data_9GQ8
# 
_entry.id   9GQ8 
# 
_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   9GQ8         pdb_00009gq8 10.2210/pdb9gq8/pdb 
WWPDB D_1292141282 ?            ?                   
# 
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 2025-01-15 ? 
2 'Structure model' 1 1 2025-03-12 ? 
3 'Structure model' 1 2 2025-03-19 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 3 'Structure model' citation        
3 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 3 'Structure model' '_citation.page_first'              
5 3 'Structure model' '_citation.page_last'               
6 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GQ8 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-09 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              felix.hausch@tu-darmstadt.de 
_pdbx_contact_author.name_first         Felix 
_pdbx_contact_author.name_last          Hausch 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3710-8838 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Meyners, C.' 1 ? 
'Spiske, M.'  2 ? 
'Hausch, F.'  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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202418511 
_citation.page_last                 e202418511 
_citation.title                     
'Conformationally Restricted Macrocycles as Improved FKBP51 Inhibitors Enabled by Systematic Linker Derivatization.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202418511 
_citation.pdbx_database_id_PubMed   39752587 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Spiske, M.'     1 ?                   
primary 'Meyners, C.'    2 ?                   
primary 'Bauder, M.'     3 ?                   
primary 'Repity, M.'     4 ?                   
primary 'Brudy, C.'      5 ?                   
primary 'Sugiarto, W.O.' 6 ?                   
primary 'Achaq, H.'      7 ?                   
primary 'Geiger, T.M.'   8 ?                   
primary 'Hausch, F.'     9 0000-0002-3710-8838 
# 
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 'Peptidyl-prolyl cis-trans isomerase FKBP5' 14004.026 2  5.2.1.8 'A19T, C103A, C107I' ? ? 
2 non-polymer syn 
'(2~{S},9~{S})-2-cyclohexyl-20,23-dimethoxy-11,18-dioxa-4-azatricyclo[17.2.2.0^{4,9}]tricosa-1(21),19,22-triene-3,10-dione' 
487.628   2  ?       ?                    ? ? 
3 water       nat water 18.015    37 ?       ?                    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;PPIase FKBP5,51 kDa FK506-binding protein,FKBP-51,54 kDa progesterone receptor-associated immunophilin,Androgen-regulated protein 6,FF1 antigen,FK506-binding protein 5,FKBP-5,FKBP54,p54,HSP90-binding immunophilin,Rotamase
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GAPATVTEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDI
GVATMKKGEIAHLLIKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAPATVTEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDI
GVATMKKGEIAHLLIKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGE
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2~{S},9~{S})-2-cyclohexyl-20,23-dimethoxy-11,18-dioxa-4-azatricyclo[17.2.2.0^{4,9}]tricosa-1(21),19,22-triene-3,10-dione' 
A1IN6 
3 water                                                                                                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   PRO n 
1 4   ALA n 
1 5   THR n 
1 6   VAL n 
1 7   THR n 
1 8   GLU n 
1 9   GLN n 
1 10  GLY n 
1 11  GLU n 
1 12  ASP n 
1 13  ILE n 
1 14  THR n 
1 15  SER n 
1 16  LYS n 
1 17  LYS n 
1 18  ASP n 
1 19  ARG n 
1 20  GLY n 
1 21  VAL n 
1 22  LEU n 
1 23  LYS n 
1 24  ILE n 
1 25  VAL n 
1 26  LYS n 
1 27  ARG n 
1 28  VAL n 
1 29  GLY n 
1 30  ASN n 
1 31  GLY n 
1 32  GLU n 
1 33  GLU n 
1 34  THR n 
1 35  PRO n 
1 36  MET n 
1 37  ILE n 
1 38  GLY n 
1 39  ASP n 
1 40  LYS n 
1 41  VAL n 
1 42  TYR n 
1 43  VAL n 
1 44  HIS n 
1 45  TYR n 
1 46  LYS n 
1 47  GLY n 
1 48  LYS n 
1 49  LEU n 
1 50  SER n 
1 51  ASN n 
1 52  GLY n 
1 53  LYS n 
1 54  LYS n 
1 55  PHE n 
1 56  ASP n 
1 57  SER n 
1 58  SER n 
1 59  HIS n 
1 60  ASP n 
1 61  ARG n 
1 62  ASN n 
1 63  GLU n 
1 64  PRO n 
1 65  PHE n 
1 66  VAL n 
1 67  PHE n 
1 68  SER n 
1 69  LEU n 
1 70  GLY n 
1 71  LYS n 
1 72  GLY n 
1 73  GLN n 
1 74  VAL n 
1 75  ILE n 
1 76  LYS n 
1 77  ALA n 
1 78  TRP n 
1 79  ASP n 
1 80  ILE n 
1 81  GLY n 
1 82  VAL n 
1 83  ALA n 
1 84  THR n 
1 85  MET n 
1 86  LYS n 
1 87  LYS n 
1 88  GLY n 
1 89  GLU n 
1 90  ILE n 
1 91  ALA n 
1 92  HIS n 
1 93  LEU n 
1 94  LEU n 
1 95  ILE n 
1 96  LYS n 
1 97  PRO n 
1 98  GLU n 
1 99  TYR n 
1 100 ALA n 
1 101 TYR n 
1 102 GLY n 
1 103 SER n 
1 104 ALA n 
1 105 GLY n 
1 106 SER n 
1 107 LEU n 
1 108 PRO n 
1 109 LYS n 
1 110 ILE n 
1 111 PRO n 
1 112 SER n 
1 113 ASN n 
1 114 ALA n 
1 115 THR n 
1 116 LEU n 
1 117 PHE n 
1 118 PHE n 
1 119 GLU n 
1 120 ILE n 
1 121 GLU n 
1 122 LEU n 
1 123 LEU n 
1 124 ASP n 
1 125 PHE n 
1 126 LYS n 
1 127 GLY n 
1 128 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   128 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'FKBP5, AIG6, FKBP51' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IN6 non-polymer         . 
'(2~{S},9~{S})-2-cyclohexyl-20,23-dimethoxy-11,18-dioxa-4-azatricyclo[17.2.2.0^{4,9}]tricosa-1(21),19,22-triene-3,10-dione' ? 
'C28 H41 N O6'   487.628 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   13  13  GLY GLY B . n 
A 1 2   ALA 2   14  14  ALA ALA B . n 
A 1 3   PRO 3   15  15  PRO PRO B . n 
A 1 4   ALA 4   16  16  ALA ALA B . n 
A 1 5   THR 5   17  17  THR THR B . n 
A 1 6   VAL 6   18  18  VAL VAL B . n 
A 1 7   THR 7   19  19  THR THR B . n 
A 1 8   GLU 8   20  20  GLU GLU B . n 
A 1 9   GLN 9   21  21  GLN GLN B . n 
A 1 10  GLY 10  22  22  GLY GLY B . n 
A 1 11  GLU 11  23  23  GLU GLU B . n 
A 1 12  ASP 12  24  24  ASP ASP B . n 
A 1 13  ILE 13  25  25  ILE ILE B . n 
A 1 14  THR 14  26  26  THR THR B . n 
A 1 15  SER 15  27  27  SER SER B . n 
A 1 16  LYS 16  28  28  LYS LYS B . n 
A 1 17  LYS 17  29  29  LYS LYS B . n 
A 1 18  ASP 18  30  30  ASP ASP B . n 
A 1 19  ARG 19  31  31  ARG ARG B . n 
A 1 20  GLY 20  32  32  GLY GLY B . n 
A 1 21  VAL 21  33  33  VAL VAL B . n 
A 1 22  LEU 22  34  34  LEU LEU B . n 
A 1 23  LYS 23  35  35  LYS LYS B . n 
A 1 24  ILE 24  36  36  ILE ILE B . n 
A 1 25  VAL 25  37  37  VAL VAL B . n 
A 1 26  LYS 26  38  38  LYS LYS B . n 
A 1 27  ARG 27  39  39  ARG ARG B . n 
A 1 28  VAL 28  40  40  VAL VAL B . n 
A 1 29  GLY 29  41  41  GLY GLY B . n 
A 1 30  ASN 30  42  42  ASN ASN B . n 
A 1 31  GLY 31  43  43  GLY GLY B . n 
A 1 32  GLU 32  44  44  GLU GLU B . n 
A 1 33  GLU 33  45  45  GLU GLU B . n 
A 1 34  THR 34  46  46  THR THR B . n 
A 1 35  PRO 35  47  47  PRO PRO B . n 
A 1 36  MET 36  48  48  MET MET B . n 
A 1 37  ILE 37  49  49  ILE ILE B . n 
A 1 38  GLY 38  50  50  GLY GLY B . n 
A 1 39  ASP 39  51  51  ASP ASP B . n 
A 1 40  LYS 40  52  52  LYS LYS B . n 
A 1 41  VAL 41  53  53  VAL VAL B . n 
A 1 42  TYR 42  54  54  TYR TYR B . n 
A 1 43  VAL 43  55  55  VAL VAL B . n 
A 1 44  HIS 44  56  56  HIS HIS B . n 
A 1 45  TYR 45  57  57  TYR TYR B . n 
A 1 46  LYS 46  58  58  LYS LYS B . n 
A 1 47  GLY 47  59  59  GLY GLY B . n 
A 1 48  LYS 48  60  60  LYS LYS B . n 
A 1 49  LEU 49  61  61  LEU LEU B . n 
A 1 50  SER 50  62  62  SER SER B . n 
A 1 51  ASN 51  63  63  ASN ASN B . n 
A 1 52  GLY 52  64  64  GLY GLY B . n 
A 1 53  LYS 53  65  65  LYS LYS B . n 
A 1 54  LYS 54  66  66  LYS LYS B . n 
A 1 55  PHE 55  67  67  PHE PHE B . n 
A 1 56  ASP 56  68  68  ASP ASP B . n 
A 1 57  SER 57  69  69  SER SER B . n 
A 1 58  SER 58  70  70  SER SER B . n 
A 1 59  HIS 59  71  71  HIS HIS B . n 
A 1 60  ASP 60  72  72  ASP ASP B . n 
A 1 61  ARG 61  73  73  ARG ARG B . n 
A 1 62  ASN 62  74  74  ASN ASN B . n 
A 1 63  GLU 63  75  75  GLU GLU B . n 
A 1 64  PRO 64  76  76  PRO PRO B . n 
A 1 65  PHE 65  77  77  PHE PHE B . n 
A 1 66  VAL 66  78  78  VAL VAL B . n 
A 1 67  PHE 67  79  79  PHE PHE B . n 
A 1 68  SER 68  80  80  SER SER B . n 
A 1 69  LEU 69  81  81  LEU LEU B . n 
A 1 70  GLY 70  82  82  GLY GLY B . n 
A 1 71  LYS 71  83  83  LYS LYS B . n 
A 1 72  GLY 72  84  84  GLY GLY B . n 
A 1 73  GLN 73  85  85  GLN GLN B . n 
A 1 74  VAL 74  86  86  VAL VAL B . n 
A 1 75  ILE 75  87  87  ILE ILE B . n 
A 1 76  LYS 76  88  88  LYS LYS B . n 
A 1 77  ALA 77  89  89  ALA ALA B . n 
A 1 78  TRP 78  90  90  TRP TRP B . n 
A 1 79  ASP 79  91  91  ASP ASP B . n 
A 1 80  ILE 80  92  92  ILE ILE B . n 
A 1 81  GLY 81  93  93  GLY GLY B . n 
A 1 82  VAL 82  94  94  VAL VAL B . n 
A 1 83  ALA 83  95  95  ALA ALA B . n 
A 1 84  THR 84  96  96  THR THR B . n 
A 1 85  MET 85  97  97  MET MET B . n 
A 1 86  LYS 86  98  98  LYS LYS B . n 
A 1 87  LYS 87  99  99  LYS LYS B . n 
A 1 88  GLY 88  100 100 GLY GLY B . n 
A 1 89  GLU 89  101 101 GLU GLU B . n 
A 1 90  ILE 90  102 102 ILE ILE B . n 
A 1 91  ALA 91  103 103 ALA ALA B . n 
A 1 92  HIS 92  104 104 HIS HIS B . n 
A 1 93  LEU 93  105 105 LEU LEU B . n 
A 1 94  LEU 94  106 106 LEU LEU B . n 
A 1 95  ILE 95  107 107 ILE ILE B . n 
A 1 96  LYS 96  108 108 LYS LYS B . n 
A 1 97  PRO 97  109 109 PRO PRO B . n 
A 1 98  GLU 98  110 110 GLU GLU B . n 
A 1 99  TYR 99  111 111 TYR TYR B . n 
A 1 100 ALA 100 112 112 ALA ALA B . n 
A 1 101 TYR 101 113 113 TYR TYR B . n 
A 1 102 GLY 102 114 114 GLY GLY B . n 
A 1 103 SER 103 115 115 SER SER B . n 
A 1 104 ALA 104 116 116 ALA ALA B . n 
A 1 105 GLY 105 117 117 GLY GLY B . n 
A 1 106 SER 106 118 118 SER SER B . n 
A 1 107 LEU 107 119 119 LEU LEU B . n 
A 1 108 PRO 108 120 120 PRO PRO B . n 
A 1 109 LYS 109 121 121 LYS LYS B . n 
A 1 110 ILE 110 122 122 ILE ILE B . n 
A 1 111 PRO 111 123 123 PRO PRO B . n 
A 1 112 SER 112 124 124 SER SER B . n 
A 1 113 ASN 113 125 125 ASN ASN B . n 
A 1 114 ALA 114 126 126 ALA ALA B . n 
A 1 115 THR 115 127 127 THR THR B . n 
A 1 116 LEU 116 128 128 LEU LEU B . n 
A 1 117 PHE 117 129 129 PHE PHE B . n 
A 1 118 PHE 118 130 130 PHE PHE B . n 
A 1 119 GLU 119 131 131 GLU GLU B . n 
A 1 120 ILE 120 132 132 ILE ILE B . n 
A 1 121 GLU 121 133 133 GLU GLU B . n 
A 1 122 LEU 122 134 134 LEU LEU B . n 
A 1 123 LEU 123 135 135 LEU LEU B . n 
A 1 124 ASP 124 136 136 ASP ASP B . n 
A 1 125 PHE 125 137 137 PHE PHE B . n 
A 1 126 LYS 126 138 138 LYS LYS B . n 
A 1 127 GLY 127 139 139 GLY GLY B . n 
A 1 128 GLU 128 140 140 GLU GLU B . n 
B 1 1   GLY 1   13  ?   ?   ?   A . n 
B 1 2   ALA 2   14  ?   ?   ?   A . n 
B 1 3   PRO 3   15  ?   ?   ?   A . n 
B 1 4   ALA 4   16  ?   ?   ?   A . n 
B 1 5   THR 5   17  17  THR THR A . n 
B 1 6   VAL 6   18  18  VAL VAL A . n 
B 1 7   THR 7   19  19  THR THR A . n 
B 1 8   GLU 8   20  20  GLU GLU A . n 
B 1 9   GLN 9   21  21  GLN GLN A . n 
B 1 10  GLY 10  22  22  GLY GLY A . n 
B 1 11  GLU 11  23  23  GLU GLU A . n 
B 1 12  ASP 12  24  24  ASP ASP A . n 
B 1 13  ILE 13  25  25  ILE ILE A . n 
B 1 14  THR 14  26  26  THR THR A . n 
B 1 15  SER 15  27  27  SER SER A . n 
B 1 16  LYS 16  28  28  LYS LYS A . n 
B 1 17  LYS 17  29  29  LYS LYS A . n 
B 1 18  ASP 18  30  30  ASP ASP A . n 
B 1 19  ARG 19  31  31  ARG ARG A . n 
B 1 20  GLY 20  32  32  GLY GLY A . n 
B 1 21  VAL 21  33  33  VAL VAL A . n 
B 1 22  LEU 22  34  34  LEU LEU A . n 
B 1 23  LYS 23  35  35  LYS LYS A . n 
B 1 24  ILE 24  36  36  ILE ILE A . n 
B 1 25  VAL 25  37  37  VAL VAL A . n 
B 1 26  LYS 26  38  38  LYS LYS A . n 
B 1 27  ARG 27  39  39  ARG ARG A . n 
B 1 28  VAL 28  40  40  VAL VAL A . n 
B 1 29  GLY 29  41  41  GLY GLY A . n 
B 1 30  ASN 30  42  42  ASN ASN A . n 
B 1 31  GLY 31  43  43  GLY GLY A . n 
B 1 32  GLU 32  44  44  GLU GLU A . n 
B 1 33  GLU 33  45  45  GLU GLU A . n 
B 1 34  THR 34  46  46  THR THR A . n 
B 1 35  PRO 35  47  47  PRO PRO A . n 
B 1 36  MET 36  48  48  MET MET A . n 
B 1 37  ILE 37  49  49  ILE ILE A . n 
B 1 38  GLY 38  50  50  GLY GLY A . n 
B 1 39  ASP 39  51  51  ASP ASP A . n 
B 1 40  LYS 40  52  52  LYS LYS A . n 
B 1 41  VAL 41  53  53  VAL VAL A . n 
B 1 42  TYR 42  54  54  TYR TYR A . n 
B 1 43  VAL 43  55  55  VAL VAL A . n 
B 1 44  HIS 44  56  56  HIS HIS A . n 
B 1 45  TYR 45  57  57  TYR TYR A . n 
B 1 46  LYS 46  58  58  LYS LYS A . n 
B 1 47  GLY 47  59  59  GLY GLY A . n 
B 1 48  LYS 48  60  60  LYS LYS A . n 
B 1 49  LEU 49  61  61  LEU LEU A . n 
B 1 50  SER 50  62  62  SER SER A . n 
B 1 51  ASN 51  63  63  ASN ASN A . n 
B 1 52  GLY 52  64  64  GLY GLY A . n 
B 1 53  LYS 53  65  65  LYS LYS A . n 
B 1 54  LYS 54  66  66  LYS LYS A . n 
B 1 55  PHE 55  67  67  PHE PHE A . n 
B 1 56  ASP 56  68  68  ASP ASP A . n 
B 1 57  SER 57  69  69  SER SER A . n 
B 1 58  SER 58  70  70  SER SER A . n 
B 1 59  HIS 59  71  71  HIS HIS A . n 
B 1 60  ASP 60  72  72  ASP ASP A . n 
B 1 61  ARG 61  73  73  ARG ARG A . n 
B 1 62  ASN 62  74  74  ASN ASN A . n 
B 1 63  GLU 63  75  75  GLU GLU A . n 
B 1 64  PRO 64  76  76  PRO PRO A . n 
B 1 65  PHE 65  77  77  PHE PHE A . n 
B 1 66  VAL 66  78  78  VAL VAL A . n 
B 1 67  PHE 67  79  79  PHE PHE A . n 
B 1 68  SER 68  80  80  SER SER A . n 
B 1 69  LEU 69  81  81  LEU LEU A . n 
B 1 70  GLY 70  82  82  GLY GLY A . n 
B 1 71  LYS 71  83  83  LYS LYS A . n 
B 1 72  GLY 72  84  84  GLY GLY A . n 
B 1 73  GLN 73  85  85  GLN GLN A . n 
B 1 74  VAL 74  86  86  VAL VAL A . n 
B 1 75  ILE 75  87  87  ILE ILE A . n 
B 1 76  LYS 76  88  88  LYS LYS A . n 
B 1 77  ALA 77  89  89  ALA ALA A . n 
B 1 78  TRP 78  90  90  TRP TRP A . n 
B 1 79  ASP 79  91  91  ASP ASP A . n 
B 1 80  ILE 80  92  92  ILE ILE A . n 
B 1 81  GLY 81  93  93  GLY GLY A . n 
B 1 82  VAL 82  94  94  VAL VAL A . n 
B 1 83  ALA 83  95  95  ALA ALA A . n 
B 1 84  THR 84  96  96  THR THR A . n 
B 1 85  MET 85  97  97  MET MET A . n 
B 1 86  LYS 86  98  98  LYS LYS A . n 
B 1 87  LYS 87  99  99  LYS LYS A . n 
B 1 88  GLY 88  100 100 GLY GLY A . n 
B 1 89  GLU 89  101 101 GLU GLU A . n 
B 1 90  ILE 90  102 102 ILE ILE A . n 
B 1 91  ALA 91  103 103 ALA ALA A . n 
B 1 92  HIS 92  104 104 HIS HIS A . n 
B 1 93  LEU 93  105 105 LEU LEU A . n 
B 1 94  LEU 94  106 106 LEU LEU A . n 
B 1 95  ILE 95  107 107 ILE ILE A . n 
B 1 96  LYS 96  108 108 LYS LYS A . n 
B 1 97  PRO 97  109 109 PRO PRO A . n 
B 1 98  GLU 98  110 110 GLU GLU A . n 
B 1 99  TYR 99  111 111 TYR TYR A . n 
B 1 100 ALA 100 112 112 ALA ALA A . n 
B 1 101 TYR 101 113 113 TYR TYR A . n 
B 1 102 GLY 102 114 114 GLY GLY A . n 
B 1 103 SER 103 115 115 SER SER A . n 
B 1 104 ALA 104 116 116 ALA ALA A . n 
B 1 105 GLY 105 117 117 GLY GLY A . n 
B 1 106 SER 106 118 118 SER SER A . n 
B 1 107 LEU 107 119 119 LEU LEU A . n 
B 1 108 PRO 108 120 120 PRO PRO A . n 
B 1 109 LYS 109 121 121 LYS LYS A . n 
B 1 110 ILE 110 122 122 ILE ILE A . n 
B 1 111 PRO 111 123 123 PRO PRO A . n 
B 1 112 SER 112 124 124 SER SER A . n 
B 1 113 ASN 113 125 125 ASN ASN A . n 
B 1 114 ALA 114 126 126 ALA ALA A . n 
B 1 115 THR 115 127 127 THR THR A . n 
B 1 116 LEU 116 128 128 LEU LEU A . n 
B 1 117 PHE 117 129 129 PHE PHE A . n 
B 1 118 PHE 118 130 130 PHE PHE A . n 
B 1 119 GLU 119 131 131 GLU GLU A . n 
B 1 120 ILE 120 132 132 ILE ILE A . n 
B 1 121 GLU 121 133 133 GLU GLU A . n 
B 1 122 LEU 122 134 134 LEU LEU A . n 
B 1 123 LEU 123 135 135 LEU LEU A . n 
B 1 124 ASP 124 136 136 ASP ASP A . n 
B 1 125 PHE 125 137 137 PHE PHE A . n 
B 1 126 LYS 126 138 138 LYS LYS A . n 
B 1 127 GLY 127 139 139 GLY GLY A . n 
B 1 128 GLU 128 140 140 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IN6 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IN6 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1IN6 1  201 201 A1IN6 PDB B . 
D 2 A1IN6 1  201 201 A1IN6 PDB A . 
E 3 HOH   1  301 21  HOH   HOH B . 
E 3 HOH   2  302 15  HOH   HOH B . 
E 3 HOH   3  303 18  HOH   HOH B . 
E 3 HOH   4  304 13  HOH   HOH B . 
E 3 HOH   5  305 3   HOH   HOH B . 
E 3 HOH   6  306 24  HOH   HOH B . 
E 3 HOH   7  307 23  HOH   HOH B . 
E 3 HOH   8  308 31  HOH   HOH B . 
E 3 HOH   9  309 6   HOH   HOH B . 
E 3 HOH   10 310 7   HOH   HOH B . 
E 3 HOH   11 311 22  HOH   HOH B . 
E 3 HOH   12 312 30  HOH   HOH B . 
E 3 HOH   13 313 37  HOH   HOH B . 
E 3 HOH   14 314 33  HOH   HOH B . 
E 3 HOH   15 315 34  HOH   HOH B . 
F 3 HOH   1  301 27  HOH   HOH A . 
F 3 HOH   2  302 8   HOH   HOH A . 
F 3 HOH   3  303 32  HOH   HOH A . 
F 3 HOH   4  304 25  HOH   HOH A . 
F 3 HOH   5  305 4   HOH   HOH A . 
F 3 HOH   6  306 11  HOH   HOH A . 
F 3 HOH   7  307 16  HOH   HOH A . 
F 3 HOH   8  308 20  HOH   HOH A . 
F 3 HOH   9  309 10  HOH   HOH A . 
F 3 HOH   10 310 5   HOH   HOH A . 
F 3 HOH   11 311 1   HOH   HOH A . 
F 3 HOH   12 312 17  HOH   HOH A . 
F 3 HOH   13 313 19  HOH   HOH A . 
F 3 HOH   14 314 14  HOH   HOH A . 
F 3 HOH   15 315 39  HOH   HOH A . 
F 3 HOH   16 316 28  HOH   HOH A . 
F 3 HOH   17 317 9   HOH   HOH A . 
F 3 HOH   18 318 35  HOH   HOH A . 
F 3 HOH   19 319 29  HOH   HOH A . 
F 3 HOH   20 320 38  HOH   HOH A . 
F 3 HOH   21 321 36  HOH   HOH A . 
F 3 HOH   22 322 26  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 B GLU 20  ? CG  ? A GLU 8   CG  
2   1 Y 1 B GLU 20  ? CD  ? A GLU 8   CD  
3   1 Y 1 B GLU 20  ? OE1 ? A GLU 8   OE1 
4   1 Y 1 B GLU 20  ? OE2 ? A GLU 8   OE2 
5   1 Y 1 B GLN 21  ? CG  ? A GLN 9   CG  
6   1 Y 1 B GLN 21  ? CD  ? A GLN 9   CD  
7   1 Y 1 B GLN 21  ? OE1 ? A GLN 9   OE1 
8   1 Y 1 B GLN 21  ? NE2 ? A GLN 9   NE2 
9   1 Y 1 B GLU 44  ? CG  ? A GLU 32  CG  
10  1 Y 1 B GLU 44  ? CD  ? A GLU 32  CD  
11  1 Y 1 B GLU 44  ? OE1 ? A GLU 32  OE1 
12  1 Y 1 B GLU 44  ? OE2 ? A GLU 32  OE2 
13  1 Y 1 B GLU 45  ? CG  ? A GLU 33  CG  
14  1 Y 1 B GLU 45  ? CD  ? A GLU 33  CD  
15  1 Y 1 B GLU 45  ? OE1 ? A GLU 33  OE1 
16  1 Y 1 B GLU 45  ? OE2 ? A GLU 33  OE2 
17  1 Y 1 B LYS 65  ? CG  ? A LYS 53  CG  
18  1 Y 1 B LYS 65  ? CD  ? A LYS 53  CD  
19  1 Y 1 B LYS 65  ? CE  ? A LYS 53  CE  
20  1 Y 1 B LYS 65  ? NZ  ? A LYS 53  NZ  
21  1 Y 1 B LYS 66  ? CG  ? A LYS 54  CG  
22  1 Y 1 B LYS 66  ? CD  ? A LYS 54  CD  
23  1 Y 1 B LYS 66  ? CE  ? A LYS 54  CE  
24  1 Y 1 B LYS 66  ? NZ  ? A LYS 54  NZ  
25  1 Y 1 B ARG 73  ? CG  ? A ARG 61  CG  
26  1 Y 1 B ARG 73  ? CD  ? A ARG 61  CD  
27  1 Y 1 B ARG 73  ? NE  ? A ARG 61  NE  
28  1 Y 1 B ARG 73  ? CZ  ? A ARG 61  CZ  
29  1 Y 1 B ARG 73  ? NH1 ? A ARG 61  NH1 
30  1 Y 1 B ARG 73  ? NH2 ? A ARG 61  NH2 
31  1 Y 1 B ASN 74  ? CG  ? A ASN 62  CG  
32  1 Y 1 B ASN 74  ? OD1 ? A ASN 62  OD1 
33  1 Y 1 B ASN 74  ? ND2 ? A ASN 62  ND2 
34  1 Y 1 B LYS 83  ? CG  ? A LYS 71  CG  
35  1 Y 1 B LYS 83  ? CD  ? A LYS 71  CD  
36  1 Y 1 B LYS 83  ? CE  ? A LYS 71  CE  
37  1 Y 1 B LYS 83  ? NZ  ? A LYS 71  NZ  
38  1 Y 1 B LYS 88  ? CG  ? A LYS 76  CG  
39  1 Y 1 B LYS 88  ? CD  ? A LYS 76  CD  
40  1 Y 1 B LYS 88  ? CE  ? A LYS 76  CE  
41  1 Y 1 B LYS 88  ? NZ  ? A LYS 76  NZ  
42  1 Y 1 B LYS 98  ? CG  ? A LYS 86  CG  
43  1 Y 1 B LYS 98  ? CD  ? A LYS 86  CD  
44  1 Y 1 B LYS 98  ? CE  ? A LYS 86  CE  
45  1 Y 1 B LYS 98  ? NZ  ? A LYS 86  NZ  
46  1 Y 1 B LYS 99  ? CG  ? A LYS 87  CG  
47  1 Y 1 B LYS 99  ? CD  ? A LYS 87  CD  
48  1 Y 1 B LYS 99  ? CE  ? A LYS 87  CE  
49  1 Y 1 B LYS 99  ? NZ  ? A LYS 87  NZ  
50  1 Y 1 B LYS 138 ? CG  ? A LYS 126 CG  
51  1 Y 1 B LYS 138 ? CD  ? A LYS 126 CD  
52  1 Y 1 B LYS 138 ? CE  ? A LYS 126 CE  
53  1 Y 1 B LYS 138 ? NZ  ? A LYS 126 NZ  
54  1 Y 1 B GLU 140 ? CG  ? A GLU 128 CG  
55  1 Y 1 B GLU 140 ? CD  ? A GLU 128 CD  
56  1 Y 1 B GLU 140 ? OE1 ? A GLU 128 OE1 
57  1 Y 1 B GLU 140 ? OE2 ? A GLU 128 OE2 
58  1 Y 1 A GLU 44  ? CG  ? B GLU 32  CG  
59  1 Y 1 A GLU 44  ? CD  ? B GLU 32  CD  
60  1 Y 1 A GLU 44  ? OE1 ? B GLU 32  OE1 
61  1 Y 1 A GLU 44  ? OE2 ? B GLU 32  OE2 
62  1 Y 1 A GLU 45  ? CG  ? B GLU 33  CG  
63  1 Y 1 A GLU 45  ? CD  ? B GLU 33  CD  
64  1 Y 1 A GLU 45  ? OE1 ? B GLU 33  OE1 
65  1 Y 1 A GLU 45  ? OE2 ? B GLU 33  OE2 
66  1 Y 1 A LYS 52  ? CG  ? B LYS 40  CG  
67  1 Y 1 A LYS 52  ? CD  ? B LYS 40  CD  
68  1 Y 1 A LYS 52  ? CE  ? B LYS 40  CE  
69  1 Y 1 A LYS 52  ? NZ  ? B LYS 40  NZ  
70  1 Y 1 A LYS 65  ? CG  ? B LYS 53  CG  
71  1 Y 1 A LYS 65  ? CD  ? B LYS 53  CD  
72  1 Y 1 A LYS 65  ? CE  ? B LYS 53  CE  
73  1 Y 1 A LYS 65  ? NZ  ? B LYS 53  NZ  
74  1 Y 1 A LYS 66  ? CG  ? B LYS 54  CG  
75  1 Y 1 A LYS 66  ? CD  ? B LYS 54  CD  
76  1 Y 1 A LYS 66  ? CE  ? B LYS 54  CE  
77  1 Y 1 A LYS 66  ? NZ  ? B LYS 54  NZ  
78  1 Y 1 A ARG 73  ? CG  ? B ARG 61  CG  
79  1 Y 1 A ARG 73  ? CD  ? B ARG 61  CD  
80  1 Y 1 A ARG 73  ? NE  ? B ARG 61  NE  
81  1 Y 1 A ARG 73  ? CZ  ? B ARG 61  CZ  
82  1 Y 1 A ARG 73  ? NH1 ? B ARG 61  NH1 
83  1 Y 1 A ARG 73  ? NH2 ? B ARG 61  NH2 
84  1 Y 1 A ASN 74  ? CG  ? B ASN 62  CG  
85  1 Y 1 A ASN 74  ? OD1 ? B ASN 62  OD1 
86  1 Y 1 A ASN 74  ? ND2 ? B ASN 62  ND2 
87  1 Y 1 A GLU 75  ? CG  ? B GLU 63  CG  
88  1 Y 1 A GLU 75  ? CD  ? B GLU 63  CD  
89  1 Y 1 A GLU 75  ? OE1 ? B GLU 63  OE1 
90  1 Y 1 A GLU 75  ? OE2 ? B GLU 63  OE2 
91  1 Y 1 A LYS 83  ? CG  ? B LYS 71  CG  
92  1 Y 1 A LYS 83  ? CD  ? B LYS 71  CD  
93  1 Y 1 A LYS 83  ? CE  ? B LYS 71  CE  
94  1 Y 1 A LYS 83  ? NZ  ? B LYS 71  NZ  
95  1 Y 1 A LYS 88  ? CG  ? B LYS 76  CG  
96  1 Y 1 A LYS 88  ? CD  ? B LYS 76  CD  
97  1 Y 1 A LYS 88  ? CE  ? B LYS 76  CE  
98  1 Y 1 A LYS 88  ? NZ  ? B LYS 76  NZ  
99  1 Y 1 A LYS 138 ? CG  ? B LYS 126 CG  
100 1 Y 1 A LYS 138 ? CD  ? B LYS 126 CD  
101 1 Y 1 A LYS 138 ? CE  ? B LYS 126 CE  
102 1 Y 1 A LYS 138 ? NZ  ? B LYS 126 NZ  
103 1 Y 1 A GLU 140 ? CG  ? B GLU 128 CG  
104 1 Y 1 A GLU 140 ? CD  ? B GLU 128 CD  
105 1 Y 1 A GLU 140 ? OE1 ? B GLU 128 OE1 
106 1 Y 1 A GLU 140 ? OE2 ? B GLU 128 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? '5.8.0430 (refmacat 0.4.82)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoXDS ? ? ? .                            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                            4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GQ8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.44 
_cell.length_a_esd                 ? 
_cell.length_b                     48.44 
_cell.length_b_esd                 ? 
_cell.length_c                     192.239 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9GQ8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 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                   9GQ8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.09 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% PEG3350, 0.2M ammonium thiocyanate, 0.1M HEPES-NaOH pH 7.5' 
_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 PILATUS3 S 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-03-18 
_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   0.918400 
_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                        'BESSY BEAMLINE 14.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.918400 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   14.1 
_diffrn_source.pdbx_synchrotron_site       BESSY 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GQ8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.16 
_reflns.d_resolution_low                               48.06 
_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                                     14911 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_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                                0.124 
_reflns.pdbx_Rpim_I_all                                0.054 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.112 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
8.91 48.06 ? 24.1 ? ? ? ? 277  ? ? ? ? ? ? ? ? ? ? ? 8.3 0.72 ? ? 0.064 0.026 ? 1 ? 0.999 ? ? 99.2 ? 0.058 ? ? ? ? ? ? ? ? ? 
2.16 2.23  ? 1.6  ? ? ? ? 1267 ? ? ? ? ? ? ? ? ? ? ? 8.3 0.77 ? ? 1.278 0.599 ? 2 ? 0.536 ? ? 99.2 ? 1.124 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.601 
_refine.aniso_B[1][2]                            -0.300 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -0.601 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            1.949 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               48.473 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.941 
_refine.correlation_coeff_Fo_to_Fc_free          0.917 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_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                                 9GQ8 
_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                            2.160 
_refine.ls_d_res_low                             41.019 
_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                     14855 
_refine.ls_number_reflns_R_free                  716 
_refine.ls_number_reflns_R_work                  14139 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.832 
_refine.ls_percent_reflns_R_free                 4.820 
_refine.ls_R_factor_all                          0.229 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2762 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2267 
_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                    'MASK BULK SOLVENT' 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.277 
_refine.pdbx_overall_ESU_R_Free                  0.226 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                 ? 
_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                             15.464 
_refine.overall_SU_ML                            0.186 
_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                       2.160 
_refine_hist.d_res_low                        41.019 
_refine_hist.number_atoms_solvent             37 
_refine_hist.number_atoms_total               1954 
_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        1847 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_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' ? 0.011  0.012  1962 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.016  1817 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.804  1.849  2658 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.089  1.825  4230 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 8.085  5.000  250  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 5.279  5.000  4    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 13.750 10.000 296  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.076 10.000 67   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.082  0.200  295  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 1.395  0.200  34   ? r_chiral_restr_other           ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  2227 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  397  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.200  0.200  347  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.200  0.200  1647 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.178  0.200  1011 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.087  0.200  985  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.139  0.200  53   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.106  0.200  13   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.203  0.200  45   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.096  0.200  6    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 2.596  2.938  1012 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.596  2.938  1012 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.809  5.276  1258 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.807  5.274  1259 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 2.527  2.984  950  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.526  2.984  951  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.688  5.446  1400 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.687  5.445  1401 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.306  27.911 2125 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.304  27.905 2125 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.116  0.050  3345 ? r_ncsr_local_group_1           ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.11635 ? 0.05009 1 'Local ncs' ? B ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.11635 ? 0.05009 2 'Local ncs' ? A ? ? ? 1 
# 
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' 2.160 2.216  1095 . 66 1019 99.0868  . 0.332 . . 0.332 . . . . . 0.331 . 20 . 0.906 0.885 0.345 
'X-RAY DIFFRACTION' 2.216 2.276  1025 . 48 977  100.0000 . 0.299 . . 0.297 . . . . . 0.292 . 20 . 0.929 0.888 0.348 
'X-RAY DIFFRACTION' 2.276 2.342  1010 . 45 965  100.0000 . 0.289 . . 0.288 . . . . . 0.281 . 20 . 0.939 0.951 0.300 
'X-RAY DIFFRACTION' 2.342 2.414  1000 . 48 951  99.9000  . 0.262 . . 0.260 . . . . . 0.247 . 20 . 0.956 0.940 0.294 
'X-RAY DIFFRACTION' 2.414 2.493  947  . 38 909  100.0000 . 0.255 . . 0.253 . . . . . 0.234 . 20 . 0.961 0.944 0.293 
'X-RAY DIFFRACTION' 2.493 2.580  924  . 40 884  100.0000 . 0.229 . . 0.226 . . . . . 0.204 . 20 . 0.966 0.940 0.305 
'X-RAY DIFFRACTION' 2.580 2.677  917  . 75 842  100.0000 . 0.241 . . 0.234 . . . . . 0.214 . 20 . 0.964 0.935 0.332 
'X-RAY DIFFRACTION' 2.677 2.786  859  . 29 830  100.0000 . 0.234 . . 0.232 . . . . . 0.212 . 20 . 0.965 0.957 0.308 
'X-RAY DIFFRACTION' 2.786 2.909  847  . 43 804  100.0000 . 0.217 . . 0.214 . . . . . 0.198 . 20 . 0.969 0.950 0.272 
'X-RAY DIFFRACTION' 2.909 3.050  800  . 31 766  99.6250  . 0.226 . . 0.224 . . . . . 0.215 . 20 . 0.964 0.954 0.264 
'X-RAY DIFFRACTION' 3.050 3.214  768  . 38 730  100.0000 . 0.218 . . 0.216 . . . . . 0.208 . 20 . 0.968 0.959 0.259 
'X-RAY DIFFRACTION' 3.214 3.408  711  . 37 674  100.0000 . 0.239 . . 0.237 . . . . . 0.232 . 20 . 0.966 0.965 0.268 
'X-RAY DIFFRACTION' 3.408 3.642  703  . 35 667  99.8577  . 0.221 . . 0.219 . . . . . 0.219 . 20 . 0.976 0.967 0.262 
'X-RAY DIFFRACTION' 3.642 3.931  621  . 38 583  100.0000 . 0.215 . . 0.215 . . . . . 0.217 . 20 . 0.977 0.983 0.211 
'X-RAY DIFFRACTION' 3.931 4.302  605  . 25 577  99.5041  . 0.201 . . 0.200 . . . . . 0.212 . 20 . 0.973 0.975 0.230 
'X-RAY DIFFRACTION' 4.302 4.803  561  . 17 544  100.0000 . 0.182 . . 0.179 . . . . . 0.198 . 20 . 0.980 0.944 0.313 
'X-RAY DIFFRACTION' 4.803 5.534  485  . 18 467  100.0000 . 0.199 . . 0.198 . . . . . 0.224 . 20 . 0.976 0.968 0.229 
'X-RAY DIFFRACTION' 5.534 6.747  432  . 17 415  100.0000 . 0.271 . . 0.272 . . . . . 0.300 . 20 . 0.954 0.954 0.252 
'X-RAY DIFFRACTION' 6.747 9.415  343  . 12 330  99.7085  . 0.228 . . 0.226 . . . . . 0.266 . 20 . 0.968 0.944 0.298 
'X-RAY DIFFRACTION' 9.415 41.019 225  . 16 205  98.2222  . 0.264 . . 0.255 . . . . . 0.300 . 20 . 0.940 0.915 0.405 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 B 
2 1 A 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
1 1 1 A THR 5 . A GLY 127 . B THR 17 B GLY 139 ? ? 
1 2 1 B THR 5 . B GLY 127 . A THR 17 A GLY 139 ? ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   'Local NCS retraints between domains:       1       2' 
# 
_struct.entry_id                     9GQ8 
_struct.title                        'The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog p5(2,2)-H2' 
_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        9GQ8 
_struct_keywords.text            'FKBP, Inhibitor, SAFIT, Macrocycle, Complex, ISOMERASE' 
_struct_keywords.pdbx_keywords   ISOMERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FKBP5_HUMAN 
_struct_ref.pdbx_db_accession          Q13451 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVA
TMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGE
;
_struct_ref.pdbx_align_begin           16 
# 
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 9GQ8 B 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
2 1 9GQ8 A 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GQ8 GLY B 1  ? UNP Q13451 ?   ?   'expression tag'      13  1  
1 9GQ8 ALA B 2  ? UNP Q13451 ?   ?   'expression tag'      14  2  
1 9GQ8 PRO B 3  ? UNP Q13451 ?   ?   'expression tag'      15  3  
1 9GQ8 THR B 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  4  
1 9GQ8 ALA B 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 5  
1 9GQ8 ILE B 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 6  
2 9GQ8 GLY A 1  ? UNP Q13451 ?   ?   'expression tag'      13  7  
2 9GQ8 ALA A 2  ? UNP Q13451 ?   ?   'expression tag'      14  8  
2 9GQ8 PRO A 3  ? UNP Q13451 ?   ?   'expression tag'      15  9  
2 9GQ8 THR A 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  10 
2 9GQ8 ALA A 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 11 
2 9GQ8 ILE A 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 12 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 GLY A 1  ? GLY A 10  ? GLY B 13  GLY B 22  1 ? 10 
HELX_P HELX_P2 AA2 HIS A 59 ? ASN A 62  ? HIS B 71  ASN B 74  5 ? 4  
HELX_P HELX_P3 AA3 ILE A 75 ? ALA A 83  ? ILE B 87  ALA B 95  1 ? 9  
HELX_P HELX_P4 AA4 PRO A 97 ? ALA A 100 ? PRO B 109 ALA B 112 5 ? 4  
HELX_P HELX_P5 AA5 HIS B 59 ? ASN B 62  ? HIS A 71  ASN A 74  5 ? 4  
HELX_P HELX_P6 AA6 ILE B 75 ? ALA B 83  ? ILE A 87  ALA A 95  1 ? 9  
HELX_P HELX_P7 AA7 PRO B 97 ? ALA B 100 ? PRO A 109 ALA A 112 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 107 A . ? LEU 119 B PRO 108 A ? PRO 120 B 1 -5.65 
2 LEU 107 B . ? LEU 119 A PRO 108 B ? PRO 120 A 1 5.89  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
# 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? 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 A 11  ? ASP A 12  ? GLU B 23  ASP B 24  
AA1 2 VAL A 21  ? ARG A 27  ? VAL B 33  ARG B 39  
AA1 3 ILE A 90  ? ILE A 95  ? ILE B 102 ILE B 107 
AA1 4 LEU A 116 ? LYS A 126 ? LEU B 128 LYS B 138 
AA1 5 LYS A 40  ? LEU A 49  ? LYS B 52  LEU B 61  
AA1 6 PHE A 55  ? SER A 57  ? PHE B 67  SER B 69  
AA2 1 GLU A 11  ? ASP A 12  ? GLU B 23  ASP B 24  
AA2 2 VAL A 21  ? ARG A 27  ? VAL B 33  ARG B 39  
AA2 3 ILE A 90  ? ILE A 95  ? ILE B 102 ILE B 107 
AA2 4 LEU A 116 ? LYS A 126 ? LEU B 128 LYS B 138 
AA2 5 LYS A 40  ? LEU A 49  ? LYS B 52  LEU B 61  
AA2 6 PHE A 65  ? SER A 68  ? PHE B 77  SER B 80  
AA3 1 GLU B 11  ? ASP B 12  ? GLU A 23  ASP A 24  
AA3 2 VAL B 21  ? ARG B 27  ? VAL A 33  ARG A 39  
AA3 3 ILE B 90  ? ILE B 95  ? ILE A 102 ILE A 107 
AA3 4 LEU B 116 ? LYS B 126 ? LEU A 128 LYS A 138 
AA3 5 LYS B 40  ? LEU B 49  ? LYS A 52  LEU A 61  
AA3 6 PHE B 55  ? SER B 57  ? PHE A 67  SER A 69  
AA4 1 GLU B 11  ? ASP B 12  ? GLU A 23  ASP A 24  
AA4 2 VAL B 21  ? ARG B 27  ? VAL A 33  ARG A 39  
AA4 3 ILE B 90  ? ILE B 95  ? ILE A 102 ILE A 107 
AA4 4 LEU B 116 ? LYS B 126 ? LEU A 128 LYS A 138 
AA4 5 LYS B 40  ? LEU B 49  ? LYS A 52  LEU A 61  
AA4 6 PHE B 65  ? SER B 68  ? PHE A 77  SER A 80  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 11  ? N GLU B 23  O LYS A 23  ? O LYS B 35  
AA1 2 3 N ILE A 24  ? N ILE B 36  O HIS A 92  ? O HIS B 104 
AA1 3 4 N ILE A 95  ? N ILE B 107 O LEU A 116 ? O LEU B 128 
AA1 4 5 O LYS A 126 ? O LYS B 138 N LYS A 40  ? N LYS B 52  
AA1 5 6 N GLY A 47  ? N GLY B 59  O ASP A 56  ? O ASP B 68  
AA2 1 2 N GLU A 11  ? N GLU B 23  O LYS A 23  ? O LYS B 35  
AA2 2 3 N ILE A 24  ? N ILE B 36  O HIS A 92  ? O HIS B 104 
AA2 3 4 N ILE A 95  ? N ILE B 107 O LEU A 116 ? O LEU B 128 
AA2 4 5 O LYS A 126 ? O LYS B 138 N LYS A 40  ? N LYS B 52  
AA2 5 6 N VAL A 41  ? N VAL B 53  O PHE A 67  ? O PHE B 79  
AA3 1 2 N GLU B 11  ? N GLU A 23  O LYS B 23  ? O LYS A 35  
AA3 2 3 N ILE B 24  ? N ILE A 36  O HIS B 92  ? O HIS A 104 
AA3 3 4 N ILE B 95  ? N ILE A 107 O LEU B 116 ? O LEU A 128 
AA3 4 5 O LYS B 126 ? O LYS A 138 N LYS B 40  ? N LYS A 52  
AA3 5 6 N GLY B 47  ? N GLY A 59  O ASP B 56  ? O ASP A 68  
AA4 1 2 N GLU B 11  ? N GLU A 23  O LYS B 23  ? O LYS A 35  
AA4 2 3 N ILE B 24  ? N ILE A 36  O HIS B 92  ? O HIS A 104 
AA4 3 4 N ILE B 95  ? N ILE A 107 O LEU B 116 ? O LEU A 128 
AA4 4 5 O LYS B 126 ? O LYS A 138 N LYS B 40  ? N LYS A 52  
AA4 5 6 N VAL B 41  ? N VAL A 53  O PHE B 67  ? O PHE A 79  
# 
_pdbx_entry_details.entry_id                   9GQ8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HH 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   TYR 
_pdbx_validate_close_contact.auth_seq_id_1    57 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OD2 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ASP 
_pdbx_validate_close_contact.auth_seq_id_2    68 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.60 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              48 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              48 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              48 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                113.70 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            13.50 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                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 B 112 ? ? -128.42 -106.13 
2 1 ALA A 112 ? ? -132.59 -101.27 
3 1 SER A 118 ? ? -150.52 72.69   
# 
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 18.6214 0.8720   3.6210  0.1864 ? -0.0981 ? -0.0172 ? 0.0571 ? 0.0207  ? 0.0736 ? 4.3280 ? -1.8586 
? -0.8248 ? 7.5973 ? -0.0516 ? 3.8316 ? -0.2245 ? 0.0014 ? 0.0466  ? -0.3756 ? 0.1554 ? -0.5934 ? -0.3053 ? 0.2098  ? 0.0691 ? 
2 'X-RAY DIFFRACTION' ? refined 9.5958  -15.4583 28.1012 0.1347 ? 0.0101  ? 0.0160  ? 0.0059 ? -0.0049 ? 0.1065 ? 2.9614 ? 0.4399  
? -0.7148 ? 4.1415 ? -1.0974 ? 3.5723 ? -0.1156 ? 0.0465 ? -0.5122 ? 0.0755  ? 0.0446 ? 0.1825  ? 0.0520  ? -0.0359 ? 0.0709 ? 
# 
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 ? ? B 13 ? ? ? B 201 ? ALL ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 17 ? ? ? A 201 ? ALL ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 13 ? B GLY 1 
2 1 Y 1 A ALA 14 ? B ALA 2 
3 1 Y 1 A PRO 15 ? B PRO 3 
4 1 Y 1 A ALA 16 ? B ALA 4 
# 
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 
A1IN6 CAM  C N N 1   
A1IN6 CAN  C N N 2   
A1IN6 CAO  C N N 3   
A1IN6 CAP  C N N 4   
A1IN6 CAQ  C N N 5   
A1IN6 CAL  C N N 6   
A1IN6 CAG  C N S 7   
A1IN6 CAH  C N N 8   
A1IN6 OAK  O N N 9   
A1IN6 N    N N N 10  
A1IN6 CAV  C N N 11  
A1IN6 CAU  C N N 12  
A1IN6 CAT  C N N 13  
A1IN6 CB   C N N 14  
A1IN6 CA   C N S 15  
A1IN6 C    C N N 16  
A1IN6 O    O N N 17  
A1IN6 OAY  O N N 18  
A1IN6 CAZ  C N N 19  
A1IN6 CBA  C N N 20  
A1IN6 CBB  C N N 21  
A1IN6 CBC  C N N 22  
A1IN6 CBE  C N N 23  
A1IN6 CBD  C N N 24  
A1IN6 OAI  O N N 25  
A1IN6 CAC  C Y N 26  
A1IN6 CAB  C Y N 27  
A1IN6 OBH  O N N 28  
A1IN6 CBI  C N N 29  
A1IN6 CAA  C Y N 30  
A1IN6 CAF  C Y N 31  
A1IN6 CAE  C Y N 32  
A1IN6 CAD  C Y N 33  
A1IN6 OBF  O N N 34  
A1IN6 CBG  C N N 35  
A1IN6 HAM  H N N 36  
A1IN6 HAN  H N N 37  
A1IN6 HAO  H N N 38  
A1IN6 HAP  H N N 39  
A1IN6 HAQ  H N N 40  
A1IN6 HAR  H N N 41  
A1IN6 HAS  H N N 42  
A1IN6 HAT  H N N 43  
A1IN6 HAV  H N N 44  
A1IN6 HAU  H N N 45  
A1IN6 HAL  H N N 46  
A1IN6 HAG  H N N 47  
A1IN6 HB7  H N N 48  
A1IN6 HB8  H N N 49  
A1IN6 HB5  H N N 50  
A1IN6 HB6  H N N 51  
A1IN6 HB3  H N N 52  
A1IN6 HB4  H N N 53  
A1IN6 HB2  H N N 54  
A1IN6 HB1  H N N 55  
A1IN6 HA   H N N 56  
A1IN6 HB9  H N N 57  
A1IN6 HAZ  H N N 58  
A1IN6 HCA  H N N 59  
A1IN6 HBA  H N N 60  
A1IN6 HCB  H N N 61  
A1IN6 HBB  H N N 62  
A1IN6 HCC  H N N 63  
A1IN6 HBC  H N N 64  
A1IN6 HCE  H N N 65  
A1IN6 HBE  H N N 66  
A1IN6 HCD  H N N 67  
A1IN6 HBD  H N N 68  
A1IN6 HCI  H N N 69  
A1IN6 HBI  H N N 70  
A1IN6 HCH  H N N 71  
A1IN6 HAA  H N N 72  
A1IN6 HAE  H N N 73  
A1IN6 HCG  H N N 74  
A1IN6 HBG  H N N 75  
A1IN6 HCF  H N N 76  
ALA   N    N N N 77  
ALA   CA   C N S 78  
ALA   C    C N N 79  
ALA   O    O N N 80  
ALA   CB   C N N 81  
ALA   OXT  O N N 82  
ALA   H    H N N 83  
ALA   H2   H N N 84  
ALA   HA   H N N 85  
ALA   HB1  H N N 86  
ALA   HB2  H N N 87  
ALA   HB3  H N N 88  
ALA   HXT  H N N 89  
ARG   N    N N N 90  
ARG   CA   C N S 91  
ARG   C    C N N 92  
ARG   O    O N N 93  
ARG   CB   C N N 94  
ARG   CG   C N N 95  
ARG   CD   C N N 96  
ARG   NE   N N N 97  
ARG   CZ   C N N 98  
ARG   NH1  N N N 99  
ARG   NH2  N N N 100 
ARG   OXT  O N N 101 
ARG   H    H N N 102 
ARG   H2   H N N 103 
ARG   HA   H N N 104 
ARG   HB2  H N N 105 
ARG   HB3  H N N 106 
ARG   HG2  H N N 107 
ARG   HG3  H N N 108 
ARG   HD2  H N N 109 
ARG   HD3  H N N 110 
ARG   HE   H N N 111 
ARG   HH11 H N N 112 
ARG   HH12 H N N 113 
ARG   HH21 H N N 114 
ARG   HH22 H N N 115 
ARG   HXT  H N N 116 
ASN   N    N N N 117 
ASN   CA   C N S 118 
ASN   C    C N N 119 
ASN   O    O N N 120 
ASN   CB   C N N 121 
ASN   CG   C N N 122 
ASN   OD1  O N N 123 
ASN   ND2  N N N 124 
ASN   OXT  O N N 125 
ASN   H    H N N 126 
ASN   H2   H N N 127 
ASN   HA   H N N 128 
ASN   HB2  H N N 129 
ASN   HB3  H N N 130 
ASN   HD21 H N N 131 
ASN   HD22 H N N 132 
ASN   HXT  H N N 133 
ASP   N    N N N 134 
ASP   CA   C N S 135 
ASP   C    C N N 136 
ASP   O    O N N 137 
ASP   CB   C N N 138 
ASP   CG   C N N 139 
ASP   OD1  O N N 140 
ASP   OD2  O N N 141 
ASP   OXT  O N N 142 
ASP   H    H N N 143 
ASP   H2   H N N 144 
ASP   HA   H N N 145 
ASP   HB2  H N N 146 
ASP   HB3  H N N 147 
ASP   HD2  H N N 148 
ASP   HXT  H N N 149 
CYS   N    N N N 150 
CYS   CA   C N R 151 
CYS   C    C N N 152 
CYS   O    O N N 153 
CYS   CB   C N N 154 
CYS   SG   S N N 155 
CYS   OXT  O N N 156 
CYS   H    H N N 157 
CYS   H2   H N N 158 
CYS   HA   H N N 159 
CYS   HB2  H N N 160 
CYS   HB3  H N N 161 
CYS   HG   H N N 162 
CYS   HXT  H N N 163 
GLN   N    N N N 164 
GLN   CA   C N S 165 
GLN   C    C N N 166 
GLN   O    O N N 167 
GLN   CB   C N N 168 
GLN   CG   C N N 169 
GLN   CD   C N N 170 
GLN   OE1  O N N 171 
GLN   NE2  N N N 172 
GLN   OXT  O N N 173 
GLN   H    H N N 174 
GLN   H2   H N N 175 
GLN   HA   H N N 176 
GLN   HB2  H N N 177 
GLN   HB3  H N N 178 
GLN   HG2  H N N 179 
GLN   HG3  H N N 180 
GLN   HE21 H N N 181 
GLN   HE22 H N N 182 
GLN   HXT  H N N 183 
GLU   N    N N N 184 
GLU   CA   C N S 185 
GLU   C    C N N 186 
GLU   O    O N N 187 
GLU   CB   C N N 188 
GLU   CG   C N N 189 
GLU   CD   C N N 190 
GLU   OE1  O N N 191 
GLU   OE2  O N N 192 
GLU   OXT  O N N 193 
GLU   H    H N N 194 
GLU   H2   H N N 195 
GLU   HA   H N N 196 
GLU   HB2  H N N 197 
GLU   HB3  H N N 198 
GLU   HG2  H N N 199 
GLU   HG3  H N N 200 
GLU   HE2  H N N 201 
GLU   HXT  H N N 202 
GLY   N    N N N 203 
GLY   CA   C N N 204 
GLY   C    C N N 205 
GLY   O    O N N 206 
GLY   OXT  O N N 207 
GLY   H    H N N 208 
GLY   H2   H N N 209 
GLY   HA2  H N N 210 
GLY   HA3  H N N 211 
GLY   HXT  H N N 212 
HIS   N    N N N 213 
HIS   CA   C N S 214 
HIS   C    C N N 215 
HIS   O    O N N 216 
HIS   CB   C N N 217 
HIS   CG   C Y N 218 
HIS   ND1  N Y N 219 
HIS   CD2  C Y N 220 
HIS   CE1  C Y N 221 
HIS   NE2  N Y N 222 
HIS   OXT  O N N 223 
HIS   H    H N N 224 
HIS   H2   H N N 225 
HIS   HA   H N N 226 
HIS   HB2  H N N 227 
HIS   HB3  H N N 228 
HIS   HD1  H N N 229 
HIS   HD2  H N N 230 
HIS   HE1  H N N 231 
HIS   HE2  H N N 232 
HIS   HXT  H N N 233 
HOH   O    O N N 234 
HOH   H1   H N N 235 
HOH   H2   H N N 236 
ILE   N    N N N 237 
ILE   CA   C N S 238 
ILE   C    C N N 239 
ILE   O    O N N 240 
ILE   CB   C N S 241 
ILE   CG1  C N N 242 
ILE   CG2  C N N 243 
ILE   CD1  C N N 244 
ILE   OXT  O N N 245 
ILE   H    H N N 246 
ILE   H2   H N N 247 
ILE   HA   H N N 248 
ILE   HB   H N N 249 
ILE   HG12 H N N 250 
ILE   HG13 H N N 251 
ILE   HG21 H N N 252 
ILE   HG22 H N N 253 
ILE   HG23 H N N 254 
ILE   HD11 H N N 255 
ILE   HD12 H N N 256 
ILE   HD13 H N N 257 
ILE   HXT  H N N 258 
LEU   N    N N N 259 
LEU   CA   C N S 260 
LEU   C    C N N 261 
LEU   O    O N N 262 
LEU   CB   C N N 263 
LEU   CG   C N N 264 
LEU   CD1  C N N 265 
LEU   CD2  C N N 266 
LEU   OXT  O N N 267 
LEU   H    H N N 268 
LEU   H2   H N N 269 
LEU   HA   H N N 270 
LEU   HB2  H N N 271 
LEU   HB3  H N N 272 
LEU   HG   H N N 273 
LEU   HD11 H N N 274 
LEU   HD12 H N N 275 
LEU   HD13 H N N 276 
LEU   HD21 H N N 277 
LEU   HD22 H N N 278 
LEU   HD23 H N N 279 
LEU   HXT  H N N 280 
LYS   N    N N N 281 
LYS   CA   C N S 282 
LYS   C    C N N 283 
LYS   O    O N N 284 
LYS   CB   C N N 285 
LYS   CG   C N N 286 
LYS   CD   C N N 287 
LYS   CE   C N N 288 
LYS   NZ   N N N 289 
LYS   OXT  O N N 290 
LYS   H    H N N 291 
LYS   H2   H N N 292 
LYS   HA   H N N 293 
LYS   HB2  H N N 294 
LYS   HB3  H N N 295 
LYS   HG2  H N N 296 
LYS   HG3  H N N 297 
LYS   HD2  H N N 298 
LYS   HD3  H N N 299 
LYS   HE2  H N N 300 
LYS   HE3  H N N 301 
LYS   HZ1  H N N 302 
LYS   HZ2  H N N 303 
LYS   HZ3  H N N 304 
LYS   HXT  H N N 305 
MET   N    N N N 306 
MET   CA   C N S 307 
MET   C    C N N 308 
MET   O    O N N 309 
MET   CB   C N N 310 
MET   CG   C N N 311 
MET   SD   S N N 312 
MET   CE   C N N 313 
MET   OXT  O N N 314 
MET   H    H N N 315 
MET   H2   H N N 316 
MET   HA   H N N 317 
MET   HB2  H N N 318 
MET   HB3  H N N 319 
MET   HG2  H N N 320 
MET   HG3  H N N 321 
MET   HE1  H N N 322 
MET   HE2  H N N 323 
MET   HE3  H N N 324 
MET   HXT  H N N 325 
PHE   N    N N N 326 
PHE   CA   C N S 327 
PHE   C    C N N 328 
PHE   O    O N N 329 
PHE   CB   C N N 330 
PHE   CG   C Y N 331 
PHE   CD1  C Y N 332 
PHE   CD2  C Y N 333 
PHE   CE1  C Y N 334 
PHE   CE2  C Y N 335 
PHE   CZ   C Y N 336 
PHE   OXT  O N N 337 
PHE   H    H N N 338 
PHE   H2   H N N 339 
PHE   HA   H N N 340 
PHE   HB2  H N N 341 
PHE   HB3  H N N 342 
PHE   HD1  H N N 343 
PHE   HD2  H N N 344 
PHE   HE1  H N N 345 
PHE   HE2  H N N 346 
PHE   HZ   H N N 347 
PHE   HXT  H N N 348 
PRO   N    N N N 349 
PRO   CA   C N S 350 
PRO   C    C N N 351 
PRO   O    O N N 352 
PRO   CB   C N N 353 
PRO   CG   C N N 354 
PRO   CD   C N N 355 
PRO   OXT  O N N 356 
PRO   H    H N N 357 
PRO   HA   H N N 358 
PRO   HB2  H N N 359 
PRO   HB3  H N N 360 
PRO   HG2  H N N 361 
PRO   HG3  H N N 362 
PRO   HD2  H N N 363 
PRO   HD3  H N N 364 
PRO   HXT  H N N 365 
SER   N    N N N 366 
SER   CA   C N S 367 
SER   C    C N N 368 
SER   O    O N N 369 
SER   CB   C N N 370 
SER   OG   O N N 371 
SER   OXT  O N N 372 
SER   H    H N N 373 
SER   H2   H N N 374 
SER   HA   H N N 375 
SER   HB2  H N N 376 
SER   HB3  H N N 377 
SER   HG   H N N 378 
SER   HXT  H N N 379 
THR   N    N N N 380 
THR   CA   C N S 381 
THR   C    C N N 382 
THR   O    O N N 383 
THR   CB   C N R 384 
THR   OG1  O N N 385 
THR   CG2  C N N 386 
THR   OXT  O N N 387 
THR   H    H N N 388 
THR   H2   H N N 389 
THR   HA   H N N 390 
THR   HB   H N N 391 
THR   HG1  H N N 392 
THR   HG21 H N N 393 
THR   HG22 H N N 394 
THR   HG23 H N N 395 
THR   HXT  H N N 396 
TRP   N    N N N 397 
TRP   CA   C N S 398 
TRP   C    C N N 399 
TRP   O    O N N 400 
TRP   CB   C N N 401 
TRP   CG   C Y N 402 
TRP   CD1  C Y N 403 
TRP   CD2  C Y N 404 
TRP   NE1  N Y N 405 
TRP   CE2  C Y N 406 
TRP   CE3  C Y N 407 
TRP   CZ2  C Y N 408 
TRP   CZ3  C Y N 409 
TRP   CH2  C Y N 410 
TRP   OXT  O N N 411 
TRP   H    H N N 412 
TRP   H2   H N N 413 
TRP   HA   H N N 414 
TRP   HB2  H N N 415 
TRP   HB3  H N N 416 
TRP   HD1  H N N 417 
TRP   HE1  H N N 418 
TRP   HE3  H N N 419 
TRP   HZ2  H N N 420 
TRP   HZ3  H N N 421 
TRP   HH2  H N N 422 
TRP   HXT  H N N 423 
TYR   N    N N N 424 
TYR   CA   C N S 425 
TYR   C    C N N 426 
TYR   O    O N N 427 
TYR   CB   C N N 428 
TYR   CG   C Y N 429 
TYR   CD1  C Y N 430 
TYR   CD2  C Y N 431 
TYR   CE1  C Y N 432 
TYR   CE2  C Y N 433 
TYR   CZ   C Y N 434 
TYR   OH   O N N 435 
TYR   OXT  O N N 436 
TYR   H    H N N 437 
TYR   H2   H N N 438 
TYR   HA   H N N 439 
TYR   HB2  H N N 440 
TYR   HB3  H N N 441 
TYR   HD1  H N N 442 
TYR   HD2  H N N 443 
TYR   HE1  H N N 444 
TYR   HE2  H N N 445 
TYR   HH   H N N 446 
TYR   HXT  H N N 447 
VAL   N    N N N 448 
VAL   CA   C N S 449 
VAL   C    C N N 450 
VAL   O    O N N 451 
VAL   CB   C N N 452 
VAL   CG1  C N N 453 
VAL   CG2  C N N 454 
VAL   OXT  O N N 455 
VAL   H    H N N 456 
VAL   H2   H N N 457 
VAL   HA   H N N 458 
VAL   HB   H N N 459 
VAL   HG11 H N N 460 
VAL   HG12 H N N 461 
VAL   HG13 H N N 462 
VAL   HG21 H N N 463 
VAL   HG22 H N N 464 
VAL   HG23 H N N 465 
VAL   HXT  H N N 466 
# 
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 
A1IN6 CBD OAI  sing N N 1   
A1IN6 CBD CBE  sing N N 2   
A1IN6 OAI CAC  sing N N 3   
A1IN6 CBE CBC  sing N N 4   
A1IN6 CBC CBB  sing N N 5   
A1IN6 OBF CBG  sing N N 6   
A1IN6 OBF CAD  sing N N 7   
A1IN6 CAC CAD  doub Y N 8   
A1IN6 CAC CAB  sing Y N 9   
A1IN6 OBH CBI  sing N N 10  
A1IN6 OBH CAB  sing N N 11  
A1IN6 CAD CAE  sing Y N 12  
A1IN6 CBB CBA  sing N N 13  
A1IN6 CAB CAA  doub Y N 14  
A1IN6 CBA CAZ  sing N N 15  
A1IN6 CAE CAF  doub Y N 16  
A1IN6 CAZ OAY  sing N N 17  
A1IN6 CAA CAF  sing Y N 18  
A1IN6 CAF CAG  sing N N 19  
A1IN6 OAY C    sing N N 20  
A1IN6 CAM CAN  sing N N 21  
A1IN6 CAM CAL  sing N N 22  
A1IN6 CAN CAO  sing N N 23  
A1IN6 CAG CAL  sing N N 24  
A1IN6 CAG CAH  sing N N 25  
A1IN6 C   O    doub N N 26  
A1IN6 C   CA   sing N N 27  
A1IN6 CAL CAQ  sing N N 28  
A1IN6 CAV N    sing N N 29  
A1IN6 CAV CAU  sing N N 30  
A1IN6 CAH OAK  doub N N 31  
A1IN6 CAH N    sing N N 32  
A1IN6 N   CA   sing N N 33  
A1IN6 CA  CB   sing N N 34  
A1IN6 CAO CAP  sing N N 35  
A1IN6 CAU CAT  sing N N 36  
A1IN6 CAT CB   sing N N 37  
A1IN6 CAQ CAP  sing N N 38  
A1IN6 CAM HAM  sing N N 39  
A1IN6 CAM HAN  sing N N 40  
A1IN6 CAN HAO  sing N N 41  
A1IN6 CAN HAP  sing N N 42  
A1IN6 CAO HAQ  sing N N 43  
A1IN6 CAO HAR  sing N N 44  
A1IN6 CAP HAS  sing N N 45  
A1IN6 CAP HAT  sing N N 46  
A1IN6 CAQ HAV  sing N N 47  
A1IN6 CAQ HAU  sing N N 48  
A1IN6 CAL HAL  sing N N 49  
A1IN6 CAG HAG  sing N N 50  
A1IN6 CAV HB7  sing N N 51  
A1IN6 CAV HB8  sing N N 52  
A1IN6 CAU HB5  sing N N 53  
A1IN6 CAU HB6  sing N N 54  
A1IN6 CAT HB3  sing N N 55  
A1IN6 CAT HB4  sing N N 56  
A1IN6 CB  HB2  sing N N 57  
A1IN6 CB  HB1  sing N N 58  
A1IN6 CA  HA   sing N N 59  
A1IN6 CAZ HB9  sing N N 60  
A1IN6 CAZ HAZ  sing N N 61  
A1IN6 CBA HCA  sing N N 62  
A1IN6 CBA HBA  sing N N 63  
A1IN6 CBB HCB  sing N N 64  
A1IN6 CBB HBB  sing N N 65  
A1IN6 CBC HCC  sing N N 66  
A1IN6 CBC HBC  sing N N 67  
A1IN6 CBE HCE  sing N N 68  
A1IN6 CBE HBE  sing N N 69  
A1IN6 CBD HCD  sing N N 70  
A1IN6 CBD HBD  sing N N 71  
A1IN6 CBI HCI  sing N N 72  
A1IN6 CBI HBI  sing N N 73  
A1IN6 CBI HCH  sing N N 74  
A1IN6 CAA HAA  sing N N 75  
A1IN6 CAE HAE  sing N N 76  
A1IN6 CBG HCG  sing N N 77  
A1IN6 CBG HBG  sing N N 78  
A1IN6 CBG HCF  sing N N 79  
ALA   N   CA   sing N N 80  
ALA   N   H    sing N N 81  
ALA   N   H2   sing N N 82  
ALA   CA  C    sing N N 83  
ALA   CA  CB   sing N N 84  
ALA   CA  HA   sing N N 85  
ALA   C   O    doub N N 86  
ALA   C   OXT  sing N N 87  
ALA   CB  HB1  sing N N 88  
ALA   CB  HB2  sing N N 89  
ALA   CB  HB3  sing N N 90  
ALA   OXT HXT  sing N N 91  
ARG   N   CA   sing N N 92  
ARG   N   H    sing N N 93  
ARG   N   H2   sing N N 94  
ARG   CA  C    sing N N 95  
ARG   CA  CB   sing N N 96  
ARG   CA  HA   sing N N 97  
ARG   C   O    doub N N 98  
ARG   C   OXT  sing N N 99  
ARG   CB  CG   sing N N 100 
ARG   CB  HB2  sing N N 101 
ARG   CB  HB3  sing N N 102 
ARG   CG  CD   sing N N 103 
ARG   CG  HG2  sing N N 104 
ARG   CG  HG3  sing N N 105 
ARG   CD  NE   sing N N 106 
ARG   CD  HD2  sing N N 107 
ARG   CD  HD3  sing N N 108 
ARG   NE  CZ   sing N N 109 
ARG   NE  HE   sing N N 110 
ARG   CZ  NH1  sing N N 111 
ARG   CZ  NH2  doub N N 112 
ARG   NH1 HH11 sing N N 113 
ARG   NH1 HH12 sing N N 114 
ARG   NH2 HH21 sing N N 115 
ARG   NH2 HH22 sing N N 116 
ARG   OXT HXT  sing N N 117 
ASN   N   CA   sing N N 118 
ASN   N   H    sing N N 119 
ASN   N   H2   sing N N 120 
ASN   CA  C    sing N N 121 
ASN   CA  CB   sing N N 122 
ASN   CA  HA   sing N N 123 
ASN   C   O    doub N N 124 
ASN   C   OXT  sing N N 125 
ASN   CB  CG   sing N N 126 
ASN   CB  HB2  sing N N 127 
ASN   CB  HB3  sing N N 128 
ASN   CG  OD1  doub N N 129 
ASN   CG  ND2  sing N N 130 
ASN   ND2 HD21 sing N N 131 
ASN   ND2 HD22 sing N N 132 
ASN   OXT HXT  sing N N 133 
ASP   N   CA   sing N N 134 
ASP   N   H    sing N N 135 
ASP   N   H2   sing N N 136 
ASP   CA  C    sing N N 137 
ASP   CA  CB   sing N N 138 
ASP   CA  HA   sing N N 139 
ASP   C   O    doub N N 140 
ASP   C   OXT  sing N N 141 
ASP   CB  CG   sing N N 142 
ASP   CB  HB2  sing N N 143 
ASP   CB  HB3  sing N N 144 
ASP   CG  OD1  doub N N 145 
ASP   CG  OD2  sing N N 146 
ASP   OD2 HD2  sing N N 147 
ASP   OXT HXT  sing N N 148 
CYS   N   CA   sing N N 149 
CYS   N   H    sing N N 150 
CYS   N   H2   sing N N 151 
CYS   CA  C    sing N N 152 
CYS   CA  CB   sing N N 153 
CYS   CA  HA   sing N N 154 
CYS   C   O    doub N N 155 
CYS   C   OXT  sing N N 156 
CYS   CB  SG   sing N N 157 
CYS   CB  HB2  sing N N 158 
CYS   CB  HB3  sing N N 159 
CYS   SG  HG   sing N N 160 
CYS   OXT HXT  sing N N 161 
GLN   N   CA   sing N N 162 
GLN   N   H    sing N N 163 
GLN   N   H2   sing N N 164 
GLN   CA  C    sing N N 165 
GLN   CA  CB   sing N N 166 
GLN   CA  HA   sing N N 167 
GLN   C   O    doub N N 168 
GLN   C   OXT  sing N N 169 
GLN   CB  CG   sing N N 170 
GLN   CB  HB2  sing N N 171 
GLN   CB  HB3  sing N N 172 
GLN   CG  CD   sing N N 173 
GLN   CG  HG2  sing N N 174 
GLN   CG  HG3  sing N N 175 
GLN   CD  OE1  doub N N 176 
GLN   CD  NE2  sing N N 177 
GLN   NE2 HE21 sing N N 178 
GLN   NE2 HE22 sing N N 179 
GLN   OXT HXT  sing N N 180 
GLU   N   CA   sing N N 181 
GLU   N   H    sing N N 182 
GLU   N   H2   sing N N 183 
GLU   CA  C    sing N N 184 
GLU   CA  CB   sing N N 185 
GLU   CA  HA   sing N N 186 
GLU   C   O    doub N N 187 
GLU   C   OXT  sing N N 188 
GLU   CB  CG   sing N N 189 
GLU   CB  HB2  sing N N 190 
GLU   CB  HB3  sing N N 191 
GLU   CG  CD   sing N N 192 
GLU   CG  HG2  sing N N 193 
GLU   CG  HG3  sing N N 194 
GLU   CD  OE1  doub N N 195 
GLU   CD  OE2  sing N N 196 
GLU   OE2 HE2  sing N N 197 
GLU   OXT HXT  sing N N 198 
GLY   N   CA   sing N N 199 
GLY   N   H    sing N N 200 
GLY   N   H2   sing N N 201 
GLY   CA  C    sing N N 202 
GLY   CA  HA2  sing N N 203 
GLY   CA  HA3  sing N N 204 
GLY   C   O    doub N N 205 
GLY   C   OXT  sing N N 206 
GLY   OXT HXT  sing N N 207 
HIS   N   CA   sing N N 208 
HIS   N   H    sing N N 209 
HIS   N   H2   sing N N 210 
HIS   CA  C    sing N N 211 
HIS   CA  CB   sing N N 212 
HIS   CA  HA   sing N N 213 
HIS   C   O    doub N N 214 
HIS   C   OXT  sing N N 215 
HIS   CB  CG   sing N N 216 
HIS   CB  HB2  sing N N 217 
HIS   CB  HB3  sing N N 218 
HIS   CG  ND1  sing Y N 219 
HIS   CG  CD2  doub Y N 220 
HIS   ND1 CE1  doub Y N 221 
HIS   ND1 HD1  sing N N 222 
HIS   CD2 NE2  sing Y N 223 
HIS   CD2 HD2  sing N N 224 
HIS   CE1 NE2  sing Y N 225 
HIS   CE1 HE1  sing N N 226 
HIS   NE2 HE2  sing N N 227 
HIS   OXT HXT  sing N N 228 
HOH   O   H1   sing N N 229 
HOH   O   H2   sing N N 230 
ILE   N   CA   sing N N 231 
ILE   N   H    sing N N 232 
ILE   N   H2   sing N N 233 
ILE   CA  C    sing N N 234 
ILE   CA  CB   sing N N 235 
ILE   CA  HA   sing N N 236 
ILE   C   O    doub N N 237 
ILE   C   OXT  sing N N 238 
ILE   CB  CG1  sing N N 239 
ILE   CB  CG2  sing N N 240 
ILE   CB  HB   sing N N 241 
ILE   CG1 CD1  sing N N 242 
ILE   CG1 HG12 sing N N 243 
ILE   CG1 HG13 sing N N 244 
ILE   CG2 HG21 sing N N 245 
ILE   CG2 HG22 sing N N 246 
ILE   CG2 HG23 sing N N 247 
ILE   CD1 HD11 sing N N 248 
ILE   CD1 HD12 sing N N 249 
ILE   CD1 HD13 sing N N 250 
ILE   OXT HXT  sing N N 251 
LEU   N   CA   sing N N 252 
LEU   N   H    sing N N 253 
LEU   N   H2   sing N N 254 
LEU   CA  C    sing N N 255 
LEU   CA  CB   sing N N 256 
LEU   CA  HA   sing N N 257 
LEU   C   O    doub N N 258 
LEU   C   OXT  sing N N 259 
LEU   CB  CG   sing N N 260 
LEU   CB  HB2  sing N N 261 
LEU   CB  HB3  sing N N 262 
LEU   CG  CD1  sing N N 263 
LEU   CG  CD2  sing N N 264 
LEU   CG  HG   sing N N 265 
LEU   CD1 HD11 sing N N 266 
LEU   CD1 HD12 sing N N 267 
LEU   CD1 HD13 sing N N 268 
LEU   CD2 HD21 sing N N 269 
LEU   CD2 HD22 sing N N 270 
LEU   CD2 HD23 sing N N 271 
LEU   OXT HXT  sing N N 272 
LYS   N   CA   sing N N 273 
LYS   N   H    sing N N 274 
LYS   N   H2   sing N N 275 
LYS   CA  C    sing N N 276 
LYS   CA  CB   sing N N 277 
LYS   CA  HA   sing N N 278 
LYS   C   O    doub N N 279 
LYS   C   OXT  sing N N 280 
LYS   CB  CG   sing N N 281 
LYS   CB  HB2  sing N N 282 
LYS   CB  HB3  sing N N 283 
LYS   CG  CD   sing N N 284 
LYS   CG  HG2  sing N N 285 
LYS   CG  HG3  sing N N 286 
LYS   CD  CE   sing N N 287 
LYS   CD  HD2  sing N N 288 
LYS   CD  HD3  sing N N 289 
LYS   CE  NZ   sing N N 290 
LYS   CE  HE2  sing N N 291 
LYS   CE  HE3  sing N N 292 
LYS   NZ  HZ1  sing N N 293 
LYS   NZ  HZ2  sing N N 294 
LYS   NZ  HZ3  sing N N 295 
LYS   OXT HXT  sing N N 296 
MET   N   CA   sing N N 297 
MET   N   H    sing N N 298 
MET   N   H2   sing N N 299 
MET   CA  C    sing N N 300 
MET   CA  CB   sing N N 301 
MET   CA  HA   sing N N 302 
MET   C   O    doub N N 303 
MET   C   OXT  sing N N 304 
MET   CB  CG   sing N N 305 
MET   CB  HB2  sing N N 306 
MET   CB  HB3  sing N N 307 
MET   CG  SD   sing N N 308 
MET   CG  HG2  sing N N 309 
MET   CG  HG3  sing N N 310 
MET   SD  CE   sing N N 311 
MET   CE  HE1  sing N N 312 
MET   CE  HE2  sing N N 313 
MET   CE  HE3  sing N N 314 
MET   OXT HXT  sing N N 315 
PHE   N   CA   sing N N 316 
PHE   N   H    sing N N 317 
PHE   N   H2   sing N N 318 
PHE   CA  C    sing N N 319 
PHE   CA  CB   sing N N 320 
PHE   CA  HA   sing N N 321 
PHE   C   O    doub N N 322 
PHE   C   OXT  sing N N 323 
PHE   CB  CG   sing N N 324 
PHE   CB  HB2  sing N N 325 
PHE   CB  HB3  sing N N 326 
PHE   CG  CD1  doub Y N 327 
PHE   CG  CD2  sing Y N 328 
PHE   CD1 CE1  sing Y N 329 
PHE   CD1 HD1  sing N N 330 
PHE   CD2 CE2  doub Y N 331 
PHE   CD2 HD2  sing N N 332 
PHE   CE1 CZ   doub Y N 333 
PHE   CE1 HE1  sing N N 334 
PHE   CE2 CZ   sing Y N 335 
PHE   CE2 HE2  sing N N 336 
PHE   CZ  HZ   sing N N 337 
PHE   OXT HXT  sing N N 338 
PRO   N   CA   sing N N 339 
PRO   N   CD   sing N N 340 
PRO   N   H    sing N N 341 
PRO   CA  C    sing N N 342 
PRO   CA  CB   sing N N 343 
PRO   CA  HA   sing N N 344 
PRO   C   O    doub N N 345 
PRO   C   OXT  sing N N 346 
PRO   CB  CG   sing N N 347 
PRO   CB  HB2  sing N N 348 
PRO   CB  HB3  sing N N 349 
PRO   CG  CD   sing N N 350 
PRO   CG  HG2  sing N N 351 
PRO   CG  HG3  sing N N 352 
PRO   CD  HD2  sing N N 353 
PRO   CD  HD3  sing N N 354 
PRO   OXT HXT  sing N N 355 
SER   N   CA   sing N N 356 
SER   N   H    sing N N 357 
SER   N   H2   sing N N 358 
SER   CA  C    sing N N 359 
SER   CA  CB   sing N N 360 
SER   CA  HA   sing N N 361 
SER   C   O    doub N N 362 
SER   C   OXT  sing N N 363 
SER   CB  OG   sing N N 364 
SER   CB  HB2  sing N N 365 
SER   CB  HB3  sing N N 366 
SER   OG  HG   sing N N 367 
SER   OXT HXT  sing N N 368 
THR   N   CA   sing N N 369 
THR   N   H    sing N N 370 
THR   N   H2   sing N N 371 
THR   CA  C    sing N N 372 
THR   CA  CB   sing N N 373 
THR   CA  HA   sing N N 374 
THR   C   O    doub N N 375 
THR   C   OXT  sing N N 376 
THR   CB  OG1  sing N N 377 
THR   CB  CG2  sing N N 378 
THR   CB  HB   sing N N 379 
THR   OG1 HG1  sing N N 380 
THR   CG2 HG21 sing N N 381 
THR   CG2 HG22 sing N N 382 
THR   CG2 HG23 sing N N 383 
THR   OXT HXT  sing N N 384 
TRP   N   CA   sing N N 385 
TRP   N   H    sing N N 386 
TRP   N   H2   sing N N 387 
TRP   CA  C    sing N N 388 
TRP   CA  CB   sing N N 389 
TRP   CA  HA   sing N N 390 
TRP   C   O    doub N N 391 
TRP   C   OXT  sing N N 392 
TRP   CB  CG   sing N N 393 
TRP   CB  HB2  sing N N 394 
TRP   CB  HB3  sing N N 395 
TRP   CG  CD1  doub Y N 396 
TRP   CG  CD2  sing Y N 397 
TRP   CD1 NE1  sing Y N 398 
TRP   CD1 HD1  sing N N 399 
TRP   CD2 CE2  doub Y N 400 
TRP   CD2 CE3  sing Y N 401 
TRP   NE1 CE2  sing Y N 402 
TRP   NE1 HE1  sing N N 403 
TRP   CE2 CZ2  sing Y N 404 
TRP   CE3 CZ3  doub Y N 405 
TRP   CE3 HE3  sing N N 406 
TRP   CZ2 CH2  doub Y N 407 
TRP   CZ2 HZ2  sing N N 408 
TRP   CZ3 CH2  sing Y N 409 
TRP   CZ3 HZ3  sing N N 410 
TRP   CH2 HH2  sing N N 411 
TRP   OXT HXT  sing N N 412 
TYR   N   CA   sing N N 413 
TYR   N   H    sing N N 414 
TYR   N   H2   sing N N 415 
TYR   CA  C    sing N N 416 
TYR   CA  CB   sing N N 417 
TYR   CA  HA   sing N N 418 
TYR   C   O    doub N N 419 
TYR   C   OXT  sing N N 420 
TYR   CB  CG   sing N N 421 
TYR   CB  HB2  sing N N 422 
TYR   CB  HB3  sing N N 423 
TYR   CG  CD1  doub Y N 424 
TYR   CG  CD2  sing Y N 425 
TYR   CD1 CE1  sing Y N 426 
TYR   CD1 HD1  sing N N 427 
TYR   CD2 CE2  doub Y N 428 
TYR   CD2 HD2  sing N N 429 
TYR   CE1 CZ   doub Y N 430 
TYR   CE1 HE1  sing N N 431 
TYR   CE2 CZ   sing Y N 432 
TYR   CE2 HE2  sing N N 433 
TYR   CZ  OH   sing N N 434 
TYR   OH  HH   sing N N 435 
TYR   OXT HXT  sing N N 436 
VAL   N   CA   sing N N 437 
VAL   N   H    sing N N 438 
VAL   N   H2   sing N N 439 
VAL   CA  C    sing N N 440 
VAL   CA  CB   sing N N 441 
VAL   CA  HA   sing N N 442 
VAL   C   O    doub N N 443 
VAL   C   OXT  sing N N 444 
VAL   CB  CG1  sing N N 445 
VAL   CB  CG2  sing N N 446 
VAL   CB  HB   sing N N 447 
VAL   CG1 HG11 sing N N 448 
VAL   CG1 HG12 sing N N 449 
VAL   CG1 HG13 sing N N 450 
VAL   CG2 HG21 sing N N 451 
VAL   CG2 HG22 sing N N 452 
VAL   CG2 HG23 sing N N 453 
VAL   OXT HXT  sing N N 454 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'German Federal Ministry for Education and Research' Germany 03VP08671 1 
'German Research Foundation (DFG)'                   Germany 525512762 2 
# 
_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   4TW7 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GQ8 
_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]   0.020644 
_atom_sites.fract_transf_matrix[1][2]   0.011919 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023838 
_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]   0.005202 
_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.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C 6  6  2.3103  20.8439 1.0201 10.2075 1.5888 0.5687  0.8651 51.6512 0.2156   
H 1  1  0.4930  10.5109 0.3229 26.1257 0.1402 3.1424  0.0408 57.7997 0.0030   
N 7  7  12.2220 0.0057  3.1346 9.8933  2.0141 28.9975 1.1672 0.5826  -11.5379 
O 8  8  3.0487  13.2771 2.2870 5.7011  1.5464 0.3239  0.8671 32.9089 0.2508   
S 16 16 6.9054  1.4679  5.2035 22.2151 1.4379 0.2536  1.5863 56.1720 1.0316   
# 
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_site.calc_flag 
_atom_site.pdbx_tls_group_id 
ATOM   1    N N    . GLY   A 1 1   ? 15.929 15.945  -6.589  1 65.978  ? 13  GLY   B N    1 ? 1 
ATOM   2    C CA   . GLY   A 1 1   ? 16.846 15.308  -5.624  1 65.881  ? 13  GLY   B CA   1 ? 1 
ATOM   3    C C    . GLY   A 1 1   ? 16.964 13.803  -5.877  1 65.354  ? 13  GLY   B C    1 ? 1 
ATOM   4    O O    . GLY   A 1 1   ? 16.296 13.258  -6.748  1 71.536  ? 13  GLY   B O    1 ? 1 
ATOM   5    H H1   . GLY   A 1 1   ? 15.827 16.821  -6.386  1 68.288  ? 13  GLY   B H1   1 c 1 
ATOM   6    H H2   . GLY   A 1 1   ? 15.12  15.54   -6.561  1 65.516  ? 13  GLY   B H2   1 c 1 
ATOM   7    H H3   . GLY   A 1 1   ? 16.264 15.874  -7.426  1 68.879  ? 13  GLY   B H3   1 c 1 
ATOM   8    H HA2  . GLY   A 1 1   ? 17.735 15.725  -5.698  1 67.385  ? 13  GLY   B HA2  1 c 1 
ATOM   9    H HA3  . GLY   A 1 1   ? 16.511 15.464  -4.71   1 63.833  ? 13  GLY   B HA3  1 c 1 
ATOM   10   N N    . ALA   A 1 2   ? 17.825 13.131  -5.113  1 62.665  ? 14  ALA   B N    1 ? 1 
ATOM   11   C CA   . ALA   A 1 2   ? 18.022 11.703  -5.263  1 64.171  ? 14  ALA   B CA   1 ? 1 
ATOM   12   C C    . ALA   A 1 2   ? 16.734 10.927  -4.968  1 61.874  ? 14  ALA   B C    1 ? 1 
ATOM   13   O O    . ALA   A 1 2   ? 16.42  9.992   -5.695  1 64.607  ? 14  ALA   B O    1 ? 1 
ATOM   14   C CB   . ALA   A 1 2   ? 19.164 11.236  -4.377  1 64.715  ? 14  ALA   B CB   1 ? 1 
ATOM   15   H H    . ALA   A 1 2   ? 18.307 13.579  -4.478  1 63.628  ? 14  ALA   B H    1 c 1 
ATOM   16   H HA   . ALA   A 1 2   ? 18.269 11.53   -6.214  1 65.831  ? 14  ALA   B HA   1 c 1 
ATOM   17   H HB1  . ALA   A 1 2   ? 19.99  11.669  -4.651  1 66.274  ? 14  ALA   B HB1  1 c 1 
ATOM   18   H HB2  . ALA   A 1 2   ? 18.976 11.463  -3.451  1 62.601  ? 14  ALA   B HB2  1 c 1 
ATOM   19   H HB3  . ALA   A 1 2   ? 19.266 10.272  -4.456  1 62.703  ? 14  ALA   B HB3  1 c 1 
ATOM   20   N N    . PRO   A 1 3   ? 15.959 11.231  -3.898  1 58.411  ? 15  PRO   B N    1 ? 1 
ATOM   21   C CA   . PRO   A 1 3   ? 14.723 10.485  -3.636  1 55.992  ? 15  PRO   B CA   1 ? 1 
ATOM   22   C C    . PRO   A 1 3   ? 13.676 10.611  -4.74   1 59.585  ? 15  PRO   B C    1 ? 1 
ATOM   23   O O    . PRO   A 1 3   ? 12.893 9.687   -4.957  1 63.445  ? 15  PRO   B O    1 ? 1 
ATOM   24   C CB   . PRO   A 1 3   ? 14.148 11.062  -2.338  1 51.861  ? 15  PRO   B CB   1 ? 1 
ATOM   25   C CG   . PRO   A 1 3   ? 15.098 12.181  -1.922  1 51.191  ? 15  PRO   B CG   1 ? 1 
ATOM   26   C CD   . PRO   A 1 3   ? 16.238 12.286  -2.909  1 55.856  ? 15  PRO   B CD   1 ? 1 
ATOM   27   H HA   . PRO   A 1 3   ? 14.94  9.539   -3.502  1 54.316  ? 15  PRO   B HA   1 c 1 
ATOM   28   H HB2  . PRO   A 1 3   ? 13.247 11.411  -2.482  1 52.763  ? 15  PRO   B HB2  1 c 1 
ATOM   29   H HB3  . PRO   A 1 3   ? 14.103 10.373  -1.646  1 49.945  ? 15  PRO   B HB3  1 c 1 
ATOM   30   H HG2  . PRO   A 1 3   ? 14.615 13.031  -1.887  1 53.475  ? 15  PRO   B HG2  1 c 1 
ATOM   31   H HG3  . PRO   A 1 3   ? 15.453 12.001  -1.029  1 50.826  ? 15  PRO   B HG3  1 c 1 
ATOM   32   H HD2  . PRO   A 1 3   ? 16.248 13.163  -3.333  1 58.194  ? 15  PRO   B HD2  1 c 1 
ATOM   33   H HD3  . PRO   A 1 3   ? 17.097 12.13   -2.472  1 55.523  ? 15  PRO   B HD3  1 c 1 
ATOM   34   N N    . ALA   A 1 4   ? 13.643 11.765  -5.414  1 59.986  ? 16  ALA   B N    1 ? 1 
ATOM   35   C CA   . ALA   A 1 4   ? 12.77  11.94   -6.565  1 62.417  ? 16  ALA   B CA   1 ? 1 
ATOM   36   C C    . ALA   A 1 4   ? 13.107 10.914  -7.639  1 62.142  ? 16  ALA   B C    1 ? 1 
ATOM   37   O O    . ALA   A 1 4   ? 12.239 10.183  -8.107  1 64.467  ? 16  ALA   B O    1 ? 1 
ATOM   38   C CB   . ALA   A 1 4   ? 12.905 13.342  -7.117  1 63.543  ? 16  ALA   B CB   1 ? 1 
ATOM   39   H H    . ALA   A 1 4   ? 14.171 12.463  -5.149  1 61.136  ? 16  ALA   B H    1 c 1 
ATOM   40   H HA   . ALA   A 1 4   ? 11.829 11.791  -6.271  1 61.113  ? 16  ALA   B HA   1 c 1 
ATOM   41   H HB1  . ALA   A 1 4   ? 12.642 13.987  -6.439  1 63.855  ? 16  ALA   B HB1  1 c 1 
ATOM   42   H HB2  . ALA   A 1 4   ? 13.826 13.507  -7.376  1 65.274  ? 16  ALA   B HB2  1 c 1 
ATOM   43   H HB3  . ALA   A 1 4   ? 12.33  13.443  -7.895  1 66.525  ? 16  ALA   B HB3  1 c 1 
ATOM   44   N N    . THR   A 1 5   ? 14.382 10.923  -8.042  1 63.936  ? 17  THR   B N    1 ? 1 
ATOM   45   C CA   . THR   A 1 5   ? 14.96  9.971   -8.983  1 64.074  ? 17  THR   B CA   1 ? 1 
ATOM   46   C C    . THR   A 1 5   ? 14.61  8.523   -8.603  1 60.597  ? 17  THR   B C    1 ? 1 
ATOM   47   O O    . THR   A 1 5   ? 14.355 7.717   -9.499  1 57.611  ? 17  THR   B O    1 ? 1 
ATOM   48   C CB   . THR   A 1 5   ? 16.467 10.239  -8.989  1 66.764  ? 17  THR   B CB   1 ? 1 
ATOM   49   O OG1  . THR   A 1 5   ? 16.58  11.585  -9.452  1 69.62   ? 17  THR   B OG1  1 ? 1 
ATOM   50   C CG2  . THR   A 1 5   ? 17.257 9.28    -9.866  1 67.897  ? 17  THR   B CG2  1 ? 1 
ATOM   51   H H    . THR   A 1 5   ? 14.931 11.571  -7.704  1 63.741  ? 17  THR   B H    1 c 1 
ATOM   52   H HA   . THR   A 1 5   ? 14.603 10.161  -9.877  1 67.32   ? 17  THR   B HA   1 c 1 
ATOM   53   H HB   . THR   A 1 5   ? 16.816 10.184  -8.068  1 63.884  ? 17  THR   B HB   1 c 1 
ATOM   54   H HG1  . THR   A 1 5   ? 16.307 11.692  -10.19  0 30      ? 17  THR   B HG1  1 c 1 
ATOM   55   H HG21 . THR   A 1 5   ? 18.187 9.559   -9.896  1 69.096  ? 17  THR   B HG21 1 c 1 
ATOM   56   H HG22 . THR   A 1 5   ? 16.889 9.285   -10.766 1 70.551  ? 17  THR   B HG22 1 c 1 
ATOM   57   H HG23 . THR   A 1 5   ? 17.202 8.381   -9.499  1 65.727  ? 17  THR   B HG23 1 c 1 
ATOM   58   N N    . VAL   A 1 6   ? 14.591 8.192   -7.288  1 54.017  ? 18  VAL   B N    1 ? 1 
ATOM   59   C CA   . VAL   A 1 6   ? 14.209 6.856   -6.847  1 50.313  ? 18  VAL   B CA   1 ? 1 
ATOM   60   C C    . VAL   A 1 6   ? 12.713 6.604   -7.05   1 51.783  ? 18  VAL   B C    1 ? 1 
ATOM   61   O O    . VAL   A 1 6   ? 12.332 5.514   -7.501  1 49.344  ? 18  VAL   B O    1 ? 1 
ATOM   62   C CB   . VAL   A 1 6   ? 14.561 6.493   -5.4    1 45.571  ? 18  VAL   B CB   1 ? 1 
ATOM   63   C CG1  . VAL   A 1 6   ? 14.207 5.032   -5.11   1 40.282  ? 18  VAL   B CG1  1 ? 1 
ATOM   64   C CG2  . VAL   A 1 6   ? 16.037 6.754   -5.105  1 47.731  ? 18  VAL   B CG2  1 ? 1 
ATOM   65   H H    . VAL   A 1 6   ? 14.827 8.814   -6.661  1 53.705  ? 18  VAL   B H    1 c 1 
ATOM   66   H HA   . VAL   A 1 6   ? 14.686 6.224   -7.42   1 51.301  ? 18  VAL   B HA   1 c 1 
ATOM   67   H HB   . VAL   A 1 6   ? 14.019 7.068   -4.811  1 44.824  ? 18  VAL   B HB   1 c 1 
ATOM   68   H HG11 . VAL   A 1 6   ? 14.565 4.465   -5.814  1 42.383  ? 18  VAL   B HG11 1 c 1 
ATOM   69   H HG12 . VAL   A 1 6   ? 13.242 4.932   -5.073  1 41.341  ? 18  VAL   B HG12 1 c 1 
ATOM   70   H HG13 . VAL   A 1 6   ? 14.591 4.769   -4.257  1 39.402  ? 18  VAL   B HG13 1 c 1 
ATOM   71   H HG21 . VAL   A 1 6   ? 16.25  6.437   -4.211  1 45.053  ? 18  VAL   B HG21 1 c 1 
ATOM   72   H HG22 . VAL   A 1 6   ? 16.216 7.705   -5.159  1 48.325  ? 18  VAL   B HG22 1 c 1 
ATOM   73   H HG23 . VAL   A 1 6   ? 16.586 6.284   -5.753  1 48.18   ? 18  VAL   B HG23 1 c 1 
ATOM   74   N N    . THR   A 1 7   ? 11.872 7.575   -6.662  1 52.902  ? 19  THR   B N    1 ? 1 
ATOM   75   C CA   . THR   A 1 7   ? 10.436 7.489   -6.896  1 55.95   ? 19  THR   B CA   1 ? 1 
ATOM   76   C C    . THR   A 1 7   ? 10.165 7.369   -8.401  1 62.837  ? 19  THR   B C    1 ? 1 
ATOM   77   O O    . THR   A 1 7   ? 9.186  6.747   -8.771  1 68.192  ? 19  THR   B O    1 ? 1 
ATOM   78   C CB   . THR   A 1 7   ? 9.721  8.672   -6.222  1 57.537  ? 19  THR   B CB   1 ? 1 
ATOM   79   O OG1  . THR   A 1 7   ? 9.391  8.346   -4.867  1 53.763  ? 19  THR   B OG1  1 ? 1 
ATOM   80   C CG2  . THR   A 1 7   ? 8.413  9.092   -6.879  1 59.363  ? 19  THR   B CG2  1 ? 1 
ATOM   81   H H    . THR   A 1 7   ? 12.206 8.309   -6.232  1 52.725  ? 19  THR   B H    1 c 1 
ATOM   82   H HA   . THR   A 1 7   ? 10.116 6.666   -6.467  1 54.819  ? 19  THR   B HA   1 c 1 
ATOM   83   H HB   . THR   A 1 7   ? 10.324 9.453   -6.224  1 57.281  ? 19  THR   B HB   1 c 1 
ATOM   84   H HG1  . THR   A 1 7   ? 8.68   7.562   -4.919  0 30      ? 19  THR   B HG1  1 c 1 
ATOM   85   H HG21 . THR   A 1 7   ? 7.954  9.731   -6.308  1 59.591  ? 19  THR   B HG21 1 c 1 
ATOM   86   H HG22 . THR   A 1 7   ? 7.847  8.312   -7.009  1 59.94   ? 19  THR   B HG22 1 c 1 
ATOM   87   H HG23 . THR   A 1 7   ? 8.597  9.505   -7.739  1 62.268  ? 19  THR   B HG23 1 c 1 
ATOM   88   N N    . GLU   A 1 8   ? 11.072 7.858   -9.257  1 66.65   ? 20  GLU   B N    1 ? 1 
ATOM   89   C CA   . GLU   A 1 8   ? 10.813 7.931   -10.692 1 76.298  ? 20  GLU   B CA   1 ? 1 
ATOM   90   C C    . GLU   A 1 8   ? 11.348 6.679   -11.391 1 78.261  ? 20  GLU   B C    1 ? 1 
ATOM   91   O O    . GLU   A 1 8   ? 10.634 6.074   -12.176 1 79.474  ? 20  GLU   B O    1 ? 1 
ATOM   92   C CB   . GLU   A 1 8   ? 11.369 9.217   -11.314 1 74.915  ? 20  GLU   B CB   1 ? 1 
ATOM   93   H H    . GLU   A 1 8   ? 11.869 8.17    -8.94   1 66.151  ? 20  GLU   B H    1 c 1 
ATOM   94   H HA   . GLU   A 1 8   ? 9.831  7.952   -10.821 1 75.781  ? 20  GLU   B HA   1 c 1 
ATOM   95   H HB2  . GLU   A 1 8   ? 12.295 9.274   -11.244 0 30      ? 20  GLU   B HB2  1 c 1 
ATOM   96   H HB3  . GLU   A 1 8   ? 10.53  9.799   -11.487 0 30      ? 20  GLU   B HB3  1 c 1 
ATOM   97   N N    . GLN   A 1 9   ? 12.602 6.291   -11.121 1 78.114  ? 21  GLN   B N    1 ? 1 
ATOM   98   C CA   . GLN   A 1 9   ? 13.269 5.248   -11.895 1 77.959  ? 21  GLN   B CA   1 ? 1 
ATOM   99   C C    . GLN   A 1 9   ? 13.526 3.981   -11.062 1 68.815  ? 21  GLN   B C    1 ? 1 
ATOM   100  O O    . GLN   A 1 9   ? 13.894 2.93    -11.601 1 64.625  ? 21  GLN   B O    1 ? 1 
ATOM   101  C CB   . GLN   A 1 9   ? 14.544 5.834   -12.52  1 83.741  ? 21  GLN   B CB   1 ? 1 
ATOM   102  H H    . GLN   A 1 9   ? 13.06  6.695   -10.44  1 75.22   ? 21  GLN   B H    1 c 1 
ATOM   103  H HA   . GLN   A 1 9   ? 12.673 4.996   -12.644 1 80.433  ? 21  GLN   B HA   1 c 1 
ATOM   104  H HB2  . GLN   A 1 9   ? 15.299 5.618   -12.282 0 30      ? 21  GLN   B HB2  1 c 1 
ATOM   105  H HB3  . GLN   A 1 9   ? 14.097 6.542   -13.354 0 30      ? 21  GLN   B HB3  1 c 1 
ATOM   106  N N    . GLY   A 1 10  ? 13.302 4.04    -9.744  1 62.344  ? 22  GLY   B N    1 ? 1 
ATOM   107  C CA   . GLY   A 1 10  ? 13.761 2.995   -8.834  1 58.783  ? 22  GLY   B CA   1 ? 1 
ATOM   108  C C    . GLY   A 1 10  ? 12.971 1.686   -8.964  1 56.966  ? 22  GLY   B C    1 ? 1 
ATOM   109  O O    . GLY   A 1 10  ? 11.77  1.701   -9.199  1 54.946  ? 22  GLY   B O    1 ? 1 
ATOM   110  H H    . GLY   A 1 10  ? 12.836 4.746   -9.397  1 62.602  ? 22  GLY   B H    1 c 1 
ATOM   111  H HA2  . GLY   A 1 10  ? 14.711 2.816   -9.016  1 58.64   ? 22  GLY   B HA2  1 c 1 
ATOM   112  H HA3  . GLY   A 1 10  ? 13.69  3.325   -7.908  1 56.014  ? 22  GLY   B HA3  1 c 1 
ATOM   113  N N    . GLU   A 1 11  ? 13.672 0.57    -8.758  1 58.091  ? 23  GLU   B N    1 ? 1 
ATOM   114  C CA   . GLU   A 1 11  ? 13.107 -0.766  -8.841  1 60.335  ? 23  GLU   B CA   1 ? 1 
ATOM   115  C C    . GLU   A 1 11  ? 12.393 -1.114  -7.529  1 55.758  ? 23  GLU   B C    1 ? 1 
ATOM   116  O O    . GLU   A 1 11  ? 12.944 -0.931  -6.436  1 48.313  ? 23  GLU   B O    1 ? 1 
ATOM   117  C CB   . GLU   A 1 11  ? 14.257 -1.736  -9.136  1 64.907  ? 23  GLU   B CB   1 ? 1 
ATOM   118  C CG   . GLU   A 1 11  ? 13.784 -3.171  -9.34   1 75.697  ? 23  GLU   B CG   1 ? 1 
ATOM   119  C CD   . GLU   A 1 11  ? 14.839 -4.272  -9.377  1 81.67   ? 23  GLU   B CD   1 ? 1 
ATOM   120  O OE1  . GLU   A 1 11  ? 16.049 -3.952  -9.458  1 80.136  ? 23  GLU   B OE1  1 ? 1 
ATOM   121  O OE2  . GLU   A 1 11  ? 14.426 -5.464  -9.304  1 81.549  ? 23  GLU   B OE2  1 ? 1 
ATOM   122  H H    . GLU   A 1 11  ? 14.557 0.649   -8.546  1 57.236  ? 23  GLU   B H    1 c 1 
ATOM   123  H HA   . GLU   A 1 11  ? 12.455 -0.79   -9.587  1 62.772  ? 23  GLU   B HA   1 c 1 
ATOM   124  H HB2  . GLU   A 1 11  ? 14.728 -1.434  -9.941  1 68.075  ? 23  GLU   B HB2  1 c 1 
ATOM   125  H HB3  . GLU   A 1 11  ? 14.893 -1.71   -8.39   1 63.627  ? 23  GLU   B HB3  1 c 1 
ATOM   126  H HG2  . GLU   A 1 11  ? 13.149 -3.393  -8.627  1 72.79   ? 23  GLU   B HG2  1 c 1 
ATOM   127  H HG3  . GLU   A 1 11  ? 13.282 -3.212  -10.182 1 77.242  ? 23  GLU   B HG3  1 c 1 
ATOM   128  N N    . ASP   A 1 12  ? 11.169 -1.65   -7.651  1 53.672  ? 24  ASP   B N    1 ? 1 
ATOM   129  C CA   . ASP   A 1 12  ? 10.418 -2.14   -6.501  1 50.839  ? 24  ASP   B CA   1 ? 1 
ATOM   130  C C    . ASP   A 1 12  ? 10.897 -3.541  -6.152  1 50.796  ? 24  ASP   B C    1 ? 1 
ATOM   131  O O    . ASP   A 1 12  ? 10.71  -4.474  -6.933  1 54.285  ? 24  ASP   B O    1 ? 1 
ATOM   132  C CB   . ASP   A 1 12  ? 8.924  -2.119  -6.75   1 51.485  ? 24  ASP   B CB   1 ? 1 
ATOM   133  C CG   . ASP   A 1 12  ? 8.085  -2.673  -5.617  1 49.029  ? 24  ASP   B CG   1 ? 1 
ATOM   134  O OD1  . ASP   A 1 12  ? 8.669  -3.098  -4.619  1 48.45   ? 24  ASP   B OD1  1 ? 1 
ATOM   135  O OD2  . ASP   A 1 12  ? 6.849  -2.69   -5.752  1 51.862  ? 24  ASP   B OD2  1 ? 1 
ATOM   136  H H    . ASP   A 1 12  ? 10.79  -1.713  -8.48   1 56.883  ? 24  ASP   B H    1 c 1 
ATOM   137  H HA   . ASP   A 1 12  ? 10.598 -1.547  -5.739  1 48.727  ? 24  ASP   B HA   1 c 1 
ATOM   138  H HB2  . ASP   A 1 12  ? 8.644  -1.195  -6.914  1 52.058  ? 24  ASP   B HB2  1 c 1 
ATOM   139  H HB3  . ASP   A 1 12  ? 8.732  -2.641  -7.557  1 54.087  ? 24  ASP   B HB3  1 c 1 
ATOM   140  N N    . ILE   A 1 13  ? 11.514 -3.658  -4.971  1 45.725  ? 25  ILE   B N    1 ? 1 
ATOM   141  C CA   . ILE   A 1 13  ? 12.186 -4.882  -4.579  1 46.387  ? 25  ILE   B CA   1 ? 1 
ATOM   142  C C    . ILE   A 1 13  ? 11.398 -5.564  -3.462  1 44.413  ? 25  ILE   B C    1 ? 1 
ATOM   143  O O    . ILE   A 1 13  ? 11.883 -6.499  -2.853  1 44.559  ? 25  ILE   B O    1 ? 1 
ATOM   144  C CB   . ILE   A 1 13  ? 13.646 -4.59   -4.18   1 44.666  ? 25  ILE   B CB   1 ? 1 
ATOM   145  C CG1  . ILE   A 1 13  ? 13.743 -3.784  -2.904  1 41.508  ? 25  ILE   B CG1  1 ? 1 
ATOM   146  C CG2  . ILE   A 1 13  ? 14.397 -3.901  -5.313  1 49.041  ? 25  ILE   B CG2  1 ? 1 
ATOM   147  C CD1  . ILE   A 1 13  ? 15.163 -3.546  -2.454  1 42.389  ? 25  ILE   B CD1  1 ? 1 
ATOM   148  H H    . ILE   A 1 13  ? 11.513 -2.951  -4.391  1 45.007  ? 25  ILE   B H    1 c 1 
ATOM   149  H HA   . ILE   A 1 13  ? 12.201 -5.483  -5.349  1 47.977  ? 25  ILE   B HA   1 c 1 
ATOM   150  H HB   . ILE   A 1 13  ? 14.082 -5.45   -4.017  1 45.075  ? 25  ILE   B HB   1 c 1 
ATOM   151  H HG12 . ILE   A 1 13  ? 13.307 -2.919  -3.041  1 42.081  ? 25  ILE   B HG12 1 c 1 
ATOM   152  H HG13 . ILE   A 1 13  ? 13.263 -4.255  -2.193  1 41.341  ? 25  ILE   B HG13 1 c 1 
ATOM   153  H HG21 . ILE   A 1 13  ? 15.354 -3.949  -5.148  1 47.677  ? 25  ILE   B HG21 1 c 1 
ATOM   154  H HG22 . ILE   A 1 13  ? 14.125 -2.97   -5.365  1 48.024  ? 25  ILE   B HG22 1 c 1 
ATOM   155  H HG23 . ILE   A 1 13  ? 14.194 -4.343  -6.154  1 50.327  ? 25  ILE   B HG23 1 c 1 
ATOM   156  H HD11 . ILE   A 1 13  ? 15.648 -4.393  -2.444  1 42.044  ? 25  ILE   B HD11 1 c 1 
ATOM   157  H HD12 . ILE   A 1 13  ? 15.158 -3.165  -1.555  1 40.299  ? 25  ILE   B HD12 1 c 1 
ATOM   158  H HD13 . ILE   A 1 13  ? 15.607 -2.927  -3.063  1 42.458  ? 25  ILE   B HD13 1 c 1 
ATOM   159  N N    . THR   A 1 14  ? 10.182 -5.104  -3.181  1 45.615  ? 26  THR   B N    1 ? 1 
ATOM   160  C CA   . THR   A 1 14  ? 9.312  -5.834  -2.269  1 46.635  ? 26  THR   B CA   1 ? 1 
ATOM   161  C C    . THR   A 1 14  ? 8.765  -7.097  -2.948  1 50.874  ? 26  THR   B C    1 ? 1 
ATOM   162  O O    . THR   A 1 14  ? 8.739  -7.241  -4.185  1 54.324  ? 26  THR   B O    1 ? 1 
ATOM   163  C CB   . THR   A 1 14  ? 8.2    -4.933  -1.726  1 44.729  ? 26  THR   B CB   1 ? 1 
ATOM   164  O OG1  . THR   A 1 14  ? 7.359  -4.581  -2.826  1 48.058  ? 26  THR   B OG1  1 ? 1 
ATOM   165  C CG2  . THR   A 1 14  ? 8.777  -3.695  -1.055  1 44.188  ? 26  THR   B CG2  1 ? 1 
ATOM   166  H H    . THR   A 1 14  ? 9.878  -4.332  -3.564  1 46.126  ? 26  THR   B H    1 c 1 
ATOM   167  H HA   . THR   A 1 14  ? 9.858  -6.118  -1.504  1 44.788  ? 26  THR   B HA   1 c 1 
ATOM   168  H HB   . THR   A 1 14  ? 7.671  -5.436  -1.062  1 45.735  ? 26  THR   B HB   1 c 1 
ATOM   169  H HG1  . THR   A 1 14  ? 7.776  -4.209  -3.367  0 30      ? 26  THR   B HG1  1 c 1 
ATOM   170  H HG21 . THR   A 1 14  ? 8.058  -3.177  -0.656  1 43.653  ? 26  THR   B HG21 1 c 1 
ATOM   171  H HG22 . THR   A 1 14  ? 9.238  -3.152  -1.715  1 43.638  ? 26  THR   B HG22 1 c 1 
ATOM   172  H HG23 . THR   A 1 14  ? 9.404  -3.964  -0.363  1 42.056  ? 26  THR   B HG23 1 c 1 
ATOM   173  N N    . SER   A 1 15  ? 8.309  -8.023  -2.1    1 50.967  ? 27  SER   B N    1 ? 1 
ATOM   174  C CA   . SER   A 1 15  ? 7.732  -9.279  -2.562  1 51.832  ? 27  SER   B CA   1 ? 1 
ATOM   175  C C    . SER   A 1 15  ? 6.296  -9.071  -3.022  1 53.586  ? 27  SER   B C    1 ? 1 
ATOM   176  O O    . SER   A 1 15  ? 5.899  -9.542  -4.089  1 53.506  ? 27  SER   B O    1 ? 1 
ATOM   177  C CB   . SER   A 1 15  ? 7.818  -10.318 -1.478  1 52.132  ? 27  SER   B CB   1 ? 1 
ATOM   178  O OG   . SER   A 1 15  ? 9.189  -10.638 -1.23   1 49.068  ? 27  SER   B OG   1 ? 1 
ATOM   179  H H    . SER   A 1 15  ? 8.356  -7.866  -1.201  1 48.832  ? 27  SER   B H    1 c 1 
ATOM   180  H HA   . SER   A 1 15  ? 8.261  -9.596  -3.338  1 53.119  ? 27  SER   B HA   1 c 1 
ATOM   181  H HB2  . SER   A 1 15  ? 7.408  -9.974  -0.661  1 50.762  ? 27  SER   B HB2  1 c 1 
ATOM   182  H HB3  . SER   A 1 15  ? 7.336  -11.119 -1.752  1 54.159  ? 27  SER   B HB3  1 c 1 
ATOM   183  H HG   . SER   A 1 15  ? 9.169  -11.331 -0.647  0 30      ? 27  SER   B HG   1 c 1 
ATOM   184  N N    . LYS   A 1 16  ? 5.54   -8.301  -2.228  1 55.155  ? 28  LYS   B N    1 ? 1 
ATOM   185  C CA   . LYS   A 1 16  ? 4.156  -7.986  -2.541  1 59.256  ? 28  LYS   B CA   1 ? 1 
ATOM   186  C C    . LYS   A 1 16  ? 4.056  -6.99   -3.695  1 57.665  ? 28  LYS   B C    1 ? 1 
ATOM   187  O O    . LYS   A 1 16  ? 2.957  -6.691  -4.147  1 54.373  ? 28  LYS   B O    1 ? 1 
ATOM   188  C CB   . LYS   A 1 16  ? 3.485  -7.43   -1.292  1 60.515  ? 28  LYS   B CB   1 ? 1 
ATOM   189  C CG   . LYS   A 1 16  ? 3.438  -8.436  -0.165  1 65.434  ? 28  LYS   B CG   1 ? 1 
ATOM   190  C CD   . LYS   A 1 16  ? 2.847  -7.899  1.131   1 71.767  ? 28  LYS   B CD   1 ? 1 
ATOM   191  C CE   . LYS   A 1 16  ? 3.664  -8.292  2.331   1 72.612  ? 28  LYS   B CE   1 ? 1 
ATOM   192  N NZ   . LYS   A 1 16  ? 2.844  -8.279  3.544   1 75.492  ? 28  LYS   B NZ   1 ? 1 
ATOM   193  H H    . LYS   A 1 16  ? 5.905  -7.958  -1.463  1 52.591  ? 28  LYS   B H    1 c 1 
ATOM   194  H HA   . LYS   A 1 16  ? 3.697  -8.824  -2.804  1 61.542  ? 28  LYS   B HA   1 c 1 
ATOM   195  H HB2  . LYS   A 1 16  ? 3.975  -6.636  -0.988  1 58.52   ? 28  LYS   B HB2  1 c 1 
ATOM   196  H HB3  . LYS   A 1 16  ? 2.569  -7.156  -1.511  1 63.149  ? 28  LYS   B HB3  1 c 1 
ATOM   197  H HG2  . LYS   A 1 16  ? 2.907  -9.207  -0.46   1 68.422  ? 28  LYS   B HG2  1 c 1 
ATOM   198  H HG3  . LYS   A 1 16  ? 4.35   -8.753  0.009   1 63.769  ? 28  LYS   B HG3  1 c 1 
ATOM   199  H HD2  . LYS   A 1 16  ? 2.798  -6.919  1.083   1 69.632  ? 28  LYS   B HD2  1 c 1 
ATOM   200  H HD3  . LYS   A 1 16  ? 1.934  -8.246  1.236   1 73.476  ? 28  LYS   B HD3  1 c 1 
ATOM   201  H HE2  . LYS   A 1 16  ? 4.032  -9.186  2.207   1 72.591  ? 28  LYS   B HE2  1 c 1 
ATOM   202  H HE3  . LYS   A 1 16  ? 4.404  -7.669  2.441   1 69.693  ? 28  LYS   B HE3  1 c 1 
ATOM   203  H HZ1  . LYS   A 1 16  ? 2.214  -8.929  3.495   1 77.393  ? 28  LYS   B HZ1  1 c 1 
ATOM   204  H HZ2  . LYS   A 1 16  ? 2.435  -7.475  3.631   1 74.805  ? 28  LYS   B HZ2  1 c 1 
ATOM   205  H HZ3  . LYS   A 1 16  ? 3.367  -8.427  4.269   1 73.507  ? 28  LYS   B HZ3  1 c 1 
ATOM   206  N N    . LYS   A 1 17  ? 5.203  -6.435  -4.112  1 56.274  ? 29  LYS   B N    1 ? 1 
ATOM   207  C CA   . LYS   A 1 17  ? 5.247  -5.447  -5.181  1 58.704  ? 29  LYS   B CA   1 ? 1 
ATOM   208  C C    . LYS   A 1 17  ? 4.34   -4.272  -4.829  1 55.374  ? 29  LYS   B C    1 ? 1 
ATOM   209  O O    . LYS   A 1 17  ? 3.485  -3.897  -5.626  1 55.489  ? 29  LYS   B O    1 ? 1 
ATOM   210  C CB   . LYS   A 1 17  ? 4.868  -6.052  -6.549  1 63.4    ? 29  LYS   B CB   1 ? 1 
ATOM   211  C CG   . LYS   A 1 17  ? 5.947  -6.945  -7.163  1 64.113  ? 29  LYS   B CG   1 ? 1 
ATOM   212  C CD   . LYS   A 1 17  ? 7.214  -6.171  -7.527  1 62.174  ? 29  LYS   B CD   1 ? 1 
ATOM   213  C CE   . LYS   A 1 17  ? 8.344  -7.009  -8.043  1 64.898  ? 29  LYS   B CE   1 ? 1 
ATOM   214  N NZ   . LYS   A 1 17  ? 9.234  -7.438  -6.952  1 64.175  ? 29  LYS   B NZ   1 ? 1 
ATOM   215  H H    . LYS   A 1 17  ? 5.987  -6.665  -3.704  1 54.248  ? 29  LYS   B H    1 c 1 
ATOM   216  H HA   . LYS   A 1 17  ? 6.174  -5.108  -5.237  1 55.87   ? 29  LYS   B HA   1 c 1 
ATOM   217  H HB2  . LYS   A 1 17  ? 4.048  -6.58   -6.45   1 65.502  ? 29  LYS   B HB2  1 c 1 
ATOM   218  H HB3  . LYS   A 1 17  ? 4.68   -5.323  -7.177  1 64.685  ? 29  LYS   B HB3  1 c 1 
ATOM   219  H HG2  . LYS   A 1 17  ? 6.174  -7.654  -6.523  1 62.81   ? 29  LYS   B HG2  1 c 1 
ATOM   220  H HG3  . LYS   A 1 17  ? 5.584  -7.369  -7.972  1 67.42   ? 29  LYS   B HG3  1 c 1 
ATOM   221  H HD2  . LYS   A 1 17  ? 6.983  -5.501  -8.208  1 64.286  ? 29  LYS   B HD2  1 c 1 
ATOM   222  H HD3  . LYS   A 1 17  ? 7.524  -5.683  -6.735  1 59.692  ? 29  LYS   B HD3  1 c 1 
ATOM   223  H HE2  . LYS   A 1 17  ? 7.988  -7.796  -8.493  1 67.65   ? 29  LYS   B HE2  1 c 1 
ATOM   224  H HE3  . LYS   A 1 17  ? 8.86   -6.496  -8.691  1 65.533  ? 29  LYS   B HE3  1 c 1 
ATOM   225  H HZ1  . LYS   A 1 17  ? 8.756  -7.883  -6.325  1 62.849  ? 29  LYS   B HZ1  1 c 1 
ATOM   226  H HZ2  . LYS   A 1 17  ? 9.625  -6.715  -6.572  1 61.027  ? 29  LYS   B HZ2  1 c 1 
ATOM   227  H HZ3  . LYS   A 1 17  ? 9.877  -7.985  -7.28   1 63.794  ? 29  LYS   B HZ3  1 c 1 
ATOM   228  N N    . ASP   A 1 18  ? 4.552  -3.703  -3.634  1 49.628  ? 30  ASP   B N    1 ? 1 
ATOM   229  C CA   . ASP   A 1 18  ? 3.725  -2.623  -3.14   1 48.772  ? 30  ASP   B CA   1 ? 1 
ATOM   230  C C    . ASP   A 1 18  ? 4.512  -1.312  -3.124  1 47.175  ? 30  ASP   B C    1 ? 1 
ATOM   231  O O    . ASP   A 1 18  ? 4.047  -0.318  -2.565  1 53.955  ? 30  ASP   B O    1 ? 1 
ATOM   232  C CB   . ASP   A 1 18  ? 3.194  -3.005  -1.774  1 48.599  ? 30  ASP   B CB   1 ? 1 
ATOM   233  C CG   . ASP   A 1 18  ? 4.262  -3.158  -0.69   1 43.998  ? 30  ASP   B CG   1 ? 1 
ATOM   234  O OD1  . ASP   A 1 18  ? 5.409  -2.719  -0.899  1 40.465  ? 30  ASP   B OD1  1 ? 1 
ATOM   235  O OD2  . ASP   A 1 18  ? 3.935  -3.711  0.354   1 43.767  ? 30  ASP   B OD2  1 ? 1 
ATOM   236  H H    . ASP   A 1 18  ? 5.241  -4.002  -3.114  1 47.85   ? 30  ASP   B H    1 c 1 
ATOM   237  H HA   . ASP   A 1 18  ? 2.954  -2.517  -3.741  1 52.067  ? 30  ASP   B HA   1 c 1 
ATOM   238  H HB2  . ASP   A 1 18  ? 2.556  -2.321  -1.481  1 48.851  ? 30  ASP   B HB2  1 c 1 
ATOM   239  H HB3  . ASP   A 1 18  ? 2.711  -3.854  -1.85   1 50.099  ? 30  ASP   B HB3  1 c 1 
ATOM   240  N N    . ARG   A 1 19  ? 5.717  -1.3    -3.7    1 45.268  ? 31  ARG   B N    1 ? 1 
ATOM   241  C CA   . ARG   A 1 19  ? 6.543  -0.098  -3.781  1 43.951  ? 31  ARG   B CA   1 ? 1 
ATOM   242  C C    . ARG   A 1 19  ? 6.911  0.451   -2.388  1 45.056  ? 31  ARG   B C    1 ? 1 
ATOM   243  O O    . ARG   A 1 19  ? 7.203  1.647   -2.243  1 44.903  ? 31  ARG   B O    1 ? 1 
ATOM   244  C CB   . ARG   A 1 19  ? 5.87   0.994   -4.623  1 46.117  ? 31  ARG   B CB   1 ? 1 
ATOM   245  C CG   . ARG   A 1 19  ? 5.581  0.636   -6.077  1 49.073  ? 31  ARG   B CG   1 ? 1 
ATOM   246  C CD   . ARG   A 1 19  ? 5.185  1.796   -7      1 53.036  ? 31  ARG   B CD   1 ? 1 
ATOM   247  N NE   . ARG   A 1 19  ? 5.92   3.054   -6.793  1 52.066  ? 31  ARG   B NE   1 ? 1 
ATOM   248  C CZ   . ARG   A 1 19  ? 6.9    3.561   -7.559  1 53.374  ? 31  ARG   B CZ   1 ? 1 
ATOM   249  N NH1  . ARG   A 1 19  ? 7.446  2.829   -8.497  1 55.927  ? 31  ARG   B NH1  1 ? 1 
ATOM   250  N NH2  . ARG   A 1 19  ? 7.39   4.782   -7.357  1 54.069  ? 31  ARG   B NH2  1 ? 1 
ATOM   251  H H    . ARG   A 1 19  ? 6.043  -2.073  -4.06   1 45.963  ? 31  ARG   B H    1 c 1 
ATOM   252  H HA   . ARG   A 1 19  ? 7.386  -0.344  -4.239  1 44.182  ? 31  ARG   B HA   1 c 1 
ATOM   253  H HB2  . ARG   A 1 19  ? 5.025  1.243   -4.194  1 46.758  ? 31  ARG   B HB2  1 c 1 
ATOM   254  H HB3  . ARG   A 1 19  ? 6.447  1.787   -4.611  1 45.157  ? 31  ARG   B HB3  1 c 1 
ATOM   255  H HG2  . ARG   A 1 19  ? 6.377  0.201   -6.453  1 49.069  ? 31  ARG   B HG2  1 c 1 
ATOM   256  H HG3  . ARG   A 1 19  ? 4.862  -0.032  -6.094  1 50.973  ? 31  ARG   B HG3  1 c 1 
ATOM   257  H HD2  . ARG   A 1 19  ? 5.308  1.505   -7.927  1 55.212  ? 31  ARG   B HD2  1 c 1 
ATOM   258  H HD3  . ARG   A 1 19  ? 4.229  1.968   -6.876  1 54.491  ? 31  ARG   B HD3  1 c 1 
ATOM   259  H HE   . ARG   A 1 19  ? 5.698  3.525   -6.095  1 50.892  ? 31  ARG   B HE   1 c 1 
ATOM   260  H HH11 . ARG   A 1 19  ? 7.589  1.966   -8.36   1 54.844  ? 31  ARG   B HH11 1 c 1 
ATOM   261  H HH12 . ARG   A 1 19  ? 7.676  3.203   -9.266  1 57.611  ? 31  ARG   B HH12 1 c 1 
ATOM   262  H HH21 . ARG   A 1 19  ? 7.052  5.293   -6.719  1 52.719  ? 31  ARG   B HH21 1 c 1 
ATOM   263  H HH22 . ARG   A 1 19  ? 8.053  5.081   -7.861  1 54.247  ? 31  ARG   B HH22 1 c 1 
ATOM   264  N N    . GLY   A 1 20  ? 6.946  -0.418  -1.366  1 42.235  ? 32  GLY   B N    1 ? 1 
ATOM   265  C CA   . GLY   A 1 20  ? 7.348  -0.022  -0.019  1 41.468  ? 32  GLY   B CA   1 ? 1 
ATOM   266  C C    . GLY   A 1 20  ? 8.858  0.165   0.116   1 38.212  ? 32  GLY   B C    1 ? 1 
ATOM   267  O O    . GLY   A 1 20  ? 9.337  0.823   1.039   1 37.185  ? 32  GLY   B O    1 ? 1 
ATOM   268  H H    . GLY   A 1 20  ? 6.726  -1.293  -1.514  1 43.618  ? 32  GLY   B H    1 c 1 
ATOM   269  H HA2  . GLY   A 1 20  ? 6.894  0.819   0.216   1 41.131  ? 32  GLY   B HA2  1 c 1 
ATOM   270  H HA3  . GLY   A 1 20  ? 7.048  -0.71   0.616   1 40.615  ? 32  GLY   B HA3  1 c 1 
ATOM   271  N N    . VAL   A 1 21  ? 9.604  -0.409  -0.825  1 39.821  ? 33  VAL   B N    1 ? 1 
ATOM   272  C CA   . VAL   A 1 21  ? 11.053 -0.312  -0.868  1 35.769  ? 33  VAL   B CA   1 ? 1 
ATOM   273  C C    . VAL   A 1 21  ? 11.472 -0.212  -2.327  1 37.358  ? 33  VAL   B C    1 ? 1 
ATOM   274  O O    . VAL   A 1 21  ? 11.377 -1.203  -3.046  1 35.32   ? 33  VAL   B O    1 ? 1 
ATOM   275  C CB   . VAL   A 1 21  ? 11.786 -1.49   -0.201  1 35.139  ? 33  VAL   B CB   1 ? 1 
ATOM   276  C CG1  . VAL   A 1 21  ? 13.303 -1.257  -0.213  1 33.786  ? 33  VAL   B CG1  1 ? 1 
ATOM   277  C CG2  . VAL   A 1 21  ? 11.299 -1.729  1.23    1 38.011  ? 33  VAL   B CG2  1 ? 1 
ATOM   278  H H    . VAL   A 1 21  ? 9.189  -0.9    -1.474  1 40.303  ? 33  VAL   B H    1 c 1 
ATOM   279  H HA   . VAL   A 1 21  ? 11.319 0.51    -0.413  1 35.623  ? 33  VAL   B HA   1 c 1 
ATOM   280  H HB   . VAL   A 1 21  ? 11.592 -2.299  -0.731  1 36.561  ? 33  VAL   B HB   1 c 1 
ATOM   281  H HG11 . VAL   A 1 21  ? 13.501 -0.391  0.181   1 33.407  ? 33  VAL   B HG11 1 c 1 
ATOM   282  H HG12 . VAL   A 1 21  ? 13.63  -1.278  -1.128  1 34.984  ? 33  VAL   B HG12 1 c 1 
ATOM   283  H HG13 . VAL   A 1 21  ? 13.743 -1.955  0.301   1 33.375  ? 33  VAL   B HG13 1 c 1 
ATOM   284  H HG21 . VAL   A 1 21  ? 11.846 -2.415  1.649   1 36.221  ? 33  VAL   B HG21 1 c 1 
ATOM   285  H HG22 . VAL   A 1 21  ? 10.372 -2.021  1.214   1 37.604  ? 33  VAL   B HG22 1 c 1 
ATOM   286  H HG23 . VAL   A 1 21  ? 11.37  -0.904  1.74    1 36.141  ? 33  VAL   B HG23 1 c 1 
ATOM   287  N N    . LEU   A 1 22  ? 11.985 0.961   -2.712  1 39.657  ? 34  LEU   B N    1 ? 1 
ATOM   288  C CA   . LEU   A 1 22  ? 12.471 1.225   -4.066  1 42.973  ? 34  LEU   B CA   1 ? 1 
ATOM   289  C C    . LEU   A 1 22  ? 13.987 1.409   -4.037  1 40.221  ? 34  LEU   B C    1 ? 1 
ATOM   290  O O    . LEU   A 1 22  ? 14.514 1.958   -3.067  1 38.586  ? 34  LEU   B O    1 ? 1 
ATOM   291  C CB   . LEU   A 1 22  ? 11.774 2.466   -4.623  1 47.405  ? 34  LEU   B CB   1 ? 1 
ATOM   292  C CG   . LEU   A 1 22  ? 10.243 2.456   -4.551  1 49.843  ? 34  LEU   B CG   1 ? 1 
ATOM   293  C CD1  . LEU   A 1 22  ? 9.596  3.77    -4.819  1 49.439  ? 34  LEU   B CD1  1 ? 1 
ATOM   294  C CD2  . LEU   A 1 22  ? 9.781  1.406   -5.544  1 54.155  ? 34  LEU   B CD2  1 ? 1 
ATOM   295  H H    . LEU   A 1 22  ? 12.036 1.637   -2.1    1 38.528  ? 34  LEU   B H    1 c 1 
ATOM   296  H HA   . LEU   A 1 22  ? 12.256 0.447   -4.635  1 43.882  ? 34  LEU   B HA   1 c 1 
ATOM   297  H HB2  . LEU   A 1 22  ? 12.101 3.249   -4.124  1 46.159  ? 34  LEU   B HB2  1 c 1 
ATOM   298  H HB3  . LEU   A 1 22  ? 12.043 2.575   -5.564  1 48.983  ? 34  LEU   B HB3  1 c 1 
ATOM   299  H HG   . LEU   A 1 22  ? 9.974  2.163   -3.642  1 47.932  ? 34  LEU   B HG   1 c 1 
ATOM   300  H HD11 . LEU   A 1 22  ? 9.916  4.427   -4.179  1 48.76   ? 34  LEU   B HD11 1 c 1 
ATOM   301  H HD12 . LEU   A 1 22  ? 8.632  3.681   -4.737  1 50.812  ? 34  LEU   B HD12 1 c 1 
ATOM   302  H HD13 . LEU   A 1 22  ? 9.818  4.063   -5.72   1 51.899  ? 34  LEU   B HD13 1 c 1 
ATOM   303  H HD21 . LEU   A 1 22  ? 10.044 0.525   -5.232  1 52.424  ? 34  LEU   B HD21 1 c 1 
ATOM   304  H HD22 . LEU   A 1 22  ? 10.184 1.576   -6.412  1 55.112  ? 34  LEU   B HD22 1 c 1 
ATOM   305  H HD23 . LEU   A 1 22  ? 8.813  1.441   -5.626  1 54.726  ? 34  LEU   B HD23 1 c 1 
ATOM   306  N N    . LYS   A 1 23  ? 14.661 0.971   -5.108  1 38.494  ? 35  LYS   B N    1 ? 1 
ATOM   307  C CA   . LYS   A 1 23  ? 16.114 0.854   -5.119  1 37.771  ? 35  LYS   B CA   1 ? 1 
ATOM   308  C C    . LYS   A 1 23  ? 16.69  1.408   -6.416  1 41.883  ? 35  LYS   B C    1 ? 1 
ATOM   309  O O    . LYS   A 1 23  ? 16.209 1.055   -7.494  1 42.907  ? 35  LYS   B O    1 ? 1 
ATOM   310  C CB   . LYS   A 1 23  ? 16.584 -0.601  -5.055  1 35.767  ? 35  LYS   B CB   1 ? 1 
ATOM   311  C CG   . LYS   A 1 23  ? 18.072 -0.771  -4.979  1 37.469  ? 35  LYS   B CG   1 ? 1 
ATOM   312  C CD   . LYS   A 1 23  ? 18.613 -2.195  -4.998  1 38.562  ? 35  LYS   B CD   1 ? 1 
ATOM   313  C CE   . LYS   A 1 23  ? 20.079 -2.245  -4.667  1 41.206  ? 35  LYS   B CE   1 ? 1 
ATOM   314  N NZ   . LYS   A 1 23  ? 20.732 -3.494  -5.087  1 44.867  ? 35  LYS   B NZ   1 ? 1 
ATOM   315  H H    . LYS   A 1 23  ? 14.198 0.738   -5.861  1 40.834  ? 35  LYS   B H    1 c 1 
ATOM   316  H HA   . LYS   A 1 23  ? 16.482 1.358   -4.355  1 36.657  ? 35  LYS   B HA   1 c 1 
ATOM   317  H HB2  . LYS   A 1 23  ? 16.183 -1.026  -4.268  1 34.894  ? 35  LYS   B HB2  1 c 1 
ATOM   318  H HB3  . LYS   A 1 23  ? 16.257 -1.076  -5.849  1 38.096  ? 35  LYS   B HB3  1 c 1 
ATOM   319  H HG2  . LYS   A 1 23  ? 18.473 -0.284  -5.73   1 39.182  ? 35  LYS   B HG2  1 c 1 
ATOM   320  H HG3  . LYS   A 1 23  ? 18.384 -0.334  -4.158  1 36.062  ? 35  LYS   B HG3  1 c 1 
ATOM   321  H HD2  . LYS   A 1 23  ? 18.117 -2.737  -4.347  1 37.457  ? 35  LYS   B HD2  1 c 1 
ATOM   322  H HD3  . LYS   A 1 23  ? 18.471 -2.581  -5.89   1 40.719  ? 35  LYS   B HD3  1 c 1 
ATOM   323  H HE2  . LYS   A 1 23  ? 20.53  -1.498  -5.099  1 42.35   ? 35  LYS   B HE2  1 c 1 
ATOM   324  H HE3  . LYS   A 1 23  ? 20.191 -2.143  -3.704  1 39.466  ? 35  LYS   B HE3  1 c 1 
ATOM   325  H HZ1  . LYS   A 1 23  ? 20.702 -3.567  -5.989  1 46.045  ? 35  LYS   B HZ1  1 c 1 
ATOM   326  H HZ2  . LYS   A 1 23  ? 20.306 -4.202  -4.717  1 43.269  ? 35  LYS   B HZ2  1 c 1 
ATOM   327  H HZ3  . LYS   A 1 23  ? 21.597 -3.493  -4.817  1 44.493  ? 35  LYS   B HZ3  1 c 1 
ATOM   328  N N    . ILE   A 1 24  ? 17.757 2.217   -6.297  1 44.656  ? 36  ILE   B N    1 ? 1 
ATOM   329  C CA   . ILE   A 1 24  ? 18.65  2.458   -7.42   1 52.163  ? 36  ILE   B CA   1 ? 1 
ATOM   330  C C    . ILE   A 1 24  ? 20.08  2.117   -7.04   1 52.614  ? 36  ILE   B C    1 ? 1 
ATOM   331  O O    . ILE   A 1 24  ? 20.579 2.6     -6.034  1 51.013  ? 36  ILE   B O    1 ? 1 
ATOM   332  C CB   . ILE   A 1 24  ? 18.58  3.899   -7.95   1 53.637  ? 36  ILE   B CB   1 ? 1 
ATOM   333  C CG1  . ILE   A 1 24  ? 17.148 4.325   -8.21   1 55.238  ? 36  ILE   B CG1  1 ? 1 
ATOM   334  C CG2  . ILE   A 1 24  ? 19.469 4.044   -9.193  1 54.686  ? 36  ILE   B CG2  1 ? 1 
ATOM   335  C CD1  . ILE   A 1 24  ? 16.971 5.221   -9.427  1 61.003  ? 36  ILE   B CD1  1 ? 1 
ATOM   336  H H    . ILE   A 1 24  ? 17.928 2.629   -5.499  1 43.452  ? 36  ILE   B H    1 c 1 
ATOM   337  H HA   . ILE   A 1 24  ? 18.383 1.864   -8.147  1 52.595  ? 36  ILE   B HA   1 c 1 
ATOM   338  H HB   . ILE   A 1 24  ? 18.941 4.486   -7.257  1 52.405  ? 36  ILE   B HB   1 c 1 
ATOM   339  H HG12 . ILE   A 1 24  ? 16.599 3.525   -8.33   1 54.794  ? 36  ILE   B HG12 1 c 1 
ATOM   340  H HG13 . ILE   A 1 24  ? 16.814 4.799   -7.421  1 53.476  ? 36  ILE   B HG13 1 c 1 
ATOM   341  H HG21 . ILE   A 1 24  ? 19.45  4.963   -9.506  1 57.269  ? 36  ILE   B HG21 1 c 1 
ATOM   342  H HG22 . ILE   A 1 24  ? 19.145 3.456   -9.897  1 56.966  ? 36  ILE   B HG22 1 c 1 
ATOM   343  H HG23 . ILE   A 1 24  ? 20.382 3.805   -8.971  1 55.662  ? 36  ILE   B HG23 1 c 1 
ATOM   344  H HD11 . ILE   A 1 24  ? 17.531 6.016   -9.342  1 61.093  ? 36  ILE   B HD11 1 c 1 
ATOM   345  H HD12 . ILE   A 1 24  ? 16.035 5.493   -9.484  1 60.517  ? 36  ILE   B HD12 1 c 1 
ATOM   346  H HD13 . ILE   A 1 24  ? 17.213 4.738   -10.239 1 62.433  ? 36  ILE   B HD13 1 c 1 
ATOM   347  N N    . VAL   A 1 25  ? 20.75  1.383   -7.941  1 58.914  ? 37  VAL   B N    1 ? 1 
ATOM   348  C CA   . VAL   A 1 25  ? 22.188 1.165   -7.874  1 57.359  ? 37  VAL   B CA   1 ? 1 
ATOM   349  C C    . VAL   A 1 25  ? 22.866 2.425   -8.402  1 58.406  ? 37  VAL   B C    1 ? 1 
ATOM   350  O O    . VAL   A 1 25  ? 22.626 2.81    -9.534  1 58.776  ? 37  VAL   B O    1 ? 1 
ATOM   351  C CB   . VAL   A 1 25  ? 22.624 -0.079  -8.676  1 58.101  ? 37  VAL   B CB   1 ? 1 
ATOM   352  C CG1  . VAL   A 1 25  ? 24.133 -0.288  -8.645  1 58.875  ? 37  VAL   B CG1  1 ? 1 
ATOM   353  C CG2  . VAL   A 1 25  ? 21.908 -1.343  -8.205  1 55.372  ? 37  VAL   B CG2  1 ? 1 
ATOM   354  H H    . VAL   A 1 25  ? 20.287 1.003   -8.631  1 58.394  ? 37  VAL   B H    1 c 1 
ATOM   355  H HA   . VAL   A 1 25  ? 22.44  1.037   -6.939  1 55.275  ? 37  VAL   B HA   1 c 1 
ATOM   356  H HB   . VAL   A 1 25  ? 22.365 0.078   -9.614  1 60.344  ? 37  VAL   B HB   1 c 1 
ATOM   357  H HG11 . VAL   A 1 25  ? 24.442 -0.292  -7.723  1 57.385  ? 37  VAL   B HG11 1 c 1 
ATOM   358  H HG12 . VAL   A 1 25  ? 24.573 0.431   -9.129  1 61.495  ? 37  VAL   B HG12 1 c 1 
ATOM   359  H HG13 . VAL   A 1 25  ? 24.352 -1.138  -9.063  1 60.451  ? 37  VAL   B HG13 1 c 1 
ATOM   360  H HG21 . VAL   A 1 25  ? 22.231 -2.107  -8.712  1 57.115  ? 37  VAL   B HG21 1 c 1 
ATOM   361  H HG22 . VAL   A 1 25  ? 20.951 -1.245  -8.343  1 54.9    ? 37  VAL   B HG22 1 c 1 
ATOM   362  H HG23 . VAL   A 1 25  ? 22.086 -1.483  -7.26   1 53.33   ? 37  VAL   B HG23 1 c 1 
ATOM   363  N N    . LYS   A 1 26  ? 23.705 3.057   -7.579  1 59.374  ? 38  LYS   B N    1 ? 1 
ATOM   364  C CA   . LYS   A 1 26  ? 24.402 4.27    -8.004  1 61.165  ? 38  LYS   B CA   1 ? 1 
ATOM   365  C C    . LYS   A 1 26  ? 25.843 3.927   -8.39   1 64.484  ? 38  LYS   B C    1 ? 1 
ATOM   366  O O    . LYS   A 1 26  ? 26.315 4.392   -9.407  1 69.889  ? 38  LYS   B O    1 ? 1 
ATOM   367  C CB   . LYS   A 1 26  ? 24.253 5.373   -6.947  1 58.655  ? 38  LYS   B CB   1 ? 1 
ATOM   368  C CG   . LYS   A 1 26  ? 22.811 5.755   -6.556  1 55.701  ? 38  LYS   B CG   1 ? 1 
ATOM   369  C CD   . LYS   A 1 26  ? 21.939 6.257   -7.709  1 55.804  ? 38  LYS   B CD   1 ? 1 
ATOM   370  C CE   . LYS   A 1 26  ? 22.294 7.609   -8.138  1 59.526  ? 38  LYS   B CE   1 ? 1 
ATOM   371  N NZ   . LYS   A 1 26  ? 21.412 8.098   -9.198  1 63.134  ? 38  LYS   B NZ   1 ? 1 
ATOM   372  H H    . LYS   A 1 26  ? 23.849 2.733   -6.737  1 56.777  ? 38  LYS   B H    1 c 1 
ATOM   373  H HA   . LYS   A 1 26  ? 23.955 4.604   -8.82   1 62.887  ? 38  LYS   B HA   1 c 1 
ATOM   374  H HB2  . LYS   A 1 26  ? 24.725 5.089   -6.135  1 57.573  ? 38  LYS   B HB2  1 c 1 
ATOM   375  H HB3  . LYS   A 1 26  ? 24.702 6.178   -7.28   1 61.303  ? 38  LYS   B HB3  1 c 1 
ATOM   376  H HG2  . LYS   A 1 26  ? 22.381 4.969   -6.154  1 52.967  ? 38  LYS   B HG2  1 c 1 
ATOM   377  H HG3  . LYS   A 1 26  ? 22.854 6.452   -5.868  1 54.593  ? 38  LYS   B HG3  1 c 1 
ATOM   378  H HD2  . LYS   A 1 26  ? 22.025 5.646   -8.472  1 57.76   ? 38  LYS   B HD2  1 c 1 
ATOM   379  H HD3  . LYS   A 1 26  ? 20.999 6.25    -7.423  1 54.449  ? 38  LYS   B HD3  1 c 1 
ATOM   380  H HE2  . LYS   A 1 26  ? 22.239 8.215   -7.377  1 58.579  ? 38  LYS   B HE2  1 c 1 
ATOM   381  H HE3  . LYS   A 1 26  ? 23.212 7.615   -8.464  1 61.983  ? 38  LYS   B HE3  1 c 1 
ATOM   382  H HZ1  . LYS   A 1 26  ? 20.549 8.055   -8.925  1 60.836  ? 38  LYS   B HZ1  1 c 1 
ATOM   383  H HZ2  . LYS   A 1 26  ? 21.515 7.59    -9.941  1 64.268  ? 38  LYS   B HZ2  1 c 1 
ATOM   384  H HZ3  . LYS   A 1 26  ? 21.618 8.958   -9.395  1 64.726  ? 38  LYS   B HZ3  1 c 1 
ATOM   385  N N    . ARG   A 1 27  ? 26.533 3.065   -7.635  1 66.041  ? 39  ARG   B N    1 ? 1 
ATOM   386  C CA   . ARG   A 1 27  ? 27.816 2.545   -8.087  1 68.673  ? 39  ARG   B CA   1 ? 1 
ATOM   387  C C    . ARG   A 1 27  ? 27.751 1.022   -8.016  1 67.031  ? 39  ARG   B C    1 ? 1 
ATOM   388  O O    . ARG   A 1 27  ? 27.383 0.469   -6.996  1 62.276  ? 39  ARG   B O    1 ? 1 
ATOM   389  C CB   . ARG   A 1 27  ? 28.994 3.113   -7.282  1 70.711  ? 39  ARG   B CB   1 ? 1 
ATOM   390  C CG   . ARG   A 1 27  ? 30.407 2.757   -7.741  1 73.602  ? 39  ARG   B CG   1 ? 1 
ATOM   391  C CD   . ARG   A 1 27  ? 31.484 3.243   -6.755  1 76.052  ? 39  ARG   B CD   1 ? 1 
ATOM   392  N NE   . ARG   A 1 27  ? 31.48  2.457   -5.512  1 76.45   ? 39  ARG   B NE   1 ? 1 
ATOM   393  C CZ   . ARG   A 1 27  ? 32.029 2.793   -4.339  1 77.457  ? 39  ARG   B CZ   1 ? 1 
ATOM   394  N NH1  . ARG   A 1 27  ? 32.708 3.919   -4.209  1 78.244  ? 39  ARG   B NH1  1 ? 1 
ATOM   395  N NH2  . ARG   A 1 27  ? 31.889 2.001   -3.281  1 74.886  ? 39  ARG   B NH2  1 ? 1 
ATOM   396  H H    . ARG   A 1 27  ? 26.206 2.802   -6.823  1 62.374  ? 39  ARG   B H    1 c 1 
ATOM   397  H HA   . ARG   A 1 27  ? 27.942 2.808   -9.033  1 71.821  ? 39  ARG   B HA   1 c 1 
ATOM   398  H HB2  . ARG   A 1 27  ? 28.912 4.091   -7.281  1 70.943  ? 39  ARG   B HB2  1 c 1 
ATOM   399  H HB3  . ARG   A 1 27  ? 28.892 2.816   -6.352  1 67.636  ? 39  ARG   B HB3  1 c 1 
ATOM   400  H HG2  . ARG   A 1 27  ? 30.481 1.783   -7.838  1 73.842  ? 39  ARG   B HG2  1 c 1 
ATOM   401  H HG3  . ARG   A 1 27  ? 30.573 3.163   -8.619  1 77.21   ? 39  ARG   B HG3  1 c 1 
ATOM   402  H HD2  . ARG   A 1 27  ? 32.364 3.174   -7.177  1 80.232  ? 39  ARG   B HD2  1 c 1 
ATOM   403  H HD3  . ARG   A 1 27  ? 31.324 4.185   -6.541  1 76.718  ? 39  ARG   B HD3  1 c 1 
ATOM   404  H HE   . ARG   A 1 27  ? 31.077 1.685   -5.539  1 73.976  ? 39  ARG   B HE   1 c 1 
ATOM   405  H HH11 . ARG   A 1 27  ? 33.122 4.272   -4.906  1 81.925  ? 39  ARG   B HH11 1 c 1 
ATOM   406  H HH12 . ARG   A 1 27  ? 32.747 4.317   -3.419  1 78.32   ? 39  ARG   B HH12 1 c 1 
ATOM   407  H HH21 . ARG   A 1 27  ? 31.296 1.345   -3.295  1 72.429  ? 39  ARG   B HH21 1 c 1 
ATOM   408  H HH22 . ARG   A 1 27  ? 32.391 2.132   -2.565  1 75.356  ? 39  ARG   B HH22 1 c 1 
ATOM   409  N N    . VAL   A 1 28  ? 28.082 0.382   -9.138  1 71.803  ? 40  VAL   B N    1 ? 1 
ATOM   410  C CA   . VAL   A 1 28  ? 28.043 -1.062  -9.305  1 71.888  ? 40  VAL   B CA   1 ? 1 
ATOM   411  C C    . VAL   A 1 28  ? 29.124 -1.717  -8.453  1 74.432  ? 40  VAL   B C    1 ? 1 
ATOM   412  O O    . VAL   A 1 28  ? 30.256 -1.237  -8.409  1 78.264  ? 40  VAL   B O    1 ? 1 
ATOM   413  C CB   . VAL   A 1 28  ? 28.269 -1.38   -10.797 1 73.516  ? 40  VAL   B CB   1 ? 1 
ATOM   414  C CG1  . VAL   A 1 28  ? 29.583 -0.785  -11.281 1 76.089  ? 40  VAL   B CG1  1 ? 1 
ATOM   415  C CG2  . VAL   A 1 28  ? 28.229 -2.88   -11.089 1 73.802  ? 40  VAL   B CG2  1 ? 1 
ATOM   416  H H    . VAL   A 1 28  ? 28.334 0.89    -9.854  1 74.232  ? 40  VAL   B H    1 c 1 
ATOM   417  H HA   . VAL   A 1 28  ? 27.165 -1.392  -9.032  1 69.026  ? 40  VAL   B HA   1 c 1 
ATOM   418  H HB   . VAL   A 1 28  ? 27.538 -0.952  -11.301 1 73.642  ? 40  VAL   B HB   1 c 1 
ATOM   419  H HG11 . VAL   A 1 28  ? 30.323 -1.163  -10.779 1 77.058  ? 40  VAL   B HG11 1 c 1 
ATOM   420  H HG12 . VAL   A 1 28  ? 29.573 0.179   -11.166 1 76.894  ? 40  VAL   B HG12 1 c 1 
ATOM   421  H HG13 . VAL   A 1 28  ? 29.698 -0.991  -12.218 1 79.908  ? 40  VAL   B HG13 1 c 1 
ATOM   422  H HG21 . VAL   A 1 28  ? 28.195 -3.023  -12.05  1 76.802  ? 40  VAL   B HG21 1 c 1 
ATOM   423  H HG22 . VAL   A 1 28  ? 27.44  -3.271  -10.676 1 70.949  ? 40  VAL   B HG22 1 c 1 
ATOM   424  H HG23 . VAL   A 1 28  ? 29.025 -3.304  -10.729 1 74.648  ? 40  VAL   B HG23 1 c 1 
ATOM   425  N N    . GLY   A 1 29  ? 28.774 -2.838  -7.811  1 75.324  ? 41  GLY   B N    1 ? 1 
ATOM   426  C CA   . GLY   A 1 29  ? 29.738 -3.622  -7.048  1 76.61   ? 41  GLY   B CA   1 ? 1 
ATOM   427  C C    . GLY   A 1 29  ? 30.518 -4.591  -7.933  1 81.959  ? 41  GLY   B C    1 ? 1 
ATOM   428  O O    . GLY   A 1 29  ? 30.502 -4.48   -9.162  1 88.089  ? 41  GLY   B O    1 ? 1 
ATOM   429  H H    . GLY   A 1 29  ? 27.907 -3.124  -7.848  1 72.636  ? 41  GLY   B H    1 c 1 
ATOM   430  H HA2  . GLY   A 1 29  ? 30.366 -3.011  -6.595  1 77.346  ? 41  GLY   B HA2  1 c 1 
ATOM   431  H HA3  . GLY   A 1 29  ? 29.257 -4.129  -6.353  1 74.009  ? 41  GLY   B HA3  1 c 1 
ATOM   432  N N    . ASN   A 1 30  ? 31.193 -5.546  -7.283  1 83.76   ? 42  ASN   B N    1 ? 1 
ATOM   433  C CA   . ASN   A 1 30  ? 31.995 -6.554  -7.958  1 90.651  ? 42  ASN   B CA   1 ? 1 
ATOM   434  C C    . ASN   A 1 30  ? 31.783 -7.891  -7.257  1 91.018  ? 42  ASN   B C    1 ? 1 
ATOM   435  O O    . ASN   A 1 30  ? 31.424 -7.941  -6.086  1 84.405  ? 42  ASN   B O    1 ? 1 
ATOM   436  C CB   . ASN   A 1 30  ? 33.467 -6.165  -7.964  1 99.05   ? 42  ASN   B CB   1 ? 1 
ATOM   437  C CG   . ASN   A 1 30  ? 33.919 -5.733  -6.589  1 100.692 ? 42  ASN   B CG   1 ? 1 
ATOM   438  O OD1  . ASN   A 1 30  ? 33.893 -6.531  -5.646  1 96.689  ? 42  ASN   B OD1  1 ? 1 
ATOM   439  N ND2  . ASN   A 1 30  ? 34.347 -4.485  -6.45   1 103.731 ? 42  ASN   B ND2  1 ? 1 
ATOM   440  H H    . ASN   A 1 30  ? 31.144 -5.571  -6.371  1 81.959  ? 42  ASN   B H    1 c 1 
ATOM   441  H HA   . ASN   A 1 30  ? 31.696 -6.629  -8.892  1 92.643  ? 42  ASN   B HA   1 c 1 
ATOM   442  H HB2  . ASN   A 1 30  ? 34.003 -6.929  -8.256  1 101.354 ? 42  ASN   B HB2  1 c 1 
ATOM   443  H HB3  . ASN   A 1 30  ? 33.607 -5.433  -8.598  1 100.769 ? 42  ASN   B HB3  1 c 1 
ATOM   444  H HD21 . ASN   A 1 30  ? 34.716 -4.228  -5.686  1 102.829 ? 42  ASN   B HD21 1 c 1 
ATOM   445  H HD22 . ASN   A 1 30  ? 34.264 -3.906  -7.118  1 104.256 ? 42  ASN   B HD22 1 c 1 
ATOM   446  N N    . GLY   A 1 31  ? 32.044 -8.987  -7.969  1 97.003  ? 43  GLY   B N    1 ? 1 
ATOM   447  C CA   . GLY   A 1 31  ? 31.587 -10.291 -7.53   1 95.634  ? 43  GLY   B CA   1 ? 1 
ATOM   448  C C    . GLY   A 1 31  ? 30.148 -10.508 -7.987  1 91.138  ? 43  GLY   B C    1 ? 1 
ATOM   449  O O    . GLY   A 1 31  ? 29.517 -9.594  -8.513  1 89.926  ? 43  GLY   B O    1 ? 1 
ATOM   450  H H    . GLY   A 1 31  ? 32.523 -8.921  -8.745  1 99.442  ? 43  GLY   B H    1 c 1 
ATOM   451  H HA2  . GLY   A 1 31  ? 32.169 -10.989 -7.913  1 98.143  ? 43  GLY   B HA2  1 c 1 
ATOM   452  H HA3  . GLY   A 1 31  ? 31.641 -10.349 -6.547  1 93.091  ? 43  GLY   B HA3  1 c 1 
ATOM   453  N N    . GLU   A 1 32  ? 29.665 -11.742 -7.838  1 85.277  ? 44  GLU   B N    1 ? 1 
ATOM   454  C CA   . GLU   A 1 32  ? 28.314 -12.079 -8.239  1 81.777  ? 44  GLU   B CA   1 ? 1 
ATOM   455  C C    . GLU   A 1 32  ? 27.492 -12.356 -6.977  1 74.847  ? 44  GLU   B C    1 ? 1 
ATOM   456  O O    . GLU   A 1 32  ? 26.274 -12.299 -7.036  1 69.968  ? 44  GLU   B O    1 ? 1 
ATOM   457  C CB   . GLU   A 1 32  ? 28.39  -13.17  -9.317  1 83.33   ? 44  GLU   B CB   1 ? 1 
ATOM   458  H H    . GLU   A 1 32  ? 30.203 -12.396 -7.494  1 87.05   ? 44  GLU   B H    1 c 1 
ATOM   459  H HA   . GLU   A 1 32  ? 27.919 -11.283 -8.676  1 80.739  ? 44  GLU   B HA   1 c 1 
ATOM   460  H HB2  . GLU   A 1 32  ? 29.427 -13.292 -9.473  0 30      ? 44  GLU   B HB2  1 c 1 
ATOM   461  H HB3  . GLU   A 1 32  ? 27.582 -13.439 -9.622  0 30      ? 44  GLU   B HB3  1 c 1 
ATOM   462  N N    . GLU   A 1 33  ? 28.156 -12.515 -5.818  1 72.31   ? 45  GLU   B N    1 ? 1 
ATOM   463  C CA   . GLU   A 1 33  ? 27.515 -13.068 -4.63   1 72.019  ? 45  GLU   B CA   1 ? 1 
ATOM   464  C C    . GLU   A 1 33  ? 26.941 -11.939 -3.773  1 65.837  ? 45  GLU   B C    1 ? 1 
ATOM   465  O O    . GLU   A 1 33  ? 27.61  -10.947 -3.517  1 64.673  ? 45  GLU   B O    1 ? 1 
ATOM   466  C CB   . GLU   A 1 33  ? 28.496 -13.951 -3.853  1 71.554  ? 45  GLU   B CB   1 ? 1 
ATOM   467  H H    . GLU   A 1 33  ? 29.028 -12.25  -5.758  1 74.701  ? 45  GLU   B H    1 c 1 
ATOM   468  H HA   . GLU   A 1 33  ? 26.765 -13.644 -4.928  1 70.659  ? 45  GLU   B HA   1 c 1 
ATOM   469  H HB2  . GLU   A 1 33  ? 29.341 -13.75  -4.102  0 30      ? 45  GLU   B HB2  1 c 1 
ATOM   470  H HB3  . GLU   A 1 33  ? 27.892 -14.673 -3.396  0 30      ? 45  GLU   B HB3  1 c 1 
ATOM   471  N N    . THR   A 1 34  ? 25.666 -12.079 -3.388  1 66.082  ? 46  THR   B N    1 ? 1 
ATOM   472  C CA   . THR   A 1 34  ? 24.959 -11.11  -2.568  1 59.658  ? 46  THR   B CA   1 ? 1 
ATOM   473  C C    . THR   A 1 34  ? 24.64  -11.789 -1.252  1 57.577  ? 46  THR   B C    1 ? 1 
ATOM   474  O O    . THR   A 1 34  ? 24.257 -12.959 -1.238  1 64.1    ? 46  THR   B O    1 ? 1 
ATOM   475  C CB   . THR   A 1 34  ? 23.673 -10.637 -3.231  1 58.036  ? 46  THR   B CB   1 ? 1 
ATOM   476  O OG1  . THR   A 1 34  ? 22.886 -11.825 -3.218  1 58.585  ? 46  THR   B OG1  1 ? 1 
ATOM   477  C CG2  . THR   A 1 34  ? 23.894 -10.118 -4.637  1 58.157  ? 46  THR   B CG2  1 ? 1 
ATOM   478  H H    . THR   A 1 34  ? 25.211 -12.826 -3.654  1 65.36   ? 46  THR   B H    1 c 1 
ATOM   479  H HA   . THR   A 1 34  ? 25.542 -10.338 -2.408  1 59.752  ? 46  THR   B HA   1 c 1 
ATOM   480  H HB   . THR   A 1 34  ? 23.24  -9.943  -2.679  1 55.63   ? 46  THR   B HB   1 c 1 
ATOM   481  H HG1  . THR   A 1 34  ? 23.277 -12.459 -3.659  0 30      ? 46  THR   B HG1  1 c 1 
ATOM   482  H HG21 . THR   A 1 34  ? 23.055 -9.78   -4.994  1 58.12   ? 46  THR   B HG21 1 c 1 
ATOM   483  H HG22 . THR   A 1 34  ? 24.219 -10.838 -5.203  1 61.009  ? 46  THR   B HG22 1 c 1 
ATOM   484  H HG23 . THR   A 1 34  ? 24.55  -9.4    -4.62   1 58.956  ? 46  THR   B HG23 1 c 1 
ATOM   485  N N    . PRO   A 1 35  ? 24.767 -11.079 -0.11   1 53.319  ? 47  PRO   B N    1 ? 1 
ATOM   486  C CA   . PRO   A 1 35  ? 24.789 -11.749 1.185   1 52.513  ? 47  PRO   B CA   1 ? 1 
ATOM   487  C C    . PRO   A 1 35  ? 23.579 -12.639 1.435   1 50.008  ? 47  PRO   B C    1 ? 1 
ATOM   488  O O    . PRO   A 1 35  ? 22.479 -12.309 1.023   1 54.776  ? 47  PRO   B O    1 ? 1 
ATOM   489  C CB   . PRO   A 1 35  ? 24.909 -10.605 2.188   1 50.483  ? 47  PRO   B CB   1 ? 1 
ATOM   490  C CG   . PRO   A 1 35  ? 24.604 -9.341  1.418   1 51.574  ? 47  PRO   B CG   1 ? 1 
ATOM   491  C CD   . PRO   A 1 35  ? 24.907 -9.62   -0.017  1 51.617  ? 47  PRO   B CD   1 ? 1 
ATOM   492  H HA   . PRO   A 1 35  ? 25.601 -12.295 1.239   1 53.985  ? 47  PRO   B HA   1 c 1 
ATOM   493  H HB2  . PRO   A 1 35  ? 24.28  -10.724 2.924   1 49.864  ? 47  PRO   B HB2  1 c 1 
ATOM   494  H HB3  . PRO   A 1 35  ? 25.811 -10.57  2.562   1 52.283  ? 47  PRO   B HB3  1 c 1 
ATOM   495  H HG2  . PRO   A 1 35  ? 23.663 -9.095  1.524   1 49.014  ? 47  PRO   B HG2  1 c 1 
ATOM   496  H HG3  . PRO   A 1 35  ? 25.156 -8.602  1.742   1 50.701  ? 47  PRO   B HG3  1 c 1 
ATOM   497  H HD2  . PRO   A 1 35  ? 24.268 -9.174  -0.605  1 51.337  ? 47  PRO   B HD2  1 c 1 
ATOM   498  H HD3  . PRO   A 1 35  ? 25.813 -9.341  -0.252  1 53.59   ? 47  PRO   B HD3  1 c 1 
ATOM   499  N N    . MET   A 1 36  ? 23.817 -13.764 2.109   1 48.5    ? 48  MET   B N    1 ? 1 
ATOM   500  C CA   . MET   A 1 36  ? 22.793 -14.71  2.505   1 49.504  ? 48  MET   B CA   1 ? 1 
ATOM   501  C C    . MET   A 1 36  ? 22.347 -14.38  3.926   1 47.757  ? 48  MET   B C    1 ? 1 
ATOM   502  O O    . MET   A 1 36  ? 23.068 -13.714 4.672   1 45.273  ? 48  MET   B O    1 ? 1 
ATOM   503  C CB   . MET   A 1 36  ? 23.34  -16.141 2.555   1 54.005  ? 48  MET   B CB   1 ? 1 
ATOM   504  C CG   . MET   A 1 36  ? 24.068 -16.597 1.299   1 59.271  ? 48  MET   B CG   1 ? 1 
ATOM   505  S SD   . MET   A 1 36  ? 22.936 -17.286 0.077   1 66.705  ? 48  MET   B SD   1 ? 1 
ATOM   506  C CE   . MET   A 1 36  ? 21.941 -16.051 -0.761  1 60.334  ? 48  MET   B CE   1 ? 1 
ATOM   507  H H    . MET   A 1 36  ? 24.682 -13.954 2.334   1 50.75   ? 48  MET   B H    1 c 1 
ATOM   508  H HA   . MET   A 1 36  ? 22.024 -14.652 1.884   1 49.177  ? 48  MET   B HA   1 c 1 
ATOM   509  H HB2  . MET   A 1 36  ? 23.955 -16.212 3.316   1 54.765  ? 48  MET   B HB2  1 c 1 
ATOM   510  H HB3  . MET   A 1 36  ? 22.591 -16.752 2.724   1 54.575  ? 48  MET   B HB3  1 c 1 
ATOM   511  H HG2  . MET   A 1 36  ? 24.541 -15.841 0.9     1 59.156  ? 48  MET   B HG2  1 c 1 
ATOM   512  H HG3  . MET   A 1 36  ? 24.73  -17.277 1.536   1 61.542  ? 48  MET   B HG3  1 c 1 
ATOM   513  H HE1  . MET   A 1 36  ? 21.381 -16.487 -1.429  1 62.514  ? 48  MET   B HE1  1 c 1 
ATOM   514  H HE2  . MET   A 1 36  ? 21.377 -15.594 -0.111  1 59.311  ? 48  MET   B HE2  1 c 1 
ATOM   515  H HE3  . MET   A 1 36  ? 22.528 -15.406 -1.197  1 61.193  ? 48  MET   B HE3  1 c 1 
ATOM   516  N N    . ILE   A 1 37  ? 21.175 -14.91  4.308   1 45.067  ? 49  ILE   B N    1 ? 1 
ATOM   517  C CA   . ILE   A 1 37  ? 20.643 -14.648 5.629   1 45.075  ? 49  ILE   B CA   1 ? 1 
ATOM   518  C C    . ILE   A 1 37  ? 21.598 -15.234 6.655   1 47.271  ? 49  ILE   B C    1 ? 1 
ATOM   519  O O    . ILE   A 1 37  ? 22.086 -16.362 6.495   1 47.108  ? 49  ILE   B O    1 ? 1 
ATOM   520  C CB   . ILE   A 1 37  ? 19.185 -15.123 5.793   1 47.861  ? 49  ILE   B CB   1 ? 1 
ATOM   521  C CG1  . ILE   A 1 37  ? 18.276 -14.232 4.905   1 48.319  ? 49  ILE   B CG1  1 ? 1 
ATOM   522  C CG2  . ILE   A 1 37  ? 18.758 -15.098 7.272   1 47.663  ? 49  ILE   B CG2  1 ? 1 
ATOM   523  C CD1  . ILE   A 1 37  ? 16.795 -14.508 4.991   1 48.998  ? 49  ILE   B CD1  1 ? 1 
ATOM   524  H H    . ILE   A 1 37  ? 20.703 -15.442 3.733   1 46.596  ? 49  ILE   B H    1 c 1 
ATOM   525  H HA   . ILE   A 1 37  ? 20.643 -13.678 5.75    1 43.939  ? 49  ILE   B HA   1 c 1 
ATOM   526  H HB   . ILE   A 1 37  ? 19.124 -16.043 5.468   1 49.302  ? 49  ILE   B HB   1 c 1 
ATOM   527  H HG12 . ILE   A 1 37  ? 18.428 -13.297 5.151   1 46.373  ? 49  ILE   B HG12 1 c 1 
ATOM   528  H HG13 . ILE   A 1 37  ? 18.555 -14.339 3.974   1 48.29   ? 49  ILE   B HG13 1 c 1 
ATOM   529  H HG21 . ILE   A 1 37  ? 17.807 -15.282 7.342   1 47.898  ? 49  ILE   B HG21 1 c 1 
ATOM   530  H HG22 . ILE   A 1 37  ? 18.943 -14.221 7.65    1 46.476  ? 49  ILE   B HG22 1 c 1 
ATOM   531  H HG23 . ILE   A 1 37  ? 19.251 -15.773 7.767   1 49.334  ? 49  ILE   B HG23 1 c 1 
ATOM   532  H HD11 . ILE   A 1 37  ? 16.637 -15.468 4.91    1 50.634  ? 49  ILE   B HD11 1 c 1 
ATOM   533  H HD12 . ILE   A 1 37  ? 16.334 -14.042 4.268   1 48.252  ? 49  ILE   B HD12 1 c 1 
ATOM   534  H HD13 . ILE   A 1 37  ? 16.45  -14.195 5.849   1 48.297  ? 49  ILE   B HD13 1 c 1 
ATOM   535  N N    . GLY   A 1 38  ? 21.863 -14.431 7.701   1 44.911  ? 50  GLY   B N    1 ? 1 
ATOM   536  C CA   . GLY   A 1 38  ? 22.761 -14.859 8.759   1 45.791  ? 50  GLY   B CA   1 ? 1 
ATOM   537  C C    . GLY   A 1 38  ? 24.166 -14.284 8.582   1 45.389  ? 50  GLY   B C    1 ? 1 
ATOM   538  O O    . GLY   A 1 38  ? 24.911 -14.224 9.557   1 46.913  ? 50  GLY   B O    1 ? 1 
ATOM   539  H H    . GLY   A 1 38  ? 21.475 -13.605 7.754   1 43.421  ? 50  GLY   B H    1 c 1 
ATOM   540  H HA2  . GLY   A 1 38  ? 22.394 -14.566 9.626   1 45.643  ? 50  GLY   B HA2  1 c 1 
ATOM   541  H HA3  . GLY   A 1 38  ? 22.807 -15.844 8.769   1 47.561  ? 50  GLY   B HA3  1 c 1 
ATOM   542  N N    . ASP   A 1 39  ? 24.516 -13.865 7.363   1 43.7    ? 51  ASP   B N    1 ? 1 
ATOM   543  C CA   . ASP   A 1 39  ? 25.834 -13.292 7.098   1 49.604  ? 51  ASP   B CA   1 ? 1 
ATOM   544  C C    . ASP   A 1 39  ? 26.067 -12.038 7.955   1 49.457  ? 51  ASP   B C    1 ? 1 
ATOM   545  O O    . ASP   A 1 39  ? 25.13  -11.285 8.235   1 50.68   ? 51  ASP   B O    1 ? 1 
ATOM   546  C CB   . ASP   A 1 39  ? 26.035 -12.943 5.622   1 48.592  ? 51  ASP   B CB   1 ? 1 
ATOM   547  C CG   . ASP   A 1 39  ? 26.289 -14.087 4.634   1 49.71   ? 51  ASP   B CG   1 ? 1 
ATOM   548  O OD1  . ASP   A 1 39  ? 26.459 -15.271 5.079   1 49.311  ? 51  ASP   B OD1  1 ? 1 
ATOM   549  O OD2  . ASP   A 1 39  ? 26.331 -13.779 3.398   1 46.52   ? 51  ASP   B OD2  1 ? 1 
ATOM   550  H H    . ASP   A 1 39  ? 23.924 -13.939 6.672   1 44.011  ? 51  ASP   B H    1 c 1 
ATOM   551  H HA   . ASP   A 1 39  ? 26.511 -13.964 7.34    1 50.782  ? 51  ASP   B HA   1 c 1 
ATOM   552  H HB2  . ASP   A 1 39  ? 25.245 -12.453 5.315   1 46.586  ? 51  ASP   B HB2  1 c 1 
ATOM   553  H HB3  . ASP   A 1 39  ? 26.799 -12.332 5.558   1 49.145  ? 51  ASP   B HB3  1 c 1 
ATOM   554  N N    . LYS   A 1 40  ? 27.325 -11.835 8.382   1 51.576  ? 52  LYS   B N    1 ? 1 
ATOM   555  C CA   . LYS   A 1 40  ? 27.741 -10.618 9.067   1 53.256  ? 52  LYS   B CA   1 ? 1 
ATOM   556  C C    . LYS   A 1 40  ? 28.096 -9.573  8.008   1 50.318  ? 52  LYS   B C    1 ? 1 
ATOM   557  O O    . LYS   A 1 40  ? 28.876 -9.842  7.106   1 49.554  ? 52  LYS   B O    1 ? 1 
ATOM   558  C CB   . LYS   A 1 40  ? 28.897 -10.868 10.057  1 55.339  ? 52  LYS   B CB   1 ? 1 
ATOM   559  C CG   . LYS   A 1 40  ? 29.099 -9.763  11.109  1 55.603  ? 52  LYS   B CG   1 ? 1 
ATOM   560  C CD   . LYS   A 1 40  ? 30.404 -9.875  11.898  1 63.284  ? 52  LYS   B CD   1 ? 1 
ATOM   561  C CE   . LYS   A 1 40  ? 30.6   -8.851  12.987  1 63.384  ? 52  LYS   B CE   1 ? 1 
ATOM   562  N NZ   . LYS   A 1 40  ? 32.005 -8.692  13.371  1 67.531  ? 52  LYS   B NZ   1 ? 1 
ATOM   563  H H    . LYS   A 1 40  ? 27.95  -12.486 8.237   1 53.881  ? 52  LYS   B H    1 c 1 
ATOM   564  H HA   . LYS   A 1 40  ? 26.969 -10.281 9.589   1 50.846  ? 52  LYS   B HA   1 c 1 
ATOM   565  H HB2  . LYS   A 1 40  ? 28.731 -11.714 10.526  1 56.507  ? 52  LYS   B HB2  1 c 1 
ATOM   566  H HB3  . LYS   A 1 40  ? 29.73  -10.967 9.549   1 57.206  ? 52  LYS   B HB3  1 c 1 
ATOM   567  H HG2  . LYS   A 1 40  ? 29.076 -8.893  10.654  1 55.219  ? 52  LYS   B HG2  1 c 1 
ATOM   568  H HG3  . LYS   A 1 40  ? 28.344 -9.791  11.737  1 55.44   ? 52  LYS   B HG3  1 c 1 
ATOM   569  H HD2  . LYS   A 1 40  ? 30.443 -10.77  12.301  1 63.584  ? 52  LYS   B HD2  1 c 1 
ATOM   570  H HD3  . LYS   A 1 40  ? 31.152 -9.812  11.267  1 63.408  ? 52  LYS   B HD3  1 c 1 
ATOM   571  H HE2  . LYS   A 1 40  ? 30.266 -7.996  12.67   1 61.807  ? 52  LYS   B HE2  1 c 1 
ATOM   572  H HE3  . LYS   A 1 40  ? 30.082 -9.106  13.771  1 63.653  ? 52  LYS   B HE3  1 c 1 
ATOM   573  H HZ1  . LYS   A 1 40  ? 32.495 -8.445  12.651  1 67.899  ? 52  LYS   B HZ1  1 c 1 
ATOM   574  H HZ2  . LYS   A 1 40  ? 32.324 -9.476  13.694  1 69.653  ? 52  LYS   B HZ2  1 c 1 
ATOM   575  H HZ3  . LYS   A 1 40  ? 32.076 -8.055  14.012  1 68.711  ? 52  LYS   B HZ3  1 c 1 
ATOM   576  N N    . VAL   A 1 41  ? 27.48  -8.39   8.1     1 51.691  ? 53  VAL   B N    1 ? 1 
ATOM   577  C CA   . VAL   A 1 41  ? 27.498 -7.425  7.013   1 52.532  ? 53  VAL   B CA   1 ? 1 
ATOM   578  C C    . VAL   A 1 41  ? 28.023 -6.08   7.511   1 51.152  ? 53  VAL   B C    1 ? 1 
ATOM   579  O O    . VAL   A 1 41  ? 27.574 -5.609  8.557   1 52.357  ? 53  VAL   B O    1 ? 1 
ATOM   580  C CB   . VAL   A 1 41  ? 26.065 -7.31   6.457   1 50.923  ? 53  VAL   B CB   1 ? 1 
ATOM   581  C CG1  . VAL   A 1 41  ? 25.885 -6.046  5.628   1 51.524  ? 53  VAL   B CG1  1 ? 1 
ATOM   582  C CG2  . VAL   A 1 41  ? 25.688 -8.533  5.633   1 48.685  ? 53  VAL   B CG2  1 ? 1 
ATOM   583  H H    . VAL   A 1 41  ? 27.036 -8.174  8.869   1 50.666  ? 53  VAL   B H    1 c 1 
ATOM   584  H HA   . VAL   A 1 41  ? 28.085 -7.754  6.306   1 53.073  ? 53  VAL   B HA   1 c 1 
ATOM   585  H HB   . VAL   A 1 41  ? 25.454 -7.26   7.229   1 49.629  ? 53  VAL   B HB   1 c 1 
ATOM   586  H HG11 . VAL   A 1 41  ? 26.608 -5.975  4.982   1 52.288  ? 53  VAL   B HG11 1 c 1 
ATOM   587  H HG12 . VAL   A 1 41  ? 25.892 -5.268  6.21    1 50.833  ? 53  VAL   B HG12 1 c 1 
ATOM   588  H HG13 . VAL   A 1 41  ? 25.036 -6.087  5.158   1 49.334  ? 53  VAL   B HG13 1 c 1 
ATOM   589  H HG21 . VAL   A 1 41  ? 24.779 -8.435  5.303   1 47.673  ? 53  VAL   B HG21 1 c 1 
ATOM   590  H HG22 . VAL   A 1 41  ? 25.747 -9.329  6.188   1 50.086  ? 53  VAL   B HG22 1 c 1 
ATOM   591  H HG23 . VAL   A 1 41  ? 26.298 -8.618  4.881   1 50.435  ? 53  VAL   B HG23 1 c 1 
ATOM   592  N N    . TYR   A 1 42  ? 28.913 -5.458  6.717   1 49.575  ? 54  TYR   B N    1 ? 1 
ATOM   593  C CA   . TYR   A 1 42  ? 29.568 -4.195  7.05    1 51.54   ? 54  TYR   B CA   1 ? 1 
ATOM   594  C C    . TYR   A 1 42  ? 29.156 -3.122  6.031   1 46.758  ? 54  TYR   B C    1 ? 1 
ATOM   595  O O    . TYR   A 1 42  ? 29.379 -3.295  4.833   1 45.726  ? 54  TYR   B O    1 ? 1 
ATOM   596  C CB   . TYR   A 1 42  ? 31.096 -4.415  7.033   1 58.287  ? 54  TYR   B CB   1 ? 1 
ATOM   597  C CG   . TYR   A 1 42  ? 31.648 -5.503  7.954   1 62.026  ? 54  TYR   B CG   1 ? 1 
ATOM   598  C CD1  . TYR   A 1 42  ? 31.516 -6.855  7.625   1 62.939  ? 54  TYR   B CD1  1 ? 1 
ATOM   599  C CD2  . TYR   A 1 42  ? 32.278 -5.196  9.157   1 64.312  ? 54  TYR   B CD2  1 ? 1 
ATOM   600  C CE1  . TYR   A 1 42  ? 31.977 -7.862  8.458   1 64.678  ? 54  TYR   B CE1  1 ? 1 
ATOM   601  C CE2  . TYR   A 1 42  ? 32.752 -6.196  9.999   1 69.723  ? 54  TYR   B CE2  1 ? 1 
ATOM   602  C CZ   . TYR   A 1 42  ? 32.59  -7.532  9.653   1 69.969  ? 54  TYR   B CZ   1 ? 1 
ATOM   603  O OH   . TYR   A 1 42  ? 33.043 -8.521  10.47   1 74.18   ? 54  TYR   B OH   1 ? 1 
ATOM   604  H H    . TYR   A 1 42  ? 29.121 -5.847  5.917   1 50.791  ? 54  TYR   B H    1 c 1 
ATOM   605  H HA   . TYR   A 1 42  ? 29.29  -3.91   7.96    1 51.037  ? 54  TYR   B HA   1 c 1 
ATOM   606  H HB2  . TYR   A 1 42  ? 31.362 -4.626  6.111   1 58.42   ? 54  TYR   B HB2  1 c 1 
ATOM   607  H HB3  . TYR   A 1 42  ? 31.528 -3.563  7.267   1 59.478  ? 54  TYR   B HB3  1 c 1 
ATOM   608  H HD1  . TYR   A 1 42  ? 31.083 -7.091  6.82    1 60.928  ? 54  TYR   B HD1  1 c 1 
ATOM   609  H HD2  . TYR   A 1 42  ? 32.378 -4.292  9.412   1 65.684  ? 54  TYR   B HD2  1 c 1 
ATOM   610  H HE1  . TYR   A 1 42  ? 31.87  -8.766  8.215   1 65.309  ? 54  TYR   B HE1  1 c 1 
ATOM   611  H HE2  . TYR   A 1 42  ? 33.168 -5.969  10.813  1 71.396  ? 54  TYR   B HE2  1 c 1 
ATOM   612  H HH   . TYR   A 1 42  ? 32.782 -9.305  10.094  0 30      ? 54  TYR   B HH   1 c 1 
ATOM   613  N N    . VAL   A 1 43  ? 28.564 -2.01   6.488   1 45.774  ? 55  VAL   B N    1 ? 1 
ATOM   614  C CA   . VAL   A 1 43  ? 28.164 -0.941  5.575   1 46.23   ? 55  VAL   B CA   1 ? 1 
ATOM   615  C C    . VAL   A 1 43  ? 28.588 0.431   6.115   1 49.154  ? 55  VAL   B C    1 ? 1 
ATOM   616  O O    . VAL   A 1 43  ? 28.77  0.617   7.313   1 49.507  ? 55  VAL   B O    1 ? 1 
ATOM   617  C CB   . VAL   A 1 43  ? 26.652 -0.886  5.287   1 42.672  ? 55  VAL   B CB   1 ? 1 
ATOM   618  C CG1  . VAL   A 1 43  ? 26.092 -2.225  4.848   1 42.206  ? 55  VAL   B CG1  1 ? 1 
ATOM   619  C CG2  . VAL   A 1 43  ? 25.882 -0.366  6.492   1 41.845  ? 55  VAL   B CG2  1 ? 1 
ATOM   620  H H    . VAL   A 1 43  ? 28.407 -1.912  7.383   1 46.062  ? 55  VAL   B H    1 c 1 
ATOM   621  H HA   . VAL   A 1 43  ? 28.625 -1.083  4.728   1 47.214  ? 55  VAL   B HA   1 c 1 
ATOM   622  H HB   . VAL   A 1 43  ? 26.519 -0.247  4.548   1 42.927  ? 55  VAL   B HB   1 c 1 
ATOM   623  H HG11 . VAL   A 1 43  ? 26.214 -2.878  5.558   1 42.11   ? 55  VAL   B HG11 1 c 1 
ATOM   624  H HG12 . VAL   A 1 43  ? 26.556 -2.525  4.049   1 42.915  ? 55  VAL   B HG12 1 c 1 
ATOM   625  H HG13 . VAL   A 1 43  ? 25.143 -2.133  4.655   1 40.072  ? 55  VAL   B HG13 1 c 1 
ATOM   626  H HG21 . VAL   A 1 43  ? 24.93  -0.42   6.313   1 39.807  ? 55  VAL   B HG21 1 c 1 
ATOM   627  H HG22 . VAL   A 1 43  ? 26.122 0.56    6.662   1 42.713  ? 55  VAL   B HG22 1 c 1 
ATOM   628  H HG23 . VAL   A 1 43  ? 26.095 -0.905  7.273   1 42.286  ? 55  VAL   B HG23 1 c 1 
ATOM   629  N N    . HIS   A 1 44  ? 28.7   1.403   5.195   1 51.163  ? 56  HIS   B N    1 ? 1 
ATOM   630  C CA   . HIS   A 1 44  ? 28.486 2.809   5.515   1 53.348  ? 56  HIS   B CA   1 ? 1 
ATOM   631  C C    . HIS   A 1 44  ? 27.123 3.229   4.985   1 49.544  ? 56  HIS   B C    1 ? 1 
ATOM   632  O O    . HIS   A 1 44  ? 26.638 2.657   4.012   1 46.804  ? 56  HIS   B O    1 ? 1 
ATOM   633  C CB   . HIS   A 1 44  ? 29.603 3.704   4.964   1 59.043  ? 56  HIS   B CB   1 ? 1 
ATOM   634  C CG   . HIS   A 1 44  ? 30.791 3.759   5.88    1 60.412  ? 56  HIS   B CG   1 ? 1 
ATOM   635  N ND1  . HIS   A 1 44  ? 30.675 4.154   7.2     1 60.928  ? 56  HIS   B ND1  1 ? 1 
ATOM   636  C CD2  . HIS   A 1 44  ? 32.084 3.447   5.685   1 61.214  ? 56  HIS   B CD2  1 ? 1 
ATOM   637  C CE1  . HIS   A 1 44  ? 31.867 4.073   7.771   1 63.689  ? 56  HIS   B CE1  1 ? 1 
ATOM   638  N NE2  . HIS   A 1 44  ? 32.723 3.633   6.868   1 63.917  ? 56  HIS   B NE2  1 ? 1 
ATOM   639  H H    . HIS   A 1 44  ? 28.919 1.178   4.337   1 51.595  ? 56  HIS   B H    1 c 1 
ATOM   640  H HA   . HIS   A 1 44  ? 28.47  2.897   6.498   1 53.466  ? 56  HIS   B HA   1 c 1 
ATOM   641  H HB2  . HIS   A 1 44  ? 29.886 3.358   4.09    1 58.538  ? 56  HIS   B HB2  1 c 1 
ATOM   642  H HB3  . HIS   A 1 44  ? 29.251 4.613   4.839   1 58.032  ? 56  HIS   B HB3  1 c 1 
ATOM   643  H HD1  . HIS   A 1 44  ? 29.942 4.432   7.567   0 30      ? 56  HIS   B HD1  1 c 1 
ATOM   644  H HD2  . HIS   A 1 44  ? 32.473 3.131   4.893   1 62.729  ? 56  HIS   B HD2  1 c 1 
ATOM   645  H HE1  . HIS   A 1 44  ? 32.068 4.293   8.665   1 65.184  ? 56  HIS   B HE1  1 c 1 
ATOM   646  H HE2  . HIS   A 1 44  ? 33.579 3.421   7.024   0 30      ? 56  HIS   B HE2  1 c 1 
ATOM   647  N N    . TYR   A 1 45  ? 26.487 4.191   5.667   1 48.783  ? 57  TYR   B N    1 ? 1 
ATOM   648  C CA   . TYR   A 1 45  ? 25.225 4.724   5.187   1 43.908  ? 57  TYR   B CA   1 ? 1 
ATOM   649  C C    . TYR   A 1 45  ? 25.087 6.215   5.509   1 43.662  ? 57  TYR   B C    1 ? 1 
ATOM   650  O O    . TYR   A 1 45  ? 25.795 6.745   6.345   1 46.691  ? 57  TYR   B O    1 ? 1 
ATOM   651  C CB   . TYR   A 1 45  ? 24.081 3.892   5.764   1 38.837  ? 57  TYR   B CB   1 ? 1 
ATOM   652  C CG   . TYR   A 1 45  ? 23.821 4.168   7.233   1 39.23   ? 57  TYR   B CG   1 ? 1 
ATOM   653  C CD1  . TYR   A 1 45  ? 24.592 3.577   8.239   1 41.172  ? 57  TYR   B CD1  1 ? 1 
ATOM   654  C CD2  . TYR   A 1 45  ? 22.845 5.08    7.605   1 36.491  ? 57  TYR   B CD2  1 ? 1 
ATOM   655  C CE1  . TYR   A 1 45  ? 24.365 3.863   9.58    1 40.459  ? 57  TYR   B CE1  1 ? 1 
ATOM   656  C CE2  . TYR   A 1 45  ? 22.628 5.39    8.932   1 37.987  ? 57  TYR   B CE2  1 ? 1 
ATOM   657  C CZ   . TYR   A 1 45  ? 23.366 4.759   9.921   1 38.866  ? 57  TYR   B CZ   1 ? 1 
ATOM   658  O OH   . TYR   A 1 45  ? 23.098 5.116   11.195  1 37.58   ? 57  TYR   B OH   1 ? 1 
ATOM   659  H H    . TYR   A 1 45  ? 26.846 4.519   6.441   1 49.58   ? 57  TYR   B H    1 c 1 
ATOM   660  H HA   . TYR   A 1 45  ? 25.209 4.623   4.201   1 43.648  ? 57  TYR   B HA   1 c 1 
ATOM   661  H HB2  . TYR   A 1 45  ? 23.264 4.083   5.252   1 37.997  ? 57  TYR   B HB2  1 c 1 
ATOM   662  H HB3  . TYR   A 1 45  ? 24.297 2.94    5.65    1 38.975  ? 57  TYR   B HB3  1 c 1 
ATOM   663  H HD1  . TYR   A 1 45  ? 25.263 2.956   8.006   1 41.359  ? 57  TYR   B HD1  1 c 1 
ATOM   664  H HD2  . TYR   A 1 45  ? 22.332 5.509   6.939   1 36.491  ? 57  TYR   B HD2  1 c 1 
ATOM   665  H HE1  . TYR   A 1 45  ? 24.879 3.446   10.251  1 41.87   ? 57  TYR   B HE1  1 c 1 
ATOM   666  H HE2  . TYR   A 1 45  ? 21.948 5.996   9.166   1 37.487  ? 57  TYR   B HE2  1 c 1 
ATOM   667  H HH   . TYR   A 1 45  ? 23.556 4.708   11.724  0 30      ? 57  TYR   B HH   1 c 1 
ATOM   668  N N    . LYS   A 1 46  ? 24.148 6.866   4.808   1 42.085  ? 58  LYS   B N    1 ? 1 
ATOM   669  C CA   . LYS   A 1 46  ? 23.608 8.157   5.159   1 43.309  ? 58  LYS   B CA   1 ? 1 
ATOM   670  C C    . LYS   A 1 46  ? 22.098 8.042   5.065   1 39.76   ? 58  LYS   B C    1 ? 1 
ATOM   671  O O    . LYS   A 1 46  ? 21.58  7.527   4.088   1 41.909  ? 58  LYS   B O    1 ? 1 
ATOM   672  C CB   . LYS   A 1 46  ? 24.188 9.225   4.225   1 51.52   ? 58  LYS   B CB   1 ? 1 
ATOM   673  C CG   . LYS   A 1 46  ? 25.621 9.584   4.577   1 57.777  ? 58  LYS   B CG   1 ? 1 
ATOM   674  C CD   . LYS   A 1 46  ? 26.621 9.88    3.458   1 63.254  ? 58  LYS   B CD   1 ? 1 
ATOM   675  C CE   . LYS   A 1 46  ? 26.285 11.04   2.614   1 64.24   ? 58  LYS   B CE   1 ? 1 
ATOM   676  N NZ   . LYS   A 1 46  ? 27.463 11.604  1.956   1 69.452  ? 58  LYS   B NZ   1 ? 1 
ATOM   677  H H    . LYS   A 1 46  ? 23.83  6.465   4.05    1 41.319  ? 58  LYS   B H    1 c 1 
ATOM   678  H HA   . LYS   A 1 46  ? 23.861 8.363   6.094   1 44.935  ? 58  LYS   B HA   1 c 1 
ATOM   679  H HB2  . LYS   A 1 46  ? 24.161 8.898   3.3     1 50.396  ? 58  LYS   B HB2  1 c 1 
ATOM   680  H HB3  . LYS   A 1 46  ? 23.637 10.035  4.277   1 50.935  ? 58  LYS   B HB3  1 c 1 
ATOM   681  H HG2  . LYS   A 1 46  ? 25.589 10.37   5.165   1 58.978  ? 58  LYS   B HG2  1 c 1 
ATOM   682  H HG3  . LYS   A 1 46  ? 25.985 8.852   5.116   1 57.139  ? 58  LYS   B HG3  1 c 1 
ATOM   683  H HD2  . LYS   A 1 46  ? 27.504 10.029  3.862   1 65      ? 58  LYS   B HD2  1 c 1 
ATOM   684  H HD3  . LYS   A 1 46  ? 26.692 9.085   2.886   1 61.575  ? 58  LYS   B HD3  1 c 1 
ATOM   685  H HE2  . LYS   A 1 46  ? 25.663 10.748  1.928   1 62.892  ? 58  LYS   B HE2  1 c 1 
ATOM   686  H HE3  . LYS   A 1 46  ? 25.849 11.723  3.152   1 64.608  ? 58  LYS   B HE3  1 c 1 
ATOM   687  H HZ1  . LYS   A 1 46  ? 27.885 10.961  1.477   1 69.355  ? 58  LYS   B HZ1  1 c 1 
ATOM   688  H HZ2  . LYS   A 1 46  ? 28.033 11.936  2.577   1 71.122  ? 58  LYS   B HZ2  1 c 1 
ATOM   689  H HZ3  . LYS   A 1 46  ? 27.211 12.272  1.398   1 70.224  ? 58  LYS   B HZ3  1 c 1 
ATOM   690  N N    . GLY   A 1 47  ? 21.401 8.486   6.099   1 39.867  ? 59  GLY   B N    1 ? 1 
ATOM   691  C CA   . GLY   A 1 47  ? 19.96  8.352   6.189   1 38.879  ? 59  GLY   B CA   1 ? 1 
ATOM   692  C C    . GLY   A 1 47  ? 19.316 9.71    6.433   1 39.744  ? 59  GLY   B C    1 ? 1 
ATOM   693  O O    . GLY   A 1 47  ? 19.958 10.591  7.006   1 43.797  ? 59  GLY   B O    1 ? 1 
ATOM   694  H H    . GLY   A 1 47  ? 21.842 8.898   6.785   1 41.456  ? 59  GLY   B H    1 c 1 
ATOM   695  H HA2  . GLY   A 1 47  ? 19.613 7.964   5.355   1 37.548  ? 59  GLY   B HA2  1 c 1 
ATOM   696  H HA3  . GLY   A 1 47  ? 19.736 7.74    6.929   1 37.633  ? 59  GLY   B HA3  1 c 1 
ATOM   697  N N    . LYS   A 1 48  ? 18.049 9.849   6.016   1 37.469  ? 60  LYS   B N    1 ? 1 
ATOM   698  C CA   . LYS   A 1 48  ? 17.25  11.018  6.372   1 40.821  ? 60  LYS   B CA   1 ? 1 
ATOM   699  C C    . LYS   A 1 48  ? 15.765 10.675  6.293   1 39.849  ? 60  LYS   B C    1 ? 1 
ATOM   700  O O    . LYS   A 1 48  ? 15.373 9.731   5.63    1 38.906  ? 60  LYS   B O    1 ? 1 
ATOM   701  C CB   . LYS   A 1 48  ? 17.537 12.263  5.526   1 42.244  ? 60  LYS   B CB   1 ? 1 
ATOM   702  C CG   . LYS   A 1 48  ? 17.168 12.143  4.081   1 44.373  ? 60  LYS   B CG   1 ? 1 
ATOM   703  C CD   . LYS   A 1 48  ? 17.692 13.215  3.137   1 49.946  ? 60  LYS   B CD   1 ? 1 
ATOM   704  C CE   . LYS   A 1 48  ? 16.697 14.317  3.039   1 53.601  ? 60  LYS   B CE   1 ? 1 
ATOM   705  N NZ   . LYS   A 1 48  ? 17.142 15.429  2.208   1 56.974  ? 60  LYS   B NZ   1 ? 1 
ATOM   706  H H    . LYS   A 1 48  ? 17.673 9.199   5.495   1 36.928  ? 60  LYS   B H    1 c 1 
ATOM   707  H HA   . LYS   A 1 48  ? 17.458 11.246  7.313   1 41.179  ? 60  LYS   B HA   1 c 1 
ATOM   708  H HB2  . LYS   A 1 48  ? 17.047 13.021  5.909   1 43.975  ? 60  LYS   B HB2  1 c 1 
ATOM   709  H HB3  . LYS   A 1 48  ? 18.495 12.468  5.584   1 44.346  ? 60  LYS   B HB3  1 c 1 
ATOM   710  H HG2  . LYS   A 1 48  ? 17.484 11.27   3.762   1 43.233  ? 60  LYS   B HG2  1 c 1 
ATOM   711  H HG3  . LYS   A 1 48  ? 16.188 12.13   4.02    1 43.707  ? 60  LYS   B HG3  1 c 1 
ATOM   712  H HD2  . LYS   A 1 48  ? 18.542 13.571  3.477   1 51.178  ? 60  LYS   B HD2  1 c 1 
ATOM   713  H HD3  . LYS   A 1 48  ? 17.842 12.828  2.246   1 49.663  ? 60  LYS   B HD3  1 c 1 
ATOM   714  H HE2  . LYS   A 1 48  ? 15.869 13.964  2.665   1 51.982  ? 60  LYS   B HE2  1 c 1 
ATOM   715  H HE3  . LYS   A 1 48  ? 16.501 14.651  3.932   1 53.259  ? 60  LYS   B HE3  1 c 1 
ATOM   716  H HZ1  . LYS   A 1 48  ? 17.371 15.125  1.386   1 57.036  ? 60  LYS   B HZ1  1 c 1 
ATOM   717  H HZ2  . LYS   A 1 48  ? 17.861 15.827  2.589   1 58.271  ? 60  LYS   B HZ2  1 c 1 
ATOM   718  H HZ3  . LYS   A 1 48  ? 16.475 16.036  2.126   1 57.755  ? 60  LYS   B HZ3  1 c 1 
ATOM   719  N N    . LEU   A 1 49  ? 14.968 11.45   7.031   1 43.062  ? 61  LEU   B N    1 ? 1 
ATOM   720  C CA   . LEU   A 1 49  ? 13.527 11.406  6.969   1 41.091  ? 61  LEU   B CA   1 ? 1 
ATOM   721  C C    . LEU   A 1 49  ? 13.131 12.21   5.75    1 46.729  ? 61  LEU   B C    1 ? 1 
ATOM   722  O O    . LEU   A 1 49  ? 13.827 13.159  5.4     1 47.253  ? 61  LEU   B O    1 ? 1 
ATOM   723  C CB   . LEU   A 1 49  ? 12.908 12.023  8.22    1 41.408  ? 61  LEU   B CB   1 ? 1 
ATOM   724  C CG   . LEU   A 1 49  ? 13.429 11.564  9.583   1 39.876  ? 61  LEU   B CG   1 ? 1 
ATOM   725  C CD1  . LEU   A 1 49  ? 12.556 12.16   10.671  1 43.125  ? 61  LEU   B CD1  1 ? 1 
ATOM   726  C CD2  . LEU   A 1 49  ? 13.511 10.072  9.715   1 37.804  ? 61  LEU   B CD2  1 ? 1 
ATOM   727  H H    . LEU   A 1 49  ? 15.356 12.051  7.601   1 43.451  ? 61  LEU   B H    1 c 1 
ATOM   728  H HA   . LEU   A 1 49  ? 13.229 10.466  6.869   1 40.522  ? 61  LEU   B HA   1 c 1 
ATOM   729  H HB2  . LEU   A 1 49  ? 13.025 12.999  8.163   1 42.886  ? 61  LEU   B HB2  1 c 1 
ATOM   730  H HB3  . LEU   A 1 49  ? 11.938 11.855  8.191   1 40.967  ? 61  LEU   B HB3  1 c 1 
ATOM   731  H HG   . LEU   A 1 49  ? 14.344 11.929  9.698   1 41.397  ? 61  LEU   B HG   1 c 1 
ATOM   732  H HD11 . LEU   A 1 49  ? 12.574 13.129  10.609  1 44.253  ? 61  LEU   B HD11 1 c 1 
ATOM   733  H HD12 . LEU   A 1 49  ? 12.89  11.886  11.542  1 43.145  ? 61  LEU   B HD12 1 c 1 
ATOM   734  H HD13 . LEU   A 1 49  ? 11.642 11.846  10.563  1 42.102  ? 61  LEU   B HD13 1 c 1 
ATOM   735  H HD21 . LEU   A 1 49  ? 14.164 9.724   9.085   1 37.031  ? 61  LEU   B HD21 1 c 1 
ATOM   736  H HD22 . LEU   A 1 49  ? 12.642 9.68    9.529   1 37.083  ? 61  LEU   B HD22 1 c 1 
ATOM   737  H HD23 . LEU   A 1 49  ? 13.783 9.841   10.619  1 38.315  ? 61  LEU   B HD23 1 c 1 
ATOM   738  N N    . SER   A 1 50  ? 11.982 11.87   5.157   1 52.005  ? 62  SER   B N    1 ? 1 
ATOM   739  C CA   . SER   A 1 50  ? 11.411 12.677  4.074   1 56.018  ? 62  SER   B CA   1 ? 1 
ATOM   740  C C    . SER   A 1 50  ? 11.015 14.071  4.553   1 50.463  ? 62  SER   B C    1 ? 1 
ATOM   741  O O    . SER   A 1 50  ? 10.857 14.979  3.753   1 52.874  ? 62  SER   B O    1 ? 1 
ATOM   742  C CB   . SER   A 1 50  ? 10.225 11.968  3.418   1 58.112  ? 62  SER   B CB   1 ? 1 
ATOM   743  O OG   . SER   A 1 50  ? 9.394  11.339  4.391   1 62.723  ? 62  SER   B OG   1 ? 1 
ATOM   744  H H    . SER   A 1 50  ? 11.539 11.118  5.429   1 49.822  ? 62  SER   B H    1 c 1 
ATOM   745  H HA   . SER   A 1 50  ? 12.114 12.789  3.385   1 54.721  ? 62  SER   B HA   1 c 1 
ATOM   746  H HB2  . SER   A 1 50  ? 9.698  12.618  2.914   1 60.254  ? 62  SER   B HB2  1 c 1 
ATOM   747  H HB3  . SER   A 1 50  ? 10.554 11.297  2.794   1 57.993  ? 62  SER   B HB3  1 c 1 
ATOM   748  H HG   . SER   A 1 50  ? 8.693  10.962  3.998   0 30      ? 62  SER   B HG   1 c 1 
ATOM   749  N N    . ASN   A 1 51  ? 10.87  14.27   5.869   1 53.039  ? 63  ASN   B N    1 ? 1 
ATOM   750  C CA   . ASN   A 1 51  ? 10.408 15.552  6.368   1 53.95   ? 63  ASN   B CA   1 ? 1 
ATOM   751  C C    . ASN   A 1 51  ? 11.581 16.539  6.436   1 54.618  ? 63  ASN   B C    1 ? 1 
ATOM   752  O O    . ASN   A 1 51  ? 11.369 17.698  6.758   1 57.272  ? 63  ASN   B O    1 ? 1 
ATOM   753  C CB   . ASN   A 1 51  ? 9.608  15.354  7.649   1 52.852  ? 63  ASN   B CB   1 ? 1 
ATOM   754  C CG   . ASN   A 1 51  ? 10.472 15.099  8.866   1 51.01   ? 63  ASN   B CG   1 ? 1 
ATOM   755  O OD1  . ASN   A 1 51  ? 11.706 15.093  8.771   1 45.35   ? 63  ASN   B OD1  1 ? 1 
ATOM   756  N ND2  . ASN   A 1 51  ? 9.845  14.905  10.023  1 49.079  ? 63  ASN   B ND2  1 ? 1 
ATOM   757  H H    . ASN   A 1 51  ? 11.043 13.598  6.463   1 50.876  ? 63  ASN   B H    1 c 1 
ATOM   758  H HA   . ASN   A 1 51  ? 9.776  15.911  5.704   1 54.737  ? 63  ASN   B HA   1 c 1 
ATOM   759  H HB2  . ASN   A 1 51  ? 9.064  16.152  7.809   1 54.656  ? 63  ASN   B HB2  1 c 1 
ATOM   760  H HB3  . ASN   A 1 51  ? 8.999  14.598  7.528   1 51.592  ? 63  ASN   B HB3  1 c 1 
ATOM   761  H HD21 . ASN   A 1 51  ? 10.313 14.727  10.755  1 49.937  ? 63  ASN   B HD21 1 c 1 
ATOM   762  H HD22 . ASN   A 1 51  ? 8.96   14.953  10.062  1 50.364  ? 63  ASN   B HD22 1 c 1 
ATOM   763  N N    . GLY   A 1 52  ? 12.813 16.064  6.16    1 56.739  ? 64  GLY   B N    1 ? 1 
ATOM   764  C CA   . GLY   A 1 52  ? 13.997 16.913  6.046   1 59.125  ? 64  GLY   B CA   1 ? 1 
ATOM   765  C C    . GLY   A 1 52  ? 14.528 17.418  7.394   1 61.035  ? 64  GLY   B C    1 ? 1 
ATOM   766  O O    . GLY   A 1 52  ? 15.383 18.297  7.432   1 61.962  ? 64  GLY   B O    1 ? 1 
ATOM   767  H H    . GLY   A 1 52  ? 12.924 15.163  6.059   1 54.132  ? 64  GLY   B H    1 c 1 
ATOM   768  H HA2  . GLY   A 1 52  ? 14.707 16.403  5.59    1 58.285  ? 64  GLY   B HA2  1 c 1 
ATOM   769  H HA3  . GLY   A 1 52  ? 13.775 17.687  5.476   1 60.841  ? 64  GLY   B HA3  1 c 1 
ATOM   770  N N    . LYS   A 1 53  ? 14.037 16.857  8.511   1 59.388  ? 65  LYS   B N    1 ? 1 
ATOM   771  C CA   . LYS   A 1 53  ? 14.271 17.438  9.825   1 62.442  ? 65  LYS   B CA   1 ? 1 
ATOM   772  C C    . LYS   A 1 53  ? 15.219 16.568  10.653  1 60.817  ? 65  LYS   B C    1 ? 1 
ATOM   773  O O    . LYS   A 1 53  ? 15.502 16.929  11.78   1 62.756  ? 65  LYS   B O    1 ? 1 
ATOM   774  C CB   . LYS   A 1 53  ? 12.926 17.717  10.521  1 61.009  ? 65  LYS   B CB   1 ? 1 
ATOM   775  H H    . LYS   A 1 53  ? 13.549 16.086  8.452   1 57.752  ? 65  LYS   B H    1 c 1 
ATOM   776  H HA   . LYS   A 1 53  ? 14.71  18.316  9.695   1 64.011  ? 65  LYS   B HA   1 c 1 
ATOM   777  H HB2  . LYS   A 1 53  ? 13.076 18.347  11.247  0 30      ? 65  LYS   B HB2  1 c 1 
ATOM   778  H HB3  . LYS   A 1 53  ? 12.197 17.491  9.851   0 30      ? 65  LYS   B HB3  1 c 1 
ATOM   779  N N    . LYS   A 1 54  ? 15.703 15.434  10.122  1 62.407  ? 66  LYS   B N    1 ? 1 
ATOM   780  C CA   . LYS   A 1 54  ? 16.688 14.61   10.823  1 63.295  ? 66  LYS   B CA   1 ? 1 
ATOM   781  C C    . LYS   A 1 54  ? 17.544 13.834  9.811   1 61.969  ? 66  LYS   B C    1 ? 1 
ATOM   782  O O    . LYS   A 1 54  ? 17.025 13.212  8.861   1 53.968  ? 66  LYS   B O    1 ? 1 
ATOM   783  C CB   . LYS   A 1 54  ? 16.085 13.642  11.859  1 60.308  ? 66  LYS   B CB   1 ? 1 
ATOM   784  H H    . LYS   A 1 54  ? 15.411 15.161  9.301   1 60.128  ? 66  LYS   B H    1 c 1 
ATOM   785  H HA   . LYS   A 1 54  ? 17.288 15.222  11.319  1 65.074  ? 66  LYS   B HA   1 c 1 
ATOM   786  H HB2  . LYS   A 1 54  ? 16.784 13.188  12.352  0 30      ? 66  LYS   B HB2  1 c 1 
ATOM   787  H HB3  . LYS   A 1 54  ? 15.072 13.676  11.818  0 30      ? 66  LYS   B HB3  1 c 1 
ATOM   788  N N    . PHE   A 1 55  ? 18.87  13.903  10.035  1 56.252  ? 67  PHE   B N    1 ? 1 
ATOM   789  C CA   . PHE   A 1 55  ? 19.858 13.2    9.238   1 57.772  ? 67  PHE   B CA   1 ? 1 
ATOM   790  C C    . PHE   A 1 55  ? 20.778 12.371  10.132  1 60.941  ? 67  PHE   B C    1 ? 1 
ATOM   791  O O    . PHE   A 1 55  ? 20.888 12.597  11.338  1 66.256  ? 67  PHE   B O    1 ? 1 
ATOM   792  C CB   . PHE   A 1 55  ? 20.723 14.188  8.466   1 61.214  ? 67  PHE   B CB   1 ? 1 
ATOM   793  C CG   . PHE   A 1 55  ? 19.933 15.225  7.692   1 67.426  ? 67  PHE   B CG   1 ? 1 
ATOM   794  C CD1  . PHE   A 1 55  ? 19.349 16.304  8.355   1 75.792  ? 67  PHE   B CD1  1 ? 1 
ATOM   795  C CD2  . PHE   A 1 55  ? 19.842 15.166  6.306   1 67.402  ? 67  PHE   B CD2  1 ? 1 
ATOM   796  C CE1  . PHE   A 1 55  ? 18.669 17.286  7.647   1 81.031  ? 67  PHE   B CE1  1 ? 1 
ATOM   797  C CE2  . PHE   A 1 55  ? 19.157 16.149  5.6     1 73.984  ? 67  PHE   B CE2  1 ? 1 
ATOM   798  C CZ   . PHE   A 1 55  ? 18.555 17.195  6.268   1 79.858  ? 67  PHE   B CZ   1 ? 1 
ATOM   799  H H    . PHE   A 1 55  ? 19.167 14.419  10.728  1 60.63   ? 67  PHE   B H    1 c 1 
ATOM   800  H HA   . PHE   A 1 55  ? 19.397 12.599  8.597   1 55.649  ? 67  PHE   B HA   1 c 1 
ATOM   801  H HB2  . PHE   A 1 55  ? 21.315 14.649  9.101   1 64.689  ? 67  PHE   B HB2  1 c 1 
ATOM   802  H HB3  . PHE   A 1 55  ? 21.288 13.685  7.838   1 61.828  ? 67  PHE   B HB3  1 c 1 
ATOM   803  H HD1  . PHE   A 1 55  ? 19.42  16.369  9.294   1 75.851  ? 67  PHE   B HD1  1 c 1 
ATOM   804  H HD2  . PHE   A 1 55  ? 20.246 14.45   5.841   1 67.405  ? 67  PHE   B HD2  1 c 1 
ATOM   805  H HE1  . PHE   A 1 55  ? 18.257 18      8.109   1 81.267  ? 67  PHE   B HE1  1 c 1 
ATOM   806  H HE2  . PHE   A 1 55  ? 19.082 16.085  4.661   1 73.314  ? 67  PHE   B HE2  1 c 1 
ATOM   807  H HZ   . PHE   A 1 55  ? 18.087 17.859  5.786   1 79.829  ? 67  PHE   B HZ   1 c 1 
ATOM   808  N N    . ASP   A 1 56  ? 21.465 11.407  9.526   1 57.661  ? 68  ASP   B N    1 ? 1 
ATOM   809  C CA   . ASP   A 1 56  ? 22.267 10.464  10.286  1 61.747  ? 68  ASP   B CA   1 ? 1 
ATOM   810  C C    . ASP   A 1 56  ? 23.188 9.744   9.316   1 63.722  ? 68  ASP   B C    1 ? 1 
ATOM   811  O O    . ASP   A 1 56  ? 22.727 9.26    8.291   1 62.949  ? 68  ASP   B O    1 ? 1 
ATOM   812  C CB   . ASP   A 1 56  ? 21.377 9.467   11.015  1 59.605  ? 68  ASP   B CB   1 ? 1 
ATOM   813  C CG   . ASP   A 1 56  ? 22.059 8.206   11.526  1 60.901  ? 68  ASP   B CG   1 ? 1 
ATOM   814  O OD1  . ASP   A 1 56  ? 23.027 8.324   12.312  1 61.551  ? 68  ASP   B OD1  1 ? 1 
ATOM   815  O OD2  . ASP   A 1 56  ? 21.599 7.104   11.148  1 54.844  ? 68  ASP   B OD2  1 ? 1 
ATOM   816  H H    . ASP   A 1 56  ? 21.433 11.332  8.616   1 58.097  ? 68  ASP   B H    1 c 1 
ATOM   817  H HA   . ASP   A 1 56  ? 22.807 10.962  10.94   1 64.004  ? 68  ASP   B HA   1 c 1 
ATOM   818  H HB2  . ASP   A 1 56  ? 20.961 9.919   11.779  1 60.796  ? 68  ASP   B HB2  1 c 1 
ATOM   819  H HB3  . ASP   A 1 56  ? 20.664 9.198   10.399  1 57.512  ? 68  ASP   B HB3  1 c 1 
ATOM   820  N N    . SER   A 1 57  ? 24.472 9.66    9.668   1 63.913  ? 69  SER   B N    1 ? 1 
ATOM   821  C CA   . SER   A 1 57  ? 25.458 8.961   8.868   1 65.073  ? 69  SER   B CA   1 ? 1 
ATOM   822  C C    . SER   A 1 57  ? 26.354 8.157   9.797   1 69.358  ? 69  SER   B C    1 ? 1 
ATOM   823  O O    . SER   A 1 57  ? 26.748 8.681   10.843  1 75.55   ? 69  SER   B O    1 ? 1 
ATOM   824  C CB   . SER   A 1 57  ? 26.288 9.932   8.053   1 73.679  ? 69  SER   B CB   1 ? 1 
ATOM   825  O OG   . SER   A 1 57  ? 27.286 9.251   7.301   1 74      ? 69  SER   B OG   1 ? 1 
ATOM   826  H H    . SER   A 1 57  ? 24.745 10.057  10.444  1 66.709  ? 69  SER   B H    1 c 1 
ATOM   827  H HA   . SER   A 1 57  ? 24.992 8.34    8.254   1 63.821  ? 69  SER   B HA   1 c 1 
ATOM   828  H HB2  . SER   A 1 57  ? 25.704 10.425  7.448   1 71.233  ? 69  SER   B HB2  1 c 1 
ATOM   829  H HB3  . SER   A 1 57  ? 26.714 10.572  8.653   1 74.811  ? 69  SER   B HB3  1 c 1 
ATOM   830  H HG   . SER   A 1 57  ? 27.683 9.948   6.879   0 30      ? 69  SER   B HG   1 c 1 
ATOM   831  N N    . SER   A 1 58  ? 26.683 6.918   9.379   1 65.239  ? 70  SER   B N    1 ? 1 
ATOM   832  C CA   . SER   A 1 58  ? 27.689 6.08    10.018  1 65.39   ? 70  SER   B CA   1 ? 1 
ATOM   833  C C    . SER   A 1 58  ? 29.021 6.815   10.179  1 75.209  ? 70  SER   B C    1 ? 1 
ATOM   834  O O    . SER   A 1 58  ? 29.715 6.609   11.173  1 80.775  ? 70  SER   B O    1 ? 1 
ATOM   835  C CB   . SER   A 1 58  ? 27.907 4.794   9.258   1 60.009  ? 70  SER   B CB   1 ? 1 
ATOM   836  O OG   . SER   A 1 58  ? 28.329 5.049   7.926   1 61.764  ? 70  SER   B OG   1 ? 1 
ATOM   837  H H    . SER   A 1 58  ? 26.245 6.579   8.651   1 63.311  ? 70  SER   B H    1 c 1 
ATOM   838  H HA   . SER   A 1 58  ? 27.359 5.85    10.923  1 65.709  ? 70  SER   B HA   1 c 1 
ATOM   839  H HB2  . SER   A 1 58  ? 28.584 4.26    9.716   1 62.789  ? 70  SER   B HB2  1 c 1 
ATOM   840  H HB3  . SER   A 1 58  ? 27.077 4.284   9.243   1 58.332  ? 70  SER   B HB3  1 c 1 
ATOM   841  H HG   . SER   A 1 58  ? 28.426 4.314   7.493   0 30      ? 70  SER   B HG   1 c 1 
ATOM   842  N N    . HIS   A 1 59  ? 29.388 7.649   9.195   1 78.771  ? 71  HIS   B N    1 ? 1 
ATOM   843  C CA   . HIS   A 1 59  ? 30.646 8.376   9.25    1 88.921  ? 71  HIS   B CA   1 ? 1 
ATOM   844  C C    . HIS   A 1 59  ? 30.708 9.25    10.511  1 95.858  ? 71  HIS   B C    1 ? 1 
ATOM   845  O O    . HIS   A 1 59  ? 31.76  9.343   11.138  1 95.209  ? 71  HIS   B O    1 ? 1 
ATOM   846  C CB   . HIS   A 1 59  ? 30.874 9.132   7.936   1 90.992  ? 71  HIS   B CB   1 ? 1 
ATOM   847  C CG   . HIS   A 1 59  ? 30.909 8.254   6.725   1 87.905  ? 71  HIS   B CG   1 ? 1 
ATOM   848  N ND1  . HIS   A 1 59  ? 29.9   8.214   5.786   1 90.209  ? 71  HIS   B ND1  1 ? 1 
ATOM   849  C CD2  . HIS   A 1 59  ? 31.85  7.412   6.284   1 91.004  ? 71  HIS   B CD2  1 ? 1 
ATOM   850  C CE1  . HIS   A 1 59  ? 30.225 7.367   4.814   1 89.234  ? 71  HIS   B CE1  1 ? 1 
ATOM   851  N NE2  . HIS   A 1 59  ? 31.411 6.866   5.098   1 88.67   ? 71  HIS   B NE2  1 ? 1 
ATOM   852  H H    . HIS   A 1 59  ? 28.842 7.762   8.471   1 77.25   ? 71  HIS   B H    1 c 1 
ATOM   853  H HA   . HIS   A 1 59  ? 31.361 7.696   9.322   1 90.02   ? 71  HIS   B HA   1 c 1 
ATOM   854  H HB2  . HIS   A 1 59  ? 30.158 9.795   7.827   1 89.324  ? 71  HIS   B HB2  1 c 1 
ATOM   855  H HB3  . HIS   A 1 59  ? 31.724 9.62    7.998   1 94.304  ? 71  HIS   B HB3  1 c 1 
ATOM   856  H HD1  . HIS   A 1 59  ? 29.1   8.668   5.763   0 30      ? 71  HIS   B HD1  1 c 1 
ATOM   857  H HD2  . HIS   A 1 59  ? 32.668 7.221   6.701   1 93.447  ? 71  HIS   B HD2  1 c 1 
ATOM   858  H HE1  . HIS   A 1 59  ? 29.698 7.156   4.062   1 86.555  ? 71  HIS   B HE1  1 c 1 
ATOM   859  H HE2  . HIS   A 1 59  ? 31.753 6.23    4.544   0 30      ? 71  HIS   B HE2  1 c 1 
ATOM   860  N N    . ASP   A 1 60  ? 29.569 9.833   10.921  1 99.794  ? 72  ASP   B N    1 ? 1 
ATOM   861  C CA   . ASP   A 1 60  ? 29.492 10.645  12.131  1 107.757 ? 72  ASP   B CA   1 ? 1 
ATOM   862  C C    . ASP   A 1 60  ? 30.023 9.873   13.34   1 109.699 ? 72  ASP   B C    1 ? 1 
ATOM   863  O O    . ASP   A 1 60  ? 30.684 10.446  14.199  1 118.932 ? 72  ASP   B O    1 ? 1 
ATOM   864  C CB   . ASP   A 1 60  ? 28.076 11.068  12.508  1 109.364 ? 72  ASP   B CB   1 ? 1 
ATOM   865  C CG   . ASP   A 1 60  ? 27.212 11.726  11.437  1 106.645 ? 72  ASP   B CG   1 ? 1 
ATOM   866  O OD1  . ASP   A 1 60  ? 27.753 12.584  10.683  1 101.023 ? 72  ASP   B OD1  1 ? 1 
ATOM   867  O OD2  . ASP   A 1 60  ? 25.987 11.409  11.412  1 94.721  ? 72  ASP   B OD2  1 ? 1 
ATOM   868  H H    . ASP   A 1 60  ? 28.811 9.723   10.421  1 96.119  ? 72  ASP   B H    1 c 1 
ATOM   869  H HA   . ASP   A 1 60  ? 30.04  11.452  12.002  1 110.67  ? 72  ASP   B HA   1 c 1 
ATOM   870  H HB2  . ASP   A 1 60  ? 27.594 10.278  12.83   1 105.697 ? 72  ASP   B HB2  1 c 1 
ATOM   871  H HB3  . ASP   A 1 60  ? 28.14  11.697  13.257  1 110.825 ? 72  ASP   B HB3  1 c 1 
ATOM   872  N N    . ARG   A 1 61  ? 29.691 8.58    13.426  1 104.978 ? 73  ARG   B N    1 ? 1 
ATOM   873  C CA   . ARG   A 1 61  ? 30.15  7.725   14.513  1 100.999 ? 73  ARG   B CA   1 ? 1 
ATOM   874  C C    . ARG   A 1 61  ? 31.585 7.258   14.249  1 99.497  ? 73  ARG   B C    1 ? 1 
ATOM   875  O O    . ARG   A 1 61  ? 32.215 6.689   15.137  1 103.478 ? 73  ARG   B O    1 ? 1 
ATOM   876  C CB   . ARG   A 1 61  ? 29.179 6.55    14.703  1 88.941  ? 73  ARG   B CB   1 ? 1 
ATOM   877  H H    . ARG   A 1 61  ? 29.155 8.216   12.781  1 100.508 ? 73  ARG   B H    1 c 1 
ATOM   878  H HA   . ARG   A 1 61  ? 30.147 8.26    15.348  1 102.258 ? 73  ARG   B HA   1 c 1 
ATOM   879  H HB2  . ARG   A 1 61  ? 29.587 5.818   15.005  0 30      ? 73  ARG   B HB2  1 c 1 
ATOM   880  H HB3  . ARG   A 1 61  ? 28.212 7.034   14.709  0 30      ? 73  ARG   B HB3  1 c 1 
ATOM   881  N N    . ASN   A 1 62  ? 32.087 7.49    13.026  1 94.582  ? 74  ASN   B N    1 ? 1 
ATOM   882  C CA   . ASN   A 1 62  ? 33.464 7.195   12.661  1 95.897  ? 74  ASN   B CA   1 ? 1 
ATOM   883  C C    . ASN   A 1 62  ? 33.705 5.688   12.735  1 93.427  ? 74  ASN   B C    1 ? 1 
ATOM   884  O O    . ASN   A 1 62  ? 34.741 5.247   13.23   1 97.316  ? 74  ASN   B O    1 ? 1 
ATOM   885  C CB   . ASN   A 1 62  ? 34.459 8.013   13.492  1 103.833 ? 74  ASN   B CB   1 ? 1 
ATOM   886  H H    . ASN   A 1 62  ? 31.536 7.824   12.38   1 92.971  ? 74  ASN   B H    1 c 1 
ATOM   887  H HA   . ASN   A 1 62  ? 33.585 7.467   11.724  1 95.922  ? 74  ASN   B HA   1 c 1 
ATOM   888  H HB2  . ASN   A 1 62  ? 35.366 7.748   13.179  0 30      ? 74  ASN   B HB2  1 c 1 
ATOM   889  H HB3  . ASN   A 1 62  ? 33.984 8.62    14.041  0 30      ? 74  ASN   B HB3  1 c 1 
ATOM   890  N N    . GLU   A 1 63  ? 32.752 4.891   12.224  1 89.497  ? 75  GLU   B N    1 ? 1 
ATOM   891  C CA   . GLU   A 1 63  ? 32.982 3.462   12.041  1 86.996  ? 75  GLU   B CA   1 ? 1 
ATOM   892  C C    . GLU   A 1 63  ? 31.886 2.84    11.188  1 75.057  ? 75  GLU   B C    1 ? 1 
ATOM   893  O O    . GLU   A 1 63  ? 30.768 3.348   11.118  1 68.052  ? 75  GLU   B O    1 ? 1 
ATOM   894  C CB   . GLU   A 1 63  ? 33.082 2.662   13.345  1 92.381  ? 75  GLU   B CB   1 ? 1 
ATOM   895  C CG   . GLU   A 1 63  ? 31.817 2.676   14.199  1 90.678  ? 75  GLU   B CG   1 ? 1 
ATOM   896  C CD   . GLU   A 1 63  ? 32.052 2.443   15.687  1 98.728  ? 75  GLU   B CD   1 ? 1 
ATOM   897  O OE1  . GLU   A 1 63  ? 31.042 2.423   16.425  1 99.868  ? 75  GLU   B OE1  1 ? 1 
ATOM   898  O OE2  . GLU   A 1 63  ? 33.22  2.302   16.121  1 98.126  ? 75  GLU   B OE2  1 ? 1 
ATOM   899  H H    . GLU   A 1 63  ? 31.944 5.245   11.983  1 86.103  ? 75  GLU   B H    1 c 1 
ATOM   900  H HA   . GLU   A 1 63  ? 33.842 3.36    11.563  1 88.879  ? 75  GLU   B HA   1 c 1 
ATOM   901  H HB2  . GLU   A 1 63  ? 33.292 1.731   13.126  1 91.04   ? 75  GLU   B HB2  1 c 1 
ATOM   902  H HB3  . GLU   A 1 63  ? 33.827 3.016   13.872  1 95.708  ? 75  GLU   B HB3  1 c 1 
ATOM   903  H HG2  . GLU   A 1 63  ? 31.368 3.542   14.09   1 90.548  ? 75  GLU   B HG2  1 c 1 
ATOM   904  H HG3  . GLU   A 1 63  ? 31.204 1.984   13.871  1 88.065  ? 75  GLU   B HG3  1 c 1 
ATOM   905  N N    . PRO   A 1 64  ? 32.174 1.697   10.525  1 73.086  ? 76  PRO   B N    1 ? 1 
ATOM   906  C CA   . PRO   A 1 64  ? 31.144 0.924   9.843   1 67.688  ? 76  PRO   B CA   1 ? 1 
ATOM   907  C C    . PRO   A 1 64  ? 29.987 0.57    10.763  1 63.101  ? 76  PRO   B C    1 ? 1 
ATOM   908  O O    . PRO   A 1 64  ? 30.202 0.334   11.949  1 64.903  ? 76  PRO   B O    1 ? 1 
ATOM   909  C CB   . PRO   A 1 64  ? 31.866 -0.347  9.398   1 68.256  ? 76  PRO   B CB   1 ? 1 
ATOM   910  C CG   . PRO   A 1 64  ? 33.295 0.12    9.26    1 73.57   ? 76  PRO   B CG   1 ? 1 
ATOM   911  C CD   . PRO   A 1 64  ? 33.504 1.091   10.381  1 76.18   ? 76  PRO   B CD   1 ? 1 
ATOM   912  H HA   . PRO   A 1 64  ? 30.816 1.42    9.064   1 66.008  ? 76  PRO   B HA   1 c 1 
ATOM   913  H HB2  . PRO   A 1 64  ? 31.789 -1.051  10.07   1 68.499  ? 76  PRO   B HB2  1 c 1 
ATOM   914  H HB3  . PRO   A 1 64  ? 31.516 -0.67   8.545   1 66.442  ? 76  PRO   B HB3  1 c 1 
ATOM   915  H HG2  . PRO   A 1 64  ? 33.915 -0.632  9.336   1 75.271  ? 76  PRO   B HG2  1 c 1 
ATOM   916  H HG3  . PRO   A 1 64  ? 33.435 0.557   8.396   1 73.551  ? 76  PRO   B HG3  1 c 1 
ATOM   917  H HD2  . PRO   A 1 64  ? 33.773 0.637   11.202  1 78.073  ? 76  PRO   B HD2  1 c 1 
ATOM   918  H HD3  . PRO   A 1 64  ? 34.172 1.764   10.146  1 79.209  ? 76  PRO   B HD3  1 c 1 
ATOM   919  N N    . PHE   A 1 65  ? 28.773 0.58    10.21   1 59.88   ? 77  PHE   B N    1 ? 1 
ATOM   920  C CA   . PHE   A 1 65  ? 27.635 -0.069  10.842  1 58.213  ? 77  PHE   B CA   1 ? 1 
ATOM   921  C C    . PHE   A 1 65  ? 27.665 -1.56   10.5    1 56.923  ? 77  PHE   B C    1 ? 1 
ATOM   922  O O    . PHE   A 1 65  ? 27.824 -1.927  9.336   1 55.489  ? 77  PHE   B O    1 ? 1 
ATOM   923  C CB   . PHE   A 1 65  ? 26.363 0.645   10.394  1 54.511  ? 77  PHE   B CB   1 ? 1 
ATOM   924  C CG   . PHE   A 1 65  ? 25.112 0.185   11.121  1 54.446  ? 77  PHE   B CG   1 ? 1 
ATOM   925  C CD1  . PHE   A 1 65  ? 24.753 0.729   12.351  1 53.097  ? 77  PHE   B CD1  1 ? 1 
ATOM   926  C CD2  . PHE   A 1 65  ? 24.27  -0.768  10.548  1 52.774  ? 77  PHE   B CD2  1 ? 1 
ATOM   927  C CE1  . PHE   A 1 65  ? 23.59  0.31    12.996  1 50.644  ? 77  PHE   B CE1  1 ? 1 
ATOM   928  C CE2  . PHE   A 1 65  ? 23.131 -1.2    11.209  1 48.138  ? 77  PHE   B CE2  1 ? 1 
ATOM   929  C CZ   . PHE   A 1 65  ? 22.79  -0.658  12.424  1 49.209  ? 77  PHE   B CZ   1 ? 1 
ATOM   930  H H    . PHE   A 1 65  ? 28.648 1.006   9.411   1 59.065  ? 77  PHE   B H    1 c 1 
ATOM   931  H HA   . PHE   A 1 65  ? 27.72  0.033   11.827  1 59.336  ? 77  PHE   B HA   1 c 1 
ATOM   932  H HB2  . PHE   A 1 65  ? 26.479 1.61    10.539  1 56.085  ? 77  PHE   B HB2  1 c 1 
ATOM   933  H HB3  . PHE   A 1 65  ? 26.243 0.496   9.43    1 53.838  ? 77  PHE   B HB3  1 c 1 
ATOM   934  H HD1  . PHE   A 1 65  ? 25.3   1.388   12.748  1 55.463  ? 77  PHE   B HD1  1 c 1 
ATOM   935  H HD2  . PHE   A 1 65  ? 24.502 -1.152  9.718   1 51.206  ? 77  PHE   B HD2  1 c 1 
ATOM   936  H HE1  . PHE   A 1 65  ? 23.361 0.675   13.836  1 52.261  ? 77  PHE   B HE1  1 c 1 
ATOM   937  H HE2  . PHE   A 1 65  ? 22.576 -1.852  10.811  1 47.445  ? 77  PHE   B HE2  1 c 1 
ATOM   938  H HZ   . PHE   A 1 65  ? 22.005 -0.942  12.865  1 48.402  ? 77  PHE   B HZ   1 c 1 
ATOM   939  N N    . VAL   A 1 66  ? 27.528 -2.405  11.534  1 58.777  ? 78  VAL   B N    1 ? 1 
ATOM   940  C CA   . VAL   A 1 66  ? 27.699 -3.845  11.407  1 57.44   ? 78  VAL   B CA   1 ? 1 
ATOM   941  C C    . VAL   A 1 66  ? 26.445 -4.526  11.943  1 54.223  ? 78  VAL   B C    1 ? 1 
ATOM   942  O O    . VAL   A 1 66  ? 25.914 -4.117  12.981  1 51.108  ? 78  VAL   B O    1 ? 1 
ATOM   943  C CB   . VAL   A 1 66  ? 28.943 -4.328  12.165  1 62.053  ? 78  VAL   B CB   1 ? 1 
ATOM   944  C CG1  . VAL   A 1 66  ? 28.899 -5.822  12.432  1 64.592  ? 78  VAL   B CG1  1 ? 1 
ATOM   945  C CG2  . VAL   A 1 66  ? 30.217 -3.976  11.42   1 65.649  ? 78  VAL   B CG2  1 ? 1 
ATOM   946  H H    . VAL   A 1 66  ? 27.314 -2.065  12.355  1 58.82   ? 78  VAL   B H    1 c 1 
ATOM   947  H HA   . VAL   A 1 66  ? 27.801 -4.067  10.464  1 56.692  ? 78  VAL   B HA   1 c 1 
ATOM   948  H HB   . VAL   A 1 66  ? 28.957 -3.861  13.034  1 63.884  ? 78  VAL   B HB   1 c 1 
ATOM   949  H HG11 . VAL   A 1 66  ? 28.777 -6.3    11.594  1 62.601  ? 78  VAL   B HG11 1 c 1 
ATOM   950  H HG12 . VAL   A 1 66  ? 28.162 -6.027  13.032  1 63.071  ? 78  VAL   B HG12 1 c 1 
ATOM   951  H HG13 . VAL   A 1 66  ? 29.733 -6.098  12.844  1 66.722  ? 78  VAL   B HG13 1 c 1 
ATOM   952  H HG21 . VAL   A 1 66  ? 30.981 -4.366  11.877  1 68.106  ? 78  VAL   B HG21 1 c 1 
ATOM   953  H HG22 . VAL   A 1 66  ? 30.318 -3.01   11.388  1 65.642  ? 78  VAL   B HG22 1 c 1 
ATOM   954  H HG23 . VAL   A 1 66  ? 30.168 -4.326  10.515  1 64.03   ? 78  VAL   B HG23 1 c 1 
ATOM   955  N N    . PHE   A 1 67  ? 25.971 -5.558  11.227  1 50.079  ? 79  PHE   B N    1 ? 1 
ATOM   956  C CA   . PHE   A 1 67  ? 24.746 -6.255  11.616  1 47.294  ? 79  PHE   B CA   1 ? 1 
ATOM   957  C C    . PHE   A 1 67  ? 24.684 -7.631  10.938  1 49.54   ? 79  PHE   B C    1 ? 1 
ATOM   958  O O    . PHE   A 1 67  ? 25.363 -7.914  9.947   1 48.904  ? 79  PHE   B O    1 ? 1 
ATOM   959  C CB   . PHE   A 1 67  ? 23.531 -5.358  11.354  1 42.904  ? 79  PHE   B CB   1 ? 1 
ATOM   960  C CG   . PHE   A 1 67  ? 23.03  -5.295  9.913   1 37.273  ? 79  PHE   B CG   1 ? 1 
ATOM   961  C CD1  . PHE   A 1 67  ? 23.673 -4.525  8.956   1 38.052  ? 79  PHE   B CD1  1 ? 1 
ATOM   962  C CD2  . PHE   A 1 67  ? 21.895 -5.982  9.522   1 33.644  ? 79  PHE   B CD2  1 ? 1 
ATOM   963  C CE1  . PHE   A 1 67  ? 23.244 -4.503  7.629   1 35.538  ? 79  PHE   B CE1  1 ? 1 
ATOM   964  C CE2  . PHE   A 1 67  ? 21.462 -5.944  8.199   1 33.193  ? 79  PHE   B CE2  1 ? 1 
ATOM   965  C CZ   . PHE   A 1 67  ? 22.15  -5.24   7.249   1 31.872  ? 79  PHE   B CZ   1 ? 1 
ATOM   966  H H    . PHE   A 1 67  ? 26.42  -5.835  10.481  1 50.576  ? 79  PHE   B H    1 c 1 
ATOM   967  H HA   . PHE   A 1 67  ? 24.794 -6.41   12.596  1 49.153  ? 79  PHE   B HA   1 c 1 
ATOM   968  H HB2  . PHE   A 1 67  ? 22.794 -5.67   11.925  1 42.145  ? 79  PHE   B HB2  1 c 1 
ATOM   969  H HB3  . PHE   A 1 67  ? 23.751 -4.446  11.645  1 42.949  ? 79  PHE   B HB3  1 c 1 
ATOM   970  H HD1  . PHE   A 1 67  ? 24.458 -4.057  9.195   1 38.975  ? 79  PHE   B HD1  1 c 1 
ATOM   971  H HD2  . PHE   A 1 67  ? 21.435 -6.515  10.151  1 34.688  ? 79  PHE   B HD2  1 c 1 
ATOM   972  H HE1  . PHE   A 1 67  ? 23.713 -3.989  6.991   1 35.566  ? 79  PHE   B HE1  1 c 1 
ATOM   973  H HE2  . PHE   A 1 67  ? 20.699 -6.44   7.947   1 32.004  ? 79  PHE   B HE2  1 c 1 
ATOM   974  H HZ   . PHE   A 1 67  ? 21.823 -5.187  6.365   1 32.043  ? 79  PHE   B HZ   1 c 1 
ATOM   975  N N    . SER   A 1 68  ? 23.885 -8.516  11.527  1 53.416  ? 80  SER   B N    1 ? 1 
ATOM   976  C CA   . SER   A 1 68  ? 23.603 -9.833  10.965  1 51.555  ? 80  SER   B CA   1 ? 1 
ATOM   977  C C    . SER   A 1 68  ? 22.347 -9.73   10.107  1 43.88   ? 80  SER   B C    1 ? 1 
ATOM   978  O O    . SER   A 1 68  ? 21.294 -9.305  10.569  1 41.201  ? 80  SER   B O    1 ? 1 
ATOM   979  C CB   . SER   A 1 68  ? 23.445 -10.877 12.038  1 55.634  ? 80  SER   B CB   1 ? 1 
ATOM   980  O OG   . SER   A 1 68  ? 24.63  -10.951 12.81   1 61.512  ? 80  SER   B OG   1 ? 1 
ATOM   981  H H    . SER   A 1 68  ? 23.492 -8.292  12.322  1 52.23   ? 80  SER   B H    1 c 1 
ATOM   982  H HA   . SER   A 1 68  ? 24.361 -10.094 10.385  1 51.89   ? 80  SER   B HA   1 c 1 
ATOM   983  H HB2  . SER   A 1 68  ? 22.692 -10.644 12.614  1 55.395  ? 80  SER   B HB2  1 c 1 
ATOM   984  H HB3  . SER   A 1 68  ? 23.265 -11.744 11.627  1 56.057  ? 80  SER   B HB3  1 c 1 
ATOM   985  H HG   . SER   A 1 68  ? 24.499 -11.596 13.409  0 30      ? 80  SER   B HG   1 c 1 
ATOM   986  N N    . LEU   A 1 69  ? 22.497 -10.082 8.829   1 42.621  ? 81  LEU   B N    1 ? 1 
ATOM   987  C CA   . LEU   A 1 69  ? 21.463 -9.877  7.832   1 37.663  ? 81  LEU   B CA   1 ? 1 
ATOM   988  C C    . LEU   A 1 69  ? 20.317 -10.848 8.088   1 39.843  ? 81  LEU   B C    1 ? 1 
ATOM   989  O O    . LEU   A 1 69  ? 20.539 -12.03  8.349   1 38.609  ? 81  LEU   B O    1 ? 1 
ATOM   990  C CB   . LEU   A 1 69  ? 22.079 -10.102 6.457   1 39.539  ? 81  LEU   B CB   1 ? 1 
ATOM   991  C CG   . LEU   A 1 69  ? 21.146 -9.891  5.265   1 42.751  ? 81  LEU   B CG   1 ? 1 
ATOM   992  C CD1  . LEU   A 1 69  ? 20.665 -8.456  5.159   1 42.786  ? 81  LEU   B CD1  1 ? 1 
ATOM   993  C CD2  . LEU   A 1 69  ? 21.846 -10.299 3.977   1 45.038  ? 81  LEU   B CD2  1 ? 1 
ATOM   994  H H    . LEU   A 1 69  ? 23.28  -10.474 8.568   1 43.348  ? 81  LEU   B H    1 c 1 
ATOM   995  H HA   . LEU   A 1 69  ? 21.134 -8.945  7.902   1 37.793  ? 81  LEU   B HA   1 c 1 
ATOM   996  H HB2  . LEU   A 1 69  ? 22.847 -9.494  6.361   1 40.423  ? 81  LEU   B HB2  1 c 1 
ATOM   997  H HB3  . LEU   A 1 69  ? 22.423 -11.025 6.422   1 41.508  ? 81  LEU   B HB3  1 c 1 
ATOM   998  H HG   . LEU   A 1 69  ? 20.353 -10.475 5.381   1 42.314  ? 81  LEU   B HG   1 c 1 
ATOM   999  H HD11 . LEU   A 1 69  ? 20.135 -8.232  5.942   1 41.538  ? 81  LEU   B HD11 1 c 1 
ATOM   1000 H HD12 . LEU   A 1 69  ? 20.122 -8.354  4.361   1 41.791  ? 81  LEU   B HD12 1 c 1 
ATOM   1001 H HD13 . LEU   A 1 69  ? 21.431 -7.86   5.107   1 42.469  ? 81  LEU   B HD13 1 c 1 
ATOM   1002 H HD21 . LEU   A 1 69  ? 22.195 -11.202 4.067   1 46.022  ? 81  LEU   B HD21 1 c 1 
ATOM   1003 H HD22 . LEU   A 1 69  ? 22.577 -9.685  3.798   1 44.954  ? 81  LEU   B HD22 1 c 1 
ATOM   1004 H HD23 . LEU   A 1 69  ? 21.213 -10.27  3.24    1 44.333  ? 81  LEU   B HD23 1 c 1 
ATOM   1005 N N    . GLY   A 1 70  ? 19.092 -10.31  8.028   1 38.577  ? 82  GLY   B N    1 ? 1 
ATOM   1006 C CA   . GLY   A 1 70  ? 17.893 -11.106 8.088   1 38.453  ? 82  GLY   B CA   1 ? 1 
ATOM   1007 C C    . GLY   A 1 70  ? 17.536 -11.53  9.51    1 43.53   ? 82  GLY   B C    1 ? 1 
ATOM   1008 O O    . GLY   A 1 70  ? 16.7   -12.421 9.666   1 50.816  ? 82  GLY   B O    1 ? 1 
ATOM   1009 H H    . GLY   A 1 70  ? 19.01  -9.403  7.947   1 37.33   ? 82  GLY   B H    1 c 1 
ATOM   1010 H HA2  . GLY   A 1 70  ? 17.147 -10.588 7.706   1 38.387  ? 82  GLY   B HA2  1 c 1 
ATOM   1011 H HA3  . GLY   A 1 70  ? 18.016 -11.909 7.53    1 40.213  ? 82  GLY   B HA3  1 c 1 
ATOM   1012 N N    . LYS   A 1 71  ? 18.172 -10.935 10.533  1 43.75   ? 83  LYS   B N    1 ? 1 
ATOM   1013 C CA   . LYS   A 1 71  ? 17.953 -11.36  11.916  1 44.41   ? 83  LYS   B CA   1 ? 1 
ATOM   1014 C C    . LYS   A 1 71  ? 17.187 -10.278 12.677  1 48.797  ? 83  LYS   B C    1 ? 1 
ATOM   1015 O O    . LYS   A 1 71  ? 17.186 -10.259 13.896  1 50.291  ? 83  LYS   B O    1 ? 1 
ATOM   1016 C CB   . LYS   A 1 71  ? 19.269 -11.769 12.599  1 45.177  ? 83  LYS   B CB   1 ? 1 
ATOM   1017 H H    . LYS   A 1 71  ? 18.746 -10.242 10.37   1 42.77   ? 83  LYS   B H    1 c 1 
ATOM   1018 H HA   . LYS   A 1 71  ? 17.383 -12.169 11.898  1 46.215  ? 83  LYS   B HA   1 c 1 
ATOM   1019 H HB2  . LYS   A 1 71  ? 19.993 -11.458 12.103  0 30      ? 83  LYS   B HB2  1 c 1 
ATOM   1020 H HB3  . LYS   A 1 71  ? 19.005 -12.228 13.476  0 30      ? 83  LYS   B HB3  1 c 1 
ATOM   1021 N N    . GLY   A 1 72  ? 16.547 -9.345  11.955  1 56.936  ? 84  GLY   B N    1 ? 1 
ATOM   1022 C CA   . GLY   A 1 72  ? 15.661 -8.363  12.565  1 58.739  ? 84  GLY   B CA   1 ? 1 
ATOM   1023 C C    . GLY   A 1 72  ? 16.387 -7.271  13.359  1 53.167  ? 84  GLY   B C    1 ? 1 
ATOM   1024 O O    . GLY   A 1 72  ? 15.745 -6.54   14.097  1 50.169  ? 84  GLY   B O    1 ? 1 
ATOM   1025 H H    . GLY   A 1 72  ? 16.667 -9.318  11.05   1 53.232  ? 84  GLY   B H    1 c 1 
ATOM   1026 H HA2  . GLY   A 1 72  ? 15.126 -7.94   11.853  1 55.567  ? 84  GLY   B HA2  1 c 1 
ATOM   1027 H HA3  . GLY   A 1 72  ? 15.036 -8.834  13.165  1 58.056  ? 84  GLY   B HA3  1 c 1 
ATOM   1028 N N    . GLN   A 1 73  ? 17.706 -7.132  13.2    1 44.746  ? 85  GLN   B N    1 ? 1 
ATOM   1029 C CA   . GLN   A 1 73  ? 18.445 -6.143  13.951  1 43.049  ? 85  GLN   B CA   1 ? 1 
ATOM   1030 C C    . GLN   A 1 73  ? 18.368 -4.774  13.299  1 37.764  ? 85  GLN   B C    1 ? 1 
ATOM   1031 O O    . GLN   A 1 73  ? 18.75  -3.818  13.942  1 38.245  ? 85  GLN   B O    1 ? 1 
ATOM   1032 C CB   . GLN   A 1 73  ? 19.908 -6.546  14.036  1 47.55   ? 85  GLN   B CB   1 ? 1 
ATOM   1033 C CG   . GLN   A 1 73  ? 20.127 -7.876  14.732  1 51.931  ? 85  GLN   B CG   1 ? 1 
ATOM   1034 C CD   . GLN   A 1 73  ? 21.57  -8.297  14.651  1 54.739  ? 85  GLN   B CD   1 ? 1 
ATOM   1035 O OE1  . GLN   A 1 73  ? 22.373 -7.682  13.946  1 55.677  ? 85  GLN   B OE1  1 ? 1 
ATOM   1036 N NE2  . GLN   A 1 73  ? 21.9   -9.368  15.348  1 60.307  ? 85  GLN   B NE2  1 ? 1 
ATOM   1037 H H    . GLN   A 1 73  ? 18.152 -7.658  12.6    1 45.87   ? 85  GLN   B H    1 c 1 
ATOM   1038 H HA   . GLN   A 1 73  ? 18.068 -6.088  14.866  1 44.751  ? 85  GLN   B HA   1 c 1 
ATOM   1039 H HB2  . GLN   A 1 73  ? 20.272 -6.595  13.127  1 46.213  ? 85  GLN   B HB2  1 c 1 
ATOM   1040 H HB3  . GLN   A 1 73  ? 20.401 -5.849  14.518  1 48.119  ? 85  GLN   B HB3  1 c 1 
ATOM   1041 H HG2  . GLN   A 1 73  ? 19.863 -7.802  15.674  1 53.182  ? 85  GLN   B HG2  1 c 1 
ATOM   1042 H HG3  . GLN   A 1 73  ? 19.568 -8.564  14.313  1 51.051  ? 85  GLN   B HG3  1 c 1 
ATOM   1043 H HE21 . GLN   A 1 73  ? 22.745 -9.636  15.372  1 60.712  ? 85  GLN   B HE21 1 c 1 
ATOM   1044 H HE22 . GLN   A 1 73  ? 21.278 -9.819  15.792  1 59.938  ? 85  GLN   B HE22 1 c 1 
ATOM   1045 N N    . VAL   A 1 74  ? 17.884 -4.705  12.048  1 36.364  ? 86  VAL   B N    1 ? 1 
ATOM   1046 C CA   . VAL   A 1 74  ? 17.565 -3.459  11.367  1 34.707  ? 86  VAL   B CA   1 ? 1 
ATOM   1047 C C    . VAL   A 1 74  ? 16.118 -3.488  10.89   1 32.205  ? 86  VAL   B C    1 ? 1 
ATOM   1048 O O    . VAL   A 1 74  ? 15.492 -4.522  10.943  1 34.929  ? 86  VAL   B O    1 ? 1 
ATOM   1049 C CB   . VAL   A 1 74  ? 18.547 -3.297  10.195  1 35.739  ? 86  VAL   B CB   1 ? 1 
ATOM   1050 C CG1  . VAL   A 1 74  ? 19.923 -2.94   10.719  1 40.377  ? 86  VAL   B CG1  1 ? 1 
ATOM   1051 C CG2  . VAL   A 1 74  ? 18.601 -4.55   9.315   1 35.624  ? 86  VAL   B CG2  1 ? 1 
ATOM   1052 H H    . VAL   A 1 74  ? 17.737 -5.486  11.599  1 36.053  ? 86  VAL   B H    1 c 1 
ATOM   1053 H HA   . VAL   A 1 74  ? 17.682 -2.714  11.988  1 35.417  ? 86  VAL   B HA   1 c 1 
ATOM   1054 H HB   . VAL   A 1 74  ? 18.225 -2.547  9.642   1 35.15   ? 86  VAL   B HB   1 c 1 
ATOM   1055 H HG11 . VAL   A 1 74  ? 20.249 -3.656  11.29   1 40.467  ? 86  VAL   B HG11 1 c 1 
ATOM   1056 H HG12 . VAL   A 1 74  ? 19.871 -2.116  11.231  1 39.838  ? 86  VAL   B HG12 1 c 1 
ATOM   1057 H HG13 . VAL   A 1 74  ? 20.533 -2.819  9.972   1 39.309  ? 86  VAL   B HG13 1 c 1 
ATOM   1058 H HG21 . VAL   A 1 74  ? 19.094 -4.352  8.501   1 35.262  ? 86  VAL   B HG21 1 c 1 
ATOM   1059 H HG22 . VAL   A 1 74  ? 17.698 -4.828  9.085   1 34.989  ? 86  VAL   B HG22 1 c 1 
ATOM   1060 H HG23 . VAL   A 1 74  ? 19.048 -5.268  9.794   1 36.543  ? 86  VAL   B HG23 1 c 1 
ATOM   1061 N N    . ILE   A 1 75  ? 15.615 -2.368  10.366  1 31.565  ? 87  ILE   B N    1 ? 1 
ATOM   1062 C CA   . ILE   A 1 75  ? 14.321 -2.329  9.699   1 30.868  ? 87  ILE   B CA   1 ? 1 
ATOM   1063 C C    . ILE   A 1 75  ? 14.315 -3.269  8.495   1 28.742  ? 87  ILE   B C    1 ? 1 
ATOM   1064 O O    . ILE   A 1 75  ? 15.353 -3.513  7.896   1 27.527  ? 87  ILE   B O    1 ? 1 
ATOM   1065 C CB   . ILE   A 1 75  ? 13.937 -0.898  9.289   1 31.609  ? 87  ILE   B CB   1 ? 1 
ATOM   1066 C CG1  . ILE   A 1 75  ? 15.01  -0.278  8.358   1 34.039  ? 87  ILE   B CG1  1 ? 1 
ATOM   1067 C CG2  . ILE   A 1 75  ? 13.654 -0.053  10.524  1 33.837  ? 87  ILE   B CG2  1 ? 1 
ATOM   1068 C CD1  . ILE   A 1 75  ? 14.641 1.084   7.811   1 34.699  ? 87  ILE   B CD1  1 ? 1 
ATOM   1069 H H    . ILE   A 1 75  ? 16.095 -1.594  10.441  1 31.67   ? 87  ILE   B H    1 c 1 
ATOM   1070 H HA   . ILE   A 1 75  ? 13.65  -2.647  10.335  1 31.506  ? 87  ILE   B HA   1 c 1 
ATOM   1071 H HB   . ILE   A 1 75  ? 13.107 -0.956  8.776   1 31.933  ? 87  ILE   B HB   1 c 1 
ATOM   1072 H HG12 . ILE   A 1 75  ? 15.85  -0.197  8.853   1 33.888  ? 87  ILE   B HG12 1 c 1 
ATOM   1073 H HG13 . ILE   A 1 75  ? 15.164 -0.884  7.606   1 33.098  ? 87  ILE   B HG13 1 c 1 
ATOM   1074 H HG21 . ILE   A 1 75  ? 13.31  0.815   10.255  1 33.401  ? 87  ILE   B HG21 1 c 1 
ATOM   1075 H HG22 . ILE   A 1 75  ? 14.474 0.068   11.031  1 33.935  ? 87  ILE   B HG22 1 c 1 
ATOM   1076 H HG23 . ILE   A 1 75  ? 12.995 -0.501  11.081  1 34.098  ? 87  ILE   B HG23 1 c 1 
ATOM   1077 H HD11 . ILE   A 1 75  ? 13.766 1.037   7.381   1 34.321  ? 87  ILE   B HD11 1 c 1 
ATOM   1078 H HD12 . ILE   A 1 75  ? 15.308 1.362   7.155   1 34.407  ? 87  ILE   B HD12 1 c 1 
ATOM   1079 H HD13 . ILE   A 1 75  ? 14.611 1.735   8.537   1 34.97   ? 87  ILE   B HD13 1 c 1 
ATOM   1080 N N    . LYS   A 1 76  ? 13.123 -3.807  8.197   1 32.683  ? 88  LYS   B N    1 ? 1 
ATOM   1081 C CA   . LYS   A 1 76  ? 12.892 -4.848  7.202   1 31.651  ? 88  LYS   B CA   1 ? 1 
ATOM   1082 C C    . LYS   A 1 76  ? 13.41  -4.433  5.838   1 28.312  ? 88  LYS   B C    1 ? 1 
ATOM   1083 O O    . LYS   A 1 76  ? 13.975 -5.239  5.123   1 31.994  ? 88  LYS   B O    1 ? 1 
ATOM   1084 C CB   . LYS   A 1 76  ? 11.394 -5.119  7.026   1 36.023  ? 88  LYS   B CB   1 ? 1 
ATOM   1085 H H    . LYS   A 1 76  ? 12.396 -3.492  8.653   1 31.872  ? 88  LYS   B H    1 c 1 
ATOM   1086 H HA   . LYS   A 1 76  ? 13.355 -5.675  7.491   1 32.361  ? 88  LYS   B HA   1 c 1 
ATOM   1087 H HB2  . LYS   A 1 76  ? 11.407 -6.162  6.634   0 30      ? 88  LYS   B HB2  1 c 1 
ATOM   1088 H HB3  . LYS   A 1 76  ? 10.913 -4.519  7.348   0 30      ? 88  LYS   B HB3  1 c 1 
ATOM   1089 N N    . ALA   A 1 77  ? 13.246 -3.163  5.494   1 30.543  ? 89  ALA   B N    1 ? 1 
ATOM   1090 C CA   . ALA   A 1 77  ? 13.755 -2.627  4.236   1 32.695  ? 89  ALA   B CA   1 ? 1 
ATOM   1091 C C    . ALA   A 1 77  ? 15.258 -2.848  4.083   1 34.178  ? 89  ALA   B C    1 ? 1 
ATOM   1092 O O    . ALA   A 1 77  ? 15.737 -3.048  2.964   1 28.215  ? 89  ALA   B O    1 ? 1 
ATOM   1093 C CB   . ALA   A 1 77  ? 13.449 -1.178  4.14    1 32.228  ? 89  ALA   B CB   1 ? 1 
ATOM   1094 H H    . ALA   A 1 77  ? 12.795 -2.602  6.057   1 30.352  ? 89  ALA   B H    1 c 1 
ATOM   1095 H HA   . ALA   A 1 77  ? 13.296 -3.103  3.491   1 33.026  ? 89  ALA   B HA   1 c 1 
ATOM   1096 H HB1  . ALA   A 1 77  ? 12.488 -1.043  4.182   1 32.644  ? 89  ALA   B HB1  1 c 1 
ATOM   1097 H HB2  . ALA   A 1 77  ? 13.872 -0.705  4.876   1 32.026  ? 89  ALA   B HB2  1 c 1 
ATOM   1098 H HB3  . ALA   A 1 77  ? 13.786 -0.828  3.298   1 32.561  ? 89  ALA   B HB3  1 c 1 
ATOM   1099 N N    . TRP   A 1 78  ? 16.006 -2.821  5.199   1 34.678  ? 90  TRP   B N    1 ? 1 
ATOM   1100 C CA   . TRP   A 1 78  ? 17.449 -3.063  5.105   1 33.491  ? 90  TRP   B CA   1 ? 1 
ATOM   1101 C C    . TRP   A 1 78  ? 17.735 -4.537  4.875   1 30.84   ? 90  TRP   B C    1 ? 1 
ATOM   1102 O O    . TRP   A 1 78  ? 18.581 -4.875  4.079   1 36.539  ? 90  TRP   B O    1 ? 1 
ATOM   1103 C CB   . TRP   A 1 78  ? 18.19  -2.582  6.358   1 32.497  ? 90  TRP   B CB   1 ? 1 
ATOM   1104 C CG   . TRP   A 1 78  ? 18.644 -1.158  6.243   1 32.745  ? 90  TRP   B CG   1 ? 1 
ATOM   1105 C CD1  . TRP   A 1 78  ? 17.917 -0.069  5.861   1 29.886  ? 90  TRP   B CD1  1 ? 1 
ATOM   1106 C CD2  . TRP   A 1 78  ? 19.981 -0.693  6.473   1 31.761  ? 90  TRP   B CD2  1 ? 1 
ATOM   1107 N NE1  . TRP   A 1 78  ? 18.697 1.048   5.885   1 29.097  ? 90  TRP   B NE1  1 ? 1 
ATOM   1108 C CE2  . TRP   A 1 78  ? 19.972 0.698   6.24    1 31.783  ? 90  TRP   B CE2  1 ? 1 
ATOM   1109 C CE3  . TRP   A 1 78  ? 21.167 -1.318  6.867   1 36.281  ? 90  TRP   B CE3  1 ? 1 
ATOM   1110 C CZ2  . TRP   A 1 78  ? 21.111 1.485   6.405   1 33.89   ? 90  TRP   B CZ2  1 ? 1 
ATOM   1111 C CZ3  . TRP   A 1 78  ? 22.298 -0.546  7.014   1 38.1    ? 90  TRP   B CZ3  1 ? 1 
ATOM   1112 C CH2  . TRP   A 1 78  ? 22.268 0.84    6.774   1 37.153  ? 90  TRP   B CH2  1 ? 1 
ATOM   1113 H H    . TRP   A 1 78  ? 15.629 -2.641  6.012   1 33.889  ? 90  TRP   B H    1 c 1 
ATOM   1114 H HA   . TRP   A 1 78  ? 17.8   -2.552  4.326   1 33.09   ? 90  TRP   B HA   1 c 1 
ATOM   1115 H HB2  . TRP   A 1 78  ? 17.594 -2.667  7.133   1 32.654  ? 90  TRP   B HB2  1 c 1 
ATOM   1116 H HB3  . TRP   A 1 78  ? 18.973 -3.155  6.502   1 33.424  ? 90  TRP   B HB3  1 c 1 
ATOM   1117 H HD1  . TRP   A 1 78  ? 16.997 -0.073  5.65    1 29.548  ? 90  TRP   B HD1  1 c 1 
ATOM   1118 H HE1  . TRP   A 1 78  ? 18.431 1.851   5.682   1 30.041  ? 90  TRP   B HE1  1 c 1 
ATOM   1119 H HE3  . TRP   A 1 78  ? 21.191 -2.246  7.026   1 35.535  ? 90  TRP   B HE3  1 c 1 
ATOM   1120 H HZ2  . TRP   A 1 78  ? 21.095 2.411   6.238   1 34.679  ? 90  TRP   B HZ2  1 c 1 
ATOM   1121 H HZ3  . TRP   A 1 78  ? 23.105 -0.954  7.276   1 38.874  ? 90  TRP   B HZ3  1 c 1 
ATOM   1122 H HH2  . TRP   A 1 78  ? 23.056 1.342   6.885   1 38.416  ? 90  TRP   B HH2  1 c 1 
ATOM   1123 N N    . ASP   A 1 79  ? 17.046 -5.408  5.595   1 33.764  ? 91  ASP   B N    1 ? 1 
ATOM   1124 C CA   . ASP   A 1 79  ? 17.193 -6.844  5.403   1 34.416  ? 91  ASP   B CA   1 ? 1 
ATOM   1125 C C    . ASP   A 1 79  ? 16.932 -7.193  3.933   1 35.405  ? 91  ASP   B C    1 ? 1 
ATOM   1126 O O    . ASP   A 1 79  ? 17.694 -7.905  3.328   1 40.849  ? 91  ASP   B O    1 ? 1 
ATOM   1127 C CB   . ASP   A 1 79  ? 16.335 -7.619  6.398   1 32.891  ? 91  ASP   B CB   1 ? 1 
ATOM   1128 C CG   . ASP   A 1 79  ? 16.929 -7.788  7.805   1 35.15   ? 91  ASP   B CG   1 ? 1 
ATOM   1129 O OD1  . ASP   A 1 79  ? 18.197 -7.639  7.977   1 31.336  ? 91  ASP   B OD1  1 ? 1 
ATOM   1130 O OD2  . ASP   A 1 79  ? 16.116 -8.079  8.734   1 37.985  ? 91  ASP   B OD2  1 ? 1 
ATOM   1131 H H    . ASP   A 1 79  ? 16.469 -5.105  6.236   1 32.748  ? 91  ASP   B H    1 c 1 
ATOM   1132 H HA   . ASP   A 1 79  ? 18.127 -7.075  5.6     1 34.711  ? 91  ASP   B HA   1 c 1 
ATOM   1133 H HB2  . ASP   A 1 79  ? 15.469 -7.168  6.486   1 33.322  ? 91  ASP   B HB2  1 c 1 
ATOM   1134 H HB3  . ASP   A 1 79  ? 16.168 -8.513  6.034   1 34.482  ? 91  ASP   B HB3  1 c 1 
ATOM   1135 N N    . ILE   A 1 80  ? 15.862 -6.674  3.35    1 34.442  ? 92  ILE   B N    1 ? 1 
ATOM   1136 C CA   . ILE   A 1 80  ? 15.523 -6.924  1.959   1 36.098  ? 92  ILE   B CA   1 ? 1 
ATOM   1137 C C    . ILE   A 1 80  ? 16.537 -6.241  1.031   1 37.951  ? 92  ILE   B C    1 ? 1 
ATOM   1138 O O    . ILE   A 1 80  ? 17.06  -6.86   0.106   1 38.205  ? 92  ILE   B O    1 ? 1 
ATOM   1139 C CB   . ILE   A 1 80  ? 14.091 -6.407  1.706   1 39.339  ? 92  ILE   B CB   1 ? 1 
ATOM   1140 C CG1  . ILE   A 1 80  ? 13.055 -7.24   2.454   1 42.56   ? 92  ILE   B CG1  1 ? 1 
ATOM   1141 C CG2  . ILE   A 1 80  ? 13.788 -6.339  0.207   1 44.09   ? 92  ILE   B CG2  1 ? 1 
ATOM   1142 C CD1  . ILE   A 1 80  ? 11.732 -6.515  2.656   1 46.646  ? 92  ILE   B CD1  1 ? 1 
ATOM   1143 H H    . ILE   A 1 80  ? 15.309 -6.14   3.844   1 34.311  ? 92  ILE   B H    1 c 1 
ATOM   1144 H HA   . ILE   A 1 80  ? 15.542 -7.887  1.797   1 37.756  ? 92  ILE   B HA   1 c 1 
ATOM   1145 H HB   . ILE   A 1 80  ? 14.042 -5.496  2.058   1 38.89   ? 92  ILE   B HB   1 c 1 
ATOM   1146 H HG12 . ILE   A 1 80  ? 12.89  -8.064  1.952   1 44.015  ? 92  ILE   B HG12 1 c 1 
ATOM   1147 H HG13 . ILE   A 1 80  ? 13.416 -7.487  3.329   1 42.231  ? 92  ILE   B HG13 1 c 1 
ATOM   1148 H HG21 . ILE   A 1 80  ? 12.848 -6.132  0.073   1 43.568  ? 92  ILE   B HG21 1 c 1 
ATOM   1149 H HG22 . ILE   A 1 80  ? 13.991 -7.195  -0.206  1 44.166  ? 92  ILE   B HG22 1 c 1 
ATOM   1150 H HG23 . ILE   A 1 80  ? 14.33  -5.646  -0.207  1 42.842  ? 92  ILE   B HG23 1 c 1 
ATOM   1151 H HD11 . ILE   A 1 80  ? 11.886 -5.69   3.155   1 44.371  ? 92  ILE   B HD11 1 c 1 
ATOM   1152 H HD12 . ILE   A 1 80  ? 11.119 -7.086  3.157   1 46.148  ? 92  ILE   B HD12 1 c 1 
ATOM   1153 H HD13 . ILE   A 1 80  ? 11.339 -6.299  1.79    1 46.192  ? 92  ILE   B HD13 1 c 1 
ATOM   1154 N N    . GLY   A 1 81  ? 16.835 -4.959  1.304   1 35.665  ? 93  GLY   B N    1 ? 1 
ATOM   1155 C CA   . GLY   A 1 81  ? 17.607 -4.127  0.403   1 33.972  ? 93  GLY   B CA   1 ? 1 
ATOM   1156 C C    . GLY   A 1 81  ? 19.053 -4.587  0.318   1 33.618  ? 93  GLY   B C    1 ? 1 
ATOM   1157 O O    . GLY   A 1 81  ? 19.61  -4.779  -0.764  1 35.863  ? 93  GLY   B O    1 ? 1 
ATOM   1158 H H    . GLY   A 1 81  ? 16.537 -4.591  2.086   1 34.607  ? 93  GLY   B H    1 c 1 
ATOM   1159 H HA2  . GLY   A 1 81  ? 17.199 -4.158  -0.494  1 35.071  ? 93  GLY   B HA2  1 c 1 
ATOM   1160 H HA3  . GLY   A 1 81  ? 17.576 -3.194  0.718   1 33.621  ? 93  GLY   B HA3  1 c 1 
ATOM   1161 N N    . VAL   A 1 82  ? 19.663 -4.762  1.487   1 32.248  ? 94  VAL   B N    1 ? 1 
ATOM   1162 C CA   . VAL   A 1 82  ? 21.078 -5.088  1.518   1 33.45   ? 94  VAL   B CA   1 ? 1 
ATOM   1163 C C    . VAL   A 1 82  ? 21.31  -6.492  0.96    1 35.913  ? 94  VAL   B C    1 ? 1 
ATOM   1164 O O    . VAL   A 1 82  ? 22.375 -6.743  0.406   1 40.587  ? 94  VAL   B O    1 ? 1 
ATOM   1165 C CB   . VAL   A 1 82  ? 21.639 -4.907  2.938   1 34.873  ? 94  VAL   B CB   1 ? 1 
ATOM   1166 C CG1  . VAL   A 1 82  ? 23.019 -5.526  3.092   1 38.384  ? 94  VAL   B CG1  1 ? 1 
ATOM   1167 C CG2  . VAL   A 1 82  ? 21.678 -3.434  3.316   1 36.824  ? 94  VAL   B CG2  1 ? 1 
ATOM   1168 H H    . VAL   A 1 82  ? 19.202 -4.676  2.272   1 31.599  ? 94  VAL   B H    1 c 1 
ATOM   1169 H HA   . VAL   A 1 82  ? 21.541 -4.455  0.935   1 34.744  ? 94  VAL   B HA   1 c 1 
ATOM   1170 H HB   . VAL   A 1 82  ? 21.027 -5.369  3.557   1 34.575  ? 94  VAL   B HB   1 c 1 
ATOM   1171 H HG11 . VAL   A 1 82  ? 23.584 -5.25   2.35    1 38.929  ? 94  VAL   B HG11 1 c 1 
ATOM   1172 H HG12 . VAL   A 1 82  ? 22.945 -6.495  3.1     1 38.223  ? 94  VAL   B HG12 1 c 1 
ATOM   1173 H HG13 . VAL   A 1 82  ? 23.415 -5.227  3.927   1 38.134  ? 94  VAL   B HG13 1 c 1 
ATOM   1174 H HG21 . VAL   A 1 82  ? 22.044 -3.337  4.212   1 36.254  ? 94  VAL   B HG21 1 c 1 
ATOM   1175 H HG22 . VAL   A 1 82  ? 20.778 -3.068  3.294   1 35.042  ? 94  VAL   B HG22 1 c 1 
ATOM   1176 H HG23 . VAL   A 1 82  ? 22.238 -2.951  2.685   1 36.976  ? 94  VAL   B HG23 1 c 1 
ATOM   1177 N N    . ALA   A 1 83  ? 20.323 -7.404  1.078   1 35.65   ? 95  ALA   B N    1 ? 1 
ATOM   1178 C CA   . ALA   A 1 83  ? 20.448 -8.739  0.516   1 40.541  ? 95  ALA   B CA   1 ? 1 
ATOM   1179 C C    . ALA   A 1 83  ? 20.561 -8.705  -1.009  1 39.432  ? 95  ALA   B C    1 ? 1 
ATOM   1180 O O    . ALA   A 1 83  ? 20.896 -9.723  -1.595  1 44.16   ? 95  ALA   B O    1 ? 1 
ATOM   1181 C CB   . ALA   A 1 83  ? 19.27  -9.634  0.922   1 38.437  ? 95  ALA   B CB   1 ? 1 
ATOM   1182 H H    . ALA   A 1 83  ? 19.559 -7.186  1.529   1 35.246  ? 95  ALA   B H    1 c 1 
ATOM   1183 H HA   . ALA   A 1 83  ? 21.288 -9.14   0.873   1 39.755  ? 95  ALA   B HA   1 c 1 
ATOM   1184 H HB1  . ALA   A 1 83  ? 19.228 -9.7    1.891   1 38.268  ? 95  ALA   B HB1  1 c 1 
ATOM   1185 H HB2  . ALA   A 1 83  ? 18.44  -9.254  0.59    1 38.516  ? 95  ALA   B HB2  1 c 1 
ATOM   1186 H HB3  . ALA   A 1 83  ? 19.39  -10.522 0.545   1 40.334  ? 95  ALA   B HB3  1 c 1 
ATOM   1187 N N    . THR   A 1 84  ? 20.177 -7.597  -1.646  1 39.415  ? 96  THR   B N    1 ? 1 
ATOM   1188 C CA   . THR   A 1 84  ? 20.303 -7.461  -3.104  1 41.656  ? 96  THR   B CA   1 ? 1 
ATOM   1189 C C    . THR   A 1 84  ? 21.637 -6.83   -3.505  1 45.92   ? 96  THR   B C    1 ? 1 
ATOM   1190 O O    . THR   A 1 84  ? 21.852 -6.643  -4.694  1 45.837  ? 96  THR   B O    1 ? 1 
ATOM   1191 C CB   . THR   A 1 84  ? 19.174 -6.612  -3.697  1 38.914  ? 96  THR   B CB   1 ? 1 
ATOM   1192 O OG1  . THR   A 1 84  ? 19.456 -5.279  -3.26   1 38.262  ? 96  THR   B OG1  1 ? 1 
ATOM   1193 C CG2  . THR   A 1 84  ? 17.781 -7.077  -3.277  1 36.002  ? 96  THR   B CG2  1 ? 1 
ATOM   1194 H H    . THR   A 1 84  ? 19.803 -6.911  -1.173  1 37.974  ? 96  THR   B H    1 c 1 
ATOM   1195 H HA   . THR   A 1 84  ? 20.251 -8.357  -3.502  1 42.997  ? 96  THR   B HA   1 c 1 
ATOM   1196 H HB   . THR   A 1 84  ? 19.228 -6.646  -4.682  1 40.959  ? 96  THR   B HB   1 c 1 
ATOM   1197 H HG1  . THR   A 1 84  ? 19.398 -5.198  -2.379  0 30      ? 96  THR   B HG1  1 c 1 
ATOM   1198 H HG21 . THR   A 1 84  ? 17.111 -6.515  -3.701  1 36.776  ? 96  THR   B HG21 1 c 1 
ATOM   1199 H HG22 . THR   A 1 84  ? 17.693 -7.01   -2.312  1 35.034  ? 96  THR   B HG22 1 c 1 
ATOM   1200 H HG23 . THR   A 1 84  ? 17.65  -8      -3.551  1 37.768  ? 96  THR   B HG23 1 c 1 
ATOM   1201 N N    . MET   A 1 85  ? 22.506 -6.451  -2.552  1 43.036  ? 97  MET   B N    1 ? 1 
ATOM   1202 C CA   . MET   A 1 85  ? 23.716 -5.717  -2.908  1 45.529  ? 97  MET   B CA   1 ? 1 
ATOM   1203 C C    . MET   A 1 85  ? 24.955 -6.622  -3.033  1 46.048  ? 97  MET   B C    1 ? 1 
ATOM   1204 O O    . MET   A 1 85  ? 25.034 -7.706  -2.446  1 42.186  ? 97  MET   B O    1 ? 1 
ATOM   1205 C CB   . MET   A 1 85  ? 23.981 -4.601  -1.892  1 43.156  ? 97  MET   B CB   1 ? 1 
ATOM   1206 C CG   . MET   A 1 85  ? 22.935 -3.507  -1.928  1 41.856  ? 97  MET   B CG   1 ? 1 
ATOM   1207 S SD   . MET   A 1 85  ? 23.139 -2.358  -0.561  1 41.643  ? 97  MET   B SD   1 ? 1 
ATOM   1208 C CE   . MET   A 1 85  ? 24.441 -1.299  -1.213  1 49.295  ? 97  MET   B CE   1 ? 1 
ATOM   1209 H H    . MET   A 1 85  ? 22.349 -6.652  -1.675  1 42.356  ? 97  MET   B H    1 c 1 
ATOM   1210 H HA   . MET   A 1 85  ? 23.563 -5.3    -3.793  1 45.926  ? 97  MET   B HA   1 c 1 
ATOM   1211 H HB2  . MET   A 1 85  ? 24.005 -4.993  -0.993  1 42.475  ? 97  MET   B HB2  1 c 1 
ATOM   1212 H HB3  . MET   A 1 85  ? 24.861 -4.209  -2.074  1 44.986  ? 97  MET   B HB3  1 c 1 
ATOM   1213 H HG2  . MET   A 1 85  ? 23.004 -3.016  -2.767  1 43.253  ? 97  MET   B HG2  1 c 1 
ATOM   1214 H HG3  . MET   A 1 85  ? 22.043 -3.904  -1.879  1 40.902  ? 97  MET   B HG3  1 c 1 
ATOM   1215 H HE1  . MET   A 1 85  ? 24.698 -0.647  -0.535  1 47.774  ? 97  MET   B HE1  1 c 1 
ATOM   1216 H HE2  . MET   A 1 85  ? 25.214 -1.844  -1.449  1 49.535  ? 97  MET   B HE2  1 c 1 
ATOM   1217 H HE3  . MET   A 1 85  ? 24.115 -0.834  -2.005  1 48.587  ? 97  MET   B HE3  1 c 1 
ATOM   1218 N N    . LYS   A 1 86  ? 25.915 -6.158  -3.856  1 46.921  ? 98  LYS   B N    1 ? 1 
ATOM   1219 C CA   . LYS   A 1 86  ? 27.212 -6.795  -4.043  1 48.878  ? 98  LYS   B CA   1 ? 1 
ATOM   1220 C C    . LYS   A 1 86  ? 28.296 -6.023  -3.274  1 50.105  ? 98  LYS   B C    1 ? 1 
ATOM   1221 O O    . LYS   A 1 86  ? 28.129 -4.836  -2.977  1 46.099  ? 98  LYS   B O    1 ? 1 
ATOM   1222 C CB   . LYS   A 1 86  ? 27.565 -6.897  -5.535  1 51.85   ? 98  LYS   B CB   1 ? 1 
ATOM   1223 H H    . LYS   A 1 86  ? 25.745 -5.391  -4.322  1 47.388  ? 98  LYS   B H    1 c 1 
ATOM   1224 H HA   . LYS   A 1 86  ? 27.163 -7.714  -3.676  1 48.821  ? 98  LYS   B HA   1 c 1 
ATOM   1225 H HB2  . LYS   A 1 86  ? 28.409 -7.022  -5.714  0 30      ? 98  LYS   B HB2  1 c 1 
ATOM   1226 H HB3  . LYS   A 1 86  ? 26.574 -7.065  -6.006  0 30      ? 98  LYS   B HB3  1 c 1 
ATOM   1227 N N    . LYS   A 1 87  ? 29.408 -6.714  -2.949  1 52.745  ? 99  LYS   B N    1 ? 1 
ATOM   1228 C CA   . LYS   A 1 87  ? 30.584 -6.088  -2.364  1 55.408  ? 99  LYS   B CA   1 ? 1 
ATOM   1229 C C    . LYS   A 1 87  ? 30.966 -4.899  -3.243  1 58.244  ? 99  LYS   B C    1 ? 1 
ATOM   1230 O O    . LYS   A 1 87  ? 31.102 -5.063  -4.445  1 59.846  ? 99  LYS   B O    1 ? 1 
ATOM   1231 C CB   . LYS   A 1 87  ? 31.808 -7.017  -2.256  1 58.302  ? 99  LYS   B CB   1 ? 1 
ATOM   1232 H H    . LYS   A 1 87  ? 29.425 -7.616  -3.101  1 53.444  ? 99  LYS   B H    1 c 1 
ATOM   1233 H HA   . LYS   A 1 87  ? 30.346 -5.759  -1.461  1 53.502  ? 99  LYS   B HA   1 c 1 
ATOM   1234 H HB2  . LYS   A 1 87  ? 32.639 -6.502  -2.35   0 30      ? 99  LYS   B HB2  1 c 1 
ATOM   1235 H HB3  . LYS   A 1 87  ? 31.507 -7.968  -2.188  0 30      ? 99  LYS   B HB3  1 c 1 
ATOM   1236 N N    . GLY   A 1 88  ? 31.059 -3.705  -2.647  1 59.742  ? 100 GLY   B N    1 ? 1 
ATOM   1237 C CA   . GLY   A 1 88  ? 31.527 -2.523  -3.359  1 64.416  ? 100 GLY   B CA   1 ? 1 
ATOM   1238 C C    . GLY   A 1 88  ? 30.387 -1.642  -3.876  1 61.76   ? 100 GLY   B C    1 ? 1 
ATOM   1239 O O    . GLY   A 1 88  ? 30.631 -0.493  -4.233  1 61.093  ? 100 GLY   B O    1 ? 1 
ATOM   1240 H H    . GLY   A 1 88  ? 30.823 -3.622  -1.768  1 57.837  ? 100 GLY   B H    1 c 1 
ATOM   1241 H HA2  . GLY   A 1 88  ? 32.094 -1.993  -2.751  1 64.738  ? 100 GLY   B HA2  1 c 1 
ATOM   1242 H HA3  . GLY   A 1 88  ? 32.089 -2.807  -4.118  1 66.526  ? 100 GLY   B HA3  1 c 1 
ATOM   1243 N N    . GLU   A 1 89  ? 29.163 -2.192  -3.911  1 59.177  ? 101 GLU   B N    1 ? 1 
ATOM   1244 C CA   . GLU   A 1 89  ? 27.977 -1.493  -4.391  1 57.826  ? 101 GLU   B CA   1 ? 1 
ATOM   1245 C C    . GLU   A 1 89  ? 27.612 -0.316  -3.471  1 57.399  ? 101 GLU   B C    1 ? 1 
ATOM   1246 O O    . GLU   A 1 89  ? 27.751 -0.375  -2.238  1 52.842  ? 101 GLU   B O    1 ? 1 
ATOM   1247 C CB   . GLU   A 1 89  ? 26.816 -2.488  -4.544  1 56.421  ? 101 GLU   B CB   1 ? 1 
ATOM   1248 C CG   . GLU   A 1 89  ? 25.551 -1.925  -5.198  1 54.468  ? 101 GLU   B CG   1 ? 1 
ATOM   1249 C CD   . GLU   A 1 89  ? 24.411 -2.923  -5.385  1 50.768  ? 101 GLU   B CD   1 ? 1 
ATOM   1250 O OE1  . GLU   A 1 89  ? 24.717 -4.02   -5.865  1 55.765  ? 101 GLU   B OE1  1 ? 1 
ATOM   1251 O OE2  . GLU   A 1 89  ? 23.229 -2.632  -5.066  1 46.969  ? 101 GLU   B OE2  1 ? 1 
ATOM   1252 H H    . GLU   A 1 89  ? 29.063 -3.051  -3.619  1 58.208  ? 101 GLU   B H    1 c 1 
ATOM   1253 H HA   . GLU   A 1 89  ? 28.185 -1.133  -5.288  1 60.446  ? 101 GLU   B HA   1 c 1 
ATOM   1254 H HB2  . GLU   A 1 89  ? 27.128 -3.249  -5.077  1 57.556  ? 101 GLU   B HB2  1 c 1 
ATOM   1255 H HB3  . GLU   A 1 89  ? 26.577 -2.827  -3.657  1 53.889  ? 101 GLU   B HB3  1 c 1 
ATOM   1256 H HG2  . GLU   A 1 89  ? 25.219 -1.18   -4.653  1 52.691  ? 101 GLU   B HG2  1 c 1 
ATOM   1257 H HG3  . GLU   A 1 89  ? 25.786 -1.559  -6.077  1 56.442  ? 101 GLU   B HG3  1 c 1 
ATOM   1258 N N    . ILE   A 1 90  ? 27.156 0.767   -4.118  1 58.449  ? 102 ILE   B N    1 ? 1 
ATOM   1259 C CA   . ILE   A 1 90  ? 26.402 1.841   -3.488  1 55.788  ? 102 ILE   B CA   1 ? 1 
ATOM   1260 C C    . ILE   A 1 90  ? 25.011 1.864   -4.115  1 52.074  ? 102 ILE   B C    1 ? 1 
ATOM   1261 O O    . ILE   A 1 90  ? 24.891 1.971   -5.337  1 53.067  ? 102 ILE   B O    1 ? 1 
ATOM   1262 C CB   . ILE   A 1 90  ? 27.11  3.211   -3.642  1 56.687  ? 102 ILE   B CB   1 ? 1 
ATOM   1263 C CG1  . ILE   A 1 90  ? 28.471 3.192   -2.96   1 61.176  ? 102 ILE   B CG1  1 ? 1 
ATOM   1264 C CG2  . ILE   A 1 90  ? 26.233 4.348   -3.111  1 53.147  ? 102 ILE   B CG2  1 ? 1 
ATOM   1265 C CD1  . ILE   A 1 90  ? 29.309 4.451   -3.159  1 69.842  ? 102 ILE   B CD1  1 ? 1 
ATOM   1266 H H    . ILE   A 1 90  ? 27.331 0.84    -5.012  1 60.198  ? 102 ILE   B H    1 c 1 
ATOM   1267 H HA   . ILE   A 1 90  ? 26.317 1.643   -2.54   1 53.308  ? 102 ILE   B HA   1 c 1 
ATOM   1268 H HB   . ILE   A 1 90  ? 27.257 3.364   -4.597  1 59.205  ? 102 ILE   B HB   1 c 1 
ATOM   1269 H HG12 . ILE   A 1 90  ? 28.334 3.058   -2.001  1 59.779  ? 102 ILE   B HG12 1 c 1 
ATOM   1270 H HG13 . ILE   A 1 90  ? 28.978 2.425   -3.297  1 62.784  ? 102 ILE   B HG13 1 c 1 
ATOM   1271 H HG21 . ILE   A 1 90  ? 26.725 5.185   -3.142  1 55.782  ? 102 ILE   B HG21 1 c 1 
ATOM   1272 H HG22 . ILE   A 1 90  ? 25.977 4.16    -2.192  1 51.638  ? 102 ILE   B HG22 1 c 1 
ATOM   1273 H HG23 . ILE   A 1 90  ? 25.433 4.428   -3.657  1 52.989  ? 102 ILE   B HG23 1 c 1 
ATOM   1274 H HD11 . ILE   A 1 90  ? 29.405 4.633   -4.113  1 70.277  ? 102 ILE   B HD11 1 c 1 
ATOM   1275 H HD12 . ILE   A 1 90  ? 30.192 4.316   -2.766  1 70.044  ? 102 ILE   B HD12 1 c 1 
ATOM   1276 H HD13 . ILE   A 1 90  ? 28.878 5.212   -2.727  1 67.303  ? 102 ILE   B HD13 1 c 1 
ATOM   1277 N N    . ALA   A 1 91  ? 23.988 1.887   -3.248  1 47.89   ? 103 ALA   B N    1 ? 1 
ATOM   1278 C CA   . ALA   A 1 91  ? 22.593 1.928   -3.655  1 46.723  ? 103 ALA   B CA   1 ? 1 
ATOM   1279 C C    . ALA   A 1 91  ? 21.861 3.057   -2.941  1 44.03   ? 103 ALA   B C    1 ? 1 
ATOM   1280 O O    . ALA   A 1 91  ? 22.279 3.441   -1.854  1 46.186  ? 103 ALA   B O    1 ? 1 
ATOM   1281 C CB   . ALA   A 1 91  ? 21.952 0.622   -3.311  1 46.252  ? 103 ALA   B CB   1 ? 1 
ATOM   1282 H H    . ALA   A 1 91  ? 24.173 1.878   -2.353  1 47.179  ? 103 ALA   B H    1 c 1 
ATOM   1283 H HA   . ALA   A 1 91  ? 22.545 2.081   -4.637  1 48.477  ? 103 ALA   B HA   1 c 1 
ATOM   1284 H HB1  . ALA   A 1 91  ? 22.402 -0.098  -3.785  1 46.886  ? 103 ALA   B HB1  1 c 1 
ATOM   1285 H HB2  . ALA   A 1 91  ? 22.02  0.467   -2.354  1 44.324  ? 103 ALA   B HB2  1 c 1 
ATOM   1286 H HB3  . ALA   A 1 91  ? 21.015 0.639   -3.568  1 45.101  ? 103 ALA   B HB3  1 c 1 
ATOM   1287 N N    . HIS   A 1 92  ? 20.764 3.543   -3.535  1 41.859  ? 104 HIS   B N    1 ? 1 
ATOM   1288 C CA   . HIS   A 1 92  ? 19.803 4.398   -2.85   1 41.36   ? 104 HIS   B CA   1 ? 1 
ATOM   1289 C C    . HIS   A 1 92  ? 18.507 3.627   -2.618  1 42.767  ? 104 HIS   B C    1 ? 1 
ATOM   1290 O O    . HIS   A 1 92  ? 18.054 2.931   -3.525  1 42.985  ? 104 HIS   B O    1 ? 1 
ATOM   1291 C CB   . HIS   A 1 92  ? 19.465 5.648   -3.663  1 44.402  ? 104 HIS   B CB   1 ? 1 
ATOM   1292 C CG   . HIS   A 1 92  ? 20.581 6.631   -3.746  1 46.296  ? 104 HIS   B CG   1 ? 1 
ATOM   1293 N ND1  . HIS   A 1 92  ? 20.513 7.771   -4.493  1 47.232  ? 104 HIS   B ND1  1 ? 1 
ATOM   1294 C CD2  . HIS   A 1 92  ? 21.781 6.653   -3.146  1 46.297  ? 104 HIS   B CD2  1 ? 1 
ATOM   1295 C CE1  . HIS   A 1 92  ? 21.656 8.417   -4.39   1 49.058  ? 104 HIS   B CE1  1 ? 1 
ATOM   1296 N NE2  . HIS   A 1 92  ? 22.433 7.756   -3.557  1 46.552  ? 104 HIS   B NE2  1 ? 1 
ATOM   1297 H H    . HIS   A 1 92  ? 20.607 3.331   -4.41   1 43.855  ? 104 HIS   B H    1 c 1 
ATOM   1298 H HA   . HIS   A 1 92  ? 20.174 4.663   -1.976  1 41.279  ? 104 HIS   B HA   1 c 1 
ATOM   1299 H HB2  . HIS   A 1 92  ? 19.215 5.374   -4.572  1 45.251  ? 104 HIS   B HB2  1 c 1 
ATOM   1300 H HB3  . HIS   A 1 92  ? 18.686 6.086   -3.257  1 43.164  ? 104 HIS   B HB3  1 c 1 
ATOM   1301 H HD1  . HIS   A 1 92  ? 19.814 7.958   -5.059  0 30      ? 104 HIS   B HD1  1 c 1 
ATOM   1302 H HD2  . HIS   A 1 92  ? 22.122 6.003   -2.565  1 44.703  ? 104 HIS   B HD2  1 c 1 
ATOM   1303 H HE1  . HIS   A 1 92  ? 21.861 9.238   -4.804  1 51.111  ? 104 HIS   B HE1  1 c 1 
ATOM   1304 H HE2  . HIS   A 1 92  ? 23.186 7.954   -3.282  0 30      ? 104 HIS   B HE2  1 c 1 
ATOM   1305 N N    . LEU   A 1 93  ? 17.934 3.736   -1.399  1 41.158  ? 105 LEU   B N    1 ? 1 
ATOM   1306 C CA   . LEU   A 1 93  ? 16.638 3.149   -1.088  1 38.117  ? 105 LEU   B CA   1 ? 1 
ATOM   1307 C C    . LEU   A 1 93  ? 15.662 4.216   -0.588  1 36.446  ? 105 LEU   B C    1 ? 1 
ATOM   1308 O O    . LEU   A 1 93  ? 16.002 4.977   0.308   1 37.448  ? 105 LEU   B O    1 ? 1 
ATOM   1309 C CB   . LEU   A 1 93  ? 16.8   2.059   -0.027  1 40.313  ? 105 LEU   B CB   1 ? 1 
ATOM   1310 C CG   . LEU   A 1 93  ? 17.763 0.905   -0.325  1 41.925  ? 105 LEU   B CG   1 ? 1 
ATOM   1311 C CD1  . LEU   A 1 93  ? 17.863 -0.067  0.868   1 41.838  ? 105 LEU   B CD1  1 ? 1 
ATOM   1312 C CD2  . LEU   A 1 93  ? 17.344 0.147   -1.574  1 42.821  ? 105 LEU   B CD2  1 ? 1 
ATOM   1313 H H    . LEU   A 1 93  ? 18.373 4.196   -0.742  1 40.436  ? 105 LEU   B H    1 c 1 
ATOM   1314 H HA   . LEU   A 1 93  ? 16.273 2.747   -1.911  1 39.609  ? 105 LEU   B HA   1 c 1 
ATOM   1315 H HB2  . LEU   A 1 93  ? 17.092 2.492   0.808   1 39.116  ? 105 LEU   B HB2  1 c 1 
ATOM   1316 H HB3  . LEU   A 1 93  ? 15.91  1.677   0.151   1 39.032  ? 105 LEU   B HB3  1 c 1 
ATOM   1317 H HG   . LEU   A 1 93  ? 18.664 1.287   -0.485  1 42.714  ? 105 LEU   B HG   1 c 1 
ATOM   1318 H HD11 . LEU   A 1 93  ? 18.189 0.411   1.649   1 41.118  ? 105 LEU   B HD11 1 c 1 
ATOM   1319 H HD12 . LEU   A 1 93  ? 18.478 -0.787  0.649   1 41.913  ? 105 LEU   B HD12 1 c 1 
ATOM   1320 H HD13 . LEU   A 1 93  ? 16.986 -0.439  1.059   1 40.847  ? 105 LEU   B HD13 1 c 1 
ATOM   1321 H HD21 . LEU   A 1 93  ? 17.394 0.735   -2.343  1 43.871  ? 105 LEU   B HD21 1 c 1 
ATOM   1322 H HD22 . LEU   A 1 93  ? 16.433 -0.173  -1.469  1 42.345  ? 105 LEU   B HD22 1 c 1 
ATOM   1323 H HD23 . LEU   A 1 93  ? 17.939 -0.61   -1.708  1 43.176  ? 105 LEU   B HD23 1 c 1 
ATOM   1324 N N    . LEU   A 1 94  ? 14.431 4.217   -1.113  1 36.469  ? 106 LEU   B N    1 ? 1 
ATOM   1325 C CA   . LEU   A 1 94  ? 13.314 5.003   -0.606  1 38.577  ? 106 LEU   B CA   1 ? 1 
ATOM   1326 C C    . LEU   A 1 94  ? 12.271 4.054   -0.007  1 38.434  ? 106 LEU   B C    1 ? 1 
ATOM   1327 O O    . LEU   A 1 94  ? 11.768 3.159   -0.678  1 36.822  ? 106 LEU   B O    1 ? 1 
ATOM   1328 C CB   . LEU   A 1 94  ? 12.676 5.855   -1.714  1 43.028  ? 106 LEU   B CB   1 ? 1 
ATOM   1329 C CG   . LEU   A 1 94  ? 11.5   6.749   -1.283  1 44.44   ? 106 LEU   B CG   1 ? 1 
ATOM   1330 C CD1  . LEU   A 1 94  ? 11.979 7.89    -0.401  1 43.646  ? 106 LEU   B CD1  1 ? 1 
ATOM   1331 C CD2  . LEU   A 1 94  ? 10.716 7.334   -2.417  1 52.181  ? 106 LEU   B CD2  1 ? 1 
ATOM   1332 H H    . LEU   A 1 94  ? 14.279 3.689   -1.844  1 37.774  ? 106 LEU   B H    1 c 1 
ATOM   1333 H HA   . LEU   A 1 94  ? 13.65  5.6     0.109   1 38.265  ? 106 LEU   B HA   1 c 1 
ATOM   1334 H HB2  . LEU   A 1 94  ? 13.377 6.429   -2.101  1 43.609  ? 106 LEU   B HB2  1 c 1 
ATOM   1335 H HB3  . LEU   A 1 94  ? 12.362 5.249   -2.424  1 43.417  ? 106 LEU   B HB3  1 c 1 
ATOM   1336 H HG   . LEU   A 1 94  ? 10.876 6.197   -0.745  1 44.222  ? 106 LEU   B HG   1 c 1 
ATOM   1337 H HD11 . LEU   A 1 94  ? 12.371 7.53    0.412   1 42.404  ? 106 LEU   B HD11 1 c 1 
ATOM   1338 H HD12 . LEU   A 1 94  ? 11.227 8.461   -0.17   1 44.484  ? 106 LEU   B HD12 1 c 1 
ATOM   1339 H HD13 . LEU   A 1 94  ? 12.646 8.411   -0.878  1 44.803  ? 106 LEU   B HD13 1 c 1 
ATOM   1340 H HD21 . LEU   A 1 94  ? 10.373 6.619   -2.978  1 51.075  ? 106 LEU   B HD21 1 c 1 
ATOM   1341 H HD22 . LEU   A 1 94  ? 11.292 7.912   -2.945  1 51.674  ? 106 LEU   B HD22 1 c 1 
ATOM   1342 H HD23 . LEU   A 1 94  ? 9.974  7.854   -2.065  1 50.957  ? 106 LEU   B HD23 1 c 1 
ATOM   1343 N N    . ILE   A 1 95  ? 11.895 4.306   1.256   1 35.806  ? 107 ILE   B N    1 ? 1 
ATOM   1344 C CA   . ILE   A 1 95  ? 11.224 3.333   2.078   1 35.15   ? 107 ILE   B CA   1 ? 1 
ATOM   1345 C C    . ILE   A 1 95  ? 9.95   3.899   2.706   1 34.394  ? 107 ILE   B C    1 ? 1 
ATOM   1346 O O    . ILE   A 1 95  ? 10.058 4.792   3.534   1 35.494  ? 107 ILE   B O    1 ? 1 
ATOM   1347 C CB   . ILE   A 1 95  ? 12.216 2.914   3.176   1 35.313  ? 107 ILE   B CB   1 ? 1 
ATOM   1348 C CG1  . ILE   A 1 95  ? 13.471 2.27    2.585   1 35.051  ? 107 ILE   B CG1  1 ? 1 
ATOM   1349 C CG2  . ILE   A 1 95  ? 11.552 2.009   4.213   1 34.235  ? 107 ILE   B CG2  1 ? 1 
ATOM   1350 C CD1  . ILE   A 1 95  ? 14.642 2.191   3.554   1 33.758  ? 107 ILE   B CD1  1 ? 1 
ATOM   1351 H H    . ILE   A 1 95  ? 12.067 5.13    1.612   1 36.38   ? 107 ILE   B H    1 c 1 
ATOM   1352 H HA   . ILE   A 1 95  ? 11     2.553   1.538   1 35.352  ? 107 ILE   B HA   1 c 1 
ATOM   1353 H HB   . ILE   A 1 95  ? 12.5   3.728   3.637   1 34.963  ? 107 ILE   B HB   1 c 1 
ATOM   1354 H HG12 . ILE   A 1 95  ? 13.248 1.365   2.287   1 34.867  ? 107 ILE   B HG12 1 c 1 
ATOM   1355 H HG13 . ILE   A 1 95  ? 13.751 2.782   1.8     1 35.577  ? 107 ILE   B HG13 1 c 1 
ATOM   1356 H HG21 . ILE   A 1 95  ? 12.223 1.675   4.832   1 33.864  ? 107 ILE   B HG21 1 c 1 
ATOM   1357 H HG22 . ILE   A 1 95  ? 11.127 1.258   3.765   1 34.67   ? 107 ILE   B HG22 1 c 1 
ATOM   1358 H HG23 . ILE   A 1 95  ? 10.883 2.511   4.707   1 34.782  ? 107 ILE   B HG23 1 c 1 
ATOM   1359 H HD11 . ILE   A 1 95  ? 14.806 3.075   3.933   1 34.206  ? 107 ILE   B HD11 1 c 1 
ATOM   1360 H HD12 . ILE   A 1 95  ? 15.44  1.889   3.08    1 34.149  ? 107 ILE   B HD12 1 c 1 
ATOM   1361 H HD13 . ILE   A 1 95  ? 14.436 1.564   4.273   1 33.496  ? 107 ILE   B HD13 1 c 1 
ATOM   1362 N N    . LYS   A 1 96  ? 8.782  3.301   2.414   1 32.959  ? 108 LYS   B N    1 ? 1 
ATOM   1363 C CA   . LYS   A 1 96  ? 7.525  3.65    3.068   1 36.905  ? 108 LYS   B CA   1 ? 1 
ATOM   1364 C C    . LYS   A 1 96  ? 7.441  3.061   4.487   1 38.459  ? 108 LYS   B C    1 ? 1 
ATOM   1365 O O    . LYS   A 1 96  ? 8.121  2.071   4.802   1 35.338  ? 108 LYS   B O    1 ? 1 
ATOM   1366 C CB   . LYS   A 1 96  ? 6.347  3.126   2.25    1 41.396  ? 108 LYS   B CB   1 ? 1 
ATOM   1367 C CG   . LYS   A 1 96  ? 6.211  3.694   0.838   1 47.531  ? 108 LYS   B CG   1 ? 1 
ATOM   1368 C CD   . LYS   A 1 96  ? 5.005  3.1     0.11    1 48.444  ? 108 LYS   B CD   1 ? 1 
ATOM   1369 C CE   . LYS   A 1 96  ? 4.586  3.851   -1.119  1 49.87   ? 108 LYS   B CE   1 ? 1 
ATOM   1370 N NZ   . LYS   A 1 96  ? 5.432  3.478   -2.25   1 51.049  ? 108 LYS   B NZ   1 ? 1 
ATOM   1371 H H    . LYS   A 1 96  ? 8.772  2.646   1.776   1 34.52   ? 108 LYS   B H    1 c 1 
ATOM   1372 H HA   . LYS   A 1 96  ? 7.467  4.638   3.125   1 37.595  ? 108 LYS   B HA   1 c 1 
ATOM   1373 H HB2  . LYS   A 1 96  ? 6.432  2.152   2.179   1 41.49   ? 108 LYS   B HB2  1 c 1 
ATOM   1374 H HB3  . LYS   A 1 96  ? 5.517  3.312   2.734   1 42.686  ? 108 LYS   B HB3  1 c 1 
ATOM   1375 H HG2  . LYS   A 1 96  ? 6.111  4.669   0.894   1 46.515  ? 108 LYS   B HG2  1 c 1 
ATOM   1376 H HG3  . LYS   A 1 96  ? 7.028  3.493   0.333   1 45.33   ? 108 LYS   B HG3  1 c 1 
ATOM   1377 H HD2  . LYS   A 1 96  ? 5.213  2.175   -0.141  1 48.314  ? 108 LYS   B HD2  1 c 1 
ATOM   1378 H HD3  . LYS   A 1 96  ? 4.247  3.07    0.734   1 49.159  ? 108 LYS   B HD3  1 c 1 
ATOM   1379 H HE2  . LYS   A 1 96  ? 3.658  3.645   -1.332  1 52.38   ? 108 LYS   B HE2  1 c 1 
ATOM   1380 H HE3  . LYS   A 1 96  ? 4.662  4.809   -0.964  1 50.352  ? 108 LYS   B HE3  1 c 1 
ATOM   1381 H HZ1  . LYS   A 1 96  ? 5.262  2.621   -2.474  1 51.087  ? 108 LYS   B HZ1  1 c 1 
ATOM   1382 H HZ2  . LYS   A 1 96  ? 6.306  3.564   -2.028  1 48.983  ? 108 LYS   B HZ2  1 c 1 
ATOM   1383 H HZ3  . LYS   A 1 96  ? 5.25   4.013   -2.958  1 52.383  ? 108 LYS   B HZ3  1 c 1 
ATOM   1384 N N    . PRO   A 1 97  ? 6.564  3.617   5.375   1 37.635  ? 109 PRO   B N    1 ? 1 
ATOM   1385 C CA   . PRO   A 1 97  ? 6.565  3.28    6.796   1 37.584  ? 109 PRO   B CA   1 ? 1 
ATOM   1386 C C    . PRO   A 1 97  ? 6.35   1.814   7.14    1 37.006  ? 109 PRO   B C    1 ? 1 
ATOM   1387 O O    . PRO   A 1 97  ? 6.805  1.37    8.179   1 38.85   ? 109 PRO   B O    1 ? 1 
ATOM   1388 C CB   . PRO   A 1 97  ? 5.529  4.191   7.411   1 38.938  ? 109 PRO   B CB   1 ? 1 
ATOM   1389 C CG   . PRO   A 1 97  ? 4.683  4.628   6.243   1 39.894  ? 109 PRO   B CG   1 ? 1 
ATOM   1390 C CD   . PRO   A 1 97  ? 5.594  4.667   5.073   1 38.738  ? 109 PRO   B CD   1 ? 1 
ATOM   1391 H HA   . PRO   A 1 97  ? 7.434  3.546   7.163   1 36.375  ? 109 PRO   B HA   1 c 1 
ATOM   1392 H HB2  . PRO   A 1 97  ? 4.991  3.714   8.072   1 39.815  ? 109 PRO   B HB2  1 c 1 
ATOM   1393 H HB3  . PRO   A 1 97  ? 5.952  4.96    7.841   1 38.786  ? 109 PRO   B HB3  1 c 1 
ATOM   1394 H HG2  . PRO   A 1 97  ? 3.956  3.993   6.087   1 41.081  ? 109 PRO   B HG2  1 c 1 
ATOM   1395 H HG3  . PRO   A 1 97  ? 4.298  5.512   6.406   1 41.075  ? 109 PRO   B HG3  1 c 1 
ATOM   1396 H HD2  . PRO   A 1 97  ? 5.114  4.476   4.249   1 39.862  ? 109 PRO   B HD2  1 c 1 
ATOM   1397 H HD3  . PRO   A 1 97  ? 6.037  5.535   4.995   1 38.693  ? 109 PRO   B HD3  1 c 1 
ATOM   1398 N N    . GLU   A 1 98  ? 5.708  1.047   6.265   1 40.826  ? 110 GLU   B N    1 ? 1 
ATOM   1399 C CA   . GLU   A 1 98  ? 5.395  -0.355  6.568   1 42.674  ? 110 GLU   B CA   1 ? 1 
ATOM   1400 C C    . GLU   A 1 98  ? 6.67   -1.207  6.59    1 37.987  ? 110 GLU   B C    1 ? 1 
ATOM   1401 O O    . GLU   A 1 98  ? 6.672  -2.267  7.176   1 37.624  ? 110 GLU   B O    1 ? 1 
ATOM   1402 C CB   . GLU   A 1 98  ? 4.411  -0.921  5.541   1 48.426  ? 110 GLU   B CB   1 ? 1 
ATOM   1403 C CG   . GLU   A 1 98  ? 3.031  -0.264  5.6     1 56.992  ? 110 GLU   B CG   1 ? 1 
ATOM   1404 C CD   . GLU   A 1 98  ? 2.844  1.15    5.034   1 63.071  ? 110 GLU   B CD   1 ? 1 
ATOM   1405 O OE1  . GLU   A 1 98  ? 3.673  1.668   4.248   1 55.63   ? 110 GLU   B OE1  1 ? 1 
ATOM   1406 O OE2  . GLU   A 1 98  ? 1.801  1.754   5.389   1 74.394  ? 110 GLU   B OE2  1 ? 1 
ATOM   1407 H H    . GLU   A 1 98  ? 5.459  1.39    5.456   1 40.898  ? 110 GLU   B H    1 c 1 
ATOM   1408 H HA   . GLU   A 1 98  ? 4.974  -0.393  7.465   1 43.351  ? 110 GLU   B HA   1 c 1 
ATOM   1409 H HB2  . GLU   A 1 98  ? 4.786  -0.798  4.644   1 48.249  ? 110 GLU   B HB2  1 c 1 
ATOM   1410 H HB3  . GLU   A 1 98  ? 4.313  -1.884  5.695   1 49.275  ? 110 GLU   B HB3  1 c 1 
ATOM   1411 H HG2  . GLU   A 1 98  ? 2.398  -0.852  5.135   1 58.436  ? 110 GLU   B HG2  1 c 1 
ATOM   1412 H HG3  . GLU   A 1 98  ? 2.746  -0.245  6.538   1 57.269  ? 110 GLU   B HG3  1 c 1 
ATOM   1413 N N    . TYR   A 1 99  ? 7.758  -0.742  5.948   1 37.245  ? 111 TYR   B N    1 ? 1 
ATOM   1414 C CA   . TYR   A 1 99  ? 9.045  -1.422  5.941   1 35.588  ? 111 TYR   B CA   1 ? 1 
ATOM   1415 C C    . TYR   A 1 99  ? 10.095 -0.699  6.799   1 33.859  ? 111 TYR   B C    1 ? 1 
ATOM   1416 O O    . TYR   A 1 99  ? 11.283 -1.043  6.771   1 31.501  ? 111 TYR   B O    1 ? 1 
ATOM   1417 C CB   . TYR   A 1 99  ? 9.489  -1.557  4.485   1 37.91   ? 111 TYR   B CB   1 ? 1 
ATOM   1418 C CG   . TYR   A 1 99  ? 8.585  -2.472  3.683   1 37.287  ? 111 TYR   B CG   1 ? 1 
ATOM   1419 C CD1  . TYR   A 1 99  ? 7.438  -1.971  3.074   1 35.381  ? 111 TYR   B CD1  1 ? 1 
ATOM   1420 C CD2  . TYR   A 1 99  ? 8.844  -3.845  3.597   1 37.638  ? 111 TYR   B CD2  1 ? 1 
ATOM   1421 C CE1  . TYR   A 1 99  ? 6.613  -2.801  2.331   1 38.241  ? 111 TYR   B CE1  1 ? 1 
ATOM   1422 C CE2  . TYR   A 1 99  ? 8.016  -4.689  2.853   1 38.454  ? 111 TYR   B CE2  1 ? 1 
ATOM   1423 C CZ   . TYR   A 1 99  ? 6.892  -4.16   2.236   1 38.922  ? 111 TYR   B CZ   1 ? 1 
ATOM   1424 O OH   . TYR   A 1 99  ? 6.018  -4.936  1.547   1 45.212  ? 111 TYR   B OH   1 ? 1 
ATOM   1425 H H    . TYR   A 1 99  ? 7.684  0.036   5.474   1 36.983  ? 111 TYR   B H    1 c 1 
ATOM   1426 H HA   . TYR   A 1 99  ? 8.918  -2.336  6.311   1 36.387  ? 111 TYR   B HA   1 c 1 
ATOM   1427 H HB2  . TYR   A 1 99  ? 9.495  -0.666  4.072   1 36.742  ? 111 TYR   B HB2  1 c 1 
ATOM   1428 H HB3  . TYR   A 1 99  ? 10.404 -1.915  4.466   1 36.027  ? 111 TYR   B HB3  1 c 1 
ATOM   1429 H HD1  . TYR   A 1 99  ? 7.246  -1.048  3.125   1 36.323  ? 111 TYR   B HD1  1 c 1 
ATOM   1430 H HD2  . TYR   A 1 99  ? 9.615  -4.2    4.01    1 36.495  ? 111 TYR   B HD2  1 c 1 
ATOM   1431 H HE1  . TYR   A 1 99  ? 5.841  -2.451  1.921   1 39.622  ? 111 TYR   B HE1  1 c 1 
ATOM   1432 H HE2  . TYR   A 1 99  ? 8.199  -5.611  2.798   1 38.944  ? 111 TYR   B HE2  1 c 1 
ATOM   1433 H HH   . TYR   A 1 99  ? 5.362  -4.439  1.281   0 30      ? 111 TYR   B HH   1 c 1 
ATOM   1434 N N    . ALA   A 1 100 ? 9.644  0.282   7.58    1 33.345  ? 112 ALA   B N    1 ? 1 
ATOM   1435 C CA   . ALA   A 1 100 ? 10.503 1.025   8.47    1 32.49   ? 112 ALA   B CA   1 ? 1 
ATOM   1436 C C    . ALA   A 1 100 ? 9.892  1.023   9.879   1 32.749  ? 112 ALA   B C    1 ? 1 
ATOM   1437 O O    . ALA   A 1 100 ? 9.976  0.004   10.536  1 33.366  ? 112 ALA   B O    1 ? 1 
ATOM   1438 C CB   . ALA   A 1 100 ? 10.784 2.362   7.88    1 30.8    ? 112 ALA   B CB   1 ? 1 
ATOM   1439 H H    . ALA   A 1 100 ? 8.757  0.496   7.559   1 34.31   ? 112 ALA   B H    1 c 1 
ATOM   1440 H HA   . ALA   A 1 100 ? 11.367 0.534   8.53    1 31.59   ? 112 ALA   B HA   1 c 1 
ATOM   1441 H HB1  . ALA   A 1 100 ? 11.329 2.26    7.082   1 30.706  ? 112 ALA   B HB1  1 c 1 
ATOM   1442 H HB2  . ALA   A 1 100 ? 9.948  2.798   7.644   1 31.897  ? 112 ALA   B HB2  1 c 1 
ATOM   1443 H HB3  . ALA   A 1 100 ? 11.261 2.911   8.526   1 31.462  ? 112 ALA   B HB3  1 c 1 
ATOM   1444 N N    . TYR   A 1 101 ? 9.315  2.115   10.373  1 32.942  ? 113 TYR   B N    1 ? 1 
ATOM   1445 C CA   . TYR   A 1 101 ? 8.924  2.206   11.79   1 36.146  ? 113 TYR   B CA   1 ? 1 
ATOM   1446 C C    . TYR   A 1 101 ? 7.399  2.285   11.956  1 37.695  ? 113 TYR   B C    1 ? 1 
ATOM   1447 O O    . TYR   A 1 101 ? 6.896  2.512   13.05   1 41.6    ? 113 TYR   B O    1 ? 1 
ATOM   1448 C CB   . TYR   A 1 101 ? 9.647  3.423   12.407  1 36.628  ? 113 TYR   B CB   1 ? 1 
ATOM   1449 C CG   . TYR   A 1 101 ? 11.151 3.224   12.468  1 33.544  ? 113 TYR   B CG   1 ? 1 
ATOM   1450 C CD1  . TYR   A 1 101 ? 11.722 2.447   13.457  1 34.273  ? 113 TYR   B CD1  1 ? 1 
ATOM   1451 C CD2  . TYR   A 1 101 ? 11.989 3.719   11.482  1 33.589  ? 113 TYR   B CD2  1 ? 1 
ATOM   1452 C CE1  . TYR   A 1 101 ? 13.085 2.187   13.488  1 34.519  ? 113 TYR   B CE1  1 ? 1 
ATOM   1453 C CE2  . TYR   A 1 101 ? 13.359 3.473   11.495  1 35.571  ? 113 TYR   B CE2  1 ? 1 
ATOM   1454 C CZ   . TYR   A 1 101 ? 13.916 2.689   12.499  1 34.506  ? 113 TYR   B CZ   1 ? 1 
ATOM   1455 O OH   . TYR   A 1 101 ? 15.266 2.447   12.537  1 31.262  ? 113 TYR   B OH   1 ? 1 
ATOM   1456 H H    . TYR   A 1 101 ? 9.16   2.831   9.827   1 33.368  ? 113 TYR   B H    1 c 1 
ATOM   1457 H HA   . TYR   A 1 101 ? 9.244  1.39    12.257  1 35.92   ? 113 TYR   B HA   1 c 1 
ATOM   1458 H HB2  . TYR   A 1 101 ? 9.448  4.219   11.867  1 36.089  ? 113 TYR   B HB2  1 c 1 
ATOM   1459 H HB3  . TYR   A 1 101 ? 9.303  3.569   13.316  1 37.637  ? 113 TYR   B HB3  1 c 1 
ATOM   1460 H HD1  . TYR   A 1 101 ? 11.17  2.075   14.126  1 35.59   ? 113 TYR   B HD1  1 c 1 
ATOM   1461 H HD2  . TYR   A 1 101 ? 11.622 4.23    10.778  1 33.503  ? 113 TYR   B HD2  1 c 1 
ATOM   1462 H HE1  . TYR   A 1 101 ? 13.448 1.664   14.181  1 35.515  ? 113 TYR   B HE1  1 c 1 
ATOM   1463 H HE2  . TYR   A 1 101 ? 13.909 3.828   10.819  1 33.995  ? 113 TYR   B HE2  1 c 1 
ATOM   1464 H HH   . TYR   A 1 101 ? 15.499 1.966   13.211  0 30      ? 113 TYR   B HH   1 c 1 
ATOM   1465 N N    . GLY   A 1 102 ? 6.657  2.191   10.853  1 37.88   ? 114 GLY   B N    1 ? 1 
ATOM   1466 C CA   . GLY   A 1 102 ? 5.231  1.934   10.898  1 39.414  ? 114 GLY   B CA   1 ? 1 
ATOM   1467 C C    . GLY   A 1 102 ? 4.473  3.132   11.429  1 40.923  ? 114 GLY   B C    1 ? 1 
ATOM   1468 O O    . GLY   A 1 102 ? 4.993  4.25    11.474  1 38.665  ? 114 GLY   B O    1 ? 1 
ATOM   1469 H H    . GLY   A 1 102 ? 7.052  2.299   10.036  1 36.498  ? 114 GLY   B H    1 c 1 
ATOM   1470 H HA2  . GLY   A 1 102 ? 4.912  1.716   9.992   1 39.275  ? 114 GLY   B HA2  1 c 1 
ATOM   1471 H HA3  . GLY   A 1 102 ? 5.063  1.153   11.476  1 40.253  ? 114 GLY   B HA3  1 c 1 
ATOM   1472 N N    . SER   A 1 103 ? 3.252  2.862   11.893  1 43.898  ? 115 SER   B N    1 ? 1 
ATOM   1473 C CA   . SER   A 1 103 ? 2.396  3.921   12.391  1 45.814  ? 115 SER   B CA   1 ? 1 
ATOM   1474 C C    . SER   A 1 103 ? 2.83   4.339   13.791  1 46.796  ? 115 SER   B C    1 ? 1 
ATOM   1475 O O    . SER   A 1 103 ? 2.571  5.469   14.207  1 45.786  ? 115 SER   B O    1 ? 1 
ATOM   1476 C CB   . SER   A 1 103 ? 0.929  3.543   12.327  1 48.245  ? 115 SER   B CB   1 ? 1 
ATOM   1477 O OG   . SER   A 1 103 ? 0.549  2.736   13.426  1 52.583  ? 115 SER   B OG   1 ? 1 
ATOM   1478 H H    . SER   A 1 103 ? 2.945  2.001   11.898  1 44.236  ? 115 SER   B H    1 c 1 
ATOM   1479 H HA   . SER   A 1 103 ? 2.525  4.703   11.807  1 45.193  ? 115 SER   B HA   1 c 1 
ATOM   1480 H HB2  . SER   A 1 103 ? 0.388  4.355   12.32   1 50.32   ? 115 SER   B HB2  1 c 1 
ATOM   1481 H HB3  . SER   A 1 103 ? 0.758  3.058   11.497  1 48.421  ? 115 SER   B HB3  1 c 1 
ATOM   1482 H HG   . SER   A 1 103 ? -0.238 2.517   13.368  0 30      ? 115 SER   B HG   1 c 1 
ATOM   1483 N N    . ALA   A 1 104 ? 3.541  3.453   14.513  1 47.211  ? 116 ALA   B N    1 ? 1 
ATOM   1484 C CA   . ALA   A 1 104 ? 3.971  3.812   15.858  1 50.409  ? 116 ALA   B CA   1 ? 1 
ATOM   1485 C C    . ALA   A 1 104 ? 5.182  4.756   15.793  1 47.822  ? 116 ALA   B C    1 ? 1 
ATOM   1486 O O    . ALA   A 1 104 ? 5.418  5.547   16.695  1 52.222  ? 116 ALA   B O    1 ? 1 
ATOM   1487 C CB   . ALA   A 1 104 ? 4.246  2.568   16.664  1 48.797  ? 116 ALA   B CB   1 ? 1 
ATOM   1488 H H    . ALA   A 1 104 ? 3.748  2.629   14.176  1 46.297  ? 116 ALA   B H    1 c 1 
ATOM   1489 H HA   . ALA   A 1 104 ? 3.224  4.308   16.294  1 51.766  ? 116 ALA   B HA   1 c 1 
ATOM   1490 H HB1  . ALA   A 1 104 ? 3.432  2.042   16.742  1 51.029  ? 116 ALA   B HB1  1 c 1 
ATOM   1491 H HB2  . ALA   A 1 104 ? 4.93   2.036   16.223  1 47.478  ? 116 ALA   B HB2  1 c 1 
ATOM   1492 H HB3  . ALA   A 1 104 ? 4.555  2.815   17.552  1 50.837  ? 116 ALA   B HB3  1 c 1 
ATOM   1493 N N    . GLY   A 1 105 ? 5.968  4.68    14.723  1 45.998  ? 117 GLY   B N    1 ? 1 
ATOM   1494 C CA   . GLY   A 1 105 ? 7.207  5.447   14.659  1 44.706  ? 117 GLY   B CA   1 ? 1 
ATOM   1495 C C    . GLY   A 1 105 ? 8.17   4.972   15.749  1 46.624  ? 117 GLY   B C    1 ? 1 
ATOM   1496 O O    . GLY   A 1 105 ? 8.016  3.865   16.276  1 45.71   ? 117 GLY   B O    1 ? 1 
ATOM   1497 H H    . GLY   A 1 105 ? 5.742  4.14    14.021  1 44.674  ? 117 GLY   B H    1 c 1 
ATOM   1498 H HA2  . GLY   A 1 105 ? 7.621  5.327   13.774  1 43.221  ? 117 GLY   B HA2  1 c 1 
ATOM   1499 H HA3  . GLY   A 1 105 ? 7.008  6.405   14.78   1 46.061  ? 117 GLY   B HA3  1 c 1 
ATOM   1500 N N    . SER   A 1 106 ? 9.183  5.79    16.043  1 45.399  ? 118 SER   B N    1 ? 1 
ATOM   1501 C CA   . SER   A 1 106 ? 10.121 5.504   17.112  1 47.833  ? 118 SER   B CA   1 ? 1 
ATOM   1502 C C    . SER   A 1 106 ? 10.442 6.824   17.81   1 51.895  ? 118 SER   B C    1 ? 1 
ATOM   1503 O O    . SER   A 1 106 ? 11.502 7.411   17.619  1 48.581  ? 118 SER   B O    1 ? 1 
ATOM   1504 C CB   . SER   A 1 106 ? 11.344 4.797   16.59   1 45.612  ? 118 SER   B CB   1 ? 1 
ATOM   1505 O OG   . SER   A 1 106 ? 12.069 4.197   17.656  1 48.769  ? 118 SER   B OG   1 ? 1 
ATOM   1506 H H    . SER   A 1 106 ? 9.29   6.558   15.558  1 45.587  ? 118 SER   B H    1 c 1 
ATOM   1507 H HA   . SER   A 1 106 ? 9.675  4.91    17.768  1 49.2    ? 118 SER   B HA   1 c 1 
ATOM   1508 H HB2  . SER   A 1 106 ? 11.072 4.108   15.954  1 44.415  ? 118 SER   B HB2  1 c 1 
ATOM   1509 H HB3  . SER   A 1 106 ? 11.916 5.435   16.123  1 45.336  ? 118 SER   B HB3  1 c 1 
ATOM   1510 H HG   . SER   A 1 106 ? 12.689 3.772   17.393  0 30      ? 118 SER   B HG   1 c 1 
ATOM   1511 N N    . LEU   A 1 107 ? 9.455  7.274   18.581  1 54.799  ? 119 LEU   B N    1 ? 1 
ATOM   1512 C CA   . LEU   A 1 107 ? 9.353  8.64    19.036  1 62.625  ? 119 LEU   B CA   1 ? 1 
ATOM   1513 C C    . LEU   A 1 107 ? 10.447 8.962   20.054  1 69.148  ? 119 LEU   B C    1 ? 1 
ATOM   1514 O O    . LEU   A 1 107 ? 10.757 8.15    20.949  1 65.484  ? 119 LEU   B O    1 ? 1 
ATOM   1515 C CB   . LEU   A 1 107 ? 7.966  8.844   19.655  1 67.576  ? 119 LEU   B CB   1 ? 1 
ATOM   1516 C CG   . LEU   A 1 107 ? 6.742  8.785   18.723  1 67.763  ? 119 LEU   B CG   1 ? 1 
ATOM   1517 C CD1  . LEU   A 1 107 ? 5.503  9.1     19.564  1 69.445  ? 119 LEU   B CD1  1 ? 1 
ATOM   1518 C CD2  . LEU   A 1 107 ? 6.795  9.711   17.506  1 62.205  ? 119 LEU   B CD2  1 ? 1 
ATOM   1519 H H    . LEU   A 1 107 ? 8.806  6.685   18.84   1 56.44   ? 119 LEU   B H    1 c 1 
ATOM   1520 H HA   . LEU   A 1 107 ? 9.452  9.228   18.251  1 61.276  ? 119 LEU   B HA   1 c 1 
ATOM   1521 H HB2  . LEU   A 1 107 ? 7.846  8.165   20.359  1 68.597  ? 119 LEU   B HB2  1 c 1 
ATOM   1522 H HB3  . LEU   A 1 107 ? 7.963  9.719   20.108  1 69.542  ? 119 LEU   B HB3  1 c 1 
ATOM   1523 H HG   . LEU   A 1 107 ? 6.654  7.854   18.391  1 64.8    ? 119 LEU   B HG   1 c 1 
ATOM   1524 H HD11 . LEU   A 1 107 ? 5.396  8.421   20.252  1 71.298  ? 119 LEU   B HD11 1 c 1 
ATOM   1525 H HD12 . LEU   A 1 107 ? 4.716  9.108   18.993  1 69.649  ? 119 LEU   B HD12 1 c 1 
ATOM   1526 H HD13 . LEU   A 1 107 ? 5.607  9.97    19.984  1 71.941  ? 119 LEU   B HD13 1 c 1 
ATOM   1527 H HD21 . LEU   A 1 107 ? 7.561  9.48    16.954  1 61.029  ? 119 LEU   B HD21 1 c 1 
ATOM   1528 H HD22 . LEU   A 1 107 ? 6.878  10.633  17.802  1 64.913  ? 119 LEU   B HD22 1 c 1 
ATOM   1529 H HD23 . LEU   A 1 107 ? 5.981  9.612   16.985  1 62.894  ? 119 LEU   B HD23 1 c 1 
ATOM   1530 N N    . PRO   A 1 108 ? 10.98  10.209  20.024  1 68.896  ? 120 PRO   B N    1 ? 1 
ATOM   1531 C CA   . PRO   A 1 108 ? 10.641 11.192  19      1 65.112  ? 120 PRO   B CA   1 ? 1 
ATOM   1532 C C    . PRO   A 1 108 ? 11.541 11.178  17.765  1 62.159  ? 120 PRO   B C    1 ? 1 
ATOM   1533 O O    . PRO   A 1 108 ? 11.335 11.965  16.848  1 57.497  ? 120 PRO   B O    1 ? 1 
ATOM   1534 C CB   . PRO   A 1 108 ? 10.741 12.51   19.74   1 70.188  ? 120 PRO   B CB   1 ? 1 
ATOM   1535 C CG   . PRO   A 1 108 ? 11.639 12.248  20.939  1 76.923  ? 120 PRO   B CG   1 ? 1 
ATOM   1536 C CD   . PRO   A 1 108 ? 11.82  10.774  21.092  1 74.592  ? 120 PRO   B CD   1 ? 1 
ATOM   1537 H HA   . PRO   A 1 108 ? 9.712  11.067  18.722  1 65.259  ? 120 PRO   B HA   1 c 1 
ATOM   1538 H HB2  . PRO   A 1 108 ? 11.125 13.202  19.167  1 70.353  ? 120 PRO   B HB2  1 c 1 
ATOM   1539 H HB3  . PRO   A 1 108 ? 9.857  12.809  20.031  1 72.209  ? 120 PRO   B HB3  1 c 1 
ATOM   1540 H HG2  . PRO   A 1 108 ? 12.507 12.676  20.806  1 76.31   ? 120 PRO   B HG2  1 c 1 
ATOM   1541 H HG3  . PRO   A 1 108 ? 11.237 12.62   21.749  1 78.89   ? 120 PRO   B HG3  1 c 1 
ATOM   1542 H HD2  . PRO   A 1 108 ? 12.754 10.513  20.976  1 73.616  ? 120 PRO   B HD2  1 c 1 
ATOM   1543 H HD3  . PRO   A 1 108 ? 11.507 10.476  21.955  1 76.373  ? 120 PRO   B HD3  1 c 1 
ATOM   1544 N N    . LYS   A 1 109 ? 12.521 10.265  17.73   1 62.117  ? 121 LYS   B N    1 ? 1 
ATOM   1545 C CA   . LYS   A 1 109 ? 13.52  10.17   16.662  1 57.965  ? 121 LYS   B CA   1 ? 1 
ATOM   1546 C C    . LYS   A 1 109 ? 12.924 9.95    15.268  1 50.489  ? 121 LYS   B C    1 ? 1 
ATOM   1547 O O    . LYS   A 1 109 ? 13.397 10.499  14.287  1 42.241  ? 121 LYS   B O    1 ? 1 
ATOM   1548 C CB   . LYS   A 1 109 ? 14.445 8.988   17.002  1 62.464  ? 121 LYS   B CB   1 ? 1 
ATOM   1549 C CG   . LYS   A 1 109 ? 15.652 8.743   16.093  1 67.893  ? 121 LYS   B CG   1 ? 1 
ATOM   1550 C CD   . LYS   A 1 109 ? 16.96  8.409   16.823  1 75.912  ? 121 LYS   B CD   1 ? 1 
ATOM   1551 C CE   . LYS   A 1 109 ? 18.114 8.602   15.858  1 79.594  ? 121 LYS   B CE   1 ? 1 
ATOM   1552 N NZ   . LYS   A 1 109 ? 19.444 8.755   16.452  1 76.155  ? 121 LYS   B NZ   1 ? 1 
ATOM   1553 H H    . LYS   A 1 109 ? 12.57  9.66    18.413  1 62.248  ? 121 LYS   B H    1 c 1 
ATOM   1554 H HA   . LYS   A 1 109 ? 14.051 11.006  16.655  1 59.692  ? 121 LYS   B HA   1 c 1 
ATOM   1555 H HB2  . LYS   A 1 109 ? 14.778 9.118   17.916  1 65.169  ? 121 LYS   B HB2  1 c 1 
ATOM   1556 H HB3  . LYS   A 1 109 ? 13.903 8.171   17.005  1 61.48   ? 121 LYS   B HB3  1 c 1 
ATOM   1557 H HG2  . LYS   A 1 109 ? 15.434 8.004   15.484  1 65.213  ? 121 LYS   B HG2  1 c 1 
ATOM   1558 H HG3  . LYS   A 1 109 ? 15.79  9.545   15.545  1 67.519  ? 121 LYS   B HG3  1 c 1 
ATOM   1559 H HD2  . LYS   A 1 109 ? 17.075 9.003   17.596  1 77.951  ? 121 LYS   B HD2  1 c 1 
ATOM   1560 H HD3  . LYS   A 1 109 ? 16.942 7.477   17.131  1 74.954  ? 121 LYS   B HD3  1 c 1 
ATOM   1561 H HE2  . LYS   A 1 109 ? 18.138 7.838   15.254  1 74.458  ? 121 LYS   B HE2  1 c 1 
ATOM   1562 H HE3  . LYS   A 1 109 ? 17.94  9.391   15.314  1 76.665  ? 121 LYS   B HE3  1 c 1 
ATOM   1563 H HZ1  . LYS   A 1 109 ? 19.691 7.979   16.851  1 78.194  ? 121 LYS   B HZ1  1 c 1 
ATOM   1564 H HZ2  . LYS   A 1 109 ? 19.429 9.416   17.071  1 80.329  ? 121 LYS   B HZ2  1 c 1 
ATOM   1565 H HZ3  . LYS   A 1 109 ? 20.045 8.963   15.808  1 77.822  ? 121 LYS   B HZ3  1 c 1 
ATOM   1566 N N    . ILE   A 1 110 ? 11.961 9.035   15.159  1 47.733  ? 122 ILE   B N    1 ? 1 
ATOM   1567 C CA   . ILE   A 1 110 ? 11.31  8.762   13.898  1 43.148  ? 122 ILE   B CA   1 ? 1 
ATOM   1568 C C    . ILE   A 1 110 ? 9.834  9.013   14.154  1 44.466  ? 122 ILE   B C    1 ? 1 
ATOM   1569 O O    . ILE   A 1 110 ? 9.275  8.336   15.026  1 48.784  ? 122 ILE   B O    1 ? 1 
ATOM   1570 C CB   . ILE   A 1 110 ? 11.539 7.306   13.449  1 41.66   ? 122 ILE   B CB   1 ? 1 
ATOM   1571 C CG1  . ILE   A 1 110 ? 12.995 6.831   13.573  1 41.332  ? 122 ILE   B CG1  1 ? 1 
ATOM   1572 C CG2  . ILE   A 1 110 ? 10.982 7.118   12.036  1 41.5    ? 122 ILE   B CG2  1 ? 1 
ATOM   1573 C CD1  . ILE   A 1 110 ? 13.911 7.283   12.444  1 38.924  ? 122 ILE   B CD1  1 ? 1 
ATOM   1574 H H    . ILE   A 1 110 ? 11.706 8.562   15.899  1 48.426  ? 122 ILE   B H    1 c 1 
ATOM   1575 H HA   . ILE   A 1 110 ? 11.64  9.373   13.213  1 43.352  ? 122 ILE   B HA   1 c 1 
ATOM   1576 H HB   . ILE   A 1 110 ? 11.009 6.739   14.042  1 42.373  ? 122 ILE   B HB   1 c 1 
ATOM   1577 H HG12 . ILE   A 1 110 ? 13.361 7.155   14.421  1 42.665  ? 122 ILE   B HG12 1 c 1 
ATOM   1578 H HG13 . ILE   A 1 110 ? 12.999 5.852   13.604  1 40.174  ? 122 ILE   B HG13 1 c 1 
ATOM   1579 H HG21 . ILE   A 1 110 ? 11.238 6.245   11.699  1 39.699  ? 122 ILE   B HG21 1 c 1 
ATOM   1580 H HG22 . ILE   A 1 110 ? 11.338 7.806   11.449  1 40.854  ? 122 ILE   B HG22 1 c 1 
ATOM   1581 H HG23 . ILE   A 1 110 ? 10.012 7.182   12.055  1 41.484  ? 122 ILE   B HG23 1 c 1 
ATOM   1582 H HD11 . ILE   A 1 110 ? 13.656 6.847   11.608  1 37.825  ? 122 ILE   B HD11 1 c 1 
ATOM   1583 H HD12 . ILE   A 1 110 ? 14.829 7.04    12.667  1 39.512  ? 122 ILE   B HD12 1 c 1 
ATOM   1584 H HD13 . ILE   A 1 110 ? 13.849 8.251   12.337  1 40.162  ? 122 ILE   B HD13 1 c 1 
ATOM   1585 N N    . PRO   A 1 111 ? 9.163  9.986   13.491  1 43.708  ? 123 PRO   B N    1 ? 1 
ATOM   1586 C CA   . PRO   A 1 111 ? 7.746  10.22   13.771  1 45.65   ? 123 PRO   B CA   1 ? 1 
ATOM   1587 C C    . PRO   A 1 111 ? 6.871  9.129   13.156  1 46.744  ? 123 PRO   B C    1 ? 1 
ATOM   1588 O O    . PRO   A 1 111 ? 7.369  8.285   12.386  1 47.13   ? 123 PRO   B O    1 ? 1 
ATOM   1589 C CB   . PRO   A 1 111 ? 7.495  11.634  13.207  1 46.731  ? 123 PRO   B CB   1 ? 1 
ATOM   1590 C CG   . PRO   A 1 111 ? 8.559  11.816  12.137  1 42.492  ? 123 PRO   B CG   1 ? 1 
ATOM   1591 C CD   . PRO   A 1 111 ? 9.71   10.902  12.467  1 42.087  ? 123 PRO   B CD   1 ? 1 
ATOM   1592 H HA   . PRO   A 1 111 ? 7.607  10.236  14.741  1 47.706  ? 123 PRO   B HA   1 c 1 
ATOM   1593 H HB2  . PRO   A 1 111 ? 6.6    11.7    12.821  1 46.664  ? 123 PRO   B HB2  1 c 1 
ATOM   1594 H HB3  . PRO   A 1 111 ? 7.587  12.309  13.907  1 48.12   ? 123 PRO   B HB3  1 c 1 
ATOM   1595 H HG2  . PRO   A 1 111 ? 8.197  11.595  11.256  1 42.261  ? 123 PRO   B HG2  1 c 1 
ATOM   1596 H HG3  . PRO   A 1 111 ? 8.864  12.746  12.118  1 44.474  ? 123 PRO   B HG3  1 c 1 
ATOM   1597 H HD2  . PRO   A 1 111 ? 10.001 10.403  11.679  1 40.362  ? 123 PRO   B HD2  1 c 1 
ATOM   1598 H HD3  . PRO   A 1 111 ? 10.468 11.405  12.825  1 42.968  ? 123 PRO   B HD3  1 c 1 
ATOM   1599 N N    . SER   A 1 112 ? 5.584  9.118   13.527  1 49.911  ? 124 SER   B N    1 ? 1 
ATOM   1600 C CA   . SER   A 1 112 ? 4.662  8.116   13.007  1 51.212  ? 124 SER   B CA   1 ? 1 
ATOM   1601 C C    . SER   A 1 112 ? 4.492  8.246   11.49   1 49.261  ? 124 SER   B C    1 ? 1 
ATOM   1602 O O    . SER   A 1 112 ? 4.511  9.336   10.928  1 49.974  ? 124 SER   B O    1 ? 1 
ATOM   1603 C CB   . SER   A 1 112 ? 3.349  8.15    13.708  1 53.377  ? 124 SER   B CB   1 ? 1 
ATOM   1604 O OG   . SER   A 1 112 ? 2.71   9.385   13.498  1 56.308  ? 124 SER   B OG   1 ? 1 
ATOM   1605 H H    . SER   A 1 112 ? 5.274  9.748   14.112  1 51.871  ? 124 SER   B H    1 c 1 
ATOM   1606 H HA   . SER   A 1 112 ? 5.068  7.229   13.185  1 49.5    ? 124 SER   B HA   1 c 1 
ATOM   1607 H HB2  . SER   A 1 112 ? 2.784  7.436   13.366  1 53.717  ? 124 SER   B HB2  1 c 1 
ATOM   1608 H HB3  . SER   A 1 112 ? 3.485  8.008   14.664  1 54.849  ? 124 SER   B HB3  1 c 1 
ATOM   1609 H HG   . SER   A 1 112 ? 2.078  9.405   13.992  0 30      ? 124 SER   B HG   1 c 1 
ATOM   1610 N N    . ASN   A 1 113 ? 4.415  7.084   10.836  1 46.782  ? 125 ASN   B N    1 ? 1 
ATOM   1611 C CA   . ASN   A 1 113 ? 4.169  6.934   9.408   1 46.182  ? 125 ASN   B CA   1 ? 1 
ATOM   1612 C C    . ASN   A 1 113 ? 5.17   7.732   8.574   1 42.108  ? 125 ASN   B C    1 ? 1 
ATOM   1613 O O    . ASN   A 1 113 ? 4.807  8.344   7.579   1 46.405  ? 125 ASN   B O    1 ? 1 
ATOM   1614 C CB   . ASN   A 1 113 ? 2.718  7.251   9.075   1 48.654  ? 125 ASN   B CB   1 ? 1 
ATOM   1615 C CG   . ASN   A 1 113 ? 1.731  6.355   9.791   1 48.469  ? 125 ASN   B CG   1 ? 1 
ATOM   1616 O OD1  . ASN   A 1 113 ? 0.762  6.843   10.372  1 53.925  ? 125 ASN   B OD1  1 ? 1 
ATOM   1617 N ND2  . ASN   A 1 113 ? 1.867  5.045   9.678   1 48.751  ? 125 ASN   B ND2  1 ? 1 
ATOM   1618 H H    . ASN   A 1 113 ? 4.525  6.318   11.323  1 46.829  ? 125 ASN   B H    1 c 1 
ATOM   1619 H HA   . ASN   A 1 113 ? 4.308  5.987   9.19    1 44.626  ? 125 ASN   B HA   1 c 1 
ATOM   1620 H HB2  . ASN   A 1 113 ? 2.533  8.181   9.314   1 49.398  ? 125 ASN   B HB2  1 c 1 
ATOM   1621 H HB3  . ASN   A 1 113 ? 2.585  7.158   8.11    1 48.032  ? 125 ASN   B HB3  1 c 1 
ATOM   1622 H HD21 . ASN   A 1 113 ? 1.149  4.527   9.716   1 49.748  ? 125 ASN   B HD21 1 c 1 
ATOM   1623 H HD22 . ASN   A 1 113 ? 2.665  4.681   9.553   1 46.489  ? 125 ASN   B HD22 1 c 1 
ATOM   1624 N N    . ALA   A 1 114 ? 6.45   7.642   8.936   1 38.083  ? 126 ALA   B N    1 ? 1 
ATOM   1625 C CA   . ALA   A 1 114 ? 7.512  8.327   8.228   1 36.849  ? 126 ALA   B CA   1 ? 1 
ATOM   1626 C C    . ALA   A 1 114 ? 8.065  7.505   7.056   1 35.023  ? 126 ALA   B C    1 ? 1 
ATOM   1627 O O    . ALA   A 1 114 ? 8.24   6.305   7.168   1 37.356  ? 126 ALA   B O    1 ? 1 
ATOM   1628 C CB   . ALA   A 1 114 ? 8.586  8.661   9.216   1 34.587  ? 126 ALA   B CB   1 ? 1 
ATOM   1629 H H    . ALA   A 1 114 ? 6.671  7.12    9.653   1 38.294  ? 126 ALA   B H    1 c 1 
ATOM   1630 H HA   . ALA   A 1 114 ? 7.141  9.177   7.862   1 37.631  ? 126 ALA   B HA   1 c 1 
ATOM   1631 H HB1  . ALA   A 1 114 ? 8.226  9.246   9.904   1 36.599  ? 126 ALA   B HB1  1 c 1 
ATOM   1632 H HB2  . ALA   A 1 114 ? 8.916  7.845   9.628   1 34.423  ? 126 ALA   B HB2  1 c 1 
ATOM   1633 H HB3  . ALA   A 1 114 ? 9.318  9.111   8.763   1 34.981  ? 126 ALA   B HB3  1 c 1 
ATOM   1634 N N    . THR   A 1 115 ? 8.387  8.184   5.952   1 33.911  ? 127 THR   B N    1 ? 1 
ATOM   1635 C CA   . THR   A 1 115 ? 9.175  7.654   4.844   1 32.995  ? 127 THR   B CA   1 ? 1 
ATOM   1636 C C    . THR   A 1 115 ? 10.653 8.013   5.039   1 29.929  ? 127 THR   B C    1 ? 1 
ATOM   1637 O O    . THR   A 1 115 ? 10.986 9.131   5.391   1 31.281  ? 127 THR   B O    1 ? 1 
ATOM   1638 C CB   . THR   A 1 115 ? 8.597  8.267   3.563   1 37.581  ? 127 THR   B CB   1 ? 1 
ATOM   1639 O OG1  . THR   A 1 115 ? 7.243  7.844   3.491   1 39.34   ? 127 THR   B OG1  1 ? 1 
ATOM   1640 C CG2  . THR   A 1 115 ? 9.315  7.862   2.293   1 36.969  ? 127 THR   B CG2  1 ? 1 
ATOM   1641 H H    . THR   A 1 115 ? 8.092  9.047   5.886   1 35.459  ? 127 THR   B H    1 c 1 
ATOM   1642 H HA   . THR   A 1 115 ? 9.072  6.68    4.812   1 32.314  ? 127 THR   B HA   1 c 1 
ATOM   1643 H HB   . THR   A 1 115 ? 8.62   9.251   3.632   1 38.149  ? 127 THR   B HB   1 c 1 
ATOM   1644 H HG1  . THR   A 1 115 ? 7.25   6.976   3.425   0 30      ? 127 THR   B HG1  1 c 1 
ATOM   1645 H HG21 . THR   A 1 115 ? 8.878  8.273   1.529   1 38.444  ? 127 THR   B HG21 1 c 1 
ATOM   1646 H HG22 . THR   A 1 115 ? 9.289  6.896   2.199   1 36.311  ? 127 THR   B HG22 1 c 1 
ATOM   1647 H HG23 . THR   A 1 115 ? 10.24  8.158   2.332   1 36.685  ? 127 THR   B HG23 1 c 1 
ATOM   1648 N N    . LEU   A 1 116 ? 11.555 7.067   4.787   1 29.382  ? 128 LEU   B N    1 ? 1 
ATOM   1649 C CA   . LEU   A 1 116 ? 13.005 7.197   4.965   1 29.282  ? 128 LEU   B CA   1 ? 1 
ATOM   1650 C C    . LEU   A 1 116 ? 13.728 7.007   3.631   1 30.894  ? 128 LEU   B C    1 ? 1 
ATOM   1651 O O    . LEU   A 1 116 ? 13.299 6.211   2.811   1 31.19   ? 128 LEU   B O    1 ? 1 
ATOM   1652 C CB   . LEU   A 1 116 ? 13.566 6.152   5.93    1 29.763  ? 128 LEU   B CB   1 ? 1 
ATOM   1653 C CG   . LEU   A 1 116 ? 13.343 6.403   7.428   1 33.38   ? 128 LEU   B CG   1 ? 1 
ATOM   1654 C CD1  . LEU   A 1 116 ? 11.914 6.673   7.727   1 33.154  ? 128 LEU   B CD1  1 ? 1 
ATOM   1655 C CD2  . LEU   A 1 116 ? 13.856 5.196   8.199   1 33.363  ? 128 LEU   B CD2  1 ? 1 
ATOM   1656 H H    . LEU   A 1 116 ? 11.244 6.267   4.474   1 28.775  ? 128 LEU   B H    1 c 1 
ATOM   1657 H HA   . LEU   A 1 116 ? 13.202 8.103   5.313   1 30.699  ? 128 LEU   B HA   1 c 1 
ATOM   1658 H HB2  . LEU   A 1 116 ? 13.168 5.28    5.701   1 29.421  ? 128 LEU   B HB2  1 c 1 
ATOM   1659 H HB3  . LEU   A 1 116 ? 14.536 6.079   5.773   1 30.086  ? 128 LEU   B HB3  1 c 1 
ATOM   1660 H HG   . LEU   A 1 116 ? 13.876 7.196   7.695   1 33.62   ? 128 LEU   B HG   1 c 1 
ATOM   1661 H HD11 . LEU   A 1 116 ? 11.693 7.582   7.466   1 34.103  ? 128 LEU   B HD11 1 c 1 
ATOM   1662 H HD12 . LEU   A 1 116 ? 11.756 6.566   8.681   1 33.735  ? 128 LEU   B HD12 1 c 1 
ATOM   1663 H HD13 . LEU   A 1 116 ? 11.354 6.049   7.236   1 32.835  ? 128 LEU   B HD13 1 c 1 
ATOM   1664 H HD21 . LEU   A 1 116 ? 14.802 5.071   8.016   1 33.118  ? 128 LEU   B HD21 1 c 1 
ATOM   1665 H HD22 . LEU   A 1 116 ? 13.366 4.402   7.924   1 32.475  ? 128 LEU   B HD22 1 c 1 
ATOM   1666 H HD23 . LEU   A 1 116 ? 13.727 5.341   9.151   1 33.791  ? 128 LEU   B HD23 1 c 1 
ATOM   1667 N N    . PHE   A 1 117 ? 14.887 7.67    3.527   1 33.47   ? 129 PHE   B N    1 ? 1 
ATOM   1668 C CA   . PHE   A 1 117 ? 15.815 7.607   2.421   1 35.518  ? 129 PHE   B CA   1 ? 1 
ATOM   1669 C C    . PHE   A 1 117 ? 17.19  7.225   2.973   1 36.919  ? 129 PHE   B C    1 ? 1 
ATOM   1670 O O    . PHE   A 1 117 ? 17.644 7.763   3.984   1 38.949  ? 129 PHE   B O    1 ? 1 
ATOM   1671 C CB   . PHE   A 1 117 ? 15.939 8.943   1.683   1 41.626  ? 129 PHE   B CB   1 ? 1 
ATOM   1672 C CG   . PHE   A 1 117 ? 16.878 8.9     0.478   1 45.702  ? 129 PHE   B CG   1 ? 1 
ATOM   1673 C CD1  . PHE   A 1 117 ? 16.406 8.572   -0.793  1 48.807  ? 129 PHE   B CD1  1 ? 1 
ATOM   1674 C CD2  . PHE   A 1 117 ? 18.233 9.172   0.612   1 46.425  ? 129 PHE   B CD2  1 ? 1 
ATOM   1675 C CE1  . PHE   A 1 117 ? 17.262 8.517   -1.889  1 48.721  ? 129 PHE   B CE1  1 ? 1 
ATOM   1676 C CE2  . PHE   A 1 117 ? 19.08  9.115   -0.489  1 49.415  ? 129 PHE   B CE2  1 ? 1 
ATOM   1677 C CZ   . PHE   A 1 117 ? 18.601 8.761   -1.732  1 47.157  ? 129 PHE   B CZ   1 ? 1 
ATOM   1678 H H    . PHE   A 1 117 ? 15.114 8.215   4.225   1 33.757  ? 129 PHE   B H    1 c 1 
ATOM   1679 H HA   . PHE   A 1 117 ? 15.512 6.911   1.783   1 35.718  ? 129 PHE   B HA   1 c 1 
ATOM   1680 H HB2  . PHE   A 1 117 ? 15.045 9.217   1.381   1 41.474  ? 129 PHE   B HB2  1 c 1 
ATOM   1681 H HB3  . PHE   A 1 117 ? 16.266 9.62    2.317   1 41.857  ? 129 PHE   B HB3  1 c 1 
ATOM   1682 H HD1  . PHE   A 1 117 ? 15.489 8.377   -0.91   1 47.228  ? 129 PHE   B HD1  1 c 1 
ATOM   1683 H HD2  . PHE   A 1 117 ? 18.582 9.391   1.461   1 46.717  ? 129 PHE   B HD2  1 c 1 
ATOM   1684 H HE1  . PHE   A 1 117 ? 16.922 8.286   -2.739  1 49.256  ? 129 PHE   B HE1  1 c 1 
ATOM   1685 H HE2  . PHE   A 1 117 ? 19.999 9.293   -0.378  1 49.613  ? 129 PHE   B HE2  1 c 1 
ATOM   1686 H HZ   . PHE   A 1 117 ? 19.177 8.746   -2.477  1 49.974  ? 129 PHE   B HZ   1 c 1 
ATOM   1687 N N    . PHE   A 1 118 ? 17.846 6.287   2.284   1 34.724  ? 130 PHE   B N    1 ? 1 
ATOM   1688 C CA   . PHE   A 1 118 ? 19.196 5.881   2.597   1 36.333  ? 130 PHE   B CA   1 ? 1 
ATOM   1689 C C    . PHE   A 1 118 ? 20.019 5.798   1.316   1 39.26   ? 130 PHE   B C    1 ? 1 
ATOM   1690 O O    . PHE   A 1 118 ? 19.544 5.412   0.234   1 36.366  ? 130 PHE   B O    1 ? 1 
ATOM   1691 C CB   . PHE   A 1 118 ? 19.336 4.54    3.322   1 34.258  ? 130 PHE   B CB   1 ? 1 
ATOM   1692 C CG   . PHE   A 1 118 ? 18.724 4.482   4.71    1 33.356  ? 130 PHE   B CG   1 ? 1 
ATOM   1693 C CD1  . PHE   A 1 118 ? 17.369 4.178   4.872   1 34.98   ? 130 PHE   B CD1  1 ? 1 
ATOM   1694 C CD2  . PHE   A 1 118 ? 19.499 4.685   5.836   1 33.666  ? 130 PHE   B CD2  1 ? 1 
ATOM   1695 C CE1  . PHE   A 1 118 ? 16.809 4.121   6.142   1 33.521  ? 130 PHE   B CE1  1 ? 1 
ATOM   1696 C CE2  . PHE   A 1 118 ? 18.944 4.621   7.1     1 36.672  ? 130 PHE   B CE2  1 ? 1 
ATOM   1697 C CZ   . PHE   A 1 118 ? 17.603 4.327   7.256   1 34.424  ? 130 PHE   B CZ   1 ? 1 
ATOM   1698 H H    . PHE   A 1 118 ? 17.424 5.88    1.583   1 35.23   ? 130 PHE   B H    1 c 1 
ATOM   1699 H HA   . PHE   A 1 118 ? 19.594 6.581   3.174   1 37.175  ? 130 PHE   B HA   1 c 1 
ATOM   1700 H HB2  . PHE   A 1 118 ? 18.919 3.844   2.767   1 33.752  ? 130 PHE   B HB2  1 c 1 
ATOM   1701 H HB3  . PHE   A 1 118 ? 20.293 4.326   3.393   1 35.24   ? 130 PHE   B HB3  1 c 1 
ATOM   1702 H HD1  . PHE   A 1 118 ? 16.83  4.034   4.112   1 33.763  ? 130 PHE   B HD1  1 c 1 
ATOM   1703 H HD2  . PHE   A 1 118 ? 20.417 4.881   5.738   1 35.758  ? 130 PHE   B HD2  1 c 1 
ATOM   1704 H HE1  . PHE   A 1 118 ? 15.892 3.919   6.244   1 33.203  ? 130 PHE   B HE1  1 c 1 
ATOM   1705 H HE2  . PHE   A 1 118 ? 19.486 4.768   7.859   1 36.596  ? 130 PHE   B HE2  1 c 1 
ATOM   1706 H HZ   . PHE   A 1 118 ? 17.225 4.285   8.119   1 34.646  ? 130 PHE   B HZ   1 c 1 
ATOM   1707 N N    . GLU   A 1 119 ? 21.278 6.204   1.501   1 42.333  ? 131 GLU   B N    1 ? 1 
ATOM   1708 C CA   . GLU   A 1 119 ? 22.383 5.848   0.636   1 46.145  ? 131 GLU   B CA   1 ? 1 
ATOM   1709 C C    . GLU   A 1 119 ? 23.217 4.842   1.426   1 46.438  ? 131 GLU   B C    1 ? 1 
ATOM   1710 O O    . GLU   A 1 119 ? 23.618 5.114   2.558   1 48.529  ? 131 GLU   B O    1 ? 1 
ATOM   1711 C CB   . GLU   A 1 119 ? 23.145 7.114   0.261   1 50.006  ? 131 GLU   B CB   1 ? 1 
ATOM   1712 C CG   . GLU   A 1 119 ? 24.317 6.853   -0.675  1 55.669  ? 131 GLU   B CG   1 ? 1 
ATOM   1713 C CD   . GLU   A 1 119 ? 25.078 8.107   -1.084  1 58.872  ? 131 GLU   B CD   1 ? 1 
ATOM   1714 O OE1  . GLU   A 1 119 ? 24.953 8.686   -2.211  1 56.647  ? 131 GLU   B OE1  1 ? 1 
ATOM   1715 O OE2  . GLU   A 1 119 ? 25.871 8.465   -0.19   1 63.211  ? 131 GLU   B OE2  1 ? 1 
ATOM   1716 H H    . GLU   A 1 119 ? 21.456 6.745   2.216   1 42.811  ? 131 GLU   B H    1 c 1 
ATOM   1717 H HA   . GLU   A 1 119 ? 22.027 5.417   -0.18   1 45.734  ? 131 GLU   B HA   1 c 1 
ATOM   1718 H HB2  . GLU   A 1 119 ? 22.526 7.741   -0.168  1 50.668  ? 131 GLU   B HB2  1 c 1 
ATOM   1719 H HB3  . GLU   A 1 119 ? 23.479 7.536   1.08    1 50.908  ? 131 GLU   B HB3  1 c 1 
ATOM   1720 H HG2  . GLU   A 1 119 ? 24.945 6.239   -0.238  1 54.864  ? 131 GLU   B HG2  1 c 1 
ATOM   1721 H HG3  . GLU   A 1 119 ? 23.989 6.411   -1.485  1 54.546  ? 131 GLU   B HG3  1 c 1 
ATOM   1722 N N    . ILE   A 1 120 ? 23.425 3.664   0.832   1 45.112  ? 132 ILE   B N    1 ? 1 
ATOM   1723 C CA   . ILE   A 1 120 ? 24.143 2.566   1.452   1 43.673  ? 132 ILE   B CA   1 ? 1 
ATOM   1724 C C    . ILE   A 1 120 ? 25.309 2.119   0.563   1 42.531  ? 132 ILE   B C    1 ? 1 
ATOM   1725 O O    . ILE   A 1 120 ? 25.113 1.931   -0.633  1 39.668  ? 132 ILE   B O    1 ? 1 
ATOM   1726 C CB   . ILE   A 1 120 ? 23.171 1.401   1.72    1 41.761  ? 132 ILE   B CB   1 ? 1 
ATOM   1727 C CG1  . ILE   A 1 120 ? 21.984 1.884   2.578   1 39.498  ? 132 ILE   B CG1  1 ? 1 
ATOM   1728 C CG2  . ILE   A 1 120 ? 23.928 0.229   2.352   1 41.841  ? 132 ILE   B CG2  1 ? 1 
ATOM   1729 C CD1  . ILE   A 1 120 ? 20.949 0.831   2.908   1 36.637  ? 132 ILE   B CD1  1 ? 1 
ATOM   1730 H H    . ILE   A 1 120 ? 23.099 3.539   -0.012  1 45.172  ? 132 ILE   B H    1 c 1 
ATOM   1731 H HA   . ILE   A 1 120 ? 24.501 2.87    2.308   1 43.659  ? 132 ILE   B HA   1 c 1 
ATOM   1732 H HB   . ILE   A 1 120 ? 22.817 1.102   0.859   1 41.494  ? 132 ILE   B HB   1 c 1 
ATOM   1733 H HG12 . ILE   A 1 120 ? 22.336 2.246   3.417   1 39.713  ? 132 ILE   B HG12 1 c 1 
ATOM   1734 H HG13 . ILE   A 1 120 ? 21.537 2.616   2.106   1 39.465  ? 132 ILE   B HG13 1 c 1 
ATOM   1735 H HG21 . ILE   A 1 120 ? 23.312 -0.5    2.531   1 40.567  ? 132 ILE   B HG21 1 c 1 
ATOM   1736 H HG22 . ILE   A 1 120 ? 24.336 0.517   3.186   1 42.364  ? 132 ILE   B HG22 1 c 1 
ATOM   1737 H HG23 . ILE   A 1 120 ? 24.621 -0.08   1.746   1 43.324  ? 132 ILE   B HG23 1 c 1 
ATOM   1738 H HD11 . ILE   A 1 120 ? 20.635 0.413   2.084   1 36.841  ? 132 ILE   B HD11 1 c 1 
ATOM   1739 H HD12 . ILE   A 1 120 ? 20.195 1.251   3.365   1 36.041  ? 132 ILE   B HD12 1 c 1 
ATOM   1740 H HD13 . ILE   A 1 120 ? 21.339 0.151   3.489   1 36.901  ? 132 ILE   B HD13 1 c 1 
ATOM   1741 N N    . GLU   A 1 121 ? 26.484 1.929   1.187   1 43.348  ? 133 GLU   B N    1 ? 1 
ATOM   1742 C CA   . GLU   A 1 121 ? 27.637 1.261   0.593   1 49.096  ? 133 GLU   B CA   1 ? 1 
ATOM   1743 C C    . GLU   A 1 121 ? 27.907 -0.06   1.318   1 51.75   ? 133 GLU   B C    1 ? 1 
ATOM   1744 O O    . GLU   A 1 121 ? 28.195 -0.053  2.515   1 55.14   ? 133 GLU   B O    1 ? 1 
ATOM   1745 C CB   . GLU   A 1 121 ? 28.869 2.176   0.668   1 50.51   ? 133 GLU   B CB   1 ? 1 
ATOM   1746 C CG   . GLU   A 1 121 ? 30.166 1.55    0.153   1 53.394  ? 133 GLU   B CG   1 ? 1 
ATOM   1747 C CD   . GLU   A 1 121 ? 31.393 2.481   0.171   1 56.464  ? 133 GLU   B CD   1 ? 1 
ATOM   1748 O OE1  . GLU   A 1 121 ? 31.216 3.713   0.383   1 53.463  ? 133 GLU   B OE1  1 ? 1 
ATOM   1749 O OE2  . GLU   A 1 121 ? 32.52  1.962   0       1 56.693  ? 133 GLU   B OE2  1 ? 1 
ATOM   1750 H H    . GLU   A 1 121 ? 26.57  2.242   2.042   1 44.194  ? 133 GLU   B H    1 c 1 
ATOM   1751 H HA   . GLU   A 1 121 ? 27.437 1.073   -0.356  1 48.882  ? 133 GLU   B HA   1 c 1 
ATOM   1752 H HB2  . GLU   A 1 121 ? 28.686 2.991   0.156   1 51.51   ? 133 GLU   B HB2  1 c 1 
ATOM   1753 H HB3  . GLU   A 1 121 ? 29.005 2.439   1.602   1 50.802  ? 133 GLU   B HB3  1 c 1 
ATOM   1754 H HG2  . GLU   A 1 121 ? 30.373 0.759   0.693   1 52.909  ? 133 GLU   B HG2  1 c 1 
ATOM   1755 H HG3  . GLU   A 1 121 ? 30.025 1.244   -0.769  1 53.489  ? 133 GLU   B HG3  1 c 1 
ATOM   1756 N N    . LEU   A 1 122 ? 27.87  -1.182  0.584   1 53.572  ? 134 LEU   B N    1 ? 1 
ATOM   1757 C CA   . LEU   A 1 122 ? 28.193 -2.49   1.141   1 53.34   ? 134 LEU   B CA   1 ? 1 
ATOM   1758 C C    . LEU   A 1 122 ? 29.698 -2.739  1.075   1 57.85   ? 134 LEU   B C    1 ? 1 
ATOM   1759 O O    . LEU   A 1 122 ? 30.257 -2.926  -0.009  1 58.997  ? 134 LEU   B O    1 ? 1 
ATOM   1760 C CB   . LEU   A 1 122 ? 27.427 -3.581  0.394   1 52.253  ? 134 LEU   B CB   1 ? 1 
ATOM   1761 C CG   . LEU   A 1 122 ? 27.641 -5.022  0.877   1 51.255  ? 134 LEU   B CG   1 ? 1 
ATOM   1762 C CD1  . LEU   A 1 122 ? 27.315 -5.159  2.347   1 50.5    ? 134 LEU   B CD1  1 ? 1 
ATOM   1763 C CD2  . LEU   A 1 122 ? 26.803 -6.003  0.08    1 49.494  ? 134 LEU   B CD2  1 ? 1 
ATOM   1764 H H    . LEU   A 1 122 ? 27.634 -1.129  -0.298  1 53.253  ? 134 LEU   B H    1 c 1 
ATOM   1765 H HA   . LEU   A 1 122 ? 27.914 -2.496  2.091   1 52.31   ? 134 LEU   B HA   1 c 1 
ATOM   1766 H HB2  . LEU   A 1 122 ? 26.465 -3.374  0.454   1 49.876  ? 134 LEU   B HB2  1 c 1 
ATOM   1767 H HB3  . LEU   A 1 122 ? 27.677 -3.534  -0.558  1 53.381  ? 134 LEU   B HB3  1 c 1 
ATOM   1768 H HG   . LEU   A 1 122 ? 28.595 -5.257  0.748   1 53.755  ? 134 LEU   B HG   1 c 1 
ATOM   1769 H HD11 . LEU   A 1 122 ? 27.966 -4.665  2.874   1 51.383  ? 134 LEU   B HD11 1 c 1 
ATOM   1770 H HD12 . LEU   A 1 122 ? 27.343 -6.098  2.6     1 50.433  ? 134 LEU   B HD12 1 c 1 
ATOM   1771 H HD13 . LEU   A 1 122 ? 26.426 -4.806  2.518   1 48.267  ? 134 LEU   B HD13 1 c 1 
ATOM   1772 H HD21 . LEU   A 1 122 ? 27.016 -5.921  -0.864  1 51.004  ? 134 LEU   B HD21 1 c 1 
ATOM   1773 H HD22 . LEU   A 1 122 ? 25.86  -5.811  0.216   1 47.737  ? 134 LEU   B HD22 1 c 1 
ATOM   1774 H HD23 . LEU   A 1 122 ? 26.994 -6.909  0.376   1 50.215  ? 134 LEU   B HD23 1 c 1 
ATOM   1775 N N    . LEU   A 1 123 ? 30.341 -2.807  2.251   1 61.395  ? 135 LEU   B N    1 ? 1 
ATOM   1776 C CA   . LEU   A 1 123 ? 31.798 -2.83   2.327   1 65.097  ? 135 LEU   B CA   1 ? 1 
ATOM   1777 C C    . LEU   A 1 123 ? 32.315 -4.259  2.185   1 68.593  ? 135 LEU   B C    1 ? 1 
ATOM   1778 O O    . LEU   A 1 123 ? 33.242 -4.509  1.419   1 73.239  ? 135 LEU   B O    1 ? 1 
ATOM   1779 C CB   . LEU   A 1 123 ? 32.281 -2.221  3.642   1 65.623  ? 135 LEU   B CB   1 ? 1 
ATOM   1780 C CG   . LEU   A 1 123 ? 31.895 -0.762  3.909   1 66.698  ? 135 LEU   B CG   1 ? 1 
ATOM   1781 C CD1  . LEU   A 1 123 ? 32.376 -0.348  5.3     1 69.442  ? 135 LEU   B CD1  1 ? 1 
ATOM   1782 C CD2  . LEU   A 1 123 ? 32.425 0.18    2.837   1 68.23   ? 135 LEU   B CD2  1 ? 1 
ATOM   1783 H H    . LEU   A 1 123 ? 29.859 -2.842  3.027   1 59.018  ? 135 LEU   B H    1 c 1 
ATOM   1784 H HA   . LEU   A 1 123 ? 32.157 -2.296  1.575   1 67.014  ? 135 LEU   B HA   1 c 1 
ATOM   1785 H HB2  . LEU   A 1 123 ? 31.934 -2.773  4.381   1 64.79   ? 135 LEU   B HB2  1 c 1 
ATOM   1786 H HB3  . LEU   A 1 123 ? 33.263 -2.289  3.667   1 69.327  ? 135 LEU   B HB3  1 c 1 
ATOM   1787 H HG   . LEU   A 1 123 ? 30.905 -0.701  3.902   1 63.398  ? 135 LEU   B HG   1 c 1 
ATOM   1788 H HD11 . LEU   A 1 123 ? 31.985 -0.935  5.968   1 67.721  ? 135 LEU   B HD11 1 c 1 
ATOM   1789 H HD12 . LEU   A 1 123 ? 32.106 0.569   5.478   1 68.835  ? 135 LEU   B HD12 1 c 1 
ATOM   1790 H HD13 . LEU   A 1 123 ? 33.345 -0.413  5.341   1 72.341  ? 135 LEU   B HD13 1 c 1 
ATOM   1791 H HD21 . LEU   A 1 123 ? 32.044 -0.057  1.976   1 67.377  ? 135 LEU   B HD21 1 c 1 
ATOM   1792 H HD22 . LEU   A 1 123 ? 33.392 0.107   2.794   1 71.656  ? 135 LEU   B HD22 1 c 1 
ATOM   1793 H HD23 . LEU   A 1 123 ? 32.18  1.094   3.058   1 68.258  ? 135 LEU   B HD23 1 c 1 
ATOM   1794 N N    . ASP   A 1 124 ? 31.724 -5.173  2.964   1 65.828  ? 136 ASP   B N    1 ? 1 
ATOM   1795 C CA   . ASP   A 1 124 ? 32.143 -6.562  3.048   1 66.989  ? 136 ASP   B CA   1 ? 1 
ATOM   1796 C C    . ASP   A 1 124 ? 30.985 -7.344  3.675   1 63.518  ? 136 ASP   B C    1 ? 1 
ATOM   1797 O O    . ASP   A 1 124 ? 30.058 -6.734  4.224   1 56.361  ? 136 ASP   B O    1 ? 1 
ATOM   1798 C CB   . ASP   A 1 124 ? 33.407 -6.694  3.885   1 69.138  ? 136 ASP   B CB   1 ? 1 
ATOM   1799 C CG   . ASP   A 1 124 ? 34.295 -7.908  3.647   1 75.537  ? 136 ASP   B CG   1 ? 1 
ATOM   1800 O OD1  . ASP   A 1 124 ? 34.061 -8.672  2.683   1 77.985  ? 136 ASP   B OD1  1 ? 1 
ATOM   1801 O OD2  . ASP   A 1 124 ? 35.274 -8.056  4.406   1 81.477  ? 136 ASP   B OD2  1 ? 1 
ATOM   1802 H H    . ASP   A 1 124 ? 31.017 -4.907  3.479   1 63.71   ? 136 ASP   B H    1 c 1 
ATOM   1803 H HA   . ASP   A 1 124 ? 32.306 -6.898  2.137   1 67.65   ? 136 ASP   B HA   1 c 1 
ATOM   1804 H HB2  . ASP   A 1 124 ? 33.958 -5.898  3.738   1 71.914  ? 136 ASP   B HB2  1 c 1 
ATOM   1805 H HB3  . ASP   A 1 124 ? 33.149 -6.698  4.831   1 69.363  ? 136 ASP   B HB3  1 c 1 
ATOM   1806 N N    . PHE   A 1 125 ? 31.038 -8.68   3.573   1 61.265  ? 137 PHE   B N    1 ? 1 
ATOM   1807 C CA   . PHE   A 1 125 ? 30.102 -9.541  4.288   1 60.46   ? 137 PHE   B CA   1 ? 1 
ATOM   1808 C C    . PHE   A 1 125 ? 30.775 -10.893 4.482   1 61.162  ? 137 PHE   B C    1 ? 1 
ATOM   1809 O O    . PHE   A 1 125 ? 31.454 -11.373 3.584   1 62.83   ? 137 PHE   B O    1 ? 1 
ATOM   1810 C CB   . PHE   A 1 125 ? 28.741 -9.688  3.589   1 57.386  ? 137 PHE   B CB   1 ? 1 
ATOM   1811 C CG   . PHE   A 1 125 ? 28.767 -10.202 2.153   1 59.056  ? 137 PHE   B CG   1 ? 1 
ATOM   1812 C CD1  . PHE   A 1 125 ? 28.923 -9.332  1.079   1 58.406  ? 137 PHE   B CD1  1 ? 1 
ATOM   1813 C CD2  . PHE   A 1 125 ? 28.611 -11.555 1.88    1 61.686  ? 137 PHE   B CD2  1 ? 1 
ATOM   1814 C CE1  . PHE   A 1 125 ? 28.939 -9.81   -0.227  1 62.593  ? 137 PHE   B CE1  1 ? 1 
ATOM   1815 C CE2  . PHE   A 1 125 ? 28.635 -12.029 0.572   1 64.559  ? 137 PHE   B CE2  1 ? 1 
ATOM   1816 C CZ   . PHE   A 1 125 ? 28.807 -11.16  -0.476  1 64.438  ? 137 PHE   B CZ   1 ? 1 
ATOM   1817 H H    . PHE   A 1 125 ? 31.671 -9.064  3.038   1 64.373  ? 137 PHE   B H    1 c 1 
ATOM   1818 H HA   . PHE   A 1 125 ? 29.946 -9.141  5.181   1 59.085  ? 137 PHE   B HA   1 c 1 
ATOM   1819 H HB2  . PHE   A 1 125 ? 28.187 -10.296 4.127   1 56.703  ? 137 PHE   B HB2  1 c 1 
ATOM   1820 H HB3  . PHE   A 1 125 ? 28.298 -8.811  3.598   1 55.917  ? 137 PHE   B HB3  1 c 1 
ATOM   1821 H HD1  . PHE   A 1 125 ? 29.025 -8.408  1.24    1 58.823  ? 137 PHE   B HD1  1 c 1 
ATOM   1822 H HD2  . PHE   A 1 125 ? 28.505 -12.163 2.594   1 61.674  ? 137 PHE   B HD2  1 c 1 
ATOM   1823 H HE1  . PHE   A 1 125 ? 29.057 -9.209  -0.945  1 62.676  ? 137 PHE   B HE1  1 c 1 
ATOM   1824 H HE2  . PHE   A 1 125 ? 28.538 -12.953 0.407   1 65.013  ? 137 PHE   B HE2  1 c 1 
ATOM   1825 H HZ   . PHE   A 1 125 ? 28.814 -11.482 -1.362  1 65.636  ? 137 PHE   B HZ   1 c 1 
ATOM   1826 N N    . LYS   A 1 126 ? 30.591 -11.466 5.677   1 60.509  ? 138 LYS   B N    1 ? 1 
ATOM   1827 C CA   . LYS   A 1 126 ? 31.227 -12.704 6.087   1 63.84   ? 138 LYS   B CA   1 ? 1 
ATOM   1828 C C    . LYS   A 1 126 ? 30.165 -13.726 6.49    1 62.078  ? 138 LYS   B C    1 ? 1 
ATOM   1829 O O    . LYS   A 1 126 ? 29.147 -13.379 7.072   1 54.908  ? 138 LYS   B O    1 ? 1 
ATOM   1830 C CB   . LYS   A 1 126 ? 32.147 -12.372 7.269   1 67.429  ? 138 LYS   B CB   1 ? 1 
ATOM   1831 H H    . LYS   A 1 126 ? 30.025 -11.059 6.269   1 59.136  ? 138 LYS   B H    1 c 1 
ATOM   1832 H HA   . LYS   A 1 126 ? 31.76  -13.061 5.332   1 65.572  ? 138 LYS   B HA   1 c 1 
ATOM   1833 H HB2  . LYS   A 1 126 ? 33.106 -12.459 6.969   0 30      ? 138 LYS   B HB2  1 c 1 
ATOM   1834 H HB3  . LYS   A 1 126 ? 31.614 -12.166 8.038   0 30      ? 138 LYS   B HB3  1 c 1 
ATOM   1835 N N    . GLY   A 1 127 ? 30.436 -15.004 6.211   1 68.323  ? 139 GLY   B N    1 ? 1 
ATOM   1836 C CA   . GLY   A 1 127 ? 29.666 -16.088 6.797   1 69.526  ? 139 GLY   B CA   1 ? 1 
ATOM   1837 C C    . GLY   A 1 127 ? 29.794 -16.095 8.32    1 72.568  ? 139 GLY   B C    1 ? 1 
ATOM   1838 O O    . GLY   A 1 127 ? 30.895 -16.036 8.867   1 76.099  ? 139 GLY   B O    1 ? 1 
ATOM   1839 H H    . GLY   A 1 127 ? 31.122 -15.207 5.642   1 69.421  ? 139 GLY   B H    1 c 1 
ATOM   1840 H HA2  . GLY   A 1 127 ? 28.719 -15.987 6.541   1 67.285  ? 139 GLY   B HA2  1 c 1 
ATOM   1841 H HA3  . GLY   A 1 127 ? 29.991 -16.944 6.435   1 71.642  ? 139 GLY   B HA3  1 c 1 
ATOM   1842 N N    . GLU   A 1 128 ? 28.654 -16.199 9.005   1 72.661  ? 140 GLU   B N    1 ? 1 
ATOM   1843 C CA   . GLU   A 1 128 ? 28.649 -16.472 10.434  1 78.372  ? 140 GLU   B CA   1 ? 1 
ATOM   1844 C C    . GLU   A 1 128 ? 29.348 -17.827 10.707  1 84.985  ? 140 GLU   B C    1 ? 1 
ATOM   1845 O O    . GLU   A 1 128 ? 29.84  -18.453 9.729   1 87.35   ? 140 GLU   B O    1 ? 1 
ATOM   1846 C CB   . GLU   A 1 128 ? 27.228 -16.415 11.008  1 71.464  ? 140 GLU   B CB   1 ? 1 
ATOM   1847 O OXT  . GLU   A 1 128 ? 29.401 -18.209 11.897  1 88.428  ? 140 GLU   B OXT  1 ? 1 
ATOM   1848 H H    . GLU   A 1 128 ? 27.856 -16.098 8.57    1 70.808  ? 140 GLU   B H    1 c 1 
ATOM   1849 H HA   . GLU   A 1 128 ? 29.178 -15.761 10.879  1 77.634  ? 140 GLU   B HA   1 c 1 
ATOM   1850 H HB2  . GLU   A 1 128 ? 27.202 -16.593 11.9    0 30      ? 140 GLU   B HB2  1 c 1 
ATOM   1851 H HB3  . GLU   A 1 128 ? 26.577 -16.468 10.156  0 30      ? 140 GLU   B HB3  1 c 1 
ATOM   1852 N N    . THR   B 1 5   ? 0.831  -3.494  43.764  1 65.17   ? 17  THR   A N    1 ? 2 
ATOM   1853 C CA   . THR   B 1 5   ? 1.977  -3.983  42.953  1 63.461  ? 17  THR   A CA   1 ? 2 
ATOM   1854 C C    . THR   B 1 5   ? 2.476  -2.863  42.027  1 61.479  ? 17  THR   A C    1 ? 2 
ATOM   1855 O O    . THR   B 1 5   ? 1.743  -1.919  41.721  1 62.631  ? 17  THR   A O    1 ? 2 
ATOM   1856 C CB   . THR   B 1 5   ? 1.607  -5.257  42.17   1 62.966  ? 17  THR   A CB   1 ? 2 
ATOM   1857 O OG1  . THR   B 1 5   ? 0.895  -4.87   40.998  1 63.965  ? 17  THR   A OG1  1 ? 2 
ATOM   1858 C CG2  . THR   B 1 5   ? 0.78   -6.264  42.949  1 59.633  ? 17  THR   A CG2  1 ? 2 
ATOM   1859 H H    . THR   B 1 5   ? 0.653  -4.08   44.426  1 66.531  ? 17  THR   A H    1 c 2 
ATOM   1860 H HA   . THR   B 1 5   ? 2.702  -4.211  43.573  1 63.465  ? 17  THR   A HA   1 c 2 
ATOM   1861 H HB   . THR   B 1 5   ? 2.442  -5.706  41.896  1 60.331  ? 17  THR   A HB   1 c 2 
ATOM   1862 H HG1  . THR   B 1 5   ? 0.289  -4.54   41.063  0 30      ? 17  THR   A HG1  1 c 2 
ATOM   1863 H HG21 . THR   B 1 5   ? 0.723  -7.095  42.448  1 59.587  ? 17  THR   A HG21 1 c 2 
ATOM   1864 H HG22 . THR   B 1 5   ? -0.115 -5.911  43.089  1 62.636  ? 17  THR   A HG22 1 c 2 
ATOM   1865 H HG23 . THR   B 1 5   ? 1.199  -6.433  43.81   1 61.952  ? 17  THR   A HG23 1 c 2 
ATOM   1866 N N    . VAL   B 1 6   ? 3.751  -2.975  41.601  1 60.186  ? 18  VAL   A N    1 ? 2 
ATOM   1867 C CA   . VAL   B 1 6   ? 4.417  -2.04   40.687  1 57.527  ? 18  VAL   A CA   1 ? 2 
ATOM   1868 C C    . VAL   B 1 6   ? 4.72   -2.777  39.383  1 50.923  ? 18  VAL   A C    1 ? 2 
ATOM   1869 O O    . VAL   B 1 6   ? 4.633  -3.998  39.317  1 60.939  ? 18  VAL   A O    1 ? 2 
ATOM   1870 C CB   . VAL   B 1 6   ? 5.723  -1.434  41.252  1 52.545  ? 18  VAL   A CB   1 ? 2 
ATOM   1871 C CG1  . VAL   B 1 6   ? 5.478  -0.563  42.469  1 55.897  ? 18  VAL   A CG1  1 ? 2 
ATOM   1872 C CG2  . VAL   B 1 6   ? 6.739  -2.518  41.606  1 52.993  ? 18  VAL   A CG2  1 ? 2 
ATOM   1873 H H    . VAL   B 1 6   ? 4.231  -3.694  41.897  1 58.938  ? 18  VAL   A H    1 c 2 
ATOM   1874 H HA   . VAL   B 1 6   ? 3.8    -1.309  40.491  1 57.122  ? 18  VAL   A HA   1 c 2 
ATOM   1875 H HB   . VAL   B 1 6   ? 6.114  -0.867  40.548  1 53.127  ? 18  VAL   A HB   1 c 2 
ATOM   1876 H HG11 . VAL   B 1 6   ? 5.084  -1.098  43.178  1 56.849  ? 18  VAL   A HG11 1 c 2 
ATOM   1877 H HG12 . VAL   B 1 6   ? 4.87   0.159   42.234  1 56.895  ? 18  VAL   A HG12 1 c 2 
ATOM   1878 H HG13 . VAL   B 1 6   ? 6.321  -0.189  42.776  1 56.519  ? 18  VAL   A HG13 1 c 2 
ATOM   1879 H HG21 . VAL   B 1 6   ? 7.53   -2.105  41.991  1 53.323  ? 18  VAL   A HG21 1 c 2 
ATOM   1880 H HG22 . VAL   B 1 6   ? 6.989  -3.005  40.804  1 50.566  ? 18  VAL   A HG22 1 c 2 
ATOM   1881 H HG23 . VAL   B 1 6   ? 6.35   -3.132  42.25   1 53.274  ? 18  VAL   A HG23 1 c 2 
ATOM   1882 N N    . THR   B 1 7   ? 5.142  -2.035  38.366  1 53.724  ? 19  THR   A N    1 ? 2 
ATOM   1883 C CA   . THR   B 1 7   ? 5.388  -2.591  37.039  1 49.762  ? 19  THR   A CA   1 ? 2 
ATOM   1884 C C    . THR   B 1 7   ? 6.737  -3.302  37.031  1 54.874  ? 19  THR   A C    1 ? 2 
ATOM   1885 O O    . THR   B 1 7   ? 6.856  -4.396  36.485  1 52.413  ? 19  THR   A O    1 ? 2 
ATOM   1886 C CB   . THR   B 1 7   ? 5.412  -1.525  35.94   1 48.148  ? 19  THR   A CB   1 ? 2 
ATOM   1887 O OG1  . THR   B 1 7   ? 4.334  -0.59   36.02   1 49.297  ? 19  THR   A OG1  1 ? 2 
ATOM   1888 C CG2  . THR   B 1 7   ? 5.485  -2.196  34.577  1 43.018  ? 19  THR   A CG2  1 ? 2 
ATOM   1889 H H    . THR   B 1 7   ? 5.275  -1.14   38.494  1 53.504  ? 19  THR   A H    1 c 2 
ATOM   1890 H HA   . THR   B 1 7   ? 4.681  -3.241  36.833  1 50.535  ? 19  THR   A HA   1 c 2 
ATOM   1891 H HB   . THR   B 1 7   ? 6.254  -1.019  36.042  1 47.864  ? 19  THR   A HB   1 c 2 
ATOM   1892 H HG1  . THR   B 1 7   ? 3.577  -1.015  35.96   0 30      ? 19  THR   A HG1  1 c 2 
ATOM   1893 H HG21 . THR   B 1 7   ? 5.379  -1.526  33.881  1 44.031  ? 19  THR   A HG21 1 c 2 
ATOM   1894 H HG22 . THR   B 1 7   ? 4.775  -2.855  34.502  1 43.743  ? 19  THR   A HG22 1 c 2 
ATOM   1895 H HG23 . THR   B 1 7   ? 6.346  -2.634  34.474  1 42.859  ? 19  THR   A HG23 1 c 2 
ATOM   1896 N N    . GLU   B 1 8   ? 7.776  -2.642  37.57   1 58.81   ? 20  GLU   A N    1 ? 2 
ATOM   1897 C CA   . GLU   B 1 8   ? 9.147  -3.151  37.491  1 55.403  ? 20  GLU   A CA   1 ? 2 
ATOM   1898 C C    . GLU   B 1 8   ? 9.387  -4.123  38.651  1 54.079  ? 20  GLU   A C    1 ? 2 
ATOM   1899 O O    . GLU   B 1 8   ? 10.303 -3.989  39.458  1 56.522  ? 20  GLU   A O    1 ? 2 
ATOM   1900 C CB   . GLU   B 1 8   ? 10.161 -2.01   37.421  1 51.834  ? 20  GLU   A CB   1 ? 2 
ATOM   1901 C CG   . GLU   B 1 8   ? 9.79   -0.952  36.39   1 57.359  ? 20  GLU   A CG   1 ? 2 
ATOM   1902 C CD   . GLU   B 1 8   ? 9.8    -1.391  34.924  1 53.016  ? 20  GLU   A CD   1 ? 2 
ATOM   1903 O OE1  . GLU   B 1 8   ? 10.361 -2.467  34.614  1 43.474  ? 20  GLU   A OE1  1 ? 2 
ATOM   1904 O OE2  . GLU   B 1 8   ? 9.307  -0.588  34.094  1 53.098  ? 20  GLU   A OE2  1 ? 2 
ATOM   1905 H H    . GLU   B 1 8   ? 7.626  -1.853  38.007  1 58.859  ? 20  GLU   A H    1 c 2 
ATOM   1906 H HA   . GLU   B 1 8   ? 9.231  -3.664  36.648  1 53.018  ? 20  GLU   A HA   1 c 2 
ATOM   1907 H HB2  . GLU   B 1 8   ? 10.228 -1.59   38.304  1 55.709  ? 20  GLU   A HB2  1 c 2 
ATOM   1908 H HB3  . GLU   B 1 8   ? 11.04  -2.381  37.199  1 53.279  ? 20  GLU   A HB3  1 c 2 
ATOM   1909 H HG2  . GLU   B 1 8   ? 8.896  -0.608  36.598  1 56.412  ? 20  GLU   A HG2  1 c 2 
ATOM   1910 H HG3  . GLU   B 1 8   ? 10.41  -0.198  36.483  1 56.43   ? 20  GLU   A HG3  1 c 2 
ATOM   1911 N N    . GLN   B 1 9   ? 8.519  -5.125  38.714  1 53.059  ? 21  GLN   A N    1 ? 2 
ATOM   1912 C CA   . GLN   B 1 9   ? 8.496  -6.064  39.814  1 53.65   ? 21  GLN   A CA   1 ? 2 
ATOM   1913 C C    . GLN   B 1 9   ? 9.023  -7.395  39.277  1 49.316  ? 21  GLN   A C    1 ? 2 
ATOM   1914 O O    . GLN   B 1 9   ? 8.849  -7.706  38.088  1 39.158  ? 21  GLN   A O    1 ? 2 
ATOM   1915 C CB   . GLN   B 1 9   ? 7.051  -6.221  40.267  1 56.482  ? 21  GLN   A CB   1 ? 2 
ATOM   1916 C CG   . GLN   B 1 9   ? 6.143  -6.816  39.189  1 56.529  ? 21  GLN   A CG   1 ? 2 
ATOM   1917 C CD   . GLN   B 1 9   ? 4.922  -7.483  39.772  1 61.245  ? 21  GLN   A CD   1 ? 2 
ATOM   1918 O OE1  . GLN   B 1 9   ? 4.717  -7.491  40.995  1 58.184  ? 21  GLN   A OE1  1 ? 2 
ATOM   1919 N NE2  . GLN   B 1 9   ? 4.145  -8.103  38.894  1 60.549  ? 21  GLN   A NE2  1 ? 2 
ATOM   1920 H H    . GLN   B 1 9   ? 7.934  -5.248  38.024  1 52.362  ? 21  GLN   A H    1 c 2 
ATOM   1921 H HA   . GLN   B 1 9   ? 9.073  -5.736  40.55   1 54.743  ? 21  GLN   A HA   1 c 2 
ATOM   1922 H HB2  . GLN   B 1 9   ? 7.032  -6.797  41.059  1 57.322  ? 21  GLN   A HB2  1 c 2 
ATOM   1923 H HB3  . GLN   B 1 9   ? 6.703  -5.342  40.527  1 57.569  ? 21  GLN   A HB3  1 c 2 
ATOM   1924 H HG2  . GLN   B 1 9   ? 5.856  -6.107  38.576  1 56.661  ? 21  GLN   A HG2  1 c 2 
ATOM   1925 H HG3  . GLN   B 1 9   ? 6.638  -7.479  38.667  1 55.345  ? 21  GLN   A HG3  1 c 2 
ATOM   1926 H HE21 . GLN   B 1 9   ? 3.41   -8.516  39.17   1 61.226  ? 21  GLN   A HE21 1 c 2 
ATOM   1927 H HE22 . GLN   B 1 9   ? 4.359  -8.106  38.033  1 59.165  ? 21  GLN   A HE22 1 c 2 
ATOM   1928 N N    . GLY   B 1 10  ? 9.652  -8.15   40.169  1 44.435  ? 22  GLY   A N    1 ? 2 
ATOM   1929 C CA   . GLY   B 1 10  ? 10.235 -9.414  39.8    1 42.792  ? 22  GLY   A CA   1 ? 2 
ATOM   1930 C C    . GLY   B 1 10  ? 11.751 -9.356  39.928  1 45.267  ? 22  GLY   A C    1 ? 2 
ATOM   1931 O O    . GLY   B 1 10  ? 12.344 -8.305  40.163  1 41.918  ? 22  GLY   A O    1 ? 2 
ATOM   1932 H H    . GLY   B 1 10  ? 9.717  -7.869  41.036  1 47.175  ? 22  GLY   A H    1 c 2 
ATOM   1933 H HA2  . GLY   B 1 10  ? 9.879  -10.121 40.389  1 44.095  ? 22  GLY   A HA2  1 c 2 
ATOM   1934 H HA3  . GLY   B 1 10  ? 9.989  -9.636  38.872  1 42.041  ? 22  GLY   A HA3  1 c 2 
ATOM   1935 N N    . GLU   B 1 11  ? 12.355 -10.531 39.756  1 45.57   ? 23  GLU   A N    1 ? 2 
ATOM   1936 C CA   . GLU   B 1 11  ? 13.776 -10.742 39.944  1 43.981  ? 23  GLU   A CA   1 ? 2 
ATOM   1937 C C    . GLU   B 1 11  ? 14.489 -10.415 38.636  1 42.752  ? 23  GLU   A C    1 ? 2 
ATOM   1938 O O    . GLU   B 1 11  ? 14.058 -10.851 37.552  1 39.177  ? 23  GLU   A O    1 ? 2 
ATOM   1939 C CB   . GLU   B 1 11  ? 13.965 -12.201 40.356  1 47.16   ? 23  GLU   A CB   1 ? 2 
ATOM   1940 C CG   . GLU   B 1 11  ? 15.418 -12.609 40.568  1 52.955  ? 23  GLU   A CG   1 ? 2 
ATOM   1941 C CD   . GLU   B 1 11  ? 15.652 -14.106 40.699  1 58.95   ? 23  GLU   A CD   1 ? 2 
ATOM   1942 O OE1  . GLU   B 1 11  ? 14.69  -14.884 40.887  1 67.699  ? 23  GLU   A OE1  1 ? 2 
ATOM   1943 O OE2  . GLU   B 1 11  ? 16.825 -14.502 40.614  1 61.197  ? 23  GLU   A OE2  1 ? 2 
ATOM   1944 H H    . GLU   B 1 11  ? 11.844 -11.245 39.502  1 44.281  ? 23  GLU   A H    1 c 2 
ATOM   1945 H HA   . GLU   B 1 11  ? 14.099 -10.141 40.663  1 46.276  ? 23  GLU   A HA   1 c 2 
ATOM   1946 H HB2  . GLU   B 1 11  ? 13.471 -12.362 41.182  1 48.641  ? 23  GLU   A HB2  1 c 2 
ATOM   1947 H HB3  . GLU   B 1 11  ? 13.579 -12.776 39.662  1 46.43   ? 23  GLU   A HB3  1 c 2 
ATOM   1948 H HG2  . GLU   B 1 11  ? 15.956 -12.278 39.818  1 52.152  ? 23  GLU   A HG2  1 c 2 
ATOM   1949 H HG3  . GLU   B 1 11  ? 15.753 -12.172 41.381  1 54.509  ? 23  GLU   A HG3  1 c 2 
ATOM   1950 N N    . ASP   B 1 12  ? 15.573 -9.628  38.767  1 43.829  ? 24  ASP   A N    1 ? 2 
ATOM   1951 C CA   . ASP   B 1 12  ? 16.392 -9.239  37.645  1 41.958  ? 24  ASP   A CA   1 ? 2 
ATOM   1952 C C    . ASP   B 1 12  ? 17.329 -10.397 37.308  1 42.636  ? 24  ASP   A C    1 ? 2 
ATOM   1953 O O    . ASP   B 1 12  ? 18.287 -10.673 38.023  1 39.01   ? 24  ASP   A O    1 ? 2 
ATOM   1954 C CB   . ASP   B 1 12  ? 17.226 -7.995  37.901  1 42.347  ? 24  ASP   A CB   1 ? 2 
ATOM   1955 C CG   . ASP   B 1 12  ? 18.011 -7.539  36.673  1 42.519  ? 24  ASP   A CG   1 ? 2 
ATOM   1956 O OD1  . ASP   B 1 12  ? 17.938 -8.251  35.644  1 39.68   ? 24  ASP   A OD1  1 ? 2 
ATOM   1957 O OD2  . ASP   B 1 12  ? 18.686 -6.484  36.74   1 44.805  ? 24  ASP   A OD2  1 ? 2 
ATOM   1958 H H    . ASP   B 1 12  ? 15.803 -9.327  39.599  1 45.006  ? 24  ASP   A H    1 c 2 
ATOM   1959 H HA   . ASP   B 1 12  ? 15.805 -9.064  36.876  1 40.798  ? 24  ASP   A HA   1 c 2 
ATOM   1960 H HB2  . ASP   B 1 12  ? 16.634 -7.265  38.179  1 43.015  ? 24  ASP   A HB2  1 c 2 
ATOM   1961 H HB3  . ASP   B 1 12  ? 17.858 -8.169  38.629  1 44.25   ? 24  ASP   A HB3  1 c 2 
ATOM   1962 N N    . ILE   B 1 13  ? 17.071 -11.018 36.163  1 40.349  ? 25  ILE   A N    1 ? 2 
ATOM   1963 C CA   . ILE   B 1 13  ? 17.75  -12.241 35.778  1 40.709  ? 25  ILE   A CA   1 ? 2 
ATOM   1964 C C    . ILE   B 1 13  ? 18.67  -11.914 34.599  1 40.577  ? 25  ILE   A C    1 ? 2 
ATOM   1965 O O    . ILE   B 1 13  ? 19.211 -12.822 33.988  1 39.935  ? 25  ILE   A O    1 ? 2 
ATOM   1966 C CB   . ILE   B 1 13  ? 16.738 -13.359 35.444  1 35.949  ? 25  ILE   A CB   1 ? 2 
ATOM   1967 C CG1  . ILE   B 1 13  ? 15.874 -13.011 34.245  1 38.758  ? 25  ILE   A CG1  1 ? 2 
ATOM   1968 C CG2  . ILE   B 1 13  ? 15.839 -13.675 36.615  1 37.825  ? 25  ILE   A CG2  1 ? 2 
ATOM   1969 C CD1  . ILE   B 1 13  ? 14.916 -14.11  33.842  1 39.324  ? 25  ILE   A CD1  1 ? 2 
ATOM   1970 H H    . ILE   B 1 13  ? 16.448 -10.666 35.596  1 39.504  ? 25  ILE   A H    1 c 2 
ATOM   1971 H HA   . ILE   B 1 13  ? 18.301 -12.541 36.527  1 41.321  ? 25  ILE   A HA   1 c 2 
ATOM   1972 H HB   . ILE   B 1 13  ? 17.244 -14.166 35.224  1 38.07   ? 25  ILE   A HB   1 c 2 
ATOM   1973 H HG12 . ILE   B 1 13  ? 15.357 -12.207 34.452  1 37.623  ? 25  ILE   A HG12 1 c 2 
ATOM   1974 H HG13 . ILE   B 1 13  ? 16.454 -12.806 33.484  1 37.625  ? 25  ILE   A HG13 1 c 2 
ATOM   1975 H HG21 . ILE   B 1 13  ? 15.393 -14.526 36.466  1 37.307  ? 25  ILE   A HG21 1 c 2 
ATOM   1976 H HG22 . ILE   B 1 13  ? 15.173 -12.975 36.713  1 37.074  ? 25  ILE   A HG22 1 c 2 
ATOM   1977 H HG23 . ILE   B 1 13  ? 16.37  -13.73  37.427  1 38.791  ? 25  ILE   A HG23 1 c 2 
ATOM   1978 H HD11 . ILE   B 1 13  ? 15.406 -14.948 33.742  1 39.428  ? 25  ILE   A HD11 1 c 2 
ATOM   1979 H HD12 . ILE   B 1 13  ? 14.496 -13.878 32.991  1 38.067  ? 25  ILE   A HD12 1 c 2 
ATOM   1980 H HD13 . ILE   B 1 13  ? 14.225 -14.219 34.522  1 39.125  ? 25  ILE   A HD13 1 c 2 
ATOM   1981 N N    . THR   B 1 14  ? 18.882 -10.625 34.301  1 41.469  ? 26  THR   A N    1 ? 2 
ATOM   1982 C CA   . THR   B 1 14  ? 19.895 -10.244 33.315  1 42.135  ? 26  THR   A CA   1 ? 2 
ATOM   1983 C C    . THR   B 1 14  ? 21.304 -10.402 33.886  1 45.732  ? 26  THR   A C    1 ? 2 
ATOM   1984 O O    . THR   B 1 14  ? 21.511 -10.477 35.11   1 50.496  ? 26  THR   A O    1 ? 2 
ATOM   1985 C CB   . THR   B 1 14  ? 19.643 -8.83   32.784  1 42.357  ? 26  THR   A CB   1 ? 2 
ATOM   1986 O OG1  . THR   B 1 14  ? 19.902 -7.875  33.812  1 37.559  ? 26  THR   A OG1  1 ? 2 
ATOM   1987 C CG2  . THR   B 1 14  ? 18.241 -8.698  32.209  1 37.999  ? 26  THR   A CG2  1 ? 2 
ATOM   1988 H H    . THR   B 1 14  ? 18.402 -9.97   34.719  1 41.282  ? 26  THR   A H    1 c 2 
ATOM   1989 H HA   . THR   B 1 14  ? 19.81  -10.86  32.555  1 41.752  ? 26  THR   A HA   1 c 2 
ATOM   1990 H HB   . THR   B 1 14  ? 20.275 -8.668  32.044  1 40.585  ? 26  THR   A HB   1 c 2 
ATOM   1991 H HG1  . THR   B 1 14  ? 19.429 -7.991  34.459  0 30      ? 26  THR   A HG1  1 c 2 
ATOM   1992 H HG21 . THR   B 1 14  ? 18.126 -7.807  31.837  1 38.606  ? 26  THR   A HG21 1 c 2 
ATOM   1993 H HG22 . THR   B 1 14  ? 17.586 -8.841  32.911  1 38.698  ? 26  THR   A HG22 1 c 2 
ATOM   1994 H HG23 . THR   B 1 14  ? 18.114 -9.359  31.508  1 38.064  ? 26  THR   A HG23 1 c 2 
ATOM   1995 N N    . SER   B 1 15  ? 22.283 -10.475 32.981  1 48.78   ? 27  SER   A N    1 ? 2 
ATOM   1996 C CA   . SER   B 1 15  ? 23.677 -10.643 33.392  1 56.812  ? 27  SER   A CA   1 ? 2 
ATOM   1997 C C    . SER   B 1 15  ? 24.279 -9.305  33.813  1 51.642  ? 27  SER   A C    1 ? 2 
ATOM   1998 O O    . SER   B 1 15  ? 24.938 -9.215  34.841  1 51.937  ? 27  SER   A O    1 ? 2 
ATOM   1999 C CB   . SER   B 1 15  ? 24.521 -11.313 32.333  1 57.423  ? 27  SER   A CB   1 ? 2 
ATOM   2000 O OG   . SER   B 1 15  ? 24.719 -12.668 32.711  1 60.805  ? 27  SER   A OG   1 ? 2 
ATOM   2001 H H    . SER   B 1 15  ? 22.085 -10.414 32.09   1 48.346  ? 27  SER   A H    1 c 2 
ATOM   2002 H HA   . SER   B 1 15  ? 23.681 -11.231 34.19   1 55.105  ? 27  SER   A HA   1 c 2 
ATOM   2003 H HB2  . SER   B 1 15  ? 24.067 -11.272 31.471  1 56.549  ? 27  SER   A HB2  1 c 2 
ATOM   2004 H HB3  . SER   B 1 15  ? 25.383 -10.861 32.259  1 59.309  ? 27  SER   A HB3  1 c 2 
ATOM   2005 H HG   . SER   B 1 15  ? 25.221 -13.054 32.259  0 30      ? 27  SER   A HG   1 c 2 
ATOM   2006 N N    . LYS   B 1 16  ? 24.005 -8.271  33.024  1 47.168  ? 28  LYS   A N    1 ? 2 
ATOM   2007 C CA   . LYS   B 1 16  ? 24.48  -6.925  33.312  1 49.878  ? 28  LYS   A CA   1 ? 2 
ATOM   2008 C C    . LYS   B 1 16  ? 23.723 -6.319  34.495  1 44.9    ? 28  LYS   A C    1 ? 2 
ATOM   2009 O O    . LYS   B 1 16  ? 24.065 -5.238  34.957  1 48.079  ? 28  LYS   A O    1 ? 2 
ATOM   2010 C CB   . LYS   B 1 16  ? 24.23  -6.013  32.107  1 52.71   ? 28  LYS   A CB   1 ? 2 
ATOM   2011 C CG   . LYS   B 1 16  ? 24.946 -6.34   30.803  1 58.719  ? 28  LYS   A CG   1 ? 2 
ATOM   2012 C CD   . LYS   B 1 16  ? 24.113 -5.83   29.627  1 62.27   ? 28  LYS   A CD   1 ? 2 
ATOM   2013 C CE   . LYS   B 1 16  ? 24.846 -5.091  28.548  1 67.665  ? 28  LYS   A CE   1 ? 2 
ATOM   2014 N NZ   . LYS   B 1 16  ? 25.626 -6.025  27.74   1 71.579  ? 28  LYS   A NZ   1 ? 2 
ATOM   2015 H H    . LYS   B 1 16  ? 23.508 -8.406  32.269  1 46.941  ? 28  LYS   A H    1 c 2 
ATOM   2016 H HA   . LYS   B 1 16  ? 25.448 -6.961  33.521  1 51.108  ? 28  LYS   A HA   1 c 2 
ATOM   2017 H HB2  . LYS   B 1 16  ? 23.265 -6.014  31.93   1 51.457  ? 28  LYS   A HB2  1 c 2 
ATOM   2018 H HB3  . LYS   B 1 16  ? 24.476 -5.099  32.362  1 53.987  ? 28  LYS   A HB3  1 c 2 
ATOM   2019 H HG2  . LYS   B 1 16  ? 25.828 -5.908  30.799  1 60.118  ? 28  LYS   A HG2  1 c 2 
ATOM   2020 H HG3  . LYS   B 1 16  ? 25.065 -7.312  30.731  1 58.18   ? 28  LYS   A HG3  1 c 2 
ATOM   2021 H HD2  . LYS   B 1 16  ? 23.659 -6.601  29.222  1 60.759  ? 28  LYS   A HD2  1 c 2 
ATOM   2022 H HD3  . LYS   B 1 16  ? 23.409 -5.242  29.977  1 61.183  ? 28  LYS   A HD3  1 c 2 
ATOM   2023 H HE2  . LYS   B 1 16  ? 24.21  -4.626  27.976  1 66.367  ? 28  LYS   A HE2  1 c 2 
ATOM   2024 H HE3  . LYS   B 1 16  ? 25.444 -4.433  28.945  1 68.877  ? 28  LYS   A HE3  1 c 2 
ATOM   2025 H HZ1  . LYS   B 1 16  ? 25.078 -6.64   27.362  1 69.197  ? 28  LYS   A HZ1  1 c 2 
ATOM   2026 H HZ2  . LYS   B 1 16  ? 26.235 -6.449  28.26   1 71.552  ? 28  LYS   A HZ2  1 c 2 
ATOM   2027 H HZ3  . LYS   B 1 16  ? 26.06  -5.573  27.085  1 71.215  ? 28  LYS   A HZ3  1 c 2 
ATOM   2028 N N    . LYS   B 1 17  ? 22.671 -6.996  34.958  1 41.076  ? 29  LYS   A N    1 ? 2 
ATOM   2029 C CA   . LYS   B 1 17  ? 21.836 -6.499  36.038  1 42.926  ? 29  LYS   A CA   1 ? 2 
ATOM   2030 C C    . LYS   B 1 17  ? 21.312 -5.105  35.68   1 41.633  ? 29  LYS   A C    1 ? 2 
ATOM   2031 O O    . LYS   B 1 17  ? 21.464 -4.18   36.445  1 41.198  ? 29  LYS   A O    1 ? 2 
ATOM   2032 C CB   . LYS   B 1 17  ? 22.588 -6.524  37.38   1 44.515  ? 29  LYS   A CB   1 ? 2 
ATOM   2033 C CG   . LYS   B 1 17  ? 22.833 -7.903  37.968  1 44.597  ? 29  LYS   A CG   1 ? 2 
ATOM   2034 C CD   . LYS   B 1 17  ? 21.556 -8.596  38.407  1 45.587  ? 29  LYS   A CD   1 ? 2 
ATOM   2035 C CE   . LYS   B 1 17  ? 21.762 -10.002 38.948  1 51.605  ? 29  LYS   A CE   1 ? 2 
ATOM   2036 N NZ   . LYS   B 1 17  ? 21.648 -11.028 37.898  1 49.344  ? 29  LYS   A NZ   1 ? 2 
ATOM   2037 H H    . LYS   B 1 17  ? 22.449 -7.795  34.575  1 41.146  ? 29  LYS   A H    1 c 2 
ATOM   2038 H HA   . LYS   B 1 17  ? 21.058 -7.103  36.115  1 41.093  ? 29  LYS   A HA   1 c 2 
ATOM   2039 H HB2  . LYS   B 1 17  ? 23.455 -6.081  37.265  1 46.05   ? 29  LYS   A HB2  1 c 2 
ATOM   2040 H HB3  . LYS   B 1 17  ? 22.076 -6.002  38.034  1 45.131  ? 29  LYS   A HB3  1 c 2 
ATOM   2041 H HG2  . LYS   B 1 17  ? 23.285 -8.457  37.295  1 44.818  ? 29  LYS   A HG2  1 c 2 
ATOM   2042 H HG3  . LYS   B 1 17  ? 23.433 -7.814  38.74   1 47.345  ? 29  LYS   A HG3  1 c 2 
ATOM   2043 H HD2  . LYS   B 1 17  ? 21.126 -8.05   39.101  1 46.763  ? 29  LYS   A HD2  1 c 2 
ATOM   2044 H HD3  . LYS   B 1 17  ? 20.942 -8.64   37.644  1 44.224  ? 29  LYS   A HD3  1 c 2 
ATOM   2045 H HE2  . LYS   B 1 17  ? 22.644 -10.066 39.358  1 52.065  ? 29  LYS   A HE2  1 c 2 
ATOM   2046 H HE3  . LYS   B 1 17  ? 21.097 -10.182 39.637  1 50.331  ? 29  LYS   A HE3  1 c 2 
ATOM   2047 H HZ1  . LYS   B 1 17  ? 22.258 -10.869 37.247  1 49.489  ? 29  LYS   A HZ1  1 c 2 
ATOM   2048 H HZ2  . LYS   B 1 17  ? 20.817 -11.009 37.539  1 47.892  ? 29  LYS   A HZ2  1 c 2 
ATOM   2049 H HZ3  . LYS   B 1 17  ? 21.8   -11.848 38.253  1 50.194  ? 29  LYS   A HZ3  1 c 2 
ATOM   2050 N N    . ASP   B 1 18  ? 20.635 -4.988  34.541  1 41.862  ? 30  ASP   A N    1 ? 2 
ATOM   2051 C CA   . ASP   B 1 18  ? 20.065 -3.734  34.083  1 42.825  ? 30  ASP   A CA   1 ? 2 
ATOM   2052 C C    . ASP   B 1 18  ? 18.533 -3.759  34.162  1 42.102  ? 30  ASP   A C    1 ? 2 
ATOM   2053 O O    . ASP   B 1 18  ? 17.875 -2.849  33.674  1 41.385  ? 30  ASP   A O    1 ? 2 
ATOM   2054 C CB   . ASP   B 1 18  ? 20.538 -3.464  32.667  1 42.379  ? 30  ASP   A CB   1 ? 2 
ATOM   2055 C CG   . ASP   B 1 18  ? 20.102 -4.503  31.647  1 39.56   ? 30  ASP   A CG   1 ? 2 
ATOM   2056 O OD1  . ASP   B 1 18  ? 19.152 -5.288  31.956  1 38.969  ? 30  ASP   A OD1  1 ? 2 
ATOM   2057 O OD2  . ASP   B 1 18  ? 20.721 -4.542  30.563  1 39.735  ? 30  ASP   A OD2  1 ? 2 
ATOM   2058 H H    . ASP   B 1 18  ? 20.519 -5.733  34.023  1 40.473  ? 30  ASP   A H    1 c 2 
ATOM   2059 H HA   . ASP   B 1 18  ? 20.397 -3.008  34.658  1 44.237  ? 30  ASP   A HA   1 c 2 
ATOM   2060 H HB2  . ASP   B 1 18  ? 20.201 -2.59   32.379  1 42.216  ? 30  ASP   A HB2  1 c 2 
ATOM   2061 H HB3  . ASP   B 1 18  ? 21.518 -3.425  32.664  1 43.331  ? 30  ASP   A HB3  1 c 2 
ATOM   2062 N N    . ARG   B 1 19  ? 17.948 -4.807  34.754  1 41.804  ? 31  ARG   A N    1 ? 2 
ATOM   2063 C CA   . ARG   B 1 19  ? 16.491 -4.917  34.917  1 39.363  ? 31  ARG   A CA   1 ? 2 
ATOM   2064 C C    . ARG   B 1 19  ? 15.757 -4.947  33.572  1 34.788  ? 31  ARG   A C    1 ? 2 
ATOM   2065 O O    . ARG   B 1 19  ? 14.582 -4.626  33.508  1 34.922  ? 31  ARG   A O    1 ? 2 
ATOM   2066 C CB   . ARG   B 1 19  ? 15.895 -3.812  35.8    1 40.777  ? 31  ARG   A CB   1 ? 2 
ATOM   2067 C CG   . ARG   B 1 19  ? 16.828 -3.424  36.933  1 46.515  ? 31  ARG   A CG   1 ? 2 
ATOM   2068 C CD   . ARG   B 1 19  ? 16.274 -3.431  38.312  1 49.224  ? 31  ARG   A CD   1 ? 2 
ATOM   2069 N NE   . ARG   B 1 19  ? 14.918 -2.902  38.441  1 50.734  ? 31  ARG   A NE   1 ? 2 
ATOM   2070 C CZ   . ARG   B 1 19  ? 13.975 -3.499  39.158  1 52.533  ? 31  ARG   A CZ   1 ? 2 
ATOM   2071 N NH1  . ARG   B 1 19  ? 14.232 -4.562  39.919  1 47.945  ? 31  ARG   A NH1  1 ? 2 
ATOM   2072 N NH2  . ARG   B 1 19  ? 12.766 -2.977  39.159  1 57.49   ? 31  ARG   A NH2  1 ? 2 
ATOM   2073 H H    . ARG   B 1 19  ? 18.472 -5.484  35.072  1 41.715  ? 31  ARG   A H    1 c 2 
ATOM   2074 H HA   . ARG   B 1 19  ? 16.308 -5.777  35.373  1 38.949  ? 31  ARG   A HA   1 c 2 
ATOM   2075 H HB2  . ARG   B 1 19  ? 15.713 -3.02   35.251  1 41.424  ? 31  ARG   A HB2  1 c 2 
ATOM   2076 H HB3  . ARG   B 1 19  ? 15.044 -4.123  36.175  1 41.362  ? 31  ARG   A HB3  1 c 2 
ATOM   2077 H HG2  . ARG   B 1 19  ? 17.603 -4.025  36.918  1 46.014  ? 31  ARG   A HG2  1 c 2 
ATOM   2078 H HG3  . ARG   B 1 19  ? 17.175 -2.525  36.748  1 46.769  ? 31  ARG   A HG3  1 c 2 
ATOM   2079 H HD2  . ARG   B 1 19  ? 16.287 -4.355  38.628  1 49.076  ? 31  ARG   A HD2  1 c 2 
ATOM   2080 H HD3  . ARG   B 1 19  ? 16.872 -2.914  38.89   1 51.09   ? 31  ARG   A HD3  1 c 2 
ATOM   2081 H HE   . ARG   B 1 19  ? 14.722 -2.162  38.027  1 50.843  ? 31  ARG   A HE   1 c 2 
ATOM   2082 H HH11 . ARG   B 1 19  ? 14.913 -4.548  40.484  1 50.68   ? 31  ARG   A HH11 1 c 2 
ATOM   2083 H HH12 . ARG   B 1 19  ? 13.715 -5.278  39.858  1 48.563  ? 31  ARG   A HH12 1 c 2 
ATOM   2084 H HH21 . ARG   B 1 19  ? 12.645 -2.136  38.913  1 56.252  ? 31  ARG   A HH21 1 c 2 
ATOM   2085 H HH22 . ARG   B 1 19  ? 12.078 -3.47   39.411  1 55.624  ? 31  ARG   A HH22 1 c 2 
ATOM   2086 N N    . GLY   B 1 20  ? 16.42  -5.415  32.514  1 33.971  ? 32  GLY   A N    1 ? 2 
ATOM   2087 C CA   . GLY   B 1 20  ? 15.781 -5.571  31.207  1 33.74   ? 32  GLY   A CA   1 ? 2 
ATOM   2088 C C    . GLY   B 1 20  ? 14.86  -6.8    31.157  1 36.588  ? 32  GLY   A C    1 ? 2 
ATOM   2089 O O    . GLY   B 1 20  ? 14.024 -6.9    30.259  1 34.644  ? 32  GLY   A O    1 ? 2 
ATOM   2090 H H    . GLY   B 1 20  ? 17.296 -5.66   32.603  1 34.825  ? 32  GLY   A H    1 c 2 
ATOM   2091 H HA2  . GLY   B 1 20  ? 15.257 -4.76   31.006  1 34.336  ? 32  GLY   A HA2  1 c 2 
ATOM   2092 H HA3  . GLY   B 1 20  ? 16.479 -5.657  30.519  1 34.215  ? 32  GLY   A HA3  1 c 2 
ATOM   2093 N N    . VAL   B 1 21  ? 15.038 -7.73   32.12   1 36.165  ? 33  VAL   A N    1 ? 2 
ATOM   2094 C CA   . VAL   B 1 21  ? 14.234 -8.934  32.2    1 35.035  ? 33  VAL   A CA   1 ? 2 
ATOM   2095 C C    . VAL   B 1 21  ? 13.932 -9.23   33.664  1 38.361  ? 33  VAL   A C    1 ? 2 
ATOM   2096 O O    . VAL   B 1 21  ? 14.835 -9.674  34.384  1 34.668  ? 33  VAL   A O    1 ? 2 
ATOM   2097 C CB   . VAL   B 1 21  ? 14.817 -10.186 31.52   1 32.852  ? 33  VAL   A CB   1 ? 2 
ATOM   2098 C CG1  . VAL   B 1 21  ? 13.839 -11.354 31.604  1 32.936  ? 33  VAL   A CG1  1 ? 2 
ATOM   2099 C CG2  . VAL   B 1 21  ? 15.137 -9.926  30.053  1 32.128  ? 33  VAL   A CG2  1 ? 2 
ATOM   2100 H H    . VAL   B 1 21  ? 15.692 -7.603  32.745  1 36.983  ? 33  VAL   A H    1 c 2 
ATOM   2101 H HA   . VAL   B 1 21  ? 13.385 -8.741  31.76   1 34.716  ? 33  VAL   A HA   1 c 2 
ATOM   2102 H HB   . VAL   B 1 21  ? 15.648 -10.427 31.992  1 33.915  ? 33  VAL   A HB   1 c 2 
ATOM   2103 H HG11 . VAL   B 1 21  ? 12.974 -11.078 31.259  1 32.381  ? 33  VAL   A HG11 1 c 2 
ATOM   2104 H HG12 . VAL   B 1 21  ? 13.744 -11.635 32.529  1 33.368  ? 33  VAL   A HG12 1 c 2 
ATOM   2105 H HG13 . VAL   B 1 21  ? 14.175 -12.097 31.075  1 32.735  ? 33  VAL   A HG13 1 c 2 
ATOM   2106 H HG21 . VAL   B 1 21  ? 15.454 -10.747 29.639  1 32.176  ? 33  VAL   A HG21 1 c 2 
ATOM   2107 H HG22 . VAL   B 1 21  ? 15.826 -9.245  29.986  1 32.588  ? 33  VAL   A HG22 1 c 2 
ATOM   2108 H HG23 . VAL   B 1 21  ? 14.336 -9.622  29.595  1 31.698  ? 33  VAL   A HG23 1 c 2 
ATOM   2109 N N    . LEU   B 1 22  ? 12.639 -9.053  34.024  1 37.189  ? 34  LEU   A N    1 ? 2 
ATOM   2110 C CA   . LEU   B 1 22  ? 12.152 -9.244  35.376  1 40.454  ? 34  LEU   A CA   1 ? 2 
ATOM   2111 C C    . LEU   B 1 22  ? 11.234 -10.454 35.396  1 36.852  ? 34  LEU   A C    1 ? 2 
ATOM   2112 O O    . LEU   B 1 22  ? 10.366 -10.549 34.555  1 33.493  ? 34  LEU   A O    1 ? 2 
ATOM   2113 C CB   . LEU   B 1 22  ? 11.438 -7.964  35.794  1 41.19   ? 34  LEU   A CB   1 ? 2 
ATOM   2114 C CG   . LEU   B 1 22  ? 12.328 -6.717  35.858  1 45.385  ? 34  LEU   A CG   1 ? 2 
ATOM   2115 C CD1  . LEU   B 1 22  ? 11.515 -5.521  36.342  1 45.436  ? 34  LEU   A CD1  1 ? 2 
ATOM   2116 C CD2  . LEU   B 1 22  ? 13.549 -6.903  36.778  1 49.4    ? 34  LEU   A CD2  1 ? 2 
ATOM   2117 H H    . LEU   B 1 22  ? 12.038 -8.8    33.384  1 37.356  ? 34  LEU   A H    1 c 2 
ATOM   2118 H HA   . LEU   B 1 22  ? 12.92  -9.407  35.974  1 40.133  ? 34  LEU   A HA   1 c 2 
ATOM   2119 H HB2  . LEU   B 1 22  ? 10.708 -7.794  35.156  1 41.317  ? 34  LEU   A HB2  1 c 2 
ATOM   2120 H HB3  . LEU   B 1 22  ? 11.041 -8.109  36.683  1 42.813  ? 34  LEU   A HB3  1 c 2 
ATOM   2121 H HG   . LEU   B 1 22  ? 12.655 -6.519  34.942  1 44.166  ? 34  LEU   A HG   1 c 2 
ATOM   2122 H HD11 . LEU   B 1 22  ? 10.738 -5.401  35.77   1 45.189  ? 34  LEU   A HD11 1 c 2 
ATOM   2123 H HD12 . LEU   B 1 22  ? 12.064 -4.719  36.312  1 46.334  ? 34  LEU   A HD12 1 c 2 
ATOM   2124 H HD13 . LEU   B 1 22  ? 11.222 -5.678  37.255  1 46.765  ? 34  LEU   A HD13 1 c 2 
ATOM   2125 H HD21 . LEU   B 1 22  ? 14.184 -7.505  36.356  1 47.862  ? 34  LEU   A HD21 1 c 2 
ATOM   2126 H HD22 . LEU   B 1 22  ? 13.262 -7.278  37.627  1 49.31   ? 34  LEU   A HD22 1 c 2 
ATOM   2127 H HD23 . LEU   B 1 22  ? 13.974 -6.043  36.931  1 49.262  ? 34  LEU   A HD23 1 c 2 
ATOM   2128 N N    . LYS   B 1 23  ? 11.46  -11.388 36.341  1 38.841  ? 35  LYS   A N    1 ? 2 
ATOM   2129 C CA   . LYS   B 1 23  ? 10.777 -12.675 36.361  1 35.789  ? 35  LYS   A CA   1 ? 2 
ATOM   2130 C C    . LYS   B 1 23  ? 10.032 -12.869 37.681  1 37.32   ? 35  LYS   A C    1 ? 2 
ATOM   2131 O O    . LYS   B 1 23  ? 10.579 -12.565 38.743  1 38.169  ? 35  LYS   A O    1 ? 2 
ATOM   2132 C CB   . LYS   B 1 23  ? 11.809 -13.798 36.238  1 35.797  ? 35  LYS   A CB   1 ? 2 
ATOM   2133 C CG   . LYS   B 1 23  ? 11.245 -15.218 36.434  1 35.346  ? 35  LYS   A CG   1 ? 2 
ATOM   2134 C CD   . LYS   B 1 23  ? 12.245 -16.34  36.661  1 33.586  ? 35  LYS   A CD   1 ? 2 
ATOM   2135 C CE   . LYS   B 1 23  ? 11.515 -17.674 36.573  1 35.265  ? 35  LYS   A CE   1 ? 2 
ATOM   2136 N NZ   . LYS   B 1 23  ? 12.339 -18.863 36.888  1 34.668  ? 35  LYS   A NZ   1 ? 2 
ATOM   2137 H H    . LYS   B 1 23  ? 12.067 -11.209 37.001  1 38.717  ? 35  LYS   A H    1 c 2 
ATOM   2138 H HA   . LYS   B 1 23  ? 10.139 -12.715 35.609  1 35.638  ? 35  LYS   A HA   1 c 2 
ATOM   2139 H HB2  . LYS   B 1 23  ? 12.22  -13.748 35.35   1 34.869  ? 35  LYS   A HB2  1 c 2 
ATOM   2140 H HB3  . LYS   B 1 23  ? 12.515 -13.651 36.903  1 36.422  ? 35  LYS   A HB3  1 c 2 
ATOM   2141 H HG2  . LYS   B 1 23  ? 10.631 -15.2   37.198  1 35.696  ? 35  LYS   A HG2  1 c 2 
ATOM   2142 H HG3  . LYS   B 1 23  ? 10.707 -15.439 35.642  1 34.218  ? 35  LYS   A HG3  1 c 2 
ATOM   2143 H HD2  . LYS   B 1 23  ? 12.948 -16.305 35.976  1 33.923  ? 35  LYS   A HD2  1 c 2 
ATOM   2144 H HD3  . LYS   B 1 23  ? 12.655 -16.248 37.548  1 35.436  ? 35  LYS   A HD3  1 c 2 
ATOM   2145 H HE2  . LYS   B 1 23  ? 10.757 -17.655 37.184  1 35.074  ? 35  LYS   A HE2  1 c 2 
ATOM   2146 H HE3  . LYS   B 1 23  ? 11.161 -17.777 35.671  1 33.743  ? 35  LYS   A HE3  1 c 2 
ATOM   2147 H HZ1  . LYS   B 1 23  ? 12.632 -18.814 37.744  1 36.188  ? 35  LYS   A HZ1  1 c 2 
ATOM   2148 H HZ2  . LYS   B 1 23  ? 13.051 -18.897 36.33   1 34.957  ? 35  LYS   A HZ2  1 c 2 
ATOM   2149 H HZ3  . LYS   B 1 23  ? 11.845 -19.614 36.784  1 35.624  ? 35  LYS   A HZ3  1 c 2 
ATOM   2150 N N    . ILE   B 1 24  ? 8.808  -13.415 37.594  1 38.15   ? 36  ILE   A N    1 ? 2 
ATOM   2151 C CA   . ILE   B 1 24  ? 8.109  -13.921 38.757  1 40.345  ? 36  ILE   A CA   1 ? 2 
ATOM   2152 C C    . ILE   B 1 24  ? 7.689  -15.371 38.542  1 41.575  ? 36  ILE   A C    1 ? 2 
ATOM   2153 O O    . ILE   B 1 24  ? 7.095  -15.703 37.525  1 40.68   ? 36  ILE   A O    1 ? 2 
ATOM   2154 C CB   . ILE   B 1 24  ? 6.884  -13.066 39.079  1 42.425  ? 36  ILE   A CB   1 ? 2 
ATOM   2155 C CG1  . ILE   B 1 24  ? 7.263  -11.602 39.158  1 41.702  ? 36  ILE   A CG1  1 ? 2 
ATOM   2156 C CG2  . ILE   B 1 24  ? 6.189  -13.597 40.348  1 42.653  ? 36  ILE   A CG2  1 ? 2 
ATOM   2157 C CD1  . ILE   B 1 24  ? 6.069  -10.686 39.265  1 46.398  ? 36  ILE   A CD1  1 ? 2 
ATOM   2158 H H    . ILE   B 1 24  ? 8.399  -13.47  36.779  1 37.317  ? 36  ILE   A H    1 c 2 
ATOM   2159 H HA   . ILE   B 1 24  ? 8.715  -13.884 39.522  1 41.455  ? 36  ILE   A HA   1 c 2 
ATOM   2160 H HB   . ILE   B 1 24  ? 6.255  -13.164 38.336  1 41.075  ? 36  ILE   A HB   1 c 2 
ATOM   2161 H HG12 . ILE   B 1 24  ? 7.841  -11.465 39.936  1 43.588  ? 36  ILE   A HG12 1 c 2 
ATOM   2162 H HG13 . ILE   B 1 24  ? 7.772  -11.36  38.358  1 41.494  ? 36  ILE   A HG13 1 c 2 
ATOM   2163 H HG21 . ILE   B 1 24  ? 5.446  -13.016 40.582  1 43.929  ? 36  ILE   A HG21 1 c 2 
ATOM   2164 H HG22 . ILE   B 1 24  ? 6.825  -13.617 41.083  1 43.975  ? 36  ILE   A HG22 1 c 2 
ATOM   2165 H HG23 . ILE   B 1 24  ? 5.854  -14.495 40.188  1 43.248  ? 36  ILE   A HG23 1 c 2 
ATOM   2166 H HD11 . ILE   B 1 24  ? 5.411  -10.921 38.584  1 44.677  ? 36  ILE   A HD11 1 c 2 
ATOM   2167 H HD12 . ILE   B 1 24  ? 6.36   -9.765  39.13   1 45.198  ? 36  ILE   A HD12 1 c 2 
ATOM   2168 H HD13 . ILE   B 1 24  ? 5.665  -10.77  40.15   1 46.623  ? 36  ILE   A HD13 1 c 2 
ATOM   2169 N N    . VAL   B 1 25  ? 7.9    -16.192 39.581  1 39.959  ? 37  VAL   A N    1 ? 2 
ATOM   2170 C CA   . VAL   B 1 25  ? 7.439  -17.565 39.59   1 38.629  ? 37  VAL   A CA   1 ? 2 
ATOM   2171 C C    . VAL   B 1 25  ? 5.989  -17.52  40.062  1 39.292  ? 37  VAL   A C    1 ? 2 
ATOM   2172 O O    . VAL   B 1 25  ? 5.725  -17.06  41.16   1 37.514  ? 37  VAL   A O    1 ? 2 
ATOM   2173 C CB   . VAL   B 1 25  ? 8.28   -18.49  40.506  1 38.28   ? 37  VAL   A CB   1 ? 2 
ATOM   2174 C CG1  . VAL   B 1 25  ? 7.767  -19.929 40.463  1 35.44   ? 37  VAL   A CG1  1 ? 2 
ATOM   2175 C CG2  . VAL   B 1 25  ? 9.777  -18.435 40.177  1 38.456  ? 37  VAL   A CG2  1 ? 2 
ATOM   2176 H H    . VAL   B 1 25  ? 8.35   -15.879 40.312  1 40.963  ? 37  VAL   A H    1 c 2 
ATOM   2177 H HA   . VAL   B 1 25  ? 7.468  -17.914 38.678  1 37.721  ? 37  VAL   A HA   1 c 2 
ATOM   2178 H HB   . VAL   B 1 25  ? 8.167  -18.162 41.429  1 39.099  ? 37  VAL   A HB   1 c 2 
ATOM   2179 H HG11 . VAL   B 1 25  ? 7.718  -20.228 39.539  1 35.575  ? 37  VAL   A HG11 1 c 2 
ATOM   2180 H HG12 . VAL   B 1 25  ? 6.884  -19.974 40.865  1 37.372  ? 37  VAL   A HG12 1 c 2 
ATOM   2181 H HG13 . VAL   B 1 25  ? 8.375  -20.504 40.956  1 37.513  ? 37  VAL   A HG13 1 c 2 
ATOM   2182 H HG21 . VAL   B 1 25  ? 10.261 -19.042 40.762  1 39.414  ? 37  VAL   A HG21 1 c 2 
ATOM   2183 H HG22 . VAL   B 1 25  ? 10.106 -17.53  40.308  1 37.888  ? 37  VAL   A HG22 1 c 2 
ATOM   2184 H HG23 . VAL   B 1 25  ? 9.916  -18.698 39.252  1 37.18   ? 37  VAL   A HG23 1 c 2 
ATOM   2185 N N    . LYS   B 1 26  ? 5.066  -18.036 39.242  1 41.46   ? 38  LYS   A N    1 ? 2 
ATOM   2186 C CA   . LYS   B 1 26  ? 3.648  -18.026 39.553  1 44.205  ? 38  LYS   A CA   1 ? 2 
ATOM   2187 C C    . LYS   B 1 26  ? 3.169  -19.417 39.979  1 47.939  ? 38  LYS   A C    1 ? 2 
ATOM   2188 O O    . LYS   B 1 26  ? 2.282  -19.525 40.809  1 50.215  ? 38  LYS   A O    1 ? 2 
ATOM   2189 C CB   . LYS   B 1 26  ? 2.906  -17.412 38.359  1 45.829  ? 38  LYS   A CB   1 ? 2 
ATOM   2190 C CG   . LYS   B 1 26  ? 3.247  -15.94  38.079  1 44.772  ? 38  LYS   A CG   1 ? 2 
ATOM   2191 C CD   . LYS   B 1 26  ? 3.038  -14.948 39.232  1 45.824  ? 38  LYS   A CD   1 ? 2 
ATOM   2192 C CE   . LYS   B 1 26  ? 1.614  -14.739 39.551  1 46.043  ? 38  LYS   A CE   1 ? 2 
ATOM   2193 N NZ   . LYS   B 1 26  ? 1.451  -13.924 40.75   1 48.149  ? 38  LYS   A NZ   1 ? 2 
ATOM   2194 H H    . LYS   B 1 26  ? 5.335  -18.407 38.451  1 40.297  ? 38  LYS   A H    1 c 2 
ATOM   2195 H HA   . LYS   B 1 26  ? 3.51   -17.421 40.323  1 45.478  ? 38  LYS   A HA   1 c 2 
ATOM   2196 H HB2  . LYS   B 1 26  ? 3.115  -17.937 37.556  1 44.494  ? 38  LYS   A HB2  1 c 2 
ATOM   2197 H HB3  . LYS   B 1 26  ? 1.94   -17.483 38.517  1 46.358  ? 38  LYS   A HB3  1 c 2 
ATOM   2198 H HG2  . LYS   B 1 26  ? 4.187  -15.895 37.796  1 43.564  ? 38  LYS   A HG2  1 c 2 
ATOM   2199 H HG3  . LYS   B 1 26  ? 2.705  -15.647 37.319  1 44.156  ? 38  LYS   A HG3  1 c 2 
ATOM   2200 H HD2  . LYS   B 1 26  ? 3.502  -15.276 40.032  1 46.171  ? 38  LYS   A HD2  1 c 2 
ATOM   2201 H HD3  . LYS   B 1 26  ? 3.439  -14.086 38.986  1 44.687  ? 38  LYS   A HD3  1 c 2 
ATOM   2202 H HE2  . LYS   B 1 26  ? 1.175  -14.295 38.803  1 45.998  ? 38  LYS   A HE2  1 c 2 
ATOM   2203 H HE3  . LYS   B 1 26  ? 1.179  -15.599 39.692  1 47.346  ? 38  LYS   A HE3  1 c 2 
ATOM   2204 H HZ1  . LYS   B 1 26  ? 1.875  -13.131 40.642  1 47.389  ? 38  LYS   A HZ1  1 c 2 
ATOM   2205 H HZ2  . LYS   B 1 26  ? 1.806  -14.356 41.464  1 48.71   ? 38  LYS   A HZ2  1 c 2 
ATOM   2206 H HZ3  . LYS   B 1 26  ? 0.571  -13.774 40.901  1 49.207  ? 38  LYS   A HZ3  1 c 2 
ATOM   2207 N N    . ARG   B 1 27  ? 3.702  -20.49  39.389  1 46.043  ? 39  ARG   A N    1 ? 2 
ATOM   2208 C CA   . ARG   B 1 27  ? 3.505  -21.831 39.915  1 45.784  ? 39  ARG   A CA   1 ? 2 
ATOM   2209 C C    . ARG   B 1 27  ? 4.876  -22.493 39.933  1 45.447  ? 39  ARG   A C    1 ? 2 
ATOM   2210 O O    . ARG   B 1 27  ? 5.59   -22.478 38.925  1 41.418  ? 39  ARG   A O    1 ? 2 
ATOM   2211 C CB   . ARG   B 1 27  ? 2.502  -22.671 39.113  1 48.599  ? 39  ARG   A CB   1 ? 2 
ATOM   2212 C CG   . ARG   B 1 27  ? 2.063  -23.988 39.737  1 51.47   ? 39  ARG   A CG   1 ? 2 
ATOM   2213 C CD   . ARG   B 1 27  ? 1.139  -24.847 38.852  1 52.604  ? 39  ARG   A CD   1 ? 2 
ATOM   2214 N NE   . ARG   B 1 27  ? 1.824  -25.319 37.636  1 51.786  ? 39  ARG   A NE   1 ? 2 
ATOM   2215 C CZ   . ARG   B 1 27  ? 1.246  -25.656 36.472  1 49.469  ? 39  ARG   A CZ   1 ? 2 
ATOM   2216 N NH1  . ARG   B 1 27  ? -0.057 -25.668 36.343  1 49.414  ? 39  ARG   A NH1  1 ? 2 
ATOM   2217 N NH2  . ARG   B 1 27  ? 1.982  -25.959 35.423  1 48.683  ? 39  ARG   A NH2  1 ? 2 
ATOM   2218 H H    . ARG   B 1 27  ? 4.194  -20.385 38.626  1 44.545  ? 39  ARG   A H    1 c 2 
ATOM   2219 H HA   . ARG   B 1 27  ? 3.177  -21.757 40.846  1 47.963  ? 39  ARG   A HA   1 c 2 
ATOM   2220 H HB2  . ARG   B 1 27  ? 1.703  -22.124 38.956  1 48.241  ? 39  ARG   A HB2  1 c 2 
ATOM   2221 H HB3  . ARG   B 1 27  ? 2.899  -22.864 38.236  1 47.147  ? 39  ARG   A HB3  1 c 2 
ATOM   2222 H HG2  . ARG   B 1 27  ? 2.861  -24.515 39.959  1 51.569  ? 39  ARG   A HG2  1 c 2 
ATOM   2223 H HG3  . ARG   B 1 27  ? 1.599  -23.797 40.581  1 52.624  ? 39  ARG   A HG3  1 c 2 
ATOM   2224 H HD2  . ARG   B 1 27  ? 0.827  -25.619 39.367  1 54.514  ? 39  ARG   A HD2  1 c 2 
ATOM   2225 H HD3  . ARG   B 1 27  ? 0.356  -24.317 38.597  1 52.617  ? 39  ARG   A HD3  1 c 2 
ATOM   2226 H HE   . ARG   B 1 27  ? 2.691  -25.389 37.673  1 50.39   ? 39  ARG   A HE   1 c 2 
ATOM   2227 H HH11 . ARG   B 1 27  ? -0.563 -25.992 36.993  1 51.426  ? 39  ARG   A HH11 1 c 2 
ATOM   2228 H HH12 . ARG   B 1 27  ? -0.426 -25.354 35.603  1 49.442  ? 39  ARG   A HH12 1 c 2 
ATOM   2229 H HH21 . ARG   B 1 27  ? 2.802  -25.635 35.352  1 47.368  ? 39  ARG   A HH21 1 c 2 
ATOM   2230 H HH22 . ARG   B 1 27  ? 1.654  -26.486 34.793  1 49.388  ? 39  ARG   A HH22 1 c 2 
ATOM   2231 N N    . VAL   B 1 28  ? 5.243  -23.03  41.099  1 50.009  ? 40  VAL   A N    1 ? 2 
ATOM   2232 C CA   . VAL   B 1 28  ? 6.512  -23.71  41.291  1 55.23   ? 40  VAL   A CA   1 ? 2 
ATOM   2233 C C    . VAL   B 1 28  ? 6.515  -25.036 40.53   1 54.836  ? 40  VAL   A C    1 ? 2 
ATOM   2234 O O    . VAL   B 1 28  ? 5.531  -25.762 40.537  1 58.162  ? 40  VAL   A O    1 ? 2 
ATOM   2235 C CB   . VAL   B 1 28  ? 6.783  -23.919 42.791  1 57.258  ? 40  VAL   A CB   1 ? 2 
ATOM   2236 C CG1  . VAL   B 1 28  ? 8.066  -24.717 43.028  1 57.17   ? 40  VAL   A CG1  1 ? 2 
ATOM   2237 C CG2  . VAL   B 1 28  ? 6.813  -22.577 43.528  1 54.372  ? 40  VAL   A CG2  1 ? 2 
ATOM   2238 H H    . VAL   B 1 28  ? 4.665  -22.982 41.806  1 51.576  ? 40  VAL   A H    1 c 2 
ATOM   2239 H HA   . VAL   B 1 28  ? 7.218  -23.142 40.929  1 52.633  ? 40  VAL   A HA   1 c 2 
ATOM   2240 H HB   . VAL   B 1 28  ? 6.03   -24.444 43.151  1 58.028  ? 40  VAL   A HB   1 c 2 
ATOM   2241 H HG11 . VAL   B 1 28  ? 8.783  -24.351 42.483  1 56.137  ? 40  VAL   A HG11 1 c 2 
ATOM   2242 H HG12 . VAL   B 1 28  ? 7.92   -25.646 42.791  1 58.347  ? 40  VAL   A HG12 1 c 2 
ATOM   2243 H HG13 . VAL   B 1 28  ? 8.314  -24.66  43.967  1 58.886  ? 40  VAL   A HG13 1 c 2 
ATOM   2244 H HG21 . VAL   B 1 28  ? 7.068  -22.721 44.455  1 56.739  ? 40  VAL   A HG21 1 c 2 
ATOM   2245 H HG22 . VAL   B 1 28  ? 5.933  -22.166 43.497  1 54.975  ? 40  VAL   A HG22 1 c 2 
ATOM   2246 H HG23 . VAL   B 1 28  ? 7.46   -21.988 43.104  1 53.688  ? 40  VAL   A HG23 1 c 2 
ATOM   2247 N N    . GLY   B 1 29  ? 7.643  -25.339 39.88   1 53.813  ? 41  GLY   A N    1 ? 2 
ATOM   2248 C CA   . GLY   B 1 29  ? 7.823  -26.615 39.203  1 59.509  ? 41  GLY   A CA   1 ? 2 
ATOM   2249 C C    . GLY   B 1 29  ? 8.317  -27.695 40.161  1 59.072  ? 41  GLY   A C    1 ? 2 
ATOM   2250 O O    . GLY   B 1 29  ? 8.272  -27.533 41.376  1 63.058  ? 41  GLY   A O    1 ? 2 
ATOM   2251 H H    . GLY   B 1 29  ? 8.324  -24.73  39.856  1 54.031  ? 41  GLY   A H    1 c 2 
ATOM   2252 H HA2  . GLY   B 1 29  ? 6.966  -26.895 38.802  1 57.85   ? 41  GLY   A HA2  1 c 2 
ATOM   2253 H HA3  . GLY   B 1 29  ? 8.475  -26.501 38.472  1 56.563  ? 41  GLY   A HA3  1 c 2 
ATOM   2254 N N    . ASN   B 1 30  ? 8.808  -28.792 39.592  1 63.414  ? 42  ASN   A N    1 ? 2 
ATOM   2255 C CA   . ASN   B 1 30  ? 9.244  -29.956 40.354  1 65.749  ? 42  ASN   A CA   1 ? 2 
ATOM   2256 C C    . ASN   B 1 30  ? 10.561 -30.463 39.772  1 65.491  ? 42  ASN   A C    1 ? 2 
ATOM   2257 O O    . ASN   B 1 30  ? 10.852 -30.269 38.591  1 62.135  ? 42  ASN   A O    1 ? 2 
ATOM   2258 C CB   . ASN   B 1 30  ? 8.163  -31.023 40.327  1 72.898  ? 42  ASN   A CB   1 ? 2 
ATOM   2259 C CG   . ASN   B 1 30  ? 7.721  -31.264 38.905  1 73.923  ? 42  ASN   A CG   1 ? 2 
ATOM   2260 O OD1  . ASN   B 1 30  ? 6.689  -30.736 38.47   1 72.97   ? 42  ASN   A OD1  1 ? 2 
ATOM   2261 N ND2  . ASN   B 1 30  ? 8.565  -31.929 38.134  1 75.293  ? 42  ASN   A ND2  1 ? 2 
ATOM   2262 H H    . ASN   B 1 30  ? 8.886  -28.814 38.682  1 61.61   ? 42  ASN   A H    1 c 2 
ATOM   2263 H HA   . ASN   B 1 30  ? 9.387  -29.692 41.291  1 67.277  ? 42  ASN   A HA   1 c 2 
ATOM   2264 H HB2  . ASN   B 1 30  ? 8.512  -31.854 40.707  1 74.121  ? 42  ASN   A HB2  1 c 2 
ATOM   2265 H HB3  . ASN   B 1 30  ? 7.4    -30.732 40.865  1 72.301  ? 42  ASN   A HB3  1 c 2 
ATOM   2266 H HD21 . ASN   B 1 30  ? 8.615  -31.74  37.268  1 73.902  ? 42  ASN   A HD21 1 c 2 
ATOM   2267 H HD22 . ASN   B 1 30  ? 9.078  -32.564 38.481  1 76.545  ? 42  ASN   A HD22 1 c 2 
ATOM   2268 N N    . GLY   B 1 31  ? 11.355 -31.113 40.62   1 68.237  ? 43  GLY   A N    1 ? 2 
ATOM   2269 C CA   . GLY   B 1 31  ? 12.74  -31.381 40.291  1 72.069  ? 43  GLY   A CA   1 ? 2 
ATOM   2270 C C    . GLY   B 1 31  ? 13.597 -30.185 40.682  1 75.71   ? 43  GLY   A C    1 ? 2 
ATOM   2271 O O    . GLY   B 1 31  ? 13.074 -29.134 41.031  1 76.197  ? 43  GLY   A O    1 ? 2 
ATOM   2272 H H    . GLY   B 1 31  ? 11.025 -31.401 41.422  1 70.324  ? 43  GLY   A H    1 c 2 
ATOM   2273 H HA2  . GLY   B 1 31  ? 13.043 -32.183 40.777  1 74.67   ? 43  GLY   A HA2  1 c 2 
ATOM   2274 H HA3  . GLY   B 1 31  ? 12.825 -31.555 39.324  1 71.581  ? 43  GLY   A HA3  1 c 2 
ATOM   2275 N N    . GLU   B 1 32  ? 14.916 -30.378 40.666  1 84.902  ? 44  GLU   A N    1 ? 2 
ATOM   2276 C CA   . GLU   B 1 32  ? 15.859 -29.294 40.885  1 82.917  ? 44  GLU   A CA   1 ? 2 
ATOM   2277 C C    . GLU   B 1 32  ? 16.708 -29.115 39.629  1 73.183  ? 44  GLU   A C    1 ? 2 
ATOM   2278 O O    . GLU   B 1 32  ? 17.773 -28.518 39.698  1 77.751  ? 44  GLU   A O    1 ? 2 
ATOM   2279 C CB   . GLU   B 1 32  ? 16.714 -29.594 42.121  1 83.303  ? 44  GLU   A CB   1 ? 2 
ATOM   2280 H H    . GLU   B 1 32  ? 15.24  -31.22  40.52   1 84.063  ? 44  GLU   A H    1 c 2 
ATOM   2281 H HA   . GLU   B 1 32  ? 15.352 -28.459 41.044  1 79.271  ? 44  GLU   A HA   1 c 2 
ATOM   2282 H HB2  . GLU   B 1 32  ? 17.584 -29.556 41.964  0 30      ? 44  GLU   A HB2  1 c 2 
ATOM   2283 H HB3  . GLU   B 1 32  ? 15.989 -29.792 42.886  0 30      ? 44  GLU   A HB3  1 c 2 
ATOM   2284 N N    . GLU   B 1 33  ? 16.281 -29.709 38.511  1 67.789  ? 45  GLU   A N    1 ? 2 
ATOM   2285 C CA   . GLU   B 1 33  ? 16.982 -29.569 37.242  1 67.448  ? 45  GLU   A CA   1 ? 2 
ATOM   2286 C C    . GLU   B 1 33  ? 16.261 -28.506 36.411  1 63.324  ? 45  GLU   A C    1 ? 2 
ATOM   2287 O O    . GLU   B 1 33  ? 15.033 -28.528 36.303  1 60.934  ? 45  GLU   A O    1 ? 2 
ATOM   2288 C CB   . GLU   B 1 33  ? 17.079 -30.937 36.55   1 69.512  ? 45  GLU   A CB   1 ? 2 
ATOM   2289 H H    . GLU   B 1 33  ? 15.516 -30.208 38.531  1 69.645  ? 45  GLU   A H    1 c 2 
ATOM   2290 H HA   . GLU   B 1 33  ? 17.903 -29.254 37.427  1 67.668  ? 45  GLU   A HA   1 c 2 
ATOM   2291 H HB2  . GLU   B 1 33  ? 18.099 -31.166 36.508  0 30      ? 45  GLU   A HB2  1 c 2 
ATOM   2292 H HB3  . GLU   B 1 33  ? 16.251 -31.333 36.431  0 30      ? 45  GLU   A HB3  1 c 2 
ATOM   2293 N N    . THR   B 1 34  ? 17.035 -27.572 35.845  1 58.27   ? 46  THR   A N    1 ? 2 
ATOM   2294 C CA   . THR   B 1 34  ? 16.562 -26.683 34.795  1 55.304  ? 46  THR   A CA   1 ? 2 
ATOM   2295 C C    . THR   B 1 34  ? 17.184 -27.102 33.463  1 52.48   ? 46  THR   A C    1 ? 2 
ATOM   2296 O O    . THR   B 1 34  ? 18.165 -27.83  33.444  1 52.864  ? 46  THR   A O    1 ? 2 
ATOM   2297 C CB   . THR   B 1 34  ? 16.955 -25.243 35.136  1 54.612  ? 46  THR   A CB   1 ? 2 
ATOM   2298 O OG1  . THR   B 1 34  ? 18.357 -25.227 34.882  1 53.746  ? 46  THR   A OG1  1 ? 2 
ATOM   2299 C CG2  . THR   B 1 34  ? 16.6   -24.847 36.559  1 56.551  ? 46  THR   A CG2  1 ? 2 
ATOM   2300 H H    . THR   B 1 34  ? 17.899 -27.483 36.13   1 59.977  ? 46  THR   A H    1 c 2 
ATOM   2301 H HA   . THR   B 1 34  ? 15.584 -26.746 34.735  1 54.214  ? 46  THR   A HA   1 c 2 
ATOM   2302 H HB   . THR   B 1 34  ? 16.507 -24.618 34.518  1 52.536  ? 46  THR   A HB   1 c 2 
ATOM   2303 H HG1  . THR   B 1 34  ? 18.725 -25.88  35.352  0 30      ? 46  THR   A HG1  1 c 2 
ATOM   2304 H HG21 . THR   B 1 34  ? 16.792 -23.904 36.69   1 55.061  ? 46  THR   A HG21 1 c 2 
ATOM   2305 H HG22 . THR   B 1 34  ? 17.126 -25.373 37.185  1 57.842  ? 46  THR   A HG22 1 c 2 
ATOM   2306 H HG23 . THR   B 1 34  ? 15.654 -25.01  36.715  1 55.696  ? 46  THR   A HG23 1 c 2 
ATOM   2307 N N    . PRO   B 1 35  ? 16.691 -26.626 32.305  1 49.296  ? 47  PRO   A N    1 ? 2 
ATOM   2308 C CA   . PRO   B 1 35  ? 17.338 -26.944 31.045  1 54.501  ? 47  PRO   A CA   1 ? 2 
ATOM   2309 C C    . PRO   B 1 35  ? 18.752 -26.364 30.897  1 54.043  ? 47  PRO   A C    1 ? 2 
ATOM   2310 O O    . PRO   B 1 35  ? 18.999 -25.207 31.259  1 50.983  ? 47  PRO   A O    1 ? 2 
ATOM   2311 C CB   . PRO   B 1 35  ? 16.377 -26.42  29.991  1 51.434  ? 47  PRO   A CB   1 ? 2 
ATOM   2312 C CG   . PRO   B 1 35  ? 15.42  -25.487 30.699  1 51.246  ? 47  PRO   A CG   1 ? 2 
ATOM   2313 C CD   . PRO   B 1 35  ? 15.499 -25.778 32.164  1 52.682  ? 47  PRO   A CD   1 ? 2 
ATOM   2314 H HA   . PRO   B 1 35  ? 17.386 -27.919 30.958  1 54.931  ? 47  PRO   A HA   1 c 2 
ATOM   2315 H HB2  . PRO   B 1 35  ? 16.862 -25.949 29.289  1 51.506  ? 47  PRO   A HB2  1 c 2 
ATOM   2316 H HB3  . PRO   B 1 35  ? 15.89  -27.159 29.577  1 52.98   ? 47  PRO   A HB3  1 c 2 
ATOM   2317 H HG2  . PRO   B 1 35  ? 15.664 -24.555 30.527  1 49.633  ? 47  PRO   A HG2  1 c 2 
ATOM   2318 H HG3  . PRO   B 1 35  ? 14.507 -25.629 30.377  1 50.579  ? 47  PRO   A HG3  1 c 2 
ATOM   2319 H HD2  . PRO   B 1 35  ? 15.601 -24.955 32.675  1 50.103  ? 47  PRO   A HD2  1 c 2 
ATOM   2320 H HD3  . PRO   B 1 35  ? 14.702 -26.251 32.474  1 51.458  ? 47  PRO   A HD3  1 c 2 
ATOM   2321 N N    . MET   B 1 36  ? 19.64  -27.194 30.334  1 57.715  ? 48  MET   A N    1 ? 2 
ATOM   2322 C CA   . MET   B 1 36  ? 20.96  -26.785 29.875  1 58.564  ? 48  MET   A CA   1 ? 2 
ATOM   2323 C C    . MET   B 1 36  ? 20.86  -26.216 28.461  1 53.834  ? 48  MET   A C    1 ? 2 
ATOM   2324 O O    . MET   B 1 36  ? 19.948 -26.545 27.705  1 48.943  ? 48  MET   A O    1 ? 2 
ATOM   2325 C CB   . MET   B 1 36  ? 21.918 -27.974 29.762  1 64.407  ? 48  MET   A CB   1 ? 2 
ATOM   2326 C CG   . MET   B 1 36  ? 22.093 -28.838 30.996  1 69.926  ? 48  MET   A CG   1 ? 2 
ATOM   2327 S SD   . MET   B 1 36  ? 23.203 -28.16  32.25   1 77.175  ? 48  MET   A SD   1 ? 2 
ATOM   2328 C CE   . MET   B 1 36  ? 21.973 -27.43  33.338  1 79.125  ? 48  MET   A CE   1 ? 2 
ATOM   2329 H H    . MET   B 1 36  ? 19.405 -28.07  30.229  1 58.774  ? 48  MET   A H    1 c 2 
ATOM   2330 H HA   . MET   B 1 36  ? 21.328 -26.101 30.492  1 57.718  ? 48  MET   A HA   1 c 2 
ATOM   2331 H HB2  . MET   B 1 36  ? 21.604 -28.546 29.03   1 65.132  ? 48  MET   A HB2  1 c 2 
ATOM   2332 H HB3  . MET   B 1 36  ? 22.799 -27.628 29.502  1 65.164  ? 48  MET   A HB3  1 c 2 
ATOM   2333 H HG2  . MET   B 1 36  ? 21.218 -28.984 31.407  1 69.342  ? 48  MET   A HG2  1 c 2 
ATOM   2334 H HG3  . MET   B 1 36  ? 22.437 -29.711 30.722  1 72.405  ? 48  MET   A HG3  1 c 2 
ATOM   2335 H HE1  . MET   B 1 36  ? 22.419 -27.025 34.104  1 78.349  ? 48  MET   A HE1  1 c 2 
ATOM   2336 H HE2  . MET   B 1 36  ? 21.472 -26.75  32.852  1 75.763  ? 48  MET   A HE2  1 c 2 
ATOM   2337 H HE3  . MET   B 1 36  ? 21.363 -28.124 33.649  1 78.465  ? 48  MET   A HE3  1 c 2 
ATOM   2338 N N    . ILE   B 1 37  ? 21.834 -25.375 28.103  1 55.944  ? 49  ILE   A N    1 ? 2 
ATOM   2339 C CA   . ILE   B 1 37  ? 21.913 -24.796 26.768  1 56.281  ? 49  ILE   A CA   1 ? 2 
ATOM   2340 C C    . ILE   B 1 37  ? 21.954 -25.923 25.745  1 53.905  ? 49  ILE   A C    1 ? 2 
ATOM   2341 O O    . ILE   B 1 37  ? 22.74  -26.859 25.89   1 53.638  ? 49  ILE   A O    1 ? 2 
ATOM   2342 C CB   . ILE   B 1 37  ? 23.144 -23.875 26.611  1 62.932  ? 49  ILE   A CB   1 ? 2 
ATOM   2343 C CG1  . ILE   B 1 37  ? 23.175 -22.731 27.628  1 66.962  ? 49  ILE   A CG1  1 ? 2 
ATOM   2344 C CG2  . ILE   B 1 37  ? 23.241 -23.331 25.185  1 60.86   ? 49  ILE   A CG2  1 ? 2 
ATOM   2345 C CD1  . ILE   B 1 37  ? 21.942 -21.841 27.611  1 67.677  ? 49  ILE   A CD1  1 ? 2 
ATOM   2346 H H    . ILE   B 1 37  ? 22.481 -25.163 28.712  1 56.45   ? 49  ILE   A H    1 c 2 
ATOM   2347 H HA   . ILE   B 1 37  ? 21.108 -24.265 26.615  1 54.416  ? 49  ILE   A HA   1 c 2 
ATOM   2348 H HB   . ILE   B 1 37  ? 23.938 -24.424 26.769  1 64.419  ? 49  ILE   A HB   1 c 2 
ATOM   2349 H HG12 . ILE   B 1 37  ? 23.275 -23.108 28.525  1 66.919  ? 49  ILE   A HG12 1 c 2 
ATOM   2350 H HG13 . ILE   B 1 37  ? 23.963 -22.176 27.451  1 66.791  ? 49  ILE   A HG13 1 c 2 
ATOM   2351 H HG21 . ILE   B 1 37  ? 23.929 -22.645 25.144  1 61.457  ? 49  ILE   A HG21 1 c 2 
ATOM   2352 H HG22 . ILE   B 1 37  ? 22.388 -22.946 24.924  1 59.601  ? 49  ILE   A HG22 1 c 2 
ATOM   2353 H HG23 . ILE   B 1 37  ? 23.47  -24.051 24.574  1 62.949  ? 49  ILE   A HG23 1 c 2 
ATOM   2354 H HD11 . ILE   B 1 37  ? 21.8   -21.492 26.711  1 65.79   ? 49  ILE   A HD11 1 c 2 
ATOM   2355 H HD12 . ILE   B 1 37  ? 22.074 -21.097 28.228  1 65.763  ? 49  ILE   A HD12 1 c 2 
ATOM   2356 H HD13 . ILE   B 1 37  ? 21.158 -22.353 27.887  1 65.949  ? 49  ILE   A HD13 1 c 2 
ATOM   2357 N N    . GLY   B 1 38  ? 21.115 -25.821 24.709  1 52.947  ? 50  GLY   A N    1 ? 2 
ATOM   2358 C CA   . GLY   B 1 38  ? 21.103 -26.822 23.65   1 55.668  ? 50  GLY   A CA   1 ? 2 
ATOM   2359 C C    . GLY   B 1 38  ? 19.992 -27.858 23.822  1 55.308  ? 50  GLY   A C    1 ? 2 
ATOM   2360 O O    . GLY   B 1 38  ? 19.665 -28.568 22.867  1 57.131  ? 50  GLY   A O    1 ? 2 
ATOM   2361 H H    . GLY   B 1 38  ? 20.537 -25.114 24.658  1 51.225  ? 50  GLY   A H    1 c 2 
ATOM   2362 H HA2  . GLY   B 1 38  ? 20.987 -26.365 22.785  1 54.878  ? 50  GLY   A HA2  1 c 2 
ATOM   2363 H HA3  . GLY   B 1 38  ? 21.976 -27.281 23.63   1 57.359  ? 50  GLY   A HA3  1 c 2 
ATOM   2364 N N    . ASP   B 1 39  ? 19.402 -27.933 25.027  1 53.862  ? 51  ASP   A N    1 ? 2 
ATOM   2365 C CA   . ASP   B 1 39  ? 18.271 -28.829 25.254  1 54.053  ? 51  ASP   A CA   1 ? 2 
ATOM   2366 C C    . ASP   B 1 39  ? 17.107 -28.43  24.336  1 50.997  ? 51  ASP   A C    1 ? 2 
ATOM   2367 O O    . ASP   B 1 39  ? 16.951 -27.261 23.993  1 49.987  ? 51  ASP   A O    1 ? 2 
ATOM   2368 C CB   . ASP   B 1 39  ? 17.794 -28.818 26.703  1 52.049  ? 51  ASP   A CB   1 ? 2 
ATOM   2369 C CG   . ASP   B 1 39  ? 18.64  -29.527 27.757  1 55.119  ? 51  ASP   A CG   1 ? 2 
ATOM   2370 O OD1  . ASP   B 1 39  ? 19.593 -30.252 27.374  1 58.986  ? 51  ASP   A OD1  1 ? 2 
ATOM   2371 O OD2  . ASP   B 1 39  ? 18.328 -29.348 28.971  1 54.655  ? 51  ASP   A OD2  1 ? 2 
ATOM   2372 H H    . ASP   B 1 39  ? 19.707 -27.423 25.72   1 52.96   ? 51  ASP   A H    1 c 2 
ATOM   2373 H HA   . ASP   B 1 39  ? 18.552 -29.744 25.028  1 55.888  ? 51  ASP   A HA   1 c 2 
ATOM   2374 H HB2  . ASP   B 1 39  ? 17.701 -27.883 26.981  1 50.544  ? 51  ASP   A HB2  1 c 2 
ATOM   2375 H HB3  . ASP   B 1 39  ? 16.9   -29.22  26.731  1 52.57   ? 51  ASP   A HB3  1 c 2 
ATOM   2376 N N    . LYS   B 1 40  ? 16.297 -29.414 23.936  1 51.69   ? 52  LYS   A N    1 ? 2 
ATOM   2377 C CA   . LYS   B 1 40  ? 15.016 -29.177 23.294  1 50.498  ? 52  LYS   A CA   1 ? 2 
ATOM   2378 C C    . LYS   B 1 40  ? 13.99  -28.926 24.404  1 51.887  ? 52  LYS   A C    1 ? 2 
ATOM   2379 O O    . LYS   B 1 40  ? 13.839 -29.708 25.346  1 53.52   ? 52  LYS   A O    1 ? 2 
ATOM   2380 C CB   . LYS   B 1 40  ? 14.607 -30.318 22.342  1 51.22   ? 52  LYS   A CB   1 ? 2 
ATOM   2381 H H    . LYS   B 1 40  ? 16.559 -30.279 24.075  1 53.802  ? 52  LYS   A H    1 c 2 
ATOM   2382 H HA   . LYS   B 1 40  ? 15.094 -28.353 22.75   1 49.502  ? 52  LYS   A HA   1 c 2 
ATOM   2383 H HB2  . LYS   B 1 40  ? 15.348 -30.691 21.901  0 30      ? 52  LYS   A HB2  1 c 2 
ATOM   2384 H HB3  . LYS   B 1 40  ? 13.569 -30.291 22.258  0 30      ? 52  LYS   A HB3  1 c 2 
ATOM   2385 N N    . VAL   B 1 41  ? 13.26  -27.818 24.259  1 52.688  ? 53  VAL   A N    1 ? 2 
ATOM   2386 C CA   . VAL   B 1 41  ? 12.378 -27.314 25.297  1 51.771  ? 53  VAL   A CA   1 ? 2 
ATOM   2387 C C    . VAL   B 1 41  ? 10.961 -27.194 24.753  1 52.786  ? 53  VAL   A C    1 ? 2 
ATOM   2388 O O    . VAL   B 1 41  ? 10.785 -26.63  23.685  1 55.057  ? 53  VAL   A O    1 ? 2 
ATOM   2389 C CB   . VAL   B 1 41  ? 12.925 -25.943 25.727  1 48.052  ? 53  VAL   A CB   1 ? 2 
ATOM   2390 C CG1  . VAL   B 1 41  ? 11.874 -25.157 26.468  1 51.819  ? 53  VAL   A CG1  1 ? 2 
ATOM   2391 C CG2  . VAL   B 1 41  ? 14.2   -26.055 26.536  1 45.298  ? 53  VAL   A CG2  1 ? 2 
ATOM   2392 H H    . VAL   B 1 41  ? 13.31  -27.355 23.472  1 51.622  ? 53  VAL   A H    1 c 2 
ATOM   2393 H HA   . VAL   B 1 41  ? 12.388 -27.923 26.06   1 52.353  ? 53  VAL   A HA   1 c 2 
ATOM   2394 H HB   . VAL   B 1 41  ? 13.139 -25.446 24.902  1 48.205  ? 53  VAL   A HB   1 c 2 
ATOM   2395 H HG11 . VAL   B 1 41  ? 11.486 -25.71  27.166  1 50.589  ? 53  VAL   A HG11 1 c 2 
ATOM   2396 H HG12 . VAL   B 1 41  ? 11.177 -24.877 25.851  1 49.684  ? 53  VAL   A HG12 1 c 2 
ATOM   2397 H HG13 . VAL   B 1 41  ? 12.281 -24.372 26.868  1 48.631  ? 53  VAL   A HG13 1 c 2 
ATOM   2398 H HG21 . VAL   B 1 41  ? 14.513 -25.166 26.775  1 44.839  ? 53  VAL   A HG21 1 c 2 
ATOM   2399 H HG22 . VAL   B 1 41  ? 14.881 -26.506 26.009  1 47.464  ? 53  VAL   A HG22 1 c 2 
ATOM   2400 H HG23 . VAL   B 1 41  ? 14.028 -26.565 27.346  1 46.794  ? 53  VAL   A HG23 1 c 2 
ATOM   2401 N N    . TYR   B 1 42  ? 9.978  -27.653 25.544  1 52.965  ? 54  TYR   A N    1 ? 2 
ATOM   2402 C CA   . TYR   B 1 42  ? 8.563  -27.643 25.191  1 51.048  ? 54  TYR   A CA   1 ? 2 
ATOM   2403 C C    . TYR   B 1 42  ? 7.809  -26.723 26.158  1 47.665  ? 54  TYR   A C    1 ? 2 
ATOM   2404 O O    . TYR   B 1 42  ? 7.848  -26.925 27.37   1 45.997  ? 54  TYR   A O    1 ? 2 
ATOM   2405 C CB   . TYR   B 1 42  ? 8.02   -29.079 25.283  1 55.498  ? 54  TYR   A CB   1 ? 2 
ATOM   2406 C CG   . TYR   B 1 42  ? 8.707  -30.141 24.432  1 57.991  ? 54  TYR   A CG   1 ? 2 
ATOM   2407 C CD1  . TYR   B 1 42  ? 9.963  -30.632 24.765  1 62.894  ? 54  TYR   A CD1  1 ? 2 
ATOM   2408 C CD2  . TYR   B 1 42  ? 8.09   -30.68  23.307  1 63.707  ? 54  TYR   A CD2  1 ? 2 
ATOM   2409 C CE1  . TYR   B 1 42  ? 10.6   -31.594 23.998  1 64.245  ? 54  TYR   A CE1  1 ? 2 
ATOM   2410 C CE2  . TYR   B 1 42  ? 8.7    -31.667 22.543  1 66.356  ? 54  TYR   A CE2  1 ? 2 
ATOM   2411 C CZ   . TYR   B 1 42  ? 9.963  -32.123 22.89   1 68.279  ? 54  TYR   A CZ   1 ? 2 
ATOM   2412 O OH   . TYR   B 1 42  ? 10.614 -33.083 22.167  1 74.306  ? 54  TYR   A OH   1 ? 2 
ATOM   2413 H H    . TYR   B 1 42  ? 10.209 -27.994 26.36   1 52.746  ? 54  TYR   A H    1 c 2 
ATOM   2414 H HA   . TYR   B 1 42  ? 8.456  -27.309 24.262  1 51.465  ? 54  TYR   A HA   1 c 2 
ATOM   2415 H HB2  . TYR   B 1 42  ? 8.067  -29.36  26.224  1 55.18   ? 54  TYR   A HB2  1 c 2 
ATOM   2416 H HB3  . TYR   B 1 42  ? 7.068  -29.058 25.041  1 55.633  ? 54  TYR   A HB3  1 c 2 
ATOM   2417 H HD1  . TYR   B 1 42  ? 10.408 -30.281 25.52   1 60.351  ? 54  TYR   A HD1  1 c 2 
ATOM   2418 H HD2  . TYR   B 1 42  ? 7.229  -30.378 23.065  1 62.718  ? 54  TYR   A HD2  1 c 2 
ATOM   2419 H HE1  . TYR   B 1 42  ? 11.452 -31.909 24.246  1 65.558  ? 54  TYR   A HE1  1 c 2 
ATOM   2420 H HE2  . TYR   B 1 42  ? 8.266  -32.012 21.781  1 68.324  ? 54  TYR   A HE2  1 c 2 
ATOM   2421 H HH   . TYR   B 1 42  ? 11.364 -33.225 22.532  0 30      ? 54  TYR   A HH   1 c 2 
ATOM   2422 N N    . VAL   B 1 43  ? 7.114  -25.703 25.638  1 45.587  ? 55  VAL   A N    1 ? 2 
ATOM   2423 C CA   . VAL   B 1 43  ? 6.375  -24.774 26.487  1 46.299  ? 55  VAL   A CA   1 ? 2 
ATOM   2424 C C    . VAL   B 1 43  ? 4.974  -24.518 25.922  1 46.189  ? 55  VAL   A C    1 ? 2 
ATOM   2425 O O    . VAL   B 1 43  ? 4.736  -24.709 24.728  1 48.06   ? 55  VAL   A O    1 ? 2 
ATOM   2426 C CB   . VAL   B 1 43  ? 7.113  -23.423 26.644  1 45.854  ? 55  VAL   A CB   1 ? 2 
ATOM   2427 C CG1  . VAL   B 1 43  ? 8.58   -23.575 27.042  1 41.218  ? 55  VAL   A CG1  1 ? 2 
ATOM   2428 C CG2  . VAL   B 1 43  ? 7.003  -22.548 25.389  1 47.075  ? 55  VAL   A CG2  1 ? 2 
ATOM   2429 H H    . VAL   B 1 43  ? 7.099  -25.581 24.732  1 46.569  ? 55  VAL   A H    1 c 2 
ATOM   2430 H HA   . VAL   B 1 43  ? 6.279  -25.176 27.37   1 46.39   ? 55  VAL   A HA   1 c 2 
ATOM   2431 H HB   . VAL   B 1 43  ? 6.664  -22.937 27.374  1 44.361  ? 55  VAL   A HB   1 c 2 
ATOM   2432 H HG11 . VAL   B 1 43  ? 9.06   -24.043 26.339  1 43.165  ? 55  VAL   A HG11 1 c 2 
ATOM   2433 H HG12 . VAL   B 1 43  ? 8.642  -24.082 27.869  1 42.923  ? 55  VAL   A HG12 1 c 2 
ATOM   2434 H HG13 . VAL   B 1 43  ? 8.974  -22.696 27.172  1 41.115  ? 55  VAL   A HG13 1 c 2 
ATOM   2435 H HG21 . VAL   B 1 43  ? 7.584  -21.776 25.482  1 45.106  ? 55  VAL   A HG21 1 c 2 
ATOM   2436 H HG22 . VAL   B 1 43  ? 6.085  -22.248 25.277  1 46.645  ? 55  VAL   A HG22 1 c 2 
ATOM   2437 H HG23 . VAL   B 1 43  ? 7.272  -23.063 24.609  1 47.411  ? 55  VAL   A HG23 1 c 2 
ATOM   2438 N N    . HIS   B 1 44  ? 4.073  -24.042 26.793  1 44.957  ? 56  HIS   A N    1 ? 2 
ATOM   2439 C CA   . HIS   B 1 44  ? 2.916  -23.25  26.387  1 45.229  ? 56  HIS   A CA   1 ? 2 
ATOM   2440 C C    . HIS   B 1 44  ? 3.115  -21.823 26.878  1 41.686  ? 56  HIS   A C    1 ? 2 
ATOM   2441 O O    . HIS   B 1 44  ? 3.664  -21.639 27.961  1 42.901  ? 56  HIS   A O    1 ? 2 
ATOM   2442 C CB   . HIS   B 1 44  ? 1.598  -23.795 26.963  1 47.111  ? 56  HIS   A CB   1 ? 2 
ATOM   2443 C CG   . HIS   B 1 44  ? 0.906  -24.773 26.076  1 48.309  ? 56  HIS   A CG   1 ? 2 
ATOM   2444 N ND1  . HIS   B 1 44  ? 0.584  -24.494 24.762  1 49.503  ? 56  HIS   A ND1  1 ? 2 
ATOM   2445 C CD2  . HIS   B 1 44  ? 0.447  -26     26.32   1 48.241  ? 56  HIS   A CD2  1 ? 2 
ATOM   2446 C CE1  . HIS   B 1 44  ? -0.01  -25.55  24.218  1 49.175  ? 56  HIS   A CE1  1 ? 2 
ATOM   2447 N NE2  . HIS   B 1 44  ? -0.126 -26.467 25.161  1 50.875  ? 56  HIS   A NE2  1 ? 2 
ATOM   2448 H H    . HIS   B 1 44  ? 4.185  -24.221 27.682  1 45.13   ? 56  HIS   A H    1 c 2 
ATOM   2449 H HA   . HIS   B 1 44  ? 2.867  -23.237 25.401  1 45.403  ? 56  HIS   A HA   1 c 2 
ATOM   2450 H HB2  . HIS   B 1 44  ? 1.788  -24.226 27.825  1 46.919  ? 56  HIS   A HB2  1 c 2 
ATOM   2451 H HB3  . HIS   B 1 44  ? 0.993  -23.041 27.136  1 46.459  ? 56  HIS   A HB3  1 c 2 
ATOM   2452 H HD1  . HIS   B 1 44  ? 0.666  -23.717 24.375  0 30      ? 56  HIS   A HD1  1 c 2 
ATOM   2453 H HD2  . HIS   B 1 44  ? 0.506  -26.469 27.129  1 49.251  ? 56  HIS   A HD2  1 c 2 
ATOM   2454 H HE1  . HIS   B 1 44  ? -0.334 -25.615 23.336  1 51.244  ? 56  HIS   A HE1  1 c 2 
ATOM   2455 H HE2  . HIS   B 1 44  ? -0.508 -27.267 25.072  0 30      ? 56  HIS   A HE2  1 c 2 
ATOM   2456 N N    . TYR   B 1 45  ? 2.614  -20.831 26.124  1 40.961  ? 57  TYR   A N    1 ? 2 
ATOM   2457 C CA   . TYR   B 1 45  ? 2.813  -19.436 26.52   1 39.766  ? 57  TYR   A CA   1 ? 2 
ATOM   2458 C C    . TYR   B 1 45  ? 1.601  -18.577 26.145  1 41.759  ? 57  TYR   A C    1 ? 2 
ATOM   2459 O O    . TYR   B 1 45  ? 0.766  -18.952 25.317  1 40.445  ? 57  TYR   A O    1 ? 2 
ATOM   2460 C CB   . TYR   B 1 45  ? 4.1    -18.869 25.928  1 35.076  ? 57  TYR   A CB   1 ? 2 
ATOM   2461 C CG   . TYR   B 1 45  ? 3.985  -18.606 24.435  1 34.334  ? 57  TYR   A CG   1 ? 2 
ATOM   2462 C CD1  . TYR   B 1 45  ? 3.45   -17.426 23.955  1 33.834  ? 57  TYR   A CD1  1 ? 2 
ATOM   2463 C CD2  . TYR   B 1 45  ? 4.427  -19.539 23.505  1 35.742  ? 57  TYR   A CD2  1 ? 2 
ATOM   2464 C CE1  . TYR   B 1 45  ? 3.343  -17.184 22.594  1 36.539  ? 57  TYR   A CE1  1 ? 2 
ATOM   2465 C CE2  . TYR   B 1 45  ? 4.301  -19.325 22.138  1 36.012  ? 57  TYR   A CE2  1 ? 2 
ATOM   2466 C CZ   . TYR   B 1 45  ? 3.751  -18.148 21.684  1 36.302  ? 57  TYR   A CZ   1 ? 2 
ATOM   2467 O OH   . TYR   B 1 45  ? 3.678  -17.952 20.346  1 38.194  ? 57  TYR   A OH   1 ? 2 
ATOM   2468 H H    . TYR   B 1 45  ? 2.146  -21.02  25.362  1 42.229  ? 57  TYR   A H    1 c 2 
ATOM   2469 H HA   . TYR   B 1 45  ? 2.901  -19.416 27.507  1 39.015  ? 57  TYR   A HA   1 c 2 
ATOM   2470 H HB2  . TYR   B 1 45  ? 4.316  -18.027 26.388  1 34.431  ? 57  TYR   A HB2  1 c 2 
ATOM   2471 H HB3  . TYR   B 1 45  ? 4.83   -19.507 26.088  1 35.376  ? 57  TYR   A HB3  1 c 2 
ATOM   2472 H HD1  . TYR   B 1 45  ? 3.152  -16.77  24.565  1 33.9    ? 57  TYR   A HD1  1 c 2 
ATOM   2473 H HD2  . TYR   B 1 45  ? 4.782  -20.359 23.81   1 35.883  ? 57  TYR   A HD2  1 c 2 
ATOM   2474 H HE1  . TYR   B 1 45  ? 2.966  -16.377 22.288  1 35.852  ? 57  TYR   A HE1  1 c 2 
ATOM   2475 H HE2  . TYR   B 1 45  ? 4.6    -19.976 21.526  1 37.193  ? 57  TYR   A HE2  1 c 2 
ATOM   2476 H HH   . TYR   B 1 45  ? 3.324  -17.216 20.162  0 30      ? 57  TYR   A HH   1 c 2 
ATOM   2477 N N    . LYS   B 1 46  ? 1.476  -17.459 26.871  1 42.969  ? 58  LYS   A N    1 ? 2 
ATOM   2478 C CA   . LYS   B 1 46  ? 0.561  -16.391 26.517  1 45.112  ? 58  LYS   A CA   1 ? 2 
ATOM   2479 C C    . LYS   B 1 46  ? 1.373  -15.109 26.536  1 40.311  ? 58  LYS   A C    1 ? 2 
ATOM   2480 O O    . LYS   B 1 46  ? 2.02   -14.821 27.528  1 38.375  ? 58  LYS   A O    1 ? 2 
ATOM   2481 C CB   . LYS   B 1 46  ? -0.644 -16.323 27.452  1 46.61   ? 58  LYS   A CB   1 ? 2 
ATOM   2482 C CG   . LYS   B 1 46  ? -1.431 -17.582 27.558  1 47.369  ? 58  LYS   A CG   1 ? 2 
ATOM   2483 C CD   . LYS   B 1 46  ? -2.423 -17.541 28.707  1 48.237  ? 58  LYS   A CD   1 ? 2 
ATOM   2484 C CE   . LYS   B 1 46  ? -2.852 -18.932 29.128  1 49.975  ? 58  LYS   A CE   1 ? 2 
ATOM   2485 N NZ   . LYS   B 1 46  ? -4.007 -18.862 30.031  1 54.721  ? 58  LYS   A NZ   1 ? 2 
ATOM   2486 H H    . LYS   B 1 46  ? 1.986  -17.362 27.623  1 41.918  ? 58  LYS   A H    1 c 2 
ATOM   2487 H HA   . LYS   B 1 46  ? 0.236  -16.548 25.594  1 44.987  ? 58  LYS   A HA   1 c 2 
ATOM   2488 H HB2  . LYS   B 1 46  ? -0.331 -16.076 28.348  1 45.602  ? 58  LYS   A HB2  1 c 2 
ATOM   2489 H HB3  . LYS   B 1 46  ? -1.243 -15.611 27.14   1 46.912  ? 58  LYS   A HB3  1 c 2 
ATOM   2490 H HG2  . LYS   B 1 46  ? -1.913 -17.728 26.716  1 48.6    ? 58  LYS   A HG2  1 c 2 
ATOM   2491 H HG3  . LYS   B 1 46  ? -0.813 -18.333 27.693  1 47.071  ? 58  LYS   A HG3  1 c 2 
ATOM   2492 H HD2  . LYS   B 1 46  ? -2.013 -17.088 29.474  1 47.423  ? 58  LYS   A HD2  1 c 2 
ATOM   2493 H HD3  . LYS   B 1 46  ? -3.214 -17.027 28.432  1 49.457  ? 58  LYS   A HD3  1 c 2 
ATOM   2494 H HE2  . LYS   B 1 46  ? -3.093 -19.454 28.342  1 51.52   ? 58  LYS   A HE2  1 c 2 
ATOM   2495 H HE3  . LYS   B 1 46  ? -2.117 -19.381 29.583  1 49.722  ? 58  LYS   A HE3  1 c 2 
ATOM   2496 H HZ1  . LYS   B 1 46  ? -4.69  -18.427 29.624  1 54.792  ? 58  LYS   A HZ1  1 c 2 
ATOM   2497 H HZ2  . LYS   B 1 46  ? -3.778 -18.416 30.786  1 53.162  ? 58  LYS   A HZ2  1 c 2 
ATOM   2498 H HZ3  . LYS   B 1 46  ? -4.276 -19.698 30.25   1 55      ? 58  LYS   A HZ3  1 c 2 
ATOM   2499 N N    . GLY   B 1 47  ? 1.454  -14.442 25.377  1 41.603  ? 59  GLY   A N    1 ? 2 
ATOM   2500 C CA   . GLY   B 1 47  ? 2.282  -13.254 25.228  1 36.684  ? 59  GLY   A CA   1 ? 2 
ATOM   2501 C C    . GLY   B 1 47  ? 1.426  -12.063 24.817  1 37.643  ? 59  GLY   A C    1 ? 2 
ATOM   2502 O O    . GLY   B 1 47  ? 0.346  -12.232 24.237  1 36.691  ? 59  GLY   A O    1 ? 2 
ATOM   2503 H H    . GLY   B 1 47  ? 0.975  -14.736 24.656  1 41.508  ? 59  GLY   A H    1 c 2 
ATOM   2504 H HA2  . GLY   B 1 47  ? 2.736  -13.061 26.078  1 36.678  ? 59  GLY   A HA2  1 c 2 
ATOM   2505 H HA3  . GLY   B 1 47  ? 2.971  -13.421 24.542  1 37.043  ? 59  GLY   A HA3  1 c 2 
ATOM   2506 N N    . LYS   B 1 48  ? 1.905  -10.859 25.15   1 38.36   ? 60  LYS   A N    1 ? 2 
ATOM   2507 C CA   . LYS   B 1 48  ? 1.241  -9.63   24.75   1 38.802  ? 60  LYS   A CA   1 ? 2 
ATOM   2508 C C    . LYS   B 1 48  ? 2.24   -8.481  24.778  1 37.122  ? 60  LYS   A C    1 ? 2 
ATOM   2509 O O    . LYS   B 1 48  ? 3.264  -8.568  25.453  1 38.158  ? 60  LYS   A O    1 ? 2 
ATOM   2510 C CB   . LYS   B 1 48  ? 0.025  -9.296  25.625  1 42.429  ? 60  LYS   A CB   1 ? 2 
ATOM   2511 C CG   . LYS   B 1 48  ? 0.336  -8.982  27.082  1 45.076  ? 60  LYS   A CG   1 ? 2 
ATOM   2512 C CD   . LYS   B 1 48  ? -0.845 -9.006  28.047  1 50.719  ? 60  LYS   A CD   1 ? 2 
ATOM   2513 C CE   . LYS   B 1 48  ? -1.54  -7.684  28.055  1 65.241  ? 60  LYS   A CE   1 ? 2 
ATOM   2514 N NZ   . LYS   B 1 48  ? -2.742 -7.702  28.902  1 77.286  ? 60  LYS   A NZ   1 ? 2 
ATOM   2515 H H    . LYS   B 1 48  ? 2.672  -10.804 25.643  1 36.804  ? 60  LYS   A H    1 c 2 
ATOM   2516 H HA   . LYS   B 1 48  ? 0.928  -9.744  23.818  1 39.981  ? 60  LYS   A HA   1 c 2 
ATOM   2517 H HB2  . LYS   B 1 48  ? -0.436 -8.523  25.235  1 43.584  ? 60  LYS   A HB2  1 c 2 
ATOM   2518 H HB3  . LYS   B 1 48  ? -0.596 -10.056 25.599  1 43.53   ? 60  LYS   A HB3  1 c 2 
ATOM   2519 H HG2  . LYS   B 1 48  ? 1.006  -9.628  27.396  1 44.056  ? 60  LYS   A HG2  1 c 2 
ATOM   2520 H HG3  . LYS   B 1 48  ? 0.752  -8.093  27.121  1 44.901  ? 60  LYS   A HG3  1 c 2 
ATOM   2521 H HD2  . LYS   B 1 48  ? -1.479 -9.704  27.773  1 53.222  ? 60  LYS   A HD2  1 c 2 
ATOM   2522 H HD3  . LYS   B 1 48  ? -0.525 -9.211  28.952  1 51.935  ? 60  LYS   A HD3  1 c 2 
ATOM   2523 H HE2  . LYS   B 1 48  ? -0.931 -7.001  28.387  1 63.106  ? 60  LYS   A HE2  1 c 2 
ATOM   2524 H HE3  . LYS   B 1 48  ? -1.796 -7.446  27.146  1 64.41   ? 60  LYS   A HE3  1 c 2 
ATOM   2525 H HZ1  . LYS   B 1 48  ? -2.526 -7.987  29.734  1 73.551  ? 60  LYS   A HZ1  1 c 2 
ATOM   2526 H HZ2  . LYS   B 1 48  ? -3.359 -8.262  28.546  1 74.879  ? 60  LYS   A HZ2  1 c 2 
ATOM   2527 H HZ3  . LYS   B 1 48  ? -3.092 -6.868  28.954  1 75      ? 60  LYS   A HZ3  1 c 2 
ATOM   2528 N N    . LEU   B 1 49  ? 1.974  -7.469  23.941  1 39.256  ? 61  LEU   A N    1 ? 2 
ATOM   2529 C CA   . LEU   B 1 49  ? 2.572  -6.146  24.019  1 40.682  ? 61  LEU   A CA   1 ? 2 
ATOM   2530 C C    . LEU   B 1 49  ? 2.034  -5.477  25.282  1 40.979  ? 61  LEU   A C    1 ? 2 
ATOM   2531 O O    . LEU   B 1 49  ? 0.882  -5.694  25.638  1 44.358  ? 61  LEU   A O    1 ? 2 
ATOM   2532 C CB   . LEU   B 1 49  ? 2.165  -5.306  22.799  1 39.629  ? 61  LEU   A CB   1 ? 2 
ATOM   2533 C CG   . LEU   B 1 49  ? 2.517  -5.863  21.415  1 42.455  ? 61  LEU   A CG   1 ? 2 
ATOM   2534 C CD1  . LEU   B 1 49  ? 2.159  -4.84   20.341  1 43.535  ? 61  LEU   A CD1  1 ? 2 
ATOM   2535 C CD2  . LEU   B 1 49  ? 3.99   -6.284  21.223  1 41.734  ? 61  LEU   A CD2  1 ? 2 
ATOM   2536 H H    . LEU   B 1 49  ? 1.367  -7.62   23.275  1 40.362  ? 61  LEU   A H    1 c 2 
ATOM   2537 H HA   . LEU   B 1 49  ? 3.558  -6.229  24.067  1 38.722  ? 61  LEU   A HA   1 c 2 
ATOM   2538 H HB2  . LEU   B 1 49  ? 1.19   -5.17   22.836  1 42.154  ? 61  LEU   A HB2  1 c 2 
ATOM   2539 H HB3  . LEU   B 1 49  ? 2.583  -4.418  22.888  1 40.721  ? 61  LEU   A HB3  1 c 2 
ATOM   2540 H HG   . LEU   B 1 49  ? 1.955  -6.666  21.259  1 42.487  ? 61  LEU   A HG   1 c 2 
ATOM   2541 H HD11 . LEU   B 1 49  ? 1.204  -4.662  20.367  1 45.069  ? 61  LEU   A HD11 1 c 2 
ATOM   2542 H HD12 . LEU   B 1 49  ? 2.4    -5.188  19.466  1 43.948  ? 61  LEU   A HD12 1 c 2 
ATOM   2543 H HD13 . LEU   B 1 49  ? 2.645  -4.014  20.505  1 43.437  ? 61  LEU   A HD13 1 c 2 
ATOM   2544 H HD21 . LEU   B 1 49  ? 4.212  -6.99   21.853  1 40.585  ? 61  LEU   A HD21 1 c 2 
ATOM   2545 H HD22 . LEU   B 1 49  ? 4.57   -5.519  21.378  1 41.069  ? 61  LEU   A HD22 1 c 2 
ATOM   2546 H HD23 . LEU   B 1 49  ? 4.12   -6.609  20.316  1 41.843  ? 61  LEU   A HD23 1 c 2 
ATOM   2547 N N    . SER   B 1 50  ? 2.823  -4.608  25.91   1 47.405  ? 62  SER   A N    1 ? 2 
ATOM   2548 C CA   . SER   B 1 50  ? 2.34   -3.897  27.093  1 50.097  ? 62  SER   A CA   1 ? 2 
ATOM   2549 C C    . SER   B 1 50  ? 1.292  -2.85   26.716  1 51.853  ? 62  SER   A C    1 ? 2 
ATOM   2550 O O    . SER   B 1 50  ? 0.553  -2.36   27.566  1 52.74   ? 62  SER   A O    1 ? 2 
ATOM   2551 C CB   . SER   B 1 50  ? 3.487  -3.317  27.858  1 49.94   ? 62  SER   A CB   1 ? 2 
ATOM   2552 O OG   . SER   B 1 50  ? 4.291  -4.41   28.297  1 56.086  ? 62  SER   A OG   1 ? 2 
ATOM   2553 H H    . SER   B 1 50  ? 3.67   -4.451  25.606  1 45.097  ? 62  SER   A H    1 c 2 
ATOM   2554 H HA   . SER   B 1 50  ? 1.897  -4.562  27.679  1 49.829  ? 62  SER   A HA   1 c 2 
ATOM   2555 H HB2  . SER   B 1 50  ? 4.008  -2.726  27.283  1 51.38   ? 62  SER   A HB2  1 c 2 
ATOM   2556 H HB3  . SER   B 1 50  ? 3.156  -2.814  28.626  1 52.409  ? 62  SER   A HB3  1 c 2 
ATOM   2557 H HG   . SER   B 1 50  ? 4.91   -4.176  28.82   0 30      ? 62  SER   A HG   1 c 2 
ATOM   2558 N N    . ASN   B 1 51  ? 1.182  -2.512  25.426  1 49.955  ? 63  ASN   A N    1 ? 2 
ATOM   2559 C CA   . ASN   B 1 51  ? 0.209  -1.504  25.037  1 48.328  ? 63  ASN   A CA   1 ? 2 
ATOM   2560 C C    . ASN   B 1 51  ? -1.175 -2.149  24.867  1 54.117  ? 63  ASN   A C    1 ? 2 
ATOM   2561 O O    . ASN   B 1 51  ? -2.141 -1.426  24.629  1 56.684  ? 63  ASN   A O    1 ? 2 
ATOM   2562 C CB   . ASN   B 1 51  ? 0.696  -0.735  23.82   1 48.487  ? 63  ASN   A CB   1 ? 2 
ATOM   2563 C CG   . ASN   B 1 51  ? 0.597  -1.51   22.525  1 51.139  ? 63  ASN   A CG   1 ? 2 
ATOM   2564 O OD1  . ASN   B 1 51  ? 0.214  -2.691  22.51   1 54.139  ? 63  ASN   A OD1  1 ? 2 
ATOM   2565 N ND2  . ASN   B 1 51  ? 0.935  -0.853  21.425  1 50.1    ? 63  ASN   A ND2  1 ? 2 
ATOM   2566 H H    . ASN   B 1 51  ? 1.719  -2.89   24.791  1 48.62   ? 63  ASN   A H    1 c 2 
ATOM   2567 H HA   . ASN   B 1 51  ? 0.142  -0.853  25.772  1 50.471  ? 63  ASN   A HA   1 c 2 
ATOM   2568 H HB2  . ASN   B 1 51  ? 0.172  0.086   23.736  1 50.814  ? 63  ASN   A HB2  1 c 2 
ATOM   2569 H HB3  . ASN   B 1 51  ? 1.629  -0.479  23.963  1 48.058  ? 63  ASN   A HB3  1 c 2 
ATOM   2570 H HD21 . ASN   B 1 51  ? 0.98   -1.282  20.65   1 50.673  ? 63  ASN   A HD21 1 c 2 
ATOM   2571 H HD22 . ASN   B 1 51  ? 1.116  0.015   21.463  1 51.204  ? 63  ASN   A HD22 1 c 2 
ATOM   2572 N N    . GLY   B 1 52  ? -1.264 -3.498  24.969  1 50.387  ? 64  GLY   A N    1 ? 2 
ATOM   2573 C CA   . GLY   B 1 52  ? -2.53  -4.22   24.965  1 50.769  ? 64  GLY   A CA   1 ? 2 
ATOM   2574 C C    . GLY   B 1 52  ? -3.134 -4.378  23.563  1 55.626  ? 64  GLY   A C    1 ? 2 
ATOM   2575 O O    . GLY   B 1 52  ? -4.342 -4.626  23.444  1 59.063  ? 64  GLY   A O    1 ? 2 
ATOM   2576 H H    . GLY   B 1 52  ? -0.495 -3.986  25.027  1 49.115  ? 64  GLY   A H    1 c 2 
ATOM   2577 H HA2  . GLY   B 1 52  ? -2.385 -5.113  25.358  1 50.861  ? 64  GLY   A HA2  1 c 2 
ATOM   2578 H HA3  . GLY   B 1 52  ? -3.17  -3.741  25.542  1 53.218  ? 64  GLY   A HA3  1 c 2 
ATOM   2579 N N    . LYS   B 1 53  ? -2.321 -4.269  22.499  1 52.503  ? 65  LYS   A N    1 ? 2 
ATOM   2580 C CA   . LYS   B 1 53  ? -2.887 -4.197  21.153  1 58.762  ? 65  LYS   A CA   1 ? 2 
ATOM   2581 C C    . LYS   B 1 53  ? -2.669 -5.501  20.375  1 59.816  ? 65  LYS   A C    1 ? 2 
ATOM   2582 O O    . LYS   B 1 53  ? -3.196 -5.648  19.271  1 57.729  ? 65  LYS   A O    1 ? 2 
ATOM   2583 C CB   . LYS   B 1 53  ? -2.374 -2.974  20.373  1 58.398  ? 65  LYS   A CB   1 ? 2 
ATOM   2584 H H    . LYS   B 1 53  ? -1.414 -4.236  22.609  1 52.361  ? 65  LYS   A H    1 c 2 
ATOM   2585 H HA   . LYS   B 1 53  ? -3.865 -4.071  21.245  1 59.938  ? 65  LYS   A HA   1 c 2 
ATOM   2586 H HB2  . LYS   B 1 53  ? -1.417 -2.941  20.413  0 30      ? 65  LYS   A HB2  1 c 2 
ATOM   2587 H HB3  . LYS   B 1 53  ? -3.176 -2.423  20.108  0 30      ? 65  LYS   A HB3  1 c 2 
ATOM   2588 N N    . LYS   B 1 54  ? -1.888 -6.44   20.939  1 58.864  ? 66  LYS   A N    1 ? 2 
ATOM   2589 C CA   . LYS   B 1 54  ? -1.626 -7.718  20.287  1 60.228  ? 66  LYS   A CA   1 ? 2 
ATOM   2590 C C    . LYS   B 1 54  ? -1.398 -8.8    21.347  1 58.79   ? 66  LYS   A C    1 ? 2 
ATOM   2591 O O    . LYS   B 1 54  ? -0.67  -8.593  22.325  1 50.639  ? 66  LYS   A O    1 ? 2 
ATOM   2592 C CB   . LYS   B 1 54  ? -0.479 -7.667  19.265  1 55.282  ? 66  LYS   A CB   1 ? 2 
ATOM   2593 H H    . LYS   B 1 54  ? -1.503 -6.278  21.752  1 57.603  ? 66  LYS   A H    1 c 2 
ATOM   2594 H HA   . LYS   B 1 54  ? -2.441 -7.964  19.782  1 60.949  ? 66  LYS   A HA   1 c 2 
ATOM   2595 H HB2  . LYS   B 1 54  ? 0.398  -7.689  19.735  0 30      ? 66  LYS   A HB2  1 c 2 
ATOM   2596 H HB3  . LYS   B 1 54  ? -0.839 -7.62   18.349  0 30      ? 66  LYS   A HB3  1 c 2 
ATOM   2597 N N    . PHE   B 1 55  ? -2.076 -9.935  21.131  1 59.33   ? 67  PHE   A N    1 ? 2 
ATOM   2598 C CA   . PHE   B 1 55  ? -1.973 -11.099 21.994  1 59.307  ? 67  PHE   A CA   1 ? 2 
ATOM   2599 C C    . PHE   B 1 55  ? -1.675 -12.325 21.142  1 57.408  ? 67  PHE   A C    1 ? 2 
ATOM   2600 O O    . PHE   B 1 55  ? -2.205 -12.472 20.047  1 64.662  ? 67  PHE   A O    1 ? 2 
ATOM   2601 C CB   . PHE   B 1 55  ? -3.267 -11.372 22.746  1 56.65   ? 67  PHE   A CB   1 ? 2 
ATOM   2602 C CG   . PHE   B 1 55  ? -3.854 -10.141 23.414  1 61.265  ? 67  PHE   A CG   1 ? 2 
ATOM   2603 C CD1  . PHE   B 1 55  ? -4.505 -9.157  22.661  1 61.768  ? 67  PHE   A CD1  1 ? 2 
ATOM   2604 C CD2  . PHE   B 1 55  ? -3.806 -9.999  24.801  1 60.76   ? 67  PHE   A CD2  1 ? 2 
ATOM   2605 C CE1  . PHE   B 1 55  ? -5.073 -8.052  23.284  1 61.646  ? 67  PHE   A CE1  1 ? 2 
ATOM   2606 C CE2  . PHE   B 1 55  ? -4.378 -8.89   25.415  1 62.718  ? 67  PHE   A CE2  1 ? 2 
ATOM   2607 C CZ   . PHE   B 1 55  ? -5.011 -7.922  24.656  1 61.716  ? 67  PHE   A CZ   1 ? 2 
ATOM   2608 H H    . PHE   B 1 55  ? -2.628 -9.985  20.405  1 61.267  ? 67  PHE   A H    1 c 2 
ATOM   2609 H HA   . PHE   B 1 55  ? -1.237 -10.962 22.646  1 55.97   ? 67  PHE   A HA   1 c 2 
ATOM   2610 H HB2  . PHE   B 1 55  ? -3.927 -11.737 22.114  1 60.28   ? 67  PHE   A HB2  1 c 2 
ATOM   2611 H HB3  . PHE   B 1 55  ? -3.094 -12.056 23.431  1 57.875  ? 67  PHE   A HB3  1 c 2 
ATOM   2612 H HD1  . PHE   B 1 55  ? -4.559 -9.246  21.723  1 62.559  ? 67  PHE   A HD1  1 c 2 
ATOM   2613 H HD2  . PHE   B 1 55  ? -3.383 -10.661 25.325  1 59.775  ? 67  PHE   A HD2  1 c 2 
ATOM   2614 H HE1  . PHE   B 1 55  ? -5.5   -7.388  22.767  1 63.576  ? 67  PHE   A HE1  1 c 2 
ATOM   2615 H HE2  . PHE   B 1 55  ? -4.33  -8.797  26.354  1 61.466  ? 67  PHE   A HE2  1 c 2 
ATOM   2616 H HZ   . PHE   B 1 55  ? -5.387 -7.164  25.076  1 63.086  ? 67  PHE   A HZ   1 c 2 
ATOM   2617 N N    . ASP   B 1 56  ? -0.799 -13.174 21.654  1 50.173  ? 68  ASP   A N    1 ? 2 
ATOM   2618 C CA   . ASP   B 1 56  ? -0.414 -14.388 20.97   1 48.632  ? 68  ASP   A CA   1 ? 2 
ATOM   2619 C C    . ASP   B 1 56  ? -0.252 -15.497 22.001  1 44.459  ? 68  ASP   A C    1 ? 2 
ATOM   2620 O O    . ASP   B 1 56  ? 0.415  -15.323 23.006  1 47.338  ? 68  ASP   A O    1 ? 2 
ATOM   2621 C CB   . ASP   B 1 56  ? 0.895  -14.217 20.217  1 49.651  ? 68  ASP   A CB   1 ? 2 
ATOM   2622 C CG   . ASP   B 1 56  ? 1.431  -15.508 19.616  1 47.24   ? 68  ASP   A CG   1 ? 2 
ATOM   2623 O OD1  . ASP   B 1 56  ? 0.687  -16.134 18.855  1 53.536  ? 68  ASP   A OD1  1 ? 2 
ATOM   2624 O OD2  . ASP   B 1 56  ? 2.586  -15.832 19.855  1 46.68   ? 68  ASP   A OD2  1 ? 2 
ATOM   2625 H H    . ASP   B 1 56  ? -0.42  -12.99  22.465  1 49.756  ? 68  ASP   A H    1 c 2 
ATOM   2626 H HA   . ASP   B 1 56  ? -1.124 -14.636 20.335  1 50.588  ? 68  ASP   A HA   1 c 2 
ATOM   2627 H HB2  . ASP   B 1 56  ? 0.765  -13.569 19.494  1 49.021  ? 68  ASP   A HB2  1 c 2 
ATOM   2628 H HB3  . ASP   B 1 56  ? 1.569  -13.858 20.831  1 46.793  ? 68  ASP   A HB3  1 c 2 
ATOM   2629 N N    . SER   B 1 57  ? -0.91  -16.612 21.75   1 46.526  ? 69  SER   A N    1 ? 2 
ATOM   2630 C CA   . SER   B 1 57  ? -0.883 -17.748 22.64   1 49.087  ? 69  SER   A CA   1 ? 2 
ATOM   2631 C C    . SER   B 1 57  ? -0.639 -19.006 21.809  1 51.601  ? 69  SER   A C    1 ? 2 
ATOM   2632 O O    . SER   B 1 57  ? -1.247 -19.15  20.753  1 52.419  ? 69  SER   A O    1 ? 2 
ATOM   2633 C CB   . SER   B 1 57  ? -2.169 -17.857 23.413  1 49.964  ? 69  SER   A CB   1 ? 2 
ATOM   2634 O OG   . SER   B 1 57  ? -2.089 -18.961 24.296  1 53.65   ? 69  SER   A OG   1 ? 2 
ATOM   2635 H H    . SER   B 1 57  ? -1.399 -16.675 20.98   1 48.603  ? 69  SER   A H    1 c 2 
ATOM   2636 H HA   . SER   B 1 57  ? -0.134 -17.637 23.277  1 46.942  ? 69  SER   A HA   1 c 2 
ATOM   2637 H HB2  . SER   B 1 57  ? -2.317 -17.037 23.921  1 50.258  ? 69  SER   A HB2  1 c 2 
ATOM   2638 H HB3  . SER   B 1 57  ? -2.914 -17.981 22.794  1 52.77   ? 69  SER   A HB3  1 c 2 
ATOM   2639 H HG   . SER   B 1 57  ? -2.897 -18.893 24.704  0 30      ? 69  SER   A HG   1 c 2 
ATOM   2640 N N    . SER   B 1 58  ? 0.215  -19.897 22.328  1 46.614  ? 70  SER   A N    1 ? 2 
ATOM   2641 C CA   . SER   B 1 58  ? 0.412  -21.227 21.777  1 51.978  ? 70  SER   A CA   1 ? 2 
ATOM   2642 C C    . SER   B 1 58  ? -0.899 -22.009 21.709  1 57.684  ? 70  SER   A C    1 ? 2 
ATOM   2643 O O    . SER   B 1 58  ? -1.095 -22.795 20.791  1 62.134  ? 70  SER   A O    1 ? 2 
ATOM   2644 C CB   . SER   B 1 58  ? 1.452  -21.963 22.577  1 51.382  ? 70  SER   A CB   1 ? 2 
ATOM   2645 O OG   . SER   B 1 58  ? 1.054  -22.096 23.929  1 49.339  ? 70  SER   A OG   1 ? 2 
ATOM   2646 H H    . SER   B 1 58  ? 0.701  -19.658 23.064  1 46.945  ? 70  SER   A H    1 c 2 
ATOM   2647 H HA   . SER   B 1 58  ? 0.752  -21.123 20.852  1 52.101  ? 70  SER   A HA   1 c 2 
ATOM   2648 H HB2  . SER   B 1 58  ? 1.59   -22.848 22.19   1 52.173  ? 70  SER   A HB2  1 c 2 
ATOM   2649 H HB3  . SER   B 1 58  ? 2.297  -21.476 22.533  1 49.299  ? 70  SER   A HB3  1 c 2 
ATOM   2650 H HG   . SER   B 1 58  ? 1.704  -22.532 24.34   0 30      ? 70  SER   A HG   1 c 2 
ATOM   2651 N N    . HIS   B 1 59  ? -1.802 -21.781 22.673  1 58.508  ? 71  HIS   A N    1 ? 2 
ATOM   2652 C CA   . HIS   B 1 59  ? -3.104 -22.431 22.683  1 62.933  ? 71  HIS   A CA   1 ? 2 
ATOM   2653 C C    . HIS   B 1 59  ? -3.873 -22.125 21.393  1 64.913  ? 71  HIS   A C    1 ? 2 
ATOM   2654 O O    . HIS   B 1 59  ? -4.533 -23.014 20.862  1 62.724  ? 71  HIS   A O    1 ? 2 
ATOM   2655 C CB   . HIS   B 1 59  ? -3.843 -22.119 23.993  1 64.01   ? 71  HIS   A CB   1 ? 2 
ATOM   2656 C CG   . HIS   B 1 59  ? -3.08  -22.548 25.219  1 62.355  ? 71  HIS   A CG   1 ? 2 
ATOM   2657 N ND1  . HIS   B 1 59  ? -2.454 -21.661 26.075  1 61.252  ? 71  HIS   A ND1  1 ? 2 
ATOM   2658 C CD2  . HIS   B 1 59  ? -2.845 -23.775 25.73   1 59.365  ? 71  HIS   A CD2  1 ? 2 
ATOM   2659 C CE1  . HIS   B 1 59  ? -1.864 -22.333 27.06   1 57.483  ? 71  HIS   A CE1  1 ? 2 
ATOM   2660 N NE2  . HIS   B 1 59  ? -2.094 -23.615 26.868  1 59.396  ? 71  HIS   A NE2  1 ? 2 
ATOM   2661 H H    . HIS   B 1 59  ? -1.595 -21.203 23.35   1 57.086  ? 71  HIS   A H    1 c 2 
ATOM   2662 H HA   . HIS   B 1 59  ? -2.921 -23.403 22.691  1 63.711  ? 71  HIS   A HA   1 c 2 
ATOM   2663 H HB2  . HIS   B 1 59  ? -4.006 -21.152 24.041  1 62.916  ? 71  HIS   A HB2  1 c 2 
ATOM   2664 H HB3  . HIS   B 1 59  ? -4.713 -22.574 23.982  1 65.975  ? 71  HIS   A HB3  1 c 2 
ATOM   2665 H HD1  . HIS   B 1 59  ? -2.38  -20.751 26.043  0 30      ? 71  HIS   A HD1  1 c 2 
ATOM   2666 H HD2  . HIS   B 1 59  ? -3.139 -24.592 25.379  1 62.552  ? 71  HIS   A HD2  1 c 2 
ATOM   2667 H HE1  . HIS   B 1 59  ? -1.374 -21.957 27.771  1 56.752  ? 71  HIS   A HE1  1 c 2 
ATOM   2668 H HE2  . HIS   B 1 59  ? -1.784 -24.232 27.446  0 30      ? 71  HIS   A HE2  1 c 2 
ATOM   2669 N N    . ASP   B 1 60  ? -3.741 -20.9   20.851  1 68.568  ? 72  ASP   A N    1 ? 2 
ATOM   2670 C CA   . ASP   B 1 60  ? -4.367 -20.531 19.58   1 74.727  ? 72  ASP   A CA   1 ? 2 
ATOM   2671 C C    . ASP   B 1 60  ? -4.013 -21.535 18.479  1 77.347  ? 72  ASP   A C    1 ? 2 
ATOM   2672 O O    . ASP   B 1 60  ? -4.847 -21.861 17.652  1 74.683  ? 72  ASP   A O    1 ? 2 
ATOM   2673 C CB   . ASP   B 1 60  ? -3.929 -19.173 19.032  1 73.479  ? 72  ASP   A CB   1 ? 2 
ATOM   2674 C CG   . ASP   B 1 60  ? -4.026 -17.953 19.942  1 71.067  ? 72  ASP   A CG   1 ? 2 
ATOM   2675 O OD1  . ASP   B 1 60  ? -5.045 -17.818 20.651  1 72.27   ? 72  ASP   A OD1  1 ? 2 
ATOM   2676 O OD2  . ASP   B 1 60  ? -3.093 -17.112 19.903  1 65.156  ? 72  ASP   A OD2  1 ? 2 
ATOM   2677 H H    . ASP   B 1 60  ? -3.247 -20.271 21.293  1 66.012  ? 72  ASP   A H    1 c 2 
ATOM   2678 H HA   . ASP   B 1 60  ? -5.344 -20.523 19.703  1 75.979  ? 72  ASP   A HA   1 c 2 
ATOM   2679 H HB2  . ASP   B 1 60  ? -2.997 -19.248 18.74   1 71.852  ? 72  ASP   A HB2  1 c 2 
ATOM   2680 H HB3  . ASP   B 1 60  ? -4.469 -18.984 18.236  1 75.181  ? 72  ASP   A HB3  1 c 2 
ATOM   2681 N N    . ARG   B 1 61  ? -2.754 -21.988 18.442  1 82.357  ? 73  ARG   A N    1 ? 2 
ATOM   2682 C CA   . ARG   B 1 61  ? -2.314 -22.979 17.466  1 84.955  ? 73  ARG   A CA   1 ? 2 
ATOM   2683 C C    . ARG   B 1 61  ? -2.725 -24.386 17.912  1 84.336  ? 73  ARG   A C    1 ? 2 
ATOM   2684 O O    . ARG   B 1 61  ? -2.637 -25.331 17.136  1 92.319  ? 73  ARG   A O    1 ? 2 
ATOM   2685 C CB   . ARG   B 1 61  ? -0.797 -22.88  17.242  1 83.385  ? 73  ARG   A CB   1 ? 2 
ATOM   2686 H H    . ARG   B 1 61  ? -2.148 -21.668 19.047  1 78.373  ? 73  ARG   A H    1 c 2 
ATOM   2687 H HA   . ARG   B 1 61  ? -2.762 -22.784 16.604  1 86.132  ? 73  ARG   A HA   1 c 2 
ATOM   2688 H HB2  . ARG   B 1 61  ? -0.357 -23.183 17.888  0 30      ? 73  ARG   A HB2  1 c 2 
ATOM   2689 H HB3  . ARG   B 1 61  ? -0.783 -22.311 16.302  0 30      ? 73  ARG   A HB3  1 c 2 
ATOM   2690 N N    . ASN   B 1 62  ? -3.152 -24.527 19.176  1 81.668  ? 74  ASN   A N    1 ? 2 
ATOM   2691 C CA   . ASN   B 1 62  ? -3.494 -25.814 19.77   1 79.856  ? 74  ASN   A CA   1 ? 2 
ATOM   2692 C C    . ASN   B 1 62  ? -2.275 -26.749 19.754  1 76.197  ? 74  ASN   A C    1 ? 2 
ATOM   2693 O O    . ASN   B 1 62  ? -2.413 -27.929 19.454  1 72.168  ? 74  ASN   A O    1 ? 2 
ATOM   2694 C CB   . ASN   B 1 62  ? -4.74  -26.408 19.108  1 83.636  ? 74  ASN   A CB   1 ? 2 
ATOM   2695 H H    . ASN   B 1 62  ? -3.22  -23.784 19.701  1 79.551  ? 74  ASN   A H    1 c 2 
ATOM   2696 H HA   . ASN   B 1 62  ? -3.724 -25.65  20.713  1 78.891  ? 74  ASN   A HA   1 c 2 
ATOM   2697 H HB2  . ASN   B 1 62  ? -4.508 -27.063 18.513  0 30      ? 74  ASN   A HB2  1 c 2 
ATOM   2698 H HB3  . ASN   B 1 62  ? -5.557 -25.998 19.599  0 30      ? 74  ASN   A HB3  1 c 2 
ATOM   2699 N N    . GLU   B 1 63  ? -1.085 -26.225 20.088  1 74.673  ? 75  GLU   A N    1 ? 2 
ATOM   2700 C CA   . GLU   B 1 63  ? 0.148  -27.001 20      1 78.638  ? 75  GLU   A CA   1 ? 2 
ATOM   2701 C C    . GLU   B 1 63  ? 1.237  -26.386 20.888  1 69.665  ? 75  GLU   A C    1 ? 2 
ATOM   2702 O O    . GLU   B 1 63  ? 1.414  -25.171 20.909  1 63.547  ? 75  GLU   A O    1 ? 2 
ATOM   2703 C CB   . GLU   B 1 63  ? 0.62   -27.123 18.543  1 80.109  ? 75  GLU   A CB   1 ? 2 
ATOM   2704 H H    . GLU   B 1 63  ? -1.041 -25.361 20.382  1 73.35   ? 75  GLU   A H    1 c 2 
ATOM   2705 H HA   . GLU   B 1 63  ? -0.046 -27.912 20.328  1 78.086  ? 75  GLU   A HA   1 c 2 
ATOM   2706 H HB2  . GLU   B 1 63  ? 1.553  -27.11  18.444  0 30      ? 75  GLU   A HB2  1 c 2 
ATOM   2707 H HB3  . GLU   B 1 63  ? -0.237 -27.161 17.954  0 30      ? 75  GLU   A HB3  1 c 2 
ATOM   2708 N N    . PRO   B 1 64  ? 2.009  -27.205 21.646  1 67.305  ? 76  PRO   A N    1 ? 2 
ATOM   2709 C CA   . PRO   B 1 64  ? 3.201  -26.714 22.328  1 60.966  ? 76  PRO   A CA   1 ? 2 
ATOM   2710 C C    . PRO   B 1 64  ? 4.177  -26.041 21.372  1 59.491  ? 76  PRO   A C    1 ? 2 
ATOM   2711 O O    . PRO   B 1 64  ? 4.314  -26.486 20.239  1 60.41   ? 76  PRO   A O    1 ? 2 
ATOM   2712 C CB   . PRO   B 1 64  ? 3.842  -27.968 22.924  1 63.877  ? 76  PRO   A CB   1 ? 2 
ATOM   2713 C CG   . PRO   B 1 64  ? 2.678  -28.95  23.036  1 66.536  ? 76  PRO   A CG   1 ? 2 
ATOM   2714 C CD   . PRO   B 1 64  ? 1.786  -28.649 21.854  1 69.029  ? 76  PRO   A CD   1 ? 2 
ATOM   2715 H HA   . PRO   B 1 64  ? 2.944  -26.092 23.04   1 60.418  ? 76  PRO   A HA   1 c 2 
ATOM   2716 H HB2  . PRO   B 1 64  ? 4.539  -28.319 22.336  1 64.014  ? 76  PRO   A HB2  1 c 2 
ATOM   2717 H HB3  . PRO   B 1 64  ? 4.228  -27.78  23.801  1 62.044  ? 76  PRO   A HB3  1 c 2 
ATOM   2718 H HG2  . PRO   B 1 64  ? 2.997  -29.873 22.999  1 68.4    ? 76  PRO   A HG2  1 c 2 
ATOM   2719 H HG3  . PRO   B 1 64  ? 2.192  -28.818 23.874  1 66.38   ? 76  PRO   A HG3  1 c 2 
ATOM   2720 H HD2  . PRO   B 1 64  ? 2.052  -29.16  21.064  1 70.602  ? 76  PRO   A HD2  1 c 2 
ATOM   2721 H HD3  . PRO   B 1 64  ? 0.85   -28.832 22.06   1 70.397  ? 76  PRO   A HD3  1 c 2 
ATOM   2722 N N    . PHE   B 1 65  ? 4.781  -24.93  21.827  1 54.119  ? 77  PHE   A N    1 ? 2 
ATOM   2723 C CA   . PHE   B 1 65  ? 5.896  -24.313 21.142  1 52.296  ? 77  PHE   A CA   1 ? 2 
ATOM   2724 C C    . PHE   B 1 65  ? 7.181  -25.027 21.568  1 53.964  ? 77  PHE   A C    1 ? 2 
ATOM   2725 O O    . PHE   B 1 65  ? 7.418  -25.233 22.752  1 47.217  ? 77  PHE   A O    1 ? 2 
ATOM   2726 C CB   . PHE   B 1 65  ? 5.856  -22.821 21.475  1 48.25   ? 77  PHE   A CB   1 ? 2 
ATOM   2727 C CG   . PHE   B 1 65  ? 6.908  -21.988 20.76   1 48.965  ? 77  PHE   A CG   1 ? 2 
ATOM   2728 C CD1  . PHE   B 1 65  ? 6.679  -21.502 19.477  1 53.996  ? 77  PHE   A CD1  1 ? 2 
ATOM   2729 C CD2  . PHE   B 1 65  ? 8.103  -21.649 21.388  1 46.299  ? 77  PHE   A CD2  1 ? 2 
ATOM   2730 C CE1  . PHE   B 1 65  ? 7.635  -20.734 18.829  1 54.15   ? 77  PHE   A CE1  1 ? 2 
ATOM   2731 C CE2  . PHE   B 1 65  ? 9.06   -20.896 20.726  1 48.646  ? 77  PHE   A CE2  1 ? 2 
ATOM   2732 C CZ   . PHE   B 1 65  ? 8.824  -20.44  19.448  1 48.272  ? 77  PHE   A CZ   1 ? 2 
ATOM   2733 H H    . PHE   B 1 65  ? 4.48   -24.549 22.601  1 53.554  ? 77  PHE   A H    1 c 2 
ATOM   2734 H HA   . PHE   B 1 65  ? 5.771  -24.425 20.162  1 53.773  ? 77  PHE   A HA   1 c 2 
ATOM   2735 H HB2  . PHE   B 1 65  ? 4.966  -22.474 21.243  1 49.422  ? 77  PHE   A HB2  1 c 2 
ATOM   2736 H HB3  . PHE   B 1 65  ? 5.975  -22.715 22.445  1 47.986  ? 77  PHE   A HB3  1 c 2 
ATOM   2737 H HD1  . PHE   B 1 65  ? 5.869  -21.711 19.038  1 54.405  ? 77  PHE   A HD1  1 c 2 
ATOM   2738 H HD2  . PHE   B 1 65  ? 8.279  -21.971 22.258  1 46.918  ? 77  PHE   A HD2  1 c 2 
ATOM   2739 H HE1  . PHE   B 1 65  ? 7.472  -20.425 17.952  1 53.55   ? 77  PHE   A HE1  1 c 2 
ATOM   2740 H HE2  . PHE   B 1 65  ? 9.872  -20.685 21.158  1 46.825  ? 77  PHE   A HE2  1 c 2 
ATOM   2741 H HZ   . PHE   B 1 65  ? 9.47   -19.912 19.007  1 49.141  ? 77  PHE   A HZ   1 c 2 
ATOM   2742 N N    . VAL   B 1 66  ? 8.018  -25.378 20.581  1 58.442  ? 78  VAL   A N    1 ? 2 
ATOM   2743 C CA   . VAL   B 1 66  ? 9.238  -26.146 20.8    1 58.619  ? 78  VAL   A CA   1 ? 2 
ATOM   2744 C C    . VAL   B 1 66  ? 10.423 -25.358 20.26   1 53.25   ? 78  VAL   A C    1 ? 2 
ATOM   2745 O O    . VAL   B 1 66  ? 10.295 -24.724 19.23   1 60.394  ? 78  VAL   A O    1 ? 2 
ATOM   2746 C CB   . VAL   B 1 66  ? 9.149  -27.522 20.113  1 64.539  ? 78  VAL   A CB   1 ? 2 
ATOM   2747 C CG1  . VAL   B 1 66  ? 10.522 -28.165 19.973  1 64.553  ? 78  VAL   A CG1  1 ? 2 
ATOM   2748 C CG2  . VAL   B 1 66  ? 8.165  -28.456 20.816  1 66.511  ? 78  VAL   A CG2  1 ? 2 
ATOM   2749 H H    . VAL   B 1 66  ? 7.818  -25.123 19.727  1 58.013  ? 78  VAL   A H    1 c 2 
ATOM   2750 H HA   . VAL   B 1 66  ? 9.358  -26.281 21.757  1 57.514  ? 78  VAL   A HA   1 c 2 
ATOM   2751 H HB   . VAL   B 1 66  ? 8.805  -27.365 19.203  1 64.773  ? 78  VAL   A HB   1 c 2 
ATOM   2752 H HG11 . VAL   B 1 66  ? 10.986 -28.129 20.827  1 63.854  ? 78  VAL   A HG11 1 c 2 
ATOM   2753 H HG12 . VAL   B 1 66  ? 11.041 -27.689 19.303  1 64.637  ? 78  VAL   A HG12 1 c 2 
ATOM   2754 H HG13 . VAL   B 1 66  ? 10.42  -29.092 19.7    1 67.107  ? 78  VAL   A HG13 1 c 2 
ATOM   2755 H HG21 . VAL   B 1 66  ? 8.207  -29.339 20.411  1 68.551  ? 78  VAL   A HG21 1 c 2 
ATOM   2756 H HG22 . VAL   B 1 66  ? 7.264  -28.103 20.731  1 66.105  ? 78  VAL   A HG22 1 c 2 
ATOM   2757 H HG23 . VAL   B 1 66  ? 8.398  -28.521 21.757  1 65.419  ? 78  VAL   A HG23 1 c 2 
ATOM   2758 N N    . PHE   B 1 67  ? 11.567 -25.393 20.957  1 50.788  ? 79  PHE   A N    1 ? 2 
ATOM   2759 C CA   . PHE   B 1 67  ? 12.759 -24.679 20.52   1 48.044  ? 79  PHE   A CA   1 ? 2 
ATOM   2760 C C    . PHE   B 1 67  ? 14     -25.225 21.237  1 50.409  ? 79  PHE   A C    1 ? 2 
ATOM   2761 O O    . PHE   B 1 67  ? 13.913 -25.879 22.282  1 51.248  ? 79  PHE   A O    1 ? 2 
ATOM   2762 C CB   . PHE   B 1 67  ? 12.593 -23.164 20.684  1 46.049  ? 79  PHE   A CB   1 ? 2 
ATOM   2763 C CG   . PHE   B 1 67  ? 12.782 -22.597 22.083  1 44.934  ? 79  PHE   A CG   1 ? 2 
ATOM   2764 C CD1  . PHE   B 1 67  ? 11.791 -22.73  23.056  1 44.827  ? 79  PHE   A CD1  1 ? 2 
ATOM   2765 C CD2  . PHE   B 1 67  ? 13.945 -21.906 22.418  1 47.264  ? 79  PHE   A CD2  1 ? 2 
ATOM   2766 C CE1  . PHE   B 1 67  ? 11.966 -22.198 24.33   1 42.825  ? 79  PHE   A CE1  1 ? 2 
ATOM   2767 C CE2  . PHE   B 1 67  ? 14.121 -21.386 23.696  1 45.445  ? 79  PHE   A CE2  1 ? 2 
ATOM   2768 C CZ   . PHE   B 1 67  ? 13.135 -21.549 24.652  1 44.236  ? 79  PHE   A CZ   1 ? 2 
ATOM   2769 H H    . PHE   B 1 67  ? 11.604 -25.877 21.731  1 50.931  ? 79  PHE   A H    1 c 2 
ATOM   2770 H HA   . PHE   B 1 67  ? 12.873 -24.862 19.55   1 50.233  ? 79  PHE   A HA   1 c 2 
ATOM   2771 H HB2  . PHE   B 1 67  ? 13.233 -22.723 20.082  1 46.2    ? 79  PHE   A HB2  1 c 2 
ATOM   2772 H HB3  . PHE   B 1 67  ? 11.695 -22.918 20.37   1 46.047  ? 79  PHE   A HB3  1 c 2 
ATOM   2773 H HD1  . PHE   B 1 67  ? 10.992 -23.187 22.846  1 45.385  ? 79  PHE   A HD1  1 c 2 
ATOM   2774 H HD2  . PHE   B 1 67  ? 14.629 -21.807 21.775  1 46.894  ? 79  PHE   A HD2  1 c 2 
ATOM   2775 H HE1  . PHE   B 1 67  ? 11.293 -22.308 24.982  1 43.285  ? 79  PHE   A HE1  1 c 2 
ATOM   2776 H HE2  . PHE   B 1 67  ? 14.919 -20.931 23.913  1 44.962  ? 79  PHE   A HE2  1 c 2 
ATOM   2777 H HZ   . PHE   B 1 67  ? 13.249 -21.183 25.515  1 43.102  ? 79  PHE   A HZ   1 c 2 
ATOM   2778 N N    . SER   B 1 68  ? 15.164 -24.972 20.627  1 48.606  ? 80  SER   A N    1 ? 2 
ATOM   2779 C CA   . SER   B 1 68  ? 16.453 -25.341 21.186  1 48.58   ? 80  SER   A CA   1 ? 2 
ATOM   2780 C C    . SER   B 1 68  ? 16.986 -24.162 21.987  1 44.828  ? 80  SER   A C    1 ? 2 
ATOM   2781 O O    . SER   B 1 68  ? 17.171 -23.07  21.452  1 45.736  ? 80  SER   A O    1 ? 2 
ATOM   2782 C CB   . SER   B 1 68  ? 17.409 -25.759 20.106  1 50.033  ? 80  SER   A CB   1 ? 2 
ATOM   2783 O OG   . SER   B 1 68  ? 16.857 -26.843 19.376  1 57.66   ? 80  SER   A OG   1 ? 2 
ATOM   2784 H H    . SER   B 1 68  ? 15.15  -24.546 19.819  1 49.016  ? 80  SER   A H    1 c 2 
ATOM   2785 H HA   . SER   B 1 68  ? 16.32  -26.106 21.798  1 49.062  ? 80  SER   A HA   1 c 2 
ATOM   2786 H HB2  . SER   B 1 68  ? 17.573 -25.007 19.505  1 50.82   ? 80  SER   A HB2  1 c 2 
ATOM   2787 H HB3  . SER   B 1 68  ? 18.257 -26.029 20.506  1 52.206  ? 80  SER   A HB3  1 c 2 
ATOM   2788 H HG   . SER   B 1 68  ? 17.472 -27.105 18.778  0 30      ? 80  SER   A HG   1 c 2 
ATOM   2789 N N    . LEU   B 1 69  ? 17.212 -24.394 23.282  1 45.039  ? 81  LEU   A N    1 ? 2 
ATOM   2790 C CA   . LEU   B 1 69  ? 17.546 -23.333 24.221  1 40.281  ? 81  LEU   A CA   1 ? 2 
ATOM   2791 C C    . LEU   B 1 69  ? 18.922 -22.755 23.923  1 42.053  ? 81  LEU   A C    1 ? 2 
ATOM   2792 O O    . LEU   B 1 69  ? 19.888 -23.491 23.731  1 45.785  ? 81  LEU   A O    1 ? 2 
ATOM   2793 C CB   . LEU   B 1 69  ? 17.505 -23.934 25.619  1 39.551  ? 81  LEU   A CB   1 ? 2 
ATOM   2794 C CG   . LEU   B 1 69  ? 17.714 -22.967 26.783  1 39.359  ? 81  LEU   A CG   1 ? 2 
ATOM   2795 C CD1  . LEU   B 1 69  ? 16.673 -21.872 26.782  1 37.691  ? 81  LEU   A CD1  1 ? 2 
ATOM   2796 C CD2  . LEU   B 1 69  ? 17.702 -23.659 28.117  1 40.088  ? 81  LEU   A CD2  1 ? 2 
ATOM   2797 H H    . LEU   B 1 69  ? 17.161 -25.252 23.594  1 45.375  ? 81  LEU   A H    1 c 2 
ATOM   2798 H HA   . LEU   B 1 69  ? 16.863 -22.62  24.144  1 39.41   ? 81  LEU   A HA   1 c 2 
ATOM   2799 H HB2  . LEU   B 1 69  ? 16.632 -24.375 25.737  1 40.072  ? 81  LEU   A HB2  1 c 2 
ATOM   2800 H HB3  . LEU   B 1 69  ? 18.196 -24.635 25.671  1 41.753  ? 81  LEU   A HB3  1 c 2 
ATOM   2801 H HG   . LEU   B 1 69  ? 18.603 -22.541 26.673  1 39.434  ? 81  LEU   A HG   1 c 2 
ATOM   2802 H HD11 . LEU   B 1 69  ? 16.802 -21.3   26.007  1 37.08   ? 81  LEU   A HD11 1 c 2 
ATOM   2803 H HD12 . LEU   B 1 69  ? 16.759 -21.342 27.592  1 36.891  ? 81  LEU   A HD12 1 c 2 
ATOM   2804 H HD13 . LEU   B 1 69  ? 15.786 -22.267 26.747  1 37.465  ? 81  LEU   A HD13 1 c 2 
ATOM   2805 H HD21 . LEU   B 1 69  ? 18.335 -24.397 28.107  1 41.8    ? 81  LEU   A HD21 1 c 2 
ATOM   2806 H HD22 . LEU   B 1 69  ? 16.81  -23.999 28.296  1 39.953  ? 81  LEU   A HD22 1 c 2 
ATOM   2807 H HD23 . LEU   B 1 69  ? 17.952 -23.028 28.813  1 39.495  ? 81  LEU   A HD23 1 c 2 
ATOM   2808 N N    . GLY   B 1 70  ? 18.993 -21.421 23.907  1 44.742  ? 82  GLY   A N    1 ? 2 
ATOM   2809 C CA   . GLY   B 1 70  ? 20.262 -20.717 23.823  1 43.114  ? 82  GLY   A CA   1 ? 2 
ATOM   2810 C C    . GLY   B 1 70  ? 20.83  -20.646 22.405  1 46.862  ? 82  GLY   A C    1 ? 2 
ATOM   2811 O O    . GLY   B 1 70  ? 21.985 -20.257 22.263  1 56.126  ? 82  GLY   A O    1 ? 2 
ATOM   2812 H H    . GLY   B 1 70  ? 18.222 -20.933 23.951  1 41.759  ? 82  GLY   A H    1 c 2 
ATOM   2813 H HA2  . GLY   B 1 70  ? 20.139 -19.802 24.167  1 42.802  ? 82  GLY   A HA2  1 c 2 
ATOM   2814 H HA3  . GLY   B 1 70  ? 20.914 -21.168 24.409  1 45.247  ? 82  GLY   A HA3  1 c 2 
ATOM   2815 N N    . LYS   B 1 71  ? 20.065 -21.018 21.369  1 46.861  ? 83  LYS   A N    1 ? 2 
ATOM   2816 C CA   . LYS   B 1 71  ? 20.543 -20.924 19.99   1 51.616  ? 83  LYS   A CA   1 ? 2 
ATOM   2817 C C    . LYS   B 1 71  ? 19.95  -19.693 19.287  1 53.964  ? 83  LYS   A C    1 ? 2 
ATOM   2818 O O    . LYS   B 1 71  ? 20.194 -19.486 18.114  1 55.053  ? 83  LYS   A O    1 ? 2 
ATOM   2819 C CB   . LYS   B 1 71  ? 20.242 -22.213 19.213  1 51.517  ? 83  LYS   A CB   1 ? 2 
ATOM   2820 H H    . LYS   B 1 71  ? 19.22  -21.33  21.521  1 47.1    ? 83  LYS   A H    1 c 2 
ATOM   2821 H HA   . LYS   B 1 71  ? 21.528 -20.817 20.012  1 52.186  ? 83  LYS   A HA   1 c 2 
ATOM   2822 H HB2  . LYS   B 1 71  ? 21.141 -22.615 18.963  0 30      ? 83  LYS   A HB2  1 c 2 
ATOM   2823 H HB3  . LYS   B 1 71  ? 19.315 -22.316 19.145  0 30      ? 83  LYS   A HB3  1 c 2 
ATOM   2824 N N    . GLY   B 1 72  ? 19.17  -18.865 19.992  1 56.692  ? 84  GLY   A N    1 ? 2 
ATOM   2825 C CA   . GLY   B 1 72  ? 18.648 -17.641 19.402  1 56.75   ? 84  GLY   A CA   1 ? 2 
ATOM   2826 C C    . GLY   B 1 72  ? 17.575 -17.878 18.334  1 53.293  ? 84  GLY   A C    1 ? 2 
ATOM   2827 O O    . GLY   B 1 72  ? 17.335 -17.031 17.481  1 50.15   ? 84  GLY   A O    1 ? 2 
ATOM   2828 H H    . GLY   B 1 72  ? 18.955 -19.065 20.858  1 54.709  ? 84  GLY   A H    1 c 2 
ATOM   2829 H HA2  . GLY   B 1 72  ? 18.268 -17.083 20.12   1 54.099  ? 84  GLY   A HA2  1 c 2 
ATOM   2830 H HA3  . GLY   B 1 72  ? 19.396 -17.139 19.001  1 56.042  ? 84  GLY   A HA3  1 c 2 
ATOM   2831 N N    . GLN   B 1 73  ? 16.826 -18.972 18.463  1 52.62   ? 85  GLN   A N    1 ? 2 
ATOM   2832 C CA   . GLN   B 1 73  ? 15.58  -19.131 17.727  1 47.168  ? 85  GLN   A CA   1 ? 2 
ATOM   2833 C C    . GLN   B 1 73  ? 14.452 -18.294 18.338  1 45.674  ? 85  GLN   A C    1 ? 2 
ATOM   2834 O O    . GLN   B 1 73  ? 13.424 -18.07  17.701  1 48.471  ? 85  GLN   A O    1 ? 2 
ATOM   2835 C CB   . GLN   B 1 73  ? 15.202 -20.598 17.757  1 49.098  ? 85  GLN   A CB   1 ? 2 
ATOM   2836 C CG   . GLN   B 1 73  ? 16.247 -21.491 17.108  1 53.023  ? 85  GLN   A CG   1 ? 2 
ATOM   2837 C CD   . GLN   B 1 73  ? 15.989 -22.961 17.364  1 52.956  ? 85  GLN   A CD   1 ? 2 
ATOM   2838 O OE1  . GLN   B 1 73  ? 15.104 -23.326 18.139  1 47.878  ? 85  GLN   A OE1  1 ? 2 
ATOM   2839 N NE2  . GLN   B 1 73  ? 16.774 -23.806 16.714  1 55.408  ? 85  GLN   A NE2  1 ? 2 
ATOM   2840 H H    . GLN   B 1 73  ? 17.088 -19.634 19.035  1 51.796  ? 85  GLN   A H    1 c 2 
ATOM   2841 H HA   . GLN   B 1 73  ? 15.725 -18.847 16.788  1 49.3    ? 85  GLN   A HA   1 c 2 
ATOM   2842 H HB2  . GLN   B 1 73  ? 15.078 -20.872 18.69   1 48.578  ? 85  GLN   A HB2  1 c 2 
ATOM   2843 H HB3  . GLN   B 1 73  ? 14.346 -20.716 17.293  1 49.744  ? 85  GLN   A HB3  1 c 2 
ATOM   2844 H HG2  . GLN   B 1 73  ? 16.252 -21.334 16.14   1 53.341  ? 85  GLN   A HG2  1 c 2 
ATOM   2845 H HG3  . GLN   B 1 73  ? 17.135 -21.261 17.453  1 52.118  ? 85  GLN   A HG3  1 c 2 
ATOM   2846 H HE21 . GLN   B 1 73  ? 16.616 -24.678 16.757  1 56.751  ? 85  GLN   A HE21 1 c 2 
ATOM   2847 H HE22 . GLN   B 1 73  ? 17.458 -23.502 16.238  1 56.064  ? 85  GLN   A HE22 1 c 2 
ATOM   2848 N N    . VAL   B 1 74  ? 14.65  -17.82  19.571  1 39.341  ? 86  VAL   A N    1 ? 2 
ATOM   2849 C CA   . VAL   B 1 74  ? 13.728 -16.923 20.231  1 36.942  ? 86  VAL   A CA   1 ? 2 
ATOM   2850 C C    . VAL   B 1 74  ? 14.468 -15.664 20.674  1 34.149  ? 86  VAL   A C    1 ? 2 
ATOM   2851 O O    . VAL   B 1 74  ? 15.679 -15.591 20.602  1 38.74   ? 86  VAL   A O    1 ? 2 
ATOM   2852 C CB   . VAL   B 1 74  ? 13.117 -17.694 21.414  1 39.077  ? 86  VAL   A CB   1 ? 2 
ATOM   2853 C CG1  . VAL   B 1 74  ? 12.181 -18.794 20.912  1 40.115  ? 86  VAL   A CG1  1 ? 2 
ATOM   2854 C CG2  . VAL   B 1 74  ? 14.198 -18.276 22.336  1 39.032  ? 86  VAL   A CG2  1 ? 2 
ATOM   2855 H H    . VAL   B 1 74  ? 15.406 -18.068 20.02   1 40.489  ? 86  VAL   A H    1 c 2 
ATOM   2856 H HA   . VAL   B 1 74  ? 13.017 -16.674 19.609  1 37.493  ? 86  VAL   A HA   1 c 2 
ATOM   2857 H HB   . VAL   B 1 74  ? 12.582 -17.052 21.937  1 37.504  ? 86  VAL   A HB   1 c 2 
ATOM   2858 H HG11 . VAL   B 1 74  ? 12.687 -19.439 20.39   1 41.376  ? 86  VAL   A HG11 1 c 2 
ATOM   2859 H HG12 . VAL   B 1 74  ? 11.487 -18.402 20.356  1 40.277  ? 86  VAL   A HG12 1 c 2 
ATOM   2860 H HG13 . VAL   B 1 74  ? 11.772 -19.243 21.671  1 40.051  ? 86  VAL   A HG13 1 c 2 
ATOM   2861 H HG21 . VAL   B 1 74  ? 13.782 -18.617 23.145  1 38.803  ? 86  VAL   A HG21 1 c 2 
ATOM   2862 H HG22 . VAL   B 1 74  ? 14.836 -17.582 22.571  1 38.524  ? 86  VAL   A HG22 1 c 2 
ATOM   2863 H HG23 . VAL   B 1 74  ? 14.659 -19.001 21.883  1 40.252  ? 86  VAL   A HG23 1 c 2 
ATOM   2864 N N    . ILE   B 1 75  ? 13.732 -14.664 21.14   1 35.023  ? 87  ILE   A N    1 ? 2 
ATOM   2865 C CA   . ILE   B 1 75  ? 14.328 -13.47  21.722  1 37.681  ? 87  ILE   A CA   1 ? 2 
ATOM   2866 C C    . ILE   B 1 75  ? 15.182 -13.86  22.937  1 36.581  ? 87  ILE   A C    1 ? 2 
ATOM   2867 O O    . ILE   B 1 75  ? 14.913 -14.881 23.585  1 35.872  ? 87  ILE   A O    1 ? 2 
ATOM   2868 C CB   . ILE   B 1 75  ? 13.224 -12.469 22.117  1 36.01   ? 87  ILE   A CB   1 ? 2 
ATOM   2869 C CG1  . ILE   B 1 75  ? 12.241 -13.071 23.119  1 32.531  ? 87  ILE   A CG1  1 ? 2 
ATOM   2870 C CG2  . ILE   B 1 75  ? 12.532 -11.949 20.865  1 36.37   ? 87  ILE   A CG2  1 ? 2 
ATOM   2871 C CD1  . ILE   B 1 75  ? 11.249 -12.09  23.684  1 31.868  ? 87  ILE   A CD1  1 ? 2 
ATOM   2872 H H    . ILE   B 1 75  ? 12.822 -14.724 21.086  1 35.211  ? 87  ILE   A H    1 c 2 
ATOM   2873 H HA   . ILE   B 1 75  ? 14.903 -13.052 21.053  1 37.089  ? 87  ILE   A HA   1 c 2 
ATOM   2874 H HB   . ILE   B 1 75  ? 13.66  -11.711 22.552  1 35.13   ? 87  ILE   A HB   1 c 2 
ATOM   2875 H HG12 . ILE   B 1 75  ? 11.747 -13.794 22.682  1 33.679  ? 87  ILE   A HG12 1 c 2 
ATOM   2876 H HG13 . ILE   B 1 75  ? 12.745 -13.461 23.861  1 33.066  ? 87  ILE   A HG13 1 c 2 
ATOM   2877 H HG21 . ILE   B 1 75  ? 11.912 -11.241 21.104  1 36.018  ? 87  ILE   A HG21 1 c 2 
ATOM   2878 H HG22 . ILE   B 1 75  ? 12.045 -12.672 20.436  1 36.909  ? 87  ILE   A HG22 1 c 2 
ATOM   2879 H HG23 . ILE   B 1 75  ? 13.197 -11.599 20.248  1 36.814  ? 87  ILE   A HG23 1 c 2 
ATOM   2880 H HD11 . ILE   B 1 75  ? 11.724 -11.326 24.062  1 31.59   ? 87  ILE   A HD11 1 c 2 
ATOM   2881 H HD12 . ILE   B 1 75  ? 10.726 -12.524 24.385  1 31.823  ? 87  ILE   A HD12 1 c 2 
ATOM   2882 H HD13 . ILE   B 1 75  ? 10.65  -11.782 22.978  1 32.24   ? 87  ILE   A HD13 1 c 2 
ATOM   2883 N N    . LYS   B 1 76  ? 16.196 -13.024 23.211  1 36.076  ? 88  LYS   A N    1 ? 2 
ATOM   2884 C CA   . LYS   B 1 76  ? 17.219 -13.283 24.228  1 41.204  ? 88  LYS   A CA   1 ? 2 
ATOM   2885 C C    . LYS   B 1 76  ? 16.564 -13.513 25.606  1 36.631  ? 88  LYS   A C    1 ? 2 
ATOM   2886 O O    . LYS   B 1 76  ? 17.001 -14.384 26.347  1 37.196  ? 88  LYS   A O    1 ? 2 
ATOM   2887 C CB   . LYS   B 1 76  ? 18.266 -12.148 24.248  1 38.593  ? 88  LYS   A CB   1 ? 2 
ATOM   2888 H H    . LYS   B 1 76  ? 16.25  -12.246 22.735  1 37.164  ? 88  LYS   A H    1 c 2 
ATOM   2889 H HA   . LYS   B 1 76  ? 17.691 -14.116 23.974  1 39.747  ? 88  LYS   A HA   1 c 2 
ATOM   2890 H HB2  . LYS   B 1 76  ? 19.127 -12.354 24.273  0 30      ? 88  LYS   A HB2  1 c 2 
ATOM   2891 H HB3  . LYS   B 1 76  ? 17.676 -11.192 24.298  0 30      ? 88  LYS   A HB3  1 c 2 
ATOM   2892 N N    . ALA   B 1 77  ? 15.491 -12.772 25.903  1 30.764  ? 89  ALA   A N    1 ? 2 
ATOM   2893 C CA   . ALA   B 1 77  ? 14.769 -12.915 27.168  1 33.915  ? 89  ALA   A CA   1 ? 2 
ATOM   2894 C C    . ALA   B 1 77  ? 14.286 -14.355 27.381  1 35.221  ? 89  ALA   A C    1 ? 2 
ATOM   2895 O O    . ALA   B 1 77  ? 14.234 -14.834 28.529  1 26.041  ? 89  ALA   A O    1 ? 2 
ATOM   2896 C CB   . ALA   B 1 77  ? 13.588 -11.978 27.264  1 28.039  ? 89  ALA   A CB   1 ? 2 
ATOM   2897 H H    . ALA   B 1 77  ? 15.2   -12.148 25.303  1 32.457  ? 89  ALA   A H    1 c 2 
ATOM   2898 H HA   . ALA   B 1 77  ? 15.406 -12.699 27.904  1 32.614  ? 89  ALA   A HA   1 c 2 
ATOM   2899 H HB1  . ALA   B 1 77  ? 13.896 -11.058 27.212  1 29.449  ? 89  ALA   A HB1  1 c 2 
ATOM   2900 H HB2  . ALA   B 1 77  ? 12.973 -12.152 26.532  1 29.45   ? 89  ALA   A HB2  1 c 2 
ATOM   2901 H HB3  . ALA   B 1 77  ? 13.129 -12.115 28.11   1 29.511  ? 89  ALA   A HB3  1 c 2 
ATOM   2902 N N    . TRP   B 1 78  ? 13.892 -15.025 26.286  1 31.856  ? 90  TRP   A N    1 ? 2 
ATOM   2903 C CA   . TRP   B 1 78  ? 13.41  -16.394 26.426  1 33.612  ? 90  TRP   A CA   1 ? 2 
ATOM   2904 C C    . TRP   B 1 78  ? 14.556 -17.359 26.703  1 33.071  ? 90  TRP   A C    1 ? 2 
ATOM   2905 O O    . TRP   B 1 78  ? 14.452 -18.207 27.568  1 35.509  ? 90  TRP   A O    1 ? 2 
ATOM   2906 C CB   . TRP   B 1 78  ? 12.623 -16.846 25.208  1 31.748  ? 90  TRP   A CB   1 ? 2 
ATOM   2907 C CG   . TRP   B 1 78  ? 11.166 -16.558 25.309  1 31.473  ? 90  TRP   A CG   1 ? 2 
ATOM   2908 C CD1  . TRP   B 1 78  ? 10.556 -15.39  25.677  1 31.139  ? 90  TRP   A CD1  1 ? 2 
ATOM   2909 C CD2  . TRP   B 1 78  ? 10.116 -17.515 25.038  1 34.824  ? 90  TRP   A CD2  1 ? 2 
ATOM   2910 N NE1  . TRP   B 1 78  ? 9.192  -15.538 25.605  1 32.726  ? 90  TRP   A NE1  1 ? 2 
ATOM   2911 C CE2  . TRP   B 1 78  ? 8.894  -16.841 25.239  1 33.686  ? 90  TRP   A CE2  1 ? 2 
ATOM   2912 C CE3  . TRP   B 1 78  ? 10.092 -18.853 24.649  1 37.171  ? 90  TRP   A CE3  1 ? 2 
ATOM   2913 C CZ2  . TRP   B 1 78  ? 7.669  -17.478 25.076  1 35.011  ? 90  TRP   A CZ2  1 ? 2 
ATOM   2914 C CZ3  . TRP   B 1 78  ? 8.875  -19.477 24.485  1 37.563  ? 90  TRP   A CZ3  1 ? 2 
ATOM   2915 C CH2  . TRP   B 1 78  ? 7.68   -18.788 24.669  1 35.589  ? 90  TRP   A CH2  1 ? 2 
ATOM   2916 H H    . TRP   B 1 78  ? 13.915 -14.634 25.461  1 32.863  ? 90  TRP   A H    1 c 2 
ATOM   2917 H HA   . TRP   B 1 78  ? 12.794 -16.42  27.208  1 32.452  ? 90  TRP   A HA   1 c 2 
ATOM   2918 H HB2  . TRP   B 1 78  ? 12.983 -16.396 24.414  1 32.302  ? 90  TRP   A HB2  1 c 2 
ATOM   2919 H HB3  . TRP   B 1 78  ? 12.748 -17.813 25.094  1 33.121  ? 90  TRP   A HB3  1 c 2 
ATOM   2920 H HD1  . TRP   B 1 78  ? 10.995 -14.582 25.888  1 30.829  ? 90  TRP   A HD1  1 c 2 
ATOM   2921 H HE1  . TRP   B 1 78  ? 8.611  -14.925 25.807  1 32.204  ? 90  TRP   A HE1  1 c 2 
ATOM   2922 H HE3  . TRP   B 1 78  ? 10.896 -19.324 24.511  1 37.181  ? 90  TRP   A HE3  1 c 2 
ATOM   2923 H HZ2  . TRP   B 1 78  ? 6.86   -17.014 25.201  1 34.803  ? 90  TRP   A HZ2  1 c 2 
ATOM   2924 H HZ3  . TRP   B 1 78  ? 8.852  -20.381 24.217  1 38.395  ? 90  TRP   A HZ3  1 c 2 
ATOM   2925 H HH2  . TRP   B 1 78  ? 6.865  -19.242 24.559  1 37.006  ? 90  TRP   A HH2  1 c 2 
ATOM   2926 N N    . ASP   B 1 79  ? 15.647 -17.21  25.97   1 36.011  ? 91  ASP   A N    1 ? 2 
ATOM   2927 C CA   . ASP   B 1 79  ? 16.839 -18.02  26.184  1 37.966  ? 91  ASP   A CA   1 ? 2 
ATOM   2928 C C    . ASP   B 1 79  ? 17.297 -17.906 27.637  1 38.518  ? 91  ASP   A C    1 ? 2 
ATOM   2929 O O    . ASP   B 1 79  ? 17.552 -18.913 28.295  1 46.013  ? 91  ASP   A O    1 ? 2 
ATOM   2930 C CB   . ASP   B 1 79  ? 17.873 -17.649 25.14   1 38.83   ? 91  ASP   A CB   1 ? 2 
ATOM   2931 C CG   . ASP   B 1 79  ? 17.721 -18.352 23.79   1 38.709  ? 91  ASP   A CG   1 ? 2 
ATOM   2932 O OD1  . ASP   B 1 79  ? 17.098 -19.429 23.738  1 41.647  ? 91  ASP   A OD1  1 ? 2 
ATOM   2933 O OD2  . ASP   B 1 79  ? 18.227 -17.835 22.797  1 37.806  ? 91  ASP   A OD2  1 ? 2 
ATOM   2934 H H    . ASP   B 1 79  ? 15.653 -16.587 25.301  1 35.216  ? 91  ASP   A H    1 c 2 
ATOM   2935 H HA   . ASP   B 1 79  ? 16.594 -18.958 26.025  1 38.699  ? 91  ASP   A HA   1 c 2 
ATOM   2936 H HB2  . ASP   B 1 79  ? 17.846 -16.682 24.987  1 37.757  ? 91  ASP   A HB2  1 c 2 
ATOM   2937 H HB3  . ASP   B 1 79  ? 18.761 -17.869 25.492  1 39.407  ? 91  ASP   A HB3  1 c 2 
ATOM   2938 N N    . ILE   B 1 80  ? 17.369 -16.684 28.155  1 37.791  ? 92  ILE   A N    1 ? 2 
ATOM   2939 C CA   . ILE   B 1 80  ? 17.756 -16.432 29.538  1 42.458  ? 92  ILE   A CA   1 ? 2 
ATOM   2940 C C    . ILE   B 1 80  ? 16.685 -16.935 30.51   1 38.82   ? 92  ILE   A C    1 ? 2 
ATOM   2941 O O    . ILE   B 1 80  ? 16.97  -17.598 31.475  1 46.15   ? 92  ILE   A O    1 ? 2 
ATOM   2942 C CB   . ILE   B 1 80  ? 18.002 -14.921 29.684  1 46.702  ? 92  ILE   A CB   1 ? 2 
ATOM   2943 C CG1  . ILE   B 1 80  ? 19.323 -14.537 29.02   1 50.937  ? 92  ILE   A CG1  1 ? 2 
ATOM   2944 C CG2  . ILE   B 1 80  ? 17.948 -14.466 31.137  1 51.544  ? 92  ILE   A CG2  1 ? 2 
ATOM   2945 C CD1  . ILE   B 1 80  ? 19.396 -13.059 28.658  1 58.79   ? 92  ILE   A CD1  1 ? 2 
ATOM   2946 H H    . ILE   B 1 80  ? 17.172 -15.969 27.621  1 38.105  ? 92  ILE   A H    1 c 2 
ATOM   2947 H HA   . ILE   B 1 80  ? 18.592 -16.904 29.719  1 42.883  ? 92  ILE   A HA   1 c 2 
ATOM   2948 H HB   . ILE   B 1 80  ? 17.287 -14.457 29.204  1 46.131  ? 92  ILE   A HB   1 c 2 
ATOM   2949 H HG12 . ILE   B 1 80  ? 20.058 -14.752 29.63   1 52.937  ? 92  ILE   A HG12 1 c 2 
ATOM   2950 H HG13 . ILE   B 1 80  ? 19.439 -15.07  28.207  1 51.978  ? 92  ILE   A HG13 1 c 2 
ATOM   2951 H HG21 . ILE   B 1 80  ? 18.247 -13.544 31.201  1 50.158  ? 92  ILE   A HG21 1 c 2 
ATOM   2952 H HG22 . ILE   B 1 80  ? 18.528 -15.03  31.677  1 51.157  ? 92  ILE   A HG22 1 c 2 
ATOM   2953 H HG23 . ILE   B 1 80  ? 17.037 -14.531 31.467  1 49.544  ? 92  ILE   A HG23 1 c 2 
ATOM   2954 H HD11 . ILE   B 1 80  ? 18.666 -12.836 28.05   1 55.228  ? 92  ILE   A HD11 1 c 2 
ATOM   2955 H HD12 . ILE   B 1 80  ? 20.249 -12.873 28.222  1 56.857  ? 92  ILE   A HD12 1 c 2 
ATOM   2956 H HD13 . ILE   B 1 80  ? 19.321 -12.517 29.466  1 56.09   ? 92  ILE   A HD13 1 c 2 
ATOM   2957 N N    . GLY   B 1 81  ? 15.43  -16.627 30.238  1 36.466  ? 93  GLY   A N    1 ? 2 
ATOM   2958 C CA   . GLY   B 1 81  ? 14.383 -16.821 31.213  1 35.235  ? 93  GLY   A CA   1 ? 2 
ATOM   2959 C C    . GLY   B 1 81  ? 14.041 -18.293 31.364  1 36.779  ? 93  GLY   A C    1 ? 2 
ATOM   2960 O O    . GLY   B 1 81  ? 13.939 -18.799 32.489  1 31.286  ? 93  GLY   A O    1 ? 2 
ATOM   2961 H H    . GLY   B 1 81  ? 15.214 -16.28  29.42   1 35.96   ? 93  GLY   A H    1 c 2 
ATOM   2962 H HA2  . GLY   B 1 81  ? 14.675 -16.458 32.081  1 36.026  ? 93  GLY   A HA2  1 c 2 
ATOM   2963 H HA3  . GLY   B 1 81  ? 13.581 -16.323 30.929  1 34.931  ? 93  GLY   A HA3  1 c 2 
ATOM   2964 N N    . VAL   B 1 82  ? 13.892 -18.969 30.22   1 34.475  ? 94  VAL   A N    1 ? 2 
ATOM   2965 C CA   . VAL   B 1 82  ? 13.546 -20.372 30.252  1 36.623  ? 94  VAL   A CA   1 ? 2 
ATOM   2966 C C    . VAL   B 1 82  ? 14.668 -21.209 30.876  1 37.724  ? 94  VAL   A C    1 ? 2 
ATOM   2967 O O    . VAL   B 1 82  ? 14.353 -22.191 31.52   1 36.477  ? 94  VAL   A O    1 ? 2 
ATOM   2968 C CB   . VAL   B 1 82  ? 13.105 -20.874 28.866  1 37.409  ? 94  VAL   A CB   1 ? 2 
ATOM   2969 C CG1  . VAL   B 1 82  ? 12.979 -22.394 28.811  1 40.784  ? 94  VAL   A CG1  1 ? 2 
ATOM   2970 C CG2  . VAL   B 1 82  ? 11.744 -20.3   28.527  1 36.097  ? 94  VAL   A CG2  1 ? 2 
ATOM   2971 H H    . VAL   B 1 82  ? 14.002 -18.551 29.414  1 34.788  ? 94  VAL   A H    1 c 2 
ATOM   2972 H HA   . VAL   B 1 82  ? 12.771 -20.456 30.841  1 36.447  ? 94  VAL   A HA   1 c 2 
ATOM   2973 H HB   . VAL   B 1 82  ? 13.768 -20.573 28.203  1 37.368  ? 94  VAL   A HB   1 c 2 
ATOM   2974 H HG11 . VAL   B 1 82  ? 12.452 -22.705 29.566  1 40.607  ? 94  VAL   A HG11 1 c 2 
ATOM   2975 H HG12 . VAL   B 1 82  ? 13.862 -22.798 28.844  1 41.099  ? 94  VAL   A HG12 1 c 2 
ATOM   2976 H HG13 . VAL   B 1 82  ? 12.539 -22.651 27.984  1 40.561  ? 94  VAL   A HG13 1 c 2 
ATOM   2977 H HG21 . VAL   B 1 82  ? 11.47  -20.61  27.648  1 36.572  ? 94  VAL   A HG21 1 c 2 
ATOM   2978 H HG22 . VAL   B 1 82  ? 11.792 -19.329 28.527  1 35.269  ? 94  VAL   A HG22 1 c 2 
ATOM   2979 H HG23 . VAL   B 1 82  ? 11.095 -20.591 29.189  1 36.509  ? 94  VAL   A HG23 1 c 2 
ATOM   2980 N N    . ALA   B 1 83  ? 15.94  -20.786 30.773  1 38.455  ? 95  ALA   A N    1 ? 2 
ATOM   2981 C CA   . ALA   B 1 83  ? 17.052 -21.49  31.416  1 36.275  ? 95  ALA   A CA   1 ? 2 
ATOM   2982 C C    . ALA   B 1 83  ? 16.942 -21.476 32.938  1 39.937  ? 95  ALA   A C    1 ? 2 
ATOM   2983 O O    . ALA   B 1 83  ? 17.634 -22.258 33.6    1 42.484  ? 95  ALA   A O    1 ? 2 
ATOM   2984 C CB   . ALA   B 1 83  ? 18.39  -20.918 31.038  1 34.114  ? 95  ALA   A CB   1 ? 2 
ATOM   2985 H H    . ALA   B 1 83  ? 16.123 -20.038 30.28   1 36.563  ? 95  ALA   A H    1 c 2 
ATOM   2986 H HA   . ALA   B 1 83  ? 17.018 -22.442 31.119  1 38.025  ? 95  ALA   A HA   1 c 2 
ATOM   2987 H HB1  . ALA   B 1 83  ? 18.503 -20.959 30.073  1 34.706  ? 95  ALA   A HB1  1 c 2 
ATOM   2988 H HB2  . ALA   B 1 83  ? 18.444 -19.992 31.328  1 34.045  ? 95  ALA   A HB2  1 c 2 
ATOM   2989 H HB3  . ALA   B 1 83  ? 19.098 -21.43  31.465  1 36.34   ? 95  ALA   A HB3  1 c 2 
ATOM   2990 N N    . THR   B 1 84  ? 16.148 -20.552 33.5    1 39.367  ? 96  THR   A N    1 ? 2 
ATOM   2991 C CA   . THR   B 1 84  ? 15.976 -20.482 34.947  1 40.576  ? 96  THR   A CA   1 ? 2 
ATOM   2992 C C    . THR   B 1 84  ? 14.792 -21.324 35.406  1 37.651  ? 96  THR   A C    1 ? 2 
ATOM   2993 O O    . THR   B 1 84  ? 14.563 -21.367 36.606  1 37.107  ? 96  THR   A O    1 ? 2 
ATOM   2994 C CB   . THR   B 1 84  ? 15.753 -19.042 35.439  1 40.216  ? 96  THR   A CB   1 ? 2 
ATOM   2995 O OG1  . THR   B 1 84  ? 14.449 -18.679 34.99   1 36.789  ? 96  THR   A OG1  1 ? 2 
ATOM   2996 C CG2  . THR   B 1 84  ? 16.772 -18.045 34.917  1 39.836  ? 96  THR   A CG2  1 ? 2 
ATOM   2997 H H    . THR   B 1 84  ? 15.72  -19.938 32.976  1 38.079  ? 96  THR   A H    1 c 2 
ATOM   2998 H HA   . THR   B 1 84  ? 16.79  -20.829 35.373  1 41.266  ? 96  THR   A HA   1 c 2 
ATOM   2999 H HB   . THR   B 1 84  ? 15.771 -19.026 36.426  1 40.594  ? 96  THR   A HB   1 c 2 
ATOM   3000 H HG1  . THR   B 1 84  ? 14.411 -18.678 34.096  0 30      ? 96  THR   A HG1  1 c 2 
ATOM   3001 H HG21 . THR   B 1 84  ? 16.585 -17.166 35.288  1 39.406  ? 96  THR   A HG21 1 c 2 
ATOM   3002 H HG22 . THR   B 1 84  ? 16.72  -18.003 33.949  1 39.012  ? 96  THR   A HG22 1 c 2 
ATOM   3003 H HG23 . THR   B 1 84  ? 17.664 -18.323 35.182  1 41      ? 96  THR   A HG23 1 c 2 
ATOM   3004 N N    . MET   B 1 85  ? 14.026 -21.938 34.483  1 36.22   ? 97  MET   A N    1 ? 2 
ATOM   3005 C CA   . MET   B 1 85  ? 12.773 -22.583 34.869  1 38.13   ? 97  MET   A CA   1 ? 2 
ATOM   3006 C C    . MET   B 1 85  ? 12.95  -24.094 35.089  1 41.182  ? 97  MET   A C    1 ? 2 
ATOM   3007 O O    . MET   B 1 85  ? 13.83  -24.731 34.533  1 38.749  ? 97  MET   A O    1 ? 2 
ATOM   3008 C CB   . MET   B 1 85  ? 11.69  -22.33  33.819  1 36.253  ? 97  MET   A CB   1 ? 2 
ATOM   3009 C CG   . MET   B 1 85  ? 11.252 -20.88  33.731  1 35.556  ? 97  MET   A CG   1 ? 2 
ATOM   3010 S SD   . MET   B 1 85  ? 10.152 -20.565 32.334  1 38.604  ? 97  MET   A SD   1 ? 2 
ATOM   3011 C CE   . MET   B 1 85  ? 8.604  -21.203 33.011  1 42.091  ? 97  MET   A CE   1 ? 2 
ATOM   3012 H H    . MET   B 1 85  ? 14.285 -21.959 33.608  1 36.406  ? 97  MET   A H    1 c 2 
ATOM   3013 H HA   . MET   B 1 85  ? 12.479 -22.185 35.727  1 38.058  ? 97  MET   A HA   1 c 2 
ATOM   3014 H HB2  . MET   B 1 85  ? 12.029 -22.614 32.944  1 36.553  ? 97  MET   A HB2  1 c 2 
ATOM   3015 H HB3  . MET   B 1 85  ? 10.91  -22.885 34.033  1 37.303  ? 97  MET   A HB3  1 c 2 
ATOM   3016 H HG2  . MET   B 1 85  ? 10.79  -20.632 34.553  1 36.31   ? 97  MET   A HG2  1 c 2 
ATOM   3017 H HG3  . MET   B 1 85  ? 12.04  -20.309 33.645  1 35.533  ? 97  MET   A HG3  1 c 2 
ATOM   3018 H HE1  . MET   B 1 85  ? 7.91   -21.161 32.328  1 41.349  ? 97  MET   A HE1  1 c 2 
ATOM   3019 H HE2  . MET   B 1 85  ? 8.729  -22.129 33.29   1 42.596  ? 97  MET   A HE2  1 c 2 
ATOM   3020 H HE3  . MET   B 1 85  ? 8.339  -20.664 33.779  1 41.425  ? 97  MET   A HE3  1 c 2 
ATOM   3021 N N    . LYS   B 1 86  ? 12.062 -24.657 35.913  1 46.079  ? 98  LYS   A N    1 ? 2 
ATOM   3022 C CA   . LYS   B 1 86  ? 11.992 -26.086 36.17   1 50.227  ? 98  LYS   A CA   1 ? 2 
ATOM   3023 C C    . LYS   B 1 86  ? 10.791 -26.669 35.441  1 47.248  ? 98  LYS   A C    1 ? 2 
ATOM   3024 O O    . LYS   B 1 86  ? 9.836  -25.96  35.136  1 44.723  ? 98  LYS   A O    1 ? 2 
ATOM   3025 C CB   . LYS   B 1 86  ? 11.7   -26.425 37.636  1 57.711  ? 98  LYS   A CB   1 ? 2 
ATOM   3026 C CG   . LYS   B 1 86  ? 12.288 -25.516 38.723  1 62.768  ? 98  LYS   A CG   1 ? 2 
ATOM   3027 C CD   . LYS   B 1 86  ? 13.642 -25.948 39.255  1 66.361  ? 98  LYS   A CD   1 ? 2 
ATOM   3028 C CE   . LYS   B 1 86  ? 14.17  -24.964 40.257  1 73.255  ? 98  LYS   A CE   1 ? 2 
ATOM   3029 N NZ   . LYS   B 1 86  ? 15.362 -25.496 40.94   1 80.607  ? 98  LYS   A NZ   1 ? 2 
ATOM   3030 H H    . LYS   B 1 86  ? 11.458 -24.116 36.333  1 45.085  ? 98  LYS   A H    1 c 2 
ATOM   3031 H HA   . LYS   B 1 86  ? 12.825 -26.525 35.86   1 50.772  ? 98  LYS   A HA   1 c 2 
ATOM   3032 H HB2  . LYS   B 1 86  ? 10.726 -26.438 37.755  1 57.243  ? 98  LYS   A HB2  1 c 2 
ATOM   3033 H HB3  . LYS   B 1 86  ? 12.021 -27.337 37.802  1 59.047  ? 98  LYS   A HB3  1 c 2 
ATOM   3034 H HG2  . LYS   B 1 86  ? 12.365 -24.607 38.363  1 60.099  ? 98  LYS   A HG2  1 c 2 
ATOM   3035 H HG3  . LYS   B 1 86  ? 11.652 -25.482 39.471  1 62.509  ? 98  LYS   A HG3  1 c 2 
ATOM   3036 H HD2  . LYS   B 1 86  ? 13.559 -26.83  39.679  1 69.174  ? 98  LYS   A HD2  1 c 2 
ATOM   3037 H HD3  . LYS   B 1 86  ? 14.276 -26.022 38.508  1 67.01   ? 98  LYS   A HD3  1 c 2 
ATOM   3038 H HE2  . LYS   B 1 86  ? 14.406 -24.134 39.806  1 71.19   ? 98  LYS   A HE2  1 c 2 
ATOM   3039 H HE3  . LYS   B 1 86  ? 13.483 -24.768 40.919  1 72.951  ? 98  LYS   A HE3  1 c 2 
ATOM   3040 H HZ1  . LYS   B 1 86  ? 15.957 -25.802 40.329  1 79.027  ? 98  LYS   A HZ1  1 c 2 
ATOM   3041 H HZ2  . LYS   B 1 86  ? 15.122 -26.175 41.488  1 80.543  ? 98  LYS   A HZ2  1 c 2 
ATOM   3042 H HZ3  . LYS   B 1 86  ? 15.75  -24.841 41.432  1 79.119  ? 98  LYS   A HZ3  1 c 2 
ATOM   3043 N N    . LYS   B 1 87  ? 10.847 -27.976 35.18   1 50.601  ? 99  LYS   A N    1 ? 2 
ATOM   3044 C CA   . LYS   B 1 87  ? 9.716  -28.693 34.623  1 51.889  ? 99  LYS   A CA   1 ? 2 
ATOM   3045 C C    . LYS   B 1 87  ? 8.517  -28.447 35.537  1 51.21   ? 99  LYS   A C    1 ? 2 
ATOM   3046 O O    . LYS   B 1 87  ? 8.638  -28.54  36.761  1 50.131  ? 99  LYS   A O    1 ? 2 
ATOM   3047 C CB   . LYS   B 1 87  ? 10.027 -30.176 34.418  1 55.162  ? 99  LYS   A CB   1 ? 2 
ATOM   3048 C CG   . LYS   B 1 87  ? 8.906  -30.95  33.763  1 59.021  ? 99  LYS   A CG   1 ? 2 
ATOM   3049 C CD   . LYS   B 1 87  ? 9.332  -32.373 33.448  1 67.036  ? 99  LYS   A CD   1 ? 2 
ATOM   3050 C CE   . LYS   B 1 87  ? 8.199  -33.27  33.064  1 73.039  ? 99  LYS   A CE   1 ? 2 
ATOM   3051 N NZ   . LYS   B 1 87  ? 7.494  -32.721 31.905  1 74.542  ? 99  LYS   A NZ   1 ? 2 
ATOM   3052 H H    . LYS   B 1 87  ? 11.617 -28.437 35.356  1 51.443  ? 99  LYS   A H    1 c 2 
ATOM   3053 H HA   . LYS   B 1 87  ? 9.517  -28.301 33.735  1 50.593  ? 99  LYS   A HA   1 c 2 
ATOM   3054 H HB2  . LYS   B 1 87  ? 10.83  -30.257 33.86   1 55.556  ? 99  LYS   A HB2  1 c 2 
ATOM   3055 H HB3  . LYS   B 1 87  ? 10.222 -30.584 35.288  1 56.875  ? 99  LYS   A HB3  1 c 2 
ATOM   3056 H HG2  . LYS   B 1 87  ? 8.131  -30.967 34.367  1 59.904  ? 99  LYS   A HG2  1 c 2 
ATOM   3057 H HG3  . LYS   B 1 87  ? 8.645  -30.494 32.934  1 58.423  ? 99  LYS   A HG3  1 c 2 
ATOM   3058 H HD2  . LYS   B 1 87  ? 9.984  -32.353 32.714  1 66.399  ? 99  LYS   A HD2  1 c 2 
ATOM   3059 H HD3  . LYS   B 1 87  ? 9.783  -32.75  34.236  1 67.731  ? 99  LYS   A HD3  1 c 2 
ATOM   3060 H HE2  . LYS   B 1 87  ? 8.538  -34.156 32.844  1 74.687  ? 99  LYS   A HE2  1 c 2 
ATOM   3061 H HE3  . LYS   B 1 87  ? 7.576  -33.353 33.809  1 73.281  ? 99  LYS   A HE3  1 c 2 
ATOM   3062 H HZ1  . LYS   B 1 87  ? 8.09   -32.464 31.275  1 72.483  ? 99  LYS   A HZ1  1 c 2 
ATOM   3063 H HZ2  . LYS   B 1 87  ? 6.99   -32.01  32.151  1 72.065  ? 99  LYS   A HZ2  1 c 2 
ATOM   3064 H HZ3  . LYS   B 1 87  ? 6.952  -33.357 31.553  1 75.134  ? 99  LYS   A HZ3  1 c 2 
ATOM   3065 N N    . GLY   B 1 88  ? 7.401  -28.022 34.922  1 48.755  ? 100 GLY   A N    1 ? 2 
ATOM   3066 C CA   . GLY   B 1 88  ? 6.141  -27.801 35.616  1 46.167  ? 100 GLY   A CA   1 ? 2 
ATOM   3067 C C    . GLY   B 1 88  ? 5.918  -26.335 35.992  1 43.497  ? 100 GLY   A C    1 ? 2 
ATOM   3068 O O    . GLY   B 1 88  ? 4.787  -25.955 36.27   1 42.714  ? 100 GLY   A O    1 ? 2 
ATOM   3069 H H    . GLY   B 1 88  ? 7.43   -27.863 34.022  1 47.689  ? 100 GLY   A H    1 c 2 
ATOM   3070 H HA2  . GLY   B 1 88  ? 5.403  -28.102 35.036  1 47.249  ? 100 GLY   A HA2  1 c 2 
ATOM   3071 H HA3  . GLY   B 1 88  ? 6.123  -28.353 36.433  1 48.218  ? 100 GLY   A HA3  1 c 2 
ATOM   3072 N N    . GLU   B 1 89  ? 6.995  -25.535 35.991  1 41.602  ? 101 GLU   A N    1 ? 2 
ATOM   3073 C CA   . GLU   B 1 89  ? 6.969  -24.129 36.388  1 42.296  ? 101 GLU   A CA   1 ? 2 
ATOM   3074 C C    . GLU   B 1 89  ? 6.114  -23.3   35.424  1 41.678  ? 101 GLU   A C    1 ? 2 
ATOM   3075 O O    . GLU   B 1 89  ? 6.073  -23.533 34.2    1 37.752  ? 101 GLU   A O    1 ? 2 
ATOM   3076 C CB   . GLU   B 1 89  ? 8.402  -23.593 36.517  1 41.734  ? 101 GLU   A CB   1 ? 2 
ATOM   3077 C CG   . GLU   B 1 89  ? 8.548  -22.179 37.079  1 40.885  ? 101 GLU   A CG   1 ? 2 
ATOM   3078 C CD   . GLU   B 1 89  ? 9.978  -21.696 37.278  1 43.062  ? 101 GLU   A CD   1 ? 2 
ATOM   3079 O OE1  . GLU   B 1 89  ? 10.794 -22.474 37.821  1 47.14   ? 101 GLU   A OE1  1 ? 2 
ATOM   3080 O OE2  . GLU   B 1 89  ? 10.329 -20.548 36.873  1 42.673  ? 101 GLU   A OE2  1 ? 2 
ATOM   3081 H H    . GLU   B 1 89  ? 7.795  -25.885 35.724  1 42.301  ? 101 GLU   A H    1 c 2 
ATOM   3082 H HA   . GLU   B 1 89  ? 6.555  -24.082 37.285  1 42.896  ? 101 GLU   A HA   1 c 2 
ATOM   3083 H HB2  . GLU   B 1 89  ? 8.91   -24.204 37.091  1 42.908  ? 101 GLU   A HB2  1 c 2 
ATOM   3084 H HB3  . GLU   B 1 89  ? 8.819  -23.607 35.631  1 40.973  ? 101 GLU   A HB3  1 c 2 
ATOM   3085 H HG2  . GLU   B 1 89  ? 8.094  -21.552 36.477  1 40.307  ? 101 GLU   A HG2  1 c 2 
ATOM   3086 H HG3  . GLU   B 1 89  ? 8.086  -22.134 37.944  1 42.26   ? 101 GLU   A HG3  1 c 2 
ATOM   3087 N N    . ILE   B 1 90  ? 5.374  -22.361 36.031  1 41.415  ? 102 ILE   A N    1 ? 2 
ATOM   3088 C CA   . ILE   B 1 90  ? 4.816  -21.217 35.318  1 40.908  ? 102 ILE   A CA   1 ? 2 
ATOM   3089 C C    . ILE   B 1 90  ? 5.474  -19.973 35.869  1 39.681  ? 102 ILE   A C    1 ? 2 
ATOM   3090 O O    . ILE   B 1 90  ? 5.468  -19.738 37.083  1 40.176  ? 102 ILE   A O    1 ? 2 
ATOM   3091 C CB   . ILE   B 1 90  ? 3.287  -21.146 35.465  1 44.317  ? 102 ILE   A CB   1 ? 2 
ATOM   3092 C CG1  . ILE   B 1 90  ? 2.619  -22.429 34.934  1 44.976  ? 102 ILE   A CG1  1 ? 2 
ATOM   3093 C CG2  . ILE   B 1 90  ? 2.722  -19.895 34.805  1 42.72   ? 102 ILE   A CG2  1 ? 2 
ATOM   3094 C CD1  . ILE   B 1 90  ? 1.14   -22.503 35.232  1 45.945  ? 102 ILE   A CD1  1 ? 2 
ATOM   3095 H H    . ILE   B 1 90  ? 5.207  -22.438 36.926  1 42.496  ? 102 ILE   A H    1 c 2 
ATOM   3096 H HA   . ILE   B 1 90  ? 5.033  -21.302 34.374  1 40.433  ? 102 ILE   A HA   1 c 2 
ATOM   3097 H HB   . ILE   B 1 90  ? 3.089  -21.089 36.421  1 44.455  ? 102 ILE   A HB   1 c 2 
ATOM   3098 H HG12 . ILE   B 1 90  ? 2.749  -22.474 33.965  1 44.384  ? 102 ILE   A HG12 1 c 2 
ATOM   3099 H HG13 . ILE   B 1 90  ? 3.06   -23.206 35.333  1 45.689  ? 102 ILE   A HG13 1 c 2 
ATOM   3100 H HG21 . ILE   B 1 90  ? 1.759  -19.864 34.932  1 43.887  ? 102 ILE   A HG21 1 c 2 
ATOM   3101 H HG22 . ILE   B 1 90  ? 2.92   -19.911 33.853  1 42.155  ? 102 ILE   A HG22 1 c 2 
ATOM   3102 H HG23 . ILE   B 1 90  ? 3.121  -19.105 35.203  1 42.158  ? 102 ILE   A HG23 1 c 2 
ATOM   3103 H HD11 . ILE   B 1 90  ? 0.998  -22.432 36.195  1 46.916  ? 102 ILE   A HD11 1 c 2 
ATOM   3104 H HD12 . ILE   B 1 90  ? 0.789  -23.357 34.916  1 47.345  ? 102 ILE   A HD12 1 c 2 
ATOM   3105 H HD13 . ILE   B 1 90  ? 0.671  -21.777 34.781  1 45.712  ? 102 ILE   A HD13 1 c 2 
ATOM   3106 N N    . ALA   B 1 91  ? 6.039  -19.191 34.958  1 38.572  ? 103 ALA   A N    1 ? 2 
ATOM   3107 C CA   . ALA   B 1 91  ? 6.677  -17.932 35.304  1 37.031  ? 103 ALA   A CA   1 ? 2 
ATOM   3108 C C    . ALA   B 1 91  ? 6.099  -16.806 34.464  1 36.722  ? 103 ALA   A C    1 ? 2 
ATOM   3109 O O    . ALA   B 1 91  ? 5.637  -17.045 33.345  1 35.743  ? 103 ALA   A O    1 ? 2 
ATOM   3110 C CB   . ALA   B 1 91  ? 8.155  -18.036 35.014  1 39.462  ? 103 ALA   A CB   1 ? 2 
ATOM   3111 H H    . ALA   B 1 91  ? 6.029  -19.447 34.08   1 37.951  ? 103 ALA   A H    1 c 2 
ATOM   3112 H HA   . ALA   B 1 91  ? 6.527  -17.737 36.268  1 38.56   ? 103 ALA   A HA   1 c 2 
ATOM   3113 H HB1  . ALA   B 1 91  ? 8.542  -18.755 35.54   1 39.298  ? 103 ALA   A HB1  1 c 2 
ATOM   3114 H HB2  . ALA   B 1 91  ? 8.291  -18.22  34.069  1 37.911  ? 103 ALA   A HB2  1 c 2 
ATOM   3115 H HB3  . ALA   B 1 91  ? 8.593  -17.199 35.243  1 38.036  ? 103 ALA   A HB3  1 c 2 
ATOM   3116 N N    . HIS   B 1 92  ? 6.209  -15.577 34.989  1 36.749  ? 104 HIS   A N    1 ? 2 
ATOM   3117 C CA   . HIS   B 1 92  ? 5.88   -14.381 34.24   1 33.724  ? 104 HIS   A CA   1 ? 2 
ATOM   3118 C C    . HIS   B 1 92  ? 7.173  -13.624 33.977  1 35.593  ? 104 HIS   A C    1 ? 2 
ATOM   3119 O O    . HIS   B 1 92  ? 7.989  -13.478 34.9    1 33.949  ? 104 HIS   A O    1 ? 2 
ATOM   3120 C CB   . HIS   B 1 92  ? 4.923  -13.483 35.027  1 35.156  ? 104 HIS   A CB   1 ? 2 
ATOM   3121 C CG   . HIS   B 1 92  ? 3.536  -13.992 35.117  1 35.387  ? 104 HIS   A CG   1 ? 2 
ATOM   3122 N ND1  . HIS   B 1 92  ? 2.547  -13.302 35.783  1 35.828  ? 104 HIS   A ND1  1 ? 2 
ATOM   3123 C CD2  . HIS   B 1 92  ? 2.965  -15.102 34.636  1 35.764  ? 104 HIS   A CD2  1 ? 2 
ATOM   3124 C CE1  . HIS   B 1 92  ? 1.415  -14.006 35.727  1 36.892  ? 104 HIS   A CE1  1 ? 2 
ATOM   3125 N NE2  . HIS   B 1 92  ? 1.63   -15.067 34.985  1 37.183  ? 104 HIS   A NE2  1 ? 2 
ATOM   3126 H H    . HIS   B 1 92  ? 6.501  -15.486 35.851  1 36.692  ? 104 HIS   A H    1 c 2 
ATOM   3127 H HA   . HIS   B 1 92  ? 5.474  -14.632 33.378  1 34.528  ? 104 HIS   A HA   1 c 2 
ATOM   3128 H HB2  . HIS   B 1 92  ? 5.278  -13.37  35.936  1 35.335  ? 104 HIS   A HB2  1 c 2 
ATOM   3129 H HB3  . HIS   B 1 92  ? 4.907  -12.597 34.605  1 34.414  ? 104 HIS   A HB3  1 c 2 
ATOM   3130 H HD1  . HIS   B 1 92  ? 2.639  -12.467 36.102  0 30      ? 104 HIS   A HD1  1 c 2 
ATOM   3131 H HD2  . HIS   B 1 92  ? 3.381  -15.76  34.116  1 35.321  ? 104 HIS   A HD2  1 c 2 
ATOM   3132 H HE1  . HIS   B 1 92  ? 0.585  -13.742 36.087  1 38.396  ? 104 HIS   A HE1  1 c 2 
ATOM   3133 H HE2  . HIS   B 1 92  ? 1.047  -15.696 34.817  0 30      ? 104 HIS   A HE2  1 c 2 
ATOM   3134 N N    . LEU   B 1 93  ? 7.326  -13.136 32.732  1 32.852  ? 105 LEU   A N    1 ? 2 
ATOM   3135 C CA   . LEU   B 1 93  ? 8.452  -12.305 32.371  1 35.801  ? 105 LEU   A CA   1 ? 2 
ATOM   3136 C C    . LEU   B 1 93  ? 8.004  -10.941 31.846  1 34.676  ? 105 LEU   A C    1 ? 2 
ATOM   3137 O O    . LEU   B 1 93  ? 7.157  -10.876 30.952  1 32.251  ? 105 LEU   A O    1 ? 2 
ATOM   3138 C CB   . LEU   B 1 93  ? 9.217  -13.06  31.294  1 38.641  ? 105 LEU   A CB   1 ? 2 
ATOM   3139 C CG   . LEU   B 1 93  ? 9.953  -14.321 31.731  1 36.872  ? 105 LEU   A CG   1 ? 2 
ATOM   3140 C CD1  . LEU   B 1 93  ? 10.533 -14.885 30.444  1 37.859  ? 105 LEU   A CD1  1 ? 2 
ATOM   3141 C CD2  . LEU   B 1 93  ? 11.012 -14     32.766  1 37.118  ? 105 LEU   A CD2  1 ? 2 
ATOM   3142 H H    . LEU   B 1 93  ? 6.702  -13.332 32.093  1 34.059  ? 105 LEU   A H    1 c 2 
ATOM   3143 H HA   . LEU   B 1 93  ? 9.028  -12.178 33.163  1 35.678  ? 105 LEU   A HA   1 c 2 
ATOM   3144 H HB2  . LEU   B 1 93  ? 8.579  -13.305 30.584  1 37.226  ? 105 LEU   A HB2  1 c 2 
ATOM   3145 H HB3  . LEU   B 1 93  ? 9.873  -12.442 30.896  1 36.89   ? 105 LEU   A HB3  1 c 2 
ATOM   3146 H HG   . LEU   B 1 93  ? 9.3    -14.964 32.11   1 37.998  ? 105 LEU   A HG   1 c 2 
ATOM   3147 H HD11 . LEU   B 1 93  ? 9.812  -15.115 29.834  1 37.482  ? 105 LEU   A HD11 1 c 2 
ATOM   3148 H HD12 . LEU   B 1 93  ? 11.052 -15.682 30.644  1 37.887  ? 105 LEU   A HD12 1 c 2 
ATOM   3149 H HD13 . LEU   B 1 93  ? 11.11  -14.222 30.028  1 37.066  ? 105 LEU   A HD13 1 c 2 
ATOM   3150 H HD21 . LEU   B 1 93  ? 10.586 -13.729 33.595  1 37.566  ? 105 LEU   A HD21 1 c 2 
ATOM   3151 H HD22 . LEU   B 1 93  ? 11.576 -13.278 32.441  1 36.795  ? 105 LEU   A HD22 1 c 2 
ATOM   3152 H HD23 . LEU   B 1 93  ? 11.558 -14.788 32.927  1 37.539  ? 105 LEU   A HD23 1 c 2 
ATOM   3153 N N    . LEU   B 1 94  ? 8.638  -9.875  32.371  1 31.594  ? 106 LEU   A N    1 ? 2 
ATOM   3154 C CA   . LEU   B 1 94  ? 8.513  -8.518  31.852  1 32.375  ? 106 LEU   A CA   1 ? 2 
ATOM   3155 C C    . LEU   B 1 94  ? 9.814  -8.127  31.149  1 32.351  ? 106 LEU   A C    1 ? 2 
ATOM   3156 O O    . LEU   B 1 94  ? 10.91  -8.139  31.732  1 31.323  ? 106 LEU   A O    1 ? 2 
ATOM   3157 C CB   . LEU   B 1 94  ? 8.185  -7.537  32.969  1 35.641  ? 106 LEU   A CB   1 ? 2 
ATOM   3158 C CG   . LEU   B 1 94  ? 7.925  -6.079  32.537  1 38.247  ? 106 LEU   A CG   1 ? 2 
ATOM   3159 C CD1  . LEU   B 1 94  ? 6.712  -5.899  31.637  1 36.824  ? 106 LEU   A CD1  1 ? 2 
ATOM   3160 C CD2  . LEU   B 1 94  ? 7.707  -5.18   33.733  1 41.338  ? 106 LEU   A CD2  1 ? 2 
ATOM   3161 H H    . LEU   B 1 94  ? 9.179  -10.007 33.096  1 32.851  ? 106 LEU   A H    1 c 2 
ATOM   3162 H HA   . LEU   B 1 94  ? 7.778  -8.506  31.189  1 32.71   ? 106 LEU   A HA   1 c 2 
ATOM   3163 H HB2  . LEU   B 1 94  ? 7.387  -7.868  33.442  1 36.147  ? 106 LEU   A HB2  1 c 2 
ATOM   3164 H HB3  . LEU   B 1 94  ? 8.933  -7.542  33.61   1 35.855  ? 106 LEU   A HB3  1 c 2 
ATOM   3165 H HG   . LEU   B 1 94  ? 8.723  -5.751  32.048  1 37.381  ? 106 LEU   A HG   1 c 2 
ATOM   3166 H HD11 . LEU   B 1 94  ? 6.842  -6.396  30.812  1 36.489  ? 106 LEU   A HD11 1 c 2 
ATOM   3167 H HD12 . LEU   B 1 94  ? 6.597  -4.956  31.431  1 37.833  ? 106 LEU   A HD12 1 c 2 
ATOM   3168 H HD13 . LEU   B 1 94  ? 5.919  -6.229  32.091  1 37.86   ? 106 LEU   A HD13 1 c 2 
ATOM   3169 H HD21 . LEU   B 1 94  ? 8.455  -5.268  34.347  1 41.051  ? 106 LEU   A HD21 1 c 2 
ATOM   3170 H HD22 . LEU   B 1 94  ? 6.886  -5.437  34.184  1 41.511  ? 106 LEU   A HD22 1 c 2 
ATOM   3171 H HD23 . LEU   B 1 94  ? 7.638  -4.257  33.437  1 41.296  ? 106 LEU   A HD23 1 c 2 
ATOM   3172 N N    . ILE   B 1 95  ? 9.677  -7.803  29.864  1 34.03   ? 107 ILE   A N    1 ? 2 
ATOM   3173 C CA   . ILE   B 1 95  ? 10.833 -7.749  28.976  1 33.536  ? 107 ILE   A CA   1 ? 2 
ATOM   3174 C C    . ILE   B 1 95  ? 10.924 -6.376  28.317  1 36.868  ? 107 ILE   A C    1 ? 2 
ATOM   3175 O O    . ILE   B 1 95  ? 10.045 -6.025  27.512  1 35.51   ? 107 ILE   A O    1 ? 2 
ATOM   3176 C CB   . ILE   B 1 95  ? 10.658 -8.829  27.928  1 33.718  ? 107 ILE   A CB   1 ? 2 
ATOM   3177 C CG1  . ILE   B 1 95  ? 10.513 -10.22  28.585  1 35.785  ? 107 ILE   A CG1  1 ? 2 
ATOM   3178 C CG2  . ILE   B 1 95  ? 11.769 -8.74   26.89   1 34.015  ? 107 ILE   A CG2  1 ? 2 
ATOM   3179 C CD1  . ILE   B 1 95  ? 10.071 -11.29  27.62   1 37.703  ? 107 ILE   A CD1  1 ? 2 
ATOM   3180 H H    . ILE   B 1 95  ? 8.85   -7.606  29.528  1 33.65   ? 107 ILE   A H    1 c 2 
ATOM   3181 H HA   . ILE   B 1 95  ? 11.647 -7.924  29.485  1 34.22   ? 107 ILE   A HA   1 c 2 
ATOM   3182 H HB   . ILE   B 1 95  ? 9.816  -8.646  27.465  1 34.146  ? 107 ILE   A HB   1 c 2 
ATOM   3183 H HG12 . ILE   B 1 95  ? 11.375 -10.478 28.973  1 35.75   ? 107 ILE   A HG12 1 c 2 
ATOM   3184 H HG13 . ILE   B 1 95  ? 9.861  -10.164 29.312  1 35.961  ? 107 ILE   A HG13 1 c 2 
ATOM   3185 H HG21 . ILE   B 1 95  ? 11.717 -9.502  26.29   1 33.851  ? 107 ILE   A HG21 1 c 2 
ATOM   3186 H HG22 . ILE   B 1 95  ? 12.632 -8.741  27.337  1 33.98   ? 107 ILE   A HG22 1 c 2 
ATOM   3187 H HG23 . ILE   B 1 95  ? 11.673 -7.921  26.375  1 34.056  ? 107 ILE   A HG23 1 c 2 
ATOM   3188 H HD11 . ILE   B 1 95  ? 9.285  -10.978 27.133  1 37.152  ? 107 ILE   A HD11 1 c 2 
ATOM   3189 H HD12 . ILE   B 1 95  ? 9.846  -12.102 28.112  1 37.247  ? 107 ILE   A HD12 1 c 2 
ATOM   3190 H HD13 . ILE   B 1 95  ? 10.788 -11.483 26.988  1 36.87   ? 107 ILE   A HD13 1 c 2 
ATOM   3191 N N    . LYS   B 1 96  ? 12.009 -5.637  28.618  1 34.861  ? 108 LYS   A N    1 ? 2 
ATOM   3192 C CA   . LYS   B 1 96  ? 12.296 -4.393  27.914  1 33.755  ? 108 LYS   A CA   1 ? 2 
ATOM   3193 C C    . LYS   B 1 96  ? 12.834 -4.684  26.51   1 33.592  ? 108 LYS   A C    1 ? 2 
ATOM   3194 O O    . LYS   B 1 96  ? 13.379 -5.757  26.249  1 33.649  ? 108 LYS   A O    1 ? 2 
ATOM   3195 C CB   . LYS   B 1 96  ? 13.338 -3.601  28.707  1 35.915  ? 108 LYS   A CB   1 ? 2 
ATOM   3196 C CG   . LYS   B 1 96  ? 12.918 -3.16   30.088  1 41.008  ? 108 LYS   A CG   1 ? 2 
ATOM   3197 C CD   . LYS   B 1 96  ? 11.953 -1.983  30.122  1 46.693  ? 108 LYS   A CD   1 ? 2 
ATOM   3198 C CE   . LYS   B 1 96  ? 11.475 -1.677  31.495  1 46.182  ? 108 LYS   A CE   1 ? 2 
ATOM   3199 N NZ   . LYS   B 1 96  ? 10.54  -2.684  31.961  1 45.694  ? 108 LYS   A NZ   1 ? 2 
ATOM   3200 H H    . LYS   B 1 96  ? 12.58  -5.917  29.274  1 35.184  ? 108 LYS   A H    1 c 2 
ATOM   3201 H HA   . LYS   B 1 96  ? 11.459 -3.867  27.843  1 34.675  ? 108 LYS   A HA   1 c 2 
ATOM   3202 H HB2  . LYS   B 1 96  ? 14.143 -4.155  28.796  1 36.382  ? 108 LYS   A HB2  1 c 2 
ATOM   3203 H HB3  . LYS   B 1 96  ? 13.588 -2.804  28.195  1 36.98   ? 108 LYS   A HB3  1 c 2 
ATOM   3204 H HG2  . LYS   B 1 96  ? 12.502 -3.923  30.541  1 40.565  ? 108 LYS   A HG2  1 c 2 
ATOM   3205 H HG3  . LYS   B 1 96  ? 13.725 -2.921  30.594  1 41.588  ? 108 LYS   A HG3  1 c 2 
ATOM   3206 H HD2  . LYS   B 1 96  ? 12.402 -1.191  29.754  1 45.771  ? 108 LYS   A HD2  1 c 2 
ATOM   3207 H HD3  . LYS   B 1 96  ? 11.18  -2.186  29.55   1 44.754  ? 108 LYS   A HD3  1 c 2 
ATOM   3208 H HE2  . LYS   B 1 96  ? 12.232 -1.635  32.106  1 47.06   ? 108 LYS   A HE2  1 c 2 
ATOM   3209 H HE3  . LYS   B 1 96  ? 11.031 -0.811  31.496  1 47.481  ? 108 LYS   A HE3  1 c 2 
ATOM   3210 H HZ1  . LYS   B 1 96  ? 10.979 -3.453  32.151  1 45.089  ? 108 LYS   A HZ1  1 c 2 
ATOM   3211 H HZ2  . LYS   B 1 96  ? 9.914  -2.847  31.326  1 45.229  ? 108 LYS   A HZ2  1 c 2 
ATOM   3212 H HZ3  . LYS   B 1 96  ? 10.125 -2.393  32.707  1 46.574  ? 108 LYS   A HZ3  1 c 2 
ATOM   3213 N N    . PRO   B 1 97  ? 12.779 -3.707  25.572  1 36.511  ? 109 PRO   A N    1 ? 2 
ATOM   3214 C CA   . PRO   B 1 97  ? 13.088 -3.965  24.164  1 34.926  ? 109 PRO   A CA   1 ? 2 
ATOM   3215 C C    . PRO   B 1 97  ? 14.497 -4.479  23.889  1 34.824  ? 109 PRO   A C    1 ? 2 
ATOM   3216 O O    . PRO   B 1 97  ? 14.696 -5.184  22.904  1 32.406  ? 109 PRO   A O    1 ? 2 
ATOM   3217 C CB   . PRO   B 1 97  ? 12.767 -2.639  23.479  1 33.821  ? 109 PRO   A CB   1 ? 2 
ATOM   3218 C CG   . PRO   B 1 97  ? 12.819 -1.632  24.605  1 35.553  ? 109 PRO   A CG   1 ? 2 
ATOM   3219 C CD   . PRO   B 1 97  ? 12.336 -2.326  25.814  1 34.279  ? 109 PRO   A CD   1 ? 2 
ATOM   3220 H HA   . PRO   B 1 97  ? 12.451 -4.632  23.831  1 34.455  ? 109 PRO   A HA   1 c 2 
ATOM   3221 H HB2  . PRO   B 1 97  ? 13.429 -2.431  22.791  1 34.932  ? 109 PRO   A HB2  1 c 2 
ATOM   3222 H HB3  . PRO   B 1 97  ? 11.879 -2.663  23.071  1 34.633  ? 109 PRO   A HB3  1 c 2 
ATOM   3223 H HG2  . PRO   B 1 97  ? 13.734 -1.314  24.739  1 35.515  ? 109 PRO   A HG2  1 c 2 
ATOM   3224 H HG3  . PRO   B 1 97  ? 12.249 -0.863  24.405  1 35.835  ? 109 PRO   A HG3  1 c 2 
ATOM   3225 H HD2  . PRO   B 1 97  ? 12.744 -1.959  26.618  1 35.544  ? 109 PRO   A HD2  1 c 2 
ATOM   3226 H HD3  . PRO   B 1 97  ? 11.364 -2.279  25.89   1 35.223  ? 109 PRO   A HD3  1 c 2 
ATOM   3227 N N    . GLU   B 1 98  ? 15.471 -4.178  24.756  1 37.626  ? 110 GLU   A N    1 ? 2 
ATOM   3228 C CA   . GLU   B 1 98  ? 16.851 -4.583  24.492  1 39.599  ? 110 GLU   A CA   1 ? 2 
ATOM   3229 C C    . GLU   B 1 98  ? 17.013 -6.109  24.559  1 38.454  ? 110 GLU   A C    1 ? 2 
ATOM   3230 O O    . GLU   B 1 98  ? 17.996 -6.641  24.042  1 38.221  ? 110 GLU   A O    1 ? 2 
ATOM   3231 C CB   . GLU   B 1 98  ? 17.843 -3.945  25.468  1 40.212  ? 110 GLU   A CB   1 ? 2 
ATOM   3232 C CG   . GLU   B 1 98  ? 17.912 -2.424  25.35   1 47.034  ? 110 GLU   A CG   1 ? 2 
ATOM   3233 C CD   . GLU   B 1 98  ? 16.765 -1.55   25.869  1 48.597  ? 110 GLU   A CD   1 ? 2 
ATOM   3234 O OE1  . GLU   B 1 98  ? 15.885 -1.997  26.654  1 42.664  ? 110 GLU   A OE1  1 ? 2 
ATOM   3235 O OE2  . GLU   B 1 98  ? 16.808 -0.362  25.47   1 47.86   ? 110 GLU   A OE2  1 ? 2 
ATOM   3236 H H    . GLU   B 1 98  ? 15.278 -3.722  25.523  1 37.532  ? 110 GLU   A H    1 c 2 
ATOM   3237 H HA   . GLU   B 1 98  ? 17.088 -4.286  23.577  1 39.523  ? 110 GLU   A HA   1 c 2 
ATOM   3238 H HB2  . GLU   B 1 98  ? 17.585 -4.185  26.382  1 41.313  ? 110 GLU   A HB2  1 c 2 
ATOM   3239 H HB3  . GLU   B 1 98  ? 18.734 -4.317  25.302  1 41.991  ? 110 GLU   A HB3  1 c 2 
ATOM   3240 H HG2  . GLU   B 1 98  ? 18.73  -2.127  25.803  1 46.837  ? 110 GLU   A HG2  1 c 2 
ATOM   3241 H HG3  . GLU   B 1 98  ? 18.037 -2.205  24.402  1 46.229  ? 110 GLU   A HG3  1 c 2 
ATOM   3242 N N    . TYR   B 1 99  ? 16.045 -6.798  25.187  1 35.371  ? 111 TYR   A N    1 ? 2 
ATOM   3243 C CA   . TYR   B 1 99  ? 16.049 -8.246  25.319  1 36.936  ? 111 TYR   A CA   1 ? 2 
ATOM   3244 C C    . TYR   B 1 99  ? 14.971 -8.896  24.456  1 35.844  ? 111 TYR   A C    1 ? 2 
ATOM   3245 O O    . TYR   B 1 99  ? 14.75  -10.103 24.576  1 33.219  ? 111 TYR   A O    1 ? 2 
ATOM   3246 C CB   . TYR   B 1 99  ? 15.895 -8.582  26.811  1 35.424  ? 111 TYR   A CB   1 ? 2 
ATOM   3247 C CG   . TYR   B 1 99  ? 17.152 -8.176  27.561  1 32.988  ? 111 TYR   A CG   1 ? 2 
ATOM   3248 C CD1  . TYR   B 1 99  ? 17.261 -6.904  28.115  1 32.067  ? 111 TYR   A CD1  1 ? 2 
ATOM   3249 C CD2  . TYR   B 1 99  ? 18.231 -9.05   27.687  1 34.74   ? 111 TYR   A CD2  1 ? 2 
ATOM   3250 C CE1  . TYR   B 1 99  ? 18.422 -6.497  28.749  1 35.271  ? 111 TYR   A CE1  1 ? 2 
ATOM   3251 C CE2  . TYR   B 1 99  ? 19.397 -8.657  28.325  1 35.454  ? 111 TYR   A CE2  1 ? 2 
ATOM   3252 C CZ   . TYR   B 1 99  ? 19.484 -7.374  28.865  1 39.097  ? 111 TYR   A CZ   1 ? 2 
ATOM   3253 O OH   . TYR   B 1 99  ? 20.616 -6.917  29.499  1 38.797  ? 111 TYR   A OH   1 ? 2 
ATOM   3254 H H    . TYR   B 1 99  ? 15.357 -6.337  25.571  1 36.115  ? 111 TYR   A H    1 c 2 
ATOM   3255 H HA   . TYR   B 1 99  ? 16.933 -8.585  25.017  1 36.664  ? 111 TYR   A HA   1 c 2 
ATOM   3256 H HB2  . TYR   B 1 99  ? 15.122 -8.096  27.175  1 34.679  ? 111 TYR   A HB2  1 c 2 
ATOM   3257 H HB3  . TYR   B 1 99  ? 15.75  -9.549  26.913  1 34.765  ? 111 TYR   A HB3  1 c 2 
ATOM   3258 H HD1  . TYR   B 1 99  ? 16.546 -6.295  28.023  1 32.654  ? 111 TYR   A HD1  1 c 2 
ATOM   3259 H HD2  . TYR   B 1 99  ? 18.179 -9.912  27.308  1 34.261  ? 111 TYR   A HD2  1 c 2 
ATOM   3260 H HE1  . TYR   B 1 99  ? 18.484 -5.631  29.114  1 36.033  ? 111 TYR   A HE1  1 c 2 
ATOM   3261 H HE2  . TYR   B 1 99  ? 20.123 -9.252  28.4    1 36.945  ? 111 TYR   A HE2  1 c 2 
ATOM   3262 H HH   . TYR   B 1 99  ? 20.483 -6.113  29.75   0 30      ? 111 TYR   A HH   1 c 2 
ATOM   3263 N N    . ALA   B 1 100 ? 14.353 -8.109  23.565  1 34.63   ? 112 ALA   A N    1 ? 2 
ATOM   3264 C CA   . ALA   B 1 100 ? 13.294 -8.594  22.705  1 31.863  ? 112 ALA   A CA   1 ? 2 
ATOM   3265 C C    . ALA   B 1 100 ? 13.552 -8.15   21.265  1 32.321  ? 112 ALA   A C    1 ? 2 
ATOM   3266 O O    . ALA   B 1 100 ? 14.39  -8.758  20.641  1 36.18   ? 112 ALA   A O    1 ? 2 
ATOM   3267 C CB   . ALA   B 1 100 ? 11.954 -8.14   23.235  1 35.107  ? 112 ALA   A CB   1 ? 2 
ATOM   3268 H H    . ALA   B 1 100 ? 14.608 -7.235  23.488  1 34.548  ? 112 ALA   A H    1 c 2 
ATOM   3269 H HA   . ALA   B 1 100 ? 13.316 -9.588  22.721  1 32.945  ? 112 ALA   A HA   1 c 2 
ATOM   3270 H HB1  . ALA   B 1 100 ? 11.739 -8.632  24.045  1 33.7    ? 112 ALA   A HB1  1 c 2 
ATOM   3271 H HB2  . ALA   B 1 100 ? 11.986 -7.19   23.437  1 34.141  ? 112 ALA   A HB2  1 c 2 
ATOM   3272 H HB3  . ALA   B 1 100 ? 11.265 -8.304  22.569  1 34.301  ? 112 ALA   A HB3  1 c 2 
ATOM   3273 N N    . TYR   B 1 101 ? 12.886 -7.099  20.741  1 32.422  ? 113 TYR   A N    1 ? 2 
ATOM   3274 C CA   . TYR   B 1 101 ? 13.001 -6.745  19.319  1 34.758  ? 113 TYR   A CA   1 ? 2 
ATOM   3275 C C    . TYR   B 1 101 ? 13.671 -5.391  19.119  1 32.354  ? 113 TYR   A C    1 ? 2 
ATOM   3276 O O    . TYR   B 1 101 ? 13.81  -4.922  18.007  1 28.716  ? 113 TYR   A O    1 ? 2 
ATOM   3277 C CB   . TYR   B 1 101 ? 11.622 -6.771  18.652  1 35.792  ? 113 TYR   A CB   1 ? 2 
ATOM   3278 C CG   . TYR   B 1 101 ? 11.059 -8.18   18.636  1 34.74   ? 113 TYR   A CG   1 ? 2 
ATOM   3279 C CD1  . TYR   B 1 101 ? 11.533 -9.142  17.732  1 36.049  ? 113 TYR   A CD1  1 ? 2 
ATOM   3280 C CD2  . TYR   B 1 101 ? 10.163 -8.586  19.604  1 34.159  ? 113 TYR   A CD2  1 ? 2 
ATOM   3281 C CE1  . TYR   B 1 101 ? 11.076 -10.446 17.77   1 37.227  ? 113 TYR   A CE1  1 ? 2 
ATOM   3282 C CE2  . TYR   B 1 101 ? 9.698  -9.898  19.651  1 36.475  ? 113 TYR   A CE2  1 ? 2 
ATOM   3283 C CZ   . TYR   B 1 101 ? 10.134 -10.821 18.72   1 35.672  ? 113 TYR   A CZ   1 ? 2 
ATOM   3284 O OH   . TYR   B 1 101 ? 9.635  -12.096 18.781  1 40.045  ? 113 TYR   A OH   1 ? 2 
ATOM   3285 H H    . TYR   B 1 101 ? 12.343 -6.596  21.276  1 32.596  ? 113 TYR   A H    1 c 2 
ATOM   3286 H HA   . TYR   B 1 101 ? 13.565 -7.432  18.875  1 34.328  ? 113 TYR   A HA   1 c 2 
ATOM   3287 H HB2  . TYR   B 1 101 ? 11.013 -6.182  19.148  1 35.328  ? 113 TYR   A HB2  1 c 2 
ATOM   3288 H HB3  . TYR   B 1 101 ? 11.704 -6.442  17.729  1 36.325  ? 113 TYR   A HB3  1 c 2 
ATOM   3289 H HD1  . TYR   B 1 101 ? 12.168 -8.893  17.079  1 36.794  ? 113 TYR   A HD1  1 c 2 
ATOM   3290 H HD2  . TYR   B 1 101 ? 9.855  -7.963  20.242  1 34.34   ? 113 TYR   A HD2  1 c 2 
ATOM   3291 H HE1  . TYR   B 1 101 ? 11.373 -11.07  17.13   1 37.589  ? 113 TYR   A HE1  1 c 2 
ATOM   3292 H HE2  . TYR   B 1 101 ? 9.056  -10.147 20.292  1 35.337  ? 113 TYR   A HE2  1 c 2 
ATOM   3293 H HH   . TYR   B 1 101 ? 10.107 -12.589 18.146  0 30      ? 113 TYR   A HH   1 c 2 
ATOM   3294 N N    . GLY   B 1 102 ? 14.089 -4.759  20.223  1 34.172  ? 114 GLY   A N    1 ? 2 
ATOM   3295 C CA   . GLY   B 1 102 ? 14.978 -3.61   20.122  1 34.609  ? 114 GLY   A CA   1 ? 2 
ATOM   3296 C C    . GLY   B 1 102 ? 14.335 -2.423  19.416  1 35.275  ? 114 GLY   A C    1 ? 2 
ATOM   3297 O O    . GLY   B 1 102 ? 13.113 -2.325  19.269  1 35.629  ? 114 GLY   A O    1 ? 2 
ATOM   3298 H H    . GLY   B 1 102 ? 13.816 -5.038  21.049  1 32.882  ? 114 GLY   A H    1 c 2 
ATOM   3299 H HA2  . GLY   B 1 102 ? 15.252 -3.339  21.03   1 34.357  ? 114 GLY   A HA2  1 c 2 
ATOM   3300 H HA3  . GLY   B 1 102 ? 15.79  -3.879  19.632  1 35.064  ? 114 GLY   A HA3  1 c 2 
ATOM   3301 N N    . SER   B 1 103 ? 15.197 -1.508  19.002  1 34.5    ? 115 SER   A N    1 ? 2 
ATOM   3302 C CA   . SER   B 1 103 ? 14.721 -0.281  18.41   1 38.982  ? 115 SER   A CA   1 ? 2 
ATOM   3303 C C    . SER   B 1 103 ? 14.276 -0.514  16.943  1 37.355  ? 115 SER   A C    1 ? 2 
ATOM   3304 O O    . SER   B 1 103 ? 13.511 0.275   16.423  1 35.71   ? 115 SER   A O    1 ? 2 
ATOM   3305 C CB   . SER   B 1 103 ? 15.774 0.8     18.602  1 41.999  ? 115 SER   A CB   1 ? 2 
ATOM   3306 O OG   . SER   B 1 103 ? 16.809 0.65    17.638  1 48.86   ? 115 SER   A OG   1 ? 2 
ATOM   3307 H H    . SER   B 1 103 ? 16.097 -1.646  19.088  1 35.831  ? 115 SER   A H    1 c 2 
ATOM   3308 H HA   . SER   B 1 103 ? 13.918 -0.001  18.917  1 37.943  ? 115 SER   A HA   1 c 2 
ATOM   3309 H HB2  . SER   B 1 103 ? 15.361 1.679   18.505  1 43.685  ? 115 SER   A HB2  1 c 2 
ATOM   3310 H HB3  . SER   B 1 103 ? 16.151 0.733   19.5    1 42.31   ? 115 SER   A HB3  1 c 2 
ATOM   3311 H HG   . SER   B 1 103 ? 17.437 1.214   17.796  0 30      ? 115 SER   A HG   1 c 2 
ATOM   3312 N N    . ALA   B 1 104 ? 14.642 -1.617  16.278  1 36.376  ? 116 ALA   A N    1 ? 2 
ATOM   3313 C CA   . ALA   B 1 104 ? 14.118 -1.852  14.929  1 40.011  ? 116 ALA   A CA   1 ? 2 
ATOM   3314 C C    . ALA   B 1 104 ? 12.687 -2.401  14.992  1 38.822  ? 116 ALA   A C    1 ? 2 
ATOM   3315 O O    . ALA   B 1 104 ? 11.926 -2.299  14.038  1 37.516  ? 116 ALA   A O    1 ? 2 
ATOM   3316 C CB   . ALA   B 1 104 ? 15.015 -2.799  14.109  1 40.452  ? 116 ALA   A CB   1 ? 2 
ATOM   3317 H H    . ALA   B 1 104 ? 15.22  -2.22   16.65   1 36.461  ? 116 ALA   A H    1 c 2 
ATOM   3318 H HA   . ALA   B 1 104 ? 14.083 -0.974  14.459  1 40.499  ? 116 ALA   A HA   1 c 2 
ATOM   3319 H HB1  . ALA   B 1 104 ? 15.891 -2.397  13.987  1 41.109  ? 116 ALA   A HB1  1 c 2 
ATOM   3320 H HB2  . ALA   B 1 104 ? 15.112 -3.646  14.577  1 39.521  ? 116 ALA   A HB2  1 c 2 
ATOM   3321 H HB3  . ALA   B 1 104 ? 14.611 -2.958  13.239  1 41.492  ? 116 ALA   A HB3  1 c 2 
ATOM   3322 N N    . GLY   B 1 105 ? 12.317 -3.029  16.103  1 36.845  ? 117 GLY   A N    1 ? 2 
ATOM   3323 C CA   . GLY   B 1 105 ? 11.029 -3.706  16.167  1 36.5    ? 117 GLY   A CA   1 ? 2 
ATOM   3324 C C    . GLY   B 1 105 ? 10.98  -4.898  15.214  1 34.404  ? 117 GLY   A C    1 ? 2 
ATOM   3325 O O    . GLY   B 1 105 ? 12.007 -5.363  14.767  1 31.671  ? 117 GLY   A O    1 ? 2 
ATOM   3326 H H    . GLY   B 1 105 ? 12.867 -3.046  16.833  1 36.096  ? 117 GLY   A H    1 c 2 
ATOM   3327 H HA2  . GLY   B 1 105 ? 10.873 -4.016  17.087  1 34.844  ? 117 GLY   A HA2  1 c 2 
ATOM   3328 H HA3  . GLY   B 1 105 ? 10.314 -3.067  15.936  1 36.698  ? 117 GLY   A HA3  1 c 2 
ATOM   3329 N N    . SER   B 1 106 ? 9.78   -5.388  14.944  1 34.792  ? 118 SER   A N    1 ? 2 
ATOM   3330 C CA   . SER   B 1 106 ? 9.578  -6.5    14.027  1 41.721  ? 118 SER   A CA   1 ? 2 
ATOM   3331 C C    . SER   B 1 106 ? 8.201  -6.312  13.409  1 41.882  ? 118 SER   A C    1 ? 2 
ATOM   3332 O O    . SER   B 1 106 ? 7.243  -6.946  13.803  1 42.21   ? 118 SER   A O    1 ? 2 
ATOM   3333 C CB   . SER   B 1 106 ? 9.712  -7.874  14.694  1 40.223  ? 118 SER   A CB   1 ? 2 
ATOM   3334 O OG   . SER   B 1 106 ? 9.82   -8.898  13.719  1 42.905  ? 118 SER   A OG   1 ? 2 
ATOM   3335 H H    . SER   B 1 106 ? 9.05   -5.017  15.35   1 36.063  ? 118 SER   A H    1 c 2 
ATOM   3336 H HA   . SER   B 1 106 ? 10.253 -6.435  13.303  1 40.868  ? 118 SER   A HA   1 c 2 
ATOM   3337 H HB2  . SER   B 1 106 ? 10.507 -7.881  15.261  1 39.585  ? 118 SER   A HB2  1 c 2 
ATOM   3338 H HB3  . SER   B 1 106 ? 8.934  -8.041  15.258  1 40.176  ? 118 SER   A HB3  1 c 2 
ATOM   3339 H HG   . SER   B 1 106 ? 9.879  -9.668  14.144  0 30      ? 118 SER   A HG   1 c 2 
ATOM   3340 N N    . LEU   B 1 107 ? 8.089  -5.338  12.524  1 44.318  ? 119 LEU   A N    1 ? 2 
ATOM   3341 C CA   . LEU   B 1 107 ? 6.797  -5.008  11.952  1 49.318  ? 119 LEU   A CA   1 ? 2 
ATOM   3342 C C    . LEU   B 1 107 ? 6.385  -6.125  10.998  1 54.797  ? 119 LEU   A C    1 ? 2 
ATOM   3343 O O    . LEU   B 1 107 ? 7.244  -6.7    10.327  1 54.928  ? 119 LEU   A O    1 ? 2 
ATOM   3344 C CB   . LEU   B 1 107 ? 6.822  -3.67   11.214  1 51.37   ? 119 LEU   A CB   1 ? 2 
ATOM   3345 C CG   . LEU   B 1 107 ? 7.094  -2.407  12.037  1 49.736  ? 119 LEU   A CG   1 ? 2 
ATOM   3346 C CD1  . LEU   B 1 107 ? 6.973  -1.276  11.052  1 51.779  ? 119 LEU   A CD1  1 ? 2 
ATOM   3347 C CD2  . LEU   B 1 107 ? 6.176  -2.191  13.234  1 48.142  ? 119 LEU   A CD2  1 ? 2 
ATOM   3348 H H    . LEU   B 1 107 ? 8.827  -4.864  12.266  1 44.906  ? 119 LEU   A H    1 c 2 
ATOM   3349 H HA   . LEU   B 1 107 ? 6.142  -4.957  12.691  1 48.727  ? 119 LEU   A HA   1 c 2 
ATOM   3350 H HB2  . LEU   B 1 107 ? 7.508  -3.729  10.509  1 51.811  ? 119 LEU   A HB2  1 c 2 
ATOM   3351 H HB3  . LEU   B 1 107 ? 5.959  -3.558  10.754  1 52.772  ? 119 LEU   A HB3  1 c 2 
ATOM   3352 H HG   . LEU   B 1 107 ? 8.031  -2.441  12.362  1 48.453  ? 119 LEU   A HG   1 c 2 
ATOM   3353 H HD11 . LEU   B 1 107 ? 7.621  -1.396  10.337  1 52.555  ? 119 LEU   A HD11 1 c 2 
ATOM   3354 H HD12 . LEU   B 1 107 ? 7.145  -0.434  11.504  1 51.601  ? 119 LEU   A HD12 1 c 2 
ATOM   3355 H HD13 . LEU   B 1 107 ? 6.076  -1.264  10.677  1 53.345  ? 119 LEU   A HD13 1 c 2 
ATOM   3356 H HD21 . LEU   B 1 107 ? 6.256  -2.941  13.846  1 46.909  ? 119 LEU   A HD21 1 c 2 
ATOM   3357 H HD22 . LEU   B 1 107 ? 5.256  -2.12   12.93   1 49.714  ? 119 LEU   A HD22 1 c 2 
ATOM   3358 H HD23 . LEU   B 1 107 ? 6.428  -1.372  13.693  1 48.076  ? 119 LEU   A HD23 1 c 2 
ATOM   3359 N N    . PRO   B 1 108 ? 5.061  -6.38   10.841  1 56.566  ? 120 PRO   A N    1 ? 2 
ATOM   3360 C CA   . PRO   B 1 108 ? 4.038  -5.539  11.456  1 53.519  ? 120 PRO   A CA   1 ? 2 
ATOM   3361 C C    . PRO   B 1 108 ? 3.674  -5.901  12.894  1 50.917  ? 120 PRO   A C    1 ? 2 
ATOM   3362 O O    . PRO   B 1 108 ? 3.018  -5.097  13.543  1 52.933  ? 120 PRO   A O    1 ? 2 
ATOM   3363 C CB   . PRO   B 1 108 ? 2.854  -5.677  10.524  1 58.075  ? 120 PRO   A CB   1 ? 2 
ATOM   3364 C CG   . PRO   B 1 108 ? 3.099  -6.964  9.747   1 60.032  ? 120 PRO   A CG   1 ? 2 
ATOM   3365 C CD   . PRO   B 1 108 ? 4.502  -7.425  9.976   1 58.914  ? 120 PRO   A CD   1 ? 2 
ATOM   3366 H HA   . PRO   B 1 108 ? 4.329  -4.609  11.432  1 54.268  ? 120 PRO   A HA   1 c 2 
ATOM   3367 H HB2  . PRO   B 1 108 ? 2.019  -5.732  11.028  1 58.128  ? 120 PRO   A HB2  1 c 2 
ATOM   3368 H HB3  . PRO   B 1 108 ? 2.8    -4.913  9.918   1 59.397  ? 120 PRO   A HB3  1 c 2 
ATOM   3369 H HG2  . PRO   B 1 108 ? 2.473  -7.656  10.04   1 60.235  ? 120 PRO   A HG2  1 c 2 
ATOM   3370 H HG3  . PRO   B 1 108 ? 2.954  -6.811  8.792   1 62.192  ? 120 PRO   A HG3  1 c 2 
ATOM   3371 H HD2  . PRO   B 1 108 ? 4.523  -8.293  10.423  1 57.739  ? 120 PRO   A HD2  1 c 2 
ATOM   3372 H HD3  . PRO   B 1 108 ? 4.998  -7.482  9.136   1 59.773  ? 120 PRO   A HD3  1 c 2 
ATOM   3373 N N    . LYS   B 1 109 ? 4.174  -7.03   13.417  1 47.741  ? 121 LYS   A N    1 ? 2 
ATOM   3374 C CA   . LYS   B 1 109 ? 3.7    -7.544  14.696  1 47.221  ? 121 LYS   A CA   1 ? 2 
ATOM   3375 C C    . LYS   B 1 109 ? 4.146  -6.679  15.874  1 44.384  ? 121 LYS   A C    1 ? 2 
ATOM   3376 O O    . LYS   B 1 109 ? 3.4    -6.493  16.815  1 45.737  ? 121 LYS   A O    1 ? 2 
ATOM   3377 C CB   . LYS   B 1 109 ? 4.164  -8.987  14.895  1 50.031  ? 121 LYS   A CB   1 ? 2 
ATOM   3378 C CG   . LYS   B 1 109 ? 3.285  -10.016 14.194  1 55.074  ? 121 LYS   A CG   1 ? 2 
ATOM   3379 C CD   . LYS   B 1 109 ? 3.934  -11.398 14.135  1 57.369  ? 121 LYS   A CD   1 ? 2 
ATOM   3380 C CE   . LYS   B 1 109 ? 3.337  -12.294 13.076  1 55.079  ? 121 LYS   A CE   1 ? 2 
ATOM   3381 N NZ   . LYS   B 1 109 ? 1.988  -12.635 13.515  1 56.071  ? 121 LYS   A NZ   1 ? 2 
ATOM   3382 H H    . LYS   B 1 109 ? 4.824  -7.49   12.969  1 48.4    ? 121 LYS   A H    1 c 2 
ATOM   3383 H HA   . LYS   B 1 109 ? 2.709  -7.544  14.675  1 48.769  ? 121 LYS   A HA   1 c 2 
ATOM   3384 H HB2  . LYS   B 1 109 ? 5.082  -9.078  14.56   1 49.34   ? 121 LYS   A HB2  1 c 2 
ATOM   3385 H HB3  . LYS   B 1 109 ? 4.175  -9.19   15.855  1 48.442  ? 121 LYS   A HB3  1 c 2 
ATOM   3386 H HG2  . LYS   B 1 109 ? 2.429  -10.079 14.672  1 55.273  ? 121 LYS   A HG2  1 c 2 
ATOM   3387 H HG3  . LYS   B 1 109 ? 3.102  -9.705  13.28   1 56.565  ? 121 LYS   A HG3  1 c 2 
ATOM   3388 H HD2  . LYS   B 1 109 ? 4.894  -11.292 13.957  1 54.762  ? 121 LYS   A HD2  1 c 2 
ATOM   3389 H HD3  . LYS   B 1 109 ? 3.839  -11.83  15.012  1 54.437  ? 121 LYS   A HD3  1 c 2 
ATOM   3390 H HE2  . LYS   B 1 109 ? 3.296  -11.832 12.22   1 57.488  ? 121 LYS   A HE2  1 c 2 
ATOM   3391 H HE3  . LYS   B 1 109 ? 3.865  -13.106 12.976  1 56.053  ? 121 LYS   A HE3  1 c 2 
ATOM   3392 H HZ1  . LYS   B 1 109 ? 1.462  -11.898 13.515  1 56.6    ? 121 LYS   A HZ1  1 c 2 
ATOM   3393 H HZ2  . LYS   B 1 109 ? 2.009  -12.988 14.35   1 54.933  ? 121 LYS   A HZ2  1 c 2 
ATOM   3394 H HZ3  . LYS   B 1 109 ? 1.634  -13.247 12.948  1 57.856  ? 121 LYS   A HZ3  1 c 2 
ATOM   3395 N N    . ILE   B 1 110 ? 5.394  -6.208  15.86   1 41.795  ? 122 ILE   A N    1 ? 2 
ATOM   3396 C CA   . ILE   B 1 110 ? 6.03   -5.649  17.032  1 40.842  ? 122 ILE   A CA   1 ? 2 
ATOM   3397 C C    . ILE   B 1 110 ? 6.559  -4.255  16.672  1 37.466  ? 122 ILE   A C    1 ? 2 
ATOM   3398 O O    . ILE   B 1 110 ? 7.464  -4.148  15.835  1 35.458  ? 122 ILE   A O    1 ? 2 
ATOM   3399 C CB   . ILE   B 1 110 ? 7.193  -6.564  17.515  1 40.222  ? 122 ILE   A CB   1 ? 2 
ATOM   3400 C CG1  . ILE   B 1 110 ? 6.883  -8.07   17.555  1 42.111  ? 122 ILE   A CG1  1 ? 2 
ATOM   3401 C CG2  . ILE   B 1 110 ? 7.701  -6.091  18.861  1 42.202  ? 122 ILE   A CG2  1 ? 2 
ATOM   3402 C CD1  . ILE   B 1 110 ? 5.943  -8.518  18.661  1 41.885  ? 122 ILE   A CD1  1 ? 2 
ATOM   3403 H H    . ILE   B 1 110 ? 5.87   -6.239  15.081  1 42.882  ? 122 ILE   A H    1 c 2 
ATOM   3404 H HA   . ILE   B 1 110 ? 5.372  -5.57   17.748  1 39.928  ? 122 ILE   A HA   1 c 2 
ATOM   3405 H HB   . ILE   B 1 110 ? 7.926  -6.449  16.878  1 41.13   ? 122 ILE   A HB   1 c 2 
ATOM   3406 H HG12 . ILE   B 1 110 ? 6.496  -8.331  16.695  1 42.923  ? 122 ILE   A HG12 1 c 2 
ATOM   3407 H HG13 . ILE   B 1 110 ? 7.728  -8.555  17.655  1 41.011  ? 122 ILE   A HG13 1 c 2 
ATOM   3408 H HG21 . ILE   B 1 110 ? 8.358  -6.718  19.199  1 40.214  ? 122 ILE   A HG21 1 c 2 
ATOM   3409 H HG22 . ILE   B 1 110 ? 6.96   -6.03   19.487  1 41.071  ? 122 ILE   A HG22 1 c 2 
ATOM   3410 H HG23 . ILE   B 1 110 ? 8.113  -5.216  18.765  1 41.227  ? 122 ILE   A HG23 1 c 2 
ATOM   3411 H HD11 . ILE   B 1 110 ? 6.38   -8.426  19.529  1 40.683  ? 122 ILE   A HD11 1 c 2 
ATOM   3412 H HD12 . ILE   B 1 110 ? 5.701  -9.453  18.518  1 42.076  ? 122 ILE   A HD12 1 c 2 
ATOM   3413 H HD13 . ILE   B 1 110 ? 5.135  -7.97   18.646  1 42.568  ? 122 ILE   A HD13 1 c 2 
ATOM   3414 N N    . PRO   B 1 111 ? 6.124  -3.153  17.336  1 39.037  ? 123 PRO   A N    1 ? 2 
ATOM   3415 C CA   . PRO   B 1 111 ? 6.683  -1.829  17.036  1 38.38   ? 123 PRO   A CA   1 ? 2 
ATOM   3416 C C    . PRO   B 1 111 ? 8.076  -1.628  17.629  1 37.065  ? 123 PRO   A C    1 ? 2 
ATOM   3417 O O    . PRO   B 1 111 ? 8.533  -2.432  18.454  1 38.216  ? 123 PRO   A O    1 ? 2 
ATOM   3418 C CB   . PRO   B 1 111 ? 5.623  -0.853  17.557  1 39      ? 123 PRO   A CB   1 ? 2 
ATOM   3419 C CG   . PRO   B 1 111 ? 4.948  -1.648  18.686  1 40.148  ? 123 PRO   A CG   1 ? 2 
ATOM   3420 C CD   . PRO   B 1 111 ? 5.1    -3.115  18.399  1 37.048  ? 123 PRO   A CD   1 ? 2 
ATOM   3421 H HA   . PRO   B 1 111 ? 6.741  -1.725  16.063  1 39.627  ? 123 PRO   A HA   1 c 2 
ATOM   3422 H HB2  . PRO   B 1 111 ? 6.036  -0.036  17.9    1 39.641  ? 123 PRO   A HB2  1 c 2 
ATOM   3423 H HB3  . PRO   B 1 111 ? 4.983  -0.623  16.856  1 41.112  ? 123 PRO   A HB3  1 c 2 
ATOM   3424 H HG2  . PRO   B 1 111 ? 5.363  -1.433  19.544  1 38.23   ? 123 PRO   A HG2  1 c 2 
ATOM   3425 H HG3  . PRO   B 1 111 ? 3.999  -1.417  18.739  1 40.267  ? 123 PRO   A HG3  1 c 2 
ATOM   3426 H HD2  . PRO   B 1 111 ? 5.405  -3.601  19.189  1 36.687  ? 123 PRO   A HD2  1 c 2 
ATOM   3427 H HD3  . PRO   B 1 111 ? 4.261  -3.504  18.085  1 38.873  ? 123 PRO   A HD3  1 c 2 
ATOM   3428 N N    . SER   B 1 112 ? 8.723  -0.514  17.243  1 36.123  ? 124 SER   A N    1 ? 2 
ATOM   3429 C CA   . SER   B 1 112 ? 9.992  -0.096  17.821  1 36.077  ? 124 SER   A CA   1 ? 2 
ATOM   3430 C C    . SER   B 1 112 ? 9.883  0.113   19.343  1 35.003  ? 124 SER   A C    1 ? 2 
ATOM   3431 O O    . SER   B 1 112 ? 8.897  0.624   19.846  1 34.123  ? 124 SER   A O    1 ? 2 
ATOM   3432 C CB   . SER   B 1 112 ? 10.444 1.16    17.146  1 39.362  ? 124 SER   A CB   1 ? 2 
ATOM   3433 O OG   . SER   B 1 112 ? 11.63  1.693   17.72   1 40.635  ? 124 SER   A OG   1 ? 2 
ATOM   3434 H H    . SER   B 1 112 ? 8.353  0.001   16.585  1 38.057  ? 124 SER   A H    1 c 2 
ATOM   3435 H HA   . SER   B 1 112 ? 10.661 -0.806  17.648  1 35.554  ? 124 SER   A HA   1 c 2 
ATOM   3436 H HB2  . SER   B 1 112 ? 10.602 0.975   16.201  1 40.006  ? 124 SER   A HB2  1 c 2 
ATOM   3437 H HB3  . SER   B 1 112 ? 9.734  1.827   17.205  1 40.243  ? 124 SER   A HB3  1 c 2 
ATOM   3438 H HG   . SER   B 1 112 ? 11.826 2.431   17.346  0 30      ? 124 SER   A HG   1 c 2 
ATOM   3439 N N    . ASN   B 1 113 ? 10.909 -0.309  20.072  1 36.353  ? 125 ASN   A N    1 ? 2 
ATOM   3440 C CA   . ASN   B 1 113 ? 11.035 -0.104  21.516  1 37.978  ? 125 ASN   A CA   1 ? 2 
ATOM   3441 C C    . ASN   B 1 113 ? 9.83   -0.622  22.298  1 33.727  ? 125 ASN   A C    1 ? 2 
ATOM   3442 O O    . ASN   B 1 113 ? 9.398  0.037   23.226  1 37.764  ? 125 ASN   A O    1 ? 2 
ATOM   3443 C CB   . ASN   B 1 113 ? 11.286 1.349   21.919  1 39.753  ? 125 ASN   A CB   1 ? 2 
ATOM   3444 C CG   . ASN   B 1 113 ? 12.562 1.894   21.325  1 42.313  ? 125 ASN   A CG   1 ? 2 
ATOM   3445 O OD1  . ASN   B 1 113 ? 13.554 1.17    21.22   1 42.781  ? 125 ASN   A OD1  1 ? 2 
ATOM   3446 N ND2  . ASN   B 1 113 ? 12.56  3.158   20.923  1 45.493  ? 125 ASN   A ND2  1 ? 2 
ATOM   3447 H H    . ASN   B 1 113 ? 11.583 -0.756  19.647  1 35.899  ? 125 ASN   A H    1 c 2 
ATOM   3448 H HA   . ASN   B 1 113 ? 11.817 -0.619  21.814  1 36.181  ? 125 ASN   A HA   1 c 2 
ATOM   3449 H HB2  . ASN   B 1 113 ? 10.533 1.899   21.622  1 40.996  ? 125 ASN   A HB2  1 c 2 
ATOM   3450 H HB3  . ASN   B 1 113 ? 11.339 1.41    22.894  1 39.793  ? 125 ASN   A HB3  1 c 2 
ATOM   3451 H HD21 . ASN   B 1 113 ? 13.258 3.48    20.48   1 45.636  ? 125 ASN   A HD21 1 c 2 
ATOM   3452 H HD22 . ASN   B 1 113 ? 11.865 3.681   21.096  1 45.67   ? 125 ASN   A HD22 1 c 2 
ATOM   3453 N N    . ALA   B 1 114 ? 9.325  -1.805  21.956  1 33.889  ? 126 ALA   A N    1 ? 2 
ATOM   3454 C CA   . ALA   B 1 114 ? 8.172  -2.38   22.636  1 32.017  ? 126 ALA   A CA   1 ? 2 
ATOM   3455 C C    . ALA   B 1 114 ? 8.604  -3.175  23.864  1 30.051  ? 126 ALA   A C    1 ? 2 
ATOM   3456 O O    . ALA   B 1 114 ? 9.576  -3.92   23.818  1 32.934  ? 126 ALA   A O    1 ? 2 
ATOM   3457 C CB   . ALA   B 1 114 ? 7.42   -3.26   21.687  1 31.364  ? 126 ALA   A CB   1 ? 2 
ATOM   3458 H H    . ALA   B 1 114 ? 9.714  -2.277  21.276  1 33.121  ? 126 ALA   A H    1 c 2 
ATOM   3459 H HA   . ALA   B 1 114 ? 7.578  -1.637  22.932  1 32.895  ? 126 ALA   A HA   1 c 2 
ATOM   3460 H HB1  . ALA   B 1 114 ? 7.101  -2.733  20.935  1 32.612  ? 126 ALA   A HB1  1 c 2 
ATOM   3461 H HB2  . ALA   B 1 114 ? 8.004  -3.965  21.361  1 31.018  ? 126 ALA   A HB2  1 c 2 
ATOM   3462 H HB3  . ALA   B 1 114 ? 6.66   -3.659  22.144  1 31.65   ? 126 ALA   A HB3  1 c 2 
ATOM   3463 N N    . THR   B 1 115 ? 7.81   -3.07   24.926  1 32.635  ? 127 THR   A N    1 ? 2 
ATOM   3464 C CA   . THR   B 1 115 ? 7.897  -3.911  26.108  1 33.126  ? 127 THR   A CA   1 ? 2 
ATOM   3465 C C    . THR   B 1 115 ? 6.924  -5.085  25.947  1 34.432  ? 127 THR   A C    1 ? 2 
ATOM   3466 O O    . THR   B 1 115 ? 5.76   -4.859  25.578  1 37.359  ? 127 THR   A O    1 ? 2 
ATOM   3467 C CB   . THR   B 1 115 ? 7.574  -3.065  27.334  1 31.882  ? 127 THR   A CB   1 ? 2 
ATOM   3468 O OG1  . THR   B 1 115 ? 8.655  -2.15   27.372  1 31.306  ? 127 THR   A OG1  1 ? 2 
ATOM   3469 C CG2  . THR   B 1 115 ? 7.764  -3.822  28.644  1 32.403  ? 127 THR   A CG2  1 ? 2 
ATOM   3470 H H    . THR   B 1 115 ? 7.162  -2.425  24.912  1 33.185  ? 127 THR   A H    1 c 2 
ATOM   3471 H HA   . THR   B 1 115 ? 8.812  -4.254  26.188  1 32.12   ? 127 THR   A HA   1 c 2 
ATOM   3472 H HB   . THR   B 1 115 ? 6.709  -2.595  27.269  1 33.128  ? 127 THR   A HB   1 c 2 
ATOM   3473 H HG1  . THR   B 1 115 ? 9.367  -2.613  27.508  0 30      ? 127 THR   A HG1  1 c 2 
ATOM   3474 H HG21 . THR   B 1 115 ? 7.577  -3.229  29.391  1 32.92   ? 127 THR   A HG21 1 c 2 
ATOM   3475 H HG22 . THR   B 1 115 ? 8.68   -4.14   28.707  1 31.535  ? 127 THR   A HG22 1 c 2 
ATOM   3476 H HG23 . THR   B 1 115 ? 7.156  -4.58   28.675  1 31.96   ? 127 THR   A HG23 1 c 2 
ATOM   3477 N N    . LEU   B 1 116 ? 7.424  -6.316  26.185  1 34.192  ? 128 LEU   A N    1 ? 2 
ATOM   3478 C CA   . LEU   B 1 116 ? 6.637  -7.549  26.081  1 33.68   ? 128 LEU   A CA   1 ? 2 
ATOM   3479 C C    . LEU   B 1 116 ? 6.411  -8.186  27.455  1 32.616  ? 128 LEU   A C    1 ? 2 
ATOM   3480 O O    . LEU   B 1 116 ? 7.304  -8.167  28.311  1 28.743  ? 128 LEU   A O    1 ? 2 
ATOM   3481 C CB   . LEU   B 1 116 ? 7.291  -8.627  25.232  1 32.087  ? 128 LEU   A CB   1 ? 2 
ATOM   3482 C CG   . LEU   B 1 116 ? 7.874  -8.269  23.854  1 38.128  ? 128 LEU   A CG   1 ? 2 
ATOM   3483 C CD1  . LEU   B 1 116 ? 7.681  -9.427  22.893  1 37.559  ? 128 LEU   A CD1  1 ? 2 
ATOM   3484 C CD2  . LEU   B 1 116 ? 7.434  -7.002  23.239  1 34.117  ? 128 LEU   A CD2  1 ? 2 
ATOM   3485 H H    . LEU   B 1 116 ? 8.303  -6.388  26.425  1 33.396  ? 128 LEU   A H    1 c 2 
ATOM   3486 H HA   . LEU   B 1 116 ? 5.756  -7.322  25.69   1 34.174  ? 128 LEU   A HA   1 c 2 
ATOM   3487 H HB2  . LEU   B 1 116 ? 8.014  -9.03   25.767  1 33.053  ? 128 LEU   A HB2  1 c 2 
ATOM   3488 H HB3  . LEU   B 1 116 ? 6.628  -9.344  25.104  1 33.953  ? 128 LEU   A HB3  1 c 2 
ATOM   3489 H HG   . LEU   B 1 116 ? 8.854  -8.18   23.977  1 35.362  ? 128 LEU   A HG   1 c 2 
ATOM   3490 H HD11 . LEU   B 1 116 ? 8.161  -10.205 23.221  1 37.372  ? 128 LEU   A HD11 1 c 2 
ATOM   3491 H HD12 . LEU   B 1 116 ? 8.024  -9.183  22.017  1 38.036  ? 128 LEU   A HD12 1 c 2 
ATOM   3492 H HD13 . LEU   B 1 116 ? 6.735  -9.637  22.82   1 38.374  ? 128 LEU   A HD13 1 c 2 
ATOM   3493 H HD21 . LEU   B 1 116 ? 7.854  -6.255  23.695  1 35.332  ? 128 LEU   A HD21 1 c 2 
ATOM   3494 H HD22 . LEU   B 1 116 ? 6.467  -6.923  23.311  1 36.103  ? 128 LEU   A HD22 1 c 2 
ATOM   3495 H HD23 . LEU   B 1 116 ? 7.689  -6.988  22.301  1 35.801  ? 128 LEU   A HD23 1 c 2 
ATOM   3496 N N    . PHE   B 1 117 ? 5.244  -8.852  27.575  1 36.589  ? 129 PHE   A N    1 ? 2 
ATOM   3497 C CA   . PHE   B 1 117 ? 4.876  -9.673  28.72   1 36.067  ? 129 PHE   A CA   1 ? 2 
ATOM   3498 C C    . PHE   B 1 117 ? 4.596  -11.104 28.256  1 32.558  ? 129 PHE   A C    1 ? 2 
ATOM   3499 O O    . PHE   B 1 117 ? 3.909  -11.322 27.265  1 31.514  ? 129 PHE   A O    1 ? 2 
ATOM   3500 C CB   . PHE   B 1 117 ? 3.64   -9.135  29.438  1 36.489  ? 129 PHE   A CB   1 ? 2 
ATOM   3501 C CG   . PHE   B 1 117 ? 3.259  -9.909  30.695  1 38.19   ? 129 PHE   A CG   1 ? 2 
ATOM   3502 C CD1  . PHE   B 1 117 ? 3.766  -9.548  31.942  1 40.439  ? 129 PHE   A CD1  1 ? 2 
ATOM   3503 C CD2  . PHE   B 1 117 ? 2.397  -10.995 30.633  1 41.254  ? 129 PHE   A CD2  1 ? 2 
ATOM   3504 C CE1  . PHE   B 1 117 ? 3.446  -10.275 33.092  1 38.833  ? 129 PHE   A CE1  1 ? 2 
ATOM   3505 C CE2  . PHE   B 1 117 ? 2.072  -11.706 31.783  1 41.762  ? 129 PHE   A CE2  1 ? 2 
ATOM   3506 C CZ   . PHE   B 1 117 ? 2.622  -11.362 32.999  1 38.858  ? 129 PHE   A CZ   1 ? 2 
ATOM   3507 H H    . PHE   B 1 117 ? 4.641  -8.784  26.891  1 36.097  ? 129 PHE   A H    1 c 2 
ATOM   3508 H HA   . PHE   B 1 117 ? 5.634  -9.684  29.359  1 34.796  ? 129 PHE   A HA   1 c 2 
ATOM   3509 H HB2  . PHE   B 1 117 ? 3.805  -8.197  29.681  1 37.094  ? 129 PHE   A HB2  1 c 2 
ATOM   3510 H HB3  . PHE   B 1 117 ? 2.883  -9.155  28.812  1 37.619  ? 129 PHE   A HB3  1 c 2 
ATOM   3511 H HD1  . PHE   B 1 117 ? 4.364  -8.819  32.004  1 39.025  ? 129 PHE   A HD1  1 c 2 
ATOM   3512 H HD2  . PHE   B 1 117 ? 2.042  -11.261 29.8    1 40.777  ? 129 PHE   A HD2  1 c 2 
ATOM   3513 H HE1  . PHE   B 1 117 ? 3.807  -10.023 33.927  1 39.512  ? 129 PHE   A HE1  1 c 2 
ATOM   3514 H HE2  . PHE   B 1 117 ? 1.497  -12.45  31.723  1 41.751  ? 129 PHE   A HE2  1 c 2 
ATOM   3515 H HZ   . PHE   B 1 117 ? 2.373  -11.831 33.776  1 40.346  ? 129 PHE   A HZ   1 c 2 
ATOM   3516 N N    . PHE   B 1 118 ? 5.122  -12.072 29.004  1 32.233  ? 130 PHE   A N    1 ? 2 
ATOM   3517 C CA   . PHE   B 1 118 ? 4.848  -13.486 28.78   1 33.015  ? 130 PHE   A CA   1 ? 2 
ATOM   3518 C C    . PHE   B 1 118 ? 4.512  -14.182 30.096  1 36.674  ? 130 PHE   A C    1 ? 2 
ATOM   3519 O O    . PHE   B 1 118 ? 5.139  -13.914 31.123  1 34.458  ? 130 PHE   A O    1 ? 2 
ATOM   3520 C CB   . PHE   B 1 118 ? 5.993  -14.247 28.11   1 31.026  ? 130 PHE   A CB   1 ? 2 
ATOM   3521 C CG   . PHE   B 1 118 ? 6.27   -13.843 26.661  1 31.06   ? 130 PHE   A CG   1 ? 2 
ATOM   3522 C CD1  . PHE   B 1 118 ? 7.105  -12.768 26.376  1 30.649  ? 130 PHE   A CD1  1 ? 2 
ATOM   3523 C CD2  . PHE   B 1 118 ? 5.68   -14.525 25.599  1 32.396  ? 130 PHE   A CD2  1 ? 2 
ATOM   3524 C CE1  . PHE   B 1 118 ? 7.377  -12.404 25.069  1 32.352  ? 130 PHE   A CE1  1 ? 2 
ATOM   3525 C CE2  . PHE   B 1 118 ? 5.938  -14.139 24.288  1 34.835  ? 130 PHE   A CE2  1 ? 2 
ATOM   3526 C CZ   . PHE   B 1 118 ? 6.813  -13.104 24.031  1 32.567  ? 130 PHE   A CZ   1 ? 2 
ATOM   3527 H H    . PHE   B 1 118 ? 5.682  -11.844 29.69   1 32.071  ? 130 PHE   A H    1 c 2 
ATOM   3528 H HA   . PHE   B 1 118 ? 4.055  -13.551 28.188  1 33.925  ? 130 PHE   A HA   1 c 2 
ATOM   3529 H HB2  . PHE   B 1 118 ? 6.81   -14.106 28.638  1 30.875  ? 130 PHE   A HB2  1 c 2 
ATOM   3530 H HB3  . PHE   B 1 118 ? 5.785  -15.207 28.135  1 31.948  ? 130 PHE   A HB3  1 c 2 
ATOM   3531 H HD1  . PHE   B 1 118 ? 7.518  -12.304 27.085  1 30.656  ? 130 PHE   A HD1  1 c 2 
ATOM   3532 H HD2  . PHE   B 1 118 ? 5.103  -15.252 25.771  1 33.547  ? 130 PHE   A HD2  1 c 2 
ATOM   3533 H HE1  . PHE   B 1 118 ? 7.959  -11.683 24.893  1 31.45   ? 130 PHE   A HE1  1 c 2 
ATOM   3534 H HE2  . PHE   B 1 118 ? 5.551  -14.619 23.573  1 34.76   ? 130 PHE   A HE2  1 c 2 
ATOM   3535 H HZ   . PHE   B 1 118 ? 6.98   -12.839 23.141  1 33.225  ? 130 PHE   A HZ   1 c 2 
ATOM   3536 N N    . GLU   B 1 119 ? 3.469  -15.032 30.031  1 40.087  ? 131 GLU   A N    1 ? 2 
ATOM   3537 C CA   . GLU   B 1 119 ? 3.305  -16.177 30.902  1 40.476  ? 131 GLU   A CA   1 ? 2 
ATOM   3538 C C    . GLU   B 1 119 ? 3.793  -17.425 30.164  1 43.843  ? 131 GLU   A C    1 ? 2 
ATOM   3539 O O    . GLU   B 1 119 ? 3.295  -17.721 29.088  1 45.503  ? 131 GLU   A O    1 ? 2 
ATOM   3540 C CB   . GLU   B 1 119 ? 1.833  -16.325 31.275  1 43.936  ? 131 GLU   A CB   1 ? 2 
ATOM   3541 C CG   . GLU   B 1 119 ? 1.608  -17.41  32.321  1 43.277  ? 131 GLU   A CG   1 ? 2 
ATOM   3542 C CD   . GLU   B 1 119 ? 0.19   -17.577 32.81   1 45.687  ? 131 GLU   A CD   1 ? 2 
ATOM   3543 O OE1  . GLU   B 1 119 ? -0.217 -17.137 33.91   1 49.825  ? 131 GLU   A OE1  1 ? 2 
ATOM   3544 O OE2  . GLU   B 1 119 ? -0.49  -18.265 32.064  1 47.928  ? 131 GLU   A OE2  1 ? 2 
ATOM   3545 H H    . GLU   B 1 119 ? 2.822  -14.876 29.404  1 39.862  ? 131 GLU   A H    1 c 2 
ATOM   3546 H HA   . GLU   B 1 119 ? 3.847  -16.041 31.719  1 41.103  ? 131 GLU   A HA   1 c 2 
ATOM   3547 H HB2  . GLU   B 1 119 ? 1.506  -15.469 31.621  1 43.201  ? 131 GLU   A HB2  1 c 2 
ATOM   3548 H HB3  . GLU   B 1 119 ? 1.32   -16.538 30.469  1 43.643  ? 131 GLU   A HB3  1 c 2 
ATOM   3549 H HG2  . GLU   B 1 119 ? 1.903  -18.268 31.951  1 43.875  ? 131 GLU   A HG2  1 c 2 
ATOM   3550 H HG3  . GLU   B 1 119 ? 2.177  -17.224 33.095  1 43.294  ? 131 GLU   A HG3  1 c 2 
ATOM   3551 N N    . ILE   B 1 120 ? 4.785  -18.118 30.742  1 43.311  ? 132 ILE   A N    1 ? 2 
ATOM   3552 C CA   . ILE   B 1 120 ? 5.35   -19.334 30.188  1 42.683  ? 132 ILE   A CA   1 ? 2 
ATOM   3553 C C    . ILE   B 1 120 ? 5.192  -20.476 31.196  1 42.986  ? 132 ILE   A C    1 ? 2 
ATOM   3554 O O    . ILE   B 1 120 ? 5.453  -20.306 32.391  1 40.937  ? 132 ILE   A O    1 ? 2 
ATOM   3555 C CB   . ILE   B 1 120 ? 6.84   -19.114 29.868  1 44.909  ? 132 ILE   A CB   1 ? 2 
ATOM   3556 C CG1  . ILE   B 1 120 ? 7.05   -17.921 28.956  1 38.938  ? 132 ILE   A CG1  1 ? 2 
ATOM   3557 C CG2  . ILE   B 1 120 ? 7.496  -20.407 29.352  1 39.617  ? 132 ILE   A CG2  1 ? 2 
ATOM   3558 C CD1  . ILE   B 1 120 ? 8.495  -17.621 28.642  1 37.917  ? 132 ILE   A CD1  1 ? 2 
ATOM   3559 H H    . ILE   B 1 120 ? 5.129  -17.808 31.53   1 42.851  ? 132 ILE   A H    1 c 2 
ATOM   3560 H HA   . ILE   B 1 120 ? 4.879  -19.561 29.364  1 43.707  ? 132 ILE   A HA   1 c 2 
ATOM   3561 H HB   . ILE   B 1 120 ? 7.278  -18.896 30.715  1 41.901  ? 132 ILE   A HB   1 c 2 
ATOM   3562 H HG12 . ILE   B 1 120 ? 6.574  -18.083 28.116  1 40.307  ? 132 ILE   A HG12 1 c 2 
ATOM   3563 H HG13 . ILE   B 1 120 ? 6.653  -17.131 29.376  1 39.629  ? 132 ILE   A HG13 1 c 2 
ATOM   3564 H HG21 . ILE   B 1 120 ? 8.442  -20.253 29.19   1 40.784  ? 132 ILE   A HG21 1 c 2 
ATOM   3565 H HG22 . ILE   B 1 120 ? 7.068  -20.68  28.523  1 41.75   ? 132 ILE   A HG22 1 c 2 
ATOM   3566 H HG23 . ILE   B 1 120 ? 7.397  -21.112 30.012  1 42.107  ? 132 ILE   A HG23 1 c 2 
ATOM   3567 H HD11 . ILE   B 1 120 ? 9.008  -17.582 29.472  1 37.878  ? 132 ILE   A HD11 1 c 2 
ATOM   3568 H HD12 . ILE   B 1 120 ? 8.556  -16.761 28.185  1 37.354  ? 132 ILE   A HD12 1 c 2 
ATOM   3569 H HD13 . ILE   B 1 120 ? 8.862  -18.318 28.067  1 38.404  ? 132 ILE   A HD13 1 c 2 
ATOM   3570 N N    . GLU   B 1 121 ? 4.74   -21.626 30.669  1 42.999  ? 133 GLU   A N    1 ? 2 
ATOM   3571 C CA   . GLU   B 1 121 ? 4.714  -22.911 31.354  1 43.068  ? 133 GLU   A CA   1 ? 2 
ATOM   3572 C C    . GLU   B 1 121 ? 5.733  -23.816 30.669  1 42.756  ? 133 GLU   A C    1 ? 2 
ATOM   3573 O O    . GLU   B 1 121 ? 5.592  -24.114 29.47   1 43.192  ? 133 GLU   A O    1 ? 2 
ATOM   3574 C CB   . GLU   B 1 121 ? 3.297  -23.495 31.31   1 43.969  ? 133 GLU   A CB   1 ? 2 
ATOM   3575 C CG   . GLU   B 1 121 ? 3.205  -24.895 31.917  1 49.829  ? 133 GLU   A CG   1 ? 2 
ATOM   3576 C CD   . GLU   B 1 121 ? 1.851  -25.607 32.027  1 51.37   ? 133 GLU   A CD   1 ? 2 
ATOM   3577 O OE1  . GLU   B 1 121 ? 0.85   -25.347 31.329  1 50.574  ? 133 GLU   A OE1  1 ? 2 
ATOM   3578 O OE2  . GLU   B 1 121 ? 1.814  -26.483 32.916  1 58.557  ? 133 GLU   A OE2  1 ? 2 
ATOM   3579 H H    . GLU   B 1 121 ? 4.421  -21.601 29.813  1 43.123  ? 133 GLU   A H    1 c 2 
ATOM   3580 H HA   . GLU   B 1 121 ? 4.979  -22.773 32.295  1 42.904  ? 133 GLU   A HA   1 c 2 
ATOM   3581 H HB2  . GLU   B 1 121 ? 2.69   -22.892 31.787  1 44.923  ? 133 GLU   A HB2  1 c 2 
ATOM   3582 H HB3  . GLU   B 1 121 ? 3.003  -23.535 30.376  1 45.211  ? 133 GLU   A HB3  1 c 2 
ATOM   3583 H HG2  . GLU   B 1 121 ? 3.799  -25.483 31.406  1 48.991  ? 133 GLU   A HG2  1 c 2 
ATOM   3584 H HG3  . GLU   B 1 121 ? 3.585  -24.852 32.821  1 48.636  ? 133 GLU   A HG3  1 c 2 
ATOM   3585 N N    . LEU   B 1 122 ? 6.759  -24.237 31.427  1 40.749  ? 134 LEU   A N    1 ? 2 
ATOM   3586 C CA   . LEU   B 1 122 ? 7.725  -25.22  30.941  1 42.547  ? 134 LEU   A CA   1 ? 2 
ATOM   3587 C C    . LEU   B 1 122 ? 7.192  -26.643 31.094  1 44.555  ? 134 LEU   A C    1 ? 2 
ATOM   3588 O O    . LEU   B 1 122 ? 7.123  -27.151 32.205  1 47.113  ? 134 LEU   A O    1 ? 2 
ATOM   3589 C CB   . LEU   B 1 122 ? 9.05   -25.033 31.683  1 39.262  ? 134 LEU   A CB   1 ? 2 
ATOM   3590 C CG   . LEU   B 1 122 ? 10.199 -25.953 31.246  1 40.439  ? 134 LEU   A CG   1 ? 2 
ATOM   3591 C CD1  . LEU   B 1 122 ? 10.494 -25.868 29.767  1 37.692  ? 134 LEU   A CD1  1 ? 2 
ATOM   3592 C CD2  . LEU   B 1 122 ? 11.452 -25.621 32.042  1 40.259  ? 134 LEU   A CD2  1 ? 2 
ATOM   3593 H H    . LEU   B 1 122 ? 6.861  -23.901 32.271  1 41.194  ? 134 LEU   A H    1 c 2 
ATOM   3594 H HA   . LEU   B 1 122 ? 7.874  -25.046 29.978  1 41.378  ? 134 LEU   A HA   1 c 2 
ATOM   3595 H HB2  . LEU   B 1 122 ? 9.338  -24.099 31.565  1 38.494  ? 134 LEU   A HB2  1 c 2 
ATOM   3596 H HB3  . LEU   B 1 122 ? 8.887  -25.175 32.644  1 40.428  ? 134 LEU   A HB3  1 c 2 
ATOM   3597 H HG   . LEU   B 1 122 ? 9.944  -26.888 31.454  1 41.543  ? 134 LEU   A HG   1 c 2 
ATOM   3598 H HD11 . LEU   B 1 122 ? 9.74   -26.218 29.263  1 39.023  ? 134 LEU   A HD11 1 c 2 
ATOM   3599 H HD12 . LEU   B 1 122 ? 11.287 -26.391 29.564  1 39.277  ? 134 LEU   A HD12 1 c 2 
ATOM   3600 H HD13 . LEU   B 1 122 ? 10.646 -24.94  29.519  1 36.959  ? 134 LEU   A HD13 1 c 2 
ATOM   3601 H HD21 . LEU   B 1 122 ? 11.266 -25.704 32.99   1 40.731  ? 134 LEU   A HD21 1 c 2 
ATOM   3602 H HD22 . LEU   B 1 122 ? 11.73  -24.711 31.846  1 38.886  ? 134 LEU   A HD22 1 c 2 
ATOM   3603 H HD23 . LEU   B 1 122 ? 12.164 -26.235 31.797  1 41.276  ? 134 LEU   A HD23 1 c 2 
ATOM   3604 N N    . LEU   B 1 123 ? 6.919  -27.321 29.972  1 50.291  ? 135 LEU   A N    1 ? 2 
ATOM   3605 C CA   . LEU   B 1 123 ? 6.235  -28.618 29.979  1 52.053  ? 135 LEU   A CA   1 ? 2 
ATOM   3606 C C    . LEU   B 1 123 ? 7.222  -29.773 30.154  1 56.503  ? 135 LEU   A C    1 ? 2 
ATOM   3607 O O    . LEU   B 1 123 ? 6.958  -30.698 30.923  1 58.209  ? 135 LEU   A O    1 ? 2 
ATOM   3608 C CB   . LEU   B 1 123 ? 5.435  -28.807 28.69   1 54.002  ? 135 LEU   A CB   1 ? 2 
ATOM   3609 C CG   . LEU   B 1 123 ? 4.332  -27.78  28.402  1 55.626  ? 135 LEU   A CG   1 ? 2 
ATOM   3610 C CD1  . LEU   B 1 123 ? 3.629  -28.051 27.069  1 59.936  ? 135 LEU   A CD1  1 ? 2 
ATOM   3611 C CD2  . LEU   B 1 123 ? 3.283  -27.78  29.493  1 56.287  ? 135 LEU   A CD2  1 ? 2 
ATOM   3612 H H    . LEU   B 1 123 ? 7.169  -26.966 29.167  1 48.222  ? 135 LEU   A H    1 c 2 
ATOM   3613 H HA   . LEU   B 1 123 ? 5.611  -28.631 30.748  1 53.237  ? 135 LEU   A HA   1 c 2 
ATOM   3614 H HB2  . LEU   B 1 123 ? 6.066  -28.802 27.934  1 54.127  ? 135 LEU   A HB2  1 c 2 
ATOM   3615 H HB3  . LEU   B 1 123 ? 5.022  -29.701 28.716  1 56.331  ? 135 LEU   A HB3  1 c 2 
ATOM   3616 H HG   . LEU   B 1 123 ? 4.744  -26.878 28.362  1 53.75   ? 135 LEU   A HG   1 c 2 
ATOM   3617 H HD11 . LEU   B 1 123 ? 4.278  -28.021 26.346  1 58.779  ? 135 LEU   A HD11 1 c 2 
ATOM   3618 H HD12 . LEU   B 1 123 ? 2.946  -27.376 26.918  1 58.527  ? 135 LEU   A HD12 1 c 2 
ATOM   3619 H HD13 . LEU   B 1 123 ? 3.213  -28.93  27.094  1 61.058  ? 135 LEU   A HD13 1 c 2 
ATOM   3620 H HD21 . LEU   B 1 123 ? 3.687  -27.511 30.335  1 55.384  ? 135 LEU   A HD21 1 c 2 
ATOM   3621 H HD22 . LEU   B 1 123 ? 2.91   -28.673 29.586  1 58.202  ? 135 LEU   A HD22 1 c 2 
ATOM   3622 H HD23 . LEU   B 1 123 ? 2.574  -27.157 29.263  1 55.92   ? 135 LEU   A HD23 1 c 2 
ATOM   3623 N N    . ASP   B 1 124 ? 8.331  -29.73  29.397  1 57.287  ? 136 ASP   A N    1 ? 2 
ATOM   3624 C CA   . ASP   B 1 124 ? 9.347  -30.77  29.385  1 58.01   ? 136 ASP   A CA   1 ? 2 
ATOM   3625 C C    . ASP   B 1 124 ? 10.606 -30.193 28.739  1 59.446  ? 136 ASP   A C    1 ? 2 
ATOM   3626 O O    . ASP   B 1 124 ? 10.528 -29.147 28.101  1 66.497  ? 136 ASP   A O    1 ? 2 
ATOM   3627 C CB   . ASP   B 1 124 ? 8.879  -31.989 28.6    1 60.483  ? 136 ASP   A CB   1 ? 2 
ATOM   3628 C CG   . ASP   B 1 124 ? 9.585  -33.321 28.875  1 60.57   ? 136 ASP   A CG   1 ? 2 
ATOM   3629 O OD1  . ASP   B 1 124 ? 10.272 -33.455 29.921  1 59.962  ? 136 ASP   A OD1  1 ? 2 
ATOM   3630 O OD2  . ASP   B 1 124 ? 9.425  -34.235 28.053  1 63.595  ? 136 ASP   A OD2  1 ? 2 
ATOM   3631 H H    . ASP   B 1 124 ? 8.452  -29.007 28.852  1 55.324  ? 136 ASP   A H    1 c 2 
ATOM   3632 H HA   . ASP   B 1 124 ? 9.549  -31.024 30.312  1 59.141  ? 136 ASP   A HA   1 c 2 
ATOM   3633 H HB2  . ASP   B 1 124 ? 7.925  -32.122 28.778  1 60.369  ? 136 ASP   A HB2  1 c 2 
ATOM   3634 H HB3  . ASP   B 1 124 ? 8.974  -31.796 27.644  1 59.716  ? 136 ASP   A HB3  1 c 2 
ATOM   3635 N N    . PHE   B 1 125 ? 11.759 -30.857 28.926  1 58.306  ? 137 PHE   A N    1 ? 2 
ATOM   3636 C CA   . PHE   B 1 125 ? 12.976 -30.507 28.217  1 56.806  ? 137 PHE   A CA   1 ? 2 
ATOM   3637 C C    . PHE   B 1 125 ? 13.842 -31.756 28.083  1 64.683  ? 137 PHE   A C    1 ? 2 
ATOM   3638 O O    . PHE   B 1 125 ? 13.906 -32.564 29.011  1 64.13   ? 137 PHE   A O    1 ? 2 
ATOM   3639 C CB   . PHE   B 1 125 ? 13.72  -29.357 28.898  1 54.184  ? 137 PHE   A CB   1 ? 2 
ATOM   3640 C CG   . PHE   B 1 125 ? 14.142 -29.563 30.349  1 56.47   ? 137 PHE   A CG   1 ? 2 
ATOM   3641 C CD1  . PHE   B 1 125 ? 15.362 -30.14  30.677  1 63.616  ? 137 PHE   A CD1  1 ? 2 
ATOM   3642 C CD2  . PHE   B 1 125 ? 13.338 -29.137 31.392  1 58.578  ? 137 PHE   A CD2  1 ? 2 
ATOM   3643 C CE1  . PHE   B 1 125 ? 15.745 -30.317 32.006  1 61.995  ? 137 PHE   A CE1  1 ? 2 
ATOM   3644 C CE2  . PHE   B 1 125 ? 13.728 -29.304 32.716  1 61.008  ? 137 PHE   A CE2  1 ? 2 
ATOM   3645 C CZ   . PHE   B 1 125 ? 14.932 -29.886 33.02   1 60.875  ? 137 PHE   A CZ   1 ? 2 
ATOM   3646 H H    . PHE   B 1 125 ? 11.783 -31.548 29.524  1 60.079  ? 137 PHE   A H    1 c 2 
ATOM   3647 H HA   . PHE   B 1 125 ? 12.72  -30.21  27.307  1 57.373  ? 137 PHE   A HA   1 c 2 
ATOM   3648 H HB2  . PHE   B 1 125 ? 14.525 -29.162 28.368  1 54.702  ? 137 PHE   A HB2  1 c 2 
ATOM   3649 H HB3  . PHE   B 1 125 ? 13.15  -28.558 28.853  1 52.896  ? 137 PHE   A HB3  1 c 2 
ATOM   3650 H HD1  . PHE   B 1 125 ? 15.933 -30.438 29.986  1 62.655  ? 137 PHE   A HD1  1 c 2 
ATOM   3651 H HD2  . PHE   B 1 125 ? 12.509 -28.729 31.2    1 57.067  ? 137 PHE   A HD2  1 c 2 
ATOM   3652 H HE1  . PHE   B 1 125 ? 16.576 -30.718 32.206  1 64.049  ? 137 PHE   A HE1  1 c 2 
ATOM   3653 H HE2  . PHE   B 1 125 ? 13.159 -29.013 33.411  1 59.59   ? 137 PHE   A HE2  1 c 2 
ATOM   3654 H HZ   . PHE   B 1 125 ? 15.189 -30.006 33.92   1 62.148  ? 137 PHE   A HZ   1 c 2 
ATOM   3655 N N    . LYS   B 1 126 ? 14.496 -31.893 26.919  1 64.994  ? 138 LYS   A N    1 ? 2 
ATOM   3656 C CA   . LYS   B 1 126 ? 15.228 -33.102 26.573  1 68.589  ? 138 LYS   A CA   1 ? 2 
ATOM   3657 C C    . LYS   B 1 126 ? 16.607 -32.7   26.059  1 68.55   ? 138 LYS   A C    1 ? 2 
ATOM   3658 O O    . LYS   B 1 126 ? 16.739 -31.779 25.263  1 63.938  ? 138 LYS   A O    1 ? 2 
ATOM   3659 C CB   . LYS   B 1 126 ? 14.496 -33.952 25.523  1 68.587  ? 138 LYS   A CB   1 ? 2 
ATOM   3660 H H    . LYS   B 1 126 ? 14.486 -31.202 26.32   1 63.78   ? 138 LYS   A H    1 c 2 
ATOM   3661 H HA   . LYS   B 1 126 ? 15.342 -33.646 27.392  1 69.258  ? 138 LYS   A HA   1 c 2 
ATOM   3662 H HB2  . LYS   B 1 126 ? 15.078 -34.441 24.955  0 30      ? 138 LYS   A HB2  1 c 2 
ATOM   3663 H HB3  . LYS   B 1 126 ? 13.464 -33.864 25.675  0 30      ? 138 LYS   A HB3  1 c 2 
ATOM   3664 N N    . GLY   B 1 127 ? 17.64  -33.384 26.548  1 74.147  ? 139 GLY   A N    1 ? 2 
ATOM   3665 C CA   . GLY   B 1 127 ? 18.958 -33.295 25.955  1 78.724  ? 139 GLY   A CA   1 ? 2 
ATOM   3666 C C    . GLY   B 1 127 ? 18.898 -33.786 24.514  1 84.976  ? 139 GLY   A C    1 ? 2 
ATOM   3667 O O    . GLY   B 1 127 ? 18.595 -34.957 24.296  1 89.138  ? 139 GLY   A O    1 ? 2 
ATOM   3668 H H    . GLY   B 1 127 ? 17.521 -33.924 27.276  1 74.991  ? 139 GLY   A H    1 c 2 
ATOM   3669 H HA2  . GLY   B 1 127 ? 19.269 -32.362 25.982  1 76.786  ? 139 GLY   A HA2  1 c 2 
ATOM   3670 H HA3  . GLY   B 1 127 ? 19.59  -33.848 26.472  1 80.695  ? 139 GLY   A HA3  1 c 2 
ATOM   3671 N N    . GLU   B 1 128 ? 19.15  -32.865 23.566  1 83.653  ? 140 GLU   A N    1 ? 2 
ATOM   3672 C CA   . GLU   B 1 128 ? 19.031 -33.108 22.133  1 87.569  ? 140 GLU   A CA   1 ? 2 
ATOM   3673 C C    . GLU   B 1 128 ? 19.591 -34.501 21.762  1 97.154  ? 140 GLU   A C    1 ? 2 
ATOM   3674 O O    . GLU   B 1 128 ? 20.541 -34.956 22.45   1 105.046 ? 140 GLU   A O    1 ? 2 
ATOM   3675 C CB   . GLU   B 1 128 ? 19.725 -31.974 21.37   1 80.572  ? 140 GLU   A CB   1 ? 2 
ATOM   3676 O OXT  . GLU   B 1 128 ? 19.052 -35.097 20.795  1 98.572  ? 140 GLU   A OXT  1 ? 2 
ATOM   3677 H H    . GLU   B 1 128 ? 19.41  -32.033 23.838  1 82.09   ? 140 GLU   A H    1 c 2 
ATOM   3678 H HA   . GLU   B 1 128 ? 18.068 -33.091 21.9    1 86.118  ? 140 GLU   A HA   1 c 2 
ATOM   3679 H HB2  . GLU   B 1 128 ? 20.709 -32.161 21.394  0 30      ? 140 GLU   A HB2  1 c 2 
ATOM   3680 H HB3  . GLU   B 1 128 ? 19.016 -31.523 20.975  0 30      ? 140 GLU   A HB3  1 c 2 
HETATM 3681 C CAM  . A1IN6 C 2 .   ? 18.127 7.979   11.935  1 35.938  ? 201 A1IN6 B CAM  1 ? 1 
HETATM 3682 C CAN  . A1IN6 C 2 .   ? 17.132 9.082   11.812  1 37.733  ? 201 A1IN6 B CAN  1 ? 1 
HETATM 3683 C CAO  . A1IN6 C 2 .   ? 17.074 9.401   10.284  1 37.005  ? 201 A1IN6 B CAO  1 ? 1 
HETATM 3684 C CAP  . A1IN6 C 2 .   ? 16.611 8.168   9.496   1 34.923  ? 201 A1IN6 B CAP  1 ? 1 
HETATM 3685 C CAQ  . A1IN6 C 2 .   ? 17.58  7.057   9.65    1 34.38   ? 201 A1IN6 B CAQ  1 ? 1 
HETATM 3686 C CAL  . A1IN6 C 2 .   ? 17.629 6.779   11.194  1 33.024  ? 201 A1IN6 B CAL  1 ? 1 
HETATM 3687 C CAG  . A1IN6 C 2 .   ? 18.458 5.481   11.577  1 34.248  ? 201 A1IN6 B CAG  1 ? 1 
HETATM 3688 C CAH  . A1IN6 C 2 .   ? 17.905 4.262   11.065  1 33.513  ? 201 A1IN6 B CAH  1 ? 1 
HETATM 3689 O OAK  . A1IN6 C 2 .   ? 16.695 4.126   10.863  1 33.674  ? 201 A1IN6 B OAK  1 ? 1 
HETATM 3690 N N    . A1IN6 C 2 .   ? 18.651 3.169   10.913  1 34.201  ? 201 A1IN6 B N    1 ? 1 
HETATM 3691 C CAV  . A1IN6 C 2 .   ? 20.143 3.185   11.244  1 36.433  ? 201 A1IN6 B CAV  1 ? 1 
HETATM 3692 C CAU  . A1IN6 C 2 .   ? 20.893 2.564   10.223  1 37.164  ? 201 A1IN6 B CAU  1 ? 1 
HETATM 3693 C CAT  . A1IN6 C 2 .   ? 20.419 1.134   10.057  1 36.143  ? 201 A1IN6 B CAT  1 ? 1 
HETATM 3694 C CB   . A1IN6 C 2 .   ? 19.008 1.116   9.503   1 33.098  ? 201 A1IN6 B CB   1 ? 1 
HETATM 3695 C CA   . A1IN6 C 2 .   ? 18.04  1.863   10.52   1 31.877  ? 201 A1IN6 B CA   1 ? 1 
HETATM 3696 C C    . A1IN6 C 2 .   ? 17.722 1.041   11.67   1 33.143  ? 201 A1IN6 B C    1 ? 1 
HETATM 3697 O O    . A1IN6 C 2 .   ? 17.28  -0.101  11.548  1 30.096  ? 201 A1IN6 B O    1 ? 1 
HETATM 3698 O OAY  . A1IN6 C 2 .   ? 17.857 1.649   12.917  1 39.069  ? 201 A1IN6 B OAY  1 ? 1 
HETATM 3699 C CAZ  . A1IN6 C 2 .   ? 17.611 0.82    14.092  1 36.283  ? 201 A1IN6 B CAZ  1 ? 1 
HETATM 3700 C CBA  . A1IN6 C 2 .   ? 18.849 0.067   14.618  1 37.198  ? 201 A1IN6 B CBA  1 ? 1 
HETATM 3701 C CBB  . A1IN6 C 2 .   ? 19.978 0.945   15.029  1 39.545  ? 201 A1IN6 B CBB  1 ? 1 
HETATM 3702 C CBC  . A1IN6 C 2 .   ? 19.529 1.622   16.385  1 44.057  ? 201 A1IN6 B CBC  1 ? 1 
HETATM 3703 C CBE  . A1IN6 C 2 .   ? 20.451 2.783   16.796  1 48.769  ? 201 A1IN6 B CBE  1 ? 1 
HETATM 3704 C CBD  . A1IN6 C 2 .   ? 19.691 3.675   17.82   1 49.83   ? 201 A1IN6 B CBD  1 ? 1 
HETATM 3705 O OAI  . A1IN6 C 2 .   ? 19.041 4.796   17.21   1 47.84   ? 201 A1IN6 B OAI  1 ? 1 
HETATM 3706 C CAC  . A1IN6 C 2 .   ? 18.894 4.943   15.838  1 41.163  ? 201 A1IN6 B CAC  1 ? 1 
HETATM 3707 C CAB  . A1IN6 C 2 .   ? 19.924 5.473   15.082  1 40.04   ? 201 A1IN6 B CAB  1 ? 1 
HETATM 3708 O OBH  . A1IN6 C 2 .   ? 21.052 5.824   15.768  1 43.788  ? 201 A1IN6 B OBH  1 ? 1 
HETATM 3709 C CBI  . A1IN6 C 2 .   ? 22.386 5.617   15.211  1 44.498  ? 201 A1IN6 B CBI  1 ? 1 
HETATM 3710 C CAA  . A1IN6 C 2 .   ? 19.765 5.639   13.719  1 37.433  ? 201 A1IN6 B CAA  1 ? 1 
HETATM 3711 C CAF  . A1IN6 C 2 .   ? 18.573 5.294   13.043  1 36.078  ? 201 A1IN6 B CAF  1 ? 1 
HETATM 3712 C CAE  . A1IN6 C 2 .   ? 17.524 4.773   13.821  1 35.29   ? 201 A1IN6 B CAE  1 ? 1 
HETATM 3713 C CAD  . A1IN6 C 2 .   ? 17.687 4.647   15.231  1 39.022  ? 201 A1IN6 B CAD  1 ? 1 
HETATM 3714 O OBF  . A1IN6 C 2 .   ? 16.776 4.116   16.054  1 37.488  ? 201 A1IN6 B OBF  1 ? 1 
HETATM 3715 C CBG  . A1IN6 C 2 .   ? 15.389 4.194   15.837  1 36.687  ? 201 A1IN6 B CBG  1 ? 1 
HETATM 3716 H HAM  . A1IN6 C 2 .   ? 18.282 7.67    12.888  1 37.429  ? 201 A1IN6 B HAM  1 c 1 
HETATM 3717 H HAN  . A1IN6 C 2 .   ? 18.947 8.5     11.49   1 37.455  ? 201 A1IN6 B HAN  1 c 1 
HETATM 3718 H HAO  . A1IN6 C 2 .   ? 17.48  9.956   12.367  1 39.774  ? 201 A1IN6 B HAO  1 c 1 
HETATM 3719 H HAP  . A1IN6 C 2 .   ? 16.159 8.775   12.182  1 36.936  ? 201 A1IN6 B HAP  1 c 1 
HETATM 3720 H HAQ  . A1IN6 C 2 .   ? 18.056 9.709   9.926   1 37.998  ? 201 A1IN6 B HAQ  1 c 1 
HETATM 3721 H HAR  . A1IN6 C 2 .   ? 16.367 10.213  10.118  1 37.515  ? 201 A1IN6 B HAR  1 c 1 
HETATM 3722 H HAS  . A1IN6 C 2 .   ? 16.533 8.428   8.441   1 34.366  ? 201 A1IN6 B HAS  1 c 1 
HETATM 3723 H HAT  . A1IN6 C 2 .   ? 15.633 7.852   9.859   1 34.126  ? 201 A1IN6 B HAT  1 c 1 
HETATM 3724 H HAV  . A1IN6 C 2 .   ? 17.26  6.143   9.273   1 32.357  ? 201 A1IN6 B HAV  1 c 1 
HETATM 3725 H HAU  . A1IN6 C 2 .   ? 18.581 7.308   9.453   1 34.816  ? 201 A1IN6 B HAU  1 c 1 
HETATM 3726 H HAL  . A1IN6 C 2 .   ? 16.609 6.599   11.521  1 33.237  ? 201 A1IN6 B HAL  1 c 1 
HETATM 3727 H HAG  . A1IN6 C 2 .   ? 19.442 5.639   11.154  1 35.02   ? 201 A1IN6 B HAG  1 c 1 
HETATM 3728 H HB7  . A1IN6 C 2 .   ? 20.3   2.639   12.172  1 37.616  ? 201 A1IN6 B HB7  1 c 1 
HETATM 3729 H HB8  . A1IN6 C 2 .   ? 20.533 4.187   11.362  1 37.949  ? 201 A1IN6 B HB8  1 c 1 
HETATM 3730 H HB5  . A1IN6 C 2 .   ? 21.904 2.522   10.453  1 38.547  ? 201 A1IN6 B HB5  1 c 1 
HETATM 3731 H HB6  . A1IN6 C 2 .   ? 20.713 2.963   9.279   1 36.182  ? 201 A1IN6 B HB6  1 c 1 
HETATM 3732 H HB3  . A1IN6 C 2 .   ? 20.306 0.583   10.939  1 36.296  ? 201 A1IN6 B HB3  1 c 1 
HETATM 3733 H HB4  . A1IN6 C 2 .   ? 20.918 0.619   9.3     1 35.533  ? 201 A1IN6 B HB4  1 c 1 
HETATM 3734 H HB2  . A1IN6 C 2 .   ? 18.875 1.713   8.655   1 32.464  ? 201 A1IN6 B HB2  1 c 1 
HETATM 3735 H HB1  . A1IN6 C 2 .   ? 18.559 0.195   9.437   1 32.202  ? 201 A1IN6 B HB1  1 c 1 
HETATM 3736 H HA   . A1IN6 C 2 .   ? 17.111 2.046   9.982   1 31.361  ? 201 A1IN6 B HA   1 c 1 
HETATM 3737 H HB9  . A1IN6 C 2 .   ? 17.223 1.471   14.867  1 38.298  ? 201 A1IN6 B HB9  1 c 1 
HETATM 3738 H HAZ  . A1IN6 C 2 .   ? 16.842 0.083   13.871  1 35.966  ? 201 A1IN6 B HAZ  1 c 1 
HETATM 3739 H HCA  . A1IN6 C 2 .   ? 18.552 -0.538  15.473  1 38.61   ? 201 A1IN6 B HCA  1 c 1 
HETATM 3740 H HBA  . A1IN6 C 2 .   ? 19.206 -0.595  13.832  1 36.278  ? 201 A1IN6 B HBA  1 c 1 
HETATM 3741 H HCB  . A1IN6 C 2 .   ? 20.878 0.347   15.184  1 41.09   ? 201 A1IN6 B HCB  1 c 1 
HETATM 3742 H HBB  . A1IN6 C 2 .   ? 20.162 1.705   14.27   1 39.151  ? 201 A1IN6 B HBB  1 c 1 
HETATM 3743 H HCC  . A1IN6 C 2 .   ? 18.528 2.021   16.288  1 43.063  ? 201 A1IN6 B HCC  1 c 1 
HETATM 3744 H HBC  . A1IN6 C 2 .   ? 19.538 0.873   17.175  1 45.48   ? 201 A1IN6 B HBC  1 c 1 
HETATM 3745 H HCE  . A1IN6 C 2 .   ? 21.325 2.365   17.294  1 50.123  ? 201 A1IN6 B HCE  1 c 1 
HETATM 3746 H HBE  . A1IN6 C 2 .   ? 20.783 3.318   15.92   1 46.85   ? 201 A1IN6 B HBE  1 c 1 
HETATM 3747 H HCD  . A1IN6 C 2 .   ? 18.799 3.277   18.197  1 49.458  ? 201 A1IN6 B HCD  1 c 1 
HETATM 3748 H HBD  . A1IN6 C 2 .   ? 20.3   4.136   18.518  1 52.685  ? 201 A1IN6 B HBD  1 c 1 
HETATM 3749 H HCI  . A1IN6 C 2 .   ? 23.134 5.803   15.982  1 47.629  ? 201 A1IN6 B HCI  1 c 1 
HETATM 3750 H HBI  . A1IN6 C 2 .   ? 22.547 6.308   14.384  1 44.06   ? 201 A1IN6 B HBI  1 c 1 
HETATM 3751 H HCH  . A1IN6 C 2 .   ? 22.48  4.594   14.852  1 43.022  ? 201 A1IN6 B HCH  1 c 1 
HETATM 3752 H HAA  . A1IN6 C 2 .   ? 20.588 6.048   13.144  1 38.488  ? 201 A1IN6 B HAA  1 c 1 
HETATM 3753 H HAE  . A1IN6 C 2 .   ? 16.581 4.487   13.365  1 34.113  ? 201 A1IN6 B HAE  1 c 1 
HETATM 3754 H HCG  . A1IN6 C 2 .   ? 14.863 3.86    16.732  1 38.017  ? 201 A1IN6 B HCG  1 c 1 
HETATM 3755 H HBG  . A1IN6 C 2 .   ? 15.117 3.558   14.997  1 34.571  ? 201 A1IN6 B HBG  1 c 1 
HETATM 3756 H HCF  . A1IN6 C 2 .   ? 15.113 5.226   15.618  1 36.83   ? 201 A1IN6 B HCF  1 c 1 
HETATM 3757 C CAM  . A1IN6 D 2 .   ? 3.672  -11.791 19.256  1 36.517  ? 201 A1IN6 A CAM  1 ? 2 
HETATM 3758 C CAN  . A1IN6 D 2 .   ? 2.877  -10.628 19.65   1 38.988  ? 201 A1IN6 A CAN  1 ? 2 
HETATM 3759 C CAO  . A1IN6 D 2 .   ? 2.552  -10.446 21.199  1 39.147  ? 201 A1IN6 A CAO  1 ? 2 
HETATM 3760 C CAP  . A1IN6 D 2 .   ? 3.781  -10.681 22.047  1 35.684  ? 201 A1IN6 A CAP  1 ? 2 
HETATM 3761 C CAQ  . A1IN6 D 2 .   ? 4.488  -12.01  21.703  1 32.863  ? 201 A1IN6 A CAQ  1 ? 2 
HETATM 3762 C CAL  . A1IN6 D 2 .   ? 4.882  -11.996 20.136  1 34.05   ? 201 A1IN6 A CAL  1 ? 2 
HETATM 3763 C CAG  . A1IN6 D 2 .   ? 5.588  -13.378 19.755  1 35.868  ? 201 A1IN6 A CAG  1 ? 2 
HETATM 3764 C CAH  . A1IN6 D 2 .   ? 6.86   -13.461 20.298  1 34.301  ? 201 A1IN6 A CAH  1 ? 2 
HETATM 3765 O OAK  . A1IN6 D 2 .   ? 7.545  -12.43  20.445  1 32.768  ? 201 A1IN6 A OAK  1 ? 2 
HETATM 3766 N N    . A1IN6 D 2 .   ? 7.392  -14.663 20.57   1 33.919  ? 201 A1IN6 A N    1 ? 2 
HETATM 3767 C CAV  . A1IN6 D 2 .   ? 6.692  -16     20.252  1 35.882  ? 201 A1IN6 A CAV  1 ? 2 
HETATM 3768 C CAU  . A1IN6 D 2 .   ? 7.046  -17.076 21.21   1 35.862  ? 201 A1IN6 A CAU  1 ? 2 
HETATM 3769 C CAT  . A1IN6 D 2 .   ? 8.632  -17.135 21.322  1 32.784  ? 201 A1IN6 A CAT  1 ? 2 
HETATM 3770 C CB   . A1IN6 D 2 .   ? 9.088  -15.878 22.047  1 32.677  ? 201 A1IN6 A CB   1 ? 2 
HETATM 3771 C CA   . A1IN6 D 2 .   ? 8.846  -14.696 21.037  1 33.361  ? 201 A1IN6 A CA   1 ? 2 
HETATM 3772 C C    . A1IN6 D 2 .   ? 9.663  -14.883 19.917  1 33.961  ? 201 A1IN6 A C    1 ? 2 
HETATM 3773 O O    . A1IN6 D 2 .   ? 10.881 -15.011 20.046  1 34.543  ? 201 A1IN6 A O    1 ? 2 
HETATM 3774 O OAY  . A1IN6 D 2 .   ? 9.046  -15.061 18.721  1 38.234  ? 201 A1IN6 A OAY  1 ? 2 
HETATM 3775 C CAZ  . A1IN6 D 2 .   ? 10.065 -15.336 17.735  1 42.487  ? 201 A1IN6 A CAZ  1 ? 2 
HETATM 3776 C CBA  . A1IN6 D 2 .   ? 9.567  -15.456 16.414  1 48.076  ? 201 A1IN6 A CBA  1 ? 2 
HETATM 3777 C CBB  . A1IN6 D 2 .   ? 8.761  -16.732 16.215  1 48.134  ? 201 A1IN6 A CBB  1 ? 2 
HETATM 3778 C CBC  . A1IN6 D 2 .   ? 8.475  -16.702 14.702  1 49.278  ? 201 A1IN6 A CBC  1 ? 2 
HETATM 3779 C CBE  . A1IN6 D 2 .   ? 6.98   -16.624 14.387  1 52.551  ? 201 A1IN6 A CBE  1 ? 2 
HETATM 3780 C CBD  . A1IN6 D 2 .   ? 6.646  -15.336 13.546  1 54.317  ? 201 A1IN6 A CBD  1 ? 2 
HETATM 3781 O OAI  . A1IN6 D 2 .   ? 5.645  -14.549 14.227  1 51.391  ? 201 A1IN6 A OAI  1 ? 2 
HETATM 3782 C CAC  . A1IN6 D 2 .   ? 5.685  -14.252 15.569  1 44.351  ? 201 A1IN6 A CAC  1 ? 2 
HETATM 3783 C CAB  . A1IN6 D 2 .   ? 4.873  -14.963 16.389  1 42.326  ? 201 A1IN6 A CAB  1 ? 2 
HETATM 3784 O OBH  . A1IN6 D 2 .   ? 4.213  -15.871 15.699  1 43.47   ? 201 A1IN6 A OBH  1 ? 2 
HETATM 3785 C CBI  . A1IN6 D 2 .   ? 3.077  -16.507 16.275  1 47.286  ? 201 A1IN6 A CBI  1 ? 2 
HETATM 3786 C CAA  . A1IN6 D 2 .   ? 4.849  -14.726 17.773  1 41.131  ? 201 A1IN6 A CAA  1 ? 2 
HETATM 3787 C CAF  . A1IN6 D 2 .   ? 5.632  -13.681 18.315  1 39.109  ? 201 A1IN6 A CAF  1 ? 2 
HETATM 3788 C CAE  . A1IN6 D 2 .   ? 6.45   -12.962 17.445  1 39.348  ? 201 A1IN6 A CAE  1 ? 2 
HETATM 3789 C CAD  . A1IN6 D 2 .   ? 6.469  -13.231 16.068  1 44.091  ? 201 A1IN6 A CAD  1 ? 2 
HETATM 3790 O OBF  . A1IN6 D 2 .   ? 7.242  -12.58  15.131  1 44.278  ? 201 A1IN6 A OBF  1 ? 2 
HETATM 3791 C CBG  . A1IN6 D 2 .   ? 8.066  -11.472 15.568  1 42.091  ? 201 A1IN6 A CBG  1 ? 2 
HETATM 3792 H HAM  . A1IN6 D 2 .   ? 4.143  -11.616 18.344  1 37.295  ? 201 A1IN6 A HAM  1 c 2 
HETATM 3793 H HAN  . A1IN6 D 2 .   ? 3.242  -12.828 19.358  1 37.548  ? 201 A1IN6 A HAN  1 c 2 
HETATM 3794 H HAO  . A1IN6 D 2 .   ? 1.928  -10.68  19.118  1 40.371  ? 201 A1IN6 A HAO  1 c 2 
HETATM 3795 H HAP  . A1IN6 D 2 .   ? 3.404  -9.735  19.316  1 38.353  ? 201 A1IN6 A HAP  1 c 2 
HETATM 3796 H HAQ  . A1IN6 D 2 .   ? 1.781  -11.156 21.491  1 39.369  ? 201 A1IN6 A HAQ  1 c 2 
HETATM 3797 H HAR  . A1IN6 D 2 .   ? 2.193  -9.433  21.374  1 38.866  ? 201 A1IN6 A HAR  1 c 2 
HETATM 3798 H HAS  . A1IN6 D 2 .   ? 3.493  -10.699 23.094  1 35.123  ? 201 A1IN6 A HAS  1 c 2 
HETATM 3799 H HAT  . A1IN6 D 2 .   ? 4.481  -9.861  21.887  1 34.808  ? 201 A1IN6 A HAT  1 c 2 
HETATM 3800 H HAV  . A1IN6 D 2 .   ? 5.428  -12.081 22.119  1 32.417  ? 201 A1IN6 A HAV  1 c 2 
HETATM 3801 H HAU  . A1IN6 D 2 .   ? 3.905  -12.893 21.757  1 34.227  ? 201 A1IN6 A HAU  1 c 2 
HETATM 3802 H HAL  . A1IN6 D 2 .   ? 5.571  -11.173 19.961  1 33.792  ? 201 A1IN6 A HAL  1 c 2 
HETATM 3803 H HAG  . A1IN6 D 2 .   ? 4.969  -14.131 20.228  1 36.27   ? 201 A1IN6 A HAG  1 c 2 
HETATM 3804 H HB7  . A1IN6 D 2 .   ? 6.961  -16.323 19.249  1 36.893  ? 201 A1IN6 A HB7  1 c 2 
HETATM 3805 H HB8  . A1IN6 D 2 .   ? 5.615  -15.893 20.301  1 36.505  ? 201 A1IN6 A HB8  1 c 2 
HETATM 3806 H HB5  . A1IN6 D 2 .   ? 6.851  -18.074 20.887  1 36.499  ? 201 A1IN6 A HB5  1 c 2 
HETATM 3807 H HB6  . A1IN6 D 2 .   ? 6.778  -16.883 22.203  1 34.524  ? 201 A1IN6 A HB6  1 c 2 
HETATM 3808 H HB3  . A1IN6 D 2 .   ? 9.15   -17.071 20.424  1 34.138  ? 201 A1IN6 A HB3  1 c 2 
HETATM 3809 H HB4  . A1IN6 D 2 .   ? 8.995  -17.858 21.982  1 33.576  ? 201 A1IN6 A HB4  1 c 2 
HETATM 3810 H HB2  . A1IN6 D 2 .   ? 8.505  -15.563 22.849  1 32.008  ? 201 A1IN6 A HB2  1 c 2 
HETATM 3811 H HB1  . A1IN6 D 2 .   ? 10.115 -15.917 22.231  1 32.113  ? 201 A1IN6 A HB1  1 c 2 
HETATM 3812 H HA   . A1IN6 D 2 .   ? 9.115  -13.763 21.531  1 32.206  ? 201 A1IN6 A HA   1 c 2 
HETATM 3813 H HB9  . A1IN6 D 2 .   ? 10.792 -14.521 17.725  1 41.766  ? 201 A1IN6 A HB9  1 c 2 
HETATM 3814 H HAZ  . A1IN6 D 2 .   ? 10.574 -16.269 17.984  1 42.755  ? 201 A1IN6 A HAZ  1 c 2 
HETATM 3815 H HCA  . A1IN6 D 2 .   ? 8.937  -14.595 16.197  1 46.754  ? 201 A1IN6 A HCA  1 c 2 
HETATM 3816 H HBA  . A1IN6 D 2 .   ? 10.424 -15.452 15.737  1 47.469  ? 201 A1IN6 A HBA  1 c 2 
HETATM 3817 H HCB  . A1IN6 D 2 .   ? 9.359  -17.607 16.475  1 48.397  ? 201 A1IN6 A HCB  1 c 2 
HETATM 3818 H HBB  . A1IN6 D 2 .   ? 7.849  -16.703 16.812  1 47.84   ? 201 A1IN6 A HBB  1 c 2 
HETATM 3819 H HCC  . A1IN6 D 2 .   ? 8.984  -15.86  14.234  1 49.788  ? 201 A1IN6 A HCC  1 c 2 
HETATM 3820 H HBC  . A1IN6 D 2 .   ? 8.864  -17.625 14.274  1 51.312  ? 201 A1IN6 A HBC  1 c 2 
HETATM 3821 H HCE  . A1IN6 D 2 .   ? 6.723  -17.49  13.779  1 54.278  ? 201 A1IN6 A HCE  1 c 2 
HETATM 3822 H HBE  . A1IN6 D 2 .   ? 6.411  -16.678 15.298  1 51.231  ? 201 A1IN6 A HBE  1 c 2 
HETATM 3823 H HCD  . A1IN6 D 2 .   ? 7.353  -14.548 13.54   1 52.483  ? 201 A1IN6 A HCD  1 c 2 
HETATM 3824 H HBD  . A1IN6 D 2 .   ? 6.034  -15.456 12.688  1 55.588  ? 201 A1IN6 A HBD  1 c 2 
HETATM 3825 H HCI  . A1IN6 D 2 .   ? 2.587  -17.126 15.523  1 48.585  ? 201 A1IN6 A HCI  1 c 2 
HETATM 3826 H HBI  . A1IN6 D 2 .   ? 2.379  -15.751 16.634  1 46.217  ? 201 A1IN6 A HBI  1 c 2 
HETATM 3827 H HCH  . A1IN6 D 2 .   ? 3.395  -17.134 17.109  1 45.416  ? 201 A1IN6 A HCH  1 c 2 
HETATM 3828 H HAA  . A1IN6 D 2 .   ? 4.19   -15.296 18.411  1 41.227  ? 201 A1IN6 A HAA  1 c 2 
HETATM 3829 H HAE  . A1IN6 D 2 .   ? 7.066  -12.16  17.848  1 38.706  ? 201 A1IN6 A HAE  1 c 2 
HETATM 3830 H HCG  . A1IN6 D 2 .   ? 8.575  -11.044 14.706  1 43.07   ? 201 A1IN6 A HCG  1 c 2 
HETATM 3831 H HBG  . A1IN6 D 2 .   ? 8.807  -11.827 16.282  1 41.071  ? 201 A1IN6 A HBG  1 c 2 
HETATM 3832 H HCF  . A1IN6 D 2 .   ? 7.442  -10.709 16.033  1 41.817  ? 201 A1IN6 A HCF  1 c 2 
HETATM 3833 O O    . HOH   E 3 .   ? 9.361  3.487   -1.342  1 37.551  ? 301 HOH   B O    1 ? ? 
HETATM 3834 O O    . HOH   E 3 .   ? 7.197  5.501   11.318  1 41.209  ? 302 HOH   B O    1 ? ? 
HETATM 3835 O O    . HOH   E 3 .   ? 3.568  5.77    18.538  1 45.285  ? 303 HOH   B O    1 ? ? 
HETATM 3836 O O    . HOH   E 3 .   ? 18.846 -7.767  10.777  1 31.269  ? 304 HOH   B O    1 ? ? 
HETATM 3837 O O    . HOH   E 3 .   ? 8.925  4.635   9.337   1 30.297  ? 305 HOH   B O    1 ? ? 
HETATM 3838 O O    . HOH   E 3 .   ? 1.358  -4.602  0.91    1 56.67   ? 306 HOH   B O    1 ? ? 
HETATM 3839 O O    . HOH   E 3 .   ? 10.767 11.031  -3.485  1 58.095  ? 307 HOH   B O    1 ? ? 
HETATM 3840 O O    . HOH   E 3 .   ? 23.984 -3.283  15.079  1 54.111  ? 308 HOH   B O    1 ? ? 
HETATM 3841 O O    . HOH   E 3 .   ? 10.348 -8.175  0.199   1 43.543  ? 309 HOH   B O    1 ? ? 
HETATM 3842 O O    . HOH   E 3 .   ? 7.838  -0.136  -9.708  1 35.903  ? 310 HOH   B O    1 ? ? 
HETATM 3843 O O    . HOH   E 3 .   ? 7.817  5.621   -1.484  1 43.131  ? 311 HOH   B O    1 ? ? 
HETATM 3844 O O    . HOH   E 3 .   ? 8.984  11.626  7.828   1 38.382  ? 312 HOH   B O    1 ? ? 
HETATM 3845 O O    . HOH   E 3 .   ? 15.263 11.153  20.089  1 52.353  ? 313 HOH   B O    1 ? ? 
HETATM 3846 O O    . HOH   E 3 .   ? 12.651 11.032  1.533   1 51.141  ? 314 HOH   B O    1 ? ? 
HETATM 3847 O O    . HOH   E 3 .   ? 24.363 -17.96  10.801  1 46.647  ? 315 HOH   B O    1 ? ? 
HETATM 3848 O O    . HOH   F 3 .   ? 9.481  -23.596 39.855  1 43.223  ? 301 HOH   A O    1 ? ? 
HETATM 3849 O O    . HOH   F 3 .   ? 15.985 -10.628 21.466  1 29.342  ? 302 HOH   A O    1 ? ? 
HETATM 3850 O O    . HOH   F 3 .   ? 16.987 -20.419 21.024  1 44.393  ? 303 HOH   A O    1 ? ? 
HETATM 3851 O O    . HOH   F 3 .   ? 4.863  -5.735  43.033  1 55.792  ? 304 HOH   A O    1 ? ? 
HETATM 3852 O O    . HOH   F 3 .   ? 10.766 -3.665  19.435  1 29.976  ? 305 HOH   A O    1 ? ? 
HETATM 3853 O O    . HOH   F 3 .   ? 22.456 -8.719  30.381  1 42.285  ? 306 HOH   A O    1 ? ? 
HETATM 3854 O O    . HOH   F 3 .   ? 17.219 -3.127  28.748  1 43.015  ? 307 HOH   A O    1 ? ? 
HETATM 3855 O O    . HOH   F 3 .   ? 10.837 -5.519  21.657  1 33.445  ? 308 HOH   A O    1 ? ? 
HETATM 3856 O O    . HOH   F 3 .   ? 7.704  0.599   14.919  1 44.841  ? 309 HOH   A O    1 ? ? 
HETATM 3857 O O    . HOH   F 3 .   ? 16.907 -3.217  16.817  1 39.525  ? 310 HOH   A O    1 ? ? 
HETATM 3858 O O    . HOH   F 3 .   ? 22.745 -29.676 26.184  1 47.806  ? 311 HOH   A O    1 ? ? 
HETATM 3859 O O    . HOH   F 3 .   ? 10.606 -3.974  12.087  1 34.386  ? 312 HOH   A O    1 ? ? 
HETATM 3860 O O    . HOH   F 3 .   ? 9.275  -15.159 41.972  1 41.498  ? 313 HOH   A O    1 ? ? 
HETATM 3861 O O    . HOH   F 3 .   ? 11.882 -5.39   32.532  1 31.601  ? 314 HOH   A O    1 ? ? 
HETATM 3862 O O    . HOH   F 3 .   ? -3.654 -10.238 18.44   1 50.755  ? 315 HOH   A O    1 ? ? 
HETATM 3863 O O    . HOH   F 3 .   ? 17.093 -5.692  40.41   1 38.905  ? 316 HOH   A O    1 ? ? 
HETATM 3864 O O    . HOH   F 3 .   ? -2.996 -24.515 37.34   1 44.172  ? 317 HOH   A O    1 ? ? 
HETATM 3865 O O    . HOH   F 3 .   ? 4.148  -2.138  23.776  1 35.072  ? 318 HOH   A O    1 ? ? 
HETATM 3866 O O    . HOH   F 3 .   ? 0.978  -13.438 16.728  1 49.551  ? 319 HOH   A O    1 ? ? 
HETATM 3867 O O    . HOH   F 3 .   ? 1.115  -2.191  18.138  1 41.301  ? 320 HOH   A O    1 ? ? 
HETATM 3868 O O    . HOH   F 3 .   ? 17.256 -6.158  18.584  1 51.449  ? 321 HOH   A O    1 ? ? 
HETATM 3869 O O    . HOH   F 3 .   ? 14.181 -13.442 17.473  1 43.428  ? 322 HOH   A 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    . GLY   A 1   ? 1.32046  0.535635 0.650752 -0.0620038  0.0749257   0.231081    13  GLY   B N    
2    C CA   . GLY   A 1   ? 1.27241  0.543284 0.687471 -0.0911976  0.0833312   0.204432    13  GLY   B CA   
3    C C    . GLY   A 1   ? 1.24747  0.574171 0.661515 -0.0928596  0.0795322   0.189704    13  GLY   B C    
4    O O    . GLY   A 1   ? 1.34862  0.671218 0.698204 -0.0734157  0.0674425   0.195958    13  GLY   B O    
5    H H1   . GLY   A 1   ? 1.36001  0.541162 0.693444 -0.0595521  0.0766907   0.239374    13  GLY   B H1   
6    H H2   . GLY   A 1   ? 1.31158  0.549895 0.627849 -0.0450305  0.047094    0.224459    13  GLY   B H2   
7    H H3   . GLY   A 1   ? 1.37984  0.569687 0.667553 -0.0620933  0.0956036   0.246359    13  GLY   B H3   
8    H HA2  . GLY   A 1   ? 1.29148  0.541156 0.727692 -0.110343   0.112313    0.211129    13  GLY   B HA2  
9    H HA3  . GLY   A 1   ? 1.22694  0.51811  0.680308 -0.0900025  0.0626438   0.189159    13  GLY   B HA3  
10   N N    . ALA   A 2   ? 1.17301  0.549434 0.658526 -0.115257   0.0876864   0.169003    14  ALA   B N    
11   C CA   . ALA   A 2   ? 1.17353  0.599    0.665667 -0.117095   0.0871653   0.154605    14  ALA   B CA   
12   C C    . ALA   A 2   ? 1.13701  0.598134 0.615781 -0.0964167  0.0449616   0.1403      14  ALA   B C    
13   O O    . ALA   A 2   ? 1.18131  0.652151 0.62132  -0.0879101  0.0400152   0.13737     14  ALA   B O    
14   C CB   . ALA   A 2   ? 1.13649  0.607993 0.714397 -0.141398   0.099991    0.136994    14  ALA   B CB   
15   H H    . ALA   A 2   ? 1.1694   0.547462 0.700725 -0.129005   0.0925491   0.163346    14  ALA   B H    
16   H HA   . ALA   A 2   ? 1.21716  0.619549 0.664584 -0.115004   0.107697    0.166692    14  ALA   B HA   
17   H HB1  . ALA   A 2   ? 1.15755  0.610262 0.750291 -0.155626   0.127976    0.146142    14  ALA   B HB1  
18   H HB2  . ALA   A 2   ? 1.09188  0.580479 0.706196 -0.142835   0.0804655   0.125432    14  ALA   B HB2  
19   H HB3  . ALA   A 2   ? 1.09937  0.601286 0.681774 -0.140464   0.099702    0.128092    14  ALA   B HB3  
20   N N    . PRO   A 3   ? 1.07483  0.556707 0.587806 -0.0882103  0.0153273   0.129496    15  PRO   B N    
21   C CA   . PRO   A 3   ? 1.03238  0.551142 0.543921 -0.0699753  -0.0189815  0.118355    15  PRO   B CA   
22   C C    . PRO   A 3   ? 1.10883  0.601899 0.553247 -0.0472111  -0.037903   0.131645    15  PRO   B C    
23   O O    . PRO   A 3   ? 1.14911  0.673278 0.588216 -0.0378826  -0.0616224  0.121628    15  PRO   B O    
24   C CB   . PRO   A 3   ? 0.960771 0.494412 0.515316 -0.0629117  -0.0374941  0.109294    15  PRO   B CB   
25   C CG   . PRO   A 3   ? 0.957791 0.456185 0.53104  -0.078109   -0.0177513  0.11262     15  PRO   B CG   
26   C CD   . PRO   A 3   ? 1.03292  0.501547 0.587799 -0.0960861  0.0156928   0.126282    15  PRO   B CD   
27   H HA   . PRO   A 3   ? 0.994083 0.545172 0.52451  -0.0763491  -0.0182992  0.107056    15  PRO   B HA   
28   H HB2  . PRO   A 3   ? 0.9813   0.506119 0.517341 -0.0456463  -0.0538865  0.114961    15  PRO   B HB2  
29   H HB3  . PRO   A 3   ? 0.912438 0.484376 0.500873 -0.0657031  -0.0442946  0.0956654   15  PRO   B HB3  
30   H HG2  . PRO   A 3   ? 1.00144  0.470462 0.5599   -0.0672559  -0.0239227  0.119836    15  PRO   B HG2  
31   H HG3  . PRO   A 3   ? 0.931519 0.454366 0.545272 -0.0866014  -0.0199272  0.0984575   15  PRO   B HG3  
32   H HD2  . PRO   A 3   ? 1.08565  0.510261 0.61518  -0.0938942  0.0249231   0.141016    15  PRO   B HD2  
33   H HD3  . PRO   A 3   ? 1.00985  0.494466 0.60529  -0.113426   0.0277102   0.117786    15  PRO   B HD3  
34   N N    . ALA   A 4   ? 1.14962  0.584593 0.544964 -0.0378103  -0.0297316  0.154154    16  ALA   B N    
35   C CA   . ALA   A 4   ? 1.21572  0.61974  0.536115 -0.0132379  -0.0490478  0.169798    16  ALA   B CA   
36   C C    . ALA   A 4   ? 1.23026  0.632806 0.498041 -0.0162677  -0.0416302  0.166746    16  ALA   B C    
37   O O    . ALA   A 4   ? 1.2617   0.683684 0.50406  -0.00241721 -0.0739462  0.157267    16  ALA   B O    
38   C CB   . ALA   A 4   ? 1.27018  0.602769 0.541409 -0.00330811 -0.0333841  0.198582    16  ALA   B CB   
39   H H    . ALA   A 4   ? 1.16731  0.579898 0.575663 -0.0462784  -0.0130993  0.160036    16  ALA   B H    
40   H HA   . ALA   A 4   ? 1.1854   0.615222 0.521407 0.00059294  -0.0784097  0.162989    16  ALA   B HA   
41   H HB1  . ALA   A 4   ? 1.2643   0.594641 0.567253 9.213e-05   -0.0394371  0.198385    16  ALA   B HB1  
42   H HB2  . ALA   A 4   ? 1.30299  0.611248 0.565868 -0.0184297  -0.00176549 0.206116    16  ALA   B HB2  
43   H HB3  . ALA   A 4   ? 1.33358  0.64448  0.549596 0.0156797   -0.0482957  0.21021     16  ALA   B HB3  
44   N N    . THR   A 5   ? 1.26655  0.642913 0.519822 -0.034201   0.00233614  0.174385    17  THR   B N    
45   C CA   . THR   A 5   ? 1.28628  0.656196 0.492057 -0.0385363  0.0222093   0.170372    17  THR   B CA   
46   C C    . THR   A 5   ? 1.20995  0.639301 0.453174 -0.0426019  -0.00140983 0.140414    17  THR   B C    
47   O O    . THR   A 5   ? 1.19404  0.615273 0.379655 -0.0341609  -0.0107951  0.132326    17  THR   B O    
48   C CB   . THR   A 5   ? 1.31823  0.67067  0.547823 -0.0616702  0.0776785   0.179944    17  THR   B CB   
49   O OG1  . THR   A 5   ? 1.3893   0.678682 0.577263 -0.0560567  0.096679    0.209788    17  THR   B OG1  
50   C CG2  . THR   A 5   ? 1.34755  0.693845 0.538375 -0.0664294  0.110035    0.175947    17  THR   B CG2  
51   H H    . THR   A 5   ? 1.26132  0.622434 0.538112 -0.044193   0.0223881   0.181981    17  THR   B H    
52   H HA   . THR   A 5   ? 1.36348  0.697339 0.497026 -0.0227877  0.0164135   0.182222    17  THR   B HA   
53   H HB   . THR   A 5   ? 1.24661  0.632755 0.547954 -0.076064   0.0792006   0.169009    17  THR   B HB   
55   H HG21 . THR   A 5   ? 1.35969  0.69493  0.570732 -0.0799391  0.147392    0.185026    17  THR   B HG21 
56   H HG22 . THR   A 5   ? 1.41878  0.730336 0.531486 -0.0508262  0.10625     0.184414    17  THR   B HG22 
57   H HG23 . THR   A 5   ? 1.29566  0.682143 0.519504 -0.0706341  0.0979628   0.155782    17  THR   B HG23 
58   N N    . VAL   A 6   ? 1.07837  0.561603 0.412406 -0.054543   -0.0107386  0.123901    18  VAL   B N    
59   C CA   . VAL   A 6   ? 1.00109  0.535983 0.374601 -0.0580094  -0.0303505  0.0994066   18  VAL   B CA   
60   C C    . VAL   A 6   ? 1.01965  0.569232 0.378633 -0.0399516  -0.0772488  0.092451    18  VAL   B C    
61   O O    . VAL   A 6   ? 0.988008 0.552527 0.334329 -0.0393116  -0.0937792  0.0757869   18  VAL   B O    
62   C CB   . VAL   A 6   ? 0.894175 0.478731 0.35859  -0.0719477  -0.0269172  0.086433    18  VAL   B CB   
63   C CG1  . VAL   A 6   ? 0.802672 0.429814 0.298063 -0.0745549  -0.0409865  0.0655732   18  VAL   B CG1  
64   C CG2  . VAL   A 6   ? 0.912959 0.492615 0.407997 -0.0902942  0.0119218   0.0906916   18  VAL   B CG2  
65   H H    . VAL   A 6   ? 1.06257  0.54664  0.43132  -0.0601802  -0.00396784 0.128368    18  VAL   B H    
66   H HA   . VAL   A 6   ? 1.02432  0.551894 0.372999 -0.0621349  -0.0156138  0.0946108   18  VAL   B HA   
67   H HB   . VAL   A 6   ? 0.875657 0.466756 0.360693 -0.0660845  -0.0418972  0.0890793   18  VAL   B HB   
68   H HG11 . VAL   A 6   ? 0.843135 0.458416 0.308801 -0.0768416  -0.0303625  0.0615456   18  VAL   B HG11 
69   H HG12 . VAL   A 6   ? 0.812105 0.450487 0.308191 -0.0654972  -0.0669612  0.061999    18  VAL   B HG12 
70   H HG13 . VAL   A 6   ? 0.766413 0.419543 0.311137 -0.08241    -0.0340072  0.0600039   18  VAL   B HG13 
71   H HG21 . VAL   A 6   ? 0.850909 0.46268  0.39823  -0.0969447  0.00956918  0.081163    18  VAL   B HG21 
72   H HG22 . VAL   A 6   ? 0.932226 0.485789 0.41811  -0.090916   0.0200772   0.10303     18  VAL   B HG22 
73   H HG23 . VAL   A 6   ? 0.92919  0.499189 0.402254 -0.0941427  0.0309638   0.0904769   18  VAL   B HG23 
74   N N    . THR   A 7   ? 1.0305   0.578502 0.401019 -0.0259346  -0.0988457  0.103088    19  THR   B N    
75   C CA   . THR   A 7   ? 1.06467  0.629923 0.431241 -0.00643628 -0.143785   0.0994556   19  THR   B CA   
76   C C    . THR   A 7   ? 1.19592  0.722239 0.469347 0.0074599   -0.160944   0.103753    19  THR   B C    
77   O O    . THR   A 7   ? 1.25683  0.805698 0.52847  0.016619    -0.200591   0.0902803   19  THR   B O    
78   C CB   . THR   A 7   ? 1.07515  0.640383 0.470625 0.00931993  -0.156426   0.112643    19  THR   B CB   
79   O OG1  . THR   A 7   ? 0.982099 0.59855  0.462112 0.00349024  -0.158346   0.0996786   19  THR   B OG1  
80   C CG2  . THR   A 7   ? 1.10899  0.669742 0.476806 0.0369714   -0.198366   0.120676    19  THR   B CG2  
81   H H    . THR   A 7   ? 1.02716  0.563799 0.412374 -0.0283788  -0.0854303  0.112047    19  THR   B H    
82   H HA   . THR   A 7   ? 1.02322  0.626983 0.432678 -0.0123823  -0.154395   0.0838876   19  THR   B HA   
83   H HB   . THR   A 7   ? 1.08931  0.620813 0.466311 0.00735907  -0.135152   0.125547    19  THR   B HB   
85   H HG21 . THR   A 7   ? 1.09925  0.666766 0.49818  0.047038    -0.203748   0.126624    19  THR   B HG21 
86   H HG22 . THR   A 7   ? 1.10021  0.692279 0.484969 0.0372127   -0.220916   0.107178    19  THR   B HG22 
87   H HG23 . THR   A 7   ? 1.18133  0.700312 0.484246 0.0453317   -0.197385   0.133432    19  THR   B HG23 
88   N N    . GLU   A 8   ? 1.28867  0.757532 0.486204 0.00771047  -0.130037   0.120457    20  GLU   B N    
89   C CA   . GLU   A 8   ? 1.46329  0.882981 0.552713 0.026731    -0.144343   0.129037    20  GLU   B CA   
90   C C    . GLU   A 8   ? 1.50342  0.918481 0.551672 0.0169548   -0.133315   0.10859     20  GLU   B C    
91   O O    . GLU   A 8   ? 1.53716  0.947926 0.534569 0.0291581   -0.17061    0.094093    20  GLU   B O    
92   C CB   . GLU   A 8   ? 1.49309  0.84298  0.510344 0.0375239   -0.114418   0.163039    20  GLU   B CB   
93   H H    . GLU   A 8   ? 1.28077  0.739611 0.493073 -0.0035613  -0.0989388  0.127238    20  GLU   B H    
94   H HA   . GLU   A 8   ? 1.4526   0.885824 0.540907 0.0415134   -0.183844   0.125667    20  GLU   B HA   
97   N N    . GLN   A 9   ? 1.49389  0.908915 0.56518  -0.00380287 -0.0839292  0.105767    21  GLN   B N    
98   C CA   . GLN   A 9   ? 1.51454  0.911946 0.535623 -0.00905807 -0.0625366  0.090359    21  GLN   B CA   
99   C C    . GLN   A 9   ? 1.35188  0.8037   0.459084 -0.0288155  -0.0590353  0.0626336   21  GLN   B C    
100  O O    . GLN   A 9   ? 1.31179  0.75465  0.389033 -0.032063   -0.0486191  0.0436351   21  GLN   B O    
101  C CB   . GLN   A 9   ? 1.62419  0.968152 0.589429 -0.0113306  -0.00261433 0.113785    21  GLN   B CB   
102  H H    . GLN   A 9   ? 1.43736  0.863135 0.557528 -0.013911   -0.0634248  0.112977    21  GLN   B H    
103  H HA   . GLN   A 9   ? 1.57218  0.951643 0.532252 0.00443137  -0.0901216  0.0833948   21  GLN   B HA   
106  N N    . GLY   A 10  ? 1.21859  0.722498 0.427701 -0.0396268  -0.0675961  0.0599496   22  GLY   B N    
107  C CA   . GLY   A 10  ? 1.13167  0.68056  0.421247 -0.0569589  -0.0547562  0.0417767   22  GLY   B CA   
108  C C    . GLY   A 10  ? 1.09768  0.668744 0.39804  -0.057885   -0.0865527  0.0144068   22  GLY   B C    
109  O O    . GLY   A 10  ? 1.07222  0.651234 0.364231 -0.0486287  -0.130529   0.00794992  22  GLY   B O    
110  H H    . GLY   A 10  ? 1.21463  0.723861 0.440104 -0.0341539  -0.0817195  0.0701282   22  GLY   B H    
111  H HA2  . GLY   A 10  ? 1.13673  0.673036 0.418298 -0.0634584  -0.021257   0.0435168   22  GLY   B HA2  
112  H HA3  . GLY   A 10  ? 1.06781  0.644122 0.416344 -0.0616296  -0.056516   0.0461114   22  GLY   B HA3  
113  N N    . GLU   A 11  ? 1.09861  0.68117  0.427426 -0.0695531  -0.0637765  -0.00135542 23  GLU   B N    
114  C CA   . GLU   A 11  ? 1.11683  0.713432 0.462202 -0.0741363  -0.0859292  -0.0284796  23  GLU   B CA   
115  C C    . GLU   A 11  ? 1.007    0.658666 0.452898 -0.0822371  -0.104787   -0.0318705  23  GLU   B C    
116  O O    . GLU   A 11  ? 0.88379  0.561995 0.389876 -0.0880278  -0.082741   -0.0208735  23  GLU   B O    
117  C CB   . GLU   A 11  ? 1.18455  0.763618 0.518011 -0.0802254  -0.0464351  -0.0403191  23  GLU   B CB   
118  C CG   . GLU   A 11  ? 1.3181   0.897971 0.660078 -0.0852925  -0.0648808  -0.0706703  23  GLU   B CG   
119  C CD   . GLU   A 11  ? 1.39462  0.962849 0.745606 -0.0898827  -0.0262723  -0.0837607  23  GLU   B CD   
120  O OE1  . GLU   A 11  ? 1.38206  0.939629 0.723094 -0.0874241  0.0182045   -0.070112   23  GLU   B OE1  
121  O OE2  . GLU   A 11  ? 1.38401  0.95468  0.759797 -0.0960748  -0.0405334  -0.107656   23  GLU   B OE2  
122  H H    . GLU   A 11  ? 1.08389  0.664832 0.425982 -0.0749689  -0.0326177  0.00519831  23  GLU   B H    
123  H HA   . GLU   A 11  ? 1.16989  0.748303 0.46685  -0.066684   -0.112673   -0.0363025  23  GLU   B HA   
124  H HB2  . GLU   A 11  ? 1.258    0.801512 0.527041 -0.0738317  -0.0291237  -0.0355679  23  GLU   B HB2  
125  H HB3  . GLU   A 11  ? 1.14403  0.744375 0.529113 -0.0864329  -0.0236651  -0.0323815  23  GLU   B HB3  
126  H HG2  . GLU   A 11  ? 1.25057  0.86305  0.652076 -0.0909849  -0.0848039  -0.0733658  23  GLU   B HG2  
127  H HG3  . GLU   A 11  ? 1.36586  0.920044 0.648929 -0.0790849  -0.0869142  -0.081162   23  GLU   B HG3  
128  N N    . ASP   A 12  ? 0.969206 0.637165 0.432906 -0.0823269  -0.145537   -0.0478229  24  ASP   B N    
129  C CA   . ASP   A 12  ? 0.885216 0.602407 0.444014 -0.0902371  -0.158202   -0.0511099  24  ASP   B CA   
130  C C    . ASP   A 12  ? 0.870639 0.592534 0.466831 -0.103276   -0.138745   -0.0670081  24  ASP   B C    
131  O O    . ASP   A 12  ? 0.930332 0.631169 0.501098 -0.108096   -0.150983   -0.0901849  24  ASP   B O    
132  C CB   . ASP   A 12  ? 0.879658 0.617526 0.459011 -0.0865437  -0.206508   -0.0599434  24  ASP   B CB   
133  C CG   . ASP   A 12  ? 0.797323 0.585768 0.479776 -0.0952341  -0.213612   -0.0618906  24  ASP   B CG   
134  O OD1  . ASP   A 12  ? 0.770528 0.572786 0.49758  -0.102312   -0.181691   -0.055594   24  ASP   B OD1  
135  O OD2  . ASP   A 12  ? 0.812749 0.626617 0.531157 -0.0937657  -0.250758   -0.0688431  24  ASP   B OD2  
136  H H    . ASP   A 12  ? 1.03271  0.680157 0.448436 -0.0771791  -0.165605   -0.0567107  24  ASP   B H    
137  H HA   . ASP   A 12  ? 0.843123 0.576662 0.43163  -0.0884313  -0.145888   -0.035857   24  ASP   B HA   
138  H HB2  . ASP   A 12  ? 0.895072 0.629913 0.452975 -0.0755398  -0.217691   -0.047549   24  ASP   B HB2  
139  H HB3  . ASP   A 12  ? 0.930321 0.649677 0.475059 -0.0880388  -0.22373    -0.0769131  24  ASP   B HB3  
140  N N    . ILE   A 13  ? 0.779667 0.525331 0.432343 -0.107095   -0.110258   -0.0548563  25  ILE   B N    
141  C CA   . ILE   A 13  ? 0.777624 0.523179 0.461684 -0.114906   -0.0860501  -0.0637768  25  ILE   B CA   
142  C C    . ILE   A 13  ? 0.713918 0.494661 0.478895 -0.121083   -0.0927146  -0.0627035  25  ILE   B C    
143  O O    . ILE   A 13  ? 0.703017 0.486628 0.503385 -0.125005   -0.071615   -0.063397   25  ILE   B O    
144  C CB   . ILE   A 13  ? 0.757774 0.49998  0.439361 -0.111853   -0.0478847  -0.0501479  25  ILE   B CB   
145  C CG1  . ILE   A 13  ? 0.691794 0.466272 0.41904  -0.108822   -0.0434869  -0.0301346  25  ILE   B CG1  
146  C CG2  . ILE   A 13  ? 0.84993  0.556255 0.457151 -0.106962   -0.0339505  -0.0481175  25  ILE   B CG2  
147  C CD1  . ILE   A 13  ? 0.698611 0.475861 0.436116 -0.107748   -0.0134348  -0.0201488  25  ILE   B CD1  
148  H H    . ILE   A 13  ? 0.759932 0.520321 0.42981  -0.10328    -0.107092   -0.0407973  25  ILE   B H    
149  H HA   . ILE   A 13  ? 0.815656 0.537896 0.469371 -0.117349   -0.08984    -0.07981    25  ILE   B HA   
150  H HB   . ILE   A 13  ? 0.757504 0.497784 0.457346 -0.114508   -0.0334047  -0.05654    25  ILE   B HB   
151  H HG12 . ILE   A 13  ? 0.704618 0.478768 0.415482 -0.105327   -0.0565227  -0.0239005  25  ILE   B HG12 
152  H HG13 . ILE   A 13  ? 0.669352 0.463404 0.43802  -0.11019    -0.0486064  -0.0299706  25  ILE   B HG13 
153  H HG21 . ILE   A 13  ? 0.830398 0.535835 0.445264 -0.107061   -0.00772152 -0.0430731  25  ILE   B HG21 
154  H HG22 . ILE   A 13  ? 0.842188 0.548718 0.433797 -0.103372   -0.0434966  -0.0376838  25  ILE   B HG22 
155  H HG23 . ILE   A 13  ? 0.887525 0.569825 0.454857 -0.106527   -0.0407861  -0.0619795  25  ILE   B HG23 
156  H HD11 . ILE   A 13  ? 0.690781 0.466005 0.440703 -0.108903   3.681e-05   -0.0260783  25  ILE   B HD11 
157  H HD12 . ILE   A 13  ? 0.655432 0.452834 0.422897 -0.105827   -0.0150177  -0.0109613  25  ILE   B HD12 
158  H HD13 . ILE   A 13  ? 0.716467 0.476867 0.41989  -0.107175   -0.0057951  -0.0169971  25  ILE   B HD13 
159  N N    . THR   A 14  ? 0.710099 0.516781 0.506282 -0.120093   -0.119104   -0.0587998  26  THR   B N    
160  C CA   . THR   A 14  ? 0.686725 0.524211 0.56099  -0.126966   -0.12177    -0.0580546  26  THR   B CA   
161  C C    . THR   A 14  ? 0.739136 0.563967 0.629896 -0.141328   -0.137663   -0.0831374  26  THR   B C    
162  O O    . THR   A 14  ? 0.810273 0.606339 0.647437 -0.143656   -0.158628   -0.104004   26  THR   B O    
163  C CB   . THR   A 14  ? 0.638559 0.51093  0.550017 -0.11983    -0.139371   -0.0453255  26  THR   B CB   
164  O OG1  . THR   A 14  ? 0.689204 0.55865  0.578142 -0.118954   -0.177706   -0.0580778  26  THR   B OG1  
165  C CG2  . THR   A 14  ? 0.637663 0.51331  0.527973 -0.106077   -0.12395    -0.024733   26  THR   B CG2  
166  H H    . THR   A 14  ? 0.725645 0.530508 0.496414 -0.11432    -0.133865   -0.0554746  26  THR   B H    
167  H HA   . THR   A 14  ? 0.655188 0.497152 0.549387 -0.126084   -0.0986156  -0.0489023  26  THR   B HA   
168  H HB   . THR   A 14  ? 0.626205 0.51929  0.592234 -0.124096   -0.13462    -0.0425545  26  THR   B HB   
170  H HG21 . THR   A 14  ? 0.615934 0.511597 0.531101 -0.0999385  -0.132281   -0.0173764  26  THR   B HG21 
171  H HG22 . THR   A 14  ? 0.653755 0.508916 0.495381 -0.102842   -0.127345   -0.025644   26  THR   B HG22 
172  H HG23 . THR   A 14  ? 0.60677  0.483374 0.50779  -0.106111   -0.102253   -0.0183042  26  THR   B HG23 
173  N N    . SER   A 15  ? 0.710178 0.552648 0.673691 -0.150718   -0.12686    -0.0811631  27  SER   B N    
174  C CA   . SER   A 15  ? 0.714032 0.544322 0.711043 -0.168068   -0.139699   -0.104853   27  SER   B CA   
175  C C    . SER   A 15  ? 0.714544 0.571215 0.75026  -0.17596    -0.182178   -0.11737    27  SER   B C    
176  O O    . SER   A 15  ? 0.725914 0.563607 0.743458 -0.185951   -0.214632   -0.146205   27  SER   B O    
177  C CB   . SER   A 15  ? 0.694955 0.529255 0.756568 -0.174906   -0.108052   -0.0940548  27  SER   B CB   
178  O OG   . SER   A 15  ? 0.677201 0.485133 0.702036 -0.165957   -0.0756932  -0.0867815  27  SER   B OG   
179  H H    . SER   A 15  ? 0.667782 0.527712 0.659909 -0.146233   -0.110386   -0.064546   27  SER   B H    
180  H HA   . SER   A 15  ? 0.756778 0.555359 0.706124 -0.169266   -0.141624   -0.120664   27  SER   B HA   
181  H HB2  . SER   A 15  ? 0.655778 0.517862 0.755092 -0.170976   -0.100525   -0.0761508  27  SER   B HB2  
182  H HB3  . SER   A 15  ? 0.713166 0.539322 0.805319 -0.188386   -0.11686    -0.109462   27  SER   B HB3  
184  N N    . LYS   A 16  ? 0.703006 0.603462 0.789174 -0.168918   -0.18351    -0.0965268  28  LYS   B N    
185  C CA   . LYS   A 16  ? 0.725494 0.662059 0.863894 -0.172581   -0.222276   -0.104015   28  LYS   B CA   
186  C C    . LYS   A 16  ? 0.733317 0.65947  0.798226 -0.159655   -0.26204    -0.113167   28  LYS   B C    
187  O O    . LYS   A 16  ? 0.671193 0.625145 0.769571 -0.159194   -0.303016   -0.121791   28  LYS   B O    
188  C CB   . LYS   A 16  ? 0.702028 0.685195 0.912071 -0.163999   -0.202815   -0.076506   28  LYS   B CB   
189  C CG   . LYS   A 16  ? 0.738661 0.729369 1.01818  -0.174768   -0.163225   -0.0644172  28  LYS   B CG   
190  C CD   . LYS   A 16  ? 0.787018 0.816638 1.12316  -0.162484   -0.135949   -0.0355705  28  LYS   B CD   
191  C CE   . LYS   A 16  ? 0.807173 0.819892 1.13184  -0.155676   -0.0872817  -0.0133301  28  LYS   B CE   
192  N NZ   . LYS   A 16  ? 0.809702 0.854747 1.20392  -0.149696   -0.0573496  0.0103677   28  LYS   B NZ   
193  H H    . LYS   A 16  ? 0.667019 0.575347 0.755837 -0.160393   -0.159834   -0.0776414  28  LYS   B H    
194  H HA   . LYS   A 16  ? 0.741566 0.677728 0.919034 -0.188325   -0.234623   -0.121075   28  LYS   B HA   
195  H HB2  . LYS   A 16  ? 0.69118  0.670683 0.861638 -0.149164   -0.190339   -0.0617243  28  LYS   B HB2  
196  H HB3  . LYS   A 16  ? 0.712865 0.723938 0.962568 -0.164301   -0.22791    -0.0803771  28  LYS   B HB3  
197  H HG2  . LYS   A 16  ? 0.760127 0.753854 1.08575  -0.191259   -0.17493    -0.0789597  28  LYS   B HG2  
198  H HG3  . LYS   A 16  ? 0.739738 0.702705 0.980472 -0.1732     -0.141862   -0.0613933  28  LYS   B HG3  
199  H HD2  . LYS   A 16  ? 0.765764 0.804964 1.07497  -0.147895   -0.145506   -0.0294006  28  LYS   B HD2  
200  H HD3  . LYS   A 16  ? 0.775862 0.831985 1.18391  -0.172023   -0.141067   -0.0374627  28  LYS   B HD3  
201  H HE2  . LYS   A 16  ? 0.813661 0.804518 1.13995  -0.166898   -0.0792919  -0.0203196  28  LYS   B HE2  
202  H HE3  . LYS   A 16  ? 0.793728 0.793412 1.06087  -0.142583   -0.0824858  -0.0072037  28  LYS   B HE3  
203  H HZ1  . LYS   A 16  ? 0.810152 0.866546 1.26387  -0.163599   -0.0570779  0.00634795  28  LYS   B HZ1  
204  H HZ2  . LYS   A 16  ? 0.793122 0.858737 1.19038  -0.138847   -0.0648068  0.0152836   28  LYS   B HZ2  
205  H HZ3  . LYS   A 16  ? 0.79526  0.827279 1.1704   -0.142084   -0.0304502  0.0245227   28  LYS   B HZ3  
206  N N    . LYS   A 17  ? 0.760236 0.648182 0.729756 -0.147493   -0.247842   -0.107979   29  LYS   B N    
207  C CA   . LYS   A 17  ? 0.825495 0.693024 0.71197  -0.132621   -0.276511   -0.110507   29  LYS   B CA   
208  C C    . LYS   A 17  ? 0.759496 0.665368 0.679112 -0.117288   -0.295292   -0.0918741  29  LYS   B C    
209  O O    . LYS   A 17  ? 0.760705 0.67525  0.672377 -0.11039    -0.340477   -0.100976   29  LYS   B O    
210  C CB   . LYS   A 17  ? 0.90844  0.749243 0.75124  -0.139346   -0.319507   -0.143421   29  LYS   B CB   
211  C CG   . LYS   A 17  ? 0.958006 0.744707 0.733297 -0.146537   -0.298764   -0.162493   29  LYS   B CG   
212  C CD   . LYS   A 17  ? 0.978732 0.726969 0.656618 -0.130541   -0.267956   -0.146841   29  LYS   B CD   
213  C CE   . LYS   A 17  ? 1.04858  0.748288 0.668959 -0.134269   -0.238494   -0.16224    29  LYS   B CE   
214  N NZ   . LYS   A 17  ? 1.01915  0.729609 0.689595 -0.139108   -0.189947   -0.146964   29  LYS   B NZ   
215  H H    . LYS   A 17  ? 0.74318  0.617346 0.700655 -0.147797   -0.218159   -0.101045   29  LYS   B H    
216  H HA   . LYS   A 17  ? 0.816089 0.658352 0.648355 -0.126074   -0.25373    -0.101987   29  LYS   B HA   
217  H HB2  . LYS   A 17  ? 0.905689 0.770992 0.812107 -0.150391   -0.34012    -0.155281   29  LYS   B HB2  
218  H HB3  . LYS   A 17  ? 0.943456 0.776515 0.737749 -0.12666    -0.342954   -0.141703   29  LYS   B HB3  
219  H HG2  . LYS   A 17  ? 0.92402  0.716175 0.746306 -0.157105   -0.274599   -0.162211   29  LYS   B HG2  
220  H HG3  . LYS   A 17  ? 1.01364  0.783495 0.764527 -0.150975   -0.328837   -0.186237   29  LYS   B HG3  
221  H HD2  . LYS   A 17  ? 1.02651  0.763522 0.652528 -0.119605   -0.290519   -0.146108   29  LYS   B HD2  
222  H HD3  . LYS   A 17  ? 0.932428 0.698835 0.63675  -0.126646   -0.2438     -0.125191   29  LYS   B HD3  
223  H HE2  . LYS   A 17  ? 1.08766  0.774173 0.708554 -0.142887   -0.257104   -0.18635    29  LYS   B HE2  
224  H HE3  . LYS   A 17  ? 1.09065  0.762009 0.637317 -0.123507   -0.232871   -0.158927   29  LYS   B HE3  
225  H HZ1  . LYS   A 17  ? 0.973138 0.707183 0.707673 -0.147609   -0.192447   -0.147045   29  LYS   B HZ1  
226  H HZ2  . LYS   A 17  ? 0.977524 0.697522 0.643699 -0.131638   -0.174296   -0.127342   29  LYS   B HZ2  
227  H HZ3  . LYS   A 17  ? 1.03313  0.716002 0.674761 -0.14019    -0.17299    -0.156962   29  LYS   B HZ3  
228  N N    . ASP   A 18  ? 0.668758 0.594849 0.622035 -0.109715   -0.261594   -0.0668889  30  ASP   B N    
229  C CA   . ASP   A 18  ? 0.634705 0.594321 0.624086 -0.0931256  -0.271078   -0.0491686  30  ASP   B CA   
230  C C    . ASP   A 18  ? 0.648066 0.579456 0.564916 -0.0750147  -0.25648    -0.0304888  30  ASP   B C    
231  O O    . ASP   A 18  ? 0.721146 0.670195 0.65871  -0.0589088  -0.255268   -0.0140715  30  ASP   B O    
232  C CB   . ASP   A 18  ? 0.586929 0.587929 0.671674 -0.0973253  -0.244174   -0.037705   30  ASP   B CB   
233  C CG   . ASP   A 18  ? 0.538183 0.524105 0.609444 -0.0977433  -0.195915   -0.0234766  30  ASP   B CG   
234  O OD1  . ASP   A 18  ? 0.529312 0.480307 0.527854 -0.0933108  -0.183466   -0.0201603  30  ASP   B OD1  
235  O OD2  . ASP   A 18  ? 0.506133 0.515691 0.641105 -0.101723   -0.171406   -0.0150136  30  ASP   B OD2  
236  H H    . ASP   A 18  ? 0.649845 0.566836 0.601394 -0.113682   -0.232344   -0.0616212  30  ASP   B H    
237  H HA   . ASP   A 18  ? 0.668532 0.640741 0.669027 -0.090351   -0.305261   -0.0574272  30  ASP   B HA   
238  H HB2  . ASP   A 18  ? 0.573019 0.597537 0.685574 -0.085107   -0.250421   -0.027693   30  ASP   B HB2  
239  H HB3  . ASP   A 18  ? 0.585029 0.60061  0.717904 -0.110941   -0.252233   -0.0492439  30  ASP   B HB3  
240  N N    . ARG   A 19  ? 0.66564  0.551819 0.502505 -0.0777395  -0.241701   -0.0327941  31  ARG   B N    
241  C CA   . ARG   A 19  ? 0.680659 0.535874 0.453422 -0.0651026  -0.225627   -0.0158107  31  ARG   B CA   
242  C C    . ARG   A 19  ? 0.677615 0.547717 0.4866   -0.0610195  -0.19386    0.00099563  31  ARG   B C    
243  O O    . ARG   A 19  ? 0.691221 0.544469 0.470419 -0.0490594  -0.187343   0.01508     31  ARG   B O    
244  C CB   . ARG   A 19  ? 0.725913 0.569192 0.45712  -0.0463311  -0.258679   -0.00858446 31  ARG   B CB   
245  C CG   . ARG   A 19  ? 0.791291 0.610558 0.462694 -0.044935   -0.294988   -0.0244597  31  ARG   B CG   
246  C CD   . ARG   A 19  ? 0.872527 0.665642 0.476952 -0.0216934  -0.324281   -0.0122598  31  ARG   B CD   
247  N NE   . ARG   A 19  ? 0.885898 0.646198 0.446171 -0.0100529  -0.29536    0.0129594   31  ARG   B NE   
248  C CZ   . ARG   A 19  ? 0.951636 0.65606  0.420269 -0.00653348 -0.275937   0.0230753   31  ARG   B CZ   
249  N NH1  . ARG   A 19  ? 1.01551  0.689057 0.420404 -0.0135439  -0.273605   0.00952037  31  ARG   B NH1  
250  N NH2  . ARG   A 19  ? 0.978663 0.654729 0.420978 0.00300526  -0.253622   0.0464854   31  ARG   B NH2  
251  H H    . ARG   A 19  ? 0.682788 0.556063 0.507536 -0.0882192  -0.239784   -0.0454783  31  ARG   B H    
252  H HA   . ARG   A 19  ? 0.708274 0.535162 0.435283 -0.0706224  -0.212813   -0.0200273  31  ARG   B HA   
253  H HB2  . ARG   A 19  ? 0.707508 0.580889 0.488201 -0.0392703  -0.271402   -0.00457667 31  ARG   B HB2  
254  H HB3  . ARG   A 19  ? 0.734522 0.553916 0.42731  -0.0394431  -0.243686   0.00411214  31  ARG   B HB3  
255  H HG2  . ARG   A 19  ? 0.81459  0.606353 0.443446 -0.0529409  -0.278939   -0.0310997  31  ARG   B HG2  
256  H HG3  . ARG   A 19  ? 0.791506 0.637094 0.508155 -0.0512474  -0.316445   -0.0380746  31  ARG   B HG3  
257  H HD2  . ARG   A 19  ? 0.928131 0.694856 0.474827 -0.0212564  -0.33951    -0.0223007  31  ARG   B HD2  
258  H HD3  . ARG   A 19  ? 0.866109 0.689538 0.514779 -0.0136893  -0.350959   -0.0121656  31  ARG   B HD3  
259  H HE   . ARG   A 19  ? 0.852311 0.629779 0.451567 -0.00537859 -0.28852    0.0223073   31  ARG   B HE   
260  H HH11 . ARG   A 19  ? 0.989795 0.676093 0.417939 -0.026152   -0.268996   -0.00548271 31  ARG   B HH11 
261  H HH12 . ARG   A 19  ? 1.07178  0.709081 0.408082 -0.00460094 -0.27503    0.0157994   31  ARG   B HH12 
262  H HH21 . ARG   A 19  ? 0.943277 0.635587 0.424209 0.00865503  -0.25381    0.0541664   31  ARG   B HH21 
263  H HH22 . ARG   A 19  ? 1.01159  0.650972 0.398586 0.00349408  -0.237419   0.0540318   31  ARG   B HH22 
264  N N    . GLY   A 20  ? 0.614268 0.509528 0.480945 -0.0702307  -0.173654   -0.00074366 32  GLY   B N    
265  C CA   . GLY   A 20  ? 0.593941 0.498789 0.482881 -0.0645811  -0.145553   0.0126007   32  GLY   B CA   
266  C C    . GLY   A 20  ? 0.576651 0.453164 0.422049 -0.0689524  -0.121832   0.0154001   32  GLY   B C    
267  O O    . GLY   A 20  ? 0.563763 0.439274 0.409823 -0.0627052  -0.106582   0.0243213   32  GLY   B O    
268  H H    . GLY   A 20  ? 0.621636 0.524987 0.510644 -0.0796822  -0.177756   -0.0107062  32  GLY   B H    
269  H HA2  . GLY   A 20  ? 0.586862 0.496792 0.479137 -0.0527924  -0.151022   0.0203344   32  GLY   B HA2  
270  H HA3  . GLY   A 20  ? 0.561815 0.487115 0.494245 -0.0685331  -0.136636   0.012121    32  GLY   B HA3  
271  N N    . VAL   A 21  ? 0.616726 0.470247 0.426034 -0.0791575  -0.119431   0.0060764   33  VAL   B N    
272  C CA   . VAL   A 21  ? 0.583109 0.414425 0.36151  -0.0840832  -0.0956394  0.00816935  33  VAL   B CA   
273  C C    . VAL   A 21  ? 0.635626 0.432061 0.351737 -0.0867403  -0.0987709  0.00259602  33  VAL   B C    
274  O O    . VAL   A 21  ? 0.616403 0.404877 0.320705 -0.0926815  -0.103737   -0.0115115  33  VAL   B O    
275  C CB   . VAL   A 21  ? 0.56096  0.403174 0.370982 -0.0915894  -0.0747047  0.00406645  33  VAL   B CB   
276  C CG1  . VAL   A 21  ? 0.555197 0.382633 0.345891 -0.0946152  -0.0522646  0.00710569  33  VAL   B CG1  
277  C CG2  . VAL   A 21  ? 0.57072  0.441884 0.431659 -0.0862055  -0.0697082  0.0115962   33  VAL   B CG2  
278  H H    . VAL   A 21  ? 0.624393 0.476551 0.430388 -0.0829294  -0.132948   -0.00285985 33  VAL   B H    
279  H HA   . VAL   A 21  ? 0.583152 0.412176 0.358197 -0.0792776  -0.0904043  0.0165819   33  VAL   B HA   
280  H HB   . VAL   A 21  ? 0.580305 0.41849  0.390339 -0.097092   -0.0783574  -0.00554799 33  VAL   B HB   
281  H HG11 . VAL   A 21  ? 0.551243 0.378652 0.339431 -0.0911821  -0.051548   0.0143033   33  VAL   B HG11 
282  H HG12 . VAL   A 21  ? 0.587475 0.395319 0.346441 -0.0977771  -0.049328   0.00287852  33  VAL   B HG12 
283  H HG13 . VAL   A 21  ? 0.538914 0.375979 0.353187 -0.096195   -0.0412865  0.00608596  33  VAL   B HG13 
284  H HG21 . VAL   A 21  ? 0.54256  0.416529 0.417159 -0.088629   -0.0565402  0.011484    33  VAL   B HG21 
285  H HG22 . VAL   A 21  ? 0.554125 0.437455 0.437191 -0.0861085  -0.0796495  0.00970493  33  VAL   B HG22 
286  H HG23 . VAL   A 21  ? 0.547827 0.4207   0.404675 -0.0794783  -0.068991   0.0186075   33  VAL   B HG23 
287  N N    . LEU   A 22  ? 0.687136 0.458147 0.361487 -0.0821422  -0.0924642  0.0136764   34  LEU   B N    
288  C CA   . LEU   A 22  ? 0.765999 0.4965   0.370291 -0.0816276  -0.0874903  0.0142079   34  LEU   B CA   
289  C C    . LEU   A 22  ? 0.738527 0.453845 0.335849 -0.0895293  -0.0506839  0.020246    34  LEU   B C    
290  O O    . LEU   A 22  ? 0.700346 0.429848 0.335883 -0.0925784  -0.0394773  0.0277957   34  LEU   B O    
291  C CB   . LEU   A 22  ? 0.843271 0.552033 0.40586  -0.0684465  -0.107234   0.026633    34  LEU   B CB   
292  C CG   . LEU   A 22  ? 0.858276 0.591324 0.444193 -0.0579273  -0.145857   0.0227858   34  LEU   B CG   
293  C CD1  . LEU   A 22  ? 0.867368 0.58421  0.426867 -0.0407445  -0.163674   0.0382401   34  LEU   B CD1  
294  C CD2  . LEU   A 22  ? 0.922851 0.651511 0.48329  -0.0606595  -0.167532   0.00451128  34  LEU   B CD2  
295  H H    . LEU   A 22  ? 0.666606 0.442618 0.354653 -0.0787907  -0.0894824  0.0217191   34  LEU   B H    
296  H HA   . LEU   A 22  ? 0.783675 0.509964 0.373661 -0.0836053  -0.0948199  0.00260532  34  LEU   B HA   
297  H HB2  . LEU   A 22  ? 0.825188 0.530883 0.397776 -0.0674984  -0.0966495  0.037158    34  LEU   B HB2  
298  H HB3  . LEU   A 22  ? 0.891487 0.569857 0.399803 -0.0663294  -0.103952   0.0280704   34  LEU   B HB3  
299  H HG   . LEU   A 22  ? 0.805894 0.569298 0.445992 -0.0606156  -0.144683   0.0204781   34  LEU   B HG   
300  H HD11 . LEU   A 22  ? 0.854164 0.569454 0.429033 -0.0399551  -0.149427   0.0473632   34  LEU   B HD11 
301  H HD12 . LEU   A 22  ? 0.869002 0.607823 0.453788 -0.033654   -0.187973   0.0349575   34  LEU   B HD12 
302  H HD13 . LEU   A 22  ? 0.928677 0.612848 0.430389 -0.0363972  -0.16491    0.0426852   34  LEU   B HD13 
303  H HD21 . LEU   A 22  ? 0.88715  0.628824 0.475914 -0.0708534  -0.15741    -0.00578054 34  LEU   B HD21 
304  H HD22 . LEU   A 22  ? 0.96623  0.661619 0.466147 -0.0578356  -0.163874   0.00562181  34  LEU   B HD22 
305  H HD23 . LEU   A 22  ? 0.919493 0.664021 0.495832 -0.0543735  -0.195366   0.00154803  34  LEU   B HD23 
306  N N    . LYS   A 23  ? 0.742254 0.428699 0.291647 -0.0919325  -0.0327284  0.0157098   35  LYS   B N    
307  C CA   . LYS   A 23  ? 0.731925 0.412583 0.290606 -0.0997741  0.00619079  0.0190936   35  LYS   B CA   
308  C C    . LYS   A 23  ? 0.824228 0.457588 0.309545 -0.096993   0.0296482   0.028252    35  LYS   B C    
309  O O    . LYS   A 23  ? 0.870034 0.473196 0.287024 -0.0890256  0.0203189   0.0211167   35  LYS   B O    
310  C CB   . LYS   A 23  ? 0.6939   0.387892 0.277198 -0.103713   0.01924     0.00327442  35  LYS   B CB   
311  C CG   . LYS   A 23  ? 0.705955 0.403299 0.314403 -0.108944   0.0584502   0.00698618  35  LYS   B CG   
312  C CD   . LYS   A 23  ? 0.709919 0.41492  0.340358 -0.108547   0.0749814   -0.00721667 35  LYS   B CD   
313  C CE   . LYS   A 23  ? 0.721679 0.443894 0.400071 -0.111475   0.110045    -0.00084167 35  LYS   B CE   
314  N NZ   . LYS   A 23  ? 0.768824 0.484791 0.451111 -0.106634   0.135176    -0.012797   35  LYS   B NZ   
315  H H    . LYS   A 23  ? 0.790321 0.460526 0.300657 -0.0876434  -0.0450539  0.0098395   35  LYS   B H    
316  H HA   . LYS   A 23  ? 0.700135 0.396233 0.296442 -0.103392   0.011704    0.026243    35  LYS   B HA   
317  H HB2  . LYS   A 23  ? 0.660105 0.380102 0.285588 -0.104658   0.00611374  -0.00092848 35  LYS   B HB2  
318  H HB3  . LYS   A 23  ? 0.743765 0.417673 0.286028 -0.100708   0.0140076   -0.00611279 35  LYS   B HB3  
319  H HG2  . LYS   A 23  ? 0.749161 0.420702 0.318881 -0.10847    0.0756332   0.0134517   35  LYS   B HG2  
320  H HG3  . LYS   A 23  ? 0.66655  0.385517 0.318113 -0.11242    0.0588036   0.0139012   35  LYS   B HG3  
321  H HD2  . LYS   A 23  ? 0.679039 0.403431 0.340733 -0.108457   0.0581973   -0.0127574  35  LYS   B HD2  
322  H HD3  . LYS   A 23  ? 0.762183 0.440082 0.344864 -0.105344   0.0791308   -0.0156287  35  LYS   B HD3  
323  H HE2  . LYS   A 23  ? 0.746245 0.455251 0.407606 -0.113971   0.126091    0.00826552  35  LYS   B HE2  
324  H HE3  . LYS   A 23  ? 0.673579 0.424591 0.401342 -0.113417   0.10091     0.00286969  35  LYS   B HE3  
325  H HZ1  . LYS   A 23  ? 0.81041  0.496822 0.442265 -0.103948   0.14597     -0.0172199  35  LYS   B HZ1  
326  H HZ2  . LYS   A 23  ? 0.740993 0.464851 0.438173 -0.104814   0.121376    -0.0207734  35  LYS   B HZ2  
327  H HZ3  . LYS   A 23  ? 0.745967 0.478196 0.466354 -0.107267   0.154337    -0.00793297 35  LYS   B HZ3  
328  N N    . ILE   A 24  ? 0.856681 0.482722 0.357309 -0.103882   0.0611873   0.0431735   36  ILE   B N    
329  C CA   . ILE   A 24  ? 0.982817 0.568687 0.430446 -0.103865   0.100529    0.0529662   36  ILE   B CA   
330  C C    . ILE   A 24  ? 0.959692 0.568664 0.470727 -0.115275   0.140307    0.0531168   36  ILE   B C    
331  O O    . ILE   A 24  ? 0.905002 0.544717 0.488546 -0.125522   0.140686    0.0575866   36  ILE   B O    
332  C CB   . ILE   A 24  ? 1.03127  0.5756   0.431084 -0.100905   0.107922    0.076213    36  ILE   B CB   
333  C CG1  . ILE   A 24  ? 1.07402  0.601891 0.422867 -0.0861256  0.063862    0.0779599   36  ILE   B CG1  
334  C CG2  . ILE   A 24  ? 1.08169  0.578819 0.417301 -0.0989425  0.155478    0.0890214   36  ILE   B CG2  
335  C CD1  . ILE   A 24  ? 1.20011  0.666116 0.451624 -0.0730232  0.0720218   0.0984077   36  ILE   B CD1  
336  H H    . ILE   A 24  ? 0.81991  0.465516 0.365568 -0.108836   0.0589762   0.0470958   36  ILE   B H    
337  H HA   . ILE   A 24  ? 1.01065  0.578121 0.409586 -0.0968814  0.0984299   0.0445492   36  ILE   B HA   
338  H HB   . ILE   A 24  ? 0.994216 0.553206 0.443735 -0.109549   0.112628    0.0826948   36  ILE   B HB   
339  H HG12 . ILE   A 24  ? 1.06777  0.606767 0.407381 -0.0815349  0.0436399   0.063088    36  ILE   B HG12 
340  H HG13 . ILE   A 24  ? 1.03134  0.57854  0.421969 -0.0881365  0.0475813   0.0802285   36  ILE   B HG13 
341  H HG21 . ILE   A 24  ? 1.13406  0.601658 0.44024  -0.0972272  0.162995    0.106379    36  ILE   B HG21 
342  H HG22 . ILE   A 24  ? 1.13568  0.614211 0.414576 -0.0891821  0.150859    0.0807264   36  ILE   B HG22 
343  H HG23 . ILE   A 24  ? 1.07355  0.587129 0.454221 -0.108307   0.184059    0.0883897   36  ILE   B HG23 
344  H HD11 . ILE   A 24  ? 1.20281  0.653774 0.464674 -0.0788242  0.0953458   0.114377    36  ILE   B HD11 
345  H HD12 . ILE   A 24  ? 1.20249  0.664645 0.432254 -0.0622354  0.0393224   0.0991518   36  ILE   B HD12 
346  H HD13 . ILE   A 24  ? 1.24324  0.686463 0.442462 -0.0683437  0.0863498   0.0952053   36  ILE   B HD13 
347  N N    . VAL   A 25  ? 1.05708  0.646602 0.534795 -0.111653   0.174272    0.0484641   37  VAL   B N    
348  C CA   . VAL   A 25  ? 1.01348  0.619721 0.546185 -0.119273   0.220552    0.0523018   37  VAL   B CA   
349  C C    . VAL   A 25  ? 1.04088  0.618305 0.55997  -0.126444   0.256387    0.0762884   37  VAL   B C    
350  O O    . VAL   A 25  ? 1.09411  0.617995 0.521102 -0.11757    0.272595    0.0871913   37  VAL   B O    
351  C CB   . VAL   A 25  ? 1.03866  0.630156 0.538756 -0.10955    0.248897    0.0383408   37  VAL   B CB   
352  C CG1  . VAL   A 25  ? 1.01947  0.632334 0.585171 -0.114382   0.300798    0.0439867   37  VAL   B CG1  
353  C CG2  . VAL   A 25  ? 0.993165 0.604322 0.506415 -0.104166   0.214678    0.014822    37  VAL   B CG2  
354  H H    . VAL   A 25  ? 1.07815  0.643163 0.497401 -0.103197   0.168115    0.0418442   37  VAL   B H    
355  H HA   . VAL   A 25  ? 0.950876 0.595601 0.553728 -0.125563   0.210699    0.048776    37  VAL   B HA   
356  H HB   . VAL   A 25  ? 1.10709  0.656754 0.528947 -0.102069   0.257451    0.040996    37  VAL   B HB   
357  H HG11 . VAL   A 25  ? 0.961435 0.615216 0.603706 -0.12154    0.290225    0.0433716   37  VAL   B HG11 
358  H HG12 . VAL   A 25  ? 1.06441  0.657773 0.614348 -0.117813   0.328682    0.0588962   37  VAL   B HG12 
359  H HG13 . VAL   A 25  ? 1.04803  0.652542 0.596292 -0.106073   0.317048    0.0333269   37  VAL   B HG13 
360  H HG21 . VAL   A 25  ? 1.02636  0.624024 0.519732 -0.0980251  0.234094    0.00492506  37  VAL   B HG21 
361  H HG22 . VAL   A 25  ? 1.00494  0.602756 0.478274 -0.101176   0.184226    0.0106073   37  VAL   B HG22 
362  H HG23 . VAL   A 25  ? 0.931727 0.580666 0.513889 -0.109331   0.20455     0.0140979   37  VAL   B HG23 
363  N N    . LYS   A 26  ? 1.01208  0.622268 0.621582 -0.142307   0.267611    0.0843511   38  LYS   B N    
364  C CA   . LYS   A 26  ? 1.04227  0.625718 0.656002 -0.153821   0.304186    0.107266    38  LYS   B CA   
365  C C    . LYS   A 26  ? 1.06198  0.660017 0.728098 -0.160855   0.362427    0.11246     38  LYS   B C    
366  O O    . LYS   A 26  ? 1.15907  0.715139 0.781234 -0.160738   0.410753    0.131147    38  LYS   B O    
367  C CB   . LYS   A 26  ? 0.985334 0.585037 0.658232 -0.168096   0.275513    0.111494    38  LYS   B CB   
368  C CG   . LYS   A 26  ? 0.96818  0.55426  0.593925 -0.15783    0.223164    0.107612    38  LYS   B CG   
369  C CD   . LYS   A 26  ? 1.02759  0.551422 0.541286 -0.142834   0.222854    0.122481    38  LYS   B CD   
370  C CE   . LYS   A 26  ? 1.09558  0.573663 0.592463 -0.150281   0.249988    0.147817    38  LYS   B CE   
371  N NZ   . LYS   A 26  ? 1.19986  0.616    0.582948 -0.131057   0.24491     0.164566    38  LYS   B NZ   
372  H H    . LYS   A 26  ? 0.946321 0.594607 0.616328 -0.146327   0.251789    0.0753825   38  LYS   B H    
373  H HA   . LYS   A 26  ? 1.10546  0.643875 0.64008  -0.145531   0.310575    0.117141    38  LYS   B HA   
374  H HB2  . LYS   A 26  ? 0.932801 0.575159 0.679539 -0.175595   0.267456    0.10165     38  LYS   B HB2  
375  H HB3  . LYS   A 26  ? 1.02566  0.602427 0.701154 -0.176975   0.301125    0.126834    38  LYS   B HB3  
376  H HG2  . LYS   A 26  ? 0.922749 0.534214 0.555548 -0.151158   0.199432    0.093078    38  LYS   B HG2  
377  H HG3  . LYS   A 26  ? 0.937747 0.532463 0.60409  -0.166625   0.210649    0.109098    38  LYS   B HG3  
378  H HD2  . LYS   A 26  ? 1.07242  0.581659 0.540532 -0.134879   0.239325    0.121066    38  LYS   B HD2  
379  H HD3  . LYS   A 26  ? 1.01584  0.542461 0.510498 -0.134187   0.18671     0.116305    38  LYS   B HD3  
380  H HE2  . LYS   A 26  ? 1.06439  0.554147 0.607204 -0.15876    0.233762    0.146929    38  LYS   B HE2  
381  H HE3  . LYS   A 26  ? 1.12047  0.595876 0.638713 -0.159436   0.288983    0.155198    38  LYS   B HE3  
382  H HZ1  . LYS   A 26  ? 1.17351  0.595986 0.541984 -0.121852   0.20834     0.157282    38  LYS   B HZ1  
383  H HZ2  . LYS   A 26  ? 1.23584  0.636093 0.569965 -0.123054   0.261276    0.165147    38  LYS   B HZ2  
384  H HZ3  . LYS   A 26  ? 1.23289  0.618525 0.607873 -0.135256   0.261766    0.181898    38  LYS   B HZ3  
385  N N    . ARG   A 27  ? 1.03237  0.68795  0.788929 -0.163802   0.36103     0.0976089   39  ARG   B N    
386  C CA   . ARG   A 27  ? 1.04353  0.716249 0.849485 -0.164543   0.416465    0.100682    39  ARG   B CA   
387  C C    . ARG   A 27  ? 1.01677  0.709823 0.820296 -0.147235   0.409266    0.0798653   39  ARG   B C    
388  O O    . ARG   A 27  ? 0.929882 0.660647 0.775684 -0.145332   0.36524     0.0652763   39  ARG   B O    
389  C CB   . ARG   A 27  ? 1.0068   0.732465 0.947441 -0.185743   0.428701    0.106123    39  ARG   B CB   
390  C CG   . ARG   A 27  ? 1.01024  0.761599 1.02472  -0.188457   0.490665    0.112917    39  ARG   B CG   
391  C CD   . ARG   A 27  ? 0.968792 0.785955 1.13489  -0.210439   0.486175    0.112786    39  ARG   B CD   
392  N NE   . ARG   A 27  ? 0.931528 0.808656 1.16456  -0.204012   0.433897    0.0918869   39  ARG   B NE   
393  C CZ   . ARG   A 27  ? 0.888792 0.822548 1.23166  -0.217983   0.39948     0.0839927   39  ARG   B CZ   
394  N NH1  . ARG   A 27  ? 0.870607 0.814778 1.28752  -0.243852   0.411066    0.0921927   39  ARG   B NH1  
395  N NH2  . ARG   A 27  ? 0.830976 0.807445 1.20689  -0.205772   0.351927    0.0675142   39  ARG   B NH2  
396  H H    . ARG   A 27  ? 0.965735 0.650017 0.754187 -0.163813   0.326254    0.0864981   39  ARG   B H    
397  H HA   . ARG   A 27  ? 1.11587  0.747995 0.865016 -0.161105   0.45255     0.112932    39  ARG   B HA   
398  H HB2  . ARG   A 27  ? 1.01656  0.723814 0.955137 -0.197756   0.42829     0.117302    39  ARG   B HB2  
399  H HB3  . ARG   A 27  ? 0.938915 0.702664 0.928293 -0.186535   0.392162    0.0936143   39  ARG   B HB3  
400  H HG2  . ARG   A 27  ? 1.01144  0.774078 1.02014  -0.174071   0.495056    0.102415    39  ARG   B HG2  
401  H HG3  . ARG   A 27  ? 1.08359  0.796306 1.05373  -0.18907    0.531538    0.127897    39  ARG   B HG3  
402  H HD2  . ARG   A 27  ? 1.00139  0.831516 1.21556  -0.213646   0.531304    0.120685    39  ARG   B HD2  
403  H HD3  . ARG   A 27  ? 0.979463 0.784042 1.15145  -0.225417   0.474249    0.119373    39  ARG   B HD3  
404  H HE   . ARG   A 27  ? 0.914335 0.787622 1.10881  -0.188787   0.42348     0.0837528   39  ARG   B HE   
405  H HH11 . ARG   A 27  ? 0.921063 0.848682 1.34301  -0.251463   0.453481    0.105054    39  ARG   B HH11 
406  H HH12 . ARG   A 27  ? 0.849566 0.815549 1.3107   -0.253694   0.376777    0.084451    39  ARG   B HH12 
407  H HH21 . ARG   A 27  ? 0.821755 0.785595 1.14461  -0.190907   0.339811    0.0622429   39  ARG   B HH21 
408  H HH22 . ARG   A 27  ? 0.798908 0.81503  1.24924  -0.212349   0.332359    0.0621758   39  ARG   B HH22 
409  N N    . VAL   A 28  ? 1.10766  0.76747  0.853038 -0.133373   0.455458    0.0795202   40  VAL   B N    
410  C CA   . VAL   A 28  ? 1.11358  0.775948 0.841887 -0.115388   0.457298    0.0589738   40  VAL   B CA   
411  C C    . VAL   A 28  ? 1.08081  0.809397 0.937868 -0.116184   0.46788     0.0538171   40  VAL   B C    
412  O O    . VAL   A 28  ? 1.09159  0.850439 1.03163  -0.12569    0.505562    0.067025    40  VAL   B O    
413  C CB   . VAL   A 28  ? 1.18784  0.789694 0.815744 -0.099742   0.512093    0.0607451   40  VAL   B CB   
414  C CG1  . VAL   A 28  ? 1.20231  0.809335 0.87941  -0.105916   0.582584    0.0826946   40  VAL   B CG1  
415  C CG2  . VAL   A 28  ? 1.20413  0.796142 0.803871 -0.0801064  0.517315    0.0358869   40  VAL   B CG2  
416  H H    . VAL   A 28  ? 1.16045  0.789639 0.870383 -0.13451    0.488996    0.0929193   40  VAL   B H    
417  H HA   . VAL   A 28  ? 1.09027  0.746979 0.785434 -0.111463   0.417054    0.0475412   40  VAL   B HA   
418  H HB   . VAL   A 28  ? 1.23178  0.791798 0.774485 -0.0975298  0.498753    0.0641682   40  VAL   B HB   
419  H HG11 . VAL   A 28  ? 1.16869  0.821571 0.937589 -0.10795    0.593885    0.0796668   40  VAL   B HG11 
420  H HG12 . VAL   A 28  ? 1.2091   0.814242 0.898293 -0.119299   0.580563    0.0982228   40  VAL   B HG12 
421  H HG13 . VAL   A 28  ? 1.28856  0.853589 0.893986 -0.0938151  0.619555    0.0844336   40  VAL   B HG13 
422  H HG21 . VAL   A 28  ? 1.28527  0.830337 0.802503 -0.0691335  0.544904    0.0342479   40  VAL   B HG21 
423  H HG22 . VAL   A 28  ? 1.17164  0.766304 0.757811 -0.0791987  0.473104    0.0226726   40  VAL   B HG22 
424  H HG23 . VAL   A 28  ? 1.17684  0.804811 0.85463  -0.0787643  0.537709    0.0347769   40  VAL   B HG23 
425  N N    . GLY   A 29  ? 1.07896  0.82869  0.954314 -0.105248   0.435441    0.0355312   41  GLY   B N    
426  C CA   . GLY   A 29  ? 1.0394   0.846277 1.02515  -0.0990053  0.44242     0.0309911   41  GLY   B CA   
427  C C    . GLY   A 29  ? 1.11449  0.906013 1.09356  -0.0803114  0.499369    0.0252401   41  GLY   B C    
428  O O    . GLY   A 29  ? 1.23875  0.976691 1.13154  -0.0745914  0.54146     0.0270858   41  GLY   B O    
429  H H    . GLY   A 29  ? 1.07097  0.798528 0.890345 -0.101013   0.408046    0.0265303   41  GLY   B H    
430  H HA2  . GLY   A 29  ? 1.01249  0.855089 1.0712   -0.109912   0.445239    0.0405103   41  GLY   B HA2  
431  H HA3  . GLY   A 29  ? 0.998671 0.819188 0.994131 -0.0950051  0.40584     0.0221385   41  GLY   B HA3  
432  N N    . ASN   A 30  ? 1.09363  0.929301 1.15956  -0.0677781  0.500321    0.0186187   42  ASN   B N    
433  C CA   . ASN   A 30  ? 1.18036  1.00727  1.25669  -0.0462441  0.553595    0.0119057   42  ASN   B CA   
434  C C    . ASN   A 30  ? 1.17289  1.01107  1.27432  -0.0283078  0.525145    -0.00337248 42  ASN   B C    
435  O O    . ASN   A 30  ? 1.06214  0.935437 1.20944  -0.0328613  0.472886    -0.0023713  42  ASN   B O    
436  C CB   . ASN   A 30  ? 1.23034  1.11026  1.42284  -0.0480691  0.602145    0.0272359   42  ASN   B CB   
437  C CG   . ASN   A 30  ? 1.18265  1.14024  1.50295  -0.0606114  0.558526    0.0344213   42  ASN   B CG   
438  O OD1  . ASN   A 30  ? 1.10529  1.09515  1.47332  -0.0481972  0.521068    0.0268379   42  ASN   B OD1  
439  N ND2  . ASN   A 30  ? 1.1943   1.17858  1.56843  -0.0843289  0.562194    0.0487045   42  ASN   B ND2  
440  H H    . ASN   A 30  ? 1.04155  0.912397 1.16013  -0.0709576  0.466239    0.0185507   42  ASN   B H    
441  H HA   . ASN   A 30  ? 1.25162  1.02732  1.24108  -0.041108   0.577731    0.00723707  42  ASN   B HA   
442  H HB2  . ASN   A 30  ? 1.25251  1.13383  1.46465  -0.0306942  0.634158    0.0221922   42  ASN   B HB2  
443  H HB3  . ASN   A 30  ? 1.26767  1.12829  1.43278  -0.0574933  0.631538    0.0373087   42  ASN   B HB3  
444  H HD21 . ASN   A 30  ? 1.14116  1.17152  1.59437  -0.0915826  0.538472    0.0508675   42  ASN   B HD21 
445  H HD22 . ASN   A 30  ? 1.22568  1.1797   1.55589  -0.0928431  0.587684    0.0558771   42  ASN   B HD22 
446  N N    . GLY   A 31  ? 1.27067  1.07467  1.34035  -0.00608009 0.563211    -0.016781   43  GLY   B N    
447  C CA   . GLY   A 31  ? 1.26052  1.04989  1.32327  0.0101306   0.538209    -0.033242   43  GLY   B CA   
448  C C    . GLY   A 31  ? 1.26687  0.989998 1.20598  0.00353574  0.506368    -0.0508231  43  GLY   B C    
449  O O    . GLY   A 31  ? 1.28461  0.981804 1.15036  -0.0116178  0.496934    -0.048121   43  GLY   B O    
450  H H    . GLY   A 31  ? 1.31347  1.09999  1.36486  -0.00050846 0.607711    -0.015473   43  GLY   B H    
451  H HA2  . GLY   A 31  ? 1.29096  1.07138  1.36664  0.0276628   0.573901    -0.0392044  43  GLY   B HA2  
452  H HA3  . GLY   A 31  ? 1.19279  1.02345  1.32077  0.00870719  0.506663    -0.02698    43  GLY   B HA3  
453  N N    . GLU   A 32  ? 1.20875  0.902838 1.12857  0.0159221   0.491752    -0.0688803  44  GLU   B N    
454  C CA   . GLU   A 32  ? 1.21712  0.853144 1.03688  0.00845543  0.458772    -0.0889309  44  GLU   B CA   
455  C C    . GLU   A 32  ? 1.10621  0.768555 0.969084 -0.00034225 0.402539    -0.0852026  44  GLU   B C    
456  O O    . GLU   A 32  ? 1.07261  0.707906 0.877946 -0.0133021  0.365305    -0.0950784  44  GLU   B O    
457  C CB   . GLU   A 32  ? 1.28299  0.851207 1.03197  0.0267409   0.494131    -0.115799   44  GLU   B CB   
458  H H    . GLU   A 32  ? 1.20777  0.918253 1.18149  0.029395    0.502908    -0.068822   44  GLU   B H    
459  H HA   . GLU   A 32  ? 1.22539  0.848821 0.993522 -0.00285868 0.452314    -0.0861308  44  GLU   B HA   
462  N N    . GLU   A 33  ? 1.02128  0.740222 0.985959 0.0066658   0.395452    -0.0684083  45  GLU   B N    
463  C CA   . GLU   A 33  ? 1.00086  0.734698 1.00085  0.00638755  0.353492    -0.0639929  45  GLU   B CA   
464  C C    . GLU   A 33  ? 0.905285 0.677783 0.918421 -0.011974   0.311249    -0.0482782  45  GLU   B C    
465  O O    . GLU   A 33  ? 0.862846 0.677755 0.916683 -0.0173379  0.313734    -0.0342172  45  GLU   B O    
466  C CB   . GLU   A 33  ? 0.955399 0.719913 1.0434   0.0298492   0.366517    -0.0543921  45  GLU   B CB   
467  H H    . GLU   A 33  ? 1.02541  0.774589 1.03832  0.0121539   0.417033    -0.0586106  45  GLU   B H    
468  H HA   . GLU   A 33  ? 1.01273  0.705913 0.966098 0.00430007  0.344814    -0.0783765  45  GLU   B HA   
471  N N    . THR   A 34  ? 0.925979 0.680306 0.904535 -0.0223685  0.274411    -0.0525101  46  THR   B N    
472  C CA   . THR   A 34  ? 0.833459 0.616564 0.816705 -0.0366861  0.235928    -0.0399168  46  THR   B CA   
473  C C    . THR   A 34  ? 0.786485 0.587432 0.813742 -0.0287231  0.212045    -0.0296857  46  THR   B C    
474  O O    . THR   A 34  ? 0.88087  0.651201 0.903436 -0.0217684  0.21557     -0.037147   46  THR   B O    
475  C CB   . THR   A 34  ? 0.849213 0.598626 0.757272 -0.0530952  0.215531    -0.0509425  46  THR   B CB   
476  O OG1  . THR   A 34  ? 0.871417 0.588425 0.76613  -0.0513115  0.206367    -0.064519   46  THR   B OG1  
477  C CG2  . THR   A 34  ? 0.882853 0.600266 0.726571 -0.0565371  0.23989     -0.0607583  46  THR   B CG2  
478  H H    . THR   A 34  ? 0.936207 0.657874 0.889282 -0.0202041  0.274661    -0.0644869  46  THR   B H    
479  H HA   . THR   A 34  ? 0.81657  0.628642 0.825099 -0.0390563  0.239159    -0.0302859  46  THR   B HA   
480  H HB   . THR   A 34  ? 0.809895 0.579482 0.724328 -0.0607298  0.192704    -0.0418305  46  THR   B HB   
482  H HG21 . THR   A 34  ? 0.904259 0.602945 0.701084 -0.065106   0.221412    -0.0663805  46  THR   B HG21 
483  H HG22 . THR   A 34  ? 0.932383 0.624522 0.761168 -0.0481054  0.26221     -0.0721116  46  THR   B HG22 
484  H HG23 . THR   A 34  ? 0.879269 0.618261 0.742535 -0.0576441  0.252279    -0.0498294  46  THR   B HG23 
485  N N    . PRO   A 35  ? 0.705055 0.550008 0.770822 -0.0290088  0.187853    -0.0125288  47  PRO   B N    
486  C CA   . PRO   A 35  ? 0.675451 0.538072 0.781734 -0.0141321  0.171778    0.00124536  47  PRO   B CA   
487  C C    . PRO   A 35  ? 0.664408 0.491356 0.744329 -0.0158501  0.162473    -0.00086212 47  PRO   B C    
488  O O    . PRO   A 35  ? 0.745149 0.552397 0.783689 -0.0328423  0.150823    -0.009741   47  PRO   B O    
489  C CB   . PRO   A 35  ? 0.628557 0.534233 0.75532  -0.0176254  0.143465    0.0143283   47  PRO   B CB   
490  C CG   . PRO   A 35  ? 0.655051 0.557509 0.747017 -0.0385213  0.142122    0.00698305  47  PRO   B CG   
491  C CD   . PRO   A 35  ? 0.674127 0.546916 0.740151 -0.0420191  0.175479    -0.00621655 47  PRO   B CD   
492  H HA   . PRO   A 35  ? 0.680145 0.550678 0.820374 3.475e-05   0.186445    0.00375751  47  PRO   B HA   
493  H HB2  . PRO   A 35  ? 0.623827 0.528163 0.742599 -0.0154684  0.125931    0.0210666   47  PRO   B HB2  
494  H HB3  . PRO   A 35  ? 0.627973 0.561659 0.796871 -0.00775871 0.144509    0.0203076   47  PRO   B HB3  
495  H HG2  . PRO   A 35  ? 0.637392 0.527243 0.697685 -0.0462714  0.127053    0.00606343  47  PRO   B HG2  
496  H HG3  . PRO   A 35  ? 0.626493 0.55633  0.743566 -0.04066    0.135527    0.0119028   47  PRO   B HG3  
497  H HD2  . PRO   A 35  ? 0.692242 0.544468 0.713879 -0.0533478  0.172525    -0.0122876  47  PRO   B HD2  
498  H HD3  . PRO   A 35  ? 0.684041 0.574118 0.778022 -0.0399348  0.191851    -0.0043086  47  PRO   B HD3  
499  N N    . MET   A 36  ? 0.637769 0.457314 0.74771  0.00243698  0.168215    0.00858042  48  MET   B N    
500  C CA   . MET   A 36  ? 0.66523  0.450779 0.764906 0.00166259  0.164531    0.0113055   48  MET   B CA   
501  C C    . MET   A 36  ? 0.631911 0.441732 0.740914 0.00749204  0.141599    0.0344855   48  MET   B C    
502  O O    . MET   A 36  ? 0.581333 0.430268 0.708573 0.0187379   0.12818     0.0469951   48  MET   B O    
503  C CB   . MET   A 36  ? 0.723185 0.479769 0.848999 0.0219023   0.18734     0.0135408   48  MET   B CB   
504  C CG   . MET   A 36  ? 0.799837 0.531708 0.920493 0.0256132   0.216573    -0.00794913 48  MET   B CG   
505  S SD   . MET   A 36  ? 0.934348 0.598555 1.00159  0.0045809   0.223894    -0.0395245  48  MET   B SD   
506  C CE   . MET   A 36  ? 0.871549 0.53953  0.881337 -0.0247825  0.201215    -0.0563472  48  MET   B CE   
507  H H    . MET   A 36  ? 0.650006 0.486434 0.791828 0.0165481   0.175739    0.0147094   48  MET   B H    
508  H HA   . MET   A 36  ? 0.677997 0.441795 0.748707 -0.0141738  0.162463    -0.00209942 48  MET   B HA   
509  H HB2  . MET   A 36  ? 0.715694 0.49504  0.870081 0.039185    0.184063    0.0299324   48  MET   B HB2  
510  H HB3  . MET   A 36  ? 0.742088 0.470753 0.860775 0.0175779   0.18688     0.0140545   48  MET   B HB3  
511  H HG2  . MET   A 36  ? 0.791722 0.546356 0.909575 0.022066    0.21872     -0.0117899  48  MET   B HG2  
512  H HG3  . MET   A 36  ? 0.81995  0.548744 0.969623 0.0445816   0.230022    -0.00145125 48  MET   B HG3  
513  H HE1  . MET   A 36  ? 0.920387 0.552366 0.902478 -0.0341354  0.201252    -0.0752624  48  MET   B HE1  
514  H HE2  . MET   A 36  ? 0.849134 0.538203 0.866219 -0.0316234  0.181757    -0.044451   48  MET   B HE2  
515  H HE3  . MET   A 36  ? 0.880849 0.564212 0.879998 -0.0232546  0.208482    -0.0581523  48  MET   B HE3  
516  N N    . ILE   A 37  ? 0.610045 0.394268 0.708047 0.00068741  0.138614    0.0394802   49  ILE   B N    
517  C CA   . ILE   A 37  ? 0.605093 0.404875 0.702666 0.00799376  0.124074    0.0624167   49  ILE   B CA   
518  C C    . ILE   A 37  ? 0.622689 0.43094  0.742467 0.0384903   0.12615     0.0848913   49  ILE   B C    
519  O O    . ILE   A 37  ? 0.622371 0.405341 0.762173 0.052296    0.144642    0.0876106   49  ILE   B O    
520  C CB   . ILE   A 37  ? 0.651617 0.424061 0.742808 -0.00617668 0.127244    0.0651178   49  ILE   B CB   
521  C CG1  . ILE   A 37  ? 0.662208 0.440735 0.732977 -0.032657   0.11391     0.0443663   49  ILE   B CG1  
522  C CG2  . ILE   A 37  ? 0.646992 0.427736 0.736232 0.00863284  0.123711    0.0943082   49  ILE   B CG2  
523  C CD1  . ILE   A 37  ? 0.673125 0.437584 0.750978 -0.0493099  0.112194    0.0441949   49  ILE   B CD1  
524  H H    . ILE   A 37  ? 0.641204 0.397074 0.732171 -0.00856606 0.146799    0.0279994   49  ILE   B H    
525  H HA   . ILE   A 37  ? 0.585924 0.410596 0.672972 0.00318496  0.109826    0.0614609   49  ILE   B HA   
526  H HB   . ILE   A 37  ? 0.676058 0.419228 0.777959 -0.00685308 0.141233    0.0608764   49  ILE   B HB   
527  H HG12 . ILE   A 37  ? 0.632577 0.436778 0.692608 -0.03141    0.101678    0.0475025   49  ILE   B HG12 
528  H HG13 . ILE   A 37  ? 0.66801  0.434937 0.731854 -0.0394153  0.117894    0.0270166   49  ILE   B HG13 
529  H HG21 . ILE   A 37  ? 0.653627 0.421899 0.744367 -0.00226544 0.128129    0.0962044   49  ILE   B HG21 
530  H HG22 . ILE   A 37  ? 0.627398 0.434559 0.703934 0.0123313   0.109296    0.097263    49  ILE   B HG22 
531  H HG23 . ILE   A 37  ? 0.668632 0.438945 0.766881 0.0262926   0.132111    0.108159    49  ILE   B HG23 
532  H HD11 . ILE   A 37  ? 0.697484 0.435315 0.791064 -0.0506805  0.124614    0.0434058   49  ILE   B HD11 
533  H HD12 . ILE   A 37  ? 0.666554 0.433546 0.733251 -0.0640941  0.10179     0.0283718   49  ILE   B HD12 
534  H HD13 . ILE   A 37  ? 0.659003 0.437687 0.738364 -0.0434066  0.109455    0.0606786   49  ILE   B HD13 
535  N N    . GLY   A 38  ? 0.583867 0.425649 0.69691  0.0505669   0.104602    0.0996203   50  GLY   B N    
536  C CA   . GLY   A 38  ? 0.58627  0.440143 0.713426 0.0824855   0.0971013   0.121094    50  GLY   B CA   
537  C C    . GLY   A 38  ? 0.555804 0.452897 0.715889 0.0912693   0.0833887   0.113139    50  GLY   B C    
538  O O    . GLY   A 38  ? 0.563058 0.484925 0.734481 0.115775    0.0630116   0.12755     50  GLY   B O    
539  H H    . GLY   A 38  ? 0.565638 0.421184 0.662988 0.039904    0.0928033   0.0954505   50  GLY   B H    
540  H HA2  . GLY   A 38  ? 0.590034 0.448151 0.696023 0.0895348   0.0853264   0.134057    50  GLY   B HA2  
541  H HA3  . GLY   A 38  ? 0.613864 0.442075 0.751175 0.0929478   0.112759    0.128949    50  GLY   B HA3  
542  N N    . ASP   A 39  ? 0.526326 0.432074 0.701996 0.07215     0.0943321   0.0910533   51  ASP   B N    
543  C CA   . ASP   A 39  ? 0.572486 0.521038 0.791201 0.0764954   0.0885381   0.0839174   51  ASP   B CA   
544  C C    . ASP   A 39  ? 0.557486 0.546365 0.775282 0.0746547   0.0532897   0.0861974   51  ASP   B C    
545  O O    . ASP   A 39  ? 0.589749 0.570539 0.765327 0.060393    0.0406405   0.0843773   51  ASP   B O    
546  C CB   . ASP   A 39  ? 0.55957  0.503672 0.783028 0.0548215   0.112369    0.0622531   51  ASP   B CB   
547  C CG   . ASP   A 39  ? 0.581963 0.49229  0.814499 0.0607239   0.147879    0.0533234   51  ASP   B CG   
548  O OD1  . ASP   A 39  ? 0.57799  0.469063 0.826558 0.0835757   0.156177    0.0646668   51  ASP   B OD1  
549  O OD2  . ASP   A 39  ? 0.550377 0.448606 0.768571 0.0441109   0.168579    0.034935    51  ASP   B OD2  
550  H H    . ASP   A 39  ? 0.54264  0.426943 0.702629 0.0561843   0.106376    0.0804927   51  ASP   B H    
551  H HA   . ASP   A 39  ? 0.575986 0.529618 0.823864 0.096735    0.0925185   0.091985    51  ASP   B HA   
552  H HB2  . ASP   A 39  ? 0.549928 0.480732 0.73938  0.0368031   0.109795    0.0553255   51  ASP   B HB2  
553  H HB3  . ASP   A 39  ? 0.546297 0.522495 0.798507 0.0538879   0.107364    0.0594497   51  ASP   B HB3  
554  N N    . LYS   A 40  ? 0.552961 0.58512  0.821562 0.0901262   0.0363541   0.0887191   52  LYS   B N    
555  C CA   . LYS   A 40  ? 0.557882 0.629335 0.836256 0.0855631   0.00038053  0.0843026   52  LYS   B CA   
556  C C    . LYS   A 40  ? 0.50606  0.595363 0.810439 0.0560487   0.0117485   0.0657953   52  LYS   B C    
557  O O    . LYS   A 40  ? 0.476683 0.577993 0.828133 0.0535746   0.0378563   0.0604468   52  LYS   B O    
558  C CB   . LYS   A 40  ? 0.555062 0.666945 0.880623 0.115055    -0.0300798  0.0938819   52  LYS   B CB   
559  C CG   . LYS   A 40  ? 0.551892 0.692683 0.868071 0.115285    -0.0778506  0.0889018   52  LYS   B CG   
560  C CD   . LYS   A 40  ? 0.612531 0.802987 0.988989 0.140805    -0.11492    0.0920589   52  LYS   B CD   
561  C CE   . LYS   A 40  ? 0.611559 0.824954 0.971808 0.142525    -0.16832    0.0828947   52  LYS   B CE   
562  N NZ   . LYS   A 40  ? 0.615593 0.889729 1.06056  0.154896    -0.205627   0.0764503   52  LYS   B NZ   
563  H H    . LYS   A 40  ? 0.569477 0.60681  0.87095  0.104088    0.0466597   0.0922034   52  LYS   B H    
564  H HA   . LYS   A 40  ? 0.54736  0.603816 0.780751 0.0826542   -0.0120084  0.0870793   52  LYS   B HA   
565  H HB2  . LYS   A 40  ? 0.58119  0.675005 0.890809 0.136179    -0.0284709  0.108209    52  LYS   B HB2  
566  H HB3  . LYS   A 40  ? 0.552162 0.688564 0.932844 0.115415    -0.0204675  0.0891277   52  LYS   B HB3  
567  H HG2  . LYS   A 40  ? 0.541702 0.691041 0.865315 0.0918961   -0.0771759  0.0753182   52  LYS   B HG2  
568  H HG3  . LYS   A 40  ? 0.576772 0.692749 0.83694  0.121792    -0.0862867  0.0961797   52  LYS   B HG3  
569  H HD2  . LYS   A 40  ? 0.622877 0.802242 0.990773 0.166208    -0.113977   0.107496    52  LYS   B HD2  
570  H HD3  . LYS   A 40  ? 0.583567 0.8023   1.02335  0.133372    -0.104183   0.0849465   52  LYS   B HD3  
571  H HE2  . LYS   A 40  ? 0.59677  0.80589  0.945735 0.11776     -0.166167   0.0698345   52  LYS   B HE2  
572  H HE3  . LYS   A 40  ? 0.642233 0.831946 0.944327 0.160145    -0.181119   0.0934395   52  LYS   B HE3  
573  H HZ1  . LYS   A 40  ? 0.593084 0.890388 1.09636  0.1382      -0.190469   0.067754    52  LYS   B HZ1  
574  H HZ2  . LYS   A 40  ? 0.637543 0.916232 1.09272  0.180577    -0.209961   0.0895031   52  LYS   B HZ2  
575  H HZ3  . LYS   A 40  ? 0.631955 0.915991 1.06275  0.154261    -0.239974   0.067965    52  LYS   B HZ3  
576  N N    . VAL   A 41  ? 0.53629  0.62182  0.805904 0.0352675   -0.00353035 0.0575983   53  VAL   B N    
577  C CA   . VAL   A 41  ? 0.54574  0.630378 0.819858 0.00659912  0.013097    0.0442083   53  VAL   B CA   
578  C C    . VAL   A 41  ? 0.509577 0.624964 0.808999 -0.0058241  -0.0163792  0.0360028   53  VAL   B C    
579  O O    . VAL   A 41  ? 0.536464 0.649747 0.803105 -0.00044841 -0.0490857  0.0360726   53  VAL   B O    
580  C CB   . VAL   A 41  ? 0.563848 0.60318  0.767816 -0.00781574 0.0262253   0.0418337   53  VAL   B CB   
581  C CG1  . VAL   A 41  ? 0.578118 0.611435 0.768115 -0.0339331  0.0320393   0.0315008   53  VAL   B CG1  
582  C CG2  . VAL   A 41  ? 0.550739 0.558481 0.74057  -0.00353451 0.0575808   0.0426086   53  VAL   B CG2  
583  H H    . VAL   A 41  ? 0.534862 0.615541 0.774663 0.0407085   -0.0235855  0.0614034   53  VAL   B H    
584  H HA   . VAL   A 41  ? 0.539669 0.630711 0.846164 0.00568589  0.0355412   0.0421532   53  VAL   B HA   
585  H HB   . VAL   A 41  ? 0.559369 0.591558 0.734752 -0.00155624 0.00895686  0.0467335   53  VAL   B HB   
586  H HG11 . VAL   A 41  ? 0.573998 0.617591 0.795103 -0.0394723  0.0489169   0.028307    53  VAL   B HG11 
587  H HG12 . VAL   A 41  ? 0.565832 0.61004  0.755531 -0.037552   0.0107374   0.0298761   53  VAL   B HG12 
588  H HG13 . VAL   A 41  ? 0.572722 0.579093 0.722667 -0.0405976  0.040721    0.0300352   53  VAL   B HG13 
589  H HG21 . VAL   A 41  ? 0.559188 0.54219  0.709962 -0.0133666  0.0610241   0.0396385   53  VAL   B HG21 
590  H HG22 . VAL   A 41  ? 0.566527 0.572918 0.763608 0.0132073   0.0550073   0.0508943   53  VAL   B HG22 
591  H HG23 . VAL   A 41  ? 0.563942 0.575783 0.776586 -0.00707706 0.0768898   0.0374352   53  VAL   B HG23 
592  N N    . TYR   A 42  ? 0.463903 0.601833 0.817894 -0.0232956  -0.00090544 0.0283944   54  TYR   B N    
593  C CA   . TYR   A 42  ? 0.464858 0.632139 0.861283 -0.0399246  -0.0246782  0.0188094   54  TYR   B CA   
594  C C    . TYR   A 42  ? 0.42165  0.561749 0.793193 -0.0691602  -0.00125166 0.0134454   54  TYR   B C    
595  O O    . TYR   A 42  ? 0.409198 0.538984 0.789196 -0.0778689  0.0399027   0.015804    54  TYR   B O    
596  C CB   . TYR   A 42  ? 0.496962 0.719326 0.998361 -0.0351028  -0.0238936  0.0177453   54  TYR   B CB   
597  C CG   . TYR   A 42  ? 0.523716 0.775555 1.05742  -0.00178673 -0.0474806  0.0254258   54  TYR   B CG   
598  C CD1  . TYR   A 42  ? 0.544921 0.780073 1.06642  0.0204123   -0.0199267  0.0370749   54  TYR   B CD1  
599  C CD2  . TYR   A 42  ? 0.527211 0.818173 1.09819  0.00942674  -0.0993065  0.02075     54  TYR   B CD2  
600  C CE1  . TYR   A 42  ? 0.552482 0.806924 1.09808  0.0538297   -0.0395604  0.0477081   54  TYR   B CE1  
601  C CE2  . TYR   A 42  ? 0.581399 0.895167 1.17259  0.0443274   -0.123299   0.0307344   54  TYR   B CE2  
602  C CZ   . TYR   A 42  ? 0.595287 0.889672 1.17353  0.0673074   -0.0917475  0.046273    54  TYR   B CZ   
603  O OH   . TYR   A 42  ? 0.637508 0.948144 1.23283  0.104187    -0.113337   0.059411    54  TYR   B OH   
604  H H    . TYR   A 42  ? 0.477143 0.609684 0.842992 -0.0253436  0.0276982   0.0290413   54  TYR   B H    
605  H HA   . TYR   A 42  ? 0.465639 0.633447 0.840088 -0.033939   -0.0565155  0.0167728   54  TYR   B HA   
606  H HB2  . TYR   A 42  ? 0.493243 0.712771 1.01367  -0.0410853  0.0117569   0.0196278   54  TYR   B HB2  
607  H HB3  . TYR   A 42  ? 0.493855 0.736364 1.02966  -0.0487456  -0.0415141  0.00990245  54  TYR   B HB3  
608  H HD1  . TYR   A 42  ? 0.538498 0.745032 1.03146  0.0132972   0.0118399   0.0375557   54  TYR   B HD1  
609  H HD2  . TYR   A 42  ? 0.538885 0.83834  1.11846  -0.00588595 -0.120125   0.0103302   54  TYR   B HD2  
610  H HE1  . TYR   A 42  ? 0.568812 0.80669  1.10595  0.0682561   -0.0189741  0.0555666   54  TYR   B HE1  
611  H HE2  . TYR   A 42  ? 0.587724 0.926766 1.19824  0.0533209   -0.162181   0.0267769   54  TYR   B HE2  
613  N N    . VAL   A 43  ? 0.426585 0.55038  0.76222  -0.0817545  -0.0256773  0.0068632   55  VAL   B N    
614  C CA   . VAL   A 43  ? 0.451047 0.544622 0.760842 -0.106366   -0.00561928 0.00461832  55  VAL   B CA   
615  C C    . VAL   A 43  ? 0.474556 0.577593 0.815486 -0.124479   -0.0321983  -0.00627455 55  VAL   B C    
616  O O    . VAL   A 43  ? 0.469186 0.590605 0.821257 -0.116331   -0.0737126  -0.0152644  55  VAL   B O    
617  C CB   . VAL   A 43  ? 0.452319 0.498052 0.670974 -0.104789   -0.00108495 0.00808949  55  VAL   B CB   
618  C CG1  . VAL   A 43  ? 0.46166  0.493287 0.648706 -0.0897198  0.0186677   0.0149205   55  VAL   B CG1  
619  C CG2  . VAL   A 43  ? 0.457906 0.494602 0.637405 -0.0974539  -0.0386864  0.00340257  55  VAL   B CG2  
620  H H    . VAL   A 43  ? 0.432554 0.561185 0.756415 -0.0732013  -0.054608   0.00418608  55  VAL   B H    
621  H HA   . VAL   A 43  ? 0.454676 0.550705 0.788536 -0.112977   0.023823    0.00778944  55  VAL   B HA   
622  H HB   . VAL   A 43  ? 0.466199 0.492992 0.671845 -0.118946   0.0148273   0.0084817   55  VAL   B HB   
623  H HG11 . VAL   A 43  ? 0.451683 0.498028 0.650292 -0.0749961  0.00582012  0.0169414   55  VAL   B HG11 
624  H HG12 . VAL   A 43  ? 0.464658 0.496864 0.669071 -0.0931828  0.0441072   0.0161097   55  VAL   B HG12 
625  H HG13 . VAL   A 43  ? 0.459594 0.465137 0.597839 -0.0907978  0.0189981   0.0158683   55  VAL   B HG13 
626  H HG21 . VAL   A 43  ? 0.456457 0.468243 0.587783 -0.0948682  -0.0338564  0.00665879  55  VAL   B HG21 
627  H HG22 . VAL   A 43  ? 0.464955 0.5015   0.656446 -0.108876   -0.0500981  -0.00323768 55  VAL   B HG22 
628  H HG23 . VAL   A 43  ? 0.454141 0.508374 0.644141 -0.0829178  -0.0553855  0.00377989  55  VAL   B HG23 
629  N N    . HIS   A 44  ? 0.504517 0.58767  0.851769 -0.148567   -0.00733259 -0.00554447 56  HIS   B N    
630  C CA   . HIS   A 44  ? 0.542388 0.604343 0.880253 -0.166645   -0.0267168  -0.0143005  56  HIS   B CA   
631  C C    . HIS   A 44  ? 0.54289  0.550326 0.789214 -0.166277   -0.0152215  -0.00782616 56  HIS   B C    
632  O O    . HIS   A 44  ? 0.52761  0.515819 0.734921 -0.161557   0.0151091   0.00310559  56  HIS   B O    
633  C CB   . HIS   A 44  ? 0.583343 0.658736 1.00129  -0.194512   -0.0083778  -0.016117   56  HIS   B CB   
634  C CG   . HIS   A 44  ? 0.550159 0.680422 1.06479  -0.198683   -0.0413808  -0.0300302  56  HIS   B CG   
635  N ND1  . HIS   A 44  ? 0.557272 0.693603 1.0641   -0.193128   -0.0964447  -0.0478169  56  HIS   B ND1  
636  C CD2  . HIS   A 44  ? 0.508033 0.690223 1.1276   -0.205366   -0.0296852  -0.0297589  56  HIS   B CD2  
637  C CE1  . HIS   A 44  ? 0.542262 0.732963 1.14468  -0.196786   -0.122561   -0.0590459  56  HIS   B CE1  
638  N NE2  . HIS   A 44  ? 0.509475 0.731881 1.18718  -0.204231   -0.0822563  -0.0474809  56  HIS   B NE2  
639  H H    . HIS   A 44  ? 0.50878  0.587854 0.863733 -0.152869   0.0241471   0.00106274  56  HIS   B H    
640  H HA   . HIS   A 44  ? 0.539792 0.612894 0.878796 -0.159371   -0.0609443  -0.0235981  56  HIS   B HA   
641  H HB2  . HIS   A 44  ? 0.57268  0.648818 1.0027   -0.197022   0.0273016   -0.00612392 56  HIS   B HB2  
642  H HB3  . HIS   A 44  ? 0.588413 0.633472 0.983082 -0.207247   -0.00894467 -0.0177353  56  HIS   B HB3  
644  H HD2  . HIS   A 44  ? 0.515569 0.70543  1.16241  -0.208314   0.00725258  -0.019723   56  HIS   B HD2  
645  H HE1  . HIS   A 44  ? 0.552874 0.757091 1.16675  -0.193477   -0.163296   -0.0733922  56  HIS   B HE1  
647  N N    . TYR   A 45  ? 0.553086 0.535839 0.76461  -0.168621   -0.0425518  -0.0163525  57  TYR   B N    
648  C CA   . TYR   A 45  ? 0.532615 0.467244 0.668456 -0.166948   -0.033858   -0.0099039  57  TYR   B CA   
649  C C    . TYR   A 45  ? 0.542065 0.445603 0.671307 -0.180581   -0.0490535  -0.0186412  57  TYR   B C    
650  O O    . TYR   A 45  ? 0.561071 0.479057 0.733922 -0.189041   -0.0747195  -0.0340728  57  TYR   B O    
651  C CB   . TYR   A 45  ? 0.48817  0.41994  0.567525 -0.142462   -0.0477602  -0.00799068 57  TYR   B CB   
652  C CG   . TYR   A 45  ? 0.496393 0.4322   0.561963 -0.12979    -0.0851415  -0.0201692  57  TYR   B CG   
653  C CD1  . TYR   A 45  ? 0.49799  0.469221 0.597126 -0.119501   -0.109023   -0.0275225  57  TYR   B CD1  
654  C CD2  . TYR   A 45  ? 0.489861 0.390984 0.505629 -0.125797   -0.0965772  -0.0245813  57  TYR   B CD2  
655  C CE1  . TYR   A 45  ? 0.499155 0.467238 0.570864 -0.105067   -0.143887   -0.0393608  57  TYR   B CE1  
656  C CE2  . TYR   A 45  ? 0.51719  0.415219 0.510914 -0.112267   -0.127038   -0.0374819  57  TYR   B CE2  
657  C CZ   . TYR   A 45  ? 0.51046  0.440156 0.526105 -0.10149    -0.150778   -0.0449347  57  TYR   B CZ   
658  O OH   . TYR   A 45  ? 0.510547 0.429023 0.488308 -0.0855401  -0.180466   -0.0580993  57  TYR   B OH   
659  H H    . TYR   A 45  ? 0.550879 0.546641 0.786301 -0.170005   -0.0677913  -0.0270277  57  TYR   B H    
660  H HA   . TYR   A 45  ? 0.536347 0.458655 0.66344  -0.172314   -0.00613729 -0.0001249  57  TYR   B HA   
661  H HB2  . TYR   A 45  ? 0.500009 0.40593  0.537792 -0.141076   -0.0382269  -0.00211066 57  TYR   B HB2  
662  H HB3  . TYR   A 45  ? 0.479462 0.430385 0.571009 -0.135024   -0.0397219  -0.00391104 57  TYR   B HB3  
663  H HD1  . TYR   A 45  ? 0.479432 0.475484 0.616549 -0.120038   -0.101419   -0.0241036  57  TYR   B HD1  
664  H HD2  . TYR   A 45  ? 0.504866 0.382397 0.499226 -0.130732   -0.083049   -0.0188069  57  TYR   B HD2  
665  H HE1  . TYR   A 45  ? 0.504187 0.494401 0.592293 -0.0957284  -0.162264   -0.0434359  57  TYR   B HE1  
666  H HE2  . TYR   A 45  ? 0.530673 0.403602 0.490067 -0.107712   -0.131491   -0.0406705  57  TYR   B HE2  
668  N N    . LYS   A 46  ? 0.555843 0.414062 0.629119 -0.181344   -0.0346518  -0.00934595 58  LYS   B N    
669  C CA   . LYS   A 46  ? 0.593945 0.411877 0.639704 -0.185103   -0.0490758  -0.0157024  58  LYS   B CA   
670  C C    . LYS   A 46  ? 0.581858 0.374732 0.554106 -0.163865   -0.0510284  -0.00806776 58  LYS   B C    
671  O O    . LYS   A 46  ? 0.620897 0.407367 0.564077 -0.158765   -0.0308529  0.00636892  58  LYS   B O    
672  C CB   . LYS   A 46  ? 0.700781 0.487029 0.769711 -0.209703   -0.023563   -0.00768553 58  LYS   B CB   
673  C CG   . LYS   A 46  ? 0.741746 0.554165 0.899338 -0.233774   -0.0279309  -0.0196999  58  LYS   B CG   
674  C CD   . LYS   A 46  ? 0.793814 0.604347 1.00521  -0.258462   0.0139072   -0.00538863 58  LYS   B CD   
675  C CE   . LYS   A 46  ? 0.837831 0.586485 1.01651  -0.270482   0.039805    0.00947313  58  LYS   B CE   
676  N NZ   . LYS   A 46  ? 0.880246 0.626817 1.13181  -0.299987   0.074682    0.0183122   58  LYS   B NZ   
677  H H    . LYS   A 46  ? 0.556278 0.407169 0.606499 -0.177982   -0.0152703  0.00134966  58  LYS   B H    
678  H HA   . LYS   A 46  ? 0.605712 0.433654 0.667957 -0.184225   -0.0738165  -0.0301776  58  LYS   B HA   
679  H HB2  . LYS   A 46  ? 0.692429 0.473736 0.748671 -0.210257   0.00239004  0.00655317  58  LYS   B HB2  
680  H HB3  . LYS   A 46  ? 0.71527  0.466033 0.753989 -0.208952   -0.0286809  -0.00806873 58  LYS   B HB3  
681  H HG2  . LYS   A 46  ? 0.761765 0.556406 0.922717 -0.239476   -0.0477224  -0.0320691  58  LYS   B HG2  
682  H HG3  . LYS   A 46  ? 0.712201 0.563234 0.895587 -0.227096   -0.0424439  -0.0272585  58  LYS   B HG3  
683  H HD2  . LYS   A 46  ? 0.784791 0.621289 1.06362  -0.272817   0.0052389   -0.0159281  58  LYS   B HD2  
684  H HD3  . LYS   A 46  ? 0.76913  0.595808 0.974646 -0.251458   0.0343066   0.00505891  58  LYS   B HD3  
685  H HE2  . LYS   A 46  ? 0.845039 0.575697 0.968891 -0.258135   0.0563798   0.0238377   58  LYS   B HE2  
686  H HE3  . LYS   A 46  ? 0.857065 0.580738 1.017    -0.269497   0.0185329   0.00023391  58  LYS   B HE3  
687  H HZ1  . LYS   A 46  ? 0.864956 0.635498 1.13472  -0.299318   0.096366    0.0263901   58  LYS   B HZ1  
688  H HZ2  . LYS   A 46  ? 0.877148 0.64014  1.18501  -0.313516   0.0570349   0.00368847  58  LYS   B HZ2  
689  H HZ3  . LYS   A 46  ? 0.913548 0.617363 1.13726  -0.305153   0.0933948   0.0306542   58  LYS   B HZ3  
690  N N    . GLY   A 47  ? 0.596668 0.377084 0.541011 -0.150406   -0.0760126  -0.0192512  59  GLY   B N    
691  C CA   . GLY   A 47  ? 0.607461 0.373158 0.496601 -0.128394   -0.0782448  -0.0129426  59  GLY   B CA   
692  C C    . GLY   A 47  ? 0.643518 0.363596 0.502992 -0.124455   -0.086092   -0.0177954  59  GLY   B C    
693  O O    . GLY   A 47  ? 0.694729 0.397538 0.571837 -0.135359   -0.0988278  -0.0329639  59  GLY   B O    
694  H H    . GLY   A 47  ? 0.610593 0.391975 0.572576 -0.154679   -0.0921406  -0.0320786  59  GLY   B H    
695  H HA2  . GLY   A 47  ? 0.594911 0.359894 0.471858 -0.127444   -0.0633792  -0.00093246 59  GLY   B HA2  
696  H HA3  . GLY   A 47  ? 0.586694 0.372229 0.470977 -0.115725   -0.0889738  -0.0174058  59  GLY   B HA3  
697  N N    . LYS   A 48  ? 0.634462 0.33585  0.453333 -0.108145   -0.0804001  -0.00641095 60  LYS   B N    
698  C CA   . LYS   A 48  ? 0.700593 0.360803 0.489627 -0.096112   -0.0876247  -0.0103285  60  LYS   B CA   
699  C C    . LYS   A 48  ? 0.69645  0.362281 0.455359 -0.0707554  -0.0863795  5.384e-05   60  LYS   B C    
700  O O    . LYS   A 48  ? 0.675521 0.367147 0.43559  -0.0683676  -0.0794653  0.0118361   60  LYS   B O    
701  C CB   . LYS   A 48  ? 0.73602  0.346893 0.522174 -0.11033    -0.0770771  -0.00321865 60  LYS   B CB   
702  C CG   . LYS   A 48  ? 0.773423 0.372867 0.539672 -0.110592   -0.0584311  0.0205113   60  LYS   B CG   
703  C CD   . LYS   A 48  ? 0.862139 0.411574 0.623997 -0.126515   -0.0406842  0.0333492   60  LYS   B CD   
704  C CE   . LYS   A 48  ? 0.937555 0.437122 0.661928 -0.108562   -0.0449832  0.040678    60  LYS   B CE   
705  N NZ   . LYS   A 48  ? 1.00272  0.443955 0.718073 -0.121468   -0.0264252  0.0558464   60  LYS   B NZ   
706  H H    . LYS   A 48  ? 0.625472 0.340216 0.43742  -0.103766   -0.0726403  0.00327101  60  LYS   B H    
707  H HA   . LYS   A 48  ? 0.704962 0.363863 0.495797 -0.0931351  -0.100698   -0.0252675  60  LYS   B HA   
708  H HB2  . LYS   A 48  ? 0.773415 0.355725 0.541719 -0.100648   -0.0834444  -0.00821699 60  LYS   B HB2  
709  H HB3  . LYS   A 48  ? 0.753331 0.363601 0.568029 -0.128662   -0.076255   -0.00989483 60  LYS   B HB3  
710  H HG2  . LYS   A 48  ? 0.74554  0.374113 0.522993 -0.115698   -0.0524667  0.023742    60  LYS   B HG2  
711  H HG3  . LYS   A 48  ? 0.774214 0.37053  0.515926 -0.0927259  -0.0629603  0.0259518   60  LYS   B HG3  
712  H HD2  . LYS   A 48  ? 0.869166 0.413938 0.661445 -0.143455   -0.0397199  0.0239399   60  LYS   B HD2  
713  H HD3  . LYS   A 48  ? 0.860191 0.412876 0.613881 -0.130747   -0.0264169  0.0467293   60  LYS   B HD3  
714  H HE2  . LYS   A 48  ? 0.922195 0.430326 0.622562 -0.0920085  -0.0477567  0.0501652   60  LYS   B HE2  
715  H HE3  . LYS   A 48  ? 0.933166 0.428645 0.661782 -0.102079   -0.0576274  0.0261439   60  LYS   B HE3  
716  H HZ1  . LYS   A 48  ? 1.00586  0.448479 0.71277  -0.126842   -0.0123459  0.0697033   60  LYS   B HZ1  
717  H HZ2  . LYS   A 48  ? 1.01302  0.444788 0.756227 -0.137891   -0.0248009  0.045842    60  LYS   B HZ2  
718  H HZ3  . LYS   A 48  ? 1.03105  0.442001 0.721382 -0.107176   -0.029749   0.0618826   60  LYS   B HZ3  
719  N N    . LEU   A 49  ? 0.752552 0.394328 0.489278 -0.0519047  -0.0935041  -0.00686112 61  LEU   B N    
720  C CA   . LEU   A 49  ? 0.732321 0.377135 0.451802 -0.0269054  -0.090982   0.00299609  61  LEU   B CA   
721  C C    . LEU   A 49  ? 0.819175 0.430654 0.525655 -0.0268794  -0.086639   0.0184546   61  LEU   B C    
722  O O    . LEU   A 49  ? 0.841141 0.411546 0.542725 -0.0405366  -0.0837525  0.0179884   61  LEU   B O    
723  C CB   . LEU   A 49  ? 0.748677 0.375858 0.448779 -0.00410003 -0.0953682  -0.0103406  61  LEU   B CB   
724  C CG   . LEU   A 49  ? 0.726542 0.368218 0.42036  -0.00063683 -0.102589   -0.028172   61  LEU   B CG   
725  C CD1  . LEU   A 49  ? 0.78611  0.404934 0.447525 0.0283921   -0.100784   -0.038512   61  LEU   B CD1  
726  C CD2  . LEU   A 49  ? 0.677932 0.370071 0.388395 -0.00181938 -0.0985875  -0.0203598  61  LEU   B CD2  
727  H H    . LEU   A 49  ? 0.764472 0.387015 0.499454 -0.0546113  -0.10021    -0.0192634  61  LEU   B H    
728  H HA   . LEU   A 49  ? 0.711104 0.38873  0.439802 -0.0241255  -0.088482   0.00873881  61  LEU   B HA   
729  H HB2  . LEU   A 49  ? 0.783361 0.373026 0.473082 -0.00509516 -0.0973749  -0.0149222  61  LEU   B HB2  
730  H HB3  . LEU   A 49  ? 0.740144 0.378175 0.438232 0.0129997   -0.0908526  -0.00238086 61  LEU   B HB3  
731  H HG   . LEU   A 49  ? 0.749041 0.376691 0.447175 -0.0158433  -0.11123    -0.0391979  61  LEU   B HG   
732  H HD11 . LEU   A 49  ? 0.816333 0.398173 0.46692  0.0289093   -0.103767   -0.0453366  61  LEU   B HD11 
733  H HD12 . LEU   A 49  ? 0.789316 0.41286  0.437133 0.0326509   -0.106066   -0.0497396  61  LEU   B HD12 
734  H HD13 . LEU   A 49  ? 0.766649 0.40153  0.431498 0.0432518   -0.0905887  -0.027124   61  LEU   B HD13 
735  H HD21 . LEU   A 49  ? 0.658187 0.36153  0.387311 -0.0193231  -0.0990424  -0.0165244  61  LEU   B HD21 
736  H HD22 . LEU   A 49  ? 0.662676 0.369928 0.376365 0.00943314  -0.0900666  -0.0096557  61  LEU   B HD22 
737  H HD23 . LEU   A 49  ? 0.68647  0.383238 0.386095 0.00441694  -0.103599   -0.0297564  61  LEU   B HD23 
738  N N    . SER   A 50  ? 0.882197 0.509404 0.584339 -0.0103108  -0.0873716  0.0322946   62  SER   B N    
739  C CA   . SER   A 50  ? 0.95095  0.544982 0.632513 -0.0017027  -0.0887257  0.0485174   62  SER   B CA   
740  C C    . SER   A 50  ? 0.901536 0.447436 0.568386 0.0149942   -0.0895161  0.0456816   62  SER   B C    
741  O O    . SER   A 50  ? 0.953349 0.45608  0.599556 0.0199217   -0.0886707  0.0592623   62  SER   B O    
742  C CB   . SER   A 50  ? 0.964513 0.592284 0.651189 0.0140004   -0.0972283  0.0603457   62  SER   B CB   
743  O OG   . SER   A 50  ? 1.00006  0.668786 0.714337 0.0290326   -0.0983323  0.0532669   62  SER   B OG   
744  H H    . SER   A 50  ? 0.840225 0.499223 0.553553 -0.0037743  -0.0881518  0.0320289   62  SER   B H    
745  H HA   . SER   A 50  ? 0.942775 0.520247 0.616122 -0.0173695  -0.0835031  0.0540046   62  SER   B HA   
746  H HB2  . SER   A 50  ? 1.00367  0.60944  0.67626  0.0263742   -0.102103   0.0700018   62  SER   B HB2  
747  H HB3  . SER   A 50  ? 0.958678 0.600468 0.644312 0.00185566  -0.0968265  0.0635585   62  SER   B HB3  
749  N N    . ASN   A 51  ? 0.93258  0.478985 0.603673 0.0258594   -0.0898998  0.0281021   63  ASN   B N    
750  C CA   . ASN   A 51  ? 0.966262 0.463342 0.620238 0.0453686   -0.0892483  0.0222008   63  ASN   B CA   
751  C C    . ASN   A 51  ? 0.996702 0.437812 0.640715 0.0232001   -0.0884441  0.0110113   63  ASN   B C    
752  O O    . ASN   A 51  ? 1.05356  0.440864 0.681652 0.0348392   -0.0875904  0.00429395  63  ASN   B O    
753  C CB   . ASN   A 51  ? 0.945421 0.462195 0.600503 0.0710907   -0.0864271  0.00912435  63  ASN   B CB   
754  C CG   . ASN   A 51  ? 0.924823 0.442793 0.570525 0.0608515   -0.0884536  -0.0149087  63  ASN   B CG   
755  O OD1  . ASN   A 51  ? 0.854958 0.363899 0.504239 0.0328063   -0.095385   -0.0236125  63  ASN   B OD1  
756  N ND2  . ASN   A 51  ? 0.900847 0.429544 0.534379 0.0850153   -0.0823213  -0.0253783  63  ASN   B ND2  
757  H H    . ASN   A 51  ? 0.892468 0.467192 0.573414 0.0229356   -0.0899087  0.0197956   63  ASN   B H    
758  H HA   . ASN   A 51  ? 0.98166  0.467312 0.630771 0.0579407   -0.0899557  0.0365122   63  ASN   B HA   
759  H HB2  . ASN   A 51  ? 0.981564 0.468666 0.626466 0.0895819   -0.0841249  0.00852874  63  ASN   B HB2  
760  H HB3  . ASN   A 51  ? 0.910505 0.467889 0.58187  0.0787543   -0.0849785  0.0176076   63  ASN   B HB3  
761  H HD21 . ASN   A 51  ? 0.915992 0.44434  0.537064 0.0820348   -0.0852512  -0.038952   63  ASN   B HD21 
762  H HD22 . ASN   A 51  ? 0.913336 0.449455 0.550811 0.105017    -0.0747305  -0.0182862  63  ASN   B HD22 
763  N N    . GLY   A 52  ? 1.01382  0.468241 0.673754 -0.00873848 -0.0877148  0.0079792   64  GLY   B N    
764  C CA   . GLY   A 52  ? 1.05636  0.465843 0.724285 -0.0357722  -0.0850378  0.0001683   64  GLY   B CA   
765  C C    . GLY   A 52  ? 1.08607  0.475883 0.757109 -0.0401596  -0.0976126  -0.0320526  64  GLY   B C    
766  O O    . GLY   A 52  ? 1.10825  0.454441 0.791572 -0.0617531  -0.0990069  -0.0432741  64  GLY   B O    
767  H H    . GLY   A 52  ? 0.96387  0.457942 0.63494  -0.0140198  -0.0879735  0.0105866   64  GLY   B H    
768  H HA2  . GLY   A 52  ? 1.03326  0.463163 0.718122 -0.0554453  -0.0807147  0.00496468  64  GLY   B HA2  
769  H HA3  . GLY   A 52  ? 1.09592  0.464653 0.751111 -0.032153   -0.0788411  0.0117394   64  GLY   B HA3  
770  N N    . LYS   A 53  ? 1.05951  0.478935 0.718021 -0.0199791  -0.106794   -0.0475699  65  LYS   B N    
771  C CA   . LYS   A 53  ? 1.1141   0.504103 0.754318 -0.0139064  -0.120455   -0.079151   65  LYS   B CA   
772  C C    . LYS   A 53  ? 1.07543  0.507038 0.728293 -0.0278358  -0.137104   -0.0978375  65  LYS   B C    
773  O O    . LYS   A 53  ? 1.11425  0.524783 0.745411 -0.022512   -0.154097   -0.126384   65  LYS   B O    
774  C CB   . LYS   A 53  ? 1.11316  0.488641 0.716247 0.026682    -0.114337   -0.0822666  65  LYS   B CB   
775  H H    . LYS   A 53  ? 1.02628  0.482805 0.685219 -0.00953478 -0.103938   -0.0384133  65  LYS   B H    
776  H HA   . LYS   A 53  ? 1.14739  0.493582 0.791143 -0.0265688  -0.122576   -0.0867419  65  LYS   B HA   
779  N N    . LYS   A 54  ? 1.06696  0.553886 0.750334 -0.0427074  -0.133991   -0.083059   66  LYS   B N    
780  C CA   . LYS   A 54  ? 1.05897  0.585507 0.76045  -0.0545875  -0.15078    -0.0977016  66  LYS   B CA   
781  C C    . LYS   A 54  ? 1.01258  0.579334 0.762643 -0.0808047  -0.142313   -0.0808354  66  LYS   B C    
782  O O    . LYS   A 54  ? 0.903494 0.491112 0.655936 -0.0775804  -0.123815   -0.056347   66  LYS   B O    
783  C CB   . LYS   A 54  ? 1.02071  0.580155 0.690578 -0.0265763  -0.154279   -0.100463   66  LYS   B CB   
784  H H    . LYS   A 54  ? 1.03128  0.530294 0.723013 -0.0439405  -0.121983   -0.0636849  66  LYS   B H    
785  H HA   . LYS   A 54  ? 1.08865  0.591298 0.792568 -0.0641968  -0.165918   -0.118162   66  LYS   B HA   
788  N N    . PHE   A 55  ? 0.923471 0.499974 0.713884 -0.106094   -0.157134   -0.0964462  67  PHE   B N    
789  C CA   . PHE   A 55  ? 0.911758 0.52783  0.755498 -0.129997   -0.147751   -0.0844359  67  PHE   B CA   
790  C C    . PHE   A 55  ? 0.927028 0.589632 0.798802 -0.132465   -0.171447   -0.100347   67  PHE   B C    
791  O O    . PHE   A 55  ? 1.00351  0.658835 0.85506  -0.122224   -0.1999     -0.124461   67  PHE   B O    
792  C CB   . PHE   A 55  ? 0.951348 0.536748 0.837753 -0.161657   -0.137779   -0.0838283  67  PHE   B CB   
793  C CG   . PHE   A 55  ? 1.06035  0.586781 0.914756 -0.157985   -0.118256   -0.0689691  67  PHE   B CG   
794  C CD1  . PHE   A 55  ? 1.19526  0.668438 1.01604  -0.145898   -0.13018    -0.0849209  67  PHE   B CD1  
795  C CD2  . PHE   A 55  ? 1.0624   0.581332 0.917241 -0.1651     -0.0884604  -0.0397474  67  PHE   B CD2  
796  C CE1  . PHE   A 55  ? 1.2893   0.705433 1.0841   -0.140079   -0.112838   -0.0696462  67  PHE   B CE1  
797  C CE2  . PHE   A 55  ? 1.17607  0.637389 0.997593 -0.158697   -0.0734956  -0.0238276  67  PHE   B CE2  
798  C CZ   . PHE   A 55  ? 1.27605  0.687499 1.07069  -0.145565   -0.0857494  -0.0375132  67  PHE   B CZ   
799  H H    . PHE   A 55  ? 0.986497 0.544439 0.772746 -0.107747   -0.174116   -0.116529   67  PHE   B H    
800  H HA   . PHE   A 55  ? 0.882125 0.514195 0.718083 -0.123463   -0.131265   -0.0655808  67  PHE   B HA   
801  H HB2  . PHE   A 55  ? 0.991515 0.568786 0.897599 -0.172051   -0.156666   -0.104552   67  PHE   B HB2  
802  H HB3  . PHE   A 55  ? 0.939428 0.551163 0.858583 -0.174797   -0.124929   -0.0724788  67  PHE   B HB3  
803  H HD1  . PHE   A 55  ? 1.1986   0.672026 1.01136  -0.139852   -0.150213   -0.10628    67  PHE   B HD1  
804  H HD2  . PHE   A 55  ? 1.04545  0.596234 0.919405 -0.172303   -0.0785313  -0.0304756  67  PHE   B HD2  
805  H HE1  . PHE   A 55  ? 1.31224  0.690847 1.08467  -0.129708   -0.119726   -0.0807938  67  PHE   B HE1  
806  H HE2  . PHE   A 55  ? 1.17261  0.626962 0.986034 -0.160878   -0.0549067  -0.00332926 67  PHE   B HE2  
807  H HZ   . PHE   A 55  ? 1.29625  0.667468 1.06942  -0.139059   -0.0756318  -0.0253534  67  PHE   B HZ   
808  N N    . ASP   A 56  ? 0.855883 0.56395  0.77103  -0.143751   -0.16034    -0.0870167  68  ASP   B N    
809  C CA   . ASP   A 56  ? 0.882286 0.638615 0.825208 -0.140529   -0.181302   -0.0965542  68  ASP   B CA   
810  C C    . ASP   A 56  ? 0.873246 0.668907 0.879009 -0.159159   -0.161345   -0.0817568  68  ASP   B C    
811  O O    . ASP   A 56  ? 0.866822 0.663458 0.861508 -0.157688   -0.131014   -0.0599278  68  ASP   B O    
812  C CB   . ASP   A 56  ? 0.867253 0.639564 0.757908 -0.108178   -0.184668   -0.090369   68  ASP   B CB   
813  C CG   . ASP   A 56  ? 0.859652 0.681253 0.773051 -0.0998563  -0.196688   -0.0886612  68  ASP   B CG   
814  O OD1  . ASP   A 56  ? 0.854329 0.691233 0.793092 -0.103631   -0.228336   -0.107797   68  ASP   B OD1  
815  O OD2  . ASP   A 56  ? 0.778315 0.621114 0.684411 -0.0885627  -0.176503   -0.0687759  68  ASP   B OD2  
816  H H    . ASP   A 56  ? 0.858339 0.565511 0.783581 -0.151785   -0.139118   -0.0714025  68  ASP   B H    
817  H HA   . ASP   A 56  ? 0.908285 0.659064 0.864502 -0.146793   -0.20503    -0.116319   68  ASP   B HA   
818  H HB2  . ASP   A 56  ? 0.902169 0.652019 0.755778 -0.095443   -0.198403   -0.10254    68  ASP   B HB2  
819  H HB3  . ASP   A 56  ? 0.847273 0.616136 0.72177  -0.102734   -0.163491   -0.0741038  68  ASP   B HB3  
820  N N    . SER   A 57  ? 0.842947 0.671358 0.914086 -0.17454    -0.17983    -0.0952404  69  SER   B N    
821  C CA   . SER   A 57  ? 0.820575 0.691135 0.960774 -0.189518   -0.159612   -0.0830548  69  SER   B CA   
822  C C    . SER   A 57  ? 0.843114 0.765951 1.02622  -0.181216   -0.191319   -0.0953271  69  SER   B C    
823  O O    . SER   A 57  ? 0.918797 0.841819 1.10993  -0.181709   -0.232147   -0.119678   69  SER   B O    
824  C CB   . SER   A 57  ? 0.913189 0.770452 1.11584  -0.223263   -0.141092   -0.0829034  69  SER   B CB   
825  O OG   . SER   A 57  ? 0.879298 0.779516 1.15285  -0.235837   -0.116163   -0.0708658  69  SER   B OG   
826  H H    . SER   A 57  ? 0.878602 0.703371 0.952678 -0.174778   -0.206628   -0.113636   69  SER   B H    
827  H HA   . SER   A 57  ? 0.811345 0.684293 0.929279 -0.181169   -0.13629    -0.0660865  69  SER   B HA   
828  H HB2  . SER   A 57  ? 0.90552  0.7262   1.07479  -0.225701   -0.120879   -0.0725626  69  SER   B HB2  
829  H HB3  . SER   A 57  ? 0.920662 0.773339 1.14846  -0.233544   -0.165423   -0.101421   69  SER   B HB3  
831  N N    . SER   A 58  ? 0.76915  0.732089 0.977547 -0.172579   -0.173654   -0.0793435  70  SER   B N    
832  C CA   . SER   A 58  ? 0.734551 0.751407 0.998571 -0.164275   -0.197713   -0.0853412  70  SER   B CA   
833  C C    . SER   A 58  ? 0.817765 0.86222  1.1776   -0.190409   -0.219361   -0.103934   70  SER   B C    
834  O O    . SER   A 58  ? 0.865898 0.944543 1.25863  -0.182307   -0.263213   -0.120585   70  SER   B O    
835  C CB   . SER   A 58  ? 0.648642 0.695852 0.935567 -0.15542    -0.165155   -0.0643223  70  SER   B CB   
836  O OG   . SER   A 58  ? 0.657112 0.702275 0.987355 -0.17855    -0.122666   -0.0533558  70  SER   B OG   
837  H H    . SER   A 58  ? 0.754095 0.708528 0.942903 -0.170514   -0.146047   -0.0642835  70  SER   B H    
838  H HA   . SER   A 58  ? 0.752491 0.767548 0.976614 -0.145136   -0.223737   -0.0920167  70  SER   B HA   
839  H HB2  . SER   A 58  ? 0.659105 0.741602 0.985008 -0.147642   -0.182216   -0.0676665  70  SER   B HB2  
840  H HB3  . SER   A 58  ? 0.651168 0.682573 0.882596 -0.139681   -0.155872   -0.0548241  70  SER   B HB3  
842  N N    . HIS   A 59  ? 0.852063 0.881954 1.25894  -0.221297   -0.188948   -0.100147   71  HIS   B N    
843  C CA   . HIS   A 59  ? 0.936354 0.992872 1.44938  -0.251361   -0.202939   -0.11619    71  HIS   B CA   
844  C C    . HIS   A 59  ? 1.0323   1.07361  1.53625  -0.254584   -0.261612   -0.149273   71  HIS   B C    
845  O O    . HIS   A 59  ? 0.982857 1.0668   1.56785  -0.264701   -0.300663   -0.170083   71  HIS   B O    
846  C CB   . HIS   A 59  ? 0.958271 0.989578 1.50943  -0.282357   -0.150852   -0.101019   71  HIS   B CB   
847  C CG   . HIS   A 59  ? 0.914278 0.95834  1.46739  -0.276753   -0.0955863  -0.072342   71  HIS   B CG   
848  N ND1  . HIS   A 59  ? 0.987876 0.983893 1.45576  -0.269066   -0.0565653  -0.0514302  71  HIS   B ND1  
849  C CD2  . HIS   A 59  ? 0.910327 1.00748  1.53992  -0.276733   -0.0735558  -0.0630923  71  HIS   B CD2  
850  C CE1  . HIS   A 59  ? 0.963612 0.978911 1.44798  -0.265088   -0.0137675  -0.0324345  71  HIS   B CE1  
851  N NE2  . HIS   A 59  ? 0.903471 0.979285 1.4863   -0.269134   -0.0202562  -0.0386439  71  HIS   B NE2  
852  H H    . HIS   A 59  ? 0.853057 0.85551  1.22656  -0.223658   -0.158536   -0.0866162  71  HIS   B H    
853  H HA   . HIS   A 59  ? 0.915919 1.01966  1.48478  -0.24712    -0.207466   -0.114635   71  HIS   B HA   
854  H HB2  . HIS   A 59  ? 0.971865 0.954938 1.4671   -0.284638   -0.145989   -0.100565   71  HIS   B HB2  
855  H HB3  . HIS   A 59  ? 0.967593 1.01781  1.59772  -0.30435    -0.158427   -0.111403   71  HIS   B HB3  
857  H HD2  . HIS   A 59  ? 0.902383 1.04346  1.60472  -0.280047   -0.0919899  -0.0723507  71  HIS   B HD2  
858  H HE1  . HIS   A 59  ? 0.954943 0.944899 1.38886  -0.259069   0.0146093   -0.0181413  71  HIS   B HE1  
860  N N    . ASP   A 60  ? 1.13528  1.11721  1.53924  -0.242836   -0.270274   -0.155723   72  ASP   B N    
861  C CA   . ASP   A 60  ? 1.25503  1.21055  1.62871  -0.240697   -0.322995   -0.18919    72  ASP   B CA   
862  C C    . ASP   A 60  ? 1.26311  1.26438  1.64057  -0.217359   -0.376473   -0.205949   72  ASP   B C    
863  O O    . ASP   A 60  ? 1.36759  1.37514  1.77614  -0.226165   -0.428152   -0.238303   72  ASP   B O    
864  C CB   . ASP   A 60  ? 1.33689  1.22797  1.59049  -0.218748   -0.320622   -0.190331   72  ASP   B CB   
865  C CG   . ASP   A 60  ? 1.33113  1.17003  1.55087  -0.228382   -0.272698   -0.170418   72  ASP   B CG   
866  O OD1  . ASP   A 60  ? 1.24535  1.06773  1.52534  -0.261179   -0.253765   -0.169603   72  ASP   B OD1  
867  O OD2  . ASP   A 60  ? 1.21711  1.03079  1.35107  -0.201993   -0.256183   -0.155808   72  ASP   B OD2  
868  H H    . ASP   A 60  ? 1.11423  1.07072  1.46711  -0.234978   -0.242343   -0.139542   72  ASP   B H    
869  H HA   . ASP   A 60  ? 1.27624  1.22421  1.70448  -0.267113   -0.328781   -0.202407   72  ASP   B HA   
870  H HB2  . ASP   A 60  ? 1.30311  1.20464  1.50826  -0.192817   -0.321284   -0.180953   72  ASP   B HB2  
871  H HB3  . ASP   A 60  ? 1.36726  1.2375   1.60609  -0.219872   -0.353541   -0.215085   72  ASP   B HB3  
872  N N    . ARG   A 61  ? 1.20704  1.23486  1.54679  -0.186106   -0.366039   -0.184317   73  ARG   B N    
873  C CA   . ARG   A 61  ? 1.14534  1.21264  1.47953  -0.158154   -0.411837   -0.192591   73  ARG   B CA   
874  C C    . ARG   A 61  ? 1.05938  1.19896  1.52209  -0.171955   -0.423323   -0.192921   73  ARG   B C    
875  O O    . ARG   A 61  ? 1.09063  1.26997  1.5711   -0.151941   -0.470108   -0.202881   73  ARG   B O    
876  C CB   . ARG   A 61  ? 1.02523  1.08449  1.26964  -0.119705   -0.39109    -0.166551   73  ARG   B CB   
877  H H    . ARG   A 61  ? 1.16162  1.18021  1.47701  -0.181555   -0.329668   -0.163409   73  ARG   B H    
878  H HA   . ARG   A 61  ? 1.17737  1.22652  1.48147  -0.154199   -0.450392   -0.216025   73  ARG   B HA   
881  N N    . ASN   A 62  ? 0.962575 1.11836  1.51277  -0.203249   -0.378938   -0.180327   74  ASN   B N    
882  C CA   . ASN   A 62  ? 0.910503 1.13534  1.5978   -0.220091   -0.380235   -0.18026    74  ASN   B CA   
883  C C    . ASN   A 62  ? 0.861015 1.1334   1.5554   -0.186595   -0.375674   -0.15965    74  ASN   B C    
884  O O    . ASN   A 62  ? 0.862552 1.19573  1.63927  -0.17931    -0.412006   -0.168006   74  ASN   B O    
885  C CB   . ASN   A 62  ? 0.974784 1.22687  1.74354  -0.240164   -0.442832   -0.216878   74  ASN   B CB   
886  H H    . ASN   A 62  ? 0.962606 1.08501  1.48485  -0.212678   -0.344387   -0.169925   74  ASN   B H    
887  H HA   . ASN   A 62  ? 0.899197 1.1195   1.6259   -0.241557   -0.338266   -0.168598   74  ASN   B HA   
890  N N    . GLU   A 63  ? 0.847787 1.09202  1.46069  -0.166026   -0.331972   -0.132987   75  GLU   B N    
891  C CA   . GLU   A 63  ? 0.799152 1.07979  1.42649  -0.138885   -0.31461    -0.110994   75  GLU   B CA   
892  C C    . GLU   A 63  ? 0.688184 0.927707 1.23593  -0.129131   -0.258849   -0.0856023  75  GLU   B C    
893  O O    . GLU   A 63  ? 0.64655  0.832026 1.10708  -0.131517   -0.248071   -0.0848617  75  GLU   B O    
894  C CB   . GLU   A 63  ? 0.872257 1.17309  1.4647   -0.10046    -0.367139   -0.114684   75  GLU   B CB   
895  C CG   . GLU   A 63  ? 0.915923 1.15975  1.36969  -0.0762673  -0.382888   -0.115138   75  GLU   B CG   
896  C CD   . GLU   A 63  ? 1.02805  1.28151  1.44167  -0.0448806  -0.447622   -0.128464   75  GLU   B CD   
897  O OE1  . GLU   A 63  ? 1.0971   1.30279  1.39463  -0.0221712  -0.455323   -0.126983   75  GLU   B OE1  
898  O OE2  . GLU   A 63  ? 0.975079 1.28263  1.47064  -0.0414654  -0.490543   -0.14017    75  GLU   B OE2  
899  H H    . GLU   A 63  ? 0.840204 1.04116  1.39017  -0.168961   -0.313488   -0.129151   75  GLU   B H    
900  H HA   . GLU   A 63  ? 0.779855 1.09975  1.49738  -0.150973   -0.302367   -0.108945   75  GLU   B HA   
901  H HB2  . GLU   A 63  ? 0.841554 1.16491  1.45264  -0.08415    -0.351217   -0.0985694  75  GLU   B HB2  
902  H HB3  . GLU   A 63  ? 0.886614 1.21722  1.53264  -0.1055     -0.407189   -0.132236   75  GLU   B HB3  
903  H HG2  . GLU   A 63  ? 0.934725 1.14545  1.36025  -0.093142   -0.379111   -0.125307   75  GLU   B HG2  
904  H HG3  . GLU   A 63  ? 0.902309 1.13036  1.3134   -0.062963   -0.35139    -0.0956031  75  GLU   B HG3  
905  N N    . PRO   A 64  ? 0.644738 0.909071 1.22313  -0.116491   -0.223844   -0.0656828  76  PRO   B N    
906  C CA   . PRO   A 64  ? 0.614444 0.841205 1.1162   -0.103866   -0.180287   -0.0454155  76  PRO   B CA   
907  C C    . PRO   A 64  ? 0.603414 0.794604 0.999522 -0.0780128  -0.20166    -0.0424243  76  PRO   B C    
908  O O    . PRO   A 64  ? 0.625372 0.831141 1.00949  -0.0564233  -0.245244   -0.0485111  76  PRO   B O    
909  C CB   . PRO   A 64  ? 0.589867 0.854469 1.14908  -0.0875735  -0.156385   -0.0311643  76  PRO   B CB   
910  C CG   . PRO   A 64  ? 0.596823 0.917361 1.28113  -0.105462   -0.164298   -0.0410669  76  PRO   B CG   
911  C CD   . PRO   A 64  ? 0.624213 0.953373 1.3169   -0.113241   -0.224451   -0.0634244  76  PRO   B CD   
912  H HA   . PRO   A 64  ? 0.605468 0.807731 1.09481  -0.121778   -0.15175    -0.0429015  76  PRO   B HA   
913  H HB2  . PRO   A 64  ? 0.597296 0.868883 1.13647  -0.0635321  -0.175983   -0.0270296  76  PRO   B HB2  
914  H HB3  . PRO   A 64  ? 0.579909 0.825109 1.11949  -0.0906297  -0.117462   -0.0210534  76  PRO   B HB3  
915  H HG2  . PRO   A 64  ? 0.590571 0.946006 1.32337  -0.0900212  -0.164906   -0.0356852  76  PRO   B HG2  
916  H HG3  . PRO   A 64  ? 0.590441 0.904295 1.29986  -0.126567   -0.13067    -0.0389173  76  PRO   B HG3  
917  H HD2  . PRO   A 64  ? 0.639283 0.990928 1.33619  -0.0923308  -0.259909   -0.0664338  76  PRO   B HD2  
918  H HD3  . PRO   A 64  ? 0.631963 0.982048 1.39558  -0.136063   -0.22554    -0.0727799  76  PRO   B HD3  
919  N N    . PHE   A 65  ? 0.603023 0.747889 0.924271 -0.079914   -0.171024   -0.0328884  77  PHE   B N    
920  C CA   . PHE   A 65  ? 0.620262 0.736124 0.855442 -0.0546543  -0.174467   -0.0232123  77  PHE   B CA   
921  C C    . PHE   A 65  ? 0.597964 0.723903 0.840953 -0.0360523  -0.149333   -0.00489344 77  PHE   B C    
922  O O    . PHE   A 65  ? 0.570212 0.696917 0.8412   -0.0472082  -0.111968   0.00127599  77  PHE   B O    
923  C CB   . PHE   A 65  ? 0.611094 0.679993 0.780101 -0.0659811  -0.155844   -0.0227114  77  PHE   B CB   
924  C CG   . PHE   A 65  ? 0.646412 0.687173 0.735101 -0.0428189  -0.158348   -0.0141465  77  PHE   B CG   
925  C CD1  . PHE   A 65  ? 0.650572 0.676645 0.690232 -0.0286838  -0.189803   -0.0234453  77  PHE   B CD1  
926  C CD2  . PHE   A 65  ? 0.638628 0.665008 0.701549 -0.0360059  -0.126793   0.00220427  77  PHE   B CD2  
927  C CE1  . PHE   A 65  ? 0.651773 0.651799 0.620668 -0.00671314 -0.183505   -0.0127221  77  PHE   B CE1  
928  C CE2  . PHE   A 65  ? 0.607276 0.611285 0.610471 -0.0172703  -0.124645   0.0117473   77  PHE   B CE2  
929  C CZ   . PHE   A 65  ? 0.640253 0.632011 0.597447 -0.00217351 -0.149797   0.00611429  77  PHE   B CZ   
930  H H    . PHE   A 65  ? 0.595527 0.726961 0.921697 -0.0972721  -0.146912   -0.0317173  77  PHE   B H    
931  H HA   . PHE   A 65  ? 0.638737 0.758709 0.857049 -0.0414779  -0.206809   -0.0296383  77  PHE   B HA   
932  H HB2  . PHE   A 65  ? 0.632232 0.69391  0.804847 -0.0785689  -0.169753   -0.0347046  77  PHE   B HB2  
933  H HB3  . PHE   A 65  ? 0.60165  0.664426 0.779505 -0.0764817  -0.126593   -0.0160335  77  PHE   B HB3  
934  H HD1  . PHE   A 65  ? 0.673321 0.705936 0.728098 -0.0340152  -0.214279   -0.0376103  77  PHE   B HD1  
935  H HD2  . PHE   A 65  ? 0.608282 0.640249 0.697074 -0.0440839  -0.10617    0.00637465  77  PHE   B HD2  
936  H HE1  . PHE   A 65  ? 0.689149 0.676751 0.619765 0.00504237  -0.20177    -0.0188847  77  PHE   B HE1  
937  H HE2  . PHE   A 65  ? 0.604323 0.599963 0.59842  -0.015165   -0.104443   0.0215419   77  PHE   B HE2  
938  H HZ   . PHE   A 65  ? 0.648384 0.624616 0.566067 0.0111142   -0.143399   0.0142056   77  PHE   B HZ   
939  N N    . VAL   A 66  ? 0.630675 0.758826 0.843769 -0.00612006 -0.169222   0.00367315  78  VAL   B N    
940  C CA   . VAL   A 66  ? 0.606809 0.742487 0.833169 0.0148983   -0.150661   0.0210775   78  VAL   B CA   
941  C C    . VAL   A 66  ? 0.605634 0.702463 0.752133 0.0339609   -0.141678   0.0359866   78  VAL   B C    
942  O O    . VAL   A 66  ? 0.590118 0.671214 0.68052  0.0461512   -0.16546    0.034919    78  VAL   B O    
943  C CB   . VAL   A 66  ? 0.632105 0.811227 0.914411 0.0363893   -0.182663   0.0219196   78  VAL   B CB   
944  C CG1  . VAL   A 66  ? 0.669736 0.843163 0.941295 0.0677589   -0.170592   0.0433642   78  VAL   B CG1  
945  C CG2  . VAL   A 66  ? 0.628245 0.852973 1.01316  0.0177469   -0.178185   0.0116964   78  VAL   B CG2  
946  H H    . VAL   A 66  ? 0.644724 0.765609 0.824567 0.00253719  -0.194223   -0.00109212 78  VAL   B H    
947  H HA   . VAL   A 66  ? 0.588829 0.724662 0.840546 0.00343403  -0.121966   0.0229403   78  VAL   B HA   
948  H HB   . VAL   A 66  ? 0.662629 0.843013 0.921654 0.043537    -0.216174   0.0150289   78  VAL   B HB   
949  H HG11 . VAL   A 66  ? 0.642598 0.807795 0.928153 0.0610481   -0.137386   0.0482415   78  VAL   B HG11 
950  H HG12 . VAL   A 66  ? 0.679595 0.82628  0.89052  0.0806389   -0.174793   0.0512769   78  VAL   B HG12 
951  H HG13 . VAL   A 66  ? 0.673421 0.876483 0.985223 0.0824992   -0.191501   0.044453    78  VAL   B HG13 
952  H HG21 . VAL   A 66  ? 0.635028 0.89094  1.06176  0.0334253   -0.198577   0.0131902   78  VAL   B HG21 
953  H HG22 . VAL   A 66  ? 0.623688 0.851508 1.01891  -0.00137707 -0.189718   -0.00141774 78  VAL   B HG22 
954  H HG23 . VAL   A 66  ? 0.60491  0.823509 1.00444  0.00986689  -0.142458   0.0169579   78  VAL   B HG23 
955  N N    . PHE   A 67  ? 0.560313 0.63952  0.702931 0.0360723   -0.105373   0.0488728   79  PHE   B N    
956  C CA   . PHE   A 67  ? 0.557184 0.600379 0.639392 0.0490912   -0.0909192  0.0637866   79  PHE   B CA   
957  C C    . PHE   A 67  ? 0.583448 0.614204 0.684641 0.054703    -0.0581145  0.0758823   79  PHE   B C    
958  O O    . PHE   A 67  ? 0.555815 0.598438 0.703862 0.0452249   -0.0403912  0.0699509   79  PHE   B O    
959  C CB   . PHE   A 67  ? 0.525176 0.54311  0.561858 0.0309241   -0.0835116  0.0569806   79  PHE   B CB   
960  C CG   . PHE   A 67  ? 0.45501  0.459941 0.501262 0.00620607  -0.0540845  0.0514136   79  PHE   B CG   
961  C CD1  . PHE   A 67  ? 0.45027  0.46708  0.528449 -0.0150974  -0.0499808  0.0386066   79  PHE   B CD1  
962  C CD2  . PHE   A 67  ? 0.426024 0.404815 0.447496 0.00449284  -0.0313645  0.0590344   79  PHE   B CD2  
963  C CE1  . PHE   A 67  ? 0.425872 0.425294 0.499128 -0.0332162  -0.023873   0.0348724   79  PHE   B CE1  
964  C CE2  . PHE   A 67  ? 0.423842 0.389621 0.447713 -0.0157888  -0.0114855  0.0513335   79  PHE   B CE2  
965  C CZ   . PHE   A 67  ? 0.39787  0.3719   0.441219 -0.0324278  -0.00763875 0.0399242   79  PHE   B CZ   
966  H H    . PHE   A 67  ? 0.550897 0.639752 0.73102  0.0288423   -0.0883683  0.0477143   79  PHE   B H    
967  H HA   . PHE   A 67  ? 0.588401 0.631389 0.647804 0.0688533   -0.109525   0.0706625   79  PHE   B HA   
968  H HB2  . PHE   A 67  ? 0.533831 0.534098 0.533407 0.0427256   -0.0805447  0.0666753   79  PHE   B HB2  
969  H HB3  . PHE   A 67  ? 0.524406 0.54977  0.557696 0.0256562   -0.102971   0.0465773   79  PHE   B HB3  
970  H HD1  . PHE   A 67  ? 0.446604 0.483069 0.551197 -0.016591   -0.0645614  0.0328592   79  PHE   B HD1  
971  H HD2  . PHE   A 67  ? 0.44838  0.417541 0.452071 0.0175258   -0.0296686  0.0695495   79  PHE   B HD2  
972  H HE1  . PHE   A 67  ? 0.418825 0.423161 0.509377 -0.0458817  -0.0178913  0.0287161   79  PHE   B HE1  
973  H HE2  . PHE   A 67  ? 0.418193 0.368058 0.429757 -0.0175346  -0.00010178 0.0544114   79  PHE   B HE2  
974  H HZ   . PHE   A 67  ? 0.407238 0.368367 0.441881 -0.0437918  0.00506223  0.0355155   79  PHE   B HZ   
975  N N    . SER   A 68  ? 0.654229 0.657271 0.718064 0.0717568   -0.0478178  0.0932947   80  SER   B N    
976  C CA   . SER   A 68  ? 0.63464  0.614186 0.710018 0.075248    -0.016241   0.103726    80  SER   B CA   
977  C C    . SER   A 68  ? 0.553258 0.506364 0.607613 0.0507371   0.00628082  0.0967148   80  SER   B C    
978  O O    . SER   A 68  ? 0.535855 0.476281 0.553326 0.0475913   0.00404308  0.100468    80  SER   B O    
979  C CB   . SER   A 68  ? 0.700128 0.660301 0.753397 0.105549    -0.0149172  0.128345    80  SER   B CB   
980  O OG   . SER   A 68  ? 0.759736 0.746529 0.830909 0.13131     -0.0424021  0.134321    80  SER   B OG   
981  H H    . SER   A 68  ? 0.653143 0.648915 0.682439 0.0815521   -0.0595315  0.0988093   80  SER   B H    
982  H HA   . SER   A 68  ? 0.621948 0.614275 0.735351 0.0737603   -0.0100606  0.0984691   80  SER   B HA   
983  H HB2  . SER   A 68  ? 0.714514 0.660889 0.729357 0.107988    -0.0166442  0.134853    80  SER   B HB2  
984  H HB3  . SER   A 68  ? 0.707993 0.649157 0.772766 0.105956    0.00705053  0.134103    80  SER   B HB3  
986  N N    . LEU   A 69  ? 0.531527 0.477794 0.61007  0.034859    0.0268217   0.0850838   81  LEU   B N    
987  C CA   . LEU   A 69  ? 0.481758 0.40719  0.542075 0.0109538   0.0403647   0.0734646   81  LEU   B CA   
988  C C    . LEU   A 69  ? 0.523911 0.418896 0.571046 0.0129727   0.0546753   0.0840353   81  LEU   B C    
989  O O    . LEU   A 69  ? 0.509159 0.387371 0.570439 0.0270462   0.068313    0.0952626   81  LEU   B O    
990  C CB   . LEU   A 69  ? 0.500207 0.421511 0.580602 -0.00098319 0.0581437   0.0581569   81  LEU   B CB   
991  C CG   . LEU   A 69  ? 0.557576 0.455126 0.611639 -0.0235687  0.067455    0.04324     81  LEU   B CG   
992  C CD1  . LEU   A 69  ? 0.562446 0.470617 0.59262  -0.0374384  0.0511075   0.0381753   81  LEU   B CD1  
993  C CD2  . LEU   A 69  ? 0.588215 0.473295 0.649741 -0.0288789  0.0890397   0.0291217   81  LEU   B CD2  
994  H H    . LEU   A 69  ? 0.528859 0.483288 0.634864 0.0407641   0.0318753   0.0839948   81  LEU   B H    
995  H HA   . LEU   A 69  ? 0.486254 0.419263 0.530455 0.00244836  0.0287676   0.0688482   81  LEU   B HA   
996  H HB2  . LEU   A 69  ? 0.499174 0.441761 0.594945 -0.00211564 0.0522337   0.0540682   81  LEU   B HB2  
997  H HB3  . LEU   A 69  ? 0.522763 0.434952 0.619407 0.00926424  0.070188    0.0619433   81  LEU   B HB3  
998  H HG   . LEU   A 69  ? 0.560628 0.440227 0.606878 -0.0244001  0.0710099   0.0460139   81  LEU   B HG   
999  H HD11 . LEU   A 69  ? 0.548168 0.460292 0.5698   -0.0330138  0.0402416   0.0457122   81  LEU   B HD11 
1000 H HD12 . LEU   A 69  ? 0.56067  0.453853 0.573329 -0.0492016  0.0551808   0.0295314   81  LEU   B HD12 
1001 H HD13 . LEU   A 69  ? 0.549426 0.473709 0.590499 -0.0381189  0.0478315   0.0361147   81  LEU   B HD13 
1002 H HD21 . LEU   A 69  ? 0.597708 0.474626 0.67628  -0.018127   0.100168    0.031936    81  LEU   B HD21 
1003 H HD22 . LEU   A 69  ? 0.577471 0.480542 0.650052 -0.0300819  0.0891127   0.0271868   81  LEU   B HD22 
1004 H HD23 . LEU   A 69  ? 0.593724 0.459344 0.631382 -0.0408641  0.0923833   0.0191904   81  LEU   B HD23 
1005 N N    . GLY   A 70  ? 0.517171 0.40563  0.542943 -0.0009106  0.0521615   0.081292    82  GLY   B N    
1006 C CA   . GLY   A 70  ? 0.52306  0.387775 0.550214 -0.00608445 0.0668938   0.0881075   82  GLY   B CA   
1007 C C    . GLY   A 70  ? 0.592831 0.451071 0.610024 0.014567    0.0728507   0.113831    82  GLY   B C    
1008 O O    . GLY   A 70  ? 0.688769 0.524382 0.717617 0.0121928   0.0921142   0.12455     82  GLY   B O    
1009 H H    . GLY   A 70  ? 0.501205 0.401313 0.515858 -0.00742286 0.0410947   0.075038    82  GLY   B H    
1010 H HA2  . GLY   A 70  ? 0.523821 0.3903   0.544405 -0.0195602  0.0627497   0.0802799   82  GLY   B HA2  
1011 H HA3  . GLY   A 70  ? 0.545862 0.39432  0.587723 -0.00990302 0.0785571   0.0834266   82  GLY   B HA3  
1012 N N    . LYS   A 71  ? 0.597701 0.472177 0.592412 0.0348099   0.0571327   0.123521    83  LYS   B N    
1013 C CA   . LYS   A 71  ? 0.618548 0.480825 0.587999 0.0602921   0.062957    0.149561    83  LYS   B CA   
1014 C C    . LYS   A 71  ? 0.684171 0.553744 0.616143 0.0637976   0.0549904   0.151755    83  LYS   B C    
1015 O O    . LYS   A 71  ? 0.718468 0.580324 0.61203  0.0885763   0.0538017   0.169428    83  LYS   B O    
1016 C CB   . LYS   A 71  ? 0.627835 0.495474 0.593219 0.0879252   0.0499316   0.160543    83  LYS   B CB   
1017 H H    . LYS   A 71  ? 0.580288 0.471758 0.573019 0.0329653   0.0422829   0.113558    83  LYS   B H    
1018 H HA   . LYS   A 71  ? 0.644563 0.486581 0.62481  0.0583921   0.0831335   0.159635    83  LYS   B HA   
1021 N N    . GLY   A 72  ? 0.78153  0.662779 0.71898  0.0419214   0.0493869   0.133629    84  GLY   B N    
1022 C CA   . GLY   A 72  ? 0.813026 0.697595 0.721177 0.0453866   0.0471581   0.134858    84  GLY   B CA   
1023 C C    . GLY   A 72  ? 0.75297  0.646841 0.620304 0.0609552   0.0206649   0.12835     84  GLY   B C    
1024 O O    . GLY   A 72  ? 0.728405 0.617404 0.560372 0.0710997   0.0206221   0.130573    84  GLY   B O    
1025 H H    . GLY   A 72  ? 0.726421 0.611831 0.684309 0.0261801   0.0475216   0.120468    84  GLY   B H    
1026 H HA2  . GLY   A 72  ? 0.766058 0.656552 0.688701 0.0285173   0.0465049   0.123481    84  GLY   B HA2  
1027 H HA3  . GLY   A 72  ? 0.810677 0.683267 0.71191  0.0546321   0.0649811   0.151101    84  GLY   B HA3  
1028 N N    . GLN   A 73  ? 0.638932 0.546173 0.515027 0.0624401   -0.00167876 0.118351    85  GLN   B N    
1029 C CA   . GLN   A 73  ? 0.624095 0.540881 0.470676 0.0742626   -0.0317681  0.108692    85  GLN   B CA   
1030 C C    . GLN   A 73  ? 0.552655 0.478161 0.404028 0.0532643   -0.0455375  0.086182    85  GLN   B C    
1031 O O    . GLN   A 73  ? 0.567011 0.493902 0.392229 0.0600175   -0.0693272  0.0752504   85  GLN   B O    
1032 C CB   . GLN   A 73  ? 0.667498 0.601561 0.53763  0.0830531   -0.0518897  0.106837    85  GLN   B CB   
1033 C CG   . GLN   A 73  ? 0.729635 0.651567 0.591959 0.109059    -0.041807   0.131243    85  GLN   B CG   
1034 C CD   . GLN   A 73  ? 0.745278 0.689748 0.644818 0.118285    -0.0615596  0.128958    85  GLN   B CD   
1035 O OE1  . GLN   A 73  ? 0.734418 0.705722 0.675317 0.101135    -0.0764332  0.10928     85  GLN   B OE1  
1036 N NE2  . GLN   A 73  ? 0.822838 0.756162 0.712398 0.146342    -0.0587957  0.151163    85  GLN   B NE2  
1037 H H    . GLN   A 73  ? 0.642662 0.553449 0.546752 0.0555017   0.00179037  0.116292    85  GLN   B H    
1038 H HA   . GLN   A 73  ? 0.662395 0.567315 0.47064  0.0917925   -0.0307664  0.118005    85  GLN   B HA   
1039 H HB2  . GLN   A 73  ? 0.634596 0.579356 0.541928 0.0666595   -0.0484684  0.0981782   85  GLN   B HB2  
1040 H HB3  . GLN   A 73  ? 0.676706 0.619161 0.532435 0.0886063   -0.0757968  0.0976645   85  GLN   B HB3  
1041 H HG2  . GLN   A 73  ? 0.763917 0.673705 0.583039 0.127858    -0.0457919  0.140944    85  GLN   B HG2  
1042 H HG3  . GLN   A 73  ? 0.718033 0.627415 0.594269 0.102676    -0.0171366  0.139924    85  GLN   B HG3  
1043 H HE21 . GLN   A 73  ? 0.815273 0.763342 0.728167 0.155381    -0.0718109  0.151226    85  GLN   B HE21 
1044 H HE22 . GLN   A 73  ? 0.835195 0.74592  0.696266 0.156845    -0.0430406  0.167063    85  GLN   B HE22 
1045 N N    . VAL   A 74  ? 0.524797 0.451568 0.405305 0.0294838   -0.0319704  0.0793127   86  VAL   B N    
1046 C CA   . VAL   A 74  ? 0.504347 0.431246 0.383132 0.0119736   -0.0395626  0.0636484   86  VAL   B CA   
1047 C C    . VAL   A 74  ? 0.47568  0.393817 0.354151 0.00487167  -0.0218606  0.0679362   86  VAL   B C    
1048 O O    . VAL   A 74  ? 0.507325 0.422039 0.397772 0.00784624  -0.003444   0.0803194   86  VAL   B O    
1049 C CB   . VAL   A 74  ? 0.502269 0.440026 0.415626 -0.00781436 -0.0433634  0.0517342   86  VAL   B CB   
1050 C CG1  . VAL   A 74  ? 0.551271 0.505181 0.477683 -0.00301182 -0.0649425  0.0446265   86  VAL   B CG1  
1051 C CG2  . VAL   A 74  ? 0.491865 0.428889 0.432787 -0.0143626  -0.0233532  0.0567448   86  VAL   B CG2  
1052 H H    . VAL   A 74  ? 0.515253 0.439844 0.414752 0.0251559   -0.0179047  0.0848898   86  VAL   B H    
1053 H HA   . VAL   A 74  ? 0.521495 0.446124 0.378061 0.0189157   -0.05326    0.0584309   86  VAL   B HA   
1054 H HB   . VAL   A 74  ? 0.497842 0.430613 0.407073 -0.0193558  -0.0445144  0.0445062   86  VAL   B HB   
1055 H HG11 . VAL   A 74  ? 0.550108 0.509121 0.478341 0.0111186   -0.066693   0.0525384   86  VAL   B HG11 
1056 H HG12 . VAL   A 74  ? 0.552018 0.502348 0.459307 -0.00061878 -0.0793222  0.0381432   86  VAL   B HG12 
1057 H HG13 . VAL   A 74  ? 0.52607  0.488108 0.479402 -0.0158499  -0.0627958  0.0384634   86  VAL   B HG13 
1058 H HG21 . VAL   A 74  ? 0.481292 0.421524 0.436987 -0.0263587  -0.0218472  0.0488591   86  VAL   B HG21 
1059 H HG22 . VAL   A 74  ? 0.488549 0.416395 0.424485 -0.0173786  -0.0132156  0.06015     86  VAL   B HG22 
1060 H HG23 . VAL   A 74  ? 0.499736 0.440413 0.448325 -0.00281192 -0.0219729  0.0640579   86  VAL   B HG23 
1061 N N    . ILE   A 75  ? 0.470993 0.385794 0.34255  -0.00525814 -0.0283455  0.0576881   87  ILE   B N    
1062 C CA   . ILE   A 75  ? 0.459354 0.372377 0.341128 -0.0129741  -0.0180395  0.0594778   87  ILE   B CA   
1063 C C    . ILE   A 75  ? 0.422131 0.337149 0.332803 -0.0296004  -0.0106246  0.0574639   87  ILE   B C    
1064 O O    . ILE   A 75  ? 0.404624 0.319357 0.321925 -0.0376887  -0.0128489  0.0512702   87  ILE   B O    
1065 C CB   . ILE   A 75  ? 0.475893 0.382124 0.342985 -0.0175908  -0.0297206  0.0496645   87  ILE   B CB   
1066 C CG1  . ILE   A 75  ? 0.507933 0.409227 0.376152 -0.0337009  -0.0410651  0.0383286   87  ILE   B CG1  
1067 C CG2  . ILE   A 75  ? 0.517482 0.415144 0.353007 0.00132784  -0.0333659  0.0496531   87  ILE   B CG2  
1068 C CD1  . ILE   A 75  ? 0.526323 0.412899 0.379173 -0.0388908  -0.0496189  0.0320642   87  ILE   B CD1  
1069 H H    . ILE   A 75  ? 0.475891 0.389354 0.338082 -0.00679291 -0.0408997  0.0493992   87  ILE   B H    
1070 H HA   . ILE   A 75  ? 0.468259 0.381222 0.347603 -0.00261304 -0.00780362 0.0687176   87  ILE   B HA   
1071 H HB   . ILE   A 75  ? 0.475623 0.383897 0.353797 -0.0217079  -0.0255283  0.0512755   87  ILE   B HB   
1072 H HG12 . ILE   A 75  ? 0.506    0.409402 0.372178 -0.0310112  -0.0470786  0.0355935   87  ILE   B HG12 
1073 H HG13 . ILE   A 75  ? 0.49047  0.394456 0.372649 -0.0429114  -0.0355757  0.038351    87  ILE   B HG13 
1074 H HG21 . ILE   A 75  ? 0.516724 0.407183 0.345185 -0.00035113 -0.0386482  0.0441554   87  ILE   B HG21 
1075 H HG22 . ILE   A 75  ? 0.523931 0.419    0.346433 0.00528876  -0.0423782  0.0456248   87  ILE   B HG22 
1076 H HG23 . ILE   A 75  ? 0.520252 0.420373 0.354934 0.0121377   -0.0209883  0.0589374   87  ILE   B HG23 
1077 H HD11 . ILE   A 75  ? 0.520662 0.407371 0.376016 -0.0387876  -0.0468655  0.0350884   87  ILE   B HD11 
1078 H HD12 . ILE   A 75  ? 0.523545 0.405084 0.378684 -0.0500599  -0.0517926  0.0277931   87  ILE   B HD12 
1079 H HD13 . ILE   A 75  ? 0.536802 0.41695  0.374958 -0.0302984  -0.0553275  0.0294914   87  ILE   B HD13 
1080 N N    . LYS   A 76  ? 0.464876 0.381854 0.395064 -0.0336919  -0.00118473 0.0616651   88  LYS   B N    
1081 C CA   . LYS   A 76  ? 0.444105 0.358268 0.400225 -0.0483645  0.00427623  0.0572171   88  LYS   B CA   
1082 C C    . LYS   A 76  ? 0.408511 0.315062 0.352164 -0.0625147  -0.0070689  0.0421853   88  LYS   B C    
1083 O O    . LYS   A 76  ? 0.456456 0.354019 0.405136 -0.0704137  -0.00157939 0.0356243   88  LYS   B O    
1084 C CB   . LYS   A 76  ? 0.487135 0.40903  0.472549 -0.0534983  0.00773381  0.059482    88  LYS   B CB   
1085 H H    . LYS   A 76  ? 0.45395  0.374028 0.383    -0.0269061  0.0015528   0.0663855   88  LYS   B H    
1086 H HA   . LYS   A 76  ? 0.451775 0.362211 0.415596 -0.0454409  0.0135116   0.0620782   88  LYS   B HA   
1089 N N    . ALA   A 77  ? 0.444143 0.349348 0.367009 -0.0635006  -0.0197982  0.0378786   89  ALA   B N    
1090 C CA   . ALA   A 77  ? 0.48305  0.374977 0.38425  -0.0743103  -0.0265535  0.0281099   89  ALA   B CA   
1091 C C    . ALA   A 77  ? 0.503846 0.391714 0.40305  -0.0774799  -0.0170871  0.0255175   89  ALA   B C    
1092 O O    . ALA   A 77  ? 0.436497 0.311489 0.324047 -0.0863248  -0.0113447  0.0183413   89  ALA   B O    
1093 C CB   . ALA   A 77  ? 0.48633  0.372515 0.365686 -0.0714715  -0.038239   0.0287335   89  ALA   B CB   
1094 H H    . ALA   A 77  ? 0.441314 0.350947 0.360994 -0.056064   -0.0224374  0.0420871   89  ALA   B H    
1095 H HA   . ALA   A 77  ? 0.488156 0.375492 0.391189 -0.0808341  -0.0286133  0.0228189   89  ALA   B HA   
1096 H HB1  . ALA   A 77  ? 0.488056 0.37919  0.373082 -0.0678597  -0.0440638  0.0304759   89  ALA   B HB1  
1097 H HB2  . ALA   A 77  ? 0.48393  0.371974 0.360935 -0.0659199  -0.0377962  0.0312885   89  ALA   B HB2  
1098 H HB3  . ALA   A 77  ? 0.500548 0.374317 0.362311 -0.077913   -0.040138   0.0249354   89  ALA   B HB3  
1099 N N    . TRP   A 78  ? 0.502684 0.401901 0.413016 -0.0684728  -0.0156042  0.0310046   90  TRP   B N    
1100 C CA   . TRP   A 78  ? 0.481545 0.385641 0.405308 -0.070205   -0.00890824 0.0287474   90  TRP   B CA   
1101 C C    . TRP   A 78  ? 0.442097 0.345199 0.384482 -0.0681954  0.00543315  0.0293033   90  TRP   B C    
1102 O O    . TRP   A 78  ? 0.513408 0.412368 0.462552 -0.0732525  0.0171011   0.0237076   90  TRP   B O    
1103 C CB   . TRP   A 78  ? 0.461285 0.379933 0.393518 -0.0600677  -0.0195899  0.0318379   90  TRP   B CB   
1104 C CG   . TRP   A 78  ? 0.467873 0.383174 0.393095 -0.0680803  -0.0298635  0.0255157   90  TRP   B CG   
1105 C CD1  . TRP   A 78  ? 0.445293 0.343957 0.346271 -0.0733871  -0.0351054  0.0234674   90  TRP   B CD1  
1106 C CD2  . TRP   A 78  ? 0.442802 0.370689 0.393264 -0.0725213  -0.0355711  0.0205818   90  TRP   B CD2  
1107 N NE1  . TRP   A 78  ? 0.435545 0.32944  0.340568 -0.0813167  -0.041635   0.0181605   90  TRP   B NE1  
1108 C CE2  . TRP   A 78  ? 0.451567 0.365287 0.39076  -0.0830385  -0.042466   0.0152539   90  TRP   B CE2  
1109 C CE3  . TRP   A 78  ? 0.480009 0.430955 0.467542 -0.0679551  -0.03669    0.0204032   90  TRP   B CE3  
1110 C CZ2  . TRP   A 78  ? 0.466164 0.387445 0.434041 -0.0930418  -0.0497653  0.00827588  90  TRP   B CZ2  
1111 C CZ3  . TRP   A 78  ? 0.487444 0.452901 0.507286 -0.0763377  -0.0465081  0.013209    90  TRP   B CZ3  
1112 C CH2  . TRP   A 78  ? 0.483096 0.433439 0.495108 -0.0908617  -0.052304   0.00654028  90  TRP   B CH2  
1113 H H    . TRP   A 78  ? 0.491104 0.395583 0.400927 -0.0602144  -0.0192978  0.0358356   90  TRP   B H    
1114 H HA   . TRP   A 78  ? 0.481557 0.378344 0.397366 -0.0788558  -0.00670178 0.024132    90  TRP   B HA   
1115 H HB2  . TRP   A 78  ? 0.465588 0.385269 0.389828 -0.0504277  -0.0236649  0.0368709   90  TRP   B HB2  
1116 H HB3  . TRP   A 78  ? 0.463786 0.391442 0.414714 -0.056837   -0.0157442  0.0328447   90  TRP   B HB3  
1117 H HD1  . TRP   A 78  ? 0.447918 0.339647 0.335133 -0.0714201  -0.0350737  0.0255605   90  TRP   B HD1  
1118 H HE1  . TRP   A 78  ? 0.456525 0.336773 0.348105 -0.0848406  -0.0447717  0.01698     90  TRP   B HE1  
1119 H HE3  . TRP   A 78  ? 0.466317 0.423101 0.460744 -0.0593112  -0.0312862  0.0251804   90  TRP   B HE3  
1120 H HZ2  . TRP   A 78  ? 0.482871 0.390164 0.444597 -0.101212   -0.0526708  0.00508163  90  TRP   B HZ2  
1121 H HZ3  . TRP   A 78  ? 0.480002 0.465479 0.53157  -0.0724889  -0.0494555  0.0128606   90  TRP   B HZ3  
1122 H HH2  . TRP   A 78  ? 0.486225 0.446353 0.527037 -0.0987801  -0.0586652  0.00097993  90  TRP   B HH2  
1123 N N    . ASP   A 79  ? 0.475909 0.379606 0.42737  -0.0597517  0.00820888  0.0370133   91  ASP   B N    
1124 C CA   . ASP   A 79  ? 0.481023 0.375658 0.450977 -0.0579478  0.0230083   0.0380861   91  ASP   B CA   
1125 C C    . ASP   A 79  ? 0.50296  0.378456 0.463822 -0.07266    0.0286232   0.023071    91  ASP   B C    
1126 O O    . ASP   A 79  ? 0.573798 0.438473 0.539798 -0.0730244  0.0419098   0.0165771   91  ASP   B O    
1127 C CB   . ASP   A 79  ? 0.458779 0.351323 0.439593 -0.0486385  0.0284441   0.0516036   91  ASP   B CB   
1128 C CG   . ASP   A 79  ? 0.484641 0.385847 0.465045 -0.0275641  0.0282943   0.0678188   91  ASP   B CG   
1129 O OD1  . ASP   A 79  ? 0.431114 0.343311 0.416211 -0.0198763  0.0219574   0.0666498   91  ASP   B OD1  
1130 O OD2  . ASP   A 79  ? 0.52326  0.420568 0.499411 -0.0177025  0.0346543   0.0821912   91  ASP   B OD2  
1131 H H    . ASP   A 79  ? 0.463548 0.37091  0.409799 -0.0544885  0.00291744  0.0423442   91  ASP   B H    
1132 H HA   . ASP   A 79  ? 0.479292 0.379592 0.459979 -0.0516004  0.0267949   0.0399853   91  ASP   B HA   
1133 H HB2  . ASP   A 79  ? 0.465307 0.36019  0.44059  -0.0518281  0.0234804   0.0522316   91  ASP   B HB2  
1134 H HB3  . ASP   A 79  ? 0.478802 0.359229 0.472145 -0.052413   0.0381428   0.0497598   91  ASP   B HB3  
1135 N N    . ILE   A 80  ? 0.498127 0.368167 0.442358 -0.0823057  0.0173113   0.0167012   92  ILE   B N    
1136 C CA   . ILE   A 80  ? 0.532957 0.38204  0.456551 -0.0939896  0.0153166   0.00064772  92  ILE   B CA   
1137 C C    . ILE   A 80  ? 0.570121 0.409009 0.462838 -0.096298   0.0220007   -0.00519106 92  ILE   B C    
1138 O O    . ILE   A 80  ? 0.58522  0.403648 0.462736 -0.0987442  0.0353565   -0.0161742  92  ILE   B O    
1139 C CB   . ILE   A 80  ? 0.574763 0.427229 0.492697 -0.100015   -0.00490499 -0.00231113 92  ILE   B CB   
1140 C CG1  . ILE   A 80  ? 0.598587 0.460699 0.557796 -0.100847   -0.0045739  0.00285591  92  ILE   B CG1  
1141 C CG2  . ILE   A 80  ? 0.6547   0.484743 0.535791 -0.109062   -0.0161488  -0.0195703  92  ILE   B CG2  
1142 C CD1  . ILE   A 80  ? 0.640056 0.520321 0.611965 -0.101465   -0.0209909  0.00652123  92  ILE   B CD1  
1143 H H    . ILE   A 80  ? 0.493536 0.372672 0.437441 -0.0799303  0.00932074  0.0221922   92  ILE   B H    
1144 H HA   . ILE   A 80  ? 0.553951 0.39216  0.488462 -0.0953648  0.0232347   -0.0042183  92  ILE   B HA   
1145 H HB   . ILE   A 80  ? 0.567979 0.430585 0.479061 -0.0959739  -0.0108394  0.00457526  92  ILE   B HB   
1146 H HG12 . ILE   A 80  ? 0.619008 0.467869 0.585502 -0.107961   -0.00298004 -0.00691669 92  ILE   B HG12 
1147 H HG13 . ILE   A 80  ? 0.587582 0.456102 0.560908 -0.0930226  0.00654643  0.0140303   92  ILE   B HG13 
1148 H HG21 . ILE   A 80  ? 0.645093 0.48043  0.529864 -0.111808   -0.032158   -0.0218454  92  ILE   B HG21 
1149 H HG22 . ILE   A 80  ? 0.660672 0.475866 0.541555 -0.112565   -0.0092754  -0.0291564  92  ILE   B HG22 
1150 H HG23 . ILE   A 80  ? 0.650416 0.473949 0.503448 -0.107583   -0.0141565  -0.0187724  92  ILE   B HG23 
1151 H HD11 . ILE   A 80  ? 0.611646 0.50082  0.57344  -0.0935141  -0.0217393  0.0149021   92  ILE   B HD11 
1152 H HD12 . ILE   A 80  ? 0.620429 0.508133 0.624843 -0.102568   -0.0159481  0.0112634   92  ILE   B HD12 
1153 H HD13 . ILE   A 80  ? 0.640595 0.515296 0.599194 -0.107705   -0.0353941  -0.0041296  92  ILE   B HD13 
1154 N N    . GLY   A 81  ? 0.540428 0.390286 0.424395 -0.0951289  0.0161462   0.00245106  93  GLY   B N    
1155 C CA   . GLY   A 81  ? 0.532275 0.369645 0.388855 -0.0998373  0.0246683   0.0004421   93  GLY   B CA   
1156 C C    . GLY   A 81  ? 0.518843 0.361046 0.397458 -0.0978504  0.0484505   0.00027332  93  GLY   B C    
1157 O O    . GLY   A 81  ? 0.56108  0.383753 0.417816 -0.10046    0.0677937   -0.00611541 93  GLY   B O    
1158 H H    . GLY   A 81  ? 0.519013 0.381864 0.414014 -0.0912393  0.00822896  0.00933318  93  GLY   B H    
1159 H HA2  . GLY   A 81  ? 0.562719 0.381119 0.388714 -0.103404   0.0228806   -0.00627053 93  GLY   B HA2  
1160 H HA3  . GLY   A 81  ? 0.526676 0.369892 0.380871 -0.100052   0.0172548   0.00624594  93  GLY   B HA3  
1161 N N    . VAL   A 82  ? 0.478374 0.347079 0.39983  -0.0906842  0.0470365   0.00766652  94  VAL   B N    
1162 C CA   . VAL   A 82  ? 0.477166 0.360115 0.433663 -0.0867418  0.0652704   0.00877653  94  VAL   B CA   
1163 C C    . VAL   A 82  ? 0.512179 0.380178 0.472189 -0.0807608  0.0851409   0.00197461  94  VAL   B C    
1164 O O    . VAL   A 82  ? 0.565745 0.434737 0.541645 -0.0782389  0.108847    -0.00053244 94  VAL   B O    
1165 C CB   . VAL   A 82  ? 0.47046  0.385961 0.468583 -0.0778449  0.050493    0.0170938   94  VAL   B CB   
1166 C CG1  . VAL   A 82  ? 0.491167 0.428609 0.538658 -0.0693878  0.0641152   0.0186145   94  VAL   B CG1  
1167 C CG2  . VAL   A 82  ? 0.49359  0.417261 0.488277 -0.0855017  0.0343633   0.0185258   94  VAL   B CG2  
1168 H H    . VAL   A 82  ? 0.464375 0.34287  0.393371 -0.0868627  0.0343992   0.012214    94  VAL   B H    
1169 H HA   . VAL   A 82  ? 0.497074 0.376107 0.446921 -0.0931509  0.0745089   0.00800873  94  VAL   B HA   
1170 H HB   . VAL   A 82  ? 0.467882 0.383098 0.462727 -0.0710156  0.041393    0.0204391   94  VAL   B HB   
1171 H HG11 . VAL   A 82  ? 0.496845 0.432531 0.549765 -0.0759891  0.079973    0.0154802   94  VAL   B HG11 
1172 H HG12 . VAL   A 82  ? 0.490057 0.421081 0.541167 -0.0611769  0.0714959   0.0189775   94  VAL   B HG12 
1173 H HG13 . VAL   A 82  ? 0.472936 0.43187  0.544095 -0.064611   0.0498006   0.0224568   94  VAL   B HG13 
1174 H HG21 . VAL   A 82  ? 0.472935 0.415024 0.489542 -0.0793634  0.0221232   0.0209343   94  VAL   B HG21 
1175 H HG22 . VAL   A 82  ? 0.484676 0.395712 0.451058 -0.0876231  0.0254739   0.0185672   94  VAL   B HG22 
1176 H HG23 . VAL   A 82  ? 0.494879 0.416116 0.493943 -0.0937488  0.0455217   0.0168341   94  VAL   B HG23 
1177 N N    . ALA   A 83  ? 0.51763  0.369946 0.466971 -0.0788045  0.0782669   -0.00167468 95  ALA   B N    
1178 C CA   . ALA   A 83  ? 0.587336 0.415995 0.537042 -0.0746431  0.0959217   -0.0113876  95  ALA   B CA   
1179 C C    . ALA   A 83  ? 0.599327 0.395895 0.503026 -0.0812055  0.111587    -0.0273093  95  ALA   B C    
1180 O O    . ALA   A 83  ? 0.668977 0.441347 0.567563 -0.0761309  0.130803    -0.038713   95  ALA   B O    
1181 C CB   . ALA   A 83  ? 0.564422 0.379229 0.516771 -0.0759528  0.0847115   -0.0129727  95  ALA   B CB   
1182 H H    . ALA   A 83  ? 0.51303  0.368522 0.457653 -0.0803252  0.0633665   0.00162723  95  ALA   B H    
1183 H HA   . ALA   A 83  ? 0.563443 0.403733 0.543334 -0.0651825  0.107059    -0.00658843 95  ALA   B HA   
1184 H HB1  . ALA   A 83  ? 0.549107 0.380223 0.524662 -0.0694482  0.079149    -0.00092811 95  ALA   B HB1  
1185 H HB2  . ALA   A 83  ? 0.574876 0.383099 0.505459 -0.0847738  0.0720046   -0.0180111  95  ALA   B HB2  
1186 H HB3  . ALA   A 83  ? 0.594562 0.389599 0.54836  -0.0740132  0.0964921   -0.020851   95  ALA   B HB3  
1187 N N    . THR   A 84  ? 0.615082 0.404613 0.477893 -0.0902509  0.102904    -0.0283505  96  THR   B N    
1188 C CA   . THR   A 84  ? 0.67503  0.428792 0.478923 -0.0930359  0.118307    -0.0404465  96  THR   B CA   
1189 C C    . THR   A 84  ? 0.724799 0.484877 0.535069 -0.090767   0.149795    -0.0324121  96  THR   B C    
1190 O O    . THR   A 84  ? 0.752534 0.480332 0.508749 -0.0906831  0.170007    -0.0384565  96  THR   B O    
1191 C CB   . THR   A 84  ? 0.664181 0.401017 0.413353 -0.100667   0.0930946   -0.0431967  96  THR   B CB   
1192 O OG1  . THR   A 84  ? 0.645189 0.40296  0.405634 -0.103351   0.0900057   -0.0263298  96  THR   B OG1  
1193 C CG2  . THR   A 84  ? 0.623258 0.363314 0.381336 -0.104934   0.0608112   -0.0498122  96  THR   B CG2  
1194 H H    . THR   A 84  ? 0.590799 0.394507 0.457533 -0.0931818  0.0874647   -0.0209856  96  THR   B H    
1195 H HA   . THR   A 84  ? 0.702339 0.435559 0.495792 -0.0902271  0.125863    -0.0524263  96  THR   B HA   
1196 H HB   . THR   A 84  ? 0.715518 0.423662 0.417081 -0.100066   0.1019      -0.0518981  96  THR   B HB   
1198 H HG21 . THR   A 84  ? 0.646041 0.378208 0.373077 -0.107944   0.0439275   -0.0515559  96  THR   B HG21 
1199 H HG22 . THR   A 84  ? 0.589294 0.354433 0.38741  -0.104034   0.0548646   -0.0398329  96  THR   B HG22 
1200 H HG23 . THR   A 84  ? 0.651677 0.375657 0.40768  -0.104981   0.0636988   -0.0621612  96  THR   B HG23 
1201 N N    . MET   A 85  ? 0.653615 0.453807 0.527735 -0.0890748  0.153574    -0.0189051  97  MET   B N    
1202 C CA   . MET   A 85  ? 0.674183 0.486259 0.569467 -0.0913401  0.181677    -0.0108265  97  MET   B CA   
1203 C C    . MET   A 85  ? 0.660909 0.485386 0.603309 -0.0798777  0.215834    -0.0129046  97  MET   B C    
1204 O O    . MET   A 85  ? 0.597865 0.431994 0.573029 -0.0684674  0.211576    -0.0163121  97  MET   B O    
1205 C CB   . MET   A 85  ? 0.616349 0.465134 0.558238 -0.0987982  0.162388    0.00178091  97  MET   B CB   
1206 C CG   . MET   A 85  ? 0.620669 0.453056 0.516607 -0.108046   0.137768    0.00519682  97  MET   B CG   
1207 S SD   . MET   A 85  ? 0.589278 0.457182 0.535797 -0.114199   0.111235    0.0141283   97  MET   B SD   
1208 C CE   . MET   A 85  ? 0.676327 0.545958 0.650703 -0.127389   0.142704    0.0216445   97  MET   B CE   
1209 H H    . MET   A 85  ? 0.627828 0.447901 0.533589 -0.0865691  0.138461    -0.014843   97  MET   B H    
1210 H HA   . MET   A 85  ? 0.704165 0.48945  0.551362 -0.0951494  0.192577    -0.0123672  97  MET   B HA   
1211 H HB2  . MET   A 85  ? 0.588242 0.459772 0.565856 -0.0933655  0.14726     0.00301302  97  MET   B HB2  
1212 H HB3  . MET   A 85  ? 0.626335 0.486759 0.596178 -0.101802   0.181604    0.00638964  97  MET   B HB3  
1213 H HG2  . MET   A 85  ? 0.657231 0.46734  0.51884  -0.112336   0.152432    0.00692124  97  MET   B HG2  
1214 H HG3  . MET   A 85  ? 0.620773 0.442227 0.491079 -0.105373   0.121364    0.00024715  97  MET   B HG3  
1215 H HE1  . MET   A 85  ? 0.640085 0.527529 0.647589 -0.133066   0.129087    0.0237975   97  MET   B HE1  
1216 H HE2  . MET   A 85  ? 0.665926 0.546926 0.66925  -0.124345   0.164175    0.0208149   97  MET   B HE2  
1217 H HE3  . MET   A 85  ? 0.692396 0.532508 0.621165 -0.131455   0.152835    0.0246674   97  MET   B HE3  
1218 N N    . LYS   A 86  ? 0.672149 0.493217 0.61741  -0.081603   0.253772    -0.00904669 98  LYS   B N    
1219 C CA   . LYS   A 86  ? 0.672207 0.511522 0.673424 -0.0701674  0.292717    -0.00864713 98  LYS   B CA   
1220 C C    . LYS   A 86  ? 0.637051 0.533424 0.733272 -0.076194   0.293461    0.00492032  98  LYS   B C    
1221 O O    . LYS   A 86  ? 0.581728 0.488137 0.681671 -0.0920453  0.275647    0.0125589   98  LYS   B O    
1222 C CB   . LYS   A 86  ? 0.744234 0.539694 0.686152 -0.0659956  0.341591    -0.0141813  98  LYS   B CB   
1223 H H    . LYS   A 86  ? 0.693854 0.500352 0.606329 -0.0895655  0.257242    -0.00522702 98  LYS   B H    
1224 H HA   . LYS   A 86  ? 0.664967 0.507243 0.682771 -0.0595281  0.286837    -0.0141393  98  LYS   B HA   
1227 N N    . LYS   A 87  ? 0.631325 0.564542 0.808213 -0.062772   0.311992    0.00644787  99  LYS   B N    
1228 C CA   . LYS   A 87  ? 0.61133  0.603183 0.890746 -0.0678833  0.314491    0.0162023   99  LYS   B CA   
1229 C C    . LYS   A 87  ? 0.653331 0.634552 0.925133 -0.087003   0.347557    0.0236235   99  LYS   B C    
1230 O O    . LYS   A 87  ? 0.702201 0.646023 0.925652 -0.0834626  0.394487    0.0232935   99  LYS   B O    
1231 C CB   . LYS   A 87  ? 0.605979 0.636081 0.97315  -0.0478531  0.340935    0.0170807   99  LYS   B CB   
1232 H H    . LYS   A 87  ? 0.646324 0.56767  0.816648 -0.0496962  0.322056    0.00049207  99  LYS   B H    
1233 H HA   . LYS   A 87  ? 0.573416 0.586709 0.872688 -0.0721132  0.277363    0.0180497   99  LYS   B HA   
1236 N N    . GLY   A 88  ? 0.651791 0.657421 0.960706 -0.106426   0.323052    0.0300365   100 GLY   B N    
1237 C CA   . GLY   A 88  ? 0.711011 0.707693 1.02882  -0.126483   0.355748    0.0402728   100 GLY   B CA   
1238 C C    . GLY   A 88  ? 0.731685 0.670731 0.944163 -0.138255   0.346001    0.0437465   100 GLY   B C    
1239 O O    . GLY   A 88  ? 0.725298 0.652929 0.943041 -0.156273   0.362849    0.0546513   100 GLY   B O    
1240 H H    . GLY   A 88  ? 0.61501  0.640078 0.942459 -0.106949   0.286037    0.0280434   100 GLY   B H    
1241 H HA2  . GLY   A 88  ? 0.677735 0.71257  1.06944  -0.136803   0.342811    0.0426394   100 GLY   B HA2  
1242 H HA3  . GLY   A 88  ? 0.737674 0.72815  1.06185  -0.121443   0.399372    0.0434277   100 GLY   B HA3  
1243 N N    . GLU   A 89  ? 0.740011 0.643859 0.864574 -0.127687   0.319191    0.0352999   101 GLU   B N    
1244 C CA   . GLU   A 89  ? 0.772447 0.625691 0.798995 -0.13379    0.303738    0.0374928   101 GLU   B CA   
1245 C C    . GLU   A 89  ? 0.754739 0.621654 0.8045   -0.14881    0.264618    0.0418748   101 GLU   B C    
1246 O O    . GLU   A 89  ? 0.662628 0.571143 0.77397  -0.149264   0.229963    0.036541    101 GLU   B O    
1247 C CB   . GLU   A 89  ? 0.789495 0.613709 0.74055  -0.119515   0.280935    0.024637    101 GLU   B CB   
1248 C CG   . GLU   A 89  ? 0.815161 0.589225 0.665166 -0.121798   0.263664    0.0251066   101 GLU   B CG   
1249 C CD   . GLU   A 89  ? 0.796449 0.546632 0.585875 -0.110931   0.238796    0.00975902  101 GLU   B CD   
1250 O OE1  . GLU   A 89  ? 0.866844 0.605724 0.646249 -0.10052    0.26013     -0.00122051 101 GLU   B OE1  
1251 O OE2  . GLU   A 89  ? 0.76152  0.50407  0.519023 -0.112824   0.199701    0.00768931  101 GLU   B OE2  
1252 H H    . GLU   A 89  ? 0.72297  0.635618 0.853051 -0.115792   0.309725    0.028157    101 GLU   B H    
1253 H HA   . GLU   A 89  ? 0.826078 0.651503 0.819075 -0.136583   0.336449    0.0444728   101 GLU   B HA   
1254 H HB2  . GLU   A 89  ? 0.810609 0.624913 0.751338 -0.110058   0.305575    0.0194755   101 GLU   B HB2  
1255 H HB3  . GLU   A 89  ? 0.739064 0.587613 0.72085  -0.11668    0.251964    0.0202586   101 GLU   B HB3  
1256 H HG2  . GLU   A 89  ? 0.786143 0.56872  0.647148 -0.129407   0.240276    0.0300822   101 GLU   B HG2  
1257 H HG3  . GLU   A 89  ? 0.862123 0.608248 0.674149 -0.122894   0.291921    0.0312166   101 GLU   B HG3  
1258 N N    . ILE   A 90  ? 0.800989 0.62639  0.793415 -0.158681   0.271878    0.0518661   102 ILE   B N    
1259 C CA   . ILE   A 90  ? 0.775017 0.591183 0.75348  -0.167791   0.234529    0.0542767   102 ILE   B CA   
1260 C C    . ILE   A 90  ? 0.779202 0.547417 0.651972 -0.157845   0.218646    0.0545762   102 ILE   B C    
1261 O O    . ILE   A 90  ? 0.82948  0.554057 0.632769 -0.154138   0.246801    0.0622566   102 ILE   B O    
1262 C CB   . ILE   A 90  ? 0.776922 0.584765 0.792164 -0.18808    0.255085    0.0673551   102 ILE   B CB   
1263 C CG1  . ILE   A 90  ? 0.775017 0.638913 0.910485 -0.19997    0.263331    0.0639205   102 ILE   B CG1  
1264 C CG2  . ILE   A 90  ? 0.749172 0.534041 0.736142 -0.194525   0.219079    0.0689504   102 ILE   B CG2  
1265 C CD1  . ILE   A 90  ? 0.867688 0.726917 1.05907  -0.224459   0.288842    0.0754439   102 ILE   B CD1  
1266 H H    . ILE   A 90  ? 0.843698 0.642322 0.801211 -0.157954   0.303369    0.0580994   102 ILE   B H    
1267 H HA   . ILE   A 90  ? 0.721656 0.56702  0.736768 -0.166244   0.205602    0.0467178   102 ILE   B HA   
1268 H HB   . ILE   A 90  ? 0.831254 0.608859 0.809404 -0.18832    0.288841    0.0774152   102 ILE   B HB   
1269 H HG12 . ILE   A 90  ? 0.7383   0.629433 0.903598 -0.198035   0.227731    0.0539961   102 ILE   B HG12 
1270 H HG13 . ILE   A 90  ? 0.784453 0.663166 0.937891 -0.19266    0.286664    0.0631741   102 ILE   B HG13 
1271 H HG21 . ILE   A 90  ? 0.774678 0.553223 0.791572 -0.208578   0.231359    0.0758616   102 ILE   B HG21 
1272 H HG22 . ILE   A 90  ? 0.714028 0.523649 0.724351 -0.191463   0.186517    0.058642    102 ILE   B HG22 
1273 H HG23 . ILE   A 90  ? 0.782473 0.532665 0.698221 -0.186641   0.21683     0.0733142   102 ILE   B HG23 
1274 H HD11 . ILE   A 90  ? 0.896035 0.723272 1.05092  -0.225425   0.32676     0.0880819   102 ILE   B HD11 
1275 H HD12 . ILE   A 90  ? 0.828524 0.729209 1.10362  -0.2314     0.293009    0.0715144   102 ILE   B HD12 
1276 H HD13 . ILE   A 90  ? 0.84337  0.688877 1.02497  -0.231891   0.263868    0.0742002   102 ILE   B HD13 
1277 N N    . ALA   A 91  ? 0.726608 0.503208 0.589768 -0.153233   0.173379    0.0474094   103 ALA   B N    
1278 C CA   . ALA   A 91  ? 0.749319 0.49293  0.533011 -0.143872   0.150252    0.0463813   103 ALA   B CA   
1279 C C    . ALA   A 91  ? 0.717173 0.456189 0.499563 -0.14678    0.119245    0.0505664   103 ALA   B C    
1280 O O    . ALA   A 91  ? 0.71537  0.482427 0.557053 -0.15341    0.106177    0.0474705   103 ALA   B O    
1281 C CB   . ALA   A 91  ? 0.73856  0.499164 0.519645 -0.132752   0.130218    0.0325188   103 ALA   B CB   
1282 H H    . ALA   A 91  ? 0.692319 0.49772  0.602551 -0.155226   0.156274    0.0430399   103 ALA   B H    
1283 H HA   . ALA   A 91  ? 0.799276 0.510353 0.532284 -0.142058   0.168817    0.0521268   103 ALA   B HA   
1284 H HB1  . ALA   A 91  ? 0.747894 0.506569 0.526995 -0.12979    0.150299    0.0285665   103 ALA   B HB1  
1285 H HB2  . ALA   A 91  ? 0.689775 0.479119 0.515222 -0.132773   0.114739    0.0292963   103 ALA   B HB2  
1286 H HB3  . ALA   A 91  ? 0.744237 0.487524 0.481876 -0.12787    0.113064    0.030736    103 ALA   B HB3  
1287 N N    . HIS   A 92  ? 0.724377 0.427781 0.438307 -0.139349   0.105302    0.055904    104 HIS   B N    
1288 C CA   . HIS   A 92  ? 0.721077 0.420654 0.429745 -0.13548    0.0732036   0.0576833   104 HIS   B CA   
1289 C C    . HIS   A 92  ? 0.741062 0.453384 0.430521 -0.122195   0.0425676   0.0483827   104 HIS   B C    
1290 O O    . HIS   A 92  ? 0.763108 0.461465 0.408652 -0.116056   0.0426162   0.0448488   104 HIS   B O    
1291 C CB   . HIS   A 92  ? 0.794251 0.444501 0.448326 -0.134178   0.07892     0.0738417   104 HIS   B CB   
1292 C CG   . HIS   A 92  ? 0.814702 0.447991 0.49636  -0.150001   0.108048    0.085241    104 HIS   B CG   
1293 N ND1  . HIS   A 92  ? 0.858349 0.440523 0.49572  -0.150854   0.122876    0.103917    104 HIS   B ND1  
1294 C CD2  . HIS   A 92  ? 0.780618 0.442003 0.53646  -0.166169   0.123757    0.0808694   104 HIS   B CD2  
1295 C CE1  . HIS   A 92  ? 0.866609 0.444599 0.552767 -0.169801   0.151455    0.110699    104 HIS   B CE1  
1296 N NE2  . HIS   A 92  ? 0.792116 0.421789 0.554851 -0.179785   0.149669    0.0952625   104 HIS   B NE2  
1297 H H    . HIS   A 92  ? 0.772809 0.452888 0.4406   -0.13487    0.115966    0.0582335   104 HIS   B H    
1298 H HA   . HIS   A 92  ? 0.698102 0.417831 0.452463 -0.140995   0.0671875   0.0544904   104 HIS   B HA   
1299 H HB2  . HIS   A 92  ? 0.828803 0.45752  0.432996 -0.127807   0.0856858   0.0773198   104 HIS   B HB2  
1300 H HB3  . HIS   A 92  ? 0.781585 0.429434 0.429028 -0.127695   0.0559235   0.0738049   104 HIS   B HB3  
1302 H HD2  . HIS   A 92  ? 0.734881 0.431349 0.532298 -0.167504   0.117981    0.0704      104 HIS   B HD2  
1303 H HE1  . HIS   A 92  ? 0.908833 0.452468 0.58068  -0.175135   0.168699    0.124637    104 HIS   B HE1  
1305 N N    . LEU   A 93  ? 0.700874 0.438528 0.424419 -0.118052   0.0178901   0.0434275   105 LEU   B N    
1306 C CA   . LEU   A 93  ? 0.659579 0.411475 0.377201 -0.106687   -0.00722653 0.0376524   105 LEU   B CA   
1307 C C    . LEU   A 93  ? 0.643134 0.387787 0.353871 -0.0975276  -0.028002   0.0428266   105 LEU   B C    
1308 O O    . LEU   A 93  ? 0.647461 0.394172 0.381204 -0.0990675  -0.0290316  0.0432996   105 LEU   B O    
1309 C CB   . LEU   A 93  ? 0.658824 0.448342 0.424546 -0.105854   -0.00994049 0.0290192   105 LEU   B CB   
1310 C CG   . LEU   A 93  ? 0.6701   0.469697 0.45315  -0.110943   0.0101347   0.0235084   105 LEU   B CG   
1311 C CD1  . LEU   A 93  ? 0.642951 0.475209 0.471483 -0.106063   0.00510486  0.0193348   105 LEU   B CD1  
1312 C CD2  . LEU   A 93  ? 0.702188 0.481059 0.44374  -0.1099     0.0146142   0.0179357   105 LEU   B CD2  
1313 H H    . LEU   A 93  ? 0.679514 0.42522  0.431652 -0.122471   0.0178443   0.0434518   105 LEU   B H    
1314 H HA   . LEU   A 93  ? 0.692684 0.432661 0.379599 -0.104232   -0.00810388 0.0363301   105 LEU   B HA   
1315 H HB2  . LEU   A 93  ? 0.632588 0.432185 0.421453 -0.106048   -0.0130427  0.0295984   105 LEU   B HB2  
1316 H HB3  . LEU   A 93  ? 0.640091 0.437692 0.405248 -0.0996543  -0.0231197  0.0266808   105 LEU   B HB3  
1317 H HG   . LEU   A 93  ? 0.67847  0.474409 0.47006  -0.117078   0.0249235   0.0263613   105 LEU   B HG   
1318 H HD11 . LEU   A 93  ? 0.623615 0.46682  0.471857 -0.105418   0.00035082  0.0212493   105 LEU   B HD11 
1319 H HD12 . LEU   A 93  ? 0.638504 0.475103 0.478912 -0.107453   0.0180889   0.0165278   105 LEU   B HD12 
1320 H HD13 . LEU   A 93  ? 0.630334 0.46615  0.455499 -0.101231   -0.00583933 0.0179552   105 LEU   B HD13 
1321 H HD21 . LEU   A 93  ? 0.735171 0.490409 0.441327 -0.110943   0.0198528   0.0221928   105 LEU   B HD21 
1322 H HD22 . LEU   A 93  ? 0.695779 0.479053 0.43407  -0.105836   -0.00199561 0.0143228   105 LEU   B HD22 
1323 H HD23 . LEU   A 93  ? 0.70138  0.484559 0.454563 -0.111476   0.0287963   0.013339    105 LEU   B HD23 
1324 N N    . LEU   A 94  ? 0.654777 0.39289  0.338    -0.0866598  -0.0466556  0.0444245   106 LEU   B N    
1325 C CA   . LEU   A 94  ? 0.679819 0.419417 0.366526 -0.0732049  -0.066739   0.048537    106 LEU   B CA   
1326 C C    . LEU   A 94  ? 0.654013 0.431008 0.37528  -0.0663585  -0.081448   0.0412153   106 LEU   B C    
1327 O O    . LEU   A 94  ? 0.632048 0.417466 0.34957  -0.0676644  -0.0903429  0.0355671   106 LEU   B O    
1328 C CB   . LEU   A 94  ? 0.764551 0.469644 0.400663 -0.0631369  -0.0780638  0.0592387   106 LEU   B CB   
1329 C CG   . LEU   A 94  ? 0.780153 0.485419 0.422958 -0.0449981  -0.0983433  0.0651295   106 LEU   B CG   
1330 C CD1  . LEU   A 94  ? 0.772548 0.459514 0.426299 -0.0447988  -0.0877556  0.0686748   106 LEU   B CD1  
1331 C CD2  . LEU   A 94  ? 0.902841 0.581029 0.49876  -0.0303269  -0.116633   0.075946    106 LEU   B CD2  
1332 H H    . LEU   A 94  ? 0.679922 0.412839 0.342463 -0.0867987  -0.0474775  0.0420209   106 LEU   B H    
1333 H HA   . LEU   A 94  ? 0.671542 0.409367 0.372995 -0.0738618  -0.0626266  0.0494926   106 LEU   B HA   
1334 H HB2  . LEU   A 94  ? 0.788376 0.466253 0.402306 -0.0683371  -0.0639907  0.0661096   106 LEU   B HB2  
1335 H HB3  . LEU   A 94  ? 0.775321 0.481408 0.392912 -0.0620992  -0.085367   0.0561484   106 LEU   B HB3  
1336 H HG   . LEU   A 94  ? 0.756626 0.492507 0.431118 -0.0410059  -0.107331   0.0588922   106 LEU   B HG   
1337 H HD11 . LEU   A 94  ? 0.740788 0.447214 0.423175 -0.0509736  -0.0815417  0.0608028   106 LEU   B HD11 
1338 H HD12 . LEU   A 94  ? 0.783848 0.4673   0.439026 -0.0311727  -0.0984929  0.0721568   106 LEU   B HD12 
1339 H HD13 . LEU   A 94  ? 0.804629 0.462219 0.435443 -0.0515228  -0.0763955  0.074958    106 LEU   B HD13 
1340 H HD21 . LEU   A 94  ? 0.888201 0.577091 0.475328 -0.0302572  -0.127791   0.0708327   106 LEU   B HD21 
1341 H HD22 . LEU   A 94  ? 0.919599 0.563393 0.4804   -0.0328461  -0.105208   0.0847905   106 LEU   B HD22 
1342 H HD23 . LEU   A 94  ? 0.881432 0.56428  0.490422 -0.0172822  -0.128857   0.0794021   106 LEU   B HD23 
1343 N N    . ILE   A 95  ? 0.60376  0.399443 0.35728  -0.058569   -0.0832447  0.0410894   107 ILE   B N    
1344 C CA   . ILE   A 95  ? 0.570662 0.401107 0.363759 -0.0545202  -0.0847462  0.0371719   107 ILE   B CA   
1345 C C    . ILE   A 95  ? 0.550469 0.39377  0.362571 -0.0373337  -0.0941139  0.0415525   107 ILE   B C    
1346 O O    . ILE   A 95  ? 0.5694   0.40251  0.37671  -0.0281107  -0.0896221  0.0434168   107 ILE   B O    
1347 C CB   . ILE   A 95  ? 0.563543 0.404051 0.374147 -0.0588065  -0.0698347  0.0343111   107 ILE   B CB   
1348 C CG1  . ILE   A 95  ? 0.563828 0.398717 0.369235 -0.0733171  -0.0582904  0.0304871   107 ILE   B CG1  
1349 C CG2  . ILE   A 95  ? 0.529232 0.398128 0.373426 -0.0511649  -0.0657046  0.0352176   107 ILE   B CG2  
1350 C CD1  . ILE   A 95  ? 0.53883  0.382045 0.361785 -0.0759877  -0.0493652  0.0283505   107 ILE   B CD1  
1351 H H    . ILE   A 95  ? 0.617065 0.399996 0.365211 -0.0552595  -0.0817721  0.0438563   107 ILE   B H    
1352 H HA   . ILE   A 95  ? 0.56931  0.407335 0.366575 -0.0593858  -0.0880065  0.0337123   107 ILE   B HA   
1353 H HB   . ILE   A 95  ? 0.565206 0.395018 0.368193 -0.0554033  -0.0695707  0.0349923   107 ILE   B HB   
1354 H HG12 . ILE   A 95  ? 0.555709 0.399652 0.369438 -0.0759334  -0.0572133  0.0278544   107 ILE   B HG12 
1355 H HG13 . ILE   A 95  ? 0.584545 0.400133 0.367101 -0.0777143  -0.0575105  0.0318745   107 ILE   B HG13 
1356 H HG21 . ILE   A 95  ? 0.521676 0.39443  0.370582 -0.0521714  -0.0581425  0.0344511   107 ILE   B HG21 
1357 H HG22 . ILE   A 95  ? 0.527276 0.405681 0.384339 -0.0551991  -0.0672097  0.0340664   107 ILE   B HG22 
1358 H HG23 . ILE   A 95  ? 0.533763 0.405823 0.381973 -0.0404817  -0.0682221  0.0380897   107 ILE   B HG23 
1359 H HD11 . ILE   A 95  ? 0.549549 0.383524 0.366589 -0.074018   -0.0529823  0.0283914   107 ILE   B HD11 
1360 H HD12 . ILE   A 95  ? 0.544171 0.384871 0.368464 -0.0843703  -0.0409915  0.0267163   107 ILE   B HD12 
1361 H HD13 . ILE   A 95  ? 0.524756 0.384027 0.363905 -0.0704248  -0.0486757  0.0284805   107 ILE   B HD13 
1362 N N    . LYS   A 96  ? 0.514779 0.382494 0.355028 -0.0332716  -0.105573   0.041266    108 LYS   B N    
1363 C CA   . LYS   A 96  ? 0.545494 0.435636 0.421083 -0.0163392  -0.109312   0.0462026   108 LYS   B CA   
1364 C C    . LYS   A 96  ? 0.54736  0.458813 0.4551   -0.0120976  -0.0877097  0.0480279   108 LYS   B C    
1365 O O    . LYS   A 96  ? 0.504903 0.420687 0.417108 -0.0233546  -0.0759151  0.0456738   108 LYS   B O    
1366 C CB   . LYS   A 96  ? 0.58297  0.498438 0.491449 -0.0161387  -0.130463   0.0442652   108 LYS   B CB   
1367 C CG   . LYS   A 96  ? 0.681226 0.574991 0.549743 -0.0140313  -0.157084   0.0437855   108 LYS   B CG   
1368 C CD   . LYS   A 96  ? 0.670153 0.594133 0.576379 -0.0133543  -0.185954   0.0379411   108 LYS   B CD   
1369 C CE   . LYS   A 96  ? 0.707917 0.613219 0.573678 -0.00160483 -0.218418   0.0403569   108 LYS   B CE   
1370 N NZ   . LYS   A 96  ? 0.756964 0.626788 0.555881 -0.0139966  -0.224455   0.0331512   108 LYS   B NZ   
1371 H H    . LYS   A 96  ? 0.533395 0.404374 0.373829 -0.0414565  -0.110843   0.0370591   108 LYS   B H    
1372 H HA   . LYS   A 96  ? 0.56569  0.439369 0.42338  -0.00615999 -0.111962   0.0498758   108 LYS   B HA   
1373 H HB2  . LYS   A 96  ? 0.574399 0.501677 0.500341 -0.0277961  -0.127665   0.0390391   108 LYS   B HB2  
1374 H HB3  . LYS   A 96  ? 0.581217 0.516969 0.523695 -0.00492782 -0.130053   0.0482672   108 LYS   B HB3  
1375 H HG2  . LYS   A 96  ? 0.678912 0.557807 0.530649 -0.0016786  -0.159097   0.0506246   108 LYS   B HG2  
1376 H HG3  . LYS   A 96  ? 0.67223  0.544655 0.50545  -0.0245412  -0.153667   0.0404673   108 LYS   B HG3  
1377 H HD2  . LYS   A 96  ? 0.664885 0.593624 0.577214 -0.0275028  -0.186033   0.0291417   108 LYS   B HD2  
1378 H HD3  . LYS   A 96  ? 0.653144 0.605708 0.608951 -0.00613334 -0.18348    0.04085     108 LYS   B HD3  
1379 H HE2  . LYS   A 96  ? 0.718148 0.650604 0.621433 0.00326627  -0.239305   0.0374668   108 LYS   B HE2  
1380 H HE3  . LYS   A 96  ? 0.726662 0.614419 0.572047 0.0110751   -0.214505   0.0500262   108 LYS   B HE3  
1381 H HZ1  . LYS   A 96  ? 0.747098 0.630693 0.563279 -0.0239997  -0.231832   0.0224938   108 LYS   B HZ1  
1382 H HZ2  . LYS   A 96  ? 0.745316 0.595565 0.520246 -0.0202706  -0.203215   0.0353281   108 LYS   B HZ2  
1383 H HZ3  . LYS   A 96  ? 0.791405 0.643684 0.555212 -0.0046108  -0.241522   0.0371064   108 LYS   B HZ3  
1384 N N    . PRO   A 97  ? 0.526112 0.449221 0.454632 0.00724941  -0.079803   0.0537696   109 PRO   B N    
1385 C CA   . PRO   A 97  ? 0.519428 0.451003 0.457601 0.0166843   -0.055245   0.0575484   109 PRO   B CA   
1386 C C    . PRO   A 97  ? 0.490425 0.447766 0.467863 0.00754553  -0.0404182  0.061734    109 PRO   B C    
1387 O O    . PRO   A 97  ? 0.518946 0.472183 0.485011 0.0121963   -0.0208716  0.0660169   109 PRO   B O    
1388 C CB   . PRO   A 97  ? 0.530571 0.46709  0.481822 0.0411479   -0.0480831  0.0625833   109 PRO   B CB   
1389 C CG   . PRO   A 97  ? 0.531001 0.478604 0.506192 0.0429242   -0.0715601  0.0636097   109 PRO   B CG   
1390 C CD   . PRO   A 97  ? 0.537516 0.460811 0.473533 0.0248858   -0.091996   0.057808    109 PRO   B CD   
1391 H HA   . PRO   A 97  ? 0.521738 0.433302 0.427027 0.0155049   -0.0522704  0.0542083   109 PRO   B HA   
1392 H HB2  . PRO   A 97  ? 0.526204 0.481734 0.504848 0.0478819   -0.0312825  0.0680503   109 PRO   B HB2  
1393 H HB3  . PRO   A 97  ? 0.548239 0.460409 0.465031 0.0494873   -0.0458834  0.0595555   109 PRO   B HB3  
1394 H HG2  . PRO   A 97  ? 0.520927 0.498366 0.541595 0.0405006   -0.0723172  0.0661141   109 PRO   B HG2  
1395 H HG3  . PRO   A 97  ? 0.550726 0.489617 0.520314 0.0590658   -0.0722161  0.0656371   109 PRO   B HG3  
1396 H HD2  . PRO   A 97  ? 0.542901 0.477543 0.494119 0.0214735   -0.108305   0.0575805   109 PRO   B HD2  
1397 H HD3  . PRO   A 97  ? 0.557807 0.453298 0.459043 0.0292488   -0.0950019  0.0572694   109 PRO   B HD3  
1398 N N    . GLU   A 98  ? 0.517319 0.496582 0.537312 -0.00535681 -0.0512975  0.0599552   110 GLU   B N    
1399 C CA   . GLU   A 98  ? 0.518432 0.518133 0.584857 -0.0160494  -0.0357168  0.0637492   110 GLU   B CA   
1400 C C    . GLU   A 98  ? 0.475832 0.455182 0.512312 -0.0289887  -0.0293003  0.0605041   110 GLU   B C    
1401 O O    . GLU   A 98  ? 0.46158  0.446228 0.521748 -0.0324728  -0.00970838 0.0673599   110 GLU   B O    
1402 C CB   . GLU   A 98  ? 0.564026 0.589487 0.686464 -0.0293995  -0.0555049  0.0573036   110 GLU   B CB   
1403 C CG   . GLU   A 98  ? 0.64463  0.701945 0.818858 -0.0151147  -0.0613188  0.0623906   110 GLU   B CG   
1404 C CD   . GLU   A 98  ? 0.735213 0.783089 0.87811  0.00085899  -0.0851755  0.0604871   110 GLU   B CD   
1405 O OE1  . GLU   A 98  ? 0.67212  0.688005 0.753572 -0.00303843 -0.10396    0.0539212   110 GLU   B OE1  
1406 O OE2  . GLU   A 98  ? 0.856481 0.928881 1.04128  0.0192147   -0.0818804  0.0676197   110 GLU   B OE2  
1407 H H    . GLU   A 98  ? 0.51847  0.497602 0.537872 -0.00765247 -0.0695734  0.0559466   110 GLU   B H    
1408 H HA   . GLU   A 98  ? 0.518329 0.527361 0.601452 -0.00495894 -0.0156677  0.0728434   110 GLU   B HA   
1409 H HB2  . GLU   A 98  ? 0.574784 0.587367 0.671097 -0.0371642  -0.0758296  0.0481807   110 GLU   B HB2  
1410 H HB3  . GLU   A 98  ? 0.562023 0.595454 0.714739 -0.0396662  -0.0451232  0.0581849   110 GLU   B HB3  
1411 H HG2  . GLU   A 98  ? 0.6395   0.718708 0.862083 -0.025567   -0.0717233  0.0583673   110 GLU   B HG2  
1412 H HG3  . GLU   A 98  ? 0.639933 0.705431 0.830584 -0.00437228 -0.0366656  0.0722782   110 GLU   B HG3  
1413 N N    . TYR   A 99  ? 0.490484 0.445945 0.478713 -0.0348994  -0.0432048  0.0518834   111 TYR   B N    
1414 C CA   . TYR   A 99  ? 0.48223  0.422093 0.447845 -0.044156   -0.0367992  0.0487438   111 TYR   B CA   
1415 C C    . TYR   A 99  ? 0.478167 0.403135 0.405193 -0.034038   -0.0319721  0.0506635   111 TYR   B C    
1416 O O    . TYR   A 99  ? 0.45634  0.372115 0.368453 -0.0399674  -0.0304713  0.0475393   111 TYR   B O    
1417 C CB   . TYR   A 99  ? 0.521647 0.448452 0.470322 -0.0595945  -0.052941   0.0367077   111 TYR   B CB   
1418 C CG   . TYR   A 99  ? 0.498588 0.436436 0.48172  -0.0710341  -0.0626199  0.0295042   111 TYR   B CG   
1419 C CD1  . TYR   A 99  ? 0.464367 0.415592 0.464372 -0.0691177  -0.0837487  0.0264248   111 TYR   B CD1  
1420 C CD2  . TYR   A 99  ? 0.497171 0.431946 0.50097  -0.0827131  -0.0525813  0.0250046   111 TYR   B CD2  
1421 C CE1  . TYR   A 99  ? 0.484323 0.447904 0.520743 -0.0811494  -0.0995364  0.0159578   111 TYR   B CE1  
1422 C CE2  . TYR   A 99  ? 0.494117 0.434926 0.532044 -0.0959855  -0.0646689  0.013907    111 TYR   B CE2  
1423 C CZ   . TYR   A 99  ? 0.488514 0.4459   0.544431 -0.0961232  -0.0900267  0.00836498  111 TYR   B CZ   
1424 O OH   . TYR   A 99  ? 0.551154 0.518857 0.647827 -0.109827   -0.108535   -0.00530446 111 TYR   B OH   
1425 H H    . TYR   A 99  ? 0.494774 0.443733 0.466678 -0.0324658  -0.0559588  0.0487841   111 TYR   B H    
1426 H HA   . TYR   A 99  ? 0.482355 0.429147 0.471037 -0.046427   -0.0248031  0.0529071   111 TYR   B HA   
1427 H HB2  . TYR   A 99  ? 0.517055 0.4354   0.443578 -0.0568396  -0.0634912  0.035109    111 TYR   B HB2  
1428 H HB3  . TYR   A 99  ? 0.505648 0.422528 0.44069  -0.0640915  -0.0465094  0.034706    111 TYR   B HB3  
1429 H HD1  . TYR   A 99  ? 0.480965 0.431616 0.467526 -0.0593963  -0.0897751  0.0303226   111 TYR   B HD1  
1430 H HD2  . TYR   A 99  ? 0.488463 0.415132 0.483056 -0.0816001  -0.039278   0.0282457   111 TYR   B HD2  
1431 H HE1  . TYR   A 99  ? 0.492797 0.46873  0.543927 -0.0787667  -0.117688   0.0134373   111 TYR   B HE1  
1432 H HE2  . TYR   A 99  ? 0.498059 0.431959 0.549661 -0.104205   -0.05712    0.00978447  111 TYR   B HE2  
1434 N N    . ALA   A 100 ? 0.476295 0.399512 0.391146 -0.0179776  -0.0304074  0.0541683   112 ALA   B N    
1435 C CA   . ALA   A 100 ? 0.483309 0.389938 0.361237 -0.00802366 -0.0306779  0.0516857   112 ALA   B CA   
1436 C C    . ALA   A 100 ? 0.487899 0.397237 0.359188 0.013715    -0.0140598  0.0600156   112 ALA   B C    
1437 O O    . ALA   A 100 ? 0.491389 0.407232 0.369139 0.0177878   0.00081412  0.0691668   112 ALA   B O    
1438 C CB   . ALA   A 100 ? 0.476279 0.363391 0.330605 -0.0106865  -0.0458889  0.0435467   112 ALA   B CB   
1439 H H    . ALA   A 100 ? 0.47992  0.41231  0.411399 -0.0125852  -0.0299778  0.0569271   112 ALA   B H    
1440 H HA   . ALA   A 100 ? 0.474096 0.378841 0.347321 -0.0138643  -0.0304825  0.0502276   112 ALA   B HA   
1441 H HB1  . ALA   A 100 ? 0.476968 0.359739 0.329998 -0.023558   -0.0515918  0.0402775   112 ALA   B HB1  
1442 H HB2  . ALA   A 100 ? 0.487409 0.376182 0.348347 -0.00496966 -0.0480007  0.0454959   112 ALA   B HB2  
1443 H HB3  . ALA   A 100 ? 0.49555  0.370649 0.329212 -0.00459994 -0.0474938  0.0397631   112 ALA   B HB3  
1444 N N    . TYR   A 101 ? 0.499517 0.399055 0.353068 0.0299281   -0.0132268  0.0580794   113 TYR   B N    
1445 C CA   . TYR   A 101 ? 0.550103 0.443332 0.379956 0.0542679   0.00562887  0.0639434   113 TYR   B CA   
1446 C C    . TYR   A 101 ? 0.552637 0.463049 0.416544 0.0681756   0.0262583   0.074293    113 TYR   B C    
1447 O O    . TYR   A 101 ? 0.611207 0.514461 0.45493  0.0915532   0.0479982   0.0799756   113 TYR   B O    
1448 C CB   . TYR   A 101 ? 0.584796 0.446544 0.360358 0.064706    -0.00827536 0.0492852   113 TYR   B CB   
1449 C CG   . TYR   A 101 ? 0.555217 0.408568 0.310737 0.052419    -0.0269756  0.0401339   113 TYR   B CG   
1450 C CD1  . TYR   A 101 ? 0.571927 0.425512 0.304786 0.062785    -0.0232592  0.0446483   113 TYR   B CD1  
1451 C CD2  . TYR   A 101 ? 0.554401 0.402313 0.319522 0.0311846   -0.0463252  0.029856    113 TYR   B CD2  
1452 C CE1  . TYR   A 101 ? 0.5768   0.430753 0.30403  0.0532624   -0.0427723  0.0372121   113 TYR   B CE1  
1453 C CE2  . TYR   A 101 ? 0.579859 0.428374 0.343293 0.0192428   -0.0603257  0.0226604   113 TYR   B CE2  
1454 C CZ   . TYR   A 101 ? 0.569121 0.423957 0.317983 0.0304311   -0.0607638  0.0255312   113 TYR   B CZ   
1455 O OH   . TYR   A 101 ? 0.523336 0.384738 0.279736 0.0212821   -0.0775899  0.0185043   113 TYR   B OH   
1456 H H    . TYR   A 101 ? 0.507445 0.400792 0.359587 0.0276242   -0.0232437  0.053269    113 TYR   B H    
1457 H HA   . TYR   A 101 ? 0.547153 0.443665 0.373964 0.055306    0.0142924   0.0704087   113 TYR   B HA   
1458 H HB2  . TYR   A 101 ? 0.579531 0.433629 0.358053 0.0618162   -0.0171243  0.0434086   113 TYR   B HB2  
1459 H HB3  . TYR   A 101 ? 0.608176 0.461536 0.360332 0.0833973   0.00400976  0.0513064   113 TYR   B HB3  
1460 H HD1  . TYR   A 101 ? 0.59192  0.445922 0.314407 0.077891    -0.00646488 0.0542373   113 TYR   B HD1  
1461 H HD2  . TYR   A 101 ? 0.551282 0.395507 0.326188 0.025572    -0.048846   0.028899    113 TYR   B HD2  
1462 H HE1  . TYR   A 101 ? 0.594996 0.449034 0.305383 0.0633024   -0.0425857  0.0413217   113 TYR   B HE1  
1463 H HE2  . TYR   A 101 ? 0.557638 0.402754 0.331274 0.00472477  -0.0688882  0.0170542   113 TYR   B HE2  
1465 N N    . GLY   A 102 ? 0.530667 0.463326 0.445289 0.0557989   0.0182758   0.075541    114 GLY   B N    
1466 C CA   . GLY   A 102 ? 0.521107 0.483475 0.492978 0.0638139   0.0359002   0.0863942   114 GLY   B CA   
1467 C C    . GLY   A 102 ? 0.545587 0.501453 0.507855 0.0899591   0.0451061   0.0862214   114 GLY   B C    
1468 O O    . GLY   A 102 ? 0.543648 0.468552 0.45691  0.0979073   0.0311129   0.0750761   114 GLY   B O    
1469 H H    . GLY   A 102 ? 0.514095 0.443937 0.428743 0.0423247   0.00060165  0.0691929   114 GLY   B H    
1470 H HA2  . GLY   A 102 ? 0.502245 0.480804 0.509237 0.0506387   0.0220982   0.0844493   114 GLY   B HA2  
1471 H HA3  . GLY   A 102 ? 0.524632 0.495069 0.509712 0.0657318   0.0564792   0.0960237   114 GLY   B HA3  
1472 N N    . SER   A 103 ? 0.557113 0.540616 0.570203 0.103679    0.0725938   0.098889    115 SER   B N    
1473 C CA   . SER   A 103 ? 0.581638 0.563044 0.596023 0.132179    0.0873293   0.100012    115 SER   B CA   
1474 C C    . SER   A 103 ? 0.632124 0.575249 0.570679 0.156936    0.111822    0.0984612   115 SER   B C    
1475 O O    . SER   A 103 ? 0.637575 0.557505 0.544565 0.180817    0.116566    0.0910535   115 SER   B O    
1476 C CB   . SER   A 103 ? 0.565579 0.595353 0.672177 0.138792    0.108853    0.113727    115 SER   B CB   
1477 O OG   . SER   A 103 ? 0.613295 0.651606 0.733017 0.148357    0.154424    0.129869    115 SER   B OG   
1478 H H    . SER   A 103 ? 0.542121 0.545696 0.592958 0.0953433   0.0841589   0.107105    115 SER   B H    
1479 H HA   . SER   A 103 ? 0.581476 0.551716 0.583926 0.132056    0.0647545   0.0912472   115 SER   B HA   
1480 H HB2  . SER   A 103 ? 0.588355 0.619867 0.70371  0.155863    0.109357    0.112264    115 SER   B HB2  
1481 H HB3  . SER   A 103 ? 0.544979 0.598257 0.696554 0.119923    0.0906478   0.113086    115 SER   B HB3  
1483 N N    . ALA   A 104 ? 0.65352  0.58462  0.555658 0.153166    0.12444     0.103948    116 ALA   B N    
1484 C CA   . ALA   A 104 ? 0.73471  0.626694 0.553927 0.179191    0.142365    0.101195    116 ALA   B CA   
1485 C C    . ALA   A 104 ? 0.738356 0.59018  0.488499 0.175525    0.10519     0.0774208   116 ALA   B C    
1486 O O    . ALA   A 104 ? 0.829297 0.643317 0.511575 0.198024    0.108273    0.0655156   116 ALA   B O    
1487 C CB   . ALA   A 104 ? 0.720352 0.611557 0.522155 0.180964    0.16734     0.118203    116 ALA   B CB   
1488 H H    . ALA   A 104 ? 0.629317 0.574389 0.555363 0.13613     0.121031    0.109084    116 ALA   B H    
1489 H HA   . ALA   A 104 ? 0.751871 0.642257 0.572726 0.200228    0.163771    0.103798    116 ALA   B HA   
1490 H HB1  . ALA   A 104 ? 0.725267 0.639216 0.574389 0.183089    0.194559    0.133672    116 ALA   B HB1  
1491 H HB2  . ALA   A 104 ? 0.701033 0.595548 0.507357 0.161722    0.148195    0.116445    116 ALA   B HB2  
1492 H HB3  . ALA   A 104 ? 0.776736 0.639602 0.515219 0.200193    0.175945    0.115887    116 ALA   B HB3  
1493 N N    . GLY   A 105 ? 0.707372 0.565105 0.475232 0.146617    0.0709544   0.069285    117 GLY   B N    
1494 C CA   . GLY   A 105 ? 0.719512 0.54344  0.435688 0.138409    0.0393243   0.0489988   117 GLY   B CA   
1495 C C    . GLY   A 105 ? 0.76964  0.574656 0.427208 0.145803    0.0377984   0.0454195   117 GLY   B C    
1496 O O    . GLY   A 105 ? 0.752454 0.571568 0.412738 0.15171     0.0588223   0.0622926   117 GLY   B O    
1497 H H    . GLY   A 105 ? 0.667093 0.54952  0.480807 0.131471    0.0680301   0.0759695   117 GLY   B H    
1498 H HA2  . GLY   A 105 ? 0.689761 0.522902 0.429555 0.117506    0.0213719   0.0469816   117 GLY   B HA2  
1499 H HA3  . GLY   A 105 ? 0.750076 0.553121 0.446923 0.149572    0.0364568   0.0395354   117 GLY   B HA3  
1500 N N    . SER   A 106 ? 0.781313 0.553961 0.389691 0.144611    0.0106609   0.0238742   118 SER   B N    
1501 C CA   . SER   A 106 ? 0.838276 0.592007 0.387145 0.154819    -0.00032389 0.0162518   118 SER   B CA   
1502 C C    . SER   A 106 ? 0.925766 0.633716 0.412301 0.169201    -0.017812   -0.0106933  118 SER   B C    
1503 O O    . SER   A 106 ? 0.891359 0.584221 0.370277 0.152569    -0.0520378  -0.0315247  118 SER   B O    
1504 C CB   . SER   A 106 ? 0.796007 0.568281 0.368757 0.129593    -0.0253672  0.015592    118 SER   B CB   
1505 O OG   . SER   A 106 ? 0.85486  0.618808 0.379345 0.144407    -0.0329807  0.0159686   118 SER   B OG   
1506 H H    . SER   A 106 ? 0.78568  0.547245 0.399167 0.137291    -0.00277007 0.0135164   118 SER   B H    
1507 H HA   . SER   A 106 ? 0.860008 0.61661  0.392741 0.171726    0.0222076   0.0294875   118 SER   B HA   
1508 H HB2  . SER   A 106 ? 0.758312 0.555098 0.374162 0.118152    -0.0150701  0.0292912   118 SER   B HB2  
1509 H HB3  . SER   A 106 ? 0.792551 0.557411 0.372591 0.115043    -0.0465582  0.00143468  118 SER   B HB3  
1511 N N    . LEU   A 107 ? 0.982362 0.668522 0.431232 0.199824    0.0093528   -0.0100265  119 LEU   B N    
1512 C CA   . LEU   A 107 ? 1.11353  0.752543 0.513399 0.215809    0.00177099  -0.0351769  119 LEU   B CA   
1513 C C    . LEU   A 107 ? 1.23543  0.835681 0.556212 0.223612    -0.0292961  -0.061653   119 LEU   B C    
1514 O O    . LEU   A 107 ? 1.2047   0.805456 0.477943 0.239337    -0.0272834  -0.0550845  119 LEU   B O    
1515 C CB   . LEU   A 107 ? 1.18538  0.814946 0.56726  0.251104    0.0464088   -0.0247101  119 LEU   B CB   
1516 C CG   . LEU   A 107 ? 1.14726  0.814454 0.612955 0.248038    0.0727634   -0.00359176 119 LEU   B CG   
1517 C CD1  . LEU   A 107 ? 1.17996  0.834606 0.624033 0.287634    0.118027    0.00303234  119 LEU   B CD1  
1518 C CD2  . LEU   A 107 ? 1.06235  0.72726  0.573882 0.22754     0.0480116   -0.0129015  119 LEU   B CD2  
1519 H H    . LEU   A 107 ? 0.996248 0.696396 0.451837 0.211706    0.0361034   0.00708922  119 LEU   B H    
1520 H HA   . LEU   A 107 ? 1.08585  0.723662 0.518677 0.199184    -0.0116319  -0.0417932  119 LEU   B HA   
1521 H HB2  . LEU   A 107 ? 1.20688  0.839499 0.55998  0.266136    0.0643563   -0.0137249  119 LEU   B HB2  
1522 H HB3  . LEU   A 107 ? 1.23797  0.829328 0.574979 0.2657      0.0421191   -0.0437198  119 LEU   B HB3  
1523 H HG   . LEU   A 107 ? 1.08455  0.787025 0.590515 0.235975    0.0798811   0.0142811   119 LEU   B HG   
1524 H HD11 . LEU   A 107 ? 1.21041  0.868741 0.629858 0.30005     0.139038    0.0141725   119 LEU   B HD11 
1525 H HD12 . LEU   A 107 ? 1.15373  0.835376 0.657246 0.286792    0.132126    0.0153117   119 LEU   B HD12 
1526 H HD13 . LEU   A 107 ? 1.2408   0.855693 0.636919 0.302186    0.11265     -0.016024   119 LEU   B HD13 
1527 H HD21 . LEU   A 107 ? 1.0395   0.713163 0.566157 0.203       0.0245563   -0.0152037  119 LEU   B HD21 
1528 H HD22 . LEU   A 107 ? 1.12114  0.748442 0.596824 0.238277    0.0417362   -0.0301162  119 LEU   B HD22 
1529 H HD23 . LEU   A 107 ? 1.04612  0.736565 0.607002 0.229263    0.0625333   0.00105168  119 LEU   B HD23 
1530 N N    . PRO   A 108 ? 1.25264  0.812762 0.55231  0.216315    -0.0585989  -0.0929713  120 PRO   B N    
1531 C CA   . PRO   A 108 ? 1.1916   0.742568 0.539797 0.200724    -0.0594053  -0.0975551  120 PRO   B CA   
1532 C C    . PRO   A 108 ? 1.12427  0.69842  0.539072 0.159067    -0.0858221  -0.0962116  120 PRO   B C    
1533 O O    . PRO   A 108 ? 1.05724  0.620189 0.507189 0.145874    -0.0866069  -0.0965079  120 PRO   B O    
1534 C CB   . PRO   A 108 ? 1.29936  0.784761 0.582706 0.217188    -0.0721711  -0.131604   120 PRO   B CB   
1535 C CG   . PRO   A 108 ? 1.41629  0.88106  0.625381 0.227214    -0.0985059  -0.15308    120 PRO   B CG   
1536 C CD   . PRO   A 108 ? 1.36682  0.880797 0.586537 0.227586    -0.0906705  -0.126125   120 PRO   B CD   
1537 H HA   . PRO   A 108 ? 1.18039  0.746223 0.552935 0.210751    -0.0324645  -0.0805958  120 PRO   B HA   
1538 H HB2  . PRO   A 108 ? 1.29845  0.768771 0.605883 0.19818     -0.0896677  -0.142938   120 PRO   B HB2  
1539 H HB3  . PRO   A 108 ? 1.33626  0.806619 0.600726 0.241335    -0.0463632  -0.12845    120 PRO   B HB3  
1540 H HG2  . PRO   A 108 ? 1.41061  0.862913 0.625908 0.207339    -0.131261   -0.172967   120 PRO   B HG2  
1541 H HG3  . PRO   A 108 ? 1.4735   0.90303  0.620937 0.254359    -0.0882441  -0.164909   120 PRO   B HG3  
1542 H HD2  . PRO   A 108 ? 1.34555  0.872517 0.579022 0.209084    -0.119596   -0.132484   120 PRO   B HD2  
1543 H HD3  . PRO   A 108 ? 1.41227  0.913557 0.576006 0.254093    -0.0764868  -0.123555   120 PRO   B HD3  
1544 N N    . LYS   A 109 ? 1.10813  0.713149 0.538871 0.141225    -0.104173   -0.0923115  121 LYS   B N    
1545 C CA   . LYS   A 109 ? 1.02808  0.655534 0.518797 0.103769    -0.125537   -0.0918228  121 LYS   B CA   
1546 C C    . LYS   A 109 ? 0.904115 0.55843  0.455793 0.0879184   -0.10642    -0.068238   121 LYS   B C    
1547 O O    . LYS   A 109 ? 0.790351 0.438672 0.375959 0.0634179   -0.116318   -0.0705968  121 LYS   B O    
1548 C CB   . LYS   A 109 ? 1.07142  0.733502 0.568435 0.097701    -0.139795   -0.0863971  121 LYS   B CB   
1549 C CG   . LYS   A 109 ? 1.11065  0.799989 0.66899  0.0628959   -0.160085   -0.0871942  121 LYS   B CG   
1550 C CD   . LYS   A 109 ? 1.21077  0.910627 0.762915 0.0593487   -0.194517   -0.102886   121 LYS   B CD   
1551 C CE   . LYS   A 109 ? 1.22714  0.946935 0.850143 0.0231527   -0.210949   -0.108461   121 LYS   B CE   
1552 N NZ   . LYS   A 109 ? 1.17715  0.903895 0.812512 0.0138382   -0.25124    -0.131684   121 LYS   B NZ   
1553 H H    . LYS   A 109 ? 1.11713  0.728696 0.519324 0.154749    -0.10128    -0.0887272  121 LYS   B H    
1554 H HA   . LYS   A 109 ? 1.06043  0.661142 0.546441 0.0935866   -0.144436   -0.111181   121 LYS   B HA   
1555 H HB2  . LYS   A 109 ? 1.12638  0.77085  0.578906 0.110927    -0.154655   -0.100985   121 LYS   B HB2  
1556 H HB3  . LYS   A 109 ? 1.05006  0.733846 0.552046 0.107148    -0.119343   -0.0668907  121 LYS   B HB3  
1557 H HG2  . LYS   A 109 ? 1.05714  0.774107 0.646535 0.0570116   -0.144731   -0.0682064  121 LYS   B HG2  
1558 H HG3  . LYS   A 109 ? 1.10533  0.77836  0.681729 0.0480191   -0.164801   -0.0954209  121 LYS   B HG3  
1559 H HD2  . LYS   A 109 ? 1.2597   0.931655 0.770419 0.0700851   -0.211226   -0.122482   121 LYS   B HD2  
1560 H HD3  . LYS   A 109 ? 1.19393  0.91481  0.739169 0.0705006   -0.188821   -0.0895231  121 LYS   B HD3  
1561 H HE2  . LYS   A 109 ? 1.14186  0.890231 0.796984 0.0164152   -0.197135   -0.090627   121 LYS   B HE2  
1562 H HE3  . LYS   A 109 ? 1.19245  0.892642 0.827814 0.0111891   -0.206024   -0.112892   121 LYS   B HE3  
1563 H HZ1  . LYS   A 109 ? 1.1979   0.945723 0.827388 0.0243081   -0.257018   -0.125334   121 LYS   B HZ1  
1564 H HZ2  . LYS   A 109 ? 1.25082  0.949306 0.851989 0.0208615   -0.26692    -0.150586   121 LYS   B HZ2  
1565 H HZ3  . LYS   A 109 ? 1.1783   0.91606  0.862525 -0.00888324 -0.255243   -0.133814   121 LYS   B HZ3  
1566 N N    . ILE   A 110 ? 0.85375  0.53923  0.420652 0.100406    -0.0800396  -0.0447235  122 ILE   B N    
1567 C CA   . ILE   A 110 ? 0.769266 0.480828 0.389349 0.0880634   -0.0674323  -0.0254377  122 ILE   B CA   
1568 C C    . ILE   A 110 ? 0.787069 0.497318 0.405108 0.114998    -0.0421386  -0.0158464  122 ILE   B C    
1569 O O    . ILE   A 110 ? 0.842378 0.5652   0.445981 0.135375    -0.0212114  -0.0072548  122 ILE   B O    
1570 C CB   . ILE   A 110 ? 0.723578 0.479279 0.380041 0.0743516   -0.0619492  -0.00815267 122 ILE   B CB   
1571 C CG1  . ILE   A 110 ? 0.716893 0.479747 0.373798 0.0572775   -0.0821859  -0.0162898  122 ILE   B CG1  
1572 C CG2  . ILE   A 110 ? 0.698754 0.474979 0.403059 0.0591473   -0.0568261  0.00557171  122 ILE   B CG2  
1573 C CD1  . ILE   A 110 ? 0.6764   0.437263 0.365264 0.0278043   -0.0973228  -0.0222968  122 ILE   B CD1  
1574 H H    . ILE   A 110 ? 0.869127 0.558639 0.41219  0.117053    -0.0703223  -0.0409286  122 ILE   B H    
1575 H HA   . ILE   A 110 ? 0.771857 0.470837 0.40449  0.0735232   -0.0779252  -0.0302397  122 ILE   B HA   
1576 H HB   . ILE   A 110 ? 0.731755 0.497824 0.380409 0.0896042   -0.0467355  0.00031461  122 ILE   B HB   
1577 H HG12 . ILE   A 110 ? 0.750594 0.496264 0.374201 0.0670293   -0.0921901  -0.0285177  122 ILE   B HG12 
1578 H HG13 . ILE   A 110 ? 0.690332 0.476106 0.359971 0.0573439   -0.0745218  -0.00503025 122 ILE   B HG13 
1579 H HG21 . ILE   A 110 ? 0.661665 0.460163 0.38655  0.0484434   -0.0554201  0.0127964   122 ILE   B HG21 
1580 H HG22 . ILE   A 110 ? 0.695483 0.455617 0.401168 0.0481488   -0.0674227  -0.00024541 122 ILE   B HG22 
1581 H HG23 . ILE   A 110 ? 0.694134 0.475733 0.406341 0.0720737   -0.0445133  0.0127625   122 ILE   B HG23 
1582 H HD11 . ILE   A 110 ? 0.648408 0.425536 0.363239 0.0188473   -0.088861   -0.0107614  122 ILE   B HD11 
1583 H HD12 . ILE   A 110 ? 0.680358 0.447594 0.373305 0.0196945   -0.109592   -0.0287958  122 ILE   B HD12 
1584 H HD13 . ILE   A 110 ? 0.703779 0.439187 0.382997 0.0267407   -0.102445   -0.0310184  122 ILE   B HD13 
1585 N N    . PRO   A 111 ? 0.778236 0.472164 0.410318 0.119033    -0.0407447  -0.0154956  123 PRO   B N    
1586 C CA   . PRO   A 111 ? 0.798172 0.497161 0.439147 0.147828    -0.0161836  -0.00610457 123 PRO   B CA   
1587 C C    . PRO   A 111 ? 0.773746 0.5272   0.475106 0.144213    -0.00188421 0.017073    123 PRO   B C    
1588 O O    . PRO   A 111 ? 0.760769 0.540062 0.489895 0.118942    -0.013106   0.0238644   123 PRO   B O    
1589 C CB   . PRO   A 111 ? 0.825702 0.486398 0.463458 0.152901    -0.0251164  -0.0136219  123 PRO   B CB   
1590 C CG   . PRO   A 111 ? 0.771392 0.423155 0.419949 0.119457    -0.0500326  -0.0158634  123 PRO   B CG   
1591 C CD   . PRO   A 111 ? 0.762722 0.431742 0.404636 0.0989008   -0.0597167  -0.021429   123 PRO   B CD   
1592 H HA   . PRO   A 111 ? 0.839252 0.526034 0.447331 0.166204    -0.00436655 -0.0115943  123 PRO   B HA   
1593 H HB2  . PRO   A 111 ? 0.809995 0.486247 0.47679  0.163901    -0.015669   -0.00211075 123 PRO   B HB2  
1594 H HB3  . PRO   A 111 ? 0.867435 0.493141 0.467761 0.166478    -0.0237055  -0.0279322  123 PRO   B HB3  
1595 H HG2  . PRO   A 111 ? 0.751515 0.423341 0.430882 0.112989    -0.0510223  -0.0025847  123 PRO   B HG2  
1596 H HG3  . PRO   A 111 ? 0.815601 0.429128 0.445075 0.118822    -0.0579776  -0.0266517  123 PRO   B HG3  
1597 H HD2  . PRO   A 111 ? 0.725123 0.415104 0.393345 0.080843    -0.0645729  -0.0127071  123 PRO   B HD2  
1598 H HD3  . PRO   A 111 ? 0.790831 0.432778 0.408992 0.0928443   -0.0718981  -0.0369048  123 PRO   B HD3  
1599 N N    . SER   A 112 ? 0.800342 0.570895 0.525153 0.169429    0.0239375   0.0276354   124 SER   B N    
1600 C CA   . SER   A 112 ? 0.775804 0.600141 0.569863 0.164895    0.0365097   0.0473242   124 SER   B CA   
1601 C C    . SER   A 112 ? 0.730604 0.572214 0.568858 0.146226    0.0107023   0.0515734   124 SER   B C    
1602 O O    . SER   A 112 ? 0.753071 0.567494 0.578206 0.150277    -0.00523021 0.0462291   124 SER   B O    
1603 C CB   . SER   A 112 ? 0.788065 0.630444 0.609577 0.194852    0.070968    0.057743    124 SER   B CB   
1604 O OG   . SER   A 112 ? 0.829856 0.654426 0.655148 0.215716    0.0690664   0.0530186   124 SER   B OG   
1605 H H    . SER   A 112 ? 0.840622 0.589076 0.541157 0.18951     0.0342103   0.0216116   124 SER   B H    
1606 H HA   . SER   A 112 ? 0.749534 0.587217 0.54402  0.153395    0.0394334   0.0512971   124 SER   B HA   
1607 H HB2  . SER   A 112 ? 0.761838 0.642205 0.636969 0.188345    0.0778788   0.0699469   124 SER   B HB2  
1608 H HB3  . SER   A 112 ? 0.823688 0.651744 0.608573 0.207615    0.0893819   0.0562097   124 SER   B HB3  
1610 N N    . ASN   A 113 ? 0.671501 0.551959 0.554031 0.125533    0.00607235  0.0607134   125 ASN   B N    
1611 C CA   . ASN   A 113 ? 0.644772 0.545037 0.564891 0.108828    -0.018585   0.0643536   125 ASN   B CA   
1612 C C    . ASN   A 113 ? 0.621257 0.482307 0.496349 0.0954274   -0.0435617  0.0560956   125 ASN   B C    
1613 O O    . ASN   A 113 ? 0.67549  0.530666 0.557009 0.0972021   -0.0615465  0.0594157   125 ASN   B O    
1614 C CB   . ASN   A 113 ? 0.646464 0.577348 0.624824 0.127335    -0.0177384  0.0731225   125 ASN   B CB   
1615 C CG   . ASN   A 113 ? 0.608817 0.584511 0.648275 0.135534    0.0111567   0.0834551   125 ASN   B CG   
1616 O OD1  . ASN   A 113 ? 0.664401 0.652234 0.732266 0.16203     0.0320999   0.0892212   125 ASN   B OD1  
1617 N ND2  . ASN   A 113 ? 0.593817 0.595413 0.663077 0.113713    0.0149228   0.0872659   125 ASN   B ND2  
1618 H H    . ASN   A 113 ? 0.66704  0.559401 0.552847 0.122526    0.0189323   0.0644221   125 ASN   B H    
1619 H HA   . ASN   A 113 ? 0.611551 0.532412 0.551635 0.0934984   -0.0188053  0.0670912   125 ASN   B HA   
1620 H HB2  . ASN   A 113 ? 0.669078 0.57855  0.629286 0.145219    -0.0153537  0.0711348   125 ASN   B HB2  
1621 H HB3  . ASN   A 113 ? 0.628885 0.570667 0.62544  0.117231    -0.0388464  0.0743226   125 ASN   B HB3  
1622 H HD21 . ASN   A 113 ? 0.578528 0.611427 0.700258 0.113717    0.0246611   0.0939636   125 ASN   B HD21 
1623 H HD22 . ASN   A 113 ? 0.579412 0.567043 0.619918 0.0990173   0.00815967  0.0831211   125 ASN   B HD22 
1624 N N    . ALA   A 114 ? 0.592292 0.428776 0.425896 0.0813694   -0.0445358  0.0471364   126 ALA   B N    
1625 C CA   . ALA   A 114 ? 0.599523 0.400838 0.399744 0.0652306   -0.0616341  0.0403554   126 ALA   B CA   
1626 C C    . ALA   A 114 ? 0.568066 0.383654 0.378981 0.0399173   -0.0727521  0.0438426   126 ALA   B C    
1627 O O    . ALA   A 114 ? 0.582213 0.425012 0.412119 0.0295621   -0.0671844  0.0449325   126 ALA   B O    
1628 C CB   . ALA   A 114 ? 0.592872 0.366135 0.355151 0.0628687   -0.0590623  0.0270558   126 ALA   B CB   
1629 H H    . ALA   A 114 ? 0.59445  0.437297 0.423235 0.0821406   -0.0335163  0.0461144   126 ALA   B H    
1630 H HA   . ALA   A 114 ? 0.617218 0.40059  0.412001 0.0741912   -0.0673324  0.0419481   126 ALA   B HA   
1631 H HB1  . ALA   A 114 ? 0.628323 0.386218 0.376062 0.0800692   -0.052933   0.0226744   126 ALA   B HB1  
1632 H HB2  . ALA   A 114 ? 0.583891 0.374297 0.349725 0.0577489   -0.0542411  0.0269078   126 ALA   B HB2  
1633 H HB3  . ALA   A 114 ? 0.609441 0.361459 0.358207 0.0499598   -0.0686383  0.0226198   126 ALA   B HB3  
1634 N N    . THR   A 115 ? 0.568635 0.358821 0.361025 0.0316585   -0.0856944  0.0459248   127 THR   B N    
1635 C CA   . THR   A 115 ? 0.560675 0.348796 0.3442   0.00926027  -0.0919022  0.0472442   127 THR   B CA   
1636 C C    . THR   A 115 ? 0.538097 0.299451 0.299606 -0.00717741 -0.0865503  0.0401013   127 THR   B C    
1637 O O    . THR   A 115 ? 0.572257 0.300218 0.316059 -0.00398076 -0.0867343  0.0361358   127 THR   B O    
1638 C CB   . THR   A 115 ? 0.629173 0.400654 0.398096 0.0145119   -0.106364   0.0565079   127 THR   B CB   
1639 O OG1  . THR   A 115 ? 0.628071 0.434589 0.43208  0.0289737   -0.115575   0.0604767   127 THR   B OG1  
1640 C CG2  . THR   A 115 ? 0.633625 0.393131 0.377905 -0.0038218  -0.110273   0.0589518   127 THR   B CG2  
1641 H H    . THR   A 115 ? 0.598588 0.368361 0.380323 0.0422042   -0.0886805  0.0474178   127 THR   B H    
1642 H HA   . THR   A 115 ? 0.537073 0.351218 0.339488 0.0034303   -0.090103   0.0469835   127 THR   B HA   
1643 H HB   . THR   A 115 ? 0.651559 0.394617 0.4033   0.0223963   -0.106607   0.0585633   127 THR   B HB   
1645 H HG21 . THR   A 115 ? 0.662162 0.408549 0.389972 0.00308724  -0.120802   0.0657806   127 THR   B HG21 
1646 H HG22 . THR   A 115 ? 0.611995 0.395806 0.371834 -0.0111252  -0.110342   0.055373    127 THR   B HG22 
1647 H HG23 . THR   A 115 ? 0.642037 0.380971 0.370848 -0.0142312  -0.101471   0.0572987   127 THR   B HG23 
1648 N N    . LEU   A 116 ? 0.52395  0.29988  0.292555 -0.0251926  -0.0819959  0.0375094   128 LEU   B N    
1649 C CA   . LEU   A 116 ? 0.527613 0.291605 0.293371 -0.0419172  -0.0770462  0.0307459   128 LEU   B CA   
1650 C C    . LEU   A 116 ? 0.554179 0.307786 0.311873 -0.0593658  -0.0707759  0.0361132   128 LEU   B C    
1651 O O    . LEU   A 116 ? 0.554971 0.320684 0.309431 -0.0600725  -0.0709412  0.0403843   128 LEU   B O    
1652 C CB   . LEU   A 116 ? 0.517337 0.310656 0.302848 -0.0438617  -0.0737365  0.0242436   128 LEU   B CB   
1653 C CG   . LEU   A 116 ? 0.564724 0.359167 0.344404 -0.0276498  -0.0768092  0.0171159   128 LEU   B CG   
1654 C CD1  . LEU   A 116 ? 0.563122 0.358361 0.338217 -0.00693601 -0.0740672  0.0223128   128 LEU   B CD1  
1655 C CD2  . LEU   A 116 ? 0.551159 0.372915 0.34356  -0.0268659  -0.07367    0.0160877   128 LEU   B CD2  
1656 H H    . LEU   A 116 ? 0.505719 0.301571 0.286047 -0.0270465  -0.0821089  0.0396413   128 LEU   B H    
1657 H HA   . LEU   A 116 ? 0.556212 0.297676 0.312544 -0.0400168  -0.07922    0.0270682   128 LEU   B HA   
1658 H HB2  . LEU   A 116 ? 0.503064 0.31576  0.299024 -0.0429784  -0.0707228  0.0282056   128 LEU   B HB2  
1659 H HB3  . LEU   A 116 ? 0.519964 0.311836 0.311321 -0.0563265  -0.0717636  0.0210804   128 LEU   B HB3  
1660 H HG   . LEU   A 116 ? 0.577638 0.351956 0.347812 -0.030667   -0.0821981  0.00959647  128 LEU   B HG   
1661 H HD11 . LEU   A 116 ? 0.586261 0.359487 0.35     -0.00366212 -0.0776998  0.0217081   128 LEU   B HD11 
1662 H HD12 . LEU   A 116 ? 0.571053 0.370197 0.340535 0.00463316  -0.0709109  0.0193483   128 LEU   B HD12 
1663 H HD13 . LEU   A 116 ? 0.548105 0.361189 0.338271 -0.00731341 -0.0712433  0.0293548   128 LEU   B HD13 
1664 H HD21 . LEU   A 116 ? 0.544653 0.368242 0.345433 -0.0386658  -0.0761595  0.0124468   128 LEU   B HD21 
1665 H HD22 . LEU   A 116 ? 0.530442 0.368653 0.334795 -0.0257844  -0.0671146  0.0231099   128 LEU   B HD22 
1666 H HD23 . LEU   A 116 ? 0.561497 0.380778 0.341612 -0.0146295  -0.0754177  0.0123332   128 LEU   B HD23 
1667 N N    . PHE   A 117 ? 0.593905 0.326133 0.351671 -0.0739001  -0.0639423  0.0338424   129 PHE   B N    
1668 C CA   . PHE   A 117 ? 0.625629 0.34512  0.378777 -0.0908772  -0.0491702  0.0397206   129 PHE   B CA   
1669 C C    . PHE   A 117 ? 0.623938 0.363459 0.415352 -0.106131   -0.0419259  0.0307891   129 PHE   B C    
1670 O O    . PHE   A 117 ? 0.642938 0.383107 0.453821 -0.108375   -0.0511956  0.0206936   129 PHE   B O    
1671 C CB   . PHE   A 117 ? 0.72764  0.399134 0.454811 -0.094942   -0.0424995  0.0497725   129 PHE   B CB   
1672 C CG   . PHE   A 117 ? 0.788943 0.442316 0.505211 -0.110833   -0.0191606  0.0598397   129 PHE   B CG   
1673 C CD1  . PHE   A 117 ? 0.848549 0.48644  0.519449 -0.104395   -0.0136519  0.071485    129 PHE   B CD1  
1674 C CD2  . PHE   A 117 ? 0.786659 0.438892 0.538378 -0.131198   -0.00228331 0.0570461   129 PHE   B CD2  
1675 C CE1  . PHE   A 117 ? 0.861603 0.477732 0.511824 -0.115574   0.0131832   0.0813781   129 PHE   B CE1  
1676 C CE2  . PHE   A 117 ? 0.831768 0.46856  0.577202 -0.144259   0.0267277   0.0683684   129 PHE   B CE2  
1677 C CZ   . PHE   A 117 ? 0.828453 0.445241 0.51807  -0.135314   0.037004    0.0809612   129 PHE   B CZ   
1678 H H    . PHE   A 117 ? 0.598479 0.323    0.361125 -0.0730767  -0.0676934  0.027726    129 PHE   B H    
1679 H HA   . PHE   A 117 ? 0.628538 0.356695 0.371874 -0.0892693  -0.0469415  0.0433284   129 PHE   B HA   
1680 H HB2  . PHE   A 117 ? 0.737496 0.397088 0.441227 -0.0821812  -0.050157   0.0559534   129 PHE   B HB2  
1681 H HB3  . PHE   A 117 ? 0.729987 0.390558 0.469816 -0.0983623  -0.0450253  0.0441229   129 PHE   B HB3  
1682 H HD1  . PHE   A 117 ? 0.833018 0.475093 0.486348 -0.0915225  -0.0282957  0.0721773   129 PHE   B HD1  
1683 H HD2  . PHE   A 117 ? 0.776913 0.439639 0.558473 -0.135724   -0.0102452  0.047046    129 PHE   B HD2  
1684 H HE1  . PHE   A 117 ? 0.886395 0.488425 0.496702 -0.109055   0.0152771   0.0879047   129 PHE   B HE1  
1685 H HE2  . PHE   A 117 ? 0.821613 0.462257 0.601197 -0.158695   0.0395734   0.0667444   129 PHE   B HE2  
1686 H HZ   . PHE   A 117 ? 0.872873 0.474874 0.551054 -0.14223    0.0598218   0.0891725   129 PHE   B HZ   
1687 N N    . PHE   A 118 ? 0.587394 0.3427   0.389276 -0.114915   -0.0270108  0.0331475   130 PHE   B N    
1688 C CA   . PHE   A 118 ? 0.585478 0.36355  0.431468 -0.127725   -0.0179352  0.0272062   130 PHE   B CA   
1689 C C    . PHE   A 118 ? 0.626808 0.392569 0.47233  -0.140959   0.0104996   0.0357166   130 PHE   B C    
1690 O O    . PHE   A 118 ? 0.609248 0.358543 0.413964 -0.136548   0.0217526   0.0432086   130 PHE   B O    
1691 C CB   . PHE   A 118 ? 0.537658 0.355351 0.408646 -0.12001    -0.0237342  0.0209053   130 PHE   B CB   
1692 C CG   . PHE   A 118 ? 0.522    0.35279  0.392587 -0.10536    -0.0454904  0.0144399   130 PHE   B CG   
1693 C CD1  . PHE   A 118 ? 0.551721 0.380973 0.396394 -0.0905045  -0.0511738  0.0181841   130 PHE   B CD1  
1694 C CD2  . PHE   A 118 ? 0.512612 0.3578   0.408753 -0.105296   -0.0595744  0.00464192  130 PHE   B CD2  
1695 C CE1  . PHE   A 118 ? 0.531435 0.369815 0.372386 -0.0751041  -0.0631209  0.0148169   130 PHE   B CE1  
1696 C CE2  . PHE   A 118 ? 0.553997 0.404385 0.434976 -0.0883008  -0.076769   -0.00062488 130 PHE   B CE2  
1697 C CZ   . PHE   A 118 ? 0.536785 0.382558 0.388606 -0.072699   -0.074685   0.00583551  130 PHE   B CZ   
1698 H H    . PHE   A 118 ? 0.601764 0.353538 0.383258 -0.111655   -0.0230455  0.0379215   130 PHE   B H    
1699 H HA   . PHE   A 118 ? 0.591871 0.365768 0.454845 -0.132833   -0.0248675  0.0220003   130 PHE   B HA   
1700 H HB2  . PHE   A 118 ? 0.535677 0.354765 0.391964 -0.116177   -0.0173654  0.0243231   130 PHE   B HB2  
1701 H HB3  . PHE   A 118 ? 0.534766 0.367057 0.437134 -0.127635   -0.0173085  0.0183358   130 PHE   B HB3  
1702 H HD1  . PHE   A 118 ? 0.543773 0.365415 0.373669 -0.0904712  -0.0464401  0.0230389   130 PHE   B HD1  
1703 H HD2  . PHE   A 118 ? 0.528109 0.379077 0.451463 -0.116332   -0.057547   0.00130626  130 PHE   B HD2  
1704 H HE1  . PHE   A 118 ? 0.530426 0.370096 0.361035 -0.0655824  -0.0633336  0.0185084   130 PHE   B HE1  
1705 H HE2  . PHE   A 118 ? 0.547243 0.404726 0.438513 -0.086809   -0.0894282  -0.00859827 130 PHE   B HE2  
1706 H HZ   . PHE   A 118 ? 0.542878 0.390627 0.382883 -0.0600379  -0.081556   0.00380482  130 PHE   B HZ   
1707 N N    . GLU   A 119 ? 0.647247 0.421023 0.540187 -0.15686    0.0212303   0.033226    131 GLU   B N    
1708 C CA   . GLU   A 119 ? 0.684958 0.46478  0.603572 -0.169019   0.0532381   0.039076    131 GLU   B CA   
1709 C C    . GLU   A 119 ? 0.651828 0.481907 0.630681 -0.167862   0.0473017   0.0286386   131 GLU   B C    
1710 O O    . GLU   A 119 ? 0.656882 0.50959  0.677391 -0.170154   0.0238879   0.0181931   131 GLU   B O    
1711 C CB   . GLU   A 119 ? 0.735375 0.489001 0.675639 -0.188365   0.0717099   0.0462916   131 GLU   B CB   
1712 C CG   . GLU   A 119 ? 0.794775 0.553596 0.766791 -0.20127    0.113644    0.0554746   131 GLU   B CG   
1713 C CD   . GLU   A 119 ? 0.835017 0.56578  0.836078 -0.223116   0.138794    0.0660042   131 GLU   B CD   
1714 O OE1  . GLU   A 119 ? 0.839343 0.521522 0.791467 -0.22555    0.17054     0.0853188   131 GLU   B OE1  
1715 O OE2  . GLU   A 119 ? 0.854366 0.614111 0.933242 -0.238098   0.124865    0.0538832   131 GLU   B OE2  
1716 H H    . GLU   A 119 ? 0.64594  0.421912 0.558787 -0.160165   0.00815738  0.0268217   131 GLU   B H    
1717 H HA   . GLU   A 119 ? 0.696512 0.463172 0.577993 -0.163396   0.0659287   0.0452045   131 GLU   B HA   
1718 H HB2  . GLU   A 119 ? 0.769975 0.488415 0.666763 -0.18555    0.0728662   0.054285    131 GLU   B HB2  
1719 H HB3  . GLU   A 119 ? 0.730216 0.495915 0.708138 -0.194879   0.0556516   0.0371971   131 GLU   B HB3  
1720 H HG2  . GLU   A 119 ? 0.755968 0.552006 0.776627 -0.202593   0.111651    0.0477003   131 GLU   B HG2  
1721 H HG3  . GLU   A 119 ? 0.800726 0.54403  0.727726 -0.193205   0.129192    0.0627156   131 GLU   B HG3  
1722 N N    . ILE   A 120 ? 0.631251 0.474574 0.608213 -0.161457   0.066059    0.0306775   132 ILE   B N    
1723 C CA   . ILE   A 120 ? 0.58142  0.467858 0.610114 -0.15521    0.0631895   0.0239756   132 ILE   B CA   
1724 C C    . ILE   A 120 ? 0.550833 0.448232 0.616912 -0.161697   0.101692    0.028389    132 ILE   B C    
1725 O O    . ILE   A 120 ? 0.539858 0.407391 0.559962 -0.16095    0.13067     0.0349529   132 ILE   B O    
1726 C CB   . ILE   A 120 ? 0.567693 0.457201 0.561821 -0.137219   0.0502497   0.0213815   132 ILE   B CB   
1727 C CG1  . ILE   A 120 ? 0.55296  0.433087 0.514712 -0.129637   0.0194104   0.0192426   132 ILE   B CG1  
1728 C CG2  . ILE   A 120 ? 0.539525 0.466771 0.583477 -0.127602   0.0493295   0.0177933   132 ILE   B CG2  
1729 C CD1  . ILE   A 120 ? 0.52349  0.407355 0.461194 -0.114624   0.00950172  0.0188178   132 ILE   B CD1  
1730 H H    . ILE   A 120 ? 0.651883 0.473584 0.590868 -0.159553   0.0808814   0.0363121   132 ILE   B H    
1731 H HA   . ILE   A 120 ? 0.56319  0.4687   0.626953 -0.157375   0.0449118   0.0184173   132 ILE   B HA   
1732 H HB   . ILE   A 120 ? 0.582177 0.452176 0.542214 -0.136039   0.0649294   0.024099    132 ILE   B HB   
1733 H HG12 . ILE   A 120 ? 0.542611 0.436713 0.529597 -0.13009    0.00456409  0.0150731   132 ILE   B HG12 
1734 H HG13 . ILE   A 120 ? 0.570385 0.426041 0.503057 -0.13393    0.0211043   0.0224569   132 ILE   B HG13 
1735 H HG21 . ILE   A 120 ? 0.530872 0.45602  0.554485 -0.117365   0.0434605   0.017408    132 ILE   B HG21 
1736 H HG22 . ILE   A 120 ? 0.528825 0.476036 0.604796 -0.12762    0.0323375   0.0146973   132 ILE   B HG22 
1737 H HG23 . ILE   A 120 ? 0.54992  0.481983 0.614221 -0.130588   0.0718047   0.0192158   132 ILE   B HG23 
1738 H HD11 . ILE   A 120 ? 0.53771  0.408554 0.453528 -0.115014   0.0211354   0.0200581   132 ILE   B HD11 
1739 H HD12 . ILE   A 120 ? 0.524264 0.401574 0.443568 -0.110161   -0.00512495 0.0188284   132 ILE   B HD12 
1740 H HD13 . ILE   A 120 ? 0.511494 0.415884 0.474694 -0.108501   0.00664922  0.0174177   132 ILE   B HD13 
1741 N N    . GLU   A 121 ? 0.519571 0.460236 0.66723  -0.165369   0.100054    0.0240059   133 GLU   B N    
1742 C CA   . GLU   A 121 ? 0.566268 0.531209 0.767962 -0.16578    0.13513     0.0270321   133 GLU   B CA   
1743 C C    . GLU   A 121 ? 0.576276 0.578391 0.811603 -0.146488   0.120949    0.021404    133 GLU   B C    
1744 O O    . GLU   A 121 ? 0.593566 0.62922  0.872297 -0.142082   0.0860502   0.0155016   133 GLU   B O    
1745 C CB   . GLU   A 121 ? 0.54721  0.537337 0.83459  -0.18624    0.146347    0.028236    133 GLU   B CB   
1746 C CG   . GLU   A 121 ? 0.546211 0.57195  0.910568 -0.186153   0.184937    0.0320792   133 GLU   B CG   
1747 C CD   . GLU   A 121 ? 0.541317 0.59692  1.00714  -0.210044   0.199466    0.0340044   133 GLU   B CD   
1748 O OE1  . GLU   A 121 ? 0.510349 0.545815 0.975194 -0.229917   0.185394    0.0331804   133 GLU   B OE1  
1749 O OE2  . GLU   A 121 ? 0.500879 0.600347 1.05286  -0.208593   0.224599    0.0356932   133 GLU   B OE2  
1750 H H    . GLU   A 121 ? 0.516919 0.473443 0.688826 -0.166464   0.0748504   0.0182972   133 GLU   B H    
1751 H HA   . GLU   A 121 ? 0.585878 0.524381 0.747022 -0.164502   0.162344    0.0323746   133 GLU   B HA   
1752 H HB2  . GLU   A 121 ? 0.577992 0.538335 0.840828 -0.198117   0.159481    0.034098    133 GLU   B HB2  
1753 H HB3  . GLU   A 121 ? 0.532441 0.544646 0.853149 -0.18807    0.114452    0.0204202   133 GLU   B HB3  
1754 H HG2  . GLU   A 121 ? 0.521228 0.576309 0.912755 -0.172814   0.170247    0.026963    133 GLU   B HG2  
1755 H HG3  . GLU   A 121 ? 0.569445 0.569698 0.893192 -0.182141   0.217885    0.0386113   133 GLU   B HG3  
1756 N N    . LEU   A 122 ? 0.610112 0.602196 0.823167 -0.133688   0.148264    0.0230198   134 LEU   B N    
1757 C CA   . LEU   A 122 ? 0.586941 0.606632 0.833098 -0.11387    0.142054    0.0202253   134 LEU   B CA   
1758 C C    . LEU   A 122 ? 0.597567 0.661695 0.938767 -0.112253   0.164262    0.0218566   134 LEU   B C    
1759 O O    . LEU   A 122 ? 0.612229 0.667652 0.961744 -0.113973   0.210409    0.0250359   134 LEU   B O    
1760 C CB   . LEU   A 122 ? 0.607209 0.58997  0.788209 -0.10157    0.160015    0.0182007   134 LEU   B CB   
1761 C CG   . LEU   A 122 ? 0.581021 0.578722 0.787699 -0.0800912  0.158252    0.0165629   134 LEU   B CG   
1762 C CD1  . LEU   A 122 ? 0.55876  0.579124 0.780875 -0.0703764  0.115159    0.0190333   134 LEU   B CD1  
1763 C CD2  . LEU   A 122 ? 0.595609 0.548407 0.736548 -0.0728665  0.174404    0.010615    134 LEU   B CD2  
1764 H H    . LEU   A 122 ? 0.62889  0.592603 0.801873 -0.136408   0.17133     0.0257625   134 LEU   B H    
1765 H HA   . LEU   A 122 ? 0.568115 0.600704 0.818708 -0.108598   0.110187    0.0183777   134 LEU   B HA   
1766 H HB2  . LEU   A 122 ? 0.601614 0.561542 0.731914 -0.103736   0.143744    0.0170628   134 LEU   B HB2  
1767 H HB3  . LEU   A 122 ? 0.632121 0.597619 0.798495 -0.105461   0.190699    0.0188519   134 LEU   B HB3  
1768 H HG   . LEU   A 122 ? 0.587758 0.60841  0.846295 -0.0757659  0.176121    0.0178316   134 LEU   B HG   
1769 H HD11 . LEU   A 122 ? 0.544777 0.595105 0.812449 -0.0727492  0.102533    0.0200043   134 LEU   B HD11 
1770 H HD12 . LEU   A 122 ? 0.555004 0.576878 0.784346 -0.0558879  0.116037    0.0203869   134 LEU   B HD12 
1771 H HD13 . LEU   A 122 ? 0.551308 0.553002 0.729631 -0.0751967  0.0996892   0.0184459   134 LEU   B HD13 
1772 H HD21 . LEU   A 122 ? 0.627262 0.561764 0.748904 -0.0767693  0.201473    0.00816014  134 LEU   B HD21 
1773 H HD22 . LEU   A 122 ? 0.593457 0.528314 0.692024 -0.0770377  0.155943    0.00937042  134 LEU   B HD22 
1774 H HD23 . LEU   A 122 ? 0.596112 0.554894 0.756925 -0.0596108  0.176017    0.0101363   134 LEU   B HD23 
1775 N N    . LEU   A 123 ? 0.602883 0.715156 1.0147   -0.105747   0.13108     0.0195448   135 LEU   B N    
1776 C CA   . LEU   A 123 ? 0.59535  0.761406 1.11662  -0.106337   0.14252     0.0201728   135 LEU   B CA   
1777 C C    . LEU   A 123 ? 0.623842 0.806756 1.17563  -0.0801134  0.16283     0.0231746   135 LEU   B C    
1778 O O    . LEU   A 123 ? 0.657945 0.858655 1.26615  -0.0787575  0.20535     0.0261061   135 LEU   B O    
1779 C CB   . LEU   A 123 ? 0.566265 0.777033 1.15007  -0.110048   0.0904276   0.0135385   135 LEU   B CB   
1780 C CG   . LEU   A 123 ? 0.592203 0.785689 1.15632  -0.135477   0.0676613   0.00714279  135 LEU   B CG   
1781 C CD1  . LEU   A 123 ? 0.595444 0.829782 1.21324  -0.134428   0.0102226   -0.0045613  135 LEU   B CD1  
1782 C CD2  . LEU   A 123 ? 0.603246 0.787987 1.20118  -0.162743   0.10998     0.011369    135 LEU   B CD2  
1783 H H    . LEU   A 123 ? 0.57937  0.691735 0.971318 -0.0998066  0.100006    0.0175447   135 LEU   B H    
1784 H HA   . LEU   A 123 ? 0.616364 0.777072 1.15279  -0.120929   0.172607    0.0227229   135 LEU   B HA   
1785 H HB2  . LEU   A 123 ? 0.562329 0.775255 1.12414  -0.0931157  0.0631613   0.0128778   135 LEU   B HB2  
1786 H HB3  . LEU   A 123 ? 0.572681 0.823837 1.23761  -0.110147   0.0962949   0.0133767   135 LEU   B HB3  
1787 H HG   . LEU   A 123 ? 0.588598 0.744599 1.07565  -0.133231   0.0617012   0.00782449  135 LEU   B HG   
1788 H HD11 . LEU   A 123 ? 0.584875 0.818413 1.16982  -0.115211   -0.0135908  -0.00463436 135 LEU   B HD11 
1789 H HD12 . LEU   A 123 ? 0.598417 0.816685 1.20031  -0.150023   -0.0039862  -0.0106408  135 LEU   B HD12 
1790 H HD13 . LEU   A 123 ? 0.590941 0.866615 1.29109  -0.136503   0.0114796   -0.00613592 135 LEU   B HD13 
1791 H HD21 . LEU   A 123 ? 0.619454 0.772354 1.16822  -0.161034   0.143254    0.0182819   135 LEU   B HD21 
1792 H HD22 . LEU   A 123 ? 0.606455 0.829826 1.28632  -0.165847   0.120393    0.011494    135 LEU   B HD22 
1793 H HD23 . LEU   A 123 ? 0.612005 0.782665 1.19881  -0.178037   0.0940984   0.00739476  135 LEU   B HD23 
1794 N N    . ASP   A 124 ? 0.603078 0.778424 1.11967  -0.058275   0.134604    0.0236232   136 ASP   B N    
1795 C CA   . ASP   A 124 ? 0.605189 0.791216 1.14889  -0.0301252  0.146494    0.0275544   136 ASP   B CA   
1796 C C    . ASP   A 124 ? 0.598898 0.748412 1.06608  -0.0148291  0.122663    0.0300019   136 ASP   B C    
1797 O O    . ASP   A 124 ? 0.532248 0.664035 0.945182 -0.0243705  0.0930607   0.0288876   136 ASP   B O    
1798 C CB   . ASP   A 124 ? 0.573492 0.826874 1.22656  -0.016337   0.124005    0.0300332   136 ASP   B CB   
1799 C CG   . ASP   A 124 ? 0.625911 0.902315 1.34182  0.0114295   0.151       0.035403    136 ASP   B CG   
1800 O OD1  . ASP   A 124 ? 0.683055 0.919769 1.36023  0.018878    0.19632     0.0351792   136 ASP   B OD1  
1801 O OD2  . ASP   A 124 ? 0.651147 0.98607  1.45854  0.0265428   0.125671    0.038351    136 ASP   B OD2  
1802 H H    . ASP   A 124 ? 0.595425 0.756084 1.06918  -0.0604465  0.10829     0.0223675   136 ASP   B H    
1803 H HA   . ASP   A 124 ? 0.620865 0.790588 1.15893  -0.0295779  0.185015    0.0270979   136 ASP   B HA   
1804 H HB2  . ASP   A 124 ? 0.584142 0.862829 1.28544  -0.0328517  0.126273    0.0271873   136 ASP   B HB2  
1805 H HB3  . ASP   A 124 ? 0.57766  0.838347 1.21947  -0.00850931 0.0849568   0.0307595   136 ASP   B HB3  
1806 N N    . PHE   A 125 ? 0.57518  0.711134 1.04148  0.00876831  0.139554    0.0337976   137 PHE   B N    
1807 C CA   . PHE   A 125 ? 0.592938 0.69831  1.00597  0.0247282   0.119873    0.0395761   137 PHE   B CA   
1808 C C    . PHE   A 125 ? 0.585288 0.697334 1.04126  0.0556657   0.132404    0.0471222   137 PHE   B C    
1809 O O    . PHE   A 125 ? 0.59555  0.707204 1.08449  0.0614497   0.171055    0.0428789   137 PHE   B O    
1810 C CB   . PHE   A 125 ? 0.60319  0.649362 0.927845 0.0111357   0.133853    0.0334643   137 PHE   B CB   
1811 C CG   . PHE   A 125 ? 0.643675 0.65438  0.945818 0.00720411  0.179131    0.0232228   137 PHE   B CG   
1812 C CD1  . PHE   A 125 ? 0.643172 0.646814 0.929169 -0.0121861  0.20271     0.0157479   137 PHE   B CD1  
1813 C CD2  . PHE   A 125 ? 0.69228  0.669641 0.981861 0.0241282   0.198784    0.0208843   137 PHE   B CD2  
1814 C CE1  . PHE   A 125 ? 0.721026 0.685969 0.971257 -0.0121047  0.244069    0.00571721  137 PHE   B CE1  
1815 C CE2  . PHE   A 125 ? 0.751619 0.690292 1.01102  0.0222686   0.238389    0.00728755  137 PHE   B CE2  
1816 C CZ   . PHE   A 125 ? 0.759809 0.69273  0.995798 0.00538682  0.260642    -0.00050295 137 PHE   B CZ   
1817 H H    . PHE   A 125 ? 0.600399 0.744177 1.10129  0.0151264   0.166483    0.0332401   137 PHE   B H    
1818 H HA   . PHE   A 125 ? 0.571177 0.691533 0.982264 0.0259835   0.0871357   0.0432644   137 PHE   B HA   
1819 H HB2  . PHE   A 125 ? 0.607455 0.63744  0.909547 0.0214061   0.122526    0.0386372   137 PHE   B HB2  
1820 H HB3  . PHE   A 125 ? 0.593596 0.637818 0.89318  -0.00500602 0.12154     0.0307887   137 PHE   B HB3  
1821 H HD1  . PHE   A 125 ? 0.639173 0.660934 0.934887 -0.0245633  0.191201    0.0176324   137 PHE   B HD1  
1822 H HD2  . PHE   A 125 ? 0.6888   0.666533 0.988011 0.0379653   0.185665    0.0283727   137 PHE   B HD2  
1823 H HE1  . PHE   A 125 ? 0.730326 0.687603 0.963456 -0.0232475  0.261577    0.00292233  137 PHE   B HE1  
1824 H HE2  . PHE   A 125 ? 0.768766 0.681427 1.02002  0.0336211   0.250756    0.00352606  137 PHE   B HE2  
1825 H HZ   . PHE   A 125 ? 0.794962 0.697832 1.00107  0.00619646  0.287565    -0.00999684 137 PHE   B HZ   
1826 N N    . LYS   A 126 ? 0.57731  0.692542 1.02921  0.0777261   0.101176    0.0596056   138 LYS   B N    
1827 C CA   . LYS   A 126 ? 0.604209 0.725119 1.0963   0.11196     0.105485    0.0714526   138 LYS   B CA   
1828 C C    . LYS   A 126 ? 0.621996 0.686854 1.04982  0.124273    0.10684     0.0815684   138 LYS   B C    
1829 O O    . LYS   A 126 ? 0.55696  0.601918 0.927392 0.114537    0.0862797   0.0854322   138 LYS   B O    
1830 C CB   . LYS   A 126 ? 0.609649 0.79009  1.16227  0.130548    0.0616154   0.0807236   138 LYS   B CB   
1831 H H    . LYS   A 126 ? 0.572341 0.683146 0.991428 0.0726654   0.0771883   0.0619022   138 LYS   B H    
1832 H HA   . LYS   A 126 ? 0.615483 0.7373   1.13867  0.115273    0.135739    0.0666336   138 LYS   B HA   
1835 N N    . GLY   A 127 ? 0.704395 0.743387 1.1482   0.146882    0.133539    0.0866598   139 GLY   B N    
1836 C CA   . GLY   A 127 ? 0.749696 0.739445 1.15252  0.163574    0.133777    0.101236    139 GLY   B CA   
1837 C C    . GLY   A 127 ? 0.781096 0.792422 1.18375  0.188669    0.0932962   0.124653    139 GLY   B C    
1838 O O    . GLY   A 127 ? 0.7911   0.850313 1.24999  0.212314    0.0718882   0.132565    139 GLY   B O    
1839 H H    . GLY   A 127 ? 0.701615 0.751911 1.18417  0.152297    0.154282    0.0813698   139 GLY   B H    
1840 H HA2  . GLY   A 127 ? 0.748006 0.705614 1.10291  0.144673    0.138893    0.0953289   139 GLY   B HA2  
1841 H HA3  . GLY   A 127 ? 0.776589 0.747357 1.19812  0.17826     0.156776    0.1018      139 GLY   B HA3  
1842 N N    . GLU   A 128 ? 0.815739 0.790664 1.15439  0.185251    0.083265    0.136035    140 GLU   B N    
1843 C CA   . GLU   A 128 ? 0.894425 0.870512 1.21286  0.215094    0.0539576   0.162057    140 GLU   B CA   
1844 C C    . GLU   A 128 ? 0.972736 0.93239  1.3239   0.254879    0.065686    0.182218    140 GLU   B C    
1845 O O    . GLU   A 128 ? 0.99148  0.942095 1.38531  0.2562      0.0976097   0.171685    140 GLU   B O    
1846 C CB   . GLU   A 128 ? 0.845751 0.779472 1.09008  0.204003    0.053923    0.172252    140 GLU   B CB   
1847 O OXT  . GLU   A 128 ? 1.02588  0.979251 1.35473  0.286396    0.0432003   0.208505    140 GLU   B OXT  
1848 H H    . GLU   A 128 ? 0.811963 0.760418 1.118    0.164858    0.0956651   0.127957    140 GLU   B H    
1849 H HA   . GLU   A 128 ? 0.866197 0.883293 1.20025  0.218622    0.0253861   0.160175    140 GLU   B HA   
1852 N N    . THR   B 5   ? 1.17556  0.667268 0.633346 0.139738    0.302976    0.00185726  17  THR   A N    
1853 C CA   . THR   B 5   ? 1.13957  0.65523  0.616429 0.118183    0.259452    0.00321329  17  THR   A CA   
1854 C C    . THR   B 5   ? 1.12173  0.617746 0.596449 0.116992    0.2418      -0.00850857 17  THR   A C    
1855 O O    . THR   B 5   ? 1.13924  0.617881 0.622581 0.135953    0.260708    -0.0126933  17  THR   A O    
1856 C CB   . THR   B 5   ? 1.08447  0.664382 0.643569 0.117035    0.249011    0.0200113   17  THR   A CB   
1857 O OG1  . THR   B 5   ? 1.06738  0.674181 0.688805 0.130627    0.249116    0.0221233   17  THR   A OG1  
1858 C CG2  . THR   B 5   ? 1.02974  0.63047  0.605572 0.122052    0.273882    0.0341756   17  THR   A CG2  
1859 H H    . THR   B 5   ? 1.19504  0.691106 0.641715 0.13811     0.313974    0.00791477  17  THR   A H    
1860 H HA   . THR   B 5   ? 1.15955  0.659097 0.592742 0.104196    0.249057    0.00086021  17  THR   A HA   
1861 H HB   . THR   B 5   ? 1.04746  0.637417 0.607417 0.10238     0.224132    0.0207498   17  THR   A HB   
1863 H HG21 . THR   B 5   ? 1.00176  0.638027 0.624256 0.116973    0.262828    0.0432292   17  THR   A HG21 
1864 H HG22 . THR   B 5   ? 1.06361  0.664056 0.652228 0.137443    0.299056    0.0354826   17  THR   A HG22 
1865 H HG23 . THR   B 5   ? 1.08286  0.66119  0.609843 0.114663    0.276158    0.0334879   17  THR   A HG23 
1866 N N    . VAL   B 6   ? 1.10801  0.606723 0.57205  0.0950044   0.20649     -0.0120679  18  VAL   A N    
1867 C CA   . VAL   B 6   ? 1.08001  0.563431 0.542317 0.0883794   0.18649     -0.0208731  18  VAL   A CA   
1868 C C    . VAL   B 6   ? 0.955755 0.493492 0.485598 0.0826013   0.161298    -0.0110312  18  VAL   A C    
1869 O O    . VAL   B 6   ? 1.05648  0.635382 0.623526 0.0797763   0.155993    -0.00041963 18  VAL   A O    
1870 C CB   . VAL   B 6   ? 1.05478  0.494912 0.446768 0.0649103   0.167244    -0.0340996  18  VAL   A CB   
1871 C CG1  . VAL   B 6   ? 1.14457  0.520695 0.458549 0.0681143   0.190806    -0.0482366  18  VAL   A CG1  
1872 C CG2  . VAL   B 6   ? 1.0522   0.52037  0.440908 0.0439962   0.141544    -0.0270381  18  VAL   A CG2  
1873 H H    . VAL   B 6   ? 1.08927  0.601315 0.548802 0.0837279   0.195029    -0.00746204 18  VAL   A H    
1874 H HA   . VAL   B 6   ? 1.07965  0.546024 0.544704 0.102822    0.202087    -0.0240121  18  VAL   A HA   
1875 H HB   . VAL   B 6   ? 1.06159  0.49613  0.460856 0.0603201   0.15504     -0.037923   18  VAL   A HB   
1876 H HG11 . VAL   B 6   ? 1.15877  0.539123 0.462113 0.0727746   0.204571    -0.0440567  18  VAL   A HG11 
1877 H HG12 . VAL   B 6   ? 1.16308  0.518747 0.479904 0.0828963   0.207981    -0.0525906  18  VAL   A HG12 
1878 H HG13 . VAL   B 6   ? 1.17546  0.525739 0.44626  0.0505436   0.175469    -0.0569406  18  VAL   A HG13 
1879 H HG21 . VAL   B 6   ? 1.07879  0.522375 0.424878 0.0287816   0.128572    -0.034584   18  VAL   A HG21 
1880 H HG22 . VAL   B 6   ? 0.994614 0.498015 0.428639 0.0413543   0.126908    -0.0202427  18  VAL   A HG22 
1881 H HG23 . VAL   B 6   ? 1.05516  0.530059 0.438954 0.0485016   0.15295     -0.0211674  18  VAL   A HG23 
1882 N N    . THR   B 7   ? 0.989415 0.522416 0.529424 0.0793674   0.146196    -0.0150741  19  THR   A N    
1883 C CA   . THR   B 7   ? 0.90504  0.483889 0.501817 0.075059    0.125103    -0.00757768 19  THR   A CA   
1884 C C    . THR   B 7   ? 0.966743 0.561263 0.556946 0.0520947   0.0991513   -0.00757733 19  THR   A C    
1885 O O    . THR   B 7   ? 0.907049 0.543739 0.540673 0.0490091   0.0884589   0.00011795  19  THR   A O    
1886 C CB   . THR   B 7   ? 0.885878 0.452588 0.490928 0.0793056   0.118856    -0.00982703 19  THR   A CB   
1887 O OG1  . THR   B 7   ? 0.909772 0.450948 0.512353 0.101791    0.142368    -0.00997271 19  THR   A OG1  
1888 C CG2  . THR   B 7   ? 0.786    0.401697 0.446773 0.0766661   0.100461    -0.00167012 19  THR   A CG2  
1889 H H    . THR   B 7   ? 1.00902  0.506671 0.517212 0.0796393   0.150065    -0.0229137  19  THR   A H    
1890 H HA   . THR   B 7   ? 0.892064 0.500818 0.527227 0.0839287   0.131497    -3.102e-05  19  THR   A HA   
1891 H HB   . THR   B 7   ? 0.901405 0.443542 0.473686 0.0662638   0.109036    -0.0164873  19  THR   A HB   
1893 H HG21 . THR   B 7   ? 0.799474 0.408279 0.46523  0.0812046   0.0980206   -0.00103952 19  THR   A HG21 
1894 H HG22 . THR   B 7   ? 0.775063 0.418245 0.468727 0.0848667   0.106311    0.0044165   19  THR   A HG22 
1895 H HG23 . THR   B 7   ? 0.781687 0.407325 0.439436 0.0620195   0.0856292   -0.00292228 19  THR   A HG23 
1896 N N    . GLU   B 8   ? 1.04531  0.60568  0.583518 0.0356289   0.0883697   -0.0162983  20  GLU   A N    
1897 C CA   . GLU   B 8   ? 0.996363 0.57503  0.533659 0.0140718   0.0620346   -0.0147381  20  GLU   A CA   
1898 C C    . GLU   B 8   ? 0.982886 0.569279 0.502598 0.00884557  0.0605187   -0.00914065 20  GLU   A C    
1899 O O    . GLU   B 8   ? 1.03335  0.603537 0.510705 -0.00750164 0.0471233   -0.0117815  20  GLU   A O    
1900 C CB   . GLU   B 8   ? 0.974816 0.520823 0.473803 -0.00389792 0.0481137   -0.0243295  20  GLU   A CB   
1901 C CG   . GLU   B 8   ? 1.04731  0.575938 0.556127 0.00352649  0.0538562   -0.0278038  20  GLU   A CG   
1902 C CD   . GLU   B 8   ? 0.958811 0.530607 0.524959 0.00743007  0.0448833   -0.0194156  20  GLU   A CD   
1903 O OE1  . GLU   B 8   ? 0.813566 0.426968 0.411274 0.00052468  0.031892    -0.0134225  20  GLU   A OE1  
1904 O OE2  . GLU   B 8   ? 0.961334 0.520555 0.535575 0.0169212   0.0507426   -0.0190606  20  GLU   A OE2  
1905 H H    . GLU   B 8   ? 1.06928  0.59435  0.572757 0.0376986   0.0977623   -0.0232785  20  GLU   A H    
1906 H HA   . GLU   B 8   ? 0.941994 0.552389 0.52006  0.0150182   0.0544508   -0.0094758  20  GLU   A HA   
1907 H HB2  . GLU   B 8   ? 1.04935  0.563381 0.503942 -0.0085966  0.0522546   -0.0307141  20  GLU   A HB2  
1908 H HB3  . GLU   B 8   ? 0.98232  0.549295 0.49273  -0.0169266  0.0307587   -0.0212835  20  GLU   A HB3  
1909 H HG2  . GLU   B 8   ? 1.04355  0.554022 0.545835 0.0186522   0.0715224   -0.0294183  20  GLU   A HG2  
1910 H HG3  . GLU   B 8   ? 1.05432  0.555986 0.533782 -0.00926235 0.0469986   -0.0341787  20  GLU   A HG3  
1911 N N    . GLN   B 9   ? 0.949924 0.562275 0.50382  0.022202    0.0736335   0.00019735  21  GLN   A N    
1912 C CA   . GLN   B 9   ? 0.961206 0.57772  0.499525 0.0209215   0.0778082   0.00858001  21  GLN   A CA   
1913 C C    . GLN   B 9   ? 0.874979 0.535583 0.463239 0.0166656   0.0619221   0.0202354   21  GLN   A C    
1914 O O    . GLN   B 9   ? 0.720191 0.408191 0.359451 0.0207564   0.0583351   0.0209138   21  GLN   A O    
1915 C CB   . GLN   B 9   ? 0.996675 0.608362 0.541037 0.0392066   0.108563    0.0119259   21  GLN   A CB   
1916 C CG   . GLN   B 9   ? 0.960431 0.611173 0.576224 0.051296    0.11508     0.0185461   21  GLN   A CG   
1917 C CD   . GLN   B 9   ? 1.0104   0.671822 0.644816 0.0637464   0.140938    0.0278916   21  GLN   A CD   
1918 O OE1  . GLN   B 9   ? 0.993914 0.631728 0.585089 0.0653817   0.15748     0.0298953   21  GLN   A OE1  
1919 N NE2  . GLN   B 9   ? 0.968066 0.666349 0.666169 0.0703154   0.14362     0.0342041   21  GLN   A NE2  
1920 H H    . GLN   B 9   ? 0.923919 0.55271  0.512883 0.0314293   0.0792697   0.00232819  21  GLN   A H    
1921 H HA   . GLN   B 9   ? 0.99721  0.591651 0.491116 0.0110934   0.0713729   0.00516647  21  GLN   A HA   
1922 H HB2  . GLN   B 9   ? 1.01302  0.623594 0.541341 0.037743    0.113133    0.0181069   21  GLN   A HB2  
1923 H HB3  . GLN   B 9   ? 1.02968  0.612463 0.54523  0.0443309   0.120678    0.00400572  21  GLN   A HB3  
1924 H HG2  . GLN   B 9   ? 0.960608 0.606919 0.585322 0.0569561   0.117099    0.0132801   21  GLN   A HG2  
1925 H HG3  . GLN   B 9   ? 0.92847  0.602948 0.57143  0.0447521   0.100028    0.0224742   21  GLN   A HG3  
1926 H HE21 . GLN   B 9   ? 0.96752  0.675858 0.682949 0.0762353   0.158303    0.0404768   21  GLN   A HE21 
1927 H HE22 . GLN   B 9   ? 0.937541 0.650407 0.660048 0.067866    0.130607    0.0321422   21  GLN   A HE22 
1928 N N    . GLY   B 10  ? 0.818314 0.482152 0.387876 0.00905722  0.0529936   0.0293615   22  GLY   A N    
1929 C CA   . GLY   B 10  ? 0.77143  0.470439 0.38405  0.00671327  0.0394082   0.0413752   22  GLY   A CA   
1930 C C    . GLY   B 10  ? 0.804684 0.510965 0.404309 -0.00836328 0.0121628   0.0437477   22  GLY   A C    
1931 O O    . GLY   B 10  ? 0.781724 0.468061 0.342899 -0.0199746  0.00179621  0.0348244   22  GLY   A O    
1932 H H    . GLY   B 10  ? 0.874348 0.516304 0.401769 0.00578446  0.0557036   0.0283888   22  GLY   A H    
1933 H HA2  . GLY   B 10  ? 0.787591 0.488248 0.399587 0.0107131   0.0474465   0.0503853   22  GLY   A HA2  
1934 H HA3  . GLY   B 10  ? 0.74267  0.459556 0.395122 0.0110962   0.0404839   0.0398241   22  GLY   A HA3  
1935 N N    . GLU   B 11  ? 0.786564 0.522233 0.422652 -0.00799439 0.00128297  0.0566227   23  GLU   A N    
1936 C CA   . GLU   B 11  ? 0.760618 0.513278 0.397196 -0.0190186  -0.0238835  0.0644893   23  GLU   A CA   
1937 C C    . GLU   B 11  ? 0.724782 0.499539 0.400042 -0.0233905  -0.0339644  0.0572032   23  GLU   A C    
1938 O O    . GLU   B 11  ? 0.660245 0.449668 0.378641 -0.0144793  -0.0244237  0.0539014   23  GLU   A O    
1939 C CB   . GLU   B 11  ? 0.786341 0.557639 0.447901 -0.0118478  -0.0260013  0.0837299   23  GLU   A CB   
1940 C CG   . GLU   B 11  ? 0.847646 0.643646 0.520763 -0.0188775  -0.0518623  0.0969057   23  GLU   A CG   
1941 C CD   . GLU   B 11  ? 0.904743 0.719849 0.615242 -0.00774531 -0.0525973  0.116904    23  GLU   A CD   
1942 O OE1  . GLU   B 11  ? 1.01701  0.820969 0.734257 0.00235153  -0.0339786  0.122316    23  GLU   A OE1  
1943 O OE2  . GLU   B 11  ? 0.915935 0.757496 0.651794 -0.00912355 -0.0714519  0.128328    23  GLU   A OE2  
1944 H H    . GLU   B 11  ? 0.757411 0.503379 0.421679 -0.00011638 0.010401    0.0611738   23  GLU   A H    
1945 H HA   . GLU   B 11  ? 0.809074 0.545307 0.403895 -0.0280364  -0.0315217  0.0626417   23  GLU   A HA   
1946 H HB2  . GLU   B 11  ? 0.81951  0.575139 0.453479 -0.00963569 -0.017995   0.088973    23  GLU   A HB2  
1947 H HB3  . GLU   B 11  ? 0.760739 0.543269 0.460137 -0.00398317 -0.0171295  0.0835984   23  GLU   A HB3  
1948 H HG2  . GLU   B 11  ? 0.825417 0.635702 0.520432 -0.0228248  -0.0590171  0.0908065   23  GLU   A HG2  
1949 H HG3  . GLU   B 11  ? 0.884026 0.669439 0.51763  -0.027624   -0.0622568  0.099143    23  GLU   A HG3  
1950 N N    . ASP   B 12  ? 0.744318 0.520345 0.400649 -0.039035   -0.0532495  0.0547074   24  ASP   A N    
1951 C CA   . ASP   B 12  ? 0.702759 0.500056 0.391407 -0.045991   -0.0624219  0.0499458   24  ASP   A CA   
1952 C C    . ASP   B 12  ? 0.680934 0.518974 0.420051 -0.0418912  -0.0724505  0.0640076   24  ASP   A C    
1953 O O    . ASP   B 12  ? 0.630103 0.484538 0.367554 -0.0489093  -0.0907996  0.0765657   24  ASP   A O    
1954 C CB   . ASP   B 12  ? 0.722785 0.508109 0.378111 -0.0666811  -0.0786044  0.0433487   24  ASP   A CB   
1955 C CG   . ASP   B 12  ? 0.706149 0.513072 0.396305 -0.0746267  -0.0841249  0.0395861   24  ASP   A CG   
1956 O OD1  . ASP   B 12  ? 0.64641  0.4779   0.383353 -0.062676   -0.0753472  0.0417507   24  ASP   A OD1  
1957 O OD2  . ASP   B 12  ? 0.745609 0.542724 0.414057 -0.0938101  -0.0961234  0.0342098   24  ASP   A OD2  
1958 H H    . ASP   B 12  ? 0.77533  0.538341 0.396363 -0.0466386  -0.0606761  0.0562508   24  ASP   A H    
1959 H HA   . ASP   B 12  ? 0.684775 0.478402 0.386965 -0.0397022  -0.050664   0.0424905   24  ASP   A HA   
1960 H HB2  . ASP   B 12  ? 0.753305 0.507663 0.373389 -0.0682753  -0.0709564  0.0340773   24  ASP   A HB2  
1961 H HB3  . ASP   B 12  ? 0.748503 0.540931 0.391867 -0.0745962  -0.093128   0.0510398   24  ASP   A HB3  
1962 N N    . ILE   B 13  ? 0.63185  0.485703 0.41553  -0.0305854  -0.0606945  0.0614237   25  ILE   A N    
1963 C CA   . ILE   B 13  ? 0.609974 0.494745 0.442033 -0.0217991  -0.0629829  0.072682    25  ILE   A CA   
1964 C C    . ILE   B 13  ? 0.589294 0.498903 0.453546 -0.0266825  -0.0661421  0.0678531   25  ILE   A C    
1965 O O    . ILE   B 13  ? 0.558812 0.492525 0.466023 -0.0176104  -0.0628147  0.0732255   25  ILE   A O    
1966 C CB   . ILE   B 13  ? 0.544264 0.422909 0.398743 -0.00602687 -0.0450394  0.0726086   25  ILE   A CB   
1967 C CG1  . ILE   B 13  ? 0.579443 0.450582 0.442609 -0.00346254 -0.0311795  0.0563026   25  ILE   A CG1  
1968 C CG2  . ILE   B 13  ? 0.585298 0.441539 0.410328 -0.0022331  -0.0389921  0.0795282   25  ILE   A CG2  
1969 C CD1  . ILE   B 13  ? 0.57954  0.447161 0.467425 0.00768612  -0.0166352  0.0549376   25  ILE   A CD1  
1970 H H    . ILE   B 13  ? 0.624859 0.468495 0.407619 -0.0279935  -0.0507346  0.0521373   25  ILE   A H    
1971 H HA   . ILE   B 13  ? 0.616179 0.509075 0.444761 -0.0236554  -0.074038   0.0842211   25  ILE   A HA   
1972 H HB   . ILE   B 13  ? 0.555802 0.450591 0.440101 -2.298e-05  -0.0460611  0.0797113   25  ILE   A HB   
1973 H HG12 . ILE   B 13  ? 0.579358 0.434414 0.415733 -0.00741692 -0.0293261  0.0504249   25  ILE   A HG12 
1974 H HG13 . ILE   B 13  ? 0.555663 0.439795 0.434107 -0.00611056 -0.0337624  0.0523308   25  ILE   A HG13 
1975 H HG21 . ILE   B 13  ? 0.571972 0.428342 0.417195 0.00614533  -0.0298091  0.0827849   25  ILE   A HG21 
1976 H HG22 . ILE   B 13  ? 0.589748 0.428878 0.390028 -0.00494669 -0.0330483  0.0711634   25  ILE   A HG22 
1977 H HG23 . ILE   B 13  ? 0.601836 0.460122 0.411927 -0.00563778 -0.0496851  0.0896745   25  ILE   A HG23 
1978 H HD11 . ILE   B 13  ? 0.569485 0.447665 0.480947 0.0123663   -0.0172814  0.061018    25  ILE   A HD11 
1979 H HD12 . ILE   B 13  ? 0.561458 0.42864  0.456256 0.00786369  -0.011297   0.0449068   25  ILE   A HD12 
1980 H HD13 . ILE   B 13  ? 0.586134 0.440885 0.459569 0.00957191  -0.01173    0.0583222   25  ILE   A HD13 
1981 N N    . THR   B 14  ? 0.610487 0.512041 0.453101 -0.0408976  -0.07078    0.0584174   26  THR   A N    
1982 C CA   . THR   B 14  ? 0.601171 0.527976 0.471797 -0.0486887  -0.0740992  0.0570796   26  THR   A CA   
1983 C C    . THR   B 14  ? 0.628643 0.588962 0.519999 -0.0578722  -0.0932371  0.0718919   26  THR   A C    
1984 O O    . THR   B 14  ? 0.696508 0.654827 0.567266 -0.063085   -0.108734   0.0814743   26  THR   A O    
1985 C CB   . THR   B 14  ? 0.620949 0.525532 0.462907 -0.0614526  -0.0718182  0.0444825   26  THR   A CB   
1986 O OG1  . THR   B 14  ? 0.579929 0.46561  0.381532 -0.078373   -0.0861564  0.0443291   26  THR   A OG1  
1987 C CG2  . THR   B 14  ? 0.579531 0.4571   0.407165 -0.0501438  -0.0550128  0.0332244   26  THR   A CG2  
1988 H H    . THR   B 14  ? 0.626581 0.505473 0.436481 -0.0458486  -0.0706731  0.053176    26  THR   A H    
1989 H HA   . THR   B 14  ? 0.583846 0.52113  0.481418 -0.0387599  -0.0640187  0.0555875   26  THR   A HA   
1990 H HB   . THR   B 14  ? 0.585733 0.507852 0.448445 -0.065862   -0.0713798  0.044563    26  THR   A HB   
1992 H HG21 . THR   B 14  ? 0.597231 0.460936 0.40869  -0.0567174  -0.0537204  0.027202    26  THR   A HG21 
1993 H HG22 . THR   B 14  ? 0.599646 0.461312 0.40939  -0.0454929  -0.0531368  0.0333846   26  THR   A HG22 
1994 H HG23 . THR   B 14  ? 0.567771 0.4579   0.420571 -0.0411666  -0.0473499  0.0324837   26  THR   A HG23 
1995 N N    . SER   B 15  ? 0.642085 0.63592  0.575425 -0.059631   -0.0919931  0.0749636   27  SER   A N    
1996 C CA   . SER   B 15  ? 0.71892  0.75456  0.685107 -0.0673233  -0.109595   0.0912645   27  SER   A CA   
1997 C C    . SER   B 15  ? 0.662441 0.69678  0.602946 -0.09516    -0.128266   0.0897997   27  SER   A C    
1998 O O    . SER   B 15  ? 0.66327  0.712163 0.597951 -0.107288   -0.151441   0.101165    27  SER   A O    
1999 C CB   . SER   B 15  ? 0.693591 0.768641 0.719581 -0.0566099  -0.0979812  0.0967578   27  SER   A CB   
2000 O OG   . SER   B 15  ? 0.719735 0.811932 0.778652 -0.0364398  -0.0969917  0.110491    27  SER   A OG   
2001 H H    . SER   B 15  ? 0.634086 0.626365 0.576487 -0.0559957  -0.0798686  0.0675121   27  SER   A H    
2002 H HA   . SER   B 15  ? 0.696667 0.735192 0.661867 -0.0615038  -0.11771    0.101027    27  SER   A HA   
2003 H HB2  . SER   B 15  ? 0.687085 0.749932 0.711592 -0.0515586  -0.0820428  0.0858593   27  SER   A HB2  
2004 H HB3  . SER   B 15  ? 0.703564 0.803414 0.746502 -0.0685018  -0.106458   0.102281    27  SER   A HB3  
2006 N N    . LYS   B 16  ? 0.61891  0.632373 0.540899 -0.105949   -0.118843   0.0759723   28  LYS   A N    
2007 C CA   . LYS   B 16  ? 0.66634  0.668302 0.560493 -0.133966   -0.133312   0.0721025   28  LYS   A CA   
2008 C C    . LYS   B 16  ? 0.64069  0.595407 0.469912 -0.142395   -0.143122   0.0641359   28  LYS   A C    
2009 O O    . LYS   B 16  ? 0.69814  0.634155 0.494497 -0.166861   -0.156963   0.0591702   28  LYS   A O    
2010 C CB   . LYS   B 16  ? 0.710663 0.694037 0.598024 -0.139926   -0.116956   0.0604897   28  LYS   A CB   
2011 C CG   . LYS   B 16  ? 0.756683 0.778591 0.695768 -0.135265   -0.103042   0.0653052   28  LYS   A CG   
2012 C CD   . LYS   B 16  ? 0.81848  0.809906 0.737583 -0.129475   -0.082155   0.0529308   28  LYS   A CD   
2013 C CE   . LYS   B 16  ? 0.877116 0.882041 0.811802 -0.143706   -0.0738714  0.0545444   28  LYS   A CE   
2014 N NZ   . LYS   B 16  ? 0.893009 0.945288 0.881392 -0.132372   -0.0613216  0.0621359   28  LYS   A NZ   
2015 H H    . LYS   B 16  ? 0.617617 0.62227  0.543643 -0.096109   -0.103212   0.0690318   28  LYS   A H    
2016 H HA   . LYS   B 16  ? 0.662489 0.697119 0.582246 -0.144327   -0.146837   0.0823471   28  LYS   A HA   
2017 H HB2  . LYS   B 16  ? 0.711938 0.66644  0.576769 -0.128717   -0.105502   0.0519906   28  LYS   A HB2  
2018 H HB3  . LYS   B 16  ? 0.739077 0.708025 0.604157 -0.159015   -0.126021   0.05754     28  LYS   A HB3  
2019 H HG2  . LYS   B 16  ? 0.761794 0.805192 0.717213 -0.1516     -0.111663   0.0713478   28  LYS   A HG2  
2020 H HG3  . LYS   B 16  ? 0.732601 0.777099 0.700863 -0.119763   -0.0986744  0.0709798   28  LYS   A HG3  
2021 H HD2  . LYS   B 16  ? 0.794565 0.789076 0.724924 -0.111634   -0.0709299  0.050894    28  LYS   A HD2  
2022 H HD3  . LYS   B 16  ? 0.829317 0.785016 0.710348 -0.132622   -0.0840793  0.0457228   28  LYS   A HD3  
2023 H HE2  . LYS   B 16  ? 0.877524 0.855429 0.788679 -0.141588   -0.0641799  0.0473644   28  LYS   A HE2  
2024 H HE3  . LYS   B 16  ? 0.892338 0.900465 0.824196 -0.16302    -0.0856755  0.0581589   28  LYS   A HE3  
2025 H HZ1  . LYS   B 16  ? 0.86477  0.911105 0.853295 -0.115818   -0.0506271  0.0574793   28  LYS   A HZ1  
2026 H HZ2  . LYS   B 16  ? 0.875263 0.95441  0.888989 -0.133069   -0.0703499  0.070418    28  LYS   A HZ2  
2027 H HZ3  . LYS   B 16  ? 0.882962 0.943489 0.879408 -0.141092   -0.0544939  0.0635683   28  LYS   A HZ3  
2028 N N    . LYS   B 17  ? 0.606366 0.538796 0.41553  -0.122897   -0.133691   0.0619769   29  LYS   A N    
2029 C CA   . LYS   B 17  ? 0.666055 0.552165 0.412779 -0.126754   -0.136251   0.0539927   29  LYS   A CA   
2030 C C    . LYS   B 17  ? 0.67794  0.519239 0.384673 -0.138082   -0.127737   0.0371975   29  LYS   A C    
2031 O O    . LYS   B 17  ? 0.69784  0.509132 0.358357 -0.157332   -0.139162   0.0305922   29  LYS   A O    
2032 C CB   . LYS   B 17  ? 0.69092  0.585471 0.414992 -0.142805   -0.16308    0.0637628   29  LYS   A CB   
2033 C CG   . LYS   B 17  ? 0.672144 0.599036 0.423291 -0.127359   -0.170423   0.0825429   29  LYS   A CG   
2034 C CD   . LYS   B 17  ? 0.702664 0.600066 0.429374 -0.106115   -0.15252    0.0809353   29  LYS   A CD   
2035 C CE   . LYS   B 17  ? 0.761079 0.685028 0.514632 -0.0901399  -0.157545   0.101386    29  LYS   A CE   
2036 N NZ   . LYS   B 17  ? 0.704829 0.651859 0.518154 -0.0686999  -0.139846   0.105388    29  LYS   A NZ   
2037 H H    . LYS   B 17  ? 0.594408 0.539681 0.429257 -0.106782   -0.123756   0.0652417   29  LYS   A H    
2038 H HA   . LYS   B 17  ? 0.646525 0.523518 0.391321 -0.109995   -0.124528   0.0537289   29  LYS   A HA   
2039 H HB2  . LYS   B 17  ? 0.700112 0.612932 0.43665  -0.159705   -0.176639   0.0663834   29  LYS   A HB2  
2040 H HB3  . LYS   B 17  ? 0.727068 0.585372 0.402315 -0.148443   -0.163395   0.0555208   29  LYS   A HB3  
2041 H HG2  . LYS   B 17  ? 0.647807 0.607352 0.44771  -0.119114   -0.167078   0.0897984   29  LYS   A HG2  
2042 H HG3  . LYS   B 17  ? 0.708204 0.644433 0.446257 -0.140021   -0.190718   0.0900791   29  LYS   A HG3  
2043 H HD2  . LYS   B 17  ? 0.74444  0.609981 0.422353 -0.113378   -0.153996   0.0740408   29  LYS   A HD2  
2044 H HD3  . LYS   B 17  ? 0.683882 0.572991 0.42343  -0.0954175  -0.134387   0.0731291   29  LYS   A HD3  
2045 H HE2  . LYS   B 17  ? 0.755838 0.703987 0.518401 -0.0990886  -0.177272   0.11259     29  LYS   A HE2  
2046 H HE3  . LYS   B 17  ? 0.763971 0.664101 0.484286 -0.0854007  -0.153071   0.101644    29  LYS   A HE3  
2047 H HZ1  . LYS   B 17  ? 0.68974  0.658302 0.532326 -0.0722792  -0.141834   0.104972    29  LYS   A HZ1  
2048 H HZ2  . LYS   B 17  ? 0.695925 0.622439 0.501323 -0.0613701  -0.123588   0.0957367   29  LYS   A HZ2  
2049 H HZ3  . LYS   B 17  ? 0.706384 0.665882 0.534889 -0.0593575  -0.142811   0.118093    29  LYS   A HZ3  
2050 N N    . ASP   B 18  ? 0.678664 0.511881 0.400013 -0.125113   -0.107551   0.0304845   30  ASP   A N    
2051 C CA   . ASP   B 18  ? 0.715757 0.506821 0.404572 -0.130932   -0.0976448  0.0179132   30  ASP   A CA   
2052 C C    . ASP   B 18  ? 0.726252 0.482622 0.390814 -0.109784   -0.0785606  0.0100903   30  ASP   A C    
2053 O O    . ASP   B 18  ? 0.734764 0.458257 0.379405 -0.107409   -0.0672935  0.00191384  30  ASP   A O    
2054 C CB   . ASP   B 18  ? 0.691779 0.50298  0.415431 -0.133961   -0.0911847  0.0193984   30  ASP   A CB   
2055 C CG   . ASP   B 18  ? 0.633732 0.471794 0.397587 -0.111461   -0.0763725  0.022283    30  ASP   A CG   
2056 O OD1  . ASP   B 18  ? 0.628547 0.461121 0.390963 -0.0927127  -0.0686355  0.0211202   30  ASP   A OD1  
2057 O OD2  . ASP   B 18  ? 0.61714  0.480511 0.412089 -0.114094   -0.0719861  0.0254158   30  ASP   A OD2  
2058 H H    . ASP   B 18  ? 0.643917 0.497811 0.396063 -0.11183    -0.100018   0.0343913   30  ASP   A H    
2059 H HA   . ASP   B 18  ? 0.750055 0.521455 0.409305 -0.14755    -0.107514   0.0143252   30  ASP   A HA   
2060 H HB2  . ASP   B 18  ? 0.707172 0.488769 0.408089 -0.138393   -0.0856843  0.012939    30  ASP   A HB2  
2061 H HB3  . ASP   B 18  ? 0.689875 0.525121 0.431402 -0.147856   -0.10207    0.0251447   30  ASP   A HB3  
2062 N N    . ARG   B 19  ? 0.717795 0.482892 0.387663 -0.0938195  -0.0741615  0.0145085   31  ARG   A N    
2063 C CA   . ARG   B 19  ? 0.700859 0.44006  0.354678 -0.0746786  -0.0554822  0.00928675  31  ARG   A CA   
2064 C C    . ARG   B 19  ? 0.630958 0.376747 0.314062 -0.0607313  -0.0413482  0.00657741  31  ARG   A C    
2065 O O    . ARG   B 19  ? 0.644346 0.367342 0.315185 -0.0479513  -0.0273016  0.00182516  31  ARG   A O    
2066 C CB   . ARG   B 19  ? 0.755825 0.442906 0.350606 -0.0788981  -0.0498763  -0.00084386 31  ARG   A CB   
2067 C CG   . ARG   B 19  ? 0.845838 0.520232 0.401288 -0.100783   -0.0685006  -0.0016602  31  ARG   A CG   
2068 C CD   . ARG   B 19  ? 0.908183 0.550548 0.411553 -0.0986863  -0.064371   -0.00504192 31  ARG   A CD   
2069 N NE   . ARG   B 19  ? 0.950192 0.55146  0.426015 -0.0820266  -0.03902    -0.0146707  31  ARG   A NE   
2070 C CZ   . ARG   B 19  ? 0.979382 0.57364  0.442982 -0.0658873  -0.0232349  -0.0121471  31  ARG   A CZ   
2071 N NH1  . ARG   B 19  ? 0.913249 0.52984  0.378617 -0.0658906  -0.0308775  -0.00092922 31  ARG   A NH1  
2072 N NH2  . ARG   B 19  ? 1.05752  0.620736 0.506095 -0.049529   0.00134016  -0.0195415  31  ARG   A NH2  
2073 H H    . ARG   B 19  ? 0.703323 0.492268 0.389408 -0.0948065  -0.0826646  0.0221976   31  ARG   A H    
2074 H HA   . ARG   B 19  ? 0.688551 0.44014  0.351175 -0.0668818  -0.0546827  0.0149703   31  ARG   A HA   
2075 H HB2  . ARG   B 19  ? 0.772128 0.441348 0.360444 -0.0802291  -0.044816   -0.00651902 31  ARG   A HB2  
2076 H HB3  . ARG   B 19  ? 0.768881 0.446452 0.35625  -0.0658677  -0.0382826  -0.00122619 31  ARG   A HB3  
2077 H HG2  . ARG   B 19  ? 0.820172 0.527457 0.400689 -0.10643    -0.081413   0.00688342  31  ARG   A HG2  
2078 H HG3  . ARG   B 19  ? 0.86077  0.516474 0.399759 -0.113726   -0.0726205  -0.00788591 31  ARG   A HG3  
2079 H HD2  . ARG   B 19  ? 0.893502 0.558861 0.412312 -0.0921518  -0.0666427  0.00405452  31  ARG   A HD2  
2080 H HD3  . ARG   B 19  ? 0.947596 0.574709 0.41889  -0.115922   -0.0772257  -0.00869482 31  ARG   A HD3  
2081 H HE   . ARG   B 19  ? 0.960518 0.541848 0.429438 -0.082305   -0.0332416  -0.0213338  31  ARG   A HE   
2082 H HH11 . ARG   B 19  ? 0.955087 0.571142 0.399389 -0.0787445  -0.0455522  0.00084961  31  ARG   A HH11 
2083 H HH12 . ARG   B 19  ? 0.908701 0.540195 0.396288 -0.0533429  -0.0216647  0.00539775  31  ARG   A HH12 
2084 H HH21 . ARG   B 19  ? 1.05494  0.593464 0.488931 -0.0508381  0.00578964  -0.0273011  31  ARG   A HH21 
2085 H HH22 . ARG   B 19  ? 1.0304   0.59797  0.485091 -0.0369701  0.0137915   -0.0159076  31  ARG   A HH22 
2086 N N    . GLY   B 20  ? 0.596149 0.375608 0.318979 -0.0620128  -0.0446559  0.0105128   32  GLY   A N    
2087 C CA   . GLY   B 20  ? 0.582593 0.370361 0.329013 -0.0503808  -0.0337447  0.00805683  32  GLY   A CA   
2088 C C    . GLY   B 20  ? 0.605934 0.407775 0.376454 -0.0331714  -0.025079   0.00947152  32  GLY   A C    
2089 O O    . GLY   B 20  ? 0.57644  0.380202 0.359658 -0.023588   -0.0171463  0.00627663  32  GLY   A O    
2090 H H    . GLY   B 20  ? 0.596497 0.394999 0.331683 -0.0702222  -0.0538654  0.0150571   32  GLY   A H    
2091 H HA2  . GLY   B 20  ? 0.604003 0.368828 0.331773 -0.0492614  -0.0289633  0.00402947  32  GLY   A HA2  
2092 H HA3  . GLY   B 20  ? 0.576291 0.382656 0.341065 -0.0557009  -0.0367539  0.00981073  32  GLY   A HA3  
2093 N N    . VAL   B 21  ? 0.595447 0.406913 0.371733 -0.0309178  -0.0280417  0.015433    33  VAL   A N    
2094 C CA   . VAL   B 21  ? 0.570407 0.391613 0.369143 -0.0175266  -0.0195684  0.0181699   33  VAL   A CA   
2095 C C    . VAL   B 21  ? 0.624362 0.4322   0.400964 -0.0156732  -0.0186663  0.0242364   33  VAL   A C    
2096 O O    . VAL   B 21  ? 0.574772 0.392455 0.349985 -0.0211615  -0.0292536  0.0325496   33  VAL   A O    
2097 C CB   . VAL   B 21  ? 0.519234 0.369823 0.359164 -0.0137405  -0.0204365  0.0215694   33  VAL   A CB   
2098 C CG1  . VAL   B 21  ? 0.513269 0.365385 0.37275  -0.00240523 -0.0108044  0.0229209   33  VAL   A CG1  
2099 C CG2  . VAL   B 21  ? 0.50105  0.363257 0.356399 -0.0158086  -0.0189009  0.0148605   33  VAL   A CG2  
2100 H H    . VAL   B 21  ? 0.609373 0.420877 0.374941 -0.0388918  -0.0362364  0.0186513   33  VAL   A H    
2101 H HA   . VAL   B 21  ? 0.568315 0.38268  0.368058 -0.0115273  -0.0121161  0.013926    33  VAL   A HA   
2102 H HB   . VAL   B 21  ? 0.52834  0.388545 0.371715 -0.0177047  -0.0277446  0.0278356   33  VAL   A HB   
2103 H HG11 . VAL   B 21  ? 0.509616 0.354418 0.366291 0.00069992  -0.00505117 0.0179568   33  VAL   A HG11 
2104 H HG12 . VAL   B 21  ? 0.52342  0.36994  0.374453 -0.0010924  -0.0108563  0.0291581   33  VAL   A HG12 
2105 H HG13 . VAL   B 21  ? 0.498357 0.363837 0.381596 -1.186e-05  -0.0100589  0.02296     33  VAL   A HG13 
2106 H HG21 . VAL   B 21  ? 0.488847 0.366112 0.367583 -0.0122978  -0.0169717  0.0154733   33  VAL   A HG21 
2107 H HG22 . VAL   B 21  ? 0.509608 0.372478 0.356094 -0.0241906  -0.0242411  0.015389    33  VAL   A HG22 
2108 H HG23 . VAL   B 21  ? 0.500388 0.353702 0.350303 -0.0124598  -0.014108   0.0099166   33  VAL   A HG23 
2109 N N    . LEU   B 22  ? 0.620253 0.409337 0.383436 -0.00678347 -0.00526029 0.0216685   34  LEU   A N    
2110 C CA   . LEU   B 22  ? 0.676158 0.448373 0.412553 -0.00380175 0.00124622  0.0267674   34  LEU   A CA   
2111 C C    . LEU   B 22  ? 0.616319 0.400791 0.383102 0.00710253  0.0132884   0.032886    34  LEU   A C    
2112 O O    . LEU   B 22  ? 0.562633 0.354708 0.355239 0.0136416   0.0214882   0.0285746   34  LEU   A O    
2113 C CB   . LEU   B 22  ? 0.710001 0.448644 0.406387 -0.00229516 0.0111046   0.0187987   34  LEU   A CB   
2114 C CG   . LEU   B 22  ? 0.781817 0.499644 0.442961 -0.016186   -0.00038119 0.0117399   34  LEU   A CG   
2115 C CD1  . LEU   B 22  ? 0.810459 0.486436 0.429469 -0.0118813  0.0134967   0.00301996  34  LEU   A CD1  
2116 C CD2  . LEU   B 22  ? 0.839256 0.559655 0.478059 -0.0312351  -0.0181413  0.0168937   34  LEU   A CD2  
2117 H H    . LEU   B 22  ? 0.6199   0.407933 0.391523 -0.00216765 0.00056266  0.0172831   34  LEU   A H    
2118 H HA   . LEU   B 22  ? 0.675524 0.449426 0.399922 -0.0104217  -0.00841588 0.031739    34  LEU   A HA   
2119 H HB2  . LEU   B 22  ? 0.705633 0.446096 0.418119 0.00527832  0.0193193   0.0157143   34  LEU   A HB2  
2120 H HB3  . LEU   B 22  ? 0.741217 0.467632 0.417854 0.00068581  0.018495    0.0215787   34  LEU   A HB3  
2121 H HG   . LEU   B 22  ? 0.756202 0.485274 0.436623 -0.0187645  -0.00532312 0.0097102   34  LEU   A HG   
2122 H HD11 . LEU   B 22  ? 0.800773 0.478593 0.437593 -0.00124545 0.0236191   0.00186207  34  LEU   A HD11 
2123 H HD12 . LEU   B 22  ? 0.834667 0.494044 0.431758 -0.0218513  0.00641249  -0.00222749 34  LEU   A HD12 
2124 H HD13 . LEU   B 22  ? 0.839236 0.502429 0.435202 -0.00972911 0.0198783   0.00425023  34  LEU   A HD13 
2125 H HD21 . LEU   B 22  ? 0.801128 0.548018 0.46939  -0.0334939  -0.0270817  0.0223776   34  LEU   A HD21 
2126 H HD22 . LEU   B 22  ? 0.846182 0.559334 0.468052 -0.028276   -0.01422    0.0209039   34  LEU   A HD22 
2127 H HD23 . LEU   B 22  ? 0.852273 0.555056 0.464405 -0.0416964  -0.0244303  0.0112806   34  LEU   A HD23 
2128 N N    . LYS   B 23  ? 0.641654 0.428403 0.405714 0.00756546  0.0126939   0.0442117   35  LYS   A N    
2129 C CA   . LYS   B 23  ? 0.588972 0.386002 0.384842 0.015002    0.0230149   0.0520381   35  LYS   A CA   
2130 C C    . LYS   B 23  ? 0.623241 0.402933 0.3918   0.0185571   0.0366075   0.0610218   35  LYS   A C    
2131 O O    . LYS   B 23  ? 0.652892 0.417968 0.379402 0.0140676   0.0309513   0.0663347   35  LYS   A O    
2132 C CB   . LYS   B 23  ? 0.574745 0.388854 0.396512 0.0140477   0.0120303   0.0612456   35  LYS   A CB   
2133 C CG   . LYS   B 23  ? 0.558809 0.375454 0.408712 0.02026     0.0223687   0.0713723   35  LYS   A CG   
2134 C CD   . LYS   B 23  ? 0.527454 0.352646 0.396007 0.022653    0.0139391   0.0847973   35  LYS   A CD   
2135 C CE   . LYS   B 23  ? 0.539642 0.360824 0.439427 0.0277838   0.0270925   0.0911577   35  LYS   A CE   
2136 N NZ   . LYS   B 23  ? 0.525464 0.347932 0.443814 0.0332774   0.0226507   0.106882    35  LYS   A NZ   
2137 H H    . LYS   B 23  ? 0.649891 0.430594 0.390603 0.00224232  0.00497693  0.0478077   35  LYS   A H    
2138 H HA   . LYS   B 23  ? 0.577488 0.380876 0.395735 0.0182615   0.0289929   0.0464124   35  LYS   A HA   
2139 H HB2  . LYS   B 23  ? 0.552786 0.37834  0.393727 0.0128175   0.00683071  0.0551635   35  LYS   A HB2  
2140 H HB3  . LYS   B 23  ? 0.590245 0.401994 0.391639 0.0102924   0.00293198  0.0673553   35  LYS   A HB3  
2141 H HG2  . LYS   B 23  ? 0.572786 0.378275 0.405227 0.0215779   0.0310982   0.076527    35  LYS   A HG2  
2142 H HG3  . LYS   B 23  ? 0.534548 0.356713 0.408849 0.0217083   0.0278988   0.0644133   35  LYS   A HG3  
2143 H HD2  . LYS   B 23  ? 0.522506 0.359532 0.40689  0.0220139   0.00629603  0.0802431   35  LYS   A HD2  
2144 H HD3  . LYS   B 23  ? 0.560275 0.380964 0.405179 0.0214086   0.00807489  0.094547    35  LYS   A HD3  
2145 H HE2  . LYS   B 23  ? 0.544847 0.356406 0.431413 0.0276936   0.0364379   0.0954336   35  LYS   A HE2  
2146 H HE3  . LYS   B 23  ? 0.511505 0.337398 0.433187 0.0273451   0.0306427   0.0806117   35  LYS   A HE3  
2147 H HZ1  . LYS   B 23  ? 0.552792 0.371757 0.450416 0.0335841   0.0181866   0.118361    35  LYS   A HZ1  
2148 H HZ2  . LYS   B 23  ? 0.520865 0.353522 0.453806 0.0345826   0.0157006   0.103346    35  LYS   A HZ2  
2149 H HZ3  . LYS   B 23  ? 0.533793 0.34988  0.469874 0.0351909   0.0316005   0.109243    35  LYS   A HZ3  
2150 N N    . ILE   B 24  ? 0.624585 0.407544 0.417392 0.0251394   0.0540672   0.0632973   36  ILE   A N    
2151 C CA   . ILE   B 24  ? 0.661343 0.432953 0.438637 0.0284896   0.0703214   0.0752385   36  ILE   A CA   
2152 C C    . ILE   B 24  ? 0.65779  0.44253  0.479358 0.0296293   0.0767453   0.0853722   36  ILE   A C    
2153 O O    . ILE   B 24  ? 0.627237 0.427073 0.491351 0.0298226   0.0793076   0.0788543   36  ILE   A O    
2154 C CB   . ILE   B 24  ? 0.696582 0.456678 0.458712 0.0349602   0.0912128   0.070098    36  ILE   A CB   
2155 C CG1  . ILE   B 24  ? 0.708341 0.448407 0.427748 0.0340412   0.0862054   0.0578411   36  ILE   A CG1  
2156 C CG2  . ILE   B 24  ? 0.709937 0.458136 0.452552 0.0381843   0.111966    0.0836138   36  ILE   A CG2  
2157 C CD1  . ILE   B 24  ? 0.774557 0.502454 0.48591  0.0442618   0.108039    0.0516244   36  ILE   A CD1  
2158 H H    . ILE   B 24  ? 0.601529 0.394989 0.421368 0.0267169   0.0557813   0.0577574   36  ILE   A H    
2159 H HA   . ILE   B 24  ? 0.689116 0.450472 0.435505 0.0256797   0.0644845   0.0810445   36  ILE   A HA   
2160 H HB   . ILE   B 24  ? 0.663311 0.437428 0.459929 0.0377227   0.0954806   0.0665349   36  ILE   A HB   
2161 H HG12 . ILE   B 24  ? 0.749576 0.474802 0.431769 0.0295925   0.0813331   0.0604572   36  ILE   A HG12 
2162 H HG13 . ILE   B 24  ? 0.698402 0.446898 0.431267 0.0308106   0.0730925   0.0515744   36  ILE   A HG13 
2163 H HG21 . ILE   B 24  ? 0.731838 0.472812 0.46444  0.0435736   0.127344    0.0802559   36  ILE   A HG21 
2164 H HG22 . ILE   B 24  ? 0.742721 0.477863 0.45027  0.034807    0.105997    0.0886482   36  ILE   A HG22 
2165 H HG23 . ILE   B 24  ? 0.70271  0.463079 0.47744  0.0380162   0.116284    0.0910908   36  ILE   A HG23 
2166 H HD11 . ILE   B 24  ? 0.73344  0.479703 0.484367 0.0486838   0.112654    0.0517608   36  ILE   A HD11 
2167 H HD12 . ILE   B 24  ? 0.771726 0.485208 0.460371 0.043549    0.103467    0.0428978   36  ILE   A HD12 
2168 H HD13 . ILE   B 24  ? 0.788851 0.504477 0.478131 0.0472742   0.122528    0.0566686   36  ILE   A HD13 
2169 N N    . VAL   B 25  ? 0.645366 0.420776 0.452135 0.0295096   0.0802826   0.102004    37  VAL   A N    
2170 C CA   . VAL   B 25  ? 0.615256 0.39456  0.457905 0.029851    0.0897303   0.114163    37  VAL   A CA   
2171 C C    . VAL   B 25  ? 0.62334  0.400166 0.469408 0.0314895   0.115078    0.117859    37  VAL   A C    
2172 O O    . VAL   B 25  ? 0.620076 0.38176  0.423507 0.0339345   0.127335    0.124498    37  VAL   A O    
2173 C CB   . VAL   B 25  ? 0.61957  0.388664 0.446225 0.030358    0.0833039   0.134355    37  VAL   A CB   
2174 C CG1  . VAL   B 25  ? 0.571526 0.338304 0.43674  0.0304041   0.0950245   0.147271    37  VAL   A CG1  
2175 C CG2  . VAL   B 25  ? 0.619598 0.39668  0.444892 0.0302873   0.0584106   0.133539    37  VAL   A CG2  
2176 H H    . VAL   B 25  ? 0.673417 0.438091 0.44489  0.0284841   0.0762433   0.106321    37  VAL   A H    
2177 H HA   . VAL   B 25  ? 0.58892  0.378977 0.465327 0.0286889   0.0849341   0.107455    37  VAL   A HA   
2178 H HB   . VAL   B 25  ? 0.646206 0.403716 0.435644 0.0305631   0.0886006   0.141166    37  VAL   A HB   
2179 H HG11 . VAL   B 25  ? 0.558932 0.33427  0.458467 0.0291535   0.092144    0.138157    37  VAL   A HG11 
2180 H HG12 . VAL   B 25  ? 0.597997 0.360733 0.46123  0.0294464   0.111181    0.15141     37  VAL   A HG12 
2181 H HG13 . VAL   B 25  ? 0.602757 0.362606 0.459948 0.0322815   0.089526    0.160908    37  VAL   A HG13 
2182 H HG21 . VAL   B 25  ? 0.635328 0.40814  0.454076 0.0320189   0.0539696   0.148373    37  VAL   A HG21 
2183 H HG22 . VAL   B 25  ? 0.621555 0.398021 0.420009 0.0279844   0.0509547   0.126711    37  VAL   A HG22 
2184 H HG23 . VAL   B 25  ? 0.589109 0.376224 0.447344 0.0306612   0.0548944   0.125601    37  VAL   A HG23 
2185 N N    . LYS   B 26  ? 0.628649 0.421086 0.525549 0.029292    0.12316     0.113956    38  LYS   A N    
2186 C CA   . LYS   B 26  ? 0.655285 0.454667 0.569626 0.0300779   0.146958    0.118532    38  LYS   A CA   
2187 C C    . LYS   B 26  ? 0.694571 0.491403 0.635476 0.0241495   0.160068    0.135554    38  LYS   A C    
2188 O O    . LYS   B 26  ? 0.725119 0.52019  0.662636 0.0247498   0.183294    0.14759     38  LYS   A O    
2189 C CB   . LYS   B 26  ? 0.655668 0.478239 0.6074   0.0304498   0.144159    0.103117    38  LYS   A CB   
2190 C CG   . LYS   B 26  ? 0.653529 0.472743 0.574874 0.0374693   0.13597     0.0896241   38  LYS   A CG   
2191 C CD   . LYS   B 26  ? 0.690237 0.489544 0.561333 0.0457775   0.152418    0.0921851   38  LYS   A CD   
2192 C CE   . LYS   B 26  ? 0.682486 0.492544 0.574387 0.0527398   0.179037    0.0972279   38  LYS   A CE   
2193 N NZ   . LYS   B 26  ? 0.735787 0.520353 0.573319 0.0613892   0.199244    0.0992474   38  LYS   A NZ   
2194 H H    . LYS   B 26  ? 0.602917 0.402994 0.525189 0.0266687   0.113372    0.108202    38  LYS   A H    
2195 H HA   . LYS   B 26  ? 0.686117 0.475374 0.566468 0.034578    0.156772    0.121399    38  LYS   A HA   
2196 H HB2  . LYS   B 26  ? 0.627238 0.457642 0.605694 0.0252162   0.132821    0.0980846   38  LYS   A HB2  
2197 H HB3  . LYS   B 26  ? 0.652349 0.484773 0.624284 0.0308362   0.159297    0.107587    38  LYS   A HB3  
2198 H HG2  . LYS   B 26  ? 0.644421 0.458133 0.552687 0.0352957   0.120234    0.0849651   38  LYS   A HG2  
2199 H HG3  . LYS   B 26  ? 0.631645 0.466447 0.57965  0.0382963   0.1345      0.0828188   38  LYS   A HG3  
2200 H HD2  . LYS   B 26  ? 0.709156 0.493577 0.551565 0.0439942   0.153802    0.100037    38  LYS   A HD2  
2201 H HD3  . LYS   B 26  ? 0.684934 0.477405 0.535568 0.0482557   0.144055    0.0827266   38  LYS   A HD3  
2202 H HE2  . LYS   B 26  ? 0.668299 0.493508 0.585916 0.0558203   0.176293    0.0903626   38  LYS   A HE2  
2203 H HE3  . LYS   B 26  ? 0.687208 0.506692 0.605045 0.0484425   0.186897    0.10654     38  LYS   A HE3  
2204 H HZ1  . LYS   B 26  ? 0.738816 0.511246 0.550517 0.0640939   0.191754    0.0900649   38  LYS   A HZ1  
2205 H HZ2  . LYS   B 26  ? 0.755767 0.527138 0.567834 0.0580769   0.201631    0.106768    38  LYS   A HZ2  
2206 H HZ3  . LYS   B 26  ? 0.740979 0.533937 0.594728 0.0672496   0.21746     0.102333    38  LYS   A HZ3  
2207 N N    . ARG   B 27  ? 0.661909 0.456725 0.630792 0.0184065   0.147978    0.136662    39  ARG   A N    
2208 C CA   . ARG   B 27  ? 0.657545 0.439486 0.642544 0.0131043   0.158908    0.154932    39  ARG   A CA   
2209 C C    . ARG   B 27  ? 0.662887 0.428224 0.635656 0.016379    0.141747    0.160787    39  ARG   A C    
2210 O O    . ARG   B 27  ? 0.604851 0.375853 0.592995 0.0170575   0.12441     0.146273    39  ARG   A O    
2211 C CB   . ARG   B 27  ? 0.669561 0.463294 0.713679 0.00139681  0.165987    0.151258    39  ARG   A CB   
2212 C CG   . ARG   B 27  ? 0.705128 0.482801 0.767688 -0.00670698 0.182352    0.171476    39  ARG   A CG   
2213 C CD   . ARG   B 27  ? 0.696364 0.483558 0.818775 -0.0229243  0.185733    0.16517     39  ARG   A CD   
2214 N NE   . ARG   B 27  ? 0.682334 0.462581 0.822706 -0.0268183  0.165113    0.14713     39  ARG   A NE   
2215 C CZ   . ARG   B 27  ? 0.635557 0.427195 0.816829 -0.0405776  0.15774     0.130197    39  ARG   A CZ   
2216 N NH1  . ARG   B 27  ? 0.614927 0.429725 0.832856 -0.0534546  0.167013    0.130975    39  ARG   A NH1  
2217 N NH2  . ARG   B 27  ? 0.627868 0.409293 0.812559 -0.0417344  0.140803    0.112364    39  ARG   A NH2  
2218 H H    . ARG   B 27  ? 0.638378 0.437995 0.616122 0.0180181   0.133802    0.125795    39  ARG   A H    
2219 H HA   . ARG   B 27  ? 0.694909 0.469729 0.657744 0.0150156   0.173086    0.167379    39  ARG   A HA   
2220 H HB2  . ARG   B 27  ? 0.655165 0.466064 0.711711 0.00045568  0.173109    0.146233    39  ARG   A HB2  
2221 H HB3  . ARG   B 27  ? 0.645042 0.440841 0.705492 -0.00099532 0.15211     0.139396    39  ARG   A HB3  
2222 H HG2  . ARG   B 27  ? 0.717049 0.476308 0.766045 -0.0036744  0.175908    0.178691    39  ARG   A HG2  
2223 H HG3  . ARG   B 27  ? 0.72523  0.502203 0.772046 -0.0049137  0.198201    0.183558    39  ARG   A HG3  
2224 H HD2  . ARG   B 27  ? 0.721578 0.496545 0.853163 -0.028754   0.198453    0.179833    39  ARG   A HD2  
2225 H HD3  . ARG   B 27  ? 0.683231 0.493035 0.822924 -0.0256677  0.190015    0.159072    39  ARG   A HD3  
2226 H HE   . ARG   B 27  ? 0.675207 0.442649 0.79672  -0.0197364  0.157062    0.147309    39  ARG   A HE   
2227 H HH11 . ARG   B 27  ? 0.638183 0.451525 0.864252 -0.057313   0.181755    0.144941    39  ARG   A HH11 
2228 H HH12 . ARG   B 27  ? 0.603294 0.436521 0.838737 -0.058404   0.158339    0.118372    39  ARG   A HH12 
2229 H HH21 . ARG   B 27  ? 0.620001 0.396847 0.782926 -0.0319235  0.132834    0.108858    39  ARG   A HH21 
2230 H HH22 . ARG   B 27  ? 0.629743 0.408757 0.838004 -0.052786   0.138002    0.103767    39  ARG   A HH22 
2231 N N    . VAL   B 28  ? 0.736629 0.482824 0.680653 0.0195723   0.147402    0.183483    40  VAL   A N    
2232 C CA   . VAL   B 28  ? 0.810251 0.542915 0.74533  0.025292    0.131938    0.195242    40  VAL   A CA   
2233 C C    . VAL   B 28  ? 0.792201 0.514818 0.776484 0.0219503   0.133254    0.195994    40  VAL   A C    
2234 O O    . VAL   B 28  ? 0.827943 0.543068 0.838873 0.0132086   0.150191    0.201235    40  VAL   A O    
2235 C CB   . VAL   B 28  ? 0.857464 0.572498 0.745582 0.0293672   0.137097    0.222272    40  VAL   A CB   
2236 C CG1  . VAL   B 28  ? 0.860791 0.565137 0.746284 0.0370878   0.11988     0.239605    40  VAL   A CG1  
2237 C CG2  . VAL   B 28  ? 0.83863  0.557138 0.67012  0.0310505   0.135781    0.21751     40  VAL   A CG2  
2238 H H    . VAL   B 28  ? 0.762426 0.504612 0.692615 0.0187211   0.161954    0.193227    40  VAL   A H    
2239 H HA   . VAL   B 28  ? 0.777558 0.51852  0.703745 0.0287052   0.116983    0.185147    40  VAL   A HA   
2240 H HB   . VAL   B 28  ? 0.867209 0.574048 0.763547 0.0254701   0.15429     0.232759    40  VAL   A HB   
2241 H HG11 . VAL   B 28  ? 0.842218 0.557757 0.732971 0.0401589   0.104205    0.228493    40  VAL   A HG11 
2242 H HG12 . VAL   B 28  ? 0.869279 0.563386 0.784237 0.036575    0.126016    0.246276    40  VAL   A HG12 
2243 H HG13 . VAL   B 28  ? 0.897251 0.593674 0.746489 0.0395376   0.11873     0.255803    40  VAL   A HG13 
2244 H HG21 . VAL   B 28  ? 0.884205 0.590544 0.681076 0.0328321   0.1366      0.233953    40  VAL   A HG21 
2245 H HG22 . VAL   B 28  ? 0.843831 0.566777 0.678196 0.028445    0.15054     0.210314    40  VAL   A HG22 
2246 H HG23 . VAL   B 28  ? 0.828716 0.556028 0.655163 0.0327076   0.119735    0.205468    40  VAL   A HG23 
2247 N N    . GLY   B 29  ? 0.775686 0.49706  0.771919 0.0284967   0.116447    0.190424    41  GLY   A N    
2248 C CA   . GLY   B 29  ? 0.840447 0.544231 0.876401 0.028035    0.118698    0.190275    41  GLY   A CA   
2249 C C    . GLY   B 29  ? 0.845582 0.523298 0.875575 0.0357472   0.122948    0.220554    41  GLY   A C    
2250 O O    . GLY   B 29  ? 0.909052 0.582871 0.903983 0.0382054   0.126378    0.242664    41  GLY   A O    
2251 H H    . GLY   B 29  ? 0.780927 0.511716 0.760277 0.0333705   0.104291    0.186332    41  GLY   A H    
2252 H HA2  . GLY   B 29  ? 0.812833 0.514574 0.870647 0.0184386   0.128267    0.182639    41  GLY   A HA2  
2253 H HA3  . GLY   B 29  ? 0.797907 0.50781  0.843405 0.032087    0.10815     0.177782    41  GLY   A HA3  
2254 N N    . ASN   B 30  ? 0.896878 0.554166 0.958392 0.0404153   0.123082    0.22153     42  ASN   A N    
2255 C CA   . ASN   B 30  ? 0.935651 0.563111 0.999389 0.0493958   0.128341    0.251281    42  ASN   A CA   
2256 C C    . ASN   B 30  ? 0.927301 0.549376 1.0117   0.0660732   0.116888    0.250617    42  ASN   A C    
2257 O O    . ASN   B 30  ? 0.874782 0.505916 0.980133 0.0661992   0.112468    0.22388     42  ASN   A O    
2258 C CB   . ASN   B 30  ? 1.02789  0.625031 1.11686  0.0362201   0.149342    0.256218    42  ASN   A CB   
2259 C CG   . ASN   B 30  ? 1.02946  0.623681 1.1556   0.0247528   0.151453    0.224008    42  ASN   A CG   
2260 O OD1  . ASN   B 30  ? 1.00873  0.62101  1.1428   0.00870846  0.15532     0.206045    42  ASN   A OD1  
2261 N ND2  . ASN   B 30  ? 1.04627  0.621884 1.19265  0.0343592   0.147183    0.215248    42  ASN   A ND2  
2262 H H    . ASN   B 30  ? 0.866511 0.526689 0.947707 0.038624    0.12028     0.203062    42  ASN   A H    
2263 H HA   . ASN   B 30  ? 0.963582 0.594394 0.998257 0.0531125   0.126012    0.269683    42  ASN   A HA   
2264 H HB2  . ASN   B 30  ? 1.04999  0.622953 1.14331  0.0430205   0.15304     0.275095    42  ASN   A HB2  
2265 H HB3  . ASN   B 30  ? 1.02274  0.625558 1.09881  0.027702    0.158043    0.262171    42  ASN   A HB3  
2266 H HD21 . ASN   B 30  ? 1.023    0.605079 1.17987  0.031494    0.143172    0.193625    42  ASN   A HD21 
2267 H HD22 . ASN   B 30  ? 1.0678   0.623898 1.21668  0.0443014   0.149128    0.231352    42  ASN   A HD22 
2268 N N    . GLY   B 31  ? 0.968777 0.57699  1.04692  0.0811577   0.112999    0.281854    43  GLY   A N    
2269 C CA   . GLY   B 31  ? 1.00914  0.623487 1.10565  0.101062    0.100052    0.286974    43  GLY   A CA   
2270 C C    . GLY   B 31  ? 1.05028  0.706456 1.11991  0.106091    0.0772899   0.289466    43  GLY   A C    
2271 O O    . GLY   B 31  ? 1.06166  0.735958 1.0975   0.0936507   0.0732735   0.281085    43  GLY   A O    
2272 H H    . GLY   B 31  ? 1.00429  0.60015  1.06756  0.0795388   0.118882    0.301645    43  GLY   A H    
2273 H HA2  . GLY   B 31  ? 1.04681  0.640894 1.14942  0.110941    0.102879    0.310004    43  GLY   A HA2  
2274 H HA3  . GLY   B 31  ? 0.995962 0.606789 1.11701  0.101215    0.10371     0.266418    43  GLY   A HA3  
2275 N N    . GLU   B 32  ? 1.15648  0.826673 1.24275  0.12439     0.0630926   0.302522    44  GLU   A N    
2276 C CA   . GLU   B 32  ? 1.12274  0.835286 1.19245  0.126995    0.0393951   0.303263    44  GLU   A CA   
2277 C C    . GLU   B 32  ? 0.979545 0.713242 1.08785  0.13497     0.0363038   0.281354    44  GLU   A C    
2278 O O    . GLU   B 32  ? 1.02436  0.79361  1.1362   0.141211    0.0175351   0.286822    44  GLU   A O    
2279 C CB   . GLU   B 32  ? 1.13011  0.850008 1.18501  0.139831    0.0219476   0.343172    44  GLU   A CB   
2280 H H    . GLU   B 32  ? 1.14354  0.796441 1.25404  0.135395    0.0685577   0.311875    44  GLU   A H    
2281 H HA   . GLU   B 32  ? 1.08277  0.804892 1.12427  0.114072    0.0371962   0.292005    44  GLU   A HA   
2284 N N    . GLU   B 33  ? 0.90916  0.619959 1.04655  0.134523    0.055091    0.258451    45  GLU   A N    
2285 C CA   . GLU   B 33  ? 0.889697 0.615404 1.05763  0.14124     0.0570076   0.235055    45  GLU   A CA   
2286 C C    . GLU   B 33  ? 0.839076 0.577712 0.98923  0.121667    0.0578616   0.200844    45  GLU   A C    
2287 O O    . GLU   B 33  ? 0.819781 0.538719 0.956698 0.106506    0.0677894   0.188297    45  GLU   A O    
2288 C CB   . GLU   B 33  ? 0.916267 0.603551 1.12132  0.154613    0.0769963   0.231842    45  GLU   A CB   
2289 H H    . GLU   B 33  ? 0.941729 0.626357 1.07809  0.128686    0.0674371   0.25684     45  GLU   A H    
2290 H HA   . GLU   B 33  ? 0.881308 0.633821 1.05595  0.150221    0.0444041   0.245504    45  GLU   A HA   
2293 N N    . THR   B 34  ? 0.762624 0.53633  0.915023 0.122098    0.047084    0.188347    46  THR   A N    
2294 C CA   . THR   B 34  ? 0.72499  0.508708 0.867583 0.107941    0.049322    0.156275    46  THR   A CA   
2295 C C    . THR   B 34  ? 0.679672 0.461645 0.852692 0.116957    0.0603131   0.137285    46  THR   A C    
2296 O O    . THR   B 34  ? 0.674473 0.456958 0.877149 0.135668    0.0641058   0.150118    46  THR   A O    
2297 C CB   . THR   B 34  ? 0.712728 0.532502 0.829759 0.0997102   0.0309125   0.156208    46  THR   A CB   
2298 O OG1  . THR   B 34  ? 0.683922 0.530841 0.827321 0.112402    0.0233838   0.163785    46  THR   A OG1  
2299 C CG2  . THR   B 34  ? 0.748979 0.568968 0.830724 0.0936691   0.0200396   0.176565    46  THR   A CG2  
2300 H H    . THR   B 34  ? 0.774989 0.567846 0.936029 0.131287    0.0375576   0.201717    46  THR   A H    
2301 H HA   . THR   B 34  ? 0.720413 0.487292 0.852163 0.0976729   0.0561345   0.147526    46  THR   A HA   
2302 H HB   . THR   B 34  ? 0.688671 0.511747 0.795712 0.0899044   0.0327171   0.136893    46  THR   A HB   
2304 H HG21 . THR   B 34  ? 0.730453 0.56835  0.793278 0.086715    0.00948305  0.172561    46  THR   A HG21 
2305 H HG22 . THR   B 34  ? 0.762986 0.583138 0.851591 0.103035    0.0152486   0.197303    46  THR   A HG22 
2306 H HG23 . THR   B 34  ? 0.748218 0.549531 0.818461 0.0871797   0.0288521   0.17319     46  THR   A HG23 
2307 N N    . PRO   B 35  ? 0.642057 0.423273 0.807675 0.105382    0.0660901   0.107258    47  PRO   A N    
2308 C CA   . PRO   B 35  ? 0.701898 0.481102 0.887781 0.113499    0.0776989   0.088579    47  PRO   A CA   
2309 C C    . PRO   B 35  ? 0.677523 0.496075 0.879806 0.125069    0.0712115   0.0961028   47  PRO   A C    
2310 O O    . PRO   B 35  ? 0.633144 0.484153 0.819824 0.116525    0.055124    0.100956    47  PRO   A O    
2311 C CB   . PRO   B 35  ? 0.672459 0.444653 0.837157 0.0952906   0.0808017   0.0581485   47  PRO   A CB   
2312 C CG   . PRO   B 35  ? 0.675256 0.458951 0.812902 0.079612    0.068057    0.0624015   47  PRO   A CG   
2313 C CD   . PRO   B 35  ? 0.694112 0.476458 0.831124 0.0855288   0.0623983   0.0916787   47  PRO   A CD   
2314 H HA   . PRO   B 35  ? 0.710255 0.464569 0.912321 0.122182    0.0887668   0.0905934   47  PRO   A HA   
2315 H HB2  . PRO   B 35  ? 0.668543 0.455823 0.832623 0.0960123   0.0812155   0.0471457   47  PRO   A HB2  
2316 H HB3  . PRO   B 35  ? 0.699802 0.444543 0.868667 0.0930844   0.090855    0.0477467   47  PRO   A HB3  
2317 H HG2  . PRO   B 35  ? 0.651288 0.457111 0.777414 0.0758361   0.0602539   0.0583701   47  PRO   A HG2  
2318 H HG3  . PRO   B 35  ? 0.673743 0.442801 0.805213 0.0694955   0.0718712   0.0507357   47  PRO   A HG3  
2319 H HD2  . PRO   B 35  ? 0.660454 0.462004 0.781216 0.0819069   0.0517627   0.0983492   47  PRO   A HD2  
2320 H HD3  . PRO   B 35  ? 0.685984 0.448603 0.820588 0.0804012   0.0675886   0.0940209   47  PRO   A HD3  
2321 N N    . MET   B 36  ? 0.714896 0.528132 0.949888 0.143897    0.0856303   0.096147    48  MET   A N    
2322 C CA   . MET   B 36  ? 0.704837 0.555715 0.964613 0.155544    0.0863503   0.0989785   48  MET   A CA   
2323 C C    . MET   B 36  ? 0.649181 0.501659 0.894588 0.145897    0.097366    0.0675516   48  MET   A C    
2324 O O    . MET   B 36  ? 0.605577 0.423462 0.830588 0.136703    0.108047    0.0435816   48  MET   A O    
2325 C CB   . MET   B 36  ? 0.766802 0.609381 1.071    0.183195    0.102814    0.11124     48  MET   A CB   
2326 C CG   . MET   B 36  ? 0.833575 0.666295 1.15698  0.198294    0.096317    0.144213    48  MET   A CG   
2327 S SD   . MET   B 36  ? 0.899207 0.792184 1.24092  0.20445     0.0672227   0.182727    48  MET   A SD   
2328 C CE   . MET   B 36  ? 0.946175 0.828883 1.23135  0.178008    0.0458702   0.186564    48  MET   A CE   
2329 H H    . MET   B 36  ? 0.735192 0.519181 0.978754 0.14992     0.096938    0.0944659   48  MET   A H    
2330 H HA   . MET   B 36  ? 0.684891 0.565585 0.94253  0.152018    0.0703821   0.113095    48  MET   A HA   
2331 H HB2  . MET   B 36  ? 0.78689  0.59854  1.08927  0.185204    0.119848    0.093136    48  MET   A HB2  
2332 H HB3  . MET   B 36  ? 0.759381 0.633257 1.08329  0.190469    0.102994    0.114885    48  MET   A HB3  
2333 H HG2  . MET   B 36  ? 0.841674 0.650297 1.14269  0.187897    0.0931326   0.143853    48  MET   A HG2  
2334 H HG3  . MET   B 36  ? 0.863228 0.676872 1.21095  0.215263    0.111743    0.145998    48  MET   A HG3  
2335 H HE1  . MET   B 36  ? 0.928173 0.837105 1.21161  0.177214    0.0281313   0.205445    48  MET   A HE1  
2336 H HE2  . MET   B 36  ? 0.911122 0.793779 1.17375  0.162786    0.0464287   0.166117    48  MET   A HE2  
2337 H HE3  . MET   B 36  ? 0.950773 0.801074 1.22947  0.179882    0.0523426   0.190658    48  MET   A HE3  
2338 N N    . ILE   B 37  ? 0.65846  0.552313 0.914842 0.14703     0.0940825   0.0691549   49  ILE   A N    
2339 C CA   . ILE   B 37  ? 0.665826 0.564429 0.908171 0.13937     0.105705    0.0435507   49  ILE   A CA   
2340 C C    . ILE   B 37  ? 0.644868 0.507494 0.895797 0.1525      0.13336     0.0242563   49  ILE   A C    
2341 O O    . ILE   B 37  ? 0.630396 0.489169 0.918422 0.175323    0.147165    0.0358232   49  ILE   A O    
2342 C CB   . ILE   B 37  ? 0.726222 0.676213 0.988687 0.140741    0.10147     0.0533018   49  ILE   A CB   
2343 C CG1  . ILE   B 37  ? 0.771063 0.752013 1.02118  0.125352    0.0733337   0.0703562   49  ILE   A CG1  
2344 C CG2  . ILE   B 37  ? 0.705182 0.65686  0.950349 0.133429    0.117009    0.028462    49  ILE   A CG2  
2345 C CD1  . ILE   B 37  ? 0.802654 0.765613 1.00315  0.102975    0.0621901   0.0556526   49  ILE   A CD1  
2346 H H    . ILE   B 37  ? 0.650513 0.5708   0.923529 0.152084    0.0841129   0.087697    49  ILE   A H    
2347 H HA   . ILE   B 37  ? 0.655103 0.545041 0.867424 0.123752    0.0988548   0.0321983   49  ILE   A HA   
2348 H HB   . ILE   B 37  ? 0.729574 0.691652 1.02641  0.157226    0.108209    0.0658899   49  ILE   A HB   
2349 H HG12 . ILE   B 37  ? 0.765997 0.748949 1.02767  0.1315      0.0641765   0.0879625   49  ILE   A HG12 
2350 H HG13 . ILE   B 37  ? 0.753735 0.765873 1.01813  0.12423     0.0713045   0.0752153   49  ILE   A HG13 
2351 H HG21 . ILE   B 37  ? 0.698336 0.682679 0.954088 0.130781    0.113063    0.0356385   49  ILE   A HG21 
2352 H HG22 . ILE   B 37  ? 0.705852 0.640801 0.91792  0.119388    0.11205     0.0151163   49  ILE   A HG22 
2353 H HG23 . ILE   B 37  ? 0.733187 0.66951  0.989092 0.145239    0.136155    0.0193329   49  ILE   A HG23 
2354 H HD11 . ILE   B 37  ? 0.784178 0.743829 0.971706 0.0971997   0.0701789   0.039324    49  ILE   A HD11 
2355 H HD12 . ILE   B 37  ? 0.775145 0.75594  0.967597 0.0944087   0.0466362   0.0655825   49  ILE   A HD12 
2356 H HD13 . ILE   B 37  ? 0.793103 0.729886 0.982771 0.102901    0.0628236   0.0532452   49  ILE   A HD13 
2357 N N    . GLY   B 38  ? 0.653717 0.489009 0.869    0.138315    0.141011    -0.00497748 50  GLY   A N    
2358 C CA   . GLY   B 38  ? 0.702513 0.497967 0.914631 0.146717    0.166856    -0.0284122  50  GLY   A CA   
2359 C C    . GLY   B 38  ? 0.719607 0.462407 0.919435 0.140925    0.168808    -0.0380997  50  GLY   A C    
2360 O O    . GLY   B 38  ? 0.762004 0.463744 0.944981 0.139017    0.185937    -0.0640673  50  GLY   A O    
2361 H H    . GLY   B 38  ? 0.638193 0.478749 0.829359 0.123065    0.129631    -0.0105518  50  GLY   A H    
2362 H HA2  . GLY   B 38  ? 0.699961 0.496215 0.888924 0.137748    0.171142    -0.0460751  50  GLY   A HA2  
2363 H HA3  . GLY   B 38  ? 0.712448 0.513764 0.953166 0.164993    0.180187    -0.0208206  50  GLY   A HA3  
2364 N N    . ASP   B 39  ? 0.699505 0.442027 0.904978 0.136144    0.151811    -0.0178921  51  ASP   A N    
2365 C CA   . ASP   B 39  ? 0.720448 0.416883 0.916431 0.12672     0.152955    -0.0244856  51  ASP   A CA   
2366 C C    . ASP   B 39  ? 0.699132 0.38164  0.856882 0.101183    0.147739    -0.0534507  51  ASP   A C    
2367 O O    . ASP   B 39  ? 0.682758 0.396452 0.820085 0.0896229   0.135585    -0.0586575  51  ASP   A O    
2368 C CB   . ASP   B 39  ? 0.690121 0.393481 0.894033 0.123926    0.136646    0.00341076  51  ASP   A CB   
2369 C CG   . ASP   B 39  ? 0.717075 0.42188  0.955317 0.146949    0.138966    0.0349773   51  ASP   A CG   
2370 O OD1  . ASP   B 39  ? 0.760439 0.455443 1.02533  0.168811    0.156339    0.0360863   51  ASP   A OD1  
2371 O OD2  . ASP   B 39  ? 0.708043 0.423546 0.945046 0.143713    0.123795    0.0594009   51  ASP   A OD2  
2372 H H    . ASP   B 39  ? 0.675618 0.446513 0.890119 0.137834    0.139806    0.00031301  51  ASP   A H    
2373 H HA   . ASP   B 39  ? 0.74907  0.416696 0.957713 0.138276    0.168704    -0.0285148  51  ASP   A HA   
2374 H HB2  . ASP   B 39  ? 0.664778 0.397838 0.857821 0.115951    0.122766    0.00881565  51  ASP   A HB2  
2375 H HB3  . ASP   B 39  ? 0.708707 0.385942 0.902761 0.112635    0.136773    -0.00362315 51  ASP   A HB3  
2376 N N    . LYS   B 40  ? 0.726677 0.361581 0.875735 0.09189     0.155975    -0.0712225  52  LYS   A N    
2377 C CA   . LYS   B 40  ? 0.725402 0.348805 0.844499 0.065126    0.14572     -0.0935326  52  LYS   A CA   
2378 C C    . LYS   B 40  ? 0.736732 0.37211  0.862623 0.0524553   0.128687    -0.0746449  52  LYS   A C    
2379 O O    . LYS   B 40  ? 0.756963 0.373282 0.903269 0.0574423   0.132428    -0.0569853  52  LYS   A O    
2380 C CB   . LYS   B 40  ? 0.757667 0.325482 0.862989 0.0568287   0.160254    -0.12263    52  LYS   A CB   
2381 H H    . LYS   B 40  ? 0.757292 0.365849 0.92109  0.102363    0.167903    -0.0686674  52  LYS   A H    
2382 H HA   . LYS   B 40  ? 0.710799 0.357228 0.812815 0.0601581   0.139932    -0.10136    52  LYS   A HA   
2385 N N    . VAL   B 41  ? 0.742902 0.40865  0.850358 0.0365821   0.111657    -0.0780064  53  VAL   A N    
2386 C CA   . VAL   B 41  ? 0.723208 0.408365 0.83549  0.0275477   0.0978954   -0.0596067  53  VAL   A CA   
2387 C C    . VAL   B 41  ? 0.740723 0.423057 0.841832 0.00352004  0.0880844   -0.0756966  53  VAL   A C    
2388 O O    . VAL   B 41  ? 0.773439 0.465129 0.853348 -0.00532676 0.0815585   -0.0947734  53  VAL   A O    
2389 C CB   . VAL   B 41  ? 0.66429  0.39274  0.768745 0.0343394   0.0870574   -0.0453464  53  VAL   A CB   
2390 C CG1  . VAL   B 41  ? 0.707537 0.455367 0.805992 0.0229857   0.0740172   -0.0345931  53  VAL   A CG1  
2391 C CG2  . VAL   B 41  ? 0.62028  0.358925 0.741906 0.0548077   0.0914848   -0.0236249  53  VAL   A CG2  
2392 H H    . VAL   B 41  ? 0.732391 0.406049 0.822953 0.0320195   0.109718    -0.0920161  53  VAL   A H    
2393 H HA   . VAL   B 41  ? 0.729767 0.401964 0.857442 0.032779    0.102428    -0.0455356  53  VAL   A HA   
2394 H HB   . VAL   B 41  ? 0.66784  0.405231 0.758493 0.0320654   0.0857586   -0.0584442  53  VAL   A HB   
2395 H HG11 . VAL   B 41  ? 0.692109 0.428355 0.801703 0.0222311   0.0767445   -0.0242081  53  VAL   A HG11 
2396 H HG12 . VAL   B 41  ? 0.682778 0.433123 0.771877 0.0114298   0.069008    -0.0474835  53  VAL   A HG12 
2397 H HG13 . VAL   B 41  ? 0.662055 0.431017 0.754699 0.0280355   0.0684694   -0.0247004  53  VAL   A HG13 
2398 H HG21 . VAL   B 41  ? 0.608    0.372754 0.72291  0.0558385   0.0832981   -0.0164238  53  VAL   A HG21 
2399 H HG22 . VAL   B 41  ? 0.648619 0.377803 0.776999 0.0637221   0.101446    -0.030453   53  VAL   A HG22 
2400 H HG23 . VAL   B 41  ? 0.638888 0.367474 0.771606 0.0578111   0.0925377   -0.00940224 53  VAL   A HG23 
2401 N N    . TYR   B 42  ? 0.740509 0.414708 0.857226 -0.0066318  0.0863633   -0.0647078  54  TYR   A N    
2402 C CA   . TYR   B 42  ? 0.714957 0.391899 0.832745 -0.0301709  0.0768053   -0.0752691  54  TYR   A CA   
2403 C C    . TYR   B 42  ? 0.65798  0.370158 0.782916 -0.0323683  0.0682564   -0.0548603  54  TYR   A C    
2404 O O    . TYR   B 42  ? 0.633372 0.344075 0.770216 -0.0248554  0.0747092   -0.0323024  54  TYR   A O    
2405 C CB   . TYR   B 42  ? 0.779562 0.414255 0.914854 -0.0420193  0.0861693   -0.0797769  54  TYR   A CB   
2406 C CG   . TYR   B 42  ? 0.829286 0.417393 0.956712 -0.0390071  0.0989358   -0.100801   54  TYR   A CG   
2407 C CD1  . TYR   B 42  ? 0.89601  0.464658 1.029    -0.014454   0.114575    -0.0914676  54  TYR   A CD1  
2408 C CD2  . TYR   B 42  ? 0.914616 0.476944 1.02903  -0.0605506  0.0956864   -0.129927   54  TYR   A CD2  
2409 C CE1  . TYR   B 42  ? 0.930029 0.453821 1.05716  -0.00825848 0.130278    -0.11067    54  TYR   A CE1  
2410 C CE2  . TYR   B 42  ? 0.96907  0.48148  1.07067  -0.0576515  0.110344    -0.151682   54  TYR   A CE2  
2411 C CZ   . TYR   B 42  ? 0.99784  0.489842 1.1066   -0.0298487  0.129692    -0.142091   54  TYR   A CZ   
2412 O OH   . TYR   B 42  ? 1.09471  0.535801 1.1928   -0.0225635  0.148382    -0.162734   54  TYR   A OH   
2413 H H    . TYR   B 42  ? 0.735659 0.404009 0.864447 0.00147333  0.0914791   -0.0484261  54  TYR   A H    
2414 H HA   . TYR   B 42  ? 0.723568 0.405824 0.826035 -0.0371581  0.0704559   -0.0923587  54  TYR   A HA   
2415 H HB2  . TYR   B 42  ? 0.772226 0.402872 0.921478 -0.0355051  0.0921099   -0.0607083  54  TYR   A HB2  
2416 H HB3  . TYR   B 42  ? 0.777972 0.418569 0.917243 -0.0596042  0.0784135   -0.0863457  54  TYR   A HB3  
2417 H HD1  . TYR   B 42  ? 0.855082 0.442105 0.995865 -0.00110122 0.114564    -0.0716158  54  TYR   A HD1  
2418 H HD2  . TYR   B 42  ? 0.896972 0.475219 1.01079  -0.0776705  0.0833051   -0.135149   54  TYR   A HD2  
2419 H HE1  . TYR   B 42  ? 0.94721  0.461031 1.08268  0.0104985   0.141459    -0.102275   54  TYR   A HE1  
2420 H HE2  . TYR   B 42  ? 1.00509  0.497935 1.09299  -0.074056   0.107202    -0.172928   54  TYR   A HE2  
2422 N N    . VAL   B 43  ? 0.624718 0.367032 0.740337 -0.0414908  0.0547635   -0.061823   55  VAL   A N    
2423 C CA   . VAL   B 43  ? 0.621333 0.394656 0.743162 -0.0412024  0.0497193   -0.0443291  55  VAL   A CA   
2424 C C    . VAL   B 43  ? 0.609306 0.402534 0.743132 -0.0597409  0.0384259   -0.0523154  55  VAL   A C    
2425 O O    . VAL   B 43  ? 0.636504 0.42613  0.76341  -0.072276   0.0288472   -0.0726648  55  VAL   A O    
2426 C CB   . VAL   B 43  ? 0.615251 0.41204  0.714944 -0.0267774  0.0447198   -0.037784   55  VAL   A CB   
2427 C CG1  . VAL   B 43  ? 0.562978 0.348983 0.654149 -0.0102437  0.0517364   -0.0305129  55  VAL   A CG1  
2428 C CG2  . VAL   B 43  ? 0.631282 0.444591 0.712754 -0.0318291  0.0323287   -0.0542804  55  VAL   A CG2  
2429 H H    . VAL   B 43  ? 0.640958 0.38333  0.745105 -0.047204   0.0492998   -0.0774591  55  VAL   A H    
2430 H HA   . VAL   B 43  ? 0.621066 0.387208 0.754322 -0.038563   0.0573248   -0.0303011  55  VAL   A HA   
2431 H HB   . VAL   B 43  ? 0.59089  0.400879 0.693735 -0.0251245  0.0447504   -0.025355   55  VAL   A HB   
2432 H HG11 . VAL   B 43  ? 0.592589 0.365685 0.681784 -0.00973474 0.0543532   -0.0423164  55  VAL   A HG11 
2433 H HG12 . VAL   B 43  ? 0.584523 0.361057 0.685297 -0.00630909 0.0579884   -0.0177082  55  VAL   A HG12 
2434 H HG13 . VAL   B 43  ? 0.56068  0.362344 0.639158 -0.00428726 0.0474621   -0.0262303  55  VAL   A HG13 
2435 H HG21 . VAL   B 43  ? 0.607693 0.430837 0.675302 -0.0231425  0.0308538   -0.0500296  55  VAL   A HG21 
2436 H HG22 . VAL   B 43  ? 0.618902 0.446084 0.707327 -0.0397459  0.0258353   -0.0543244  55  VAL   A HG22 
2437 H HG23 . VAL   B 43  ? 0.641887 0.441414 0.718082 -0.035919   0.0326668   -0.0682936  55  VAL   A HG23 
2438 N N    . HIS   B 44  ? 0.580415 0.396561 0.731184 -0.0606461  0.0396036   -0.0354129  56  HIS   A N    
2439 C CA   . HIS   B 44  ? 0.5686   0.418818 0.731096 -0.0694205  0.027839    -0.036566   56  HIS   A CA   
2440 C C    . HIS   B 44  ? 0.521894 0.394203 0.667799 -0.0526344  0.027409    -0.0248916  56  HIS   A C    
2441 O O    . HIS   B 44  ? 0.543144 0.407634 0.679279 -0.039925   0.0385894   -0.0108049  56  HIS   A O    
2442 C CB   . HIS   B 44  ? 0.575437 0.437494 0.777053 -0.0834072  0.0326535   -0.0260078  56  HIS   A CB   
2443 C CG   . HIS   B 44  ? 0.586191 0.441322 0.807997 -0.107925   0.0234437   -0.041625   56  HIS   A CG   
2444 N ND1  . HIS   B 44  ? 0.599232 0.468013 0.813643 -0.119823   0.00325388  -0.0600048  56  HIS   A ND1  
2445 C CD2  . HIS   B 44  ? 0.583869 0.418523 0.830529 -0.124713   0.0305762   -0.0413861  56  HIS   A CD2  
2446 C CE1  . HIS   B 44  ? 0.593712 0.449371 0.825355 -0.14433    -0.00292929 -0.072852   56  HIS   A CE1  
2447 N NE2  . HIS   B 44  ? 0.614869 0.44946  0.868698 -0.148088   0.0141324   -0.0616849  56  HIS   A NE2  
2448 H H    . HIS   B 44  ? 0.582881 0.393507 0.738339 -0.054669   0.0487886   -0.0218131  56  HIS   A H    
2449 H HA   . HIS   B 44  ? 0.572677 0.424366 0.728057 -0.0770327  0.0171223   -0.0512408  56  HIS   A HA   
2450 H HB2  . HIS   B 44  ? 0.576267 0.424477 0.781968 -0.0790243  0.0453728   -0.0145209  56  HIS   A HB2  
2451 H HB3  . HIS   B 44  ? 0.555482 0.444157 0.76558  -0.0806426  0.0301284   -0.018609   56  HIS   A HB3  
2453 H HD2  . HIS   B 44  ? 0.598171 0.419254 0.853872 -0.122111   0.0439117   -0.0293717  56  HIS   A HD2  
2454 H HE1  . HIS   B 44  ? 0.619488 0.480102 0.847462 -0.157766   -0.0175249  -0.0866457  56  HIS   A HE1  
2456 N N    . TYR   B 45  ? 0.505566 0.403321 0.64745  -0.0534168  0.014116    -0.029762   57  TYR   A N    
2457 C CA   . TYR   B 45  ? 0.491886 0.403508 0.615523 -0.0376341  0.0145626   -0.0201224  57  TYR   A CA   
2458 C C    . TYR   B 45  ? 0.5004   0.444598 0.641666 -0.0387976  0.00529974  -0.0160766  57  TYR   A C    
2459 O O    . TYR   B 45  ? 0.470963 0.4317   0.634044 -0.0528504  -0.00725832 -0.0228373  57  TYR   A O    
2460 C CB   . TYR   B 45  ? 0.448489 0.348392 0.535862 -0.0297514  0.00958691  -0.0287048  57  TYR   A CB   
2461 C CG   . TYR   B 45  ? 0.440082 0.348095 0.51636  -0.037644   -0.00622152 -0.0438029  57  TYR   A CG   
2462 C CD1  . TYR   B 45  ? 0.428718 0.358043 0.498785 -0.0340757  -0.0169824  -0.0403535  57  TYR   A CD1  
2463 C CD2  . TYR   B 45  ? 0.466278 0.35728  0.534489 -0.0478262  -0.00945242 -0.0610864  57  TYR   A CD2  
2464 C CE1  . TYR   B 45  ? 0.465583 0.401983 0.520763 -0.0414561  -0.032838   -0.0516519  57  TYR   A CE1  
2465 C CE2  . TYR   B 45  ? 0.474025 0.370017 0.524263 -0.0564403  -0.0237841  -0.0754499  57  TYR   A CE2  
2466 C CZ   . TYR   B 45  ? 0.471947 0.3922   0.515172 -0.0537721  -0.0366964  -0.0697026  57  TYR   A CZ   
2467 O OH   . TYR   B 45  ? 0.502324 0.426223 0.522632 -0.0622094  -0.0517038  -0.0817857  57  TYR   A OH   
2468 H H    . TYR   B 45  ? 0.516773 0.421608 0.666139 -0.0640515  0.00434784  -0.0388192  57  TYR   A H    
2469 H HA   . TYR   B 45  ? 0.483855 0.390546 0.608004 -0.0308513  0.0256356   -0.00888597 57  TYR   A HA   
2470 H HB2  . TYR   B 45  ? 0.443256 0.346783 0.518174 -0.0202421  0.0119179   -0.0211355  57  TYR   A HB2  
2471 H HB3  . TYR   B 45  ? 0.459724 0.34226  0.542144 -0.0289296  0.0151259   -0.0310675  57  TYR   A HB3  
2472 H HD1  . TYR   B 45  ? 0.425416 0.362996 0.499624 -0.0259773  -0.013105   -0.0296433  57  TYR   A HD1  
2473 H HD2  . TYR   B 45  ? 0.471896 0.345901 0.5456   -0.0489818  -0.00129936 -0.0630626  57  TYR   A HD2  
2474 H HE1  . TYR   B 45  ? 0.453336 0.403905 0.504972 -0.0379715  -0.0405705  -0.0469562  57  TYR   A HE1  
2475 H HE2  . TYR   B 45  ? 0.49708  0.378197 0.537885 -0.0634679  -0.0242441  -0.0886229  57  TYR   A HE2  
2477 N N    . LYS   B 46  ? 0.515539 0.468065 0.649024 -0.0237369  0.0124334   -0.00364416 58  LYS   A N    
2478 C CA   . LYS   B 46  ? 0.52976  0.509551 0.674731 -0.0177475  0.00537484  0.00205233  58  LYS   A CA   
2479 C C    . LYS   B 46  ? 0.486079 0.453398 0.592145 -0.00292449 0.00536636  0.0030482   58  LYS   A C    
2480 O O    . LYS   B 46  ? 0.47497  0.42328  0.55981  0.00583774  0.0182261   0.00814605  58  LYS   A O    
2481 C CB   . LYS   B 46  ? 0.529515 0.530388 0.711067 -0.0136015  0.0191088   0.0173917   58  LYS   A CB   
2482 C CG   . LYS   B 46  ? 0.52149  0.534074 0.744243 -0.0305445  0.0214371   0.0187494   58  LYS   A CG   
2483 C CD   . LYS   B 46  ? 0.515844 0.545739 0.771201 -0.0250117  0.0420985   0.0362866   58  LYS   A CD   
2484 C CE   . LYS   B 46  ? 0.527947 0.555988 0.814893 -0.0426618  0.0507651   0.0396164   58  LYS   A CE   
2485 N NZ   . LYS   B 46  ? 0.566101 0.620302 0.89274  -0.0396661  0.0703913   0.0575042   58  LYS   A NZ   
2486 H H    . LYS   B 46  ? 0.511225 0.450493 0.630981 -0.016559   0.0221478   0.00163848  58  LYS   A H    
2487 H HA   . LYS   B 46  ? 0.52138  0.513162 0.674769 -0.0264893  -0.0085247  -0.00476931 58  LYS   A HA   
2488 H HB2  . LYS   B 46  ? 0.526148 0.513414 0.69311  -0.0044474  0.0329533   0.0236455   58  LYS   A HB2  
2489 H HB3  . LYS   B 46  ? 0.523198 0.543693 0.715564 -0.00797362 0.0140228   0.0215692   58  LYS   A HB3  
2490 H HG2  . LYS   B 46  ? 0.52554  0.555618 0.765431 -0.0403495  0.00680518  0.0134666   58  LYS   A HG2  
2491 H HG3  . LYS   B 46  ? 0.528769 0.519423 0.740293 -0.0365647  0.0243291   0.0135285   58  LYS   A HG3  
2492 H HD2  . LYS   B 46  ? 0.518471 0.533022 0.750378 -0.0126545  0.0550039   0.0415158   58  LYS   A HD2  
2493 H HD3  . LYS   B 46  ? 0.514237 0.571547 0.793375 -0.0219534  0.0381044   0.0412627   58  LYS   A HD3  
2494 H HE2  . LYS   B 46  ? 0.539412 0.575337 0.842764 -0.0572119  0.0367094   0.0314034   58  LYS   A HE2  
2495 H HE3  . LYS   B 46  ? 0.541367 0.541894 0.805953 -0.0420826  0.0579905   0.0385392   58  LYS   A HE3  
2496 H HZ1  . LYS   B 46  ? 0.54945  0.631861 0.900516 -0.0386811  0.0638836   0.0598777   58  LYS   A HZ1  
2497 H HZ2  . LYS   B 46  ? 0.556486 0.599822 0.863588 -0.0266744  0.0846769   0.0640689   58  LYS   A HZ2  
2498 H HZ3  . LYS   B 46  ? 0.563396 0.616392 0.909962 -0.0518283  0.075517    0.0602177   58  LYS   A HZ3  
2499 N N    . GLY   B 47  ? 0.504439 0.47913  0.597148 -0.00309256 -0.0106498  -0.00275208 59  GLY   A N    
2500 C CA   . GLY   B 47  ? 0.459522 0.419449 0.514837 0.00758185  -0.011631   -0.00224797 59  GLY   A CA   
2501 C C    . GLY   B 47  ? 0.464005 0.440924 0.525343 0.0178133   -0.0183341  0.00674195  59  GLY   A C    
2502 O O    . GLY   B 47  ? 0.432021 0.437419 0.524643 0.0141377   -0.029171   0.0100474   59  GLY   A O    
2503 H H    . GLY   B 47  ? 0.494094 0.482699 0.600333 -0.011122   -0.0216066  -0.00666347 59  GLY   A H    
2504 H HA2  . GLY   B 47  ? 0.468317 0.413828 0.511462 0.0134628   -0.00064398 0.00134072  59  GLY   A HA2  
2505 H HA3  . GLY   B 47  ? 0.472508 0.424655 0.51029  0.00208195  -0.0185636  -0.0108058  59  GLY   A HA3  
2506 N N    . LYS   B 48  ? 0.488531 0.447456 0.521529 0.0304177   -0.0122931  0.0116663   60  LYS   A N    
2507 C CA   . LYS   B 48  ? 0.491207 0.45792  0.525162 0.0431537   -0.0169307  0.0213325   60  LYS   A CA   
2508 C C    . LYS   B 48  ? 0.495097 0.430385 0.48499  0.0497302   -0.0138168  0.0211212   60  LYS   A C    
2509 O O    . LYS   B 48  ? 0.524244 0.436081 0.489494 0.0461507   -0.0052236  0.0157098   60  LYS   A O    
2510 C CB   . LYS   B 48  ? 0.521134 0.502712 0.588247 0.0570837   -0.00332132 0.0339607   60  LYS   A CB   
2511 C CG   . LYS   B 48  ? 0.569659 0.524344 0.618671 0.0662799   0.0202319   0.0359181   60  LYS   A CG   
2512 C CD   . LYS   B 48  ? 0.624729 0.594734 0.707638 0.0776899   0.0393741   0.0465478   60  LYS   A CD   
2513 C CE   . LYS   B 48  ? 0.807716 0.776793 0.894364 0.0988236   0.0465848   0.0565686   60  LYS   A CE   
2514 N NZ   . LYS   B 48  ? 0.940819 0.929622 1.06608  0.111972    0.0679045   0.0676713   60  LYS   A NZ   
2515 H H    . LYS   B 48  ? 0.481779 0.422038 0.494551 0.030894    -0.00540077 0.00935135  60  LYS   A H    
2516 H HA   . LYS   B 48  ? 0.498172 0.480984 0.539922 0.0381739   -0.0312932  0.0204093   60  LYS   A HA   
2517 H HB2  . LYS   B 48  ? 0.531977 0.520556 0.603461 0.0666309   -0.00771516 0.0410664   60  LYS   A HB2  
2518 H HB3  . LYS   B 48  ? 0.517442 0.52101  0.615508 0.0507182   -0.00537669 0.0347492   60  LYS   A HB3  
2519 H HG2  . LYS   B 48  ? 0.564279 0.508313 0.601334 0.0572638   0.02201     0.0296592   60  LYS   A HG2  
2520 H HG3  . LYS   B 48  ? 0.583259 0.517404 0.605357 0.0733475   0.0222039   0.0362438   60  LYS   A HG3  
2521 H HD2  . LYS   B 48  ? 0.635814 0.632953 0.753408 0.0712411   0.0344591   0.0488046   60  LYS   A HD2  
2522 H HD3  . LYS   B 48  ? 0.650723 0.603717 0.718868 0.0776244   0.0528995   0.0451799   60  LYS   A HD3  
2523 H HE2  . LYS   B 48  ? 0.802847 0.74113  0.853746 0.103974    0.0526713   0.0535191   60  LYS   A HE2  
2524 H HE3  . LYS   B 48  ? 0.787964 0.77292  0.886385 0.0993196   0.0315895   0.0594424   60  LYS   A HE3  
2525 H HZ1  . LYS   B 48  ? 0.902579 0.876974 1.01506  0.110484    0.0818629   0.0653692   60  LYS   A HZ1  
2526 H HZ2  . LYS   B 48  ? 0.887551 0.90768  1.04982  0.106716    0.061159    0.0716957   60  LYS   A HZ2  
2527 H HZ3  . LYS   B 48  ? 0.913475 0.897524 1.03866  0.126853    0.0745651   0.0733473   60  LYS   A HZ3  
2528 N N    . LEU   B 49  ? 0.524637 0.461143 0.505754 0.0571121   -0.023445   0.0277918   61  LEU   A N    
2529 C CA   . LEU   B 49  ? 0.564824 0.47032  0.510592 0.0657606   -0.0186077  0.0318015   61  LEU   A CA   
2530 C C    . LEU   B 49  ? 0.572481 0.462328 0.522213 0.0816507   0.00071963  0.0383077   61  LEU   A C    
2531 O O    . LEU   B 49  ? 0.595574 0.508003 0.581833 0.0912347   0.00672389  0.0454757   61  LEU   A O    
2532 C CB   . LEU   B 49  ? 0.550657 0.463118 0.491933 0.0717403   -0.0334243  0.0412402   61  LEU   A CB   
2533 C CG   . LEU   B 49  ? 0.584719 0.512451 0.51593  0.0570365   -0.0527883  0.0356152   61  LEU   A CG   
2534 C CD1  . LEU   B 49  ? 0.60237  0.531243 0.520523 0.0647939   -0.0664005  0.0486724   61  LEU   A CD1  
2535 C CD2  . LEU   B 49  ? 0.592801 0.501535 0.49137  0.0419732   -0.0499919  0.022264    61  LEU   A CD2  
2536 H H    . LEU   B 49  ? 0.525989 0.483312 0.524255 0.0560543   -0.0342995  0.0306575   61  LEU   A H    
2537 H HA   . LEU   B 49  ? 0.553282 0.442588 0.475391 0.0575193   -0.0175055  0.0249137   61  LEU   A HA   
2538 H HB2  . LEU   B 49  ? 0.567929 0.497952 0.535766 0.0815654   -0.0343422  0.0497601   61  LEU   A HB2  
2539 H HB3  . LEU   B 49  ? 0.580755 0.468481 0.497972 0.0769706   -0.0287378  0.0443437   61  LEU   A HB3  
2540 H HG   . LEU   B 49  ? 0.569047 0.520469 0.524791 0.0519765   -0.0590935  0.0329732   61  LEU   A HG   
2541 H HD11 . LEU   B 49  ? 0.607242 0.553867 0.551291 0.0746533   -0.0701564  0.0581525   61  LEU   A HD11 
2542 H HD12 . LEU   B 49  ? 0.608967 0.545701 0.515159 0.0548028   -0.0780764  0.0446582   61  LEU   A HD12 
2543 H HD13 . LEU   B 49  ? 0.617155 0.520588 0.512663 0.0698026   -0.0594657  0.0522506   61  LEU   A HD13 
2544 H HD21 . LEU   B 49  ? 0.574835 0.484243 0.48297  0.0376782   -0.0430713  0.0154871   61  LEU   A HD21 
2545 H HD22 . LEU   B 49  ? 0.598897 0.486194 0.475341 0.0444971   -0.0445499  0.024877    61  LEU   A HD22 
2546 H HD23 . LEU   B 49  ? 0.593801 0.511318 0.484727 0.0342402   -0.0601763  0.0185978   61  LEU   A HD23 
2547 N N    . SER   B 50  ? 0.679355 0.530489 0.591321 0.084142    0.0108954   0.0359695   62  SER   A N    
2548 C CA   . SER   B 50  ? 0.723307 0.5513   0.628837 0.0991576   0.0310427   0.0394903   62  SER   A CA   
2549 C C    . SER   B 50  ? 0.7404   0.568804 0.660972 0.120203    0.0342233   0.0522765   62  SER   A C    
2550 O O    . SER   B 50  ? 0.75286  0.570395 0.680612 0.137346    0.0534615   0.0568858   62  SER   A O    
2551 C CB   . SER   B 50  ? 0.751653 0.536371 0.609455 0.0923086   0.0383467   0.0314544   62  SER   A CB   
2552 O OG   . SER   B 50  ? 0.827829 0.620739 0.682456 0.0763816   0.0353989   0.0234481   62  SER   A OG   
2553 H H    . SER   B 50  ? 0.662084 0.500226 0.551171 0.0757987   0.00585184  0.0316965   62  SER   A H    
2554 H HA   . SER   B 50  ? 0.708732 0.550848 0.6337   0.0999161   0.0384864   0.0392896   62  SER   A HA   
2555 H HB2  . SER   B 50  ? 0.78056  0.551624 0.62004  0.0887638   0.0311991   0.0314851   62  SER   A HB2  
2556 H HB3  . SER   B 50  ? 0.792737 0.557845 0.640716 0.101882    0.0521545   0.0322456   62  SER   A HB3  
2558 N N    . ASN   B 51  ? 0.710164 0.55179  0.636106 0.120661    0.0162723   0.0594609   63  ASN   A N    
2559 C CA   . ASN   B 51  ? 0.683616 0.526663 0.625947 0.142711    0.0173327   0.0751212   63  ASN   A CA   
2560 C C    . ASN   B 51  ? 0.719135 0.615391 0.721681 0.151915    0.0133149   0.0855293   63  ASN   A C    
2561 O O    . ASN   B 51  ? 0.739    0.646743 0.767975 0.173101    0.0146909   0.10138     63  ASN   A O    
2562 C CB   . ASN   B 51  ? 0.698511 0.528245 0.615543 0.140378    0.00063144  0.0816638   63  ASN   A CB   
2563 C CG   . ASN   B 51  ? 0.713434 0.584031 0.645596 0.127646    -0.0247383  0.0837302   63  ASN   A CG   
2564 O OD1  . ASN   B 51  ? 0.729012 0.636669 0.691364 0.118097    -0.0312392  0.0781005   63  ASN   A OD1  
2565 N ND2  . ASN   B 51  ? 0.711657 0.572475 0.619433 0.126279    -0.0387041  0.0916224   63  ASN   A ND2  
2566 H H    . ASN   B 51  ? 0.693442 0.542231 0.611667 0.108151    0.00392077  0.0554054   63  ASN   A H    
2567 H HA   . ASN   B 51  ? 0.724379 0.539348 0.653931 0.153709    0.033738    0.0753669   63  ASN   A HA   
2568 H HB2  . ASN   B 51  ? 0.729811 0.549725 0.651146 0.156943    0.00449051  0.092672    63  ASN   A HB2  
2569 H HB3  . ASN   B 51  ? 0.714152 0.514665 0.59716  0.130709    0.00338174  0.0741442   63  ASN   A HB3  
2570 H HD21 . ASN   B 51  ? 0.712332 0.592488 0.620537 0.117319    -0.0531109  0.0913411   63  ASN   A HD21 
2571 H HD22 . ASN   B 51  ? 0.741041 0.574243 0.630224 0.133936    -0.0331438  0.097226    63  ASN   A HD22 
2572 N N    . GLY   B 52  ? 0.65294  0.581783 0.679741 0.135775    0.00801537  0.0778748   64  GLY   A N    
2573 C CA   . GLY   B 52  ? 0.621088 0.60035  0.707559 0.139278    0.00574316  0.0863208   64  GLY   A CA   
2574 C C    . GLY   B 52  ? 0.659636 0.680319 0.773574 0.13515     -0.0235036  0.0956616   64  GLY   A C    
2575 O O    . GLY   B 52  ? 0.669724 0.735752 0.838664 0.141858    -0.02838    0.107865    64  GLY   A O    
2576 H H    . GLY   B 52  ? 0.646861 0.565859 0.653426 0.121522    0.00563361  0.0674992   64  GLY   A H    
2577 H HA2  . GLY   B 52  ? 0.617481 0.604455 0.710556 0.127074    0.00881154  0.078442    64  GLY   A HA2  
2578 H HA3  . GLY   B 52  ? 0.646423 0.625604 0.750007 0.156181    0.0211707   0.0943379   64  GLY   A HA3  
2579 N N    . LYS   B 53  ? 0.636653 0.644916 0.713319 0.122836    -0.043382   0.0906242   65  LYS   A N    
2580 C CA   . LYS   B 53  ? 0.700258 0.741383 0.791064 0.120921    -0.0716657  0.101294    65  LYS   A CA   
2581 C C    . LYS   B 53  ? 0.705872 0.770435 0.79642  0.0935587   -0.09233    0.0874572   65  LYS   A C    
2582 O O    . LYS   B 53  ? 0.665914 0.760927 0.766614 0.0871489   -0.118419   0.0935562   65  LYS   A O    
2583 C CB   . LYS   B 53  ? 0.719545 0.730902 0.768396 0.130125    -0.0792354  0.110509    65  LYS   A CB   
2584 H H    . LYS   B 53  ? 0.65576  0.636049 0.697678 0.115377    -0.0393688  0.0811802   65  LYS   A H    
2585 H HA   . LYS   B 53  ? 0.692248 0.761716 0.823398 0.132465    -0.0726178  0.113603    65  LYS   A HA   
2588 N N    . LYS   B 54  ? 0.704041 0.752028 0.78048  0.0776733   -0.0811453  0.0690335   66  LYS   A N    
2589 C CA   . LYS   B 54  ? 0.717783 0.778853 0.791749 0.0530847   -0.0959669  0.0536827   66  LYS   A CA   
2590 C C    . LYS   B 54  ? 0.696546 0.751624 0.785594 0.0438995   -0.0783119  0.0419268   66  LYS   A C    
2591 O O    . LYS   B 54  ? 0.609845 0.634686 0.679509 0.0499435   -0.0575472  0.038605    66  LYS   A O    
2592 C CB   . LYS   B 54  ? 0.681433 0.718132 0.70088  0.0412889   -0.106338   0.0428507   66  LYS   A CB   
2593 H H    . LYS   B 54  ? 0.69849  0.72477  0.765409 0.0826138   -0.0638127  0.0660777   66  LYS   A H    
2594 H HA   . LYS   B 54  ? 0.707534 0.799795 0.808462 0.0495707   -0.111367   0.0590124   66  LYS   A HA   
2597 N N    . PHE   B 55  ? 0.682087 0.766346 0.805822 0.0282871   -0.0884257  0.0371112   67  PHE   A N    
2598 C CA   . PHE   B 55  ? 0.677498 0.757215 0.818665 0.0172986   -0.0741284  0.0279272   67  PHE   A CA   
2599 C C    . PHE   B 55  ? 0.656239 0.735747 0.789264 -0.00717325 -0.0894665  0.0105835   67  PHE   A C    
2600 O O    . PHE   B 55  ? 0.739068 0.840759 0.877049 -0.018154   -0.113266   0.00876053  67  PHE   A O    
2601 C CB   . PHE   B 55  ? 0.612759 0.726487 0.813188 0.0210801   -0.0660654  0.0403528   67  PHE   A CB   
2602 C CG   . PHE   B 55  ? 0.664105 0.784067 0.879635 0.0473369   -0.0513586  0.0583109   67  PHE   A CG   
2603 C CD1  . PHE   B 55  ? 0.658998 0.801291 0.886618 0.0605595   -0.0663033  0.0721126   67  PHE   A CD1  
2604 C CD2  . PHE   B 55  ? 0.663022 0.765366 0.880198 0.0594064   -0.0219088  0.0620184   67  PHE   A CD2  
2605 C CE1  . PHE   B 55  ? 0.65137  0.795602 0.895289 0.0872044   -0.0498048  0.0885416   67  PHE   A CE1  
2606 C CE2  . PHE   B 55  ? 0.683941 0.787079 0.911974 0.0842047   -0.00518881 0.076198    67  PHE   A CE2  
2607 C CZ   . PHE   B 55  ? 0.65945  0.782654 0.902832 0.0989468   -0.0180865  0.0891634   67  PHE   A CZ   
2608 H H    . PHE   B 55  ? 0.694815 0.801876 0.831189 0.023482    -0.105698   0.0402447   67  PHE   A H    
2609 H HA   . PHE   B 55  ? 0.651371 0.70466  0.770564 0.0224218   -0.0589175  0.0248844   67  PHE   A HA   
2610 H HB2  . PHE   B 55  ? 0.641174 0.782741 0.866436 0.0111528   -0.0826738  0.0414202   67  PHE   A HB2  
2611 H HB3  . PHE   B 55  ? 0.62955  0.733906 0.835532 0.0153546   -0.0531923  0.0357819   67  PHE   A HB3  
2612 H HD1  . PHE   B 55  ? 0.666359 0.82091  0.889678 0.0519762   -0.087316   0.070578    67  PHE   A HD1  
2613 H HD2  . PHE   B 55  ? 0.658076 0.74614  0.866949 0.0511226   -0.0128014  0.0549187   67  PHE   A HD2  
2614 H HE1  . PHE   B 55  ? 0.668043 0.826222 0.92135  0.0977305   -0.0598546  0.0993541   67  PHE   A HE1  
2615 H HE2  . PHE   B 55  ? 0.674632 0.76283  0.897983 0.0916719   0.0154813   0.0772761   67  PHE   A HE2  
2616 H HZ   . PHE   B 55  ? 0.675186 0.795704 0.92611  0.117532    -0.00495401 0.0987068   67  PHE   A HZ   
2617 N N    . ASP   B 56  ? 0.579029 0.630831 0.696491 -0.0148722  -0.0757457  -0.00190717 68  ASP   A N    
2618 C CA   . ASP   B 56  ? 0.566274 0.608021 0.673504 -0.0356371  -0.0842866  -0.0201136  68  ASP   A CA   
2619 C C    . ASP   B 56  ? 0.511751 0.539342 0.638161 -0.0414667  -0.066234   -0.0238238  68  ASP   A C    
2620 O O    . ASP   B 56  ? 0.558279 0.566116 0.674232 -0.0300231  -0.0472851  -0.0192287  68  ASP   A O    
2621 C CB   . ASP   B 56  ? 0.60649  0.619179 0.660835 -0.036461   -0.0856138  -0.0327032  68  ASP   A CB   
2622 C CG   . ASP   B 56  ? 0.587007 0.581021 0.626892 -0.0544313  -0.0876172  -0.0534606  68  ASP   A CG   
2623 O OD1  . ASP   B 56  ? 0.658859 0.666192 0.709082 -0.0711872  -0.104526   -0.0615879  68  ASP   A OD1  
2624 O OD2  . ASP   B 56  ? 0.596528 0.562937 0.614179 -0.0515371  -0.0732019  -0.0613357  68  ASP   A OD2  
2625 H H    . ASP   B 56  ? 0.580392 0.617599 0.692501 -0.00641521 -0.060301   0.00113895  68  ASP   A H    
2626 H HA   . ASP   B 56  ? 0.579006 0.641344 0.701772 -0.0457777  -0.100105   -0.0213442  68  ASP   A HA   
2627 H HB2  . ASP   B 56  ? 0.600637 0.621284 0.640656 -0.0344476  -0.097659   -0.0298161  68  ASP   A HB2  
2628 H HB3  . ASP   B 56  ? 0.579843 0.576464 0.62161  -0.0266028  -0.0721352  -0.0296382  68  ASP   A HB3  
2629 N N    . SER   B 57  ? 0.525383 0.563003 0.679374 -0.0604312  -0.0736182  -0.0308649  69  SER   A N    
2630 C CA   . SER   B 57  ? 0.555705 0.578761 0.73062  -0.0680915  -0.0575635  -0.0325311  69  SER   A CA   
2631 C C    . SER   B 57  ? 0.597081 0.600644 0.76289  -0.0902261  -0.0666942  -0.0531408  69  SER   A C    
2632 O O    . SER   B 57  ? 0.601226 0.620858 0.7696   -0.105952   -0.0884291  -0.0617885  69  SER   A O    
2633 C CB   . SER   B 57  ? 0.538492 0.593004 0.766907 -0.0697491  -0.0519187  -0.0168026  69  SER   A CB   
2634 O OG   . SER   B 57  ? 0.585965 0.622122 0.830364 -0.0776023  -0.0346732  -0.0164759  69  SER   A OG   
2635 H H    . SER   B 57  ? 0.544847 0.597942 0.703908 -0.0699783  -0.0900264  -0.034434   69  SER   A H    
2636 H HA   . SER   B 57  ? 0.540888 0.543768 0.698918 -0.0577681  -0.0433407  -0.0304338  69  SER   A HA   
2637 H HB2  . SER   B 57  ? 0.538199 0.60197  0.769387 -0.0542945  -0.0441922  -0.00496528 69  SER   A HB2  
2638 H HB3  . SER   B 57  ? 0.559186 0.637282 0.808548 -0.0809201  -0.067361   -0.0178856  69  SER   A HB3  
2640 N N    . SER   B 58  ? 0.54924  0.517519 0.704374 -0.0908094  -0.0501264  -0.0599386  70  SER   A N    
2641 C CA   . SER   B 58  ? 0.627607 0.568866 0.778456 -0.109915   -0.0521374  -0.0788162  70  SER   A CA   
2642 C C    . SER   B 58  ? 0.67952  0.6389   0.873301 -0.13324    -0.0618922  -0.0791195  70  SER   A C    
2643 O O    . SER   B 58  ? 0.742238 0.6894   0.929161 -0.154966   -0.0752503  -0.0979159  70  SER   A O    
2644 C CB   . SER   B 58  ? 0.63554  0.539374 0.777375 -0.101427   -0.030156   -0.0790792  70  SER   A CB   
2645 O OG   . SER   B 58  ? 0.597584 0.507406 0.769653 -0.0954714  -0.0150674  -0.059687   70  SER   A OG   
2646 H H    . SER   B 58  ? 0.558257 0.517571 0.707872 -0.0783353  -0.0370118  -0.0522001  70  SER   A H    
2647 H HA   . SER   B 58  ? 0.640386 0.575014 0.7642   -0.113698   -0.0621601  -0.0915972  70  SER   A HA   
2648 H HB2  . SER   B 58  ? 0.653835 0.535982 0.792521 -0.112732   -0.029984   -0.0919559  70  SER   A HB2  
2649 H HB3  . SER   B 58  ? 0.620143 0.515981 0.737013 -0.0887113  -0.0261291  -0.0794652  70  SER   A HB3  
2651 N N    . HIS   B 59  ? 0.66578  0.654166 0.903108 -0.129917   -0.0545607  -0.0587419  71  HIS   A N    
2652 C CA   . HIS   B 59  ? 0.696486 0.710764 0.983916 -0.152493   -0.062625   -0.0550755  71  HIS   A CA   
2653 C C    . HIS   B 59  ? 0.709095 0.755936 1.00135  -0.168742   -0.0942682  -0.063619   71  HIS   A C    
2654 O O    . HIS   B 59  ? 0.673593 0.723824 0.985798 -0.196995   -0.108824   -0.0743984  71  HIS   A O    
2655 C CB   . HIS   B 59  ? 0.686492 0.727846 1.01775  -0.14184    -0.0439654  -0.0296211  71  HIS   A CB   
2656 C CG   . HIS   B 59  ? 0.681377 0.68726  1.00057  -0.129481   -0.0158712  -0.0216466  71  HIS   A CG   
2657 N ND1  . HIS   B 59  ? 0.676923 0.677472 0.972919 -0.103184   -0.00013691 -0.00939621 71  HIS   A ND1  
2658 C CD2  . HIS   B 59  ? 0.652556 0.625151 0.977878 -0.140543   -0.00222614 -0.023205   71  HIS   A CD2  
2659 C CE1  . HIS   B 59  ? 0.642474 0.611488 0.930125 -0.0989602  0.0199886   -0.00317927 71  HIS   A CE1  
2660 N NE2  . HIS   B 59  ? 0.666263 0.617848 0.972662 -0.120058   0.019763    -0.0101621  71  HIS   A NE2  
2661 H H    . HIS   B 59  ? 0.646988 0.639174 0.882833 -0.113656   -0.0434378  -0.0468157  71  HIS   A H    
2662 H HA   . HIS   B 59  ? 0.715392 0.702913 1.00243  -0.165509   -0.0580756  -0.0644582  71  HIS   A HA   
2663 H HB2  . HIS   B 59  ? 0.665208 0.729116 0.996204 -0.127149   -0.0459144  -0.0205492  71  HIS   A HB2  
2664 H HB3  . HIS   B 59  ? 0.692202 0.753608 1.06092  -0.15802    -0.0485699  -0.0263546  71  HIS   A HB3  
2666 H HD2  . HIS   B 59  ? 0.691405 0.655076 1.03019  -0.159378   -0.00731694 -0.0314162  71  HIS   A HD2  
2667 H HE1  . HIS   B 59  ? 0.64214  0.601764 0.912398 -0.0841354  0.0316099   0.00506894  71  HIS   A HE1  
2669 N N    . ASP   B 60  ? 0.756034 0.823119 1.02612  -0.152635   -0.106347   -0.0592369  72  ASP   A N    
2670 C CA   . ASP   B 60  ? 0.825374 0.922119 1.0918   -0.165585   -0.138645   -0.0649128  72  ASP   A CA   
2671 C C    . ASP   B 60  ? 0.881466 0.945665 1.11169  -0.191885   -0.153932   -0.0934064  72  ASP   A C    
2672 O O    . ASP   B 60  ? 0.83626  0.922568 1.07878  -0.216518   -0.180843   -0.100673   72  ASP   A O    
2673 C CB   . ASP   B 60  ? 0.818828 0.924208 1.04883  -0.143911   -0.147026   -0.0589603  72  ASP   A CB   
2674 C CG   . ASP   B 60  ? 0.776429 0.900926 1.02286  -0.114138   -0.131437   -0.0349625  72  ASP   A CG   
2675 O OD1  . ASP   B 60  ? 0.761649 0.921628 1.06266  -0.110847   -0.126379   -0.0172611  72  ASP   A OD1  
2676 O OD2  . ASP   B 60  ? 0.722786 0.826096 0.926751 -0.0949512  -0.123876   -0.0344011  72  ASP   A OD2  
2677 H H    . ASP   B 60  ? 0.730362 0.791699 0.986093 -0.133456   -0.0946634  -0.05174    72  ASP   A H    
2678 H HA   . ASP   B 60  ? 0.814989 0.947269 1.12459  -0.173124   -0.146892   -0.0543839  72  ASP   A HA   
2679 H HB2  . ASP   B 60  ? 0.823054 0.896054 1.01096  -0.14069    -0.141702   -0.0710421  72  ASP   A HB2  
2680 H HB3  . ASP   B 60  ? 0.832069 0.960413 1.06405  -0.153433   -0.169697   -0.0598772  72  ASP   A HB3  
2681 N N    . ARG   B 61  ? 0.977841 0.989614 1.16172  -0.186089   -0.136973   -0.109712   73  ARG   A N    
2682 C CA   . ARG   B 61  ? 1.03717  1.00876  1.18198  -0.207564   -0.144428   -0.138828   73  ARG   A CA   
2683 C C    . ARG   B 61  ? 1.02652  0.975328 1.20252  -0.230559   -0.136781   -0.147342   73  ARG   A C    
2684 O O    . ARG   B 61  ? 1.14711  1.062    1.29859  -0.253797   -0.144552   -0.172519   73  ARG   A O    
2685 C CB   . ARG   B 61  ? 1.05074  0.978215 1.13932  -0.189366   -0.126131   -0.151048   73  ARG   A CB   
2686 H H    . ARG   B 61  ? 0.933578 0.934152 1.1101   -0.167906   -0.119773   -0.102528   73  ARG   A H    
2687 H HA   . ARG   B 61  ? 1.05017  1.03836  1.18407  -0.219934   -0.167056   -0.14491    73  ARG   A HA   
2690 N N    . ASN   B 62  ? 0.971258 0.934124 1.19763  -0.224265   -0.119574   -0.126535   74  ASN   A N    
2691 C CA   . ASN   B 62  ? 0.945711 0.884593 1.20387  -0.243625   -0.107583   -0.129265   74  ASN   A CA   
2692 C C    . ASN   B 62  ? 0.935412 0.806267 1.15346  -0.239941   -0.0876588  -0.147975   74  ASN   A C    
2693 O O    . ASN   B 62  ? 0.896603 0.730973 1.11447  -0.263983   -0.0879108  -0.165628   74  ASN   A O    
2694 C CB   . ASN   B 62  ? 0.975331 0.937334 1.26512  -0.281126   -0.133964   -0.137809   74  ASN   A CB   
2695 H H    . ASN   B 62  ? 0.93243  0.918402 1.17173  -0.20704    -0.113818   -0.109647   74  ASN   A H    
2696 H HA   . ASN   B 62  ? 0.918308 0.872106 1.2071   -0.233381   -0.0936738  -0.110342   74  ASN   A HA   
2699 N N    . GLU   B 63  ? 0.932258 0.785912 1.11905  -0.209901   -0.0700396  -0.143461   75  GLU   A N    
2700 C CA   . GLU   B 63  ? 1.01329  0.809259 1.16536  -0.20179    -0.0512933  -0.159054   75  GLU   A CA   
2701 C C    . GLU   B 63  ? 0.903572 0.697047 1.04632  -0.168198   -0.0304402  -0.141669   75  GLU   A C    
2702 O O    . GLU   B 63  ? 0.818973 0.643948 0.951563 -0.151831   -0.0354437  -0.13091    75  GLU   A O    
2703 C CB   . GLU   B 63  ? 1.05739  0.828944 1.15744  -0.211238   -0.0633454  -0.18891    75  GLU   A CB   
2704 H H    . GLU   B 63  ? 0.906288 0.785365 1.09531  -0.194055   -0.0695626  -0.129903   75  GLU   A H    
2705 H HA   . GLU   B 63  ? 1.00849  0.780845 1.17759  -0.21309    -0.0434818  -0.161293   75  GLU   A HA   
2708 N N    . PRO   B 64  ? 0.885541 0.64055  1.03121  -0.157648   -0.00772429 -0.137651   76  PRO   A N    
2709 C CA   . PRO   B 64  ? 0.811318 0.561973 0.943154 -0.128193   0.00830606  -0.124279   76  PRO   A CA   
2710 C C    . PRO   B 64  ? 0.806886 0.556405 0.897078 -0.116437   0.00488558  -0.138177   76  PRO   A C    
2711 O O    . PRO   B 64  ? 0.834579 0.561789 0.898942 -0.128028   2.39e-05    -0.162588   76  PRO   A O    
2712 C CB   . PRO   B 64  ? 0.861391 0.56492  1.00074  -0.123435   0.0288904   -0.123039   76  PRO   A CB   
2713 C CG   . PRO   B 64  ? 0.889113 0.580425 1.05854  -0.150398   0.0262542   -0.125602   76  PRO   A CG   
2714 C CD   . PRO   B 64  ? 0.915805 0.6286   1.07837  -0.174318   0.00223918  -0.144913   76  PRO   A CD   
2715 H HA   . PRO   B 64  ? 0.791119 0.567474 0.93703  -0.120145   0.00894798  -0.106498   76  PRO   A HA   
2716 H HB2  . PRO   B 64  ? 0.878686 0.55645  0.99709  -0.119799   0.0335653   -0.137813   76  PRO   A HB2  
2717 H HB3  . PRO   B 64  ? 0.834149 0.542137 0.98109  -0.108238   0.0383879   -0.105301   76  PRO   A HB3  
2718 H HG2  . PRO   B 64  ? 0.926272 0.578701 1.09391  -0.153459   0.036167    -0.133258   76  PRO   A HG2  
2719 H HG3  . PRO   B 64  ? 0.873047 0.58216  1.06695  -0.149607   0.0296344   -0.10691    76  PRO   A HG3  
2720 H HD2  . PRO   B 64  ? 0.95252  0.636758 1.09329  -0.182873   0.00037573  -0.16576    76  PRO   A HD2  
2721 H HD3  . PRO   B 64  ? 0.918843 0.646938 1.10899  -0.190549   -0.00419525 -0.13949    76  PRO   A HD3  
2722 N N    . PHE   B 65  ? 0.733499 0.507122 0.815643 -0.0956966  0.00731526  -0.122648   77  PHE   A N    
2723 C CA   . PHE   B 65  ? 0.722602 0.49419  0.770209 -0.0824503  0.00939751  -0.130714   77  PHE   A CA   
2724 C C    . PHE   B 65  ? 0.754206 0.495335 0.800843 -0.0661236  0.0301762   -0.129569   77  PHE   A C    
2725 O O    . PHE   B 65  ? 0.661923 0.401906 0.730205 -0.0552584  0.0396188   -0.110341   77  PHE   A O    
2726 C CB   . PHE   B 65  ? 0.660108 0.469477 0.703676 -0.071199   0.00163641  -0.113856   77  PHE   A CB   
2727 C CG   . PHE   B 65  ? 0.679397 0.492019 0.689038 -0.0603216  0.00233822  -0.119083   77  PHE   A CG   
2728 C CD1  . PHE   B 65  ? 0.750437 0.569934 0.731214 -0.069381   -0.0106731  -0.132907   77  PHE   A CD1  
2729 C CD2  . PHE   B 65  ? 0.646853 0.458391 0.653922 -0.0424181  0.0148869   -0.10805    77  PHE   A CD2  
2730 C CE1  . PHE   B 65  ? 0.762147 0.583916 0.711407 -0.0604436  -0.00758198 -0.135656   77  PHE   A CE1  
2731 C CE2  . PHE   B 65  ? 0.68358  0.500473 0.664273 -0.0349478  0.0167484   -0.111706   77  PHE   A CE2  
2732 C CZ   . PHE   B 65  ? 0.687304 0.508105 0.638722 -0.0437675  0.00711837  -0.125296   77  PHE   A CZ   
2733 H H    . PHE   B 65  ? 0.715067 0.506112 0.813611 -0.0905798  0.00843658  -0.106522   77  PHE   A H    
2734 H HA   . PHE   B 65  ? 0.749938 0.514873 0.778311 -0.0926165  0.00218986  -0.147646   77  PHE   A HA   
2735 H HB2  . PHE   B 65  ? 0.666688 0.494679 0.716458 -0.0804256  -0.0106851  -0.113108   77  PHE   A HB2  
2736 H HB3  . PHE   B 65  ? 0.650459 0.464055 0.70875  -0.0622296  0.00869402  -0.0986575  77  PHE   A HB3  
2737 H HD1  . PHE   B 65  ? 0.753918 0.576909 0.736317 -0.0825505  -0.0219239  -0.139747   77  PHE   A HD1  
2738 H HD2  . PHE   B 65  ? 0.650557 0.45783  0.67429  -0.0362977  0.0220609   -0.0976397  77  PHE   A HD2  
2739 H HE1  . PHE   B 65  ? 0.76111  0.585898 0.68764  -0.0668043  -0.0159781  -0.144033   77  PHE   A HE1  
2740 H HE2  . PHE   B 65  ? 0.659201 0.478071 0.641877 -0.024504   0.0242244   -0.103755   77  PHE   A HE2  
2741 H HZ   . PHE   B 65  ? 0.703363 0.527495 0.636277 -0.0391438  0.00979092  -0.12639    77  PHE   A HZ   
2742 N N    . VAL   B 66  ? 0.827414 0.545207 0.84791  -0.0634101  0.0376141   -0.149202   78  VAL   A N    
2743 C CA   . VAL   B 66  ? 0.83825  0.527233 0.861767 -0.0465193  0.0587396   -0.14987    78  VAL   A CA   
2744 C C    . VAL   B 66  ? 0.772928 0.475789 0.774548 -0.0313541  0.0648015   -0.151569   78  VAL   A C    
2745 O O    . VAL   B 66  ? 0.87016  0.582617 0.841908 -0.0392197  0.0566542   -0.164841   78  VAL   A O    
2746 C CB   . VAL   B 66  ? 0.931969 0.571904 0.948301 -0.0568076  0.068684    -0.173893   78  VAL   A CB   
2747 C CG1  . VAL   B 66  ? 0.942894 0.55366  0.956177 -0.0357813  0.0926532   -0.178805   78  VAL   A CG1  
2748 C CG2  . VAL   B 66  ? 0.953755 0.574724 0.998619 -0.0711718  0.0670778   -0.168641   78  VAL   A CG2  
2749 H H    . VAL   B 66  ? 0.82793  0.548445 0.827849 -0.0717009  0.0297579   -0.162147   78  VAL   A H    
2750 H HA   . VAL   B 66  ? 0.816224 0.507993 0.86107  -0.0383001  0.063249    -0.132809   78  VAL   A HA   
2751 H HB   . VAL   B 66  ? 0.943219 0.581875 0.935977 -0.0692633  0.0604674   -0.190981   78  VAL   A HB   
2752 H HG11 . VAL   B 66  ? 0.923919 0.543705 0.958534 -0.0215432  0.0981779   -0.159627   78  VAL   A HG11 
2753 H HG12 . VAL   B 66  ? 0.948277 0.567134 0.940512 -0.0311991  0.0947924   -0.187077   78  VAL   A HG12 
2754 H HG13 . VAL   B 66  ? 0.987875 0.562595 0.999304 -0.0410601  0.100818    -0.192288   78  VAL   A HG13 
2755 H HG21 . VAL   B 66  ? 0.993428 0.578406 1.0328   -0.0770985  0.0748215   -0.183995   78  VAL   A HG21 
2756 H HG22 . VAL   B 66  ? 0.941314 0.581454 0.988926 -0.0859693  0.0524922   -0.168523   78  VAL   A HG22 
2757 H HG23 . VAL   B 66  ? 0.931524 0.55685  0.997245 -0.0599287  0.0733087   -0.149461   78  VAL   A HG23 
2758 N N    . PHE   B 67  ? 0.735341 0.441377 0.752997 -0.0106066  0.0782705   -0.136298   79  PHE   A N    
2759 C CA   . PHE   B 67  ? 0.698987 0.422304 0.704175 0.00280936  0.0855602   -0.135308   79  PHE   A CA   
2760 C C    . PHE   B 67  ? 0.720989 0.440571 0.753762 0.0247707   0.102374    -0.120872   79  PHE   A C    
2761 O O    . PHE   B 67  ? 0.72596  0.436098 0.78514  0.0308071   0.104171    -0.105473   79  PHE   A O    
2762 C CB   . PHE   B 67  ? 0.664056 0.426598 0.658994 -2.941e-05  0.0698332   -0.122625   79  PHE   A CB   
2763 C CG   . PHE   B 67  ? 0.634934 0.420321 0.652035 0.00862142  0.0644892   -0.0960347  79  PHE   A CG   
2764 C CD1  . PHE   B 67  ? 0.628467 0.414412 0.660325 0.00308398  0.05642     -0.0844138  79  PHE   A CD1  
2765 C CD2  . PHE   B 67  ? 0.655989 0.462714 0.677096 0.0205663   0.0676497   -0.0829054  79  PHE   A CD2  
2766 C CE1  . PHE   B 67  ? 0.593824 0.396576 0.636764 0.0103955   0.0526883   -0.0617903  79  PHE   A CE1  
2767 C CE2  . PHE   B 67  ? 0.622615 0.447085 0.657017 0.025719    0.0605398   -0.0605844  79  PHE   A CE2  
2768 C CZ   . PHE   B 67  ? 0.606287 0.426311 0.648158 0.0212005   0.053648    -0.0507805  79  PHE   A CZ   
2769 H H    . PHE   B 67  ? 0.73279  0.43143  0.770943 -0.00528361 0.082613    -0.125088   79  PHE   A H    
2770 H HA   . PHE   B 67  ? 0.738356 0.448015 0.72226  -0.00115649 0.0907158   -0.1535     79  PHE   A HA   
2771 H HB2  . PHE   B 67  ? 0.668391 0.43821  0.648798 0.00361416  0.0742201   -0.127117   79  PHE   A HB2  
2772 H HB3  . PHE   B 67  ? 0.666791 0.431888 0.65091  -0.0124095  0.0584175   -0.128447   79  PHE   A HB3  
2773 H HD1  . PHE   B 67  ? 0.638851 0.413493 0.672062 -0.0065316  0.0538729   -0.0921552  79  PHE   A HD1  
2774 H HD2  . PHE   B 67  ? 0.652908 0.461823 0.667035 0.0242814   0.074866    -0.0893998  79  PHE   A HD2  
2775 H HE1  . PHE   B 67  ? 0.597317 0.399236 0.648074 0.00706711  0.0497384   -0.0540807  79  PHE   A HE1  
2776 H HE2  . PHE   B 67  ? 0.61053  0.449865 0.647964 0.0315823   0.0608933   -0.0522145  79  PHE   A HE2  
2777 H HZ   . PHE   B 67  ? 0.587545 0.417233 0.632918 0.0243724   0.049587    -0.0366218  79  PHE   A HZ   
2778 N N    . SER   B 68  ? 0.697045 0.425332 0.724421 0.0368633   0.115251    -0.124732   80  SER   A N    
2779 C CA   . SER   B 68  ? 0.683966 0.419438 0.7424   0.0590734   0.129984    -0.109164   80  SER   A CA   
2780 C C    . SER   B 68  ? 0.617585 0.398072 0.687589 0.0627309   0.117224    -0.0850653  80  SER   A C    
2781 O O    . SER   B 68  ? 0.627654 0.431591 0.678505 0.0562301   0.111817    -0.0877484  80  SER   A O    
2782 C CB   . SER   B 68  ? 0.708918 0.431421 0.760669 0.0703158   0.153593    -0.125916   80  SER   A CB   
2783 O OG   . SER   B 68  ? 0.8279   0.50146  0.861475 0.0644391   0.16477     -0.151317   80  SER   A OG   
2784 H H    . SER   B 68  ? 0.708717 0.440437 0.713223 0.0309901   0.114834    -0.136552   80  SER   A H    
2785 H HA   . SER   B 68  ? 0.689595 0.408115 0.766431 0.0640325   0.132782    -0.102344   80  SER   A HA   
2786 H HB2  . SER   B 68  ? 0.719666 0.458875 0.752379 0.0653332   0.151993    -0.131245   80  SER   A HB2  
2787 H HB3  . SER   B 68  ? 0.724883 0.455371 0.803324 0.0864844   0.163465    -0.113663   80  SER   A HB3  
2789 N N    . LEU   B 69  ? 0.60805  0.397127 0.70611  0.0717522   0.111882    -0.0613201  81  LEU   A N    
2790 C CA   . LEU   B 69  ? 0.533839 0.359335 0.637331 0.0712747   0.0962177   -0.039305   81  LEU   A CA   
2791 C C    . LEU   B 69  ? 0.541445 0.398594 0.65777  0.0803829   0.101715    -0.0327593  81  LEU   A C    
2792 O O    . LEU   B 69  ? 0.579687 0.437175 0.722765 0.0969612   0.117775    -0.0300772  81  LEU   A O    
2793 C CB   . LEU   B 69  ? 0.518446 0.339998 0.644311 0.0791161   0.0908759   -0.0164653  81  LEU   A CB   
2794 C CG   . LEU   B 69  ? 0.506518 0.357999 0.630953 0.0765839   0.0730033   0.00586137  81  LEU   A CG   
2795 C CD1  . LEU   B 69  ? 0.49442  0.350128 0.58755  0.0592321   0.060366    -0.00093981 81  LEU   A CD1  
2796 C CD2  . LEU   B 69  ? 0.512797 0.357365 0.653005 0.0846657   0.0687192   0.0288516   81  LEU   A CD2  
2797 H H    . LEU   B 69  ? 0.614238 0.38363  0.726179 0.0778894   0.118106    -0.0588208  81  LEU   A H    
2798 H HA   . LEU   B 69  ? 0.527837 0.358355 0.611211 0.0591027   0.0857498   -0.0432101  81  LEU   A HA   
2799 H HB2  . LEU   B 69  ? 0.534144 0.334436 0.653978 0.0727574   0.0902869   -0.0211082  81  LEU   A HB2  
2800 H HB3  . LEU   B 69  ? 0.540749 0.357586 0.688073 0.0925558   0.100843    -0.0111677  81  LEU   A HB3  
2801 H HG   . LEU   B 69  ? 0.497251 0.370996 0.630056 0.0810661   0.0724445   0.0108484   81  LEU   A HG   
2802 H HD11 . LEU   B 69  ? 0.48776  0.351308 0.56981  0.0547043   0.0609997   -0.0116097  81  LEU   A HD11 
2803 H HD12 . LEU   B 69  ? 0.481383 0.349578 0.570719 0.0578578   0.0506925   0.0121622   81  LEU   A HD12 
2804 H HD13 . LEU   B 69  ? 0.499328 0.336957 0.587231 0.0540539   0.0616582   -0.00717402 81  LEU   A HD13 
2805 H HD21 . LEU   B 69  ? 0.528591 0.368825 0.69081  0.0974221   0.0770049   0.0344731   81  LEU   A HD21 
2806 H HD22 . LEU   B 69  ? 0.520317 0.345116 0.652581 0.0787605   0.0693717   0.0257001   81  LEU   A HD22 
2807 H HD23 . LEU   B 69  ? 0.500438 0.364055 0.63614  0.0828582   0.0572634   0.041892    81  LEU   A HD23 
2808 N N    . GLY   B 70  ? 0.5722   0.455868 0.671941 0.0694896   0.0891874   -0.0290658  82  GLY   A N    
2809 C CA   . GLY   B 70  ? 0.534816 0.453554 0.649781 0.0734448   0.090774    -0.0187107  82  GLY   A CA   
2810 C C    . GLY   B 70  ? 0.584002 0.504754 0.691792 0.0751175   0.109942    -0.0352503  82  GLY   A C    
2811 O O    . GLY   B 70  ? 0.684079 0.63541  0.813042 0.0801866   0.116568    -0.0260418  82  GLY   A O    
2812 H H    . GLY   B 70  ? 0.542423 0.421957 0.622256 0.0589728   0.0797292   -0.0326429  82  GLY   A H    
2813 H HA2  . GLY   B 70  ? 0.530378 0.462618 0.633267 0.0638263   0.0777312   -0.0126343  82  GLY   A HA2  
2814 H HA3  . GLY   B 70  ? 0.549083 0.478205 0.691885 0.0843261   0.092135    -0.00509369 82  GLY   A HA3  
2815 N N    . LYS   B 71  ? 0.604022 0.494322 0.68217  0.0699443   0.118954    -0.0587114  83  LYS   A N    
2816 C CA   . LYS   B 71  ? 0.670922 0.558998 0.731266 0.0702326   0.137979    -0.0756434  83  LYS   A CA   
2817 C C    . LYS   B 71  ? 0.713305 0.605929 0.731167 0.0518547   0.126745    -0.0829165  83  LYS   A C    
2818 O O    . LYS   B 71  ? 0.736695 0.625589 0.729463 0.0489535   0.140047    -0.0962397  83  LYS   A O    
2819 C CB   . LYS   B 71  ? 0.686689 0.534087 0.736628 0.0768805   0.157031    -0.0982814  83  LYS   A CB   
2820 H H    . LYS   B 71  ? 0.617149 0.487955 0.684494 0.0651823   0.112923    -0.0641782  83  LYS   A H    
2821 H HA   . LYS   B 71  ? 0.66318  0.573323 0.746311 0.078561    0.147134    -0.0666322  83  LYS   A HA   
2824 N N    . GLY   B 72  ? 0.749164 0.647936 0.756942 0.0405775   0.103703    -0.0733629  84  GLY   A N    
2825 C CA   . GLY   B 72  ? 0.760571 0.663302 0.732368 0.0261464   0.0929819   -0.0763039  84  GLY   A CA   
2826 C C    . GLY   B 72  ? 0.73791  0.615199 0.671796 0.0176184   0.0914443   -0.0968177  84  GLY   A C    
2827 O O    . GLY   B 72  ? 0.708625 0.587498 0.609361 0.00839083  0.0876149   -0.100989   84  GLY   A O    
2828 H H    . GLY   B 72  ? 0.718951 0.618059 0.741694 0.0427289   0.095457    -0.0643276  84  GLY   A H    
2829 H HA2  . GLY   B 72  ? 0.724671 0.633303 0.697559 0.0217219   0.0787583   -0.0663749  84  GLY   A HA2  
2830 H HA3  . GLY   B 72  ? 0.747112 0.664346 0.717883 0.0257804   0.100236    -0.073201   84  GLY   A HA3  
2831 N N    . GLN   B 73  ? 0.73573  0.589616 0.673992 0.0186009   0.0908224   -0.107503   85  GLN   A N    
2832 C CA   . GLN   B 73  ? 0.683495 0.517816 0.590876 0.00615026  0.0807195   -0.123831   85  GLN   A CA   
2833 C C    . GLN   B 73  ? 0.661661 0.50671  0.567044 -0.00255903 0.0575925   -0.112717   85  GLN   A C    
2834 O O    . GLN   B 73  ? 0.706491 0.546591 0.588605 -0.0133877  0.0450036   -0.121022   85  GLN   A O    
2835 C CB   . GLN   B 73  ? 0.714165 0.519259 0.632058 0.00784291  0.0880381   -0.137947   85  GLN   A CB   
2836 C CG   . GLN   B 73  ? 0.769527 0.557189 0.687903 0.01907     0.114308    -0.151136   85  GLN   A CG   
2837 C CD   . GLN   B 73  ? 0.774724 0.528055 0.709324 0.023316    0.123475    -0.161831   85  GLN   A CD   
2838 O OE1  . GLN   B 73  ? 0.707608 0.453738 0.657788 0.0174286   0.110295    -0.156322   85  GLN   A OE1  
2839 N NE2  . GLN   B 73  ? 0.814672 0.544714 0.745882 0.0339824   0.148489    -0.176631   85  GLN   A NE2  
2840 H H    . GLN   B 73  ? 0.718473 0.569    0.680536 0.0264022   0.0958387   -0.103594   85  GLN   A H    
2841 H HA   . GLN   B 73  ? 0.720094 0.552191 0.600884 0.00216149  0.0849544   -0.132793   85  GLN   A HA   
2842 H HB2  . GLN   B 73  ? 0.698464 0.505486 0.641776 0.0119224   0.0846197   -0.127307   85  GLN   A HB2  
2843 H HB3  . GLN   B 73  ? 0.732327 0.526201 0.631525 -0.00281062 0.0791655   -0.148789   85  GLN   A HB3  
2844 H HG2  . GLN   B 73  ? 0.786052 0.566761 0.673888 0.0136883   0.118685    -0.164304   85  GLN   A HG2  
2845 H HG3  . GLN   B 73  ? 0.74584  0.550602 0.683785 0.0293109   0.122538    -0.139331   85  GLN   A HG3  
2846 H HE21 . GLN   B 73  ? 0.838491 0.542749 0.775056 0.0359874   0.155236    -0.185053   85  GLN   A HE21 
2847 H HE22 . GLN   B 73  ? 0.822405 0.561557 0.746208 0.0393616   0.159698    -0.178037   85  GLN   A HE22 
2848 N N    . VAL   B 74  ? 0.568445 0.428687 0.497655 0.00259783  0.0521314   -0.093584   86  VAL   A N    
2849 C CA   . VAL   B 74  ? 0.535975 0.404973 0.46269  -0.00245266 0.0352883   -0.0822958  86  VAL   A CA   
2850 C C    . VAL   B 74  ? 0.496221 0.38175  0.419524 -0.00093386 0.0327757   -0.067321   86  VAL   A C    
2851 O O    . VAL   B 74  ? 0.548967 0.443747 0.479246 0.00291713  0.0424674   -0.0637425  86  VAL   A O    
2852 C CB   . VAL   B 74  ? 0.556142 0.419085 0.509513 0.00036434  0.032744    -0.0756823  86  VAL   A CB   
2853 C CG1  . VAL   B 74  ? 0.574616 0.419599 0.529974 -0.00631938 0.0324938   -0.0907215  86  VAL   A CG1  
2854 C CG2  . VAL   B 74  ? 0.546397 0.411319 0.525318 0.0113552   0.0424297   -0.0649404  86  VAL   A CG2  
2855 H H    . VAL   B 74  ? 0.575508 0.440419 0.522474 0.00997019  0.0596859   -0.0873401  86  VAL   A H    
2856 H HA   . VAL   B 74  ? 0.549444 0.41597  0.459139 -0.00899968 0.0281258   -0.0886399  86  VAL   A HA   
2857 H HB   . VAL   B 74  ? 0.534411 0.403926 0.486637 -0.00134614 0.0242766   -0.0672595  86  VAL   A HB   
2858 H HG11 . VAL   B 74  ? 0.594992 0.428809 0.54829  -0.00446949 0.0420458   -0.100684   86  VAL   A HG11 
2859 H HG12 . VAL   B 74  ? 0.580532 0.428288 0.521511 -0.0137558  0.023674    -0.095797   86  VAL   A HG12 
2860 H HG13 . VAL   B 74  ? 0.569207 0.410532 0.542026 -0.00550096 0.031731    -0.0849344  86  VAL   A HG13 
2861 H HG21 . VAL   B 74  ? 0.540599 0.401808 0.531932 0.0126618   0.0398176   -0.0580371  86  VAL   A HG21 
2862 H HG22 . VAL   B 74  ? 0.536125 0.413969 0.513644 0.0131811   0.0412052   -0.0565519  86  VAL   A HG22 
2863 H HG23 . VAL   B 74  ? 0.562789 0.419609 0.546991 0.0151323   0.0524324   -0.0726778  86  VAL   A HG23 
2864 N N    . ILE   B 75  ? 0.509239 0.398015 0.423472 -0.00437888 0.0203904   -0.0584719  87  ILE   A N    
2865 C CA   . ILE   B 75  ? 0.542062 0.438878 0.45078  -0.00506109 0.0170478   -0.0453254  87  ILE   A CA   
2866 C C    . ILE   B 75  ? 0.517897 0.421538 0.450477 -0.00014301 0.0198274   -0.0351615  87  ILE   A C    
2867 O O    . ILE   B 75  ? 0.504131 0.403306 0.455551 0.005159    0.021699    -0.0344656  87  ILE   A O    
2868 C CB   . ILE   B 75  ? 0.527036 0.418831 0.422343 -0.00694186 0.00572067  -0.039059   87  ILE   A CB   
2869 C CG1  . ILE   B 75  ? 0.47847  0.366603 0.390967 -0.00316089 0.00301047  -0.0363757  87  ILE   A CG1  
2870 C CG2  . ILE   B 75  ? 0.539905 0.429492 0.412495 -0.0108935  0.00027877  -0.0447136  87  ILE   A CG2  
2871 C CD1  . ILE   B 75  ? 0.474125 0.358553 0.378158 -0.00165722 -0.00340732 -0.0287665  87  ILE   A CD1  
2872 H H    . ILE   B 75  ? 0.513707 0.39871  0.425454 -0.00663714 0.0141775   -0.0609748  87  ILE   A H    
2873 H HA   . ILE   B 75  ? 0.537028 0.437503 0.434695 -0.00766685 0.0206153   -0.04662    87  ILE   A HA   
2874 H HB   . ILE   B 75  ? 0.517646 0.409888 0.407242 -0.00803663 0.00438042  -0.0316777  87  ILE   A HB   
2875 H HG12 . ILE   B 75  ? 0.491201 0.37822  0.410236 -0.00405278 0.00336627  -0.043684   87  ILE   A HG12 
2876 H HG13 . ILE   B 75  ? 0.481209 0.369978 0.40516  -0.00061738 0.00629881  -0.0319673  87  ILE   A HG13 
2877 H HG21 . ILE   B 75  ? 0.538211 0.425511 0.4048   -0.0100935  -0.00599052 -0.0388634  87  ILE   A HG21 
2878 H HG22 . ILE   B 75  ? 0.545783 0.434674 0.421926 -0.0117622  -0.00050592 -0.0527822  87  ILE   A HG22 
2879 H HG23 . ILE   B 75  ? 0.549336 0.440152 0.409271 -0.013534   0.00387054  -0.0454812  87  ILE   A HG23 
2880 H HD11 . ILE   B 75  ? 0.475278 0.356402 0.36859  -0.00194634 -0.00375936 -0.0231885  87  ILE   A HD11 
2881 H HD12 . ILE   B 75  ? 0.4698   0.353248 0.386097 0.00086772  -0.0023002  -0.0262621  87  ILE   A HD12 
2882 H HD13 . ILE   B 75  ? 0.480797 0.366467 0.377707 -0.00281738 -0.00775977 -0.0314538  87  ILE   A HD13 
2883 N N    . LYS   B 76  ? 0.508447 0.422882 0.439388 -0.00338946 0.0188254   -0.0261562  88  LYS   A N    
2884 C CA   . LYS   B 76  ? 0.561581 0.489144 0.514838 -0.00082743 0.0181202   -0.0148207  88  LYS   A CA   
2885 C C    . LYS   B 76  ? 0.505973 0.424756 0.461083 0.0019236   0.0100924   -0.00712244 88  LYS   A C    
2886 O O    . LYS   B 76  ? 0.504252 0.428507 0.480519 0.00824676  0.0108583   0.0002276   88  LYS   A O    
2887 C CB   . LYS   B 76  ? 0.525533 0.466799 0.474038 -0.0100332  0.0147342   -0.00679583 88  LYS   A CB   
2888 H H    . LYS   B 76  ? 0.527501 0.441628 0.442919 -0.0083111  0.0174988   -0.0263126  88  LYS   A H    
2889 H HA   . LYS   B 76  ? 0.535163 0.468617 0.506419 0.00499164  0.0259623   -0.0169498  88  LYS   A HA   
2892 N N    . ALA   B 77  ? 0.443755 0.34834  0.376816 -0.00130107 0.00429705  -0.00792492 89  ALA   A N    
2893 C CA   . ALA   B 77  ? 0.488008 0.38257  0.418047 0.00145264  0.00069062  -0.00124859 89  ALA   A CA   
2894 C C    . ALA   B 77  ? 0.498068 0.38994  0.450246 0.00861398  0.00660071  -0.00182243 89  ALA   A C    
2895 O O    . ALA   B 77  ? 0.381375 0.269671 0.338409 0.011976    0.00584025  0.00812494  89  ALA   A O    
2896 C CB   . ALA   B 77  ? 0.425647 0.306124 0.333565 7.624e-05   -0.00146319 -0.00326339 89  ALA   A CB   
2897 H H    . ALA   B 77  ? 0.471018 0.371921 0.390295 -0.00457012 0.00362987  -0.0119628  89  ALA   A H    
2898 H HA   . ALA   B 77  ? 0.47097  0.369025 0.399189 -0.00042546 -0.00362309 0.00635428  89  ALA   A HA   
2899 H HB1  . ALA   B 77  ? 0.449744 0.327039 0.342131 -0.00432065 -0.00465874 -0.00224466 89  ALA   A HB1  
2900 H HB2  . ALA   B 77  ? 0.44248  0.322915 0.353576 0.00124709  0.00040288  -0.00936079 89  ALA   A HB2  
2901 H HB3  . ALA   B 77  ? 0.446987 0.3212   0.353097 0.00253152  -0.0010861  0.00107103  89  ALA   A HB3  
2902 N N    . TRP   B 78  ? 0.452928 0.34308  0.414367 0.00948389  0.0122728   -0.0133938  90  TRP   A N    
2903 C CA   . TRP   B 78  ? 0.471218 0.353111 0.452782 0.0135701   0.0183116   -0.0155371  90  TRP   A CA   
2904 C C    . TRP   B 78  ? 0.456196 0.341027 0.459332 0.0212169   0.0242175   -0.00974126 90  TRP   A C    
2905 O O    . TRP   B 78  ? 0.484829 0.36246  0.501892 0.026304    0.0263889   -0.00056896 90  TRP   A O    
2906 C CB   . TRP   B 78  ? 0.449715 0.325291 0.431292 0.00936907  0.0207      -0.0313442  90  TRP   A CB   
2907 C CG   . TRP   B 78  ? 0.447928 0.321654 0.426265 0.00464006  0.0153746   -0.0322072  90  TRP   A CG   
2908 C CD1  . TRP   B 78  ? 0.44662  0.325041 0.411497 0.00416903  0.00965872  -0.0259634  90  TRP   A CD1  
2909 C CD2  . TRP   B 78  ? 0.487482 0.35475  0.480924 -0.00023727 0.0163582   -0.0393143  90  TRP   A CD2  
2910 N NE1  . TRP   B 78  ? 0.462847 0.343267 0.437331 0.00143395  0.00756132  -0.0274794  90  TRP   A NE1  
2911 C CE2  . TRP   B 78  ? 0.470435 0.345929 0.46354  -0.00311716 0.0103687   -0.0353048  90  TRP   A CE2  
2912 C CE3  . TRP   B 78  ? 0.516755 0.370737 0.524819 -0.00299151 0.0221769   -0.0486636  90  TRP   A CE3  
2913 C CZ2  . TRP   B 78  ? 0.480289 0.357875 0.492087 -0.010135   0.0085041   -0.0388284  90  TRP   A CZ2  
2914 C CZ3  . TRP   B 78  ? 0.518703 0.368614 0.539896 -0.0121388  0.0196978   -0.0540558  90  TRP   A CZ3  
2915 C CH2  . TRP   B 78  ? 0.487397 0.352489 0.512337 -0.016548   0.0119186   -0.0487759  90  TRP   A CH2  
2916 H H    . TRP   B 78  ? 0.467804 0.359876 0.420981 0.00660816  0.0122432   -0.0199727  90  TRP   A H    
2917 H HA   . TRP   B 78  ? 0.458166 0.335432 0.43943  0.013887    0.0169936   -0.00929411 90  TRP   A HA   
2918 H HB2  . TRP   B 78  ? 0.458903 0.338744 0.429666 0.00731007  0.0202937   -0.0373594  90  TRP   A HB2  
2919 H HB3  . TRP   B 78  ? 0.465037 0.333487 0.459913 0.0115464   0.0265001   -0.0349865  90  TRP   A HB3  
2920 H HD1  . TRP   B 78  ? 0.446536 0.326474 0.398349 0.00517571  0.00763314  -0.0216272  90  TRP   A HD1  
2921 H HE1  . TRP   B 78  ? 0.456229 0.340051 0.427315 0.0024823   0.00544882  -0.023602   90  TRP   A HE1  
2922 H HE3  . TRP   B 78  ? 0.518314 0.365796 0.528598 0.00108084  0.0280901   -0.051045   90  TRP   A HE3  
2923 H HZ2  . TRP   B 78  ? 0.473048 0.360124 0.489182 -0.0108817  0.00510073  -0.0347998  90  TRP   A HZ2  
2924 H HZ3  . TRP   B 78  ? 0.530842 0.367871 0.560134 -0.0156758  0.0235708   -0.0614547  90  TRP   A HZ3  
2925 H HH2  . TRP   B 78  ? 0.50046  0.366578 0.539005 -0.0237493  0.00985808  -0.0514616  90  TRP   A HH2  
2926 N N    . ASP   B 79  ? 0.488221 0.384498 0.495535 0.0229375   0.0279001   -0.013172   91  ASP   A N    
2927 C CA   . ASP   B 79  ? 0.501213 0.406158 0.535154 0.032954    0.0344655   -0.00552584 91  ASP   A CA   
2928 C C    . ASP   B 79  ? 0.502569 0.417289 0.543646 0.0356647   0.0245779   0.0149058   91  ASP   A C    
2929 O O    . ASP   B 79  ? 0.591852 0.502993 0.653421 0.0452088   0.0271013   0.0256108   91  ASP   A O    
2930 C CB   . ASP   B 79  ? 0.505865 0.426498 0.543002 0.0332759   0.0416701   -0.0116646  91  ASP   A CB   
2931 C CG   . ASP   B 79  ? 0.509996 0.416581 0.544189 0.03567     0.0565007   -0.0308404  91  ASP   A CG   
2932 O OD1  . ASP   B 79  ? 0.552665 0.437259 0.592483 0.0392348   0.0621257   -0.0384184  91  ASP   A OD1  
2933 O OD2  . ASP   B 79  ? 0.499272 0.414371 0.522817 0.0327002   0.0629795   -0.0384498  91  ASP   A OD2  
2934 H H    . ASP   B 79  ? 0.481219 0.380926 0.475885 0.0184081   0.0271348   -0.0194643  91  ASP   A H    
2935 H HA   . ASP   B 79  ? 0.511155 0.403312 0.5559   0.0377779   0.0416877   -0.00991055 91  ASP   A HA   
2936 H HB2  . ASP   B 79  ? 0.495591 0.422716 0.516274 0.0255319   0.0357949   -0.0119021  91  ASP   A HB2  
2937 H HB3  . ASP   B 79  ? 0.501905 0.43638  0.559004 0.0393411   0.0430985   -0.00199027 91  ASP   A HB3  
2938 N N    . ILE   B 80  ? 0.497374 0.420713 0.517807 0.0267555   0.0128665   0.0205189   92  ILE   A N    
2939 C CA   . ILE   B 80  ? 0.55579  0.485599 0.571821 0.0256466   0.0008536   0.0376944   92  ILE   A CA   
2940 C C    . ILE   B 80  ? 0.52021  0.429628 0.525148 0.0280015   0.00106299  0.0432427   92  ILE   A C    
2941 O O    . ILE   B 80  ? 0.61041  0.519872 0.623222 0.0337614   -0.00211745 0.0583408   92  ILE   A O    
2942 C CB   . ILE   B 80  ? 0.616332 0.552142 0.606004 0.0125835   -0.00993229 0.0371781   92  ILE   A CB   
2943 C CG1  . ILE   B 80  ? 0.655227 0.617056 0.663087 0.00901431  -0.0108902  0.0386176   92  ILE   A CG1  
2944 C CG2  . ILE   B 80  ? 0.687195 0.617363 0.653896 0.00738356  -0.0227313  0.0490482   92  ILE   A CG2  
2945 C CD1  . ILE   B 80  ? 0.763763 0.724285 0.745699 -0.00571498 -0.0162882  0.0330131   92  ILE   A CD1  
2946 H H    . ILE   B 80  ? 0.506199 0.429375 0.512227 0.0206333   0.0120997   0.0131663   92  ILE   A H    
2947 H HA   . ILE   B 80  ? 0.54974  0.492911 0.586723 0.0313045   0.00010902  0.0464338   92  ILE   A HA   
2948 H HB   . ILE   B 80  ? 0.618101 0.542585 0.592093 0.00914963  -0.00681767 0.0275207   92  ILE   A HB   
2949 H HG12 . ILE   B 80  ? 0.67078  0.647615 0.692967 0.0103465   -0.0176423  0.0502704   92  ILE   A HG12 
2950 H HG13 . ILE   B 80  ? 0.662112 0.626926 0.685897 0.0150282   -0.0004808  0.0325182   92  ILE   A HG13 
2951 H HG21 . ILE   B 80  ? 0.674132 0.606465 0.625169 -0.00177403 -0.029557   0.0479596   92  ILE   A HG21 
2952 H HG22 . ILE   B 80  ? 0.674052 0.614514 0.655149 0.0115577   -0.0271308  0.0602195   92  ILE   A HG22 
2953 H HG23 . ILE   B 80  ? 0.672343 0.585621 0.624497 0.00874093  -0.0194271  0.0468756   92  ILE   A HG23 
2954 H HD11 . ILE   B 80  ? 0.727789 0.67453  0.696103 -0.00589649 -0.0105623  0.0232914   92  ILE   A HD11 
2955 H HD12 . ILE   B 80  ? 0.728405 0.707004 0.724879 -0.00877452 -0.0154284  0.0349766   92  ILE   A HD12 
2956 H HD13 . ILE   B 80  ? 0.737541 0.692012 0.701617 -0.0121313  -0.0259541  0.0376739   92  ILE   A HD13 
2957 N N    . GLY   B 81  ? 0.501209 0.394881 0.489462 0.0237957   0.0054079   0.0326897   93  GLY   A N    
2958 C CA   . GLY   B 81  ? 0.494852 0.37308  0.470845 0.0240146   0.00723481  0.0388847   93  GLY   A CA   
2959 C C    . GLY   B 81  ? 0.509794 0.377808 0.509844 0.0309124   0.0161584   0.0436194   93  GLY   A C    
2960 O O    . GLY   B 81  ? 0.443589 0.304151 0.441004 0.0342281   0.016369    0.0588296   93  GLY   A O    
2961 H H    . GLY   B 81  ? 0.495686 0.389668 0.480946 0.0208992   0.00764338  0.0223053   93  GLY   A H    
2962 H HA2  . GLY   B 81  ? 0.509514 0.388339 0.470986 0.0227005   0.00108299  0.0482059   93  GLY   A HA2  
2963 H HA3  . GLY   B 81  ? 0.496408 0.369128 0.46169  0.0205039   0.00931438  0.0312558   93  GLY   A HA3  
2964 N N    . VAL   B 82  ? 0.475276 0.339693 0.494931 0.0320918   0.0237316   0.0305188   94  VAL   A N    
2965 C CA   . VAL   B 82  ? 0.500643 0.348627 0.542225 0.0365619   0.0332189   0.0322389   94  VAL   A CA   
2966 C C    . VAL   B 82  ? 0.508339 0.356968 0.568038 0.0483216   0.0338998   0.0487771   94  VAL   A C    
2967 O O    . VAL   B 82  ? 0.494629 0.326661 0.564676 0.0526023   0.0394783   0.0598358   94  VAL   A O    
2968 C CB   . VAL   B 82  ? 0.510251 0.34918  0.561935 0.0326149   0.0402071   0.0114815   94  VAL   A CB   
2969 C CG1  . VAL   B 82  ? 0.55323  0.368837 0.62752  0.0365237   0.0509817   0.0110329   94  VAL   A CG1  
2970 C CG2  . VAL   B 82  ? 0.497391 0.336517 0.537622 0.0216284   0.0374096   0.00173366  94  VAL   A CG2  
2971 H H    . VAL   B 82  ? 0.478352 0.348155 0.495261 0.0293567   0.0232073   0.0202216   94  VAL   A H    
2972 H HA   . VAL   B 82  ? 0.502531 0.343052 0.539231 0.0338284   0.0347101   0.0373128   94  VAL   A HA   
2973 H HB   . VAL   B 82  ? 0.507409 0.354669 0.557732 0.0341382   0.0396695   0.00474521  94  VAL   A HB   
2974 H HG11 . VAL   B 82  ? 0.552706 0.360814 0.629375 0.0353739   0.0521126   0.0209674   94  VAL   A HG11 
2975 H HG12 . VAL   B 82  ? 0.553758 0.369143 0.638666 0.0455596   0.0540729   0.0159637   94  VAL   A HG12 
2976 H HG13 . VAL   B 82  ? 0.552808 0.360176 0.628165 0.0308867   0.0540222   -0.00376175 94  VAL   A HG13 
2977 H HG21 . VAL   B 82  ? 0.503687 0.338047 0.547823 0.0175434   0.0392216   -0.0112398  94  VAL   A HG21 
2978 H HG22 . VAL   B 82  ? 0.488234 0.338225 0.513615 0.0201109   0.0317389   0.00181854  94  VAL   A HG22 
2979 H HG23 . VAL   B 82  ? 0.503294 0.336457 0.547422 0.020152    0.0396709   0.00900803  94  VAL   A HG23 
2980 N N    . ALA   B 83  ? 0.508875 0.378324 0.573927 0.053224    0.0276474   0.0534701   95  ALA   A N    
2981 C CA   . ALA   B 83  ? 0.470988 0.348858 0.558442 0.0658947   0.0254369   0.0729549   95  ALA   A CA   
2982 C C    . ALA   B 83  ? 0.522994 0.399308 0.595108 0.0659253   0.015216    0.0954803   95  ALA   A C    
2983 O O    . ALA   B 83  ? 0.548556 0.427292 0.63836  0.0772788   0.0125902   0.115552    95  ALA   A O    
2984 C CB   . ALA   B 83  ? 0.429085 0.337443 0.529638 0.0688042   0.0193211   0.0751619   95  ALA   A CB   
2985 H H    . ALA   B 83  ? 0.484154 0.364276 0.540813 0.0485389   0.0245022   0.0454844   95  ALA   A H    
2986 H HA   . ALA   B 83  ? 0.491742 0.355573 0.597476 0.0731649   0.0353943   0.0715061   95  ALA   A HA   
2987 H HB1  . ALA   B 83  ? 0.433961 0.342525 0.542189 0.0695139   0.0277772   0.0616486   95  ALA   A HB1  
2988 H HB2  . ALA   B 83  ? 0.430654 0.350095 0.512824 0.0601887   0.0092536   0.0762267   95  ALA   A HB2  
2989 H HB3  . ALA   B 83  ? 0.447957 0.364818 0.567992 0.0782848   0.017319    0.0895963   95  ALA   A HB3  
2990 N N    . THR   B 84  ? 0.528536 0.401087 0.56615  0.054502    0.00960469  0.0933649   96  THR   A N    
2991 C CA   . THR   B 84  ? 0.553929 0.42086  0.566931 0.0533519   0.00221405  0.11259     96  THR   A CA   
2992 C C    . THR   B 84  ? 0.526266 0.367132 0.537172 0.0542041   0.0155341   0.117391    96  THR   A C    
2993 O O    . THR   B 84  ? 0.529825 0.362698 0.517388 0.0537324   0.0131256   0.134221    96  THR   A O    
2994 C CB   . THR   B 84  ? 0.561752 0.432647 0.533634 0.0413597   -0.00745234 0.107841    96  THR   A CB   
2995 O OG1  . THR   B 84  ? 0.526571 0.383178 0.488053 0.0360349   0.00433162  0.0920399   96  THR   A OG1  
2996 C CG2  . THR   B 84  ? 0.549451 0.443072 0.521058 0.0354869   -0.0197654  0.100911    96  THR   A CG2  
2997 H H    . THR   B 84  ? 0.515552 0.388216 0.543075 0.0479047   0.0109603   0.0800339   96  THR   A H    
2998 H HA   . THR   B 84  ? 0.556275 0.432556 0.579105 0.0595511   -0.00490548 0.126978    96  THR   A HA   
2999 H HB   . THR   B 84  ? 0.574632 0.441139 0.526621 0.0406981   -0.0127393  0.120657    96  THR   A HB   
3001 H HG21 . THR   B 84  ? 0.554628 0.444846 0.497782 0.0273914   -0.0251775  0.0978676   96  THR   A HG21 
3002 H HG22 . THR   B 84  ? 0.533035 0.429761 0.519489 0.0357624   -0.0135876  0.0884743   96  THR   A HG22 
3003 H HG23 . THR   B 84  ? 0.55494  0.463    0.539888 0.0391608   -0.0280628  0.112501    96  THR   A HG23 
3004 N N    . MET   B 85  ? 0.505566 0.333265 0.537381 0.0532192   0.0290723   0.102801    97  MET   A N    
3005 C CA   . MET   B 85  ? 0.536786 0.343128 0.568839 0.0492342   0.0415579   0.105933    97  MET   A CA   
3006 C C    . MET   B 85  ? 0.573814 0.359459 0.631443 0.0575359   0.0501802   0.119714    97  MET   A C    
3007 O O    . MET   B 85  ? 0.535361 0.319839 0.61708  0.0671567   0.0505554   0.118964    97  MET   A O    
3008 C CB   . MET   B 85  ? 0.511045 0.315911 0.550504 0.0394927   0.0485096   0.0832172   97  MET   A CB   
3009 C CG   . MET   B 85  ? 0.505737 0.325109 0.520128 0.0329805   0.042916    0.0734115   97  MET   A CG   
3010 S SD   . MET   B 85  ? 0.538412 0.362603 0.565758 0.0238325   0.0461033   0.0495634   97  MET   A SD   
3011 C CE   . MET   B 85  ? 0.581795 0.396124 0.62133  0.0176514   0.059254    0.0577239   97  MET   A CE   
3012 H H    . MET   B 85  ? 0.501773 0.334067 0.547406 0.0539303   0.030506    0.0909093   97  MET   A H    
3013 H HA   . MET   B 85  ? 0.543574 0.349242 0.553229 0.0469417   0.0400729   0.115335    97  MET   A HA   
3014 H HB2  . MET   B 85  ? 0.509667 0.314792 0.564405 0.0407557   0.0489406   0.0722773   97  MET   A HB2  
3015 H HB3  . MET   B 85  ? 0.525912 0.31877  0.572677 0.0360976   0.0568418   0.0861558   97  MET   A HB3  
3016 H HG2  . MET   B 85  ? 0.521665 0.337631 0.520301 0.0318014   0.0454811   0.082058    97  MET   A HG2  
3017 H HG3  . MET   B 85  ? 0.505169 0.334619 0.510308 0.0348682   0.0345799   0.072463    97  MET   A HG3  
3018 H HE1  . MET   B 85  ? 0.566749 0.386    0.618341 0.0115747   0.0598356   0.0470965   97  MET   A HE1  
3019 H HE2  . MET   B 85  ? 0.588443 0.390419 0.639598 0.0187654   0.0641394   0.0652552   97  MET   A HE2  
3020 H HE3  . MET   B 85  ? 0.578236 0.394662 0.601049 0.0189397   0.0614079   0.0658434   97  MET   A HE3  
3021 N N    . LYS   B 86  ? 0.643734 0.410911 0.696139 0.0541191   0.0596115   0.132944    98  LYS   A N    
3022 C CA   . LYS   B 86  ? 0.697953 0.438178 0.772262 0.0593607   0.0703236   0.147088    98  LYS   A CA   
3023 C C    . LYS   B 86  ? 0.659604 0.38195  0.75365  0.0470171   0.0840109   0.130939    98  LYS   A C    
3024 O O    . LYS   B 86  ? 0.625779 0.36004  0.713449 0.0350295   0.0850642   0.11699     98  LYS   A O    
3025 C CB   . LYS   B 86  ? 0.803567 0.531521 0.857674 0.0607722   0.0738367   0.175889    98  LYS   A CB   
3026 C CG   . LYS   B 86  ? 0.87483  0.62028  0.889798 0.0639709   0.0596793   0.191609    98  LYS   A CG   
3027 C CD   . LYS   B 86  ? 0.917522 0.668331 0.935562 0.0782732   0.0458416   0.21442     98  LYS   A CD   
3028 C CE   . LYS   B 86  ? 1.01289  0.782122 0.988348 0.0763562   0.028168    0.226277    98  LYS   A CE   
3029 N NZ   . LYS   B 86  ? 1.10216  0.878917 1.08162  0.089134    0.0125504   0.25423     98  LYS   A NZ   
3030 H H    . LYS   B 86  ? 0.636153 0.406413 0.670441 0.0482194   0.0607359   0.133497    98  LYS   A H    
3031 H HA   . LYS   B 86  ? 0.700105 0.438888 0.790123 0.0689145   0.0679407   0.149005    98  LYS   A HA   
3032 H HB2  . LYS   B 86  ? 0.800836 0.521899 0.852219 0.0516703   0.0833883   0.173183    98  LYS   A HB2  
3033 H HB3  . LYS   B 86  ? 0.821012 0.53261  0.889879 0.067937    0.0775584   0.188608    98  LYS   A HB3  
3034 H HG2  . LYS   B 86  ? 0.83885  0.600815 0.843807 0.0599598   0.0530418   0.177229    98  LYS   A HG2  
3035 H HG3  . LYS   B 86  ? 0.880928 0.618096 0.876029 0.0595704   0.0660956   0.201364    98  LYS   A HG3  
3036 H HD2  . LYS   B 86  ? 0.956772 0.689241 0.982285 0.0833316   0.0523281   0.231136    98  LYS   A HD2  
3037 H HD3  . LYS   B 86  ? 0.914918 0.674932 0.956216 0.0837477   0.0419797   0.205455    98  LYS   A HD3  
3038 H HE2  . LYS   B 86  ? 0.982576 0.768586 0.953742 0.0720826   0.0208444   0.210838    98  LYS   A HE2  
3039 H HE3  . LYS   B 86  ? 1.02147  0.780844 0.969492 0.0703086   0.0340942   0.231134    98  LYS   A HE3  
3040 H HZ1  . LYS   B 86  ? 1.06934  0.854014 1.07933  0.0966668   0.0104062   0.251271    98  LYS   A HZ1  
3041 H HZ2  . LYS   B 86  ? 1.10804  0.867792 1.08442  0.0927516   0.0184601   0.271017    98  LYS   A HZ2  
3042 H HZ3  . LYS   B 86  ? 1.087    0.877562 1.04158  0.0858988   -0.00093348 0.258503    98  LYS   A HZ3  
3043 N N    . LYS   B 87  ? 0.703401 0.39644  0.822758 0.0498383   0.0939135   0.133827    99  LYS   A N    
3044 C CA   . LYS   B 87  ? 0.720573 0.391981 0.858981 0.0346991   0.10578     0.121013    99  LYS   A CA   
3045 C C    . LYS   B 87  ? 0.713549 0.389743 0.842465 0.0228122   0.112577    0.133895    99  LYS   A C    
3046 O O    . LYS   B 87  ? 0.70688  0.378607 0.819244 0.0289906   0.115741    0.160076    99  LYS   A O    
3047 C CB   . LYS   B 87  ? 0.767682 0.398218 0.930013 0.0398046   0.116815    0.125463    99  LYS   A CB   
3048 C CG   . LYS   B 87  ? 0.818811 0.423433 1.00027  0.0200605   0.127189    0.109222    99  LYS   A CG   
3049 C CD   . LYS   B 87  ? 0.929829 0.486186 1.13105  0.0256832   0.13887     0.109473    99  LYS   A CD   
3050 C CE   . LYS   B 87  ? 1.01099  0.5346   1.22958  0.00272227  0.149253    0.0983894   99  LYS   A CE   
3051 N NZ   . LYS   B 87  ? 1.02389  0.565926 1.24246  -0.0164529  0.141086    0.0658238   99  LYS   A NZ   
3052 H H    . LYS   B 87  ? 0.714353 0.40014  0.840091 0.0611676   0.0929795   0.144297    99  LYS   A H    
3053 H HA   . LYS   B 87  ? 0.699939 0.381219 0.841134 0.0282729   0.10226     0.0999757   99  LYS   A HA   
3054 H HB2  . LYS   B 87  ? 0.771127 0.400876 0.93888  0.0496446   0.114261    0.117429    99  LYS   A HB2  
3055 H HB3  . LYS   B 87  ? 0.793734 0.413621 0.953618 0.0468314   0.12        0.148189    99  LYS   A HB3  
3056 H HG2  . LYS   B 87  ? 0.829773 0.435433 1.01088  0.010812    0.131665    0.120019    99  LYS   A HG2  
3057 H HG3  . LYS   B 87  ? 0.807017 0.424698 0.988084 0.011986    0.122058    0.087751    99  LYS   A HG3  
3058 H HD2  . LYS   B 87  ? 0.921648 0.476862 1.12436  0.0334017   0.136775    0.0947807   99  LYS   A HD2  
3059 H HD3  . LYS   B 87  ? 0.942154 0.488171 1.14314  0.0377624   0.142065    0.13251     99  LYS   A HD3  
3060 H HE2  . LYS   B 87  ? 1.04038  0.528574 1.2688   0.00712615  0.157284    0.0972065   99  LYS   A HE2  
3061 H HE3  . LYS   B 87  ? 1.01323  0.537692 1.23343  -0.00459938 0.153555    0.114726    99  LYS   A HE3  
3062 H HZ1  . LYS   B 87  ? 0.998443 0.545298 1.21027  -0.00893335 0.13662     0.0521741   99  LYS   A HZ1  
3063 H HZ2  . LYS   B 87  ? 0.984518 0.555285 1.19833  -0.0223237  0.13574     0.0685796   99  LYS   A HZ2  
3064 H HZ3  . LYS   B 87  ? 1.03515  0.554527 1.26506  -0.0304585  0.145874    0.0567354   99  LYS   A HZ3  
3065 N N    . GLY   B 88  ? 0.675082 0.364705 0.812687 0.0067119   0.11403     0.115733    100 GLY   A N    
3066 C CA   . GLY   B 88  ? 0.639015 0.337749 0.777388 -0.0048599  0.123866    0.125545    100 GLY   A CA   
3067 C C    . GLY   B 88  ? 0.603182 0.333977 0.715543 -0.00148255 0.118843    0.124443    100 GLY   A C    
3068 O O    . GLY   B 88  ? 0.586732 0.331599 0.704605 -0.0100843  0.127671    0.126194    100 GLY   A O    
3069 H H    . GLY   B 88  ? 0.65764  0.352387 0.80193  0.00324261  0.108918    0.0971872   100 GLY   A H    
3070 H HA2  . GLY   B 88  ? 0.645961 0.343767 0.80553  -0.0175702  0.126751    0.114408    100 GLY   A HA2  
3071 H HA3  . GLY   B 88  ? 0.671092 0.354209 0.806775 -0.00281037 0.132387    0.144809    100 GLY   A HA3  
3072 N N    . GLU   B 89  ? 0.584229 0.325502 0.670967 0.0107817   0.105902    0.121749    101 GLU   A N    
3073 C CA   . GLU   B 89  ? 0.595999 0.359024 0.652031 0.0143802   0.100629    0.120162    101 GLU   A CA   
3074 C C    . GLU   B 89  ? 0.577051 0.361478 0.64503  0.00661617  0.0981362   0.0990632   101 GLU   A C    
3075 O O    . GLU   B 89  ? 0.51895  0.306675 0.608788 0.00084788  0.0915063   0.0809166   101 GLU   A O    
3076 C CB   . GLU   B 89  ? 0.595625 0.363178 0.626882 0.0256448   0.0854838   0.121932    101 GLU   A CB   
3077 C CG   . GLU   B 89  ? 0.593158 0.374539 0.585729 0.0278421   0.079085    0.1214      101 GLU   A CG   
3078 C CD   . GLU   B 89  ? 0.625812 0.413464 0.596872 0.034779    0.0621714   0.124889    101 GLU   A CD   
3079 O OE1  . GLU   B 89  ? 0.679404 0.45967  0.652013 0.0413943   0.0578752   0.142204    101 GLU   A OE1  
3080 O OE2  . GLU   B 89  ? 0.621622 0.422679 0.57708  0.0334052   0.0523025   0.111825    101 GLU   A OE2  
3081 H H    . GLU   B 89  ? 0.594762 0.328317 0.684161 0.0169071   0.10062     0.120779    101 GLU   A H    
3082 H HA   . GLU   B 89  ? 0.609043 0.368874 0.651942 0.0143453   0.109339    0.133866    101 GLU   A HA   
3083 H HB2  . GLU   B 89  ? 0.615312 0.371309 0.643696 0.0309439   0.0858601   0.136975    101 GLU   A HB2  
3084 H HB3  . GLU   B 89  ? 0.580297 0.352096 0.624377 0.026153    0.0789987   0.108796    101 GLU   A HB3  
3085 H HG2  . GLU   B 89  ? 0.581111 0.372929 0.577455 0.0242808   0.0785087   0.107424    101 GLU   A HG2  
3086 H HG3  . GLU   B 89  ? 0.617882 0.393542 0.594258 0.027377    0.0873115   0.132801    101 GLU   A HG3  
3087 N N    . ILE   B 90  ? 0.574881 0.372012 0.626686 0.00707457  0.104785    0.102929    102 ILE   A N    
3088 C CA   . ILE   B 90  ? 0.560791 0.379595 0.613934 0.00596636  0.0999637   0.0872345   102 ILE   A CA   
3089 C C    . ILE   B 90  ? 0.559449 0.378647 0.569582 0.0152396   0.0947398   0.0879281   102 ILE   A C    
3090 O O    . ILE   B 90  ? 0.578843 0.388346 0.559335 0.0195023   0.103641    0.101553    102 ILE   A O    
3091 C CB   . ILE   B 90  ? 0.59063  0.42442  0.668802 -0.00027906 0.11429     0.0904408   102 ILE   A CB   
3092 C CG1  . ILE   B 90  ? 0.58459  0.417168 0.707131 -0.0143789  0.11769     0.0895536   102 ILE   A CG1  
3093 C CG2  . ILE   B 90  ? 0.562023 0.418882 0.642246 0.00247798  0.109057    0.0780578   102 ILE   A CG2  
3094 C CD1  . ILE   B 90  ? 0.579906 0.431377 0.734436 -0.0226053  0.132983    0.0973933   102 ILE   A CD1  
3095 H H    . ILE   B 90  ? 0.595105 0.3858   0.633742 0.00899217  0.113554    0.116433    102 ILE   A H    
3096 H HA   . ILE   B 90  ? 0.54913  0.372109 0.615019 0.00308389  0.0906952   0.0746963   102 ILE   A HA   
3097 H HB   . ILE   B 90  ? 0.599138 0.427258 0.662672 0.00306339  0.126043    0.103076    102 ILE   A HB   
3098 H HG12 . ILE   B 90  ? 0.571758 0.408934 0.7057   -0.0186257  0.106301    0.075604    102 ILE   A HG12 
3099 H HG13 . ILE   B 90  ? 0.600906 0.414661 0.720405 -0.0145837  0.12109     0.0978977   102 ILE   A HG13 
3100 H HG21 . ILE   B 90  ? 0.565814 0.435474 0.666222 -6.319e-05  0.118569    0.0819507   102 ILE   A HG21 
3101 H HG22 . ILE   B 90  ? 0.549541 0.411936 0.640239 -0.001049   0.09697     0.0662053   102 ILE   A HG22 
3102 H HG23 . ILE   B 90  ? 0.566114 0.418851 0.616829 0.0103433   0.108529    0.0787054   102 ILE   A HG23 
3103 H HD11 . ILE   B 90  ? 0.5986   0.444835 0.739148 -0.0179268  0.146552    0.111075    102 ILE   A HD11 
3104 H HD12 . ILE   B 90  ? 0.589505 0.438032 0.77137  -0.0339351  0.133818    0.096838    102 ILE   A HD12 
3105 H HD13 . ILE   B 90  ? 0.567485 0.439392 0.729959 -0.0215185  0.128971    0.0900038   102 ILE   A HD13 
3106 N N    . ALA   B 91  ? 0.544564 0.372428 0.548567 0.0166684   0.0805712   0.0728639   103 ALA   A N    
3107 C CA   . ALA   B 91  ? 0.538428 0.364822 0.503753 0.0221235   0.0738572   0.0706511   103 ALA   A CA   
3108 C C    . ALA   B 91  ? 0.529651 0.368491 0.497142 0.0226074   0.0709721   0.057078    103 ALA   A C    
3109 O O    . ALA   B 91  ? 0.502986 0.354872 0.500225 0.0183883   0.0665788   0.0474491   103 ALA   A O    
3110 C CB   . ALA   B 91  ? 0.572943 0.397245 0.529179 0.0232525   0.0586528   0.0687404   103 ALA   A CB   
3111 H H    . ALA   B 91  ? 0.528553 0.361841 0.551554 0.0131178   0.0751087   0.063464    103 ALA   A H    
3112 H HA   . ALA   B 91  ? 0.567678 0.385942 0.511498 0.0245891   0.0813611   0.0798792   103 ALA   A HA   
3113 H HB1  . ALA   B 91  ? 0.572959 0.390272 0.529922 0.0246248   0.0595892   0.0791056   103 ALA   A HB1  
3114 H HB2  . ALA   B 91  ? 0.545    0.375771 0.519661 0.0213516   0.0537584   0.059196    103 ALA   A HB2  
3115 H HB3  . ALA   B 91  ? 0.563368 0.386887 0.494945 0.0244173   0.0531453   0.0672626   103 ALA   A HB3  
3116 N N    . HIS   B 92  ? 0.544122 0.375799 0.476363 0.027375    0.0719513   0.0563643   104 HIS   A N    
3117 C CA   . HIS   B 92  ? 0.505163 0.342676 0.433522 0.0300414   0.0681688   0.0455914   104 HIS   A CA   
3118 C C    . HIS   B 92  ? 0.541129 0.370566 0.44068  0.0280826   0.0535287   0.0392813   104 HIS   A C    
3119 O O    . HIS   B 92  ? 0.535155 0.351157 0.403577 0.0268604   0.0507948   0.0446736   104 HIS   A O    
3120 C CB   . HIS   B 92  ? 0.53145  0.361609 0.442725 0.0378987   0.0843525   0.0490856   104 HIS   A CB   
3121 C CG   . HIS   B 92  ? 0.516899 0.362991 0.464647 0.0401607   0.0999707   0.0554381   104 HIS   A CG   
3122 N ND1  . HIS   B 92  ? 0.524904 0.369257 0.467151 0.0496365   0.119316    0.0599853   104 HIS   A ND1  
3123 C CD2  . HIS   B 92  ? 0.50095  0.365181 0.492736 0.0333891   0.10016     0.0580531   104 HIS   A CD2  
3124 C CE1  . HIS   B 92  ? 0.516026 0.382669 0.503016 0.0484718   0.130936    0.0672897   104 HIS   A CE1  
3125 N NE2  . HIS   B 92  ? 0.505534 0.384259 0.52298  0.0371323   0.117729    0.0653922   104 HIS   A NE2  
3126 H H    . HIS   B 92  ? 0.55518  0.37572  0.463212 0.0288471   0.0750156   0.0630732   104 HIS   A H    
3127 H HA   . HIS   B 92  ? 0.502016 0.352749 0.45714  0.0279075   0.0648269   0.0406015   104 HIS   A HA   
3128 H HB2  . HIS   B 92  ? 0.548604 0.363427 0.430522 0.0387123   0.08865     0.0537335   104 HIS   A HB2  
3129 H HB3  . HIS   B 92  ? 0.52545  0.354079 0.42805  0.0408786   0.0807807   0.0427875   104 HIS   A HB3  
3131 H HD2  . HIS   B 92  ? 0.490381 0.357053 0.494612 0.0270727   0.0906089   0.0548851   104 HIS   A HD2  
3132 H HE1  . HIS   B 92  ? 0.529523 0.402806 0.526541 0.0546672   0.14612     0.0722304   104 HIS   A HE1  
3134 N N    . LEU   B 93  ? 0.499995 0.338781 0.409468 0.026458    0.0437889   0.0290801   105 LEU   A N    
3135 C CA   . LEU   B 93  ? 0.547072 0.380151 0.43307  0.0231387   0.0321474   0.0237031   105 LEU   A CA   
3136 C C    . LEU   B 93  ? 0.539538 0.36657  0.411415 0.026188    0.0319215   0.0178467   105 LEU   A C    
3137 O O    . LEU   B 93  ? 0.497384 0.336739 0.391253 0.0292623   0.03218     0.0148724   105 LEU   A O    
3138 C CB   . LEU   B 93  ? 0.570822 0.417824 0.479524 0.0185246   0.022941    0.0185731   105 LEU   A CB   
3139 C CG   . LEU   B 93  ? 0.543219 0.392367 0.465395 0.0177246   0.0224211   0.0250141   105 LEU   A CG   
3140 C CD1  . LEU   B 93  ? 0.545043 0.404807 0.488628 0.0154922   0.0176318   0.0161759   105 LEU   A CD1  
3141 C CD2  . LEU   B 93  ? 0.557019 0.399589 0.453715 0.0164669   0.0165626   0.0335801   105 LEU   A CD2  
3142 H H    . LEU   B 93  ? 0.50449  0.353918 0.43569  0.0265203   0.0443234   0.0260956   105 LEU   A H    
3143 H HA   . LEU   B 93  ? 0.555763 0.379139 0.420693 0.0217116   0.0309804   0.0278816   105 LEU   A HA   
3144 H HB2  . LEU   B 93  ? 0.544194 0.399174 0.471055 0.0186842   0.0238513   0.0142192   105 LEU   A HB2  
3145 H HB3  . LEU   B 93  ? 0.552728 0.399222 0.449703 0.0159839   0.0165447   0.014981    105 LEU   A HB3  
3146 H HG   . LEU   B 93  ? 0.554141 0.401737 0.487885 0.0193004   0.0293833   0.0292928   105 LEU   A HG   
3147 H HD11 . LEU   B 93  ? 0.535054 0.397826 0.491275 0.0145973   0.0196936   0.0104591   105 LEU   A HD11 
3148 H HD12 . LEU   B 93  ? 0.541673 0.401726 0.496128 0.016745    0.0182518   0.0200864   105 LEU   A HD12 
3149 H HD13 . LEU   B 93  ? 0.537572 0.400078 0.470677 0.0135857   0.0124351   0.0125997   105 LEU   A HD13 
3150 H HD21 . LEU   B 93  ? 0.571867 0.404531 0.450937 0.0176257   0.0210195   0.0381625   105 LEU   A HD21 
3151 H HD22 . LEU   B 93  ? 0.556163 0.40009  0.44177  0.0132194   0.0101013   0.0295387   105 LEU   A HD22 
3152 H HD23 . LEU   B 93  ? 0.556958 0.403642 0.465717 0.0173522   0.0147226   0.0390122   105 LEU   A HD23 
3153 N N    . LEU   B 94  ? 0.519476 0.326612 0.354337 0.0241954   0.0295821   0.0167596   106 LEU   A N    
3154 C CA   . LEU   B 94  ? 0.539855 0.333647 0.356608 0.025912    0.0283653   0.0117513   106 LEU   A CA   
3155 C C    . LEU   B 94  ? 0.542249 0.337059 0.349882 0.0153197   0.0148555   0.0079813   106 LEU   A C    
3156 O O    . LEU   B 94  ? 0.53601  0.326525 0.32758  0.00638864  0.00796749  0.00923454  106 LEU   A O    
3157 C CB   . LEU   B 94  ? 0.60403  0.367228 0.382955 0.0302526   0.0387736   0.0117759   106 LEU   A CB   
3158 C CG   . LEU   B 94  ? 0.651243 0.391852 0.410105 0.0346739   0.0410849   0.00740626  106 LEU   A CG   
3159 C CD1  . LEU   B 94  ? 0.618056 0.373208 0.40789  0.0477076   0.0464226   0.0100539   106 LEU   A CD1  
3160 C CD2  . LEU   B 94  ? 0.717664 0.420071 0.432934 0.0383785   0.0536082   0.00468328  106 LEU   A CD2  
3161 H H    . LEU   B 94  ? 0.542903 0.342999 0.362294 0.0209778   0.0281882   0.0196752   106 LEU   A H    
3162 H HA   . LEU   B 94  ? 0.534434 0.338144 0.370234 0.0310911   0.030273    0.0112334   106 LEU   A HA   
3163 H HB2  . LEU   B 94  ? 0.607202 0.372287 0.393935 0.0372993   0.0496487   0.0151047   106 LEU   A HB2  
3164 H HB3  . LEU   B 94  ? 0.617176 0.370719 0.37442  0.0232062   0.0344696   0.0119095   106 LEU   A HB3  
3165 H HG   . LEU   B 94  ? 0.643383 0.382048 0.39489  0.0263387   0.0309196   0.00492247  106 LEU   A HG   
3166 H HD11 . LEU   B 94  ? 0.599458 0.375549 0.411393 0.0441526   0.0376687   0.0102168   106 LEU   A HD11 
3167 H HD12 . LEU   B 94  ? 0.641418 0.379282 0.416779 0.0517542   0.048167    0.00897984  106 LEU   A HD12 
3168 H HD13 . LEU   B 94  ? 0.625189 0.386023 0.427285 0.0553625   0.0568173   0.0132814   106 LEU   A HD13 
3169 H HD21 . LEU   B 94  ? 0.724628 0.417864 0.417253 0.0288358   0.0482105   0.00326189  106 LEU   A HD21 
3170 H HD22 . LEU   B 94  ? 0.71679  0.421114 0.439307 0.0477392   0.0662084   0.00752218  106 LEU   A HD22 
3171 H HD23 . LEU   B 94  ? 0.727702 0.411832 0.429511 0.0407623   0.0549201   0.00171849  106 LEU   A HD23 
3172 N N    . ILE   B 95  ? 0.556548 0.360184 0.376267 0.0157959   0.0107411   0.0048058   107 ILE   A N    
3173 C CA   . ILE   B 95  ? 0.546989 0.35957  0.367656 0.00616464  0.00132622  0.00222443  107 ILE   A CA   
3174 C C    . ILE   B 95  ? 0.601857 0.3979   0.401053 0.0039144   -0.00082618 0.00122798  107 ILE   A C    
3175 O O    . ILE   B 95  ? 0.582425 0.379537 0.387268 0.0113899   0.00034844  0.00180497  107 ILE   A O    
3176 C CB   . ILE   B 95  ? 0.531085 0.367797 0.38223  0.00735448  -0.00026351 -0.00074293 107 ILE   A CB   
3177 C CG1  . ILE   B 95  ? 0.546485 0.393433 0.419737 0.00958223  0.00340173  0.00109014  107 ILE   A CG1  
3178 C CG2  . ILE   B 95  ? 0.532092 0.377702 0.382612 -0.00056067 -0.00543747 -0.00390701 107 ILE   A CG2  
3179 C CD1  . ILE   B 95  ? 0.556379 0.41908  0.457077 0.0101019   0.00338774  -0.00419294 107 ILE   A CD1  
3180 H H    . ILE   B 95  ? 0.548664 0.353772 0.376093 0.0223238   0.0141668   0.00508195  107 ILE   A H    
3181 H HA   . ILE   B 95  ? 0.557361 0.370142 0.372686 0.00023254  -0.00183804 0.00352606  107 ILE   A HA   
3182 H HB   . ILE   B 95  ? 0.534358 0.372581 0.390451 0.0120672   0.00068056  -0.00139257 107 ILE   A HB   
3183 H HG12 . ILE   B 95  ? 0.546248 0.394484 0.417607 0.00604191  0.00125803  0.00315241  107 ILE   A HG12 
3184 H HG13 . ILE   B 95  ? 0.551946 0.392157 0.422238 0.0137945   0.00833519  0.00430305  107 ILE   A HG13 
3185 H HG21 . ILE   B 95  ? 0.520758 0.37847  0.386957 0.00011195  -0.00507565 -0.00733276 107 ILE   A HG21 
3186 H HG22 . ILE   B 95  ? 0.532675 0.378649 0.379756 -0.0054782  -0.00708043 -0.00194406 107 ILE   A HG22 
3187 H HG23 . ILE   B 95  ? 0.539232 0.377792 0.376946 -0.00154639 -0.00687721 -0.00398645 107 ILE   A HG23 
3188 H HD11 . ILE   B 95  ? 0.547973 0.412762 0.450862 0.0121272   0.00259037  -0.00579019 107 ILE   A HD11 
3189 H HD12 . ILE   B 95  ? 0.545483 0.41019  0.459534 0.0115146   0.00692685  -0.00217552 107 ILE   A HD12 
3190 H HD13 . ILE   B 95  ? 0.543544 0.41148  0.445849 0.00661989  0.00085355  -0.00783969 107 ILE   A HD13 
3191 N N    . LYS   B 96  ? 0.588558 0.370777 0.365226 -0.00748833 -0.00534405 0.0011582   108 LYS   A N    
3192 C CA   . LYS   B 96  ? 0.586951 0.351479 0.344088 -0.0129642  -0.00716545 0.00136491  108 LYS   A CA   
3193 C C    . LYS   B 96  ? 0.572198 0.359063 0.345087 -0.0175396  -0.0106156  0.00177494  108 LYS   A C    
3194 O O    . LYS   B 96  ? 0.55683  0.36966  0.352009 -0.0197411  -0.0118324  0.00020115  108 LYS   A O    
3195 C CB   . LYS   B 96  ? 0.630195 0.373926 0.360479 -0.0280715  -0.0117435  0.00068664  108 LYS   A CB   
3196 C CG   . LYS   B 96  ? 0.714422 0.427848 0.415832 -0.0261674  -0.00788614 -0.00201025 108 LYS   A CG   
3197 C CD   . LYS   B 96  ? 0.807592 0.482538 0.484001 -0.0163249  0.00199944  -0.0038122  108 LYS   A CD   
3198 C CE   . LYS   B 96  ? 0.821636 0.465537 0.467546 -0.0121357  0.0103698   -0.00832319 108 LYS   A CE   
3199 N NZ   . LYS   B 96  ? 0.80218  0.465586 0.468406 0.00265476  0.018952    -0.00592535 108 LYS   A NZ   
3200 H H    . LYS   B 96  ? 0.592992 0.376933 0.366915 -0.0127389  -0.00789437 0.00183453  108 LYS   A H    
3201 H HA   . LYS   B 96  ? 0.605733 0.356064 0.355705 -0.00439064 -0.0027912  0.0021341   108 LYS   A HA   
3202 H HB2  . LYS   B 96  ? 0.625904 0.38837  0.368062 -0.0355375  -0.0168926  0.00161687  108 LYS   A HB2  
3203 H HB3  . LYS   B 96  ? 0.651675 0.382878 0.370533 -0.0334689  -0.0125099  0.0013352   108 LYS   A HB3  
3204 H HG2  . LYS   B 96  ? 0.701495 0.426113 0.413693 -0.0190139  -0.00504046 -0.00132125 108 LYS   A HG2  
3205 H HG3  . LYS   B 96  ? 0.728643 0.435647 0.415872 -0.0387635  -0.0142127  -0.00294574 108 LYS   A HG3  
3206 H HD2  . LYS   B 96  ? 0.805896 0.46475  0.468437 -0.0244356  -0.00065149 -0.0040059  108 LYS   A HD2  
3207 H HD3  . LYS   B 96  ? 0.773637 0.459183 0.467615 -0.00424536 0.00630219  -0.00123967 108 LYS   A HD3  
3208 H HE2  . LYS   B 96  ? 0.840682 0.478041 0.469325 -0.025065   0.00378125  -0.010819   108 LYS   A HE2  
3209 H HE3  . LYS   B 96  ? 0.853769 0.468788 0.481491 -0.00682537 0.0174246   -0.0101099  108 LYS   A HE3  
3210 H HZ1  . LYS   B 96  ? 0.784159 0.46742  0.461607 -0.00255478 0.0132493   -0.00441765 108 LYS   A HZ1  
3211 H HZ2  . LYS   B 96  ? 0.784704 0.461208 0.472596 0.0123249   0.0222185   -0.00309167 108 LYS   A HZ2  
3212 H HZ3  . LYS   B 96  ? 0.827012 0.469369 0.473203 0.00732994  0.0272592   -0.00826338 108 LYS   A HZ3  
3213 N N    . PRO   B 97  ? 0.618264 0.392388 0.376595 -0.0191513  -0.0107888  0.0044492   109 PRO   A N    
3214 C CA   . PRO   B 97  ? 0.589433 0.382085 0.355528 -0.0218672  -0.0119496  0.00513673  109 PRO   A CA   
3215 C C    . PRO   B 97  ? 0.577465 0.390885 0.354805 -0.0343414  -0.0115302  0.00385776  109 PRO   A C    
3216 O O    . PRO   B 97  ? 0.536349 0.369817 0.325113 -0.0335533  -0.00898641 0.00120846  109 PRO   A O    
3217 C CB   . PRO   B 97  ? 0.591803 0.359648 0.333583 -0.0212415  -0.0119081  0.0116244   109 PRO   A CB   
3218 C CG   . PRO   B 97  ? 0.632168 0.365596 0.353081 -0.0239539  -0.00994589 0.0124005   109 PRO   A CG   
3219 C CD   . PRO   B 97  ? 0.611495 0.348791 0.342168 -0.0168404  -0.00826475 0.00748867  109 PRO   A CD   
3220 H HA   . PRO   B 97  ? 0.574739 0.380554 0.353832 -0.0144375  -0.0122529  0.0030751   109 PRO   A HA   
3221 H HB2  . PRO   B 97  ? 0.606555 0.377755 0.342954 -0.0293906  -0.0117229  0.0136661   109 PRO   A HB2  
3222 H HB3  . PRO   B 97  ? 0.600692 0.370111 0.345094 -0.0112373  -0.0129565  0.0134577   109 PRO   A HB3  
3223 H HG2  . PRO   B 97  ? 0.635815 0.364415 0.349177 -0.0369154  -0.0110516  0.0124238   109 PRO   A HG2  
3224 H HG3  . PRO   B 97  ? 0.646935 0.359761 0.354854 -0.0176581  -0.00822007 0.0163836   109 PRO   A HG3  
3225 H HD2  . PRO   B 97  ? 0.637587 0.358682 0.354246 -0.0233809  -0.00815783 0.00572639  109 PRO   A HD2  
3226 H HD3  . PRO   B 97  ? 0.624061 0.356781 0.357456 -0.0046042  -0.00523825 0.00856525  109 PRO   A HD3  
3227 N N    . GLU   B 98  ? 0.614692 0.42499  0.389953 -0.0457094  -0.0138472  0.00554621  110 GLU   A N    
3228 C CA   . GLU   B 98  ? 0.62504  0.460988 0.418553 -0.0569317  -0.0133286  0.00729202  110 GLU   A CA   
3229 C C    . GLU   B 98  ? 0.590527 0.455407 0.415139 -0.0483948  -0.0109557  0.00405662  110 GLU   A C    
3230 O O    . GLU   B 98  ? 0.572551 0.461861 0.417807 -0.051745   -0.00632919 0.00498479  110 GLU   A O    
3231 C CB   . GLU   B 98  ? 0.6361   0.46715  0.424618 -0.0729937  -0.0202998  0.0111758   110 GLU   A CB   
3232 C CG   . GLU   B 98  ? 0.743842 0.541654 0.501594 -0.0854191  -0.0213554  0.0136858   110 GLU   A CG   
3233 C CD   . GLU   B 98  ? 0.788936 0.543331 0.514182 -0.0780171  -0.021038   0.0110425   110 GLU   A CD   
3234 O OE1  . GLU   B 98  ? 0.716581 0.464632 0.439805 -0.0649537  -0.020709   0.00710361  110 GLU   A OE1  
3235 O OE2  . GLU   B 98  ? 0.797031 0.522206 0.499228 -0.0857051  -0.0192047  0.0140991   110 GLU   A OE2  
3236 H H    . GLU   B 98  ? 0.623325 0.416387 0.38632  -0.0466057  -0.0158012  0.00577651  110 GLU   A H    
3237 H HA   . GLU   B 98  ? 0.62457  0.462852 0.414276 -0.0602749  -0.00948481 0.0087404   110 GLU   A HA   
3238 H HB2  . GLU   B 98  ? 0.65243  0.478472 0.438798 -0.0700163  -0.0244272  0.00990126  110 GLU   A HB2  
3239 H HB3  . GLU   B 98  ? 0.644303 0.498882 0.452284 -0.0789885  -0.0201612  0.0137513   110 GLU   A HB3  
3240 H HG2  . GLU   B 98  ? 0.740025 0.540597 0.498972 -0.0992407  -0.026401   0.015755    110 GLU   A HG2  
3241 H HG3  . GLU   B 98  ? 0.732585 0.533653 0.490243 -0.0867685  -0.0163967  0.016149    110 GLU   A HG3  
3242 N N    . TYR   B 99  ? 0.551456 0.411985 0.380504 -0.0369375  -0.012006   0.0010125   111 TYR   A N    
3243 C CA   . TYR   B 99  ? 0.55585  0.435426 0.412109 -0.0286475  -0.00913727 -0.00148959 111 TYR   A CA   
3244 C C    . TYR   B 99  ? 0.540912 0.420065 0.400925 -0.0195389  -0.00498091 -0.00877689 111 TYR   A C    
3245 O O    . TYR   B 99  ? 0.498249 0.38566  0.378259 -0.0132673  -0.00206496 -0.012256   111 TYR   A O    
3246 C CB   . TYR   B 99  ? 0.537672 0.41247  0.395828 -0.0262217  -0.0139394  0.00276955  111 TYR   A CB   
3247 C CG   . TYR   B 99  ? 0.504388 0.386797 0.362226 -0.0377152  -0.0216291  0.00973495  111 TYR   A CG   
3248 C CD1  . TYR   B 99  ? 0.509542 0.370873 0.337979 -0.0489836  -0.0280291  0.010938    111 TYR   A CD1  
3249 C CD2  . TYR   B 99  ? 0.507145 0.417525 0.395298 -0.0377079  -0.0229877  0.0153382   111 TYR   A CD2  
3250 C CE1  . TYR   B 99  ? 0.547646 0.417136 0.375357 -0.0637911  -0.038151   0.0165472   111 TYR   A CE1  
3251 C CE2  . TYR   B 99  ? 0.509817 0.434242 0.403033 -0.0497638  -0.0331426  0.023619    111 TYR   A CE2  
3252 C CZ   . TYR   B 99  ? 0.573043 0.477501 0.434945 -0.0646858  -0.0421282  0.0237303   111 TYR   A CZ   
3253 O OH   . TYR   B 99  ? 0.563886 0.481603 0.428613 -0.0811082  -0.0553058  0.0309593   111 TYR   A OH   
3254 H H    . TYR   B 99  ? 0.571188 0.414853 0.386149 -0.0341996  -0.0135187  0.00103057  111 TYR   A H    
3255 H HA   . TYR   B 99  ? 0.542256 0.437944 0.412875 -0.0315577  -0.00674906 -0.00043965 111 TYR   A HA   
3256 H HB2  . TYR   B 99  ? 0.539315 0.397161 0.381154 -0.0240853  -0.0144784  0.00213086  111 TYR   A HB2  
3257 H HB3  . TYR   B 99  ? 0.520705 0.404186 0.396009 -0.0197522  -0.0114249  0.00217741  111 TYR   A HB3  
3258 H HD1  . TYR   B 99  ? 0.53018  0.371054 0.339483 -0.0470637  -0.0256777  0.00786513  111 TYR   A HD1  
3259 H HD2  . TYR   B 99  ? 0.491553 0.411883 0.398344 -0.0295308  -0.0171288  0.0137469   111 TYR   A HD2  
3260 H HE1  . TYR   B 99  ? 0.570893 0.422243 0.375937 -0.0732338  -0.0426913  0.0158089   111 TYR   A HE1  
3261 H HE2  . TYR   B 99  ? 0.512949 0.459733 0.431061 -0.04821    -0.034316   0.0291883   111 TYR   A HE2  
3263 N N    . ALA   B 100 ? 0.535218 0.404451 0.376122 -0.0200191  -0.00583353 -0.0101841  112 ALA   A N    
3264 C CA   . ALA   B 100 ? 0.499156 0.370368 0.341117 -0.0141462  -0.00644279 -0.0161018  112 ALA   A CA   
3265 C C    . ALA   B 100 ? 0.510637 0.382989 0.334406 -0.0186816  -0.00540732 -0.017898   112 ALA   A C    
3266 O O    . ALA   B 100 ? 0.554331 0.437446 0.38291  -0.021815   0.00155006  -0.0229766  112 ALA   A O    
3267 C CB   . ALA   B 100 ? 0.545052 0.405362 0.383499 -0.00717003 -0.0108556  -0.0127046  112 ALA   A CB   
3268 H H    . ALA   B 100 ? 0.541744 0.402624 0.368309 -0.0248361  -0.0070558  -0.00663691 112 ALA   A H    
3269 H HA   . ALA   B 100 ? 0.504758 0.384415 0.362579 -0.0119945  -0.00394702 -0.0208621  112 ALA   A HA   
3270 H HB1  . ALA   B 100 ? 0.522995 0.384268 0.373184 -0.00423648 -0.00947539 -0.0124896  112 ALA   A HB1  
3271 H HB2  . ALA   B 100 ? 0.541868 0.38986  0.365484 -0.00791707 -0.0117675  -0.00789895 112 ALA   A HB2  
3272 H HB3  . ALA   B 100 ? 0.533123 0.397538 0.372624 -0.00479162 -0.0136333  -0.0149996  112 ALA   A HB3  
3273 N N    . TYR   B 101 ? 0.523127 0.383573 0.325207 -0.0179834  -0.0106816  -0.012531   113 TYR   A N    
3274 C CA   . TYR   B 101 ? 0.560122 0.420677 0.339861 -0.0218968  -0.0107601  -0.0123501  113 TYR   A CA   
3275 C C    . TYR   B 101 ? 0.54193  0.387841 0.299547 -0.028566   -0.00835695 -0.00188471 113 TYR   A C    
3276 O O    . TYR   B 101 ? 0.504612 0.347108 0.239365 -0.0323212  -0.00728101 0.00184838  113 TYR   A O    
3277 C CB   . TYR   B 101 ? 0.575174 0.436627 0.34812  -0.015914   -0.0213625  -0.0123791  113 TYR   A CB   
3278 C CG   . TYR   B 101 ? 0.550335 0.425721 0.343917 -0.0144703  -0.0235697  -0.0242645  113 TYR   A CG   
3279 C CD1  . TYR   B 101 ? 0.566901 0.448351 0.354446 -0.0199534  -0.0189966  -0.0366135  113 TYR   A CD1  
3280 C CD2  . TYR   B 101 ? 0.533348 0.412435 0.352097 -0.00845642 -0.0269727  -0.0237453  113 TYR   A CD2  
3281 C CE1  . TYR   B 101 ? 0.574064 0.46114  0.379261 -0.0203189  -0.019854   -0.0487416  113 TYR   A CE1  
3282 C CE2  . TYR   B 101 ? 0.552475 0.441352 0.392055 -0.00964446 -0.0278332  -0.0337447  113 TYR   A CE2  
3283 C CZ   . TYR   B 101 ? 0.543964 0.435018 0.376374 -0.0161122  -0.0253162  -0.0466505  113 TYR   A CZ   
3284 O OH   . TYR   B 101 ? 0.591983 0.486189 0.443348 -0.0186823  -0.0260249  -0.0572952  113 TYR   A OH   
3285 H H    . TYR   B 101 ? 0.529094 0.380269 0.329119 -0.0142644  -0.0137166  -0.00820027 113 TYR   A H    
3286 H HA   . TYR   B 101 ? 0.550276 0.420356 0.333681 -0.0248035  -0.00511383 -0.0188298  113 TYR   A HA   
3287 H HB2  . TYR   B 101 ? 0.571128 0.425247 0.345935 -0.0105867  -0.0253794  -0.00574528 113 TYR   A HB2  
3288 H HB3  . TYR   B 101 ? 0.589093 0.448887 0.342202 -0.0187974  -0.0227807  -0.010574   113 TYR   A HB3  
3289 H HD1  . TYR   B 101 ? 0.582852 0.462338 0.352813 -0.0237218  -0.0140786  -0.0369228  113 TYR   A HD1  
3290 H HD2  . TYR   B 101 ? 0.536841 0.410013 0.357921 -0.0038538  -0.0275322  -0.0165034  113 TYR   A HD2  
3291 H HE1  . TYR   B 101 ? 0.581354 0.467922 0.37895  -0.0238563  -0.0158569  -0.0584386  113 TYR   A HE1  
3292 H HE2  . TYR   B 101 ? 0.531126 0.423154 0.388361 -0.00635391 -0.029243   -0.0319632  113 TYR   A HE2  
3294 N N    . GLY   B 102 ? 0.567456 0.402022 0.328916 -0.0316197  -0.00764433 0.00297815  114 GLY   A N    
3295 C CA   . GLY   B 102 ? 0.583401 0.403715 0.32788  -0.0429171  -0.00433543 0.0111698   114 GLY   A CA   
3296 C C    . GLY   B 102 ? 0.609457 0.405541 0.325297 -0.0406661  -0.0072592  0.020871    114 GLY   A C    
3297 O O    . GLY   B 102 ? 0.617253 0.407234 0.32926  -0.0282817  -0.0137777  0.0229629   114 GLY   A O    
3298 H H    . GLY   B 102 ? 0.547334 0.381695 0.320356 -0.0278586  -0.00932263 0.00111978  114 GLY   A H    
3299 H HA2  . GLY   B 102 ? 0.581225 0.394327 0.329862 -0.046237   -0.00540666 0.0120226   114 GLY   A HA2  
3300 H HA3  . GLY   B 102 ? 0.583651 0.416957 0.331664 -0.0495054  0.00140962  0.0102587   114 GLY   A HA3  
3301 N N    . SER   B 103 ? 0.609485 0.392995 0.30837  -0.0530032  -0.00224995 0.0287938   115 SER   A N    
3302 C CA   . SER   B 103 ? 0.685489 0.439949 0.355699 -0.0514723  -0.00393923 0.0409969   115 SER   A CA   
3303 C C    . SER   B 103 ? 0.667149 0.431909 0.320254 -0.0465486  -0.00558881 0.0451423   115 SER   A C    
3304 O O    . SER   B 103 ? 0.659519 0.405298 0.292008 -0.0391908  -0.0112209  0.0565961   115 SER   A O    
3305 C CB   . SER   B 103 ? 0.735139 0.467695 0.392946 -0.06886    0.00198457  0.0485497   115 SER   A CB   
3306 O OG   . SER   B 103 ? 0.81677  0.567427 0.472247 -0.0817309  0.0110008   0.0519648   115 SER   A OG   
3307 H H    . SER   B 103 ? 0.620402 0.413805 0.327213 -0.0624832  0.00250699  0.0277343   115 SER   A H    
3308 H HA   . SER   B 103 ? 0.677056 0.417632 0.346965 -0.0418249  -0.00853871 0.0419597   115 SER   A HA   
3309 H HB2  . SER   B 103 ? 0.771624 0.476892 0.411311 -0.0663457  0.00071222  0.0563978   115 SER   A HB2  
3310 H HB3  . SER   B 103 ? 0.735248 0.467688 0.404666 -0.0741319  0.00131379  0.0436767   115 SER   A HB3  
3312 N N    . ALA   B 104 ? 0.64334  0.436105 0.302678 -0.0489052  -0.00167163 0.0358746   116 ALA   A N    
3313 C CA   . ALA   B 104 ? 0.69554  0.494176 0.330521 -0.0454071  -0.005346   0.037583    116 ALA   A CA   
3314 C C    . ALA   B 104 ? 0.674744 0.481471 0.318828 -0.0317395  -0.0205291  0.0333067   116 ALA   A C    
3315 O O    . ALA   B 104 ? 0.664755 0.472628 0.288043 -0.0275153  -0.0307208  0.0388173   116 ALA   A O    
3316 C CB   . ALA   B 104 ? 0.695443 0.51501  0.326552 -0.053179   0.00695233  0.0272707   116 ALA   A CB   
3317 H H    . ALA   B 104 ? 0.633907 0.440733 0.310715 -0.0526051  0.00320838  0.0285259   116 ALA   A H    
3318 H HA   . ALA   B 104 ? 0.714625 0.49674  0.327421 -0.0471137  -0.00582284 0.0495805   116 ALA   A HA   
3319 H HB1  . ALA   B 104 ? 0.705706 0.52326  0.332986 -0.061832   0.0172679   0.0321412   116 ALA   A HB1  
3320 H HB2  . ALA   B 104 ? 0.671617 0.504775 0.325217 -0.0510335  0.0084928   0.0164089   116 ALA   A HB2  
3321 H HB3  . ALA   B 104 ? 0.715424 0.535998 0.325084 -0.0515586  0.00355316  0.0270361   116 ALA   A HB3  
3322 N N    . GLY   B 105 ? 0.636243 0.451362 0.312339 -0.0259294  -0.0227444  0.0244319   117 GLY   A N    
3323 C CA   . GLY   B 105 ? 0.622128 0.450733 0.313976 -0.0157898  -0.0349499  0.0198531   117 GLY   A CA   
3324 C C    . GLY   B 105 ? 0.590958 0.438714 0.277514 -0.020661   -0.0375984  0.00692331  117 GLY   A C    
3325 O O    . GLY   B 105 ? 0.558524 0.409315 0.235512 -0.0289587  -0.0259515  -0.00104828 117 GLY   A O    
3326 H H    . GLY   B 105 ? 0.623155 0.436577 0.31174  -0.0291152  -0.016892   0.0218963   117 GLY   A H    
3327 H HA2  . GLY   B 105 ? 0.592969 0.424057 0.306885 -0.012413   -0.0335502  0.0156695   117 GLY   A HA2  
3328 H HA3  . GLY   B 105 ? 0.629492 0.45133  0.313537 -0.00930202 -0.0427682  0.0297763   117 GLY   A HA3  
3329 N N    . SER   B 106 ? 0.589082 0.449336 0.283524 -0.0157987  -0.0521847  0.00453306  118 SER   A N    
3330 C CA   . SER   B 106 ? 0.675759 0.549045 0.360399 -0.0226919  -0.0576679  -0.00966808 118 SER   A CA   
3331 C C    . SER   B 106 ? 0.675533 0.559904 0.355889 -0.0191789  -0.0801352  -0.00207342 118 SER   A C    
3332 O O    . SER   B 106 ? 0.664501 0.564695 0.374593 -0.0170575  -0.0904541  -0.00638883 118 SER   A O    
3333 C CB   . SER   B 106 ? 0.643787 0.525807 0.358683 -0.0249449  -0.0509911  -0.0272278  118 SER   A CB   
3334 O OG   . SER   B 106 ? 0.68295  0.567562 0.379673 -0.0335253  -0.0511734  -0.0436759  118 SER   A OG   
3335 H H    . SER   B 106 ? 0.601034 0.461451 0.307737 -0.00846017 -0.0588819  0.0116989   118 SER   A H    
3336 H HA   . SER   B 106 ? 0.675434 0.543397 0.333966 -0.0285293  -0.0512705  -0.011576   118 SER   A HA   
3337 H HB2  . SER   B 106 ? 0.634231 0.511835 0.357965 -0.0247659  -0.0388715  -0.028157   118 SER   A HB2  
3338 H HB3  . SER   B 106 ? 0.633204 0.522091 0.371198 -0.0206496  -0.0580698  -0.0257148  118 SER   A HB3  
3340 N N    . LEU   B 107 ? 0.719866 0.597066 0.366959 -0.0179526  -0.0879325  0.0127979   119 LEU   A N    
3341 C CA   . LEU   B 107 ? 0.77913  0.670021 0.424711 -0.0125611  -0.111861   0.0251996   119 LEU   A CA   
3342 C C    . LEU   B 107 ? 0.848396 0.755296 0.478356 -0.0250077  -0.126321   0.00962125  119 LEU   A C    
3343 O O    . LEU   B 107 ? 0.864436 0.761432 0.461151 -0.0362731  -0.116053   -0.00540674 119 LEU   A O    
3344 C CB   . LEU   B 107 ? 0.821724 0.697829 0.432287 -0.00722963 -0.117101   0.047971    119 LEU   A CB   
3345 C CG   . LEU   B 107 ? 0.805644 0.658434 0.425664 0.00422189  -0.105164   0.0646423   119 LEU   A CG   
3346 C CD1  . LEU   B 107 ? 0.849163 0.687238 0.430981 0.00812963  -0.113618   0.087505    119 LEU   A CD1  
3347 C CD2  . LEU   B 107 ? 0.767907 0.626507 0.434769 0.0194118   -0.107123   0.0699173   119 LEU   A CD2  
3348 H H    . LEU   B 107 ? 0.738474 0.603129 0.364627 -0.0205466  -0.0786073  0.0167135   119 LEU   A H    
3349 H HA   . LEU   B 107 ? 0.757879 0.657063 0.436472 -0.0044908  -0.115425   0.0292606   119 LEU   A HA   
3350 H HB2  . LEU   B 107 ? 0.841256 0.709001 0.41831  -0.0158368  -0.111329   0.044248    119 LEU   A HB2  
3351 H HB3  . LEU   B 107 ? 0.835467 0.724287 0.445326 -0.00365004 -0.135163   0.0565303   119 LEU   A HB3  
3352 H HG   . LEU   B 107 ? 0.794866 0.635598 0.410512 -0.00185511 -0.0892858  0.0576172   119 LEU   A HG   
3353 H HD11 . LEU   B 107 ? 0.871432 0.70418  0.421236 -0.00198266 -0.109169   0.084202    119 LEU   A HD11 
3354 H HD12 . LEU   B 107 ? 0.852529 0.671049 0.437007 0.0147044   -0.105834   0.0982145   119 LEU   A HD12 
3355 H HD13 . LEU   B 107 ? 0.862713 0.715424 0.448732 0.0140838   -0.131019   0.0955884   119 LEU   A HD13 
3356 H HD21 . LEU   B 107 ? 0.742089 0.6095   0.430748 0.0162208   -0.101643   0.0564583   119 LEU   A HD21 
3357 H HD22 . LEU   B 107 ? 0.779687 0.653248 0.455956 0.026264    -0.122134   0.0785734   119 LEU   A HD22 
3358 H HD23 . LEU   B 107 ? 0.774486 0.612511 0.439677 0.025402    -0.0982448  0.0785379   119 LEU   A HD23 
3359 N N    . PRO   B 108 ? 0.855669 0.786969 0.506608 -0.0237839  -0.150603   0.013764    120 PRO   A N    
3360 C CA   . PRO   B 108 ? 0.800248 0.744922 0.488294 -0.00741385 -0.160993   0.0354605   120 PRO   A CA   
3361 C C    . PRO   B 108 ? 0.745972 0.698705 0.489918 0.00030404  -0.150034   0.0314026   120 PRO   A C    
3362 O O    . PRO   B 108 ? 0.760773 0.717638 0.532794 0.0164858   -0.150315   0.0485468   120 PRO   A O    
3363 C CB   . PRO   B 108 ? 0.84904  0.822135 0.535406 -0.0108922  -0.192632   0.0433276   120 PRO   A CB   
3364 C CG   . PRO   B 108 ? 0.882197 0.857581 0.541177 -0.0328255  -0.198732   0.017676    120 PRO   A CG   
3365 C CD   . PRO   B 108 ? 0.884695 0.831512 0.522274 -0.0388512  -0.169455   -0.00144439 120 PRO   A CD   
3366 H HA   . PRO   B 108 ? 0.819447 0.749263 0.49324  0.00045788  -0.155748   0.0490947   120 PRO   A HA   
3367 H HB2  . PRO   B 108 ? 0.829579 0.82273  0.556297 -0.00439664 -0.200298   0.0492634   120 PRO   A HB2  
3368 H HB3  . PRO   B 108 ? 0.875557 0.844227 0.537039 -0.00621369 -0.200719   0.0585562   120 PRO   A HB3  
3369 H HG2  . PRO   B 108 ? 0.868598 0.861721 0.558319 -0.0375555  -0.206898   0.0101255   120 PRO   A HG2  
3370 H HG3  . PRO   B 108 ? 0.920326 0.897854 0.544844 -0.0385024  -0.213606   0.0215185   120 PRO   A HG3  
3371 H HD2  . PRO   B 108 ? 0.86191  0.81129  0.520632 -0.0441939  -0.163754   -0.0166516  120 PRO   A HD2  
3372 H HD3  . PRO   B 108 ? 0.913432 0.849216 0.508438 -0.0466326  -0.168498   -0.00688088 120 PRO   A HD3  
3373 N N    . LYS   B 109 ? 0.702347 0.652748 0.458856 -0.00945544 -0.137361   0.0102695   121 LYS   A N    
3374 C CA   . LYS   B 109 ? 0.675745 0.636179 0.482255 -0.00441939 -0.12939    0.00705162  121 LYS   A CA   
3375 C C    . LYS   B 109 ? 0.64266  0.584184 0.459533 0.00956805  -0.110039   0.0165184   121 LYS   A C    
3376 O O    . LYS   B 109 ? 0.645182 0.595094 0.497524 0.0205442   -0.106703   0.0242084   121 LYS   A O    
3377 C CB   . LYS   B 109 ? 0.709832 0.668027 0.523072 -0.0182252  -0.12107    -0.0159958  121 LYS   A CB   
3378 C CG   . LYS   B 109 ? 0.764053 0.742665 0.585853 -0.0325307  -0.140659   -0.0268809  121 LYS   A CG   
3379 C CD   . LYS   B 109 ? 0.800203 0.764511 0.615057 -0.0467746  -0.130344   -0.0515885  121 LYS   A CD   
3380 C CE   . LYS   B 109 ? 0.773452 0.745535 0.573779 -0.0654199  -0.150136   -0.0666395  121 LYS   A CE   
3381 N NZ   . LYS   B 109 ? 0.759661 0.761309 0.609467 -0.0691067  -0.166237   -0.060462   121 LYS   A NZ   
3382 H H    . LYS   B 109 ? 0.721503 0.663017 0.454453 -0.0187683  -0.132594   -0.00156417 121 LYS   A H    
3383 H HA   . LYS   B 109 ? 0.680448 0.661761 0.510798 -0.00138353 -0.142504   0.0142896   121 LYS   A HA   
3384 H HB2  . LYS   B 109 ? 0.715396 0.657835 0.501456 -0.0227402  -0.112178   -0.0236411  121 LYS   A HB2  
3385 H HB3  . LYS   B 109 ? 0.681528 0.638585 0.520468 -0.0137587  -0.110415   -0.0164224  121 LYS   A HB3  
3386 H HG2  . LYS   B 109 ? 0.748738 0.74564  0.60573  -0.0292697  -0.146768   -0.0202639  121 LYS   A HG2  
3387 H HG3  . LYS   B 109 ? 0.789898 0.772614 0.586682 -0.036045   -0.15455    -0.0236676  121 LYS   A HG3  
3388 H HD2  . LYS   B 109 ? 0.781716 0.728217 0.570782 -0.0460184  -0.117912   -0.0563959  121 LYS   A HD2  
3389 H HD3  . LYS   B 109 ? 0.752541 0.71799  0.597821 -0.044555   -0.121518   -0.0530586  121 LYS   A HD3  
3390 H HE2  . LYS   B 109 ? 0.813694 0.787276 0.583324 -0.0676142  -0.161534   -0.0632287  121 LYS   A HE2  
3391 H HE3  . LYS   B 109 ? 0.794693 0.750771 0.584299 -0.0731669  -0.140722   -0.083226   121 LYS   A HE3  
3392 H HZ1  . LYS   B 109 ? 0.75746  0.775529 0.61755  -0.0612118  -0.175542   -0.0449851  121 LYS   A HZ1  
3393 H HZ2  . LYS   B 109 ? 0.73664  0.736547 0.614012 -0.0661417  -0.154446   -0.0613794  121 LYS   A HZ2  
3394 H HZ3  . LYS   B 109 ? 0.782998 0.788781 0.626489 -0.0827717  -0.178736   -0.0708055  121 LYS   A HZ3  
3395 N N    . ILE   B 110 ? 0.62887  0.544582 0.414574 0.00750673  -0.0960242  0.0146462   122 ILE   A N    
3396 C CA   . ILE   B 110 ? 0.621552 0.517017 0.413233 0.0141287   -0.0782125  0.0175733   122 ILE   A CA   
3397 C C    . ILE   B 110 ? 0.597593 0.468805 0.357136 0.0181728   -0.0751286  0.0312662   122 ILE   A C    
3398 O O    . ILE   B 110 ? 0.585817 0.448241 0.313196 0.00846699  -0.0727676  0.0290648   122 ILE   A O    
3399 C CB   . ILE   B 110 ? 0.615623 0.504996 0.407652 0.00409986  -0.0638683  0.0014971   122 ILE   A CB   
3400 C CG1  . ILE   B 110 ? 0.626478 0.532568 0.440994 -0.00293776 -0.0660322  -0.0134913  122 ILE   A CG1  
3401 C CG2  . ILE   B 110 ? 0.643158 0.516293 0.444047 0.00925306  -0.0500977  0.00471507  122 ILE   A CG2  
3402 C CD1  . ILE   B 110 ? 0.606481 0.523941 0.461031 0.00309731  -0.0651917  -0.0116412  122 ILE   A CD1  
3403 H H    . ILE   B 110 ? 0.653054 0.564151 0.412125 0.00064635  -0.097895   0.0113802   122 ILE   A H    
3404 H HA   . ILE   B 110 ? 0.600233 0.500708 0.416137 0.0222471   -0.0772473  0.0218954   122 ILE   A HA   
3405 H HB   . ILE   B 110 ? 0.637224 0.519848 0.405694 -0.00193327 -0.0613896  -0.00075746 122 ILE   A HB   
3406 H HG12 . ILE   B 110 ? 0.636719 0.551467 0.442696 -0.0076772  -0.0765187  -0.0164216  122 ILE   A HG12 
3407 H HG13 . ILE   B 110 ? 0.616119 0.516086 0.426034 -0.00791343 -0.0568944  -0.0219044  122 ILE   A HG13 
3408 H HG21 . ILE   B 110 ? 0.616367 0.489758 0.421823 0.00394772  -0.0432761  -0.00343462 122 ILE   A HG21 
3409 H HG22 . ILE   B 110 ? 0.621482 0.498109 0.440926 0.0166924   -0.0505399  0.0085629   122 ILE   A HG22 
3410 H HG23 . ILE   B 110 ? 0.641852 0.500103 0.424491 0.0100762   -0.0475014  0.0114204   122 ILE   A HG23 
3411 H HD11 . ILE   B 110 ? 0.592829 0.500648 0.452278 0.00626381  -0.0545083  -0.010859   122 ILE   A HD11 
3412 H HD12 . ILE   B 110 ? 0.601733 0.528487 0.468477 -0.00329042 -0.0680857  -0.0204121  122 ILE   A HD12 
3413 H HD13 . ILE   B 110 ? 0.609828 0.534667 0.472882 0.00996509  -0.0719605  -0.00195977 122 ILE   A HD13 
3414 N N    . PRO   B 111 ? 0.62083  0.476073 0.386328 0.0318403   -0.0714419  0.0450883   123 PRO   A N    
3415 C CA   . PRO   B 111 ? 0.633293 0.457931 0.367047 0.0338795   -0.0669403  0.0577386   123 PRO   A CA   
3416 C C    . PRO   B 111 ? 0.629478 0.430974 0.347867 0.0224696   -0.0512022  0.0501361   123 PRO   A C    
3417 O O    . PRO   B 111 ? 0.636087 0.444935 0.37103  0.016823    -0.0439496  0.0370654   123 PRO   A O    
3418 C CB   . PRO   B 111 ? 0.63973  0.453575 0.388506 0.0539063   -0.067547   0.073311    123 PRO   A CB   
3419 C CG   . PRO   B 111 ? 0.634903 0.467168 0.423377 0.0598312   -0.0624903  0.0643568   123 PRO   A CG   
3420 C CD   . PRO   B 111 ? 0.581545 0.443501 0.382624 0.0458607   -0.0685315  0.0490296   123 PRO   A CD   
3421 H HA   . PRO   B 111 ? 0.654362 0.482363 0.368914 0.0301788   -0.074644   0.0623126   123 PRO   A HA   
3422 H HB2  . PRO   B 111 ? 0.662174 0.44781  0.396179 0.0558998   -0.058778   0.0777636   123 PRO   A HB2  
3423 H HB3  . PRO   B 111 ? 0.663057 0.487156 0.411838 0.0602495   -0.0790462  0.0839504   123 PRO   A HB3  
3424 H HG2  . PRO   B 111 ? 0.617734 0.431251 0.403569 0.0599123   -0.0504533  0.0600729   123 PRO   A HG2  
3425 H HG3  . PRO   B 111 ? 0.626618 0.468903 0.434426 0.0724917   -0.0666882  0.0734144   123 PRO   A HG3  
3426 H HD2  . PRO   B 111 ? 0.574082 0.434471 0.385393 0.0427328   -0.0595338  0.0401408   123 PRO   A HD2  
3427 H HD3  . PRO   B 111 ? 0.59067  0.47561  0.410732 0.0488767   -0.078834   0.0513821   123 PRO   A HD3  
3428 N N    . SER   B 112 ? 0.636747 0.410438 0.325342 0.0188343   -0.046815   0.0604954   124 SER   A N    
3429 C CA   . SER   B 112 ? 0.647564 0.39909  0.324104 0.00627042  -0.0339613  0.0564869   124 SER   A CA   
3430 C C    . SER   B 112 ? 0.634557 0.369701 0.32571  0.0109837   -0.0267838  0.0513038   124 SER   A C    
3431 O O    . SER   B 112 ? 0.625427 0.347681 0.323414 0.0265069   -0.0267367  0.0571732   124 SER   A O    
3432 C CB   . SER   B 112 ? 0.709827 0.431545 0.354221 0.00193836  -0.0313737  0.0711928   124 SER   A CB   
3433 O OG   . SER   B 112 ? 0.736511 0.435981 0.371444 -0.0129492  -0.0204227  0.0687173   124 SER   A OG   
3434 H H    . SER   B 112 ? 0.666953 0.435994 0.343046 0.0235381   -0.052838   0.071342    124 SER   A H    
3435 H HA   . SER   B 112 ? 0.634995 0.401845 0.314068 -0.00356822 -0.0313625  0.0476826   124 SER   A HA   
3436 H HB2  . SER   B 112 ? 0.718752 0.451047 0.350246 -0.00237979 -0.0345703  0.0740549   124 SER   A HB2  
3437 H HB3  . SER   B 112 ? 0.726944 0.433222 0.368879 0.0135643   -0.0342583  0.0809649   124 SER   A HB3  
3439 N N    . ASN   B 113 ? 0.649643 0.386559 0.345049 -0.00198053 -0.0203117  0.0407686   125 ASN   A N    
3440 C CA   . ASN   B 113 ? 0.675003 0.393903 0.374101 -0.00208892 -0.0145219  0.0351661   125 ASN   A CA   
3441 C C    . ASN   B 113 ? 0.610982 0.338919 0.331554 0.0142584   -0.014167   0.0321089   125 ASN   A C    
3442 O O    . ASN   B 113 ? 0.67322  0.374686 0.386971 0.0222432   -0.00776336 0.0329469   125 ASN   A O    
3443 C CB   . ASN   B 113 ? 0.721865 0.394642 0.393912 -0.00506368 -0.00937863 0.0413485   125 ASN   A CB   
3444 C CG   . ASN   B 113 ? 0.763529 0.426621 0.417552 -0.0251552  -0.00803964 0.0450674   125 ASN   A CG   
3445 O OD1  . ASN   B 113 ? 0.75696  0.446466 0.422052 -0.0391105  -0.00805026 0.0393617   125 ASN   A OD1  
3446 N ND2  . ASN   B 113 ? 0.82458  0.450396 0.453545 -0.0263975  -0.00543796 0.0560116   125 ASN   A ND2  
3447 H H    . ASN   B 113 ? 0.639427 0.389994 0.334579 -0.0112477  -0.0195871  0.0371886   125 ASN   A H    
3448 H HA   . ASN   B 113 ? 0.646643 0.376596 0.351456 -0.0123801  -0.0132343  0.0287115   125 ASN   A HA   
3449 H HB2  . ASN   B 113 ? 0.743655 0.40333  0.410693 0.00687122  -0.00964233 0.0490759   125 ASN   A HB2  
3450 H HB3  . ASN   B 113 ? 0.726813 0.387309 0.397826 -0.00581082 -0.00600769 0.035668    125 ASN   A HB3  
3451 H HD21 . ASN   B 113 ? 0.831195 0.452378 0.450371 -0.0385556  -0.0039865  0.0598604   125 ASN   A HD21 
3452 H HD22 . ASN   B 113 ? 0.835833 0.440789 0.45864  -0.0148006  -0.00429221 0.0601272   125 ASN   A HD22 
3453 N N    . ALA   B 114 ? 0.593125 0.356081 0.33841  0.0178692   -0.0192018  0.0278513   126 ALA   A N    
3454 C CA   . ALA   B 114 ? 0.556321 0.332825 0.327371 0.0309124   -0.0180568  0.0264474   126 ALA   A CA   
3455 C C    . ALA   B 114 ? 0.527119 0.306955 0.307715 0.0258019   -0.0115503  0.0172203   126 ALA   A C    
3456 O O    . ALA   B 114 ? 0.55874  0.350748 0.341838 0.0138302   -0.0128639  0.0107964   126 ALA   A O    
3457 C CB   . ALA   B 114 ? 0.529673 0.339874 0.322141 0.0335503   -0.0281122  0.0264653   126 ALA   A CB   
3458 H H    . ALA   B 114 ? 0.578147 0.356173 0.32413  0.0112766   -0.0225521  0.0255435   126 ALA   A H    
3459 H HA   . ALA   B 114 ? 0.574127 0.334196 0.341543 0.0412896   -0.0146355  0.0324567   126 ALA   A HA   
3460 H HB1  . ALA   B 114 ? 0.548566 0.357354 0.333183 0.0372872   -0.0338868  0.0338603   126 ALA   A HB1  
3461 H HB2  . ALA   B 114 ? 0.521182 0.343067 0.31429  0.0240829   -0.0298438  0.0195847   126 ALA   A HB2  
3462 H HB3  . ALA   B 114 ? 0.52267  0.344056 0.335848 0.040541    -0.0271271  0.0262376   126 ALA   A HB3  
3463 N N    . THR   B 115 ? 0.560452 0.331499 0.348014 0.036728    -0.00372681 0.0180669   127 THR   A N    
3464 C CA   . THR   B 115 ? 0.561831 0.338078 0.358729 0.0348875   0.00250896  0.0123143   127 THR   A CA   
3465 C C    . THR   B 115 ? 0.555303 0.364279 0.388696 0.0406019   0.00130846  0.0123718   127 THR   A C    
3466 O O    . THR   B 115 ? 0.582958 0.402491 0.434016 0.0521548   0.00075042  0.0185665   127 THR   A O    
3467 C CB   . THR   B 115 ? 0.56372  0.307337 0.340297 0.042599    0.0144408   0.0129681   127 THR   A CB   
3468 O OG1  . THR   B 115 ? 0.577251 0.291687 0.320551 0.0309587   0.0121581   0.0108083   127 THR   A OG1  
3469 C CG2  . THR   B 115 ? 0.570668 0.314501 0.345985 0.0393316   0.0209463   0.00847494  127 THR   A CG2  
3470 H H    . THR   B 115 ? 0.571526 0.332117 0.357239 0.0467195   -0.00117507 0.0234618   127 THR   A H    
3471 H HA   . THR   B 115 ? 0.550219 0.328602 0.341599 0.0242647   -5.389e-05  0.00837455  127 THR   A HA   
3472 H HB   . THR   B 115 ? 0.579442 0.318093 0.361195 0.0550369   0.0192375   0.0176157   127 THR   A HB   
3474 H HG21 . THR   B 115 ? 0.591621 0.311445 0.347762 0.0435914   0.0291494   0.007778    127 THR   A HG21 
3475 H HG22 . THR   B 115 ? 0.560708 0.307558 0.32993  0.0279494   0.0152413   0.00554635  127 THR   A HG22 
3476 H HG23 . THR   B 115 ? 0.55029  0.314633 0.34943  0.0442241   0.0228422   0.00987623  127 THR   A HG23 
3477 N N    . LEU   B 116 ? 0.542482 0.367525 0.389146 0.0320074   0.00021058  0.0066391   128 LEU   A N    
3478 C CA   . LEU   B 116 ? 0.516136 0.367247 0.396298 0.0330986   -0.00054244 0.00532581  128 LEU   A CA   
3479 C C    . LEU   B 116 ? 0.500653 0.349158 0.389452 0.0354198   0.0104696   0.0066984   128 LEU   A C    
3480 O O    . LEU   B 116 ? 0.463392 0.296409 0.332297 0.0311535   0.0138983   0.00577484  128 LEU   A O    
3481 C CB   . LEU   B 116 ? 0.487713 0.354425 0.377023 0.0223321   -0.00790572 -0.00230358 128 LEU   A CB   
3482 C CG   . LEU   B 116 ? 0.568832 0.437414 0.442451 0.0163958   -0.0166131  -0.00562895 128 LEU   A CG   
3483 C CD1  . LEU   B 116 ? 0.55058  0.437296 0.439193 0.00999005  -0.0227349  -0.0140462  128 LEU   A CD1  
3484 C CD2  . LEU   B 116 ? 0.525922 0.38671  0.383662 0.0219842   -0.0212803  0.00153819  128 LEU   A CD2  
3485 H H    . LEU   B 116 ? 0.538243 0.357043 0.373603 0.0248638   -0.00012405 0.00398562  128 LEU   A H    
3486 H HA   . LEU   B 116 ? 0.515325 0.375425 0.407724 0.0393411   -0.00258353 0.00904194  128 LEU   A HA   
3487 H HB2  . LEU   B 116 ? 0.5025   0.364714 0.388665 0.0185126   -0.00457259 -0.00420762 128 LEU   A HB2  
3488 H HB3  . LEU   B 116 ? 0.499704 0.380272 0.410075 0.0223929   -0.00903602 -0.00348918 128 LEU   A HB3  
3489 H HG   . LEU   B 116 ? 0.540342 0.401475 0.40176  0.0115368   -0.0144172  -0.00737017 128 LEU   A HG   
3490 H HD11 . LEU   B 116 ? 0.545589 0.432735 0.441626 0.00666978  -0.0185205  -0.018545   128 LEU   A HD11 
3491 H HD12 . LEU   B 116 ? 0.561383 0.448062 0.435732 0.00645559  -0.0270642  -0.0162385  128 LEU   A HD12 
3492 H HD13 . LEU   B 116 ? 0.552252 0.449219 0.456584 0.0123894   -0.0262565  -0.012594   128 LEU   A HD13 
3493 H HD21 . LEU   B 116 ? 0.552434 0.395877 0.394128 0.0230488   -0.017037   0.00448402  128 LEU   A HD21 
3494 H HD22 . LEU   B 116 ? 0.544047 0.41204  0.415674 0.029065    -0.0225426  0.00573357  128 LEU   A HD22 
3495 H HD23 . LEU   B 116 ? 0.548667 0.413768 0.397842 0.0175015   -0.0270735  -0.00022884 128 LEU   A HD23 
3496 N N    . PHE   B 117 ? 0.534244 0.401453 0.454529 0.0400359   0.0142825   0.00977944  129 PHE   A N    
3497 C CA   . PHE   B 117 ? 0.522587 0.391565 0.456245 0.0410064   0.025904    0.0129144   129 PHE   A CA   
3498 C C    . PHE   B 117 ? 0.459969 0.350435 0.426667 0.032502    0.0213477   0.0100904   129 PHE   A C    
3499 O O    . PHE   B 117 ? 0.432707 0.342795 0.421893 0.0298406   0.0124649   0.008048    129 PHE   A O    
3500 C CB   . PHE   B 117 ? 0.524162 0.393916 0.46834  0.053933    0.0399643   0.020798    129 PHE   A CB   
3501 C CG   . PHE   B 117 ? 0.543146 0.412277 0.495621 0.0547807   0.0556448   0.0257607   129 PHE   A CG   
3502 C CD1  . PHE   B 117 ? 0.593059 0.434652 0.508797 0.0572921   0.0670563   0.0269239   129 PHE   A CD1  
3503 C CD2  . PHE   B 117 ? 0.559698 0.454123 0.553655 0.051159    0.0585785   0.0297181   129 PHE   A CD2  
3504 C CE1  . PHE   B 117 ? 0.572999 0.412339 0.49014  0.0576751   0.0817896   0.0332187   129 PHE   A CE1  
3505 C CE2  . PHE   B 117 ? 0.565036 0.456885 0.564862 0.0510596   0.0746991   0.0364861   129 PHE   A CE2  
3506 C CZ   . PHE   B 117 ? 0.550802 0.415048 0.510578 0.0549345   0.0864067   0.0387936   129 PHE   A CZ   
3507 H H    . PHE   B 117 ? 0.518885 0.399275 0.453377 0.041924    0.00903121  0.0109085   129 PHE   A H    
3508 H HA   . PHE   B 117 ? 0.517906 0.37238  0.431795 0.0383812   0.0285671   0.0122038   129 PHE   A HA   
3509 H HB2  . PHE   B 117 ? 0.545689 0.397145 0.466567 0.0597741   0.0436112   0.0212361   129 PHE   A HB2  
3510 H HB3  . PHE   B 117 ? 0.524055 0.412608 0.492696 0.0565191   0.0359733   0.0230695   129 PHE   A HB3  
3511 H HD1  . PHE   B 117 ? 0.590702 0.414009 0.47806  0.0573448   0.0641223   0.0235645   129 PHE   A HD1  
3512 H HD2  . PHE   B 117 ? 0.539972 0.452528 0.556834 0.0474555   0.0492562   0.028038    129 PHE   A HD2  
3513 H HE1  . PHE   B 117 ? 0.598083 0.417825 0.485362 0.0585947   0.0882081   0.0338896   129 PHE   A HE1  
3514 H HE2  . PHE   B 117 ? 0.54963  0.457745 0.578957 0.0469292   0.0769659   0.0396574   129 PHE   A HE2  
3515 H HZ   . PHE   B 117 ? 0.570149 0.432054 0.530777 0.0550762   0.0978398   0.0445237   129 PHE   A HZ   
3516 N N    . PHE   B 118 ? 0.457577 0.341874 0.425256 0.0277268   0.0267879   0.0105404   130 PHE   A N    
3517 C CA   . PHE   B 118 ? 0.453796 0.349452 0.451166 0.0198214   0.0261949   0.00850951  130 PHE   A CA   
3518 C C    . PHE   B 118 ? 0.499163 0.389335 0.504951 0.0212066   0.0405283   0.0180143   130 PHE   A C    
3519 O O    . PHE   B 118 ? 0.485507 0.358956 0.464788 0.0252058   0.0468788   0.0234292   130 PHE   A O    
3520 C CB   . PHE   B 118 ? 0.431969 0.322341 0.424549 0.0123503   0.0186193   -0.00023831 130 PHE   A CB   
3521 C CG   . PHE   B 118 ? 0.432959 0.329476 0.417701 0.0085194   0.00652176  -0.0103983  130 PHE   A CG   
3522 C CD1  . PHE   B 118 ? 0.439507 0.328827 0.39618  0.0111454   0.00277575  -0.0110056  130 PHE   A CD1  
3523 C CD2  . PHE   B 118 ? 0.440312 0.348071 0.442526 0.00048272  -0.00114038 -0.0189898  130 PHE   A CD2  
3524 C CE1  . PHE   B 118 ? 0.463321 0.356773 0.409117 0.00740863  -0.00613671 -0.0181869  130 PHE   A CE1  
3525 C CE2  . PHE   B 118 ? 0.475132 0.386414 0.462012 -0.00333919 -0.0119209  -0.0276804  130 PHE   A CE2  
3526 C CZ   . PHE   B 118 ? 0.458283 0.362349 0.416764 0.00085433  -0.0131666  -0.0264951  130 PHE   A CZ   
3527 H H    . PHE   B 118 ? 0.466489 0.337375 0.41469  0.0291173   0.0306086   0.0126087   130 PHE   A H    
3528 H HA   . PHE   B 118 ? 0.453866 0.36421  0.470903 0.018116    0.0222962   0.00721536  130 PHE   A HA   
3529 H HB2  . PHE   B 118 ? 0.438997 0.31906  0.415064 0.014303    0.0205899   0.00225725  130 PHE   A HB2  
3530 H HB3  . PHE   B 118 ? 0.437119 0.329069 0.447685 0.00795459  0.0207781   -0.00112662 130 PHE   A HB3  
3531 H HD1  . PHE   B 118 ? 0.447029 0.327433 0.390311 0.0143142   0.00647138  -0.00634925 130 PHE   A HD1  
3532 H HD2  . PHE   B 118 ? 0.446724 0.358697 0.469198 -0.00349553 0.00084331  -0.0188554  130 PHE   A HD2  
3533 H HE1  . PHE   B 118 ? 0.459837 0.347687 0.387422 0.00821166  -0.00745749 -0.0174159  130 PHE   A HE1  
3534 H HE2  . PHE   B 118 ? 0.469772 0.38702  0.463919 -0.0100721  -0.0181784  -0.0344791  130 PHE   A HE2  
3535 H HZ   . PHE   B 118 ? 0.470071 0.375892 0.416425 -0.00187193 -0.0192271  -0.0310917  130 PHE   A HZ   
3536 N N    . GLU   B 119 ? 0.525446 0.430483 0.567182 0.0162981   0.0447427   0.0206584   131 GLU   A N    
3537 C CA   . GLU   B 119 ? 0.52752  0.426711 0.58368  0.0121105   0.0560802   0.0283486   131 GLU   A CA   
3538 C C    . GLU   B 119 ? 0.566768 0.461283 0.637788 0.00124813  0.0481685   0.0200846   131 GLU   A C    
3539 O O    . GLU   B 119 ? 0.576924 0.48376  0.668236 -0.00737303 0.0386797   0.0105258   131 GLU   A O    
3540 C CB   . GLU   B 119 ? 0.553752 0.471812 0.643808 0.0115365   0.0677598   0.0370487   131 GLU   A CB   
3541 C CG   . GLU   B 119 ? 0.544448 0.453842 0.646057 0.00712602  0.0833315   0.0484044   131 GLU   A CG   
3542 C CD   . GLU   B 119 ? 0.556183 0.486037 0.693693 0.00570769  0.0991132   0.0594401   131 GLU   A CD   
3543 O OE1  . GLU   B 119 ? 0.613205 0.540191 0.739735 0.0150945   0.118573    0.0709027   131 GLU   A OE1  
3544 O OE2  . GLU   B 119 ? 0.565014 0.513369 0.742653 -0.00687463 0.0921924   0.0561119   131 GLU   A OE2  
3545 H H    . GLU   B 119 ? 0.51211  0.431892 0.570556 0.0147899   0.0397768   0.0184217   131 GLU   A H    
3546 H HA   . GLU   B 119 ? 0.547545 0.432711 0.581469 0.0166306   0.0618747   0.0337435   131 GLU   A HA   
3547 H HB2  . GLU   B 119 ? 0.546514 0.467203 0.627707 0.0203543   0.0737643   0.040902    131 GLU   A HB2  
3548 H HB3  . GLU   B 119 ? 0.53673  0.470669 0.650847 0.00514263  0.0595712   0.0322005   131 GLU   A HB3  
3549 H HG2  . GLU   B 119 ? 0.550375 0.454514 0.662149 -0.00114784 0.0779144   0.0445455   131 GLU   A HG2  
3550 H HG3  . GLU   B 119 ? 0.559194 0.452494 0.633279 0.0129178   0.0892576   0.0534227   131 GLU   A HG3  
3551 N N    . ILE   B 120 ? 0.57058  0.445857 0.629185 0.00235442  0.0517289   0.0239075   132 ILE   A N    
3552 C CA   . ILE   B 120 ? 0.562272 0.426111 0.633377 -0.00412933 0.0486922   0.0171935   132 ILE   A CA   
3553 C C    . ILE   B 120 ? 0.566548 0.415677 0.651051 -0.00579214 0.0611692   0.030504    132 ILE   A C    
3554 O O    . ILE   B 120 ? 0.548698 0.390661 0.616076 0.00143557  0.0689072   0.0453363   132 ILE   A O    
3555 C CB   . ILE   B 120 ? 0.600945 0.456225 0.649187 0.00188724  0.0419476   0.0121626   132 ILE   A CB   
3556 C CG1  . ILE   B 120 ? 0.527101 0.394023 0.558336 0.00288209  0.0317519   0.00196019  132 ILE   A CG1  
3557 C CG2  . ILE   B 120 ? 0.534449 0.37455  0.596255 -0.00071617 0.0431689   0.00572011  132 ILE   A CG2  
3558 C CD1  . ILE   B 120 ? 0.521688 0.384679 0.534297 0.00706403  0.0269998   -0.00148411 132 ILE   A CD1  
3559 H H    . ILE   B 120 ? 0.57305  0.441161 0.613944 0.00802417  0.0563631   0.0313768   132 ILE   A H    
3560 H HA   . ILE   B 120 ? 0.568166 0.438633 0.653854 -0.0113934  0.0435796   0.00797168  132 ILE   A HA   
3561 H HB   . ILE   B 120 ? 0.568877 0.419501 0.603655 0.0075305   0.0448882   0.0219477   132 ILE   A HB   
3562 H HG12 . ILE   B 120 ? 0.539173 0.411771 0.580533 -0.00287177 0.0274409   -0.00695485 132 ILE   A HG12 
3563 H HG13 . ILE   B 120 ? 0.537044 0.409049 0.559624 0.00606808  0.0327623   0.00700675  132 ILE   A HG13 
3564 H HG21 . ILE   B 120 ? 0.553363 0.391618 0.604631 0.00445124  0.0406062   0.00417099  132 ILE   A HG21 
3565 H HG22 . ILE   B 120 ? 0.557862 0.399178 0.629278 -0.00785223 0.0402144   -0.00544521 132 ILE   A HG22 
3566 H HG23 . ILE   B 120 ? 0.566226 0.396333 0.637308 -0.00037183 0.0500148   0.0146554   132 ILE   A HG23 
3567 H HD11 . ILE   B 120 ? 0.525211 0.383834 0.530155 0.0113417   0.0292139   0.00769575  132 ILE   A HD11 
3568 H HD12 . ILE   B 120 ? 0.516734 0.385873 0.516666 0.00713076  0.0218582   -0.00555833 132 ILE   A HD12 
3569 H HD13 . ILE   B 120 ? 0.52646  0.385159 0.547554 0.00521105  0.0271992   -0.00825172 132 ILE   A HD13 
3570 N N    . GLU   B 121 ? 0.559853 0.402052 0.671847 -0.0168606  0.0624955   0.0247684   133 GLU   A N    
3571 C CA   . GLU   B 121 ? 0.56285  0.383757 0.689782 -0.0203403  0.0737341   0.0356472   133 GLU   A CA   
3572 C C    . GLU   B 121 ? 0.566525 0.364337 0.693679 -0.0195046  0.0704953   0.0254591   133 GLU   A C    
3573 O O    . GLU   B 121 ? 0.570103 0.365547 0.705448 -0.0286938  0.0638359   0.00621795  133 GLU   A O    
3574 C CB   . GLU   B 121 ? 0.560278 0.388739 0.721613 -0.0357878  0.0798264   0.0371354   133 GLU   A CB   
3575 C CG   . GLU   B 121 ? 0.637703 0.439291 0.816285 -0.0425358  0.0924271   0.0483328   133 GLU   A CG   
3576 C CD   . GLU   B 121 ? 0.642842 0.449647 0.859345 -0.0610812  0.10088     0.0531806   133 GLU   A CD   
3577 O OE1  . GLU   B 121 ? 0.615923 0.448502 0.857158 -0.0741453  0.0936853   0.0436468   133 GLU   A OE1  
3578 O OE2  . GLU   B 121 ? 0.739049 0.523944 0.96191  -0.0628005  0.115385    0.0700266   133 GLU   A OE2  
3579 H H    . GLU   B 121 ? 0.556169 0.405604 0.676714 -0.0234041  0.0555852   0.0133412   133 GLU   A H    
3580 H HA   . GLU   B 121 ? 0.566565 0.38313  0.680478 -0.0129136  0.0798912   0.0493559   133 GLU   A HA   
3581 H HB2  . GLU   B 121 ? 0.566422 0.411175 0.729263 -0.0337409  0.0843159   0.0448932   133 GLU   A HB2  
3582 H HB3  . GLU   B 121 ? 0.570241 0.40555  0.74203  -0.0442283  0.0710527   0.0233276   133 GLU   A HB3  
3583 H HG2  . GLU   B 121 ? 0.633523 0.416808 0.811113 -0.0432957  0.088943    0.0397144   133 GLU   A HG2  
3584 H HG3  . GLU   B 121 ? 0.629875 0.424023 0.794044 -0.0333486  0.0996834   0.0628587   133 GLU   A HG3  
3585 N N    . LEU   B 122 ? 0.550138 0.331123 0.667025 -0.00776479 0.0753178   0.0387134   134 LEU   A N    
3586 C CA   . LEU   B 122 ? 0.57872  0.335892 0.701965 -0.00293132 0.0768841   0.0331715   134 LEU   A CA   
3587 C C    . LEU   B 122 ? 0.606235 0.333593 0.75306  -0.0114929  0.0879106   0.0369519   134 LEU   A C    
3588 O O    . LEU   B 122 ? 0.641678 0.356754 0.791657 -0.00788432 0.0968323   0.0588095   134 LEU   A O    
3589 C CB   . LEU   B 122 ? 0.542044 0.299322 0.650406 0.0143184   0.0753469   0.0487062   134 LEU   A CB   
3590 C CG   . LEU   B 122 ? 0.559676 0.297566 0.679236 0.0249599   0.0786299   0.046463    134 LEU   A CG   
3591 C CD1  . LEU   B 122 ? 0.524473 0.262776 0.644887 0.0221079   0.0764811   0.0200749   134 LEU   A CD1  
3592 C CD2  . LEU   B 122 ? 0.556663 0.306042 0.666938 0.0411411   0.0733547   0.0652679   134 LEU   A CD2  
3593 H H    . LEU   B 122 ? 0.55842  0.342857 0.663918 -0.00200881 0.077802    0.0519364   134 LEU   A H    
3594 H HA   . LEU   B 122 ? 0.563325 0.323828 0.685018 -0.0056746  0.071588    0.016473    134 LEU   A HA   
3595 H HB2  . LEU   B 122 ? 0.531249 0.306475 0.624883 0.0169084   0.0680911   0.0453251   134 LEU   A HB2  
3596 H HB3  . LEU   B 122 ? 0.559102 0.312701 0.664286 0.0164816   0.0794012   0.0655251   134 LEU   A HB3  
3597 H HG   . LEU   B 122 ? 0.576634 0.29243  0.709394 0.0233907   0.0865616   0.0515664   134 LEU   A HG   
3598 H HD11 . LEU   B 122 ? 0.542629 0.271171 0.668896 0.0108957   0.0783392   0.00843463  134 LEU   A HD11 
3599 H HD12 . LEU   B 122 ? 0.546043 0.273114 0.673205 0.0313515   0.0809243   0.019792    134 LEU   A HD12 
3600 H HD13 . LEU   B 122 ? 0.512614 0.271528 0.620144 0.0220547   0.0691903   0.0153928   134 LEU   A HD13 
3601 H HD21 . LEU   B 122 ? 0.565267 0.312203 0.670106 0.0424504   0.0742541   0.0821651   134 LEU   A HD21 
3602 H HD22 . LEU   B 122 ? 0.536906 0.306093 0.634509 0.0411723   0.0657156   0.0601705   134 LEU   A HD22 
3603 H HD23 . LEU   B 122 ? 0.568857 0.308181 0.691267 0.049789    0.0766651   0.0659761   134 LEU   A HD23 
3604 N N    . LEU   B 123 ? 0.680143 0.391259 0.839439 -0.0230591  0.087434    0.0157597   135 LEU   A N    
3605 C CA   . LEU   B 123 ? 0.705321 0.385191 0.887275 -0.0370648  0.0967878   0.0152299   135 LEU   A CA   
3606 C C    . LEU   B 123 ? 0.77418  0.412789 0.959893 -0.0248027  0.107697    0.0210554   135 LEU   A C    
3607 O O    . LEU   B 123 ? 0.799946 0.412275 0.999459 -0.0269176  0.11879     0.038079    135 LEU   A O    
3608 C CB   . LEU   B 123 ? 0.727764 0.406451 0.917621 -0.0583687  0.0890435   -0.0119538  135 LEU   A CB   
3609 C CG   . LEU   B 123 ? 0.732831 0.45368  0.927032 -0.0708243  0.0768419   -0.0163921  135 LEU   A CG   
3610 C CD1  . LEU   B 123 ? 0.785722 0.505728 0.985826 -0.0929047  0.064914    -0.0424758  135 LEU   A CD1  
3611 C CD2  . LEU   B 123 ? 0.728734 0.464635 0.945273 -0.0777058  0.0846756   0.00530349  135 LEU   A CD2  
3612 H H    . LEU   B 123 ? 0.65433  0.372122 0.805759 -0.0233534  0.0811351   0.00075251  135 LEU   A H    
3613 H HA   . LEU   B 123 ? 0.715691 0.401345 0.905709 -0.0413253  0.101397    0.030129    135 LEU   A HA   
3614 H HB2  . LEU   B 123 ? 0.736119 0.406792 0.913686 -0.0538808  0.0861036   -0.0268888  135 LEU   A HB2  
3615 H HB3  . LEU   B 123 ? 0.76021  0.415179 0.964928 -0.0693573  0.0950807   -0.0127647  135 LEU   A HB3  
3616 H HG   . LEU   B 123 ? 0.707901 0.448446 0.885899 -0.0599694  0.0714373   -0.0157724  135 LEU   A HG   
3617 H HD11 . LEU   B 123 ? 0.780546 0.490326 0.96248  -0.0885481  0.0614929   -0.0569838  135 LEU   A HD11 
3618 H HD12 . LEU   B 123 ? 0.756019 0.506022 0.961702 -0.0988445  0.0561488   -0.0423704  135 LEU   A HD12 
3619 H HD13 . LEU   B 123 ? 0.801626 0.500873 1.01741  -0.105765   0.069497    -0.0442846  135 LEU   A HD13 
3620 H HD21 . LEU   B 123 ? 0.719966 0.457552 0.926824 -0.0644799  0.0909649   0.0212242   135 LEU   A HD21 
3621 H HD22 . LEU   B 123 ? 0.754058 0.469941 0.987424 -0.0889629  0.0908999   0.00661825  135 LEU   A HD22 
3622 H HD23 . LEU   B 123 ? 0.712517 0.476116 0.936067 -0.0842542  0.0778053   0.00250083  135 LEU   A HD23 
3623 N N    . ASP   B 124 ? 0.789617 0.422116 0.964903 -0.0116757  0.106125    0.007561    136 ASP   A N    
3624 C CA   . ASP   B 124 ? 0.808664 0.404278 0.991177 0.00387656  0.117767    0.0108731   136 ASP   A CA   
3625 C C    . ASP   B 124 ? 0.825283 0.437016 0.996373 0.0215203   0.114812    0.00141849  136 ASP   A C    
3626 O O    . ASP   B 124 ? 0.909624 0.551855 1.06509  0.0162361   0.104363    -0.0125422  136 ASP   A O    
3627 C CB   . ASP   B 124 ? 0.852392 0.400812 1.04487  -0.0105376  0.1272      -0.00924117 136 ASP   A CB   
3628 C CG   . ASP   B 124 ? 0.86606  0.363383 1.07195  0.00377652  0.144157    -8.655e-05  136 ASP   A CG   
3629 O OD1  . ASP   B 124 ? 0.855306 0.354536 1.06845  0.0240374   0.148104    0.0295518   136 ASP   A OD1  
3630 O OD2  . ASP   B 124 ? 0.918451 0.371764 1.12611  -0.00565817 0.152966    -0.0221884  136 ASP   A OD2  
3631 H H    . ASP   B 124 ? 0.761691 0.414439 0.925924 -0.0117793  0.0984754   -0.0036156  136 ASP   A H    
3632 H HA   . ASP   B 124 ? 0.822671 0.413801 1.01061  0.0125596   0.121774    0.033058    136 ASP   A HA   
3633 H HB2  . ASP   B 124 ? 0.848692 0.396599 1.04844  -0.0275043  0.12564     -0.00828317 136 ASP   A HB2  
3634 H HB3  . ASP   B 124 ? 0.845781 0.395067 1.02809  -0.0148087  0.123876    -0.031361   136 ASP   A HB3  
3635 N N    . PHE   B 125 ? 0.813544 0.406659 0.995152 0.0430326   0.124683    0.0114398   137 PHE   A N    
3636 C CA   . PHE   B 125 ? 0.791023 0.397514 0.96984  0.0596408   0.126454    0.00195757  137 PHE   A CA   
3637 C C    . PHE   B 125 ? 0.897539 0.464261 1.09587  0.0789382   0.144475    0.00443365  137 PHE   A C    
3638 O O    . PHE   B 125 ? 0.892417 0.436916 1.10732  0.0880228   0.150194    0.0281284   137 PHE   A O    
3639 C CB   . PHE   B 125 ? 0.743396 0.397724 0.917636 0.0709573   0.113907    0.02141     137 PHE   A CB   
3640 C CG   . PHE   B 125 ? 0.766931 0.427115 0.951549 0.0842504   0.110658    0.0566429   137 PHE   A CG   
3641 C CD1  . PHE   B 125 ? 0.851385 0.508727 1.05702  0.107833    0.115798    0.0744809   137 PHE   A CD1  
3642 C CD2  . PHE   B 125 ? 0.794242 0.465129 0.966322 0.0740508   0.10232     0.0731947   137 PHE   A CD2  
3643 C CE1  . PHE   B 125 ? 0.826403 0.490954 1.03817  0.119266    0.109224    0.108821    137 PHE   A CE1  
3644 C CE2  . PHE   B 125 ? 0.823528 0.498104 0.996377 0.0850045   0.0985373   0.105343    137 PHE   A CE2  
3645 C CZ   . PHE   B 125 ? 0.816508 0.488549 1.00792  0.106849    0.0999997   0.123587    137 PHE   A CZ   
3646 H H    . PHE   B 125 ? 0.839131 0.411781 1.03181  0.04793     0.131123    0.0260603   137 PHE   A H    
3647 H HA   . PHE   B 125 ? 0.801592 0.410175 0.968149 0.0497955   0.124828    -0.0201832  137 PHE   A HA   
3648 H HB2  . PHE   B 125 ? 0.746085 0.410195 0.922139 0.0805632   0.116247    0.0148967   137 PHE   A HB2  
3649 H HB3  . PHE   B 125 ? 0.725146 0.399471 0.885172 0.0590388   0.104558    0.0163955   137 PHE   A HB3  
3650 H HD1  . PHE   B 125 ? 0.838107 0.488466 1.05401  0.116693    0.124123    0.0638312   137 PHE   A HD1  
3651 H HD2  . PHE   B 125 ? 0.776814 0.452652 0.938804 0.0597936   0.0995653   0.0628916   137 PHE   A HD2  
3652 H HE1  . PHE   B 125 ? 0.846457 0.511645 1.07548  0.136046    0.111289    0.122402    137 PHE   A HE1  
3653 H HE2  . PHE   B 125 ? 0.808092 0.487733 0.968322 0.0777989   0.094937    0.11539     137 PHE   A HE2  
3654 H HZ   . PHE   B 125 ? 0.83188  0.507242 1.02223  0.113867    0.0953565   0.14674     137 PHE   A HZ   
3655 N N    . LYS   B 126 ? 0.906125 0.462608 1.10075  0.0860814   0.154884    -0.0193341  138 LYS   A N    
3656 C CA   . LYS   B 126 ? 0.961035 0.472805 1.17222  0.1047      0.176595    -0.0235787  138 LYS   A CA   
3657 C C    . LYS   B 126 ? 0.948727 0.487283 1.16859  0.128051    0.184274    -0.024882   138 LYS   A C    
3658 O O    . LYS   B 126 ? 0.886909 0.454617 1.08784  0.120871    0.17939     -0.0423291  138 LYS   A O    
3659 C CB   . LYS   B 126 ? 0.984715 0.441362 1.17991  0.0872976   0.188598    -0.0577004  138 LYS   A CB   
3660 H H    . LYS   B 126 ? 0.888801 0.465503 1.06904  0.0798395   0.149557    -0.0330959  138 LYS   A H    
3661 H HA   . LYS   B 126 ? 0.967979 0.467379 1.19613  0.114135    0.179174    -0.00177816 138 LYS   A HA   
3664 N N    . GLY   B 127 ? 1.01156  0.542617 1.26307  0.156521    0.196432    -0.00342774 139 GLY   A N    
3665 C CA   . GLY   B 127 ? 1.05753  0.606962 1.32667  0.18089     0.210436    -0.00586673 139 GLY   A CA   
3666 C C    . GLY   B 127 ? 1.15765  0.664757 1.40629  0.177654    0.23299     -0.0453472  139 GLY   A C    
3667 O O    . GLY   B 127 ? 1.23102  0.676449 1.47938  0.179683    0.250046    -0.0568974  139 GLY   A O    
3668 H H    . GLY   B 127 ? 1.0233   0.538587 1.28744  0.161417    0.196463    0.0145677   139 GLY   A H    
3669 H HA2  . GLY   B 127 ? 1.01907  0.612925 1.28552  0.178725    0.199031    -0.00134167 139 GLY   A HA2  
3670 H HA3  . GLY   B 127 ? 1.07477  0.619641 1.37163  0.201632    0.217094    0.0143647   139 GLY   A HA3  
3671 N N    . GLU   B 128 ? 1.13791  0.675428 1.36511  0.170675    0.232411    -0.0655181  140 GLU   A N    
3672 C CA   . GLU   B 128 ? 1.2099   0.712826 1.40452  0.163217    0.250621    -0.104825   140 GLU   A CA   
3673 C C    . GLU   B 128 ? 1.34665  0.789152 1.55562  0.186137    0.283301    -0.115024   140 GLU   A C    
3674 O O    . GLU   B 128 ? 1.42887  0.879648 1.68274  0.216623    0.29393     -0.0874404  140 GLU   A O    
3675 C CB   . GLU   B 128 ? 1.10906  0.660824 1.29148  0.164662    0.251174    -0.112563   140 GLU   A CB   
3676 O OXT  . GLU   B 128 ? 1.39472  0.781967 1.56861  0.172718    0.296619    -0.150221   140 GLU   A OXT  
3677 H H    . GLU   B 128 ? 1.10251  0.683389 1.33317  0.169861    0.219857    -0.0537235  140 GLU   A H    
3678 H HA   . GLU   B 128 ? 1.20617  0.691165 1.37477  0.140535    0.241012    -0.11995    140 GLU   A HA   
3681 C CAM  . A1IN6 C .   ? 0.610918 0.379444 0.375117 -0.0378811  -0.154125   -0.0597884  201 A1IN6 B CAM  
3682 C CAN  . A1IN6 C .   ? 0.657274 0.385438 0.390972 -0.0303281  -0.146551   -0.0621282  201 A1IN6 B CAN  
3683 C CAO  . A1IN6 C .   ? 0.64041  0.362631 0.402974 -0.0504582  -0.129857   -0.0478807  201 A1IN6 B CAO  
3684 C CAP  . A1IN6 C .   ? 0.598257 0.354154 0.374517 -0.0490315  -0.111907   -0.0269118  201 A1IN6 B CAP  
3685 C CAQ  . A1IN6 C .   ? 0.569911 0.36191  0.374445 -0.0563665  -0.114996   -0.0264189  201 A1IN6 B CAQ  
3686 C CAL  . A1IN6 C .   ? 0.559283 0.356819 0.338658 -0.0359999  -0.131444   -0.0370111  201 A1IN6 B CAL  
3687 C CAG  . A1IN6 C .   ? 0.555084 0.389797 0.356377 -0.0337961  -0.136658   -0.032791   201 A1IN6 B CAG  
3688 C CAH  . A1IN6 C .   ? 0.535921 0.391014 0.3464   -0.0293438  -0.115351   -0.0137854  201 A1IN6 B CAH  
3689 O OAK  . A1IN6 C .   ? 0.545706 0.394213 0.339552 -0.0203913  -0.099766   -0.00370414 201 A1IN6 B OAK  
3690 N N    . A1IN6 C .   ? 0.525793 0.407944 0.365755 -0.0324701  -0.112924   -0.00740542 201 A1IN6 B N    
3691 C CAV  . A1IN6 C .   ? 0.536923 0.437548 0.409802 -0.039913   -0.133539   -0.0183616  201 A1IN6 B CAV  
3692 C CAU  . A1IN6 C .   ? 0.523003 0.445012 0.44405  -0.0554402  -0.119713   -0.012124   201 A1IN6 B CAU  
3693 C CAT  . A1IN6 C .   ? 0.507115 0.440464 0.425689 -0.0436368  -0.101111   0.00395446  201 A1IN6 B CAT  
3694 C CB   . A1IN6 C .   ? 0.484197 0.39871  0.374676 -0.0429385  -0.0828623  0.0121761   201 A1IN6 B CB   
3695 C CA   . A1IN6 C .   ? 0.489652 0.385283 0.336252 -0.0268913  -0.0918414  0.00943493  201 A1IN6 B CA   
3696 C C    . A1IN6 C .   ? 0.511601 0.411766 0.335902 -0.00388484 -0.0913033  0.0179078   201 A1IN6 B C    
3697 O O    . A1IN6 C .   ? 0.467563 0.375667 0.300291 0.00137342  -0.0738843  0.0321781   201 A1IN6 B O    
3698 O OAY  . A1IN6 C .   ? 0.603098 0.491463 0.389881 0.0127151   -0.109934   0.00899859  201 A1IN6 B OAY  
3699 C CAZ  . A1IN6 C .   ? 0.579519 0.466841 0.332236 0.0392591   -0.107177   0.0204556   201 A1IN6 B CAZ  
3700 C CBA  . A1IN6 C .   ? 0.581528 0.48652  0.345315 0.0474484   -0.126056   0.0217323   201 A1IN6 B CBA  
3701 C CBB  . A1IN6 C .   ? 0.608666 0.517825 0.376052 0.0431864   -0.163094   -0.00044318 201 A1IN6 B CBB  
3702 C CBC  . A1IN6 C .   ? 0.700784 0.580435 0.392765 0.0678471   -0.179382   -0.0103416  201 A1IN6 B CBC  
3703 C CBE  . A1IN6 C .   ? 0.762908 0.636844 0.453253 0.0600342   -0.220585   -0.040341   201 A1IN6 B CBE  
3704 C CBD  . A1IN6 C .   ? 0.817283 0.64917  0.426871 0.0805291   -0.227321   -0.054151   201 A1IN6 B CBD  
3705 O OAI  . A1IN6 C .   ? 0.798162 0.607152 0.412381 0.0645583   -0.214817   -0.0647908  201 A1IN6 B OAI  
3706 C CAC  . A1IN6 C .   ? 0.689906 0.510997 0.363096 0.0372454   -0.194493   -0.0572465  201 A1IN6 B CAC  
3707 C CAB  . A1IN6 C .   ? 0.652326 0.485533 0.38347  0.00803296  -0.210097   -0.069893   201 A1IN6 B CAB  
3708 O OBH  . A1IN6 C .   ? 0.695119 0.533785 0.43485  0.00530045  -0.248844   -0.0916435  201 A1IN6 B OBH  
3709 C CBI  . A1IN6 C .   ? 0.66561  0.54139  0.48373  -0.0179568  -0.263605   -0.0957321  201 A1IN6 B CBI  
3710 C CAA  . A1IN6 C .   ? 0.602993 0.440922 0.378366 -0.0155641  -0.187036   -0.0604276  201 A1IN6 B CAA  
3711 C CAF  . A1IN6 C .   ? 0.590492 0.42403  0.35626  -0.011477   -0.155345   -0.0413587  201 A1IN6 B CAF  
3712 C CAE  . A1IN6 C .   ? 0.597401 0.424884 0.318582 0.0152113   -0.142729   -0.0308377  201 A1IN6 B CAE  
3713 C CAD  . A1IN6 C .   ? 0.663747 0.482343 0.336574 0.0396619   -0.158949   -0.0379423  201 A1IN6 B CAD  
3714 O OBF  . A1IN6 C .   ? 0.662685 0.472641 0.289057 0.067054    -0.141656   -0.0251456  201 A1IN6 B OBF  
3715 C CBG  . A1IN6 C .   ? 0.658579 0.459338 0.276026 0.0754412   -0.110556   -0.0125356  201 A1IN6 B CBG  
3716 H HAM  . A1IN6 C .   ? 0.634673 0.408596 0.378877 -0.024177   -0.166941   -0.0668143  201 A1IN6 B HAM  
3717 H HAN  . A1IN6 C .   ? 0.621233 0.385758 0.416124 -0.0585178  -0.160957   -0.0671805  201 A1IN6 B HAN  
3718 H HAO  . A1IN6 C .   ? 0.696506 0.397803 0.416935 -0.0316556  -0.162749   -0.0808913  201 A1IN6 B HAO  
3719 H HAP  . A1IN6 C .   ? 0.655954 0.384699 0.362738 -0.00959152 -0.135995   -0.0546043  201 A1IN6 B HAP  
3720 H HAQ  . A1IN6 C .   ? 0.643806 0.36465  0.435297 -0.0712096  -0.135044   -0.0534957  201 A1IN6 B HAQ  
3721 H HAR  . A1IN6 C .   ? 0.66341  0.355711 0.406263 -0.0437252  -0.12531    -0.0472749  201 A1IN6 B HAR  
3722 H HAS  . A1IN6 C .   ? 0.591302 0.338278 0.376169 -0.0600723  -0.102227   -0.0181383  201 A1IN6 B HAS  
3723 H HAT  . A1IN6 C .   ? 0.593204 0.353182 0.350255 -0.0306154  -0.106072   -0.0211362  201 A1IN6 B HAT  
3724 H HAV  . A1IN6 C .   ? 0.535638 0.347145 0.346646 -0.0535409  -0.103601   -0.0147668  201 A1IN6 B HAV  
3725 H HAU  . A1IN6 C .   ? 0.565848 0.360346 0.396647 -0.0726176  -0.121101   -0.0330696  201 A1IN6 B HAU  
3726 H HAL  . A1IN6 C .   ? 0.572349 0.365348 0.325159 -0.0182718  -0.121926   -0.0302062  201 A1IN6 B HAL  
3727 H HAG  . A1IN6 C .   ? 0.549896 0.39393  0.386779 -0.0515029  -0.143228   -0.0383285  201 A1IN6 B HAG  
3728 H HB7  . A1IN6 C .   ? 0.553664 0.463099 0.412468 -0.0228714  -0.144813   -0.0174473  201 A1IN6 B HB7  
3729 H HB8  . A1IN6 C .   ? 0.558945 0.447833 0.435115 -0.0492124  -0.147911   -0.0321008  201 A1IN6 B HB8  
3730 H HB5  . A1IN6 C .   ? 0.523785 0.46403  0.47678  -0.0593773  -0.132565   -0.0184819  201 A1IN6 B HB5  
3731 H HB6  . A1IN6 C .   ? 0.512092 0.423442 0.439218 -0.0694954  -0.105825   -0.0102923  201 A1IN6 B HB6  
3732 H HB3  . A1IN6 C .   ? 0.512815 0.450668 0.415616 -0.0262251  -0.107745   0.00821804  201 A1IN6 B HB3  
3733 H HB4  . A1IN6 C .   ? 0.485541 0.430513 0.434027 -0.0526178  -0.0889821  0.00739423  201 A1IN6 B HB4  
3734 H HB2  . A1IN6 C .   ? 0.479015 0.382888 0.371595 -0.0561019  -0.0771349  0.00992086  201 A1IN6 B HB2  
3735 H HB1  . A1IN6 C .   ? 0.471373 0.390532 0.361623 -0.0365899  -0.0711617  0.0214709   201 A1IN6 B HB1  
3736 H HA   . A1IN6 C .   ? 0.489121 0.375037 0.327435 -0.0288789  -0.0805865  0.0139434   201 A1IN6 B HA   
3737 H HB9  . A1IN6 C .   ? 0.625129 0.49389  0.336125 0.0528936   -0.113192   0.0139737   201 A1IN6 B HB9  
3738 H HAZ  . A1IN6 C .   ? 0.573057 0.462446 0.331032 0.0424341   -0.0840241  0.0357494   201 A1IN6 B HAZ  
3739 H HCA  . A1IN6 C .   ? 0.613106 0.511042 0.342869 0.0696765   -0.12127    0.0336513   201 A1IN6 B HCA  
3740 H HBA  . A1IN6 C .   ? 0.550365 0.471884 0.356131 0.0355977   -0.116345   0.0281129   201 A1IN6 B HBA  
3741 H HCB  . A1IN6 C .   ? 0.613356 0.54299  0.404902 0.0466947   -0.176308   0.00152759  201 A1IN6 B HCB  
3742 H HBB  . A1IN6 C .   ? 0.594272 0.503474 0.389819 0.0215028   -0.164478   -0.0114978  201 A1IN6 B HBB  
3743 H HCC  . A1IN6 C .   ? 0.702017 0.562882 0.371316 0.0695373   -0.160034   -0.00788477 201 A1IN6 B HCC  
3744 H HBC  . A1IN6 C .   ? 0.729544 0.608263 0.390226 0.0907267   -0.180307   0.00129641  201 A1IN6 B HBC  
3745 H HCE  . A1IN6 C .   ? 0.772023 0.662889 0.469536 0.0681403   -0.245319   -0.0431628  201 A1IN6 B HCE  
3746 H HBE  . A1IN6 C .   ? 0.720292 0.60165  0.458133 0.0344945   -0.220054   -0.0484333  201 A1IN6 B HBE  
3747 H HCD  . A1IN6 C .   ? 0.830532 0.649201 0.399453 0.0997631   -0.203676   -0.0391065  201 A1IN6 B HCD  
3748 H HBD  . A1IN6 C .   ? 0.863686 0.687371 0.450732 0.0864447   -0.26       -0.0734257  201 A1IN6 B HBD  
3749 H HCI  . A1IN6 C .   ? 0.703016 0.585009 0.521678 -0.0138562  -0.298712   -0.113197   201 A1IN6 B HCI  
3750 H HBI  . A1IN6 C .   ? 0.64984  0.519479 0.504758 -0.0422154  -0.254577   -0.0999712  201 A1IN6 B HBI  
3751 H HCH  . A1IN6 C .   ? 0.630751 0.532803 0.471099 -0.0143192  -0.247962   -0.0771337  201 A1IN6 B HCH  
3752 H HAA  . A1IN6 C .   ? 0.599355 0.444481 0.418516 -0.0375761  -0.194124   -0.0679413  201 A1IN6 B HAA  
3753 H HAE  . A1IN6 C .   ? 0.581733 0.410199 0.304217 0.0179918   -0.120521   -0.0172929  201 A1IN6 B HAE  
3754 H HCG  . A1IN6 C .   ? 0.69216  0.48363  0.2687   0.0993108   -0.0986283  -0.00489464 201 A1IN6 B HCG  
3755 H HBG  . A1IN6 C .   ? 0.611533 0.432574 0.269424 0.0634134   -0.0947934  0.00168191  201 A1IN6 B HBG  
3756 H HCF  . A1IN6 C .   ? 0.668707 0.450128 0.280533 0.0710867   -0.113881   -0.0246253  201 A1IN6 B HCF  
3757 C CAM  . A1IN6 D .   ? 0.493361 0.456226 0.437898 -0.0150313  -0.07659    -0.0309862  201 A1IN6 A CAM  
3758 C CAN  . A1IN6 D .   ? 0.516369 0.490809 0.474183 -0.00096602 -0.078983   -0.0130298  201 A1IN6 A CAN  
3759 C CAO  . A1IN6 D .   ? 0.510096 0.482423 0.494887 0.0108465   -0.0617366  -0.00378093 201 A1IN6 A CAO  
3760 C CAP  . A1IN6 D .   ? 0.480809 0.427183 0.447851 0.010706    -0.0452305  -0.00967385 201 A1IN6 A CAP  
3761 C CAQ  . A1IN6 D .   ? 0.447829 0.388637 0.412197 -0.00272804 -0.0446055  -0.0248214  201 A1IN6 A CAQ  
3762 C CAL  . A1IN6 D .   ? 0.472507 0.412924 0.408328 -0.0115892  -0.0574461  -0.0345811  201 A1IN6 A CAL  
3763 C CAG  . A1IN6 D .   ? 0.500679 0.430113 0.432042 -0.0232565  -0.0528937  -0.05235    201 A1IN6 A CAG  
3764 C CAH  . A1IN6 D .   ? 0.489558 0.402665 0.411065 -0.0189299  -0.0381002  -0.0536987  201 A1IN6 A CAH  
3765 O OAK  . A1IN6 D .   ? 0.478019 0.385748 0.381268 -0.0125919  -0.0344095  -0.0460635  201 A1IN6 A OAK  
3766 N N    . A1IN6 D .   ? 0.484655 0.387568 0.416552 -0.0224216  -0.0287143  -0.0629783  201 A1IN6 A N    
3767 C CAV  . A1IN6 D .   ? 0.504325 0.405398 0.453647 -0.0333537  -0.0320831  -0.0751598  201 A1IN6 A CAV  
3768 C CAU  . A1IN6 D .   ? 0.50098  0.38914  0.472457 -0.0316689  -0.0188325  -0.0754322  201 A1IN6 A CAU  
3769 C CAT  . A1IN6 D .   ? 0.471106 0.346018 0.428531 -0.0233727  -0.00553437 -0.0767388  201 A1IN6 A CAT  
3770 C CB   . A1IN6 D .   ? 0.469362 0.352771 0.419432 -0.0142975  -0.00484502 -0.0614534  201 A1IN6 A CB   
3771 C CA   . A1IN6 D .   ? 0.483875 0.375426 0.408284 -0.0165416  -0.0151041  -0.0619134  201 A1IN6 A CA   
3772 C C    . A1IN6 D .   ? 0.500848 0.386332 0.403182 -0.0201944  -0.0119263  -0.0734189  201 A1IN6 A C    
3773 O O    . A1IN6 D .   ? 0.510491 0.391354 0.410638 -0.0160753  -0.00040271 -0.0736816  201 A1IN6 A O    
3774 O OAY  . A1IN6 D .   ? 0.560433 0.446249 0.446018 -0.0288678  -0.0213627  -0.0845052  201 A1IN6 A OAY  
3775 C CAZ  . A1IN6 D .   ? 0.626416 0.50172  0.486179 -0.0309673  -0.0121066  -0.0967194  201 A1IN6 A CAZ  
3776 C CBA  . A1IN6 D .   ? 0.708026 0.580107 0.538525 -0.0410382  -0.0216486  -0.109334   201 A1IN6 A CBA  
3777 C CBB  . A1IN6 D .   ? 0.708342 0.571302 0.549235 -0.0514167  -0.0271265  -0.124917   201 A1IN6 A CBB  
3778 C CBC  . A1IN6 D .   ? 0.738945 0.596896 0.536512 -0.0634054  -0.0380073  -0.139126   201 A1IN6 A CBC  
3779 C CBE  . A1IN6 D .   ? 0.773225 0.647275 0.576193 -0.0753697  -0.0642946  -0.137659   201 A1IN6 A CBE  
3780 C CBD  . A1IN6 D .   ? 0.800493 0.690781 0.572526 -0.0751866  -0.0811741  -0.125942   201 A1IN6 A CBD  
3781 O OAI  . A1IN6 D .   ? 0.743826 0.6599   0.548889 -0.0691975  -0.0954249  -0.105297   201 A1IN6 A OAI  
3782 C CAC  . A1IN6 D .   ? 0.640256 0.561968 0.482922 -0.0567585  -0.0846739  -0.0914117  201 A1IN6 A CAC  
3783 C CAB  . A1IN6 D .   ? 0.597751 0.528307 0.48215  -0.0597092  -0.0864398  -0.0907675  201 A1IN6 A CAB  
3784 O OBH  . A1IN6 D .   ? 0.612016 0.543724 0.495906 -0.0762077  -0.0993329  -0.105065   201 A1IN6 A OBH  
3785 C CBI  . A1IN6 D .   ? 0.640179 0.588053 0.568413 -0.0842135  -0.107325   -0.102619   201 A1IN6 A CBI  
3786 C CAA  . A1IN6 D .   ? 0.570358 0.504811 0.487633 -0.0479093  -0.0746381  -0.0771527  201 A1IN6 A CAA  
3787 C CAF  . A1IN6 D .   ? 0.550291 0.47911  0.456563 -0.0341172  -0.0639803  -0.0651013  201 A1IN6 A CAF  
3788 C CAE  . A1IN6 D .   ? 0.568869 0.489473 0.436704 -0.0330955  -0.0638206  -0.0660851  201 A1IN6 A CAE  
3789 C CAD  . A1IN6 D .   ? 0.640373 0.558269 0.476597 -0.0435733  -0.0731256  -0.0781016  201 A1IN6 A CAD  
3790 O OBF  . A1IN6 D .   ? 0.659398 0.568796 0.454174 -0.0437703  -0.0710445  -0.0785114  201 A1IN6 A OBF  
3791 C CBG  . A1IN6 D .   ? 0.635856 0.540121 0.423308 -0.0338062  -0.060289   -0.0646742  201 A1IN6 A CBG  
3792 H HAM  . A1IN6 D .   ? 0.514764 0.471614 0.430668 -0.0193311  -0.082351   -0.0360761  201 A1IN6 A HAM  
3793 H HAN  . A1IN6 D .   ? 0.496945 0.466603 0.463116 -0.0241141  -0.0781412  -0.0385352  201 A1IN6 A HAN  
3794 H HAO  . A1IN6 D .   ? 0.521033 0.517581 0.495284 -0.00362059 -0.0935143  -0.00926639 201 A1IN6 A HAO  
3795 H HAP  . A1IN6 D .   ? 0.521446 0.483828 0.451958 0.00446524  -0.0788608  -0.00846346 201 A1IN6 A HAP  
3796 H HAQ  . A1IN6 D .   ? 0.496789 0.485845 0.513214 0.00685424  -0.0625035  -0.00378717 201 A1IN6 A HAQ  
3797 H HAR  . A1IN6 D .   ? 0.506594 0.479285 0.490865 0.0229693   -0.0607563  0.00770609  201 A1IN6 A HAR  
3798 H HAS  . A1IN6 D .   ? 0.469091 0.413992 0.451415 0.0167407   -0.0345234  -0.00424842 201 A1IN6 A HAS  
3799 H HAT  . A1IN6 D .   ? 0.483487 0.415304 0.423771 0.0144944   -0.0436661  -0.00765383 201 A1IN6 A HAT  
3800 H HAV  . A1IN6 D .   ? 0.45129  0.3773   0.403114 -0.00173028 -0.035557   -0.0271281  201 A1IN6 A HAV  
3801 H HAU  . A1IN6 D .   ? 0.454336 0.404541 0.441591 -0.0092464  -0.0464938  -0.0286318  201 A1IN6 A HAU  
3802 H HAL  . A1IN6 D .   ? 0.480796 0.410894 0.392267 -0.00712197 -0.0548432  -0.031026   201 A1IN6 A HAL  
3803 H HAG  . A1IN6 D .   ? 0.495121 0.429992 0.452966 -0.0268297  -0.0522463  -0.0535457  201 A1IN6 A HAG  
3804 H HB7  . A1IN6 D .   ? 0.525876 0.42011  0.455762 -0.0400514  -0.0349275  -0.0879222  201 A1IN6 A HB7  
3805 H HB8  . A1IN6 D .   ? 0.502254 0.417293 0.467482 -0.0367708  -0.0414642  -0.0708009  201 A1IN6 A HB8  
3806 H HB5  . A1IN6 D .   ? 0.50991  0.388576 0.488297 -0.0397379  -0.0182379  -0.0862103  201 A1IN6 A HB5  
3807 H HB6  . A1IN6 D .   ? 0.477218 0.370016 0.464505 -0.0262771  -0.0151985  -0.0636692  201 A1IN6 A HB6  
3808 H HB3  . A1IN6 D .   ? 0.496129 0.367068 0.433901 -0.0253217  -0.00497223 -0.0858599  201 A1IN6 A HB3  
3809 H HB4  . A1IN6 D .   ? 0.479117 0.345223 0.451407 -0.0200953  0.0031861   -0.0747972  201 A1IN6 A HB4  
3810 H HB2  . A1IN6 D .   ? 0.455767 0.344    0.416386 -0.0115198  -0.0061671  -0.0518144  201 A1IN6 A HB2  
3811 H HB1  . A1IN6 D .   ? 0.464805 0.344072 0.41128  -0.0100792  0.00241428  -0.0602235  201 A1IN6 A HB1  
3812 H HA   . A1IN6 D .   ? 0.470813 0.364095 0.388781 -0.0111961  -0.0144123  -0.051771   201 A1IN6 A HA   
3813 H HB9  . A1IN6 D .   ? 0.619935 0.498519 0.468467 -0.0266469  -0.00752438 -0.0890262  201 A1IN6 A HB9  
3814 H HAZ  . A1IN6 D .   ? 0.629065 0.494392 0.501051 -0.0291617  -0.00090035 -0.103803   201 A1IN6 A HAZ  
3815 H HCA  . A1IN6 D .   ? 0.690317 0.573612 0.51251  -0.0420258  -0.0348046  -0.100349   201 A1IN6 A HCA  
3816 H HBA  . A1IN6 D .   ? 0.710766 0.57498  0.517874 -0.0407968  -0.0116142  -0.116141   201 A1IN6 A HBA  
3817 H HCB  . A1IN6 D .   ? 0.713478 0.561537 0.563847 -0.0490147  -0.0130346  -0.132956   201 A1IN6 A HCB  
3818 H HBB  . A1IN6 D .   ? 0.692659 0.566877 0.55818  -0.0529545  -0.0370146  -0.117142   201 A1IN6 A HBB  
3819 H HCC  . A1IN6 D .   ? 0.752516 0.613883 0.525299 -0.0595962  -0.0360833  -0.133313   201 A1IN6 A HCC  
3820 H HBC  . A1IN6 D .   ? 0.775174 0.613373 0.56107  -0.0678561  -0.0283016  -0.156453   201 A1IN6 A HBC  
3821 H HCE  . A1IN6 D .   ? 0.803541 0.664857 0.593915 -0.0877841  -0.0683018  -0.155173   201 A1IN6 A HCE  
3822 H HBE  . A1IN6 D .   ? 0.7405   0.625821 0.580221 -0.0725981  -0.0669626  -0.127892   201 A1IN6 A HBE  
3823 H HCD  . A1IN6 D .   ? 0.782328 0.671441 0.540338 -0.0663282  -0.0725242  -0.116918   201 A1IN6 A HCD  
3824 H HBD  . A1IN6 D .   ? 0.82233  0.715977 0.573768 -0.0864222  -0.0976923  -0.1327     201 A1IN6 A HBD  
3825 H HCI  . A1IN6 D .   ? 0.658812 0.607258 0.579945 -0.100448   -0.121129   -0.115155   201 A1IN6 A HCI  
3826 H HBI  . A1IN6 D .   ? 0.611554 0.583202 0.561295 -0.0770322  -0.114722   -0.0859626  201 A1IN6 A HBI  
3827 H HCH  . A1IN6 D .   ? 0.614152 0.549613 0.561831 -0.0816324  -0.0918014  -0.10428    201 A1IN6 A HCH  
3828 H HAA  . A1IN6 D .   ? 0.558712 0.500125 0.507611 -0.0506226  -0.0742967  -0.0754961  201 A1IN6 A HAA  
3829 H HAE  . A1IN6 D .   ? 0.565046 0.480299 0.425301 -0.0251414  -0.0561788  -0.0571247  201 A1IN6 A HAE  
3830 H HCG  . A1IN6 D .   ? 0.661074 0.559523 0.415881 -0.0363768  -0.0591315  -0.0650419  201 A1IN6 A HCG  
3831 H HBG  . A1IN6 D .   ? 0.620434 0.518407 0.421673 -0.0307899  -0.0461287  -0.067194   201 A1IN6 A HBG  
3832 H HCF  . A1IN6 D .   ? 0.6257   0.53739  0.425756 -0.0272403  -0.0672143  -0.0509646  201 A1IN6 A HCF  
# 
