data_9GAU
# 
_entry.id   9GAU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GAU         pdb_00009gau 10.2210/pdb9gau/pdb 
WWPDB D_1292139679 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-12 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GAU 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'Sumo-Darpin-A10 complex' 
_pdbx_database_related.db_id          9G8I 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              evawolf1@uni-mainz.de 
_pdbx_contact_author.name_first         Eva 
_pdbx_contact_author.name_last          Wolf 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1345-6114 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wolf, E.'      1 ? 
'Cakilkaya, B.' 2 ? 
'Boergel, A.'   3 ? 
# 
_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            'Cell Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2211-1247 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            44 
_citation.language                  ? 
_citation.page_first                115353 
_citation.page_last                 115353 
_citation.title                     
'Custom affinity probes reveal DNA-damage-induced, ssDNA-independent chromatin SUMOylation in budding yeast.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.celrep.2025.115353 
_citation.pdbx_database_id_PubMed   40019834 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Troster, V.'      1  ? 
primary 'Wong, R.P.'       2  ? 
primary 'Borgel, A.'       3  ? 
primary 'Cakilkaya, B.'    4  ? 
primary 'Renz, C.'         5  ? 
primary 'Mockel, M.M.'     6  ? 
primary 'Eifler-Olivi, K.' 7  ? 
primary 'Marinho, J.'      8  ? 
primary 'Reinberg, T.'     9  ? 
primary 'Furler, S.'       10 ? 
primary 'Schaefer, J.V.'   11 ? 
primary 'Pluckthun, A.'    12 ? 
primary 'Wolf, E.'         13 ? 
primary 'Ulrich, H.D.'     14 ? 
# 
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 DARPin                        13211.627 1  ? ? ? ? 
2 polymer man 'Ubiquitin-like protein SMT3' 8938.099  1  ? ? ? ? 
3 water   nat water                         18.015    31 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;SDLGKKLLEAARAGQDDEVRILMANGADVNAQDTQGRTPLHLAAQRGHLEIVEVLLKAGADVNAHDQYGWTPLHLAAHAN
GHLEIVEVLLKHGADVNAQDWIGVTPFDLAVDDGNEDIAEVLQ
;
;SDLGKKLLEAARAGQDDEVRILMANGADVNAQDTQGRTPLHLAAQRGHLEIVEVLLKAGADVNAHDQYGWTPLHLAAHAN
GHLEIVEVLLKHGADVNAQDWIGVTPFDLAVDDGNEDIAEVLQ
;
A ? 
2 'polypeptide(L)' no no ETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQI 
ETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQI                                                   B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASP n 
1 3   LEU n 
1 4   GLY n 
1 5   LYS n 
1 6   LYS n 
1 7   LEU n 
1 8   LEU n 
1 9   GLU n 
1 10  ALA n 
1 11  ALA n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  GLN n 
1 16  ASP n 
1 17  ASP n 
1 18  GLU n 
1 19  VAL n 
1 20  ARG n 
1 21  ILE n 
1 22  LEU n 
1 23  MET n 
1 24  ALA n 
1 25  ASN n 
1 26  GLY n 
1 27  ALA n 
1 28  ASP n 
1 29  VAL n 
1 30  ASN n 
1 31  ALA n 
1 32  GLN n 
1 33  ASP n 
1 34  THR n 
1 35  GLN n 
1 36  GLY n 
1 37  ARG n 
1 38  THR n 
1 39  PRO n 
1 40  LEU n 
1 41  HIS n 
1 42  LEU n 
1 43  ALA n 
1 44  ALA n 
1 45  GLN n 
1 46  ARG n 
1 47  GLY n 
1 48  HIS n 
1 49  LEU n 
1 50  GLU n 
1 51  ILE n 
1 52  VAL n 
1 53  GLU n 
1 54  VAL n 
1 55  LEU n 
1 56  LEU n 
1 57  LYS n 
1 58  ALA n 
1 59  GLY n 
1 60  ALA n 
1 61  ASP n 
1 62  VAL n 
1 63  ASN n 
1 64  ALA n 
1 65  HIS n 
1 66  ASP n 
1 67  GLN n 
1 68  TYR n 
1 69  GLY n 
1 70  TRP n 
1 71  THR n 
1 72  PRO n 
1 73  LEU n 
1 74  HIS n 
1 75  LEU n 
1 76  ALA n 
1 77  ALA n 
1 78  HIS n 
1 79  ALA n 
1 80  ASN n 
1 81  GLY n 
1 82  HIS n 
1 83  LEU n 
1 84  GLU n 
1 85  ILE n 
1 86  VAL n 
1 87  GLU n 
1 88  VAL n 
1 89  LEU n 
1 90  LEU n 
1 91  LYS n 
1 92  HIS n 
1 93  GLY n 
1 94  ALA n 
1 95  ASP n 
1 96  VAL n 
1 97  ASN n 
1 98  ALA n 
1 99  GLN n 
1 100 ASP n 
1 101 TRP n 
1 102 ILE n 
1 103 GLY n 
1 104 VAL n 
1 105 THR n 
1 106 PRO n 
1 107 PHE n 
1 108 ASP n 
1 109 LEU n 
1 110 ALA n 
1 111 VAL n 
1 112 ASP n 
1 113 ASP n 
1 114 GLY n 
1 115 ASN n 
1 116 GLU n 
1 117 ASP n 
1 118 ILE n 
1 119 ALA n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 GLN n 
2 1   GLU n 
2 2   THR n 
2 3   HIS n 
2 4   ILE n 
2 5   ASN n 
2 6   LEU n 
2 7   LYS n 
2 8   VAL n 
2 9   SER n 
2 10  ASP n 
2 11  GLY n 
2 12  SER n 
2 13  SER n 
2 14  GLU n 
2 15  ILE n 
2 16  PHE n 
2 17  PHE n 
2 18  LYS n 
2 19  ILE n 
2 20  LYS n 
2 21  LYS n 
2 22  THR n 
2 23  THR n 
2 24  PRO n 
2 25  LEU n 
2 26  ARG n 
2 27  ARG n 
2 28  LEU n 
2 29  MET n 
2 30  GLU n 
2 31  ALA n 
2 32  PHE n 
2 33  ALA n 
2 34  LYS n 
2 35  ARG n 
2 36  GLN n 
2 37  GLY n 
2 38  LYS n 
2 39  GLU n 
2 40  MET n 
2 41  ASP n 
2 42  SER n 
2 43  LEU n 
2 44  ARG n 
2 45  PHE n 
2 46  LEU n 
2 47  TYR n 
2 48  ASP n 
2 49  GLY n 
2 50  ILE n 
2 51  ARG n 
2 52  ILE n 
2 53  GLN n 
2 54  ALA n 
2 55  ASP n 
2 56  GLN n 
2 57  THR n 
2 58  PRO n 
2 59  GLU n 
2 60  ASP n 
2 61  LEU n 
2 62  ASP n 
2 63  MET n 
2 64  GLU n 
2 65  ASP n 
2 66  ASN n 
2 67  ASP n 
2 68  ILE n 
2 69  ILE n 
2 70  GLU n 
2 71  ALA n 
2 72  HIS n 
2 73  ARG n 
2 74  GLU n 
2 75  GLN n 
2 76  ILE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 123 ?                ? ?                         ? ? ? ? ? ? 'synthetic construct'      32630 ? 
? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 76  
;brewer's yeast
;
? 'SMT3, YDR510W, D9719.15' ? ? ? ? ? ? 'Saccharomyces cerevisiae' 4932  ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 469008 ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
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   SER 1   14  14  SER SER A . n 
A 1 2   ASP 2   15  15  ASP ASP A . n 
A 1 3   LEU 3   16  16  LEU LEU A . n 
A 1 4   GLY 4   17  17  GLY GLY A . n 
A 1 5   LYS 5   18  18  LYS LYS A . n 
A 1 6   LYS 6   19  19  LYS LYS A . n 
A 1 7   LEU 7   20  20  LEU LEU A . n 
A 1 8   LEU 8   21  21  LEU LEU A . n 
A 1 9   GLU 9   22  22  GLU GLU A . n 
A 1 10  ALA 10  23  23  ALA ALA A . n 
A 1 11  ALA 11  24  24  ALA ALA A . n 
A 1 12  ARG 12  25  25  ARG ARG A . n 
A 1 13  ALA 13  26  26  ALA ALA A . n 
A 1 14  GLY 14  27  27  GLY GLY A . n 
A 1 15  GLN 15  28  28  GLN GLN A . n 
A 1 16  ASP 16  29  29  ASP ASP A . n 
A 1 17  ASP 17  30  30  ASP ASP A . n 
A 1 18  GLU 18  31  31  GLU GLU A . n 
A 1 19  VAL 19  32  32  VAL VAL A . n 
A 1 20  ARG 20  33  33  ARG ARG A . n 
A 1 21  ILE 21  34  34  ILE ILE A . n 
A 1 22  LEU 22  35  35  LEU LEU A . n 
A 1 23  MET 23  36  36  MET MET A . n 
A 1 24  ALA 24  37  37  ALA ALA A . n 
A 1 25  ASN 25  38  38  ASN ASN A . n 
A 1 26  GLY 26  39  39  GLY GLY A . n 
A 1 27  ALA 27  40  40  ALA ALA A . n 
A 1 28  ASP 28  41  41  ASP ASP A . n 
A 1 29  VAL 29  42  42  VAL VAL A . n 
A 1 30  ASN 30  43  43  ASN ASN A . n 
A 1 31  ALA 31  44  44  ALA ALA A . n 
A 1 32  GLN 32  45  45  GLN GLN A . n 
A 1 33  ASP 33  46  46  ASP ASP A . n 
A 1 34  THR 34  47  47  THR THR A . n 
A 1 35  GLN 35  48  48  GLN GLN A . n 
A 1 36  GLY 36  49  49  GLY GLY A . n 
A 1 37  ARG 37  50  50  ARG ARG A . n 
A 1 38  THR 38  51  51  THR THR A . n 
A 1 39  PRO 39  52  52  PRO PRO A . n 
A 1 40  LEU 40  53  53  LEU LEU A . n 
A 1 41  HIS 41  54  54  HIS HIS A . n 
A 1 42  LEU 42  55  55  LEU LEU A . n 
A 1 43  ALA 43  56  56  ALA ALA A . n 
A 1 44  ALA 44  57  57  ALA ALA A . n 
A 1 45  GLN 45  58  58  GLN GLN A . n 
A 1 46  ARG 46  59  59  ARG ARG A . n 
A 1 47  GLY 47  60  60  GLY GLY A . n 
A 1 48  HIS 48  61  61  HIS HIS A . n 
A 1 49  LEU 49  62  62  LEU LEU A . n 
A 1 50  GLU 50  63  63  GLU GLU A . n 
A 1 51  ILE 51  64  64  ILE ILE A . n 
A 1 52  VAL 52  65  65  VAL VAL A . n 
A 1 53  GLU 53  66  66  GLU GLU A . n 
A 1 54  VAL 54  67  67  VAL VAL A . n 
A 1 55  LEU 55  68  68  LEU LEU A . n 
A 1 56  LEU 56  69  69  LEU LEU A . n 
A 1 57  LYS 57  70  70  LYS LYS A . n 
A 1 58  ALA 58  71  71  ALA ALA A . n 
A 1 59  GLY 59  72  72  GLY GLY A . n 
A 1 60  ALA 60  73  73  ALA ALA A . n 
A 1 61  ASP 61  74  74  ASP ASP A . n 
A 1 62  VAL 62  75  75  VAL VAL A . n 
A 1 63  ASN 63  76  76  ASN ASN A . n 
A 1 64  ALA 64  77  77  ALA ALA A . n 
A 1 65  HIS 65  78  78  HIS HIS A . n 
A 1 66  ASP 66  79  79  ASP ASP A . n 
A 1 67  GLN 67  80  80  GLN GLN A . n 
A 1 68  TYR 68  81  81  TYR TYR A . n 
A 1 69  GLY 69  82  82  GLY GLY A . n 
A 1 70  TRP 70  83  83  TRP TRP A . n 
A 1 71  THR 71  84  84  THR THR A . n 
A 1 72  PRO 72  85  85  PRO PRO A . n 
A 1 73  LEU 73  86  86  LEU LEU A . n 
A 1 74  HIS 74  87  87  HIS HIS A . n 
A 1 75  LEU 75  88  88  LEU LEU A . n 
A 1 76  ALA 76  89  89  ALA ALA A . n 
A 1 77  ALA 77  90  90  ALA ALA A . n 
A 1 78  HIS 78  91  91  HIS HIS A . n 
A 1 79  ALA 79  92  92  ALA ALA A . n 
A 1 80  ASN 80  93  93  ASN ASN A . n 
A 1 81  GLY 81  94  94  GLY GLY A . n 
A 1 82  HIS 82  95  95  HIS HIS A . n 
A 1 83  LEU 83  96  96  LEU LEU A . n 
A 1 84  GLU 84  97  97  GLU GLU A . n 
A 1 85  ILE 85  98  98  ILE ILE A . n 
A 1 86  VAL 86  99  99  VAL VAL A . n 
A 1 87  GLU 87  100 100 GLU GLU A . n 
A 1 88  VAL 88  101 101 VAL VAL A . n 
A 1 89  LEU 89  102 102 LEU LEU A . n 
A 1 90  LEU 90  103 103 LEU LEU A . n 
A 1 91  LYS 91  104 104 LYS LYS A . n 
A 1 92  HIS 92  105 105 HIS HIS A . n 
A 1 93  GLY 93  106 106 GLY GLY A . n 
A 1 94  ALA 94  107 107 ALA ALA A . n 
A 1 95  ASP 95  108 108 ASP ASP A . n 
A 1 96  VAL 96  109 109 VAL VAL A . n 
A 1 97  ASN 97  110 110 ASN ASN A . n 
A 1 98  ALA 98  111 111 ALA ALA A . n 
A 1 99  GLN 99  112 112 GLN GLN A . n 
A 1 100 ASP 100 113 113 ASP ASP A . n 
A 1 101 TRP 101 114 114 TRP TRP A . n 
A 1 102 ILE 102 115 115 ILE ILE A . n 
A 1 103 GLY 103 116 116 GLY GLY A . n 
A 1 104 VAL 104 117 117 VAL VAL A . n 
A 1 105 THR 105 118 118 THR THR A . n 
A 1 106 PRO 106 119 119 PRO PRO A . n 
A 1 107 PHE 107 120 120 PHE PHE A . n 
A 1 108 ASP 108 121 121 ASP ASP A . n 
A 1 109 LEU 109 122 122 LEU LEU A . n 
A 1 110 ALA 110 123 123 ALA ALA A . n 
A 1 111 VAL 111 124 124 VAL VAL A . n 
A 1 112 ASP 112 125 125 ASP ASP A . n 
A 1 113 ASP 113 126 126 ASP ASP A . n 
A 1 114 GLY 114 127 127 GLY GLY A . n 
A 1 115 ASN 115 128 128 ASN ASN A . n 
A 1 116 GLU 116 129 129 GLU GLU A . n 
A 1 117 ASP 117 130 130 ASP ASP A . n 
A 1 118 ILE 118 131 131 ILE ILE A . n 
A 1 119 ALA 119 132 132 ALA ALA A . n 
A 1 120 GLU 120 133 133 GLU GLU A . n 
A 1 121 VAL 121 134 134 VAL VAL A . n 
A 1 122 LEU 122 135 135 LEU LEU A . n 
A 1 123 GLN 123 136 136 GLN GLN A . n 
B 2 1   GLU 1   21  21  GLU GLU B . n 
B 2 2   THR 2   22  22  THR THR B . n 
B 2 3   HIS 3   23  23  HIS HIS B . n 
B 2 4   ILE 4   24  24  ILE ILE B . n 
B 2 5   ASN 5   25  25  ASN ASN B . n 
B 2 6   LEU 6   26  26  LEU LEU B . n 
B 2 7   LYS 7   27  27  LYS LYS B . n 
B 2 8   VAL 8   28  28  VAL VAL B . n 
B 2 9   SER 9   29  29  SER SER B . n 
B 2 10  ASP 10  30  30  ASP ASP B . n 
B 2 11  GLY 11  31  31  GLY GLY B . n 
B 2 12  SER 12  32  32  SER SER B . n 
B 2 13  SER 13  33  33  SER SER B . n 
B 2 14  GLU 14  34  34  GLU GLU B . n 
B 2 15  ILE 15  35  35  ILE ILE B . n 
B 2 16  PHE 16  36  36  PHE PHE B . n 
B 2 17  PHE 17  37  37  PHE PHE B . n 
B 2 18  LYS 18  38  38  LYS LYS B . n 
B 2 19  ILE 19  39  39  ILE ILE B . n 
B 2 20  LYS 20  40  40  LYS LYS B . n 
B 2 21  LYS 21  41  41  LYS LYS B . n 
B 2 22  THR 22  42  42  THR THR B . n 
B 2 23  THR 23  43  43  THR THR B . n 
B 2 24  PRO 24  44  44  PRO PRO B . n 
B 2 25  LEU 25  45  45  LEU LEU B . n 
B 2 26  ARG 26  46  46  ARG ARG B . n 
B 2 27  ARG 27  47  47  ARG ARG B . n 
B 2 28  LEU 28  48  48  LEU LEU B . n 
B 2 29  MET 29  49  49  MET MET B . n 
B 2 30  GLU 30  50  50  GLU GLU B . n 
B 2 31  ALA 31  51  51  ALA ALA B . n 
B 2 32  PHE 32  52  52  PHE PHE B . n 
B 2 33  ALA 33  53  53  ALA ALA B . n 
B 2 34  LYS 34  54  54  LYS LYS B . n 
B 2 35  ARG 35  55  55  ARG ARG B . n 
B 2 36  GLN 36  56  56  GLN GLN B . n 
B 2 37  GLY 37  57  57  GLY GLY B . n 
B 2 38  LYS 38  58  58  LYS LYS B . n 
B 2 39  GLU 39  59  59  GLU GLU B . n 
B 2 40  MET 40  60  60  MET MET B . n 
B 2 41  ASP 41  61  61  ASP ASP B . n 
B 2 42  SER 42  62  62  SER SER B . n 
B 2 43  LEU 43  63  63  LEU LEU B . n 
B 2 44  ARG 44  64  64  ARG ARG B . n 
B 2 45  PHE 45  65  65  PHE PHE B . n 
B 2 46  LEU 46  66  66  LEU LEU B . n 
B 2 47  TYR 47  67  67  TYR TYR B . n 
B 2 48  ASP 48  68  68  ASP ALA B . n 
B 2 49  GLY 49  69  69  GLY ASP B . n 
B 2 50  ILE 50  70  70  ILE ILE B . n 
B 2 51  ARG 51  71  71  ARG ARG B . n 
B 2 52  ILE 52  72  72  ILE ILE B . n 
B 2 53  GLN 53  73  73  GLN GLN B . n 
B 2 54  ALA 54  74  74  ALA ALA B . n 
B 2 55  ASP 55  75  75  ASP ASP B . n 
B 2 56  GLN 56  76  76  GLN GLN B . n 
B 2 57  THR 57  77  77  THR THR B . n 
B 2 58  PRO 58  78  78  PRO PRO B . n 
B 2 59  GLU 59  79  79  GLU GLU B . n 
B 2 60  ASP 60  80  80  ASP ASP B . n 
B 2 61  LEU 61  81  81  LEU LEU B . n 
B 2 62  ASP 62  82  82  ASP ASP B . n 
B 2 63  MET 63  83  83  MET MET B . n 
B 2 64  GLU 64  84  84  GLU GLU B . n 
B 2 65  ASP 65  85  85  ASP ASP B . n 
B 2 66  ASN 66  86  86  ASN ASN B . n 
B 2 67  ASP 67  87  87  ASP ASP B . n 
B 2 68  ILE 68  88  88  ILE ILE B . n 
B 2 69  ILE 69  89  89  ILE ILE B . n 
B 2 70  GLU 70  90  90  GLU GLU B . n 
B 2 71  ALA 71  91  91  ALA ALA B . n 
B 2 72  HIS 72  92  92  HIS HIS B . n 
B 2 73  ARG 73  93  93  ARG ARG B . n 
B 2 74  GLU 74  94  94  GLU GLU B . n 
B 2 75  GLN 75  95  95  GLN GLN B . n 
B 2 76  ILE 76  96  96  ILE ILE B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 HOH 1  201 20 HOH HOH A . 
C 3 HOH 2  202 2  HOH HOH A . 
C 3 HOH 3  203 5  HOH HOH A . 
C 3 HOH 4  204 1  HOH HOH A . 
C 3 HOH 5  205 31 HOH HOH A . 
C 3 HOH 6  206 3  HOH HOH A . 
C 3 HOH 7  207 28 HOH HOH A . 
C 3 HOH 8  208 6  HOH HOH A . 
C 3 HOH 9  209 16 HOH HOH A . 
C 3 HOH 10 210 10 HOH HOH A . 
C 3 HOH 11 211 4  HOH HOH A . 
C 3 HOH 12 212 21 HOH HOH A . 
C 3 HOH 13 213 26 HOH HOH A . 
C 3 HOH 14 214 17 HOH HOH A . 
C 3 HOH 15 215 18 HOH HOH A . 
C 3 HOH 16 216 7  HOH HOH A . 
C 3 HOH 17 217 29 HOH HOH A . 
C 3 HOH 18 218 19 HOH HOH A . 
C 3 HOH 19 219 11 HOH HOH A . 
C 3 HOH 20 220 9  HOH HOH A . 
C 3 HOH 21 221 8  HOH HOH A . 
C 3 HOH 22 222 12 HOH HOH A . 
D 3 HOH 1  101 30 HOH HOH B . 
D 3 HOH 2  102 27 HOH HOH B . 
D 3 HOH 3  103 23 HOH HOH B . 
D 3 HOH 4  104 24 HOH HOH B . 
D 3 HOH 5  105 25 HOH HOH B . 
D 3 HOH 6  106 13 HOH HOH B . 
D 3 HOH 7  107 15 HOH HOH B . 
D 3 HOH 8  108 14 HOH HOH B . 
D 3 HOH 9  109 22 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 18  ? CD  ? A LYS 5   CD  
2  1 Y 1 A LYS 18  ? CE  ? A LYS 5   CE  
3  1 Y 1 A LYS 18  ? NZ  ? A LYS 5   NZ  
4  1 Y 1 A ASP 30  ? CG  ? A ASP 17  CG  
5  1 Y 1 A ASP 30  ? OD1 ? A ASP 17  OD1 
6  1 Y 1 A ASP 30  ? OD2 ? A ASP 17  OD2 
7  1 Y 1 A ASN 93  ? CG  ? A ASN 80  CG  
8  1 Y 1 A ASN 93  ? OD1 ? A ASN 80  OD1 
9  1 Y 1 A ASN 93  ? ND2 ? A ASN 80  ND2 
10 1 Y 1 A HIS 95  ? CG  ? A HIS 82  CG  
11 1 Y 1 A HIS 95  ? ND1 ? A HIS 82  ND1 
12 1 Y 1 A HIS 95  ? CD2 ? A HIS 82  CD2 
13 1 Y 1 A HIS 95  ? CE1 ? A HIS 82  CE1 
14 1 Y 1 A HIS 95  ? NE2 ? A HIS 82  NE2 
15 1 Y 1 A GLU 97  ? CG  ? A GLU 84  CG  
16 1 Y 1 A GLU 97  ? CD  ? A GLU 84  CD  
17 1 Y 1 A GLU 97  ? OE1 ? A GLU 84  OE1 
18 1 Y 1 A GLU 97  ? OE2 ? A GLU 84  OE2 
19 1 Y 1 A PHE 120 ? CG  ? A PHE 107 CG  
20 1 Y 1 A PHE 120 ? CD1 ? A PHE 107 CD1 
21 1 Y 1 A PHE 120 ? CD2 ? A PHE 107 CD2 
22 1 Y 1 A PHE 120 ? CE1 ? A PHE 107 CE1 
23 1 Y 1 A PHE 120 ? CE2 ? A PHE 107 CE2 
24 1 Y 1 A PHE 120 ? CZ  ? A PHE 107 CZ  
25 1 Y 1 A GLU 129 ? CG  ? A GLU 116 CG  
26 1 Y 1 A GLU 129 ? CD  ? A GLU 116 CD  
27 1 Y 1 A GLU 129 ? OE1 ? A GLU 116 OE1 
28 1 Y 1 A GLU 129 ? OE2 ? A GLU 116 OE2 
29 1 Y 1 B SER 32  ? OG  ? B SER 12  OG  
30 1 Y 1 B GLU 34  ? CG  ? B GLU 14  CG  
31 1 Y 1 B GLU 34  ? CD  ? B GLU 14  CD  
32 1 Y 1 B GLU 34  ? OE1 ? B GLU 14  OE1 
33 1 Y 1 B GLU 34  ? OE2 ? B GLU 14  OE2 
34 1 Y 1 B ASP 68  ? CG  ? B ASP 48  CG  
35 1 Y 1 B ASP 68  ? OD1 ? B ASP 48  OD1 
36 1 Y 1 B ASP 68  ? OD2 ? B ASP 48  OD2 
37 1 Y 1 B GLN 73  ? CG  ? B GLN 53  CG  
38 1 Y 1 B GLN 73  ? CD  ? B GLN 53  CD  
39 1 Y 1 B GLN 73  ? OE1 ? B GLN 53  OE1 
40 1 Y 1 B GLN 73  ? NE2 ? B GLN 53  NE2 
41 1 Y 1 B GLU 84  ? CG  ? B GLU 64  CG  
42 1 Y 1 B GLU 84  ? CD  ? B GLU 64  CD  
43 1 Y 1 B GLU 84  ? OE1 ? B GLU 64  OE1 
44 1 Y 1 B GLU 84  ? OE2 ? B GLU 64  OE2 
45 1 Y 1 B ARG 93  ? CG  ? B ARG 73  CG  
46 1 Y 1 B ARG 93  ? CD  ? B ARG 73  CD  
47 1 Y 1 B ARG 93  ? NE  ? B ARG 73  NE  
48 1 Y 1 B ARG 93  ? CZ  ? B ARG 73  CZ  
49 1 Y 1 B ARG 93  ? NH1 ? B ARG 73  NH1 
50 1 Y 1 B ARG 93  ? NH2 ? B ARG 73  NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.760 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GAU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.461 
_cell.length_a_esd                 ? 
_cell.length_b                     44.687 
_cell.length_b_esd                 ? 
_cell.length_c                     47.602 
_cell.length_c_esd                 ? 
_cell.volume                       190183.106 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9GAU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_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                   9GAU 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.66 
_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              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Bis-Tris. 16% (v/v)PEG 3350' 
_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         2020-04-02 
_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   0.999 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          45.20 
_reflns.entry_id                                       9GAU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.64 
_reflns.d_resolution_low                               47.05 
_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                                     5539 
_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                           98.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_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                                0.329 
_reflns.pdbx_Rpim_I_all                                0.144 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.974 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.293 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.64 
_reflns_shell.d_res_low                                     2.77 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           3612 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             695 
_reflns_shell.percent_possible_obs                          95.8 
_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                               5.2 
_reflns_shell.pdbx_chi_squared                              0.98 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.798 
_reflns_shell.pdbx_Rpim_I_all                               0.776 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.401 
_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                                  1.614 
_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                               53.27 
_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                                 9GAU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.64 
_refine.ls_d_res_low                             47.05 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     5531 
_refine.ls_number_reflns_R_free                  554 
_refine.ls_number_reflns_R_work                  4977 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.10 
_refine.ls_percent_reflns_R_free                 10.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2385 
_refine.ls_R_factor_R_free                       0.2883 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2330 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.1653 
_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                            0.3983 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.64 
_refine_hist.d_res_low                        47.05 
_refine_hist.number_atoms_solvent             31 
_refine_hist.number_atoms_total               1537 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1506 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0022 ? 1527 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5891 ? 2070 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0407 ? 241  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0039 ? 275  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 4.3494 ? 208  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.64 2.91  . . 133 1190 96.29 . . . . 0.3032 . . . . . . . . . . . 0.3720 
'X-RAY DIFFRACTION' 2.91 3.33  . . 137 1241 98.57 . . . . 0.2822 . . . . . . . . . . . 0.3040 
'X-RAY DIFFRACTION' 3.33 4.19  . . 142 1270 99.86 . . . . 0.2168 . . . . . . . . . . . 0.3165 
'X-RAY DIFFRACTION' 4.19 47.05 . . 142 1276 97.73 . . . . 0.2052 . . . . . . . . . . . 0.2362 
# 
_struct.entry_id                     9GAU 
_struct.title                        Sumo-Darpin-C10-complex 
_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        9GAU 
_struct_keywords.text            'Sumo, Darpin, Ankyrin repeats, SIGNALING PROTEIN' 
_struct_keywords.pdbx_keywords   'SIGNALING 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 2 ? 
C N N 3 ? 
D N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 9GAU       9GAU   ? 1 ?                                                                            1  
2 UNP SMT3_YEAST Q12306 ? 2 ETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQI 21 
# 
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 9GAU A 1 ? 123 ? 9GAU   14 ? 136 ? 14 136 
2 2 9GAU B 1 ? 76  ? Q12306 21 ? 96  ? 21 96  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 2   ? GLY A 14  ? ASP A 15  GLY A 27  1 ? 13 
HELX_P HELX_P2  AA2 GLN A 15  ? ASN A 25  ? GLN A 28  ASN A 38  1 ? 11 
HELX_P HELX_P3  AA3 THR A 38  ? ARG A 46  ? THR A 51  ARG A 59  1 ? 9  
HELX_P HELX_P4  AA4 HIS A 48  ? ALA A 58  ? HIS A 61  ALA A 71  1 ? 11 
HELX_P HELX_P5  AA5 THR A 71  ? HIS A 78  ? THR A 84  HIS A 91  1 ? 8  
HELX_P HELX_P6  AA6 HIS A 82  ? HIS A 92  ? HIS A 95  HIS A 105 1 ? 11 
HELX_P HELX_P7  AA7 THR A 105 ? GLY A 114 ? THR A 118 GLY A 127 1 ? 10 
HELX_P HELX_P8  AA8 GLU A 116 ? GLN A 123 ? GLU A 129 GLN A 136 1 ? 8  
HELX_P HELX_P9  AA9 LEU B 25  ? GLN B 36  ? LEU B 45  GLN B 56  1 ? 12 
HELX_P HELX_P10 AB1 GLU B 39  ? ASP B 41  ? GLU B 59  ASP B 61  5 ? 3  
HELX_P HELX_P11 AB2 THR B 57  ? ASP B 62  ? THR B 77  ASP B 82  5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? 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 GLU B 14 ? LYS B 20 ? GLU B 34 LYS B 40 
AA1 2 HIS B 3  ? SER B 9  ? HIS B 23 SER B 29 
AA1 3 ASP B 67 ? ARG B 73 ? ASP B 87 ARG B 93 
AA1 4 LEU B 43 ? TYR B 47 ? LEU B 63 TYR B 67 
AA1 5 ILE B 50 ? ARG B 51 ? ILE B 70 ARG B 71 
# 
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 ILE B 19 ? O ILE B 39 N ILE B 4  ? N ILE B 24 
AA1 2 3 N LYS B 7  ? N LYS B 27 O ILE B 69 ? O ILE B 89 
AA1 3 4 O GLU B 70 ? O GLU B 90 N LEU B 46 ? N LEU B 66 
AA1 4 5 N TYR B 47 ? N TYR B 67 O ILE B 50 ? O ILE B 70 
# 
_pdbx_entry_details.entry_id                   9GAU 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 92  ? ? 59.37  -105.11 
2 1 HIS A 95  ? ? 60.80  66.82   
3 1 ASP A 113 ? ? -79.59 -166.76 
4 1 GLU A 129 ? ? 52.95  -74.68  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 29.8224807361 -17.2695404014  7.2515449984  0.853591177256 ? 0.00861496744955  ? 0.0696113864892  
? 0.449771811526 ? -0.0532040307156 ? 0.492747085204 ? 9.33751614841 ? 1.40327772653  ? -0.479697928122 ? 4.46330016068 ? 
4.40640660219   ? 4.76976363238  ? 0.735162439795  ? -0.888779404394  ? -0.753875525875 ? 2.26521901186    ? -0.804580713013  ? 
0.932064427966   ? 0.56004745063    ? -0.304116527584  ? 0.153351692133    ? 
2  'X-RAY DIFFRACTION' ? refined 37.9492823854 -17.6828018922  2.61103413085 0.685979873577 ? 0.0654925985728   ? -0.0743836043363 
? 0.575789582973 ? 0.0190343050902  ? 0.31347199559  ? 5.38313791153 ? 3.77209926175  ? 1.29525616047   ? 6.77259598877 ? 
2.39906536056   ? 2.79908912903  ? -0.913224193283 ? -0.100913779472  ? -0.263895659467 ? -0.978408339516  ? 0.465989780776   ? 
-0.0334062209562 ? -0.314896063329  ? -0.516991324346  ? 0.302467021851    ? 
3  'X-RAY DIFFRACTION' ? refined 25.2669405094 -9.92509454829  5.40757841965 0.404581491897 ? 0.0780126882441   ? -0.0116526243348 
? 0.319380106463 ? -0.0171491705249 ? 0.408483020987 ? 3.03959042045 ? -1.02423246715 ? -1.44424090866  ? 5.23861047891 ? 
0.215266043066  ? 5.37021722055  ? 0.652422045903  ? 0.527829701165   ? 0.379083312791  ? -0.514318733404  ? -0.0288938125799 ? 
-0.278562275639  ? -0.0256619470469 ? -0.0346443288982 ? -0.563400652672   ? 
4  'X-RAY DIFFRACTION' ? refined 33.7047693934 -6.34181081789  10.4528316133 0.541349068184 ? 0.0466855225164   ? 0.00494312805584 
? 0.458462114705 ? 0.0317254666267  ? 0.382048035574 ? 5.27034065287 ? 3.29611830066  ? 4.7506267467    ? 2.44842696847 ? 
3.15217336323   ? 4.36137949381  ? 0.359473537502  ? -1.58817870806   ? 0.463922576652  ? 0.645476739844   ? -0.220540916003  ? 
0.194597224182   ? 0.122918878494   ? -0.930322546735  ? -0.247127113831   ? 
5  'X-RAY DIFFRACTION' ? refined 39.7356531174 -6.93772134778  2.51215790723 0.419028325159 ? 0.00454055906735  ? 0.0451745294327  
? 0.486674182286 ? -0.0297861094033 ? 0.630568847005 ? 5.58906843319 ? 1.62066690411  ? 4.24251441706   ? 7.90752039953 ? 
1.54220334615   ? 3.4710762174   ? 0.463772517538  ? 0.807693021457   ? 2.19430818069   ? -0.11127475545   ? -0.216956346204  ? 
0.320720602843   ? -0.0111607006625 ? 0.605179437202   ? -0.385011319533   ? 
6  'X-RAY DIFFRACTION' ? refined 25.7116531348 -0.938111631792 5.70411494389 0.558592681488 ? 0.149423293205    ? 0.0234244297551  
? 0.550399508189 ? 0.0918243597073  ? 0.283175961745 ? 6.48101559962 ? -3.76464907452 ? -6.08978213922  ? 4.88886854717 ? 
4.79741934482   ? 6.322567357    ? 0.596030837958  ? 1.15851636558    ? 0.708618317705  ? -0.0179886665946 ? -0.510288611233  ? 
-0.0911960605384 ? -0.261632211977  ? -0.30501793986   ? 0.000421208480205 ? 
7  'X-RAY DIFFRACTION' ? refined 33.534052764  2.29564202277   12.8632408786 0.5450322524   ? 0.167018210274    ? -0.0784768026016 
? 0.599007219673 ? -0.0831279760802 ? 0.739887546086 ? 4.98394088891 ? -4.13965099275 ? -4.93170953631  ? 7.64953847908 ? 
3.29724514757   ? 5.58589363995  ? -1.13601423371  ? -1.42107520489   ? 1.01004844557   ? 0.410352426738   ? 0.603282285389   ? 
-1.82650975286   ? -0.370143412018  ? 1.5219796947     ? 0.237847556237    ? 
8  'X-RAY DIFFRACTION' ? refined 40.3592944846 3.29277739469   4.87460067237 0.507517548828 ? -0.0395291955512  ? -0.0446657919107 
? 0.436879162927 ? 0.0371175307656  ? 0.55649030445  ? 6.21133580509 ? 1.34839358024  ? -1.56393205363  ? 2.84649459355 ? 
-0.636458813911 ? 8.31490987566  ? 0.773068729777  ? -0.194625331414  ? 0.911503633385  ? 0.710987244506   ? 0.0504673387762  ? 
-0.474609743585  ? -0.696062023019  ? 1.24199184073    ? -0.50428040013    ? 
9  'X-RAY DIFFRACTION' ? refined 28.385033806  8.70257375594   9.88638381088 0.538193719691 ? 0.0011247837602   ? -0.0504019014273 
? 0.386144306795 ? 0.0364449992929  ? 0.469549412851 ? 9.47979220571 ? -4.8223200433  ? -5.21224746994  ? 4.35447358947 ? 
3.24231975942   ? 3.42581149128  ? 0.713935747926  ? -0.0520237929204 ? 2.61707832877   ? -0.388184110275  ? 0.142384947041   ? 
-1.03271837811   ? -0.613515673662  ? 0.912526532607   ? 0.112238778605    ? 
10 'X-RAY DIFFRACTION' ? refined 39.878867242  11.2245356025   11.7708080037 0.68727559727  ? -0.0894652979242  ? 0.100872722925   
? 0.494016063749 ? -0.247094927891  ? 1.5113825785   ? 7.27188404583 ? -3.39136136745 ? -4.66158795799  ? 7.9826760535  ? 
0.388166288463  ? 3.49099555406  ? -0.128359606401 ? -1.00099777455   ? 2.28376654454   ? 0.51968667878    ? 0.675907018009   ? 
-1.85491840377   ? -1.71464910057   ? 1.49331134777    ? -0.311076392848   ? 
11 'X-RAY DIFFRACTION' ? refined 17.1328213718 2.97144689833   18.9175707832 0.600513778916 ? 0.109397117893    ? -0.113180146173  
? 0.391382176013 ? -0.119268701539  ? 0.40167594001  ? 4.55043024523 ? -2.11232024039 ? -0.59261323756  ? 6.05612702005 ? 
-1.26862537121  ? 0.590498121368 ? -0.400923635892 ? 0.0169936546178  ? 0.572109517892  ? 0.547357522736   ? 0.270878504785   ? 
-1.03920235386   ? -0.0539190311407 ? 0.151640991867   ? 0.151818654732    ? 
12 'X-RAY DIFFRACTION' ? refined 11.0522151214 10.3571458157   13.2022192858 0.646231390256 ? -0.0328504881433  ? 0.0615990690787  
? 0.554063084499 ? -0.0217768508935 ? 0.375274229637 ? 6.85206474121 ? -3.87483093199 ? 0.0792680417914 ? 2.66170304091 ? 
-1.89959475233  ? 8.71064965919  ? -0.042872792754 ? 1.04884344156    ? 0.703052106801  ? -0.192893337577  ? -0.553215001739  ? 
-0.331984674063  ? -0.922097442714  ? -0.5605248034    ? 0.332586764019    ? 
13 'X-RAY DIFFRACTION' ? refined 3.84932707802 11.1385965793   16.5410276669 0.59425940426  ? -0.00529377294747 ? -0.0451077220423 
? 0.563971440397 ? 0.014943501966   ? 0.183391822156 ? 7.97105994134 ? -2.50272965177 ? 0.904520306944  ? 8.1585439792  ? 
-0.397401133675 ? 0.105955502373 ? -0.178458696654 ? 0.853083006458   ? 0.893091308132  ? -0.111194858651  ? 0.639416140869   ? 
-0.669879946233  ? -0.812100178388  ? -0.727430062427  ? -0.186820128729   ? 
14 'X-RAY DIFFRACTION' ? refined 11.1678556167 8.01789976167   27.7990557347 1.23165777817  ? 0.17103776126     ? -0.0134941803241 
? 0.499536675937 ? -0.044566878218  ? 0.307158860566 ? 9.56123800014 ? 3.220324304    ? 2.91309450699   ? 5.91773616876 ? 
-1.430785392    ? 2.0992359672   ? -1.02716661745  ? -0.652982702847  ? 0.757380585242  ? 1.81013260204    ? 0.571440847282   ? 
0.374223521492   ? 0.970012395166   ? 0.311797958616   ? 0.292923481695    ? 
15 'X-RAY DIFFRACTION' ? refined 7.06030480963 2.5435066625    22.0892671341 0.818276269265 ? 0.0427860245211   ? -0.154921827916  
? 0.597150668907 ? 0.0641992226877  ? 0.224062038962 ? 3.53594357817 ? -1.13858364164 ? 2.26950635621   ? 5.30429530703 ? 
-1.31142761216  ? 7.23527002531  ? -0.351110832301 ? -0.395476158676  ? -0.059563212483 ? 0.601351553308   ? 0.520135938861   ? 
0.348951966307   ? 0.914732605995   ? -0.614756761777  ? -0.262246502794   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 14  ? A 13  A 26  ? ? 
;chain 'A' and (resid 14 through 26 )
;
2  'X-RAY DIFFRACTION' 2  A 14  A 27  ? A 25  A 38  ? ? 
;chain 'A' and (resid 27 through 38 )
;
3  'X-RAY DIFFRACTION' 3  A 26  A 39  ? A 38  A 51  ? ? 
;chain 'A' and (resid 39 through 51 )
;
4  'X-RAY DIFFRACTION' 4  A 39  A 52  ? A 48  A 61  ? ? 
;chain 'A' and (resid 52 through 61 )
;
5  'X-RAY DIFFRACTION' 5  A 49  A 62  ? A 57  A 70  ? ? 
;chain 'A' and (resid 62 through 70 )
;
6  'X-RAY DIFFRACTION' 6  A 58  A 71  ? A 71  A 84  ? ? 
;chain 'A' and (resid 71 through 84 )
;
7  'X-RAY DIFFRACTION' 7  A 72  A 85  ? A 82  A 95  ? ? 
;chain 'A' and (resid 85 through 95 )
;
8  'X-RAY DIFFRACTION' 8  A 83  A 96  ? A 91  A 104 ? ? 
;chain 'A' and (resid 96 through 104 )
;
9  'X-RAY DIFFRACTION' 9  A 92  A 105 ? A 113 A 126 ? ? 
;chain 'A' and (resid 105 through 126 )
;
10 'X-RAY DIFFRACTION' 10 A 114 A 127 ? A 123 A 136 ? ? 
;chain 'A' and (resid 127 through 136 )
;
11 'X-RAY DIFFRACTION' 11 B 1   B 21  ? B 25  B 45  ? ? 
;chain 'B' and (resid 21 through 45 )
;
12 'X-RAY DIFFRACTION' 12 B 26  B 46  ? B 36  B 56  ? ? 
;chain 'B' and (resid 46 through 56 )
;
13 'X-RAY DIFFRACTION' 13 B 37  B 57  ? B 46  B 66  ? ? 
;chain 'B' and (resid 57 through 66 )
;
14 'X-RAY DIFFRACTION' 14 B 47  B 67  ? B 61  B 81  ? ? 
;chain 'B' and (resid 67 through 81 )
;
15 'X-RAY DIFFRACTION' 15 B 62  B 82  ? B 76  B 96  ? ? 
;chain 'B' and (resid 82 through 96 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       222 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.56 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
THR N    N N N 290 
THR CA   C N S 291 
THR C    C N N 292 
THR O    O N N 293 
THR CB   C N R 294 
THR OG1  O N N 295 
THR CG2  C N N 296 
THR OXT  O N N 297 
THR H    H N N 298 
THR H2   H N N 299 
THR HA   H N N 300 
THR HB   H N N 301 
THR HG1  H N N 302 
THR HG21 H N N 303 
THR HG22 H N N 304 
THR HG23 H N N 305 
THR HXT  H N N 306 
TRP N    N N N 307 
TRP CA   C N S 308 
TRP C    C N N 309 
TRP O    O N N 310 
TRP CB   C N N 311 
TRP CG   C Y N 312 
TRP CD1  C Y N 313 
TRP CD2  C Y N 314 
TRP NE1  N Y N 315 
TRP CE2  C Y N 316 
TRP CE3  C Y N 317 
TRP CZ2  C Y N 318 
TRP CZ3  C Y N 319 
TRP CH2  C Y N 320 
TRP OXT  O N N 321 
TRP H    H N N 322 
TRP H2   H N N 323 
TRP HA   H N N 324 
TRP HB2  H N N 325 
TRP HB3  H N N 326 
TRP HD1  H N N 327 
TRP HE1  H N N 328 
TRP HE3  H N N 329 
TRP HZ2  H N N 330 
TRP HZ3  H N N 331 
TRP HH2  H N N 332 
TRP HXT  H N N 333 
TYR N    N N N 334 
TYR CA   C N S 335 
TYR C    C N N 336 
TYR O    O N N 337 
TYR CB   C N N 338 
TYR CG   C Y N 339 
TYR CD1  C Y N 340 
TYR CD2  C Y N 341 
TYR CE1  C Y N 342 
TYR CE2  C Y N 343 
TYR CZ   C Y N 344 
TYR OH   O N N 345 
TYR OXT  O N N 346 
TYR H    H N N 347 
TYR H2   H N N 348 
TYR HA   H N N 349 
TYR HB2  H N N 350 
TYR HB3  H N N 351 
TYR HD1  H N N 352 
TYR HD2  H N N 353 
TYR HE1  H N N 354 
TYR HE2  H N N 355 
TYR HH   H N N 356 
TYR HXT  H N N 357 
VAL N    N N N 358 
VAL CA   C N S 359 
VAL C    C N N 360 
VAL O    O N N 361 
VAL CB   C N N 362 
VAL CG1  C N N 363 
VAL CG2  C N N 364 
VAL OXT  O N N 365 
VAL H    H N N 366 
VAL H2   H N N 367 
VAL HA   H N N 368 
VAL HB   H N N 369 
VAL HG11 H N N 370 
VAL HG12 H N N 371 
VAL HG13 H N N 372 
VAL HG21 H N N 373 
VAL HG22 H N N 374 
VAL HG23 H N N 375 
VAL HXT  H N N 376 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TRP N   CA   sing N N 293 
TRP N   H    sing N N 294 
TRP N   H2   sing N N 295 
TRP CA  C    sing N N 296 
TRP CA  CB   sing N N 297 
TRP CA  HA   sing N N 298 
TRP C   O    doub N N 299 
TRP C   OXT  sing N N 300 
TRP CB  CG   sing N N 301 
TRP CB  HB2  sing N N 302 
TRP CB  HB3  sing N N 303 
TRP CG  CD1  doub Y N 304 
TRP CG  CD2  sing Y N 305 
TRP CD1 NE1  sing Y N 306 
TRP CD1 HD1  sing N N 307 
TRP CD2 CE2  doub Y N 308 
TRP CD2 CE3  sing Y N 309 
TRP NE1 CE2  sing Y N 310 
TRP NE1 HE1  sing N N 311 
TRP CE2 CZ2  sing Y N 312 
TRP CE3 CZ3  doub Y N 313 
TRP CE3 HE3  sing N N 314 
TRP CZ2 CH2  doub Y N 315 
TRP CZ2 HZ2  sing N N 316 
TRP CZ3 CH2  sing Y N 317 
TRP CZ3 HZ3  sing N N 318 
TRP CH2 HH2  sing N N 319 
TRP OXT HXT  sing N N 320 
TYR N   CA   sing N N 321 
TYR N   H    sing N N 322 
TYR N   H2   sing N N 323 
TYR CA  C    sing N N 324 
TYR CA  CB   sing N N 325 
TYR CA  HA   sing N N 326 
TYR C   O    doub N N 327 
TYR C   OXT  sing N N 328 
TYR CB  CG   sing N N 329 
TYR CB  HB2  sing N N 330 
TYR CB  HB3  sing N N 331 
TYR CG  CD1  doub Y N 332 
TYR CG  CD2  sing Y N 333 
TYR CD1 CE1  sing Y N 334 
TYR CD1 HD1  sing N N 335 
TYR CD2 CE2  doub Y N 336 
TYR CD2 HD2  sing N N 337 
TYR CE1 CZ   doub Y N 338 
TYR CE1 HE1  sing N N 339 
TYR CE2 CZ   sing Y N 340 
TYR CE2 HE2  sing N N 341 
TYR CZ  OH   sing N N 342 
TYR OH  HH   sing N N 343 
TYR OXT HXT  sing N N 344 
VAL N   CA   sing N N 345 
VAL N   H    sing N N 346 
VAL N   H2   sing N N 347 
VAL CA  C    sing N N 348 
VAL CA  CB   sing N N 349 
VAL CA  HA   sing N N 350 
VAL C   O    doub N N 351 
VAL C   OXT  sing N N 352 
VAL CB  CG1  sing N N 353 
VAL CB  CG2  sing N N 354 
VAL CB  HB   sing N N 355 
VAL CG1 HG11 sing N N 356 
VAL CG1 HG12 sing N N 357 
VAL CG1 HG13 sing N N 358 
VAL CG2 HG21 sing N N 359 
VAL CG2 HG22 sing N N 360 
VAL CG2 HG23 sing N N 361 
VAL OXT HXT  sing N N 362 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_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   1mj0 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9GAU 
_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]   0.011054 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001703 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022378 
_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]   0.021255 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 1   ? 21.90143 -21.42463 -0.00119 1.000 58.35314  ? 14  SER A N   1 
ATOM   2    C CA  . SER A 1 1   ? 22.38449 -22.40889 0.95985  1.000 60.44849  ? 14  SER A CA  1 
ATOM   3    C C   . SER A 1 1   ? 22.92931 -21.73526 2.21455  1.000 66.13118  ? 14  SER A C   1 
ATOM   4    O O   . SER A 1 1   ? 22.24390 -20.93250 2.84720  1.000 66.69066  ? 14  SER A O   1 
ATOM   5    C CB  . SER A 1 1   ? 23.45999 -23.29509 0.32739  1.000 59.34317  ? 14  SER A CB  1 
ATOM   6    O OG  . SER A 1 1   ? 24.61452 -22.54336 -0.00659 1.000 58.04031  ? 14  SER A OG  1 
ATOM   7    N N   . ASP A 1 2   ? 24.17208 -22.06433 2.56983  1.000 61.16832  ? 15  ASP A N   1 
ATOM   8    C CA  . ASP A 1 2   ? 24.76638 -21.59094 3.81252  1.000 61.53311  ? 15  ASP A CA  1 
ATOM   9    C C   . ASP A 1 2   ? 26.11628 -20.91157 3.61067  1.000 60.26177  ? 15  ASP A C   1 
ATOM   10   O O   . ASP A 1 2   ? 26.76807 -20.56038 4.60036  1.000 59.85704  ? 15  ASP A O   1 
ATOM   11   C CB  . ASP A 1 2   ? 24.89613 -22.75562 4.80252  1.000 64.86862  ? 15  ASP A CB  1 
ATOM   12   C CG  . ASP A 1 2   ? 25.46926 -24.00767 4.15926  1.000 65.03289  ? 15  ASP A CG  1 
ATOM   13   O OD1 . ASP A 1 2   ? 25.27515 -24.19205 2.93798  1.000 63.23849  ? 15  ASP A OD1 1 
ATOM   14   O OD2 . ASP A 1 2   ? 26.07477 -24.82814 4.88166  1.000 70.07112  ? 15  ASP A OD2 1 
ATOM   15   N N   . LEU A 1 3   ? 26.54127 -20.69870 2.36117  1.000 59.64075  ? 16  LEU A N   1 
ATOM   16   C CA  . LEU A 1 3   ? 27.83791 -20.07495 2.10858  1.000 55.29136  ? 16  LEU A CA  1 
ATOM   17   C C   . LEU A 1 3   ? 27.90821 -18.67219 2.70218  1.000 49.35907  ? 16  LEU A C   1 
ATOM   18   O O   . LEU A 1 3   ? 28.95178 -18.26511 3.22661  1.000 46.81032  ? 16  LEU A O   1 
ATOM   19   C CB  . LEU A 1 3   ? 28.11975 -20.03622 0.60557  1.000 51.92721  ? 16  LEU A CB  1 
ATOM   20   C CG  . LEU A 1 3   ? 28.59475 -21.33855 -0.04407 1.000 46.76589  ? 16  LEU A CG  1 
ATOM   21   C CD1 . LEU A 1 3   ? 28.58389 -21.22356 -1.56133 1.000 47.46472  ? 16  LEU A CD1 1 
ATOM   22   C CD2 . LEU A 1 3   ? 29.98029 -21.71943 0.45688  1.000 44.57690  ? 16  LEU A CD2 1 
ATOM   23   N N   . GLY A 1 4   ? 26.81280 -17.91423 2.62125  1.000 49.39823  ? 17  GLY A N   1 
ATOM   24   C CA  . GLY A 1 4   ? 26.79546 -16.59542 3.23397  1.000 51.20765  ? 17  GLY A CA  1 
ATOM   25   C C   . GLY A 1 4   ? 26.96976 -16.64973 4.73992  1.000 51.99358  ? 17  GLY A C   1 
ATOM   26   O O   . GLY A 1 4   ? 27.64805 -15.80274 5.32756  1.000 48.47743  ? 17  GLY A O   1 
ATOM   27   N N   . LYS A 1 5   ? 26.35559 -17.64530 5.38600  1.000 52.21016  ? 18  LYS A N   1 
ATOM   28   C CA  . LYS A 1 5   ? 26.50698 -17.79689 6.82980  1.000 51.27222  ? 18  LYS A CA  1 
ATOM   29   C C   . LYS A 1 5   ? 27.95431 -18.09096 7.20838  1.000 50.55838  ? 18  LYS A C   1 
ATOM   30   O O   . LYS A 1 5   ? 28.48365 -17.50683 8.16087  1.000 51.94284  ? 18  LYS A O   1 
ATOM   31   C CB  . LYS A 1 5   ? 25.57907 -18.89952 7.34092  1.000 55.80353  ? 18  LYS A CB  1 
ATOM   32   C CG  . LYS A 1 5   ? 24.51233 -18.41183 8.30994  1.000 60.01265  ? 18  LYS A CG  1 
ATOM   33   N N   . LYS A 1 6   ? 28.61470 -18.98805 6.46924  1.000 48.86518  ? 19  LYS A N   1 
ATOM   34   C CA  . LYS A 1 6   ? 30.02465 -19.26458 6.73163  1.000 48.36199  ? 19  LYS A CA  1 
ATOM   35   C C   . LYS A 1 6   ? 30.89157 -18.03965 6.47000  1.000 46.62497  ? 19  LYS A C   1 
ATOM   36   O O   . LYS A 1 6   ? 31.85060 -17.78494 7.20542  1.000 45.81285  ? 19  LYS A O   1 
ATOM   37   C CB  . LYS A 1 6   ? 30.50634 -20.44690 5.89039  1.000 47.75342  ? 19  LYS A CB  1 
ATOM   38   C CG  . LYS A 1 6   ? 29.47712 -21.52649 5.66742  1.000 50.15388  ? 19  LYS A CG  1 
ATOM   39   C CD  . LYS A 1 6   ? 30.10576 -22.90478 5.76779  1.000 52.73616  ? 19  LYS A CD  1 
ATOM   40   C CE  . LYS A 1 6   ? 29.03652 -23.98440 5.77325  1.000 60.30116  ? 19  LYS A CE  1 
ATOM   41   N NZ  . LYS A 1 6   ? 29.44290 -25.17731 4.98697  1.000 58.54348  ? 19  LYS A NZ  1 
ATOM   42   N N   . LEU A 1 7   ? 30.58489 -17.27823 5.41722  1.000 46.44738  ? 20  LEU A N   1 
ATOM   43   C CA  . LEU A 1 7   ? 31.35854 -16.07185 5.13982  1.000 44.63991  ? 20  LEU A CA  1 
ATOM   44   C C   . LEU A 1 7   ? 31.21511 -15.05411 6.26478  1.000 45.46590  ? 20  LEU A C   1 
ATOM   45   O O   . LEU A 1 7   ? 32.20429 -14.44822 6.69455  1.000 46.41850  ? 20  LEU A O   1 
ATOM   46   C CB  . LEU A 1 7   ? 30.92819 -15.46446 3.80583  1.000 43.61773  ? 20  LEU A CB  1 
ATOM   47   C CG  . LEU A 1 7   ? 31.69812 -14.21384 3.37988  1.000 38.86061  ? 20  LEU A CG  1 
ATOM   48   C CD1 . LEU A 1 7   ? 33.16893 -14.53568 3.17482  1.000 42.80412  ? 20  LEU A CD1 1 
ATOM   49   C CD2 . LEU A 1 7   ? 31.09577 -13.62537 2.11865  1.000 40.63526  ? 20  LEU A CD2 1 
ATOM   50   N N   . LEU A 1 8   ? 29.98924 -14.85506 6.75582  1.000 43.49493  ? 21  LEU A N   1 
ATOM   51   C CA  . LEU A 1 8   ? 29.77999 -13.95326 7.88402  1.000 46.29263  ? 21  LEU A CA  1 
ATOM   52   C C   . LEU A 1 8   ? 30.50018 -14.45650 9.12794  1.000 49.45602  ? 21  LEU A C   1 
ATOM   53   O O   . LEU A 1 8   ? 31.10368 -13.67000 9.86780  1.000 50.65349  ? 21  LEU A O   1 
ATOM   54   C CB  . LEU A 1 8   ? 28.28426 -13.79308 8.15914  1.000 48.97199  ? 21  LEU A CB  1 
ATOM   55   C CG  . LEU A 1 8   ? 27.46816 -13.01371 7.12617  1.000 47.17099  ? 21  LEU A CG  1 
ATOM   56   C CD1 . LEU A 1 8   ? 26.01857 -13.46576 7.13548  1.000 49.73314  ? 21  LEU A CD1 1 
ATOM   57   C CD2 . LEU A 1 8   ? 27.56384 -11.52197 7.39109  1.000 47.65234  ? 21  LEU A CD2 1 
ATOM   58   N N   . GLU A 1 9   ? 30.45039 -15.76859 9.37026  1.000 51.43105  ? 22  GLU A N   1 
ATOM   59   C CA  . GLU A 1 9   ? 31.12065 -16.34282 10.53115 1.000 55.38468  ? 22  GLU A CA  1 
ATOM   60   C C   . GLU A 1 9   ? 32.62947 -16.14457 10.45126 1.000 53.60036  ? 22  GLU A C   1 
ATOM   61   O O   . GLU A 1 9   ? 33.27512 -15.81755 11.45319 1.000 56.41451  ? 22  GLU A O   1 
ATOM   62   C CB  . GLU A 1 9   ? 30.77225 -17.82757 10.63813 1.000 58.22088  ? 22  GLU A CB  1 
ATOM   63   C CG  . GLU A 1 9   ? 30.85763 -18.40016 12.03612 1.000 64.52814  ? 22  GLU A CG  1 
ATOM   64   C CD  . GLU A 1 9   ? 30.89692 -19.91585 12.03858 1.000 67.52840  ? 22  GLU A CD  1 
ATOM   65   O OE1 . GLU A 1 9   ? 32.00666 -20.48301 11.96150 1.000 67.59976  ? 22  GLU A OE1 1 
ATOM   66   O OE2 . GLU A 1 9   ? 29.81741 -20.54050 12.11709 1.000 70.27763  ? 22  GLU A OE2 1 
ATOM   67   N N   . ALA A 1 10  ? 33.20776 -16.33735 9.26381  1.000 49.37613  ? 23  ALA A N   1 
ATOM   68   C CA  . ALA A 1 10  ? 34.64525 -16.15554 9.09014  1.000 48.76152  ? 23  ALA A CA  1 
ATOM   69   C C   . ALA A 1 10  ? 35.03921 -14.68950 9.21708  1.000 48.69351  ? 23  ALA A C   1 
ATOM   70   O O   . ALA A 1 10  ? 36.08780 -14.37210 9.79071  1.000 51.88656  ? 23  ALA A O   1 
ATOM   71   C CB  . ALA A 1 10  ? 35.08619 -16.71722 7.73879  1.000 45.60520  ? 23  ALA A CB  1 
ATOM   72   N N   . ALA A 1 11  ? 34.21717 -13.78154 8.68262  1.000 45.06543  ? 24  ALA A N   1 
ATOM   73   C CA  . ALA A 1 11  ? 34.48814 -12.35706 8.84506  1.000 44.27067  ? 24  ALA A CA  1 
ATOM   74   C C   . ALA A 1 11  ? 34.43859 -11.95892 10.31328 1.000 48.70311  ? 24  ALA A C   1 
ATOM   75   O O   . ALA A 1 11  ? 35.23597 -11.13059 10.76863 1.000 49.57803  ? 24  ALA A O   1 
ATOM   76   C CB  . ALA A 1 11  ? 33.49299 -11.53417 8.02809  1.000 42.44813  ? 24  ALA A CB  1 
ATOM   77   N N   . ARG A 1 12  ? 33.49712 -12.53200 11.06590 1.000 52.01944  ? 25  ARG A N   1 
ATOM   78   C CA  . ARG A 1 12  ? 33.46712 -12.32988 12.51046 1.000 57.11804  ? 25  ARG A CA  1 
ATOM   79   C C   . ARG A 1 12  ? 34.73811 -12.85931 13.16349 1.000 59.24517  ? 25  ARG A C   1 
ATOM   80   O O   . ARG A 1 12  ? 35.34746 -12.18850 14.00448 1.000 61.88723  ? 25  ARG A O   1 
ATOM   81   C CB  . ARG A 1 12  ? 32.24293 -13.02594 13.10419 1.000 60.74246  ? 25  ARG A CB  1 
ATOM   82   C CG  . ARG A 1 12  ? 31.12727 -12.10661 13.55635 1.000 62.97731  ? 25  ARG A CG  1 
ATOM   83   C CD  . ARG A 1 12  ? 30.06593 -12.91022 14.28972 1.000 67.58302  ? 25  ARG A CD  1 
ATOM   84   N NE  . ARG A 1 12  ? 29.45012 -13.90445 13.41876 1.000 65.54627  ? 25  ARG A NE  1 
ATOM   85   C CZ  . ARG A 1 12  ? 28.17149 -13.90582 13.06732 1.000 65.83089  ? 25  ARG A CZ  1 
ATOM   86   N NH1 . ARG A 1 12  ? 27.33025 -12.98739 13.51493 1.000 68.18123  ? 25  ARG A NH1 1 
ATOM   87   N NH2 . ARG A 1 12  ? 27.72545 -14.85218 12.24568 1.000 64.13291  ? 25  ARG A NH2 1 
ATOM   88   N N   . ALA A 1 13  ? 35.15636 -14.06567 12.77859 1.000 58.59992  ? 26  ALA A N   1 
ATOM   89   C CA  . ALA A 1 13  ? 36.22545 -14.77661 13.46706 1.000 61.86517  ? 26  ALA A CA  1 
ATOM   90   C C   . ALA A 1 13  ? 37.61975 -14.41106 12.97638 1.000 59.29071  ? 26  ALA A C   1 
ATOM   91   O O   . ALA A 1 13  ? 38.60164 -14.80619 13.61438 1.000 62.47150  ? 26  ALA A O   1 
ATOM   92   C CB  . ALA A 1 13  ? 36.01601 -16.28491 13.32675 1.000 63.41523  ? 26  ALA A CB  1 
ATOM   93   N N   . GLY A 1 14  ? 37.73635 -13.67373 11.87835 1.000 51.93571  ? 27  GLY A N   1 
ATOM   94   C CA  . GLY A 1 14  ? 39.04578 -13.29232 11.37845 1.000 51.28432  ? 27  GLY A CA  1 
ATOM   95   C C   . GLY A 1 14  ? 39.85683 -14.39278 10.72706 1.000 51.23469  ? 27  GLY A C   1 
ATOM   96   O O   . GLY A 1 14  ? 41.07062 -14.47618 10.95509 1.000 48.71816  ? 27  GLY A O   1 
ATOM   97   N N   . GLN A 1 15  ? 39.21948 -15.24465 9.92451  1.000 50.91159  ? 28  GLN A N   1 
ATOM   98   C CA  . GLN A 1 15  ? 39.92088 -16.22614 9.10169  1.000 50.58543  ? 28  GLN A CA  1 
ATOM   99   C C   . GLN A 1 15  ? 40.01257 -15.68770 7.67864  1.000 49.14198  ? 28  GLN A C   1 
ATOM   100  O O   . GLN A 1 15  ? 39.02697 -15.71125 6.93526  1.000 48.46284  ? 28  GLN A O   1 
ATOM   101  C CB  . GLN A 1 15  ? 39.21441 -17.58014 9.11703  1.000 50.33531  ? 28  GLN A CB  1 
ATOM   102  C CG  . GLN A 1 15  ? 39.48828 -18.44244 10.33679 1.000 51.63814  ? 28  GLN A CG  1 
ATOM   103  C CD  . GLN A 1 15  ? 38.35211 -18.42762 11.33099 1.000 57.48235  ? 28  GLN A CD  1 
ATOM   104  O OE1 . GLN A 1 15  ? 38.51573 -17.99345 12.46976 1.000 61.14551  ? 28  GLN A OE1 1 
ATOM   105  N NE2 . GLN A 1 15  ? 37.18899 -18.90375 10.90594 1.000 56.45064  ? 28  GLN A NE2 1 
ATOM   106  N N   . ASP A 1 16  ? 41.19770 -15.20786 7.29836  1.000 49.62795  ? 29  ASP A N   1 
ATOM   107  C CA  . ASP A 1 16  ? 41.38184 -14.70492 5.94111  1.000 45.34341  ? 29  ASP A CA  1 
ATOM   108  C C   . ASP A 1 16  ? 41.38657 -15.84391 4.92857  1.000 43.93364  ? 29  ASP A C   1 
ATOM   109  O O   . ASP A 1 16  ? 40.79646 -15.72590 3.84716  1.000 44.77819  ? 29  ASP A O   1 
ATOM   110  C CB  . ASP A 1 16  ? 42.67723 -13.90051 5.85687  1.000 45.10246  ? 29  ASP A CB  1 
ATOM   111  C CG  . ASP A 1 16  ? 42.91168 -13.04998 7.08848  1.000 47.97132  ? 29  ASP A CG  1 
ATOM   112  O OD1 . ASP A 1 16  ? 42.90875 -11.80875 6.96984  1.000 49.86474  ? 29  ASP A OD1 1 
ATOM   113  O OD2 . ASP A 1 16  ? 43.11337 -13.62624 8.17767  1.000 50.58018  ? 29  ASP A OD2 1 
ATOM   114  N N   . ASP A 1 17  ? 42.04541 -16.95617 5.26487  1.000 43.49730  ? 30  ASP A N   1 
ATOM   115  C CA  . ASP A 1 17  ? 42.09651 -18.09559 4.35468  1.000 44.00646  ? 30  ASP A CA  1 
ATOM   116  C C   . ASP A 1 17  ? 40.70716 -18.66783 4.10303  1.000 45.14234  ? 30  ASP A C   1 
ATOM   117  O O   . ASP A 1 17  ? 40.34817 -18.96136 2.95602  1.000 45.33668  ? 30  ASP A O   1 
ATOM   118  C CB  . ASP A 1 17  ? 43.02587 -19.17093 4.91589  1.000 45.17533  ? 30  ASP A CB  1 
ATOM   119  N N   . GLU A 1 18  ? 39.90828 -18.82679 5.16295  1.000 46.68507  ? 31  GLU A N   1 
ATOM   120  C CA  . GLU A 1 18  ? 38.54281 -19.31710 4.99633  1.000 45.69388  ? 31  GLU A CA  1 
ATOM   121  C C   . GLU A 1 18  ? 37.68961 -18.33037 4.20811  1.000 44.65262  ? 31  GLU A C   1 
ATOM   122  O O   . GLU A 1 18  ? 36.84658 -18.74148 3.40450  1.000 44.43643  ? 31  GLU A O   1 
ATOM   123  C CB  . GLU A 1 18  ? 37.91130 -19.60830 6.36038  1.000 49.87900  ? 31  GLU A CB  1 
ATOM   124  C CG  . GLU A 1 18  ? 36.71064 -20.58081 6.35504  1.000 52.50884  ? 31  GLU A CG  1 
ATOM   125  C CD  . GLU A 1 18  ? 36.84094 -21.77424 5.40911  1.000 55.17777  ? 31  GLU A CD  1 
ATOM   126  O OE1 . GLU A 1 18  ? 35.79223 -22.30675 4.98191  1.000 56.67091  ? 31  GLU A OE1 1 
ATOM   127  O OE2 . GLU A 1 18  ? 37.97221 -22.23220 5.14905  1.000 57.88739  ? 31  GLU A OE2 1 
ATOM   128  N N   . VAL A 1 19  ? 37.89029 -17.02680 4.42258  1.000 42.15346  ? 32  VAL A N   1 
ATOM   129  C CA  . VAL A 1 19  ? 37.15635 -16.02399 3.65027  1.000 45.55166  ? 32  VAL A CA  1 
ATOM   130  C C   . VAL A 1 19  ? 37.47860 -16.15725 2.16638  1.000 46.23012  ? 32  VAL A C   1 
ATOM   131  O O   . VAL A 1 19  ? 36.58185 -16.15253 1.31305  1.000 47.80107  ? 32  VAL A O   1 
ATOM   132  C CB  . VAL A 1 19  ? 37.46557 -14.60699 4.17090  1.000 44.99732  ? 32  VAL A CB  1 
ATOM   133  C CG1 . VAL A 1 19  ? 37.18220 -13.56532 3.10068  1.000 42.89969  ? 32  VAL A CG1 1 
ATOM   134  C CG2 . VAL A 1 19  ? 36.64425 -14.30465 5.41428  1.000 44.84524  ? 32  VAL A CG2 1 
ATOM   135  N N   . ARG A 1 20  ? 38.76627 -16.28803 1.83761  1.000 45.55099  ? 33  ARG A N   1 
ATOM   136  C CA  . ARG A 1 20  ? 39.15912 -16.43167 0.43929  1.000 44.03874  ? 33  ARG A CA  1 
ATOM   137  C C   . ARG A 1 20  ? 38.60949 -17.72050 -0.16065 1.000 46.18380  ? 33  ARG A C   1 
ATOM   138  O O   . ARG A 1 20  ? 38.14034 -17.72943 -1.30521 1.000 46.58625  ? 33  ARG A O   1 
ATOM   139  C CB  . ARG A 1 20  ? 40.68275 -16.37630 0.31356  1.000 43.38736  ? 33  ARG A CB  1 
ATOM   140  C CG  . ARG A 1 20  ? 41.25285 -14.97543 0.48489  1.000 43.41716  ? 33  ARG A CG  1 
ATOM   141  C CD  . ARG A 1 20  ? 42.76523 -14.93620 0.32297  1.000 43.74785  ? 33  ARG A CD  1 
ATOM   142  N NE  . ARG A 1 20  ? 43.45312 -15.84451 1.23270  1.000 42.58533  ? 33  ARG A NE  1 
ATOM   143  C CZ  . ARG A 1 20  ? 44.22867 -15.45440 2.23549  1.000 45.58441  ? 33  ARG A CZ  1 
ATOM   144  N NH1 . ARG A 1 20  ? 44.41136 -14.17280 2.51018  1.000 41.52709  ? 33  ARG A NH1 1 
ATOM   145  N NH2 . ARG A 1 20  ? 44.83694 -16.37328 2.98102  1.000 47.79445  ? 33  ARG A NH2 1 
ATOM   146  N N   . ILE A 1 21  ? 38.64853 -18.81685 0.60117  1.000 44.99199  ? 34  ILE A N   1 
ATOM   147  C CA  . ILE A 1 21  ? 38.12260 -20.08925 0.10948  1.000 46.44130  ? 34  ILE A CA  1 
ATOM   148  C C   . ILE A 1 21  ? 36.62624 -19.97675 -0.16141 1.000 49.22804  ? 34  ILE A C   1 
ATOM   149  O O   . ILE A 1 21  ? 36.12691 -20.42844 -1.19992 1.000 50.92594  ? 34  ILE A O   1 
ATOM   150  C CB  . ILE A 1 21  ? 38.43366 -21.21977 1.10810  1.000 45.29622  ? 34  ILE A CB  1 
ATOM   151  C CG1 . ILE A 1 21  ? 39.84809 -21.75840 0.88590  1.000 46.98465  ? 34  ILE A CG1 1 
ATOM   152  C CG2 . ILE A 1 21  ? 37.41808 -22.34639 0.98482  1.000 47.01111  ? 34  ILE A CG2 1 
ATOM   153  C CD1 . ILE A 1 21  ? 40.49027 -22.31809 2.13619  1.000 46.64986  ? 34  ILE A CD1 1 
ATOM   154  N N   . LEU A 1 22  ? 35.89010 -19.36178 0.76726  1.000 46.52668  ? 35  LEU A N   1 
ATOM   155  C CA  . LEU A 1 22  ? 34.44577 -19.23774 0.61138  1.000 46.66870  ? 35  LEU A CA  1 
ATOM   156  C C   . LEU A 1 22  ? 34.08795 -18.33695 -0.56470 1.000 48.76733  ? 35  LEU A C   1 
ATOM   157  O O   . LEU A 1 22  ? 33.14044 -18.62673 -1.30494 1.000 50.97963  ? 35  LEU A O   1 
ATOM   158  C CB  . LEU A 1 22  ? 33.82690 -18.71786 1.90841  1.000 44.88443  ? 35  LEU A CB  1 
ATOM   159  C CG  . LEU A 1 22  ? 33.76426 -19.73853 3.04857  1.000 45.38907  ? 35  LEU A CG  1 
ATOM   160  C CD1 . LEU A 1 22  ? 33.58189 -19.04616 4.39012  1.000 45.01416  ? 35  LEU A CD1 1 
ATOM   161  C CD2 . LEU A 1 22  ? 32.65853 -20.75344 2.80811  1.000 47.60282  ? 35  LEU A CD2 1 
ATOM   162  N N   . MET A 1 23  ? 34.82639 -17.23811 -0.75475 1.000 48.26998  ? 36  MET A N   1 
ATOM   163  C CA  . MET A 1 23  ? 34.58582 -16.39731 -1.92489 1.000 49.82056  ? 36  MET A CA  1 
ATOM   164  C C   . MET A 1 23  ? 34.88421 -17.14939 -3.21506 1.000 51.43735  ? 36  MET A C   1 
ATOM   165  O O   . MET A 1 23  ? 34.13344 -17.04025 -4.19103 1.000 54.09856  ? 36  MET A O   1 
ATOM   166  C CB  . MET A 1 23  ? 35.41540 -15.11491 -1.85800 1.000 49.77906  ? 36  MET A CB  1 
ATOM   167  C CG  . MET A 1 23  ? 35.11769 -14.21787 -0.67011 1.000 48.81406  ? 36  MET A CG  1 
ATOM   168  S SD  . MET A 1 23  ? 36.42652 -13.00886 -0.37491 1.000 54.92513  ? 36  MET A SD  1 
ATOM   169  C CE  . MET A 1 23  ? 37.54640 -13.34774 -1.73492 1.000 50.94522  ? 36  MET A CE  1 
ATOM   170  N N   . ALA A 1 24  ? 35.97946 -17.91536 -3.24292 1.000 50.36364  ? 37  ALA A N   1 
ATOM   171  C CA  . ALA A 1 24  ? 36.29824 -18.69678 -4.43316 1.000 52.31836  ? 37  ALA A CA  1 
ATOM   172  C C   . ALA A 1 24  ? 35.23813 -19.75461 -4.70628 1.000 53.19384  ? 37  ALA A C   1 
ATOM   173  O O   . ALA A 1 24  ? 35.01743 -20.12838 -5.86426 1.000 55.78431  ? 37  ALA A O   1 
ATOM   174  C CB  . ALA A 1 24  ? 37.67443 -19.34593 -4.28533 1.000 51.37649  ? 37  ALA A CB  1 
ATOM   175  N N   . ASN A 1 25  ? 34.57426 -20.24849 -3.66078 1.000 51.45109  ? 38  ASN A N   1 
ATOM   176  C CA  . ASN A 1 25  ? 33.50489 -21.22220 -3.83620 1.000 52.42906  ? 38  ASN A CA  1 
ATOM   177  C C   . ASN A 1 25  ? 32.15837 -20.57918 -4.14249 1.000 54.32967  ? 38  ASN A C   1 
ATOM   178  O O   . ASN A 1 25  ? 31.19441 -21.30305 -4.41378 1.000 55.68077  ? 38  ASN A O   1 
ATOM   179  C CB  . ASN A 1 25  ? 33.38536 -22.10525 -2.59117 1.000 50.39291  ? 38  ASN A CB  1 
ATOM   180  C CG  . ASN A 1 25  ? 34.51448 -23.11189 -2.48268 1.000 51.74845  ? 38  ASN A CG  1 
ATOM   181  O OD1 . ASN A 1 25  ? 35.61898 -22.87718 -2.97361 1.000 52.61643  ? 38  ASN A OD1 1 
ATOM   182  N ND2 . ASN A 1 25  ? 34.24131 -24.24268 -1.84165 1.000 52.04628  ? 38  ASN A ND2 1 
ATOM   183  N N   . GLY A 1 26  ? 32.06738 -19.25526 -4.11031 1.000 50.25777  ? 39  GLY A N   1 
ATOM   184  C CA  . GLY A 1 26  ? 30.85848 -18.55751 -4.47851 1.000 49.11572  ? 39  GLY A CA  1 
ATOM   185  C C   . GLY A 1 26  ? 30.00264 -18.05346 -3.33860 1.000 46.64360  ? 39  GLY A C   1 
ATOM   186  O O   . GLY A 1 26  ? 28.77891 -17.97828 -3.49718 1.000 45.37107  ? 39  GLY A O   1 
ATOM   187  N N   . ALA A 1 27  ? 30.59694 -17.71117 -2.19911 1.000 48.30246  ? 40  ALA A N   1 
ATOM   188  C CA  . ALA A 1 27  ? 29.82671 -17.15291 -1.09727 1.000 47.13366  ? 40  ALA A CA  1 
ATOM   189  C C   . ALA A 1 27  ? 29.31021 -15.76635 -1.45971 1.000 48.02833  ? 40  ALA A C   1 
ATOM   190  O O   . ALA A 1 27  ? 29.97705 -15.00173 -2.16243 1.000 46.20498  ? 40  ALA A O   1 
ATOM   191  C CB  . ALA A 1 27  ? 30.67888 -17.08312 0.16891  1.000 45.94385  ? 40  ALA A CB  1 
ATOM   192  N N   . ASP A 1 28  ? 28.11151 -15.44465 -0.97698 1.000 50.00449  ? 41  ASP A N   1 
ATOM   193  C CA  . ASP A 1 28  ? 27.51231 -14.13820 -1.23172 1.000 49.23485  ? 41  ASP A CA  1 
ATOM   194  C C   . ASP A 1 28  ? 28.31353 -13.06870 -0.49933 1.000 49.70073  ? 41  ASP A C   1 
ATOM   195  O O   . ASP A 1 28  ? 28.26752 -12.98166 0.73176  1.000 49.59690  ? 41  ASP A O   1 
ATOM   196  C CB  . ASP A 1 28  ? 26.05214 -14.13051 -0.78789 1.000 48.90686  ? 41  ASP A CB  1 
ATOM   197  C CG  . ASP A 1 28  ? 25.27917 -12.93839 -1.33012 1.000 48.17450  ? 41  ASP A CG  1 
ATOM   198  O OD1 . ASP A 1 28  ? 25.90828 -12.01276 -1.88447 1.000 48.14291  ? 41  ASP A OD1 1 
ATOM   199  O OD2 . ASP A 1 28  ? 24.03722 -12.92628 -1.19797 1.000 51.20956  ? 41  ASP A OD2 1 
ATOM   200  N N   . VAL A 1 29  ? 29.04740 -12.24917 -1.25750 1.000 47.88105  ? 42  VAL A N   1 
ATOM   201  C CA  . VAL A 1 29  ? 29.87104 -11.20347 -0.66146 1.000 46.87200  ? 42  VAL A CA  1 
ATOM   202  C C   . VAL A 1 29  ? 29.02441 -10.15514 0.04712  1.000 46.03461  ? 42  VAL A C   1 
ATOM   203  O O   . VAL A 1 29  ? 29.52222 -9.45597  0.93663  1.000 44.41099  ? 42  VAL A O   1 
ATOM   204  C CB  . VAL A 1 29  ? 30.77320 -10.55680 -1.73633 1.000 46.58898  ? 42  VAL A CB  1 
ATOM   205  C CG1 . VAL A 1 29  ? 29.98767 -9.55772  -2.57293 1.000 47.93424  ? 42  VAL A CG1 1 
ATOM   206  C CG2 . VAL A 1 29  ? 31.97538 -9.88960  -1.09098 1.000 47.53234  ? 42  VAL A CG2 1 
ATOM   207  N N   . ASN A 1 30  ? 27.75056 -10.02387 -0.32533 1.000 47.16863  ? 43  ASN A N   1 
ATOM   208  C CA  . ASN A 1 30  ? 26.83879 -9.08437  0.31379  1.000 47.71316  ? 43  ASN A CA  1 
ATOM   209  C C   . ASN A 1 30  ? 25.76814 -9.78718  1.14190  1.000 45.83513  ? 43  ASN A C   1 
ATOM   210  O O   . ASN A 1 30  ? 24.68798 -9.22802  1.35462  1.000 46.60165  ? 43  ASN A O   1 
ATOM   211  C CB  . ASN A 1 30  ? 26.19352 -8.17638  -0.73299 1.000 48.15548  ? 43  ASN A CB  1 
ATOM   212  C CG  . ASN A 1 30  ? 27.20525 -7.30260  -1.44624 1.000 47.23250  ? 43  ASN A CG  1 
ATOM   213  O OD1 . ASN A 1 30  ? 28.15627 -6.81276  -0.83715 1.000 49.12592  ? 43  ASN A OD1 1 
ATOM   214  N ND2 . ASN A 1 30  ? 27.00606 -7.10233  -2.74358 1.000 47.29778  ? 43  ASN A ND2 1 
ATOM   215  N N   . ALA A 1 31  ? 26.04030 -11.00627 1.60216  1.000 46.18297  ? 44  ALA A N   1 
ATOM   216  C CA  . ALA A 1 31  ? 25.11139 -11.68755 2.49250  1.000 48.21888  ? 44  ALA A CA  1 
ATOM   217  C C   . ALA A 1 31  ? 25.01776 -10.94573 3.81936  1.000 46.73876  ? 44  ALA A C   1 
ATOM   218  O O   . ALA A 1 31  ? 26.01467 -10.44009 4.33928  1.000 44.55990  ? 44  ALA A O   1 
ATOM   219  C CB  . ALA A 1 31  ? 25.55540 -13.13195 2.72392  1.000 49.72531  ? 44  ALA A CB  1 
ATOM   220  N N   . GLN A 1 32  ? 23.81045 -10.87941 4.36958  1.000 47.68777  ? 45  GLN A N   1 
ATOM   221  C CA  . GLN A 1 32  ? 23.56008 -10.13971 5.59576  1.000 48.54541  ? 45  GLN A CA  1 
ATOM   222  C C   . GLN A 1 32  ? 23.02640 -11.07386 6.67210  1.000 48.21014  ? 45  GLN A C   1 
ATOM   223  O O   . GLN A 1 32  ? 22.30283 -12.03216 6.38469  1.000 47.01167  ? 45  GLN A O   1 
ATOM   224  C CB  . GLN A 1 32  ? 22.56968 -8.99129  5.35877  1.000 47.88920  ? 45  GLN A CB  1 
ATOM   225  C CG  . GLN A 1 32  ? 22.62200 -8.40769  3.95339  1.000 47.30591  ? 45  GLN A CG  1 
ATOM   226  C CD  . GLN A 1 32  ? 21.68460 -7.22839  3.77215  1.000 48.21791  ? 45  GLN A CD  1 
ATOM   227  O OE1 . GLN A 1 32  ? 21.39860 -6.81492  2.64809  1.000 53.65666  ? 45  GLN A OE1 1 
ATOM   228  N NE2 . GLN A 1 32  ? 21.20365 -6.67819  4.88104  1.000 47.27093  ? 45  GLN A NE2 1 
ATOM   229  N N   . ASP A 1 33  ? 23.39674 -10.78719 7.91670  1.000 46.09560  ? 46  ASP A N   1 
ATOM   230  C CA  . ASP A 1 33  ? 22.93131 -11.56078 9.05593  1.000 47.82804  ? 46  ASP A CA  1 
ATOM   231  C C   . ASP A 1 33  ? 21.58319 -11.01209 9.52472  1.000 46.10608  ? 46  ASP A C   1 
ATOM   232  O O   . ASP A 1 33  ? 20.94559 -10.20426 8.84356  1.000 44.36275  ? 46  ASP A O   1 
ATOM   233  C CB  . ASP A 1 33  ? 23.98759 -11.56267 10.16148 1.000 44.98896  ? 46  ASP A CB  1 
ATOM   234  C CG  . ASP A 1 33  ? 24.35096 -10.16605 10.63506 1.000 42.29870  ? 46  ASP A CG  1 
ATOM   235  O OD1 . ASP A 1 33  ? 23.76778 -9.18336  10.13254 1.000 45.69038  ? 46  ASP A OD1 1 
ATOM   236  O OD2 . ASP A 1 33  ? 25.22956 -10.05220 11.51560 1.000 40.60909  ? 46  ASP A OD2 1 
ATOM   237  N N   . THR A 1 34  ? 21.13350 -11.45236 10.70227 1.000 47.34022  ? 47  THR A N   1 
ATOM   238  C CA  . THR A 1 34  ? 19.81621 -11.05361 11.18850 1.000 49.71464  ? 47  THR A CA  1 
ATOM   239  C C   . THR A 1 34  ? 19.74258 -9.55929  11.47858 1.000 48.45297  ? 47  THR A C   1 
ATOM   240  O O   . THR A 1 34  ? 18.66559 -8.96227  11.36853 1.000 49.43844  ? 47  THR A O   1 
ATOM   241  C CB  . THR A 1 34  ? 19.45468 -11.85380 12.43793 1.000 51.26971  ? 47  THR A CB  1 
ATOM   242  O OG1 . THR A 1 34  ? 20.39624 -11.56504 13.47746 1.000 54.69078  ? 47  THR A OG1 1 
ATOM   243  C CG2 . THR A 1 34  ? 19.48431 -13.34481 12.13691 1.000 54.27195  ? 47  THR A CG2 1 
ATOM   244  N N   . GLN A 1 35  ? 20.86185 -8.93959  11.84318 1.000 48.10757  ? 48  GLN A N   1 
ATOM   245  C CA  . GLN A 1 35  ? 20.90531 -7.50229  12.07410 1.000 44.51752  ? 48  GLN A CA  1 
ATOM   246  C C   . GLN A 1 35  ? 21.18838 -6.70964  10.80486 1.000 43.85160  ? 48  GLN A C   1 
ATOM   247  O O   . GLN A 1 35  ? 21.31043 -5.48211  10.87307 1.000 43.08531  ? 48  GLN A O   1 
ATOM   248  C CB  . GLN A 1 35  ? 21.95681 -7.16302  13.13703 1.000 45.84036  ? 48  GLN A CB  1 
ATOM   249  C CG  . GLN A 1 35  ? 22.19656 -8.26256  14.16044 1.000 50.40318  ? 48  GLN A CG  1 
ATOM   250  C CD  . GLN A 1 35  ? 22.67430 -7.71970  15.49516 1.000 52.01826  ? 48  GLN A CD  1 
ATOM   251  O OE1 . GLN A 1 35  ? 22.43945 -6.55695  15.82495 1.000 48.61036  ? 48  GLN A OE1 1 
ATOM   252  N NE2 . GLN A 1 35  ? 23.34714 -8.56193  16.27113 1.000 57.49841  ? 48  GLN A NE2 1 
ATOM   253  N N   . GLY A 1 36  ? 21.29644 -7.37493  9.65635  1.000 41.55715  ? 49  GLY A N   1 
ATOM   254  C CA  . GLY A 1 36  ? 21.57591 -6.69487  8.40927  1.000 44.16229  ? 49  GLY A CA  1 
ATOM   255  C C   . GLY A 1 36  ? 23.03373 -6.39293  8.15609  1.000 43.14726  ? 49  GLY A C   1 
ATOM   256  O O   . GLY A 1 36  ? 23.34091 -5.64381  7.22197  1.000 41.09915  ? 49  GLY A O   1 
ATOM   257  N N   . ARG A 1 37  ? 23.94119 -6.94888  8.95376  1.000 42.06080  ? 50  ARG A N   1 
ATOM   258  C CA  . ARG A 1 37  ? 25.36157 -6.66908  8.80321  1.000 41.10060  ? 50  ARG A CA  1 
ATOM   259  C C   . ARG A 1 37  ? 25.97116 -7.56592  7.73228  1.000 41.73426  ? 50  ARG A C   1 
ATOM   260  O O   . ARG A 1 37  ? 25.80373 -8.78885  7.76200  1.000 42.48380  ? 50  ARG A O   1 
ATOM   261  C CB  . ARG A 1 37  ? 26.08509 -6.86889  10.13469 1.000 40.08405  ? 50  ARG A CB  1 
ATOM   262  C CG  . ARG A 1 37  ? 26.27373 -5.59335  10.94250 1.000 39.94845  ? 50  ARG A CG  1 
ATOM   263  C CD  . ARG A 1 37  ? 25.12789 -5.36016  11.91029 1.000 41.13074  ? 50  ARG A CD  1 
ATOM   264  N NE  . ARG A 1 37  ? 25.43922 -4.30056  12.86218 1.000 38.84432  ? 50  ARG A NE  1 
ATOM   265  C CZ  . ARG A 1 37  ? 25.86054 -4.50739  14.10234 1.000 42.30328  ? 50  ARG A CZ  1 
ATOM   266  N NH1 . ARG A 1 37  ? 26.02716 -5.72955  14.58141 1.000 49.37121  ? 50  ARG A NH1 1 
ATOM   267  N NH2 . ARG A 1 37  ? 26.12290 -3.46199  14.88114 1.000 41.93037  ? 50  ARG A NH2 1 
ATOM   268  N N   . THR A 1 38  ? 26.67138 -6.95189  6.78640  1.000 43.01855  ? 51  THR A N   1 
ATOM   269  C CA  . THR A 1 38  ? 27.41976 -7.67115  5.76692  1.000 40.66596  ? 51  THR A CA  1 
ATOM   270  C C   . THR A 1 38  ? 28.73196 -8.17541  6.35552  1.000 39.80886  ? 51  THR A C   1 
ATOM   271  O O   . THR A 1 38  ? 29.13450 -7.76138  7.44419  1.000 38.26905  ? 51  THR A O   1 
ATOM   272  C CB  . THR A 1 38  ? 27.67017 -6.75196  4.57400  1.000 40.08172  ? 51  THR A CB  1 
ATOM   273  O OG1 . THR A 1 38  ? 28.11901 -5.47447  5.04229  1.000 40.84529  ? 51  THR A OG1 1 
ATOM   274  C CG2 . THR A 1 38  ? 26.39457 -6.57169  3.76566  1.000 43.24157  ? 51  THR A CG2 1 
ATOM   275  N N   . PRO A 1 39  ? 29.42333 -9.09531  5.67095  1.000 42.47431  ? 52  PRO A N   1 
ATOM   276  C CA  . PRO A 1 39  ? 30.76661 -9.46952  6.14216  1.000 40.16829  ? 52  PRO A CA  1 
ATOM   277  C C   . PRO A 1 39  ? 31.70946 -8.28524  6.21008  1.000 38.85697  ? 52  PRO A C   1 
ATOM   278  O O   . PRO A 1 39  ? 32.60547 -8.26267  7.06275  1.000 39.60063  ? 52  PRO A O   1 
ATOM   279  C CB  . PRO A 1 39  ? 31.22808 -10.50870 5.11067  1.000 39.11608  ? 52  PRO A CB  1 
ATOM   280  C CG  . PRO A 1 39  ? 29.97486 -11.03862 4.51909  1.000 41.69204  ? 52  PRO A CG  1 
ATOM   281  C CD  . PRO A 1 39  ? 29.02150 -9.88676  4.49474  1.000 42.83043  ? 52  PRO A CD  1 
ATOM   282  N N   . LEU A 1 40  ? 31.52679 -7.29482  5.33313  1.000 40.12099  ? 53  LEU A N   1 
ATOM   283  C CA  . LEU A 1 40  ? 32.28442 -6.05333  5.44047  1.000 39.27300  ? 53  LEU A CA  1 
ATOM   284  C C   . LEU A 1 40  ? 31.98025 -5.33633  6.75035  1.000 39.74284  ? 53  LEU A C   1 
ATOM   285  O O   . LEU A 1 40  ? 32.89075 -4.81794  7.40731  1.000 40.11799  ? 53  LEU A O   1 
ATOM   286  C CB  . LEU A 1 40  ? 31.97343 -5.15080  4.24650  1.000 41.67305  ? 53  LEU A CB  1 
ATOM   287  C CG  . LEU A 1 40  ? 33.05620 -4.15920  3.81966  1.000 44.84933  ? 53  LEU A CG  1 
ATOM   288  C CD1 . LEU A 1 40  ? 34.24543 -4.88819  3.21883  1.000 48.09791  ? 53  LEU A CD1 1 
ATOM   289  C CD2 . LEU A 1 40  ? 32.49091 -3.15234  2.83345  1.000 46.50081  ? 53  LEU A CD2 1 
ATOM   290  N N   . HIS A 1 41  ? 30.70349 -5.29937  7.14560  1.000 39.89868  ? 54  HIS A N   1 
ATOM   291  C CA  . HIS A 1 41  ? 30.32534 -4.67463  8.41094  1.000 38.83531  ? 54  HIS A CA  1 
ATOM   292  C C   . HIS A 1 41  ? 31.06536 -5.31284  9.57980  1.000 38.49941  ? 54  HIS A C   1 
ATOM   293  O O   . HIS A 1 41  ? 31.71377 -4.62263  10.37646 1.000 39.42962  ? 54  HIS A O   1 
ATOM   294  C CB  . HIS A 1 41  ? 28.81580 -4.79952  8.62389  1.000 39.70742  ? 54  HIS A CB  1 
ATOM   295  C CG  . HIS A 1 41  ? 28.00751 -3.72893  7.96048  1.000 40.67916  ? 54  HIS A CG  1 
ATOM   296  N ND1 . HIS A 1 41  ? 27.26556 -3.95755  6.82170  1.000 39.84507  ? 54  HIS A ND1 1 
ATOM   297  C CD2 . HIS A 1 41  ? 27.80061 -2.43221  8.28998  1.000 43.30496  ? 54  HIS A CD2 1 
ATOM   298  C CE1 . HIS A 1 41  ? 26.64744 -2.84450  6.47047  1.000 41.13543  ? 54  HIS A CE1 1 
ATOM   299  N NE2 . HIS A 1 41  ? 26.95421 -1.90391  7.34551  1.000 43.64829  ? 54  HIS A NE2 1 
ATOM   300  N N   . LEU A 1 42  ? 30.98521 -6.64107  9.68752  1.000 39.23829  ? 55  LEU A N   1 
ATOM   301  C CA  . LEU A 1 42  ? 31.60918 -7.34326  10.80324 1.000 39.64468  ? 55  LEU A CA  1 
ATOM   302  C C   . LEU A 1 42  ? 33.12668 -7.22128  10.75866 1.000 40.31510  ? 55  LEU A C   1 
ATOM   303  O O   . LEU A 1 42  ? 33.77171 -7.05675  11.80097 1.000 42.82231  ? 55  LEU A O   1 
ATOM   304  C CB  . LEU A 1 42  ? 31.18329 -8.81086  10.79496 1.000 43.53291  ? 55  LEU A CB  1 
ATOM   305  C CG  . LEU A 1 42  ? 29.67922 -9.06258  10.65973 1.000 41.85410  ? 55  LEU A CG  1 
ATOM   306  C CD1 . LEU A 1 42  ? 29.38692 -10.55022 10.53187 1.000 44.97584  ? 55  LEU A CD1 1 
ATOM   307  C CD2 . LEU A 1 42  ? 28.92625 -8.46329  11.83746 1.000 45.31385  ? 55  LEU A CD2 1 
ATOM   308  N N   . ALA A 1 43  ? 33.71453 -7.30716  9.56252  1.000 38.94741  ? 56  ALA A N   1 
ATOM   309  C CA  . ALA A 1 43  ? 35.16467 -7.20442  9.44090  1.000 40.54856  ? 56  ALA A CA  1 
ATOM   310  C C   . ALA A 1 43  ? 35.66068 -5.82592  9.85717  1.000 39.77940  ? 56  ALA A C   1 
ATOM   311  O O   . ALA A 1 43  ? 36.67921 -5.70826  10.54873 1.000 39.43767  ? 56  ALA A O   1 
ATOM   312  C CB  . ALA A 1 43  ? 35.59353 -7.52134  8.00970  1.000 41.55807  ? 56  ALA A CB  1 
ATOM   313  N N   . ALA A 1 44  ? 34.95780 -4.76829  9.44382  1.000 38.91649  ? 57  ALA A N   1 
ATOM   314  C CA  . ALA A 1 44  ? 35.34101 -3.42419  9.85979  1.000 40.00448  ? 57  ALA A CA  1 
ATOM   315  C C   . ALA A 1 44  ? 35.12758 -3.22929  11.35487 1.000 39.85691  ? 57  ALA A C   1 
ATOM   316  O O   . ALA A 1 44  ? 35.90080 -2.52103  12.01034 1.000 39.46198  ? 57  ALA A O   1 
ATOM   317  C CB  . ALA A 1 44  ? 34.55642 -2.38334  9.06225  1.000 40.32244  ? 57  ALA A CB  1 
ATOM   318  N N   . GLN A 1 45  ? 34.08150 -3.84748  11.91025 1.000 40.09637  ? 58  GLN A N   1 
ATOM   319  C CA  . GLN A 1 45  ? 33.80851 -3.70644  13.33737 1.000 43.63717  ? 58  GLN A CA  1 
ATOM   320  C C   . GLN A 1 45  ? 34.91647 -4.32188  14.18582 1.000 43.81260  ? 58  GLN A C   1 
ATOM   321  O O   . GLN A 1 45  ? 35.30818 -3.75440  15.21245 1.000 45.92591  ? 58  GLN A O   1 
ATOM   322  C CB  . GLN A 1 45  ? 32.45940 -4.34036  13.67627 1.000 46.04639  ? 58  GLN A CB  1 
ATOM   323  C CG  . GLN A 1 45  ? 31.80224 -3.77507  14.92506 1.000 50.58690  ? 58  GLN A CG  1 
ATOM   324  C CD  . GLN A 1 45  ? 30.88905 -4.77449  15.60874 1.000 53.54868  ? 58  GLN A CD  1 
ATOM   325  O OE1 . GLN A 1 45  ? 30.36871 -5.69272  14.97504 1.000 52.32103  ? 58  GLN A OE1 1 
ATOM   326  N NE2 . GLN A 1 45  ? 30.68803 -4.59862  16.90968 1.000 57.78714  ? 58  GLN A NE2 1 
ATOM   327  N N   . ARG A 1 46  ? 35.43465 -5.47953  13.77613 1.000 43.96880  ? 59  ARG A N   1 
ATOM   328  C CA  . ARG A 1 46  ? 36.40011 -6.22862  14.57053 1.000 45.29067  ? 59  ARG A CA  1 
ATOM   329  C C   . ARG A 1 46  ? 37.84672 -5.93079  14.19496 1.000 44.68515  ? 59  ARG A C   1 
ATOM   330  O O   . ARG A 1 46  ? 38.75525 -6.59741  14.70094 1.000 44.55345  ? 59  ARG A O   1 
ATOM   331  C CB  . ARG A 1 46  ? 36.12739 -7.72963  14.45393 1.000 45.20190  ? 59  ARG A CB  1 
ATOM   332  C CG  . ARG A 1 46  ? 34.96337 -8.20298  15.30848 1.000 46.37753  ? 59  ARG A CG  1 
ATOM   333  C CD  . ARG A 1 46  ? 33.97036 -9.01683  14.50150 1.000 47.52102  ? 59  ARG A CD  1 
ATOM   334  N NE  . ARG A 1 46  ? 32.80759 -9.38724  15.29863 1.000 53.98078  ? 59  ARG A NE  1 
ATOM   335  C CZ  . ARG A 1 46  ? 31.64004 -8.76119  15.25217 1.000 52.35004  ? 59  ARG A CZ  1 
ATOM   336  N NH1 . ARG A 1 46  ? 31.44121 -7.73025  14.44763 1.000 48.69030  ? 59  ARG A NH1 1 
ATOM   337  N NH2 . ARG A 1 46  ? 30.64775 -9.17929  16.03318 1.000 55.82536  ? 59  ARG A NH2 1 
ATOM   338  N N   . GLY A 1 47  ? 38.08298 -4.94855  13.33267 1.000 42.83244  ? 60  GLY A N   1 
ATOM   339  C CA  . GLY A 1 47  ? 39.44290 -4.59404  12.96454 1.000 43.53117  ? 60  GLY A CA  1 
ATOM   340  C C   . GLY A 1 47  ? 40.17497 -5.63800  12.14818 1.000 43.00846  ? 60  GLY A C   1 
ATOM   341  O O   . GLY A 1 47  ? 41.36167 -5.88946  12.39347 1.000 41.52663  ? 60  GLY A O   1 
ATOM   342  N N   . HIS A 1 48  ? 39.49691 -6.25605  11.18257 1.000 43.13056  ? 61  HIS A N   1 
ATOM   343  C CA  . HIS A 1 48  ? 40.09528 -7.27546  10.31957 1.000 42.45706  ? 61  HIS A CA  1 
ATOM   344  C C   . HIS A 1 48  ? 40.43526 -6.60708  8.99282  1.000 42.52890  ? 61  HIS A C   1 
ATOM   345  O O   . HIS A 1 48  ? 39.60925 -6.52691  8.08282  1.000 41.49659  ? 61  HIS A O   1 
ATOM   346  C CB  . HIS A 1 48  ? 39.15329 -8.45782  10.14120 1.000 42.67200  ? 61  HIS A CB  1 
ATOM   347  C CG  . HIS A 1 48  ? 38.91000 -9.22234  11.40297 1.000 43.63774  ? 61  HIS A CG  1 
ATOM   348  N ND1 . HIS A 1 48  ? 37.74486 -9.91732  11.64021 1.000 47.21355  ? 61  HIS A ND1 1 
ATOM   349  C CD2 . HIS A 1 48  ? 39.68282 -9.39430  12.50124 1.000 44.17254  ? 61  HIS A CD2 1 
ATOM   350  C CE1 . HIS A 1 48  ? 37.80965 -10.48595 12.83140 1.000 50.35105  ? 61  HIS A CE1 1 
ATOM   351  N NE2 . HIS A 1 48  ? 38.97580 -10.18586 13.37315 1.000 50.28710  ? 61  HIS A NE2 1 
ATOM   352  N N   . LEU A 1 49  ? 41.67420 -6.12212  8.89389  1.000 46.04811  ? 62  LEU A N   1 
ATOM   353  C CA  . LEU A 1 49  ? 42.06688 -5.27961  7.76924  1.000 44.91728  ? 62  LEU A CA  1 
ATOM   354  C C   . LEU A 1 49  ? 42.08863 -6.07143  6.46744  1.000 47.49067  ? 62  LEU A C   1 
ATOM   355  O O   . LEU A 1 49  ? 41.54788 -5.62810  5.44588  1.000 48.25872  ? 62  LEU A O   1 
ATOM   356  C CB  . LEU A 1 49  ? 43.43972 -4.66763  8.04624  1.000 47.56993  ? 62  LEU A CB  1 
ATOM   357  C CG  . LEU A 1 49  ? 43.70718 -3.21123  7.65597  1.000 51.90518  ? 62  LEU A CG  1 
ATOM   358  C CD1 . LEU A 1 49  ? 45.06565 -2.76724  8.20495  1.000 49.60277  ? 62  LEU A CD1 1 
ATOM   359  C CD2 . LEU A 1 49  ? 43.57184 -2.94131  6.15513  1.000 50.51464  ? 62  LEU A CD2 1 
ATOM   360  N N   . GLU A 1 50  ? 42.71215 -7.25148  6.49001  1.000 48.28628  ? 63  GLU A N   1 
ATOM   361  C CA  . GLU A 1 50  ? 42.85998 -8.04465  5.27417  1.000 46.32130  ? 63  GLU A CA  1 
ATOM   362  C C   . GLU A 1 50  ? 41.51589 -8.55615  4.77335  1.000 45.39396  ? 63  GLU A C   1 
ATOM   363  O O   . GLU A 1 50  ? 41.27999 -8.60933  3.56074  1.000 47.04815  ? 63  GLU A O   1 
ATOM   364  C CB  . GLU A 1 50  ? 43.81251 -9.21019  5.52423  1.000 45.42667  ? 63  GLU A CB  1 
ATOM   365  C CG  . GLU A 1 50  ? 45.17660 -8.79672  6.03724  1.000 52.52760  ? 63  GLU A CG  1 
ATOM   366  C CD  . GLU A 1 50  ? 45.26641 -8.87299  7.54660  1.000 54.20013  ? 63  GLU A CD  1 
ATOM   367  O OE1 . GLU A 1 50  ? 45.32673 -10.00144 8.07953  1.000 54.55278  ? 63  GLU A OE1 1 
ATOM   368  O OE2 . GLU A 1 50  ? 45.28415 -7.80666  8.19819  1.000 51.51909  ? 63  GLU A OE2 1 
ATOM   369  N N   . ILE A 1 51  ? 40.63043 -8.95732  5.68763  1.000 45.63715  ? 64  ILE A N   1 
ATOM   370  C CA  . ILE A 1 51  ? 39.30100 -9.40020  5.27902  1.000 45.58290  ? 64  ILE A CA  1 
ATOM   371  C C   . ILE A 1 51  ? 38.52316 -8.24392  4.66272  1.000 42.70605  ? 64  ILE A C   1 
ATOM   372  O O   . ILE A 1 51  ? 37.82327 -8.41552  3.65752  1.000 40.39404  ? 64  ILE A O   1 
ATOM   373  C CB  . ILE A 1 51  ? 38.55358 -10.02820 6.46973  1.000 44.18077  ? 64  ILE A CB  1 
ATOM   374  C CG1 . ILE A 1 51  ? 39.17717 -11.37309 6.83661  1.000 44.65251  ? 64  ILE A CG1 1 
ATOM   375  C CG2 . ILE A 1 51  ? 37.08541 -10.22610 6.14545  1.000 40.97933  ? 64  ILE A CG2 1 
ATOM   376  C CD1 . ILE A 1 51  ? 38.70894 -11.90478 8.16213  1.000 47.13290  ? 64  ILE A CD1 1 
ATOM   377  N N   . VAL A 1 52  ? 38.64121 -7.04849  5.24558  1.000 41.67234  ? 65  VAL A N   1 
ATOM   378  C CA  . VAL A 1 52  ? 38.01939 -5.86424  4.65703  1.000 44.12064  ? 65  VAL A CA  1 
ATOM   379  C C   . VAL A 1 52  ? 38.53144 -5.64922  3.23695  1.000 47.72724  ? 65  VAL A C   1 
ATOM   380  O O   . VAL A 1 52  ? 37.74763 -5.45258  2.29696  1.000 48.56889  ? 65  VAL A O   1 
ATOM   381  C CB  . VAL A 1 52  ? 38.27559 -4.63050  5.54246  1.000 43.95841  ? 65  VAL A CB  1 
ATOM   382  C CG1 . VAL A 1 52  ? 38.17542 -3.35264  4.72603  1.000 47.29035  ? 65  VAL A CG1 1 
ATOM   383  C CG2 . VAL A 1 52  ? 37.30319 -4.59787  6.70801  1.000 44.43783  ? 65  VAL A CG2 1 
ATOM   384  N N   . GLU A 1 53  ? 39.85706 -5.70177  3.05925  1.000 51.54634  ? 66  GLU A N   1 
ATOM   385  C CA  . GLU A 1 53  ? 40.43849 -5.51303  1.73212  1.000 50.41191  ? 66  GLU A CA  1 
ATOM   386  C C   . GLU A 1 53  ? 39.90133 -6.53549  0.74388  1.000 50.29035  ? 66  GLU A C   1 
ATOM   387  O O   . GLU A 1 53  ? 39.45590 -6.18220  -0.35287 1.000 48.56852  ? 66  GLU A O   1 
ATOM   388  C CB  . GLU A 1 53  ? 41.96039 -5.63070  1.77859  1.000 49.22395  ? 66  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 53  ? 42.73054 -4.49825  2.40323  1.000 50.23647  ? 66  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 53  ? 44.10719 -4.96444  2.83119  1.000 53.18229  ? 66  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 53  ? 44.50477 -6.06624  2.39364  1.000 55.21105  ? 66  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 53  ? 44.79839 -4.23274  3.57001  1.000 53.43398  ? 66  GLU A OE2 1 
ATOM   393  N N   . VAL A 1 54  ? 39.95997 -7.81741  1.11142  1.000 45.95679  ? 67  VAL A N   1 
ATOM   394  C CA  . VAL A 1 54  ? 39.61693 -8.87930  0.17298  1.000 45.06138  ? 67  VAL A CA  1 
ATOM   395  C C   . VAL A 1 54  ? 38.12652 -8.86968  -0.14356 1.000 46.05657  ? 67  VAL A C   1 
ATOM   396  O O   . VAL A 1 54  ? 37.72414 -9.21604  -1.26146 1.000 46.59917  ? 67  VAL A O   1 
ATOM   397  C CB  . VAL A 1 54  ? 40.09550 -10.24377 0.71019  1.000 42.29232  ? 67  VAL A CB  1 
ATOM   398  C CG1 . VAL A 1 54  ? 39.15847 -10.78148 1.77552  1.000 43.14427  ? 67  VAL A CG1 1 
ATOM   399  C CG2 . VAL A 1 54  ? 40.24631 -11.23783 -0.43094 1.000 47.39283  ? 67  VAL A CG2 1 
ATOM   400  N N   . LEU A 1 55  ? 37.28155 -8.47550  0.81466  1.000 47.51098  ? 68  LEU A N   1 
ATOM   401  C CA  . LEU A 1 55  ? 35.86316 -8.33227  0.51375  1.000 45.40944  ? 68  LEU A CA  1 
ATOM   402  C C   . LEU A 1 55  ? 35.62535 -7.17864  -0.44835 1.000 48.36606  ? 68  LEU A C   1 
ATOM   403  O O   . LEU A 1 55  ? 34.85127 -7.31355  -1.40310 1.000 46.17673  ? 68  LEU A O   1 
ATOM   404  C CB  . LEU A 1 55  ? 35.05933 -8.13177  1.79678  1.000 47.05512  ? 68  LEU A CB  1 
ATOM   405  C CG  . LEU A 1 55  ? 34.80527 -9.37946  2.64452  1.000 46.97861  ? 68  LEU A CG  1 
ATOM   406  C CD1 . LEU A 1 55  ? 34.47177 -8.99012  4.07813  1.000 39.96749  ? 68  LEU A CD1 1 
ATOM   407  C CD2 . LEU A 1 55  ? 33.72113 -10.26336 2.04259  1.000 44.69745  ? 68  LEU A CD2 1 
ATOM   408  N N   . LEU A 1 56  ? 36.29115 -6.03972  -0.22440 1.000 49.09690  ? 69  LEU A N   1 
ATOM   409  C CA  . LEU A 1 56  ? 36.14552 -4.92062  -1.15094 1.000 49.07405  ? 69  LEU A CA  1 
ATOM   410  C C   . LEU A 1 56  ? 36.62252 -5.30035  -2.54707 1.000 50.32280  ? 69  LEU A C   1 
ATOM   411  O O   . LEU A 1 56  ? 36.03491 -4.87890  -3.55024 1.000 53.27029  ? 69  LEU A O   1 
ATOM   412  C CB  . LEU A 1 56  ? 36.90848 -3.69783  -0.63842 1.000 51.36895  ? 69  LEU A CB  1 
ATOM   413  C CG  . LEU A 1 56  ? 36.44582 -3.05195  0.66996  1.000 51.55016  ? 69  LEU A CG  1 
ATOM   414  C CD1 . LEU A 1 56  ? 37.58116 -2.27058  1.31162  1.000 52.72560  ? 69  LEU A CD1 1 
ATOM   415  C CD2 . LEU A 1 56  ? 35.24348 -2.15321  0.42922  1.000 54.85351  ? 69  LEU A CD2 1 
ATOM   416  N N   . LYS A 1 57  ? 37.68576 -6.10161  -2.63034 1.000 48.66252  ? 70  LYS A N   1 
ATOM   417  C CA  . LYS A 1 57  ? 38.21092 -6.52284  -3.92263 1.000 50.42791  ? 70  LYS A CA  1 
ATOM   418  C C   . LYS A 1 57  ? 37.32441 -7.56157  -4.59475 1.000 49.24847  ? 70  LYS A C   1 
ATOM   419  O O   . LYS A 1 57  ? 37.42113 -7.74778  -5.81238 1.000 51.72360  ? 70  LYS A O   1 
ATOM   420  C CB  . LYS A 1 57  ? 39.62691 -7.06867  -3.74879 1.000 49.60218  ? 70  LYS A CB  1 
ATOM   421  C CG  . LYS A 1 57  ? 40.66563 -5.98493  -3.55833 1.000 52.36807  ? 70  LYS A CG  1 
ATOM   422  C CD  . LYS A 1 57  ? 42.07075 -6.54338  -3.60101 1.000 55.09766  ? 70  LYS A CD  1 
ATOM   423  C CE  . LYS A 1 57  ? 42.94891 -5.82051  -2.59897 1.000 57.91592  ? 70  LYS A CE  1 
ATOM   424  N NZ  . LYS A 1 57  ? 43.64815 -6.76872  -1.68488 1.000 55.30689  ? 70  LYS A NZ  1 
ATOM   425  N N   . ALA A 1 58  ? 36.46650 -8.23562  -3.83483 1.000 49.00000  ? 71  ALA A N   1 
ATOM   426  C CA  . ALA A 1 58  ? 35.53283 -9.20721  -4.38391 1.000 48.95520  ? 71  ALA A CA  1 
ATOM   427  C C   . ALA A 1 58  ? 34.19773 -8.58549  -4.76793 1.000 49.14783  ? 71  ALA A C   1 
ATOM   428  O O   . ALA A 1 58  ? 33.28957 -9.31099  -5.18583 1.000 49.59745  ? 71  ALA A O   1 
ATOM   429  C CB  . ALA A 1 58  ? 35.30539 -10.34643 -3.38405 1.000 50.16812  ? 71  ALA A CB  1 
ATOM   430  N N   . GLY A 1 59  ? 34.05903 -7.27126  -4.63866 1.000 48.97526  ? 72  GLY A N   1 
ATOM   431  C CA  . GLY A 1 59  ? 32.83919 -6.58809  -5.00436 1.000 47.67500  ? 72  GLY A CA  1 
ATOM   432  C C   . GLY A 1 59  ? 31.87505 -6.30171  -3.87496 1.000 49.62101  ? 72  GLY A C   1 
ATOM   433  O O   . GLY A 1 59  ? 30.69826 -6.04109  -4.14982 1.000 49.33493  ? 72  GLY A O   1 
ATOM   434  N N   . ALA A 1 60  ? 32.32512 -6.35083  -2.62240 1.000 49.30105  ? 73  ALA A N   1 
ATOM   435  C CA  . ALA A 1 60  ? 31.43673 -6.07085  -1.50250 1.000 48.16083  ? 73  ALA A CA  1 
ATOM   436  C C   . ALA A 1 60  ? 30.93739 -4.63369  -1.56151 1.000 48.65305  ? 73  ALA A C   1 
ATOM   437  O O   . ALA A 1 60  ? 31.68818 -3.70824  -1.88250 1.000 49.10629  ? 73  ALA A O   1 
ATOM   438  C CB  . ALA A 1 60  ? 32.15097 -6.32130  -0.17435 1.000 47.20901  ? 73  ALA A CB  1 
ATOM   439  N N   . ASP A 1 61  ? 29.65676 -4.45249  -1.24852 1.000 50.76959  ? 74  ASP A N   1 
ATOM   440  C CA  . ASP A 1 61  ? 29.04501 -3.12841  -1.26271 1.000 50.51563  ? 74  ASP A CA  1 
ATOM   441  C C   . ASP A 1 61  ? 29.59819 -2.31103  -0.10232 1.000 52.12018  ? 74  ASP A C   1 
ATOM   442  O O   . ASP A 1 61  ? 29.25413 -2.55304  1.05917  1.000 53.53585  ? 74  ASP A O   1 
ATOM   443  C CB  . ASP A 1 61  ? 27.52630 -3.24952  -1.18047 1.000 50.33263  ? 74  ASP A CB  1 
ATOM   444  C CG  . ASP A 1 61  ? 26.82475 -1.91196  -1.31769 1.000 53.86117  ? 74  ASP A CG  1 
ATOM   445  O OD1 . ASP A 1 61  ? 27.46109 -0.94868  -1.79538 1.000 54.26860  ? 74  ASP A OD1 1 
ATOM   446  O OD2 . ASP A 1 61  ? 25.63254 -1.82580  -0.95533 1.000 56.62739  ? 74  ASP A OD2 1 
ATOM   447  N N   . VAL A 1 62  ? 30.46570 -1.34638  -0.41629 1.000 50.89616  ? 75  VAL A N   1 
ATOM   448  C CA  . VAL A 1 62  ? 31.07962 -0.53073  0.62554  1.000 48.97049  ? 75  VAL A CA  1 
ATOM   449  C C   . VAL A 1 62  ? 30.04202 0.35720   1.30308  1.000 49.91609  ? 75  VAL A C   1 
ATOM   450  O O   . VAL A 1 62  ? 30.14805 0.64463   2.50222  1.000 49.07467  ? 75  VAL A O   1 
ATOM   451  C CB  . VAL A 1 62  ? 32.24656 0.28686   0.03678  1.000 49.75786  ? 75  VAL A CB  1 
ATOM   452  C CG1 . VAL A 1 62  ? 31.75803 1.22534   -1.06080 1.000 50.55264  ? 75  VAL A CG1 1 
ATOM   453  C CG2 . VAL A 1 62  ? 32.97969 1.04957   1.13173  1.000 47.62529  ? 75  VAL A CG2 1 
ATOM   454  N N   . ASN A 1 63  ? 29.02158 0.79077   0.56629  1.000 52.58768  ? 76  ASN A N   1 
ATOM   455  C CA  . ASN A 1 63  ? 28.00099 1.68824   1.08937  1.000 50.91440  ? 76  ASN A CA  1 
ATOM   456  C C   . ASN A 1 63  ? 26.78420 0.95325   1.64180  1.000 48.67884  ? 76  ASN A C   1 
ATOM   457  O O   . ASN A 1 63  ? 25.78187 1.59930   1.96342  1.000 51.87677  ? 76  ASN A O   1 
ATOM   458  C CB  . ASN A 1 63  ? 27.56243 2.67452   0.00337  1.000 55.86849  ? 76  ASN A CB  1 
ATOM   459  C CG  . ASN A 1 63  ? 28.70353 3.54625   -0.48789 1.000 56.48530  ? 76  ASN A CG  1 
ATOM   460  O OD1 . ASN A 1 63  ? 29.33888 4.25547   0.29283  1.000 55.92996  ? 76  ASN A OD1 1 
ATOM   461  N ND2 . ASN A 1 63  ? 28.96835 3.49772   -1.78889 1.000 58.71135  ? 76  ASN A ND2 1 
ATOM   462  N N   . ALA A 1 64  ? 26.84331 -0.37151  1.75216  1.000 48.98764  ? 77  ALA A N   1 
ATOM   463  C CA  . ALA A 1 64  ? 25.72829 -1.12666  2.30688  1.000 51.59638  ? 77  ALA A CA  1 
ATOM   464  C C   . ALA A 1 64  ? 25.50502 -0.75252  3.76701  1.000 48.64990  ? 77  ALA A C   1 
ATOM   465  O O   . ALA A 1 64  ? 26.45535 -0.52754  4.51960  1.000 46.43773  ? 77  ALA A O   1 
ATOM   466  C CB  . ALA A 1 64  ? 25.98630 -2.62782  2.18105  1.000 49.39608  ? 77  ALA A CB  1 
ATOM   467  N N   . HIS A 1 65  ? 24.23825 -0.67773  4.16461  1.000 47.37567  ? 78  HIS A N   1 
ATOM   468  C CA  . HIS A 1 65  ? 23.86325 -0.29674  5.51744  1.000 48.10256  ? 78  HIS A CA  1 
ATOM   469  C C   . HIS A 1 65  ? 23.09709 -1.42904  6.18719  1.000 47.24133  ? 78  HIS A C   1 
ATOM   470  O O   . HIS A 1 65  ? 22.36809 -2.17992  5.53227  1.000 46.78812  ? 78  HIS A O   1 
ATOM   471  C CB  . HIS A 1 65  ? 23.01081 0.97867   5.52017  1.000 48.19455  ? 78  HIS A CB  1 
ATOM   472  C CG  . HIS A 1 65  ? 21.84906 0.92983   4.57755  1.000 47.71264  ? 78  HIS A CG  1 
ATOM   473  N ND1 . HIS A 1 65  ? 20.62543 0.40362   4.93157  1.000 47.72471  ? 78  HIS A ND1 1 
ATOM   474  C CD2 . HIS A 1 65  ? 21.72495 1.33939   3.29271  1.000 52.92209  ? 78  HIS A CD2 1 
ATOM   475  C CE1 . HIS A 1 65  ? 19.79698 0.49216   3.90616  1.000 50.80084  ? 78  HIS A CE1 1 
ATOM   476  N NE2 . HIS A 1 65  ? 20.43954 1.05594   2.89915  1.000 55.04085  ? 78  HIS A NE2 1 
ATOM   477  N N   . ASP A 1 66  ? 23.27017 -1.54594  7.50138  1.000 43.76662  ? 79  ASP A N   1 
ATOM   478  C CA  . ASP A 1 66  ? 22.55918 -2.54983  8.28176  1.000 43.43265  ? 79  ASP A CA  1 
ATOM   479  C C   . ASP A 1 66  ? 21.14982 -2.04746  8.59744  1.000 42.60530  ? 79  ASP A C   1 
ATOM   480  O O   . ASP A 1 66  ? 20.67354 -1.05641  8.03707  1.000 42.74413  ? 79  ASP A O   1 
ATOM   481  C CB  . ASP A 1 66  ? 23.34648 -2.90403  9.54321  1.000 43.26273  ? 79  ASP A CB  1 
ATOM   482  C CG  . ASP A 1 66  ? 23.68691 -1.68802  10.39198 1.000 41.68414  ? 79  ASP A CG  1 
ATOM   483  O OD1 . ASP A 1 66  ? 23.04259 -0.63092  10.22971 1.000 39.87629  ? 79  ASP A OD1 1 
ATOM   484  O OD2 . ASP A 1 66  ? 24.60560 -1.79410  11.23173 1.000 41.20609  ? 79  ASP A OD2 1 
ATOM   485  N N   . GLN A 1 67  ? 20.46137 -2.73881  9.50844  1.000 44.62068  ? 80  GLN A N   1 
ATOM   486  C CA  . GLN A 1 67  ? 19.11143 -2.33918  9.88718  1.000 40.86919  ? 80  GLN A CA  1 
ATOM   487  C C   . GLN A 1 67  ? 19.08600 -1.02198  10.65252 1.000 41.38223  ? 80  GLN A C   1 
ATOM   488  O O   . GLN A 1 67  ? 18.04073 -0.36391  10.69201 1.000 40.48375  ? 80  GLN A O   1 
ATOM   489  C CB  . GLN A 1 67  ? 18.45353 -3.44325  10.71531 1.000 39.94613  ? 80  GLN A CB  1 
ATOM   490  C CG  . GLN A 1 67  ? 18.98807 -3.56574  12.13044 1.000 43.31398  ? 80  GLN A CG  1 
ATOM   491  C CD  . GLN A 1 67  ? 18.43768 -4.77815  12.85254 1.000 43.52346  ? 80  GLN A CD  1 
ATOM   492  O OE1 . GLN A 1 67  ? 17.56674 -5.47904  12.33647 1.000 43.70597  ? 80  GLN A OE1 1 
ATOM   493  N NE2 . GLN A 1 67  ? 18.94157 -5.03108  14.05474 1.000 42.99198  ? 80  GLN A NE2 1 
ATOM   494  N N   . TYR A 1 68  ? 20.20410 -0.62178  11.25386 1.000 39.70233  ? 81  TYR A N   1 
ATOM   495  C CA  . TYR A 1 68  ? 20.30835 0.65887   11.93789 1.000 37.94083  ? 81  TYR A CA  1 
ATOM   496  C C   . TYR A 1 68  ? 20.75882 1.78017   11.01212 1.000 38.33791  ? 81  TYR A C   1 
ATOM   497  O O   . TYR A 1 68  ? 20.98794 2.89979   11.47997 1.000 39.81201  ? 81  TYR A O   1 
ATOM   498  C CB  . TYR A 1 68  ? 21.27049 0.55611   13.12489 1.000 38.53036  ? 81  TYR A CB  1 
ATOM   499  C CG  . TYR A 1 68  ? 21.08247 -0.67615  13.97907 1.000 42.82184  ? 81  TYR A CG  1 
ATOM   500  C CD1 . TYR A 1 68  ? 20.03041 -0.76451  14.88108 1.000 44.17963  ? 81  TYR A CD1 1 
ATOM   501  C CD2 . TYR A 1 68  ? 21.96451 -1.74550  13.89419 1.000 43.36991  ? 81  TYR A CD2 1 
ATOM   502  C CE1 . TYR A 1 68  ? 19.85584 -1.88661  15.66834 1.000 44.82367  ? 81  TYR A CE1 1 
ATOM   503  C CE2 . TYR A 1 68  ? 21.79892 -2.87198  14.67822 1.000 44.11354  ? 81  TYR A CE2 1 
ATOM   504  C CZ  . TYR A 1 68  ? 20.74366 -2.93686  15.56343 1.000 47.04567  ? 81  TYR A CZ  1 
ATOM   505  O OH  . TYR A 1 68  ? 20.57535 -4.05703  16.34483 1.000 47.67892  ? 81  TYR A OH  1 
ATOM   506  N N   . GLY A 1 69  ? 20.89166 1.50732   9.71664  1.000 38.92659  ? 82  GLY A N   1 
ATOM   507  C CA  . GLY A 1 69  ? 21.41167 2.49792   8.79893  1.000 38.54775  ? 82  GLY A CA  1 
ATOM   508  C C   . GLY A 1 69  ? 22.90352 2.70245   8.88476  1.000 39.51506  ? 82  GLY A C   1 
ATOM   509  O O   . GLY A 1 69  ? 23.40834 3.71499   8.39067  1.000 41.78021  ? 82  GLY A O   1 
ATOM   510  N N   . TRP A 1 70  ? 23.62764 1.77045   9.49863  1.000 39.25392  ? 83  TRP A N   1 
ATOM   511  C CA  . TRP A 1 70  ? 25.06055 1.91543   9.71588  1.000 39.44736  ? 83  TRP A CA  1 
ATOM   512  C C   . TRP A 1 70  ? 25.82695 1.20571   8.60613  1.000 41.23250  ? 83  TRP A C   1 
ATOM   513  O O   . TRP A 1 70  ? 25.65977 -0.00127  8.39781  1.000 41.85343  ? 83  TRP A O   1 
ATOM   514  C CB  . TRP A 1 70  ? 25.45757 1.36025   11.08337 1.000 39.85284  ? 83  TRP A CB  1 
ATOM   515  C CG  . TRP A 1 70  ? 25.17776 2.30114   12.21355 1.000 41.67059  ? 83  TRP A CG  1 
ATOM   516  C CD1 . TRP A 1 70  ? 24.08757 3.10816   12.35678 1.000 40.68361  ? 83  TRP A CD1 1 
ATOM   517  C CD2 . TRP A 1 70  ? 26.00458 2.53620   13.36000 1.000 41.92952  ? 83  TRP A CD2 1 
ATOM   518  N NE1 . TRP A 1 70  ? 24.18438 3.83199   13.52014 1.000 43.14165  ? 83  TRP A NE1 1 
ATOM   519  C CE2 . TRP A 1 70  ? 25.35200 3.49886   14.15456 1.000 43.53977  ? 83  TRP A CE2 1 
ATOM   520  C CE3 . TRP A 1 70  ? 27.23302 2.02629   13.79102 1.000 44.27395  ? 83  TRP A CE3 1 
ATOM   521  C CZ2 . TRP A 1 70  ? 25.88665 3.96367   15.35440 1.000 47.03576  ? 83  TRP A CZ2 1 
ATOM   522  C CZ3 . TRP A 1 70  ? 27.76100 2.48606   14.98409 1.000 47.01329  ? 83  TRP A CZ3 1 
ATOM   523  C CH2 . TRP A 1 70  ? 27.08774 3.44442   15.75261 1.000 49.00818  ? 83  TRP A CH2 1 
ATOM   524  N N   . THR A 1 71  ? 26.65889 1.96058   7.89926  1.000 42.91664  ? 84  THR A N   1 
ATOM   525  C CA  . THR A 1 71  ? 27.57008 1.42066   6.90392  1.000 42.14147  ? 84  THR A CA  1 
ATOM   526  C C   . THR A 1 71  ? 28.80371 0.85449   7.59621  1.000 41.23791  ? 84  THR A C   1 
ATOM   527  O O   . THR A 1 71  ? 29.02191 1.08859   8.78609  1.000 41.78829  ? 84  THR A O   1 
ATOM   528  C CB  . THR A 1 71  ? 27.94810 2.51736   5.91092  1.000 43.59391  ? 84  THR A CB  1 
ATOM   529  O OG1 . THR A 1 71  ? 28.48620 3.64122   6.61971  1.000 42.80113  ? 84  THR A OG1 1 
ATOM   530  C CG2 . THR A 1 71  ? 26.72648 2.96194   5.12229  1.000 44.14448  ? 84  THR A CG2 1 
ATOM   531  N N   . PRO A 1 72  ? 29.62802 0.07722   6.88358  1.000 41.84546  ? 85  PRO A N   1 
ATOM   532  C CA  . PRO A 1 72  ? 30.89608 -0.36090  7.48899  1.000 41.33784  ? 85  PRO A CA  1 
ATOM   533  C C   . PRO A 1 72  ? 31.78135 0.79497   7.91404  1.000 43.89267  ? 85  PRO A C   1 
ATOM   534  O O   . PRO A 1 72  ? 32.58660 0.63807   8.83947  1.000 46.49833  ? 85  PRO A O   1 
ATOM   535  C CB  . PRO A 1 72  ? 31.54409 -1.19534  6.37645  1.000 44.39486  ? 85  PRO A CB  1 
ATOM   536  C CG  . PRO A 1 72  ? 30.39739 -1.69612  5.57883  1.000 43.08875  ? 85  PRO A CG  1 
ATOM   537  C CD  . PRO A 1 72  ? 29.38479 -0.58827  5.59113  1.000 42.66878  ? 85  PRO A CD  1 
ATOM   538  N N   . LEU A 1 73  ? 31.66022 1.95358   7.26183  1.000 44.86035  ? 86  LEU A N   1 
ATOM   539  C CA  . LEU A 1 73  ? 32.38240 3.13687   7.71620  1.000 45.10544  ? 86  LEU A CA  1 
ATOM   540  C C   . LEU A 1 73  ? 31.92062 3.55685   9.10811  1.000 45.70045  ? 86  LEU A C   1 
ATOM   541  O O   . LEU A 1 73  ? 32.74253 3.90546   9.96676  1.000 47.86831  ? 86  LEU A O   1 
ATOM   542  C CB  . LEU A 1 73  ? 32.19240 4.27449   6.71282  1.000 46.09076  ? 86  LEU A CB  1 
ATOM   543  C CG  . LEU A 1 73  ? 33.15759 5.45633   6.79558  1.000 50.95625  ? 86  LEU A CG  1 
ATOM   544  C CD1 . LEU A 1 73  ? 34.59815 4.96517   6.78883  1.000 51.01702  ? 86  LEU A CD1 1 
ATOM   545  C CD2 . LEU A 1 73  ? 32.91230 6.43097   5.65644  1.000 54.40793  ? 86  LEU A CD2 1 
ATOM   546  N N   . HIS A 1 74  ? 30.60537 3.52356   9.34893  1.000 45.66765  ? 87  HIS A N   1 
ATOM   547  C CA  . HIS A 1 74  ? 30.07188 3.81239   10.67748 1.000 43.96204  ? 87  HIS A CA  1 
ATOM   548  C C   . HIS A 1 74  ? 30.68306 2.89033   11.72379 1.000 45.67150  ? 87  HIS A C   1 
ATOM   549  O O   . HIS A 1 74  ? 31.15221 3.34075   12.77497 1.000 48.43386  ? 87  HIS A O   1 
ATOM   550  C CB  . HIS A 1 74  ? 28.54841 3.65677   10.68118 1.000 43.19749  ? 87  HIS A CB  1 
ATOM   551  C CG  . HIS A 1 74  ? 27.80720 4.83028   10.12030 1.000 43.52098  ? 87  HIS A CG  1 
ATOM   552  N ND1 . HIS A 1 74  ? 27.24421 4.81992   8.86255  1.000 41.81706  ? 87  HIS A ND1 1 
ATOM   553  C CD2 . HIS A 1 74  ? 27.51899 6.04217   10.65140 1.000 43.13269  ? 87  HIS A CD2 1 
ATOM   554  C CE1 . HIS A 1 74  ? 26.64796 5.97721   8.63944  1.000 43.08609  ? 87  HIS A CE1 1 
ATOM   555  N NE2 . HIS A 1 74  ? 26.80057 6.73728   9.70879  1.000 42.51545  ? 87  HIS A NE2 1 
ATOM   556  N N   . LEU A 1 75  ? 30.68444 1.58560   11.44435 1.000 45.64182  ? 88  LEU A N   1 
ATOM   557  C CA  . LEU A 1 75  ? 31.16432 0.61386   12.41899 1.000 46.86072  ? 88  LEU A CA  1 
ATOM   558  C C   . LEU A 1 75  ? 32.66741 0.72337   12.63147 1.000 48.10989  ? 88  LEU A C   1 
ATOM   559  O O   . LEU A 1 75  ? 33.15003 0.51462   13.75015 1.000 48.37268  ? 88  LEU A O   1 
ATOM   560  C CB  . LEU A 1 75  ? 30.78862 -0.79743  11.97031 1.000 44.52515  ? 88  LEU A CB  1 
ATOM   561  C CG  . LEU A 1 75  ? 29.40193 -1.27386  12.40890 1.000 42.45182  ? 88  LEU A CG  1 
ATOM   562  C CD1 . LEU A 1 75  ? 29.06480 -2.62123  11.78491 1.000 41.36013  ? 88  LEU A CD1 1 
ATOM   563  C CD2 . LEU A 1 75  ? 29.29325 -1.33047  13.92538 1.000 42.14001  ? 88  LEU A CD2 1 
ATOM   564  N N   . ALA A 1 76  ? 33.41942 1.04887   11.57836 1.000 47.04943  ? 89  ALA A N   1 
ATOM   565  C CA  . ALA A 1 76  ? 34.86349 1.19237   11.71668 1.000 50.48377  ? 89  ALA A CA  1 
ATOM   566  C C   . ALA A 1 76  ? 35.23496 2.45740   12.48018 1.000 54.67020  ? 89  ALA A C   1 
ATOM   567  O O   . ALA A 1 76  ? 36.22093 2.46031   13.22646 1.000 59.55365  ? 89  ALA A O   1 
ATOM   568  C CB  . ALA A 1 76  ? 35.52368 1.18249   10.33921 1.000 50.52308  ? 89  ALA A CB  1 
ATOM   569  N N   . ALA A 1 77  ? 34.46771 3.53828   12.31120 1.000 53.42880  ? 90  ALA A N   1 
ATOM   570  C CA  . ALA A 1 77  ? 34.74974 4.75428   13.06817 1.000 57.64995  ? 90  ALA A CA  1 
ATOM   571  C C   . ALA A 1 77  ? 34.37395 4.60513   14.53835 1.000 58.76017  ? 90  ALA A C   1 
ATOM   572  O O   . ALA A 1 77  ? 34.94172 5.29410   15.39437 1.000 63.75585  ? 90  ALA A O   1 
ATOM   573  C CB  . ALA A 1 77  ? 34.01550 5.94532   12.45101 1.000 56.34929  ? 90  ALA A CB  1 
ATOM   574  N N   . HIS A 1 78  ? 33.43251 3.71866   14.84882 1.000 54.81297  ? 91  HIS A N   1 
ATOM   575  C CA  . HIS A 1 78  ? 32.96106 3.54829   16.21377 1.000 57.78147  ? 91  HIS A CA  1 
ATOM   576  C C   . HIS A 1 78  ? 33.90961 2.66135   17.01200 1.000 64.31243  ? 91  HIS A C   1 
ATOM   577  O O   . HIS A 1 78  ? 34.62582 1.82164   16.45859 1.000 67.68597  ? 91  HIS A O   1 
ATOM   578  C CB  . HIS A 1 78  ? 31.55431 2.94608   16.21669 1.000 54.23790  ? 91  HIS A CB  1 
ATOM   579  C CG  . HIS A 1 78  ? 30.87380 2.99772   17.55011 1.000 58.25616  ? 91  HIS A CG  1 
ATOM   580  N ND1 . HIS A 1 78  ? 30.33769 1.88187   18.15638 1.000 59.46285  ? 91  HIS A ND1 1 
ATOM   581  C CD2 . HIS A 1 78  ? 30.63977 4.03154   18.39295 1.000 58.22545  ? 91  HIS A CD2 1 
ATOM   582  C CE1 . HIS A 1 78  ? 29.80709 2.22469   19.31678 1.000 56.71258  ? 91  HIS A CE1 1 
ATOM   583  N NE2 . HIS A 1 78  ? 29.97665 3.52377   19.48420 1.000 56.52085  ? 91  HIS A NE2 1 
ATOM   584  N N   . ALA A 1 79  ? 33.90535 2.86511   18.33037 1.000 65.89108  ? 92  ALA A N   1 
ATOM   585  C CA  . ALA A 1 79  ? 34.62646 2.02387   19.28094 1.000 70.49407  ? 92  ALA A CA  1 
ATOM   586  C C   . ALA A 1 79  ? 36.13116 1.97524   19.03706 1.000 75.62182  ? 92  ALA A C   1 
ATOM   587  O O   . ALA A 1 79  ? 36.84804 2.92958   19.35581 1.000 80.76349  ? 92  ALA A O   1 
ATOM   588  C CB  . ALA A 1 79  ? 34.05843 0.60214   19.26971 1.000 67.20317  ? 92  ALA A CB  1 
ATOM   589  N N   . ASN A 1 80  ? 36.61386 0.85672   18.48857 1.000 74.70068  ? 93  ASN A N   1 
ATOM   590  C CA  . ASN A 1 80  ? 38.04366 0.55665   18.50823 1.000 78.40199  ? 93  ASN A CA  1 
ATOM   591  C C   . ASN A 1 80  ? 38.84991 1.56885   17.69891 1.000 82.73723  ? 93  ASN A C   1 
ATOM   592  O O   . ASN A 1 80  ? 39.70194 2.27971   18.24467 1.000 87.18415  ? 93  ASN A O   1 
ATOM   593  C CB  . ASN A 1 80  ? 38.28161 -0.86318  17.99044 1.000 81.07706  ? 93  ASN A CB  1 
ATOM   594  N N   . GLY A 1 81  ? 38.59808 1.65030   16.39269 1.000 80.96564  ? 94  GLY A N   1 
ATOM   595  C CA  . GLY A 1 81  ? 39.41967 2.49411   15.54348 1.000 79.09384  ? 94  GLY A CA  1 
ATOM   596  C C   . GLY A 1 81  ? 39.97141 1.80549   14.31104 1.000 76.39557  ? 94  GLY A C   1 
ATOM   597  O O   . GLY A 1 81  ? 39.21306 1.47923   13.39236 1.000 70.39397  ? 94  GLY A O   1 
ATOM   598  N N   . HIS A 1 82  ? 41.28949 1.58649   14.27747 1.000 82.10393  ? 95  HIS A N   1 
ATOM   599  C CA  . HIS A 1 82  ? 41.98650 1.01887   13.11953 1.000 81.59541  ? 95  HIS A CA  1 
ATOM   600  C C   . HIS A 1 82  ? 41.81768 1.91825   11.88815 1.000 79.47047  ? 95  HIS A C   1 
ATOM   601  O O   . HIS A 1 82  ? 41.16114 1.57812   10.90059 1.000 73.81909  ? 95  HIS A O   1 
ATOM   602  C CB  . HIS A 1 82  ? 41.51746 -0.41619  12.84185 1.000 76.60022  ? 95  HIS A CB  1 
ATOM   603  N N   . LEU A 1 83  ? 42.42665 3.10511   12.00420 1.000 69.03167  ? 96  LEU A N   1 
ATOM   604  C CA  . LEU A 1 83  ? 42.38690 4.12294   10.95388 1.000 66.50915  ? 96  LEU A CA  1 
ATOM   605  C C   . LEU A 1 83  ? 42.73085 3.57298   9.56919  1.000 64.56296  ? 96  LEU A C   1 
ATOM   606  O O   . LEU A 1 83  ? 42.26963 4.11093   8.55205  1.000 63.60302  ? 96  LEU A O   1 
ATOM   607  C CB  . LEU A 1 83  ? 43.32192 5.27387   11.35255 1.000 67.03721  ? 96  LEU A CB  1 
ATOM   608  C CG  . LEU A 1 83  ? 44.83967 5.20472   11.12567 1.000 70.21151  ? 96  LEU A CG  1 
ATOM   609  C CD1 . LEU A 1 83  ? 45.26474 5.70084   9.75491  1.000 65.99911  ? 96  LEU A CD1 1 
ATOM   610  C CD2 . LEU A 1 83  ? 45.56984 5.97704   12.22254 1.000 76.61728  ? 96  LEU A CD2 1 
ATOM   611  N N   . GLU A 1 84  ? 43.52691 2.50438   9.50054  1.000 65.94461  ? 97  GLU A N   1 
ATOM   612  C CA  . GLU A 1 84  ? 43.82396 1.90262   8.20504  1.000 59.88755  ? 97  GLU A CA  1 
ATOM   613  C C   . GLU A 1 84  ? 42.55815 1.38209   7.53400  1.000 54.70005  ? 97  GLU A C   1 
ATOM   614  O O   . GLU A 1 84  ? 42.40403 1.49680   6.31339  1.000 53.19145  ? 97  GLU A O   1 
ATOM   615  C CB  . GLU A 1 84  ? 44.84568 0.77992   8.36815  1.000 58.63648  ? 97  GLU A CB  1 
ATOM   616  N N   . ILE A 1 85  ? 41.64115 0.80609   8.31437  1.000 56.75009  ? 98  ILE A N   1 
ATOM   617  C CA  . ILE A 1 85  ? 40.42798 0.23583   7.73551  1.000 53.62455  ? 98  ILE A CA  1 
ATOM   618  C C   . ILE A 1 85  ? 39.52320 1.32838   7.17959  1.000 53.28325  ? 98  ILE A C   1 
ATOM   619  O O   . ILE A 1 85  ? 38.96818 1.18791   6.08281  1.000 51.87096  ? 98  ILE A O   1 
ATOM   620  C CB  . ILE A 1 85  ? 39.70045 -0.63995  8.77031  1.000 54.23809  ? 98  ILE A CB  1 
ATOM   621  C CG1 . ILE A 1 85  ? 40.52589 -1.89153  9.06680  1.000 47.90271  ? 98  ILE A CG1 1 
ATOM   622  C CG2 . ILE A 1 85  ? 38.30785 -1.01778  8.27898  1.000 50.28139  ? 98  ILE A CG2 1 
ATOM   623  C CD1 . ILE A 1 85  ? 39.89241 -2.80070  10.07171 1.000 46.67816  ? 98  ILE A CD1 1 
ATOM   624  N N   . VAL A 1 86  ? 39.35588 2.43338   7.91346  1.000 53.94064  ? 99  VAL A N   1 
ATOM   625  C CA  . VAL A 1 86  ? 38.54489 3.51613   7.36541  1.000 52.02879  ? 99  VAL A CA  1 
ATOM   626  C C   . VAL A 1 86  ? 39.21808 4.11315   6.13637  1.000 52.39250  ? 99  VAL A C   1 
ATOM   627  O O   . VAL A 1 86  ? 38.53353 4.51583   5.18874  1.000 50.49296  ? 99  VAL A O   1 
ATOM   628  C CB  . VAL A 1 86  ? 38.23348 4.60351   8.41590  1.000 53.90465  ? 99  VAL A CB  1 
ATOM   629  C CG1 . VAL A 1 86  ? 37.06014 4.19347   9.28857  1.000 52.27300  ? 99  VAL A CG1 1 
ATOM   630  C CG2 . VAL A 1 86  ? 39.43458 4.91535   9.26606  1.000 57.78677  ? 99  VAL A CG2 1 
ATOM   631  N N   . GLU A 1 87  ? 40.55556 4.18065   6.11648  1.000 53.88828  ? 100 GLU A N   1 
ATOM   632  C CA  . GLU A 1 87  ? 41.23321 4.67114   4.91574  1.000 51.75233  ? 100 GLU A CA  1 
ATOM   633  C C   . GLU A 1 87  ? 40.96471 3.76954   3.71614  1.000 51.98413  ? 100 GLU A C   1 
ATOM   634  O O   . GLU A 1 87  ? 40.68489 4.25547   2.61491  1.000 51.57033  ? 100 GLU A O   1 
ATOM   635  C CB  . GLU A 1 87  ? 42.73862 4.79517   5.14513  1.000 54.33578  ? 100 GLU A CB  1 
ATOM   636  C CG  . GLU A 1 87  ? 43.17401 6.14292   5.68519  1.000 60.40931  ? 100 GLU A CG  1 
ATOM   637  C CD  . GLU A 1 87  ? 44.46503 6.06458   6.46488  1.000 63.98021  ? 100 GLU A CD  1 
ATOM   638  O OE1 . GLU A 1 87  ? 44.95899 4.93795   6.68208  1.000 62.52776  ? 100 GLU A OE1 1 
ATOM   639  O OE2 . GLU A 1 87  ? 44.99341 7.13133   6.84400  1.000 65.55261  ? 100 GLU A OE2 1 
ATOM   640  N N   . VAL A 1 88  ? 41.06074 2.45103   3.90567  1.000 54.54135  ? 101 VAL A N   1 
ATOM   641  C CA  . VAL A 1 88  ? 40.80723 1.52842   2.79925  1.000 52.75677  ? 101 VAL A CA  1 
ATOM   642  C C   . VAL A 1 88  ? 39.35568 1.62088   2.34595  1.000 51.96042  ? 101 VAL A C   1 
ATOM   643  O O   . VAL A 1 88  ? 39.05869 1.54360   1.14687  1.000 53.66732  ? 101 VAL A O   1 
ATOM   644  C CB  . VAL A 1 88  ? 41.19383 0.08977   3.18911  1.000 52.06034  ? 101 VAL A CB  1 
ATOM   645  C CG1 . VAL A 1 88  ? 41.02161 -0.83441  2.00063  1.000 53.48942  ? 101 VAL A CG1 1 
ATOM   646  C CG2 . VAL A 1 88  ? 42.64079 0.04656   3.63652  1.000 55.06534  ? 101 VAL A CG2 1 
ATOM   647  N N   . LEU A 1 89  ? 38.42908 1.77982   3.29267  1.000 50.95705  ? 102 LEU A N   1 
ATOM   648  C CA  . LEU A 1 89  ? 37.02568 1.94469   2.93034  1.000 51.24467  ? 102 LEU A CA  1 
ATOM   649  C C   . LEU A 1 89  ? 36.82381 3.20112   2.09287  1.000 51.85636  ? 102 LEU A C   1 
ATOM   650  O O   . LEU A 1 89  ? 36.14953 3.16869   1.05728  1.000 53.58047  ? 102 LEU A O   1 
ATOM   651  C CB  . LEU A 1 89  ? 36.16227 1.99066   4.19126  1.000 51.92417  ? 102 LEU A CB  1 
ATOM   652  C CG  . LEU A 1 89  ? 35.89073 0.65821   4.89216  1.000 48.64142  ? 102 LEU A CG  1 
ATOM   653  C CD1 . LEU A 1 89  ? 35.37682 0.89086   6.30372  1.000 48.12123  ? 102 LEU A CD1 1 
ATOM   654  C CD2 . LEU A 1 89  ? 34.90587 -0.17994  4.09395  1.000 45.40633  ? 102 LEU A CD2 1 
ATOM   655  N N   . LEU A 1 90  ? 37.41696 4.31920   2.52227  1.000 52.06263  ? 103 LEU A N   1 
ATOM   656  C CA  . LEU A 1 90  ? 37.27522 5.57145   1.78485  1.000 53.73695  ? 103 LEU A CA  1 
ATOM   657  C C   . LEU A 1 90  ? 37.88837 5.46836   0.39404  1.000 51.77043  ? 103 LEU A C   1 
ATOM   658  O O   . LEU A 1 90  ? 37.31280 5.95861   -0.58541 1.000 52.98449  ? 103 LEU A O   1 
ATOM   659  C CB  . LEU A 1 90  ? 37.91560 6.71602   2.57040  1.000 52.71410  ? 103 LEU A CB  1 
ATOM   660  C CG  . LEU A 1 90  ? 37.21024 7.14543   3.85805  1.000 53.52152  ? 103 LEU A CG  1 
ATOM   661  C CD1 . LEU A 1 90  ? 38.15258 7.96001   4.72976  1.000 55.44415  ? 103 LEU A CD1 1 
ATOM   662  C CD2 . LEU A 1 90  ? 35.94669 7.93100   3.54574  1.000 52.23701  ? 103 LEU A CD2 1 
ATOM   663  N N   . LYS A 1 91  ? 39.05999 4.83570   0.28855  1.000 50.75134  ? 104 LYS A N   1 
ATOM   664  C CA  . LYS A 1 91  ? 39.69332 4.66145   -1.01386 1.000 55.73062  ? 104 LYS A CA  1 
ATOM   665  C C   . LYS A 1 91  ? 38.83559 3.80383   -1.93736 1.000 54.92213  ? 104 LYS A C   1 
ATOM   666  O O   . LYS A 1 91  ? 38.89277 3.95871   -3.16325 1.000 56.42789  ? 104 LYS A O   1 
ATOM   667  C CB  . LYS A 1 91  ? 41.08662 4.05125   -0.83306 1.000 56.44049  ? 104 LYS A CB  1 
ATOM   668  C CG  . LYS A 1 91  ? 41.72196 3.51039   -2.10190 1.000 57.63345  ? 104 LYS A CG  1 
ATOM   669  C CD  . LYS A 1 91  ? 43.17360 3.95023   -2.22669 1.000 55.38769  ? 104 LYS A CD  1 
ATOM   670  C CE  . LYS A 1 91  ? 43.64471 3.86845   -3.67144 1.000 54.56164  ? 104 LYS A CE  1 
ATOM   671  N NZ  . LYS A 1 91  ? 43.84655 5.21754   -4.26812 1.000 56.41661  ? 104 LYS A NZ  1 
ATOM   672  N N   . HIS A 1 92  ? 38.01503 2.92016   -1.37213 1.000 53.36398  ? 105 HIS A N   1 
ATOM   673  C CA  . HIS A 1 92  ? 37.14179 2.05084   -2.14765 1.000 54.60944  ? 105 HIS A CA  1 
ATOM   674  C C   . HIS A 1 92  ? 35.74345 2.62978   -2.32399 1.000 54.25807  ? 105 HIS A C   1 
ATOM   675  O O   . HIS A 1 92  ? 34.83167 1.90605   -2.73711 1.000 57.13834  ? 105 HIS A O   1 
ATOM   676  C CB  . HIS A 1 92  ? 37.06358 0.66668   -1.49894 1.000 55.09612  ? 105 HIS A CB  1 
ATOM   677  C CG  . HIS A 1 92  ? 38.19022 -0.24178  -1.88365 1.000 56.99104  ? 105 HIS A CG  1 
ATOM   678  N ND1 . HIS A 1 92  ? 39.42572 -0.19391  -1.27443 1.000 55.76651  ? 105 HIS A ND1 1 
ATOM   679  C CD2 . HIS A 1 92  ? 38.27079 -1.21635  -2.82053 1.000 57.41835  ? 105 HIS A CD2 1 
ATOM   680  C CE1 . HIS A 1 92  ? 40.21735 -1.10225  -1.81622 1.000 59.06067  ? 105 HIS A CE1 1 
ATOM   681  N NE2 . HIS A 1 92  ? 39.54101 -1.73607  -2.75733 1.000 59.19861  ? 105 HIS A NE2 1 
ATOM   682  N N   . GLY A 1 93  ? 35.55487 3.91129   -2.01682 1.000 51.63060  ? 106 GLY A N   1 
ATOM   683  C CA  . GLY A 1 93  ? 34.29448 4.57223   -2.27974 1.000 49.09145  ? 106 GLY A CA  1 
ATOM   684  C C   . GLY A 1 93  ? 33.32217 4.63243   -1.12572 1.000 50.51459  ? 106 GLY A C   1 
ATOM   685  O O   . GLY A 1 93  ? 32.10966 4.68792   -1.35991 1.000 52.74733  ? 106 GLY A O   1 
ATOM   686  N N   . ALA A 1 94  ? 33.80588 4.62132   0.11451  1.000 48.61036  ? 107 ALA A N   1 
ATOM   687  C CA  . ALA A 1 94  ? 32.91134 4.72243   1.26006  1.000 50.65103  ? 107 ALA A CA  1 
ATOM   688  C C   . ALA A 1 94  ? 32.30996 6.11813   1.33708  1.000 51.65810  ? 107 ALA A C   1 
ATOM   689  O O   . ALA A 1 94  ? 33.02773 7.12046   1.26543  1.000 53.65419  ? 107 ALA A O   1 
ATOM   690  C CB  . ALA A 1 94  ? 33.65463 4.40039   2.55446  1.000 50.76002  ? 107 ALA A CB  1 
ATOM   691  N N   . ASP A 1 95  ? 30.99004 6.18199   1.48945  1.000 54.53891  ? 108 ASP A N   1 
ATOM   692  C CA  . ASP A 1 95  ? 30.30103 7.45948   1.63107  1.000 52.99558  ? 108 ASP A CA  1 
ATOM   693  C C   . ASP A 1 95  ? 30.66797 8.07324   2.97629  1.000 56.57316  ? 108 ASP A C   1 
ATOM   694  O O   . ASP A 1 95  ? 30.21663 7.60477   4.02618  1.000 57.55767  ? 108 ASP A O   1 
ATOM   695  C CB  . ASP A 1 95  ? 28.79375 7.26174   1.50467  1.000 55.01888  ? 108 ASP A CB  1 
ATOM   696  C CG  . ASP A 1 95  ? 28.03007 8.57191   1.50555  1.000 57.02556  ? 108 ASP A CG  1 
ATOM   697  O OD1 . ASP A 1 95  ? 28.65118 9.62692   1.25511  1.000 56.28499  ? 108 ASP A OD1 1 
ATOM   698  O OD2 . ASP A 1 95  ? 26.80534 8.54446   1.75027  1.000 55.84674  ? 108 ASP A OD2 1 
ATOM   699  N N   . VAL A 1 96  ? 31.49462 9.12005   2.94650  1.000 56.40001  ? 109 VAL A N   1 
ATOM   700  C CA  . VAL A 1 96  ? 31.97649 9.72580   4.18413  1.000 56.72410  ? 109 VAL A CA  1 
ATOM   701  C C   . VAL A 1 96  ? 30.82741 10.37619  4.94617  1.000 55.97408  ? 109 VAL A C   1 
ATOM   702  O O   . VAL A 1 96  ? 30.76755 10.31302  6.18079  1.000 54.56271  ? 109 VAL A O   1 
ATOM   703  C CB  . VAL A 1 96  ? 33.10703 10.72764  3.87684  1.000 59.38959  ? 109 VAL A CB  1 
ATOM   704  C CG1 . VAL A 1 96  ? 32.72216 11.63507  2.71566  1.000 62.77847  ? 109 VAL A CG1 1 
ATOM   705  C CG2 . VAL A 1 96  ? 33.46232 11.54275  5.11427  1.000 61.83194  ? 109 VAL A CG2 1 
ATOM   706  N N   . ASN A 1 97  ? 29.88760 10.99100  4.22897  1.000 54.89537  ? 110 ASN A N   1 
ATOM   707  C CA  . ASN A 1 97  ? 28.76275 11.68680  4.83776  1.000 56.68320  ? 110 ASN A CA  1 
ATOM   708  C C   . ASN A 1 97  ? 27.51754 10.81178  4.94010  1.000 53.70764  ? 110 ASN A C   1 
ATOM   709  O O   . ASN A 1 97  ? 26.40388 11.33991  5.03206  1.000 51.63210  ? 110 ASN A O   1 
ATOM   710  C CB  . ASN A 1 97  ? 28.44578 12.96282  4.05602  1.000 58.16926  ? 110 ASN A CB  1 
ATOM   711  C CG  . ASN A 1 97  ? 29.65213 13.86796  3.90261  1.000 64.44015  ? 110 ASN A CG  1 
ATOM   712  O OD1 . ASN A 1 97  ? 30.08630 14.15886  2.78746  1.000 68.68485  ? 110 ASN A OD1 1 
ATOM   713  N ND2 . ASN A 1 97  ? 30.20289 14.31615  5.02520  1.000 65.65337  ? 110 ASN A ND2 1 
ATOM   714  N N   . ALA A 1 98  ? 27.68065 9.49024   4.91941  1.000 51.45385  ? 111 ALA A N   1 
ATOM   715  C CA  . ALA A 1 98  ? 26.53523 8.59711   5.02813  1.000 50.82402  ? 111 ALA A CA  1 
ATOM   716  C C   . ALA A 1 98  ? 25.86909 8.75689   6.38835  1.000 48.25168  ? 111 ALA A C   1 
ATOM   717  O O   . ALA A 1 98  ? 26.53300 8.72227   7.42779  1.000 44.74746  ? 111 ALA A O   1 
ATOM   718  C CB  . ALA A 1 98  ? 26.97154 7.14761   4.81454  1.000 51.16943  ? 111 ALA A CB  1 
ATOM   719  N N   . GLN A 1 99  ? 24.55176 8.93114   6.37809  1.000 45.63384  ? 112 GLN A N   1 
ATOM   720  C CA  . GLN A 1 99  ? 23.77759 9.15998   7.58835  1.000 44.92520  ? 112 GLN A CA  1 
ATOM   721  C C   . GLN A 1 99  ? 22.93712 7.93332   7.91051  1.000 46.09709  ? 112 GLN A C   1 
ATOM   722  O O   . GLN A 1 99  ? 22.39953 7.28323   7.00853  1.000 47.11733  ? 112 GLN A O   1 
ATOM   723  C CB  . GLN A 1 99  ? 22.86613 10.38184  7.43730  1.000 46.12237  ? 112 GLN A CB  1 
ATOM   724  C CG  . GLN A 1 99  ? 23.58116 11.71920  7.51661  1.000 45.63895  ? 112 GLN A CG  1 
ATOM   725  C CD  . GLN A 1 99  ? 22.61601 12.89093  7.52478  1.000 49.62910  ? 112 GLN A CD  1 
ATOM   726  O OE1 . GLN A 1 99  ? 21.55412 12.83935  6.90338  1.000 50.25906  ? 112 GLN A OE1 1 
ATOM   727  N NE2 . GLN A 1 99  ? 22.98110 13.95510  8.23127  1.000 52.24330  ? 112 GLN A NE2 1 
ATOM   728  N N   . ASP A 1 100 ? 22.82756 7.62003   9.19830  1.000 42.79229  ? 113 ASP A N   1 
ATOM   729  C CA  . ASP A 1 100 ? 21.91556 6.57870   9.65027  1.000 41.00140  ? 113 ASP A CA  1 
ATOM   730  C C   . ASP A 1 100 ? 20.50160 7.15850   9.70201  1.000 39.82903  ? 113 ASP A C   1 
ATOM   731  O O   . ASP A 1 100 ? 20.22878 8.23364   9.16076  1.000 39.14351  ? 113 ASP A O   1 
ATOM   732  C CB  . ASP A 1 100 ? 22.38155 5.99773   10.98511 1.000 38.54248  ? 113 ASP A CB  1 
ATOM   733  C CG  . ASP A 1 100 ? 22.26552 6.98206   12.13632 1.000 41.11082  ? 113 ASP A CG  1 
ATOM   734  O OD1 . ASP A 1 100 ? 22.09341 8.19425   11.88788 1.000 41.89735  ? 113 ASP A OD1 1 
ATOM   735  O OD2 . ASP A 1 100 ? 22.34588 6.53398   13.30069 1.000 39.60124  ? 113 ASP A OD2 1 
ATOM   736  N N   . TRP A 1 101 ? 19.57586 6.44424   10.34671 1.000 39.60403  ? 114 TRP A N   1 
ATOM   737  C CA  . TRP A 1 101 ? 18.18382 6.88506   10.35092 1.000 39.30448  ? 114 TRP A CA  1 
ATOM   738  C C   . TRP A 1 101 ? 18.02952 8.25212   11.01039 1.000 36.05119  ? 114 TRP A C   1 
ATOM   739  O O   . TRP A 1 101 ? 17.22234 9.07389   10.56044 1.000 31.81343  ? 114 TRP A O   1 
ATOM   740  C CB  . TRP A 1 101 ? 17.29640 5.85406   11.04986 1.000 39.26724  ? 114 TRP A CB  1 
ATOM   741  C CG  . TRP A 1 101 ? 17.47562 4.42553   10.60415 1.000 38.68105  ? 114 TRP A CG  1 
ATOM   742  C CD1 . TRP A 1 101 ? 17.51558 3.32933   11.40951 1.000 36.98595  ? 114 TRP A CD1 1 
ATOM   743  C CD2 . TRP A 1 101 ? 17.61307 3.93806   9.25909  1.000 35.81466  ? 114 TRP A CD2 1 
ATOM   744  N NE1 . TRP A 1 101 ? 17.67863 2.19169   10.65967 1.000 35.32396  ? 114 TRP A NE1 1 
ATOM   745  C CE2 . TRP A 1 101 ? 17.74257 2.53738   9.33630  1.000 36.33290  ? 114 TRP A CE2 1 
ATOM   746  C CE3 . TRP A 1 101 ? 17.64463 4.54832   8.00078  1.000 35.96376  ? 114 TRP A CE3 1 
ATOM   747  C CZ2 . TRP A 1 101 ? 17.90165 1.73819   8.20637  1.000 38.54670  ? 114 TRP A CZ2 1 
ATOM   748  C CZ3 . TRP A 1 101 ? 17.80340 3.75351   6.88096  1.000 36.13307  ? 114 TRP A CZ3 1 
ATOM   749  C CH2 . TRP A 1 101 ? 17.92953 2.36350   6.99106  1.000 39.40720  ? 114 TRP A CH2 1 
ATOM   750  N N   . ILE A 1 102 ? 18.78890 8.51755   12.07357 1.000 40.01247  ? 115 ILE A N   1 
ATOM   751  C CA  . ILE A 1 102 ? 18.69772 9.79420   12.77430 1.000 40.04713  ? 115 ILE A CA  1 
ATOM   752  C C   . ILE A 1 102 ? 19.83769 10.73827  12.39045 1.000 41.07819  ? 115 ILE A C   1 
ATOM   753  O O   . ILE A 1 102 ? 20.00039 11.79410  13.01037 1.000 44.99880  ? 115 ILE A O   1 
ATOM   754  C CB  . ILE A 1 102 ? 18.60945 9.58465   14.29962 1.000 41.65520  ? 115 ILE A CB  1 
ATOM   755  C CG1 . ILE A 1 102 ? 19.95313 9.18685   14.91683 1.000 40.65386  ? 115 ILE A CG1 1 
ATOM   756  C CG2 . ILE A 1 102 ? 17.55365 8.53670   14.63354 1.000 41.87709  ? 115 ILE A CG2 1 
ATOM   757  C CD1 . ILE A 1 102 ? 20.60214 10.29395  15.73129 1.000 45.06253  ? 115 ILE A CD1 1 
ATOM   758  N N   . GLY A 1 103 ? 20.60690 10.39852  11.36076 1.000 41.29366  ? 116 GLY A N   1 
ATOM   759  C CA  . GLY A 1 103 ? 21.56363 11.33174  10.79256 1.000 42.98698  ? 116 GLY A CA  1 
ATOM   760  C C   . GLY A 1 103 ? 22.93401 11.35282  11.43240 1.000 44.73254  ? 116 GLY A C   1 
ATOM   761  O O   . GLY A 1 103 ? 23.53218 12.42805  11.57070 1.000 44.95932  ? 116 GLY A O   1 
ATOM   762  N N   . VAL A 1 104 ? 23.45605 10.19667  11.82579 1.000 43.13099  ? 117 VAL A N   1 
ATOM   763  C CA  . VAL A 1 104 ? 24.80148 10.09372  12.37778 1.000 46.24787  ? 117 VAL A CA  1 
ATOM   764  C C   . VAL A 1 104 ? 25.73807 9.68920   11.24983 1.000 45.86998  ? 117 VAL A C   1 
ATOM   765  O O   . VAL A 1 104 ? 25.63571 8.58283   10.70965 1.000 44.22141  ? 117 VAL A O   1 
ATOM   766  C CB  . VAL A 1 104 ? 24.87153 9.09355   13.53875 1.000 44.40332  ? 117 VAL A CB  1 
ATOM   767  C CG1 . VAL A 1 104 ? 26.18367 9.25287   14.29238 1.000 45.64253  ? 117 VAL A CG1 1 
ATOM   768  C CG2 . VAL A 1 104 ? 23.70968 9.29924   14.48095 1.000 42.73765  ? 117 VAL A CG2 1 
ATOM   769  N N   . THR A 1 105 ? 26.64721 10.58478  10.88966 1.000 46.03689  ? 118 THR A N   1 
ATOM   770  C CA  . THR A 1 105 ? 27.71768 10.24382  9.97305  1.000 45.73664  ? 118 THR A CA  1 
ATOM   771  C C   . THR A 1 105 ? 28.82624 9.52087   10.72891 1.000 48.86497  ? 118 THR A C   1 
ATOM   772  O O   . THR A 1 105 ? 28.91073 9.61091   11.95636 1.000 50.39911  ? 118 THR A O   1 
ATOM   773  C CB  . THR A 1 105 ? 28.26623 11.50142  9.30574  1.000 48.58794  ? 118 THR A CB  1 
ATOM   774  O OG1 . THR A 1 105 ? 28.69147 12.43042  10.30964 1.000 50.14930  ? 118 THR A OG1 1 
ATOM   775  C CG2 . THR A 1 105 ? 27.19641 12.15112  8.44182  1.000 51.89286  ? 118 THR A CG2 1 
ATOM   776  N N   . PRO A 1 106 ? 29.67936 8.77241   10.02451 1.000 46.39224  ? 119 PRO A N   1 
ATOM   777  C CA  . PRO A 1 106 ? 30.84582 8.18527   10.70269 1.000 47.16661  ? 119 PRO A CA  1 
ATOM   778  C C   . PRO A 1 106 ? 31.73500 9.22762   11.35540 1.000 51.06555  ? 119 PRO A C   1 
ATOM   779  O O   . PRO A 1 106 ? 32.39475 8.92991   12.35971 1.000 53.15385  ? 119 PRO A O   1 
ATOM   780  C CB  . PRO A 1 106 ? 31.56917 7.44347   9.57126  1.000 48.24995  ? 119 PRO A CB  1 
ATOM   781  C CG  . PRO A 1 106 ? 30.49235 7.12472   8.59344  1.000 45.84156  ? 119 PRO A CG  1 
ATOM   782  C CD  . PRO A 1 106 ? 29.54558 8.28813   8.63914  1.000 44.84957  ? 119 PRO A CD  1 
ATOM   783  N N   . PHE A 1 107 ? 31.76948 10.44661  10.81062 1.000 52.61609  ? 120 PHE A N   1 
ATOM   784  C CA  . PHE A 1 107 ? 32.53106 11.52233  11.43642 1.000 55.36055  ? 120 PHE A CA  1 
ATOM   785  C C   . PHE A 1 107 ? 31.97524 11.86620  12.81261 1.000 55.65189  ? 120 PHE A C   1 
ATOM   786  O O   . PHE A 1 107 ? 32.73894 12.11648  13.75242 1.000 59.32098  ? 120 PHE A O   1 
ATOM   787  C CB  . PHE A 1 107 ? 32.53346 12.75520  10.53336 1.000 60.13478  ? 120 PHE A CB  1 
ATOM   788  N N   . ASP A 1 108 ? 30.64609 11.89473  12.94901 1.000 53.71872  ? 121 ASP A N   1 
ATOM   789  C CA  . ASP A 1 108 ? 30.04444 12.14411  14.25594 1.000 54.16141  ? 121 ASP A CA  1 
ATOM   790  C C   . ASP A 1 108 ? 30.42019 11.05092  15.24697 1.000 56.13683  ? 121 ASP A C   1 
ATOM   791  O O   . ASP A 1 108 ? 30.71207 11.33193  16.41562 1.000 58.83044  ? 121 ASP A O   1 
ATOM   792  C CB  . ASP A 1 108 ? 28.52392 12.24826  14.12846 1.000 49.49069  ? 121 ASP A CB  1 
ATOM   793  C CG  . ASP A 1 108 ? 28.08990 13.35061  13.18296 1.000 51.39749  ? 121 ASP A CG  1 
ATOM   794  O OD1 . ASP A 1 108 ? 28.64435 14.46608  13.27115 1.000 57.09624  ? 121 ASP A OD1 1 
ATOM   795  O OD2 . ASP A 1 108 ? 27.19177 13.10068  12.35127 1.000 48.39425  ? 121 ASP A OD2 1 
ATOM   796  N N   . LEU A 1 109 ? 30.41512 9.79573   14.79450 1.000 55.01963  ? 122 LEU A N   1 
ATOM   797  C CA  . LEU A 1 109 ? 30.81110 8.68781   15.65596 1.000 56.35800  ? 122 LEU A CA  1 
ATOM   798  C C   . LEU A 1 109 ? 32.26551 8.81822   16.08973 1.000 60.17935  ? 122 LEU A C   1 
ATOM   799  O O   . LEU A 1 109 ? 32.59477 8.59323   17.25998 1.000 62.78709  ? 122 LEU A O   1 
ATOM   800  C CB  . LEU A 1 109 ? 30.58531 7.36693   14.92480 1.000 52.93194  ? 122 LEU A CB  1 
ATOM   801  C CG  . LEU A 1 109 ? 29.14184 6.87431   14.84982 1.000 49.96966  ? 122 LEU A CG  1 
ATOM   802  C CD1 . LEU A 1 109 ? 29.08653 5.60473   14.02644 1.000 46.93579  ? 122 LEU A CD1 1 
ATOM   803  C CD2 . LEU A 1 109 ? 28.57646 6.64363   16.24372 1.000 50.63903  ? 122 LEU A CD2 1 
ATOM   804  N N   . ALA A 1 110 ? 33.15116 9.17966   15.15745 1.000 57.99279  ? 123 ALA A N   1 
ATOM   805  C CA  . ALA A 1 110 ? 34.55793 9.36127   15.50226 1.000 61.61866  ? 123 ALA A CA  1 
ATOM   806  C C   . ALA A 1 110 ? 34.74073 10.50152  16.49586 1.000 62.81849  ? 123 ALA A C   1 
ATOM   807  O O   . ALA A 1 110 ? 35.54637 10.39892  17.42855 1.000 67.71243  ? 123 ALA A O   1 
ATOM   808  C CB  . ALA A 1 110 ? 35.38171 9.61211   14.23936 1.000 59.71546  ? 123 ALA A CB  1 
ATOM   809  N N   . VAL A 1 111 ? 34.00530 11.60007  16.30796 1.000 64.06695  ? 124 VAL A N   1 
ATOM   810  C CA  . VAL A 1 111 ? 34.10342 12.73230  17.22575 1.000 70.04464  ? 124 VAL A CA  1 
ATOM   811  C C   . VAL A 1 111 ? 33.62157 12.33580  18.61626 1.000 69.30285  ? 124 VAL A C   1 
ATOM   812  O O   . VAL A 1 111 ? 34.25860 12.65922  19.62686 1.000 74.78690  ? 124 VAL A O   1 
ATOM   813  C CB  . VAL A 1 111 ? 33.31771 13.93614  16.67150 1.000 71.34352  ? 124 VAL A CB  1 
ATOM   814  C CG1 . VAL A 1 111 ? 33.05508 14.95767  17.76788 1.000 76.23255  ? 124 VAL A CG1 1 
ATOM   815  C CG2 . VAL A 1 111 ? 34.06772 14.57054  15.50777 1.000 75.13623  ? 124 VAL A CG2 1 
ATOM   816  N N   . ASP A 1 112 ? 32.49325 11.62442  18.69059 1.000 66.12571  ? 125 ASP A N   1 
ATOM   817  C CA  . ASP A 1 112 ? 31.97467 11.19381  19.98578 1.000 64.79316  ? 125 ASP A CA  1 
ATOM   818  C C   . ASP A 1 112 ? 32.92964 10.22465  20.67159 1.000 65.43022  ? 125 ASP A C   1 
ATOM   819  O O   . ASP A 1 112 ? 33.14589 10.30912  21.88629 1.000 68.27188  ? 125 ASP A O   1 
ATOM   820  C CB  . ASP A 1 112 ? 30.59417 10.56030  19.81566 1.000 59.93958  ? 125 ASP A CB  1 
ATOM   821  C CG  . ASP A 1 112 ? 29.57656 11.52769  19.24390 1.000 62.16677  ? 125 ASP A CG  1 
ATOM   822  O OD1 . ASP A 1 112 ? 29.71822 12.74687  19.47783 1.000 59.58502  ? 125 ASP A OD1 1 
ATOM   823  O OD2 . ASP A 1 112 ? 28.63423 11.07078  18.56268 1.000 61.97763  ? 125 ASP A OD2 1 
ATOM   824  N N   . ASP A 1 113 ? 33.51342 9.29927   19.91084 1.000 62.97412  ? 126 ASP A N   1 
ATOM   825  C CA  . ASP A 1 113 ? 34.45446 8.33826   20.46846 1.000 67.05307  ? 126 ASP A CA  1 
ATOM   826  C C   . ASP A 1 113 ? 35.85082 8.91737   20.65475 1.000 72.02869  ? 126 ASP A C   1 
ATOM   827  O O   . ASP A 1 113 ? 36.69968 8.25566   21.26207 1.000 76.59041  ? 126 ASP A O   1 
ATOM   828  C CB  . ASP A 1 113 ? 34.52194 7.09589   19.57525 1.000 71.72808  ? 126 ASP A CB  1 
ATOM   829  C CG  . ASP A 1 113 ? 33.22677 6.30261   19.57959 1.000 69.80155  ? 126 ASP A CG  1 
ATOM   830  O OD1 . ASP A 1 113 ? 32.14723 6.92079   19.46706 1.000 64.56257  ? 126 ASP A OD1 1 
ATOM   831  O OD2 . ASP A 1 113 ? 33.28778 5.05972   19.68892 1.000 68.94043  ? 126 ASP A OD2 1 
ATOM   832  N N   . GLY A 1 114 ? 36.10611 10.12151  20.15100 1.000 74.84281  ? 127 GLY A N   1 
ATOM   833  C CA  . GLY A 1 114 ? 37.38368 10.78164  20.37537 1.000 81.71079  ? 127 GLY A CA  1 
ATOM   834  C C   . GLY A 1 114 ? 38.57644 10.05026  19.80032 1.000 85.47219  ? 127 GLY A C   1 
ATOM   835  O O   . GLY A 1 114 ? 39.61568 9.94687   20.46368 1.000 86.81524  ? 127 GLY A O   1 
ATOM   836  N N   . ASN A 1 115 ? 38.45640 9.54324   18.57615 1.000 83.71688  ? 128 ASN A N   1 
ATOM   837  C CA  . ASN A 1 115 ? 39.52541 8.77351   17.95607 1.000 82.92648  ? 128 ASN A CA  1 
ATOM   838  C C   . ASN A 1 115 ? 40.49647 9.63859   17.15957 1.000 86.84393  ? 128 ASN A C   1 
ATOM   839  O O   . ASN A 1 115 ? 41.40648 9.09659   16.52376 1.000 87.02796  ? 128 ASN A O   1 
ATOM   840  C CB  . ASN A 1 115 ? 38.93679 7.67933   17.06344 1.000 79.43776  ? 128 ASN A CB  1 
ATOM   841  C CG  . ASN A 1 115 ? 38.68209 6.39118   17.82026 1.000 80.19008  ? 128 ASN A CG  1 
ATOM   842  O OD1 . ASN A 1 115 ? 37.87550 6.35324   18.75067 1.000 78.24928  ? 128 ASN A OD1 1 
ATOM   843  N ND2 . ASN A 1 115 ? 39.37592 5.32900   17.43042 1.000 80.32029  ? 128 ASN A ND2 1 
ATOM   844  N N   . GLU A 1 116 ? 40.32456 10.96240  17.18766 1.000 86.44029  ? 129 GLU A N   1 
ATOM   845  C CA  . GLU A 1 116 ? 41.29629 11.91542  16.65575 1.000 88.67951  ? 129 GLU A CA  1 
ATOM   846  C C   . GLU A 1 116 ? 41.70380 11.63334  15.21298 1.000 87.20355  ? 129 GLU A C   1 
ATOM   847  O O   . GLU A 1 116 ? 41.29129 12.35075  14.29524 1.000 84.67482  ? 129 GLU A O   1 
ATOM   848  C CB  . GLU A 1 116 ? 42.54171 11.94070  17.54663 1.000 95.76326  ? 129 GLU A CB  1 
ATOM   849  N N   . ASP A 1 117 ? 42.53168 10.60469  15.01046 1.000 90.97743  ? 130 ASP A N   1 
ATOM   850  C CA  . ASP A 1 117 ? 43.05645 10.31416  13.67856 1.000 88.88617  ? 130 ASP A CA  1 
ATOM   851  C C   . ASP A 1 117 ? 41.93096 10.01809  12.69542 1.000 81.84268  ? 130 ASP A C   1 
ATOM   852  O O   . ASP A 1 117 ? 41.93552 10.50694  11.55878 1.000 81.75808  ? 130 ASP A O   1 
ATOM   853  C CB  . ASP A 1 117 ? 44.03159 9.13842   13.74827 1.000 89.51920  ? 130 ASP A CB  1 
ATOM   854  C CG  . ASP A 1 117 ? 44.99428 9.24782   14.91602 1.000 96.16948  ? 130 ASP A CG  1 
ATOM   855  O OD1 . ASP A 1 117 ? 45.74582 10.24383  14.97928 1.000 102.58755 ? 130 ASP A OD1 1 
ATOM   856  O OD2 . ASP A 1 117 ? 44.99443 8.33975   15.77416 1.000 97.91733  ? 130 ASP A OD2 1 
ATOM   857  N N   . ILE A 1 118 ? 40.95284 9.21652   13.11854 1.000 84.92862  ? 131 ILE A N   1 
ATOM   858  C CA  . ILE A 1 118 ? 39.82277 8.90786   12.24890 1.000 75.47800  ? 131 ILE A CA  1 
ATOM   859  C C   . ILE A 1 118 ? 39.06449 10.18124  11.89849 1.000 75.10879  ? 131 ILE A C   1 
ATOM   860  O O   . ILE A 1 118 ? 38.61570 10.36273  10.75994 1.000 74.56155  ? 131 ILE A O   1 
ATOM   861  C CB  . ILE A 1 118 ? 38.91007 7.86156   12.91480 1.000 68.62512  ? 131 ILE A CB  1 
ATOM   862  C CG1 . ILE A 1 118 ? 39.71452 6.60410   13.25825 1.000 70.41122  ? 131 ILE A CG1 1 
ATOM   863  C CG2 . ILE A 1 118 ? 37.73789 7.52219   12.00790 1.000 62.85056  ? 131 ILE A CG2 1 
ATOM   864  C CD1 . ILE A 1 118 ? 38.89776 5.32753   13.28852 1.000 68.59037  ? 131 ILE A CD1 1 
ATOM   865  N N   . ALA A 1 119 ? 38.92776 11.09117  12.86605 1.000 77.53176  ? 132 ALA A N   1 
ATOM   866  C CA  . ALA A 1 119 ? 38.20931 12.33699  12.61933 1.000 75.71743  ? 132 ALA A CA  1 
ATOM   867  C C   . ALA A 1 119 ? 38.90312 13.18532  11.55863 1.000 78.36484  ? 132 ALA A C   1 
ATOM   868  O O   . ALA A 1 119 ? 38.24379 13.74172  10.67251 1.000 75.27982  ? 132 ALA A O   1 
ATOM   869  C CB  . ALA A 1 119 ? 38.06097 13.12140  13.92257 1.000 75.92597  ? 132 ALA A CB  1 
ATOM   870  N N   . GLU A 1 120 ? 40.23323 13.29686  11.62581 1.000 79.84422  ? 133 GLU A N   1 
ATOM   871  C CA  . GLU A 1 120 ? 40.93561 14.13576  10.65808 1.000 84.34343  ? 133 GLU A CA  1 
ATOM   872  C C   . GLU A 1 120 ? 40.99445 13.47386  9.28598  1.000 80.36133  ? 133 GLU A C   1 
ATOM   873  O O   . GLU A 1 120 ? 40.89963 14.15864  8.26037  1.000 82.18701  ? 133 GLU A O   1 
ATOM   874  C CB  . GLU A 1 120 ? 42.34158 14.47935  11.15673 1.000 91.39545  ? 133 GLU A CB  1 
ATOM   875  C CG  . GLU A 1 120 ? 43.19022 13.29417  11.56901 1.000 91.43094  ? 133 GLU A CG  1 
ATOM   876  C CD  . GLU A 1 120 ? 44.15666 12.86116  10.48215 1.000 94.05336  ? 133 GLU A CD  1 
ATOM   877  O OE1 . GLU A 1 120 ? 44.05866 13.38551  9.35237  1.000 94.08241  ? 133 GLU A OE1 1 
ATOM   878  O OE2 . GLU A 1 120 ? 45.01148 11.99189  10.75542 1.000 94.03764  ? 133 GLU A OE2 1 
ATOM   879  N N   . VAL A 1 121 ? 41.15116 12.14710  9.23893  1.000 82.46662  ? 134 VAL A N   1 
ATOM   880  C CA  . VAL A 1 121 ? 41.13852 11.46199  7.94722  1.000 81.20042  ? 134 VAL A CA  1 
ATOM   881  C C   . VAL A 1 121 ? 39.76377 11.56351  7.29341  1.000 77.89525  ? 134 VAL A C   1 
ATOM   882  O O   . VAL A 1 121 ? 39.65464 11.69012  6.06734  1.000 77.89744  ? 134 VAL A O   1 
ATOM   883  C CB  . VAL A 1 121 ? 41.59273 9.99812   8.09598  1.000 76.98327  ? 134 VAL A CB  1 
ATOM   884  C CG1 . VAL A 1 121 ? 41.66808 9.33405   6.73535  1.000 70.79946  ? 134 VAL A CG1 1 
ATOM   885  C CG2 . VAL A 1 121 ? 42.96627 9.94136   8.73551  1.000 77.81467  ? 134 VAL A CG2 1 
ATOM   886  N N   . LEU A 1 122 ? 38.69461 11.51331  8.09371  1.000 79.60461  ? 135 LEU A N   1 
ATOM   887  C CA  . LEU A 1 122 ? 37.35162 11.62862  7.53283  1.000 77.19596  ? 135 LEU A CA  1 
ATOM   888  C C   . LEU A 1 122 ? 37.13352 12.98109  6.86754  1.000 85.00595  ? 135 LEU A C   1 
ATOM   889  O O   . LEU A 1 122 ? 36.38747 13.07050  5.88546  1.000 86.62115  ? 135 LEU A O   1 
ATOM   890  C CB  . LEU A 1 122 ? 36.30471 11.39487  8.62112  1.000 71.76881  ? 135 LEU A CB  1 
ATOM   891  C CG  . LEU A 1 122 ? 35.94250 9.93333   8.88049  1.000 66.72619  ? 135 LEU A CG  1 
ATOM   892  C CD1 . LEU A 1 122 ? 35.44708 9.74712   10.30266 1.000 58.98815  ? 135 LEU A CD1 1 
ATOM   893  C CD2 . LEU A 1 122 ? 34.90033 9.45964   7.88200  1.000 63.35511  ? 135 LEU A CD2 1 
ATOM   894  N N   . GLN A 1 123 ? 37.78460 14.02834  7.37822  1.000 81.60380  ? 136 GLN A N   1 
ATOM   895  C CA  . GLN A 1 123 ? 37.74349 15.39626  6.83675  1.000 84.83966  ? 136 GLN A CA  1 
ATOM   896  C C   . GLN A 1 123 ? 36.39742 15.80448  6.23544  1.000 87.02225  ? 136 GLN A C   1 
ATOM   897  O O   . GLN A 1 123 ? 35.81235 16.81244  6.62976  1.000 91.02021  ? 136 GLN A O   1 
ATOM   898  C CB  . GLN A 1 123 ? 38.86598 15.59189  5.79755  1.000 88.70739  ? 136 GLN A CB  1 
ATOM   899  C CG  . GLN A 1 123 ? 38.87364 14.62843  4.60635  1.000 86.35157  ? 136 GLN A CG  1 
ATOM   900  C CD  . GLN A 1 123 ? 37.82134 14.95376  3.56175  1.000 88.92430  ? 136 GLN A CD  1 
ATOM   901  O OE1 . GLN A 1 123 ? 37.54267 16.12067  3.28474  1.000 91.67226  ? 136 GLN A OE1 1 
ATOM   902  N NE2 . GLN A 1 123 ? 37.22785 13.91899  2.97942  1.000 85.15411  ? 136 GLN A NE2 1 
ATOM   903  N N   . GLU B 2 1   ? 28.16451 -0.19014  24.35647 1.000 59.37082  ? 21  GLU B N   1 
ATOM   904  C CA  . GLU B 2 1   ? 28.77853 0.37992   25.55030 1.000 65.31985  ? 21  GLU B CA  1 
ATOM   905  C C   . GLU B 2 1   ? 28.24195 1.79121   25.79039 1.000 63.60915  ? 21  GLU B C   1 
ATOM   906  O O   . GLU B 2 1   ? 27.71549 2.09111   26.86296 1.000 64.67051  ? 21  GLU B O   1 
ATOM   907  C CB  . GLU B 2 1   ? 30.30393 0.38472   25.41432 1.000 69.73231  ? 21  GLU B CB  1 
ATOM   908  C CG  . GLU B 2 1   ? 31.01396 1.50869   26.14707 1.000 70.73736  ? 21  GLU B CG  1 
ATOM   909  C CD  . GLU B 2 1   ? 32.47998 1.60398   25.77267 1.000 75.60689  ? 21  GLU B CD  1 
ATOM   910  O OE1 . GLU B 2 1   ? 33.16586 0.55990   25.77957 1.000 74.97254  ? 21  GLU B OE1 1 
ATOM   911  O OE2 . GLU B 2 1   ? 32.94559 2.72150   25.46656 1.000 76.86891  ? 21  GLU B OE2 1 
ATOM   912  N N   . THR B 2 2   ? 28.37633 2.65485   24.78518 1.000 63.11599  ? 22  THR B N   1 
ATOM   913  C CA  . THR B 2 2   ? 27.77883 3.98251   24.80903 1.000 61.89144  ? 22  THR B CA  1 
ATOM   914  C C   . THR B 2 2   ? 26.54063 4.07792   23.93081 1.000 57.86640  ? 22  THR B C   1 
ATOM   915  O O   . THR B 2 2   ? 25.90212 5.13426   23.89253 1.000 57.61034  ? 22  THR B O   1 
ATOM   916  C CB  . THR B 2 2   ? 28.79804 5.03969   24.36826 1.000 64.88948  ? 22  THR B CB  1 
ATOM   917  O OG1 . THR B 2 2   ? 29.00479 4.94809   22.95301 1.000 63.23747  ? 22  THR B OG1 1 
ATOM   918  C CG2 . THR B 2 2   ? 30.12243 4.84095   25.08610 1.000 69.15863  ? 22  THR B CG2 1 
ATOM   919  N N   . HIS B 2 3   ? 26.18710 3.00311   23.23097 1.000 57.99101  ? 23  HIS B N   1 
ATOM   920  C CA  . HIS B 2 3   ? 25.06081 2.99759   22.31305 1.000 54.36769  ? 23  HIS B CA  1 
ATOM   921  C C   . HIS B 2 3   ? 24.12065 1.85397   22.66509 1.000 52.01336  ? 23  HIS B C   1 
ATOM   922  O O   . HIS B 2 3   ? 24.51301 0.86275   23.28543 1.000 52.62360  ? 23  HIS B O   1 
ATOM   923  C CB  . HIS B 2 3   ? 25.52460 2.87181   20.85516 1.000 53.64035  ? 23  HIS B CB  1 
ATOM   924  C CG  . HIS B 2 3   ? 26.04571 4.15023   20.27589 1.000 55.21362  ? 23  HIS B CG  1 
ATOM   925  N ND1 . HIS B 2 3   ? 27.29114 4.65280   20.58502 1.000 56.21864  ? 23  HIS B ND1 1 
ATOM   926  C CD2 . HIS B 2 3   ? 25.49082 5.02859   19.40725 1.000 52.58497  ? 23  HIS B CD2 1 
ATOM   927  C CE1 . HIS B 2 3   ? 27.48138 5.78538   19.93214 1.000 57.37653  ? 23  HIS B CE1 1 
ATOM   928  N NE2 . HIS B 2 3   ? 26.40405 6.03590   19.21034 1.000 54.70661  ? 23  HIS B NE2 1 
ATOM   929  N N   . ILE B 2 4   ? 22.86581 2.00961   22.25681 1.000 53.48475  ? 24  ILE B N   1 
ATOM   930  C CA  . ILE B 2 4   ? 21.80692 1.05424   22.54713 1.000 52.06714  ? 24  ILE B CA  1 
ATOM   931  C C   . ILE B 2 4   ? 20.96642 0.87615   21.29013 1.000 51.18707  ? 24  ILE B C   1 
ATOM   932  O O   . ILE B 2 4   ? 20.74581 1.83185   20.53314 1.000 49.65340  ? 24  ILE B O   1 
ATOM   933  C CB  . ILE B 2 4   ? 20.94553 1.51862   23.74292 1.000 51.55778  ? 24  ILE B CB  1 
ATOM   934  C CG1 . ILE B 2 4   ? 19.71243 0.63025   23.91865 1.000 51.42470  ? 24  ILE B CG1 1 
ATOM   935  C CG2 . ILE B 2 4   ? 20.53498 2.97260   23.57412 1.000 56.28476  ? 24  ILE B CG2 1 
ATOM   936  C CD1 . ILE B 2 4   ? 18.84752 1.02122   25.09641 1.000 55.60552  ? 24  ILE B CD1 1 
ATOM   937  N N   . ASN B 2 5   ? 20.52908 -0.36046  21.05493 1.000 51.18445  ? 25  ASN B N   1 
ATOM   938  C CA  . ASN B 2 5   ? 19.62436 -0.68840  19.96271 1.000 50.16655  ? 25  ASN B CA  1 
ATOM   939  C C   . ASN B 2 5   ? 18.18469 -0.65248  20.45792 1.000 49.93342  ? 25  ASN B C   1 
ATOM   940  O O   . ASN B 2 5   ? 17.86518 -1.22437  21.50508 1.000 49.51421  ? 25  ASN B O   1 
ATOM   941  C CB  . ASN B 2 5   ? 19.94196 -2.07052  19.39040 1.000 50.13909  ? 25  ASN B CB  1 
ATOM   942  C CG  . ASN B 2 5   ? 21.34223 -2.16222  18.82669 1.000 50.94031  ? 25  ASN B CG  1 
ATOM   943  O OD1 . ASN B 2 5   ? 21.77835 -1.28962  18.08075 1.000 50.62926  ? 25  ASN B OD1 1 
ATOM   944  N ND2 . ASN B 2 5   ? 22.05712 -3.22374  19.18286 1.000 54.61627  ? 25  ASN B ND2 1 
ATOM   945  N N   . LEU B 2 6   ? 17.32360 0.01894   19.70151 1.000 46.49703  ? 26  LEU B N   1 
ATOM   946  C CA  . LEU B 2 6   ? 15.90305 0.10153   19.99693 1.000 44.71334  ? 26  LEU B CA  1 
ATOM   947  C C   . LEU B 2 6   ? 15.11713 -0.19463  18.73018 1.000 42.19834  ? 26  LEU B C   1 
ATOM   948  O O   . LEU B 2 6   ? 15.61161 -0.00256  17.61813 1.000 42.23695  ? 26  LEU B O   1 
ATOM   949  C CB  . LEU B 2 6   ? 15.51870 1.48447   20.53605 1.000 47.49605  ? 26  LEU B CB  1 
ATOM   950  C CG  . LEU B 2 6   ? 15.84216 1.76612   22.00239 1.000 48.65906  ? 26  LEU B CG  1 
ATOM   951  C CD1 . LEU B 2 6   ? 16.09730 3.24989   22.20442 1.000 48.76810  ? 26  LEU B CD1 1 
ATOM   952  C CD2 . LEU B 2 6   ? 14.71577 1.28605   22.90257 1.000 52.45356  ? 26  LEU B CD2 1 
ATOM   953  N N   . LYS B 2 7   ? 13.89100 -0.67713  18.90362 1.000 42.47635  ? 27  LYS B N   1 
ATOM   954  C CA  . LYS B 2 7   ? 12.98526 -0.91730  17.78976 1.000 39.99956  ? 27  LYS B CA  1 
ATOM   955  C C   . LYS B 2 7   ? 11.72326 -0.09364  17.99061 1.000 45.46731  ? 27  LYS B C   1 
ATOM   956  O O   . LYS B 2 7   ? 11.10074 -0.15164  19.05612 1.000 45.65605  ? 27  LYS B O   1 
ATOM   957  C CB  . LYS B 2 7   ? 12.63282 -2.40141  17.65737 1.000 39.57835  ? 27  LYS B CB  1 
ATOM   958  C CG  . LYS B 2 7   ? 11.94308 -2.74465  16.34347 1.000 42.76957  ? 27  LYS B CG  1 
ATOM   959  C CD  . LYS B 2 7   ? 10.72116 -3.62050  16.55948 1.000 43.87001  ? 27  LYS B CD  1 
ATOM   960  C CE  . LYS B 2 7   ? 11.10934 -5.07310  16.76725 1.000 42.12343  ? 27  LYS B CE  1 
ATOM   961  N NZ  . LYS B 2 7   ? 10.10949 -6.00144  16.16927 1.000 43.27897  ? 27  LYS B NZ  1 
ATOM   962  N N   . VAL B 2 8   ? 11.35377 0.67243   16.97021 1.000 44.03613  ? 28  VAL B N   1 
ATOM   963  C CA  . VAL B 2 8   ? 10.13212 1.46664   16.97578 1.000 42.85907  ? 28  VAL B CA  1 
ATOM   964  C C   . VAL B 2 8   ? 9.18365  0.84926   15.96061 1.000 40.49201  ? 28  VAL B C   1 
ATOM   965  O O   . VAL B 2 8   ? 9.52727  0.71496   14.77918 1.000 42.71910  ? 28  VAL B O   1 
ATOM   966  C CB  . VAL B 2 8   ? 10.40896 2.94333   16.65894 1.000 40.18288  ? 28  VAL B CB  1 
ATOM   967  C CG1 . VAL B 2 8   ? 9.12326  3.75093   16.74230 1.000 41.00442  ? 28  VAL B CG1 1 
ATOM   968  C CG2 . VAL B 2 8   ? 11.45334 3.49316   17.61279 1.000 36.17351  ? 28  VAL B CG2 1 
ATOM   969  N N   . SER B 2 9   ? 8.00014  0.45928   16.42409 1.000 40.79334  ? 29  SER B N   1 
ATOM   970  C CA  . SER B 2 9   ? 7.02508  -0.23300  15.59913 1.000 43.97882  ? 29  SER B CA  1 
ATOM   971  C C   . SER B 2 9   ? 5.64871  0.38666   15.78757 1.000 46.06936  ? 29  SER B C   1 
ATOM   972  O O   . SER B 2 9   ? 5.31475  0.88829   16.86443 1.000 47.78625  ? 29  SER B O   1 
ATOM   973  C CB  . SER B 2 9   ? 6.97113  -1.72900  15.93675 1.000 43.01722  ? 29  SER B CB  1 
ATOM   974  O OG  . SER B 2 9   ? 5.96634  -2.38499  15.18514 1.000 47.81607  ? 29  SER B OG  1 
ATOM   975  N N   . ASP B 2 10  ? 4.85236  0.34959   14.71873 1.000 46.10791  ? 30  ASP B N   1 
ATOM   976  C CA  . ASP B 2 10  ? 3.45842  0.77584   14.76123 1.000 48.61692  ? 30  ASP B CA  1 
ATOM   977  C C   . ASP B 2 10  ? 2.50837  -0.36372  14.40967 1.000 53.49629  ? 30  ASP B C   1 
ATOM   978  O O   . ASP B 2 10  ? 1.34889  -0.11880  14.06146 1.000 54.46384  ? 30  ASP B O   1 
ATOM   979  C CB  . ASP B 2 10  ? 3.23106  1.97137   13.83217 1.000 48.26405  ? 30  ASP B CB  1 
ATOM   980  C CG  . ASP B 2 10  ? 3.50796  1.64574   12.37354 1.000 48.32880  ? 30  ASP B CG  1 
ATOM   981  O OD1 . ASP B 2 10  ? 4.01690  0.54206   12.08618 1.000 51.15513  ? 30  ASP B OD1 1 
ATOM   982  O OD2 . ASP B 2 10  ? 3.21331  2.49914   11.50999 1.000 47.50272  ? 30  ASP B OD2 1 
ATOM   983  N N   . GLY B 2 11  ? 2.98089  -1.60653  14.49316 1.000 56.29972  ? 31  GLY B N   1 
ATOM   984  C CA  . GLY B 2 11  ? 2.20843  -2.76289  14.11014 1.000 52.29689  ? 31  GLY B CA  1 
ATOM   985  C C   . GLY B 2 11  ? 2.39196  -3.19518  12.67193 1.000 53.99531  ? 31  GLY B C   1 
ATOM   986  O O   . GLY B 2 11  ? 2.10551  -4.35267  12.34603 1.000 53.35666  ? 31  GLY B O   1 
ATOM   987  N N   . SER B 2 12  ? 2.86669  -2.30099  11.80354 1.000 55.29396  ? 32  SER B N   1 
ATOM   988  C CA  . SER B 2 12  ? 3.17451  -2.66172  10.42282 1.000 51.37716  ? 32  SER B CA  1 
ATOM   989  C C   . SER B 2 12  ? 4.52763  -2.16506  9.93673  1.000 50.70281  ? 32  SER B C   1 
ATOM   990  O O   . SER B 2 12  ? 5.05665  -2.73898  8.97848  1.000 53.84235  ? 32  SER B O   1 
ATOM   991  C CB  . SER B 2 12  ? 2.08583  -2.14210  9.47548  1.000 49.30844  ? 32  SER B CB  1 
ATOM   992  N N   . SER B 2 13  ? 5.11449  -1.13810  10.54702 1.000 51.13104  ? 33  SER B N   1 
ATOM   993  C CA  . SER B 2 13  ? 6.42682  -0.63134  10.16779 1.000 49.85875  ? 33  SER B CA  1 
ATOM   994  C C   . SER B 2 13  ? 7.35420  -0.70184  11.37223 1.000 46.46084  ? 33  SER B C   1 
ATOM   995  O O   . SER B 2 13  ? 7.03986  -0.15029  12.43149 1.000 45.67372  ? 33  SER B O   1 
ATOM   996  C CB  . SER B 2 13  ? 6.33436  0.80796   9.65166  1.000 49.36271  ? 33  SER B CB  1 
ATOM   997  O OG  . SER B 2 13  ? 7.60545  1.43526   9.66124  1.000 49.13586  ? 33  SER B OG  1 
ATOM   998  N N   . GLU B 2 14  ? 8.49589  -1.36695  11.20655 1.000 47.28337  ? 34  GLU B N   1 
ATOM   999  C CA  . GLU B 2 14  ? 9.46528  -1.55540  12.27932 1.000 44.26507  ? 34  GLU B CA  1 
ATOM   1000 C C   . GLU B 2 14  ? 10.81054 -0.97842  11.85940 1.000 45.27685  ? 34  GLU B C   1 
ATOM   1001 O O   . GLU B 2 14  ? 11.29232 -1.25544  10.75543 1.000 44.66943  ? 34  GLU B O   1 
ATOM   1002 C CB  . GLU B 2 14  ? 9.60799  -3.03846  12.63698 1.000 40.61635  ? 34  GLU B CB  1 
ATOM   1003 N N   . ILE B 2 15  ? 11.40674 -0.17130  12.73796 1.000 43.47746  ? 35  ILE B N   1 
ATOM   1004 C CA  . ILE B 2 15  ? 12.67557 0.50031   12.47438 1.000 42.58336  ? 35  ILE B CA  1 
ATOM   1005 C C   . ILE B 2 15  ? 13.61983 0.23981   13.63943 1.000 40.90862  ? 35  ILE B C   1 
ATOM   1006 O O   . ILE B 2 15  ? 13.24233 0.42221   14.80112 1.000 42.30814  ? 35  ILE B O   1 
ATOM   1007 C CB  . ILE B 2 15  ? 12.49262 2.01719   12.27057 1.000 44.33866  ? 35  ILE B CB  1 
ATOM   1008 C CG1 . ILE B 2 15  ? 11.29143 2.30349   11.36458 1.000 44.92106  ? 35  ILE B CG1 1 
ATOM   1009 C CG2 . ILE B 2 15  ? 13.76597 2.63352   11.71040 1.000 41.17072  ? 35  ILE B CG2 1 
ATOM   1010 C CD1 . ILE B 2 15  ? 11.28056 3.70168   10.78411 1.000 44.96233  ? 35  ILE B CD1 1 
ATOM   1011 N N   . PHE B 2 16  ? 14.84538 -0.17300  13.33070 1.000 39.62196  ? 36  PHE B N   1 
ATOM   1012 C CA  . PHE B 2 16  ? 15.87594 -0.38663  14.33855 1.000 40.64662  ? 36  PHE B CA  1 
ATOM   1013 C C   . PHE B 2 16  ? 16.81295 0.81561   14.35490 1.000 41.90373  ? 36  PHE B C   1 
ATOM   1014 O O   . PHE B 2 16  ? 17.39431 1.16713   13.32438 1.000 42.57263  ? 36  PHE B O   1 
ATOM   1015 C CB  . PHE B 2 16  ? 16.65727 -1.67118  14.06133 1.000 41.91477  ? 36  PHE B CB  1 
ATOM   1016 C CG  . PHE B 2 16  ? 15.84996 -2.92649  14.23470 1.000 43.07368  ? 36  PHE B CG  1 
ATOM   1017 C CD1 . PHE B 2 16  ? 15.74722 -3.52829  15.47777 1.000 41.93212  ? 36  PHE B CD1 1 
ATOM   1018 C CD2 . PHE B 2 16  ? 15.20353 -3.51056  13.15664 1.000 40.92393  ? 36  PHE B CD2 1 
ATOM   1019 C CE1 . PHE B 2 16  ? 15.01065 -4.68305  15.64665 1.000 41.13040  ? 36  PHE B CE1 1 
ATOM   1020 C CE2 . PHE B 2 16  ? 14.46457 -4.66895  13.31952 1.000 41.36577  ? 36  PHE B CE2 1 
ATOM   1021 C CZ  . PHE B 2 16  ? 14.36904 -5.25487  14.56710 1.000 41.76159  ? 36  PHE B CZ  1 
ATOM   1022 N N   . PHE B 2 17  ? 16.95947 1.43564   15.52172 1.000 40.90297  ? 37  PHE B N   1 
ATOM   1023 C CA  . PHE B 2 17  ? 17.86474 2.55719   15.72522 1.000 42.79513  ? 37  PHE B CA  1 
ATOM   1024 C C   . PHE B 2 17  ? 18.98937 2.13383   16.65933 1.000 46.41401  ? 37  PHE B C   1 
ATOM   1025 O O   . PHE B 2 17  ? 18.74659 1.47407   17.67272 1.000 49.38197  ? 37  PHE B O   1 
ATOM   1026 C CB  . PHE B 2 17  ? 17.13580 3.76077   16.33311 1.000 42.65309  ? 37  PHE B CB  1 
ATOM   1027 C CG  . PHE B 2 17  ? 15.99772 4.27858   15.50000 1.000 42.28424  ? 37  PHE B CG  1 
ATOM   1028 C CD1 . PHE B 2 17  ? 16.21420 5.22846   14.51598 1.000 40.99953  ? 37  PHE B CD1 1 
ATOM   1029 C CD2 . PHE B 2 17  ? 14.70682 3.82128   15.70919 1.000 42.01753  ? 37  PHE B CD2 1 
ATOM   1030 C CE1 . PHE B 2 17  ? 15.16335 5.71231   13.75809 1.000 42.79795  ? 37  PHE B CE1 1 
ATOM   1031 C CE2 . PHE B 2 17  ? 13.65524 4.29917   14.95227 1.000 38.92776  ? 37  PHE B CE2 1 
ATOM   1032 C CZ  . PHE B 2 17  ? 13.88358 5.24609   13.97703 1.000 39.78828  ? 37  PHE B CZ  1 
ATOM   1033 N N   . LYS B 2 18  ? 20.21849 2.50885   16.32213 1.000 48.79891  ? 38  LYS B N   1 
ATOM   1034 C CA  . LYS B 2 18  ? 21.35668 2.34691   17.22448 1.000 48.76286  ? 38  LYS B CA  1 
ATOM   1035 C C   . LYS B 2 18  ? 21.81044 3.74882   17.61008 1.000 51.86247  ? 38  LYS B C   1 
ATOM   1036 O O   . LYS B 2 18  ? 22.45811 4.44254   16.81978 1.000 50.36322  ? 38  LYS B O   1 
ATOM   1037 C CB  . LYS B 2 18  ? 22.48085 1.53859   16.58434 1.000 48.02927  ? 38  LYS B CB  1 
ATOM   1038 C CG  . LYS B 2 18  ? 23.56756 1.14524   17.57592 1.000 48.75383  ? 38  LYS B CG  1 
ATOM   1039 C CD  . LYS B 2 18  ? 24.93743 1.09200   16.93909 1.000 47.29891  ? 38  LYS B CD  1 
ATOM   1040 C CE  . LYS B 2 18  ? 25.60886 -0.25012  17.17640 1.000 47.03850  ? 38  LYS B CE  1 
ATOM   1041 N NZ  . LYS B 2 18  ? 27.08828 -0.09505  17.30316 1.000 52.39176  ? 38  LYS B NZ  1 
ATOM   1042 N N   . ILE B 2 19  ? 21.46465 4.16590   18.82773 1.000 55.18559  ? 39  ILE B N   1 
ATOM   1043 C CA  . ILE B 2 19  ? 21.64971 5.55096   19.23620 1.000 53.03098  ? 39  ILE B CA  1 
ATOM   1044 C C   . ILE B 2 19  ? 22.28163 5.59646   20.61909 1.000 52.05275  ? 39  ILE B C   1 
ATOM   1045 O O   . ILE B 2 19  ? 22.20630 4.64445   21.39421 1.000 52.60855  ? 39  ILE B O   1 
ATOM   1046 C CB  . ILE B 2 19  ? 20.32149 6.33719   19.22309 1.000 55.05340  ? 39  ILE B CB  1 
ATOM   1047 C CG1 . ILE B 2 19  ? 19.21221 5.52417   19.89356 1.000 52.68843  ? 39  ILE B CG1 1 
ATOM   1048 C CG2 . ILE B 2 19  ? 19.93828 6.71683   17.79994 1.000 52.77865  ? 39  ILE B CG2 1 
ATOM   1049 C CD1 . ILE B 2 19  ? 18.24270 6.36246   20.70021 1.000 56.97576  ? 39  ILE B CD1 1 
ATOM   1050 N N   . LYS B 2 20  ? 22.91014 6.72916   20.92145 1.000 55.62339  ? 40  LYS B N   1 
ATOM   1051 C CA  . LYS B 2 20  ? 23.55887 6.89421   22.21410 1.000 55.42232  ? 40  LYS B CA  1 
ATOM   1052 C C   . LYS B 2 20  ? 22.53910 6.82487   23.34389 1.000 55.59669  ? 40  LYS B C   1 
ATOM   1053 O O   . LYS B 2 20  ? 21.37406 7.19943   23.18655 1.000 58.02469  ? 40  LYS B O   1 
ATOM   1054 C CB  . LYS B 2 20  ? 24.30010 8.22889   22.27736 1.000 56.37029  ? 40  LYS B CB  1 
ATOM   1055 C CG  . LYS B 2 20  ? 25.73934 8.17977   21.81008 1.000 58.33594  ? 40  LYS B CG  1 
ATOM   1056 C CD  . LYS B 2 20  ? 26.28229 9.58595   21.61791 1.000 62.35011  ? 40  LYS B CD  1 
ATOM   1057 C CE  . LYS B 2 20  ? 27.21415 9.97301   22.75577 1.000 65.91471  ? 40  LYS B CE  1 
ATOM   1058 N NZ  . LYS B 2 20  ? 28.47223 10.59958  22.27585 1.000 69.12841  ? 40  LYS B NZ  1 
ATOM   1059 N N   . LYS B 2 21  ? 22.99165 6.32791   24.49759 1.000 54.41812  ? 41  LYS B N   1 
ATOM   1060 C CA  . LYS B 2 21  ? 22.15220 6.35782   25.69001 1.000 58.59967  ? 41  LYS B CA  1 
ATOM   1061 C C   . LYS B 2 21  ? 21.81306 7.78652   26.09290 1.000 61.56672  ? 41  LYS B C   1 
ATOM   1062 O O   . LYS B 2 21  ? 20.77690 8.02579   26.72422 1.000 59.46893  ? 41  LYS B O   1 
ATOM   1063 C CB  . LYS B 2 21  ? 22.84756 5.63299   26.84341 1.000 58.63989  ? 41  LYS B CB  1 
ATOM   1064 C CG  . LYS B 2 21  ? 23.03689 4.14108   26.62460 1.000 58.62212  ? 41  LYS B CG  1 
ATOM   1065 C CD  . LYS B 2 21  ? 22.84612 3.36665   27.91970 1.000 64.57206  ? 41  LYS B CD  1 
ATOM   1066 C CE  . LYS B 2 21  ? 21.44043 3.54516   28.47274 1.000 65.60720  ? 41  LYS B CE  1 
ATOM   1067 N NZ  . LYS B 2 21  ? 20.65523 2.28037   28.40015 1.000 63.28907  ? 41  LYS B NZ  1 
ATOM   1068 N N   . THR B 2 22  ? 22.66845 8.74407   25.73646 1.000 61.21728  ? 42  THR B N   1 
ATOM   1069 C CA  . THR B 2 22  ? 22.46810 10.14855  26.05943 1.000 60.80094  ? 42  THR B CA  1 
ATOM   1070 C C   . THR B 2 22  ? 21.86152 10.93943  24.90737 1.000 58.72724  ? 42  THR B C   1 
ATOM   1071 O O   . THR B 2 22  ? 21.82744 12.17267  24.96909 1.000 61.23576  ? 42  THR B O   1 
ATOM   1072 C CB  . THR B 2 22  ? 23.79239 10.78640  26.48388 1.000 65.33753  ? 42  THR B CB  1 
ATOM   1073 O OG1 . THR B 2 22  ? 24.47952 11.27901  25.32731 1.000 65.42818  ? 42  THR B OG1 1 
ATOM   1074 C CG2 . THR B 2 22  ? 24.67046 9.76813   27.19732 1.000 67.10114  ? 42  THR B CG2 1 
ATOM   1075 N N   . THR B 2 23  ? 21.38724 10.26583  23.85964 1.000 56.06883  ? 43  THR B N   1 
ATOM   1076 C CA  . THR B 2 23  ? 20.78753 11.16707  22.88541 1.000 59.51694  ? 43  THR B CA  1 
ATOM   1077 C C   . THR B 2 23  ? 19.28288 11.27804  23.11176 1.000 59.54420  ? 43  THR B C   1 
ATOM   1078 O O   . THR B 2 23  ? 18.63374 10.29347  23.48483 1.000 58.71056  ? 43  THR B O   1 
ATOM   1079 C CB  . THR B 2 23  ? 21.06512 10.69716  21.45258 1.000 59.28811  ? 43  THR B CB  1 
ATOM   1080 O OG1 . THR B 2 23  ? 20.69719 11.72695  20.52505 1.000 59.09858  ? 43  THR B OG1 1 
ATOM   1081 C CG2 . THR B 2 23  ? 20.30285 9.42134   21.12256 1.000 57.68401  ? 43  THR B CG2 1 
ATOM   1082 N N   . PRO B 2 24  ? 18.71196 12.47025  22.94209 1.000 57.85777  ? 44  PRO B N   1 
ATOM   1083 C CA  . PRO B 2 24  ? 17.26266 12.62026  23.11413 1.000 57.84407  ? 44  PRO B CA  1 
ATOM   1084 C C   . PRO B 2 24  ? 16.49522 11.80172  22.08761 1.000 58.45280  ? 44  PRO B C   1 
ATOM   1085 O O   . PRO B 2 24  ? 16.93512 11.61497  20.95079 1.000 58.59580  ? 44  PRO B O   1 
ATOM   1086 C CB  . PRO B 2 24  ? 17.03165 14.12409  22.91895 1.000 57.53410  ? 44  PRO B CB  1 
ATOM   1087 C CG  . PRO B 2 24  ? 18.36451 14.75577  23.16143 1.000 57.89475  ? 44  PRO B CG  1 
ATOM   1088 C CD  . PRO B 2 24  ? 19.37932 13.75925  22.69563 1.000 57.38316  ? 44  PRO B CD  1 
ATOM   1089 N N   . LEU B 2 25  ? 15.32802 11.31499  22.50381 1.000 56.40736  ? 45  LEU B N   1 
ATOM   1090 C CA  . LEU B 2 25  ? 14.48890 10.49244  21.64365 1.000 52.50937  ? 45  LEU B CA  1 
ATOM   1091 C C   . LEU B 2 25  ? 13.73741 11.30372  20.59706 1.000 49.84373  ? 45  LEU B C   1 
ATOM   1092 O O   . LEU B 2 25  ? 13.04156 10.71137  19.76589 1.000 48.18030  ? 45  LEU B O   1 
ATOM   1093 C CB  . LEU B 2 25  ? 13.50222 9.68708   22.49304 1.000 50.40456  ? 45  LEU B CB  1 
ATOM   1094 C CG  . LEU B 2 25  ? 14.15460 8.62444   23.38083 1.000 53.32912  ? 45  LEU B CG  1 
ATOM   1095 C CD1 . LEU B 2 25  ? 13.16446 8.05822   24.37951 1.000 49.75291  ? 45  LEU B CD1 1 
ATOM   1096 C CD2 . LEU B 2 25  ? 14.75006 7.51376   22.52793 1.000 51.13916  ? 45  LEU B CD2 1 
ATOM   1097 N N   . ARG B 2 26  ? 13.85925 12.63432  20.61938 1.000 52.19628  ? 46  ARG B N   1 
ATOM   1098 C CA  . ARG B 2 26  ? 13.18314 13.46325  19.62612 1.000 51.51746  ? 46  ARG B CA  1 
ATOM   1099 C C   . ARG B 2 26  ? 13.59132 13.07723  18.20955 1.000 50.89230  ? 46  ARG B C   1 
ATOM   1100 O O   . ARG B 2 26  ? 12.75235 13.04709  17.30312 1.000 50.07719  ? 46  ARG B O   1 
ATOM   1101 C CB  . ARG B 2 26  ? 13.48217 14.94067  19.88431 1.000 51.93725  ? 46  ARG B CB  1 
ATOM   1102 C CG  . ARG B 2 26  ? 12.86919 15.89123  18.86368 1.000 55.13897  ? 46  ARG B CG  1 
ATOM   1103 C CD  . ARG B 2 26  ? 12.84346 17.32148  19.38218 1.000 57.14460  ? 46  ARG B CD  1 
ATOM   1104 N NE  . ARG B 2 26  ? 11.65550 18.04739  18.94816 1.000 63.75403  ? 46  ARG B NE  1 
ATOM   1105 C CZ  . ARG B 2 26  ? 11.62191 19.35177  18.70996 1.000 71.03818  ? 46  ARG B CZ  1 
ATOM   1106 N NH1 . ARG B 2 26  ? 12.69799 20.10871  18.85331 1.000 66.44580  ? 46  ARG B NH1 1 
ATOM   1107 N NH2 . ARG B 2 26  ? 10.48055 19.91098  18.31738 1.000 70.39724  ? 46  ARG B NH2 1 
ATOM   1108 N N   . ARG B 2 27  ? 14.87595 12.77858  17.99857 1.000 49.23680  ? 47  ARG B N   1 
ATOM   1109 C CA  . ARG B 2 27  ? 15.33690 12.41973  16.66042 1.000 48.96665  ? 47  ARG B CA  1 
ATOM   1110 C C   . ARG B 2 27  ? 14.78814 11.06483  16.22332 1.000 48.48521  ? 47  ARG B C   1 
ATOM   1111 O O   . ARG B 2 27  ? 14.46827 10.87264  15.04671 1.000 47.94847  ? 47  ARG B O   1 
ATOM   1112 C CB  . ARG B 2 27  ? 16.86476 12.43154  16.61035 1.000 49.75289  ? 47  ARG B CB  1 
ATOM   1113 C CG  . ARG B 2 27  ? 17.45643 13.81270  16.38320 1.000 49.33812  ? 47  ARG B CG  1 
ATOM   1114 C CD  . ARG B 2 27  ? 18.55849 13.77884  15.33788 1.000 53.74504  ? 47  ARG B CD  1 
ATOM   1115 N NE  . ARG B 2 27  ? 19.00922 15.11739  14.97487 1.000 60.20434  ? 47  ARG B NE  1 
ATOM   1116 C CZ  . ARG B 2 27  ? 18.61400 15.77232  13.89150 1.000 60.62982  ? 47  ARG B CZ  1 
ATOM   1117 N NH1 . ARG B 2 27  ? 17.74994 15.24297  13.04039 1.000 58.13375  ? 47  ARG B NH1 1 
ATOM   1118 N NH2 . ARG B 2 27  ? 19.09751 16.98919  13.65623 1.000 64.64012  ? 47  ARG B NH2 1 
ATOM   1119 N N   . LEU B 2 28  ? 14.66283 10.11642  17.15345 1.000 49.84774  ? 48  LEU B N   1 
ATOM   1120 C CA  . LEU B 2 28  ? 14.12104 8.80163   16.81414 1.000 45.94667  ? 48  LEU B CA  1 
ATOM   1121 C C   . LEU B 2 28  ? 12.65671 8.89923   16.39255 1.000 44.77278  ? 48  LEU B C   1 
ATOM   1122 O O   . LEU B 2 28  ? 12.25702 8.37187   15.34121 1.000 42.08599  ? 48  LEU B O   1 
ATOM   1123 C CB  . LEU B 2 28  ? 14.29336 7.86258   18.01213 1.000 45.11323  ? 48  LEU B CB  1 
ATOM   1124 C CG  . LEU B 2 28  ? 13.51871 6.54935   18.12070 1.000 42.16438  ? 48  LEU B CG  1 
ATOM   1125 C CD1 . LEU B 2 28  ? 14.39531 5.49109   18.76138 1.000 41.75408  ? 48  LEU B CD1 1 
ATOM   1126 C CD2 . LEU B 2 28  ? 12.25814 6.74794   18.94855 1.000 41.58630  ? 48  LEU B CD2 1 
ATOM   1127 N N   . MET B 2 29  ? 11.84355 9.57732   17.20644 1.000 43.92294  ? 49  MET B N   1 
ATOM   1128 C CA  . MET B 2 29  ? 10.44498 9.79501   16.85774 1.000 43.06979  ? 49  MET B CA  1 
ATOM   1129 C C   . MET B 2 29  ? 10.32640 10.58922  15.56579 1.000 46.29462  ? 49  MET B C   1 
ATOM   1130 O O   . MET B 2 29  ? 9.45482  10.31131  14.73271 1.000 46.50922  ? 49  MET B O   1 
ATOM   1131 C CB  . MET B 2 29  ? 9.73178  10.51744  18.00138 1.000 44.09481  ? 49  MET B CB  1 
ATOM   1132 C CG  . MET B 2 29  ? 9.96605  9.89929   19.37315 1.000 45.06386  ? 49  MET B CG  1 
ATOM   1133 S SD  . MET B 2 29  ? 10.02372 11.12386  20.69908 1.000 48.41093  ? 49  MET B SD  1 
ATOM   1134 C CE  . MET B 2 29  ? 8.34111  11.07370  21.30848 1.000 48.12332  ? 49  MET B CE  1 
ATOM   1135 N N   . GLU B 2 30  ? 11.20094 11.58080  15.38167 1.000 45.39421  ? 50  GLU B N   1 
ATOM   1136 C CA  . GLU B 2 30  ? 11.18623 12.37504  14.16020 1.000 44.09123  ? 50  GLU B CA  1 
ATOM   1137 C C   . GLU B 2 30  ? 11.45960 11.51021  12.93806 1.000 44.37975  ? 50  GLU B C   1 
ATOM   1138 O O   . GLU B 2 30  ? 10.77614 11.63232  11.92071 1.000 45.15415  ? 50  GLU B O   1 
ATOM   1139 C CB  . GLU B 2 30  ? 12.21025 13.50475  14.25805 1.000 46.48881  ? 50  GLU B CB  1 
ATOM   1140 C CG  . GLU B 2 30  ? 11.59782 14.88342  14.41409 1.000 52.19794  ? 50  GLU B CG  1 
ATOM   1141 C CD  . GLU B 2 30  ? 12.60205 15.91319  14.88653 1.000 53.93957  ? 50  GLU B CD  1 
ATOM   1142 O OE1 . GLU B 2 30  ? 13.79099 15.56113  15.03636 1.000 54.06578  ? 50  GLU B OE1 1 
ATOM   1143 O OE2 . GLU B 2 30  ? 12.20320 17.07627  15.10326 1.000 58.48878  ? 50  GLU B OE2 1 
ATOM   1144 N N   . ALA B 2 31  ? 12.46193 10.63200  13.01722 1.000 42.69415  ? 51  ALA B N   1 
ATOM   1145 C CA  . ALA B 2 31  ? 12.77765 9.76914   11.88313 1.000 42.14277  ? 51  ALA B CA  1 
ATOM   1146 C C   . ALA B 2 31  ? 11.62215 8.82872   11.57116 1.000 42.69180  ? 51  ALA B C   1 
ATOM   1147 O O   . ALA B 2 31  ? 11.26070 8.63845   10.39881 1.000 45.26895  ? 51  ALA B O   1 
ATOM   1148 C CB  . ALA B 2 31  ? 14.05550 8.97829   12.16355 1.000 40.89522  ? 51  ALA B CB  1 
ATOM   1149 N N   . PHE B 2 32  ? 11.02102 8.23862   12.61051 1.000 44.43382  ? 52  PHE B N   1 
ATOM   1150 C CA  . PHE B 2 32  ? 9.88689  7.34820   12.38115 1.000 43.53922  ? 52  PHE B CA  1 
ATOM   1151 C C   . PHE B 2 32  ? 8.72538  8.09368   11.73453 1.000 43.86598  ? 52  PHE B C   1 
ATOM   1152 O O   . PHE B 2 32  ? 8.06098  7.56305   10.83697 1.000 44.37428  ? 52  PHE B O   1 
ATOM   1153 C CB  . PHE B 2 32  ? 9.44305  6.69388   13.68977 1.000 40.29498  ? 52  PHE B CB  1 
ATOM   1154 C CG  . PHE B 2 32  ? 8.49834  5.53803   13.49662 1.000 39.60714  ? 52  PHE B CG  1 
ATOM   1155 C CD1 . PHE B 2 32  ? 8.98174  4.25446   13.30487 1.000 47.10207  ? 52  PHE B CD1 1 
ATOM   1156 C CD2 . PHE B 2 32  ? 7.12783  5.73614   13.49969 1.000 41.69780  ? 52  PHE B CD2 1 
ATOM   1157 C CE1 . PHE B 2 32  ? 8.11717  3.18960   13.12206 1.000 44.89119  ? 52  PHE B CE1 1 
ATOM   1158 C CE2 . PHE B 2 32  ? 6.25760  4.67555   13.31740 1.000 44.54786  ? 52  PHE B CE2 1 
ATOM   1159 C CZ  . PHE B 2 32  ? 6.75358  3.40107   13.12896 1.000 44.58158  ? 52  PHE B CZ  1 
ATOM   1160 N N   . ALA B 2 33  ? 8.46321  9.32546   12.17914 1.000 43.27576  ? 53  ALA B N   1 
ATOM   1161 C CA  . ALA B 2 33  ? 7.38453  10.11104  11.58757 1.000 45.26890  ? 53  ALA B CA  1 
ATOM   1162 C C   . ALA B 2 33  ? 7.69695  10.49903  10.14610 1.000 47.55559  ? 53  ALA B C   1 
ATOM   1163 O O   . ALA B 2 33  ? 6.81968  10.43092  9.27734  1.000 49.70332  ? 53  ALA B O   1 
ATOM   1164 C CB  . ALA B 2 33  ? 7.12035  11.35523  12.43334 1.000 47.64763  ? 53  ALA B CB  1 
ATOM   1165 N N   . LYS B 2 34  ? 8.93835  10.91372  9.87399  1.000 47.69149  ? 54  LYS B N   1 
ATOM   1166 C CA  . LYS B 2 34  ? 9.30577  11.34022  8.52670  1.000 50.44461  ? 54  LYS B CA  1 
ATOM   1167 C C   . LYS B 2 34  ? 9.18840  10.19340  7.53582  1.000 50.88127  ? 54  LYS B C   1 
ATOM   1168 O O   . LYS B 2 34  ? 8.73973  10.39046  6.40035  1.000 53.74702  ? 54  LYS B O   1 
ATOM   1169 C CB  . LYS B 2 34  ? 10.73011 11.90175  8.50217  1.000 50.94102  ? 54  LYS B CB  1 
ATOM   1170 C CG  . LYS B 2 34  ? 10.97625 13.12394  9.37211  1.000 51.72196  ? 54  LYS B CG  1 
ATOM   1171 C CD  . LYS B 2 34  ? 10.60944 14.42465  8.68794  1.000 55.74589  ? 54  LYS B CD  1 
ATOM   1172 C CE  . LYS B 2 34  ? 10.51422 15.54405  9.71300  1.000 56.88980  ? 54  LYS B CE  1 
ATOM   1173 N NZ  . LYS B 2 34  ? 9.66941  16.67509  9.24900  1.000 60.73660  ? 54  LYS B NZ  1 
ATOM   1174 N N   . ARG B 2 35  ? 9.59958  8.98713   7.93947  1.000 48.60323  ? 55  ARG B N   1 
ATOM   1175 C CA  . ARG B 2 35  ? 9.53670  7.86077   7.01251  1.000 49.72256  ? 55  ARG B CA  1 
ATOM   1176 C C   . ARG B 2 35  ? 8.10436  7.53897   6.60069  1.000 51.76957  ? 55  ARG B C   1 
ATOM   1177 O O   . ARG B 2 35  ? 7.88261  6.98464   5.51790  1.000 54.33365  ? 55  ARG B O   1 
ATOM   1178 C CB  . ARG B 2 35  ? 10.22078 6.63593   7.61731  1.000 47.45503  ? 55  ARG B CB  1 
ATOM   1179 C CG  . ARG B 2 35  ? 11.64124 6.46350   7.10314  1.000 52.25932  ? 55  ARG B CG  1 
ATOM   1180 C CD  . ARG B 2 35  ? 12.49018 5.57099   7.98058  1.000 50.84488  ? 55  ARG B CD  1 
ATOM   1181 N NE  . ARG B 2 35  ? 12.42554 4.17482   7.56588  1.000 49.11510  ? 55  ARG B NE  1 
ATOM   1182 C CZ  . ARG B 2 35  ? 13.33799 3.26189   7.86798  1.000 45.56782  ? 55  ARG B CZ  1 
ATOM   1183 N NH1 . ARG B 2 35  ? 14.43902 3.57873   8.52808  1.000 43.97190  ? 55  ARG B NH1 1 
ATOM   1184 N NH2 . ARG B 2 35  ? 13.14339 2.00089   7.49321  1.000 47.04446  ? 55  ARG B NH2 1 
ATOM   1185 N N   . GLN B 2 36  ? 7.12424  7.88117   7.43348  1.000 50.89672  ? 56  GLN B N   1 
ATOM   1186 C CA  . GLN B 2 36  ? 5.72043  7.74086   7.06920  1.000 53.30590  ? 56  GLN B CA  1 
ATOM   1187 C C   . GLN B 2 36  ? 5.14047  9.00428   6.44566  1.000 56.01789  ? 56  GLN B C   1 
ATOM   1188 O O   . GLN B 2 36  ? 3.94437  9.03133   6.13681  1.000 58.48058  ? 56  GLN B O   1 
ATOM   1189 C CB  . GLN B 2 36  ? 4.88720  7.34521   8.29390  1.000 51.86449  ? 56  GLN B CB  1 
ATOM   1190 C CG  . GLN B 2 36  ? 4.54264  5.86525   8.36255  1.000 52.76265  ? 56  GLN B CG  1 
ATOM   1191 C CD  . GLN B 2 36  ? 5.69613  5.01940   8.85789  1.000 55.42318  ? 56  GLN B CD  1 
ATOM   1192 O OE1 . GLN B 2 36  ? 5.93211  4.91836   10.06162 1.000 50.33800  ? 56  GLN B OE1 1 
ATOM   1193 N NE2 . GLN B 2 36  ? 6.42498  4.40805   7.93060  1.000 54.84955  ? 56  GLN B NE2 1 
ATOM   1194 N N   . GLY B 2 37  ? 5.95029  10.03920  6.24848  1.000 56.95773  ? 57  GLY B N   1 
ATOM   1195 C CA  . GLY B 2 37  ? 5.44922  11.29595  5.71912  1.000 60.62511  ? 57  GLY B CA  1 
ATOM   1196 C C   . GLY B 2 37  ? 4.52449  12.03573  6.66100  1.000 58.20239  ? 57  GLY B C   1 
ATOM   1197 O O   . GLY B 2 37  ? 3.54152  12.63996  6.21215  1.000 60.61343  ? 57  GLY B O   1 
ATOM   1198 N N   . LYS B 2 38  ? 4.81669  12.00572  7.95929  1.000 53.96073  ? 58  LYS B N   1 
ATOM   1199 C CA  . LYS B 2 38  ? 4.02247  12.68612  8.97064  1.000 53.30873  ? 58  LYS B CA  1 
ATOM   1200 C C   . LYS B 2 38  ? 4.94695  13.46509  9.89524  1.000 52.39555  ? 58  LYS B C   1 
ATOM   1201 O O   . LYS B 2 38  ? 6.17116  13.31715  9.85851  1.000 52.55530  ? 58  LYS B O   1 
ATOM   1202 C CB  . LYS B 2 38  ? 3.18058  11.69978  9.79329  1.000 52.00079  ? 58  LYS B CB  1 
ATOM   1203 C CG  . LYS B 2 38  ? 2.56995  10.56119  8.99803  1.000 50.94475  ? 58  LYS B CG  1 
ATOM   1204 C CD  . LYS B 2 38  ? 2.09724  9.45167   9.92191  1.000 57.10613  ? 58  LYS B CD  1 
ATOM   1205 C CE  . LYS B 2 38  ? 0.61382  9.58325   10.23243 1.000 59.25827  ? 58  LYS B CE  1 
ATOM   1206 N NZ  . LYS B 2 38  ? 0.04261  8.30902   10.75188 1.000 57.37929  ? 58  LYS B NZ  1 
ATOM   1207 N N   . GLU B 2 39  ? 4.34638  14.30411  10.73209 1.000 52.34663  ? 59  GLU B N   1 
ATOM   1208 C CA  . GLU B 2 39  ? 5.08116  14.99467  11.77938 1.000 52.79903  ? 59  GLU B CA  1 
ATOM   1209 C C   . GLU B 2 39  ? 5.01974  14.18579  13.06943 1.000 53.14802  ? 59  GLU B C   1 
ATOM   1210 O O   . GLU B 2 39  ? 4.09269  13.40154  13.28965 1.000 51.78501  ? 59  GLU B O   1 
ATOM   1211 C CB  . GLU B 2 39  ? 4.52380  16.40112  12.00516 1.000 52.95361  ? 59  GLU B CB  1 
ATOM   1212 C CG  . GLU B 2 39  ? 5.31087  17.49552  11.29721 1.000 56.42261  ? 59  GLU B CG  1 
ATOM   1213 C CD  . GLU B 2 39  ? 6.78411  17.49062  11.66737 1.000 58.55182  ? 59  GLU B CD  1 
ATOM   1214 O OE1 . GLU B 2 39  ? 7.09895  17.36428  12.87014 1.000 57.25275  ? 59  GLU B OE1 1 
ATOM   1215 O OE2 . GLU B 2 39  ? 7.62846  17.61140  10.75423 1.000 59.42674  ? 59  GLU B OE2 1 
ATOM   1216 N N   . MET B 2 40  ? 6.02587  14.38551  13.92435 1.000 53.76307  ? 60  MET B N   1 
ATOM   1217 C CA  . MET B 2 40  ? 6.17167  13.54601  15.11082 1.000 53.99187  ? 60  MET B CA  1 
ATOM   1218 C C   . MET B 2 40  ? 5.01210  13.73673  16.08329 1.000 55.38979  ? 60  MET B C   1 
ATOM   1219 O O   . MET B 2 40  ? 4.54396  12.76989  16.69692 1.000 56.98625  ? 60  MET B O   1 
ATOM   1220 C CB  . MET B 2 40  ? 7.51015  13.83713  15.79118 1.000 50.71788  ? 60  MET B CB  1 
ATOM   1221 C CG  . MET B 2 40  ? 7.51368  13.63745  17.29603 1.000 53.13091  ? 60  MET B CG  1 
ATOM   1222 S SD  . MET B 2 40  ? 9.02433  14.24208  18.07238 1.000 53.67341  ? 60  MET B SD  1 
ATOM   1223 C CE  . MET B 2 40  ? 9.27749  15.77769  17.18482 1.000 53.42560  ? 60  MET B CE  1 
ATOM   1224 N N   . ASP B 2 41  ? 4.52548  14.97282  16.22957 1.000 54.19722  ? 61  ASP B N   1 
ATOM   1225 C CA  . ASP B 2 41  ? 3.44831  15.24605  17.17658 1.000 53.84385  ? 61  ASP B CA  1 
ATOM   1226 C C   . ASP B 2 41  ? 2.14531  14.54968  16.80276 1.000 53.00659  ? 61  ASP B C   1 
ATOM   1227 O O   . ASP B 2 41  ? 1.25118  14.44001  17.64928 1.000 47.77169  ? 61  ASP B O   1 
ATOM   1228 C CB  . ASP B 2 41  ? 3.21802  16.75334  17.29172 1.000 53.48611  ? 61  ASP B CB  1 
ATOM   1229 C CG  . ASP B 2 41  ? 4.39774  17.47534  17.90972 1.000 58.70166  ? 61  ASP B CG  1 
ATOM   1230 O OD1 . ASP B 2 41  ? 4.67658  17.24207  19.10470 1.000 57.25262  ? 61  ASP B OD1 1 
ATOM   1231 O OD2 . ASP B 2 41  ? 5.04597  18.27556  17.20244 1.000 59.84279  ? 61  ASP B OD2 1 
ATOM   1232 N N   . SER B 2 42  ? 2.01627  14.08074  15.56183 1.000 51.97033  ? 62  SER B N   1 
ATOM   1233 C CA  . SER B 2 42  ? 0.85009  13.30933  15.15415 1.000 49.13477  ? 62  SER B CA  1 
ATOM   1234 C C   . SER B 2 42  ? 0.87413  11.87807  15.67230 1.000 50.78955  ? 62  SER B C   1 
ATOM   1235 O O   . SER B 2 42  ? -0.12474 11.16632  15.51883 1.000 51.97853  ? 62  SER B O   1 
ATOM   1236 C CB  . SER B 2 42  ? 0.73541  13.29172  13.62824 1.000 48.09515  ? 62  SER B CB  1 
ATOM   1237 O OG  . SER B 2 42  ? -0.08879 14.34584  13.16537 1.000 51.50748  ? 62  SER B OG  1 
ATOM   1238 N N   . LEU B 2 43  ? 1.97798  11.43919  16.27202 1.000 49.56620  ? 63  LEU B N   1 
ATOM   1239 C CA  . LEU B 2 43  ? 2.13911  10.06110  16.70833 1.000 47.63801  ? 63  LEU B CA  1 
ATOM   1240 C C   . LEU B 2 43  ? 2.39085  9.99527   18.20822 1.000 49.18970  ? 63  LEU B C   1 
ATOM   1241 O O   . LEU B 2 43  ? 3.14418  10.80129  18.76371 1.000 50.19338  ? 63  LEU B O   1 
ATOM   1242 C CB  . LEU B 2 43  ? 3.28991  9.37439   15.96241 1.000 47.76703  ? 63  LEU B CB  1 
ATOM   1243 C CG  . LEU B 2 43  ? 3.20429  9.32265   14.43532 1.000 48.95226  ? 63  LEU B CG  1 
ATOM   1244 C CD1 . LEU B 2 43  ? 4.57023  9.04919   13.82529 1.000 49.81659  ? 63  LEU B CD1 1 
ATOM   1245 C CD2 . LEU B 2 43  ? 2.19626  8.27466   13.98684 1.000 51.27572  ? 63  LEU B CD2 1 
ATOM   1246 N N   . ARG B 2 44  ? 1.74796  9.02462   18.84871 1.000 50.96121  ? 64  ARG B N   1 
ATOM   1247 C CA  . ARG B 2 44  ? 1.99225  8.68767   20.24341 1.000 49.22852  ? 64  ARG B CA  1 
ATOM   1248 C C   . ARG B 2 44  ? 3.10435  7.65048   20.31465 1.000 46.02409  ? 64  ARG B C   1 
ATOM   1249 O O   . ARG B 2 44  ? 3.06267  6.64176   19.60409 1.000 46.54524  ? 64  ARG B O   1 
ATOM   1250 C CB  . ARG B 2 44  ? 0.72342  8.13404   20.89328 1.000 51.37978  ? 64  ARG B CB  1 
ATOM   1251 C CG  . ARG B 2 44  ? -0.20865 9.17350   21.48232 1.000 59.16935  ? 64  ARG B CG  1 
ATOM   1252 C CD  . ARG B 2 44  ? -1.53738 8.53839   21.86386 1.000 58.57149  ? 64  ARG B CD  1 
ATOM   1253 N NE  . ARG B 2 44  ? -1.56737 8.11878   23.25972 1.000 61.17383  ? 64  ARG B NE  1 
ATOM   1254 C CZ  . ARG B 2 44  ? -1.91276 8.90396   24.27111 1.000 67.68927  ? 64  ARG B CZ  1 
ATOM   1255 N NH1 . ARG B 2 44  ? -2.26711 10.16413  24.07900 1.000 68.38385  ? 64  ARG B NH1 1 
ATOM   1256 N NH2 . ARG B 2 44  ? -1.90334 8.41253   25.50649 1.000 67.61134  ? 64  ARG B NH2 1 
ATOM   1257 N N   . PHE B 2 45  ? 4.09361  7.89790   21.16754 1.000 44.87578  ? 65  PHE B N   1 
ATOM   1258 C CA  . PHE B 2 45  ? 5.21679  6.98768   21.35377 1.000 46.78944  ? 65  PHE B CA  1 
ATOM   1259 C C   . PHE B 2 45  ? 5.20482  6.48888   22.79065 1.000 50.54119  ? 65  PHE B C   1 
ATOM   1260 O O   . PHE B 2 45  ? 5.24389  7.29100   23.72958 1.000 52.56642  ? 65  PHE B O   1 
ATOM   1261 C CB  . PHE B 2 45  ? 6.53832  7.67926   21.01759 1.000 44.57452  ? 65  PHE B CB  1 
ATOM   1262 C CG  . PHE B 2 45  ? 6.65640  8.07643   19.57412 1.000 41.28942  ? 65  PHE B CG  1 
ATOM   1263 C CD1 . PHE B 2 45  ? 7.18692  7.20080   18.64130 1.000 43.29588  ? 65  PHE B CD1 1 
ATOM   1264 C CD2 . PHE B 2 45  ? 6.21647  9.31750   19.14584 1.000 41.89900  ? 65  PHE B CD2 1 
ATOM   1265 C CE1 . PHE B 2 45  ? 7.28962  7.56254   17.31012 1.000 41.21768  ? 65  PHE B CE1 1 
ATOM   1266 C CE2 . PHE B 2 45  ? 6.31528  9.68446   17.81845 1.000 43.55720  ? 65  PHE B CE2 1 
ATOM   1267 C CZ  . PHE B 2 45  ? 6.85212  8.80608   16.89898 1.000 42.16420  ? 65  PHE B CZ  1 
ATOM   1268 N N   . LEU B 2 46  ? 5.15719  5.16935   22.95776 1.000 49.93174  ? 66  LEU B N   1 
ATOM   1269 C CA  . LEU B 2 46  ? 4.96638  4.54426   24.25958 1.000 50.35389  ? 66  LEU B CA  1 
ATOM   1270 C C   . LEU B 2 46  ? 6.10068  3.57293   24.55295 1.000 50.70211  ? 66  LEU B C   1 
ATOM   1271 O O   . LEU B 2 46  ? 6.44567  2.74064   23.70772 1.000 49.71163  ? 66  LEU B O   1 
ATOM   1272 C CB  . LEU B 2 46  ? 3.62759  3.80290   24.31781 1.000 51.76481  ? 66  LEU B CB  1 
ATOM   1273 C CG  . LEU B 2 46  ? 2.39011  4.51167   23.76431 1.000 51.44496  ? 66  LEU B CG  1 
ATOM   1274 C CD1 . LEU B 2 46  ? 1.17534  3.60216   23.86120 1.000 48.35069  ? 66  LEU B CD1 1 
ATOM   1275 C CD2 . LEU B 2 46  ? 2.13615  5.81984   24.49189 1.000 54.76030  ? 66  LEU B CD2 1 
ATOM   1276 N N   . TYR B 2 47  ? 6.67271  3.68016   25.74980 1.000 52.46103  ? 67  TYR B N   1 
ATOM   1277 C CA  . TYR B 2 47  ? 7.58012  2.67774   26.29246 1.000 54.20481  ? 67  TYR B CA  1 
ATOM   1278 C C   . TYR B 2 47  ? 6.96872  2.11312   27.56354 1.000 57.61382  ? 67  TYR B C   1 
ATOM   1279 O O   . TYR B 2 47  ? 6.58668  2.87404   28.45877 1.000 59.60951  ? 67  TYR B O   1 
ATOM   1280 C CB  . TYR B 2 47  ? 8.95872  3.26126   26.59608 1.000 54.05404  ? 67  TYR B CB  1 
ATOM   1281 C CG  . TYR B 2 47  ? 9.93085  2.25123   27.15777 1.000 56.33128  ? 67  TYR B CG  1 
ATOM   1282 C CD1 . TYR B 2 47  ? 10.18358 1.05710   26.49536 1.000 56.71073  ? 67  TYR B CD1 1 
ATOM   1283 C CD2 . TYR B 2 47  ? 10.58344 2.48499   28.36012 1.000 58.73135  ? 67  TYR B CD2 1 
ATOM   1284 C CE1 . TYR B 2 47  ? 11.06875 0.12894   27.01095 1.000 59.40516  ? 67  TYR B CE1 1 
ATOM   1285 C CE2 . TYR B 2 47  ? 11.46822 1.56424   28.88358 1.000 61.31466  ? 67  TYR B CE2 1 
ATOM   1286 C CZ  . TYR B 2 47  ? 11.70750 0.38870   28.20596 1.000 61.63916  ? 67  TYR B CZ  1 
ATOM   1287 O OH  . TYR B 2 47  ? 12.58948 -0.52823  28.72810 1.000 64.78591  ? 67  TYR B OH  1 
ATOM   1288 N N   . ASP B 2 48  ? 6.88617  0.78451   27.64158 1.000 59.41771  ? 68  ASP B N   1 
ATOM   1289 C CA  . ASP B 2 48  ? 6.21233  0.10494   28.74853 1.000 63.19228  ? 68  ASP B CA  1 
ATOM   1290 C C   . ASP B 2 48  ? 4.79689  0.64694   28.93083 1.000 63.58120  ? 68  ASP B C   1 
ATOM   1291 O O   . ASP B 2 48  ? 4.33130  0.87071   30.05075 1.000 66.76637  ? 68  ASP B O   1 
ATOM   1292 C CB  . ASP B 2 48  ? 7.01793  0.21763   30.04522 1.000 66.27489  ? 68  ASP B CB  1 
ATOM   1293 N N   . GLY B 2 49  ? 4.11838  0.87823   27.80605 1.000 60.82394  ? 69  GLY B N   1 
ATOM   1294 C CA  . GLY B 2 49  ? 2.76585  1.42459   27.73132 1.000 60.98896  ? 69  GLY B CA  1 
ATOM   1295 C C   . GLY B 2 49  ? 2.66458  2.83993   28.28712 1.000 61.29669  ? 69  GLY B C   1 
ATOM   1296 O O   . GLY B 2 49  ? 1.55669  3.31093   28.56548 1.000 62.85908  ? 69  GLY B O   1 
ATOM   1297 N N   . ILE B 2 50  ? 3.78616  3.53590   28.45387 1.000 60.31151  ? 70  ILE B N   1 
ATOM   1298 C CA  . ILE B 2 50  ? 3.80722  4.88289   29.01187 1.000 61.14822  ? 70  ILE B CA  1 
ATOM   1299 C C   . ILE B 2 50  ? 4.38536  5.83059   27.97073 1.000 60.06899  ? 70  ILE B C   1 
ATOM   1300 O O   . ILE B 2 50  ? 5.43005  5.54291   27.37367 1.000 55.38535  ? 70  ILE B O   1 
ATOM   1301 C CB  . ILE B 2 50  ? 4.60820  4.93821   30.32504 1.000 64.33766  ? 70  ILE B CB  1 
ATOM   1302 C CG1 . ILE B 2 50  ? 3.88417  4.12946   31.40119 1.000 68.85119  ? 70  ILE B CG1 1 
ATOM   1303 C CG2 . ILE B 2 50  ? 4.79536  6.37562   30.78297 1.000 65.28842  ? 70  ILE B CG2 1 
ATOM   1304 C CD1 . ILE B 2 50  ? 4.79828  3.45547   32.38652 1.000 71.83416  ? 70  ILE B CD1 1 
ATOM   1305 N N   . ARG B 2 51  ? 3.70546  6.95531   27.75512 1.000 64.49210  ? 71  ARG B N   1 
ATOM   1306 C CA  . ARG B 2 51  ? 4.11379  7.89845   26.72474 1.000 61.63975  ? 71  ARG B CA  1 
ATOM   1307 C C   . ARG B 2 51  ? 5.46846  8.51478   27.05139 1.000 61.35150  ? 71  ARG B C   1 
ATOM   1308 O O   . ARG B 2 51  ? 5.85164  8.65791   28.21553 1.000 63.97849  ? 71  ARG B O   1 
ATOM   1309 C CB  . ARG B 2 51  ? 3.07211  9.00345   26.55743 1.000 62.56588  ? 71  ARG B CB  1 
ATOM   1310 C CG  . ARG B 2 51  ? 3.04646  9.60866   25.16151 1.000 61.55565  ? 71  ARG B CG  1 
ATOM   1311 C CD  . ARG B 2 51  ? 2.73153  11.09233  25.20574 1.000 61.25962  ? 71  ARG B CD  1 
ATOM   1312 N NE  . ARG B 2 51  ? 2.38971  11.62199  23.89125 1.000 62.44435  ? 71  ARG B NE  1 
ATOM   1313 C CZ  . ARG B 2 51  ? 1.16497  11.96851  23.51995 1.000 62.99212  ? 71  ARG B CZ  1 
ATOM   1314 N NH1 . ARG B 2 51  ? 0.13500  11.85144  24.34168 1.000 63.53395  ? 71  ARG B NH1 1 
ATOM   1315 N NH2 . ARG B 2 51  ? 0.96916  12.44652  22.29433 1.000 62.68891  ? 71  ARG B NH2 1 
ATOM   1316 N N   . ILE B 2 52  ? 6.19144  8.88512   25.99858 1.000 59.63436  ? 72  ILE B N   1 
ATOM   1317 C CA  . ILE B 2 52  ? 7.55071  9.39890   26.09886 1.000 58.27988  ? 72  ILE B CA  1 
ATOM   1318 C C   . ILE B 2 52  ? 7.55999  10.85155  25.64820 1.000 58.53433  ? 72  ILE B C   1 
ATOM   1319 O O   . ILE B 2 52  ? 7.08216  11.17109  24.55263 1.000 57.12331  ? 72  ILE B O   1 
ATOM   1320 C CB  . ILE B 2 52  ? 8.52596  8.57055   25.24620 1.000 59.20174  ? 72  ILE B CB  1 
ATOM   1321 C CG1 . ILE B 2 52  ? 8.52869  7.10613   25.68504 1.000 56.75379  ? 72  ILE B CG1 1 
ATOM   1322 C CG2 . ILE B 2 52  ? 9.92005  9.15843   25.32941 1.000 61.16785  ? 72  ILE B CG2 1 
ATOM   1323 C CD1 . ILE B 2 52  ? 9.84006  6.40060   25.40844 1.000 55.53173  ? 72  ILE B CD1 1 
ATOM   1324 N N   . GLN B 2 53  ? 8.09888  11.72850  26.48971 1.000 61.29280  ? 73  GLN B N   1 
ATOM   1325 C CA  . GLN B 2 53  ? 8.40084  13.08248  26.05252 1.000 58.60476  ? 73  GLN B CA  1 
ATOM   1326 C C   . GLN B 2 53  ? 9.63338  13.07367  25.15319 1.000 57.19928  ? 73  GLN B C   1 
ATOM   1327 O O   . GLN B 2 53  ? 10.53845 12.25104  25.31213 1.000 55.41948  ? 73  GLN B O   1 
ATOM   1328 C CB  . GLN B 2 53  ? 8.62608  13.99859  27.25523 1.000 55.83578  ? 73  GLN B CB  1 
ATOM   1329 N N   . ALA B 2 54  ? 9.66283  14.00417  24.19621 1.000 55.81752  ? 74  ALA B N   1 
ATOM   1330 C CA  . ALA B 2 54  ? 10.74775 14.02114  23.21832 1.000 51.66549  ? 74  ALA B CA  1 
ATOM   1331 C C   . ALA B 2 54  ? 12.09682 14.27445  23.88131 1.000 55.98850  ? 74  ALA B C   1 
ATOM   1332 O O   . ALA B 2 54  ? 13.12008 13.72961  23.45058 1.000 55.37539  ? 74  ALA B O   1 
ATOM   1333 C CB  . ALA B 2 54  ? 10.47260 15.07444  22.14561 1.000 49.80207  ? 74  ALA B CB  1 
ATOM   1334 N N   . ASP B 2 55  ? 12.11852 15.09497  24.93432 1.000 56.85983  ? 75  ASP B N   1 
ATOM   1335 C CA  . ASP B 2 55  ? 13.37653 15.48040  25.56545 1.000 58.20284  ? 75  ASP B CA  1 
ATOM   1336 C C   . ASP B 2 55  ? 14.07080 14.32070  26.27071 1.000 58.43649  ? 75  ASP B C   1 
ATOM   1337 O O   . ASP B 2 55  ? 15.27289 14.41220  26.54201 1.000 59.17964  ? 75  ASP B O   1 
ATOM   1338 C CB  . ASP B 2 55  ? 13.13513 16.61678  26.56069 1.000 61.45848  ? 75  ASP B CB  1 
ATOM   1339 C CG  . ASP B 2 55  ? 12.67356 16.11614  27.91589 1.000 63.96415  ? 75  ASP B CG  1 
ATOM   1340 O OD1 . ASP B 2 55  ? 11.55834 15.55951  27.99681 1.000 63.86806  ? 75  ASP B OD1 1 
ATOM   1341 O OD2 . ASP B 2 55  ? 13.42509 16.27990  28.90027 1.000 66.44342  ? 75  ASP B OD2 1 
ATOM   1342 N N   . GLN B 2 56  ? 13.35399 13.24247  26.57576 1.000 60.21438  ? 76  GLN B N   1 
ATOM   1343 C CA  . GLN B 2 56  ? 13.95030 12.13922  27.31538 1.000 58.79503  ? 76  GLN B CA  1 
ATOM   1344 C C   . GLN B 2 56  ? 14.91414 11.34412  26.43933 1.000 58.96833  ? 76  GLN B C   1 
ATOM   1345 O O   . GLN B 2 56  ? 14.80319 11.31856  25.21026 1.000 56.79556  ? 76  GLN B O   1 
ATOM   1346 C CB  . GLN B 2 56  ? 12.86437 11.21763  27.87072 1.000 59.10244  ? 76  GLN B CB  1 
ATOM   1347 C CG  . GLN B 2 56  ? 11.60564 11.94292  28.31522 1.000 60.32268  ? 76  GLN B CG  1 
ATOM   1348 C CD  . GLN B 2 56  ? 10.63597 11.03518  29.04586 1.000 57.41694  ? 76  GLN B CD  1 
ATOM   1349 O OE1 . GLN B 2 56  ? 9.66059  10.55581  28.46775 1.000 55.83842  ? 76  GLN B OE1 1 
ATOM   1350 N NE2 . GLN B 2 56  ? 10.89884 10.79608  30.32565 1.000 60.58724  ? 76  GLN B NE2 1 
ATOM   1351 N N   . THR B 2 57  ? 15.86792 10.69154  27.09324 1.000 59.68297  ? 77  THR B N   1 
ATOM   1352 C CA  . THR B 2 57  ? 16.89351 9.87365   26.46897 1.000 58.98976  ? 77  THR B CA  1 
ATOM   1353 C C   . THR B 2 57  ? 16.78013 8.43812   26.97103 1.000 59.54459  ? 77  THR B C   1 
ATOM   1354 O O   . THR B 2 57  ? 16.17488 8.18852   28.01993 1.000 59.25747  ? 77  THR B O   1 
ATOM   1355 C CB  . THR B 2 57  ? 18.29564 10.42461  26.77471 1.000 58.40141  ? 77  THR B CB  1 
ATOM   1356 O OG1 . THR B 2 57  ? 18.68076 10.05412  28.10402 1.000 60.40482  ? 77  THR B OG1 1 
ATOM   1357 C CG2 . THR B 2 57  ? 18.31509 11.94010  26.64815 1.000 58.91083  ? 77  THR B CG2 1 
ATOM   1358 N N   . PRO B 2 58  ? 17.33335 7.46480   26.23701 1.000 57.61617  ? 78  PRO B N   1 
ATOM   1359 C CA  . PRO B 2 58  ? 17.24305 6.06833   26.69985 1.000 59.74033  ? 78  PRO B CA  1 
ATOM   1360 C C   . PRO B 2 58  ? 17.81868 5.84473   28.08724 1.000 63.95959  ? 78  PRO B C   1 
ATOM   1361 O O   . PRO B 2 58  ? 17.30865 4.99319   28.82665 1.000 66.09352  ? 78  PRO B O   1 
ATOM   1362 C CB  . PRO B 2 58  ? 18.02883 5.29627   25.63113 1.000 59.24228  ? 78  PRO B CB  1 
ATOM   1363 C CG  . PRO B 2 58  ? 17.92024 6.13583   24.41120 1.000 56.18550  ? 78  PRO B CG  1 
ATOM   1364 C CD  . PRO B 2 58  ? 17.91946 7.55842   24.88784 1.000 56.62262  ? 78  PRO B CD  1 
ATOM   1365 N N   . GLU B 2 59  ? 18.86848 6.57765   28.46584 1.000 60.15728  ? 79  GLU B N   1 
ATOM   1366 C CA  . GLU B 2 59  ? 19.37826 6.47423   29.82875 1.000 63.01719  ? 79  GLU B CA  1 
ATOM   1367 C C   . GLU B 2 59  ? 18.36402 6.98458   30.84428 1.000 64.26997  ? 79  GLU B C   1 
ATOM   1368 O O   . GLU B 2 59  ? 18.28964 6.46131   31.96192 1.000 67.71429  ? 79  GLU B O   1 
ATOM   1369 C CB  . GLU B 2 59  ? 20.69363 7.24144   29.96065 1.000 64.06951  ? 79  GLU B CB  1 
ATOM   1370 C CG  . GLU B 2 59  ? 21.52980 6.83573   31.16226 1.000 69.05375  ? 79  GLU B CG  1 
ATOM   1371 C CD  . GLU B 2 59  ? 22.10595 8.02872   31.89971 1.000 75.62656  ? 79  GLU B CD  1 
ATOM   1372 O OE1 . GLU B 2 59  ? 21.96602 8.08695   33.13989 1.000 77.62781  ? 79  GLU B OE1 1 
ATOM   1373 O OE2 . GLU B 2 59  ? 22.69952 8.90783   31.23996 1.000 75.54637  ? 79  GLU B OE2 1 
ATOM   1374 N N   . ASP B 2 60  ? 17.57841 7.99899   30.47575 1.000 63.51930  ? 80  ASP B N   1 
ATOM   1375 C CA  . ASP B 2 60  ? 16.56888 8.55431   31.36868 1.000 63.78736  ? 80  ASP B CA  1 
ATOM   1376 C C   . ASP B 2 60  ? 15.40777 7.60213   31.61898 1.000 64.51790  ? 80  ASP B C   1 
ATOM   1377 O O   . ASP B 2 60  ? 14.63283 7.83278   32.55334 1.000 67.06652  ? 80  ASP B O   1 
ATOM   1378 C CB  . ASP B 2 60  ? 16.02961 9.86982   30.80043 1.000 61.73729  ? 80  ASP B CB  1 
ATOM   1379 C CG  . ASP B 2 60  ? 17.11443 10.90796  30.59428 1.000 61.61181  ? 80  ASP B CG  1 
ATOM   1380 O OD1 . ASP B 2 60  ? 18.13248 10.85897  31.31456 1.000 64.11784  ? 80  ASP B OD1 1 
ATOM   1381 O OD2 . ASP B 2 60  ? 16.94624 11.77776  29.71364 1.000 59.36307  ? 80  ASP B OD2 1 
ATOM   1382 N N   . LEU B 2 61  ? 15.26281 6.55065   30.81372 1.000 64.99355  ? 81  LEU B N   1 
ATOM   1383 C CA  . LEU B 2 61  ? 14.14500 5.62491   30.94235 1.000 65.38325  ? 81  LEU B CA  1 
ATOM   1384 C C   . LEU B 2 61  ? 14.58758 4.20949   31.28972 1.000 65.52374  ? 81  LEU B C   1 
ATOM   1385 O O   . LEU B 2 61  ? 13.77695 3.27977   31.19079 1.000 65.91855  ? 81  LEU B O   1 
ATOM   1386 C CB  . LEU B 2 61  ? 13.31841 5.61946   29.65360 1.000 61.80927  ? 81  LEU B CB  1 
ATOM   1387 C CG  . LEU B 2 61  ? 12.21573 6.67760   29.58538 1.000 60.77810  ? 81  LEU B CG  1 
ATOM   1388 C CD1 . LEU B 2 61  ? 12.03447 7.17121   28.16069 1.000 57.90562  ? 81  LEU B CD1 1 
ATOM   1389 C CD2 . LEU B 2 61  ? 10.90981 6.11754   30.12669 1.000 60.21605  ? 81  LEU B CD2 1 
ATOM   1390 N N   . ASP B 2 62  ? 15.84821 4.02237   31.69019 1.000 66.99282  ? 82  ASP B N   1 
ATOM   1391 C CA  . ASP B 2 62  ? 16.37126 2.71927   32.10738 1.000 68.63076  ? 82  ASP B CA  1 
ATOM   1392 C C   . ASP B 2 62  ? 16.18163 1.65779   31.02634 1.000 67.06726  ? 82  ASP B C   1 
ATOM   1393 O O   . ASP B 2 62  ? 15.96627 0.48081   31.32623 1.000 68.43249  ? 82  ASP B O   1 
ATOM   1394 C CB  . ASP B 2 62  ? 15.73210 2.26377   33.42362 1.000 71.29005  ? 82  ASP B CB  1 
ATOM   1395 C CG  . ASP B 2 62  ? 16.62221 1.32221   34.20986 1.000 74.07127  ? 82  ASP B CG  1 
ATOM   1396 O OD1 . ASP B 2 62  ? 17.69194 1.76421   34.67936 1.000 75.58947  ? 82  ASP B OD1 1 
ATOM   1397 O OD2 . ASP B 2 62  ? 16.25245 0.13835   34.35608 1.000 75.13315  ? 82  ASP B OD2 1 
ATOM   1398 N N   . MET B 2 63  ? 16.26234 2.06606   29.76311 1.000 66.82399  ? 83  MET B N   1 
ATOM   1399 C CA  . MET B 2 63  ? 16.00502 1.15684   28.65883 1.000 61.57357  ? 83  MET B CA  1 
ATOM   1400 C C   . MET B 2 63  ? 17.17069 0.19097   28.46281 1.000 60.91573  ? 83  MET B C   1 
ATOM   1401 O O   . MET B 2 63  ? 18.29041 0.41235   28.93223 1.000 62.14732  ? 83  MET B O   1 
ATOM   1402 C CB  . MET B 2 63  ? 15.74254 1.94192   27.37319 1.000 60.35217  ? 83  MET B CB  1 
ATOM   1403 C CG  . MET B 2 63  ? 14.66815 3.00866   27.52425 1.000 60.59355  ? 83  MET B CG  1 
ATOM   1404 S SD  . MET B 2 63  ? 13.53080 3.09372   26.12816 1.000 56.06406  ? 83  MET B SD  1 
ATOM   1405 C CE  . MET B 2 63  ? 14.30314 4.37709   25.14901 1.000 51.85917  ? 83  MET B CE  1 
ATOM   1406 N N   . GLU B 2 64  ? 16.88737 -0.89853  27.75539 1.000 59.92432  ? 84  GLU B N   1 
ATOM   1407 C CA  . GLU B 2 64  ? 17.87387 -1.92315  27.45810 1.000 57.97948  ? 84  GLU B CA  1 
ATOM   1408 C C   . GLU B 2 64  ? 17.87250 -2.19902  25.96193 1.000 55.07898  ? 84  GLU B C   1 
ATOM   1409 O O   . GLU B 2 64  ? 16.95759 -1.80134  25.23735 1.000 54.74909  ? 84  GLU B O   1 
ATOM   1410 C CB  . GLU B 2 64  ? 17.59845 -3.21854  28.23562 1.000 57.10452  ? 84  GLU B CB  1 
ATOM   1411 N N   . ASP B 2 65  ? 18.92529 -2.87128  25.50466 1.000 57.40875  ? 85  ASP B N   1 
ATOM   1412 C CA  . ASP B 2 65  ? 19.02902 -3.22725  24.09675 1.000 54.74056  ? 85  ASP B CA  1 
ATOM   1413 C C   . ASP B 2 65  ? 17.84645 -4.09272  23.67687 1.000 54.52019  ? 85  ASP B C   1 
ATOM   1414 O O   . ASP B 2 65  ? 17.37907 -4.94465  24.43843 1.000 56.14272  ? 85  ASP B O   1 
ATOM   1415 C CB  . ASP B 2 65  ? 20.34740 -3.95642  23.83347 1.000 57.75536  ? 85  ASP B CB  1 
ATOM   1416 C CG  . ASP B 2 65  ? 21.44322 -3.02185  23.36163 1.000 57.87247  ? 85  ASP B CG  1 
ATOM   1417 O OD1 . ASP B 2 65  ? 21.13530 -2.09137  22.58856 1.000 55.58747  ? 85  ASP B OD1 1 
ATOM   1418 O OD2 . ASP B 2 65  ? 22.60785 -3.21028  23.76911 1.000 60.64633  ? 85  ASP B OD2 1 
ATOM   1419 N N   . ASN B 2 66  ? 17.34846 -3.84170  22.46381 1.000 52.88113  ? 86  ASN B N   1 
ATOM   1420 C CA  . ASN B 2 66  ? 16.21654 -4.52427  21.83545 1.000 52.82439  ? 86  ASN B CA  1 
ATOM   1421 C C   . ASN B 2 66  ? 14.87195 -4.13453  22.43746 1.000 51.42397  ? 86  ASN B C   1 
ATOM   1422 O O   . ASN B 2 66  ? 13.86135 -4.78373  22.13936 1.000 52.08930  ? 86  ASN B O   1 
ATOM   1423 C CB  . ASN B 2 66  ? 16.36137 -6.05209  21.87624 1.000 56.14518  ? 86  ASN B CB  1 
ATOM   1424 C CG  . ASN B 2 66  ? 17.24271 -6.58583  20.76540 1.000 58.67287  ? 86  ASN B CG  1 
ATOM   1425 O OD1 . ASN B 2 66  ? 18.42101 -6.24281  20.67253 1.000 61.24122  ? 86  ASN B OD1 1 
ATOM   1426 N ND2 . ASN B 2 66  ? 16.67482 -7.43373  19.91608 1.000 61.91516  ? 86  ASN B ND2 1 
ATOM   1427 N N   . ASP B 2 67  ? 14.82403 -3.10301  23.27704 1.000 51.76204  ? 87  ASP B N   1 
ATOM   1428 C CA  . ASP B 2 67  ? 13.55169 -2.63336  23.80729 1.000 51.81880  ? 87  ASP B CA  1 
ATOM   1429 C C   . ASP B 2 67  ? 12.70465 -2.01750  22.69734 1.000 49.05833  ? 87  ASP B C   1 
ATOM   1430 O O   . ASP B 2 67  ? 13.22123 -1.46083  21.72456 1.000 47.82051  ? 87  ASP B O   1 
ATOM   1431 C CB  . ASP B 2 67  ? 13.77449 -1.61644  24.92728 1.000 53.22268  ? 87  ASP B CB  1 
ATOM   1432 C CG  . ASP B 2 67  ? 13.61511 -2.22544  26.30657 1.000 52.32229  ? 87  ASP B CG  1 
ATOM   1433 O OD1 . ASP B 2 67  ? 13.06483 -3.34157  26.40279 1.000 52.86417  ? 87  ASP B OD1 1 
ATOM   1434 O OD2 . ASP B 2 67  ? 14.04015 -1.58952  27.29382 1.000 56.51004  ? 87  ASP B OD2 1 
ATOM   1435 N N   . ILE B 2 68  ? 11.38642 -2.12151  22.85400 1.000 47.43383  ? 88  ILE B N   1 
ATOM   1436 C CA  . ILE B 2 68  ? 10.42997 -1.70962  21.83190 1.000 46.23879  ? 88  ILE B CA  1 
ATOM   1437 C C   . ILE B 2 68  ? 9.76533  -0.40814  22.25694 1.000 44.86757  ? 88  ILE B C   1 
ATOM   1438 O O   . ILE B 2 68  ? 9.40690  -0.23096  23.42864 1.000 45.81617  ? 88  ILE B O   1 
ATOM   1439 C CB  . ILE B 2 68  ? 9.38215  -2.81429  21.58634 1.000 48.34001  ? 88  ILE B CB  1 
ATOM   1440 C CG1 . ILE B 2 68  ? 9.97002  -3.92625  20.71764 1.000 49.69572  ? 88  ILE B CG1 1 
ATOM   1441 C CG2 . ILE B 2 68  ? 8.12813  -2.24885  20.93352 1.000 49.75172  ? 88  ILE B CG2 1 
ATOM   1442 C CD1 . ILE B 2 68  ? 9.13713  -5.18899  20.69687 1.000 52.72987  ? 88  ILE B CD1 1 
ATOM   1443 N N   . ILE B 2 69  ? 9.61327  0.51195   21.30686 1.000 44.65510  ? 89  ILE B N   1 
ATOM   1444 C CA  . ILE B 2 69  ? 8.82801  1.72696   21.49270 1.000 47.34472  ? 89  ILE B CA  1 
ATOM   1445 C C   . ILE B 2 69  ? 7.64955  1.64865   20.53186 1.000 47.78419  ? 89  ILE B C   1 
ATOM   1446 O O   . ILE B 2 69  ? 7.83214  1.69621   19.30863 1.000 44.38987  ? 89  ILE B O   1 
ATOM   1447 C CB  . ILE B 2 69  ? 9.65316  2.99818   21.25222 1.000 43.01543  ? 89  ILE B CB  1 
ATOM   1448 C CG1 . ILE B 2 69  ? 11.01122 2.89590   21.94933 1.000 43.34975  ? 89  ILE B CG1 1 
ATOM   1449 C CG2 . ILE B 2 69  ? 8.89075  4.22308   21.73661 1.000 47.32589  ? 89  ILE B CG2 1 
ATOM   1450 C CD1 . ILE B 2 69  ? 11.79969 4.18812   21.94923 1.000 41.88297  ? 89  ILE B CD1 1 
ATOM   1451 N N   . GLU B 2 70  ? 6.44403  1.52809   21.07932 1.000 50.07161  ? 90  GLU B N   1 
ATOM   1452 C CA  . GLU B 2 70  ? 5.24708  1.43805   20.25755 1.000 50.10302  ? 90  GLU B CA  1 
ATOM   1453 C C   . GLU B 2 70  ? 4.86329  2.80880   19.71532 1.000 51.54527  ? 90  GLU B C   1 
ATOM   1454 O O   . GLU B 2 70  ? 5.03598  3.83496   20.37945 1.000 52.57030  ? 90  GLU B O   1 
ATOM   1455 C CB  . GLU B 2 70  ? 4.08273  0.85576   21.05958 1.000 49.87896  ? 90  GLU B CB  1 
ATOM   1456 C CG  . GLU B 2 70  ? 4.24955  -0.60559  21.44160 1.000 54.02792  ? 90  GLU B CG  1 
ATOM   1457 C CD  . GLU B 2 70  ? 3.24665  -1.04954  22.48977 1.000 63.81530  ? 90  GLU B CD  1 
ATOM   1458 O OE1 . GLU B 2 70  ? 2.72107  -0.18089  23.21839 1.000 58.47324  ? 90  GLU B OE1 1 
ATOM   1459 O OE2 . GLU B 2 70  ? 2.98219  -2.26685  22.58429 1.000 71.04520  ? 90  GLU B OE2 1 
ATOM   1460 N N   . ALA B 2 71  ? 4.32677  2.81434   18.49709 1.000 51.20627  ? 91  ALA B N   1 
ATOM   1461 C CA  . ALA B 2 71  ? 3.89339  4.03621   17.83458 1.000 48.93727  ? 91  ALA B CA  1 
ATOM   1462 C C   . ALA B 2 71  ? 2.43289  3.89932   17.43391 1.000 51.66985  ? 91  ALA B C   1 
ATOM   1463 O O   . ALA B 2 71  ? 2.04123  2.89847   16.82549 1.000 50.63935  ? 91  ALA B O   1 
ATOM   1464 C CB  . ALA B 2 71  ? 4.75649  4.33955   16.60537 1.000 45.15206  ? 91  ALA B CB  1 
ATOM   1465 N N   . HIS B 2 72  ? 1.63502  4.90475   17.77858 1.000 51.02492  ? 92  HIS B N   1 
ATOM   1466 C CA  . HIS B 2 72  ? 0.21794  4.95864   17.44781 1.000 51.85608  ? 92  HIS B CA  1 
ATOM   1467 C C   . HIS B 2 72  ? -0.09903 6.33868   16.88642 1.000 51.13535  ? 92  HIS B C   1 
ATOM   1468 O O   . HIS B 2 72  ? 0.75109  7.22913   16.86224 1.000 48.91334  ? 92  HIS B O   1 
ATOM   1469 C CB  . HIS B 2 72  ? -0.65419 4.65784   18.67367 1.000 51.06756  ? 92  HIS B CB  1 
ATOM   1470 C CG  . HIS B 2 72  ? -0.22217 3.44895   19.44288 1.000 53.29307  ? 92  HIS B CG  1 
ATOM   1471 N ND1 . HIS B 2 72  ? -0.82000 2.21648   19.29033 1.000 54.82067  ? 92  HIS B ND1 1 
ATOM   1472 C CD2 . HIS B 2 72  ? 0.74804  3.28364   20.37285 1.000 53.62634  ? 92  HIS B CD2 1 
ATOM   1473 C CE1 . HIS B 2 72  ? -0.23651 1.34395   20.09239 1.000 54.52313  ? 92  HIS B CE1 1 
ATOM   1474 N NE2 . HIS B 2 72  ? 0.71843  1.96590   20.76026 1.000 56.66922  ? 92  HIS B NE2 1 
ATOM   1475 N N   . ARG B 2 73  ? -1.34080 6.52676   16.45490 1.000 51.65247  ? 93  ARG B N   1 
ATOM   1476 C CA  . ARG B 2 73  ? -1.79139 7.79908   15.90739 1.000 54.03759  ? 93  ARG B CA  1 
ATOM   1477 C C   . ARG B 2 73  ? -2.50845 8.59639   16.98888 1.000 57.30089  ? 93  ARG B C   1 
ATOM   1478 O O   . ARG B 2 73  ? -3.35929 8.05511   17.70143 1.000 58.66181  ? 93  ARG B O   1 
ATOM   1479 C CB  . ARG B 2 73  ? -2.71819 7.57917   14.71058 1.000 53.80965  ? 93  ARG B CB  1 
ATOM   1480 N N   . GLU B 2 74  ? -2.15193 9.87264   17.12256 1.000 55.71288  ? 94  GLU B N   1 
ATOM   1481 C CA  . GLU B 2 74  ? -2.89036 10.74786  18.02251 1.000 57.80258  ? 94  GLU B CA  1 
ATOM   1482 C C   . GLU B 2 74  ? -4.34064 10.84115  17.56783 1.000 60.93256  ? 94  GLU B C   1 
ATOM   1483 O O   . GLU B 2 74  ? -4.62691 10.89347  16.36748 1.000 60.83014  ? 94  GLU B O   1 
ATOM   1484 C CB  . GLU B 2 74  ? -2.25429 12.13846  18.06833 1.000 55.35193  ? 94  GLU B CB  1 
ATOM   1485 C CG  . GLU B 2 74  ? -2.55794 12.92198  19.33992 1.000 56.14435  ? 94  GLU B CG  1 
ATOM   1486 C CD  . GLU B 2 74  ? -1.84606 12.36687  20.56041 1.000 60.87198  ? 94  GLU B CD  1 
ATOM   1487 O OE1 . GLU B 2 74  ? -0.60162 12.26728  20.52926 1.000 58.09096  ? 94  GLU B OE1 1 
ATOM   1488 O OE2 . GLU B 2 74  ? -2.52970 12.03401  21.55250 1.000 63.52277  ? 94  GLU B OE2 1 
ATOM   1489 N N   . GLN B 2 75  ? -5.25695 10.85189  18.53966 1.000 61.39427  ? 95  GLN B N   1 
ATOM   1490 C CA  . GLN B 2 75  ? -6.69331 10.76993  18.27339 1.000 65.72608  ? 95  GLN B CA  1 
ATOM   1491 C C   . GLN B 2 75  ? -7.02470 9.48832   17.50689 1.000 66.00111  ? 95  GLN B C   1 
ATOM   1492 O O   . GLN B 2 75  ? -7.75934 9.49791   16.51621 1.000 67.69671  ? 95  GLN B O   1 
ATOM   1493 C CB  . GLN B 2 75  ? -7.19322 12.00760  17.51613 1.000 67.00654  ? 95  GLN B CB  1 
ATOM   1494 C CG  . GLN B 2 75  ? -6.92499 13.39420  18.14608 1.000 67.46354  ? 95  GLN B CG  1 
ATOM   1495 C CD  . GLN B 2 75  ? -7.31240 13.55178  19.61721 1.000 70.66899  ? 95  GLN B CD  1 
ATOM   1496 O OE1 . GLN B 2 75  ? -7.71715 12.60624  20.28958 1.000 72.44186  ? 95  GLN B OE1 1 
ATOM   1497 N NE2 . GLN B 2 75  ? -7.18827 14.77698  20.11759 1.000 71.90685  ? 95  GLN B NE2 1 
ATOM   1498 N N   . ILE B 2 76  ? -6.45623 8.37622   17.96584 1.000 64.65632  ? 96  ILE B N   1 
ATOM   1499 C CA  . ILE B 2 76  ? -6.72912 7.07768   17.36038 1.000 65.48020  ? 96  ILE B CA  1 
ATOM   1500 C C   . ILE B 2 76  ? -8.15305 6.65571   17.67665 1.000 71.03874  ? 96  ILE B C   1 
ATOM   1501 O O   . ILE B 2 76  ? -8.64076 6.88215   18.78247 1.000 73.88841  ? 96  ILE B O   1 
ATOM   1502 C CB  . ILE B 2 76  ? -5.73466 6.00410   17.83352 1.000 65.35795  ? 96  ILE B CB  1 
ATOM   1503 C CG1 . ILE B 2 76  ? -6.18323 4.62170   17.35731 1.000 65.28406  ? 96  ILE B CG1 1 
ATOM   1504 C CG2 . ILE B 2 76  ? -5.60381 6.02309   19.34995 1.000 64.17225  ? 96  ILE B CG2 1 
ATOM   1505 C CD1 . ILE B 2 76  ? -6.12942 4.44724   15.85311 1.000 64.26982  ? 96  ILE B CD1 1 
HETATM 1506 O O   . HOH C 3 .   ? 33.64477 -0.36607  16.16098 1.000 54.35909  ? 201 HOH A O   1 
HETATM 1507 O O   . HOH C 3 .   ? 41.72539 -10.44009 8.61695  1.000 44.28451  ? 202 HOH A O   1 
HETATM 1508 O O   . HOH C 3 .   ? 32.30946 -15.40030 -4.17683 1.000 41.75388  ? 203 HOH A O   1 
HETATM 1509 O O   . HOH C 3 .   ? 20.26416 4.14640   13.53859 1.000 35.17081  ? 204 HOH A O   1 
HETATM 1510 O O   . HOH C 3 .   ? 23.95405 4.59475   5.98815  1.000 41.88042  ? 205 HOH A O   1 
HETATM 1511 O O   . HOH C 3 .   ? 29.33246 -5.02292  2.21638  1.000 45.67664  ? 206 HOH A O   1 
HETATM 1512 O O   . HOH C 3 .   ? 28.08327 -8.54141  15.10858 1.000 50.27158  ? 207 HOH A O   1 
HETATM 1513 O O   . HOH C 3 .   ? 25.19390 -8.98156  -3.75947 1.000 42.18692  ? 208 HOH A O   1 
HETATM 1514 O O   . HOH C 3 .   ? 26.03015 -17.64482 -1.42278 1.000 47.06178  ? 209 HOH A O   1 
HETATM 1515 O O   . HOH C 3 .   ? 35.16986 -20.69248 12.42994 1.000 59.65092  ? 210 HOH A O   1 
HETATM 1516 O O   . HOH C 3 .   ? 15.03564 -1.11930  10.21712 1.000 38.37072  ? 211 HOH A O   1 
HETATM 1517 O O   . HOH C 3 .   ? 34.56638 14.81230  1.54145  1.000 67.37839  ? 212 HOH A O   1 
HETATM 1518 O O   . HOH C 3 .   ? 32.67662 -24.30639 1.10233  1.000 39.33189  ? 213 HOH A O   1 
HETATM 1519 O O   . HOH C 3 .   ? 22.65830 -26.16537 1.98236  1.000 61.12572  ? 214 HOH A O   1 
HETATM 1520 O O   . HOH C 3 .   ? 43.57937 -19.36693 1.70565  1.000 41.56893  ? 215 HOH A O   1 
HETATM 1521 O O   . HOH C 3 .   ? 25.641   15.866    9.711    1.000 29.75196  ? 216 HOH A O   1 
HETATM 1522 O O   . HOH C 3 .   ? 29.76351 -5.95869  -7.86228 1.000 43.85698  ? 217 HOH A O   1 
HETATM 1523 O O   . HOH C 3 .   ? 17.77872 -8.14859  5.89938  1.000 58.55850  ? 218 HOH A O   1 
HETATM 1524 O O   . HOH C 3 .   ? 27.22082 -22.38578 14.40520 1.000 50.81229  ? 219 HOH A O   1 
HETATM 1525 O O   . HOH C 3 .   ? 30.76718 -24.40703 14.21886 1.000 49.77663  ? 220 HOH A O   1 
HETATM 1526 O O   . HOH C 3 .   ? 27.905   19.240    13.306   1.000 47.98984  ? 221 HOH A O   1 
HETATM 1527 O O   . HOH C 3 .   ? 46.20815 -22.24542 5.55892  1.000 37.75388  ? 222 HOH A O   1 
HETATM 1528 O O   . HOH D 3 .   ? 9.05300  17.48731  14.35949 1.000 53.18246  ? 101 HOH B O   1 
HETATM 1529 O O   . HOH D 3 .   ? 16.78224 16.16836  27.48922 1.000 51.69161  ? 102 HOH B O   1 
HETATM 1530 O O   . HOH D 3 .   ? 15.17435 -2.43166  32.94009 1.000 62.73288  ? 103 HOH B O   1 
HETATM 1531 O O   . HOH D 3 .   ? 13.19664 0.27715   32.80287 1.000 57.82734  ? 104 HOH B O   1 
HETATM 1532 O O   . HOH D 3 .   ? 14.84622 -2.92201  30.26834 1.000 55.81283  ? 105 HOH B O   1 
HETATM 1533 O O   . HOH D 3 .   ? 2.919    8.677     2.626    1.000 41.96802  ? 106 HOH B O   1 
HETATM 1534 O O   . HOH D 3 .   ? -2.588   4.450     23.997   1.000 49.54319  ? 107 HOH B O   1 
HETATM 1535 O O   . HOH D 3 .   ? 0.51921  -5.98840  16.02866 1.000 40.85749  ? 108 HOH B O   1 
HETATM 1536 O O   . HOH D 3 .   ? 6.70387  -6.73596  11.00677 1.000 38.38906  ? 109 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   . SER A 1   ? 0.52777 0.67987 1.00951 0.07253  0.15362  -0.28799 14  SER A N   
2    C CA  . SER A 1   ? 0.57779 0.65144 1.06753 0.05133  0.18855  -0.29605 14  SER A CA  
3    C C   . SER A 1   ? 0.71884 0.69117 1.10268 0.04064  0.21495  -0.27277 14  SER A C   
4    O O   . SER A 1   ? 0.74092 0.70338 1.08964 0.02727  0.25576  -0.28271 14  SER A O   
5    C CB  . SER A 1   ? 0.55173 0.62922 1.07382 0.06615  0.14098  -0.28739 14  SER A CB  
6    O OG  . SER A 1   ? 0.55127 0.63471 1.01929 0.09504  0.09262  -0.25944 14  SER A OG  
7    N N   . ASP A 2   ? 0.70497 0.60586 1.01329 0.03724  0.17448  -0.22597 15  ASP A N   
8    C CA  . ASP A 2   ? 0.78804 0.59120 0.95874 0.01304  0.17812  -0.18089 15  ASP A CA  
9    C C   . ASP A 2   ? 0.79169 0.59086 0.90712 0.04180  0.12197  -0.15351 15  ASP A C   
10   O O   . ASP A 2   ? 0.84838 0.57408 0.85184 0.02452  0.11680  -0.11898 15  ASP A O   
11   C CB  . ASP A 2   ? 0.88530 0.58423 0.99518 -0.03044 0.19081  -0.14506 15  ASP A CB  
12   C CG  . ASP A 2   ? 0.86613 0.56101 1.04382 -0.01828 0.14973  -0.13901 15  ASP A CG  
13   O OD1 . ASP A 2   ? 0.77156 0.56188 1.06933 0.01162  0.13414  -0.18085 15  ASP A OD1 
14   O OD2 . ASP A 2   ? 0.98315 0.58164 1.09760 -0.03871 0.13335  -0.09445 15  ASP A OD2 
15   N N   . LEU A 3   ? 0.73123 0.61394 0.92091 0.08228  0.08211  -0.17134 16  LEU A N   
16   C CA  . LEU A 3   ? 0.69079 0.57557 0.83447 0.10473  0.03273  -0.15040 16  LEU A CA  
17   C C   . LEU A 3   ? 0.64994 0.51047 0.71501 0.10272  0.04977  -0.14024 16  LEU A C   
18   O O   . LEU A 3   ? 0.66029 0.47513 0.64316 0.09892  0.02525  -0.11504 16  LEU A O   
19   C CB  . LEU A 3   ? 0.58117 0.57200 0.81982 0.14266  -0.00342 -0.17575 16  LEU A CB  
20   C CG  . LEU A 3   ? 0.48186 0.50153 0.79350 0.14875  -0.03817 -0.18817 16  LEU A CG  
21   C CD1 . LEU A 3   ? 0.44734 0.56915 0.78695 0.14364  -0.05711 -0.19068 16  LEU A CD1 
22   C CD2 . LEU A 3   ? 0.49703 0.45168 0.74501 0.14456  -0.08253 -0.15756 16  LEU A CD2 
23   N N   . GLY A 4   ? 0.62826 0.52273 0.72592 0.10649  0.09078  -0.16501 17  GLY A N   
24   C CA  . GLY A 4   ? 0.68062 0.54805 0.71699 0.10336  0.11140  -0.16180 17  GLY A CA  
25   C C   . GLY A 4   ? 0.75700 0.53480 0.68372 0.06123  0.13601  -0.14256 17  GLY A C   
26   O O   . GLY A 4   ? 0.74900 0.49227 0.60065 0.05593  0.13046  -0.13051 17  GLY A O   
27   N N   . LYS A 5   ? 0.77590 0.51737 0.69048 0.02807  0.16524  -0.14036 18  LYS A N   
28   C CA  . LYS A 5   ? 0.83060 0.48877 0.62874 -0.01603 0.18828  -0.11619 18  LYS A CA  
29   C C   . LYS A 5   ? 0.86713 0.47337 0.58050 -0.01497 0.13529  -0.07450 18  LYS A C   
30   O O   . LYS A 5   ? 0.93192 0.49680 0.54488 -0.03259 0.13658  -0.06034 18  LYS A O   
31   C CB  . LYS A 5   ? 0.89679 0.52367 0.69983 -0.05446 0.23002  -0.11640 18  LYS A CB  
32   C CG  . LYS A 5   ? 0.96628 0.58149 0.73244 -0.09446 0.29895  -0.14026 18  LYS A CG  
33   N N   . LYS A 6   ? 0.82734 0.44295 0.58637 0.00651  0.08717  -0.06094 19  LYS A N   
34   C CA  . LYS A 6   ? 0.85485 0.43229 0.55039 0.01415  0.03061  -0.02900 19  LYS A CA  
35   C C   . LYS A 6   ? 0.82863 0.43903 0.50388 0.03571  0.00606  -0.03872 19  LYS A C   
36   O O   . LYS A 6   ? 0.86035 0.43277 0.44757 0.02833  -0.01854 -0.02035 19  LYS A O   
37   C CB  . LYS A 6   ? 0.81681 0.40912 0.58848 0.03550  -0.01481 -0.02440 19  LYS A CB  
38   C CG  . LYS A 6   ? 0.82459 0.41317 0.66786 0.02176  0.01479  -0.03260 19  LYS A CG  
39   C CD  . LYS A 6   ? 0.87312 0.40699 0.72362 0.02094  -0.02456 -0.00483 19  LYS A CD  
40   C CE  . LYS A 6   ? 0.95716 0.46706 0.86695 -0.00348 0.01495  -0.00982 19  LYS A CE  
41   N NZ  . LYS A 6   ? 0.89829 0.41800 0.90810 0.01577  -0.02445 -0.01733 19  LYS A NZ  
42   N N   . LEU A 7   ? 0.77585 0.45737 0.53157 0.06201  0.01143  -0.06700 20  LEU A N   
43   C CA  . LEU A 7   ? 0.75077 0.45575 0.48960 0.07817  -0.00555 -0.07377 20  LEU A CA  
44   C C   . LEU A 7   ? 0.80267 0.46565 0.45918 0.05408  0.03004  -0.07673 20  LEU A C   
45   O O   . LEU A 7   ? 0.84111 0.48645 0.43613 0.05039  0.01048  -0.07266 20  LEU A O   
46   C CB  . LEU A 7   ? 0.68002 0.46216 0.51509 0.10942  -0.00351 -0.09555 20  LEU A CB  
47   C CG  . LEU A 7   ? 0.61675 0.41870 0.44108 0.12446  -0.01815 -0.09795 20  LEU A CG  
48   C CD1 . LEU A 7   ? 0.67360 0.47975 0.47302 0.12831  -0.07009 -0.08870 20  LEU A CD1 
49   C CD2 . LEU A 7   ? 0.58792 0.45850 0.49754 0.15430  -0.01283 -0.11029 20  LEU A CD2 
50   N N   . LEU A 8   ? 0.77921 0.43334 0.44006 0.03576  0.08400  -0.09136 21  LEU A N   
51   C CA  . LEU A 8   ? 0.84966 0.47098 0.43827 0.00850  0.12246  -0.10293 21  LEU A CA  
52   C C   . LEU A 8   ? 0.94908 0.51185 0.41818 -0.02359 0.11027  -0.07718 21  LEU A C   
53   O O   . LEU A 8   ? 0.99294 0.54017 0.39148 -0.03657 0.11090  -0.08330 21  LEU A O   
54   C CB  . LEU A 8   ? 0.86760 0.49963 0.49348 -0.00728 0.18342  -0.13062 21  LEU A CB  
55   C CG  . LEU A 8   ? 0.78825 0.47906 0.52497 0.02659  0.19867  -0.16112 21  LEU A CG  
56   C CD1 . LEU A 8   ? 0.79228 0.50774 0.58961 0.01642  0.24421  -0.18762 21  LEU A CD1 
57   C CD2 . LEU A 8   ? 0.79814 0.48545 0.52698 0.03161  0.21613  -0.18235 21  LEU A CD2 
58   N N   . GLU A 9   ? 0.99262 0.52257 0.43896 -0.03619 0.09784  -0.04817 22  GLU A N   
59   C CA  . GLU A 9   ? 1.10251 0.57203 0.42983 -0.06299 0.07966  -0.01389 22  GLU A CA  
60   C C   . GLU A 9   ? 1.09070 0.56244 0.38343 -0.04140 0.01751  -0.00317 22  GLU A C   
61   O O   . GLU A 9   ? 1.16812 0.61525 0.36012 -0.05909 0.00825  0.00434  22  GLU A O   
62   C CB  . GLU A 9   ? 1.15340 0.57963 0.47910 -0.07561 0.07482  0.02012  22  GLU A CB  
63   C CG  . GLU A 9   ? 1.30152 0.65534 0.49491 -0.11649 0.08295  0.05931  22  GLU A CG  
64   C CD  . GLU A 9   ? 1.35918 0.65524 0.55135 -0.12048 0.05906  0.10432  22  GLU A CD  
65   O OE1 . GLU A 9   ? 1.37463 0.64575 0.54811 -0.09693 -0.00583 0.13400  22  GLU A OE1 
66   O OE2 . GLU A 9   ? 1.39272 0.66811 0.60941 -0.14740 0.10577  0.10673  22  GLU A OE2 
67   N N   . ALA A 10  ? 0.99621 0.50642 0.37343 -0.00487 -0.02476 -0.00782 23  ALA A N   
68   C CA  . ALA A 10  ? 0.99007 0.51359 0.34906 0.01461  -0.08199 -0.00677 23  ALA A CA  
69   C C   . ALA A 10  ? 0.98715 0.53616 0.32682 0.01230  -0.06742 -0.03632 23  ALA A C   
70   O O   . ALA A 10  ? 1.05096 0.59408 0.32641 0.00815  -0.09601 -0.03864 23  ALA A O   
71   C CB  . ALA A 10  ? 0.90061 0.46993 0.36225 0.04898  -0.12357 -0.01235 23  ALA A CB  
72   N N   . ALA A 11  ? 0.91151 0.48914 0.31163 0.01619  -0.02439 -0.06112 24  ALA A N   
73   C CA  . ALA A 11  ? 0.90106 0.49071 0.29032 0.01192  -0.00432 -0.08893 24  ALA A CA  
74   C C   . ALA A 11  ? 1.00194 0.55751 0.29104 -0.02339 0.02339  -0.09727 24  ALA A C   
75   O O   . ALA A 11  ? 1.00735 0.58644 0.28994 -0.03018 0.01680  -0.11157 24  ALA A O   
76   C CB  . ALA A 11  ? 0.83953 0.45702 0.31628 0.02640  0.03486  -0.10857 24  ALA A CB  
77   N N   . ARG A 12  ? 1.06646 0.59420 0.31584 -0.04817 0.05675  -0.08653 25  ARG A N   
78   C CA  . ARG A 12  ? 1.16871 0.67790 0.32361 -0.08564 0.07989  -0.08940 25  ARG A CA  
79   C C   . ARG A 12  ? 1.21125 0.72376 0.31603 -0.08500 0.02471  -0.06168 25  ARG A C   
80   O O   . ARG A 12  ? 1.23941 0.78464 0.32739 -0.09551 0.02269  -0.07596 25  ARG A O   
81   C CB  . ARG A 12  ? 1.23947 0.71573 0.35273 -0.11666 0.12621  -0.07906 25  ARG A CB  
82   C CG  . ARG A 12  ? 1.24839 0.74924 0.39522 -0.13909 0.19264  -0.12014 25  ARG A CG  
83   C CD  . ARG A 12  ? 1.33044 0.80647 0.43094 -0.17780 0.23640  -0.10934 25  ARG A CD  
84   N NE  . ARG A 12  ? 1.28791 0.75277 0.44978 -0.16345 0.23573  -0.08995 25  ARG A NE  
85   C CZ  . ARG A 12  ? 1.25760 0.74509 0.49858 -0.16810 0.28419  -0.11664 25  ARG A CZ  
86   N NH1 . ARG A 12  ? 1.27311 0.78659 0.53087 -0.18747 0.34083  -0.16497 25  ARG A NH1 
87   N NH2 . ARG A 12  ? 1.21122 0.70124 0.52430 -0.15238 0.27530  -0.10096 25  ARG A NH2 
88   N N   . ALA A 13  ? 1.21642 0.70122 0.30889 -0.06896 -0.02121 -0.02586 26  ALA A N   
89   C CA  . ALA A 13  ? 1.26947 0.75499 0.32613 -0.06529 -0.07146 0.00294  26  ALA A CA  
90   C C   . ALA A 13  ? 1.19466 0.73894 0.31917 -0.03713 -0.11667 -0.01336 26  ALA A C   
91   O O   . ALA A 13  ? 1.23558 0.79699 0.34106 -0.03254 -0.15233 -0.00093 26  ALA A O   
92   C CB  . ALA A 13  ? 1.31734 0.74417 0.34798 -0.06052 -0.09863 0.04874  26  ALA A CB  
93   N N   . GLY A 14  ? 0.67088 0.87117 0.43127 0.23666  -0.13484 -0.00937 27  GLY A N   
94   C CA  . GLY A 14  ? 0.68253 0.82946 0.43658 0.23179  -0.13780 -0.00092 27  GLY A CA  
95   C C   . GLY A 14  ? 0.69457 0.81237 0.43974 0.22087  -0.12560 0.02382  27  GLY A C   
96   O O   . GLY A 14  ? 0.66595 0.76718 0.41794 0.21918  -0.12182 0.03368  27  GLY A O   
97   N N   . GLN A 15  ? 0.69343 0.80145 0.43953 0.20628  -0.11361 0.02949  28  GLN A N   
98   C CA  . GLN A 15  ? 0.69994 0.77010 0.45198 0.18627  -0.09336 0.04321  28  GLN A CA  
99   C C   . GLN A 15  ? 0.70760 0.72506 0.43451 0.17275  -0.09799 0.03213  28  GLN A C   
100  O O   . GLN A 15  ? 0.70672 0.71687 0.41778 0.16492  -0.10511 0.02649  28  GLN A O   
101  C CB  . GLN A 15  ? 0.68596 0.77484 0.45171 0.17361  -0.07513 0.05565  28  GLN A CB  
102  C CG  . GLN A 15  ? 0.68582 0.80558 0.47062 0.17494  -0.06693 0.07655  28  GLN A CG  
103  C CD  . GLN A 15  ? 0.74456 0.91903 0.52048 0.17935  -0.07005 0.07483  28  GLN A CD  
104  O OE1 . GLN A 15  ? 0.78379 0.98839 0.55107 0.18824  -0.07829 0.07594  28  GLN A OE1 
105  N NE2 . GLN A 15  ? 0.72569 0.91543 0.50374 0.16987  -0.06175 0.06894  28  GLN A NE2 
106  N N   . ASP A 16  ? 0.72818 0.70817 0.44928 0.16641  -0.09504 0.02913  29  ASP A N   
107  C CA  . ASP A 16  ? 0.70484 0.62870 0.38931 0.14447  -0.09663 0.02030  29  ASP A CA  
108  C C   . ASP A 16  ? 0.69613 0.59587 0.37728 0.11492  -0.06895 0.02137  29  ASP A C   
109  O O   . ASP A 16  ? 0.73110 0.59835 0.37191 0.09428  -0.07487 0.01670  29  ASP A O   
110  C CB  . ASP A 16  ? 0.71344 0.60688 0.39337 0.14048  -0.09548 0.01400  29  ASP A CB  
111  C CG  . ASP A 16  ? 0.73375 0.65877 0.43017 0.16959  -0.11593 0.01246  29  ASP A CG  
112  O OD1 . ASP A 16  ? 0.77272 0.67655 0.44536 0.17539  -0.13921 0.00351  29  ASP A OD1 
113  O OD2 . ASP A 16  ? 0.74119 0.70886 0.47177 0.18416  -0.11031 0.02062  29  ASP A OD2 
114  N N   . ASP A 17  ? 0.67166 0.58467 0.39637 0.11149  -0.04148 0.02688  30  ASP A N   
115  C CA  . ASP A 17  ? 0.68264 0.57431 0.41509 0.08391  -0.01184 0.02268  30  ASP A CA  
116  C C   . ASP A 17  ? 0.69709 0.60349 0.41462 0.07955  -0.01732 0.02725  30  ASP A C   
117  O O   . ASP A 17  ? 0.71988 0.59561 0.40710 0.05199  -0.00836 0.01835  30  ASP A O   
118  C CB  . ASP A 17  ? 0.67099 0.57597 0.46949 0.08718  0.01182  0.02786  30  ASP A CB  
119  N N   . GLU A 18  ? 0.69434 0.64870 0.43078 0.10276  -0.03108 0.03900  31  GLU A N   
120  C CA  . GLU A 18  ? 0.67671 0.65244 0.40700 0.09869  -0.03600 0.04008  31  GLU A CA  
121  C C   . GLU A 18  ? 0.68308 0.64230 0.37121 0.09574  -0.06475 0.02885  31  GLU A C   
122  O O   . GLU A 18  ? 0.68833 0.63885 0.36121 0.07841  -0.06729 0.02486  31  GLU A O   
123  C CB  . GLU A 18  ? 0.70140 0.73477 0.45900 0.11941  -0.04091 0.05141  31  GLU A CB  
124  C CG  . GLU A 18  ? 0.72160 0.78269 0.49081 0.10944  -0.03250 0.05455  31  GLU A CG  
125  C CD  . GLU A 18  ? 0.76343 0.79281 0.54026 0.08237  -0.00784 0.05559  31  GLU A CD  
126  O OE1 . GLU A 18  ? 0.77924 0.81950 0.55450 0.06967  -0.00600 0.05144  31  GLU A OE1 
127  O OE2 . GLU A 18  ? 0.80308 0.80081 0.59556 0.07359  0.01092  0.05769  31  GLU A OE2 
128  N N   . VAL A 19  ? 0.65941 0.61139 0.33085 0.11200  -0.09064 0.02415  32  VAL A N   
129  C CA  . VAL A 19  ? 0.72316 0.64911 0.35849 0.10979  -0.12628 0.01641  32  VAL A CA  
130  C C   . VAL A 19  ? 0.77044 0.63218 0.35391 0.07141  -0.12104 0.01536  32  VAL A C   
131  O O   . VAL A 19  ? 0.80603 0.64938 0.36081 0.05593  -0.14171 0.01391  32  VAL A O   
132  C CB  . VAL A 19  ? 0.71869 0.64090 0.35010 0.13327  -0.15434 0.01147  32  VAL A CB  
133  C CG1 . VAL A 19  ? 0.72652 0.59255 0.31092 0.12159  -0.19144 0.00887  32  VAL A CG1 
134  C CG2 . VAL A 19  ? 0.68108 0.66804 0.35479 0.16642  -0.16781 0.00371  32  VAL A CG2 
135  N N   . ARG A 20  ? 0.77708 0.60525 0.34840 0.05242  -0.09297 0.01375  33  ARG A N   
136  C CA  . ARG A 20  ? 0.79611 0.56453 0.31263 0.00815  -0.07938 0.00740  33  ARG A CA  
137  C C   . ARG A 20  ? 0.82085 0.59345 0.34047 -0.01530 -0.05672 0.00352  33  ARG A C   
138  O O   . ARG A 20  ? 0.85757 0.59129 0.32120 -0.04834 -0.06598 -0.00017 33  ARG A O   
139  C CB  . ARG A 20  ? 0.79554 0.53835 0.31463 -0.00793 -0.04594 -0.00109 33  ARG A CB  
140  C CG  . ARG A 20  ? 0.81234 0.53094 0.30637 0.00036  -0.06950 0.00031  33  ARG A CG  
141  C CD  . ARG A 20  ? 0.82073 0.51788 0.32361 -0.01910 -0.03382 -0.01201 33  ARG A CD  
142  N NE  . ARG A 20  ? 0.76377 0.50654 0.34774 0.00130  -0.00444 -0.01506 33  ARG A NE  
143  C CZ  . ARG A 20  ? 0.77855 0.54636 0.40710 0.02790  -0.00768 -0.01331 33  ARG A CZ  
144  N NH1 . ARG A 20  ? 0.73936 0.49527 0.34321 0.03925  -0.03467 -0.01146 33  ARG A NH1 
145  N NH2 . ARG A 20  ? 0.77089 0.57357 0.47151 0.04257  0.01314  -0.01280 33  ARG A NH2 
146  N N   . ILE A 21  ? 0.77070 0.58668 0.35211 -0.00106 -0.02991 0.00552  34  ILE A N   
147  C CA  . ILE A 21  ? 0.78392 0.60438 0.37626 -0.02217 -0.00760 0.00114  34  ILE A CA  
148  C C   . ILE A 21  ? 0.82134 0.65594 0.39316 -0.02090 -0.04101 0.00444  34  ILE A C   
149  O O   . ILE A 21  ? 0.86276 0.67213 0.40006 -0.05275 -0.03971 -0.00272 34  ILE A O   
150  C CB  . ILE A 21  ? 0.73175 0.59199 0.39731 -0.00483 0.02017  0.00778  34  ILE A CB  
151  C CG1 . ILE A 21  ? 0.75126 0.58712 0.44682 -0.01969 0.05845  -0.00334 34  ILE A CG1 
152  C CG2 . ILE A 21  ? 0.74088 0.62125 0.42407 -0.01434 0.02839  0.00926  34  ILE A CG2 
153  C CD1 . ILE A 21  ? 0.71209 0.58036 0.48003 0.00804  0.06728  0.00982  34  ILE A CD1 
154  N N   . LEU A 22  ? 0.76465 0.64192 0.36123 0.01442  -0.07147 0.01173  35  LEU A N   
155  C CA  . LEU A 22  ? 0.75838 0.65890 0.35591 0.01969  -0.10398 0.00984  35  LEU A CA  
156  C C   . LEU A 22  ? 0.82306 0.67154 0.35833 0.00041  -0.14417 0.00761  35  LEU A C   
157  O O   . LEU A 22  ? 0.85853 0.70097 0.37749 -0.01713 -0.16344 0.00470  35  LEU A O   
158  C CB  . LEU A 22  ? 0.69947 0.66072 0.34521 0.06009  -0.12224 0.01037  35  LEU A CB  
159  C CG  . LEU A 22  ? 0.67057 0.68637 0.36764 0.07123  -0.08993 0.01601  35  LEU A CG  
160  C CD1 . LEU A 22  ? 0.63867 0.70523 0.36643 0.10467  -0.10077 0.01452  35  LEU A CD1 
161  C CD2 . LEU A 22  ? 0.68317 0.72539 0.40013 0.05671  -0.08233 0.01283  35  LEU A CD2 
162  N N   . MET A 23  ? 0.84296 0.65030 0.34078 0.00091  -0.16081 0.01063  36  MET A N   
163  C CA  . MET A 23  ? 0.90740 0.65186 0.33369 -0.02472 -0.20168 0.01410  36  MET A CA  
164  C C   . MET A 23  ? 0.96563 0.66016 0.32859 -0.07888 -0.17771 0.01037  36  MET A C   
165  O O   . MET A 23  ? 1.02755 0.68850 0.33946 -0.10531 -0.21136 0.01321  36  MET A O   
166  C CB  . MET A 23  ? 0.93044 0.63506 0.32588 -0.01864 -0.21993 0.01933  36  MET A CB  
167  C CG  . MET A 23  ? 0.88193 0.63250 0.34028 0.03125  -0.24430 0.01814  36  MET A CG  
168  S SD  . MET A 23  ? 0.97189 0.69206 0.42295 0.03633  -0.23919 0.02032  36  MET A SD  
169  C CE  . MET A 23  ? 0.97657 0.61924 0.33987 -0.02353 -0.20916 0.02288  36  MET A CE  
170  N N   . ALA A 24  ? 0.95211 0.64112 0.32036 -0.09750 -0.12100 0.00149  37  ALA A N   
171  C CA  . ALA A 24  ? 1.00822 0.65529 0.32435 -0.15128 -0.08936 -0.01076 37  ALA A CA  
172  C C   . ALA A 24  ? 1.00508 0.67735 0.33869 -0.16028 -0.08832 -0.01535 37  ALA A C   
173  O O   . ALA A 24  ? 1.07155 0.70435 0.34365 -0.20679 -0.08601 -0.02362 37  ALA A O   
174  C CB  . ALA A 24  ? 0.98694 0.63301 0.33211 -0.16314 -0.02705 -0.02621 37  ALA A CB  
175  N N   . ASN A 25  ? 0.93522 0.67212 0.34757 -0.12085 -0.08889 -0.01120 38  ASN A N   
176  C CA  . ASN A 25  ? 0.93035 0.69568 0.36604 -0.12845 -0.08882 -0.01569 38  ASN A CA  
177  C C   . ASN A 25  ? 0.95746 0.72903 0.37780 -0.12180 -0.14982 -0.01010 38  ASN A C   
178  O O   . ASN A 25  ? 0.96192 0.75533 0.39837 -0.13199 -0.15565 -0.01561 38  ASN A O   
179  C CB  . ASN A 25  ? 0.85392 0.68323 0.37755 -0.09643 -0.05979 -0.01335 38  ASN A CB  
180  C CG  . ASN A 25  ? 0.86510 0.68522 0.41589 -0.10925 -0.00348 -0.02025 38  ASN A CG  
181  O OD1 . ASN A 25  ? 0.89947 0.67858 0.42114 -0.12820 0.01710  -0.02858 38  ASN A OD1 
182  N ND2 . ASN A 25  ? 0.83613 0.69351 0.44789 -0.10043 0.02095  -0.01808 38  ASN A ND2 
183  N N   . GLY A 26  ? 0.84645 0.59313 0.46999 0.27125  -0.00239 -0.14786 39  GLY A N   
184  C CA  . GLY A 26  ? 0.84101 0.58777 0.43740 0.25613  -0.01443 -0.13188 39  GLY A CA  
185  C C   . GLY A 26  ? 0.78559 0.55631 0.43035 0.22782  -0.03718 -0.12075 39  GLY A C   
186  O O   . GLY A 26  ? 0.78046 0.54528 0.39815 0.21487  -0.06197 -0.11388 39  GLY A O   
187  N N   . ALA A 27  ? 0.77359 0.57314 0.48854 0.21860  -0.03005 -0.11966 40  ALA A N   
188  C CA  . ALA A 27  ? 0.73843 0.55754 0.49489 0.19344  -0.04657 -0.10916 40  ALA A CA  
189  C C   . ALA A 27  ? 0.74044 0.57898 0.50544 0.18821  -0.02680 -0.08665 40  ALA A C   
190  O O   . ALA A 27  ? 0.71400 0.56063 0.48095 0.20060  0.00906  -0.07811 40  ALA A O   
191  C CB  . ALA A 27  ? 0.69378 0.53661 0.51527 0.18713  -0.04346 -0.11535 40  ALA A CB  
192  N N   . ASP A 28  ? 0.76200 0.60605 0.53190 0.17103  -0.04764 -0.07586 41  ASP A N   
193  C CA  . ASP A 28  ? 0.74468 0.60391 0.52211 0.16935  -0.03079 -0.05276 41  ASP A CA  
194  C C   . ASP A 28  ? 0.72406 0.60302 0.56133 0.16219  0.00105  -0.04662 41  ASP A C   
195  O O   . ASP A 28  ? 0.70453 0.59497 0.58495 0.14504  -0.00861 -0.05092 41  ASP A O   
196  C CB  . ASP A 28  ? 0.73841 0.60445 0.51537 0.15439  -0.06094 -0.04424 41  ASP A CB  
197  C CG  . ASP A 28  ? 0.72760 0.60558 0.49723 0.16159  -0.04810 -0.01921 41  ASP A CG  
198  O OD1 . ASP A 28  ? 0.72891 0.60405 0.49625 0.17495  -0.01239 -0.00687 41  ASP A OD1 
199  O OD2 . ASP A 28  ? 0.76259 0.65293 0.53021 0.15468  -0.07235 -0.01094 41  ASP A OD2 
200  N N   . VAL A 29  ? 0.70073 0.58083 0.53770 0.17394  0.04011  -0.03725 42  VAL A N   
201  C CA  . VAL A 29  ? 0.66292 0.55992 0.55809 0.16322  0.07322  -0.03382 42  VAL A CA  
202  C C   . VAL A 29  ? 0.64410 0.54329 0.56172 0.14845  0.07474  -0.01820 42  VAL A C   
203  O O   . VAL A 29  ? 0.60287 0.51307 0.57148 0.13220  0.08997  -0.02160 42  VAL A O   
204  C CB  . VAL A 29  ? 0.66363 0.55644 0.55010 0.17716  0.11975  -0.02521 42  VAL A CB  
205  C CG1 . VAL A 29  ? 0.70104 0.57361 0.54663 0.18687  0.13891  0.00229  42  VAL A CG1 
206  C CG2 . VAL A 29  ? 0.64397 0.56063 0.60141 0.16233  0.15061  -0.03269 42  VAL A CG2 
207  N N   . ASN A 30  ? 0.67359 0.56379 0.55481 0.15448  0.05885  -0.00228 43  ASN A N   
208  C CA  . ASN A 30  ? 0.67334 0.56579 0.57375 0.14568  0.06046  0.01370  43  ASN A CA  
209  C C   . ASN A 30  ? 0.64467 0.54698 0.54988 0.13428  0.02026  0.00831  43  ASN A C   
210  O O   . ASN A 30  ? 0.65199 0.55922 0.55945 0.13407  0.01570  0.02414  43  ASN A O   
211  C CB  . ASN A 30  ? 0.69569 0.57543 0.55857 0.16514  0.07934  0.04092  43  ASN A CB  
212  C CG  . ASN A 30  ? 0.69096 0.55368 0.54998 0.17361  0.12764  0.05055  43  ASN A CG  
213  O OD1 . ASN A 30  ? 0.69876 0.56348 0.60432 0.15768  0.15366  0.04197  43  ASN A OD1 
214  N ND2 . ASN A 30  ? 0.71623 0.56216 0.51872 0.19776  0.14008  0.06811  43  ASN A ND2 
215  N N   . ALA A 31  ? 0.64800 0.55194 0.55480 0.12615  -0.00641 -0.01252 44  ALA A N   
216  C CA  . ALA A 31  ? 0.67013 0.57841 0.58356 0.11165  -0.03907 -0.01751 44  ALA A CA  
217  C C   . ALA A 31  ? 0.63525 0.54928 0.59133 0.09608  -0.02956 -0.01520 44  ALA A C   
218  O O   . ALA A 31  ? 0.59826 0.51220 0.58261 0.09076  -0.01002 -0.02271 44  ALA A O   
219  C CB  . ALA A 31  ? 0.69699 0.59451 0.59784 0.10778  -0.06442 -0.03926 44  ALA A CB  
220  N N   . GLN A 32  ? 0.64332 0.56394 0.60466 0.08816  -0.04316 -0.00610 45  GLN A N   
221  C CA  . GLN A 32  ? 0.64345 0.56479 0.63627 0.07582  -0.03210 -0.00287 45  GLN A CA  
222  C C   . GLN A 32  ? 0.63831 0.55855 0.63490 0.06003  -0.05777 -0.01208 45  GLN A C   
223  O O   . GLN A 32  ? 0.62772 0.55118 0.60732 0.05724  -0.08231 -0.01278 45  GLN A O   
224  C CB  . GLN A 32  ? 0.63134 0.55917 0.62907 0.08452  -0.01481 0.02040  45  GLN A CB  
225  C CG  . GLN A 32  ? 0.63219 0.55887 0.60635 0.10586  0.00077  0.03605  45  GLN A CG  
226  C CD  . GLN A 32  ? 0.64176 0.57113 0.61918 0.11966  0.01879  0.06136  45  GLN A CD  
227  O OE1 . GLN A 32  ? 0.71918 0.64900 0.67053 0.14097  0.02541  0.07884  45  GLN A OE1 
228  N NE2 . GLN A 32  ? 0.62094 0.54923 0.62590 0.11062  0.02763  0.06405  45  GLN A NE2 
229  N N   . ASP A 33  ? 0.60768 0.52021 0.62354 0.04846  -0.05124 -0.01975 46  ASP A N   
230  C CA  . ASP A 33  ? 0.63295 0.53767 0.64663 0.03466  -0.06989 -0.02597 46  ASP A CA  
231  C C   . ASP A 33  ? 0.60476 0.51803 0.62903 0.02976  -0.06256 -0.00995 46  ASP A C   
232  O O   . ASP A 33  ? 0.57532 0.50329 0.60697 0.04008  -0.04926 0.00616  46  ASP A O   
233  C CB  . ASP A 33  ? 0.59850 0.49085 0.62003 0.02772  -0.06927 -0.04233 46  ASP A CB  
234  C CG  . ASP A 33  ? 0.55712 0.44937 0.60066 0.02452  -0.04258 -0.04194 46  ASP A CG  
235  O OD1 . ASP A 33  ? 0.59654 0.49231 0.64718 0.02973  -0.02118 -0.02671 46  ASP A OD1 
236  O OD2 . ASP A 33  ? 0.53474 0.42150 0.58672 0.01728  -0.04390 -0.05756 46  ASP A OD2 
237  N N   . THR A 34  ? 0.62378 0.52748 0.64745 0.01652  -0.06962 -0.01293 47  THR A N   
238  C CA  . THR A 34  ? 0.64559 0.56082 0.68252 0.01220  -0.06054 0.00199  47  THR A CA  
239  C C   . THR A 34  ? 0.62480 0.53888 0.67731 0.02015  -0.02986 0.01068  47  THR A C   
240  O O   . THR A 34  ? 0.62655 0.55776 0.69413 0.02705  -0.01745 0.02769  47  THR A O   
241  C CB  . THR A 34  ? 0.67401 0.57258 0.70143 -0.00378 -0.06915 -0.00295 47  THR A CB  
242  O OG1 . THR A 34  ? 0.72957 0.60239 0.74604 -0.00626 -0.06257 -0.01565 47  THR A OG1 
243  C CG2 . THR A 34  ? 0.72134 0.61100 0.72975 -0.01213 -0.09671 -0.01061 47  THR A CG2 
244  N N   . GLN A 35  ? 0.62743 0.52194 0.67850 0.01943  -0.01713 -0.00132 48  GLN A N   
245  C CA  . GLN A 35  ? 0.58219 0.46523 0.64405 0.02430  0.01399  0.00385  48  GLN A CA  
246  C C   . GLN A 35  ? 0.57018 0.45818 0.63780 0.03907  0.03050  0.01457  48  GLN A C   
247  O O   . GLN A 35  ? 0.56423 0.43472 0.63810 0.04346  0.05967  0.01965  48  GLN A O   
248  C CB  . GLN A 35  ? 0.60832 0.46671 0.66670 0.01178  0.01949  -0.01697 48  GLN A CB  
249  C CG  . GLN A 35  ? 0.67437 0.52511 0.71562 0.00040  -0.00552 -0.03134 48  GLN A CG  
250  C CD  . GLN A 35  ? 0.70641 0.53239 0.73765 -0.00985 0.00170  -0.04703 48  GLN A CD  
251  O OE1 . GLN A 35  ? 0.66700 0.47780 0.70217 -0.01049 0.02775  -0.04533 48  GLN A OE1 
252  N NE2 . GLN A 35  ? 0.78425 0.60255 0.79788 -0.01626 -0.02204 -0.06284 48  GLN A NE2 
253  N N   . GLY A 36  ? 0.53806 0.44300 0.59792 0.04713  0.01458  0.01809  49  GLY A N   
254  C CA  . GLY A 36  ? 0.57226 0.47791 0.62779 0.06325  0.03102  0.02989  49  GLY A CA  
255  C C   . GLY A 36  ? 0.56310 0.45470 0.62160 0.05905  0.04534  0.01645  49  GLY A C   
256  O O   . GLY A 36  ? 0.54108 0.42534 0.59517 0.07076  0.06826  0.02756  49  GLY A O   
257  N N   . ARG A 37  ? 0.54736 0.43663 0.61412 0.04366  0.03333  -0.00612 50  ARG A N   
258  C CA  . ARG A 37  ? 0.53104 0.41788 0.61272 0.03781  0.04592  -0.02108 50  ARG A CA  
259  C C   . ARG A 37  ? 0.53772 0.43871 0.60928 0.04814  0.03414  -0.02446 50  ARG A C   
260  O O   . ARG A 37  ? 0.54974 0.45787 0.60658 0.05010  0.00478  -0.03099 50  ARG A O   
261  C CB  . ARG A 37  ? 0.51379 0.39877 0.61045 0.02006  0.03436  -0.04449 50  ARG A CB  
262  C CG  . ARG A 37  ? 0.51350 0.37908 0.62528 0.00661  0.05911  -0.05024 50  ARG A CG  
263  C CD  . ARG A 37  ? 0.53913 0.38766 0.63600 0.00462  0.05845  -0.04360 50  ARG A CD  
264  N NE  . ARG A 37  ? 0.51612 0.33986 0.61993 -0.00992 0.07776  -0.05609 50  ARG A NE  
265  C CZ  . ARG A 37  ? 0.56323 0.38100 0.66311 -0.02443 0.06224  -0.07759 50  ARG A CZ  
266  N NH1 . ARG A 37  ? 0.65140 0.48416 0.74032 -0.02431 0.02882  -0.08634 50  ARG A NH1 
267  N NH2 . ARG A 37  ? 0.56664 0.35806 0.66846 -0.03857 0.08060  -0.09088 50  ARG A NH2 
268  N N   . THR A 38  ? 0.55301 0.45253 0.62898 0.05487  0.06026  -0.01982 51  THR A N   
269  C CA  . THR A 38  ? 0.52311 0.43309 0.58892 0.06594  0.05719  -0.02454 51  THR A CA  
270  C C   . THR A 38  ? 0.49702 0.42276 0.59277 0.05609  0.04979  -0.04928 51  THR A C   
271  O O   . THR A 38  ? 0.46693 0.39570 0.59142 0.03955  0.05001  -0.06203 51  THR A O   
272  C CB  . THR A 38  ? 0.52209 0.42193 0.57891 0.07754  0.09359  -0.00800 51  THR A CB  
273  O OG1 . THR A 38  ? 0.52611 0.41333 0.61250 0.06369  0.12655  -0.00762 51  THR A OG1 
274  C CG2 . THR A 38  ? 0.57804 0.46877 0.59618 0.09602  0.09100  0.01683  51  THR A CG2 
275  N N   . PRO A 39  ? 0.60181 0.48876 0.52326 0.04129  0.01128  0.13955  52  PRO A N   
276  C CA  . PRO A 39  ? 0.58961 0.45055 0.48605 0.03404  -0.00505 0.14522  52  PRO A CA  
277  C C   . PRO A 39  ? 0.57556 0.41659 0.48423 0.05063  -0.00367 0.11416  52  PRO A C   
278  O O   . PRO A 39  ? 0.59217 0.43349 0.47899 0.04611  -0.01045 0.10604  52  PRO A O   
279  C CB  . PRO A 39  ? 0.58857 0.40693 0.49073 0.03018  -0.02412 0.17169  52  PRO A CB  
280  C CG  . PRO A 39  ? 0.61358 0.44898 0.52155 0.02361  -0.01705 0.17510  52  PRO A CG  
281  C CD  . PRO A 39  ? 0.61065 0.47134 0.54537 0.03905  0.00478  0.16863  52  PRO A CD  
282  N N   . LEU A 40  ? 0.58788 0.40789 0.52865 0.06706  0.00106  0.09831  53  LEU A N   
283  C CA  . LEU A 40  ? 0.58062 0.38094 0.53064 0.07913  -0.00085 0.06923  53  LEU A CA  
284  C C   . LEU A 40  ? 0.57355 0.41791 0.51859 0.08608  0.00891  0.03840  53  LEU A C   
285  O O   . LEU A 40  ? 0.58363 0.42318 0.51749 0.08851  0.00597  0.02049  53  LEU A O   
286  C CB  . LEU A 40  ? 0.61290 0.37704 0.59344 0.08882  -0.00574 0.06329  53  LEU A CB  
287  C CG  . LEU A 40  ? 0.66663 0.38769 0.64975 0.08877  -0.01729 0.04912  53  LEU A CG  
288  C CD1 . LEU A 40  ? 0.71215 0.42682 0.68854 0.06926  -0.02100 0.06329  53  LEU A CD1 
289  C CD2 . LEU A 40  ? 0.68552 0.38540 0.69590 0.08968  -0.02392 0.04400  53  LEU A CD2 
290  N N   . HIS A 41  ? 0.55523 0.45003 0.51071 0.08837  0.02115  0.02766  54  HIS A N   
291  C CA  . HIS A 41  ? 0.52181 0.47718 0.47657 0.09217  0.03259  -0.00949 54  HIS A CA  
292  C C   . HIS A 41  ? 0.52538 0.50401 0.43341 0.07032  0.03390  -0.00035 54  HIS A C   
293  O O   . HIS A 41  ? 0.53644 0.52372 0.43799 0.07560  0.03426  -0.02654 54  HIS A O   
294  C CB  . HIS A 41  ? 0.50460 0.52708 0.47702 0.09092  0.04704  -0.02354 54  HIS A CB  
295  C CG  . HIS A 41  ? 0.50019 0.51731 0.52812 0.11987  0.04209  -0.05663 54  HIS A CG  
296  N ND1 . HIS A 41  ? 0.49014 0.48168 0.54211 0.12542  0.03679  -0.03879 54  HIS A ND1 
297  C CD2 . HIS A 41  ? 0.51588 0.54716 0.58236 0.14539  0.03582  -0.10802 54  HIS A CD2 
298  C CE1 . HIS A 41  ? 0.49190 0.47762 0.59343 0.15234  0.02500  -0.07599 54  HIS A CE1 
299  N NE2 . HIS A 41  ? 0.51215 0.52075 0.62554 0.16601  0.02229  -0.11965 54  HIS A NE2 
300  N N   . LEU A 42  ? 0.54436 0.52795 0.41856 0.04440  0.02971  0.03814  55  LEU A N   
301  C CA  . LEU A 42  ? 0.56092 0.55938 0.38602 0.01826  0.02179  0.05231  55  LEU A CA  
302  C C   . LEU A 42  ? 0.59052 0.53218 0.40909 0.02674  0.00407  0.05347  55  LEU A C   
303  O O   . LEU A 42  ? 0.62659 0.58161 0.41885 0.01850  0.00073  0.04229  55  LEU A O   
304  C CB  . LEU A 42  ? 0.62044 0.62142 0.41220 -0.01272 0.00998  0.09720  55  LEU A CB  
305  C CG  . LEU A 42  ? 0.57852 0.63455 0.37719 -0.02443 0.02719  0.10009  55  LEU A CG  
306  C CD1 . LEU A 42  ? 0.63390 0.67737 0.39761 -0.05667 0.00899  0.15017  55  LEU A CD1 
307  C CD2 . LEU A 42  ? 0.59470 0.74297 0.38405 -0.03803 0.05023  0.06333  55  LEU A CD2 
308  N N   . ALA A 43  ? 0.58436 0.46884 0.42662 0.04050  -0.00708 0.06430  56  ALA A N   
309  C CA  . ALA A 43  ? 0.61938 0.46076 0.46053 0.04654  -0.02275 0.05916  56  ALA A CA  
310  C C   . ALA A 43  ? 0.60532 0.44935 0.45677 0.06203  -0.01348 0.02214  56  ALA A C   
311  O O   . ALA A 43  ? 0.60906 0.44598 0.44341 0.06023  -0.02165 0.01204  56  ALA A O   
312  C CB  . ALA A 43  ? 0.63814 0.43538 0.50550 0.05302  -0.03271 0.07098  56  ALA A CB  
313  N N   . ALA A 44  ? 0.58238 0.43264 0.46363 0.07798  -0.00125 0.00069  57  ALA A N   
314  C CA  . ALA A 44  ? 0.59236 0.44138 0.48625 0.09344  0.00113  -0.03587 57  ALA A CA  
315  C C   . ALA A 44  ? 0.57790 0.48404 0.45245 0.08974  0.01115  -0.05858 57  ALA A C   
316  O O   . ALA A 44  ? 0.57531 0.47938 0.44468 0.09598  0.00908  -0.08227 57  ALA A O   
317  C CB  . ALA A 44  ? 0.58776 0.42311 0.52119 0.11134  0.00098  -0.05370 57  ALA A CB  
318  N N   . GLN A 45  ? 0.56635 0.52903 0.42809 0.07565  0.02249  -0.05274 58  GLN A N   
319  C CA  . GLN A 45  ? 0.59587 0.62751 0.43463 0.06307  0.03412  -0.07605 58  GLN A CA  
320  C C   . GLN A 45  ? 0.61813 0.63729 0.40926 0.04231  0.02219  -0.05820 58  GLN A C   
321  O O   . GLN A 45  ? 0.63963 0.68795 0.41739 0.04085  0.02652  -0.08482 58  GLN A O   
322  C CB  . GLN A 45  ? 0.60607 0.70797 0.43551 0.04224  0.04861  -0.07111 58  GLN A CB  
323  C CG  . GLN A 45  ? 0.63273 0.82972 0.45962 0.03385  0.06754  -0.11586 58  GLN A CG  
324  C CD  . GLN A 45  ? 0.65837 0.93096 0.44528 -0.00917 0.07896  -0.09903 58  GLN A CD  
325  O OE1 . GLN A 45  ? 0.65063 0.90878 0.42855 -0.02361 0.07504  -0.06131 58  GLN A OE1 
326  N NE2 . GLN A 45  ? 0.69287 1.04978 0.45300 -0.03413 0.09240  -0.12715 58  GLN A NE2 
327  N N   . ARG A 46  ? 0.64228 0.61762 0.41072 0.02735  0.00319  -0.01616 59  ARG A N   
328  C CA  . ARG A 46  ? 0.67910 0.63765 0.40409 0.00652  -0.01799 0.00295  59  ARG A CA  
329  C C   . ARG A 46  ? 0.68634 0.58655 0.42494 0.02515  -0.03406 -0.00498 59  ARG A C   
330  O O   . ARG A 46  ? 0.70146 0.57838 0.41299 0.01299  -0.05818 0.00853  59  ARG A O   
331  C CB  . ARG A 46  ? 0.69277 0.63720 0.38749 -0.02149 -0.03965 0.04939  59  ARG A CB  
332  C CG  . ARG A 46  ? 0.69828 0.70905 0.35481 -0.05776 -0.02983 0.06153  59  ARG A CG  
333  C CD  . ARG A 46  ? 0.71042 0.72143 0.37373 -0.06732 -0.03028 0.09084  59  ARG A CD  
334  N NE  . ARG A 46  ? 0.77939 0.86520 0.40644 -0.10648 -0.01736 0.09814  59  ARG A NE  
335  C CZ  . ARG A 46  ? 0.72699 0.88277 0.37931 -0.10169 0.01552  0.06881  59  ARG A CZ  
336  N NH1 . ARG A 46  ? 0.66243 0.81203 0.37555 -0.05806 0.03334  0.03410  59  ARG A NH1 
337  N NH2 . ARG A 46  ? 0.75669 0.99198 0.37244 -0.14452 0.02716  0.07271  59  ARG A NH2 
338  N N   . GLY A 47  ? 0.65727 0.53418 0.43599 0.05103  -0.02481 -0.02734 60  GLY A N   
339  C CA  . GLY A 47  ? 0.67711 0.50985 0.46703 0.06248  -0.03710 -0.03856 60  GLY A CA  
340  C C   . GLY A 47  ? 0.68167 0.47545 0.47700 0.05816  -0.05940 -0.01680 60  GLY A C   
341  O O   . GLY A 47  ? 0.67136 0.44516 0.46130 0.05797  -0.07796 -0.02339 60  GLY A O   
342  N N   . HIS A 48  ? 0.68068 0.46698 0.49110 0.05607  -0.05971 0.00434  61  HIS A N   
343  C CA  . HIS A 48  ? 0.67736 0.43437 0.50144 0.05386  -0.08186 0.01888  61  HIS A CA  
344  C C   . HIS A 48  ? 0.67215 0.41262 0.53114 0.06295  -0.07224 0.00392  61  HIS A C   
345  O O   . HIS A 48  ? 0.65420 0.39323 0.52926 0.06335  -0.06146 0.01464  61  HIS A O   
346  C CB  . HIS A 48  ? 0.68188 0.44248 0.49698 0.04171  -0.09152 0.05271  61  HIS A CB  
347  C CG  . HIS A 48  ? 0.70442 0.47758 0.47603 0.02126  -0.10837 0.07294  61  HIS A CG  
348  N ND1 . HIS A 48  ? 0.75053 0.54405 0.49931 0.00152  -0.10785 0.10203  61  HIS A ND1 
349  C CD2 . HIS A 48  ? 0.72255 0.49110 0.46470 0.01195  -0.12842 0.06988  61  HIS A CD2 
350  C CE1 . HIS A 48  ? 0.80297 0.60451 0.50563 -0.02385 -0.12764 0.11802  61  HIS A CE1 
351  N NE2 . HIS A 48  ? 0.80957 0.59361 0.50750 -0.01709 -0.14155 0.09962  61  HIS A NE2 
352  N N   . LEU A 49  ? 0.55252 0.45309 0.74401 -0.08951 0.06743  -0.26618 62  LEU A N   
353  C CA  . LEU A 49  ? 0.49116 0.43944 0.77605 -0.07659 0.07274  -0.21531 62  LEU A CA  
354  C C   . LEU A 49  ? 0.52216 0.51620 0.76608 -0.05314 0.06189  -0.17149 62  LEU A C   
355  O O   . LEU A 49  ? 0.50735 0.52690 0.79935 -0.04380 0.06935  -0.12702 62  LEU A O   
356  C CB  . LEU A 49  ? 0.50668 0.46341 0.83735 -0.08405 0.06562  -0.21851 62  LEU A CB  
357  C CG  . LEU A 49  ? 0.51365 0.48721 0.97130 -0.09105 0.07716  -0.18715 62  LEU A CG  
358  C CD1 . LEU A 49  ? 0.47269 0.44556 0.96643 -0.10275 0.06571  -0.20186 62  LEU A CD1 
359  C CD2 . LEU A 49  ? 0.46476 0.49019 0.96438 -0.07908 0.08267  -0.11995 62  LEU A CD2 
360  N N   . GLU A 50  ? 0.56053 0.56079 0.71333 -0.04286 0.03963  -0.18550 63  GLU A N   
361  C CA  . GLU A 50  ? 0.53507 0.58046 0.64447 -0.01720 0.02747  -0.15239 63  GLU A CA  
362  C C   . GLU A 50  ? 0.53908 0.57313 0.61256 -0.00789 0.02498  -0.13712 63  GLU A C   
363  O O   . GLU A 50  ? 0.54750 0.61588 0.62423 0.01012  0.02372  -0.09499 63  GLU A O   
364  C CB  . GLU A 50  ? 0.54946 0.59843 0.57811 -0.00580 -0.00222 -0.18137 63  GLU A CB  
365  C CG  . GLU A 50  ? 0.62165 0.68241 0.69174 -0.01366 -0.00623 -0.20018 63  GLU A CG  
366  C CD  . GLU A 50  ? 0.67633 0.66854 0.71449 -0.03662 -0.02165 -0.25063 63  GLU A CD  
367  O OE1 . GLU A 50  ? 0.72458 0.67953 0.66865 -0.03305 -0.05054 -0.25925 63  GLU A OE1 
368  O OE2 . GLU A 50  ? 0.62854 0.59824 0.73071 -0.05735 -0.00467 -0.25940 63  GLU A OE2 
369  N N   . ILE A 51  ? 0.57061 0.55680 0.60659 -0.02205 0.02351  -0.17073 64  ILE A N   
370  C CA  . ILE A 51  ? 0.57891 0.55616 0.59687 -0.01652 0.02148  -0.15794 64  ILE A CA  
371  C C   . ILE A 51  ? 0.50285 0.49370 0.62608 -0.01579 0.04209  -0.12508 64  ILE A C   
372  O O   . ILE A 51  ? 0.46755 0.47223 0.59501 0.00006  0.03249  -0.08975 64  ILE A O   
373  C CB  . ILE A 51  ? 0.59625 0.52484 0.55758 -0.03921 0.02131  -0.20172 64  ILE A CB  
374  C CG1 . ILE A 51  ? 0.64807 0.55364 0.49489 -0.03506 -0.01513 -0.21072 64  ILE A CG1 
375  C CG2 . ILE A 51  ? 0.55169 0.47664 0.52869 -0.03907 0.02700  -0.19036 64  ILE A CG2 
376  C CD1 . ILE A 51  ? 0.70968 0.56655 0.51460 -0.04231 -0.02631 -0.19869 64  ILE A CD1 
377  N N   . VAL A 52  ? 0.46378 0.44533 0.67424 -0.03217 0.06407  -0.13683 65  VAL A N   
378  C CA  . VAL A 52  ? 0.45520 0.44435 0.77683 -0.03102 0.07481  -0.10541 65  VAL A CA  
379  C C   . VAL A 52  ? 0.48502 0.51164 0.81676 -0.01527 0.06256  -0.04346 65  VAL A C   
380  O O   . VAL A 52  ? 0.48503 0.51574 0.84462 -0.00532 0.05310  -0.00449 65  VAL A O   
381  C CB  . VAL A 52  ? 0.42934 0.39972 0.84116 -0.04956 0.09356  -0.13200 65  VAL A CB  
382  C CG1 . VAL A 52  ? 0.42977 0.41114 0.95591 -0.04720 0.09200  -0.08681 65  VAL A CG1 
383  C CG2 . VAL A 52  ? 0.44261 0.37960 0.86622 -0.06433 0.11264  -0.18811 65  VAL A CG2 
384  N N   . GLU A 53  ? 0.53205 0.58714 0.83933 -0.01444 0.06207  -0.03431 66  GLU A N   
385  C CA  . GLU A 53  ? 0.50266 0.60188 0.81088 -0.00443 0.05846  0.02249  66  GLU A CA  
386  C C   . GLU A 53  ? 0.52457 0.63629 0.74995 0.01860  0.04076  0.04466  66  GLU A C   
387  O O   . GLU A 53  ? 0.49488 0.61555 0.73496 0.02440  0.03413  0.09451  66  GLU A O   
388  C CB  . GLU A 53  ? 0.48020 0.61853 0.77155 -0.00633 0.06421  0.01783  66  GLU A CB  
389  C CG  . GLU A 53  ? 0.46364 0.60003 0.84509 -0.02874 0.07703  0.01273  66  GLU A CG  
390  C CD  . GLU A 53  ? 0.50054 0.66501 0.85513 -0.02865 0.07589  -0.01468 66  GLU A CD  
391  O OE1 . GLU A 53  ? 0.54236 0.73790 0.81751 -0.00899 0.06686  -0.02086 66  GLU A OE1 
392  O OE2 . GLU A 53  ? 0.48565 0.64090 0.90369 -0.04640 0.07997  -0.03138 66  GLU A OE2 
393  N N   . VAL A 54  ? 0.50192 0.60852 0.63572 0.03112  0.02713  0.00881  67  VAL A N   
394  C CA  . VAL A 54  ? 0.51484 0.63331 0.56398 0.05592  0.00458  0.02519  67  VAL A CA  
395  C C   . VAL A 54  ? 0.53266 0.61921 0.59808 0.05868  -0.00790 0.04170  67  VAL A C   
396  O O   . VAL A 54  ? 0.54915 0.64412 0.57728 0.07663  -0.02671 0.07680  67  VAL A O   
397  C CB  . VAL A 54  ? 0.51271 0.62661 0.46759 0.06785  -0.01540 -0.01963 67  VAL A CB  
398  C CG1 . VAL A 54  ? 0.54893 0.60970 0.48065 0.05525  -0.02542 -0.05736 67  VAL A CG1 
399  C CG2 . VAL A 54  ? 0.59541 0.73744 0.46786 0.09852  -0.03870 -0.00320 67  VAL A CG2 
400  N N   . LEU A 55  ? 0.54365 0.59484 0.66671 0.04135  0.00181  0.01449  68  LEU A N   
401  C CA  . LEU A 55  ? 0.51030 0.53886 0.67620 0.04332  -0.00807 0.02812  68  LEU A CA  
402  C C   . LEU A 55  ? 0.51899 0.55270 0.76600 0.04432  -0.01094 0.08048  68  LEU A C   
403  O O   . LEU A 55  ? 0.49531 0.52130 0.73789 0.05736  -0.03555 0.11551  68  LEU A O   
404  C CB  . LEU A 55  ? 0.52333 0.52345 0.74110 0.02308  0.01042  -0.01964 68  LEU A CB  
405  C CG  . LEU A 55  ? 0.55721 0.53921 0.68856 0.01626  0.00542  -0.06234 68  LEU A CG  
406  C CD1 . LEU A 55  ? 0.46266 0.42324 0.63268 -0.01202 0.03616  -0.11360 68  LEU A CD1 
407  C CD2 . LEU A 55  ? 0.54179 0.51565 0.64086 0.02850  -0.02131 -0.04796 68  LEU A CD2 
408  N N   . LEU A 56  ? 0.50165 0.54244 0.82137 0.02907  0.00789  0.08874  69  LEU A N   
409  C CA  . LEU A 56  ? 0.47761 0.51659 0.87039 0.02512  -0.00127 0.14447  69  LEU A CA  
410  C C   . LEU A 56  ? 0.51159 0.57667 0.82378 0.03741  -0.01677 0.19941  69  LEU A C   
411  O O   . LEU A 56  ? 0.54812 0.59849 0.87743 0.03986  -0.03967 0.24939  69  LEU A O   
412  C CB  . LEU A 56  ? 0.47713 0.51811 0.95655 0.00408  0.01787  0.14420  69  LEU A CB  
413  C CG  . LEU A 56  ? 0.45856 0.47067 1.02943 -0.00854 0.03301  0.09083  69  LEU A CG  
414  C CD1 . LEU A 56  ? 0.45728 0.47569 1.07037 -0.02618 0.05028  0.07875  69  LEU A CD1 
415  C CD2 . LEU A 56  ? 0.47300 0.45504 1.15614 -0.00827 0.01699  0.10410  69  LEU A CD2 
416  N N   . LYS A 57  ? 0.50781 0.61058 0.73057 0.04536  -0.00645 0.18835  70  LYS A N   
417  C CA  . LYS A 57  ? 0.54661 0.68348 0.68594 0.05829  -0.01413 0.23078  70  LYS A CA  
418  C C   . LYS A 57  ? 0.56430 0.68396 0.62296 0.08329  -0.04591 0.23498  70  LYS A C   
419  O O   . LYS A 57  ? 0.61233 0.74633 0.60660 0.09402  -0.05901 0.27675  70  LYS A O   
420  C CB  . LYS A 57  ? 0.53697 0.72589 0.62180 0.06234  0.00704  0.20716  70  LYS A CB  
421  C CG  . LYS A 57  ? 0.53814 0.75572 0.69589 0.03716  0.03480  0.22345  70  LYS A CG  
422  C CD  . LYS A 57  ? 0.56748 0.84675 0.67923 0.04331  0.05381  0.20436  70  LYS A CD  
423  C CE  . LYS A 57  ? 0.57276 0.86033 0.76745 0.02105  0.07348  0.18144  70  LYS A CE  
424  N NZ  . LYS A 57  ? 0.54873 0.84648 0.70619 0.03383  0.07085  0.11806  70  LYS A NZ  
425  N N   . ALA A 58  ? 0.61231 0.91166 0.33781 0.21339  0.01293  0.09255  71  ALA A N   
426  C CA  . ALA A 58  ? 0.60558 0.92232 0.33217 0.21015  0.00625  0.07028  71  ALA A CA  
427  C C   . ALA A 58  ? 0.60123 0.93624 0.32992 0.21943  0.00855  0.07407  71  ALA A C   
428  O O   . ALA A 58  ? 0.59539 0.96158 0.32751 0.21944  0.00264  0.04977  71  ALA A O   
429  C CB  . ALA A 58  ? 0.63514 0.91960 0.35142 0.19525  -0.00432 0.04254  71  ALA A CB  
430  N N   . GLY A 59  ? 0.60417 0.92589 0.33078 0.23051  0.01928  0.10186  72  GLY A N   
431  C CA  . GLY A 59  ? 0.58174 0.92215 0.30755 0.24810  0.02245  0.10796  72  GLY A CA  
432  C C   . GLY A 59  ? 0.61532 0.93046 0.33960 0.23683  0.01435  0.09922  72  GLY A C   
433  O O   . GLY A 59  ? 0.60160 0.94587 0.32703 0.25148  0.01203  0.09284  72  GLY A O   
434  N N   . ALA A 60  ? 0.62825 0.89652 0.34844 0.21571  0.00928  0.09660  73  ALA A N   
435  C CA  . ALA A 60  ? 0.62547 0.86452 0.33990 0.20560  0.00312  0.08904  73  ALA A CA  
436  C C   . ALA A 60  ? 0.63316 0.86666 0.34878 0.22234  0.01712  0.11836  73  ALA A C   
437  O O   . ALA A 60  ? 0.64275 0.86364 0.35942 0.23409  0.03778  0.15029  73  ALA A O   
438  C CB  . ALA A 60  ? 0.63281 0.82355 0.33737 0.18827  -0.00455 0.08228  73  ALA A CB  
439  N N   . ASP A 61  ? 0.65823 0.89879 0.37200 0.22554  0.01185  0.10803  74  ASP A N   
440  C CA  . ASP A 61  ? 0.65785 0.89060 0.37092 0.24567  0.02654  0.13506  74  ASP A CA  
441  C C   . ASP A 61  ? 0.69928 0.87085 0.41020 0.23079  0.03769  0.15549  74  ASP A C   
442  O O   . ASP A 61  ? 0.72866 0.87270 0.43276 0.21176  0.02510  0.13884  74  ASP A O   
443  C CB  . ASP A 61  ? 0.64432 0.91138 0.35672 0.25499  0.01526  0.11288  74  ASP A CB  
444  C CG  . ASP A 61  ? 0.69059 0.95556 0.40033 0.28443  0.03102  0.14081  74  ASP A CG  
445  O OD1 . ASP A 61  ? 0.70469 0.94509 0.41218 0.30283  0.05677  0.17799  74  ASP A OD1 
446  O OD2 . ASP A 61  ? 0.71890 1.00503 0.42765 0.29134  0.02218  0.12483  74  ASP A OD2 
447  N N   . VAL A 62  ? 0.69007 0.83853 0.40522 0.24109  0.06740  0.19081  75  VAL A N   
448  C CA  . VAL A 62  ? 0.67291 0.76652 0.42122 0.21451  0.08452  0.19183  75  VAL A CA  
449  C C   . VAL A 62  ? 0.69380 0.75780 0.44498 0.21566  0.09343  0.19983  75  VAL A C   
450  O O   . VAL A 62  ? 0.68655 0.71468 0.46339 0.18629  0.09062  0.18081  75  VAL A O   
451  C CB  . VAL A 62  ? 0.68061 0.75451 0.45545 0.21570  0.12667  0.21403  75  VAL A CB  
452  C CG1 . VAL A 62  ? 0.70254 0.76860 0.44963 0.25862  0.16733  0.26215  75  VAL A CG1 
453  C CG2 . VAL A 62  ? 0.64889 0.68161 0.47905 0.17955  0.14499  0.19448  75  VAL A CG2 
454  N N   . ASN A 63  ? 0.73017 0.81458 0.45335 0.25360  0.10263  0.22526  76  ASN A N   
455  C CA  . ASN A 63  ? 0.71670 0.77638 0.44144 0.26194  0.11395  0.23620  76  ASN A CA  
456  C C   . ASN A 63  ? 0.68185 0.77140 0.39632 0.25594  0.07763  0.20298  76  ASN A C   
457  O O   . ASN A 63  ? 0.72480 0.80729 0.43899 0.26777  0.08307  0.20862  76  ASN A O   
458  C CB  . ASN A 63  ? 0.77858 0.84506 0.49911 0.30534  0.14520  0.26593  76  ASN A CB  
459  C CG  . ASN A 63  ? 0.79874 0.81680 0.53064 0.31057  0.19674  0.29899  76  ASN A CG  
460  O OD1 . ASN A 63  ? 0.80446 0.75974 0.56088 0.28397  0.23218  0.31057  76  ASN A OD1 
461  N ND2 . ASN A 63  ? 0.82218 0.86776 0.54082 0.34319  0.20768  0.31034  76  ASN A ND2 
462  N N   . ALA A 64  ? 0.67832 0.79653 0.38646 0.23787  0.04757  0.16703  77  ALA A N   
463  C CA  . ALA A 64  ? 0.70680 0.84259 0.41104 0.22591  0.02600  0.12896  77  ALA A CA  
464  C C   . ALA A 64  ? 0.68594 0.75764 0.40489 0.19439  0.02848  0.11826  77  ALA A C   
465  O O   . ALA A 64  ? 0.66992 0.69395 0.40055 0.17172  0.03306  0.12088  77  ALA A O   
466  C CB  . ALA A 64  ? 0.67426 0.83331 0.36925 0.20987  0.00824  0.09337  77  ALA A CB  
467  N N   . HIS A 65  ? 0.66685 0.74571 0.38750 0.19478  0.02516  0.10094  78  HIS A N   
468  C CA  . HIS A 65  ? 0.69244 0.71223 0.42301 0.16793  0.02943  0.09045  78  HIS A CA  
469  C C   . HIS A 65  ? 0.68721 0.69954 0.40821 0.14581  0.02047  0.04610  78  HIS A C   
470  O O   . HIS A 65  ? 0.66318 0.73010 0.38446 0.15388  0.01570  0.01895  78  HIS A O   
471  C CB  . HIS A 65  ? 0.68971 0.70789 0.43357 0.18690  0.04459  0.11191  78  HIS A CB  
472  C CG  . HIS A 65  ? 0.66033 0.75368 0.39885 0.22437  0.03809  0.10565  78  HIS A CG  
473  N ND1 . HIS A 65  ? 0.64759 0.77025 0.39548 0.21620  0.02773  0.06322  78  HIS A ND1 
474  C CD2 . HIS A 65  ? 0.71133 0.86384 0.43563 0.27471  0.04145  0.13159  78  HIS A CD2 
475  C CE1 . HIS A 65  ? 0.65752 0.86776 0.40492 0.25907  0.01999  0.05661  78  HIS A CE1 
476  N NE2 . HIS A 65  ? 0.71171 0.94132 0.43827 0.29953  0.02637  0.10074  78  HIS A NE2 
477  N N   . ASP A 66  ? 0.66851 0.61317 0.38126 0.11909  0.02321  0.03494  79  ASP A N   
478  C CA  . ASP A 66  ? 0.68071 0.59325 0.37628 0.09913  0.02826  -0.00243 79  ASP A CA  
479  C C   . ASP A 66  ? 0.66156 0.58030 0.37694 0.09500  0.03720  -0.01852 79  ASP A C   
480  O O   . ASP A 66  ? 0.64164 0.60238 0.38006 0.11518  0.03544  -0.00093 79  ASP A O   
481  C CB  . ASP A 66  ? 0.71433 0.55116 0.37829 0.08431  0.02932  -0.00442 79  ASP A CB  
482  C CG  . ASP A 66  ? 0.70075 0.50631 0.37674 0.07909  0.02783  0.01270  79  ASP A CG  
483  O OD1 . ASP A 66  ? 0.66304 0.48301 0.36906 0.08070  0.03441  0.02451  79  ASP A OD1 
484  O OD2 . ASP A 66  ? 0.71306 0.48365 0.36893 0.07624  0.02137  0.01077  79  ASP A OD2 
485  N N   . GLN A 67  ? 0.70649 0.57892 0.40997 0.07226  0.05173  -0.05193 80  GLN A N   
486  C CA  . GLN A 67  ? 0.64938 0.52676 0.37671 0.06411  0.06302  -0.07473 80  GLN A CA  
487  C C   . GLN A 67  ? 0.66614 0.50580 0.40040 0.06355  0.06260  -0.04693 80  GLN A C   
488  O O   . GLN A 67  ? 0.63875 0.49958 0.39987 0.06698  0.06778  -0.05469 80  GLN A O   
489  C CB  . GLN A 67  ? 0.66116 0.48354 0.37307 0.03638  0.09014  -0.11881 80  GLN A CB  
490  C CG  . GLN A 67  ? 0.75550 0.47119 0.41904 0.02357  0.10216  -0.10656 80  GLN A CG  
491  C CD  . GLN A 67  ? 0.78405 0.44039 0.42925 0.00369  0.13659  -0.13857 80  GLN A CD  
492  O OE1 . GLN A 67  ? 0.75493 0.45951 0.44618 -0.00800 0.14947  -0.17177 80  GLN A OE1 
493  N NE2 . GLN A 67  ? 0.80972 0.40040 0.42337 0.00282  0.14006  -0.11425 80  GLN A NE2 
494  N N   . TYR A 68  ? 0.66703 0.45853 0.38294 0.05985  0.05777  -0.02074 81  TYR A N   
495  C CA  . TYR A 68  ? 0.64982 0.41069 0.38107 0.05572  0.06167  -0.00071 81  TYR A CA  
496  C C   . TYR A 68  ? 0.63206 0.43176 0.39284 0.07707  0.06240  0.03523  81  TYR A C   
497  O O   . TYR A 68  ? 0.65357 0.42502 0.43409 0.07208  0.07446  0.05154  81  TYR A O   
498  C CB  . TYR A 68  ? 0.68679 0.38733 0.38987 0.04157  0.05881  -0.00326 81  TYR A CB  
499  C CG  . TYR A 68  ? 0.77553 0.42335 0.42815 0.03304  0.06483  -0.02894 81  TYR A CG  
500  C CD1 . TYR A 68  ? 0.81303 0.41256 0.45304 0.01842  0.08353  -0.04895 81  TYR A CD1 
501  C CD2 . TYR A 68  ? 0.79862 0.43676 0.41248 0.04261  0.05852  -0.03144 81  TYR A CD2 
502  C CE1 . TYR A 68  ? 0.86095 0.39543 0.44672 0.01414  0.10196  -0.06882 81  TYR A CE1 
503  C CE2 . TYR A 68  ? 0.84822 0.42241 0.40548 0.04238  0.07509  -0.04914 81  TYR A CE2 
504  C CZ  . TYR A 68  ? 0.90943 0.42753 0.45056 0.02842  0.09985  -0.06675 81  TYR A CZ  
505  O OH  . TYR A 68  ? 0.93208 0.42280 0.45670 0.02633  0.11674  -0.06369 81  TYR A OH  
506  N N   . GLY A 69  ? 0.61919 0.47819 0.38166 0.10167  0.05604  0.04665  82  GLY A N   
507  C CA  . GLY A 69  ? 0.60164 0.48387 0.37913 0.12786  0.06597  0.08582  82  GLY A CA  
508  C C   . GLY A 69  ? 0.62071 0.47781 0.40287 0.11697  0.07047  0.10011  82  GLY A C   
509  O O   . GLY A 69  ? 0.64443 0.49691 0.44612 0.12952  0.09317  0.13016  82  GLY A O   
510  N N   . TRP A 70  ? 0.62876 0.46888 0.39383 0.09685  0.05431  0.07712  83  TRP A N   
511  C CA  . TRP A 70  ? 0.63111 0.46078 0.40692 0.08711  0.05394  0.07830  83  TRP A CA  
512  C C   . TRP A 70  ? 0.64328 0.51342 0.40995 0.10240  0.04561  0.08699  83  TRP A C   
513  O O   . TRP A 70  ? 0.65592 0.54117 0.39315 0.10616  0.02914  0.07233  83  TRP A O   
514  C CB  . TRP A 70  ? 0.65492 0.44933 0.40998 0.06833  0.03893  0.04803  83  TRP A CB  
515  C CG  . TRP A 70  ? 0.68397 0.44235 0.45697 0.05114  0.04937  0.03801  83  TRP A CG  
516  C CD1 . TRP A 70  ? 0.67192 0.41281 0.46106 0.04761  0.06646  0.04691  83  TRP A CD1 
517  C CD2 . TRP A 70  ? 0.69051 0.43408 0.46854 0.03794  0.04271  0.01246  83  TRP A CD2 
518  N NE1 . TRP A 70  ? 0.70865 0.41697 0.51357 0.02835  0.07385  0.03048  83  TRP A NE1 
519  C CE2 . TRP A 70  ? 0.71388 0.42785 0.51258 0.02249  0.05837  0.00660  83  TRP A CE2 
520  C CE3 . TRP A 70  ? 0.71767 0.47922 0.48532 0.04193  0.02338  -0.01016 83  TRP A CE3 
521  C CZ2 . TRP A 70  ? 0.75742 0.46188 0.56784 0.00824  0.05551  -0.02408 83  TRP A CZ2 
522  C CZ3 . TRP A 70  ? 0.74947 0.50944 0.52737 0.03320  0.01728  -0.04222 83  TRP A CZ3 
523  C CH2 . TRP A 70  ? 0.77660 0.50932 0.57617 0.01514  0.03336  -0.05039 83  TRP A CH2 
524  N N   . THR A 71  ? 0.65164 0.53369 0.44531 0.10962  0.06393  0.10895  84  THR A N   
525  C CA  . THR A 71  ? 0.63188 0.54777 0.42153 0.12154  0.06033  0.11713  84  THR A CA  
526  C C   . THR A 71  ? 0.61960 0.53237 0.41488 0.10400  0.04417  0.08992  84  THR A C   
527  O O   . THR A 71  ? 0.63127 0.52053 0.43596 0.08688  0.03874  0.06673  84  THR A O   
528  C CB  . THR A 71  ? 0.64139 0.56006 0.45492 0.13813  0.09685  0.15212  84  THR A CB  
529  O OG1 . THR A 71  ? 0.62922 0.50974 0.48729 0.11588  0.12621  0.14764  84  THR A OG1 
530  C CG2 . THR A 71  ? 0.65073 0.58331 0.44324 0.17290  0.10856  0.18171  84  THR A CG2 
531  N N   . PRO A 72  ? 0.61955 0.36908 0.60130 0.10354  0.14968  0.00418  85  PRO A N   
532  C CA  . PRO A 72  ? 0.57539 0.38159 0.61367 0.10877  0.15571  0.02368  85  PRO A CA  
533  C C   . PRO A 72  ? 0.58263 0.41076 0.67433 0.09193  0.11200  0.01425  85  PRO A C   
534  O O   . PRO A 72  ? 0.57960 0.47125 0.71588 0.10658  0.09327  0.01189  85  PRO A O   
535  C CB  . PRO A 72  ? 0.61044 0.41105 0.66531 0.09588  0.21089  0.05519  85  PRO A CB  
536  C CG  . PRO A 72  ? 0.62842 0.38393 0.62482 0.09706  0.23907  0.04650  85  PRO A CG  
537  C CD  . PRO A 72  ? 0.64809 0.36731 0.60582 0.09480  0.19482  0.01655  85  PRO A CD  
538  N N   . LEU A 73  ? 0.61303 0.38993 0.70152 0.06431  0.09742  0.00577  86  LEU A N   
539  C CA  . LEU A 73  ? 0.59359 0.38258 0.73763 0.04338  0.06109  -0.01262 86  LEU A CA  
540  C C   . LEU A 73  ? 0.59525 0.41369 0.72747 0.06439  0.00825  -0.04623 86  LEU A C   
541  O O   . LEU A 73  ? 0.58393 0.46023 0.77462 0.06350  -0.02421 -0.06555 86  LEU A O   
542  C CB  . LEU A 73  ? 0.63976 0.34592 0.76556 0.01521  0.06890  -0.01188 86  LEU A CB  
543  C CG  . LEU A 73  ? 0.67860 0.37935 0.87815 -0.01915 0.05827  -0.02621 86  LEU A CG  
544  C CD1 . LEU A 73  ? 0.62320 0.39275 0.92247 -0.03560 0.07886  -0.01620 86  LEU A CD1 
545  C CD2 . LEU A 73  ? 0.76994 0.36617 0.93114 -0.03845 0.08552  -0.01481 86  LEU A CD2 
546  N N   . HIS A 74  ? 0.63110 0.41388 0.69019 0.08515  -0.00112 -0.05766 87  HIS A N   
547  C CA  . HIS A 74  ? 0.61086 0.41286 0.64664 0.11028  -0.04345 -0.08661 87  HIS A CA  
548  C C   . HIS A 74  ? 0.60240 0.47760 0.65530 0.14385  -0.04694 -0.08296 87  HIS A C   
549  O O   . HIS A 74  ? 0.61569 0.53474 0.68983 0.15656  -0.09028 -0.10664 87  HIS A O   
550  C CB  . HIS A 74  ? 0.64091 0.39744 0.60296 0.12977  -0.03849 -0.09626 87  HIS A CB  
551  C CG  . HIS A 74  ? 0.67621 0.36841 0.60898 0.11383  -0.05661 -0.11098 87  HIS A CG  
552  N ND1 . HIS A 74  ? 0.68103 0.32588 0.58195 0.10680  -0.03169 -0.09975 87  HIS A ND1 
553  C CD2 . HIS A 74  ? 0.68342 0.34843 0.60700 0.10954  -0.09610 -0.13633 87  HIS A CD2 
554  C CE1 . HIS A 74  ? 0.72065 0.32175 0.59468 0.10087  -0.05290 -0.11141 87  HIS A CE1 
555  N NE2 . HIS A 74  ? 0.70680 0.31394 0.59465 0.10033  -0.08903 -0.13270 87  HIS A NE2 
556  N N   . LEU A 75  ? 0.60270 0.48989 0.64160 0.16286  -0.00006 -0.05482 88  LEU A N   
557  C CA  . LEU A 75  ? 0.60030 0.54368 0.63652 0.20692  0.00650  -0.04476 88  LEU A CA  
558  C C   . LEU A 75  ? 0.56546 0.58389 0.67860 0.20475  -0.01493 -0.04259 88  LEU A C   
559  O O   . LEU A 75  ? 0.54856 0.62645 0.66293 0.24559  -0.04389 -0.05246 88  LEU A O   
560  C CB  . LEU A 75  ? 0.58731 0.51270 0.59174 0.22468  0.07344  -0.01490 88  LEU A CB  
561  C CG  . LEU A 75  ? 0.59718 0.48105 0.53475 0.24268  0.09450  -0.02504 88  LEU A CG  
562  C CD1 . LEU A 75  ? 0.58653 0.46782 0.51715 0.21168  0.14313  -0.00087 88  LEU A CD1 
563  C CD2 . LEU A 75  ? 0.59744 0.50401 0.49968 0.27687  0.06838  -0.03307 88  LEU A CD2 
564  N N   . ALA A 76  ? 0.53058 0.54893 0.70815 0.16145  -0.00027 -0.03226 89  ALA A N   
565  C CA  . ALA A 76  ? 0.51695 0.61319 0.78802 0.15365  -0.01700 -0.03676 89  ALA A CA  
566  C C   . ALA A 76  ? 0.54215 0.67356 0.86151 0.13926  -0.08125 -0.08489 89  ALA A C   
567  O O   . ALA A 76  ? 0.55260 0.77519 0.93498 0.15662  -0.11596 -0.10616 89  ALA A O   
568  C CB  . ALA A 76  ? 0.50581 0.58083 0.83301 0.10965  0.02795  -0.01206 89  ALA A CB  
569  N N   . ALA A 77  ? 0.55790 0.62162 0.85053 0.11014  -0.09821 -0.10629 90  ALA A N   
570  C CA  . ALA A 77  ? 0.58911 0.67709 0.92424 0.09454  -0.15446 -0.15627 90  ALA A CA  
571  C C   . ALA A 77  ? 0.60671 0.73641 0.88950 0.14693  -0.20335 -0.18224 90  ALA A C   
572  O O   . ALA A 77  ? 0.63501 0.82315 0.96427 0.14818  -0.25670 -0.22820 90  ALA A O   
573  C CB  . ALA A 77  ? 0.61237 0.60419 0.92446 0.05373  -0.15095 -0.16731 90  ALA A CB  
574  N N   . HIS A 78  ? 0.59882 0.69751 0.78632 0.19092  -0.18269 -0.15713 91  HIS A N   
575  C CA  . HIS A 78  ? 0.65306 0.77006 0.77231 0.24630  -0.21685 -0.17576 91  HIS A CA  
576  C C   . HIS A 78  ? 0.70104 0.91038 0.83217 0.30158  -0.22928 -0.17041 91  HIS A C   
577  O O   . HIS A 78  ? 0.71901 0.96348 0.88927 0.30538  -0.19429 -0.13888 91  HIS A O   
578  C CB  . HIS A 78  ? 0.66724 0.70720 0.68635 0.27076  -0.17808 -0.15288 91  HIS A CB  
579  C CG  . HIS A 78  ? 0.74704 0.77848 0.68795 0.32124  -0.20551 -0.17346 91  HIS A CG  
580  N ND1 . HIS A 78  ? 0.79351 0.80887 0.65694 0.37872  -0.16850 -0.14983 91  HIS A ND1 
581  C CD2 . HIS A 78  ? 0.75324 0.78161 0.67746 0.32408  -0.25992 -0.21536 91  HIS A CD2 
582  C CE1 . HIS A 78  ? 0.78512 0.78631 0.58339 0.41749  -0.19855 -0.17387 91  HIS A CE1 
583  N NE2 . HIS A 78  ? 0.76762 0.77927 0.60064 0.38521  -0.25733 -0.21472 91  HIS A NE2 
584  N N   . ALA A 79  ? 0.72208 0.96907 0.81241 0.35015  -0.27996 -0.20183 92  ALA A N   
585  C CA  . ALA A 79  ? 0.76048 1.08845 0.82953 0.42410  -0.29730 -0.19781 92  ALA A CA  
586  C C   . ALA A 79  ? 0.74972 1.18818 0.93538 0.41472  -0.32011 -0.20996 92  ALA A C   
587  O O   . ALA A 79  ? 0.76701 1.26962 1.03202 0.38779  -0.37685 -0.26360 92  ALA A O   
588  C CB  . ALA A 79  ? 0.76821 1.04155 0.74366 0.46601  -0.22272 -0.14043 92  ALA A CB  
589  N N   . ASN A 80  ? 0.72729 1.18466 0.92634 0.43312  -0.26946 -0.16283 93  ASN A N   
590  C CA  . ASN A 80  ? 0.70841 1.27306 0.99745 0.44125  -0.28498 -0.16865 93  ASN A CA  
591  C C   . ASN A 80  ? 0.69538 1.31014 1.13812 0.36594  -0.30809 -0.20655 93  ASN A C   
592  O O   . ASN A 80  ? 0.69354 1.39932 1.21975 0.35795  -0.36769 -0.26303 93  ASN A O   
593  C CB  . ASN A 80  ? 0.75533 1.30679 1.01844 0.46909  -0.21368 -0.10467 93  ASN A CB  
594  N N   . GLY A 81  ? 0.68931 1.22712 1.15990 0.30123  -0.24990 -0.17550 94  GLY A N   
595  C CA  . GLY A 81  ? 0.61364 1.17380 1.21777 0.22720  -0.24805 -0.19979 94  GLY A CA  
596  C C   . GLY A 81  ? 0.56616 1.11452 1.22200 0.20084  -0.18009 -0.15198 94  GLY A C   
597  O O   . GLY A 81  ? 0.54505 0.99162 1.13798 0.17999  -0.12235 -0.10776 94  GLY A O   
598  N N   . HIS A 82  ? 0.56366 1.21952 1.33640 0.20309  -0.18751 -0.16448 95  HIS A N   
599  C CA  . HIS A 82  ? 0.53579 1.18895 1.37551 0.17522  -0.12302 -0.12417 95  HIS A CA  
600  C C   . HIS A 82  ? 0.52791 1.08466 1.40695 0.09178  -0.08030 -0.12138 95  HIS A C   
601  O O   . HIS A 82  ? 0.51467 0.96671 1.32340 0.07425  -0.02126 -0.07359 95  HIS A O   
602  C CB  . HIS A 82  ? 0.52209 1.13002 1.25835 0.22341  -0.06636 -0.05668 95  HIS A CB  
603  N N   . LEU A 83  ? 0.92838 0.90082 0.79369 -0.17261 -0.14785 -0.09760 96  LEU A N   
604  C CA  . LEU A 83  ? 0.89251 0.83636 0.79818 -0.18307 -0.10566 -0.09784 96  LEU A CA  
605  C C   . LEU A 83  ? 0.83570 0.82318 0.79422 -0.14714 -0.11438 -0.07184 96  LEU A C   
606  O O   . LEU A 83  ? 0.82653 0.77949 0.81060 -0.13916 -0.08087 -0.05615 96  LEU A O   
607  C CB  . LEU A 83  ? 0.89150 0.85302 0.80259 -0.24210 -0.09052 -0.13535 96  LEU A CB  
608  C CG  . LEU A 83  ? 0.88254 0.95070 0.83448 -0.26311 -0.11806 -0.14847 96  LEU A CG  
609  C CD1 . LEU A 83  ? 0.80457 0.88906 0.81404 -0.26281 -0.09432 -0.13690 96  LEU A CD1 
610  C CD2 . LEU A 83  ? 0.96424 1.05653 0.89033 -0.32811 -0.11977 -0.19137 96  LEU A CD2 
611  N N   . GLU A 84  ? 0.82268 0.88630 0.79661 -0.12283 -0.15768 -0.06606 97  GLU A N   
612  C CA  . GLU A 84  ? 0.71797 0.82095 0.73653 -0.08588 -0.16404 -0.04587 97  GLU A CA  
613  C C   . GLU A 84  ? 0.67707 0.71804 0.68324 -0.04934 -0.15183 -0.01729 97  GLU A C   
614  O O   . GLU A 84  ? 0.64652 0.69058 0.68393 -0.03447 -0.13337 -0.00220 97  GLU A O   
615  C CB  . GLU A 84  ? 0.66898 0.85677 0.70217 -0.05894 -0.21130 -0.04604 97  GLU A CB  
616  N N   . ILE A 85  ? 0.73516 0.72666 0.69443 -0.03815 -0.16213 -0.00888 98  ILE A N   
617  C CA  . ILE A 85  ? 0.71584 0.65920 0.66244 -0.00888 -0.15367 0.01767  98  ILE A CA  
618  C C   . ILE A 85  ? 0.72360 0.62025 0.68067 -0.01967 -0.10679 0.02700  98  ILE A C   
619  O O   . ILE A 85  ? 0.70054 0.59352 0.67680 0.00128  -0.09411 0.04937  98  ILE A O   
620  C CB  . ILE A 85  ? 0.75359 0.66070 0.64651 -0.00041 -0.17555 0.02533  98  ILE A CB  
621  C CG1 . ILE A 85  ? 0.66287 0.60895 0.54827 0.02314  -0.22249 0.02732  98  ILE A CG1 
622  C CG2 . ILE A 85  ? 0.72465 0.58296 0.60285 0.01708  -0.16036 0.05039  98  ILE A CG2 
623  C CD1 . ILE A 85  ? 0.67885 0.58651 0.50820 0.02994  -0.24549 0.03987  98  ILE A CD1 
624  N N   . VAL A 86  ? 0.74871 0.60892 0.69187 -0.05118 -0.07958 0.01047  99  VAL A N   
625  C CA  . VAL A 86  ? 0.73670 0.54713 0.69303 -0.05465 -0.03231 0.02233  99  VAL A CA  
626  C C   . VAL A 86  ? 0.71580 0.55447 0.72041 -0.05786 -0.01592 0.02981  99  VAL A C   
627  O O   . VAL A 86  ? 0.69199 0.51087 0.71564 -0.04228 0.01127  0.05656  99  VAL A O   
628  C CB  . VAL A 86  ? 0.78916 0.54166 0.71731 -0.08562 -0.00130 -0.00092 99  VAL A CB  
629  C CG1 . VAL A 86  ? 0.79557 0.51053 0.68004 -0.07419 0.00003  0.00419  99  VAL A CG1 
630  C CG2 . VAL A 86  ? 0.83288 0.61221 0.75055 -0.12558 -0.01636 -0.03842 99  VAL A CG2 
631  N N   . GLU A 87  ? 0.70947 0.60287 0.73517 -0.07847 -0.03206 0.00929  100 GLU A N   
632  C CA  . GLU A 87  ? 0.65499 0.58514 0.72622 -0.08363 -0.01678 0.01793  100 GLU A CA  
633  C C   . GLU A 87  ? 0.63955 0.60573 0.72988 -0.04349 -0.02886 0.04538  100 GLU A C   
634  O O   . GLU A 87  ? 0.62733 0.59144 0.74067 -0.03757 -0.00304 0.06851  100 GLU A O   
635  C CB  . GLU A 87  ? 0.65698 0.65727 0.75026 -0.11382 -0.03458 -0.00969 100 GLU A CB  
636  C CG  . GLU A 87  ? 0.74526 0.71423 0.83579 -0.16786 -0.00560 -0.03412 100 GLU A CG  
637  C CD  . GLU A 87  ? 0.76482 0.80651 0.85963 -0.20278 -0.03395 -0.06804 100 GLU A CD  
638  O OE1 . GLU A 87  ? 0.72120 0.83427 0.82030 -0.17740 -0.07704 -0.06910 100 GLU A OE1 
639  O OE2 . GLU A 87  ? 0.78946 0.81778 0.88347 -0.25589 -0.01276 -0.09281 100 GLU A OE2 
640  N N   . VAL A 88  ? 0.66585 0.66299 0.74349 -0.01673 -0.06742 0.04325  101 VAL A N   
641  C CA  . VAL A 88  ? 0.63081 0.65460 0.71911 0.01812  -0.07825 0.06240  101 VAL A CA  
642  C C   . VAL A 88  ? 0.64212 0.61697 0.71517 0.03141  -0.05731 0.09077  101 VAL A C   
643  O O   . VAL A 88  ? 0.65124 0.64678 0.74109 0.04569  -0.04690 0.11110  101 VAL A O   
644  C CB  . VAL A 88  ? 0.61895 0.66795 0.69116 0.04432  -0.12147 0.05270  101 VAL A CB  
645  C CG1 . VAL A 88  ? 0.62733 0.69751 0.70752 0.07638  -0.12892 0.06492  101 VAL A CG1 
646  C CG2 . VAL A 88  ? 0.62830 0.74158 0.72235 0.03550  -0.14262 0.02881  101 VAL A CG2 
647  N N   . LEU A 89  ? 0.65862 0.57776 0.69976 0.02651  -0.05091 0.09292  102 LEU A N   
648  C CA  . LEU A 89  ? 0.67650 0.56172 0.70885 0.03927  -0.02931 0.12120  102 LEU A CA  
649  C C   . LEU A 89  ? 0.67684 0.55413 0.73934 0.03446  0.01121  0.14144  102 LEU A C   
650  O O   . LEU A 89  ? 0.68903 0.58261 0.76417 0.05180  0.02190  0.17138  102 LEU A O   
651  C CB  . LEU A 89  ? 0.71426 0.54881 0.70981 0.03329  -0.02558 0.11674  102 LEU A CB  
652  C CG  . LEU A 89  ? 0.68599 0.51826 0.64390 0.04186  -0.06170 0.11227  102 LEU A CG  
653  C CD1 . LEU A 89  ? 0.70569 0.49655 0.62615 0.02691  -0.05642 0.10123  102 LEU A CD1 
654  C CD2 . LEU A 89  ? 0.64421 0.48401 0.59702 0.06151  -0.06780 0.13788  102 LEU A CD2 
655  N N   . LEU A 90  ? 0.68488 0.53660 0.75666 0.00882  0.03403  0.12647  103 LEU A N   
656  C CA  . LEU A 90  ? 0.70547 0.53398 0.80231 0.00290  0.07538  0.14800  103 LEU A CA  
657  C C   . LEU A 90  ? 0.64996 0.53848 0.77861 0.00770  0.07343  0.16544  103 LEU A C   
658  O O   . LEU A 90  ? 0.66022 0.54871 0.80424 0.02059  0.09721  0.20144  103 LEU A O   
659  C CB  . LEU A 90  ? 0.70913 0.49022 0.80355 -0.03331 0.09922  0.12180  103 LEU A CB  
660  C CG  . LEU A 90  ? 0.75406 0.46477 0.81474 -0.04042 0.11523  0.10467  103 LEU A CG  
661  C CD1 . LEU A 90  ? 0.79197 0.47262 0.84204 -0.08573 0.12579  0.06449  103 LEU A CD1 
662  C CD2 . LEU A 90  ? 0.75545 0.40938 0.81995 -0.01679 0.15695  0.13741  103 LEU A CD2 
663  N N   . LYS A 91  ? 0.61431 0.56074 0.75327 -0.00070 0.04589  0.14177  104 LYS A N   
664  C CA  . LYS A 91  ? 0.64600 0.65815 0.81336 0.00430  0.04487  0.15369  104 LYS A CA  
665  C C   . LYS A 91  ? 0.62962 0.66731 0.78986 0.03637  0.03476  0.17867  104 LYS A C   
666  O O   . LYS A 91  ? 0.62935 0.70769 0.80696 0.04142  0.04665  0.20095  104 LYS A O   
667  C CB  . LYS A 91  ? 0.62890 0.70524 0.81035 -0.00473 0.01671  0.12057  104 LYS A CB  
668  C CG  . LYS A 91  ? 0.60962 0.76452 0.81567 0.00901  0.00986  0.12577  104 LYS A CG  
669  C CD  . LYS A 91  ? 0.54924 0.76606 0.78918 -0.01771 0.01281  0.10621  104 LYS A CD  
670  C CE  . LYS A 91  ? 0.50624 0.79461 0.77224 -0.01114 0.02351  0.11997  104 LYS A CE  
671  N NZ  . LYS A 91  ? 0.52544 0.80756 0.81057 -0.04508 0.06231  0.14219  104 LYS A NZ  
672  N N   . HIS A 92  ? 0.71163 0.83444 0.48152 0.10990  0.08433  0.28175  105 HIS A N   
673  C CA  . HIS A 92  ? 0.74149 0.85311 0.48032 0.11567  0.05174  0.24806  105 HIS A CA  
674  C C   . HIS A 92  ? 0.74856 0.83314 0.47986 0.12347  0.04804  0.25076  105 HIS A C   
675  O O   . HIS A 92  ? 0.78108 0.88657 0.50335 0.13808  0.03159  0.23068  105 HIS A O   
676  C CB  . HIS A 92  ? 0.74932 0.86532 0.47876 0.09936  0.01302  0.19597  105 HIS A CB  
677  C CG  . HIS A 92  ? 0.76136 0.90889 0.49515 0.10105  0.01362  0.18851  105 HIS A CG  
678  N ND1 . HIS A 92  ? 0.73415 0.90817 0.47655 0.09385  0.01866  0.19170  105 HIS A ND1 
679  C CD2 . HIS A 92  ? 0.75399 0.93634 0.49130 0.11882  0.01456  0.18359  105 HIS A CD2 
680  C CE1 . HIS A 92  ? 0.76949 0.96144 0.51311 0.09512  0.01642  0.18127  105 HIS A CE1 
681  N NE2 . HIS A 92  ? 0.76897 0.96862 0.51169 0.11140  0.01526  0.17872  105 HIS A NE2 
682  N N   . GLY A 93  ? 0.71521 0.77970 0.46682 0.13043  0.07839  0.28786  106 GLY A N   
683  C CA  . GLY A 93  ? 0.69179 0.73505 0.43841 0.14364  0.07992  0.29579  106 GLY A CA  
684  C C   . GLY A 93  ? 0.71889 0.73961 0.46082 0.12634  0.05246  0.26982  106 GLY A C   
685  O O   . GLY A 93  ? 0.75354 0.76721 0.48342 0.13265  0.03825  0.25873  106 GLY A O   
686  N N   . ALA A 94  ? 0.69269 0.70933 0.44495 0.10816  0.04634  0.26163  107 ALA A N   
687  C CA  . ALA A 94  ? 0.72725 0.72339 0.47387 0.09613  0.02174  0.23891  107 ALA A CA  
688  C C   . ALA A 94  ? 0.74202 0.70273 0.51802 0.10535  0.05532  0.27772  107 ALA A C   
689  O O   . ALA A 94  ? 0.75561 0.69594 0.58706 0.10590  0.10997  0.32239  107 ALA A O   
690  C CB  . ALA A 94  ? 0.72106 0.73835 0.46923 0.08408  0.00738  0.22290  107 ALA A CB  
691  N N   . ASP A 95  ? 0.78927 0.73408 0.54888 0.10588  0.03206  0.25857  108 ASP A N   
692  C CA  . ASP A 95  ? 0.77231 0.68004 0.56124 0.11451  0.06072  0.28850  108 ASP A CA  
693  C C   . ASP A 95  ? 0.81361 0.68718 0.64874 0.09656  0.07919  0.29844  108 ASP A C   
694  O O   . ASP A 95  ? 0.83392 0.70878 0.64423 0.08824  0.04168  0.26806  108 ASP A O   
695  C CB  . ASP A 95  ? 0.80661 0.71562 0.56824 0.11841  0.02878  0.26340  108 ASP A CB  
696  C CG  . ASP A 95  ? 0.83443 0.71004 0.62224 0.13239  0.05782  0.29342  108 ASP A CG  
697  O OD1 . ASP A 95  ? 0.81774 0.66787 0.65296 0.14097  0.11096  0.33448  108 ASP A OD1 
698  O OD2 . ASP A 95  ? 0.82525 0.69808 0.59859 0.13220  0.03329  0.27467  108 ASP A OD2 
699  N N   . VAL A 96  ? 0.79157 0.63384 0.71753 0.08309  0.14163  0.32731  109 VAL A N   
700  C CA  . VAL A 96  ? 0.76186 0.60125 0.79216 0.03622  0.14578  0.26173  109 VAL A CA  
701  C C   . VAL A 96  ? 0.76004 0.56079 0.80593 0.03039  0.13769  0.24722  109 VAL A C   
702  O O   . VAL A 96  ? 0.72755 0.54479 0.80079 0.00385  0.10505  0.18122  109 VAL A O   
703  C CB  . VAL A 96  ? 0.75920 0.58307 0.91426 0.01263  0.21688  0.26642  109 VAL A CB  
704  C CG1 . VAL A 96  ? 0.81916 0.58291 0.98322 0.04444  0.28696  0.35335  109 VAL A CG1 
705  C CG2 . VAL A 96  ? 0.74689 0.57274 1.02970 -0.03488 0.22695  0.18971  109 VAL A CG2 
706  N N   . ASN A 97  ? 0.76932 0.52349 0.79296 0.06061  0.16647  0.30877  110 ASN A N   
707  C CA  . ASN A 97  ? 0.79958 0.51291 0.84121 0.05822  0.16486  0.30213  110 ASN A CA  
708  C C   . ASN A 97  ? 0.79103 0.52585 0.72376 0.08144  0.10127  0.29132  110 ASN A C   
709  O O   . ASN A 97  ? 0.77142 0.48990 0.70046 0.08789  0.09537  0.28778  110 ASN A O   
710  C CB  . ASN A 97  ? 0.81121 0.49949 0.89947 0.07426  0.21870  0.33575  110 ASN A CB  
711  C CG  . ASN A 97  ? 0.85739 0.52479 1.06625 0.05199  0.29019  0.33976  110 ASN A CG  
712  O OD1 . ASN A 97  ? 0.90843 0.58551 1.11577 0.07880  0.32725  0.37736  110 ASN A OD1 
713  N ND2 . ASN A 97  ? 0.84060 0.48790 1.16603 0.00079  0.30893  0.28651  110 ASN A ND2 
714  N N   . ALA A 98  ? 0.77215 0.55315 0.62971 0.08749  0.05377  0.27052  111 ALA A N   
715  C CA  . ALA A 98  ? 0.77451 0.58526 0.57131 0.08953  -0.00084 0.23295  111 ALA A CA  
716  C C   . ALA A 98  ? 0.75180 0.52934 0.55220 0.08156  -0.01725 0.21124  111 ALA A C   
717  O O   . ALA A 98  ? 0.69769 0.47583 0.52668 0.05866  -0.02410 0.17113  111 ALA A O   
718  C CB  . ALA A 98  ? 0.77209 0.63657 0.53555 0.07989  -0.03406 0.20119  111 ALA A CB  
719  N N   . GLN A 99  ? 0.71643 0.49807 0.51938 0.08215  -0.03080 0.20264  112 GLN A N   
720  C CA  . GLN A 99  ? 0.71661 0.46531 0.52503 0.07737  -0.04102 0.17930  112 GLN A CA  
721  C C   . GLN A 99  ? 0.71735 0.52819 0.50593 0.07473  -0.06581 0.13890  112 GLN A C   
722  O O   . GLN A 99  ? 0.70906 0.57457 0.50661 0.07396  -0.06766 0.13983  112 GLN A O   
723  C CB  . GLN A 99  ? 0.73180 0.44155 0.57909 0.07944  -0.02126 0.19872  112 GLN A CB  
724  C CG  . GLN A 99  ? 0.71966 0.37300 0.64141 0.06890  0.03248  0.21879  112 GLN A CG  
725  C CD  . GLN A 99  ? 0.76593 0.39365 0.72610 0.06939  0.05230  0.22451  112 GLN A CD  
726  O OE1 . GLN A 99  ? 0.78049 0.43083 0.69830 0.09042  0.03441  0.23491  112 GLN A OE1 
727  N NE2 . GLN A 99  ? 0.77985 0.37034 0.83481 0.04224  0.08986  0.20833  112 GLN A NE2 
728  N N   . ASP A 100 ? 0.69244 0.47584 0.45764 0.06667  -0.08412 0.09920  113 ASP A N   
729  C CA  . ASP A 100 ? 0.65877 0.47549 0.42361 0.06275  -0.08782 0.06395  113 ASP A CA  
730  C C   . ASP A 100 ? 0.64882 0.44356 0.42094 0.06678  -0.08620 0.06511  113 ASP A C   
731  O O   . ASP A 100 ? 0.63911 0.41756 0.43061 0.07416  -0.07674 0.09759  113 ASP A O   
732  C CB  . ASP A 100 ? 0.63726 0.44138 0.38580 0.05647  -0.09986 0.02852  113 ASP A CB  
733  C CG  . ASP A 100 ? 0.70082 0.43774 0.42346 0.05405  -0.12590 0.01296  113 ASP A CG  
734  O OD1 . ASP A 100 ? 0.71542 0.40990 0.46659 0.04835  -0.12127 0.03241  113 ASP A OD1 
735  O OD2 . ASP A 100 ? 0.67644 0.42645 0.40178 0.05432  -0.12903 -0.01711 113 ASP A OD2 
736  N N   . TRP A 101 ? 0.64896 0.44054 0.41527 0.06384  -0.08919 0.03366  114 TRP A N   
737  C CA  . TRP A 101 ? 0.64984 0.42494 0.41861 0.06822  -0.09012 0.03113  114 TRP A CA  
738  C C   . TRP A 101 ? 0.62245 0.34920 0.39813 0.06424  -0.09480 0.04061  114 TRP A C   
739  O O   . TRP A 101 ? 0.56035 0.28555 0.36287 0.07163  -0.08459 0.06164  114 TRP A O   
740  C CB  . TRP A 101 ? 0.66163 0.41556 0.41479 0.06868  -0.09259 -0.00521 114 TRP A CB  
741  C CG  . TRP A 101 ? 0.65208 0.41557 0.40205 0.07931  -0.08638 -0.01508 114 TRP A CG  
742  C CD1 . TRP A 101 ? 0.62953 0.38725 0.38852 0.08077  -0.07883 -0.02477 114 TRP A CD1 
743  C CD2 . TRP A 101 ? 0.60241 0.40402 0.35437 0.09001  -0.08399 -0.00432 114 TRP A CD2 
744  N NE1 . TRP A 101 ? 0.60581 0.37373 0.36261 0.09401  -0.07508 -0.02689 114 TRP A NE1 
745  C CE2 . TRP A 101 ? 0.60889 0.40891 0.36268 0.09770  -0.07872 -0.01817 114 TRP A CE2 
746  C CE3 . TRP A 101 ? 0.59170 0.42954 0.34522 0.09778  -0.08493 0.02032  114 TRP A CE3 
747  C CZ2 . TRP A 101 ? 0.62422 0.45991 0.38048 0.10853  -0.07709 -0.01633 114 TRP A CZ2 
748  C CZ3 . TRP A 101 ? 0.58356 0.45550 0.33384 0.11066  -0.08358 0.02122  114 TRP A CZ3 
749  C CH2 . TRP A 101 ? 0.62428 0.49633 0.37668 0.11432  -0.08057 -0.00029 114 TRP A CH2 
750  N N   . ILE A 102 ? 0.68875 0.37706 0.45449 0.05351  -0.10761 0.02502  115 ILE A N   
751  C CA  . ILE A 102 ? 0.68639 0.33530 0.49992 0.04117  -0.10029 0.02215  115 ILE A CA  
752  C C   . ILE A 102 ? 0.69416 0.30970 0.55692 0.03170  -0.08253 0.03936  115 ILE A C   
753  O O   . ILE A 102 ? 0.72864 0.32013 0.66098 0.01041  -0.06496 0.01889  115 ILE A O   
754  C CB  . ILE A 102 ? 0.70665 0.36007 0.51599 0.03108  -0.11353 -0.01971 115 ILE A CB  
755  C CG1 . ILE A 102 ? 0.69506 0.35728 0.49232 0.02809  -0.12791 -0.04805 115 ILE A CG1 
756  C CG2 . ILE A 102 ? 0.71427 0.39680 0.48007 0.04214  -0.12144 -0.02152 115 ILE A CG2 
757  C CD1 . ILE A 102 ? 0.72097 0.39580 0.59540 0.00423  -0.11612 -0.08761 115 ILE A CD1 
758  N N   . GLY A 103 ? 0.69961 0.32712 0.54224 0.04340  -0.07805 0.07244  116 GLY A N   
759  C CA  . GLY A 103 ? 0.70344 0.31943 0.61044 0.03329  -0.04293 0.09629  116 GLY A CA  
760  C C   . GLY A 103 ? 0.69786 0.34792 0.65386 0.00562  -0.04052 0.05257  116 GLY A C   
761  O O   . GLY A 103 ? 0.67189 0.31232 0.72403 -0.01805 -0.00573 0.04005  116 GLY A O   
762  N N   . VAL A 104 ? 0.68196 0.37497 0.58185 0.00993  -0.07311 0.02579  117 VAL A N   
763  C CA  . VAL A 104 ? 0.69252 0.43438 0.63031 -0.00751 -0.07656 -0.01781 117 VAL A CA  
764  C C   . VAL A 104 ? 0.68399 0.44785 0.61101 -0.00009 -0.06409 0.01805  117 VAL A C   
765  O O   . VAL A 104 ? 0.68604 0.46318 0.53099 0.02283  -0.08365 0.04249  117 VAL A O   
766  C CB  . VAL A 104 ? 0.67615 0.45555 0.55543 0.00217  -0.11551 -0.06478 117 VAL A CB  
767  C CG1 . VAL A 104 ? 0.65292 0.49571 0.58558 -0.01167 -0.12106 -0.12255 117 VAL A CG1 
768  C CG2 . VAL A 104 ? 0.66957 0.41902 0.53524 0.00420  -0.12626 -0.08599 117 VAL A CG2 
769  N N   . THR A 105 ? 0.65500 0.42192 0.67227 -0.02008 -0.02674 0.01852  118 THR A N   
770  C CA  . THR A 105 ? 0.64207 0.43517 0.66054 -0.01633 -0.01161 0.04361  118 THR A CA  
771  C C   . THR A 105 ? 0.65906 0.51964 0.67794 -0.02510 -0.04026 -0.01377 118 THR A C   
772  O O   . THR A 105 ? 0.66047 0.55080 0.70367 -0.03573 -0.06168 -0.07615 118 THR A O   
773  C CB  . THR A 105 ? 0.65222 0.41690 0.77700 -0.03290 0.05037  0.06760  118 THR A CB  
774  O OG1 . THR A 105 ? 0.63027 0.40406 0.87111 -0.06906 0.06691  0.00173  118 THR A OG1 
775  C CG2 . THR A 105 ? 0.72015 0.42212 0.82942 -0.00971 0.08197  0.13699  118 THR A CG2 
776  N N   . PRO A 106 ? 0.62776 0.51992 0.61502 -0.01513 -0.04236 0.00542  119 PRO A N   
777  C CA  . PRO A 106 ? 0.61051 0.57309 0.60852 -0.02017 -0.06550 -0.04896 119 PRO A CA  
778  C C   . PRO A 106 ? 0.60479 0.60272 0.73275 -0.05279 -0.04528 -0.11286 119 PRO A C   
779  O O   . PRO A 106 ? 0.60317 0.67086 0.74558 -0.05317 -0.07458 -0.18015 119 PRO A O   
780  C CB  . PRO A 106 ? 0.63202 0.61019 0.59107 -0.00707 -0.05835 -0.00684 119 PRO A CB  
781  C CG  . PRO A 106 ? 0.64359 0.57261 0.52557 0.01658  -0.05478 0.05921  119 PRO A CG  
782  C CD  . PRO A 106 ? 0.63414 0.50885 0.56109 0.00828  -0.03046 0.07363  119 PRO A CD  
783  N N   . PHE A 107 ? 0.60509 0.56093 0.83315 -0.07649 0.00781  -0.09628 120 PHE A N   
784  C CA  . PHE A 107 ? 0.58043 0.56631 0.95671 -0.11290 0.03625  -0.16679 120 PHE A CA  
785  C C   . PHE A 107 ? 0.56981 0.57736 0.96735 -0.12049 0.00746  -0.23560 120 PHE A C   
786  O O   . PHE A 107 ? 0.56484 0.64825 1.04084 -0.13632 -0.00555 -0.32430 120 PHE A O   
787  C CB  . PHE A 107 ? 0.62873 0.54715 1.10896 -0.13274 0.11238  -0.12430 120 PHE A CB  
788  N N   . ASP A 108 ? 0.58683 0.53615 0.91809 -0.10691 -0.00304 -0.20067 121 ASP A N   
789  C CA  . ASP A 108 ? 0.58429 0.55159 0.92201 -0.10967 -0.03086 -0.26105 121 ASP A CA  
790  C C   . ASP A 108 ? 0.60903 0.65683 0.86708 -0.08353 -0.08836 -0.31007 121 ASP A C   
791  O O   . ASP A 108 ? 0.60900 0.72092 0.90537 -0.08325 -0.10482 -0.38068 121 ASP A O   
792  C CB  . ASP A 108 ? 0.57330 0.46150 0.84562 -0.09653 -0.03118 -0.20806 121 ASP A CB  
793  C CG  . ASP A 108 ? 0.59976 0.41111 0.94200 -0.11052 0.02729  -0.15393 121 ASP A CG  
794  O OD1 . ASP A 108 ? 0.62709 0.43649 1.10582 -0.14205 0.07270  -0.18798 121 ASP A OD1 
795  O OD2 . ASP A 108 ? 0.60581 0.36230 0.87064 -0.08645 0.03113  -0.07939 121 ASP A OD2 
796  N N   . LEU A 109 ? 0.63421 0.68174 0.77454 -0.05259 -0.11216 -0.26184 122 LEU A N   
797  C CA  . LEU A 109 ? 0.65514 0.77173 0.71448 -0.01928 -0.15684 -0.29544 122 LEU A CA  
798  C C   . LEU A 109 ? 0.64924 0.85740 0.77990 -0.02209 -0.15462 -0.34689 122 LEU A C   
799  O O   . LEU A 109 ? 0.66892 0.93014 0.78656 0.00457  -0.16199 -0.36589 122 LEU A O   
800  C CB  . LEU A 109 ? 0.66091 0.74971 0.60056 0.01057  -0.16780 -0.22780 122 LEU A CB  
801  C CG  . LEU A 109 ? 0.67595 0.69240 0.53028 0.02694  -0.16723 -0.17390 122 LEU A CG  
802  C CD1 . LEU A 109 ? 0.66381 0.66638 0.45316 0.04255  -0.15396 -0.10942 122 LEU A CD1 
803  C CD2 . LEU A 109 ? 0.68530 0.71066 0.52808 0.03766  -0.15740 -0.17533 122 LEU A CD2 
804  N N   . ALA A 110 ? 0.58934 0.81148 0.80264 -0.05083 -0.13445 -0.35804 123 ALA A N   
805  C CA  . ALA A 110 ? 0.57596 0.89110 0.87417 -0.05700 -0.13234 -0.42086 123 ALA A CA  
806  C C   . ALA A 110 ? 0.54303 0.89539 0.94840 -0.06916 -0.11327 -0.48308 123 ALA A C   
807  O O   . ALA A 110 ? 0.57105 1.00897 0.99274 -0.04403 -0.12346 -0.52865 123 ALA A O   
808  C CB  . ALA A 110 ? 0.53078 0.83335 0.90479 -0.08672 -0.09515 -0.39979 123 ALA A CB  
809  N N   . VAL A 111 ? 0.55398 0.84392 1.03635 -0.10332 -0.08134 -0.48391 124 VAL A N   
810  C CA  . VAL A 111 ? 0.58436 0.90903 1.16799 -0.11192 -0.05915 -0.54074 124 VAL A CA  
811  C C   . VAL A 111 ? 0.58715 0.95727 1.08877 -0.06989 -0.09602 -0.55351 124 VAL A C   
812  O O   . VAL A 111 ? 0.60907 1.06774 1.16475 -0.05393 -0.09882 -0.61540 124 VAL A O   
813  C CB  . VAL A 111 ? 0.60286 0.83604 1.27183 -0.14941 -0.00881 -0.51786 124 VAL A CB  
814  C CG1 . VAL A 111 ? 0.63119 0.89609 1.36921 -0.14848 0.00425  -0.56812 124 VAL A CG1 
815  C CG2 . VAL A 111 ? 0.62358 0.82176 1.40950 -0.18487 0.05100  -0.50578 124 VAL A CG2 
816  N N   . ASP A 112 ? 0.60829 0.91887 0.98531 -0.04949 -0.11933 -0.49498 125 ASP A N   
817  C CA  . ASP A 112 ? 0.60667 0.94540 0.90977 -0.01025 -0.14274 -0.49310 125 ASP A CA  
818  C C   . ASP A 112 ? 0.60153 1.02380 0.86072 0.03352  -0.16312 -0.50459 125 ASP A C   
819  O O   . ASP A 112 ? 0.60848 1.10248 0.88306 0.06193  -0.17199 -0.54319 125 ASP A O   
820  C CB  . ASP A 112 ? 0.61404 0.86219 0.80121 0.00048  -0.15215 -0.42338 125 ASP A CB  
821  C CG  . ASP A 112 ? 0.65496 0.82237 0.88473 -0.03521 -0.13182 -0.41181 125 ASP A CG  
822  O OD1 . ASP A 112 ? 0.57941 0.76212 0.92243 -0.06094 -0.10794 -0.45485 125 ASP A OD1 
823  O OD2 . ASP A 112 ? 0.70329 0.79228 0.85930 -0.03450 -0.13476 -0.35835 125 ASP A OD2 
824  N N   . ASP A 113 ? 0.58916 1.00570 0.79786 0.04231  -0.16867 -0.47130 126 ASP A N   
825  C CA  . ASP A 113 ? 0.62972 1.11614 0.80185 0.08486  -0.18121 -0.47499 126 ASP A CA  
826  C C   . ASP A 113 ? 0.62110 1.21260 0.90306 0.08116  -0.17731 -0.55443 126 ASP A C   
827  O O   . ASP A 113 ? 0.65913 1.32572 0.92524 0.12120  -0.18808 -0.57139 126 ASP A O   
828  C CB  . ASP A 113 ? 0.73648 1.17123 0.81762 0.09514  -0.18254 -0.40593 126 ASP A CB  
829  C CG  . ASP A 113 ? 0.77597 1.11960 0.75657 0.10627  -0.17941 -0.33324 126 ASP A CG  
830  O OD1 . ASP A 113 ? 0.72828 1.01686 0.70795 0.08507  -0.17612 -0.32458 126 ASP A OD1 
831  O OD2 . ASP A 113 ? 0.79214 1.11907 0.70821 0.13371  -0.17514 -0.28877 126 ASP A OD2 
832  N N   . GLY A 114 ? 0.94768 0.67580 1.22020 0.24306  -0.05454 -0.42814 127 GLY A N   
833  C CA  . GLY A 114 ? 0.99801 0.77426 1.33237 0.19572  -0.10175 -0.50073 127 GLY A CA  
834  C C   . GLY A 114 ? 0.97614 0.87462 1.39679 0.16996  -0.11855 -0.48950 127 GLY A C   
835  O O   . GLY A 114 ? 0.95661 0.94500 1.39697 0.16694  -0.16812 -0.53916 127 GLY A O   
836  N N   . ASN A 115 ? 0.93381 0.84029 1.40676 0.15286  -0.07919 -0.42689 128 ASN A N   
837  C CA  . ASN A 115 ? 0.86117 0.87577 1.41389 0.13169  -0.08449 -0.40867 128 ASN A CA  
838  C C   . ASN A 115 ? 0.87080 0.89407 1.53480 0.05260  -0.08660 -0.43053 128 ASN A C   
839  O O   . ASN A 115 ? 0.82023 0.92482 1.56161 0.02901  -0.08359 -0.41274 128 ASN A O   
840  C CB  . ASN A 115 ? 0.81632 0.83798 1.36397 0.15686  -0.03812 -0.33413 128 ASN A CB  
841  C CG  . ASN A 115 ? 0.82767 0.90423 1.31496 0.22956  -0.03781 -0.31436 128 ASN A CG  
842  O OD1 . ASN A 115 ? 0.84650 0.87837 1.24825 0.28201  -0.03859 -0.32199 128 ASN A OD1 
843  N ND2 . ASN A 115 ? 0.78340 0.95227 1.31614 0.23567  -0.02983 -0.28633 128 ASN A ND2 
844  N N   . GLU A 116 ? 0.88974 0.82672 1.56787 0.01280  -0.08478 -0.46715 129 GLU A N   
845  C CA  . GLU A 116 ? 0.87997 0.81824 1.67120 -0.06168 -0.08461 -0.50040 129 GLU A CA  
846  C C   . GLU A 116 ? 0.82994 0.78415 1.69925 -0.09622 -0.04053 -0.44147 129 GLU A C   
847  O O   . GLU A 116 ? 0.82159 0.68716 1.70851 -0.12437 0.00496  -0.41003 129 GLU A O   
848  C CB  . GLU A 116 ? 0.91560 0.95975 1.76321 -0.07836 -0.14575 -0.57528 129 GLU A CB  
849  N N   . ASP A 117 ? 0.82616 0.89145 1.73912 -0.09076 -0.05108 -0.42497 130 ASP A N   
850  C CA  . ASP A 117 ? 0.76835 0.85314 1.75578 -0.12403 -0.00848 -0.37458 130 ASP A CA  
851  C C   . ASP A 117 ? 0.72654 0.73587 1.64724 -0.10113 0.04181  -0.30316 130 ASP A C   
852  O O   . ASP A 117 ? 0.73191 0.68799 1.68653 -0.13394 0.08529  -0.26831 130 ASP A O   
853  C CB  . ASP A 117 ? 0.71686 0.93336 1.75110 -0.11153 -0.02663 -0.36723 130 ASP A CB  
854  C CG  . ASP A 117 ? 0.75433 1.06463 1.83504 -0.11518 -0.09016 -0.43874 130 ASP A CG  
855  O OD1 . ASP A 117 ? 0.80439 1.11563 1.97784 -0.17100 -0.10523 -0.49150 130 ASP A OD1 
856  O OD2 . ASP A 117 ? 0.76991 1.15417 1.79634 -0.06010 -0.12403 -0.44321 130 ASP A OD2 
857  N N   . ILE A 118 ? 0.79803 0.80360 1.62527 -0.04217 0.03756  -0.28124 131 ILE A N   
858  C CA  . ILE A 118 ? 0.71733 0.66174 1.48875 -0.01903 0.07780  -0.22218 131 ILE A CA  
859  C C   . ILE A 118 ? 0.75760 0.58570 1.51049 -0.03682 0.09853  -0.21745 131 ILE A C   
860  O O   . ILE A 118 ? 0.76825 0.54826 1.51649 -0.04458 0.13593  -0.16976 131 ILE A O   
861  C CB  . ILE A 118 ? 0.65143 0.61281 1.34320 0.04645  0.07113  -0.20832 131 ILE A CB  
862  C CG1 . ILE A 118 ? 0.62905 0.70329 1.34296 0.06796  0.05850  -0.20776 131 ILE A CG1 
863  C CG2 . ILE A 118 ? 0.60936 0.51872 1.25996 0.06724  0.10807  -0.15547 131 ILE A CG2 
864  C CD1 . ILE A 118 ? 0.61745 0.70870 1.27998 0.12365  0.08042  -0.17058 131 ILE A CD1 
865  N N   . ALA A 119 ? 0.80836 0.58960 1.54790 -0.04096 0.07579  -0.26700 132 ALA A N   
866  C CA  . ALA A 119 ? 0.82856 0.50854 1.53982 -0.05359 0.09881  -0.25585 132 ALA A CA  
867  C C   . ALA A 119 ? 0.84658 0.51548 1.61544 -0.10239 0.13054  -0.23361 132 ALA A C   
868  O O   . ALA A 119 ? 0.83802 0.45799 1.56428 -0.09704 0.16333  -0.18205 132 ALA A O   
869  C CB  . ALA A 119 ? 0.85381 0.49782 1.53321 -0.04988 0.06960  -0.31517 132 ALA A CB  
870  N N   . GLU A 120 ? 0.81658 0.53897 1.67816 -0.14443 0.12047  -0.27096 133 GLU A N   
871  C CA  . GLU A 120 ? 0.86170 0.57183 1.77114 -0.18128 0.15703  -0.24774 133 GLU A CA  
872  C C   . GLU A 120 ? 0.80743 0.53631 1.70962 -0.17308 0.19315  -0.18162 133 GLU A C   
873  O O   . GLU A 120 ? 0.85090 0.53530 1.73653 -0.17736 0.23252  -0.14011 133 GLU A O   
874  C CB  . GLU A 120 ? 0.89876 0.66721 1.90664 -0.22375 0.13583  -0.30593 133 GLU A CB  
875  C CG  . GLU A 120 ? 0.84409 0.72243 1.90744 -0.22487 0.09911  -0.33282 133 GLU A CG  
876  C CD  . GLU A 120 ? 0.84313 0.77156 1.95891 -0.24085 0.12965  -0.29183 133 GLU A CD  
877  O OE1 . GLU A 120 ? 0.86840 0.74011 1.96619 -0.24553 0.17892  -0.24219 133 GLU A OE1 
878  O OE2 . GLU A 120 ? 0.79401 0.81920 1.95980 -0.24286 0.10408  -0.30789 133 GLU A OE2 
879  N N   . VAL A 121 ? 0.80936 0.60374 1.72026 -0.15846 0.18154  -0.17255 134 VAL A N   
880  C CA  . VAL A 121 ? 0.79572 0.60613 1.68340 -0.14666 0.21509  -0.11288 134 VAL A CA  
881  C C   . VAL A 121 ? 0.80485 0.55505 1.59976 -0.11206 0.23338  -0.06566 134 VAL A C   
882  O O   . VAL A 121 ? 0.82119 0.55392 1.58464 -0.10689 0.26454  -0.02058 134 VAL A O   
883  C CB  . VAL A 121 ? 0.70335 0.60230 1.61936 -0.13739 0.20165  -0.11368 134 VAL A CB  
884  C CG1 . VAL A 121 ? 0.63382 0.54443 1.51181 -0.12455 0.23574  -0.05862 134 VAL A CG1 
885  C CG2 . VAL A 121 ? 0.65887 0.63540 1.66234 -0.16629 0.17629  -0.15871 134 VAL A CG2 
886  N N   . LEU A 122 ? 0.85269 0.57514 1.59678 -0.08354 0.21125  -0.07698 135 LEU A N   
887  C CA  . LEU A 122 ? 0.86428 0.54756 1.52126 -0.04948 0.22069  -0.03477 135 LEU A CA  
888  C C   . LEU A 122 ? 0.99087 0.61151 1.62746 -0.05983 0.24500  -0.01268 135 LEU A C   
889  O O   . LEU A 122 ? 1.03496 0.63717 1.61908 -0.03936 0.26112  0.03085  135 LEU A O   
890  C CB  . LEU A 122 ? 0.81721 0.49084 1.41884 -0.01590 0.19147  -0.05213 135 LEU A CB  
891  C CG  . LEU A 122 ? 0.74082 0.47286 1.32160 0.01566  0.17785  -0.04783 135 LEU A CG  
892  C CD1 . LEU A 122 ? 0.65632 0.38843 1.19653 0.04304  0.14831  -0.07939 135 LEU A CD1 
893  C CD2 . LEU A 122 ? 0.71467 0.45787 1.23466 0.03678  0.18732  -0.00297 135 LEU A CD2 
894  N N   . GLN A 123 ? 0.94279 0.53315 1.62462 -0.09024 0.24806  -0.04480 136 GLN A N   
895  C CA  . GLN A 123 ? 1.00517 0.53342 1.68492 -0.10248 0.27873  -0.02807 136 GLN A CA  
896  C C   . GLN A 123 ? 1.07456 0.55791 1.67398 -0.06766 0.28938  0.01701  136 GLN A C   
897  O O   . GLN A 123 ? 1.15006 0.57967 1.72862 -0.06382 0.29258  0.01253  136 GLN A O   
898  C CB  . GLN A 123 ? 1.03229 0.57297 1.76522 -0.12768 0.31424  -0.01009 136 GLN A CB  
899  C CG  . GLN A 123 ? 1.00086 0.57592 1.70418 -0.10942 0.32927  0.03515  136 GLN A CG  
900  C CD  . GLN A 123 ? 1.07293 0.60607 1.69971 -0.07700 0.34977  0.08749  136 GLN A CD  
901  O OE1 . GLN A 123 ? 1.13020 0.60588 1.74705 -0.07571 0.37339  0.10257  136 GLN A OE1 
902  N NE2 . GLN A 123 ? 1.03147 0.59602 1.60797 -0.04965 0.34097  0.11356  136 GLN A NE2 
903  N N   . GLU B 1   ? 0.75855 0.54809 0.94918 0.17638  -0.37226 -0.16308 21  GLU B N   
904  C CA  . GLU B 1   ? 0.83645 0.60736 1.03804 0.19006  -0.43928 -0.18291 21  GLU B CA  
905  C C   . GLU B 1   ? 0.82772 0.57834 1.01081 0.18736  -0.46334 -0.20338 21  GLU B C   
906  O O   . GLU B 1   ? 0.87885 0.59768 0.98066 0.20599  -0.49711 -0.22433 21  GLU B O   
907  C CB  . GLU B 1   ? 0.84337 0.63536 1.17078 0.18328  -0.46554 -0.17586 21  GLU B CB  
908  C CG  . GLU B 1   ? 0.84151 0.62090 1.22529 0.18538  -0.53345 -0.19780 21  GLU B CG  
909  C CD  . GLU B 1   ? 0.84496 0.65031 1.37745 0.17400  -0.55106 -0.18574 21  GLU B CD  
910  O OE1 . GLU B 1   ? 0.82066 0.64186 1.38609 0.17887  -0.54478 -0.16945 21  GLU B OE1 
911  O OE2 . GLU B 1   ? 0.82985 0.63915 1.45167 0.15988  -0.56779 -0.19058 21  GLU B OE2 
912  N N   . THR B 2   ? 0.79090 0.55847 1.04875 0.16609  -0.44320 -0.19597 22  THR B N   
913  C CA  . THR B 2   ? 0.78380 0.53538 1.03241 0.16087  -0.45462 -0.21072 22  THR B CA  
914  C C   . THR B 2   ? 0.74925 0.50599 0.94341 0.15147  -0.39861 -0.19784 22  THR B C   
915  O O   . THR B 2   ? 0.75446 0.49874 0.93573 0.14746  -0.40112 -0.20655 22  THR B O   
916  C CB  . THR B 2   ? 0.77284 0.53851 1.15415 0.14503  -0.47575 -0.21006 22  THR B CB  
917  O OG1 . THR B 2   ? 0.71825 0.51705 1.16743 0.12661  -0.41998 -0.17981 22  THR B OG1 
918  C CG2 . THR B 2   ? 0.80163 0.56850 1.25758 0.15162  -0.53047 -0.21896 22  THR B CG2 
919  N N   . HIS B 3   ? 0.75483 0.52880 0.91977 0.14817  -0.35045 -0.17827 23  HIS B N   
920  C CA  . HIS B 3   ? 0.72164 0.50321 0.84087 0.13864  -0.30054 -0.16584 23  HIS B CA  
921  C C   . HIS B 3   ? 0.72788 0.49882 0.74957 0.15080  -0.27992 -0.16496 23  HIS B C   
922  O O   . HIS B 3   ? 0.74252 0.50939 0.74755 0.16353  -0.29009 -0.16577 23  HIS B O   
923  C CB  . HIS B 3   ? 0.67833 0.49260 0.86716 0.12080  -0.25712 -0.14210 23  HIS B CB  
924  C CG  . HIS B 3   ? 0.66517 0.49057 0.94212 0.10815  -0.26106 -0.13560 23  HIS B CG  
925  N ND1 . HIS B 3   ? 0.64334 0.47270 1.02001 0.10660  -0.29519 -0.13838 23  HIS B ND1 
926  C CD2 . HIS B 3   ? 0.62564 0.45962 0.91272 0.09713  -0.23505 -0.12423 23  HIS B CD2 
927  C CE1 . HIS B 3   ? 0.63073 0.47004 1.07928 0.09496  -0.28755 -0.12859 23  HIS B CE1 
928  N NE2 . HIS B 3   ? 0.61442 0.45684 1.00734 0.08973  -0.25033 -0.11897 23  HIS B NE2 
929  N N   . ILE B 4   ? 0.76681 0.53407 0.73130 0.14705  -0.25055 -0.16116 24  ILE B N   
930  C CA  . ILE B 4   ? 0.78030 0.53675 0.66127 0.15742  -0.22859 -0.15878 24  ILE B CA  
931  C C   . ILE B 4   ? 0.76586 0.54063 0.63839 0.14160  -0.18310 -0.14484 24  ILE B C   
932  O O   . ILE B 4   ? 0.73471 0.51947 0.63241 0.12845  -0.17420 -0.14004 24  ILE B O   
933  C CB  . ILE B 4   ? 0.81031 0.53265 0.61600 0.17637  -0.25057 -0.17276 24  ILE B CB  
934  C CG1 . ILE B 4   ? 0.83673 0.54959 0.56759 0.18611  -0.21978 -0.16465 24  ILE B CG1 
935  C CG2 . ILE B 4   ? 0.86886 0.58386 0.68584 0.16862  -0.25938 -0.17986 24  ILE B CG2 
936  C CD1 . ILE B 4   ? 0.92692 0.60429 0.58154 0.20864  -0.23337 -0.17413 24  ILE B CD1 
937  N N   . ASN B 5   ? 0.77507 0.55419 0.61551 0.14354  -0.15595 -0.13825 25  ASN B N   
938  C CA  . ASN B 5   ? 0.76382 0.55628 0.58601 0.13102  -0.11842 -0.12924 25  ASN B CA  
939  C C   . ASN B 5   ? 0.78848 0.56304 0.54573 0.13865  -0.11314 -0.13050 25  ASN B C   
940  O O   . ASN B 5   ? 0.80333 0.55794 0.52004 0.15624  -0.12037 -0.13356 25  ASN B O   
941  C CB  . ASN B 5   ? 0.75627 0.56125 0.58753 0.12825  -0.09272 -0.12433 25  ASN B CB  
942  C CG  . ASN B 5   ? 0.73797 0.56052 0.63700 0.12191  -0.09066 -0.11988 25  ASN B CG  
943  O OD1 . ASN B 5   ? 0.71560 0.55170 0.65638 0.11136  -0.08709 -0.11412 25  ASN B OD1 
944  N ND2 . ASN B 5   ? 0.77902 0.60156 0.69459 0.12959  -0.09026 -0.11954 25  ASN B ND2 
945  N N   . LEU B 6   ? 0.74482 0.52682 0.49504 0.12708  -0.09886 -0.12521 26  LEU B N   
946  C CA  . LEU B 6   ? 0.74290 0.51157 0.44443 0.13199  -0.08985 -0.12278 26  LEU B CA  
947  C C   . LEU B 6   ? 0.70442 0.49286 0.40606 0.11610  -0.06292 -0.11403 26  LEU B C   
948  O O   . LEU B 6   ? 0.68778 0.49757 0.41945 0.10227  -0.05380 -0.10999 26  LEU B O   
949  C CB  . LEU B 6   ? 0.78641 0.53944 0.47879 0.13653  -0.10750 -0.12631 26  LEU B CB  
950  C CG  . LEU B 6   ? 0.82014 0.54279 0.48589 0.15802  -0.13623 -0.13918 26  LEU B CG  
951  C CD1 . LEU B 6   ? 0.81756 0.53096 0.50445 0.15633  -0.15967 -0.14807 26  LEU B CD1 
952  C CD2 . LEU B 6   ? 0.89450 0.59605 0.50244 0.17563  -0.12455 -0.13387 26  LEU B CD2 
953  N N   . LYS B 7   ? 0.72171 0.50203 0.39017 0.11979  -0.05043 -0.11042 27  LYS B N   
954  C CA  . LYS B 7   ? 0.68545 0.48199 0.35236 0.10569  -0.03202 -0.10432 27  LYS B CA  
955  C C   . LYS B 7   ? 0.76281 0.55186 0.41288 0.10685  -0.03207 -0.09647 27  LYS B C   
956  O O   . LYS B 7   ? 0.78039 0.54729 0.40704 0.12199  -0.03282 -0.09495 27  LYS B O   
957  C CB  . LYS B 7   ? 0.68244 0.47896 0.34239 0.10633  -0.01649 -0.10679 27  LYS B CB  
958  C CG  . LYS B 7   ? 0.71614 0.53039 0.37852 0.09034  -0.00362 -0.10644 27  LYS B CG  
959  C CD  . LYS B 7   ? 0.73528 0.54154 0.39005 0.09255  0.00555  -0.10494 27  LYS B CD  
960  C CE  . LYS B 7   ? 0.71208 0.51264 0.37577 0.09727  0.01585  -0.11242 27  LYS B CE  
961  N NZ  . LYS B 7   ? 0.72268 0.52623 0.39550 0.08914  0.02562  -0.11614 27  LYS B NZ  
962  N N   . VAL B 8   ? 0.73484 0.54172 0.39661 0.09298  -0.02917 -0.08924 28  VAL B N   
963  C CA  . VAL B 8   ? 0.72321 0.52744 0.37780 0.09195  -0.02776 -0.07888 28  VAL B CA  
964  C C   . VAL B 8   ? 0.68788 0.50910 0.34153 0.08020  -0.01705 -0.07328 28  VAL B C   
965  O O   . VAL B 8   ? 0.70711 0.54927 0.36676 0.06809  -0.01434 -0.07386 28  VAL B O   
966  C CB  . VAL B 8   ? 0.68054 0.49159 0.35463 0.08668  -0.03585 -0.07262 28  VAL B CB  
967  C CG1 . VAL B 8   ? 0.69379 0.50050 0.36369 0.08711  -0.03296 -0.06057 28  VAL B CG1 
968  C CG2 . VAL B 8   ? 0.63260 0.42631 0.31552 0.09695  -0.05213 -0.08295 28  VAL B CG2 
969  N N   . SER B 9   ? 0.69747 0.50825 0.34424 0.08535  -0.01120 -0.06791 29  SER B N   
970  C CA  . SER B 9   ? 0.73097 0.55511 0.38492 0.07486  -0.00612 -0.06493 29  SER B CA  
971  C C   . SER B 9   ? 0.75540 0.57676 0.41826 0.07596  -0.00453 -0.04929 29  SER B C   
972  O O   . SER B 9   ? 0.78587 0.58641 0.44337 0.09009  0.00002  -0.04235 29  SER B O   
973  C CB  . SER B 9   ? 0.72110 0.53638 0.37697 0.07934  0.00216  -0.07355 29  SER B CB  
974  O OG  . SER B 9   ? 0.77332 0.59917 0.44430 0.06881  0.00314  -0.07328 29  SER B OG  
975  N N   . ASP B 10  ? 0.74502 0.58645 0.42042 0.06230  -0.00882 -0.04391 30  ASP B N   
976  C CA  . ASP B 10  ? 0.76970 0.61251 0.46501 0.06145  -0.00827 -0.02719 30  ASP B CA  
977  C C   . ASP B 10  ? 0.82222 0.67009 0.54031 0.05524  -0.00893 -0.02871 30  ASP B C   
978  O O   . ASP B 10  ? 0.82265 0.67980 0.56692 0.04956  -0.01386 -0.01555 30  ASP B O   
979  C CB  . ASP B 10  ? 0.75674 0.62040 0.45667 0.05140  -0.01775 -0.01498 30  ASP B CB  
980  C CG  . ASP B 10  ? 0.75237 0.64145 0.44246 0.03728  -0.02877 -0.02175 30  ASP B CG  
981  O OD1 . ASP B 10  ? 0.79218 0.68077 0.47071 0.03475  -0.02868 -0.03947 30  ASP B OD1 
982  O OD2 . ASP B 10  ? 0.73509 0.64326 0.42654 0.03054  -0.03644 -0.00874 30  ASP B OD2 
983  N N   . GLY B 11  ? 0.86043 0.70239 0.57632 0.05604  -0.00511 -0.04433 31  GLY B N   
984  C CA  . GLY B 11  ? 0.79895 0.64447 0.54362 0.04902  -0.00750 -0.05003 31  GLY B CA  
985  C C   . GLY B 11  ? 0.81669 0.68200 0.55290 0.03258  -0.02482 -0.06756 31  GLY B C   
986  O O   . GLY B 11  ? 0.80264 0.66683 0.55784 0.02701  -0.02855 -0.08175 31  GLY B O   
987  N N   . SER B 12  ? 0.83727 0.71874 0.54491 0.02641  -0.03441 -0.06695 32  SER B N   
988  C CA  . SER B 12  ? 0.79036 0.68735 0.47438 0.01567  -0.04775 -0.08333 32  SER B CA  
989  C C   . SER B 12  ? 0.79242 0.69522 0.43884 0.01773  -0.04105 -0.08720 32  SER B C   
990  O O   . SER B 12  ? 0.83901 0.74703 0.45973 0.01387  -0.04333 -0.10403 32  SER B O   
991  C CB  . SER B 12  ? 0.75595 0.67190 0.44565 0.00629  -0.06897 -0.07426 32  SER B CB  
992  N N   . SER B 13  ? 0.79899 0.69942 0.44434 0.02455  -0.03222 -0.07288 33  SER B N   
993  C CA  . SER B 13  ? 0.78749 0.69346 0.41345 0.02685  -0.02448 -0.07329 33  SER B CA  
994  C C   . SER B 13  ? 0.74671 0.63525 0.38333 0.03651  -0.01426 -0.07641 33  SER B C   
995  O O   . SER B 13  ? 0.73652 0.61288 0.38599 0.04356  -0.01440 -0.06713 33  SER B O   
996  C CB  . SER B 13  ? 0.77652 0.69822 0.40082 0.02540  -0.02758 -0.05217 33  SER B CB  
997  O OG  . SER B 13  ? 0.77303 0.69616 0.39774 0.02975  -0.01711 -0.04790 33  SER B OG  
998  N N   . GLU B 14  ? 0.76023 0.64640 0.38993 0.03834  -0.00608 -0.08949 34  GLU B N   
999  C CA  . GLU B 14  ? 0.72306 0.59446 0.36436 0.04778  -0.00053 -0.09343 34  GLU B CA  
1000 C C   . GLU B 14  ? 0.73129 0.61126 0.37776 0.04833  0.00474  -0.09084 34  GLU B C   
1001 O O   . GLU B 14  ? 0.72338 0.61499 0.35886 0.04415  0.01337  -0.09444 34  GLU B O   
1002 C CB  . GLU B 14  ? 0.67997 0.53953 0.32374 0.05091  0.00589  -0.10885 34  GLU B CB  
1003 N N   . ILE B 15  ? 0.70486 0.57744 0.36964 0.05480  -0.00022 -0.08469 35  ILE B N   
1004 C CA  . ILE B 15  ? 0.68348 0.56383 0.37066 0.05534  0.00278  -0.07957 35  ILE B CA  
1005 C C   . ILE B 15  ? 0.66085 0.52589 0.36760 0.06448  -0.00442 -0.08762 35  ILE B C   
1006 O O   . ILE B 15  ? 0.68606 0.53368 0.38778 0.07258  -0.01668 -0.09015 35  ILE B O   
1007 C CB  . ILE B 15  ? 0.69775 0.58648 0.40044 0.05292  -0.00198 -0.06289 35  ILE B CB  
1008 C CG1 . ILE B 15  ? 0.70801 0.60992 0.38887 0.04615  -0.00026 -0.05259 35  ILE B CG1 
1009 C CG2 . ILE B 15  ? 0.64271 0.54345 0.37814 0.05236  0.00608  -0.05394 35  ILE B CG2 
1010 C CD1 . ILE B 15  ? 0.69792 0.61416 0.39628 0.04362  0.00124  -0.03184 35  ILE B CD1 
1011 N N   . PHE B 16  ? 0.63570 0.50632 0.36343 0.06505  0.00327  -0.09064 36  PHE B N   
1012 C CA  . PHE B 16  ? 0.64370 0.50328 0.39740 0.07351  -0.00711 -0.09662 36  PHE B CA  
1013 C C   . PHE B 16  ? 0.64269 0.50836 0.44110 0.07284  -0.01584 -0.08822 36  PHE B C   
1014 O O   . PHE B 16  ? 0.63739 0.51997 0.46020 0.06730  -0.00054 -0.07753 36  PHE B O   
1015 C CB  . PHE B 16  ? 0.65667 0.51818 0.41772 0.07501  0.00674  -0.10403 36  PHE B CB  
1016 C CG  . PHE B 16  ? 0.68467 0.53691 0.41502 0.07675  0.01317  -0.11398 36  PHE B CG  
1017 C CD1 . PHE B 16  ? 0.67730 0.51259 0.40334 0.08769  0.00365  -0.11839 36  PHE B CD1 
1018 C CD2 . PHE B 16  ? 0.66266 0.52205 0.37022 0.06889  0.02803  -0.11866 36  PHE B CD2 
1019 C CE1 . PHE B 16  ? 0.67558 0.50258 0.38460 0.09006  0.01274  -0.12403 36  PHE B CE1 
1020 C CE2 . PHE B 16  ? 0.67651 0.52665 0.36855 0.06950  0.03223  -0.12891 36  PHE B CE2 
1021 C CZ  . PHE B 16  ? 0.68483 0.51946 0.38246 0.07974  0.02658  -0.12997 36  PHE B CZ  
1022 N N   . PHE B 17  ? 0.63133 0.48155 0.44125 0.08001  -0.03982 -0.09303 37  PHE B N   
1023 C CA  . PHE B 17  ? 0.63730 0.48923 0.49949 0.07965  -0.05482 -0.08938 37  PHE B CA  
1024 C C   . PHE B 17  ? 0.67691 0.51885 0.56775 0.08823  -0.07495 -0.09984 37  PHE B C   
1025 O O   . PHE B 17  ? 0.73195 0.55589 0.58845 0.09912  -0.08830 -0.11110 37  PHE B O   
1026 C CB  . PHE B 17  ? 0.64233 0.48104 0.49726 0.08167  -0.07221 -0.09040 37  PHE B CB  
1027 C CG  . PHE B 17  ? 0.64137 0.49051 0.47473 0.07402  -0.05586 -0.07750 37  PHE B CG  
1028 C CD1 . PHE B 17  ? 0.60670 0.47466 0.47644 0.06575  -0.04483 -0.06052 37  PHE B CD1 
1029 C CD2 . PHE B 17  ? 0.65790 0.49865 0.43992 0.07629  -0.05137 -0.07960 37  PHE B CD2 
1030 C CE1 . PHE B 17  ? 0.63283 0.51149 0.48180 0.06023  -0.03239 -0.04656 37  PHE B CE1 
1031 C CE2 . PHE B 17  ? 0.61965 0.47142 0.38800 0.06923  -0.04029 -0.06680 37  PHE B CE2 
1032 C CZ  . PHE B 17  ? 0.61404 0.48500 0.41273 0.06137  -0.03220 -0.05061 37  PHE B CZ  
1033 N N   . LYS B 18  ? 0.68107 0.53504 0.63802 0.08476  -0.07670 -0.09365 38  LYS B N   
1034 C CA  . LYS B 18  ? 0.66909 0.51527 0.66841 0.09212  -0.10343 -0.10242 38  LYS B CA  
1035 C C   . LYS B 18  ? 0.69190 0.53344 0.74519 0.09060  -0.13072 -0.10434 38  LYS B C   
1036 O O   . LYS B 18  ? 0.64487 0.50353 0.76517 0.08219  -0.11968 -0.08996 38  LYS B O   
1037 C CB  . LYS B 18  ? 0.63843 0.50146 0.68501 0.08990  -0.08447 -0.09371 38  LYS B CB  
1038 C CG  . LYS B 18  ? 0.63645 0.49226 0.72371 0.09861  -0.11390 -0.10195 38  LYS B CG  
1039 C CD  . LYS B 18  ? 0.58221 0.45698 0.75795 0.09428  -0.10204 -0.08829 38  LYS B CD  
1040 C CE  . LYS B 18  ? 0.57585 0.45195 0.75946 0.10108  -0.09668 -0.08926 38  LYS B CE  
1041 N NZ  . LYS B 18  ? 0.60675 0.49321 0.89069 0.10170  -0.11063 -0.08124 38  LYS B NZ  
1042 N N   . ILE B 19  ? 0.75191 0.56829 0.77660 0.10035  -0.16496 -0.12195 39  ILE B N   
1043 C CA  . ILE B 19  ? 0.71452 0.52048 0.77994 0.09932  -0.19250 -0.12907 39  ILE B CA  
1044 C C   . ILE B 19  ? 0.70916 0.49073 0.77788 0.11279  -0.24057 -0.15216 39  ILE B C   
1045 O O   . ILE B 19  ? 0.73835 0.50678 0.75376 0.12605  -0.25069 -0.16139 39  ILE B O   
1046 C CB  . ILE B 19  ? 0.75998 0.55468 0.77712 0.09864  -0.18494 -0.12922 39  ILE B CB  
1047 C CG1 . ILE B 19  ? 0.76767 0.54349 0.69077 0.11055  -0.18063 -0.13741 39  ILE B CG1 
1048 C CG2 . ILE B 19  ? 0.71544 0.53655 0.75336 0.08462  -0.14747 -0.10493 39  ILE B CG2 
1049 C CD1 . ILE B 19  ? 0.84590 0.59388 0.72505 0.11979  -0.19446 -0.14865 39  ILE B CD1 
1050 N N   . LYS B 20  ? 0.73494 0.50982 0.86867 0.11036  -0.27158 -0.16127 40  LYS B N   
1051 C CA  . LYS B 20  ? 0.73884 0.48873 0.87822 0.12356  -0.32508 -0.18697 40  LYS B CA  
1052 C C   . LYS B 20  ? 0.78887 0.50296 0.82059 0.14254  -0.34131 -0.20712 40  LYS B C   
1053 O O   . LYS B 20  ? 0.83966 0.54517 0.81984 0.14252  -0.31903 -0.20402 40  LYS B O   
1054 C CB  . LYS B 20  ? 0.72026 0.46712 0.95444 0.11612  -0.35667 -0.19580 40  LYS B CB  
1055 C CG  . LYS B 20  ? 0.69754 0.46913 1.04983 0.10641  -0.36417 -0.18413 40  LYS B CG  
1056 C CD  . LYS B 20  ? 0.71249 0.48510 1.17143 0.09598  -0.38342 -0.18599 40  LYS B CD  
1057 C CE  . LYS B 20  ? 0.74781 0.49916 1.25750 0.10336  -0.45109 -0.21591 40  LYS B CE  
1058 N NZ  . LYS B 20  ? 0.73011 0.50192 1.39453 0.09027  -0.46277 -0.20435 40  LYS B NZ  
1059 N N   . LYS B 21  ? 0.79224 0.48507 0.79033 0.16091  -0.37939 -0.22567 41  LYS B N   
1060 C CA  . LYS B 21  ? 0.89265 0.54628 0.78759 0.18430  -0.39731 -0.24522 41  LYS B CA  
1061 C C   . LYS B 21  ? 0.93155 0.57195 0.83575 0.18538  -0.41032 -0.25387 41  LYS B C   
1062 O O   . LYS B 21  ? 0.93467 0.55894 0.76593 0.19878  -0.39536 -0.25124 41  LYS B O   
1063 C CB  . LYS B 21  ? 0.90505 0.54937 0.77363 0.20570  -0.42801 -0.25076 41  LYS B CB  
1064 C CG  . LYS B 21  ? 0.90783 0.56417 0.75537 0.20888  -0.41237 -0.23994 41  LYS B CG  
1065 C CD  . LYS B 21  ? 1.01679 0.65254 0.78411 0.23798  -0.41913 -0.23805 41  LYS B CD  
1066 C CE  . LYS B 21  ? 1.06364 0.68122 0.74792 0.25161  -0.38673 -0.22855 41  LYS B CE  
1067 N NZ  . LYS B 21  ? 1.05160 0.67258 0.68051 0.25925  -0.34728 -0.20985 41  LYS B NZ  
1068 N N   . THR B 22  ? 0.89248 0.53963 0.89387 0.17128  -0.43585 -0.26261 42  THR B N   
1069 C CA  . THR B 22  ? 0.88303 0.51905 0.90808 0.17104  -0.45024 -0.27243 42  THR B CA  
1070 C C   . THR B 22  ? 0.84020 0.48370 0.90746 0.15058  -0.42002 -0.26281 42  THR B C   
1071 O O   . THR B 22  ? 0.85891 0.49735 0.97042 0.14603  -0.43079 -0.26925 42  THR B O   
1072 C CB  . THR B 22  ? 0.90975 0.54764 1.02514 0.17080  -0.49803 -0.28636 42  THR B CB  
1073 O OG1 . THR B 22  ? 0.86205 0.52351 1.10041 0.14540  -0.49374 -0.27751 42  THR B OG1 
1074 C CG2 . THR B 22  ? 0.93730 0.57242 1.03982 0.18555  -0.52521 -0.29069 42  THR B CG2 
1075 N N   . THR B 23  ? 0.80275 0.46726 0.86035 0.13953  -0.37543 -0.23902 43  THR B N   
1076 C CA  . THR B 23  ? 0.82845 0.50827 0.92465 0.12406  -0.34314 -0.22009 43  THR B CA  
1077 C C   . THR B 23  ? 0.86570 0.52637 0.87034 0.13290  -0.32027 -0.21950 43  THR B C   
1078 O O   . THR B 23  ? 0.88614 0.53902 0.80557 0.14492  -0.30694 -0.21827 43  THR B O   
1079 C CB  . THR B 23  ? 0.79339 0.51815 0.94113 0.10626  -0.30028 -0.18503 43  THR B CB  
1080 O OG1 . THR B 23  ? 0.76895 0.50904 0.96749 0.09301  -0.27537 -0.16540 43  THR B OG1 
1081 C CG2 . THR B 23  ? 0.79676 0.53245 0.86252 0.10938  -0.26567 -0.17118 43  THR B CG2 
1082 N N   . PRO B 24  ? 0.84001 0.49162 0.86670 0.12833  -0.31512 -0.21934 44  PRO B N   
1083 C CA  . PRO B 24  ? 0.87087 0.50568 0.82126 0.13653  -0.29069 -0.21533 44  PRO B CA  
1084 C C   . PRO B 24  ? 0.87629 0.54379 0.80087 0.12700  -0.24445 -0.18306 44  PRO B C   
1085 O O   . PRO B 24  ? 0.84789 0.55233 0.82616 0.11050  -0.22469 -0.16030 44  PRO B O   
1086 C CB  . PRO B 24  ? 0.85084 0.47701 0.85819 0.12950  -0.29322 -0.21706 44  PRO B CB  
1087 C CG  . PRO B 24  ? 0.82761 0.44948 0.92264 0.12474  -0.33349 -0.23590 44  PRO B CG  
1088 C CD  . PRO B 24  ? 0.79954 0.45256 0.92819 0.11722  -0.33338 -0.22370 44  PRO B CD  
1089 N N   . LEU B 25  ? 0.88324 0.53490 0.72508 0.13915  -0.22723 -0.18150 45  LEU B N   
1090 C CA  . LEU B 25  ? 0.83389 0.51214 0.64909 0.13139  -0.18907 -0.15525 45  LEU B CA  
1091 C C   . LEU B 25  ? 0.78169 0.48124 0.63090 0.11681  -0.16344 -0.13139 45  LEU B C   
1092 O O   . LEU B 25  ? 0.75820 0.48171 0.59073 0.10902  -0.13598 -0.11007 45  LEU B O   
1093 C CB  . LEU B 25  ? 0.84453 0.49826 0.57235 0.15026  -0.17952 -0.15949 45  LEU B CB  
1094 C CG  . LEU B 25  ? 0.90007 0.53902 0.58717 0.16600  -0.19751 -0.17479 45  LEU B CG  
1095 C CD1 . LEU B 25  ? 0.88215 0.50658 0.50164 0.18456  -0.18165 -0.16679 45  LEU B CD1 
1096 C CD2 . LEU B 25  ? 0.85210 0.52623 0.56472 0.15265  -0.18477 -0.16116 45  LEU B CD2 
1097 N N   . ARG B 26  ? 0.87330 0.48812 0.62179 -0.08548 -0.03796 -0.06991 46  ARG B N   
1098 C CA  . ARG B 26  ? 0.87910 0.46870 0.60963 -0.07027 -0.04180 -0.05602 46  ARG B CA  
1099 C C   . ARG B 26  ? 0.84898 0.48307 0.60162 -0.08746 -0.01976 -0.02203 46  ARG B C   
1100 O O   . ARG B 26  ? 0.83399 0.49629 0.57243 -0.06648 -0.00793 -0.01822 46  ARG B O   
1101 C CB  . ARG B 26  ? 0.92163 0.41543 0.63632 -0.07214 -0.07632 -0.05053 46  ARG B CB  
1102 C CG  . ARG B 26  ? 0.98188 0.43853 0.67461 -0.05242 -0.07868 -0.02888 46  ARG B CG  
1103 C CD  . ARG B 26  ? 1.05569 0.39788 0.71766 -0.04198 -0.11401 -0.03493 46  ARG B CD  
1104 N NE  . ARG B 26  ? 1.16496 0.47666 0.78074 0.00721  -0.11450 -0.03541 46  ARG B NE  
1105 C CZ  . ARG B 26  ? 1.30017 0.51021 0.88875 0.01851  -0.13464 -0.02007 46  ARG B CZ  
1106 N NH1 . ARG B 26  ? 1.26405 0.38836 0.87223 -0.02321 -0.15852 -0.00364 46  ARG B NH1 
1107 N NH2 . ARG B 26  ? 1.31290 0.50723 0.85464 0.07250  -0.13086 -0.01961 46  ARG B NH2 
1108 N N   . ARG B 27  ? 0.81176 0.46181 0.59720 -0.12117 -0.01440 0.00319  47  ARG B N   
1109 C CA  . ARG B 27  ? 0.78697 0.48497 0.58857 -0.13017 0.00734  0.03795  47  ARG B CA  
1110 C C   . ARG B 27  ? 0.76051 0.52653 0.55517 -0.11568 0.03556  0.01940  47  ARG B C   
1111 O O   . ARG B 27  ? 0.74421 0.54669 0.53092 -0.10349 0.04941  0.03092  47  ARG B O   
1112 C CB  . ARG B 27  ? 0.78055 0.48997 0.61986 -0.16603 0.00680  0.07267  47  ARG B CB  
1113 C CG  . ARG B 27  ? 0.78865 0.44126 0.64471 -0.18874 -0.01639 0.10819  47  ARG B CG  
1114 C CD  . ARG B 27  ? 0.81608 0.51813 0.70786 -0.21107 -0.00043 0.16427  47  ARG B CD  
1115 N NE  . ARG B 27  ? 0.90923 0.55663 0.82163 -0.23488 -0.01883 0.20651  47  ARG B NE  
1116 C CZ  . ARG B 27  ? 0.92236 0.55730 0.82399 -0.21873 -0.01036 0.24071  47  ARG B CZ  
1117 N NH1 . ARG B 27  ? 0.88619 0.56723 0.75540 -0.17759 0.01290  0.23368  47  ARG B NH1 
1118 N NH2 . ARG B 27  ? 0.98550 0.56052 0.91001 -0.24487 -0.02636 0.28358  47  ARG B NH2 
1119 N N   . LEU B 28  ? 0.77202 0.55368 0.56828 -0.11605 0.04360  -0.00957 48  LEU B N   
1120 C CA  . LEU B 28  ? 0.70763 0.53876 0.49937 -0.10811 0.06870  -0.02904 48  LEU B CA  
1121 C C   . LEU B 28  ? 0.69368 0.54104 0.46644 -0.08621 0.06742  -0.05033 48  LEU B C   
1122 O O   . LEU B 28  ? 0.64790 0.53618 0.41499 -0.08056 0.07961  -0.05359 48  LEU B O   
1123 C CB  . LEU B 28  ? 0.69333 0.52835 0.49242 -0.11281 0.07851  -0.04892 48  LEU B CB  
1124 C CG  . LEU B 28  ? 0.64692 0.51174 0.44339 -0.10760 0.10122  -0.07429 48  LEU B CG  
1125 C CD1 . LEU B 28  ? 0.63697 0.50660 0.44289 -0.11554 0.12061  -0.07141 48  LEU B CD1 
1126 C CD2 . LEU B 28  ? 0.64207 0.50589 0.43213 -0.09274 0.09368  -0.09832 48  LEU B CD2 
1127 N N   . MET B 29  ? 0.69554 0.51733 0.45600 -0.07023 0.05122  -0.06619 49  MET B N   
1128 C CA  . MET B 29  ? 0.68160 0.52987 0.42499 -0.04504 0.04866  -0.08197 49  MET B CA  
1129 C C   . MET B 29  ? 0.72587 0.57764 0.45547 -0.03191 0.04371  -0.05991 49  MET B C   
1130 O O   . MET B 29  ? 0.71358 0.61837 0.43519 -0.01724 0.04989  -0.06893 49  MET B O   
1131 C CB  . MET B 29  ? 0.71025 0.52874 0.43641 -0.02135 0.03191  -0.09734 49  MET B CB  
1132 C CG  . MET B 29  ? 0.72070 0.53492 0.45661 -0.02738 0.03577  -0.11316 49  MET B CG  
1133 S SD  . MET B 29  ? 0.79507 0.54107 0.50326 -0.00254 0.00606  -0.12267 49  MET B SD  
1134 C CE  . MET B 29  ? 0.78290 0.57487 0.47071 0.04116  0.00959  -0.14449 49  MET B CE  
1135 N N   . GLU B 30  ? 0.73219 0.53165 0.46093 -0.03769 0.03227  -0.02907 50  GLU B N   
1136 C CA  . GLU B 30  ? 0.71949 0.51930 0.43647 -0.02346 0.03136  0.00193  50  GLU B CA  
1137 C C   . GLU B 30  ? 0.69809 0.56609 0.42205 -0.02688 0.05179  0.01161  50  GLU B C   
1138 O O   . GLU B 30  ? 0.69966 0.61000 0.40599 -0.00189 0.05568  0.01478  50  GLU B O   
1139 C CB  . GLU B 30  ? 0.77147 0.49858 0.49631 -0.03908 0.01702  0.03860  50  GLU B CB  
1140 C CG  . GLU B 30  ? 0.87675 0.53393 0.57260 -0.01321 -0.00300 0.04516  50  GLU B CG  
1141 C CD  . GLU B 30  ? 0.92548 0.49096 0.63301 -0.03922 -0.02379 0.06934  50  GLU B CD  
1142 O OE1 . GLU B 30  ? 0.91243 0.48542 0.65639 -0.07888 -0.02208 0.08475  50  GLU B OE1 
1143 O OE2 . GLU B 30  ? 1.01892 0.50461 0.69878 -0.01979 -0.04289 0.07269  50  GLU B OE2 
1144 N N   . ALA B 31  ? 0.66517 0.54729 0.40972 -0.05204 0.06440  0.01538  51  ALA B N   
1145 C CA  . ALA B 31  ? 0.63941 0.58024 0.38158 -0.04854 0.08312  0.02102  51  ALA B CA  
1146 C C   . ALA B 31  ? 0.63469 0.62452 0.36288 -0.03640 0.08827  -0.02225 51  ALA B C   
1147 O O   . ALA B 31  ? 0.65638 0.69597 0.36767 -0.01737 0.09263  -0.02401 51  ALA B O   
1148 C CB  . ALA B 31  ? 0.61642 0.55966 0.37775 -0.07132 0.09629  0.03178  51  ALA B CB  
1149 N N   . PHE B 32  ? 0.65670 0.63810 0.39348 -0.04755 0.08691  -0.05656 52  PHE B N   
1150 C CA  . PHE B 32  ? 0.63029 0.65984 0.36416 -0.04522 0.09005  -0.09557 52  PHE B CA  
1151 C C   . PHE B 32  ? 0.62643 0.69601 0.34427 -0.01780 0.07765  -0.09958 52  PHE B C   
1152 O O   . PHE B 32  ? 0.61556 0.74470 0.32576 -0.01049 0.07783  -0.12067 52  PHE B O   
1153 C CB  . PHE B 32  ? 0.58757 0.60390 0.33955 -0.06208 0.09322  -0.12080 52  PHE B CB  
1154 C CG  . PHE B 32  ? 0.56075 0.62234 0.32179 -0.07367 0.09964  -0.15692 52  PHE B CG  
1155 C CD1 . PHE B 32  ? 0.65644 0.71145 0.42178 -0.09355 0.11479  -0.17194 52  PHE B CD1 
1156 C CD2 . PHE B 32  ? 0.56942 0.67985 0.33505 -0.06492 0.08976  -0.17514 52  PHE B CD2 
1157 C CE1 . PHE B 32  ? 0.61508 0.69931 0.39127 -0.11096 0.11783  -0.20686 52  PHE B CE1 
1158 C CE2 . PHE B 32  ? 0.58409 0.74131 0.36721 -0.08426 0.09283  -0.20739 52  PHE B CE2 
1159 C CZ  . PHE B 32  ? 0.58878 0.72684 0.37828 -0.11057 0.10580  -0.22446 52  PHE B CZ  
1160 N N   . ALA B 33  ? 0.63265 0.66987 0.34176 0.00048  0.06535  -0.08143 53  ALA B N   
1161 C CA  . ALA B 33  ? 0.65272 0.72659 0.34070 0.03542  0.05556  -0.08005 53  ALA B CA  
1162 C C   . ALA B 33  ? 0.67850 0.78047 0.34792 0.05610  0.05890  -0.05368 53  ALA B C   
1163 O O   . ALA B 33  ? 0.68720 0.85946 0.34184 0.08034  0.05632  -0.06581 53  ALA B O   
1164 C CB  . ALA B 33  ? 0.70704 0.72253 0.38083 0.05638  0.04239  -0.06606 53  ALA B CB  
1165 N N   . LYS B 34  ? 0.69422 0.75191 0.36593 0.04834  0.06472  -0.01503 54  LYS B N   
1166 C CA  . LYS B 34  ? 0.72433 0.81274 0.37960 0.07204  0.07162  0.02024  54  LYS B CA  
1167 C C   . LYS B 34  ? 0.70629 0.87371 0.35325 0.07701  0.08015  -0.00502 54  LYS B C   
1168 O O   . LYS B 34  ? 0.73036 0.95833 0.35345 0.11098  0.08041  0.00091  54  LYS B O   
1169 C CB  . LYS B 34  ? 0.74344 0.77875 0.41334 0.05565  0.07809  0.07112  54  LYS B CB  
1170 C CG  . LYS B 34  ? 0.78102 0.72640 0.45778 0.04700  0.06489  0.09612  54  LYS B CG  
1171 C CD  . LYS B 34  ? 0.84672 0.77096 0.50041 0.08151  0.06160  0.13523  54  LYS B CD  
1172 C CE  . LYS B 34  ? 0.89699 0.71843 0.54614 0.07788  0.04297  0.14086  54  LYS B CE  
1173 N NZ  . LYS B 34  ? 0.96589 0.76328 0.57854 0.12429  0.03853  0.16122  54  LYS B NZ  
1174 N N   . ARG B 35  ? 0.67335 0.83820 0.33515 0.04716  0.08657  -0.03422 55  ARG B N   
1175 C CA  . ARG B 35  ? 0.67304 0.89594 0.32025 0.05238  0.09202  -0.06383 55  ARG B CA  
1176 C C   . ARG B 35  ? 0.68038 0.96898 0.31765 0.06441  0.07862  -0.10807 55  ARG B C   
1177 O O   . ARG B 35  ? 0.70011 1.04879 0.31554 0.08148  0.07627  -0.12957 55  ARG B O   
1178 C CB  . ARG B 35  ? 0.65025 0.84163 0.31119 0.02029  0.10224  -0.08643 55  ARG B CB  
1179 C CG  . ARG B 35  ? 0.71589 0.90062 0.36910 0.02655  0.11819  -0.05158 55  ARG B CG  
1180 C CD  . ARG B 35  ? 0.70753 0.84824 0.37610 -0.00091 0.13009  -0.05875 55  ARG B CD  
1181 N NE  . ARG B 35  ? 0.68852 0.84107 0.33656 0.00012  0.13696  -0.10095 55  ARG B NE  
1182 C CZ  . ARG B 35  ? 0.65422 0.77848 0.29867 -0.00695 0.15271  -0.10233 55  ARG B CZ  
1183 N NH1 . ARG B 35  ? 0.63582 0.73573 0.29918 -0.01541 0.16329  -0.06193 55  ARG B NH1 
1184 N NH2 . ARG B 35  ? 0.68262 0.80237 0.30248 -0.00451 0.15670  -0.14612 55  ARG B NH2 
1185 N N   . GLN B 36  ? 0.66516 0.95143 0.31726 0.05823  0.06841  -0.12250 56  GLN B N   
1186 C CA  . GLN B 36  ? 0.67055 1.03529 0.31955 0.07084  0.05467  -0.15667 56  GLN B CA  
1187 C C   . GLN B 36  ? 0.70063 1.10319 0.32460 0.11901  0.04809  -0.12803 56  GLN B C   
1188 O O   . GLN B 36  ? 0.70662 1.17460 0.34078 0.13288  0.03455  -0.14653 56  GLN B O   
1189 C CB  . GLN B 36  ? 0.64305 1.00406 0.32350 0.04263  0.04992  -0.18448 56  GLN B CB  
1190 C CG  . GLN B 36  ? 0.63855 1.01475 0.35145 0.00327  0.04765  -0.22572 56  GLN B CG  
1191 C CD  . GLN B 36  ? 0.69468 1.00012 0.41103 -0.02621 0.06362  -0.22802 56  GLN B CD  
1192 O OE1 . GLN B 36  ? 0.63999 0.90001 0.37262 -0.04682 0.07318  -0.22430 56  GLN B OE1 
1193 N NE2 . GLN B 36  ? 0.69574 0.99246 0.39583 -0.02234 0.06681  -0.23119 56  GLN B NE2 
1194 N N   . GLY B 37  ? 0.86084 1.00934 0.29395 -0.07707 0.10449  0.09024  57  GLY B N   
1195 C CA  . GLY B 37  ? 0.92799 1.05270 0.32279 -0.06111 0.11527  0.14182  57  GLY B CA  
1196 C C   . GLY B 37  ? 0.89652 1.00280 0.31211 -0.05019 0.08941  0.16098  57  GLY B C   
1197 O O   . GLY B 37  ? 0.93843 1.03662 0.32799 -0.03600 0.07551  0.18761  57  GLY B O   
1198 N N   . LYS B 38  ? 0.83012 0.93018 0.28996 -0.05806 0.08155  0.14664  58  LYS B N   
1199 C CA  . LYS B 38  ? 0.82261 0.90339 0.29949 -0.04426 0.05983  0.16190  58  LYS B CA  
1200 C C   . LYS B 38  ? 0.80943 0.86253 0.31884 -0.05597 0.07431  0.17605  58  LYS B C   
1201 O O   . LYS B 38  ? 0.80553 0.83713 0.35420 -0.07419 0.09601  0.15618  58  LYS B O   
1202 C CB  . LYS B 38  ? 0.79533 0.88607 0.29439 -0.03657 0.02586  0.12418  58  LYS B CB  
1203 C CG  . LYS B 38  ? 0.77452 0.89288 0.26827 -0.03577 0.01061  0.10099  58  LYS B CG  
1204 C CD  . LYS B 38  ? 0.83446 0.96420 0.37112 -0.03606 -0.01292 0.06821  58  LYS B CD  
1205 C CE  . LYS B 38  ? 0.85881 0.98912 0.40362 -0.01980 -0.03377 0.08188  58  LYS B CE  
1206 N NZ  . LYS B 38  ? 0.81380 0.96681 0.39954 -0.02216 -0.05169 0.05717  58  LYS B NZ  
1207 N N   . GLU B 39  ? 0.81086 0.83245 0.34563 -0.03411 0.05762  0.19039  59  GLU B N   
1208 C CA  . GLU B 39  ? 0.81422 0.77260 0.41931 -0.02898 0.05587  0.17347  59  GLU B CA  
1209 C C   . GLU B 39  ? 0.81889 0.76626 0.43423 -0.02610 0.02795  0.12188  59  GLU B C   
1210 O O   . GLU B 39  ? 0.80173 0.78677 0.37910 -0.02031 0.01063  0.11327  59  GLU B O   
1211 C CB  . GLU B 39  ? 0.81867 0.74495 0.44838 -0.00342 0.05292  0.21237  59  GLU B CB  
1212 C CG  . GLU B 39  ? 0.85639 0.75407 0.53334 -0.00775 0.08258  0.25286  59  GLU B CG  
1213 C CD  . GLU B 39  ? 0.87287 0.72720 0.62463 -0.02511 0.09466  0.22138  59  GLU B CD  
1214 O OE1 . GLU B 39  ? 0.85622 0.67243 0.64669 -0.01994 0.06875  0.17389  59  GLU B OE1 
1215 O OE2 . GLU B 39  ? 0.87572 0.73416 0.64807 -0.04222 0.13020  0.24503  59  GLU B OE2 
1216 N N   . MET B 40  ? 0.82536 0.72014 0.49725 -0.02893 0.02259  0.08977  60  MET B N   
1217 C CA  . MET B 40  ? 0.83104 0.71311 0.50729 -0.02723 -0.00340 0.04157  60  MET B CA  
1218 C C   . MET B 40  ? 0.85999 0.73878 0.50579 0.00448  -0.02469 0.04272  60  MET B C   
1219 O O   . MET B 40  ? 0.88128 0.78288 0.50105 0.00784  -0.03887 0.02313  60  MET B O   
1220 C CB  . MET B 40  ? 0.78695 0.60879 0.53131 -0.03374 -0.01077 0.00785  60  MET B CB  
1221 C CG  . MET B 40  ? 0.82967 0.61416 0.57490 -0.01440 -0.04565 -0.03254 60  MET B CG  
1222 S SD  . MET B 40  ? 0.83392 0.53950 0.66592 -0.01576 -0.06558 -0.07202 60  MET B SD  
1223 C CE  . MET B 40  ? 0.81851 0.49980 0.71162 -0.01424 -0.03917 -0.02968 60  MET B CE  
1224 N N   . ASP B 41  ? 0.85082 0.70268 0.50575 0.02904  -0.02418 0.06773  61  ASP B N   
1225 C CA  . ASP B 41  ? 0.85646 0.70240 0.48696 0.06272  -0.03887 0.06732  61  ASP B CA  
1226 C C   . ASP B 41  ? 0.83966 0.74891 0.42545 0.06644  -0.03673 0.09130  61  ASP B C   
1227 O O   . ASP B 41  ? 0.77778 0.69167 0.34566 0.09184  -0.04443 0.08849  61  ASP B O   
1228 C CB  . ASP B 41  ? 0.85501 0.66035 0.51686 0.08742  -0.03772 0.08816  61  ASP B CB  
1229 C CG  . ASP B 41  ? 0.92430 0.66111 0.64498 0.09054  -0.04876 0.05679  61  ASP B CG  
1230 O OD1 . ASP B 41  ? 0.91945 0.62223 0.63366 0.10597  -0.07146 0.01183  61  ASP B OD1 
1231 O OD2 . ASP B 41  ? 0.92694 0.64362 0.70319 0.07906  -0.03596 0.07838  61  ASP B OD2 
1232 N N   . SER B 42  ? 0.81566 0.77335 0.38563 0.04396  -0.02671 0.11376  62  SER B N   
1233 C CA  . SER B 42  ? 0.76688 0.77962 0.32039 0.03990  -0.03260 0.12485  62  SER B CA  
1234 C C   . SER B 42  ? 0.77899 0.80248 0.34830 0.02332  -0.04138 0.08704  62  SER B C   
1235 O O   . SER B 42  ? 0.78140 0.82436 0.36919 0.02233  -0.04621 0.08669  62  SER B O   
1236 C CB  . SER B 42  ? 0.74937 0.78268 0.29535 0.02189  -0.02443 0.14378  62  SER B CB  
1237 O OG  . SER B 42  ? 0.79225 0.82542 0.33938 0.03673  -0.02412 0.18219  62  SER B OG  
1238 N N   . LEU B 43  ? 0.76891 0.77861 0.33578 0.01614  -0.04444 0.05756  63  LEU B N   
1239 C CA  . LEU B 43  ? 0.73702 0.74718 0.32583 0.00399  -0.05191 0.02727  63  LEU B CA  
1240 C C   . LEU B 43  ? 0.75399 0.75693 0.35807 0.01354  -0.06016 0.00816  63  LEU B C   
1241 O O   . LEU B 43  ? 0.79472 0.73848 0.37392 0.03405  -0.06824 -0.00771 63  LEU B O   
1242 C CB  . LEU B 43  ? 0.72484 0.75668 0.33341 -0.01701 -0.04691 0.00450  63  LEU B CB  
1243 C CG  . LEU B 43  ? 0.73085 0.79333 0.33578 -0.03071 -0.03375 0.01932  63  LEU B CG  
1244 C CD1 . LEU B 43  ? 0.73847 0.80756 0.34677 -0.06316 -0.02122 -0.00053 63  LEU B CD1 
1245 C CD2 . LEU B 43  ? 0.74311 0.83370 0.37144 -0.02762 -0.04195 0.01769  63  LEU B CD2 
1246 N N   . ARG B 44  ? 0.76573 0.77945 0.39112 0.00946  -0.06216 0.00730  64  ARG B N   
1247 C CA  . ARG B 44  ? 0.74383 0.74661 0.38002 0.02387  -0.06647 -0.00881 64  ARG B CA  
1248 C C   . ARG B 44  ? 0.69233 0.70092 0.35546 -0.00219 -0.07352 -0.03439 64  ARG B C   
1249 O O   . ARG B 44  ? 0.70172 0.69216 0.37463 -0.01371 -0.07666 -0.03292 64  ARG B O   
1250 C CB  . ARG B 44  ? 0.76326 0.78210 0.40684 0.03759  -0.06046 0.00974  64  ARG B CB  
1251 C CG  . ARG B 44  ? 0.87160 0.88083 0.49574 0.07564  -0.05154 0.02487  64  ARG B CG  
1252 C CD  . ARG B 44  ? 0.84879 0.88830 0.48836 0.08883  -0.04103 0.04561  64  ARG B CD  
1253 N NE  . ARG B 44  ? 0.88855 0.91708 0.51869 0.11062  -0.03572 0.04033  64  ARG B NE  
1254 C CZ  . ARG B 44  ? 0.98921 0.99322 0.58946 0.14982  -0.02632 0.03981  64  ARG B CZ  
1255 N NH1 . ARG B 44  ? 1.01061 0.99722 0.59044 0.17331  -0.02193 0.04367  64  ARG B NH1 
1256 N NH2 . ARG B 44  ? 0.99665 0.99046 0.58181 0.16947  -0.02138 0.03594  64  ARG B NH2 
1257 N N   . PHE B 45  ? 0.68979 0.65918 0.35611 0.01024  -0.08395 -0.05967 65  PHE B N   
1258 C CA  . PHE B 45  ? 0.69978 0.67134 0.40667 -0.01068 -0.09056 -0.08406 65  PHE B CA  
1259 C C   . PHE B 45  ? 0.75351 0.70723 0.45960 0.00509  -0.09784 -0.08426 65  PHE B C   
1260 O O   . PHE B 45  ? 0.80387 0.71158 0.48183 0.03475  -0.10681 -0.08891 65  PHE B O   
1261 C CB  . PHE B 45  ? 0.68313 0.60701 0.40349 -0.01826 -0.09980 -0.11012 65  PHE B CB  
1262 C CG  . PHE B 45  ? 0.64397 0.57338 0.35146 -0.03369 -0.09299 -0.10897 65  PHE B CG  
1263 C CD1 . PHE B 45  ? 0.64750 0.60508 0.39246 -0.05430 -0.08703 -0.11778 65  PHE B CD1 
1264 C CD2 . PHE B 45  ? 0.68391 0.57512 0.33294 -0.02152 -0.09205 -0.09193 65  PHE B CD2 
1265 C CE1 . PHE B 45  ? 0.62692 0.59241 0.34676 -0.08081 -0.06903 -0.10869 65  PHE B CE1 
1266 C CE2 . PHE B 45  ? 0.69408 0.60807 0.35283 -0.04001 -0.06899 -0.07212 65  PHE B CE2 
1267 C CZ  . PHE B 45  ? 0.65774 0.60778 0.33653 -0.07240 -0.05765 -0.08266 65  PHE B CZ  
1268 N N   . LEU B 46  ? 0.72608 0.71331 0.45779 -0.01158 -0.09622 -0.08030 66  LEU B N   
1269 C CA  . LEU B 46  ? 0.73900 0.71521 0.45901 0.00621  -0.10327 -0.07385 66  LEU B CA  
1270 C C   . LEU B 46  ? 0.73057 0.70548 0.49040 -0.01118 -0.11261 -0.09003 66  LEU B C   
1271 O O   . LEU B 46  ? 0.69235 0.70141 0.49506 -0.04166 -0.10555 -0.09525 66  LEU B O   
1272 C CB  . LEU B 46  ? 0.75014 0.75852 0.45817 0.00969  -0.09581 -0.04524 66  LEU B CB  
1273 C CG  . LEU B 46  ? 0.75003 0.76695 0.43770 0.02107  -0.08283 -0.02414 66  LEU B CG  
1274 C CD1 . LEU B 46  ? 0.69975 0.74381 0.39355 0.03165  -0.07712 0.00098  66  LEU B CD1 
1275 C CD2 . LEU B 46  ? 0.81346 0.80074 0.46644 0.05650  -0.07708 -0.02469 66  LEU B CD2 
1276 N N   . TYR B 47  ? 1.22195 0.41623 0.35510 0.04753  0.17394  0.03546  67  TYR B N   
1277 C CA  . TYR B 47  ? 1.26774 0.43314 0.35866 0.08179  0.16552  0.03222  67  TYR B CA  
1278 C C   . TYR B 47  ? 1.34072 0.46044 0.38790 0.10168  0.19082  0.03918  67  TYR B C   
1279 O O   . TYR B 47  ? 1.37215 0.49074 0.40200 0.11224  0.19892  0.03661  67  TYR B O   
1280 C CB  . TYR B 47  ? 1.26287 0.44952 0.34141 0.11184  0.12710  0.02152  67  TYR B CB  
1281 C CG  . TYR B 47  ? 1.31724 0.46974 0.35335 0.14602  0.11753  0.02262  67  TYR B CG  
1282 C CD1 . TYR B 47  ? 1.33409 0.46057 0.36009 0.14310  0.12651  0.02583  67  TYR B CD1 
1283 C CD2 . TYR B 47  ? 1.36543 0.50338 0.36271 0.18052  0.09956  0.01986  67  TYR B CD2 
1284 C CE1 . TYR B 47  ? 1.40129 0.47962 0.37622 0.17778  0.11843  0.02795  67  TYR B CE1 
1285 C CE2 . TYR B 47  ? 1.42652 0.52513 0.37803 0.21010  0.08887  0.02405  67  TYR B CE2 
1286 C CZ  . TYR B 47  ? 1.44578 0.51113 0.38509 0.21073  0.09845  0.02871  67  TYR B CZ  
1287 O OH  . TYR B 47  ? 1.52114 0.53499 0.40544 0.24403  0.08689  0.03312  67  TYR B OH  
1288 N N   . ASP B 48  ? 1.38381 0.46676 0.40703 0.10546  0.20369  0.04716  68  ASP B N   
1289 C CA  . ASP B 48  ? 1.45661 0.50490 0.43951 0.11559  0.22775  0.05979  68  ASP B CA  
1290 C C   . ASP B 48  ? 1.44614 0.51221 0.45745 0.09342  0.25856  0.06504  68  ASP B C   
1291 O O   . ASP B 48  ? 1.50038 0.55829 0.47814 0.10450  0.27671  0.07028  68  ASP B O   
1292 C CB  . ASP B 48  ? 1.52125 0.55256 0.44433 0.15039  0.21238  0.06074  68  ASP B CB  
1293 N N   . GLY B 49  ? 1.38021 0.47648 0.45434 0.05996  0.26455  0.06392  69  GLY B N   
1294 C CA  . GLY B 49  ? 1.35882 0.47892 0.47957 0.03499  0.29149  0.07085  69  GLY B CA  
1295 C C   . GLY B 49  ? 1.36555 0.48636 0.47709 0.04371  0.30164  0.06269  69  GLY B C   
1296 O O   . GLY B 49  ? 1.37569 0.50074 0.51193 0.03160  0.33570  0.06802  69  GLY B O   
1297 N N   . ILE B 50  ? 1.36410 0.48332 0.44414 0.06529  0.27365  0.04874  70  ILE B N   
1298 C CA  . ILE B 50  ? 1.37908 0.50176 0.44252 0.07857  0.27765  0.03179  70  ILE B CA  
1299 C C   . ILE B 50  ? 1.34744 0.49324 0.44167 0.06332  0.24740  0.02455  70  ILE B C   
1300 O O   . ILE B 50  ? 1.28012 0.44470 0.37957 0.06528  0.20789  0.02541  70  ILE B O   
1301 C CB  . ILE B 50  ? 1.44001 0.56046 0.44407 0.11800  0.25965  0.01653  70  ILE B CB  
1302 C CG1 . ILE B 50  ? 1.51682 0.61890 0.48031 0.12350  0.29401  0.02862  70  ILE B CG1 
1303 C CG2 . ILE B 50  ? 1.44326 0.58616 0.45124 0.13373  0.24859  -0.01909 70  ILE B CG2 
1304 C CD1 . ILE B 50  ? 1.57900 0.67049 0.47988 0.14892  0.27153  0.03202  70  ILE B CD1 
1305 N N   . ARG B 51  ? 1.35488 0.54161 0.55392 0.04408  0.24447  0.01469  71  ARG B N   
1306 C CA  . ARG B 51  ? 1.25928 0.50926 0.57349 0.01743  0.19152  0.01474  71  ARG B CA  
1307 C C   . ARG B 51  ? 1.25769 0.52456 0.54883 0.05006  0.14179  -0.01193 71  ARG B C   
1308 O O   . ARG B 51  ? 1.32636 0.56293 0.54159 0.09238  0.14599  -0.04028 71  ARG B O   
1309 C CB  . ARG B 51  ? 1.21142 0.50094 0.66485 -0.00791 0.19195  0.01187  71  ARG B CB  
1310 C CG  . ARG B 51  ? 1.13325 0.48706 0.71853 -0.06033 0.14534  0.03909  71  ARG B CG  
1311 C CD  . ARG B 51  ? 1.06573 0.46569 0.79617 -0.06750 0.11218  0.02440  71  ARG B CD  
1312 N NE  . ARG B 51  ? 1.01381 0.47534 0.88346 -0.12842 0.07164  0.06392  71  ARG B NE  
1313 C CZ  . ARG B 51  ? 0.97495 0.45366 0.96481 -0.16555 0.08196  0.08694  71  ARG B CZ  
1314 N NH1 . ARG B 51  ? 0.99205 0.43486 0.98709 -0.14614 0.13690  0.07127  71  ARG B NH1 
1315 N NH2 . ARG B 51  ? 0.91299 0.46749 1.00142 -0.21663 0.03856  0.11904  71  ARG B NH2 
1316 N N   . ILE B 52  ? 1.19624 0.51646 0.55314 0.02612  0.09305  -0.00030 72  ILE B N   
1317 C CA  . ILE B 52  ? 1.17364 0.51908 0.52165 0.05044  0.04103  -0.01638 72  ILE B CA  
1318 C C   . ILE B 52  ? 1.10820 0.51950 0.59634 0.02773  -0.00954 -0.01918 72  ILE B C   
1319 O O   . ILE B 52  ? 1.03857 0.50127 0.63059 -0.02284 -0.02439 0.00933  72  ILE B O   
1320 C CB  . ILE B 52  ? 1.19247 0.55419 0.50273 0.04243  0.02582  0.00069  72  ILE B CB  
1321 C CG1 . ILE B 52  ? 1.22562 0.51659 0.41418 0.06569  0.06972  0.00413  72  ILE B CG1 
1322 C CG2 . ILE B 52  ? 1.20363 0.60021 0.52026 0.06588  -0.02857 -0.01176 72  ILE B CG2 
1323 C CD1 . ILE B 52  ? 1.22248 0.51873 0.36874 0.08521  0.04901  0.00271  72  ILE B CD1 
1324 N N   . GLN B 53  ? 1.14193 0.55116 0.63576 0.06189  -0.04039 -0.05126 73  GLN B N   
1325 C CA  . GLN B 53  ? 1.04224 0.51305 0.67143 0.04391  -0.10260 -0.05221 73  GLN B CA  
1326 C C   . GLN B 53  ? 1.00084 0.52746 0.64502 0.02818  -0.15289 -0.02703 73  GLN B C   
1327 O O   . GLN B 53  ? 1.01934 0.52621 0.56014 0.05357  -0.14730 -0.02866 73  GLN B O   
1328 C CB  . GLN B 53  ? 1.01536 0.46202 0.64413 0.08623  -0.12233 -0.10025 73  GLN B CB  
1329 N N   . ALA B 54  ? 0.91220 0.51403 0.69458 -0.01602 -0.20322 -0.00100 74  ALA B N   
1330 C CA  . ALA B 54  ? 0.82827 0.50078 0.63400 -0.04076 -0.24684 0.02824  74  ALA B CA  
1331 C C   . ALA B 54  ? 0.89928 0.56775 0.66028 0.00447  -0.28511 0.00739  74  ALA B C   
1332 O O   . ALA B 54  ? 0.89690 0.59434 0.61277 0.00766  -0.29427 0.01944  74  ALA B O   
1333 C CB  . ALA B 54  ? 0.72159 0.48093 0.68973 -0.10220 -0.29936 0.06705  74  ALA B CB  
1334 N N   . ASP B 55  ? 0.91690 0.55063 0.69288 0.03953  -0.30776 -0.02653 75  ASP B N   
1335 C CA  . ASP B 55  ? 0.94466 0.57580 0.69098 0.07743  -0.35506 -0.04409 75  ASP B CA  
1336 C C   . ASP B 55  ? 1.01963 0.59310 0.60760 0.12264  -0.32299 -0.05845 75  ASP B C   
1337 O O   . ASP B 55  ? 1.03444 0.61683 0.59728 0.14745  -0.36319 -0.06013 75  ASP B O   
1338 C CB  . ASP B 55  ? 0.97975 0.58072 0.77467 0.10229  -0.38533 -0.08485 75  ASP B CB  
1339 C CG  . ASP B 55  ? 1.08435 0.59650 0.74949 0.14867  -0.33279 -0.13222 75  ASP B CG  
1340 O OD1 . ASP B 55  ? 1.10327 0.58510 0.73832 0.14149  -0.27016 -0.13551 75  ASP B OD1 
1341 O OD2 . ASP B 55  ? 1.15199 0.62832 0.74424 0.18889  -0.35570 -0.16313 75  ASP B OD2 
1342 N N   . GLN B 56  ? 1.09397 0.60954 0.58436 0.13221  -0.25642 -0.06415 76  GLN B N   
1343 C CA  . GLN B 56  ? 1.14287 0.59859 0.49248 0.17348  -0.23082 -0.07273 76  GLN B CA  
1344 C C   . GLN B 56  ? 1.13591 0.62905 0.47557 0.16685  -0.23732 -0.04672 76  GLN B C   
1345 O O   . GLN B 56  ? 1.06337 0.62021 0.47439 0.12466  -0.23699 -0.02324 76  GLN B O   
1346 C CB  . GLN B 56  ? 1.19987 0.58654 0.45921 0.18102  -0.16088 -0.07988 76  GLN B CB  
1347 C CG  . GLN B 56  ? 1.20510 0.57820 0.50869 0.17183  -0.13838 -0.10108 76  GLN B CG  
1348 C CD  . GLN B 56  ? 1.22328 0.53115 0.42715 0.18353  -0.06913 -0.10727 76  GLN B CD  
1349 O OE1 . GLN B 56  ? 1.19438 0.50292 0.42431 0.15432  -0.02776 -0.08762 76  GLN B OE1 
1350 N NE2 . GLN B 56  ? 1.30888 0.57640 0.41676 0.21901  -0.05841 -0.12519 76  GLN B NE2 
1351 N N   . THR B 57  ? 1.16851 0.64023 0.45893 0.20074  -0.23080 -0.05117 77  THR B N   
1352 C CA  . THR B 57  ? 1.13993 0.65156 0.44986 0.19976  -0.22443 -0.03672 77  THR B CA  
1353 C C   . THR B 57  ? 1.19640 0.64209 0.42393 0.22285  -0.17746 -0.03705 77  THR B C   
1354 O O   . THR B 57  ? 1.23428 0.61609 0.40114 0.24048  -0.15522 -0.04336 77  THR B O   
1355 C CB  . THR B 57  ? 1.10060 0.65470 0.46368 0.21407  -0.26562 -0.03822 77  THR B CB  
1356 O OG1 . THR B 57  ? 1.17103 0.65897 0.46511 0.25245  -0.26255 -0.05144 77  THR B OG1 
1357 C CG2 . THR B 57  ? 1.05953 0.66480 0.51401 0.19329  -0.31016 -0.03885 77  THR B CG2 
1358 N N   . PRO B 58  ? 1.16605 0.62869 0.39441 0.22167  -0.16328 -0.02918 78  PRO B N   
1359 C CA  . PRO B 58  ? 1.23818 0.63216 0.39952 0.24435  -0.12742 -0.02747 78  PRO B CA  
1360 C C   . PRO B 58  ? 1.32491 0.66600 0.43926 0.28220  -0.14075 -0.02990 78  PRO B C   
1361 O O   . PRO B 58  ? 1.39369 0.66993 0.44763 0.29390  -0.11350 -0.02426 78  PRO B O   
1362 C CB  . PRO B 58  ? 1.21691 0.64335 0.39068 0.24429  -0.12555 -0.02662 78  PRO B CB  
1363 C CG  . PRO B 58  ? 1.12738 0.64171 0.36570 0.20258  -0.13886 -0.02412 78  PRO B CG  
1364 C CD  . PRO B 58  ? 1.10670 0.65136 0.39334 0.19625  -0.17770 -0.02150 78  PRO B CD  
1365 N N   . GLU B 59  ? 1.25703 0.62811 0.40056 0.29601  -0.18335 -0.03558 79  GLU B N   
1366 C CA  . GLU B 59  ? 1.32471 0.64925 0.42040 0.32343  -0.19894 -0.03836 79  GLU B CA  
1367 C C   . GLU B 59  ? 1.36876 0.65449 0.41872 0.32174  -0.18650 -0.04494 79  GLU B C   
1368 O O   . GLU B 59  ? 1.45216 0.68640 0.43427 0.33688  -0.17824 -0.04117 79  GLU B O   
1369 C CB  . GLU B 59  ? 1.30483 0.67650 0.45302 0.32992  -0.24660 -0.04262 79  GLU B CB  
1370 C CG  . GLU B 59  ? 1.39734 0.72771 0.49867 0.35467  -0.26629 -0.04020 79  GLU B CG  
1371 C CD  . GLU B 59  ? 1.46644 0.81577 0.59126 0.35356  -0.30589 -0.04986 79  GLU B CD  
1372 O OE1 . GLU B 59  ? 1.53057 0.83049 0.58844 0.36523  -0.31229 -0.05404 79  GLU B OE1 
1373 O OE2 . GLU B 59  ? 1.41503 0.83059 0.62480 0.33836  -0.33069 -0.05123 79  GLU B OE2 
1374 N N   . ASP B 60  ? 1.33905 0.65167 0.42272 0.30244  -0.18703 -0.05415 80  ASP B N   
1375 C CA  . ASP B 60  ? 1.36668 0.64843 0.40852 0.30279  -0.17369 -0.06566 80  ASP B CA  
1376 C C   . ASP B 60  ? 1.40599 0.64803 0.39736 0.29385  -0.11854 -0.05420 80  ASP B C   
1377 O O   . ASP B 60  ? 1.46027 0.68013 0.40782 0.29461  -0.09926 -0.06268 80  ASP B O   
1378 C CB  . ASP B 60  ? 1.31076 0.62794 0.40704 0.28594  -0.19392 -0.08206 80  ASP B CB  
1379 C CG  . ASP B 60  ? 1.27201 0.63373 0.43523 0.28941  -0.25383 -0.09085 80  ASP B CG  
1380 O OD1 . ASP B 60  ? 1.31101 0.66467 0.46050 0.30885  -0.27606 -0.09249 80  ASP B OD1 
1381 O OD2 . ASP B 60  ? 1.20264 0.61124 0.44165 0.26725  -0.28068 -0.09277 80  ASP B OD2 
1382 N N   . LEU B 61  ? 1.41086 0.64781 0.41079 0.28343  -0.09247 -0.03750 81  LEU B N   
1383 C CA  . LEU B 61  ? 1.43933 0.63965 0.40529 0.27104  -0.04342 -0.02461 81  LEU B CA  
1384 C C   . LEU B 61  ? 1.47225 0.62597 0.39139 0.28691  -0.03357 -0.00896 81  LEU B C   
1385 O O   . LEU B 61  ? 1.49459 0.61643 0.39358 0.27584  0.00259  0.00377  81  LEU B O   
1386 C CB  . LEU B 61  ? 1.36976 0.59456 0.38415 0.23905  -0.01979 -0.02058 81  LEU B CB  
1387 C CG  . LEU B 61  ? 1.34569 0.58485 0.37875 0.21920  -0.00833 -0.03169 81  LEU B CG  
1388 C CD1 . LEU B 61  ? 1.27712 0.55645 0.36658 0.18865  -0.01741 -0.03165 81  LEU B CD1 
1389 C CD2 . LEU B 61  ? 1.36176 0.56464 0.36154 0.20913  0.04182  -0.02354 81  LEU B CD2 
1390 N N   . ASP B 62  ? 1.17989 0.82038 0.54516 0.25180  -0.24010 -0.04697 82  ASP B N   
1391 C CA  . ASP B 62  ? 1.22093 0.83253 0.55420 0.26376  -0.24054 -0.04210 82  ASP B CA  
1392 C C   . ASP B 62  ? 1.19822 0.81216 0.53786 0.25081  -0.22626 -0.03056 82  ASP B C   
1393 O O   . ASP B 62  ? 1.24155 0.81921 0.53936 0.25499  -0.21753 -0.02120 82  ASP B O   
1394 C CB  . ASP B 62  ? 1.28906 0.86088 0.55875 0.27724  -0.23067 -0.03648 82  ASP B CB  
1395 C CG  . ASP B 62  ? 1.34854 0.88322 0.58261 0.29710  -0.24402 -0.03763 82  ASP B CG  
1396 O OD1 . ASP B 62  ? 1.36466 0.89908 0.60832 0.31241  -0.27001 -0.05144 82  ASP B OD1 
1397 O OD2 . ASP B 62  ? 1.38534 0.88915 0.58022 0.29632  -0.23074 -0.02402 82  ASP B OD2 
1398 N N   . MET B 63  ? 1.16728 0.81792 0.55381 0.23508  -0.22548 -0.03098 83  MET B N   
1399 C CA  . MET B 63  ? 1.10093 0.74988 0.48870 0.22337  -0.21301 -0.02201 83  MET B CA  
1400 C C   . MET B 63  ? 1.10091 0.73328 0.48034 0.24311  -0.22464 -0.02633 83  MET B C   
1401 O O   . MET B 63  ? 1.10952 0.75136 0.50043 0.26207  -0.24412 -0.03591 83  MET B O   
1402 C CB  . MET B 63  ? 1.05511 0.74776 0.49023 0.20280  -0.20943 -0.02136 83  MET B CB  
1403 C CG  . MET B 63  ? 1.04900 0.75925 0.49403 0.18905  -0.20187 -0.01945 83  MET B CG  
1404 S SD  . MET B 63  ? 0.97666 0.71200 0.44151 0.16070  -0.18586 -0.00856 83  MET B SD  
1405 C CE  . MET B 63  ? 0.88937 0.66856 0.41249 0.15353  -0.20120 -0.01601 83  MET B CE  
1406 N N   . GLU B 64  ? 1.10499 0.71053 0.46133 0.23979  -0.21452 -0.01958 84  GLU B N   
1407 C CA  . GLU B 64  ? 1.09456 0.67559 0.43281 0.26418  -0.22414 -0.02481 84  GLU B CA  
1408 C C   . GLU B 64  ? 1.04896 0.64255 0.40123 0.25767  -0.21779 -0.02470 84  GLU B C   
1409 O O   . GLU B 64  ? 1.03427 0.64427 0.40168 0.23008  -0.20523 -0.01819 84  GLU B O   
1410 C CB  . GLU B 64  ? 1.12966 0.63843 0.40162 0.27447  -0.22194 -0.01856 84  GLU B CB  
1411 N N   . ASP B 65  ? 1.08317 0.67056 0.42755 0.28681  -0.22746 -0.03281 85  ASP B N   
1412 C CA  . ASP B 65  ? 1.04701 0.64043 0.39246 0.28934  -0.22171 -0.03486 85  ASP B CA  
1413 C C   . ASP B 65  ? 1.08070 0.61155 0.37927 0.26781  -0.20886 -0.02685 85  ASP B C   
1414 O O   . ASP B 65  ? 1.13890 0.60592 0.38835 0.26660  -0.20881 -0.02126 85  ASP B O   
1415 C CB  . ASP B 65  ? 1.09041 0.68152 0.42252 0.33489  -0.23381 -0.04602 85  ASP B CB  
1416 C CG  . ASP B 65  ? 1.04100 0.72202 0.43588 0.34763  -0.24300 -0.05028 85  ASP B CG  
1417 O OD1 . ASP B 65  ? 0.98222 0.71291 0.41694 0.32198  -0.23635 -0.04522 85  ASP B OD1 
1418 O OD2 . ASP B 65  ? 1.06418 0.76929 0.47081 0.38137  -0.25821 -0.05679 85  ASP B OD2 
1419 N N   . ASN B 66  ? 1.04861 0.59882 0.36181 0.24737  -0.19978 -0.02492 86  ASN B N   
1420 C CA  . ASN B 66  ? 1.07643 0.57718 0.35348 0.22044  -0.19124 -0.01769 86  ASN B CA  
1421 C C   . ASN B 66  ? 1.05553 0.55970 0.33865 0.18223  -0.18245 -0.00319 86  ASN B C   
1422 O O   . ASN B 66  ? 1.08935 0.55067 0.33914 0.15664  -0.17854 0.00607  86  ASN B O   
1423 C CB  . ASN B 66  ? 1.17410 0.58126 0.37790 0.24005  -0.19830 -0.02082 86  ASN B CB  
1424 C CG  . ASN B 66  ? 1.21760 0.61085 0.40085 0.27376  -0.20279 -0.03500 86  ASN B CG  
1425 O OD1 . ASN B 66  ? 1.22549 0.66717 0.43423 0.30995  -0.20697 -0.04497 86  ASN B OD1 
1426 N ND2 . ASN B 66  ? 1.29698 0.62478 0.43073 0.26342  -0.20315 -0.03595 86  ASN B ND2 
1427 N N   . ASP B 67  ? 1.03137 0.58368 0.35167 0.17913  -0.18087 -0.00101 87  ASP B N   
1428 C CA  . ASP B 67  ? 1.02635 0.59147 0.35105 0.15082  -0.17079 0.01175  87  ASP B CA  
1429 C C   . ASP B 67  ? 0.96905 0.57125 0.32369 0.12229  -0.16418 0.01608  87  ASP B C   
1430 O O   . ASP B 67  ? 0.93067 0.56789 0.31840 0.12447  -0.16694 0.00835  87  ASP B O   
1431 C CB  . ASP B 67  ? 1.02381 0.62490 0.37351 0.16130  -0.17263 0.00899  87  ASP B CB  
1432 C CG  . ASP B 67  ? 1.04125 0.60082 0.34594 0.17107  -0.17157 0.01525  87  ASP B CG  
1433 O OD1 . ASP B 67  ? 1.08123 0.58894 0.33842 0.16135  -0.16682 0.02660  87  ASP B OD1 
1434 O OD2 . ASP B 67  ? 1.08677 0.66109 0.39925 0.18707  -0.17701 0.00944  87  ASP B OD2 
1435 N N   . ILE B 68  ? 0.95503 0.55169 0.29554 0.09539  -0.15598 0.03054  88  ILE B N   
1436 C CA  . ILE B 68  ? 0.92392 0.54823 0.28471 0.06708  -0.15264 0.03685  88  ILE B CA  
1437 C C   . ILE B 68  ? 0.87515 0.55741 0.27220 0.06197  -0.14718 0.04132  88  ILE B C   
1438 O O   . ILE B 68  ? 0.89083 0.57542 0.27456 0.06856  -0.14118 0.04755  88  ILE B O   
1439 C CB  . ILE B 68  ? 0.98250 0.55642 0.29777 0.03796  -0.15202 0.05207  88  ILE B CB  
1440 C CG1 . ILE B 68  ? 1.03272 0.54409 0.31140 0.04175  -0.16200 0.04295  88  ILE B CG1 
1441 C CG2 . ILE B 68  ? 0.98049 0.59206 0.31779 0.00573  -0.14970 0.06413  88  ILE B CG2 
1442 C CD1 . ILE B 68  ? 1.11609 0.55217 0.33524 0.01335  -0.16801 0.05699  88  ILE B CD1 
1443 N N   . ILE B 69  ? 0.84486 0.56984 0.28199 0.05316  -0.14979 0.03783  89  ILE B N   
1444 C CA  . ILE B 69  ? 0.85412 0.62524 0.31952 0.04838  -0.14794 0.04218  89  ILE B CA  
1445 C C   . ILE B 69  ? 0.85513 0.63768 0.32277 0.01983  -0.14800 0.05449  89  ILE B C   
1446 O O   . ILE B 69  ? 0.80456 0.59269 0.28936 0.00947  -0.15391 0.05008  89  ILE B O   
1447 C CB  . ILE B 69  ? 0.77302 0.57884 0.28252 0.06156  -0.15614 0.02954  89  ILE B CB  
1448 C CG1 . ILE B 69  ? 0.78273 0.57368 0.29068 0.08489  -0.16179 0.01805  89  ILE B CG1 
1449 C CG2 . ILE B 69  ? 0.81208 0.64782 0.33827 0.06484  -0.15723 0.03127  89  ILE B CG2 
1450 C CD1 . ILE B 69  ? 0.74137 0.56181 0.28819 0.09385  -0.17341 0.00896  89  ILE B CD1 
1451 N N   . GLU B 70  ? 0.88883 0.67663 0.33703 0.00620  -0.14167 0.07191  90  GLU B N   
1452 C CA  . GLU B 70  ? 0.88278 0.68545 0.33545 -0.02724 -0.14550 0.08813  90  GLU B CA  
1453 C C   . GLU B 70  ? 0.86872 0.72458 0.36519 -0.02401 -0.15284 0.08561  90  GLU B C   
1454 O O   . GLU B 70  ? 0.87002 0.74863 0.37879 0.00235  -0.15189 0.07839  90  GLU B O   
1455 C CB  . GLU B 70  ? 0.88901 0.69236 0.31380 -0.04925 -0.13411 0.11467  90  GLU B CB  
1456 C CG  . GLU B 70  ? 0.97953 0.71884 0.35445 -0.06312 -0.13125 0.12371  90  GLU B CG  
1457 C CD  . GLU B 70  ? 1.10629 0.85618 0.46222 -0.08109 -0.11247 0.15265  90  GLU B CD  
1458 O OE1 . GLU B 70  ? 1.00896 0.81953 0.39323 -0.06433 -0.09471 0.15708  90  GLU B OE1 
1459 O OE2 . GLU B 70  ? 1.22752 0.92697 0.54490 -0.11040 -0.11356 0.17044  90  GLU B OE2 
1460 N N   . ALA B 71  ? 0.85262 0.72268 0.37030 -0.05041 -0.16295 0.09091  91  ALA B N   
1461 C CA  . ALA B 71  ? 0.79199 0.71095 0.35646 -0.04953 -0.17156 0.09047  91  ALA B CA  
1462 C C   . ALA B 71  ? 0.80101 0.76266 0.39955 -0.07896 -0.17040 0.10920  91  ALA B C   
1463 O O   . ALA B 71  ? 0.79966 0.74068 0.38372 -0.11189 -0.17685 0.11833  91  ALA B O   
1464 C CB  . ALA B 71  ? 0.74017 0.65146 0.32394 -0.04653 -0.17862 0.07557  91  ALA B CB  
1465 N N   . HIS B 72  ? 0.75845 0.77848 0.40178 -0.06574 -0.16473 0.11443  92  HIS B N   
1466 C CA  . HIS B 72  ? 0.73331 0.81326 0.42372 -0.08766 -0.16391 0.13334  92  HIS B CA  
1467 C C   . HIS B 72  ? 0.69522 0.81721 0.43049 -0.06917 -0.17597 0.12875  92  HIS B C   
1468 O O   . HIS B 72  ? 0.67724 0.77728 0.40396 -0.04262 -0.18359 0.11272  92  HIS B O   
1469 C CB  . HIS B 72  ? 0.70607 0.82691 0.40736 -0.08515 -0.13812 0.14998  92  HIS B CB  
1470 C CG  . HIS B 72  ? 0.76913 0.83878 0.41699 -0.09640 -0.12572 0.15532  92  HIS B CG  
1471 N ND1 . HIS B 72  ? 0.79491 0.85374 0.43429 -0.14023 -0.12528 0.17629  92  HIS B ND1 
1472 C CD2 . HIS B 72  ? 0.80621 0.82756 0.40378 -0.07004 -0.11705 0.14353  92  HIS B CD2 
1473 C CE1 . HIS B 72  ? 0.82909 0.83056 0.41198 -0.13902 -0.11555 0.17786  92  HIS B CE1 
1474 N NE2 . HIS B 72  ? 0.87168 0.85244 0.42905 -0.09517 -0.11020 0.15793  92  HIS B NE2 
1475 N N   . ARG B 73  ? 0.66496 0.84776 0.44984 -0.08394 -0.18002 0.14471  93  ARG B N   
1476 C CA  . ARG B 73  ? 0.66764 0.89023 0.49531 -0.06468 -0.19403 0.14312  93  ARG B CA  
1477 C C   . ARG B 73  ? 0.67987 0.95823 0.53907 -0.02676 -0.17513 0.14507  93  ARG B C   
1478 O O   . ARG B 73  ? 0.67397 1.00203 0.55288 -0.03288 -0.15335 0.16078  93  ARG B O   
1479 C CB  . ARG B 73  ? 0.64099 0.89896 0.50457 -0.09860 -0.21479 0.15854  93  ARG B CB  
1480 N N   . GLU B 74  ? 0.66312 0.93058 0.52314 0.01275  -0.18324 0.12982  94  GLU B N   
1481 C CA  . GLU B 74  ? 0.66542 0.98069 0.55013 0.05655  -0.16906 0.12805  94  GLU B CA  
1482 C C   . GLU B 74  ? 0.65359 1.05697 0.60460 0.05011  -0.16926 0.14841  94  GLU B C   
1483 O O   . GLU B 74  ? 0.64040 1.05326 0.61762 0.02548  -0.19434 0.15656  94  GLU B O   
1484 C CB  . GLU B 74  ? 0.65375 0.92641 0.52296 0.09684  -0.18722 0.10727  94  GLU B CB  
1485 C CG  . GLU B 74  ? 0.66275 0.94783 0.52265 0.15112  -0.17112 0.09490  94  GLU B CG  
1486 C CD  . GLU B 74  ? 0.75253 1.00124 0.55909 0.16056  -0.15053 0.08459  94  GLU B CD  
1487 O OE1 . GLU B 74  ? 0.75333 0.93359 0.52027 0.15086  -0.16456 0.07176  94  GLU B OE1 
1488 O OE2 . GLU B 74  ? 0.77210 1.06464 0.57684 0.17846  -0.12016 0.09100  94  GLU B OE2 
1489 N N   . GLN B 75  ? 0.62741 1.09996 0.60532 0.07337  -0.14092 0.15778  95  GLN B N   
1490 C CA  . GLN B 75  ? 0.62311 1.19964 0.67454 0.06520  -0.13545 0.18184  95  GLN B CA  
1491 C C   . GLN B 75  ? 0.61514 1.20676 0.68584 -0.00216 -0.14459 0.20444  95  GLN B C   
1492 O O   . GLN B 75  ? 0.60505 1.24154 0.72558 -0.02581 -0.16769 0.21824  95  GLN B O   
1493 C CB  . GLN B 75  ? 0.61671 1.22006 0.70917 0.09584  -0.16160 0.17748  95  GLN B CB  
1494 C CG  . GLN B 75  ? 0.63947 1.21440 0.70943 0.16421  -0.16168 0.15361  95  GLN B CG  
1495 C CD  . GLN B 75  ? 0.67011 1.28419 0.73080 0.21167  -0.12265 0.14865  95  GLN B CD  
1496 O OE1 . GLN B 75  ? 0.67313 1.33743 0.74190 0.19318  -0.09005 0.16533  95  GLN B OE1 
1497 N NE2 . GLN B 75  ? 0.70313 1.28850 0.74051 0.27421  -0.12712 0.12593  95  GLN B NE2 
1498 N N   . ILE B 76  ? 0.62872 1.17419 0.65373 -0.03236 -0.13045 0.20729  96  ILE B N   
1499 C CA  . ILE B 76  ? 0.63855 1.18079 0.66861 -0.09594 -0.14057 0.22706  96  ILE B CA  
1500 C C   . ILE B 76  ? 0.64858 1.30096 0.74961 -0.11780 -0.12407 0.25969  96  ILE B C   
1501 O O   . ILE B 76  ? 0.65802 1.37176 0.77764 -0.08834 -0.08877 0.26850  96  ILE B O   
1502 C CB  . ILE B 76  ? 0.69018 1.14585 0.64727 -0.11713 -0.13101 0.22155  96  ILE B CB  
1503 C CG1 . ILE B 76  ? 0.69043 1.14005 0.65001 -0.18171 -0.14118 0.24413  96  ILE B CG1 
1504 C CG2 . ILE B 76  ? 0.68087 1.14469 0.61270 -0.08444 -0.09326 0.22150  96  ILE B CG2 
1505 C CD1 . ILE B 76  ? 0.68793 1.10569 0.64835 -0.21443 -0.18178 0.23962  96  ILE B CD1 
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