data_9JIS
# 
_entry.id   9JIS 
# 
_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   9JIS         pdb_00009jis 10.2210/pdb9jis/pdb 
WWPDB D_1300051391 ?            ?                   
# 
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                        9JIS 
_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 Aclonifen     264.664   2   ? ?    ? ? 
3 non-polymer syn 'SODIUM ION'  22.990    1   ? ?    ? ? 
4 water       nat water         18.015    204 ? ?    ? ? 
# 
_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 Aclonifen    A1L38 
3 'SODIUM ION' NA    
4 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 
A1L38 non-polymer         . Aclonifen       '2-chloranyl-6-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]-3-phenoxy-aniline' 
'C12 H9 Cl N2 O3' 264.664 
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 
NA    non-polymer         . 'SODIUM ION'    ?                                                                         'Na 1' 
22.990  
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        A1L38 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L38 
_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 A1L38 1   201 201 A1L38 DRG A . 
D 3 NA    1   202 1   NA    NA  A . 
E 2 A1L38 1   201 201 A1L38 DRG B . 
F 4 HOH   1   301 200 HOH   HOH A . 
F 4 HOH   2   302 96  HOH   HOH A . 
F 4 HOH   3   303 166 HOH   HOH A . 
F 4 HOH   4   304 15  HOH   HOH A . 
F 4 HOH   5   305 37  HOH   HOH A . 
F 4 HOH   6   306 146 HOH   HOH A . 
F 4 HOH   7   307 97  HOH   HOH A . 
F 4 HOH   8   308 188 HOH   HOH A . 
F 4 HOH   9   309 194 HOH   HOH A . 
F 4 HOH   10  310 152 HOH   HOH A . 
F 4 HOH   11  311 73  HOH   HOH A . 
F 4 HOH   12  312 21  HOH   HOH A . 
F 4 HOH   13  313 118 HOH   HOH A . 
F 4 HOH   14  314 29  HOH   HOH A . 
F 4 HOH   15  315 199 HOH   HOH A . 
F 4 HOH   16  316 1   HOH   HOH A . 
F 4 HOH   17  317 203 HOH   HOH A . 
F 4 HOH   18  318 22  HOH   HOH A . 
F 4 HOH   19  319 16  HOH   HOH A . 
F 4 HOH   20  320 42  HOH   HOH A . 
F 4 HOH   21  321 123 HOH   HOH A . 
F 4 HOH   22  322 50  HOH   HOH A . 
F 4 HOH   23  323 41  HOH   HOH A . 
F 4 HOH   24  324 201 HOH   HOH A . 
F 4 HOH   25  325 19  HOH   HOH A . 
F 4 HOH   26  326 76  HOH   HOH A . 
F 4 HOH   27  327 17  HOH   HOH A . 
F 4 HOH   28  328 9   HOH   HOH A . 
F 4 HOH   29  329 4   HOH   HOH A . 
F 4 HOH   30  330 91  HOH   HOH A . 
F 4 HOH   31  331 142 HOH   HOH A . 
F 4 HOH   32  332 106 HOH   HOH A . 
F 4 HOH   33  333 52  HOH   HOH A . 
F 4 HOH   34  334 54  HOH   HOH A . 
F 4 HOH   35  335 40  HOH   HOH A . 
F 4 HOH   36  336 39  HOH   HOH A . 
F 4 HOH   37  337 111 HOH   HOH A . 
F 4 HOH   38  338 80  HOH   HOH A . 
F 4 HOH   39  339 93  HOH   HOH A . 
F 4 HOH   40  340 87  HOH   HOH A . 
F 4 HOH   41  341 5   HOH   HOH A . 
F 4 HOH   42  342 157 HOH   HOH A . 
F 4 HOH   43  343 58  HOH   HOH A . 
F 4 HOH   44  344 6   HOH   HOH A . 
F 4 HOH   45  345 130 HOH   HOH A . 
F 4 HOH   46  346 150 HOH   HOH A . 
F 4 HOH   47  347 191 HOH   HOH A . 
F 4 HOH   48  348 49  HOH   HOH A . 
F 4 HOH   49  349 57  HOH   HOH A . 
F 4 HOH   50  350 12  HOH   HOH A . 
F 4 HOH   51  351 197 HOH   HOH A . 
F 4 HOH   52  352 64  HOH   HOH A . 
F 4 HOH   53  353 24  HOH   HOH A . 
F 4 HOH   54  354 163 HOH   HOH A . 
F 4 HOH   55  355 47  HOH   HOH A . 
F 4 HOH   56  356 131 HOH   HOH A . 
F 4 HOH   57  357 181 HOH   HOH A . 
F 4 HOH   58  358 30  HOH   HOH A . 
F 4 HOH   59  359 151 HOH   HOH A . 
F 4 HOH   60  360 112 HOH   HOH A . 
F 4 HOH   61  361 56  HOH   HOH A . 
F 4 HOH   62  362 204 HOH   HOH A . 
F 4 HOH   63  363 55  HOH   HOH A . 
F 4 HOH   64  364 104 HOH   HOH A . 
F 4 HOH   65  365 72  HOH   HOH A . 
F 4 HOH   66  366 174 HOH   HOH A . 
F 4 HOH   67  367 59  HOH   HOH A . 
F 4 HOH   68  368 98  HOH   HOH A . 
F 4 HOH   69  369 89  HOH   HOH A . 
F 4 HOH   70  370 133 HOH   HOH A . 
F 4 HOH   71  371 61  HOH   HOH A . 
F 4 HOH   72  372 137 HOH   HOH A . 
F 4 HOH   73  373 187 HOH   HOH A . 
F 4 HOH   74  374 160 HOH   HOH A . 
F 4 HOH   75  375 83  HOH   HOH A . 
F 4 HOH   76  376 101 HOH   HOH A . 
F 4 HOH   77  377 177 HOH   HOH A . 
F 4 HOH   78  378 100 HOH   HOH A . 
F 4 HOH   79  379 156 HOH   HOH A . 
F 4 HOH   80  380 153 HOH   HOH A . 
F 4 HOH   81  381 185 HOH   HOH A . 
F 4 HOH   82  382 148 HOH   HOH A . 
F 4 HOH   83  383 69  HOH   HOH A . 
F 4 HOH   84  384 167 HOH   HOH A . 
F 4 HOH   85  385 155 HOH   HOH A . 
F 4 HOH   86  386 36  HOH   HOH A . 
F 4 HOH   87  387 205 HOH   HOH A . 
F 4 HOH   88  388 94  HOH   HOH A . 
F 4 HOH   89  389 125 HOH   HOH A . 
F 4 HOH   90  390 71  HOH   HOH A . 
F 4 HOH   91  391 196 HOH   HOH A . 
F 4 HOH   92  392 171 HOH   HOH A . 
F 4 HOH   93  393 144 HOH   HOH A . 
F 4 HOH   94  394 175 HOH   HOH A . 
F 4 HOH   95  395 169 HOH   HOH A . 
F 4 HOH   96  396 129 HOH   HOH A . 
F 4 HOH   97  397 139 HOH   HOH A . 
F 4 HOH   98  398 135 HOH   HOH A . 
F 4 HOH   99  399 172 HOH   HOH A . 
F 4 HOH   100 400 86  HOH   HOH A . 
F 4 HOH   101 401 180 HOH   HOH A . 
F 4 HOH   102 402 121 HOH   HOH A . 
G 4 HOH   1   301 168 HOH   HOH B . 
G 4 HOH   2   302 202 HOH   HOH B . 
G 4 HOH   3   303 143 HOH   HOH B . 
G 4 HOH   4   304 173 HOH   HOH B . 
G 4 HOH   5   305 38  HOH   HOH B . 
G 4 HOH   6   306 102 HOH   HOH B . 
G 4 HOH   7   307 99  HOH   HOH B . 
G 4 HOH   8   308 48  HOH   HOH B . 
G 4 HOH   9   309 136 HOH   HOH B . 
G 4 HOH   10  310 164 HOH   HOH B . 
G 4 HOH   11  311 13  HOH   HOH B . 
G 4 HOH   12  312 145 HOH   HOH B . 
G 4 HOH   13  313 75  HOH   HOH B . 
G 4 HOH   14  314 27  HOH   HOH B . 
G 4 HOH   15  315 51  HOH   HOH B . 
G 4 HOH   16  316 158 HOH   HOH B . 
G 4 HOH   17  317 14  HOH   HOH B . 
G 4 HOH   18  318 105 HOH   HOH B . 
G 4 HOH   19  319 68  HOH   HOH B . 
G 4 HOH   20  320 138 HOH   HOH B . 
G 4 HOH   21  321 182 HOH   HOH B . 
G 4 HOH   22  322 120 HOH   HOH B . 
G 4 HOH   23  323 2   HOH   HOH B . 
G 4 HOH   24  324 183 HOH   HOH B . 
G 4 HOH   25  325 65  HOH   HOH B . 
G 4 HOH   26  326 26  HOH   HOH B . 
G 4 HOH   27  327 7   HOH   HOH B . 
G 4 HOH   28  328 62  HOH   HOH B . 
G 4 HOH   29  329 113 HOH   HOH B . 
G 4 HOH   30  330 44  HOH   HOH B . 
G 4 HOH   31  331 8   HOH   HOH B . 
G 4 HOH   32  332 90  HOH   HOH B . 
G 4 HOH   33  333 34  HOH   HOH B . 
G 4 HOH   34  334 108 HOH   HOH B . 
G 4 HOH   35  335 84  HOH   HOH B . 
G 4 HOH   36  336 115 HOH   HOH B . 
G 4 HOH   37  337 28  HOH   HOH B . 
G 4 HOH   38  338 192 HOH   HOH B . 
G 4 HOH   39  339 10  HOH   HOH B . 
G 4 HOH   40  340 176 HOH   HOH B . 
G 4 HOH   41  341 66  HOH   HOH B . 
G 4 HOH   42  342 20  HOH   HOH B . 
G 4 HOH   43  343 3   HOH   HOH B . 
G 4 HOH   44  344 35  HOH   HOH B . 
G 4 HOH   45  345 18  HOH   HOH B . 
G 4 HOH   46  346 67  HOH   HOH B . 
G 4 HOH   47  347 11  HOH   HOH B . 
G 4 HOH   48  348 114 HOH   HOH B . 
G 4 HOH   49  349 110 HOH   HOH B . 
G 4 HOH   50  350 43  HOH   HOH B . 
G 4 HOH   51  351 117 HOH   HOH B . 
G 4 HOH   52  352 134 HOH   HOH B . 
G 4 HOH   53  353 122 HOH   HOH B . 
G 4 HOH   54  354 161 HOH   HOH B . 
G 4 HOH   55  355 132 HOH   HOH B . 
G 4 HOH   56  356 165 HOH   HOH B . 
G 4 HOH   57  357 95  HOH   HOH B . 
G 4 HOH   58  358 179 HOH   HOH B . 
G 4 HOH   59  359 60  HOH   HOH B . 
G 4 HOH   60  360 184 HOH   HOH B . 
G 4 HOH   61  361 53  HOH   HOH B . 
G 4 HOH   62  362 33  HOH   HOH B . 
G 4 HOH   63  363 109 HOH   HOH B . 
G 4 HOH   64  364 126 HOH   HOH B . 
G 4 HOH   65  365 170 HOH   HOH B . 
G 4 HOH   66  366 128 HOH   HOH B . 
G 4 HOH   67  367 85  HOH   HOH B . 
G 4 HOH   68  368 107 HOH   HOH B . 
G 4 HOH   69  369 116 HOH   HOH B . 
G 4 HOH   70  370 77  HOH   HOH B . 
G 4 HOH   71  371 23  HOH   HOH B . 
G 4 HOH   72  372 32  HOH   HOH B . 
G 4 HOH   73  373 45  HOH   HOH B . 
G 4 HOH   74  374 25  HOH   HOH B . 
G 4 HOH   75  375 162 HOH   HOH B . 
G 4 HOH   76  376 189 HOH   HOH B . 
G 4 HOH   77  377 63  HOH   HOH B . 
G 4 HOH   78  378 195 HOH   HOH B . 
G 4 HOH   79  379 88  HOH   HOH B . 
G 4 HOH   80  380 78  HOH   HOH B . 
G 4 HOH   81  381 79  HOH   HOH B . 
G 4 HOH   82  382 74  HOH   HOH B . 
G 4 HOH   83  383 141 HOH   HOH B . 
G 4 HOH   84  384 81  HOH   HOH B . 
G 4 HOH   85  385 154 HOH   HOH B . 
G 4 HOH   86  386 190 HOH   HOH B . 
G 4 HOH   87  387 140 HOH   HOH B . 
G 4 HOH   88  388 127 HOH   HOH B . 
G 4 HOH   89  389 31  HOH   HOH B . 
G 4 HOH   90  390 159 HOH   HOH B . 
G 4 HOH   91  391 103 HOH   HOH B . 
G 4 HOH   92  392 92  HOH   HOH B . 
G 4 HOH   93  393 46  HOH   HOH B . 
G 4 HOH   94  394 198 HOH   HOH B . 
G 4 HOH   95  395 119 HOH   HOH B . 
G 4 HOH   96  396 186 HOH   HOH B . 
G 4 HOH   97  397 70  HOH   HOH B . 
G 4 HOH   98  398 82  HOH   HOH B . 
G 4 HOH   99  399 149 HOH   HOH B . 
G 4 HOH   100 400 178 HOH   HOH B . 
G 4 HOH   101 401 124 HOH   HOH B . 
G 4 HOH   102 402 147 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 B GLU 92 ? CG  ? B GLU 124 CG  
2 1 Y 1 B GLU 92 ? CD  ? B GLU 124 CD  
3 1 Y 1 B GLU 92 ? OE1 ? B GLU 124 OE1 
4 1 Y 1 B GLU 92 ? OE2 ? B GLU 124 OE2 
# 
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                     9JIS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     43.113 
_cell.length_a_esd                 ? 
_cell.length_b                     84.561 
_cell.length_b_esd                 ? 
_cell.length_c                     63.552 
_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                         9JIS 
_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                   9JIS 
_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                                       9JIS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.41 
_reflns.d_resolution_low                               43.11 
_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                                     45611 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.2 
_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                                0.049 
_reflns.pdbx_Rpim_I_all                                0.018 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.00 
_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                                    1.41 
_reflns_shell.d_res_low                                     1.43 
_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                             2204 
_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                               1.075 
_reflns_shell.pdbx_Rpim_I_all                               0.386 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.783 
_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                                 9JIS 
_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                            1.410 
_refine.ls_d_res_low                             42.280 
_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                     45556 
_refine.ls_number_reflns_R_free                  2299 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1594 
_refine.ls_R_factor_R_free                       0.1891 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1579 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      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                 18.37 
_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                            0.13 
_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        1790 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.number_atoms_solvent             204 
_refine_hist.number_atoms_total               2031 
_refine_hist.d_res_high                       1.410 
_refine_hist.d_res_low                        42.280 
# 
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' ? 0.006  ? 1898 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.785  ? 2597 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.550 ? 679  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.084  ? 289  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 331  ? 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' 1.4100 1.4407 . . 147 2658 100.00 . . . . 0.2078 . . . . . . . . . . . 0.2662 
'X-RAY DIFFRACTION' 1.4407 1.4742 . . 131 2649 100.00 . . . . 0.1847 . . . . . . . . . . . 0.2405 
'X-RAY DIFFRACTION' 1.4742 1.5110 . . 134 2701 100.00 . . . . 0.1713 . . . . . . . . . . . 0.2101 
'X-RAY DIFFRACTION' 1.5110 1.5519 . . 150 2649 100.00 . . . . 0.1584 . . . . . . . . . . . 0.2144 
'X-RAY DIFFRACTION' 1.5519 1.5976 . . 149 2669 100.00 . . . . 0.1480 . . . . . . . . . . . 0.2193 
'X-RAY DIFFRACTION' 1.5976 1.6491 . . 136 2656 100.00 . . . . 0.1361 . . . . . . . . . . . 0.1917 
'X-RAY DIFFRACTION' 1.6491 1.7081 . . 139 2684 100.00 . . . . 0.1411 . . . . . . . . . . . 0.1946 
'X-RAY DIFFRACTION' 1.7081 1.7765 . . 159 2666 100.00 . . . . 0.1500 . . . . . . . . . . . 0.1809 
'X-RAY DIFFRACTION' 1.7765 1.8573 . . 150 2676 100.00 . . . . 0.1430 . . . . . . . . . . . 0.1919 
'X-RAY DIFFRACTION' 1.8573 1.9552 . . 142 2694 100.00 . . . . 0.1306 . . . . . . . . . . . 0.1733 
'X-RAY DIFFRACTION' 1.9552 2.0777 . . 139 2704 100.00 . . . . 0.1300 . . . . . . . . . . . 0.1749 
'X-RAY DIFFRACTION' 2.0777 2.2382 . . 134 2722 100.00 . . . . 0.1344 . . . . . . . . . . . 0.1765 
'X-RAY DIFFRACTION' 2.2382 2.4634 . . 144 2705 100.00 . . . . 0.1534 . . . . . . . . . . . 0.1771 
'X-RAY DIFFRACTION' 2.4634 2.8198 . . 137 2758 100.00 . . . . 0.1802 . . . . . . . . . . . 0.1840 
'X-RAY DIFFRACTION' 2.8198 3.5523 . . 162 2756 100.00 . . . . 0.1711 . . . . . . . . . . . 0.1931 
'X-RAY DIFFRACTION' 3.5523 42.28  . . 146 2910 100.00 . . . . 0.1630 . . . . . . . . . . . 0.1880 
# 
_struct.entry_id                     9JIS 
_struct.title                        'Crystal structure of V30M-TTR in complex with aclonifen' 
_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        9JIS 
_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 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_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 9JIS A 13 ? 159 ? P02766 1 ? 147 ? -19 127 
2 1 9JIS 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 9JIS MET A 1  ? UNP P02766 ?   ?  'initiating methionine' -31 1  
1 9JIS ARG A 2  ? UNP P02766 ?   ?  'expression tag'        -30 2  
1 9JIS GLY A 3  ? UNP P02766 ?   ?  'expression tag'        -29 3  
1 9JIS SER A 4  ? UNP P02766 ?   ?  'expression tag'        -28 4  
1 9JIS HIS A 5  ? UNP P02766 ?   ?  'expression tag'        -27 5  
1 9JIS HIS A 6  ? UNP P02766 ?   ?  'expression tag'        -26 6  
1 9JIS HIS A 7  ? UNP P02766 ?   ?  'expression tag'        -25 7  
1 9JIS HIS A 8  ? UNP P02766 ?   ?  'expression tag'        -24 8  
1 9JIS HIS A 9  ? UNP P02766 ?   ?  'expression tag'        -23 9  
1 9JIS HIS A 10 ? UNP P02766 ?   ?  'expression tag'        -22 10 
1 9JIS GLY A 11 ? UNP P02766 ?   ?  'expression tag'        -21 11 
1 9JIS SER A 12 ? UNP P02766 ?   ?  'expression tag'        -20 12 
1 9JIS MET A 62 ? UNP P02766 VAL 50 'engineered mutation'   30  13 
2 9JIS MET B 1  ? UNP P02766 ?   ?  'initiating methionine' -31 14 
2 9JIS ARG B 2  ? UNP P02766 ?   ?  'expression tag'        -30 15 
2 9JIS GLY B 3  ? UNP P02766 ?   ?  'expression tag'        -29 16 
2 9JIS SER B 4  ? UNP P02766 ?   ?  'expression tag'        -28 17 
2 9JIS HIS B 5  ? UNP P02766 ?   ?  'expression tag'        -27 18 
2 9JIS HIS B 6  ? UNP P02766 ?   ?  'expression tag'        -26 19 
2 9JIS HIS B 7  ? UNP P02766 ?   ?  'expression tag'        -25 20 
2 9JIS HIS B 8  ? UNP P02766 ?   ?  'expression tag'        -24 21 
2 9JIS HIS B 9  ? UNP P02766 ?   ?  'expression tag'        -23 22 
2 9JIS HIS B 10 ? UNP P02766 ?   ?  'expression tag'        -22 23 
2 9JIS GLY B 11 ? UNP P02766 ?   ?  'expression tag'        -21 24 
2 9JIS SER B 12 ? UNP P02766 ?   ?  'expression tag'        -20 25 
2 9JIS MET B 62 ? UNP P02766 VAL 50 'engineered mutation'   30  26 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G 
1 2 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 -43.1130000000 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   ? 
# 
_struct_conn.id                            metalc1 
_struct_conn.conn_type_id                  metalc 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           ASP 
_struct_conn.ptnr1_label_seq_id            131 
_struct_conn.ptnr1_label_atom_id           O 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           D 
_struct_conn.ptnr2_label_comp_id           NA 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           NA 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            ASP 
_struct_conn.ptnr1_auth_seq_id             99 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            NA 
_struct_conn.ptnr2_auth_seq_id             202 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.292 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_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 LEU A 49  ? N LEU A 17  O LEU A 143 ? O LEU A 111 
AA1 3 4 N ARG A 136 ? N ARG A 104 O THR A 155 ? O THR A 123 
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 155 ? O THR B 123 N ARG B 136 ? N ARG B 104 
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 LEU A 49  ? N LEU A 17  O LEU A 143 ? O LEU A 111 
AA2 3 4 N ARG A 136 ? N ARG A 104 O THR A 155 ? O THR A 123 
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 155 ? O THR B 123 N ARG B 136 ? N ARG B 104 
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                   9JIS 
_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 
# 
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 A1L38 201 ? C A1L38 . 
2 1 B A1L38 201 ? E A1L38 . 
# 
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 
A1L38 CAA  C  Y N 1   
A1L38 CAB  C  Y N 2   
A1L38 CAC  C  Y N 3   
A1L38 CAD  C  Y N 4   
A1L38 CAE  C  Y N 5   
A1L38 CAF  C  Y N 6   
A1L38 CAH  C  Y N 7   
A1L38 CAI  C  Y N 8   
A1L38 CAJ  C  Y N 9   
A1L38 CAK  C  Y N 10  
A1L38 CAL  C  Y N 11  
A1L38 CAM  C  Y N 12  
A1L38 NAO  N  N N 13  
A1L38 NAP  N  N N 14  
A1L38 OAG  O  N N 15  
A1L38 OAQ  O  N N 16  
A1L38 OAR  O  N N 17  
A1L38 CLAN CL N N 18  
A1L38 H1   H  N N 19  
A1L38 H2   H  N N 20  
A1L38 H3   H  N N 21  
A1L38 H4   H  N N 22  
A1L38 H5   H  N N 23  
A1L38 H6   H  N N 24  
A1L38 H7   H  N N 25  
A1L38 H8   H  N N 26  
A1L38 H9   H  N N 27  
ALA   N    N  N N 28  
ALA   CA   C  N S 29  
ALA   C    C  N N 30  
ALA   O    O  N N 31  
ALA   CB   C  N N 32  
ALA   OXT  O  N N 33  
ALA   H    H  N N 34  
ALA   H2   H  N N 35  
ALA   HA   H  N N 36  
ALA   HB1  H  N N 37  
ALA   HB2  H  N N 38  
ALA   HB3  H  N N 39  
ALA   HXT  H  N N 40  
ARG   N    N  N N 41  
ARG   CA   C  N S 42  
ARG   C    C  N N 43  
ARG   O    O  N N 44  
ARG   CB   C  N N 45  
ARG   CG   C  N N 46  
ARG   CD   C  N N 47  
ARG   NE   N  N N 48  
ARG   CZ   C  N N 49  
ARG   NH1  N  N N 50  
ARG   NH2  N  N N 51  
ARG   OXT  O  N N 52  
ARG   H    H  N N 53  
ARG   H2   H  N N 54  
ARG   HA   H  N N 55  
ARG   HB2  H  N N 56  
ARG   HB3  H  N N 57  
ARG   HG2  H  N N 58  
ARG   HG3  H  N N 59  
ARG   HD2  H  N N 60  
ARG   HD3  H  N N 61  
ARG   HE   H  N N 62  
ARG   HH11 H  N N 63  
ARG   HH12 H  N N 64  
ARG   HH21 H  N N 65  
ARG   HH22 H  N N 66  
ARG   HXT  H  N N 67  
ASN   N    N  N N 68  
ASN   CA   C  N S 69  
ASN   C    C  N N 70  
ASN   O    O  N N 71  
ASN   CB   C  N N 72  
ASN   CG   C  N N 73  
ASN   OD1  O  N N 74  
ASN   ND2  N  N N 75  
ASN   OXT  O  N N 76  
ASN   H    H  N N 77  
ASN   H2   H  N N 78  
ASN   HA   H  N N 79  
ASN   HB2  H  N N 80  
ASN   HB3  H  N N 81  
ASN   HD21 H  N N 82  
ASN   HD22 H  N N 83  
ASN   HXT  H  N N 84  
ASP   N    N  N N 85  
ASP   CA   C  N S 86  
ASP   C    C  N N 87  
ASP   O    O  N N 88  
ASP   CB   C  N N 89  
ASP   CG   C  N N 90  
ASP   OD1  O  N N 91  
ASP   OD2  O  N N 92  
ASP   OXT  O  N N 93  
ASP   H    H  N N 94  
ASP   H2   H  N N 95  
ASP   HA   H  N N 96  
ASP   HB2  H  N N 97  
ASP   HB3  H  N N 98  
ASP   HD2  H  N N 99  
ASP   HXT  H  N N 100 
CYS   N    N  N N 101 
CYS   CA   C  N R 102 
CYS   C    C  N N 103 
CYS   O    O  N N 104 
CYS   CB   C  N N 105 
CYS   SG   S  N N 106 
CYS   OXT  O  N N 107 
CYS   H    H  N N 108 
CYS   H2   H  N N 109 
CYS   HA   H  N N 110 
CYS   HB2  H  N N 111 
CYS   HB3  H  N N 112 
CYS   HG   H  N N 113 
CYS   HXT  H  N N 114 
GLU   N    N  N N 115 
GLU   CA   C  N S 116 
GLU   C    C  N N 117 
GLU   O    O  N N 118 
GLU   CB   C  N N 119 
GLU   CG   C  N N 120 
GLU   CD   C  N N 121 
GLU   OE1  O  N N 122 
GLU   OE2  O  N N 123 
GLU   OXT  O  N N 124 
GLU   H    H  N N 125 
GLU   H2   H  N N 126 
GLU   HA   H  N N 127 
GLU   HB2  H  N N 128 
GLU   HB3  H  N N 129 
GLU   HG2  H  N N 130 
GLU   HG3  H  N N 131 
GLU   HE2  H  N N 132 
GLU   HXT  H  N N 133 
GLY   N    N  N N 134 
GLY   CA   C  N N 135 
GLY   C    C  N N 136 
GLY   O    O  N N 137 
GLY   OXT  O  N N 138 
GLY   H    H  N N 139 
GLY   H2   H  N N 140 
GLY   HA2  H  N N 141 
GLY   HA3  H  N N 142 
GLY   HXT  H  N N 143 
HIS   N    N  N N 144 
HIS   CA   C  N S 145 
HIS   C    C  N N 146 
HIS   O    O  N N 147 
HIS   CB   C  N N 148 
HIS   CG   C  Y N 149 
HIS   ND1  N  Y N 150 
HIS   CD2  C  Y N 151 
HIS   CE1  C  Y N 152 
HIS   NE2  N  Y N 153 
HIS   OXT  O  N N 154 
HIS   H    H  N N 155 
HIS   H2   H  N N 156 
HIS   HA   H  N N 157 
HIS   HB2  H  N N 158 
HIS   HB3  H  N N 159 
HIS   HD1  H  N N 160 
HIS   HD2  H  N N 161 
HIS   HE1  H  N N 162 
HIS   HE2  H  N N 163 
HIS   HXT  H  N N 164 
HOH   O    O  N N 165 
HOH   H1   H  N N 166 
HOH   H2   H  N N 167 
ILE   N    N  N N 168 
ILE   CA   C  N S 169 
ILE   C    C  N N 170 
ILE   O    O  N N 171 
ILE   CB   C  N S 172 
ILE   CG1  C  N N 173 
ILE   CG2  C  N N 174 
ILE   CD1  C  N N 175 
ILE   OXT  O  N N 176 
ILE   H    H  N N 177 
ILE   H2   H  N N 178 
ILE   HA   H  N N 179 
ILE   HB   H  N N 180 
ILE   HG12 H  N N 181 
ILE   HG13 H  N N 182 
ILE   HG21 H  N N 183 
ILE   HG22 H  N N 184 
ILE   HG23 H  N N 185 
ILE   HD11 H  N N 186 
ILE   HD12 H  N N 187 
ILE   HD13 H  N N 188 
ILE   HXT  H  N N 189 
LEU   N    N  N N 190 
LEU   CA   C  N S 191 
LEU   C    C  N N 192 
LEU   O    O  N N 193 
LEU   CB   C  N N 194 
LEU   CG   C  N N 195 
LEU   CD1  C  N N 196 
LEU   CD2  C  N N 197 
LEU   OXT  O  N N 198 
LEU   H    H  N N 199 
LEU   H2   H  N N 200 
LEU   HA   H  N N 201 
LEU   HB2  H  N N 202 
LEU   HB3  H  N N 203 
LEU   HG   H  N N 204 
LEU   HD11 H  N N 205 
LEU   HD12 H  N N 206 
LEU   HD13 H  N N 207 
LEU   HD21 H  N N 208 
LEU   HD22 H  N N 209 
LEU   HD23 H  N N 210 
LEU   HXT  H  N N 211 
LYS   N    N  N N 212 
LYS   CA   C  N S 213 
LYS   C    C  N N 214 
LYS   O    O  N N 215 
LYS   CB   C  N N 216 
LYS   CG   C  N N 217 
LYS   CD   C  N N 218 
LYS   CE   C  N N 219 
LYS   NZ   N  N N 220 
LYS   OXT  O  N N 221 
LYS   H    H  N N 222 
LYS   H2   H  N N 223 
LYS   HA   H  N N 224 
LYS   HB2  H  N N 225 
LYS   HB3  H  N N 226 
LYS   HG2  H  N N 227 
LYS   HG3  H  N N 228 
LYS   HD2  H  N N 229 
LYS   HD3  H  N N 230 
LYS   HE2  H  N N 231 
LYS   HE3  H  N N 232 
LYS   HZ1  H  N N 233 
LYS   HZ2  H  N N 234 
LYS   HZ3  H  N N 235 
LYS   HXT  H  N N 236 
MET   N    N  N N 237 
MET   CA   C  N S 238 
MET   C    C  N N 239 
MET   O    O  N N 240 
MET   CB   C  N N 241 
MET   CG   C  N N 242 
MET   SD   S  N N 243 
MET   CE   C  N N 244 
MET   OXT  O  N N 245 
MET   H    H  N N 246 
MET   H2   H  N N 247 
MET   HA   H  N N 248 
MET   HB2  H  N N 249 
MET   HB3  H  N N 250 
MET   HG2  H  N N 251 
MET   HG3  H  N N 252 
MET   HE1  H  N N 253 
MET   HE2  H  N N 254 
MET   HE3  H  N N 255 
MET   HXT  H  N N 256 
NA    NA   NA N N 257 
PHE   N    N  N N 258 
PHE   CA   C  N S 259 
PHE   C    C  N N 260 
PHE   O    O  N N 261 
PHE   CB   C  N N 262 
PHE   CG   C  Y N 263 
PHE   CD1  C  Y N 264 
PHE   CD2  C  Y N 265 
PHE   CE1  C  Y N 266 
PHE   CE2  C  Y N 267 
PHE   CZ   C  Y N 268 
PHE   OXT  O  N N 269 
PHE   H    H  N N 270 
PHE   H2   H  N N 271 
PHE   HA   H  N N 272 
PHE   HB2  H  N N 273 
PHE   HB3  H  N N 274 
PHE   HD1  H  N N 275 
PHE   HD2  H  N N 276 
PHE   HE1  H  N N 277 
PHE   HE2  H  N N 278 
PHE   HZ   H  N N 279 
PHE   HXT  H  N N 280 
PRO   N    N  N N 281 
PRO   CA   C  N S 282 
PRO   C    C  N N 283 
PRO   O    O  N N 284 
PRO   CB   C  N N 285 
PRO   CG   C  N N 286 
PRO   CD   C  N N 287 
PRO   OXT  O  N N 288 
PRO   H    H  N N 289 
PRO   HA   H  N N 290 
PRO   HB2  H  N N 291 
PRO   HB3  H  N N 292 
PRO   HG2  H  N N 293 
PRO   HG3  H  N N 294 
PRO   HD2  H  N N 295 
PRO   HD3  H  N N 296 
PRO   HXT  H  N N 297 
SER   N    N  N N 298 
SER   CA   C  N S 299 
SER   C    C  N N 300 
SER   O    O  N N 301 
SER   CB   C  N N 302 
SER   OG   O  N N 303 
SER   OXT  O  N N 304 
SER   H    H  N N 305 
SER   H2   H  N N 306 
SER   HA   H  N N 307 
SER   HB2  H  N N 308 
SER   HB3  H  N N 309 
SER   HG   H  N N 310 
SER   HXT  H  N N 311 
THR   N    N  N N 312 
THR   CA   C  N S 313 
THR   C    C  N N 314 
THR   O    O  N N 315 
THR   CB   C  N R 316 
THR   OG1  O  N N 317 
THR   CG2  C  N N 318 
THR   OXT  O  N N 319 
THR   H    H  N N 320 
THR   H2   H  N N 321 
THR   HA   H  N N 322 
THR   HB   H  N N 323 
THR   HG1  H  N N 324 
THR   HG21 H  N N 325 
THR   HG22 H  N N 326 
THR   HG23 H  N N 327 
THR   HXT  H  N N 328 
TRP   N    N  N N 329 
TRP   CA   C  N S 330 
TRP   C    C  N N 331 
TRP   O    O  N N 332 
TRP   CB   C  N N 333 
TRP   CG   C  Y N 334 
TRP   CD1  C  Y N 335 
TRP   CD2  C  Y N 336 
TRP   NE1  N  Y N 337 
TRP   CE2  C  Y N 338 
TRP   CE3  C  Y N 339 
TRP   CZ2  C  Y N 340 
TRP   CZ3  C  Y N 341 
TRP   CH2  C  Y N 342 
TRP   OXT  O  N N 343 
TRP   H    H  N N 344 
TRP   H2   H  N N 345 
TRP   HA   H  N N 346 
TRP   HB2  H  N N 347 
TRP   HB3  H  N N 348 
TRP   HD1  H  N N 349 
TRP   HE1  H  N N 350 
TRP   HE3  H  N N 351 
TRP   HZ2  H  N N 352 
TRP   HZ3  H  N N 353 
TRP   HH2  H  N N 354 
TRP   HXT  H  N N 355 
TYR   N    N  N N 356 
TYR   CA   C  N S 357 
TYR   C    C  N N 358 
TYR   O    O  N N 359 
TYR   CB   C  N N 360 
TYR   CG   C  Y N 361 
TYR   CD1  C  Y N 362 
TYR   CD2  C  Y N 363 
TYR   CE1  C  Y N 364 
TYR   CE2  C  Y N 365 
TYR   CZ   C  Y N 366 
TYR   OH   O  N N 367 
TYR   OXT  O  N N 368 
TYR   H    H  N N 369 
TYR   H2   H  N N 370 
TYR   HA   H  N N 371 
TYR   HB2  H  N N 372 
TYR   HB3  H  N N 373 
TYR   HD1  H  N N 374 
TYR   HD2  H  N N 375 
TYR   HE1  H  N N 376 
TYR   HE2  H  N N 377 
TYR   HH   H  N N 378 
TYR   HXT  H  N N 379 
VAL   N    N  N N 380 
VAL   CA   C  N S 381 
VAL   C    C  N N 382 
VAL   O    O  N N 383 
VAL   CB   C  N N 384 
VAL   CG1  C  N N 385 
VAL   CG2  C  N N 386 
VAL   OXT  O  N N 387 
VAL   H    H  N N 388 
VAL   H2   H  N N 389 
VAL   HA   H  N N 390 
VAL   HB   H  N N 391 
VAL   HG11 H  N N 392 
VAL   HG12 H  N N 393 
VAL   HG13 H  N N 394 
VAL   HG21 H  N N 395 
VAL   HG22 H  N N 396 
VAL   HG23 H  N N 397 
VAL   HXT  H  N N 398 
# 
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 
A1L38 OAR  NAP  doub N N 1   
A1L38 NAO  CAL  sing N N 2   
A1L38 NAP  OAQ  sing N N 3   
A1L38 NAP  CAM  sing N N 4   
A1L38 CAL  CAM  doub Y N 5   
A1L38 CAL  CAJ  sing Y N 6   
A1L38 CAM  CAK  sing Y N 7   
A1L38 CLAN CAJ  sing N N 8   
A1L38 CAJ  CAH  doub Y N 9   
A1L38 CAK  CAI  doub Y N 10  
A1L38 CAH  CAI  sing Y N 11  
A1L38 CAH  OAG  sing N N 12  
A1L38 OAG  CAD  sing N N 13  
A1L38 CAD  CAF  doub Y N 14  
A1L38 CAD  CAB  sing Y N 15  
A1L38 CAF  CAE  sing Y N 16  
A1L38 CAB  CAA  doub Y N 17  
A1L38 CAE  CAC  doub Y N 18  
A1L38 CAA  CAC  sing Y N 19  
A1L38 CAA  H1   sing N N 20  
A1L38 CAB  H2   sing N N 21  
A1L38 CAC  H3   sing N N 22  
A1L38 CAE  H4   sing N N 23  
A1L38 CAF  H5   sing N N 24  
A1L38 CAI  H6   sing N N 25  
A1L38 CAK  H7   sing N N 26  
A1L38 NAO  H8   sing N N 27  
A1L38 NAO  H9   sing N N 28  
ALA   N    CA   sing N N 29  
ALA   N    H    sing N N 30  
ALA   N    H2   sing N N 31  
ALA   CA   C    sing N N 32  
ALA   CA   CB   sing N N 33  
ALA   CA   HA   sing N N 34  
ALA   C    O    doub N N 35  
ALA   C    OXT  sing N N 36  
ALA   CB   HB1  sing N N 37  
ALA   CB   HB2  sing N N 38  
ALA   CB   HB3  sing N N 39  
ALA   OXT  HXT  sing N N 40  
ARG   N    CA   sing N N 41  
ARG   N    H    sing N N 42  
ARG   N    H2   sing N N 43  
ARG   CA   C    sing N N 44  
ARG   CA   CB   sing N N 45  
ARG   CA   HA   sing N N 46  
ARG   C    O    doub N N 47  
ARG   C    OXT  sing N N 48  
ARG   CB   CG   sing N N 49  
ARG   CB   HB2  sing N N 50  
ARG   CB   HB3  sing N N 51  
ARG   CG   CD   sing N N 52  
ARG   CG   HG2  sing N N 53  
ARG   CG   HG3  sing N N 54  
ARG   CD   NE   sing N N 55  
ARG   CD   HD2  sing N N 56  
ARG   CD   HD3  sing N N 57  
ARG   NE   CZ   sing N N 58  
ARG   NE   HE   sing N N 59  
ARG   CZ   NH1  sing N N 60  
ARG   CZ   NH2  doub N N 61  
ARG   NH1  HH11 sing N N 62  
ARG   NH1  HH12 sing N N 63  
ARG   NH2  HH21 sing N N 64  
ARG   NH2  HH22 sing N N 65  
ARG   OXT  HXT  sing N N 66  
ASN   N    CA   sing N N 67  
ASN   N    H    sing N N 68  
ASN   N    H2   sing N N 69  
ASN   CA   C    sing N N 70  
ASN   CA   CB   sing N N 71  
ASN   CA   HA   sing N N 72  
ASN   C    O    doub N N 73  
ASN   C    OXT  sing N N 74  
ASN   CB   CG   sing N N 75  
ASN   CB   HB2  sing N N 76  
ASN   CB   HB3  sing N N 77  
ASN   CG   OD1  doub N N 78  
ASN   CG   ND2  sing N N 79  
ASN   ND2  HD21 sing N N 80  
ASN   ND2  HD22 sing N N 81  
ASN   OXT  HXT  sing N N 82  
ASP   N    CA   sing N N 83  
ASP   N    H    sing N N 84  
ASP   N    H2   sing N N 85  
ASP   CA   C    sing N N 86  
ASP   CA   CB   sing N N 87  
ASP   CA   HA   sing N N 88  
ASP   C    O    doub N N 89  
ASP   C    OXT  sing N N 90  
ASP   CB   CG   sing N N 91  
ASP   CB   HB2  sing N N 92  
ASP   CB   HB3  sing N N 93  
ASP   CG   OD1  doub N N 94  
ASP   CG   OD2  sing N N 95  
ASP   OD2  HD2  sing N N 96  
ASP   OXT  HXT  sing N N 97  
CYS   N    CA   sing N N 98  
CYS   N    H    sing N N 99  
CYS   N    H2   sing N N 100 
CYS   CA   C    sing N N 101 
CYS   CA   CB   sing N N 102 
CYS   CA   HA   sing N N 103 
CYS   C    O    doub N N 104 
CYS   C    OXT  sing N N 105 
CYS   CB   SG   sing N N 106 
CYS   CB   HB2  sing N N 107 
CYS   CB   HB3  sing N N 108 
CYS   SG   HG   sing N N 109 
CYS   OXT  HXT  sing N N 110 
GLU   N    CA   sing N N 111 
GLU   N    H    sing N N 112 
GLU   N    H2   sing N N 113 
GLU   CA   C    sing N N 114 
GLU   CA   CB   sing N N 115 
GLU   CA   HA   sing N N 116 
GLU   C    O    doub N N 117 
GLU   C    OXT  sing N N 118 
GLU   CB   CG   sing N N 119 
GLU   CB   HB2  sing N N 120 
GLU   CB   HB3  sing N N 121 
GLU   CG   CD   sing N N 122 
GLU   CG   HG2  sing N N 123 
GLU   CG   HG3  sing N N 124 
GLU   CD   OE1  doub N N 125 
GLU   CD   OE2  sing N N 126 
GLU   OE2  HE2  sing N N 127 
GLU   OXT  HXT  sing N N 128 
GLY   N    CA   sing N N 129 
GLY   N    H    sing N N 130 
GLY   N    H2   sing N N 131 
GLY   CA   C    sing N N 132 
GLY   CA   HA2  sing N N 133 
GLY   CA   HA3  sing N N 134 
GLY   C    O    doub N N 135 
GLY   C    OXT  sing N N 136 
GLY   OXT  HXT  sing N N 137 
HIS   N    CA   sing N N 138 
HIS   N    H    sing N N 139 
HIS   N    H2   sing N N 140 
HIS   CA   C    sing N N 141 
HIS   CA   CB   sing N N 142 
HIS   CA   HA   sing N N 143 
HIS   C    O    doub N N 144 
HIS   C    OXT  sing N N 145 
HIS   CB   CG   sing N N 146 
HIS   CB   HB2  sing N N 147 
HIS   CB   HB3  sing N N 148 
HIS   CG   ND1  sing Y N 149 
HIS   CG   CD2  doub Y N 150 
HIS   ND1  CE1  doub Y N 151 
HIS   ND1  HD1  sing N N 152 
HIS   CD2  NE2  sing Y N 153 
HIS   CD2  HD2  sing N N 154 
HIS   CE1  NE2  sing Y N 155 
HIS   CE1  HE1  sing N N 156 
HIS   NE2  HE2  sing N N 157 
HIS   OXT  HXT  sing N N 158 
HOH   O    H1   sing N N 159 
HOH   O    H2   sing N N 160 
ILE   N    CA   sing N N 161 
ILE   N    H    sing N N 162 
ILE   N    H2   sing N N 163 
ILE   CA   C    sing N N 164 
ILE   CA   CB   sing N N 165 
ILE   CA   HA   sing N N 166 
ILE   C    O    doub N N 167 
ILE   C    OXT  sing N N 168 
ILE   CB   CG1  sing N N 169 
ILE   CB   CG2  sing N N 170 
ILE   CB   HB   sing N N 171 
ILE   CG1  CD1  sing N N 172 
ILE   CG1  HG12 sing N N 173 
ILE   CG1  HG13 sing N N 174 
ILE   CG2  HG21 sing N N 175 
ILE   CG2  HG22 sing N N 176 
ILE   CG2  HG23 sing N N 177 
ILE   CD1  HD11 sing N N 178 
ILE   CD1  HD12 sing N N 179 
ILE   CD1  HD13 sing N N 180 
ILE   OXT  HXT  sing N N 181 
LEU   N    CA   sing N N 182 
LEU   N    H    sing N N 183 
LEU   N    H2   sing N N 184 
LEU   CA   C    sing N N 185 
LEU   CA   CB   sing N N 186 
LEU   CA   HA   sing N N 187 
LEU   C    O    doub N N 188 
LEU   C    OXT  sing N N 189 
LEU   CB   CG   sing N N 190 
LEU   CB   HB2  sing N N 191 
LEU   CB   HB3  sing N N 192 
LEU   CG   CD1  sing N N 193 
LEU   CG   CD2  sing N N 194 
LEU   CG   HG   sing N N 195 
LEU   CD1  HD11 sing N N 196 
LEU   CD1  HD12 sing N N 197 
LEU   CD1  HD13 sing N N 198 
LEU   CD2  HD21 sing N N 199 
LEU   CD2  HD22 sing N N 200 
LEU   CD2  HD23 sing N N 201 
LEU   OXT  HXT  sing N N 202 
LYS   N    CA   sing N N 203 
LYS   N    H    sing N N 204 
LYS   N    H2   sing N N 205 
LYS   CA   C    sing N N 206 
LYS   CA   CB   sing N N 207 
LYS   CA   HA   sing N N 208 
LYS   C    O    doub N N 209 
LYS   C    OXT  sing N N 210 
LYS   CB   CG   sing N N 211 
LYS   CB   HB2  sing N N 212 
LYS   CB   HB3  sing N N 213 
LYS   CG   CD   sing N N 214 
LYS   CG   HG2  sing N N 215 
LYS   CG   HG3  sing N N 216 
LYS   CD   CE   sing N N 217 
LYS   CD   HD2  sing N N 218 
LYS   CD   HD3  sing N N 219 
LYS   CE   NZ   sing N N 220 
LYS   CE   HE2  sing N N 221 
LYS   CE   HE3  sing N N 222 
LYS   NZ   HZ1  sing N N 223 
LYS   NZ   HZ2  sing N N 224 
LYS   NZ   HZ3  sing N N 225 
LYS   OXT  HXT  sing N N 226 
MET   N    CA   sing N N 227 
MET   N    H    sing N N 228 
MET   N    H2   sing N N 229 
MET   CA   C    sing N N 230 
MET   CA   CB   sing N N 231 
MET   CA   HA   sing N N 232 
MET   C    O    doub N N 233 
MET   C    OXT  sing N N 234 
MET   CB   CG   sing N N 235 
MET   CB   HB2  sing N N 236 
MET   CB   HB3  sing N N 237 
MET   CG   SD   sing N N 238 
MET   CG   HG2  sing N N 239 
MET   CG   HG3  sing N N 240 
MET   SD   CE   sing N N 241 
MET   CE   HE1  sing N N 242 
MET   CE   HE2  sing N N 243 
MET   CE   HE3  sing N N 244 
MET   OXT  HXT  sing N N 245 
PHE   N    CA   sing N N 246 
PHE   N    H    sing N N 247 
PHE   N    H2   sing N N 248 
PHE   CA   C    sing N N 249 
PHE   CA   CB   sing N N 250 
PHE   CA   HA   sing N N 251 
PHE   C    O    doub N N 252 
PHE   C    OXT  sing N N 253 
PHE   CB   CG   sing N N 254 
PHE   CB   HB2  sing N N 255 
PHE   CB   HB3  sing N N 256 
PHE   CG   CD1  doub Y N 257 
PHE   CG   CD2  sing Y N 258 
PHE   CD1  CE1  sing Y N 259 
PHE   CD1  HD1  sing N N 260 
PHE   CD2  CE2  doub Y N 261 
PHE   CD2  HD2  sing N N 262 
PHE   CE1  CZ   doub Y N 263 
PHE   CE1  HE1  sing N N 264 
PHE   CE2  CZ   sing Y N 265 
PHE   CE2  HE2  sing N N 266 
PHE   CZ   HZ   sing N N 267 
PHE   OXT  HXT  sing N N 268 
PRO   N    CA   sing N N 269 
PRO   N    CD   sing N N 270 
PRO   N    H    sing N N 271 
PRO   CA   C    sing N N 272 
PRO   CA   CB   sing N N 273 
PRO   CA   HA   sing N N 274 
PRO   C    O    doub N N 275 
PRO   C    OXT  sing N N 276 
PRO   CB   CG   sing N N 277 
PRO   CB   HB2  sing N N 278 
PRO   CB   HB3  sing N N 279 
PRO   CG   CD   sing N N 280 
PRO   CG   HG2  sing N N 281 
PRO   CG   HG3  sing N N 282 
PRO   CD   HD2  sing N N 283 
PRO   CD   HD3  sing N N 284 
PRO   OXT  HXT  sing N N 285 
SER   N    CA   sing N N 286 
SER   N    H    sing N N 287 
SER   N    H2   sing N N 288 
SER   CA   C    sing N N 289 
SER   CA   CB   sing N N 290 
SER   CA   HA   sing N N 291 
SER   C    O    doub N N 292 
SER   C    OXT  sing N N 293 
SER   CB   OG   sing N N 294 
SER   CB   HB2  sing N N 295 
SER   CB   HB3  sing N N 296 
SER   OG   HG   sing N N 297 
SER   OXT  HXT  sing N N 298 
THR   N    CA   sing N N 299 
THR   N    H    sing N N 300 
THR   N    H2   sing N N 301 
THR   CA   C    sing N N 302 
THR   CA   CB   sing N N 303 
THR   CA   HA   sing N N 304 
THR   C    O    doub N N 305 
THR   C    OXT  sing N N 306 
THR   CB   OG1  sing N N 307 
THR   CB   CG2  sing N N 308 
THR   CB   HB   sing N N 309 
THR   OG1  HG1  sing N N 310 
THR   CG2  HG21 sing N N 311 
THR   CG2  HG22 sing N N 312 
THR   CG2  HG23 sing N N 313 
THR   OXT  HXT  sing N N 314 
TRP   N    CA   sing N N 315 
TRP   N    H    sing N N 316 
TRP   N    H2   sing N N 317 
TRP   CA   C    sing N N 318 
TRP   CA   CB   sing N N 319 
TRP   CA   HA   sing N N 320 
TRP   C    O    doub N N 321 
TRP   C    OXT  sing N N 322 
TRP   CB   CG   sing N N 323 
TRP   CB   HB2  sing N N 324 
TRP   CB   HB3  sing N N 325 
TRP   CG   CD1  doub Y N 326 
TRP   CG   CD2  sing Y N 327 
TRP   CD1  NE1  sing Y N 328 
TRP   CD1  HD1  sing N N 329 
TRP   CD2  CE2  doub Y N 330 
TRP   CD2  CE3  sing Y N 331 
TRP   NE1  CE2  sing Y N 332 
TRP   NE1  HE1  sing N N 333 
TRP   CE2  CZ2  sing Y N 334 
TRP   CE3  CZ3  doub Y N 335 
TRP   CE3  HE3  sing N N 336 
TRP   CZ2  CH2  doub Y N 337 
TRP   CZ2  HZ2  sing N N 338 
TRP   CZ3  CH2  sing Y N 339 
TRP   CZ3  HZ3  sing N N 340 
TRP   CH2  HH2  sing N N 341 
TRP   OXT  HXT  sing N N 342 
TYR   N    CA   sing N N 343 
TYR   N    H    sing N N 344 
TYR   N    H2   sing N N 345 
TYR   CA   C    sing N N 346 
TYR   CA   CB   sing N N 347 
TYR   CA   HA   sing N N 348 
TYR   C    O    doub N N 349 
TYR   C    OXT  sing N N 350 
TYR   CB   CG   sing N N 351 
TYR   CB   HB2  sing N N 352 
TYR   CB   HB3  sing N N 353 
TYR   CG   CD1  doub Y N 354 
TYR   CG   CD2  sing Y N 355 
TYR   CD1  CE1  sing Y N 356 
TYR   CD1  HD1  sing N N 357 
TYR   CD2  CE2  doub Y N 358 
TYR   CD2  HD2  sing N N 359 
TYR   CE1  CZ   doub Y N 360 
TYR   CE1  HE1  sing N N 361 
TYR   CE2  CZ   sing Y N 362 
TYR   CE2  HE2  sing N N 363 
TYR   CZ   OH   sing N N 364 
TYR   OH   HH   sing N N 365 
TYR   OXT  HXT  sing N N 366 
VAL   N    CA   sing N N 367 
VAL   N    H    sing N N 368 
VAL   N    H2   sing N N 369 
VAL   CA   C    sing N N 370 
VAL   CA   CB   sing N N 371 
VAL   CA   HA   sing N N 372 
VAL   C    O    doub N N 373 
VAL   C    OXT  sing N N 374 
VAL   CB   CG1  sing N N 375 
VAL   CB   CG2  sing N N 376 
VAL   CB   HB   sing N N 377 
VAL   CG1  HG11 sing N N 378 
VAL   CG1  HG12 sing N N 379 
VAL   CG1  HG13 sing N N 380 
VAL   CG2  HG21 sing N N 381 
VAL   CG2  HG22 sing N N 382 
VAL   CG2  HG23 sing N N 383 
VAL   OXT  HXT  sing N N 384 
# 
_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                    9JIS 
_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]   0.023195 
_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]   0.011826 
_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]   0.015735 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
NA 
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  ? -28.507 11.261 7.733   1.00 46.24 ? 10  CYS   A N    1 
ATOM   2    C  CA   . CYS   A 1 42  ? -27.612 11.438 6.596   1.00 44.44 ? 10  CYS   A CA   1 
ATOM   3    C  C    . CYS   A 1 42  ? -28.384 11.248 5.297   1.00 36.88 ? 10  CYS   A C    1 
ATOM   4    O  O    . CYS   A 1 42  ? -28.397 10.157 4.729   1.00 37.29 ? 10  CYS   A O    1 
ATOM   5    C  CB   . CYS   A 1 42  ? -26.454 10.442 6.674   1.00 49.57 ? 10  CYS   A CB   1 
ATOM   6    S  SG   . CYS   A 1 42  ? -25.113 10.741 5.490   1.00 53.08 ? 10  CYS   A SG   1 
ATOM   7    N  N    . PRO   A 1 43  ? -29.050 12.309 4.834   1.00 29.31 ? 11  PRO   A N    1 
ATOM   8    C  CA   . PRO   A 1 43  ? -29.920 12.174 3.658   1.00 25.66 ? 11  PRO   A CA   1 
ATOM   9    C  C    . PRO   A 1 43  ? -29.197 12.108 2.324   1.00 20.89 ? 11  PRO   A C    1 
ATOM   10   O  O    . PRO   A 1 43  ? -29.841 11.779 1.319   1.00 22.63 ? 11  PRO   A O    1 
ATOM   11   C  CB   . PRO   A 1 43  ? -30.811 13.422 3.737   1.00 28.80 ? 11  PRO   A CB   1 
ATOM   12   C  CG   . PRO   A 1 43  ? -30.012 14.398 4.498   1.00 29.78 ? 11  PRO   A CG   1 
ATOM   13   C  CD   . PRO   A 1 43  ? -29.240 13.604 5.509   1.00 29.85 ? 11  PRO   A CD   1 
ATOM   14   N  N    . LEU   A 1 44  ? -27.902 12.419 2.265   1.00 19.02 ? 12  LEU   A N    1 
ATOM   15   C  CA   . LEU   A 1 44  ? -27.156 12.366 1.009   1.00 18.52 ? 12  LEU   A CA   1 
ATOM   16   C  C    . LEU   A 1 44  ? -25.764 11.819 1.282   1.00 18.99 ? 12  LEU   A C    1 
ATOM   17   O  O    . LEU   A 1 44  ? -25.012 12.400 2.070   1.00 22.41 ? 12  LEU   A O    1 
ATOM   18   C  CB   . LEU   A 1 44  ? -27.061 13.760 0.368   1.00 18.87 ? 12  LEU   A CB   1 
ATOM   19   C  CG   . LEU   A 1 44  ? -26.256 13.872 -0.930  1.00 20.58 ? 12  LEU   A CG   1 
ATOM   20   C  CD1  . LEU   A 1 44  ? -26.903 13.058 -2.029  1.00 20.62 ? 12  LEU   A CD1  1 
ATOM   21   C  CD2  . LEU   A 1 44  ? -26.143 15.338 -1.347  1.00 21.32 ? 12  LEU   A CD2  1 
ATOM   22   N  N    . MET   A 1 45  ? -25.419 10.717 0.622   1.00 17.02 ? 13  MET   A N    1 
ATOM   23   C  CA   . MET   A 1 45  ? -24.102 10.109 0.736   1.00 16.82 ? 13  MET   A CA   1 
ATOM   24   C  C    . MET   A 1 45  ? -23.622 9.769  -0.665  1.00 15.60 ? 13  MET   A C    1 
ATOM   25   O  O    . MET   A 1 45  ? -24.424 9.401  -1.526  1.00 16.91 ? 13  MET   A O    1 
ATOM   26   C  CB   . MET   A 1 45  ? -24.145 8.832  1.605   1.00 20.05 ? 13  MET   A CB   1 
ATOM   27   C  CG   . MET   A 1 45  ? -22.766 8.242  1.943   1.00 23.95 ? 13  MET   A CG   1 
ATOM   28   S  SD   . MET   A 1 45  ? -22.144 7.035  0.748   1.00 28.27 ? 13  MET   A SD   1 
ATOM   29   C  CE   . MET   A 1 45  ? -22.982 5.539  1.287   1.00 30.35 ? 13  MET   A CE   1 
ATOM   30   N  N    . VAL   A 1 46  ? -22.324 9.912  -0.904  1.00 14.94 ? 14  VAL   A N    1 
ATOM   31   C  CA   . VAL   A 1 46  ? -21.734 9.600  -2.203  1.00 14.47 ? 14  VAL   A CA   1 
ATOM   32   C  C    . VAL   A 1 46  ? -20.614 8.596  -1.986  1.00 15.16 ? 14  VAL   A C    1 
ATOM   33   O  O    . VAL   A 1 46  ? -19.783 8.770  -1.085  1.00 16.89 ? 14  VAL   A O    1 
ATOM   34   C  CB   . VAL   A 1 46  ? -21.202 10.855 -2.919  1.00 15.24 ? 14  VAL   A CB   1 
ATOM   35   C  CG1  . VAL   A 1 46  ? -20.669 10.487 -4.309  1.00 16.64 ? 14  VAL   A CG1  1 
ATOM   36   C  CG2  . VAL   A 1 46  ? -22.278 11.926 -3.019  1.00 17.00 ? 14  VAL   A CG2  1 
ATOM   37   N  N    . LYS   A 1 47  ? -20.594 7.550  -2.811  1.00 14.95 ? 15  LYS   A N    1 
ATOM   38   C  CA   . LYS   A 1 47  ? -19.589 6.498  -2.726  1.00 15.90 ? 15  LYS   A CA   1 
ATOM   39   C  C    . LYS   A 1 47  ? -18.943 6.342  -4.093  1.00 15.34 ? 15  LYS   A C    1 
ATOM   40   O  O    . LYS   A 1 47  ? -19.643 6.285  -5.110  1.00 16.62 ? 15  LYS   A O    1 
ATOM   41   C  CB   . LYS   A 1 47  ? -20.209 5.170  -2.283  1.00 19.75 ? 15  LYS   A CB   1 
ATOM   42   C  CG   . LYS   A 1 47  ? -19.178 4.057  -2.181  1.00 25.51 ? 15  LYS   A CG   1 
ATOM   43   C  CD   . LYS   A 1 47  ? -19.588 2.988  -1.179  1.00 30.08 ? 15  LYS   A CD   1 
ATOM   44   C  CE   . LYS   A 1 47  ? -18.443 2.023  -0.891  1.00 32.74 ? 15  LYS   A CE   1 
ATOM   45   N  NZ   . LYS   A 1 47  ? -18.650 1.266  0.380   1.00 36.99 ? 15  LYS   A NZ   1 
ATOM   46   N  N    . VAL   A 1 48  ? -17.616 6.275  -4.122  1.00 14.33 ? 16  VAL   A N    1 
ATOM   47   C  CA   . VAL   A 1 48  ? -16.861 6.274  -5.372  1.00 13.90 ? 16  VAL   A CA   1 
ATOM   48   C  C    . VAL   A 1 48  ? -15.875 5.112  -5.349  1.00 13.82 ? 16  VAL   A C    1 
ATOM   49   O  O    . VAL   A 1 48  ? -15.135 4.933  -4.371  1.00 15.97 ? 16  VAL   A O    1 
ATOM   50   C  CB   . VAL   A 1 48  ? -16.133 7.616  -5.601  1.00 14.80 ? 16  VAL   A CB   1 
ATOM   51   C  CG1  . VAL   A 1 48  ? -15.576 7.694  -7.022  1.00 16.35 ? 16  VAL   A CG1  1 
ATOM   52   C  CG2  . VAL   A 1 48  ? -17.086 8.794  -5.347  1.00 16.52 ? 16  VAL   A CG2  1 
ATOM   53   N  N    . LEU   A 1 49  ? -15.880 4.314  -6.416  1.00 13.91 ? 17  LEU   A N    1 
ATOM   54   C  CA   . LEU   A 1 49  ? -15.014 3.148  -6.548  1.00 14.20 ? 17  LEU   A CA   1 
ATOM   55   C  C    . LEU   A 1 49  ? -14.116 3.285  -7.769  1.00 12.92 ? 17  LEU   A C    1 
ATOM   56   O  O    . LEU   A 1 49  ? -14.471 3.934  -8.755  1.00 14.47 ? 17  LEU   A O    1 
ATOM   57   C  CB   . LEU   A 1 49  ? -15.833 1.860  -6.698  1.00 15.57 ? 17  LEU   A CB   1 
ATOM   58   C  CG   . LEU   A 1 49  ? -16.685 1.425  -5.506  1.00 17.89 ? 17  LEU   A CG   1 
ATOM   59   C  CD1  . LEU   A 1 49  ? -17.320 0.097  -5.839  1.00 21.77 ? 17  LEU   A CD1  1 
ATOM   60   C  CD2  . LEU   A 1 49  ? -15.882 1.309  -4.223  1.00 20.28 ? 17  LEU   A CD2  1 
ATOM   61   N  N    . ASP   A 1 50  ? -12.958 2.644  -7.701  1.00 13.51 ? 18  ASP   A N    1 
ATOM   62   C  CA   . ASP   A 1 50  ? -11.931 2.702  -8.735  1.00 13.11 ? 18  ASP   A CA   1 
ATOM   63   C  C    . ASP   A 1 50  ? -11.900 1.342  -9.430  1.00 13.63 ? 18  ASP   A C    1 
ATOM   64   O  O    . ASP   A 1 50  ? -11.553 0.325  -8.813  1.00 15.01 ? 18  ASP   A O    1 
ATOM   65   C  CB   . ASP   A 1 50  ? -10.590 3.060  -8.085  1.00 14.00 ? 18  ASP   A CB   1 
ATOM   66   C  CG   . ASP   A 1 50  ? -9.426  3.112  -9.064  1.00 15.60 ? 18  ASP   A CG   1 
ATOM   67   O  OD1  . ASP   A 1 50  ? -9.415  2.367  -10.063 1.00 16.07 ? 18  ASP   A OD1  1 
ATOM   68   O  OD2  . ASP   A 1 50  ? -8.481  3.891  -8.794  1.00 18.74 ? 18  ASP   A OD2  1 
ATOM   69   N  N    . ALA   A 1 51  ? -12.275 1.328  -10.710 1.00 13.60 ? 19  ALA   A N    1 
ATOM   70   C  CA   . ALA   A 1 51  ? -12.363 0.097  -11.494 1.00 13.78 ? 19  ALA   A CA   1 
ATOM   71   C  C    . ALA   A 1 51  ? -11.019 -0.362 -12.061 1.00 14.03 ? 19  ALA   A C    1 
ATOM   72   O  O    . ALA   A 1 51  ? -10.929 -1.485 -12.579 1.00 15.84 ? 19  ALA   A O    1 
ATOM   73   C  CB   . ALA   A 1 51  ? -13.381 0.275  -12.627 1.00 14.70 ? 19  ALA   A CB   1 
ATOM   74   N  N    . VAL   A 1 52  ? -9.982  0.464  -11.976 1.00 14.48 ? 20  VAL   A N    1 
ATOM   75   C  CA   . VAL   A 1 52  ? -8.651  0.068  -12.429 1.00 16.13 ? 20  VAL   A CA   1 
ATOM   76   C  C    . VAL   A 1 52  ? -7.901  -0.665 -11.335 1.00 17.28 ? 20  VAL   A C    1 
ATOM   77   O  O    . VAL   A 1 52  ? -7.276  -1.701 -11.582 1.00 19.89 ? 20  VAL   A O    1 
ATOM   78   C  CB   . VAL   A 1 52  ? -7.874  1.312  -12.902 1.00 17.08 ? 20  VAL   A CB   1 
ATOM   79   C  CG1  . VAL   A 1 52  ? -6.412  0.960  -13.162 1.00 19.66 ? 20  VAL   A CG1  1 
ATOM   80   C  CG2  . VAL   A 1 52  ? -8.517  1.877  -14.139 1.00 16.64 ? 20  VAL   A CG2  1 
ATOM   81   N  N    . ARG   A 1 53  ? -7.971  -0.137 -10.117 1.00 16.08 ? 21  ARG   A N    1 
ATOM   82   C  CA   . ARG   A 1 53  ? -7.218  -0.670 -8.999  1.00 17.60 ? 21  ARG   A CA   1 
ATOM   83   C  C    . ARG   A 1 53  ? -8.025  -1.606 -8.113  1.00 17.02 ? 21  ARG   A C    1 
ATOM   84   O  O    . ARG   A 1 53  ? -7.427  -2.314 -7.297  1.00 19.81 ? 21  ARG   A O    1 
ATOM   85   C  CB   . ARG   A 1 53  ? -6.645  0.484  -8.173  1.00 21.12 ? 21  ARG   A CB   1 
ATOM   86   C  CG   . ARG   A 1 53  ? -5.774  1.414  -9.013  1.00 27.10 ? 21  ARG   A CG   1 
ATOM   87   C  CD   . ARG   A 1 53  ? -4.847  2.246  -8.159  1.00 34.46 ? 21  ARG   A CD   1 
ATOM   88   N  NE   . ARG   A 1 53  ? -5.555  3.325  -7.485  1.00 39.24 ? 21  ARG   A NE   1 
ATOM   89   C  CZ   . ARG   A 1 53  ? -5.031  4.060  -6.510  1.00 45.61 ? 21  ARG   A CZ   1 
ATOM   90   N  NH1  . ARG   A 1 53  ? -3.797  3.820  -6.089  1.00 46.40 ? 21  ARG   A NH1  1 
ATOM   91   N  NH2  . ARG   A 1 53  ? -5.744  5.028  -5.950  1.00 48.06 ? 21  ARG   A NH2  1 
ATOM   92   N  N    . GLY   A 1 54  ? -9.349  -1.646 -8.262  1.00 15.00 ? 22  GLY   A N    1 
ATOM   93   C  CA   . GLY   A 1 54  ? -10.175 -2.495 -7.418  1.00 15.64 ? 22  GLY   A CA   1 
ATOM   94   C  C    . GLY   A 1 54  ? -10.156 -2.022 -5.980  1.00 15.82 ? 22  GLY   A C    1 
ATOM   95   O  O    . GLY   A 1 54  ? -9.882  -2.788 -5.054  1.00 17.18 ? 22  GLY   A O    1 
ATOM   96   N  N    . SER   A 1 55  ? -10.452 -0.747 -5.785  1.00 15.67 ? 23  SER   A N    1 
ATOM   97   C  CA   . SER   A 1 55  ? -10.321 -0.136 -4.473  1.00 15.36 ? 23  SER   A CA   1 
ATOM   98   C  C    . SER   A 1 55  ? -11.367 0.953  -4.364  1.00 14.96 ? 23  SER   A C    1 
ATOM   99   O  O    . SER   A 1 55  ? -11.907 1.404  -5.378  1.00 15.98 ? 23  SER   A O    1 
ATOM   100  C  CB   . SER   A 1 55  ? -8.937  0.498  -4.324  1.00 20.00 ? 23  SER   A CB   1 
ATOM   101  O  OG   . SER   A 1 55  ? -8.786  1.549  -5.266  1.00 24.10 ? 23  SER   A OG   1 
ATOM   102  N  N    . PRO   A 1 56  ? -11.661 1.416  -3.155  1.00 15.54 ? 24  PRO   A N    1 
ATOM   103  C  CA   . PRO   A 1 56  ? -12.361 2.695  -3.032  1.00 15.50 ? 24  PRO   A CA   1 
ATOM   104  C  C    . PRO   A 1 56  ? -11.542 3.770  -3.723  1.00 15.55 ? 24  PRO   A C    1 
ATOM   105  O  O    . PRO   A 1 56  ? -10.314 3.693  -3.794  1.00 16.81 ? 24  PRO   A O    1 
ATOM   106  C  CB   . PRO   A 1 56  ? -12.409 2.936  -1.518  1.00 17.14 ? 24  PRO   A CB   1 
ATOM   107  C  CG   . PRO   A 1 56  ? -12.163 1.618  -0.905  1.00 22.59 ? 24  PRO   A CG   1 
ATOM   108  C  CD   . PRO   A 1 56  ? -11.281 0.864  -1.845  1.00 17.94 ? 24  PRO   A CD   1 
ATOM   109  N  N    . ALA   A 1 57  ? -12.228 4.780  -4.244  1.00 15.48 ? 25  ALA   A N    1 
ATOM   110  C  CA   . ALA   A 1 57  ? -11.554 5.953  -4.784  1.00 15.29 ? 25  ALA   A CA   1 
ATOM   111  C  C    . ALA   A 1 57  ? -11.430 6.950  -3.639  1.00 15.18 ? 25  ALA   A C    1 
ATOM   112  O  O    . ALA   A 1 57  ? -12.417 7.568  -3.239  1.00 16.36 ? 25  ALA   A O    1 
ATOM   113  C  CB   . ALA   A 1 57  ? -12.326 6.533  -5.963  1.00 16.76 ? 25  ALA   A CB   1 
ATOM   114  N  N    . ILE   A 1 58  ? -10.218 7.086  -3.104  1.00 15.24 ? 26  ILE   A N    1 
ATOM   115  C  CA   . ILE   A 1 58  ? -9.951  7.843  -1.890  1.00 17.37 ? 26  ILE   A CA   1 
ATOM   116  C  C    . ILE   A 1 58  ? -9.542  9.265  -2.255  1.00 18.19 ? 26  ILE   A C    1 
ATOM   117  O  O    . ILE   A 1 58  ? -8.890  9.507  -3.277  1.00 19.46 ? 26  ILE   A O    1 
ATOM   118  C  CB   . ILE   A 1 58  ? -8.853  7.122  -1.077  1.00 20.35 ? 26  ILE   A CB   1 
ATOM   119  C  CG1  . ILE   A 1 58  ? -9.281  5.687  -0.740  1.00 20.56 ? 26  ILE   A CG1  1 
ATOM   120  C  CG2  . ILE   A 1 58  ? -8.514  7.875  0.195   1.00 24.37 ? 26  ILE   A CG2  1 
ATOM   121  C  CD1  . ILE   A 1 58  ? -8.218  4.913  0.007   1.00 24.25 ? 26  ILE   A CD1  1 
ATOM   122  N  N    . ASN   A 1 59  ? -9.937  10.216 -1.405  1.00 18.53 ? 27  ASN   A N    1 
ATOM   123  C  CA   A ASN   A 1 59  ? -9.565  11.626 -1.549  0.50 21.15 ? 27  ASN   A CA   1 
ATOM   124  C  CA   B ASN   A 1 59  ? -9.549  11.622 -1.558  0.50 20.05 ? 27  ASN   A CA   1 
ATOM   125  C  C    . ASN   A 1 59  ? -10.056 12.230 -2.862  1.00 19.47 ? 27  ASN   A C    1 
ATOM   126  O  O    . ASN   A 1 59  ? -9.397  13.084 -3.464  1.00 21.51 ? 27  ASN   A O    1 
ATOM   127  C  CB   A ASN   A 1 59  ? -8.069  11.859 -1.342  0.50 25.47 ? 27  ASN   A CB   1 
ATOM   128  C  CB   B ASN   A 1 59  ? -8.040  11.823 -1.409  0.50 22.07 ? 27  ASN   A CB   1 
ATOM   129  C  CG   A ASN   A 1 59  ? -7.745  12.283 0.073   0.50 30.69 ? 27  ASN   A CG   1 
ATOM   130  C  CG   B ASN   A 1 59  ? -7.547  11.481 -0.023  0.50 25.50 ? 27  ASN   A CG   1 
ATOM   131  O  OD1  A ASN   A 1 59  ? -7.793  13.467 0.403   0.50 34.04 ? 27  ASN   A OD1  1 
ATOM   132  O  OD1  B ASN   A 1 59  ? -8.274  11.631 0.961   0.50 26.80 ? 27  ASN   A OD1  1 
ATOM   133  N  ND2  A ASN   A 1 59  ? -7.423  11.313 0.923   0.50 32.47 ? 27  ASN   A ND2  1 
ATOM   134  N  ND2  B ASN   A 1 59  ? -6.305  11.020 0.066   0.50 26.98 ? 27  ASN   A ND2  1 
ATOM   135  N  N    . VAL   A 1 60  ? -11.228 11.803 -3.302  1.00 17.06 ? 28  VAL   A N    1 
ATOM   136  C  CA   . VAL   A 1 60  ? -11.865 12.363 -4.487  1.00 16.37 ? 28  VAL   A CA   1 
ATOM   137  C  C    . VAL   A 1 60  ? -12.698 13.562 -4.053  1.00 15.31 ? 28  VAL   A C    1 
ATOM   138  O  O    . VAL   A 1 60  ? -13.595 13.429 -3.212  1.00 15.49 ? 28  VAL   A O    1 
ATOM   139  C  CB   . VAL   A 1 60  ? -12.749 11.316 -5.176  1.00 16.80 ? 28  VAL   A CB   1 
ATOM   140  C  CG1  . VAL   A 1 60  ? -13.501 11.955 -6.313  1.00 18.31 ? 28  VAL   A CG1  1 
ATOM   141  C  CG2  . VAL   A 1 60  ? -11.905 10.158 -5.661  1.00 18.64 ? 28  VAL   A CG2  1 
ATOM   142  N  N    . ALA   A 1 61  ? -12.423 14.725 -4.635  1.00 15.51 ? 29  ALA   A N    1 
ATOM   143  C  CA   . ALA   A 1 61  ? -13.187 15.917 -4.300  1.00 14.24 ? 29  ALA   A CA   1 
ATOM   144  C  C    . ALA   A 1 61  ? -14.486 15.948 -5.090  1.00 13.82 ? 29  ALA   A C    1 
ATOM   145  O  O    . ALA   A 1 61  ? -14.552 15.485 -6.233  1.00 15.89 ? 29  ALA   A O    1 
ATOM   146  C  CB   . ALA   A 1 61  ? -12.381 17.171 -4.638  1.00 15.86 ? 29  ALA   A CB   1 
ATOM   147  N  N    . MET   A 1 62  ? -15.519 16.524 -4.481  1.00 13.43 ? 30  MET   A N    1 
ATOM   148  C  CA   . MET   A 1 62  ? -16.756 16.760 -5.212  1.00 14.09 ? 30  MET   A CA   1 
ATOM   149  C  C    . MET   A 1 62  ? -17.478 17.977 -4.656  1.00 14.29 ? 30  MET   A C    1 
ATOM   150  O  O    . MET   A 1 62  ? -17.342 18.326 -3.478  1.00 15.05 ? 30  MET   A O    1 
ATOM   151  C  CB   . MET   A 1 62  ? -17.688 15.549 -5.194  1.00 15.86 ? 30  MET   A CB   1 
ATOM   152  C  CG   . MET   A 1 62  ? -18.274 15.243 -3.828  1.00 16.46 ? 30  MET   A CG   1 
ATOM   153  S  SD   . MET   A 1 62  ? -19.039 13.608 -3.826  1.00 17.51 ? 30  MET   A SD   1 
ATOM   154  C  CE   . MET   A 1 62  ? -17.592 12.559 -3.723  1.00 18.59 ? 30  MET   A CE   1 
ATOM   155  N  N    . HIS   A 1 63  ? -18.233 18.629 -5.529  1.00 14.47 ? 31  HIS   A N    1 
ATOM   156  C  CA   . HIS   A 1 63  ? -19.042 19.779 -5.165  1.00 14.74 ? 31  HIS   A CA   1 
ATOM   157  C  C    . HIS   A 1 63  ? -20.493 19.486 -5.498  1.00 14.70 ? 31  HIS   A C    1 
ATOM   158  O  O    . HIS   A 1 63  ? -20.791 18.920 -6.553  1.00 16.11 ? 31  HIS   A O    1 
ATOM   159  C  CB   . HIS   A 1 63  ? -18.578 21.027 -5.924  1.00 18.25 ? 31  HIS   A CB   1 
ATOM   160  C  CG   . HIS   A 1 63  ? -17.298 21.604 -5.401  1.00 22.31 ? 31  HIS   A CG   1 
ATOM   161  N  ND1  . HIS   A 1 63  ? -16.069 21.041 -5.662  1.00 25.46 ? 31  HIS   A ND1  1 
ATOM   162  C  CD2  . HIS   A 1 63  ? -17.060 22.684 -4.620  1.00 23.70 ? 31  HIS   A CD2  1 
ATOM   163  C  CE1  . HIS   A 1 63  ? -15.126 21.753 -5.072  1.00 26.24 ? 31  HIS   A CE1  1 
ATOM   164  N  NE2  . HIS   A 1 63  ? -15.700 22.758 -4.434  1.00 26.08 ? 31  HIS   A NE2  1 
ATOM   165  N  N    . VAL   A 1 64  ? -21.392 19.872 -4.594  1.00 14.16 ? 32  VAL   A N    1 
ATOM   166  C  CA   . VAL   A 1 64  ? -22.827 19.712 -4.788  1.00 14.05 ? 32  VAL   A CA   1 
ATOM   167  C  C    . VAL   A 1 64  ? -23.430 21.093 -4.991  1.00 14.46 ? 32  VAL   A C    1 
ATOM   168  O  O    . VAL   A 1 64  ? -23.089 22.044 -4.275  1.00 15.49 ? 32  VAL   A O    1 
ATOM   169  C  CB   . VAL   A 1 64  ? -23.492 18.991 -3.601  1.00 15.10 ? 32  VAL   A CB   1 
ATOM   170  C  CG1  . VAL   A 1 64  ? -24.942 18.688 -3.917  1.00 15.72 ? 32  VAL   A CG1  1 
ATOM   171  C  CG2  . VAL   A 1 64  ? -22.738 17.716 -3.261  1.00 16.12 ? 32  VAL   A CG2  1 
ATOM   172  N  N    . PHE   A 1 65  ? -24.319 21.202 -5.970  1.00 14.32 ? 33  PHE   A N    1 
ATOM   173  C  CA   . PHE   A 1 65  ? -24.986 22.451 -6.295  1.00 15.27 ? 33  PHE   A CA   1 
ATOM   174  C  C    . PHE   A 1 65  ? -26.486 22.215 -6.271  1.00 15.95 ? 33  PHE   A C    1 
ATOM   175  O  O    . PHE   A 1 65  ? -26.957 21.090 -6.433  1.00 16.02 ? 33  PHE   A O    1 
ATOM   176  C  CB   . PHE   A 1 65  ? -24.591 22.955 -7.696  1.00 16.81 ? 33  PHE   A CB   1 
ATOM   177  C  CG   . PHE   A 1 65  ? -23.106 23.115 -7.892  1.00 17.09 ? 33  PHE   A CG   1 
ATOM   178  C  CD1  . PHE   A 1 65  ? -22.331 22.031 -8.274  1.00 17.53 ? 33  PHE   A CD1  1 
ATOM   179  C  CD2  . PHE   A 1 65  ? -22.482 24.340 -7.689  1.00 18.85 ? 33  PHE   A CD2  1 
ATOM   180  C  CE1  . PHE   A 1 65  ? -20.959 22.161 -8.463  1.00 18.64 ? 33  PHE   A CE1  1 
ATOM   181  C  CE2  . PHE   A 1 65  ? -21.107 24.478 -7.871  1.00 19.99 ? 33  PHE   A CE2  1 
ATOM   182  C  CZ   . PHE   A 1 65  ? -20.349 23.389 -8.250  1.00 19.84 ? 33  PHE   A CZ   1 
ATOM   183  N  N    . ARG   A 1 66  ? -27.238 23.291 -6.059  1.00 16.61 ? 34  ARG   A N    1 
ATOM   184  C  CA   . ARG   A 1 66  ? -28.691 23.242 -6.100  1.00 17.40 ? 34  ARG   A CA   1 
ATOM   185  C  C    . ARG   A 1 66  ? -29.191 24.348 -7.015  1.00 17.20 ? 34  ARG   A C    1 
ATOM   186  O  O    . ARG   A 1 66  ? -28.696 25.476 -6.959  1.00 18.82 ? 34  ARG   A O    1 
ATOM   187  C  CB   . ARG   A 1 66  ? -29.277 23.434 -4.703  1.00 18.78 ? 34  ARG   A CB   1 
ATOM   188  C  CG   . ARG   A 1 66  ? -30.782 23.321 -4.660  1.00 20.72 ? 34  ARG   A CG   1 
ATOM   189  C  CD   . ARG   A 1 66  ? -31.327 23.619 -3.280  1.00 22.07 ? 34  ARG   A CD   1 
ATOM   190  N  NE   . ARG   A 1 66  ? -32.781 23.547 -3.314  1.00 23.24 ? 34  ARG   A NE   1 
ATOM   191  C  CZ   . ARG   A 1 66  ? -33.577 24.560 -3.632  1.00 22.19 ? 34  ARG   A CZ   1 
ATOM   192  N  NH1  . ARG   A 1 66  ? -33.067 25.757 -3.918  1.00 23.07 ? 34  ARG   A NH1  1 
ATOM   193  N  NH2  . ARG   A 1 66  ? -34.889 24.371 -3.660  1.00 21.71 ? 34  ARG   A NH2  1 
ATOM   194  N  N    . LYS   A 1 67  ? -30.178 24.029 -7.849  1.00 16.89 ? 35  LYS   A N    1 
ATOM   195  C  CA   . LYS   A 1 67  ? -30.676 25.006 -8.812  1.00 19.79 ? 35  LYS   A CA   1 
ATOM   196  C  C    . LYS   A 1 67  ? -31.480 26.080 -8.086  1.00 19.07 ? 35  LYS   A C    1 
ATOM   197  O  O    . LYS   A 1 67  ? -32.410 25.773 -7.334  1.00 19.74 ? 35  LYS   A O    1 
ATOM   198  C  CB   . LYS   A 1 67  ? -31.550 24.302 -9.850  1.00 24.95 ? 35  LYS   A CB   1 
ATOM   199  C  CG   . LYS   A 1 67  ? -31.711 25.036 -11.172 1.00 32.34 ? 35  LYS   A CG   1 
ATOM   200  C  CD   . LYS   A 1 67  ? -30.507 24.800 -12.079 1.00 37.42 ? 35  LYS   A CD   1 
ATOM   201  C  CE   . LYS   A 1 67  ? -30.902 24.785 -13.552 1.00 41.22 ? 35  LYS   A CE   1 
ATOM   202  N  NZ   . LYS   A 1 67  ? -31.698 23.578 -13.914 1.00 43.17 ? 35  LYS   A NZ   1 
ATOM   203  N  N    . ALA   A 1 68  ? -31.111 27.342 -8.300  1.00 20.69 ? 36  ALA   A N    1 
ATOM   204  C  CA   . ALA   A 1 68  ? -31.798 28.456 -7.667  1.00 23.61 ? 36  ALA   A CA   1 
ATOM   205  C  C    . ALA   A 1 68  ? -33.041 28.835 -8.464  1.00 25.47 ? 36  ALA   A C    1 
ATOM   206  O  O    . ALA   A 1 68  ? -33.291 28.326 -9.561  1.00 25.37 ? 36  ALA   A O    1 
ATOM   207  C  CB   . ALA   A 1 68  ? -30.874 29.667 -7.573  1.00 24.87 ? 36  ALA   A CB   1 
ATOM   208  N  N    . ALA   A 1 69  ? -33.822 29.761 -7.896  1.00 29.34 ? 37  ALA   A N    1 
ATOM   209  C  CA   . ALA   A 1 69  ? -35.044 30.212 -8.551  1.00 32.88 ? 37  ALA   A CA   1 
ATOM   210  C  C    . ALA   A 1 69  ? -34.758 30.835 -9.910  1.00 34.52 ? 37  ALA   A C    1 
ATOM   211  O  O    . ALA   A 1 69  ? -35.605 30.776 -10.809 1.00 36.01 ? 37  ALA   A O    1 
ATOM   212  C  CB   . ALA   A 1 69  ? -35.788 31.208 -7.660  1.00 33.71 ? 37  ALA   A CB   1 
ATOM   213  N  N    . ASP   A 1 70  ? -33.592 31.457 -10.074 1.00 35.05 ? 38  ASP   A N    1 
ATOM   214  C  CA   . ASP   A 1 70  ? -33.220 32.056 -11.349 1.00 37.95 ? 38  ASP   A CA   1 
ATOM   215  C  C    . ASP   A 1 70  ? -32.564 31.068 -12.312 1.00 38.63 ? 38  ASP   A C    1 
ATOM   216  O  O    . ASP   A 1 70  ? -31.982 31.499 -13.314 1.00 38.76 ? 38  ASP   A O    1 
ATOM   217  C  CB   . ASP   A 1 70  ? -32.333 33.289 -11.133 1.00 40.36 ? 38  ASP   A CB   1 
ATOM   218  C  CG   . ASP   A 1 70  ? -31.019 32.959 -10.447 1.00 43.28 ? 38  ASP   A CG   1 
ATOM   219  O  OD1  . ASP   A 1 70  ? -30.744 31.768 -10.199 1.00 42.71 ? 38  ASP   A OD1  1 
ATOM   220  O  OD2  . ASP   A 1 70  ? -30.253 33.901 -10.157 1.00 44.96 ? 38  ASP   A OD2  1 
ATOM   221  N  N    . ASP   A 1 71  ? -32.637 29.768 -12.025 1.00 39.49 ? 39  ASP   A N    1 
ATOM   222  C  CA   . ASP   A 1 71  ? -32.110 28.686 -12.856 1.00 43.33 ? 39  ASP   A CA   1 
ATOM   223  C  C    . ASP   A 1 71  ? -30.589 28.589 -12.875 1.00 40.08 ? 39  ASP   A C    1 
ATOM   224  O  O    . ASP   A 1 71  ? -30.039 27.839 -13.693 1.00 41.81 ? 39  ASP   A O    1 
ATOM   225  C  CB   . ASP   A 1 71  ? -32.676 28.672 -14.283 1.00 50.77 ? 39  ASP   A CB   1 
ATOM   226  C  CG   . ASP   A 1 71  ? -34.053 28.045 -14.355 1.00 57.55 ? 39  ASP   A CG   1 
ATOM   227  O  OD1  . ASP   A 1 71  ? -35.050 28.770 -14.157 1.00 60.04 ? 39  ASP   A OD1  1 
ATOM   228  O  OD2  . ASP   A 1 71  ? -34.135 26.822 -14.602 1.00 59.78 ? 39  ASP   A OD2  1 
ATOM   229  N  N    . THR   A 1 72  ? -29.888 29.309 -12.007 1.00 34.70 ? 40  THR   A N    1 
ATOM   230  C  CA   . THR   A 1 72  ? -28.449 29.124 -11.906 1.00 32.43 ? 40  THR   A CA   1 
ATOM   231  C  C    . THR   A 1 72  ? -28.129 28.097 -10.823 1.00 27.46 ? 40  THR   A C    1 
ATOM   232  O  O    . THR   A 1 72  ? -28.955 27.786 -9.963  1.00 26.08 ? 40  THR   A O    1 
ATOM   233  C  CB   . THR   A 1 72  ? -27.749 30.449 -11.602 1.00 34.65 ? 40  THR   A CB   1 
ATOM   234  O  OG1  . THR   A 1 72  ? -28.106 30.887 -10.286 1.00 35.87 ? 40  THR   A OG1  1 
ATOM   235  C  CG2  . THR   A 1 72  ? -28.159 31.509 -12.616 1.00 37.01 ? 40  THR   A CG2  1 
ATOM   236  N  N    . TRP   A 1 73  ? -26.910 27.566 -10.876 1.00 24.78 ? 41  TRP   A N    1 
ATOM   237  C  CA   . TRP   A 1 73  ? -26.450 26.584 -9.905  1.00 23.18 ? 41  TRP   A CA   1 
ATOM   238  C  C    . TRP   A 1 73  ? -25.844 27.306 -8.709  1.00 24.77 ? 41  TRP   A C    1 
ATOM   239  O  O    . TRP   A 1 73  ? -24.872 28.053 -8.861  1.00 30.02 ? 41  TRP   A O    1 
ATOM   240  C  CB   . TRP   A 1 73  ? -25.404 25.665 -10.533 1.00 22.83 ? 41  TRP   A CB   1 
ATOM   241  C  CG   . TRP   A 1 73  ? -25.985 24.702 -11.508 1.00 24.86 ? 41  TRP   A CG   1 
ATOM   242  C  CD1  . TRP   A 1 73  ? -25.791 24.686 -12.855 1.00 26.58 ? 41  TRP   A CD1  1 
ATOM   243  C  CD2  . TRP   A 1 73  ? -26.870 23.610 -11.215 1.00 22.91 ? 41  TRP   A CD2  1 
ATOM   244  N  NE1  . TRP   A 1 73  ? -26.494 23.651 -13.422 1.00 27.99 ? 41  TRP   A NE1  1 
ATOM   245  C  CE2  . TRP   A 1 73  ? -27.168 22.976 -12.437 1.00 24.90 ? 41  TRP   A CE2  1 
ATOM   246  C  CE3  . TRP   A 1 73  ? -27.441 23.111 -10.039 1.00 20.72 ? 41  TRP   A CE3  1 
ATOM   247  C  CZ2  . TRP   A 1 73  ? -28.002 21.864 -12.518 1.00 25.32 ? 41  TRP   A CZ2  1 
ATOM   248  C  CZ3  . TRP   A 1 73  ? -28.271 22.009 -10.121 1.00 21.43 ? 41  TRP   A CZ3  1 
ATOM   249  C  CH2  . TRP   A 1 73  ? -28.546 21.399 -11.353 1.00 24.00 ? 41  TRP   A CH2  1 
ATOM   250  N  N    . GLU   A 1 74  ? -26.416 27.088 -7.530  1.00 22.68 ? 42  GLU   A N    1 
ATOM   251  C  CA   . GLU   A 1 74  ? -25.850 27.694 -6.336  1.00 25.50 ? 42  GLU   A CA   1 
ATOM   252  C  C    . GLU   A 1 74  ? -25.057 26.659 -5.550  1.00 22.42 ? 42  GLU   A C    1 
ATOM   253  O  O    . GLU   A 1 74  ? -25.447 25.489 -5.497  1.00 21.22 ? 42  GLU   A O    1 
ATOM   254  C  CB   . GLU   A 1 74  ? -26.963 28.229 -5.439  1.00 32.05 ? 42  GLU   A CB   1 
ATOM   255  C  CG   . GLU   A 1 74  ? -27.721 29.394 -6.041  1.00 39.91 ? 42  GLU   A CG   1 
ATOM   256  C  CD   . GLU   A 1 74  ? -28.666 30.045 -5.053  1.00 46.66 ? 42  GLU   A CD   1 
ATOM   257  O  OE1  . GLU   A 1 74  ? -28.685 31.292 -4.981  1.00 48.71 ? 42  GLU   A OE1  1 
ATOM   258  O  OE2  . GLU   A 1 74  ? -29.390 29.307 -4.349  1.00 49.64 ? 42  GLU   A OE2  1 
ATOM   259  N  N    . PRO   A 1 75  ? -23.945 27.044 -4.924  1.00 22.19 ? 43  PRO   A N    1 
ATOM   260  C  CA   . PRO   A 1 75  ? -23.201 26.086 -4.092  1.00 23.22 ? 43  PRO   A CA   1 
ATOM   261  C  C    . PRO   A 1 75  ? -24.070 25.561 -2.957  1.00 23.27 ? 43  PRO   A C    1 
ATOM   262  O  O    . PRO   A 1 75  ? -24.789 26.315 -2.297  1.00 27.24 ? 43  PRO   A O    1 
ATOM   263  C  CB   . PRO   A 1 75  ? -22.027 26.915 -3.556  1.00 24.50 ? 43  PRO   A CB   1 
ATOM   264  C  CG   . PRO   A 1 75  ? -21.927 28.089 -4.468  1.00 27.56 ? 43  PRO   A CG   1 
ATOM   265  C  CD   . PRO   A 1 75  ? -23.304 28.368 -4.966  1.00 24.04 ? 43  PRO   A CD   1 
ATOM   266  N  N    . PHE   A 1 76  ? -24.013 24.247 -2.746  1.00 19.52 ? 44  PHE   A N    1 
ATOM   267  C  CA   . PHE   A 1 76  ? -24.803 23.598 -1.706  1.00 18.32 ? 44  PHE   A CA   1 
ATOM   268  C  C    . PHE   A 1 76  ? -23.937 22.921 -0.655  1.00 17.42 ? 44  PHE   A C    1 
ATOM   269  O  O    . PHE   A 1 76  ? -24.159 23.110 0.544   1.00 20.20 ? 44  PHE   A O    1 
ATOM   270  C  CB   . PHE   A 1 76  ? -25.806 22.601 -2.327  1.00 18.20 ? 44  PHE   A CB   1 
ATOM   271  C  CG   . PHE   A 1 76  ? -26.692 21.936 -1.317  1.00 18.79 ? 44  PHE   A CG   1 
ATOM   272  C  CD1  . PHE   A 1 76  ? -27.777 22.611 -0.773  1.00 19.62 ? 44  PHE   A CD1  1 
ATOM   273  C  CD2  . PHE   A 1 76  ? -26.439 20.636 -0.899  1.00 19.55 ? 44  PHE   A CD2  1 
ATOM   274  C  CE1  . PHE   A 1 76  ? -28.587 22.003 0.168   1.00 21.28 ? 44  PHE   A CE1  1 
ATOM   275  C  CE2  . PHE   A 1 76  ? -27.249 20.023 0.043   1.00 19.02 ? 44  PHE   A CE2  1 
ATOM   276  C  CZ   . PHE   A 1 76  ? -28.325 20.712 0.577   1.00 20.65 ? 44  PHE   A CZ   1 
ATOM   277  N  N    . ALA   A 1 77  ? -22.944 22.146 -1.068  1.00 16.56 ? 45  ALA   A N    1 
ATOM   278  C  CA   . ALA   A 1 77  ? -22.035 21.484 -0.141  1.00 16.02 ? 45  ALA   A CA   1 
ATOM   279  C  C    . ALA   A 1 77  ? -20.862 20.942 -0.944  1.00 14.35 ? 45  ALA   A C    1 
ATOM   280  O  O    . ALA   A 1 77  ? -20.921 20.854 -2.173  1.00 16.95 ? 45  ALA   A O    1 
ATOM   281  C  CB   . ALA   A 1 77  ? -22.729 20.357 0.628   1.00 18.48 ? 45  ALA   A CB   1 
ATOM   282  N  N    . SER   A 1 78  ? -19.793 20.580 -0.238  1.00 14.89 ? 46  SER   A N    1 
ATOM   283  C  CA   . SER   A 1 78  ? -18.656 19.938 -0.892  1.00 13.57 ? 46  SER   A CA   1 
ATOM   284  C  C    . SER   A 1 78  ? -17.896 19.102 0.130   1.00 14.53 ? 46  SER   A C    1 
ATOM   285  O  O    . SER   A 1 78  ? -18.098 19.224 1.341   1.00 15.81 ? 46  SER   A O    1 
ATOM   286  C  CB   . SER   A 1 78  ? -17.745 20.953 -1.607  1.00 15.37 ? 46  SER   A CB   1 
ATOM   287  O  OG   . SER   A 1 78  ? -17.168 21.869 -0.694  1.00 17.19 ? 46  SER   A OG   1 
ATOM   288  N  N    . GLY   A 1 79  ? -17.019 18.244 -0.378  1.00 14.31 ? 47  GLY   A N    1 
ATOM   289  C  CA   . GLY   A 1 79  ? -16.206 17.419 0.490   1.00 14.62 ? 47  GLY   A CA   1 
ATOM   290  C  C    . GLY   A 1 79  ? -15.349 16.490 -0.340  1.00 14.91 ? 47  GLY   A C    1 
ATOM   291  O  O    . GLY   A 1 79  ? -15.318 16.578 -1.572  1.00 15.54 ? 47  GLY   A O    1 
ATOM   292  N  N    . LYS   A 1 80  ? -14.641 15.594 0.347   1.00 15.95 ? 48  LYS   A N    1 
ATOM   293  C  CA   . LYS   A 1 80  ? -13.841 14.588 -0.332  1.00 17.72 ? 48  LYS   A CA   1 
ATOM   294  C  C    . LYS   A 1 80  ? -14.078 13.221 0.290   1.00 17.28 ? 48  LYS   A C    1 
ATOM   295  O  O    . LYS   A 1 80  ? -14.387 13.102 1.480   1.00 18.18 ? 48  LYS   A O    1 
ATOM   296  C  CB   . LYS   A 1 80  ? -12.357 14.924 -0.346  1.00 23.60 ? 48  LYS   A CB   1 
ATOM   297  C  CG   . LYS   A 1 80  ? -11.743 15.137 1.007   1.00 30.99 ? 48  LYS   A CG   1 
ATOM   298  C  CD   . LYS   A 1 80  ? -10.260 15.473 0.871   1.00 37.35 ? 48  LYS   A CD   1 
ATOM   299  C  CE   . LYS   A 1 80  ? -9.991  16.345 -0.352  1.00 41.15 ? 48  LYS   A CE   1 
ATOM   300  N  NZ   . LYS   A 1 80  ? -8.540  16.670 -0.530  1.00 43.28 ? 48  LYS   A NZ   1 
ATOM   301  N  N    . THR   A 1 81  ? -13.952 12.189 -0.538  1.00 15.66 ? 49  THR   A N    1 
ATOM   302  C  CA   . THR   A 1 81  ? -14.168 10.830 -0.058  1.00 15.54 ? 49  THR   A CA   1 
ATOM   303  C  C    . THR   A 1 81  ? -13.085 10.414 0.934   1.00 17.02 ? 49  THR   A C    1 
ATOM   304  O  O    . THR   A 1 81  ? -11.926 10.833 0.852   1.00 17.94 ? 49  THR   A O    1 
ATOM   305  C  CB   . THR   A 1 81  ? -14.200 9.832  -1.217  1.00 15.04 ? 49  THR   A CB   1 
ATOM   306  O  OG1  . THR   A 1 81  ? -12.957 9.869  -1.930  1.00 15.81 ? 49  THR   A OG1  1 
ATOM   307  C  CG2  . THR   A 1 81  ? -15.353 10.125 -2.163  1.00 16.05 ? 49  THR   A CG2  1 
ATOM   308  N  N    . SER   A 1 82  ? -13.486 9.564  1.870   1.00 17.02 ? 50  SER   A N    1 
ATOM   309  C  CA   . SER   A 1 82  ? -12.624 9.016  2.905   1.00 18.16 ? 50  SER   A CA   1 
ATOM   310  C  C    . SER   A 1 82  ? -11.862 7.804  2.372   1.00 20.10 ? 50  SER   A C    1 
ATOM   311  O  O    . SER   A 1 82  ? -11.927 7.456  1.189   1.00 18.53 ? 50  SER   A O    1 
ATOM   312  C  CB   . SER   A 1 82  ? -13.491 8.574  4.073   1.00 21.45 ? 50  SER   A CB   1 
ATOM   313  O  OG   . SER   A 1 82  ? -14.258 7.447  3.677   1.00 23.54 ? 50  SER   A OG   1 
ATOM   314  N  N    . GLU   A 1 83  ? -11.146 7.125  3.271   1.00 22.16 ? 51  GLU   A N    1 
ATOM   315  C  CA   . GLU   A 1 83  ? -10.425 5.910  2.905   1.00 24.54 ? 51  GLU   A CA   1 
ATOM   316  C  C    . GLU   A 1 83  ? -11.354 4.790  2.454   1.00 23.83 ? 51  GLU   A C    1 
ATOM   317  O  O    . GLU   A 1 83  ? -10.890 3.839  1.813   1.00 25.41 ? 51  GLU   A O    1 
ATOM   318  C  CB   . GLU   A 1 83  ? -9.575  5.413  4.077   1.00 32.31 ? 51  GLU   A CB   1 
ATOM   319  C  CG   . GLU   A 1 83  ? -8.756  6.481  4.770   1.00 42.21 ? 51  GLU   A CG   1 
ATOM   320  C  CD   . GLU   A 1 83  ? -9.470  7.065  5.977   1.00 49.77 ? 51  GLU   A CD   1 
ATOM   321  O  OE1  . GLU   A 1 83  ? -10.137 8.116  5.834   1.00 51.52 ? 51  GLU   A OE1  1 
ATOM   322  O  OE2  . GLU   A 1 83  ? -9.371  6.462  7.068   1.00 52.88 ? 51  GLU   A OE2  1 
ATOM   323  N  N    . SER   A 1 84  ? -12.643 4.868  2.783   1.00 21.52 ? 52  SER   A N    1 
ATOM   324  C  CA   . SER   A 1 84  ? -13.635 3.907  2.321   1.00 20.51 ? 52  SER   A CA   1 
ATOM   325  C  C    . SER   A 1 84  ? -14.257 4.312  0.992   1.00 18.37 ? 52  SER   A C    1 
ATOM   326  O  O    . SER   A 1 84  ? -15.138 3.605  0.491   1.00 19.87 ? 52  SER   A O    1 
ATOM   327  C  CB   . SER   A 1 84  ? -14.743 3.756  3.366   1.00 23.23 ? 52  SER   A CB   1 
ATOM   328  O  OG   . SER   A 1 84  ? -15.513 4.942  3.427   1.00 27.07 ? 52  SER   A OG   1 
ATOM   329  N  N    . GLY   A 1 85  ? -13.832 5.437  0.416   1.00 16.16 ? 53  GLY   A N    1 
ATOM   330  C  CA   . GLY   A 1 85  ? -14.442 5.927  -0.800  1.00 15.51 ? 53  GLY   A CA   1 
ATOM   331  C  C    . GLY   A 1 85  ? -15.768 6.614  -0.595  1.00 15.13 ? 53  GLY   A C    1 
ATOM   332  O  O    . GLY   A 1 85  ? -16.444 6.922  -1.579  1.00 15.44 ? 53  GLY   A O    1 
ATOM   333  N  N    . GLU   A 1 86  ? -16.150 6.899  0.645   1.00 15.80 ? 54  GLU   A N    1 
ATOM   334  C  CA   . GLU   A 1 86  ? -17.458 7.461  0.945   1.00 15.63 ? 54  GLU   A CA   1 
ATOM   335  C  C    . GLU   A 1 86  ? -17.333 8.888  1.449   1.00 14.92 ? 54  GLU   A C    1 
ATOM   336  O  O    . GLU   A 1 86  ? -16.348 9.257  2.092   1.00 17.28 ? 54  GLU   A O    1 
ATOM   337  C  CB   . GLU   A 1 86  ? -18.197 6.597  1.970   1.00 18.72 ? 54  GLU   A CB   1 
ATOM   338  C  CG   . GLU   A 1 86  ? -18.378 5.170  1.463   1.00 24.40 ? 54  GLU   A CG   1 
ATOM   339  C  CD   . GLU   A 1 86  ? -19.112 4.260  2.426   1.00 29.42 ? 54  GLU   A CD   1 
ATOM   340  O  OE1  . GLU   A 1 86  ? -19.415 4.694  3.553   1.00 31.81 ? 54  GLU   A OE1  1 
ATOM   341  O  OE2  . GLU   A 1 86  ? -19.379 3.096  2.053   1.00 32.93 ? 54  GLU   A OE2  1 
ATOM   342  N  N    . LEU   A 1 87  ? -18.337 9.696  1.127   1.00 15.37 ? 55  LEU   A N    1 
ATOM   343  C  CA   . LEU   A 1 87  ? -18.440 11.059 1.632   1.00 14.83 ? 55  LEU   A CA   1 
ATOM   344  C  C    . LEU   A 1 87  ? -19.771 11.163 2.355   1.00 16.43 ? 55  LEU   A C    1 
ATOM   345  O  O    . LEU   A 1 87  ? -20.830 11.096 1.723   1.00 16.14 ? 55  LEU   A O    1 
ATOM   346  C  CB   . LEU   A 1 87  ? -18.337 12.071 0.493   1.00 15.61 ? 55  LEU   A CB   1 
ATOM   347  C  CG   . LEU   A 1 87  ? -18.575 13.536 0.863   1.00 15.53 ? 55  LEU   A CG   1 
ATOM   348  C  CD1  . LEU   A 1 87  ? -17.749 13.946 2.089   1.00 17.84 ? 55  LEU   A CD1  1 
ATOM   349  C  CD2  . LEU   A 1 87  ? -18.248 14.420 -0.342  1.00 16.24 ? 55  LEU   A CD2  1 
ATOM   350  N  N    . HIS   A 1 88  ? -19.705 11.296 3.677   1.00 18.53 ? 56  HIS   A N    1 
ATOM   351  C  CA   . HIS   A 1 88  ? -20.851 11.413 4.561   1.00 19.48 ? 56  HIS   A CA   1 
ATOM   352  C  C    . HIS   A 1 88  ? -20.948 12.842 5.075   1.00 20.98 ? 56  HIS   A C    1 
ATOM   353  O  O    . HIS   A 1 88  ? -20.001 13.628 4.985   1.00 21.75 ? 56  HIS   A O    1 
ATOM   354  C  CB   . HIS   A 1 88  ? -20.699 10.470 5.761   1.00 22.18 ? 56  HIS   A CB   1 
ATOM   355  C  CG   . HIS   A 1 88  ? -20.721 9.020  5.395   1.00 25.02 ? 56  HIS   A CG   1 
ATOM   356  N  ND1  . HIS   A 1 88  ? -21.849 8.238  5.523   1.00 27.25 ? 56  HIS   A ND1  1 
ATOM   357  C  CD2  . HIS   A 1 88  ? -19.753 8.207  4.911   1.00 26.66 ? 56  HIS   A CD2  1 
ATOM   358  C  CE1  . HIS   A 1 88  ? -21.575 7.006  5.133   1.00 27.44 ? 56  HIS   A CE1  1 
ATOM   359  N  NE2  . HIS   A 1 88  ? -20.309 6.960  4.758   1.00 26.61 ? 56  HIS   A NE2  1 
ATOM   360  N  N    . GLY   A 1 89  ? -22.113 13.168 5.626   1.00 20.53 ? 57  GLY   A N    1 
ATOM   361  C  CA   . GLY   A 1 89  ? -22.276 14.430 6.317   1.00 21.97 ? 57  GLY   A CA   1 
ATOM   362  C  C    . GLY   A 1 89  ? -22.378 15.664 5.451   1.00 21.96 ? 57  GLY   A C    1 
ATOM   363  O  O    . GLY   A 1 89  ? -22.176 16.772 5.955   1.00 23.25 ? 57  GLY   A O    1 
ATOM   364  N  N    . LEU   A 1 90  ? -22.705 15.513 4.163   1.00 19.26 ? 58  LEU   A N    1 
ATOM   365  C  CA   . LEU   A 1 90  ? -22.799 16.677 3.281   1.00 19.27 ? 58  LEU   A CA   1 
ATOM   366  C  C    . LEU   A 1 90  ? -23.908 17.632 3.701   1.00 19.27 ? 58  LEU   A C    1 
ATOM   367  O  O    . LEU   A 1 90  ? -23.762 18.849 3.539   1.00 21.72 ? 58  LEU   A O    1 
ATOM   368  C  CB   . LEU   A 1 90  ? -23.021 16.234 1.833   1.00 20.47 ? 58  LEU   A CB   1 
ATOM   369  C  CG   . LEU   A 1 90  ? -21.784 15.762 1.074   1.00 21.08 ? 58  LEU   A CG   1 
ATOM   370  C  CD1  . LEU   A 1 90  ? -22.192 14.968 -0.174  1.00 21.48 ? 58  LEU   A CD1  1 
ATOM   371  C  CD2  . LEU   A 1 90  ? -20.904 16.952 0.708   1.00 23.26 ? 58  LEU   A CD2  1 
ATOM   372  N  N    . THR   A 1 91  ? -25.014 17.113 4.235   1.00 18.37 ? 59  THR   A N    1 
ATOM   373  C  CA   . THR   A 1 91  ? -26.178 17.943 4.507   1.00 19.06 ? 59  THR   A CA   1 
ATOM   374  C  C    . THR   A 1 91  ? -26.981 17.345 5.659   1.00 20.64 ? 59  THR   A C    1 
ATOM   375  O  O    . THR   A 1 91  ? -26.599 16.337 6.264   1.00 22.09 ? 59  THR   A O    1 
ATOM   376  C  CB   . THR   A 1 91  ? -27.007 18.155 3.226   1.00 19.04 ? 59  THR   A CB   1 
ATOM   377  O  OG1  . THR   A 1 91  ? -28.000 19.165 3.444   1.00 20.14 ? 59  THR   A OG1  1 
ATOM   378  C  CG2  . THR   A 1 91  ? -27.690 16.858 2.753   1.00 20.21 ? 59  THR   A CG2  1 
ATOM   379  N  N    . THR   A 1 92  ? -28.102 17.992 5.962   1.00 19.56 ? 60  THR   A N    1 
ATOM   380  C  CA   . THR   A 1 92  ? -29.018 17.593 7.018   1.00 19.07 ? 60  THR   A CA   1 
ATOM   381  C  C    . THR   A 1 92  ? -30.413 17.491 6.423   1.00 19.58 ? 60  THR   A C    1 
ATOM   382  O  O    . THR   A 1 92  ? -30.685 18.013 5.339   1.00 19.26 ? 60  THR   A O    1 
ATOM   383  C  CB   . THR   A 1 92  ? -29.043 18.624 8.153   1.00 22.26 ? 60  THR   A CB   1 
ATOM   384  O  OG1  . THR   A 1 92  ? -29.602 19.853 7.669   1.00 22.34 ? 60  THR   A OG1  1 
ATOM   385  C  CG2  . THR   A 1 92  ? -27.640 18.892 8.667   1.00 25.45 ? 60  THR   A CG2  1 
ATOM   386  N  N    . GLU   A 1 93  ? -31.314 16.836 7.165   1.00 21.15 ? 61  GLU   A N    1 
ATOM   387  C  CA   . GLU   A 1 93  ? -32.697 16.721 6.712   1.00 22.89 ? 61  GLU   A CA   1 
ATOM   388  C  C    . GLU   A 1 93  ? -33.336 18.093 6.536   1.00 22.35 ? 61  GLU   A C    1 
ATOM   389  O  O    . GLU   A 1 93  ? -34.114 18.311 5.598   1.00 22.65 ? 61  GLU   A O    1 
ATOM   390  C  CB   . GLU   A 1 93  ? -33.508 15.896 7.712   1.00 29.04 ? 61  GLU   A CB   1 
ATOM   391  C  CG   . GLU   A 1 93  ? -32.856 14.589 8.139   1.00 38.70 ? 61  GLU   A CG   1 
ATOM   392  C  CD   . GLU   A 1 93  ? -33.628 13.895 9.250   1.00 46.83 ? 61  GLU   A CD   1 
ATOM   393  O  OE1  . GLU   A 1 93  ? -34.690 13.304 8.960   1.00 49.81 ? 61  GLU   A OE1  1 
ATOM   394  O  OE2  . GLU   A 1 93  ? -33.179 13.949 10.415  1.00 50.11 ? 61  GLU   A OE2  1 
ATOM   395  N  N    . GLU   A 1 94  ? -33.020 19.033 7.429   1.00 20.45 ? 62  GLU   A N    1 
ATOM   396  C  CA   . GLU   A 1 94  ? -33.647 20.348 7.358   1.00 20.71 ? 62  GLU   A CA   1 
ATOM   397  C  C    . GLU   A 1 94  ? -33.155 21.128 6.147   1.00 18.49 ? 62  GLU   A C    1 
ATOM   398  O  O    . GLU   A 1 94  ? -33.930 21.850 5.507   1.00 19.62 ? 62  GLU   A O    1 
ATOM   399  C  CB   . GLU   A 1 94  ? -33.356 21.144 8.632   1.00 25.24 ? 62  GLU   A CB   1 
ATOM   400  C  CG   . GLU   A 1 94  ? -34.045 20.632 9.893   1.00 31.14 ? 62  GLU   A CG   1 
ATOM   401  C  CD   . GLU   A 1 94  ? -33.549 19.266 10.327  1.00 37.52 ? 62  GLU   A CD   1 
ATOM   402  O  OE1  . GLU   A 1 94  ? -34.388 18.437 10.739  1.00 42.08 ? 62  GLU   A OE1  1 
ATOM   403  O  OE2  . GLU   A 1 94  ? -32.325 19.012 10.241  1.00 37.31 ? 62  GLU   A OE2  1 
ATOM   404  N  N    . GLU   A 1 95  ? -31.867 21.003 5.827   1.00 17.22 ? 63  GLU   A N    1 
ATOM   405  C  CA   . GLU   A 1 95  ? -31.271 21.797 4.761   1.00 18.12 ? 63  GLU   A CA   1 
ATOM   406  C  C    . GLU   A 1 95  ? -31.568 21.209 3.390   1.00 15.78 ? 63  GLU   A C    1 
ATOM   407  O  O    . GLU   A 1 95  ? -31.654 21.947 2.405   1.00 16.44 ? 63  GLU   A O    1 
ATOM   408  C  CB   . GLU   A 1 95  ? -29.755 21.865 4.972   1.00 19.83 ? 63  GLU   A CB   1 
ATOM   409  C  CG   . GLU   A 1 95  ? -28.999 22.660 3.915   1.00 23.58 ? 63  GLU   A CG   1 
ATOM   410  C  CD   . GLU   A 1 95  ? -27.492 22.626 4.111   1.00 28.07 ? 63  GLU   A CD   1 
ATOM   411  O  OE1  . GLU   A 1 95  ? -26.898 23.704 4.324   1.00 31.31 ? 63  GLU   A OE1  1 
ATOM   412  O  OE2  . GLU   A 1 95  ? -26.902 21.525 4.051   1.00 27.74 ? 63  GLU   A OE2  1 
ATOM   413  N  N    . PHE   A 1 96  ? -31.760 19.895 3.316   1.00 16.27 ? 64  PHE   A N    1 
ATOM   414  C  CA   . PHE   A 1 96  ? -31.879 19.169 2.048   1.00 16.06 ? 64  PHE   A CA   1 
ATOM   415  C  C    . PHE   A 1 96  ? -33.345 19.157 1.605   1.00 16.65 ? 64  PHE   A C    1 
ATOM   416  O  O    . PHE   A 1 96  ? -34.052 18.145 1.638   1.00 17.88 ? 64  PHE   A O    1 
ATOM   417  C  CB   . PHE   A 1 96  ? -31.303 17.769 2.219   1.00 16.23 ? 64  PHE   A CB   1 
ATOM   418  C  CG   . PHE   A 1 96  ? -31.144 16.988 0.947   1.00 17.57 ? 64  PHE   A CG   1 
ATOM   419  C  CD1  . PHE   A 1 96  ? -30.638 17.564 -0.207  1.00 18.66 ? 64  PHE   A CD1  1 
ATOM   420  C  CD2  . PHE   A 1 96  ? -31.431 15.630 0.943   1.00 20.13 ? 64  PHE   A CD2  1 
ATOM   421  C  CE1  . PHE   A 1 96  ? -30.469 16.792 -1.368  1.00 19.87 ? 64  PHE   A CE1  1 
ATOM   422  C  CE2  . PHE   A 1 96  ? -31.263 14.870 -0.196  1.00 22.49 ? 64  PHE   A CE2  1 
ATOM   423  C  CZ   . PHE   A 1 96  ? -30.782 15.450 -1.350  1.00 20.89 ? 64  PHE   A CZ   1 
ATOM   424  N  N    . VAL   A 1 97  ? -33.788 20.330 1.161   1.00 15.62 ? 65  VAL   A N    1 
ATOM   425  C  CA   . VAL   A 1 97  ? -35.161 20.562 0.721   1.00 14.59 ? 65  VAL   A CA   1 
ATOM   426  C  C    . VAL   A 1 97  ? -35.369 20.047 -0.699  1.00 14.95 ? 65  VAL   A C    1 
ATOM   427  O  O    . VAL   A 1 97  ? -34.416 19.611 -1.357  1.00 15.89 ? 65  VAL   A O    1 
ATOM   428  C  CB   . VAL   A 1 97  ? -35.515 22.058 0.818   1.00 14.76 ? 65  VAL   A CB   1 
ATOM   429  C  CG1  . VAL   A 1 97  ? -35.500 22.527 2.279   1.00 15.96 ? 65  VAL   A CG1  1 
ATOM   430  C  CG2  . VAL   A 1 97  ? -34.546 22.891 -0.018  1.00 16.54 ? 65  VAL   A CG2  1 
ATOM   431  N  N    . GLU   A 1 98  ? -36.622 20.059 -1.168  1.00 15.51 ? 66  GLU   A N    1 
ATOM   432  C  CA   . GLU   A 1 98  ? -36.907 19.801 -2.578  1.00 17.86 ? 66  GLU   A CA   1 
ATOM   433  C  C    . GLU   A 1 98  ? -36.015 20.655 -3.461  1.00 17.46 ? 66  GLU   A C    1 
ATOM   434  O  O    . GLU   A 1 98  ? -35.766 21.826 -3.170  1.00 18.76 ? 66  GLU   A O    1 
ATOM   435  C  CB   . GLU   A 1 98  ? -38.334 20.228 -2.922  1.00 22.35 ? 66  GLU   A CB   1 
ATOM   436  C  CG   . GLU   A 1 98  ? -39.460 19.432 -2.384  1.00 27.67 ? 66  GLU   A CG   1 
ATOM   437  C  CD   . GLU   A 1 98  ? -40.750 19.830 -3.086  1.00 28.93 ? 66  GLU   A CD   1 
ATOM   438  O  OE1  . GLU   A 1 98  ? -40.874 19.531 -4.292  1.00 31.24 ? 66  GLU   A OE1  1 
ATOM   439  O  OE2  . GLU   A 1 98  ? -41.610 20.480 -2.456  1.00 28.54 ? 66  GLU   A OE2  1 
ATOM   440  N  N    . GLY   A 1 99  ? -35.596 20.091 -4.582  1.00 15.67 ? 67  GLY   A N    1 
ATOM   441  C  CA   . GLY   A 1 99  ? -34.905 20.884 -5.575  1.00 16.91 ? 67  GLY   A CA   1 
ATOM   442  C  C    . GLY   A 1 99  ? -34.224 19.986 -6.577  1.00 15.46 ? 67  GLY   A C    1 
ATOM   443  O  O    . GLY   A 1 99  ? -34.296 18.753 -6.502  1.00 16.81 ? 67  GLY   A O    1 
ATOM   444  N  N    . ILE   A 1 100 ? -33.569 20.630 -7.530  1.00 15.90 ? 68  ILE   A N    1 
ATOM   445  C  CA   . ILE   A 1 100 ? -32.710 19.946 -8.485  1.00 15.12 ? 68  ILE   A CA   1 
ATOM   446  C  C    . ILE   A 1 100 ? -31.278 20.126 -8.013  1.00 14.69 ? 68  ILE   A C    1 
ATOM   447  O  O    . ILE   A 1 100 ? -30.816 21.258 -7.814  1.00 15.95 ? 68  ILE   A O    1 
ATOM   448  C  CB   . ILE   A 1 100 ? -32.903 20.480 -9.912  1.00 16.20 ? 68  ILE   A CB   1 
ATOM   449  C  CG1  . ILE   A 1 100 ? -34.367 20.348 -10.335 1.00 19.91 ? 68  ILE   A CG1  1 
ATOM   450  C  CG2  . ILE   A 1 100 ? -31.989 19.736 -10.876 1.00 18.03 ? 68  ILE   A CG2  1 
ATOM   451  C  CD1  . ILE   A 1 100 ? -34.655 20.892 -11.720 1.00 22.40 ? 68  ILE   A CD1  1 
ATOM   452  N  N    . TYR   A 1 101 ? -30.584 19.010 -7.827  1.00 13.54 ? 69  TYR   A N    1 
ATOM   453  C  CA   . TYR   A 1 101 ? -29.235 18.996 -7.297  1.00 13.29 ? 69  TYR   A CA   1 
ATOM   454  C  C    . TYR   A 1 101 ? -28.282 18.428 -8.332  1.00 13.49 ? 69  TYR   A C    1 
ATOM   455  O  O    . TYR   A 1 101 ? -28.655 17.573 -9.144  1.00 14.83 ? 69  TYR   A O    1 
ATOM   456  C  CB   . TYR   A 1 101 ? -29.163 18.146 -6.023  1.00 13.20 ? 69  TYR   A CB   1 
ATOM   457  C  CG   . TYR   A 1 101 ? -29.907 18.758 -4.864  1.00 13.14 ? 69  TYR   A CG   1 
ATOM   458  C  CD1  . TYR   A 1 101 ? -31.288 18.602 -4.725  1.00 14.18 ? 69  TYR   A CD1  1 
ATOM   459  C  CD2  . TYR   A 1 101 ? -29.231 19.523 -3.915  1.00 14.54 ? 69  TYR   A CD2  1 
ATOM   460  C  CE1  . TYR   A 1 101 ? -31.974 19.186 -3.653  1.00 14.68 ? 69  TYR   A CE1  1 
ATOM   461  C  CE2  . TYR   A 1 101 ? -29.900 20.111 -2.851  1.00 15.04 ? 69  TYR   A CE2  1 
ATOM   462  C  CZ   . TYR   A 1 101 ? -31.266 19.933 -2.719  1.00 14.24 ? 69  TYR   A CZ   1 
ATOM   463  O  OH   . TYR   A 1 101 ? -31.917 20.525 -1.656  1.00 16.42 ? 69  TYR   A OH   1 
ATOM   464  N  N    . LYS   A 1 102 ? -27.045 18.913 -8.294  1.00 14.20 ? 70  LYS   A N    1 
ATOM   465  C  CA   . LYS   A 1 102 ? -25.975 18.422 -9.149  1.00 13.95 ? 70  LYS   A CA   1 
ATOM   466  C  C    . LYS   A 1 102 ? -24.785 18.055 -8.283  1.00 14.53 ? 70  LYS   A C    1 
ATOM   467  O  O    . LYS   A 1 102 ? -24.318 18.878 -7.493  1.00 15.27 ? 70  LYS   A O    1 
ATOM   468  C  CB   . LYS   A 1 102 ? -25.549 19.486 -10.170 1.00 15.74 ? 70  LYS   A CB   1 
ATOM   469  C  CG   . LYS   A 1 102 ? -24.347 19.069 -11.029 1.00 18.37 ? 70  LYS   A CG   1 
ATOM   470  C  CD   . LYS   A 1 102 ? -24.105 20.007 -12.202 1.00 21.90 ? 70  LYS   A CD   1 
ATOM   471  C  CE   . LYS   A 1 102 ? -23.715 21.395 -11.736 1.00 25.74 ? 70  LYS   A CE   1 
ATOM   472  N  NZ   . LYS   A 1 102 ? -23.199 22.232 -12.862 1.00 29.02 ? 70  LYS   A NZ   1 
ATOM   473  N  N    . VAL   A 1 103 ? -24.296 16.828 -8.427  1.00 14.31 ? 71  VAL   A N    1 
ATOM   474  C  CA   . VAL   A 1 103 ? -23.049 16.415 -7.798  1.00 14.65 ? 71  VAL   A CA   1 
ATOM   475  C  C    . VAL   A 1 103 ? -21.996 16.353 -8.892  1.00 15.50 ? 71  VAL   A C    1 
ATOM   476  O  O    . VAL   A 1 103 ? -22.155 15.612 -9.867  1.00 17.42 ? 71  VAL   A O    1 
ATOM   477  C  CB   . VAL   A 1 103 ? -23.181 15.057 -7.090  1.00 16.65 ? 71  VAL   A CB   1 
ATOM   478  C  CG1  . VAL   A 1 103 ? -21.857 14.697 -6.384  1.00 18.43 ? 71  VAL   A CG1  1 
ATOM   479  C  CG2  . VAL   A 1 103 ? -24.344 15.061 -6.103  1.00 17.55 ? 71  VAL   A CG2  1 
ATOM   480  N  N    . GLU   A 1 104 ? -20.931 17.129 -8.739  1.00 15.54 ? 72  GLU   A N    1 
ATOM   481  C  CA   . GLU   A 1 104 ? -19.838 17.188 -9.706  1.00 15.71 ? 72  GLU   A CA   1 
ATOM   482  C  C    . GLU   A 1 104 ? -18.612 16.560 -9.051  1.00 14.80 ? 72  GLU   A C    1 
ATOM   483  O  O    . GLU   A 1 104 ? -18.018 17.149 -8.146  1.00 15.67 ? 72  GLU   A O    1 
ATOM   484  C  CB   . GLU   A 1 104 ? -19.573 18.645 -10.067 1.00 20.77 ? 72  GLU   A CB   1 
ATOM   485  C  CG   . GLU   A 1 104 ? -19.094 18.894 -11.456 1.00 29.22 ? 72  GLU   A CG   1 
ATOM   486  C  CD   . GLU   A 1 104 ? -19.312 20.346 -11.853 1.00 33.18 ? 72  GLU   A CD   1 
ATOM   487  O  OE1  . GLU   A 1 104 ? -20.242 20.637 -12.644 1.00 36.91 ? 72  GLU   A OE1  1 
ATOM   488  O  OE2  . GLU   A 1 104 ? -18.569 21.204 -11.343 1.00 32.33 ? 72  GLU   A OE2  1 
ATOM   489  N  N    . ILE   A 1 105 ? -18.229 15.368 -9.510  1.00 13.61 ? 73  ILE   A N    1 
ATOM   490  C  CA   . ILE   A 1 105 ? -17.137 14.607 -8.907  1.00 13.91 ? 73  ILE   A CA   1 
ATOM   491  C  C    . ILE   A 1 105 ? -15.868 14.881 -9.699  1.00 14.04 ? 73  ILE   A C    1 
ATOM   492  O  O    . ILE   A 1 105 ? -15.834 14.662 -10.915 1.00 14.58 ? 73  ILE   A O    1 
ATOM   493  C  CB   . ILE   A 1 105 ? -17.458 13.105 -8.904  1.00 14.85 ? 73  ILE   A CB   1 
ATOM   494  C  CG1  . ILE   A 1 105 ? -18.795 12.853 -8.200  1.00 16.37 ? 73  ILE   A CG1  1 
ATOM   495  C  CG2  . ILE   A 1 105 ? -16.342 12.316 -8.252  1.00 16.57 ? 73  ILE   A CG2  1 
ATOM   496  C  CD1  . ILE   A 1 105 ? -19.206 11.393 -8.214  1.00 18.17 ? 73  ILE   A CD1  1 
ATOM   497  N  N    . ASP   A 1 106 ? -14.816 15.353 -9.019  1.00 14.27 ? 74  ASP   A N    1 
ATOM   498  C  CA   . ASP   A 1 106 ? -13.566 15.715 -9.698  1.00 15.46 ? 74  ASP   A CA   1 
ATOM   499  C  C    . ASP   A 1 106 ? -12.744 14.462 -10.005 1.00 14.38 ? 74  ASP   A C    1 
ATOM   500  O  O    . ASP   A 1 106 ? -11.705 14.192 -9.401  1.00 15.86 ? 74  ASP   A O    1 
ATOM   501  C  CB   . ASP   A 1 106 ? -12.760 16.721 -8.888  1.00 17.78 ? 74  ASP   A CB   1 
ATOM   502  C  CG   . ASP   A 1 106 ? -11.500 17.173 -9.611  1.00 21.68 ? 74  ASP   A CG   1 
ATOM   503  O  OD1  . ASP   A 1 106 ? -11.320 16.809 -10.794 1.00 22.42 ? 74  ASP   A OD1  1 
ATOM   504  O  OD2  . ASP   A 1 106 ? -10.683 17.891 -8.996  1.00 25.46 ? 74  ASP   A OD2  1 
ATOM   505  N  N    . THR   A 1 107 ? -13.219 13.710 -11.005 1.00 14.83 ? 75  THR   A N    1 
ATOM   506  C  CA   . THR   A 1 107 ? -12.516 12.514 -11.450 1.00 14.17 ? 75  THR   A CA   1 
ATOM   507  C  C    . THR   A 1 107 ? -11.213 12.849 -12.169 1.00 14.89 ? 75  THR   A C    1 
ATOM   508  O  O    . THR   A 1 107 ? -10.274 12.046 -12.145 1.00 15.01 ? 75  THR   A O    1 
ATOM   509  C  CB   . THR   A 1 107 ? -13.424 11.691 -12.365 1.00 14.63 ? 75  THR   A CB   1 
ATOM   510  O  OG1  . THR   A 1 107 ? -13.823 12.489 -13.481 1.00 15.16 ? 75  THR   A OG1  1 
ATOM   511  C  CG2  . THR   A 1 107 ? -14.666 11.239 -11.618 1.00 16.09 ? 75  THR   A CG2  1 
ATOM   512  N  N    . LYS   A 1 108 ? -11.131 14.018 -12.808 1.00 14.68 ? 76  LYS   A N    1 
ATOM   513  C  CA   . LYS   A 1 108 ? -9.930  14.346 -13.570 1.00 15.26 ? 76  LYS   A CA   1 
ATOM   514  C  C    . LYS   A 1 108 ? -8.707  14.451 -12.663 1.00 16.80 ? 76  LYS   A C    1 
ATOM   515  O  O    . LYS   A 1 108 ? -7.650  13.884 -12.965 1.00 18.11 ? 76  LYS   A O    1 
ATOM   516  C  CB   . LYS   A 1 108 ? -10.137 15.634 -14.365 1.00 17.19 ? 76  LYS   A CB   1 
ATOM   517  C  CG   . LYS   A 1 108 ? -9.004  15.922 -15.327 1.00 20.49 ? 76  LYS   A CG   1 
ATOM   518  C  CD   . LYS   A 1 108 ? -9.296  17.171 -16.121 1.00 23.01 ? 76  LYS   A CD   1 
ATOM   519  C  CE   . LYS   A 1 108 ? -8.200  17.477 -17.137 1.00 26.18 ? 76  LYS   A CE   1 
ATOM   520  N  NZ   . LYS   A 1 108 ? -8.521  18.709 -17.901 1.00 28.24 ? 76  LYS   A NZ   1 
ATOM   521  N  N    . SER   A 1 109 ? -8.832  15.162 -11.536 1.00 18.50 ? 77  SER   A N    1 
ATOM   522  C  CA   . SER   A 1 109 ? -7.701  15.269 -10.614 1.00 19.91 ? 77  SER   A CA   1 
ATOM   523  C  C    . SER   A 1 109 ? -7.321  13.910 -10.044 1.00 19.41 ? 77  SER   A C    1 
ATOM   524  O  O    . SER   A 1 109 ? -6.136  13.627 -9.818  1.00 20.34 ? 77  SER   A O    1 
ATOM   525  C  CB   . SER   A 1 109 ? -8.026  16.239 -9.481  1.00 21.99 ? 77  SER   A CB   1 
ATOM   526  O  OG   . SER   A 1 109 ? -8.252  17.539 -9.992  1.00 23.87 ? 77  SER   A OG   1 
ATOM   527  N  N    . TYR   A 1 110 ? -8.316  13.055 -9.800  1.00 18.61 ? 78  TYR   A N    1 
ATOM   528  C  CA   . TYR   A 1 110 ? -8.047  11.721 -9.276  1.00 18.73 ? 78  TYR   A CA   1 
ATOM   529  C  C    . TYR   A 1 110 ? -7.153  10.928 -10.220 1.00 18.67 ? 78  TYR   A C    1 
ATOM   530  O  O    . TYR   A 1 110 ? -6.136  10.361 -9.802  1.00 19.13 ? 78  TYR   A O    1 
ATOM   531  C  CB   . TYR   A 1 110 ? -9.371  10.994 -9.035  1.00 16.60 ? 78  TYR   A CB   1 
ATOM   532  C  CG   . TYR   A 1 110 ? -9.201  9.580  -8.525  1.00 16.76 ? 78  TYR   A CG   1 
ATOM   533  C  CD1  . TYR   A 1 110 ? -8.901  9.341  -7.191  1.00 18.14 ? 78  TYR   A CD1  1 
ATOM   534  C  CD2  . TYR   A 1 110 ? -9.335  8.487  -9.376  1.00 16.56 ? 78  TYR   A CD2  1 
ATOM   535  C  CE1  . TYR   A 1 110 ? -8.746  8.058  -6.709  1.00 17.50 ? 78  TYR   A CE1  1 
ATOM   536  C  CE2  . TYR   A 1 110 ? -9.172  7.197  -8.905  1.00 17.19 ? 78  TYR   A CE2  1 
ATOM   537  C  CZ   . TYR   A 1 110 ? -8.878  6.988  -7.567  1.00 16.99 ? 78  TYR   A CZ   1 
ATOM   538  O  OH   . TYR   A 1 110 ? -8.716  5.716  -7.064  1.00 18.78 ? 78  TYR   A OH   1 
ATOM   539  N  N    . TRP   A 1 111 ? -7.514  10.876 -11.503 1.00 17.35 ? 79  TRP   A N    1 
ATOM   540  C  CA   . TRP   A 1 111 ? -6.725  10.089 -12.446 1.00 17.61 ? 79  TRP   A CA   1 
ATOM   541  C  C    . TRP   A 1 111 ? -5.360  10.715 -12.675 1.00 20.40 ? 79  TRP   A C    1 
ATOM   542  O  O    . TRP   A 1 111 ? -4.355  10.003 -12.765 1.00 21.33 ? 79  TRP   A O    1 
ATOM   543  C  CB   . TRP   A 1 111 ? -7.479  9.929  -13.765 1.00 16.18 ? 79  TRP   A CB   1 
ATOM   544  C  CG   . TRP   A 1 111 ? -8.676  9.051  -13.623 1.00 15.54 ? 79  TRP   A CG   1 
ATOM   545  C  CD1  . TRP   A 1 111 ? -9.981  9.401  -13.810 1.00 15.16 ? 79  TRP   A CD1  1 
ATOM   546  C  CD2  . TRP   A 1 111 ? -8.679  7.673  -13.234 1.00 14.94 ? 79  TRP   A CD2  1 
ATOM   547  N  NE1  . TRP   A 1 111 ? -10.800 8.325  -13.567 1.00 14.37 ? 79  TRP   A NE1  1 
ATOM   548  C  CE2  . TRP   A 1 111 ? -10.026 7.249  -13.213 1.00 14.79 ? 79  TRP   A CE2  1 
ATOM   549  C  CE3  . TRP   A 1 111 ? -7.672  6.754  -12.899 1.00 17.44 ? 79  TRP   A CE3  1 
ATOM   550  C  CZ2  . TRP   A 1 111 ? -10.393 5.949  -12.871 1.00 15.17 ? 79  TRP   A CZ2  1 
ATOM   551  C  CZ3  . TRP   A 1 111 ? -8.040  5.463  -12.562 1.00 16.79 ? 79  TRP   A CZ3  1 
ATOM   552  C  CH2  . TRP   A 1 111 ? -9.391  5.074  -12.550 1.00 16.27 ? 79  TRP   A CH2  1 
ATOM   553  N  N    . LYS   A 1 112 ? -5.305  12.043 -12.782 1.00 20.64 ? 80  LYS   A N    1 
ATOM   554  C  CA   . LYS   A 1 112 ? -4.030  12.703 -13.043 1.00 22.79 ? 80  LYS   A CA   1 
ATOM   555  C  C    . LYS   A 1 112 ? -3.023  12.419 -11.940 1.00 25.22 ? 80  LYS   A C    1 
ATOM   556  O  O    . LYS   A 1 112 ? -1.830  12.232 -12.213 1.00 25.95 ? 80  LYS   A O    1 
ATOM   557  C  CB   . LYS   A 1 112 ? -4.236  14.206 -13.220 1.00 25.20 ? 80  LYS   A CB   1 
ATOM   558  C  CG   . LYS   A 1 112 ? -4.904  14.565 -14.521 1.00 28.16 ? 80  LYS   A CG   1 
ATOM   559  C  CD   . LYS   A 1 112 ? -4.965  16.065 -14.700 1.00 33.44 ? 80  LYS   A CD   1 
ATOM   560  C  CE   . LYS   A 1 112 ? -4.190  16.476 -15.933 1.00 38.99 ? 80  LYS   A CE   1 
ATOM   561  N  NZ   . LYS   A 1 112 ? -4.814  15.878 -17.149 1.00 41.51 ? 80  LYS   A NZ   1 
ATOM   562  N  N    . ALA   A 1 113 ? -3.482  12.372 -10.686 1.00 25.85 ? 81  ALA   A N    1 
ATOM   563  C  CA   . ALA   A 1 113 ? -2.578  12.078 -9.578  1.00 27.48 ? 81  ALA   A CA   1 
ATOM   564  C  C    . ALA   A 1 113 ? -2.045  10.654 -9.635  1.00 29.22 ? 81  ALA   A C    1 
ATOM   565  O  O    . ALA   A 1 113 ? -0.982  10.379 -9.071  1.00 30.27 ? 81  ALA   A O    1 
ATOM   566  C  CB   . ALA   A 1 113 ? -3.270  12.340 -8.240  1.00 28.52 ? 81  ALA   A CB   1 
ATOM   567  N  N    . LEU   A 1 114 ? -2.752  9.748  -10.300 1.00 30.42 ? 82  LEU   A N    1 
ATOM   568  C  CA   . LEU   A 1 114 ? -2.273  8.392  -10.516 1.00 32.18 ? 82  LEU   A CA   1 
ATOM   569  C  C    . LEU   A 1 114 ? -1.479  8.254  -11.810 1.00 32.87 ? 82  LEU   A C    1 
ATOM   570  O  O    . LEU   A 1 114 ? -1.129  7.132  -12.194 1.00 33.80 ? 82  LEU   A O    1 
ATOM   571  C  CB   . LEU   A 1 114 ? -3.451  7.414  -10.495 1.00 31.82 ? 82  LEU   A CB   1 
ATOM   572  C  CG   . LEU   A 1 114 ? -4.281  7.457  -9.208  1.00 32.19 ? 82  LEU   A CG   1 
ATOM   573  C  CD1  . LEU   A 1 114 ? -5.482  6.535  -9.313  1.00 33.00 ? 82  LEU   A CD1  1 
ATOM   574  C  CD2  . LEU   A 1 114 ? -3.434  7.099  -7.990  1.00 33.34 ? 82  LEU   A CD2  1 
ATOM   575  N  N    . GLY   A 1 115 ? -1.185  9.364  -12.485 1.00 33.76 ? 83  GLY   A N    1 
ATOM   576  C  CA   . GLY   A 1 115 ? -0.438  9.322  -13.725 1.00 35.09 ? 83  GLY   A CA   1 
ATOM   577  C  C    . GLY   A 1 115 ? -1.250  8.942  -14.937 1.00 35.91 ? 83  GLY   A C    1 
ATOM   578  O  O    . GLY   A 1 115 ? -0.675  8.576  -15.966 1.00 35.81 ? 83  GLY   A O    1 
ATOM   579  N  N    . ILE   A 1 116 ? -2.572  9.007  -14.843 1.00 33.91 ? 84  ILE   A N    1 
ATOM   580  C  CA   . ILE   A 1 116 ? -3.467  8.691  -15.949 1.00 35.07 ? 84  ILE   A CA   1 
ATOM   581  C  C    . ILE   A 1 116 ? -4.026  9.990  -16.503 1.00 33.02 ? 84  ILE   A C    1 
ATOM   582  O  O    . ILE   A 1 116 ? -4.462  10.867 -15.744 1.00 33.22 ? 84  ILE   A O    1 
ATOM   583  C  CB   . ILE   A 1 116 ? -4.619  7.790  -15.467 1.00 37.41 ? 84  ILE   A CB   1 
ATOM   584  C  CG1  . ILE   A 1 116 ? -4.095  6.655  -14.584 1.00 39.47 ? 84  ILE   A CG1  1 
ATOM   585  C  CG2  . ILE   A 1 116 ? -5.409  7.264  -16.656 1.00 38.41 ? 84  ILE   A CG2  1 
ATOM   586  C  CD1  . ILE   A 1 116 ? -3.564  5.486  -15.343 1.00 40.50 ? 84  ILE   A CD1  1 
ATOM   587  N  N    . SER   A 1 117 ? -4.053  10.103 -17.831 1.00 31.16 ? 85  SER   A N    1 
ATOM   588  C  CA   . SER   A 1 117 ? -4.708  11.224 -18.485 1.00 30.30 ? 85  SER   A CA   1 
ATOM   589  C  C    . SER   A 1 117 ? -6.124  10.785 -18.840 1.00 26.54 ? 85  SER   A C    1 
ATOM   590  O  O    . SER   A 1 117 ? -6.314  10.054 -19.823 1.00 28.19 ? 85  SER   A O    1 
ATOM   591  C  CB   . SER   A 1 117 ? -3.940  11.636 -19.743 1.00 34.45 ? 85  SER   A CB   1 
ATOM   592  O  OG   . SER   A 1 117 ? -2.596  11.959 -19.428 1.00 39.35 ? 85  SER   A OG   1 
ATOM   593  N  N    . PRO   A 1 118 ? -7.140  11.199 -18.092 1.00 21.65 ? 86  PRO   A N    1 
ATOM   594  C  CA   . PRO   A 1 118 ? -8.484  10.654 -18.279 1.00 19.10 ? 86  PRO   A CA   1 
ATOM   595  C  C    . PRO   A 1 118 ? -9.269  11.431 -19.331 1.00 18.64 ? 86  PRO   A C    1 
ATOM   596  O  O    . PRO   A 1 118 ? -8.877  12.510 -19.781 1.00 20.70 ? 86  PRO   A O    1 
ATOM   597  C  CB   . PRO   A 1 118 ? -9.110  10.872 -16.901 1.00 20.94 ? 86  PRO   A CB   1 
ATOM   598  C  CG   . PRO   A 1 118 ? -8.528  12.186 -16.475 1.00 21.20 ? 86  PRO   A CG   1 
ATOM   599  C  CD   . PRO   A 1 118 ? -7.101  12.192 -17.001 1.00 22.39 ? 86  PRO   A CD   1 
ATOM   600  N  N    . PHE   A 1 119 ? -10.418 10.861 -19.693 1.00 16.70 ? 87  PHE   A N    1 
ATOM   601  C  CA   . PHE   A 1 119 ? -11.245 11.451 -20.739 1.00 16.08 ? 87  PHE   A CA   1 
ATOM   602  C  C    . PHE   A 1 119 ? -12.121 12.586 -20.206 1.00 14.43 ? 87  PHE   A C    1 
ATOM   603  O  O    . PHE   A 1 119 ? -12.205 13.661 -20.817 1.00 15.47 ? 87  PHE   A O    1 
ATOM   604  C  CB   . PHE   A 1 119 ? -12.112 10.366 -21.383 1.00 17.08 ? 87  PHE   A CB   1 
ATOM   605  C  CG   . PHE   A 1 119 ? -12.996 10.889 -22.470 1.00 18.03 ? 87  PHE   A CG   1 
ATOM   606  C  CD1  . PHE   A 1 119 ? -12.462 11.233 -23.698 1.00 20.51 ? 87  PHE   A CD1  1 
ATOM   607  C  CD2  . PHE   A 1 119 ? -14.352 11.069 -22.258 1.00 19.78 ? 87  PHE   A CD2  1 
ATOM   608  C  CE1  . PHE   A 1 119 ? -13.267 11.733 -24.703 1.00 21.58 ? 87  PHE   A CE1  1 
ATOM   609  C  CE2  . PHE   A 1 119 ? -15.165 11.570 -23.260 1.00 20.49 ? 87  PHE   A CE2  1 
ATOM   610  C  CZ   . PHE   A 1 119 ? -14.621 11.900 -24.484 1.00 21.06 ? 87  PHE   A CZ   1 
ATOM   611  N  N    . HIS   A 1 120 ? -12.799 12.365 -19.087 1.00 14.55 ? 88  HIS   A N    1 
ATOM   612  C  CA   . HIS   A 1 120 ? -13.819 13.294 -18.623 1.00 14.44 ? 88  HIS   A CA   1 
ATOM   613  C  C    . HIS   A 1 120 ? -13.223 14.388 -17.751 1.00 14.20 ? 88  HIS   A C    1 
ATOM   614  O  O    . HIS   A 1 120 ? -12.241 14.176 -17.033 1.00 14.46 ? 88  HIS   A O    1 
ATOM   615  C  CB   . HIS   A 1 120 ? -14.876 12.540 -17.821 1.00 13.95 ? 88  HIS   A CB   1 
ATOM   616  C  CG   . HIS   A 1 120 ? -15.559 11.464 -18.603 1.00 14.85 ? 88  HIS   A CG   1 
ATOM   617  N  ND1  . HIS   A 1 120 ? -15.159 10.145 -18.559 1.00 15.85 ? 88  HIS   A ND1  1 
ATOM   618  C  CD2  . HIS   A 1 120 ? -16.597 11.515 -19.470 1.00 15.27 ? 88  HIS   A CD2  1 
ATOM   619  C  CE1  . HIS   A 1 120 ? -15.925 9.427  -19.360 1.00 16.42 ? 88  HIS   A CE1  1 
ATOM   620  N  NE2  . HIS   A 1 120 ? -16.811 10.233 -19.921 1.00 16.34 ? 88  HIS   A NE2  1 
ATOM   621  N  N    . GLU   A 1 121 ? -13.858 15.564 -17.792 1.00 14.49 ? 89  GLU   A N    1 
ATOM   622  C  CA   . GLU   A 1 121 ? -13.492 16.621 -16.853 1.00 16.02 ? 89  GLU   A CA   1 
ATOM   623  C  C    . GLU   A 1 121 ? -13.954 16.288 -15.444 1.00 16.02 ? 89  GLU   A C    1 
ATOM   624  O  O    . GLU   A 1 121 ? -13.278 16.617 -14.462 1.00 19.14 ? 89  GLU   A O    1 
ATOM   625  C  CB   . GLU   A 1 121 ? -14.104 17.946 -17.304 1.00 16.97 ? 89  GLU   A CB   1 
ATOM   626  C  CG   . GLU   A 1 121 ? -13.463 18.504 -18.540 1.00 19.32 ? 89  GLU   A CG   1 
ATOM   627  C  CD   . GLU   A 1 121 ? -12.025 18.906 -18.283 1.00 24.10 ? 89  GLU   A CD   1 
ATOM   628  O  OE1  . GLU   A 1 121 ? -11.796 19.755 -17.400 1.00 25.58 ? 89  GLU   A OE1  1 
ATOM   629  O  OE2  . GLU   A 1 121 ? -11.125 18.351 -18.939 1.00 26.60 ? 89  GLU   A OE2  1 
ATOM   630  N  N    . HIS   A 1 122 ? -15.113 15.655 -15.331 1.00 15.66 ? 90  HIS   A N    1 
ATOM   631  C  CA   . HIS   A 1 122 ? -15.700 15.283 -14.056 1.00 16.41 ? 90  HIS   A CA   1 
ATOM   632  C  C    . HIS   A 1 122 ? -16.814 14.303 -14.378 1.00 16.50 ? 90  HIS   A C    1 
ATOM   633  O  O    . HIS   A 1 122 ? -17.184 14.122 -15.542 1.00 18.68 ? 90  HIS   A O    1 
ATOM   634  C  CB   . HIS   A 1 122 ? -16.220 16.499 -13.272 1.00 20.38 ? 90  HIS   A CB   1 
ATOM   635  C  CG   . HIS   A 1 122 ? -17.066 17.438 -14.074 1.00 26.72 ? 90  HIS   A CG   1 
ATOM   636  N  ND1  . HIS   A 1 122 ? -16.618 18.678 -14.478 1.00 30.45 ? 90  HIS   A ND1  1 
ATOM   637  C  CD2  . HIS   A 1 122 ? -18.341 17.338 -14.518 1.00 30.12 ? 90  HIS   A CD2  1 
ATOM   638  C  CE1  . HIS   A 1 122 ? -17.574 19.294 -15.149 1.00 31.79 ? 90  HIS   A CE1  1 
ATOM   639  N  NE2  . HIS   A 1 122 ? -18.632 18.503 -15.187 1.00 32.63 ? 90  HIS   A NE2  1 
ATOM   640  N  N    . ALA   A 1 123 ? -17.318 13.643 -13.342 1.00 16.63 ? 91  ALA   A N    1 
ATOM   641  C  CA   . ALA   A 1 123 ? -18.529 12.841 -13.442 1.00 17.77 ? 91  ALA   A CA   1 
ATOM   642  C  C    . ALA   A 1 123 ? -19.644 13.632 -12.776 1.00 19.02 ? 91  ALA   A C    1 
ATOM   643  O  O    . ALA   A 1 123 ? -19.488 14.083 -11.638 1.00 20.74 ? 91  ALA   A O    1 
ATOM   644  C  CB   . ALA   A 1 123 ? -18.351 11.492 -12.742 1.00 18.07 ? 91  ALA   A CB   1 
ATOM   645  N  N    . GLU   A 1 124 ? -20.747 13.820 -13.496 1.00 22.18 ? 92  GLU   A N    1 
ATOM   646  C  CA   . GLU   A 1 124 ? -21.831 14.706 -13.094 1.00 24.80 ? 92  GLU   A CA   1 
ATOM   647  C  C    . GLU   A 1 124 ? -23.085 13.872 -12.877 1.00 24.03 ? 92  GLU   A C    1 
ATOM   648  O  O    . GLU   A 1 124 ? -23.395 12.995 -13.688 1.00 27.85 ? 92  GLU   A O    1 
ATOM   649  C  CB   . GLU   A 1 124 ? -22.066 15.736 -14.211 1.00 32.38 ? 92  GLU   A CB   1 
ATOM   650  C  CG   . GLU   A 1 124 ? -22.845 16.979 -13.835 1.00 39.84 ? 92  GLU   A CG   1 
ATOM   651  C  CD   . GLU   A 1 124 ? -22.757 18.059 -14.913 1.00 45.85 ? 92  GLU   A CD   1 
ATOM   652  O  OE1  . GLU   A 1 124 ? -21.641 18.570 -15.160 1.00 47.33 ? 92  GLU   A OE1  1 
ATOM   653  O  OE2  . GLU   A 1 124 ? -23.798 18.386 -15.524 1.00 48.37 ? 92  GLU   A OE2  1 
ATOM   654  N  N    . VAL   A 1 125 ? -23.797 14.142 -11.785 1.00 19.07 ? 93  VAL   A N    1 
ATOM   655  C  CA   . VAL   A 1 125 ? -25.063 13.491 -11.460 1.00 17.18 ? 93  VAL   A CA   1 
ATOM   656  C  C    . VAL   A 1 125 ? -26.077 14.581 -11.137 1.00 15.17 ? 93  VAL   A C    1 
ATOM   657  O  O    . VAL   A 1 125 ? -25.889 15.335 -10.176 1.00 16.70 ? 93  VAL   A O    1 
ATOM   658  C  CB   . VAL   A 1 125 ? -24.913 12.542 -10.260 1.00 19.50 ? 93  VAL   A CB   1 
ATOM   659  C  CG1  . VAL   A 1 125 ? -26.236 11.883 -9.963  1.00 21.72 ? 93  VAL   A CG1  1 
ATOM   660  C  CG2  . VAL   A 1 125 ? -23.818 11.510 -10.533 1.00 20.85 ? 93  VAL   A CG2  1 
ATOM   661  N  N    . VAL   A 1 126 ? -27.135 14.684 -11.942 1.00 13.74 ? 94  VAL   A N    1 
ATOM   662  C  CA   . VAL   A 1 126 ? -28.144 15.737 -11.797 1.00 14.72 ? 94  VAL   A CA   1 
ATOM   663  C  C    . VAL   A 1 126 ? -29.505 15.086 -11.574 1.00 13.69 ? 94  VAL   A C    1 
ATOM   664  O  O    . VAL   A 1 126 ? -29.936 14.252 -12.380 1.00 14.72 ? 94  VAL   A O    1 
ATOM   665  C  CB   . VAL   A 1 126 ? -28.180 16.670 -13.026 1.00 15.22 ? 94  VAL   A CB   1 
ATOM   666  C  CG1  . VAL   A 1 126 ? -29.174 17.809 -12.796 1.00 15.80 ? 94  VAL   A CG1  1 
ATOM   667  C  CG2  . VAL   A 1 126 ? -26.783 17.218 -13.333 1.00 17.08 ? 94  VAL   A CG2  1 
ATOM   668  N  N    . PHE   A 1 127 ? -30.191 15.477 -10.495 1.00 13.42 ? 95  PHE   A N    1 
ATOM   669  C  CA   . PHE   A 1 127 ? -31.428 14.790 -10.124 1.00 14.00 ? 95  PHE   A CA   1 
ATOM   670  C  C    . PHE   A 1 127 ? -32.332 15.707 -9.305  1.00 14.94 ? 95  PHE   A C    1 
ATOM   671  O  O    . PHE   A 1 127 ? -31.860 16.577 -8.575  1.00 14.72 ? 95  PHE   A O    1 
ATOM   672  C  CB   . PHE   A 1 127 ? -31.133 13.511 -9.324  1.00 14.75 ? 95  PHE   A CB   1 
ATOM   673  C  CG   . PHE   A 1 127 ? -30.417 13.748 -8.021  1.00 17.07 ? 95  PHE   A CG   1 
ATOM   674  C  CD1  . PHE   A 1 127 ? -29.056 14.008 -7.997  1.00 18.23 ? 95  PHE   A CD1  1 
ATOM   675  C  CD2  . PHE   A 1 127 ? -31.103 13.668 -6.810  1.00 17.57 ? 95  PHE   A CD2  1 
ATOM   676  C  CE1  . PHE   A 1 127 ? -28.392 14.210 -6.795  1.00 20.12 ? 95  PHE   A CE1  1 
ATOM   677  C  CE2  . PHE   A 1 127 ? -30.441 13.859 -5.606  1.00 19.61 ? 95  PHE   A CE2  1 
ATOM   678  C  CZ   . PHE   A 1 127 ? -29.083 14.134 -5.600  1.00 20.55 ? 95  PHE   A CZ   1 
ATOM   679  N  N    . THR   A 1 128 ? -33.641 15.477 -9.413  1.00 14.92 ? 96  THR   A N    1 
ATOM   680  C  CA   . THR   A 1 128 ? -34.595 16.092 -8.498  1.00 15.45 ? 96  THR   A CA   1 
ATOM   681  C  C    . THR   A 1 128 ? -34.656 15.276 -7.213  1.00 15.93 ? 96  THR   A C    1 
ATOM   682  O  O    . THR   A 1 128 ? -34.747 14.044 -7.254  1.00 19.36 ? 96  THR   A O    1 
ATOM   683  C  CB   . THR   A 1 128 ? -35.976 16.141 -9.152  1.00 16.66 ? 96  THR   A CB   1 
ATOM   684  O  OG1  . THR   A 1 128 ? -35.924 16.976 -10.316 1.00 19.65 ? 96  THR   A OG1  1 
ATOM   685  C  CG2  . THR   A 1 128 ? -37.012 16.699 -8.190  1.00 19.69 ? 96  THR   A CG2  1 
ATOM   686  N  N    . ALA   A 1 129 ? -34.619 15.958 -6.070  1.00 15.84 ? 97  ALA   A N    1 
ATOM   687  C  CA   . ALA   A 1 129 ? -34.654 15.293 -4.774  1.00 16.46 ? 97  ALA   A CA   1 
ATOM   688  C  C    . ALA   A 1 129 ? -35.860 15.755 -3.971  1.00 16.90 ? 97  ALA   A C    1 
ATOM   689  O  O    . ALA   A 1 129 ? -36.273 16.918 -4.058  1.00 18.21 ? 97  ALA   A O    1 
ATOM   690  C  CB   . ALA   A 1 129 ? -33.377 15.568 -3.971  1.00 18.95 ? 97  ALA   A CB   1 
ATOM   691  N  N    . ASN   A 1 130 ? -36.422 14.822 -3.197  1.00 18.03 ? 98  ASN   A N    1 
ATOM   692  C  CA   . ASN   A 1 130 ? -37.428 15.088 -2.169  1.00 20.82 ? 98  ASN   A CA   1 
ATOM   693  C  C    . ASN   A 1 130 ? -38.746 15.608 -2.735  1.00 23.12 ? 98  ASN   A C    1 
ATOM   694  O  O    . ASN   A 1 130 ? -39.530 16.236 -2.014  1.00 26.27 ? 98  ASN   A O    1 
ATOM   695  C  CB   . ASN   A 1 130 ? -36.873 15.986 -1.059  1.00 21.33 ? 98  ASN   A CB   1 
ATOM   696  C  CG   . ASN   A 1 130 ? -35.553 15.479 -0.533  1.00 20.69 ? 98  ASN   A CG   1 
ATOM   697  O  OD1  . ASN   A 1 130 ? -35.447 14.322 -0.111  1.00 20.20 ? 98  ASN   A OD1  1 
ATOM   698  N  ND2  . ASN   A 1 130 ? -34.516 16.315 -0.616  1.00 21.32 ? 98  ASN   A ND2  1 
ATOM   699  N  N    . ASP   A 1 131 ? -39.002 15.305 -4.011  1.00 25.88 ? 99  ASP   A N    1 
ATOM   700  C  CA   . ASP   A 1 131 ? -40.208 15.750 -4.704  1.00 32.71 ? 99  ASP   A CA   1 
ATOM   701  C  C    . ASP   A 1 131 ? -41.477 15.245 -4.025  1.00 32.35 ? 99  ASP   A C    1 
ATOM   702  O  O    . ASP   A 1 131 ? -42.514 15.919 -4.063  1.00 32.38 ? 99  ASP   A O    1 
ATOM   703  C  CB   . ASP   A 1 131 ? -40.148 15.228 -6.144  1.00 40.55 ? 99  ASP   A CB   1 
ATOM   704  C  CG   . ASP   A 1 131 ? -41.125 15.921 -7.070  1.00 48.38 ? 99  ASP   A CG   1 
ATOM   705  O  OD1  . ASP   A 1 131 ? -41.648 16.994 -6.706  1.00 51.02 ? 99  ASP   A OD1  1 
ATOM   706  O  OD2  . ASP   A 1 131 ? -41.364 15.389 -8.174  1.00 51.33 ? 99  ASP   A OD2  1 
ATOM   707  N  N    . SER   A 1 132 ? -41.424 14.062 -3.413  1.00 32.16 ? 100 SER   A N    1 
ATOM   708  C  CA   . SER   A 1 132 ? -42.576 13.466 -2.744  1.00 33.51 ? 100 SER   A CA   1 
ATOM   709  C  C    . SER   A 1 132 ? -42.328 13.304 -1.250  1.00 32.35 ? 100 SER   A C    1 
ATOM   710  O  O    . SER   A 1 132 ? -42.826 12.362 -0.628  1.00 35.60 ? 100 SER   A O    1 
ATOM   711  C  CB   . SER   A 1 132 ? -42.935 12.119 -3.370  1.00 38.57 ? 100 SER   A CB   1 
ATOM   712  O  OG   . SER   A 1 132 ? -43.042 12.218 -4.777  1.00 42.77 ? 100 SER   A OG   1 
ATOM   713  N  N    . GLY   A 1 133 ? -41.573 14.220 -0.656  1.00 29.13 ? 101 GLY   A N    1 
ATOM   714  C  CA   . GLY   A 1 133 ? -41.213 14.106 0.733   1.00 26.43 ? 101 GLY   A CA   1 
ATOM   715  C  C    . GLY   A 1 133 ? -39.780 13.648 0.897   1.00 24.84 ? 101 GLY   A C    1 
ATOM   716  O  O    . GLY   A 1 133 ? -39.122 13.221 -0.061  1.00 24.24 ? 101 GLY   A O    1 
ATOM   717  N  N    . PRO   A 1 134 ? -39.274 13.713 2.126   1.00 25.77 ? 102 PRO   A N    1 
ATOM   718  C  CA   . PRO   A 1 134 ? -37.854 13.436 2.350   1.00 24.94 ? 102 PRO   A CA   1 
ATOM   719  C  C    . PRO   A 1 134 ? -37.509 12.003 1.990   1.00 23.41 ? 102 PRO   A C    1 
ATOM   720  O  O    . PRO   A 1 134 ? -38.244 11.063 2.306   1.00 24.48 ? 102 PRO   A O    1 
ATOM   721  C  CB   . PRO   A 1 134 ? -37.676 13.686 3.852   1.00 27.00 ? 102 PRO   A CB   1 
ATOM   722  C  CG   . PRO   A 1 134 ? -38.847 14.524 4.245   1.00 28.59 ? 102 PRO   A CG   1 
ATOM   723  C  CD   . PRO   A 1 134 ? -39.968 14.052 3.378   1.00 26.91 ? 102 PRO   A CD   1 
ATOM   724  N  N    . ARG   A 1 135 ? -36.387 11.852 1.297   1.00 22.71 ? 103 ARG   A N    1 
ATOM   725  C  CA   . ARG   A 1 135 ? -35.800 10.553 1.017   1.00 22.36 ? 103 ARG   A CA   1 
ATOM   726  C  C    . ARG   A 1 135 ? -34.323 10.604 1.374   1.00 21.16 ? 103 ARG   A C    1 
ATOM   727  O  O    . ARG   A 1 135 ? -33.735 11.679 1.523   1.00 21.03 ? 103 ARG   A O    1 
ATOM   728  C  CB   . ARG   A 1 135 ? -35.939 10.170 -0.465  1.00 21.70 ? 103 ARG   A CB   1 
ATOM   729  C  CG   . ARG   A 1 135 ? -37.369 10.093 -0.973  1.00 23.37 ? 103 ARG   A CG   1 
ATOM   730  C  CD   . ARG   A 1 135 ? -38.130 8.921  -0.351  1.00 26.67 ? 103 ARG   A CD   1 
ATOM   731  N  NE   . ARG   A 1 135 ? -39.464 8.778  -0.927  1.00 29.46 ? 103 ARG   A NE   1 
ATOM   732  C  CZ   . ARG   A 1 135 ? -40.546 9.389  -0.455  1.00 30.49 ? 103 ARG   A CZ   1 
ATOM   733  N  NH1  . ARG   A 1 135 ? -40.452 10.177 0.606   1.00 30.94 ? 103 ARG   A NH1  1 
ATOM   734  N  NH2  . ARG   A 1 135 ? -41.721 9.213  -1.041  1.00 32.19 ? 103 ARG   A NH2  1 
ATOM   735  N  N    . ARG   A 1 136 ? -33.723 9.426  1.502   1.00 20.54 ? 104 ARG   A N    1 
ATOM   736  C  CA   . ARG   A 1 136 ? -32.283 9.301  1.674   1.00 21.53 ? 104 ARG   A CA   1 
ATOM   737  C  C    . ARG   A 1 136 ? -31.688 8.813  0.361   1.00 18.05 ? 104 ARG   A C    1 
ATOM   738  O  O    . ARG   A 1 136 ? -32.202 7.864  -0.244  1.00 19.81 ? 104 ARG   A O    1 
ATOM   739  C  CB   . ARG   A 1 136 ? -31.950 8.314  2.791   1.00 28.45 ? 104 ARG   A CB   1 
ATOM   740  C  CG   . ARG   A 1 136 ? -32.354 8.794  4.176   1.00 36.92 ? 104 ARG   A CG   1 
ATOM   741  C  CD   . ARG   A 1 136 ? -31.417 8.245  5.240   1.00 45.13 ? 104 ARG   A CD   1 
ATOM   742  N  NE   . ARG   A 1 136 ? -31.864 8.588  6.587   1.00 52.60 ? 104 ARG   A NE   1 
ATOM   743  C  CZ   . ARG   A 1 136 ? -32.506 7.750  7.395   1.00 57.88 ? 104 ARG   A CZ   1 
ATOM   744  N  NH1  . ARG   A 1 136 ? -32.772 6.514  6.995   1.00 59.53 ? 104 ARG   A NH1  1 
ATOM   745  N  NH2  . ARG   A 1 136 ? -32.877 8.147  8.604   1.00 59.40 ? 104 ARG   A NH2  1 
ATOM   746  N  N    . TYR   A 1 137 ? -30.615 9.467  -0.081  1.00 18.12 ? 105 TYR   A N    1 
ATOM   747  C  CA   . TYR   A 1 137 ? -30.004 9.207  -1.377  1.00 16.27 ? 105 TYR   A CA   1 
ATOM   748  C  C    . TYR   A 1 137 ? -28.567 8.755  -1.185  1.00 16.56 ? 105 TYR   A C    1 
ATOM   749  O  O    . TYR   A 1 137 ? -27.788 9.433  -0.510  1.00 18.05 ? 105 TYR   A O    1 
ATOM   750  C  CB   . TYR   A 1 137 ? -30.012 10.478 -2.245  1.00 17.68 ? 105 TYR   A CB   1 
ATOM   751  C  CG   . TYR   A 1 137 ? -31.400 10.959 -2.560  1.00 17.72 ? 105 TYR   A CG   1 
ATOM   752  C  CD1  . TYR   A 1 137 ? -32.095 11.767 -1.664  1.00 17.34 ? 105 TYR   A CD1  1 
ATOM   753  C  CD2  . TYR   A 1 137 ? -32.028 10.597 -3.741  1.00 18.38 ? 105 TYR   A CD2  1 
ATOM   754  C  CE1  . TYR   A 1 137 ? -33.380 12.194 -1.942  1.00 18.33 ? 105 TYR   A CE1  1 
ATOM   755  C  CE2  . TYR   A 1 137 ? -33.312 11.027 -4.032  1.00 18.60 ? 105 TYR   A CE2  1 
ATOM   756  C  CZ   . TYR   A 1 137 ? -33.983 11.822 -3.123  1.00 17.75 ? 105 TYR   A CZ   1 
ATOM   757  O  OH   . TYR   A 1 137 ? -35.263 12.249 -3.377  1.00 18.62 ? 105 TYR   A OH   1 
ATOM   758  N  N    . THR   A 1 138 ? -28.220 7.615  -1.776  1.00 15.62 ? 106 THR   A N    1 
ATOM   759  C  CA   . THR   A 1 138 ? -26.831 7.227  -1.971  1.00 16.49 ? 106 THR   A CA   1 
ATOM   760  C  C    . THR   A 1 138 ? -26.541 7.307  -3.460  1.00 17.26 ? 106 THR   A C    1 
ATOM   761  O  O    . THR   A 1 138 ? -27.221 6.663  -4.263  1.00 18.45 ? 106 THR   A O    1 
ATOM   762  C  CB   . THR   A 1 138 ? -26.567 5.815  -1.456  1.00 19.23 ? 106 THR   A CB   1 
ATOM   763  O  OG1  . THR   A 1 138 ? -26.786 5.791  -0.042  1.00 23.16 ? 106 THR   A OG1  1 
ATOM   764  C  CG2  . THR   A 1 138 ? -25.135 5.425  -1.755  1.00 21.21 ? 106 THR   A CG2  1 
ATOM   765  N  N    . ILE   A 1 139 ? -25.584 8.146  -3.826  1.00 17.36 ? 107 ILE   A N    1 
ATOM   766  C  CA   . ILE   A 1 139 ? -25.103 8.252  -5.195  1.00 17.55 ? 107 ILE   A CA   1 
ATOM   767  C  C    . ILE   A 1 139 ? -23.807 7.466  -5.251  1.00 16.71 ? 107 ILE   A C    1 
ATOM   768  O  O    . ILE   A 1 139 ? -22.881 7.723  -4.472  1.00 17.43 ? 107 ILE   A O    1 
ATOM   769  C  CB   . ILE   A 1 139 ? -24.856 9.718  -5.588  1.00 19.96 ? 107 ILE   A CB   1 
ATOM   770  C  CG1  . ILE   A 1 139 ? -26.108 10.574 -5.364  1.00 24.12 ? 107 ILE   A CG1  1 
ATOM   771  C  CG2  . ILE   A 1 139 ? -24.358 9.798  -7.031  1.00 21.06 ? 107 ILE   A CG2  1 
ATOM   772  C  CD1  . ILE   A 1 139 ? -27.308 10.137 -6.169  1.00 26.16 ? 107 ILE   A CD1  1 
ATOM   773  N  N    . ALA   A 1 140 ? -23.733 6.492  -6.140  1.00 17.85 ? 108 ALA   A N    1 
ATOM   774  C  CA   . ALA   A 1 140 ? -22.512 5.722  -6.290  1.00 18.05 ? 108 ALA   A CA   1 
ATOM   775  C  C    . ALA   A 1 140 ? -21.947 5.926  -7.684  1.00 16.87 ? 108 ALA   A C    1 
ATOM   776  O  O    . ALA   A 1 140 ? -22.693 6.077  -8.653  1.00 17.98 ? 108 ALA   A O    1 
ATOM   777  C  CB   . ALA   A 1 140 ? -22.758 4.242  -6.037  1.00 20.03 ? 108 ALA   A CB   1 
ATOM   778  N  N    . ALA   A 1 141 ? -20.624 5.931  -7.776  1.00 15.45 ? 109 ALA   A N    1 
ATOM   779  C  CA   . ALA   A 1 141 ? -19.944 6.098  -9.051  1.00 15.09 ? 109 ALA   A CA   1 
ATOM   780  C  C    . ALA   A 1 141 ? -18.802 5.100  -9.137  1.00 14.11 ? 109 ALA   A C    1 
ATOM   781  O  O    . ALA   A 1 141 ? -18.056 4.932  -8.176  1.00 15.81 ? 109 ALA   A O    1 
ATOM   782  C  CB   . ALA   A 1 141 ? -19.403 7.525  -9.203  1.00 18.05 ? 109 ALA   A CB   1 
ATOM   783  N  N    . LEU   A 1 142 ? -18.675 4.436  -10.284 1.00 13.16 ? 110 LEU   A N    1 
ATOM   784  C  CA   . LEU   A 1 142 ? -17.581 3.511  -10.566 1.00 13.18 ? 110 LEU   A CA   1 
ATOM   785  C  C    . LEU   A 1 142 ? -16.747 4.115  -11.690 1.00 13.38 ? 110 LEU   A C    1 
ATOM   786  O  O    . LEU   A 1 142 ? -17.268 4.347  -12.786 1.00 15.06 ? 110 LEU   A O    1 
ATOM   787  C  CB   . LEU   A 1 142 ? -18.141 2.142  -10.972 1.00 15.59 ? 110 LEU   A CB   1 
ATOM   788  C  CG   . LEU   A 1 142 ? -17.120 1.082  -11.384 1.00 15.77 ? 110 LEU   A CG   1 
ATOM   789  C  CD1  . LEU   A 1 142 ? -16.183 0.749  -10.237 1.00 15.88 ? 110 LEU   A CD1  1 
ATOM   790  C  CD2  . LEU   A 1 142 ? -17.821 -0.186 -11.876 1.00 19.56 ? 110 LEU   A CD2  1 
ATOM   791  N  N    . LEU   A 1 143 ? -15.461 4.362  -11.425 1.00 12.52 ? 111 LEU   A N    1 
ATOM   792  C  CA   . LEU   A 1 143 ? -14.618 5.168  -12.303 1.00 12.14 ? 111 LEU   A CA   1 
ATOM   793  C  C    . LEU   A 1 143 ? -13.572 4.346  -13.053 1.00 12.92 ? 111 LEU   A C    1 
ATOM   794  O  O    . LEU   A 1 143 ? -12.861 3.532  -12.455 1.00 13.35 ? 111 LEU   A O    1 
ATOM   795  C  CB   . LEU   A 1 143 ? -13.862 6.216  -11.491 1.00 14.40 ? 111 LEU   A CB   1 
ATOM   796  C  CG   . LEU   A 1 143 ? -14.645 7.130  -10.556 1.00 13.73 ? 111 LEU   A CG   1 
ATOM   797  C  CD1  . LEU   A 1 143 ? -13.662 8.155  -9.993  1.00 15.88 ? 111 LEU   A CD1  1 
ATOM   798  C  CD2  . LEU   A 1 143 ? -15.798 7.790  -11.297 1.00 13.75 ? 111 LEU   A CD2  1 
ATOM   799  N  N    . SER   A 1 144 ? -13.426 4.640  -14.341 1.00 13.01 ? 112 SER   A N    1 
ATOM   800  C  CA   . SER   A 1 144 ? -12.329 4.206  -15.192 1.00 13.56 ? 112 SER   A CA   1 
ATOM   801  C  C    . SER   A 1 144 ? -11.814 5.421  -15.952 1.00 13.28 ? 112 SER   A C    1 
ATOM   802  O  O    . SER   A 1 144 ? -12.505 6.439  -16.046 1.00 13.52 ? 112 SER   A O    1 
ATOM   803  C  CB   . SER   A 1 144 ? -12.808 3.150  -16.198 1.00 14.56 ? 112 SER   A CB   1 
ATOM   804  O  OG   . SER   A 1 144 ? -13.272 1.993  -15.522 1.00 16.20 ? 112 SER   A OG   1 
ATOM   805  N  N    . PRO   A 1 145 ? -10.607 5.346  -16.522 1.00 13.79 ? 113 PRO   A N    1 
ATOM   806  C  CA   . PRO   A 1 145 ? -10.062 6.537  -17.197 1.00 14.37 ? 113 PRO   A CA   1 
ATOM   807  C  C    . PRO   A 1 145 ? -10.934 7.082  -18.315 1.00 14.23 ? 113 PRO   A C    1 
ATOM   808  O  O    . PRO   A 1 145 ? -11.005 8.311  -18.485 1.00 14.46 ? 113 PRO   A O    1 
ATOM   809  C  CB   . PRO   A 1 145 ? -8.693  6.048  -17.690 1.00 14.66 ? 113 PRO   A CB   1 
ATOM   810  C  CG   . PRO   A 1 145 ? -8.290  5.058  -16.637 1.00 16.20 ? 113 PRO   A CG   1 
ATOM   811  C  CD   . PRO   A 1 145 ? -9.567  4.329  -16.304 1.00 15.57 ? 113 PRO   A CD   1 
ATOM   812  N  N    . TYR   A 1 146 ? -11.597 6.214  -19.087 1.00 13.60 ? 114 TYR   A N    1 
ATOM   813  C  CA   . TYR   A 1 146 ? -12.431 6.659  -20.199 1.00 14.14 ? 114 TYR   A CA   1 
ATOM   814  C  C    . TYR   A 1 146 ? -13.909 6.383  -19.994 1.00 14.62 ? 114 TYR   A C    1 
ATOM   815  O  O    . TYR   A 1 146 ? -14.680 6.496  -20.952 1.00 15.89 ? 114 TYR   A O    1 
ATOM   816  C  CB   . TYR   A 1 146 ? -11.962 6.059  -21.528 1.00 16.33 ? 114 TYR   A CB   1 
ATOM   817  C  CG   . TYR   A 1 146 ? -10.744 6.755  -22.090 1.00 16.11 ? 114 TYR   A CG   1 
ATOM   818  C  CD1  . TYR   A 1 146 ? -9.485  6.503  -21.553 1.00 20.39 ? 114 TYR   A CD1  1 
ATOM   819  C  CD2  . TYR   A 1 146 ? -10.842 7.647  -23.154 1.00 16.97 ? 114 TYR   A CD2  1 
ATOM   820  C  CE1  . TYR   A 1 146 ? -8.359  7.118  -22.046 1.00 23.64 ? 114 TYR   A CE1  1 
ATOM   821  C  CE2  . TYR   A 1 146 ? -9.710  8.286  -23.654 1.00 19.44 ? 114 TYR   A CE2  1 
ATOM   822  C  CZ   . TYR   A 1 146 ? -8.469  8.011  -23.092 1.00 23.37 ? 114 TYR   A CZ   1 
ATOM   823  O  OH   . TYR   A 1 146 ? -7.333  8.616  -23.580 1.00 26.37 ? 114 TYR   A OH   1 
ATOM   824  N  N    . SER   A 1 147 ? -14.333 6.045  -18.778 1.00 13.81 ? 115 SER   A N    1 
ATOM   825  C  CA   . SER   A 1 147 ? -15.713 5.639  -18.595 1.00 14.75 ? 115 SER   A CA   1 
ATOM   826  C  C    . SER   A 1 147 ? -16.093 5.846  -17.143 1.00 13.45 ? 115 SER   A C    1 
ATOM   827  O  O    . SER   A 1 147 ? -15.242 5.780  -16.256 1.00 16.22 ? 115 SER   A O    1 
ATOM   828  C  CB   . SER   A 1 147 ? -15.867 4.165  -18.988 1.00 18.56 ? 115 SER   A CB   1 
ATOM   829  O  OG   . SER   A 1 147 ? -17.175 3.677  -18.741 1.00 24.00 ? 115 SER   A OG   1 
ATOM   830  N  N    . TYR   A 1 148 ? -17.374 6.108  -16.906 1.00 14.05 ? 116 TYR   A N    1 
ATOM   831  C  CA   . TYR   A 1 148 ? -17.881 6.008  -15.549 1.00 14.83 ? 116 TYR   A CA   1 
ATOM   832  C  C    . TYR   A 1 148 ? -19.315 5.520  -15.576 1.00 14.87 ? 116 TYR   A C    1 
ATOM   833  O  O    . TYR   A 1 148 ? -20.041 5.704  -16.553 1.00 14.90 ? 116 TYR   A O    1 
ATOM   834  C  CB   . TYR   A 1 148 ? -17.747 7.294  -14.722 1.00 15.79 ? 116 TYR   A CB   1 
ATOM   835  C  CG   . TYR   A 1 148 ? -18.574 8.456  -15.202 1.00 15.81 ? 116 TYR   A CG   1 
ATOM   836  C  CD1  . TYR   A 1 148 ? -19.861 8.666  -14.726 1.00 17.07 ? 116 TYR   A CD1  1 
ATOM   837  C  CD2  . TYR   A 1 148 ? -18.042 9.385  -16.088 1.00 17.07 ? 116 TYR   A CD2  1 
ATOM   838  C  CE1  . TYR   A 1 148 ? -20.605 9.758  -15.145 1.00 19.37 ? 116 TYR   A CE1  1 
ATOM   839  C  CE2  . TYR   A 1 148 ? -18.774 10.463 -16.518 1.00 18.96 ? 116 TYR   A CE2  1 
ATOM   840  C  CZ   . TYR   A 1 148 ? -20.055 10.650 -16.046 1.00 19.31 ? 116 TYR   A CZ   1 
ATOM   841  O  OH   . TYR   A 1 148 ? -20.778 11.747 -16.466 1.00 24.50 ? 116 TYR   A OH   1 
ATOM   842  N  N    . SER   A 1 149 ? -19.696 4.874  -14.488 1.00 15.27 ? 117 SER   A N    1 
ATOM   843  C  CA   A SER   A 1 149 ? -21.056 4.425  -14.273 0.50 16.17 ? 117 SER   A CA   1 
ATOM   844  C  CA   B SER   A 1 149 ? -21.049 4.402  -14.264 0.50 16.91 ? 117 SER   A CA   1 
ATOM   845  C  C    . SER   A 1 149 ? -21.544 5.026  -12.970 1.00 16.23 ? 117 SER   A C    1 
ATOM   846  O  O    . SER   A 1 149 ? -20.781 5.169  -12.011 1.00 17.39 ? 117 SER   A O    1 
ATOM   847  C  CB   A SER   A 1 149 ? -21.120 2.902  -14.187 0.50 17.54 ? 117 SER   A CB   1 
ATOM   848  C  CB   B SER   A 1 149 ? -21.051 2.872  -14.143 0.50 19.29 ? 117 SER   A CB   1 
ATOM   849  O  OG   A SER   A 1 149 ? -20.604 2.309  -15.361 0.50 18.86 ? 117 SER   A OG   1 
ATOM   850  O  OG   B SER   A 1 149 ? -22.336 2.362  -13.825 0.50 22.32 ? 117 SER   A OG   1 
ATOM   851  N  N    . THR   A 1 150 ? -22.807 5.406  -12.942 1.00 15.45 ? 118 THR   A N    1 
ATOM   852  C  CA   . THR   A 1 150 ? -23.347 5.982  -11.728 1.00 16.26 ? 118 THR   A CA   1 
ATOM   853  C  C    . THR   A 1 150 ? -24.736 5.424  -11.495 1.00 16.34 ? 118 THR   A C    1 
ATOM   854  O  O    . THR   A 1 150 ? -25.473 5.166  -12.448 1.00 16.61 ? 118 THR   A O    1 
ATOM   855  C  CB   . THR   A 1 150 ? -23.332 7.510  -11.774 1.00 18.93 ? 118 THR   A CB   1 
ATOM   856  O  OG1  . THR   A 1 150 ? -23.776 8.012  -10.518 1.00 20.36 ? 118 THR   A OG1  1 
ATOM   857  C  CG2  . THR   A 1 150 ? -24.227 8.055  -12.894 1.00 20.38 ? 118 THR   A CG2  1 
ATOM   858  N  N    . THR   A 1 151 ? -25.077 5.205  -10.231 1.00 14.83 ? 119 THR   A N    1 
ATOM   859  C  CA   . THR   A 1 151 ? -26.403 4.728  -9.873  1.00 15.52 ? 119 THR   A CA   1 
ATOM   860  C  C    . THR   A 1 151 ? -26.836 5.432  -8.598  1.00 15.73 ? 119 THR   A C    1 
ATOM   861  O  O    . THR   A 1 151 ? -26.037 6.081  -7.914  1.00 17.73 ? 119 THR   A O    1 
ATOM   862  C  CB   . THR   A 1 151 ? -26.453 3.197  -9.720  1.00 17.68 ? 119 THR   A CB   1 
ATOM   863  O  OG1  . THR   A 1 151 ? -27.824 2.752  -9.725  1.00 19.03 ? 119 THR   A OG1  1 
ATOM   864  C  CG2  . THR   A 1 151 ? -25.784 2.769  -8.426  1.00 19.51 ? 119 THR   A CG2  1 
ATOM   865  N  N    . ALA   A 1 152 ? -28.117 5.319  -8.293  1.00 15.52 ? 120 ALA   A N    1 
ATOM   866  C  CA   . ALA   A 1 152 ? -28.668 5.913  -7.089  1.00 15.02 ? 120 ALA   A CA   1 
ATOM   867  C  C    . ALA   A 1 152 ? -29.459 4.858  -6.336  1.00 14.99 ? 120 ALA   A C    1 
ATOM   868  O  O    . ALA   A 1 152 ? -30.148 4.034  -6.942  1.00 16.31 ? 120 ALA   A O    1 
ATOM   869  C  CB   . ALA   A 1 152 ? -29.594 7.080  -7.437  1.00 16.60 ? 120 ALA   A CB   1 
ATOM   870  N  N    . VAL   A 1 153 ? -29.333 4.878  -5.013  1.00 15.50 ? 121 VAL   A N    1 
ATOM   871  C  CA   . VAL   A 1 153 ? -30.178 4.100  -4.118  1.00 16.61 ? 121 VAL   A CA   1 
ATOM   872  C  C    . VAL   A 1 153 ? -31.005 5.102  -3.332  1.00 17.88 ? 121 VAL   A C    1 
ATOM   873  O  O    . VAL   A 1 153 ? -30.452 5.947  -2.614  1.00 19.36 ? 121 VAL   A O    1 
ATOM   874  C  CB   . VAL   A 1 153 ? -29.340 3.213  -3.187  1.00 20.17 ? 121 VAL   A CB   1 
ATOM   875  C  CG1  . VAL   A 1 153 ? -30.247 2.450  -2.223  1.00 22.69 ? 121 VAL   A CG1  1 
ATOM   876  C  CG2  . VAL   A 1 153 ? -28.501 2.247  -4.007  1.00 25.74 ? 121 VAL   A CG2  1 
ATOM   877  N  N    . VAL   A 1 154 ? -32.323 5.043  -3.496  1.00 18.74 ? 122 VAL   A N    1 
ATOM   878  C  CA   . VAL   A 1 154 ? -33.232 6.004  -2.881  1.00 18.80 ? 122 VAL   A CA   1 
ATOM   879  C  C    . VAL   A 1 154 ? -34.108 5.238  -1.909  1.00 19.98 ? 122 VAL   A C    1 
ATOM   880  O  O    . VAL   A 1 154 ? -34.792 4.286  -2.304  1.00 21.83 ? 122 VAL   A O    1 
ATOM   881  C  CB   . VAL   A 1 154 ? -34.083 6.736  -3.932  1.00 21.29 ? 122 VAL   A CB   1 
ATOM   882  C  CG1  . VAL   A 1 154 ? -34.964 7.813  -3.276  1.00 23.01 ? 122 VAL   A CG1  1 
ATOM   883  C  CG2  . VAL   A 1 154 ? -33.190 7.331  -5.004  1.00 22.30 ? 122 VAL   A CG2  1 
ATOM   884  N  N    . THR   A 1 155 ? -34.095 5.655  -0.642  1.00 20.99 ? 123 THR   A N    1 
ATOM   885  C  CA   . THR   A 1 155 ? -34.838 4.964  0.401   1.00 24.73 ? 123 THR   A CA   1 
ATOM   886  C  C    . THR   A 1 155 ? -35.734 5.943  1.148   1.00 25.72 ? 123 THR   A C    1 
ATOM   887  O  O    . THR   A 1 155 ? -35.404 7.121  1.307   1.00 25.18 ? 123 THR   A O    1 
ATOM   888  C  CB   . THR   A 1 155 ? -33.905 4.243  1.386   1.00 29.92 ? 123 THR   A CB   1 
ATOM   889  O  OG1  . THR   A 1 155 ? -33.162 5.204  2.139   1.00 34.34 ? 123 THR   A OG1  1 
ATOM   890  C  CG2  . THR   A 1 155 ? -32.938 3.343  0.644   1.00 29.09 ? 123 THR   A CG2  1 
ATOM   891  N  N    . ASN   A 1 156 ? -36.883 5.438  1.603   1.00 28.57 ? 124 ASN   A N    1 
ATOM   892  C  CA   . ASN   A 1 156 ? -37.832 6.242  2.356   1.00 33.96 ? 124 ASN   A CA   1 
ATOM   893  C  C    . ASN   A 1 156 ? -37.661 5.942  3.835   1.00 39.37 ? 124 ASN   A C    1 
ATOM   894  O  O    . ASN   A 1 156 ? -37.918 4.803  4.256   1.00 39.06 ? 124 ASN   A O    1 
ATOM   895  C  CB   . ASN   A 1 156 ? -39.254 5.912  1.916   1.00 36.06 ? 124 ASN   A CB   1 
ATOM   896  C  CG   . ASN   A 1 156 ? -40.287 6.870  2.487   1.00 38.24 ? 124 ASN   A CG   1 
ATOM   897  O  OD1  . ASN   A 1 156 ? -40.048 7.544  3.489   1.00 39.53 ? 124 ASN   A OD1  1 
ATOM   898  N  ND2  . ASN   A 1 156 ? -41.450 6.929  1.847   1.00 38.93 ? 124 ASN   A ND2  1 
ATOM   899  N  N    . PRO   A 1 157 ? -37.247 6.914  4.662   1.00 44.63 ? 125 PRO   A N    1 
ATOM   900  C  CA   . PRO   A 1 157 ? -37.023 6.681  6.093   1.00 48.73 ? 125 PRO   A CA   1 
ATOM   901  C  C    . PRO   A 1 157 ? -38.333 6.533  6.860   1.00 51.67 ? 125 PRO   A C    1 
ATOM   902  O  O    . PRO   A 1 157 ? -38.530 5.509  7.514   1.00 53.79 ? 125 PRO   A O    1 
ATOM   903  C  CB   . PRO   A 1 157 ? -36.300 7.953  6.536   1.00 48.50 ? 125 PRO   A CB   1 
ATOM   904  C  CG   . PRO   A 1 157 ? -36.829 9.004  5.622   1.00 47.65 ? 125 PRO   A CG   1 
ATOM   905  C  CD   . PRO   A 1 157 ? -37.019 8.322  4.291   1.00 45.91 ? 125 PRO   A CD   1 
ATOM   906  N  N    . CYS   B 1 42  ? -16.731 11.762 -39.473 1.00 48.34 ? 10  CYS   B N    1 
ATOM   907  C  CA   . CYS   B 1 42  ? -17.591 11.824 -38.295 1.00 46.09 ? 10  CYS   B CA   1 
ATOM   908  C  C    . CYS   B 1 42  ? -16.773 12.114 -37.035 1.00 37.80 ? 10  CYS   B C    1 
ATOM   909  O  O    . CYS   B 1 42  ? -16.439 11.208 -36.271 1.00 36.96 ? 10  CYS   B O    1 
ATOM   910  C  CB   . CYS   B 1 42  ? -18.385 10.526 -38.140 1.00 51.85 ? 10  CYS   B CB   1 
ATOM   911  S  SG   . CYS   B 1 42  ? -20.074 10.763 -37.539 1.00 56.09 ? 10  CYS   B SG   1 
ATOM   912  N  N    . PRO   B 1 43  ? -16.443 13.388 -36.826 1.00 30.66 ? 11  PRO   B N    1 
ATOM   913  C  CA   . PRO   B 1 43  ? -15.619 13.744 -35.660 1.00 25.44 ? 11  PRO   B CA   1 
ATOM   914  C  C    . PRO   B 1 43  ? -16.281 13.480 -34.319 1.00 21.55 ? 11  PRO   B C    1 
ATOM   915  O  O    . PRO   B 1 43  ? -15.569 13.248 -33.334 1.00 21.30 ? 11  PRO   B O    1 
ATOM   916  C  CB   . PRO   B 1 43  ? -15.336 15.242 -35.867 1.00 29.15 ? 11  PRO   B CB   1 
ATOM   917  C  CG   . PRO   B 1 43  ? -16.272 15.684 -36.931 1.00 32.95 ? 11  PRO   B CG   1 
ATOM   918  C  CD   . PRO   B 1 43  ? -16.572 14.505 -37.774 1.00 32.47 ? 11  PRO   B CD   1 
ATOM   919  N  N    . LEU   B 1 44  ? -17.608 13.518 -34.238 1.00 18.58 ? 12  LEU   B N    1 
ATOM   920  C  CA   . LEU   B 1 44  ? -18.302 13.323 -32.969 1.00 17.28 ? 12  LEU   B CA   1 
ATOM   921  C  C    . LEU   B 1 44  ? -19.584 12.556 -33.234 1.00 17.45 ? 12  LEU   B C    1 
ATOM   922  O  O    . LEU   B 1 44  ? -20.427 13.009 -34.012 1.00 18.89 ? 12  LEU   B O    1 
ATOM   923  C  CB   . LEU   B 1 44  ? -18.626 14.678 -32.317 1.00 18.17 ? 12  LEU   B CB   1 
ATOM   924  C  CG   . LEU   B 1 44  ? -19.351 14.640 -30.972 1.00 19.01 ? 12  LEU   B CG   1 
ATOM   925  C  CD1  . LEU   B 1 44  ? -18.504 13.919 -29.930 1.00 19.55 ? 12  LEU   B CD1  1 
ATOM   926  C  CD2  . LEU   B 1 44  ? -19.701 16.047 -30.506 1.00 21.95 ? 12  LEU   B CD2  1 
ATOM   927  N  N    . MET   B 1 45  ? -19.725 11.395 -32.593 1.00 16.37 ? 13  MET   B N    1 
ATOM   928  C  CA   . MET   B 1 45  ? -20.923 10.580 -32.701 1.00 18.03 ? 13  MET   B CA   1 
ATOM   929  C  C    . MET   B 1 45  ? -21.323 10.158 -31.298 1.00 15.00 ? 13  MET   B C    1 
ATOM   930  O  O    . MET   B 1 45  ? -20.460 9.932  -30.444 1.00 15.89 ? 13  MET   B O    1 
ATOM   931  C  CB   . MET   B 1 45  ? -20.652 9.326  -33.555 1.00 24.33 ? 13  MET   B CB   1 
ATOM   932  C  CG   . MET   B 1 45  ? -21.903 8.522  -33.909 1.00 35.03 ? 13  MET   B CG   1 
ATOM   933  S  SD   . MET   B 1 45  ? -22.296 7.206  -32.732 1.00 46.84 ? 13  MET   B SD   1 
ATOM   934  C  CE   . MET   B 1 45  ? -21.034 6.000  -33.130 1.00 60.33 ? 13  MET   B CE   1 
ATOM   935  N  N    . VAL   B 1 46  ? -22.626 10.060 -31.053 1.00 14.25 ? 14  VAL   B N    1 
ATOM   936  C  CA   . VAL   B 1 46  ? -23.146 9.606  -29.768 1.00 14.35 ? 14  VAL   B CA   1 
ATOM   937  C  C    . VAL   B 1 46  ? -24.029 8.391  -30.015 1.00 14.56 ? 14  VAL   B C    1 
ATOM   938  O  O    . VAL   B 1 46  ? -24.844 8.392  -30.942 1.00 16.54 ? 14  VAL   B O    1 
ATOM   939  C  CB   . VAL   B 1 46  ? -23.919 10.722 -29.046 1.00 15.97 ? 14  VAL   B CB   1 
ATOM   940  C  CG1  . VAL   B 1 46  ? -24.371 10.240 -27.680 1.00 17.01 ? 14  VAL   B CG1  1 
ATOM   941  C  CG2  . VAL   B 1 46  ? -23.054 11.975 -28.921 1.00 16.91 ? 14  VAL   B CG2  1 
ATOM   942  N  N    . LYS   B 1 47  ? -23.848 7.349  -29.212 1.00 14.39 ? 15  LYS   B N    1 
ATOM   943  C  CA   . LYS   B 1 47  ? -24.644 6.136  -29.327 1.00 15.81 ? 15  LYS   B CA   1 
ATOM   944  C  C    . LYS   B 1 47  ? -25.258 5.844  -27.968 1.00 14.37 ? 15  LYS   B C    1 
ATOM   945  O  O    . LYS   B 1 47  ? -24.569 5.919  -26.945 1.00 15.76 ? 15  LYS   B O    1 
ATOM   946  C  CB   . LYS   B 1 47  ? -23.797 4.950  -29.793 1.00 20.20 ? 15  LYS   B CB   1 
ATOM   947  C  CG   . LYS   B 1 47  ? -24.624 3.710  -30.065 1.00 25.59 ? 15  LYS   B CG   1 
ATOM   948  C  CD   . LYS   B 1 47  ? -23.841 2.702  -30.891 1.00 30.60 ? 15  LYS   B CD   1 
ATOM   949  C  CE   . LYS   B 1 47  ? -24.606 1.400  -31.062 1.00 34.18 ? 15  LYS   B CE   1 
ATOM   950  N  NZ   . LYS   B 1 47  ? -25.764 1.550  -31.982 1.00 37.52 ? 15  LYS   B NZ   1 
ATOM   951  N  N    . VAL   B 1 48  ? -26.550 5.531  -27.949 1.00 14.41 ? 16  VAL   B N    1 
ATOM   952  C  CA   . VAL   B 1 48  ? -27.292 5.360  -26.705 1.00 14.75 ? 16  VAL   B CA   1 
ATOM   953  C  C    . VAL   B 1 48  ? -28.030 4.029  -26.748 1.00 15.39 ? 16  VAL   B C    1 
ATOM   954  O  O    . VAL   B 1 48  ? -28.698 3.715  -27.741 1.00 16.09 ? 16  VAL   B O    1 
ATOM   955  C  CB   . VAL   B 1 48  ? -28.270 6.524  -26.444 1.00 16.16 ? 16  VAL   B CB   1 
ATOM   956  C  CG1  . VAL   B 1 48  ? -28.789 6.452  -25.013 1.00 16.02 ? 16  VAL   B CG1  1 
ATOM   957  C  CG2  . VAL   B 1 48  ? -27.594 7.888  -26.697 1.00 17.09 ? 16  VAL   B CG2  1 
ATOM   958  N  N    . LEU   B 1 49  ? -27.924 3.262  -25.662 1.00 15.32 ? 17  LEU   B N    1 
ATOM   959  C  CA   . LEU   B 1 49  ? -28.555 1.954  -25.529 1.00 13.59 ? 17  LEU   B CA   1 
ATOM   960  C  C    . LEU   B 1 49  ? -29.468 1.933  -24.311 1.00 13.70 ? 17  LEU   B C    1 
ATOM   961  O  O    . LEU   B 1 49  ? -29.250 2.661  -23.339 1.00 13.93 ? 17  LEU   B O    1 
ATOM   962  C  CB   . LEU   B 1 49  ? -27.512 0.854  -25.346 1.00 15.96 ? 17  LEU   B CB   1 
ATOM   963  C  CG   . LEU   B 1 49  ? -26.553 0.615  -26.503 1.00 17.78 ? 17  LEU   B CG   1 
ATOM   964  C  CD1  . LEU   B 1 49  ? -25.641 -0.487 -26.080 1.00 23.12 ? 17  LEU   B CD1  1 
ATOM   965  C  CD2  . LEU   B 1 49  ? -27.307 0.223  -27.758 1.00 20.53 ? 17  LEU   B CD2  1 
ATOM   966  N  N    . ASP   B 1 50  ? -30.477 1.068  -24.365 1.00 13.82 ? 18  ASP   B N    1 
ATOM   967  C  CA   . ASP   B 1 50  ? -31.498 0.944  -23.329 1.00 13.38 ? 18  ASP   B CA   1 
ATOM   968  C  C    . ASP   B 1 50  ? -31.297 -0.411 -22.646 1.00 13.30 ? 18  ASP   B C    1 
ATOM   969  O  O    . ASP   B 1 50  ? -31.439 -1.461 -23.282 1.00 14.01 ? 18  ASP   B O    1 
ATOM   970  C  CB   . ASP   B 1 50  ? -32.865 1.045  -24.005 1.00 14.06 ? 18  ASP   B CB   1 
ATOM   971  C  CG   . ASP   B 1 50  ? -34.035 0.909  -23.047 1.00 15.63 ? 18  ASP   B CG   1 
ATOM   972  O  OD1  . ASP   B 1 50  ? -33.951 0.172  -22.044 1.00 15.55 ? 18  ASP   B OD1  1 
ATOM   973  O  OD2  . ASP   B 1 50  ? -35.068 1.554  -23.323 1.00 17.48 ? 18  ASP   B OD2  1 
ATOM   974  N  N    . ALA   B 1 51  ? -30.942 -0.379 -21.359 1.00 13.55 ? 19  ALA   B N    1 
ATOM   975  C  CA   . ALA   B 1 51  ? -30.650 -1.580 -20.577 1.00 14.39 ? 19  ALA   B CA   1 
ATOM   976  C  C    . ALA   B 1 51  ? -31.895 -2.267 -20.028 1.00 15.13 ? 19  ALA   B C    1 
ATOM   977  O  O    . ALA   B 1 51  ? -31.787 -3.389 -19.502 1.00 16.35 ? 19  ALA   B O    1 
ATOM   978  C  CB   . ALA   B 1 51  ? -29.707 -1.244 -19.421 1.00 15.37 ? 19  ALA   B CB   1 
ATOM   979  N  N    . VAL   B 1 52  ? -33.054 -1.619 -20.112 1.00 15.07 ? 20  VAL   B N    1 
ATOM   980  C  CA   . VAL   B 1 52  ? -34.311 -2.220 -19.680 1.00 16.07 ? 20  VAL   B CA   1 
ATOM   981  C  C    . VAL   B 1 52  ? -34.931 -3.051 -20.790 1.00 16.79 ? 20  VAL   B C    1 
ATOM   982  O  O    . VAL   B 1 52  ? -35.426 -4.154 -20.545 1.00 20.15 ? 20  VAL   B O    1 
ATOM   983  C  CB   . VAL   B 1 52  ? -35.275 -1.117 -19.203 1.00 17.30 ? 20  VAL   B CB   1 
ATOM   984  C  CG1  . VAL   B 1 52  ? -36.674 -1.694 -18.972 1.00 18.45 ? 20  VAL   B CG1  1 
ATOM   985  C  CG2  . VAL   B 1 52  ? -34.755 -0.467 -17.952 1.00 19.11 ? 20  VAL   B CG2  1 
ATOM   986  N  N    . ARG   B 1 53  ? -34.899 -2.535 -22.018 1.00 17.05 ? 21  ARG   B N    1 
ATOM   987  C  CA   . ARG   B 1 53  ? -35.531 -3.181 -23.156 1.00 17.65 ? 21  ARG   B CA   1 
ATOM   988  C  C    . ARG   B 1 53  ? -34.560 -3.964 -24.027 1.00 16.70 ? 21  ARG   B C    1 
ATOM   989  O  O    . ARG   B 1 53  ? -35.013 -4.755 -24.855 1.00 19.86 ? 21  ARG   B O    1 
ATOM   990  C  CB   . ARG   B 1 53  ? -36.268 -2.141 -24.005 1.00 23.74 ? 21  ARG   B CB   1 
ATOM   991  C  CG   . ARG   B 1 53  ? -37.454 -1.508 -23.277 1.00 31.05 ? 21  ARG   B CG   1 
ATOM   992  C  CD   . ARG   B 1 53  ? -37.606 -0.039 -23.618 1.00 38.52 ? 21  ARG   B CD   1 
ATOM   993  N  NE   . ARG   B 1 53  ? -38.712 0.240  -24.524 1.00 46.07 ? 21  ARG   B NE   1 
ATOM   994  C  CZ   . ARG   B 1 53  ? -38.594 0.346  -25.842 1.00 50.90 ? 21  ARG   B CZ   1 
ATOM   995  N  NH1  . ARG   B 1 53  ? -37.412 0.184  -26.420 1.00 52.55 ? 21  ARG   B NH1  1 
ATOM   996  N  NH2  . ARG   B 1 53  ? -39.661 0.613  -26.581 1.00 52.33 ? 21  ARG   B NH2  1 
ATOM   997  N  N    . GLY   B 1 54  ? -33.248 -3.779 -23.860 1.00 15.00 ? 22  GLY   B N    1 
ATOM   998  C  CA   . GLY   B 1 54  ? -32.278 -4.495 -24.671 1.00 15.71 ? 22  GLY   B CA   1 
ATOM   999  C  C    . GLY   B 1 54  ? -32.332 -4.033 -26.109 1.00 15.49 ? 22  GLY   B C    1 
ATOM   1000 O  O    . GLY   B 1 54  ? -32.421 -4.842 -27.041 1.00 16.72 ? 22  GLY   B O    1 
ATOM   1001 N  N    . SER   B 1 55  ? -32.246 -2.725 -26.302 1.00 15.75 ? 23  SER   B N    1 
ATOM   1002 C  CA   . SER   B 1 55  ? -32.489 -2.142 -27.610 1.00 16.42 ? 23  SER   B CA   1 
ATOM   1003 C  C    . SER   B 1 55  ? -31.693 -0.855 -27.713 1.00 14.74 ? 23  SER   B C    1 
ATOM   1004 O  O    . SER   B 1 55  ? -31.274 -0.294 -26.696 1.00 16.09 ? 23  SER   B O    1 
ATOM   1005 C  CB   . SER   B 1 55  ? -33.974 -1.809 -27.769 1.00 18.85 ? 23  SER   B CB   1 
ATOM   1006 O  OG   . SER   B 1 55  ? -34.346 -0.806 -26.849 1.00 22.34 ? 23  SER   B OG   1 
ATOM   1007 N  N    . PRO   B 1 56  ? -31.488 -0.348 -28.926 1.00 15.66 ? 24  PRO   B N    1 
ATOM   1008 C  CA   . PRO   B 1 56  ? -31.044 1.044  -29.045 1.00 15.55 ? 24  PRO   B CA   1 
ATOM   1009 C  C    . PRO   B 1 56  ? -32.055 1.957  -28.371 1.00 14.91 ? 24  PRO   B C    1 
ATOM   1010 O  O    . PRO   B 1 56  ? -33.253 1.659  -28.318 1.00 16.42 ? 24  PRO   B O    1 
ATOM   1011 C  CB   . PRO   B 1 56  ? -31.014 1.284  -30.561 1.00 17.25 ? 24  PRO   B CB   1 
ATOM   1012 C  CG   . PRO   B 1 56  ? -31.881 0.221  -31.145 1.00 21.41 ? 24  PRO   B CG   1 
ATOM   1013 C  CD   . PRO   B 1 56  ? -31.768 -0.961 -30.235 1.00 18.02 ? 24  PRO   B CD   1 
ATOM   1014 N  N    . ALA   B 1 57  ? -31.565 3.079  -27.840 1.00 15.73 ? 25  ALA   B N    1 
ATOM   1015 C  CA   . ALA   B 1 57  ? -32.452 4.103  -27.300 1.00 16.19 ? 25  ALA   B CA   1 
ATOM   1016 C  C    . ALA   B 1 57  ? -32.741 5.086  -28.429 1.00 15.85 ? 25  ALA   B C    1 
ATOM   1017 O  O    . ALA   B 1 57  ? -31.867 5.861  -28.822 1.00 16.65 ? 25  ALA   B O    1 
ATOM   1018 C  CB   . ALA   B 1 57  ? -31.815 4.795  -26.098 1.00 15.88 ? 25  ALA   B CB   1 
ATOM   1019 N  N    . ILE   B 1 58  ? -33.961 5.039  -28.956 1.00 15.16 ? 26  ILE   B N    1 
ATOM   1020 C  CA   . ILE   B 1 58  ? -34.346 5.763  -30.163 1.00 17.51 ? 26  ILE   B CA   1 
ATOM   1021 C  C    . ILE   B 1 58  ? -34.997 7.080  -29.772 1.00 18.24 ? 26  ILE   B C    1 
ATOM   1022 O  O    . ILE   B 1 58  ? -35.698 7.171  -28.759 1.00 19.76 ? 26  ILE   B O    1 
ATOM   1023 C  CB   . ILE   B 1 58  ? -35.299 4.893  -31.012 1.00 21.37 ? 26  ILE   B CB   1 
ATOM   1024 C  CG1  . ILE   B 1 58  ? -34.615 3.570  -31.371 1.00 23.68 ? 26  ILE   B CG1  1 
ATOM   1025 C  CG2  . ILE   B 1 58  ? -35.741 5.624  -32.264 1.00 24.94 ? 26  ILE   B CG2  1 
ATOM   1026 C  CD1  . ILE   B 1 58  ? -35.548 2.527  -31.960 1.00 28.01 ? 26  ILE   B CD1  1 
ATOM   1027 N  N    . ASN   B 1 59  ? -34.768 8.113  -30.584 1.00 18.30 ? 27  ASN   B N    1 
ATOM   1028 C  CA   . ASN   B 1 59  ? -35.407 9.412  -30.380 1.00 19.91 ? 27  ASN   B CA   1 
ATOM   1029 C  C    . ASN   B 1 59  ? -34.985 10.066 -29.072 1.00 20.15 ? 27  ASN   B C    1 
ATOM   1030 O  O    . ASN   B 1 59  ? -35.762 10.795 -28.451 1.00 21.69 ? 27  ASN   B O    1 
ATOM   1031 C  CB   . ASN   B 1 59  ? -36.931 9.321  -30.473 1.00 22.72 ? 27  ASN   B CB   1 
ATOM   1032 C  CG   . ASN   B 1 59  ? -37.402 8.966  -31.858 1.00 30.46 ? 27  ASN   B CG   1 
ATOM   1033 O  OD1  . ASN   B 1 59  ? -36.864 9.455  -32.852 1.00 34.05 ? 27  ASN   B OD1  1 
ATOM   1034 N  ND2  . ASN   B 1 59  ? -38.408 8.102  -31.938 1.00 33.19 ? 27  ASN   B ND2  1 
ATOM   1035 N  N    . VAL   B 1 60  ? -33.754 9.822  -28.647 1.00 16.36 ? 28  VAL   B N    1 
ATOM   1036 C  CA   . VAL   B 1 60  ? -33.198 10.476 -27.468 1.00 16.29 ? 28  VAL   B CA   1 
ATOM   1037 C  C    . VAL   B 1 60  ? -32.614 11.807 -27.914 1.00 16.33 ? 28  VAL   B C    1 
ATOM   1038 O  O    . VAL   B 1 60  ? -31.721 11.846 -28.766 1.00 16.55 ? 28  VAL   B O    1 
ATOM   1039 C  CB   . VAL   B 1 60  ? -32.123 9.607  -26.801 1.00 16.51 ? 28  VAL   B CB   1 
ATOM   1040 C  CG1  . VAL   B 1 60  ? -31.559 10.327 -25.596 1.00 17.91 ? 28  VAL   B CG1  1 
ATOM   1041 C  CG2  . VAL   B 1 60  ? -32.706 8.289  -26.366 1.00 17.75 ? 28  VAL   B CG2  1 
ATOM   1042 N  N    . ALA   B 1 61  ? -33.110 12.891 -27.334 1.00 15.89 ? 29  ALA   B N    1 
ATOM   1043 C  CA   . ALA   B 1 61  ? -32.661 14.232 -27.673 1.00 15.33 ? 29  ALA   B CA   1 
ATOM   1044 C  C    . ALA   B 1 61  ? -31.434 14.603 -26.851 1.00 13.79 ? 29  ALA   B C    1 
ATOM   1045 O  O    . ALA   B 1 61  ? -31.291 14.195 -25.696 1.00 16.40 ? 29  ALA   B O    1 
ATOM   1046 C  CB   . ALA   B 1 61  ? -33.777 15.231 -27.378 1.00 16.61 ? 29  ALA   B CB   1 
ATOM   1047 N  N    . MET   B 1 62  ? -30.538 15.376 -27.459 1.00 13.71 ? 30  MET   B N    1 
ATOM   1048 C  CA   . MET   B 1 62  ? -29.375 15.873 -26.739 1.00 13.93 ? 30  MET   B CA   1 
ATOM   1049 C  C    . MET   B 1 62  ? -28.900 17.178 -27.361 1.00 13.88 ? 30  MET   B C    1 
ATOM   1050 O  O    . MET   B 1 62  ? -29.084 17.420 -28.556 1.00 14.12 ? 30  MET   B O    1 
ATOM   1051 C  CB   . MET   B 1 62  ? -28.228 14.856 -26.715 1.00 14.51 ? 30  MET   B CB   1 
ATOM   1052 C  CG   . MET   B 1 62  ? -27.583 14.608 -28.078 1.00 15.04 ? 30  MET   B CG   1 
ATOM   1053 S  SD   . MET   B 1 62  ? -26.565 13.104 -28.053 1.00 16.39 ? 30  MET   B SD   1 
ATOM   1054 C  CE   . MET   B 1 62  ? -27.847 11.855 -28.151 1.00 18.03 ? 30  MET   B CE   1 
ATOM   1055 N  N    . HIS   B 1 63  ? -28.287 18.012 -26.529 1.00 14.35 ? 31  HIS   B N    1 
ATOM   1056 C  CA   . HIS   B 1 63  ? -27.588 19.207 -26.976 1.00 15.33 ? 31  HIS   B CA   1 
ATOM   1057 C  C    . HIS   B 1 63  ? -26.118 19.082 -26.606 1.00 15.47 ? 31  HIS   B C    1 
ATOM   1058 O  O    . HIS   B 1 63  ? -25.770 18.467 -25.595 1.00 16.65 ? 31  HIS   B O    1 
ATOM   1059 C  CB   . HIS   B 1 63  ? -28.135 20.477 -26.307 1.00 17.59 ? 31  HIS   B CB   1 
ATOM   1060 C  CG   . HIS   B 1 63  ? -29.510 20.868 -26.754 1.00 18.64 ? 31  HIS   B CG   1 
ATOM   1061 N  ND1  . HIS   B 1 63  ? -29.801 21.239 -28.048 1.00 24.20 ? 31  HIS   B ND1  1 
ATOM   1062 C  CD2  . HIS   B 1 63  ? -30.667 20.991 -26.060 1.00 21.39 ? 31  HIS   B CD2  1 
ATOM   1063 C  CE1  . HIS   B 1 63  ? -31.083 21.548 -28.139 1.00 23.73 ? 31  HIS   B CE1  1 
ATOM   1064 N  NE2  . HIS   B 1 63  ? -31.632 21.396 -26.948 1.00 22.72 ? 31  HIS   B NE2  1 
ATOM   1065 N  N    . VAL   B 1 64  ? -25.260 19.666 -27.438 1.00 14.83 ? 32  VAL   B N    1 
ATOM   1066 C  CA   . VAL   B 1 64  ? -23.825 19.734 -27.192 1.00 14.75 ? 32  VAL   B CA   1 
ATOM   1067 C  C    . VAL   B 1 64  ? -23.456 21.195 -27.004 1.00 14.37 ? 32  VAL   B C    1 
ATOM   1068 O  O    . VAL   B 1 64  ? -23.880 22.055 -27.788 1.00 16.14 ? 32  VAL   B O    1 
ATOM   1069 C  CB   . VAL   B 1 64  ? -23.018 19.102 -28.340 1.00 14.42 ? 32  VAL   B CB   1 
ATOM   1070 C  CG1  . VAL   B 1 64  ? -21.536 19.037 -27.967 1.00 15.83 ? 32  VAL   B CG1  1 
ATOM   1071 C  CG2  . VAL   B 1 64  ? -23.547 17.712 -28.661 1.00 17.39 ? 32  VAL   B CG2  1 
ATOM   1072 N  N    . PHE   B 1 65  ? -22.689 21.477 -25.957 1.00 14.77 ? 33  PHE   B N    1 
ATOM   1073 C  CA   . PHE   B 1 65  ? -22.222 22.822 -25.665 1.00 16.02 ? 33  PHE   B CA   1 
ATOM   1074 C  C    . PHE   B 1 65  ? -20.703 22.821 -25.617 1.00 16.15 ? 33  PHE   B C    1 
ATOM   1075 O  O    . PHE   B 1 65  ? -20.067 21.782 -25.404 1.00 15.75 ? 33  PHE   B O    1 
ATOM   1076 C  CB   . PHE   B 1 65  ? -22.764 23.329 -24.317 1.00 17.72 ? 33  PHE   B CB   1 
ATOM   1077 C  CG   . PHE   B 1 65  ? -24.261 23.265 -24.200 1.00 18.19 ? 33  PHE   B CG   1 
ATOM   1078 C  CD1  . PHE   B 1 65  ? -24.894 22.092 -23.809 1.00 19.48 ? 33  PHE   B CD1  1 
ATOM   1079 C  CD2  . PHE   B 1 65  ? -25.040 24.377 -24.490 1.00 19.82 ? 33  PHE   B CD2  1 
ATOM   1080 C  CE1  . PHE   B 1 65  ? -26.279 22.032 -23.707 1.00 19.64 ? 33  PHE   B CE1  1 
ATOM   1081 C  CE2  . PHE   B 1 65  ? -26.419 24.316 -24.391 1.00 21.00 ? 33  PHE   B CE2  1 
ATOM   1082 C  CZ   . PHE   B 1 65  ? -27.038 23.151 -24.000 1.00 20.39 ? 33  PHE   B CZ   1 
ATOM   1083 N  N    . ARG   B 1 66  ? -20.127 24.009 -25.797 1.00 17.66 ? 34  ARG   B N    1 
ATOM   1084 C  CA   . ARG   B 1 66  ? -18.691 24.198 -25.692 1.00 17.42 ? 34  ARG   B CA   1 
ATOM   1085 C  C    . ARG   B 1 66  ? -18.440 25.328 -24.706 1.00 18.89 ? 34  ARG   B C    1 
ATOM   1086 O  O    . ARG   B 1 66  ? -19.092 26.374 -24.783 1.00 20.47 ? 34  ARG   B O    1 
ATOM   1087 C  CB   . ARG   B 1 66  ? -18.092 24.536 -27.057 1.00 18.45 ? 34  ARG   B CB   1 
ATOM   1088 C  CG   . ARG   B 1 66  ? -16.596 24.767 -27.032 1.00 21.88 ? 34  ARG   B CG   1 
ATOM   1089 C  CD   . ARG   B 1 66  ? -16.071 25.194 -28.387 1.00 26.17 ? 34  ARG   B CD   1 
ATOM   1090 N  NE   . ARG   B 1 66  ? -14.627 25.395 -28.343 1.00 30.20 ? 34  ARG   B NE   1 
ATOM   1091 C  CZ   . ARG   B 1 66  ? -14.039 26.468 -27.824 1.00 33.22 ? 34  ARG   B CZ   1 
ATOM   1092 N  NH1  . ARG   B 1 66  ? -14.774 27.445 -27.303 1.00 34.62 ? 34  ARG   B NH1  1 
ATOM   1093 N  NH2  . ARG   B 1 66  ? -12.718 26.566 -27.825 1.00 34.90 ? 34  ARG   B NH2  1 
ATOM   1094 N  N    . LYS   B 1 67  ? -17.506 25.117 -23.783 1.00 19.97 ? 35  LYS   B N    1 
ATOM   1095 C  CA   . LYS   B 1 67  ? -17.271 26.094 -22.726 1.00 21.79 ? 35  LYS   B CA   1 
ATOM   1096 C  C    . LYS   B 1 67  ? -16.640 27.362 -23.294 1.00 23.12 ? 35  LYS   B C    1 
ATOM   1097 O  O    . LYS   B 1 67  ? -15.639 27.308 -24.021 1.00 23.67 ? 35  LYS   B O    1 
ATOM   1098 C  CB   . LYS   B 1 67  ? -16.384 25.488 -21.638 1.00 24.62 ? 35  LYS   B CB   1 
ATOM   1099 C  CG   . LYS   B 1 67  ? -16.572 26.104 -20.255 1.00 30.67 ? 35  LYS   B CG   1 
ATOM   1100 C  CD   . LYS   B 1 67  ? -15.862 25.270 -19.194 1.00 34.69 ? 35  LYS   B CD   1 
ATOM   1101 C  CE   . LYS   B 1 67  ? -16.289 25.648 -17.788 1.00 38.83 ? 35  LYS   B CE   1 
ATOM   1102 N  NZ   . LYS   B 1 67  ? -15.689 24.721 -16.787 1.00 40.41 ? 35  LYS   B NZ   1 
ATOM   1103 N  N    . ALA   B 1 68  ? -17.235 28.506 -22.968 1.00 24.81 ? 36  ALA   B N    1 
ATOM   1104 C  CA   . ALA   B 1 68  ? -16.751 29.791 -23.444 1.00 27.85 ? 36  ALA   B CA   1 
ATOM   1105 C  C    . ALA   B 1 68  ? -15.700 30.355 -22.492 1.00 31.10 ? 36  ALA   B C    1 
ATOM   1106 O  O    . ALA   B 1 68  ? -15.481 29.846 -21.391 1.00 30.82 ? 36  ALA   B O    1 
ATOM   1107 C  CB   . ALA   B 1 68  ? -17.906 30.782 -23.588 1.00 29.24 ? 36  ALA   B CB   1 
ATOM   1108 N  N    . ALA   B 1 69  ? -15.059 31.443 -22.933 1.00 34.89 ? 37  ALA   B N    1 
ATOM   1109 C  CA   . ALA   B 1 69  ? -13.983 32.053 -22.156 1.00 39.24 ? 37  ALA   B CA   1 
ATOM   1110 C  C    . ALA   B 1 69  ? -14.459 32.527 -20.787 1.00 41.46 ? 37  ALA   B C    1 
ATOM   1111 O  O    . ALA   B 1 69  ? -13.666 32.576 -19.840 1.00 42.96 ? 37  ALA   B O    1 
ATOM   1112 C  CB   . ALA   B 1 69  ? -13.357 33.208 -22.939 1.00 40.13 ? 37  ALA   B CB   1 
ATOM   1113 N  N    . ASP   B 1 70  ? -15.739 32.877 -20.658 1.00 42.03 ? 38  ASP   B N    1 
ATOM   1114 C  CA   . ASP   B 1 70  ? -16.302 33.310 -19.386 1.00 44.23 ? 38  ASP   B CA   1 
ATOM   1115 C  C    . ASP   B 1 70  ? -16.887 32.159 -18.569 1.00 44.58 ? 38  ASP   B C    1 
ATOM   1116 O  O    . ASP   B 1 70  ? -17.666 32.404 -17.639 1.00 44.43 ? 38  ASP   B O    1 
ATOM   1117 C  CB   . ASP   B 1 70  ? -17.348 34.408 -19.604 1.00 45.77 ? 38  ASP   B CB   1 
ATOM   1118 C  CG   . ASP   B 1 70  ? -18.488 33.963 -20.502 1.00 46.76 ? 38  ASP   B CG   1 
ATOM   1119 O  OD1  . ASP   B 1 70  ? -18.513 32.779 -20.901 1.00 46.20 ? 38  ASP   B OD1  1 
ATOM   1120 O  OD2  . ASP   B 1 70  ? -19.361 34.798 -20.814 1.00 47.92 ? 38  ASP   B OD2  1 
ATOM   1121 N  N    . ASP   B 1 71  ? -16.537 30.916 -18.901 1.00 44.91 ? 39  ASP   B N    1 
ATOM   1122 C  CA   . ASP   B 1 71  ? -16.998 29.703 -18.228 1.00 46.07 ? 39  ASP   B CA   1 
ATOM   1123 C  C    . ASP   B 1 71  ? -18.478 29.401 -18.436 1.00 42.43 ? 39  ASP   B C    1 
ATOM   1124 O  O    . ASP   B 1 71  ? -19.014 28.502 -17.774 1.00 43.03 ? 39  ASP   B O    1 
ATOM   1125 C  CB   . ASP   B 1 71  ? -16.631 29.650 -16.738 1.00 50.56 ? 39  ASP   B CB   1 
ATOM   1126 C  CG   . ASP   B 1 71  ? -15.182 29.266 -16.508 1.00 54.92 ? 39  ASP   B CG   1 
ATOM   1127 O  OD1  . ASP   B 1 71  ? -14.468 29.002 -17.498 1.00 56.05 ? 39  ASP   B OD1  1 
ATOM   1128 O  OD2  . ASP   B 1 71  ? -14.758 29.225 -15.333 1.00 56.86 ? 39  ASP   B OD2  1 
ATOM   1129 N  N    . THR   B 1 72  ? -19.156 30.107 -19.334 1.00 37.95 ? 40  THR   B N    1 
ATOM   1130 C  CA   . THR   B 1 72  ? -20.517 29.737 -19.688 1.00 35.75 ? 40  THR   B CA   1 
ATOM   1131 C  C    . THR   B 1 72  ? -20.499 28.700 -20.810 1.00 31.27 ? 40  THR   B C    1 
ATOM   1132 O  O    . THR   B 1 72  ? -19.501 28.515 -21.506 1.00 30.13 ? 40  THR   B O    1 
ATOM   1133 C  CB   . THR   B 1 72  ? -21.323 30.959 -20.121 1.00 38.08 ? 40  THR   B CB   1 
ATOM   1134 O  OG1  . THR   B 1 72  ? -20.747 31.513 -21.309 1.00 39.24 ? 40  THR   B OG1  1 
ATOM   1135 C  CG2  . THR   B 1 72  ? -21.338 32.017 -19.017 1.00 38.60 ? 40  THR   B CG2  1 
ATOM   1136 N  N    . TRP   B 1 73  ? -21.635 28.037 -20.998 1.00 29.04 ? 41  TRP   B N    1 
ATOM   1137 C  CA   . TRP   B 1 73  ? -21.764 26.959 -21.972 1.00 26.51 ? 41  TRP   B CA   1 
ATOM   1138 C  C    . TRP   B 1 73  ? -22.419 27.491 -23.242 1.00 28.92 ? 41  TRP   B C    1 
ATOM   1139 O  O    . TRP   B 1 73  ? -23.616 27.800 -23.247 1.00 31.88 ? 41  TRP   B O    1 
ATOM   1140 C  CB   . TRP   B 1 73  ? -22.593 25.824 -21.382 1.00 26.14 ? 41  TRP   B CB   1 
ATOM   1141 C  CG   . TRP   B 1 73  ? -21.887 25.073 -20.320 1.00 26.18 ? 41  TRP   B CG   1 
ATOM   1142 C  CD1  . TRP   B 1 73  ? -22.153 25.098 -18.982 1.00 28.28 ? 41  TRP   B CD1  1 
ATOM   1143 C  CD2  . TRP   B 1 73  ? -20.789 24.175 -20.498 1.00 22.94 ? 41  TRP   B CD2  1 
ATOM   1144 N  NE1  . TRP   B 1 73  ? -21.286 24.266 -18.314 1.00 27.91 ? 41  TRP   B NE1  1 
ATOM   1145 C  CE2  . TRP   B 1 73  ? -20.440 23.684 -19.223 1.00 24.95 ? 41  TRP   B CE2  1 
ATOM   1146 C  CE3  . TRP   B 1 73  ? -20.063 23.740 -21.613 1.00 21.33 ? 41  TRP   B CE3  1 
ATOM   1147 C  CZ2  . TRP   B 1 73  ? -19.395 22.775 -19.032 1.00 25.47 ? 41  TRP   B CZ2  1 
ATOM   1148 C  CZ3  . TRP   B 1 73  ? -19.029 22.832 -21.423 1.00 22.18 ? 41  TRP   B CZ3  1 
ATOM   1149 C  CH2  . TRP   B 1 73  ? -18.704 22.363 -20.141 1.00 23.60 ? 41  TRP   B CH2  1 
ATOM   1150 N  N    . GLU   B 1 74  ? -21.633 27.579 -24.327 1.00 26.00 ? 42  GLU   B N    1 
ATOM   1151 C  CA   . GLU   B 1 74  ? -22.118 28.065 -25.615 1.00 27.35 ? 42  GLU   B CA   1 
ATOM   1152 C  C    . GLU   B 1 74  ? -22.742 26.920 -26.410 1.00 22.43 ? 42  GLU   B C    1 
ATOM   1153 O  O    . GLU   B 1 74  ? -22.161 25.836 -26.489 1.00 21.59 ? 42  GLU   B O    1 
ATOM   1154 C  CB   . GLU   B 1 74  ? -20.957 28.632 -26.428 1.00 34.21 ? 42  GLU   B CB   1 
ATOM   1155 C  CG   . GLU   B 1 74  ? -20.322 29.878 -25.845 1.00 43.15 ? 42  GLU   B CG   1 
ATOM   1156 C  CD   . GLU   B 1 74  ? -21.143 31.129 -26.078 1.00 50.50 ? 42  GLU   B CD   1 
ATOM   1157 O  OE1  . GLU   B 1 74  ? -22.109 31.072 -26.870 1.00 53.16 ? 42  GLU   B OE1  1 
ATOM   1158 O  OE2  . GLU   B 1 74  ? -20.816 32.173 -25.471 1.00 53.12 ? 42  GLU   B OE2  1 
ATOM   1159 N  N    . PRO   B 1 75  ? -23.906 27.141 -27.022 1.00 20.54 ? 43  PRO   B N    1 
ATOM   1160 C  CA   . PRO   B 1 75  ? -24.487 26.116 -27.903 1.00 19.89 ? 43  PRO   B CA   1 
ATOM   1161 C  C    . PRO   B 1 75  ? -23.518 25.720 -29.008 1.00 18.86 ? 43  PRO   B C    1 
ATOM   1162 O  O    . PRO   B 1 75  ? -22.830 26.564 -29.591 1.00 20.59 ? 43  PRO   B O    1 
ATOM   1163 C  CB   . PRO   B 1 75  ? -25.729 26.808 -28.476 1.00 21.56 ? 43  PRO   B CB   1 
ATOM   1164 C  CG   . PRO   B 1 75  ? -26.050 27.886 -27.492 1.00 24.71 ? 43  PRO   B CG   1 
ATOM   1165 C  CD   . PRO   B 1 75  ? -24.740 28.354 -26.946 1.00 22.74 ? 43  PRO   B CD   1 
ATOM   1166 N  N    . PHE   B 1 76  ? -23.428 24.413 -29.255 1.00 17.16 ? 44  PHE   B N    1 
ATOM   1167 C  CA   . PHE   B 1 76  ? -22.501 23.920 -30.269 1.00 16.15 ? 44  PHE   B CA   1 
ATOM   1168 C  C    . PHE   B 1 76  ? -23.137 22.996 -31.302 1.00 15.91 ? 44  PHE   B C    1 
ATOM   1169 O  O    . PHE   B 1 76  ? -22.877 23.154 -32.500 1.00 17.91 ? 44  PHE   B O    1 
ATOM   1170 C  CB   . PHE   B 1 76  ? -21.296 23.239 -29.588 1.00 17.00 ? 44  PHE   B CB   1 
ATOM   1171 C  CG   . PHE   B 1 76  ? -20.269 22.737 -30.550 1.00 16.16 ? 44  PHE   B CG   1 
ATOM   1172 C  CD1  . PHE   B 1 76  ? -19.385 23.617 -31.168 1.00 18.58 ? 44  PHE   B CD1  1 
ATOM   1173 C  CD2  . PHE   B 1 76  ? -20.197 21.389 -30.856 1.00 17.10 ? 44  PHE   B CD2  1 
ATOM   1174 C  CE1  . PHE   B 1 76  ? -18.433 23.150 -32.069 1.00 19.03 ? 44  PHE   B CE1  1 
ATOM   1175 C  CE2  . PHE   B 1 76  ? -19.255 20.914 -31.752 1.00 18.46 ? 44  PHE   B CE2  1 
ATOM   1176 C  CZ   . PHE   B 1 76  ? -18.375 21.797 -32.367 1.00 20.20 ? 44  PHE   B CZ   1 
ATOM   1177 N  N    . ALA   B 1 77  ? -23.972 22.051 -30.879 1.00 14.35 ? 45  ALA   B N    1 
ATOM   1178 C  CA   . ALA   B 1 77  ? -24.598 21.102 -31.796 1.00 14.77 ? 45  ALA   B CA   1 
ATOM   1179 C  C    . ALA   B 1 77  ? -25.781 20.471 -31.078 1.00 15.38 ? 45  ALA   B C    1 
ATOM   1180 O  O    . ALA   B 1 77  ? -25.962 20.659 -29.874 1.00 17.09 ? 45  ALA   B O    1 
ATOM   1181 C  CB   . ALA   B 1 77  ? -23.602 20.024 -32.255 1.00 16.65 ? 45  ALA   B CB   1 
ATOM   1182 N  N    . SER   B 1 78  ? -26.595 19.728 -31.826 1.00 15.36 ? 46  SER   B N    1 
ATOM   1183 C  CA   . SER   B 1 78  ? -27.674 18.984 -31.176 1.00 15.59 ? 46  SER   B CA   1 
ATOM   1184 C  C    . SER   B 1 78  ? -28.296 18.009 -32.166 1.00 14.93 ? 46  SER   B C    1 
ATOM   1185 O  O    . SER   B 1 78  ? -27.969 18.014 -33.356 1.00 17.09 ? 46  SER   B O    1 
ATOM   1186 C  CB   . SER   B 1 78  ? -28.744 19.901 -30.597 1.00 23.72 ? 46  SER   B CB   1 
ATOM   1187 O  OG   . SER   B 1 78  ? -29.521 20.433 -31.626 1.00 25.73 ? 46  SER   B OG   1 
ATOM   1188 N  N    . GLY   B 1 79  ? -29.201 17.177 -31.653 1.00 15.16 ? 47  GLY   B N    1 
ATOM   1189 C  CA   . GLY   B 1 79  ? -29.928 16.236 -32.482 1.00 15.76 ? 47  GLY   B CA   1 
ATOM   1190 C  C    . GLY   B 1 79  ? -30.631 15.194 -31.631 1.00 15.16 ? 47  GLY   B C    1 
ATOM   1191 O  O    . GLY   B 1 79  ? -30.648 15.279 -30.400 1.00 16.64 ? 47  GLY   B O    1 
ATOM   1192 N  N    . LYS   B 1 80  ? -31.223 14.212 -32.316 1.00 15.62 ? 48  LYS   B N    1 
ATOM   1193 C  CA   . LYS   B 1 80  ? -31.901 13.085 -31.683 1.00 17.80 ? 48  LYS   B CA   1 
ATOM   1194 C  C    . LYS   B 1 80  ? -31.329 11.790 -32.240 1.00 17.09 ? 48  LYS   B C    1 
ATOM   1195 O  O    . LYS   B 1 80  ? -30.980 11.717 -33.419 1.00 18.33 ? 48  LYS   B O    1 
ATOM   1196 C  CB   . LYS   B 1 80  ? -33.393 13.053 -32.042 1.00 23.84 ? 48  LYS   B CB   1 
ATOM   1197 C  CG   . LYS   B 1 80  ? -34.289 14.012 -31.311 1.00 31.83 ? 48  LYS   B CG   1 
ATOM   1198 C  CD   . LYS   B 1 80  ? -35.752 13.622 -31.556 1.00 36.19 ? 48  LYS   B CD   1 
ATOM   1199 C  CE   . LYS   B 1 80  ? -36.001 13.268 -33.021 1.00 38.50 ? 48  LYS   B CE   1 
ATOM   1200 N  NZ   . LYS   B 1 80  ? -37.429 12.932 -33.303 1.00 40.01 ? 48  LYS   B NZ   1 
ATOM   1201 N  N    . THR   B 1 81  ? -31.261 10.752 -31.405 1.00 15.60 ? 49  THR   B N    1 
ATOM   1202 C  CA   . THR   B 1 81  ? -30.768 9.471  -31.901 1.00 15.65 ? 49  THR   B CA   1 
ATOM   1203 C  C    . THR   B 1 81  ? -31.733 8.864  -32.915 1.00 15.93 ? 49  THR   B C    1 
ATOM   1204 O  O    . THR   B 1 81  ? -32.954 9.035  -32.837 1.00 16.41 ? 49  THR   B O    1 
ATOM   1205 C  CB   . THR   B 1 81  ? -30.546 8.466  -30.771 1.00 15.01 ? 49  THR   B CB   1 
ATOM   1206 O  OG1  . THR   B 1 81  ? -31.769 8.261  -30.048 1.00 15.42 ? 49  THR   B OG1  1 
ATOM   1207 C  CG2  . THR   B 1 81  ? -29.437 8.927  -29.830 1.00 16.49 ? 49  THR   B CG2  1 
ATOM   1208 N  N    . SER   B 1 82  ? -31.162 8.132  -33.864 1.00 17.38 ? 50  SER   B N    1 
ATOM   1209 C  CA   . SER   B 1 82  ? -31.905 7.454  -34.919 1.00 18.48 ? 50  SER   B CA   1 
ATOM   1210 C  C    . SER   B 1 82  ? -32.485 6.137  -34.402 1.00 18.51 ? 50  SER   B C    1 
ATOM   1211 O  O    . SER   B 1 82  ? -32.378 5.792  -33.220 1.00 17.76 ? 50  SER   B O    1 
ATOM   1212 C  CB   . SER   B 1 82  ? -30.962 7.156  -36.076 1.00 21.33 ? 50  SER   B CB   1 
ATOM   1213 O  OG   . SER   B 1 82  ? -30.015 6.187  -35.654 1.00 23.04 ? 50  SER   B OG   1 
ATOM   1214 N  N    . GLU   B 1 83  ? -33.079 5.359  -35.309 1.00 21.26 ? 51  GLU   B N    1 
ATOM   1215 C  CA   . GLU   B 1 83  ? -33.580 4.037  -34.941 1.00 24.56 ? 51  GLU   B CA   1 
ATOM   1216 C  C    . GLU   B 1 83  ? -32.465 3.080  -34.537 1.00 22.20 ? 51  GLU   B C    1 
ATOM   1217 O  O    . GLU   B 1 83  ? -32.746 2.041  -33.925 1.00 23.07 ? 51  GLU   B O    1 
ATOM   1218 C  CB   . GLU   B 1 83  ? -34.407 3.444  -36.084 1.00 31.50 ? 51  GLU   B CB   1 
ATOM   1219 C  CG   . GLU   B 1 83  ? -35.693 4.213  -36.349 1.00 40.10 ? 51  GLU   B CG   1 
ATOM   1220 C  CD   . GLU   B 1 83  ? -36.536 3.603  -37.454 1.00 48.06 ? 51  GLU   B CD   1 
ATOM   1221 O  OE1  . GLU   B 1 83  ? -36.028 2.724  -38.186 1.00 50.38 ? 51  GLU   B OE1  1 
ATOM   1222 O  OE2  . GLU   B 1 83  ? -37.711 4.007  -37.588 1.00 51.06 ? 51  GLU   B OE2  1 
ATOM   1223 N  N    . SER   B 1 84  ? -31.213 3.397  -34.867 1.00 20.93 ? 52  SER   B N    1 
ATOM   1224 C  CA   . SER   B 1 84  ? -30.080 2.608  -34.411 1.00 20.51 ? 52  SER   B CA   1 
ATOM   1225 C  C    . SER   B 1 84  ? -29.547 3.087  -33.071 1.00 17.68 ? 52  SER   B C    1 
ATOM   1226 O  O    . SER   B 1 84  ? -28.559 2.535  -32.580 1.00 19.42 ? 52  SER   B O    1 
ATOM   1227 C  CB   . SER   B 1 84  ? -28.950 2.643  -35.445 1.00 24.24 ? 52  SER   B CB   1 
ATOM   1228 O  OG   . SER   B 1 84  ? -28.397 3.945  -35.542 1.00 28.76 ? 52  SER   B OG   1 
ATOM   1229 N  N    . GLY   B 1 85  ? -30.175 4.097  -32.469 1.00 15.82 ? 53  GLY   B N    1 
ATOM   1230 C  CA   . GLY   B 1 85  ? -29.656 4.678  -31.252 1.00 15.23 ? 53  GLY   B CA   1 
ATOM   1231 C  C    . GLY   B 1 85  ? -28.457 5.578  -31.449 1.00 14.20 ? 53  GLY   B C    1 
ATOM   1232 O  O    . GLY   B 1 85  ? -27.799 5.930  -30.465 1.00 16.43 ? 53  GLY   B O    1 
ATOM   1233 N  N    . GLU   B 1 86  ? -28.153 5.975  -32.681 1.00 16.92 ? 54  GLU   B N    1 
ATOM   1234 C  CA   . GLU   B 1 86  ? -26.956 6.750  -32.970 1.00 16.67 ? 54  GLU   B CA   1 
ATOM   1235 C  C    . GLU   B 1 86  ? -27.309 8.142  -33.464 1.00 15.23 ? 54  GLU   B C    1 
ATOM   1236 O  O    . GLU   B 1 86  ? -28.336 8.352  -34.119 1.00 16.97 ? 54  GLU   B O    1 
ATOM   1237 C  CB   . GLU   B 1 86  ? -26.085 6.037  -34.007 1.00 19.80 ? 54  GLU   B CB   1 
ATOM   1238 C  CG   . GLU   B 1 86  ? -25.573 4.698  -33.470 1.00 24.71 ? 54  GLU   B CG   1 
ATOM   1239 C  CD   . GLU   B 1 86  ? -24.760 3.890  -34.461 1.00 30.64 ? 54  GLU   B CD   1 
ATOM   1240 O  OE1  . GLU   B 1 86  ? -24.503 4.377  -35.579 1.00 32.47 ? 54  GLU   B OE1  1 
ATOM   1241 O  OE2  . GLU   B 1 86  ? -24.382 2.751  -34.111 1.00 33.03 ? 54  GLU   B OE2  1 
ATOM   1242 N  N    . LEU   B 1 87  ? -26.439 9.096  -33.137 1.00 15.66 ? 55  LEU   B N    1 
ATOM   1243 C  CA   . LEU   B 1 87  ? -26.560 10.467 -33.616 1.00 15.77 ? 55  LEU   B CA   1 
ATOM   1244 C  C    . LEU   B 1 87  ? -25.255 10.837 -34.309 1.00 16.09 ? 55  LEU   B C    1 
ATOM   1245 O  O    . LEU   B 1 87  ? -24.222 11.003 -33.650 1.00 17.29 ? 55  LEU   B O    1 
ATOM   1246 C  CB   . LEU   B 1 87  ? -26.870 11.424 -32.465 1.00 15.48 ? 55  LEU   B CB   1 
ATOM   1247 C  CG   . LEU   B 1 87  ? -26.937 12.906 -32.835 1.00 16.51 ? 55  LEU   B CG   1 
ATOM   1248 C  CD1  . LEU   B 1 87  ? -27.817 13.128 -34.054 1.00 17.91 ? 55  LEU   B CD1  1 
ATOM   1249 C  CD2  . LEU   B 1 87  ? -27.447 13.701 -31.646 1.00 17.27 ? 55  LEU   B CD2  1 
ATOM   1250 N  N    . HIS   B 1 88  ? -25.304 10.927 -35.637 1.00 19.07 ? 56  HIS   B N    1 
ATOM   1251 C  CA   . HIS   B 1 88  ? -24.184 11.279 -36.494 1.00 22.12 ? 56  HIS   B CA   1 
ATOM   1252 C  C    . HIS   B 1 88  ? -24.369 12.705 -37.004 1.00 21.39 ? 56  HIS   B C    1 
ATOM   1253 O  O    . HIS   B 1 88  ? -25.447 13.293 -36.898 1.00 23.32 ? 56  HIS   B O    1 
ATOM   1254 C  CB   . HIS   B 1 88  ? -24.107 10.318 -37.691 1.00 25.57 ? 56  HIS   B CB   1 
ATOM   1255 C  CG   . HIS   B 1 88  ? -23.901 8.885  -37.313 1.00 28.25 ? 56  HIS   B CG   1 
ATOM   1256 N  ND1  . HIS   B 1 88  ? -22.676 8.260  -37.411 1.00 30.93 ? 56  HIS   B ND1  1 
ATOM   1257 C  CD2  . HIS   B 1 88  ? -24.763 7.950  -36.848 1.00 30.44 ? 56  HIS   B CD2  1 
ATOM   1258 C  CE1  . HIS   B 1 88  ? -22.791 7.004  -37.020 1.00 31.60 ? 56  HIS   B CE1  1 
ATOM   1259 N  NE2  . HIS   B 1 88  ? -24.047 6.790  -36.672 1.00 31.83 ? 56  HIS   B NE2  1 
ATOM   1260 N  N    . GLY   B 1 89  ? -23.300 13.267 -37.558 1.00 21.49 ? 57  GLY   B N    1 
ATOM   1261 C  CA   . GLY   B 1 89  ? -23.408 14.551 -38.227 1.00 21.65 ? 57  GLY   B CA   1 
ATOM   1262 C  C    . GLY   B 1 89  ? -23.506 15.759 -37.320 1.00 21.27 ? 57  GLY   B C    1 
ATOM   1263 O  O    . GLY   B 1 89  ? -23.979 16.813 -37.759 1.00 24.36 ? 57  GLY   B O    1 
ATOM   1264 N  N    . LEU   B 1 90  ? -23.047 15.643 -36.072 1.00 20.44 ? 58  LEU   B N    1 
ATOM   1265 C  CA   . LEU   B 1 90  ? -23.131 16.754 -35.128 1.00 18.82 ? 58  LEU   B CA   1 
ATOM   1266 C  C    . LEU   B 1 90  ? -22.226 17.912 -35.529 1.00 18.85 ? 58  LEU   B C    1 
ATOM   1267 O  O    . LEU   B 1 90  ? -22.578 19.079 -35.318 1.00 19.77 ? 58  LEU   B O    1 
ATOM   1268 C  CB   . LEU   B 1 90  ? -22.767 16.273 -33.726 1.00 18.09 ? 58  LEU   B CB   1 
ATOM   1269 C  CG   . LEU   B 1 90  ? -23.881 15.514 -33.006 1.00 18.65 ? 58  LEU   B CG   1 
ATOM   1270 C  CD1  . LEU   B 1 90  ? -23.320 14.726 -31.829 1.00 20.15 ? 58  LEU   B CD1  1 
ATOM   1271 C  CD2  . LEU   B 1 90  ? -24.958 16.501 -32.550 1.00 21.12 ? 58  LEU   B CD2  1 
ATOM   1272 N  N    . THR   B 1 91  ? -21.053 17.618 -36.080 1.00 18.07 ? 59  THR   B N    1 
ATOM   1273 C  CA   . THR   B 1 91  ? -20.081 18.660 -36.377 1.00 18.75 ? 59  THR   B CA   1 
ATOM   1274 C  C    . THR   B 1 91  ? -19.215 18.215 -37.551 1.00 20.03 ? 59  THR   B C    1 
ATOM   1275 O  O    . THR   B 1 91  ? -19.416 17.144 -38.130 1.00 22.15 ? 59  THR   B O    1 
ATOM   1276 C  CB   . THR   B 1 91  ? -19.272 19.005 -35.119 1.00 18.73 ? 59  THR   B CB   1 
ATOM   1277 O  OG1  . THR   B 1 91  ? -18.460 20.165 -35.354 1.00 19.90 ? 59  THR   B OG1  1 
ATOM   1278 C  CG2  . THR   B 1 91  ? -18.379 17.833 -34.705 1.00 19.38 ? 59  THR   B CG2  1 
ATOM   1279 N  N    . THR   B 1 92  ? -18.269 19.070 -37.928 1.00 20.43 ? 60  THR   B N    1 
ATOM   1280 C  CA   . THR   B 1 92  ? -17.278 18.758 -38.945 1.00 21.05 ? 60  THR   B CA   1 
ATOM   1281 C  C    . THR   B 1 92  ? -15.896 18.885 -38.326 1.00 20.92 ? 60  THR   B C    1 
ATOM   1282 O  O    . THR   B 1 92  ? -15.724 19.517 -37.282 1.00 20.88 ? 60  THR   B O    1 
ATOM   1283 C  CB   . THR   B 1 92  ? -17.362 19.717 -40.143 1.00 24.46 ? 60  THR   B CB   1 
ATOM   1284 O  OG1  . THR   B 1 92  ? -17.070 21.052 -39.707 1.00 25.97 ? 60  THR   B OG1  1 
ATOM   1285 C  CG2  . THR   B 1 92  ? -18.739 19.673 -40.779 1.00 26.68 ? 60  THR   B CG2  1 
ATOM   1286 N  N    . GLU   B 1 93  ? -14.898 18.302 -38.994 1.00 20.73 ? 61  GLU   B N    1 
ATOM   1287 C  CA   . GLU   B 1 93  ? -13.544 18.361 -38.455 1.00 21.91 ? 61  GLU   B CA   1 
ATOM   1288 C  C    . GLU   B 1 93  ? -13.084 19.802 -38.261 1.00 21.75 ? 61  GLU   B C    1 
ATOM   1289 O  O    . GLU   B 1 93  ? -12.484 20.133 -37.232 1.00 21.06 ? 61  GLU   B O    1 
ATOM   1290 C  CB   . GLU   B 1 93  ? -12.563 17.603 -39.349 1.00 28.45 ? 61  GLU   B CB   1 
ATOM   1291 C  CG   . GLU   B 1 93  ? -11.206 17.428 -38.694 1.00 35.51 ? 61  GLU   B CG   1 
ATOM   1292 C  CD   . GLU   B 1 93  ? -10.182 16.817 -39.621 1.00 42.76 ? 61  GLU   B CD   1 
ATOM   1293 O  OE1  . GLU   B 1 93  ? -9.321  17.563 -40.131 1.00 44.38 ? 61  GLU   B OE1  1 
ATOM   1294 O  OE2  . GLU   B 1 93  ? -10.241 15.591 -39.844 1.00 46.01 ? 61  GLU   B OE2  1 
ATOM   1295 N  N    . GLU   B 1 94  ? -13.374 20.682 -39.227 1.00 21.17 ? 62  GLU   B N    1 
ATOM   1296 C  CA   . GLU   B 1 94  ? -12.858 22.045 -39.137 1.00 23.87 ? 62  GLU   B CA   1 
ATOM   1297 C  C    . GLU   B 1 94  ? -13.542 22.849 -38.036 1.00 20.27 ? 62  GLU   B C    1 
ATOM   1298 O  O    . GLU   B 1 94  ? -12.918 23.736 -37.450 1.00 21.50 ? 62  GLU   B O    1 
ATOM   1299 C  CB   . GLU   B 1 94  ? -12.945 22.764 -40.491 1.00 30.55 ? 62  GLU   B CB   1 
ATOM   1300 C  CG   . GLU   B 1 94  ? -14.332 22.831 -41.092 1.00 37.33 ? 62  GLU   B CG   1 
ATOM   1301 C  CD   . GLU   B 1 94  ? -14.665 21.622 -41.960 1.00 44.34 ? 62  GLU   B CD   1 
ATOM   1302 O  OE1  . GLU   B 1 94  ? -15.596 21.731 -42.788 1.00 47.63 ? 62  GLU   B OE1  1 
ATOM   1303 O  OE2  . GLU   B 1 94  ? -13.998 20.570 -41.823 1.00 45.43 ? 62  GLU   B OE2  1 
ATOM   1304 N  N    . GLU   B 1 95  ? -14.810 22.557 -37.734 1.00 20.01 ? 63  GLU   B N    1 
ATOM   1305 C  CA   . GLU   B 1 95  ? -15.528 23.280 -36.689 1.00 21.48 ? 63  GLU   B CA   1 
ATOM   1306 C  C    . GLU   B 1 95  ? -15.213 22.764 -35.291 1.00 20.35 ? 63  GLU   B C    1 
ATOM   1307 O  O    . GLU   B 1 95  ? -15.399 23.494 -34.309 1.00 22.26 ? 63  GLU   B O    1 
ATOM   1308 C  CB   . GLU   B 1 95  ? -17.040 23.161 -36.924 1.00 26.01 ? 63  GLU   B CB   1 
ATOM   1309 C  CG   . GLU   B 1 95  ? -17.548 23.865 -38.172 1.00 31.93 ? 63  GLU   B CG   1 
ATOM   1310 C  CD   . GLU   B 1 95  ? -19.025 23.605 -38.424 1.00 38.06 ? 63  GLU   B CD   1 
ATOM   1311 O  OE1  . GLU   B 1 95  ? -19.412 22.425 -38.548 1.00 39.12 ? 63  GLU   B OE1  1 
ATOM   1312 O  OE2  . GLU   B 1 95  ? -19.803 24.579 -38.485 1.00 42.67 ? 63  GLU   B OE2  1 
ATOM   1313 N  N    . PHE   B 1 96  ? -14.747 21.529 -35.182 1.00 18.20 ? 64  PHE   B N    1 
ATOM   1314 C  CA   . PHE   B 1 96  ? -14.597 20.839 -33.904 1.00 17.04 ? 64  PHE   B CA   1 
ATOM   1315 C  C    . PHE   B 1 96  ? -13.147 21.009 -33.463 1.00 17.42 ? 64  PHE   B C    1 
ATOM   1316 O  O    . PHE   B 1 96  ? -12.290 20.178 -33.752 1.00 19.18 ? 64  PHE   B O    1 
ATOM   1317 C  CB   . PHE   B 1 96  ? -14.961 19.374 -34.107 1.00 18.72 ? 64  PHE   B CB   1 
ATOM   1318 C  CG   . PHE   B 1 96  ? -15.143 18.590 -32.841 1.00 18.51 ? 64  PHE   B CG   1 
ATOM   1319 C  CD1  . PHE   B 1 96  ? -15.682 19.163 -31.702 1.00 18.97 ? 64  PHE   B CD1  1 
ATOM   1320 C  CD2  . PHE   B 1 96  ? -14.802 17.249 -32.811 1.00 20.36 ? 64  PHE   B CD2  1 
ATOM   1321 C  CE1  . PHE   B 1 96  ? -15.856 18.411 -30.550 1.00 19.92 ? 64  PHE   B CE1  1 
ATOM   1322 C  CE2  . PHE   B 1 96  ? -14.974 16.494 -31.667 1.00 21.32 ? 64  PHE   B CE2  1 
ATOM   1323 C  CZ   . PHE   B 1 96  ? -15.499 17.070 -30.537 1.00 20.10 ? 64  PHE   B CZ   1 
ATOM   1324 N  N    . VAL   B 1 97  ? -12.879 22.089 -32.734 1.00 17.13 ? 65  VAL   B N    1 
ATOM   1325 C  CA   . VAL   B 1 97  ? -11.519 22.430 -32.330 1.00 18.83 ? 65  VAL   B CA   1 
ATOM   1326 C  C    . VAL   B 1 97  ? -11.387 22.224 -30.830 1.00 16.82 ? 65  VAL   B C    1 
ATOM   1327 O  O    . VAL   B 1 97  ? -12.310 21.720 -30.176 1.00 17.22 ? 65  VAL   B O    1 
ATOM   1328 C  CB   . VAL   B 1 97  ? -11.133 23.865 -32.722 1.00 23.21 ? 65  VAL   B CB   1 
ATOM   1329 C  CG1  . VAL   B 1 97  ? -11.146 24.030 -34.237 1.00 23.96 ? 65  VAL   B CG1  1 
ATOM   1330 C  CG2  . VAL   B 1 97  ? -12.063 24.849 -32.049 1.00 25.27 ? 65  VAL   B CG2  1 
ATOM   1331 N  N    . GLU   B 1 98  ? -10.211 22.539 -30.292 1.00 18.27 ? 66  GLU   B N    1 
ATOM   1332 C  CA   . GLU   B 1 98  ? -9.975  22.371 -28.866 1.00 20.23 ? 66  GLU   B CA   1 
ATOM   1333 C  C    . GLU   B 1 98  ? -11.044 23.086 -28.060 1.00 19.33 ? 66  GLU   B C    1 
ATOM   1334 O  O    . GLU   B 1 98  ? -11.482 24.189 -28.406 1.00 22.04 ? 66  GLU   B O    1 
ATOM   1335 C  CB   . GLU   B 1 98  ? -8.595  22.906 -28.483 1.00 21.87 ? 66  GLU   B CB   1 
ATOM   1336 C  CG   . GLU   B 1 98  ? -8.203  22.652 -27.027 1.00 27.26 ? 66  GLU   B CG   1 
ATOM   1337 C  CD   . GLU   B 1 98  ? -8.795  23.660 -26.050 1.00 35.39 ? 66  GLU   B CD   1 
ATOM   1338 O  OE1  . GLU   B 1 98  ? -9.099  24.799 -26.471 1.00 36.90 ? 66  GLU   B OE1  1 
ATOM   1339 O  OE2  . GLU   B 1 98  ? -8.970  23.304 -24.860 1.00 38.77 ? 66  GLU   B OE2  1 
ATOM   1340 N  N    . GLY   B 1 99  ? -11.476 22.431 -26.993 1.00 18.26 ? 67  GLY   B N    1 
ATOM   1341 C  CA   . GLY   B 1 99  ? -12.412 23.019 -26.067 1.00 17.47 ? 67  GLY   B CA   1 
ATOM   1342 C  C    . GLY   B 1 99  ? -12.840 21.978 -25.067 1.00 17.31 ? 67  GLY   B C    1 
ATOM   1343 O  O    . GLY   B 1 99  ? -12.502 20.795 -25.171 1.00 17.61 ? 67  GLY   B O    1 
ATOM   1344 N  N    . ILE   B 1 100 ? -13.571 22.443 -24.070 1.00 16.86 ? 68  ILE   B N    1 
ATOM   1345 C  CA   . ILE   B 1 100 ? -14.295 21.555 -23.176 1.00 16.10 ? 68  ILE   B CA   1 
ATOM   1346 C  C    . ILE   B 1 100 ? -15.721 21.485 -23.692 1.00 15.38 ? 68  ILE   B C    1 
ATOM   1347 O  O    . ILE   B 1 100 ? -16.381 22.521 -23.867 1.00 17.34 ? 68  ILE   B O    1 
ATOM   1348 C  CB   . ILE   B 1 100 ? -14.244 22.050 -21.725 1.00 17.40 ? 68  ILE   B CB   1 
ATOM   1349 C  CG1  . ILE   B 1 100 ? -12.790 22.110 -21.253 1.00 20.53 ? 68  ILE   B CG1  1 
ATOM   1350 C  CG2  . ILE   B 1 100 ? -15.084 21.138 -20.829 1.00 17.96 ? 68  ILE   B CG2  1 
ATOM   1351 C  CD1  . ILE   B 1 100 ? -12.622 22.638 -19.857 1.00 22.87 ? 68  ILE   B CD1  1 
ATOM   1352 N  N    . TYR   B 1 101 ? -16.188 20.269 -23.947 1.00 15.06 ? 69  TYR   B N    1 
ATOM   1353 C  CA   . TYR   B 1 101 ? -17.502 20.031 -24.517 1.00 14.17 ? 69  TYR   B CA   1 
ATOM   1354 C  C    . TYR   B 1 101 ? -18.381 19.303 -23.512 1.00 14.13 ? 69  TYR   B C    1 
ATOM   1355 O  O    . TYR   B 1 101 ? -17.896 18.506 -22.699 1.00 14.93 ? 69  TYR   B O    1 
ATOM   1356 C  CB   . TYR   B 1 101 ? -17.390 19.220 -25.813 1.00 14.48 ? 69  TYR   B CB   1 
ATOM   1357 C  CG   . TYR   B 1 101 ? -16.720 20.001 -26.925 1.00 13.59 ? 69  TYR   B CG   1 
ATOM   1358 C  CD1  . TYR   B 1 101 ? -15.334 20.045 -27.026 1.00 14.34 ? 69  TYR   B CD1  1 
ATOM   1359 C  CD2  . TYR   B 1 101 ? -17.475 20.722 -27.854 1.00 15.00 ? 69  TYR   B CD2  1 
ATOM   1360 C  CE1  . TYR   B 1 101 ? -14.712 20.783 -28.027 1.00 15.24 ? 69  TYR   B CE1  1 
ATOM   1361 C  CE2  . TYR   B 1 101 ? -16.867 21.450 -28.859 1.00 14.47 ? 69  TYR   B CE2  1 
ATOM   1362 C  CZ   . TYR   B 1 101 ? -15.491 21.474 -28.946 1.00 14.84 ? 69  TYR   B CZ   1 
ATOM   1363 O  OH   . TYR   B 1 101 ? -14.886 22.201 -29.942 1.00 17.63 ? 69  TYR   B OH   1 
ATOM   1364 N  N    . LYS   B 1 102 ? -19.677 19.600 -23.562 1.00 14.37 ? 70  LYS   B N    1 
ATOM   1365 C  CA   . LYS   B 1 102 ? -20.662 18.948 -22.712 1.00 15.24 ? 70  LYS   B CA   1 
ATOM   1366 C  C    . LYS   B 1 102 ? -21.757 18.405 -23.608 1.00 15.06 ? 70  LYS   B C    1 
ATOM   1367 O  O    . LYS   B 1 102 ? -22.368 19.165 -24.364 1.00 16.86 ? 70  LYS   B O    1 
ATOM   1368 C  CB   . LYS   B 1 102 ? -21.271 19.926 -21.699 1.00 18.09 ? 70  LYS   B CB   1 
ATOM   1369 C  CG   . LYS   B 1 102 ? -22.430 19.315 -20.895 1.00 19.72 ? 70  LYS   B CG   1 
ATOM   1370 C  CD   . LYS   B 1 102 ? -22.873 20.198 -19.734 1.00 22.96 ? 70  LYS   B CD   1 
ATOM   1371 C  CE   . LYS   B 1 102 ? -23.485 21.499 -20.213 1.00 26.63 ? 70  LYS   B CE   1 
ATOM   1372 N  NZ   . LYS   B 1 102 ? -24.203 22.197 -19.100 1.00 29.84 ? 70  LYS   B NZ   1 
ATOM   1373 N  N    . VAL   B 1 103 ? -21.969 17.094 -23.553 1.00 15.19 ? 71  VAL   B N    1 
ATOM   1374 C  CA   . VAL   B 1 103 ? -23.111 16.448 -24.187 1.00 15.92 ? 71  VAL   B CA   1 
ATOM   1375 C  C    . VAL   B 1 103 ? -24.164 16.234 -23.113 1.00 16.76 ? 71  VAL   B C    1 
ATOM   1376 O  O    . VAL   B 1 103 ? -23.937 15.488 -22.152 1.00 17.66 ? 71  VAL   B O    1 
ATOM   1377 C  CB   . VAL   B 1 103 ? -22.715 15.113 -24.835 1.00 16.92 ? 71  VAL   B CB   1 
ATOM   1378 C  CG1  . VAL   B 1 103 ? -23.933 14.479 -25.506 1.00 18.35 ? 71  VAL   B CG1  1 
ATOM   1379 C  CG2  . VAL   B 1 103 ? -21.578 15.328 -25.826 1.00 17.33 ? 71  VAL   B CG2  1 
ATOM   1380 N  N    . GLU   B 1 104 ? -25.310 16.887 -23.267 1.00 15.78 ? 72  GLU   B N    1 
ATOM   1381 C  CA   . GLU   B 1 104 ? -26.395 16.824 -22.294 1.00 16.04 ? 72  GLU   B CA   1 
ATOM   1382 C  C    . GLU   B 1 104 ? -27.524 16.016 -22.920 1.00 13.66 ? 72  GLU   B C    1 
ATOM   1383 O  O    . GLU   B 1 104 ? -28.205 16.498 -23.832 1.00 15.14 ? 72  GLU   B O    1 
ATOM   1384 C  CB   . GLU   B 1 104 ? -26.853 18.234 -21.949 1.00 20.32 ? 72  GLU   B CB   1 
ATOM   1385 C  CG   . GLU   B 1 104 ? -27.616 18.352 -20.679 1.00 25.24 ? 72  GLU   B CG   1 
ATOM   1386 C  CD   . GLU   B 1 104 ? -27.580 19.780 -20.160 1.00 28.77 ? 72  GLU   B CD   1 
ATOM   1387 O  OE1  . GLU   B 1 104 ? -26.710 20.097 -19.323 1.00 33.31 ? 72  GLU   B OE1  1 
ATOM   1388 O  OE2  . GLU   B 1 104 ? -28.392 20.599 -20.629 1.00 28.93 ? 72  GLU   B OE2  1 
ATOM   1389 N  N    . ILE   B 1 105 ? -27.719 14.795 -22.432 1.00 14.43 ? 73  ILE   B N    1 
ATOM   1390 C  CA   . ILE   B 1 105 ? -28.635 13.832 -23.036 1.00 14.37 ? 73  ILE   B CA   1 
ATOM   1391 C  C    . ILE   B 1 105 ? -29.927 13.830 -22.230 1.00 13.84 ? 73  ILE   B C    1 
ATOM   1392 O  O    . ILE   B 1 105 ? -29.907 13.577 -21.023 1.00 15.35 ? 73  ILE   B O    1 
ATOM   1393 C  CB   . ILE   B 1 105 ? -28.006 12.431 -23.053 1.00 15.51 ? 73  ILE   B CB   1 
ATOM   1394 C  CG1  . ILE   B 1 105 ? -26.641 12.476 -23.742 1.00 16.57 ? 73  ILE   B CG1  1 
ATOM   1395 C  CG2  . ILE   B 1 105 ? -28.926 11.447 -23.716 1.00 17.66 ? 73  ILE   B CG2  1 
ATOM   1396 C  CD1  . ILE   B 1 105 ? -25.874 11.164 -23.648 1.00 18.30 ? 73  ILE   B CD1  1 
ATOM   1397 N  N    . ASP   B 1 106 ? -31.061 14.103 -22.881 1.00 14.08 ? 74  ASP   B N    1 
ATOM   1398 C  CA   . ASP   B 1 106 ? -32.331 14.190 -22.156 1.00 14.75 ? 74  ASP   B CA   1 
ATOM   1399 C  C    . ASP   B 1 106 ? -32.879 12.785 -21.899 1.00 14.94 ? 74  ASP   B C    1 
ATOM   1400 O  O    . ASP   B 1 106 ? -33.814 12.305 -22.549 1.00 15.30 ? 74  ASP   B O    1 
ATOM   1401 C  CB   . ASP   B 1 106 ? -33.332 15.076 -22.879 1.00 16.54 ? 74  ASP   B CB   1 
ATOM   1402 C  CG   . ASP   B 1 106 ? -34.617 15.255 -22.088 1.00 17.91 ? 74  ASP   B CG   1 
ATOM   1403 O  OD1  . ASP   B 1 106 ? -34.707 14.744 -20.943 1.00 17.97 ? 74  ASP   B OD1  1 
ATOM   1404 O  OD2  . ASP   B 1 106 ? -35.546 15.900 -22.611 1.00 20.93 ? 74  ASP   B OD2  1 
ATOM   1405 N  N    . THR   B 1 107 ? -32.289 12.123 -20.902 1.00 14.51 ? 75  THR   B N    1 
ATOM   1406 C  CA   . THR   B 1 107 ? -32.736 10.786 -20.524 1.00 13.97 ? 75  THR   B CA   1 
ATOM   1407 C  C    . THR   B 1 107 ? -34.087 10.823 -19.819 1.00 14.04 ? 75  THR   B C    1 
ATOM   1408 O  O    . THR   B 1 107 ? -34.847 9.848  -19.876 1.00 16.35 ? 75  THR   B O    1 
ATOM   1409 C  CB   . THR   B 1 107 ? -31.683 10.129 -19.622 1.00 14.91 ? 75  THR   B CB   1 
ATOM   1410 O  OG1  . THR   B 1 107 ? -31.437 10.964 -18.479 1.00 15.48 ? 75  THR   B OG1  1 
ATOM   1411 C  CG2  . THR   B 1 107 ? -30.379 9.941  -20.384 1.00 15.81 ? 75  THR   B CG2  1 
ATOM   1412 N  N    . LYS   B 1 108 ? -34.396 11.925 -19.136 1.00 13.91 ? 76  LYS   B N    1 
ATOM   1413 C  CA   . LYS   B 1 108 ? -35.647 11.988 -18.391 1.00 15.82 ? 76  LYS   B CA   1 
ATOM   1414 C  C    . LYS   B 1 108 ? -36.847 11.897 -19.323 1.00 16.35 ? 76  LYS   B C    1 
ATOM   1415 O  O    . LYS   B 1 108 ? -37.792 11.150 -19.049 1.00 17.26 ? 76  LYS   B O    1 
ATOM   1416 C  CB   . LYS   B 1 108 ? -35.694 13.265 -17.554 1.00 17.40 ? 76  LYS   B CB   1 
ATOM   1417 C  CG   . LYS   B 1 108 ? -36.939 13.410 -16.702 1.00 21.60 ? 76  LYS   B CG   1 
ATOM   1418 C  CD   . LYS   B 1 108 ? -36.858 14.673 -15.859 1.00 25.52 ? 76  LYS   B CD   1 
ATOM   1419 C  CE   . LYS   B 1 108 ? -38.085 14.833 -14.986 1.00 30.24 ? 76  LYS   B CE   1 
ATOM   1420 N  NZ   . LYS   B 1 108 ? -37.959 15.990 -14.062 1.00 33.53 ? 76  LYS   B NZ   1 
ATOM   1421 N  N    . SER   B 1 109 ? -36.823 12.638 -20.437 1.00 16.08 ? 77  SER   B N    1 
ATOM   1422 C  CA   . SER   B 1 109 ? -37.926 12.573 -21.390 1.00 16.82 ? 77  SER   B CA   1 
ATOM   1423 C  C    . SER   B 1 109 ? -38.033 11.197 -22.019 1.00 17.93 ? 77  SER   B C    1 
ATOM   1424 O  O    . SER   B 1 109 ? -39.143 10.734 -22.312 1.00 18.90 ? 77  SER   B O    1 
ATOM   1425 C  CB   . SER   B 1 109 ? -37.739 13.629 -22.479 1.00 18.39 ? 77  SER   B CB   1 
ATOM   1426 O  OG   . SER   B 1 109 ? -37.862 14.923 -21.931 1.00 19.99 ? 77  SER   B OG   1 
ATOM   1427 N  N    . TYR   B 1 110 ? -36.893 10.535 -22.224 1.00 17.64 ? 78  TYR   B N    1 
ATOM   1428 C  CA   . TYR   B 1 110 ? -36.896 9.192  -22.785 1.00 16.38 ? 78  TYR   B CA   1 
ATOM   1429 C  C    . TYR   B 1 110 ? -37.663 8.237  -21.885 1.00 16.33 ? 78  TYR   B C    1 
ATOM   1430 O  O    . TYR   B 1 110 ? -38.563 7.523  -22.341 1.00 18.83 ? 78  TYR   B O    1 
ATOM   1431 C  CB   . TYR   B 1 110 ? -35.457 8.713  -22.964 1.00 16.36 ? 78  TYR   B CB   1 
ATOM   1432 C  CG   . TYR   B 1 110 ? -35.364 7.303  -23.491 1.00 15.78 ? 78  TYR   B CG   1 
ATOM   1433 C  CD1  . TYR   B 1 110 ? -35.590 7.036  -24.831 1.00 16.62 ? 78  TYR   B CD1  1 
ATOM   1434 C  CD2  . TYR   B 1 110 ? -35.058 6.241  -22.647 1.00 15.72 ? 78  TYR   B CD2  1 
ATOM   1435 C  CE1  . TYR   B 1 110 ? -35.489 5.757  -25.329 1.00 17.53 ? 78  TYR   B CE1  1 
ATOM   1436 C  CE2  . TYR   B 1 110 ? -34.956 4.953  -23.135 1.00 15.38 ? 78  TYR   B CE2  1 
ATOM   1437 C  CZ   . TYR   B 1 110 ? -35.182 4.715  -24.478 1.00 16.60 ? 78  TYR   B CZ   1 
ATOM   1438 O  OH   . TYR   B 1 110 ? -35.101 3.439  -24.990 1.00 18.37 ? 78  TYR   B OH   1 
ATOM   1439 N  N    . TRP   B 1 111 ? -37.321 8.215  -20.591 1.00 16.11 ? 79  TRP   B N    1 
ATOM   1440 C  CA   . TRP   B 1 111 ? -38.001 7.311  -19.666 1.00 16.16 ? 79  TRP   B CA   1 
ATOM   1441 C  C    . TRP   B 1 111 ? -39.461 7.699  -19.470 1.00 18.53 ? 79  TRP   B C    1 
ATOM   1442 O  O    . TRP   B 1 111 ? -40.334 6.825  -19.397 1.00 20.72 ? 79  TRP   B O    1 
ATOM   1443 C  CB   . TRP   B 1 111 ? -37.260 7.246  -18.330 1.00 16.78 ? 79  TRP   B CB   1 
ATOM   1444 C  CG   . TRP   B 1 111 ? -35.922 6.596  -18.449 1.00 15.10 ? 79  TRP   B CG   1 
ATOM   1445 C  CD1  . TRP   B 1 111 ? -34.704 7.177  -18.243 1.00 15.44 ? 79  TRP   B CD1  1 
ATOM   1446 C  CD2  . TRP   B 1 111 ? -35.657 5.248  -18.865 1.00 15.42 ? 79  TRP   B CD2  1 
ATOM   1447 N  NE1  . TRP   B 1 111 ? -33.701 6.266  -18.468 1.00 14.49 ? 79  TRP   B NE1  1 
ATOM   1448 C  CE2  . TRP   B 1 111 ? -34.256 5.078  -18.863 1.00 15.35 ? 79  TRP   B CE2  1 
ATOM   1449 C  CE3  . TRP   B 1 111 ? -36.468 4.165  -19.229 1.00 16.10 ? 79  TRP   B CE3  1 
ATOM   1450 C  CZ2  . TRP   B 1 111 ? -33.647 3.867  -19.202 1.00 16.33 ? 79  TRP   B CZ2  1 
ATOM   1451 C  CZ3  . TRP   B 1 111 ? -35.861 2.969  -19.578 1.00 16.70 ? 79  TRP   B CZ3  1 
ATOM   1452 C  CH2  . TRP   B 1 111 ? -34.464 2.830  -19.560 1.00 16.19 ? 79  TRP   B CH2  1 
ATOM   1453 N  N    . LYS   B 1 112 ? -39.753 8.998  -19.385 1.00 18.10 ? 80  LYS   B N    1 
ATOM   1454 C  CA   . LYS   B 1 112 ? -41.141 9.400  -19.190 1.00 20.80 ? 80  LYS   B CA   1 
ATOM   1455 C  C    . LYS   B 1 112 ? -42.022 8.984  -20.364 1.00 23.07 ? 80  LYS   B C    1 
ATOM   1456 O  O    . LYS   B 1 112 ? -43.193 8.633  -20.167 1.00 25.67 ? 80  LYS   B O    1 
ATOM   1457 C  CB   . LYS   B 1 112 ? -41.226 10.898 -18.891 1.00 24.36 ? 80  LYS   B CB   1 
ATOM   1458 C  CG   . LYS   B 1 112 ? -40.653 11.256 -17.519 1.00 31.11 ? 80  LYS   B CG   1 
ATOM   1459 C  CD   . LYS   B 1 112 ? -41.043 12.649 -17.076 1.00 38.25 ? 80  LYS   B CD   1 
ATOM   1460 C  CE   . LYS   B 1 112 ? -42.536 12.729 -16.806 1.00 43.52 ? 80  LYS   B CE   1 
ATOM   1461 N  NZ   . LYS   B 1 112 ? -42.887 13.982 -16.093 1.00 47.21 ? 80  LYS   B NZ   1 
ATOM   1462 N  N    . ALA   B 1 113 ? -41.475 8.986  -21.585 1.00 23.99 ? 81  ALA   B N    1 
ATOM   1463 C  CA   . ALA   B 1 113 ? -42.246 8.521  -22.735 1.00 26.87 ? 81  ALA   B CA   1 
ATOM   1464 C  C    . ALA   B 1 113 ? -42.571 7.034  -22.630 1.00 29.03 ? 81  ALA   B C    1 
ATOM   1465 O  O    . ALA   B 1 113 ? -43.587 6.581  -23.172 1.00 31.01 ? 81  ALA   B O    1 
ATOM   1466 C  CB   . ALA   B 1 113 ? -41.495 8.821  -24.033 1.00 28.06 ? 81  ALA   B CB   1 
ATOM   1467 N  N    . LEU   B 1 114 ? -41.735 6.267  -21.937 1.00 28.62 ? 82  LEU   B N    1 
ATOM   1468 C  CA   . LEU   B 1 114 ? -41.978 4.852  -21.707 1.00 30.10 ? 82  LEU   B CA   1 
ATOM   1469 C  C    . LEU   B 1 114 ? -42.823 4.601  -20.465 1.00 30.93 ? 82  LEU   B C    1 
ATOM   1470 O  O    . LEU   B 1 114 ? -43.035 3.440  -20.093 1.00 32.53 ? 82  LEU   B O    1 
ATOM   1471 C  CB   . LEU   B 1 114 ? -40.646 4.105  -21.616 1.00 29.55 ? 82  LEU   B CB   1 
ATOM   1472 C  CG   . LEU   B 1 114 ? -39.835 4.165  -22.911 1.00 31.08 ? 82  LEU   B CG   1 
ATOM   1473 C  CD1  . LEU   B 1 114 ? -38.437 3.587  -22.719 1.00 31.61 ? 82  LEU   B CD1  1 
ATOM   1474 C  CD2  . LEU   B 1 114 ? -40.575 3.432  -24.020 1.00 33.69 ? 82  LEU   B CD2  1 
ATOM   1475 N  N    . GLY   B 1 115 ? -43.326 5.662  -19.835 1.00 29.56 ? 83  GLY   B N    1 
ATOM   1476 C  CA   . GLY   B 1 115 ? -44.108 5.520  -18.625 1.00 30.18 ? 83  GLY   B CA   1 
ATOM   1477 C  C    . GLY   B 1 115 ? -43.311 5.091  -17.420 1.00 29.32 ? 83  GLY   B C    1 
ATOM   1478 O  O    . GLY   B 1 115 ? -43.870 4.498  -16.493 1.00 31.85 ? 83  GLY   B O    1 
ATOM   1479 N  N    . ILE   B 1 116 ? -42.011 5.359  -17.414 1.00 29.55 ? 84  ILE   B N    1 
ATOM   1480 C  CA   . ILE   B 1 116 ? -41.113 4.948  -16.346 1.00 30.51 ? 84  ILE   B CA   1 
ATOM   1481 C  C    . ILE   B 1 116 ? -40.596 6.202  -15.659 1.00 31.34 ? 84  ILE   B C    1 
ATOM   1482 O  O    . ILE   B 1 116 ? -40.185 7.159  -16.328 1.00 32.14 ? 84  ILE   B O    1 
ATOM   1483 C  CB   . ILE   B 1 116 ? -39.960 4.101  -16.913 1.00 30.95 ? 84  ILE   B CB   1 
ATOM   1484 C  CG1  . ILE   B 1 116 ? -40.514 2.822  -17.552 1.00 31.39 ? 84  ILE   B CG1  1 
ATOM   1485 C  CG2  . ILE   B 1 116 ? -38.943 3.784  -15.832 1.00 31.52 ? 84  ILE   B CG2  1 
ATOM   1486 C  CD1  . ILE   B 1 116 ? -39.522 2.098  -18.436 1.00 32.26 ? 84  ILE   B CD1  1 
ATOM   1487 N  N    . SER   B 1 117 ? -40.612 6.197  -14.327 1.00 29.85 ? 85  SER   B N    1 
ATOM   1488 C  CA   . SER   B 1 117 ? -40.129 7.335  -13.556 1.00 28.71 ? 85  SER   B CA   1 
ATOM   1489 C  C    . SER   B 1 117 ? -38.619 7.216  -13.387 1.00 27.57 ? 85  SER   B C    1 
ATOM   1490 O  O    . SER   B 1 117 ? -38.152 6.232  -12.798 1.00 30.76 ? 85  SER   B O    1 
ATOM   1491 C  CB   . SER   B 1 117 ? -40.787 7.358  -12.188 1.00 31.30 ? 85  SER   B CB   1 
ATOM   1492 O  OG   . SER   B 1 117 ? -40.462 8.549  -11.498 1.00 33.97 ? 85  SER   B OG   1 
ATOM   1493 N  N    . PRO   B 1 118 ? -37.821 8.154  -13.915 1.00 22.23 ? 86  PRO   B N    1 
ATOM   1494 C  CA   . PRO   B 1 118 ? -36.364 8.038  -13.779 1.00 21.03 ? 86  PRO   B CA   1 
ATOM   1495 C  C    . PRO   B 1 118 ? -35.773 8.855  -12.643 1.00 19.86 ? 86  PRO   B C    1 
ATOM   1496 O  O    . PRO   B 1 118 ? -36.422 9.734  -12.062 1.00 23.77 ? 86  PRO   B O    1 
ATOM   1497 C  CB   . PRO   B 1 118 ? -35.862 8.550  -15.128 1.00 22.68 ? 86  PRO   B CB   1 
ATOM   1498 C  CG   . PRO   B 1 118 ? -36.840 9.629  -15.458 1.00 23.83 ? 86  PRO   B CG   1 
ATOM   1499 C  CD   . PRO   B 1 118 ? -38.186 9.200  -14.887 1.00 24.13 ? 86  PRO   B CD   1 
ATOM   1500 N  N    . PHE   B 1 119 ? -34.502 8.587  -12.353 1.00 16.80 ? 87  PHE   B N    1 
ATOM   1501 C  CA   . PHE   B 1 119 ? -33.797 9.325  -11.311 1.00 16.48 ? 87  PHE   B CA   1 
ATOM   1502 C  C    . PHE   B 1 119 ? -33.199 10.632 -11.831 1.00 15.89 ? 87  PHE   B C    1 
ATOM   1503 O  O    . PHE   B 1 119 ? -33.378 11.692 -11.218 1.00 17.16 ? 87  PHE   B O    1 
ATOM   1504 C  CB   . PHE   B 1 119 ? -32.701 8.450  -10.708 1.00 18.36 ? 87  PHE   B CB   1 
ATOM   1505 C  CG   . PHE   B 1 119 ? -31.886 9.159  -9.670  1.00 18.60 ? 87  PHE   B CG   1 
ATOM   1506 C  CD1  . PHE   B 1 119 ? -32.421 9.426  -8.423  1.00 20.71 ? 87  PHE   B CD1  1 
ATOM   1507 C  CD2  . PHE   B 1 119 ? -30.594 9.570  -9.945  1.00 19.08 ? 87  PHE   B CD2  1 
ATOM   1508 C  CE1  . PHE   B 1 119 ? -31.685 10.094 -7.460  1.00 20.84 ? 87  PHE   B CE1  1 
ATOM   1509 C  CE2  . PHE   B 1 119 ? -29.846 10.240 -8.986  1.00 20.93 ? 87  PHE   B CE2  1 
ATOM   1510 C  CZ   . PHE   B 1 119 ? -30.398 10.497 -7.738  1.00 21.09 ? 87  PHE   B CZ   1 
ATOM   1511 N  N    . HIS   B 1 120 ? -32.471 10.580 -12.941 1.00 15.25 ? 88  HIS   B N    1 
ATOM   1512 C  CA   . HIS   B 1 120 ? -31.658 11.708 -13.379 1.00 14.21 ? 88  HIS   B CA   1 
ATOM   1513 C  C    . HIS   B 1 120 ? -32.474 12.701 -14.197 1.00 14.49 ? 88  HIS   B C    1 
ATOM   1514 O  O    . HIS   B 1 120 ? -33.396 12.332 -14.924 1.00 15.46 ? 88  HIS   B O    1 
ATOM   1515 C  CB   . HIS   B 1 120 ? -30.491 11.213 -14.238 1.00 14.83 ? 88  HIS   B CB   1 
ATOM   1516 C  CG   . HIS   B 1 120 ? -29.586 10.260 -13.528 1.00 15.12 ? 88  HIS   B CG   1 
ATOM   1517 N  ND1  . HIS   B 1 120 ? -29.730 8.890  -13.611 1.00 16.26 ? 88  HIS   B ND1  1 
ATOM   1518 C  CD2  . HIS   B 1 120 ? -28.534 10.481 -12.707 1.00 17.73 ? 88  HIS   B CD2  1 
ATOM   1519 C  CE1  . HIS   B 1 120 ? -28.797 8.311  -12.879 1.00 18.09 ? 88  HIS   B CE1  1 
ATOM   1520 N  NE2  . HIS   B 1 120 ? -28.057 9.253  -12.322 1.00 19.06 ? 88  HIS   B NE2  1 
ATOM   1521 N  N    . GLU   B 1 121 ? -32.116 13.980 -14.076 1.00 14.76 ? 89  GLU   B N    1 
ATOM   1522 C  CA   . GLU   B 1 121 ? -32.685 14.982 -14.976 1.00 15.18 ? 89  GLU   B CA   1 
ATOM   1523 C  C    . GLU   B 1 121 ? -32.182 14.778 -16.393 1.00 16.54 ? 89  GLU   B C    1 
ATOM   1524 O  O    . GLU   B 1 121 ? -32.918 14.989 -17.364 1.00 19.45 ? 89  GLU   B O    1 
ATOM   1525 C  CB   . GLU   B 1 121 ? -32.323 16.387 -14.497 1.00 17.97 ? 89  GLU   B CB   1 
ATOM   1526 C  CG   . GLU   B 1 121 ? -33.101 16.816 -13.291 1.00 20.46 ? 89  GLU   B CG   1 
ATOM   1527 C  CD   . GLU   B 1 121 ? -34.582 16.894 -13.583 1.00 23.10 ? 89  GLU   B CD   1 
ATOM   1528 O  OE1  . GLU   B 1 121 ? -34.976 17.685 -14.461 1.00 27.31 ? 89  GLU   B OE1  1 
ATOM   1529 O  OE2  . GLU   B 1 121 ? -35.347 16.156 -12.941 1.00 25.67 ? 89  GLU   B OE2  1 
ATOM   1530 N  N    . HIS   B 1 122 ? -30.919 14.406 -16.527 1.00 15.94 ? 90  HIS   B N    1 
ATOM   1531 C  CA   . HIS   B 1 122 ? -30.294 14.177 -17.819 1.00 15.82 ? 90  HIS   B CA   1 
ATOM   1532 C  C    . HIS   B 1 122 ? -28.994 13.451 -17.526 1.00 17.77 ? 90  HIS   B C    1 
ATOM   1533 O  O    . HIS   B 1 122 ? -28.601 13.301 -16.368 1.00 20.22 ? 90  HIS   B O    1 
ATOM   1534 C  CB   . HIS   B 1 122 ? -30.071 15.484 -18.607 1.00 18.81 ? 90  HIS   B CB   1 
ATOM   1535 C  CG   . HIS   B 1 122 ? -29.508 16.614 -17.800 1.00 25.60 ? 90  HIS   B CG   1 
ATOM   1536 N  ND1  . HIS   B 1 122 ? -28.175 16.696 -17.461 1.00 31.33 ? 90  HIS   B ND1  1 
ATOM   1537 C  CD2  . HIS   B 1 122 ? -30.091 17.732 -17.305 1.00 29.62 ? 90  HIS   B CD2  1 
ATOM   1538 C  CE1  . HIS   B 1 122 ? -27.963 17.806 -16.776 1.00 32.91 ? 90  HIS   B CE1  1 
ATOM   1539 N  NE2  . HIS   B 1 122 ? -29.111 18.451 -16.663 1.00 31.88 ? 90  HIS   B NE2  1 
ATOM   1540 N  N    . ALA   B 1 123 ? -28.350 12.965 -18.578 1.00 18.05 ? 91  ALA   B N    1 
ATOM   1541 C  CA   . ALA   B 1 123 ? -27.016 12.388 -18.475 1.00 19.73 ? 91  ALA   B CA   1 
ATOM   1542 C  C    . ALA   B 1 123 ? -26.068 13.363 -19.148 1.00 20.71 ? 91  ALA   B C    1 
ATOM   1543 O  O    . ALA   B 1 123 ? -26.275 13.731 -20.310 1.00 22.55 ? 91  ALA   B O    1 
ATOM   1544 C  CB   . ALA   B 1 123 ? -26.945 11.017 -19.149 1.00 22.96 ? 91  ALA   B CB   1 
ATOM   1545 N  N    . GLU   B 1 124 ? -25.058 13.808 -18.413 1.00 21.97 ? 92  GLU   B N    1 
ATOM   1546 C  CA   . GLU   B 1 124 ? -24.104 14.781 -18.919 1.00 23.10 ? 92  GLU   B CA   1 
ATOM   1547 C  C    . GLU   B 1 124 ? -22.748 14.113 -19.097 1.00 21.85 ? 92  GLU   B C    1 
ATOM   1548 O  O    . GLU   B 1 124 ? -22.329 13.302 -18.264 1.00 24.54 ? 92  GLU   B O    1 
ATOM   1549 C  CB   . GLU   B 1 124 ? -23.981 15.985 -17.973 1.00 26.28 ? 92  GLU   B CB   1 
ATOM   1550 N  N    . VAL   B 1 125 ? -22.080 14.438 -20.198 1.00 16.87 ? 93  VAL   B N    1 
ATOM   1551 C  CA   . VAL   B 1 125 ? -20.746 13.937 -20.494 1.00 15.13 ? 93  VAL   B CA   1 
ATOM   1552 C  C    . VAL   B 1 125 ? -19.886 15.152 -20.823 1.00 13.37 ? 93  VAL   B C    1 
ATOM   1553 O  O    . VAL   B 1 125 ? -20.115 15.822 -21.837 1.00 15.61 ? 93  VAL   B O    1 
ATOM   1554 C  CB   . VAL   B 1 125 ? -20.762 12.950 -21.670 1.00 17.92 ? 93  VAL   B CB   1 
ATOM   1555 C  CG1  . VAL   B 1 125 ? -19.369 12.408 -21.913 1.00 20.43 ? 93  VAL   B CG1  1 
ATOM   1556 C  CG2  . VAL   B 1 125 ? -21.750 11.806 -21.408 1.00 19.93 ? 93  VAL   B CG2  1 
ATOM   1557 N  N    . VAL   B 1 126 ? -18.910 15.448 -19.968 1.00 12.83 ? 94  VAL   B N    1 
ATOM   1558 C  CA   . VAL   B 1 126 ? -18.082 16.642 -20.101 1.00 13.61 ? 94  VAL   B CA   1 
ATOM   1559 C  C    . VAL   B 1 126 ? -16.636 16.210 -20.303 1.00 14.13 ? 94  VAL   B C    1 
ATOM   1560 O  O    . VAL   B 1 126 ? -16.091 15.453 -19.491 1.00 13.84 ? 94  VAL   B O    1 
ATOM   1561 C  CB   . VAL   B 1 126 ? -18.225 17.556 -18.869 1.00 15.21 ? 94  VAL   B CB   1 
ATOM   1562 C  CG1  . VAL   B 1 126 ? -17.406 18.836 -19.045 1.00 17.61 ? 94  VAL   B CG1  1 
ATOM   1563 C  CG2  . VAL   B 1 126 ? -19.698 17.886 -18.628 1.00 18.04 ? 94  VAL   B CG2  1 
ATOM   1564 N  N    . PHE   B 1 127 ? -16.005 16.717 -21.362 1.00 15.03 ? 95  PHE   B N    1 
ATOM   1565 C  CA   . PHE   B 1 127 ? -14.684 16.240 -21.750 1.00 14.12 ? 95  PHE   B CA   1 
ATOM   1566 C  C    . PHE   B 1 127 ? -13.955 17.304 -22.559 1.00 14.79 ? 95  PHE   B C    1 
ATOM   1567 O  O    . PHE   B 1 127 ? -14.574 18.076 -23.289 1.00 15.91 ? 95  PHE   B O    1 
ATOM   1568 C  CB   . PHE   B 1 127 ? -14.797 14.942 -22.565 1.00 14.89 ? 95  PHE   B CB   1 
ATOM   1569 C  CG   . PHE   B 1 127 ? -15.586 15.079 -23.846 1.00 16.40 ? 95  PHE   B CG   1 
ATOM   1570 C  CD1  . PHE   B 1 127 ? -16.971 15.033 -23.837 1.00 18.16 ? 95  PHE   B CD1  1 
ATOM   1571 C  CD2  . PHE   B 1 127 ? -14.935 15.234 -25.064 1.00 17.26 ? 95  PHE   B CD2  1 
ATOM   1572 C  CE1  . PHE   B 1 127 ? -17.696 15.152 -25.014 1.00 20.34 ? 95  PHE   B CE1  1 
ATOM   1573 C  CE2  . PHE   B 1 127 ? -15.662 15.346 -26.251 1.00 18.45 ? 95  PHE   B CE2  1 
ATOM   1574 C  CZ   . PHE   B 1 127 ? -17.038 15.314 -26.218 1.00 20.22 ? 95  PHE   B CZ   1 
ATOM   1575 N  N    . THR   B 1 128 ? -12.627 17.321 -22.439 1.00 16.78 ? 96  THR   B N    1 
ATOM   1576 C  CA   . THR   B 1 128 ? -11.802 18.110 -23.345 1.00 16.70 ? 96  THR   B CA   1 
ATOM   1577 C  C    . THR   B 1 128 ? -11.598 17.331 -24.638 1.00 18.40 ? 96  THR   B C    1 
ATOM   1578 O  O    . THR   B 1 128 ? -11.332 16.125 -24.613 1.00 19.82 ? 96  THR   B O    1 
ATOM   1579 C  CB   . THR   B 1 128 ? -10.450 18.423 -22.698 1.00 17.70 ? 96  THR   B CB   1 
ATOM   1580 O  OG1  . THR   B 1 128 ? -10.662 19.201 -21.518 1.00 19.67 ? 96  THR   B OG1  1 
ATOM   1581 C  CG2  . THR   B 1 128 ? -9.563  19.208 -23.648 1.00 19.59 ? 96  THR   B CG2  1 
ATOM   1582 N  N    . ALA   B 1 129 ? -11.753 18.011 -25.769 1.00 16.33 ? 97  ALA   B N    1 
ATOM   1583 C  CA   . ALA   B 1 129 ? -11.562 17.402 -27.076 1.00 16.10 ? 97  ALA   B CA   1 
ATOM   1584 C  C    . ALA   B 1 129 ? -10.597 18.241 -27.898 1.00 18.13 ? 97  ALA   B C    1 
ATOM   1585 O  O    . ALA   B 1 129 ? -10.540 19.469 -27.759 1.00 18.30 ? 97  ALA   B O    1 
ATOM   1586 C  CB   . ALA   B 1 129 ? -12.897 17.287 -27.834 1.00 18.35 ? 97  ALA   B CB   1 
ATOM   1587 N  N    . ASN   B 1 130 ? -9.852  17.555 -28.765 1.00 17.57 ? 98  ASN   B N    1 
ATOM   1588 C  CA   . ASN   B 1 130 ? -8.997  18.141 -29.793 1.00 18.56 ? 98  ASN   B CA   1 
ATOM   1589 C  C    . ASN   B 1 130 ? -7.806  18.914 -29.238 1.00 20.01 ? 98  ASN   B C    1 
ATOM   1590 O  O    . ASN   B 1 130 ? -7.210  19.724 -29.954 1.00 19.32 ? 98  ASN   B O    1 
ATOM   1591 C  CB   . ASN   B 1 130 ? -9.795  18.978 -30.799 1.00 19.80 ? 98  ASN   B CB   1 
ATOM   1592 C  CG   . ASN   B 1 130 ? -10.977 18.214 -31.357 1.00 19.06 ? 98  ASN   B CG   1 
ATOM   1593 O  OD1  . ASN   B 1 130 ? -10.811 17.193 -32.030 1.00 19.95 ? 98  ASN   B OD1  1 
ATOM   1594 N  ND2  . ASN   B 1 130 ? -12.182 18.677 -31.044 1.00 18.73 ? 98  ASN   B ND2  1 
ATOM   1595 N  N    . ASP   B 1 131 ? -7.430  18.664 -27.982 1.00 22.66 ? 99  ASP   B N    1 
ATOM   1596 C  CA   . ASP   B 1 131 ? -6.308  19.389 -27.396 1.00 27.95 ? 99  ASP   B CA   1 
ATOM   1597 C  C    . ASP   B 1 131 ? -4.989  19.016 -28.059 1.00 26.48 ? 99  ASP   B C    1 
ATOM   1598 O  O    . ASP   B 1 131 ? -4.044  19.810 -28.043 1.00 28.43 ? 99  ASP   B O    1 
ATOM   1599 C  CB   . ASP   B 1 131 ? -6.251  19.153 -25.886 1.00 37.62 ? 99  ASP   B CB   1 
ATOM   1600 C  CG   . ASP   B 1 131 ? -5.187  19.989 -25.205 1.00 48.81 ? 99  ASP   B CG   1 
ATOM   1601 O  OD1  . ASP   B 1 131 ? -5.376  21.221 -25.098 1.00 51.17 ? 99  ASP   B OD1  1 
ATOM   1602 O  OD2  . ASP   B 1 131 ? -4.162  19.414 -24.779 1.00 53.46 ? 99  ASP   B OD2  1 
ATOM   1603 N  N    . SER   B 1 132 ? -4.897  17.813 -28.627 1.00 22.65 ? 100 SER   B N    1 
ATOM   1604 C  CA   . SER   B 1 132 ? -3.729  17.398 -29.394 1.00 23.51 ? 100 SER   B CA   1 
ATOM   1605 C  C    . SER   B 1 132 ? -4.032  17.339 -30.886 1.00 22.18 ? 100 SER   B C    1 
ATOM   1606 O  O    . SER   B 1 132 ? -3.485  16.502 -31.608 1.00 22.17 ? 100 SER   B O    1 
ATOM   1607 C  CB   . SER   B 1 132 ? -3.198  16.055 -28.897 1.00 27.53 ? 100 SER   B CB   1 
ATOM   1608 O  OG   . SER   B 1 132 ? -2.740  16.165 -27.562 1.00 31.33 ? 100 SER   B OG   1 
ATOM   1609 N  N    . GLY   B 1 133 ? -4.889  18.239 -31.357 1.00 19.09 ? 101 GLY   B N    1 
ATOM   1610 C  CA   . GLY   B 1 133 ? -5.350  18.232 -32.723 1.00 20.14 ? 101 GLY   B CA   1 
ATOM   1611 C  C    . GLY   B 1 133 ? -6.553  17.328 -32.889 1.00 20.16 ? 101 GLY   B C    1 
ATOM   1612 O  O    . GLY   B 1 133 ? -6.994  16.658 -31.944 1.00 20.64 ? 101 GLY   B O    1 
ATOM   1613 N  N    . PRO   B 1 134 ? -7.084  17.262 -34.110 1.00 20.69 ? 102 PRO   B N    1 
ATOM   1614 C  CA   . PRO   B 1 134 ? -8.316  16.495 -34.341 1.00 22.08 ? 102 PRO   B CA   1 
ATOM   1615 C  C    . PRO   B 1 134 ? -8.220  15.051 -33.871 1.00 22.45 ? 102 PRO   B C    1 
ATOM   1616 O  O    . PRO   B 1 134 ? -7.193  14.385 -34.020 1.00 22.26 ? 102 PRO   B O    1 
ATOM   1617 C  CB   . PRO   B 1 134 ? -8.497  16.561 -35.862 1.00 23.28 ? 102 PRO   B CB   1 
ATOM   1618 C  CG   . PRO   B 1 134 ? -7.763  17.774 -36.286 1.00 23.09 ? 102 PRO   B CG   1 
ATOM   1619 C  CD   . PRO   B 1 134 ? -6.636  17.979 -35.318 1.00 21.01 ? 102 PRO   B CD   1 
ATOM   1620 N  N    . ARG   B 1 135 ? -9.313  14.582 -33.281 1.00 19.72 ? 103 ARG   B N    1 
ATOM   1621 C  CA   . ARG   B 1 135 ? -9.543  13.167 -33.054 1.00 19.45 ? 103 ARG   B CA   1 
ATOM   1622 C  C    . ARG   B 1 135 ? -10.990 12.888 -33.420 1.00 20.40 ? 103 ARG   B C    1 
ATOM   1623 O  O    . ARG   B 1 135 ? -11.806 13.805 -33.552 1.00 20.61 ? 103 ARG   B O    1 
ATOM   1624 C  CB   . ARG   B 1 135 ? -9.309  12.767 -31.588 1.00 20.68 ? 103 ARG   B CB   1 
ATOM   1625 C  CG   . ARG   B 1 135 ? -7.885  12.959 -31.073 1.00 21.36 ? 103 ARG   B CG   1 
ATOM   1626 C  CD   . ARG   B 1 135 ? -6.901  11.992 -31.726 1.00 20.99 ? 103 ARG   B CD   1 
ATOM   1627 N  NE   . ARG   B 1 135 ? -5.597  12.028 -31.063 1.00 21.52 ? 103 ARG   B NE   1 
ATOM   1628 C  CZ   . ARG   B 1 135 ? -4.712  13.016 -31.196 1.00 22.16 ? 103 ARG   B CZ   1 
ATOM   1629 N  NH1  . ARG   B 1 135 ? -4.980  14.055 -31.974 1.00 24.01 ? 103 ARG   B NH1  1 
ATOM   1630 N  NH2  . ARG   B 1 135 ? -3.558  12.968 -30.545 1.00 24.35 ? 103 ARG   B NH2  1 
ATOM   1631 N  N    . ARG   B 1 136 ? -11.307 11.609 -33.574 1.00 21.36 ? 104 ARG   B N    1 
ATOM   1632 C  CA   . ARG   B 1 136 ? -12.680 11.157 -33.757 1.00 22.52 ? 104 ARG   B CA   1 
ATOM   1633 C  C    . ARG   B 1 136 ? -13.178 10.598 -32.434 1.00 20.03 ? 104 ARG   B C    1 
ATOM   1634 O  O    . ARG   B 1 136 ? -12.506 9.767  -31.812 1.00 20.91 ? 104 ARG   B O    1 
ATOM   1635 C  CB   . ARG   B 1 136 ? -12.770 10.073 -34.832 1.00 29.13 ? 104 ARG   B CB   1 
ATOM   1636 C  CG   . ARG   B 1 136 ? -12.610 10.561 -36.269 1.00 39.11 ? 104 ARG   B CG   1 
ATOM   1637 C  CD   . ARG   B 1 136 ? -12.609 9.367  -37.216 1.00 48.84 ? 104 ARG   B CD   1 
ATOM   1638 N  NE   . ARG   B 1 136 ? -13.314 9.624  -38.470 1.00 56.73 ? 104 ARG   B NE   1 
ATOM   1639 C  CZ   . ARG   B 1 136 ? -14.511 9.127  -38.777 1.00 61.99 ? 104 ARG   B CZ   1 
ATOM   1640 N  NH1  . ARG   B 1 136 ? -15.150 8.337  -37.922 1.00 62.94 ? 104 ARG   B NH1  1 
ATOM   1641 N  NH2  . ARG   B 1 136 ? -15.067 9.414  -39.947 1.00 63.46 ? 104 ARG   B NH2  1 
ATOM   1642 N  N    . TYR   B 1 137 ? -14.352 11.052 -32.010 1.00 16.56 ? 105 TYR   B N    1 
ATOM   1643 C  CA   . TYR   B 1 137 ? -14.890 10.723 -30.699 1.00 16.65 ? 105 TYR   B CA   1 
ATOM   1644 C  C    . TYR   B 1 137 ? -16.219 10.010 -30.862 1.00 17.13 ? 105 TYR   B C    1 
ATOM   1645 O  O    . TYR   B 1 137 ? -17.113 10.512 -31.549 1.00 18.13 ? 105 TYR   B O    1 
ATOM   1646 C  CB   . TYR   B 1 137 ? -15.117 11.995 -29.869 1.00 17.79 ? 105 TYR   B CB   1 
ATOM   1647 C  CG   . TYR   B 1 137 ? -13.844 12.724 -29.549 1.00 16.48 ? 105 TYR   B CG   1 
ATOM   1648 C  CD1  . TYR   B 1 137 ? -13.276 13.601 -30.467 1.00 18.26 ? 105 TYR   B CD1  1 
ATOM   1649 C  CD2  . TYR   B 1 137 ? -13.197 12.527 -28.342 1.00 18.25 ? 105 TYR   B CD2  1 
ATOM   1650 C  CE1  . TYR   B 1 137 ? -12.099 14.265 -30.183 1.00 19.38 ? 105 TYR   B CE1  1 
ATOM   1651 C  CE2  . TYR   B 1 137 ? -12.022 13.188 -28.044 1.00 18.67 ? 105 TYR   B CE2  1 
ATOM   1652 C  CZ   . TYR   B 1 137 ? -11.474 14.053 -28.970 1.00 17.98 ? 105 TYR   B CZ   1 
ATOM   1653 O  OH   . TYR   B 1 137 ? -10.295 14.702 -28.685 1.00 20.28 ? 105 TYR   B OH   1 
ATOM   1654 N  N    . THR   B 1 138 ? -16.351 8.850  -30.222 1.00 16.80 ? 106 THR   B N    1 
ATOM   1655 C  CA   . THR   B 1 138 ? -17.647 8.225  -30.005 1.00 16.47 ? 106 THR   B CA   1 
ATOM   1656 C  C    . THR   B 1 138 ? -17.946 8.263  -28.515 1.00 16.00 ? 106 THR   B C    1 
ATOM   1657 O  O    . THR   B 1 138 ? -17.169 7.740  -27.708 1.00 17.60 ? 106 THR   B O    1 
ATOM   1658 C  CB   . THR   B 1 138 ? -17.685 6.786  -30.514 1.00 18.57 ? 106 THR   B CB   1 
ATOM   1659 O  OG1  . THR   B 1 138 ? -17.544 6.782  -31.941 1.00 22.36 ? 106 THR   B OG1  1 
ATOM   1660 C  CG2  . THR   B 1 138 ? -19.014 6.135  -30.142 1.00 19.95 ? 106 THR   B CG2  1 
ATOM   1661 N  N    . ILE   B 1 139 ? -19.057 8.888  -28.159 1.00 15.01 ? 107 ILE   B N    1 
ATOM   1662 C  CA   . ILE   B 1 139 ? -19.557 8.903  -26.792 1.00 15.16 ? 107 ILE   B CA   1 
ATOM   1663 C  C    . ILE   B 1 139 ? -20.685 7.894  -26.739 1.00 14.39 ? 107 ILE   B C    1 
ATOM   1664 O  O    . ILE   B 1 139 ? -21.656 8.009  -27.490 1.00 16.49 ? 107 ILE   B O    1 
ATOM   1665 C  CB   . ILE   B 1 139 ? -20.080 10.298 -26.404 1.00 17.05 ? 107 ILE   B CB   1 
ATOM   1666 C  CG1  . ILE   B 1 139 ? -18.994 11.368 -26.549 1.00 20.37 ? 107 ILE   B CG1  1 
ATOM   1667 C  CG2  . ILE   B 1 139 ? -20.640 10.271 -24.974 1.00 17.71 ? 107 ILE   B CG2  1 
ATOM   1668 C  CD1  . ILE   B 1 139 ? -17.822 11.146 -25.657 1.00 23.28 ? 107 ILE   B CD1  1 
ATOM   1669 N  N    . ALA   B 1 140 ? -20.574 6.907  -25.863 1.00 15.52 ? 108 ALA   B N    1 
ATOM   1670 C  CA   . ALA   B 1 140 ? -21.630 5.919  -25.719 1.00 15.96 ? 108 ALA   B CA   1 
ATOM   1671 C  C    . ALA   B 1 140 ? -22.225 6.002  -24.322 1.00 15.38 ? 108 ALA   B C    1 
ATOM   1672 O  O    . ALA   B 1 140 ? -21.528 6.308  -23.349 1.00 16.47 ? 108 ALA   B O    1 
ATOM   1673 C  CB   . ALA   B 1 140 ? -21.112 4.508  -25.981 1.00 17.63 ? 108 ALA   B CB   1 
ATOM   1674 N  N    . ALA   B 1 141 ? -23.520 5.726  -24.229 1.00 14.77 ? 109 ALA   B N    1 
ATOM   1675 C  CA   . ALA   B 1 141 ? -24.211 5.723  -22.951 1.00 14.67 ? 109 ALA   B CA   1 
ATOM   1676 C  C    . ALA   B 1 141 ? -25.175 4.554  -22.910 1.00 14.23 ? 109 ALA   B C    1 
ATOM   1677 O  O    . ALA   B 1 141 ? -25.851 4.264  -23.899 1.00 16.27 ? 109 ALA   B O    1 
ATOM   1678 C  CB   . ALA   B 1 141 ? -24.986 7.025  -22.721 1.00 16.26 ? 109 ALA   B CB   1 
ATOM   1679 N  N    . LEU   B 1 142 ? -25.222 3.882  -21.761 1.00 13.98 ? 110 LEU   B N    1 
ATOM   1680 C  CA   . LEU   B 1 142 ? -26.137 2.779  -21.503 1.00 13.62 ? 110 LEU   B CA   1 
ATOM   1681 C  C    . LEU   B 1 142 ? -27.064 3.212  -20.380 1.00 13.65 ? 110 LEU   B C    1 
ATOM   1682 O  O    . LEU   B 1 142 ? -26.598 3.505  -19.272 1.00 15.51 ? 110 LEU   B O    1 
ATOM   1683 C  CB   . LEU   B 1 142 ? -25.340 1.540  -21.090 1.00 14.09 ? 110 LEU   B CB   1 
ATOM   1684 C  CG   . LEU   B 1 142 ? -26.149 0.312  -20.695 1.00 15.03 ? 110 LEU   B CG   1 
ATOM   1685 C  CD1  . LEU   B 1 142 ? -26.980 -0.181 -21.872 1.00 16.93 ? 110 LEU   B CD1  1 
ATOM   1686 C  CD2  . LEU   B 1 142 ? -25.225 -0.787 -20.193 1.00 17.26 ? 110 LEU   B CD2  1 
ATOM   1687 N  N    . LEU   B 1 143 ? -28.364 3.268  -20.663 1.00 13.22 ? 111 LEU   B N    1 
ATOM   1688 C  CA   . LEU   B 1 143 ? -29.342 3.902  -19.781 1.00 12.93 ? 111 LEU   B CA   1 
ATOM   1689 C  C    . LEU   B 1 143 ? -30.195 2.879  -19.039 1.00 12.41 ? 111 LEU   B C    1 
ATOM   1690 O  O    . LEU   B 1 143 ? -30.751 1.961  -19.653 1.00 13.29 ? 111 LEU   B O    1 
ATOM   1691 C  CB   . LEU   B 1 143 ? -30.291 4.790  -20.582 1.00 13.16 ? 111 LEU   B CB   1 
ATOM   1692 C  CG   . LEU   B 1 143 ? -29.671 5.844  -21.489 1.00 14.04 ? 111 LEU   B CG   1 
ATOM   1693 C  CD1  . LEU   B 1 143 ? -30.793 6.678  -22.091 1.00 15.32 ? 111 LEU   B CD1  1 
ATOM   1694 C  CD2  . LEU   B 1 143 ? -28.667 6.689  -20.714 1.00 13.30 ? 111 LEU   B CD2  1 
ATOM   1695 N  N    . SER   B 1 144 ? -30.363 3.098  -17.740 1.00 13.35 ? 112 SER   B N    1 
ATOM   1696 C  CA   . SER   B 1 144 ? -31.369 2.461  -16.906 1.00 13.17 ? 112 SER   B CA   1 
ATOM   1697 C  C    . SER   B 1 144 ? -32.090 3.562  -16.141 1.00 13.54 ? 112 SER   B C    1 
ATOM   1698 O  O    . SER   B 1 144 ? -31.610 4.698  -16.085 1.00 14.32 ? 112 SER   B O    1 
ATOM   1699 C  CB   . SER   B 1 144 ? -30.720 1.483  -15.913 1.00 15.74 ? 112 SER   B CB   1 
ATOM   1700 O  OG   . SER   B 1 144 ? -30.008 0.469  -16.602 1.00 17.04 ? 112 SER   B OG   1 
ATOM   1701 N  N    . PRO   B 1 145 ? -33.266 3.276  -15.570 1.00 14.61 ? 113 PRO   B N    1 
ATOM   1702 C  CA   . PRO   B 1 145 ? -34.023 4.369  -14.926 1.00 14.62 ? 113 PRO   B CA   1 
ATOM   1703 C  C    . PRO   B 1 145 ? -33.285 5.057  -13.788 1.00 13.75 ? 113 PRO   B C    1 
ATOM   1704 O  O    . PRO   B 1 145 ? -33.414 6.280  -13.631 1.00 16.03 ? 113 PRO   B O    1 
ATOM   1705 C  CB   . PRO   B 1 145 ? -35.309 3.669  -14.469 1.00 16.07 ? 113 PRO   B CB   1 
ATOM   1706 C  CG   . PRO   B 1 145 ? -35.501 2.600  -15.509 1.00 16.74 ? 113 PRO   B CG   1 
ATOM   1707 C  CD   . PRO   B 1 145 ? -34.105 2.084  -15.787 1.00 15.82 ? 113 PRO   B CD   1 
ATOM   1708 N  N    . TYR   B 1 146 ? -32.504 4.320  -12.994 1.00 13.82 ? 114 TYR   B N    1 
ATOM   1709 C  CA   . TYR   B 1 146 ? -31.775 4.905  -11.870 1.00 14.39 ? 114 TYR   B CA   1 
ATOM   1710 C  C    . TYR   B 1 146 ? -30.268 4.877  -12.055 1.00 14.28 ? 114 TYR   B C    1 
ATOM   1711 O  O    . TYR   B 1 146 ? -29.530 5.120  -11.096 1.00 16.05 ? 114 TYR   B O    1 
ATOM   1712 C  CB   . TYR   B 1 146 ? -32.171 4.242  -10.546 1.00 15.57 ? 114 TYR   B CB   1 
ATOM   1713 C  CG   . TYR   B 1 146 ? -33.460 4.775  -9.986  1.00 16.62 ? 114 TYR   B CG   1 
ATOM   1714 C  CD1  . TYR   B 1 146 ? -34.667 4.448  -10.575 1.00 21.45 ? 114 TYR   B CD1  1 
ATOM   1715 C  CD2  . TYR   B 1 146 ? -33.470 5.611  -8.875  1.00 15.85 ? 114 TYR   B CD2  1 
ATOM   1716 C  CE1  . TYR   B 1 146 ? -35.851 4.921  -10.076 1.00 24.19 ? 114 TYR   B CE1  1 
ATOM   1717 C  CE2  . TYR   B 1 146 ? -34.653 6.112  -8.380  1.00 18.97 ? 114 TYR   B CE2  1 
ATOM   1718 C  CZ   . TYR   B 1 146 ? -35.843 5.757  -8.987  1.00 23.95 ? 114 TYR   B CZ   1 
ATOM   1719 O  OH   . TYR   B 1 146 ? -37.040 6.226  -8.502  1.00 28.95 ? 114 TYR   B OH   1 
ATOM   1720 N  N    . SER   B 1 147 ? -29.786 4.622  -13.265 1.00 14.59 ? 115 SER   B N    1 
ATOM   1721 C  CA   A SER   B 1 147 ? -28.352 4.487  -13.466 0.38 13.78 ? 115 SER   B CA   1 
ATOM   1722 C  CA   C SER   B 1 147 ? -28.350 4.520  -13.461 0.62 16.24 ? 115 SER   B CA   1 
ATOM   1723 C  C    . SER   B 1 147 ? -28.028 4.790  -14.917 1.00 14.58 ? 115 SER   B C    1 
ATOM   1724 O  O    . SER   B 1 147 ? -28.852 4.571  -15.802 1.00 16.17 ? 115 SER   B O    1 
ATOM   1725 C  CB   A SER   B 1 147 ? -27.898 3.059  -13.126 0.38 12.27 ? 115 SER   B CB   1 
ATOM   1726 C  CB   C SER   B 1 147 ? -27.840 3.121  -13.096 0.62 19.91 ? 115 SER   B CB   1 
ATOM   1727 O  OG   A SER   B 1 147 ? -26.512 2.894  -13.343 0.38 12.25 ? 115 SER   B OG   1 
ATOM   1728 O  OG   C SER   B 1 147 ? -28.118 2.214  -14.144 0.62 23.59 ? 115 SER   B OG   1 
ATOM   1729 N  N    . TYR   B 1 148 ? -26.818 5.283  -15.153 1.00 14.88 ? 116 TYR   B N    1 
ATOM   1730 C  CA   . TYR   B 1 148 ? -26.307 5.281  -16.512 1.00 14.91 ? 116 TYR   B CA   1 
ATOM   1731 C  C    . TYR   B 1 148 ? -24.809 5.053  -16.473 1.00 13.93 ? 116 TYR   B C    1 
ATOM   1732 O  O    . TYR   B 1 148 ? -24.134 5.359  -15.488 1.00 14.24 ? 116 TYR   B O    1 
ATOM   1733 C  CB   . TYR   B 1 148 ? -26.677 6.512  -17.357 1.00 16.38 ? 116 TYR   B CB   1 
ATOM   1734 C  CG   . TYR   B 1 148 ? -26.035 7.814  -16.932 1.00 18.05 ? 116 TYR   B CG   1 
ATOM   1735 C  CD1  . TYR   B 1 148 ? -24.798 8.209  -17.435 1.00 19.15 ? 116 TYR   B CD1  1 
ATOM   1736 C  CD2  . TYR   B 1 148 ? -26.681 8.663  -16.049 1.00 22.04 ? 116 TYR   B CD2  1 
ATOM   1737 C  CE1  . TYR   B 1 148 ? -24.220 9.413  -17.052 1.00 22.06 ? 116 TYR   B CE1  1 
ATOM   1738 C  CE2  . TYR   B 1 148 ? -26.117 9.865  -15.663 1.00 24.66 ? 116 TYR   B CE2  1 
ATOM   1739 C  CZ   . TYR   B 1 148 ? -24.891 10.234 -16.162 1.00 24.19 ? 116 TYR   B CZ   1 
ATOM   1740 O  OH   . TYR   B 1 148 ? -24.342 11.439 -15.771 1.00 28.93 ? 116 TYR   B OH   1 
ATOM   1741 N  N    . SER   B 1 149 ? -24.316 4.458  -17.543 1.00 15.12 ? 117 SER   B N    1 
ATOM   1742 C  CA   A SER   B 1 149 ? -22.898 4.235  -17.768 0.25 14.45 ? 117 SER   B CA   1 
ATOM   1743 C  CA   B SER   B 1 149 ? -22.895 4.257  -17.758 0.25 14.77 ? 117 SER   B CA   1 
ATOM   1744 C  CA   C SER   B 1 149 ? -22.891 4.283  -17.745 0.50 16.33 ? 117 SER   B CA   1 
ATOM   1745 C  C    . SER   B 1 149 ? -22.516 4.941  -19.059 1.00 14.78 ? 117 SER   B C    1 
ATOM   1746 O  O    . SER   B 1 149 ? -23.291 4.941  -20.016 1.00 16.57 ? 117 SER   B O    1 
ATOM   1747 C  CB   A SER   B 1 149 ? -22.643 2.728  -17.907 0.25 14.02 ? 117 SER   B CB   1 
ATOM   1748 C  CB   B SER   B 1 149 ? -22.569 2.763  -17.849 0.25 14.87 ? 117 SER   B CB   1 
ATOM   1749 C  CB   C SER   B 1 149 ? -22.508 2.804  -17.767 0.50 20.10 ? 117 SER   B CB   1 
ATOM   1750 O  OG   A SER   B 1 149 ? -21.319 2.448  -18.318 0.25 12.91 ? 117 SER   B OG   1 
ATOM   1751 O  OG   B SER   B 1 149 ? -22.963 2.092  -16.666 0.25 14.34 ? 117 SER   B OG   1 
ATOM   1752 O  OG   C SER   B 1 149 ? -23.167 2.144  -18.823 0.50 22.40 ? 117 SER   B OG   1 
ATOM   1753 N  N    . THR   B 1 150 ? -21.337 5.542  -19.089 1.00 13.76 ? 118 THR   B N    1 
ATOM   1754 C  CA   . THR   B 1 150 ? -20.890 6.200  -20.302 1.00 14.22 ? 118 THR   B CA   1 
ATOM   1755 C  C    . THR   B 1 150 ? -19.421 5.893  -20.531 1.00 14.83 ? 118 THR   B C    1 
ATOM   1756 O  O    . THR   B 1 150 ? -18.646 5.780  -19.578 1.00 16.17 ? 118 THR   B O    1 
ATOM   1757 C  CB   . THR   B 1 150 ? -21.174 7.719  -20.260 1.00 14.97 ? 118 THR   B CB   1 
ATOM   1758 O  OG1  . THR   B 1 150 ? -20.860 8.301  -21.527 1.00 17.04 ? 118 THR   B OG1  1 
ATOM   1759 C  CG2  . THR   B 1 150 ? -20.352 8.405  -19.193 1.00 16.83 ? 118 THR   B CG2  1 
ATOM   1760 N  N    . THR   B 1 151 ? -19.046 5.725  -21.793 1.00 14.64 ? 119 THR   B N    1 
ATOM   1761 C  CA   . THR   B 1 151 ? -17.654 5.500  -22.148 1.00 14.61 ? 119 THR   B CA   1 
ATOM   1762 C  C    . THR   B 1 151 ? -17.350 6.280  -23.416 1.00 14.46 ? 119 THR   B C    1 
ATOM   1763 O  O    . THR   B 1 151 ? -18.245 6.808  -24.075 1.00 16.86 ? 119 THR   B O    1 
ATOM   1764 C  CB   . THR   B 1 151 ? -17.345 4.007  -22.311 1.00 16.01 ? 119 THR   B CB   1 
ATOM   1765 O  OG1  . THR   B 1 151 ? -15.919 3.816  -22.334 1.00 17.39 ? 119 THR   B OG1  1 
ATOM   1766 C  CG2  . THR   B 1 151 ? -17.956 3.473  -23.595 1.00 18.19 ? 119 THR   B CG2  1 
ATOM   1767 N  N    . ALA   B 1 152 ? -16.070 6.394  -23.727 1.00 13.59 ? 120 ALA   B N    1 
ATOM   1768 C  CA   . ALA   B 1 152 ? -15.629 7.084  -24.924 1.00 15.49 ? 120 ALA   B CA   1 
ATOM   1769 C  C    . ALA   B 1 152 ? -14.696 6.181  -25.707 1.00 15.65 ? 120 ALA   B C    1 
ATOM   1770 O  O    . ALA   B 1 152 ? -13.892 5.447  -25.125 1.00 16.78 ? 120 ALA   B O    1 
ATOM   1771 C  CB   . ALA   B 1 152 ? -14.894 8.375  -24.566 1.00 17.37 ? 120 ALA   B CB   1 
ATOM   1772 N  N    . VAL   B 1 153 ? -14.812 6.243  -27.029 1.00 16.12 ? 121 VAL   B N    1 
ATOM   1773 C  CA   . VAL   B 1 153 ? -13.845 5.662  -27.948 1.00 17.80 ? 121 VAL   B CA   1 
ATOM   1774 C  C    . VAL   B 1 153 ? -13.237 6.818  -28.727 1.00 19.71 ? 121 VAL   B C    1 
ATOM   1775 O  O    . VAL   B 1 153 ? -13.957 7.558  -29.414 1.00 21.66 ? 121 VAL   B O    1 
ATOM   1776 C  CB   . VAL   B 1 153 ? -14.501 4.653  -28.898 1.00 20.64 ? 121 VAL   B CB   1 
ATOM   1777 C  CG1  . VAL   B 1 153 ? -13.466 4.113  -29.883 1.00 23.18 ? 121 VAL   B CG1  1 
ATOM   1778 C  CG2  . VAL   B 1 153 ? -15.160 3.527  -28.102 1.00 23.02 ? 121 VAL   B CG2  1 
ATOM   1779 N  N    . VAL   B 1 154 ? -11.926 6.995  -28.600 1.00 20.11 ? 122 VAL   B N    1 
ATOM   1780 C  CA   . VAL   B 1 154 ? -11.217 8.108  -29.223 1.00 21.52 ? 122 VAL   B CA   1 
ATOM   1781 C  C    . VAL   B 1 154 ? -10.199 7.534  -30.195 1.00 22.34 ? 122 VAL   B C    1 
ATOM   1782 O  O    . VAL   B 1 154 ? -9.372  6.699  -29.807 1.00 23.74 ? 122 VAL   B O    1 
ATOM   1783 C  CB   . VAL   B 1 154 ? -10.523 8.995  -28.173 1.00 21.75 ? 122 VAL   B CB   1 
ATOM   1784 C  CG1  . VAL   B 1 154 ? -9.823  10.176 -28.846 1.00 23.36 ? 122 VAL   B CG1  1 
ATOM   1785 C  CG2  . VAL   B 1 154 ? -11.529 9.477  -27.144 1.00 22.47 ? 122 VAL   B CG2  1 
ATOM   1786 N  N    . THR   B 1 155 ? -10.257 7.977  -31.454 1.00 24.30 ? 123 THR   B N    1 
ATOM   1787 C  CA   . THR   B 1 155 ? -9.378  7.445  -32.491 1.00 28.87 ? 123 THR   B CA   1 
ATOM   1788 C  C    . THR   B 1 155 ? -8.682  8.575  -33.234 1.00 32.39 ? 123 THR   B C    1 
ATOM   1789 O  O    . THR   B 1 155 ? -9.273  9.629  -33.480 1.00 28.34 ? 123 THR   B O    1 
ATOM   1790 C  CB   . THR   B 1 155 ? -10.140 6.570  -33.501 1.00 33.36 ? 123 THR   B CB   1 
ATOM   1791 O  OG1  . THR   B 1 155 ? -11.104 7.366  -34.197 1.00 36.40 ? 123 THR   B OG1  1 
ATOM   1792 C  CG2  . THR   B 1 155 ? -10.848 5.427  -32.799 1.00 32.37 ? 123 THR   B CG2  1 
ATOM   1793 N  N    . ASN   B 1 156 ? -7.420  8.351  -33.589 1.00 41.52 ? 124 ASN   B N    1 
ATOM   1794 C  CA   . ASN   B 1 156 ? -6.684  9.321  -34.386 1.00 51.70 ? 124 ASN   B CA   1 
ATOM   1795 C  C    . ASN   B 1 156 ? -6.973  9.070  -35.860 1.00 59.92 ? 124 ASN   B C    1 
ATOM   1796 O  O    . ASN   B 1 156 ? -6.702  7.965  -36.350 1.00 60.29 ? 124 ASN   B O    1 
ATOM   1797 C  CB   . ASN   B 1 156 ? -5.194  9.203  -34.125 1.00 53.11 ? 124 ASN   B CB   1 
ATOM   1798 C  CG   . ASN   B 1 156 ? -4.427  10.435 -34.567 1.00 53.67 ? 124 ASN   B CG   1 
ATOM   1799 O  OD1  . ASN   B 1 156 ? -4.664  10.975 -35.648 1.00 53.16 ? 124 ASN   B OD1  1 
ATOM   1800 N  ND2  . ASN   B 1 156 ? -3.511  10.894 -33.724 1.00 54.47 ? 124 ASN   B ND2  1 
ATOM   1801 N  N    . PRO   B 1 157 ? -7.518  10.049 -36.599 1.00 66.73 ? 125 PRO   B N    1 
ATOM   1802 C  CA   . PRO   B 1 157 ? -7.903  9.876  -38.006 1.00 70.51 ? 125 PRO   B CA   1 
ATOM   1803 C  C    . PRO   B 1 157 ? -6.715  9.624  -38.934 1.00 72.62 ? 125 PRO   B C    1 
ATOM   1804 O  O    . PRO   B 1 157 ? -5.569  9.663  -38.487 1.00 73.39 ? 125 PRO   B O    1 
ATOM   1805 C  CB   . PRO   B 1 157 ? -8.570  11.213 -38.351 1.00 71.06 ? 125 PRO   B CB   1 
ATOM   1806 C  CG   . PRO   B 1 157 ? -7.990  12.188 -37.379 1.00 70.65 ? 125 PRO   B CG   1 
ATOM   1807 C  CD   . PRO   B 1 157 ? -7.799  11.411 -36.114 1.00 69.26 ? 125 PRO   B CD   1 
HETATM 1808 C  CAA  . A1L38 C 2 .   ? -22.290 0.463  -3.317  0.50 41.99 ? 201 A1L38 A CAA  1 
HETATM 1809 C  CAB  . A1L38 C 2 .   ? -22.906 0.658  -4.544  0.50 41.84 ? 201 A1L38 A CAB  1 
HETATM 1810 C  CAC  . A1L38 C 2 .   ? -20.926 0.674  -3.208  0.50 43.09 ? 201 A1L38 A CAC  1 
HETATM 1811 C  CAD  . A1L38 C 2 .   ? -22.186 1.050  -5.667  0.50 40.24 ? 201 A1L38 A CAD  1 
HETATM 1812 C  CAE  . A1L38 C 2 .   ? -20.194 1.080  -4.316  0.50 42.79 ? 201 A1L38 A CAE  1 
HETATM 1813 C  CAF  . A1L38 C 2 .   ? -20.817 1.271  -5.545  0.50 41.62 ? 201 A1L38 A CAF  1 
HETATM 1814 C  CAH  . A1L38 C 2 .   ? -22.354 0.336  -7.773  0.50 32.00 ? 201 A1L38 A CAH  1 
HETATM 1815 C  CAI  . A1L38 C 2 .   ? -22.219 -1.004 -7.425  0.50 32.03 ? 201 A1L38 A CAI  1 
HETATM 1816 C  CAJ  . A1L38 C 2 .   ? -22.015 0.794  -9.050  0.50 28.22 ? 201 A1L38 A CAJ  1 
HETATM 1817 C  CAK  . A1L38 C 2 .   ? -21.739 -1.921 -8.347  0.50 32.20 ? 201 A1L38 A CAK  1 
HETATM 1818 C  CAL  . A1L38 C 2 .   ? -21.535 -0.137 -9.955  0.50 29.68 ? 201 A1L38 A CAL  1 
HETATM 1819 C  CAM  . A1L38 C 2 .   ? -21.401 -1.474 -9.614  0.50 31.66 ? 201 A1L38 A CAM  1 
HETATM 1820 N  NAO  . A1L38 C 2 .   ? -21.205 0.264  -11.180 0.50 29.45 ? 201 A1L38 A NAO  1 
HETATM 1821 N  NAP  . A1L38 C 2 .   ? -20.928 -2.306 -10.525 0.50 31.48 ? 201 A1L38 A NAP  1 
HETATM 1822 O  OAG  . A1L38 C 2 .   ? -22.820 1.240  -6.870  0.50 37.12 ? 201 A1L38 A OAG  1 
HETATM 1823 O  OAQ  . A1L38 C 2 .   ? -20.840 -3.591 -10.197 0.50 32.35 ? 201 A1L38 A OAQ  1 
HETATM 1824 O  OAR  . A1L38 C 2 .   ? -20.497 -1.817 -11.681 0.50 34.53 ? 201 A1L38 A OAR  1 
HETATM 1825 CL CLAN . A1L38 C 2 .   ? -22.166 2.454  -9.531  0.50 26.06 ? 201 A1L38 A CLAN 1 
HETATM 1826 NA NA   . NA    D 3 .   ? -44.383 17.171 -4.500  1.00 35.14 ? 202 NA    A NA   1 
HETATM 1827 C  CAA  . A1L38 E 2 .   ? -20.621 1.246  -28.707 0.50 34.88 ? 201 A1L38 B CAA  1 
HETATM 1828 C  CAB  . A1L38 E 2 .   ? -20.198 1.483  -27.409 0.50 35.51 ? 201 A1L38 B CAB  1 
HETATM 1829 C  CAC  . A1L38 E 2 .   ? -21.933 0.855  -28.917 0.50 35.54 ? 201 A1L38 B CAC  1 
HETATM 1830 C  CAD  . A1L38 E 2 .   ? -21.045 1.318  -26.320 0.50 33.11 ? 201 A1L38 B CAD  1 
HETATM 1831 C  CAE  . A1L38 E 2 .   ? -22.806 0.707  -27.847 0.50 36.84 ? 201 A1L38 B CAE  1 
HETATM 1832 C  CAF  . A1L38 E 2 .   ? -22.369 0.948  -26.550 0.50 35.08 ? 201 A1L38 B CAF  1 
HETATM 1833 C  CAH  . A1L38 E 2 .   ? -20.834 0.535  -24.205 0.50 25.52 ? 201 A1L38 B CAH  1 
HETATM 1834 C  CAI  . A1L38 E 2 .   ? -20.697 -0.793 -24.609 0.50 25.24 ? 201 A1L38 B CAI  1 
HETATM 1835 C  CAJ  . A1L38 E 2 .   ? -21.238 0.860  -22.912 0.50 20.39 ? 201 A1L38 B CAJ  1 
HETATM 1836 C  CAK  . A1L38 E 2 .   ? -20.978 -1.827 -23.733 0.50 25.51 ? 201 A1L38 B CAK  1 
HETATM 1837 C  CAL  . A1L38 E 2 .   ? -21.514 -0.189 -22.043 0.50 24.83 ? 201 A1L38 B CAL  1 
HETATM 1838 C  CAM  . A1L38 E 2 .   ? -21.383 -1.512 -22.448 0.50 27.31 ? 201 A1L38 B CAM  1 
HETATM 1839 N  NAO  . A1L38 E 2 .   ? -21.903 0.084  -20.800 0.50 27.18 ? 201 A1L38 B NAO  1 
HETATM 1840 N  NAP  . A1L38 E 2 .   ? -21.668 -2.479 -21.587 0.50 30.15 ? 201 A1L38 B NAP  1 
HETATM 1841 O  OAG  . A1L38 E 2 .   ? -20.571 1.569  -25.053 0.50 26.80 ? 201 A1L38 B OAG  1 
HETATM 1842 O  OAQ  . A1L38 E 2 .   ? -21.406 -3.760 -21.973 0.50 32.10 ? 201 A1L38 B OAQ  1 
HETATM 1843 O  OAR  . A1L38 E 2 .   ? -22.279 -2.178 -20.441 0.50 29.38 ? 201 A1L38 B OAR  1 
HETATM 1844 CL CLAN . A1L38 E 2 .   ? -21.398 2.517  -22.398 0.50 22.39 ? 201 A1L38 B CLAN 1 
HETATM 1845 O  O    . HOH   F 4 .   ? -4.991  17.759 -18.395 1.00 53.51 ? 301 HOH   A O    1 
HETATM 1846 O  O    . HOH   F 4 .   ? -42.908 18.745 -5.766  1.00 38.96 ? 302 HOH   A O    1 
HETATM 1847 O  O    . HOH   F 4 .   ? -11.102 16.263 -20.237 1.00 23.48 ? 303 HOH   A O    1 
HETATM 1848 O  O    . HOH   F 4 .   ? -22.684 13.073 2.486   1.00 24.08 ? 304 HOH   A O    1 
HETATM 1849 O  O    . HOH   F 4 .   ? -0.938  11.887 -21.293 1.00 39.09 ? 305 HOH   A O    1 
HETATM 1850 O  O    . HOH   F 4 .   ? -22.295 27.851 -8.635  1.00 46.29 ? 306 HOH   A O    1 
HETATM 1851 O  O    . HOH   F 4 .   ? -13.324 21.539 -16.265 1.00 45.33 ? 307 HOH   A O    1 
HETATM 1852 O  O    . HOH   F 4 .   ? -34.957 16.413 3.391   0.50 45.23 ? 308 HOH   A O    1 
HETATM 1853 O  O    . HOH   F 4 .   ? -12.357 18.531 -12.896 1.00 50.31 ? 309 HOH   A O    1 
HETATM 1854 O  O    . HOH   F 4 .   ? -5.027  -2.931 -12.244 1.00 44.85 ? 310 HOH   A O    1 
HETATM 1855 O  O    . HOH   F 4 .   ? -24.604 24.352 5.517   1.00 42.83 ? 311 HOH   A O    1 
HETATM 1856 O  O    . HOH   F 4 .   ? -26.387 8.417  -10.141 1.00 23.18 ? 312 HOH   A O    1 
HETATM 1857 O  O    . HOH   F 4 .   ? -17.590 24.505 -0.821  1.00 41.00 ? 313 HOH   A O    1 
HETATM 1858 O  O    . HOH   F 4 .   ? -36.717 10.949 -5.206  1.00 26.59 ? 314 HOH   A O    1 
HETATM 1859 O  O    . HOH   F 4 .   ? -31.348 21.019 -14.650 1.00 56.04 ? 315 HOH   A O    1 
HETATM 1860 O  O    . HOH   F 4 .   ? -12.007 11.973 -15.420 1.00 15.33 ? 316 HOH   A O    1 
HETATM 1861 O  O    . HOH   F 4 .   ? -5.061  8.075  -21.179 1.00 47.31 ? 317 HOH   A O    1 
HETATM 1862 O  O    . HOH   F 4 .   ? -14.841 12.142 3.974   1.00 27.73 ? 318 HOH   A O    1 
HETATM 1863 O  O    . HOH   F 4 .   ? -36.748 26.317 -3.324  1.00 22.09 ? 319 HOH   A O    1 
HETATM 1864 O  O    . HOH   F 4 .   ? -39.280 12.433 -2.652  1.00 28.61 ? 320 HOH   A O    1 
HETATM 1865 O  O    . HOH   F 4 .   ? -39.934 10.267 4.281   1.00 44.80 ? 321 HOH   A O    1 
HETATM 1866 O  O    . HOH   F 4 .   ? -37.839 18.832 -10.844 1.00 36.43 ? 322 HOH   A O    1 
HETATM 1867 O  O    . HOH   F 4 .   ? -33.884 13.732 3.314   1.00 34.73 ? 323 HOH   A O    1 
HETATM 1868 O  O    . HOH   F 4 .   ? -28.091 24.834 6.504   1.00 50.96 ? 324 HOH   A O    1 
HETATM 1869 O  O    . HOH   F 4 .   ? -35.014 11.929 -8.976  1.00 22.17 ? 325 HOH   A O    1 
HETATM 1870 O  O    . HOH   F 4 .   ? -19.292 23.773 -11.972 1.00 43.01 ? 326 HOH   A O    1 
HETATM 1871 O  O    . HOH   F 4 .   ? -33.890 23.465 -7.185  1.00 26.20 ? 327 HOH   A O    1 
HETATM 1872 O  O    . HOH   F 4 .   ? -19.002 13.805 -17.580 1.00 19.14 ? 328 HOH   A O    1 
HETATM 1873 O  O    . HOH   F 4 .   ? -12.794 9.964  -17.160 1.00 15.86 ? 329 HOH   A O    1 
HETATM 1874 O  O    . HOH   F 4 .   ? -26.074 24.690 1.780   1.00 36.56 ? 330 HOH   A O    1 
HETATM 1875 O  O    . HOH   F 4 .   ? -34.430 1.619  -1.607  1.00 40.39 ? 331 HOH   A O    1 
HETATM 1876 O  O    . HOH   F 4 .   ? -30.287 26.694 -4.671  1.00 26.72 ? 332 HOH   A O    1 
HETATM 1877 O  O    . HOH   F 4 .   ? -6.476  9.031  -4.582  1.00 39.47 ? 333 HOH   A O    1 
HETATM 1878 O  O    . HOH   F 4 .   ? -8.870  15.815 -3.739  1.00 27.94 ? 334 HOH   A O    1 
HETATM 1879 O  O    . HOH   F 4 .   ? -33.515 30.570 -5.237  1.00 38.66 ? 335 HOH   A O    1 
HETATM 1880 O  O    . HOH   F 4 .   ? -7.991  5.514  -4.344  1.00 26.85 ? 336 HOH   A O    1 
HETATM 1881 O  O    . HOH   F 4 .   ? -29.221 1.352  -7.729  1.00 21.14 ? 337 HOH   A O    1 
HETATM 1882 O  O    . HOH   F 4 .   ? -15.321 0.822  0.901   1.00 48.67 ? 338 HOH   A O    1 
HETATM 1883 O  O    . HOH   F 4 .   ? -27.843 26.363 4.282   1.00 53.73 ? 339 HOH   A O    1 
HETATM 1884 O  O    . HOH   F 4 .   ? -22.044 24.528 -11.694 1.00 42.79 ? 340 HOH   A O    1 
HETATM 1885 O  O    . HOH   F 4 .   ? -13.636 8.369  -14.323 1.00 15.81 ? 341 HOH   A O    1 
HETATM 1886 O  O    . HOH   F 4 .   ? -7.139  8.961  -26.377 1.00 47.12 ? 342 HOH   A O    1 
HETATM 1887 O  O    . HOH   F 4 .   ? -4.161  15.645 -9.671  1.00 33.59 ? 343 HOH   A O    1 
HETATM 1888 O  O    . HOH   F 4 .   ? -10.561 14.644 -6.853  1.00 17.35 ? 344 HOH   A O    1 
HETATM 1889 O  O    . HOH   F 4 .   ? -4.678  -2.920 -7.637  1.00 54.69 ? 345 HOH   A O    1 
HETATM 1890 O  O    . HOH   F 4 .   ? -35.196 26.758 -10.988 1.00 57.69 ? 346 HOH   A O    1 
HETATM 1891 O  O    . HOH   F 4 .   ? -35.044 26.768 -6.877  1.00 46.71 ? 347 HOH   A O    1 
HETATM 1892 O  O    . HOH   F 4 .   ? -15.387 10.512 -14.822 1.00 22.20 ? 348 HOH   A O    1 
HETATM 1893 O  O    . HOH   F 4 .   ? -8.377  12.962 -6.133  1.00 27.07 ? 349 HOH   A O    1 
HETATM 1894 O  O    . HOH   F 4 .   ? -20.733 23.621 -3.834  1.00 23.24 ? 350 HOH   A O    1 
HETATM 1895 O  O    . HOH   F 4 .   ? -10.060 19.045 -12.093 1.00 49.21 ? 351 HOH   A O    1 
HETATM 1896 O  O    . HOH   F 4 .   ? -19.158 16.379 4.902   1.00 45.17 ? 352 HOH   A O    1 
HETATM 1897 O  O    . HOH   F 4 .   ? -16.036 2.378  -14.739 1.00 25.78 ? 353 HOH   A O    1 
HETATM 1898 O  O    . HOH   F 4 .   ? -28.026 13.811 9.050   1.00 66.29 ? 354 HOH   A O    1 
HETATM 1899 O  O    . HOH   F 4 .   ? -44.044 19.021 -3.152  1.00 33.82 ? 355 HOH   A O    1 
HETATM 1900 O  O    . HOH   F 4 .   ? -21.308 3.207  5.215   1.00 55.06 ? 356 HOH   A O    1 
HETATM 1901 O  O    . HOH   F 4 .   ? -25.817 13.884 4.463   1.00 24.40 ? 357 HOH   A O    1 
HETATM 1902 O  O    . HOH   F 4 .   ? -17.136 11.031 5.060   1.00 27.58 ? 358 HOH   A O    1 
HETATM 1903 O  O    . HOH   F 4 .   ? -30.295 5.455  0.280   1.00 31.32 ? 359 HOH   A O    1 
HETATM 1904 O  O    . HOH   F 4 .   ? -15.673 18.825 -8.831  1.00 24.89 ? 360 HOH   A O    1 
HETATM 1905 O  O    . HOH   F 4 .   ? -37.813 2.863  0.467   1.00 49.76 ? 361 HOH   A O    1 
HETATM 1906 O  O    . HOH   F 4 .   ? -35.101 25.705 -17.190 1.00 61.07 ? 362 HOH   A O    1 
HETATM 1907 O  O    . HOH   F 4 .   ? -27.758 8.289  2.476   1.00 43.10 ? 363 HOH   A O    1 
HETATM 1908 O  O    . HOH   F 4 .   ? -37.536 13.357 -6.380  1.00 31.95 ? 364 HOH   A O    1 
HETATM 1909 O  O    . HOH   F 4 .   ? -24.891 28.594 -12.873 1.00 41.68 ? 365 HOH   A O    1 
HETATM 1910 O  O    . HOH   F 4 .   ? -36.883 14.822 7.513   1.00 45.18 ? 366 HOH   A O    1 
HETATM 1911 O  O    . HOH   F 4 .   ? -5.667  10.160 -6.800  1.00 35.64 ? 367 HOH   A O    1 
HETATM 1912 O  O    . HOH   F 4 .   ? -6.996  18.114 -12.708 1.00 33.44 ? 368 HOH   A O    1 
HETATM 1913 O  O    . HOH   F 4 .   ? -24.019 18.802 7.308   1.00 44.53 ? 369 HOH   A O    1 
HETATM 1914 O  O    . HOH   F 4 .   ? -24.949 15.703 8.766   1.00 58.09 ? 370 HOH   A O    1 
HETATM 1915 O  O    . HOH   F 4 .   ? -23.085 26.611 0.243   1.00 51.95 ? 371 HOH   A O    1 
HETATM 1916 O  O    . HOH   F 4 .   ? 0.939   13.513 -11.609 1.00 48.75 ? 372 HOH   A O    1 
HETATM 1917 O  O    . HOH   F 4 .   ? -9.264  17.127 -6.334  1.00 38.16 ? 373 HOH   A O    1 
HETATM 1918 O  O    . HOH   F 4 .   ? -38.820 7.336  -3.676  1.00 48.51 ? 374 HOH   A O    1 
HETATM 1919 O  O    . HOH   F 4 .   ? -6.767  16.223 2.062   1.00 37.86 ? 375 HOH   A O    1 
HETATM 1920 O  O    . HOH   F 4 .   ? -42.884 11.168 2.402   1.00 46.86 ? 376 HOH   A O    1 
HETATM 1921 O  O    . HOH   F 4 .   ? -13.536 5.421  6.091   1.00 51.42 ? 377 HOH   A O    1 
HETATM 1922 O  O    . HOH   F 4 .   ? -16.640 -0.994 -0.875  1.00 44.43 ? 378 HOH   A O    1 
HETATM 1923 O  O    . HOH   F 4 .   ? -9.426  21.854 -18.351 1.00 47.23 ? 379 HOH   A O    1 
HETATM 1924 O  O    . HOH   F 4 .   ? -6.443  3.486  -3.091  1.00 52.13 ? 380 HOH   A O    1 
HETATM 1925 O  O    . HOH   F 4 .   ? -15.029 25.281 -2.368  0.50 35.40 ? 381 HOH   A O    1 
HETATM 1926 O  O    . HOH   F 4 .   ? -38.033 5.261  -2.085  1.00 48.56 ? 382 HOH   A O    1 
HETATM 1927 O  O    . HOH   F 4 .   ? -45.749 15.932 -2.917  1.00 42.21 ? 383 HOH   A O    1 
HETATM 1928 O  O    . HOH   F 4 .   ? -20.265 24.397 -1.305  1.00 34.78 ? 384 HOH   A O    1 
HETATM 1929 O  O    . HOH   F 4 .   ? -38.519 20.621 -6.751  1.00 47.67 ? 385 HOH   A O    1 
HETATM 1930 O  O    . HOH   F 4 .   ? -39.097 10.138 -4.251  1.00 31.82 ? 386 HOH   A O    1 
HETATM 1931 O  O    . HOH   F 4 .   ? -4.812  17.870 -11.209 1.00 54.07 ? 387 HOH   A O    1 
HETATM 1932 O  O    . HOH   F 4 .   ? -2.409  11.022 -22.985 1.00 48.07 ? 388 HOH   A O    1 
HETATM 1933 O  O    . HOH   F 4 .   ? -36.478 24.121 -7.007  1.00 48.07 ? 389 HOH   A O    1 
HETATM 1934 O  O    . HOH   F 4 .   ? -1.510  15.504 -10.375 1.00 44.18 ? 390 HOH   A O    1 
HETATM 1935 O  O    . HOH   F 4 .   ? -16.094 23.544 -8.456  1.00 49.49 ? 391 HOH   A O    1 
HETATM 1936 O  O    . HOH   F 4 .   ? -20.867 24.978 0.806   1.00 46.03 ? 392 HOH   A O    1 
HETATM 1937 O  O    . HOH   F 4 .   ? -14.703 19.067 -11.167 1.00 36.20 ? 393 HOH   A O    1 
HETATM 1938 O  O    . HOH   F 4 .   ? -16.696 8.821  6.468   1.00 56.48 ? 394 HOH   A O    1 
HETATM 1939 O  O    . HOH   F 4 .   ? -17.569 25.515 -7.035  1.00 44.66 ? 395 HOH   A O    1 
HETATM 1940 O  O    . HOH   F 4 .   ? -0.644  16.280 -13.015 1.00 47.38 ? 396 HOH   A O    1 
HETATM 1941 O  O    . HOH   F 4 .   ? -18.135 25.343 -10.285 1.00 49.35 ? 397 HOH   A O    1 
HETATM 1942 O  O    . HOH   F 4 .   ? -2.961  10.340 -5.133  1.00 49.76 ? 398 HOH   A O    1 
HETATM 1943 O  O    . HOH   F 4 .   ? -20.020 28.145 -6.998  1.00 46.87 ? 399 HOH   A O    1 
HETATM 1944 O  O    . HOH   F 4 .   ? -45.847 20.936 -4.144  1.00 42.57 ? 400 HOH   A O    1 
HETATM 1945 O  O    . HOH   F 4 .   ? -13.119 -0.572 1.386   1.00 53.88 ? 401 HOH   A O    1 
HETATM 1946 O  O    . HOH   F 4 .   ? -37.879 21.366 -9.634  1.00 45.39 ? 402 HOH   A O    1 
HETATM 1947 O  O    . HOH   G 4 .   ? -35.264 8.731  -34.265 1.00 39.55 ? 301 HOH   B O    1 
HETATM 1948 O  O    . HOH   G 4 .   ? -17.311 23.019 -42.003 1.00 58.77 ? 302 HOH   B O    1 
HETATM 1949 O  O    . HOH   G 4 .   ? -6.907  22.258 -23.699 1.00 51.04 ? 303 HOH   B O    1 
HETATM 1950 O  O    . HOH   G 4 .   ? -15.118 23.926 -31.992 1.00 42.60 ? 304 HOH   B O    1 
HETATM 1951 O  O    . HOH   G 4 .   ? -36.063 16.318 -24.962 1.00 30.45 ? 305 HOH   B O    1 
HETATM 1952 O  O    . HOH   G 4 .   ? -21.718 21.563 -38.539 1.00 43.71 ? 306 HOH   B O    1 
HETATM 1953 O  O    . HOH   G 4 .   ? -9.946  24.024 -22.640 1.00 46.65 ? 307 HOH   B O    1 
HETATM 1954 O  O    . HOH   G 4 .   ? -8.808  13.843 -26.762 1.00 27.56 ? 308 HOH   B O    1 
HETATM 1955 O  O    . HOH   G 4 .   ? -7.528  17.026 -41.911 1.00 45.81 ? 309 HOH   B O    1 
HETATM 1956 O  O    . HOH   G 4 .   ? -34.870 13.997 -11.587 1.00 21.10 ? 310 HOH   B O    1 
HETATM 1957 O  O    . HOH   G 4 .   ? -18.446 9.203  -22.050 1.00 19.48 ? 311 HOH   B O    1 
HETATM 1958 O  O    . HOH   G 4 .   ? -28.259 23.227 -20.519 1.00 44.56 ? 312 HOH   B O    1 
HETATM 1959 O  O    . HOH   G 4 .   ? -25.365 1.728  -15.648 1.00 41.99 ? 313 HOH   B O    1 
HETATM 1960 O  O    . HOH   G 4 .   ? -19.887 22.375 -35.635 1.00 29.40 ? 314 HOH   B O    1 
HETATM 1961 O  O    . HOH   G 4 .   ? -27.316 15.107 -37.367 1.00 32.66 ? 315 HOH   B O    1 
HETATM 1962 O  O    . HOH   G 4 .   ? -39.432 4.495  -11.264 1.00 48.69 ? 316 HOH   B O    1 
HETATM 1963 O  O    . HOH   G 4 .   ? -10.486 14.218 -22.975 1.00 23.61 ? 317 HOH   B O    1 
HETATM 1964 O  O    . HOH   G 4 .   ? -39.876 16.467 -22.740 1.00 43.42 ? 318 HOH   B O    1 
HETATM 1965 O  O    . HOH   G 4 .   ? -33.638 19.793 -15.399 1.00 44.36 ? 319 HOH   B O    1 
HETATM 1966 O  O    . HOH   G 4 .   ? -41.273 15.693 -17.375 1.00 54.57 ? 320 HOH   B O    1 
HETATM 1967 O  O    . HOH   G 4 .   ? -4.247  22.374 -28.798 1.00 32.48 ? 321 HOH   B O    1 
HETATM 1968 O  O    . HOH   G 4 .   ? -3.050  22.263 -25.936 1.00 43.35 ? 322 HOH   B O    1 
HETATM 1969 O  O    . HOH   G 4 .   ? -33.219 10.136 -16.626 1.00 15.37 ? 323 HOH   B O    1 
HETATM 1970 O  O    . HOH   G 4 .   ? -37.921 6.185  -27.567 1.00 37.46 ? 324 HOH   B O    1 
HETATM 1971 O  O    . HOH   G 4 .   ? -34.602 0.158  -33.326 1.00 47.84 ? 325 HOH   B O    1 
HETATM 1972 O  O    . HOH   G 4 .   ? -11.684 17.853 -35.012 1.00 26.50 ? 326 HOH   B O    1 
HETATM 1973 O  O    . HOH   G 4 .   ? -26.770 13.139 -14.369 1.00 17.28 ? 327 HOH   B O    1 
HETATM 1974 O  O    . HOH   G 4 .   ? -36.717 10.547 -25.920 1.00 31.30 ? 328 HOH   B O    1 
HETATM 1975 O  O    . HOH   G 4 .   ? -29.729 20.352 -22.983 1.00 27.62 ? 329 HOH   B O    1 
HETATM 1976 O  O    . HOH   G 4 .   ? -1.889  19.832 -26.374 1.00 32.50 ? 330 HOH   B O    1 
HETATM 1977 O  O    . HOH   G 4 .   ? -32.033 8.210  -14.988 1.00 18.40 ? 331 HOH   B O    1 
HETATM 1978 O  O    . HOH   G 4 .   ? -10.178 20.111 -40.668 1.00 44.47 ? 332 HOH   B O    1 
HETATM 1979 O  O    . HOH   G 4 .   ? -9.262  21.529 -21.132 1.00 29.20 ? 333 HOH   B O    1 
HETATM 1980 O  O    . HOH   G 4 .   ? -10.234 24.235 -37.751 1.00 18.99 ? 334 HOH   B O    1 
HETATM 1981 O  O    . HOH   G 4 .   ? -39.727 6.782  -29.916 1.00 48.26 ? 335 HOH   B O    1 
HETATM 1982 O  O    . HOH   G 4 .   ? -36.946 13.275 -28.602 1.00 34.09 ? 336 HOH   B O    1 
HETATM 1983 O  O    . HOH   G 4 .   ? -12.293 15.447 -35.708 1.00 27.99 ? 337 HOH   B O    1 
HETATM 1984 O  O    . HOH   G 4 .   ? -16.022 22.003 -17.076 1.00 44.77 ? 338 HOH   B O    1 
HETATM 1985 O  O    . HOH   G 4 .   ? -14.357 2.684  -24.301 1.00 19.03 ? 339 HOH   B O    1 
HETATM 1986 O  O    . HOH   G 4 .   ? -22.304 3.367  -36.897 1.00 49.98 ? 340 HOH   B O    1 
HETATM 1987 O  O    . HOH   G 4 .   ? -45.818 8.153  -19.446 1.00 45.18 ? 341 HOH   B O    1 
HETATM 1988 O  O    . HOH   G 4 .   ? -13.732 25.316 -24.267 1.00 26.96 ? 342 HOH   B O    1 
HETATM 1989 O  O    . HOH   G 4 .   ? -30.922 6.845  -17.697 1.00 15.74 ? 343 HOH   B O    1 
HETATM 1990 O  O    . HOH   G 4 .   ? -30.108 10.991 -35.948 1.00 28.44 ? 344 HOH   B O    1 
HETATM 1991 O  O    . HOH   G 4 .   ? -19.896 14.757 -36.106 1.00 24.34 ? 345 HOH   B O    1 
HETATM 1992 O  O    . HOH   G 4 .   ? -41.375 12.394 -22.421 1.00 36.25 ? 346 HOH   B O    1 
HETATM 1993 O  O    . HOH   G 4 .   ? -34.959 12.478 -25.081 1.00 19.00 ? 347 HOH   B O    1 
HETATM 1994 O  O    . HOH   G 4 .   ? -21.566 25.302 -33.708 1.00 32.89 ? 348 HOH   B O    1 
HETATM 1995 O  O    . HOH   G 4 .   ? -6.780  15.817 -29.290 1.00 22.51 ? 349 HOH   B O    1 
HETATM 1996 O  O    . HOH   G 4 .   ? -22.471 21.850 -34.970 1.00 36.91 ? 350 HOH   B O    1 
HETATM 1997 O  O    . HOH   G 4 .   ? -16.894 9.213  -34.360 1.00 43.50 ? 351 HOH   B O    1 
HETATM 1998 O  O    . HOH   G 4 .   ? -15.991 26.169 -33.732 1.00 52.27 ? 352 HOH   B O    1 
HETATM 1999 O  O    . HOH   G 4 .   ? -38.504 15.362 -32.419 1.00 53.15 ? 353 HOH   B O    1 
HETATM 2000 O  O    . HOH   G 4 .   ? -6.825  25.696 -27.846 1.00 41.81 ? 354 HOH   B O    1 
HETATM 2001 O  O    . HOH   G 4 .   ? -11.944 29.141 -27.017 1.00 46.25 ? 355 HOH   B O    1 
HETATM 2002 O  O    . HOH   G 4 .   ? -27.719 10.414 -37.002 1.00 31.44 ? 356 HOH   B O    1 
HETATM 2003 O  O    . HOH   G 4 .   ? -31.000 20.368 -19.575 1.00 49.99 ? 357 HOH   B O    1 
HETATM 2004 O  O    . HOH   G 4 .   ? -41.989 4.243  -12.823 1.00 46.29 ? 358 HOH   B O    1 
HETATM 2005 O  O    . HOH   G 4 .   ? -29.586 9.235  -17.206 1.00 25.54 ? 359 HOH   B O    1 
HETATM 2006 O  O    . HOH   G 4 .   ? -35.160 -6.146 -27.323 1.00 30.35 ? 360 HOH   B O    1 
HETATM 2007 O  O    . HOH   G 4 .   ? -33.878 6.604  -37.739 1.00 30.41 ? 361 HOH   B O    1 
HETATM 2008 O  O    . HOH   G 4 .   ? -27.393 1.272  -17.394 1.00 24.15 ? 362 HOH   B O    1 
HETATM 2009 O  O    . HOH   G 4 .   ? -30.693 17.810 -23.344 1.00 19.95 ? 363 HOH   B O    1 
HETATM 2010 O  O    . HOH   G 4 .   ? -17.126 4.027  -32.702 1.00 49.10 ? 364 HOH   B O    1 
HETATM 2011 O  O    . HOH   G 4 .   ? -27.827 5.953  -37.554 1.00 49.38 ? 365 HOH   B O    1 
HETATM 2012 O  O    . HOH   G 4 .   ? -6.385  5.691  -33.042 1.00 46.58 ? 366 HOH   B O    1 
HETATM 2013 O  O    . HOH   G 4 .   ? -15.631 16.410 -41.075 1.00 34.25 ? 367 HOH   B O    1 
HETATM 2014 O  O    . HOH   G 4 .   ? -37.842 -5.111 -19.214 1.00 47.41 ? 368 HOH   B O    1 
HETATM 2015 O  O    . HOH   G 4 .   ? -22.744 27.974 -32.147 1.00 36.62 ? 369 HOH   B O    1 
HETATM 2016 O  O    . HOH   G 4 .   ? -10.960 26.299 -24.755 1.00 50.59 ? 370 HOH   B O    1 
HETATM 2017 O  O    . HOH   G 4 .   ? -35.867 3.091  -27.829 1.00 25.66 ? 371 HOH   B O    1 
HETATM 2018 O  O    . HOH   G 4 .   ? -14.006 6.984  -32.311 1.00 32.98 ? 372 HOH   B O    1 
HETATM 2019 O  O    . HOH   G 4 .   ? -38.931 7.159  -25.251 1.00 30.77 ? 373 HOH   B O    1 
HETATM 2020 O  O    . HOH   G 4 .   ? -31.150 14.907 -35.190 1.00 26.85 ? 374 HOH   B O    1 
HETATM 2021 O  O    . HOH   G 4 .   ? -38.854 15.300 -19.162 1.00 53.82 ? 375 HOH   B O    1 
HETATM 2022 O  O    . HOH   G 4 .   ? -37.687 -5.959 -24.383 1.00 50.19 ? 376 HOH   B O    1 
HETATM 2023 O  O    . HOH   G 4 .   ? -19.907 27.064 -29.827 1.00 43.81 ? 377 HOH   B O    1 
HETATM 2024 O  O    . HOH   G 4 .   ? -22.330 18.942 -39.122 1.00 46.32 ? 378 HOH   B O    1 
HETATM 2025 O  O    . HOH   G 4 .   ? -23.916 28.511 -19.057 1.00 43.82 ? 379 HOH   B O    1 
HETATM 2026 O  O    . HOH   G 4 .   ? -17.719 28.175 -26.806 1.00 38.07 ? 380 HOH   B O    1 
HETATM 2027 O  O    . HOH   G 4 .   ? -37.451 19.262 -13.634 1.00 46.36 ? 381 HOH   B O    1 
HETATM 2028 O  O    . HOH   G 4 .   ? -15.226 32.108 -25.929 1.00 53.26 ? 382 HOH   B O    1 
HETATM 2029 O  O    . HOH   G 4 .   ? -25.918 24.357 -20.532 1.00 41.98 ? 383 HOH   B O    1 
HETATM 2030 O  O    . HOH   G 4 .   ? -22.487 24.627 -36.886 1.00 47.73 ? 384 HOH   B O    1 
HETATM 2031 O  O    . HOH   G 4 .   ? -5.950  10.518 -28.222 1.00 51.44 ? 385 HOH   B O    1 
HETATM 2032 O  O    . HOH   G 4 .   ? -37.717 6.052  -5.314  1.00 52.55 ? 386 HOH   B O    1 
HETATM 2033 O  O    . HOH   G 4 .   ? -18.121 7.427  -36.134 1.00 52.14 ? 387 HOH   B O    1 
HETATM 2034 O  O    . HOH   G 4 .   ? -19.505 25.150 -34.954 1.00 51.53 ? 388 HOH   B O    1 
HETATM 2035 O  O    . HOH   G 4 .   ? -6.254  13.450 -27.727 1.00 26.44 ? 389 HOH   B O    1 
HETATM 2036 O  O    . HOH   G 4 .   ? -41.481 14.710 -20.878 1.00 52.42 ? 390 HOH   B O    1 
HETATM 2037 O  O    . HOH   G 4 .   ? -27.814 11.818 -39.456 1.00 49.93 ? 391 HOH   B O    1 
HETATM 2038 O  O    . HOH   G 4 .   ? -17.114 30.627 -27.497 1.00 54.60 ? 392 HOH   B O    1 
HETATM 2039 O  O    . HOH   G 4 .   ? -35.508 9.733  -7.289  1.00 31.97 ? 393 HOH   B O    1 
HETATM 2040 O  O    . HOH   G 4 .   ? -11.836 25.855 -22.369 1.00 52.76 ? 394 HOH   B O    1 
HETATM 2041 O  O    . HOH   G 4 .   ? -31.537 17.768 -20.874 1.00 33.34 ? 395 HOH   B O    1 
HETATM 2042 O  O    . HOH   G 4 .   ? -9.589  12.292 -24.857 1.00 37.99 ? 396 HOH   B O    1 
HETATM 2043 O  O    . HOH   G 4 .   ? -29.853 13.548 -37.142 1.00 43.15 ? 397 HOH   B O    1 
HETATM 2044 O  O    . HOH   G 4 .   ? -32.260 10.218 -37.694 1.00 48.73 ? 398 HOH   B O    1 
HETATM 2045 O  O    . HOH   G 4 .   ? -17.601 1.932  -31.209 1.00 53.22 ? 399 HOH   B O    1 
HETATM 2046 O  O    . HOH   G 4 .   ? -30.686 8.847  -39.774 1.00 49.29 ? 400 HOH   B O    1 
HETATM 2047 O  O    . HOH   G 4 .   ? -39.592 -3.406 -17.736 1.00 44.18 ? 401 HOH   B O    1 
HETATM 2048 O  O    . HOH   G 4 .   ? -40.271 -2.207 -20.004 1.00 52.94 ? 402 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  ? 0.6416 0.5802 0.5349 0.0103  0.1020  0.0358  10  CYS A N   
2    C  CA  . CYS A 42  ? 0.6004 0.5656 0.5223 0.0101  0.1241  0.0236  10  CYS A CA  
3    C  C   . CYS A 42  ? 0.4594 0.4705 0.4714 0.0182  0.1501  0.0021  10  CYS A C   
4    O  O   . CYS A 42  ? 0.4552 0.4667 0.4951 0.0414  0.1755  0.0223  10  CYS A O   
5    C  CB  . CYS A 42  ? 0.7100 0.6164 0.5568 0.0097  0.1252  0.0307  10  CYS A CB  
6    S  SG  . CYS A 42  ? 0.8054 0.6277 0.5837 -0.0004 0.1208  0.0374  10  CYS A SG  
7    N  N   . PRO A 43  ? 0.3517 0.3676 0.3943 0.0135  0.1432  -0.0274 11  PRO A N   
8    C  CA  . PRO A 43  ? 0.3169 0.3235 0.3346 0.0051  0.0890  -0.0554 11  PRO A CA  
9    C  C   . PRO A 43  ? 0.2175 0.2916 0.2845 0.0120  0.0673  -0.1054 11  PRO A C   
10   O  O   . PRO A 43  ? 0.2546 0.3102 0.2949 -0.0247 0.0345  -0.1144 11  PRO A O   
11   C  CB  . PRO A 43  ? 0.3812 0.3570 0.3560 0.0364  0.0710  -0.0568 11  PRO A CB  
12   C  CG  . PRO A 43  ? 0.4052 0.3418 0.3845 0.0006  0.0667  -0.0597 11  PRO A CG  
13   C  CD  . PRO A 43  ? 0.4017 0.3541 0.3782 -0.0157 0.0854  -0.0542 11  PRO A CD  
14   N  N   . LEU A 44  ? 0.2017 0.2690 0.2521 0.0138  0.0419  -0.0999 12  LEU A N   
15   C  CA  . LEU A 44  ? 0.2012 0.2615 0.2410 0.0098  0.0528  -0.0699 12  LEU A CA  
16   C  C   . LEU A 44  ? 0.2067 0.2752 0.2395 0.0031  0.0672  -0.0969 12  LEU A C   
17   O  O   . LEU A 44  ? 0.2558 0.3140 0.2818 0.0104  0.0138  -0.1246 12  LEU A O   
18   C  CB  . LEU A 44  ? 0.2459 0.2491 0.2219 -0.0330 0.0379  -0.0477 12  LEU A CB  
19   C  CG  . LEU A 44  ? 0.2918 0.2486 0.2414 -0.0222 0.0237  -0.0470 12  LEU A CG  
20   C  CD1 . LEU A 44  ? 0.2981 0.2563 0.2292 -0.0076 0.0021  -0.0410 12  LEU A CD1 
21   C  CD2 . LEU A 44  ? 0.3025 0.2431 0.2646 -0.0130 0.0119  -0.0287 12  LEU A CD2 
22   N  N   . MET A 45  ? 0.1914 0.2429 0.2125 0.0034  0.0413  -0.0524 13  MET A N   
23   C  CA  . MET A 45  ? 0.1736 0.2492 0.2161 0.0135  0.0638  -0.0398 13  MET A CA  
24   C  C   . MET A 45  ? 0.1710 0.2313 0.1903 0.0140  0.0247  -0.0525 13  MET A C   
25   O  O   . MET A 45  ? 0.1911 0.2723 0.1791 -0.0041 -0.0031 -0.0478 13  MET A O   
26   C  CB  . MET A 45  ? 0.2247 0.2830 0.2540 0.0272  0.0545  0.0027  13  MET A CB  
27   C  CG  . MET A 45  ? 0.3180 0.2945 0.2973 0.0279  0.0534  -0.0167 13  MET A CG  
28   S  SD  . MET A 45  ? 0.3978 0.3181 0.3583 0.0088  0.0359  0.0029  13  MET A SD  
29   C  CE  . MET A 45  ? 0.4457 0.3099 0.3976 -0.0015 0.0345  0.0361  13  MET A CE  
30   N  N   . VAL A 46  ? 0.1924 0.2049 0.1704 0.0411  0.0215  -0.0284 14  VAL A N   
31   C  CA  . VAL A 46  ? 0.1847 0.2065 0.1585 0.0144  0.0196  -0.0314 14  VAL A CA  
32   C  C   . VAL A 46  ? 0.1910 0.2140 0.1710 0.0043  -0.0137 -0.0365 14  VAL A C   
33   O  O   . VAL A 46  ? 0.2118 0.2454 0.1847 0.0199  -0.0342 -0.0574 14  VAL A O   
34   C  CB  . VAL A 46  ? 0.2139 0.2003 0.1650 0.0068  -0.0033 -0.0156 14  VAL A CB  
35   C  CG1 . VAL A 46  ? 0.2347 0.2229 0.1746 -0.0013 0.0278  -0.0081 14  VAL A CG1 
36   C  CG2 . VAL A 46  ? 0.2115 0.2149 0.2197 0.0303  -0.0060 -0.0082 14  VAL A CG2 
37   N  N   . LYS A 47  ? 0.1877 0.2077 0.1727 0.0190  0.0193  -0.0239 15  LYS A N   
38   C  CA  . LYS A 47  ? 0.2079 0.2081 0.1880 0.0317  0.0044  -0.0210 15  LYS A CA  
39   C  C   . LYS A 47  ? 0.1899 0.2237 0.1691 0.0390  0.0082  -0.0290 15  LYS A C   
40   O  O   . LYS A 47  ? 0.1991 0.2630 0.1693 0.0229  -0.0168 -0.0302 15  LYS A O   
41   C  CB  . LYS A 47  ? 0.2897 0.2245 0.2361 0.0248  0.0239  0.0072  15  LYS A CB  
42   C  CG  . LYS A 47  ? 0.3963 0.2548 0.3184 0.0324  0.0529  0.0335  15  LYS A CG  
43   C  CD  . LYS A 47  ? 0.4927 0.2889 0.3614 0.0355  0.0584  0.0555  15  LYS A CD  
44   C  CE  . LYS A 47  ? 0.5475 0.3154 0.3811 0.0405  0.0668  0.0789  15  LYS A CE  
45   N  NZ  . LYS A 47  ? 0.6130 0.3698 0.4225 0.0386  0.0600  0.0505  15  LYS A NZ  
46   N  N   . VAL A 48  ? 0.1781 0.2000 0.1665 0.0430  0.0131  -0.0195 16  VAL A N   
47   C  CA  . VAL A 48  ? 0.1688 0.1984 0.1611 0.0430  0.0058  -0.0234 16  VAL A CA  
48   C  C   . VAL A 48  ? 0.1680 0.1973 0.1597 0.0298  -0.0259 -0.0059 16  VAL A C   
49   O  O   . VAL A 48  ? 0.2110 0.2195 0.1761 0.0393  -0.0295 -0.0015 16  VAL A O   
50   C  CB  . VAL A 48  ? 0.2036 0.1946 0.1640 0.0399  0.0026  -0.0198 16  VAL A CB  
51   C  CG1 . VAL A 48  ? 0.2196 0.2233 0.1784 0.0462  -0.0139 -0.0010 16  VAL A CG1 
52   C  CG2 . VAL A 48  ? 0.2244 0.2007 0.2025 0.0448  -0.0111 -0.0123 16  VAL A CG2 
53   N  N   . LEU A 49  ? 0.1818 0.1824 0.1645 0.0329  -0.0109 -0.0212 17  LEU A N   
54   C  CA  . LEU A 49  ? 0.1730 0.1836 0.1830 0.0062  0.0110  -0.0031 17  LEU A CA  
55   C  C   . LEU A 49  ? 0.1529 0.1697 0.1684 0.0123  0.0180  -0.0103 17  LEU A C   
56   O  O   . LEU A 49  ? 0.1880 0.1958 0.1660 0.0270  -0.0151 0.0035  17  LEU A O   
57   C  CB  . LEU A 49  ? 0.2067 0.2008 0.1843 0.0003  0.0127  0.0140  17  LEU A CB  
58   C  CG  . LEU A 49  ? 0.2254 0.2379 0.2165 -0.0296 -0.0155 0.0373  17  LEU A CG  
59   C  CD1 . LEU A 49  ? 0.2975 0.2658 0.2638 -0.0810 0.0083  0.0158  17  LEU A CD1 
60   C  CD2 . LEU A 49  ? 0.2620 0.2735 0.2351 -0.0003 -0.0415 0.0786  17  LEU A CD2 
61   N  N   . ASP A 50  ? 0.1648 0.1717 0.1768 0.0263  0.0279  -0.0002 18  ASP A N   
62   C  CA  . ASP A 50  ? 0.1712 0.1706 0.1565 0.0276  0.0011  -0.0150 18  ASP A CA  
63   C  C   . ASP A 50  ? 0.2022 0.1585 0.1573 0.0213  0.0094  0.0103  18  ASP A C   
64   O  O   . ASP A 50  ? 0.2149 0.1655 0.1900 0.0391  0.0026  0.0129  18  ASP A O   
65   C  CB  . ASP A 50  ? 0.1716 0.1883 0.1720 0.0040  -0.0097 -0.0030 18  ASP A CB  
66   C  CG  . ASP A 50  ? 0.2029 0.2003 0.1895 -0.0027 -0.0084 -0.0151 18  ASP A CG  
67   O  OD1 . ASP A 50  ? 0.2165 0.2026 0.1917 0.0112  0.0163  -0.0186 18  ASP A OD1 
68   O  OD2 . ASP A 50  ? 0.2285 0.2358 0.2477 -0.0274 -0.0014 -0.0207 18  ASP A OD2 
69   N  N   . ALA A 51  ? 0.2039 0.1592 0.1538 0.0103  0.0009  0.0023  19  ALA A N   
70   C  CA  . ALA A 51  ? 0.2124 0.1631 0.1483 0.0178  0.0001  0.0017  19  ALA A CA  
71   C  C   . ALA A 51  ? 0.2196 0.1527 0.1607 0.0226  0.0186  0.0090  19  ALA A C   
72   O  O   . ALA A 51  ? 0.2430 0.1720 0.1867 0.0324  -0.0125 0.0059  19  ALA A O   
73   C  CB  . ALA A 51  ? 0.2314 0.1978 0.1291 0.0184  -0.0570 -0.0263 19  ALA A CB  
74   N  N   . VAL A 52  ? 0.1789 0.1934 0.1779 0.0142  0.0152  0.0088  20  VAL A N   
75   C  CA  . VAL A 52  ? 0.2040 0.2185 0.1905 0.0358  0.0168  0.0268  20  VAL A CA  
76   C  C   . VAL A 52  ? 0.2095 0.2439 0.2031 0.0591  0.0232  0.0296  20  VAL A C   
77   O  O   . VAL A 52  ? 0.2549 0.2651 0.2355 0.0822  0.0204  0.0370  20  VAL A O   
78   C  CB  . VAL A 52  ? 0.2081 0.2290 0.2120 0.0417  0.0334  0.0349  20  VAL A CB  
79   C  CG1 . VAL A 52  ? 0.2476 0.2447 0.2546 0.0318  0.0647  0.0250  20  VAL A CG1 
80   C  CG2 . VAL A 52  ? 0.2271 0.2343 0.1707 0.0228  0.0086  0.0319  20  VAL A CG2 
81   N  N   . ARG A 53  ? 0.1724 0.2578 0.1808 0.0159  0.0183  0.0302  21  ARG A N   
82   C  CA  . ARG A 53  ? 0.1891 0.2612 0.2182 0.0273  -0.0307 0.0294  21  ARG A CA  
83   C  C   . ARG A 53  ? 0.1795 0.2439 0.2233 0.0166  -0.0177 0.0197  21  ARG A C   
84   O  O   . ARG A 53  ? 0.2166 0.2857 0.2505 0.0236  -0.0393 0.0565  21  ARG A O   
85   C  CB  . ARG A 53  ? 0.2066 0.3101 0.2858 -0.0257 -0.0608 0.0237  21  ARG A CB  
86   C  CG  . ARG A 53  ? 0.3016 0.3617 0.3665 -0.0290 -0.0447 -0.0073 21  ARG A CG  
87   C  CD  . ARG A 53  ? 0.4418 0.4167 0.4508 -0.0201 -0.0237 -0.0441 21  ARG A CD  
88   N  NE  . ARG A 53  ? 0.5339 0.4426 0.5143 -0.0041 -0.0172 -0.0643 21  ARG A NE  
89   C  CZ  . ARG A 53  ? 0.6456 0.4908 0.5966 0.0092  -0.0060 -0.0614 21  ARG A CZ  
90   N  NH1 . ARG A 53  ? 0.6437 0.5066 0.6127 0.0157  -0.0161 -0.0585 21  ARG A NH1 
91   N  NH2 . ARG A 53  ? 0.7088 0.5002 0.6169 0.0099  0.0027  -0.0622 21  ARG A NH2 
92   N  N   . GLY A 54  ? 0.2069 0.1811 0.1817 0.0175  0.0003  0.0030  22  GLY A N   
93   C  CA  . GLY A 54  ? 0.2180 0.1866 0.1898 -0.0053 0.0121  0.0069  22  GLY A CA  
94   C  C   . GLY A 54  ? 0.2260 0.1754 0.1995 0.0184  -0.0147 0.0148  22  GLY A C   
95   O  O   . GLY A 54  ? 0.2445 0.2045 0.2037 0.0175  -0.0047 0.0248  22  GLY A O   
96   N  N   . SER A 55  ? 0.2458 0.1691 0.1803 0.0227  -0.0041 -0.0040 23  SER A N   
97   C  CA  . SER A 55  ? 0.2007 0.2039 0.1791 0.0476  -0.0096 -0.0266 23  SER A CA  
98   C  C   . SER A 55  ? 0.2211 0.1853 0.1621 0.0330  -0.0391 -0.0029 23  SER A C   
99   O  O   . SER A 55  ? 0.2481 0.1917 0.1674 0.0317  -0.0389 0.0074  23  SER A O   
100  C  CB  . SER A 55  ? 0.2716 0.2605 0.2276 -0.0091 -0.0222 0.0325  23  SER A CB  
101  O  OG  . SER A 55  ? 0.3514 0.3006 0.2635 0.0028  -0.0154 0.0203  23  SER A OG  
102  N  N   . PRO A 56  ? 0.2497 0.1710 0.1698 0.0138  -0.0186 -0.0062 24  PRO A N   
103  C  CA  . PRO A 56  ? 0.2500 0.1628 0.1761 0.0208  -0.0027 -0.0096 24  PRO A CA  
104  C  C   . PRO A 56  ? 0.2147 0.1734 0.2026 0.0257  0.0199  -0.0008 24  PRO A C   
105  O  O   . PRO A 56  ? 0.2382 0.1725 0.2281 0.0390  0.0222  0.0015  24  PRO A O   
106  C  CB  . PRO A 56  ? 0.2664 0.1875 0.1973 0.0352  0.0059  -0.0125 24  PRO A CB  
107  C  CG  . PRO A 56  ? 0.3889 0.2400 0.2292 0.0778  -0.0105 -0.0025 24  PRO A CG  
108  C  CD  . PRO A 56  ? 0.3024 0.1929 0.1865 0.0473  -0.0563 -0.0241 24  PRO A CD  
109  N  N   . ALA A 57  ? 0.2321 0.1588 0.1974 0.0334  0.0049  0.0147  25  ALA A N   
110  C  CA  . ALA A 57  ? 0.2102 0.1758 0.1949 0.0264  -0.0312 -0.0017 25  ALA A CA  
111  C  C   . ALA A 57  ? 0.1966 0.1893 0.1909 0.0081  -0.0045 -0.0087 25  ALA A C   
112  O  O   . ALA A 57  ? 0.2218 0.1911 0.2085 0.0173  0.0019  -0.0233 25  ALA A O   
113  C  CB  . ALA A 57  ? 0.2490 0.2083 0.1798 0.0255  -0.0282 0.0005  25  ALA A CB  
114  N  N   . ILE A 58  ? 0.1919 0.1921 0.1950 0.0101  -0.0550 -0.0269 26  ILE A N   
115  C  CA  . ILE A 58  ? 0.2331 0.2003 0.2268 0.0281  -0.0353 -0.0075 26  ILE A CA  
116  C  C   . ILE A 58  ? 0.2358 0.2035 0.2518 0.0134  -0.0463 -0.0075 26  ILE A C   
117  O  O   . ILE A 58  ? 0.2419 0.2136 0.2837 -0.0062 -0.0197 -0.0038 26  ILE A O   
118  C  CB  . ILE A 58  ? 0.3025 0.2059 0.2649 0.0427  -0.0961 0.0071  26  ILE A CB  
119  C  CG1 . ILE A 58  ? 0.3049 0.2013 0.2749 0.0594  -0.0846 0.0301  26  ILE A CG1 
120  C  CG2 . ILE A 58  ? 0.3445 0.2663 0.3152 0.0285  -0.0792 -0.0043 26  ILE A CG2 
121  C  CD1 . ILE A 58  ? 0.3332 0.2593 0.3288 0.0620  -0.0820 0.0366  26  ILE A CD1 
122  N  N   . ASN A 59  ? 0.2152 0.2161 0.2727 0.0036  -0.0410 -0.0095 27  ASN A N   
123  C  CA  A ASN A 59  ? 0.2574 0.2351 0.3110 -0.0113 -0.0418 -0.0117 27  ASN A CA  
124  C  CA  B ASN A 59  ? 0.2309 0.2344 0.2965 -0.0086 -0.0327 -0.0171 27  ASN A CA  
125  C  C   . ASN A 59  ? 0.2272 0.2241 0.2884 0.0008  -0.0021 -0.0098 27  ASN A C   
126  O  O   . ASN A 59  ? 0.2441 0.2411 0.3321 -0.0228 -0.0121 -0.0141 27  ASN A O   
127  C  CB  A ASN A 59  ? 0.3196 0.2693 0.3790 -0.0179 -0.0516 -0.0057 27  ASN A CB  
128  C  CB  B ASN A 59  ? 0.2354 0.2660 0.3374 -0.0079 -0.0260 -0.0188 27  ASN A CB  
129  C  CG  A ASN A 59  ? 0.4184 0.3127 0.4349 -0.0283 -0.0543 0.0009  27  ASN A CG  
130  C  CG  B ASN A 59  ? 0.2934 0.3088 0.3667 -0.0094 -0.0194 -0.0156 27  ASN A CG  
131  O  OD1 A ASN A 59  ? 0.4857 0.3415 0.4660 -0.0279 -0.0538 0.0037  27  ASN A OD1 
132  O  OD1 B ASN A 59  ? 0.3033 0.3323 0.3825 0.0043  -0.0329 -0.0117 27  ASN A OD1 
133  N  ND2 A ASN A 59  ? 0.4508 0.3306 0.4523 -0.0254 -0.0544 -0.0051 27  ASN A ND2 
134  N  ND2 B ASN A 59  ? 0.3180 0.3243 0.3830 -0.0245 -0.0060 -0.0191 27  ASN A ND2 
135  N  N   . VAL A 60  ? 0.2146 0.2092 0.2243 0.0352  -0.0258 -0.0304 28  VAL A N   
136  C  CA  . VAL A 60  ? 0.2213 0.1930 0.2077 0.0214  -0.0350 -0.0267 28  VAL A CA  
137  C  C   . VAL A 60  ? 0.1918 0.1812 0.2086 0.0173  -0.0100 -0.0274 28  VAL A C   
138  O  O   . VAL A 60  ? 0.1841 0.1995 0.2050 0.0186  0.0147  -0.0324 28  VAL A O   
139  C  CB  . VAL A 60  ? 0.2436 0.1968 0.1980 0.0313  -0.0492 -0.0479 28  VAL A CB  
140  C  CG1 . VAL A 60  ? 0.2649 0.2144 0.2165 0.0372  -0.0385 -0.0154 28  VAL A CG1 
141  C  CG2 . VAL A 60  ? 0.2837 0.1934 0.2312 0.0566  -0.0061 -0.0368 28  VAL A CG2 
142  N  N   . ALA A 61  ? 0.2177 0.1482 0.2232 0.0151  -0.0347 -0.0287 29  ALA A N   
143  C  CA  . ALA A 61  ? 0.1719 0.1699 0.1993 0.0050  -0.0284 -0.0176 29  ALA A CA  
144  C  C   . ALA A 61  ? 0.1583 0.1777 0.1890 0.0227  -0.0174 -0.0139 29  ALA A C   
145  O  O   . ALA A 61  ? 0.2124 0.1983 0.1931 0.0038  0.0053  -0.0372 29  ALA A O   
146  C  CB  . ALA A 61  ? 0.1906 0.1754 0.2365 -0.0022 -0.0164 -0.0219 29  ALA A CB  
147  N  N   . MET A 62  ? 0.1358 0.1902 0.1842 0.0216  -0.0167 -0.0289 30  MET A N   
148  C  CA  . MET A 62  ? 0.1470 0.1891 0.1992 0.0193  -0.0250 -0.0397 30  MET A CA  
149  C  C   . MET A 62  ? 0.1662 0.1926 0.1843 0.0236  -0.0248 -0.0331 30  MET A C   
150  O  O   . MET A 62  ? 0.1871 0.1972 0.1877 0.0169  0.0003  -0.0313 30  MET A O   
151  C  CB  . MET A 62  ? 0.1913 0.1970 0.2145 -0.0316 0.0109  -0.0288 30  MET A CB  
152  C  CG  . MET A 62  ? 0.2091 0.1922 0.2242 -0.0359 0.0333  -0.0210 30  MET A CG  
153  S  SD  . MET A 62  ? 0.2132 0.2084 0.2438 -0.0084 -0.0156 -0.0010 30  MET A SD  
154  C  CE  . MET A 62  ? 0.2254 0.2252 0.2557 0.0058  -0.0163 -0.0019 30  MET A CE  
155  N  N   . HIS A 63  ? 0.1485 0.2043 0.1971 0.0263  -0.0250 -0.0313 31  HIS A N   
156  C  CA  . HIS A 63  ? 0.1424 0.2085 0.2091 0.0205  -0.0212 -0.0087 31  HIS A CA  
157  C  C   . HIS A 63  ? 0.1377 0.2168 0.2038 0.0094  -0.0021 -0.0445 31  HIS A C   
158  O  O   . HIS A 63  ? 0.1864 0.2387 0.1871 0.0044  0.0068  -0.0607 31  HIS A O   
159  C  CB  . HIS A 63  ? 0.1954 0.2392 0.2588 -0.0261 -0.0443 0.0328  31  HIS A CB  
160  C  CG  . HIS A 63  ? 0.2389 0.3035 0.3053 -0.0456 -0.0608 0.0656  31  HIS A CG  
161  N  ND1 . HIS A 63  ? 0.2939 0.3496 0.3240 -0.0818 -0.0751 0.0895  31  HIS A ND1 
162  C  CD2 . HIS A 63  ? 0.2437 0.3326 0.3242 -0.0762 -0.0829 0.0643  31  HIS A CD2 
163  C  CE1 . HIS A 63  ? 0.2913 0.3642 0.3414 -0.1099 -0.0795 0.0794  31  HIS A CE1 
164  N  NE2 . HIS A 63  ? 0.2886 0.3652 0.3372 -0.1158 -0.0869 0.0734  31  HIS A NE2 
165  N  N   . VAL A 64  ? 0.1224 0.2005 0.2150 0.0204  -0.0001 -0.0315 32  VAL A N   
166  C  CA  . VAL A 64  ? 0.1431 0.1902 0.2006 0.0178  -0.0153 -0.0336 32  VAL A CA  
167  C  C   . VAL A 64  ? 0.1441 0.1871 0.2184 0.0083  -0.0188 -0.0376 32  VAL A C   
168  O  O   . VAL A 64  ? 0.1676 0.1888 0.2321 0.0005  -0.0135 -0.0702 32  VAL A O   
169  C  CB  . VAL A 64  ? 0.1553 0.2150 0.2033 0.0132  -0.0053 -0.0214 32  VAL A CB  
170  C  CG1 . VAL A 64  ? 0.1503 0.2317 0.2153 -0.0008 0.0052  -0.0172 32  VAL A CG1 
171  C  CG2 . VAL A 64  ? 0.2000 0.2034 0.2090 0.0238  -0.0121 -0.0071 32  VAL A CG2 
172  N  N   . PHE A 65  ? 0.1371 0.1910 0.2159 0.0163  -0.0493 -0.0040 33  PHE A N   
173  C  CA  . PHE A 65  ? 0.1625 0.2007 0.2169 0.0139  -0.0298 -0.0106 33  PHE A CA  
174  C  C   . PHE A 65  ? 0.1805 0.2000 0.2256 0.0258  -0.0254 -0.0319 33  PHE A C   
175  O  O   . PHE A 65  ? 0.1822 0.2009 0.2257 -0.0140 0.0070  -0.0474 33  PHE A O   
176  C  CB  . PHE A 65  ? 0.1956 0.2217 0.2214 0.0046  -0.0108 0.0090  33  PHE A CB  
177  C  CG  . PHE A 65  ? 0.1674 0.2379 0.2442 -0.0186 -0.0141 0.0056  33  PHE A CG  
178  C  CD1 . PHE A 65  ? 0.1535 0.2647 0.2478 0.0186  -0.0045 -0.0056 33  PHE A CD1 
179  C  CD2 . PHE A 65  ? 0.1823 0.2505 0.2834 -0.0153 -0.0009 -0.0006 33  PHE A CD2 
180  C  CE1 . PHE A 65  ? 0.1755 0.2908 0.2420 -0.0065 -0.0263 -0.0129 33  PHE A CE1 
181  C  CE2 . PHE A 65  ? 0.2121 0.2669 0.2805 -0.0202 0.0062  -0.0032 33  PHE A CE2 
182  C  CZ  . PHE A 65  ? 0.1949 0.2919 0.2672 -0.0111 -0.0011 -0.0082 33  PHE A CZ  
183  N  N   . ARG A 66  ? 0.1667 0.2061 0.2585 0.0295  -0.0176 -0.0453 34  ARG A N   
184  C  CA  . ARG A 66  ? 0.1780 0.2106 0.2723 0.0305  -0.0151 -0.0408 34  ARG A CA  
185  C  C   . ARG A 66  ? 0.1866 0.2096 0.2575 0.0287  -0.0288 -0.0313 34  ARG A C   
186  O  O   . ARG A 66  ? 0.2280 0.2017 0.2854 0.0143  -0.0376 -0.0390 34  ARG A O   
187  C  CB  . ARG A 66  ? 0.1826 0.2443 0.2868 0.0164  0.0159  -0.0213 34  ARG A CB  
188  C  CG  . ARG A 66  ? 0.2199 0.2513 0.3161 0.0256  -0.0066 -0.0361 34  ARG A CG  
189  C  CD  . ARG A 66  ? 0.2462 0.2666 0.3257 -0.0139 -0.0093 -0.0476 34  ARG A CD  
190  N  NE  . ARG A 66  ? 0.2862 0.2841 0.3126 0.0225  0.0274  -0.0442 34  ARG A NE  
191  C  CZ  . ARG A 66  ? 0.2791 0.2685 0.2957 0.0241  0.0575  -0.0058 34  ARG A CZ  
192  N  NH1 . ARG A 66  ? 0.2879 0.2672 0.3214 -0.0053 0.0601  -0.0270 34  ARG A NH1 
193  N  NH2 . ARG A 66  ? 0.2770 0.2656 0.2824 -0.0078 0.0688  0.0040  34  ARG A NH2 
194  N  N   . LYS A 67  ? 0.1923 0.1968 0.2527 0.0107  -0.0429 -0.0072 35  LYS A N   
195  C  CA  . LYS A 67  ? 0.2461 0.2314 0.2744 0.0366  -0.0117 0.0090  35  LYS A CA  
196  C  C   . LYS A 67  ? 0.2393 0.2128 0.2727 0.0396  0.0008  0.0220  35  LYS A C   
197  O  O   . LYS A 67  ? 0.2585 0.2169 0.2745 0.0304  0.0210  0.0154  35  LYS A O   
198  C  CB  . LYS A 67  ? 0.3320 0.2964 0.3196 0.0104  -0.0221 0.0147  35  LYS A CB  
199  C  CG  . LYS A 67  ? 0.4475 0.3768 0.4044 -0.0009 0.0036  0.0241  35  LYS A CG  
200  C  CD  . LYS A 67  ? 0.5364 0.4285 0.4570 -0.0074 0.0106  0.0269  35  LYS A CD  
201  C  CE  . LYS A 67  ? 0.6061 0.4546 0.5054 -0.0338 0.0068  0.0194  35  LYS A CE  
202  N  NZ  . LYS A 67  ? 0.6387 0.4621 0.5393 -0.0419 0.0233  0.0240  35  LYS A NZ  
203  N  N   . ALA A 68  ? 0.2643 0.2280 0.2937 0.0505  0.0094  -0.0052 36  ALA A N   
204  C  CA  . ALA A 68  ? 0.3170 0.2628 0.3172 0.0410  0.0111  -0.0069 36  ALA A CA  
205  C  C   . ALA A 68  ? 0.3320 0.3023 0.3334 0.0796  0.0486  0.0223  36  ALA A C   
206  O  O   . ALA A 68  ? 0.3158 0.3152 0.3330 0.0618  0.0264  0.0182  36  ALA A O   
207  C  CB  . ALA A 68  ? 0.3425 0.2694 0.3332 0.0145  0.0065  -0.0161 36  ALA A CB  
208  N  N   . ALA A 69  ? 0.4102 0.3466 0.3582 0.1141  0.0594  0.0614  37  ALA A N   
209  C  CA  . ALA A 69  ? 0.4638 0.3871 0.3984 0.1426  0.0610  0.0840  37  ALA A CA  
210  C  C   . ALA A 69  ? 0.4843 0.4102 0.4172 0.1324  0.0544  0.1066  37  ALA A C   
211  O  O   . ALA A 69  ? 0.4905 0.4474 0.4303 0.1147  0.0499  0.1162  37  ALA A O   
212  C  CB  . ALA A 69  ? 0.4709 0.3997 0.4102 0.1788  0.0551  0.0983  37  ALA A CB  
213  N  N   . ASP A 70  ? 0.4904 0.3948 0.4465 0.1423  0.0353  0.1057  38  ASP A N   
214  C  CA  . ASP A 70  ? 0.5558 0.4008 0.4855 0.1063  0.0215  0.1174  38  ASP A CA  
215  C  C   . ASP A 70  ? 0.5489 0.4293 0.4896 0.1062  0.0260  0.1411  38  ASP A C   
216  O  O   . ASP A 70  ? 0.5508 0.4402 0.4818 0.1089  0.0370  0.1597  38  ASP A O   
217  C  CB  . ASP A 70  ? 0.6293 0.3659 0.5385 0.0872  -0.0148 0.1091  38  ASP A CB  
218  C  CG  . ASP A 70  ? 0.7025 0.3491 0.5929 0.0438  -0.0287 0.0780  38  ASP A CG  
219  O  OD1 . ASP A 70  ? 0.7070 0.3170 0.5988 0.0436  -0.0376 0.0749  38  ASP A OD1 
220  O  OD2 . ASP A 70  ? 0.7532 0.3335 0.6216 0.0233  -0.0408 0.0600  38  ASP A OD2 
221  N  N   . ASP A 71  ? 0.5464 0.4522 0.5016 0.0891  0.0109  0.1358  39  ASP A N   
222  C  CA  . ASP A 71  ? 0.5861 0.5027 0.5574 0.0564  0.0270  0.1127  39  ASP A CA  
223  C  C   . ASP A 71  ? 0.5154 0.4716 0.5358 0.0128  0.0573  0.1114  39  ASP A C   
224  O  O   . ASP A 71  ? 0.5405 0.4873 0.5609 0.0083  0.0695  0.0907  39  ASP A O   
225  C  CB  . ASP A 71  ? 0.7124 0.5715 0.6452 0.0485  0.0377  0.0868  39  ASP A CB  
226  C  CG  . ASP A 71  ? 0.8255 0.6271 0.7341 0.0342  0.0385  0.0608  39  ASP A CG  
227  O  OD1 . ASP A 71  ? 0.8739 0.6473 0.7600 0.0294  0.0379  0.0530  39  ASP A OD1 
228  O  OD2 . ASP A 71  ? 0.8673 0.6464 0.7576 0.0281  0.0393  0.0540  39  ASP A OD2 
229  N  N   . THR A 72  ? 0.4193 0.4049 0.4942 0.0094  0.0534  0.1264  40  THR A N   
230  C  CA  . THR A 72  ? 0.3958 0.3582 0.4781 0.0010  0.0080  0.1040  40  THR A CA  
231  C  C   . THR A 72  ? 0.3103 0.3053 0.4277 0.0210  -0.0019 0.0719  40  THR A C   
232  O  O   . THR A 72  ? 0.2820 0.2780 0.4309 0.0385  0.0244  0.0478  40  THR A O   
233  C  CB  . THR A 72  ? 0.4467 0.3632 0.5064 -0.0185 -0.0084 0.0985  40  THR A CB  
234  O  OG1 . THR A 72  ? 0.4734 0.3626 0.5269 -0.0318 -0.0066 0.0830  40  THR A OG1 
235  C  CG2 . THR A 72  ? 0.4938 0.3795 0.5328 -0.0238 -0.0137 0.0899  40  THR A CG2 
236  N  N   . TRP A 73  ? 0.2734 0.2753 0.3928 0.0157  0.0016  0.0515  41  TRP A N   
237  C  CA  . TRP A 73  ? 0.2299 0.2854 0.3653 -0.0265 0.0185  0.0108  41  TRP A CA  
238  C  C   . TRP A 73  ? 0.2760 0.2742 0.3909 -0.0641 -0.0058 -0.0378 41  TRP A C   
239  O  O   . TRP A 73  ? 0.3327 0.3573 0.4507 -0.0898 0.0314  -0.0564 41  TRP A O   
240  C  CB  . TRP A 73  ? 0.2299 0.2932 0.3445 -0.0084 0.0471  0.0129  41  TRP A CB  
241  C  CG  . TRP A 73  ? 0.3038 0.3138 0.3268 -0.0174 0.0334  0.0119  41  TRP A CG  
242  C  CD1 . TRP A 73  ? 0.3651 0.3305 0.3143 -0.0239 0.0643  0.0171  41  TRP A CD1 
243  C  CD2 . TRP A 73  ? 0.2716 0.2889 0.3099 -0.0030 0.0282  0.0187  41  TRP A CD2 
244  N  NE1 . TRP A 73  ? 0.3916 0.3481 0.3238 -0.0254 0.0408  0.0024  41  TRP A NE1 
245  C  CE2 . TRP A 73  ? 0.3221 0.3089 0.3150 -0.0242 0.0253  0.0193  41  TRP A CE2 
246  C  CE3 . TRP A 73  ? 0.1984 0.2747 0.3141 0.0168  -0.0244 0.0364  41  TRP A CE3 
247  C  CZ2 . TRP A 73  ? 0.3238 0.3092 0.3291 0.0066  0.0074  0.0113  41  TRP A CZ2 
248  C  CZ3 . TRP A 73  ? 0.2438 0.2669 0.3037 0.0297  -0.0341 0.0066  41  TRP A CZ3 
249  C  CH2 . TRP A 73  ? 0.2967 0.2939 0.3213 0.0139  -0.0047 0.0047  41  TRP A CH2 
250  N  N   . GLU A 74  ? 0.2510 0.2382 0.3726 -0.0193 -0.0926 -0.0234 42  GLU A N   
251  C  CA  . GLU A 74  ? 0.3052 0.2706 0.3931 0.0055  -0.1087 -0.0282 42  GLU A CA  
252  C  C   . GLU A 74  ? 0.2449 0.2334 0.3734 -0.0084 -0.1147 -0.0302 42  GLU A C   
253  O  O   . GLU A 74  ? 0.2275 0.2153 0.3635 -0.0220 -0.0822 -0.0530 42  GLU A O   
254  C  CB  . GLU A 74  ? 0.4424 0.3477 0.4278 0.0340  -0.1201 -0.0357 42  GLU A CB  
255  C  CG  . GLU A 74  ? 0.5924 0.4343 0.4897 0.0206  -0.0946 -0.0596 42  GLU A CG  
256  C  CD  . GLU A 74  ? 0.7400 0.4967 0.5363 0.0099  -0.0663 -0.0754 42  GLU A CD  
257  O  OE1 . GLU A 74  ? 0.7853 0.5151 0.5502 -0.0231 -0.0598 -0.0931 42  GLU A OE1 
258  O  OE2 . GLU A 74  ? 0.8039 0.5374 0.5450 0.0194  -0.0637 -0.0785 42  GLU A OE2 
259  N  N   . PRO A 75  ? 0.2466 0.2139 0.3825 -0.0193 -0.1215 -0.0441 43  PRO A N   
260  C  CA  . PRO A 75  ? 0.2841 0.2193 0.3791 -0.0094 -0.0970 -0.0334 43  PRO A CA  
261  C  C   . PRO A 75  ? 0.3161 0.2335 0.3346 0.0266  -0.0343 -0.0495 43  PRO A C   
262  O  O   . PRO A 75  ? 0.4139 0.2623 0.3586 0.0747  0.0441  -0.0419 43  PRO A O   
263  C  CB  . PRO A 75  ? 0.3190 0.2027 0.4092 -0.0362 -0.1154 -0.0226 43  PRO A CB  
264  C  CG  . PRO A 75  ? 0.3545 0.2451 0.4474 -0.0408 -0.1195 -0.0027 43  PRO A CG  
265  C  CD  . PRO A 75  ? 0.2721 0.2103 0.4311 -0.0483 -0.1307 -0.0333 43  PRO A CD  
266  N  N   . PHE A 76  ? 0.2328 0.2253 0.2834 0.0073  -0.0457 -0.0419 44  PHE A N   
267  C  CA  . PHE A 76  ? 0.1987 0.2491 0.2482 0.0214  -0.0357 -0.0627 44  PHE A CA  
268  C  C   . PHE A 76  ? 0.1908 0.2542 0.2169 0.0411  -0.0171 -0.0712 44  PHE A C   
269  O  O   . PHE A 76  ? 0.2601 0.2773 0.2300 0.0531  -0.0054 -0.0729 44  PHE A O   
270  C  CB  . PHE A 76  ? 0.1867 0.2668 0.2379 0.0260  -0.0216 -0.0544 44  PHE A CB  
271  C  CG  . PHE A 76  ? 0.1792 0.3022 0.2324 0.0270  0.0098  -0.0543 44  PHE A CG  
272  C  CD1 . PHE A 76  ? 0.1927 0.3212 0.2317 0.0028  0.0124  -0.0775 44  PHE A CD1 
273  C  CD2 . PHE A 76  ? 0.2095 0.3121 0.2213 -0.0004 0.0083  -0.0423 44  PHE A CD2 
274  C  CE1 . PHE A 76  ? 0.2402 0.3408 0.2274 -0.0133 0.0195  -0.0837 44  PHE A CE1 
275  C  CE2 . PHE A 76  ? 0.1850 0.3270 0.2105 -0.0012 0.0155  -0.0497 44  PHE A CE2 
276  C  CZ  . PHE A 76  ? 0.2330 0.3425 0.2089 -0.0061 0.0091  -0.0679 44  PHE A CZ  
277  N  N   . ALA A 77  ? 0.1728 0.2415 0.2150 0.0436  -0.0131 -0.0467 45  ALA A N   
278  C  CA  . ALA A 77  ? 0.1466 0.2502 0.2120 0.0156  0.0079  -0.0328 45  ALA A CA  
279  C  C   . ALA A 77  ? 0.1396 0.2207 0.1851 0.0190  0.0027  -0.0468 45  ALA A C   
280  O  O   . ALA A 77  ? 0.1945 0.2440 0.2056 0.0112  -0.0071 -0.0452 45  ALA A O   
281  C  CB  . ALA A 77  ? 0.2223 0.2561 0.2240 0.0058  0.0333  -0.0446 45  ALA A CB  
282  N  N   . SER A 78  ? 0.1710 0.2207 0.1743 0.0146  -0.0287 -0.0588 46  SER A N   
283  C  CA  . SER A 78  ? 0.1268 0.1934 0.1953 0.0057  -0.0083 -0.0558 46  SER A CA  
284  C  C   . SER A 78  ? 0.1654 0.1977 0.1889 0.0326  -0.0040 -0.0554 46  SER A C   
285  O  O   . SER A 78  ? 0.1977 0.2302 0.1729 0.0085  -0.0098 -0.0506 46  SER A O   
286  C  CB  . SER A 78  ? 0.1762 0.1930 0.2150 -0.0427 -0.0033 -0.0500 46  SER A CB  
287  O  OG  . SER A 78  ? 0.2061 0.2215 0.2255 -0.0354 -0.0540 -0.0580 46  SER A OG  
288  N  N   . GLY A 79  ? 0.1647 0.1848 0.1943 0.0277  -0.0130 -0.0307 47  GLY A N   
289  C  CA  . GLY A 79  ? 0.1869 0.1915 0.1771 0.0513  -0.0097 -0.0219 47  GLY A CA  
290  C  C   . GLY A 79  ? 0.2032 0.1776 0.1856 0.0437  -0.0182 -0.0192 47  GLY A C   
291  O  O   . GLY A 79  ? 0.2193 0.1877 0.1834 0.0232  -0.0162 -0.0314 47  GLY A O   
292  N  N   . LYS A 80  ? 0.2039 0.1621 0.2400 0.0237  0.0053  -0.0344 48  LYS A N   
293  C  CA  . LYS A 80  ? 0.2267 0.1693 0.2773 0.0245  0.0204  -0.0317 48  LYS A CA  
294  C  C   . LYS A 80  ? 0.2484 0.1733 0.2350 0.0074  -0.0054 -0.0111 48  LYS A C   
295  O  O   . LYS A 80  ? 0.2621 0.1928 0.2358 0.0056  -0.0144 -0.0091 48  LYS A O   
296  C  CB  . LYS A 80  ? 0.2867 0.2424 0.3673 -0.0153 0.0883  -0.0382 48  LYS A CB  
297  C  CG  . LYS A 80  ? 0.3846 0.3483 0.4446 -0.0308 0.0982  -0.0505 48  LYS A CG  
298  C  CD  . LYS A 80  ? 0.4661 0.4343 0.5185 -0.0812 0.1057  -0.0528 48  LYS A CD  
299  C  CE  . LYS A 80  ? 0.5250 0.4883 0.5502 -0.0944 0.1464  -0.0748 48  LYS A CE  
300  N  NZ  . LYS A 80  ? 0.5647 0.5124 0.5674 -0.1056 0.1765  -0.1158 48  LYS A NZ  
301  N  N   . THR A 81  ? 0.2058 0.1779 0.2114 -0.0041 -0.0073 -0.0249 49  THR A N   
302  C  CA  . THR A 81  ? 0.2308 0.1690 0.1907 -0.0004 -0.0560 -0.0024 49  THR A CA  
303  C  C   . THR A 81  ? 0.2362 0.2089 0.2015 0.0097  -0.0419 -0.0153 49  THR A C   
304  O  O   . THR A 81  ? 0.2452 0.2249 0.2114 0.0317  -0.0177 -0.0280 49  THR A O   
305  C  CB  . THR A 81  ? 0.2186 0.1931 0.1598 0.0079  -0.0115 -0.0110 49  THR A CB  
306  O  OG1 . THR A 81  ? 0.2296 0.1822 0.1890 0.0227  0.0208  -0.0098 49  THR A OG1 
307  C  CG2 . THR A 81  ? 0.2472 0.1988 0.1639 0.0198  -0.0493 0.0033  49  THR A CG2 
308  N  N   . SER A 82  ? 0.2413 0.2379 0.1674 -0.0129 -0.0557 -0.0042 50  SER A N   
309  C  CA  . SER A 82  ? 0.2632 0.2420 0.1850 0.0303  -0.0777 -0.0018 50  SER A CA  
310  C  C   . SER A 82  ? 0.2963 0.2617 0.2059 0.0285  -0.0709 -0.0096 50  SER A C   
311  O  O   . SER A 82  ? 0.2630 0.2532 0.1877 0.0343  -0.0366 -0.0075 50  SER A O   
312  C  CB  . SER A 82  ? 0.3365 0.2682 0.2104 -0.0038 -0.0429 -0.0113 50  SER A CB  
313  O  OG  . SER A 82  ? 0.3472 0.2823 0.2649 0.0192  -0.0246 0.0154  50  SER A OG  
314  N  N   . GLU A 83  ? 0.3266 0.2770 0.2382 0.0596  -0.0786 0.0082  51  GLU A N   
315  C  CA  . GLU A 83  ? 0.3655 0.2963 0.2706 0.1122  -0.1041 0.0204  51  GLU A CA  
316  C  C   . GLU A 83  ? 0.3559 0.2900 0.2596 0.0794  -0.0538 0.0237  51  GLU A C   
317  O  O   . GLU A 83  ? 0.3843 0.2836 0.2975 0.0814  -0.0334 0.0130  51  GLU A O   
318  C  CB  . GLU A 83  ? 0.4924 0.3770 0.3582 0.1112  -0.1210 0.0432  51  GLU A CB  
319  C  CG  . GLU A 83  ? 0.6621 0.4807 0.4609 0.0841  -0.0842 0.0499  51  GLU A CG  
320  C  CD  . GLU A 83  ? 0.7941 0.5595 0.5375 0.0543  -0.0441 0.0497  51  GLU A CD  
321  O  OE1 . GLU A 83  ? 0.8315 0.5789 0.5472 0.0452  -0.0330 0.0406  51  GLU A OE1 
322  O  OE2 . GLU A 83  ? 0.8441 0.5914 0.5739 0.0364  -0.0303 0.0511  51  GLU A OE2 
323  N  N   . SER A 84  ? 0.3345 0.2700 0.2130 0.0625  -0.0517 0.0395  52  SER A N   
324  C  CA  . SER A 84  ? 0.3063 0.2692 0.2037 0.0450  0.0061  0.0218  52  SER A CA  
325  C  C   . SER A 84  ? 0.2805 0.2302 0.1871 0.0292  -0.0072 0.0210  52  SER A C   
326  O  O   . SER A 84  ? 0.3126 0.2276 0.2147 0.0275  0.0130  0.0137  52  SER A O   
327  C  CB  . SER A 84  ? 0.3369 0.3060 0.2398 0.0167  0.0077  0.0376  52  SER A CB  
328  O  OG  . SER A 84  ? 0.3934 0.3631 0.2719 0.0007  0.0143  -0.0133 52  SER A OG  
329  N  N   . GLY A 85  ? 0.2525 0.2152 0.1462 0.0396  -0.0238 0.0122  53  GLY A N   
330  C  CA  . GLY A 85  ? 0.2267 0.2190 0.1436 0.0306  -0.0491 -0.0087 53  GLY A CA  
331  C  C   . GLY A 85  ? 0.2001 0.2119 0.1628 0.0173  -0.0296 -0.0140 53  GLY A C   
332  O  O   . GLY A 85  ? 0.2156 0.2225 0.1487 0.0169  -0.0452 -0.0150 53  GLY A O   
333  N  N   . GLU A 86  ? 0.2143 0.1971 0.1888 0.0275  -0.0212 -0.0101 54  GLU A N   
334  C  CA  . GLU A 86  ? 0.2058 0.1947 0.1934 0.0223  -0.0010 -0.0193 54  GLU A CA  
335  C  C   . GLU A 86  ? 0.1767 0.2092 0.1811 0.0236  -0.0116 -0.0119 54  GLU A C   
336  O  O   . GLU A 86  ? 0.2035 0.2471 0.2058 0.0312  -0.0376 -0.0513 54  GLU A O   
337  C  CB  . GLU A 86  ? 0.2692 0.2064 0.2359 0.0241  0.0190  0.0207  54  GLU A CB  
338  C  CG  . GLU A 86  ? 0.3897 0.2198 0.3176 -0.0010 0.0490  0.0063  54  GLU A CG  
339  C  CD  . GLU A 86  ? 0.5018 0.2334 0.3825 0.0056  0.0775  0.0134  54  GLU A CD  
340  O  OE1 . GLU A 86  ? 0.5437 0.2647 0.4004 0.0065  0.0907  0.0194  54  GLU A OE1 
341  O  OE2 . GLU A 86  ? 0.5611 0.2542 0.4360 -0.0025 0.0952  0.0154  54  GLU A OE2 
342  N  N   . LEU A 87  ? 0.1945 0.1972 0.1922 0.0304  -0.0078 -0.0259 55  LEU A N   
343  C  CA  . LEU A 87  ? 0.1876 0.1908 0.1852 0.0137  0.0028  -0.0186 55  LEU A CA  
344  C  C   . LEU A 87  ? 0.2147 0.2099 0.1996 0.0177  -0.0378 -0.0185 55  LEU A C   
345  O  O   . LEU A 87  ? 0.2075 0.2138 0.1921 0.0211  -0.0157 -0.0277 55  LEU A O   
346  C  CB  . LEU A 87  ? 0.1994 0.1890 0.2048 0.0007  -0.0154 -0.0101 55  LEU A CB  
347  C  CG  . LEU A 87  ? 0.2064 0.1984 0.1854 -0.0088 -0.0271 -0.0148 55  LEU A CG  
348  C  CD1 . LEU A 87  ? 0.2314 0.2189 0.2275 0.0041  -0.0288 -0.0421 55  LEU A CD1 
349  C  CD2 . LEU A 87  ? 0.2301 0.2092 0.1779 -0.0118 0.0081  0.0315  55  LEU A CD2 
350  N  N   . HIS A 88  ? 0.2716 0.2373 0.1953 0.0375  -0.0059 -0.0330 56  HIS A N   
351  C  CA  . HIS A 88  ? 0.2913 0.2503 0.1988 0.0556  0.0265  -0.0105 56  HIS A CA  
352  C  C   . HIS A 88  ? 0.3002 0.2754 0.2216 0.0366  0.0301  -0.0263 56  HIS A C   
353  O  O   . HIS A 88  ? 0.2977 0.2923 0.2364 0.0253  0.0197  -0.0230 56  HIS A O   
354  C  CB  . HIS A 88  ? 0.3180 0.2827 0.2422 0.0274  0.0428  0.0091  56  HIS A CB  
355  C  CG  . HIS A 88  ? 0.3663 0.3116 0.2726 0.0027  0.0643  0.0175  56  HIS A CG  
356  N  ND1 . HIS A 88  ? 0.3872 0.3383 0.3097 -0.0087 0.0651  0.0139  56  HIS A ND1 
357  C  CD2 . HIS A 88  ? 0.3835 0.3258 0.3036 -0.0117 0.0785  0.0160  56  HIS A CD2 
358  C  CE1 . HIS A 88  ? 0.3933 0.3323 0.3171 -0.0240 0.0748  0.0099  56  HIS A CE1 
359  N  NE2 . HIS A 88  ? 0.3850 0.3312 0.2947 -0.0214 0.1001  0.0175  56  HIS A NE2 
360  N  N   . GLY A 89  ? 0.2815 0.2907 0.2078 0.0492  0.0084  -0.0396 57  GLY A N   
361  C  CA  . GLY A 89  ? 0.2957 0.2937 0.2454 0.0641  -0.0066 -0.0646 57  GLY A CA  
362  C  C   . GLY A 89  ? 0.2894 0.2832 0.2618 0.0386  -0.0420 -0.0745 57  GLY A C   
363  O  O   . GLY A 89  ? 0.3149 0.2912 0.2774 0.0434  -0.0651 -0.0983 57  GLY A O   
364  N  N   . LEU A 90  ? 0.2407 0.2636 0.2277 0.0372  -0.0281 -0.0725 58  LEU A N   
365  C  CA  . LEU A 90  ? 0.2388 0.2562 0.2371 0.0198  0.0001  -0.0653 58  LEU A CA  
366  C  C   . LEU A 90  ? 0.2462 0.2420 0.2440 0.0085  -0.0025 -0.0607 58  LEU A C   
367  O  O   . LEU A 90  ? 0.3094 0.2395 0.2763 0.0230  0.0154  -0.0521 58  LEU A O   
368  C  CB  . LEU A 90  ? 0.2642 0.2616 0.2519 0.0068  -0.0221 -0.0661 58  LEU A CB  
369  C  CG  . LEU A 90  ? 0.2691 0.2600 0.2717 0.0317  -0.0057 -0.0701 58  LEU A CG  
370  C  CD1 . LEU A 90  ? 0.2729 0.2767 0.2666 0.0517  -0.0258 -0.0703 58  LEU A CD1 
371  C  CD2 . LEU A 90  ? 0.3030 0.2673 0.3137 0.0428  0.0534  -0.0779 58  LEU A CD2 
372  N  N   . THR A 91  ? 0.2111 0.2575 0.2294 0.0406  0.0028  -0.0431 59  THR A N   
373  C  CA  . THR A 91  ? 0.2561 0.2505 0.2177 0.0487  0.0053  -0.0484 59  THR A CA  
374  C  C   . THR A 91  ? 0.2907 0.2558 0.2376 0.0645  -0.0139 -0.0453 59  THR A C   
375  O  O   . THR A 91  ? 0.3117 0.2770 0.2506 0.0781  0.0136  -0.0142 59  THR A O   
376  C  CB  . THR A 91  ? 0.2732 0.2519 0.1981 0.0304  -0.0415 -0.0608 59  THR A CB  
377  O  OG1 . THR A 91  ? 0.2900 0.2466 0.2287 0.0420  -0.0140 -0.0280 59  THR A OG1 
378  C  CG2 . THR A 91  ? 0.2896 0.2536 0.2249 0.0344  -0.0274 -0.0709 59  THR A CG2 
379  N  N   . THR A 92  ? 0.2608 0.2582 0.2243 0.0610  -0.0220 -0.0463 60  THR A N   
380  C  CA  . THR A 92  ? 0.2381 0.2680 0.2184 0.0494  0.0080  -0.0408 60  THR A CA  
381  C  C   . THR A 92  ? 0.2666 0.2649 0.2126 0.0300  0.0310  -0.0134 60  THR A C   
382  O  O   . THR A 92  ? 0.2760 0.2616 0.1942 0.0167  0.0396  -0.0186 60  THR A O   
383  C  CB  . THR A 92  ? 0.3078 0.3022 0.2357 0.0553  -0.0275 -0.0469 60  THR A CB  
384  O  OG1 . THR A 92  ? 0.3330 0.2882 0.2276 0.0571  0.0124  -0.0514 60  THR A OG1 
385  C  CG2 . THR A 92  ? 0.3471 0.3478 0.2719 0.0386  -0.0433 -0.0614 60  THR A CG2 
386  N  N   . GLU A 93  ? 0.2891 0.2655 0.2489 0.0308  0.0622  -0.0065 61  GLU A N   
387  C  CA  . GLU A 93  ? 0.3030 0.2874 0.2791 0.0232  0.0825  0.0170  61  GLU A CA  
388  C  C   . GLU A 93  ? 0.2955 0.2816 0.2719 0.0317  0.0444  0.0134  61  GLU A C   
389  O  O   . GLU A 93  ? 0.2948 0.2735 0.2922 -0.0052 0.0217  0.0060  61  GLU A O   
390  C  CB  . GLU A 93  ? 0.3979 0.3477 0.3578 0.0273  0.0810  0.0523  61  GLU A CB  
391  C  CG  . GLU A 93  ? 0.5638 0.4541 0.4524 -0.0193 0.0494  0.0530  61  GLU A CG  
392  C  CD  . GLU A 93  ? 0.6957 0.5476 0.5362 -0.0590 0.0163  0.0433  61  GLU A CD  
393  O  OE1 . GLU A 93  ? 0.7409 0.5887 0.5629 -0.0828 0.0142  0.0397  61  GLU A OE1 
394  O  OE2 . GLU A 93  ? 0.7496 0.5939 0.5606 -0.0581 0.0085  0.0425  61  GLU A OE2 
395  N  N   . GLU A 94  ? 0.2660 0.2627 0.2484 0.0250  0.0614  -0.0034 62  GLU A N   
396  C  CA  . GLU A 94  ? 0.2726 0.2577 0.2567 0.0334  0.0390  -0.0179 62  GLU A CA  
397  C  C   . GLU A 94  ? 0.2286 0.2390 0.2348 0.0169  0.0288  -0.0322 62  GLU A C   
398  O  O   . GLU A 94  ? 0.2169 0.2611 0.2673 0.0091  0.0110  -0.0202 62  GLU A O   
399  C  CB  . GLU A 94  ? 0.3575 0.2959 0.3058 0.0507  0.0410  -0.0046 62  GLU A CB  
400  C  CG  . GLU A 94  ? 0.4486 0.3487 0.3860 0.0454  0.0681  0.0172  62  GLU A CG  
401  C  CD  . GLU A 94  ? 0.5545 0.4034 0.4678 0.0331  0.0706  0.0539  62  GLU A CD  
402  O  OE1 . GLU A 94  ? 0.6345 0.4408 0.5235 0.0326  0.0829  0.0661  62  GLU A OE1 
403  O  OE2 . GLU A 94  ? 0.5624 0.4161 0.4389 0.0423  0.0600  0.0573  62  GLU A OE2 
404  N  N   . GLU A 95  ? 0.2159 0.2287 0.2098 0.0058  0.0105  -0.0482 63  GLU A N   
405  C  CA  . GLU A 95  ? 0.2377 0.2244 0.2266 -0.0075 -0.0070 -0.0430 63  GLU A CA  
406  C  C   . GLU A 95  ? 0.2001 0.2090 0.1906 0.0087  -0.0232 -0.0668 63  GLU A C   
407  O  O   . GLU A 95  ? 0.1974 0.2182 0.2090 0.0070  -0.0276 -0.0447 63  GLU A O   
408  C  CB  . GLU A 95  ? 0.2238 0.2663 0.2634 -0.0299 -0.0108 -0.0494 63  GLU A CB  
409  C  CG  . GLU A 95  ? 0.2632 0.2990 0.3335 -0.0137 -0.0186 -0.0584 63  GLU A CG  
410  C  CD  . GLU A 95  ? 0.3306 0.3140 0.4218 -0.0216 0.0022  -0.0883 63  GLU A CD  
411  O  OE1 . GLU A 95  ? 0.3949 0.3228 0.4719 -0.0014 0.0251  -0.0788 63  GLU A OE1 
412  O  OE2 . GLU A 95  ? 0.2974 0.3194 0.4373 -0.0014 -0.0197 -0.0993 63  GLU A OE2 
413  N  N   . PHE A 96  ? 0.2002 0.2035 0.2145 0.0138  0.0154  -0.0647 64  PHE A N   
414  C  CA  . PHE A 96  ? 0.1982 0.2040 0.2079 0.0090  -0.0134 -0.0710 64  PHE A CA  
415  C  C   . PHE A 96  ? 0.1954 0.2064 0.2307 0.0320  -0.0042 -0.0506 64  PHE A C   
416  O  O   . PHE A 96  ? 0.2133 0.2068 0.2594 -0.0052 -0.0154 -0.0618 64  PHE A O   
417  C  CB  . PHE A 96  ? 0.2227 0.1915 0.2024 0.0500  -0.0322 -0.0588 64  PHE A CB  
418  C  CG  . PHE A 96  ? 0.2386 0.2161 0.2129 0.0460  -0.0494 -0.0478 64  PHE A CG  
419  C  CD1 . PHE A 96  ? 0.2414 0.2384 0.2293 0.0364  -0.0701 -0.0612 64  PHE A CD1 
420  C  CD2 . PHE A 96  ? 0.3096 0.2233 0.2320 0.0163  -0.0348 -0.0771 64  PHE A CD2 
421  C  CE1 . PHE A 96  ? 0.2638 0.2504 0.2407 -0.0039 -0.0536 -0.0658 64  PHE A CE1 
422  C  CE2 . PHE A 96  ? 0.3662 0.2524 0.2360 0.0073  -0.0245 -0.0839 64  PHE A CE2 
423  C  CZ  . PHE A 96  ? 0.3024 0.2649 0.2265 0.0306  -0.0330 -0.0618 64  PHE A CZ  
424  N  N   . VAL A 97  ? 0.1758 0.2032 0.2144 0.0341  0.0055  -0.0527 65  VAL A N   
425  C  CA  . VAL A 97  ? 0.1482 0.1939 0.2121 0.0253  -0.0215 -0.0476 65  VAL A CA  
426  C  C   . VAL A 97  ? 0.1610 0.2043 0.2026 -0.0010 0.0214  -0.0509 65  VAL A C   
427  O  O   . VAL A 97  ? 0.1756 0.2271 0.2010 0.0031  0.0272  -0.0407 65  VAL A O   
428  C  CB  . VAL A 97  ? 0.1753 0.1896 0.1960 0.0049  0.0315  -0.0451 65  VAL A CB  
429  C  CG1 . VAL A 97  ? 0.2400 0.1943 0.1720 0.0121  -0.0006 -0.0547 65  VAL A CG1 
430  C  CG2 . VAL A 97  ? 0.1983 0.2009 0.2295 0.0042  0.0066  -0.0288 65  VAL A CG2 
431  N  N   . GLU A 98  ? 0.1526 0.2245 0.2122 -0.0045 0.0166  -0.0505 66  GLU A N   
432  C  CA  . GLU A 98  ? 0.1662 0.2799 0.2326 0.0236  0.0236  -0.0583 66  GLU A CA  
433  C  C   . GLU A 98  ? 0.1879 0.2527 0.2228 0.0262  0.0210  -0.0417 66  GLU A C   
434  O  O   . GLU A 98  ? 0.2635 0.2183 0.2310 0.0298  0.0238  -0.0393 66  GLU A O   
435  C  CB  . GLU A 98  ? 0.2211 0.3752 0.2530 -0.0007 0.0431  -0.0937 66  GLU A CB  
436  C  CG  . GLU A 98  ? 0.3083 0.4257 0.3174 -0.0218 -0.0082 -0.1213 66  GLU A CG  
437  C  CD  . GLU A 98  ? 0.3066 0.4535 0.3391 -0.0134 -0.0343 -0.1525 66  GLU A CD  
438  O  OE1 . GLU A 98  ? 0.3289 0.4731 0.3848 0.0014  -0.0231 -0.1501 66  GLU A OE1 
439  O  OE2 . GLU A 98  ? 0.3201 0.4454 0.3190 -0.0339 -0.0102 -0.1672 66  GLU A OE2 
440  N  N   . GLY A 99  ? 0.1845 0.2315 0.1794 0.0130  0.0283  -0.0359 67  GLY A N   
441  C  CA  . GLY A 99  ? 0.2192 0.2313 0.1919 0.0400  0.0543  -0.0384 67  GLY A CA  
442  C  C   . GLY A 99  ? 0.1941 0.2163 0.1769 0.0444  0.0180  -0.0499 67  GLY A C   
443  O  O   . GLY A 99  ? 0.2291 0.2171 0.1923 0.0147  -0.0053 -0.0562 67  GLY A O   
444  N  N   . ILE A 100 ? 0.1757 0.2275 0.2010 0.0320  0.0045  -0.0407 68  ILE A N   
445  C  CA  . ILE A 100 ? 0.1732 0.2338 0.1676 0.0038  -0.0047 -0.0388 68  ILE A CA  
446  C  C   . ILE A 100 ? 0.1715 0.2024 0.1843 -0.0032 -0.0024 -0.0494 68  ILE A C   
447  O  O   . ILE A 100 ? 0.1882 0.1939 0.2238 -0.0036 -0.0089 -0.0317 68  ILE A O   
448  C  CB  . ILE A 100 ? 0.1730 0.2786 0.1640 0.0133  -0.0194 -0.0179 68  ILE A CB  
449  C  CG1 . ILE A 100 ? 0.2279 0.3241 0.2045 -0.0149 -0.0616 -0.0045 68  ILE A CG1 
450  C  CG2 . ILE A 100 ? 0.2287 0.2881 0.1684 0.0307  0.0433  -0.0255 68  ILE A CG2 
451  C  CD1 . ILE A 100 ? 0.2576 0.3633 0.2302 0.0013  -0.0555 0.0085  68  ILE A CD1 
452  N  N   . TYR A 101 ? 0.1547 0.1990 0.1608 0.0125  0.0014  -0.0306 69  TYR A N   
453  C  CA  . TYR A 101 ? 0.1418 0.1977 0.1654 0.0131  -0.0006 -0.0237 69  TYR A CA  
454  C  C   . TYR A 101 ? 0.1511 0.1901 0.1713 0.0010  -0.0027 -0.0188 69  TYR A C   
455  O  O   . TYR A 101 ? 0.1624 0.2076 0.1934 -0.0091 -0.0114 -0.0430 69  TYR A O   
456  C  CB  . TYR A 101 ? 0.1585 0.1985 0.1447 -0.0047 0.0177  -0.0249 69  TYR A CB  
457  C  CG  . TYR A 101 ? 0.1401 0.2065 0.1528 0.0023  0.0341  -0.0328 69  TYR A CG  
458  C  CD1 . TYR A 101 ? 0.1587 0.2213 0.1587 0.0100  0.0173  -0.0236 69  TYR A CD1 
459  C  CD2 . TYR A 101 ? 0.1694 0.2015 0.1817 0.0032  0.0068  -0.0509 69  TYR A CD2 
460  C  CE1 . TYR A 101 ? 0.1796 0.2078 0.1705 0.0077  0.0156  -0.0390 69  TYR A CE1 
461  C  CE2 . TYR A 101 ? 0.1760 0.2105 0.1847 0.0131  0.0136  -0.0530 69  TYR A CE2 
462  C  CZ  . TYR A 101 ? 0.1528 0.1987 0.1894 0.0019  0.0179  -0.0529 69  TYR A CZ  
463  O  OH  . TYR A 101 ? 0.2009 0.2158 0.2073 -0.0017 0.0322  -0.0645 69  TYR A OH  
464  N  N   . LYS A 102 ? 0.1620 0.2048 0.1728 -0.0121 0.0105  -0.0321 70  LYS A N   
465  C  CA  . LYS A 102 ? 0.1379 0.2370 0.1550 0.0079  0.0086  -0.0206 70  LYS A CA  
466  C  C   . LYS A 102 ? 0.1579 0.2242 0.1699 0.0204  -0.0214 -0.0465 70  LYS A C   
467  O  O   . LYS A 102 ? 0.1784 0.2198 0.1819 0.0193  -0.0162 -0.0571 70  LYS A O   
468  C  CB  . LYS A 102 ? 0.1972 0.2599 0.1410 -0.0108 0.0407  0.0096  70  LYS A CB  
469  C  CG  . LYS A 102 ? 0.2218 0.2833 0.1928 -0.0334 0.0427  0.0094  70  LYS A CG  
470  C  CD  . LYS A 102 ? 0.2913 0.2946 0.2463 -0.0591 0.0716  0.0199  70  LYS A CD  
471  C  CE  . LYS A 102 ? 0.3494 0.3369 0.2917 -0.0409 0.0800  0.0450  70  LYS A CE  
472  N  NZ  . LYS A 102 ? 0.4084 0.3850 0.3094 -0.0312 0.0634  0.0633  70  LYS A NZ  
473  N  N   . VAL A 103 ? 0.1423 0.2243 0.1769 0.0227  -0.0208 -0.0617 71  VAL A N   
474  C  CA  . VAL A 103 ? 0.1451 0.2408 0.1706 0.0127  -0.0327 -0.0557 71  VAL A CA  
475  C  C   . VAL A 103 ? 0.1600 0.2427 0.1862 0.0177  -0.0006 -0.0548 71  VAL A C   
476  O  O   . VAL A 103 ? 0.2146 0.2646 0.1827 0.0172  -0.0059 -0.0852 71  VAL A O   
477  C  CB  . VAL A 103 ? 0.1715 0.2663 0.1949 0.0526  -0.0261 -0.0558 71  VAL A CB  
478  C  CG1 . VAL A 103 ? 0.1967 0.2925 0.2111 0.0302  -0.0402 -0.0368 71  VAL A CG1 
479  C  CG2 . VAL A 103 ? 0.1886 0.2787 0.1994 0.0215  0.0135  -0.0524 71  VAL A CG2 
480  N  N   . GLU A 104 ? 0.1690 0.2345 0.1870 0.0026  0.0008  -0.0435 72  GLU A N   
481  C  CA  . GLU A 104 ? 0.2025 0.2118 0.1825 0.0266  -0.0028 -0.0111 72  GLU A CA  
482  C  C   . GLU A 104 ? 0.1937 0.2011 0.1677 0.0234  -0.0061 -0.0249 72  GLU A C   
483  O  O   . GLU A 104 ? 0.2049 0.2014 0.1890 0.0172  -0.0205 -0.0411 72  GLU A O   
484  C  CB  . GLU A 104 ? 0.2937 0.2432 0.2525 0.0221  -0.0460 0.0079  72  GLU A CB  
485  C  CG  . GLU A 104 ? 0.4677 0.2990 0.3433 -0.0235 0.0074  0.0052  72  GLU A CG  
486  C  CD  . GLU A 104 ? 0.5362 0.3383 0.3860 -0.0221 0.0200  0.0518  72  GLU A CD  
487  O  OE1 . GLU A 104 ? 0.5746 0.3934 0.4345 -0.0315 0.0969  0.0531  72  GLU A OE1 
488  O  OE2 . GLU A 104 ? 0.5285 0.3278 0.3720 -0.0355 0.0213  0.0365  72  GLU A OE2 
489  N  N   . ILE A 105 ? 0.1683 0.1855 0.1634 0.0378  0.0136  -0.0195 73  ILE A N   
490  C  CA  . ILE A 105 ? 0.1587 0.1868 0.1830 0.0256  0.0094  -0.0097 73  ILE A CA  
491  C  C   . ILE A 105 ? 0.1780 0.2022 0.1531 0.0112  0.0162  -0.0059 73  ILE A C   
492  O  O   . ILE A 105 ? 0.1909 0.2191 0.1439 0.0124  0.0130  -0.0076 73  ILE A O   
493  C  CB  . ILE A 105 ? 0.1846 0.1870 0.1926 0.0119  0.0271  -0.0114 73  ILE A CB  
494  C  CG1 . ILE A 105 ? 0.2046 0.2118 0.2055 -0.0147 0.0324  -0.0303 73  ILE A CG1 
495  C  CG2 . ILE A 105 ? 0.2385 0.2140 0.1770 0.0341  0.0527  -0.0150 73  ILE A CG2 
496  C  CD1 . ILE A 105 ? 0.2712 0.2124 0.2070 -0.0459 0.0278  -0.0305 73  ILE A CD1 
497  N  N   . ASP A 106 ? 0.1629 0.1929 0.1865 0.0085  -0.0005 -0.0291 74  ASP A N   
498  C  CA  . ASP A 106 ? 0.1624 0.1985 0.2264 -0.0010 0.0201  -0.0333 74  ASP A CA  
499  C  C   . ASP A 106 ? 0.1519 0.2001 0.1942 0.0023  0.0182  -0.0253 74  ASP A C   
500  O  O   . ASP A 106 ? 0.1825 0.2210 0.1992 -0.0037 -0.0098 -0.0117 74  ASP A O   
501  C  CB  . ASP A 106 ? 0.1599 0.2179 0.2978 -0.0272 0.0218  -0.0308 74  ASP A CB  
502  C  CG  . ASP A 106 ? 0.2169 0.2529 0.3539 -0.0217 0.0191  -0.0443 74  ASP A CG  
503  O  OD1 . ASP A 106 ? 0.2345 0.2651 0.3522 -0.0231 0.0484  -0.0061 74  ASP A OD1 
504  O  OD2 . ASP A 106 ? 0.2776 0.2911 0.3987 -0.0455 0.0108  -0.0619 74  ASP A OD2 
505  N  N   . THR A 107 ? 0.2022 0.1801 0.1813 -0.0156 0.0635  -0.0251 75  THR A N   
506  C  CA  . THR A 107 ? 0.1982 0.1823 0.1580 0.0002  0.0489  -0.0268 75  THR A CA  
507  C  C   . THR A 107 ? 0.1906 0.1839 0.1914 -0.0011 0.0280  -0.0026 75  THR A C   
508  O  O   . THR A 107 ? 0.1675 0.1989 0.2038 0.0011  -0.0114 0.0036  75  THR A O   
509  C  CB  . THR A 107 ? 0.1867 0.1885 0.1808 -0.0110 0.0316  -0.0112 75  THR A CB  
510  O  OG1 . THR A 107 ? 0.1933 0.1962 0.1866 0.0013  0.0130  0.0193  75  THR A OG1 
511  C  CG2 . THR A 107 ? 0.1836 0.2219 0.2058 0.0081  0.0521  0.0019  75  THR A CG2 
512  N  N   . LYS A 108 ? 0.1687 0.2075 0.1814 -0.0277 0.0383  0.0297  76  LYS A N   
513  C  CA  . LYS A 108 ? 0.1713 0.2161 0.1923 -0.0470 0.0262  0.0655  76  LYS A CA  
514  C  C   . LYS A 108 ? 0.1777 0.2303 0.2301 -0.0345 0.0050  0.0275  76  LYS A C   
515  O  O   . LYS A 108 ? 0.1662 0.2606 0.2612 -0.0163 0.0238  0.0228  76  LYS A O   
516  C  CB  . LYS A 108 ? 0.1997 0.2381 0.2153 -0.0368 0.0359  0.0933  76  LYS A CB  
517  C  CG  . LYS A 108 ? 0.2573 0.2784 0.2429 -0.0249 0.0292  0.1173  76  LYS A CG  
518  C  CD  . LYS A 108 ? 0.2732 0.3298 0.2712 -0.0558 0.0071  0.1432  76  LYS A CD  
519  C  CE  . LYS A 108 ? 0.3132 0.3673 0.3143 -0.0471 0.0136  0.1265  76  LYS A CE  
520  N  NZ  . LYS A 108 ? 0.3339 0.3953 0.3437 -0.0673 0.0042  0.1177  76  LYS A NZ  
521  N  N   . SER A 109 ? 0.2139 0.2485 0.2405 -0.0216 -0.0168 0.0129  77  SER A N   
522  C  CA  . SER A 109 ? 0.2356 0.2454 0.2754 -0.0046 -0.0273 0.0043  77  SER A CA  
523  C  C   . SER A 109 ? 0.2148 0.2405 0.2822 -0.0032 -0.0170 0.0225  77  SER A C   
524  O  O   . SER A 109 ? 0.2105 0.2617 0.3006 -0.0102 -0.0137 0.0259  77  SER A O   
525  C  CB  . SER A 109 ? 0.2721 0.2443 0.3190 -0.0142 0.0029  -0.0013 77  SER A CB  
526  O  OG  . SER A 109 ? 0.2831 0.2517 0.3722 -0.0405 0.0134  -0.0121 77  SER A OG  
527  N  N   . TYR A 110 ? 0.2385 0.2082 0.2602 -0.0576 -0.0292 0.0050  78  TYR A N   
528  C  CA  . TYR A 110 ? 0.2229 0.2269 0.2620 -0.0437 -0.0036 0.0368  78  TYR A CA  
529  C  C   . TYR A 110 ? 0.2160 0.2352 0.2582 -0.0171 -0.0167 0.0441  78  TYR A C   
530  O  O   . TYR A 110 ? 0.1776 0.2845 0.2647 -0.0225 -0.0099 0.0355  78  TYR A O   
531  C  CB  . TYR A 110 ? 0.1879 0.2092 0.2336 -0.0445 0.0187  0.0376  78  TYR A CB  
532  C  CG  . TYR A 110 ? 0.2158 0.2125 0.2083 -0.0272 -0.0017 0.0188  78  TYR A CG  
533  C  CD1 . TYR A 110 ? 0.2603 0.2306 0.1982 -0.0074 -0.0017 0.0078  78  TYR A CD1 
534  C  CD2 . TYR A 110 ? 0.1845 0.2277 0.2169 -0.0218 0.0224  -0.0061 78  TYR A CD2 
535  C  CE1 . TYR A 110 ? 0.2402 0.2147 0.2102 -0.0226 0.0189  -0.0155 78  TYR A CE1 
536  C  CE2 . TYR A 110 ? 0.1998 0.2278 0.2254 -0.0323 0.0150  0.0086  78  TYR A CE2 
537  C  CZ  . TYR A 110 ? 0.2369 0.2102 0.1984 -0.0121 0.0026  -0.0018 78  TYR A CZ  
538  O  OH  . TYR A 110 ? 0.2517 0.2209 0.2411 -0.0179 0.0041  0.0038  78  TYR A OH  
539  N  N   . TRP A 111 ? 0.1904 0.2320 0.2368 0.0101  -0.0097 0.0363  79  TRP A N   
540  C  CA  . TRP A 111 ? 0.1623 0.2551 0.2517 -0.0038 -0.0067 0.0459  79  TRP A CA  
541  C  C   . TRP A 111 ? 0.1668 0.2949 0.3133 -0.0174 0.0247  0.0540  79  TRP A C   
542  O  O   . TRP A 111 ? 0.1363 0.3268 0.3472 0.0092  0.0212  0.0438  79  TRP A O   
543  C  CB  . TRP A 111 ? 0.1741 0.2242 0.2164 -0.0136 0.0017  0.0337  79  TRP A CB  
544  C  CG  . TRP A 111 ? 0.1619 0.2162 0.2124 -0.0039 -0.0007 0.0382  79  TRP A CG  
545  C  CD1 . TRP A 111 ? 0.1647 0.2106 0.2007 0.0158  0.0010  0.0110  79  TRP A CD1 
546  C  CD2 . TRP A 111 ? 0.1641 0.2015 0.2020 0.0334  0.0131  0.0262  79  TRP A CD2 
547  N  NE1 . TRP A 111 ? 0.1874 0.1852 0.1735 0.0184  0.0057  0.0021  79  TRP A NE1 
548  C  CE2 . TRP A 111 ? 0.1759 0.1931 0.1930 0.0355  0.0041  0.0107  79  TRP A CE2 
549  C  CE3 . TRP A 111 ? 0.2243 0.2141 0.2243 0.0291  -0.0032 0.0214  79  TRP A CE3 
550  C  CZ2 . TRP A 111 ? 0.1933 0.1795 0.2036 0.0346  0.0111  0.0028  79  TRP A CZ2 
551  C  CZ3 . TRP A 111 ? 0.2067 0.2083 0.2229 0.0144  -0.0302 0.0054  79  TRP A CZ3 
552  C  CH2 . TRP A 111 ? 0.1959 0.1977 0.2245 0.0244  -0.0177 -0.0184 79  TRP A CH2 
553  N  N   . LYS A 112 ? 0.1639 0.2969 0.3236 -0.0464 0.0059  0.0395  80  LYS A N   
554  C  CA  . LYS A 112 ? 0.1687 0.3442 0.3530 -0.0517 0.0044  0.0529  80  LYS A CA  
555  C  C   . LYS A 112 ? 0.2074 0.3859 0.3649 -0.0449 -0.0247 0.0662  80  LYS A C   
556  O  O   . LYS A 112 ? 0.1959 0.4215 0.3684 -0.0384 -0.0323 0.0747  80  LYS A O   
557  C  CB  . LYS A 112 ? 0.2098 0.3644 0.3834 -0.0657 -0.0283 0.0541  80  LYS A CB  
558  C  CG  . LYS A 112 ? 0.2823 0.3762 0.4115 -0.0600 -0.0248 0.0527  80  LYS A CG  
559  C  CD  . LYS A 112 ? 0.4169 0.4023 0.4515 -0.0588 -0.0154 0.0483  80  LYS A CD  
560  C  CE  . LYS A 112 ? 0.5381 0.4430 0.5002 -0.0496 -0.0202 0.0247  80  LYS A CE  
561  N  NZ  . LYS A 112 ? 0.5774 0.4696 0.5303 -0.0505 -0.0385 0.0179  80  LYS A NZ  
562  N  N   . ALA A 113 ? 0.2196 0.4000 0.3626 -0.0436 -0.0482 0.0589  81  ALA A N   
563  C  CA  . ALA A 113 ? 0.2149 0.4282 0.4009 -0.0128 -0.0981 0.0620  81  ALA A CA  
564  C  C   . ALA A 113 ? 0.2454 0.4451 0.4196 -0.0116 -0.1215 0.0880  81  ALA A C   
565  O  O   . ALA A 113 ? 0.2476 0.4759 0.4265 -0.0268 -0.1538 0.0946  81  ALA A O   
566  C  CB  . ALA A 113 ? 0.2356 0.4391 0.4090 -0.0433 -0.0802 0.0623  81  ALA A CB  
567  N  N   . LEU A 114 ? 0.2540 0.4393 0.4623 0.0112  -0.0761 0.0820  82  LEU A N   
568  C  CA  . LEU A 114 ? 0.2958 0.4418 0.4849 0.0148  -0.0804 0.0627  82  LEU A CA  
569  C  C   . LEU A 114 ? 0.2888 0.4500 0.5101 0.0184  -0.0488 0.0402  82  LEU A C   
570  O  O   . LEU A 114 ? 0.3153 0.4393 0.5298 0.0271  -0.0456 0.0316  82  LEU A O   
571  C  CB  . LEU A 114 ? 0.3064 0.4325 0.4700 0.0273  -0.0834 0.0823  82  LEU A CB  
572  C  CG  . LEU A 114 ? 0.3240 0.4436 0.4556 0.0566  -0.1112 0.0970  82  LEU A CG  
573  C  CD1 . LEU A 114 ? 0.3420 0.4459 0.4659 0.0604  -0.1044 0.0895  82  LEU A CD1 
574  C  CD2 . LEU A 114 ? 0.3543 0.4607 0.4519 0.0551  -0.1157 0.0889  82  LEU A CD2 
575  N  N   . GLY A 115 ? 0.2827 0.4898 0.5102 0.0372  -0.0410 0.0249  83  GLY A N   
576  C  CA  . GLY A 115 ? 0.3226 0.5101 0.5005 0.0280  -0.0345 -0.0005 83  GLY A CA  
577  C  C   . GLY A 115 ? 0.3301 0.5364 0.4980 0.0229  0.0052  -0.0155 83  GLY A C   
578  O  O   . GLY A 115 ? 0.2927 0.5631 0.5047 0.0103  -0.0199 -0.0357 83  GLY A O   
579  N  N   . ILE A 116 ? 0.2772 0.5286 0.4826 0.0122  0.0544  -0.0147 84  ILE A N   
580  C  CA  . ILE A 116 ? 0.3490 0.5148 0.4687 0.0201  0.0815  -0.0243 84  ILE A CA  
581  C  C   . ILE A 116 ? 0.3242 0.4933 0.4371 0.0201  0.0767  -0.0176 84  ILE A C   
582  O  O   . ILE A 116 ? 0.3212 0.4980 0.4428 0.0363  0.0458  -0.0099 84  ILE A O   
583  C  CB  . ILE A 116 ? 0.4085 0.5233 0.4896 0.0049  0.0743  -0.0352 84  ILE A CB  
584  C  CG1 . ILE A 116 ? 0.4540 0.5396 0.5061 0.0239  0.0502  -0.0457 84  ILE A CG1 
585  C  CG2 . ILE A 116 ? 0.4350 0.5309 0.4938 -0.0201 0.0811  -0.0296 84  ILE A CG2 
586  C  CD1 . ILE A 116 ? 0.4881 0.5444 0.5062 0.0382  0.0332  -0.0609 84  ILE A CD1 
587  N  N   . SER A 117 ? 0.2893 0.4786 0.4160 -0.0053 0.1211  -0.0208 85  SER A N   
588  C  CA  . SER A 117 ? 0.2983 0.4596 0.3932 -0.0433 0.1088  -0.0121 85  SER A CA  
589  C  C   . SER A 117 ? 0.2621 0.4053 0.3411 -0.0305 0.0815  -0.0251 85  SER A C   
590  O  O   . SER A 117 ? 0.2634 0.4316 0.3761 0.0018  0.1092  -0.0589 85  SER A O   
591  C  CB  . SER A 117 ? 0.3942 0.4954 0.4193 -0.0886 0.1126  -0.0069 85  SER A CB  
592  O  OG  . SER A 117 ? 0.5255 0.5185 0.4511 -0.0890 0.0967  0.0105  85  SER A OG  
593  N  N   . PRO A 118 ? 0.2401 0.3296 0.2531 0.0020  0.0666  0.0104  86  PRO A N   
594  C  CA  . PRO A 118 ? 0.2177 0.2901 0.2179 0.0203  0.0612  0.0269  86  PRO A CA  
595  C  C   . PRO A 118 ? 0.2301 0.2517 0.2264 0.0110  0.0568  0.0363  86  PRO A C   
596  O  O   . PRO A 118 ? 0.2813 0.2629 0.2422 -0.0392 0.0472  0.0467  86  PRO A O   
597  C  CB  . PRO A 118 ? 0.2590 0.3107 0.2259 0.0178  0.0547  0.0251  86  PRO A CB  
598  C  CG  . PRO A 118 ? 0.2665 0.3049 0.2341 0.0422  0.0505  0.0208  86  PRO A CG  
599  C  CD  . PRO A 118 ? 0.2779 0.3235 0.2493 -0.0067 0.0457  0.0108  86  PRO A CD  
600  N  N   . PHE A 119 ? 0.2029 0.2241 0.2077 0.0231  0.0514  0.0201  87  PHE A N   
601  C  CA  . PHE A 119 ? 0.2198 0.2035 0.1878 0.0136  0.0283  -0.0080 87  PHE A CA  
602  C  C   . PHE A 119 ? 0.1957 0.1931 0.1594 0.0102  0.0667  -0.0010 87  PHE A C   
603  O  O   . PHE A 119 ? 0.2218 0.1804 0.1857 0.0200  0.0345  0.0376  87  PHE A O   
604  C  CB  . PHE A 119 ? 0.2707 0.1843 0.1940 0.0218  0.0182  0.0007  87  PHE A CB  
605  C  CG  . PHE A 119 ? 0.3216 0.1735 0.1901 0.0120  -0.0138 0.0073  87  PHE A CG  
606  C  CD1 . PHE A 119 ? 0.3934 0.1937 0.1922 -0.0081 -0.0160 0.0190  87  PHE A CD1 
607  C  CD2 . PHE A 119 ? 0.3496 0.1668 0.2351 0.0055  -0.0271 0.0018  87  PHE A CD2 
608  C  CE1 . PHE A 119 ? 0.4043 0.2091 0.2065 -0.0059 -0.0479 0.0171  87  PHE A CE1 
609  C  CE2 . PHE A 119 ? 0.3723 0.1840 0.2222 -0.0238 -0.0507 -0.0029 87  PHE A CE2 
610  C  CZ  . PHE A 119 ? 0.3871 0.1969 0.2161 -0.0102 -0.0644 0.0053  87  PHE A CZ  
611  N  N   . HIS A 120 ? 0.1977 0.1884 0.1668 0.0185  0.0361  0.0084  88  HIS A N   
612  C  CA  . HIS A 120 ? 0.1956 0.1879 0.1652 0.0238  0.0385  0.0039  88  HIS A CA  
613  C  C   . HIS A 120 ? 0.1763 0.1897 0.1736 0.0055  0.0209  0.0049  88  HIS A C   
614  O  O   . HIS A 120 ? 0.1769 0.1950 0.1774 0.0089  -0.0182 0.0197  88  HIS A O   
615  C  CB  . HIS A 120 ? 0.1707 0.1946 0.1648 0.0017  0.0086  0.0119  88  HIS A CB  
616  C  CG  . HIS A 120 ? 0.1889 0.1810 0.1945 0.0181  -0.0004 0.0100  88  HIS A CG  
617  N  ND1 . HIS A 120 ? 0.2126 0.1756 0.2141 0.0078  -0.0072 0.0212  88  HIS A ND1 
618  C  CD2 . HIS A 120 ? 0.2091 0.1770 0.1939 -0.0133 -0.0046 0.0061  88  HIS A CD2 
619  C  CE1 . HIS A 120 ? 0.2230 0.1842 0.2168 0.0067  -0.0122 0.0112  88  HIS A CE1 
620  N  NE2 . HIS A 120 ? 0.2163 0.1711 0.2334 0.0010  -0.0016 0.0070  88  HIS A NE2 
621  N  N   . GLU A 121 ? 0.1937 0.1851 0.1717 0.0316  0.0272  0.0010  89  GLU A N   
622  C  CA  . GLU A 121 ? 0.2148 0.1996 0.1941 0.0205  0.0146  -0.0172 89  GLU A CA  
623  C  C   . GLU A 121 ? 0.1858 0.2339 0.1889 0.0152  0.0103  -0.0347 89  GLU A C   
624  O  O   . GLU A 121 ? 0.2248 0.2872 0.2152 0.0195  0.0037  -0.0339 89  GLU A O   
625  C  CB  . GLU A 121 ? 0.2298 0.2018 0.2133 0.0392  -0.0168 0.0030  89  GLU A CB  
626  C  CG  . GLU A 121 ? 0.2394 0.2543 0.2403 0.0020  -0.0261 0.0255  89  GLU A CG  
627  C  CD  . GLU A 121 ? 0.3139 0.3182 0.2835 -0.0197 -0.0257 0.0509  89  GLU A CD  
628  O  OE1 . GLU A 121 ? 0.3272 0.3473 0.2974 -0.0374 -0.0302 0.0405  89  GLU A OE1 
629  O  OE2 . GLU A 121 ? 0.3562 0.3507 0.3037 0.0272  -0.0431 0.0779  89  GLU A OE2 
630  N  N   . HIS A 122 ? 0.1743 0.2410 0.1798 0.0222  0.0351  -0.0271 90  HIS A N   
631  C  CA  . HIS A 122 ? 0.1782 0.2687 0.1766 0.0465  0.0474  -0.0452 90  HIS A CA  
632  C  C   . HIS A 122 ? 0.1720 0.3017 0.1534 -0.0147 0.0117  -0.0423 90  HIS A C   
633  O  O   . HIS A 122 ? 0.2109 0.3413 0.1577 -0.0340 0.0073  -0.0376 90  HIS A O   
634  C  CB  . HIS A 122 ? 0.2462 0.3036 0.2248 0.0616  0.0231  -0.0345 90  HIS A CB  
635  C  CG  . HIS A 122 ? 0.3565 0.3562 0.3026 0.1013  0.0245  -0.0515 90  HIS A CG  
636  N  ND1 . HIS A 122 ? 0.4273 0.3858 0.3438 0.1136  0.0186  -0.0185 90  HIS A ND1 
637  C  CD2 . HIS A 122 ? 0.4262 0.3737 0.3445 0.1212  -0.0337 -0.0521 90  HIS A CD2 
638  C  CE1 . HIS A 122 ? 0.4601 0.3911 0.3569 0.1198  -0.0152 -0.0259 90  HIS A CE1 
639  N  NE2 . HIS A 122 ? 0.4858 0.3940 0.3600 0.1165  -0.0548 -0.0390 90  HIS A NE2 
640  N  N   . ALA A 123 ? 0.1902 0.2974 0.1442 -0.0263 0.0334  -0.0233 91  ALA A N   
641  C  CA  . ALA A 123 ? 0.2061 0.2916 0.1776 -0.0308 0.0293  -0.0340 91  ALA A CA  
642  C  C   . ALA A 123 ? 0.1934 0.3142 0.2152 -0.0324 0.0567  -0.0683 91  ALA A C   
643  O  O   . ALA A 123 ? 0.2286 0.3208 0.2384 -0.0294 0.0153  -0.0899 91  ALA A O   
644  C  CB  . ALA A 123 ? 0.2316 0.2696 0.1854 -0.0161 0.0449  -0.0486 91  ALA A CB  
645  N  N   . GLU A 124 ? 0.2187 0.3530 0.2712 -0.0016 0.0699  -0.0619 92  GLU A N   
646  C  CA  . GLU A 124 ? 0.2388 0.3532 0.3504 -0.0146 0.0328  -0.0597 92  GLU A CA  
647  C  C   . GLU A 124 ? 0.2450 0.3247 0.3435 -0.0048 0.0452  -0.0780 92  GLU A C   
648  O  O   . GLU A 124 ? 0.2928 0.3486 0.4166 -0.0214 0.0333  -0.1226 92  GLU A O   
649  C  CB  . GLU A 124 ? 0.3736 0.4202 0.4363 -0.0085 0.0177  -0.0392 92  GLU A CB  
650  C  CG  . GLU A 124 ? 0.5122 0.4609 0.5408 -0.0149 0.0236  -0.0095 92  GLU A CG  
651  C  CD  . GLU A 124 ? 0.6258 0.5004 0.6158 -0.0021 0.0438  -0.0033 92  GLU A CD  
652  O  OE1 . GLU A 124 ? 0.6513 0.5181 0.6289 -0.0060 0.0780  0.0124  92  GLU A OE1 
653  O  OE2 . GLU A 124 ? 0.6658 0.5188 0.6532 0.0096  0.0362  -0.0142 92  GLU A OE2 
654  N  N   . VAL A 125 ? 0.1715 0.2816 0.2715 0.0158  0.0001  -0.0740 93  VAL A N   
655  C  CA  . VAL A 125 ? 0.2006 0.2301 0.2221 0.0186  -0.0030 -0.0311 93  VAL A CA  
656  C  C   . VAL A 125 ? 0.1726 0.2087 0.1951 0.0064  -0.0040 -0.0420 93  VAL A C   
657  O  O   . VAL A 125 ? 0.1928 0.2336 0.2081 0.0187  -0.0385 -0.0738 93  VAL A O   
658  C  CB  . VAL A 125 ? 0.2757 0.2261 0.2390 0.0185  0.0083  -0.0361 93  VAL A CB  
659  C  CG1 . VAL A 125 ? 0.2965 0.2674 0.2614 -0.0383 0.0064  -0.0148 93  VAL A CG1 
660  C  CG2 . VAL A 125 ? 0.3136 0.2344 0.2441 0.0390  0.0246  -0.0246 93  VAL A CG2 
661  N  N   . VAL A 126 ? 0.1639 0.1896 0.1687 0.0240  0.0029  -0.0182 94  VAL A N   
662  C  CA  . VAL A 126 ? 0.1852 0.2068 0.1673 0.0133  0.0008  0.0126  94  VAL A CA  
663  C  C   . VAL A 126 ? 0.1589 0.1979 0.1636 0.0035  0.0284  0.0084  94  VAL A C   
664  O  O   . VAL A 126 ? 0.2068 0.1873 0.1650 -0.0166 0.0094  -0.0229 94  VAL A O   
665  C  CB  . VAL A 126 ? 0.1726 0.2090 0.1968 0.0012  0.0125  0.0202  94  VAL A CB  
666  C  CG1 . VAL A 126 ? 0.1902 0.2092 0.2010 0.0338  0.0008  0.0130  94  VAL A CG1 
667  C  CG2 . VAL A 126 ? 0.1961 0.2459 0.2069 -0.0445 -0.0055 0.0259  94  VAL A CG2 
668  N  N   . PHE A 127 ? 0.1563 0.1892 0.1643 -0.0025 0.0301  0.0008  95  PHE A N   
669  C  CA  . PHE A 127 ? 0.1724 0.1880 0.1716 0.0197  0.0157  -0.0116 95  PHE A CA  
670  C  C   . PHE A 127 ? 0.1888 0.2097 0.1691 0.0018  0.0254  -0.0305 95  PHE A C   
671  O  O   . PHE A 127 ? 0.1997 0.1914 0.1682 -0.0057 -0.0032 -0.0348 95  PHE A O   
672  C  CB  . PHE A 127 ? 0.2038 0.1900 0.1664 0.0077  -0.0168 -0.0004 95  PHE A CB  
673  C  CG  . PHE A 127 ? 0.2467 0.2087 0.1932 0.0175  0.0023  0.0072  95  PHE A CG  
674  C  CD1 . PHE A 127 ? 0.2657 0.2021 0.2249 0.0182  -0.0519 0.0267  95  PHE A CD1 
675  C  CD2 . PHE A 127 ? 0.2977 0.2026 0.1672 0.0421  -0.0088 -0.0068 95  PHE A CD2 
676  C  CE1 . PHE A 127 ? 0.2969 0.2240 0.2436 -0.0008 -0.0504 0.0106  95  PHE A CE1 
677  C  CE2 . PHE A 127 ? 0.3351 0.2065 0.2036 0.0342  -0.0350 -0.0064 95  PHE A CE2 
678  C  CZ  . PHE A 127 ? 0.3491 0.2166 0.2152 0.0268  -0.0626 -0.0104 95  PHE A CZ  
679  N  N   . THR A 128 ? 0.1643 0.2278 0.1748 0.0150  0.0343  -0.0409 96  THR A N   
680  C  CA  . THR A 128 ? 0.1724 0.2385 0.1762 -0.0108 0.0472  -0.0336 96  THR A CA  
681  C  C   . THR A 128 ? 0.2176 0.2040 0.1836 -0.0367 0.0421  -0.0538 96  THR A C   
682  O  O   . THR A 128 ? 0.3268 0.2030 0.2057 -0.0596 0.0505  -0.0746 96  THR A O   
683  C  CB  . THR A 128 ? 0.1582 0.2558 0.2191 0.0187  0.0132  -0.0576 96  THR A CB  
684  O  OG1 . THR A 128 ? 0.2281 0.2871 0.2315 0.0425  -0.0015 -0.0479 96  THR A OG1 
685  C  CG2 . THR A 128 ? 0.2083 0.2870 0.2528 0.0064  0.0253  -0.0771 96  THR A CG2 
686  N  N   . ALA A 129 ? 0.2053 0.2122 0.1842 -0.0078 0.0392  -0.0540 97  ALA A N   
687  C  CA  . ALA A 129 ? 0.2114 0.2344 0.1795 -0.0251 0.0429  -0.0540 97  ALA A CA  
688  C  C   . ALA A 129 ? 0.2109 0.2205 0.2107 0.0011  0.0562  -0.0528 97  ALA A C   
689  O  O   . ALA A 129 ? 0.2558 0.2028 0.2331 0.0325  0.0847  -0.0354 97  ALA A O   
690  C  CB  . ALA A 129 ? 0.2483 0.2742 0.1977 -0.0272 0.0216  -0.0420 97  ALA A CB  
691  N  N   . ASN A 130 ? 0.2165 0.2410 0.2277 -0.0204 0.0708  -0.0343 98  ASN A N   
692  C  CA  . ASN A 130 ? 0.2443 0.2695 0.2774 0.0191  0.0866  -0.0279 98  ASN A CA  
693  C  C   . ASN A 130 ? 0.2314 0.3029 0.3443 0.0609  0.1176  0.0095  98  ASN A C   
694  O  O   . ASN A 130 ? 0.2902 0.3285 0.3796 0.0839  0.1281  0.0061  98  ASN A O   
695  C  CB  . ASN A 130 ? 0.2828 0.2667 0.2609 0.0206  0.0747  -0.0494 98  ASN A CB  
696  C  CG  . ASN A 130 ? 0.2781 0.2506 0.2574 -0.0104 0.0659  -0.0518 98  ASN A CG  
697  O  OD1 . ASN A 130 ? 0.2552 0.2448 0.2676 0.0029  0.0563  -0.0254 98  ASN A OD1 
698  N  ND2 . ASN A 130 ? 0.3215 0.2436 0.2450 -0.0446 0.0366  -0.0598 98  ASN A ND2 
699  N  N   . ASP A 131 ? 0.2596 0.3418 0.3820 0.0410  0.0612  0.0304  99  ASP A N   
700  C  CA  . ASP A 131 ? 0.3715 0.4122 0.4592 0.0194  0.0889  -0.0010 99  ASP A CA  
701  C  C   . ASP A 131 ? 0.3368 0.4284 0.4642 0.0145  0.0817  0.0002  99  ASP A C   
702  O  O   . ASP A 131 ? 0.3093 0.4529 0.4680 0.0512  0.0323  -0.0095 99  ASP A O   
703  C  CB  . ASP A 131 ? 0.5626 0.4539 0.5243 -0.0192 0.0721  -0.0247 99  ASP A CB  
704  C  CG  . ASP A 131 ? 0.7560 0.4904 0.5916 -0.0353 0.0935  -0.0551 99  ASP A CG  
705  O  OD1 . ASP A 131 ? 0.8194 0.5029 0.6160 -0.0318 0.0961  -0.0679 99  ASP A OD1 
706  O  OD2 . ASP A 131 ? 0.8356 0.4963 0.6185 -0.0378 0.1170  -0.0703 99  ASP A OD2 
707  N  N   . SER A 132 ? 0.3389 0.4258 0.4573 -0.0539 0.1158  0.0178  100 SER A N   
708  C  CA  . SER A 132 ? 0.3717 0.4262 0.4753 -0.0876 0.1240  0.0214  100 SER A CA  
709  C  C   . SER A 132 ? 0.3527 0.4072 0.4694 -0.0842 0.1265  0.0152  100 SER A C   
710  O  O   . SER A 132 ? 0.4234 0.4344 0.4949 -0.1154 0.1182  0.0286  100 SER A O   
711  C  CB  . SER A 132 ? 0.4935 0.4657 0.5062 -0.0932 0.0843  0.0190  100 SER A CB  
712  O  OG  . SER A 132 ? 0.5846 0.5020 0.5383 -0.0902 0.0662  0.0145  100 SER A OG  
713  N  N   . GLY A 133 ? 0.3007 0.3832 0.4230 -0.0101 0.1312  -0.0100 101 GLY A N   
714  C  CA  . GLY A 133 ? 0.2564 0.3553 0.3924 0.0010  0.1520  -0.0336 101 GLY A CA  
715  C  C   . GLY A 133 ? 0.2452 0.3314 0.3671 -0.0034 0.1624  -0.0522 101 GLY A C   
716  O  O   . GLY A 133 ? 0.2420 0.3085 0.3704 -0.0213 0.1184  -0.0329 101 GLY A O   
717  N  N   . PRO A 134 ? 0.2818 0.3434 0.3538 0.0217  0.1619  -0.0819 102 PRO A N   
718  C  CA  . PRO A 134 ? 0.2813 0.3209 0.3455 0.0180  0.1532  -0.0994 102 PRO A CA  
719  C  C   . PRO A 134 ? 0.2722 0.2835 0.3336 -0.0012 0.1414  -0.0973 102 PRO A C   
720  O  O   . PRO A 134 ? 0.3025 0.2824 0.3451 -0.0144 0.1096  -0.0699 102 PRO A O   
721  C  CB  . PRO A 134 ? 0.3257 0.3444 0.3559 0.0169  0.1473  -0.1076 102 PRO A CB  
722  C  CG  . PRO A 134 ? 0.3421 0.3757 0.3685 0.0208  0.1360  -0.1149 102 PRO A CG  
723  C  CD  . PRO A 134 ? 0.3060 0.3716 0.3449 0.0004  0.1510  -0.1193 102 PRO A CD  
724  N  N   . ARG A 135 ? 0.2691 0.2888 0.3049 0.0078  0.1313  -0.1091 103 ARG A N   
725  C  CA  . ARG A 135 ? 0.2586 0.2893 0.3015 0.0093  0.0924  -0.0927 103 ARG A CA  
726  C  C   . ARG A 135 ? 0.2297 0.2881 0.2863 0.0181  0.0937  -0.0759 103 ARG A C   
727  O  O   . ARG A 135 ? 0.2284 0.2829 0.2878 0.0130  0.0588  -0.0638 103 ARG A O   
728  C  CB  . ARG A 135 ? 0.2302 0.2883 0.3059 -0.0195 0.1017  -0.0860 103 ARG A CB  
729  C  CG  . ARG A 135 ? 0.2144 0.3160 0.3575 -0.0309 0.0735  -0.0571 103 ARG A CG  
730  C  CD  . ARG A 135 ? 0.2460 0.3584 0.4088 -0.0393 0.0695  -0.0368 103 ARG A CD  
731  N  NE  . ARG A 135 ? 0.2834 0.3801 0.4556 -0.0522 0.0549  -0.0254 103 ARG A NE  
732  C  CZ  . ARG A 135 ? 0.2706 0.4098 0.4781 -0.0808 0.0461  -0.0117 103 ARG A CZ  
733  N  NH1 . ARG A 135 ? 0.2822 0.4067 0.4867 -0.0711 0.0499  -0.0139 103 ARG A NH1 
734  N  NH2 . ARG A 135 ? 0.2900 0.4372 0.4960 -0.0711 0.0124  -0.0131 103 ARG A NH2 
735  N  N   . ARG A 136 ? 0.2138 0.3022 0.2642 0.0338  0.0884  -0.0591 104 ARG A N   
736  C  CA  . ARG A 136 ? 0.2414 0.3150 0.2618 0.0203  0.0948  -0.0841 104 ARG A CA  
737  C  C   . ARG A 136 ? 0.1941 0.2675 0.2242 -0.0149 0.0606  -0.0652 104 ARG A C   
738  O  O   . ARG A 136 ? 0.2407 0.2567 0.2555 -0.0335 0.0859  -0.0591 104 ARG A O   
739  C  CB  . ARG A 136 ? 0.3758 0.3980 0.3073 0.0149  0.1145  -0.0790 104 ARG A CB  
740  C  CG  . ARG A 136 ? 0.5306 0.4761 0.3961 -0.0003 0.1098  -0.0541 104 ARG A CG  
741  C  CD  . ARG A 136 ? 0.6664 0.5528 0.4955 -0.0219 0.0942  -0.0386 104 ARG A CD  
742  N  NE  . ARG A 136 ? 0.7869 0.6138 0.5981 -0.0428 0.0760  -0.0237 104 ARG A NE  
743  C  CZ  . ARG A 136 ? 0.8630 0.6575 0.6786 -0.0616 0.0597  -0.0101 104 ARG A CZ  
744  N  NH1 . ARG A 136 ? 0.8906 0.6718 0.6993 -0.0656 0.0444  -0.0097 104 ARG A NH1 
745  N  NH2 . ARG A 136 ? 0.8910 0.6716 0.6944 -0.0674 0.0524  -0.0080 104 ARG A NH2 
746  N  N   . TYR A 137 ? 0.1980 0.2507 0.2398 -0.0207 0.0499  -0.0476 105 TYR A N   
747  C  CA  . TYR A 137 ? 0.1789 0.2325 0.2069 -0.0215 0.0603  -0.0393 105 TYR A CA  
748  C  C   . TYR A 137 ? 0.1953 0.2279 0.2060 -0.0088 0.0409  -0.0620 105 TYR A C   
749  O  O   . TYR A 137 ? 0.2188 0.2251 0.2418 -0.0281 0.0295  -0.0862 105 TYR A O   
750  C  CB  . TYR A 137 ? 0.2050 0.2317 0.2349 -0.0321 0.0789  -0.0254 105 TYR A CB  
751  C  CG  . TYR A 137 ? 0.2023 0.2287 0.2421 -0.0229 0.0647  -0.0277 105 TYR A CG  
752  C  CD1 . TYR A 137 ? 0.2130 0.1993 0.2467 -0.0181 0.0704  -0.0329 105 TYR A CD1 
753  C  CD2 . TYR A 137 ? 0.2003 0.2385 0.2597 -0.0328 0.0422  -0.0324 105 TYR A CD2 
754  C  CE1 . TYR A 137 ? 0.2392 0.2107 0.2463 -0.0083 0.0319  -0.0539 105 TYR A CE1 
755  C  CE2 . TYR A 137 ? 0.1952 0.2439 0.2676 -0.0231 0.0468  -0.0238 105 TYR A CE2 
756  C  CZ  . TYR A 137 ? 0.2118 0.2064 0.2563 0.0085  0.0222  -0.0311 105 TYR A CZ  
757  O  OH  . TYR A 137 ? 0.2168 0.2229 0.2676 0.0151  -0.0049 -0.0334 105 TYR A OH  
758  N  N   . THR A 138 ? 0.1770 0.2245 0.1920 0.0051  0.0470  -0.0334 106 THR A N   
759  C  CA  . THR A 138 ? 0.2145 0.2253 0.1869 -0.0148 0.0253  -0.0160 106 THR A CA  
760  C  C   . THR A 138 ? 0.2029 0.2617 0.1913 -0.0266 0.0203  -0.0533 106 THR A C   
761  O  O   . THR A 138 ? 0.1932 0.2962 0.2116 -0.0360 0.0338  -0.0837 106 THR A O   
762  C  CB  . THR A 138 ? 0.2708 0.2398 0.2201 0.0264  0.0077  0.0018  106 THR A CB  
763  O  OG1 . THR A 138 ? 0.3577 0.2757 0.2468 0.0164  0.0201  0.0209  106 THR A OG1 
764  C  CG2 . THR A 138 ? 0.2941 0.2506 0.2614 0.0336  -0.0020 0.0003  106 THR A CG2 
765  N  N   . ILE A 139 ? 0.1762 0.2945 0.1887 -0.0202 0.0344  -0.0610 107 ILE A N   
766  C  CA  . ILE A 139 ? 0.1700 0.3054 0.1915 0.0009  0.0559  -0.0435 107 ILE A CA  
767  C  C   . ILE A 139 ? 0.1615 0.3002 0.1730 -0.0091 0.0181  -0.0654 107 ILE A C   
768  O  O   . ILE A 139 ? 0.1743 0.3034 0.1847 -0.0127 -0.0225 -0.0869 107 ILE A O   
769  C  CB  . ILE A 139 ? 0.2037 0.3345 0.2204 -0.0192 0.0336  -0.0291 107 ILE A CB  
770  C  CG1 . ILE A 139 ? 0.3003 0.3618 0.2542 -0.0317 0.0219  -0.0196 107 ILE A CG1 
771  C  CG2 . ILE A 139 ? 0.2263 0.3555 0.2183 -0.0117 0.0424  -0.0330 107 ILE A CG2 
772  C  CD1 . ILE A 139 ? 0.3505 0.3595 0.2840 -0.0197 -0.0071 -0.0229 107 ILE A CD1 
773  N  N   . ALA A 140 ? 0.1893 0.3054 0.1837 0.0051  0.0498  -0.0568 108 ALA A N   
774  C  CA  . ALA A 140 ? 0.2217 0.2870 0.1770 0.0171  0.0256  -0.0618 108 ALA A CA  
775  C  C   . ALA A 140 ? 0.1884 0.2887 0.1638 0.0230  -0.0027 -0.0427 108 ALA A C   
776  O  O   . ALA A 140 ? 0.1857 0.3468 0.1506 0.0372  -0.0213 -0.0373 108 ALA A O   
777  C  CB  . ALA A 140 ? 0.2725 0.2940 0.1945 0.0156  -0.0078 -0.0379 108 ALA A CB  
778  N  N   . ALA A 141 ? 0.1896 0.2433 0.1540 0.0264  0.0170  -0.0155 109 ALA A N   
779  C  CA  . ALA A 141 ? 0.1751 0.2284 0.1697 0.0329  -0.0001 -0.0037 109 ALA A CA  
780  C  C   . ALA A 141 ? 0.1786 0.2155 0.1419 0.0355  -0.0220 -0.0097 109 ALA A C   
781  O  O   . ALA A 141 ? 0.2002 0.2555 0.1452 0.0508  -0.0393 -0.0157 109 ALA A O   
782  C  CB  . ALA A 141 ? 0.2141 0.2341 0.2377 0.0043  0.0037  0.0097  109 ALA A CB  
783  N  N   . LEU A 142 ? 0.1658 0.2032 0.1311 0.0231  -0.0058 -0.0187 110 LEU A N   
784  C  CA  . LEU A 142 ? 0.1564 0.1967 0.1478 0.0104  0.0130  -0.0087 110 LEU A CA  
785  C  C   . LEU A 142 ? 0.1466 0.2172 0.1447 -0.0034 -0.0088 -0.0031 110 LEU A C   
786  O  O   . LEU A 142 ? 0.1657 0.2402 0.1665 -0.0073 -0.0178 0.0046  110 LEU A O   
787  C  CB  . LEU A 142 ? 0.2001 0.1932 0.1992 -0.0006 0.0064  -0.0036 110 LEU A CB  
788  C  CG  . LEU A 142 ? 0.2102 0.1938 0.1951 0.0079  -0.0067 -0.0047 110 LEU A CG  
789  C  CD1 . LEU A 142 ? 0.2023 0.2056 0.1955 0.0141  -0.0070 0.0374  110 LEU A CD1 
790  C  CD2 . LEU A 142 ? 0.2684 0.2251 0.2496 -0.0041 -0.0136 -0.0311 110 LEU A CD2 
791  N  N   . LEU A 143 ? 0.1523 0.1898 0.1338 0.0253  0.0138  -0.0031 111 LEU A N   
792  C  CA  . LEU A 143 ? 0.1619 0.1795 0.1197 0.0093  0.0115  -0.0039 111 LEU A CA  
793  C  C   . LEU A 143 ? 0.1864 0.1744 0.1300 0.0079  -0.0042 0.0095  111 LEU A C   
794  O  O   . LEU A 143 ? 0.1921 0.1514 0.1638 0.0286  0.0044  0.0311  111 LEU A O   
795  C  CB  . LEU A 143 ? 0.2124 0.1992 0.1357 0.0018  -0.0128 -0.0153 111 LEU A CB  
796  C  CG  . LEU A 143 ? 0.1927 0.1922 0.1368 0.0161  -0.0092 -0.0057 111 LEU A CG  
797  C  CD1 . LEU A 143 ? 0.2335 0.1865 0.1833 0.0041  -0.0092 -0.0272 111 LEU A CD1 
798  C  CD2 . LEU A 143 ? 0.1917 0.1759 0.1550 0.0243  0.0029  -0.0031 111 LEU A CD2 
799  N  N   . SER A 144 ? 0.1867 0.1783 0.1294 -0.0002 0.0003  0.0118  112 SER A N   
800  C  CA  . SER A 144 ? 0.1948 0.1711 0.1491 -0.0118 0.0067  -0.0028 112 SER A CA  
801  C  C   . SER A 144 ? 0.1680 0.1843 0.1524 0.0020  -0.0018 0.0121  112 SER A C   
802  O  O   . SER A 144 ? 0.1727 0.1779 0.1633 0.0173  0.0077  0.0179  112 SER A O   
803  C  CB  . SER A 144 ? 0.2335 0.1722 0.1474 -0.0161 0.0284  0.0085  112 SER A CB  
804  O  OG  . SER A 144 ? 0.2655 0.1815 0.1684 0.0014  0.0071  0.0008  112 SER A OG  
805  N  N   . PRO A 145 ? 0.1722 0.1864 0.1655 0.0335  0.0204  0.0226  113 PRO A N   
806  C  CA  . PRO A 145 ? 0.1766 0.2066 0.1628 0.0324  0.0321  0.0406  113 PRO A CA  
807  C  C   . PRO A 145 ? 0.2037 0.1841 0.1530 0.0105  0.0321  0.0212  113 PRO A C   
808  O  O   . PRO A 145 ? 0.2144 0.1643 0.1708 0.0129  0.0454  0.0144  113 PRO A O   
809  C  CB  . PRO A 145 ? 0.1684 0.2113 0.1774 0.0314  0.0267  0.0435  113 PRO A CB  
810  C  CG  . PRO A 145 ? 0.1908 0.2398 0.1848 0.0197  0.0150  0.0516  113 PRO A CG  
811  C  CD  . PRO A 145 ? 0.1759 0.2060 0.2097 0.0415  0.0290  0.0493  113 PRO A CD  
812  N  N   . TYR A 146 ? 0.1748 0.1933 0.1487 0.0144  -0.0002 0.0240  114 TYR A N   
813  C  CA  . TYR A 146 ? 0.1958 0.1935 0.1482 0.0101  0.0160  0.0113  114 TYR A CA  
814  C  C   . TYR A 146 ? 0.2045 0.2023 0.1486 -0.0022 0.0069  0.0150  114 TYR A C   
815  O  O   . TYR A 146 ? 0.2141 0.2366 0.1529 -0.0005 0.0147  0.0105  114 TYR A O   
816  C  CB  . TYR A 146 ? 0.2348 0.2051 0.1807 -0.0005 0.0582  0.0225  114 TYR A CB  
817  C  CG  . TYR A 146 ? 0.2215 0.2079 0.1827 -0.0026 0.0423  0.0371  114 TYR A CG  
818  C  CD1 . TYR A 146 ? 0.2898 0.2687 0.2165 -0.0305 0.0277  0.0419  114 TYR A CD1 
819  C  CD2 . TYR A 146 ? 0.2496 0.2125 0.1828 -0.0120 0.0913  0.0094  114 TYR A CD2 
820  C  CE1 . TYR A 146 ? 0.3587 0.3060 0.2334 -0.0448 0.0943  0.0606  114 TYR A CE1 
821  C  CE2 . TYR A 146 ? 0.2716 0.2558 0.2113 0.0085  0.1235  0.0269  114 TYR A CE2 
822  C  CZ  . TYR A 146 ? 0.3479 0.2867 0.2534 -0.0554 0.1168  0.0611  114 TYR A CZ  
823  O  OH  . TYR A 146 ? 0.3683 0.3434 0.2903 -0.0605 0.1404  0.0249  114 TYR A OH  
824  N  N   . SER A 147 ? 0.1730 0.1793 0.1722 0.0152  0.0168  0.0144  115 SER A N   
825  C  CA  . SER A 147 ? 0.1908 0.1985 0.1711 0.0009  -0.0028 0.0284  115 SER A CA  
826  C  C   . SER A 147 ? 0.1046 0.2271 0.1792 0.0303  0.0179  0.0411  115 SER A C   
827  O  O   . SER A 147 ? 0.1575 0.2647 0.1939 0.0255  -0.0243 0.0529  115 SER A O   
828  C  CB  . SER A 147 ? 0.2679 0.1995 0.2378 -0.0420 -0.0260 0.0349  115 SER A CB  
829  O  OG  . SER A 147 ? 0.3829 0.2476 0.2816 0.0133  -0.0140 0.0026  115 SER A OG  
830  N  N   . TYR A 148 ? 0.1516 0.2346 0.1475 0.0093  0.0241  0.0189  116 TYR A N   
831  C  CA  . TYR A 148 ? 0.1663 0.2452 0.1521 -0.0018 0.0149  -0.0005 116 TYR A CA  
832  C  C   . TYR A 148 ? 0.1614 0.2545 0.1490 0.0064  -0.0067 0.0099  116 TYR A C   
833  O  O   . TYR A 148 ? 0.1617 0.2638 0.1406 0.0046  -0.0065 0.0129  116 TYR A O   
834  C  CB  . TYR A 148 ? 0.1808 0.2499 0.1695 0.0175  -0.0091 0.0000  116 TYR A CB  
835  C  CG  . TYR A 148 ? 0.2014 0.2174 0.1819 0.0088  -0.0064 -0.0241 116 TYR A CG  
836  C  CD1 . TYR A 148 ? 0.2354 0.2235 0.1897 0.0063  -0.0256 -0.0266 116 TYR A CD1 
837  C  CD2 . TYR A 148 ? 0.2424 0.2092 0.1970 -0.0307 -0.0165 -0.0196 116 TYR A CD2 
838  C  CE1 . TYR A 148 ? 0.2801 0.2181 0.2378 -0.0042 -0.0461 -0.0272 116 TYR A CE1 
839  C  CE2 . TYR A 148 ? 0.2861 0.2105 0.2237 -0.0195 -0.0477 -0.0131 116 TYR A CE2 
840  C  CZ  . TYR A 148 ? 0.2674 0.2119 0.2545 0.0141  -0.0730 -0.0021 116 TYR A CZ  
841  O  OH  . TYR A 148 ? 0.3770 0.2283 0.3256 0.0093  -0.0697 0.0187  116 TYR A OH  
842  N  N   . SER A 149 ? 0.1462 0.2675 0.1664 -0.0018 -0.0291 0.0115  117 SER A N   
843  C  CA  A SER A 149 ? 0.1678 0.2732 0.1734 0.0049  -0.0025 0.0107  117 SER A CA  
844  C  CA  B SER A 149 ? 0.1753 0.2752 0.1920 -0.0154 0.0030  0.0090  117 SER A CA  
845  C  C   . SER A 149 ? 0.1630 0.2753 0.1782 -0.0094 -0.0176 -0.0046 117 SER A C   
846  O  O   . SER A 149 ? 0.1689 0.3179 0.1737 0.0011  -0.0149 -0.0076 117 SER A O   
847  C  CB  A SER A 149 ? 0.1976 0.2758 0.1931 -0.0174 0.0376  -0.0060 117 SER A CB  
848  C  CB  B SER A 149 ? 0.2061 0.2785 0.2482 -0.0804 0.0510  -0.0031 117 SER A CB  
849  O  OG  A SER A 149 ? 0.2543 0.2833 0.1789 0.0254  0.0244  -0.0207 117 SER A OG  
850  O  OG  B SER A 149 ? 0.2656 0.2965 0.2860 -0.0655 0.0529  -0.0069 117 SER A OG  
851  N  N   . THR A 150 ? 0.1819 0.2606 0.1446 -0.0115 0.0058  -0.0056 118 THR A N   
852  C  CA  . THR A 150 ? 0.1939 0.2524 0.1716 0.0019  -0.0101 -0.0265 118 THR A CA  
853  C  C   . THR A 150 ? 0.1783 0.2655 0.1770 0.0014  -0.0301 -0.0123 118 THR A C   
854  O  O   . THR A 150 ? 0.1722 0.2817 0.1772 -0.0076 -0.0226 -0.0223 118 THR A O   
855  C  CB  . THR A 150 ? 0.2559 0.2575 0.2057 -0.0002 -0.0294 -0.0061 118 THR A CB  
856  O  OG1 . THR A 150 ? 0.2651 0.2796 0.2290 -0.0012 -0.0023 -0.0279 118 THR A OG1 
857  C  CG2 . THR A 150 ? 0.2910 0.2627 0.2208 0.0248  -0.0557 -0.0024 118 THR A CG2 
858  N  N   . THR A 151 ? 0.1427 0.2309 0.1898 0.0156  -0.0033 -0.0113 119 THR A N   
859  C  CA  . THR A 151 ? 0.1762 0.2145 0.1989 -0.0142 0.0271  -0.0246 119 THR A CA  
860  C  C   . THR A 151 ? 0.1777 0.2251 0.1948 -0.0110 0.0160  -0.0438 119 THR A C   
861  O  O   . THR A 151 ? 0.1847 0.2766 0.2125 -0.0124 0.0217  -0.0764 119 THR A O   
862  C  CB  . THR A 151 ? 0.2258 0.2043 0.2415 -0.0029 -0.0102 -0.0086 119 THR A CB  
863  O  OG1 . THR A 151 ? 0.2632 0.2040 0.2559 -0.0124 0.0225  -0.0289 119 THR A OG1 
864  C  CG2 . THR A 151 ? 0.2817 0.2212 0.2383 0.0229  -0.0165 -0.0062 119 THR A CG2 
865  N  N   . ALA A 152 ? 0.2056 0.2075 0.1764 -0.0032 0.0114  -0.0232 120 ALA A N   
866  C  CA  . ALA A 152 ? 0.1953 0.1891 0.1864 -0.0007 0.0694  -0.0219 120 ALA A CA  
867  C  C   . ALA A 152 ? 0.1899 0.2060 0.1736 -0.0187 0.0334  -0.0242 120 ALA A C   
868  O  O   . ALA A 152 ? 0.1959 0.2191 0.2046 -0.0372 0.0228  -0.0457 120 ALA A O   
869  C  CB  . ALA A 152 ? 0.2088 0.1952 0.2265 0.0570  0.0485  0.0025  120 ALA A CB  
870  N  N   . VAL A 153 ? 0.2071 0.2146 0.1673 -0.0062 0.0395  -0.0154 121 VAL A N   
871  C  CA  . VAL A 153 ? 0.1996 0.2254 0.2060 -0.0148 0.0577  -0.0223 121 VAL A CA  
872  C  C   . VAL A 153 ? 0.2242 0.2404 0.2147 -0.0426 0.0763  -0.0465 121 VAL A C   
873  O  O   . VAL A 153 ? 0.2438 0.2542 0.2378 -0.0724 0.0532  -0.0599 121 VAL A O   
874  C  CB  . VAL A 153 ? 0.2896 0.2489 0.2279 0.0117  0.0591  0.0055  121 VAL A CB  
875  C  CG1 . VAL A 153 ? 0.3333 0.2618 0.2672 -0.0581 0.0386  0.0402  121 VAL A CG1 
876  C  CG2 . VAL A 153 ? 0.4055 0.2892 0.2832 0.0798  0.0316  -0.0063 121 VAL A CG2 
877  N  N   . VAL A 154 ? 0.2445 0.2426 0.2249 -0.0151 0.0935  -0.0480 122 VAL A N   
878  C  CA  . VAL A 154 ? 0.2280 0.2495 0.2368 -0.0208 0.1056  -0.0544 122 VAL A CA  
879  C  C   . VAL A 154 ? 0.2672 0.2361 0.2560 -0.0381 0.0964  -0.0510 122 VAL A C   
880  O  O   . VAL A 154 ? 0.2902 0.2130 0.3263 -0.0595 0.1086  -0.0592 122 VAL A O   
881  C  CB  . VAL A 154 ? 0.2706 0.2636 0.2749 -0.0055 0.1283  -0.0645 122 VAL A CB  
882  C  CG1 . VAL A 154 ? 0.3071 0.2772 0.2899 -0.0059 0.1314  -0.0725 122 VAL A CG1 
883  C  CG2 . VAL A 154 ? 0.3026 0.2670 0.2776 -0.0347 0.1290  -0.0650 122 VAL A CG2 
884  N  N   . THR A 155 ? 0.2808 0.2579 0.2589 -0.0213 0.1371  -0.0199 123 THR A N   
885  C  CA  . THR A 155 ? 0.3184 0.3175 0.3037 -0.0311 0.1632  0.0108  123 THR A CA  
886  C  C   . THR A 155 ? 0.3146 0.3186 0.3439 -0.0282 0.1622  -0.0195 123 THR A C   
887  O  O   . THR A 155 ? 0.3057 0.3310 0.3198 -0.0479 0.1457  -0.0328 123 THR A O   
888  C  CB  . THR A 155 ? 0.4064 0.3641 0.3664 -0.0195 0.1121  0.0287  123 THR A CB  
889  O  OG1 . THR A 155 ? 0.4896 0.4067 0.4086 -0.0500 0.0781  0.0423  123 THR A OG1 
890  C  CG2 . THR A 155 ? 0.3815 0.3625 0.3612 0.0239  0.1097  0.0368  123 THR A CG2 
891  N  N   . ASN A 156 ? 0.3336 0.3376 0.4142 -0.0424 0.1852  -0.0498 124 ASN A N   
892  C  CA  . ASN A 156 ? 0.4177 0.3856 0.4870 -0.0465 0.1975  -0.0342 124 ASN A CA  
893  C  C   . ASN A 156 ? 0.5229 0.4344 0.5387 -0.0395 0.1996  -0.0434 124 ASN A C   
894  O  O   . ASN A 156 ? 0.5255 0.4130 0.5455 -0.0161 0.2175  -0.0340 124 ASN A O   
895  C  CB  . ASN A 156 ? 0.4386 0.3980 0.5337 -0.0218 0.1651  -0.0239 124 ASN A CB  
896  C  CG  . ASN A 156 ? 0.4657 0.4105 0.5767 -0.0018 0.1199  -0.0184 124 ASN A CG  
897  O  OD1 . ASN A 156 ? 0.4982 0.4122 0.5917 0.0212  0.1197  -0.0241 124 ASN A OD1 
898  N  ND2 . ASN A 156 ? 0.4663 0.4168 0.5960 0.0037  0.0876  -0.0085 124 ASN A ND2 
899  N  N   . PRO A 157 ? 0.6224 0.5016 0.5718 -0.0303 0.1913  -0.0519 125 PRO A N   
900  C  CA  . PRO A 157 ? 0.7107 0.5350 0.6059 -0.0284 0.1610  -0.0517 125 PRO A CA  
901  C  C   . PRO A 157 ? 0.7942 0.5507 0.6181 -0.0304 0.1581  -0.0492 125 PRO A C   
902  O  O   . PRO A 157 ? 0.8484 0.5630 0.6325 -0.0241 0.1417  -0.0523 125 PRO A O   
903  C  CB  . PRO A 157 ? 0.6950 0.5391 0.6087 -0.0410 0.1523  -0.0562 125 PRO A CB  
904  C  CG  . PRO A 157 ? 0.6694 0.5374 0.6037 -0.0412 0.1647  -0.0600 125 PRO A CG  
905  C  CD  . PRO A 157 ? 0.6399 0.5200 0.5845 -0.0416 0.1831  -0.0608 125 PRO A CD  
906  N  N   . CYS B 42  ? 0.6416 0.6158 0.5792 -0.0592 0.1104  0.0306  10  CYS B N   
907  C  CA  . CYS B 42  ? 0.5956 0.5987 0.5570 -0.0548 0.1361  0.0413  10  CYS B CA  
908  C  C   . CYS B 42  ? 0.4650 0.4744 0.4969 -0.0266 0.1506  0.0442  10  CYS B C   
909  O  O   . CYS B 42  ? 0.4284 0.4488 0.5270 -0.0267 0.1736  0.0237  10  CYS B O   
910  C  CB  . CYS B 42  ? 0.6812 0.6776 0.6112 -0.0678 0.1306  0.0464  10  CYS B CB  
911  S  SG  . CYS B 42  ? 0.7451 0.7346 0.6514 -0.0705 0.1247  0.0540  10  CYS B SG  
912  N  N   . PRO B 43  ? 0.3927 0.3690 0.4032 -0.0004 0.1493  0.0702  11  PRO B N   
913  C  CA  . PRO B 43  ? 0.3391 0.3057 0.3217 0.0329  0.1006  0.0841  11  PRO B CA  
914  C  C   . PRO B 43  ? 0.2671 0.2794 0.2725 0.0081  0.0481  0.0816  11  PRO B C   
915  O  O   . PRO B 43  ? 0.2614 0.2954 0.2526 -0.0312 0.0251  0.1051  11  PRO B O   
916  C  CB  . PRO B 43  ? 0.4282 0.3360 0.3435 -0.0069 0.1229  0.0807  11  PRO B CB  
917  C  CG  . PRO B 43  ? 0.4816 0.3701 0.4003 0.0166  0.1013  0.0643  11  PRO B CG  
918  C  CD  . PRO B 43  ? 0.4619 0.3782 0.3938 0.0290  0.1202  0.0723  11  PRO B CD  
919  N  N   . LEU B 44  ? 0.2336 0.2513 0.2212 -0.0071 0.0384  0.0545  12  LEU B N   
920  C  CA  . LEU B 44  ? 0.2002 0.2435 0.2130 -0.0074 0.0492  0.0233  12  LEU B CA  
921  C  C   . LEU B 44  ? 0.2301 0.2367 0.1961 -0.0287 0.0145  0.0341  12  LEU B C   
922  O  O   . LEU B 44  ? 0.2573 0.2508 0.2095 -0.0083 -0.0038 0.0462  12  LEU B O   
923  C  CB  . LEU B 44  ? 0.2255 0.2427 0.2223 0.0289  0.0464  0.0048  12  LEU B CB  
924  C  CG  . LEU B 44  ? 0.2353 0.2368 0.2502 0.0293  0.0034  -0.0023 12  LEU B CG  
925  C  CD1 . LEU B 44  ? 0.2577 0.2291 0.2559 0.0296  -0.0152 0.0174  12  LEU B CD1 
926  C  CD2 . LEU B 44  ? 0.2960 0.2420 0.2960 0.0341  -0.0105 -0.0209 12  LEU B CD2 
927  N  N   . MET B 45  ? 0.1863 0.2412 0.1945 -0.0406 0.0012  0.0444  13  MET B N   
928  C  CA  . MET B 45  ? 0.2031 0.2624 0.2195 -0.0360 0.0343  0.0555  13  MET B CA  
929  C  C   . MET B 45  ? 0.1730 0.2287 0.1683 -0.0261 0.0331  0.0318  13  MET B C   
930  O  O   . MET B 45  ? 0.1945 0.2581 0.1512 -0.0127 0.0050  0.0236  13  MET B O   
931  C  CB  . MET B 45  ? 0.2841 0.3566 0.2838 -0.0486 0.0604  0.0461  13  MET B CB  
932  C  CG  . MET B 45  ? 0.4662 0.4541 0.4106 -0.0474 0.1310  0.0867  13  MET B CG  
933  S  SD  . MET B 45  ? 0.6065 0.5867 0.5865 -0.0521 0.1876  0.0995  13  MET B SD  
934  C  CE  . MET B 45  ? 0.7640 0.7643 0.7641 -0.0381 0.1463  0.0691  13  MET B CE  
935  N  N   . VAL B 46  ? 0.1900 0.2002 0.1513 -0.0132 0.0222  0.0135  14  VAL B N   
936  C  CA  . VAL B 46  ? 0.1898 0.2033 0.1522 -0.0321 0.0338  0.0189  14  VAL B CA  
937  C  C   . VAL B 46  ? 0.1940 0.2161 0.1431 -0.0227 -0.0163 0.0348  14  VAL B C   
938  O  O   . VAL B 46  ? 0.2128 0.2412 0.1743 -0.0334 -0.0502 0.0465  14  VAL B O   
939  C  CB  . VAL B 46  ? 0.1980 0.2146 0.1943 -0.0140 0.0249  0.0335  14  VAL B CB  
940  C  CG1 . VAL B 46  ? 0.1932 0.2442 0.2090 0.0199  0.0221  0.0529  14  VAL B CG1 
941  C  CG2 . VAL B 46  ? 0.2005 0.2206 0.2215 -0.0239 -0.0137 0.0055  14  VAL B CG2 
942  N  N   . LYS B 47  ? 0.1800 0.2044 0.1624 -0.0304 -0.0103 0.0167  15  LYS B N   
943  C  CA  . LYS B 47  ? 0.1950 0.2206 0.1852 -0.0370 0.0229  0.0099  15  LYS B CA  
944  C  C   . LYS B 47  ? 0.1759 0.2137 0.1566 -0.0217 -0.0150 0.0313  15  LYS B C   
945  O  O   . LYS B 47  ? 0.1871 0.2528 0.1587 -0.0356 -0.0411 0.0382  15  LYS B O   
946  C  CB  . LYS B 47  ? 0.3015 0.2379 0.2280 -0.0275 0.0318  -0.0002 15  LYS B CB  
947  C  CG  . LYS B 47  ? 0.3883 0.2717 0.3123 -0.0197 0.0577  -0.0336 15  LYS B CG  
948  C  CD  . LYS B 47  ? 0.4858 0.2946 0.3821 -0.0227 0.0336  -0.0367 15  LYS B CD  
949  C  CE  . LYS B 47  ? 0.5467 0.3158 0.4364 -0.0337 0.0036  -0.0231 15  LYS B CE  
950  N  NZ  . LYS B 47  ? 0.5936 0.3523 0.4798 -0.0486 -0.0082 -0.0238 15  LYS B NZ  
951  N  N   . VAL B 48  ? 0.1861 0.1895 0.1721 -0.0205 0.0054  0.0168  16  VAL B N   
952  C  CA  . VAL B 48  ? 0.1854 0.1975 0.1777 -0.0246 -0.0170 0.0155  16  VAL B CA  
953  C  C   . VAL B 48  ? 0.1815 0.2066 0.1965 -0.0203 -0.0351 0.0058  16  VAL B C   
954  O  O   . VAL B 48  ? 0.2120 0.2101 0.1891 -0.0433 -0.0420 0.0238  16  VAL B O   
955  C  CB  . VAL B 48  ? 0.2099 0.2098 0.1944 -0.0345 -0.0001 0.0359  16  VAL B CB  
956  C  CG1 . VAL B 48  ? 0.2211 0.2164 0.1712 -0.0447 0.0063  0.0297  16  VAL B CG1 
957  C  CG2 . VAL B 48  ? 0.2176 0.2152 0.2166 -0.0265 -0.0097 0.0261  16  VAL B CG2 
958  N  N   . LEU B 49  ? 0.1895 0.1935 0.1990 -0.0261 -0.0204 0.0185  17  LEU B N   
959  C  CA  . LEU B 49  ? 0.1535 0.1721 0.1906 0.0019  0.0085  0.0237  17  LEU B CA  
960  C  C   . LEU B 49  ? 0.1779 0.1753 0.1674 -0.0281 0.0040  0.0356  17  LEU B C   
961  O  O   . LEU B 49  ? 0.1765 0.1871 0.1659 -0.0215 -0.0199 0.0072  17  LEU B O   
962  C  CB  . LEU B 49  ? 0.1850 0.2122 0.2094 0.0098  0.0331  0.0098  17  LEU B CB  
963  C  CG  . LEU B 49  ? 0.1845 0.2566 0.2345 0.0207  -0.0089 -0.0112 17  LEU B CG  
964  C  CD1 . LEU B 49  ? 0.2806 0.2993 0.2987 0.0432  -0.0055 -0.0062 17  LEU B CD1 
965  C  CD2 . LEU B 49  ? 0.2279 0.3003 0.2517 0.0015  0.0065  -0.0291 17  LEU B CD2 
966  N  N   . ASP B 50  ? 0.1873 0.1702 0.1677 -0.0263 0.0129  0.0149  18  ASP B N   
967  C  CA  . ASP B 50  ? 0.1859 0.1645 0.1580 -0.0299 -0.0034 0.0198  18  ASP B CA  
968  C  C   . ASP B 50  ? 0.1885 0.1579 0.1590 -0.0038 -0.0154 0.0014  18  ASP B C   
969  O  O   . ASP B 50  ? 0.2041 0.1567 0.1715 -0.0128 -0.0105 -0.0001 18  ASP B O   
970  C  CB  . ASP B 50  ? 0.1591 0.1908 0.1845 -0.0040 -0.0107 0.0181  18  ASP B CB  
971  C  CG  . ASP B 50  ? 0.2052 0.1924 0.1962 0.0166  -0.0058 0.0051  18  ASP B CG  
972  O  OD1 . ASP B 50  ? 0.2074 0.1819 0.2017 -0.0100 -0.0038 -0.0033 18  ASP B OD1 
973  O  OD2 . ASP B 50  ? 0.2098 0.2224 0.2321 0.0320  -0.0093 0.0186  18  ASP B OD2 
974  N  N   . ALA B 51  ? 0.1954 0.1738 0.1454 0.0057  0.0037  0.0164  19  ALA B N   
975  C  CA  . ALA B 51  ? 0.2007 0.1985 0.1476 0.0099  -0.0128 0.0144  19  ALA B CA  
976  C  C   . ALA B 51  ? 0.2354 0.1651 0.1745 0.0064  -0.0171 0.0035  19  ALA B C   
977  O  O   . ALA B 51  ? 0.2971 0.1637 0.1607 0.0034  -0.0223 -0.0079 19  ALA B O   
978  C  CB  . ALA B 51  ? 0.2175 0.2224 0.1442 0.0140  -0.0117 -0.0046 19  ALA B CB  
979  N  N   . VAL B 52  ? 0.1999 0.1881 0.1845 -0.0238 -0.0159 -0.0117 20  VAL B N   
980  C  CA  . VAL B 52  ? 0.2105 0.2041 0.1959 -0.0279 0.0259  -0.0455 20  VAL B CA  
981  C  C   . VAL B 52  ? 0.2243 0.2149 0.1987 -0.0380 0.0269  -0.0316 20  VAL B C   
982  O  O   . VAL B 52  ? 0.3003 0.2282 0.2372 -0.0606 0.0381  -0.0177 20  VAL B O   
983  C  CB  . VAL B 52  ? 0.2143 0.2273 0.2158 -0.0386 0.0369  -0.0442 20  VAL B CB  
984  C  CG1 . VAL B 52  ? 0.2169 0.2538 0.2302 -0.0715 0.0511  -0.0398 20  VAL B CG1 
985  C  CG2 . VAL B 52  ? 0.2639 0.2421 0.2202 -0.0470 0.0184  -0.0426 20  VAL B CG2 
986  N  N   . ARG B 53  ? 0.2000 0.2433 0.2045 -0.0144 -0.0261 -0.0510 21  ARG B N   
987  C  CA  . ARG B 53  ? 0.1743 0.2587 0.2375 -0.0093 -0.0064 -0.0491 21  ARG B CA  
988  C  C   . ARG B 53  ? 0.1908 0.2253 0.2187 -0.0276 0.0067  -0.0233 21  ARG B C   
989  O  O   . ARG B 53  ? 0.2677 0.2408 0.2461 -0.0334 -0.0076 -0.0654 21  ARG B O   
990  C  CB  . ARG B 53  ? 0.2309 0.3561 0.3150 0.0666  -0.0106 -0.0820 21  ARG B CB  
991  C  CG  . ARG B 53  ? 0.3372 0.4265 0.4161 0.1102  0.0175  -0.0804 21  ARG B CG  
992  C  CD  . ARG B 53  ? 0.4594 0.5017 0.5026 0.1212  0.0195  -0.0758 21  ARG B CD  
993  N  NE  . ARG B 53  ? 0.6140 0.5770 0.5594 0.1140  0.0173  -0.0739 21  ARG B NE  
994  C  CZ  . ARG B 53  ? 0.6909 0.6315 0.6116 0.1297  0.0128  -0.0670 21  ARG B CZ  
995  N  NH1 . ARG B 53  ? 0.7204 0.6394 0.6368 0.1311  0.0047  -0.0623 21  ARG B NH1 
996  N  NH2 . ARG B 53  ? 0.7103 0.6469 0.6311 0.1390  0.0012  -0.0628 21  ARG B NH2 
997  N  N   . GLY B 54  ? 0.1839 0.1893 0.1968 -0.0016 0.0038  0.0037  22  GLY B N   
998  C  CA  . GLY B 54  ? 0.2164 0.1893 0.1913 0.0004  -0.0016 0.0106  22  GLY B CA  
999  C  C   . GLY B 54  ? 0.2146 0.1779 0.1962 0.0029  0.0317  -0.0042 22  GLY B C   
1000 O  O   . GLY B 54  ? 0.2500 0.1756 0.2097 0.0129  -0.0021 -0.0066 22  GLY B O   
1001 N  N   . SER B 55  ? 0.2327 0.1815 0.1843 -0.0168 0.0193  0.0107  23  SER B N   
1002 C  CA  . SER B 55  ? 0.2339 0.1965 0.1935 -0.0260 -0.0175 0.0164  23  SER B CA  
1003 C  C   . SER B 55  ? 0.2241 0.1772 0.1587 -0.0091 -0.0414 0.0158  23  SER B C   
1004 O  O   . SER B 55  ? 0.2570 0.1792 0.1750 -0.0290 -0.0256 -0.0063 23  SER B O   
1005 C  CB  . SER B 55  ? 0.2371 0.2343 0.2450 -0.0063 -0.0298 -0.0059 23  SER B CB  
1006 O  OG  . SER B 55  ? 0.2798 0.2885 0.2805 -0.0182 -0.0001 0.0040  23  SER B OG  
1007 N  N   . PRO B 56  ? 0.2547 0.1783 0.1620 0.0061  -0.0274 -0.0015 24  PRO B N   
1008 C  CA  . PRO B 56  ? 0.2486 0.1659 0.1764 -0.0055 -0.0014 -0.0005 24  PRO B CA  
1009 C  C   . PRO B 56  ? 0.1845 0.1737 0.2082 -0.0044 0.0157  -0.0091 24  PRO B C   
1010 O  O   . PRO B 56  ? 0.1975 0.1774 0.2491 -0.0045 -0.0027 -0.0196 24  PRO B O   
1011 C  CB  . PRO B 56  ? 0.2867 0.1874 0.1815 -0.0180 -0.0276 -0.0226 24  PRO B CB  
1012 C  CG  . PRO B 56  ? 0.3787 0.2248 0.2098 -0.0542 -0.0249 -0.0148 24  PRO B CG  
1013 C  CD  . PRO B 56  ? 0.3034 0.2071 0.1744 -0.0156 -0.0334 0.0019  24  PRO B CD  
1014 N  N   . ALA B 57  ? 0.2170 0.1742 0.2066 -0.0124 0.0029  -0.0235 25  ALA B N   
1015 C  CA  . ALA B 57  ? 0.2347 0.1917 0.1888 0.0118  -0.0151 -0.0117 25  ALA B CA  
1016 C  C   . ALA B 57  ? 0.2152 0.1989 0.1880 0.0145  -0.0067 0.0100  25  ALA B C   
1017 O  O   . ALA B 57  ? 0.1989 0.2206 0.2132 -0.0072 -0.0073 0.0117  25  ALA B O   
1018 C  CB  . ALA B 57  ? 0.2112 0.1925 0.1996 -0.0277 0.0021  -0.0086 25  ALA B CB  
1019 N  N   . ILE B 58  ? 0.1994 0.2021 0.1747 0.0181  -0.0260 0.0111  26  ILE B N   
1020 C  CA  . ILE B 58  ? 0.2523 0.2138 0.1993 0.0204  -0.0672 -0.0228 26  ILE B CA  
1021 C  C   . ILE B 58  ? 0.2697 0.2052 0.2181 0.0194  -0.0512 0.0109  26  ILE B C   
1022 O  O   . ILE B 58  ? 0.2809 0.2439 0.2261 0.0100  -0.0412 0.0054  26  ILE B O   
1023 C  CB  . ILE B 58  ? 0.3359 0.2387 0.2372 0.0137  -0.1046 -0.0190 26  ILE B CB  
1024 C  CG1 . ILE B 58  ? 0.3741 0.2560 0.2698 0.0031  -0.1089 -0.0429 26  ILE B CG1 
1025 C  CG2 . ILE B 58  ? 0.3805 0.2679 0.2991 0.0409  -0.0902 -0.0024 26  ILE B CG2 
1026 C  CD1 . ILE B 58  ? 0.4451 0.3009 0.3182 0.0125  -0.0809 -0.0416 26  ILE B CD1 
1027 N  N   . ASN B 59  ? 0.2423 0.2133 0.2398 0.0057  -0.0622 0.0006  27  ASN B N   
1028 C  CA  . ASN B 59  ? 0.2322 0.2322 0.2923 0.0131  -0.0456 -0.0180 27  ASN B CA  
1029 C  C   . ASN B 59  ? 0.2554 0.2322 0.2779 0.0126  -0.0227 0.0053  27  ASN B C   
1030 O  O   . ASN B 59  ? 0.2517 0.2657 0.3067 0.0460  -0.0410 0.0123  27  ASN B O   
1031 C  CB  . ASN B 59  ? 0.2327 0.2667 0.3639 0.0354  -0.0481 -0.0062 27  ASN B CB  
1032 C  CG  . ASN B 59  ? 0.3588 0.3421 0.4564 0.0006  -0.0298 0.0047  27  ASN B CG  
1033 O  OD1 . ASN B 59  ? 0.4287 0.3783 0.4868 -0.0125 -0.0312 0.0067  27  ASN B OD1 
1034 N  ND2 . ASN B 59  ? 0.3736 0.3911 0.4963 0.0064  -0.0528 0.0006  27  ASN B ND2 
1035 N  N   . VAL B 60  ? 0.1901 0.2063 0.2251 -0.0149 -0.0249 0.0121  28  VAL B N   
1036 C  CA  . VAL B 60  ? 0.2110 0.1917 0.2164 -0.0219 -0.0129 0.0153  28  VAL B CA  
1037 C  C   . VAL B 60  ? 0.2353 0.1891 0.1959 -0.0133 -0.0168 0.0278  28  VAL B C   
1038 O  O   . VAL B 60  ? 0.2474 0.1936 0.1878 -0.0153 0.0208  0.0217  28  VAL B O   
1039 C  CB  . VAL B 60  ? 0.2257 0.1943 0.2075 -0.0230 -0.0347 0.0318  28  VAL B CB  
1040 C  CG1 . VAL B 60  ? 0.2648 0.2098 0.2058 -0.0186 -0.0295 0.0076  28  VAL B CG1 
1041 C  CG2 . VAL B 60  ? 0.2575 0.1963 0.2206 -0.0311 -0.0024 0.0539  28  VAL B CG2 
1042 N  N   . ALA B 61  ? 0.2268 0.1726 0.2044 0.0081  -0.0383 0.0265  29  ALA B N   
1043 C  CA  . ALA B 61  ? 0.1952 0.1692 0.2179 0.0030  -0.0307 0.0204  29  ALA B CA  
1044 C  C   . ALA B 61  ? 0.1601 0.1805 0.1833 -0.0014 0.0001  0.0363  29  ALA B C   
1045 O  O   . ALA B 61  ? 0.2337 0.2166 0.1729 -0.0015 -0.0065 0.0294  29  ALA B O   
1046 C  CB  . ALA B 61  ? 0.1962 0.1783 0.2566 0.0225  -0.0148 0.0162  29  ALA B CB  
1047 N  N   . MET B 62  ? 0.1718 0.1710 0.1781 -0.0130 -0.0126 0.0258  30  MET B N   
1048 C  CA  . MET B 62  ? 0.1743 0.1881 0.1670 0.0129  -0.0231 0.0253  30  MET B CA  
1049 C  C   . MET B 62  ? 0.1744 0.1968 0.1563 -0.0041 -0.0339 0.0206  30  MET B C   
1050 O  O   . MET B 62  ? 0.1719 0.2001 0.1644 -0.0059 -0.0112 0.0117  30  MET B O   
1051 C  CB  . MET B 62  ? 0.1952 0.1984 0.1577 0.0478  0.0065  0.0358  30  MET B CB  
1052 C  CG  . MET B 62  ? 0.1904 0.2124 0.1686 0.0520  0.0013  0.0201  30  MET B CG  
1053 S  SD  . MET B 62  ? 0.1955 0.2132 0.2143 0.0139  -0.0124 -0.0013 30  MET B SD  
1054 C  CE  . MET B 62  ? 0.2162 0.2272 0.2415 -0.0024 -0.0307 -0.0129 30  MET B CE  
1055 N  N   . HIS B 63  ? 0.1668 0.2009 0.1777 -0.0164 -0.0148 0.0160  31  HIS B N   
1056 C  CA  . HIS B 63  ? 0.1618 0.2143 0.2062 -0.0279 -0.0032 0.0196  31  HIS B CA  
1057 C  C   . HIS B 63  ? 0.1674 0.2225 0.1980 0.0062  -0.0018 0.0332  31  HIS B C   
1058 O  O   . HIS B 63  ? 0.1909 0.2390 0.2027 -0.0149 -0.0176 0.0366  31  HIS B O   
1059 C  CB  . HIS B 63  ? 0.1873 0.2501 0.2311 0.0105  0.0100  0.0181  31  HIS B CB  
1060 C  CG  . HIS B 63  ? 0.1868 0.2879 0.2335 0.0075  -0.0164 0.0660  31  HIS B CG  
1061 N  ND1 . HIS B 63  ? 0.2820 0.3402 0.2973 0.0687  -0.0172 0.0467  31  HIS B ND1 
1062 C  CD2 . HIS B 63  ? 0.2109 0.3094 0.2926 0.0211  -0.0229 0.0568  31  HIS B CD2 
1063 C  CE1 . HIS B 63  ? 0.2614 0.3358 0.3044 0.0673  -0.0303 0.0256  31  HIS B CE1 
1064 N  NE2 . HIS B 63  ? 0.2447 0.3133 0.3054 0.0347  -0.0284 0.0462  31  HIS B NE2 
1065 N  N   . VAL B 64  ? 0.1504 0.2195 0.1935 -0.0097 -0.0057 0.0229  32  VAL B N   
1066 C  CA  . VAL B 64  ? 0.1747 0.2052 0.1804 -0.0073 0.0109  0.0166  32  VAL B CA  
1067 C  C   . VAL B 64  ? 0.1719 0.2013 0.1730 -0.0061 -0.0120 0.0248  32  VAL B C   
1068 O  O   . VAL B 64  ? 0.2007 0.2156 0.1970 0.0099  0.0007  0.0471  32  VAL B O   
1069 C  CB  . VAL B 64  ? 0.1696 0.1988 0.1795 -0.0093 -0.0198 0.0317  32  VAL B CB  
1070 C  CG1 . VAL B 64  ? 0.1763 0.2178 0.2072 0.0047  -0.0365 0.0142  32  VAL B CG1 
1071 C  CG2 . VAL B 64  ? 0.2244 0.2162 0.2199 -0.0496 -0.0168 0.0198  32  VAL B CG2 
1072 N  N   . PHE B 65  ? 0.1801 0.1960 0.1849 -0.0044 -0.0286 0.0086  33  PHE B N   
1073 C  CA  . PHE B 65  ? 0.2164 0.1981 0.1941 0.0096  -0.0188 0.0192  33  PHE B CA  
1074 C  C   . PHE B 65  ? 0.2245 0.1852 0.2039 0.0037  -0.0268 0.0428  33  PHE B C   
1075 O  O   . PHE B 65  ? 0.2130 0.1946 0.1907 0.0117  -0.0206 0.0320  33  PHE B O   
1076 C  CB  . PHE B 65  ? 0.2250 0.2247 0.2235 0.0366  -0.0286 -0.0018 33  PHE B CB  
1077 C  CG  . PHE B 65  ? 0.1974 0.2579 0.2359 0.0387  -0.0498 -0.0114 33  PHE B CG  
1078 C  CD1 . PHE B 65  ? 0.2048 0.2848 0.2504 0.0158  -0.0299 -0.0301 33  PHE B CD1 
1079 C  CD2 . PHE B 65  ? 0.2231 0.2726 0.2572 0.0496  -0.0348 -0.0187 33  PHE B CD2 
1080 C  CE1 . PHE B 65  ? 0.2075 0.2907 0.2480 0.0046  -0.0158 -0.0277 33  PHE B CE1 
1081 C  CE2 . PHE B 65  ? 0.2365 0.2895 0.2719 0.0513  -0.0212 -0.0209 33  PHE B CE2 
1082 C  CZ  . PHE B 65  ? 0.2224 0.2972 0.2551 0.0212  -0.0091 -0.0270 33  PHE B CZ  
1083 N  N   . ARG B 66  ? 0.2318 0.2020 0.2374 -0.0048 -0.0497 0.0348  34  ARG B N   
1084 C  CA  . ARG B 66  ? 0.2171 0.1930 0.2518 -0.0228 -0.0334 0.0370  34  ARG B CA  
1085 C  C   . ARG B 66  ? 0.2569 0.2063 0.2544 -0.0276 -0.0750 0.0233  34  ARG B C   
1086 O  O   . ARG B 66  ? 0.2989 0.2149 0.2641 0.0195  -0.0589 0.0187  34  ARG B O   
1087 C  CB  . ARG B 66  ? 0.2368 0.2154 0.2487 -0.0100 -0.0017 0.0372  34  ARG B CB  
1088 C  CG  . ARG B 66  ? 0.2945 0.2508 0.2860 -0.0128 0.0312  0.0444  34  ARG B CG  
1089 C  CD  . ARG B 66  ? 0.3781 0.2950 0.3213 -0.0429 0.0742  0.0083  34  ARG B CD  
1090 N  NE  . ARG B 66  ? 0.4799 0.3070 0.3604 -0.0740 0.1004  0.0157  34  ARG B NE  
1091 C  CZ  . ARG B 66  ? 0.5391 0.3080 0.4151 -0.0540 0.1133  -0.0305 34  ARG B CZ  
1092 N  NH1 . ARG B 66  ? 0.5737 0.3031 0.4388 -0.0424 0.1285  -0.0319 34  ARG B NH1 
1093 N  NH2 . ARG B 66  ? 0.5663 0.3259 0.4336 -0.0541 0.1161  -0.0400 34  ARG B NH2 
1094 N  N   . LYS B 67  ? 0.2919 0.2254 0.2415 -0.0305 -0.0866 0.0066  35  LYS B N   
1095 C  CA  . LYS B 67  ? 0.3193 0.2399 0.2687 -0.0240 -0.0901 -0.0050 35  LYS B CA  
1096 C  C   . LYS B 67  ? 0.3332 0.2510 0.2944 -0.0273 -0.0438 -0.0075 35  LYS B C   
1097 O  O   . LYS B 67  ? 0.3005 0.2788 0.3199 -0.0291 -0.0266 0.0135  35  LYS B O   
1098 C  CB  . LYS B 67  ? 0.3978 0.2773 0.2602 -0.0017 -0.1289 -0.0249 35  LYS B CB  
1099 C  CG  . LYS B 67  ? 0.5018 0.3458 0.3177 0.0488  -0.1035 -0.0298 35  LYS B CG  
1100 C  CD  . LYS B 67  ? 0.5724 0.4036 0.3420 0.0513  -0.1100 -0.0326 35  LYS B CD  
1101 C  CE  . LYS B 67  ? 0.6377 0.4429 0.3949 0.0374  -0.0998 -0.0103 35  LYS B CE  
1102 N  NZ  . LYS B 67  ? 0.6721 0.4527 0.4106 0.0316  -0.1000 0.0068  35  LYS B NZ  
1103 N  N   . ALA B 68  ? 0.3969 0.2257 0.3203 -0.0281 -0.0150 -0.0220 36  ALA B N   
1104 C  CA  . ALA B 68  ? 0.4097 0.2601 0.3886 -0.0483 0.0176  -0.0110 36  ALA B CA  
1105 C  C   . ALA B 68  ? 0.4568 0.2888 0.4361 -0.0796 0.0141  -0.0366 36  ALA B C   
1106 O  O   . ALA B 68  ? 0.4664 0.2851 0.4197 -0.1119 0.0291  -0.0370 36  ALA B O   
1107 C  CB  . ALA B 68  ? 0.4460 0.2556 0.4095 -0.0403 0.0162  0.0133  36  ALA B CB  
1108 N  N   . ALA B 69  ? 0.5039 0.3352 0.4864 -0.1125 0.0140  -0.0753 37  ALA B N   
1109 C  CA  . ALA B 69  ? 0.5634 0.3962 0.5312 -0.0894 0.0378  -0.0809 37  ALA B CA  
1110 C  C   . ALA B 69  ? 0.5875 0.4289 0.5588 -0.0822 0.0298  -0.0899 37  ALA B C   
1111 O  O   . ALA B 69  ? 0.6046 0.4483 0.5795 -0.0872 0.0212  -0.0799 37  ALA B O   
1112 C  CB  . ALA B 69  ? 0.5832 0.4019 0.5397 -0.0853 0.0480  -0.0743 37  ALA B CB  
1113 N  N   . ASP B 70  ? 0.5742 0.4484 0.5742 -0.0606 0.0362  -0.0858 38  ASP B N   
1114 C  CA  . ASP B 70  ? 0.5989 0.4822 0.5994 -0.0240 0.0300  -0.0811 38  ASP B CA  
1115 C  C   . ASP B 70  ? 0.6005 0.5032 0.5900 -0.0157 0.0220  -0.0852 38  ASP B C   
1116 O  O   . ASP B 70  ? 0.6005 0.5023 0.5853 -0.0281 0.0246  -0.0846 38  ASP B O   
1117 C  CB  . ASP B 70  ? 0.6204 0.4902 0.6284 0.0026  0.0358  -0.0763 38  ASP B CB  
1118 C  CG  . ASP B 70  ? 0.6370 0.4910 0.6485 0.0232  0.0328  -0.0762 38  ASP B CG  
1119 O  OD1 . ASP B 70  ? 0.6288 0.4752 0.6515 0.0276  0.0385  -0.0937 38  ASP B OD1 
1120 O  OD2 . ASP B 70  ? 0.6636 0.4942 0.6629 0.0377  0.0333  -0.0706 38  ASP B OD2 
1121 N  N   . ASP B 71  ? 0.6051 0.5207 0.5806 0.0058  -0.0046 -0.0954 39  ASP B N   
1122 C  CA  . ASP B 71  ? 0.6179 0.5476 0.5849 0.0379  -0.0126 -0.0931 39  ASP B CA  
1123 C  C   . ASP B 71  ? 0.5754 0.4955 0.5414 0.0488  0.0084  -0.1046 39  ASP B C   
1124 O  O   . ASP B 71  ? 0.5902 0.5044 0.5403 0.0464  0.0096  -0.0868 39  ASP B O   
1125 C  CB  . ASP B 71  ? 0.6822 0.6142 0.6247 0.0541  -0.0299 -0.0907 39  ASP B CB  
1126 C  CG  . ASP B 71  ? 0.7529 0.6711 0.6627 0.0605  -0.0508 -0.0903 39  ASP B CG  
1127 O  OD1 . ASP B 71  ? 0.7700 0.6845 0.6751 0.0559  -0.0594 -0.0913 39  ASP B OD1 
1128 O  OD2 . ASP B 71  ? 0.7899 0.6887 0.6817 0.0679  -0.0558 -0.0914 39  ASP B OD2 
1129 N  N   . THR B 72  ? 0.5169 0.4299 0.4952 0.0757  0.0174  -0.1239 40  THR B N   
1130 C  CA  . THR B 72  ? 0.5067 0.3912 0.4603 0.0954  0.0118  -0.1113 40  THR B CA  
1131 C  C   . THR B 72  ? 0.4469 0.3371 0.4038 0.0896  -0.0175 -0.0945 40  THR B C   
1132 O  O   . THR B 72  ? 0.4210 0.3165 0.4072 0.0746  -0.0180 -0.0847 40  THR B O   
1133 C  CB  . THR B 72  ? 0.5587 0.4014 0.4866 0.1085  0.0221  -0.1198 40  THR B CB  
1134 O  OG1 . THR B 72  ? 0.5790 0.4122 0.4995 0.1122  0.0050  -0.1004 40  THR B OG1 
1135 C  CG2 . THR B 72  ? 0.5775 0.4025 0.4867 0.0960  0.0247  -0.1346 40  THR B CG2 
1136 N  N   . TRP B 73  ? 0.4158 0.3360 0.3515 0.0971  -0.0360 -0.0808 41  TRP B N   
1137 C  CA  . TRP B 73  ? 0.3804 0.3244 0.3024 0.0872  -0.0746 -0.0524 41  TRP B CA  
1138 C  C   . TRP B 73  ? 0.3947 0.3472 0.3569 0.1061  -0.1182 -0.0253 41  TRP B C   
1139 O  O   . TRP B 73  ? 0.4201 0.4078 0.3835 0.1095  -0.1070 -0.0084 41  TRP B O   
1140 C  CB  . TRP B 73  ? 0.3819 0.3242 0.2872 0.0888  -0.0158 -0.0373 41  TRP B CB  
1141 C  CG  . TRP B 73  ? 0.3665 0.3434 0.2849 0.0731  -0.0029 -0.0251 41  TRP B CG  
1142 C  CD1 . TRP B 73  ? 0.4118 0.3633 0.2993 0.0829  0.0298  -0.0158 41  TRP B CD1 
1143 C  CD2 . TRP B 73  ? 0.2906 0.3081 0.2730 0.0723  0.0112  -0.0061 41  TRP B CD2 
1144 N  NE1 . TRP B 73  ? 0.4002 0.3597 0.3007 0.0896  0.0216  0.0097  41  TRP B NE1 
1145 C  CE2 . TRP B 73  ? 0.3318 0.3279 0.2882 0.0848  0.0445  0.0040  41  TRP B CE2 
1146 C  CE3 . TRP B 73  ? 0.2460 0.2822 0.2821 0.0350  0.0223  -0.0242 41  TRP B CE3 
1147 C  CZ2 . TRP B 73  ? 0.3570 0.3063 0.3046 0.0503  0.0363  0.0333  41  TRP B CZ2 
1148 C  CZ3 . TRP B 73  ? 0.2817 0.2676 0.2935 -0.0160 0.0109  0.0233  41  TRP B CZ3 
1149 C  CH2 . TRP B 73  ? 0.3173 0.2775 0.3018 0.0271  0.0113  0.0419  41  TRP B CH2 
1150 N  N   . GLU B 74  ? 0.3498 0.3051 0.3330 0.0753  -0.1591 -0.0484 42  GLU B N   
1151 C  CA  . GLU B 74  ? 0.3659 0.3096 0.3636 0.0549  -0.1436 -0.0245 42  GLU B CA  
1152 C  C   . GLU B 74  ? 0.3001 0.2492 0.3028 0.0567  -0.0958 -0.0129 42  GLU B C   
1153 O  O   . GLU B 74  ? 0.3028 0.2351 0.2824 0.0617  -0.0945 -0.0022 42  GLU B O   
1154 C  CB  . GLU B 74  ? 0.4539 0.3813 0.4649 0.0165  -0.1526 -0.0248 42  GLU B CB  
1155 C  CG  . GLU B 74  ? 0.5809 0.4745 0.5841 0.0153  -0.1465 -0.0256 42  GLU B CG  
1156 C  CD  . GLU B 74  ? 0.6903 0.5422 0.6861 -0.0009 -0.1325 -0.0248 42  GLU B CD  
1157 O  OE1 . GLU B 74  ? 0.7316 0.5690 0.7193 -0.0083 -0.1146 -0.0154 42  GLU B OE1 
1158 O  OE2 . GLU B 74  ? 0.7392 0.5621 0.7170 0.0080  -0.1255 -0.0237 42  GLU B OE2 
1159 N  N   . PRO B 75  ? 0.2639 0.2187 0.2977 0.0509  -0.0582 -0.0188 43  PRO B N   
1160 C  CA  . PRO B 75  ? 0.2397 0.2173 0.2988 0.0429  -0.0741 0.0057  43  PRO B CA  
1161 C  C   . PRO B 75  ? 0.2419 0.2070 0.2677 0.0190  -0.0554 0.0337  43  PRO B C   
1162 O  O   . PRO B 75  ? 0.3069 0.1989 0.2766 0.0053  -0.0442 0.0264  43  PRO B O   
1163 C  CB  . PRO B 75  ? 0.2450 0.2306 0.3438 0.0533  -0.0622 -0.0047 43  PRO B CB  
1164 C  CG  . PRO B 75  ? 0.3048 0.2631 0.3710 0.0496  -0.0581 -0.0167 43  PRO B CG  
1165 C  CD  . PRO B 75  ? 0.2834 0.2353 0.3454 0.0437  -0.0673 -0.0121 43  PRO B CD  
1166 N  N   . PHE B 76  ? 0.2027 0.2151 0.2340 0.0388  -0.0371 0.0258  44  PHE B N   
1167 C  CA  . PHE B 76  ? 0.1853 0.2317 0.1968 0.0133  -0.0458 0.0323  44  PHE B CA  
1168 C  C   . PHE B 76  ? 0.1691 0.2291 0.2062 -0.0058 -0.0318 0.0408  44  PHE B C   
1169 O  O   . PHE B 76  ? 0.2239 0.2432 0.2133 0.0032  -0.0140 0.0573  44  PHE B O   
1170 C  CB  . PHE B 76  ? 0.1851 0.2638 0.1970 -0.0129 -0.0230 0.0463  44  PHE B CB  
1171 C  CG  . PHE B 76  ? 0.1625 0.2811 0.1702 -0.0068 -0.0065 0.0589  44  PHE B CG  
1172 C  CD1 . PHE B 76  ? 0.1886 0.3188 0.1985 -0.0075 -0.0143 0.0435  44  PHE B CD1 
1173 C  CD2 . PHE B 76  ? 0.1913 0.2845 0.1737 0.0344  -0.0160 0.0183  44  PHE B CD2 
1174 C  CE1 . PHE B 76  ? 0.2047 0.3283 0.1901 0.0217  -0.0185 0.0415  44  PHE B CE1 
1175 C  CE2 . PHE B 76  ? 0.1967 0.3116 0.1930 0.0115  -0.0314 0.0234  44  PHE B CE2 
1176 C  CZ  . PHE B 76  ? 0.2459 0.3348 0.1868 0.0160  -0.0237 0.0426  44  PHE B CZ  
1177 N  N   . ALA B 77  ? 0.1414 0.2028 0.2010 -0.0162 -0.0193 0.0342  45  ALA B N   
1178 C  CA  . ALA B 77  ? 0.1473 0.2124 0.2017 -0.0132 -0.0096 0.0213  45  ALA B CA  
1179 C  C   . ALA B 77  ? 0.1788 0.2230 0.1825 -0.0206 -0.0372 0.0412  45  ALA B C   
1180 O  O   . ALA B 77  ? 0.2051 0.2599 0.1843 -0.0422 -0.0120 0.0240  45  ALA B O   
1181 C  CB  . ALA B 77  ? 0.1692 0.2461 0.2174 -0.0006 0.0396  0.0468  45  ALA B CB  
1182 N  N   . SER B 78  ? 0.1934 0.1869 0.2034 -0.0092 -0.0335 0.0402  46  SER B N   
1183 C  CA  . SER B 78  ? 0.1877 0.1902 0.2143 -0.0124 -0.0089 0.0315  46  SER B CA  
1184 C  C   . SER B 78  ? 0.1830 0.1870 0.1973 -0.0352 -0.0462 0.0307  46  SER B C   
1185 O  O   . SER B 78  ? 0.2470 0.2065 0.1957 -0.0102 -0.0357 0.0462  46  SER B O   
1186 C  CB  . SER B 78  ? 0.3228 0.2412 0.3373 0.0134  -0.0337 -0.0143 46  SER B CB  
1187 O  OG  . SER B 78  ? 0.3145 0.2667 0.3965 0.0684  -0.0753 -0.0310 46  SER B OG  
1188 N  N   . GLY B 79  ? 0.1910 0.1820 0.2029 -0.0299 -0.0144 0.0227  47  GLY B N   
1189 C  CA  . GLY B 79  ? 0.2263 0.1835 0.1891 -0.0513 -0.0219 0.0246  47  GLY B CA  
1190 C  C   . GLY B 79  ? 0.2260 0.1702 0.1797 -0.0115 -0.0343 0.0405  47  GLY B C   
1191 O  O   . GLY B 79  ? 0.2445 0.1989 0.1888 -0.0094 -0.0108 0.0421  47  GLY B O   
1192 N  N   . LYS B 80  ? 0.2231 0.1766 0.1939 -0.0208 -0.0082 0.0344  48  LYS B N   
1193 C  CA  . LYS B 80  ? 0.2345 0.1787 0.2631 -0.0143 0.0060  0.0247  48  LYS B CA  
1194 C  C   . LYS B 80  ? 0.2511 0.1753 0.2229 0.0051  -0.0128 0.0051  48  LYS B C   
1195 O  O   . LYS B 80  ? 0.2777 0.2112 0.2075 -0.0015 -0.0239 0.0023  48  LYS B O   
1196 C  CB  . LYS B 80  ? 0.2574 0.2346 0.4139 0.0038  0.0781  0.0303  48  LYS B CB  
1197 C  CG  . LYS B 80  ? 0.3941 0.3358 0.4796 -0.0566 0.0410  0.0337  48  LYS B CG  
1198 C  CD  . LYS B 80  ? 0.4659 0.3983 0.5109 -0.0846 0.0060  0.0453  48  LYS B CD  
1199 C  CE  . LYS B 80  ? 0.5218 0.4236 0.5176 -0.1109 -0.0018 0.0528  48  LYS B CE  
1200 N  NZ  . LYS B 80  ? 0.5584 0.4468 0.5151 -0.1167 -0.0168 0.0776  48  LYS B NZ  
1201 N  N   . THR B 81  ? 0.2096 0.1690 0.2140 0.0099  -0.0170 0.0151  49  THR B N   
1202 C  CA  . THR B 81  ? 0.2112 0.1869 0.1966 0.0363  -0.0249 0.0019  49  THR B CA  
1203 C  C   . THR B 81  ? 0.2028 0.2094 0.1932 -0.0093 -0.0322 0.0118  49  THR B C   
1204 O  O   . THR B 81  ? 0.2162 0.2163 0.1911 -0.0028 -0.0150 0.0275  49  THR B O   
1205 C  CB  . THR B 81  ? 0.1766 0.1902 0.2033 0.0172  -0.0294 0.0173  49  THR B CB  
1206 O  OG1 . THR B 81  ? 0.1985 0.1860 0.2015 -0.0020 -0.0031 0.0089  49  THR B OG1 
1207 C  CG2 . THR B 81  ? 0.2031 0.2014 0.2219 -0.0168 -0.0369 0.0145  49  THR B CG2 
1208 N  N   . SER B 82  ? 0.2476 0.2360 0.1767 -0.0399 -0.0373 -0.0100 50  SER B N   
1209 C  CA  . SER B 82  ? 0.2736 0.2474 0.1812 -0.0364 -0.0491 -0.0110 50  SER B CA  
1210 C  C   . SER B 82  ? 0.2777 0.2285 0.1972 -0.0167 -0.0454 -0.0028 50  SER B C   
1211 O  O   . SER B 82  ? 0.2765 0.2183 0.1801 -0.0266 -0.0234 0.0083  50  SER B O   
1212 C  CB  . SER B 82  ? 0.3071 0.2952 0.2080 0.0048  -0.0486 -0.0187 50  SER B CB  
1213 O  OG  . SER B 82  ? 0.3082 0.3224 0.2450 -0.0036 -0.0187 -0.0553 50  SER B OG  
1214 N  N   . GLU B 83  ? 0.3005 0.2391 0.2683 -0.0212 -0.0310 -0.0181 51  GLU B N   
1215 C  CA  . GLU B 83  ? 0.3523 0.2711 0.3095 -0.0413 -0.0919 -0.0333 51  GLU B CA  
1216 C  C   . GLU B 83  ? 0.3334 0.2448 0.2654 -0.0425 -0.0705 -0.0318 51  GLU B C   
1217 O  O   . GLU B 83  ? 0.3492 0.2392 0.2880 -0.0210 -0.0403 -0.0219 51  GLU B O   
1218 C  CB  . GLU B 83  ? 0.4318 0.3547 0.4104 -0.0238 -0.1066 -0.0511 51  GLU B CB  
1219 C  CG  . GLU B 83  ? 0.5459 0.4597 0.5182 0.0053  -0.1178 -0.0655 51  GLU B CG  
1220 C  CD  . GLU B 83  ? 0.6555 0.5435 0.6272 0.0253  -0.1085 -0.0798 51  GLU B CD  
1221 O  OE1 . GLU B 83  ? 0.7034 0.5650 0.6458 0.0208  -0.1160 -0.0939 51  GLU B OE1 
1222 O  OE2 . GLU B 83  ? 0.6955 0.5802 0.6643 0.0330  -0.1008 -0.0766 51  GLU B OE2 
1223 N  N   . SER B 84  ? 0.3331 0.2344 0.2278 -0.0247 -0.0666 -0.0306 52  SER B N   
1224 C  CA  . SER B 84  ? 0.2990 0.2565 0.2237 -0.0193 -0.0379 -0.0357 52  SER B CA  
1225 C  C   . SER B 84  ? 0.2654 0.2170 0.1892 -0.0254 -0.0355 -0.0208 52  SER B C   
1226 O  O   . SER B 84  ? 0.2872 0.2254 0.2252 0.0012  -0.0061 -0.0115 52  SER B O   
1227 C  CB  . SER B 84  ? 0.3633 0.3061 0.2516 -0.0055 -0.0217 -0.0344 52  SER B CB  
1228 O  OG  . SER B 84  ? 0.4404 0.3633 0.2890 0.0243  0.0120  0.0246  52  SER B OG  
1229 N  N   . GLY B 85  ? 0.2403 0.1942 0.1667 -0.0290 -0.0148 -0.0203 53  GLY B N   
1230 C  CA  . GLY B 85  ? 0.2222 0.2047 0.1518 -0.0320 -0.0336 -0.0051 53  GLY B CA  
1231 C  C   . GLY B 85  ? 0.1939 0.1924 0.1533 -0.0164 -0.0410 0.0205  53  GLY B C   
1232 O  O   . GLY B 85  ? 0.2277 0.2231 0.1736 -0.0004 -0.0451 0.0204  53  GLY B O   
1233 N  N   . GLU B 86  ? 0.2545 0.1934 0.1950 -0.0380 -0.0075 0.0320  54  GLU B N   
1234 C  CA  . GLU B 86  ? 0.2489 0.1901 0.1942 -0.0087 0.0008  0.0242  54  GLU B CA  
1235 C  C   . GLU B 86  ? 0.1990 0.2076 0.1721 -0.0051 -0.0330 0.0160  54  GLU B C   
1236 O  O   . GLU B 86  ? 0.2284 0.2300 0.1864 -0.0069 -0.0574 0.0308  54  GLU B O   
1237 C  CB  . GLU B 86  ? 0.2882 0.2182 0.2460 0.0226  0.0581  0.0016  54  GLU B CB  
1238 C  CG  . GLU B 86  ? 0.3828 0.2274 0.3287 0.0302  0.0467  0.0074  54  GLU B CG  
1239 C  CD  . GLU B 86  ? 0.5152 0.2567 0.3922 0.0451  0.0623  0.0006  54  GLU B CD  
1240 O  OE1 . GLU B 86  ? 0.5690 0.2729 0.3917 0.0481  0.0871  -0.0065 54  GLU B OE1 
1241 O  OE2 . GLU B 86  ? 0.5341 0.2777 0.4431 0.0703  0.0695  -0.0249 54  GLU B OE2 
1242 N  N   . LEU B 87  ? 0.2320 0.1976 0.1655 -0.0345 -0.0205 0.0151  55  LEU B N   
1243 C  CA  . LEU B 87  ? 0.2198 0.2035 0.1761 -0.0103 -0.0063 0.0363  55  LEU B CA  
1244 C  C   . LEU B 87  ? 0.1948 0.2270 0.1895 -0.0228 -0.0102 0.0125  55  LEU B C   
1245 O  O   . LEU B 87  ? 0.2115 0.2523 0.1933 -0.0095 -0.0166 0.0162  55  LEU B O   
1246 C  CB  . LEU B 87  ? 0.2128 0.1987 0.1765 0.0034  -0.0064 0.0314  55  LEU B CB  
1247 C  CG  . LEU B 87  ? 0.2153 0.2159 0.1960 0.0078  -0.0039 0.0209  55  LEU B CG  
1248 C  CD1 . LEU B 87  ? 0.2229 0.2423 0.2154 -0.0023 -0.0024 0.0422  55  LEU B CD1 
1249 C  CD2 . LEU B 87  ? 0.2367 0.2111 0.2085 -0.0145 -0.0008 -0.0015 55  LEU B CD2 
1250 N  N   . HIS B 88  ? 0.2706 0.2386 0.2152 -0.0160 0.0422  0.0280  56  HIS B N   
1251 C  CA  . HIS B 88  ? 0.3367 0.2613 0.2425 -0.0060 0.0654  0.0070  56  HIS B CA  
1252 C  C   . HIS B 88  ? 0.3214 0.2631 0.2280 -0.0260 0.0381  0.0269  56  HIS B C   
1253 O  O   . HIS B 88  ? 0.3306 0.2934 0.2621 0.0081  0.0216  0.0563  56  HIS B O   
1254 C  CB  . HIS B 88  ? 0.4081 0.2842 0.2793 0.0000  0.0868  -0.0182 56  HIS B CB  
1255 C  CG  . HIS B 88  ? 0.4479 0.3046 0.3207 0.0199  0.1144  -0.0323 56  HIS B CG  
1256 N  ND1 . HIS B 88  ? 0.4758 0.3272 0.3721 0.0267  0.0971  -0.0206 56  HIS B ND1 
1257 C  CD2 . HIS B 88  ? 0.4740 0.3173 0.3654 0.0128  0.0988  -0.0448 56  HIS B CD2 
1258 C  CE1 . HIS B 88  ? 0.4942 0.3205 0.3861 0.0260  0.0925  -0.0146 56  HIS B CE1 
1259 N  NE2 . HIS B 88  ? 0.4947 0.3319 0.3827 0.0193  0.1072  -0.0377 56  HIS B NE2 
1260 N  N   . GLY B 89  ? 0.3178 0.2656 0.2331 -0.0327 0.0026  0.0195  57  GLY B N   
1261 C  CA  . GLY B 89  ? 0.3181 0.2667 0.2379 -0.0270 -0.0117 0.0564  57  GLY B CA  
1262 C  C   . GLY B 89  ? 0.2986 0.2736 0.2358 -0.0045 -0.0234 0.0499  57  GLY B C   
1263 O  O   . GLY B 89  ? 0.3572 0.2948 0.2734 -0.0249 -0.0636 0.0546  57  GLY B O   
1264 N  N   . LEU B 90  ? 0.2669 0.2713 0.2385 -0.0168 -0.0135 0.0271  58  LEU B N   
1265 C  CA  . LEU B 90  ? 0.2217 0.2521 0.2412 -0.0172 0.0262  0.0442  58  LEU B CA  
1266 C  C   . LEU B 90  ? 0.2226 0.2572 0.2365 -0.0160 -0.0032 0.0525  58  LEU B C   
1267 O  O   . LEU B 90  ? 0.2586 0.2540 0.2387 -0.0003 -0.0165 0.0587  58  LEU B O   
1268 C  CB  . LEU B 90  ? 0.2026 0.2572 0.2275 -0.0189 0.0347  0.0508  58  LEU B CB  
1269 C  CG  . LEU B 90  ? 0.2045 0.2679 0.2364 0.0008  0.0500  0.0716  58  LEU B CG  
1270 C  CD1 . LEU B 90  ? 0.2549 0.2788 0.2319 0.0087  0.0278  0.0739  58  LEU B CD1 
1271 C  CD2 . LEU B 90  ? 0.2257 0.2859 0.2910 0.0308  0.0863  0.0672  58  LEU B CD2 
1272 N  N   . THR B 91  ? 0.1940 0.2598 0.2327 -0.0258 -0.0274 0.0422  59  THR B N   
1273 C  CA  . THR B 91  ? 0.2062 0.2693 0.2369 -0.0476 -0.0270 0.0378  59  THR B CA  
1274 C  C   . THR B 91  ? 0.2351 0.2841 0.2419 -0.0329 -0.0059 0.0467  59  THR B C   
1275 O  O   . THR B 91  ? 0.3009 0.2955 0.2453 -0.0332 0.0293  0.0152  59  THR B O   
1276 C  CB  . THR B 91  ? 0.2229 0.2692 0.2197 -0.0490 -0.0510 0.0413  59  THR B CB  
1277 O  OG1 . THR B 91  ? 0.2520 0.2719 0.2324 -0.0473 -0.0218 0.0254  59  THR B OG1 
1278 C  CG2 . THR B 91  ? 0.2316 0.2660 0.2388 -0.0353 -0.0447 0.0631  59  THR B CG2 
1279 N  N   . THR B 92  ? 0.2294 0.2979 0.2487 -0.0575 -0.0071 0.0418  60  THR B N   
1280 C  CA  . THR B 92  ? 0.2459 0.3183 0.2356 -0.0646 -0.0006 0.0601  60  THR B CA  
1281 C  C   . THR B 92  ? 0.2665 0.3001 0.2282 -0.0613 0.0229  0.0379  60  THR B C   
1282 O  O   . THR B 92  ? 0.2971 0.2776 0.2185 -0.0512 0.0153  0.0168  60  THR B O   
1283 C  CB  . THR B 92  ? 0.3076 0.3549 0.2669 -0.0777 -0.0548 0.0874  60  THR B CB  
1284 O  OG1 . THR B 92  ? 0.3444 0.3630 0.2795 -0.0936 -0.0697 0.1046  60  THR B OG1 
1285 C  CG2 . THR B 92  ? 0.3402 0.3832 0.2905 -0.0855 -0.0557 0.0648  60  THR B CG2 
1286 N  N   . GLU B 93  ? 0.2738 0.2707 0.2431 -0.0617 0.0387  0.0412  61  GLU B N   
1287 C  CA  . GLU B 93  ? 0.2756 0.2745 0.2824 -0.0531 0.0539  0.0348  61  GLU B CA  
1288 C  C   . GLU B 93  ? 0.2834 0.2748 0.2680 -0.0370 0.0318  0.0617  61  GLU B C   
1289 O  O   . GLU B 93  ? 0.2552 0.2695 0.2757 -0.0216 0.0282  0.0524  61  GLU B O   
1290 C  CB  . GLU B 93  ? 0.3734 0.3360 0.3714 -0.0207 0.1056  0.0127  61  GLU B CB  
1291 C  CG  . GLU B 93  ? 0.4843 0.4063 0.4587 0.0565  0.1349  -0.0104 61  GLU B CG  
1292 C  CD  . GLU B 93  ? 0.5972 0.4740 0.5535 0.0798  0.1531  -0.0079 61  GLU B CD  
1293 O  OE1 . GLU B 93  ? 0.6096 0.5004 0.5762 0.0915  0.1447  -0.0075 61  GLU B OE1 
1294 O  OE2 . GLU B 93  ? 0.6618 0.5069 0.5793 0.0841  0.1601  0.0081  61  GLU B OE2 
1295 N  N   . GLU B 94  ? 0.2537 0.2895 0.2613 -0.0331 0.0126  0.0905  62  GLU B N   
1296 C  CA  . GLU B 94  ? 0.3083 0.3063 0.2923 -0.0481 -0.0013 0.1096  62  GLU B CA  
1297 C  C   . GLU B 94  ? 0.1970 0.2995 0.2735 -0.0372 0.0327  0.0788  62  GLU B C   
1298 O  O   . GLU B 94  ? 0.2133 0.3090 0.2946 -0.0446 0.0154  0.0430  62  GLU B O   
1299 C  CB  . GLU B 94  ? 0.4406 0.3525 0.3676 -0.0691 -0.0324 0.1300  62  GLU B CB  
1300 C  CG  . GLU B 94  ? 0.5693 0.4056 0.4434 -0.0604 -0.0689 0.1419  62  GLU B CG  
1301 C  CD  . GLU B 94  ? 0.6795 0.4789 0.5265 -0.0373 -0.1042 0.1341  62  GLU B CD  
1302 O  OE1 . GLU B 94  ? 0.7283 0.5143 0.5670 -0.0359 -0.1235 0.1243  62  GLU B OE1 
1303 O  OE2 . GLU B 94  ? 0.7060 0.4923 0.5278 -0.0500 -0.1050 0.1489  62  GLU B OE2 
1304 N  N   . GLU B 95  ? 0.1956 0.2986 0.2661 -0.0218 0.0254  0.0973  63  GLU B N   
1305 C  CA  . GLU B 95  ? 0.2011 0.3202 0.2948 -0.0069 -0.0144 0.1001  63  GLU B CA  
1306 C  C   . GLU B 95  ? 0.2327 0.2941 0.2465 -0.0225 0.0237  0.0746  63  GLU B C   
1307 O  O   . GLU B 95  ? 0.3049 0.2932 0.2476 -0.0235 0.0613  0.0688  63  GLU B O   
1308 C  CB  . GLU B 95  ? 0.2581 0.3522 0.3778 -0.0104 -0.0504 0.1189  63  GLU B CB  
1309 C  CG  . GLU B 95  ? 0.3613 0.3900 0.4620 -0.0061 -0.0953 0.1217  63  GLU B CG  
1310 C  CD  . GLU B 95  ? 0.4709 0.4238 0.5513 0.0110  -0.1163 0.1159  63  GLU B CD  
1311 O  OE1 . GLU B 95  ? 0.4927 0.4374 0.5562 0.0200  -0.1135 0.1196  63  GLU B OE1 
1312 O  OE2 . GLU B 95  ? 0.5578 0.4624 0.6009 0.0003  -0.1119 0.1032  63  GLU B OE2 
1313 N  N   . PHE B 96  ? 0.2071 0.2670 0.2176 -0.0026 -0.0249 0.0550  64  PHE B N   
1314 C  CA  . PHE B 96  ? 0.1964 0.2506 0.2005 -0.0075 -0.0413 0.0652  64  PHE B CA  
1315 C  C   . PHE B 96  ? 0.2154 0.2536 0.1926 -0.0250 -0.0099 0.0328  64  PHE B C   
1316 O  O   . PHE B 96  ? 0.2348 0.2619 0.2323 -0.0267 -0.0124 0.0186  64  PHE B O   
1317 C  CB  . PHE B 96  ? 0.2331 0.2606 0.2176 -0.0121 -0.0243 0.0243  64  PHE B CB  
1318 C  CG  . PHE B 96  ? 0.2088 0.2655 0.2289 -0.0244 -0.0333 0.0101  64  PHE B CG  
1319 C  CD1 . PHE B 96  ? 0.2177 0.2799 0.2234 -0.0260 -0.0392 0.0284  64  PHE B CD1 
1320 C  CD2 . PHE B 96  ? 0.2746 0.2561 0.2428 -0.0087 -0.0272 0.0029  64  PHE B CD2 
1321 C  CE1 . PHE B 96  ? 0.2428 0.2696 0.2443 -0.0182 -0.0425 0.0290  64  PHE B CE1 
1322 C  CE2 . PHE B 96  ? 0.3023 0.2606 0.2473 -0.0113 -0.0332 0.0192  64  PHE B CE2 
1323 C  CZ  . PHE B 96  ? 0.2654 0.2705 0.2280 -0.0320 -0.0329 0.0188  64  PHE B CZ  
1324 N  N   . VAL B 97  ? 0.2098 0.2613 0.1796 -0.0377 0.0097  0.0454  65  VAL B N   
1325 C  CA  . VAL B 97  ? 0.2530 0.2560 0.2066 -0.0596 0.0040  0.0387  65  VAL B CA  
1326 C  C   . VAL B 97  ? 0.2047 0.2436 0.1907 -0.0103 0.0326  0.0370  65  VAL B C   
1327 O  O   . VAL B 97  ? 0.2045 0.2501 0.1997 -0.0169 0.0345  0.0472  65  VAL B O   
1328 C  CB  . VAL B 97  ? 0.3353 0.2838 0.2627 -0.0703 -0.0291 0.0397  65  VAL B CB  
1329 C  CG1 . VAL B 97  ? 0.3657 0.2966 0.2479 -0.1199 -0.0581 0.0881  65  VAL B CG1 
1330 C  CG2 . VAL B 97  ? 0.3512 0.2881 0.3208 -0.0321 -0.0500 0.0152  65  VAL B CG2 
1331 N  N   . GLU B 98  ? 0.2256 0.2630 0.2054 -0.0109 0.0092  0.0413  66  GLU B N   
1332 C  CA  . GLU B 98  ? 0.2376 0.2914 0.2398 -0.0196 -0.0204 0.0383  66  GLU B CA  
1333 C  C   . GLU B 98  ? 0.2550 0.2551 0.2242 -0.0165 0.0096  0.0686  66  GLU B C   
1334 O  O   . GLU B 98  ? 0.3202 0.2569 0.2604 0.0164  0.0457  0.0800  66  GLU B O   
1335 C  CB  . GLU B 98  ? 0.2559 0.3034 0.2717 -0.0555 -0.0328 0.0419  66  GLU B CB  
1336 C  CG  . GLU B 98  ? 0.3769 0.3431 0.3158 -0.0666 -0.0500 0.0423  66  GLU B CG  
1337 C  CD  . GLU B 98  ? 0.5389 0.4038 0.4018 -0.0709 -0.0451 0.0475  66  GLU B CD  
1338 O  OE1 . GLU B 98  ? 0.5615 0.4103 0.4304 -0.0814 -0.0470 0.0161  66  GLU B OE1 
1339 O  OE2 . GLU B 98  ? 0.6181 0.4376 0.4173 -0.0591 -0.0460 0.0583  66  GLU B OE2 
1340 N  N   . GLY B 99  ? 0.2206 0.2748 0.1986 -0.0617 0.0197  0.0232  67  GLY B N   
1341 C  CA  . GLY B 99  ? 0.2049 0.2737 0.1853 -0.0355 0.0475  0.0386  67  GLY B CA  
1342 C  C   . GLY B 99  ? 0.1976 0.2680 0.1920 -0.0537 0.0233  0.0341  67  GLY B C   
1343 O  O   . GLY B 99  ? 0.2105 0.2728 0.1857 -0.0316 0.0169  0.0288  67  GLY B O   
1344 N  N   . ILE B 100 ? 0.2035 0.2516 0.1854 -0.0339 0.0057  0.0400  68  ILE B N   
1345 C  CA  . ILE B 100 ? 0.2113 0.2361 0.1644 -0.0312 0.0101  0.0368  68  ILE B CA  
1346 C  C   . ILE B 100 ? 0.2048 0.2116 0.1678 -0.0119 -0.0056 0.0333  68  ILE B C   
1347 O  O   . ILE B 100 ? 0.2379 0.2088 0.2121 -0.0038 -0.0201 0.0264  68  ILE B O   
1348 C  CB  . ILE B 100 ? 0.2332 0.2692 0.1586 -0.0048 -0.0006 0.0228  68  ILE B CB  
1349 C  CG1 . ILE B 100 ? 0.2792 0.3108 0.1901 -0.0054 -0.0311 -0.0046 68  ILE B CG1 
1350 C  CG2 . ILE B 100 ? 0.2638 0.2815 0.1371 -0.0226 0.0210  0.0538  68  ILE B CG2 
1351 C  CD1 . ILE B 100 ? 0.3075 0.3441 0.2172 -0.0009 -0.0380 -0.0117 68  ILE B CD1 
1352 N  N   . TYR B 101 ? 0.2134 0.2013 0.1576 -0.0388 -0.0108 0.0282  69  TYR B N   
1353 C  CA  . TYR B 101 ? 0.1798 0.1922 0.1662 -0.0065 -0.0103 0.0272  69  TYR B CA  
1354 C  C   . TYR B 101 ? 0.1743 0.1866 0.1759 0.0086  0.0117  0.0242  69  TYR B C   
1355 O  O   . TYR B 101 ? 0.1730 0.2170 0.1771 0.0231  0.0169  0.0338  69  TYR B O   
1356 C  CB  . TYR B 101 ? 0.2045 0.1978 0.1478 -0.0200 0.0032  0.0079  69  TYR B CB  
1357 C  CG  . TYR B 101 ? 0.1803 0.1929 0.1432 -0.0168 -0.0096 0.0406  69  TYR B CG  
1358 C  CD1 . TYR B 101 ? 0.1787 0.1971 0.1690 -0.0228 -0.0168 0.0457  69  TYR B CD1 
1359 C  CD2 . TYR B 101 ? 0.1938 0.2329 0.1432 -0.0076 0.0180  0.0487  69  TYR B CD2 
1360 C  CE1 . TYR B 101 ? 0.1839 0.2278 0.1672 -0.0168 -0.0088 0.0661  69  TYR B CE1 
1361 C  CE2 . TYR B 101 ? 0.1699 0.2261 0.1538 -0.0202 0.0247  0.0369  69  TYR B CE2 
1362 C  CZ  . TYR B 101 ? 0.1651 0.2476 0.1510 -0.0149 0.0233  0.0596  69  TYR B CZ  
1363 O  OH  . TYR B 101 ? 0.2132 0.2907 0.1658 -0.0170 0.0236  0.0642  69  TYR B OH  
1364 N  N   . LYS B 102 ? 0.1816 0.2082 0.1562 0.0146  0.0231  0.0276  70  LYS B N   
1365 C  CA  . LYS B 102 ? 0.1755 0.2473 0.1562 0.0019  -0.0001 0.0300  70  LYS B CA  
1366 C  C   . LYS B 102 ? 0.1655 0.2338 0.1730 -0.0070 -0.0101 0.0484  70  LYS B C   
1367 O  O   . LYS B 102 ? 0.2159 0.2350 0.1897 -0.0017 -0.0153 0.0752  70  LYS B O   
1368 C  CB  . LYS B 102 ? 0.2142 0.2993 0.1740 0.0087  0.0301  0.0102  70  LYS B CB  
1369 C  CG  . LYS B 102 ? 0.2185 0.3292 0.2017 0.0341  0.0419  -0.0015 70  LYS B CG  
1370 C  CD  . LYS B 102 ? 0.2936 0.3635 0.2155 0.0746  0.0551  0.0007  70  LYS B CD  
1371 C  CE  . LYS B 102 ? 0.3793 0.3812 0.2515 0.0891  0.0818  -0.0316 70  LYS B CE  
1372 N  NZ  . LYS B 102 ? 0.4382 0.4192 0.2764 0.0746  0.0986  -0.0439 70  LYS B NZ  
1373 N  N   . VAL B 103 ? 0.1554 0.2230 0.1987 -0.0164 -0.0371 0.0551  71  VAL B N   
1374 C  CA  . VAL B 103 ? 0.1642 0.2437 0.1971 -0.0128 -0.0019 0.0457  71  VAL B CA  
1375 C  C   . VAL B 103 ? 0.1765 0.2635 0.1967 -0.0186 0.0031  0.0472  71  VAL B C   
1376 O  O   . VAL B 103 ? 0.1790 0.2865 0.2054 -0.0162 -0.0065 0.0753  71  VAL B O   
1377 C  CB  . VAL B 103 ? 0.1983 0.2430 0.2015 -0.0281 -0.0161 0.0409  71  VAL B CB  
1378 C  CG1 . VAL B 103 ? 0.2419 0.2595 0.1960 -0.0365 -0.0126 0.0275  71  VAL B CG1 
1379 C  CG2 . VAL B 103 ? 0.1868 0.2304 0.2414 -0.0098 0.0103  0.0389  71  VAL B CG2 
1380 N  N   . GLU B 104 ? 0.1728 0.2364 0.1903 -0.0082 0.0102  0.0362  72  GLU B N   
1381 C  CA  . GLU B 104 ? 0.1620 0.2432 0.2043 0.0146  -0.0081 0.0114  72  GLU B CA  
1382 C  C   . GLU B 104 ? 0.1520 0.2227 0.1444 0.0031  -0.0175 0.0273  72  GLU B C   
1383 O  O   . GLU B 104 ? 0.1870 0.2266 0.1618 0.0130  -0.0116 0.0186  72  GLU B O   
1384 C  CB  . GLU B 104 ? 0.2414 0.2818 0.2490 0.0229  -0.0246 -0.0124 72  GLU B CB  
1385 C  CG  . GLU B 104 ? 0.3267 0.3369 0.2954 0.0592  -0.0320 -0.0330 72  GLU B CG  
1386 C  CD  . GLU B 104 ? 0.3932 0.3853 0.3146 0.0756  -0.0256 -0.0461 72  GLU B CD  
1387 O  OE1 . GLU B 104 ? 0.4574 0.4459 0.3621 0.0767  0.0071  -0.0299 72  GLU B OE1 
1388 O  OE2 . GLU B 104 ? 0.3885 0.3946 0.3161 0.0975  -0.0476 -0.0351 72  GLU B OE2 
1389 N  N   . ILE B 105 ? 0.1680 0.2169 0.1632 -0.0074 -0.0104 0.0190  73  ILE B N   
1390 C  CA  . ILE B 105 ? 0.1688 0.2091 0.1680 -0.0198 0.0100  0.0234  73  ILE B CA  
1391 C  C   . ILE B 105 ? 0.1533 0.2077 0.1648 -0.0187 0.0276  0.0320  73  ILE B C   
1392 O  O   . ILE B 105 ? 0.2002 0.2263 0.1567 0.0064  0.0185  0.0143  73  ILE B O   
1393 C  CB  . ILE B 105 ? 0.1979 0.2182 0.1731 -0.0017 0.0196  0.0099  73  ILE B CB  
1394 C  CG1 . ILE B 105 ? 0.2159 0.2258 0.1877 0.0539  0.0383  0.0269  73  ILE B CG1 
1395 C  CG2 . ILE B 105 ? 0.2725 0.2138 0.1847 -0.0103 0.0511  -0.0011 73  ILE B CG2 
1396 C  CD1 . ILE B 105 ? 0.2566 0.2334 0.2053 0.0606  0.0458  0.0279  73  ILE B CD1 
1397 N  N   . ASP B 106 ? 0.1511 0.2050 0.1789 -0.0088 0.0191  0.0115  74  ASP B N   
1398 C  CA  . ASP B 106 ? 0.1681 0.1938 0.1987 0.0051  0.0231  0.0308  74  ASP B CA  
1399 C  C   . ASP B 106 ? 0.1862 0.1911 0.1905 -0.0266 0.0322  0.0112  74  ASP B C   
1400 O  O   . ASP B 106 ? 0.1940 0.1899 0.1974 -0.0239 0.0174  0.0209  74  ASP B O   
1401 C  CB  . ASP B 106 ? 0.1801 0.2154 0.2328 0.0295  0.0329  0.0426  74  ASP B CB  
1402 C  CG  . ASP B 106 ? 0.1971 0.2224 0.2611 0.0277  0.0514  0.0597  74  ASP B CG  
1403 O  OD1 . ASP B 106 ? 0.2055 0.2137 0.2634 0.0015  0.0312  0.0328  74  ASP B OD1 
1404 O  OD2 . ASP B 106 ? 0.2282 0.2506 0.3162 0.0480  0.0335  0.0634  74  ASP B OD2 
1405 N  N   . THR B 107 ? 0.2043 0.1763 0.1709 0.0181  0.0296  0.0182  75  THR B N   
1406 C  CA  . THR B 107 ? 0.1802 0.1736 0.1769 0.0046  0.0224  0.0382  75  THR B CA  
1407 C  C   . THR B 107 ? 0.1845 0.1690 0.1798 0.0197  0.0105  0.0290  75  THR B C   
1408 O  O   . THR B 107 ? 0.2188 0.1841 0.2184 -0.0113 0.0129  0.0159  75  THR B O   
1409 C  CB  . THR B 107 ? 0.1987 0.1748 0.1929 -0.0065 0.0391  0.0007  75  THR B CB  
1410 O  OG1 . THR B 107 ? 0.1923 0.1862 0.2097 -0.0004 0.0149  0.0070  75  THR B OG1 
1411 C  CG2 . THR B 107 ? 0.1979 0.1796 0.2233 0.0003  0.0545  0.0061  75  THR B CG2 
1412 N  N   . LYS B 108 ? 0.1577 0.1940 0.1766 0.0136  0.0431  0.0126  76  LYS B N   
1413 C  CA  . LYS B 108 ? 0.1835 0.2152 0.2024 0.0280  0.0447  -0.0154 76  LYS B CA  
1414 C  C   . LYS B 108 ? 0.2058 0.2140 0.2015 0.0078  0.0209  0.0087  76  LYS B C   
1415 O  O   . LYS B 108 ? 0.1921 0.2327 0.2310 0.0115  0.0282  0.0372  76  LYS B O   
1416 C  CB  . LYS B 108 ? 0.2088 0.2232 0.2290 0.0474  0.0752  -0.0430 76  LYS B CB  
1417 C  CG  . LYS B 108 ? 0.2592 0.2781 0.2834 0.0252  0.1046  -0.0891 76  LYS B CG  
1418 C  CD  . LYS B 108 ? 0.3111 0.3408 0.3177 0.0299  0.0898  -0.1145 76  LYS B CD  
1419 C  CE  . LYS B 108 ? 0.3917 0.3985 0.3588 0.0144  0.0667  -0.1266 76  LYS B CE  
1420 N  NZ  . LYS B 108 ? 0.4519 0.4272 0.3950 0.0175  0.0306  -0.1199 76  LYS B NZ  
1421 N  N   . SER B 109 ? 0.1791 0.2244 0.2077 0.0316  0.0248  0.0054  77  SER B N   
1422 C  CA  . SER B 109 ? 0.1998 0.2243 0.2152 0.0166  0.0018  0.0242  77  SER B CA  
1423 C  C   . SER B 109 ? 0.2009 0.2550 0.2252 0.0116  0.0002  0.0074  77  SER B C   
1424 O  O   . SER B 109 ? 0.1929 0.2776 0.2475 0.0098  0.0068  -0.0153 77  SER B O   
1425 C  CB  . SER B 109 ? 0.2117 0.2377 0.2493 0.0198  0.0103  0.0389  77  SER B CB  
1426 O  OG  . SER B 109 ? 0.2281 0.2520 0.2794 0.0417  0.0132  0.0338  77  SER B OG  
1427 N  N   . TYR B 110 ? 0.2079 0.2384 0.2237 0.0252  -0.0066 -0.0064 78  TYR B N   
1428 C  CA  . TYR B 110 ? 0.1729 0.2247 0.2248 0.0182  0.0052  -0.0167 78  TYR B CA  
1429 C  C   . TYR B 110 ? 0.1668 0.2184 0.2353 -0.0072 0.0012  -0.0291 78  TYR B C   
1430 O  O   . TYR B 110 ? 0.1790 0.2561 0.2804 0.0015  -0.0116 -0.0394 78  TYR B O   
1431 C  CB  . TYR B 110 ? 0.1731 0.2132 0.2352 0.0157  0.0087  -0.0279 78  TYR B CB  
1432 C  CG  . TYR B 110 ? 0.1800 0.2068 0.2129 0.0055  0.0088  -0.0165 78  TYR B CG  
1433 C  CD1 . TYR B 110 ? 0.1962 0.2089 0.2263 0.0238  0.0346  -0.0359 78  TYR B CD1 
1434 C  CD2 . TYR B 110 ? 0.1683 0.2190 0.2099 0.0261  0.0162  0.0074  78  TYR B CD2 
1435 C  CE1 . TYR B 110 ? 0.2314 0.1972 0.2374 0.0408  0.0144  -0.0156 78  TYR B CE1 
1436 C  CE2 . TYR B 110 ? 0.1839 0.2241 0.1762 0.0307  -0.0023 0.0053  78  TYR B CE2 
1437 C  CZ  . TYR B 110 ? 0.2195 0.2136 0.1978 0.0410  0.0043  -0.0156 78  TYR B CZ  
1438 O  OH  . TYR B 110 ? 0.2459 0.2191 0.2329 0.0243  0.0042  0.0054  78  TYR B OH  
1439 N  N   . TRP B 111 ? 0.1717 0.2138 0.2266 0.0134  0.0046  -0.0077 79  TRP B N   
1440 C  CA  . TRP B 111 ? 0.1556 0.2061 0.2524 0.0137  0.0189  0.0073  79  TRP B CA  
1441 C  C   . TRP B 111 ? 0.1639 0.2158 0.3246 0.0268  0.0076  -0.0017 79  TRP B C   
1442 O  O   . TRP B 111 ? 0.1655 0.2498 0.3718 -0.0085 0.0284  0.0164  79  TRP B O   
1443 C  CB  . TRP B 111 ? 0.1768 0.2144 0.2464 0.0105  0.0300  0.0025  79  TRP B CB  
1444 C  CG  . TRP B 111 ? 0.1576 0.1973 0.2190 0.0066  0.0163  -0.0086 79  TRP B CG  
1445 C  CD1 . TRP B 111 ? 0.1842 0.2057 0.1969 -0.0058 0.0258  0.0038  79  TRP B CD1 
1446 C  CD2 . TRP B 111 ? 0.1813 0.1765 0.2282 0.0016  -0.0005 -0.0088 79  TRP B CD2 
1447 N  NE1 . TRP B 111 ? 0.1809 0.1738 0.1960 0.0054  0.0217  0.0076  79  TRP B NE1 
1448 C  CE2 . TRP B 111 ? 0.1958 0.1759 0.2114 0.0072  0.0199  -0.0127 79  TRP B CE2 
1449 C  CE3 . TRP B 111 ? 0.1951 0.1785 0.2382 -0.0014 -0.0244 -0.0106 79  TRP B CE3 
1450 C  CZ2 . TRP B 111 ? 0.2267 0.1736 0.2203 0.0128  0.0093  0.0027  79  TRP B CZ2 
1451 C  CZ3 . TRP B 111 ? 0.1950 0.1801 0.2594 0.0159  -0.0410 0.0168  79  TRP B CZ3 
1452 C  CH2 . TRP B 111 ? 0.1910 0.1919 0.2321 0.0066  -0.0329 -0.0012 79  TRP B CH2 
1453 N  N   . LYS B 112 ? 0.1289 0.2183 0.3405 0.0303  0.0176  -0.0195 80  LYS B N   
1454 C  CA  . LYS B 112 ? 0.1305 0.2618 0.3979 0.0464  0.0444  -0.0299 80  LYS B CA  
1455 C  C   . LYS B 112 ? 0.1614 0.2900 0.4252 0.0344  0.0417  -0.0282 80  LYS B C   
1456 O  O   . LYS B 112 ? 0.1862 0.3343 0.4550 0.0219  0.0483  -0.0099 80  LYS B O   
1457 C  CB  . LYS B 112 ? 0.2144 0.2880 0.4233 0.0633  0.0295  -0.0375 80  LYS B CB  
1458 C  CG  . LYS B 112 ? 0.3752 0.3307 0.4760 0.0584  0.0330  -0.0503 80  LYS B CG  
1459 C  CD  . LYS B 112 ? 0.5166 0.3948 0.5419 0.0896  0.0209  -0.0614 80  LYS B CD  
1460 C  CE  . LYS B 112 ? 0.6447 0.4253 0.5836 0.1051  0.0003  -0.0691 80  LYS B CE  
1461 N  NZ  . LYS B 112 ? 0.7333 0.4438 0.6166 0.1074  -0.0203 -0.0655 80  LYS B NZ  
1462 N  N   . ALA B 113 ? 0.2057 0.2836 0.4222 0.0353  -0.0241 -0.0403 81  ALA B N   
1463 C  CA  . ALA B 113 ? 0.2462 0.3221 0.4527 -0.0023 -0.0711 -0.0525 81  ALA B CA  
1464 C  C   . ALA B 113 ? 0.2592 0.3518 0.4919 -0.0141 -0.0849 -0.0708 81  ALA B C   
1465 O  O   . ALA B 113 ? 0.2715 0.3784 0.5282 -0.0268 -0.1331 -0.0702 81  ALA B O   
1466 C  CB  . ALA B 113 ? 0.2873 0.3314 0.4474 -0.0013 -0.0861 -0.0547 81  ALA B CB  
1467 N  N   . LEU B 114 ? 0.2593 0.3398 0.4885 -0.0086 -0.0361 -0.0729 82  LEU B N   
1468 C  CA  . LEU B 114 ? 0.2664 0.3590 0.5184 -0.0326 -0.0149 -0.0525 82  LEU B CA  
1469 C  C   . LEU B 114 ? 0.2707 0.3511 0.5535 -0.0448 0.0419  -0.0183 82  LEU B C   
1470 O  O   . LEU B 114 ? 0.2916 0.3538 0.5905 -0.0549 0.0389  -0.0100 82  LEU B O   
1471 C  CB  . LEU B 114 ? 0.2730 0.3570 0.4926 -0.0097 -0.0467 -0.0652 82  LEU B CB  
1472 C  CG  . LEU B 114 ? 0.3053 0.3954 0.4802 -0.0040 -0.0617 -0.0758 82  LEU B CG  
1473 C  CD1 . LEU B 114 ? 0.3198 0.4015 0.4799 0.0133  -0.0581 -0.0804 82  LEU B CD1 
1474 C  CD2 . LEU B 114 ? 0.3761 0.4195 0.4845 -0.0167 -0.0485 -0.0826 82  LEU B CD2 
1475 N  N   . GLY B 115 ? 0.2215 0.3438 0.5580 -0.0096 0.0588  0.0036  83  GLY B N   
1476 C  CA  . GLY B 115 ? 0.2322 0.3591 0.5555 -0.0370 0.0900  0.0261  83  GLY B CA  
1477 C  C   . GLY B 115 ? 0.1882 0.3735 0.5522 -0.0197 0.0976  0.0442  83  GLY B C   
1478 O  O   . GLY B 115 ? 0.2271 0.3942 0.5890 -0.0222 0.1016  0.0373  83  GLY B O   
1479 N  N   . ILE B 116 ? 0.2138 0.3848 0.5244 -0.0390 0.1032  0.0506  84  ILE B N   
1480 C  CA  . ILE B 116 ? 0.2534 0.4114 0.4945 -0.0397 0.1071  0.0513  84  ILE B CA  
1481 C  C   . ILE B 116 ? 0.2798 0.4476 0.4634 -0.0447 0.1166  0.0452  84  ILE B C   
1482 O  O   . ILE B 116 ? 0.3067 0.4541 0.4603 -0.0504 0.1063  0.0506  84  ILE B O   
1483 C  CB  . ILE B 116 ? 0.2596 0.4107 0.5056 -0.0085 0.0781  0.0427  84  ILE B CB  
1484 C  CG1 . ILE B 116 ? 0.2714 0.4047 0.5167 -0.0043 0.0950  0.0345  84  ILE B CG1 
1485 C  CG2 . ILE B 116 ? 0.2663 0.4247 0.5067 0.0076  0.0517  0.0450  84  ILE B CG2 
1486 C  CD1 . ILE B 116 ? 0.2924 0.4022 0.5310 0.0032  0.0905  0.0289  84  ILE B CD1 
1487 N  N   . SER B 117 ? 0.2286 0.4618 0.4439 -0.0443 0.1297  0.0379  85  SER B N   
1488 C  CA  . SER B 117 ? 0.2325 0.4472 0.4113 -0.0537 0.1340  0.0350  85  SER B CA  
1489 C  C   . SER B 117 ? 0.2682 0.3962 0.3832 -0.0197 0.0908  0.0491  85  SER B C   
1490 O  O   . SER B 117 ? 0.3429 0.4266 0.3992 -0.0855 0.0716  0.0815  85  SER B O   
1491 C  CB  . SER B 117 ? 0.2735 0.4892 0.4265 -0.0689 0.1185  0.0180  85  SER B CB  
1492 O  OG  . SER B 117 ? 0.3359 0.5222 0.4326 -0.0420 0.1160  -0.0056 85  SER B OG  
1493 N  N   . PRO B 118 ? 0.2191 0.3173 0.3083 -0.0052 0.0890  0.0227  86  PRO B N   
1494 C  CA  . PRO B 118 ? 0.2463 0.2813 0.2716 -0.0374 0.0766  -0.0061 86  PRO B CA  
1495 C  C   . PRO B 118 ? 0.2596 0.2490 0.2459 -0.0025 0.0846  -0.0284 86  PRO B C   
1496 O  O   . PRO B 118 ? 0.3041 0.2967 0.3024 0.0371  0.0679  -0.0339 86  PRO B O   
1497 C  CB  . PRO B 118 ? 0.3021 0.2845 0.2751 -0.0370 0.0843  -0.0073 86  PRO B CB  
1498 C  CG  . PRO B 118 ? 0.3297 0.2754 0.3005 -0.0235 0.0614  0.0094  86  PRO B CG  
1499 C  CD  . PRO B 118 ? 0.3091 0.2897 0.3181 -0.0052 0.0693  0.0171  86  PRO B CD  
1500 N  N   . PHE B 119 ? 0.2400 0.2005 0.1977 -0.0236 0.0594  0.0043  87  PHE B N   
1501 C  CA  . PHE B 119 ? 0.2705 0.1977 0.1578 -0.0070 0.0573  0.0095  87  PHE B CA  
1502 C  C   . PHE B 119 ? 0.2668 0.1855 0.1513 -0.0182 0.0507  -0.0009 87  PHE B C   
1503 O  O   . PHE B 119 ? 0.2768 0.1868 0.1884 0.0093  0.0566  -0.0144 87  PHE B O   
1504 C  CB  . PHE B 119 ? 0.3150 0.1979 0.1846 0.0032  0.0461  0.0212  87  PHE B CB  
1505 C  CG  . PHE B 119 ? 0.3517 0.1716 0.1833 0.0181  0.0214  -0.0079 87  PHE B CG  
1506 C  CD1 . PHE B 119 ? 0.3951 0.1960 0.1958 0.0450  0.0138  0.0147  87  PHE B CD1 
1507 C  CD2 . PHE B 119 ? 0.3524 0.1708 0.2018 0.0004  -0.0302 -0.0088 87  PHE B CD2 
1508 C  CE1 . PHE B 119 ? 0.3981 0.1968 0.1968 0.0435  -0.0056 -0.0121 87  PHE B CE1 
1509 C  CE2 . PHE B 119 ? 0.3954 0.1945 0.2052 0.0184  -0.0274 -0.0161 87  PHE B CE2 
1510 C  CZ  . PHE B 119 ? 0.4007 0.1913 0.2093 0.0306  -0.0131 -0.0152 87  PHE B CZ  
1511 N  N   . HIS B 120 ? 0.2329 0.1891 0.1575 -0.0235 0.0129  0.0038  88  HIS B N   
1512 C  CA  . HIS B 120 ? 0.1961 0.1819 0.1617 -0.0082 0.0274  -0.0031 88  HIS B CA  
1513 C  C   . HIS B 120 ? 0.1923 0.1976 0.1605 -0.0206 0.0121  -0.0090 88  HIS B C   
1514 O  O   . HIS B 120 ? 0.2165 0.1909 0.1800 -0.0270 -0.0173 -0.0198 88  HIS B O   
1515 C  CB  . HIS B 120 ? 0.2150 0.1954 0.1532 0.0149  0.0053  0.0110  88  HIS B CB  
1516 C  CG  . HIS B 120 ? 0.2199 0.1640 0.1905 0.0012  0.0044  0.0143  88  HIS B CG  
1517 N  ND1 . HIS B 120 ? 0.2230 0.1706 0.2244 -0.0051 -0.0019 0.0121  88  HIS B ND1 
1518 C  CD2 . HIS B 120 ? 0.2698 0.1830 0.2206 0.0109  -0.0007 0.0133  88  HIS B CD2 
1519 C  CE1 . HIS B 120 ? 0.2612 0.1803 0.2458 -0.0061 -0.0439 0.0006  88  HIS B CE1 
1520 N  NE2 . HIS B 120 ? 0.2885 0.1846 0.2513 -0.0088 -0.0426 0.0008  88  HIS B NE2 
1521 N  N   . GLU B 121 ? 0.1935 0.1799 0.1873 -0.0128 0.0096  -0.0060 89  GLU B N   
1522 C  CA  . GLU B 121 ? 0.1929 0.1860 0.1978 -0.0007 -0.0013 -0.0071 89  GLU B CA  
1523 C  C   . GLU B 121 ? 0.1974 0.2246 0.2065 -0.0296 -0.0097 0.0053  89  GLU B C   
1524 O  O   . GLU B 121 ? 0.2395 0.2717 0.2279 -0.0325 0.0069  0.0106  89  GLU B O   
1525 C  CB  . GLU B 121 ? 0.2363 0.1971 0.2495 0.0201  0.0003  -0.0152 89  GLU B CB  
1526 C  CG  . GLU B 121 ? 0.2447 0.2507 0.2822 0.0290  -0.0031 -0.0300 89  GLU B CG  
1527 C  CD  . GLU B 121 ? 0.2980 0.2853 0.2943 0.0613  -0.0292 -0.0534 89  GLU B CD  
1528 O  OE1 . GLU B 121 ? 0.3882 0.3358 0.3138 0.0644  -0.0359 -0.0390 89  GLU B OE1 
1529 O  OE2 . GLU B 121 ? 0.3458 0.3046 0.3248 0.0599  -0.0107 -0.0762 89  GLU B OE2 
1530 N  N   . HIS B 122 ? 0.2117 0.2158 0.1780 -0.0348 0.0119  0.0320  90  HIS B N   
1531 C  CA  . HIS B 122 ? 0.2064 0.2373 0.1573 -0.0210 0.0431  0.0457  90  HIS B CA  
1532 C  C   . HIS B 122 ? 0.2104 0.2938 0.1709 -0.0009 0.0329  0.0476  90  HIS B C   
1533 O  O   . HIS B 122 ? 0.2283 0.3545 0.1854 -0.0006 0.0194  0.0554  90  HIS B O   
1534 C  CB  . HIS B 122 ? 0.2657 0.2461 0.2028 -0.0386 0.0263  0.0418  90  HIS B CB  
1535 C  CG  . HIS B 122 ? 0.4071 0.2839 0.2818 -0.0473 0.0220  0.0398  90  HIS B CG  
1536 N  ND1 . HIS B 122 ? 0.5330 0.3132 0.3443 -0.0463 -0.0204 0.0158  90  HIS B ND1 
1537 C  CD2 . HIS B 122 ? 0.4805 0.3208 0.3242 -0.0616 0.0225  0.0372  90  HIS B CD2 
1538 C  CE1 . HIS B 122 ? 0.5771 0.3285 0.3448 -0.0500 -0.0066 0.0167  90  HIS B CE1 
1539 N  NE2 . HIS B 122 ? 0.5616 0.3217 0.3281 -0.0555 0.0167  0.0331  90  HIS B NE2 
1540 N  N   . ALA B 123 ? 0.1754 0.3409 0.1696 0.0187  0.0693  0.0758  91  ALA B N   
1541 C  CA  . ALA B 123 ? 0.1845 0.3591 0.2060 0.0266  0.0377  0.0798  91  ALA B CA  
1542 C  C   . ALA B 123 ? 0.1896 0.3746 0.2228 0.0018  0.0215  0.0916  91  ALA B C   
1543 O  O   . ALA B 123 ? 0.2318 0.4013 0.2236 -0.0284 -0.0002 0.1110  91  ALA B O   
1544 C  CB  . ALA B 123 ? 0.2558 0.3593 0.2571 0.0517  0.0194  0.0891  91  ALA B CB  
1545 N  N   . GLU B 124 ? 0.1918 0.3983 0.2446 0.0171  0.0350  0.0622  92  GLU B N   
1546 C  CA  . GLU B 124 ? 0.1980 0.3872 0.2927 0.0025  0.0345  0.0439  92  GLU B CA  
1547 C  C   . GLU B 124 ? 0.2190 0.3585 0.2529 0.0030  0.0231  0.0587  92  GLU B C   
1548 O  O   . GLU B 124 ? 0.2996 0.3789 0.2540 0.0244  0.0080  0.0577  92  GLU B O   
1549 C  CB  . GLU B 124 ? 0.2623 0.4095 0.3267 0.0180  0.0132  0.0416  92  GLU B CB  
1550 N  N   . VAL B 125 ? 0.1538 0.2870 0.2000 -0.0507 0.0015  0.0331  93  VAL B N   
1551 C  CA  . VAL B 125 ? 0.1447 0.2429 0.1874 -0.0396 0.0062  0.0260  93  VAL B CA  
1552 C  C   . VAL B 125 ? 0.1232 0.2202 0.1647 -0.0244 0.0124  0.0287  93  VAL B C   
1553 O  O   . VAL B 125 ? 0.2009 0.2155 0.1765 -0.0150 -0.0147 0.0385  93  VAL B O   
1554 C  CB  . VAL B 125 ? 0.2089 0.2358 0.2361 -0.0468 0.0030  -0.0039 93  VAL B CB  
1555 C  CG1 . VAL B 125 ? 0.2512 0.2554 0.2699 -0.0180 0.0060  -0.0249 93  VAL B CG1 
1556 C  CG2 . VAL B 125 ? 0.2403 0.2665 0.2502 -0.0619 0.0054  0.0006  93  VAL B CG2 
1557 N  N   . VAL B 126 ? 0.1213 0.2072 0.1589 -0.0014 -0.0019 0.0201  94  VAL B N   
1558 C  CA  . VAL B 126 ? 0.1559 0.2081 0.1529 -0.0119 0.0113  0.0061  94  VAL B CA  
1559 C  C   . VAL B 126 ? 0.1805 0.1908 0.1654 0.0009  0.0239  0.0159  94  VAL B C   
1560 O  O   . VAL B 126 ? 0.1808 0.1799 0.1654 0.0240  0.0270  0.0330  94  VAL B O   
1561 C  CB  . VAL B 126 ? 0.1732 0.2279 0.1768 0.0083  0.0109  -0.0115 94  VAL B CB  
1562 C  CG1 . VAL B 126 ? 0.2433 0.2150 0.2107 -0.0012 -0.0265 -0.0097 94  VAL B CG1 
1563 C  CG2 . VAL B 126 ? 0.2133 0.2553 0.2168 0.0235  0.0050  0.0068  94  VAL B CG2 
1564 N  N   . PHE B 127 ? 0.1894 0.2076 0.1741 0.0209  0.0361  0.0190  95  PHE B N   
1565 C  CA  . PHE B 127 ? 0.1587 0.2115 0.1663 -0.0047 0.0249  0.0170  95  PHE B CA  
1566 C  C   . PHE B 127 ? 0.1299 0.2424 0.1896 -0.0035 0.0131  0.0072  95  PHE B C   
1567 O  O   . PHE B 127 ? 0.1874 0.2106 0.2063 0.0176  0.0087  -0.0041 95  PHE B O   
1568 C  CB  . PHE B 127 ? 0.1996 0.2021 0.1641 0.0148  -0.0174 0.0012  95  PHE B CB  
1569 C  CG  . PHE B 127 ? 0.2184 0.2197 0.1852 -0.0210 -0.0183 0.0027  95  PHE B CG  
1570 C  CD1 . PHE B 127 ? 0.2586 0.2287 0.2025 -0.0104 -0.0475 -0.0052 95  PHE B CD1 
1571 C  CD2 . PHE B 127 ? 0.2706 0.2081 0.1769 -0.0262 -0.0305 0.0347  95  PHE B CD2 
1572 C  CE1 . PHE B 127 ? 0.3132 0.2392 0.2206 -0.0137 -0.0505 0.0061  95  PHE B CE1 
1573 C  CE2 . PHE B 127 ? 0.2999 0.1983 0.2029 -0.0343 -0.0446 0.0130  95  PHE B CE2 
1574 C  CZ  . PHE B 127 ? 0.3364 0.2179 0.2142 -0.0236 -0.0668 0.0018  95  PHE B CZ  
1575 N  N   . THR B 128 ? 0.1589 0.2786 0.2001 -0.0123 0.0210  0.0410  96  THR B N   
1576 C  CA  . THR B 128 ? 0.1615 0.2940 0.1792 -0.0225 0.0143  0.0334  96  THR B CA  
1577 C  C   . THR B 128 ? 0.2088 0.2928 0.1975 -0.0052 0.0197  0.0331  96  THR B C   
1578 O  O   . THR B 128 ? 0.2684 0.2805 0.2041 0.0042  0.0577  0.0328  96  THR B O   
1579 C  CB  . THR B 128 ? 0.1843 0.2999 0.1883 -0.0374 0.0269  0.0148  96  THR B CB  
1580 O  OG1 . THR B 128 ? 0.2424 0.2982 0.2069 -0.0113 -0.0034 -0.0121 96  THR B OG1 
1581 C  CG2 . THR B 128 ? 0.2278 0.3069 0.2098 -0.0396 0.0480  0.0186  96  THR B CG2 
1582 N  N   . ALA B 129 ? 0.1841 0.2726 0.1638 -0.0128 0.0186  0.0315  97  ALA B N   
1583 C  CA  . ALA B 129 ? 0.1741 0.2415 0.1959 -0.0115 0.0195  0.0385  97  ALA B CA  
1584 C  C   . ALA B 129 ? 0.2451 0.2270 0.2167 0.0220  0.0219  0.0476  97  ALA B C   
1585 O  O   . ALA B 129 ? 0.2425 0.2186 0.2340 0.0107  0.0278  0.0414  97  ALA B O   
1586 C  CB  . ALA B 129 ? 0.2412 0.2639 0.1920 -0.0025 -0.0294 0.0282  97  ALA B CB  
1587 N  N   . ASN B 130 ? 0.2354 0.2425 0.1897 0.0163  0.0217  0.0259  98  ASN B N   
1588 C  CA  . ASN B 130 ? 0.2137 0.2601 0.2316 -0.0029 0.0233  0.0321  98  ASN B CA  
1589 C  C   . ASN B 130 ? 0.2134 0.2754 0.2717 -0.0084 0.0203  0.0044  98  ASN B C   
1590 O  O   . ASN B 130 ? 0.2019 0.2525 0.2796 -0.0017 0.0350  0.0397  98  ASN B O   
1591 C  CB  . ASN B 130 ? 0.2577 0.2715 0.2231 -0.0007 0.0055  0.0407  98  ASN B CB  
1592 C  CG  . ASN B 130 ? 0.2394 0.2756 0.2090 -0.0069 0.0419  0.0306  98  ASN B CG  
1593 O  OD1 . ASN B 130 ? 0.2489 0.2789 0.2300 0.0053  0.0482  -0.0045 98  ASN B OD1 
1594 N  ND2 . ASN B 130 ? 0.2210 0.2761 0.2144 0.0007  0.0125  0.0503  98  ASN B ND2 
1595 N  N   . ASP B 131 ? 0.2385 0.3154 0.3072 0.0189  -0.0029 -0.0103 99  ASP B N   
1596 C  CA  . ASP B 131 ? 0.3462 0.3637 0.3522 0.0497  -0.0238 -0.0061 99  ASP B CA  
1597 C  C   . ASP B 131 ? 0.3722 0.3108 0.3231 0.0737  0.0051  -0.0083 99  ASP B C   
1598 O  O   . ASP B 131 ? 0.4287 0.3195 0.3322 0.1041  -0.0210 0.0092  99  ASP B O   
1599 C  CB  . ASP B 131 ? 0.5167 0.4784 0.4345 0.0477  -0.0657 -0.0190 99  ASP B CB  
1600 C  CG  . ASP B 131 ? 0.7349 0.5650 0.5546 0.0692  -0.0653 -0.0253 99  ASP B CG  
1601 O  OD1 . ASP B 131 ? 0.7767 0.5840 0.5837 0.0688  -0.0745 -0.0347 99  ASP B OD1 
1602 O  OD2 . ASP B 131 ? 0.8375 0.6027 0.5910 0.0651  -0.0738 -0.0299 99  ASP B OD2 
1603 N  N   . SER B 132 ? 0.2963 0.2741 0.2900 0.0343  0.0171  0.0152  100 SER B N   
1604 C  CA  . SER B 132 ? 0.3160 0.2894 0.2880 0.0342  0.0122  0.0429  100 SER B CA  
1605 C  C   . SER B 132 ? 0.2794 0.2728 0.2906 -0.0167 0.0384  0.0398  100 SER B C   
1606 O  O   . SER B 132 ? 0.2541 0.2699 0.3182 -0.0056 0.0785  0.0147  100 SER B O   
1607 C  CB  . SER B 132 ? 0.3876 0.3373 0.3212 0.0699  0.0077  0.0623  100 SER B CB  
1608 O  OG  . SER B 132 ? 0.4526 0.3869 0.3507 0.0539  -0.0117 0.0614  100 SER B OG  
1609 N  N   . GLY B 133 ? 0.2291 0.2312 0.2649 -0.0078 0.0142  0.0538  101 GLY B N   
1610 C  CA  . GLY B 133 ? 0.2385 0.2473 0.2795 -0.0250 -0.0027 0.0342  101 GLY B CA  
1611 C  C   . GLY B 133 ? 0.2500 0.2536 0.2625 -0.0436 0.0376  0.0388  101 GLY B C   
1612 O  O   . GLY B 133 ? 0.2711 0.2446 0.2684 -0.0218 0.0590  0.0189  101 GLY B O   
1613 N  N   . PRO B 134 ? 0.2532 0.2722 0.2605 -0.0248 0.0214  0.0776  102 PRO B N   
1614 C  CA  . PRO B 134 ? 0.2722 0.2897 0.2770 -0.0430 0.0210  0.0775  102 PRO B CA  
1615 C  C   . PRO B 134 ? 0.2758 0.2741 0.3030 -0.0272 0.0214  0.0652  102 PRO B C   
1616 O  O   . PRO B 134 ? 0.2699 0.2708 0.3049 -0.0168 0.0166  0.0434  102 PRO B O   
1617 C  CB  . PRO B 134 ? 0.2991 0.3047 0.2809 -0.0576 -0.0023 0.0660  102 PRO B CB  
1618 C  CG  . PRO B 134 ? 0.3092 0.2924 0.2759 -0.1002 -0.0366 0.0659  102 PRO B CG  
1619 C  CD  . PRO B 134 ? 0.2485 0.2892 0.2605 -0.0714 -0.0124 0.0943  102 PRO B CD  
1620 N  N   . ARG B 135 ? 0.2244 0.2520 0.2731 -0.0397 0.0086  0.0669  103 ARG B N   
1621 C  CA  . ARG B 135 ? 0.2277 0.2369 0.2745 -0.0207 -0.0060 0.0476  103 ARG B CA  
1622 C  C   . ARG B 135 ? 0.2073 0.2848 0.2831 -0.0077 0.0139  0.0472  103 ARG B C   
1623 O  O   . ARG B 135 ? 0.2378 0.2757 0.2696 -0.0208 0.0176  0.0440  103 ARG B O   
1624 C  CB  . ARG B 135 ? 0.2520 0.2568 0.2769 -0.0036 -0.0133 0.0448  103 ARG B CB  
1625 C  CG  . ARG B 135 ? 0.2593 0.2650 0.2872 -0.0090 -0.0095 0.0364  103 ARG B CG  
1626 C  CD  . ARG B 135 ? 0.2355 0.2714 0.2906 0.0160  -0.0090 0.0354  103 ARG B CD  
1627 N  NE  . ARG B 135 ? 0.2218 0.2837 0.3119 -0.0239 0.0113  0.0347  103 ARG B NE  
1628 C  CZ  . ARG B 135 ? 0.2219 0.2908 0.3292 0.0131  0.0339  0.0523  103 ARG B CZ  
1629 N  NH1 . ARG B 135 ? 0.2598 0.3031 0.3493 0.0435  0.0611  0.0535  103 ARG B NH1 
1630 N  NH2 . ARG B 135 ? 0.2662 0.3088 0.3501 0.0176  -0.0212 0.0293  103 ARG B NH2 
1631 N  N   . ARG B 136 ? 0.2226 0.3089 0.2802 -0.0437 0.0088  0.0396  104 ARG B N   
1632 C  CA  . ARG B 136 ? 0.2454 0.3435 0.2666 -0.0214 0.0335  0.0490  104 ARG B CA  
1633 C  C   . ARG B 136 ? 0.2306 0.3048 0.2257 0.0052  0.0247  0.0465  104 ARG B C   
1634 O  O   . ARG B 136 ? 0.2382 0.3273 0.2290 0.0408  0.0455  0.0606  104 ARG B O   
1635 C  CB  . ARG B 136 ? 0.3646 0.4121 0.3301 0.0155  0.0408  0.0474  104 ARG B CB  
1636 C  CG  . ARG B 136 ? 0.5295 0.5223 0.4343 0.0243  -0.0110 0.0427  104 ARG B CG  
1637 C  CD  . ARG B 136 ? 0.6851 0.6300 0.5407 0.0088  -0.0505 0.0402  104 ARG B CD  
1638 N  NE  . ARG B 136 ? 0.7991 0.7237 0.6325 -0.0108 -0.0735 0.0428  104 ARG B NE  
1639 C  CZ  . ARG B 136 ? 0.8644 0.7988 0.6921 -0.0248 -0.0777 0.0489  104 ARG B CZ  
1640 N  NH1 . ARG B 136 ? 0.8724 0.8160 0.7030 -0.0390 -0.0751 0.0564  104 ARG B NH1 
1641 N  NH2 . ARG B 136 ? 0.8865 0.8152 0.7094 -0.0239 -0.0782 0.0506  104 ARG B NH2 
1642 N  N   . TYR B 137 ? 0.1694 0.2656 0.1941 -0.0118 0.0222  0.0198  105 TYR B N   
1643 C  CA  . TYR B 137 ? 0.1975 0.2543 0.1808 -0.0033 0.0536  0.0250  105 TYR B CA  
1644 C  C   . TYR B 137 ? 0.2140 0.2503 0.1865 -0.0192 0.0177  0.0436  105 TYR B C   
1645 O  O   . TYR B 137 ? 0.2085 0.2588 0.2216 -0.0108 -0.0024 0.0647  105 TYR B O   
1646 C  CB  . TYR B 137 ? 0.2105 0.2530 0.2125 -0.0129 0.0141  0.0000  105 TYR B CB  
1647 C  CG  . TYR B 137 ? 0.1757 0.2431 0.2073 -0.0268 -0.0004 0.0343  105 TYR B CG  
1648 C  CD1 . TYR B 137 ? 0.1976 0.2566 0.2396 -0.0180 -0.0071 0.0604  105 TYR B CD1 
1649 C  CD2 . TYR B 137 ? 0.2387 0.2476 0.2070 -0.0320 -0.0101 0.0447  105 TYR B CD2 
1650 C  CE1 . TYR B 137 ? 0.2370 0.2531 0.2464 -0.0210 -0.0366 0.0446  105 TYR B CE1 
1651 C  CE2 . TYR B 137 ? 0.2482 0.2382 0.2230 -0.0381 -0.0034 0.0506  105 TYR B CE2 
1652 C  CZ  . TYR B 137 ? 0.2216 0.2290 0.2326 -0.0337 -0.0181 0.0389  105 TYR B CZ  
1653 O  OH  . TYR B 137 ? 0.2458 0.2330 0.2919 -0.0230 -0.0144 0.0292  105 TYR B OH  
1654 N  N   . THR B 138 ? 0.1997 0.2529 0.1858 -0.0243 0.0284  0.0397  106 THR B N   
1655 C  CA  . THR B 138 ? 0.2007 0.2463 0.1789 -0.0096 0.0299  0.0196  106 THR B CA  
1656 C  C   . THR B 138 ? 0.1913 0.2423 0.1745 0.0027  0.0358  0.0324  106 THR B C   
1657 O  O   . THR B 138 ? 0.2004 0.2656 0.2026 0.0238  0.0145  0.0412  106 THR B O   
1658 C  CB  . THR B 138 ? 0.2314 0.2562 0.2181 -0.0072 0.0516  0.0006  106 THR B CB  
1659 O  OG1 . THR B 138 ? 0.3103 0.3016 0.2378 0.0370  0.0465  -0.0186 106 THR B OG1 
1660 C  CG2 . THR B 138 ? 0.2575 0.2484 0.2521 -0.0251 -0.0006 -0.0193 106 THR B CG2 
1661 N  N   . ILE B 139 ? 0.1722 0.2345 0.1636 -0.0094 0.0262  0.0246  107 ILE B N   
1662 C  CA  . ILE B 139 ? 0.1642 0.2459 0.1658 -0.0186 0.0005  0.0317  107 ILE B CA  
1663 C  C   . ILE B 139 ? 0.1511 0.2542 0.1412 -0.0161 -0.0060 0.0390  107 ILE B C   
1664 O  O   . ILE B 139 ? 0.1879 0.2835 0.1553 -0.0195 -0.0606 0.0492  107 ILE B O   
1665 C  CB  . ILE B 139 ? 0.1971 0.2668 0.1839 -0.0091 0.0237  0.0137  107 ILE B CB  
1666 C  CG1 . ILE B 139 ? 0.2356 0.3161 0.2221 -0.0101 -0.0070 0.0193  107 ILE B CG1 
1667 C  CG2 . ILE B 139 ? 0.2170 0.2760 0.1800 -0.0042 -0.0030 0.0144  107 ILE B CG2 
1668 C  CD1 . ILE B 139 ? 0.2852 0.3372 0.2623 -0.0093 -0.0301 0.0270  107 ILE B CD1 
1669 N  N   . ALA B 140 ? 0.2006 0.2428 0.1461 -0.0189 0.0202  0.0294  108 ALA B N   
1670 C  CA  . ALA B 140 ? 0.2104 0.2307 0.1655 0.0061  0.0337  0.0150  108 ALA B CA  
1671 C  C   . ALA B 140 ? 0.1799 0.2471 0.1575 -0.0148 0.0145  0.0050  108 ALA B C   
1672 O  O   . ALA B 140 ? 0.1950 0.2774 0.1535 -0.0132 -0.0212 0.0130  108 ALA B O   
1673 C  CB  . ALA B 140 ? 0.2444 0.2437 0.1817 0.0020  0.0348  -0.0050 108 ALA B CB  
1674 N  N   . ALA B 141 ? 0.1990 0.2135 0.1486 -0.0320 0.0140  0.0114  109 ALA B N   
1675 C  CA  . ALA B 141 ? 0.1998 0.1995 0.1582 -0.0556 0.0218  -0.0150 109 ALA B CA  
1676 C  C   . ALA B 141 ? 0.1946 0.1960 0.1500 -0.0463 -0.0253 0.0059  109 ALA B C   
1677 O  O   . ALA B 141 ? 0.2073 0.2327 0.1781 -0.0712 -0.0198 0.0240  109 ALA B O   
1678 C  CB  . ALA B 141 ? 0.2000 0.2047 0.2131 -0.0136 0.0100  -0.0190 109 ALA B CB  
1679 N  N   . LEU B 142 ? 0.1856 0.1872 0.1583 -0.0353 0.0154  0.0158  110 LEU B N   
1680 C  CA  . LEU B 142 ? 0.1775 0.1773 0.1625 -0.0002 0.0170  0.0287  110 LEU B CA  
1681 C  C   . LEU B 142 ? 0.1672 0.1880 0.1636 -0.0049 0.0233  0.0238  110 LEU B C   
1682 O  O   . LEU B 142 ? 0.1869 0.2274 0.1749 -0.0021 -0.0079 -0.0029 110 LEU B O   
1683 C  CB  . LEU B 142 ? 0.1596 0.1775 0.1983 -0.0036 -0.0335 0.0426  110 LEU B CB  
1684 C  CG  . LEU B 142 ? 0.2137 0.1701 0.1873 -0.0086 -0.0308 0.0441  110 LEU B CG  
1685 C  CD1 . LEU B 142 ? 0.2457 0.2134 0.1840 -0.0232 -0.0146 0.0279  110 LEU B CD1 
1686 C  CD2 . LEU B 142 ? 0.2553 0.1716 0.2288 0.0313  -0.0242 0.0503  110 LEU B CD2 
1687 N  N   . LEU B 143 ? 0.1619 0.1787 0.1615 -0.0134 0.0239  0.0079  111 LEU B N   
1688 C  CA  . LEU B 143 ? 0.1704 0.1816 0.1394 0.0183  0.0205  -0.0072 111 LEU B CA  
1689 C  C   . LEU B 143 ? 0.1721 0.1676 0.1319 0.0115  0.0094  0.0033  111 LEU B C   
1690 O  O   . LEU B 143 ? 0.1806 0.1619 0.1623 -0.0005 0.0009  -0.0132 111 LEU B O   
1691 C  CB  . LEU B 143 ? 0.1647 0.1935 0.1419 0.0113  0.0033  0.0138  111 LEU B CB  
1692 C  CG  . LEU B 143 ? 0.1766 0.1947 0.1622 -0.0096 -0.0075 0.0213  111 LEU B CG  
1693 C  CD1 . LEU B 143 ? 0.1771 0.2116 0.1934 0.0094  -0.0098 0.0292  111 LEU B CD1 
1694 C  CD2 . LEU B 143 ? 0.1658 0.1809 0.1588 -0.0175 -0.0039 -0.0151 111 LEU B CD2 
1695 N  N   . SER B 144 ? 0.1591 0.1976 0.1504 0.0045  0.0099  0.0111  112 SER B N   
1696 C  CA  . SER B 144 ? 0.1508 0.1912 0.1583 0.0250  0.0261  0.0067  112 SER B CA  
1697 C  C   . SER B 144 ? 0.1511 0.1918 0.1717 0.0019  0.0225  -0.0011 112 SER B C   
1698 O  O   . SER B 144 ? 0.1739 0.1753 0.1949 0.0033  0.0099  -0.0167 112 SER B O   
1699 C  CB  . SER B 144 ? 0.2123 0.2036 0.1822 0.0439  0.0036  -0.0033 112 SER B CB  
1700 O  OG  . SER B 144 ? 0.2435 0.2115 0.1926 0.0385  0.0151  -0.0135 112 SER B OG  
1701 N  N   . PRO B 145 ? 0.1832 0.1760 0.1961 -0.0256 -0.0036 -0.0118 113 PRO B N   
1702 C  CA  . PRO B 145 ? 0.1536 0.1936 0.2083 -0.0117 0.0092  -0.0253 113 PRO B CA  
1703 C  C   . PRO B 145 ? 0.1655 0.1794 0.1775 0.0030  0.0306  -0.0017 113 PRO B C   
1704 O  O   . PRO B 145 ? 0.2293 0.1702 0.2096 0.0196  0.0367  -0.0254 113 PRO B O   
1705 C  CB  . PRO B 145 ? 0.1618 0.2159 0.2328 -0.0220 0.0075  -0.0360 113 PRO B CB  
1706 C  CG  . PRO B 145 ? 0.1612 0.2316 0.2433 -0.0171 0.0084  -0.0373 113 PRO B CG  
1707 C  CD  . PRO B 145 ? 0.1597 0.2083 0.2332 -0.0319 0.0041  -0.0129 113 PRO B CD  
1708 N  N   . TYR B 146 ? 0.1581 0.1890 0.1778 -0.0063 0.0099  -0.0054 114 TYR B N   
1709 C  CA  . TYR B 146 ? 0.1854 0.1995 0.1617 -0.0055 0.0368  -0.0092 114 TYR B CA  
1710 C  C   . TYR B 146 ? 0.1737 0.2134 0.1556 0.0119  -0.0135 -0.0220 114 TYR B C   
1711 O  O   . TYR B 146 ? 0.1984 0.2666 0.1447 0.0070  0.0113  -0.0297 114 TYR B O   
1712 C  CB  . TYR B 146 ? 0.2024 0.2017 0.1873 0.0085  0.0734  -0.0029 114 TYR B CB  
1713 C  CG  . TYR B 146 ? 0.2162 0.2533 0.1622 -0.0022 0.0366  0.0018  114 TYR B CG  
1714 C  CD1 . TYR B 146 ? 0.2453 0.3434 0.2262 0.0154  0.0700  -0.0265 114 TYR B CD1 
1715 C  CD2 . TYR B 146 ? 0.2113 0.2155 0.1754 0.0204  0.0562  0.0085  114 TYR B CD2 
1716 C  CE1 . TYR B 146 ? 0.2719 0.3924 0.2548 0.0456  0.0971  -0.0343 114 TYR B CE1 
1717 C  CE2 . TYR B 146 ? 0.2357 0.2800 0.2053 0.0287  0.0954  0.0145  114 TYR B CE2 
1718 C  CZ  . TYR B 146 ? 0.2717 0.3674 0.2709 0.1012  0.0956  -0.0343 114 TYR B CZ  
1719 O  OH  . TYR B 146 ? 0.3041 0.4623 0.3337 0.1136  0.0798  -0.0038 114 TYR B OH  
1720 N  N   . SER B 147 ? 0.1695 0.1977 0.1873 0.0063  0.0231  -0.0158 115 SER B N   
1721 C  CA  A SER B 147 ? 0.1546 0.1907 0.1784 0.0137  0.0173  -0.0254 115 SER B CA  
1722 C  CA  C SER B 147 ? 0.1944 0.2071 0.2157 0.0101  0.0182  -0.0032 115 SER B CA  
1723 C  C   . SER B 147 ? 0.1480 0.2192 0.1868 -0.0107 0.0215  -0.0279 115 SER B C   
1724 O  O   . SER B 147 ? 0.1558 0.2640 0.1945 -0.0084 -0.0101 -0.0266 115 SER B O   
1725 C  CB  A SER B 147 ? 0.1549 0.1598 0.1516 0.0385  -0.0055 -0.0578 115 SER B CB  
1726 C  CB  C SER B 147 ? 0.2780 0.2140 0.2646 0.0175  -0.0015 0.0015  115 SER B CB  
1727 O  OG  A SER B 147 ? 0.1794 0.1502 0.1357 0.0710  -0.0201 -0.0481 115 SER B OG  
1728 O  OG  C SER B 147 ? 0.3634 0.2295 0.3035 0.0271  0.0064  0.0279  115 SER B OG  
1729 N  N   . TYR B 148 ? 0.1759 0.2263 0.1631 -0.0060 0.0206  -0.0300 116 TYR B N   
1730 C  CA  . TYR B 148 ? 0.1634 0.2286 0.1746 -0.0014 0.0112  -0.0021 116 TYR B CA  
1731 C  C   . TYR B 148 ? 0.1463 0.2324 0.1506 -0.0108 -0.0017 -0.0166 116 TYR B C   
1732 O  O   . TYR B 148 ? 0.1636 0.2412 0.1361 -0.0163 -0.0109 -0.0117 116 TYR B O   
1733 C  CB  . TYR B 148 ? 0.2149 0.2334 0.1741 0.0274  -0.0005 0.0080  116 TYR B CB  
1734 C  CG  . TYR B 148 ? 0.2639 0.2288 0.1930 0.0405  -0.0256 0.0011  116 TYR B CG  
1735 C  CD1 . TYR B 148 ? 0.2742 0.2304 0.2231 0.0375  -0.0471 -0.0068 116 TYR B CD1 
1736 C  CD2 . TYR B 148 ? 0.3667 0.2507 0.2200 0.0556  -0.0321 -0.0009 116 TYR B CD2 
1737 C  CE1 . TYR B 148 ? 0.3325 0.2463 0.2595 0.0176  -0.0721 -0.0205 116 TYR B CE1 
1738 C  CE2 . TYR B 148 ? 0.4251 0.2640 0.2479 0.0389  -0.0851 -0.0132 116 TYR B CE2 
1739 C  CZ  . TYR B 148 ? 0.4138 0.2346 0.2707 0.0141  -0.0897 -0.0243 116 TYR B CZ  
1740 O  OH  . TYR B 148 ? 0.5354 0.2455 0.3185 0.0340  -0.0994 -0.0397 116 TYR B OH  
1741 N  N   . SER B 149 ? 0.1762 0.2329 0.1656 -0.0029 -0.0205 -0.0103 117 SER B N   
1742 C  CA  A SER B 149 ? 0.1597 0.2366 0.1527 -0.0085 -0.0162 -0.0073 117 SER B CA  
1743 C  CA  B SER B 149 ? 0.1817 0.2307 0.1488 -0.0163 -0.0120 -0.0023 117 SER B CA  
1744 C  CA  C SER B 149 ? 0.2050 0.2456 0.1698 -0.0131 -0.0183 -0.0077 117 SER B CA  
1745 C  C   . SER B 149 ? 0.1672 0.2437 0.1509 -0.0168 -0.0262 -0.0066 117 SER B C   
1746 O  O   . SER B 149 ? 0.1812 0.2925 0.1560 -0.0395 -0.0293 0.0130  117 SER B O   
1747 C  CB  A SER B 149 ? 0.1317 0.2472 0.1537 0.0047  0.0033  0.0026  117 SER B CB  
1748 C  CB  B SER B 149 ? 0.1934 0.2276 0.1439 -0.0238 0.0135  0.0206  117 SER B CB  
1749 C  CB  C SER B 149 ? 0.2793 0.2764 0.2079 -0.0053 -0.0121 -0.0033 117 SER B CB  
1750 O  OG  A SER B 149 ? 0.0860 0.2585 0.1459 0.0197  0.0057  0.0214  117 SER B OG  
1751 O  OG  B SER B 149 ? 0.1938 0.2212 0.1299 -0.0380 0.0255  0.0482  117 SER B OG  
1752 O  OG  C SER B 149 ? 0.3351 0.2916 0.2243 -0.0083 -0.0213 -0.0029 117 SER B OG  
1753 N  N   . THR B 150 ? 0.1540 0.2166 0.1524 -0.0153 0.0122  -0.0005 118 THR B N   
1754 C  CA  . THR B 150 ? 0.1567 0.2122 0.1713 -0.0001 0.0268  0.0044  118 THR B CA  
1755 C  C   . THR B 150 ? 0.1661 0.2364 0.1609 -0.0136 0.0147  0.0014  118 THR B C   
1756 O  O   . THR B 150 ? 0.1699 0.2771 0.1673 0.0015  -0.0107 0.0087  118 THR B O   
1757 C  CB  . THR B 150 ? 0.1908 0.2065 0.1715 -0.0030 -0.0200 -0.0092 118 THR B CB  
1758 O  OG1 . THR B 150 ? 0.2132 0.2199 0.2144 -0.0158 -0.0134 0.0006  118 THR B OG1 
1759 C  CG2 . THR B 150 ? 0.2141 0.2421 0.1833 -0.0260 -0.0360 -0.0431 118 THR B CG2 
1760 N  N   . THR B 151 ? 0.1513 0.2204 0.1847 0.0037  0.0097  -0.0010 119 THR B N   
1761 C  CA  . THR B 151 ? 0.1768 0.2047 0.1736 0.0133  0.0347  0.0350  119 THR B CA  
1762 C  C   . THR B 151 ? 0.1678 0.2251 0.1565 0.0140  0.0150  0.0295  119 THR B C   
1763 O  O   . THR B 151 ? 0.1748 0.2848 0.1812 -0.0102 -0.0011 0.0625  119 THR B O   
1764 C  CB  . THR B 151 ? 0.2070 0.2054 0.1958 -0.0070 -0.0169 0.0272  119 THR B CB  
1765 O  OG1 . THR B 151 ? 0.2163 0.2180 0.2263 0.0153  -0.0076 0.0254  119 THR B OG1 
1766 C  CG2 . THR B 151 ? 0.2627 0.2313 0.1973 -0.0127 -0.0283 0.0176  119 THR B CG2 
1767 N  N   . ALA B 152 ? 0.1698 0.1982 0.1482 0.0005  0.0338  0.0047  120 ALA B N   
1768 C  CA  . ALA B 152 ? 0.1886 0.2007 0.1992 0.0095  0.0325  0.0102  120 ALA B CA  
1769 C  C   . ALA B 152 ? 0.1868 0.2172 0.1905 0.0222  0.0166  0.0121  120 ALA B C   
1770 O  O   . ALA B 152 ? 0.2039 0.2374 0.1963 0.0364  0.0280  0.0539  120 ALA B O   
1771 C  CB  . ALA B 152 ? 0.2294 0.2073 0.2233 -0.0250 0.0431  0.0095  120 ALA B CB  
1772 N  N   . VAL B 153 ? 0.1727 0.2411 0.1987 0.0102  0.0178  0.0012  121 VAL B N   
1773 C  CA  . VAL B 153 ? 0.2035 0.2540 0.2190 0.0349  0.0586  0.0279  121 VAL B CA  
1774 C  C   . VAL B 153 ? 0.2482 0.2860 0.2147 0.0485  0.1066  0.0617  121 VAL B C   
1775 O  O   . VAL B 153 ? 0.2688 0.3030 0.2511 0.0474  0.0741  0.0910  121 VAL B O   
1776 C  CB  . VAL B 153 ? 0.2813 0.2517 0.2512 0.0390  0.0554  -0.0001 121 VAL B CB  
1777 C  CG1 . VAL B 153 ? 0.3014 0.3013 0.2781 0.0857  0.0544  -0.0225 121 VAL B CG1 
1778 C  CG2 . VAL B 153 ? 0.3545 0.2369 0.2834 0.0042  -0.0158 0.0016  121 VAL B CG2 
1779 N  N   . VAL B 154 ? 0.2346 0.2967 0.2329 0.0349  0.0853  0.0310  122 VAL B N   
1780 C  CA  . VAL B 154 ? 0.2411 0.3256 0.2511 0.0308  0.0896  0.0641  122 VAL B CA  
1781 C  C   . VAL B 154 ? 0.2475 0.3511 0.2502 0.0463  0.0830  0.0635  122 VAL B C   
1782 O  O   . VAL B 154 ? 0.2689 0.3412 0.2919 0.0906  0.0475  0.0553  122 VAL B O   
1783 C  CB  . VAL B 154 ? 0.2495 0.3083 0.2685 0.0135  0.0767  0.0835  122 VAL B CB  
1784 C  CG1 . VAL B 154 ? 0.2944 0.2805 0.3126 0.0117  0.0945  0.0762  122 VAL B CG1 
1785 C  CG2 . VAL B 154 ? 0.2630 0.3177 0.2730 0.0292  0.0749  0.0839  122 VAL B CG2 
1786 N  N   . THR B 155 ? 0.2843 0.3767 0.2621 0.0310  0.0851  0.0712  123 THR B N   
1787 C  CA  . THR B 155 ? 0.3331 0.4358 0.3279 0.0088  0.1161  0.0769  123 THR B CA  
1788 C  C   . THR B 155 ? 0.3917 0.4627 0.3762 0.0235  0.1645  0.0706  123 THR B C   
1789 O  O   . THR B 155 ? 0.3335 0.4148 0.3286 0.0748  0.1609  0.0283  123 THR B O   
1790 C  CB  . THR B 155 ? 0.4415 0.4631 0.3629 -0.0114 0.0720  0.1015  123 THR B CB  
1791 O  OG1 . THR B 155 ? 0.4897 0.4923 0.4008 0.0089  0.0208  0.0778  123 THR B OG1 
1792 C  CG2 . THR B 155 ? 0.4421 0.4334 0.3544 -0.0724 0.0991  0.1591  123 THR B CG2 
1793 N  N   . ASN B 156 ? 0.5257 0.5557 0.4960 0.0063  0.1833  0.0788  124 ASN B N   
1794 C  CA  . ASN B 156 ? 0.6648 0.6662 0.6335 -0.0202 0.1688  0.0746  124 ASN B CA  
1795 C  C   . ASN B 156 ? 0.7873 0.7592 0.7302 -0.0219 0.1555  0.0892  124 ASN B C   
1796 O  O   . ASN B 156 ? 0.7913 0.7608 0.7385 -0.0323 0.1751  0.0886  124 ASN B O   
1797 C  CB  . ASN B 156 ? 0.6761 0.6690 0.6728 -0.0380 0.1566  0.0481  124 ASN B CB  
1798 C  CG  . ASN B 156 ? 0.6732 0.6647 0.7012 -0.0498 0.1421  0.0224  124 ASN B CG  
1799 O  OD1 . ASN B 156 ? 0.6537 0.6604 0.7056 -0.0602 0.1456  0.0035  124 ASN B OD1 
1800 N  ND2 . ASN B 156 ? 0.6884 0.6677 0.7135 -0.0476 0.1259  0.0242  124 ASN B ND2 
1801 N  N   . PRO B 157 ? 0.8960 0.8354 0.8041 -0.0091 0.1192  0.1065  125 PRO B N   
1802 C  CA  . PRO B 157 ? 0.9516 0.8813 0.8460 -0.0035 0.0980  0.1157  125 PRO B CA  
1803 C  C   . PRO B 157 ? 0.9799 0.9122 0.8672 0.0039  0.0895  0.1248  125 PRO B C   
1804 O  O   . PRO B 157 ? 0.9928 0.9191 0.8767 0.0108  0.0918  0.1312  125 PRO B O   
1805 C  CB  . PRO B 157 ? 0.9630 0.8844 0.8526 -0.0025 0.0954  0.1180  125 PRO B CB  
1806 C  CG  . PRO B 157 ? 0.9582 0.8782 0.8481 -0.0029 0.0987  0.1178  125 PRO B CG  
1807 C  CD  . PRO B 157 ? 0.9381 0.8622 0.8310 -0.0058 0.1062  0.1140  125 PRO B CD  
1826 NA NA  . NA  D .   ? 0.3514 0.4782 0.5057 0.0700  0.0084  -0.0229 202 NA  A NA  
1845 O  O   . HOH F .   ? 0.6069 0.7474 0.6789 -0.0654 0.1000  0.0749  301 HOH A O   
1846 O  O   . HOH F .   ? 0.2855 0.4379 0.7569 0.0872  0.0127  -0.0933 302 HOH A O   
1847 O  O   . HOH F .   ? 0.2688 0.3422 0.2810 -0.0363 -0.0291 0.1041  303 HOH A O   
1848 O  O   . HOH F .   ? 0.3022 0.3098 0.3031 0.0079  -0.0488 -0.0628 304 HOH A O   
1849 O  O   . HOH F .   ? 0.2227 0.7763 0.4861 0.0021  0.0378  0.1824  305 HOH A O   
1850 O  O   . HOH F .   ? 0.3127 0.6690 0.7770 0.0220  -0.0268 0.1450  306 HOH A O   
1851 O  O   . HOH F .   ? 0.8937 0.4120 0.4167 -0.0538 0.2077  0.0314  307 HOH A O   
1852 O  O   . HOH F .   ? 0.7050 0.4464 0.5671 0.0127  -0.0852 -0.0672 308 HOH A O   
1853 O  O   . HOH F .   ? 0.7396 0.5980 0.5740 0.0305  -0.0855 -0.0944 309 HOH A O   
1854 O  O   . HOH F .   ? 0.2660 0.6464 0.7915 0.0372  0.0073  -0.2769 310 HOH A O   
1855 O  O   . HOH F .   ? 0.3515 0.4660 0.8100 0.0091  0.0074  -0.2529 311 HOH A O   
1856 O  O   . HOH F .   ? 0.2732 0.2895 0.3180 0.0488  -0.0050 0.0293  312 HOH A O   
1857 O  O   . HOH F .   ? 0.3924 0.4454 0.7201 -0.0260 -0.1787 -0.2313 313 HOH A O   
1858 O  O   . HOH F .   ? 0.3138 0.3666 0.3298 -0.0207 -0.0845 -0.0520 314 HOH A O   
1859 O  O   . HOH F .   ? 0.6481 0.9510 0.5303 0.0214  -0.0723 0.0673  315 HOH A O   
1860 O  O   . HOH F .   ? 0.1857 0.2125 0.1843 0.0305  0.0071  0.0052  316 HOH A O   
1861 O  O   . HOH F .   ? 0.4876 0.5591 0.7509 -0.0991 0.1443  -0.0933 317 HOH A O   
1862 O  O   . HOH F .   ? 0.3724 0.4368 0.2445 0.0121  -0.0109 0.0082  318 HOH A O   
1863 O  O   . HOH F .   ? 0.2937 0.3487 0.1967 0.0027  0.0354  0.0097  319 HOH A O   
1864 O  O   . HOH F .   ? 0.3522 0.3662 0.3688 0.0403  0.0617  -0.0052 320 HOH A O   
1865 O  O   . HOH F .   ? 0.5339 0.5614 0.6068 -0.0519 0.3373  -0.0494 321 HOH A O   
1866 O  O   . HOH F .   ? 0.3295 0.4550 0.5996 0.0884  -0.0416 0.0233  322 HOH A O   
1867 O  O   . HOH F .   ? 0.3360 0.3274 0.6563 -0.0633 0.1330  -0.0825 323 HOH A O   
1868 O  O   . HOH F .   ? 0.5688 0.7622 0.6053 0.0338  0.0793  -0.0812 324 HOH A O   
1869 O  O   . HOH F .   ? 0.3455 0.2462 0.2505 -0.0305 0.0793  -0.0759 325 HOH A O   
1870 O  O   . HOH F .   ? 0.6797 0.3655 0.5891 -0.0434 0.2298  0.1218  326 HOH A O   
1871 O  O   . HOH F .   ? 0.3228 0.1888 0.4838 0.0246  0.0919  -0.0173 327 HOH A O   
1872 O  O   . HOH F .   ? 0.2735 0.2455 0.2083 -0.0546 -0.0317 0.0623  328 HOH A O   
1873 O  O   . HOH F .   ? 0.2265 0.1900 0.1859 0.0224  0.0393  -0.0022 329 HOH A O   
1874 O  O   . HOH F .   ? 0.3682 0.5780 0.4431 0.1094  0.0503  -0.2018 330 HOH A O   
1875 O  O   . HOH F .   ? 0.7446 0.3044 0.4857 0.1488  0.2331  0.0659  331 HOH A O   
1876 O  O   . HOH F .   ? 0.3183 0.3551 0.3418 -0.0313 0.0198  -0.0768 332 HOH A O   
1877 O  O   . HOH F .   ? 0.3310 0.6544 0.5143 0.1013  -0.0412 0.0473  333 HOH A O   
1878 O  O   . HOH F .   ? 0.3430 0.3283 0.3905 0.0083  0.0460  -0.0202 334 HOH A O   
1879 O  O   . HOH F .   ? 0.8007 0.3662 0.3020 0.1171  0.0904  -0.0194 335 HOH A O   
1880 O  O   . HOH F .   ? 0.3252 0.3538 0.3410 0.1207  -0.0289 -0.0610 336 HOH A O   
1881 O  O   . HOH F .   ? 0.2827 0.2477 0.2726 -0.0038 0.0697  -0.0402 337 HOH A O   
1882 O  O   . HOH F .   ? 0.6217 0.3425 0.8850 -0.1433 0.0722  -0.0577 338 HOH A O   
1883 O  O   . HOH F .   ? 0.6583 0.7399 0.6434 0.3841  -0.0886 -0.2106 339 HOH A O   
1884 O  O   . HOH F .   ? 0.4672 0.4580 0.7009 -0.0178 -0.1120 -0.0493 340 HOH A O   
1885 O  O   . HOH F .   ? 0.1773 0.2126 0.2107 0.0145  0.0056  0.0073  341 HOH A O   
1886 O  O   . HOH F .   ? 0.3958 0.6989 0.6955 -0.1879 -0.0176 0.1338  342 HOH A O   
1887 O  O   . HOH F .   ? 0.3436 0.4724 0.4602 -0.0998 -0.0437 0.0271  343 HOH A O   
1888 O  O   . HOH F .   ? 0.2185 0.2531 0.1878 0.0247  0.0233  0.0051  344 HOH A O   
1889 O  O   . HOH F .   ? 0.5868 0.7657 0.7255 0.3288  0.0185  0.2206  345 HOH A O   
1890 O  O   . HOH F .   ? 0.8130 0.6870 0.6920 -0.1751 0.0129  -0.0705 346 HOH A O   
1891 O  O   . HOH F .   ? 0.5576 0.5463 0.6709 0.1842  0.2146  0.0091  347 HOH A O   
1892 O  O   . HOH F .   ? 0.3022 0.2570 0.2843 0.0238  -0.0427 -0.0108 348 HOH A O   
1893 O  O   . HOH F .   ? 0.3670 0.3571 0.3045 0.0628  0.0115  -0.0845 349 HOH A O   
1894 O  O   . HOH F .   ? 0.2256 0.3257 0.3316 -0.0621 0.0063  -0.0320 350 HOH A O   
1895 O  O   . HOH F .   ? 0.6340 0.6606 0.5753 -0.0691 0.0615  0.1449  351 HOH A O   
1896 O  O   . HOH F .   ? 0.9089 0.4038 0.4033 -0.2265 0.1241  -0.0723 352 HOH A O   
1897 O  O   . HOH F .   ? 0.2881 0.3843 0.3072 -0.0378 0.0382  -0.0626 353 HOH A O   
1898 O  O   . HOH F .   ? 0.7350 1.1031 0.6806 0.0632  0.0454  -0.0042 354 HOH A O   
1899 O  O   . HOH F .   ? 0.3203 0.5771 0.3875 -0.0503 0.0134  -0.1457 355 HOH A O   
1900 O  O   . HOH F .   ? 0.6633 0.6245 0.8041 -0.0979 0.0717  -0.0356 356 HOH A O   
1901 O  O   . HOH F .   ? 0.2663 0.3051 0.3557 -0.0052 -0.0042 -0.1267 357 HOH A O   
1902 O  O   . HOH F .   ? 0.2746 0.4688 0.3045 0.0168  -0.0798 0.0240  358 HOH A O   
1903 O  O   . HOH F .   ? 0.4657 0.4274 0.2970 0.1037  0.1192  0.0015  359 HOH A O   
1904 O  O   . HOH F .   ? 0.3039 0.2804 0.3614 -0.0643 -0.0715 -0.0057 360 HOH A O   
1905 O  O   . HOH F .   ? 0.6051 0.4084 0.8771 -0.1663 0.3908  -0.2031 361 HOH A O   
1906 O  O   . HOH F .   ? 0.6984 0.7945 0.8274 -0.0517 0.0415  0.0506  362 HOH A O   
1907 O  O   . HOH F .   ? 0.4199 0.7928 0.4248 -0.0635 0.1084  -0.0531 363 HOH A O   
1908 O  O   . HOH F .   ? 0.3763 0.3977 0.4400 -0.0505 -0.0881 0.0323  364 HOH A O   
1909 O  O   . HOH F .   ? 0.4632 0.5535 0.5669 0.1146  0.2529  0.2001  365 HOH A O   
1910 O  O   . HOH F .   ? 0.5638 0.5331 0.6196 -0.1425 -0.0839 -0.1501 366 HOH A O   
1911 O  O   . HOH F .   ? 0.2844 0.6475 0.4225 -0.0638 -0.0938 0.1967  367 HOH A O   
1912 O  O   . HOH F .   ? 0.4370 0.4039 0.4296 -0.0303 0.1045  -0.0457 368 HOH A O   
1913 O  O   . HOH F .   ? 0.3721 0.8540 0.4659 0.0857  -0.0276 -0.2366 369 HOH A O   
1914 O  O   . HOH F .   ? 0.6465 0.8493 0.7115 0.2169  0.1638  -0.0462 370 HOH A O   
1915 O  O   . HOH F .   ? 0.5320 0.8763 0.5655 -0.2770 -0.0881 -0.2010 371 HOH A O   
1916 O  O   . HOH F .   ? 0.5094 0.7101 0.6328 0.0825  -0.1106 -0.0807 372 HOH A O   
1917 O  O   . HOH F .   ? 0.4088 0.5365 0.5047 -0.1041 0.0543  -0.0719 373 HOH A O   
1918 O  O   . HOH F .   ? 0.4418 0.8498 0.5516 0.0231  -0.1655 0.0429  374 HOH A O   
1919 O  O   . HOH F .   ? 0.5045 0.3269 0.6073 0.0393  0.0968  -0.1033 375 HOH A O   
1920 O  O   . HOH F .   ? 0.4860 0.5114 0.7832 0.1342  0.2915  0.1297  376 HOH A O   
1921 O  O   . HOH F .   ? 0.7652 0.6447 0.5439 -0.0236 0.0408  -0.1038 377 HOH A O   
1922 O  O   . HOH F .   ? 0.6653 0.5017 0.5210 0.1268  0.0478  0.0600  378 HOH A O   
1923 O  O   . HOH F .   ? 0.7223 0.6219 0.4502 0.1049  -0.1969 -0.0864 379 HOH A O   
1924 O  O   . HOH F .   ? 0.7242 0.6293 0.6273 0.2706  0.0386  0.1497  380 HOH A O   
1925 O  O   . HOH F .   ? 0.5752 0.4596 0.3103 0.1674  0.0042  -0.1267 381 HOH A O   
1926 O  O   . HOH F .   ? 0.4552 0.6695 0.7204 0.0992  0.0730  -0.1740 382 HOH A O   
1927 O  O   . HOH F .   ? 0.5481 0.4572 0.5984 -0.0210 0.1459  -0.0926 383 HOH A O   
1928 O  O   . HOH F .   ? 0.5752 0.3948 0.3516 -0.1305 -0.0890 -0.0894 384 HOH A O   
1929 O  O   . HOH F .   ? 0.9730 0.3857 0.4527 0.0305  -0.2835 0.0177  385 HOH A O   
1930 O  O   . HOH F .   ? 0.3466 0.5035 0.3588 -0.0633 0.0382  -0.0269 386 HOH A O   
1931 O  O   . HOH F .   ? 0.5875 0.7788 0.6882 -0.0671 0.0427  0.1101  387 HOH A O   
1932 O  O   . HOH F .   ? 0.4214 0.9884 0.4168 0.0116  0.0339  0.0800  388 HOH A O   
1933 O  O   . HOH F .   ? 0.3236 0.8075 0.6954 0.1429  0.0379  0.3016  389 HOH A O   
1934 O  O   . HOH F .   ? 0.3446 0.4580 0.8762 -0.0575 -0.0845 0.0576  390 HOH A O   
1935 O  O   . HOH F .   ? 0.6968 0.5191 0.6644 -0.0945 0.1779  0.0298  391 HOH A O   
1936 O  O   . HOH F .   ? 0.7163 0.4660 0.5667 -0.1522 0.1341  -0.1481 392 HOH A O   
1937 O  O   . HOH F .   ? 0.4967 0.3518 0.5269 -0.0489 0.0755  -0.0091 393 HOH A O   
1938 O  O   . HOH F .   ? 0.6475 0.7937 0.7047 -0.0592 -0.0064 0.2210  394 HOH A O   
1939 O  O   . HOH F .   ? 0.6407 0.4880 0.5682 -0.1855 0.0882  0.0341  395 HOH A O   
1940 O  O   . HOH F .   ? 0.4078 0.6841 0.7083 -0.0614 0.1046  -0.0651 396 HOH A O   
1941 O  O   . HOH F .   ? 0.6848 0.6317 0.5584 -0.2107 -0.1416 0.0370  397 HOH A O   
1942 O  O   . HOH F .   ? 0.3605 0.8825 0.6478 0.0297  0.0252  0.3161  398 HOH A O   
1943 O  O   . HOH F .   ? 0.4109 0.6956 0.6743 -0.1606 -0.0957 -0.0044 399 HOH A O   
1944 O  O   . HOH F .   ? 0.2749 0.6462 0.6962 -0.0708 0.0880  -0.2934 400 HOH A O   
1945 O  O   . HOH F .   ? 0.5184 0.7489 0.7800 0.0816  -0.0284 0.0662  401 HOH A O   
1946 O  O   . HOH F .   ? 0.4305 0.5751 0.7188 0.1190  0.1211  0.0170  402 HOH A O   
1947 O  O   . HOH G .   ? 0.4028 0.6035 0.4963 -0.0722 -0.1612 0.0881  301 HOH B O   
1948 O  O   . HOH G .   ? 0.6825 0.8542 0.6962 -0.0742 -0.0327 -0.0100 302 HOH B O   
1949 O  O   . HOH G .   ? 0.6514 0.4768 0.8109 0.0869  0.0784  -0.2408 303 HOH B O   
1950 O  O   . HOH G .   ? 0.4999 0.4631 0.6554 -0.1259 0.0120  0.1272  304 HOH B O   
1951 O  O   . HOH G .   ? 0.4258 0.4217 0.3095 0.0060  0.0016  0.0725  305 HOH B O   
1952 O  O   . HOH G .   ? 0.3691 0.7797 0.5122 -0.0895 -0.0516 0.0962  306 HOH B O   
1953 O  O   . HOH G .   ? 0.6415 0.6643 0.4667 -0.2188 0.2402  -0.0810 307 HOH B O   
1954 O  O   . HOH G .   ? 0.3047 0.3477 0.3948 -0.0008 -0.0434 0.0707  308 HOH B O   
1955 O  O   . HOH G .   ? 0.5745 0.5474 0.6188 -0.0914 0.1195  -0.1223 309 HOH B O   
1956 O  O   . HOH G .   ? 0.2540 0.3284 0.2192 -0.0055 0.0131  -0.1101 310 HOH B O   
1957 O  O   . HOH G .   ? 0.2618 0.1883 0.2900 -0.0289 0.0063  -0.0169 311 HOH B O   
1958 O  O   . HOH G .   ? 0.6968 0.4629 0.5332 0.0686  0.1193  -0.1055 312 HOH B O   
1959 O  O   . HOH G .   ? 0.5780 0.6478 0.3695 0.2597  -0.1296 -0.2228 313 HOH B O   
1960 O  O   . HOH G .   ? 0.3375 0.3930 0.3867 0.0668  -0.0316 0.0392  314 HOH B O   
1961 O  O   . HOH G .   ? 0.4344 0.4785 0.3280 0.0754  -0.0761 -0.0122 315 HOH B O   
1962 O  O   . HOH G .   ? 0.3291 0.4501 1.0707 0.1008  0.0663  0.0608  316 HOH B O   
1963 O  O   . HOH G .   ? 0.3449 0.2674 0.2847 0.0854  0.0955  0.0736  317 HOH B O   
1964 O  O   . HOH G .   ? 0.4355 0.6587 0.5555 0.1783  -0.0950 0.0762  318 HOH B O   
1965 O  O   . HOH G .   ? 0.6653 0.5397 0.4807 0.2298  0.1686  0.1584  319 HOH B O   
1966 O  O   . HOH G .   ? 0.6657 0.4644 0.9432 0.1254  0.0384  -0.0006 320 HOH B O   
1967 O  O   . HOH G .   ? 0.5598 0.4261 0.2481 0.2582  0.0996  0.1015  321 HOH B O   
1968 O  O   . HOH G .   ? 0.5072 0.4534 0.6864 0.0281  0.1435  0.1355  322 HOH B O   
1969 O  O   . HOH G .   ? 0.2005 0.2149 0.1684 -0.0265 0.0125  -0.0090 323 HOH B O   
1970 O  O   . HOH G .   ? 0.2598 0.7647 0.3989 -0.0678 -0.0151 0.0200  324 HOH B O   
1971 O  O   . HOH G .   ? 0.5325 0.4277 0.8574 -0.1836 -0.1293 0.0894  325 HOH B O   
1972 O  O   . HOH G .   ? 0.3412 0.3206 0.3449 -0.0431 0.0145  -0.0352 326 HOH B O   
1973 O  O   . HOH G .   ? 0.2404 0.2192 0.1970 0.0339  -0.0425 -0.0607 327 HOH B O   
1974 O  O   . HOH G .   ? 0.3776 0.3560 0.4555 -0.0595 0.0232  0.0557  328 HOH B O   
1975 O  O   . HOH G .   ? 0.3344 0.3278 0.3871 0.0563  0.0279  0.0695  329 HOH B O   
1976 O  O   . HOH G .   ? 0.2993 0.5899 0.3458 0.0569  -0.0092 0.1104  330 HOH B O   
1977 O  O   . HOH G .   ? 0.2787 0.2003 0.2202 -0.0327 0.0011  -0.0008 331 HOH B O   
1978 O  O   . HOH G .   ? 0.4557 0.3917 0.8422 -0.0832 0.2274  0.1067  332 HOH B O   
1979 O  O   . HOH G .   ? 0.3700 0.3921 0.3472 -0.0855 0.0430  0.0119  333 HOH B O   
1980 O  O   . HOH G .   ? 0.2303 0.2203 0.2712 -0.0076 0.0129  0.0088  334 HOH B O   
1981 O  O   . HOH G .   ? 0.3782 0.9310 0.5243 -0.0108 -0.0365 0.0836  335 HOH B O   
1982 O  O   . HOH G .   ? 0.3044 0.4764 0.5145 0.1102  0.0146  0.0252  336 HOH B O   
1983 O  O   . HOH G .   ? 0.4326 0.3606 0.2704 0.0186  0.0071  0.0789  337 HOH B O   
1984 O  O   . HOH G .   ? 0.7162 0.6179 0.3669 -0.0717 -0.0840 -0.0673 338 HOH B O   
1985 O  O   . HOH G .   ? 0.2511 0.2344 0.2374 0.0170  0.0413  0.0234  339 HOH B O   
1986 O  O   . HOH G .   ? 0.5818 0.6787 0.6387 0.2562  -0.0614 -0.0969 340 HOH B O   
1987 O  O   . HOH G .   ? 0.8305 0.5248 0.3612 0.1681  0.1785  0.0345  341 HOH B O   
1988 O  O   . HOH G .   ? 0.3900 0.2315 0.4028 -0.0104 0.1170  0.0083  342 HOH B O   
1989 O  O   . HOH G .   ? 0.2234 0.1903 0.1841 -0.0026 -0.0062 0.0214  343 HOH B O   
1990 O  O   . HOH G .   ? 0.4425 0.3693 0.2689 -0.0431 0.0310  0.0058  344 HOH B O   
1991 O  O   . HOH G .   ? 0.2838 0.3131 0.3280 0.0206  -0.0323 0.1323  345 HOH B O   
1992 O  O   . HOH G .   ? 0.2734 0.4624 0.6414 0.0800  -0.0575 0.0427  346 HOH B O   
1993 O  O   . HOH G .   ? 0.2428 0.2727 0.2063 -0.0074 0.0222  0.0138  347 HOH B O   
1994 O  O   . HOH G .   ? 0.3625 0.4145 0.4728 -0.0508 -0.0110 0.2431  348 HOH B O   
1995 O  O   . HOH G .   ? 0.2431 0.3342 0.2779 -0.0139 0.0299  0.0119  349 HOH B O   
1996 O  O   . HOH G .   ? 0.5728 0.3704 0.4591 0.1047  0.1554  0.1925  350 HOH B O   
1997 O  O   . HOH G .   ? 0.5941 0.6381 0.4207 -0.2287 0.1964  -0.1952 351 HOH B O   
1998 O  O   . HOH G .   ? 0.8373 0.4699 0.6789 0.1560  0.3732  0.2223  352 HOH B O   
1999 O  O   . HOH G .   ? 0.8753 0.5947 0.5495 0.0787  -0.1235 0.3082  353 HOH B O   
2000 O  O   . HOH G .   ? 0.7999 0.5129 0.2756 -0.2614 0.0172  -0.0166 354 HOH B O   
2001 O  O   . HOH G .   ? 0.8699 0.4730 0.4143 -0.2963 0.0481  -0.0363 355 HOH B O   
2002 O  O   . HOH G .   ? 0.3072 0.6126 0.2746 0.0054  -0.0546 -0.0632 356 HOH B O   
2003 O  O   . HOH G .   ? 0.5925 0.7078 0.5993 0.0196  0.2546  0.0459  357 HOH B O   
2004 O  O   . HOH G .   ? 0.6413 0.6683 0.4491 -0.1688 0.1465  0.1295  358 HOH B O   
2005 O  O   . HOH G .   ? 0.3391 0.2985 0.3327 -0.0478 -0.0097 0.0549  359 HOH B O   
2006 O  O   . HOH G .   ? 0.4579 0.3772 0.3180 0.0138  -0.0576 -0.1267 360 HOH B O   
2007 O  O   . HOH G .   ? 0.4190 0.4209 0.3157 0.0710  -0.0871 0.0181  361 HOH B O   
2008 O  O   . HOH G .   ? 0.2750 0.3659 0.2765 0.0286  0.0160  0.0346  362 HOH B O   
2009 O  O   . HOH G .   ? 0.2286 0.2588 0.2705 0.0412  -0.0221 0.0165  363 HOH B O   
2010 O  O   . HOH G .   ? 0.8121 0.5173 0.5363 0.1042  0.0315  -0.2296 364 HOH B O   
2011 O  O   . HOH G .   ? 0.6753 0.7905 0.4106 -0.0655 0.0588  0.0919  365 HOH B O   
2012 O  O   . HOH G .   ? 0.6117 0.3525 0.8056 0.0864  0.2329  0.1796  366 HOH B O   
2013 O  O   . HOH G .   ? 0.5437 0.3957 0.3621 -0.0415 0.0047  -0.1049 367 HOH B O   
2014 O  O   . HOH G .   ? 0.4945 0.5332 0.7736 -0.2828 -0.0468 0.0307  368 HOH B O   
2015 O  O   . HOH G .   ? 0.3826 0.5182 0.4904 -0.0777 -0.0968 0.2332  369 HOH B O   
2016 O  O   . HOH G .   ? 0.6727 0.7915 0.4581 0.2469  0.1549  -0.1247 370 HOH B O   
2017 O  O   . HOH G .   ? 0.2604 0.3378 0.3768 -0.0828 -0.0620 0.0959  371 HOH B O   
2018 O  O   . HOH G .   ? 0.5589 0.3900 0.3044 -0.0564 0.0900  0.0044  372 HOH B O   
2019 O  O   . HOH G .   ? 0.3138 0.4915 0.3637 0.0312  -0.0539 -0.0433 373 HOH B O   
2020 O  O   . HOH G .   ? 0.3368 0.4616 0.2220 -0.0299 -0.0645 0.0972  374 HOH B O   
2021 O  O   . HOH G .   ? 0.7870 0.7902 0.4676 0.2575  0.1406  -0.1350 375 HOH B O   
2022 O  O   . HOH G .   ? 0.5683 0.6648 0.6739 -0.0803 -0.0443 -0.0878 376 HOH B O   
2023 O  O   . HOH G .   ? 0.5879 0.4114 0.6652 0.1582  0.1144  0.1318  377 HOH B O   
2024 O  O   . HOH G .   ? 0.5873 0.6822 0.4904 -0.0633 -0.0751 0.2757  378 HOH B O   
2025 O  O   . HOH G .   ? 0.6914 0.5373 0.4363 0.1289  0.2320  -0.1216 379 HOH B O   
2026 O  O   . HOH G .   ? 0.7275 0.3499 0.3689 -0.0810 -0.0197 0.0752  380 HOH B O   
2027 O  O   . HOH G .   ? 0.4603 0.5999 0.7014 -0.0916 -0.1963 0.0746  381 HOH B O   
2028 O  O   . HOH G .   ? 0.3998 0.9176 0.7061 -0.0124 0.0304  0.3860  382 HOH B O   
2029 O  O   . HOH G .   ? 0.4771 0.4855 0.6326 0.0496  0.0524  0.0842  383 HOH B O   
2030 O  O   . HOH G .   ? 0.4785 0.5019 0.8332 0.0602  -0.0640 0.2084  384 HOH B O   
2031 O  O   . HOH G .   ? 0.5925 0.6442 0.7178 0.0110  -0.0495 0.2961  385 HOH B O   
2032 O  O   . HOH G .   ? 0.6002 0.8098 0.5869 -0.0320 -0.0789 -0.0790 386 HOH B O   
2033 O  O   . HOH G .   ? 0.6662 0.6373 0.6776 0.0700  0.1535  0.1421  387 HOH B O   
2034 O  O   . HOH G .   ? 0.4596 0.7231 0.7750 0.1813  0.1123  0.3613  388 HOH B O   
2035 O  O   . HOH G .   ? 0.3036 0.4227 0.2783 0.0611  0.0246  0.0812  389 HOH B O   
2036 O  O   . HOH G .   ? 0.6458 0.5277 0.8182 0.2134  0.0793  0.0229  390 HOH B O   
2037 O  O   . HOH G .   ? 0.6387 0.8364 0.4219 -0.0556 -0.0594 -0.0192 391 HOH B O   
2038 O  O   . HOH G .   ? 0.9687 0.5142 0.5916 0.1104  -0.0442 0.0406  392 HOH B O   
2039 O  O   . HOH G .   ? 0.4657 0.2925 0.4564 0.0964  0.1559  0.0240  393 HOH B O   
2040 O  O   . HOH G .   ? 0.5933 0.6432 0.7682 0.0339  -0.0781 0.0470  394 HOH B O   
2041 O  O   . HOH G .   ? 0.5554 0.4991 0.2122 -0.0020 -0.0458 0.0616  395 HOH B O   
2042 O  O   . HOH G .   ? 0.4173 0.5256 0.5004 0.0763  0.1954  0.0374  396 HOH B O   
2043 O  O   . HOH G .   ? 0.6291 0.5368 0.4735 0.1345  0.1405  0.1592  397 HOH B O   
2044 O  O   . HOH G .   ? 0.7108 0.6424 0.4984 -0.1633 -0.0843 -0.0697 398 HOH B O   
2045 O  O   . HOH G .   ? 0.7892 0.7353 0.4977 0.1515  -0.0748 0.0076  399 HOH B O   
2046 O  O   . HOH G .   ? 0.5869 0.8325 0.4535 0.0734  0.0037  -0.1006 400 HOH B O   
2047 O  O   . HOH G .   ? 0.5416 0.5993 0.5379 -0.1150 0.0558  -0.3050 401 HOH B O   
2048 O  O   . HOH G .   ? 0.4532 0.6805 0.8778 -0.1055 0.0653  0.2202  402 HOH B O   
# 
