOH B . 
G 3 HOH   8   308 10  HOH   HOH B . 
G 3 HOH   9   309 186 HOH   HOH B . 
G 3 HOH   10  310 153 HOH   HOH B . 
G 3 HOH   11  311 194 HOH   HOH B . 
G 3 HOH   12  312 210 HOH   HOH B . 
G 3 HOH   13  313 102 HOH   HOH B . 
G 3 HOH   14  314 42  HOH   HOH B . 
G 3 HOH   15  315 104 HOH   HOH B . 
G 3 HOH   16  316 140 HOH   HOH B . 
G 3 HOH   17  317 24  HOH   HOH B . 
G 3 HOH   18  318 18  HOH   HOH B . 
G 3 HOH   19  319 169 HOH   HOH B . 
G 3 HOH   20  320 110 HOH   HOH B . 
G 3 HOH   21  321 22  HOH   HOH B . 
G 3 HOH   22  322 4   HOH   HOH B . 
G 3 HOH   23  323 2   HOH   HOH B . 
G 3 HOH   24  324 182 HOH   HOH B . 
G 3 HOH   25  325 50  HOH   HOH B . 
G 3 HOH   26  326 209 HOH   HOH B . 
G 3 HOH   27  327 164 HOH   HOH B . 
G 3 HOH   28  328 53  HOH   HOH B . 
G 3 HOH   29  329 167 HOH   HOH B . 
G 3 HOH   30  330 137 HOH   HOH B . 
G 3 HOH   31  331 16  HOH   HOH B . 
G 3 HOH   32  332 9   HOH   HOH B . 
G 3 HOH   33  333 64  HOH   HOH B . 
G 3 HOH   34  334 138 HOH   HOH B . 
G 3 HOH   35  335 36  HOH   HOH B . 
G 3 HOH   36  336 116 HOH   HOH B . 
G 3 HOH   37  337 48  HOH   HOH B . 
G 3 HOH   38  338 121 HOH   HOH B . 
G 3 HOH   39  339 56  HOH   HOH B . 
G 3 HOH   40  340 17  HOH   HOH B . 
G 3 HOH   41  341 11  HOH   HOH B . 
G 3 HOH   42  342 207 HOH   HOH B . 
G 3 HOH   43  343 151 HOH   HOH B . 
G 3 HOH   44  344 55  HOH   HOH B . 
G 3 HOH   45  345 59  HOH   HOH B . 
G 3 HOH   46  346 6   HOH   HOH B . 
G 3 HOH   47  347 127 HOH   HOH B . 
G 3 HOH   48  348 122 HOH   HOH B . 
G 3 HOH   49  349 77  HOH   HOH B . 
G 3 HOH   50  350 175 HOH   HOH B . 
G 3 HOH   51  351 73  HOH   HOH B . 
G 3 HOH   52  352 25  HOH   HOH B . 
G 3 HOH   53  353 54  HOH   HOH B . 
G 3 HOH   54  354 216 HOH   HOH B . 
G 3 HOH   55  355 118 HOH   HOH B . 
G 3 HOH   56  356 81  HOH   HOH B . 
G 3 HOH   57  357 34  HOH   HOH B . 
G 3 HOH   58  358 79  HOH   HOH B . 
G 3 HOH   59  359 41  HOH   HOH B . 
G 3 HOH   60  360 125 HOH   HOH B . 
G 3 HOH   61  361 163 HOH   HOH B . 
G 3 HOH   62  362 67  HOH   HOH B . 
G 3 HOH   63  363 38  HOH   HOH B . 
G 3 HOH   64  364 90  HOH   HOH B . 
G 3 HOH   65  365 20  HOH   HOH B . 
G 3 HOH   66  366 43  HOH   HOH B . 
G 3 HOH   67  367 184 HOH   HOH B . 
G 3 HOH   68  368 33  HOH   HOH B . 
G 3 HOH   69  369 40  HOH   HOH B . 
G 3 HOH   70  370 98  HOH   HOH B . 
G 3 HOH   71  371 35  HOH   HOH B . 
G 3 HOH   72  372 131 HOH   HOH B . 
G 3 HOH   73  373 80  HOH   HOH B . 
G 3 HOH   74  374 203 HOH   HOH B . 
G 3 HOH   75  375 159 HOH   HOH B . 
G 3 HOH   76  376 91  HOH   HOH B . 
G 3 HOH   77  377 156 HOH   HOH B . 
G 3 HOH   78  378 174 HOH   HOH B . 
G 3 HOH   79  379 161 HOH   HOH B . 
G 3 HOH   80  380 218 HOH   HOH B . 
G 3 HOH   81  381 201 HOH   HOH B . 
G 3 HOH   82  382 188 HOH   HOH B . 
G 3 HOH   83  383 179 HOH   HOH B . 
G 3 HOH   84  384 177 HOH   HOH B . 
G 3 HOH   85  385 57  HOH   HOH B . 
G 3 HOH   86  386 154 HOH   HOH B . 
G 3 HOH   87  387 205 HOH   HOH B . 
G 3 HOH   88  388 76  HOH   HOH B . 
G 3 HOH   89  389 223 HOH   HOH B . 
G 3 HOH   90  390 148 HOH   HOH B . 
G 3 HOH   91  391 134 HOH   HOH B . 
G 3 HOH   92  392 195 HOH   HOH B . 
G 3 HOH   93  393 97  HOH   HOH B . 
G 3 HOH   94  394 204 HOH   HOH B . 
G 3 HOH   95  395 109 HOH   HOH B . 
G 3 HOH   96  396 206 HOH   HOH B . 
G 3 HOH   97  397 32  HOH   HOH B . 
G 3 HOH   98  398 160 HOH   HOH B . 
G 3 HOH   99  399 214 HOH   HOH B . 
G 3 HOH   100 400 61  HOH   HOH B . 
G 3 HOH   101 401 155 HOH   HOH B . 
G 3 HOH   102 402 130 HOH   HOH B . 
G 3 HOH   103 403 135 HOH   HOH B . 
G 3 HOH   104 404 133 HOH   HOH B . 
G 3 HOH   105 405 99  HOH   HOH B . 
G 3 HOH   106 406 88  HOH   HOH B . 
G 3 HOH   107 407 95  HOH   HOH B . 
G 3 HOH   108 408 83  HOH   HOH B . 
G 3 HOH   109 409 71  HOH   HOH B . 
G 3 HOH   110 410 224 HOH   HOH B . 
G 3 HOH   111 411 113 HOH   HOH B . 
G 3 HOH   112 412 215 HOH   HOH B . 
G 3 HOH   113 413 85  HOH   HOH B . 
G 3 HOH   114 414 144 HOH   HOH B . 
G 3 HOH   115 415 200 HOH   HOH B . 
G 3 HOH   116 416 199 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 92  ? CG  ? A GLU 124 CG  
2  1 Y 1 A GLU 92  ? CD  ? A GLU 124 CD  
3  1 Y 1 A GLU 92  ? OE1 ? A GLU 124 OE1 
4  1 Y 1 A GLU 92  ? OE2 ? A GLU 124 OE2 
5  1 Y 1 B GLU 92  ? CG  ? B GLU 124 CG  
6  1 Y 1 B GLU 92  ? CD  ? B GLU 124 CD  
7  1 Y 1 B GLU 92  ? OE1 ? B GLU 124 OE1 
8  1 Y 1 B GLU 92  ? OE2 ? B GLU 124 OE2 
9  1 Y 1 B ARG 104 ? CG  ? B ARG 136 CG  
10 1 Y 1 B ARG 104 ? CD  ? B ARG 136 CD  
11 1 Y 1 B ARG 104 ? NE  ? B ARG 136 NE  
12 1 Y 1 B ARG 104 ? CZ  ? B ARG 136 CZ  
13 1 Y 1 B ARG 104 ? NH1 ? B ARG 136 NH1 
14 1 Y 1 B ARG 104 ? NH2 ? B ARG 136 NH2 
# 
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 ? ? ? '(1.12_2829: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JIR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.252 
_cell.length_a_esd                 ? 
_cell.length_b                     84.398 
_cell.length_b_esd                 ? 
_cell.length_c                     63.368 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JIR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JIR 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Disodium malonate, 0.1 M NaOAc pH 4.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_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                        'PHOTON FACTORY BEAMLINE BL-17A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL-17A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JIR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.3 
_reflns.d_resolution_low                               42.2 
_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                                     57811 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.8 
_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                                0.05 
_reflns.pdbx_Rpim_I_all                                0.019 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.3 
_reflns_shell.d_res_low                                     1.32 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2820 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.068 
_reflns_shell.pdbx_Rpim_I_all                               0.393 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.74 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JIR 
_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                            1.300 
_refine.ls_d_res_low                             35.124 
_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                     57753 
_refine.ls_number_reflns_R_free                  2930 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1754 
_refine.ls_R_factor_R_free                       0.1973 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1742 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4PWE 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.96 
_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                            0.12 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1780 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_refine_hist.number_atoms_solvent             221 
_refine_hist.number_atoms_total               2034 
_refine_hist.d_res_high                       1.300 
_refine_hist.d_res_low                        35.124 
# 
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' ? 0.005  ? 1861 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.835  ? 2540 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.702 ? 639  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.087  ? 284  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 320  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.3000 1.3213 . . 137 2572 100.00 . . . . 0.2273 . . . . . . . . . . . 0.2678 
'X-RAY DIFFRACTION' 1.3213 1.3441 . . 117 2594 100.00 . . . . 0.2099 . . . . . . . . . . . 0.2618 
'X-RAY DIFFRACTION' 1.3441 1.3686 . . 121 2576 100.00 . . . . 0.2062 . . . . . . . . . . . 0.2564 
'X-RAY DIFFRACTION' 1.3686 1.3949 . . 140 2594 100.00 . . . . 0.1805 . . . . . . . . . . . 0.2217 
'X-RAY DIFFRACTION' 1.3949 1.4234 . . 146 2559 100.00 . . . . 0.1769 . . . . . . . . . . . 0.2295 
'X-RAY DIFFRACTION' 1.4234 1.4543 . . 149 2556 100.00 . . . . 0.1693 . . . . . . . . . . . 0.2058 
'X-RAY DIFFRACTION' 1.4543 1.4882 . . 139 2588 100.00 . . . . 0.1636 . . . . . . . . . . . 0.2086 
'X-RAY DIFFRACTION' 1.4882 1.5254 . . 137 2568 100.00 . . . . 0.1594 . . . . . . . . . . . 0.1814 
'X-RAY DIFFRACTION' 1.5254 1.5666 . . 139 2608 100.00 . . . . 0.1553 . . . . . . . . . . . 0.1954 
'X-RAY DIFFRACTION' 1.5666 1.6127 . . 106 2619 100.00 . . . . 0.1467 . . . . . . . . . . . 0.1984 
'X-RAY DIFFRACTION' 1.6127 1.6648 . . 166 2589 100.00 . . . . 0.1516 . . . . . . . . . . . 0.1849 
'X-RAY DIFFRACTION' 1.6648 1.7243 . . 138 2598 100.00 . . . . 0.1636 . . . . . . . . . . . 0.1892 
'X-RAY DIFFRACTION' 1.7243 1.7933 . . 149 2571 100.00 . . . . 0.1628 . . . . . . . . . . . 0.1710 
'X-RAY DIFFRACTION' 1.7933 1.8749 . . 148 2614 100.00 . . . . 0.1548 . . . . . . . . . . . 0.1812 
'X-RAY DIFFRACTION' 1.8749 1.9737 . . 147 2606 100.00 . . . . 0.1574 . . . . . . . . . . . 0.1875 
'X-RAY DIFFRACTION' 1.9737 2.0974 . . 129 2601 100.00 . . . . 0.1605 . . . . . . . . . . . 0.1921 
'X-RAY DIFFRACTION' 2.0974 2.2593 . . 132 2650 100.00 . . . . 0.1623 . . . . . . . . . . . 0.1939 
'X-RAY DIFFRACTION' 2.2593 2.4866 . . 141 2618 100.00 . . . . 0.1739 . . . . . . . . . . . 0.1946 
'X-RAY DIFFRACTION' 2.4866 2.8463 . . 138 2668 100.00 . . . . 0.1932 . . . . . . . . . . . 0.2185 
'X-RAY DIFFRACTION' 2.8463 3.5855 . . 150 2669 100.00 . . . . 0.1778 . . . . . . . . . . . 0.2118 
'X-RAY DIFFRACTION' 3.5855 35.124 . . 161 2805 100.00 . . . . 0.1838 . . . . . . . . . . . 0.1830 
# 
_struct.entry_id                     9JIR 
_struct.title                        'Crystal structure of V30M-TTR in complex with ioxynil' 
_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        9JIR 
_struct_keywords.text            'amyloidosis, tyroxine, inhibitor, stabilizer, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT 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 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TTHY_HUMAN 
_struct_ref.pdbx_db_accession          P02766 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTT
EEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_struct_ref.pdbx_align_begin           1 
# 
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 9JIR A 13 ? 159 ? P02766 1 ? 147 ? -19 127 
2 1 9JIR B 13 ? 159 ? P02766 1 ? 147 ? -19 127 
# 
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 9JIR MET A 1  ? UNP P02766 ?   ?  'initiating methionine' -31 1  
1 9JIR ARG A 2  ? UNP P02766 ?   ?  'expression tag'        -30 2  
1 9JIR GLY A 3  ? UNP P02766 ?   ?  'expression tag'        -29 3  
1 9JIR SER A 4  ? UNP P02766 ?   ?  'expression tag'        -28 4  
1 9JIR HIS A 5  ? UNP P02766 ?   ?  'expression tag'        -27 5  
1 9JIR HIS A 6  ? UNP P02766 ?   ?  'expression tag'        -26 6  
1 9JIR HIS A 7  ? UNP P02766 ?   ?  'expression tag'        -25 7  
1 9JIR HIS A 8  ? UNP P02766 ?   ?  'expression tag'        -24 8  
1 9JIR HIS A 9  ? UNP P02766 ?   ?  'expression tag'        -23 9  
1 9JIR HIS A 10 ? UNP P02766 ?   ?  'expression tag'        -22 10 
1 9JIR GLY A 11 ? UNP P02766 ?   ?  'expression tag'        -21 11 
1 9JIR SER A 12 ? UNP P02766 ?   ?  'expression tag'        -20 12 
1 9JIR MET A 62 ? UNP P02766 VAL 50 'engineered mutation'   30  13 
2 9JIR MET B 1  ? UNP P02766 ?   ?  'initiating methionine' -31 14 
2 9JIR ARG B 2  ? UNP P02766 ?   ?  'expression tag'        -30 15 
2 9JIR GLY B 3  ? UNP P02766 ?   ?  'expression tag'        -29 16 
2 9JIR SER B 4  ? UNP P02766 ?   ?  'expression tag'        -28 17 
2 9JIR HIS B 5  ? UNP P02766 ?   ?  'expression tag'        -27 18 
2 9JIR HIS B 6  ? UNP P02766 ?   ?  'expression tag'        -26 19 
2 9JIR HIS B 7  ? UNP P02766 ?   ?  'expression tag'        -25 20 
2 9JIR HIS B 8  ? UNP P02766 ?   ?  'expression tag'        -24 21 
2 9JIR HIS B 9  ? UNP P02766 ?   ?  'expression tag'        -23 22 
2 9JIR HIS B 10 ? UNP P02766 ?   ?  'expression tag'        -22 23 
2 9JIR GLY B 11 ? UNP P02766 ?   ?  'expression tag'        -21 24 
2 9JIR SER B 12 ? UNP P02766 ?   ?  'expression tag'        -20 25 
2 9JIR MET B 62 ? UNP P02766 VAL 50 'engineered mutation'   30  26 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 6570  ? 
1 MORE         -46   ? 
1 'SSA (A^2)'  18930 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_455 -x-1,-y,z -1.0000000000 0.0000000000 0.0000000000 -43.2520000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 106 ? LEU A 114 ? ASP A 74 LEU A 82 1 ? 9 
HELX_P HELX_P2 AA2 ASP B 106 ? LEU B 114 ? ASP B 74 LEU B 82 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 55  ? PRO A 56  ? SER A 23  PRO A 24  
AA1 2 LEU A 44  ? ASP A 50  ? LEU A 12  ASP A 18  
AA1 3 ARG A 136 ? SER A 144 ? ARG A 104 SER A 112 
AA1 4 SER A 147 ? THR A 155 ? SER A 115 THR A 123 
AA1 5 SER B 147 ? THR B 155 ? SER B 115 THR B 123 
AA1 6 ARG B 136 ? SER B 144 ? ARG B 104 SER B 112 
AA1 7 LEU B 44  ? ASP B 50  ? LEU B 12  ASP B 18  
AA1 8 SER B 55  ? PRO B 56  ? SER B 23  PRO B 24  
AA2 1 GLU A 86  ? LEU A 87  ? GLU A 54  LEU A 55  
AA2 2 LEU A 44  ? ASP A 50  ? LEU A 12  ASP A 18  
AA2 3 ARG A 136 ? SER A 144 ? ARG A 104 SER A 112 
AA2 4 SER A 147 ? THR A 155 ? SER A 115 THR A 123 
AA2 5 SER B 147 ? THR B 155 ? SER B 115 THR B 123 
AA2 6 ARG B 136 ? SER B 144 ? ARG B 104 SER B 112 
AA2 7 LEU B 44  ? ASP B 50  ? LEU B 12  ASP B 18  
AA2 8 GLU B 86  ? LEU B 87  ? GLU B 54  LEU B 55  
AA3 1 TRP A 73  ? LYS A 80  ? TRP A 41  LYS A 48  
AA3 2 ALA A 61  ? LYS A 67  ? ALA A 29  LYS A 35  
AA3 3 GLY A 99  ? ILE A 105 ? GLY A 67  ILE A 73  
AA3 4 HIS A 120 ? ALA A 129 ? HIS A 88  ALA A 97  
AA3 5 HIS B 120 ? ALA B 129 ? HIS B 88  ALA B 97  
AA3 6 GLY B 99  ? ILE B 105 ? GLY B 67  ILE B 73  
AA3 7 ALA B 61  ? LYS B 67  ? ALA B 29  LYS B 35  
AA3 8 TRP B 73  ? LYS B 80  ? TRP B 41  LYS B 48  
# 
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 SER A 55  ? O SER A 23  N ASP A 50  ? N ASP A 18  
AA1 2 3 N LYS A 47  ? N LYS A 15  O ILE A 139 ? O ILE A 107 
AA1 3 4 N ALA A 140 ? N ALA A 108 O THR A 151 ? O THR A 119 
AA1 4 5 N TYR A 148 ? N TYR A 116 O THR B 150 ? O THR B 118 
AA1 5 6 O THR B 151 ? O THR B 119 N ALA B 140 ? N ALA B 108 
AA1 6 7 O LEU B 143 ? O LEU B 111 N LEU B 49  ? N LEU B 17  
AA1 7 8 N ASP B 50  ? N ASP B 18  O SER B 55  ? O SER B 23  
AA2 1 2 O LEU A 87  ? O LEU A 55  N VAL A 46  ? N VAL A 14  
AA2 2 3 N LYS A 47  ? N LYS A 15  O ILE A 139 ? O ILE A 107 
AA2 3 4 N ALA A 140 ? N ALA A 108 O THR A 151 ? O THR A 119 
AA2 4 5 N TYR A 148 ? N TYR A 116 O THR B 150 ? O THR B 118 
AA2 5 6 O THR B 151 ? O THR B 119 N ALA B 140 ? N ALA B 108 
AA2 6 7 O LEU B 143 ? O LEU B 111 N LEU B 49  ? N LEU B 17  
AA2 7 8 N VAL B 46  ? N VAL B 14  O LEU B 87  ? O LEU B 55  
AA3 1 2 O ALA A 77  ? O ALA A 45  N VAL A 64  ? N VAL A 32  
AA3 2 3 N HIS A 63  ? N HIS A 31  O GLU A 104 ? O GLU A 72  
AA3 3 4 N ILE A 105 ? N ILE A 73  O ALA A 123 ? O ALA A 91  
AA3 4 5 N VAL A 126 ? N VAL A 94  O GLU B 121 ? O GLU B 89  
AA3 5 6 O ALA B 123 ? O ALA B 91  N ILE B 105 ? N ILE B 73  
AA3 6 7 O GLU B 104 ? O GLU B 72  N HIS B 63  ? N HIS B 31  
AA3 7 8 N VAL B 64  ? N VAL B 32  O ALA B 77  ? O ALA B 45  
# 
_pdbx_entry_details.entry_id                   9JIR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    PHE 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     44 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -121.23 
_pdbx_validate_torsion.psi             -50.10 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 356 ? F HOH . 
2 1 B HOH 371 ? G HOH . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 414 ? 5.83 . 
2 1 O ? B HOH 415 ? 6.29 . 
3 1 O ? B HOH 416 ? 8.23 . 
# 
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 MET -31 ? A MET 1   
2  1 Y 1 A ARG -30 ? A ARG 2   
3  1 Y 1 A GLY -29 ? A GLY 3   
4  1 Y 1 A SER -28 ? A SER 4   
5  1 Y 1 A HIS -27 ? A HIS 5   
6  1 Y 1 A HIS -26 ? A HIS 6   
7  1 Y 1 A HIS -25 ? A HIS 7   
8  1 Y 1 A HIS -24 ? A HIS 8   
9  1 Y 1 A HIS -23 ? A HIS 9   
10 1 Y 1 A HIS -22 ? A HIS 10  
11 1 Y 1 A GLY -21 ? A GLY 11  
12 1 Y 1 A SER -20 ? A SER 12  
13 1 Y 1 A MET -19 ? A MET 13  
14 1 Y 1 A ALA -18 ? A ALA 14  
15 1 Y 1 A SER -17 ? A SER 15  
16 1 Y 1 A HIS -16 ? A HIS 16  
17 1 Y 1 A ARG -15 ? A ARG 17  
18 1 Y 1 A LEU -14 ? A LEU 18  
19 1 Y 1 A LEU -13 ? A LEU 19  
20 1 Y 1 A LEU -12 ? A LEU 20  
21 1 Y 1 A LEU -11 ? A LEU 21  
22 1 Y 1 A CYS -10 ? A CYS 22  
23 1 Y 1 A LEU -9  ? A LEU 23  
24 1 Y 1 A ALA -8  ? A ALA 24  
25 1 Y 1 A GLY -7  ? A GLY 25  
26 1 Y 1 A LEU -6  ? A LEU 26  
27 1 Y 1 A VAL -5  ? A VAL 27  
28 1 Y 1 A PHE -4  ? A PHE 28  
29 1 Y 1 A VAL -3  ? A VAL 29  
30 1 Y 1 A SER -2  ? A SER 30  
31 1 Y 1 A GLU -1  ? A GLU 31  
32 1 Y 1 A ALA 0   ? A ALA 32  
33 1 Y 1 A GLY 1   ? A GLY 33  
34 1 Y 1 A PRO 2   ? A PRO 34  
35 1 Y 1 A THR 3   ? A THR 35  
36 1 Y 1 A GLY 4   ? A GLY 36  
37 1 Y 1 A THR 5   ? A THR 37  
38 1 Y 1 A GLY 6   ? A GLY 38  
39 1 Y 1 A GLU 7   ? A GLU 39  
40 1 Y 1 A SER 8   ? A SER 40  
41 1 Y 1 A LYS 9   ? A LYS 41  
42 1 Y 1 A LYS 126 ? A LYS 158 
43 1 Y 1 A GLU 127 ? A GLU 159 
44 1 Y 1 B MET -31 ? B MET 1   
45 1 Y 1 B ARG -30 ? B ARG 2   
46 1 Y 1 B GLY -29 ? B GLY 3   
47 1 Y 1 B SER -28 ? B SER 4   
48 1 Y 1 B HIS -27 ? B HIS 5   
49 1 Y 1 B HIS -26 ? B HIS 6   
50 1 Y 1 B HIS -25 ? B HIS 7   
51 1 Y 1 B HIS -24 ? B HIS 8   
52 1 Y 1 B HIS -23 ? B HIS 9   
53 1 Y 1 B HIS -22 ? B HIS 10  
54 1 Y 1 B GLY -21 ? B GLY 11  
55 1 Y 1 B SER -20 ? B SER 12  
56 1 Y 1 B MET -19 ? B MET 13  
57 1 Y 1 B ALA -18 ? B ALA 14  
58 1 Y 1 B SER -17 ? B SER 15  
59 1 Y 1 B HIS -16 ? B HIS 16  
60 1 Y 1 B ARG -15 ? B ARG 17  
61 1 Y 1 B LEU -14 ? B LEU 18  
62 1 Y 1 B LEU -13 ? B LEU 19  
63 1 Y 1 B LEU -12 ? B LEU 20  
64 1 Y 1 B LEU -11 ? B LEU 21  
65 1 Y 1 B CYS -10 ? B CYS 22  
66 1 Y 1 B LEU -9  ? B LEU 23  
67 1 Y 1 B ALA -8  ? B ALA 24  
68 1 Y 1 B GLY -7  ? B GLY 25  
69 1 Y 1 B LEU -6  ? B LEU 26  
70 1 Y 1 B VAL -5  ? B VAL 27  
71 1 Y 1 B PHE -4  ? B PHE 28  
72 1 Y 1 B VAL -3  ? B VAL 29  
73 1 Y 1 B SER -2  ? B SER 30  
74 1 Y 1 B GLU -1  ? B GLU 31  
75 1 Y 1 B ALA 0   ? B ALA 32  
76 1 Y 1 B GLY 1   ? B GLY 33  
77 1 Y 1 B PRO 2   ? B PRO 34  
78 1 Y 1 B THR 3   ? B THR 35  
79 1 Y 1 B GLY 4   ? B GLY 36  
80 1 Y 1 B THR 5   ? B THR 37  
81 1 Y 1 B GLY 6   ? B GLY 38  
82 1 Y 1 B GLU 7   ? B GLU 39  
83 1 Y 1 B SER 8   ? B SER 40  
84 1 Y 1 B LYS 9   ? B LYS 41  
85 1 Y 1 B LYS 126 ? B LYS 158 
86 1 Y 1 B GLU 127 ? B GLU 159 
# 
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 
A1L37 CAA  C Y N 1   
A1L37 CAB  C Y N 2   
A1L37 CAC  C Y N 3   
A1L37 CAD  C Y N 4   
A1L37 CAE  C Y N 5   
A1L37 CAF  C Y N 6   
A1L37 CAJ  C N N 7   
A1L37 IAH  I N N 8   
A1L37 IAI  I N N 9   
A1L37 NAK  N N N 10  
A1L37 OAG  O N N 11  
A1L37 H1   H N N 12  
A1L37 H2   H N N 13  
A1L37 H3   H N N 14  
ALA   N    N N N 15  
ALA   CA   C N S 16  
ALA   C    C N N 17  
ALA   O    O N N 18  
ALA   CB   C N N 19  
ALA   OXT  O N N 20  
ALA   H    H N N 21  
ALA   H2   H N N 22  
ALA   HA   H N N 23  
ALA   HB1  H N N 24  
ALA   HB2  H N N 25  
ALA   HB3  H N N 26  
ALA   HXT  H N N 27  
ARG   N    N N N 28  
ARG   CA   C N S 29  
ARG   C    C N N 30  
ARG   O    O N N 31  
ARG   CB   C N N 32  
ARG   CG   C N N 33  
ARG   CD   C N N 34  
ARG   NE   N N N 35  
ARG   CZ   C N N 36  
ARG   NH1  N N N 37  
ARG   NH2  N N N 38  
ARG   OXT  O N N 39  
ARG   H    H N N 40  
ARG   H2   H N N 41  
ARG   HA   H N N 42  
ARG   HB2  H N N 43  
ARG   HB3  H N N 44  
ARG   HG2  H N N 45  
ARG   HG3  H N N 46  
ARG   HD2  H N N 47  
ARG   HD3  H N N 48  
ARG   HE   H N N 49  
ARG   HH11 H N N 50  
ARG   HH12 H N N 51  
ARG   HH21 H N N 52  
ARG   HH22 H N N 53  
ARG   HXT  H N N 54  
ASN   N    N N N 55  
ASN   CA   C N S 56  
ASN   C    C N N 57  
ASN   O    O N N 58  
ASN   CB   C N N 59  
ASN   CG   C N N 60  
ASN   OD1  O N N 61  
ASN   ND2  N N N 62  
ASN   OXT  O N N 63  
ASN   H    H N N 64  
ASN   H2   H N N 65  
ASN   HA   H N N 66  
ASN   HB2  H N N 67  
ASN   HB3  H N N 68  
ASN   HD21 H N N 69  
ASN   HD22 H N N 70  
ASN   HXT  H N N 71  
ASP   N    N N N 72  
ASP   CA   C N S 73  
ASP   C    C N N 74  
ASP   O    O N N 75  
ASP   CB   C N N 76  
ASP   CG   C N N 77  
ASP   OD1  O N N 78  
ASP   OD2  O N N 79  
ASP   OXT  O N N 80  
ASP   H    H N N 81  
ASP   H2   H N N 82  
ASP   HA   H N N 83  
ASP   HB2  H N N 84  
ASP   HB3  H N N 85  
ASP   HD2  H N N 86  
ASP   HXT  H N N 87  
CYS   N    N N N 88  
CYS   CA   C N R 89  
CYS   C    C N N 90  
CYS   O    O N N 91  
CYS   CB   C N N 92  
CYS   SG   S N N 93  
CYS   OXT  O N N 94  
CYS   H    H N N 95  
CYS   H2   H N N 96  
CYS   HA   H N N 97  
CYS   HB2  H N N 98  
CYS   HB3  H N N 99  
CYS   HG   H N N 100 
CYS   HXT  H N N 101 
GLU   N    N N N 102 
GLU   CA   C N S 103 
GLU   C    C N N 104 
GLU   O    O N N 105 
GLU   CB   C N N 106 
GLU   CG   C N N 107 
GLU   CD   C N N 108 
GLU   OE1  O N N 109 
GLU   OE2  O N N 110 
GLU   OXT  O N N 111 
GLU   H    H N N 112 
GLU   H2   H N N 113 
GLU   HA   H N N 114 
GLU   HB2  H N N 115 
GLU   HB3  H N N 116 
GLU   HG2  H N N 117 
GLU   HG3  H N N 118 
GLU   HE2  H N N 119 
GLU   HXT  H N N 120 
GLY   N    N N N 121 
GLY   CA   C N N 122 
GLY   C    C N N 123 
GLY   O    O N N 124 
GLY   OXT  O N N 125 
GLY   H    H N N 126 
GLY   H2   H N N 127 
GLY   HA2  H N N 128 
GLY   HA3  H N N 129 
GLY   HXT  H N N 130 
HIS   N    N N N 131 
HIS   CA   C N S 132 
HIS   C    C N N 133 
HIS   O    O N N 134 
HIS   CB   C N N 135 
HIS   CG   C Y N 136 
HIS   ND1  N Y N 137 
HIS   CD2  C Y N 138 
HIS   CE1  C Y N 139 
HIS   NE2  N Y N 140 
HIS   OXT  O N N 141 
HIS   H    H N N 142 
HIS   H2   H N N 143 
HIS   HA   H N N 144 
HIS   HB2  H N N 145 
HIS   HB3  H N N 146 
HIS   HD1  H N N 147 
HIS   HD2  H N N 148 
HIS   HE1  H N N 149 
HIS   HE2  H N N 150 
HIS   HXT  H N N 151 
HOH   O    O N N 152 
HOH   H1   H N N 153 
HOH   H2   H N N 154 
ILE   N    N N N 155 
ILE   CA   C N S 156 
ILE   C    C N N 157 
ILE   O    O N N 158 
ILE   CB   C N S 159 
ILE   CG1  C N N 160 
ILE   CG2  C N N 161 
ILE   CD1  C N N 162 
ILE   OXT  O N N 163 
ILE   H    H N N 164 
ILE   H2   H N N 165 
ILE   HA   H N N 166 
ILE   HB   H N N 167 
ILE   HG12 H N N 168 
ILE   HG13 H N N 169 
ILE   HG21 H N N 170 
ILE   HG22 H N N 171 
ILE   HG23 H N N 172 
ILE   HD11 H N N 173 
ILE   HD12 H N N 174 
ILE   HD13 H N N 175 
ILE   HXT  H N N 176 
LEU   N    N N N 177 
LEU   CA   C N S 178 
LEU   C    C N N 179 
LEU   O    O N N 180 
LEU   CB   C N N 181 
LEU   CG   C N N 182 
LEU   CD1  C N N 183 
LEU   CD2  C N N 184 
LEU   OXT  O N N 185 
LEU   H    H N N 186 
LEU   H2   H N N 187 
LEU   HA   H N N 188 
LEU   HB2  H N N 189 
LEU   HB3  H N N 190 
LEU   HG   H N N 191 
LEU   HD11 H N N 192 
LEU   HD12 H N N 193 
LEU   HD13 H N N 194 
LEU   HD21 H N N 195 
LEU   HD22 H N N 196 
LEU   HD23 H N N 197 
LEU   HXT  H N N 198 
LYS   N    N N N 199 
LYS   CA   C N S 200 
LYS   C    C N N 201 
LYS   O    O N N 202 
LYS   CB   C N N 203 
LYS   CG   C N N 204 
LYS   CD   C N N 205 
LYS   CE   C N N 206 
LYS   NZ   N N N 207 
LYS   OXT  O N N 208 
LYS   H    H N N 209 
LYS   H2   H N N 210 
LYS   HA   H N N 211 
LYS   HB2  H N N 212 
LYS   HB3  H N N 213 
LYS   HG2  H N N 214 
LYS   HG3  H N N 215 
LYS   HD2  H N N 216 
LYS   HD3  H N N 217 
LYS   HE2  H N N 218 
LYS   HE3  H N N 219 
LYS   HZ1  H N N 220 
LYS   HZ2  H N N 221 
LYS   HZ3  H N N 222 
LYS   HXT  H N N 223 
MET   N    N N N 224 
MET   CA   C N S 225 
MET   C    C N N 226 
MET   O    O N N 227 
MET   CB   C N N 228 
MET   CG   C N N 229 
MET   SD   S N N 230 
MET   CE   C N N 231 
MET   OXT  O N N 232 
MET   H    H N N 233 
MET   H2   H N N 234 
MET   HA   H N N 235 
MET   HB2  H N N 236 
MET   HB3  H N N 237 
MET   HG2  H N N 238 
MET   HG3  H N N 239 
MET   HE1  H N N 240 
MET   HE2  H N N 241 
MET   HE3  H N N 242 
MET   HXT  H N N 243 
PHE   N    N N N 244 
PHE   CA   C N S 245 
PHE   C    C N N 246 
PHE   O    O N N 247 
PHE   CB   C N N 248 
PHE   CG   C Y N 249 
PHE   CD1  C Y N 250 
PHE   CD2  C Y N 251 
PHE   CE1  C Y N 252 
PHE   CE2  C Y N 253 
PHE   CZ   C Y N 254 
PHE   OXT  O N N 255 
PHE   H    H N N 256 
PHE   H2   H N N 257 
PHE   HA   H N N 258 
PHE   HB2  H N N 259 
PHE   HB3  H N N 260 
PHE   HD1  H N N 261 
PHE   HD2  H N N 262 
PHE   HE1  H N N 263 
PHE   HE2  H N N 264 
PHE   HZ   H N N 265 
PHE   HXT  H N N 266 
PRO   N    N N N 267 
PRO   CA   C N S 268 
PRO   C    C N N 269 
PRO   O    O N N 270 
PRO   CB   C N N 271 
PRO   CG   C N N 272 
PRO   CD   C N N 273 
PRO   OXT  O N N 274 
PRO   H    H N N 275 
PRO   HA   H N N 276 
PRO   HB2  H N N 277 
PRO   HB3  H N N 278 
PRO   HG2  H N N 279 
PRO   HG3  H N N 280 
PRO   HD2  H N N 281 
PRO   HD3  H N N 282 
PRO   HXT  H N N 283 
SER   N    N N N 284 
SER   CA   C N S 285 
SER   C    C N N 286 
SER   O    O N N 287 
SER   CB   C N N 288 
SER   OG   O N N 289 
SER   OXT  O N N 290 
SER   H    H N N 291 
SER   H2   H N N 292 
SER   HA   H N N 293 
SER   HB2  H N N 294 
SER   HB3  H N N 295 
SER   HG   H N N 296 
SER   HXT  H N N 297 
THR   N    N N N 298 
THR   CA   C N S 299 
THR   C    C N N 300 
THR   O    O N N 301 
THR   CB   C N R 302 
THR   OG1  O N N 303 
THR   CG2  C N N 304 
THR   OXT  O N N 305 
THR   H    H N N 306 
THR   H2   H N N 307 
THR   HA   H N N 308 
THR   HB   H N N 309 
THR   HG1  H N N 310 
THR   HG21 H N N 311 
THR   HG22 H N N 312 
THR   HG23 H N N 313 
THR   HXT  H N N 314 
TRP   N    N N N 315 
TRP   CA   C N S 316 
TRP   C    C N N 317 
TRP   O    O N N 318 
TRP   CB   C N N 319 
TRP   CG   C Y N 320 
TRP   CD1  C Y N 321 
TRP   CD2  C Y N 322 
TRP   NE1  N Y N 323 
TRP   CE2  C Y N 324 
TRP   CE3  C Y N 325 
TRP   CZ2  C Y N 326 
TRP   CZ3  C Y N 327 
TRP   CH2  C Y N 328 
TRP   OXT  O N N 329 
TRP   H    H N N 330 
TRP   H2   H N N 331 
TRP   HA   H N N 332 
TRP   HB2  H N N 333 
TRP   HB3  H N N 334 
TRP   HD1  H N N 335 
TRP   HE1  H N N 336 
TRP   HE3  H N N 337 
TRP   HZ2  H N N 338 
TRP   HZ3  H N N 339 
TRP   HH2  H N N 340 
TRP   HXT  H N N 341 
TYR   N    N N N 342 
TYR   CA   C N S 343 
TYR   C    C N N 344 
TYR   O    O N N 345 
TYR   CB   C N N 346 
TYR   CG   C Y N 347 
TYR   CD1  C Y N 348 
TYR   CD2  C Y N 349 
TYR   CE1  C Y N 350 
TYR   CE2  C Y N 351 
TYR   CZ   C Y N 352 
TYR   OH   O N N 353 
TYR   OXT  O N N 354 
TYR   H    H N N 355 
TYR   H2   H N N 356 
TYR   HA   H N N 357 
TYR   HB2  H N N 358 
TYR   HB3  H N N 359 
TYR   HD1  H N N 360 
TYR   HD2  H N N 361 
TYR   HE1  H N N 362 
TYR   HE2  H N N 363 
TYR   HH   H N N 364 
TYR   HXT  H N N 365 
VAL   N    N N N 366 
VAL   CA   C N S 367 
VAL   C    C N N 368 
VAL   O    O N N 369 
VAL   CB   C N N 370 
VAL   CG1  C N N 371 
VAL   CG2  C N N 372 
VAL   OXT  O N N 373 
VAL   H    H N N 374 
VAL   H2   H N N 375 
VAL   HA   H N N 376 
VAL   HB   H N N 377 
VAL   HG11 H N N 378 
VAL   HG12 H N N 379 
VAL   HG13 H N N 380 
VAL   HG21 H N N 381 
VAL   HG22 H N N 382 
VAL   HG23 H N N 383 
VAL   HXT  H N N 384 
# 
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 
A1L37 NAK CAJ  trip N N 1   
A1L37 CAJ CAD  sing N N 2   
A1L37 CAD CAF  doub Y N 3   
A1L37 CAD CAB  sing Y N 4   
A1L37 CAF CAE  sing Y N 5   
A1L37 CAB CAA  doub Y N 6   
A1L37 CAE CAC  doub Y N 7   
A1L37 CAE IAH  sing N N 8   
A1L37 CAA CAC  sing Y N 9   
A1L37 CAA IAI  sing N N 10  
A1L37 CAC OAG  sing N N 11  
A1L37 CAB H1   sing N N 12  
A1L37 CAF H2   sing N N 13  
A1L37 OAG H3   sing N N 14  
ALA   N   CA   sing N N 15  
ALA   N   H    sing N N 16  
ALA   N   H2   sing N N 17  
ALA   CA  C    sing N N 18  
ALA   CA  CB   sing N N 19  
ALA   CA  HA   sing N N 20  
ALA   C   O    doub N N 21  
ALA   C   OXT  sing N N 22  
ALA   CB  HB1  sing N N 23  
ALA   CB  HB2  sing N N 24  
ALA   CB  HB3  sing N N 25  
ALA   OXT HXT  sing N N 26  
ARG   N   CA   sing N N 27  
ARG   N   H    sing N N 28  
ARG   N   H2   sing N N 29  
ARG   CA  C    sing N N 30  
ARG   CA  CB   sing N N 31  
ARG   CA  HA   sing N N 32  
ARG   C   O    doub N N 33  
ARG   C   OXT  sing N N 34  
ARG   CB  CG   sing N N 35  
ARG   CB  HB2  sing N N 36  
ARG   CB  HB3  sing N N 37  
ARG   CG  CD   sing N N 38  
ARG   CG  HG2  sing N N 39  
ARG   CG  HG3  sing N N 40  
ARG   CD  NE   sing N N 41  
ARG   CD  HD2  sing N N 42  
ARG   CD  HD3  sing N N 43  
ARG   NE  CZ   sing N N 44  
ARG   NE  HE   sing N N 45  
ARG   CZ  NH1  sing N N 46  
ARG   CZ  NH2  doub N N 47  
ARG   NH1 HH11 sing N N 48  
ARG   NH1 HH12 sing N N 49  
ARG   NH2 HH21 sing N N 50  
ARG   NH2 HH22 sing N N 51  
ARG   OXT HXT  sing N N 52  
ASN   N   CA   sing N N 53  
ASN   N   H    sing N N 54  
ASN   N   H2   sing N N 55  
ASN   CA  C    sing N N 56  
ASN   CA  CB   sing N N 57  
ASN   CA  HA   sing N N 58  
ASN   C   O    doub N N 59  
ASN   C   OXT  sing N N 60  
ASN   CB  CG   sing N N 61  
ASN   CB  HB2  sing N N 62  
ASN   CB  HB3  sing N N 63  
ASN   CG  OD1  doub N N 64  
ASN   CG  ND2  sing N N 65  
ASN   ND2 HD21 sing N N 66  
ASN   ND2 HD22 sing N N 67  
ASN   OXT HXT  sing N N 68  
ASP   N   CA   sing N N 69  
ASP   N   H    sing N N 70  
ASP   N   H2   sing N N 71  
ASP   CA  C    sing N N 72  
ASP   CA  CB   sing N N 73  
ASP   CA  HA   sing N N 74  
ASP   C   O    doub N N 75  
ASP   C   OXT  sing N N 76  
ASP   CB  CG   sing N N 77  
ASP   CB  HB2  sing N N 78  
ASP   CB  HB3  sing N N 79  
ASP   CG  OD1  doub N N 80  
ASP   CG  OD2  sing N N 81  
ASP   OD2 HD2  sing N N 82  
ASP   OXT HXT  sing N N 83  
CYS   N   CA   sing N N 84  
CYS   N   H    sing N N 85  
CYS   N   H2   sing N N 86  
CYS   CA  C    sing N N 87  
CYS   CA  CB   sing N N 88  
CYS   CA  HA   sing N N 89  
CYS   C   O    doub N N 90  
CYS   C   OXT  sing N N 91  
CYS   CB  SG   sing N N 92  
CYS   CB  HB2  sing N N 93  
CYS   CB  HB3  sing N N 94  
CYS   SG  HG   sing N N 95  
CYS   OXT HXT  sing N N 96  
GLU   N   CA   sing N N 97  
GLU   N   H    sing N N 98  
GLU   N   H2   sing N N 99  
GLU   CA  C    sing N N 100 
GLU   CA  CB   sing N N 101 
GLU   CA  HA   sing N N 102 
GLU   C   O    doub N N 103 
GLU   C   OXT  sing N N 104 
GLU   CB  CG   sing N N 105 
GLU   CB  HB2  sing N N 106 
GLU   CB  HB3  sing N N 107 
GLU   CG  CD   sing N N 108 
GLU   CG  HG2  sing N N 109 
GLU   CG  HG3  sing N N 110 
GLU   CD  OE1  doub N N 111 
GLU   CD  OE2  sing N N 112 
GLU   OE2 HE2  sing N N 113 
GLU   OXT HXT  sing N N 114 
GLY   N   CA   sing N N 115 
GLY   N   H    sing N N 116 
GLY   N   H2   sing N N 117 
GLY   CA  C    sing N N 118 
GLY   CA  HA2  sing N N 119 
GLY   CA  HA3  sing N N 120 
GLY   C   O    doub N N 121 
GLY   C   OXT  sing N N 122 
GLY   OXT HXT  sing N N 123 
HIS   N   CA   sing N N 124 
HIS   N   H    sing N N 125 
HIS   N   H2   sing N N 126 
HIS   CA  C    sing N N 127 
HIS   CA  CB   sing N N 128 
HIS   CA  HA   sing N N 129 
HIS   C   O    doub N N 130 
HIS   C   OXT  sing N N 131 
HIS   CB  CG   sing N N 132 
HIS   CB  HB2  sing N N 133 
HIS   CB  HB3  sing N N 134 
HIS   CG  ND1  sing Y N 135 
HIS   CG  CD2  doub Y N 136 
HIS   ND1 CE1  doub Y N 137 
HIS   ND1 HD1  sing N N 138 
HIS   CD2 NE2  sing Y N 139 
HIS   CD2 HD2  sing N N 140 
HIS   CE1 NE2  sing Y N 141 
HIS   CE1 HE1  sing N N 142 
HIS   NE2 HE2  sing N N 143 
HIS   OXT HXT  sing N N 144 
HOH   O   H1   sing N N 145 
HOH   O   H2   sing N N 146 
ILE   N   CA   sing N N 147 
ILE   N   H    sing N N 148 
ILE   N   H2   sing N N 149 
ILE   CA  C    sing N N 150 
ILE   CA  CB   sing N N 151 
ILE   CA  HA   sing N N 152 
ILE   C   O    doub N N 153 
ILE   C   OXT  sing N N 154 
ILE   CB  CG1  sing N N 155 
ILE   CB  CG2  sing N N 156 
ILE   CB  HB   sing N N 157 
ILE   CG1 CD1  sing N N 158 
ILE   CG1 HG12 sing N N 159 
ILE   CG1 HG13 sing N N 160 
ILE   CG2 HG21 sing N N 161 
ILE   CG2 HG22 sing N N 162 
ILE   CG2 HG23 sing N N 163 
ILE   CD1 HD11 sing N N 164 
ILE   CD1 HD12 sing N N 165 
ILE   CD1 HD13 sing N N 166 
ILE   OXT HXT  sing N N 167 
LEU   N   CA   sing N N 168 
LEU   N   H    sing N N 169 
LEU   N   H2   sing N N 170 
LEU   CA  C    sing N N 171 
LEU   CA  CB   sing N N 172 
LEU   CA  HA   sing N N 173 
LEU   C   O    doub N N 174 
LEU   C   OXT  sing N N 175 
LEU   CB  CG   sing N N 176 
LEU   CB  HB2  sing N N 177 
LEU   CB  HB3  sing N N 178 
LEU   CG  CD1  sing N N 179 
LEU   CG  CD2  sing N N 180 
LEU   CG  HG   sing N N 181 
LEU   CD1 HD11 sing N N 182 
LEU   CD1 HD12 sing N N 183 
LEU   CD1 HD13 sing N N 184 
LEU   CD2 HD21 sing N N 185 
LEU   CD2 HD22 sing N N 186 
LEU   CD2 HD23 sing N N 187 
LEU   OXT HXT  sing N N 188 
LYS   N   CA   sing N N 189 
LYS   N   H    sing N N 190 
LYS   N   H2   sing N N 191 
LYS   CA  C    sing N N 192 
LYS   CA  CB   sing N N 193 
LYS   CA  HA   sing N N 194 
LYS   C   O    doub N N 195 
LYS   C   OXT  sing N N 196 
LYS   CB  CG   sing N N 197 
LYS   CB  HB2  sing N N 198 
LYS   CB  HB3  sing N N 199 
LYS   CG  CD   sing N N 200 
LYS   CG  HG2  sing N N 201 
LYS   CG  HG3  sing N N 202 
LYS   CD  CE   sing N N 203 
LYS   CD  HD2  sing N N 204 
LYS   CD  HD3  sing N N 205 
LYS   CE  NZ   sing N N 206 
LYS   CE  HE2  sing N N 207 
LYS   CE  HE3  sing N N 208 
LYS   NZ  HZ1  sing N N 209 
LYS   NZ  HZ2  sing N N 210 
LYS   NZ  HZ3  sing N N 211 
LYS   OXT HXT  sing N N 212 
MET   N   CA   sing N N 213 
MET   N   H    sing N N 214 
MET   N   H2   sing N N 215 
MET   CA  C    sing N N 216 
MET   CA  CB   sing N N 217 
MET   CA  HA   sing N N 218 
MET   C   O    doub N N 219 
MET   C   OXT  sing N N 220 
MET   CB  CG   sing N N 221 
MET   CB  HB2  sing N N 222 
MET   CB  HB3  sing N N 223 
MET   CG  SD   sing N N 224 
MET   CG  HG2  sing N N 225 
MET   CG  HG3  sing N N 226 
MET   SD  CE   sing N N 227 
MET   CE  HE1  sing N N 228 
MET   CE  HE2  sing N N 229 
MET   CE  HE3  sing N N 230 
MET   OXT HXT  sing N N 231 
PHE   N   CA   sing N N 232 
PHE   N   H    sing N N 233 
PHE   N   H2   sing N N 234 
PHE   CA  C    sing N N 235 
PHE   CA  CB   sing N N 236 
PHE   CA  HA   sing N N 237 
PHE   C   O    doub N N 238 
PHE   C   OXT  sing N N 239 
PHE   CB  CG   sing N N 240 
PHE   CB  HB2  sing N N 241 
PHE   CB  HB3  sing N N 242 
PHE   CG  CD1  doub Y N 243 
PHE   CG  CD2  sing Y N 244 
PHE   CD1 CE1  sing Y N 245 
PHE   CD1 HD1  sing N N 246 
PHE   CD2 CE2  doub Y N 247 
PHE   CD2 HD2  sing N N 248 
PHE   CE1 CZ   doub Y N 249 
PHE   CE1 HE1  sing N N 250 
PHE   CE2 CZ   sing Y N 251 
PHE   CE2 HE2  sing N N 252 
PHE   CZ  HZ   sing N N 253 
PHE   OXT HXT  sing N N 254 
PRO   N   CA   sing N N 255 
PRO   N   CD   sing N N 256 
PRO   N   H    sing N N 257 
PRO   CA  C    sing N N 258 
PRO   CA  CB   sing N N 259 
PRO   CA  HA   sing N N 260 
PRO   C   O    doub N N 261 
PRO   C   OXT  sing N N 262 
PRO   CB  CG   sing N N 263 
PRO   CB  HB2  sing N N 264 
PRO   CB  HB3  sing N N 265 
PRO   CG  CD   sing N N 266 
PRO   CG  HG2  sing N N 267 
PRO   CG  HG3  sing N N 268 
PRO   CD  HD2  sing N N 269 
PRO   CD  HD3  sing N N 270 
PRO   OXT HXT  sing N N 271 
SER   N   CA   sing N N 272 
SER   N   H    sing N N 273 
SER   N   H2   sing N N 274 
SER   CA  C    sing N N 275 
SER   CA  CB   sing N N 276 
SER   CA  HA   sing N N 277 
SER   C   O    doub N N 278 
SER   C   OXT  sing N N 279 
SER   CB  OG   sing N N 280 
SER   CB  HB2  sing N N 281 
SER   CB  HB3  sing N N 282 
SER   OG  HG   sing N N 283 
SER   OXT HXT  sing N N 284 
THR   N   CA   sing N N 285 
THR   N   H    sing N N 286 
THR   N   H2   sing N N 287 
THR   CA  C    sing N N 288 
THR   CA  CB   sing N N 289 
THR   CA  HA   sing N N 290 
THR   C   O    doub N N 291 
THR   C   OXT  sing N N 292 
THR   CB  OG1  sing N N 293 
THR   CB  CG2  sing N N 294 
THR   CB  HB   sing N N 295 
THR   OG1 HG1  sing N N 296 
THR   CG2 HG21 sing N N 297 
THR   CG2 HG22 sing N N 298 
THR   CG2 HG23 sing N N 299 
THR   OXT HXT  sing N N 300 
TRP   N   CA   sing N N 301 
TRP   N   H    sing N N 302 
TRP   N   H2   sing N N 303 
TRP   CA  C    sing N N 304 
TRP   CA  CB   sing N N 305 
TRP   CA  HA   sing N N 306 
TRP   C   O    doub N N 307 
TRP   C   OXT  sing N N 308 
TRP   CB  CG   sing N N 309 
TRP   CB  HB2  sing N N 310 
TRP   CB  HB3  sing N N 311 
TRP   CG  CD1  doub Y N 312 
TRP   CG  CD2  sing Y N 313 
TRP   CD1 NE1  sing Y N 314 
TRP   CD1 HD1  sing N N 315 
TRP   CD2 CE2  doub Y N 316 
TRP   CD2 CE3  sing Y N 317 
TRP   NE1 CE2  sing Y N 318 
TRP   NE1 HE1  sing N N 319 
TRP   CE2 CZ2  sing Y N 320 
TRP   CE3 CZ3  doub Y N 321 
TRP   CE3 HE3  sing N N 322 
TRP   CZ2 CH2  doub Y N 323 
TRP   CZ2 HZ2  sing N N 324 
TRP   CZ3 CH2  sing Y N 325 
TRP   CZ3 HZ3  sing N N 326 
TRP   CH2 HH2  sing N N 327 
TRP   OXT HXT  sing N N 328 
TYR   N   CA   sing N N 329 
TYR   N   H    sing N N 330 
TYR   N   H2   sing N N 331 
TYR   CA  C    sing N N 332 
TYR   CA  CB   sing N N 333 
TYR   CA  HA   sing N N 334 
TYR   C   O    doub N N 335 
TYR   C   OXT  sing N N 336 
TYR   CB  CG   sing N N 337 
TYR   CB  HB2  sing N N 338 
TYR   CB  HB3  sing N N 339 
TYR   CG  CD1  doub Y N 340 
TYR   CG  CD2  sing Y N 341 
TYR   CD1 CE1  sing Y N 342 
TYR   CD1 HD1  sing N N 343 
TYR   CD2 CE2  doub Y N 344 
TYR   CD2 HD2  sing N N 345 
TYR   CE1 CZ   doub Y N 346 
TYR   CE1 HE1  sing N N 347 
TYR   CE2 CZ   sing Y N 348 
TYR   CE2 HE2  sing N N 349 
TYR   CZ  OH   sing N N 350 
TYR   OH  HH   sing N N 351 
TYR   OXT HXT  sing N N 352 
VAL   N   CA   sing N N 353 
VAL   N   H    sing N N 354 
VAL   N   H2   sing N N 355 
VAL   CA  C    sing N N 356 
VAL   CA  CB   sing N N 357 
VAL   CA  HA   sing N N 358 
VAL   C   O    doub N N 359 
VAL   C   OXT  sing N N 360 
VAL   CB  CG1  sing N N 361 
VAL   CB  CG2  sing N N 362 
VAL   CB  HB   sing N N 363 
VAL   CG1 HG11 sing N N 364 
VAL   CG1 HG12 sing N N 365 
VAL   CG1 HG13 sing N N 366 
VAL   CG2 HG21 sing N N 367 
VAL   CG2 HG22 sing N N 368 
VAL   CG2 HG23 sing N N 369 
VAL   OXT HXT  sing N N 370 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4pwe 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JIR 
_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]   0.023120 
_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]   0.011849 
_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]   0.015781 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
I 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . CYS   A 1 42  ? -28.012 12.139 7.808   1.00 39.44 ? 10  CYS   A N   1 
ATOM   2    C CA  . CYS   A 1 42  ? -27.256 12.030 6.565   1.00 38.47 ? 10  CYS   A CA  1 
ATOM   3    C C   . CYS   A 1 42  ? -28.140 11.551 5.415   1.00 32.36 ? 10  CYS   A C   1 
ATOM   4    O O   . CYS   A 1 42  ? -28.148 10.369 5.081   1.00 32.75 ? 10  CYS   A O   1 
ATOM   5    C CB  . CYS   A 1 42  ? -26.069 11.081 6.748   1.00 43.23 ? 10  CYS   A CB  1 
ATOM   6    S SG  . CYS   A 1 42  ? -24.987 10.923 5.306   1.00 46.36 ? 10  CYS   A SG  1 
ATOM   7    N N   . PRO   A 1 43  ? -28.891 12.472 4.807   1.00 26.82 ? 11  PRO   A N   1 
ATOM   8    C CA  . PRO   A 1 43  ? -29.777 12.098 3.698   1.00 22.83 ? 11  PRO   A CA  1 
ATOM   9    C C   . PRO   A 1 43  ? -29.098 12.045 2.340   1.00 18.17 ? 11  PRO   A C   1 
ATOM   10   O O   . PRO   A 1 43  ? -29.758 11.706 1.353   1.00 18.16 ? 11  PRO   A O   1 
ATOM   11   C CB  . PRO   A 1 43  ? -30.831 13.210 3.729   1.00 25.78 ? 11  PRO   A CB  1 
ATOM   12   C CG  . PRO   A 1 43  ? -30.071 14.389 4.202   1.00 26.78 ? 11  PRO   A CG  1 
ATOM   13   C CD  . PRO   A 1 43  ? -29.109 13.866 5.233   1.00 27.36 ? 11  PRO   A CD  1 
ATOM   14   N N   . LEU   A 1 44  ? -27.816 12.387 2.245   1.00 16.18 ? 12  LEU   A N   1 
ATOM   15   C CA  . LEU   A 1 44  ? -27.103 12.332 0.976   1.00 15.79 ? 12  LEU   A CA  1 
ATOM   16   C C   . LEU   A 1 44  ? -25.709 11.793 1.247   1.00 17.09 ? 12  LEU   A C   1 
ATOM   17   O O   . LEU   A 1 44  ? -24.959 12.385 2.027   1.00 19.63 ? 12  LEU   A O   1 
ATOM   18   C CB  . LEU   A 1 44  ? -27.034 13.726 0.340   1.00 17.10 ? 12  LEU   A CB  1 
ATOM   19   C CG  . LEU   A 1 44  ? -26.306 13.856 -0.998  1.00 17.92 ? 12  LEU   A CG  1 
ATOM   20   C CD1 . LEU   A 1 44  ? -26.932 12.989 -2.072  1.00 18.07 ? 12  LEU   A CD1 1 
ATOM   21   C CD2 . LEU   A 1 44  ? -26.285 15.315 -1.433  1.00 19.14 ? 12  LEU   A CD2 1 
ATOM   22   N N   . MET   A 1 45  ? -25.373 10.664 0.625   1.00 14.62 ? 13  MET   A N   1 
ATOM   23   C CA  . MET   A 1 45  ? -24.048 10.065 0.719   1.00 13.54 ? 13  MET   A CA  1 
ATOM   24   C C   . MET   A 1 45  ? -23.574 9.734  -0.687  1.00 12.05 ? 13  MET   A C   1 
ATOM   25   O O   . MET   A 1 45  ? -24.370 9.343  -1.544  1.00 13.10 ? 13  MET   A O   1 
ATOM   26   C CB  . MET   A 1 45  ? -24.060 8.794  1.592   1.00 15.67 ? 13  MET   A CB  1 
ATOM   27   C CG  . MET   A 1 45  ? -22.666 8.242  1.917   1.00 18.34 ? 13  MET   A CG  1 
ATOM   28   S SD  . MET   A 1 45  ? -22.062 7.042  0.709   1.00 20.26 ? 13  MET   A SD  1 
ATOM   29   C CE  . MET   A 1 45  ? -22.782 5.527  1.328   1.00 21.44 ? 13  MET   A CE  1 
ATOM   30   N N   . VAL   A 1 46  ? -22.291 9.939  -0.944  1.00 12.05 ? 14  VAL   A N   1 
ATOM   31   C CA  . VAL   A 1 46  ? -21.701 9.629  -2.241  1.00 10.97 ? 14  VAL   A CA  1 
ATOM   32   C C   . VAL   A 1 46  ? -20.545 8.670  -2.023  1.00 11.50 ? 14  VAL   A C   1 
ATOM   33   O O   . VAL   A 1 46  ? -19.702 8.891  -1.146  1.00 13.89 ? 14  VAL   A O   1 
ATOM   34   C CB  . VAL   A 1 46  ? -21.211 10.893 -2.965  1.00 12.80 ? 14  VAL   A CB  1 
ATOM   35   C CG1 . VAL   A 1 46  ? -20.657 10.519 -4.330  1.00 14.12 ? 14  VAL   A CG1 1 
ATOM   36   C CG2 . VAL   A 1 46  ? -22.333 11.912 -3.091  1.00 14.11 ? 14  VAL   A CG2 1 
ATOM   37   N N   . LYS   A 1 47  ? -20.503 7.605  -2.814  1.00 11.71 ? 15  LYS   A N   1 
ATOM   38   C CA  . LYS   A 1 47  ? -19.456 6.597  -2.719  1.00 12.34 ? 15  LYS   A CA  1 
ATOM   39   C C   . LYS   A 1 47  ? -18.813 6.454  -4.088  1.00 11.58 ? 15  LYS   A C   1 
ATOM   40   O O   . LYS   A 1 47  ? -19.517 6.371  -5.099  1.00 12.44 ? 15  LYS   A O   1 
ATOM   41   C CB  . LYS   A 1 47  ? -20.041 5.257  -2.276  1.00 15.51 ? 15  LYS   A CB  1 
ATOM   42   C CG  . LYS   A 1 47  ? -19.007 4.172  -2.069  1.00 19.16 ? 15  LYS   A CG  1 
ATOM   43   C CD  . LYS   A 1 47  ? -19.632 2.929  -1.446  1.00 22.90 ? 15  LYS   A CD  1 
ATOM   44   C CE  . LYS   A 1 47  ? -18.571 1.932  -1.027  1.00 26.24 ? 15  LYS   A CE  1 
ATOM   45   N NZ  . LYS   A 1 47  ? -19.193 0.825  -0.255  1.00 28.91 ? 15  LYS   A NZ  1 
ATOM   46   N N   . VAL   A 1 48  ? -17.484 6.433  -4.127  1.00 10.82 ? 16  VAL   A N   1 
ATOM   47   C CA  . VAL   A 1 48  ? -16.743 6.409  -5.381  1.00 10.82 ? 16  VAL   A CA  1 
ATOM   48   C C   . VAL   A 1 48  ? -15.768 5.239  -5.354  1.00 11.38 ? 16  VAL   A C   1 
ATOM   49   O O   . VAL   A 1 48  ? -15.018 5.075  -4.385  1.00 12.51 ? 16  VAL   A O   1 
ATOM   50   C CB  . VAL   A 1 48  ? -16.002 7.746  -5.608  1.00 11.58 ? 16  VAL   A CB  1 
ATOM   51   C CG1 . VAL   A 1 48  ? -15.416 7.800  -7.004  1.00 13.16 ? 16  VAL   A CG1 1 
ATOM   52   C CG2 . VAL   A 1 48  ? -16.938 8.938  -5.366  1.00 13.12 ? 16  VAL   A CG2 1 
ATOM   53   N N   . LEU   A 1 49  ? -15.787 4.425  -6.411  1.00 11.91 ? 17  LEU   A N   1 
ATOM   54   C CA  . LEU   A 1 49  ? -14.932 3.250  -6.541  1.00 11.48 ? 17  LEU   A CA  1 
ATOM   55   C C   . LEU   A 1 49  ? -14.043 3.378  -7.770  1.00 10.79 ? 17  LEU   A C   1 
ATOM   56   O O   . LEU   A 1 49  ? -14.440 3.950  -8.790  1.00 11.41 ? 17  LEU   A O   1 
ATOM   57   C CB  . LEU   A 1 49  ? -15.746 1.962  -6.685  1.00 14.62 ? 17  LEU   A CB  1 
ATOM   58   C CG  . LEU   A 1 49  ? -16.661 1.629  -5.516  1.00 16.64 ? 17  LEU   A CG  1 
ATOM   59   C CD1 . LEU   A 1 49  ? -17.311 0.302  -5.803  1.00 20.89 ? 17  LEU   A CD1 1 
ATOM   60   C CD2 . LEU   A 1 49  ? -15.910 1.603  -4.188  1.00 17.59 ? 17  LEU   A CD2 1 
ATOM   61   N N   . ASP   A 1 50  ? -12.835 2.826  -7.657  1.00 10.93 ? 18  ASP   A N   1 
ATOM   62   C CA  . ASP   A 1 50  ? -11.834 2.837  -8.717  1.00 11.30 ? 18  ASP   A CA  1 
ATOM   63   C C   . ASP   A 1 50  ? -11.844 1.457  -9.380  1.00 11.29 ? 18  ASP   A C   1 
ATOM   64   O O   . ASP   A 1 50  ? -11.429 0.464  -8.769  1.00 11.86 ? 18  ASP   A O   1 
ATOM   65   C CB  . ASP   A 1 50  ? -10.478 3.164  -8.088  1.00 11.86 ? 18  ASP   A CB  1 
ATOM   66   C CG  . ASP   A 1 50  ? -9.327  3.159  -9.074  1.00 13.53 ? 18  ASP   A CG  1 
ATOM   67   O OD1 . ASP   A 1 50  ? -9.364  2.418  -10.072 1.00 13.12 ? 18  ASP   A OD1 1 
ATOM   68   O OD2 . ASP   A 1 50  ? -8.348  3.888  -8.813  1.00 15.83 ? 18  ASP   A OD2 1 
ATOM   69   N N   . ALA   A 1 51  ? -12.311 1.399  -10.630 1.00 11.39 ? 19  ALA   A N   1 
ATOM   70   C CA  . ALA   A 1 51  ? -12.429 0.143  -11.368 1.00 12.63 ? 19  ALA   A CA  1 
ATOM   71   C C   . ALA   A 1 51  ? -11.116 -0.325 -11.991 1.00 12.53 ? 19  ALA   A C   1 
ATOM   72   O O   . ALA   A 1 51  ? -11.065 -1.443 -12.529 1.00 14.67 ? 19  ALA   A O   1 
ATOM   73   C CB  . ALA   A 1 51  ? -13.503 0.279  -12.453 1.00 14.14 ? 19  ALA   A CB  1 
ATOM   74   N N   . VAL   A 1 52  ? -10.068 0.500  -11.954 1.00 13.63 ? 20  VAL   A N   1 
ATOM   75   C CA  . VAL   A 1 52  ? -8.761  0.073  -12.447 1.00 14.65 ? 20  VAL   A CA  1 
ATOM   76   C C   . VAL   A 1 52  ? -8.018  -0.690 -11.372 1.00 14.27 ? 20  VAL   A C   1 
ATOM   77   O O   . VAL   A 1 52  ? -7.415  -1.735 -11.637 1.00 17.07 ? 20  VAL   A O   1 
ATOM   78   C CB  . VAL   A 1 52  ? -7.944  1.286  -12.936 1.00 15.10 ? 20  VAL   A CB  1 
ATOM   79   C CG1 . VAL   A 1 52  ? -6.490  0.897  -13.222 1.00 17.72 ? 20  VAL   A CG1 1 
ATOM   80   C CG2 . VAL   A 1 52  ? -8.589  1.902  -14.163 1.00 15.81 ? 20  VAL   A CG2 1 
ATOM   81   N N   . ARG   A 1 53  ? -8.071  -0.191 -10.142 1.00 14.11 ? 21  ARG   A N   1 
ATOM   82   C CA  . ARG   A 1 53  ? -7.305  -0.744 -9.043  1.00 15.92 ? 21  ARG   A CA  1 
ATOM   83   C C   . ARG   A 1 53  ? -8.122  -1.634 -8.123  1.00 14.53 ? 21  ARG   A C   1 
ATOM   84   O O   . ARG   A 1 53  ? -7.534  -2.352 -7.307  1.00 16.52 ? 21  ARG   A O   1 
ATOM   85   C CB  . ARG   A 1 53  ? -6.662  0.394  -8.248  1.00 18.86 ? 21  ARG   A CB  1 
ATOM   86   C CG  . ARG   A 1 53  ? -5.740  1.247  -9.104  1.00 22.86 ? 21  ARG   A CG  1 
ATOM   87   C CD  . ARG   A 1 53  ? -4.850  2.129  -8.262  1.00 27.08 ? 21  ARG   A CD  1 
ATOM   88   N NE  . ARG   A 1 53  ? -5.608  3.200  -7.632  1.00 28.89 ? 21  ARG   A NE  1 
ATOM   89   C CZ  . ARG   A 1 53  ? -5.097  4.075  -6.772  1.00 31.30 ? 21  ARG   A CZ  1 
ATOM   90   N NH1 . ARG   A 1 53  ? -5.868  5.017  -6.251  1.00 32.76 ? 21  ARG   A NH1 1 
ATOM   91   N NH2 . ARG   A 1 53  ? -3.821  4.000  -6.423  1.00 31.62 ? 21  ARG   A NH2 1 
ATOM   92   N N   . GLY   A 1 54  ? -9.444  -1.624 -8.240  1.00 12.49 ? 22  GLY   A N   1 
ATOM   93   C CA  . GLY   A 1 54  ? -10.268 -2.436 -7.366  1.00 13.21 ? 22  GLY   A CA  1 
ATOM   94   C C   . GLY   A 1 54  ? -10.211 -1.945 -5.940  1.00 12.70 ? 22  GLY   A C   1 
ATOM   95   O O   . GLY   A 1 54  ? -10.005 -2.725 -5.006  1.00 13.24 ? 22  GLY   A O   1 
ATOM   96   N N   . SER   A 1 55  ? -10.416 -0.645 -5.760  1.00 13.01 ? 23  SER   A N   1 
ATOM   97   C CA  . SER   A 1 55  ? -10.284 -0.023 -4.455  1.00 13.57 ? 23  SER   A CA  1 
ATOM   98   C C   . SER   A 1 55  ? -11.313 1.084  -4.354  1.00 13.19 ? 23  SER   A C   1 
ATOM   99   O O   . SER   A 1 55  ? -11.816 1.564  -5.377  1.00 13.68 ? 23  SER   A O   1 
ATOM   100  C CB  . SER   A 1 55  ? -8.891  0.594  -4.294  1.00 16.91 ? 23  SER   A CB  1 
ATOM   101  O OG  . SER   A 1 55  ? -8.697  1.603  -5.270  1.00 21.66 ? 23  SER   A OG  1 
ATOM   102  N N   . PRO   A 1 56  ? -11.638 1.526  -3.144  1.00 13.10 ? 24  PRO   A N   1 
ATOM   103  C CA  . PRO   A 1 56  ? -12.323 2.812  -3.018  1.00 12.56 ? 24  PRO   A CA  1 
ATOM   104  C C   . PRO   A 1 56  ? -11.468 3.878  -3.683  1.00 12.97 ? 24  PRO   A C   1 
ATOM   105  O O   . PRO   A 1 56  ? -10.233 3.795  -3.699  1.00 14.41 ? 24  PRO   A O   1 
ATOM   106  C CB  . PRO   A 1 56  ? -12.398 3.037  -1.501  1.00 15.09 ? 24  PRO   A CB  1 
ATOM   107  C CG  . PRO   A 1 56  ? -12.126 1.730  -0.883  1.00 19.11 ? 24  PRO   A CG  1 
ATOM   108  C CD  . PRO   A 1 56  ? -11.286 0.942  -1.834  1.00 15.45 ? 24  PRO   A CD  1 
ATOM   109  N N   . ALA   A 1 57  ? -12.131 4.877  -4.251  1.00 12.86 ? 25  ALA   A N   1 
ATOM   110  C CA  . ALA   A 1 57  ? -11.444 6.054  -4.768  1.00 12.93 ? 25  ALA   A CA  1 
ATOM   111  C C   . ALA   A 1 57  ? -11.363 7.061  -3.627  1.00 13.20 ? 25  ALA   A C   1 
ATOM   112  O O   . ALA   A 1 57  ? -12.373 7.661  -3.246  1.00 13.47 ? 25  ALA   A O   1 
ATOM   113  C CB  . ALA   A 1 57  ? -12.176 6.623  -5.977  1.00 13.24 ? 25  ALA   A CB  1 
ATOM   114  N N   . ILE   A 1 58  ? -10.168 7.227  -3.076  1.00 13.73 ? 26  ILE   A N   1 
ATOM   115  C CA  . ILE   A 1 58  ? -9.951  8.004  -1.862  1.00 14.08 ? 26  ILE   A CA  1 
ATOM   116  C C   . ILE   A 1 58  ? -9.567  9.434  -2.228  1.00 15.02 ? 26  ILE   A C   1 
ATOM   117  O O   . ILE   A 1 58  ? -8.906  9.683  -3.243  1.00 16.20 ? 26  ILE   A O   1 
ATOM   118  C CB  . ILE   A 1 58  ? -8.871  7.320  -0.996  1.00 17.74 ? 26  ILE   A CB  1 
ATOM   119  C CG1 . ILE   A 1 58  ? -9.276  5.876  -0.686  1.00 19.11 ? 26  ILE   A CG1 1 
ATOM   120  C CG2 . ILE   A 1 58  ? -8.614  8.090  0.284   1.00 19.90 ? 26  ILE   A CG2 1 
ATOM   121  C CD1 . ILE   A 1 58  ? -8.190  5.083  0.013   1.00 21.60 ? 26  ILE   A CD1 1 
ATOM   122  N N   . ASN   A 1 59  ? -9.995  10.389 -1.395  1.00 15.59 ? 27  ASN   A N   1 
ATOM   123  C CA  . ASN   A 1 59  ? -9.641  11.803 -1.554  1.00 17.42 ? 27  ASN   A CA  1 
ATOM   124  C C   . ASN   A 1 59  ? -10.146 12.377 -2.874  1.00 16.44 ? 27  ASN   A C   1 
ATOM   125  O O   . ASN   A 1 59  ? -9.517  13.251 -3.471  1.00 17.91 ? 27  ASN   A O   1 
ATOM   126  C CB  . ASN   A 1 59  ? -8.141  12.043 -1.384  1.00 20.86 ? 27  ASN   A CB  1 
ATOM   127  C CG  . ASN   A 1 59  ? -7.671  11.796 0.030   1.00 25.97 ? 27  ASN   A CG  1 
ATOM   128  O OD1 . ASN   A 1 59  ? -8.380  12.099 0.990   1.00 28.56 ? 27  ASN   A OD1 1 
ATOM   129  N ND2 . ASN   A 1 59  ? -6.471  11.244 0.169   1.00 27.87 ? 27  ASN   A ND2 1 
ATOM   130  N N   . VAL   A 1 60  ? -11.307 11.915 -3.321  1.00 14.40 ? 28  VAL   A N   1 
ATOM   131  C CA  . VAL   A 1 60  ? -11.942 12.459 -4.513  1.00 13.36 ? 28  VAL   A CA  1 
ATOM   132  C C   . VAL   A 1 60  ? -12.803 13.639 -4.083  1.00 12.93 ? 28  VAL   A C   1 
ATOM   133  O O   . VAL   A 1 60  ? -13.699 13.491 -3.243  1.00 12.61 ? 28  VAL   A O   1 
ATOM   134  C CB  . VAL   A 1 60  ? -12.790 11.391 -5.214  1.00 13.92 ? 28  VAL   A CB  1 
ATOM   135  C CG1 . VAL   A 1 60  ? -13.490 11.986 -6.416  1.00 15.40 ? 28  VAL   A CG1 1 
ATOM   136  C CG2 . VAL   A 1 60  ? -11.922 10.212 -5.638  1.00 15.66 ? 28  VAL   A CG2 1 
ATOM   137  N N   . ALA   A 1 61  ? -12.533 14.808 -4.652  1.00 12.47 ? 29  ALA   A N   1 
ATOM   138  C CA  . ALA   A 1 61  ? -13.281 16.007 -4.317  1.00 12.07 ? 29  ALA   A CA  1 
ATOM   139  C C   . ALA   A 1 61  ? -14.583 16.046 -5.101  1.00 11.85 ? 29  ALA   A C   1 
ATOM   140  O O   . ALA   A 1 61  ? -14.659 15.584 -6.241  1.00 12.95 ? 29  ALA   A O   1 
ATOM   141  C CB  . ALA   A 1 61  ? -12.462 17.236 -4.691  1.00 13.64 ? 29  ALA   A CB  1 
ATOM   142  N N   . MET   A 1 62  ? -15.616 16.611 -4.484  1.00 11.52 ? 30  MET   A N   1 
ATOM   143  C CA  . MET   A 1 62  ? -16.851 16.845 -5.212  1.00 12.40 ? 30  MET   A CA  1 
ATOM   144  C C   . MET   A 1 62  ? -17.523 18.111 -4.709  1.00 11.75 ? 30  MET   A C   1 
ATOM   145  O O   . MET   A 1 62  ? -17.348 18.523 -3.556  1.00 12.60 ? 30  MET   A O   1 
ATOM   146  C CB  . MET   A 1 62  ? -17.801 15.645 -5.171  1.00 14.90 ? 30  MET   A CB  1 
ATOM   147  C CG  . MET   A 1 62  ? -18.357 15.322 -3.806  1.00 15.73 ? 30  MET   A CG  1 
ATOM   148  S SD  . MET   A 1 62  ? -19.090 13.677 -3.795  1.00 16.35 ? 30  MET   A SD  1 
ATOM   149  C CE  . MET   A 1 62  ? -17.633 12.635 -3.659  1.00 17.51 ? 30  MET   A CE  1 
ATOM   150  N N   . HIS   A 1 63  ? -18.289 18.717 -5.606  1.00 11.79 ? 31  HIS   A N   1 
ATOM   151  C CA  . HIS   A 1 63  ? -18.983 19.967 -5.358  1.00 12.70 ? 31  HIS   A CA  1 
ATOM   152  C C   . HIS   A 1 63  ? -20.447 19.751 -5.702  1.00 13.29 ? 31  HIS   A C   1 
ATOM   153  O O   . HIS   A 1 63  ? -20.761 19.236 -6.781  1.00 15.00 ? 31  HIS   A O   1 
ATOM   154  C CB  . HIS   A 1 63  ? -18.370 21.069 -6.231  1.00 15.43 ? 31  HIS   A CB  1 
ATOM   155  C CG  . HIS   A 1 63  ? -16.902 21.258 -5.994  1.00 16.99 ? 31  HIS   A CG  1 
ATOM   156  N ND1 . HIS   A 1 63  ? -16.397 22.297 -5.245  1.00 18.91 ? 31  HIS   A ND1 1 
ATOM   157  C CD2 . HIS   A 1 63  ? -15.835 20.507 -6.361  1.00 17.32 ? 31  HIS   A CD2 1 
ATOM   158  C CE1 . HIS   A 1 63  ? -15.080 22.193 -5.180  1.00 18.46 ? 31  HIS   A CE1 1 
ATOM   159  N NE2 . HIS   A 1 63  ? -14.713 21.117 -5.853  1.00 18.36 ? 31  HIS   A NE2 1 
ATOM   160  N N   . VAL   A 1 64  ? -21.334 20.124 -4.782  1.00 12.79 ? 32  VAL   A N   1 
ATOM   161  C CA  . VAL   A 1 64  ? -22.770 19.917 -4.932  1.00 13.19 ? 32  VAL   A CA  1 
ATOM   162  C C   . VAL   A 1 64  ? -23.437 21.274 -5.089  1.00 12.89 ? 32  VAL   A C   1 
ATOM   163  O O   . VAL   A 1 64  ? -23.222 22.181 -4.271  1.00 14.02 ? 32  VAL   A O   1 
ATOM   164  C CB  . VAL   A 1 64  ? -23.362 19.140 -3.744  1.00 14.03 ? 32  VAL   A CB  1 
ATOM   165  C CG1 . VAL   A 1 64  ? -24.828 18.803 -4.019  1.00 14.07 ? 32  VAL   A CG1 1 
ATOM   166  C CG2 . VAL   A 1 64  ? -22.553 17.865 -3.486  1.00 14.96 ? 32  VAL   A CG2 1 
ATOM   167  N N   . PHE   A 1 65  ? -24.242 21.404 -6.135  1.00 12.81 ? 33  PHE   A N   1 
ATOM   168  C CA  . PHE   A 1 65  ? -24.962 22.622 -6.456  1.00 12.76 ? 33  PHE   A CA  1 
ATOM   169  C C   . PHE   A 1 65  ? -26.450 22.336 -6.367  1.00 12.54 ? 33  PHE   A C   1 
ATOM   170  O O   . PHE   A 1 65  ? -26.891 21.187 -6.463  1.00 11.98 ? 33  PHE   A O   1 
ATOM   171  C CB  . PHE   A 1 65  ? -24.663 23.073 -7.889  1.00 14.64 ? 33  PHE   A CB  1 
ATOM   172  C CG  . PHE   A 1 65  ? -23.205 23.288 -8.176  1.00 16.80 ? 33  PHE   A CG  1 
ATOM   173  C CD1 . PHE   A 1 65  ? -22.378 22.219 -8.473  1.00 18.84 ? 33  PHE   A CD1 1 
ATOM   174  C CD2 . PHE   A 1 65  ? -22.675 24.566 -8.184  1.00 19.49 ? 33  PHE   A CD2 1 
ATOM   175  C CE1 . PHE   A 1 65  ? -21.039 22.418 -8.743  1.00 20.18 ? 33  PHE   A CE1 1 
ATOM   176  C CE2 . PHE   A 1 65  ? -21.341 24.770 -8.460  1.00 21.34 ? 33  PHE   A CE2 1 
ATOM   177  C CZ  . PHE   A 1 65  ? -20.523 23.696 -8.734  1.00 20.47 ? 33  PHE   A CZ  1 
ATOM   178  N N   . ARG   A 1 66  ? -27.219 23.395 -6.170  1.00 13.35 ? 34  ARG   A N   1 
ATOM   179  C CA  . ARG   A 1 66  ? -28.668 23.318 -6.160  1.00 14.04 ? 34  ARG   A CA  1 
ATOM   180  C C   . ARG   A 1 66  ? -29.199 24.423 -7.058  1.00 14.27 ? 34  ARG   A C   1 
ATOM   181  O O   . ARG   A 1 66  ? -28.729 25.563 -6.992  1.00 16.36 ? 34  ARG   A O   1 
ATOM   182  C CB  . ARG   A 1 66  ? -29.215 23.480 -4.740  1.00 15.07 ? 34  ARG   A CB  1 
ATOM   183  C CG  . ARG   A 1 66  ? -30.716 23.432 -4.668  1.00 16.44 ? 34  ARG   A CG  1 
ATOM   184  C CD  . ARG   A 1 66  ? -31.228 23.608 -3.261  1.00 17.54 ? 34  ARG   A CD  1 
ATOM   185  N NE  . ARG   A 1 66  ? -32.684 23.510 -3.276  1.00 19.82 ? 34  ARG   A NE  1 
ATOM   186  C CZ  . ARG   A 1 66  ? -33.514 24.490 -3.617  1.00 20.44 ? 34  ARG   A CZ  1 
ATOM   187  N NH1 . ARG   A 1 66  ? -33.048 25.692 -3.939  1.00 21.44 ? 34  ARG   A NH1 1 
ATOM   188  N NH2 . ARG   A 1 66  ? -34.819 24.260 -3.628  1.00 19.98 ? 34  ARG   A NH2 1 
ATOM   189  N N   . LYS   A 1 67  ? -30.171 24.086 -7.897  1.00 15.14 ? 35  LYS   A N   1 
ATOM   190  C CA  . LYS   A 1 67  ? -30.690 25.055 -8.851  1.00 16.71 ? 35  LYS   A CA  1 
ATOM   191  C C   . LYS   A 1 67  ? -31.531 26.101 -8.131  1.00 16.82 ? 35  LYS   A C   1 
ATOM   192  O O   . LYS   A 1 67  ? -32.465 25.767 -7.399  1.00 17.11 ? 35  LYS   A O   1 
ATOM   193  C CB  . LYS   A 1 67  ? -31.519 24.337 -9.915  1.00 21.84 ? 35  LYS   A CB  1 
ATOM   194  C CG  . LYS   A 1 67  ? -31.747 25.152 -11.175 1.00 29.32 ? 35  LYS   A CG  1 
ATOM   195  C CD  . LYS   A 1 67  ? -33.214 25.506 -11.336 1.00 35.63 ? 35  LYS   A CD  1 
ATOM   196  C CE  . LYS   A 1 67  ? -34.083 24.261 -11.279 1.00 39.60 ? 35  LYS   A CE  1 
ATOM   197  N NZ  . LYS   A 1 67  ? -35.501 24.537 -11.639 1.00 41.28 ? 35  LYS   A NZ  1 
ATOM   198  N N   . ALA   A 1 68  ? -31.188 27.370 -8.336  1.00 17.64 ? 36  ALA   A N   1 
ATOM   199  C CA  . ALA   A 1 68  ? -31.885 28.475 -7.703  1.00 20.01 ? 36  ALA   A CA  1 
ATOM   200  C C   . ALA   A 1 68  ? -33.144 28.828 -8.489  1.00 22.39 ? 36  ALA   A C   1 
ATOM   201  O O   . ALA   A 1 68  ? -33.395 28.311 -9.582  1.00 22.02 ? 36  ALA   A O   1 
ATOM   202  C CB  . ALA   A 1 68  ? -30.966 29.691 -7.616  1.00 19.93 ? 36  ALA   A CB  1 
ATOM   203  N N   . ALA   A 1 69  ? -33.932 29.743 -7.917  1.00 24.84 ? 37  ALA   A N   1 
ATOM   204  C CA  . ALA   A 1 69  ? -35.192 30.145 -8.533  1.00 28.68 ? 37  ALA   A CA  1 
ATOM   205  C C   . ALA   A 1 69  ? -34.987 30.767 -9.911  1.00 31.34 ? 37  ALA   A C   1 
ATOM   206  O O   . ALA   A 1 69  ? -35.862 30.652 -10.777 1.00 33.61 ? 37  ALA   A O   1 
ATOM   207  C CB  . ALA   A 1 69  ? -35.949 31.108 -7.615  1.00 29.51 ? 37  ALA   A CB  1 
ATOM   208  N N   . ASP   A 1 70  ? -33.851 31.428 -10.135 1.00 31.40 ? 38  ASP   A N   1 
ATOM   209  C CA  . ASP   A 1 70  ? -33.550 32.042 -11.421 1.00 32.84 ? 38  ASP   A CA  1 
ATOM   210  C C   . ASP   A 1 70  ? -32.893 31.077 -12.405 1.00 32.99 ? 38  ASP   A C   1 
ATOM   211  O O   . ASP   A 1 70  ? -32.338 31.526 -13.415 1.00 32.79 ? 38  ASP   A O   1 
ATOM   212  C CB  . ASP   A 1 70  ? -32.695 33.301 -11.236 1.00 33.84 ? 38  ASP   A CB  1 
ATOM   213  C CG  . ASP   A 1 70  ? -31.323 33.005 -10.653 1.00 35.03 ? 38  ASP   A CG  1 
ATOM   214  O OD1 . ASP   A 1 70  ? -31.037 31.834 -10.333 1.00 33.92 ? 38  ASP   A OD1 1 
ATOM   215  O OD2 . ASP   A 1 70  ? -30.524 33.954 -10.518 1.00 36.34 ? 38  ASP   A OD2 1 
ATOM   216  N N   . ASP   A 1 71  ? -32.941 29.773 -12.129 1.00 33.86 ? 39  ASP   A N   1 
ATOM   217  C CA  . ASP   A 1 71  ? -32.397 28.724 -12.990 1.00 36.18 ? 39  ASP   A CA  1 
ATOM   218  C C   . ASP   A 1 71  ? -30.873 28.706 -13.058 1.00 33.28 ? 39  ASP   A C   1 
ATOM   219  O O   . ASP   A 1 71  ? -30.306 28.116 -13.983 1.00 35.09 ? 39  ASP   A O   1 
ATOM   220  C CB  . ASP   A 1 71  ? -33.008 28.728 -14.399 1.00 41.33 ? 39  ASP   A CB  1 
ATOM   221  C CG  . ASP   A 1 71  ? -34.172 27.770 -14.529 1.00 45.91 ? 39  ASP   A CG  1 
ATOM   222  O OD1 . ASP   A 1 71  ? -35.239 28.048 -13.947 1.00 48.16 ? 39  ASP   A OD1 1 
ATOM   223  O OD2 . ASP   A 1 71  ? -34.016 26.736 -15.211 1.00 47.55 ? 39  ASP   A OD2 1 
ATOM   224  N N   . THR   A 1 72  ? -30.185 29.310 -12.096 1.00 28.60 ? 40  THR   A N   1 
ATOM   225  C CA  . THR   A 1 72  ? -28.735 29.202 -12.019 1.00 26.99 ? 40  THR   A CA  1 
ATOM   226  C C   . THR   A 1 72  ? -28.347 28.205 -10.931 1.00 22.57 ? 40  THR   A C   1 
ATOM   227  O O   . THR   A 1 72  ? -29.148 27.864 -10.059 1.00 22.38 ? 40  THR   A O   1 
ATOM   228  C CB  . THR   A 1 72  ? -28.101 30.566 -11.731 1.00 29.19 ? 40  THR   A CB  1 
ATOM   229  O OG1 . THR   A 1 72  ? -28.492 31.013 -10.426 1.00 30.40 ? 40  THR   A OG1 1 
ATOM   230  C CG2 . THR   A 1 72  ? -28.550 31.583 -12.766 1.00 30.65 ? 40  THR   A CG2 1 
ATOM   231  N N   . TRP   A 1 73  ? -27.108 27.725 -11.000 1.00 21.72 ? 41  TRP   A N   1 
ATOM   232  C CA  . TRP   A 1 73  ? -26.602 26.759 -10.032 1.00 20.80 ? 41  TRP   A CA  1 
ATOM   233  C C   . TRP   A 1 73  ? -26.000 27.497 -8.844  1.00 21.40 ? 41  TRP   A C   1 
ATOM   234  O O   . TRP   A 1 73  ? -25.048 28.268 -9.006  1.00 25.53 ? 41  TRP   A O   1 
ATOM   235  C CB  . TRP   A 1 73  ? -25.542 25.857 -10.666 1.00 19.71 ? 41  TRP   A CB  1 
ATOM   236  C CG  . TRP   A 1 73  ? -26.093 24.881 -11.661 1.00 20.91 ? 41  TRP   A CG  1 
ATOM   237  C CD1 . TRP   A 1 73  ? -25.869 24.872 -13.006 1.00 22.66 ? 41  TRP   A CD1 1 
ATOM   238  C CD2 . TRP   A 1 73  ? -26.964 23.773 -11.389 1.00 20.11 ? 41  TRP   A CD2 1 
ATOM   239  N NE1 . TRP   A 1 73  ? -26.544 23.827 -13.590 1.00 23.62 ? 41  TRP   A NE1 1 
ATOM   240  C CE2 . TRP   A 1 73  ? -27.223 23.136 -12.619 1.00 22.05 ? 41  TRP   A CE2 1 
ATOM   241  C CE3 . TRP   A 1 73  ? -27.551 23.262 -10.227 1.00 18.94 ? 41  TRP   A CE3 1 
ATOM   242  C CZ2 . TRP   A 1 73  ? -28.038 22.012 -12.720 1.00 22.56 ? 41  TRP   A CZ2 1 
ATOM   243  C CZ3 . TRP   A 1 73  ? -28.359 22.138 -10.329 1.00 19.58 ? 41  TRP   A CZ3 1 
ATOM   244  C CH2 . TRP   A 1 73  ? -28.599 21.531 -11.568 1.00 20.74 ? 41  TRP   A CH2 1 
ATOM   245  N N   . GLU   A 1 74  ? -26.551 27.272 -7.669  1.00 20.16 ? 42  GLU   A N   1 
ATOM   246  C CA  . GLU   A 1 74  ? -26.028 27.866 -6.450  1.00 23.16 ? 42  GLU   A CA  1 
ATOM   247  C C   . GLU   A 1 74  ? -25.226 26.843 -5.657  1.00 19.83 ? 42  GLU   A C   1 
ATOM   248  O O   . GLU   A 1 74  ? -25.565 25.656 -5.641  1.00 18.41 ? 42  GLU   A O   1 
ATOM   249  C CB  . GLU   A 1 74  ? -27.176 28.348 -5.564  1.00 31.34 ? 42  GLU   A CB  1 
ATOM   250  C CG  . GLU   A 1 74  ? -27.741 29.694 -5.948  1.00 40.17 ? 42  GLU   A CG  1 
ATOM   251  C CD  . GLU   A 1 74  ? -28.763 30.188 -4.945  1.00 47.48 ? 42  GLU   A CD  1 
ATOM   252  O OE1 . GLU   A 1 74  ? -29.287 29.351 -4.176  1.00 50.25 ? 42  GLU   A OE1 1 
ATOM   253  O OE2 . GLU   A 1 74  ? -29.040 31.404 -4.925  1.00 49.65 ? 42  GLU   A OE2 1 
ATOM   254  N N   . PRO   A 1 75  ? -24.170 27.267 -4.967  1.00 19.40 ? 43  PRO   A N   1 
ATOM   255  C CA  . PRO   A 1 75  ? -23.403 26.318 -4.149  1.00 19.98 ? 43  PRO   A CA  1 
ATOM   256  C C   . PRO   A 1 75  ? -24.259 25.731 -3.037  1.00 19.97 ? 43  PRO   A C   1 
ATOM   257  O O   . PRO   A 1 75  ? -25.038 26.435 -2.388  1.00 23.21 ? 43  PRO   A O   1 
ATOM   258  C CB  . PRO   A 1 75  ? -22.269 27.174 -3.577  1.00 21.99 ? 43  PRO   A CB  1 
ATOM   259  C CG  . PRO   A 1 75  ? -22.164 28.327 -4.509  1.00 23.31 ? 43  PRO   A CG  1 
ATOM   260  C CD  . PRO   A 1 75  ? -23.548 28.601 -5.001  1.00 21.31 ? 43  PRO   A CD  1 
ATOM   261  N N   . PHE   A 1 76  ? -24.111 24.426 -2.824  1.00 16.62 ? 44  PHE   A N   1 
ATOM   262  C CA  . PHE   A 1 76  ? -24.858 23.736 -1.779  1.00 14.99 ? 44  PHE   A CA  1 
ATOM   263  C C   . PHE   A 1 76  ? -23.967 23.054 -0.751  1.00 14.45 ? 44  PHE   A C   1 
ATOM   264  O O   . PHE   A 1 76  ? -24.173 23.244 0.450   1.00 16.83 ? 44  PHE   A O   1 
ATOM   265  C CB  . PHE   A 1 76  ? -25.880 22.765 -2.392  1.00 15.85 ? 44  PHE   A CB  1 
ATOM   266  C CG  . PHE   A 1 76  ? -26.725 22.062 -1.373  1.00 15.43 ? 44  PHE   A CG  1 
ATOM   267  C CD1 . PHE   A 1 76  ? -27.777 22.720 -0.750  1.00 16.49 ? 44  PHE   A CD1 1 
ATOM   268  C CD2 . PHE   A 1 76  ? -26.467 20.747 -1.029  1.00 16.42 ? 44  PHE   A CD2 1 
ATOM   269  C CE1 . PHE   A 1 76  ? -28.553 22.077 0.203   1.00 18.38 ? 44  PHE   A CE1 1 
ATOM   270  C CE2 . PHE   A 1 76  ? -27.233 20.099 -0.071  1.00 17.66 ? 44  PHE   A CE2 1 
ATOM   271  C CZ  . PHE   A 1 76  ? -28.279 20.770 0.541   1.00 18.06 ? 44  PHE   A CZ  1 
ATOM   272  N N   . ALA   A 1 77  ? -22.985 22.260 -1.179  1.00 14.12 ? 45  ALA   A N   1 
ATOM   273  C CA  . ALA   A 1 77  ? -22.107 21.548 -0.258  1.00 14.35 ? 45  ALA   A CA  1 
ATOM   274  C C   . ALA   A 1 77  ? -20.895 21.055 -1.034  1.00 12.85 ? 45  ALA   A C   1 
ATOM   275  O O   . ALA   A 1 77  ? -20.875 21.066 -2.264  1.00 14.03 ? 45  ALA   A O   1 
ATOM   276  C CB  . ALA   A 1 77  ? -22.822 20.353 0.381   1.00 17.09 ? 45  ALA   A CB  1 
ATOM   277  N N   . SER   A 1 78  ? -19.881 20.612 -0.301  1.00 13.70 ? 46  SER   A N   1 
ATOM   278  C CA  . SER   A 1 78  ? -18.706 20.028 -0.936  1.00 13.08 ? 46  SER   A CA  1 
ATOM   279  C C   . SER   A 1 78  ? -17.974 19.163 0.075   1.00 12.61 ? 46  SER   A C   1 
ATOM   280  O O   . SER   A 1 78  ? -18.207 19.255 1.279   1.00 15.29 ? 46  SER   A O   1 
ATOM   281  C CB  . SER   A 1 78  ? -17.763 21.092 -1.516  1.00 14.94 ? 46  SER   A CB  1 
ATOM   282  O OG  . SER   A 1 78  ? -17.201 21.874 -0.487  1.00 16.69 ? 46  SER   A OG  1 
ATOM   283  N N   . GLY   A 1 79  ? -17.079 18.326 -0.432  1.00 11.15 ? 47  GLY   A N   1 
ATOM   284  C CA  . GLY   A 1 79  ? -16.261 17.512 0.448   1.00 11.40 ? 47  GLY   A CA  1 
ATOM   285  C C   . GLY   A 1 79  ? -15.402 16.576 -0.368  1.00 11.77 ? 47  GLY   A C   1 
ATOM   286  O O   . GLY   A 1 79  ? -15.363 16.657 -1.594  1.00 12.19 ? 47  GLY   A O   1 
ATOM   287  N N   . LYS   A 1 80  ? -14.717 15.665 0.317   1.00 12.60 ? 48  LYS   A N   1 
ATOM   288  C CA  . LYS   A 1 80  ? -13.952 14.661 -0.404  1.00 14.57 ? 48  LYS   A CA  1 
ATOM   289  C C   . LYS   A 1 80  ? -14.126 13.294 0.232   1.00 13.65 ? 48  LYS   A C   1 
ATOM   290  O O   . LYS   A 1 80  ? -14.440 13.170 1.420   1.00 14.73 ? 48  LYS   A O   1 
ATOM   291  C CB  . LYS   A 1 80  ? -12.483 15.030 -0.602  1.00 20.04 ? 48  LYS   A CB  1 
ATOM   292  C CG  . LYS   A 1 80  ? -11.669 15.249 0.638   1.00 25.27 ? 48  LYS   A CG  1 
ATOM   293  C CD  . LYS   A 1 80  ? -10.299 15.795 0.213   1.00 29.76 ? 48  LYS   A CD  1 
ATOM   294  C CE  . LYS   A 1 80  ? -10.482 16.865 -0.873  1.00 32.16 ? 48  LYS   A CE  1 
ATOM   295  N NZ  . LYS   A 1 80  ? -9.245  17.421 -1.497  1.00 31.72 ? 48  LYS   A NZ  1 
ATOM   296  N N   . THR   A 1 81  ? -13.939 12.262 -0.584  1.00 12.71 ? 49  THR   A N   1 
ATOM   297  C CA  . THR   A 1 81  ? -14.173 10.911 -0.104  1.00 12.73 ? 49  THR   A CA  1 
ATOM   298  C C   . THR   A 1 81  ? -13.103 10.505 0.898   1.00 13.99 ? 49  THR   A C   1 
ATOM   299  O O   . THR   A 1 81  ? -11.943 10.911 0.809   1.00 15.03 ? 49  THR   A O   1 
ATOM   300  C CB  . THR   A 1 81  ? -14.193 9.904  -1.254  1.00 12.06 ? 49  THR   A CB  1 
ATOM   301  O OG1 . THR   A 1 81  ? -12.944 9.957  -1.953  1.00 12.69 ? 49  THR   A OG1 1 
ATOM   302  C CG2 . THR   A 1 81  ? -15.347 10.172 -2.211  1.00 13.67 ? 49  THR   A CG2 1 
ATOM   303  N N   . SER   A 1 82  ? -13.513 9.666  1.835   1.00 14.26 ? 50  SER   A N   1 
ATOM   304  C CA  . SER   A 1 82  ? -12.649 9.136  2.876   1.00 15.45 ? 50  SER   A CA  1 
ATOM   305  C C   . SER   A 1 82  ? -11.878 7.922  2.357   1.00 17.02 ? 50  SER   A C   1 
ATOM   306  O O   . SER   A 1 82  ? -11.957 7.542  1.183   1.00 16.36 ? 50  SER   A O   1 
ATOM   307  C CB  . SER   A 1 82  ? -13.508 8.703  4.057   1.00 17.54 ? 50  SER   A CB  1 
ATOM   308  O OG  . SER   A 1 82  ? -14.268 7.563  3.690   1.00 20.49 ? 50  SER   A OG  1 
ATOM   309  N N   . GLU   A 1 83  ? -11.167 7.263  3.276   1.00 19.55 ? 51  GLU   A N   1 
ATOM   310  C CA  . GLU   A 1 83  ? -10.437 6.042  2.968   1.00 22.13 ? 51  GLU   A CA  1 
ATOM   311  C C   . GLU   A 1 83  ? -11.356 4.924  2.496   1.00 19.97 ? 51  GLU   A C   1 
ATOM   312  O O   . GLU   A 1 83  ? -10.889 3.991  1.833   1.00 20.96 ? 51  GLU   A O   1 
ATOM   313  C CB  . GLU   A 1 83  ? -9.685  5.577  4.217   1.00 29.86 ? 51  GLU   A CB  1 
ATOM   314  C CG  . GLU   A 1 83  ? -8.331  4.942  3.950   1.00 39.40 ? 51  GLU   A CG  1 
ATOM   315  C CD  . GLU   A 1 83  ? -7.206  5.965  3.912   1.00 46.61 ? 51  GLU   A CD  1 
ATOM   316  O OE1 . GLU   A 1 83  ? -7.499  7.176  3.809   1.00 48.97 ? 51  GLU   A OE1 1 
ATOM   317  O OE2 . GLU   A 1 83  ? -6.028  5.554  3.990   1.00 49.53 ? 51  GLU   A OE2 1 
ATOM   318  N N   . SER   A 1 84  ? -12.646 4.994  2.817   1.00 18.74 ? 52  SER   A N   1 
ATOM   319  C CA  . SER   A 1 84  ? -13.611 4.000  2.371   1.00 18.05 ? 52  SER   A CA  1 
ATOM   320  C C   . SER   A 1 84  ? -14.244 4.363  1.039   1.00 15.61 ? 52  SER   A C   1 
ATOM   321  O O   . SER   A 1 84  ? -15.122 3.637  0.563   1.00 16.78 ? 52  SER   A O   1 
ATOM   322  C CB  . SER   A 1 84  ? -14.719 3.829  3.419   1.00 20.44 ? 52  SER   A CB  1 
ATOM   323  O OG  . SER   A 1 84  ? -15.544 4.981  3.476   1.00 24.00 ? 52  SER   A OG  1 
ATOM   324  N N   . GLY   A 1 85  ? -13.831 5.469  0.431   1.00 13.44 ? 53  GLY   A N   1 
ATOM   325  C CA  . GLY   A 1 85  ? -14.460 5.935  -0.785  1.00 12.78 ? 53  GLY   A CA  1 
ATOM   326  C C   . GLY   A 1 85  ? -15.763 6.665  -0.577  1.00 12.53 ? 53  GLY   A C   1 
ATOM   327  O O   . GLY   A 1 85  ? -16.427 7.004  -1.561  1.00 13.00 ? 53  GLY   A O   1 
ATOM   328  N N   . GLU   A 1 86  ? -16.150 6.923  0.668   1.00 14.21 ? 54  GLU   A N   1 
ATOM   329  C CA  . GLU   A 1 86  ? -17.448 7.499  0.975   1.00 14.27 ? 54  GLU   A CA  1 
ATOM   330  C C   . GLU   A 1 86  ? -17.308 8.931  1.466   1.00 13.88 ? 54  GLU   A C   1 
ATOM   331  O O   . GLU   A 1 86  ? -16.341 9.293  2.144   1.00 14.94 ? 54  GLU   A O   1 
ATOM   332  C CB  . GLU   A 1 86  ? -18.198 6.658  2.015   1.00 17.29 ? 54  GLU   A CB  1 
ATOM   333  C CG  . GLU   A 1 86  ? -18.457 5.234  1.528   1.00 19.42 ? 54  GLU   A CG  1 
ATOM   334  C CD  . GLU   A 1 86  ? -19.100 4.323  2.564   1.00 23.63 ? 54  GLU   A CD  1 
ATOM   335  O OE1 . GLU   A 1 86  ? -19.443 4.796  3.666   1.00 25.87 ? 54  GLU   A OE1 1 
ATOM   336  O OE2 . GLU   A 1 86  ? -19.256 3.119  2.270   1.00 27.10 ? 54  GLU   A OE2 1 
ATOM   337  N N   . LEU   A 1 87  ? -18.302 9.740  1.130   1.00 13.14 ? 55  LEU   A N   1 
ATOM   338  C CA  . LEU   A 1 87  ? -18.394 11.106 1.617   1.00 13.12 ? 55  LEU   A CA  1 
ATOM   339  C C   . LEU   A 1 87  ? -19.719 11.212 2.348   1.00 13.32 ? 55  LEU   A C   1 
ATOM   340  O O   . LEU   A 1 87  ? -20.783 11.171 1.722   1.00 14.34 ? 55  LEU   A O   1 
ATOM   341  C CB  . LEU   A 1 87  ? -18.311 12.096 0.464   1.00 13.26 ? 55  LEU   A CB  1 
ATOM   342  C CG  . LEU   A 1 87  ? -18.552 13.558 0.846   1.00 14.21 ? 55  LEU   A CG  1 
ATOM   343  C CD1 . LEU   A 1 87  ? -17.729 13.984 2.080   1.00 15.33 ? 55  LEU   A CD1 1 
ATOM   344  C CD2 . LEU   A 1 87  ? -18.286 14.478 -0.345  1.00 15.42 ? 55  LEU   A CD2 1 
ATOM   345  N N   . HIS   A 1 88  ? -19.641 11.331 3.668   1.00 15.52 ? 56  HIS   A N   1 
ATOM   346  C CA  . HIS   A 1 88  ? -20.785 11.473 4.552   1.00 16.79 ? 56  HIS   A CA  1 
ATOM   347  C C   . HIS   A 1 88  ? -20.875 12.914 5.035   1.00 18.96 ? 56  HIS   A C   1 
ATOM   348  O O   . HIS   A 1 88  ? -19.908 13.676 4.977   1.00 20.25 ? 56  HIS   A O   1 
ATOM   349  C CB  . HIS   A 1 88  ? -20.645 10.544 5.767   1.00 18.39 ? 56  HIS   A CB  1 
ATOM   350  C CG  . HIS   A 1 88  ? -20.675 9.087  5.422   1.00 20.46 ? 56  HIS   A CG  1 
ATOM   351  N ND1 . HIS   A 1 88  ? -21.820 8.326  5.513   1.00 22.14 ? 56  HIS   A ND1 1 
ATOM   352  C CD2 . HIS   A 1 88  ? -19.702 8.249  4.990   1.00 22.02 ? 56  HIS   A CD2 1 
ATOM   353  C CE1 . HIS   A 1 88  ? -21.552 7.083  5.152   1.00 22.22 ? 56  HIS   A CE1 1 
ATOM   354  N NE2 . HIS   A 1 88  ? -20.274 7.009  4.831   1.00 22.16 ? 56  HIS   A NE2 1 
ATOM   355  N N   . GLY   A 1 89  ? -22.058 13.282 5.511   1.00 18.82 ? 57  GLY   A N   1 
ATOM   356  C CA  . GLY   A 1 89  ? -22.215 14.560 6.175   1.00 20.11 ? 57  GLY   A CA  1 
ATOM   357  C C   . GLY   A 1 89  ? -22.276 15.778 5.282   1.00 19.50 ? 57  GLY   A C   1 
ATOM   358  O O   . GLY   A 1 89  ? -22.078 16.894 5.771   1.00 20.81 ? 57  GLY   A O   1 
ATOM   359  N N   . LEU   A 1 90  ? -22.537 15.604 3.983   1.00 17.94 ? 58  LEU   A N   1 
ATOM   360  C CA  . LEU   A 1 90  ? -22.661 16.751 3.082   1.00 16.55 ? 58  LEU   A CA  1 
ATOM   361  C C   . LEU   A 1 90  ? -23.754 17.714 3.528   1.00 17.33 ? 58  LEU   A C   1 
ATOM   362  O O   . LEU   A 1 90  ? -23.600 18.934 3.399   1.00 18.08 ? 58  LEU   A O   1 
ATOM   363  C CB  . LEU   A 1 90  ? -22.937 16.280 1.653   1.00 17.21 ? 58  LEU   A CB  1 
ATOM   364  C CG  . LEU   A 1 90  ? -21.732 15.892 0.794   1.00 17.79 ? 58  LEU   A CG  1 
ATOM   365  C CD1 . LEU   A 1 90  ? -22.180 15.107 -0.435  1.00 18.34 ? 58  LEU   A CD1 1 
ATOM   366  C CD2 . LEU   A 1 90  ? -20.956 17.125 0.385   1.00 19.40 ? 58  LEU   A CD2 1 
ATOM   367  N N   . THR   A 1 91  ? -24.859 17.191 4.061   1.00 16.17 ? 59  THR   A N   1 
ATOM   368  C CA  . THR   A 1 91  ? -26.012 18.022 4.381   1.00 15.63 ? 59  THR   A CA  1 
ATOM   369  C C   . THR   A 1 91  ? -26.763 17.423 5.567   1.00 17.70 ? 59  THR   A C   1 
ATOM   370  O O   . THR   A 1 91  ? -26.355 16.412 6.150   1.00 20.03 ? 59  THR   A O   1 
ATOM   371  C CB  . THR   A 1 91  ? -26.900 18.222 3.141   1.00 17.02 ? 59  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 91  ? -27.902 19.210 3.411   1.00 16.91 ? 59  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 91  ? -27.583 16.920 2.726   1.00 17.21 ? 59  THR   A CG2 1 
ATOM   374  N N   . THR   A 1 92  ? -27.872 18.067 5.927   1.00 18.09 ? 60  THR   A N   1 
ATOM   375  C CA  . THR   A 1 92  ? -28.732 17.644 7.020   1.00 18.65 ? 60  THR   A CA  1 
ATOM   376  C C   . THR   A 1 92  ? -30.145 17.490 6.486   1.00 17.43 ? 60  THR   A C   1 
ATOM   377  O O   . THR   A 1 92  ? -30.479 18.004 5.415   1.00 16.65 ? 60  THR   A O   1 
ATOM   378  C CB  . THR   A 1 92  ? -28.749 18.675 8.157   1.00 20.25 ? 60  THR   A CB  1 
ATOM   379  O OG1 . THR   A 1 92  ? -29.300 19.905 7.672   1.00 20.40 ? 60  THR   A OG1 1 
ATOM   380  C CG2 . THR   A 1 92  ? -27.342 18.921 8.680   1.00 21.73 ? 60  THR   A CG2 1 
ATOM   381  N N   . GLU   A 1 93  ? -30.991 16.808 7.261   1.00 18.68 ? 61  GLU   A N   1 
ATOM   382  C CA  . GLU   A 1 93  ? -32.384 16.665 6.855   1.00 19.98 ? 61  GLU   A CA  1 
ATOM   383  C C   . GLU   A 1 93  ? -33.057 18.024 6.716   1.00 18.53 ? 61  GLU   A C   1 
ATOM   384  O O   . GLU   A 1 93  ? -33.876 18.230 5.814   1.00 19.65 ? 61  GLU   A O   1 
ATOM   385  C CB  . GLU   A 1 93  ? -33.142 15.797 7.857   1.00 24.76 ? 61  GLU   A CB  1 
ATOM   386  C CG  . GLU   A 1 93  ? -32.687 14.355 7.875   1.00 30.76 ? 61  GLU   A CG  1 
ATOM   387  C CD  . GLU   A 1 93  ? -33.480 13.522 8.856   1.00 36.56 ? 61  GLU   A CD  1 
ATOM   388  O OE1 . GLU   A 1 93  ? -34.270 14.108 9.626   1.00 38.69 ? 61  GLU   A OE1 1 
ATOM   389  O OE2 . GLU   A 1 93  ? -33.317 12.285 8.851   1.00 39.11 ? 61  GLU   A OE2 1 
ATOM   390  N N   . GLU   A 1 94  ? -32.714 18.970 7.591   1.00 18.05 ? 62  GLU   A N   1 
ATOM   391  C CA  . GLU   A 1 94  ? -33.367 20.275 7.558   1.00 18.56 ? 62  GLU   A CA  1 
ATOM   392  C C   . GLU   A 1 94  ? -32.966 21.063 6.318   1.00 16.10 ? 62  GLU   A C   1 
ATOM   393  O O   . GLU   A 1 94  ? -33.794 21.754 5.712   1.00 16.55 ? 62  GLU   A O   1 
ATOM   394  C CB  . GLU   A 1 94  ? -33.005 21.064 8.819   1.00 22.80 ? 62  GLU   A CB  1 
ATOM   395  C CG  . GLU   A 1 94  ? -33.596 20.515 10.114  1.00 27.56 ? 62  GLU   A CG  1 
ATOM   396  C CD  . GLU   A 1 94  ? -32.908 19.246 10.603  1.00 31.72 ? 62  GLU   A CD  1 
ATOM   397  O OE1 . GLU   A 1 94  ? -31.736 19.004 10.233  1.00 31.94 ? 62  GLU   A OE1 1 
ATOM   398  O OE2 . GLU   A 1 94  ? -33.547 18.484 11.362  1.00 34.76 ? 62  GLU   A OE2 1 
ATOM   399  N N   . GLU   A 1 95  ? -31.699 20.970 5.927   1.00 14.82 ? 63  GLU   A N   1 
ATOM   400  C CA  . GLU   A 1 95  ? -31.183 21.767 4.827   1.00 14.99 ? 63  GLU   A CA  1 
ATOM   401  C C   . GLU   A 1 95  ? -31.506 21.155 3.468   1.00 12.86 ? 63  GLU   A C   1 
ATOM   402  O O   . GLU   A 1 95  ? -31.597 21.875 2.470   1.00 14.29 ? 63  GLU   A O   1 
ATOM   403  C CB  . GLU   A 1 95  ? -29.669 21.879 4.997   1.00 17.72 ? 63  GLU   A CB  1 
ATOM   404  C CG  . GLU   A 1 95  ? -28.951 22.671 3.923   1.00 22.22 ? 63  GLU   A CG  1 
ATOM   405  C CD  . GLU   A 1 95  ? -27.445 22.653 4.088   1.00 25.26 ? 63  GLU   A CD  1 
ATOM   406  O OE1 . GLU   A 1 95  ? -26.829 21.567 4.016   1.00 24.47 ? 63  GLU   A OE1 1 
ATOM   407  O OE2 . GLU   A 1 95  ? -26.870 23.736 4.289   1.00 27.22 ? 63  GLU   A OE2 1 
ATOM   408  N N   . PHE   A 1 96  ? -31.690 19.839 3.408   1.00 13.34 ? 64  PHE   A N   1 
ATOM   409  C CA  . PHE   A 1 96  ? -31.834 19.124 2.138   1.00 13.47 ? 64  PHE   A CA  1 
ATOM   410  C C   . PHE   A 1 96  ? -33.305 19.121 1.716   1.00 13.26 ? 64  PHE   A C   1 
ATOM   411  O O   . PHE   A 1 96  ? -34.017 18.117 1.794   1.00 15.43 ? 64  PHE   A O   1 
ATOM   412  C CB  . PHE   A 1 96  ? -31.259 17.725 2.294   1.00 13.55 ? 64  PHE   A CB  1 
ATOM   413  C CG  . PHE   A 1 96  ? -31.151 16.944 1.020   1.00 14.94 ? 64  PHE   A CG  1 
ATOM   414  C CD1 . PHE   A 1 96  ? -30.590 17.488 -0.123  1.00 16.30 ? 64  PHE   A CD1 1 
ATOM   415  C CD2 . PHE   A 1 96  ? -31.565 15.627 0.995   1.00 15.22 ? 64  PHE   A CD2 1 
ATOM   416  C CE1 . PHE   A 1 96  ? -30.469 16.727 -1.282  1.00 17.27 ? 64  PHE   A CE1 1 
ATOM   417  C CE2 . PHE   A 1 96  ? -31.452 14.865 -0.151  1.00 18.00 ? 64  PHE   A CE2 1 
ATOM   418  C CZ  . PHE   A 1 96  ? -30.903 15.409 -1.292  1.00 17.08 ? 64  PHE   A CZ  1 
ATOM   419  N N   . VAL   A 1 97  ? -33.751 20.271 1.221   1.00 12.86 ? 65  VAL   A N   1 
ATOM   420  C CA  . VAL   A 1 97  ? -35.123 20.475 0.760   1.00 11.92 ? 65  VAL   A CA  1 
ATOM   421  C C   . VAL   A 1 97  ? -35.315 19.951 -0.659  1.00 12.32 ? 65  VAL   A C   1 
ATOM   422  O O   . VAL   A 1 97  ? -34.357 19.528 -1.312  1.00 13.38 ? 65  VAL   A O   1 
ATOM   423  C CB  . VAL   A 1 97  ? -35.502 21.965 0.854   1.00 12.97 ? 65  VAL   A CB  1 
ATOM   424  C CG1 . VAL   A 1 97  ? -35.479 22.405 2.304   1.00 14.89 ? 65  VAL   A CG1 1 
ATOM   425  C CG2 . VAL   A 1 97  ? -34.543 22.802 0.005   1.00 14.31 ? 65  VAL   A CG2 1 
ATOM   426  N N   . GLU   A 1 98  ? -36.563 19.952 -1.133  1.00 13.36 ? 66  GLU   A N   1 
ATOM   427  C CA  . GLU   A 1 98  ? -36.839 19.716 -2.547  1.00 15.55 ? 66  GLU   A CA  1 
ATOM   428  C C   . GLU   A 1 98  ? -35.954 20.592 -3.418  1.00 14.44 ? 66  GLU   A C   1 
ATOM   429  O O   . GLU   A 1 98  ? -35.697 21.755 -3.100  1.00 16.81 ? 66  GLU   A O   1 
ATOM   430  C CB  . GLU   A 1 98  ? -38.281 20.113 -2.871  1.00 21.20 ? 66  GLU   A CB  1 
ATOM   431  C CG  . GLU   A 1 98  ? -39.364 19.208 -2.372  1.00 27.84 ? 66  GLU   A CG  1 
ATOM   432  C CD  . GLU   A 1 98  ? -40.718 19.643 -2.896  1.00 32.76 ? 66  GLU   A CD  1 
ATOM   433  O OE1 . GLU   A 1 98  ? -40.984 19.427 -4.099  1.00 35.04 ? 66  GLU   A OE1 1 
ATOM   434  O OE2 . GLU   A 1 98  ? -41.500 20.226 -2.120  1.00 33.27 ? 66  GLU   A OE2 1 
ATOM   435  N N   . GLY   A 1 99  ? -35.545 20.053 -4.553  1.00 13.75 ? 67  GLY   A N   1 
ATOM   436  C CA  . GLY   A 1 99  ? -34.840 20.855 -5.528  1.00 14.79 ? 67  GLY   A CA  1 
ATOM   437  C C   . GLY   A 1 99  ? -34.168 19.968 -6.546  1.00 12.16 ? 67  GLY   A C   1 
ATOM   438  O O   . GLY   A 1 99  ? -34.195 18.737 -6.453  1.00 13.41 ? 67  GLY   A O   1 
ATOM   439  N N   . ILE   A 1 100 ? -33.545 20.622 -7.515  1.00 12.52 ? 68  ILE   A N   1 
ATOM   440  C CA  . ILE   A 1 100 ? -32.688 19.950 -8.479  1.00 12.76 ? 68  ILE   A CA  1 
ATOM   441  C C   . ILE   A 1 100 ? -31.252 20.149 -8.023  1.00 11.88 ? 68  ILE   A C   1 
ATOM   442  O O   . ILE   A 1 100 ? -30.806 21.291 -7.842  1.00 13.67 ? 68  ILE   A O   1 
ATOM   443  C CB  . ILE   A 1 100 ? -32.904 20.480 -9.905  1.00 13.86 ? 68  ILE   A CB  1 
ATOM   444  C CG1 . ILE   A 1 100 ? -34.358 20.265 -10.337 1.00 16.22 ? 68  ILE   A CG1 1 
ATOM   445  C CG2 . ILE   A 1 100 ? -31.943 19.790 -10.866 1.00 14.94 ? 68  ILE   A CG2 1 
ATOM   446  C CD1 . ILE   A 1 100 ? -34.692 20.799 -11.712 1.00 18.53 ? 68  ILE   A CD1 1 
ATOM   447  N N   . TYR   A 1 101 ? -30.547 19.038 -7.801  1.00 11.08 ? 69  TYR   A N   1 
ATOM   448  C CA  . TYR   A 1 101 ? -29.190 19.046 -7.284  1.00 11.61 ? 69  TYR   A CA  1 
ATOM   449  C C   . TYR   A 1 101 ? -28.254 18.495 -8.343  1.00 11.20 ? 69  TYR   A C   1 
ATOM   450  O O   . TYR   A 1 101 ? -28.637 17.644 -9.150  1.00 12.25 ? 69  TYR   A O   1 
ATOM   451  C CB  . TYR   A 1 101 ? -29.092 18.195 -6.009  1.00 11.26 ? 69  TYR   A CB  1 
ATOM   452  C CG  . TYR   A 1 101 ? -29.841 18.795 -4.839  1.00 11.25 ? 69  TYR   A CG  1 
ATOM   453  C CD1 . TYR   A 1 101 ? -31.211 18.604 -4.685  1.00 12.05 ? 69  TYR   A CD1 1 
ATOM   454  C CD2 . TYR   A 1 101 ? -29.179 19.568 -3.895  1.00 12.54 ? 69  TYR   A CD2 1 
ATOM   455  C CE1 . TYR   A 1 101 ? -31.902 19.180 -3.616  1.00 12.33 ? 69  TYR   A CE1 1 
ATOM   456  C CE2 . TYR   A 1 101 ? -29.857 20.134 -2.827  1.00 12.89 ? 69  TYR   A CE2 1 
ATOM   457  C CZ  . TYR   A 1 101 ? -31.213 19.933 -2.691  1.00 12.70 ? 69  TYR   A CZ  1 
ATOM   458  O OH  . TYR   A 1 101 ? -31.864 20.508 -1.623  1.00 13.54 ? 69  TYR   A OH  1 
ATOM   459  N N   . LYS   A 1 102 ? -27.033 19.010 -8.346  1.00 11.76 ? 70  LYS   A N   1 
ATOM   460  C CA  . LYS   A 1 102 ? -25.981 18.537 -9.233  1.00 11.67 ? 70  LYS   A CA  1 
ATOM   461  C C   . LYS   A 1 102 ? -24.756 18.228 -8.392  1.00 11.97 ? 70  LYS   A C   1 
ATOM   462  O O   . LYS   A 1 102 ? -24.228 19.112 -7.714  1.00 13.25 ? 70  LYS   A O   1 
ATOM   463  C CB  . LYS   A 1 102 ? -25.634 19.570 -10.311 1.00 13.22 ? 70  LYS   A CB  1 
ATOM   464  C CG  . LYS   A 1 102 ? -24.396 19.187 -11.117 1.00 14.50 ? 70  LYS   A CG  1 
ATOM   465  C CD  . LYS   A 1 102 ? -24.141 20.111 -12.295 1.00 17.85 ? 70  LYS   A CD  1 
ATOM   466  C CE  . LYS   A 1 102 ? -23.876 21.537 -11.843 1.00 21.00 ? 70  LYS   A CE  1 
ATOM   467  N NZ  . LYS   A 1 102 ? -23.272 22.353 -12.939 1.00 24.12 ? 70  LYS   A NZ  1 
ATOM   468  N N   . VAL   A 1 103 ? -24.308 16.981 -8.443  1.00 11.81 ? 71  VAL   A N   1 
ATOM   469  C CA  . VAL   A 1 103 ? -23.054 16.564 -7.831  1.00 12.31 ? 71  VAL   A CA  1 
ATOM   470  C C   . VAL   A 1 103 ? -22.006 16.482 -8.930  1.00 12.39 ? 71  VAL   A C   1 
ATOM   471  O O   . VAL   A 1 103 ? -22.151 15.710 -9.885  1.00 14.14 ? 71  VAL   A O   1 
ATOM   472  C CB  . VAL   A 1 103 ? -23.202 15.202 -7.139  1.00 13.51 ? 71  VAL   A CB  1 
ATOM   473  C CG1 . VAL   A 1 103 ? -21.887 14.817 -6.455  1.00 14.98 ? 71  VAL   A CG1 1 
ATOM   474  C CG2 . VAL   A 1 103 ? -24.357 15.221 -6.146  1.00 14.42 ? 71  VAL   A CG2 1 
ATOM   475  N N   . GLU   A 1 104 ? -20.944 17.254 -8.788  1.00 12.53 ? 72  GLU   A N   1 
ATOM   476  C CA  . GLU   A 1 104 ? -19.840 17.270 -9.735  1.00 12.62 ? 72  GLU   A CA  1 
ATOM   477  C C   . GLU   A 1 104 ? -18.645 16.626 -9.046  1.00 12.10 ? 72  GLU   A C   1 
ATOM   478  O O   . GLU   A 1 104 ? -18.081 17.196 -8.109  1.00 13.88 ? 72  GLU   A O   1 
ATOM   479  C CB  . GLU   A 1 104 ? -19.554 18.716 -10.108 1.00 17.45 ? 72  GLU   A CB  1 
ATOM   480  C CG  . GLU   A 1 104 ? -18.345 18.970 -10.930 1.00 25.25 ? 72  GLU   A CG  1 
ATOM   481  C CD  . GLU   A 1 104 ? -18.244 20.443 -11.227 1.00 31.91 ? 72  GLU   A CD  1 
ATOM   482  O OE1 . GLU   A 1 104 ? -19.153 20.957 -11.914 1.00 32.44 ? 72  GLU   A OE1 1 
ATOM   483  O OE2 . GLU   A 1 104 ? -17.303 21.099 -10.726 1.00 35.90 ? 72  GLU   A OE2 1 
ATOM   484  N N   . ILE   A 1 105 ? -18.268 15.443 -9.505  1.00 11.90 ? 73  ILE   A N   1 
ATOM   485  C CA  . ILE   A 1 105 ? -17.193 14.659 -8.903  1.00 11.69 ? 73  ILE   A CA  1 
ATOM   486  C C   . ILE   A 1 105 ? -15.921 14.903 -9.701  1.00 11.54 ? 73  ILE   A C   1 
ATOM   487  O O   . ILE   A 1 105 ? -15.894 14.662 -10.910 1.00 13.00 ? 73  ILE   A O   1 
ATOM   488  C CB  . ILE   A 1 105 ? -17.551 13.166 -8.889  1.00 13.32 ? 73  ILE   A CB  1 
ATOM   489  C CG1 . ILE   A 1 105 ? -18.896 12.935 -8.190  1.00 14.44 ? 73  ILE   A CG1 1 
ATOM   490  C CG2 . ILE   A 1 105 ? -16.440 12.369 -8.244  1.00 15.14 ? 73  ILE   A CG2 1 
ATOM   491  C CD1 . ILE   A 1 105 ? -19.307 11.479 -8.196  1.00 15.38 ? 73  ILE   A CD1 1 
ATOM   492  N N   . ASP   A 1 106 ? -14.860 15.361 -9.036  1.00 12.25 ? 74  ASP   A N   1 
ATOM   493  C CA  . ASP   A 1 106 ? -13.622 15.725 -9.732  1.00 14.02 ? 74  ASP   A CA  1 
ATOM   494  C C   . ASP   A 1 106 ? -12.788 14.481 -10.037 1.00 12.87 ? 74  ASP   A C   1 
ATOM   495  O O   . ASP   A 1 106 ? -11.746 14.214 -9.434  1.00 14.65 ? 74  ASP   A O   1 
ATOM   496  C CB  . ASP   A 1 106 ? -12.829 16.755 -8.944  1.00 16.71 ? 74  ASP   A CB  1 
ATOM   497  C CG  . ASP   A 1 106 ? -11.540 17.157 -9.648  1.00 20.98 ? 74  ASP   A CG  1 
ATOM   498  O OD1 . ASP   A 1 106 ? -11.350 16.781 -10.834 1.00 21.67 ? 74  ASP   A OD1 1 
ATOM   499  O OD2 . ASP   A 1 106 ? -10.704 17.834 -9.014  1.00 24.26 ? 74  ASP   A OD2 1 
ATOM   500  N N   . THR   A 1 107 ? -13.260 13.734 -11.032 1.00 12.46 ? 75  THR   A N   1 
ATOM   501  C CA  . THR   A 1 107 ? -12.577 12.515 -11.443 1.00 12.75 ? 75  THR   A CA  1 
ATOM   502  C C   . THR   A 1 107 ? -11.271 12.815 -12.167 1.00 12.98 ? 75  THR   A C   1 
ATOM   503  O O   . THR   A 1 107 ? -10.336 12.010 -12.107 1.00 12.76 ? 75  THR   A O   1 
ATOM   504  C CB  . THR   A 1 107 ? -13.501 11.692 -12.340 1.00 12.79 ? 75  THR   A CB  1 
ATOM   505  O OG1 . THR   A 1 107 ? -13.892 12.473 -13.475 1.00 12.74 ? 75  THR   A OG1 1 
ATOM   506  C CG2 . THR   A 1 107 ? -14.752 11.283 -11.591 1.00 14.38 ? 75  THR   A CG2 1 
ATOM   507  N N   . LYS   A 1 108 ? -11.177 13.967 -12.838 1.00 12.89 ? 76  LYS   A N   1 
ATOM   508  C CA  . LYS   A 1 108 ? -9.978  14.271 -13.613 1.00 13.54 ? 76  LYS   A CA  1 
ATOM   509  C C   . LYS   A 1 108 ? -8.757  14.402 -12.711 1.00 14.11 ? 76  LYS   A C   1 
ATOM   510  O O   . LYS   A 1 108 ? -7.702  13.833 -12.998 1.00 14.92 ? 76  LYS   A O   1 
ATOM   511  C CB  . LYS   A 1 108 ? -10.188 15.531 -14.448 1.00 14.58 ? 76  LYS   A CB  1 
ATOM   512  C CG  . LYS   A 1 108 ? -9.056  15.799 -15.416 1.00 17.23 ? 76  LYS   A CG  1 
ATOM   513  C CD  . LYS   A 1 108 ? -9.350  17.046 -16.229 1.00 20.32 ? 76  LYS   A CD  1 
ATOM   514  C CE  . LYS   A 1 108 ? -8.272  17.320 -17.258 1.00 23.16 ? 76  LYS   A CE  1 
ATOM   515  N NZ  . LYS   A 1 108 ? -8.524  18.591 -17.978 1.00 24.66 ? 76  LYS   A NZ  1 
ATOM   516  N N   . SER   A 1 109 ? -8.891  15.117 -11.592 1.00 16.61 ? 77  SER   A N   1 
ATOM   517  C CA  . SER   A 1 109 ? -7.759  15.243 -10.672 1.00 18.28 ? 77  SER   A CA  1 
ATOM   518  C C   . SER   A 1 109 ? -7.353  13.892 -10.098 1.00 16.72 ? 77  SER   A C   1 
ATOM   519  O O   . SER   A 1 109 ? -6.163  13.616 -9.906  1.00 17.82 ? 77  SER   A O   1 
ATOM   520  C CB  . SER   A 1 109 ? -8.093  16.213 -9.540  1.00 21.25 ? 77  SER   A CB  1 
ATOM   521  O OG  . SER   A 1 109 ? -8.325  17.517 -10.041 1.00 23.14 ? 77  SER   A OG  1 
ATOM   522  N N   . TYR   A 1 110 ? -8.335  13.038 -9.813  1.00 15.64 ? 78  TYR   A N   1 
ATOM   523  C CA  . TYR   A 1 110 ? -8.043  11.714 -9.283  1.00 16.13 ? 78  TYR   A CA  1 
ATOM   524  C C   . TYR   A 1 110 ? -7.164  10.919 -10.243 1.00 15.89 ? 78  TYR   A C   1 
ATOM   525  O O   . TYR   A 1 110 ? -6.141  10.349 -9.842  1.00 16.22 ? 78  TYR   A O   1 
ATOM   526  C CB  . TYR   A 1 110 ? -9.358  10.987 -9.003  1.00 15.35 ? 78  TYR   A CB  1 
ATOM   527  C CG  . TYR   A 1 110 ? -9.157  9.587  -8.498  1.00 14.56 ? 78  TYR   A CG  1 
ATOM   528  C CD1 . TYR   A 1 110 ? -8.859  9.353  -7.167  1.00 15.38 ? 78  TYR   A CD1 1 
ATOM   529  C CD2 . TYR   A 1 110 ? -9.254  8.498  -9.353  1.00 15.10 ? 78  TYR   A CD2 1 
ATOM   530  C CE1 . TYR   A 1 110 ? -8.668  8.085  -6.690  1.00 15.63 ? 78  TYR   A CE1 1 
ATOM   531  C CE2 . TYR   A 1 110 ? -9.068  7.212  -8.886  1.00 15.26 ? 78  TYR   A CE2 1 
ATOM   532  C CZ  . TYR   A 1 110 ? -8.781  7.013  -7.548  1.00 15.28 ? 78  TYR   A CZ  1 
ATOM   533  O OH  . TYR   A 1 110 ? -8.576  5.747  -7.059  1.00 16.67 ? 78  TYR   A OH  1 
ATOM   534  N N   . TRP   A 1 111 ? -7.551  10.858 -11.519 1.00 15.07 ? 79  TRP   A N   1 
ATOM   535  C CA  . TRP   A 1 111 ? -6.759  10.085 -12.471 1.00 15.06 ? 79  TRP   A CA  1 
ATOM   536  C C   . TRP   A 1 111 ? -5.403  10.726 -12.714 1.00 16.41 ? 79  TRP   A C   1 
ATOM   537  O O   . TRP   A 1 111 ? -4.385  10.029 -12.787 1.00 17.36 ? 79  TRP   A O   1 
ATOM   538  C CB  . TRP   A 1 111 ? -7.524  9.913  -13.780 1.00 13.40 ? 79  TRP   A CB  1 
ATOM   539  C CG  . TRP   A 1 111 ? -8.727  9.039  -13.638 1.00 11.61 ? 79  TRP   A CG  1 
ATOM   540  C CD1 . TRP   A 1 111 ? -10.031 9.387  -13.842 1.00 11.18 ? 79  TRP   A CD1 1 
ATOM   541  C CD2 . TRP   A 1 111 ? -8.738  7.673  -13.207 1.00 11.93 ? 79  TRP   A CD2 1 
ATOM   542  N NE1 . TRP   A 1 111 ? -10.850 8.315  -13.590 1.00 11.09 ? 79  TRP   A NE1 1 
ATOM   543  C CE2 . TRP   A 1 111 ? -10.080 7.252  -13.193 1.00 11.24 ? 79  TRP   A CE2 1 
ATOM   544  C CE3 . TRP   A 1 111 ? -7.740  6.763  -12.834 1.00 13.68 ? 79  TRP   A CE3 1 
ATOM   545  C CZ2 . TRP   A 1 111 ? -10.451 5.958  -12.824 1.00 12.53 ? 79  TRP   A CZ2 1 
ATOM   546  C CZ3 . TRP   A 1 111 ? -8.111  5.484  -12.471 1.00 14.28 ? 79  TRP   A CZ3 1 
ATOM   547  C CH2 . TRP   A 1 111 ? -9.452  5.091  -12.466 1.00 13.66 ? 79  TRP   A CH2 1 
ATOM   548  N N   . LYS   A 1 112 ? -5.368  12.052 -12.831 1.00 17.71 ? 80  LYS   A N   1 
ATOM   549  C CA  . LYS   A 1 112 ? -4.107  12.726 -13.121 1.00 20.54 ? 80  LYS   A CA  1 
ATOM   550  C C   . LYS   A 1 112 ? -3.072  12.456 -12.038 1.00 21.37 ? 80  LYS   A C   1 
ATOM   551  O O   . LYS   A 1 112 ? -1.888  12.263 -12.337 1.00 22.04 ? 80  LYS   A O   1 
ATOM   552  C CB  . LYS   A 1 112 ? -4.343  14.223 -13.313 1.00 23.09 ? 80  LYS   A CB  1 
ATOM   553  C CG  . LYS   A 1 112 ? -4.931  14.563 -14.675 1.00 27.18 ? 80  LYS   A CG  1 
ATOM   554  C CD  . LYS   A 1 112 ? -4.711  16.013 -15.048 1.00 33.43 ? 80  LYS   A CD  1 
ATOM   555  C CE  . LYS   A 1 112 ? -5.035  16.250 -16.517 1.00 37.73 ? 80  LYS   A CE  1 
ATOM   556  N NZ  . LYS   A 1 112 ? -4.315  15.310 -17.421 1.00 40.17 ? 80  LYS   A NZ  1 
ATOM   557  N N   . ALA   A 1 113 ? -3.504  12.418 -10.775 1.00 21.99 ? 81  ALA   A N   1 
ATOM   558  C CA  . ALA   A 1 113 ? -2.582  12.140 -9.679  1.00 23.77 ? 81  ALA   A CA  1 
ATOM   559  C C   . ALA   A 1 113 ? -1.983  10.744 -9.775  1.00 25.03 ? 81  ALA   A C   1 
ATOM   560  O O   . ALA   A 1 113 ? -0.889  10.514 -9.249  1.00 26.20 ? 81  ALA   A O   1 
ATOM   561  C CB  . ALA   A 1 113 ? -3.275  12.344 -8.331  1.00 24.46 ? 81  ALA   A CB  1 
ATOM   562  N N   . LEU   A 1 114 ? -2.673  9.816  -10.431 1.00 25.33 ? 82  LEU   A N   1 
ATOM   563  C CA  . LEU   A 1 114 ? -2.156  8.483  -10.705 1.00 27.68 ? 82  LEU   A CA  1 
ATOM   564  C C   . LEU   A 1 114 ? -1.350  8.414  -11.996 1.00 28.68 ? 82  LEU   A C   1 
ATOM   565  O O   . LEU   A 1 114 ? -0.914  7.323  -12.377 1.00 29.77 ? 82  LEU   A O   1 
ATOM   566  C CB  . LEU   A 1 114 ? -3.312  7.476  -10.769 1.00 30.11 ? 82  LEU   A CB  1 
ATOM   567  C CG  . LEU   A 1 114 ? -3.815  6.806  -9.484  1.00 32.71 ? 82  LEU   A CG  1 
ATOM   568  C CD1 . LEU   A 1 114 ? -3.233  7.437  -8.216  1.00 34.03 ? 82  LEU   A CD1 1 
ATOM   569  C CD2 . LEU   A 1 114 ? -5.343  6.779  -9.436  1.00 32.72 ? 82  LEU   A CD2 1 
ATOM   570  N N   . GLY   A 1 115 ? -1.135  9.544  -12.671 1.00 28.63 ? 83  GLY   A N   1 
ATOM   571  C CA  . GLY   A 1 115 ? -0.420  9.565  -13.933 1.00 29.16 ? 83  GLY   A CA  1 
ATOM   572  C C   . GLY   A 1 115 ? -1.249  9.202  -15.143 1.00 28.03 ? 83  GLY   A C   1 
ATOM   573  O O   . GLY   A 1 115 ? -0.680  8.927  -16.207 1.00 29.11 ? 83  GLY   A O   1 
ATOM   574  N N   . ILE   A 1 116 ? -2.571  9.188  -15.021 1.00 26.57 ? 84  ILE   A N   1 
ATOM   575  C CA  . ILE   A 1 116 ? -3.466  8.836  -16.114 1.00 25.90 ? 84  ILE   A CA  1 
ATOM   576  C C   . ILE   A 1 116 ? -4.129  10.103 -16.633 1.00 25.31 ? 84  ILE   A C   1 
ATOM   577  O O   . ILE   A 1 116 ? -4.565  10.955 -15.848 1.00 25.85 ? 84  ILE   A O   1 
ATOM   578  C CB  . ILE   A 1 116 ? -4.504  7.804  -15.632 1.00 26.94 ? 84  ILE   A CB  1 
ATOM   579  C CG1 . ILE   A 1 116 ? -3.808  6.480  -15.293 1.00 28.32 ? 84  ILE   A CG1 1 
ATOM   580  C CG2 . ILE   A 1 116 ? -5.574  7.588  -16.680 1.00 27.29 ? 84  ILE   A CG2 1 
ATOM   581  C CD1 . ILE   A 1 116 ? -4.616  5.551  -14.401 1.00 29.47 ? 84  ILE   A CD1 1 
ATOM   582  N N   . SER   A 1 117 ? -4.192  10.240 -17.961 1.00 23.88 ? 85  SER   A N   1 
ATOM   583  C CA  . SER   A 1 117 ? -4.901  11.348 -18.582 1.00 22.70 ? 85  SER   A CA  1 
ATOM   584  C C   . SER   A 1 117 ? -6.290  10.855 -18.956 1.00 19.24 ? 85  SER   A C   1 
ATOM   585  O O   . SER   A 1 117 ? -6.445  10.162 -19.973 1.00 20.84 ? 85  SER   A O   1 
ATOM   586  C CB  . SER   A 1 117 ? -4.148  11.834 -19.822 1.00 25.37 ? 85  SER   A CB  1 
ATOM   587  O OG  . SER   A 1 117 ? -2.912  12.418 -19.454 1.00 29.96 ? 85  SER   A OG  1 
ATOM   588  N N   . PRO   A 1 118 ? -7.322  11.164 -18.183 1.00 15.70 ? 86  PRO   A N   1 
ATOM   589  C CA  . PRO   A 1 118 ? -8.631  10.555 -18.408 1.00 13.95 ? 86  PRO   A CA  1 
ATOM   590  C C   . PRO   A 1 118 ? -9.444  11.339 -19.433 1.00 13.58 ? 86  PRO   A C   1 
ATOM   591  O O   . PRO   A 1 118 ? -9.067  12.424 -19.876 1.00 15.69 ? 86  PRO   A O   1 
ATOM   592  C CB  . PRO   A 1 118 ? -9.276  10.670 -17.028 1.00 14.83 ? 86  PRO   A CB  1 
ATOM   593  C CG  . PRO   A 1 118 ? -8.767  11.988 -16.540 1.00 15.97 ? 86  PRO   A CG  1 
ATOM   594  C CD  . PRO   A 1 118 ? -7.336  12.075 -17.024 1.00 16.78 ? 86  PRO   A CD  1 
ATOM   595  N N   . PHE   A 1 119 ? -10.596 10.773 -19.777 1.00 12.64 ? 87  PHE   A N   1 
ATOM   596  C CA  . PHE   A 1 119 ? -11.447 11.390 -20.786 1.00 12.65 ? 87  PHE   A CA  1 
ATOM   597  C C   . PHE   A 1 119 ? -12.277 12.539 -20.217 1.00 11.44 ? 87  PHE   A C   1 
ATOM   598  O O   . PHE   A 1 119 ? -12.328 13.632 -20.799 1.00 12.41 ? 87  PHE   A O   1 
ATOM   599  C CB  . PHE   A 1 119 ? -12.354 10.332 -21.420 1.00 14.26 ? 87  PHE   A CB  1 
ATOM   600  C CG  . PHE   A 1 119 ? -13.282 10.893 -22.450 1.00 16.53 ? 87  PHE   A CG  1 
ATOM   601  C CD1 . PHE   A 1 119 ? -12.807 11.274 -23.694 1.00 18.62 ? 87  PHE   A CD1 1 
ATOM   602  C CD2 . PHE   A 1 119 ? -14.621 11.079 -22.161 1.00 17.26 ? 87  PHE   A CD2 1 
ATOM   603  C CE1 . PHE   A 1 119 ? -13.661 11.820 -24.638 1.00 19.57 ? 87  PHE   A CE1 1 
ATOM   604  C CE2 . PHE   A 1 119 ? -15.483 11.612 -23.105 1.00 19.25 ? 87  PHE   A CE2 1 
ATOM   605  C CZ  . PHE   A 1 119 ? -14.999 11.985 -24.342 1.00 19.77 ? 87  PHE   A CZ  1 
ATOM   606  N N   . HIS   A 1 120 ? -12.953 12.316 -19.099 1.00 11.55 ? 88  HIS   A N   1 
ATOM   607  C CA  . HIS   A 1 120 ? -13.941 13.265 -18.616 1.00 11.47 ? 88  HIS   A CA  1 
ATOM   608  C C   . HIS   A 1 120 ? -13.315 14.347 -17.747 1.00 11.53 ? 88  HIS   A C   1 
ATOM   609  O O   . HIS   A 1 120 ? -12.330 14.120 -17.044 1.00 12.31 ? 88  HIS   A O   1 
ATOM   610  C CB  . HIS   A 1 120 ? -15.019 12.545 -17.814 1.00 12.15 ? 88  HIS   A CB  1 
ATOM   611  C CG  . HIS   A 1 120 ? -15.698 11.454 -18.575 1.00 13.46 ? 88  HIS   A CG  1 
ATOM   612  N ND1 . HIS   A 1 120 ? -15.311 10.135 -18.488 1.00 13.46 ? 88  HIS   A ND1 1 
ATOM   613  C CD2 . HIS   A 1 120 ? -16.715 11.494 -19.469 1.00 15.44 ? 88  HIS   A CD2 1 
ATOM   614  C CE1 . HIS   A 1 120 ? -16.076 9.406  -19.281 1.00 16.10 ? 88  HIS   A CE1 1 
ATOM   615  N NE2 . HIS   A 1 120 ? -16.933 10.206 -19.889 1.00 17.14 ? 88  HIS   A NE2 1 
ATOM   616  N N   . GLU   A 1 121 ? -13.915 15.536 -17.794 1.00 11.49 ? 89  GLU   A N   1 
ATOM   617  C CA  . GLU   A 1 121 ? -13.543 16.586 -16.855 1.00 12.78 ? 89  GLU   A CA  1 
ATOM   618  C C   . GLU   A 1 121 ? -13.999 16.247 -15.448 1.00 14.03 ? 89  GLU   A C   1 
ATOM   619  O O   . GLU   A 1 121 ? -13.302 16.532 -14.467 1.00 16.34 ? 89  GLU   A O   1 
ATOM   620  C CB  . GLU   A 1 121 ? -14.175 17.906 -17.285 1.00 15.58 ? 89  GLU   A CB  1 
ATOM   621  C CG  . GLU   A 1 121 ? -13.515 18.515 -18.495 1.00 16.95 ? 89  GLU   A CG  1 
ATOM   622  C CD  . GLU   A 1 121 ? -12.074 18.882 -18.223 1.00 19.69 ? 89  GLU   A CD  1 
ATOM   623  O OE1 . GLU   A 1 121 ? -11.815 19.688 -17.303 1.00 22.15 ? 89  GLU   A OE1 1 
ATOM   624  O OE2 . GLU   A 1 121 ? -11.199 18.346 -18.913 1.00 21.05 ? 89  GLU   A OE2 1 
ATOM   625  N N   . HIS   A 1 122 ? -15.179 15.660 -15.332 1.00 13.58 ? 90  HIS   A N   1 
ATOM   626  C CA  . HIS   A 1 122 ? -15.739 15.286 -14.047 1.00 14.71 ? 90  HIS   A CA  1 
ATOM   627  C C   . HIS   A 1 122 ? -16.875 14.321 -14.341 1.00 15.84 ? 90  HIS   A C   1 
ATOM   628  O O   . HIS   A 1 122 ? -17.282 14.150 -15.492 1.00 17.95 ? 90  HIS   A O   1 
ATOM   629  C CB  . HIS   A 1 122 ? -16.171 16.513 -13.217 1.00 19.06 ? 90  HIS   A CB  1 
ATOM   630  C CG  . HIS   A 1 122 ? -16.978 17.520 -13.972 1.00 25.23 ? 90  HIS   A CG  1 
ATOM   631  N ND1 . HIS   A 1 122 ? -18.323 17.360 -14.224 1.00 29.68 ? 90  HIS   A ND1 1 
ATOM   632  C CD2 . HIS   A 1 122 ? -16.635 18.717 -14.502 1.00 27.88 ? 90  HIS   A CD2 1 
ATOM   633  C CE1 . HIS   A 1 122 ? -18.772 18.408 -14.892 1.00 30.94 ? 90  HIS   A CE1 1 
ATOM   634  N NE2 . HIS   A 1 122 ? -17.766 19.246 -15.075 1.00 30.39 ? 90  HIS   A NE2 1 
ATOM   635  N N   . ALA   A 1 123 ? -17.351 13.659 -13.299 1.00 16.87 ? 91  ALA   A N   1 
ATOM   636  C CA  . ALA   A 1 123 ? -18.550 12.843 -13.381 1.00 18.44 ? 91  ALA   A CA  1 
ATOM   637  C C   . ALA   A 1 123 ? -19.664 13.644 -12.734 1.00 18.16 ? 91  ALA   A C   1 
ATOM   638  O O   . ALA   A 1 123 ? -19.519 14.101 -11.597 1.00 18.63 ? 91  ALA   A O   1 
ATOM   639  C CB  . ALA   A 1 123 ? -18.363 11.519 -12.639 1.00 19.41 ? 91  ALA   A CB  1 
ATOM   640  N N   . GLU   A 1 124 ? -20.757 13.832 -13.463 1.00 20.15 ? 92  GLU   A N   1 
ATOM   641  C CA  . GLU   A 1 124 ? -21.857 14.679 -13.030 1.00 21.86 ? 92  GLU   A CA  1 
ATOM   642  C C   . GLU   A 1 124 ? -23.073 13.821 -12.717 1.00 21.73 ? 92  GLU   A C   1 
ATOM   643  O O   . GLU   A 1 124 ? -23.328 12.811 -13.384 1.00 25.17 ? 92  GLU   A O   1 
ATOM   644  C CB  . GLU   A 1 124 ? -22.219 15.697 -14.113 1.00 24.30 ? 92  GLU   A CB  1 
ATOM   645  N N   . VAL   A 1 125 ? -23.820 14.223 -11.694 1.00 17.13 ? 93  VAL   A N   1 
ATOM   646  C CA  . VAL   A 1 125 ? -25.063 13.556 -11.317 1.00 15.00 ? 93  VAL   A CA  1 
ATOM   647  C C   . VAL   A 1 125 ? -26.089 14.655 -11.041 1.00 12.44 ? 93  VAL   A C   1 
ATOM   648  O O   . VAL   A 1 125 ? -25.934 15.422 -10.088 1.00 13.50 ? 93  VAL   A O   1 
ATOM   649  C CB  . VAL   A 1 125 ? -24.877 12.665 -10.078 1.00 17.40 ? 93  VAL   A CB  1 
ATOM   650  C CG1 . VAL   A 1 125 ? -26.152 11.910 -9.788  1.00 18.22 ? 93  VAL   A CG1 1 
ATOM   651  C CG2 . VAL   A 1 125 ? -23.701 11.690 -10.263 1.00 19.17 ? 93  VAL   A CG2 1 
ATOM   652  N N   . VAL   A 1 126 ? -27.122 14.747 -11.876 1.00 11.15 ? 94  VAL   A N   1 
ATOM   653  C CA  . VAL   A 1 126 ? -28.137 15.791 -11.768 1.00 11.18 ? 94  VAL   A CA  1 
ATOM   654  C C   . VAL   A 1 126 ? -29.488 15.132 -11.529 1.00 10.28 ? 94  VAL   A C   1 
ATOM   655  O O   . VAL   A 1 126 ? -29.898 14.260 -12.302 1.00 11.09 ? 94  VAL   A O   1 
ATOM   656  C CB  . VAL   A 1 126 ? -28.169 16.675 -13.030 1.00 12.11 ? 94  VAL   A CB  1 
ATOM   657  C CG1 . VAL   A 1 126 ? -29.136 17.848 -12.836 1.00 13.24 ? 94  VAL   A CG1 1 
ATOM   658  C CG2 . VAL   A 1 126 ? -26.774 17.167 -13.388 1.00 14.41 ? 94  VAL   A CG2 1 
ATOM   659  N N   . PHE   A 1 127 ? -30.177 15.535 -10.462 1.00 10.98 ? 95  PHE   A N   1 
ATOM   660  C CA  . PHE   A 1 127 ? -31.390 14.829 -10.068 1.00 11.21 ? 95  PHE   A CA  1 
ATOM   661  C C   . PHE   A 1 127 ? -32.304 15.743 -9.267  1.00 11.20 ? 95  PHE   A C   1 
ATOM   662  O O   . PHE   A 1 127 ? -31.841 16.632 -8.551  1.00 12.43 ? 95  PHE   A O   1 
ATOM   663  C CB  . PHE   A 1 127 ? -31.078 13.571 -9.248  1.00 11.61 ? 95  PHE   A CB  1 
ATOM   664  C CG  . PHE   A 1 127 ? -30.422 13.836 -7.911  1.00 11.55 ? 95  PHE   A CG  1 
ATOM   665  C CD1 . PHE   A 1 127 ? -29.074 14.159 -7.826  1.00 13.56 ? 95  PHE   A CD1 1 
ATOM   666  C CD2 . PHE   A 1 127 ? -31.138 13.681 -6.735  1.00 12.88 ? 95  PHE   A CD2 1 
ATOM   667  C CE1 . PHE   A 1 127 ? -28.467 14.368 -6.589  1.00 14.91 ? 95  PHE   A CE1 1 
ATOM   668  C CE2 . PHE   A 1 127 ? -30.535 13.871 -5.500  1.00 15.32 ? 95  PHE   A CE2 1 
ATOM   669  C CZ  . PHE   A 1 127 ? -29.202 14.225 -5.429  1.00 16.18 ? 95  PHE   A CZ  1 
ATOM   670  N N   . THR   A 1 128 ? -33.609 15.487 -9.374  1.00 11.53 ? 96  THR   A N   1 
ATOM   671  C CA  . THR   A 1 128 ? -34.577 16.102 -8.474  1.00 12.78 ? 96  THR   A CA  1 
ATOM   672  C C   . THR   A 1 128 ? -34.667 15.279 -7.194  1.00 13.31 ? 96  THR   A C   1 
ATOM   673  O O   . THR   A 1 128 ? -34.809 14.053 -7.239  1.00 14.67 ? 96  THR   A O   1 
ATOM   674  C CB  . THR   A 1 128 ? -35.952 16.175 -9.142  1.00 14.66 ? 96  THR   A CB  1 
ATOM   675  O OG1 . THR   A 1 128 ? -35.888 17.015 -10.299 1.00 16.71 ? 96  THR   A OG1 1 
ATOM   676  C CG2 . THR   A 1 128 ? -36.962 16.763 -8.184  1.00 16.21 ? 96  THR   A CG2 1 
ATOM   677  N N   . ALA   A 1 129 ? -34.582 15.947 -6.050  1.00 12.91 ? 97  ALA   A N   1 
ATOM   678  C CA  . ALA   A 1 129 ? -34.611 15.280 -4.759  1.00 13.49 ? 97  ALA   A CA  1 
ATOM   679  C C   . ALA   A 1 129 ? -35.861 15.678 -3.995  1.00 13.12 ? 97  ALA   A C   1 
ATOM   680  O O   . ALA   A 1 129 ? -36.307 16.827 -4.071  1.00 14.30 ? 97  ALA   A O   1 
ATOM   681  C CB  . ALA   A 1 129 ? -33.381 15.635 -3.928  1.00 15.24 ? 97  ALA   A CB  1 
ATOM   682  N N   . ASN   A 1 130 ? -36.421 14.712 -3.260  1.00 13.91 ? 98  ASN   A N   1 
ATOM   683  C CA  . ASN   A 1 130 ? -37.446 14.928 -2.243  1.00 15.61 ? 98  ASN   A CA  1 
ATOM   684  C C   . ASN   A 1 130 ? -38.767 15.424 -2.809  1.00 18.66 ? 98  ASN   A C   1 
ATOM   685  O O   . ASN   A 1 130 ? -39.566 16.010 -2.074  1.00 20.29 ? 98  ASN   A O   1 
ATOM   686  C CB  . ASN   A 1 130 ? -36.943 15.836 -1.115  1.00 16.10 ? 98  ASN   A CB  1 
ATOM   687  C CG  . ASN   A 1 130 ? -35.611 15.383 -0.577  1.00 15.66 ? 98  ASN   A CG  1 
ATOM   688  O OD1 . ASN   A 1 130 ? -35.447 14.216 -0.204  1.00 16.21 ? 98  ASN   A OD1 1 
ATOM   689  N ND2 . ASN   A 1 130 ? -34.632 16.286 -0.582  1.00 16.24 ? 98  ASN   A ND2 1 
ATOM   690  N N   . ASP   A 1 131 ? -39.016 15.157 -4.096  1.00 21.05 ? 99  ASP   A N   1 
ATOM   691  C CA  . ASP   A 1 131 ? -40.225 15.621 -4.769  1.00 26.21 ? 99  ASP   A CA  1 
ATOM   692  C C   . ASP   A 1 131 ? -41.489 15.105 -4.092  1.00 26.16 ? 99  ASP   A C   1 
ATOM   693  O O   . ASP   A 1 131 ? -42.532 15.772 -4.133  1.00 26.25 ? 99  ASP   A O   1 
ATOM   694  C CB  . ASP   A 1 131 ? -40.190 15.146 -6.224  1.00 32.54 ? 99  ASP   A CB  1 
ATOM   695  C CG  . ASP   A 1 131 ? -40.855 16.112 -7.177  1.00 39.69 ? 99  ASP   A CG  1 
ATOM   696  O OD1 . ASP   A 1 131 ? -41.087 17.278 -6.791  1.00 41.82 ? 99  ASP   A OD1 1 
ATOM   697  O OD2 . ASP   A 1 131 ? -41.142 15.702 -8.322  1.00 42.49 ? 99  ASP   A OD2 1 
ATOM   698  N N   . SER   A 1 132 ? -41.428 13.915 -3.490  1.00 27.58 ? 100 SER   A N   1 
ATOM   699  C CA  . SER   A 1 132 ? -42.574 13.286 -2.842  1.00 30.60 ? 100 SER   A CA  1 
ATOM   700  C C   . SER   A 1 132 ? -42.332 13.097 -1.348  1.00 29.87 ? 100 SER   A C   1 
ATOM   701  O O   . SER   A 1 132 ? -42.813 12.129 -0.753  1.00 32.75 ? 100 SER   A O   1 
ATOM   702  C CB  . SER   A 1 132 ? -42.906 11.943 -3.495  1.00 34.05 ? 100 SER   A CB  1 
ATOM   703  O OG  . SER   A 1 132 ? -42.849 12.033 -4.908  1.00 37.13 ? 100 SER   A OG  1 
ATOM   704  N N   . GLY   A 1 133 ? -41.597 14.016 -0.728  1.00 25.03 ? 101 GLY   A N   1 
ATOM   705  C CA  . GLY   A 1 133 ? -41.257 13.897 0.668   1.00 21.77 ? 101 GLY   A CA  1 
ATOM   706  C C   . GLY   A 1 133 ? -39.804 13.520 0.861   1.00 19.93 ? 101 GLY   A C   1 
ATOM   707  O O   . GLY   A 1 133 ? -39.094 13.176 -0.090  1.00 19.44 ? 101 GLY   A O   1 
ATOM   708  N N   . PRO   A 1 134 ? -39.334 13.578 2.107   1.00 19.89 ? 102 PRO   A N   1 
ATOM   709  C CA  . PRO   A 1 134 ? -37.907 13.360 2.364   1.00 19.07 ? 102 PRO   A CA  1 
ATOM   710  C C   . PRO   A 1 134 ? -37.495 11.937 2.023   1.00 18.30 ? 102 PRO   A C   1 
ATOM   711  O O   . PRO   A 1 134 ? -38.198 10.972 2.331   1.00 19.17 ? 102 PRO   A O   1 
ATOM   712  C CB  . PRO   A 1 134 ? -37.764 13.627 3.868   1.00 20.76 ? 102 PRO   A CB  1 
ATOM   713  C CG  . PRO   A 1 134 ? -39.031 14.287 4.288   1.00 23.15 ? 102 PRO   A CG  1 
ATOM   714  C CD  . PRO   A 1 134 ? -40.090 13.852 3.340   1.00 21.75 ? 102 PRO   A CD  1 
ATOM   715  N N   . ARG   A 1 135 ? -36.348 11.817 1.365   1.00 17.18 ? 103 ARG   A N   1 
ATOM   716  C CA  . ARG   A 1 135 ? -35.762 10.526 1.057   1.00 16.35 ? 103 ARG   A CA  1 
ATOM   717  C C   . ARG   A 1 135 ? -34.283 10.580 1.401   1.00 15.78 ? 103 ARG   A C   1 
ATOM   718  O O   . ARG   A 1 135 ? -33.694 11.654 1.540   1.00 16.99 ? 103 ARG   A O   1 
ATOM   719  C CB  . ARG   A 1 135 ? -35.894 10.179 -0.434  1.00 17.58 ? 103 ARG   A CB  1 
ATOM   720  C CG  . ARG   A 1 135 ? -37.323 10.054 -0.938  1.00 18.77 ? 103 ARG   A CG  1 
ATOM   721  C CD  . ARG   A 1 135 ? -38.036 8.851  -0.347  1.00 20.90 ? 103 ARG   A CD  1 
ATOM   722  N NE  . ARG   A 1 135 ? -39.361 8.703  -0.936  1.00 22.60 ? 103 ARG   A NE  1 
ATOM   723  C CZ  . ARG   A 1 135 ? -40.449 9.290  -0.456  1.00 24.45 ? 103 ARG   A CZ  1 
ATOM   724  N NH1 . ARG   A 1 135 ? -40.364 10.043 0.631   1.00 25.16 ? 103 ARG   A NH1 1 
ATOM   725  N NH2 . ARG   A 1 135 ? -41.618 9.116  -1.052  1.00 26.63 ? 103 ARG   A NH2 1 
ATOM   726  N N   . ARG   A 1 136 ? -33.686 9.402  1.522   1.00 15.71 ? 104 ARG   A N   1 
ATOM   727  C CA  . ARG   A 1 136 ? -32.246 9.277  1.667   1.00 16.73 ? 104 ARG   A CA  1 
ATOM   728  C C   . ARG   A 1 136 ? -31.658 8.782  0.353   1.00 15.19 ? 104 ARG   A C   1 
ATOM   729  O O   . ARG   A 1 136 ? -32.202 7.876  -0.282  1.00 16.10 ? 104 ARG   A O   1 
ATOM   730  C CB  . ARG   A 1 136 ? -31.891 8.328  2.814   1.00 23.00 ? 104 ARG   A CB  1 
ATOM   731  C CG  . ARG   A 1 136 ? -32.118 8.927  4.195   1.00 30.90 ? 104 ARG   A CG  1 
ATOM   732  C CD  . ARG   A 1 136 ? -32.091 7.858  5.277   1.00 38.69 ? 104 ARG   A CD  1 
ATOM   733  N NE  . ARG   A 1 136 ? -30.976 6.927  5.122   1.00 45.54 ? 104 ARG   A NE  1 
ATOM   734  C CZ  . ARG   A 1 136 ? -29.802 7.051  5.736   1.00 50.56 ? 104 ARG   A CZ  1 
ATOM   735  N NH1 . ARG   A 1 136 ? -29.581 8.073  6.552   1.00 52.33 ? 104 ARG   A NH1 1 
ATOM   736  N NH2 . ARG   A 1 136 ? -28.849 6.152  5.534   1.00 52.22 ? 104 ARG   A NH2 1 
ATOM   737  N N   . TYR   A 1 137 ? -30.553 9.391  -0.057  1.00 13.55 ? 105 TYR   A N   1 
ATOM   738  C CA  . TYR   A 1 137 ? -29.929 9.109  -1.343  1.00 12.67 ? 105 TYR   A CA  1 
ATOM   739  C C   . TYR   A 1 137 ? -28.503 8.648  -1.124  1.00 12.90 ? 105 TYR   A C   1 
ATOM   740  O O   . TYR   A 1 137 ? -27.727 9.329  -0.446  1.00 14.21 ? 105 TYR   A O   1 
ATOM   741  C CB  . TYR   A 1 137 ? -29.893 10.372 -2.212  1.00 13.63 ? 105 TYR   A CB  1 
ATOM   742  C CG  . TYR   A 1 137 ? -31.271 10.859 -2.557  1.00 14.09 ? 105 TYR   A CG  1 
ATOM   743  C CD1 . TYR   A 1 137 ? -31.967 11.701 -1.693  1.00 14.17 ? 105 TYR   A CD1 1 
ATOM   744  C CD2 . TYR   A 1 137 ? -31.897 10.463 -3.731  1.00 15.45 ? 105 TYR   A CD2 1 
ATOM   745  C CE1 . TYR   A 1 137 ? -33.239 12.126 -1.989  1.00 14.75 ? 105 TYR   A CE1 1 
ATOM   746  C CE2 . TYR   A 1 137 ? -33.170 10.896 -4.039  1.00 15.56 ? 105 TYR   A CE2 1 
ATOM   747  C CZ  . TYR   A 1 137 ? -33.836 11.723 -3.162  1.00 14.64 ? 105 TYR   A CZ  1 
ATOM   748  O OH  . TYR   A 1 137 ? -35.112 12.146 -3.449  1.00 15.89 ? 105 TYR   A OH  1 
ATOM   749  N N   . THR   A 1 138 ? -28.156 7.511  -1.716  1.00 12.60 ? 106 THR   A N   1 
ATOM   750  C CA  . THR   A 1 138 ? -26.768 7.105  -1.890  1.00 13.23 ? 106 THR   A CA  1 
ATOM   751  C C   . THR   A 1 138 ? -26.469 7.132  -3.378  1.00 12.63 ? 106 THR   A C   1 
ATOM   752  O O   . THR   A 1 138 ? -27.168 6.491  -4.168  1.00 15.06 ? 106 THR   A O   1 
ATOM   753  C CB  . THR   A 1 138 ? -26.500 5.720  -1.312  1.00 16.02 ? 106 THR   A CB  1 
ATOM   754  O OG1 . THR   A 1 138 ? -26.677 5.765  0.106   1.00 19.25 ? 106 THR   A OG1 1 
ATOM   755  C CG2 . THR   A 1 138 ? -25.073 5.300  -1.623  1.00 18.41 ? 106 THR   A CG2 1 
ATOM   756  N N   . ILE   A 1 139 ? -25.450 7.890  -3.754  1.00 13.25 ? 107 ILE   A N   1 
ATOM   757  C CA  . ILE   A 1 139 ? -24.995 7.995  -5.131  1.00 13.78 ? 107 ILE   A CA  1 
ATOM   758  C C   . ILE   A 1 139 ? -23.686 7.233  -5.201  1.00 13.07 ? 107 ILE   A C   1 
ATOM   759  O O   . ILE   A 1 139 ? -22.760 7.517  -4.433  1.00 13.95 ? 107 ILE   A O   1 
ATOM   760  C CB  . ILE   A 1 139 ? -24.770 9.461  -5.527  1.00 16.21 ? 107 ILE   A CB  1 
ATOM   761  C CG1 . ILE   A 1 139 ? -26.018 10.301 -5.245  1.00 21.66 ? 107 ILE   A CG1 1 
ATOM   762  C CG2 . ILE   A 1 139 ? -24.319 9.556  -6.988  1.00 16.53 ? 107 ILE   A CG2 1 
ATOM   763  C CD1 . ILE   A 1 139 ? -27.226 9.849  -5.972  1.00 24.33 ? 107 ILE   A CD1 1 
ATOM   764  N N   . ALA   A 1 140 ? -23.610 6.249  -6.085  1.00 12.44 ? 108 ALA   A N   1 
ATOM   765  C CA  . ALA   A 1 140 ? -22.371 5.525  -6.306  1.00 13.19 ? 108 ALA   A CA  1 
ATOM   766  C C   . ALA   A 1 140 ? -21.815 5.884  -7.671  1.00 12.98 ? 108 ALA   A C   1 
ATOM   767  O O   . ALA   A 1 140 ? -22.553 5.976  -8.651  1.00 15.52 ? 108 ALA   A O   1 
ATOM   768  C CB  . ALA   A 1 140 ? -22.593 4.018  -6.231  1.00 14.97 ? 108 ALA   A CB  1 
ATOM   769  N N   . ALA   A 1 141 ? -20.515 6.097  -7.731  1.00 11.18 ? 109 ALA   A N   1 
ATOM   770  C CA  . ALA   A 1 141 ? -19.829 6.339  -8.989  1.00 11.96 ? 109 ALA   A CA  1 
ATOM   771  C C   . ALA   A 1 141 ? -18.711 5.322  -9.136  1.00 11.37 ? 109 ALA   A C   1 
ATOM   772  O O   . ALA   A 1 141 ? -17.884 5.167  -8.231  1.00 12.77 ? 109 ALA   A O   1 
ATOM   773  C CB  . ALA   A 1 141 ? -19.251 7.753  -9.039  1.00 14.04 ? 109 ALA   A CB  1 
ATOM   774  N N   . LEU   A 1 142 ? -18.699 4.623  -10.264 1.00 11.37 ? 110 LEU   A N   1 
ATOM   775  C CA  . LEU   A 1 142 ? -17.699 3.610  -10.574 1.00 12.13 ? 110 LEU   A CA  1 
ATOM   776  C C   . LEU   A 1 142 ? -16.829 4.158  -11.697 1.00 11.88 ? 110 LEU   A C   1 
ATOM   777  O O   . LEU   A 1 142 ? -17.329 4.408  -12.796 1.00 13.23 ? 110 LEU   A O   1 
ATOM   778  C CB  . LEU   A 1 142 ? -18.414 2.338  -11.019 1.00 15.55 ? 110 LEU   A CB  1 
ATOM   779  C CG  . LEU   A 1 142 ? -17.583 1.155  -11.461 1.00 19.89 ? 110 LEU   A CG  1 
ATOM   780  C CD1 . LEU   A 1 142 ? -16.705 0.736  -10.301 1.00 21.74 ? 110 LEU   A CD1 1 
ATOM   781  C CD2 . LEU   A 1 142 ? -18.523 0.050  -11.896 1.00 22.86 ? 110 LEU   A CD2 1 
ATOM   782  N N   . LEU   A 1 143 ? -15.545 4.367  -11.422 1.00 10.86 ? 111 LEU   A N   1 
ATOM   783  C CA  . LEU   A 1 143 ? -14.676 5.158  -12.286 1.00 10.61 ? 111 LEU   A CA  1 
ATOM   784  C C   . LEU   A 1 143 ? -13.650 4.325  -13.044 1.00 10.65 ? 111 LEU   A C   1 
ATOM   785  O O   . LEU   A 1 143 ? -12.916 3.533  -12.445 1.00 10.81 ? 111 LEU   A O   1 
ATOM   786  C CB  . LEU   A 1 143 ? -13.903 6.187  -11.472 1.00 11.75 ? 111 LEU   A CB  1 
ATOM   787  C CG  . LEU   A 1 143 ? -14.684 7.126  -10.574 1.00 11.55 ? 111 LEU   A CG  1 
ATOM   788  C CD1 . LEU   A 1 143 ? -13.704 8.159  -10.015 1.00 12.95 ? 111 LEU   A CD1 1 
ATOM   789  C CD2 . LEU   A 1 143 ? -15.833 7.792  -11.333 1.00 12.34 ? 111 LEU   A CD2 1 
ATOM   790  N N   . SER   A 1 144 ? -13.532 4.595  -14.339 1.00 10.67 ? 112 SER   A N   1 
ATOM   791  C CA  . SER   A 1 144 ? -12.421 4.177  -15.178 1.00 10.74 ? 112 SER   A CA  1 
ATOM   792  C C   . SER   A 1 144 ? -11.960 5.393  -15.966 1.00 10.96 ? 112 SER   A C   1 
ATOM   793  O O   . SER   A 1 144 ? -12.704 6.363  -16.103 1.00 11.04 ? 112 SER   A O   1 
ATOM   794  C CB  . SER   A 1 144 ? -12.848 3.068  -16.149 1.00 12.04 ? 112 SER   A CB  1 
ATOM   795  O OG  . SER   A 1 144 ? -13.336 1.951  -15.430 1.00 13.77 ? 112 SER   A OG  1 
ATOM   796  N N   . PRO   A 1 145 ? -10.740 5.378  -16.500 1.00 10.64 ? 113 PRO   A N   1 
ATOM   797  C CA  . PRO   A 1 145 ? -10.254 6.589  -17.175 1.00 11.19 ? 113 PRO   A CA  1 
ATOM   798  C C   . PRO   A 1 145 ? -11.117 7.056  -18.326 1.00 10.37 ? 113 PRO   A C   1 
ATOM   799  O O   . PRO   A 1 145 ? -11.223 8.272  -18.524 1.00 11.66 ? 113 PRO   A O   1 
ATOM   800  C CB  . PRO   A 1 145 ? -8.838  6.197  -17.612 1.00 12.03 ? 113 PRO   A CB  1 
ATOM   801  C CG  . PRO   A 1 145 ? -8.420  5.273  -16.520 1.00 12.59 ? 113 PRO   A CG  1 
ATOM   802  C CD  . PRO   A 1 145 ? -9.639  4.441  -16.236 1.00 12.69 ? 113 PRO   A CD  1 
ATOM   803  N N   . TYR   A 1 146 ? -11.740 6.149  -19.084 1.00 10.63 ? 114 TYR   A N   1 
ATOM   804  C CA  . TYR   A 1 146 ? -12.562 6.538  -20.226 1.00 11.40 ? 114 TYR   A CA  1 
ATOM   805  C C   . TYR   A 1 146 ? -14.031 6.161  -20.058 1.00 11.27 ? 114 TYR   A C   1 
ATOM   806  O O   . TYR   A 1 146 ? -14.777 6.143  -21.043 1.00 13.15 ? 114 TYR   A O   1 
ATOM   807  C CB  . TYR   A 1 146 ? -11.979 6.001  -21.538 1.00 12.40 ? 114 TYR   A CB  1 
ATOM   808  C CG  . TYR   A 1 146 ? -10.936 6.920  -22.129 1.00 13.80 ? 114 TYR   A CG  1 
ATOM   809  C CD1 . TYR   A 1 146 ? -9.716  7.113  -21.500 1.00 17.11 ? 114 TYR   A CD1 1 
ATOM   810  C CD2 . TYR   A 1 146 ? -11.187 7.632  -23.295 1.00 14.24 ? 114 TYR   A CD2 1 
ATOM   811  C CE1 . TYR   A 1 146 ? -8.768  7.970  -22.025 1.00 19.50 ? 114 TYR   A CE1 1 
ATOM   812  C CE2 . TYR   A 1 146 ? -10.242 8.480  -23.826 1.00 17.04 ? 114 TYR   A CE2 1 
ATOM   813  C CZ  . TYR   A 1 146 ? -9.041  8.653  -23.188 1.00 20.26 ? 114 TYR   A CZ  1 
ATOM   814  O OH  . TYR   A 1 146 ? -8.112  9.515  -23.731 1.00 24.30 ? 114 TYR   A OH  1 
ATOM   815  N N   . SER   A 1 147 ? -14.477 5.895  -18.830 1.00 11.02 ? 115 SER   A N   1 
ATOM   816  C CA  . SER   A 1 147 ? -15.844 5.439  -18.625 1.00 11.98 ? 115 SER   A CA  1 
ATOM   817  C C   . SER   A 1 147 ? -16.211 5.632  -17.167 1.00 11.96 ? 115 SER   A C   1 
ATOM   818  O O   . SER   A 1 147 ? -15.377 5.430  -16.287 1.00 13.58 ? 115 SER   A O   1 
ATOM   819  C CB  . SER   A 1 147 ? -15.953 3.947  -18.972 1.00 13.71 ? 115 SER   A CB  1 
ATOM   820  O OG  . SER   A 1 147 ? -17.285 3.488  -18.851 1.00 14.10 ? 115 SER   A OG  1 
ATOM   821  N N   . TYR   A 1 148 ? -17.463 5.998  -16.909 1.00 11.14 ? 116 TYR   A N   1 
ATOM   822  C CA  . TYR   A 1 148 ? -17.938 5.921  -15.539 1.00 12.08 ? 116 TYR   A CA  1 
ATOM   823  C C   . TYR   A 1 148 ? -19.400 5.531  -15.538 1.00 12.17 ? 116 TYR   A C   1 
ATOM   824  O O   . TYR   A 1 148 ? -20.125 5.745  -16.513 1.00 12.59 ? 116 TYR   A O   1 
ATOM   825  C CB  . TYR   A 1 148 ? -17.721 7.204  -14.736 1.00 14.26 ? 116 TYR   A CB  1 
ATOM   826  C CG  . TYR   A 1 148 ? -18.508 8.390  -15.217 1.00 14.27 ? 116 TYR   A CG  1 
ATOM   827  C CD1 . TYR   A 1 148 ? -19.785 8.642  -14.743 1.00 15.61 ? 116 TYR   A CD1 1 
ATOM   828  C CD2 . TYR   A 1 148 ? -17.954 9.286  -16.124 1.00 17.01 ? 116 TYR   A CD2 1 
ATOM   829  C CE1 . TYR   A 1 148 ? -20.498 9.740  -15.182 1.00 17.41 ? 116 TYR   A CE1 1 
ATOM   830  C CE2 . TYR   A 1 148 ? -18.648 10.380 -16.554 1.00 18.68 ? 116 TYR   A CE2 1 
ATOM   831  C CZ  . TYR   A 1 148 ? -19.921 10.609 -16.087 1.00 19.40 ? 116 TYR   A CZ  1 
ATOM   832  O OH  . TYR   A 1 148 ? -20.606 11.717 -16.525 1.00 23.47 ? 116 TYR   A OH  1 
ATOM   833  N N   . SER   A 1 149 ? -19.817 4.932  -14.438 1.00 12.97 ? 117 SER   A N   1 
ATOM   834  C CA  . SER   A 1 149 ? -21.224 4.684  -14.212 1.00 15.32 ? 117 SER   A CA  1 
ATOM   835  C C   . SER   A 1 149 ? -21.634 5.345  -12.909 1.00 13.92 ? 117 SER   A C   1 
ATOM   836  O O   . SER   A 1 149 ? -20.828 5.521  -11.984 1.00 14.11 ? 117 SER   A O   1 
ATOM   837  C CB  . SER   A 1 149 ? -21.558 3.199  -14.193 1.00 21.19 ? 117 SER   A CB  1 
ATOM   838  O OG  . SER   A 1 149 ? -21.259 2.644  -12.945 1.00 23.71 ? 117 SER   A OG  1 
ATOM   839  N N   . THR   A 1 150 ? -22.892 5.732  -12.852 1.00 14.37 ? 118 THR   A N   1 
ATOM   840  C CA  . THR   A 1 150 ? -23.415 6.321  -11.642 1.00 14.71 ? 118 THR   A CA  1 
ATOM   841  C C   . THR   A 1 150 ? -24.804 5.775  -11.392 1.00 14.07 ? 118 THR   A C   1 
ATOM   842  O O   . THR   A 1 150 ? -25.621 5.666  -12.311 1.00 16.48 ? 118 THR   A O   1 
ATOM   843  C CB  . THR   A 1 150 ? -23.392 7.843  -11.665 1.00 17.55 ? 118 THR   A CB  1 
ATOM   844  O OG1 . THR   A 1 150 ? -23.801 8.298  -10.384 1.00 20.20 ? 118 THR   A OG1 1 
ATOM   845  C CG2 . THR   A 1 150 ? -24.315 8.423  -12.741 1.00 17.49 ? 118 THR   A CG2 1 
ATOM   846  N N   . THR   A 1 151 ? -25.037 5.401  -10.142 1.00 13.10 ? 119 THR   A N   1 
ATOM   847  C CA  . THR   A 1 151 ? -26.257 4.729  -9.738  1.00 12.24 ? 119 THR   A CA  1 
ATOM   848  C C   . THR   A 1 151 ? -26.735 5.363  -8.449  1.00 12.83 ? 119 THR   A C   1 
ATOM   849  O O   . THR   A 1 151 ? -25.932 5.810  -7.627  1.00 14.23 ? 119 THR   A O   1 
ATOM   850  C CB  . THR   A 1 151 ? -25.972 3.257  -9.476  1.00 14.97 ? 119 THR   A CB  1 
ATOM   851  O OG1 . THR   A 1 151 ? -25.324 2.708  -10.625 1.00 16.30 ? 119 THR   A OG1 1 
ATOM   852  C CG2 . THR   A 1 151 ? -27.269 2.528  -9.209  1.00 17.87 ? 119 THR   A CG2 1 
ATOM   853  N N   . ALA   A 1 152 ? -28.044 5.412  -8.280  1.00 11.70 ? 120 ALA   A N   1 
ATOM   854  C CA  . ALA   A 1 152 ? -28.632 5.944  -7.063  1.00 12.36 ? 120 ALA   A CA  1 
ATOM   855  C C   . ALA   A 1 152 ? -29.445 4.865  -6.368  1.00 12.20 ? 120 ALA   A C   1 
ATOM   856  O O   . ALA   A 1 152 ? -30.189 4.113  -7.011  1.00 14.16 ? 120 ALA   A O   1 
ATOM   857  C CB  . ALA   A 1 152 ? -29.539 7.128  -7.367  1.00 14.29 ? 120 ALA   A CB  1 
ATOM   858  N N   . VAL   A 1 153 ? -29.283 4.787  -5.055  1.00 11.77 ? 121 VAL   A N   1 
ATOM   859  C CA  . VAL   A 1 153 ? -30.154 4.005  -4.189  1.00 13.89 ? 121 VAL   A CA  1 
ATOM   860  C C   . VAL   A 1 153 ? -30.940 5.002  -3.362  1.00 14.08 ? 121 VAL   A C   1 
ATOM   861  O O   . VAL   A 1 153 ? -30.350 5.808  -2.635  1.00 14.73 ? 121 VAL   A O   1 
ATOM   862  C CB  . VAL   A 1 153 ? -29.344 3.071  -3.283  1.00 16.45 ? 121 VAL   A CB  1 
ATOM   863  C CG1 . VAL   A 1 153 ? -30.279 2.259  -2.377  1.00 18.56 ? 121 VAL   A CG1 1 
ATOM   864  C CG2 . VAL   A 1 153 ? -28.468 2.152  -4.123  1.00 19.55 ? 121 VAL   A CG2 1 
ATOM   865  N N   . VAL   A 1 154 ? -32.264 4.971  -3.493  1.00 14.35 ? 122 VAL   A N   1 
ATOM   866  C CA  . VAL   A 1 154 ? -33.147 5.944  -2.853  1.00 15.60 ? 122 VAL   A CA  1 
ATOM   867  C C   . VAL   A 1 154 ? -34.027 5.188  -1.876  1.00 17.15 ? 122 VAL   A C   1 
ATOM   868  O O   . VAL   A 1 154 ? -34.726 4.249  -2.269  1.00 18.54 ? 122 VAL   A O   1 
ATOM   869  C CB  . VAL   A 1 154 ? -33.999 6.709  -3.881  1.00 17.38 ? 122 VAL   A CB  1 
ATOM   870  C CG1 . VAL   A 1 154 ? -34.878 7.754  -3.192  1.00 18.84 ? 122 VAL   A CG1 1 
ATOM   871  C CG2 . VAL   A 1 154 ? -33.106 7.368  -4.930  1.00 19.04 ? 122 VAL   A CG2 1 
ATOM   872  N N   . THR   A 1 155 ? -34.015 5.604  -0.610  1.00 18.14 ? 123 THR   A N   1 
ATOM   873  C CA  . THR   A 1 155 ? -34.772 4.906  0.417   1.00 22.49 ? 123 THR   A CA  1 
ATOM   874  C C   . THR   A 1 155 ? -35.670 5.871  1.173   1.00 23.09 ? 123 THR   A C   1 
ATOM   875  O O   . THR   A 1 155 ? -35.402 7.072  1.258   1.00 22.28 ? 123 THR   A O   1 
ATOM   876  C CB  . THR   A 1 155 ? -33.881 4.131  1.403   1.00 27.74 ? 123 THR   A CB  1 
ATOM   877  O OG1 . THR   A 1 155 ? -34.703 3.513  2.400   1.00 31.40 ? 123 THR   A OG1 1 
ATOM   878  C CG2 . THR   A 1 155 ? -32.910 5.044  2.088   1.00 28.58 ? 123 THR   A CG2 1 
ATOM   879  N N   . ASN   A 1 156 ? -36.751 5.321  1.715   1.00 26.48 ? 124 ASN   A N   1 
ATOM   880  C CA  . ASN   A 1 156 ? -37.715 6.098  2.469   1.00 30.92 ? 124 ASN   A CA  1 
ATOM   881  C C   . ASN   A 1 156 ? -37.478 5.827  3.946   1.00 35.39 ? 124 ASN   A C   1 
ATOM   882  O O   . ASN   A 1 156 ? -37.703 4.694  4.398   1.00 36.65 ? 124 ASN   A O   1 
ATOM   883  C CB  . ASN   A 1 156 ? -39.129 5.686  2.073   1.00 32.64 ? 124 ASN   A CB  1 
ATOM   884  C CG  . ASN   A 1 156 ? -40.163 6.722  2.451   1.00 33.93 ? 124 ASN   A CG  1 
ATOM   885  O OD1 . ASN   A 1 156 ? -39.988 7.469  3.411   1.00 33.91 ? 124 ASN   A OD1 1 
ATOM   886  N ND2 . ASN   A 1 156 ? -41.251 6.774  1.691   1.00 35.34 ? 124 ASN   A ND2 1 
ATOM   887  N N   . PRO   A 1 157 ? -37.029 6.819  4.735   1.00 38.57 ? 125 PRO   A N   1 
ATOM   888  C CA  . PRO   A 1 157 ? -36.644 6.671  6.146   1.00 41.08 ? 125 PRO   A CA  1 
ATOM   889  C C   . PRO   A 1 157 ? -37.781 6.199  7.048   1.00 42.63 ? 125 PRO   A C   1 
ATOM   890  O O   . PRO   A 1 157 ? -38.933 6.177  6.615   1.00 43.85 ? 125 PRO   A O   1 
ATOM   891  C CB  . PRO   A 1 157 ? -36.217 8.089  6.539   1.00 40.96 ? 125 PRO   A CB  1 
ATOM   892  C CG  . PRO   A 1 157 ? -36.937 8.977  5.586   1.00 40.37 ? 125 PRO   A CG  1 
ATOM   893  C CD  . PRO   A 1 157 ? -36.949 8.222  4.295   1.00 39.08 ? 125 PRO   A CD  1 
ATOM   894  N N   . CYS   B 1 42  ? -16.795 11.611 -39.385 1.00 43.57 ? 10  CYS   B N   1 
ATOM   895  C CA  . CYS   B 1 42  ? -17.699 11.705 -38.245 1.00 42.36 ? 10  CYS   B CA  1 
ATOM   896  C C   . CYS   B 1 42  ? -16.916 12.009 -36.967 1.00 35.23 ? 10  CYS   B C   1 
ATOM   897  O O   . CYS   B 1 42  ? -16.614 11.108 -36.185 1.00 35.14 ? 10  CYS   B O   1 
ATOM   898  C CB  . CYS   B 1 42  ? -18.501 10.411 -38.094 1.00 47.27 ? 10  CYS   B CB  1 
ATOM   899  S SG  . CYS   B 1 42  ? -20.210 10.637 -37.531 1.00 50.86 ? 10  CYS   B SG  1 
ATOM   900  N N   . PRO   B 1 43  ? -16.597 13.288 -36.756 1.00 28.12 ? 11  PRO   B N   1 
ATOM   901  C CA  . PRO   B 1 43  ? -15.762 13.659 -35.599 1.00 23.59 ? 11  PRO   B CA  1 
ATOM   902  C C   . PRO   B 1 43  ? -16.398 13.386 -34.242 1.00 19.73 ? 11  PRO   B C   1 
ATOM   903  O O   . PRO   B 1 43  ? -15.675 13.134 -33.267 1.00 19.01 ? 11  PRO   B O   1 
ATOM   904  C CB  . PRO   B 1 43  ? -15.508 15.159 -35.815 1.00 26.88 ? 11  PRO   B CB  1 
ATOM   905  C CG  . PRO   B 1 43  ? -16.567 15.602 -36.767 1.00 29.41 ? 11  PRO   B CG  1 
ATOM   906  C CD  . PRO   B 1 43  ? -16.883 14.433 -37.634 1.00 29.25 ? 11  PRO   B CD  1 
ATOM   907  N N   . LEU   B 1 44  ? -17.720 13.447 -34.134 1.00 16.19 ? 12  LEU   B N   1 
ATOM   908  C CA  . LEU   B 1 44  ? -18.397 13.234 -32.860 1.00 15.78 ? 12  LEU   B CA  1 
ATOM   909  C C   . LEU   B 1 44  ? -19.690 12.486 -33.127 1.00 15.04 ? 12  LEU   B C   1 
ATOM   910  O O   . LEU   B 1 44  ? -20.536 12.965 -33.890 1.00 17.30 ? 12  LEU   B O   1 
ATOM   911  C CB  . LEU   B 1 44  ? -18.697 14.575 -32.178 1.00 17.39 ? 12  LEU   B CB  1 
ATOM   912  C CG  . LEU   B 1 44  ? -19.435 14.531 -30.838 1.00 17.89 ? 12  LEU   B CG  1 
ATOM   913  C CD1 . LEU   B 1 44  ? -18.626 13.751 -29.808 1.00 17.32 ? 12  LEU   B CD1 1 
ATOM   914  C CD2 . LEU   B 1 44  ? -19.711 15.938 -30.336 1.00 20.00 ? 12  LEU   B CD2 1 
ATOM   915  N N   . MET   B 1 45  ? -19.839 11.321 -32.508 1.00 13.82 ? 13  MET   B N   1 
ATOM   916  C CA  . MET   B 1 45  ? -21.046 10.514 -32.619 1.00 13.08 ? 13  MET   B CA  1 
ATOM   917  C C   . MET   B 1 45  ? -21.448 10.088 -31.219 1.00 11.73 ? 13  MET   B C   1 
ATOM   918  O O   . MET   B 1 45  ? -20.580 9.822  -30.381 1.00 12.71 ? 13  MET   B O   1 
ATOM   919  C CB  . MET   B 1 45  ? -20.806 9.268  -33.493 1.00 16.35 ? 13  MET   B CB  1 
ATOM   920  C CG  . MET   B 1 45  ? -22.067 8.446  -33.800 1.00 19.11 ? 13  MET   B CG  1 
ATOM   921  S SD  . MET   B 1 45  ? -22.428 7.161  -32.582 1.00 20.76 ? 13  MET   B SD  1 
ATOM   922  C CE  . MET   B 1 45  ? -21.481 5.783  -33.216 1.00 22.55 ? 13  MET   B CE  1 
ATOM   923  N N   . VAL   B 1 46  ? -22.753 10.041 -30.959 1.00 12.11 ? 14  VAL   B N   1 
ATOM   924  C CA  . VAL   B 1 46  ? -23.271 9.608  -29.666 1.00 11.87 ? 14  VAL   B CA  1 
ATOM   925  C C   . VAL   B 1 46  ? -24.196 8.433  -29.904 1.00 12.11 ? 14  VAL   B C   1 
ATOM   926  O O   . VAL   B 1 46  ? -25.053 8.489  -30.791 1.00 14.00 ? 14  VAL   B O   1 
ATOM   927  C CB  . VAL   B 1 46  ? -24.022 10.735 -28.934 1.00 12.78 ? 14  VAL   B CB  1 
ATOM   928  C CG1 . VAL   B 1 46  ? -24.518 10.246 -27.565 1.00 13.39 ? 14  VAL   B CG1 1 
ATOM   929  C CG2 . VAL   B 1 46  ? -23.135 11.962 -28.792 1.00 13.93 ? 14  VAL   B CG2 1 
ATOM   930  N N   . LYS   B 1 47  ? -24.013 7.372  -29.127 1.00 11.43 ? 15  LYS   B N   1 
ATOM   931  C CA  . LYS   B 1 47  ? -24.833 6.173  -29.227 1.00 11.71 ? 15  LYS   B CA  1 
ATOM   932  C C   . LYS   B 1 47  ? -25.463 5.918  -27.869 1.00 11.17 ? 15  LYS   B C   1 
ATOM   933  O O   . LYS   B 1 47  ? -24.769 5.968  -26.849 1.00 13.10 ? 15  LYS   B O   1 
ATOM   934  C CB  . LYS   B 1 47  ? -23.985 4.970  -29.639 1.00 14.43 ? 15  LYS   B CB  1 
ATOM   935  C CG  . LYS   B 1 47  ? -24.799 3.708  -29.846 1.00 16.74 ? 15  LYS   B CG  1 
ATOM   936  C CD  . LYS   B 1 47  ? -23.995 2.627  -30.550 1.00 20.24 ? 15  LYS   B CD  1 
ATOM   937  C CE  . LYS   B 1 47  ? -24.869 1.451  -30.935 1.00 23.64 ? 15  LYS   B CE  1 
ATOM   938  N NZ  . LYS   B 1 47  ? -24.093 0.491  -31.757 1.00 26.31 ? 15  LYS   B NZ  1 
ATOM   939  N N   . VAL   B 1 48  ? -26.769 5.657  -27.849 1.00 11.77 ? 16  VAL   B N   1 
ATOM   940  C CA  . VAL   B 1 48  ? -27.513 5.504  -26.604 1.00 11.29 ? 16  VAL   B CA  1 
ATOM   941  C C   . VAL   B 1 48  ? -28.261 4.178  -26.640 1.00 12.16 ? 16  VAL   B C   1 
ATOM   942  O O   . VAL   B 1 48  ? -28.965 3.880  -27.614 1.00 12.95 ? 16  VAL   B O   1 
ATOM   943  C CB  . VAL   B 1 48  ? -28.483 6.683  -26.368 1.00 12.24 ? 16  VAL   B CB  1 
ATOM   944  C CG1 . VAL   B 1 48  ? -29.087 6.598  -24.982 1.00 13.29 ? 16  VAL   B CG1 1 
ATOM   945  C CG2 . VAL   B 1 48  ? -27.770 8.024  -26.577 1.00 13.08 ? 16  VAL   B CG2 1 
ATOM   946  N N   . LEU   B 1 49  ? -28.110 3.387  -25.578 1.00 11.64 ? 17  LEU   B N   1 
ATOM   947  C CA  . LEU   B 1 49  ? -28.728 2.075  -25.457 1.00 11.49 ? 17  LEU   B CA  1 
ATOM   948  C C   . LEU   B 1 49  ? -29.623 2.028  -24.227 1.00 10.98 ? 17  LEU   B C   1 
ATOM   949  O O   . LEU   B 1 49  ? -29.356 2.681  -23.213 1.00 11.37 ? 17  LEU   B O   1 
ATOM   950  C CB  . LEU   B 1 49  ? -27.686 0.968  -25.326 1.00 14.21 ? 17  LEU   B CB  1 
ATOM   951  C CG  . LEU   B 1 49  ? -26.718 0.773  -26.486 1.00 16.43 ? 17  LEU   B CG  1 
ATOM   952  C CD1 . LEU   B 1 49  ? -25.895 -0.447 -26.181 1.00 19.70 ? 17  LEU   B CD1 1 
ATOM   953  C CD2 . LEU   B 1 49  ? -27.449 0.616  -27.818 1.00 17.91 ? 17  LEU   B CD2 1 
ATOM   954  N N   . ASP   B 1 50  ? -30.687 1.235  -24.332 1.00 11.58 ? 18  ASP   B N   1 
ATOM   955  C CA  . ASP   B 1 50  ? -31.661 1.034  -23.269 1.00 11.87 ? 18  ASP   B CA  1 
ATOM   956  C C   . ASP   B 1 50  ? -31.365 -0.315 -22.618 1.00 11.74 ? 18  ASP   B C   1 
ATOM   957  O O   . ASP   B 1 50  ? -31.568 -1.369 -23.231 1.00 12.17 ? 18  ASP   B O   1 
ATOM   958  C CB  . ASP   B 1 50  ? -33.054 1.081  -23.896 1.00 12.00 ? 18  ASP   B CB  1 
ATOM   959  C CG  . ASP   B 1 50  ? -34.172 0.859  -22.907 1.00 13.45 ? 18  ASP   B CG  1 
ATOM   960  O OD1 . ASP   B 1 50  ? -33.992 0.159  -21.891 1.00 13.20 ? 18  ASP   B OD1 1 
ATOM   961  O OD2 . ASP   B 1 50  ? -35.269 1.378  -23.180 1.00 15.70 ? 18  ASP   B OD2 1 
ATOM   962  N N   . ALA   B 1 51  ? -30.877 -0.270 -21.381 1.00 12.38 ? 19  ALA   B N   1 
ATOM   963  C CA  . ALA   B 1 51  ? -30.465 -1.461 -20.649 1.00 13.57 ? 19  ALA   B CA  1 
ATOM   964  C C   . ALA   B 1 51  ? -31.631 -2.205 -20.013 1.00 14.58 ? 19  ALA   B C   1 
ATOM   965  O O   . ALA   B 1 51  ? -31.429 -3.304 -19.481 1.00 17.27 ? 19  ALA   B O   1 
ATOM   966  C CB  . ALA   B 1 51  ? -29.460 -1.082 -19.563 1.00 14.59 ? 19  ALA   B CB  1 
ATOM   967  N N   . VAL   B 1 52  ? -32.823 -1.614 -20.018 1.00 15.22 ? 20  VAL   B N   1 
ATOM   968  C CA  . VAL   B 1 52  ? -34.014 -2.284 -19.509 1.00 17.01 ? 20  VAL   B CA  1 
ATOM   969  C C   . VAL   B 1 52  ? -34.629 -3.166 -20.578 1.00 17.07 ? 20  VAL   B C   1 
ATOM   970  O O   . VAL   B 1 52  ? -34.987 -4.317 -20.322 1.00 19.67 ? 20  VAL   B O   1 
ATOM   971  C CB  . VAL   B 1 52  ? -35.026 -1.239 -19.005 1.00 18.31 ? 20  VAL   B CB  1 
ATOM   972  C CG1 . VAL   B 1 52  ? -36.336 -1.920 -18.631 1.00 19.69 ? 20  VAL   B CG1 1 
ATOM   973  C CG2 . VAL   B 1 52  ? -34.463 -0.502 -17.828 1.00 19.36 ? 20  VAL   B CG2 1 
ATOM   974  N N   . ARG   B 1 53  ? -34.744 -2.641 -21.791 1.00 15.10 ? 21  ARG   B N   1 
ATOM   975  C CA  . ARG   B 1 53  ? -35.422 -3.330 -22.871 1.00 15.11 ? 21  ARG   B CA  1 
ATOM   976  C C   . ARG   B 1 53  ? -34.472 -4.044 -23.816 1.00 14.17 ? 21  ARG   B C   1 
ATOM   977  O O   . ARG   B 1 53  ? -34.927 -4.865 -24.614 1.00 16.67 ? 21  ARG   B O   1 
ATOM   978  C CB  . ARG   B 1 53  ? -36.296 -2.339 -23.634 1.00 17.05 ? 21  ARG   B CB  1 
ATOM   979  C CG  . ARG   B 1 53  ? -37.337 -1.683 -22.734 1.00 20.56 ? 21  ARG   B CG  1 
ATOM   980  C CD  . ARG   B 1 53  ? -38.372 -0.931 -23.526 1.00 23.19 ? 21  ARG   B CD  1 
ATOM   981  N NE  . ARG   B 1 53  ? -37.815 0.234  -24.201 1.00 25.23 ? 21  ARG   B NE  1 
ATOM   982  C CZ  . ARG   B 1 53  ? -38.453 0.911  -25.151 1.00 27.02 ? 21  ARG   B CZ  1 
ATOM   983  N NH1 . ARG   B 1 53  ? -39.661 0.526  -25.538 1.00 27.81 ? 21  ARG   B NH1 1 
ATOM   984  N NH2 . ARG   B 1 53  ? -37.882 1.961  -25.722 1.00 28.20 ? 21  ARG   B NH2 1 
ATOM   985  N N   . GLY   B 1 54  ? -33.175 -3.768 -23.738 1.00 13.32 ? 22  GLY   B N   1 
ATOM   986  C CA  . GLY   B 1 54  ? -32.221 -4.433 -24.604 1.00 13.29 ? 22  GLY   B CA  1 
ATOM   987  C C   . GLY   B 1 54  ? -32.350 -3.964 -26.035 1.00 12.67 ? 22  GLY   B C   1 
ATOM   988  O O   . GLY   B 1 54  ? -32.438 -4.767 -26.966 1.00 13.23 ? 22  GLY   B O   1 
ATOM   989  N N   . SER   B 1 55  ? -32.327 -2.653 -26.226 1.00 13.36 ? 23  SER   B N   1 
ATOM   990  C CA  . SER   B 1 55  ? -32.587 -2.076 -27.534 1.00 13.50 ? 23  SER   B CA  1 
ATOM   991  C C   . SER   B 1 55  ? -31.813 -0.781 -27.644 1.00 13.06 ? 23  SER   B C   1 
ATOM   992  O O   . SER   B 1 55  ? -31.435 -0.190 -26.625 1.00 14.10 ? 23  SER   B O   1 
ATOM   993  C CB  . SER   B 1 55  ? -34.074 -1.749 -27.678 1.00 17.34 ? 23  SER   B CB  1 
ATOM   994  O OG  . SER   B 1 55  ? -34.432 -0.746 -26.756 1.00 20.87 ? 23  SER   B OG  1 
ATOM   995  N N   . PRO   B 1 56  ? -31.605 -0.277 -28.860 1.00 13.17 ? 24  PRO   B N   1 
ATOM   996  C CA  . PRO   B 1 56  ? -31.197 1.121  -28.998 1.00 12.81 ? 24  PRO   B CA  1 
ATOM   997  C C   . PRO   B 1 56  ? -32.236 2.015  -28.346 1.00 12.91 ? 24  PRO   B C   1 
ATOM   998  O O   . PRO   B 1 56  ? -33.425 1.689  -28.295 1.00 14.90 ? 24  PRO   B O   1 
ATOM   999  C CB  . PRO   B 1 56  ? -31.159 1.334  -30.517 1.00 14.07 ? 24  PRO   B CB  1 
ATOM   1000 C CG  . PRO   B 1 56  ? -32.013 0.276  -31.081 1.00 18.37 ? 24  PRO   B CG  1 
ATOM   1001 C CD  . PRO   B 1 56  ? -31.902 -0.895 -30.163 1.00 14.49 ? 24  PRO   B CD  1 
ATOM   1002 N N   . ALA   B 1 57  ? -31.768 3.136  -27.809 1.00 12.57 ? 25  ALA   B N   1 
ATOM   1003 C CA  . ALA   B 1 57  ? -32.660 4.148  -27.256 1.00 12.58 ? 25  ALA   B CA  1 
ATOM   1004 C C   . ALA   B 1 57  ? -32.918 5.155  -28.365 1.00 12.50 ? 25  ALA   B C   1 
ATOM   1005 O O   . ALA   B 1 57  ? -32.024 5.923  -28.731 1.00 13.26 ? 25  ALA   B O   1 
ATOM   1006 C CB  . ALA   B 1 57  ? -32.033 4.805  -26.031 1.00 13.10 ? 25  ALA   B CB  1 
ATOM   1007 N N   . ILE   B 1 58  ? -34.134 5.139  -28.902 1.00 13.38 ? 26  ILE   B N   1 
ATOM   1008 C CA  . ILE   B 1 58  ? -34.496 5.877  -30.107 1.00 14.65 ? 26  ILE   B CA  1 
ATOM   1009 C C   . ILE   B 1 58  ? -35.145 7.198  -29.721 1.00 15.27 ? 26  ILE   B C   1 
ATOM   1010 O O   . ILE   B 1 58  ? -35.833 7.307  -28.700 1.00 16.72 ? 26  ILE   B O   1 
ATOM   1011 C CB  . ILE   B 1 58  ? -35.432 5.015  -30.983 1.00 18.06 ? 26  ILE   B CB  1 
ATOM   1012 C CG1 . ILE   B 1 58  ? -34.758 3.679  -31.317 1.00 20.21 ? 26  ILE   B CG1 1 
ATOM   1013 C CG2 . ILE   B 1 58  ? -35.842 5.745  -32.250 1.00 20.94 ? 26  ILE   B CG2 1 
ATOM   1014 C CD1 . ILE   B 1 58  ? -35.723 2.618  -31.835 1.00 24.07 ? 26  ILE   B CD1 1 
ATOM   1015 N N   . ASN   B 1 59  ? -34.899 8.227  -30.533 1.00 15.58 ? 27  ASN   B N   1 
ATOM   1016 C CA  . ASN   B 1 59  ? -35.529 9.535  -30.341 1.00 16.74 ? 27  ASN   B CA  1 
ATOM   1017 C C   . ASN   B 1 59  ? -35.098 10.198 -29.041 1.00 15.71 ? 27  ASN   B C   1 
ATOM   1018 O O   . ASN   B 1 59  ? -35.861 10.951 -28.433 1.00 16.87 ? 27  ASN   B O   1 
ATOM   1019 C CB  . ASN   B 1 59  ? -37.056 9.462  -30.420 1.00 20.45 ? 27  ASN   B CB  1 
ATOM   1020 C CG  . ASN   B 1 59  ? -37.541 9.067  -31.783 1.00 26.11 ? 27  ASN   B CG  1 
ATOM   1021 O OD1 . ASN   B 1 59  ? -36.970 9.476  -32.795 1.00 28.52 ? 27  ASN   B OD1 1 
ATOM   1022 N ND2 . ASN   B 1 59  ? -38.597 8.260  -31.827 1.00 28.24 ? 27  ASN   B ND2 1 
ATOM   1023 N N   . VAL   B 1 60  ? -33.886 9.910  -28.593 1.00 13.26 ? 28  VAL   B N   1 
ATOM   1024 C CA  . VAL   B 1 60  ? -33.335 10.554 -27.408 1.00 13.31 ? 28  VAL   B CA  1 
ATOM   1025 C C   . VAL   B 1 60  ? -32.714 11.878 -27.830 1.00 12.43 ? 28  VAL   B C   1 
ATOM   1026 O O   . VAL   B 1 60  ? -31.795 11.909 -28.656 1.00 13.04 ? 28  VAL   B O   1 
ATOM   1027 C CB  . VAL   B 1 60  ? -32.298 9.658  -26.721 1.00 14.03 ? 28  VAL   B CB  1 
ATOM   1028 C CG1 . VAL   B 1 60  ? -31.727 10.361 -25.513 1.00 15.78 ? 28  VAL   B CG1 1 
ATOM   1029 C CG2 . VAL   B 1 60  ? -32.930 8.333  -26.299 1.00 14.88 ? 28  VAL   B CG2 1 
ATOM   1030 N N   . ALA   B 1 61  ? -33.209 12.966 -27.257 1.00 12.85 ? 29  ALA   B N   1 
ATOM   1031 C CA  . ALA   B 1 61  ? -32.735 14.298 -27.584 1.00 12.60 ? 29  ALA   B CA  1 
ATOM   1032 C C   . ALA   B 1 61  ? -31.500 14.644 -26.760 1.00 11.58 ? 29  ALA   B C   1 
ATOM   1033 O O   . ALA   B 1 61  ? -31.367 14.248 -25.597 1.00 12.79 ? 29  ALA   B O   1 
ATOM   1034 C CB  . ALA   B 1 61  ? -33.829 15.314 -27.271 1.00 13.07 ? 29  ALA   B CB  1 
ATOM   1035 N N   . MET   B 1 62  ? -30.595 15.412 -27.362 1.00 11.83 ? 30  MET   B N   1 
ATOM   1036 C CA  . MET   B 1 62  ? -29.441 15.907 -26.630 1.00 11.89 ? 30  MET   B CA  1 
ATOM   1037 C C   . MET   B 1 62  ? -28.983 17.222 -27.242 1.00 12.13 ? 30  MET   B C   1 
ATOM   1038 O O   . MET   B 1 62  ? -29.171 17.471 -28.438 1.00 12.18 ? 30  MET   B O   1 
ATOM   1039 C CB  . MET   B 1 62  ? -28.288 14.894 -26.613 1.00 12.78 ? 30  MET   B CB  1 
ATOM   1040 C CG  . MET   B 1 62  ? -27.646 14.629 -27.975 1.00 12.37 ? 30  MET   B CG  1 
ATOM   1041 S SD  . MET   B 1 62  ? -26.628 13.141 -27.981 1.00 12.91 ? 30  MET   B SD  1 
ATOM   1042 C CE  . MET   B 1 62  ? -27.895 11.875 -28.121 1.00 14.00 ? 30  MET   B CE  1 
ATOM   1043 N N   . HIS   B 1 63  ? -28.363 18.051 -26.406 1.00 12.25 ? 31  HIS   B N   1 
ATOM   1044 C CA  . HIS   B 1 63  ? -27.679 19.253 -26.846 1.00 12.84 ? 31  HIS   B CA  1 
ATOM   1045 C C   . HIS   B 1 63  ? -26.206 19.138 -26.478 1.00 12.95 ? 31  HIS   B C   1 
ATOM   1046 O O   . HIS   B 1 63  ? -25.853 18.534 -25.462 1.00 13.89 ? 31  HIS   B O   1 
ATOM   1047 C CB  . HIS   B 1 63  ? -28.241 20.516 -26.170 1.00 15.37 ? 31  HIS   B CB  1 
ATOM   1048 C CG  . HIS   B 1 63  ? -29.605 20.913 -26.645 1.00 17.12 ? 31  HIS   B CG  1 
ATOM   1049 N ND1 . HIS   B 1 63  ? -29.848 21.379 -27.918 1.00 20.45 ? 31  HIS   B ND1 1 
ATOM   1050 C CD2 . HIS   B 1 63  ? -30.795 20.948 -26.001 1.00 19.31 ? 31  HIS   B CD2 1 
ATOM   1051 C CE1 . HIS   B 1 63  ? -31.132 21.664 -28.045 1.00 20.79 ? 31  HIS   B CE1 1 
ATOM   1052 N NE2 . HIS   B 1 63  ? -31.729 21.410 -26.896 1.00 20.25 ? 31  HIS   B NE2 1 
ATOM   1053 N N   . VAL   B 1 64  ? -25.349 19.712 -27.318 1.00 12.65 ? 32  VAL   B N   1 
ATOM   1054 C CA  . VAL   B 1 64  ? -23.917 19.789 -27.071 1.00 12.97 ? 32  VAL   B CA  1 
ATOM   1055 C C   . VAL   B 1 64  ? -23.558 21.254 -26.891 1.00 12.81 ? 32  VAL   B C   1 
ATOM   1056 O O   . VAL   B 1 64  ? -24.011 22.108 -27.665 1.00 13.92 ? 32  VAL   B O   1 
ATOM   1057 C CB  . VAL   B 1 64  ? -23.110 19.161 -28.222 1.00 12.97 ? 32  VAL   B CB  1 
ATOM   1058 C CG1 . VAL   B 1 64  ? -21.614 19.131 -27.887 1.00 14.07 ? 32  VAL   B CG1 1 
ATOM   1059 C CG2 . VAL   B 1 64  ? -23.621 17.759 -28.517 1.00 14.58 ? 32  VAL   B CG2 1 
ATOM   1060 N N   . PHE   B 1 65  ? -22.753 21.540 -25.875 1.00 13.12 ? 33  PHE   B N   1 
ATOM   1061 C CA  . PHE   B 1 65  ? -22.288 22.885 -25.592 1.00 13.99 ? 33  PHE   B CA  1 
ATOM   1062 C C   . PHE   B 1 65  ? -20.768 22.885 -25.550 1.00 13.47 ? 33  PHE   B C   1 
ATOM   1063 O O   . PHE   B 1 65  ? -20.128 21.847 -25.351 1.00 13.51 ? 33  PHE   B O   1 
ATOM   1064 C CB  . PHE   B 1 65  ? -22.817 23.370 -24.238 1.00 15.36 ? 33  PHE   B CB  1 
ATOM   1065 C CG  . PHE   B 1 65  ? -24.317 23.333 -24.122 1.00 15.58 ? 33  PHE   B CG  1 
ATOM   1066 C CD1 . PHE   B 1 65  ? -24.962 22.171 -23.726 1.00 17.55 ? 33  PHE   B CD1 1 
ATOM   1067 C CD2 . PHE   B 1 65  ? -25.082 24.467 -24.385 1.00 16.16 ? 33  PHE   B CD2 1 
ATOM   1068 C CE1 . PHE   B 1 65  ? -26.342 22.129 -23.606 1.00 18.27 ? 33  PHE   B CE1 1 
ATOM   1069 C CE2 . PHE   B 1 65  ? -26.465 24.429 -24.268 1.00 17.90 ? 33  PHE   B CE2 1 
ATOM   1070 C CZ  . PHE   B 1 65  ? -27.095 23.267 -23.882 1.00 18.62 ? 33  PHE   B CZ  1 
ATOM   1071 N N   . ARG   B 1 66  ? -20.197 24.071 -25.736 1.00 14.33 ? 34  ARG   B N   1 
ATOM   1072 C CA  . ARG   B 1 66  ? -18.761 24.272 -25.636 1.00 15.79 ? 34  ARG   B CA  1 
ATOM   1073 C C   . ARG   B 1 66  ? -18.514 25.390 -24.636 1.00 16.69 ? 34  ARG   B C   1 
ATOM   1074 O O   . ARG   B 1 66  ? -19.170 26.436 -24.693 1.00 17.75 ? 34  ARG   B O   1 
ATOM   1075 C CB  . ARG   B 1 66  ? -18.161 24.630 -26.996 1.00 17.09 ? 34  ARG   B CB  1 
ATOM   1076 C CG  . ARG   B 1 66  ? -16.662 24.803 -26.968 1.00 20.83 ? 34  ARG   B CG  1 
ATOM   1077 C CD  . ARG   B 1 66  ? -16.117 25.171 -28.333 1.00 25.75 ? 34  ARG   B CD  1 
ATOM   1078 N NE  . ARG   B 1 66  ? -14.660 25.272 -28.314 1.00 30.80 ? 34  ARG   B NE  1 
ATOM   1079 C CZ  . ARG   B 1 66  ? -13.982 26.266 -27.747 1.00 34.23 ? 34  ARG   B CZ  1 
ATOM   1080 N NH1 . ARG   B 1 66  ? -14.624 27.256 -27.140 1.00 35.75 ? 34  ARG   B NH1 1 
ATOM   1081 N NH2 . ARG   B 1 66  ? -12.658 26.267 -27.779 1.00 35.52 ? 34  ARG   B NH2 1 
ATOM   1082 N N   . LYS   B 1 67  ? -17.580 25.169 -23.716 1.00 17.55 ? 35  LYS   B N   1 
ATOM   1083 C CA  . LYS   B 1 67  ? -17.346 26.139 -22.656 1.00 18.42 ? 35  LYS   B CA  1 
ATOM   1084 C C   . LYS   B 1 67  ? -16.694 27.395 -23.223 1.00 19.21 ? 35  LYS   B C   1 
ATOM   1085 O O   . LYS   B 1 67  ? -15.710 27.316 -23.967 1.00 19.33 ? 35  LYS   B O   1 
ATOM   1086 C CB  . LYS   B 1 67  ? -16.470 25.529 -21.565 1.00 21.74 ? 35  LYS   B CB  1 
ATOM   1087 C CG  . LYS   B 1 67  ? -16.566 26.264 -20.235 1.00 26.35 ? 35  LYS   B CG  1 
ATOM   1088 C CD  . LYS   B 1 67  ? -15.939 25.459 -19.102 1.00 30.75 ? 35  LYS   B CD  1 
ATOM   1089 C CE  . LYS   B 1 67  ? -16.245 26.089 -17.752 1.00 34.23 ? 35  LYS   B CE  1 
ATOM   1090 N NZ  . LYS   B 1 67  ? -15.749 25.256 -16.624 1.00 36.73 ? 35  LYS   B NZ  1 
ATOM   1091 N N   . ALA   B 1 68  ? -17.261 28.553 -22.890 1.00 21.11 ? 36  ALA   B N   1 
ATOM   1092 C CA  . ALA   B 1 68  ? -16.731 29.841 -23.312 1.00 23.94 ? 36  ALA   B CA  1 
ATOM   1093 C C   . ALA   B 1 68  ? -15.661 30.337 -22.343 1.00 26.89 ? 36  ALA   B C   1 
ATOM   1094 O O   . ALA   B 1 68  ? -15.489 29.817 -21.239 1.00 26.42 ? 36  ALA   B O   1 
ATOM   1095 C CB  . ALA   B 1 68  ? -17.849 30.878 -23.409 1.00 25.24 ? 36  ALA   B CB  1 
ATOM   1096 N N   . ALA   B 1 69  ? -14.957 31.392 -22.764 1.00 31.09 ? 37  ALA   B N   1 
ATOM   1097 C CA  . ALA   B 1 69  ? -13.871 31.942 -21.962 1.00 35.12 ? 37  ALA   B CA  1 
ATOM   1098 C C   . ALA   B 1 69  ? -14.352 32.482 -20.621 1.00 38.35 ? 37  ALA   B C   1 
ATOM   1099 O O   . ALA   B 1 69  ? -13.556 32.570 -19.680 1.00 39.49 ? 37  ALA   B O   1 
ATOM   1100 C CB  . ALA   B 1 69  ? -13.144 33.040 -22.741 1.00 35.79 ? 37  ALA   B CB  1 
ATOM   1101 N N   . ASP   B 1 70  ? -15.625 32.851 -20.514 1.00 39.49 ? 38  ASP   B N   1 
ATOM   1102 C CA  . ASP   B 1 70  ? -16.201 33.298 -19.254 1.00 41.90 ? 38  ASP   B CA  1 
ATOM   1103 C C   . ASP   B 1 70  ? -16.833 32.161 -18.456 1.00 42.30 ? 38  ASP   B C   1 
ATOM   1104 O O   . ASP   B 1 70  ? -17.578 32.428 -17.507 1.00 42.12 ? 38  ASP   B O   1 
ATOM   1105 C CB  . ASP   B 1 70  ? -17.215 34.421 -19.500 1.00 43.96 ? 38  ASP   B CB  1 
ATOM   1106 C CG  . ASP   B 1 70  ? -18.275 34.040 -20.516 1.00 45.47 ? 38  ASP   B CG  1 
ATOM   1107 O OD1 . ASP   B 1 70  ? -18.381 32.843 -20.859 1.00 46.02 ? 38  ASP   B OD1 1 
ATOM   1108 O OD2 . ASP   B 1 70  ? -19.003 34.943 -20.979 1.00 46.40 ? 38  ASP   B OD2 1 
ATOM   1109 N N   . ASP   B 1 71  ? -16.551 30.910 -18.822 1.00 42.63 ? 39  ASP   B N   1 
ATOM   1110 C CA  . ASP   B 1 71  ? -17.024 29.685 -18.177 1.00 43.61 ? 39  ASP   B CA  1 
ATOM   1111 C C   . ASP   B 1 71  ? -18.497 29.377 -18.423 1.00 40.52 ? 39  ASP   B C   1 
ATOM   1112 O O   . ASP   B 1 71  ? -19.010 28.399 -17.862 1.00 41.56 ? 39  ASP   B O   1 
ATOM   1113 C CB  . ASP   B 1 71  ? -16.690 29.605 -16.679 1.00 47.56 ? 39  ASP   B CB  1 
ATOM   1114 C CG  . ASP   B 1 71  ? -15.204 29.436 -16.423 1.00 51.07 ? 39  ASP   B CG  1 
ATOM   1115 O OD1 . ASP   B 1 71  ? -14.466 29.122 -17.381 1.00 52.12 ? 39  ASP   B OD1 1 
ATOM   1116 O OD2 . ASP   B 1 71  ? -14.773 29.626 -15.266 1.00 52.58 ? 39  ASP   B OD2 1 
ATOM   1117 N N   . THR   B 1 72  ? -19.193 30.158 -19.243 1.00 35.84 ? 40  THR   B N   1 
ATOM   1118 C CA  . THR   B 1 72  ? -20.558 29.818 -19.607 1.00 32.72 ? 40  THR   B CA  1 
ATOM   1119 C C   . THR   B 1 72  ? -20.562 28.765 -20.712 1.00 27.64 ? 40  THR   B C   1 
ATOM   1120 O O   . THR   B 1 72  ? -19.559 28.531 -21.387 1.00 25.29 ? 40  THR   B O   1 
ATOM   1121 C CB  . THR   B 1 72  ? -21.306 31.058 -20.089 1.00 34.47 ? 40  THR   B CB  1 
ATOM   1122 O OG1 . THR   B 1 72  ? -20.647 31.587 -21.246 1.00 35.15 ? 40  THR   B OG1 1 
ATOM   1123 C CG2 . THR   B 1 72  ? -21.344 32.116 -18.993 1.00 35.34 ? 40  THR   B CG2 1 
ATOM   1124 N N   . TRP   B 1 73  ? -21.714 28.131 -20.899 1.00 25.46 ? 41  TRP   B N   1 
ATOM   1125 C CA  . TRP   B 1 73  ? -21.861 27.060 -21.879 1.00 24.37 ? 41  TRP   B CA  1 
ATOM   1126 C C   . TRP   B 1 73  ? -22.506 27.624 -23.139 1.00 25.38 ? 41  TRP   B C   1 
ATOM   1127 O O   . TRP   B 1 73  ? -23.667 28.044 -23.114 1.00 28.39 ? 41  TRP   B O   1 
ATOM   1128 C CB  . TRP   B 1 73  ? -22.686 25.914 -21.304 1.00 23.06 ? 41  TRP   B CB  1 
ATOM   1129 C CG  . TRP   B 1 73  ? -21.955 25.150 -20.254 1.00 22.45 ? 41  TRP   B CG  1 
ATOM   1130 C CD1 . TRP   B 1 73  ? -22.199 25.166 -18.913 1.00 24.09 ? 41  TRP   B CD1 1 
ATOM   1131 C CD2 . TRP   B 1 73  ? -20.843 24.266 -20.451 1.00 20.69 ? 41  TRP   B CD2 1 
ATOM   1132 N NE1 . TRP   B 1 73  ? -21.314 24.342 -18.260 1.00 24.40 ? 41  TRP   B NE1 1 
ATOM   1133 C CE2 . TRP   B 1 73  ? -20.473 23.774 -19.182 1.00 22.37 ? 41  TRP   B CE2 1 
ATOM   1134 C CE3 . TRP   B 1 73  ? -20.128 23.839 -21.576 1.00 19.16 ? 41  TRP   B CE3 1 
ATOM   1135 C CZ2 . TRP   B 1 73  ? -19.414 22.879 -19.006 1.00 23.03 ? 41  TRP   B CZ2 1 
ATOM   1136 C CZ3 . TRP   B 1 73  ? -19.079 22.943 -21.397 1.00 19.35 ? 41  TRP   B CZ3 1 
ATOM   1137 C CH2 . TRP   B 1 73  ? -18.734 22.477 -20.122 1.00 20.74 ? 41  TRP   B CH2 1 
ATOM   1138 N N   . GLU   B 1 74  ? -21.757 27.622 -24.239 1.00 23.48 ? 42  GLU   B N   1 
ATOM   1139 C CA  . GLU   B 1 74  ? -22.260 28.129 -25.510 1.00 24.60 ? 42  GLU   B CA  1 
ATOM   1140 C C   . GLU   B 1 74  ? -22.841 26.994 -26.345 1.00 19.92 ? 42  GLU   B C   1 
ATOM   1141 O O   . GLU   B 1 74  ? -22.229 25.929 -26.450 1.00 18.67 ? 42  GLU   B O   1 
ATOM   1142 C CB  . GLU   B 1 74  ? -21.135 28.776 -26.302 1.00 32.65 ? 42  GLU   B CB  1 
ATOM   1143 C CG  . GLU   B 1 74  ? -20.396 29.841 -25.530 1.00 40.90 ? 42  GLU   B CG  1 
ATOM   1144 C CD  . GLU   B 1 74  ? -19.764 30.881 -26.427 1.00 47.55 ? 42  GLU   B CD  1 
ATOM   1145 O OE1 . GLU   B 1 74  ? -20.086 32.076 -26.258 1.00 49.79 ? 42  GLU   B OE1 1 
ATOM   1146 O OE2 . GLU   B 1 74  ? -18.951 30.505 -27.300 1.00 50.18 ? 42  GLU   B OE2 1 
ATOM   1147 N N   . PRO   B 1 75  ? -24.008 27.212 -26.948 1.00 18.63 ? 43  PRO   B N   1 
ATOM   1148 C CA  . PRO   B 1 75  ? -24.602 26.182 -27.813 1.00 17.49 ? 43  PRO   B CA  1 
ATOM   1149 C C   . PRO   B 1 75  ? -23.651 25.789 -28.930 1.00 15.97 ? 43  PRO   B C   1 
ATOM   1150 O O   . PRO   B 1 75  ? -23.022 26.641 -29.563 1.00 18.02 ? 43  PRO   B O   1 
ATOM   1151 C CB  . PRO   B 1 75  ? -25.846 26.877 -28.375 1.00 19.12 ? 43  PRO   B CB  1 
ATOM   1152 C CG  . PRO   B 1 75  ? -26.173 27.939 -27.360 1.00 21.47 ? 43  PRO   B CG  1 
ATOM   1153 C CD  . PRO   B 1 75  ? -24.852 28.415 -26.840 1.00 20.35 ? 43  PRO   B CD  1 
ATOM   1154 N N   . PHE   B 1 76  ? -23.531 24.479 -29.153 1.00 14.97 ? 44  PHE   B N   1 
ATOM   1155 C CA  . PHE   B 1 76  ? -22.614 23.966 -30.168 1.00 14.21 ? 44  PHE   B CA  1 
ATOM   1156 C C   . PHE   B 1 76  ? -23.267 23.065 -31.220 1.00 14.08 ? 44  PHE   B C   1 
ATOM   1157 O O   . PHE   B 1 76  ? -23.021 23.223 -32.420 1.00 15.53 ? 44  PHE   B O   1 
ATOM   1158 C CB  . PHE   B 1 76  ? -21.421 23.265 -29.508 1.00 14.82 ? 44  PHE   B CB  1 
ATOM   1159 C CG  . PHE   B 1 76  ? -20.390 22.785 -30.482 1.00 14.86 ? 44  PHE   B CG  1 
ATOM   1160 C CD1 . PHE   B 1 76  ? -19.489 23.684 -31.049 1.00 16.87 ? 44  PHE   B CD1 1 
ATOM   1161 C CD2 . PHE   B 1 76  ? -20.314 21.444 -30.836 1.00 15.23 ? 44  PHE   B CD2 1 
ATOM   1162 C CE1 . PHE   B 1 76  ? -18.533 23.256 -31.958 1.00 17.99 ? 44  PHE   B CE1 1 
ATOM   1163 C CE2 . PHE   B 1 76  ? -19.357 21.003 -31.743 1.00 16.60 ? 44  PHE   B CE2 1 
ATOM   1164 C CZ  . PHE   B 1 76  ? -18.461 21.916 -32.301 1.00 17.39 ? 44  PHE   B CZ  1 
ATOM   1165 N N   . ALA   B 1 77  ? -24.073 22.099 -30.789 1.00 13.09 ? 45  ALA   B N   1 
ATOM   1166 C CA  . ALA   B 1 77  ? -24.721 21.174 -31.713 1.00 13.35 ? 45  ALA   B CA  1 
ATOM   1167 C C   . ALA   B 1 77  ? -25.892 20.543 -30.980 1.00 12.84 ? 45  ALA   B C   1 
ATOM   1168 O O   . ALA   B 1 77  ? -26.041 20.711 -29.770 1.00 14.00 ? 45  ALA   B O   1 
ATOM   1169 C CB  . ALA   B 1 77  ? -23.753 20.080 -32.182 1.00 15.22 ? 45  ALA   B CB  1 
ATOM   1170 N N   . SER   B 1 78  ? -26.732 19.822 -31.721 1.00 12.93 ? 46  SER   B N   1 
ATOM   1171 C CA  . SER   B 1 78  ? -27.806 19.062 -31.080 1.00 13.69 ? 46  SER   B CA  1 
ATOM   1172 C C   . SER   B 1 78  ? -28.421 18.074 -32.067 1.00 12.54 ? 46  SER   B C   1 
ATOM   1173 O O   . SER   B 1 78  ? -28.103 18.073 -33.257 1.00 14.44 ? 46  SER   B O   1 
ATOM   1174 C CB  . SER   B 1 78  ? -28.873 19.962 -30.467 1.00 19.56 ? 46  SER   B CB  1 
ATOM   1175 O OG  . SER   B 1 78  ? -29.641 20.563 -31.474 1.00 20.90 ? 46  SER   B OG  1 
ATOM   1176 N N   . GLY   B 1 79  ? -29.305 17.227 -31.551 1.00 12.42 ? 47  GLY   B N   1 
ATOM   1177 C CA  . GLY   B 1 79  ? -30.028 16.285 -32.382 1.00 13.44 ? 47  GLY   B CA  1 
ATOM   1178 C C   . GLY   B 1 79  ? -30.720 15.244 -31.524 1.00 12.69 ? 47  GLY   B C   1 
ATOM   1179 O O   . GLY   B 1 79  ? -30.728 15.332 -30.293 1.00 13.20 ? 47  GLY   B O   1 
ATOM   1180 N N   . LYS   B 1 80  ? -31.314 14.261 -32.191 1.00 13.11 ? 48  LYS   B N   1 
ATOM   1181 C CA  . LYS   B 1 80  ? -31.878 13.126 -31.481 1.00 14.85 ? 48  LYS   B CA  1 
ATOM   1182 C C   . LYS   B 1 80  ? -31.434 11.819 -32.119 1.00 14.39 ? 48  LYS   B C   1 
ATOM   1183 O O   . LYS   B 1 80  ? -31.130 11.761 -33.315 1.00 15.17 ? 48  LYS   B O   1 
ATOM   1184 C CB  . LYS   B 1 80  ? -33.402 13.187 -31.367 1.00 18.68 ? 48  LYS   B CB  1 
ATOM   1185 C CG  . LYS   B 1 80  ? -34.144 13.090 -32.665 1.00 23.02 ? 48  LYS   B CG  1 
ATOM   1186 C CD  . LYS   B 1 80  ? -35.633 13.269 -32.398 1.00 26.03 ? 48  LYS   B CD  1 
ATOM   1187 C CE  . LYS   B 1 80  ? -36.468 13.017 -33.635 1.00 29.97 ? 48  LYS   B CE  1 
ATOM   1188 N NZ  . LYS   B 1 80  ? -37.916 13.249 -33.367 1.00 33.16 ? 48  LYS   B NZ  1 
ATOM   1189 N N   . THR   B 1 81  ? -31.380 10.773 -31.305 1.00 13.25 ? 49  THR   B N   1 
ATOM   1190 C CA  . THR   B 1 81  ? -30.893 9.499  -31.815 1.00 13.27 ? 49  THR   B CA  1 
ATOM   1191 C C   . THR   B 1 81  ? -31.852 8.902  -32.839 1.00 12.95 ? 49  THR   B C   1 
ATOM   1192 O O   . THR   B 1 81  ? -33.075 9.072  -32.771 1.00 13.56 ? 49  THR   B O   1 
ATOM   1193 C CB  . THR   B 1 81  ? -30.664 8.498  -30.683 1.00 12.19 ? 49  THR   B CB  1 
ATOM   1194 O OG1 . THR   B 1 81  ? -31.892 8.285  -29.976 1.00 12.65 ? 49  THR   B OG1 1 
ATOM   1195 C CG2 . THR   B 1 81  ? -29.559 8.981  -29.736 1.00 13.11 ? 49  THR   B CG2 1 
ATOM   1196 N N   . SER   B 1 82  ? -31.266 8.182  -33.786 1.00 14.28 ? 50  SER   B N   1 
ATOM   1197 C CA  . SER   B 1 82  ? -31.982 7.489  -34.840 1.00 15.27 ? 50  SER   B CA  1 
ATOM   1198 C C   . SER   B 1 82  ? -32.526 6.161  -34.320 1.00 15.97 ? 50  SER   B C   1 
ATOM   1199 O O   . SER   B 1 82  ? -32.387 5.810  -33.144 1.00 15.60 ? 50  SER   B O   1 
ATOM   1200 C CB  . SER   B 1 82  ? -31.024 7.204  -35.987 1.00 16.85 ? 50  SER   B CB  1 
ATOM   1201 O OG  . SER   B 1 82  ? -30.079 6.226  -35.574 1.00 18.72 ? 50  SER   B OG  1 
ATOM   1202 N N   . GLU   B 1 83  ? -33.128 5.390  -35.229 1.00 17.97 ? 51  GLU   B N   1 
ATOM   1203 C CA  . GLU   B 1 83  ? -33.644 4.077  -34.866 1.00 21.02 ? 51  GLU   B CA  1 
ATOM   1204 C C   . GLU   B 1 83  ? -32.543 3.107  -34.464 1.00 18.98 ? 51  GLU   B C   1 
ATOM   1205 O O   . GLU   B 1 83  ? -32.840 2.094  -33.833 1.00 19.15 ? 51  GLU   B O   1 
ATOM   1206 C CB  . GLU   B 1 83  ? -34.501 3.509  -36.002 1.00 28.89 ? 51  GLU   B CB  1 
ATOM   1207 C CG  . GLU   B 1 83  ? -35.720 4.371  -36.326 1.00 38.79 ? 51  GLU   B CG  1 
ATOM   1208 C CD  . GLU   B 1 83  ? -36.706 3.686  -37.258 1.00 47.38 ? 51  GLU   B CD  1 
ATOM   1209 O OE1 . GLU   B 1 83  ? -37.059 2.515  -37.005 1.00 50.25 ? 51  GLU   B OE1 1 
ATOM   1210 O OE2 . GLU   B 1 83  ? -37.128 4.324  -38.246 1.00 50.61 ? 51  GLU   B OE2 1 
ATOM   1211 N N   . SER   B 1 84  ? -31.287 3.390  -34.809 1.00 17.12 ? 52  SER   B N   1 
ATOM   1212 C CA  . SER   B 1 84  ? -30.163 2.595  -34.333 1.00 17.62 ? 52  SER   B CA  1 
ATOM   1213 C C   . SER   B 1 84  ? -29.620 3.087  -32.999 1.00 15.72 ? 52  SER   B C   1 
ATOM   1214 O O   . SER   B 1 84  ? -28.633 2.532  -32.509 1.00 16.02 ? 52  SER   B O   1 
ATOM   1215 C CB  . SER   B 1 84  ? -29.028 2.606  -35.358 1.00 21.53 ? 52  SER   B CB  1 
ATOM   1216 O OG  . SER   B 1 84  ? -28.446 3.897  -35.442 1.00 24.68 ? 52  SER   B OG  1 
ATOM   1217 N N   . GLY   B 1 85  ? -30.228 4.116  -32.407 1.00 13.62 ? 53  GLY   B N   1 
ATOM   1218 C CA  . GLY   B 1 85  ? -29.713 4.695  -31.188 1.00 13.75 ? 53  GLY   B CA  1 
ATOM   1219 C C   . GLY   B 1 85  ? -28.547 5.636  -31.388 1.00 12.97 ? 53  GLY   B C   1 
ATOM   1220 O O   . GLY   B 1 85  ? -27.941 6.065  -30.403 1.00 13.51 ? 53  GLY   B O   1 
ATOM   1221 N N   . GLU   B 1 86  ? -28.205 5.967  -32.630 1.00 13.74 ? 54  GLU   B N   1 
ATOM   1222 C CA  . GLU   B 1 86  ? -27.025 6.763  -32.927 1.00 13.73 ? 54  GLU   B CA  1 
ATOM   1223 C C   . GLU   B 1 86  ? -27.412 8.155  -33.396 1.00 13.25 ? 54  GLU   B C   1 
ATOM   1224 O O   . GLU   B 1 86  ? -28.447 8.351  -34.036 1.00 13.83 ? 54  GLU   B O   1 
ATOM   1225 C CB  . GLU   B 1 86  ? -26.164 6.071  -33.986 1.00 15.79 ? 54  GLU   B CB  1 
ATOM   1226 C CG  . GLU   B 1 86  ? -25.615 4.732  -33.490 1.00 19.19 ? 54  GLU   B CG  1 
ATOM   1227 C CD  . GLU   B 1 86  ? -24.881 3.938  -34.555 1.00 23.91 ? 54  GLU   B CD  1 
ATOM   1228 O OE1 . GLU   B 1 86  ? -24.688 4.451  -35.673 1.00 26.15 ? 54  GLU   B OE1 1 
ATOM   1229 O OE2 . GLU   B 1 86  ? -24.498 2.789  -34.264 1.00 25.93 ? 54  GLU   B OE2 1 
ATOM   1230 N N   . LEU   B 1 87  ? -26.572 9.126  -33.052 1.00 12.59 ? 55  LEU   B N   1 
ATOM   1231 C CA  . LEU   B 1 87  ? -26.702 10.493 -33.535 1.00 12.67 ? 55  LEU   B CA  1 
ATOM   1232 C C   . LEU   B 1 87  ? -25.390 10.860 -34.208 1.00 13.76 ? 55  LEU   B C   1 
ATOM   1233 O O   . LEU   B 1 87  ? -24.359 10.987 -33.539 1.00 14.06 ? 55  LEU   B O   1 
ATOM   1234 C CB  . LEU   B 1 87  ? -27.041 11.452 -32.397 1.00 12.72 ? 55  LEU   B CB  1 
ATOM   1235 C CG  . LEU   B 1 87  ? -27.054 12.937 -32.761 1.00 12.96 ? 55  LEU   B CG  1 
ATOM   1236 C CD1 . LEU   B 1 87  ? -27.929 13.223 -33.981 1.00 13.76 ? 55  LEU   B CD1 1 
ATOM   1237 C CD2 . LEU   B 1 87  ? -27.519 13.718 -31.544 1.00 13.84 ? 55  LEU   B CD2 1 
ATOM   1238 N N   . HIS   B 1 88  ? -25.437 10.971 -35.533 1.00 16.09 ? 56  HIS   B N   1 
ATOM   1239 C CA  . HIS   B 1 88  ? -24.330 11.335 -36.404 1.00 18.98 ? 56  HIS   B CA  1 
ATOM   1240 C C   . HIS   B 1 88  ? -24.514 12.767 -36.892 1.00 19.55 ? 56  HIS   B C   1 
ATOM   1241 O O   . HIS   B 1 88  ? -25.584 13.365 -36.764 1.00 20.48 ? 56  HIS   B O   1 
ATOM   1242 C CB  . HIS   B 1 88  ? -24.278 10.399 -37.621 1.00 21.14 ? 56  HIS   B CB  1 
ATOM   1243 C CG  . HIS   B 1 88  ? -24.017 8.966  -37.279 1.00 23.12 ? 56  HIS   B CG  1 
ATOM   1244 N ND1 . HIS   B 1 88  ? -22.757 8.411  -37.324 1.00 24.78 ? 56  HIS   B ND1 1 
ATOM   1245 C CD2 . HIS   B 1 88  ? -24.852 7.970  -36.902 1.00 24.60 ? 56  HIS   B CD2 1 
ATOM   1246 C CE1 . HIS   B 1 88  ? -22.826 7.135  -36.989 1.00 25.18 ? 56  HIS   B CE1 1 
ATOM   1247 N NE2 . HIS   B 1 88  ? -24.086 6.842  -36.726 1.00 25.72 ? 56  HIS   B NE2 1 
ATOM   1248 N N   . GLY   B 1 89  ? -23.452 13.313 -37.472 1.00 18.93 ? 57  GLY   B N   1 
ATOM   1249 C CA  . GLY   B 1 89  ? -23.549 14.613 -38.110 1.00 19.20 ? 57  GLY   B CA  1 
ATOM   1250 C C   . GLY   B 1 89  ? -23.630 15.805 -37.182 1.00 18.54 ? 57  GLY   B C   1 
ATOM   1251 O O   . GLY   B 1 89  ? -24.112 16.865 -37.599 1.00 20.50 ? 57  GLY   B O   1 
ATOM   1252 N N   . LEU   B 1 90  ? -23.174 15.668 -35.932 1.00 17.42 ? 58  LEU   B N   1 
ATOM   1253 C CA  . LEU   B 1 90  ? -23.235 16.782 -34.988 1.00 16.56 ? 58  LEU   B CA  1 
ATOM   1254 C C   . LEU   B 1 90  ? -22.324 17.933 -35.393 1.00 15.86 ? 58  LEU   B C   1 
ATOM   1255 O O   . LEU   B 1 90  ? -22.684 19.101 -35.213 1.00 17.10 ? 58  LEU   B O   1 
ATOM   1256 C CB  . LEU   B 1 90  ? -22.891 16.301 -33.580 1.00 16.09 ? 58  LEU   B CB  1 
ATOM   1257 C CG  . LEU   B 1 90  ? -24.002 15.532 -32.863 1.00 16.32 ? 58  LEU   B CG  1 
ATOM   1258 C CD1 . LEU   B 1 90  ? -23.428 14.776 -31.677 1.00 17.33 ? 58  LEU   B CD1 1 
ATOM   1259 C CD2 . LEU   B 1 90  ? -25.102 16.485 -32.428 1.00 16.73 ? 58  LEU   B CD2 1 
ATOM   1260 N N   . THR   B 1 91  ? -21.139 17.633 -35.918 1.00 15.63 ? 59  THR   B N   1 
ATOM   1261 C CA  . THR   B 1 91  ? -20.170 18.673 -36.229 1.00 16.36 ? 59  THR   B CA  1 
ATOM   1262 C C   . THR   B 1 91  ? -19.314 18.216 -37.406 1.00 17.53 ? 59  THR   B C   1 
ATOM   1263 O O   . THR   B 1 91  ? -19.540 17.157 -37.994 1.00 19.18 ? 59  THR   B O   1 
ATOM   1264 C CB  . THR   B 1 91  ? -19.364 19.038 -34.971 1.00 15.79 ? 59  THR   B CB  1 
ATOM   1265 O OG1 . THR   B 1 91  ? -18.530 20.179 -35.222 1.00 16.85 ? 59  THR   B OG1 1 
ATOM   1266 C CG2 . THR   B 1 91  ? -18.501 17.858 -34.512 1.00 16.29 ? 59  THR   B CG2 1 
ATOM   1267 N N   . THR   B 1 92  ? -18.340 19.041 -37.772 1.00 18.02 ? 60  THR   B N   1 
ATOM   1268 C CA  . THR   B 1 92  ? -17.369 18.697 -38.798 1.00 19.37 ? 60  THR   B CA  1 
ATOM   1269 C C   . THR   B 1 92  ? -15.984 18.819 -38.192 1.00 18.82 ? 60  THR   B C   1 
ATOM   1270 O O   . THR   B 1 92  ? -15.802 19.462 -37.155 1.00 18.23 ? 60  THR   B O   1 
ATOM   1271 C CB  . THR   B 1 92  ? -17.451 19.640 -39.999 1.00 21.43 ? 60  THR   B CB  1 
ATOM   1272 O OG1 . THR   B 1 92  ? -17.115 20.968 -39.577 1.00 22.82 ? 60  THR   B OG1 1 
ATOM   1273 C CG2 . THR   B 1 92  ? -18.840 19.620 -40.602 1.00 23.06 ? 60  THR   B CG2 1 
ATOM   1274 N N   . GLU   B 1 93  ? -14.993 18.224 -38.858 1.00 19.99 ? 61  GLU   B N   1 
ATOM   1275 C CA  . GLU   B 1 93  ? -13.648 18.292 -38.297 1.00 22.96 ? 61  GLU   B CA  1 
ATOM   1276 C C   . GLU   B 1 93  ? -13.164 19.731 -38.172 1.00 20.04 ? 61  GLU   B C   1 
ATOM   1277 O O   . GLU   B 1 93  ? -12.576 20.094 -37.151 1.00 18.85 ? 61  GLU   B O   1 
ATOM   1278 C CB  . GLU   B 1 93  ? -12.655 17.393 -39.041 1.00 32.43 ? 61  GLU   B CB  1 
ATOM   1279 C CG  . GLU   B 1 93  ? -12.468 17.640 -40.513 1.00 42.62 ? 61  GLU   B CG  1 
ATOM   1280 C CD  . GLU   B 1 93  ? -11.444 16.683 -41.102 1.00 50.71 ? 61  GLU   B CD  1 
ATOM   1281 O OE1 . GLU   B 1 93  ? -11.026 15.750 -40.379 1.00 52.49 ? 61  GLU   B OE1 1 
ATOM   1282 O OE2 . GLU   B 1 93  ? -11.056 16.862 -42.278 1.00 53.93 ? 61  GLU   B OE2 1 
ATOM   1283 N N   . GLU   B 1 94  ? -13.457 20.577 -39.171 1.00 19.96 ? 62  GLU   B N   1 
ATOM   1284 C CA  . GLU   B 1 94  ? -12.992 21.964 -39.144 1.00 22.58 ? 62  GLU   B CA  1 
ATOM   1285 C C   . GLU   B 1 94  ? -13.578 22.739 -37.969 1.00 18.93 ? 62  GLU   B C   1 
ATOM   1286 O O   . GLU   B 1 94  ? -12.912 23.608 -37.396 1.00 19.37 ? 62  GLU   B O   1 
ATOM   1287 C CB  . GLU   B 1 94  ? -13.356 22.672 -40.452 1.00 31.57 ? 62  GLU   B CB  1 
ATOM   1288 C CG  . GLU   B 1 94  ? -12.671 22.154 -41.704 1.00 41.63 ? 62  GLU   B CG  1 
ATOM   1289 C CD  . GLU   B 1 94  ? -13.031 22.988 -42.924 1.00 50.01 ? 62  GLU   B CD  1 
ATOM   1290 O OE1 . GLU   B 1 94  ? -14.108 23.623 -42.908 1.00 52.86 ? 62  GLU   B OE1 1 
ATOM   1291 O OE2 . GLU   B 1 94  ? -12.238 23.020 -43.890 1.00 52.57 ? 62  GLU   B OE2 1 
ATOM   1292 N N   . GLU   B 1 95  ? -14.836 22.466 -37.618 1.00 18.21 ? 63  GLU   B N   1 
ATOM   1293 C CA  . GLU   B 1 95  ? -15.532 23.201 -36.569 1.00 19.89 ? 63  GLU   B CA  1 
ATOM   1294 C C   . GLU   B 1 95  ? -15.196 22.686 -35.178 1.00 18.42 ? 63  GLU   B C   1 
ATOM   1295 O O   . GLU   B 1 95  ? -15.319 23.427 -34.195 1.00 20.52 ? 63  GLU   B O   1 
ATOM   1296 C CB  . GLU   B 1 95  ? -17.045 23.061 -36.766 1.00 25.07 ? 63  GLU   B CB  1 
ATOM   1297 C CG  . GLU   B 1 95  ? -17.873 23.870 -35.776 1.00 32.76 ? 63  GLU   B CG  1 
ATOM   1298 C CD  . GLU   B 1 95  ? -19.331 23.451 -35.707 1.00 38.67 ? 63  GLU   B CD  1 
ATOM   1299 O OE1 . GLU   B 1 95  ? -19.645 22.274 -36.000 1.00 39.93 ? 63  GLU   B OE1 1 
ATOM   1300 O OE2 . GLU   B 1 95  ? -20.166 24.312 -35.359 1.00 41.66 ? 63  GLU   B OE2 1 
ATOM   1301 N N   . PHE   B 1 96  ? -14.778 21.436 -35.073 1.00 16.19 ? 64  PHE   B N   1 
ATOM   1302 C CA  . PHE   B 1 96  ? -14.627 20.761 -33.789 1.00 15.73 ? 64  PHE   B CA  1 
ATOM   1303 C C   . PHE   B 1 96  ? -13.175 20.924 -33.366 1.00 15.32 ? 64  PHE   B C   1 
ATOM   1304 O O   . PHE   B 1 96  ? -12.316 20.111 -33.691 1.00 17.93 ? 64  PHE   B O   1 
ATOM   1305 C CB  . PHE   B 1 96  ? -15.015 19.304 -33.974 1.00 16.33 ? 64  PHE   B CB  1 
ATOM   1306 C CG  . PHE   B 1 96  ? -15.210 18.541 -32.697 1.00 15.28 ? 64  PHE   B CG  1 
ATOM   1307 C CD1 . PHE   B 1 96  ? -15.799 19.115 -31.577 1.00 15.54 ? 64  PHE   B CD1 1 
ATOM   1308 C CD2 . PHE   B 1 96  ? -14.848 17.215 -32.641 1.00 17.33 ? 64  PHE   B CD2 1 
ATOM   1309 C CE1 . PHE   B 1 96  ? -15.987 18.374 -30.425 1.00 16.21 ? 64  PHE   B CE1 1 
ATOM   1310 C CE2 . PHE   B 1 96  ? -15.037 16.470 -31.494 1.00 18.61 ? 64  PHE   B CE2 1 
ATOM   1311 C CZ  . PHE   B 1 96  ? -15.605 17.046 -30.386 1.00 17.61 ? 64  PHE   B CZ  1 
ATOM   1312 N N   . VAL   B 1 97  ? -12.897 22.004 -32.644 1.00 15.49 ? 65  VAL   B N   1 
ATOM   1313 C CA  . VAL   B 1 97  ? -11.535 22.317 -32.231 1.00 15.48 ? 65  VAL   B CA  1 
ATOM   1314 C C   . VAL   B 1 97  ? -11.412 22.145 -30.729 1.00 14.76 ? 65  VAL   B C   1 
ATOM   1315 O O   . VAL   B 1 97  ? -12.351 21.690 -30.063 1.00 14.85 ? 65  VAL   B O   1 
ATOM   1316 C CB  . VAL   B 1 97  ? -11.112 23.735 -32.657 1.00 18.61 ? 65  VAL   B CB  1 
ATOM   1317 C CG1 . VAL   B 1 97  ? -11.049 23.829 -34.157 1.00 18.81 ? 65  VAL   B CG1 1 
ATOM   1318 C CG2 . VAL   B 1 97  ? -12.069 24.771 -32.083 1.00 21.46 ? 65  VAL   B CG2 1 
ATOM   1319 N N   . GLU   B 1 98  ? -10.235 22.459 -30.198 1.00 16.00 ? 66  GLU   B N   1 
ATOM   1320 C CA  . GLU   B 1 98  ? -9.995  22.278 -28.777 1.00 17.92 ? 66  GLU   B CA  1 
ATOM   1321 C C   . GLU   B 1 98  ? -11.023 23.039 -27.966 1.00 16.99 ? 66  GLU   B C   1 
ATOM   1322 O O   . GLU   B 1 98  ? -11.371 24.182 -28.275 1.00 19.70 ? 66  GLU   B O   1 
ATOM   1323 C CB  . GLU   B 1 98  ? -8.596  22.762 -28.407 1.00 20.31 ? 66  GLU   B CB  1 
ATOM   1324 C CG  . GLU   B 1 98  ? -8.217  22.511 -26.949 1.00 26.61 ? 66  GLU   B CG  1 
ATOM   1325 C CD  . GLU   B 1 98  ? -8.792  23.539 -25.983 1.00 33.97 ? 66  GLU   B CD  1 
ATOM   1326 O OE1 . GLU   B 1 98  ? -9.057  23.168 -24.816 1.00 36.85 ? 66  GLU   B OE1 1 
ATOM   1327 O OE2 . GLU   B 1 98  ? -9.001  24.701 -26.392 1.00 36.46 ? 66  GLU   B OE2 1 
ATOM   1328 N N   . GLY   B 1 99  ? -11.498 22.394 -26.914 1.00 16.59 ? 67  GLY   B N   1 
ATOM   1329 C CA  . GLY   B 1 99  ? -12.402 23.016 -25.977 1.00 15.95 ? 67  GLY   B CA  1 
ATOM   1330 C C   . GLY   B 1 99  ? -12.886 21.975 -25.006 1.00 13.39 ? 67  GLY   B C   1 
ATOM   1331 O O   . GLY   B 1 99  ? -12.593 20.781 -25.127 1.00 14.09 ? 67  GLY   B O   1 
ATOM   1332 N N   . ILE   B 1 100 ? -13.621 22.450 -24.018 1.00 14.13 ? 68  ILE   B N   1 
ATOM   1333 C CA  . ILE   B 1 100 ? -14.354 21.577 -23.119 1.00 13.61 ? 68  ILE   B CA  1 
ATOM   1334 C C   . ILE   B 1 100 ? -15.785 21.531 -23.623 1.00 12.35 ? 68  ILE   B C   1 
ATOM   1335 O O   . ILE   B 1 100 ? -16.426 22.578 -23.801 1.00 14.32 ? 68  ILE   B O   1 
ATOM   1336 C CB  . ILE   B 1 100 ? -14.288 22.072 -21.669 1.00 14.41 ? 68  ILE   B CB  1 
ATOM   1337 C CG1 . ILE   B 1 100 ? -12.837 22.099 -21.188 1.00 16.22 ? 68  ILE   B CG1 1 
ATOM   1338 C CG2 . ILE   B 1 100 ? -15.149 21.189 -20.784 1.00 14.19 ? 68  ILE   B CG2 1 
ATOM   1339 C CD1 . ILE   B 1 100 ? -12.641 22.679 -19.811 1.00 18.91 ? 68  ILE   B CD1 1 
ATOM   1340 N N   . TYR   B 1 101 ? -16.271 20.320 -23.881 1.00 11.77 ? 69  TYR   B N   1 
ATOM   1341 C CA  . TYR   B 1 101 ? -17.590 20.104 -24.444 1.00 11.15 ? 69  TYR   B CA  1 
ATOM   1342 C C   . TYR   B 1 101 ? -18.462 19.390 -23.427 1.00 11.70 ? 69  TYR   B C   1 
ATOM   1343 O O   . TYR   B 1 101 ? -17.976 18.608 -22.605 1.00 12.51 ? 69  TYR   B O   1 
ATOM   1344 C CB  . TYR   B 1 101 ? -17.506 19.271 -25.727 1.00 12.21 ? 69  TYR   B CB  1 
ATOM   1345 C CG  . TYR   B 1 101 ? -16.816 20.010 -26.841 1.00 11.28 ? 69  TYR   B CG  1 
ATOM   1346 C CD1 . TYR   B 1 101 ? -15.427 20.033 -26.936 1.00 12.34 ? 69  TYR   B CD1 1 
ATOM   1347 C CD2 . TYR   B 1 101 ? -17.554 20.725 -27.780 1.00 12.31 ? 69  TYR   B CD2 1 
ATOM   1348 C CE1 . TYR   B 1 101 ? -14.793 20.734 -27.951 1.00 12.84 ? 69  TYR   B CE1 1 
ATOM   1349 C CE2 . TYR   B 1 101 ? -16.932 21.421 -28.792 1.00 12.81 ? 69  TYR   B CE2 1 
ATOM   1350 C CZ  . TYR   B 1 101 ? -15.556 21.423 -28.877 1.00 12.93 ? 69  TYR   B CZ  1 
ATOM   1351 O OH  . TYR   B 1 101 ? -14.952 22.125 -29.896 1.00 14.52 ? 69  TYR   B OH  1 
ATOM   1352 N N   . LYS   B 1 102 ? -19.756 19.675 -23.490 1.00 11.22 ? 70  LYS   B N   1 
ATOM   1353 C CA  . LYS   B 1 102 ? -20.740 19.048 -22.624 1.00 12.74 ? 70  LYS   B CA  1 
ATOM   1354 C C   . LYS   B 1 102 ? -21.854 18.504 -23.498 1.00 12.60 ? 70  LYS   B C   1 
ATOM   1355 O O   . LYS   B 1 102 ? -22.470 19.250 -24.261 1.00 14.18 ? 70  LYS   B O   1 
ATOM   1356 C CB  . LYS   B 1 102 ? -21.310 20.056 -21.620 1.00 14.72 ? 70  LYS   B CB  1 
ATOM   1357 C CG  . LYS   B 1 102 ? -22.493 19.493 -20.828 1.00 16.31 ? 70  LYS   B CG  1 
ATOM   1358 C CD  . LYS   B 1 102 ? -22.917 20.382 -19.667 1.00 19.72 ? 70  LYS   B CD  1 
ATOM   1359 C CE  . LYS   B 1 102 ? -23.531 21.682 -20.154 1.00 22.27 ? 70  LYS   B CE  1 
ATOM   1360 N NZ  . LYS   B 1 102 ? -24.144 22.452 -19.031 1.00 24.33 ? 70  LYS   B NZ  1 
ATOM   1361 N N   . VAL   B 1 103 ? -22.101 17.209 -23.397 1.00 12.68 ? 71  VAL   B N   1 
ATOM   1362 C CA  . VAL   B 1 103 ? -23.252 16.584 -24.027 1.00 13.34 ? 71  VAL   B CA  1 
ATOM   1363 C C   . VAL   B 1 103 ? -24.302 16.387 -22.940 1.00 13.62 ? 71  VAL   B C   1 
ATOM   1364 O O   . VAL   B 1 103 ? -24.060 15.671 -21.961 1.00 15.24 ? 71  VAL   B O   1 
ATOM   1365 C CB  . VAL   B 1 103 ? -22.874 15.245 -24.677 1.00 15.17 ? 71  VAL   B CB  1 
ATOM   1366 C CG1 . VAL   B 1 103 ? -24.097 14.652 -25.370 1.00 17.29 ? 71  VAL   B CG1 1 
ATOM   1367 C CG2 . VAL   B 1 103 ? -21.715 15.420 -25.656 1.00 16.39 ? 71  VAL   B CG2 1 
ATOM   1368 N N   . GLU   B 1 104 ? -25.454 17.041 -23.089 1.00 12.95 ? 72  GLU   B N   1 
ATOM   1369 C CA  . GLU   B 1 104 ? -26.563 16.915 -22.146 1.00 13.29 ? 72  GLU   B CA  1 
ATOM   1370 C C   . GLU   B 1 104 ? -27.642 16.074 -22.814 1.00 11.76 ? 72  GLU   B C   1 
ATOM   1371 O O   . GLU   B 1 104 ? -28.313 16.540 -23.742 1.00 11.94 ? 72  GLU   B O   1 
ATOM   1372 C CB  . GLU   B 1 104 ? -27.118 18.284 -21.749 1.00 17.52 ? 72  GLU   B CB  1 
ATOM   1373 C CG  . GLU   B 1 104 ? -26.327 19.012 -20.683 1.00 23.27 ? 72  GLU   B CG  1 
ATOM   1374 C CD  . GLU   B 1 104 ? -27.080 20.195 -20.071 1.00 27.24 ? 72  GLU   B CD  1 
ATOM   1375 O OE1 . GLU   B 1 104 ? -28.203 20.533 -20.533 1.00 27.17 ? 72  GLU   B OE1 1 
ATOM   1376 O OE2 . GLU   B 1 104 ? -26.536 20.801 -19.124 1.00 29.60 ? 72  GLU   B OE2 1 
ATOM   1377 N N   . ILE   B 1 105 ? -27.810 14.841 -22.344 1.00 11.68 ? 73  ILE   B N   1 
ATOM   1378 C CA  . ILE   B 1 105 ? -28.720 13.872 -22.949 1.00 11.54 ? 73  ILE   B CA  1 
ATOM   1379 C C   . ILE   B 1 105 ? -29.999 13.857 -22.125 1.00 11.53 ? 73  ILE   B C   1 
ATOM   1380 O O   . ILE   B 1 105 ? -29.954 13.608 -20.913 1.00 11.99 ? 73  ILE   B O   1 
ATOM   1381 C CB  . ILE   B 1 105 ? -28.086 12.471 -22.990 1.00 12.39 ? 73  ILE   B CB  1 
ATOM   1382 C CG1 . ILE   B 1 105 ? -26.729 12.504 -23.687 1.00 13.41 ? 73  ILE   B CG1 1 
ATOM   1383 C CG2 . ILE   B 1 105 ? -29.016 11.496 -23.663 1.00 13.95 ? 73  ILE   B CG2 1 
ATOM   1384 C CD1 . ILE   B 1 105 ? -25.984 11.181 -23.614 1.00 15.17 ? 73  ILE   B CD1 1 
ATOM   1385 N N   . ASP   B 1 106 ? -31.141 14.119 -22.767 1.00 11.63 ? 74  ASP   B N   1 
ATOM   1386 C CA  . ASP   B 1 106 ? -32.417 14.169 -22.045 1.00 12.68 ? 74  ASP   B CA  1 
ATOM   1387 C C   . ASP   B 1 106 ? -32.950 12.758 -21.803 1.00 12.53 ? 74  ASP   B C   1 
ATOM   1388 O O   . ASP   B 1 106 ? -33.871 12.272 -22.465 1.00 13.52 ? 74  ASP   B O   1 
ATOM   1389 C CB  . ASP   B 1 106 ? -33.433 15.040 -22.765 1.00 13.75 ? 74  ASP   B CB  1 
ATOM   1390 C CG  . ASP   B 1 106 ? -34.714 15.202 -21.968 1.00 15.13 ? 74  ASP   B CG  1 
ATOM   1391 O OD1 . ASP   B 1 106 ? -34.787 14.671 -20.836 1.00 15.94 ? 74  ASP   B OD1 1 
ATOM   1392 O OD2 . ASP   B 1 106 ? -35.646 15.858 -22.471 1.00 17.52 ? 74  ASP   B OD2 1 
ATOM   1393 N N   . THR   B 1 107 ? -32.366 12.107 -20.800 1.00 13.02 ? 75  THR   B N   1 
ATOM   1394 C CA  . THR   B 1 107 ? -32.782 10.760 -20.438 1.00 12.26 ? 75  THR   B CA  1 
ATOM   1395 C C   . THR   B 1 107 ? -34.115 10.772 -19.706 1.00 11.78 ? 75  THR   B C   1 
ATOM   1396 O O   . THR   B 1 107 ? -34.874 9.803  -19.787 1.00 13.16 ? 75  THR   B O   1 
ATOM   1397 C CB  . THR   B 1 107 ? -31.707 10.119 -19.564 1.00 12.51 ? 75  THR   B CB  1 
ATOM   1398 O OG1 . THR   B 1 107 ? -31.464 10.948 -18.420 1.00 12.31 ? 75  THR   B OG1 1 
ATOM   1399 C CG2 . THR   B 1 107 ? -30.406 9.954  -20.357 1.00 13.50 ? 75  THR   B CG2 1 
ATOM   1400 N N   . LYS   B 1 108 ? -34.430 11.861 -19.004 1.00 12.04 ? 76  LYS   B N   1 
ATOM   1401 C CA  . LYS   B 1 108 ? -35.677 11.911 -18.250 1.00 13.30 ? 76  LYS   B CA  1 
ATOM   1402 C C   . LYS   B 1 108 ? -36.877 11.797 -19.179 1.00 13.14 ? 76  LYS   B C   1 
ATOM   1403 O O   . LYS   B 1 108 ? -37.815 11.045 -18.902 1.00 13.42 ? 76  LYS   B O   1 
ATOM   1404 C CB  . LYS   B 1 108 ? -35.738 13.197 -17.427 1.00 14.91 ? 76  LYS   B CB  1 
ATOM   1405 C CG  . LYS   B 1 108 ? -36.923 13.302 -16.479 1.00 17.70 ? 76  LYS   B CG  1 
ATOM   1406 C CD  . LYS   B 1 108 ? -36.837 14.584 -15.669 1.00 20.75 ? 76  LYS   B CD  1 
ATOM   1407 C CE  . LYS   B 1 108 ? -37.928 14.663 -14.623 1.00 24.98 ? 76  LYS   B CE  1 
ATOM   1408 N NZ  . LYS   B 1 108 ? -37.864 15.945 -13.864 1.00 28.12 ? 76  LYS   B NZ  1 
ATOM   1409 N N   . SER   B 1 109 ? -36.866 12.539 -20.291 1.00 12.93 ? 77  SER   B N   1 
ATOM   1410 C CA  . SER   B 1 109 ? -37.989 12.474 -21.222 1.00 14.26 ? 77  SER   B CA  1 
ATOM   1411 C C   . SER   B 1 109 ? -38.123 11.082 -21.815 1.00 14.85 ? 77  SER   B C   1 
ATOM   1412 O O   . SER   B 1 109 ? -39.238 10.612 -22.064 1.00 15.83 ? 77  SER   B O   1 
ATOM   1413 C CB  . SER   B 1 109 ? -37.831 13.520 -22.325 1.00 14.86 ? 77  SER   B CB  1 
ATOM   1414 O OG  . SER   B 1 109 ? -37.939 14.816 -21.779 1.00 16.69 ? 77  SER   B OG  1 
ATOM   1415 N N   . TYR   B 1 110 ? -36.991 10.417 -22.054 1.00 13.08 ? 78  TYR   B N   1 
ATOM   1416 C CA  . TYR   B 1 110 ? -37.014 9.065  -22.594 1.00 13.31 ? 78  TYR   B CA  1 
ATOM   1417 C C   . TYR   B 1 110 ? -37.757 8.118  -21.661 1.00 13.76 ? 78  TYR   B C   1 
ATOM   1418 O O   . TYR   B 1 110 ? -38.655 7.383  -22.091 1.00 15.19 ? 78  TYR   B O   1 
ATOM   1419 C CB  . TYR   B 1 110 ? -35.581 8.584  -22.830 1.00 13.59 ? 78  TYR   B CB  1 
ATOM   1420 C CG  . TYR   B 1 110 ? -35.523 7.182  -23.379 1.00 13.01 ? 78  TYR   B CG  1 
ATOM   1421 C CD1 . TYR   B 1 110 ? -35.780 6.939  -24.721 1.00 13.34 ? 78  TYR   B CD1 1 
ATOM   1422 C CD2 . TYR   B 1 110 ? -35.232 6.097  -22.555 1.00 12.93 ? 78  TYR   B CD2 1 
ATOM   1423 C CE1 . TYR   B 1 110 ? -35.732 5.653  -25.230 1.00 13.82 ? 78  TYR   B CE1 1 
ATOM   1424 C CE2 . TYR   B 1 110 ? -35.182 4.820  -23.059 1.00 13.77 ? 78  TYR   B CE2 1 
ATOM   1425 C CZ  . TYR   B 1 110 ? -35.450 4.602  -24.391 1.00 13.94 ? 78  TYR   B CZ  1 
ATOM   1426 O OH  . TYR   B 1 110 ? -35.399 3.336  -24.897 1.00 15.59 ? 78  TYR   B OH  1 
ATOM   1427 N N   . TRP   B 1 111 ? -37.400 8.129  -20.372 1.00 13.69 ? 79  TRP   B N   1 
ATOM   1428 C CA  . TRP   B 1 111 ? -38.041 7.222  -19.420 1.00 12.77 ? 79  TRP   B CA  1 
ATOM   1429 C C   . TRP   B 1 111 ? -39.496 7.598  -19.184 1.00 14.03 ? 79  TRP   B C   1 
ATOM   1430 O O   . TRP   B 1 111 ? -40.362 6.721  -19.082 1.00 15.20 ? 79  TRP   B O   1 
ATOM   1431 C CB  . TRP   B 1 111 ? -37.258 7.174  -18.100 1.00 12.59 ? 79  TRP   B CB  1 
ATOM   1432 C CG  . TRP   B 1 111 ? -35.917 6.546  -18.257 1.00 11.23 ? 79  TRP   B CG  1 
ATOM   1433 C CD1 . TRP   B 1 111 ? -34.707 7.139  -18.074 1.00 10.81 ? 79  TRP   B CD1 1 
ATOM   1434 C CD2 . TRP   B 1 111 ? -35.648 5.203  -18.695 1.00 11.59 ? 79  TRP   B CD2 1 
ATOM   1435 N NE1 . TRP   B 1 111 ? -33.697 6.244  -18.353 1.00 11.37 ? 79  TRP   B NE1 1 
ATOM   1436 C CE2 . TRP   B 1 111 ? -34.247 5.051  -18.737 1.00 11.42 ? 79  TRP   B CE2 1 
ATOM   1437 C CE3 . TRP   B 1 111 ? -36.456 4.113  -19.048 1.00 12.37 ? 79  TRP   B CE3 1 
ATOM   1438 C CZ2 . TRP   B 1 111 ? -33.637 3.854  -19.122 1.00 12.53 ? 79  TRP   B CZ2 1 
ATOM   1439 C CZ3 . TRP   B 1 111 ? -35.852 2.935  -19.431 1.00 13.10 ? 79  TRP   B CZ3 1 
ATOM   1440 C CH2 . TRP   B 1 111 ? -34.459 2.806  -19.461 1.00 13.12 ? 79  TRP   B CH2 1 
ATOM   1441 N N   . LYS   B 1 112 ? -39.784 8.894  -19.086 1.00 14.38 ? 80  LYS   B N   1 
ATOM   1442 C CA  . LYS   B 1 112 ? -41.155 9.322  -18.848 1.00 16.62 ? 80  LYS   B CA  1 
ATOM   1443 C C   . LYS   B 1 112 ? -42.072 8.874  -19.976 1.00 18.05 ? 80  LYS   B C   1 
ATOM   1444 O O   . LYS   B 1 112 ? -43.221 8.498  -19.731 1.00 19.44 ? 80  LYS   B O   1 
ATOM   1445 C CB  . LYS   B 1 112 ? -41.202 10.838 -18.647 1.00 19.08 ? 80  LYS   B CB  1 
ATOM   1446 C CG  . LYS   B 1 112 ? -40.820 11.258 -17.232 1.00 24.90 ? 80  LYS   B CG  1 
ATOM   1447 C CD  . LYS   B 1 112 ? -40.696 12.769 -17.081 1.00 30.02 ? 80  LYS   B CD  1 
ATOM   1448 C CE  . LYS   B 1 112 ? -41.036 13.199 -15.663 1.00 33.94 ? 80  LYS   B CE  1 
ATOM   1449 N NZ  . LYS   B 1 112 ? -40.460 12.273 -14.647 1.00 35.08 ? 80  LYS   B NZ  1 
ATOM   1450 N N   . ALA   B 1 113 ? -41.571 8.871  -21.214 1.00 18.10 ? 81  ALA   B N   1 
ATOM   1451 C CA  . ALA   B 1 113 ? -42.362 8.383  -22.340 1.00 20.48 ? 81  ALA   B CA  1 
ATOM   1452 C C   . ALA   B 1 113 ? -42.675 6.895  -22.231 1.00 20.59 ? 81  ALA   B C   1 
ATOM   1453 O O   . ALA   B 1 113 ? -43.646 6.429  -22.840 1.00 22.44 ? 81  ALA   B O   1 
ATOM   1454 C CB  . ALA   B 1 113 ? -41.636 8.681  -23.653 1.00 22.64 ? 81  ALA   B CB  1 
ATOM   1455 N N   . LEU   B 1 114 ? -41.879 6.143  -21.481 1.00 20.57 ? 82  LEU   B N   1 
ATOM   1456 C CA  . LEU   B 1 114 ? -42.136 4.737  -21.207 1.00 21.73 ? 82  LEU   B CA  1 
ATOM   1457 C C   . LEU   B 1 114 ? -42.889 4.521  -19.899 1.00 23.08 ? 82  LEU   B C   1 
ATOM   1458 O O   . LEU   B 1 114 ? -43.072 3.372  -19.484 1.00 25.03 ? 82  LEU   B O   1 
ATOM   1459 C CB  . LEU   B 1 114 ? -40.818 3.954  -21.194 1.00 22.35 ? 82  LEU   B CB  1 
ATOM   1460 C CG  . LEU   B 1 114 ? -39.998 4.008  -22.484 1.00 22.90 ? 82  LEU   B CG  1 
ATOM   1461 C CD1 . LEU   B 1 114 ? -38.630 3.368  -22.303 1.00 23.74 ? 82  LEU   B CD1 1 
ATOM   1462 C CD2 . LEU   B 1 114 ? -40.757 3.341  -23.619 1.00 25.36 ? 82  LEU   B CD2 1 
ATOM   1463 N N   . GLY   B 1 115 ? -43.338 5.594  -19.247 1.00 22.59 ? 83  GLY   B N   1 
ATOM   1464 C CA  . GLY   B 1 115 ? -44.090 5.450  -18.020 1.00 22.72 ? 83  GLY   B CA  1 
ATOM   1465 C C   . GLY   B 1 115 ? -43.253 5.126  -16.811 1.00 23.54 ? 83  GLY   B C   1 
ATOM   1466 O O   . GLY   B 1 115 ? -43.768 4.538  -15.852 1.00 25.23 ? 83  GLY   B O   1 
ATOM   1467 N N   . ILE   B 1 116 ? -41.970 5.471  -16.838 1.00 24.09 ? 84  ILE   B N   1 
ATOM   1468 C CA  . ILE   B 1 116 ? -41.041 5.195  -15.756 1.00 26.02 ? 84  ILE   B CA  1 
ATOM   1469 C C   . ILE   B 1 116 ? -40.557 6.528  -15.203 1.00 24.96 ? 84  ILE   B C   1 
ATOM   1470 O O   . ILE   B 1 116 ? -40.195 7.430  -15.970 1.00 24.75 ? 84  ILE   B O   1 
ATOM   1471 C CB  . ILE   B 1 116 ? -39.864 4.345  -16.264 1.00 27.27 ? 84  ILE   B CB  1 
ATOM   1472 C CG1 . ILE   B 1 116 ? -40.377 2.979  -16.738 1.00 27.85 ? 84  ILE   B CG1 1 
ATOM   1473 C CG2 . ILE   B 1 116 ? -38.811 4.203  -15.187 1.00 29.06 ? 84  ILE   B CG2 1 
ATOM   1474 C CD1 . ILE   B 1 116 ? -39.389 2.187  -17.577 1.00 28.42 ? 84  ILE   B CD1 1 
ATOM   1475 N N   . SER   B 1 117 ? -40.560 6.660  -13.878 1.00 24.74 ? 85  SER   B N   1 
ATOM   1476 C CA  . SER   B 1 117 ? -40.041 7.861  -13.243 1.00 23.66 ? 85  SER   B CA  1 
ATOM   1477 C C   . SER   B 1 117 ? -38.565 7.633  -12.950 1.00 21.74 ? 85  SER   B C   1 
ATOM   1478 O O   . SER   B 1 117 ? -38.239 6.858  -12.039 1.00 23.50 ? 85  SER   B O   1 
ATOM   1479 C CB  . SER   B 1 117 ? -40.796 8.153  -11.956 1.00 27.23 ? 85  SER   B CB  1 
ATOM   1480 O OG  . SER   B 1 117 ? -40.495 9.458  -11.492 1.00 30.87 ? 85  SER   B OG  1 
ATOM   1481 N N   . PRO   B 1 118 ? -37.655 8.277  -13.663 1.00 16.58 ? 86  PRO   B N   1 
ATOM   1482 C CA  . PRO   B 1 118 ? -36.234 7.984  -13.493 1.00 14.81 ? 86  PRO   B CA  1 
ATOM   1483 C C   . PRO   B 1 118 ? -35.597 8.873  -12.433 1.00 14.10 ? 86  PRO   B C   1 
ATOM   1484 O O   . PRO   B 1 118 ? -36.192 9.828  -11.926 1.00 16.55 ? 86  PRO   B O   1 
ATOM   1485 C CB  . PRO   B 1 118 ? -35.668 8.341  -14.867 1.00 15.53 ? 86  PRO   B CB  1 
ATOM   1486 C CG  . PRO   B 1 118 ? -36.502 9.521  -15.278 1.00 17.30 ? 86  PRO   B CG  1 
ATOM   1487 C CD  . PRO   B 1 118 ? -37.887 9.267  -14.728 1.00 17.73 ? 86  PRO   B CD  1 
ATOM   1488 N N   . PHE   B 1 119 ? -34.339 8.563  -12.140 1.00 13.04 ? 87  PHE   B N   1 
ATOM   1489 C CA  . PHE   B 1 119 ? -33.598 9.317  -11.140 1.00 12.77 ? 87  PHE   B CA  1 
ATOM   1490 C C   . PHE   B 1 119 ? -33.025 10.606 -11.714 1.00 11.69 ? 87  PHE   B C   1 
ATOM   1491 O O   . PHE   B 1 119 ? -33.210 11.682 -11.136 1.00 13.00 ? 87  PHE   B O   1 
ATOM   1492 C CB  . PHE   B 1 119 ? -32.468 8.458  -10.569 1.00 13.25 ? 87  PHE   B CB  1 
ATOM   1493 C CG  . PHE   B 1 119 ? -31.611 9.193  -9.589  1.00 13.77 ? 87  PHE   B CG  1 
ATOM   1494 C CD1 . PHE   B 1 119 ? -32.108 9.533  -8.335  1.00 15.46 ? 87  PHE   B CD1 1 
ATOM   1495 C CD2 . PHE   B 1 119 ? -30.318 9.568  -9.922  1.00 14.32 ? 87  PHE   B CD2 1 
ATOM   1496 C CE1 . PHE   B 1 119 ? -31.328 10.237 -7.428  1.00 16.80 ? 87  PHE   B CE1 1 
ATOM   1497 C CE2 . PHE   B 1 119 ? -29.527 10.258 -9.010  1.00 16.73 ? 87  PHE   B CE2 1 
ATOM   1498 C CZ  . PHE   B 1 119 ? -30.036 10.588 -7.767  1.00 17.25 ? 87  PHE   B CZ  1 
ATOM   1499 N N   . HIS   B 1 120 ? -32.321 10.525 -12.840 1.00 11.55 ? 88  HIS   B N   1 
ATOM   1500 C CA  . HIS   B 1 120 ? -31.553 11.665 -13.324 1.00 12.50 ? 88  HIS   B CA  1 
ATOM   1501 C C   . HIS   B 1 120 ? -32.417 12.631 -14.116 1.00 12.10 ? 88  HIS   B C   1 
ATOM   1502 O O   . HIS   B 1 120 ? -33.339 12.235 -14.830 1.00 13.19 ? 88  HIS   B O   1 
ATOM   1503 C CB  . HIS   B 1 120 ? -30.415 11.187 -14.221 1.00 13.20 ? 88  HIS   B CB  1 
ATOM   1504 C CG  . HIS   B 1 120 ? -29.484 10.232 -13.552 1.00 13.33 ? 88  HIS   B CG  1 
ATOM   1505 N ND1 . HIS   B 1 120 ? -29.676 8.870  -13.585 1.00 12.69 ? 88  HIS   B ND1 1 
ATOM   1506 C CD2 . HIS   B 1 120 ? -28.359 10.437 -12.828 1.00 16.33 ? 88  HIS   B CD2 1 
ATOM   1507 C CE1 . HIS   B 1 120 ? -28.705 8.272  -12.917 1.00 14.79 ? 88  HIS   B CE1 1 
ATOM   1508 N NE2 . HIS   B 1 120 ? -27.889 9.202  -12.453 1.00 16.81 ? 88  HIS   B NE2 1 
ATOM   1509 N N   . GLU   B 1 121 ? -32.089 13.917 -14.002 1.00 11.59 ? 89  GLU   B N   1 
ATOM   1510 C CA  . GLU   B 1 121 ? -32.699 14.908 -14.886 1.00 13.36 ? 89  GLU   B CA  1 
ATOM   1511 C C   . GLU   B 1 121 ? -32.210 14.736 -16.312 1.00 13.63 ? 89  GLU   B C   1 
ATOM   1512 O O   . GLU   B 1 121 ? -32.967 14.931 -17.270 1.00 15.62 ? 89  GLU   B O   1 
ATOM   1513 C CB  . GLU   B 1 121 ? -32.366 16.318 -14.405 1.00 15.13 ? 89  GLU   B CB  1 
ATOM   1514 C CG  . GLU   B 1 121 ? -33.112 16.692 -13.167 1.00 17.38 ? 89  GLU   B CG  1 
ATOM   1515 C CD  . GLU   B 1 121 ? -34.599 16.786 -13.430 1.00 19.49 ? 89  GLU   B CD  1 
ATOM   1516 O OE1 . GLU   B 1 121 ? -35.011 17.600 -14.287 1.00 22.07 ? 89  GLU   B OE1 1 
ATOM   1517 O OE2 . GLU   B 1 121 ? -35.355 16.034 -12.794 1.00 20.73 ? 89  GLU   B OE2 1 
ATOM   1518 N N   . HIS   B 1 122 ? -30.941 14.400 -16.467 1.00 13.25 ? 90  HIS   B N   1 
ATOM   1519 C CA  . HIS   B 1 122 ? -30.326 14.194 -17.767 1.00 14.18 ? 90  HIS   B CA  1 
ATOM   1520 C C   . HIS   B 1 122 ? -28.999 13.522 -17.477 1.00 15.61 ? 90  HIS   B C   1 
ATOM   1521 O O   . HIS   B 1 122 ? -28.563 13.465 -16.326 1.00 17.38 ? 90  HIS   B O   1 
ATOM   1522 C CB  . HIS   B 1 122 ? -30.159 15.510 -18.545 1.00 17.83 ? 90  HIS   B CB  1 
ATOM   1523 C CG  . HIS   B 1 122 ? -29.380 16.568 -17.824 1.00 22.67 ? 90  HIS   B CG  1 
ATOM   1524 N ND1 . HIS   B 1 122 ? -29.981 17.553 -17.070 1.00 25.31 ? 90  HIS   B ND1 1 
ATOM   1525 C CD2 . HIS   B 1 122 ? -28.051 16.820 -17.778 1.00 24.94 ? 90  HIS   B CD2 1 
ATOM   1526 C CE1 . HIS   B 1 122 ? -29.054 18.358 -16.579 1.00 26.78 ? 90  HIS   B CE1 1 
ATOM   1527 N NE2 . HIS   B 1 122 ? -27.873 17.938 -16.997 1.00 26.93 ? 90  HIS   B NE2 1 
ATOM   1528 N N   . ALA   B 1 123 ? -28.387 12.973 -18.519 1.00 16.86 ? 91  ALA   B N   1 
ATOM   1529 C CA  . ALA   B 1 123 ? -27.050 12.405 -18.429 1.00 19.97 ? 91  ALA   B CA  1 
ATOM   1530 C C   . ALA   B 1 123 ? -26.103 13.412 -19.051 1.00 20.43 ? 91  ALA   B C   1 
ATOM   1531 O O   . ALA   B 1 123 ? -26.303 13.829 -20.197 1.00 21.92 ? 91  ALA   B O   1 
ATOM   1532 C CB  . ALA   B 1 123 ? -26.967 11.073 -19.171 1.00 21.91 ? 91  ALA   B CB  1 
ATOM   1533 N N   . GLU   B 1 124 ? -25.084 13.808 -18.300 1.00 20.86 ? 92  GLU   B N   1 
ATOM   1534 C CA  . GLU   B 1 124 ? -24.130 14.808 -18.747 1.00 21.55 ? 92  GLU   B CA  1 
ATOM   1535 C C   . GLU   B 1 124 ? -22.785 14.144 -19.002 1.00 20.41 ? 92  GLU   B C   1 
ATOM   1536 O O   . GLU   B 1 124 ? -22.328 13.309 -18.210 1.00 23.76 ? 92  GLU   B O   1 
ATOM   1537 C CB  . GLU   B 1 124 ? -23.952 15.902 -17.695 1.00 23.94 ? 92  GLU   B CB  1 
ATOM   1538 N N   . VAL   B 1 125 ? -22.152 14.510 -20.113 1.00 15.38 ? 93  VAL   B N   1 
ATOM   1539 C CA  . VAL   B 1 125 ? -20.830 14.012 -20.453 1.00 14.20 ? 93  VAL   B CA  1 
ATOM   1540 C C   . VAL   B 1 125 ? -19.977 15.233 -20.767 1.00 12.43 ? 93  VAL   B C   1 
ATOM   1541 O O   . VAL   B 1 125 ? -20.219 15.920 -21.765 1.00 13.45 ? 93  VAL   B O   1 
ATOM   1542 C CB  . VAL   B 1 125 ? -20.869 13.041 -21.641 1.00 16.35 ? 93  VAL   B CB  1 
ATOM   1543 C CG1 . VAL   B 1 125 ? -19.492 12.417 -21.859 1.00 16.99 ? 93  VAL   B CG1 1 
ATOM   1544 C CG2 . VAL   B 1 125 ? -21.946 11.965 -21.434 1.00 17.84 ? 93  VAL   B CG2 1 
ATOM   1545 N N   . VAL   B 1 126 ? -18.993 15.516 -19.914 1.00 11.57 ? 94  VAL   B N   1 
ATOM   1546 C CA  . VAL   B 1 126 ? -18.163 16.711 -20.025 1.00 11.41 ? 94  VAL   B CA  1 
ATOM   1547 C C   . VAL   B 1 126 ? -16.719 16.267 -20.226 1.00 11.52 ? 94  VAL   B C   1 
ATOM   1548 O O   . VAL   B 1 126 ? -16.190 15.485 -19.427 1.00 12.43 ? 94  VAL   B O   1 
ATOM   1549 C CB  . VAL   B 1 126 ? -18.304 17.608 -18.776 1.00 12.45 ? 94  VAL   B CB  1 
ATOM   1550 C CG1 . VAL   B 1 126 ? -17.509 18.896 -18.938 1.00 13.76 ? 94  VAL   B CG1 1 
ATOM   1551 C CG2 . VAL   B 1 126 ? -19.784 17.937 -18.499 1.00 14.92 ? 94  VAL   B CG2 1 
ATOM   1552 N N   . PHE   B 1 127 ? -16.082 16.768 -21.282 1.00 11.54 ? 95  PHE   B N   1 
ATOM   1553 C CA  . PHE   B 1 127 ? -14.765 16.276 -21.665 1.00 11.18 ? 95  PHE   B CA  1 
ATOM   1554 C C   . PHE   B 1 127 ? -14.034 17.338 -22.471 1.00 12.11 ? 95  PHE   B C   1 
ATOM   1555 O O   . PHE   B 1 127 ? -14.651 18.120 -23.188 1.00 12.92 ? 95  PHE   B O   1 
ATOM   1556 C CB  . PHE   B 1 127 ? -14.895 14.989 -22.494 1.00 11.32 ? 95  PHE   B CB  1 
ATOM   1557 C CG  . PHE   B 1 127 ? -15.667 15.158 -23.791 1.00 12.84 ? 95  PHE   B CG  1 
ATOM   1558 C CD1 . PHE   B 1 127 ? -17.051 15.170 -23.791 1.00 14.41 ? 95  PHE   B CD1 1 
ATOM   1559 C CD2 . PHE   B 1 127 ? -15.006 15.276 -25.002 1.00 14.07 ? 95  PHE   B CD2 1 
ATOM   1560 C CE1 . PHE   B 1 127 ? -17.769 15.311 -24.979 1.00 16.53 ? 95  PHE   B CE1 1 
ATOM   1561 C CE2 . PHE   B 1 127 ? -15.718 15.415 -26.199 1.00 16.28 ? 95  PHE   B CE2 1 
ATOM   1562 C CZ  . PHE   B 1 127 ? -17.099 15.443 -26.178 1.00 17.54 ? 95  PHE   B CZ  1 
ATOM   1563 N N   . THR   B 1 128 ? -12.709 17.338 -22.370 1.00 13.49 ? 96  THR   B N   1 
ATOM   1564 C CA  . THR   B 1 128 ? -11.889 18.117 -23.285 1.00 14.06 ? 96  THR   B CA  1 
ATOM   1565 C C   . THR   B 1 128 ? -11.686 17.322 -24.568 1.00 14.77 ? 96  THR   B C   1 
ATOM   1566 O O   . THR   B 1 128 ? -11.448 16.114 -24.539 1.00 16.87 ? 96  THR   B O   1 
ATOM   1567 C CB  . THR   B 1 128 ? -10.532 18.429 -22.649 1.00 16.11 ? 96  THR   B CB  1 
ATOM   1568 O OG1 . THR   B 1 128 ? -10.724 19.239 -21.482 1.00 16.71 ? 96  THR   B OG1 1 
ATOM   1569 C CG2 . THR   B 1 128 ? -9.629  19.181 -23.624 1.00 16.15 ? 96  THR   B CG2 1 
ATOM   1570 N N   . ALA   B 1 129 ? -11.820 17.997 -25.696 1.00 13.62 ? 97  ALA   B N   1 
ATOM   1571 C CA  . ALA   B 1 129 ? -11.665 17.372 -26.995 1.00 13.91 ? 97  ALA   B CA  1 
ATOM   1572 C C   . ALA   B 1 129 ? -10.684 18.181 -27.825 1.00 15.62 ? 97  ALA   B C   1 
ATOM   1573 O O   . ALA   B 1 129 ? -10.588 19.409 -27.691 1.00 15.74 ? 97  ALA   B O   1 
ATOM   1574 C CB  . ALA   B 1 129 ? -13.007 17.294 -27.734 1.00 16.31 ? 97  ALA   B CB  1 
ATOM   1575 N N   . ASN   B 1 130 ? -9.941  17.470 -28.673 1.00 15.49 ? 98  ASN   B N   1 
ATOM   1576 C CA  . ASN   B 1 130 ? -9.072  18.044 -29.699 1.00 15.68 ? 98  ASN   B CA  1 
ATOM   1577 C C   . ASN   B 1 130 ? -7.884  18.823 -29.144 1.00 17.39 ? 98  ASN   B C   1 
ATOM   1578 O O   . ASN   B 1 130 ? -7.285  19.629 -29.867 1.00 17.90 ? 98  ASN   B O   1 
ATOM   1579 C CB  . ASN   B 1 130 ? -9.852  18.883 -30.716 1.00 16.13 ? 98  ASN   B CB  1 
ATOM   1580 C CG  . ASN   B 1 130 ? -11.038 18.138 -31.267 1.00 16.76 ? 98  ASN   B CG  1 
ATOM   1581 O OD1 . ASN   B 1 130 ? -10.884 17.128 -31.952 1.00 18.18 ? 98  ASN   B OD1 1 
ATOM   1582 N ND2 . ASN   B 1 130 ? -12.231 18.614 -30.953 1.00 16.91 ? 98  ASN   B ND2 1 
ATOM   1583 N N   . ASP   B 1 131 ? -7.503  18.604 -27.884 1.00 21.61 ? 99  ASP   B N   1 
ATOM   1584 C CA  . ASP   B 1 131 ? -6.370  19.358 -27.352 1.00 28.88 ? 99  ASP   B CA  1 
ATOM   1585 C C   . ASP   B 1 131 ? -5.041  18.914 -27.954 1.00 28.91 ? 99  ASP   B C   1 
ATOM   1586 O O   . ASP   B 1 131 ? -4.066  19.668 -27.889 1.00 31.07 ? 99  ASP   B O   1 
ATOM   1587 C CB  . ASP   B 1 131 ? -6.351  19.359 -25.818 1.00 35.99 ? 99  ASP   B CB  1 
ATOM   1588 C CG  . ASP   B 1 131 ? -5.980  18.013 -25.228 1.00 42.56 ? 99  ASP   B CG  1 
ATOM   1589 O OD1 . ASP   B 1 131 ? -6.344  16.976 -25.819 1.00 45.35 ? 99  ASP   B OD1 1 
ATOM   1590 O OD2 . ASP   B 1 131 ? -5.331  17.992 -24.160 1.00 45.00 ? 99  ASP   B OD2 1 
ATOM   1591 N N   . SER   B 1 132 ? -4.978  17.712 -28.530 1.00 24.98 ? 100 SER   B N   1 
ATOM   1592 C CA  . SER   B 1 132 ? -3.823  17.257 -29.294 1.00 24.51 ? 100 SER   B CA  1 
ATOM   1593 C C   . SER   B 1 132 ? -4.112  17.234 -30.792 1.00 21.07 ? 100 SER   B C   1 
ATOM   1594 O O   . SER   B 1 132 ? -3.556  16.413 -31.527 1.00 20.32 ? 100 SER   B O   1 
ATOM   1595 C CB  . SER   B 1 132 ? -3.365  15.884 -28.812 1.00 26.64 ? 100 SER   B CB  1 
ATOM   1596 O OG  . SER   B 1 132 ? -2.947  15.945 -27.459 1.00 28.43 ? 100 SER   B OG  1 
ATOM   1597 N N   . GLY   B 1 133 ? -4.975  18.136 -31.253 1.00 19.42 ? 101 GLY   B N   1 
ATOM   1598 C CA  . GLY   B 1 133 ? -5.432  18.130 -32.622 1.00 20.32 ? 101 GLY   B CA  1 
ATOM   1599 C C   . GLY   B 1 133 ? -6.627  17.216 -32.812 1.00 18.95 ? 101 GLY   B C   1 
ATOM   1600 O O   . GLY   B 1 133 ? -7.089  16.552 -31.874 1.00 19.00 ? 101 GLY   B O   1 
ATOM   1601 N N   . PRO   B 1 134 ? -7.136  17.145 -34.043 1.00 19.69 ? 102 PRO   B N   1 
ATOM   1602 C CA  . PRO   B 1 134 ? -8.352  16.361 -34.298 1.00 19.73 ? 102 PRO   B CA  1 
ATOM   1603 C C   . PRO   B 1 134 ? -8.262  14.919 -33.825 1.00 19.12 ? 102 PRO   B C   1 
ATOM   1604 O O   . PRO   B 1 134 ? -7.245  14.240 -33.988 1.00 19.46 ? 102 PRO   B O   1 
ATOM   1605 C CB  . PRO   B 1 134 ? -8.503  16.422 -35.822 1.00 22.02 ? 102 PRO   B CB  1 
ATOM   1606 C CG  . PRO   B 1 134 ? -7.795  17.650 -36.218 1.00 23.73 ? 102 PRO   B CG  1 
ATOM   1607 C CD  . PRO   B 1 134 ? -6.658  17.831 -35.255 1.00 21.42 ? 102 PRO   B CD  1 
ATOM   1608 N N   . ARG   B 1 135 ? -9.365  14.460 -33.242 1.00 17.92 ? 103 ARG   B N   1 
ATOM   1609 C CA  . ARG   B 1 135 ? -9.633  13.052 -32.997 1.00 18.49 ? 103 ARG   B CA  1 
ATOM   1610 C C   . ARG   B 1 135 ? -11.091 12.795 -33.345 1.00 18.18 ? 103 ARG   B C   1 
ATOM   1611 O O   . ARG   B 1 135 ? -11.898 13.726 -33.469 1.00 19.00 ? 103 ARG   B O   1 
ATOM   1612 C CB  . ARG   B 1 135 ? -9.427  12.667 -31.524 1.00 19.17 ? 103 ARG   B CB  1 
ATOM   1613 C CG  . ARG   B 1 135 ? -8.020  12.820 -30.996 1.00 18.97 ? 103 ARG   B CG  1 
ATOM   1614 C CD  . ARG   B 1 135 ? -7.039  11.899 -31.710 1.00 20.87 ? 103 ARG   B CD  1 
ATOM   1615 N NE  . ARG   B 1 135 ? -5.740  11.909 -31.046 1.00 21.46 ? 103 ARG   B NE  1 
ATOM   1616 C CZ  . ARG   B 1 135 ? -4.837  12.879 -31.168 1.00 22.11 ? 103 ARG   B CZ  1 
ATOM   1617 N NH1 . ARG   B 1 135 ? -5.080  13.923 -31.949 1.00 21.78 ? 103 ARG   B NH1 1 
ATOM   1618 N NH2 . ARG   B 1 135 ? -3.684  12.799 -30.514 1.00 23.04 ? 103 ARG   B NH2 1 
ATOM   1619 N N   . ARG   B 1 136 ? -11.432 11.514 -33.477 1.00 17.76 ? 104 ARG   B N   1 
ATOM   1620 C CA  . ARG   B 1 136 ? -12.811 11.072 -33.649 1.00 17.68 ? 104 ARG   B CA  1 
ATOM   1621 C C   . ARG   B 1 136 ? -13.315 10.508 -32.327 1.00 17.57 ? 104 ARG   B C   1 
ATOM   1622 O O   . ARG   B 1 136 ? -12.627 9.708  -31.684 1.00 18.18 ? 104 ARG   B O   1 
ATOM   1623 C CB  . ARG   B 1 136 ? -12.906 9.992  -34.726 1.00 19.43 ? 104 ARG   B CB  1 
ATOM   1624 N N   . TYR   B 1 137 ? -14.512 10.924 -31.926 1.00 15.17 ? 105 TYR   B N   1 
ATOM   1625 C CA  . TYR   B 1 137 ? -15.054 10.599 -30.614 1.00 14.21 ? 105 TYR   B CA  1 
ATOM   1626 C C   . TYR   B 1 137 ? -16.390 9.895  -30.780 1.00 14.31 ? 105 TYR   B C   1 
ATOM   1627 O O   . TYR   B 1 137 ? -17.287 10.416 -31.453 1.00 15.54 ? 105 TYR   B O   1 
ATOM   1628 C CB  . TYR   B 1 137 ? -15.271 11.876 -29.791 1.00 15.40 ? 105 TYR   B CB  1 
ATOM   1629 C CG  . TYR   B 1 137 ? -13.996 12.623 -29.470 1.00 16.13 ? 105 TYR   B CG  1 
ATOM   1630 C CD1 . TYR   B 1 137 ? -13.443 13.514 -30.382 1.00 17.43 ? 105 TYR   B CD1 1 
ATOM   1631 C CD2 . TYR   B 1 137 ? -13.352 12.445 -28.258 1.00 15.88 ? 105 TYR   B CD2 1 
ATOM   1632 C CE1 . TYR   B 1 137 ? -12.268 14.189 -30.097 1.00 16.73 ? 105 TYR   B CE1 1 
ATOM   1633 C CE2 . TYR   B 1 137 ? -12.175 13.119 -27.965 1.00 16.95 ? 105 TYR   B CE2 1 
ATOM   1634 C CZ  . TYR   B 1 137 ? -11.643 13.992 -28.886 1.00 16.60 ? 105 TYR   B CZ  1 
ATOM   1635 O OH  . TYR   B 1 137 ? -10.466 14.648 -28.589 1.00 17.83 ? 105 TYR   B OH  1 
ATOM   1636 N N   . THR   B 1 138 ? -16.524 8.720  -30.166 1.00 13.62 ? 106 THR   B N   1 
ATOM   1637 C CA  . THR   B 1 138 ? -17.819 8.075  -29.979 1.00 13.66 ? 106 THR   B CA  1 
ATOM   1638 C C   . THR   B 1 138 ? -18.122 8.072  -28.488 1.00 13.31 ? 106 THR   B C   1 
ATOM   1639 O O   . THR   B 1 138 ? -17.325 7.569  -27.690 1.00 14.09 ? 106 THR   B O   1 
ATOM   1640 C CB  . THR   B 1 138 ? -17.843 6.651  -30.537 1.00 15.48 ? 106 THR   B CB  1 
ATOM   1641 O OG1 . THR   B 1 138 ? -17.719 6.695  -31.962 1.00 18.18 ? 106 THR   B OG1 1 
ATOM   1642 C CG2 . THR   B 1 138 ? -19.143 5.958  -30.183 1.00 17.60 ? 106 THR   B CG2 1 
ATOM   1643 N N   . ILE   B 1 139 ? -19.252 8.663  -28.114 1.00 13.03 ? 107 ILE   B N   1 
ATOM   1644 C CA  . ILE   B 1 139 ? -19.729 8.676  -26.737 1.00 13.22 ? 107 ILE   B CA  1 
ATOM   1645 C C   . ILE   B 1 139 ? -20.880 7.688  -26.669 1.00 12.50 ? 107 ILE   B C   1 
ATOM   1646 O O   . ILE   B 1 139 ? -21.888 7.861  -27.360 1.00 13.53 ? 107 ILE   B O   1 
ATOM   1647 C CB  . ILE   B 1 139 ? -20.231 10.076 -26.344 1.00 16.55 ? 107 ILE   B CB  1 
ATOM   1648 C CG1 . ILE   B 1 139 ? -19.144 11.138 -26.538 1.00 20.17 ? 107 ILE   B CG1 1 
ATOM   1649 C CG2 . ILE   B 1 139 ? -20.797 10.061 -24.922 1.00 16.86 ? 107 ILE   B CG2 1 
ATOM   1650 C CD1 . ILE   B 1 139 ? -17.940 10.927 -25.693 1.00 22.24 ? 107 ILE   B CD1 1 
ATOM   1651 N N   . ALA   B 1 140 ? -20.748 6.655  -25.849 1.00 12.13 ? 108 ALA   B N   1 
ATOM   1652 C CA  . ALA   B 1 140 ? -21.816 5.688  -25.637 1.00 12.48 ? 108 ALA   B CA  1 
ATOM   1653 C C   . ALA   B 1 140 ? -22.444 5.936  -24.273 1.00 12.54 ? 108 ALA   B C   1 
ATOM   1654 O O   . ALA   B 1 140 ? -21.740 6.207  -23.297 1.00 14.45 ? 108 ALA   B O   1 
ATOM   1655 C CB  . ALA   B 1 140 ? -21.276 4.255  -25.703 1.00 13.75 ? 108 ALA   B CB  1 
ATOM   1656 N N   . ALA   B 1 141 ? -23.765 5.863  -24.212 1.00 11.37 ? 109 ALA   B N   1 
ATOM   1657 C CA  . ALA   B 1 141 ? -24.488 5.977  -22.956 1.00 12.01 ? 109 ALA   B CA  1 
ATOM   1658 C C   . ALA   B 1 141 ? -25.416 4.782  -22.839 1.00 11.56 ? 109 ALA   B C   1 
ATOM   1659 O O   . ALA   B 1 141 ? -26.196 4.503  -23.756 1.00 13.25 ? 109 ALA   B O   1 
ATOM   1660 C CB  . ALA   B 1 141 ? -25.310 7.263  -22.907 1.00 13.54 ? 109 ALA   B CB  1 
ATOM   1661 N N   . LEU   B 1 142 ? -25.336 4.093  -21.709 1.00 11.26 ? 110 LEU   B N   1 
ATOM   1662 C CA  . LEU   B 1 142 ? -26.116 2.894  -21.429 1.00 10.52 ? 110 LEU   B CA  1 
ATOM   1663 C C   . LEU   B 1 142 ? -27.060 3.256  -20.293 1.00 10.96 ? 110 LEU   B C   1 
ATOM   1664 O O   . LEU   B 1 142 ? -26.610 3.524  -19.173 1.00 12.33 ? 110 LEU   B O   1 
ATOM   1665 C CB  . LEU   B 1 142 ? -25.162 1.782  -21.013 1.00 14.69 ? 110 LEU   B CB  1 
ATOM   1666 C CG  . LEU   B 1 142 ? -25.762 0.481  -20.539 1.00 19.13 ? 110 LEU   B CG  1 
ATOM   1667 C CD1 . LEU   B 1 142 ? -26.565 -0.133 -21.664 1.00 20.70 ? 110 LEU   B CD1 1 
ATOM   1668 C CD2 . LEU   B 1 142 ? -24.615 -0.398 -20.124 1.00 21.63 ? 110 LEU   B CD2 1 
ATOM   1669 N N   . LEU   B 1 143 ? -28.363 3.271  -20.579 1.00 10.61 ? 111 LEU   B N   1 
ATOM   1670 C CA  . LEU   B 1 143 ? -29.353 3.901  -19.713 1.00 11.28 ? 111 LEU   B CA  1 
ATOM   1671 C C   . LEU   B 1 143 ? -30.198 2.898  -18.948 1.00 9.87  ? 111 LEU   B C   1 
ATOM   1672 O O   . LEU   B 1 143 ? -30.767 1.974  -19.538 1.00 10.56 ? 111 LEU   B O   1 
ATOM   1673 C CB  . LEU   B 1 143 ? -30.304 4.766  -20.532 1.00 11.29 ? 111 LEU   B CB  1 
ATOM   1674 C CG  . LEU   B 1 143 ? -29.715 5.861  -21.403 1.00 12.11 ? 111 LEU   B CG  1 
ATOM   1675 C CD1 . LEU   B 1 143 ? -30.869 6.702  -21.950 1.00 13.01 ? 111 LEU   B CD1 1 
ATOM   1676 C CD2 . LEU   B 1 143 ? -28.715 6.694  -20.619 1.00 11.75 ? 111 LEU   B CD2 1 
ATOM   1677 N N   . SER   B 1 144 ? -30.349 3.144  -17.658 1.00 11.24 ? 112 SER   B N   1 
ATOM   1678 C CA  . SER   B 1 144 ? -31.343 2.507  -16.810 1.00 10.77 ? 112 SER   B CA  1 
ATOM   1679 C C   . SER   B 1 144 ? -32.036 3.602  -16.016 1.00 10.36 ? 112 SER   B C   1 
ATOM   1680 O O   . SER   B 1 144 ? -31.512 4.711  -15.888 1.00 11.32 ? 112 SER   B O   1 
ATOM   1681 C CB  . SER   B 1 144 ? -30.697 1.504  -15.843 1.00 11.81 ? 112 SER   B CB  1 
ATOM   1682 O OG  . SER   B 1 144 ? -29.994 0.508  -16.560 1.00 12.94 ? 112 SER   B OG  1 
ATOM   1683 N N   . PRO   B 1 145 ? -33.212 3.326  -15.458 1.00 11.14 ? 113 PRO   B N   1 
ATOM   1684 C CA  . PRO   B 1 145 ? -33.923 4.414  -14.761 1.00 10.63 ? 113 PRO   B CA  1 
ATOM   1685 C C   . PRO   B 1 145 ? -33.143 5.047  -13.617 1.00 10.50 ? 113 PRO   B C   1 
ATOM   1686 O O   . PRO   B 1 145 ? -33.228 6.266  -13.425 1.00 11.27 ? 113 PRO   B O   1 
ATOM   1687 C CB  . PRO   B 1 145 ? -35.212 3.727  -14.297 1.00 11.45 ? 113 PRO   B CB  1 
ATOM   1688 C CG  . PRO   B 1 145 ? -35.475 2.743  -15.389 1.00 12.66 ? 113 PRO   B CG  1 
ATOM   1689 C CD  . PRO   B 1 145 ? -34.103 2.182  -15.714 1.00 12.42 ? 113 PRO   B CD  1 
ATOM   1690 N N   . TYR   B 1 146 ? -32.383 4.269  -12.846 1.00 10.12 ? 114 TYR   B N   1 
ATOM   1691 C CA  . TYR   B 1 146 ? -31.652 4.793  -11.698 1.00 10.93 ? 114 TYR   B CA  1 
ATOM   1692 C C   . TYR   B 1 146 ? -30.147 4.671  -11.864 1.00 10.86 ? 114 TYR   B C   1 
ATOM   1693 O O   . TYR   B 1 146 ? -29.411 4.750  -10.877 1.00 13.10 ? 114 TYR   B O   1 
ATOM   1694 C CB  . TYR   B 1 146 ? -32.121 4.146  -10.392 1.00 12.34 ? 114 TYR   B CB  1 
ATOM   1695 C CG  . TYR   B 1 146 ? -33.378 4.780  -9.860  1.00 12.90 ? 114 TYR   B CG  1 
ATOM   1696 C CD1 . TYR   B 1 146 ? -34.596 4.585  -10.492 1.00 16.92 ? 114 TYR   B CD1 1 
ATOM   1697 C CD2 . TYR   B 1 146 ? -33.345 5.595  -8.740  1.00 13.92 ? 114 TYR   B CD2 1 
ATOM   1698 C CE1 . TYR   B 1 146 ? -35.745 5.179  -10.018 1.00 20.06 ? 114 TYR   B CE1 1 
ATOM   1699 C CE2 . TYR   B 1 146 ? -34.482 6.190  -8.262  1.00 17.21 ? 114 TYR   B CE2 1 
ATOM   1700 C CZ  . TYR   B 1 146 ? -35.679 5.977  -8.904  1.00 20.39 ? 114 TYR   B CZ  1 
ATOM   1701 O OH  . TYR   B 1 146 ? -36.825 6.567  -8.433  1.00 25.23 ? 114 TYR   B OH  1 
ATOM   1702 N N   . SER   B 1 147 ? -29.670 4.479  -13.092 1.00 10.67 ? 115 SER   B N   1 
ATOM   1703 C CA  . SER   B 1 147 ? -28.244 4.304  -13.318 1.00 11.36 ? 115 SER   B CA  1 
ATOM   1704 C C   . SER   B 1 147 ? -27.938 4.573  -14.775 1.00 11.55 ? 115 SER   B C   1 
ATOM   1705 O O   . SER   B 1 147 ? -28.722 4.220  -15.649 1.00 13.87 ? 115 SER   B O   1 
ATOM   1706 C CB  . SER   B 1 147 ? -27.839 2.861  -12.980 1.00 12.48 ? 115 SER   B CB  1 
ATOM   1707 O OG  . SER   B 1 147 ? -26.447 2.652  -13.131 1.00 14.17 ? 115 SER   B OG  1 
ATOM   1708 N N   . TYR   B 1 148 ? -26.802 5.201  -15.040 1.00 11.08 ? 116 TYR   B N   1 
ATOM   1709 C CA  . TYR   B 1 148 ? -26.307 5.201  -16.407 1.00 12.41 ? 116 TYR   B CA  1 
ATOM   1710 C C   . TYR   B 1 148 ? -24.797 5.074  -16.409 1.00 12.01 ? 116 TYR   B C   1 
ATOM   1711 O O   . TYR   B 1 148 ? -24.115 5.445  -15.454 1.00 12.17 ? 116 TYR   B O   1 
ATOM   1712 C CB  . TYR   B 1 148 ? -26.766 6.401  -17.249 1.00 15.15 ? 116 TYR   B CB  1 
ATOM   1713 C CG  . TYR   B 1 148 ? -26.166 7.714  -16.842 1.00 17.10 ? 116 TYR   B CG  1 
ATOM   1714 C CD1 . TYR   B 1 148 ? -24.952 8.140  -17.364 1.00 18.61 ? 116 TYR   B CD1 1 
ATOM   1715 C CD2 . TYR   B 1 148 ? -26.822 8.539  -15.950 1.00 20.16 ? 116 TYR   B CD2 1 
ATOM   1716 C CE1 . TYR   B 1 148 ? -24.407 9.344  -16.998 1.00 20.74 ? 116 TYR   B CE1 1 
ATOM   1717 C CE2 . TYR   B 1 148 ? -26.290 9.738  -15.580 1.00 22.97 ? 116 TYR   B CE2 1 
ATOM   1718 C CZ  . TYR   B 1 148 ? -25.085 10.139 -16.104 1.00 23.19 ? 116 TYR   B CZ  1 
ATOM   1719 O OH  . TYR   B 1 148 ? -24.559 11.346 -15.727 1.00 26.90 ? 116 TYR   B OH  1 
ATOM   1720 N N   . SER   B 1 149 ? -24.287 4.530  -17.494 1.00 11.82 ? 117 SER   B N   1 
ATOM   1721 C CA  . SER   B 1 149 ? -22.861 4.493  -17.719 1.00 13.62 ? 117 SER   B CA  1 
ATOM   1722 C C   . SER   B 1 149 ? -22.565 5.205  -19.023 1.00 11.84 ? 117 SER   B C   1 
ATOM   1723 O O   . SER   B 1 149 ? -23.386 5.237  -19.947 1.00 12.72 ? 117 SER   B O   1 
ATOM   1724 C CB  . SER   B 1 149 ? -22.318 3.070  -17.730 1.00 19.51 ? 117 SER   B CB  1 
ATOM   1725 O OG  . SER   B 1 149 ? -22.455 2.491  -18.999 1.00 22.73 ? 117 SER   B OG  1 
ATOM   1726 N N   . THR   B 1 150 ? -21.394 5.802  -19.080 1.00 12.62 ? 118 THR   B N   1 
ATOM   1727 C CA  . THR   B 1 150 ? -20.972 6.444  -20.302 1.00 12.93 ? 118 THR   B CA  1 
ATOM   1728 C C   . THR   B 1 150 ? -19.519 6.114  -20.559 1.00 13.26 ? 118 THR   B C   1 
ATOM   1729 O O   . THR   B 1 150 ? -18.711 6.059  -19.629 1.00 14.51 ? 118 THR   B O   1 
ATOM   1730 C CB  . THR   B 1 150 ? -21.239 7.950  -20.286 1.00 14.13 ? 118 THR   B CB  1 
ATOM   1731 O OG1 . THR   B 1 150 ? -20.950 8.465  -21.580 1.00 16.16 ? 118 THR   B OG1 1 
ATOM   1732 C CG2 . THR   B 1 150 ? -20.397 8.677  -19.242 1.00 14.73 ? 118 THR   B CG2 1 
ATOM   1733 N N   . THR   B 1 151 ? -19.212 5.838  -21.814 1.00 12.62 ? 119 THR   B N   1 
ATOM   1734 C CA  . THR   B 1 151 ? -17.868 5.464  -22.207 1.00 12.29 ? 119 THR   B CA  1 
ATOM   1735 C C   . THR   B 1 151 ? -17.521 6.225  -23.470 1.00 11.99 ? 119 THR   B C   1 
ATOM   1736 O O   . THR   B 1 151 ? -18.395 6.564  -24.266 1.00 14.36 ? 119 THR   B O   1 
ATOM   1737 C CB  . THR   B 1 151 ? -17.777 3.957  -22.459 1.00 14.79 ? 119 THR   B CB  1 
ATOM   1738 O OG1 . THR   B 1 151 ? -18.386 3.263  -21.364 1.00 16.64 ? 119 THR   B OG1 1 
ATOM   1739 C CG2 . THR   B 1 151 ? -16.308 3.532  -22.598 1.00 17.49 ? 119 THR   B CG2 1 
ATOM   1740 N N   . ALA   B 1 152 ? -16.242 6.515  -23.633 1.00 11.09 ? 120 ALA   B N   1 
ATOM   1741 C CA  . ALA   B 1 152 ? -15.759 7.166  -24.832 1.00 12.05 ? 120 ALA   B CA  1 
ATOM   1742 C C   . ALA   B 1 152 ? -14.813 6.239  -25.570 1.00 12.47 ? 120 ALA   B C   1 
ATOM   1743 O O   . ALA   B 1 152 ? -13.951 5.600  -24.960 1.00 13.94 ? 120 ALA   B O   1 
ATOM   1744 C CB  . ALA   B 1 152 ? -15.018 8.441  -24.472 1.00 14.36 ? 120 ALA   B CB  1 
ATOM   1745 N N   . VAL   B 1 153 ? -14.980 6.178  -26.884 1.00 12.95 ? 121 VAL   B N   1 
ATOM   1746 C CA  . VAL   B 1 153 ? -14.012 5.578  -27.787 1.00 15.41 ? 121 VAL   B CA  1 
ATOM   1747 C C   . VAL   B 1 153 ? -13.418 6.707  -28.612 1.00 16.56 ? 121 VAL   B C   1 
ATOM   1748 O O   . VAL   B 1 153 ? -14.139 7.393  -29.348 1.00 17.31 ? 121 VAL   B O   1 
ATOM   1749 C CB  . VAL   B 1 153 ? -14.663 4.524  -28.688 1.00 18.04 ? 121 VAL   B CB  1 
ATOM   1750 C CG1 . VAL   B 1 153 ? -13.623 3.924  -29.618 1.00 20.31 ? 121 VAL   B CG1 1 
ATOM   1751 C CG2 . VAL   B 1 153 ? -15.333 3.463  -27.847 1.00 19.46 ? 121 VAL   B CG2 1 
ATOM   1752 N N   . VAL   B 1 154 ? -12.110 6.907  -28.489 1.00 17.17 ? 122 VAL   B N   1 
ATOM   1753 C CA  . VAL   B 1 154 ? -11.421 8.017  -29.136 1.00 19.11 ? 122 VAL   B CA  1 
ATOM   1754 C C   . VAL   B 1 154 ? -10.381 7.444  -30.083 1.00 20.82 ? 122 VAL   B C   1 
ATOM   1755 O O   . VAL   B 1 154 ? -9.550  6.626  -29.671 1.00 21.11 ? 122 VAL   B O   1 
ATOM   1756 C CB  . VAL   B 1 154 ? -10.767 8.951  -28.102 1.00 20.25 ? 122 VAL   B CB  1 
ATOM   1757 C CG1 . VAL   B 1 154 ? -10.095 10.122 -28.809 1.00 21.90 ? 122 VAL   B CG1 1 
ATOM   1758 C CG2 . VAL   B 1 154 ? -11.813 9.456  -27.121 1.00 20.76 ? 122 VAL   B CG2 1 
ATOM   1759 N N   . THR   B 1 155 ? -10.429 7.865  -31.346 1.00 22.29 ? 123 THR   B N   1 
ATOM   1760 C CA  . THR   B 1 155 ? -9.534  7.326  -32.360 1.00 24.37 ? 123 THR   B CA  1 
ATOM   1761 C C   . THR   B 1 155 ? -8.832  8.450  -33.108 1.00 24.78 ? 123 THR   B C   1 
ATOM   1762 O O   . THR   B 1 155 ? -9.383  9.535  -33.309 1.00 23.09 ? 123 THR   B O   1 
ATOM   1763 C CB  . THR   B 1 155 ? -10.260 6.411  -33.366 1.00 27.71 ? 123 THR   B CB  1 
ATOM   1764 O OG1 . THR   B 1 155 ? -11.131 7.192  -34.187 1.00 30.43 ? 123 THR   B OG1 1 
ATOM   1765 C CG2 . THR   B 1 155 ? -11.077 5.366  -32.643 1.00 27.82 ? 123 THR   B CG2 1 
ATOM   1766 N N   . ASN   B 1 156 ? -7.604  8.177  -33.519 1.00 28.43 ? 124 ASN   B N   1 
ATOM   1767 C CA  . ASN   B 1 156 ? -6.833  9.155  -34.267 1.00 33.75 ? 124 ASN   B CA  1 
ATOM   1768 C C   . ASN   B 1 156 ? -7.067  8.937  -35.756 1.00 40.23 ? 124 ASN   B C   1 
ATOM   1769 O O   . ASN   B 1 156 ? -6.829  7.827  -36.251 1.00 41.14 ? 124 ASN   B O   1 
ATOM   1770 C CB  . ASN   B 1 156 ? -5.357  9.013  -33.949 1.00 35.00 ? 124 ASN   B CB  1 
ATOM   1771 C CG  . ASN   B 1 156 ? -4.555  10.227 -34.368 1.00 36.12 ? 124 ASN   B CG  1 
ATOM   1772 O OD1 . ASN   B 1 156 ? -4.816  10.831 -35.409 1.00 36.69 ? 124 ASN   B OD1 1 
ATOM   1773 N ND2 . ASN   B 1 156 ? -3.577  10.596 -33.552 1.00 37.02 ? 124 ASN   B ND2 1 
ATOM   1774 N N   . PRO   B 1 157 ? -7.539  9.950  -36.502 1.00 45.19 ? 125 PRO   B N   1 
ATOM   1775 C CA  . PRO   B 1 157 ? -7.764  9.847  -37.949 1.00 48.24 ? 125 PRO   B CA  1 
ATOM   1776 C C   . PRO   B 1 157 ? -6.469  9.625  -38.725 1.00 50.35 ? 125 PRO   B C   1 
ATOM   1777 O O   . PRO   B 1 157 ? -6.248  8.516  -39.213 1.00 51.77 ? 125 PRO   B O   1 
ATOM   1778 C CB  . PRO   B 1 157 ? -8.368  11.210 -38.308 1.00 48.39 ? 125 PRO   B CB  1 
ATOM   1779 C CG  . PRO   B 1 157 ? -7.938  12.125 -37.207 1.00 47.83 ? 125 PRO   B CG  1 
ATOM   1780 C CD  . PRO   B 1 157 ? -7.919  11.274 -35.979 1.00 46.77 ? 125 PRO   B CD  1 
HETATM 1781 C CAA . A1L37 C 2 .   ? -22.301 0.597  -3.919  0.50 29.59 ? 201 A1L37 A CAA 1 
HETATM 1782 C CAB . A1L37 C 2 .   ? -22.458 0.488  -5.302  0.50 28.94 ? 201 A1L37 A CAB 1 
HETATM 1783 C CAC . A1L37 C 2 .   ? -21.211 -0.008 -3.315  0.50 29.26 ? 201 A1L37 A CAC 1 
HETATM 1784 C CAD . A1L37 C 2 .   ? -21.517 -0.229 -6.042  0.50 28.99 ? 201 A1L37 A CAD 1 
HETATM 1785 C CAE . A1L37 C 2 .   ? -20.278 -0.713 -4.047  0.50 29.61 ? 201 A1L37 A CAE 1 
HETATM 1786 C CAF . A1L37 C 2 .   ? -20.440 -0.818 -5.411  0.50 28.83 ? 201 A1L37 A CAF 1 
HETATM 1787 C CAJ . A1L37 C 2 .   ? -21.605 -0.391 -7.456  0.50 29.69 ? 201 A1L37 A CAJ 1 
HETATM 1788 I IAH . A1L37 C 2 .   ? -18.648 -1.617 -3.159  0.50 38.33 ? 201 A1L37 A IAH 1 
HETATM 1789 I IAI . A1L37 C 2 .   ? -23.662 1.656  -2.754  0.50 30.88 ? 201 A1L37 A IAI 1 
HETATM 1790 N NAK . A1L37 C 2 .   ? -21.647 -0.538 -8.586  0.50 30.34 ? 201 A1L37 A NAK 1 
HETATM 1791 O OAG . A1L37 C 2 .   ? -21.050 0.092  -1.967  0.50 29.86 ? 201 A1L37 A OAG 1 
HETATM 1792 C CAA . A1L37 D 2 .   ? -17.658 24.684 -2.177  1.00 19.36 ? 202 A1L37 A CAA 1 
HETATM 1793 C CAB . A1L37 D 2 .   ? -18.399 24.789 -1.003  1.00 21.09 ? 202 A1L37 A CAB 1 
HETATM 1794 C CAC . A1L37 D 2 .   ? -18.326 24.509 -3.372  1.00 19.19 ? 202 A1L37 A CAC 1 
HETATM 1795 C CAD . A1L37 D 2 .   ? -19.795 24.727 -1.064  1.00 18.48 ? 202 A1L37 A CAD 1 
HETATM 1796 C CAE . A1L37 D 2 .   ? -19.700 24.455 -3.448  1.00 20.31 ? 202 A1L37 A CAE 1 
HETATM 1797 C CAF . A1L37 D 2 .   ? -20.443 24.559 -2.281  1.00 18.66 ? 202 A1L37 A CAF 1 
HETATM 1798 C CAJ . A1L37 D 2 .   ? -20.570 24.843 0.135   1.00 23.79 ? 202 A1L37 A CAJ 1 
HETATM 1799 I IAH . A1L37 D 2 .   ? -20.589 24.204 -5.285  1.00 21.94 ? 202 A1L37 A IAH 1 
HETATM 1800 I IAI . A1L37 D 2 .   ? -15.591 24.745 -2.182  1.00 18.32 ? 202 A1L37 A IAI 1 
HETATM 1801 N NAK . A1L37 D 2 .   ? -21.198 24.937 1.110   1.00 26.51 ? 202 A1L37 A NAK 1 
HETATM 1802 O OAG . A1L37 D 2 .   ? -17.625 24.408 -4.522  1.00 19.02 ? 202 A1L37 A OAG 1 
HETATM 1803 C CAA . A1L37 E 2 .   ? -20.327 1.014  -28.451 0.50 28.71 ? 201 A1L37 B CAA 1 
HETATM 1804 C CAB . A1L37 E 2 .   ? -20.379 1.244  -27.082 0.50 27.21 ? 201 A1L37 B CAB 1 
HETATM 1805 C CAC . A1L37 E 2 .   ? -21.191 0.057  -28.970 0.50 28.36 ? 201 A1L37 B CAC 1 
HETATM 1806 C CAD . A1L37 E 2 .   ? -21.249 0.536  -26.261 0.50 27.59 ? 201 A1L37 B CAD 1 
HETATM 1807 C CAE . A1L37 E 2 .   ? -22.072 -0.659 -28.170 0.50 27.72 ? 201 A1L37 B CAE 1 
HETATM 1808 C CAF . A1L37 E 2 .   ? -22.100 -0.417 -26.804 0.50 28.65 ? 201 A1L37 B CAF 1 
HETATM 1809 C CAJ . A1L37 E 2 .   ? -21.276 0.787  -24.866 0.50 29.55 ? 201 A1L37 B CAJ 1 
HETATM 1810 I IAH . A1L37 E 2 .   ? -23.342 -2.100 -28.998 0.50 28.91 ? 201 A1L37 B IAH 1 
HETATM 1811 I IAI . A1L37 E 2 .   ? -18.979 2.114  -29.649 0.50 34.44 ? 201 A1L37 B IAI 1 
HETATM 1812 N NAK . A1L37 E 2 .   ? -21.300 0.987  -23.736 0.50 32.23 ? 201 A1L37 B NAK 1 
HETATM 1813 O OAG . A1L37 E 2 .   ? -21.180 -0.189 -30.304 0.50 30.26 ? 201 A1L37 B OAG 1 
HETATM 1814 O O   . HOH   F 3 .   ? -1.249  11.072 -18.187 1.00 37.69 ? 301 HOH   A O   1 
HETATM 1815 O O   . HOH   F 3 .   ? -22.603 13.191 2.398   1.00 19.64 ? 302 HOH   A O   1 
HETATM 1816 O O   . HOH   F 3 .   ? -13.372 21.399 -16.252 1.00 45.00 ? 303 HOH   A O   1 
HETATM 1817 O O   . HOH   F 3 .   ? -43.005 18.538 -5.656  1.00 40.39 ? 304 HOH   A O   1 
HETATM 1818 O O   . HOH   F 3 .   ? -28.530 6.308  1.789   1.00 42.39 ? 305 HOH   A O   1 
HETATM 1819 O O   . HOH   F 3 .   ? -38.859 18.240 -5.889  1.00 42.32 ? 306 HOH   A O   1 
HETATM 1820 O O   . HOH   F 3 .   ? -27.648 26.179 3.864   1.00 49.15 ? 307 HOH   A O   1 
HETATM 1821 O O   . HOH   F 3 .   ? -11.202 16.106 -20.278 1.00 18.16 ? 308 HOH   A O   1 
HETATM 1822 O O   . HOH   F 3 .   ? -32.881 10.368 7.053   1.00 50.58 ? 309 HOH   A O   1 
HETATM 1823 O O   . HOH   F 3 .   ? -26.437 8.442  -10.019 1.00 21.53 ? 310 HOH   A O   1 
HETATM 1824 O O   . HOH   F 3 .   ? -36.677 10.819 -5.180  1.00 20.91 ? 311 HOH   A O   1 
HETATM 1825 O O   . HOH   F 3 .   ? -12.089 11.901 -15.386 1.00 11.99 ? 312 HOH   A O   1 
HETATM 1826 O O   . HOH   F 3 .   ? -33.818 23.459 -7.124  1.00 21.74 ? 313 HOH   A O   1 
HETATM 1827 O O   . HOH   F 3 .   ? -22.407 28.300 -8.497  1.00 40.89 ? 314 HOH   A O   1 
HETATM 1828 O O   . HOH   F 3 .   ? -18.991 13.857 -17.561 1.00 15.16 ? 315 HOH   A O   1 
HETATM 1829 O O   . HOH   F 3 .   ? -22.240 24.741 -12.180 1.00 35.85 ? 316 HOH   A O   1 
HETATM 1830 O O   . HOH   F 3 .   ? -0.816  13.239 -14.632 1.00 41.64 ? 317 HOH   A O   1 
HETATM 1831 O O   . HOH   F 3 .   ? -17.636 25.644 -6.942  1.00 31.75 ? 318 HOH   A O   1 
HETATM 1832 O O   . HOH   F 3 .   ? -19.541 23.605 -12.398 1.00 45.11 ? 319 HOH   A O   1 
HETATM 1833 O O   . HOH   F 3 .   ? -39.358 12.145 -2.593  1.00 29.16 ? 320 HOH   A O   1 
HETATM 1834 O O   . HOH   F 3 .   ? -40.128 10.063 4.218   1.00 40.21 ? 321 HOH   A O   1 
HETATM 1835 O O   . HOH   F 3 .   ? -25.936 24.934 1.649   1.00 34.00 ? 322 HOH   A O   1 
HETATM 1836 O O   . HOH   F 3 .   ? -34.952 11.875 -8.866  1.00 18.60 ? 323 HOH   A O   1 
HETATM 1837 O O   . HOH   F 3 .   ? -22.623 3.051  -10.575 1.00 18.22 ? 324 HOH   A O   1 
HETATM 1838 O O   . HOH   F 3 .   ? -18.847 16.177 5.192   1.00 45.02 ? 325 HOH   A O   1 
HETATM 1839 O O   . HOH   F 3 .   ? -16.290 6.662  5.498   1.00 44.13 ? 326 HOH   A O   1 
HETATM 1840 O O   . HOH   F 3 .   ? -6.431  9.208  -4.305  1.00 37.93 ? 327 HOH   A O   1 
HETATM 1841 O O   . HOH   F 3 .   ? -33.868 13.516 3.543   1.00 32.68 ? 328 HOH   A O   1 
HETATM 1842 O O   . HOH   F 3 .   ? -18.806 1.026  3.986   1.00 48.05 ? 329 HOH   A O   1 
HETATM 1843 O O   . HOH   F 3 .   ? -12.977 9.902  -17.060 1.00 13.94 ? 330 HOH   A O   1 
HETATM 1844 O O   . HOH   F 3 .   ? -37.820 18.899 -10.822 1.00 37.86 ? 331 HOH   A O   1 
HETATM 1845 O O   . HOH   F 3 .   ? -6.948  14.173 -19.678 1.00 46.03 ? 332 HOH   A O   1 
HETATM 1846 O O   . HOH   F 3 .   ? -0.820  11.698 -21.098 1.00 33.12 ? 333 HOH   A O   1 
HETATM 1847 O O   . HOH   F 3 .   ? -36.811 26.141 -3.269  1.00 20.22 ? 334 HOH   A O   1 
HETATM 1848 O O   . HOH   F 3 .   ? -34.433 16.284 3.822   1.00 25.90 ? 335 HOH   A O   1 
HETATM 1849 O O   . HOH   F 3 .   ? -8.933  15.990 -3.843  1.00 31.26 ? 336 HOH   A O   1 
HETATM 1850 O O   . HOH   F 3 .   ? -14.746 12.216 4.004   1.00 22.08 ? 337 HOH   A O   1 
HETATM 1851 O O   . HOH   F 3 .   ? -17.461 17.953 3.626   1.00 31.85 ? 338 HOH   A O   1 
HETATM 1852 O O   . HOH   F 3 .   ? -43.754 7.646  2.556   1.00 49.48 ? 339 HOH   A O   1 
HETATM 1853 O O   . HOH   F 3 .   ? -10.633 14.723 -6.925  1.00 15.92 ? 340 HOH   A O   1 
HETATM 1854 O O   . HOH   F 3 .   ? -13.664 8.313  -14.331 1.00 12.16 ? 341 HOH   A O   1 
HETATM 1855 O O   . HOH   F 3 .   ? -33.650 30.511 -5.231  1.00 30.43 ? 342 HOH   A O   1 
HETATM 1856 O O   . HOH   F 3 .   ? -7.447  9.017  -26.428 1.00 40.70 ? 343 HOH   A O   1 
HETATM 1857 O O   . HOH   F 3 .   ? -15.483 0.906  1.230   1.00 46.44 ? 344 HOH   A O   1 
HETATM 1858 O O   . HOH   F 3 .   ? -7.061  -3.585 -4.796  1.00 32.59 ? 345 HOH   A O   1 
HETATM 1859 O O   . HOH   F 3 .   ? -37.545 2.800  0.644   1.00 41.36 ? 346 HOH   A O   1 
HETATM 1860 O O   . HOH   F 3 .   ? -30.303 26.738 -4.731  1.00 30.48 ? 347 HOH   A O   1 
HETATM 1861 O O   . HOH   F 3 .   ? -4.152  15.651 -9.709  1.00 32.09 ? 348 HOH   A O   1 
HETATM 1862 O O   . HOH   F 3 .   ? -16.079 2.223  -14.637 1.00 20.52 ? 349 HOH   A O   1 
HETATM 1863 O O   . HOH   F 3 .   ? -15.450 10.448 -14.779 1.00 21.14 ? 350 HOH   A O   1 
HETATM 1864 O O   . HOH   F 3 .   ? -8.004  5.541  -4.221  1.00 21.73 ? 351 HOH   A O   1 
HETATM 1865 O O   . HOH   F 3 .   ? -29.669 15.211 9.268   1.00 43.47 ? 352 HOH   A O   1 
HETATM 1866 O O   . HOH   F 3 .   ? -17.095 11.166 5.027   1.00 23.21 ? 353 HOH   A O   1 
HETATM 1867 O O   . HOH   F 3 .   ? -8.358  13.037 -6.116  1.00 28.83 ? 354 HOH   A O   1 
HETATM 1868 O O   . HOH   F 3 .   ? -37.486 13.428 -6.257  1.00 21.58 ? 355 HOH   A O   1 
HETATM 1869 O O   . HOH   F 3 .   ? -21.626 -0.000 -14.127 0.50 29.45 ? 356 HOH   A O   1 
HETATM 1870 O O   . HOH   F 3 .   ? -22.814 23.104 3.036   1.00 36.91 ? 357 HOH   A O   1 
HETATM 1871 O O   . HOH   F 3 .   ? -25.389 28.563 -13.218 1.00 43.22 ? 358 HOH   A O   1 
HETATM 1872 O O   . HOH   F 3 .   ? -23.911 18.643 7.273   1.00 44.67 ? 359 HOH   A O   1 
HETATM 1873 O O   . HOH   F 3 .   ? -30.368 5.219  0.256   1.00 22.72 ? 360 HOH   A O   1 
HETATM 1874 O O   . HOH   F 3 .   ? -5.480  9.961  -6.984  1.00 33.47 ? 361 HOH   A O   1 
HETATM 1875 O O   . HOH   F 3 .   ? -25.625 13.999 4.444   1.00 25.01 ? 362 HOH   A O   1 
HETATM 1876 O O   . HOH   F 3 .   ? -10.304 8.813  5.707   1.00 38.13 ? 363 HOH   A O   1 
HETATM 1877 O O   . HOH   F 3 .   ? -4.625  -2.884 -7.941  1.00 53.78 ? 364 HOH   A O   1 
HETATM 1878 O O   . HOH   F 3 .   ? -42.793 10.950 2.211   1.00 38.83 ? 365 HOH   A O   1 
HETATM 1879 O O   . HOH   F 3 .   ? -40.404 11.105 -6.462  1.00 52.11 ? 366 HOH   A O   1 
HETATM 1880 O O   . HOH   F 3 .   ? -4.839  11.078 -2.414  1.00 45.52 ? 367 HOH   A O   1 
HETATM 1881 O O   . HOH   F 3 .   ? -36.193 14.047 7.243   1.00 49.79 ? 368 HOH   A O   1 
HETATM 1882 O O   . HOH   F 3 .   ? -27.747 8.404  2.474   1.00 37.17 ? 369 HOH   A O   1 
HETATM 1883 O O   . HOH   F 3 .   ? -25.016 15.924 8.872   1.00 49.11 ? 370 HOH   A O   1 
HETATM 1884 O O   . HOH   F 3 .   ? -38.858 7.253  -3.599  1.00 49.74 ? 371 HOH   A O   1 
HETATM 1885 O O   . HOH   F 3 .   ? -13.769 -1.211 -7.687  1.00 41.79 ? 372 HOH   A O   1 
HETATM 1886 O O   . HOH   F 3 .   ? -7.243  18.058 -12.875 1.00 35.20 ? 373 HOH   A O   1 
HETATM 1887 O O   . HOH   F 3 .   ? -15.565 18.748 -9.031  1.00 34.17 ? 374 HOH   A O   1 
HETATM 1888 O O   . HOH   F 3 .   ? -16.880 -1.238 -0.896  1.00 39.42 ? 375 HOH   A O   1 
HETATM 1889 O O   . HOH   F 3 .   ? -16.758 23.595 -8.811  1.00 43.37 ? 376 HOH   A O   1 
HETATM 1890 O O   . HOH   F 3 .   ? -9.582  21.768 -18.333 1.00 46.25 ? 377 HOH   A O   1 
HETATM 1891 O O   . HOH   F 3 .   ? -36.534 16.405 5.764   1.00 35.46 ? 378 HOH   A O   1 
HETATM 1892 O O   . HOH   F 3 .   ? -25.229 21.202 -15.300 1.00 48.88 ? 379 HOH   A O   1 
HETATM 1893 O O   . HOH   F 3 .   ? -37.727 20.489 -7.005  1.00 46.41 ? 380 HOH   A O   1 
HETATM 1894 O O   . HOH   F 3 .   ? -13.459 5.590  6.244   1.00 55.36 ? 381 HOH   A O   1 
HETATM 1895 O O   . HOH   F 3 .   ? -9.841  12.187 -24.722 1.00 25.69 ? 382 HOH   A O   1 
HETATM 1896 O O   . HOH   F 3 .   ? -28.366 26.155 -2.253  1.00 33.45 ? 383 HOH   A O   1 
HETATM 1897 O O   . HOH   F 3 .   ? 0.813   13.788 -11.085 1.00 48.06 ? 384 HOH   A O   1 
HETATM 1898 O O   . HOH   F 3 .   ? -4.177  -2.578 -11.142 1.00 38.95 ? 385 HOH   A O   1 
HETATM 1899 O O   . HOH   F 3 .   ? -36.272 18.344 8.201   1.00 43.01 ? 386 HOH   A O   1 
HETATM 1900 O O   . HOH   F 3 .   ? -23.794 26.522 2.637   1.00 45.46 ? 387 HOH   A O   1 
HETATM 1901 O O   . HOH   F 3 .   ? -38.041 5.111  -1.944  1.00 45.16 ? 388 HOH   A O   1 
HETATM 1902 O O   . HOH   F 3 .   ? -39.085 9.890  -4.234  1.00 32.42 ? 389 HOH   A O   1 
HETATM 1903 O O   . HOH   F 3 .   ? -34.477 11.879 5.478   1.00 35.56 ? 390 HOH   A O   1 
HETATM 1904 O O   . HOH   F 3 .   ? -22.717 25.129 4.360   1.00 35.06 ? 391 HOH   A O   1 
HETATM 1905 O O   . HOH   F 3 .   ? -20.857 20.965 -16.015 1.00 49.07 ? 392 HOH   A O   1 
HETATM 1906 O O   . HOH   F 3 .   ? -6.583  3.479  -2.888  1.00 41.88 ? 393 HOH   A O   1 
HETATM 1907 O O   . HOH   F 3 .   ? -1.461  15.556 -10.684 1.00 46.92 ? 394 HOH   A O   1 
HETATM 1908 O O   . HOH   F 3 .   ? -1.210  15.038 -21.514 1.00 47.16 ? 395 HOH   A O   1 
HETATM 1909 O O   . HOH   F 3 .   ? -36.489 24.348 -7.083  1.00 38.94 ? 396 HOH   A O   1 
HETATM 1910 O O   . HOH   F 3 .   ? -4.669  17.723 -11.340 1.00 50.19 ? 397 HOH   A O   1 
HETATM 1911 O O   . HOH   F 3 .   ? -2.738  10.409 -5.643  1.00 52.79 ? 398 HOH   A O   1 
HETATM 1912 O O   . HOH   F 3 .   ? -12.145 3.486  6.554   1.00 51.37 ? 399 HOH   A O   1 
HETATM 1913 O O   . HOH   F 3 .   ? -12.136 0.288  2.975   1.00 49.32 ? 400 HOH   A O   1 
HETATM 1914 O O   . HOH   F 3 .   ? -16.853 8.995  6.545   1.00 53.52 ? 401 HOH   A O   1 
HETATM 1915 O O   . HOH   F 3 .   ? -13.396 -0.355 0.726   1.00 52.99 ? 402 HOH   A O   1 
HETATM 1916 O O   . HOH   F 3 .   ? -16.154 19.311 5.168   1.00 49.81 ? 403 HOH   A O   1 
HETATM 1917 O O   . HOH   F 3 .   ? -37.808 21.268 -9.318  1.00 45.74 ? 404 HOH   A O   1 
HETATM 1918 O O   . HOH   F 3 .   ? -20.187 28.335 -7.081  1.00 40.71 ? 405 HOH   A O   1 
HETATM 1919 O O   . HOH   G 3 .   ? -22.748 13.082 -34.341 1.00 40.97 ? 301 HOH   B O   1 
HETATM 1920 O O   . HOH   G 3 .   ? -35.450 8.456  -34.313 1.00 43.00 ? 302 HOH   B O   1 
HETATM 1921 O O   . HOH   G 3 .   ? -6.926  22.219 -24.178 1.00 49.43 ? 303 HOH   B O   1 
HETATM 1922 O O   . HOH   G 3 .   ? -38.628 15.302 -32.271 1.00 44.29 ? 304 HOH   B O   1 
HETATM 1923 O O   . HOH   G 3 .   ? -13.643 28.925 -19.867 1.00 45.95 ? 305 HOH   B O   1 
HETATM 1924 O O   . HOH   G 3 .   ? -27.254 15.201 -37.165 1.00 40.92 ? 306 HOH   B O   1 
HETATM 1925 O O   . HOH   G 3 .   ? -36.232 16.208 -24.913 1.00 34.08 ? 307 HOH   B O   1 
HETATM 1926 O O   . HOH   G 3 .   ? -34.808 13.904 -11.503 1.00 15.91 ? 308 HOH   B O   1 
HETATM 1927 O O   . HOH   G 3 .   ? -7.142  25.702 -27.825 1.00 32.30 ? 309 HOH   B O   1 
HETATM 1928 O O   . HOH   G 3 .   ? -9.755  23.757 -22.414 1.00 51.44 ? 310 HOH   B O   1 
HETATM 1929 O O   . HOH   G 3 .   ? -10.674 23.600 -45.847 1.00 45.75 ? 311 HOH   B O   1 
HETATM 1930 O O   . HOH   G 3 .   ? -19.360 23.072 -38.429 1.00 42.03 ? 312 HOH   B O   1 
HETATM 1931 O O   . HOH   G 3 .   ? -21.724 25.415 -33.634 1.00 26.71 ? 313 HOH   B O   1 
HETATM 1932 O O   . HOH   G 3 .   ? -8.901  13.800 -26.687 1.00 26.88 ? 314 HOH   B O   1 
HETATM 1933 O O   . HOH   G 3 .   ? -28.169 6.010  -37.376 1.00 40.43 ? 315 HOH   B O   1 
HETATM 1934 O O   . HOH   G 3 .   ? -17.617 28.304 -26.719 1.00 50.50 ? 316 HOH   B O   1 
HETATM 1935 O O   . HOH   G 3 .   ? -10.625 14.172 -22.931 1.00 21.45 ? 317 HOH   B O   1 
HETATM 1936 O O   . HOH   G 3 .   ? -18.443 9.197  -22.108 1.00 20.10 ? 318 HOH   B O   1 
HETATM 1937 O O   . HOH   G 3 .   ? -34.370 -0.087 -33.695 1.00 47.83 ? 319 HOH   B O   1 
HETATM 1938 O O   . HOH   G 3 .   ? -4.365  22.166 -28.778 1.00 27.57 ? 320 HOH   B O   1 
HETATM 1939 O O   . HOH   G 3 .   ? -13.912 25.362 -24.322 1.00 22.60 ? 321 HOH   B O   1 
HETATM 1940 O O   . HOH   G 3 .   ? -31.906 8.196  -14.915 1.00 13.79 ? 322 HOH   B O   1 
HETATM 1941 O O   . HOH   G 3 .   ? -33.178 10.066 -16.543 1.00 12.60 ? 323 HOH   B O   1 
HETATM 1942 O O   . HOH   G 3 .   ? -39.380 4.785  -10.752 1.00 42.55 ? 324 HOH   B O   1 
HETATM 1943 O O   . HOH   G 3 .   ? -11.770 17.779 -34.926 1.00 34.63 ? 325 HOH   B O   1 
HETATM 1944 O O   . HOH   G 3 .   ? -38.150 6.470  -27.579 1.00 36.33 ? 326 HOH   B O   1 
HETATM 1945 O O   . HOH   G 3 .   ? -12.803 25.586 -44.572 1.00 47.23 ? 327 HOH   B O   1 
HETATM 1946 O O   . HOH   G 3 .   ? -9.254  21.442 -20.868 1.00 28.72 ? 328 HOH   B O   1 
HETATM 1947 O O   . HOH   G 3 .   ? -40.102 16.168 -22.757 1.00 43.84 ? 329 HOH   B O   1 
HETATM 1948 O O   . HOH   G 3 .   ? -12.417 15.331 -35.620 1.00 27.32 ? 330 HOH   B O   1 
HETATM 1949 O O   . HOH   G 3 .   ? -21.145 3.091  -21.326 1.00 19.45 ? 331 HOH   B O   1 
HETATM 1950 O O   . HOH   G 3 .   ? -26.777 13.181 -14.262 1.00 13.89 ? 332 HOH   B O   1 
HETATM 1951 O O   . HOH   G 3 .   ? -25.462 1.658  -15.494 1.00 39.29 ? 333 HOH   B O   1 
HETATM 1952 O O   . HOH   G 3 .   ? -1.037  17.637 -26.441 1.00 50.08 ? 334 HOH   B O   1 
HETATM 1953 O O   . HOH   G 3 .   ? -30.288 11.118 -35.851 1.00 24.60 ? 335 HOH   B O   1 
HETATM 1954 O O   . HOH   G 3 .   ? -37.017 13.440 -28.596 1.00 38.17 ? 336 HOH   B O   1 
HETATM 1955 O O   . HOH   G 3 .   ? -45.974 8.326  -19.601 1.00 30.04 ? 337 HOH   B O   1 
HETATM 1956 O O   . HOH   G 3 .   ? -6.439  5.780  -32.781 1.00 47.51 ? 338 HOH   B O   1 
HETATM 1957 O O   . HOH   G 3 .   ? -29.719 20.467 -22.866 1.00 24.57 ? 339 HOH   B O   1 
HETATM 1958 O O   . HOH   G 3 .   ? -27.403 1.239  -17.305 1.00 17.98 ? 340 HOH   B O   1 
HETATM 1959 O O   . HOH   G 3 .   ? -30.743 17.832 -23.256 1.00 17.35 ? 341 HOH   B O   1 
HETATM 1960 O O   . HOH   G 3 .   ? -35.091 -6.181 -27.076 1.00 27.79 ? 342 HOH   B O   1 
HETATM 1961 O O   . HOH   G 3 .   ? -14.980 26.015 -44.078 1.00 43.98 ? 343 HOH   B O   1 
HETATM 1962 O O   . HOH   G 3 .   ? -22.533 21.879 -34.868 1.00 24.69 ? 344 HOH   B O   1 
HETATM 1963 O O   . HOH   G 3 .   ? -41.517 12.255 -22.159 1.00 27.25 ? 345 HOH   B O   1 
HETATM 1964 O O   . HOH   G 3 .   ? -35.081 12.585 -24.983 1.00 15.08 ? 346 HOH   B O   1 
HETATM 1965 O O   . HOH   G 3 .   ? -22.563 3.044  -36.874 1.00 51.42 ? 347 HOH   B O   1 
HETATM 1966 O O   . HOH   G 3 .   ? -20.732 13.127 -38.215 1.00 59.29 ? 348 HOH   B O   1 
HETATM 1967 O O   . HOH   G 3 .   ? -28.190 23.360 -20.567 1.00 49.76 ? 349 HOH   B O   1 
HETATM 1968 O O   . HOH   G 3 .   ? -6.878  15.663 -29.197 1.00 19.56 ? 350 HOH   B O   1 
HETATM 1969 O O   . HOH   G 3 .   ? -29.555 9.221  -17.240 1.00 24.28 ? 351 HOH   B O   1 
HETATM 1970 O O   . HOH   G 3 .   ? -20.034 14.670 -36.117 1.00 23.53 ? 352 HOH   B O   1 
HETATM 1971 O O   . HOH   G 3 .   ? -10.128 24.490 -42.649 1.00 28.79 ? 353 HOH   B O   1 
HETATM 1972 O O   . HOH   G 3 .   ? -23.291 29.491 -29.742 1.00 45.49 ? 354 HOH   B O   1 
HETATM 1973 O O   . HOH   G 3 .   ? -22.868 28.124 -32.020 1.00 32.09 ? 355 HOH   B O   1 
HETATM 1974 O O   . HOH   G 3 .   ? -11.935 28.921 -26.942 1.00 46.85 ? 356 HOH   B O   1 
HETATM 1975 O O   . HOH   G 3 .   ? -27.897 10.512 -36.957 1.00 26.66 ? 357 HOH   B O   1 
HETATM 1976 O O   . HOH   G 3 .   ? -15.891 26.179 -33.566 1.00 51.72 ? 358 HOH   B O   1 
HETATM 1977 O O   . HOH   G 3 .   ? -39.113 6.843  -24.883 1.00 31.17 ? 359 HOH   B O   1 
HETATM 1978 O O   . HOH   G 3 .   ? -23.884 28.699 -19.089 1.00 40.43 ? 360 HOH   B O   1 
HETATM 1979 O O   . HOH   G 3 .   ? -25.097 18.720 -16.740 1.00 34.66 ? 361 HOH   B O   1 
HETATM 1980 O O   . HOH   G 3 .   ? -17.148 22.662 -41.928 1.00 48.84 ? 362 HOH   B O   1 
HETATM 1981 O O   . HOH   G 3 .   ? -14.083 6.792  -32.206 1.00 32.63 ? 363 HOH   B O   1 
HETATM 1982 O O   . HOH   G 3 .   ? -15.653 16.400 -41.048 1.00 42.14 ? 364 HOH   B O   1 
HETATM 1983 O O   . HOH   G 3 .   ? -31.324 14.970 -35.046 1.00 22.32 ? 365 HOH   B O   1 
HETATM 1984 O O   . HOH   G 3 .   ? -33.898 6.598  -37.799 1.00 28.32 ? 366 HOH   B O   1 
HETATM 1985 O O   . HOH   G 3 .   ? -41.433 4.353  -12.266 1.00 50.55 ? 367 HOH   B O   1 
HETATM 1986 O O   . HOH   G 3 .   ? -36.054 3.185  -27.814 1.00 22.81 ? 368 HOH   B O   1 
HETATM 1987 O O   . HOH   G 3 .   ? -36.823 10.596 -25.664 1.00 25.42 ? 369 HOH   B O   1 
HETATM 1988 O O   . HOH   G 3 .   ? -37.660 -5.939 -24.275 1.00 46.30 ? 370 HOH   B O   1 
HETATM 1989 O O   . HOH   G 3 .   ? -21.626 -0.000 -17.619 0.50 26.61 ? 371 HOH   B O   1 
HETATM 1990 O O   . HOH   G 3 .   ? -37.930 9.125  -9.459  1.00 43.33 ? 372 HOH   B O   1 
HETATM 1991 O O   . HOH   G 3 .   ? -25.858 24.446 -20.452 1.00 37.25 ? 373 HOH   B O   1 
HETATM 1992 O O   . HOH   G 3 .   ? -26.324 27.249 -21.981 1.00 46.58 ? 374 HOH   B O   1 
HETATM 1993 O O   . HOH   G 3 .   ? -37.407 19.253 -13.569 1.00 54.09 ? 375 HOH   B O   1 
HETATM 1994 O O   . HOH   G 3 .   ? -40.138 7.438  -29.354 1.00 47.50 ? 376 HOH   B O   1 
HETATM 1995 O O   . HOH   G 3 .   ? -38.995 15.135 -18.949 1.00 39.89 ? 377 HOH   B O   1 
HETATM 1996 O O   . HOH   G 3 .   ? -40.596 2.599  -27.571 1.00 49.13 ? 378 HOH   B O   1 
HETATM 1997 O O   . HOH   G 3 .   ? -15.194 32.139 -25.715 1.00 60.95 ? 379 HOH   B O   1 
HETATM 1998 O O   . HOH   G 3 .   ? -37.483 6.238  -5.452  1.00 44.50 ? 380 HOH   B O   1 
HETATM 1999 O O   . HOH   G 3 .   ? -22.814 22.053 -16.259 1.00 46.84 ? 381 HOH   B O   1 
HETATM 2000 O O   . HOH   G 3 .   ? -11.062 26.413 -24.821 1.00 38.68 ? 382 HOH   B O   1 
HETATM 2001 O O   . HOH   G 3 .   ? -37.630 7.233  -34.879 1.00 53.56 ? 383 HOH   B O   1 
HETATM 2002 O O   . HOH   G 3 .   ? -17.281 34.424 -23.556 1.00 48.59 ? 384 HOH   B O   1 
HETATM 2003 O O   . HOH   G 3 .   ? -15.879 22.135 -17.053 1.00 34.87 ? 385 HOH   B O   1 
HETATM 2004 O O   . HOH   G 3 .   ? -2.961  9.179  -30.777 1.00 50.77 ? 386 HOH   B O   1 
HETATM 2005 O O   . HOH   G 3 .   ? -37.334 -6.536 -20.442 1.00 12.02 ? 387 HOH   B O   1 
HETATM 2006 O O   . HOH   G 3 .   ? -46.292 8.299  -22.866 1.00 57.10 ? 388 HOH   B O   1 
HETATM 2007 O O   . HOH   G 3 .   ? -11.601 13.921 -37.731 1.00 47.18 ? 389 HOH   B O   1 
HETATM 2008 O O   . HOH   G 3 .   ? -6.091  10.382 -28.150 1.00 48.11 ? 390 HOH   B O   1 
HETATM 2009 O O   . HOH   G 3 .   ? -31.057 4.365  -38.151 1.00 53.41 ? 391 HOH   B O   1 
HETATM 2010 O O   . HOH   G 3 .   ? -24.601 16.640 -40.892 1.00 44.40 ? 392 HOH   B O   1 
HETATM 2011 O O   . HOH   G 3 .   ? -21.824 21.429 -38.393 1.00 41.29 ? 393 HOH   B O   1 
HETATM 2012 O O   . HOH   G 3 .   ? -39.506 10.785 -25.462 1.00 44.18 ? 394 HOH   B O   1 
HETATM 2013 O O   . HOH   G 3 .   ? -31.865 18.075 -25.632 1.00 17.04 ? 395 HOH   B O   1 
HETATM 2014 O O   . HOH   G 3 .   ? -45.145 2.388  -22.162 1.00 17.65 ? 396 HOH   B O   1 
HETATM 2015 O O   . HOH   G 3 .   ? -35.431 9.637  -7.246  1.00 21.48 ? 397 HOH   B O   1 
HETATM 2016 O O   . HOH   G 3 .   ? -5.874  8.556  -29.739 1.00 45.50 ? 398 HOH   B O   1 
HETATM 2017 O O   . HOH   G 3 .   ? -46.666 2.786  -19.321 1.00 41.26 ? 399 HOH   B O   1 
HETATM 2018 O O   . HOH   G 3 .   ? -6.422  13.370 -27.685 1.00 32.22 ? 400 HOH   B O   1 
HETATM 2019 O O   . HOH   G 3 .   ? -28.449 8.185  -38.313 1.00 43.30 ? 401 HOH   B O   1 
HETATM 2020 O O   . HOH   G 3 .   ? -39.684 14.579 -25.228 1.00 48.04 ? 402 HOH   B O   1 
HETATM 2021 O O   . HOH   G 3 .   ? -23.740 22.382 -36.994 1.00 23.27 ? 403 HOH   B O   1 
HETATM 2022 O O   . HOH   G 3 .   ? -28.172 11.594 -39.466 1.00 46.58 ? 404 HOH   B O   1 
HETATM 2023 O O   . HOH   G 3 .   ? -31.868 22.128 -22.818 1.00 38.05 ? 405 HOH   B O   1 
HETATM 2024 O O   . HOH   G 3 .   ? -11.833 25.824 -22.382 1.00 49.55 ? 406 HOH   B O   1 
HETATM 2025 O O   . HOH   G 3 .   ? -37.418 14.477 -25.974 1.00 38.78 ? 407 HOH   B O   1 
HETATM 2026 O O   . HOH   G 3 .   ? -23.604 -0.187 -15.960 1.00 37.05 ? 408 HOH   B O   1 
HETATM 2027 O O   . HOH   G 3 .   ? -30.039 13.714 -36.884 1.00 42.67 ? 409 HOH   B O   1 
HETATM 2028 O O   . HOH   G 3 .   ? -12.662 11.998 -38.148 1.00 45.66 ? 410 HOH   B O   1 
HETATM 2029 O O   . HOH   G 3 .   ? -32.486 10.178 -37.585 1.00 47.94 ? 411 HOH   B O   1 
HETATM 2030 O O   . HOH   G 3 .   ? -13.041 33.214 -26.387 1.00 45.12 ? 412 HOH   B O   1 
HETATM 2031 O O   . HOH   G 3 .   ? -45.452 10.873 -23.083 1.00 39.20 ? 413 HOH   B O   1 
HETATM 2032 O O   . HOH   G 3 .   ? -24.935 -2.381 -16.439 1.00 42.96 ? 414 HOH   B O   1 
HETATM 2033 O O   . HOH   G 3 .   ? -27.943 4.778  -41.652 1.00 49.06 ? 415 HOH   B O   1 
HETATM 2034 O O   . HOH   G 3 .   ? -29.404 5.065  -43.692 1.00 47.26 ? 416 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   . CYS A 42  ? 0.6289 0.4690 0.4006 0.1162  0.0591  0.0115  10  CYS A N   
2    C CA  . CYS A 42  ? 0.6175 0.4581 0.3862 0.1147  0.0832  0.0070  10  CYS A CA  
3    C C   . CYS A 42  ? 0.4822 0.3938 0.3534 0.1083  0.1118  0.0112  10  CYS A C   
4    O O   . CYS A 42  ? 0.4883 0.3835 0.3725 0.1376  0.1005  0.0448  10  CYS A O   
5    C CB  . CYS A 42  ? 0.7297 0.4950 0.4178 0.1048  0.0794  -0.0001 10  CYS A CB  
6    S SG  . CYS A 42  ? 0.8111 0.5056 0.4445 0.0777  0.0740  -0.0067 10  CYS A SG  
7    N N   . PRO A 43  ? 0.3769 0.3359 0.3063 0.0761  0.1080  -0.0108 11  PRO A N   
8    C CA  . PRO A 43  ? 0.2985 0.2997 0.2690 0.0584  0.0923  -0.0427 11  PRO A CA  
9    C C   . PRO A 43  ? 0.2142 0.2545 0.2218 0.0340  0.0596  -0.0687 11  PRO A C   
10   O O   . PRO A 43  ? 0.2186 0.2439 0.2277 0.0017  0.0224  -0.0887 11  PRO A O   
11   C CB  . PRO A 43  ? 0.3610 0.3191 0.2994 0.0706  0.0811  -0.0405 11  PRO A CB  
12   C CG  . PRO A 43  ? 0.3939 0.3107 0.3131 0.0726  0.0893  -0.0278 11  PRO A CG  
13   C CD  . PRO A 43  ? 0.4024 0.3287 0.3086 0.0741  0.1016  -0.0302 11  PRO A CD  
14   N N   . LEU A 44  ? 0.2081 0.2282 0.1785 0.0231  0.0299  -0.0622 12  LEU A N   
15   C CA  . LEU A 44  ? 0.2077 0.2160 0.1761 0.0069  0.0143  -0.0525 12  LEU A CA  
16   C C   . LEU A 44  ? 0.2246 0.2298 0.1949 0.0052  0.0001  -0.0687 12  LEU A C   
17   O O   . LEU A 44  ? 0.2478 0.2620 0.2359 0.0262  -0.0369 -0.1149 12  LEU A O   
18   C CB  . LEU A 44  ? 0.2566 0.2102 0.1830 -0.0198 0.0171  -0.0355 12  LEU A CB  
19   C CG  . LEU A 44  ? 0.2656 0.2204 0.1948 -0.0331 -0.0016 -0.0255 12  LEU A CG  
20   C CD1 . LEU A 44  ? 0.2547 0.2434 0.1886 -0.0506 0.0006  -0.0284 12  LEU A CD1 
21   C CD2 . LEU A 44  ? 0.2933 0.2169 0.2169 -0.0515 -0.0120 -0.0032 12  LEU A CD2 
22   N N   . MET A 45  ? 0.1881 0.2083 0.1589 -0.0027 0.0223  -0.0373 13  MET A N   
23   C CA  . MET A 45  ? 0.1786 0.2020 0.1337 0.0159  0.0023  -0.0211 13  MET A CA  
24   C C   . MET A 45  ? 0.1759 0.1683 0.1139 0.0152  -0.0058 -0.0320 13  MET A C   
25   O O   . MET A 45  ? 0.1788 0.2061 0.1127 -0.0023 -0.0065 -0.0330 13  MET A O   
26   C CB  . MET A 45  ? 0.1986 0.2383 0.1586 0.0259  0.0021  -0.0074 13  MET A CB  
27   C CG  . MET A 45  ? 0.2458 0.2464 0.2044 0.0256  0.0029  -0.0195 13  MET A CG  
28   S SD  . MET A 45  ? 0.2776 0.2456 0.2465 0.0105  0.0172  0.0001  13  MET A SD  
29   C CE  . MET A 45  ? 0.3225 0.2393 0.2529 0.0041  0.0183  0.0259  13  MET A CE  
30   N N   . VAL A 46  ? 0.1915 0.1593 0.1070 0.0245  0.0107  -0.0262 14  VAL A N   
31   C CA  . VAL A 46  ? 0.1539 0.1601 0.1029 0.0100  0.0080  -0.0217 14  VAL A CA  
32   C C   . VAL A 46  ? 0.1558 0.1647 0.1164 0.0096  -0.0167 -0.0369 14  VAL A C   
33   O O   . VAL A 46  ? 0.1889 0.1963 0.1425 0.0018  -0.0262 -0.0409 14  VAL A O   
34   C CB  . VAL A 46  ? 0.2105 0.1578 0.1181 -0.0053 0.0166  -0.0100 14  VAL A CB  
35   C CG1 . VAL A 46  ? 0.2561 0.1808 0.0997 -0.0313 0.0388  -0.0054 14  VAL A CG1 
36   C CG2 . VAL A 46  ? 0.2173 0.1661 0.1528 -0.0064 0.0033  -0.0004 14  VAL A CG2 
37   N N   . LYS A 47  ? 0.1776 0.1525 0.1149 0.0131  0.0015  -0.0164 15  LYS A N   
38   C CA  . LYS A 47  ? 0.1994 0.1542 0.1154 0.0252  0.0212  0.0151  15  LYS A CA  
39   C C   . LYS A 47  ? 0.1672 0.1695 0.1031 0.0094  -0.0013 -0.0054 15  LYS A C   
40   O O   . LYS A 47  ? 0.1680 0.2035 0.1010 0.0255  -0.0139 -0.0207 15  LYS A O   
41   C CB  . LYS A 47  ? 0.2925 0.1472 0.1495 0.0339  0.0209  0.0368  15  LYS A CB  
42   C CG  . LYS A 47  ? 0.3642 0.1682 0.1957 0.0330  0.0125  0.0489  15  LYS A CG  
43   C CD  . LYS A 47  ? 0.4464 0.1908 0.2328 0.0431  0.0134  0.0687  15  LYS A CD  
44   C CE  . LYS A 47  ? 0.5338 0.1994 0.2637 0.0265  0.0127  0.0854  15  LYS A CE  
45   N NZ  . LYS A 47  ? 0.6003 0.2118 0.2864 0.0092  0.0111  0.0813  15  LYS A NZ  
46   N N   . VAL A 48  ? 0.1476 0.1537 0.1097 0.0274  0.0189  0.0017  16  VAL A N   
47   C CA  . VAL A 48  ? 0.1598 0.1428 0.1086 0.0308  0.0101  0.0020  16  VAL A CA  
48   C C   . VAL A 48  ? 0.1499 0.1597 0.1229 0.0356  -0.0200 -0.0109 16  VAL A C   
49   O O   . VAL A 48  ? 0.1569 0.1931 0.1253 0.0297  -0.0118 -0.0039 16  VAL A O   
50   C CB  . VAL A 48  ? 0.1746 0.1458 0.1195 0.0130  -0.0061 0.0258  16  VAL A CB  
51   C CG1 . VAL A 48  ? 0.1944 0.1717 0.1337 0.0143  -0.0027 0.0247  16  VAL A CG1 
52   C CG2 . VAL A 48  ? 0.1880 0.1677 0.1427 0.0287  -0.0227 -0.0017 16  VAL A CG2 
53   N N   . LEU A 49  ? 0.1659 0.1590 0.1276 0.0328  -0.0064 -0.0163 17  LEU A N   
54   C CA  . LEU A 49  ? 0.1704 0.1468 0.1188 0.0265  -0.0029 -0.0054 17  LEU A CA  
55   C C   . LEU A 49  ? 0.1686 0.1437 0.0976 0.0183  -0.0208 -0.0108 17  LEU A C   
56   O O   . LEU A 49  ? 0.1726 0.1506 0.1102 0.0171  -0.0220 0.0032  17  LEU A O   
57   C CB  . LEU A 49  ? 0.2424 0.1751 0.1379 0.0107  0.0089  0.0008  17  LEU A CB  
58   C CG  . LEU A 49  ? 0.2801 0.1998 0.1522 -0.0192 0.0149  0.0108  17  LEU A CG  
59   C CD1 . LEU A 49  ? 0.3488 0.2374 0.2074 -0.0296 0.0232  -0.0010 17  LEU A CD1 
60   C CD2 . LEU A 49  ? 0.3106 0.2087 0.1490 -0.0259 0.0081  0.0219  17  LEU A CD2 
61   N N   . ASP A 50  ? 0.1610 0.1477 0.1065 0.0274  -0.0051 -0.0034 18  ASP A N   
62   C CA  . ASP A 50  ? 0.1576 0.1556 0.1162 0.0182  -0.0094 -0.0004 18  ASP A CA  
63   C C   . ASP A 50  ? 0.1756 0.1440 0.1094 0.0327  -0.0243 0.0048  18  ASP A C   
64   O O   . ASP A 50  ? 0.1887 0.1516 0.1104 0.0272  -0.0048 0.0150  18  ASP A O   
65   C CB  . ASP A 50  ? 0.1660 0.1637 0.1210 0.0076  -0.0211 -0.0080 18  ASP A CB  
66   C CG  . ASP A 50  ? 0.1936 0.1657 0.1548 0.0030  -0.0084 -0.0130 18  ASP A CG  
67   O OD1 . ASP A 50  ? 0.1893 0.1699 0.1393 0.0297  -0.0064 -0.0061 18  ASP A OD1 
68   O OD2 . ASP A 50  ? 0.2078 0.1952 0.1985 0.0068  -0.0117 -0.0411 18  ASP A OD2 
69   N N   . ALA A 51  ? 0.1818 0.1414 0.1094 0.0078  -0.0001 -0.0079 19  ALA A N   
70   C CA  . ALA A 51  ? 0.2288 0.1526 0.0986 0.0204  -0.0134 -0.0119 19  ALA A CA  
71   C C   . ALA A 51  ? 0.2524 0.1357 0.0881 0.0308  -0.0164 -0.0075 19  ALA A C   
72   O O   . ALA A 51  ? 0.3054 0.1219 0.1303 0.0303  -0.0125 -0.0089 19  ALA A O   
73   C CB  . ALA A 51  ? 0.2619 0.1726 0.1027 0.0010  -0.0272 -0.0108 19  ALA A CB  
74   N N   . VAL A 52  ? 0.2376 0.1678 0.1126 0.0511  -0.0177 0.0114  20  VAL A N   
75   C CA  . VAL A 52  ? 0.2483 0.1833 0.1249 0.0637  0.0118  0.0148  20  VAL A CA  
76   C C   . VAL A 52  ? 0.2246 0.1819 0.1356 0.0515  0.0149  0.0060  20  VAL A C   
77   O O   . VAL A 52  ? 0.2755 0.1907 0.1824 0.0931  0.0101  -0.0026 20  VAL A O   
78   C CB  . VAL A 52  ? 0.2425 0.1930 0.1383 0.0560  0.0365  0.0366  20  VAL A CB  
79   C CG1 . VAL A 52  ? 0.2814 0.2190 0.1729 0.0598  0.0524  0.0442  20  VAL A CG1 
80   C CG2 . VAL A 52  ? 0.2812 0.1854 0.1340 0.0764  0.0158  0.0352  20  VAL A CG2 
81   N N   . ARG A 53  ? 0.1904 0.2067 0.1391 0.0406  0.0052  0.0153  21  ARG A N   
82   C CA  . ARG A 53  ? 0.1988 0.2317 0.1744 0.0368  -0.0155 0.0183  21  ARG A CA  
83   C C   . ARG A 53  ? 0.2007 0.1999 0.1515 0.0368  -0.0059 0.0109  21  ARG A C   
84   O O   . ARG A 53  ? 0.2266 0.2208 0.1805 0.0475  -0.0313 0.0581  21  ARG A O   
85   C CB  . ARG A 53  ? 0.2140 0.2709 0.2317 0.0201  -0.0255 0.0233  21  ARG A CB  
86   C CG  . ARG A 53  ? 0.2461 0.3075 0.3151 0.0226  0.0005  0.0086  21  ARG A CG  
87   C CD  . ARG A 53  ? 0.2921 0.3475 0.3892 0.0229  0.0095  0.0061  21  ARG A CD  
88   N NE  . ARG A 53  ? 0.2769 0.3720 0.4490 0.0390  0.0071  0.0130  21  ARG A NE  
89   C CZ  . ARG A 53  ? 0.2837 0.4006 0.5049 0.0439  -0.0043 0.0248  21  ARG A CZ  
90   N NH1 . ARG A 53  ? 0.3199 0.4074 0.5175 0.0469  0.0138  0.0229  21  ARG A NH1 
91   N NH2 . ARG A 53  ? 0.2699 0.4061 0.5253 0.0451  -0.0264 0.0344  21  ARG A NH2 
92   N N   . GLY A 54  ? 0.2018 0.1538 0.1189 0.0309  0.0163  -0.0004 22  GLY A N   
93   C CA  . GLY A 54  ? 0.2334 0.1379 0.1308 0.0038  0.0169  -0.0019 22  GLY A CA  
94   C C   . GLY A 54  ? 0.2196 0.1296 0.1331 0.0163  0.0189  0.0107  22  GLY A C   
95   O O   . GLY A 54  ? 0.2381 0.1403 0.1247 0.0015  0.0040  0.0063  22  GLY A O   
96   N N   . SER A 55  ? 0.2337 0.1306 0.1302 0.0206  0.0133  -0.0048 23  SER A N   
97   C CA  . SER A 55  ? 0.2341 0.1484 0.1332 0.0373  -0.0171 -0.0155 23  SER A CA  
98   C C   . SER A 55  ? 0.2446 0.1482 0.1083 0.0390  -0.0253 0.0004  23  SER A C   
99   O O   . SER A 55  ? 0.2488 0.1604 0.1106 0.0396  -0.0357 -0.0002 23  SER A O   
100  C CB  . SER A 55  ? 0.2580 0.1884 0.1962 0.0333  -0.0250 -0.0028 23  SER A CB  
101  O OG  . SER A 55  ? 0.3351 0.2393 0.2486 0.0176  -0.0152 -0.0054 23  SER A OG  
102  N N   . PRO A 56  ? 0.2419 0.1417 0.1142 0.0324  -0.0342 0.0009  24  PRO A N   
103  C CA  . PRO A 56  ? 0.2070 0.1372 0.1330 0.0346  -0.0211 -0.0120 24  PRO A CA  
104  C C   . PRO A 56  ? 0.1956 0.1373 0.1601 0.0273  -0.0043 -0.0065 24  PRO A C   
105  O O   . PRO A 56  ? 0.2022 0.1494 0.1959 0.0260  -0.0100 0.0120  24  PRO A O   
106  C CB  . PRO A 56  ? 0.2783 0.1606 0.1344 0.0600  -0.0009 -0.0263 24  PRO A CB  
107  C CG  . PRO A 56  ? 0.3703 0.1985 0.1575 0.0782  -0.0068 -0.0137 24  PRO A CG  
108  C CD  . PRO A 56  ? 0.2891 0.1679 0.1300 0.0414  -0.0271 -0.0130 24  PRO A CD  
109  N N   . ALA A 57  ? 0.1947 0.1341 0.1599 0.0260  0.0032  0.0006  25  ALA A N   
110  C CA  . ALA A 57  ? 0.1913 0.1447 0.1551 0.0228  -0.0097 -0.0100 25  ALA A CA  
111  C C   . ALA A 57  ? 0.2101 0.1503 0.1413 0.0141  -0.0125 -0.0038 25  ALA A C   
112  O O   . ALA A 57  ? 0.2007 0.1613 0.1500 0.0137  -0.0097 -0.0192 25  ALA A O   
113  C CB  . ALA A 57  ? 0.1928 0.1644 0.1459 0.0335  -0.0219 -0.0117 25  ALA A CB  
114  N N   . ILE A 58  ? 0.2003 0.1725 0.1488 0.0098  -0.0344 0.0006  26  ILE A N   
115  C CA  . ILE A 58  ? 0.1901 0.1763 0.1685 0.0034  -0.0382 0.0022  26  ILE A CA  
116  C C   . ILE A 58  ? 0.1884 0.1783 0.2040 -0.0039 -0.0372 -0.0115 26  ILE A C   
117  O O   . ILE A 58  ? 0.1968 0.1953 0.2234 -0.0010 0.0008  -0.0024 26  ILE A O   
118  C CB  . ILE A 58  ? 0.2823 0.1982 0.1936 0.0135  -0.0510 0.0050  26  ILE A CB  
119  C CG1 . ILE A 58  ? 0.3091 0.2138 0.2033 0.0457  -0.0688 0.0175  26  ILE A CG1 
120  C CG2 . ILE A 58  ? 0.3116 0.2175 0.2270 -0.0112 -0.0495 -0.0075 26  ILE A CG2 
121  C CD1 . ILE A 58  ? 0.3676 0.2368 0.2162 0.0377  -0.0580 0.0150  26  ILE A CD1 
122  N N   . ASN A 59  ? 0.2062 0.1720 0.2143 0.0016  -0.0601 -0.0056 27  ASN A N   
123  C CA  . ASN A 59  ? 0.2191 0.1942 0.2485 -0.0288 -0.0456 -0.0024 27  ASN A CA  
124  C C   . ASN A 59  ? 0.2146 0.1762 0.2338 -0.0148 -0.0161 0.0015  27  ASN A C   
125  O O   . ASN A 59  ? 0.2140 0.1963 0.2701 -0.0454 -0.0016 0.0139  27  ASN A O   
126  C CB  . ASN A 59  ? 0.2450 0.2512 0.2965 -0.0274 -0.0718 0.0040  27  ASN A CB  
127  C CG  . ASN A 59  ? 0.3007 0.3323 0.3538 -0.0148 -0.0794 -0.0075 27  ASN A CG  
128  O OD1 . ASN A 59  ? 0.3301 0.3788 0.3762 -0.0097 -0.0852 -0.0188 27  ASN A OD1 
129  N ND2 . ASN A 59  ? 0.3347 0.3436 0.3807 -0.0035 -0.0934 -0.0003 27  ASN A ND2 
130  N N   . VAL A 60  ? 0.2007 0.1703 0.1762 0.0165  -0.0093 -0.0106 28  VAL A N   
131  C CA  . VAL A 60  ? 0.2037 0.1422 0.1618 0.0135  0.0104  -0.0124 28  VAL A CA  
132  C C   . VAL A 60  ? 0.1914 0.1517 0.1484 0.0238  0.0023  -0.0129 28  VAL A C   
133  O O   . VAL A 60  ? 0.1842 0.1636 0.1312 0.0076  0.0039  -0.0100 28  VAL A O   
134  C CB  . VAL A 60  ? 0.2480 0.1289 0.1521 0.0081  0.0058  -0.0150 28  VAL A CB  
135  C CG1 . VAL A 60  ? 0.2903 0.1396 0.1554 0.0329  -0.0044 -0.0116 28  VAL A CG1 
136  C CG2 . VAL A 60  ? 0.2729 0.1454 0.1766 0.0450  0.0167  -0.0043 28  VAL A CG2 
137  N N   . ALA A 61  ? 0.1810 0.1488 0.1440 0.0232  -0.0022 -0.0080 29  ALA A N   
138  C CA  . ALA A 61  ? 0.1629 0.1485 0.1470 0.0075  -0.0007 -0.0136 29  ALA A CA  
139  C C   . ALA A 61  ? 0.1796 0.1428 0.1281 0.0138  -0.0150 -0.0087 29  ALA A C   
140  O O   . ALA A 61  ? 0.2099 0.1757 0.1063 -0.0046 -0.0005 -0.0127 29  ALA A O   
141  C CB  . ALA A 61  ? 0.1934 0.1519 0.1730 -0.0135 -0.0103 -0.0143 29  ALA A CB  
142  N N   . MET A 62  ? 0.1783 0.1360 0.1234 0.0178  -0.0191 -0.0144 30  MET A N   
143  C CA  . MET A 62  ? 0.1826 0.1382 0.1504 0.0124  -0.0508 -0.0219 30  MET A CA  
144  C C   . MET A 62  ? 0.1716 0.1550 0.1198 0.0133  -0.0313 -0.0186 30  MET A C   
145  O O   . MET A 62  ? 0.1809 0.1726 0.1253 0.0112  -0.0187 -0.0158 30  MET A O   
146  C CB  . MET A 62  ? 0.2073 0.1692 0.1897 -0.0195 -0.0219 0.0030  30  MET A CB  
147  C CG  . MET A 62  ? 0.2100 0.1807 0.2069 -0.0216 -0.0140 0.0101  30  MET A CG  
148  S SD  . MET A 62  ? 0.1989 0.1970 0.2254 -0.0256 -0.0428 0.0347  30  MET A SD  
149  C CE  . MET A 62  ? 0.2268 0.2132 0.2252 0.0056  -0.0311 0.0397  30  MET A CE  
150  N N   . HIS A 63  ? 0.1475 0.1667 0.1339 0.0260  -0.0242 -0.0155 31  HIS A N   
151  C CA  . HIS A 63  ? 0.1568 0.1742 0.1515 0.0245  -0.0152 -0.0091 31  HIS A CA  
152  C C   . HIS A 63  ? 0.1718 0.1871 0.1461 0.0054  -0.0112 -0.0519 31  HIS A C   
153  O O   . HIS A 63  ? 0.1836 0.2233 0.1629 0.0051  0.0015  -0.0620 31  HIS A O   
154  C CB  . HIS A 63  ? 0.1951 0.1876 0.2036 0.0073  -0.0224 0.0204  31  HIS A CB  
155  C CG  . HIS A 63  ? 0.2027 0.1973 0.2457 -0.0061 -0.0348 0.0242  31  HIS A CG  
156  N ND1 . HIS A 63  ? 0.2261 0.2200 0.2723 -0.0396 -0.0537 0.0219  31  HIS A ND1 
157  C CD2 . HIS A 63  ? 0.2036 0.2003 0.2541 -0.0037 -0.0364 0.0317  31  HIS A CD2 
158  C CE1 . HIS A 63  ? 0.2038 0.2118 0.2860 -0.0364 -0.0541 0.0114  31  HIS A CE1 
159  N NE2 . HIS A 63  ? 0.2256 0.1977 0.2745 -0.0188 -0.0272 0.0360  31  HIS A NE2 
160  N N   . VAL A 64  ? 0.1677 0.1837 0.1346 0.0164  -0.0306 -0.0519 32  VAL A N   
161  C CA  . VAL A 64  ? 0.1793 0.1674 0.1544 0.0186  -0.0353 -0.0310 32  VAL A CA  
162  C C   . VAL A 64  ? 0.1679 0.1639 0.1582 0.0040  -0.0293 -0.0388 32  VAL A C   
163  O O   . VAL A 64  ? 0.2017 0.1817 0.1491 0.0063  -0.0226 -0.0479 32  VAL A O   
164  C CB  . VAL A 64  ? 0.1838 0.1854 0.1639 0.0076  -0.0229 -0.0308 32  VAL A CB  
165  C CG1 . VAL A 64  ? 0.1582 0.1992 0.1772 0.0065  -0.0247 -0.0287 32  VAL A CG1 
166  C CG2 . VAL A 64  ? 0.2088 0.1964 0.1631 0.0038  -0.0376 -0.0277 32  VAL A CG2 
167  N N   . PHE A 65  ? 0.1653 0.1520 0.1695 0.0101  -0.0269 -0.0214 33  PHE A N   
168  C CA  . PHE A 65  ? 0.1732 0.1525 0.1591 0.0037  -0.0250 -0.0318 33  PHE A CA  
169  C C   . PHE A 65  ? 0.1841 0.1442 0.1483 0.0161  -0.0218 -0.0308 33  PHE A C   
170  O O   . PHE A 65  ? 0.1811 0.1266 0.1474 0.0031  -0.0102 -0.0409 33  PHE A O   
171  C CB  . PHE A 65  ? 0.1972 0.1905 0.1688 0.0043  0.0163  -0.0186 33  PHE A CB  
172  C CG  . PHE A 65  ? 0.2110 0.2127 0.2147 -0.0068 0.0186  -0.0131 33  PHE A CG  
173  C CD1 . PHE A 65  ? 0.2372 0.2412 0.2375 0.0150  0.0235  -0.0125 33  PHE A CD1 
174  C CD2 . PHE A 65  ? 0.2384 0.2401 0.2620 -0.0239 0.0324  -0.0031 33  PHE A CD2 
175  C CE1 . PHE A 65  ? 0.2547 0.2565 0.2555 0.0067  0.0345  -0.0134 33  PHE A CE1 
176  C CE2 . PHE A 65  ? 0.2692 0.2589 0.2827 -0.0216 0.0313  -0.0122 33  PHE A CE2 
177  C CZ  . PHE A 65  ? 0.2345 0.2646 0.2785 -0.0102 0.0321  -0.0117 33  PHE A CZ  
178  N N   . ARG A 66  ? 0.1708 0.1573 0.1793 0.0206  -0.0191 -0.0354 34  ARG A N   
179  C CA  . ARG A 66  ? 0.1827 0.1594 0.1913 0.0155  -0.0212 -0.0350 34  ARG A CA  
180  C C   . ARG A 66  ? 0.1789 0.1546 0.2088 0.0136  -0.0136 -0.0206 34  ARG A C   
181  O O   . ARG A 66  ? 0.2338 0.1574 0.2303 0.0077  -0.0236 -0.0255 34  ARG A O   
182  C CB  . ARG A 66  ? 0.1923 0.1808 0.1995 0.0136  -0.0275 -0.0208 34  ARG A CB  
183  C CG  . ARG A 66  ? 0.2098 0.2000 0.2148 0.0168  0.0017  -0.0202 34  ARG A CG  
184  C CD  . ARG A 66  ? 0.2237 0.2112 0.2314 0.0210  0.0428  -0.0254 34  ARG A CD  
185  N NE  . ARG A 66  ? 0.2794 0.2173 0.2564 0.0339  0.0512  -0.0176 34  ARG A NE  
186  C CZ  . ARG A 66  ? 0.2990 0.2178 0.2600 0.0297  0.0802  0.0044  34  ARG A CZ  
187  N NH1 . ARG A 66  ? 0.3072 0.2262 0.2810 0.0395  0.0764  0.0112  34  ARG A NH1 
188  N NH2 . ARG A 66  ? 0.2911 0.2076 0.2606 -0.0149 0.0713  0.0137  34  ARG A NH2 
189  N N   . LYS A 67  ? 0.1998 0.1591 0.2161 0.0128  -0.0264 -0.0064 35  LYS A N   
190  C CA  . LYS A 67  ? 0.2170 0.1756 0.2422 -0.0006 -0.0292 0.0031  35  LYS A CA  
191  C C   . LYS A 67  ? 0.2382 0.1693 0.2318 0.0186  -0.0172 0.0201  35  LYS A C   
192  O O   . LYS A 67  ? 0.2353 0.1845 0.2303 0.0357  0.0077  0.0131  35  LYS A O   
193  C CB  . LYS A 67  ? 0.2824 0.2212 0.3262 0.0000  -0.0782 0.0274  35  LYS A CB  
194  C CG  . LYS A 67  ? 0.3987 0.2863 0.4288 0.0024  -0.1081 0.0446  35  LYS A CG  
195  C CD  . LYS A 67  ? 0.4960 0.3345 0.5233 0.0135  -0.1084 0.0593  35  LYS A CD  
196  C CE  . LYS A 67  ? 0.5521 0.3624 0.5903 0.0331  -0.1175 0.0709  35  LYS A CE  
197  N NZ  . LYS A 67  ? 0.5643 0.3777 0.6265 0.0482  -0.1124 0.0762  35  LYS A NZ  
198  N N   . ALA A 68  ? 0.2726 0.1702 0.2275 0.0365  0.0010  0.0066  36  ALA A N   
199  C CA  . ALA A 68  ? 0.3083 0.1984 0.2535 0.0355  0.0073  0.0155  36  ALA A CA  
200  C C   . ALA A 68  ? 0.3277 0.2441 0.2789 0.0692  0.0347  0.0333  36  ALA A C   
201  O O   . ALA A 68  ? 0.2856 0.2582 0.2929 0.0703  0.0137  0.0223  36  ALA A O   
202  C CB  . ALA A 68  ? 0.3164 0.1840 0.2568 0.0148  -0.0208 0.0095  36  ALA A CB  
203  N N   . ALA A 69  ? 0.3726 0.2755 0.2958 0.1125  0.0545  0.0765  37  ALA A N   
204  C CA  . ALA A 69  ? 0.4439 0.3148 0.3308 0.1305  0.0643  0.0910  37  ALA A CA  
205  C C   . ALA A 69  ? 0.5006 0.3366 0.3536 0.1326  0.0544  0.1055  37  ALA A C   
206  O O   . ALA A 69  ? 0.5345 0.3663 0.3762 0.1335  0.0597  0.0994  37  ALA A O   
207  C CB  . ALA A 69  ? 0.4579 0.3200 0.3433 0.1427  0.0684  0.0857  37  ALA A CB  
208  N N   . ASP A 70  ? 0.5093 0.3221 0.3617 0.1339  0.0527  0.1174  38  ASP A N   
209  C CA  . ASP A 70  ? 0.5308 0.3295 0.3874 0.1146  0.0546  0.1128  38  ASP A CA  
210  C C   . ASP A 70  ? 0.5124 0.3473 0.3939 0.1327  0.0622  0.1135  38  ASP A C   
211  O O   . ASP A 70  ? 0.5117 0.3505 0.3839 0.1273  0.0605  0.1334  38  ASP A O   
212  C CB  . ASP A 70  ? 0.5568 0.3125 0.4164 0.0875  0.0355  0.1053  38  ASP A CB  
213  C CG  . ASP A 70  ? 0.5814 0.3036 0.4461 0.0419  0.0279  0.0945  38  ASP A CG  
214  O OD1 . ASP A 70  ? 0.5583 0.2885 0.4419 0.0377  0.0191  0.0995  38  ASP A OD1 
215  O OD2 . ASP A 70  ? 0.6171 0.2961 0.4676 0.0107  0.0334  0.0839  38  ASP A OD2 
216  N N   . ASP A 71  ? 0.5021 0.3668 0.4176 0.1476  0.0649  0.0924  39  ASP A N   
217  C CA  . ASP A 71  ? 0.5285 0.3871 0.4589 0.1419  0.0970  0.0667  39  ASP A CA  
218  C C   . ASP A 71  ? 0.4652 0.3632 0.4361 0.1039  0.1227  0.0597  39  ASP A C   
219  O O   . ASP A 71  ? 0.4957 0.3851 0.4523 0.0792  0.1404  0.0387  39  ASP A O   
220  C CB  . ASP A 71  ? 0.6143 0.4318 0.5242 0.1708  0.1045  0.0507  39  ASP A CB  
221  C CG  . ASP A 71  ? 0.6924 0.4675 0.5845 0.1987  0.1047  0.0335  39  ASP A CG  
222  O OD1 . ASP A 71  ? 0.7348 0.4857 0.6095 0.1975  0.0954  0.0292  39  ASP A OD1 
223  O OD2 . ASP A 71  ? 0.7173 0.4808 0.6086 0.2146  0.1078  0.0308  39  ASP A OD2 
224  N N   . THR A 72  ? 0.3814 0.3121 0.3929 0.0795  0.1145  0.0821  40  THR A N   
225  C CA  . THR A 72  ? 0.3607 0.2791 0.3860 0.0327  0.0778  0.0715  40  THR A CA  
226  C C   . THR A 72  ? 0.2669 0.2433 0.3472 0.0148  0.0508  0.0514  40  THR A C   
227  O O   . THR A 72  ? 0.2613 0.2453 0.3439 -0.0059 0.0396  0.0368  40  THR A O   
228  C CB  . THR A 72  ? 0.4140 0.2826 0.4125 -0.0081 0.0803  0.0835  40  THR A CB  
229  O OG1 . THR A 72  ? 0.4307 0.2860 0.4385 -0.0229 0.0877  0.0624  40  THR A OG1 
230  C CG2 . THR A 72  ? 0.4479 0.2888 0.4277 0.0007  0.0677  0.0934  40  THR A CG2 
231  N N   . TRP A 73  ? 0.2604 0.2387 0.3262 -0.0119 0.0450  0.0531  41  TRP A N   
232  C CA  . TRP A 73  ? 0.2476 0.2290 0.3138 -0.0231 0.0313  0.0260  41  TRP A CA  
233  C C   . TRP A 73  ? 0.2671 0.2205 0.3254 -0.0515 -0.0016 -0.0096 41  TRP A C   
234  O O   . TRP A 73  ? 0.3143 0.2940 0.3619 -0.0913 0.0319  -0.0301 41  TRP A O   
235  C CB  . TRP A 73  ? 0.2261 0.2294 0.2934 -0.0212 0.0533  0.0156  41  TRP A CB  
236  C CG  . TRP A 73  ? 0.2597 0.2455 0.2892 -0.0132 0.0404  0.0130  41  TRP A CG  
237  C CD1 . TRP A 73  ? 0.3044 0.2614 0.2952 -0.0174 0.0412  0.0195  41  TRP A CD1 
238  C CD2 . TRP A 73  ? 0.2431 0.2352 0.2858 0.0007  0.0230  0.0063  41  TRP A CD2 
239  N NE1 . TRP A 73  ? 0.3340 0.2662 0.2973 -0.0273 0.0389  0.0188  41  TRP A NE1 
240  C CE2 . TRP A 73  ? 0.2984 0.2482 0.2912 -0.0240 0.0210  0.0138  41  TRP A CE2 
241  C CE3 . TRP A 73  ? 0.2132 0.2143 0.2922 0.0026  0.0066  0.0116  41  TRP A CE3 
242  C CZ2 . TRP A 73  ? 0.3146 0.2424 0.3001 -0.0031 0.0055  -0.0046 41  TRP A CZ2 
243  C CZ3 . TRP A 73  ? 0.2424 0.2106 0.2911 0.0112  -0.0058 0.0058  41  TRP A CZ3 
244  C CH2 . TRP A 73  ? 0.2761 0.2114 0.3003 0.0019  0.0047  0.0024  41  TRP A CH2 
245  N N   . GLU A 74  ? 0.2653 0.1900 0.3107 -0.0176 -0.0662 -0.0196 42  GLU A N   
246  C CA  . GLU A 74  ? 0.3396 0.2152 0.3254 0.0073  -0.0906 -0.0225 42  GLU A CA  
247  C C   . GLU A 74  ? 0.2717 0.1793 0.3026 -0.0007 -0.0692 -0.0269 42  GLU A C   
248  O O   . GLU A 74  ? 0.2370 0.1578 0.3046 0.0048  -0.0507 -0.0423 42  GLU A O   
249  C CB  . GLU A 74  ? 0.5240 0.2788 0.3879 0.0354  -0.1040 -0.0241 42  GLU A CB  
250  C CG  . GLU A 74  ? 0.7328 0.3370 0.4566 0.0307  -0.0882 -0.0211 42  GLU A CG  
251  C CD  . GLU A 74  ? 0.9183 0.3791 0.5067 0.0145  -0.0695 -0.0171 42  GLU A CD  
252  O OE1 . GLU A 74  ? 1.0016 0.3833 0.5245 0.0141  -0.0620 -0.0084 42  GLU A OE1 
253  O OE2 . GLU A 74  ? 0.9697 0.3922 0.5245 -0.0065 -0.0668 -0.0232 42  GLU A OE2 
254  N N   . PRO A 75  ? 0.2665 0.1670 0.3037 -0.0158 -0.0588 -0.0354 43  PRO A N   
255  C CA  . PRO A 75  ? 0.2773 0.1871 0.2949 -0.0244 -0.0629 -0.0392 43  PRO A CA  
256  C C   . PRO A 75  ? 0.3131 0.1938 0.2519 0.0040  -0.0261 -0.0513 43  PRO A C   
257  O O   . PRO A 75  ? 0.4006 0.2185 0.2627 0.0464  0.0077  -0.0402 43  PRO A O   
258  C CB  . PRO A 75  ? 0.3011 0.1987 0.3357 -0.0567 -0.0930 -0.0327 43  PRO A CB  
259  C CG  . PRO A 75  ? 0.3213 0.2078 0.3565 -0.0473 -0.0926 -0.0083 43  PRO A CG  
260  C CD  . PRO A 75  ? 0.2846 0.1897 0.3355 -0.0459 -0.0861 -0.0186 43  PRO A CD  
261  N N   . PHE A 76  ? 0.2297 0.1923 0.2095 -0.0021 -0.0275 -0.0416 44  PHE A N   
262  C CA  . PHE A 76  ? 0.1831 0.1998 0.1865 0.0150  -0.0147 -0.0526 44  PHE A CA  
263  C C   . PHE A 76  ? 0.1609 0.2129 0.1752 0.0341  -0.0102 -0.0564 44  PHE A C   
264  O O   . PHE A 76  ? 0.2282 0.2324 0.1788 0.0494  -0.0133 -0.0650 44  PHE A O   
265  C CB  . PHE A 76  ? 0.2104 0.2092 0.1826 -0.0067 -0.0106 -0.0557 44  PHE A CB  
266  C CG  . PHE A 76  ? 0.1960 0.2220 0.1684 0.0063  -0.0026 -0.0474 44  PHE A CG  
267  C CD1 . PHE A 76  ? 0.2234 0.2242 0.1791 0.0123  0.0270  -0.0543 44  PHE A CD1 
268  C CD2 . PHE A 76  ? 0.2125 0.2289 0.1823 -0.0052 -0.0202 -0.0334 44  PHE A CD2 
269  C CE1 . PHE A 76  ? 0.2774 0.2368 0.1843 -0.0024 0.0155  -0.0556 44  PHE A CE1 
270  C CE2 . PHE A 76  ? 0.2379 0.2487 0.1846 -0.0058 -0.0367 -0.0278 44  PHE A CE2 
271  C CZ  . PHE A 76  ? 0.2512 0.2479 0.1869 -0.0109 -0.0127 -0.0422 44  PHE A CZ  
272  N N   . ALA A 77  ? 0.1656 0.1956 0.1754 0.0241  -0.0492 -0.0564 45  ALA A N   
273  C CA  . ALA A 77  ? 0.1848 0.1862 0.1745 0.0280  -0.0408 -0.0552 45  ALA A CA  
274  C C   . ALA A 77  ? 0.1632 0.1705 0.1545 0.0240  -0.0246 -0.0518 45  ALA A C   
275  O O   . ALA A 77  ? 0.1891 0.1939 0.1500 0.0048  -0.0356 -0.0522 45  ALA A O   
276  C CB  . ALA A 77  ? 0.2414 0.2129 0.1950 0.0368  0.0025  -0.0316 45  ALA A CB  
277  N N   . SER A 78  ? 0.1886 0.1766 0.1553 0.0339  -0.0312 -0.0465 46  SER A N   
278  C CA  . SER A 78  ? 0.1661 0.1673 0.1638 0.0039  -0.0320 -0.0345 46  SER A CA  
279  C C   . SER A 78  ? 0.1742 0.1705 0.1345 0.0094  -0.0348 -0.0376 46  SER A C   
280  O O   . SER A 78  ? 0.2365 0.2160 0.1285 0.0340  -0.0136 -0.0501 46  SER A O   
281  C CB  . SER A 78  ? 0.1993 0.1831 0.1852 -0.0118 -0.0569 -0.0354 46  SER A CB  
282  O OG  . SER A 78  ? 0.2141 0.1826 0.2373 0.0047  -0.0956 -0.0396 46  SER A OG  
283  N N   . GLY A 79  ? 0.1656 0.1369 0.1213 0.0100  -0.0201 -0.0228 47  GLY A N   
284  C CA  . GLY A 79  ? 0.1855 0.1446 0.1029 0.0242  -0.0234 -0.0046 47  GLY A CA  
285  C C   . GLY A 79  ? 0.1900 0.1433 0.1140 0.0158  -0.0168 -0.0141 47  GLY A C   
286  O O   . GLY A 79  ? 0.2033 0.1590 0.1010 0.0074  -0.0095 -0.0117 47  GLY A O   
287  N N   . LYS A 80  ? 0.1987 0.1498 0.1304 0.0201  -0.0143 -0.0285 48  LYS A N   
288  C CA  . LYS A 80  ? 0.2248 0.1511 0.1775 -0.0034 0.0209  -0.0194 48  LYS A CA  
289  C C   . LYS A 80  ? 0.2143 0.1497 0.1548 0.0186  -0.0038 -0.0087 48  LYS A C   
290  O O   . LYS A 80  ? 0.2439 0.1556 0.1603 -0.0014 0.0033  -0.0148 48  LYS A O   
291  C CB  . LYS A 80  ? 0.3055 0.1944 0.2614 0.0030  0.0383  -0.0181 48  LYS A CB  
292  C CG  . LYS A 80  ? 0.3841 0.2463 0.3299 -0.0128 0.0557  -0.0126 48  LYS A CG  
293  C CD  . LYS A 80  ? 0.4619 0.2783 0.3904 -0.0489 0.0766  -0.0108 48  LYS A CD  
294  C CE  . LYS A 80  ? 0.5223 0.2889 0.4110 -0.0464 0.0968  -0.0258 48  LYS A CE  
295  N NZ  . LYS A 80  ? 0.5305 0.2692 0.4057 -0.0607 0.1129  -0.0473 48  LYS A NZ  
296  N N   . THR A 81  ? 0.1975 0.1334 0.1519 0.0029  -0.0057 -0.0126 49  THR A N   
297  C CA  . THR A 81  ? 0.2212 0.1284 0.1339 0.0106  -0.0433 -0.0108 49  THR A CA  
298  C C   . THR A 81  ? 0.2267 0.1519 0.1531 -0.0007 -0.0433 -0.0137 49  THR A C   
299  O O   . THR A 81  ? 0.2329 0.1635 0.1745 0.0206  -0.0267 -0.0181 49  THR A O   
300  C CB  . THR A 81  ? 0.1929 0.1479 0.1176 -0.0071 -0.0306 -0.0151 49  THR A CB  
301  O OG1 . THR A 81  ? 0.1915 0.1542 0.1363 -0.0052 -0.0131 -0.0115 49  THR A OG1 
302  C CG2 . THR A 81  ? 0.2258 0.1639 0.1295 0.0028  -0.0577 0.0131  49  THR A CG2 
303  N N   . SER A 82  ? 0.2453 0.1612 0.1352 -0.0067 -0.0361 0.0036  50  SER A N   
304  C CA  . SER A 82  ? 0.2532 0.1810 0.1529 0.0162  -0.0383 0.0126  50  SER A CA  
305  C C   . SER A 82  ? 0.2918 0.1965 0.1582 0.0132  -0.0545 -0.0157 50  SER A C   
306  O O   . SER A 82  ? 0.2833 0.1821 0.1563 0.0398  -0.0327 -0.0381 50  SER A O   
307  C CB  . SER A 82  ? 0.2951 0.1938 0.1776 -0.0048 -0.0283 -0.0010 50  SER A CB  
308  O OG  . SER A 82  ? 0.3395 0.2210 0.2183 -0.0157 -0.0483 0.0291  50  SER A OG  
309  N N   . GLU A 83  ? 0.3192 0.2300 0.1935 0.0419  -0.0777 -0.0016 51  GLU A N   
310  C CA  . GLU A 83  ? 0.3410 0.2537 0.2462 0.0651  -0.1033 0.0054  51  GLU A CA  
311  C C   . GLU A 83  ? 0.3295 0.2306 0.1988 0.0594  -0.0522 0.0032  51  GLU A C   
312  O O   . GLU A 83  ? 0.3444 0.2394 0.2125 0.0778  -0.0270 -0.0145 51  GLU A O   
313  C CB  . GLU A 83  ? 0.4300 0.3141 0.3905 0.0906  -0.1184 0.0109  51  GLU A CB  
314  C CG  . GLU A 83  ? 0.5690 0.3895 0.5387 0.0730  -0.1087 0.0086  51  GLU A CG  
315  C CD  . GLU A 83  ? 0.6691 0.4420 0.6597 0.0640  -0.1054 0.0055  51  GLU A CD  
316  O OE1 . GLU A 83  ? 0.7087 0.4583 0.6938 0.0721  -0.1014 0.0008  51  GLU A OE1 
317  O OE2 . GLU A 83  ? 0.7008 0.4692 0.7119 0.0516  -0.1100 0.0091  51  GLU A OE2 
318  N N   . SER A 84  ? 0.3310 0.2225 0.1584 0.0467  -0.0449 0.0095  52  SER A N   
319  C CA  . SER A 84  ? 0.3187 0.2185 0.1486 0.0418  -0.0167 -0.0017 52  SER A CA  
320  C C   . SER A 84  ? 0.2700 0.1893 0.1338 0.0362  -0.0077 0.0049  52  SER A C   
321  O O   . SER A 84  ? 0.2904 0.1896 0.1577 0.0124  0.0077  0.0098  52  SER A O   
322  C CB  . SER A 84  ? 0.3524 0.2490 0.1754 0.0236  0.0001  0.0068  52  SER A CB  
323  O OG  . SER A 84  ? 0.4251 0.2806 0.2062 0.0000  0.0147  -0.0330 52  SER A OG  
324  N N   . GLY A 85  ? 0.2196 0.1770 0.1140 0.0377  -0.0034 0.0228  53  GLY A N   
325  C CA  . GLY A 85  ? 0.1926 0.1853 0.1077 0.0375  -0.0134 0.0093  53  GLY A CA  
326  C C   . GLY A 85  ? 0.1801 0.1924 0.1038 0.0265  -0.0154 0.0009  53  GLY A C   
327  O O   . GLY A 85  ? 0.1764 0.2027 0.1147 0.0038  -0.0302 -0.0070 53  GLY A O   
328  N N   . GLU A 86  ? 0.2286 0.1875 0.1237 0.0438  0.0122  0.0002  54  GLU A N   
329  C CA  . GLU A 86  ? 0.2426 0.1791 0.1206 0.0381  0.0017  -0.0132 54  GLU A CA  
330  C C   . GLU A 86  ? 0.2153 0.1936 0.1184 0.0311  -0.0234 -0.0209 54  GLU A C   
331  O O   . GLU A 86  ? 0.2086 0.2227 0.1364 0.0427  -0.0391 -0.0353 54  GLU A O   
332  C CB  . GLU A 86  ? 0.3113 0.1878 0.1579 0.0197  0.0050  0.0056  54  GLU A CB  
333  C CG  . GLU A 86  ? 0.3577 0.1878 0.1922 0.0200  0.0179  0.0096  54  GLU A CG  
334  C CD  . GLU A 86  ? 0.4365 0.2149 0.2466 0.0210  0.0384  0.0124  54  GLU A CD  
335  O OE1 . GLU A 86  ? 0.4731 0.2388 0.2710 0.0056  0.0699  0.0291  54  GLU A OE1 
336  O OE2 . GLU A 86  ? 0.4901 0.2480 0.2915 -0.0034 0.0215  0.0028  54  GLU A OE2 
337  N N   . LEU A 87  ? 0.1948 0.1749 0.1297 0.0223  -0.0120 -0.0298 55  LEU A N   
338  C CA  . LEU A 87  ? 0.1877 0.1706 0.1401 0.0140  -0.0189 -0.0322 55  LEU A CA  
339  C C   . LEU A 87  ? 0.1934 0.1798 0.1330 0.0309  -0.0178 -0.0309 55  LEU A C   
340  O O   . LEU A 87  ? 0.1924 0.2012 0.1514 -0.0026 -0.0029 -0.0228 55  LEU A O   
341  C CB  . LEU A 87  ? 0.1858 0.1674 0.1507 0.0145  -0.0289 -0.0233 55  LEU A CB  
342  C CG  . LEU A 87  ? 0.2071 0.1697 0.1630 0.0153  -0.0338 -0.0129 55  LEU A CG  
343  C CD1 . LEU A 87  ? 0.2319 0.1776 0.1729 0.0205  -0.0305 -0.0449 55  LEU A CD1 
344  C CD2 . LEU A 87  ? 0.2207 0.1812 0.1838 0.0196  -0.0288 0.0076  55  LEU A CD2 
345  N N   . HIS A 88  ? 0.2477 0.2069 0.1349 0.0248  0.0078  -0.0320 56  HIS A N   
346  C CA  . HIS A 88  ? 0.2587 0.2286 0.1508 0.0395  0.0314  -0.0034 56  HIS A CA  
347  C C   . HIS A 88  ? 0.2819 0.2574 0.1811 0.0422  0.0013  -0.0194 56  HIS A C   
348  O O   . HIS A 88  ? 0.3061 0.2590 0.2045 0.0286  0.0102  -0.0245 56  HIS A O   
349  C CB  . HIS A 88  ? 0.3024 0.2390 0.1572 0.0123  0.0376  0.0132  56  HIS A CB  
350  C CG  . HIS A 88  ? 0.3428 0.2512 0.1835 0.0113  0.0533  0.0234  56  HIS A CG  
351  N ND1 . HIS A 88  ? 0.3640 0.2688 0.2084 0.0022  0.0410  0.0331  56  HIS A ND1 
352  C CD2 . HIS A 88  ? 0.3822 0.2500 0.2045 0.0114  0.0686  0.0185  56  HIS A CD2 
353  C CE1 . HIS A 88  ? 0.3777 0.2564 0.2102 -0.0119 0.0470  0.0289  56  HIS A CE1 
354  N NE2 . HIS A 88  ? 0.3851 0.2529 0.2039 0.0025  0.0537  0.0210  56  HIS A NE2 
355  N N   . GLY A 89  ? 0.2626 0.2641 0.1885 0.0630  0.0106  -0.0349 57  GLY A N   
356  C CA  . GLY A 89  ? 0.2943 0.2559 0.2139 0.0710  -0.0059 -0.0443 57  GLY A CA  
357  C C   . GLY A 89  ? 0.2692 0.2427 0.2291 0.0500  -0.0465 -0.0575 57  GLY A C   
358  O O   . GLY A 89  ? 0.3055 0.2418 0.2433 0.0435  -0.0647 -0.0804 57  GLY A O   
359  N N   . LEU A 90  ? 0.2380 0.2389 0.2047 0.0437  -0.0265 -0.0585 58  LEU A N   
360  C CA  . LEU A 90  ? 0.2075 0.2227 0.1987 0.0271  -0.0060 -0.0606 58  LEU A CA  
361  C C   . LEU A 90  ? 0.2187 0.2289 0.2110 0.0216  -0.0083 -0.0628 58  LEU A C   
362  O O   . LEU A 90  ? 0.2275 0.2240 0.2354 0.0441  0.0025  -0.0543 58  LEU A O   
363  C CB  . LEU A 90  ? 0.2442 0.2113 0.1985 0.0316  0.0181  -0.0669 58  LEU A CB  
364  C CG  . LEU A 90  ? 0.2515 0.2028 0.2216 0.0334  0.0087  -0.0575 58  LEU A CG  
365  C CD1 . LEU A 90  ? 0.2891 0.2012 0.2063 0.0477  0.0081  -0.0663 58  LEU A CD1 
366  C CD2 . LEU A 90  ? 0.2770 0.2039 0.2562 0.0249  0.0188  -0.0430 58  LEU A CD2 
367  N N   . THR A 91  ? 0.1969 0.2374 0.1801 0.0311  0.0089  -0.0654 59  THR A N   
368  C CA  . THR A 91  ? 0.1975 0.2270 0.1694 0.0378  0.0114  -0.0529 59  THR A CA  
369  C C   . THR A 91  ? 0.2449 0.2419 0.1856 0.0470  -0.0047 -0.0410 59  THR A C   
370  O O   . THR A 91  ? 0.2731 0.2647 0.2231 0.0660  0.0386  -0.0219 59  THR A O   
371  C CB  . THR A 91  ? 0.2330 0.2283 0.1854 0.0347  -0.0071 -0.0318 59  THR A CB  
372  O OG1 . THR A 91  ? 0.2247 0.2372 0.1804 0.0424  0.0070  -0.0066 59  THR A OG1 
373  C CG2 . THR A 91  ? 0.2520 0.2202 0.1815 0.0265  -0.0164 -0.0208 59  THR A CG2 
374  N N   . THR A 92  ? 0.2748 0.2438 0.1688 0.0567  -0.0106 -0.0325 60  THR A N   
375  C CA  . THR A 92  ? 0.2986 0.2500 0.1602 0.0641  0.0057  -0.0256 60  THR A CA  
376  C C   . THR A 92  ? 0.2767 0.2364 0.1492 0.0507  0.0423  -0.0213 60  THR A C   
377  O O   . THR A 92  ? 0.2549 0.2423 0.1355 0.0214  0.0221  -0.0208 60  THR A O   
378  C CB  . THR A 92  ? 0.3139 0.2858 0.1696 0.0771  -0.0109 -0.0313 60  THR A CB  
379  O OG1 . THR A 92  ? 0.3082 0.2890 0.1779 0.0808  -0.0009 -0.0323 60  THR A OG1 
380  C CG2 . THR A 92  ? 0.3501 0.3053 0.1702 0.0606  -0.0240 -0.0630 60  THR A CG2 
381  N N   . GLU A 93  ? 0.2911 0.2398 0.1787 0.0417  0.0500  -0.0169 61  GLU A N   
382  C CA  . GLU A 93  ? 0.3099 0.2475 0.2018 0.0237  0.0792  0.0191  61  GLU A CA  
383  C C   . GLU A 93  ? 0.2810 0.2402 0.1829 0.0259  0.0523  -0.0002 61  GLU A C   
384  O O   . GLU A 93  ? 0.3075 0.2483 0.1907 0.0127  0.0460  -0.0071 61  GLU A O   
385  C CB  . GLU A 93  ? 0.4139 0.2645 0.2626 0.0144  0.1137  0.0531  61  GLU A CB  
386  C CG  . GLU A 93  ? 0.5460 0.3017 0.3210 0.0056  0.1124  0.0568  61  GLU A CG  
387  C CD  . GLU A 93  ? 0.6713 0.3441 0.3737 -0.0113 0.1118  0.0535  61  GLU A CD  
388  O OE1 . GLU A 93  ? 0.7098 0.3653 0.3950 -0.0229 0.1098  0.0543  61  GLU A OE1 
389  O OE2 . GLU A 93  ? 0.7234 0.3600 0.4024 -0.0193 0.1036  0.0513  61  GLU A OE2 
390  N N   . GLU A 94  ? 0.2826 0.2388 0.1646 0.0321  0.0620  -0.0146 62  GLU A N   
391  C CA  . GLU A 94  ? 0.2707 0.2545 0.1799 0.0251  0.0462  -0.0086 62  GLU A CA  
392  C C   . GLU A 94  ? 0.2136 0.2247 0.1736 0.0087  0.0352  -0.0206 62  GLU A C   
393  O O   . GLU A 94  ? 0.1996 0.2301 0.1991 0.0281  0.0163  -0.0022 62  GLU A O   
394  C CB  . GLU A 94  ? 0.3515 0.3181 0.1967 0.0546  0.0457  -0.0049 62  GLU A CB  
395  C CG  . GLU A 94  ? 0.4461 0.3832 0.2180 0.0764  0.0553  0.0023  62  GLU A CG  
396  C CD  . GLU A 94  ? 0.5243 0.4413 0.2397 0.0845  0.0576  0.0241  62  GLU A CD  
397  O OE1 . GLU A 94  ? 0.5321 0.4573 0.2242 0.0867  0.0473  0.0241  62  GLU A OE1 
398  O OE2 . GLU A 94  ? 0.5749 0.4616 0.2843 0.0834  0.0650  0.0323  62  GLU A OE2 
399  N N   . GLU A 95  ? 0.2099 0.2051 0.1480 0.0046  0.0249  -0.0569 63  GLU A N   
400  C CA  . GLU A 95  ? 0.1956 0.2094 0.1644 0.0018  -0.0008 -0.0621 63  GLU A CA  
401  C C   . GLU A 95  ? 0.1725 0.1749 0.1414 0.0264  -0.0050 -0.0477 63  GLU A C   
402  O O   . GLU A 95  ? 0.2144 0.1833 0.1453 0.0034  -0.0118 -0.0387 63  GLU A O   
403  C CB  . GLU A 95  ? 0.1919 0.2507 0.2308 -0.0212 -0.0108 -0.0748 63  GLU A CB  
404  C CG  . GLU A 95  ? 0.2544 0.2747 0.3153 -0.0279 -0.0122 -0.0769 63  GLU A CG  
405  C CD  . GLU A 95  ? 0.2848 0.2818 0.3930 0.0061  -0.0030 -0.0912 63  GLU A CD  
406  O OE1 . GLU A 95  ? 0.2689 0.2674 0.3935 0.0235  -0.0094 -0.1033 63  GLU A OE1 
407  O OE2 . GLU A 95  ? 0.3012 0.2919 0.4413 -0.0075 0.0053  -0.0943 63  GLU A OE2 
408  N N   . PHE A 96  ? 0.1940 0.1612 0.1514 0.0245  0.0080  -0.0523 64  PHE A N   
409  C CA  . PHE A 96  ? 0.1891 0.1624 0.1602 0.0337  -0.0164 -0.0473 64  PHE A CA  
410  C C   . PHE A 96  ? 0.1734 0.1605 0.1698 0.0327  0.0084  -0.0397 64  PHE A C   
411  O O   . PHE A 96  ? 0.2224 0.1683 0.1956 -0.0035 -0.0144 -0.0347 64  PHE A O   
412  C CB  . PHE A 96  ? 0.1985 0.1591 0.1573 0.0316  -0.0368 -0.0320 64  PHE A CB  
413  C CG  . PHE A 96  ? 0.2189 0.1815 0.1671 0.0276  -0.0245 -0.0356 64  PHE A CG  
414  C CD1 . PHE A 96  ? 0.2625 0.1860 0.1707 0.0311  -0.0381 -0.0353 64  PHE A CD1 
415  C CD2 . PHE A 96  ? 0.2102 0.1788 0.1891 0.0203  -0.0368 -0.0494 64  PHE A CD2 
416  C CE1 . PHE A 96  ? 0.2846 0.1935 0.1780 0.0332  -0.0252 -0.0386 64  PHE A CE1 
417  C CE2 . PHE A 96  ? 0.2859 0.1951 0.2031 0.0240  -0.0389 -0.0483 64  PHE A CE2 
418  C CZ  . PHE A 96  ? 0.2879 0.1900 0.1710 0.0510  -0.0348 -0.0339 64  PHE A CZ  
419  N N   . VAL A 97  ? 0.1647 0.1636 0.1603 0.0341  0.0087  -0.0412 65  VAL A N   
420  C CA  . VAL A 97  ? 0.1558 0.1461 0.1511 0.0216  -0.0082 -0.0284 65  VAL A CA  
421  C C   . VAL A 97  ? 0.1739 0.1436 0.1505 0.0087  0.0378  -0.0280 65  VAL A C   
422  O O   . VAL A 97  ? 0.1818 0.1686 0.1580 0.0090  0.0194  -0.0354 65  VAL A O   
423  C CB  . VAL A 97  ? 0.1739 0.1615 0.1575 0.0178  0.0103  -0.0349 65  VAL A CB  
424  C CG1 . VAL A 97  ? 0.2149 0.1994 0.1516 0.0382  -0.0052 -0.0387 65  VAL A CG1 
425  C CG2 . VAL A 97  ? 0.1742 0.1752 0.1941 0.0198  0.0106  -0.0270 65  VAL A CG2 
426  N N   . GLU A 98  ? 0.1857 0.1696 0.1523 -0.0152 0.0210  -0.0413 66  GLU A N   
427  C CA  . GLU A 98  ? 0.2172 0.2081 0.1655 0.0041  0.0218  -0.0478 66  GLU A CA  
428  C C   . GLU A 98  ? 0.2173 0.1845 0.1467 0.0192  0.0116  -0.0259 66  GLU A C   
429  O O   . GLU A 98  ? 0.2988 0.1764 0.1636 -0.0018 0.0343  -0.0222 66  GLU A O   
430  C CB  . GLU A 98  ? 0.3074 0.2749 0.2234 -0.0243 -0.0058 -0.0749 66  GLU A CB  
431  C CG  . GLU A 98  ? 0.4280 0.3324 0.2975 -0.0249 -0.0293 -0.1044 66  GLU A CG  
432  C CD  . GLU A 98  ? 0.5139 0.3772 0.3537 -0.0227 -0.0365 -0.1388 66  GLU A CD  
433  O OE1 . GLU A 98  ? 0.5583 0.4004 0.3727 -0.0151 -0.0481 -0.1516 66  GLU A OE1 
434  O OE2 . GLU A 98  ? 0.5272 0.3806 0.3562 -0.0222 -0.0089 -0.1582 66  GLU A OE2 
435  N N   . GLY A 99  ? 0.1952 0.1883 0.1390 0.0207  0.0147  -0.0294 67  GLY A N   
436  C CA  . GLY A 99  ? 0.2309 0.1932 0.1377 0.0237  0.0437  -0.0353 67  GLY A CA  
437  C C   . GLY A 99  ? 0.1589 0.1825 0.1205 0.0226  0.0193  -0.0344 67  GLY A C   
438  O O   . GLY A 99  ? 0.1960 0.1775 0.1362 0.0080  0.0102  -0.0297 67  GLY A O   
439  N N   . ILE A 100 ? 0.1657 0.1992 0.1110 0.0207  -0.0084 -0.0300 68  ILE A N   
440  C CA  . ILE A 100 ? 0.1725 0.2050 0.1072 0.0240  -0.0028 -0.0253 68  ILE A CA  
441  C C   . ILE A 100 ? 0.1681 0.1674 0.1158 0.0251  -0.0241 -0.0270 68  ILE A C   
442  O O   . ILE A 100 ? 0.1980 0.1653 0.1560 0.0126  -0.0156 -0.0259 68  ILE A O   
443  C CB  . ILE A 100 ? 0.1875 0.2329 0.1062 0.0114  -0.0207 -0.0216 68  ILE A CB  
444  C CG1 . ILE A 100 ? 0.2060 0.2731 0.1371 -0.0102 -0.0482 -0.0058 68  ILE A CG1 
445  C CG2 . ILE A 100 ? 0.2183 0.2393 0.1101 0.0088  0.0105  -0.0352 68  ILE A CG2 
446  C CD1 . ILE A 100 ? 0.2562 0.2916 0.1561 0.0066  -0.0529 0.0047  68  ILE A CD1 
447  N N   . TYR A 101 ? 0.1379 0.1694 0.1139 0.0226  -0.0057 -0.0255 69  TYR A N   
448  C CA  . TYR A 101 ? 0.1598 0.1608 0.1207 0.0112  0.0100  -0.0307 69  TYR A CA  
449  C C   . TYR A 101 ? 0.1455 0.1581 0.1221 0.0130  0.0025  -0.0213 69  TYR A C   
450  O O   . TYR A 101 ? 0.1637 0.1696 0.1321 -0.0062 -0.0068 -0.0307 69  TYR A O   
451  C CB  . TYR A 101 ? 0.1437 0.1756 0.1086 0.0152  -0.0133 -0.0245 69  TYR A CB  
452  C CG  . TYR A 101 ? 0.1398 0.1716 0.1160 0.0206  0.0057  -0.0350 69  TYR A CG  
453  C CD1 . TYR A 101 ? 0.1632 0.1660 0.1288 0.0144  0.0251  -0.0168 69  TYR A CD1 
454  C CD2 . TYR A 101 ? 0.1816 0.1805 0.1143 0.0137  0.0012  -0.0367 69  TYR A CD2 
455  C CE1 . TYR A 101 ? 0.1769 0.1540 0.1376 0.0222  0.0102  -0.0222 69  TYR A CE1 
456  C CE2 . TYR A 101 ? 0.1800 0.1847 0.1252 0.0152  0.0236  -0.0248 69  TYR A CE2 
457  C CZ  . TYR A 101 ? 0.1803 0.1732 0.1290 0.0190  -0.0032 -0.0343 69  TYR A CZ  
458  O OH  . TYR A 101 ? 0.2054 0.1659 0.1430 0.0097  0.0230  -0.0492 69  TYR A OH  
459  N N   . LYS A 102 ? 0.1518 0.1688 0.1263 -0.0057 0.0272  -0.0121 70  LYS A N   
460  C CA  . LYS A 102 ? 0.1479 0.1911 0.1046 -0.0193 0.0142  -0.0244 70  LYS A CA  
461  C C   . LYS A 102 ? 0.1538 0.1820 0.1190 0.0001  -0.0044 -0.0574 70  LYS A C   
462  O O   . LYS A 102 ? 0.1626 0.1852 0.1559 0.0089  -0.0283 -0.0607 70  LYS A O   
463  C CB  . LYS A 102 ? 0.1731 0.2195 0.1095 -0.0259 0.0324  -0.0122 70  LYS A CB  
464  C CG  . LYS A 102 ? 0.1905 0.2404 0.1202 -0.0355 0.0575  -0.0074 70  LYS A CG  
465  C CD  . LYS A 102 ? 0.2446 0.2700 0.1635 -0.0391 0.0599  0.0104  70  LYS A CD  
466  C CE  . LYS A 102 ? 0.3050 0.2897 0.2034 -0.0434 0.0788  0.0282  70  LYS A CE  
467  N NZ  . LYS A 102 ? 0.3712 0.3035 0.2416 -0.0229 0.0821  0.0460  70  LYS A NZ  
468  N N   . VAL A 103 ? 0.1443 0.1757 0.1288 0.0084  -0.0163 -0.0466 71  VAL A N   
469  C CA  . VAL A 103 ? 0.1510 0.1837 0.1332 0.0186  -0.0131 -0.0345 71  VAL A CA  
470  C C   . VAL A 103 ? 0.1505 0.1970 0.1234 0.0085  -0.0114 -0.0538 71  VAL A C   
471  O O   . VAL A 103 ? 0.1666 0.2247 0.1459 0.0070  -0.0069 -0.0803 71  VAL A O   
472  C CB  . VAL A 103 ? 0.1668 0.1955 0.1509 0.0188  -0.0147 -0.0172 71  VAL A CB  
473  C CG1 . VAL A 103 ? 0.1872 0.2206 0.1615 0.0199  -0.0170 -0.0363 71  VAL A CG1 
474  C CG2 . VAL A 103 ? 0.1601 0.2094 0.1785 -0.0030 -0.0003 -0.0059 71  VAL A CG2 
475  N N   . GLU A 104 ? 0.1678 0.1937 0.1146 0.0045  -0.0169 -0.0272 72  GLU A N   
476  C CA  . GLU A 104 ? 0.1715 0.1728 0.1352 -0.0056 -0.0056 -0.0066 72  GLU A CA  
477  C C   . GLU A 104 ? 0.1620 0.1754 0.1223 0.0102  0.0043  -0.0330 72  GLU A C   
478  O O   . GLU A 104 ? 0.1950 0.1952 0.1374 0.0250  -0.0367 -0.0563 72  GLU A O   
479  C CB  . GLU A 104 ? 0.2526 0.1975 0.2129 -0.0100 -0.0047 0.0336  72  GLU A CB  
480  C CG  . GLU A 104 ? 0.4186 0.2495 0.2913 -0.0034 0.0320  0.0367  72  GLU A CG  
481  C CD  . GLU A 104 ? 0.5755 0.2777 0.3591 -0.0293 0.0747  0.0493  72  GLU A CD  
482  O OE1 . GLU A 104 ? 0.6136 0.2699 0.3490 0.0186  0.1022  0.0913  72  GLU A OE1 
483  O OE2 . GLU A 104 ? 0.6457 0.3027 0.4155 -0.0621 0.0638  0.0290  72  GLU A OE2 
484  N N   . ILE A 105 ? 0.1574 0.1644 0.1302 0.0130  0.0012  -0.0226 73  ILE A N   
485  C CA  . ILE A 105 ? 0.1539 0.1551 0.1352 0.0172  0.0039  -0.0167 73  ILE A CA  
486  C C   . ILE A 105 ? 0.1653 0.1553 0.1181 0.0118  0.0052  -0.0158 73  ILE A C   
487  O O   . ILE A 105 ? 0.2169 0.1781 0.0990 0.0028  0.0000  -0.0121 73  ILE A O   
488  C CB  . ILE A 105 ? 0.2004 0.1617 0.1440 0.0083  0.0260  -0.0177 73  ILE A CB  
489  C CG1 . ILE A 105 ? 0.2197 0.1789 0.1500 -0.0248 0.0436  -0.0143 73  ILE A CG1 
490  C CG2 . ILE A 105 ? 0.2462 0.1836 0.1453 0.0536  0.0248  -0.0142 73  ILE A CG2 
491  C CD1 . ILE A 105 ? 0.2661 0.1770 0.1411 -0.0521 0.0547  -0.0163 73  ILE A CD1 
492  N N   . ASP A 106 ? 0.1665 0.1576 0.1415 0.0078  0.0066  -0.0106 74  ASP A N   
493  C CA  . ASP A 106 ? 0.1969 0.1656 0.1702 0.0011  0.0137  -0.0205 74  ASP A CA  
494  C C   . ASP A 106 ? 0.1608 0.1732 0.1548 -0.0082 0.0110  -0.0196 74  ASP A C   
495  O O   . ASP A 106 ? 0.1985 0.1920 0.1661 -0.0170 -0.0137 -0.0278 74  ASP A O   
496  C CB  . ASP A 106 ? 0.2225 0.1795 0.2330 -0.0062 0.0168  -0.0398 74  ASP A CB  
497  C CG  . ASP A 106 ? 0.2556 0.2229 0.3187 -0.0225 0.0398  -0.0506 74  ASP A CG  
498  O OD1 . ASP A 106 ? 0.2490 0.2326 0.3418 -0.0239 0.0618  -0.0096 74  ASP A OD1 
499  O OD2 . ASP A 106 ? 0.2902 0.2730 0.3585 -0.0521 0.0264  -0.0630 74  ASP A OD2 
500  N N   . THR A 107 ? 0.1939 0.1604 0.1192 -0.0145 0.0420  -0.0194 75  THR A N   
501  C CA  . THR A 107 ? 0.1967 0.1510 0.1367 -0.0039 0.0293  -0.0135 75  THR A CA  
502  C C   . THR A 107 ? 0.1966 0.1604 0.1360 -0.0083 0.0096  -0.0110 75  THR A C   
503  O O   . THR A 107 ? 0.1689 0.1747 0.1414 -0.0001 -0.0078 -0.0165 75  THR A O   
504  C CB  . THR A 107 ? 0.1701 0.1505 0.1655 -0.0118 0.0141  -0.0017 75  THR A CB  
505  O OG1 . THR A 107 ? 0.1636 0.1519 0.1684 -0.0147 0.0058  -0.0173 75  THR A OG1 
506  C CG2 . THR A 107 ? 0.1901 0.1650 0.1913 0.0007  0.0261  0.0022  75  THR A CG2 
507  N N   . LYS A 108 ? 0.1779 0.1700 0.1420 -0.0126 0.0096  0.0037  76  LYS A N   
508  C CA  . LYS A 108 ? 0.1671 0.1948 0.1527 -0.0139 0.0030  0.0251  76  LYS A CA  
509  C C   . LYS A 108 ? 0.1718 0.2101 0.1542 -0.0459 0.0100  0.0113  76  LYS A C   
510  O O   . LYS A 108 ? 0.1600 0.2306 0.1764 -0.0173 0.0049  0.0193  76  LYS A O   
511  C CB  . LYS A 108 ? 0.1680 0.2085 0.1775 -0.0259 0.0191  0.0397  76  LYS A CB  
512  C CG  . LYS A 108 ? 0.2154 0.2452 0.1942 -0.0197 0.0184  0.0716  76  LYS A CG  
513  C CD  . LYS A 108 ? 0.2642 0.2810 0.2270 -0.0491 0.0092  0.0901  76  LYS A CD  
514  C CE  . LYS A 108 ? 0.3237 0.3147 0.2416 -0.0601 0.0162  0.0985  76  LYS A CE  
515  N NZ  . LYS A 108 ? 0.3444 0.3390 0.2535 -0.0586 0.0063  0.0973  76  LYS A NZ  
516  N N   . SER A 109 ? 0.2404 0.2196 0.1712 -0.0770 0.0146  -0.0143 77  SER A N   
517  C CA  . SER A 109 ? 0.2491 0.2310 0.2146 -0.0754 -0.0024 -0.0394 77  SER A CA  
518  C C   . SER A 109 ? 0.1877 0.2484 0.1993 -0.0614 -0.0035 -0.0121 77  SER A C   
519  O O   . SER A 109 ? 0.1979 0.2676 0.2117 -0.0741 -0.0236 -0.0024 77  SER A O   
520  C CB  . SER A 109 ? 0.3094 0.2270 0.2708 -0.0505 0.0207  -0.0570 77  SER A CB  
521  O OG  . SER A 109 ? 0.3312 0.2278 0.3201 -0.0715 0.0265  -0.0541 77  SER A OG  
522  N N   . TYR A 110 ? 0.2010 0.2245 0.1689 -0.0707 -0.0337 -0.0042 78  TYR A N   
523  C CA  . TYR A 110 ? 0.2124 0.2339 0.1665 -0.0574 -0.0209 0.0041  78  TYR A CA  
524  C C   . TYR A 110 ? 0.1913 0.2543 0.1581 -0.0437 -0.0211 0.0242  78  TYR A C   
525  O O   . TYR A 110 ? 0.1799 0.2729 0.1637 -0.0436 -0.0257 0.0251  78  TYR A O   
526  C CB  . TYR A 110 ? 0.1937 0.2274 0.1622 -0.0581 -0.0022 -0.0055 78  TYR A CB  
527  C CG  . TYR A 110 ? 0.1767 0.2285 0.1479 -0.0563 0.0109  -0.0121 78  TYR A CG  
528  C CD1 . TYR A 110 ? 0.1923 0.2395 0.1524 -0.0250 -0.0109 -0.0197 78  TYR A CD1 
529  C CD2 . TYR A 110 ? 0.1847 0.2352 0.1540 -0.0310 0.0293  -0.0281 78  TYR A CD2 
530  C CE1 . TYR A 110 ? 0.2023 0.2345 0.1570 -0.0371 -0.0059 -0.0234 78  TYR A CE1 
531  C CE2 . TYR A 110 ? 0.1775 0.2379 0.1643 -0.0366 0.0367  -0.0152 78  TYR A CE2 
532  C CZ  . TYR A 110 ? 0.1862 0.2283 0.1661 -0.0287 -0.0025 -0.0197 78  TYR A CZ  
533  O OH  . TYR A 110 ? 0.2271 0.2161 0.1901 -0.0172 -0.0003 -0.0213 78  TYR A OH  
534  N N   . TRP A 111 ? 0.1731 0.2460 0.1536 -0.0277 -0.0201 0.0219  79  TRP A N   
535  C CA  . TRP A 111 ? 0.1506 0.2624 0.1593 -0.0063 -0.0129 0.0298  79  TRP A CA  
536  C C   . TRP A 111 ? 0.1450 0.3010 0.1774 -0.0082 -0.0041 0.0485  79  TRP A C   
537  O O   . TRP A 111 ? 0.1457 0.3176 0.1962 0.0018  -0.0224 0.0248  79  TRP A O   
538  C CB  . TRP A 111 ? 0.1430 0.2299 0.1362 -0.0197 -0.0349 0.0093  79  TRP A CB  
539  C CG  . TRP A 111 ? 0.1203 0.2015 0.1193 -0.0052 -0.0084 -0.0058 79  TRP A CG  
540  C CD1 . TRP A 111 ? 0.1309 0.1928 0.1012 -0.0028 -0.0044 0.0012  79  TRP A CD1 
541  C CD2 . TRP A 111 ? 0.1586 0.1838 0.1108 0.0264  -0.0210 -0.0091 79  TRP A CD2 
542  N NE1 . TRP A 111 ? 0.1444 0.1778 0.0990 0.0089  0.0001  -0.0196 79  TRP A NE1 
543  C CE2 . TRP A 111 ? 0.1365 0.1724 0.1183 0.0231  -0.0174 -0.0124 79  TRP A CE2 
544  C CE3 . TRP A 111 ? 0.1890 0.1959 0.1347 0.0189  -0.0156 -0.0169 79  TRP A CE3 
545  C CZ2 . TRP A 111 ? 0.1791 0.1663 0.1307 0.0282  -0.0180 -0.0305 79  TRP A CZ2 
546  C CZ3 . TRP A 111 ? 0.2001 0.1936 0.1487 0.0358  -0.0213 -0.0187 79  TRP A CZ3 
547  C CH2 . TRP A 111 ? 0.1910 0.1937 0.1344 0.0361  -0.0233 -0.0281 79  TRP A CH2 
548  N N   . LYS A 112 ? 0.1494 0.3250 0.1986 -0.0596 -0.0059 0.0516  80  LYS A N   
549  C CA  . LYS A 112 ? 0.1800 0.3706 0.2298 -0.0813 -0.0161 0.0722  80  LYS A CA  
550  C C   . LYS A 112 ? 0.1698 0.4039 0.2383 -0.0785 -0.0273 0.0645  80  LYS A C   
551  O O   . LYS A 112 ? 0.1602 0.4191 0.2582 -0.0563 -0.0227 0.0732  80  LYS A O   
552  C CB  . LYS A 112 ? 0.2110 0.3881 0.2781 -0.1068 -0.0475 0.0719  80  LYS A CB  
553  C CG  . LYS A 112 ? 0.2994 0.4118 0.3213 -0.0804 -0.0592 0.0823  80  LYS A CG  
554  C CD  . LYS A 112 ? 0.4691 0.4289 0.3723 -0.0532 -0.0606 0.0787  80  LYS A CD  
555  C CE  . LYS A 112 ? 0.5779 0.4378 0.4177 -0.0425 -0.0391 0.0770  80  LYS A CE  
556  N NZ  . LYS A 112 ? 0.6370 0.4449 0.4444 -0.0382 -0.0315 0.0746  80  LYS A NZ  
557  N N   . ALA A 113 ? 0.1952 0.4162 0.2241 -0.0818 -0.0465 0.0547  81  ALA A N   
558  C CA  . ALA A 113 ? 0.2087 0.4382 0.2564 -0.0502 -0.0716 0.0521  81  ALA A CA  
559  C C   . ALA A 113 ? 0.1906 0.4735 0.2868 -0.0171 -0.0640 0.0510  81  ALA A C   
560  O O   . ALA A 113 ? 0.2116 0.4926 0.2914 0.0024  -0.0773 0.0512  81  ALA A O   
561  C CB  . ALA A 113 ? 0.2392 0.4277 0.2624 -0.0663 -0.0891 0.0459  81  ALA A CB  
562  N N   . LEU A 114 ? 0.1648 0.4823 0.3153 -0.0077 -0.0536 0.0453  82  LEU A N   
563  C CA  . LEU A 114 ? 0.1884 0.5063 0.3569 -0.0045 -0.0707 0.0377  82  LEU A CA  
564  C C   . LEU A 114 ? 0.1860 0.5254 0.3783 -0.0027 -0.0408 0.0228  82  LEU A C   
565  O O   . LEU A 114 ? 0.2011 0.5285 0.4016 -0.0090 -0.0142 0.0257  82  LEU A O   
566  C CB  . LEU A 114 ? 0.2624 0.5068 0.3748 -0.0190 -0.0858 0.0392  82  LEU A CB  
567  C CG  . LEU A 114 ? 0.3364 0.5168 0.3895 -0.0204 -0.0975 0.0346  82  LEU A CG  
568  C CD1 . LEU A 114 ? 0.3678 0.5238 0.4012 -0.0115 -0.0997 0.0356  82  LEU A CD1 
569  C CD2 . LEU A 114 ? 0.3430 0.5129 0.3874 -0.0050 -0.1065 0.0432  82  LEU A CD2 
570  N N   . GLY A 115 ? 0.1716 0.5453 0.3710 0.0072  -0.0554 0.0094  83  GLY A N   
571  C CA  . GLY A 115 ? 0.1845 0.5552 0.3682 0.0101  -0.0514 -0.0078 83  GLY A CA  
572  C C   . GLY A 115 ? 0.1504 0.5610 0.3534 0.0140  -0.0375 -0.0219 83  GLY A C   
573  O O   . GLY A 115 ? 0.1575 0.5887 0.3599 0.0049  -0.0084 -0.0348 83  GLY A O   
574  N N   . ILE A 116 ? 0.1449 0.5347 0.3301 0.0065  -0.0463 -0.0135 84  ILE A N   
575  C CA  . ILE A 116 ? 0.1655 0.5033 0.3153 0.0193  -0.0192 0.0007  84  ILE A CA  
576  C C   . ILE A 116 ? 0.2039 0.4807 0.2770 0.0114  0.0174  0.0100  84  ILE A C   
577  O O   . ILE A 116 ? 0.2277 0.4796 0.2750 0.0065  -0.0010 0.0131  84  ILE A O   
578  C CB  . ILE A 116 ? 0.1965 0.4919 0.3351 0.0079  -0.0261 0.0068  84  ILE A CB  
579  C CG1 . ILE A 116 ? 0.2355 0.4911 0.3494 0.0056  -0.0081 0.0129  84  ILE A CG1 
580  C CG2 . ILE A 116 ? 0.2069 0.4871 0.3430 -0.0155 -0.0411 0.0119  84  ILE A CG2 
581  C CD1 . ILE A 116 ? 0.2729 0.4909 0.3559 -0.0080 0.0019  0.0168  84  ILE A CD1 
582  N N   . SER A 117 ? 0.2015 0.4559 0.2501 0.0130  0.0610  0.0028  85  SER A N   
583  C CA  . SER A 117 ? 0.2021 0.4251 0.2352 -0.0303 0.0653  -0.0049 85  SER A CA  
584  C C   . SER A 117 ? 0.1870 0.3603 0.1837 -0.0109 0.0353  -0.0189 85  SER A C   
585  O O   . SER A 117 ? 0.2210 0.3760 0.1947 0.0086  0.0488  -0.0320 85  SER A O   
586  C CB  . SER A 117 ? 0.2198 0.4627 0.2814 -0.0784 0.0825  -0.0013 85  SER A CB  
587  O OG  . SER A 117 ? 0.3157 0.4929 0.3299 -0.0630 0.0689  -0.0061 85  SER A OG  
588  N N   . PRO A 118 ? 0.1718 0.2816 0.1429 0.0021  0.0141  -0.0065 86  PRO A N   
589  C CA  . PRO A 118 ? 0.1600 0.2422 0.1280 0.0137  0.0172  0.0054  86  PRO A CA  
590  C C   . PRO A 118 ? 0.1575 0.2168 0.1416 0.0222  0.0169  0.0276  86  PRO A C   
591  O O   . PRO A 118 ? 0.1883 0.2371 0.1709 -0.0067 0.0082  0.0447  86  PRO A O   
592  C CB  . PRO A 118 ? 0.2023 0.2430 0.1181 0.0178  0.0284  -0.0081 86  PRO A CB  
593  C CG  . PRO A 118 ? 0.2106 0.2518 0.1442 0.0174  0.0215  -0.0074 86  PRO A CG  
594  C CD  . PRO A 118 ? 0.2160 0.2799 0.1416 -0.0205 0.0088  -0.0108 86  PRO A CD  
595  N N   . PHE A 119 ? 0.1570 0.1816 0.1416 0.0305  0.0093  0.0185  87  PHE A N   
596  C CA  . PHE A 119 ? 0.1810 0.1585 0.1410 0.0324  0.0065  0.0041  87  PHE A CA  
597  C C   . PHE A 119 ? 0.1702 0.1505 0.1140 0.0301  0.0055  0.0055  87  PHE A C   
598  O O   . PHE A 119 ? 0.1905 0.1583 0.1226 0.0206  0.0105  0.0172  87  PHE A O   
599  C CB  . PHE A 119 ? 0.2460 0.1427 0.1530 0.0271  -0.0046 -0.0074 87  PHE A CB  
600  C CG  . PHE A 119 ? 0.3341 0.1413 0.1526 0.0098  -0.0530 0.0011  87  PHE A CG  
601  C CD1 . PHE A 119 ? 0.3832 0.1516 0.1728 -0.0036 -0.0647 0.0158  87  PHE A CD1 
602  C CD2 . PHE A 119 ? 0.3370 0.1377 0.1809 0.0123  -0.0641 -0.0017 87  PHE A CD2 
603  C CE1 . PHE A 119 ? 0.3907 0.1605 0.1922 -0.0039 -0.0829 0.0197  87  PHE A CE1 
604  C CE2 . PHE A 119 ? 0.3811 0.1597 0.1907 -0.0071 -0.0783 -0.0040 87  PHE A CE2 
605  C CZ  . PHE A 119 ? 0.3902 0.1614 0.1995 -0.0014 -0.0955 0.0183  87  PHE A CZ  
606  N N   . HIS A 120 ? 0.1655 0.1583 0.1150 0.0253  0.0005  0.0026  88  HIS A N   
607  C CA  . HIS A 120 ? 0.1713 0.1468 0.1177 0.0027  -0.0062 0.0065  88  HIS A CA  
608  C C   . HIS A 120 ? 0.1670 0.1570 0.1142 -0.0054 -0.0058 0.0046  88  HIS A C   
609  O O   . HIS A 120 ? 0.1576 0.1816 0.1285 0.0035  -0.0123 0.0130  88  HIS A O   
610  C CB  . HIS A 120 ? 0.1554 0.1614 0.1450 -0.0060 -0.0091 0.0020  88  HIS A CB  
611  C CG  . HIS A 120 ? 0.1695 0.1467 0.1951 -0.0023 -0.0149 0.0044  88  HIS A CG  
612  N ND1 . HIS A 120 ? 0.1658 0.1355 0.2102 -0.0012 -0.0213 0.0324  88  HIS A ND1 
613  C CD2 . HIS A 120 ? 0.1890 0.1594 0.2382 -0.0088 -0.0284 0.0010  88  HIS A CD2 
614  C CE1 . HIS A 120 ? 0.2155 0.1453 0.2511 0.0180  -0.0609 0.0044  88  HIS A CE1 
615  N NE2 . HIS A 120 ? 0.2221 0.1640 0.2651 0.0083  -0.0536 -0.0129 88  HIS A NE2 
616  N N   . GLU A 121 ? 0.1539 0.1623 0.1205 0.0107  -0.0035 0.0149  89  GLU A N   
617  C CA  . GLU A 121 ? 0.1643 0.1713 0.1499 0.0010  -0.0115 0.0017  89  GLU A CA  
618  C C   . GLU A 121 ? 0.1725 0.2055 0.1550 0.0202  -0.0285 -0.0225 89  GLU A C   
619  O O   . GLU A 121 ? 0.2183 0.2341 0.1685 0.0298  -0.0323 -0.0214 89  GLU A O   
620  C CB  . GLU A 121 ? 0.2321 0.1783 0.1817 0.0319  -0.0140 0.0224  89  GLU A CB  
621  C CG  . GLU A 121 ? 0.2376 0.2081 0.1985 0.0075  -0.0156 0.0270  89  GLU A CG  
622  C CD  . GLU A 121 ? 0.2742 0.2503 0.2237 -0.0079 -0.0084 0.0375  89  GLU A CD  
623  O OE1 . GLU A 121 ? 0.3078 0.2888 0.2450 -0.0227 -0.0061 0.0078  89  GLU A OE1 
624  O OE2 . GLU A 121 ? 0.3003 0.2736 0.2258 -0.0081 0.0075  0.0600  89  GLU A OE2 
625  N N   . HIS A 122 ? 0.1645 0.2107 0.1408 0.0326  0.0111  -0.0528 90  HIS A N   
626  C CA  . HIS A 122 ? 0.1736 0.2578 0.1273 0.0237  0.0333  -0.0680 90  HIS A CA  
627  C C   . HIS A 122 ? 0.1695 0.3099 0.1224 -0.0260 -0.0009 -0.0572 90  HIS A C   
628  O O   . HIS A 122 ? 0.2071 0.3486 0.1264 -0.0498 -0.0200 -0.0557 90  HIS A O   
629  C CB  . HIS A 122 ? 0.2757 0.2900 0.1583 0.0344  0.0294  -0.0436 90  HIS A CB  
630  C CG  . HIS A 122 ? 0.4079 0.3328 0.2178 0.0527  0.0611  -0.0359 90  HIS A CG  
631  N ND1 . HIS A 122 ? 0.5133 0.3539 0.2604 0.0548  0.0309  -0.0204 90  HIS A ND1 
632  C CD2 . HIS A 122 ? 0.4667 0.3544 0.2381 0.0708  0.0692  -0.0133 90  HIS A CD2 
633  C CE1 . HIS A 122 ? 0.5459 0.3643 0.2653 0.0578  0.0184  -0.0093 90  HIS A CE1 
634  N NE2 . HIS A 122 ? 0.5256 0.3676 0.2614 0.0620  0.0453  -0.0037 90  HIS A NE2 
635  N N   . ALA A 123 ? 0.1885 0.3191 0.1334 -0.0326 0.0233  -0.0554 91  ALA A N   
636  C CA  . ALA A 123 ? 0.2263 0.3182 0.1563 -0.0271 0.0322  -0.0783 91  ALA A CA  
637  C C   . ALA A 123 ? 0.1789 0.3359 0.1752 -0.0199 0.0200  -0.0990 91  ALA A C   
638  O O   . ALA A 123 ? 0.1939 0.3333 0.1806 -0.0076 0.0064  -0.1220 91  ALA A O   
639  C CB  . ALA A 123 ? 0.2611 0.3064 0.1702 -0.0207 0.0474  -0.0787 91  ALA A CB  
640  N N   . GLU A 124 ? 0.1884 0.3667 0.2106 0.0018  0.0342  -0.0788 92  GLU A N   
641  C CA  . GLU A 124 ? 0.2147 0.3619 0.2541 -0.0060 0.0106  -0.0779 92  GLU A CA  
642  C C   . GLU A 124 ? 0.2320 0.3379 0.2558 -0.0088 0.0198  -0.1049 92  GLU A C   
643  O O   . GLU A 124 ? 0.2799 0.3687 0.3076 -0.0382 0.0241  -0.1362 92  GLU A O   
644  C CB  . GLU A 124 ? 0.2544 0.3860 0.2828 -0.0420 0.0124  -0.0645 92  GLU A CB  
645  N N   . VAL A 125 ? 0.1510 0.2924 0.2073 0.0208  -0.0117 -0.0632 93  VAL A N   
646  C CA  . VAL A 125 ? 0.1451 0.2344 0.1905 0.0203  -0.0225 -0.0310 93  VAL A CA  
647  C C   . VAL A 125 ? 0.1321 0.1878 0.1528 0.0017  -0.0013 -0.0341 93  VAL A C   
648  O O   . VAL A 125 ? 0.1653 0.1870 0.1605 0.0121  -0.0274 -0.0479 93  VAL A O   
649  C CB  . VAL A 125 ? 0.1978 0.2287 0.2348 0.0352  -0.0332 -0.0287 93  VAL A CB  
650  C CG1 . VAL A 125 ? 0.2126 0.2405 0.2391 -0.0168 -0.0670 -0.0394 93  VAL A CG1 
651  C CG2 . VAL A 125 ? 0.2261 0.2342 0.2680 0.0286  -0.0355 -0.0244 93  VAL A CG2 
652  N N   . VAL A 126 ? 0.1453 0.1615 0.1169 0.0076  0.0106  -0.0250 94  VAL A N   
653  C CA  . VAL A 126 ? 0.1463 0.1722 0.1063 -0.0019 0.0126  -0.0117 94  VAL A CA  
654  C C   . VAL A 126 ? 0.1419 0.1465 0.1022 -0.0026 0.0151  -0.0085 94  VAL A C   
655  O O   . VAL A 126 ? 0.1687 0.1485 0.1042 -0.0122 -0.0071 -0.0267 94  VAL A O   
656  C CB  . VAL A 126 ? 0.1563 0.1791 0.1248 -0.0016 0.0190  0.0046  94  VAL A CB  
657  C CG1 . VAL A 126 ? 0.1999 0.1527 0.1505 0.0123  0.0246  -0.0053 94  VAL A CG1 
658  C CG2 . VAL A 126 ? 0.1860 0.2268 0.1346 -0.0209 -0.0019 0.0047  94  VAL A CG2 
659  N N   . PHE A 127 ? 0.1388 0.1636 0.1149 0.0007  0.0054  0.0034  95  PHE A N   
660  C CA  . PHE A 127 ? 0.1535 0.1552 0.1170 0.0093  0.0134  -0.0008 95  PHE A CA  
661  C C   . PHE A 127 ? 0.1365 0.1672 0.1218 -0.0089 0.0179  -0.0214 95  PHE A C   
662  O O   . PHE A 127 ? 0.1722 0.1522 0.1479 -0.0118 0.0018  -0.0238 95  PHE A O   
663  C CB  . PHE A 127 ? 0.1815 0.1510 0.1086 -0.0025 -0.0195 -0.0055 95  PHE A CB  
664  C CG  . PHE A 127 ? 0.1670 0.1541 0.1177 0.0143  -0.0091 0.0028  95  PHE A CG  
665  C CD1 . PHE A 127 ? 0.1963 0.1773 0.1418 0.0142  -0.0454 -0.0032 95  PHE A CD1 
666  C CD2 . PHE A 127 ? 0.2347 0.1516 0.1030 0.0461  -0.0063 -0.0269 95  PHE A CD2 
667  C CE1 . PHE A 127 ? 0.2484 0.1678 0.1504 0.0091  -0.0265 -0.0025 95  PHE A CE1 
668  C CE2 . PHE A 127 ? 0.2852 0.1665 0.1303 0.0329  -0.0215 -0.0133 95  PHE A CE2 
669  C CZ  . PHE A 127 ? 0.2985 0.1686 0.1478 0.0204  -0.0455 -0.0101 95  PHE A CZ  
670  N N   . THR A 128 ? 0.1303 0.1831 0.1248 -0.0019 0.0228  -0.0231 96  THR A N   
671  C CA  . THR A 128 ? 0.1512 0.2059 0.1285 0.0013  0.0302  -0.0220 96  THR A CA  
672  C C   . THR A 128 ? 0.1822 0.1846 0.1391 -0.0109 0.0166  -0.0308 96  THR A C   
673  O O   . THR A 128 ? 0.2301 0.1839 0.1432 -0.0184 0.0436  -0.0432 96  THR A O   
674  C CB  . THR A 128 ? 0.1677 0.2356 0.1536 0.0316  0.0294  -0.0281 96  THR A CB  
675  O OG1 . THR A 128 ? 0.1969 0.2597 0.1783 0.0350  0.0127  -0.0159 96  THR A OG1 
676  C CG2 . THR A 128 ? 0.1744 0.2597 0.1820 0.0381  0.0442  -0.0391 96  THR A CG2 
677  N N   . ALA A 129 ? 0.1740 0.1827 0.1337 -0.0094 0.0432  -0.0220 97  ALA A N   
678  C CA  . ALA A 129 ? 0.1879 0.1753 0.1493 -0.0276 0.0265  -0.0325 97  ALA A CA  
679  C C   . ALA A 129 ? 0.1721 0.1703 0.1560 -0.0045 0.0477  -0.0369 97  ALA A C   
680  O O   . ALA A 129 ? 0.2097 0.1739 0.1598 0.0148  0.0427  -0.0411 97  ALA A O   
681  C CB  . ALA A 129 ? 0.2123 0.2023 0.1645 -0.0089 0.0054  -0.0267 97  ALA A CB  
682  N N   . ASN A 130 ? 0.1785 0.1896 0.1604 -0.0083 0.0445  -0.0071 98  ASN A N   
683  C CA  . ASN A 130 ? 0.1733 0.2214 0.1982 -0.0050 0.0309  0.0013  98  ASN A CA  
684  C C   . ASN A 130 ? 0.1869 0.2619 0.2602 0.0049  0.0479  0.0296  98  ASN A C   
685  O O   . ASN A 130 ? 0.2395 0.2620 0.2694 0.0263  0.0664  0.0124  98  ASN A O   
686  C CB  . ASN A 130 ? 0.1883 0.2250 0.1984 -0.0124 0.0130  -0.0131 98  ASN A CB  
687  C CG  . ASN A 130 ? 0.1991 0.2126 0.1833 -0.0032 0.0265  -0.0318 98  ASN A CG  
688  O OD1 . ASN A 130 ? 0.2131 0.2134 0.1895 0.0034  0.0286  -0.0134 98  ASN A OD1 
689  N ND2 . ASN A 130 ? 0.2167 0.2304 0.1699 -0.0026 0.0087  -0.0527 98  ASN A ND2 
690  N N   . ASP A 131 ? 0.1774 0.3037 0.3186 0.0068  0.0198  0.0500  99  ASP A N   
691  C CA  . ASP A 131 ? 0.2343 0.3605 0.4009 -0.0011 0.0073  0.0562  99  ASP A CA  
692  C C   . ASP A 131 ? 0.2057 0.3595 0.4287 -0.0141 0.0091  0.0600  99  ASP A C   
693  O O   . ASP A 131 ? 0.2153 0.3616 0.4203 0.0092  0.0084  0.0540  99  ASP A O   
694  C CB  . ASP A 131 ? 0.3630 0.4224 0.4510 0.0003  -0.0142 0.0463  99  ASP A CB  
695  C CG  . ASP A 131 ? 0.5217 0.4806 0.5059 -0.0068 -0.0192 0.0303  99  ASP A CG  
696  O OD1 . ASP A 131 ? 0.5672 0.4923 0.5295 0.0095  -0.0143 0.0293  99  ASP A OD1 
697  O OD2 . ASP A 131 ? 0.5891 0.4976 0.5279 -0.0188 -0.0278 0.0209  99  ASP A OD2 
698  N N   . SER A 132 ? 0.2388 0.3553 0.4539 -0.0491 0.0330  0.0633  100 SER A N   
699  C CA  . SER A 132 ? 0.3112 0.3594 0.4922 -0.0683 0.0306  0.0584  100 SER A CA  
700  C C   . SER A 132 ? 0.3143 0.3290 0.4918 -0.0572 0.0495  0.0625  100 SER A C   
701  O O   . SER A 132 ? 0.3736 0.3481 0.5227 -0.0807 0.0276  0.0698  100 SER A O   
702  C CB  . SER A 132 ? 0.3765 0.3934 0.5237 -0.0814 0.0183  0.0543  100 SER A CB  
703  O OG  . SER A 132 ? 0.4374 0.4227 0.5508 -0.0819 0.0183  0.0444  100 SER A OG  
704  N N   . GLY A 133 ? 0.2394 0.2800 0.4317 -0.0069 0.0745  0.0440  101 GLY A N   
705  C CA  . GLY A 133 ? 0.2046 0.2408 0.3818 0.0232  0.0904  0.0128  101 GLY A CA  
706  C C   . GLY A 133 ? 0.2186 0.2120 0.3268 0.0078  0.0973  -0.0032 101 GLY A C   
707  O O   . GLY A 133 ? 0.2118 0.2156 0.3114 -0.0115 0.0587  0.0105  101 GLY A O   
708  N N   . PRO A 134 ? 0.2636 0.2050 0.2871 0.0120  0.1249  -0.0237 102 PRO A N   
709  C CA  . PRO A 134 ? 0.2566 0.2006 0.2674 0.0340  0.1019  -0.0420 102 PRO A CA  
710  C C   . PRO A 134 ? 0.2571 0.1989 0.2394 0.0250  0.1090  -0.0419 102 PRO A C   
711  O O   . PRO A 134 ? 0.2756 0.1981 0.2547 0.0122  0.0971  -0.0198 102 PRO A O   
712  C CB  . PRO A 134 ? 0.2732 0.2314 0.2842 0.0129  0.1236  -0.0440 102 PRO A CB  
713  C CG  . PRO A 134 ? 0.3192 0.2573 0.3031 0.0190  0.1159  -0.0492 102 PRO A CG  
714  C CD  . PRO A 134 ? 0.3006 0.2339 0.2918 0.0075  0.1333  -0.0459 102 PRO A CD  
715  N N   . ARG A 135 ? 0.2304 0.2050 0.2175 0.0119  0.0897  -0.0252 103 ARG A N   
716  C CA  . ARG A 135 ? 0.2018 0.2102 0.2093 0.0133  0.0779  -0.0244 103 ARG A CA  
717  C C   . ARG A 135 ? 0.1979 0.2162 0.1856 0.0095  0.0705  -0.0356 103 ARG A C   
718  O O   . ARG A 135 ? 0.2204 0.2216 0.2033 0.0117  0.0403  -0.0360 103 ARG A O   
719  C CB  . ARG A 135 ? 0.2143 0.2068 0.2469 -0.0064 0.0747  -0.0232 103 ARG A CB  
720  C CG  . ARG A 135 ? 0.1985 0.2095 0.3051 -0.0149 0.0560  -0.0249 103 ARG A CG  
721  C CD  . ARG A 135 ? 0.1958 0.2447 0.3536 -0.0194 0.0380  -0.0137 103 ARG A CD  
722  N NE  . ARG A 135 ? 0.1924 0.2662 0.4002 -0.0262 0.0208  -0.0171 103 ARG A NE  
723  C CZ  . ARG A 135 ? 0.2008 0.2844 0.4439 -0.0408 0.0169  -0.0221 103 ARG A CZ  
724  N NH1 . ARG A 135 ? 0.2326 0.2702 0.4530 -0.0430 0.0292  -0.0197 103 ARG A NH1 
725  N NH2 . ARG A 135 ? 0.2346 0.3084 0.4686 -0.0494 -0.0039 -0.0267 103 ARG A NH2 
726  N N   . ARG A 136 ? 0.1941 0.2269 0.1761 0.0240  0.0637  -0.0226 104 ARG A N   
727  C CA  . ARG A 136 ? 0.2066 0.2433 0.1860 0.0351  0.0626  -0.0220 104 ARG A CA  
728  C C   . ARG A 136 ? 0.2054 0.2026 0.1692 0.0093  0.0440  -0.0321 104 ARG A C   
729  O O   . ARG A 136 ? 0.2288 0.1880 0.1948 -0.0140 0.0617  -0.0327 104 ARG A O   
730  C CB  . ARG A 136 ? 0.3004 0.3285 0.2448 0.0422  0.0583  -0.0233 104 ARG A CB  
731  C CG  . ARG A 136 ? 0.4199 0.4061 0.3481 0.0304  0.0283  -0.0193 104 ARG A CG  
732  C CD  . ARG A 136 ? 0.5373 0.4839 0.4487 0.0217  -0.0005 -0.0214 104 ARG A CD  
733  N NE  . ARG A 136 ? 0.6459 0.5493 0.5349 0.0083  -0.0288 -0.0236 104 ARG A NE  
734  C CZ  . ARG A 136 ? 0.7280 0.5958 0.5973 -0.0091 -0.0445 -0.0273 104 ARG A CZ  
735  N NH1 . ARG A 136 ? 0.7590 0.6126 0.6168 -0.0193 -0.0454 -0.0291 104 ARG A NH1 
736  N NH2 . ARG A 136 ? 0.7512 0.6139 0.6188 -0.0138 -0.0468 -0.0285 104 ARG A NH2 
737  N N   . TYR A 137 ? 0.1709 0.1944 0.1496 0.0007  0.0443  -0.0289 105 TYR A N   
738  C CA  . TYR A 137 ? 0.1600 0.1880 0.1335 -0.0056 0.0303  -0.0210 105 TYR A CA  
739  C C   . TYR A 137 ? 0.1603 0.1871 0.1428 0.0069  0.0176  -0.0412 105 TYR A C   
740  O O   . TYR A 137 ? 0.1747 0.1907 0.1745 -0.0013 0.0054  -0.0553 105 TYR A O   
741  C CB  . TYR A 137 ? 0.1643 0.1930 0.1607 -0.0267 0.0208  -0.0059 105 TYR A CB  
742  C CG  . TYR A 137 ? 0.1633 0.1902 0.1821 -0.0321 0.0234  -0.0167 105 TYR A CG  
743  C CD1 . TYR A 137 ? 0.1789 0.1828 0.1766 -0.0071 0.0310  -0.0144 105 TYR A CD1 
744  C CD2 . TYR A 137 ? 0.2094 0.1872 0.1903 -0.0257 0.0175  0.0017  105 TYR A CD2 
745  C CE1 . TYR A 137 ? 0.2016 0.1791 0.1796 -0.0064 0.0026  -0.0115 105 TYR A CE1 
746  C CE2 . TYR A 137 ? 0.2295 0.1714 0.1905 -0.0042 0.0186  -0.0026 105 TYR A CE2 
747  C CZ  . TYR A 137 ? 0.2137 0.1565 0.1860 0.0083  0.0003  -0.0174 105 TYR A CZ  
748  O OH  . TYR A 137 ? 0.2187 0.1710 0.2139 0.0114  0.0125  -0.0231 105 TYR A OH  
749  N N   . THR A 138 ? 0.1633 0.1898 0.1255 0.0101  0.0364  -0.0378 106 THR A N   
750  C CA  . THR A 138 ? 0.1795 0.1961 0.1270 0.0104  0.0112  -0.0401 106 THR A CA  
751  C C   . THR A 138 ? 0.1495 0.2184 0.1118 0.0057  0.0044  -0.0605 106 THR A C   
752  O O   . THR A 138 ? 0.1797 0.2557 0.1367 -0.0195 0.0191  -0.0713 106 THR A O   
753  C CB  . THR A 138 ? 0.2209 0.2159 0.1720 0.0287  -0.0116 -0.0285 106 THR A CB  
754  O OG1 . THR A 138 ? 0.3232 0.2292 0.1789 0.0193  -0.0073 -0.0163 106 THR A OG1 
755  C CG2 . THR A 138 ? 0.2362 0.2544 0.2088 0.0516  -0.0254 -0.0129 106 THR A CG2 
756  N N   . ILE A 139 ? 0.1441 0.2473 0.1121 0.0109  0.0041  -0.0524 107 ILE A N   
757  C CA  . ILE A 139 ? 0.1536 0.2563 0.1135 0.0042  0.0124  -0.0504 107 ILE A CA  
758  C C   . ILE A 139 ? 0.1578 0.2384 0.1005 0.0047  -0.0042 -0.0498 107 ILE A C   
759  O O   . ILE A 139 ? 0.1464 0.2479 0.1356 0.0109  -0.0121 -0.0786 107 ILE A O   
760  C CB  . ILE A 139 ? 0.1702 0.2815 0.1641 0.0223  0.0278  -0.0303 107 ILE A CB  
761  C CG1 . ILE A 139 ? 0.2799 0.3178 0.2255 0.0144  0.0397  -0.0213 107 ILE A CG1 
762  C CG2 . ILE A 139 ? 0.1828 0.2787 0.1666 0.0077  -0.0074 -0.0247 107 ILE A CG2 
763  C CD1 . ILE A 139 ? 0.3327 0.3264 0.2653 -0.0199 0.0555  -0.0275 107 ILE A CD1 
764  N N   . ALA A 140 ? 0.1644 0.2099 0.0983 0.0160  0.0024  -0.0169 108 ALA A N   
765  C CA  . ALA A 140 ? 0.1819 0.2086 0.1105 0.0071  0.0126  -0.0220 108 ALA A CA  
766  C C   . ALA A 140 ? 0.1679 0.2278 0.0974 0.0052  -0.0059 -0.0271 108 ALA A C   
767  O O   . ALA A 140 ? 0.1719 0.3022 0.1156 -0.0160 0.0009  -0.0106 108 ALA A O   
768  C CB  . ALA A 140 ? 0.2275 0.2020 0.1393 0.0058  -0.0145 -0.0226 108 ALA A CB  
769  N N   . ALA A 141 ? 0.1262 0.1955 0.1031 0.0175  0.0061  -0.0166 109 ALA A N   
770  C CA  . ALA A 141 ? 0.1406 0.1943 0.1196 0.0180  -0.0014 -0.0054 109 ALA A CA  
771  C C   . ALA A 141 ? 0.1460 0.1887 0.0973 0.0275  -0.0072 -0.0170 109 ALA A C   
772  O O   . ALA A 141 ? 0.1636 0.2159 0.1056 0.0539  -0.0196 -0.0361 109 ALA A O   
773  C CB  . ALA A 141 ? 0.1733 0.2019 0.1582 0.0183  -0.0268 0.0078  109 ALA A CB  
774  N N   . LEU A 142 ? 0.1641 0.1694 0.0984 0.0004  -0.0006 -0.0176 110 LEU A N   
775  C CA  . LEU A 142 ? 0.1954 0.1673 0.0984 0.0173  -0.0207 -0.0276 110 LEU A CA  
776  C C   . LEU A 142 ? 0.1774 0.1833 0.0909 0.0211  0.0023  0.0089  110 LEU A C   
777  O O   . LEU A 142 ? 0.1708 0.2325 0.0992 0.0172  0.0000  0.0181  110 LEU A O   
778  C CB  . LEU A 142 ? 0.2634 0.1805 0.1469 0.0197  -0.0221 -0.0268 110 LEU A CB  
779  C CG  . LEU A 142 ? 0.3408 0.2145 0.2003 0.0114  -0.0314 -0.0356 110 LEU A CG  
780  C CD1 . LEU A 142 ? 0.3785 0.2236 0.2241 0.0429  -0.0250 -0.0124 110 LEU A CD1 
781  C CD2 . LEU A 142 ? 0.4160 0.2231 0.2293 -0.0227 -0.0550 -0.0537 110 LEU A CD2 
782  N N   . LEU A 143 ? 0.1630 0.1561 0.0936 0.0289  -0.0009 -0.0026 111 LEU A N   
783  C CA  . LEU A 143 ? 0.1541 0.1530 0.0959 0.0181  0.0015  0.0078  111 LEU A CA  
784  C C   . LEU A 143 ? 0.1536 0.1501 0.1011 0.0222  -0.0017 0.0164  111 LEU A C   
785  O O   . LEU A 143 ? 0.1738 0.1335 0.1033 0.0151  -0.0093 0.0186  111 LEU A O   
786  C CB  . LEU A 143 ? 0.1789 0.1637 0.1038 0.0019  -0.0133 -0.0144 111 LEU A CB  
787  C CG  . LEU A 143 ? 0.1727 0.1493 0.1169 0.0080  0.0002  -0.0148 111 LEU A CG  
788  C CD1 . LEU A 143 ? 0.2121 0.1526 0.1274 -0.0004 0.0007  -0.0270 111 LEU A CD1 
789  C CD2 . LEU A 143 ? 0.1833 0.1589 0.1267 0.0084  -0.0183 -0.0038 111 LEU A CD2 
790  N N   . SER A 144 ? 0.1742 0.1385 0.0926 0.0150  -0.0049 0.0155  112 SER A N   
791  C CA  . SER A 144 ? 0.1551 0.1479 0.1050 0.0128  0.0095  0.0090  112 SER A CA  
792  C C   . SER A 144 ? 0.1547 0.1450 0.1166 0.0106  -0.0185 0.0124  112 SER A C   
793  O O   . SER A 144 ? 0.1670 0.1369 0.1155 0.0270  -0.0087 0.0078  112 SER A O   
794  C CB  . SER A 144 ? 0.1908 0.1483 0.1183 0.0032  -0.0059 0.0003  112 SER A CB  
795  O OG  . SER A 144 ? 0.2435 0.1676 0.1120 0.0007  0.0050  -0.0032 112 SER A OG  
796  N N   . PRO A 145 ? 0.1468 0.1421 0.1152 0.0158  -0.0070 0.0177  113 PRO A N   
797  C CA  . PRO A 145 ? 0.1683 0.1447 0.1120 0.0146  -0.0045 0.0156  113 PRO A CA  
798  C C   . PRO A 145 ? 0.1565 0.1324 0.1052 0.0019  0.0041  0.0074  113 PRO A C   
799  O O   . PRO A 145 ? 0.1907 0.1180 0.1343 0.0025  0.0015  0.0048  113 PRO A O   
800  C CB  . PRO A 145 ? 0.1780 0.1599 0.1194 0.0190  -0.0078 0.0232  113 PRO A CB  
801  C CG  . PRO A 145 ? 0.1699 0.1833 0.1252 0.0351  -0.0094 0.0147  113 PRO A CG  
802  C CD  . PRO A 145 ? 0.1714 0.1732 0.1374 0.0268  0.0069  0.0212  113 PRO A CD  
803  N N   . TYR A 146 ? 0.1412 0.1621 0.1008 0.0183  0.0034  0.0060  114 TYR A N   
804  C CA  . TYR A 146 ? 0.1709 0.1646 0.0976 0.0191  0.0010  0.0046  114 TYR A CA  
805  C C   . TYR A 146 ? 0.1540 0.1838 0.0902 0.0262  -0.0006 0.0212  114 TYR A C   
806  O O   . TYR A 146 ? 0.1700 0.2212 0.1084 0.0171  -0.0048 0.0239  114 TYR A O   
807  C CB  . TYR A 146 ? 0.1874 0.1878 0.0959 0.0066  0.0123  0.0152  114 TYR A CB  
808  C CG  . TYR A 146 ? 0.2047 0.2122 0.1073 -0.0072 0.0178  -0.0042 114 TYR A CG  
809  C CD1 . TYR A 146 ? 0.2293 0.2734 0.1476 -0.0333 0.0357  0.0021  114 TYR A CD1 
810  C CD2 . TYR A 146 ? 0.2265 0.2043 0.1103 -0.0087 0.0506  -0.0094 114 TYR A CD2 
811  C CE1 . TYR A 146 ? 0.2540 0.3047 0.1823 -0.0668 0.0448  0.0021  114 TYR A CE1 
812  C CE2 . TYR A 146 ? 0.2399 0.2490 0.1585 -0.0462 0.0571  -0.0231 114 TYR A CE2 
813  C CZ  . TYR A 146 ? 0.2683 0.2988 0.2029 -0.0987 0.0775  -0.0010 114 TYR A CZ  
814  O OH  . TYR A 146 ? 0.3234 0.3472 0.2524 -0.1388 0.0817  -0.0065 114 TYR A OH  
815  N N   . SER A 147 ? 0.1316 0.1771 0.1098 0.0223  0.0097  0.0184  115 SER A N   
816  C CA  . SER A 147 ? 0.1583 0.1798 0.1171 0.0053  0.0092  0.0208  115 SER A CA  
817  C C   . SER A 147 ? 0.1386 0.2028 0.1130 0.0175  0.0131  0.0235  115 SER A C   
818  O O   . SER A 147 ? 0.1532 0.2485 0.1144 0.0291  -0.0166 0.0404  115 SER A O   
819  C CB  . SER A 147 ? 0.1857 0.1805 0.1545 0.0009  -0.0043 0.0309  115 SER A CB  
820  O OG  . SER A 147 ? 0.1983 0.1785 0.1590 -0.0004 0.0009  0.0323  115 SER A OG  
821  N N   . TYR A 148 ? 0.1459 0.1946 0.0826 -0.0070 0.0133  0.0104  116 TYR A N   
822  C CA  . TYR A 148 ? 0.1422 0.2244 0.0922 -0.0155 0.0066  -0.0014 116 TYR A CA  
823  C C   . TYR A 148 ? 0.1474 0.2266 0.0884 -0.0050 0.0015  0.0069  116 TYR A C   
824  O O   . TYR A 148 ? 0.1587 0.2232 0.0966 -0.0114 -0.0104 0.0033  116 TYR A O   
825  C CB  . TYR A 148 ? 0.1803 0.2368 0.1245 -0.0189 -0.0189 -0.0001 116 TYR A CB  
826  C CG  . TYR A 148 ? 0.1770 0.2110 0.1543 -0.0310 -0.0194 -0.0092 116 TYR A CG  
827  C CD1 . TYR A 148 ? 0.2062 0.2143 0.1725 -0.0094 -0.0234 -0.0183 116 TYR A CD1 
828  C CD2 . TYR A 148 ? 0.2501 0.2099 0.1863 -0.0335 -0.0128 -0.0059 116 TYR A CD2 
829  C CE1 . TYR A 148 ? 0.2426 0.2041 0.2149 -0.0130 -0.0573 -0.0147 116 TYR A CE1 
830  C CE2 . TYR A 148 ? 0.2816 0.2068 0.2212 -0.0310 -0.0299 -0.0137 116 TYR A CE2 
831  C CZ  . TYR A 148 ? 0.2882 0.2007 0.2483 -0.0109 -0.0399 -0.0131 116 TYR A CZ  
832  O OH  . TYR A 148 ? 0.3654 0.2059 0.3205 -0.0003 -0.0349 0.0031  116 TYR A OH  
833  N N   . SER A 149 ? 0.1535 0.2506 0.0889 -0.0096 0.0130  0.0098  117 SER A N   
834  C CA  . SER A 149 ? 0.1906 0.2599 0.1314 -0.0087 0.0062  0.0123  117 SER A CA  
835  C C   . SER A 149 ? 0.1545 0.2693 0.1051 -0.0222 -0.0310 0.0064  117 SER A C   
836  O O   . SER A 149 ? 0.1555 0.2723 0.1081 -0.0317 -0.0032 0.0103  117 SER A O   
837  C CB  . SER A 149 ? 0.3223 0.2858 0.1969 -0.0002 -0.0002 0.0030  117 SER A CB  
838  O OG  . SER A 149 ? 0.3823 0.2899 0.2288 0.0523  0.0146  0.0114  117 SER A OG  
839  N N   . THR A 150 ? 0.1660 0.2877 0.0923 -0.0202 -0.0017 -0.0012 118 THR A N   
840  C CA  . THR A 150 ? 0.1513 0.2947 0.1129 -0.0324 -0.0095 -0.0082 118 THR A CA  
841  C C   . THR A 150 ? 0.1347 0.2812 0.1186 -0.0398 -0.0103 -0.0128 118 THR A C   
842  O O   . THR A 150 ? 0.1765 0.3216 0.1282 -0.0657 -0.0193 0.0012  118 THR A O   
843  C CB  . THR A 150 ? 0.1948 0.3034 0.1685 -0.0393 -0.0299 -0.0078 118 THR A CB  
844  O OG1 . THR A 150 ? 0.2489 0.3137 0.2049 -0.0111 -0.0095 -0.0363 118 THR A OG1 
845  C CG2 . THR A 150 ? 0.2101 0.2965 0.1578 -0.0452 -0.0542 -0.0046 118 THR A CG2 
846  N N   . THR A 151 ? 0.1469 0.2334 0.1176 -0.0005 0.0173  -0.0124 119 THR A N   
847  C CA  . THR A 151 ? 0.1550 0.1919 0.1182 0.0140  0.0361  0.0058  119 THR A CA  
848  C C   . THR A 151 ? 0.1600 0.1983 0.1291 0.0000  0.0190  -0.0122 119 THR A C   
849  O O   . THR A 151 ? 0.1489 0.2479 0.1440 -0.0124 -0.0084 -0.0536 119 THR A O   
850  C CB  . THR A 151 ? 0.2123 0.1913 0.1653 0.0193  0.0462  -0.0186 119 THR A CB  
851  O OG1 . THR A 151 ? 0.2352 0.2037 0.1805 0.0138  -0.0013 -0.0294 119 THR A OG1 
852  C CG2 . THR A 151 ? 0.2988 0.1791 0.2013 -0.0094 0.0724  -0.0065 119 THR A CG2 
853  N N   . ALA A 152 ? 0.1500 0.1885 0.1062 -0.0125 0.0119  -0.0112 120 ALA A N   
854  C CA  . ALA A 152 ? 0.1634 0.1865 0.1199 0.0038  0.0302  -0.0194 120 ALA A CA  
855  C C   . ALA A 152 ? 0.1557 0.1758 0.1320 -0.0103 0.0260  -0.0248 120 ALA A C   
856  O O   . ALA A 152 ? 0.1768 0.2033 0.1580 -0.0227 0.0308  -0.0252 120 ALA A O   
857  C CB  . ALA A 152 ? 0.1879 0.1934 0.1618 0.0230  0.0075  -0.0172 120 ALA A CB  
858  N N   . VAL A 153 ? 0.1602 0.1610 0.1260 0.0013  0.0201  -0.0239 121 VAL A N   
859  C CA  . VAL A 153 ? 0.2016 0.1840 0.1421 -0.0029 0.0361  -0.0189 121 VAL A CA  
860  C C   . VAL A 153 ? 0.2100 0.1881 0.1368 -0.0197 0.0379  -0.0387 121 VAL A C   
861  O O   . VAL A 153 ? 0.2103 0.2008 0.1484 -0.0230 0.0333  -0.0562 121 VAL A O   
862  C CB  . VAL A 153 ? 0.2503 0.1918 0.1828 0.0112  0.0203  -0.0019 121 VAL A CB  
863  C CG1 . VAL A 153 ? 0.2855 0.2107 0.2091 -0.0515 0.0022  0.0148  121 VAL A CG1 
864  C CG2 . VAL A 153 ? 0.3274 0.1988 0.2167 0.0475  0.0110  -0.0151 121 VAL A CG2 
865  N N   . VAL A 154 ? 0.2131 0.1705 0.1617 0.0010  0.0402  -0.0304 122 VAL A N   
866  C CA  . VAL A 154 ? 0.2294 0.1808 0.1823 0.0059  0.0458  -0.0480 122 VAL A CA  
867  C C   . VAL A 154 ? 0.2421 0.1906 0.2191 -0.0195 0.0826  -0.0365 122 VAL A C   
868  O O   . VAL A 154 ? 0.2389 0.2117 0.2538 -0.0518 0.0695  -0.0574 122 VAL A O   
869  C CB  . VAL A 154 ? 0.2614 0.1917 0.2074 0.0267  0.0696  -0.0513 122 VAL A CB  
870  C CG1 . VAL A 154 ? 0.3037 0.1855 0.2266 0.0338  0.0619  -0.0580 122 VAL A CG1 
871  C CG2 . VAL A 154 ? 0.2998 0.1980 0.2256 0.0108  0.0714  -0.0372 122 VAL A CG2 
872  N N   . THR A 155 ? 0.2655 0.1956 0.2281 -0.0177 0.1324  -0.0197 123 THR A N   
873  C CA  . THR A 155 ? 0.3243 0.2538 0.2762 -0.0233 0.1551  -0.0019 123 THR A CA  
874  C C   . THR A 155 ? 0.3280 0.2512 0.2980 -0.0316 0.1585  -0.0131 123 THR A C   
875  O O   . THR A 155 ? 0.3299 0.2392 0.2772 -0.0339 0.1403  -0.0070 123 THR A O   
876  C CB  . THR A 155 ? 0.4162 0.3086 0.3294 -0.0077 0.1331  0.0229  123 THR A CB  
877  O OG1 . THR A 155 ? 0.4655 0.3496 0.3779 0.0001  0.1060  0.0181  123 THR A OG1 
878  C CG2 . THR A 155 ? 0.4397 0.3154 0.3307 -0.0129 0.1257  0.0357  123 THR A CG2 
879  N N   . ASN A 156 ? 0.3667 0.2906 0.3487 -0.0401 0.1892  -0.0353 124 ASN A N   
880  C CA  . ASN A 156 ? 0.4443 0.3262 0.4043 -0.0327 0.2178  -0.0334 124 ASN A CA  
881  C C   . ASN A 156 ? 0.5412 0.3711 0.4324 -0.0286 0.2218  -0.0270 124 ASN A C   
882  O O   . ASN A 156 ? 0.5762 0.3762 0.4403 -0.0267 0.2339  -0.0173 124 ASN A O   
883  C CB  . ASN A 156 ? 0.4645 0.3327 0.4428 -0.0065 0.2050  -0.0378 124 ASN A CB  
884  C CG  . ASN A 156 ? 0.4754 0.3413 0.4725 0.0105  0.1929  -0.0255 124 ASN A CG  
885  O OD1 . ASN A 156 ? 0.4759 0.3425 0.4702 0.0266  0.2154  -0.0240 124 ASN A OD1 
886  N ND2 . ASN A 156 ? 0.5049 0.3475 0.4906 0.0037  0.1582  -0.0209 124 ASN A ND2 
887  N N   . PRO A 157 ? 0.5939 0.4132 0.4582 -0.0252 0.1995  -0.0331 125 PRO A N   
888  C CA  . PRO A 157 ? 0.6324 0.4393 0.4890 -0.0224 0.1727  -0.0404 125 PRO A CA  
889  C C   . PRO A 157 ? 0.6520 0.4593 0.5084 -0.0199 0.1798  -0.0418 125 PRO A C   
890  O O   . PRO A 157 ? 0.6718 0.4734 0.5208 -0.0229 0.1893  -0.0422 125 PRO A O   
891  C CB  . PRO A 157 ? 0.6270 0.4395 0.4899 -0.0320 0.1567  -0.0400 125 PRO A CB  
892  C CG  . PRO A 157 ? 0.6173 0.4337 0.4830 -0.0363 0.1659  -0.0404 125 PRO A CG  
893  C CD  . PRO A 157 ? 0.5978 0.4219 0.4653 -0.0335 0.1926  -0.0392 125 PRO A CD  
894  N N   . CYS B 42  ? 0.5484 0.6126 0.4944 -0.0343 0.1151  0.0657  10  CYS B N   
895  C CA  . CYS B 42  ? 0.5229 0.6017 0.4848 -0.0296 0.1230  0.0688  10  CYS B CA  
896  C C   . CYS B 42  ? 0.3972 0.5027 0.4388 -0.0129 0.1307  0.0619  10  CYS B C   
897  O O   . CYS B 42  ? 0.3723 0.4987 0.4643 0.0136  0.1562  0.0499  10  CYS B O   
898  C CB  . CYS B 42  ? 0.6111 0.6660 0.5188 -0.0404 0.1256  0.0790  10  CYS B CB  
899  S SG  . CYS B 42  ? 0.6808 0.7011 0.5507 -0.0498 0.1165  0.0860  10  CYS B SG  
900  N N   . PRO B 43  ? 0.3015 0.4046 0.3625 -0.0293 0.1207  0.0697  11  PRO B N   
901  C CA  . PRO B 43  ? 0.2588 0.3350 0.3026 -0.0461 0.0816  0.0752  11  PRO B CA  
902  C C   . PRO B 43  ? 0.2354 0.2805 0.2338 -0.0390 0.0209  0.0761  11  PRO B C   
903  O O   . PRO B 43  ? 0.2253 0.2882 0.2086 -0.0343 0.0150  0.0822  11  PRO B O   
904  C CB  . PRO B 43  ? 0.3435 0.3475 0.3302 -0.0409 0.0839  0.0676  11  PRO B CB  
905  C CG  . PRO B 43  ? 0.3878 0.3704 0.3593 -0.0274 0.0765  0.0560  11  PRO B CG  
906  C CD  . PRO B 43  ? 0.3584 0.3917 0.3614 -0.0229 0.0961  0.0606  11  PRO B CD  
907  N N   . LEU B 44  ? 0.2110 0.2198 0.1844 -0.0472 0.0067  0.0668  12  LEU B N   
908  C CA  . LEU B 44  ? 0.2091 0.2150 0.1755 -0.0380 0.0118  0.0554  12  LEU B CA  
909  C C   . LEU B 44  ? 0.2049 0.2125 0.1539 -0.0292 0.0117  0.0659  12  LEU B C   
910  O O   . LEU B 44  ? 0.2435 0.2412 0.1725 -0.0150 -0.0200 0.0767  12  LEU B O   
911  C CB  . LEU B 44  ? 0.2441 0.2273 0.1892 -0.0102 0.0301  0.0325  12  LEU B CB  
912  C CG  . LEU B 44  ? 0.2332 0.2372 0.2094 0.0051  0.0103  0.0205  12  LEU B CG  
913  C CD1 . LEU B 44  ? 0.2012 0.2487 0.2081 0.0237  0.0016  0.0175  12  LEU B CD1 
914  C CD2 . LEU B 44  ? 0.2845 0.2330 0.2424 0.0226  0.0101  0.0180  12  LEU B CD2 
915  N N   . MET B 45  ? 0.2018 0.1895 0.1337 -0.0399 0.0221  0.0424  13  MET B N   
916  C CA  . MET B 45  ? 0.1806 0.1938 0.1225 -0.0325 0.0221  0.0395  13  MET B CA  
917  C C   . MET B 45  ? 0.1541 0.1754 0.1163 -0.0061 0.0002  0.0353  13  MET B C   
918  O O   . MET B 45  ? 0.1658 0.2038 0.1134 -0.0034 -0.0131 0.0284  13  MET B O   
919  C CB  . MET B 45  ? 0.2475 0.2210 0.1526 -0.0355 0.0237  0.0249  13  MET B CB  
920  C CG  . MET B 45  ? 0.2959 0.2325 0.1978 -0.0207 0.0294  0.0210  13  MET B CG  
921  S SD  . MET B 45  ? 0.3035 0.2415 0.2438 -0.0043 0.0215  0.0142  13  MET B SD  
922  C CE  . MET B 45  ? 0.3400 0.2452 0.2717 -0.0031 0.0066  -0.0072 13  MET B CE  
923  N N   . VAL B 46  ? 0.1710 0.1614 0.1278 -0.0117 0.0048  0.0243  14  VAL B N   
924  C CA  . VAL B 46  ? 0.1700 0.1620 0.1192 -0.0133 0.0175  0.0352  14  VAL B CA  
925  C C   . VAL B 46  ? 0.1572 0.1809 0.1218 -0.0137 -0.0227 0.0370  14  VAL B C   
926  O O   . VAL B 46  ? 0.1981 0.2030 0.1308 -0.0281 -0.0522 0.0570  14  VAL B O   
927  C CB  . VAL B 46  ? 0.1698 0.1792 0.1368 0.0122  0.0193  0.0382  14  VAL B CB  
928  C CG1 . VAL B 46  ? 0.1932 0.1843 0.1315 0.0260  0.0162  0.0535  14  VAL B CG1 
929  C CG2 . VAL B 46  ? 0.1943 0.1771 0.1578 -0.0068 0.0058  0.0232  14  VAL B CG2 
930  N N   . LYS B 47  ? 0.1630 0.1550 0.1164 -0.0127 -0.0117 0.0403  15  LYS B N   
931  C CA  . LYS B 47  ? 0.1737 0.1559 0.1154 -0.0215 -0.0121 0.0235  15  LYS B CA  
932  C C   . LYS B 47  ? 0.1542 0.1730 0.0974 -0.0255 -0.0195 0.0263  15  LYS B C   
933  O O   . LYS B 47  ? 0.1874 0.2122 0.0981 -0.0325 -0.0266 0.0279  15  LYS B O   
934  C CB  . LYS B 47  ? 0.2424 0.1506 0.1551 -0.0114 0.0043  -0.0167 15  LYS B CB  
935  C CG  . LYS B 47  ? 0.2757 0.1673 0.1932 -0.0162 0.0173  -0.0443 15  LYS B CG  
936  C CD  . LYS B 47  ? 0.3485 0.1874 0.2330 -0.0411 0.0227  -0.0556 15  LYS B CD  
937  C CE  . LYS B 47  ? 0.4195 0.2142 0.2646 -0.0320 0.0409  -0.0761 15  LYS B CE  
938  N NZ  . LYS B 47  ? 0.4595 0.2554 0.2846 -0.0129 0.0713  -0.0787 15  LYS B NZ  
939  N N   . VAL B 48  ? 0.1762 0.1691 0.1020 -0.0200 -0.0047 0.0157  16  VAL B N   
940  C CA  . VAL B 48  ? 0.1595 0.1570 0.1127 -0.0269 -0.0113 0.0092  16  VAL B CA  
941  C C   . VAL B 48  ? 0.1619 0.1760 0.1240 -0.0239 -0.0280 0.0103  16  VAL B C   
942  O O   . VAL B 48  ? 0.1807 0.1770 0.1344 -0.0268 -0.0224 0.0054  16  VAL B O   
943  C CB  . VAL B 48  ? 0.1840 0.1617 0.1194 -0.0274 -0.0002 0.0154  16  VAL B CB  
944  C CG1 . VAL B 48  ? 0.2074 0.1873 0.1104 -0.0248 0.0149  -0.0147 16  VAL B CG1 
945  C CG2 . VAL B 48  ? 0.1889 0.1595 0.1486 -0.0293 -0.0347 0.0042  16  VAL B CG2 
946  N N   . LEU B 49  ? 0.1578 0.1672 0.1171 -0.0255 -0.0067 0.0134  17  LEU B N   
947  C CA  . LEU B 49  ? 0.1490 0.1635 0.1242 -0.0109 -0.0031 0.0157  17  LEU B CA  
948  C C   . LEU B 49  ? 0.1712 0.1476 0.0983 -0.0192 -0.0132 0.0135  17  LEU B C   
949  O O   . LEU B 49  ? 0.1675 0.1482 0.1165 -0.0124 -0.0201 0.0032  17  LEU B O   
950  C CB  . LEU B 49  ? 0.1830 0.2058 0.1512 0.0170  0.0152  0.0061  17  LEU B CB  
951  C CG  . LEU B 49  ? 0.2076 0.2440 0.1725 0.0346  -0.0038 0.0032  17  LEU B CG  
952  C CD1 . LEU B 49  ? 0.2568 0.2698 0.2220 0.0330  -0.0082 -0.0027 17  LEU B CD1 
953  C CD2 . LEU B 49  ? 0.2467 0.2616 0.1721 0.0325  0.0085  -0.0067 17  LEU B CD2 
954  N N   . ASP B 50  ? 0.1789 0.1514 0.1096 -0.0228 -0.0002 0.0185  18  ASP B N   
955  C CA  . ASP B 50  ? 0.1955 0.1425 0.1128 -0.0317 0.0007  0.0099  18  ASP B CA  
956  C C   . ASP B 50  ? 0.2106 0.1255 0.1101 -0.0191 0.0013  -0.0067 18  ASP B C   
957  O O   . ASP B 50  ? 0.2110 0.1359 0.1155 -0.0102 0.0184  -0.0142 18  ASP B O   
958  C CB  . ASP B 50  ? 0.1667 0.1542 0.1350 -0.0152 0.0001  0.0060  18  ASP B CB  
959  C CG  . ASP B 50  ? 0.1837 0.1639 0.1637 -0.0146 0.0084  -0.0006 18  ASP B CG  
960  O OD1 . ASP B 50  ? 0.1958 0.1470 0.1586 -0.0218 0.0107  -0.0037 18  ASP B OD1 
961  O OD2 . ASP B 50  ? 0.1958 0.1912 0.2096 0.0084  0.0038  0.0173  18  ASP B OD2 
962  N N   . ALA B 51  ? 0.2294 0.1319 0.1091 0.0143  -0.0082 0.0083  19  ALA B N   
963  C CA  . ALA B 51  ? 0.2602 0.1390 0.1162 0.0248  -0.0332 0.0077  19  ALA B CA  
964  C C   . ALA B 51  ? 0.3113 0.1298 0.1127 -0.0010 -0.0171 0.0003  19  ALA B C   
965  O O   . ALA B 51  ? 0.3853 0.1435 0.1274 0.0113  -0.0509 -0.0011 19  ALA B O   
966  C CB  . ALA B 51  ? 0.2382 0.1702 0.1461 0.0377  -0.0485 -0.0054 19  ALA B CB  
967  N N   . VAL B 52  ? 0.2974 0.1592 0.1218 -0.0415 0.0110  -0.0131 20  VAL B N   
968  C CA  . VAL B 52  ? 0.3318 0.1708 0.1438 -0.0642 0.0345  -0.0348 20  VAL B CA  
969  C C   . VAL B 52  ? 0.3269 0.1830 0.1388 -0.0658 0.0490  -0.0238 20  VAL B C   
970  O O   . VAL B 52  ? 0.3951 0.1768 0.1756 -0.0859 0.0365  0.0013  20  VAL B O   
971  C CB  . VAL B 52  ? 0.3648 0.1791 0.1518 -0.0760 0.0600  -0.0382 20  VAL B CB  
972  C CG1 . VAL B 52  ? 0.3649 0.2093 0.1738 -0.1029 0.0849  -0.0252 20  VAL B CG1 
973  C CG2 . VAL B 52  ? 0.4081 0.1764 0.1513 -0.0811 0.0451  -0.0357 20  VAL B CG2 
974  N N   . ARG B 53  ? 0.2478 0.1912 0.1346 -0.0365 0.0170  -0.0401 21  ARG B N   
975  C CA  . ARG B 53  ? 0.2078 0.2027 0.1636 -0.0142 0.0207  -0.0425 21  ARG B CA  
976  C C   . ARG B 53  ? 0.2119 0.1798 0.1467 -0.0244 0.0267  -0.0226 21  ARG B C   
977  O O   . ARG B 53  ? 0.2551 0.2119 0.1664 -0.0414 0.0082  -0.0596 21  ARG B O   
978  C CB  . ARG B 53  ? 0.1753 0.2427 0.2297 0.0099  0.0134  -0.0478 21  ARG B CB  
979  C CG  . ARG B 53  ? 0.2279 0.2708 0.2827 0.0248  0.0268  -0.0427 21  ARG B CG  
980  C CD  . ARG B 53  ? 0.2601 0.2990 0.3219 0.0093  0.0111  -0.0375 21  ARG B CD  
981  N NE  . ARG B 53  ? 0.2979 0.3161 0.3447 0.0046  -0.0061 -0.0304 21  ARG B NE  
982  C CZ  . ARG B 53  ? 0.3336 0.3367 0.3564 -0.0038 -0.0272 -0.0289 21  ARG B CZ  
983  N NH1 . ARG B 53  ? 0.3472 0.3435 0.3660 -0.0062 -0.0396 -0.0328 21  ARG B NH1 
984  N NH2 . ARG B 53  ? 0.3651 0.3453 0.3609 -0.0027 -0.0298 -0.0243 21  ARG B NH2 
985  N N   . GLY B 54  ? 0.2061 0.1622 0.1377 0.0063  0.0290  0.0021  22  GLY B N   
986  C CA  . GLY B 54  ? 0.2186 0.1670 0.1195 0.0158  0.0287  0.0048  22  GLY B CA  
987  C C   . GLY B 54  ? 0.2021 0.1583 0.1210 0.0113  0.0094  -0.0049 22  GLY B C   
988  O O   . GLY B 54  ? 0.1952 0.1704 0.1372 0.0132  0.0073  -0.0156 22  GLY B O   
989  N N   . SER B 55  ? 0.2261 0.1560 0.1256 -0.0035 0.0066  0.0136  23  SER B N   
990  C CA  . SER B 55  ? 0.2109 0.1753 0.1268 -0.0192 -0.0097 0.0151  23  SER B CA  
991  C C   . SER B 55  ? 0.2178 0.1597 0.1189 -0.0071 -0.0297 0.0120  23  SER B C   
992  O O   . SER B 55  ? 0.2435 0.1653 0.1270 -0.0114 -0.0202 -0.0013 23  SER B O   
993  C CB  . SER B 55  ? 0.2511 0.2252 0.1827 -0.0174 -0.0127 -0.0028 23  SER B CB  
994  O OG  . SER B 55  ? 0.2944 0.2743 0.2243 -0.0195 -0.0104 0.0153  23  SER B OG  
995  N N   . PRO B 56  ? 0.2298 0.1552 0.1155 -0.0143 -0.0402 0.0072  24  PRO B N   
996  C CA  . PRO B 56  ? 0.2294 0.1425 0.1147 -0.0138 -0.0167 0.0065  24  PRO B CA  
997  C C   . PRO B 56  ? 0.1937 0.1413 0.1554 -0.0291 -0.0244 0.0090  24  PRO B C   
998  O O   . PRO B 56  ? 0.2130 0.1581 0.1950 -0.0283 -0.0098 -0.0083 24  PRO B O   
999  C CB  . PRO B 56  ? 0.2696 0.1567 0.1085 -0.0094 -0.0372 0.0001  24  PRO B CB  
1000 C CG  . PRO B 56  ? 0.3592 0.1928 0.1460 -0.0256 -0.0342 0.0056  24  PRO B CG  
1001 C CD  . PRO B 56  ? 0.2702 0.1610 0.1192 -0.0039 -0.0584 -0.0049 24  PRO B CD  
1002 N N   . ALA B 57  ? 0.2036 0.1339 0.1401 -0.0070 -0.0149 -0.0002 25  ALA B N   
1003 C CA  . ALA B 57  ? 0.1879 0.1548 0.1351 -0.0001 -0.0242 0.0069  25  ALA B CA  
1004 C C   . ALA B 57  ? 0.1741 0.1630 0.1379 -0.0149 -0.0233 0.0110  25  ALA B C   
1005 O O   . ALA B 57  ? 0.1771 0.1700 0.1565 -0.0120 -0.0150 0.0266  25  ALA B O   
1006 C CB  . ALA B 57  ? 0.1982 0.1768 0.1228 -0.0246 -0.0073 0.0109  25  ALA B CB  
1007 N N   . ILE B 58  ? 0.1766 0.1885 0.1433 -0.0004 -0.0403 0.0113  26  ILE B N   
1008 C CA  . ILE B 58  ? 0.1999 0.2029 0.1538 0.0080  -0.0447 -0.0043 26  ILE B CA  
1009 C C   . ILE B 58  ? 0.2060 0.2015 0.1727 0.0040  -0.0420 0.0106  26  ILE B C   
1010 O O   . ILE B 58  ? 0.2395 0.2021 0.1936 -0.0148 -0.0192 0.0167  26  ILE B O   
1011 C CB  . ILE B 58  ? 0.2905 0.2263 0.1692 -0.0064 -0.0715 -0.0280 26  ILE B CB  
1012 C CG1 . ILE B 58  ? 0.3338 0.2437 0.1905 -0.0213 -0.0957 -0.0362 26  ILE B CG1 
1013 C CG2 . ILE B 58  ? 0.3285 0.2582 0.2091 -0.0056 -0.0712 -0.0370 26  ILE B CG2 
1014 C CD1 . ILE B 58  ? 0.4006 0.2736 0.2403 -0.0347 -0.0908 -0.0304 26  ILE B CD1 
1015 N N   . ASN B 59  ? 0.2010 0.2044 0.1864 -0.0013 -0.0708 0.0031  27  ASN B N   
1016 C CA  . ASN B 59  ? 0.1951 0.2302 0.2105 0.0148  -0.0345 -0.0087 27  ASN B CA  
1017 C C   . ASN B 59  ? 0.2015 0.2034 0.1921 0.0044  -0.0003 -0.0017 27  ASN B C   
1018 O O   . ASN B 59  ? 0.2028 0.2129 0.2252 0.0190  -0.0056 -0.0103 27  ASN B O   
1019 C CB  . ASN B 59  ? 0.2232 0.2934 0.2604 0.0187  -0.0265 -0.0170 27  ASN B CB  
1020 C CG  . ASN B 59  ? 0.3285 0.3453 0.3184 0.0208  -0.0251 -0.0211 27  ASN B CG  
1021 O OD1 . ASN B 59  ? 0.3766 0.3674 0.3398 0.0193  -0.0348 -0.0105 27  ASN B OD1 
1022 N ND2 . ASN B 59  ? 0.3567 0.3655 0.3506 0.0165  -0.0414 -0.0244 27  ASN B ND2 
1023 N N   . VAL B 60  ? 0.1669 0.1754 0.1614 -0.0112 -0.0165 0.0042  28  VAL B N   
1024 C CA  . VAL B 60  ? 0.1993 0.1475 0.1591 -0.0029 -0.0116 0.0048  28  VAL B CA  
1025 C C   . VAL B 60  ? 0.1827 0.1404 0.1493 0.0029  -0.0144 0.0261  28  VAL B C   
1026 O O   . VAL B 60  ? 0.1962 0.1688 0.1305 -0.0151 0.0051  0.0164  28  VAL B O   
1027 C CB  . VAL B 60  ? 0.2340 0.1553 0.1437 -0.0100 -0.0100 0.0164  28  VAL B CB  
1028 C CG1 . VAL B 60  ? 0.2703 0.1756 0.1536 -0.0161 0.0083  0.0077  28  VAL B CG1 
1029 C CG2 . VAL B 60  ? 0.2683 0.1368 0.1602 -0.0107 0.0396  0.0117  28  VAL B CG2 
1030 N N   . ALA B 61  ? 0.1900 0.1421 0.1563 0.0063  -0.0115 0.0182  29  ALA B N   
1031 C CA  . ALA B 61  ? 0.1843 0.1365 0.1581 0.0169  -0.0110 0.0193  29  ALA B CA  
1032 C C   . ALA B 61  ? 0.1678 0.1435 0.1286 0.0170  -0.0122 0.0217  29  ALA B C   
1033 O O   . ALA B 61  ? 0.1947 0.1765 0.1149 0.0140  -0.0212 0.0266  29  ALA B O   
1034 C CB  . ALA B 61  ? 0.1845 0.1519 0.1603 0.0373  -0.0211 0.0085  29  ALA B CB  
1035 N N   . MET B 62  ? 0.1676 0.1586 0.1232 -0.0039 -0.0118 0.0208  30  MET B N   
1036 C CA  . MET B 62  ? 0.1628 0.1645 0.1244 0.0186  -0.0207 0.0223  30  MET B CA  
1037 C C   . MET B 62  ? 0.1705 0.1718 0.1186 0.0168  -0.0286 0.0260  30  MET B C   
1038 O O   . MET B 62  ? 0.1629 0.1707 0.1291 0.0116  -0.0193 0.0204  30  MET B O   
1039 C CB  . MET B 62  ? 0.1849 0.1708 0.1300 0.0480  -0.0069 0.0282  30  MET B CB  
1040 C CG  . MET B 62  ? 0.1767 0.1675 0.1257 0.0419  -0.0039 0.0238  30  MET B CG  
1041 S SD  . MET B 62  ? 0.1710 0.1704 0.1493 0.0130  -0.0126 0.0108  30  MET B SD  
1042 C CE  . MET B 62  ? 0.1823 0.1862 0.1636 -0.0109 0.0034  -0.0059 30  MET B CE  
1043 N N   . HIS B 63  ? 0.1482 0.1743 0.1429 -0.0050 -0.0100 0.0108  31  HIS B N   
1044 C CA  . HIS B 63  ? 0.1457 0.1903 0.1519 0.0036  -0.0160 0.0227  31  HIS B CA  
1045 C C   . HIS B 63  ? 0.1569 0.1962 0.1388 -0.0079 -0.0235 0.0188  31  HIS B C   
1046 O O   . HIS B 63  ? 0.1695 0.2065 0.1520 -0.0007 -0.0123 0.0421  31  HIS B O   
1047 C CB  . HIS B 63  ? 0.1820 0.2190 0.1830 0.0179  -0.0078 0.0257  31  HIS B CB  
1048 C CG  . HIS B 63  ? 0.2024 0.2577 0.1903 0.0215  -0.0221 0.0520  31  HIS B CG  
1049 N ND1 . HIS B 63  ? 0.2481 0.3062 0.2228 0.0603  0.0088  0.0476  31  HIS B ND1 
1050 C CD2 . HIS B 63  ? 0.2314 0.2791 0.2231 0.0181  -0.0332 0.0602  31  HIS B CD2 
1051 C CE1 . HIS B 63  ? 0.2505 0.3085 0.2308 0.0815  -0.0179 0.0505  31  HIS B CE1 
1052 N NE2 . HIS B 63  ? 0.2378 0.2876 0.2441 0.0274  -0.0399 0.0663  31  HIS B NE2 
1053 N N   . VAL B 64  ? 0.1253 0.2082 0.1471 0.0011  -0.0110 0.0241  32  VAL B N   
1054 C CA  . VAL B 64  ? 0.1544 0.1881 0.1502 -0.0093 -0.0139 0.0361  32  VAL B CA  
1055 C C   . VAL B 64  ? 0.1436 0.1865 0.1568 0.0032  -0.0197 0.0392  32  VAL B C   
1056 O O   . VAL B 64  ? 0.1753 0.1885 0.1650 0.0054  -0.0056 0.0383  32  VAL B O   
1057 C CB  . VAL B 64  ? 0.1714 0.1746 0.1467 0.0029  -0.0155 0.0286  32  VAL B CB  
1058 C CG1 . VAL B 64  ? 0.1885 0.1760 0.1703 0.0211  -0.0142 0.0283  32  VAL B CG1 
1059 C CG2 . VAL B 64  ? 0.2107 0.1842 0.1593 -0.0027 -0.0208 0.0201  32  VAL B CG2 
1060 N N   . PHE B 65  ? 0.1484 0.1764 0.1737 -0.0103 -0.0201 0.0225  33  PHE B N   
1061 C CA  . PHE B 65  ? 0.1777 0.1745 0.1793 0.0060  -0.0119 0.0235  33  PHE B CA  
1062 C C   . PHE B 65  ? 0.1724 0.1624 0.1770 0.0004  -0.0229 0.0397  33  PHE B C   
1063 O O   . PHE B 65  ? 0.1759 0.1632 0.1742 0.0011  -0.0055 0.0556  33  PHE B O   
1064 C CB  . PHE B 65  ? 0.2041 0.1887 0.1906 0.0130  -0.0176 0.0071  33  PHE B CB  
1065 C CG  . PHE B 65  ? 0.1971 0.2039 0.1909 0.0196  -0.0271 -0.0054 33  PHE B CG  
1066 C CD1 . PHE B 65  ? 0.2360 0.2284 0.2022 0.0016  -0.0266 -0.0089 33  PHE B CD1 
1067 C CD2 . PHE B 65  ? 0.1888 0.2272 0.1981 0.0328  -0.0128 0.0043  33  PHE B CD2 
1068 C CE1 . PHE B 65  ? 0.2474 0.2443 0.2026 0.0139  -0.0192 -0.0085 33  PHE B CE1 
1069 C CE2 . PHE B 65  ? 0.2316 0.2425 0.2061 0.0467  0.0054  -0.0024 33  PHE B CE2 
1070 C CZ  . PHE B 65  ? 0.2648 0.2463 0.1963 0.0301  -0.0111 -0.0256 33  PHE B CZ  
1071 N N   . ARG B 66  ? 0.1909 0.1644 0.1889 -0.0035 -0.0438 0.0434  34  ARG B N   
1072 C CA  . ARG B 66  ? 0.2059 0.1814 0.2128 -0.0287 -0.0377 0.0339  34  ARG B CA  
1073 C C   . ARG B 66  ? 0.2484 0.1722 0.2136 -0.0134 -0.0412 0.0265  34  ARG B C   
1074 O O   . ARG B 66  ? 0.2822 0.1758 0.2165 0.0061  -0.0661 0.0275  34  ARG B O   
1075 C CB  . ARG B 66  ? 0.2129 0.2024 0.2340 -0.0320 -0.0114 0.0259  34  ARG B CB  
1076 C CG  . ARG B 66  ? 0.2813 0.2369 0.2733 -0.0498 0.0027  0.0276  34  ARG B CG  
1077 C CD  . ARG B 66  ? 0.3837 0.2758 0.3187 -0.0772 0.0031  0.0273  34  ARG B CD  
1078 N NE  . ARG B 66  ? 0.4925 0.3084 0.3695 -0.0908 0.0119  0.0247  34  ARG B NE  
1079 C CZ  . ARG B 66  ? 0.5682 0.3256 0.4069 -0.1054 0.0294  0.0046  34  ARG B CZ  
1080 N NH1 . ARG B 66  ? 0.6013 0.3302 0.4269 -0.1075 0.0309  -0.0149 34  ARG B NH1 
1081 N NH2 . ARG B 66  ? 0.5894 0.3432 0.4170 -0.1040 0.0182  0.0062  34  ARG B NH2 
1082 N N   . LYS B 67  ? 0.2714 0.1888 0.2066 -0.0262 -0.0531 0.0248  35  LYS B N   
1083 C CA  . LYS B 67  ? 0.2640 0.2188 0.2171 -0.0248 -0.0722 0.0157  35  LYS B CA  
1084 C C   . LYS B 67  ? 0.2768 0.2239 0.2292 -0.0407 -0.0290 0.0046  35  LYS B C   
1085 O O   . LYS B 67  ? 0.2637 0.2288 0.2418 -0.0558 0.0080  -0.0049 35  LYS B O   
1086 C CB  . LYS B 67  ? 0.3358 0.2583 0.2318 -0.0140 -0.0913 0.0155  35  LYS B CB  
1087 C CG  . LYS B 67  ? 0.4376 0.2912 0.2725 0.0155  -0.0911 0.0057  35  LYS B CG  
1088 C CD  . LYS B 67  ? 0.5289 0.3372 0.3024 0.0374  -0.1059 0.0050  35  LYS B CD  
1089 C CE  . LYS B 67  ? 0.5946 0.3718 0.3344 0.0539  -0.1135 0.0151  35  LYS B CE  
1090 N NZ  . LYS B 67  ? 0.6422 0.3920 0.3613 0.0518  -0.1144 0.0232  35  LYS B NZ  
1091 N N   . ALA B 68  ? 0.3311 0.2209 0.2500 -0.0162 0.0005  0.0002  36  ALA B N   
1092 C CA  . ALA B 68  ? 0.3729 0.2328 0.3041 -0.0322 0.0248  -0.0039 36  ALA B CA  
1093 C C   . ALA B 68  ? 0.4207 0.2560 0.3451 -0.0732 0.0258  -0.0247 36  ALA B C   
1094 O O   . ALA B 68  ? 0.4096 0.2630 0.3311 -0.0743 -0.0040 -0.0228 36  ALA B O   
1095 C CB  . ALA B 68  ? 0.3920 0.2407 0.3261 -0.0220 0.0278  0.0012  36  ALA B CB  
1096 N N   . ALA B 69  ? 0.4917 0.2922 0.3975 -0.0870 0.0526  -0.0568 37  ALA B N   
1097 C CA  . ALA B 69  ? 0.5604 0.3271 0.4469 -0.1044 0.0549  -0.0952 37  ALA B CA  
1098 C C   . ALA B 69  ? 0.6036 0.3544 0.4993 -0.1051 0.0429  -0.1204 37  ALA B C   
1099 O O   . ALA B 69  ? 0.6207 0.3725 0.5073 -0.1047 0.0469  -0.1163 37  ALA B O   
1100 C CB  . ALA B 69  ? 0.5722 0.3352 0.4526 -0.1185 0.0664  -0.0899 37  ALA B CB  
1101 N N   . ASP B 70  ? 0.5990 0.3625 0.5389 -0.1030 0.0248  -0.1373 38  ASP B N   
1102 C CA  . ASP B 70  ? 0.6279 0.3813 0.5827 -0.0684 0.0001  -0.1447 38  ASP B CA  
1103 C C   . ASP B 70  ? 0.6432 0.3997 0.5642 -0.0738 -0.0072 -0.1426 38  ASP B C   
1104 O O   . ASP B 70  ? 0.6320 0.4035 0.5647 -0.0895 -0.0028 -0.1408 38  ASP B O   
1105 C CB  . ASP B 70  ? 0.6423 0.3866 0.6413 -0.0271 -0.0172 -0.1503 38  ASP B CB  
1106 C CG  . ASP B 70  ? 0.6520 0.3842 0.6914 0.0017  -0.0344 -0.1572 38  ASP B CG  
1107 O OD1 . ASP B 70  ? 0.6601 0.3813 0.7073 0.0215  -0.0350 -0.1706 38  ASP B OD1 
1108 O OD2 . ASP B 70  ? 0.6640 0.3856 0.7134 0.0129  -0.0403 -0.1491 38  ASP B OD2 
1109 N N   . ASP B 71  ? 0.6723 0.4086 0.5389 -0.0589 -0.0236 -0.1440 39  ASP B N   
1110 C CA  . ASP B 71  ? 0.7081 0.4253 0.5235 -0.0365 -0.0292 -0.1352 39  ASP B CA  
1111 C C   . ASP B 71  ? 0.6722 0.3934 0.4739 0.0040  -0.0058 -0.1159 39  ASP B C   
1112 O O   . ASP B 71  ? 0.6860 0.4066 0.4863 0.0026  -0.0090 -0.1009 39  ASP B O   
1113 C CB  . ASP B 71  ? 0.7808 0.4682 0.5582 -0.0491 -0.0459 -0.1416 39  ASP B CB  
1114 C CG  . ASP B 71  ? 0.8462 0.5037 0.5903 -0.0637 -0.0656 -0.1461 39  ASP B CG  
1115 O OD1 . ASP B 71  ? 0.8628 0.5145 0.6029 -0.0709 -0.0738 -0.1513 39  ASP B OD1 
1116 O OD2 . ASP B 71  ? 0.8767 0.5145 0.6065 -0.0677 -0.0683 -0.1390 39  ASP B OD2 
1117 N N   . THR B 72  ? 0.6076 0.3458 0.4085 0.0490  0.0184  -0.1082 40  THR B N   
1118 C CA  . THR B 72  ? 0.5719 0.3155 0.3557 0.0687  0.0398  -0.0804 40  THR B CA  
1119 C C   . THR B 72  ? 0.4729 0.2823 0.2951 0.0675  0.0449  -0.0485 40  THR B C   
1120 O O   . THR B 72  ? 0.4121 0.2657 0.2833 0.0398  0.0648  -0.0531 40  THR B O   
1121 C CB  . THR B 72  ? 0.6241 0.3180 0.3674 0.0873  0.0354  -0.0793 40  THR B CB  
1122 O OG1 . THR B 72  ? 0.6379 0.3173 0.3804 0.1007  0.0338  -0.0581 40  THR B OG1 
1123 C CG2 . THR B 72  ? 0.6505 0.3250 0.3674 0.0767  0.0389  -0.0934 40  THR B CG2 
1124 N N   . TRP B 73  ? 0.4226 0.2820 0.2628 0.0848  0.0407  -0.0242 41  TRP B N   
1125 C CA  . TRP B 73  ? 0.3857 0.2898 0.2504 0.0877  0.0047  -0.0112 41  TRP B CA  
1126 C C   . TRP B 73  ? 0.3953 0.2987 0.2703 0.1062  -0.0320 0.0034  41  TRP B C   
1127 O O   . TRP B 73  ? 0.4147 0.3533 0.3108 0.1151  -0.0203 0.0232  41  TRP B O   
1128 C CB  . TRP B 73  ? 0.3511 0.2900 0.2352 0.0699  0.0155  0.0022  41  TRP B CB  
1129 C CG  . TRP B 73  ? 0.3439 0.2848 0.2241 0.0460  0.0253  0.0148  41  TRP B CG  
1130 C CD1 . TRP B 73  ? 0.3825 0.2963 0.2364 0.0466  0.0372  0.0146  41  TRP B CD1 
1131 C CD2 . TRP B 73  ? 0.2946 0.2734 0.2181 0.0309  0.0308  0.0211  41  TRP B CD2 
1132 N NE1 . TRP B 73  ? 0.3824 0.3008 0.2440 0.0489  0.0283  0.0197  41  TRP B NE1 
1133 C CE2 . TRP B 73  ? 0.3296 0.2853 0.2353 0.0466  0.0339  0.0286  41  TRP B CE2 
1134 C CE3 . TRP B 73  ? 0.2495 0.2512 0.2272 0.0079  0.0268  0.0233  41  TRP B CE3 
1135 C CZ2 . TRP B 73  ? 0.3474 0.2784 0.2494 0.0296  0.0110  0.0486  41  TRP B CZ2 
1136 C CZ3 . TRP B 73  ? 0.2594 0.2431 0.2328 -0.0167 0.0093  0.0561  41  TRP B CZ3 
1137 C CH2 . TRP B 73  ? 0.2823 0.2594 0.2464 0.0067  0.0203  0.0606  41  TRP B CH2 
1138 N N   . GLU B 74  ? 0.3883 0.2624 0.2415 0.0731  -0.0764 -0.0068 42  GLU B N   
1139 C CA  . GLU B 74  ? 0.4251 0.2536 0.2561 0.0800  -0.0957 0.0187  42  GLU B CA  
1140 C C   . GLU B 74  ? 0.3045 0.2091 0.2432 0.0595  -0.0742 0.0230  42  GLU B C   
1141 O O   . GLU B 74  ? 0.2608 0.1916 0.2571 0.0615  -0.0688 0.0409  42  GLU B O   
1142 C CB  . GLU B 74  ? 0.6264 0.3117 0.3023 0.0767  -0.0757 0.0314  42  GLU B CB  
1143 C CG  . GLU B 74  ? 0.8131 0.3733 0.3675 0.0935  -0.0349 0.0482  42  GLU B CG  
1144 C CD  . GLU B 74  ? 0.9617 0.4254 0.4196 0.1112  0.0049  0.0614  42  GLU B CD  
1145 O OE1 . GLU B 74  ? 1.0024 0.4458 0.4437 0.1182  0.0156  0.0688  42  GLU B OE1 
1146 O OE2 . GLU B 74  ? 1.0253 0.4457 0.4355 0.1179  0.0171  0.0615  42  GLU B OE2 
1147 N N   . PRO B 75  ? 0.2799 0.1891 0.2388 0.0536  -0.0692 0.0072  43  PRO B N   
1148 C CA  . PRO B 75  ? 0.2364 0.1985 0.2295 0.0365  -0.0799 0.0133  43  PRO B CA  
1149 C C   . PRO B 75  ? 0.2251 0.1777 0.2039 0.0122  -0.0468 0.0339  43  PRO B C   
1150 O O   . PRO B 75  ? 0.2932 0.1694 0.2220 0.0014  -0.0159 0.0345  43  PRO B O   
1151 C CB  . PRO B 75  ? 0.2601 0.2064 0.2599 0.0594  -0.0565 0.0128  43  PRO B CB  
1152 C CG  . PRO B 75  ? 0.3083 0.2295 0.2780 0.0349  -0.0562 -0.0148 43  PRO B CG  
1153 C CD  . PRO B 75  ? 0.2945 0.2149 0.2639 0.0613  -0.0816 -0.0073 43  PRO B CD  
1154 N N   . PHE B 76  ? 0.2009 0.1815 0.1864 0.0169  -0.0418 0.0242  44  PHE B N   
1155 C CA  . PHE B 76  ? 0.1885 0.1877 0.1638 -0.0033 -0.0118 0.0439  44  PHE B CA  
1156 C C   . PHE B 76  ? 0.1715 0.1960 0.1674 -0.0001 -0.0152 0.0602  44  PHE B C   
1157 O O   . PHE B 76  ? 0.2164 0.2063 0.1675 -0.0098 -0.0086 0.0602  44  PHE B O   
1158 C CB  . PHE B 76  ? 0.1766 0.2142 0.1723 -0.0055 -0.0172 0.0411  44  PHE B CB  
1159 C CG  . PHE B 76  ? 0.1724 0.2405 0.1517 -0.0029 -0.0090 0.0507  44  PHE B CG  
1160 C CD1 . PHE B 76  ? 0.2080 0.2659 0.1673 0.0016  -0.0081 0.0518  44  PHE B CD1 
1161 C CD2 . PHE B 76  ? 0.1774 0.2578 0.1436 0.0109  -0.0027 0.0244  44  PHE B CD2 
1162 C CE1 . PHE B 76  ? 0.2333 0.2883 0.1617 -0.0108 0.0014  0.0474  44  PHE B CE1 
1163 C CE2 . PHE B 76  ? 0.2135 0.2718 0.1453 0.0202  -0.0057 0.0330  44  PHE B CE2 
1164 C CZ  . PHE B 76  ? 0.2385 0.2808 0.1412 0.0155  -0.0027 0.0395  44  PHE B CZ  
1165 N N   . ALA B 77  ? 0.1542 0.1797 0.1633 -0.0016 -0.0124 0.0519  45  ALA B N   
1166 C CA  . ALA B 77  ? 0.1648 0.1857 0.1565 -0.0102 -0.0050 0.0490  45  ALA B CA  
1167 C C   . ALA B 77  ? 0.1587 0.1842 0.1449 0.0002  -0.0210 0.0577  45  ALA B C   
1168 O O   . ALA B 77  ? 0.1819 0.2294 0.1207 -0.0106 -0.0208 0.0307  45  ALA B O   
1169 C CB  . ALA B 77  ? 0.2128 0.1991 0.1663 -0.0141 0.0123  0.0398  45  ALA B CB  
1170 N N   . SER B 78  ? 0.1579 0.1733 0.1601 -0.0153 -0.0308 0.0514  46  SER B N   
1171 C CA  . SER B 78  ? 0.1685 0.1749 0.1769 0.0002  -0.0238 0.0457  46  SER B CA  
1172 C C   . SER B 78  ? 0.1762 0.1584 0.1418 -0.0066 -0.0326 0.0507  46  SER B C   
1173 O O   . SER B 78  ? 0.2324 0.1788 0.1375 -0.0166 -0.0184 0.0462  46  SER B O   
1174 C CB  . SER B 78  ? 0.2626 0.2139 0.2666 0.0116  -0.0211 0.0094  46  SER B CB  
1175 O OG  . SER B 78  ? 0.2564 0.2333 0.3046 0.0289  -0.0355 0.0139  46  SER B OG  
1176 N N   . GLY B 79  ? 0.1947 0.1510 0.1263 -0.0188 -0.0189 0.0183  47  GLY B N   
1177 C CA  . GLY B 79  ? 0.2153 0.1662 0.1290 -0.0287 -0.0373 0.0217  47  GLY B CA  
1178 C C   . GLY B 79  ? 0.2040 0.1549 0.1232 -0.0070 -0.0305 0.0287  47  GLY B C   
1179 O O   . GLY B 79  ? 0.2280 0.1597 0.1137 -0.0108 -0.0184 0.0219  47  GLY B O   
1180 N N   . LYS B 80  ? 0.1996 0.1540 0.1445 0.0048  -0.0200 0.0344  48  LYS B N   
1181 C CA  . LYS B 80  ? 0.2007 0.1689 0.1948 -0.0004 -0.0201 0.0307  48  LYS B CA  
1182 C C   . LYS B 80  ? 0.2082 0.1709 0.1677 0.0127  -0.0248 0.0154  48  LYS B C   
1183 O O   . LYS B 80  ? 0.2284 0.1927 0.1554 0.0109  -0.0278 0.0077  48  LYS B O   
1184 C CB  . LYS B 80  ? 0.2105 0.2166 0.2827 0.0043  -0.0387 0.0345  48  LYS B CB  
1185 C CG  . LYS B 80  ? 0.2312 0.2777 0.3658 0.0178  -0.0710 0.0463  48  LYS B CG  
1186 C CD  . LYS B 80  ? 0.2269 0.3261 0.4359 0.0199  -0.1078 0.0535  48  LYS B CD  
1187 C CE  . LYS B 80  ? 0.2847 0.3671 0.4871 0.0157  -0.1155 0.0590  48  LYS B CE  
1188 N NZ  . LYS B 80  ? 0.3523 0.3842 0.5232 0.0064  -0.0901 0.0539  48  LYS B NZ  
1189 N N   . THR B 81  ? 0.1944 0.1478 0.1611 -0.0005 -0.0166 0.0142  49  THR B N   
1190 C CA  . THR B 81  ? 0.2028 0.1522 0.1493 0.0101  -0.0435 0.0030  49  THR B CA  
1191 C C   . THR B 81  ? 0.1746 0.1661 0.1514 0.0026  -0.0236 0.0109  49  THR B C   
1192 O O   . THR B 81  ? 0.1993 0.1757 0.1403 -0.0045 -0.0400 0.0135  49  THR B O   
1193 C CB  . THR B 81  ? 0.1763 0.1575 0.1293 -0.0026 -0.0475 0.0068  49  THR B CB  
1194 O OG1 . THR B 81  ? 0.1802 0.1606 0.1399 -0.0028 -0.0020 0.0090  49  THR B OG1 
1195 C CG2 . THR B 81  ? 0.2053 0.1640 0.1287 -0.0110 -0.0377 -0.0139 49  THR B CG2 
1196 N N   . SER B 82  ? 0.2177 0.1823 0.1425 -0.0113 -0.0225 -0.0099 50  SER B N   
1197 C CA  . SER B 82  ? 0.2399 0.1888 0.1515 -0.0227 -0.0261 -0.0165 50  SER B CA  
1198 C C   . SER B 82  ? 0.2471 0.1966 0.1630 -0.0202 -0.0280 -0.0096 50  SER B C   
1199 O O   . SER B 82  ? 0.2358 0.1934 0.1636 -0.0168 -0.0307 -0.0096 50  SER B O   
1200 C CB  . SER B 82  ? 0.2641 0.2055 0.1705 0.0067  -0.0253 -0.0282 50  SER B CB  
1201 O OG  . SER B 82  ? 0.2763 0.2254 0.2095 0.0083  -0.0148 -0.0318 50  SER B OG  
1202 N N   . GLU B 83  ? 0.2786 0.2119 0.1925 -0.0421 -0.0426 0.0067  51  GLU B N   
1203 C CA  . GLU B 83  ? 0.3271 0.2400 0.2316 -0.0527 -0.0832 -0.0038 51  GLU B CA  
1204 C C   . GLU B 83  ? 0.2949 0.2270 0.1993 -0.0377 -0.0583 -0.0250 51  GLU B C   
1205 O O   . GLU B 83  ? 0.2925 0.2062 0.2290 -0.0295 -0.0253 -0.0272 51  GLU B O   
1206 C CB  . GLU B 83  ? 0.4749 0.3036 0.3193 -0.0797 -0.1476 0.0114  51  GLU B CB  
1207 C CG  . GLU B 83  ? 0.6598 0.3937 0.4205 -0.0978 -0.1760 0.0241  51  GLU B CG  
1208 C CD  . GLU B 83  ? 0.8201 0.4640 0.5163 -0.1012 -0.1875 0.0426  51  GLU B CD  
1209 O OE1 . GLU B 83  ? 0.8754 0.4841 0.5497 -0.1092 -0.1922 0.0413  51  GLU B OE1 
1210 O OE2 . GLU B 83  ? 0.8851 0.4946 0.5431 -0.0917 -0.1857 0.0499  51  GLU B OE2 
1211 N N   . SER B 84  ? 0.2773 0.2190 0.1542 -0.0156 -0.0459 -0.0332 52  SER B N   
1212 C CA  . SER B 84  ? 0.2968 0.2163 0.1564 -0.0049 -0.0254 -0.0292 52  SER B CA  
1213 C C   . SER B 84  ? 0.2682 0.1901 0.1390 -0.0230 -0.0250 -0.0081 52  SER B C   
1214 O O   . SER B 84  ? 0.2745 0.1821 0.1522 -0.0180 0.0051  -0.0066 52  SER B O   
1215 C CB  . SER B 84  ? 0.3809 0.2524 0.1847 0.0157  -0.0205 -0.0195 52  SER B CB  
1216 O OG  . SER B 84  ? 0.4372 0.2811 0.2193 0.0342  -0.0071 0.0104  52  SER B OG  
1217 N N   . GLY B 85  ? 0.2417 0.1686 0.1074 -0.0325 -0.0332 -0.0055 53  GLY B N   
1218 C CA  . GLY B 85  ? 0.2278 0.1875 0.1071 -0.0169 -0.0273 0.0049  53  GLY B CA  
1219 C C   . GLY B 85  ? 0.2148 0.1791 0.0990 -0.0194 -0.0054 0.0125  53  GLY B C   
1220 O O   . GLY B 85  ? 0.1977 0.2056 0.1100 -0.0001 -0.0028 0.0187  53  GLY B O   
1221 N N   . GLU B 86  ? 0.2146 0.1941 0.1132 -0.0414 -0.0105 0.0167  54  GLU B N   
1222 C CA  . GLU B 86  ? 0.2138 0.1735 0.1344 -0.0240 -0.0205 0.0198  54  GLU B CA  
1223 C C   . GLU B 86  ? 0.1903 0.1732 0.1400 -0.0259 -0.0152 0.0257  54  GLU B C   
1224 O O   . GLU B 86  ? 0.1906 0.1894 0.1453 -0.0254 -0.0383 0.0177  54  GLU B O   
1225 C CB  . GLU B 86  ? 0.2458 0.1932 0.1610 0.0046  0.0045  0.0054  54  GLU B CB  
1226 C CG  . GLU B 86  ? 0.3175 0.2079 0.2038 0.0140  0.0152  0.0056  54  GLU B CG  
1227 C CD  . GLU B 86  ? 0.4054 0.2439 0.2592 0.0303  0.0268  -0.0091 54  GLU B CD  
1228 O OE1 . GLU B 86  ? 0.4471 0.2654 0.2811 0.0388  0.0453  -0.0282 54  GLU B OE1 
1229 O OE2 . GLU B 86  ? 0.4278 0.2706 0.2870 0.0599  0.0282  -0.0108 54  GLU B OE2 
1230 N N   . LEU B 87  ? 0.1723 0.1739 0.1322 -0.0237 -0.0252 0.0309  55  LEU B N   
1231 C CA  . LEU B 87  ? 0.1757 0.1728 0.1329 -0.0237 -0.0046 0.0279  55  LEU B CA  
1232 C C   . LEU B 87  ? 0.1729 0.1890 0.1608 -0.0097 -0.0209 0.0338  55  LEU B C   
1233 O O   . LEU B 87  ? 0.1769 0.1849 0.1724 -0.0118 -0.0002 0.0342  55  LEU B O   
1234 C CB  . LEU B 87  ? 0.1989 0.1592 0.1252 -0.0232 -0.0064 0.0100  55  LEU B CB  
1235 C CG  . LEU B 87  ? 0.1980 0.1659 0.1286 -0.0037 -0.0173 0.0042  55  LEU B CG  
1236 C CD1 . LEU B 87  ? 0.2094 0.1679 0.1457 0.0002  -0.0186 0.0114  55  LEU B CD1 
1237 C CD2 . LEU B 87  ? 0.2050 0.1818 0.1389 -0.0090 -0.0082 -0.0096 55  LEU B CD2 
1238 N N   . HIS B 88  ? 0.2381 0.2099 0.1632 -0.0019 0.0201  0.0527  56  HIS B N   
1239 C CA  . HIS B 88  ? 0.3195 0.2185 0.1830 -0.0013 0.0556  0.0227  56  HIS B CA  
1240 C C   . HIS B 88  ? 0.3328 0.2212 0.1887 -0.0187 0.0287  0.0236  56  HIS B C   
1241 O O   . HIS B 88  ? 0.3411 0.2431 0.1940 -0.0024 0.0127  0.0451  56  HIS B O   
1242 C CB  . HIS B 88  ? 0.3680 0.2338 0.2013 0.0077  0.0739  0.0025  56  HIS B CB  
1243 C CG  . HIS B 88  ? 0.3884 0.2495 0.2406 0.0095  0.0791  -0.0036 56  HIS B CG  
1244 N ND1 . HIS B 88  ? 0.4066 0.2642 0.2706 0.0122  0.0721  -0.0032 56  HIS B ND1 
1245 C CD2 . HIS B 88  ? 0.4147 0.2596 0.2602 0.0125  0.0803  0.0017  56  HIS B CD2 
1246 C CE1 . HIS B 88  ? 0.4223 0.2628 0.2717 0.0035  0.0685  -0.0014 56  HIS B CE1 
1247 N NE2 . HIS B 88  ? 0.4403 0.2663 0.2705 0.0136  0.0656  -0.0121 56  HIS B NE2 
1248 N N   . GLY B 89  ? 0.3038 0.2156 0.1998 -0.0333 0.0297  0.0302  57  GLY B N   
1249 C CA  . GLY B 89  ? 0.3133 0.2096 0.2067 -0.0192 -0.0076 0.0401  57  GLY B CA  
1250 C C   . GLY B 89  ? 0.2776 0.2212 0.2057 -0.0122 -0.0389 0.0382  57  GLY B C   
1251 O O   . GLY B 89  ? 0.3025 0.2451 0.2314 -0.0142 -0.0352 0.0437  57  GLY B O   
1252 N N   . LEU B 90  ? 0.2357 0.2237 0.2026 -0.0321 -0.0347 0.0258  58  LEU B N   
1253 C CA  . LEU B 90  ? 0.2109 0.2184 0.1998 -0.0366 0.0050  0.0333  58  LEU B CA  
1254 C C   . LEU B 90  ? 0.1932 0.2186 0.1910 -0.0313 -0.0057 0.0277  58  LEU B C   
1255 O O   . LEU B 90  ? 0.2308 0.2206 0.1984 -0.0225 -0.0011 0.0276  58  LEU B O   
1256 C CB  . LEU B 90  ? 0.1950 0.2132 0.2030 -0.0051 -0.0011 0.0470  58  LEU B CB  
1257 C CG  . LEU B 90  ? 0.2029 0.2056 0.2117 0.0029  0.0197  0.0657  58  LEU B CG  
1258 C CD1 . LEU B 90  ? 0.2337 0.2111 0.2136 0.0043  0.0088  0.0733  58  LEU B CD1 
1259 C CD2 . LEU B 90  ? 0.1831 0.2270 0.2256 0.0088  0.0461  0.0627  58  LEU B CD2 
1260 N N   . THR B 91  ? 0.1847 0.2311 0.1781 -0.0533 0.0029  0.0296  59  THR B N   
1261 C CA  . THR B 91  ? 0.2033 0.2335 0.1849 -0.0499 0.0077  0.0327  59  THR B CA  
1262 C C   . THR B 91  ? 0.2083 0.2604 0.1974 -0.0548 0.0214  0.0204  59  THR B C   
1263 O O   . THR B 91  ? 0.2578 0.2661 0.2048 -0.0464 0.0370  0.0158  59  THR B O   
1264 C CB  . THR B 91  ? 0.1969 0.2281 0.1748 -0.0328 -0.0169 0.0383  59  THR B CB  
1265 O OG1 . THR B 91  ? 0.2301 0.2467 0.1633 -0.0532 -0.0158 0.0404  59  THR B OG1 
1266 C CG2 . THR B 91  ? 0.2046 0.2325 0.1819 -0.0172 -0.0146 0.0524  59  THR B CG2 
1267 N N   . THR B 92  ? 0.2145 0.2635 0.2067 -0.0579 0.0224  0.0267  60  THR B N   
1268 C CA  . THR B 92  ? 0.2464 0.2810 0.2085 -0.0578 -0.0083 0.0579  60  THR B CA  
1269 C C   . THR B 92  ? 0.2368 0.2686 0.2095 -0.0758 0.0040  0.0449  60  THR B C   
1270 O O   . THR B 92  ? 0.2317 0.2699 0.1912 -0.0568 0.0016  0.0262  60  THR B O   
1271 C CB  . THR B 92  ? 0.2844 0.3059 0.2238 -0.0681 -0.0348 0.0830  60  THR B CB  
1272 O OG1 . THR B 92  ? 0.3049 0.3154 0.2467 -0.0800 -0.0363 0.1047  60  THR B OG1 
1273 C CG2 . THR B 92  ? 0.3117 0.3242 0.2403 -0.0713 -0.0385 0.0759  60  THR B CG2 
1274 N N   . GLU B 93  ? 0.2634 0.2580 0.2383 -0.0590 0.0382  0.0506  61  GLU B N   
1275 C CA  . GLU B 93  ? 0.3076 0.2726 0.2922 -0.0594 0.0968  0.0388  61  GLU B CA  
1276 C C   . GLU B 93  ? 0.2557 0.2511 0.2548 -0.0664 0.0795  0.0614  61  GLU B C   
1277 O O   . GLU B 93  ? 0.2341 0.2341 0.2482 -0.0314 0.0307  0.0433  61  GLU B O   
1278 C CB  . GLU B 93  ? 0.5012 0.3411 0.3901 -0.0233 0.1636  0.0368  61  GLU B CB  
1279 C CG  . GLU B 93  ? 0.6859 0.4293 0.5042 0.0109  0.2004  0.0352  61  GLU B CG  
1280 C CD  . GLU B 93  ? 0.8327 0.5010 0.5930 0.0374  0.2451  0.0423  61  GLU B CD  
1281 O OE1 . GLU B 93  ? 0.8682 0.5162 0.6099 0.0434  0.2707  0.0479  61  GLU B OE1 
1282 O OE2 . GLU B 93  ? 0.8939 0.5284 0.6270 0.0428  0.2596  0.0428  61  GLU B OE2 
1283 N N   . GLU B 94  ? 0.2471 0.2697 0.2415 -0.0480 0.0540  0.0719  62  GLU B N   
1284 C CA  . GLU B 94  ? 0.2876 0.3041 0.2661 -0.0311 0.0662  0.0956  62  GLU B CA  
1285 C C   . GLU B 94  ? 0.1999 0.2778 0.2417 -0.0492 0.0557  0.0957  62  GLU B C   
1286 O O   . GLU B 94  ? 0.2230 0.2790 0.2339 -0.0499 0.0351  0.0431  62  GLU B O   
1287 C CB  . GLU B 94  ? 0.4605 0.3913 0.3476 -0.0132 0.1256  0.1148  62  GLU B CB  
1288 C CG  . GLU B 94  ? 0.6357 0.4937 0.4523 0.0409  0.1332  0.1209  62  GLU B CG  
1289 C CD  . GLU B 94  ? 0.7777 0.5730 0.5496 0.0904  0.1410  0.1152  62  GLU B CD  
1290 O OE1 . GLU B 94  ? 0.8248 0.5986 0.5852 0.1068  0.1464  0.1123  62  GLU B OE1 
1291 O OE2 . GLU B 94  ? 0.8282 0.6018 0.5674 0.1072  0.1425  0.1137  62  GLU B OE2 
1292 N N   . GLU B 95  ? 0.1626 0.2771 0.2524 -0.0273 0.0317  0.1098  63  GLU B N   
1293 C CA  . GLU B 95  ? 0.1511 0.3037 0.3010 -0.0132 0.0475  0.0906  63  GLU B CA  
1294 C C   . GLU B 95  ? 0.1969 0.2679 0.2351 -0.0356 0.0310  0.0740  63  GLU B C   
1295 O O   . GLU B 95  ? 0.2838 0.2610 0.2350 -0.0026 0.0747  0.0730  63  GLU B O   
1296 C CB  . GLU B 95  ? 0.1644 0.3682 0.4198 0.0152  0.0379  0.0944  63  GLU B CB  
1297 C CG  . GLU B 95  ? 0.2622 0.4326 0.5498 0.0542  0.0032  0.0934  63  GLU B CG  
1298 C CD  . GLU B 95  ? 0.3401 0.4776 0.6515 0.0797  -0.0166 0.0917  63  GLU B CD  
1299 O OE1 . GLU B 95  ? 0.3620 0.4757 0.6794 0.0717  -0.0349 0.0898  63  GLU B OE1 
1300 O OE2 . GLU B 95  ? 0.3909 0.4944 0.6977 0.0980  -0.0342 0.0963  63  GLU B OE2 
1301 N N   . PHE B 96  ? 0.1729 0.2497 0.1925 -0.0330 0.0031  0.0598  64  PHE B N   
1302 C CA  . PHE B 96  ? 0.1974 0.2392 0.1608 -0.0265 -0.0064 0.0482  64  PHE B CA  
1303 C C   . PHE B 96  ? 0.1837 0.2313 0.1671 -0.0364 -0.0007 0.0464  64  PHE B C   
1304 O O   . PHE B 96  ? 0.2385 0.2437 0.1990 -0.0189 -0.0099 0.0146  64  PHE B O   
1305 C CB  . PHE B 96  ? 0.2276 0.2327 0.1604 -0.0254 0.0119  0.0298  64  PHE B CB  
1306 C CG  . PHE B 96  ? 0.1812 0.2320 0.1671 -0.0313 0.0001  0.0241  64  PHE B CG  
1307 C CD1 . PHE B 96  ? 0.1793 0.2337 0.1776 -0.0296 -0.0107 0.0270  64  PHE B CD1 
1308 C CD2 . PHE B 96  ? 0.2341 0.2303 0.1942 -0.0104 0.0072  0.0042  64  PHE B CD2 
1309 C CE1 . PHE B 96  ? 0.1966 0.2215 0.1980 -0.0463 -0.0197 0.0283  64  PHE B CE1 
1310 C CE2 . PHE B 96  ? 0.2768 0.2243 0.2060 -0.0206 0.0114  0.0231  64  PHE B CE2 
1311 C CZ  . PHE B 96  ? 0.2388 0.2316 0.1988 -0.0461 -0.0056 0.0239  64  PHE B CZ  
1312 N N   . VAL B 97  ? 0.1820 0.2379 0.1688 -0.0392 0.0058  0.0573  65  VAL B N   
1313 C CA  . VAL B 97  ? 0.1970 0.2290 0.1622 -0.0536 0.0070  0.0538  65  VAL B CA  
1314 C C   . VAL B 97  ? 0.1871 0.2223 0.1515 -0.0276 0.0169  0.0485  65  VAL B C   
1315 O O   . VAL B 97  ? 0.1867 0.2266 0.1509 -0.0245 0.0325  0.0457  65  VAL B O   
1316 C CB  . VAL B 97  ? 0.2658 0.2434 0.1980 -0.0515 -0.0329 0.0485  65  VAL B CB  
1317 C CG1 . VAL B 97  ? 0.2681 0.2579 0.1889 -0.0879 -0.0508 0.0701  65  VAL B CG1 
1318 C CG2 . VAL B 97  ? 0.3134 0.2739 0.2281 -0.0267 -0.0345 0.0380  65  VAL B CG2 
1319 N N   . GLU B 98  ? 0.2085 0.2323 0.1670 -0.0366 0.0041  0.0387  66  GLU B N   
1320 C CA  . GLU B 98  ? 0.2233 0.2558 0.2016 -0.0360 0.0007  0.0470  66  GLU B CA  
1321 C C   . GLU B 98  ? 0.2261 0.2289 0.1904 -0.0255 0.0241  0.0620  66  GLU B C   
1322 O O   . GLU B 98  ? 0.3068 0.2273 0.2145 0.0074  0.0618  0.0658  66  GLU B O   
1323 C CB  . GLU B 98  ? 0.2557 0.2773 0.2387 -0.0550 -0.0075 0.0524  66  GLU B CB  
1324 C CG  . GLU B 98  ? 0.3793 0.3232 0.3084 -0.0730 -0.0087 0.0489  66  GLU B CG  
1325 C CD  . GLU B 98  ? 0.5219 0.3640 0.4049 -0.0914 0.0037  0.0442  66  GLU B CD  
1326 O OE1 . GLU B 98  ? 0.5984 0.3895 0.4122 -0.0870 -0.0042 0.0358  66  GLU B OE1 
1327 O OE2 . GLU B 98  ? 0.5631 0.3706 0.4516 -0.1031 0.0044  0.0263  66  GLU B OE2 
1328 N N   . GLY B 99  ? 0.2159 0.2334 0.1811 -0.0447 0.0505  0.0389  67  GLY B N   
1329 C CA  . GLY B 99  ? 0.2149 0.2282 0.1628 -0.0425 0.0388  0.0373  67  GLY B CA  
1330 C C   . GLY B 99  ? 0.1685 0.2026 0.1376 -0.0451 0.0123  0.0225  67  GLY B C   
1331 O O   . GLY B 99  ? 0.2056 0.2045 0.1254 -0.0094 0.0135  0.0216  67  GLY B O   
1332 N N   . ILE B 100 ? 0.2042 0.2044 0.1283 -0.0379 0.0185  0.0148  68  ILE B N   
1333 C CA  . ILE B 100 ? 0.2036 0.1966 0.1170 -0.0414 0.0060  0.0251  68  ILE B CA  
1334 C C   . ILE B 100 ? 0.1712 0.1660 0.1321 -0.0165 -0.0092 0.0225  68  ILE B C   
1335 O O   . ILE B 100 ? 0.2167 0.1648 0.1627 -0.0141 -0.0168 0.0268  68  ILE B O   
1336 C CB  . ILE B 100 ? 0.2131 0.2202 0.1141 -0.0364 -0.0063 0.0165  68  ILE B CB  
1337 C CG1 . ILE B 100 ? 0.2197 0.2585 0.1383 -0.0227 -0.0276 -0.0161 68  ILE B CG1 
1338 C CG2 . ILE B 100 ? 0.2187 0.2034 0.1172 -0.0410 -0.0020 0.0269  68  ILE B CG2 
1339 C CD1 . ILE B 100 ? 0.2752 0.2840 0.1594 -0.0113 -0.0485 -0.0219 68  ILE B CD1 
1340 N N   . TYR B 101 ? 0.1708 0.1643 0.1120 -0.0288 -0.0110 0.0227  69  TYR B N   
1341 C CA  . TYR B 101 ? 0.1406 0.1651 0.1180 -0.0272 -0.0011 0.0101  69  TYR B CA  
1342 C C   . TYR B 101 ? 0.1449 0.1728 0.1268 -0.0164 -0.0064 0.0241  69  TYR B C   
1343 O O   . TYR B 101 ? 0.1593 0.1907 0.1254 0.0006  0.0032  0.0465  69  TYR B O   
1344 C CB  . TYR B 101 ? 0.1661 0.1756 0.1221 -0.0194 -0.0027 0.0065  69  TYR B CB  
1345 C CG  . TYR B 101 ? 0.1405 0.1731 0.1149 -0.0223 -0.0065 0.0297  69  TYR B CG  
1346 C CD1 . TYR B 101 ? 0.1649 0.1905 0.1135 -0.0164 0.0004  0.0153  69  TYR B CD1 
1347 C CD2 . TYR B 101 ? 0.1662 0.1896 0.1118 -0.0060 -0.0050 0.0336  69  TYR B CD2 
1348 C CE1 . TYR B 101 ? 0.1721 0.1975 0.1183 -0.0090 0.0291  0.0240  69  TYR B CE1 
1349 C CE2 . TYR B 101 ? 0.1626 0.2030 0.1212 -0.0125 0.0266  0.0291  69  TYR B CE2 
1350 C CZ  . TYR B 101 ? 0.1668 0.2036 0.1208 -0.0258 0.0252  0.0374  69  TYR B CZ  
1351 O OH  . TYR B 101 ? 0.1882 0.2176 0.1460 -0.0130 0.0342  0.0587  69  TYR B OH  
1352 N N   . LYS B 102 ? 0.1363 0.1737 0.1165 -0.0098 0.0016  0.0396  70  LYS B N   
1353 C CA  . LYS B 102 ? 0.1708 0.2067 0.1067 -0.0154 -0.0081 0.0403  70  LYS B CA  
1354 C C   . LYS B 102 ? 0.1461 0.2171 0.1157 -0.0072 -0.0212 0.0491  70  LYS B C   
1355 O O   . LYS B 102 ? 0.1709 0.2204 0.1475 -0.0100 -0.0318 0.0602  70  LYS B O   
1356 C CB  . LYS B 102 ? 0.2076 0.2375 0.1140 -0.0086 0.0138  0.0286  70  LYS B CB  
1357 C CG  . LYS B 102 ? 0.2101 0.2689 0.1406 -0.0063 0.0248  0.0216  70  LYS B CG  
1358 C CD  . LYS B 102 ? 0.2772 0.2906 0.1815 0.0142  0.0303  0.0130  70  LYS B CD  
1359 C CE  . LYS B 102 ? 0.3229 0.3123 0.2110 0.0228  0.0359  -0.0021 70  LYS B CE  
1360 N NZ  . LYS B 102 ? 0.3604 0.3295 0.2345 0.0120  0.0253  -0.0225 70  LYS B NZ  
1361 N N   . VAL B 103 ? 0.1410 0.2088 0.1321 -0.0280 -0.0212 0.0350  71  VAL B N   
1362 C CA  . VAL B 103 ? 0.1449 0.2165 0.1454 -0.0360 -0.0280 0.0496  71  VAL B CA  
1363 C C   . VAL B 103 ? 0.1410 0.2342 0.1422 -0.0153 -0.0333 0.0647  71  VAL B C   
1364 O O   . VAL B 103 ? 0.1507 0.2721 0.1563 -0.0055 -0.0040 0.0833  71  VAL B O   
1365 C CB  . VAL B 103 ? 0.1941 0.2119 0.1705 -0.0520 -0.0091 0.0382  71  VAL B CB  
1366 C CG1 . VAL B 103 ? 0.2364 0.2350 0.1857 -0.0312 -0.0250 0.0376  71  VAL B CG1 
1367 C CG2 . VAL B 103 ? 0.2125 0.2197 0.1907 -0.0012 0.0098  0.0215  71  VAL B CG2 
1368 N N   . GLU B 104 ? 0.1587 0.2066 0.1267 0.0031  -0.0202 0.0467  72  GLU B N   
1369 C CA  . GLU B 104 ? 0.1812 0.2020 0.1217 0.0091  -0.0245 0.0138  72  GLU B CA  
1370 C C   . GLU B 104 ? 0.1574 0.1988 0.0904 0.0128  -0.0243 0.0199  72  GLU B C   
1371 O O   . GLU B 104 ? 0.1724 0.1927 0.0886 0.0027  -0.0131 0.0033  72  GLU B O   
1372 C CB  . GLU B 104 ? 0.2655 0.2259 0.1741 0.0204  -0.0409 -0.0274 72  GLU B CB  
1373 C CG  . GLU B 104 ? 0.3623 0.2980 0.2238 0.0307  -0.0089 -0.0427 72  GLU B CG  
1374 C CD  . GLU B 104 ? 0.4416 0.3423 0.2512 0.0700  -0.0009 -0.0575 72  GLU B CD  
1375 O OE1 . GLU B 104 ? 0.4324 0.3511 0.2487 0.0811  -0.0114 -0.0681 72  GLU B OE1 
1376 O OE2 . GLU B 104 ? 0.4992 0.3661 0.2593 0.0821  0.0229  -0.0580 72  GLU B OE2 
1377 N N   . ILE B 105 ? 0.1531 0.1880 0.1028 -0.0088 -0.0048 0.0225  73  ILE B N   
1378 C CA  . ILE B 105 ? 0.1644 0.1741 0.0998 0.0033  0.0013  0.0136  73  ILE B CA  
1379 C C   . ILE B 105 ? 0.1688 0.1750 0.0942 -0.0066 0.0063  0.0323  73  ILE B C   
1380 O O   . ILE B 105 ? 0.1722 0.1884 0.0950 -0.0036 0.0101  0.0285  73  ILE B O   
1381 C CB  . ILE B 105 ? 0.1691 0.1877 0.1139 0.0072  0.0098  0.0069  73  ILE B CB  
1382 C CG1 . ILE B 105 ? 0.1893 0.1935 0.1268 0.0176  0.0483  0.0057  73  ILE B CG1 
1383 C CG2 . ILE B 105 ? 0.2140 0.1911 0.1248 -0.0118 0.0131  0.0047  73  ILE B CG2 
1384 C CD1 . ILE B 105 ? 0.2199 0.2056 0.1511 0.0456  0.0165  0.0147  73  ILE B CD1 
1385 N N   . ASP B 106 ? 0.1531 0.1659 0.1231 -0.0010 0.0070  0.0290  74  ASP B N   
1386 C CA  . ASP B 106 ? 0.1677 0.1775 0.1364 0.0088  -0.0001 0.0430  74  ASP B CA  
1387 C C   . ASP B 106 ? 0.1517 0.1926 0.1316 -0.0046 -0.0011 0.0137  74  ASP B C   
1388 O O   . ASP B 106 ? 0.1727 0.2050 0.1359 0.0175  -0.0018 0.0224  74  ASP B O   
1389 C CB  . ASP B 106 ? 0.1719 0.1741 0.1763 0.0233  0.0110  0.0370  74  ASP B CB  
1390 C CG  . ASP B 106 ? 0.1746 0.1856 0.2147 0.0175  0.0330  0.0397  74  ASP B CG  
1391 O OD1 . ASP B 106 ? 0.1874 0.1957 0.2226 0.0133  0.0344  0.0233  74  ASP B OD1 
1392 O OD2 . ASP B 106 ? 0.2053 0.2042 0.2561 0.0346  0.0352  0.0560  74  ASP B OD2 
1393 N N   . THR B 107 ? 0.1909 0.1697 0.1340 0.0192  0.0200  0.0116  75  THR B N   
1394 C CA  . THR B 107 ? 0.1716 0.1611 0.1332 0.0013  0.0210  0.0075  75  THR B CA  
1395 C C   . THR B 107 ? 0.1562 0.1642 0.1273 0.0117  0.0092  0.0152  75  THR B C   
1396 O O   . THR B 107 ? 0.1711 0.1863 0.1425 -0.0176 -0.0029 0.0136  75  THR B O   
1397 C CB  . THR B 107 ? 0.1694 0.1629 0.1429 -0.0018 0.0112  -0.0050 75  THR B CB  
1398 O OG1 . THR B 107 ? 0.1774 0.1541 0.1363 0.0048  0.0109  0.0239  75  THR B OG1 
1399 C CG2 . THR B 107 ? 0.1754 0.1682 0.1693 0.0006  0.0308  0.0069  75  THR B CG2 
1400 N N   . LYS B 108 ? 0.1626 0.1700 0.1249 0.0166  0.0105  0.0007  76  LYS B N   
1401 C CA  . LYS B 108 ? 0.1731 0.1825 0.1498 0.0167  0.0104  -0.0089 76  LYS B CA  
1402 C C   . LYS B 108 ? 0.1699 0.1816 0.1478 0.0154  0.0171  0.0009  76  LYS B C   
1403 O O   . LYS B 108 ? 0.1468 0.2033 0.1599 0.0118  0.0134  -0.0004 76  LYS B O   
1404 C CB  . LYS B 108 ? 0.1925 0.2109 0.1632 0.0135  0.0312  -0.0368 76  LYS B CB  
1405 C CG  . LYS B 108 ? 0.2149 0.2475 0.2103 0.0054  0.0569  -0.0420 76  LYS B CG  
1406 C CD  . LYS B 108 ? 0.2436 0.2948 0.2501 0.0221  0.0699  -0.0627 76  LYS B CD  
1407 C CE  . LYS B 108 ? 0.3342 0.3275 0.2875 0.0094  0.0549  -0.0710 76  LYS B CE  
1408 N NZ  . LYS B 108 ? 0.4025 0.3515 0.3143 0.0167  0.0368  -0.0749 76  LYS B NZ  
1409 N N   . SER B 109 ? 0.1565 0.1894 0.1454 0.0220  0.0021  0.0058  77  SER B N   
1410 C CA  . SER B 109 ? 0.1867 0.1892 0.1659 0.0208  -0.0189 0.0092  77  SER B CA  
1411 C C   . SER B 109 ? 0.1972 0.2041 0.1629 0.0097  -0.0181 -0.0107 77  SER B C   
1412 O O   . SER B 109 ? 0.1984 0.2180 0.1852 0.0041  -0.0337 -0.0062 77  SER B O   
1413 C CB  . SER B 109 ? 0.1857 0.1841 0.1949 0.0149  -0.0032 0.0083  77  SER B CB  
1414 O OG  . SER B 109 ? 0.2015 0.1968 0.2357 0.0310  0.0191  0.0083  77  SER B OG  
1415 N N   . TYR B 110 ? 0.1686 0.1874 0.1408 0.0142  0.0188  -0.0062 78  TYR B N   
1416 C CA  . TYR B 110 ? 0.1569 0.2048 0.1442 0.0112  -0.0021 -0.0106 78  TYR B CA  
1417 C C   . TYR B 110 ? 0.1426 0.2192 0.1609 -0.0057 -0.0092 -0.0159 78  TYR B C   
1418 O O   . TYR B 110 ? 0.1612 0.2384 0.1775 -0.0118 -0.0238 -0.0176 78  TYR B O   
1419 C CB  . TYR B 110 ? 0.1637 0.2066 0.1460 0.0254  0.0124  -0.0092 78  TYR B CB  
1420 C CG  . TYR B 110 ? 0.1628 0.2000 0.1317 0.0240  0.0226  0.0100  78  TYR B CG  
1421 C CD1 . TYR B 110 ? 0.1770 0.1972 0.1326 0.0189  0.0152  0.0092  78  TYR B CD1 
1422 C CD2 . TYR B 110 ? 0.1558 0.2019 0.1334 0.0276  0.0334  0.0138  78  TYR B CD2 
1423 C CE1 . TYR B 110 ? 0.1780 0.1950 0.1521 0.0285  -0.0047 0.0230  78  TYR B CE1 
1424 C CE2 . TYR B 110 ? 0.1768 0.2115 0.1350 0.0359  0.0221  0.0198  78  TYR B CE2 
1425 C CZ  . TYR B 110 ? 0.1721 0.2076 0.1499 0.0161  0.0090  0.0185  78  TYR B CZ  
1426 O OH  . TYR B 110 ? 0.1946 0.2146 0.1832 0.0286  -0.0046 0.0115  78  TYR B OH  
1427 N N   . TRP B 111 ? 0.1576 0.2085 0.1540 0.0047  0.0110  -0.0203 79  TRP B N   
1428 C CA  . TRP B 111 ? 0.1419 0.1939 0.1496 0.0041  0.0235  -0.0061 79  TRP B CA  
1429 C C   . TRP B 111 ? 0.1429 0.2054 0.1849 -0.0003 0.0235  -0.0117 79  TRP B C   
1430 O O   . TRP B 111 ? 0.1366 0.2223 0.2185 -0.0307 0.0053  -0.0187 79  TRP B O   
1431 C CB  . TRP B 111 ? 0.1511 0.1883 0.1388 0.0001  -0.0071 -0.0140 79  TRP B CB  
1432 C CG  . TRP B 111 ? 0.1336 0.1645 0.1286 -0.0027 0.0059  0.0026  79  TRP B CG  
1433 C CD1 . TRP B 111 ? 0.1493 0.1419 0.1194 -0.0112 0.0053  0.0027  79  TRP B CD1 
1434 C CD2 . TRP B 111 ? 0.1570 0.1523 0.1310 -0.0139 0.0022  0.0082  79  TRP B CD2 
1435 N NE1 . TRP B 111 ? 0.1662 0.1502 0.1158 0.0004  0.0031  0.0068  79  TRP B NE1 
1436 C CE2 . TRP B 111 ? 0.1546 0.1556 0.1236 0.0099  0.0134  0.0068  79  TRP B CE2 
1437 C CE3 . TRP B 111 ? 0.1901 0.1519 0.1279 -0.0085 -0.0161 -0.0137 79  TRP B CE3 
1438 C CZ2 . TRP B 111 ? 0.1841 0.1540 0.1379 0.0093  -0.0139 0.0198  79  TRP B CZ2 
1439 C CZ3 . TRP B 111 ? 0.1854 0.1593 0.1530 -0.0206 -0.0408 -0.0029 79  TRP B CZ3 
1440 C CH2 . TRP B 111 ? 0.1743 0.1706 0.1536 -0.0078 -0.0347 0.0180  79  TRP B CH2 
1441 N N   . LYS B 112 ? 0.1221 0.2145 0.2096 0.0068  0.0214  -0.0213 80  LYS B N   
1442 C CA  . LYS B 112 ? 0.1277 0.2432 0.2605 0.0176  0.0213  -0.0069 80  LYS B CA  
1443 C C   . LYS B 112 ? 0.1323 0.2648 0.2888 0.0337  -0.0028 -0.0084 80  LYS B C   
1444 O O   . LYS B 112 ? 0.1374 0.2871 0.3141 0.0078  -0.0140 -0.0089 80  LYS B O   
1445 C CB  . LYS B 112 ? 0.1584 0.2777 0.2887 0.0344  0.0169  -0.0132 80  LYS B CB  
1446 C CG  . LYS B 112 ? 0.2803 0.3454 0.3204 0.0131  0.0110  -0.0245 80  LYS B CG  
1447 C CD  . LYS B 112 ? 0.3509 0.4274 0.3621 0.0085  -0.0211 -0.0165 80  LYS B CD  
1448 C CE  . LYS B 112 ? 0.3955 0.4912 0.4029 0.0007  -0.0606 -0.0002 80  LYS B CE  
1449 N NZ  . LYS B 112 ? 0.3962 0.5141 0.4224 -0.0049 -0.0754 0.0043  80  LYS B NZ  
1450 N N   . ALA B 113 ? 0.1272 0.2734 0.2872 0.0215  -0.0334 -0.0085 81  ALA B N   
1451 C CA  . ALA B 113 ? 0.1769 0.3043 0.2970 -0.0080 -0.0360 -0.0224 81  ALA B CA  
1452 C C   . ALA B 113 ? 0.1727 0.3055 0.3040 -0.0206 -0.0373 -0.0456 81  ALA B C   
1453 O O   . ALA B 113 ? 0.2179 0.3235 0.3113 -0.0264 -0.0678 -0.0504 81  ALA B O   
1454 C CB  . ALA B 113 ? 0.2442 0.3256 0.2904 -0.0124 -0.0438 -0.0342 81  ALA B CB  
1455 N N   . LEU B 114 ? 0.1769 0.2818 0.3227 -0.0317 -0.0155 -0.0513 82  LEU B N   
1456 C CA  . LEU B 114 ? 0.1939 0.2820 0.3499 -0.0270 -0.0336 -0.0538 82  LEU B CA  
1457 C C   . LEU B 114 ? 0.2062 0.2970 0.3736 -0.0169 -0.0151 -0.0379 82  LEU B C   
1458 O O   . LEU B 114 ? 0.2464 0.3047 0.4001 -0.0255 -0.0126 -0.0324 82  LEU B O   
1459 C CB  . LEU B 114 ? 0.2058 0.2886 0.3549 -0.0178 -0.0635 -0.0683 82  LEU B CB  
1460 C CG  . LEU B 114 ? 0.2096 0.3069 0.3536 -0.0106 -0.0700 -0.0723 82  LEU B CG  
1461 C CD1 . LEU B 114 ? 0.2270 0.3101 0.3648 0.0105  -0.0418 -0.0723 82  LEU B CD1 
1462 C CD2 . LEU B 114 ? 0.2825 0.3289 0.3523 -0.0097 -0.0644 -0.0717 82  LEU B CD2 
1463 N N   . GLY B 115 ? 0.1904 0.3096 0.3584 -0.0419 -0.0258 -0.0316 83  GLY B N   
1464 C CA  . GLY B 115 ? 0.1665 0.3384 0.3584 -0.0195 -0.0091 -0.0061 83  GLY B CA  
1465 C C   . GLY B 115 ? 0.1645 0.3672 0.3626 -0.0441 0.0203  0.0435  83  GLY B C   
1466 O O   . GLY B 115 ? 0.2065 0.3782 0.3741 -0.0462 0.0377  0.0512  83  GLY B O   
1467 N N   . ILE B 116 ? 0.1622 0.3993 0.3538 -0.0623 0.0168  0.0671  84  ILE B N   
1468 C CA  . ILE B 116 ? 0.1904 0.4452 0.3532 -0.0546 0.0292  0.0851  84  ILE B CA  
1469 C C   . ILE B 116 ? 0.1853 0.4623 0.3007 -0.0761 0.0278  0.0785  84  ILE B C   
1470 O O   . ILE B 116 ? 0.1974 0.4660 0.2771 -0.0871 0.0137  0.0673  84  ILE B O   
1471 C CB  . ILE B 116 ? 0.1785 0.4655 0.3923 -0.0291 0.0162  0.1031  84  ILE B CB  
1472 C CG1 . ILE B 116 ? 0.1832 0.4656 0.4095 -0.0238 0.0546  0.1216  84  ILE B CG1 
1473 C CG2 . ILE B 116 ? 0.2128 0.4824 0.4091 0.0008  -0.0123 0.1001  84  ILE B CG2 
1474 C CD1 . ILE B 116 ? 0.1889 0.4730 0.4179 -0.0090 0.0670  0.1347  84  ILE B CD1 
1475 N N   . SER B 117 ? 0.1841 0.4720 0.2838 -0.0650 0.0312  0.0746  85  SER B N   
1476 C CA  . SER B 117 ? 0.1719 0.4596 0.2676 -0.0472 0.0463  0.0645  85  SER B CA  
1477 C C   . SER B 117 ? 0.1967 0.3893 0.2398 -0.0237 0.0019  0.0637  85  SER B C   
1478 O O   . SER B 117 ? 0.1964 0.4187 0.2780 -0.0456 -0.0098 0.0957  85  SER B O   
1479 C CB  . SER B 117 ? 0.2260 0.5038 0.3048 -0.0484 0.0663  0.0409  85  SER B CB  
1480 O OG  . SER B 117 ? 0.3155 0.5225 0.3351 -0.0250 0.0715  0.0189  85  SER B OG  
1481 N N   . PRO B 118 ? 0.1752 0.2851 0.1697 -0.0042 0.0010  0.0120  86  PRO B N   
1482 C CA  . PRO B 118 ? 0.1745 0.2408 0.1474 -0.0128 0.0016  -0.0015 86  PRO B CA  
1483 C C   . PRO B 118 ? 0.1799 0.2001 0.1556 -0.0041 0.0142  -0.0113 86  PRO B C   
1484 O O   . PRO B 118 ? 0.2098 0.2397 0.1792 0.0229  0.0270  -0.0235 86  PRO B O   
1485 C CB  . PRO B 118 ? 0.2167 0.2321 0.1415 -0.0134 0.0250  -0.0041 86  PRO B CB  
1486 C CG  . PRO B 118 ? 0.2422 0.2394 0.1756 -0.0214 0.0007  -0.0042 86  PRO B CG  
1487 C CD  . PRO B 118 ? 0.2320 0.2676 0.1741 0.0133  0.0014  -0.0002 86  PRO B CD  
1488 N N   . PHE B 119 ? 0.1831 0.1588 0.1537 -0.0001 -0.0099 -0.0195 87  PHE B N   
1489 C CA  . PHE B 119 ? 0.2010 0.1473 0.1368 -0.0029 0.0194  -0.0064 87  PHE B CA  
1490 C C   . PHE B 119 ? 0.1806 0.1449 0.1188 -0.0020 0.0300  0.0069  87  PHE B C   
1491 O O   . PHE B 119 ? 0.2193 0.1441 0.1304 -0.0005 0.0269  -0.0135 87  PHE B O   
1492 C CB  . PHE B 119 ? 0.2167 0.1416 0.1451 0.0006  0.0190  -0.0097 87  PHE B CB  
1493 C CG  . PHE B 119 ? 0.2520 0.1364 0.1350 0.0202  -0.0159 -0.0211 87  PHE B CG  
1494 C CD1 . PHE B 119 ? 0.2995 0.1428 0.1453 0.0324  -0.0147 -0.0064 87  PHE B CD1 
1495 C CD2 . PHE B 119 ? 0.2657 0.1275 0.1509 0.0044  -0.0293 -0.0144 87  PHE B CD2 
1496 C CE1 . PHE B 119 ? 0.3311 0.1397 0.1675 0.0361  -0.0341 -0.0126 87  PHE B CE1 
1497 C CE2 . PHE B 119 ? 0.3146 0.1556 0.1653 0.0047  -0.0372 -0.0151 87  PHE B CE2 
1498 C CZ  . PHE B 119 ? 0.3371 0.1428 0.1755 0.0317  -0.0419 -0.0185 87  PHE B CZ  
1499 N N   . HIS B 120 ? 0.1807 0.1445 0.1136 -0.0173 0.0048  0.0059  88  HIS B N   
1500 C CA  . HIS B 120 ? 0.1843 0.1616 0.1292 -0.0266 0.0186  0.0085  88  HIS B CA  
1501 C C   . HIS B 120 ? 0.1802 0.1574 0.1221 -0.0232 0.0031  -0.0003 88  HIS B C   
1502 O O   . HIS B 120 ? 0.1874 0.1714 0.1422 -0.0269 -0.0113 -0.0127 88  HIS B O   
1503 C CB  . HIS B 120 ? 0.1996 0.1567 0.1453 -0.0242 -0.0081 0.0143  88  HIS B CB  
1504 C CG  . HIS B 120 ? 0.1832 0.1600 0.1632 -0.0198 -0.0387 0.0003  88  HIS B CG  
1505 N ND1 . HIS B 120 ? 0.1661 0.1443 0.1717 -0.0118 -0.0244 -0.0156 88  HIS B ND1 
1506 C CD2 . HIS B 120 ? 0.2264 0.1751 0.2188 -0.0073 -0.0685 0.0178  88  HIS B CD2 
1507 C CE1 . HIS B 120 ? 0.1951 0.1564 0.2105 -0.0190 -0.0416 0.0023  88  HIS B CE1 
1508 N NE2 . HIS B 120 ? 0.2264 0.1670 0.2454 -0.0123 -0.0966 0.0181  88  HIS B NE2 
1509 N N   . GLU B 121 ? 0.1588 0.1500 0.1317 -0.0001 -0.0047 0.0086  89  GLU B N   
1510 C CA  . GLU B 121 ? 0.1906 0.1622 0.1550 0.0056  -0.0176 0.0065  89  GLU B CA  
1511 C C   . GLU B 121 ? 0.1804 0.1883 0.1492 -0.0224 -0.0093 0.0175  89  GLU B C   
1512 O O   . GLU B 121 ? 0.1995 0.2281 0.1660 -0.0198 -0.0353 0.0292  89  GLU B O   
1513 C CB  . GLU B 121 ? 0.2042 0.1789 0.1919 0.0172  -0.0263 -0.0309 89  GLU B CB  
1514 C CG  . GLU B 121 ? 0.2208 0.2225 0.2172 0.0156  -0.0144 -0.0516 89  GLU B CG  
1515 C CD  . GLU B 121 ? 0.2413 0.2635 0.2358 0.0460  -0.0162 -0.0334 89  GLU B CD  
1516 O OE1 . GLU B 121 ? 0.2925 0.2976 0.2485 0.0410  0.0049  -0.0088 89  GLU B OE1 
1517 O OE2 . GLU B 121 ? 0.2610 0.2768 0.2498 0.0339  -0.0202 -0.0449 89  GLU B OE2 
1518 N N   . HIS B 122 ? 0.1758 0.2034 0.1244 -0.0274 0.0008  0.0254  90  HIS B N   
1519 C CA  . HIS B 122 ? 0.1874 0.2374 0.1141 -0.0500 0.0182  0.0518  90  HIS B CA  
1520 C C   . HIS B 122 ? 0.1765 0.2997 0.1169 0.0039  -0.0061 0.0515  90  HIS B C   
1521 O O   . HIS B 122 ? 0.2004 0.3372 0.1229 0.0243  -0.0263 0.0507  90  HIS B O   
1522 C CB  . HIS B 122 ? 0.2806 0.2472 0.1496 -0.0515 0.0058  0.0562  90  HIS B CB  
1523 C CG  . HIS B 122 ? 0.3856 0.2748 0.2011 -0.0812 0.0158  0.0516  90  HIS B CG  
1524 N ND1 . HIS B 122 ? 0.4380 0.2951 0.2286 -0.1172 0.0289  0.0391  90  HIS B ND1 
1525 C CD2 . HIS B 122 ? 0.4344 0.2825 0.2306 -0.1122 -0.0096 0.0377  90  HIS B CD2 
1526 C CE1 . HIS B 122 ? 0.4710 0.3031 0.2434 -0.1089 0.0120  0.0133  90  HIS B CE1 
1527 N NE2 . HIS B 122 ? 0.4716 0.3043 0.2472 -0.1195 0.0026  0.0231  90  HIS B NE2 
1528 N N   . ALA B 123 ? 0.1575 0.3444 0.1387 0.0166  0.0054  0.0677  91  ALA B N   
1529 C CA  . ALA B 123 ? 0.1943 0.3872 0.1773 0.0132  -0.0065 0.0762  91  ALA B CA  
1530 C C   . ALA B 123 ? 0.1725 0.4128 0.1908 -0.0108 -0.0294 0.0888  91  ALA B C   
1531 O O   . ALA B 123 ? 0.2116 0.4256 0.1957 -0.0351 -0.0252 0.1251  91  ALA B O   
1532 C CB  . ALA B 123 ? 0.2279 0.3883 0.2162 0.0303  0.0162  0.0850  91  ALA B CB  
1533 N N   . GLU B 124 ? 0.1727 0.4321 0.1877 -0.0116 0.0084  0.0697  92  GLU B N   
1534 C CA  . GLU B 124 ? 0.1882 0.4173 0.2131 -0.0192 0.0116  0.0464  92  GLU B CA  
1535 C C   . GLU B 124 ? 0.1982 0.3748 0.2023 -0.0029 -0.0039 0.0686  92  GLU B C   
1536 O O   . GLU B 124 ? 0.2588 0.3997 0.2445 0.0108  -0.0017 0.0908  92  GLU B O   
1537 C CB  . GLU B 124 ? 0.2353 0.4402 0.2341 0.0166  -0.0032 0.0215  92  GLU B CB  
1538 N N   . VAL B 125 ? 0.1408 0.2863 0.1572 -0.0291 -0.0198 0.0478  93  VAL B N   
1539 C CA  . VAL B 125 ? 0.1377 0.2398 0.1621 -0.0170 -0.0240 0.0336  93  VAL B CA  
1540 C C   . VAL B 125 ? 0.1248 0.2028 0.1448 -0.0082 0.0036  0.0421  93  VAL B C   
1541 O O   . VAL B 125 ? 0.1544 0.1960 0.1607 -0.0027 -0.0055 0.0605  93  VAL B O   
1542 C CB  . VAL B 125 ? 0.1709 0.2424 0.2078 -0.0273 -0.0448 0.0170  93  VAL B CB  
1543 C CG1 . VAL B 125 ? 0.1853 0.2417 0.2185 0.0005  -0.0547 0.0052  93  VAL B CG1 
1544 C CG2 . VAL B 125 ? 0.1877 0.2480 0.2420 -0.0328 -0.0478 0.0128  93  VAL B CG2 
1545 N N   . VAL B 126 ? 0.1335 0.1748 0.1313 -0.0181 0.0090  0.0243  94  VAL B N   
1546 C CA  . VAL B 126 ? 0.1344 0.1793 0.1198 -0.0097 0.0173  0.0146  94  VAL B CA  
1547 C C   . VAL B 126 ? 0.1428 0.1774 0.1176 -0.0037 0.0067  0.0175  94  VAL B C   
1548 O O   . VAL B 126 ? 0.1664 0.1763 0.1297 0.0178  -0.0299 0.0337  94  VAL B O   
1549 C CB  . VAL B 126 ? 0.1476 0.1902 0.1351 -0.0119 0.0174  -0.0024 94  VAL B CB  
1550 C CG1 . VAL B 126 ? 0.1727 0.1825 0.1677 -0.0116 -0.0068 0.0144  94  VAL B CG1 
1551 C CG2 . VAL B 126 ? 0.1952 0.2074 0.1643 0.0198  0.0215  -0.0097 94  VAL B CG2 
1552 N N   . PHE B 127 ? 0.1441 0.1878 0.1065 -0.0031 0.0161  0.0162  95  PHE B N   
1553 C CA  . PHE B 127 ? 0.1325 0.1847 0.1077 0.0037  0.0045  0.0188  95  PHE B CA  
1554 C C   . PHE B 127 ? 0.1378 0.2010 0.1212 0.0063  0.0092  0.0048  95  PHE B C   
1555 O O   . PHE B 127 ? 0.1734 0.1749 0.1426 0.0022  0.0086  -0.0009 95  PHE B O   
1556 C CB  . PHE B 127 ? 0.1543 0.1793 0.0966 0.0090  -0.0044 0.0187  95  PHE B CB  
1557 C CG  . PHE B 127 ? 0.1799 0.1830 0.1249 -0.0081 0.0019  0.0077  95  PHE B CG  
1558 C CD1 . PHE B 127 ? 0.1919 0.1994 0.1564 -0.0018 -0.0414 -0.0121 95  PHE B CD1 
1559 C CD2 . PHE B 127 ? 0.2534 0.1727 0.1083 -0.0058 -0.0311 0.0270  95  PHE B CD2 
1560 C CE1 . PHE B 127 ? 0.2533 0.1975 0.1771 0.0147  -0.0587 -0.0123 95  PHE B CE1 
1561 C CE2 . PHE B 127 ? 0.2949 0.1834 0.1403 -0.0216 -0.0475 0.0071  95  PHE B CE2 
1562 C CZ  . PHE B 127 ? 0.3148 0.1850 0.1664 0.0084  -0.0718 -0.0029 95  PHE B CZ  
1563 N N   . THR B 128 ? 0.1425 0.2276 0.1423 -0.0177 0.0249  0.0258  96  THR B N   
1564 C CA  . THR B 128 ? 0.1566 0.2340 0.1435 -0.0245 0.0214  0.0250  96  THR B CA  
1565 C C   . THR B 128 ? 0.1901 0.2166 0.1543 -0.0124 0.0361  0.0282  96  THR B C   
1566 O O   . THR B 128 ? 0.2789 0.2159 0.1463 0.0088  0.0387  0.0368  96  THR B O   
1567 C CB  . THR B 128 ? 0.1939 0.2670 0.1512 -0.0364 0.0133  0.0180  96  THR B CB  
1568 O OG1 . THR B 128 ? 0.2138 0.2684 0.1526 -0.0393 0.0038  0.0237  96  THR B OG1 
1569 C CG2 . THR B 128 ? 0.1844 0.2769 0.1523 -0.0397 0.0283  0.0210  96  THR B CG2 
1570 N N   . ALA B 129 ? 0.1714 0.2065 0.1396 -0.0186 0.0383  0.0210  97  ALA B N   
1571 C CA  . ALA B 129 ? 0.1690 0.1987 0.1607 -0.0293 0.0380  0.0186  97  ALA B CA  
1572 C C   . ALA B 129 ? 0.2125 0.2042 0.1766 -0.0227 0.0280  0.0240  97  ALA B C   
1573 O O   . ALA B 129 ? 0.2159 0.1942 0.1880 -0.0087 0.0294  0.0275  97  ALA B O   
1574 C CB  . ALA B 129 ? 0.2181 0.2257 0.1759 -0.0026 0.0134  0.0183  97  ALA B CB  
1575 N N   . ASN B 130 ? 0.2051 0.2216 0.1617 -0.0005 0.0485  0.0230  98  ASN B N   
1576 C CA  . ASN B 130 ? 0.1763 0.2473 0.1724 -0.0037 0.0423  0.0332  98  ASN B CA  
1577 C C   . ASN B 130 ? 0.1890 0.2762 0.1954 -0.0120 0.0344  0.0368  98  ASN B C   
1578 O O   . ASN B 130 ? 0.2032 0.2668 0.2101 -0.0020 0.0280  0.0656  98  ASN B O   
1579 C CB  . ASN B 130 ? 0.1992 0.2596 0.1540 -0.0030 0.0127  0.0286  98  ASN B CB  
1580 C CG  . ASN B 130 ? 0.2252 0.2524 0.1592 -0.0070 0.0434  0.0164  98  ASN B CG  
1581 O OD1 . ASN B 130 ? 0.2648 0.2420 0.1839 -0.0126 0.0400  -0.0100 98  ASN B OD1 
1582 N ND2 . ASN B 130 ? 0.2317 0.2595 0.1515 -0.0006 0.0342  0.0353  98  ASN B ND2 
1583 N N   . ASP B 131 ? 0.2757 0.3405 0.2048 -0.0024 0.0465  0.0191  99  ASP B N   
1584 C CA  . ASP B 131 ? 0.4331 0.4403 0.2239 0.0295  0.0480  0.0365  99  ASP B CA  
1585 C C   . ASP B 131 ? 0.4447 0.4176 0.2362 0.0499  0.0899  0.0528  99  ASP B C   
1586 O O   . ASP B 131 ? 0.5188 0.4138 0.2481 0.0652  0.0815  0.0610  99  ASP B O   
1587 C CB  . ASP B 131 ? 0.5979 0.5426 0.2270 0.0293  0.0264  0.0458  99  ASP B CB  
1588 C CG  . ASP B 131 ? 0.7424 0.6219 0.2528 0.0239  -0.0018 0.0487  99  ASP B CG  
1589 O OD1 . ASP B 131 ? 0.8075 0.6550 0.2607 0.0180  -0.0150 0.0512  99  ASP B OD1 
1590 O OD2 . ASP B 131 ? 0.7823 0.6498 0.2776 0.0271  -0.0245 0.0508  99  ASP B OD2 
1591 N N   . SER B 132 ? 0.3346 0.3800 0.2344 0.0344  0.1217  0.0674  100 SER B N   
1592 C CA  . SER B 132 ? 0.3192 0.3501 0.2619 0.0248  0.1002  0.0808  100 SER B CA  
1593 C C   . SER B 132 ? 0.2428 0.3034 0.2543 -0.0197 0.0844  0.0714  100 SER B C   
1594 O O   . SER B 132 ? 0.2302 0.2854 0.2564 -0.0219 0.0741  0.0653  100 SER B O   
1595 C CB  . SER B 132 ? 0.3504 0.3646 0.2973 0.0663  0.0886  0.0942  100 SER B CB  
1596 O OG  . SER B 132 ? 0.3811 0.3749 0.3241 0.0690  0.0740  0.0861  100 SER B OG  
1597 N N   . GLY B 133 ? 0.2215 0.2692 0.2470 -0.0115 0.0567  0.0757  101 GLY B N   
1598 C CA  . GLY B 133 ? 0.2373 0.2686 0.2661 -0.0157 0.0471  0.0702  101 GLY B CA  
1599 C C   . GLY B 133 ? 0.2210 0.2407 0.2582 -0.0140 0.0715  0.0821  101 GLY B C   
1600 O O   . GLY B 133 ? 0.2472 0.2213 0.2536 -0.0035 0.0680  0.0670  101 GLY B O   
1601 N N   . PRO B 134 ? 0.2146 0.2528 0.2806 -0.0202 0.0562  0.0995  102 PRO B N   
1602 C CA  . PRO B 134 ? 0.2004 0.2653 0.2839 -0.0325 0.0375  0.0973  102 PRO B CA  
1603 C C   . PRO B 134 ? 0.1883 0.2541 0.2840 -0.0031 0.0305  0.0601  102 PRO B C   
1604 O O   . PRO B 134 ? 0.2040 0.2453 0.2901 0.0062  0.0352  0.0514  102 PRO B O   
1605 C CB  . PRO B 134 ? 0.2587 0.2896 0.2885 -0.0387 0.0325  0.0984  102 PRO B CB  
1606 C CG  . PRO B 134 ? 0.3092 0.2931 0.2992 -0.0526 0.0104  0.1098  102 PRO B CG  
1607 C CD  . PRO B 134 ? 0.2474 0.2813 0.2851 -0.0436 0.0269  0.1183  102 PRO B CD  
1608 N N   . ARG B 135 ? 0.1799 0.2469 0.2542 -0.0251 0.0271  0.0618  103 ARG B N   
1609 C CA  . ARG B 135 ? 0.2135 0.2588 0.2300 -0.0254 0.0198  0.0839  103 ARG B CA  
1610 C C   . ARG B 135 ? 0.1990 0.2640 0.2279 -0.0125 0.0187  0.0759  103 ARG B C   
1611 O O   . ARG B 135 ? 0.2164 0.2767 0.2286 -0.0213 0.0088  0.0634  103 ARG B O   
1612 C CB  . ARG B 135 ? 0.2205 0.2769 0.2308 -0.0033 -0.0163 0.0841  103 ARG B CB  
1613 C CG  . ARG B 135 ? 0.1969 0.2823 0.2414 0.0017  -0.0095 0.0927  103 ARG B CG  
1614 C CD  . ARG B 135 ? 0.2262 0.3053 0.2613 0.0277  -0.0006 0.0838  103 ARG B CD  
1615 N NE  . ARG B 135 ? 0.2239 0.3174 0.2741 0.0271  0.0191  0.0776  103 ARG B NE  
1616 C CZ  . ARG B 135 ? 0.2371 0.3240 0.2788 0.0484  0.0141  0.0753  103 ARG B CZ  
1617 N NH1 . ARG B 135 ? 0.2496 0.3184 0.2594 0.0575  0.0135  0.0902  103 ARG B NH1 
1618 N NH2 . ARG B 135 ? 0.2477 0.3332 0.2944 0.0527  -0.0240 0.0434  103 ARG B NH2 
1619 N N   . ARG B 136 ? 0.2037 0.2591 0.2118 -0.0225 0.0118  0.0567  104 ARG B N   
1620 C CA  . ARG B 136 ? 0.2075 0.2706 0.1934 -0.0013 0.0430  0.0377  104 ARG B CA  
1621 C C   . ARG B 136 ? 0.2116 0.2689 0.1870 -0.0037 0.0248  0.0471  104 ARG B C   
1622 O O   . ARG B 136 ? 0.2166 0.2746 0.1994 0.0304  0.0382  0.0633  104 ARG B O   
1623 C CB  . ARG B 136 ? 0.2467 0.2861 0.2054 0.0153  0.0368  0.0100  104 ARG B CB  
1624 N N   . TYR B 137 ? 0.1547 0.2614 0.1605 -0.0172 0.0210  0.0385  105 TYR B N   
1625 C CA  . TYR B 137 ? 0.1499 0.2335 0.1565 -0.0073 0.0240  0.0360  105 TYR B CA  
1626 C C   . TYR B 137 ? 0.1531 0.2275 0.1630 -0.0036 0.0176  0.0387  105 TYR B C   
1627 O O   . TYR B 137 ? 0.1674 0.2312 0.1917 -0.0189 0.0009  0.0521  105 TYR B O   
1628 C CB  . TYR B 137 ? 0.1759 0.2330 0.1763 0.0019  0.0046  0.0156  105 TYR B CB  
1629 C CG  . TYR B 137 ? 0.1858 0.2383 0.1889 0.0036  0.0022  0.0284  105 TYR B CG  
1630 C CD1 . TYR B 137 ? 0.2324 0.2294 0.2007 -0.0109 -0.0009 0.0269  105 TYR B CD1 
1631 C CD2 . TYR B 137 ? 0.1765 0.2314 0.1956 -0.0044 -0.0064 0.0387  105 TYR B CD2 
1632 C CE1 . TYR B 137 ? 0.2339 0.2085 0.1934 -0.0228 -0.0080 0.0428  105 TYR B CE1 
1633 C CE2 . TYR B 137 ? 0.2200 0.2129 0.2110 -0.0165 -0.0063 0.0329  105 TYR B CE2 
1634 C CZ  . TYR B 137 ? 0.2207 0.2042 0.2059 -0.0206 -0.0144 0.0288  105 TYR B CZ  
1635 O OH  . TYR B 137 ? 0.2474 0.1958 0.2343 -0.0181 -0.0110 0.0260  105 TYR B OH  
1636 N N   . THR B 138 ? 0.1581 0.2281 0.1312 0.0074  0.0145  0.0380  106 THR B N   
1637 C CA  . THR B 138 ? 0.1771 0.2306 0.1113 0.0089  0.0148  0.0355  106 THR B CA  
1638 C C   . THR B 138 ? 0.1779 0.2228 0.1051 -0.0059 0.0037  0.0494  106 THR B C   
1639 O O   . THR B 138 ? 0.1739 0.2350 0.1263 0.0082  0.0052  0.0426  106 THR B O   
1640 C CB  . THR B 138 ? 0.2005 0.2520 0.1358 0.0120  0.0126  0.0077  106 THR B CB  
1641 O OG1 . THR B 138 ? 0.2676 0.2666 0.1563 0.0252  0.0020  -0.0059 106 THR B OG1 
1642 C CG2 . THR B 138 ? 0.2358 0.2779 0.1551 -0.0049 0.0160  -0.0106 106 THR B CG2 
1643 N N   . ILE B 139 ? 0.1529 0.2297 0.1125 -0.0111 0.0064  0.0417  107 ILE B N   
1644 C CA  . ILE B 139 ? 0.1385 0.2408 0.1229 -0.0015 0.0123  0.0454  107 ILE B CA  
1645 C C   . ILE B 139 ? 0.1356 0.2306 0.1087 -0.0177 0.0098  0.0426  107 ILE B C   
1646 O O   . ILE B 139 ? 0.1516 0.2423 0.1203 -0.0289 -0.0265 0.0452  107 ILE B O   
1647 C CB  . ILE B 139 ? 0.1913 0.2761 0.1612 -0.0114 0.0095  0.0251  107 ILE B CB  
1648 C CG1 . ILE B 139 ? 0.2282 0.3146 0.2236 -0.0177 0.0149  0.0222  107 ILE B CG1 
1649 C CG2 . ILE B 139 ? 0.1952 0.2845 0.1610 0.0051  0.0322  0.0119  107 ILE B CG2 
1650 C CD1 . ILE B 139 ? 0.2628 0.3183 0.2639 -0.0025 0.0211  0.0373  107 ILE B CD1 
1651 N N   . ALA B 140 ? 0.1499 0.2166 0.0945 -0.0149 0.0041  0.0275  108 ALA B N   
1652 C CA  . ALA B 140 ? 0.1715 0.2015 0.1012 -0.0020 0.0132  0.0232  108 ALA B CA  
1653 C C   . ALA B 140 ? 0.1561 0.2239 0.0964 -0.0090 -0.0083 0.0215  108 ALA B C   
1654 O O   . ALA B 140 ? 0.1675 0.2746 0.1072 0.0106  -0.0174 0.0074  108 ALA B O   
1655 C CB  . ALA B 140 ? 0.1964 0.1882 0.1377 -0.0056 -0.0037 0.0158  108 ALA B CB  
1656 N N   . ALA B 141 ? 0.1516 0.1936 0.0869 -0.0199 -0.0001 0.0266  109 ALA B N   
1657 C CA  . ALA B 141 ? 0.1555 0.1907 0.1101 -0.0469 -0.0154 0.0024  109 ALA B CA  
1658 C C   . ALA B 141 ? 0.1543 0.1867 0.0981 -0.0458 0.0017  0.0223  109 ALA B C   
1659 O O   . ALA B 141 ? 0.1713 0.2154 0.1169 -0.0606 -0.0258 0.0274  109 ALA B O   
1660 C CB  . ALA B 141 ? 0.1723 0.1905 0.1517 -0.0171 -0.0016 -0.0086 109 ALA B CB  
1661 N N   . LEU B 142 ? 0.1733 0.1631 0.0915 -0.0142 0.0078  0.0182  110 LEU B N   
1662 C CA  . LEU B 142 ? 0.1512 0.1524 0.0959 0.0070  0.0070  0.0192  110 LEU B CA  
1663 C C   . LEU B 142 ? 0.1561 0.1651 0.0951 -0.0166 0.0110  0.0054  110 LEU B C   
1664 O O   . LEU B 142 ? 0.1858 0.1979 0.0849 -0.0075 0.0049  -0.0035 110 LEU B O   
1665 C CB  . LEU B 142 ? 0.2206 0.1876 0.1500 0.0130  -0.0394 0.0235  110 LEU B CB  
1666 C CG  . LEU B 142 ? 0.3145 0.2071 0.2054 0.0300  -0.0652 0.0282  110 LEU B CG  
1667 C CD1 . LEU B 142 ? 0.3502 0.2146 0.2217 0.0230  -0.0483 0.0265  110 LEU B CD1 
1668 C CD2 . LEU B 142 ? 0.3853 0.1913 0.2452 0.0567  -0.0756 0.0366  110 LEU B CD2 
1669 N N   . LEU B 143 ? 0.1413 0.1535 0.1083 -0.0136 0.0144  0.0103  111 LEU B N   
1670 C CA  . LEU B 143 ? 0.1610 0.1583 0.1093 -0.0115 0.0111  0.0049  111 LEU B CA  
1671 C C   . LEU B 143 ? 0.1360 0.1521 0.0868 -0.0149 0.0079  -0.0050 111 LEU B C   
1672 O O   . LEU B 143 ? 0.1450 0.1449 0.1112 -0.0129 -0.0055 -0.0068 111 LEU B O   
1673 C CB  . LEU B 143 ? 0.1823 0.1504 0.0964 -0.0018 -0.0027 0.0115  111 LEU B CB  
1674 C CG  . LEU B 143 ? 0.1924 0.1538 0.1139 -0.0049 -0.0044 0.0119  111 LEU B CG  
1675 C CD1 . LEU B 143 ? 0.2031 0.1789 0.1123 0.0044  -0.0002 0.0227  111 LEU B CD1 
1676 C CD2 . LEU B 143 ? 0.1737 0.1465 0.1263 -0.0177 0.0197  -0.0123 111 LEU B CD2 
1677 N N   . SER B 144 ? 0.1869 0.1645 0.0756 -0.0108 0.0028  0.0036  112 SER B N   
1678 C CA  . SER B 144 ? 0.1788 0.1452 0.0851 -0.0001 -0.0087 0.0007  112 SER B CA  
1679 C C   . SER B 144 ? 0.1400 0.1517 0.1017 0.0041  -0.0052 -0.0264 112 SER B C   
1680 O O   . SER B 144 ? 0.1721 0.1490 0.1091 -0.0198 -0.0089 -0.0187 112 SER B O   
1681 C CB  . SER B 144 ? 0.1922 0.1518 0.1047 0.0218  -0.0096 -0.0048 112 SER B CB  
1682 O OG  . SER B 144 ? 0.2109 0.1686 0.1122 0.0280  0.0117  -0.0112 112 SER B OG  
1683 N N   . PRO B 145 ? 0.1536 0.1412 0.1282 0.0001  0.0010  -0.0192 113 PRO B N   
1684 C CA  . PRO B 145 ? 0.1407 0.1380 0.1250 -0.0063 0.0043  -0.0339 113 PRO B CA  
1685 C C   . PRO B 145 ? 0.1386 0.1410 0.1195 -0.0042 0.0111  -0.0237 113 PRO B C   
1686 O O   . PRO B 145 ? 0.1797 0.1234 0.1251 -0.0084 0.0238  -0.0249 113 PRO B O   
1687 C CB  . PRO B 145 ? 0.1459 0.1562 0.1330 -0.0062 0.0127  -0.0219 113 PRO B CB  
1688 C CG  . PRO B 145 ? 0.1679 0.1622 0.1508 -0.0119 -0.0184 -0.0234 113 PRO B CG  
1689 C CD  . PRO B 145 ? 0.1692 0.1510 0.1520 -0.0188 -0.0018 -0.0246 113 PRO B CD  
1690 N N   . TYR B 146 ? 0.1369 0.1430 0.1047 -0.0046 0.0117  -0.0195 114 TYR B N   
1691 C CA  . TYR B 146 ? 0.1498 0.1534 0.1121 -0.0180 0.0075  -0.0181 114 TYR B CA  
1692 C C   . TYR B 146 ? 0.1479 0.1639 0.1009 -0.0177 0.0029  -0.0256 114 TYR B C   
1693 O O   . TYR B 146 ? 0.1747 0.2064 0.1165 -0.0176 -0.0109 -0.0319 114 TYR B O   
1694 C CB  . TYR B 146 ? 0.1659 0.1711 0.1320 -0.0027 0.0212  -0.0154 114 TYR B CB  
1695 C CG  . TYR B 146 ? 0.1507 0.2201 0.1194 -0.0007 0.0132  -0.0039 114 TYR B CG  
1696 C CD1 . TYR B 146 ? 0.1669 0.3054 0.1705 0.0075  0.0399  -0.0167 114 TYR B CD1 
1697 C CD2 . TYR B 146 ? 0.1953 0.2175 0.1163 0.0098  0.0390  0.0195  114 TYR B CD2 
1698 C CE1 . TYR B 146 ? 0.2077 0.3566 0.1977 0.0492  0.0443  -0.0115 114 TYR B CE1 
1699 C CE2 . TYR B 146 ? 0.2227 0.2686 0.1625 0.0363  0.0606  0.0282  114 TYR B CE2 
1700 C CZ  . TYR B 146 ? 0.2163 0.3507 0.2076 0.0909  0.0707  0.0024  114 TYR B CZ  
1701 O OH  . TYR B 146 ? 0.2753 0.4265 0.2567 0.1242  0.0937  0.0234  114 TYR B OH  
1702 N N   . SER B 147 ? 0.1375 0.1576 0.1101 -0.0166 0.0191  -0.0263 115 SER B N   
1703 C CA  . SER B 147 ? 0.1410 0.1668 0.1238 -0.0147 0.0213  -0.0267 115 SER B CA  
1704 C C   . SER B 147 ? 0.1361 0.1899 0.1129 -0.0200 0.0070  -0.0211 115 SER B C   
1705 O O   . SER B 147 ? 0.1617 0.2401 0.1254 -0.0449 -0.0109 -0.0212 115 SER B O   
1706 C CB  . SER B 147 ? 0.1481 0.1684 0.1576 0.0016  0.0070  -0.0177 115 SER B CB  
1707 O OG  . SER B 147 ? 0.1783 0.1886 0.1713 0.0070  0.0056  -0.0192 115 SER B OG  
1708 N N   . TYR B 148 ? 0.1464 0.1870 0.0875 -0.0061 0.0023  -0.0113 116 TYR B N   
1709 C CA  . TYR B 148 ? 0.1498 0.2073 0.1144 0.0061  0.0225  0.0125  116 TYR B CA  
1710 C C   . TYR B 148 ? 0.1503 0.2003 0.1056 -0.0014 0.0008  0.0035  116 TYR B C   
1711 O O   . TYR B 148 ? 0.1548 0.1990 0.1085 -0.0061 -0.0258 -0.0086 116 TYR B O   
1712 C CB  . TYR B 148 ? 0.1914 0.2207 0.1637 0.0091  0.0133  -0.0009 116 TYR B CB  
1713 C CG  . TYR B 148 ? 0.2430 0.2226 0.1841 0.0503  -0.0168 -0.0037 116 TYR B CG  
1714 C CD1 . TYR B 148 ? 0.2876 0.2208 0.1985 0.0469  -0.0188 -0.0021 116 TYR B CD1 
1715 C CD2 . TYR B 148 ? 0.3320 0.2260 0.2079 0.0845  -0.0177 0.0012  116 TYR B CD2 
1716 C CE1 . TYR B 148 ? 0.3453 0.2226 0.2201 0.0339  -0.0282 -0.0247 116 TYR B CE1 
1717 C CE2 . TYR B 148 ? 0.4121 0.2373 0.2233 0.0681  -0.0544 -0.0151 116 TYR B CE2 
1718 C CZ  . TYR B 148 ? 0.4377 0.2207 0.2228 0.0301  -0.0451 -0.0224 116 TYR B CZ  
1719 O OH  . TYR B 148 ? 0.5708 0.2164 0.2348 0.0160  -0.0634 -0.0401 116 TYR B OH  
1720 N N   . SER B 149 ? 0.1544 0.2037 0.0911 -0.0117 0.0091  0.0044  117 SER B N   
1721 C CA  . SER B 149 ? 0.1866 0.2214 0.1093 0.0082  0.0073  0.0242  117 SER B CA  
1722 C C   . SER B 149 ? 0.1391 0.2230 0.0879 0.0098  -0.0245 -0.0037 117 SER B C   
1723 O O   . SER B 149 ? 0.1655 0.2302 0.0876 -0.0058 -0.0109 0.0016  117 SER B O   
1724 C CB  . SER B 149 ? 0.3326 0.2481 0.1604 0.0169  0.0300  0.0301  117 SER B CB  
1725 O OG  . SER B 149 ? 0.4116 0.2519 0.2003 -0.0104 0.0395  0.0198  117 SER B OG  
1726 N N   . THR B 150 ? 0.1376 0.2329 0.1089 0.0053  -0.0006 0.0217  118 THR B N   
1727 C CA  . THR B 150 ? 0.1308 0.2421 0.1183 0.0197  0.0077  0.0165  118 THR B CA  
1728 C C   . THR B 150 ? 0.1521 0.2480 0.1038 0.0081  0.0080  0.0207  118 THR B C   
1729 O O   . THR B 150 ? 0.1408 0.2987 0.1118 0.0093  -0.0149 0.0092  118 THR B O   
1730 C CB  . THR B 150 ? 0.1682 0.2230 0.1456 0.0211  -0.0317 0.0114  118 THR B CB  
1731 O OG1 . THR B 150 ? 0.2375 0.2143 0.1623 -0.0044 -0.0352 0.0352  118 THR B OG1 
1732 C CG2 . THR B 150 ? 0.1894 0.2188 0.1516 -0.0031 -0.0440 -0.0063 118 THR B CG2 
1733 N N   . THR B 151 ? 0.1632 0.2119 0.1044 -0.0132 0.0289  0.0269  119 THR B N   
1734 C CA  . THR B 151 ? 0.1592 0.1985 0.1093 -0.0059 0.0447  0.0447  119 THR B CA  
1735 C C   . THR B 151 ? 0.1372 0.2087 0.1097 0.0029  0.0002  0.0349  119 THR B C   
1736 O O   . THR B 151 ? 0.1461 0.2648 0.1346 -0.0179 -0.0190 0.0476  119 THR B O   
1737 C CB  . THR B 151 ? 0.2101 0.2034 0.1484 -0.0083 0.0300  0.0585  119 THR B CB  
1738 O OG1 . THR B 151 ? 0.2336 0.2136 0.1850 -0.0045 -0.0333 0.0305  119 THR B OG1 
1739 C CG2 . THR B 151 ? 0.2744 0.2070 0.1833 0.0509  0.0785  0.0732  119 THR B CG2 
1740 N N   . ALA B 152 ? 0.1474 0.1796 0.0946 0.0012  0.0049  0.0150  120 ALA B N   
1741 C CA  . ALA B 152 ? 0.1702 0.1654 0.1221 -0.0055 0.0193  0.0180  120 ALA B CA  
1742 C C   . ALA B 152 ? 0.1525 0.1883 0.1329 0.0044  0.0072  0.0097  120 ALA B C   
1743 O O   . ALA B 152 ? 0.1876 0.2028 0.1394 0.0330  0.0100  0.0277  120 ALA B O   
1744 C CB  . ALA B 152 ? 0.2213 0.1566 0.1678 -0.0182 0.0315  0.0089  120 ALA B CB  
1745 N N   . VAL B 153 ? 0.1632 0.1922 0.1366 0.0210  0.0104  -0.0088 121 VAL B N   
1746 C CA  . VAL B 153 ? 0.1845 0.2209 0.1803 0.0390  0.0091  0.0146  121 VAL B CA  
1747 C C   . VAL B 153 ? 0.2092 0.2622 0.1577 0.0429  0.0170  0.0555  121 VAL B C   
1748 O O   . VAL B 153 ? 0.2163 0.2828 0.1588 0.0644  0.0184  0.0706  121 VAL B O   
1749 C CB  . VAL B 153 ? 0.2423 0.2101 0.2331 0.0446  0.0078  -0.0073 121 VAL B CB  
1750 C CG1 . VAL B 153 ? 0.2951 0.2204 0.2561 0.0516  0.0309  -0.0212 121 VAL B CG1 
1751 C CG2 . VAL B 153 ? 0.2838 0.2038 0.2517 0.0047  -0.0001 -0.0231 121 VAL B CG2 
1752 N N   . VAL B 154 ? 0.2150 0.2691 0.1684 0.0325  0.0294  0.0703  122 VAL B N   
1753 C CA  . VAL B 154 ? 0.2352 0.2874 0.2035 0.0196  0.0360  0.0834  122 VAL B CA  
1754 C C   . VAL B 154 ? 0.2473 0.3053 0.2385 0.0456  0.0472  0.0748  122 VAL B C   
1755 O O   . VAL B 154 ? 0.2433 0.3006 0.2582 0.0804  0.0389  0.0735  122 VAL B O   
1756 C CB  . VAL B 154 ? 0.2566 0.2996 0.2134 -0.0071 0.0104  0.1007  122 VAL B CB  
1757 C CG1 . VAL B 154 ? 0.2928 0.3001 0.2391 -0.0056 0.0324  0.1003  122 VAL B CG1 
1758 C CG2 . VAL B 154 ? 0.2636 0.3044 0.2208 0.0060  -0.0045 0.0990  122 VAL B CG2 
1759 N N   . THR B 155 ? 0.2618 0.3159 0.2693 0.0532  0.0572  0.0627  123 THR B N   
1760 C CA  . THR B 155 ? 0.2852 0.3470 0.2936 0.0189  0.0726  0.0606  123 THR B CA  
1761 C C   . THR B 155 ? 0.2792 0.3511 0.3111 0.0148  0.0918  0.0698  123 THR B C   
1762 O O   . THR B 155 ? 0.2645 0.3093 0.3035 0.0223  0.0775  0.0326  123 THR B O   
1763 C CB  . THR B 155 ? 0.3546 0.3742 0.3240 -0.0064 0.0389  0.0617  123 THR B CB  
1764 O OG1 . THR B 155 ? 0.4160 0.3939 0.3462 0.0155  0.0091  0.0416  123 THR B OG1 
1765 C CG2 . THR B 155 ? 0.3593 0.3771 0.3205 -0.0333 0.0649  0.0932  123 THR B CG2 
1766 N N   . ASN B 156 ? 0.3356 0.3965 0.3482 -0.0114 0.1433  0.1076  124 ASN B N   
1767 C CA  . ASN B 156 ? 0.4226 0.4538 0.4060 -0.0354 0.1652  0.1209  124 ASN B CA  
1768 C C   . ASN B 156 ? 0.5774 0.5071 0.4439 -0.0370 0.1666  0.1290  124 ASN B C   
1769 O O   . ASN B 156 ? 0.5965 0.5078 0.4588 -0.0448 0.1707  0.1177  124 ASN B O   
1770 C CB  . ASN B 156 ? 0.4167 0.4705 0.4427 -0.0311 0.1397  0.1092  124 ASN B CB  
1771 C CG  . ASN B 156 ? 0.4148 0.4852 0.4723 -0.0120 0.1181  0.0972  124 ASN B CG  
1772 O OD1 . ASN B 156 ? 0.4157 0.4935 0.4849 -0.0002 0.1122  0.0854  124 ASN B OD1 
1773 N ND2 . ASN B 156 ? 0.4268 0.4922 0.4877 0.0081  0.0869  0.0931  124 ASN B ND2 
1774 N N   . PRO B 157 ? 0.7074 0.5535 0.4562 -0.0254 0.1565  0.1454  125 PRO B N   
1775 C CA  . PRO B 157 ? 0.7854 0.5782 0.4691 -0.0193 0.1557  0.1511  125 PRO B CA  
1776 C C   . PRO B 157 ? 0.8411 0.5941 0.4778 -0.0139 0.1476  0.1544  125 PRO B C   
1777 O O   . PRO B 157 ? 0.8748 0.6077 0.4846 -0.0133 0.1370  0.1549  125 PRO B O   
1778 C CB  . PRO B 157 ? 0.7880 0.5813 0.4692 -0.0195 0.1573  0.1499  125 PRO B CB  
1779 C CG  . PRO B 157 ? 0.7720 0.5786 0.4667 -0.0240 0.1557  0.1500  125 PRO B CG  
1780 C CD  . PRO B 157 ? 0.7484 0.5690 0.4598 -0.0230 0.1504  0.1487  125 PRO B CD  
1814 O O   . HOH F .   ? 0.1845 0.5885 0.6591 -0.0031 0.0447  -0.0874 301 HOH A O   
1815 O O   . HOH F .   ? 0.2377 0.2344 0.2743 0.0186  -0.0233 -0.0732 302 HOH A O   
1816 O O   . HOH F .   ? 1.0009 0.4086 0.3004 -0.2203 0.0656  -0.0164 303 HOH A O   
1817 O O   . HOH F .   ? 0.4435 0.6540 0.4374 0.1922  0.0129  -0.0208 304 HOH A O   
1818 O O   . HOH F .   ? 0.4695 0.3828 0.7585 -0.0125 0.1731  0.1549  305 HOH A O   
1819 O O   . HOH F .   ? 0.7258 0.5415 0.3408 -0.1888 0.0677  -0.1799 306 HOH A O   
1820 O O   . HOH F .   ? 0.3530 0.7848 0.7298 0.1030  0.0713  0.1011  307 HOH A O   
1821 O O   . HOH F .   ? 0.2370 0.2699 0.1833 -0.0170 -0.0193 0.0642  308 HOH A O   
1822 O O   . HOH F .   ? 0.8153 0.6198 0.4866 -0.0724 -0.2181 0.0893  309 HOH A O   
1823 O O   . HOH F .   ? 0.2857 0.2773 0.2550 0.0605  -0.0259 0.0128  310 HOH A O   
1824 O O   . HOH F .   ? 0.2731 0.2800 0.2412 -0.0303 -0.0391 -0.0489 311 HOH A O   
1825 O O   . HOH F .   ? 0.1638 0.1856 0.1060 0.0231  0.0142  0.0059  312 HOH A O   
1826 O O   . HOH F .   ? 0.2742 0.1968 0.3552 0.0245  0.0882  -0.0164 313 HOH A O   
1827 O O   . HOH F .   ? 0.4271 0.5878 0.5388 -0.0588 -0.0030 -0.0168 314 HOH A O   
1828 O O   . HOH F .   ? 0.2445 0.1954 0.1362 -0.0441 -0.0384 0.0379  315 HOH A O   
1829 O O   . HOH F .   ? 0.3651 0.3729 0.6242 0.0217  -0.0173 -0.0264 316 HOH A O   
1830 O O   . HOH F .   ? 0.3557 0.8382 0.3882 -0.0673 0.1405  0.0310  317 HOH A O   
1831 O O   . HOH F .   ? 0.3560 0.4305 0.4199 -0.0841 0.0790  0.0024  318 HOH A O   
1832 O O   . HOH F .   ? 0.8114 0.3453 0.5573 -0.0905 0.0972  0.1185  319 HOH A O   
1833 O O   . HOH F .   ? 0.3869 0.2678 0.4532 0.0824  0.0671  0.0823  320 HOH A O   
1834 O O   . HOH F .   ? 0.5524 0.4283 0.5471 -0.1264 0.2832  -0.1426 321 HOH A O   
1835 O O   . HOH F .   ? 0.3675 0.5763 0.3480 0.1113  0.0269  -0.2152 322 HOH A O   
1836 O O   . HOH F .   ? 0.2937 0.2054 0.2075 -0.0204 0.0603  -0.0624 323 HOH A O   
1837 O O   . HOH F .   ? 0.2122 0.2811 0.1989 -0.0001 0.0178  -0.0066 324 HOH A O   
1838 O O   . HOH F .   ? 0.8278 0.4537 0.4290 -0.1528 0.1189  -0.1168 325 HOH A O   
1839 O O   . HOH F .   ? 0.5855 0.6500 0.4414 0.0963  0.0695  0.0286  326 HOH A O   
1840 O O   . HOH F .   ? 0.2447 0.4162 0.7805 0.0679  0.0763  0.0988  327 HOH A O   
1841 O O   . HOH F .   ? 0.4467 0.2812 0.5137 -0.0155 0.0584  -0.1401 328 HOH A O   
1842 O O   . HOH F .   ? 0.6632 0.6518 0.5107 0.0066  -0.0687 0.0104  329 HOH A O   
1843 O O   . HOH F .   ? 0.2063 0.1571 0.1661 0.0309  -0.0103 -0.0059 330 HOH A O   
1844 O O   . HOH F .   ? 0.3028 0.5330 0.6027 0.1536  0.0423  0.1786  331 HOH A O   
1845 O O   . HOH F .   ? 0.7309 0.4249 0.5933 -0.0462 -0.0847 0.2688  332 HOH A O   
1846 O O   . HOH F .   ? 0.2695 0.4774 0.5117 0.0443  0.1449  0.0233  333 HOH A O   
1847 O O   . HOH F .   ? 0.3121 0.3146 0.1415 0.0194  0.0306  -0.0306 334 HOH A O   
1848 O O   . HOH F .   ? 0.3007 0.2846 0.3989 0.0058  0.0285  -0.0342 335 HOH A O   
1849 O O   . HOH F .   ? 0.3959 0.2134 0.5785 -0.0091 0.1155  -0.0878 336 HOH A O   
1850 O O   . HOH F .   ? 0.3241 0.3368 0.1779 0.0482  -0.0139 0.0056  337 HOH A O   
1851 O O   . HOH F .   ? 0.5675 0.3886 0.2538 -0.0853 -0.1094 0.0947  338 HOH A O   
1852 O O   . HOH F .   ? 0.7457 0.5837 0.5506 0.1317  0.0952  0.1009  339 HOH A O   
1853 O O   . HOH F .   ? 0.2463 0.1865 0.1721 -0.0078 0.0315  -0.0122 340 HOH A O   
1854 O O   . HOH F .   ? 0.1458 0.1824 0.1337 -0.0002 -0.0014 -0.0003 341 HOH A O   
1855 O O   . HOH F .   ? 0.6085 0.2671 0.2805 -0.0020 0.0660  -0.0604 342 HOH A O   
1856 O O   . HOH F .   ? 0.3820 0.7543 0.4101 -0.1756 0.0272  -0.0064 343 HOH A O   
1857 O O   . HOH F .   ? 0.9316 0.3665 0.4663 -0.1212 -0.1406 0.0121  344 HOH A O   
1858 O O   . HOH F .   ? 0.4888 0.4264 0.3230 0.0305  -0.0699 0.1506  345 HOH A O   
1859 O O   . HOH F .   ? 0.5578 0.4630 0.5505 -0.1874 0.1156  -0.0462 346 HOH A O   
1860 O O   . HOH F .   ? 0.3224 0.3021 0.5336 0.0002  0.0505  -0.1157 347 HOH A O   
1861 O O   . HOH F .   ? 0.2525 0.4187 0.5480 -0.0742 -0.0307 -0.0111 348 HOH A O   
1862 O O   . HOH F .   ? 0.2733 0.2905 0.2158 0.0064  0.0209  0.0077  349 HOH A O   
1863 O O   . HOH F .   ? 0.3223 0.2324 0.2485 0.0226  -0.0175 -0.0409 350 HOH A O   
1864 O O   . HOH F .   ? 0.2236 0.3221 0.2799 0.0765  -0.0410 -0.0602 351 HOH A O   
1865 O O   . HOH F .   ? 0.5627 0.5984 0.4906 0.0921  -0.1569 0.2211  352 HOH A O   
1866 O O   . HOH F .   ? 0.2667 0.4271 0.1882 0.0289  -0.0653 0.0125  353 HOH A O   
1867 O O   . HOH F .   ? 0.5307 0.2985 0.2660 0.1141  0.0849  -0.0551 354 HOH A O   
1868 O O   . HOH F .   ? 0.2376 0.3216 0.2607 0.0028  -0.0027 -0.0055 355 HOH A O   
1869 O O   . HOH F .   ? 0.4890 0.2431 0.3869 0.0009  0.0000  0.0000  356 HOH A O   
1870 O O   . HOH F .   ? 0.5022 0.6483 0.2518 0.2357  0.0972  0.0286  357 HOH A O   
1871 O O   . HOH F .   ? 0.6570 0.4264 0.5588 0.0896  0.3294  0.1569  358 HOH A O   
1872 O O   . HOH F .   ? 0.4483 0.7684 0.4807 0.1312  -0.0488 -0.2796 359 HOH A O   
1873 O O   . HOH F .   ? 0.3913 0.2638 0.2082 0.0316  0.0623  0.0081  360 HOH A O   
1874 O O   . HOH F .   ? 0.2821 0.6524 0.3371 -0.1019 -0.0699 0.2087  361 HOH A O   
1875 O O   . HOH F .   ? 0.2282 0.3084 0.4137 0.0118  -0.0145 -0.2080 362 HOH A O   
1876 O O   . HOH F .   ? 0.5498 0.5704 0.3284 0.1394  -0.1656 -0.1823 363 HOH A O   
1877 O O   . HOH F .   ? 0.5062 0.6386 0.8987 0.3352  -0.0309 0.0229  364 HOH A O   
1878 O O   . HOH F .   ? 0.4031 0.4119 0.6605 0.0403  0.1515  0.0063  365 HOH A O   
1879 O O   . HOH F .   ? 0.3560 1.0352 0.5885 -0.1089 -0.0400 0.1851  366 HOH A O   
1880 O O   . HOH F .   ? 0.2542 0.8674 0.6081 0.1110  -0.0394 -0.0840 367 HOH A O   
1881 O O   . HOH F .   ? 0.7565 0.6064 0.5289 -0.2199 0.0096  0.1588  368 HOH A O   
1882 O O   . HOH F .   ? 0.4382 0.5627 0.4114 -0.1377 0.0995  -0.0775 369 HOH A O   
1883 O O   . HOH F .   ? 0.6629 0.6617 0.5412 0.0190  0.0160  0.0408  370 HOH A O   
1884 O O   . HOH F .   ? 0.5779 0.7976 0.5145 -0.0887 -0.1084 -0.0385 371 HOH A O   
1885 O O   . HOH F .   ? 0.5283 0.2875 0.7719 0.1502  -0.0671 0.0766  372 HOH A O   
1886 O O   . HOH F .   ? 0.6612 0.3684 0.3076 -0.2436 0.0119  -0.0311 373 HOH A O   
1887 O O   . HOH F .   ? 0.4265 0.4077 0.4642 -0.0823 -0.0886 0.0045  374 HOH A O   
1888 O O   . HOH F .   ? 0.6129 0.3066 0.5783 0.1200  0.3129  0.1460  375 HOH A O   
1889 O O   . HOH F .   ? 0.5435 0.5618 0.5424 -0.2631 -0.1484 0.2606  376 HOH A O   
1890 O O   . HOH F .   ? 0.6522 0.6551 0.4500 -0.1237 -0.1170 -0.0657 377 HOH A O   
1891 O O   . HOH F .   ? 0.3940 0.2940 0.6592 -0.0107 0.0782  -0.0471 378 HOH A O   
1892 O O   . HOH F .   ? 0.9005 0.6113 0.3455 0.0768  0.1727  -0.0143 379 HOH A O   
1893 O O   . HOH F .   ? 0.6238 0.3654 0.7742 -0.1710 -0.2176 0.0463  380 HOH A O   
1894 O O   . HOH F .   ? 1.2557 0.4858 0.3618 -0.2406 0.0760  -0.0309 381 HOH A O   
1895 O O   . HOH F .   ? 0.3642 0.3079 0.3038 0.0348  0.0674  0.0636  382 HOH A O   
1896 O O   . HOH F .   ? 0.5709 0.3280 0.3720 -0.1248 -0.0440 -0.0132 383 HOH A O   
1897 O O   . HOH F .   ? 0.4894 0.7775 0.5593 -0.0713 -0.1182 0.0492  384 HOH A O   
1898 O O   . HOH F .   ? 0.5099 0.5301 0.4398 0.2348  0.1764  -0.0147 385 HOH A O   
1899 O O   . HOH F .   ? 0.4260 0.4900 0.7184 -0.1366 0.0907  -0.2714 386 HOH A O   
1900 O O   . HOH F .   ? 0.6075 0.5915 0.5282 -0.0990 -0.0781 -0.0590 387 HOH A O   
1901 O O   . HOH F .   ? 0.5257 0.6338 0.5564 -0.0192 0.1211  -0.0617 388 HOH A O   
1902 O O   . HOH F .   ? 0.2892 0.4165 0.5261 -0.0706 0.1246  -0.0566 389 HOH A O   
1903 O O   . HOH F .   ? 0.4632 0.4002 0.4877 0.1397  0.1541  0.1012  390 HOH A O   
1904 O O   . HOH F .   ? 0.3930 0.4977 0.4415 -0.1855 -0.1347 -0.0215 391 HOH A O   
1905 O O   . HOH F .   ? 0.6792 0.6301 0.5550 -0.0043 -0.0194 0.0983  392 HOH A O   
1906 O O   . HOH F .   ? 0.7068 0.3523 0.5321 0.1905  0.2597  0.1085  393 HOH A O   
1907 O O   . HOH F .   ? 0.4640 0.4429 0.8759 -0.1014 -0.1774 0.0580  394 HOH A O   
1908 O O   . HOH F .   ? 0.6128 0.6546 0.5243 -0.0094 -0.0190 -0.0124 395 HOH A O   
1909 O O   . HOH F .   ? 0.3256 0.5816 0.5725 0.0459  0.0895  0.2026  396 HOH A O   
1910 O O   . HOH F .   ? 0.5692 0.4033 0.9344 -0.1659 0.2168  -0.0997 397 HOH A O   
1911 O O   . HOH F .   ? 0.6429 0.8061 0.5567 0.0627  -0.0870 0.2929  398 HOH A O   
1912 O O   . HOH F .   ? 0.6903 0.7263 0.5352 0.2482  -0.1270 -0.0298 399 HOH A O   
1913 O O   . HOH F .   ? 0.7134 0.4135 0.7470 0.0720  -0.0559 0.2600  400 HOH A O   
1914 O O   . HOH F .   ? 0.8230 0.4765 0.7341 -0.1455 0.0139  0.1479  401 HOH A O   
1915 O O   . HOH F .   ? 0.7001 0.6158 0.6976 0.2656  0.1741  0.3204  402 HOH A O   
1916 O O   . HOH F .   ? 0.6166 0.7193 0.5568 -0.0793 -0.0989 0.0418  403 HOH A O   
1917 O O   . HOH F .   ? 0.5631 0.6439 0.5308 0.2818  0.0564  0.1097  404 HOH A O   
1918 O O   . HOH F .   ? 0.4779 0.6072 0.4617 -0.1488 -0.1639 -0.1165 405 HOH A O   
1919 O O   . HOH G .   ? 0.3112 0.4451 0.8004 0.0205  0.0278  0.3282  301 HOH B O   
1920 O O   . HOH G .   ? 0.4257 0.8756 0.3324 0.0630  -0.1493 -0.0332 302 HOH B O   
1921 O O   . HOH G .   ? 0.4160 0.5352 0.9271 0.0376  -0.0097 -0.3106 303 HOH B O   
1922 O O   . HOH G .   ? 0.6514 0.4413 0.5900 0.0926  -0.0604 0.2779  304 HOH B O   
1923 O O   . HOH G .   ? 0.6056 0.6133 0.5271 0.0193  -0.0090 0.0241  305 HOH B O   
1924 O O   . HOH G .   ? 0.4558 0.6945 0.4045 0.2807  0.1123  0.2275  306 HOH B O   
1925 O O   . HOH G .   ? 0.2882 0.6306 0.3762 0.0844  0.0227  0.2631  307 HOH B O   
1926 O O   . HOH G .   ? 0.2457 0.2082 0.1506 0.0321  -0.0140 -0.0484 308 HOH B O   
1927 O O   . HOH G .   ? 0.4905 0.3541 0.3825 0.0630  0.0775  0.0875  309 HOH B O   
1928 O O   . HOH G .   ? 0.5106 0.6243 0.8194 -0.2350 0.1300  0.1591  310 HOH B O   
1929 O O   . HOH G .   ? 0.6791 0.5567 0.5026 -0.1289 0.0040  0.2000  311 HOH B O   
1930 O O   . HOH G .   ? 0.4756 0.6851 0.4360 0.0870  -0.0646 -0.0334 312 HOH B O   
1931 O O   . HOH G .   ? 0.3342 0.3517 0.3290 -0.0557 -0.0145 0.1848  313 HOH B O   
1932 O O   . HOH G .   ? 0.2448 0.4452 0.3315 0.0037  -0.0708 0.0877  314 HOH B O   
1933 O O   . HOH G .   ? 0.5580 0.7177 0.2603 -0.0098 0.0745  0.0498  315 HOH B O   
1934 O O   . HOH G .   ? 1.1695 0.3205 0.4288 0.0299  -0.0038 0.0603  316 HOH B O   
1935 O O   . HOH G .   ? 0.3991 0.2164 0.1994 0.0641  0.0455  0.0471  317 HOH B O   
1936 O O   . HOH G .   ? 0.2764 0.1608 0.3265 -0.0058 -0.0335 -0.0279 318 HOH B O   
1937 O O   . HOH G .   ? 0.4801 0.5893 0.7479 -0.2550 -0.1978 0.2550  319 HOH B O   
1938 O O   . HOH G .   ? 0.4267 0.4390 0.1817 0.2206  0.0301  0.0589  320 HOH B O   
1939 O O   . HOH G .   ? 0.3249 0.2175 0.3164 -0.0187 0.0975  0.0334  321 HOH B O   
1940 O O   . HOH G .   ? 0.2210 0.1445 0.1586 -0.0246 -0.0065 -0.0027 322 HOH B O   
1941 O O   . HOH G .   ? 0.1863 0.1901 0.1024 -0.0196 0.0080  0.0071  323 HOH B O   
1942 O O   . HOH G .   ? 0.3272 0.6304 0.6591 0.1174  0.1956  0.2165  324 HOH B O   
1943 O O   . HOH G .   ? 0.4502 0.3268 0.5388 -0.1473 0.2346  -0.1616 325 HOH B O   
1944 O O   . HOH G .   ? 0.3138 0.6693 0.3974 0.0027  -0.0552 0.0336  326 HOH B O   
1945 O O   . HOH G .   ? 0.5926 0.5835 0.6186 -0.2102 0.1892  0.1967  327 HOH B O   
1946 O O   . HOH G .   ? 0.3624 0.3515 0.3772 -0.0875 0.0835  -0.0543 328 HOH B O   
1947 O O   . HOH G .   ? 0.4257 0.5823 0.6577 0.2101  0.1502  0.2468  329 HOH B O   
1948 O O   . HOH G .   ? 0.4306 0.3820 0.2255 0.0182  -0.0126 0.0438  330 HOH B O   
1949 O O   . HOH G .   ? 0.2435 0.2439 0.2517 -0.0458 0.0212  -0.0029 331 HOH B O   
1950 O O   . HOH G .   ? 0.2176 0.1919 0.1183 0.0434  -0.0276 -0.0486 332 HOH B O   
1951 O O   . HOH G .   ? 0.4314 0.5209 0.5407 0.1270  -0.1064 -0.2902 333 HOH B O   
1952 O O   . HOH G .   ? 0.4947 0.8317 0.5766 0.0307  -0.0098 0.4000  334 HOH B O   
1953 O O   . HOH G .   ? 0.3679 0.3418 0.2252 -0.0452 -0.0309 -0.0209 335 HOH B O   
1954 O O   . HOH G .   ? 0.3594 0.4109 0.6802 0.1817  -0.1016 -0.0042 336 HOH B O   
1955 O O   . HOH G .   ? 0.1911 0.6053 0.3449 0.0712  0.0057  -0.0444 337 HOH B O   
1956 O O   . HOH G .   ? 0.7628 0.4116 0.6309 -0.0541 0.0957  0.2534  338 HOH B O   
1957 O O   . HOH G .   ? 0.3132 0.3588 0.2615 0.0608  0.0230  0.0495  339 HOH B O   
1958 O O   . HOH G .   ? 0.2310 0.2606 0.1917 -0.0203 0.0055  0.0074  340 HOH B O   
1959 O O   . HOH G .   ? 0.1885 0.2612 0.2095 0.0287  -0.0352 0.0051  341 HOH B O   
1960 O O   . HOH G .   ? 0.4760 0.2898 0.2899 -0.0529 0.0030  -0.0716 342 HOH B O   
1961 O O   . HOH G .   ? 0.6032 0.4313 0.6364 -0.2199 -0.2286 0.1051  343 HOH B O   
1962 O O   . HOH G .   ? 0.3633 0.2896 0.2853 0.0170  -0.0551 0.0417  344 HOH B O   
1963 O O   . HOH G .   ? 0.1988 0.3476 0.4890 0.0217  -0.0301 0.0023  345 HOH B O   
1964 O O   . HOH G .   ? 0.1890 0.2289 0.1551 0.0037  0.0094  0.0002  346 HOH B O   
1965 O O   . HOH G .   ? 0.6740 0.7226 0.5572 0.3310  0.1811  -0.0611 347 HOH B O   
1966 O O   . HOH G .   ? 0.5836 0.4976 1.1714 0.2153  0.0402  -0.1319 348 HOH B O   
1967 O O   . HOH G .   ? 0.5383 0.6236 0.7287 0.1715  0.1918  0.2335  349 HOH B O   
1968 O O   . HOH G .   ? 0.1987 0.3310 0.2136 0.0126  0.0068  0.0051  350 HOH B O   
1969 O O   . HOH G .   ? 0.3889 0.2804 0.2532 0.0518  0.0155  0.0320  351 HOH B O   
1970 O O   . HOH G .   ? 0.2534 0.3021 0.3386 -0.0145 -0.0556 0.1716  352 HOH B O   
1971 O O   . HOH G .   ? 0.5106 0.3626 0.2208 -0.1488 -0.0056 0.0493  353 HOH B O   
1972 O O   . HOH G .   ? 0.5560 0.6309 0.5415 -0.0174 -0.0167 0.0120  354 HOH B O   
1973 O O   . HOH G .   ? 0.3118 0.4730 0.4344 -0.0611 -0.0278 0.2303  355 HOH B O   
1974 O O   . HOH G .   ? 0.6614 0.3974 0.7213 -0.2359 0.1455  -0.0496 356 HOH B O   
1975 O O   . HOH G .   ? 0.2631 0.5237 0.2262 0.0035  -0.0345 -0.0532 357 HOH B O   
1976 O O   . HOH G .   ? 0.7311 0.5523 0.6818 0.2166  0.3283  0.2951  358 HOH B O   
1977 O O   . HOH G .   ? 0.2259 0.6872 0.2713 0.0024  -0.0380 -0.1106 359 HOH B O   
1978 O O   . HOH G .   ? 0.5670 0.5431 0.4261 0.1290  0.2647  -0.0026 360 HOH B O   
1979 O O   . HOH G .   ? 0.5080 0.5267 0.2822 -0.1784 -0.1017 0.1716  361 HOH B O   
1980 O O   . HOH G .   ? 0.6575 0.7944 0.4039 -0.3348 -0.0009 0.1733  362 HOH B O   
1981 O O   . HOH G .   ? 0.6306 0.4209 0.1882 0.0925  0.0083  -0.0204 363 HOH B O   
1982 O O   . HOH G .   ? 0.6275 0.4566 0.5172 -0.1235 0.0031  -0.2258 364 HOH B O   
1983 O O   . HOH G .   ? 0.3340 0.3552 0.1589 -0.0055 -0.0560 0.0669  365 HOH B O   
1984 O O   . HOH G .   ? 0.3889 0.4157 0.2714 0.0129  -0.1142 0.0696  366 HOH B O   
1985 O O   . HOH G .   ? 0.6068 0.8315 0.4822 -0.1606 0.1084  0.2695  367 HOH B O   
1986 O O   . HOH G .   ? 0.2474 0.3042 0.3150 -0.0841 -0.0621 0.0679  368 HOH B O   
1987 O O   . HOH G .   ? 0.3469 0.2870 0.3320 -0.0557 -0.0812 0.0798  369 HOH B O   
1988 O O   . HOH G .   ? 0.3478 0.5013 0.9103 -0.1099 -0.0236 -0.2431 370 HOH B O   
1989 O O   . HOH G .   ? 0.2654 0.3270 0.4186 0.0173  0.0000  0.0000  371 HOH B O   
1990 O O   . HOH G .   ? 0.4939 0.8814 0.2710 0.2137  -0.0244 -0.0645 372 HOH B O   
1991 O O   . HOH G .   ? 0.4284 0.4552 0.5317 0.0195  0.0644  -0.0162 373 HOH B O   
1992 O O   . HOH G .   ? 0.6330 0.6281 0.5089 0.0007  0.0635  -0.1525 374 HOH B O   
1993 O O   . HOH G .   ? 0.4790 0.6367 0.9394 -0.0369 0.0648  -0.0948 375 HOH B O   
1994 O O   . HOH G .   ? 0.3316 0.8877 0.5854 -0.1485 -0.0506 0.2246  376 HOH B O   
1995 O O   . HOH G .   ? 0.5931 0.4323 0.4904 0.1108  0.2037  0.0999  377 HOH B O   
1996 O O   . HOH G .   ? 0.7175 0.6532 0.4962 0.3173  -0.0393 0.0564  378 HOH B O   
1997 O O   . HOH G .   ? 0.7605 0.6763 0.8792 0.2313  0.1117  0.4064  379 HOH B O   
1998 O O   . HOH G .   ? 0.5621 0.6389 0.4899 -0.0055 -0.0715 -0.0712 380 HOH B O   
1999 O O   . HOH G .   ? 0.5792 0.6882 0.5123 -0.1095 -0.0540 0.0327  381 HOH B O   
2000 O O   . HOH G .   ? 0.5773 0.5080 0.3843 -0.0871 0.0399  -0.0987 382 HOH B O   
2001 O O   . HOH G .   ? 0.8077 0.7612 0.4660 0.0796  -0.2372 0.0543  383 HOH B O   
2002 O O   . HOH G .   ? 0.9633 0.4043 0.4788 -0.0921 0.2825  -0.0031 384 HOH B O   
2003 O O   . HOH G .   ? 0.6549 0.3994 0.2705 0.0337  -0.0810 -0.0690 385 HOH B O   
2004 O O   . HOH G .   ? 0.6425 0.7423 0.5442 0.1392  0.0235  0.1473  386 HOH B O   
2005 O O   . HOH G .   ? 0.1192 0.2120 0.1256 0.0013  -0.0001 -0.0039 387 HOH B O   
2006 O O   . HOH G .   ? 0.9649 0.5986 0.6059 0.1275  -0.0581 0.2372  388 HOH B O   
2007 O O   . HOH G .   ? 0.6308 0.6188 0.5428 0.0049  0.0310  0.0343  389 HOH B O   
2008 O O   . HOH G .   ? 0.4581 0.6204 0.7495 0.1134  0.1165  0.3084  390 HOH B O   
2009 O O   . HOH G .   ? 0.8890 0.5865 0.5538 0.2875  -0.1911 -0.2345 391 HOH B O   
2010 O O   . HOH G .   ? 0.5413 0.6069 0.5388 0.0345  -0.0542 0.1690  392 HOH B O   
2011 O O   . HOH G .   ? 0.3659 0.7584 0.4447 -0.2071 -0.1498 0.1054  393 HOH B O   
2012 O O   . HOH G .   ? 0.4519 0.7868 0.4399 -0.0717 -0.0127 0.0818  394 HOH B O   
2013 O O   . HOH G .   ? 0.2110 0.2028 0.2336 0.0278  -0.0149 0.0049  395 HOH B O   
2014 O O   . HOH G .   ? 0.1450 0.2619 0.2637 -0.0085 -0.0047 -0.1060 396 HOH B O   
2015 O O   . HOH G .   ? 0.2796 0.2507 0.2857 0.0182  0.0467  -0.0233 397 HOH B O   
2016 O O   . HOH G .   ? 0.6904 0.6459 0.3926 0.1291  0.0862  0.0282  398 HOH B O   
2017 O O   . HOH G .   ? 0.4358 0.5873 0.5445 -0.0970 -0.0827 -0.0803 399 HOH B O   
2018 O O   . HOH G .   ? 0.3903 0.4156 0.4183 0.0942  0.1260  0.2235  400 HOH B O   
2019 O O   . HOH G .   ? 0.3751 0.5440 0.7261 0.0177  0.1339  0.0854  401 HOH B O   
2020 O O   . HOH G .   ? 0.5631 0.5707 0.6913 0.0985  -0.2024 0.0938  402 HOH B O   
2021 O O   . HOH G .   ? 0.2213 0.4188 0.2443 -0.0327 0.0133  0.1000  403 HOH B O   
2022 O O   . HOH G .   ? 0.5635 0.6458 0.5605 -0.0839 -0.0525 0.2018  404 HOH B O   
2023 O O   . HOH G .   ? 0.4522 0.5143 0.4792 0.1784  -0.1963 -0.0088 405 HOH B O   
2024 O O   . HOH G .   ? 0.5375 0.3215 1.0234 -0.0510 -0.2716 0.1441  406 HOH B O   
2025 O O   . HOH G .   ? 0.4669 0.5539 0.4526 -0.1107 0.2349  -0.1442 407 HOH B O   
2026 O O   . HOH G .   ? 0.4490 0.4323 0.5262 -0.1937 0.0988  -0.1227 408 HOH B O   
2027 O O   . HOH G .   ? 0.4674 0.5667 0.5873 0.1002  -0.0230 0.2573  409 HOH B O   
2028 O O   . HOH G .   ? 0.6448 0.6152 0.4747 0.0304  0.0246  -0.0319 410 HOH B O   
2029 O O   . HOH G .   ? 0.6768 0.8057 0.3389 0.2526  -0.1146 0.0793  411 HOH B O   
2030 O O   . HOH G .   ? 0.6678 0.6173 0.4293 -0.0251 -0.0174 -0.0230 412 HOH B O   
2031 O O   . HOH G .   ? 0.3946 0.7026 0.3921 0.1454  -0.0655 -0.0820 413 HOH B O   
2032 O O   . HOH G .   ? 0.6195 0.4923 0.5204 -0.1371 0.0653  -0.1730 414 HOH B O   
2033 O O   . HOH G .   ? 0.5989 0.7016 0.5636 -0.0300 0.0002  0.0345  415 HOH B O   
2034 O O   . HOH G .   ? 0.6950 0.5993 0.5015 0.0958  0.0568  -0.1067 416 HOH B O   
# 
