data_9GQ6
# 
_entry.id   9GQ6 
# 
_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   9GQ6         pdb_00009gq6 10.2210/pdb9gq6/pdb 
WWPDB D_1292141277 ?            ?                   
# 
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                        9GQ6 
_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-19,22-dimethoxy-11,17-dioxa-4-azatricyclo[16.2.2.0^{4,9}]docosa-1(20),18,21-triene-3,10-dione' 473.602 
2  ?       ?                    ? ? 
3 water       nat water 18.015    59 ?       ?                    ? ? 
# 
_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-19,22-dimethoxy-11,17-dioxa-4-azatricyclo[16.2.2.0^{4,9}]docosa-1(20),18,21-triene-3,10-dione' A1IN4 
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 
A1IN4 non-polymer         . 
'(2~{S},9~{S})-2-cyclohexyl-19,22-dimethoxy-11,17-dioxa-4-azatricyclo[16.2.2.0^{4,9}]docosa-1(20),18,21-triene-3,10-dione' ? 
'C27 H39 N O6'   473.602 
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        A1IN4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IN4 
_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 A1IN4 1  201 201 A1IN4 PDB B . 
D 2 A1IN4 1  201 201 A1IN4 PDB A . 
E 3 HOH   1  301 47  HOH   HOH B . 
E 3 HOH   2  302 51  HOH   HOH B . 
E 3 HOH   3  303 48  HOH   HOH B . 
E 3 HOH   4  304 7   HOH   HOH B . 
E 3 HOH   5  305 34  HOH   HOH B . 
E 3 HOH   6  306 6   HOH   HOH B . 
E 3 HOH   7  307 31  HOH   HOH B . 
E 3 HOH   8  308 19  HOH   HOH B . 
E 3 HOH   9  309 33  HOH   HOH B . 
E 3 HOH   10 310 59  HOH   HOH B . 
E 3 HOH   11 311 1   HOH   HOH B . 
E 3 HOH   12 312 32  HOH   HOH B . 
E 3 HOH   13 313 40  HOH   HOH B . 
E 3 HOH   14 314 53  HOH   HOH B . 
E 3 HOH   15 315 3   HOH   HOH B . 
E 3 HOH   16 316 2   HOH   HOH B . 
E 3 HOH   17 317 42  HOH   HOH B . 
E 3 HOH   18 318 18  HOH   HOH B . 
E 3 HOH   19 319 13  HOH   HOH B . 
E 3 HOH   20 320 21  HOH   HOH B . 
E 3 HOH   21 321 4   HOH   HOH B . 
E 3 HOH   22 322 26  HOH   HOH B . 
E 3 HOH   23 323 12  HOH   HOH B . 
E 3 HOH   24 324 36  HOH   HOH B . 
E 3 HOH   25 325 56  HOH   HOH B . 
E 3 HOH   26 326 50  HOH   HOH B . 
E 3 HOH   27 327 44  HOH   HOH B . 
E 3 HOH   28 328 43  HOH   HOH B . 
E 3 HOH   29 329 52  HOH   HOH B . 
E 3 HOH   30 330 60  HOH   HOH B . 
F 3 HOH   1  301 5   HOH   HOH A . 
F 3 HOH   2  302 30  HOH   HOH A . 
F 3 HOH   3  303 14  HOH   HOH A . 
F 3 HOH   4  304 41  HOH   HOH A . 
F 3 HOH   5  305 15  HOH   HOH A . 
F 3 HOH   6  306 9   HOH   HOH A . 
F 3 HOH   7  307 10  HOH   HOH A . 
F 3 HOH   8  308 45  HOH   HOH A . 
F 3 HOH   9  309 20  HOH   HOH A . 
F 3 HOH   10 310 22  HOH   HOH A . 
F 3 HOH   11 311 55  HOH   HOH A . 
F 3 HOH   12 312 8   HOH   HOH A . 
F 3 HOH   13 313 38  HOH   HOH A . 
F 3 HOH   14 314 29  HOH   HOH A . 
F 3 HOH   15 315 27  HOH   HOH A . 
F 3 HOH   16 316 16  HOH   HOH A . 
F 3 HOH   17 317 11  HOH   HOH A . 
F 3 HOH   18 318 23  HOH   HOH A . 
F 3 HOH   19 319 57  HOH   HOH A . 
F 3 HOH   20 320 24  HOH   HOH A . 
F 3 HOH   21 321 17  HOH   HOH A . 
F 3 HOH   22 322 35  HOH   HOH A . 
F 3 HOH   23 323 28  HOH   HOH A . 
F 3 HOH   24 324 58  HOH   HOH A . 
F 3 HOH   25 325 25  HOH   HOH A . 
F 3 HOH   26 326 54  HOH   HOH A . 
F 3 HOH   27 327 39  HOH   HOH A . 
F 3 HOH   28 328 46  HOH   HOH A . 
F 3 HOH   29 329 49  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 44  ? CG  ? A GLU 32  CG  
2   1 Y 1 B GLU 44  ? CD  ? A GLU 32  CD  
3   1 Y 1 B GLU 44  ? OE1 ? A GLU 32  OE1 
4   1 Y 1 B GLU 44  ? OE2 ? A GLU 32  OE2 
5   1 Y 1 B GLU 45  ? CG  ? A GLU 33  CG  
6   1 Y 1 B GLU 45  ? CD  ? A GLU 33  CD  
7   1 Y 1 B GLU 45  ? OE1 ? A GLU 33  OE1 
8   1 Y 1 B GLU 45  ? OE2 ? A GLU 33  OE2 
9   1 Y 1 B LYS 65  ? CG  ? A LYS 53  CG  
10  1 Y 1 B LYS 65  ? CD  ? A LYS 53  CD  
11  1 Y 1 B LYS 65  ? CE  ? A LYS 53  CE  
12  1 Y 1 B LYS 65  ? NZ  ? A LYS 53  NZ  
13  1 Y 1 B LYS 66  ? CG  ? A LYS 54  CG  
14  1 Y 1 B LYS 66  ? CD  ? A LYS 54  CD  
15  1 Y 1 B LYS 66  ? CE  ? A LYS 54  CE  
16  1 Y 1 B LYS 66  ? NZ  ? A LYS 54  NZ  
17  1 Y 1 B ARG 73  ? CG  ? A ARG 61  CG  
18  1 Y 1 B ARG 73  ? CD  ? A ARG 61  CD  
19  1 Y 1 B ARG 73  ? NE  ? A ARG 61  NE  
20  1 Y 1 B ARG 73  ? CZ  ? A ARG 61  CZ  
21  1 Y 1 B ARG 73  ? NH1 ? A ARG 61  NH1 
22  1 Y 1 B ARG 73  ? NH2 ? A ARG 61  NH2 
23  1 Y 1 B ASN 74  ? CG  ? A ASN 62  CG  
24  1 Y 1 B ASN 74  ? OD1 ? A ASN 62  OD1 
25  1 Y 1 B ASN 74  ? ND2 ? A ASN 62  ND2 
26  1 Y 1 B LYS 83  ? CG  ? A LYS 71  CG  
27  1 Y 1 B LYS 83  ? CD  ? A LYS 71  CD  
28  1 Y 1 B LYS 83  ? CE  ? A LYS 71  CE  
29  1 Y 1 B LYS 83  ? NZ  ? A LYS 71  NZ  
30  1 Y 1 B LYS 88  ? CG  ? A LYS 76  CG  
31  1 Y 1 B LYS 88  ? CD  ? A LYS 76  CD  
32  1 Y 1 B LYS 88  ? CE  ? A LYS 76  CE  
33  1 Y 1 B LYS 88  ? NZ  ? A LYS 76  NZ  
34  1 Y 1 B LYS 98  ? CG  ? A LYS 86  CG  
35  1 Y 1 B LYS 98  ? CD  ? A LYS 86  CD  
36  1 Y 1 B LYS 98  ? CE  ? A LYS 86  CE  
37  1 Y 1 B LYS 98  ? NZ  ? A LYS 86  NZ  
38  1 Y 1 B LYS 99  ? CG  ? A LYS 87  CG  
39  1 Y 1 B LYS 99  ? CD  ? A LYS 87  CD  
40  1 Y 1 B LYS 99  ? CE  ? A LYS 87  CE  
41  1 Y 1 B LYS 99  ? NZ  ? A LYS 87  NZ  
42  1 Y 1 B LYS 138 ? CG  ? A LYS 126 CG  
43  1 Y 1 B LYS 138 ? CD  ? A LYS 126 CD  
44  1 Y 1 B LYS 138 ? CE  ? A LYS 126 CE  
45  1 Y 1 B LYS 138 ? NZ  ? A LYS 126 NZ  
46  1 Y 1 B GLU 140 ? CG  ? A GLU 128 CG  
47  1 Y 1 B GLU 140 ? CD  ? A GLU 128 CD  
48  1 Y 1 B GLU 140 ? OE1 ? A GLU 128 OE1 
49  1 Y 1 B GLU 140 ? OE2 ? A GLU 128 OE2 
50  1 Y 1 A LYS 28  ? CE  ? B LYS 16  CE  
51  1 Y 1 A LYS 28  ? NZ  ? B LYS 16  NZ  
52  1 Y 1 A GLU 44  ? CG  ? B GLU 32  CG  
53  1 Y 1 A GLU 44  ? CD  ? B GLU 32  CD  
54  1 Y 1 A GLU 44  ? OE1 ? B GLU 32  OE1 
55  1 Y 1 A GLU 44  ? OE2 ? B GLU 32  OE2 
56  1 Y 1 A LYS 52  ? CG  ? B LYS 40  CG  
57  1 Y 1 A LYS 52  ? CD  ? B LYS 40  CD  
58  1 Y 1 A LYS 52  ? CE  ? B LYS 40  CE  
59  1 Y 1 A LYS 52  ? NZ  ? B LYS 40  NZ  
60  1 Y 1 A LYS 65  ? CG  ? B LYS 53  CG  
61  1 Y 1 A LYS 65  ? CD  ? B LYS 53  CD  
62  1 Y 1 A LYS 65  ? CE  ? B LYS 53  CE  
63  1 Y 1 A LYS 65  ? NZ  ? B LYS 53  NZ  
64  1 Y 1 A LYS 66  ? CG  ? B LYS 54  CG  
65  1 Y 1 A LYS 66  ? CD  ? B LYS 54  CD  
66  1 Y 1 A LYS 66  ? CE  ? B LYS 54  CE  
67  1 Y 1 A LYS 66  ? NZ  ? B LYS 54  NZ  
68  1 Y 1 A ARG 73  ? CG  ? B ARG 61  CG  
69  1 Y 1 A ARG 73  ? CD  ? B ARG 61  CD  
70  1 Y 1 A ARG 73  ? NE  ? B ARG 61  NE  
71  1 Y 1 A ARG 73  ? CZ  ? B ARG 61  CZ  
72  1 Y 1 A ARG 73  ? NH1 ? B ARG 61  NH1 
73  1 Y 1 A ARG 73  ? NH2 ? B ARG 61  NH2 
74  1 Y 1 A ASN 74  ? CG  ? B ASN 62  CG  
75  1 Y 1 A ASN 74  ? OD1 ? B ASN 62  OD1 
76  1 Y 1 A ASN 74  ? ND2 ? B ASN 62  ND2 
77  1 Y 1 A GLU 75  ? CG  ? B GLU 63  CG  
78  1 Y 1 A GLU 75  ? CD  ? B GLU 63  CD  
79  1 Y 1 A GLU 75  ? OE1 ? B GLU 63  OE1 
80  1 Y 1 A GLU 75  ? OE2 ? B GLU 63  OE2 
81  1 Y 1 A LYS 83  ? CG  ? B LYS 71  CG  
82  1 Y 1 A LYS 83  ? CD  ? B LYS 71  CD  
83  1 Y 1 A LYS 83  ? CE  ? B LYS 71  CE  
84  1 Y 1 A LYS 83  ? NZ  ? B LYS 71  NZ  
85  1 Y 1 A LYS 88  ? CG  ? B LYS 76  CG  
86  1 Y 1 A LYS 88  ? CD  ? B LYS 76  CD  
87  1 Y 1 A LYS 88  ? CE  ? B LYS 76  CE  
88  1 Y 1 A LYS 88  ? NZ  ? B LYS 76  NZ  
89  1 Y 1 A LYS 121 ? CG  ? B LYS 109 CG  
90  1 Y 1 A LYS 121 ? CD  ? B LYS 109 CD  
91  1 Y 1 A LYS 121 ? CE  ? B LYS 109 CE  
92  1 Y 1 A LYS 121 ? NZ  ? B LYS 109 NZ  
93  1 Y 1 A LYS 138 ? CG  ? B LYS 126 CG  
94  1 Y 1 A LYS 138 ? CD  ? B LYS 126 CD  
95  1 Y 1 A LYS 138 ? CE  ? B LYS 126 CE  
96  1 Y 1 A LYS 138 ? NZ  ? B LYS 126 NZ  
97  1 Y 1 A GLU 140 ? CG  ? B GLU 128 CG  
98  1 Y 1 A GLU 140 ? CD  ? B GLU 128 CD  
99  1 Y 1 A GLU 140 ? OE1 ? B GLU 128 OE1 
100 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                     9GQ6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.843 
_cell.length_a_esd                 ? 
_cell.length_b                     48.843 
_cell.length_b_esd                 ? 
_cell.length_c                     194.255 
_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                         9GQ6 
_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                   9GQ6 
_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             2.39 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.50 
_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                                       9GQ6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.88 
_reflns.d_resolution_low                               48.56 
_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                                     22952 
_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                                10.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.02 
_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                                0.048 
_reflns.pdbx_Rpim_I_all                                0.020 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.043 
_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 
9.01 48.56 ? 65.2 ? ? ? ? 278  ? ? ? ? ? ? ? ? ? ? ? 8.2 0.99 ? ? 0.028 0.012 ? 1 ? 0.999 ? ? 99.5 ? 0.025 ? ? ? ? ? ? ? ? ? 
1.88 1.92  ? 1.6  ? ? ? ? 1374 ? ? ? ? ? ? ? ? ? ? ? 9.8 1.07 ? ? 1.516 0.655 ? 2 ? 0.637 ? ? 98.3 ? 1.362 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.097 
_refine.aniso_B[1][2]                            -0.049 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            -0.097 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            0.315 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               57.493 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.952 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_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                                 9GQ6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.88 
_refine.ls_d_res_low                             42.335 
_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                     22884 
_refine.ls_number_reflns_R_free                  1139 
_refine.ls_number_reflns_R_work                  21745 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.856 
_refine.ls_percent_reflns_R_free                 4.977 
_refine.ls_R_factor_all                          0.241 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2737 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2393 
_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                       0.173 
_refine.pdbx_overall_ESU_R_Free                  0.158 
_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                             12.446 
_refine.overall_SU_ML                            0.170 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.88 
_refine_hist.d_res_low                        42.335 
_refine_hist.number_atoms_solvent             59 
_refine_hist.number_atoms_total               1980 
_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        1853 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_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' ? 0.012  0.012  1966 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.016  1809 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.850  1.848  2665 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.309  1.818  4211 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 8.124  5.000  250  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 5.932  5.000  4    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 12.931 10.000 296  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.755 10.000 70   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.093  0.200  295  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 1.897  0.200  32   ? r_chiral_restr_other           ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  2241 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  399  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.202  0.200  365  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.201  0.200  1679 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.177  0.200  1027 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.090  0.200  1000 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.152  0.200  68   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.030  0.200  1    ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.327  0.200  8    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.232  0.200  39   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.094  0.200  4    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 2.811  2.750  1012 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.809  2.750  1012 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.789  4.924  1258 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.788  4.923  1259 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 2.975  2.874  954  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.973  2.874  955  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 4.070  5.212  1407 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 4.068  5.212  1408 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 6.256  26.161 2161 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 6.259  25.878 2156 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.114  0.050  3376 ? 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 ? ? 0.11402 ? 0.05008 1 'Local ncs' ? B ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.11402 ? 0.05008 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' 1.88  1.927  1629 . 93 1510 98.4039  . 0.347 . . 0.343 . . . . . 0.339 . 20 . 0.905 0.865 0.415 
'X-RAY DIFFRACTION' 1.927 1.980  1602 . 95 1507 100.0000 . 0.326 . . 0.323 . . . . . 0.316 . 20 . 0.921 0.898 0.379 
'X-RAY DIFFRACTION' 1.980 2.037  1590 . 65 1525 100.0000 . 0.319 . . 0.316 . . . . . 0.302 . 20 . 0.927 0.911 0.364 
'X-RAY DIFFRACTION' 2.037 2.099  1510 . 70 1440 100.0000 . 0.308 . . 0.306 . . . . . 0.282 . 20 . 0.937 0.880 0.359 
'X-RAY DIFFRACTION' 2.099 2.168  1488 . 64 1424 100.0000 . 0.284 . . 0.281 . . . . . 0.259 . 20 . 0.947 0.920 0.351 
'X-RAY DIFFRACTION' 2.168 2.244  1445 . 82 1363 100.0000 . 0.286 . . 0.285 . . . . . 0.255 . 20 . 0.946 0.934 0.305 
'X-RAY DIFFRACTION' 2.244 2.328  1396 . 75 1321 100.0000 . 0.284 . . 0.282 . . . . . 0.253 . 20 . 0.950 0.936 0.315 
'X-RAY DIFFRACTION' 2.328 2.423  1334 . 59 1274 99.9250  . 0.269 . . 0.267 . . . . . 0.236 . 20 . 0.956 0.933 0.316 
'X-RAY DIFFRACTION' 2.423 2.531  1292 . 72 1219 99.9226  . 0.278 . . 0.275 . . . . . 0.244 . 20 . 0.953 0.945 0.333 
'X-RAY DIFFRACTION' 2.531 2.654  1235 . 54 1181 100.0000 . 0.269 . . 0.270 . . . . . 0.239 . 20 . 0.956 0.965 0.242 
'X-RAY DIFFRACTION' 2.654 2.797  1180 . 66 1114 100.0000 . 0.287 . . 0.283 . . . . . 0.260 . 20 . 0.947 0.918 0.381 
'X-RAY DIFFRACTION' 2.797 2.965  1113 . 65 1048 100.0000 . 0.268 . . 0.264 . . . . . 0.249 . 20 . 0.953 0.942 0.334 
'X-RAY DIFFRACTION' 2.965 3.169  1069 . 50 1019 100.0000 . 0.259 . . 0.256 . . . . . 0.249 . 20 . 0.959 0.940 0.332 
'X-RAY DIFFRACTION' 3.169 3.421  985  . 43 942  100.0000 . 0.258 . . 0.259 . . . . . 0.258 . 20 . 0.960 0.966 0.248 
'X-RAY DIFFRACTION' 3.421 3.745  946  . 51 895  100.0000 . 0.242 . . 0.239 . . . . . 0.244 . 20 . 0.972 0.955 0.291 
'X-RAY DIFFRACTION' 3.745 4.183  835  . 35 800  100.0000 . 0.203 . . 0.202 . . . . . 0.213 . 20 . 0.977 0.971 0.225 
'X-RAY DIFFRACTION' 4.183 4.823  749  . 38 711  100.0000 . 0.159 . . 0.157 . . . . . 0.181 . 20 . 0.985 0.983 0.182 
'X-RAY DIFFRACTION' 4.823 5.888  656  . 22 634  100.0000 . 0.199 . . 0.197 . . . . . 0.228 . 20 . 0.978 0.948 0.236 
'X-RAY DIFFRACTION' 5.888 8.247  526  . 33 492  99.8099  . 0.249 . . 0.250 . . . . . 0.292 . 20 . 0.970 0.970 0.218 
'X-RAY DIFFRACTION' 8.247 42.335 336  . 7  326  99.1071  . 0.241 . . 0.241 . . . . . 0.312 . 20 . 0.951 0.976 0.261 
# 
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                     9GQ6 
_struct.title                        'The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog p5(1,2)-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        9GQ6 
_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 9GQ6 B 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
2 1 9GQ6 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 9GQ6 GLY B 1  ? UNP Q13451 ?   ?   'expression tag'      13  1  
1 9GQ6 ALA B 2  ? UNP Q13451 ?   ?   'expression tag'      14  2  
1 9GQ6 PRO B 3  ? UNP Q13451 ?   ?   'expression tag'      15  3  
1 9GQ6 THR B 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  4  
1 9GQ6 ALA B 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 5  
1 9GQ6 ILE B 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 6  
2 9GQ6 GLY A 1  ? UNP Q13451 ?   ?   'expression tag'      13  7  
2 9GQ6 ALA A 2  ? UNP Q13451 ?   ?   'expression tag'      14  8  
2 9GQ6 PRO A 3  ? UNP Q13451 ?   ?   'expression tag'      15  9  
2 9GQ6 THR A 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  10 
2 9GQ6 ALA A 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 11 
2 9GQ6 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 -2.11 
2 LEU 107 B . ? LEU 119 A PRO 108 B ? PRO 120 A 1 2.01  
# 
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 LYS A 26  ? N LYS B 38  O ILE A 90  ? O ILE B 102 
AA1 3 4 N ALA A 91  ? N ALA B 103 O ILE A 120 ? O ILE B 132 
AA1 4 5 O ASP A 124 ? O ASP B 136 N TYR A 42  ? N TYR B 54  
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 LYS A 26  ? N LYS B 38  O ILE A 90  ? O ILE B 102 
AA2 3 4 N ALA A 91  ? N ALA B 103 O ILE A 120 ? O ILE B 132 
AA2 4 5 O ASP A 124 ? O ASP B 136 N TYR A 42  ? N TYR B 54  
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 LYS B 26  ? N LYS A 38  O ILE B 90  ? O ILE A 102 
AA3 3 4 N ALA B 91  ? N ALA A 103 O ILE B 120 ? O ILE A 132 
AA3 4 5 O ASP B 124 ? O ASP A 136 N TYR B 42  ? N TYR A 54  
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 LYS B 26  ? N LYS A 38  O ILE B 90  ? O ILE A 102 
AA4 3 4 N ALA B 91  ? N ALA A 103 O ILE B 120 ? O ILE A 132 
AA4 4 5 O ASP B 124 ? O ASP A 136 N TYR B 42  ? N TYR A 54  
AA4 5 6 N VAL B 41  ? N VAL A 53  O PHE B 67  ? O PHE A 79  
# 
_pdbx_entry_details.entry_id                   9GQ6 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HH A TYR 57 ? ? OD2 A ASP 68  ? ? 1.58 
2 1 H2 B GLY 13 ? ? O   B HOH 304 ? ? 1.59 
# 
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 ? ? -130.88 -103.26 
2 1 ALA A 112 ? ? -134.40 -106.87 
3 1 SER A 118 ? ? -151.15 72.73   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 325 ? E HOH . 
2 1 B HOH 330 ? E HOH . 
# 
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 18.4709 0.4568   3.4876  0.2710 ? -0.1276 ? -0.0908 ? 0.1190 ? 0.1598 ? 0.3185 ? 5.8133 ? -2.3678 
? -0.6371 ? 6.8447 ? -0.2258 ? 5.2967 ? 0.0167  ? -0.3213 ? -0.1953 ? -0.4737 ? -0.0647 ? -0.9155 ? -0.3254 ? 0.0694 ? 0.0479 ? 
2 'X-RAY DIFFRACTION' ? refined 9.1023  -15.8645 28.5081 0.1360 ? -0.0244 ? 0.0020  ? 0.1693 ? 0.1105 ? 0.1638 ? 4.4812 ? 0.2570  
? 0.0882  ? 3.2525 ? -0.9318 ? 5.6716 ? -0.3445 ? 0.3039  ? -0.2942 ? 0.0188  ? -0.0155 ? 0.1339  ? 0.1115  ? 0.1888 ? 0.3600 ? 
# 
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 
A1IN4 CAK  C N N 1   
A1IN4 CAL  C N N 2   
A1IN4 CAM  C N N 3   
A1IN4 CAN  C N N 4   
A1IN4 CAO  C N N 5   
A1IN4 CAJ  C N N 6   
A1IN4 CAI  C N S 7   
A1IN4 CAB  C N N 8   
A1IN4 OAA  O N N 9   
A1IN4 N    N N N 10  
A1IN4 CAH  C N N 11  
A1IN4 CAG  C N N 12  
A1IN4 CAF  C N N 13  
A1IN4 CB   C N N 14  
A1IN4 CA   C N S 15  
A1IN4 C    C N N 16  
A1IN4 O    O N N 17  
A1IN4 OBB  O N N 18  
A1IN4 CBA  C N N 19  
A1IN4 CAZ  C N N 20  
A1IN4 CAY  C N N 21  
A1IN4 CAX  C N N 22  
A1IN4 CAW  C N N 23  
A1IN4 OAV  O N N 24  
A1IN4 CAU  C Y N 25  
A1IN4 CAR  C Y N 26  
A1IN4 OAS  O N N 27  
A1IN4 CAT  C N N 28  
A1IN4 CAQ  C Y N 29  
A1IN4 CAP  C Y N 30  
A1IN4 CBH  C Y N 31  
A1IN4 CBE  C Y N 32  
A1IN4 OBF  O N N 33  
A1IN4 CBG  C N N 34  
A1IN4 HAK  H N N 35  
A1IN4 HB6  H N N 36  
A1IN4 HAL  H N N 37  
A1IN4 HB7  H N N 38  
A1IN4 HAM  H N N 39  
A1IN4 HB8  H N N 40  
A1IN4 HAN  H N N 41  
A1IN4 HB9  H N N 42  
A1IN4 HCA  H N N 43  
A1IN4 HAO  H N N 44  
A1IN4 HAJ  H N N 45  
A1IN4 HAI  H N N 46  
A1IN4 HAH  H N N 47  
A1IN4 HB5  H N N 48  
A1IN4 HAG  H N N 49  
A1IN4 HB4  H N N 50  
A1IN4 HAF  H N N 51  
A1IN4 HB3  H N N 52  
A1IN4 HB2  H N N 53  
A1IN4 HB1  H N N 54  
A1IN4 HA   H N N 55  
A1IN4 HCH  H N N 56  
A1IN4 HBA  H N N 57  
A1IN4 HCG  H N N 58  
A1IN4 HAZ  H N N 59  
A1IN4 HCF  H N N 60  
A1IN4 HAY  H N N 61  
A1IN4 HCE  H N N 62  
A1IN4 HAX  H N N 63  
A1IN4 HCD  H N N 64  
A1IN4 HAW  H N N 65  
A1IN4 HCC  H N N 66  
A1IN4 HAT  H N N 67  
A1IN4 HCB  H N N 68  
A1IN4 HAQ  H N N 69  
A1IN4 HBH  H N N 70  
A1IN4 HCJ  H N N 71  
A1IN4 HBG  H N N 72  
A1IN4 HCI  H N N 73  
ALA   N    N N N 74  
ALA   CA   C N S 75  
ALA   C    C N N 76  
ALA   O    O N N 77  
ALA   CB   C N N 78  
ALA   OXT  O N N 79  
ALA   H    H N N 80  
ALA   H2   H N N 81  
ALA   HA   H N N 82  
ALA   HB1  H N N 83  
ALA   HB2  H N N 84  
ALA   HB3  H N N 85  
ALA   HXT  H N N 86  
ARG   N    N N N 87  
ARG   CA   C N S 88  
ARG   C    C N N 89  
ARG   O    O N N 90  
ARG   CB   C N N 91  
ARG   CG   C N N 92  
ARG   CD   C N N 93  
ARG   NE   N N N 94  
ARG   CZ   C N N 95  
ARG   NH1  N N N 96  
ARG   NH2  N N N 97  
ARG   OXT  O N N 98  
ARG   H    H N N 99  
ARG   H2   H N N 100 
ARG   HA   H N N 101 
ARG   HB2  H N N 102 
ARG   HB3  H N N 103 
ARG   HG2  H N N 104 
ARG   HG3  H N N 105 
ARG   HD2  H N N 106 
ARG   HD3  H N N 107 
ARG   HE   H N N 108 
ARG   HH11 H N N 109 
ARG   HH12 H N N 110 
ARG   HH21 H N N 111 
ARG   HH22 H N N 112 
ARG   HXT  H N N 113 
ASN   N    N N N 114 
ASN   CA   C N S 115 
ASN   C    C N N 116 
ASN   O    O N N 117 
ASN   CB   C N N 118 
ASN   CG   C N N 119 
ASN   OD1  O N N 120 
ASN   ND2  N N N 121 
ASN   OXT  O N N 122 
ASN   H    H N N 123 
ASN   H2   H N N 124 
ASN   HA   H N N 125 
ASN   HB2  H N N 126 
ASN   HB3  H N N 127 
ASN   HD21 H N N 128 
ASN   HD22 H N N 129 
ASN   HXT  H N N 130 
ASP   N    N N N 131 
ASP   CA   C N S 132 
ASP   C    C N N 133 
ASP   O    O N N 134 
ASP   CB   C N N 135 
ASP   CG   C N N 136 
ASP   OD1  O N N 137 
ASP   OD2  O N N 138 
ASP   OXT  O N N 139 
ASP   H    H N N 140 
ASP   H2   H N N 141 
ASP   HA   H N N 142 
ASP   HB2  H N N 143 
ASP   HB3  H N N 144 
ASP   HD2  H N N 145 
ASP   HXT  H N N 146 
CYS   N    N N N 147 
CYS   CA   C N R 148 
CYS   C    C N N 149 
CYS   O    O N N 150 
CYS   CB   C N N 151 
CYS   SG   S N N 152 
CYS   OXT  O N N 153 
CYS   H    H N N 154 
CYS   H2   H N N 155 
CYS   HA   H N N 156 
CYS   HB2  H N N 157 
CYS   HB3  H N N 158 
CYS   HG   H N N 159 
CYS   HXT  H N N 160 
GLN   N    N N N 161 
GLN   CA   C N S 162 
GLN   C    C N N 163 
GLN   O    O N N 164 
GLN   CB   C N N 165 
GLN   CG   C N N 166 
GLN   CD   C N N 167 
GLN   OE1  O N N 168 
GLN   NE2  N N N 169 
GLN   OXT  O N N 170 
GLN   H    H N N 171 
GLN   H2   H N N 172 
GLN   HA   H N N 173 
GLN   HB2  H N N 174 
GLN   HB3  H N N 175 
GLN   HG2  H N N 176 
GLN   HG3  H N N 177 
GLN   HE21 H N N 178 
GLN   HE22 H N N 179 
GLN   HXT  H N N 180 
GLU   N    N N N 181 
GLU   CA   C N S 182 
GLU   C    C N N 183 
GLU   O    O N N 184 
GLU   CB   C N N 185 
GLU   CG   C N N 186 
GLU   CD   C N N 187 
GLU   OE1  O N N 188 
GLU   OE2  O N N 189 
GLU   OXT  O N N 190 
GLU   H    H N N 191 
GLU   H2   H N N 192 
GLU   HA   H N N 193 
GLU   HB2  H N N 194 
GLU   HB3  H N N 195 
GLU   HG2  H N N 196 
GLU   HG3  H N N 197 
GLU   HE2  H N N 198 
GLU   HXT  H N N 199 
GLY   N    N N N 200 
GLY   CA   C N N 201 
GLY   C    C N N 202 
GLY   O    O N N 203 
GLY   OXT  O N N 204 
GLY   H    H N N 205 
GLY   H2   H N N 206 
GLY   HA2  H N N 207 
GLY   HA3  H N N 208 
GLY   HXT  H N N 209 
HIS   N    N N N 210 
HIS   CA   C N S 211 
HIS   C    C N N 212 
HIS   O    O N N 213 
HIS   CB   C N N 214 
HIS   CG   C Y N 215 
HIS   ND1  N Y N 216 
HIS   CD2  C Y N 217 
HIS   CE1  C Y N 218 
HIS   NE2  N Y N 219 
HIS   OXT  O N N 220 
HIS   H    H N N 221 
HIS   H2   H N N 222 
HIS   HA   H N N 223 
HIS   HB2  H N N 224 
HIS   HB3  H N N 225 
HIS   HD1  H N N 226 
HIS   HD2  H N N 227 
HIS   HE1  H N N 228 
HIS   HE2  H N N 229 
HIS   HXT  H N N 230 
HOH   O    O N N 231 
HOH   H1   H N N 232 
HOH   H2   H N N 233 
ILE   N    N N N 234 
ILE   CA   C N S 235 
ILE   C    C N N 236 
ILE   O    O N N 237 
ILE   CB   C N S 238 
ILE   CG1  C N N 239 
ILE   CG2  C N N 240 
ILE   CD1  C N N 241 
ILE   OXT  O N N 242 
ILE   H    H N N 243 
ILE   H2   H N N 244 
ILE   HA   H N N 245 
ILE   HB   H N N 246 
ILE   HG12 H N N 247 
ILE   HG13 H N N 248 
ILE   HG21 H N N 249 
ILE   HG22 H N N 250 
ILE   HG23 H N N 251 
ILE   HD11 H N N 252 
ILE   HD12 H N N 253 
ILE   HD13 H N N 254 
ILE   HXT  H N N 255 
LEU   N    N N N 256 
LEU   CA   C N S 257 
LEU   C    C N N 258 
LEU   O    O N N 259 
LEU   CB   C N N 260 
LEU   CG   C N N 261 
LEU   CD1  C N N 262 
LEU   CD2  C N N 263 
LEU   OXT  O N N 264 
LEU   H    H N N 265 
LEU   H2   H N N 266 
LEU   HA   H N N 267 
LEU   HB2  H N N 268 
LEU   HB3  H N N 269 
LEU   HG   H N N 270 
LEU   HD11 H N N 271 
LEU   HD12 H N N 272 
LEU   HD13 H N N 273 
LEU   HD21 H N N 274 
LEU   HD22 H N N 275 
LEU   HD23 H N N 276 
LEU   HXT  H N N 277 
LYS   N    N N N 278 
LYS   CA   C N S 279 
LYS   C    C N N 280 
LYS   O    O N N 281 
LYS   CB   C N N 282 
LYS   CG   C N N 283 
LYS   CD   C N N 284 
LYS   CE   C N N 285 
LYS   NZ   N N N 286 
LYS   OXT  O N N 287 
LYS   H    H N N 288 
LYS   H2   H N N 289 
LYS   HA   H N N 290 
LYS   HB2  H N N 291 
LYS   HB3  H N N 292 
LYS   HG2  H N N 293 
LYS   HG3  H N N 294 
LYS   HD2  H N N 295 
LYS   HD3  H N N 296 
LYS   HE2  H N N 297 
LYS   HE3  H N N 298 
LYS   HZ1  H N N 299 
LYS   HZ2  H N N 300 
LYS   HZ3  H N N 301 
LYS   HXT  H N N 302 
MET   N    N N N 303 
MET   CA   C N S 304 
MET   C    C N N 305 
MET   O    O N N 306 
MET   CB   C N N 307 
MET   CG   C N N 308 
MET   SD   S N N 309 
MET   CE   C N N 310 
MET   OXT  O N N 311 
MET   H    H N N 312 
MET   H2   H N N 313 
MET   HA   H N N 314 
MET   HB2  H N N 315 
MET   HB3  H N N 316 
MET   HG2  H N N 317 
MET   HG3  H N N 318 
MET   HE1  H N N 319 
MET   HE2  H N N 320 
MET   HE3  H N N 321 
MET   HXT  H N N 322 
PHE   N    N N N 323 
PHE   CA   C N S 324 
PHE   C    C N N 325 
PHE   O    O N N 326 
PHE   CB   C N N 327 
PHE   CG   C Y N 328 
PHE   CD1  C Y N 329 
PHE   CD2  C Y N 330 
PHE   CE1  C Y N 331 
PHE   CE2  C Y N 332 
PHE   CZ   C Y N 333 
PHE   OXT  O N N 334 
PHE   H    H N N 335 
PHE   H2   H N N 336 
PHE   HA   H N N 337 
PHE   HB2  H N N 338 
PHE   HB3  H N N 339 
PHE   HD1  H N N 340 
PHE   HD2  H N N 341 
PHE   HE1  H N N 342 
PHE   HE2  H N N 343 
PHE   HZ   H N N 344 
PHE   HXT  H N N 345 
PRO   N    N N N 346 
PRO   CA   C N S 347 
PRO   C    C N N 348 
PRO   O    O N N 349 
PRO   CB   C N N 350 
PRO   CG   C N N 351 
PRO   CD   C N N 352 
PRO   OXT  O N N 353 
PRO   H    H N N 354 
PRO   HA   H N N 355 
PRO   HB2  H N N 356 
PRO   HB3  H N N 357 
PRO   HG2  H N N 358 
PRO   HG3  H N N 359 
PRO   HD2  H N N 360 
PRO   HD3  H N N 361 
PRO   HXT  H N N 362 
SER   N    N N N 363 
SER   CA   C N S 364 
SER   C    C N N 365 
SER   O    O N N 366 
SER   CB   C N N 367 
SER   OG   O N N 368 
SER   OXT  O N N 369 
SER   H    H N N 370 
SER   H2   H N N 371 
SER   HA   H N N 372 
SER   HB2  H N N 373 
SER   HB3  H N N 374 
SER   HG   H N N 375 
SER   HXT  H N N 376 
THR   N    N N N 377 
THR   CA   C N S 378 
THR   C    C N N 379 
THR   O    O N N 380 
THR   CB   C N R 381 
THR   OG1  O N N 382 
THR   CG2  C N N 383 
THR   OXT  O N N 384 
THR   H    H N N 385 
THR   H2   H N N 386 
THR   HA   H N N 387 
THR   HB   H N N 388 
THR   HG1  H N N 389 
THR   HG21 H N N 390 
THR   HG22 H N N 391 
THR   HG23 H N N 392 
THR   HXT  H N N 393 
TRP   N    N N N 394 
TRP   CA   C N S 395 
TRP   C    C N N 396 
TRP   O    O N N 397 
TRP   CB   C N N 398 
TRP   CG   C Y N 399 
TRP   CD1  C Y N 400 
TRP   CD2  C Y N 401 
TRP   NE1  N Y N 402 
TRP   CE2  C Y N 403 
TRP   CE3  C Y N 404 
TRP   CZ2  C Y N 405 
TRP   CZ3  C Y N 406 
TRP   CH2  C Y N 407 
TRP   OXT  O N N 408 
TRP   H    H N N 409 
TRP   H2   H N N 410 
TRP   HA   H N N 411 
TRP   HB2  H N N 412 
TRP   HB3  H N N 413 
TRP   HD1  H N N 414 
TRP   HE1  H N N 415 
TRP   HE3  H N N 416 
TRP   HZ2  H N N 417 
TRP   HZ3  H N N 418 
TRP   HH2  H N N 419 
TRP   HXT  H N N 420 
TYR   N    N N N 421 
TYR   CA   C N S 422 
TYR   C    C N N 423 
TYR   O    O N N 424 
TYR   CB   C N N 425 
TYR   CG   C Y N 426 
TYR   CD1  C Y N 427 
TYR   CD2  C Y N 428 
TYR   CE1  C Y N 429 
TYR   CE2  C Y N 430 
TYR   CZ   C Y N 431 
TYR   OH   O N N 432 
TYR   OXT  O N N 433 
TYR   H    H N N 434 
TYR   H2   H N N 435 
TYR   HA   H N N 436 
TYR   HB2  H N N 437 
TYR   HB3  H N N 438 
TYR   HD1  H N N 439 
TYR   HD2  H N N 440 
TYR   HE1  H N N 441 
TYR   HE2  H N N 442 
TYR   HH   H N N 443 
TYR   HXT  H N N 444 
VAL   N    N N N 445 
VAL   CA   C N S 446 
VAL   C    C N N 447 
VAL   O    O N N 448 
VAL   CB   C N N 449 
VAL   CG1  C N N 450 
VAL   CG2  C N N 451 
VAL   OXT  O N N 452 
VAL   H    H N N 453 
VAL   H2   H N N 454 
VAL   HA   H N N 455 
VAL   HB   H N N 456 
VAL   HG11 H N N 457 
VAL   HG12 H N N 458 
VAL   HG13 H N N 459 
VAL   HG21 H N N 460 
VAL   HG22 H N N 461 
VAL   HG23 H N N 462 
VAL   HXT  H N N 463 
# 
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 
A1IN4 CAW OAV  sing N N 1   
A1IN4 CAW CAX  sing N N 2   
A1IN4 OAV CAU  sing N N 3   
A1IN4 CAX CAY  sing N N 4   
A1IN4 OBF CBG  sing N N 5   
A1IN4 OBF CBE  sing N N 6   
A1IN4 CAU CBE  doub Y N 7   
A1IN4 CAU CAR  sing Y N 8   
A1IN4 OAS CAR  sing N N 9   
A1IN4 OAS CAT  sing N N 10  
A1IN4 CAY CAZ  sing N N 11  
A1IN4 CBE CBH  sing Y N 12  
A1IN4 CAR CAQ  doub Y N 13  
A1IN4 CAZ CBA  sing N N 14  
A1IN4 CBH CAP  doub Y N 15  
A1IN4 CBA OBB  sing N N 16  
A1IN4 CAQ CAP  sing Y N 17  
A1IN4 CAP CAI  sing N N 18  
A1IN4 OBB C    sing N N 19  
A1IN4 CAK CAL  sing N N 20  
A1IN4 CAK CAJ  sing N N 21  
A1IN4 CAL CAM  sing N N 22  
A1IN4 CAI CAJ  sing N N 23  
A1IN4 CAI CAB  sing N N 24  
A1IN4 C   O    doub N N 25  
A1IN4 C   CA   sing N N 26  
A1IN4 CAJ CAO  sing N N 27  
A1IN4 CAB OAA  doub N N 28  
A1IN4 CAB N    sing N N 29  
A1IN4 CAH N    sing N N 30  
A1IN4 CAH CAG  sing N N 31  
A1IN4 N   CA   sing N N 32  
A1IN4 CAM CAN  sing N N 33  
A1IN4 CA  CB   sing N N 34  
A1IN4 CAG CAF  sing N N 35  
A1IN4 CAF CB   sing N N 36  
A1IN4 CAO CAN  sing N N 37  
A1IN4 CAK HAK  sing N N 38  
A1IN4 CAK HB6  sing N N 39  
A1IN4 CAL HAL  sing N N 40  
A1IN4 CAL HB7  sing N N 41  
A1IN4 CAM HAM  sing N N 42  
A1IN4 CAM HB8  sing N N 43  
A1IN4 CAN HAN  sing N N 44  
A1IN4 CAN HB9  sing N N 45  
A1IN4 CAO HCA  sing N N 46  
A1IN4 CAO HAO  sing N N 47  
A1IN4 CAJ HAJ  sing N N 48  
A1IN4 CAI HAI  sing N N 49  
A1IN4 CAH HAH  sing N N 50  
A1IN4 CAH HB5  sing N N 51  
A1IN4 CAG HAG  sing N N 52  
A1IN4 CAG HB4  sing N N 53  
A1IN4 CAF HAF  sing N N 54  
A1IN4 CAF HB3  sing N N 55  
A1IN4 CB  HB2  sing N N 56  
A1IN4 CB  HB1  sing N N 57  
A1IN4 CA  HA   sing N N 58  
A1IN4 CBA HCH  sing N N 59  
A1IN4 CBA HBA  sing N N 60  
A1IN4 CAZ HCG  sing N N 61  
A1IN4 CAZ HAZ  sing N N 62  
A1IN4 CAY HCF  sing N N 63  
A1IN4 CAY HAY  sing N N 64  
A1IN4 CAX HCE  sing N N 65  
A1IN4 CAX HAX  sing N N 66  
A1IN4 CAW HCD  sing N N 67  
A1IN4 CAW HAW  sing N N 68  
A1IN4 CAT HCC  sing N N 69  
A1IN4 CAT HAT  sing N N 70  
A1IN4 CAT HCB  sing N N 71  
A1IN4 CAQ HAQ  sing N N 72  
A1IN4 CBH HBH  sing N N 73  
A1IN4 CBG HCJ  sing N N 74  
A1IN4 CBG HBG  sing N N 75  
A1IN4 CBG HCI  sing N N 76  
ALA   N   CA   sing N N 77  
ALA   N   H    sing N N 78  
ALA   N   H2   sing N N 79  
ALA   CA  C    sing N N 80  
ALA   CA  CB   sing N N 81  
ALA   CA  HA   sing N N 82  
ALA   C   O    doub N N 83  
ALA   C   OXT  sing N N 84  
ALA   CB  HB1  sing N N 85  
ALA   CB  HB2  sing N N 86  
ALA   CB  HB3  sing N N 87  
ALA   OXT HXT  sing N N 88  
ARG   N   CA   sing N N 89  
ARG   N   H    sing N N 90  
ARG   N   H2   sing N N 91  
ARG   CA  C    sing N N 92  
ARG   CA  CB   sing N N 93  
ARG   CA  HA   sing N N 94  
ARG   C   O    doub N N 95  
ARG   C   OXT  sing N N 96  
ARG   CB  CG   sing N N 97  
ARG   CB  HB2  sing N N 98  
ARG   CB  HB3  sing N N 99  
ARG   CG  CD   sing N N 100 
ARG   CG  HG2  sing N N 101 
ARG   CG  HG3  sing N N 102 
ARG   CD  NE   sing N N 103 
ARG   CD  HD2  sing N N 104 
ARG   CD  HD3  sing N N 105 
ARG   NE  CZ   sing N N 106 
ARG   NE  HE   sing N N 107 
ARG   CZ  NH1  sing N N 108 
ARG   CZ  NH2  doub N N 109 
ARG   NH1 HH11 sing N N 110 
ARG   NH1 HH12 sing N N 111 
ARG   NH2 HH21 sing N N 112 
ARG   NH2 HH22 sing N N 113 
ARG   OXT HXT  sing N N 114 
ASN   N   CA   sing N N 115 
ASN   N   H    sing N N 116 
ASN   N   H2   sing N N 117 
ASN   CA  C    sing N N 118 
ASN   CA  CB   sing N N 119 
ASN   CA  HA   sing N N 120 
ASN   C   O    doub N N 121 
ASN   C   OXT  sing N N 122 
ASN   CB  CG   sing N N 123 
ASN   CB  HB2  sing N N 124 
ASN   CB  HB3  sing N N 125 
ASN   CG  OD1  doub N N 126 
ASN   CG  ND2  sing N N 127 
ASN   ND2 HD21 sing N N 128 
ASN   ND2 HD22 sing N N 129 
ASN   OXT HXT  sing N N 130 
ASP   N   CA   sing N N 131 
ASP   N   H    sing N N 132 
ASP   N   H2   sing N N 133 
ASP   CA  C    sing N N 134 
ASP   CA  CB   sing N N 135 
ASP   CA  HA   sing N N 136 
ASP   C   O    doub N N 137 
ASP   C   OXT  sing N N 138 
ASP   CB  CG   sing N N 139 
ASP   CB  HB2  sing N N 140 
ASP   CB  HB3  sing N N 141 
ASP   CG  OD1  doub N N 142 
ASP   CG  OD2  sing N N 143 
ASP   OD2 HD2  sing N N 144 
ASP   OXT HXT  sing N N 145 
CYS   N   CA   sing N N 146 
CYS   N   H    sing N N 147 
CYS   N   H2   sing N N 148 
CYS   CA  C    sing N N 149 
CYS   CA  CB   sing N N 150 
CYS   CA  HA   sing N N 151 
CYS   C   O    doub N N 152 
CYS   C   OXT  sing N N 153 
CYS   CB  SG   sing N N 154 
CYS   CB  HB2  sing N N 155 
CYS   CB  HB3  sing N N 156 
CYS   SG  HG   sing N N 157 
CYS   OXT HXT  sing N N 158 
GLN   N   CA   sing N N 159 
GLN   N   H    sing N N 160 
GLN   N   H2   sing N N 161 
GLN   CA  C    sing N N 162 
GLN   CA  CB   sing N N 163 
GLN   CA  HA   sing N N 164 
GLN   C   O    doub N N 165 
GLN   C   OXT  sing N N 166 
GLN   CB  CG   sing N N 167 
GLN   CB  HB2  sing N N 168 
GLN   CB  HB3  sing N N 169 
GLN   CG  CD   sing N N 170 
GLN   CG  HG2  sing N N 171 
GLN   CG  HG3  sing N N 172 
GLN   CD  OE1  doub N N 173 
GLN   CD  NE2  sing N N 174 
GLN   NE2 HE21 sing N N 175 
GLN   NE2 HE22 sing N N 176 
GLN   OXT HXT  sing N N 177 
GLU   N   CA   sing N N 178 
GLU   N   H    sing N N 179 
GLU   N   H2   sing N N 180 
GLU   CA  C    sing N N 181 
GLU   CA  CB   sing N N 182 
GLU   CA  HA   sing N N 183 
GLU   C   O    doub N N 184 
GLU   C   OXT  sing N N 185 
GLU   CB  CG   sing N N 186 
GLU   CB  HB2  sing N N 187 
GLU   CB  HB3  sing N N 188 
GLU   CG  CD   sing N N 189 
GLU   CG  HG2  sing N N 190 
GLU   CG  HG3  sing N N 191 
GLU   CD  OE1  doub N N 192 
GLU   CD  OE2  sing N N 193 
GLU   OE2 HE2  sing N N 194 
GLU   OXT HXT  sing N N 195 
GLY   N   CA   sing N N 196 
GLY   N   H    sing N N 197 
GLY   N   H2   sing N N 198 
GLY   CA  C    sing N N 199 
GLY   CA  HA2  sing N N 200 
GLY   CA  HA3  sing N N 201 
GLY   C   O    doub N N 202 
GLY   C   OXT  sing N N 203 
GLY   OXT HXT  sing N N 204 
HIS   N   CA   sing N N 205 
HIS   N   H    sing N N 206 
HIS   N   H2   sing N N 207 
HIS   CA  C    sing N N 208 
HIS   CA  CB   sing N N 209 
HIS   CA  HA   sing N N 210 
HIS   C   O    doub N N 211 
HIS   C   OXT  sing N N 212 
HIS   CB  CG   sing N N 213 
HIS   CB  HB2  sing N N 214 
HIS   CB  HB3  sing N N 215 
HIS   CG  ND1  sing Y N 216 
HIS   CG  CD2  doub Y N 217 
HIS   ND1 CE1  doub Y N 218 
HIS   ND1 HD1  sing N N 219 
HIS   CD2 NE2  sing Y N 220 
HIS   CD2 HD2  sing N N 221 
HIS   CE1 NE2  sing Y N 222 
HIS   CE1 HE1  sing N N 223 
HIS   NE2 HE2  sing N N 224 
HIS   OXT HXT  sing N N 225 
HOH   O   H1   sing N N 226 
HOH   O   H2   sing N N 227 
ILE   N   CA   sing N N 228 
ILE   N   H    sing N N 229 
ILE   N   H2   sing N N 230 
ILE   CA  C    sing N N 231 
ILE   CA  CB   sing N N 232 
ILE   CA  HA   sing N N 233 
ILE   C   O    doub N N 234 
ILE   C   OXT  sing N N 235 
ILE   CB  CG1  sing N N 236 
ILE   CB  CG2  sing N N 237 
ILE   CB  HB   sing N N 238 
ILE   CG1 CD1  sing N N 239 
ILE   CG1 HG12 sing N N 240 
ILE   CG1 HG13 sing N N 241 
ILE   CG2 HG21 sing N N 242 
ILE   CG2 HG22 sing N N 243 
ILE   CG2 HG23 sing N N 244 
ILE   CD1 HD11 sing N N 245 
ILE   CD1 HD12 sing N N 246 
ILE   CD1 HD13 sing N N 247 
ILE   OXT HXT  sing N N 248 
LEU   N   CA   sing N N 249 
LEU   N   H    sing N N 250 
LEU   N   H2   sing N N 251 
LEU   CA  C    sing N N 252 
LEU   CA  CB   sing N N 253 
LEU   CA  HA   sing N N 254 
LEU   C   O    doub N N 255 
LEU   C   OXT  sing N N 256 
LEU   CB  CG   sing N N 257 
LEU   CB  HB2  sing N N 258 
LEU   CB  HB3  sing N N 259 
LEU   CG  CD1  sing N N 260 
LEU   CG  CD2  sing N N 261 
LEU   CG  HG   sing N N 262 
LEU   CD1 HD11 sing N N 263 
LEU   CD1 HD12 sing N N 264 
LEU   CD1 HD13 sing N N 265 
LEU   CD2 HD21 sing N N 266 
LEU   CD2 HD22 sing N N 267 
LEU   CD2 HD23 sing N N 268 
LEU   OXT HXT  sing N N 269 
LYS   N   CA   sing N N 270 
LYS   N   H    sing N N 271 
LYS   N   H2   sing N N 272 
LYS   CA  C    sing N N 273 
LYS   CA  CB   sing N N 274 
LYS   CA  HA   sing N N 275 
LYS   C   O    doub N N 276 
LYS   C   OXT  sing N N 277 
LYS   CB  CG   sing N N 278 
LYS   CB  HB2  sing N N 279 
LYS   CB  HB3  sing N N 280 
LYS   CG  CD   sing N N 281 
LYS   CG  HG2  sing N N 282 
LYS   CG  HG3  sing N N 283 
LYS   CD  CE   sing N N 284 
LYS   CD  HD2  sing N N 285 
LYS   CD  HD3  sing N N 286 
LYS   CE  NZ   sing N N 287 
LYS   CE  HE2  sing N N 288 
LYS   CE  HE3  sing N N 289 
LYS   NZ  HZ1  sing N N 290 
LYS   NZ  HZ2  sing N N 291 
LYS   NZ  HZ3  sing N N 292 
LYS   OXT HXT  sing N N 293 
MET   N   CA   sing N N 294 
MET   N   H    sing N N 295 
MET   N   H2   sing N N 296 
MET   CA  C    sing N N 297 
MET   CA  CB   sing N N 298 
MET   CA  HA   sing N N 299 
MET   C   O    doub N N 300 
MET   C   OXT  sing N N 301 
MET   CB  CG   sing N N 302 
MET   CB  HB2  sing N N 303 
MET   CB  HB3  sing N N 304 
MET   CG  SD   sing N N 305 
MET   CG  HG2  sing N N 306 
MET   CG  HG3  sing N N 307 
MET   SD  CE   sing N N 308 
MET   CE  HE1  sing N N 309 
MET   CE  HE2  sing N N 310 
MET   CE  HE3  sing N N 311 
MET   OXT HXT  sing N N 312 
PHE   N   CA   sing N N 313 
PHE   N   H    sing N N 314 
PHE   N   H2   sing N N 315 
PHE   CA  C    sing N N 316 
PHE   CA  CB   sing N N 317 
PHE   CA  HA   sing N N 318 
PHE   C   O    doub N N 319 
PHE   C   OXT  sing N N 320 
PHE   CB  CG   sing N N 321 
PHE   CB  HB2  sing N N 322 
PHE   CB  HB3  sing N N 323 
PHE   CG  CD1  doub Y N 324 
PHE   CG  CD2  sing Y N 325 
PHE   CD1 CE1  sing Y N 326 
PHE   CD1 HD1  sing N N 327 
PHE   CD2 CE2  doub Y N 328 
PHE   CD2 HD2  sing N N 329 
PHE   CE1 CZ   doub Y N 330 
PHE   CE1 HE1  sing N N 331 
PHE   CE2 CZ   sing Y N 332 
PHE   CE2 HE2  sing N N 333 
PHE   CZ  HZ   sing N N 334 
PHE   OXT HXT  sing N N 335 
PRO   N   CA   sing N N 336 
PRO   N   CD   sing N N 337 
PRO   N   H    sing N N 338 
PRO   CA  C    sing N N 339 
PRO   CA  CB   sing N N 340 
PRO   CA  HA   sing N N 341 
PRO   C   O    doub N N 342 
PRO   C   OXT  sing N N 343 
PRO   CB  CG   sing N N 344 
PRO   CB  HB2  sing N N 345 
PRO   CB  HB3  sing N N 346 
PRO   CG  CD   sing N N 347 
PRO   CG  HG2  sing N N 348 
PRO   CG  HG3  sing N N 349 
PRO   CD  HD2  sing N N 350 
PRO   CD  HD3  sing N N 351 
PRO   OXT HXT  sing N N 352 
SER   N   CA   sing N N 353 
SER   N   H    sing N N 354 
SER   N   H2   sing N N 355 
SER   CA  C    sing N N 356 
SER   CA  CB   sing N N 357 
SER   CA  HA   sing N N 358 
SER   C   O    doub N N 359 
SER   C   OXT  sing N N 360 
SER   CB  OG   sing N N 361 
SER   CB  HB2  sing N N 362 
SER   CB  HB3  sing N N 363 
SER   OG  HG   sing N N 364 
SER   OXT HXT  sing N N 365 
THR   N   CA   sing N N 366 
THR   N   H    sing N N 367 
THR   N   H2   sing N N 368 
THR   CA  C    sing N N 369 
THR   CA  CB   sing N N 370 
THR   CA  HA   sing N N 371 
THR   C   O    doub N N 372 
THR   C   OXT  sing N N 373 
THR   CB  OG1  sing N N 374 
THR   CB  CG2  sing N N 375 
THR   CB  HB   sing N N 376 
THR   OG1 HG1  sing N N 377 
THR   CG2 HG21 sing N N 378 
THR   CG2 HG22 sing N N 379 
THR   CG2 HG23 sing N N 380 
THR   OXT HXT  sing N N 381 
TRP   N   CA   sing N N 382 
TRP   N   H    sing N N 383 
TRP   N   H2   sing N N 384 
TRP   CA  C    sing N N 385 
TRP   CA  CB   sing N N 386 
TRP   CA  HA   sing N N 387 
TRP   C   O    doub N N 388 
TRP   C   OXT  sing N N 389 
TRP   CB  CG   sing N N 390 
TRP   CB  HB2  sing N N 391 
TRP   CB  HB3  sing N N 392 
TRP   CG  CD1  doub Y N 393 
TRP   CG  CD2  sing Y N 394 
TRP   CD1 NE1  sing Y N 395 
TRP   CD1 HD1  sing N N 396 
TRP   CD2 CE2  doub Y N 397 
TRP   CD2 CE3  sing Y N 398 
TRP   NE1 CE2  sing Y N 399 
TRP   NE1 HE1  sing N N 400 
TRP   CE2 CZ2  sing Y N 401 
TRP   CE3 CZ3  doub Y N 402 
TRP   CE3 HE3  sing N N 403 
TRP   CZ2 CH2  doub Y N 404 
TRP   CZ2 HZ2  sing N N 405 
TRP   CZ3 CH2  sing Y N 406 
TRP   CZ3 HZ3  sing N N 407 
TRP   CH2 HH2  sing N N 408 
TRP   OXT HXT  sing N N 409 
TYR   N   CA   sing N N 410 
TYR   N   H    sing N N 411 
TYR   N   H2   sing N N 412 
TYR   CA  C    sing N N 413 
TYR   CA  CB   sing N N 414 
TYR   CA  HA   sing N N 415 
TYR   C   O    doub N N 416 
TYR   C   OXT  sing N N 417 
TYR   CB  CG   sing N N 418 
TYR   CB  HB2  sing N N 419 
TYR   CB  HB3  sing N N 420 
TYR   CG  CD1  doub Y N 421 
TYR   CG  CD2  sing Y N 422 
TYR   CD1 CE1  sing Y N 423 
TYR   CD1 HD1  sing N N 424 
TYR   CD2 CE2  doub Y N 425 
TYR   CD2 HD2  sing N N 426 
TYR   CE1 CZ   doub Y N 427 
TYR   CE1 HE1  sing N N 428 
TYR   CE2 CZ   sing Y N 429 
TYR   CE2 HE2  sing N N 430 
TYR   CZ  OH   sing N N 431 
TYR   OH  HH   sing N N 432 
TYR   OXT HXT  sing N N 433 
VAL   N   CA   sing N N 434 
VAL   N   H    sing N N 435 
VAL   N   H2   sing N N 436 
VAL   CA  C    sing N N 437 
VAL   CA  CB   sing N N 438 
VAL   CA  HA   sing N N 439 
VAL   C   O    doub N N 440 
VAL   C   OXT  sing N N 441 
VAL   CB  CG1  sing N N 442 
VAL   CB  CG2  sing N N 443 
VAL   CB  HB   sing N N 444 
VAL   CG1 HG11 sing N N 445 
VAL   CG1 HG12 sing N N 446 
VAL   CG1 HG13 sing N N 447 
VAL   CG2 HG21 sing N N 448 
VAL   CG2 HG22 sing N N 449 
VAL   CG2 HG23 sing N N 450 
VAL   OXT HXT  sing N N 451 
# 
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                    9GQ6 
_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]   0.020474 
_atom_sites.fract_transf_matrix[1][2]   0.011821 
_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]   0.023641 
_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]   0.005148 
_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   ? 15.745 15.338  -5.805  1   73.435  ? 13  GLY   B N    1 ? 1 
ATOM   2    C CA   . GLY   A 1 1   ? 17.11  14.786  -5.893  1   76.725  ? 13  GLY   B CA   1 ? 1 
ATOM   3    C C    . GLY   A 1 1   ? 17.088 13.267  -5.787  1   72.054  ? 13  GLY   B C    1 ? 1 
ATOM   4    O O    . GLY   A 1 1   ? 16.284 12.61   -6.435  1   70.528  ? 13  GLY   B O    1 ? 1 
ATOM   5    H H1   . GLY   A 1 1   ? 15.779 16.24   -5.749  1   76.805  ? 13  GLY   B H1   1 c 1 
ATOM   6    H H2   . GLY   A 1 1   ? 15.323 15.014  -5.073  1   71.99   ? 13  GLY   B H2   1 c 1 
ATOM   7    H H3   . GLY   A 1 1   ? 15.271 15.108  -6.542  1   74.994  ? 13  GLY   B H3   1 c 1 
ATOM   8    H HA2  . GLY   A 1 1   ? 17.514 15.054  -6.751  1   78.729  ? 13  GLY   B HA2  1 c 1 
ATOM   9    H HA3  . GLY   A 1 1   ? 17.658 15.163  -5.165  1   76.012  ? 13  GLY   B HA3  1 c 1 
ATOM   10   N N    . ALA   A 1 2   ? 17.94  12.712  -4.926  1   71.582  ? 14  ALA   B N    1 ? 1 
ATOM   11   C CA   . ALA   A 1 2   ? 18.201 11.287  -4.93   1   66.297  ? 14  ALA   B CA   1 ? 1 
ATOM   12   C C    . ALA   A 1 2   ? 16.93  10.481  -4.639  1   64.423  ? 14  ALA   B C    1 ? 1 
ATOM   13   O O    . ALA   A 1 2   ? 16.702 9.45    -5.302  1   61.732  ? 14  ALA   B O    1 ? 1 
ATOM   14   C CB   . ALA   A 1 2   ? 19.308 10.957  -3.945  1   66.416  ? 14  ALA   B CB   1 ? 1 
ATOM   15   H H    . ALA   A 1 2   ? 18.372 13.238  -4.317  1   71.311  ? 14  ALA   B H    1 c 1 
ATOM   16   H HA   . ALA   A 1 2   ? 18.511 11.04   -5.845  1   68.87   ? 14  ALA   B HA   1 c 1 
ATOM   17   H HB1  . ALA   A 1 2   ? 20.112 11.451  -4.179  1   68.689  ? 14  ALA   B HB1  1 c 1 
ATOM   18   H HB2  . ALA   A 1 2   ? 19.033 11.202  -3.046  1   64.873  ? 14  ALA   B HB2  1 c 1 
ATOM   19   H HB3  . ALA   A 1 2   ? 19.498 10.004  -3.973  1   64.593  ? 14  ALA   B HB3  1 c 1 
ATOM   20   N N    . PRO   A 1 3   ? 16.094 10.885  -3.643  1   58.406  ? 15  PRO   B N    1 ? 1 
ATOM   21   C CA   . PRO   A 1 3   ? 14.854 10.18   -3.343  1   60.785  ? 15  PRO   B CA   1 ? 1 
ATOM   22   C C    . PRO   A 1 3   ? 13.823 10.181  -4.474  1   58.667  ? 15  PRO   B C    1 ? 1 
ATOM   23   O O    . PRO   A 1 3   ? 13.192 9.15    -4.737  1   54.992  ? 15  PRO   B O    1 ? 1 
ATOM   24   C CB   . PRO   A 1 3   ? 14.305 10.833  -2.056  1   60.011  ? 15  PRO   B CB   1 ? 1 
ATOM   25   C CG   . PRO   A 1 3   ? 15.485 11.641  -1.532  1   64.102  ? 15  PRO   B CG   1 ? 1 
ATOM   26   C CD   . PRO   A 1 3   ? 16.287 12.042  -2.751  1   64.222  ? 15  PRO   B CD   1 ? 1 
ATOM   27   H HA   . PRO   A 1 3   ? 15.076 9.249   -3.133  1   57.416  ? 15  PRO   B HA   1 c 1 
ATOM   28   H HB2  . PRO   A 1 3   ? 13.544 11.414  -2.254  1   61.545  ? 15  PRO   B HB2  1 c 1 
ATOM   29   H HB3  . PRO   A 1 3   ? 14.03  10.154  -1.409  1   58.468  ? 15  PRO   B HB3  1 c 1 
ATOM   30   H HG2  . PRO   A 1 3   ? 15.175 12.434  -1.051  1   63.735  ? 15  PRO   B HG2  1 c 1 
ATOM   31   H HG3  . PRO   A 1 3   ? 16.031 11.101  -0.927  1   61.553  ? 15  PRO   B HG3  1 c 1 
ATOM   32   H HD2  . PRO   A 1 3   ? 15.94  12.856  -3.155  1   65.811  ? 15  PRO   B HD2  1 c 1 
ATOM   33   H HD3  . PRO   A 1 3   ? 17.227 12.164  -2.529  1   64.523  ? 15  PRO   B HD3  1 c 1 
ATOM   34   N N    . ALA   A 1 4   ? 13.627 11.324  -5.106  1   61.755  ? 16  ALA   B N    1 ? 1 
ATOM   35   C CA   . ALA   A 1 4   ? 12.698 11.407  -6.22   1   66.964  ? 16  ALA   B CA   1 ? 1 
ATOM   36   C C    . ALA   A 1 4   ? 13.146 10.531  -7.4    1   68.274  ? 16  ALA   B C    1 ? 1 
ATOM   37   O O    . ALA   A 1 4   ? 12.301 9.965   -8.085  1   64.427  ? 16  ALA   B O    1 ? 1 
ATOM   38   C CB   . ALA   A 1 4   ? 12.537 12.847  -6.63   1   70.846  ? 16  ALA   B CB   1 ? 1 
ATOM   39   H H    . ALA   A 1 4   ? 14.076 12.075  -4.842  1   63.542  ? 16  ALA   B H    1 c 1 
ATOM   40   H HA   . ALA   A 1 4   ? 11.815 11.066  -5.907  1   65.113  ? 16  ALA   B HA   1 c 1 
ATOM   41   H HB1  . ALA   A 1 4   ? 12.204 13.366  -5.878  1   70.241  ? 16  ALA   B HB1  1 c 1 
ATOM   42   H HB2  . ALA   A 1 4   ? 13.396 13.204  -6.911  1   72.344  ? 16  ALA   B HB2  1 c 1 
ATOM   43   H HB3  . ALA   A 1 4   ? 11.907 12.909  -7.367  1   72.565  ? 16  ALA   B HB3  1 c 1 
ATOM   44   N N    . THR   A 1 5   ? 14.461 10.453  -7.664  1   66.702  ? 17  THR   B N    1 ? 1 
ATOM   45   C CA   . THR   A 1 5   ? 15.009 9.599   -8.718  1   65.801  ? 17  THR   B CA   1 ? 1 
ATOM   46   C C    . THR   A 1 5   ? 14.689 8.133   -8.374  1   58.752  ? 17  THR   B C    1 ? 1 
ATOM   47   O O    . THR   A 1 5   ? 14.557 7.286   -9.256  1   56.137  ? 17  THR   B O    1 ? 1 
ATOM   48   C CB   . THR   A 1 5   ? 16.524 9.816   -8.893  1   64.826  ? 17  THR   B CB   1 ? 1 
ATOM   49   O OG1  . THR   A 1 5   ? 16.846 11.104  -9.414  1   66.859  ? 17  THR   B OG1  1 ? 1 
ATOM   50   C CG2  . THR   A 1 5   ? 17.177 8.846   -9.87   1   65.259  ? 17  THR   B CG2  1 ? 1 
ATOM   51   H H    . THR   A 1 5   ? 15.04  10.96   -7.171  1   66.543  ? 17  THR   B H    1 c 1 
ATOM   52   H HA   . THR   A 1 5   ? 14.562 9.828   -9.562  1   67.447  ? 17  THR   B HA   1 c 1 
ATOM   53   H HB   . THR   A 1 5   ? 16.963 9.71    -8.015  1   62.609  ? 17  THR   B HB   1 c 1 
ATOM   54   H HG1  . THR   A 1 5   ? 16.573 11.343  -9.991  0   30      ? 17  THR   B HG1  1 c 1 
ATOM   55   H HG21 . THR   A 1 5   ? 18.106 9.099   -10.008 1   67.25   ? 17  THR   B HG21 1 c 1 
ATOM   56   H HG22 . THR   A 1 5   ? 16.705 8.873   -10.72  1   67.758  ? 17  THR   B HG22 1 c 1 
ATOM   57   H HG23 . THR   A 1 5   ? 17.141 7.945   -9.51   1   63.26   ? 17  THR   B HG23 1 c 1 
ATOM   58   N N    . VAL   A 1 6   ? 14.573 7.806   -7.095  1   56.951  ? 18  VAL   B N    1 ? 1 
ATOM   59   C CA   . VAL   A 1 6   ? 14.258 6.434   -6.725  1   56.314  ? 18  VAL   B CA   1 ? 1 
ATOM   60   C C    . VAL   A 1 6   ? 12.766 6.15    -6.922  1   56.035  ? 18  VAL   B C    1 ? 1 
ATOM   61   O O    . VAL   A 1 6   ? 12.416 5.127   -7.513  1   52.67   ? 18  VAL   B O    1 ? 1 
ATOM   62   C CB   . VAL   A 1 6   ? 14.754 6.065   -5.326  1   51.673  ? 18  VAL   B CB   1 ? 1 
ATOM   63   C CG1  . VAL   A 1 6   ? 14.307 4.656   -4.946  1   52.053  ? 18  VAL   B CG1  1 ? 1 
ATOM   64   C CG2  . VAL   A 1 6   ? 16.273 6.175   -5.266  1   50.127  ? 18  VAL   B CG2  1 ? 1 
ATOM   65   H H    . VAL   A 1 6   ? 14.712 8.427   -6.44   1   56.407  ? 18  VAL   B H    1 c 1 
ATOM   66   H HA   . VAL   A 1 6   ? 14.736 5.856   -7.348  1   56.497  ? 18  VAL   B HA   1 c 1 
ATOM   67   H HB   . VAL   A 1 6   ? 14.362 6.708   -4.69   1   51.26   ? 18  VAL   B HB   1 c 1 
ATOM   68   H HG11 . VAL   A 1 6   ? 14.509 4.044   -5.673  1   52.405  ? 18  VAL   B HG11 1 c 1 
ATOM   69   H HG12 . VAL   A 1 6   ? 13.349 4.652   -4.777  1   50.941  ? 18  VAL   B HG12 1 c 1 
ATOM   70   H HG13 . VAL   A 1 6   ? 14.777 4.372   -4.144  1   49.801  ? 18  VAL   B HG13 1 c 1 
ATOM   71   H HG21 . VAL   A 1 6   ? 16.563 6.141   -4.339  1   49.262  ? 18  VAL   B HG21 1 c 1 
ATOM   72   H HG22 . VAL   A 1 6   ? 16.556 7.014   -5.662  1   52.794  ? 18  VAL   B HG22 1 c 1 
ATOM   73   H HG23 . VAL   A 1 6   ? 16.671 5.436   -5.755  1   51.3    ? 18  VAL   B HG23 1 c 1 
ATOM   74   N N    . THR   A 1 7   ? 11.899 7.065   -6.474  1   54.812  ? 19  THR   B N    1 ? 1 
ATOM   75   C CA   . THR   A 1 7   ? 10.506 7.068   -6.895  1   59.307  ? 19  THR   B CA   1 ? 1 
ATOM   76   C C    . THR   A 1 7   ? 10.405 6.817   -8.405  1   62.371  ? 19  THR   B C    1 ? 1 
ATOM   77   O O    . THR   A 1 7   ? 9.648  5.958   -8.815  1   65.827  ? 19  THR   B O    1 ? 1 
ATOM   78   C CB   . THR   A 1 7   ? 9.832  8.383   -6.524  1   61.859  ? 19  THR   B CB   1 ? 1 
ATOM   79   O OG1  . THR   A 1 7   ? 9.81   8.331   -5.102  1   57.125  ? 19  THR   B OG1  1 ? 1 
ATOM   80   C CG2  . THR   A 1 7   ? 8.464  8.541   -7.17   1   65.547  ? 19  THR   B CG2  1 ? 1 
ATOM   81   H H    . THR   A 1 7   ? 12.183 7.703   -5.884  1   55.15   ? 19  THR   B H    1 c 1 
ATOM   82   H HA   . THR   A 1 7   ? 10.044 6.339   -6.425  1   57.456  ? 19  THR   B HA   1 c 1 
ATOM   83   H HB   . THR   A 1 7   ? 10.402 9.136   -6.808  1   62.683  ? 19  THR   B HB   1 c 1 
ATOM   84   H HG1  . THR   A 1 7   ? 9.365  7.595   -4.828  0   30      ? 19  THR   B HG1  1 c 1 
ATOM   85   H HG21 . THR   A 1 7   ? 7.989  9.277   -6.748  1   65.542  ? 19  THR   B HG21 1 c 1 
ATOM   86   H HG22 . THR   A 1 7   ? 7.954  7.721   -7.057  1   64.557  ? 19  THR   B HG22 1 c 1 
ATOM   87   H HG23 . THR   A 1 7   ? 8.569  8.729   -8.118  1   67.691  ? 19  THR   B HG23 1 c 1 
ATOM   88   N N    . GLU   A 1 8   ? 11.197 7.525   -9.221  1   66.378  ? 20  GLU   B N    1 ? 1 
ATOM   89   C CA   . GLU   A 1 8   ? 11.02  7.524   -10.662 1   73.227  ? 20  GLU   B CA   1 ? 1 
ATOM   90   C C    . GLU   A 1 8   ? 11.62  6.273   -11.313 1   73.477  ? 20  GLU   B C    1 ? 1 
ATOM   91   O O    . GLU   A 1 8   ? 11.026 5.773   -12.254 1   74.166  ? 20  GLU   B O    1 ? 1 
ATOM   92   C CB   . GLU   A 1 8   ? 11.653 8.735   -11.352 1   78.281  ? 20  GLU   B CB   1 ? 1 
ATOM   93   C CG   . GLU   A 1 8   ? 11.258 10.089  -10.772 1   76.858  ? 20  GLU   B CG   1 ? 1 
ATOM   94   C CD   . GLU   A 1 8   ? 12.097 11.276  -11.263 1   82.623  ? 20  GLU   B CD   1 ? 1 
ATOM   95   O OE1  . GLU   A 1 8   ? 12.895 11.183  -12.246 1   82.902  ? 20  GLU   B OE1  1 ? 1 
ATOM   96   O OE2  . GLU   A 1 8   ? 11.919 12.342  -10.635 1   85.329  ? 20  GLU   B OE2  1 ? 1 
ATOM   97   H H    . GLU   A 1 8   ? 11.87  8.028   -8.863  1   65.931  ? 20  GLU   B H    1 c 1 
ATOM   98   H HA   . GLU   A 1 8   ? 10.048 7.54    -10.853 1   74.008  ? 20  GLU   B HA   1 c 1 
ATOM   99   H HB2  . GLU   A 1 8   ? 12.628 8.65    -11.3   1   77.074  ? 20  GLU   B HB2  1 c 1 
ATOM   100  H HB3  . GLU   A 1 8   ? 11.404 8.72    -12.3   1   80.686  ? 20  GLU   B HB3  1 c 1 
ATOM   101  H HG2  . GLU   A 1 8   ? 10.319 10.265  -10.996 1   79.078  ? 20  GLU   B HG2  1 c 1 
ATOM   102  H HG3  . GLU   A 1 8   ? 11.318 10.051  -9.798  1   74.75   ? 20  GLU   B HG3  1 c 1 
ATOM   103  N N    . GLN   A 1 9   ? 12.82  5.848   -10.886 1   65.2    ? 21  GLN   B N    1 ? 1 
ATOM   104  C CA   . GLN   A 1 9   ? 13.627 4.877   -11.626 1   69.722  ? 21  GLN   B CA   1 ? 1 
ATOM   105  C C    . GLN   A 1 9   ? 13.873 3.622   -10.779 1   64.499  ? 21  GLN   B C    1 ? 1 
ATOM   106  O O    . GLN   A 1 9   ? 14.498 2.68    -11.249 1   68.659  ? 21  GLN   B O    1 ? 1 
ATOM   107  C CB   . GLN   A 1 9   ? 15.034 5.365   -12.031 1   73.569  ? 21  GLN   B CB   1 ? 1 
ATOM   108  C CG   . GLN   A 1 9   ? 15.138 6.828   -12.462 1   78.973  ? 21  GLN   B CG   1 ? 1 
ATOM   109  C CD   . GLN   A 1 9   ? 14.269 7.136   -13.649 1   89.248  ? 21  GLN   B CD   1 ? 1 
ATOM   110  O OE1  . GLN   A 1 9   ? 13.755 6.214   -14.293 1   95.454  ? 21  GLN   B OE1  1 ? 1 
ATOM   111  N NE2  . GLN   A 1 9   ? 14.118 8.422   -13.964 1   96.071  ? 21  GLN   B NE2  1 ? 1 
ATOM   112  H H    . GLN   A 1 9   ? 13.16  6.196   -10.113 1   65.197  ? 21  GLN   B H    1 c 1 
ATOM   113  H HA   . GLN   A 1 9   ? 13.133 4.612   -12.442 1   71.806  ? 21  GLN   B HA   1 c 1 
ATOM   114  H HB2  . GLN   A 1 9   ? 15.638 5.223   -11.272 1   71.277  ? 21  GLN   B HB2  1 c 1 
ATOM   115  H HB3  . GLN   A 1 9   ? 15.353 4.8     -12.765 1   75.857  ? 21  GLN   B HB3  1 c 1 
ATOM   116  H HG2  . GLN   A 1 9   ? 14.875 7.408   -11.717 1   77.579  ? 21  GLN   B HG2  1 c 1 
ATOM   117  H HG3  . GLN   A 1 9   ? 16.07  7.035   -12.688 1   81.013  ? 21  GLN   B HG3  1 c 1 
ATOM   118  H HE21 . GLN   A 1 9   ? 13.607 8.652   -14.652 1   97.57   ? 21  GLN   B HE21 1 c 1 
ATOM   119  H HE22 . GLN   A 1 9   ? 14.527 9.047   -13.485 1   93.888  ? 21  GLN   B HE22 1 c 1 
ATOM   120  N N    . GLY   A 1 10  ? 13.405 3.608   -9.532  1   60.529  ? 22  GLY   B N    1 ? 1 
ATOM   121  C CA   . GLY   A 1 10  ? 13.778 2.548   -8.595  1   57.704  ? 22  GLY   B CA   1 ? 1 
ATOM   122  C C    . GLY   A 1 10  ? 13.116 1.225   -8.96   1   57.034  ? 22  GLY   B C    1 ? 1 
ATOM   123  O O    . GLY   A 1 10  ? 11.973 1.219   -9.389  1   55.247  ? 22  GLY   B O    1 ? 1 
ATOM   124  H H    . GLY   A 1 10  ? 12.826 4.257   -9.252  1   60.265  ? 22  GLY   B H    1 c 1 
ATOM   125  H HA2  . GLY   A 1 10  ? 14.758 2.441   -8.604  1   57.342  ? 22  GLY   B HA2  1 c 1 
ATOM   126  H HA3  . GLY   A 1 10  ? 13.51  2.81    -7.685  1   55.075  ? 22  GLY   B HA3  1 c 1 
ATOM   127  N N    . GLU   A 1 11  ? 13.845 0.116   -8.734  1   55.867  ? 23  GLU   B N    1 ? 1 
ATOM   128  C CA   . GLU   A 1 11  ? 13.312 -1.219  -8.909  1   57.908  ? 23  GLU   B CA   1 ? 1 
ATOM   129  C C    . GLU   A 1 11  ? 12.536 -1.572  -7.646  1   52.325  ? 23  GLU   B C    1 ? 1 
ATOM   130  O O    . GLU   A 1 11  ? 13.042 -1.369  -6.536  1   47.961  ? 23  GLU   B O    1 ? 1 
ATOM   131  C CB   . GLU   A 1 11  ? 14.49  -2.17   -9.165  1   63.215  ? 23  GLU   B CB   1 ? 1 
ATOM   132  C CG   . GLU   A 1 11  ? 14.105 -3.596  -9.55   1   70.026  ? 23  GLU   B CG   1 ? 1 
ATOM   133  C CD   . GLU   A 1 11  ? 15.195 -4.668  -9.367  1   78.05   ? 23  GLU   B CD   1 ? 1 
ATOM   134  O OE1  . GLU   A 1 11  ? 16.369 -4.326  -9.079  1   75.534  ? 23  GLU   B OE1  1 ? 1 
ATOM   135  O OE2  . GLU   A 1 11  ? 14.862 -5.88   -9.446  1   82.809  ? 23  GLU   B OE2  1 ? 1 
ATOM   136  H H    . GLU   A 1 11  ? 14.711 0.205   -8.457  1   55.497  ? 23  GLU   B H    1 c 1 
ATOM   137  H HA   . GLU   A 1 11  ? 12.699 -1.222  -9.688  1   60.164  ? 23  GLU   B HA   1 c 1 
ATOM   138  H HB2  . GLU   A 1 11  ? 15.041 -1.796  -9.884  1   64.957  ? 23  GLU   B HB2  1 c 1 
ATOM   139  H HB3  . GLU   A 1 11  ? 15.042 -2.204  -8.356  1   61.008  ? 23  GLU   B HB3  1 c 1 
ATOM   140  H HG2  . GLU   A 1 11  ? 13.324 -3.864  -9.021  1   69.364  ? 23  GLU   B HG2  1 c 1 
ATOM   141  H HG3  . GLU   A 1 11  ? 13.828 -3.601  -10.491 1   73.278  ? 23  GLU   B HG3  1 c 1 
ATOM   142  N N    . ASP   A 1 12  ? 11.332 -2.129  -7.802  1   50.061  ? 24  ASP   B N    1 ? 1 
ATOM   143  C CA   . ASP   A 1 12  ? 10.56  -2.583  -6.654  1   48.293  ? 24  ASP   B CA   1 ? 1 
ATOM   144  C C    . ASP   A 1 12  ? 11.095 -3.949  -6.266  1   49.854  ? 24  ASP   B C    1 ? 1 
ATOM   145  O O    . ASP   A 1 12  ? 10.902 -4.888  -7.027  1   49.89   ? 24  ASP   B O    1 ? 1 
ATOM   146  C CB   . ASP   A 1 12  ? 9.065  -2.649  -6.94   1   52.39   ? 24  ASP   B CB   1 ? 1 
ATOM   147  C CG   . ASP   A 1 12  ? 8.215  -3.101  -5.756  1   51.115  ? 24  ASP   B CG   1 ? 1 
ATOM   148  O OD1  . ASP   A 1 12  ? 8.789  -3.461  -4.709  1   50.789  ? 24  ASP   B OD1  1 ? 1 
ATOM   149  O OD2  . ASP   A 1 12  ? 6.98   -3.109  -5.879  1   52.124  ? 24  ASP   B OD2  1 ? 1 
ATOM   150  H H    . ASP   A 1 12  ? 10.983 -2.23   -8.64   1   53.474  ? 24  ASP   B H    1 c 1 
ATOM   151  H HA   . ASP   A 1 12  ? 10.706 -1.961  -5.909  1   46.751  ? 24  ASP   B HA   1 c 1 
ATOM   152  H HB2  . ASP   A 1 12  ? 8.758  -1.761  -7.216  1   52.271  ? 24  ASP   B HB2  1 c 1 
ATOM   153  H HB3  . ASP   A 1 12  ? 8.909  -3.267  -7.685  1   54.466  ? 24  ASP   B HB3  1 c 1 
ATOM   154  N N    . ILE   A 1 13  ? 11.761 -4.06   -5.093  1   46.219  ? 25  ILE   B N    1 ? 1 
ATOM   155  C CA   . ILE   A 1 13  ? 12.358 -5.339  -4.68   1   48.348  ? 25  ILE   B CA   1 ? 1 
ATOM   156  C C    . ILE   A 1 13  ? 11.517 -6.04   -3.609  1   48.545  ? 25  ILE   B C    1 ? 1 
ATOM   157  O O    . ILE   A 1 13  ? 11.972 -6.982  -2.962  1   50.654  ? 25  ILE   B O    1 ? 1 
ATOM   158  C CB   . ILE   A 1 13  ? 13.807 -5.127  -4.207  1   45.888  ? 25  ILE   B CB   1 ? 1 
ATOM   159  C CG1  . ILE   A 1 13  ? 13.883 -4.136  -3.065  1   43.939  ? 25  ILE   B CG1  1 ? 1 
ATOM   160  C CG2  . ILE   A 1 13  ? 14.702 -4.675  -5.362  1   46.649  ? 25  ILE   B CG2  1 ? 1 
ATOM   161  C CD1  . ILE   A 1 13  ? 15.269 -4.059  -2.425  1   47.196  ? 25  ILE   B CD1  1 ? 1 
ATOM   162  H H    . ILE   A 1 13  ? 11.828 -3.336  -4.54   1   45.081  ? 25  ILE   B H    1 c 1 
ATOM   163  H HA   . ILE   A 1 13  ? 12.388 -5.922  -5.463  1   50.143  ? 25  ILE   B HA   1 c 1 
ATOM   164  H HB   . ILE   A 1 13  ? 14.146 -5.985  -3.881  1   46.396  ? 25  ILE   B HB   1 c 1 
ATOM   165  H HG12 . ILE   A 1 13  ? 13.643 -3.248  -3.399  1   44.448  ? 25  ILE   B HG12 1 c 1 
ATOM   166  H HG13 . ILE   A 1 13  ? 13.232 -4.387  -2.379  1   44.043  ? 25  ILE   B HG13 1 c 1 
ATOM   167  H HG21 . ILE   A 1 13  ? 15.634 -4.708  -5.087  1   46.398  ? 25  ILE   B HG21 1 c 1 
ATOM   168  H HG22 . ILE   A 1 13  ? 14.473 -3.766  -5.615  1   46.611  ? 25  ILE   B HG22 1 c 1 
ATOM   169  H HG23 . ILE   A 1 13  ? 14.572 -5.264  -6.124  1   49.092  ? 25  ILE   B HG23 1 c 1 
ATOM   170  H HD11 . ILE   A 1 13  ? 15.584 -4.961  -2.226  1   46.346  ? 25  ILE   B HD11 1 c 1 
ATOM   171  H HD12 . ILE   A 1 13  ? 15.217 -3.544  -1.597  1   44.312  ? 25  ILE   B HD12 1 c 1 
ATOM   172  H HD13 . ILE   A 1 13  ? 15.894 -3.625  -3.036  1   46.372  ? 25  ILE   B HD13 1 c 1 
ATOM   173  N N    . THR   A 1 14  ? 10.266 -5.625  -3.418  1   48.803  ? 26  THR   B N    1 ? 1 
ATOM   174  C CA   . THR   A 1 14  ? 9.368  -6.387  -2.55   1   50.111  ? 26  THR   B CA   1 ? 1 
ATOM   175  C C    . THR   A 1 14  ? 8.886  -7.648  -3.278  1   51.51   ? 26  THR   B C    1 ? 1 
ATOM   176  O O    . THR   A 1 14  ? 8.784  -7.672  -4.504  1   50.917  ? 26  THR   B O    1 ? 1 
ATOM   177  C CB   . THR   A 1 14  ? 8.19   -5.552  -2.046  1   48.842  ? 26  THR   B CB   1 ? 1 
ATOM   178  O OG1  . THR   A 1 14  ? 7.385  -5.122  -3.15   1   50.322  ? 26  THR   B OG1  1 ? 1 
ATOM   179  C CG2  . THR   A 1 14  ? 8.676  -4.4    -1.189  1   44.471  ? 26  THR   B CG2  1 ? 1 
ATOM   180  H H    . THR   A 1 14  ? 9.96   -4.864  -3.82   1   48.943  ? 26  THR   B H    1 c 1 
ATOM   181  H HA   . THR   A 1 14  ? 9.885  -6.669  -1.766  1   48.208  ? 26  THR   B HA   1 c 1 
ATOM   182  H HB   . THR   A 1 14  ? 7.637  -6.128  -1.467  1   49.568  ? 26  THR   B HB   1 c 1 
ATOM   183  H HG1  . THR   A 1 14  ? 7.872  -4.674  -3.655  0   30      ? 26  THR   B HG1  1 c 1 
ATOM   184  H HG21 . THR   A 1 14  ? 7.917  -3.87   -0.895  1   44.844  ? 26  THR   B HG21 1 c 1 
ATOM   185  H HG22 . THR   A 1 14  ? 9.278  -3.842  -1.708  1   44.148  ? 26  THR   B HG22 1 c 1 
ATOM   186  H HG23 . THR   A 1 14  ? 9.146  -4.749  -0.413  1   43.775  ? 26  THR   B HG23 1 c 1 
ATOM   187  N N    . SER   A 1 15  ? 8.607  -8.686  -2.483  1   51.921  ? 27  SER   B N    1 ? 1 
ATOM   188  C CA   . SER   A 1 15  ? 7.978  -9.903  -2.962  1   57.614  ? 27  SER   B CA   1 ? 1 
ATOM   189  C C    . SER   A 1 15  ? 6.532  -9.658  -3.351  1   59.402  ? 27  SER   B C    1 ? 1 
ATOM   190  O O    . SER   A 1 15  ? 6.013  -10.29  -4.284  1   61.015  ? 27  SER   B O    1 ? 1 
ATOM   191  C CB   . SER   A 1 15  ? 8.061  -10.982 -1.909  1   60.01   ? 27  SER   B CB   1 ? 1 
ATOM   192  O OG   . SER   A 1 15  ? 9.413  -11.391 -1.802  1   55.301  ? 27  SER   B OG   1 ? 1 
ATOM   193  H H    . SER   A 1 15  ? 8.82   -8.629  -1.596  1   50.821  ? 27  SER   B H    1 c 1 
ATOM   194  H HA   . SER   A 1 15  ? 8.469  -10.211 -3.766  1   58.665  ? 27  SER   B HA   1 c 1 
ATOM   195  H HB2  . SER   A 1 15  ? 7.751  -10.632 -1.052  1   57.314  ? 27  SER   B HB2  1 c 1 
ATOM   196  H HB3  . SER   A 1 15  ? 7.501  -11.736 -2.162  1   61.849  ? 27  SER   B HB3  1 c 1 
ATOM   197  H HG   . SER   A 1 15  ? 9.393  -11.953 -1.083  0   30      ? 27  SER   B HG   1 c 1 
ATOM   198  N N    . LYS   A 1 16  ? 5.889  -8.747  -2.615  1   57.504  ? 28  LYS   B N    1 ? 1 
ATOM   199  C CA   . LYS   A 1 16  ? 4.489  -8.429  -2.849  1   63.866  ? 28  LYS   B CA   1 ? 1 
ATOM   200  C C    . LYS   A 1 16  ? 4.302  -7.418  -3.985  1   62.019  ? 28  LYS   B C    1 ? 1 
ATOM   201  O O    . LYS   A 1 16  ? 3.187  -7.238  -4.435  1   62.159  ? 28  LYS   B O    1 ? 1 
ATOM   202  C CB   . LYS   A 1 16  ? 3.855  -7.874  -1.571  1   66.807  ? 28  LYS   B CB   1 ? 1 
ATOM   203  C CG   . LYS   A 1 16  ? 3.491  -8.901  -0.5    1   71.232  ? 28  LYS   B CG   1 ? 1 
ATOM   204  C CD   . LYS   A 1 16  ? 2.393  -8.387  0.429   1   76.627  ? 28  LYS   B CD   1 ? 1 
ATOM   205  C CE   . LYS   A 1 16  ? 2.912  -7.868  1.731   1   78.733  ? 28  LYS   B CE   1 ? 1 
ATOM   206  N NZ   . LYS   A 1 16  ? 2.969  -8.966  2.706   1   83.424  ? 28  LYS   B NZ   1 ? 1 
ATOM   207  H H    . LYS   A 1 16  ? 6.332  -8.314  -1.942  1   55.689  ? 28  LYS   B H    1 c 1 
ATOM   208  H HA   . LYS   A 1 16  ? 4.016  -9.265  -3.093  1   66.616  ? 28  LYS   B HA   1 c 1 
ATOM   209  H HB2  . LYS   A 1 16  ? 4.472  -7.223  -1.176  1   63.221  ? 28  LYS   B HB2  1 c 1 
ATOM   210  H HB3  . LYS   A 1 16  ? 3.039  -7.39   -1.82   1   67.657  ? 28  LYS   B HB3  1 c 1 
ATOM   211  H HG2  . LYS   A 1 16  ? 3.186  -9.724  -0.939  1   74.61   ? 28  LYS   B HG2  1 c 1 
ATOM   212  H HG3  . LYS   A 1 16  ? 4.293  -9.111  0.026   1   69.724  ? 28  LYS   B HG3  1 c 1 
ATOM   213  H HD2  . LYS   A 1 16  ? 1.896  -7.671  -0.022  1   76.885  ? 28  LYS   B HD2  1 c 1 
ATOM   214  H HD3  . LYS   A 1 16  ? 1.763  -9.119  0.606   1   79.835  ? 28  LYS   B HD3  1 c 1 
ATOM   215  H HE2  . LYS   A 1 16  ? 3.803  -7.493  1.614   1   75.215  ? 28  LYS   B HE2  1 c 1 
ATOM   216  H HE3  . LYS   A 1 16  ? 2.323  -7.17   2.068   1   77.983  ? 28  LYS   B HE3  1 c 1 
ATOM   217  H HZ1  . LYS   A 1 16  ? 3.454  -9.653  2.369   1   82.87   ? 28  LYS   B HZ1  1 c 1 
ATOM   218  H HZ2  . LYS   A 1 16  ? 2.132  -9.256  2.895   1   85.051  ? 28  LYS   B HZ2  1 c 1 
ATOM   219  H HZ3  . LYS   A 1 16  ? 3.36   -8.675  3.47    1   80.522  ? 28  LYS   B HZ3  1 c 1 
ATOM   220  N N    . LYS   A 1 17  ? 5.38   -6.754  -4.429  1   57.918  ? 29  LYS   B N    1 ? 1 
ATOM   221  C CA   . LYS   A 1 17  ? 5.321  -5.763  -5.502  1   59.662  ? 29  LYS   B CA   1 ? 1 
ATOM   222  C C    . LYS   A 1 17  ? 4.37   -4.619  -5.127  1   57.284  ? 29  LYS   B C    1 ? 1 
ATOM   223  O O    . LYS   A 1 17  ? 3.497  -4.207  -5.89   1   57.006  ? 29  LYS   B O    1 ? 1 
ATOM   224  C CB   . LYS   A 1 17  ? 5.021  -6.412  -6.852  1   67.375  ? 29  LYS   B CB   1 ? 1 
ATOM   225  C CG   . LYS   A 1 17  ? 6.11   -7.333  -7.369  1   71.118  ? 29  LYS   B CG   1 ? 1 
ATOM   226  C CD   . LYS   A 1 17  ? 7.341  -6.519  -7.733  1   70.466  ? 29  LYS   B CD   1 ? 1 
ATOM   227  C CE   . LYS   A 1 17  ? 8.386  -7.341  -8.424  1   74.291  ? 29  LYS   B CE   1 ? 1 
ATOM   228  N NZ   . LYS   A 1 17  ? 9.322  -7.86   -7.423  1   71.124  ? 29  LYS   B NZ   1 ? 1 
ATOM   229  H H    . LYS   A 1 17  ? 6.19   -6.919  -4.041  1   56.505  ? 29  LYS   B H    1 c 1 
ATOM   230  H HA   . LYS   A 1 17  ? 6.224  -5.37   -5.577  1   57.556  ? 29  LYS   B HA   1 c 1 
ATOM   231  H HB2  . LYS   A 1 17  ? 4.189  -6.926  -6.779  1   69.762  ? 29  LYS   B HB2  1 c 1 
ATOM   232  H HB3  . LYS   A 1 17  ? 4.875  -5.704  -7.515  1   68.081  ? 29  LYS   B HB3  1 c 1 
ATOM   233  H HG2  . LYS   A 1 17  ? 6.339  -7.987  -6.674  1   69.846  ? 29  LYS   B HG2  1 c 1 
ATOM   234  H HG3  . LYS   A 1 17  ? 5.781  -7.811  -8.161  1   74.382  ? 29  LYS   B HG3  1 c 1 
ATOM   235  H HD2  . LYS   A 1 17  ? 7.074  -5.781  -8.323  1   71.31   ? 29  LYS   B HD2  1 c 1 
ATOM   236  H HD3  . LYS   A 1 17  ? 7.726  -6.131  -6.918  1   67.182  ? 29  LYS   B HD3  1 c 1 
ATOM   237  H HE2  . LYS   A 1 17  ? 7.975  -8.086  -8.899  1   76.914  ? 29  LYS   B HE2  1 c 1 
ATOM   238  H HE3  . LYS   A 1 17  ? 8.871  -6.793  -9.066  1   73.88   ? 29  LYS   B HE3  1 c 1 
ATOM   239  H HZ1  . LYS   A 1 17  ? 8.867  -8.293  -6.769  1   70.975  ? 29  LYS   B HZ1  1 c 1 
ATOM   240  H HZ2  . LYS   A 1 17  ? 9.792  -7.177  -7.056  1   68.533  ? 29  LYS   B HZ2  1 c 1 
ATOM   241  H HZ3  . LYS   A 1 17  ? 9.899  -8.438  -7.814  1   72.463  ? 29  LYS   B HZ3  1 c 1 
ATOM   242  N N    . ASP   A 1 18  ? 4.597  -4.062  -3.946  1   52.729  ? 30  ASP   B N    1 ? 1 
ATOM   243  C CA   . ASP   A 1 18  ? 3.771  -3.004  -3.378  1   53.692  ? 30  ASP   B CA   1 ? 1 
ATOM   244  C C    . ASP   A 1 18  ? 4.551  -1.693  -3.299  1   50.708  ? 30  ASP   B C    1 ? 1 
ATOM   245  O O    . ASP   A 1 18  ? 4.145  -0.801  -2.572  1   50.368  ? 30  ASP   B O    1 ? 1 
ATOM   246  C CB   . ASP   A 1 18  ? 3.239  -3.441  -2.022  1   52.207  ? 30  ASP   B CB   1 ? 1 
ATOM   247  C CG   . ASP   A 1 18  ? 4.274  -3.709  -0.927  1   51.424  ? 30  ASP   B CG   1 ? 1 
ATOM   248  O OD1  . ASP   A 1 18  ? 5.459  -3.346  -1.095  1   45.314  ? 30  ASP   B OD1  1 ? 1 
ATOM   249  O OD2  . ASP   A 1 18  ? 3.886  -4.303  0.099   1   51.684  ? 30  ASP   B OD2  1 ? 1 
ATOM   250  H H    . ASP   A 1 18  ? 5.316  -4.352  -3.462  1   51.436  ? 30  ASP   B H    1 c 1 
ATOM   251  H HA   . ASP   A 1 18  ? 2.994  -2.866  -3.965  1   55.804  ? 30  ASP   B HA   1 c 1 
ATOM   252  H HB2  . ASP   A 1 18  ? 2.623  -2.754  -1.693  1   53.2    ? 30  ASP   B HB2  1 c 1 
ATOM   253  H HB3  . ASP   A 1 18  ? 2.722  -4.264  -2.149  1   55.429  ? 30  ASP   B HB3  1 c 1 
ATOM   254  N N    . ARG   A 1 19  ? 5.695  -1.626  -4.003  1   49.657  ? 31  ARG   B N    1 ? 1 
ATOM   255  C CA   . ARG   A 1 19  ? 6.592  -0.473  -4.015  1   47.255  ? 31  ARG   B CA   1 ? 1 
ATOM   256  C C    . ARG   A 1 19  ? 7.017  -0.059  -2.625  1   45.061  ? 31  ARG   B C    1 ? 1 
ATOM   257  O O    . ARG   A 1 19  ? 7.326  1.118   -2.4    1   42.46   ? 31  ARG   B O    1 ? 1 
ATOM   258  C CB   . ARG   A 1 19  ? 6.01   0.733   -4.777  1   48.784  ? 31  ARG   B CB   1 ? 1 
ATOM   259  C CG   . ARG   A 1 19  ? 5.678  0.371   -6.202  1   50.607  ? 31  ARG   B CG   1 ? 1 
ATOM   260  C CD   . ARG   A 1 19  ? 5.18   1.563   -7.065  1   53.88   ? 31  ARG   B CD   1 ? 1 
ATOM   261  N NE   . ARG   A 1 19  ? 5.968  2.784   -6.875  1   52.5    ? 31  ARG   B NE   1 ? 1 
ATOM   262  C CZ   . ARG   A 1 19  ? 7.024  3.158   -7.628  1   54.484  ? 31  ARG   B CZ   1 ? 1 
ATOM   263  N NH1  . ARG   A 1 19  ? 7.546  2.383   -8.559  1   54.644  ? 31  ARG   B NH1  1 ? 1 
ATOM   264  N NH2  . ARG   A 1 19  ? 7.586  4.36    -7.475  1   57.671  ? 31  ARG   B NH2  1 ? 1 
ATOM   265  H H    . ARG   A 1 19  ? 5.924  -2.344  -4.518  1   50.766  ? 31  ARG   B H    1 c 1 
ATOM   266  H HA   . ARG   A 1 19  ? 7.41   -0.743  -4.502  1   47.268  ? 31  ARG   B HA   1 c 1 
ATOM   267  H HB2  . ARG   A 1 19  ? 5.196  1.04    -4.329  1   48.958  ? 31  ARG   B HB2  1 c 1 
ATOM   268  H HB3  . ARG   A 1 19  ? 6.659  1.469   -4.773  1   47.249  ? 31  ARG   B HB3  1 c 1 
ATOM   269  H HG2  . ARG   A 1 19  ? 6.476  -0.012  -6.626  1   51.035  ? 31  ARG   B HG2  1 c 1 
ATOM   270  H HG3  . ARG   A 1 19  ? 4.986  -0.325  -6.2    1   52.764  ? 31  ARG   B HG3  1 c 1 
ATOM   271  H HD2  . ARG   A 1 19  ? 5.208  1.304   -8.009  1   56.239  ? 31  ARG   B HD2  1 c 1 
ATOM   272  H HD3  . ARG   A 1 19  ? 4.246  1.747   -6.836  1   55.054  ? 31  ARG   B HD3  1 c 1 
ATOM   273  H HE   . ARG   A 1 19  ? 5.74   3.312   -6.22   1   51.724  ? 31  ARG   B HE   1 c 1 
ATOM   274  H HH11 . ARG   A 1 19  ? 7.64   1.515   -8.41   1   54.649  ? 31  ARG   B HH11 1 c 1 
ATOM   275  H HH12 . ARG   A 1 19  ? 7.802  2.733   -9.33   1   56.988  ? 31  ARG   B HH12 1 c 1 
ATOM   276  H HH21 . ARG   A 1 19  ? 7.284  4.91    -6.852  1   55.362  ? 31  ARG   B HH21 1 c 1 
ATOM   277  H HH22 . ARG   A 1 19  ? 8.257  4.604   -7.996  1   56.934  ? 31  ARG   B HH22 1 c 1 
ATOM   278  N N    . GLY   A 1 20  ? 7.075  -1.04   -1.693  1   43.597  ? 32  GLY   B N    1 ? 1 
ATOM   279  C CA   . GLY   A 1 20  ? 7.387  -0.72   -0.32   1   40.467  ? 32  GLY   B CA   1 ? 1 
ATOM   280  C C    . GLY   A 1 20  ? 8.876  -0.476  -0.124  1   38.356  ? 32  GLY   B C    1 ? 1 
ATOM   281  O O    . GLY   A 1 20  ? 9.247  0.266   0.781   1   38.714  ? 32  GLY   B O    1 ? 1 
ATOM   282  H H    . GLY   A 1 20  ? 6.936  -1.912  -1.927  1   44.627  ? 32  GLY   B H    1 c 1 
ATOM   283  H HA2  . GLY   A 1 20  ? 6.883  0.081   -0.051  1   40.772  ? 32  GLY   B HA2  1 c 1 
ATOM   284  H HA3  . GLY   A 1 20  ? 7.099  -1.466  0.255   1   40.991  ? 32  GLY   B HA3  1 c 1 
ATOM   285  N N    . VAL   A 1 21  ? 9.681  -1.092  -0.985  1   37.465  ? 33  VAL   B N    1 ? 1 
ATOM   286  C CA   . VAL   A 1 21  ? 11.116 -0.942  -0.952  1   41.641  ? 33  VAL   B CA   1 ? 1 
ATOM   287  C C    . VAL   A 1 21  ? 11.531 -0.767  -2.394  1   41.498  ? 33  VAL   B C    1 ? 1 
ATOM   288  O O    . VAL   A 1 21  ? 11.366 -1.691  -3.173  1   43.313  ? 33  VAL   B O    1 ? 1 
ATOM   289  C CB   . VAL   A 1 21  ? 11.902 -2.106  -0.297  1   38.471  ? 33  VAL   B CB   1 ? 1 
ATOM   290  C CG1  . VAL   A 1 21  ? 13.366 -1.762  -0.181  1   40.438  ? 33  VAL   B CG1  1 ? 1 
ATOM   291  C CG2  . VAL   A 1 21  ? 11.348 -2.516  1.048   1   40.47   ? 33  VAL   B CG2  1 ? 1 
ATOM   292  H H    . VAL   A 1 21  ? 9.317  -1.635  -1.623  1   40.355  ? 33  VAL   B H    1 c 1 
ATOM   293  H HA   . VAL   A 1 21  ? 11.327 -0.121  -0.467  1   38.78   ? 33  VAL   B HA   1 c 1 
ATOM   294  H HB   . VAL   A 1 21  ? 11.824 -2.883  -0.899  1   41.108  ? 33  VAL   B HB   1 c 1 
ATOM   295  H HG11 . VAL   A 1 21  ? 13.465 -0.915  0.284   1   38.787  ? 33  VAL   B HG11 1 c 1 
ATOM   296  H HG12 . VAL   A 1 21  ? 13.756 -1.691  -1.068  1   40.376  ? 33  VAL   B HG12 1 c 1 
ATOM   297  H HG13 . VAL   A 1 21  ? 13.825 -2.459  0.317   1   39.414  ? 33  VAL   B HG13 1 c 1 
ATOM   298  H HG21 . VAL   A 1 21  ? 11.902 -3.218  1.428   1   39.609  ? 33  VAL   B HG21 1 c 1 
ATOM   299  H HG22 . VAL   A 1 21  ? 10.44  -2.845  0.939   1   40.616  ? 33  VAL   B HG22 1 c 1 
ATOM   300  H HG23 . VAL   A 1 21  ? 11.344 -1.749  1.645   1   38.8    ? 33  VAL   B HG23 1 c 1 
ATOM   301  N N    . LEU   A 1 22  ? 12.01  0.435   -2.741  1   42.51   ? 34  LEU   B N    1 ? 1 
ATOM   302  C CA   . LEU   A 1 22  ? 12.527 0.748   -4.066  1   42.911  ? 34  LEU   B CA   1 ? 1 
ATOM   303  C C    . LEU   A 1 22  ? 14.046 0.951   -4.033  1   43.526  ? 34  LEU   B C    1 ? 1 
ATOM   304  O O    . LEU   A 1 22  ? 14.543 1.674   -3.156  1   42.435  ? 34  LEU   B O    1 ? 1 
ATOM   305  C CB   . LEU   A 1 22  ? 11.851 2.03    -4.545  1   44.999  ? 34  LEU   B CB   1 ? 1 
ATOM   306  C CG   . LEU   A 1 22  ? 10.327 1.952   -4.708  1   45.472  ? 34  LEU   B CG   1 ? 1 
ATOM   307  C CD1  . LEU   A 1 22  ? 9.774  3.364   -4.917  1   46.46   ? 34  LEU   B CD1  1 ? 1 
ATOM   308  C CD2  . LEU   A 1 22  ? 10.011 0.967   -5.854  1   44.566  ? 34  LEU   B CD2  1 ? 1 
ATOM   309  H H    . LEU   A 1 22  ? 12.011 1.1     -2.113  1   40.964  ? 34  LEU   B H    1 c 1 
ATOM   310  H HA   . LEU   A 1 22  ? 12.309 0.007   -4.68   1   44.785  ? 34  LEU   B HA   1 c 1 
ATOM   311  H HB2  . LEU   A 1 22  ? 12.059 2.746   -3.902  1   43.537  ? 34  LEU   B HB2  1 c 1 
ATOM   312  H HB3  . LEU   A 1 22  ? 12.245 2.281   -5.412  1   46.159  ? 34  LEU   B HB3  1 c 1 
ATOM   313  H HG   . LEU   A 1 22  ? 9.941  1.589   -3.87   1   43.673  ? 34  LEU   B HG   1 c 1 
ATOM   314  H HD11 . LEU   A 1 22  ? 10.005 3.921   -4.154  1   45.085  ? 34  LEU   B HD11 1 c 1 
ATOM   315  H HD12 . LEU   A 1 22  ? 8.807  3.325   -5.006  1   47.468  ? 34  LEU   B HD12 1 c 1 
ATOM   316  H HD13 . LEU   A 1 22  ? 10.157 3.748   -5.723  1   47.935  ? 34  LEU   B HD13 1 c 1 
ATOM   317  H HD21 . LEU   A 1 22  ? 10.214 0.062   -5.569  1   44.989  ? 34  LEU   B HD21 1 c 1 
ATOM   318  H HD22 . LEU   A 1 22  ? 10.547 1.19    -6.633  1   46.813  ? 34  LEU   B HD22 1 c 1 
ATOM   319  H HD23 . LEU   A 1 22  ? 9.068  1.029   -6.083  1   46.865  ? 34  LEU   B HD23 1 c 1 
ATOM   320  N N    . LYS   A 1 23  ? 14.738 0.459   -5.067  1   44.843  ? 35  LYS   B N    1 ? 1 
ATOM   321  C CA   . LYS   A 1 23  ? 16.195 0.496   -5.112  1   45.701  ? 35  LYS   B CA   1 ? 1 
ATOM   322  C C    . LYS   A 1 23  ? 16.74  0.997   -6.44   1   50.54   ? 35  LYS   B C    1 ? 1 
ATOM   323  O O    . LYS   A 1 23  ? 16.24  0.581   -7.487  1   52.04   ? 35  LYS   B O    1 ? 1 
ATOM   324  C CB   . LYS   A 1 23  ? 16.715 -0.934  -5.007  1   47.76   ? 35  LYS   B CB   1 ? 1 
ATOM   325  C CG   . LYS   A 1 23  ? 18.21  -1.116  -4.937  1   48.453  ? 35  LYS   B CG   1 ? 1 
ATOM   326  C CD   . LYS   A 1 23  ? 18.658 -2.543  -4.673  1   46.174  ? 35  LYS   B CD   1 ? 1 
ATOM   327  C CE   . LYS   A 1 23  ? 20.151 -2.64   -4.671  1   48.459  ? 35  LYS   B CE   1 ? 1 
ATOM   328  N NZ   . LYS   A 1 23  ? 20.707 -3.926  -5.106  1   50.964  ? 35  LYS   B NZ   1 ? 1 
ATOM   329  H H    . LYS   A 1 23  ? 14.288 0.088   -5.771  1   46.495  ? 35  LYS   B H    1 c 1 
ATOM   330  H HA   . LYS   A 1 23  ? 16.536 1.051   -4.37   1   45.141  ? 35  LYS   B HA   1 c 1 
ATOM   331  H HB2  . LYS   A 1 23  ? 16.323 -1.342  -4.206  1   45.81   ? 35  LYS   B HB2  1 c 1 
ATOM   332  H HB3  . LYS   A 1 23  ? 16.384 -1.438  -5.781  1   48.84   ? 35  LYS   B HB3  1 c 1 
ATOM   333  H HG2  . LYS   A 1 23  ? 18.602 -0.814  -5.785  1   49.734  ? 35  LYS   B HG2  1 c 1 
ATOM   334  H HG3  . LYS   A 1 23  ? 18.56  -0.537  -4.225  1   46.763  ? 35  LYS   B HG3  1 c 1 
ATOM   335  H HD2  . LYS   A 1 23  ? 18.312 -2.839  -3.803  1   45.343  ? 35  LYS   B HD2  1 c 1 
ATOM   336  H HD3  . LYS   A 1 23  ? 18.296 -3.132  -5.37   1   48.3    ? 35  LYS   B HD3  1 c 1 
ATOM   337  H HE2  . LYS   A 1 23  ? 20.514 -1.943  -5.246  1   49.593  ? 35  LYS   B HE2  1 c 1 
ATOM   338  H HE3  . LYS   A 1 23  ? 20.468 -2.462  -3.767  1   47.095  ? 35  LYS   B HE3  1 c 1 
ATOM   339  H HZ1  . LYS   A 1 23  ? 20.404 -4.126  -5.936  1   52.265  ? 35  LYS   B HZ1  1 c 1 
ATOM   340  H HZ2  . LYS   A 1 23  ? 20.455 -4.579  -4.531  1   49.977  ? 35  LYS   B HZ2  1 c 1 
ATOM   341  H HZ3  . LYS   A 1 23  ? 21.612 -3.878  -5.124  1   51.916  ? 35  LYS   B HZ3  1 c 1 
ATOM   342  N N    . ILE   A 1 24  ? 17.804 1.824   -6.37   1   50.999  ? 36  ILE   B N    1 ? 1 
ATOM   343  C CA   . ILE   A 1 24  ? 18.725 2.087   -7.474  1   53.052  ? 36  ILE   B CA   1 ? 1 
ATOM   344  C C    . ILE   A 1 24  ? 20.123 1.713   -6.994  1   54.34   ? 36  ILE   B C    1 ? 1 
ATOM   345  O O    . ILE   A 1 24  ? 20.539 2.106   -5.912  1   50.446  ? 36  ILE   B O    1 ? 1 
ATOM   346  C CB   . ILE   A 1 24  ? 18.689 3.54    -7.96   1   55.364  ? 36  ILE   B CB   1 ? 1 
ATOM   347  C CG1  . ILE   A 1 24  ? 17.29  3.935   -8.424  1   56.929  ? 36  ILE   B CG1  1 ? 1 
ATOM   348  C CG2  . ILE   A 1 24  ? 19.703 3.785   -9.092  1   60.409  ? 36  ILE   B CG2  1 ? 1 
ATOM   349  C CD1  . ILE   A 1 24  ? 17.137 5.408   -8.676  1   58.815  ? 36  ILE   B CD1  1 ? 1 
ATOM   350  H H    . ILE   A 1 24  ? 17.96  2.252   -5.577  1   49.368  ? 36  ILE   B H    1 c 1 
ATOM   351  H HA   . ILE   A 1 24  ? 18.485 1.507   -8.222  1   55.002  ? 36  ILE   B HA   1 c 1 
ATOM   352  H HB   . ILE   A 1 24  ? 18.929 4.115   -7.207  1   54.533  ? 36  ILE   B HB   1 c 1 
ATOM   353  H HG12 . ILE   A 1 24  ? 17.083 3.45    -9.249  1   58.426  ? 36  ILE   B HG12 1 c 1 
ATOM   354  H HG13 . ILE   A 1 24  ? 16.641 3.663   -7.744  1   54.408  ? 36  ILE   B HG13 1 c 1 
ATOM   355  H HG21 . ILE   A 1 24  ? 19.718 4.73    -9.32   1   61.524  ? 36  ILE   B HG21 1 c 1 
ATOM   356  H HG22 . ILE   A 1 24  ? 19.448 3.269   -9.875  1   61.663  ? 36  ILE   B HG22 1 c 1 
ATOM   357  H HG23 . ILE   A 1 24  ? 20.588 3.514   -8.803  1   60.241  ? 36  ILE   B HG23 1 c 1 
ATOM   358  H HD11 . ILE   A 1 24  ? 17.374 5.911   -7.875  1   57.379  ? 36  ILE   B HD11 1 c 1 
ATOM   359  H HD12 . ILE   A 1 24  ? 16.21  5.593   -8.912  1   58.942  ? 36  ILE   B HD12 1 c 1 
ATOM   360  H HD13 . ILE   A 1 24  ? 17.715 5.682   -9.413  1   61.409  ? 36  ILE   B HD13 1 c 1 
ATOM   361  N N    . VAL   A 1 25  ? 20.832 0.933   -7.802  1   55.995  ? 37  VAL   B N    1 ? 1 
ATOM   362  C CA   . VAL   A 1 25  ? 22.261 0.729   -7.682  1   56.684  ? 37  VAL   B CA   1 ? 1 
ATOM   363  C C    . VAL   A 1 25  ? 22.966 1.98    -8.206  1   60.358  ? 37  VAL   B C    1 ? 1 
ATOM   364  O O    . VAL   A 1 25  ? 22.778 2.338   -9.359  1   61.067  ? 37  VAL   B O    1 ? 1 
ATOM   365  C CB   . VAL   A 1 25  ? 22.6   -0.5    -8.548  1   59.229  ? 37  VAL   B CB   1 ? 1 
ATOM   366  C CG1  . VAL   A 1 25  ? 24.102 -0.734  -8.683  1   61.482  ? 37  VAL   B CG1  1 ? 1 
ATOM   367  C CG2  . VAL   A 1 25  ? 21.857 -1.758  -8.069  1   57.615  ? 37  VAL   B CG2  1 ? 1 
ATOM   368  H H    . VAL   A 1 25  ? 20.393 0.511   -8.484  1   57.017  ? 37  VAL   B H    1 c 1 
ATOM   369  H HA   . VAL   A 1 25  ? 22.501 0.564   -6.749  1   55.241  ? 37  VAL   B HA   1 c 1 
ATOM   370  H HB   . VAL   A 1 25  ? 22.266 -0.304  -9.455  1   61.099  ? 37  VAL   B HB   1 c 1 
ATOM   371  H HG11 . VAL   A 1 25  ? 24.512 -0.733  -7.802  1   60.259  ? 37  VAL   B HG11 1 c 1 
ATOM   372  H HG12 . VAL   A 1 25  ? 24.496 -0.029  -9.224  1   63.921  ? 37  VAL   B HG12 1 c 1 
ATOM   373  H HG13 . VAL   A 1 25  ? 24.259 -1.593  -9.111  1   63.066  ? 37  VAL   B HG13 1 c 1 
ATOM   374  H HG21 . VAL   A 1 25  ? 22.185 -2.534  -8.554  1   59.304  ? 37  VAL   B HG21 1 c 1 
ATOM   375  H HG22 . VAL   A 1 25  ? 20.904 -1.657  -8.23   1   56.617  ? 37  VAL   B HG22 1 c 1 
ATOM   376  H HG23 . VAL   A 1 25  ? 22.012 -1.884  -7.117  1   55.439  ? 37  VAL   B HG23 1 c 1 
ATOM   377  N N    . LYS   A 1 26  ? 23.775 2.639   -7.371  1   60.368  ? 38  LYS   B N    1 ? 1 
ATOM   378  C CA   . LYS   A 1 26  ? 24.483 3.839   -7.789  1   63.672  ? 38  LYS   B CA   1 ? 1 
ATOM   379  C C    . LYS   A 1 26  ? 25.941 3.544   -8.135  1   68.181  ? 38  LYS   B C    1 ? 1 
ATOM   380  O O    . LYS   A 1 26  ? 26.475 4.156   -9.046  1   71.53   ? 38  LYS   B O    1 ? 1 
ATOM   381  C CB   . LYS   A 1 26  ? 24.303 4.877   -6.692  1   62.032  ? 38  LYS   B CB   1 ? 1 
ATOM   382  C CG   . LYS   A 1 26  ? 22.877 5.438   -6.604  1   60.305  ? 38  LYS   B CG   1 ? 1 
ATOM   383  C CD   . LYS   A 1 26  ? 22.407 5.995   -7.939  1   62.935  ? 38  LYS   B CD   1 ? 1 
ATOM   384  C CE   . LYS   A 1 26  ? 21.547 7.208   -7.827  1   63.658  ? 38  LYS   B CE   1 ? 1 
ATOM   385  N NZ   . LYS   A 1 26  ? 21.523 7.926   -9.093  1   66.142  ? 38  LYS   B NZ   1 ? 1 
ATOM   386  H H    . LYS   A 1 26  ? 23.887 2.334   -6.516  1   58.499  ? 38  LYS   B H    1 c 1 
ATOM   387  H HA   . LYS   A 1 26  ? 24.047 4.182   -8.608  1   65.248  ? 38  LYS   B HA   1 c 1 
ATOM   388  H HB2  . LYS   A 1 26  ? 24.534 4.473   -5.828  1   60.44   ? 38  LYS   B HB2  1 c 1 
ATOM   389  H HB3  . LYS   A 1 26  ? 24.922 5.621   -6.852  1   64.704  ? 38  LYS   B HB3  1 c 1 
ATOM   390  H HG2  . LYS   A 1 26  ? 22.27  4.722   -6.318  1   57.674  ? 38  LYS   B HG2  1 c 1 
ATOM   391  H HG3  . LYS   A 1 26  ? 22.857 6.148   -5.927  1   59.562  ? 38  LYS   B HG3  1 c 1 
ATOM   392  H HD2  . LYS   A 1 26  ? 23.194 6.219   -8.482  1   66.217  ? 38  LYS   B HD2  1 c 1 
ATOM   393  H HD3  . LYS   A 1 26  ? 21.91  5.297   -8.415  1   62.702  ? 38  LYS   B HD3  1 c 1 
ATOM   394  H HE2  . LYS   A 1 26  ? 20.641 6.943   -7.591  1   60.834  ? 38  LYS   B HE2  1 c 1 
ATOM   395  H HE3  . LYS   A 1 26  ? 21.889 7.798   -7.131  1   62.898  ? 38  LYS   B HE3  1 c 1 
ATOM   396  H HZ1  . LYS   A 1 26  ? 21.253 7.371   -9.756  1   67.2    ? 38  LYS   B HZ1  1 c 1 
ATOM   397  H HZ2  . LYS   A 1 26  ? 22.351 8.241   -9.285  1   69.096  ? 38  LYS   B HZ2  1 c 1 
ATOM   398  H HZ3  . LYS   A 1 26  ? 20.947 8.623   -9.037  1   66.672  ? 38  LYS   B HZ3  1 c 1 
ATOM   399  N N    . ARG   A 1 27  ? 26.588 2.603   -7.434  1   68.853  ? 39  ARG   B N    1 ? 1 
ATOM   400  C CA   . ARG   A 1 27  ? 27.92  2.154   -7.816  1   72.436  ? 39  ARG   B CA   1 ? 1 
ATOM   401  C C    . ARG   A 1 27  ? 27.926 0.628   -7.747  1   71.528  ? 39  ARG   B C    1 ? 1 
ATOM   402  O O    . ARG   A 1 27  ? 27.511 0.052   -6.757  1   72.408  ? 39  ARG   B O    1 ? 1 
ATOM   403  C CB   . ARG   A 1 27  ? 29.019 2.793   -6.949  1   73.559  ? 39  ARG   B CB   1 ? 1 
ATOM   404  C CG   . ARG   A 1 27  ? 30.447 2.486   -7.39   1   78.885  ? 39  ARG   B CG   1 ? 1 
ATOM   405  C CD   . ARG   A 1 27  ? 31.512 2.93    -6.371  1   80.078  ? 39  ARG   B CD   1 ? 1 
ATOM   406  N NE   . ARG   A 1 27  ? 31.552 2.01    -5.218  1   78.65   ? 39  ARG   B NE   1 ? 1 
ATOM   407  C CZ   . ARG   A 1 27  ? 31.993 2.343   -4.002  1   77.695  ? 39  ARG   B CZ   1 ? 1 
ATOM   408  N NH1  . ARG   A 1 27  ? 32.48  3.56    -3.784  1   81.717  ? 39  ARG   B NH1  1 ? 1 
ATOM   409  N NH2  . ARG   A 1 27  ? 31.939 1.48    -3.003  1   73.972  ? 39  ARG   B NH2  1 ? 1 
ATOM   410  H H    . ARG   A 1 27  ? 26.195 2.239   -6.694  1   65.512  ? 39  ARG   B H    1 c 1 
ATOM   411  H HA   . ARG   A 1 27  ? 28.079 2.422   -8.757  1   75.339  ? 39  ARG   B HA   1 c 1 
ATOM   412  H HB2  . ARG   A 1 27  ? 28.893 3.765   -6.952  1   74.333  ? 39  ARG   B HB2  1 c 1 
ATOM   413  H HB3  . ARG   A 1 27  ? 28.905 2.484   -6.025  1   71.244  ? 39  ARG   B HB3  1 c 1 
ATOM   414  H HG2  . ARG   A 1 27  ? 30.537 1.521   -7.542  1   78.536  ? 39  ARG   B HG2  1 c 1 
ATOM   415  H HG3  . ARG   A 1 27  ? 30.621 2.937   -8.245  1   81.639  ? 39  ARG   B HG3  1 c 1 
ATOM   416  H HD2  . ARG   A 1 27  ? 32.391 2.949   -6.802  1   84.549  ? 39  ARG   B HD2  1 c 1 
ATOM   417  H HD3  . ARG   A 1 27  ? 31.304 3.834   -6.061  1   80.235  ? 39  ARG   B HD3  1 c 1 
ATOM   418  H HE   . ARG   A 1 27  ? 31.271 1.194   -5.336  1   76.713  ? 39  ARG   B HE   1 c 1 
ATOM   419  H HH11 . ARG   A 1 27  ? 32.961 3.964   -4.406  1   84.526  ? 39  ARG   B HH11 1 c 1 
ATOM   420  H HH12 . ARG   A 1 27  ? 32.334 3.957   -3.008  1   80.199  ? 39  ARG   B HH12 1 c 1 
ATOM   421  H HH21 . ARG   A 1 27  ? 31.397 0.784   -3.05   1   72.111  ? 39  ARG   B HH21 1 c 1 
ATOM   422  H HH22 . ARG   A 1 27  ? 32.448 1.603   -2.29   1   75.431  ? 39  ARG   B HH22 1 c 1 
ATOM   423  N N    . VAL   A 1 28  ? 28.366 -0.028  -8.817  1   74.981  ? 40  VAL   B N    1 ? 1 
ATOM   424  C CA   . VAL   A 1 28  ? 28.19  -1.461  -8.956  1   76.179  ? 40  VAL   B CA   1 ? 1 
ATOM   425  C C    . VAL   A 1 28  ? 29.312 -2.162  -8.196  1   78.433  ? 40  VAL   B C    1 ? 1 
ATOM   426  O O    . VAL   A 1 28  ? 30.455 -1.707  -8.229  1   80.796  ? 40  VAL   B O    1 ? 1 
ATOM   427  C CB   . VAL   A 1 28  ? 28.153 -1.88   -10.437 1   80.739  ? 40  VAL   B CB   1 ? 1 
ATOM   428  C CG1  . VAL   A 1 28  ? 29.489 -1.638  -11.131 1   87.261  ? 40  VAL   B CG1  1 ? 1 
ATOM   429  C CG2  . VAL   A 1 28  ? 27.722 -3.332  -10.602 1   80.061  ? 40  VAL   B CG2  1 ? 1 
ATOM   430  H H    . VAL   A 1 28  ? 28.788 0.433   -9.483  1   78.471  ? 40  VAL   B H    1 c 1 
ATOM   431  H HA   . VAL   A 1 28  ? 27.337 -1.706  -8.548  1   73.014  ? 40  VAL   B HA   1 c 1 
ATOM   432  H HB   . VAL   A 1 28  ? 27.478 -1.314  -10.881 1   80.371  ? 40  VAL   B HB   1 c 1 
ATOM   433  H HG11 . VAL   A 1 28  ? 30.151 -2.264  -10.794 1   87.845  ? 40  VAL   B HG11 1 c 1 
ATOM   434  H HG12 . VAL   A 1 28  ? 29.788 -0.729  -10.96  1   87.49   ? 40  VAL   B HG12 1 c 1 
ATOM   435  H HG13 . VAL   A 1 28  ? 29.383 -1.767  -12.088 1   89.65   ? 40  VAL   B HG13 1 c 1 
ATOM   436  H HG21 . VAL   A 1 28  ? 27.646 -3.542  -11.548 1   82.866  ? 40  VAL   B HG21 1 c 1 
ATOM   437  H HG22 . VAL   A 1 28  ? 26.861 -3.466  -10.171 1   76.925  ? 40  VAL   B HG22 1 c 1 
ATOM   438  H HG23 . VAL   A 1 28  ? 28.382 -3.917  -10.193 1   80.769  ? 40  VAL   B HG23 1 c 1 
ATOM   439  N N    . GLY   A 1 29  ? 28.954 -3.268  -7.535  1   77.075  ? 41  GLY   B N    1 ? 1 
ATOM   440  C CA   . GLY   A 1 29  ? 29.884 -4.095  -6.785  1   80.407  ? 41  GLY   B CA   1 ? 1 
ATOM   441  C C    . GLY   A 1 29  ? 30.63  -5.073  -7.696  1   83.282  ? 41  GLY   B C    1 ? 1 
ATOM   442  O O    . GLY   A 1 29  ? 30.778 -4.837  -8.89   1   86.728  ? 41  GLY   B O    1 ? 1 
ATOM   443  H H    . GLY   A 1 29  ? 28.076 -3.523  -7.556  1   75.075  ? 41  GLY   B H    1 c 1 
ATOM   444  H HA2  . GLY   A 1 29  ? 30.533 -3.514  -6.322  1   80.264  ? 41  GLY   B HA2  1 c 1 
ATOM   445  H HA3  . GLY   A 1 29  ? 29.385 -4.598  -6.1    1   76.853  ? 41  GLY   B HA3  1 c 1 
ATOM   446  N N    . ASN   A 1 30  ? 31.11  -6.162  -7.104  1   82.329  ? 42  ASN   B N    1 ? 1 
ATOM   447  C CA   . ASN   A 1 30  ? 31.796 -7.234  -7.801  1   87.279  ? 42  ASN   B CA   1 ? 1 
ATOM   448  C C    . ASN   A 1 30  ? 31.469 -8.547  -7.1    1   86.123  ? 42  ASN   B C    1 ? 1 
ATOM   449  O O    . ASN   A 1 30  ? 30.971 -8.549  -5.979  1   80.352  ? 42  ASN   B O    1 ? 1 
ATOM   450  C CB   . ASN   A 1 30  ? 33.297 -6.995  -7.789  1   96.356  ? 42  ASN   B CB   1 ? 1 
ATOM   451  C CG   . ASN   A 1 30  ? 33.752 -6.533  -6.425  1   96.982  ? 42  ASN   B CG   1 ? 1 
ATOM   452  O OD1  . ASN   A 1 30  ? 33.814 -7.337  -5.489  1   101.433 ? 42  ASN   B OD1  1 ? 1 
ATOM   453  N ND2  . ASN   A 1 30  ? 34.064 -5.253  -6.276  1   98.155  ? 42  ASN   B ND2  1 ? 1 
ATOM   454  H H    . ASN   A 1 30  ? 30.997 -6.243  -6.201  1   80.718  ? 42  ASN   B H    1 c 1 
ATOM   455  H HA   . ASN   A 1 30  ? 31.49  -7.269  -8.735  1   89.338  ? 42  ASN   B HA   1 c 1 
ATOM   456  H HB2  . ASN   A 1 30  ? 33.763 -7.822  -8.024  1   98.512  ? 42  ASN   B HB2  1 c 1 
ATOM   457  H HB3  . ASN   A 1 30  ? 33.524 -6.316  -8.455  1   97.751  ? 42  ASN   B HB3  1 c 1 
ATOM   458  H HD21 . ASN   A 1 30  ? 34.497 -4.986  -5.55   1   98.008  ? 42  ASN   B HD21 1 c 1 
ATOM   459  H HD22 . ASN   A 1 30  ? 33.838 -4.663  -6.9    1   98.106  ? 42  ASN   B HD22 1 c 1 
ATOM   460  N N    . GLY   A 1 31  ? 31.801 -9.661  -7.749  1   92.127  ? 43  GLY   B N    1 ? 1 
ATOM   461  C CA   . GLY   A 1 31  ? 31.39  -10.971 -7.276  1   90.338  ? 43  GLY   B CA   1 ? 1 
ATOM   462  C C    . GLY   A 1 31  ? 29.938 -11.229 -7.656  1   89.05   ? 43  GLY   B C    1 ? 1 
ATOM   463  O O    . GLY   A 1 31  ? 29.162 -10.29  -7.809  1   88.34   ? 43  GLY   B O    1 ? 1 
ATOM   464  H H    . GLY   A 1 31  ? 32.299 -9.605  -8.513  1   94.576  ? 43  GLY   B H    1 c 1 
ATOM   465  H HA2  . GLY   A 1 31  ? 31.97  -11.659 -7.679  1   94.61   ? 43  GLY   B HA2  1 c 1 
ATOM   466  H HA3  . GLY   A 1 31  ? 31.494 -11.017 -6.296  1   89.193  ? 43  GLY   B HA3  1 c 1 
ATOM   467  N N    . GLU   A 1 32  ? 29.615 -12.51  -7.848  1   93.448  ? 44  GLU   B N    1 ? 1 
ATOM   468  C CA   . GLU   A 1 32  ? 28.265 -12.97  -8.121  1   92.95   ? 44  GLU   B CA   1 ? 1 
ATOM   469  C C    . GLU   A 1 32  ? 27.48  -13.113 -6.806  1   89.392  ? 44  GLU   B C    1 ? 1 
ATOM   470  O O    . GLU   A 1 32  ? 26.255 -13.182 -6.823  1   88.848  ? 44  GLU   B O    1 ? 1 
ATOM   471  C CB   . GLU   A 1 32  ? 28.382 -14.283 -8.911  1   95.757  ? 44  GLU   B CB   1 ? 1 
ATOM   472  H H    . GLU   A 1 32  ? 30.281 -13.134 -7.797  1   95.707  ? 44  GLU   B H    1 c 1 
ATOM   473  H HA   . GLU   A 1 32  ? 27.813 -12.296 -8.69   1   91.634  ? 44  GLU   B HA   1 c 1 
ATOM   474  H HB2  . GLU   A 1 32  ? 29.287 -14.4   -9.086  0   30      ? 44  GLU   B HB2  1 c 1 
ATOM   475  H HB3  . GLU   A 1 32  ? 27.432 -14.477 -9.137  0   30      ? 44  GLU   B HB3  1 c 1 
ATOM   476  N N    . GLU   A 1 33  ? 28.18  -13.139 -5.659  1   86.802  ? 45  GLU   B N    1 ? 1 
ATOM   477  C CA   . GLU   A 1 33  ? 27.607 -13.561 -4.388  1   81.574  ? 45  GLU   B CA   1 ? 1 
ATOM   478  C C    . GLU   A 1 33  ? 26.916 -12.381 -3.714  1   76.256  ? 45  GLU   B C    1 ? 1 
ATOM   479  O O    . GLU   A 1 33  ? 27.452 -11.281 -3.655  1   72.594  ? 45  GLU   B O    1 ? 1 
ATOM   480  C CB   . GLU   A 1 33  ? 28.691 -14.143 -3.474  1   83.425  ? 45  GLU   B CB   1 ? 1 
ATOM   481  H H    . GLU   A 1 33  ? 29.056 -12.879 -5.671  1   88.095  ? 45  GLU   B H    1 c 1 
ATOM   482  H HA   . GLU   A 1 33  ? 26.934 -14.266 -4.568  1   82.419  ? 45  GLU   B HA   1 c 1 
ATOM   483  H HB2  . GLU   A 1 33  ? 29.493 -13.942 -3.819  0   30      ? 45  GLU   B HB2  1 c 1 
ATOM   484  H HB3  . GLU   A 1 33  ? 28.156 -14.63  -2.731  0   30      ? 45  GLU   B HB3  1 c 1 
ATOM   485  N N    . THR   A 1 34  ? 25.688 -12.608 -3.239  1   73.407  ? 46  THR   B N    1 ? 1 
ATOM   486  C CA   . THR   A 1 34  ? 24.993 -11.627 -2.422  1   67.516  ? 46  THR   B CA   1 ? 1 
ATOM   487  C C    . THR   A 1 34  ? 24.859 -12.207 -1.024  1   68.034  ? 46  THR   B C    1 ? 1 
ATOM   488  O O    . THR   A 1 34  ? 24.888 -13.405 -0.842  1   64.897  ? 46  THR   B O    1 ? 1 
ATOM   489  C CB   . THR   A 1 34  ? 23.618 -11.3   -2.99   1   65.426  ? 46  THR   B CB   1 ? 1 
ATOM   490  O OG1  . THR   A 1 34  ? 22.934 -12.554 -3.013  1   66.691  ? 46  THR   B OG1  1 ? 1 
ATOM   491  C CG2  . THR   A 1 34  ? 23.697 -10.639 -4.355  1   64.686  ? 46  THR   B CG2  1 ? 1 
ATOM   492  H H    . THR   A 1 34  ? 25.269 -13.397 -3.432  1   74.28   ? 46  THR   B H    1 c 1 
ATOM   493  H HA   . THR   A 1 34  ? 25.527 -10.806 -2.384  1   67.542  ? 46  THR   B HA   1 c 1 
ATOM   494  H HB   . THR   A 1 34  ? 23.155 -10.689 -2.37   1   62.543  ? 46  THR   B HB   1 c 1 
ATOM   495  H HG1  . THR   A 1 34  ? 23.322 -13.086 -3.553  0   30      ? 46  THR   B HG1  1 c 1 
ATOM   496  H HG21 . THR   A 1 34  ? 22.801 -10.426 -4.665  1   64.206  ? 46  THR   B HG21 1 c 1 
ATOM   497  H HG22 . THR   A 1 34  ? 24.121 -11.244 -4.986  1   68.019  ? 46  THR   B HG22 1 c 1 
ATOM   498  H HG23 . THR   A 1 34  ? 24.219 -9.821  -4.29   1   64.561  ? 46  THR   B HG23 1 c 1 
ATOM   499  N N    . PRO   A 1 35  ? 24.673 -11.404 0.037   1   66.263  ? 47  PRO   B N    1 ? 1 
ATOM   500  C CA   . PRO   A 1 35  ? 24.541 -11.988 1.365   1   64.857  ? 47  PRO   B CA   1 ? 1 
ATOM   501  C C    . PRO   A 1 35  ? 23.352 -12.958 1.479   1   65.838  ? 47  PRO   B C    1 ? 1 
ATOM   502  O O    . PRO   A 1 35  ? 22.287 -12.673 0.938   1   62.208  ? 47  PRO   B O    1 ? 1 
ATOM   503  C CB   . PRO   A 1 35  ? 24.369 -10.772 2.261   1   61.278  ? 47  PRO   B CB   1 ? 1 
ATOM   504  C CG   . PRO   A 1 35  ? 24.829 -9.58   1.441   1   65.641  ? 47  PRO   B CG   1 ? 1 
ATOM   505  C CD   . PRO   A 1 35  ? 24.615 -9.939  0.007   1   66.217  ? 47  PRO   B CD   1 ? 1 
ATOM   506  H HA   . PRO   A 1 35  ? 25.37  -12.454 1.599   1   67.279  ? 47  PRO   B HA   1 c 1 
ATOM   507  H HB2  . PRO   A 1 35  ? 23.436 -10.666 2.521   1   60.872  ? 47  PRO   B HB2  1 c 1 
ATOM   508  H HB3  . PRO   A 1 35  ? 24.908 -10.862 3.071   1   63.347  ? 47  PRO   B HB3  1 c 1 
ATOM   509  H HG2  . PRO   A 1 35  ? 24.31  -8.784  1.673   1   62.197  ? 47  PRO   B HG2  1 c 1 
ATOM   510  H HG3  . PRO   A 1 35  ? 25.774 -9.393  1.607   1   65.671  ? 47  PRO   B HG3  1 c 1 
ATOM   511  H HD2  . PRO   A 1 35  ? 23.746 -9.629  -0.316  1   64.131  ? 47  PRO   B HD2  1 c 1 
ATOM   512  H HD3  . PRO   A 1 35  ? 25.322 -9.574  -0.556  1   66.824  ? 47  PRO   B HD3  1 c 1 
ATOM   513  N N    . MET   A 1 36  ? 23.575 -14.106 2.132   1   71.381  ? 48  MET   B N    1 ? 1 
ATOM   514  C CA   . MET   A 1 36  ? 22.538 -15.053 2.527   1   74.449  ? 48  MET   B CA   1 ? 1 
ATOM   515  C C    . MET   A 1 36  ? 22.073 -14.703 3.947   1   72.34   ? 48  MET   B C    1 ? 1 
ATOM   516  O O    . MET   A 1 36  ? 22.827 -14.128 4.743   1   70.272  ? 48  MET   B O    1 ? 1 
ATOM   517  C CB   . MET   A 1 36  ? 23.064 -16.496 2.546   1   87.4    ? 48  MET   B CB   1 ? 1 
ATOM   518  C CG   . MET   A 1 36  ? 23.476 -17.129 1.2     1   96.315  ? 48  MET   B CG   1 ? 1 
ATOM   519  S SD   . MET   A 1 36  ? 22.204 -17.344 -0.074  1   96.258  ? 48  MET   B SD   1 ? 1 
ATOM   520  C CE   . MET   A 1 36  ? 22.448 -15.865 -1.072  1   94.982  ? 48  MET   B CE   1 ? 1 
ATOM   521  H H    . MET   A 1 36  ? 24.439 -14.313 2.345   1   72.718  ? 48  MET   B H    1 c 1 
ATOM   522  H HA   . MET   A 1 36  ? 21.774 -14.979 1.9     1   74.478  ? 48  MET   B HA   1 c 1 
ATOM   523  H HB2  . MET   A 1 36  ? 23.841 -16.523 3.145   1   87.323  ? 48  MET   B HB2  1 c 1 
ATOM   524  H HB3  . MET   A 1 36  ? 22.372 -17.063 2.948   1   87.144  ? 48  MET   B HB3  1 c 1 
ATOM   525  H HG2  . MET   A 1 36  ? 24.19  -16.583 0.814   1   94.412  ? 48  MET   B HG2  1 c 1 
ATOM   526  H HG3  . MET   A 1 36  ? 23.86  -18.009 1.384   1   97.666  ? 48  MET   B HG3  1 c 1 
ATOM   527  H HE1  . MET   A 1 36  ? 22.003 -15.98  -1.931  1   95.445  ? 48  MET   B HE1  1 c 1 
ATOM   528  H HE2  . MET   A 1 36  ? 22.073 -15.094 -0.608  1   91.713  ? 48  MET   B HE2  1 c 1 
ATOM   529  H HE3  . MET   A 1 36  ? 23.401 -15.726 -1.219  1   95.403  ? 48  MET   B HE3  1 c 1 
ATOM   530  N N    . ILE   A 1 37  ? 20.833 -15.086 4.296   1   67.197  ? 49  ILE   B N    1 ? 1 
ATOM   531  C CA   . ILE   A 1 37  ? 20.325 -14.899 5.654   1   61.684  ? 49  ILE   B CA   1 ? 1 
ATOM   532  C C    . ILE   A 1 37  ? 21.278 -15.571 6.653   1   61.452  ? 49  ILE   B C    1 ? 1 
ATOM   533  O O    . ILE   A 1 37  ? 21.658 -16.724 6.475   1   61.686  ? 49  ILE   B O    1 ? 1 
ATOM   534  C CB   . ILE   A 1 37  ? 18.885 -15.429 5.824   1   63.674  ? 49  ILE   B CB   1 ? 1 
ATOM   535  C CG1  . ILE   A 1 37  ? 17.854 -14.642 4.982   1   62.342  ? 49  ILE   B CG1  1 ? 1 
ATOM   536  C CG2  . ILE   A 1 37  ? 18.488 -15.462 7.306   1   63.195  ? 49  ILE   B CG2  1 ? 1 
ATOM   537  C CD1  . ILE   A 1 37  ? 16.498 -15.331 4.87    1   66.956  ? 49  ILE   B CD1  1 ? 1 
ATOM   538  H H    . ILE   A 1 37  ? 20.293 -15.479 3.672   1   67.804  ? 49  ILE   B H    1 c 1 
ATOM   539  H HA   . ILE   A 1 37  ? 20.315 -13.94  5.839   1   59.8    ? 49  ILE   B HA   1 c 1 
ATOM   540  H HB   . ILE   A 1 37  ? 18.877 -16.351 5.499   1   65.908  ? 49  ILE   B HB   1 c 1 
ATOM   541  H HG12 . ILE   A 1 37  ? 17.727 -13.759 5.384   1   60.502  ? 49  ILE   B HG12 1 c 1 
ATOM   542  H HG13 . ILE   A 1 37  ? 18.215 -14.512 4.081   1   62.457  ? 49  ILE   B HG13 1 c 1 
ATOM   543  H HG21 . ILE   A 1 37  ? 17.536 -15.637 7.387   1   63.839  ? 49  ILE   B HG21 1 c 1 
ATOM   544  H HG22 . ILE   A 1 37  ? 18.693 -14.606 7.718   1   61.615  ? 49  ILE   B HG22 1 c 1 
ATOM   545  H HG23 . ILE   A 1 37  ? 18.981 -16.165 7.762   1   65.9    ? 49  ILE   B HG23 1 c 1 
ATOM   546  H HD11 . ILE   A 1 37  ? 16.624 -16.257 4.589   1   68.678  ? 49  ILE   B HD11 1 c 1 
ATOM   547  H HD12 . ILE   A 1 37  ? 15.952 -14.864 4.21    1   64.851  ? 49  ILE   B HD12 1 c 1 
ATOM   548  H HD13 . ILE   A 1 37  ? 16.045 -15.313 5.734   1   66.157  ? 49  ILE   B HD13 1 c 1 
ATOM   549  N N    . GLY   A 1 38  ? 21.629 -14.85  7.726   1   58.732  ? 50  GLY   B N    1 ? 1 
ATOM   550  C CA   . GLY   A 1 38  ? 22.542 -15.393 8.717   1   63.439  ? 50  GLY   B CA   1 ? 1 
ATOM   551  C C    . GLY   A 1 38  ? 23.917 -14.725 8.687   1   64.837  ? 50  GLY   B C    1 ? 1 
ATOM   552  O O    . GLY   A 1 38  ? 24.674 -14.802 9.664   1   69.668  ? 50  GLY   B O    1 ? 1 
ATOM   553  H H    . GLY   A 1 38  ? 21.293 -14.008 7.842   1   57.302  ? 50  GLY   B H    1 c 1 
ATOM   554  H HA2  . GLY   A 1 38  ? 22.144 -15.273 9.611   1   63.459  ? 50  GLY   B HA2  1 c 1 
ATOM   555  H HA3  . GLY   A 1 38  ? 22.648 -16.361 8.566   1   65.821  ? 50  GLY   B HA3  1 c 1 
ATOM   556  N N    . ASP   A 1 39  ? 24.282 -14.176 7.532   1   61.125  ? 51  ASP   B N    1 ? 1 
ATOM   557  C CA   . ASP   A 1 39  ? 25.609 -13.619 7.333   1   65.466  ? 51  ASP   B CA   1 ? 1 
ATOM   558  C C    . ASP   A 1 39  ? 25.839 -12.401 8.234   1   62.667  ? 51  ASP   B C    1 ? 1 
ATOM   559  O O    . ASP   A 1 39  ? 24.909 -11.666 8.549   1   60.293  ? 51  ASP   B O    1 ? 1 
ATOM   560  C CB   . ASP   A 1 39  ? 25.809 -13.209 5.878   1   65.98   ? 51  ASP   B CB   1 ? 1 
ATOM   561  C CG   . ASP   A 1 39  ? 25.949 -14.363 4.892   1   69.635  ? 51  ASP   B CG   1 ? 1 
ATOM   562  O OD1  . ASP   A 1 39  ? 26.02  -15.524 5.349   1   71.007  ? 51  ASP   B OD1  1 ? 1 
ATOM   563  O OD2  . ASP   A 1 39  ? 26.002 -14.079 3.67    1   70.3    ? 51  ASP   B OD2  1 ? 1 
ATOM   564  H H    . ASP   A 1 39  ? 23.687 -14.146 6.839   1   61.022  ? 51  ASP   B H    1 c 1 
ATOM   565  H HA   . ASP   A 1 39  ? 26.272 -14.309 7.56    1   67.655  ? 51  ASP   B HA   1 c 1 
ATOM   566  H HB2  . ASP   A 1 39  ? 25.048 -12.66  5.598   1   63.265  ? 51  ASP   B HB2  1 c 1 
ATOM   567  H HB3  . ASP   A 1 39  ? 26.617 -12.658 5.813   1   66.266  ? 51  ASP   B HB3  1 c 1 
ATOM   568  N N    . LYS   A 1 40  ? 27.104 -12.201 8.64    1   67.187  ? 52  LYS   B N    1 ? 1 
ATOM   569  C CA   . LYS   A 1 40  ? 27.519 -10.962 9.269   1   66.127  ? 52  LYS   B CA   1 ? 1 
ATOM   570  C C    . LYS   A 1 40  ? 27.818 -9.965  8.155   1   64.807  ? 52  LYS   B C    1 ? 1 
ATOM   571  O O    . LYS   A 1 40  ? 28.718 -10.184 7.355   1   68.034  ? 52  LYS   B O    1 ? 1 
ATOM   572  C CB   . LYS   A 1 40  ? 28.786 -11.039 10.139  1   72.803  ? 52  LYS   B CB   1 ? 1 
ATOM   573  C CG   . LYS   A 1 40  ? 28.505 -11.116 11.628  1   77.083  ? 52  LYS   B CG   1 ? 1 
ATOM   574  C CD   . LYS   A 1 40  ? 29.764 -10.942 12.481  1   85.387  ? 52  LYS   B CD   1 ? 1 
ATOM   575  C CE   . LYS   A 1 40  ? 30.144 -9.488  12.577  1   86.838  ? 52  LYS   B CE   1 ? 1 
ATOM   576  N NZ   . LYS   A 1 40  ? 31.581 -9.291  12.775  1   94.551  ? 52  LYS   B NZ   1 ? 1 
ATOM   577  H H    . LYS   A 1 40  ? 27.724 -12.861 8.518   1   69.062  ? 52  LYS   B H    1 c 1 
ATOM   578  H HA   . LYS   A 1 40  ? 26.769 -10.62  9.819   1   65.211  ? 52  LYS   B HA   1 c 1 
ATOM   579  H HB2  . LYS   A 1 40  ? 29.303 -11.832 9.879   1   75.069  ? 52  LYS   B HB2  1 c 1 
ATOM   580  H HB3  . LYS   A 1 40  ? 29.342 -10.25  9.966   1   72.994  ? 52  LYS   B HB3  1 c 1 
ATOM   581  H HG2  . LYS   A 1 40  ? 27.857 -10.417 11.864  1   74.971  ? 52  LYS   B HG2  1 c 1 
ATOM   582  H HG3  . LYS   A 1 40  ? 28.098 -11.987 11.827  1   77.955  ? 52  LYS   B HG3  1 c 1 
ATOM   583  H HD2  . LYS   A 1 40  ? 29.599 -11.295 13.383  1   86.686  ? 52  LYS   B HD2  1 c 1 
ATOM   584  H HD3  . LYS   A 1 40  ? 30.503 -11.447 12.078  1   87.112  ? 52  LYS   B HD3  1 c 1 
ATOM   585  H HE2  . LYS   A 1 40  ? 29.875 -9.023  11.765  1   84.177  ? 52  LYS   B HE2  1 c 1 
ATOM   586  H HE3  . LYS   A 1 40  ? 29.667 -9.083  13.323  1   86.59   ? 52  LYS   B HE3  1 c 1 
ATOM   587  H HZ1  . LYS   A 1 40  ? 32.047 -9.745  12.145  1   94.372  ? 52  LYS   B HZ1  1 c 1 
ATOM   588  H HZ2  . LYS   A 1 40  ? 31.82  -9.591  13.596  1   96.201  ? 52  LYS   B HZ2  1 c 1 
ATOM   589  H HZ3  . LYS   A 1 40  ? 31.779 -8.408  12.713  1   93.158  ? 52  LYS   B HZ3  1 c 1 
ATOM   590  N N    . VAL   A 1 41  ? 27.11  -8.843  8.177   1   60.679  ? 53  VAL   B N    1 ? 1 
ATOM   591  C CA   . VAL   A 1 41  ? 27.194 -7.863  7.112   1   61.744  ? 53  VAL   B CA   1 ? 1 
ATOM   592  C C    . VAL   A 1 41  ? 27.788 -6.559  7.645   1   60.591  ? 53  VAL   B C    1 ? 1 
ATOM   593  O O    . VAL   A 1 41  ? 27.382 -6.089  8.701   1   65.209  ? 53  VAL   B O    1 ? 1 
ATOM   594  C CB   . VAL   A 1 41  ? 25.772 -7.675  6.567   1   56.748  ? 53  VAL   B CB   1 ? 1 
ATOM   595  C CG1  . VAL   A 1 41  ? 25.733 -6.648  5.454   1   57.212  ? 53  VAL   B CG1  1 ? 1 
ATOM   596  C CG2  . VAL   A 1 41  ? 25.202 -8.998  6.069   1   57.635  ? 53  VAL   B CG2  1 ? 1 
ATOM   597  H H    . VAL   A 1 41  ? 26.553 -8.676  8.882   1   60.751  ? 53  VAL   B H    1 c 1 
ATOM   598  H HA   . VAL   A 1 41  ? 27.765 -8.21   6.399   1   61.894  ? 53  VAL   B HA   1 c 1 
ATOM   599  H HB   . VAL   A 1 41  ? 25.21  -7.352  7.31    1   56.481  ? 53  VAL   B HB   1 c 1 
ATOM   600  H HG11 . VAL   A 1 41  ? 26.407 -6.866  4.79    1   58.041  ? 53  VAL   B HG11 1 c 1 
ATOM   601  H HG12 . VAL   A 1 41  ? 25.91  -5.764  5.817   1   56.4    ? 53  VAL   B HG12 1 c 1 
ATOM   602  H HG13 . VAL   A 1 41  ? 24.857 -6.656  5.038   1   54.768  ? 53  VAL   B HG13 1 c 1 
ATOM   603  H HG21 . VAL   A 1 41  ? 24.377 -8.835  5.582   1   55.574  ? 53  VAL   B HG21 1 c 1 
ATOM   604  H HG22 . VAL   A 1 41  ? 25.019 -9.58   6.826   1   58.233  ? 53  VAL   B HG22 1 c 1 
ATOM   605  H HG23 . VAL   A 1 41  ? 25.845 -9.427  5.479   1   59.029  ? 53  VAL   B HG23 1 c 1 
ATOM   606  N N    . TYR   A 1 42  ? 28.698 -5.972  6.876   1   62.486  ? 54  TYR   B N    1 ? 1 
ATOM   607  C CA   . TYR   A 1 42  ? 29.375 -4.734  7.254   1   63.98   ? 54  TYR   B CA   1 ? 1 
ATOM   608  C C    . TYR   A 1 42  ? 29.009 -3.636  6.234   1   59.677  ? 54  TYR   B C    1 ? 1 
ATOM   609  O O    . TYR   A 1 42  ? 29.267 -3.812  5.045   1   62.575  ? 54  TYR   B O    1 ? 1 
ATOM   610  C CB   . TYR   A 1 42  ? 30.897 -4.954  7.331   1   70.137  ? 54  TYR   B CB   1 ? 1 
ATOM   611  C CG   . TYR   A 1 42  ? 31.45  -6.061  8.237   1   77.064  ? 54  TYR   B CG   1 ? 1 
ATOM   612  C CD1  . TYR   A 1 42  ? 31.204 -7.408  7.969   1   78.381  ? 54  TYR   B CD1  1 ? 1 
ATOM   613  C CD2  . TYR   A 1 42  ? 32.277 -5.769  9.315   1   82.275  ? 54  TYR   B CD2  1 ? 1 
ATOM   614  C CE1  . TYR   A 1 42  ? 31.715 -8.419  8.768   1   85.647  ? 54  TYR   B CE1  1 ? 1 
ATOM   615  C CE2  . TYR   A 1 42  ? 32.803 -6.771  10.121  1   89.33   ? 54  TYR   B CE2  1 ? 1 
ATOM   616  C CZ   . TYR   A 1 42  ? 32.524 -8.099  9.843   1   89.907  ? 54  TYR   B CZ   1 ? 1 
ATOM   617  O OH   . TYR   A 1 42  ? 33.031 -9.101  10.617  1   103.621 ? 54  TYR   B OH   1 ? 1 
ATOM   618  H H    . TYR   A 1 42  ? 28.911 -6.355  6.074   1   62.765  ? 54  TYR   B H    1 c 1 
ATOM   619  H HA   . TYR   A 1 42  ? 29.052 -4.454  8.151   1   63.493  ? 54  TYR   B HA   1 c 1 
ATOM   620  H HB2  . TYR   A 1 42  ? 31.218 -5.124  6.418   1   71.128  ? 54  TYR   B HB2  1 c 1 
ATOM   621  H HB3  . TYR   A 1 42  ? 31.305 -4.104  7.609   1   71.984  ? 54  TYR   B HB3  1 c 1 
ATOM   622  H HD1  . TYR   A 1 42  ? 30.655 -7.638  7.237   1   76.781  ? 54  TYR   B HD1  1 c 1 
ATOM   623  H HD2  . TYR   A 1 42  ? 32.475 -4.867  9.515   1   83.328  ? 54  TYR   B HD2  1 c 1 
ATOM   624  H HE1  . TYR   A 1 42  ? 31.525 -9.32   8.572   1   84.926  ? 54  TYR   B HE1  1 c 1 
ATOM   625  H HE2  . TYR   A 1 42  ? 33.35  -6.549  10.855  1   91.479  ? 54  TYR   B HE2  1 c 1 
ATOM   626  H HH   . TYR   A 1 42  ? 32.724 -9.782  10.346  0   30      ? 54  TYR   B HH   1 c 1 
ATOM   627  N N    . VAL   A 1 43  ? 28.417 -2.507  6.672   1   55.348  ? 55  VAL   B N    1 ? 1 
ATOM   628  C CA   . VAL   A 1 43  ? 28.035 -1.453  5.741   1   54.241  ? 55  VAL   B CA   1 ? 1 
ATOM   629  C C    . VAL   A 1 43  ? 28.474 -0.079  6.248   1   59.172  ? 55  VAL   B C    1 ? 1 
ATOM   630  O O    . VAL   A 1 43  ? 28.674 0.09    7.443   1   62.632  ? 55  VAL   B O    1 ? 1 
ATOM   631  C CB   . VAL   A 1 43  ? 26.532 -1.359  5.441   1   51.015  ? 55  VAL   B CB   1 ? 1 
ATOM   632  C CG1  . VAL   A 1 43  ? 25.96  -2.724  5.078   1   48.001  ? 55  VAL   B CG1  1 ? 1 
ATOM   633  C CG2  . VAL   A 1 43  ? 25.751 -0.706  6.588   1   49.837  ? 55  VAL   B CG2  1 ? 1 
ATOM   634  H H    . VAL   A 1 43  ? 28.252 -2.396  7.563   1   56.245  ? 55  VAL   B H    1 c 1 
ATOM   635  H HA   . VAL   A 1 43  ? 28.496 -1.619  4.898   1   55.892  ? 55  VAL   B HA   1 c 1 
ATOM   636  H HB   . VAL   A 1 43  ? 26.431 -0.778  4.653   1   50.25   ? 55  VAL   B HB   1 c 1 
ATOM   637  H HG11 . VAL   A 1 43  ? 26.029 -3.32   5.843   1   48.985  ? 55  VAL   B HG11 1 c 1 
ATOM   638  H HG12 . VAL   A 1 43  ? 26.459 -3.097  4.332   1   49.542  ? 55  VAL   B HG12 1 c 1 
ATOM   639  H HG13 . VAL   A 1 43  ? 25.026 -2.628  4.827   1   46.363  ? 55  VAL   B HG13 1 c 1 
ATOM   640  H HG21 . VAL   A 1 43  ? 24.802 -0.771  6.404   1   47.662  ? 55  VAL   B HG21 1 c 1 
ATOM   641  H HG22 . VAL   A 1 43  ? 26     0.23    6.665   1   50.752  ? 55  VAL   B HG22 1 c 1 
ATOM   642  H HG23 . VAL   A 1 43  ? 25.951 -1.166  7.42    1   50.804  ? 55  VAL   B HG23 1 c 1 
ATOM   643  N N    . HIS   A 1 44  ? 28.508 0.897   5.332   1   58.551  ? 56  HIS   B N    1 ? 1 
ATOM   644  C CA   . HIS   A 1 44  ? 28.381 2.318   5.653   1   62.399  ? 56  HIS   B CA   1 ? 1 
ATOM   645  C C    . HIS   A 1 44  ? 27.054 2.829   5.083   1   59.867  ? 56  HIS   B C    1 ? 1 
ATOM   646  O O    . HIS   A 1 44  ? 26.602 2.343   4.059   1   57.658  ? 56  HIS   B O    1 ? 1 
ATOM   647  C CB   . HIS   A 1 44  ? 29.569 3.127   5.13    1   68.564  ? 56  HIS   B CB   1 ? 1 
ATOM   648  C CG   . HIS   A 1 44  ? 30.711 3.263   6.09    1   73.325  ? 56  HIS   B CG   1 ? 1 
ATOM   649  N ND1  . HIS   A 1 44  ? 30.565 3.731   7.384   1   72.699  ? 56  HIS   B ND1  1 ? 1 
ATOM   650  C CD2  . HIS   A 1 44  ? 32.016 3.016   5.92    1   75.594  ? 56  HIS   B CD2  1 ? 1 
ATOM   651  C CE1  . HIS   A 1 44  ? 31.753 3.75    7.961   1   78.919  ? 56  HIS   B CE1  1 ? 1 
ATOM   652  N NE2  . HIS   A 1 44  ? 32.641 3.321   7.092   1   79.225  ? 56  HIS   B NE2  1 ? 1 
ATOM   653  H H    . HIS   A 1 44  ? 28.62  0.664   4.455   1   59.337  ? 56  HIS   B H    1 c 1 
ATOM   654  H HA   . HIS   A 1 44  ? 28.346 2.405   6.636   1   62.738  ? 56  HIS   B HA   1 c 1 
ATOM   655  H HB2  . HIS   A 1 44  ? 29.897 2.701   4.308   1   68.612  ? 56  HIS   B HB2  1 c 1 
ATOM   656  H HB3  . HIS   A 1 44  ? 29.254 4.024   4.886   1   68.108  ? 56  HIS   B HB3  1 c 1 
ATOM   657  H HD1  . HIS   A 1 44  ? 29.807 4.014   7.757   0   30      ? 56  HIS   B HD1  1 c 1 
ATOM   658  H HD2  . HIS   A 1 44  ? 32.431 2.692   5.145   1   76.958  ? 56  HIS   B HD2  1 c 1 
ATOM   659  H HE1  . HIS   A 1 44  ? 31.93  4.02    8.846   1   80.024  ? 56  HIS   B HE1  1 c 1 
ATOM   660  H HE2  . HIS   A 1 44  ? 33.491 3.214   7.263   0   30      ? 56  HIS   B HE2  1 c 1 
ATOM   661  N N    . TYR   A 1 45  ? 26.423 3.796   5.76    1   58.433  ? 57  TYR   B N    1 ? 1 
ATOM   662  C CA   . TYR   A 1 45  ? 25.124 4.281   5.313   1   53.699  ? 57  TYR   B CA   1 ? 1 
ATOM   663  C C    . TYR   A 1 45  ? 24.963 5.74    5.684   1   53.969  ? 57  TYR   B C    1 ? 1 
ATOM   664  O O    . TYR   A 1 45  ? 25.595 6.222   6.62    1   53.345  ? 57  TYR   B O    1 ? 1 
ATOM   665  C CB   . TYR   A 1 45  ? 23.924 3.492   5.858   1   48.514  ? 57  TYR   B CB   1 ? 1 
ATOM   666  C CG   . TYR   A 1 45  ? 23.605 3.715   7.332   1   48.511  ? 57  TYR   B CG   1 ? 1 
ATOM   667  C CD1  . TYR   A 1 45  ? 24.283 3.004   8.331   1   50.731  ? 57  TYR   B CD1  1 ? 1 
ATOM   668  C CD2  . TYR   A 1 45  ? 22.673 4.657   7.733   1   44.532  ? 57  TYR   B CD2  1 ? 1 
ATOM   669  C CE1  . TYR   A 1 45  ? 24.026 3.213   9.672   1   49.751  ? 57  TYR   B CE1  1 ? 1 
ATOM   670  C CE2  . TYR   A 1 45  ? 22.461 4.925   9.077   1   46.591  ? 57  TYR   B CE2  1 ? 1 
ATOM   671  C CZ   . TYR   A 1 45  ? 23.099 4.168   10.048  1   48.742  ? 57  TYR   B CZ   1 ? 1 
ATOM   672  O OH   . TYR   A 1 45  ? 22.859 4.409   11.368  1   49.28   ? 57  TYR   B OH   1 ? 1 
ATOM   673  H H    . TYR   A 1 45  ? 26.803 4.158   6.508   1   59.962  ? 57  TYR   B H    1 c 1 
ATOM   674  H HA   . TYR   A 1 45  ? 25.106 4.216   4.325   1   53.166  ? 57  TYR   B HA   1 c 1 
ATOM   675  H HB2  . TYR   A 1 45  ? 23.132 3.73    5.326   1   47.27   ? 57  TYR   B HB2  1 c 1 
ATOM   676  H HB3  . TYR   A 1 45  ? 24.096 2.534   5.716   1   48.399  ? 57  TYR   B HB3  1 c 1 
ATOM   677  H HD1  . TYR   A 1 45  ? 24.913 2.347   8.081   1   50.738  ? 57  TYR   B HD1  1 c 1 
ATOM   678  H HD2  . TYR   A 1 45  ? 22.236 5.183   7.083   1   44.796  ? 57  TYR   B HD2  1 c 1 
ATOM   679  H HE1  . TYR   A 1 45  ? 24.488 2.72    10.328  1   51.516  ? 57  TYR   B HE1  1 c 1 
ATOM   680  H HE2  . TYR   A 1 45  ? 21.81  5.556   9.33    1   46.328  ? 57  TYR   B HE2  1 c 1 
ATOM   681  H HH   . TYR   A 1 45  ? 23.299 3.885   11.846  0   30      ? 57  TYR   B HH   1 c 1 
ATOM   682  N N    . LYS   A 1 46  ? 24.102 6.411   4.909   1   51.868  ? 58  LYS   B N    1 ? 1 
ATOM   683  C CA   . LYS   A 1 46  ? 23.534 7.694   5.261   1   52.744  ? 58  LYS   B CA   1 ? 1 
ATOM   684  C C    . LYS   A 1 46  ? 22.029 7.563   5.16    1   51.575  ? 58  LYS   B C    1 ? 1 
ATOM   685  O O    . LYS   A 1 46  ? 21.533 7.034   4.168   1   49.489  ? 58  LYS   B O    1 ? 1 
ATOM   686  C CB   . LYS   A 1 46  ? 24.07  8.753   4.306   1   54.247  ? 58  LYS   B CB   1 ? 1 
ATOM   687  C CG   . LYS   A 1 46  ? 25.577 8.947   4.395   1   59.028  ? 58  LYS   B CG   1 ? 1 
ATOM   688  C CD   . LYS   A 1 46  ? 26.027 9.874   3.267   1   61.376  ? 58  LYS   B CD   1 ? 1 
ATOM   689  C CE   . LYS   A 1 46  ? 27.499 9.987   3.056   1   67.077  ? 58  LYS   B CE   1 ? 1 
ATOM   690  N NZ   . LYS   A 1 46  ? 27.834 11.012  2.055   1   70.61   ? 58  LYS   B NZ   1 ? 1 
ATOM   691  H H    . LYS   A 1 46  ? 23.86  6.04    4.109   1   50.958  ? 58  LYS   B H    1 c 1 
ATOM   692  H HA   . LYS   A 1 46  ? 23.786 7.916   6.193   1   54.144  ? 58  LYS   B HA   1 c 1 
ATOM   693  H HB2  . LYS   A 1 46  ? 23.839 8.498   3.387   1   53.694  ? 58  LYS   B HB2  1 c 1 
ATOM   694  H HB3  . LYS   A 1 46  ? 23.631 9.609   4.499   1   55.325  ? 58  LYS   B HB3  1 c 1 
ATOM   695  H HG2  . LYS   A 1 46  ? 25.805 9.344   5.264   1   60.304  ? 58  LYS   B HG2  1 c 1 
ATOM   696  H HG3  . LYS   A 1 46  ? 26.026 8.079   4.31    1   58.311  ? 58  LYS   B HG3  1 c 1 
ATOM   697  H HD2  . LYS   A 1 46  ? 25.618 9.563   2.431   1   60.2    ? 58  LYS   B HD2  1 c 1 
ATOM   698  H HD3  . LYS   A 1 46  ? 25.67  10.771  3.448   1   62.757  ? 58  LYS   B HD3  1 c 1 
ATOM   699  H HE2  . LYS   A 1 46  ? 27.93  10.215  3.899   1   68.604  ? 58  LYS   B HE2  1 c 1 
ATOM   700  H HE3  . LYS   A 1 46  ? 27.85  9.128   2.759   1   66.103  ? 58  LYS   B HE3  1 c 1 
ATOM   701  H HZ1  . LYS   A 1 46  ? 27.525 11.819  2.328   1   71.532  ? 58  LYS   B HZ1  1 c 1 
ATOM   702  H HZ2  . LYS   A 1 46  ? 27.452 10.8    1.261   1   69.252  ? 58  LYS   B HZ2  1 c 1 
ATOM   703  H HZ3  . LYS   A 1 46  ? 28.733 11.056  1.951   1   73.626  ? 58  LYS   B HZ3  1 c 1 
ATOM   704  N N    . GLY   A 1 47  ? 21.306 7.976   6.192   1   50.979  ? 59  GLY   B N    1 ? 1 
ATOM   705  C CA   . GLY   A 1 47  ? 19.861 7.818   6.151   1   49.279  ? 59  GLY   B CA   1 ? 1 
ATOM   706  C C    . GLY   A 1 47  ? 19.184 9.122   6.535   1   47.147  ? 59  GLY   B C    1 ? 1 
ATOM   707  O O    . GLY   A 1 47  ? 19.775 9.91    7.244   1   49.896  ? 59  GLY   B O    1 ? 1 
ATOM   708  H H    . GLY   A 1 47  ? 21.702 8.358   6.922   1   52.951  ? 59  GLY   B H    1 c 1 
ATOM   709  H HA2  . GLY   A 1 47  ? 19.582 7.552   5.246   1   47.098  ? 59  GLY   B HA2  1 c 1 
ATOM   710  H HA3  . GLY   A 1 47  ? 19.593 7.105   6.778   1   47.154  ? 59  GLY   B HA3  1 c 1 
ATOM   711  N N    . LYS   A 1 48  ? 17.927 9.289   6.123   1   43.139  ? 60  LYS   B N    1 ? 1 
ATOM   712  C CA   . LYS   A 1 48  ? 17.121 10.424  6.517   1   46.41   ? 60  LYS   B CA   1 ? 1 
ATOM   713  C C    . LYS   A 1 48  ? 15.637 10.085  6.478   1   44.441  ? 60  LYS   B C    1 ? 1 
ATOM   714  O O    . LYS   A 1 48  ? 15.223 9.142   5.835   1   44.639  ? 60  LYS   B O    1 ? 1 
ATOM   715  C CB   . LYS   A 1 48  ? 17.401 11.633  5.607   1   51.149  ? 60  LYS   B CB   1 ? 1 
ATOM   716  C CG   . LYS   A 1 48  ? 17.211 11.406  4.137   1   50.983  ? 60  LYS   B CG   1 ? 1 
ATOM   717  C CD   . LYS   A 1 48  ? 17.514 12.623  3.259   1   57.525  ? 60  LYS   B CD   1 ? 1 
ATOM   718  C CE   . LYS   A 1 48  ? 16.528 13.712  3.404   1   61.265  ? 60  LYS   B CE   1 ? 1 
ATOM   719  N NZ   . LYS   A 1 48  ? 16.867 14.782  2.446   1   68.819  ? 60  LYS   B NZ   1 ? 1 
ATOM   720  H H    . LYS   A 1 48  ? 17.557 8.662   5.57    1   42.581  ? 60  LYS   B H    1 c 1 
ATOM   721  H HA   . LYS   A 1 48  ? 17.361 10.664  7.446   1   47.71   ? 60  LYS   B HA   1 c 1 
ATOM   722  H HB2  . LYS   A 1 48  ? 16.815 12.369  5.883   1   51.826  ? 60  LYS   B HB2  1 c 1 
ATOM   723  H HB3  . LYS   A 1 48  ? 18.327 11.922  5.755   1   52.569  ? 60  LYS   B HB3  1 c 1 
ATOM   724  H HG2  . LYS   A 1 48  ? 17.792 10.664  3.86    1   50.708  ? 60  LYS   B HG2  1 c 1 
ATOM   725  H HG3  . LYS   A 1 48  ? 16.282 11.128  3.983   1   50.061  ? 60  LYS   B HG3  1 c 1 
ATOM   726  H HD2  . LYS   A 1 48  ? 18.404 12.967  3.49    1   59.123  ? 60  LYS   B HD2  1 c 1 
ATOM   727  H HD3  . LYS   A 1 48  ? 17.538 12.337  2.32    1   56.855  ? 60  LYS   B HD3  1 c 1 
ATOM   728  H HE2  . LYS   A 1 48  ? 15.631 13.381  3.217   1   60.035  ? 60  LYS   B HE2  1 c 1 
ATOM   729  H HE3  . LYS   A 1 48  ? 16.549 14.07   4.309   1   62.413  ? 60  LYS   B HE3  1 c 1 
ATOM   730  H HZ1  . LYS   A 1 48  ? 16.816 14.466  1.599   1   66.808  ? 60  LYS   B HZ1  1 c 1 
ATOM   731  H HZ2  . LYS   A 1 48  ? 17.709 15.08   2.603   1   69.104  ? 60  LYS   B HZ2  1 c 1 
ATOM   732  H HZ3  . LYS   A 1 48  ? 16.287 15.471  2.541   1   68.57   ? 60  LYS   B HZ3  1 c 1 
ATOM   733  N N    . LEU   A 1 49  ? 14.836 10.907  7.142   1   45.947  ? 61  LEU   B N    1 ? 1 
ATOM   734  C CA   . LEU   A 1 49  ? 13.393 10.801  7.073   1   46.138  ? 61  LEU   B CA   1 ? 1 
ATOM   735  C C    . LEU   A 1 49  ? 12.997 11.557  5.824   1   45.202  ? 61  LEU   B C    1 ? 1 
ATOM   736  O O    . LEU   A 1 49  ? 13.685 12.504  5.462   1   44.738  ? 61  LEU   B O    1 ? 1 
ATOM   737  C CB   . LEU   A 1 49  ? 12.774 11.463  8.307   1   48.768  ? 61  LEU   B CB   1 ? 1 
ATOM   738  C CG   . LEU   A 1 49  ? 13.191 10.899  9.662   1   54.287  ? 61  LEU   B CG   1 ? 1 
ATOM   739  C CD1  . LEU   A 1 49  ? 12.614 11.671  10.82   1   56.485  ? 61  LEU   B CD1  1 ? 1 
ATOM   740  C CD2  . LEU   A 1 49  ? 12.745 9.473   9.669   1   54.766  ? 61  LEU   B CD2  1 ? 1 
ATOM   741  H H    . LEU   A 1 49  ? 15.203 11.564  7.661   1   48.044  ? 61  LEU   B H    1 c 1 
ATOM   742  H HA   . LEU   A 1 49  ? 13.122 9.85    7.009   1   44.107  ? 61  LEU   B HA   1 c 1 
ATOM   743  H HB2  . LEU   A 1 49  ? 13.009 12.419  8.287   1   51.63   ? 61  LEU   B HB2  1 c 1 
ATOM   744  H HB3  . LEU   A 1 49  ? 11.794 11.399  8.23    1   49.396  ? 61  LEU   B HB3  1 c 1 
ATOM   745  H HG   . LEU   A 1 49  ? 14.181 10.923  9.725   1   54.143  ? 61  LEU   B HG   1 c 1 
ATOM   746  H HD11 . LEU   A 1 49  ? 12.929 12.59   10.787  1   58.528  ? 61  LEU   B HD11 1 c 1 
ATOM   747  H HD12 . LEU   A 1 49  ? 12.897 11.263  11.656  1   57.127  ? 61  LEU   B HD12 1 c 1 
ATOM   748  H HD13 . LEU   A 1 49  ? 11.644 11.66   10.767  1   56.37   ? 61  LEU   B HD13 1 c 1 
ATOM   749  H HD21 . LEU   A 1 49  ? 13.34  8.945   9.112   1   52.458  ? 61  LEU   B HD21 1 c 1 
ATOM   750  H HD22 . LEU   A 1 49  ? 11.838 9.411   9.325   1   53.154  ? 61  LEU   B HD22 1 c 1 
ATOM   751  H HD23 . LEU   A 1 49  ? 12.769 9.13    10.578  1   54.324  ? 61  LEU   B HD23 1 c 1 
ATOM   752  N N    . SER   A 1 50  ? 11.888 11.162  5.181   1   47.225  ? 62  SER   B N    1 ? 1 
ATOM   753  C CA   . SER   A 1 50  ? 11.302 11.988  4.129   1   53.497  ? 62  SER   B CA   1 ? 1 
ATOM   754  C C    . SER   A 1 50  ? 10.916 13.387  4.579   1   53.639  ? 62  SER   B C    1 ? 1 
ATOM   755  O O    . SER   A 1 50  ? 10.976 14.286  3.758   1   59.97   ? 62  SER   B O    1 ? 1 
ATOM   756  C CB   . SER   A 1 50  ? 10.111 11.345  3.514   1   56.017  ? 62  SER   B CB   1 ? 1 
ATOM   757  O OG   . SER   A 1 50  ? 10.602 10.144  2.977   1   63.739  ? 62  SER   B OG   1 ? 1 
ATOM   758  H H    . SER   A 1 50  ? 11.49  10.369  5.399   1   46.115  ? 62  SER   B H    1 c 1 
ATOM   759  H HA   . SER   A 1 50  ? 11.988 12.087  3.42    1   52.974  ? 62  SER   B HA   1 c 1 
ATOM   760  H HB2  . SER   A 1 50  ? 9.431  11.166  4.19    1   57.087  ? 62  SER   B HB2  1 c 1 
ATOM   761  H HB3  . SER   A 1 50  ? 9.743  11.911  2.808   1   58.493  ? 62  SER   B HB3  1 c 1 
ATOM   762  H HG   . SER   A 1 50  ? 9.821  9.724   2.718   0   30      ? 62  SER   B HG   1 c 1 
ATOM   763  N N    . ASN   A 1 51  ? 10.549 13.6    5.845   1   55.355  ? 63  ASN   B N    1 ? 1 
ATOM   764  C CA   . ASN   A 1 51  ? 10.19  14.937  6.301   1   60.423  ? 63  ASN   B CA   1 ? 1 
ATOM   765  C C    . ASN   A 1 51  ? 11.397 15.889  6.399   1   61.437  ? 63  ASN   B C    1 ? 1 
ATOM   766  O O    . ASN   A 1 51  ? 11.213 17.063  6.712   1   62.743  ? 63  ASN   B O    1 ? 1 
ATOM   767  C CB   . ASN   A 1 51  ? 9.416  14.898  7.613   1   62.545  ? 63  ASN   B CB   1 ? 1 
ATOM   768  C CG   . ASN   A 1 51  ? 10.288 14.588  8.812   1   66.528  ? 63  ASN   B CG   1 ? 1 
ATOM   769  O OD1  . ASN   A 1 51  ? 11.502 14.346  8.687   1   61.665  ? 63  ASN   B OD1  1 ? 1 
ATOM   770  N ND2  . ASN   A 1 51  ? 9.694  14.626  9.998   1   69.374  ? 63  ASN   B ND2  1 ? 1 
ATOM   771  H H    . ASN   A 1 51  ? 10.512 12.903  6.435   1   54.244  ? 63  ASN   B H    1 c 1 
ATOM   772  H HA   . ASN   A 1 51  ? 9.579  15.317  5.629   1   60.852  ? 63  ASN   B HA   1 c 1 
ATOM   773  H HB2  . ASN   A 1 51  ? 8.982  15.763  7.751   1   65.4    ? 63  ASN   B HB2  1 c 1 
ATOM   774  H HB3  . ASN   A 1 51  ? 8.715  14.219  7.547   1   61.723  ? 63  ASN   B HB3  1 c 1 
ATOM   775  H HD21 . ASN   A 1 51  ? 10.177 14.542  10.737  1   69.502  ? 63  ASN   B HD21 1 c 1 
ATOM   776  H HD22 . ASN   A 1 51  ? 8.815  14.734  10.051  1   69.432  ? 63  ASN   B HD22 1 c 1 
ATOM   777  N N    . GLY   A 1 52  ? 12.619 15.415  6.129   1   60.804  ? 64  GLY   B N    1 ? 1 
ATOM   778  C CA   . GLY   A 1 52  ? 13.791 16.287  6.052   1   63.601  ? 64  GLY   B CA   1 ? 1 
ATOM   779  C C    . GLY   A 1 52  ? 14.375 16.673  7.425   1   66.58   ? 64  GLY   B C    1 ? 1 
ATOM   780  O O    . GLY   A 1 52  ? 15.304 17.474  7.507   1   67.968  ? 64  GLY   B O    1 ? 1 
ATOM   781  H H    . GLY   A 1 52  ? 12.737 14.517  6.008   1   58.439  ? 64  GLY   B H    1 c 1 
ATOM   782  H HA2  . GLY   A 1 52  ? 14.487 15.83   5.525   1   62.82   ? 64  GLY   B HA2  1 c 1 
ATOM   783  H HA3  . GLY   A 1 52  ? 13.543 17.108  5.565   1   65.782  ? 64  GLY   B HA3  1 c 1 
ATOM   784  N N    . LYS   A 1 53  ? 13.837 16.115  8.516   1   64.473  ? 65  LYS   B N    1 ? 1 
ATOM   785  C CA   . LYS   A 1 53  ? 14.059 16.666  9.842   1   70.819  ? 65  LYS   B CA   1 ? 1 
ATOM   786  C C    . LYS   A 1 53  ? 15.08  15.818  10.613  1   69.129  ? 65  LYS   B C    1 ? 1 
ATOM   787  O O    . LYS   A 1 53  ? 15.552 16.255  11.659  1   71.989  ? 65  LYS   B O    1 ? 1 
ATOM   788  C CB   . LYS   A 1 53  ? 12.73  16.944  10.57   1   71.328  ? 65  LYS   B CB   1 ? 1 
ATOM   789  H H    . LYS   A 1 53  ? 13.321 15.365  8.432   1   63.046  ? 65  LYS   B H    1 c 1 
ATOM   790  H HA   . LYS   A 1 53  ? 14.472 17.559  9.721   1   72.669  ? 65  LYS   B HA   1 c 1 
ATOM   791  H HB2  . LYS   A 1 53  ? 12.938 17.037  11.587  0   30      ? 65  LYS   B HB2  1 c 1 
ATOM   792  H HB3  . LYS   A 1 53  ? 11.983 16.718  10.025  0   30      ? 65  LYS   B HB3  1 c 1 
ATOM   793  N N    . LYS   A 1 54  ? 15.472 14.634  10.116  1   65.835  ? 66  LYS   B N    1 ? 1 
ATOM   794  C CA   . LYS   A 1 54  ? 16.514 13.862  10.797  1   62.753  ? 66  LYS   B CA   1 ? 1 
ATOM   795  C C    . LYS   A 1 54  ? 17.405 13.178  9.769   1   60.224  ? 66  LYS   B C    1 ? 1 
ATOM   796  O O    . LYS   A 1 54  ? 16.909 12.63   8.774   1   56.988  ? 66  LYS   B O    1 ? 1 
ATOM   797  C CB   . LYS   A 1 54  ? 15.984 12.818  11.791  1   59.995  ? 66  LYS   B CB   1 ? 1 
ATOM   798  H H    . LYS   A 1 54  ? 15.09  14.298  9.357   1   62.996  ? 66  LYS   B H    1 c 1 
ATOM   799  H HA   . LYS   A 1 54  ? 17.075 14.497  11.31   1   65.924  ? 66  LYS   B HA   1 c 1 
ATOM   800  H HB2  . LYS   A 1 54  ? 16.739 12.444  12.236  0   30      ? 66  LYS   B HB2  1 c 1 
ATOM   801  H HB3  . LYS   A 1 54  ? 15.006 12.929  11.77   0   30      ? 66  LYS   B HB3  1 c 1 
ATOM   802  N N    . PHE   A 1 55  ? 18.714 13.222  10.047  1   57.274  ? 67  PHE   B N    1 ? 1 
ATOM   803  C CA   . PHE   A 1 55  ? 19.752 12.555  9.271   1   57.879  ? 67  PHE   B CA   1 ? 1 
ATOM   804  C C    . PHE   A 1 55  ? 20.645 11.754  10.212  1   60.921  ? 67  PHE   B C    1 ? 1 
ATOM   805  O O    . PHE   A 1 55  ? 20.933 12.188  11.328  1   63.669  ? 67  PHE   B O    1 ? 1 
ATOM   806  C CB   . PHE   A 1 55  ? 20.673 13.545  8.553   1   60.864  ? 67  PHE   B CB   1 ? 1 
ATOM   807  C CG   . PHE   A 1 55  ? 19.856 14.587  7.818   1   64.05   ? 67  PHE   B CG   1 ? 1 
ATOM   808  C CD1  . PHE   A 1 55  ? 19.272 15.655  8.504   1   68.562  ? 67  PHE   B CD1  1 ? 1 
ATOM   809  C CD2  . PHE   A 1 55  ? 19.619 14.46   6.45    1   64.992  ? 67  PHE   B CD2  1 ? 1 
ATOM   810  C CE1  . PHE   A 1 55  ? 18.518 16.613  7.824   1   73.444  ? 67  PHE   B CE1  1 ? 1 
ATOM   811  C CE2  . PHE   A 1 55  ? 18.862 15.417  5.774   1   67.505  ? 67  PHE   B CE2  1 ? 1 
ATOM   812  C CZ   . PHE   A 1 55  ? 18.305 16.487  6.457   1   70.034  ? 67  PHE   B CZ   1 ? 1 
ATOM   813  H H    . PHE   A 1 55  ? 18.978 13.706  10.776  1   61.381  ? 67  PHE   B H    1 c 1 
ATOM   814  H HA   . PHE   A 1 55  ? 19.333 11.947  8.608   1   55.205  ? 67  PHE   B HA   1 c 1 
ATOM   815  H HB2  . PHE   A 1 55  ? 21.25  13.989  9.214   1   64.485  ? 67  PHE   B HB2  1 c 1 
ATOM   816  H HB3  . PHE   A 1 55  ? 21.234 13.056  7.911   1   60.828  ? 67  PHE   B HB3  1 c 1 
ATOM   817  H HD1  . PHE   A 1 55  ? 19.421 15.749  9.431   1   70.382  ? 67  PHE   B HD1  1 c 1 
ATOM   818  H HD2  . PHE   A 1 55  ? 20     13.739  5.974   1   63.191  ? 67  PHE   B HD2  1 c 1 
ATOM   819  H HE1  . PHE   A 1 55  ? 18.141 17.337  8.296   1   74.056  ? 67  PHE   B HE1  1 c 1 
ATOM   820  H HE2  . PHE   A 1 55  ? 18.72  15.329  4.845   1   66.395  ? 67  PHE   B HE2  1 c 1 
ATOM   821  H HZ   . PHE   A 1 55  ? 17.788 17.128  5.995   1   71.344  ? 67  PHE   B HZ   1 c 1 
ATOM   822  N N    . ASP   A 1 56  ? 21.213 10.682  9.696   1   56.946  ? 68  ASP   B N    1 ? 1 
ATOM   823  C CA   . ASP   A 1 56  ? 22.013 9.804   10.524  1   60.32   ? 68  ASP   B CA   1 ? 1 
ATOM   824  C C    . ASP   A 1 56  ? 22.979 9.097   9.594   1   59.435  ? 68  ASP   B C    1 ? 1 
ATOM   825  O O    . ASP   A 1 56  ? 22.574 8.644   8.533   1   53.058  ? 68  ASP   B O    1 ? 1 
ATOM   826  C CB   . ASP   A 1 56  ? 21.126 8.771   11.222  1   58.636  ? 68  ASP   B CB   1 ? 1 
ATOM   827  C CG   . ASP   A 1 56  ? 21.858 7.6     11.859  1   59.204  ? 68  ASP   B CG   1 ? 1 
ATOM   828  O OD1  . ASP   A 1 56  ? 22.799 7.846   12.627  1   63.757  ? 68  ASP   B OD1  1 ? 1 
ATOM   829  O OD2  . ASP   A 1 56  ? 21.509 6.454   11.541  1   53.468  ? 68  ASP   B OD2  1 ? 1 
ATOM   830  H H    . ASP   A 1 56  ? 21.105 10.487  8.81    1   56.397  ? 68  ASP   B H    1 c 1 
ATOM   831  H HA   . ASP   A 1 56  ? 22.514 10.338  11.181  1   62.941  ? 68  ASP   B HA   1 c 1 
ATOM   832  H HB2  . ASP   A 1 56  ? 20.605 9.223   11.918  1   59.357  ? 68  ASP   B HB2  1 c 1 
ATOM   833  H HB3  . ASP   A 1 56  ? 20.498 8.414   10.559  1   55.749  ? 68  ASP   B HB3  1 c 1 
ATOM   834  N N    . SER   A 1 57  ? 24.233 8.974   10.006  1   62.376  ? 69  SER   B N    1 ? 1 
ATOM   835  C CA   . SER   A 1 57  ? 25.22  8.316   9.18    1   63.793  ? 69  SER   B CA   1 ? 1 
ATOM   836  C C    . SER   A 1 57  ? 26.106 7.442   10.046  1   66.633  ? 69  SER   B C    1 ? 1 
ATOM   837  O O    . SER   A 1 57  ? 26.526 7.864   11.123  1   73.63   ? 69  SER   B O    1 ? 1 
ATOM   838  C CB   . SER   A 1 57  ? 26.048 9.297   8.415   1   69.947  ? 69  SER   B CB   1 ? 1 
ATOM   839  O OG   . SER   A 1 57  ? 27.203 8.643   7.918   1   76.534  ? 69  SER   B OG   1 ? 1 
ATOM   840  H H    . SER   A 1 57  ? 24.482 9.306   10.82   1   65.044  ? 69  SER   B H    1 c 1 
ATOM   841  H HA   . SER   A 1 57  ? 24.748 7.734   8.534   1   61.299  ? 69  SER   B HA   1 c 1 
ATOM   842  H HB2  . SER   A 1 57  ? 25.527 9.658   7.673   1   68.999  ? 69  SER   B HB2  1 c 1 
ATOM   843  H HB3  . SER   A 1 57  ? 26.311 10.032  9.001   1   73.213  ? 69  SER   B HB3  1 c 1 
ATOM   844  H HG   . SER   A 1 57  ? 27.65  9.294   7.414   0   30      ? 69  SER   B HG   1 c 1 
ATOM   845  N N    . SER   A 1 58  ? 26.467 6.271   9.513   1   64.048  ? 70  SER   B N    1 ? 1 
ATOM   846  C CA   . SER   A 1 58  ? 27.44  5.41    10.155  1   69.313  ? 70  SER   B CA   1 ? 1 
ATOM   847  C C    . SER   A 1 58  ? 28.739 6.184   10.382  1   76.799  ? 70  SER   B C    1 ? 1 
ATOM   848  O O    . SER   A 1 58  ? 29.422 5.953   11.386  1   86.168  ? 70  SER   B O    1 ? 1 
ATOM   849  C CB   . SER   A 1 58  ? 27.66  4.163   9.356   1   65.824  ? 70  SER   B CB   1 ? 1 
ATOM   850  O OG   . SER   A 1 58  ? 28.034 4.486   8.026   1   64.325  ? 70  SER   B OG   1 ? 1 
ATOM   851  H H    . SER   A 1 58  ? 26.092 6.001   8.724   1   62.66   ? 70  SER   B H    1 c 1 
ATOM   852  H HA   . SER   A 1 58  ? 27.079 5.151   11.041  1   68.645  ? 70  SER   B HA   1 c 1 
ATOM   853  H HB2  . SER   A 1 58  ? 28.364 3.63    9.773   1   67.75   ? 70  SER   B HB2  1 c 1 
ATOM   854  H HB3  . SER   A 1 58  ? 26.84  3.635   9.346   1   62.835  ? 70  SER   B HB3  1 c 1 
ATOM   855  H HG   . SER   A 1 58  ? 28.14  3.81    7.632   0   30      ? 70  SER   B HG   1 c 1 
ATOM   856  N N    . HIS   A 1 59  ? 29.06  7.116   9.468   1   76.849  ? 71  HIS   B N    1 ? 1 
ATOM   857  C CA   . HIS   A 1 59  ? 30.312 7.864   9.535   1   86.099  ? 71  HIS   B CA   1 ? 1 
ATOM   858  C C    . HIS   A 1 59  ? 30.383 8.764   10.768  1   89.684  ? 71  HIS   B C    1 ? 1 
ATOM   859  O O    . HIS   A 1 59  ? 31.461 8.968   11.309  1   87.951  ? 71  HIS   B O    1 ? 1 
ATOM   860  C CB   . HIS   A 1 59  ? 30.541 8.677   8.26    1   85.505  ? 71  HIS   B CB   1 ? 1 
ATOM   861  C CG   . HIS   A 1 59  ? 30.899 7.82    7.103   1   85.616  ? 71  HIS   B CG   1 ? 1 
ATOM   862  N ND1  . HIS   A 1 59  ? 30.028 7.508   6.077   1   81.944  ? 71  HIS   B ND1  1 ? 1 
ATOM   863  C CD2  . HIS   A 1 59  ? 32.055 7.199   6.829   1   90.755  ? 71  HIS   B CD2  1 ? 1 
ATOM   864  C CE1  . HIS   A 1 59  ? 30.647 6.735   5.198   1   81.618  ? 71  HIS   B CE1  1 ? 1 
ATOM   865  N NE2  . HIS   A 1 59  ? 31.877 6.515   5.647   1   88.218  ? 71  HIS   B NE2  1 ? 1 
ATOM   866  H H    . HIS   A 1 59  ? 28.492 7.277   8.771   1   75.527  ? 71  HIS   B H    1 c 1 
ATOM   867  H HA   . HIS   A 1 59  ? 31.041 7.2     9.604   1   86.555  ? 71  HIS   B HA   1 c 1 
ATOM   868  H HB2  . HIS   A 1 59  ? 29.724 9.179   8.05    1   84.161  ? 71  HIS   B HB2  1 c 1 
ATOM   869  H HB3  . HIS   A 1 59  ? 31.266 9.321   8.419   1   90.428  ? 71  HIS   B HB3  1 c 1 
ATOM   870  H HD1  . HIS   A 1 59  ? 29.153 7.814   6.014   0   30      ? 71  HIS   B HD1  1 c 1 
ATOM   871  H HD2  . HIS   A 1 59  ? 32.837 7.211   7.345   1   93.69   ? 71  HIS   B HD2  1 c 1 
ATOM   872  H HE1  . HIS   A 1 59  ? 30.272 6.38    4.411   1   80.196  ? 71  HIS   B HE1  1 c 1 
ATOM   873  H HE2  . HIS   A 1 59  ? 32.396 5.997   5.189   0   30      ? 71  HIS   B HE2  1 c 1 
ATOM   874  N N    . ASP   A 1 60  ? 29.221 9.26    11.219  1   93.965  ? 72  ASP   B N    1 ? 1 
ATOM   875  C CA   . ASP   A 1 60  ? 29.095 9.973   12.485  1   100.112 ? 72  ASP   B CA   1 ? 1 
ATOM   876  C C    . ASP   A 1 60  ? 29.779 9.21    13.622  1   101.558 ? 72  ASP   B C    1 ? 1 
ATOM   877  O O    . ASP   A 1 60  ? 30.299 9.82    14.536  1   112.546 ? 72  ASP   B O    1 ? 1 
ATOM   878  C CB   . ASP   A 1 60  ? 27.637 10.168  12.888  1   96.912  ? 72  ASP   B CB   1 ? 1 
ATOM   879  C CG   . ASP   A 1 60  ? 26.772 10.971  11.925  1   91.623  ? 72  ASP   B CG   1 ? 1 
ATOM   880  O OD1  . ASP   A 1 60  ? 27.32  11.917  11.322  1   89.676  ? 72  ASP   B OD1  1 ? 1 
ATOM   881  O OD2  . ASP   A 1 60  ? 25.56  10.656  11.81   1   84.963  ? 72  ASP   B OD2  1 ? 1 
ATOM   882  H H    . ASP   A 1 60  ? 28.471 9.15    10.708  1   89.277  ? 72  ASP   B H    1 c 1 
ATOM   883  H HA   . ASP   A 1 60  ? 29.522 10.855  12.391  1   102.682 ? 72  ASP   B HA   1 c 1 
ATOM   884  H HB2  . ASP   A 1 60  ? 27.224 9.289   13.016  1   93.138  ? 72  ASP   B HB2  1 c 1 
ATOM   885  H HB3  . ASP   A 1 60  ? 27.619 10.629  13.752  1   98.853  ? 72  ASP   B HB3  1 c 1 
ATOM   886  N N    . ARG   A 1 61  ? 29.715 7.874   13.588  1   99.101  ? 73  ARG   B N    1 ? 1 
ATOM   887  C CA   . ARG   A 1 61  ? 30.281 7.012   14.617  1   97.42   ? 73  ARG   B CA   1 ? 1 
ATOM   888  C C    . ARG   A 1 61  ? 31.718 6.608   14.252  1   96.245  ? 73  ARG   B C    1 ? 1 
ATOM   889  O O    . ARG   A 1 61  ? 32.342 5.846   14.979  1   99.231  ? 73  ARG   B O    1 ? 1 
ATOM   890  C CB   . ARG   A 1 61  ? 29.309 5.827   14.796  1   88.154  ? 73  ARG   B CB   1 ? 1 
ATOM   891  H H    . ARG   A 1 61  ? 29.282 7.478   12.888  1   94.196  ? 73  ARG   B H    1 c 1 
ATOM   892  H HA   . ARG   A 1 61  ? 30.307 7.519   15.468  1   99.503  ? 73  ARG   B HA   1 c 1 
ATOM   893  H HB2  . ARG   A 1 61  ? 29.87  5.065   15.007  0   30      ? 73  ARG   B HB2  1 c 1 
ATOM   894  H HB3  . ARG   A 1 61  ? 28.414 6.204   14.812  0   30      ? 73  ARG   B HB3  1 c 1 
ATOM   895  N N    . ASN   A 1 62  ? 32.246 7.103   13.123  1   93.727  ? 74  ASN   B N    1 ? 1 
ATOM   896  C CA   . ASN   A 1 62  ? 33.584 6.755   12.658  1   94.973  ? 74  ASN   B CA   1 ? 1 
ATOM   897  C C    . ASN   A 1 62  ? 33.758 5.233   12.684  1   93.01   ? 74  ASN   B C    1 ? 1 
ATOM   898  O O    . ASN   A 1 62  ? 34.817 4.742   13.036  1   97.801  ? 74  ASN   B O    1 ? 1 
ATOM   899  C CB   . ASN   A 1 62  ? 34.67  7.538   13.407  1   103.412 ? 74  ASN   B CB   1 ? 1 
ATOM   900  H H    . ASN   A 1 62  ? 31.754 7.684   12.621  1   92.232  ? 74  ASN   B H    1 c 1 
ATOM   901  H HA   . ASN   A 1 62  ? 33.642 7.033   11.716  1   94.644  ? 74  ASN   B HA   1 c 1 
ATOM   902  H HB2  . ASN   A 1 62  ? 35.53  7.196   13.156  0   30      ? 74  ASN   B HB2  1 c 1 
ATOM   903  H HB3  . ASN   A 1 62  ? 34.222 8.135   14.063  0   30      ? 74  ASN   B HB3  1 c 1 
ATOM   904  N N    . GLU   A 1 63  ? 32.74  4.451   12.277  1   90.119  ? 75  GLU   B N    1 ? 1 
ATOM   905  C CA   . GLU   A 1 63  ? 32.927 3.005   12.199  1   88.448  ? 75  GLU   B CA   1 ? 1 
ATOM   906  C C    . GLU   A 1 63  ? 31.807 2.354   11.39   1   78.517  ? 75  GLU   B C    1 ? 1 
ATOM   907  O O    . GLU   A 1 63  ? 30.68  2.851   11.383  1   73.523  ? 75  GLU   B O    1 ? 1 
ATOM   908  C CB   . GLU   A 1 63  ? 32.993 2.331   13.574  1   92.349  ? 75  GLU   B CB   1 ? 1 
ATOM   909  C CG   . GLU   A 1 63  ? 31.716 2.495   14.396  1   91.643  ? 75  GLU   B CG   1 ? 1 
ATOM   910  C CD   . GLU   A 1 63  ? 31.674 1.602   15.627  1   93.854  ? 75  GLU   B CD   1 ? 1 
ATOM   911  O OE1  . GLU   A 1 63  ? 30.574 1.028   15.858  1   90.011  ? 75  GLU   B OE1  1 ? 1 
ATOM   912  O OE2  . GLU   A 1 63  ? 32.721 1.458   16.316  1   97.128  ? 75  GLU   B OE2  1 ? 1 
ATOM   913  H H    . GLU   A 1 63  ? 31.936 4.815   12.041  1   86.24   ? 75  GLU   B H    1 c 1 
ATOM   914  H HA   . GLU   A 1 63  ? 33.785 2.833   11.74   1   90.631  ? 75  GLU   B HA   1 c 1 
ATOM   915  H HB2  . GLU   A 1 63  ? 33.165 1.375   13.448  1   91.896  ? 75  GLU   B HB2  1 c 1 
ATOM   916  H HB3  . GLU   A 1 63  ? 33.745 2.705   14.077  1   96.849  ? 75  GLU   B HB3  1 c 1 
ATOM   917  H HG2  . GLU   A 1 63  ? 31.636 3.428   14.684  1   92.566  ? 75  GLU   B HG2  1 c 1 
ATOM   918  H HG3  . GLU   A 1 63  ? 30.94  2.287   13.836  1   86.905  ? 75  GLU   B HG3  1 c 1 
ATOM   919  N N    . PRO   A 1 64  ? 32.079 1.216   10.701  1   76.872  ? 76  PRO   B N    1 ? 1 
ATOM   920  C CA   . PRO   A 1 64  ? 31.036 0.494   9.985   1   72.246  ? 76  PRO   B CA   1 ? 1 
ATOM   921  C C    . PRO   A 1 64  ? 29.858 0.148   10.887  1   68.627  ? 76  PRO   B C    1 ? 1 
ATOM   922  O O    . PRO   A 1 64  ? 30.026 0.01    12.089  1   71.745  ? 76  PRO   B O    1 ? 1 
ATOM   923  C CB   . PRO   A 1 64  ? 31.723 -0.779  9.499   1   73.313  ? 76  PRO   B CB   1 ? 1 
ATOM   924  C CG   . PRO   A 1 64  ? 33.206 -0.543  9.626   1   80.927  ? 76  PRO   B CG   1 ? 1 
ATOM   925  C CD   . PRO   A 1 64  ? 33.391 0.541   10.645  1   83.367  ? 76  PRO   B CD   1 ? 1 
ATOM   926  H HA   . PRO   A 1 64  ? 30.729 1.026   9.222   1   70.357  ? 76  PRO   B HA   1 c 1 
ATOM   927  H HB2  . PRO   A 1 64  ? 31.451 -1.546  10.04   1   73.213  ? 76  PRO   B HB2  1 c 1 
ATOM   928  H HB3  . PRO   A 1 64  ? 31.484 -0.963  8.569   1   71.808  ? 76  PRO   B HB3  1 c 1 
ATOM   929  H HG2  . PRO   A 1 64  ? 33.66  -1.36   9.915   1   82.131  ? 76  PRO   B HG2  1 c 1 
ATOM   930  H HG3  . PRO   A 1 64  ? 33.584 -0.267  8.767   1   80.998  ? 76  PRO   B HG3  1 c 1 
ATOM   931  H HD2  . PRO   A 1 64  ? 33.623 0.168   11.517  1   84.958  ? 76  PRO   B HD2  1 c 1 
ATOM   932  H HD3  . PRO   A 1 64  ? 34.088 1.165   10.368  1   85.82   ? 76  PRO   B HD3  1 c 1 
ATOM   933  N N    . PHE   A 1 65  ? 28.673 0.032   10.297  1   63.582  ? 77  PHE   B N    1 ? 1 
ATOM   934  C CA   . PHE   A 1 65  ? 27.5   -0.539  10.924  1   63.625  ? 77  PHE   B CA   1 ? 1 
ATOM   935  C C    . PHE   A 1 65  ? 27.457 -2.029  10.598  1   63.352  ? 77  PHE   B C    1 ? 1 
ATOM   936  O O    . PHE   A 1 65  ? 27.493 -2.398  9.431   1   64.818  ? 77  PHE   B O    1 ? 1 
ATOM   937  C CB   . PHE   A 1 65  ? 26.268 0.149   10.335  1   63.274  ? 77  PHE   B CB   1 ? 1 
ATOM   938  C CG   . PHE   A 1 65  ? 24.99  -0.284  11.014  1   60.406  ? 77  PHE   B CG   1 ? 1 
ATOM   939  C CD1  . PHE   A 1 65  ? 24.592 0.3     12.211  1   62.774  ? 77  PHE   B CD1  1 ? 1 
ATOM   940  C CD2  . PHE   A 1 65  ? 24.193 -1.272  10.459  1   58.8    ? 77  PHE   B CD2  1 ? 1 
ATOM   941  C CE1  . PHE   A 1 65  ? 23.44  -0.113  12.852  1   60.765  ? 77  PHE   B CE1  1 ? 1 
ATOM   942  C CE2  . PHE   A 1 65  ? 23.05  -1.687  11.111  1   56.782  ? 77  PHE   B CE2  1 ? 1 
ATOM   943  C CZ   . PHE   A 1 65  ? 22.684 -1.12   12.309  1   61.584  ? 77  PHE   B CZ   1 ? 1 
ATOM   944  H H    . PHE   A 1 65  ? 28.592 0.331   9.437   1   63.162  ? 77  PHE   B H    1 c 1 
ATOM   945  H HA   . PHE   A 1 65  ? 27.533 -0.399  11.907  1   65.399  ? 77  PHE   B HA   1 c 1 
ATOM   946  H HB2  . PHE   A 1 65  ? 26.372 1.121   10.433  1   63.15   ? 77  PHE   B HB2  1 c 1 
ATOM   947  H HB3  . PHE   A 1 65  ? 26.213 -0.062  9.377   1   60.86   ? 77  PHE   B HB3  1 c 1 
ATOM   948  H HD1  . PHE   A 1 65  ? 25.129 0.971   12.601  1   64.539  ? 77  PHE   B HD1  1 c 1 
ATOM   949  H HD2  . PHE   A 1 65  ? 24.455 -1.689  9.654   1   57.937  ? 77  PHE   B HD2  1 c 1 
ATOM   950  H HE1  . PHE   A 1 65  ? 23.185 0.284   13.67   1   62.801  ? 77  PHE   B HE1  1 c 1 
ATOM   951  H HE2  . PHE   A 1 65  ? 22.516 -2.366  10.73   1   56.382  ? 77  PHE   B HE2  1 c 1 
ATOM   952  H HZ   . PHE   A 1 65  ? 21.882 -1.386  12.73   1   59.273  ? 77  PHE   B HZ   1 c 1 
ATOM   953  N N    . VAL   A 1 66  ? 27.402 -2.878  11.629  1   64.56   ? 78  VAL   B N    1 ? 1 
ATOM   954  C CA   . VAL   A 1 66  ? 27.498 -4.32   11.465  1   63.871  ? 78  VAL   B CA   1 ? 1 
ATOM   955  C C    . VAL   A 1 66  ? 26.196 -4.923  11.97   1   63.045  ? 78  VAL   B C    1 ? 1 
ATOM   956  O O    . VAL   A 1 66  ? 25.603 -4.437  12.94   1   63.922  ? 78  VAL   B O    1 ? 1 
ATOM   957  C CB   . VAL   A 1 66  ? 28.732 -4.88   12.188  1   70.192  ? 78  VAL   B CB   1 ? 1 
ATOM   958  C CG1  . VAL   A 1 66  ? 28.887 -6.387  12.002  1   70.563  ? 78  VAL   B CG1  1 ? 1 
ATOM   959  C CG2  . VAL   A 1 66  ? 30.005 -4.138  11.767  1   71.837  ? 78  VAL   B CG2  1 ? 1 
ATOM   960  H H    . VAL   A 1 66  ? 27.298 -2.543  12.473  1   65.495  ? 78  VAL   B H    1 c 1 
ATOM   961  H HA   . VAL   A 1 66  ? 27.584 -4.517  10.515  1   63.534  ? 78  VAL   B HA   1 c 1 
ATOM   962  H HB   . VAL   A 1 66  ? 28.599 -4.715  13.151  1   70.874  ? 78  VAL   B HB   1 c 1 
ATOM   963  H HG11 . VAL   A 1 66  ? 28.886 -6.599  11.053  1   69.385  ? 78  VAL   B HG11 1 c 1 
ATOM   964  H HG12 . VAL   A 1 66  ? 28.15  -6.848  12.436  1   69.836  ? 78  VAL   B HG12 1 c 1 
ATOM   965  H HG13 . VAL   A 1 66  ? 29.726 -6.678  12.396  1   74.016  ? 78  VAL   B HG13 1 c 1 
ATOM   966  H HG21 . VAL   A 1 66  ? 30.779 -4.569  12.166  1   75.372  ? 78  VAL   B HG21 1 c 1 
ATOM   967  H HG22 . VAL   A 1 66  ? 29.959 -3.215  12.069  1   72.392  ? 78  VAL   B HG22 1 c 1 
ATOM   968  H HG23 . VAL   A 1 66  ? 30.087 -4.158  10.799  1   70.927  ? 78  VAL   B HG23 1 c 1 
ATOM   969  N N    . PHE   A 1 67  ? 25.676 -5.899  11.218  1   60.392  ? 79  PHE   B N    1 ? 1 
ATOM   970  C CA   . PHE   A 1 67  ? 24.462 -6.584  11.64   1   57.099  ? 79  PHE   B CA   1 ? 1 
ATOM   971  C C    . PHE   A 1 67  ? 24.363 -7.946  10.947  1   59.134  ? 79  PHE   B C    1 ? 1 
ATOM   972  O O    . PHE   A 1 67  ? 25.052 -8.205  9.959   1   56.956  ? 79  PHE   B O    1 ? 1 
ATOM   973  C CB   . PHE   A 1 67  ? 23.224 -5.741  11.386  1   56.891  ? 79  PHE   B CB   1 ? 1 
ATOM   974  C CG   . PHE   A 1 67  ? 22.818 -5.689  9.919   1   51.126  ? 79  PHE   B CG   1 ? 1 
ATOM   975  C CD1  . PHE   A 1 67  ? 23.489 -4.876  9.01    1   49.933  ? 79  PHE   B CD1  1 ? 1 
ATOM   976  C CD2  . PHE   A 1 67  ? 21.774 -6.49   9.456   1   49.474  ? 79  PHE   B CD2  1 ? 1 
ATOM   977  C CE1  . PHE   A 1 67  ? 23.117 -4.841  7.677   1   47.978  ? 79  PHE   B CE1  1 ? 1 
ATOM   978  C CE2  . PHE   A 1 67  ? 21.39  -6.429  8.114   1   48.397  ? 79  PHE   B CE2  1 ? 1 
ATOM   979  C CZ   . PHE   A 1 67  ? 22.093 -5.662  7.226   1   47.377  ? 79  PHE   B CZ   1 ? 1 
ATOM   980  H H    . PHE   A 1 67  ? 26.079 -6.142  10.435  1   60.096  ? 79  PHE   B H    1 c 1 
ATOM   981  H HA   . PHE   A 1 67  ? 24.526 -6.744  12.619  1   60.263  ? 79  PHE   B HA   1 c 1 
ATOM   982  H HB2  . PHE   A 1 67  ? 22.479 -6.111  11.911  1   55.333  ? 79  PHE   B HB2  1 c 1 
ATOM   983  H HB3  . PHE   A 1 67  ? 23.392 -4.826  11.703  1   55.584  ? 79  PHE   B HB3  1 c 1 
ATOM   984  H HD1  . PHE   A 1 67  ? 24.206 -4.341  9.309   1   51.417  ? 79  PHE   B HD1  1 c 1 
ATOM   985  H HD2  . PHE   A 1 67  ? 21.302 -7.043  10.058  1   50.38   ? 79  PHE   B HD2  1 c 1 
ATOM   986  H HE1  . PHE   A 1 67  ? 23.587 -4.292  7.069   1   48.26   ? 79  PHE   B HE1  1 c 1 
ATOM   987  H HE2  . PHE   A 1 67  ? 20.692 -6.982  7.804   1   47.62   ? 79  PHE   B HE2  1 c 1 
ATOM   988  H HZ   . PHE   A 1 67  ? 21.821 -5.622  6.323   1   46.467  ? 79  PHE   B HZ   1 c 1 
ATOM   989  N N    . SER   A 1 68  ? 23.517 -8.823  11.507  1   55.717  ? 80  SER   B N    1 ? 1 
ATOM   990  C CA   . SER   A 1 68  ? 23.351 -10.169 10.971  1   59.662  ? 80  SER   B CA   1 ? 1 
ATOM   991  C C    . SER   A 1 68  ? 22.076 -10.187 10.129  1   55.893  ? 80  SER   B C    1 ? 1 
ATOM   992  O O    . SER   A 1 68  ? 20.988 -9.866  10.612  1   54.52   ? 80  SER   B O    1 ? 1 
ATOM   993  C CB   . SER   A 1 68  ? 23.348 -11.238 12.053  1   62.499  ? 80  SER   B CB   1 ? 1 
ATOM   994  O OG   . SER   A 1 68  ? 24.685 -11.569 12.45   1   70.059  ? 80  SER   B OG   1 ? 1 
ATOM   995  H H    . SER   A 1 68  ? 23.03  -8.576  12.24   1   57.361  ? 80  SER   B H    1 c 1 
ATOM   996  H HA   . SER   A 1 68  ? 24.115 -10.351 10.372  1   59.459  ? 80  SER   B HA   1 c 1 
ATOM   997  H HB2  . SER   A 1 68  ? 22.851 -10.912 12.827  1   63.567  ? 80  SER   B HB2  1 c 1 
ATOM   998  H HB3  . SER   A 1 68  ? 22.902 -12.038 11.717  1   63.841  ? 80  SER   B HB3  1 c 1 
ATOM   999  H HG   . SER   A 1 68  ? 24.593 -12.041 13.144  0   30      ? 80  SER   B HG   1 c 1 
ATOM   1000 N N    . LEU   A 1 69  ? 22.254 -10.477 8.839   1   53.83   ? 81  LEU   B N    1 ? 1 
ATOM   1001 C CA   . LEU   A 1 69  ? 21.168 -10.346 7.888   1   53.022  ? 81  LEU   B CA   1 ? 1 
ATOM   1002 C C    . LEU   A 1 69  ? 20.044 -11.327 8.219   1   54.046  ? 81  LEU   B C    1 ? 1 
ATOM   1003 O O    . LEU   A 1 69  ? 20.291 -12.484 8.58    1   54.581  ? 81  LEU   B O    1 ? 1 
ATOM   1004 C CB   . LEU   A 1 69  ? 21.708 -10.559 6.481   1   57.406  ? 81  LEU   B CB   1 ? 1 
ATOM   1005 C CG   . LEU   A 1 69  ? 20.686 -10.312 5.362   1   57.393  ? 81  LEU   B CG   1 ? 1 
ATOM   1006 C CD1  . LEU   A 1 69  ? 20.543 -8.824  5.133   1   54.757  ? 81  LEU   B CD1  1 ? 1 
ATOM   1007 C CD2  . LEU   A 1 69  ? 21.039 -11.004 4.064   1   61.799  ? 81  LEU   B CD2  1 ? 1 
ATOM   1008 H H    . LEU   A 1 69  ? 23.069 -10.768 8.545   1   55.852  ? 81  LEU   B H    1 c 1 
ATOM   1009 H HA   . LEU   A 1 69  ? 20.812 -9.424  7.958   1   51.715  ? 81  LEU   B HA   1 c 1 
ATOM   1010 H HB2  . LEU   A 1 69  ? 22.473 -9.954  6.348   1   56.658  ? 81  LEU   B HB2  1 c 1 
ATOM   1011 H HB3  . LEU   A 1 69  ? 22.032 -11.486 6.41    1   58.78   ? 81  LEU   B HB3  1 c 1 
ATOM   1012 H HG   . LEU   A 1 69  ? 19.807 -10.66  5.661   1   57.437  ? 81  LEU   B HG   1 c 1 
ATOM   1013 H HD11 . LEU   A 1 69  ? 20.216 -8.4    5.944   1   53.993  ? 81  LEU   B HD11 1 c 1 
ATOM   1014 H HD12 . LEU   A 1 69  ? 19.912 -8.666  4.41    1   53.882  ? 81  LEU   B HD12 1 c 1 
ATOM   1015 H HD13 . LEU   A 1 69  ? 21.406 -8.446  4.896   1   55.099  ? 81  LEU   B HD13 1 c 1 
ATOM   1016 H HD21 . LEU   A 1 69  ? 21.063 -11.966 4.204   1   62.722  ? 81  LEU   B HD21 1 c 1 
ATOM   1017 H HD22 . LEU   A 1 69  ? 21.909 -10.7   3.763   1   61.229  ? 81  LEU   B HD22 1 c 1 
ATOM   1018 H HD23 . LEU   A 1 69  ? 20.372 -10.793 3.39    1   59.879  ? 81  LEU   B HD23 1 c 1 
ATOM   1019 N N    . GLY   A 1 70  ? 18.81  -10.807 8.198   1   56.129  ? 82  GLY   B N    1 ? 1 
ATOM   1020 C CA   . GLY   A 1 70  ? 17.625 -11.623 8.433   1   61.093  ? 82  GLY   B CA   1 ? 1 
ATOM   1021 C C    . GLY   A 1 70  ? 17.474 -12.047 9.891   1   69.163  ? 82  GLY   B C    1 ? 1 
ATOM   1022 O O    . GLY   A 1 70  ? 16.675 -12.94  10.175  1   74.562  ? 82  GLY   B O    1 ? 1 
ATOM   1023 H H    . GLY   A 1 70  ? 18.703 -9.915  8.032   1   54.058  ? 82  GLY   B H    1 c 1 
ATOM   1024 H HA2  . GLY   A 1 70  ? 16.828 -11.113 8.159   1   59.839  ? 82  GLY   B HA2  1 c 1 
ATOM   1025 H HA3  . GLY   A 1 70  ? 17.676 -12.427 7.865   1   62.488  ? 82  GLY   B HA3  1 c 1 
ATOM   1026 N N    . LYS   A 1 71  ? 18.293 -11.501 10.811  1   70.223  ? 83  LYS   B N    1 ? 1 
ATOM   1027 C CA   . LYS   A 1 71  ? 18.327 -12.017 12.177  1   65.543  ? 83  LYS   B CA   1 ? 1 
ATOM   1028 C C    . LYS   A 1 71  ? 17.64  -10.997 13.091  1   71.288  ? 83  LYS   B C    1 ? 1 
ATOM   1029 O O    . LYS   A 1 71  ? 17.934 -10.935 14.278  1   70.791  ? 83  LYS   B O    1 ? 1 
ATOM   1030 C CB   . LYS   A 1 71  ? 19.718 -12.524 12.609  1   70.295  ? 83  LYS   B CB   1 ? 1 
ATOM   1031 H H    . LYS   A 1 71  ? 18.821 -10.789 10.592  1   66.62   ? 83  LYS   B H    1 c 1 
ATOM   1032 H HA   . LYS   A 1 71  ? 17.758 -12.827 12.195  1   70.087  ? 83  LYS   B HA   1 c 1 
ATOM   1033 H HB2  . LYS   A 1 71  ? 20.31  -11.955 12.116  0   30      ? 83  LYS   B HB2  1 c 1 
ATOM   1034 H HB3  . LYS   A 1 71  ? 19.531 -13.145 13.312  0   30      ? 83  LYS   B HB3  1 c 1 
ATOM   1035 N N    . GLY   A 1 72  ? 16.718 -10.194 12.535  1   71.89   ? 84  GLY   B N    1 ? 1 
ATOM   1036 C CA   . GLY   A 1 72  ? 15.826 -9.344  13.319  1   78.196  ? 84  GLY   B CA   1 ? 1 
ATOM   1037 C C    . GLY   A 1 72  ? 16.454 -8.043  13.854  1   72.87   ? 84  GLY   B C    1 ? 1 
ATOM   1038 O O    . GLY   A 1 72  ? 15.897 -7.399  14.736  1   79.683  ? 84  GLY   B O    1 ? 1 
ATOM   1039 H H    . GLY   A 1 72  ? 16.641 -10.172 11.625  1   70.848  ? 84  GLY   B H    1 c 1 
ATOM   1040 H HA2  . GLY   A 1 72  ? 15.048 -9.112  12.759  1   74.122  ? 84  GLY   B HA2  1 c 1 
ATOM   1041 H HA3  . GLY   A 1 72  ? 15.489 -9.869  14.083  1   77.751  ? 84  GLY   B HA3  1 c 1 
ATOM   1042 N N    . GLN   A 1 73  ? 17.629 -7.653  13.38   1   60.842  ? 85  GLN   B N    1 ? 1 
ATOM   1043 C CA   . GLN   A 1 73  ? 18.345 -6.553  14.01   1   60.123  ? 85  GLN   B CA   1 ? 1 
ATOM   1044 C C    . GLN   A 1 73  ? 18.053 -5.196  13.351  1   55.077  ? 85  GLN   B C    1 ? 1 
ATOM   1045 O O    . GLN   A 1 73  ? 18.347 -4.166  13.942  1   53.877  ? 85  GLN   B O    1 ? 1 
ATOM   1046 C CB   . GLN   A 1 73  ? 19.816 -6.936  13.957  1   58.985  ? 85  GLN   B CB   1 ? 1 
ATOM   1047 C CG   . GLN   A 1 73  ? 20.12  -8.131  14.85   1   65.126  ? 85  GLN   B CG   1 ? 1 
ATOM   1048 C CD   . GLN   A 1 73  ? 21.51  -8.664  14.647  1   65.699  ? 85  GLN   B CD   1 ? 1 
ATOM   1049 O OE1  . GLN   A 1 73  ? 22.344 -8.06   13.964  1   67.38   ? 85  GLN   B OE1  1 ? 1 
ATOM   1050 N NE2  . GLN   A 1 73  ? 21.756 -9.804  15.26   1   77.445  ? 85  GLN   B NE2  1 ? 1 
ATOM   1051 H H    . GLN   A 1 73  ? 17.991 -8.063  12.648  1   62.322  ? 85  GLN   B H    1 c 1 
ATOM   1052 H HA   . GLN   A 1 73  ? 18.074 -6.505  14.962  1   61.259  ? 85  GLN   B HA   1 c 1 
ATOM   1053 H HB2  . GLN   A 1 73  ? 20.061 -7.15   13.032  1   58.946  ? 85  GLN   B HB2  1 c 1 
ATOM   1054 H HB3  . GLN   A 1 73  ? 20.358 -6.171  14.244  1   60.524  ? 85  GLN   B HB3  1 c 1 
ATOM   1055 H HG2  . GLN   A 1 73  ? 20.014 -7.868  15.789  1   65.91   ? 85  GLN   B HG2  1 c 1 
ATOM   1056 H HG3  . GLN   A 1 73  ? 19.477 -8.847  14.665  1   64.289  ? 85  GLN   B HG3  1 c 1 
ATOM   1057 H HE21 . GLN   A 1 73  ? 22.552 -10.186 15.176  1   76.028  ? 85  GLN   B HE21 1 c 1 
ATOM   1058 H HE22 . GLN   A 1 73  ? 21.129 -10.188 15.757  1   75.498  ? 85  GLN   B HE22 1 c 1 
ATOM   1059 N N    . VAL   A 1 74  ? 17.456 -5.185  12.155  1   46.603  ? 86  VAL   B N    1 ? 1 
ATOM   1060 C CA   . VAL   A 1 74  ? 17.284 -3.972  11.374  1   44.78   ? 86  VAL   B CA   1 ? 1 
ATOM   1061 C C    . VAL   A 1 74  ? 15.864 -4.004  10.814  1   42.599  ? 86  VAL   B C    1 ? 1 
ATOM   1062 O O    . VAL   A 1 74  ? 15.182 -5.003  10.926  1   44.219  ? 86  VAL   B O    1 ? 1 
ATOM   1063 C CB   . VAL   A 1 74  ? 18.311 -3.861  10.226  1   43.33   ? 86  VAL   B CB   1 ? 1 
ATOM   1064 C CG1  . VAL   A 1 74  ? 19.717 -3.578  10.766  1   45.369  ? 86  VAL   B CG1  1 ? 1 
ATOM   1065 C CG2  . VAL   A 1 74  ? 18.313 -5.136  9.378   1   42.564  ? 86  VAL   B CG2  1 ? 1 
ATOM   1066 H H    . VAL   A 1 74  ? 17.14  -5.97   11.811  1   48.147  ? 86  VAL   B H    1 c 1 
ATOM   1067 H HA   . VAL   A 1 74  ? 17.376 -3.198  11.961  1   44.964  ? 86  VAL   B HA   1 c 1 
ATOM   1068 H HB   . VAL   A 1 74  ? 18.039 -3.105  9.654   1   42.041  ? 86  VAL   B HB   1 c 1 
ATOM   1069 H HG11 . VAL   A 1 74  ? 19.991 -4.301  11.356  1   46.87   ? 86  VAL   B HG11 1 c 1 
ATOM   1070 H HG12 . VAL   A 1 74  ? 19.713 -2.742  11.261  1   45.617  ? 86  VAL   B HG12 1 c 1 
ATOM   1071 H HG13 . VAL   A 1 74  ? 20.343 -3.512  10.025  1   45.046  ? 86  VAL   B HG13 1 c 1 
ATOM   1072 H HG21 . VAL   A 1 74  ? 18.93  -5.029  8.635   1   42.505  ? 86  VAL   B HG21 1 c 1 
ATOM   1073 H HG22 . VAL   A 1 74  ? 17.42  -5.301  9.033   1   42.062  ? 86  VAL   B HG22 1 c 1 
ATOM   1074 H HG23 . VAL   A 1 74  ? 18.593 -5.889  9.924   1   44.41   ? 86  VAL   B HG23 1 c 1 
ATOM   1075 N N    . ILE   A 1 75  ? 15.44  -2.913  10.224  1   42.282  ? 87  ILE   B N    1 ? 1 
ATOM   1076 C CA   . ILE   A 1 75  ? 14.129 -2.873  9.577   1   43.15   ? 87  ILE   B CA   1 ? 1 
ATOM   1077 C C    . ILE   A 1 75  ? 14.062 -3.841  8.407   1   37.128  ? 87  ILE   B C    1 ? 1 
ATOM   1078 O O    . ILE   A 1 75  ? 15.089 -4.191  7.825   1   37.048  ? 87  ILE   B O    1 ? 1 
ATOM   1079 C CB   . ILE   A 1 75  ? 13.732 -1.459  9.216   1   39.574  ? 87  ILE   B CB   1 ? 1 
ATOM   1080 C CG1  . ILE   A 1 75  ? 14.795 -0.803  8.301   1   42.901  ? 87  ILE   B CG1  1 ? 1 
ATOM   1081 C CG2  . ILE   A 1 75  ? 13.44  -0.638  10.461  1   44.624  ? 87  ILE   B CG2  1 ? 1 
ATOM   1082 C CD1  . ILE   A 1 75  ? 14.344 0.503   7.702   1   41.177  ? 87  ILE   B CD1  1 ? 1 
ATOM   1083 H H    . ILE   A 1 75  ? 15.962 -2.163  10.23   1   42.173  ? 87  ILE   B H    1 c 1 
ATOM   1084 H HA   . ILE   A 1 75  ? 13.482 -3.184  10.24   1   42.183  ? 87  ILE   B HA   1 c 1 
ATOM   1085 H HB   . ILE   A 1 75  ? 12.903 -1.514  8.701   1   41.099  ? 87  ILE   B HB   1 c 1 
ATOM   1086 H HG12 . ILE   A 1 75  ? 15.609 -0.645  8.821   1   42.241  ? 87  ILE   B HG12 1 c 1 
ATOM   1087 H HG13 . ILE   A 1 75  ? 15.017 -1.422  7.576   1   41.295  ? 87  ILE   B HG13 1 c 1 
ATOM   1088 H HG21 . ILE   A 1 75  ? 13.108 0.238   10.205  1   42.959  ? 87  ILE   B HG21 1 c 1 
ATOM   1089 H HG22 . ILE   A 1 75  ? 14.255 -0.535  10.981  1   44.059  ? 87  ILE   B HG22 1 c 1 
ATOM   1090 H HG23 . ILE   A 1 75  ? 12.77  -1.091  11      1   44.269  ? 87  ILE   B HG23 1 c 1 
ATOM   1091 H HD11 . ILE   A 1 75  ? 13.487 0.378   7.253   1   41.159  ? 87  ILE   B HD11 1 c 1 
ATOM   1092 H HD12 . ILE   A 1 75  ? 15.007 0.809   7.054   1   41.237  ? 87  ILE   B HD12 1 c 1 
ATOM   1093 H HD13 . ILE   A 1 75  ? 14.247 1.172   8.405   1   42.02   ? 87  ILE   B HD13 1 c 1 
ATOM   1094 N N    . LYS   A 1 76  ? 12.839 -4.378  8.19    1   42.583  ? 88  LYS   B N    1 ? 1 
ATOM   1095 C CA   . LYS   A 1 76  ? 12.548 -5.315  7.115   1   43.191  ? 88  LYS   B CA   1 ? 1 
ATOM   1096 C C    . LYS   A 1 76  ? 13.187 -4.878  5.804   1   39.99   ? 88  LYS   B C    1 ? 1 
ATOM   1097 O O    . LYS   A 1 76  ? 13.833 -5.69   5.142   1   39.716  ? 88  LYS   B O    1 ? 1 
ATOM   1098 C CB   . LYS   A 1 76  ? 11.025 -5.539  7.01    1   47.603  ? 88  LYS   B CB   1 ? 1 
ATOM   1099 H H    . LYS   A 1 76  ? 12.156 -4.139  8.749   1   41.865  ? 88  LYS   B H    1 c 1 
ATOM   1100 H HA   . LYS   A 1 76  ? 12.95  -6.186  7.365   1   44.321  ? 88  LYS   B HA   1 c 1 
ATOM   1101 H HB2  . LYS   A 1 76  ? 10.856 -6.027  6.152   0   30      ? 88  LYS   B HB2  1 c 1 
ATOM   1102 H HB3  . LYS   A 1 76  ? 10.548 -4.907  7.603   0   30      ? 88  LYS   B HB3  1 c 1 
ATOM   1103 N N    . ALA   A 1 77  ? 13.081 -3.579  5.459   1   40.488  ? 89  ALA   B N    1 ? 1 
ATOM   1104 C CA   . ALA   A 1 77  ? 13.617 -3.068  4.21    1   40.982  ? 89  ALA   B CA   1 ? 1 
ATOM   1105 C C    . ALA   A 1 77  ? 15.108 -3.316  4.091   1   44.581  ? 89  ALA   B C    1 ? 1 
ATOM   1106 O O    . ALA   A 1 77  ? 15.613 -3.458  2.967   1   40.806  ? 89  ALA   B O    1 ? 1 
ATOM   1107 C CB   . ALA   A 1 77  ? 13.344 -1.623  4.047   1   38.486  ? 89  ALA   B CB   1 ? 1 
ATOM   1108 H H    . ALA   A 1 77  ? 12.654 -3      6.022   1   40.106  ? 89  ALA   B H    1 c 1 
ATOM   1109 H HA   . ALA   A 1 77  ? 13.17  -3.56   3.467   1   41.591  ? 89  ALA   B HA   1 c 1 
ATOM   1110 H HB1  . ALA   A 1 77  ? 12.385 -1.468  4.058   1   39.142  ? 89  ALA   B HB1  1 c 1 
ATOM   1111 H HB2  . ALA   A 1 77  ? 13.757 -1.128  4.774   1   38.726  ? 89  ALA   B HB2  1 c 1 
ATOM   1112 H HB3  . ALA   A 1 77  ? 13.709 -1.313  3.201   1   38.977  ? 89  ALA   B HB3  1 c 1 
ATOM   1113 N N    . TRP   A 1 78  ? 15.822 -3.299  5.236   1   40.769  ? 90  TRP   B N    1 ? 1 
ATOM   1114 C CA   . TRP   A 1 78  ? 17.247 -3.557  5.161   1   40.814  ? 90  TRP   B CA   1 ? 1 
ATOM   1115 C C    . TRP   A 1 78  ? 17.498 -5.023  4.917   1   38.628  ? 90  TRP   B C    1 ? 1 
ATOM   1116 O O    . TRP   A 1 78  ? 18.403 -5.353  4.154   1   45.118  ? 90  TRP   B O    1 ? 1 
ATOM   1117 C CB   . TRP   A 1 78  ? 17.987 -3.038  6.408   1   38.826  ? 90  TRP   B CB   1 ? 1 
ATOM   1118 C CG   . TRP   A 1 78  ? 18.519 -1.651  6.239   1   42.037  ? 90  TRP   B CG   1 ? 1 
ATOM   1119 C CD1  . TRP   A 1 78  ? 17.851 -0.527  5.805   1   41.497  ? 90  TRP   B CD1  1 ? 1 
ATOM   1120 C CD2  . TRP   A 1 78  ? 19.887 -1.227  6.455   1   41.304  ? 90  TRP   B CD2  1 ? 1 
ATOM   1121 N NE1  . TRP   A 1 78  ? 18.702 0.552   5.802   1   39.068  ? 90  TRP   B NE1  1 ? 1 
ATOM   1122 C CE2  . TRP   A 1 78  ? 19.952 0.155   6.177   1   42.288  ? 90  TRP   B CE2  1 ? 1 
ATOM   1123 C CE3  . TRP   A 1 78  ? 21.046 -1.876  6.856   1   44.559  ? 90  TRP   B CE3  1 ? 1 
ATOM   1124 C CZ2  . TRP   A 1 78  ? 21.131 0.893   6.291   1   41.436  ? 90  TRP   B CZ2  1 ? 1 
ATOM   1125 C CZ3  . TRP   A 1 78  ? 22.202 -1.152  6.982   1   45.031  ? 90  TRP   B CZ3  1 ? 1 
ATOM   1126 C CH2  . TRP   A 1 78  ? 22.25  0.209   6.674   1   44.304  ? 90  TRP   B CH2  1 ? 1 
ATOM   1127 H H    . TRP   A 1 78  ? 15.43  -3.118  6.041   1   41.392  ? 90  TRP   B H    1 c 1 
ATOM   1128 H HA   . TRP   A 1 78  ? 17.602 -3.056  4.378   1   39.688  ? 90  TRP   B HA   1 c 1 
ATOM   1129 H HB2  . TRP   A 1 78  ? 17.37  -3.052  7.171   1   40.127  ? 90  TRP   B HB2  1 c 1 
ATOM   1130 H HB3  . TRP   A 1 78  ? 18.733 -3.643  6.605   1   41.114  ? 90  TRP   B HB3  1 c 1 
ATOM   1131 H HD1  . TRP   A 1 78  ? 16.93  -0.48   5.603   1   39.91   ? 90  TRP   B HD1  1 c 1 
ATOM   1132 H HE1  . TRP   A 1 78  ? 18.484 1.358   5.569   1   40.117  ? 90  TRP   B HE1  1 c 1 
ATOM   1133 H HE3  . TRP   A 1 78  ? 21.032 -2.797  7.058   1   44.236  ? 90  TRP   B HE3  1 c 1 
ATOM   1134 H HZ2  . TRP   A 1 78  ? 21.157 1.813   6.091   1   42.606  ? 90  TRP   B HZ2  1 c 1 
ATOM   1135 H HZ3  . TRP   A 1 78  ? 22.992 -1.592  7.247   1   46.609  ? 90  TRP   B HZ3  1 c 1 
ATOM   1136 H HH2  . TRP   A 1 78  ? 23.061 0.675   6.772   1   45.841  ? 90  TRP   B HH2  1 c 1 
ATOM   1137 N N    . ASP   A 1 79  ? 16.744 -5.902  5.595   1   38.307  ? 91  ASP   B N    1 ? 1 
ATOM   1138 C CA   . ASP   A 1 79  ? 16.931 -7.321  5.386   1   43.426  ? 91  ASP   B CA   1 ? 1 
ATOM   1139 C C    . ASP   A 1 79  ? 16.655 -7.661  3.926   1   47.537  ? 91  ASP   B C    1 ? 1 
ATOM   1140 O O    . ASP   A 1 79  ? 17.381 -8.456  3.34    1   45.771  ? 91  ASP   B O    1 ? 1 
ATOM   1141 C CB   . ASP   A 1 79  ? 16.095 -8.16   6.347   1   46.654  ? 91  ASP   B CB   1 ? 1 
ATOM   1142 C CG   . ASP   A 1 79  ? 16.655 -8.341  7.757   1   50.689  ? 91  ASP   B CG   1 ? 1 
ATOM   1143 O OD1  . ASP   A 1 79  ? 17.869 -8.266  7.886   1   47.06   ? 91  ASP   B OD1  1 ? 1 
ATOM   1144 O OD2  . ASP   A 1 79  ? 15.857 -8.612  8.701   1   49.345  ? 91  ASP   B OD2  1 ? 1 
ATOM   1145 H H    . ASP   A 1 79  ? 16.117 -5.613  6.195   1   39.057  ? 91  ASP   B H    1 c 1 
ATOM   1146 H HA   . ASP   A 1 79  ? 17.875 -7.53   5.569   1   44.434  ? 91  ASP   B HA   1 c 1 
ATOM   1147 H HB2  . ASP   A 1 79  ? 15.208 -7.75   6.426   1   46.15   ? 91  ASP   B HB2  1 c 1 
ATOM   1148 H HB3  . ASP   A 1 79  ? 15.975 -9.052  5.958   1   48.077  ? 91  ASP   B HB3  1 c 1 
ATOM   1149 N N    . ILE   A 1 80  ? 15.62  -7.017  3.347   1   45.945  ? 92  ILE   B N    1 ? 1 
ATOM   1150 C CA   . ILE   A 1 80  ? 15.276 -7.223  1.947   1   47.332  ? 92  ILE   B CA   1 ? 1 
ATOM   1151 C C    . ILE   A 1 80  ? 16.353 -6.59   1.059   1   43.207  ? 92  ILE   B C    1 ? 1 
ATOM   1152 O O    . ILE   A 1 80  ? 16.877 -7.246  0.173   1   44.586  ? 92  ILE   B O    1 ? 1 
ATOM   1153 C CB   . ILE   A 1 80  ? 13.886 -6.626  1.637   1   46.979  ? 92  ILE   B CB   1 ? 1 
ATOM   1154 C CG1  . ILE   A 1 80  ? 12.785 -7.375  2.3     1   50.956  ? 92  ILE   B CG1  1 ? 1 
ATOM   1155 C CG2  . ILE   A 1 80  ? 13.671 -6.5    0.116   1   47.37   ? 92  ILE   B CG2  1 ? 1 
ATOM   1156 C CD1  . ILE   A 1 80  ? 11.484 -6.584  2.387   1   51.121  ? 92  ILE   B CD1  1 ? 1 
ATOM   1157 H H    . ILE   A 1 80  ? 15.113 -6.443  3.845   1   45.323  ? 92  ILE   B H    1 c 1 
ATOM   1158 H HA   . ILE   A 1 80  ? 15.248 -8.184  1.771   1   47.93   ? 92  ILE   B HA   1 c 1 
ATOM   1159 H HB   . ILE   A 1 80  ? 13.877 -5.72   2.005   1   46.07   ? 92  ILE   B HB   1 c 1 
ATOM   1160 H HG12 . ILE   A 1 80  ? 12.62  -8.201  1.803   1   52.028  ? 92  ILE   B HG12 1 c 1 
ATOM   1161 H HG13 . ILE   A 1 80  ? 13.067 -7.619  3.205   1   50.249  ? 92  ILE   B HG13 1 c 1 
ATOM   1162 H HG21 . ILE   A 1 80  ? 12.74  -6.292  -0.067  1   47.872  ? 92  ILE   B HG21 1 c 1 
ATOM   1163 H HG22 . ILE   A 1 80  ? 13.904 -7.339  -0.317  1   49.04   ? 92  ILE   B HG22 1 c 1 
ATOM   1164 H HG23 . ILE   A 1 80  ? 14.232 -5.789  -0.237  1   46.838  ? 92  ILE   B HG23 1 c 1 
ATOM   1165 H HD11 . ILE   A 1 80  ? 11.645 -5.742  2.853   1   49.51   ? 92  ILE   B HD11 1 c 1 
ATOM   1166 H HD12 . ILE   A 1 80  ? 10.822 -7.105  2.88    1   52.034  ? 92  ILE   B HD12 1 c 1 
ATOM   1167 H HD13 . ILE   A 1 80  ? 11.147 -6.399  1.491   1   51.403  ? 92  ILE   B HD13 1 c 1 
ATOM   1168 N N    . GLY   A 1 81  ? 16.732 -5.329  1.321   1   40.406  ? 93  GLY   B N    1 ? 1 
ATOM   1169 C CA   . GLY   A 1 81  ? 17.55  -4.599  0.373   1   41.031  ? 93  GLY   B CA   1 ? 1 
ATOM   1170 C C    . GLY   A 1 81  ? 19.005 -5.056  0.337   1   46.089  ? 93  GLY   B C    1 ? 1 
ATOM   1171 O O    . GLY   A 1 81  ? 19.643 -5.088  -0.72   1   44.02   ? 93  GLY   B O    1 ? 1 
ATOM   1172 H H    . GLY   A 1 81  ? 16.475 -4.922  2.098   1   39.976  ? 93  GLY   B H    1 c 1 
ATOM   1173 H HA2  . GLY   A 1 81  ? 17.159 -4.7    -0.525  1   42.48   ? 93  GLY   B HA2  1 c 1 
ATOM   1174 H HA3  . GLY   A 1 81  ? 17.52  -3.641  0.604   1   40.84   ? 93  GLY   B HA3  1 c 1 
ATOM   1175 N N    . VAL   A 1 82  ? 19.577 -5.301  1.533   1   44.897  ? 94  VAL   B N    1 ? 1 
ATOM   1176 C CA   . VAL   A 1 82  ? 20.978 -5.607  1.596   1   44.279  ? 94  VAL   B CA   1 ? 1 
ATOM   1177 C C    . VAL   A 1 82  ? 21.189 -7.016  1.033   1   47.583  ? 94  VAL   B C    1 ? 1 
ATOM   1178 O O    . VAL   A 1 82  ? 22.257 -7.247  0.457   1   47.15   ? 94  VAL   B O    1 ? 1 
ATOM   1179 C CB   . VAL   A 1 82  ? 21.519 -5.426  3.033   1   50.105  ? 94  VAL   B CB   1 ? 1 
ATOM   1180 C CG1  . VAL   A 1 82  ? 22.975 -5.884  3.159   1   52.282  ? 94  VAL   B CG1  1 ? 1 
ATOM   1181 C CG2  . VAL   A 1 82  ? 21.406 -3.964  3.469   1   47.656  ? 94  VAL   B CG2  1 ? 1 
ATOM   1182 H H    . VAL   A 1 82  ? 19.085 -5.271  2.303   1   43.798  ? 94  VAL   B H    1 c 1 
ATOM   1183 H HA   . VAL   A 1 82  ? 21.45  -4.976  1.017   1   46.331  ? 94  VAL   B HA   1 c 1 
ATOM   1184 H HB   . VAL   A 1 82  ? 20.963 -5.977  3.632   1   48.351  ? 94  VAL   B HB   1 c 1 
ATOM   1185 H HG11 . VAL   A 1 82  ? 23.493 -5.526  2.418   1   53.063  ? 94  VAL   B HG11 1 c 1 
ATOM   1186 H HG12 . VAL   A 1 82  ? 23.015 -6.855  3.143   1   53.279  ? 94  VAL   B HG12 1 c 1 
ATOM   1187 H HG13 . VAL   A 1 82  ? 23.344 -5.559  3.997   1   52.56   ? 94  VAL   B HG13 1 c 1 
ATOM   1188 H HG21 . VAL   A 1 82  ? 21.783 -3.861  4.359   1   48.429  ? 94  VAL   B HG21 1 c 1 
ATOM   1189 H HG22 . VAL   A 1 82  ? 20.471 -3.7    3.482   1   46.7    ? 94  VAL   B HG22 1 c 1 
ATOM   1190 H HG23 . VAL   A 1 82  ? 21.893 -3.401  2.844   1   48.506  ? 94  VAL   B HG23 1 c 1 
ATOM   1191 N N    . ALA   A 1 83  ? 20.186 -7.929  1.126   1   46.941  ? 95  ALA   B N    1 ? 1 
ATOM   1192 C CA   . ALA   A 1 83  ? 20.3   -9.244  0.488   1   49.649  ? 95  ALA   B CA   1 ? 1 
ATOM   1193 C C    . ALA   A 1 83  ? 20.493 -9.128  -1.022  1   51.741  ? 95  ALA   B C    1 ? 1 
ATOM   1194 O O    . ALA   A 1 83  ? 20.986 -10.057 -1.648  1   57.861  ? 95  ALA   B O    1 ? 1 
ATOM   1195 C CB   . ALA   A 1 83  ? 19.125 -10.171 0.746   1   50.248  ? 95  ALA   B CB   1 ? 1 
ATOM   1196 H H    . ALA   A 1 83  ? 19.431 -7.73   1.601   1   46.008  ? 95  ALA   B H    1 c 1 
ATOM   1197 H HA   . ALA   A 1 83  ? 21.118 -9.677  0.856   1   50.917  ? 95  ALA   B HA   1 c 1 
ATOM   1198 H HB1  . ALA   A 1 83  ? 18.979 -10.256 1.703   1   49.731  ? 95  ALA   B HB1  1 c 1 
ATOM   1199 H HB2  . ALA   A 1 83  ? 18.325 -9.808  0.331   1   49.496  ? 95  ALA   B HB2  1 c 1 
ATOM   1200 H HB3  . ALA   A 1 83  ? 19.312 -11.048 0.371   1   52.239  ? 95  ALA   B HB3  1 c 1 
ATOM   1201 N N    . THR   A 1 84  ? 20.101 -8.007  -1.621  1   54.849  ? 96  THR   B N    1 ? 1 
ATOM   1202 C CA   . THR   A 1 84  ? 20.268 -7.843  -3.062  1   58.179  ? 96  THR   B CA   1 ? 1 
ATOM   1203 C C    . THR   A 1 84  ? 21.642 -7.272  -3.421  1   59.35   ? 96  THR   B C    1 ? 1 
ATOM   1204 O O    . THR   A 1 84  ? 21.952 -7.169  -4.594  1   58.794  ? 96  THR   B O    1 ? 1 
ATOM   1205 C CB   . THR   A 1 84  ? 19.155 -6.978  -3.66   1   57.047  ? 96  THR   B CB   1 ? 1 
ATOM   1206 O OG1  . THR   A 1 84  ? 19.375 -5.615  -3.297  1   55.181  ? 96  THR   B OG1  1 ? 1 
ATOM   1207 C CG2  . THR   A 1 84  ? 17.763 -7.406  -3.22   1   57.244  ? 96  THR   B CG2  1 ? 1 
ATOM   1208 H H    . THR   A 1 84  ? 19.709 -7.338  -1.14   1   52.233  ? 96  THR   B H    1 c 1 
ATOM   1209 H HA   . THR   A 1 84  ? 20.198 -8.732  -3.471  1   59.614  ? 96  THR   B HA   1 c 1 
ATOM   1210 H HB   . THR   A 1 84  ? 19.196 -7.053  -4.643  1   59.07   ? 96  THR   B HB   1 c 1 
ATOM   1211 H HG1  . THR   A 1 84  ? 19.36  -5.555  -2.486  0   30      ? 96  THR   B HG1  1 c 1 
ATOM   1212 H HG21 . THR   A 1 84  ? 17.096 -6.913  -3.727  1   56.831  ? 96  THR   B HG21 1 c 1 
ATOM   1213 H HG22 . THR   A 1 84  ? 17.649 -7.221  -2.274  1   55.174  ? 96  THR   B HG22 1 c 1 
ATOM   1214 H HG23 . THR   A 1 84  ? 17.65  -8.358  -3.379  1   58.452  ? 96  THR   B HG23 1 c 1 
ATOM   1215 N N    . MET   A 1 85  ? 22.491 -6.894  -2.464  1   58.463  ? 97  MET   B N    1 ? 1 
ATOM   1216 C CA   . MET   A 1 85  ? 23.652 -6.095  -2.844  1   60.272  ? 97  MET   B CA   1 ? 1 
ATOM   1217 C C    . MET   A 1 85  ? 24.898 -6.961  -3.028  1   62.893  ? 97  MET   B C    1 ? 1 
ATOM   1218 O O    . MET   A 1 85  ? 25.024 -8.053  -2.459  1   57.655  ? 97  MET   B O    1 ? 1 
ATOM   1219 C CB   . MET   A 1 85  ? 23.892 -4.985  -1.828  1   56.371  ? 97  MET   B CB   1 ? 1 
ATOM   1220 C CG   . MET   A 1 85  ? 22.751 -4.009  -1.762  1   55.047  ? 97  MET   B CG   1 ? 1 
ATOM   1221 S SD   . MET   A 1 85  ? 23.013 -2.734  -0.524  1   55.56   ? 97  MET   B SD   1 ? 1 
ATOM   1222 C CE   . MET   A 1 85  ? 24.386 -1.818  -1.236  1   58.988  ? 97  MET   B CE   1 ? 1 
ATOM   1223 H H    . MET   A 1 85  ? 22.363 -7.128  -1.59   1   57.488  ? 97  MET   B H    1 c 1 
ATOM   1224 H HA   . MET   A 1 85  ? 23.453 -5.675  -3.718  1   60.301  ? 97  MET   B HA   1 c 1 
ATOM   1225 H HB2  . MET   A 1 85  ? 24.023 -5.388  -0.943  1   56.63   ? 97  MET   B HB2  1 c 1 
ATOM   1226 H HB3  . MET   A 1 85  ? 24.714 -4.508  -2.069  1   58.61   ? 97  MET   B HB3  1 c 1 
ATOM   1227 H HG2  . MET   A 1 85  ? 22.637 -3.583  -2.633  1   55.813  ? 97  MET   B HG2  1 c 1 
ATOM   1228 H HG3  . MET   A 1 85  ? 21.927 -4.487  -1.551  1   53.925  ? 97  MET   B HG3  1 c 1 
ATOM   1229 H HE1  . MET   A 1 85  ? 24.65  -1.106  -0.625  1   58.708  ? 97  MET   B HE1  1 c 1 
ATOM   1230 H HE2  . MET   A 1 85  ? 25.14  -2.419  -1.376  1   60.533  ? 97  MET   B HE2  1 c 1 
ATOM   1231 H HE3  . MET   A 1 85  ? 24.112 -1.433  -2.088  1   59.272  ? 97  MET   B HE3  1 c 1 
ATOM   1232 N N    . LYS   A 1 86  ? 25.838 -6.442  -3.833  1   63.018  ? 98  LYS   B N    1 ? 1 
ATOM   1233 C CA   . LYS   A 1 86  ? 27.119 -7.118  -4.033  1   66.201  ? 98  LYS   B CA   1 ? 1 
ATOM   1234 C C    . LYS   A 1 86  ? 28.19  -6.356  -3.247  1   67.461  ? 98  LYS   B C    1 ? 1 
ATOM   1235 O O    . LYS   A 1 86  ? 27.955 -5.204  -2.857  1   63.101  ? 98  LYS   B O    1 ? 1 
ATOM   1236 C CB   . LYS   A 1 86  ? 27.403 -7.219  -5.534  1   68.579  ? 98  LYS   B CB   1 ? 1 
ATOM   1237 H H    . LYS   A 1 86  ? 25.683 -5.649  -4.26   1   63.249  ? 98  LYS   B H    1 c 1 
ATOM   1238 H HA   . LYS   A 1 86  ? 27.053 -8.035  -3.666  1   66.406  ? 98  LYS   B HA   1 c 1 
ATOM   1239 H HB2  . LYS   A 1 86  ? 28.379 -7.242  -5.61   0   30      ? 98  LYS   B HB2  1 c 1 
ATOM   1240 H HB3  . LYS   A 1 86  ? 26.559 -7.275  -5.985  0   30      ? 98  LYS   B HB3  1 c 1 
ATOM   1241 N N    . LYS   A 1 87  ? 29.327 -7.024  -2.966  1   69.822  ? 99  LYS   B N    1 ? 1 
ATOM   1242 C CA   . LYS   A 1 87  ? 30.44  -6.447  -2.214  1   70.576  ? 99  LYS   B CA   1 ? 1 
ATOM   1243 C C    . LYS   A 1 87  ? 30.877 -5.174  -2.934  1   74.257  ? 99  LYS   B C    1 ? 1 
ATOM   1244 O O    . LYS   A 1 87  ? 31.031 -5.182  -4.145  1   80.634  ? 99  LYS   B O    1 ? 1 
ATOM   1245 C CB   . LYS   A 1 87  ? 31.631 -7.404  -2.003  1   72.295  ? 99  LYS   B CB   1 ? 1 
ATOM   1246 H H    . LYS   A 1 87  ? 29.406 -7.885  -3.262  1   71.142  ? 99  LYS   B H    1 c 1 
ATOM   1247 H HA   . LYS   A 1 87  ? 30.099 -6.194  -1.319  1   68.565  ? 99  LYS   B HA   1 c 1 
ATOM   1248 H HB2  . LYS   A 1 87  ? 32.414 -6.829  -2.121  0   30      ? 99  LYS   B HB2  1 c 1 
ATOM   1249 H HB3  . LYS   A 1 87  ? 31.232 -8.24   -1.863  0   30      ? 99  LYS   B HB3  1 c 1 
ATOM   1250 N N    . GLY   A 1 88  ? 30.983 -4.064  -2.203  1   72.398  ? 100 GLY   B N    1 ? 1 
ATOM   1251 C CA   . GLY   A 1 88  ? 31.407 -2.814  -2.803  1   77.491  ? 100 GLY   B CA   1 ? 1 
ATOM   1252 C C    . GLY   A 1 88  ? 30.294 -2.066  -3.547  1   73.823  ? 100 GLY   B C    1 ? 1 
ATOM   1253 O O    . GLY   A 1 88  ? 30.563 -1.008  -4.115  1   74.691  ? 100 GLY   B O    1 ? 1 
ATOM   1254 H H    . GLY   A 1 88  ? 30.788 -4.084  -1.31   1   71.682  ? 100 GLY   B H    1 c 1 
ATOM   1255 H HA2  . GLY   A 1 88  ? 31.763 -2.232  -2.093  1   76.774  ? 100 GLY   B HA2  1 c 1 
ATOM   1256 H HA3  . GLY   A 1 88  ? 32.145 -2.999  -3.431  1   79.726  ? 100 GLY   B HA3  1 c 1 
ATOM   1257 N N    . GLU   A 1 89  ? 29.056 -2.589  -3.525  1   70.849  ? 101 GLU   B N    1 ? 1 
ATOM   1258 C CA   . GLU   A 1 89  ? 27.937 -1.876  -4.132  1   68.182  ? 101 GLU   B CA   1 ? 1 
ATOM   1259 C C    . GLU   A 1 89  ? 27.525 -0.681  -3.264  1   64.885  ? 101 GLU   B C    1 ? 1 
ATOM   1260 O O    . GLU   A 1 89  ? 27.569 -0.765  -2.042  1   57.889  ? 101 GLU   B O    1 ? 1 
ATOM   1261 C CB   . GLU   A 1 89  ? 26.768 -2.824  -4.364  1   65.72   ? 101 GLU   B CB   1 ? 1 
ATOM   1262 C CG   . GLU   A 1 89  ? 25.602 -2.24   -5.156  1   64.197  ? 101 GLU   B CG   1 ? 1 
ATOM   1263 C CD   . GLU   A 1 89  ? 24.489 -3.273  -5.307  1   62.605  ? 101 GLU   B CD   1 ? 1 
ATOM   1264 O OE1  . GLU   A 1 89  ? 24.758 -4.429  -5.703  1   65.577  ? 101 GLU   B OE1  1 ? 1 
ATOM   1265 O OE2  . GLU   A 1 89  ? 23.338 -2.92   -4.961  1   58.902  ? 101 GLU   B OE2  1 ? 1 
ATOM   1266 H H    . GLU   A 1 89  ? 28.903 -3.395  -3.124  1   69.633  ? 101 GLU   B H    1 c 1 
ATOM   1267 H HA   . GLU   A 1 89  ? 28.233 -1.537  -5.013  1   70.356  ? 101 GLU   B HA   1 c 1 
ATOM   1268 H HB2  . GLU   A 1 89  ? 27.1   -3.615  -4.838  1   67.428  ? 101 GLU   B HB2  1 c 1 
ATOM   1269 H HB3  . GLU   A 1 89  ? 26.43  -3.121  -3.493  1   63.569  ? 101 GLU   B HB3  1 c 1 
ATOM   1270 H HG2  . GLU   A 1 89  ? 25.247 -1.452  -4.691  1   62.647  ? 101 GLU   B HG2  1 c 1 
ATOM   1271 H HG3  . GLU   A 1 89  ? 25.911 -1.967  -6.046  1   66.611  ? 101 GLU   B HG3  1 c 1 
ATOM   1272 N N    . ILE   A 1 90  ? 27.197 0.457   -3.906  1   65.021  ? 102 ILE   B N    1 ? 1 
ATOM   1273 C CA   . ILE   A 1 90  ? 26.412 1.513   -3.273  1   63.954  ? 102 ILE   B CA   1 ? 1 
ATOM   1274 C C    . ILE   A 1 90  ? 25.03  1.545   -3.922  1   60.331  ? 102 ILE   B C    1 ? 1 
ATOM   1275 O O    . ILE   A 1 90  ? 24.914 1.679   -5.137  1   59.771  ? 102 ILE   B O    1 ? 1 
ATOM   1276 C CB   . ILE   A 1 90  ? 27.069 2.902   -3.325  1   65.365  ? 102 ILE   B CB   1 ? 1 
ATOM   1277 C CG1  . ILE   A 1 90  ? 28.478 2.872   -2.729  1   71.392  ? 102 ILE   B CG1  1 ? 1 
ATOM   1278 C CG2  . ILE   A 1 90  ? 26.207 3.979   -2.654  1   59.772  ? 102 ILE   B CG2  1 ? 1 
ATOM   1279 C CD1  . ILE   A 1 90  ? 29.262 4.157   -2.943  1   72.505  ? 102 ILE   B CD1  1 ? 1 
ATOM   1280 H H    . ILE   A 1 90  ? 27.474 0.576   -4.769  1   67.578  ? 102 ILE   B H    1 c 1 
ATOM   1281 H HA   . ILE   A 1 90  ? 26.301 1.277   -2.336  1   61.426  ? 102 ILE   B HA   1 c 1 
ATOM   1282 H HB   . ILE   A 1 90  ? 27.159 3.145   -4.268  1   67.314  ? 102 ILE   B HB   1 c 1 
ATOM   1283 H HG12 . ILE   A 1 90  ? 28.409 2.701   -1.768  1   68.488  ? 102 ILE   B HG12 1 c 1 
ATOM   1284 H HG13 . ILE   A 1 90  ? 28.975 2.13    -3.131  1   71.358  ? 102 ILE   B HG13 1 c 1 
ATOM   1285 H HG21 . ILE   A 1 90  ? 26.663 4.835   -2.689  1   62.936  ? 102 ILE   B HG21 1 c 1 
ATOM   1286 H HG22 . ILE   A 1 90  ? 26.047 3.737   -1.727  1   59.006  ? 102 ILE   B HG22 1 c 1 
ATOM   1287 H HG23 . ILE   A 1 90  ? 25.356 4.053   -3.118  1   59.423  ? 102 ILE   B HG23 1 c 1 
ATOM   1288 H HD11 . ILE   A 1 90  ? 29.322 4.35    -3.898  1   75.048  ? 102 ILE   B HD11 1 c 1 
ATOM   1289 H HD12 . ILE   A 1 90  ? 30.159 4.047   -2.578  1   75.479  ? 102 ILE   B HD12 1 c 1 
ATOM   1290 H HD13 . ILE   A 1 90  ? 28.82  4.899   -2.49   1   72.218  ? 102 ILE   B HD13 1 c 1 
ATOM   1291 N N    . ALA   A 1 91  ? 24.008 1.51    -3.069  1   55.306  ? 103 ALA   B N    1 ? 1 
ATOM   1292 C CA   . ALA   A 1 91  ? 22.616 1.531   -3.486  1   53.952  ? 103 ALA   B CA   1 ? 1 
ATOM   1293 C C    . ALA   A 1 91  ? 21.87  2.616   -2.714  1   53.076  ? 103 ALA   B C    1 ? 1 
ATOM   1294 O O    . ALA   A 1 91  ? 22.269 2.973   -1.599  1   54.1    ? 103 ALA   B O    1 ? 1 
ATOM   1295 C CB   . ALA   A 1 91  ? 21.992 0.167   -3.258  1   53.23   ? 103 ALA   B CB   1 ? 1 
ATOM   1296 H H    . ALA   A 1 91  ? 24.187 1.473   -2.174  1   55.007  ? 103 ALA   B H    1 c 1 
ATOM   1297 H HA   . ALA   A 1 91  ? 22.58  1.752   -4.455  1   55.721  ? 103 ALA   B HA   1 c 1 
ATOM   1298 H HB1  . ALA   A 1 91  ? 22.47  -0.502  -3.777  1   54.363  ? 103 ALA   B HB1  1 c 1 
ATOM   1299 H HB2  . ALA   A 1 91  ? 22.043 -0.063  -2.315  1   51.658  ? 103 ALA   B HB2  1 c 1 
ATOM   1300 H HB3  . ALA   A 1 91  ? 21.061 0.183   -3.535  1   52.018  ? 103 ALA   B HB3  1 c 1 
ATOM   1301 N N    . HIS   A 1 92  ? 20.823 3.146   -3.362  1   49.895  ? 104 HIS   B N    1 ? 1 
ATOM   1302 C CA   . HIS   A 1 92  ? 19.789 3.998   -2.791  1   47.392  ? 104 HIS   B CA   1 ? 1 
ATOM   1303 C C    . HIS   A 1 92  ? 18.496 3.193   -2.573  1   45.623  ? 104 HIS   B C    1 ? 1 
ATOM   1304 O O    . HIS   A 1 92  ? 18.08  2.453   -3.453  1   50.653  ? 104 HIS   B O    1 ? 1 
ATOM   1305 C CB   . HIS   A 1 92  ? 19.556 5.161   -3.747  1   51.022  ? 104 HIS   B CB   1 ? 1 
ATOM   1306 C CG   . HIS   A 1 92  ? 20.658 6.159   -3.706  1   54.334  ? 104 HIS   B CG   1 ? 1 
ATOM   1307 N ND1  . HIS   A 1 92  ? 20.609 7.325   -4.406  1   57.176  ? 104 HIS   B ND1  1 ? 1 
ATOM   1308 C CD2  . HIS   A 1 92  ? 21.849 6.151   -3.079  1   55.615  ? 104 HIS   B CD2  1 ? 1 
ATOM   1309 C CE1  . HIS   A 1 92  ? 21.727 8       -4.2    1   61.395  ? 104 HIS   B CE1  1 ? 1 
ATOM   1310 N NE2  . HIS   A 1 92  ? 22.481 7.308   -3.372  1   59.371  ? 104 HIS   B NE2  1 ? 1 
ATOM   1311 H H    . HIS   A 1 92  ? 20.75  2.95    -4.252  1   51.536  ? 104 HIS   B H    1 c 1 
ATOM   1312 H HA   . HIS   A 1 92  ? 20.101 4.339   -1.92   1   47.547  ? 104 HIS   B HA   1 c 1 
ATOM   1313 H HB2  . HIS   A 1 92  ? 19.472 4.811   -4.661  1   51.962  ? 104 HIS   B HB2  1 c 1 
ATOM   1314 H HB3  . HIS   A 1 92  ? 18.713 5.605   -3.508  1   49.954  ? 104 HIS   B HB3  1 c 1 
ATOM   1315 H HD1  . HIS   A 1 92  ? 19.991 7.597   -4.943  0   30      ? 104 HIS   B HD1  1 c 1 
ATOM   1316 H HD2  . HIS   A 1 92  ? 22.175 5.484   -2.509  1   54.725  ? 104 HIS   B HD2  1 c 1 
ATOM   1317 H HE1  . HIS   A 1 92  ? 21.932 8.846   -4.56   1   63.066  ? 104 HIS   B HE1  1 c 1 
ATOM   1318 H HE2  . HIS   A 1 92  ? 23.297 7.546   -3.06   0   30      ? 104 HIS   B HE2  1 c 1 
ATOM   1319 N N    . LEU   A 1 93  ? 17.908 3.278   -1.375  1   44.254  ? 105 LEU   B N    1 ? 1 
ATOM   1320 C CA   . LEU   A 1 93  ? 16.662 2.62    -1.009  1   42.718  ? 105 LEU   B CA   1 ? 1 
ATOM   1321 C C    . LEU   A 1 93  ? 15.674 3.681   -0.541  1   45.095  ? 105 LEU   B C    1 ? 1 
ATOM   1322 O O    . LEU   A 1 93  ? 16.031 4.485   0.348   1   41.208  ? 105 LEU   B O    1 ? 1 
ATOM   1323 C CB   . LEU   A 1 93  ? 16.828 1.592   0.122   1   43.473  ? 105 LEU   B CB   1 ? 1 
ATOM   1324 C CG   . LEU   A 1 93  ? 17.695 0.359   -0.145  1   41.731  ? 105 LEU   B CG   1 ? 1 
ATOM   1325 C CD1  . LEU   A 1 93  ? 17.721 -0.566  1.092   1   40.192  ? 105 LEU   B CD1  1 ? 1 
ATOM   1326 C CD2  . LEU   A 1 93  ? 17.229 -0.414  -1.358  1   45.56   ? 105 LEU   B CD2  1 ? 1 
ATOM   1327 H H    . LEU   A 1 93  ? 18.318 3.788   -0.737  1   44.144  ? 105 LEU   B H    1 c 1 
ATOM   1328 H HA   . LEU   A 1 93  ? 16.298 2.17    -1.807  1   44.044  ? 105 LEU   B HA   1 c 1 
ATOM   1329 H HB2  . LEU   A 1 93  ? 17.199 2.062   0.904   1   42.23   ? 105 LEU   B HB2  1 c 1 
ATOM   1330 H HB3  . LEU   A 1 93  ? 15.93  1.282   0.382   1   41.724  ? 105 LEU   B HB3  1 c 1 
ATOM   1331 H HG   . LEU   A 1 93  ? 18.623 0.666   -0.316  1   43.487  ? 105 LEU   B HG   1 c 1 
ATOM   1332 H HD11 . LEU   A 1 93  ? 18.095 -0.086  1.849   1   40.209  ? 105 LEU   B HD11 1 c 1 
ATOM   1333 H HD12 . LEU   A 1 93  ? 18.268 -1.347  0.902   1   41.033  ? 105 LEU   B HD12 1 c 1 
ATOM   1334 H HD13 . LEU   A 1 93  ? 16.816 -0.85   1.304   1   39.739  ? 105 LEU   B HD13 1 c 1 
ATOM   1335 H HD21 . LEU   A 1 93  ? 17.371 0.119   -2.158  1   45.682  ? 105 LEU   B HD21 1 c 1 
ATOM   1336 H HD22 . LEU   A 1 93  ? 16.283 -0.617  -1.27   1   44.128  ? 105 LEU   B HD22 1 c 1 
ATOM   1337 H HD23 . LEU   A 1 93  ? 17.732 -1.242  -1.429  1   45.178  ? 105 LEU   B HD23 1 c 1 
ATOM   1338 N N    . LEU   A 1 94  ? 14.444 3.647   -1.093  1   37.322  ? 106 LEU   B N    1 ? 1 
ATOM   1339 C CA   . LEU   A 1 94  ? 13.336 4.442   -0.582  1   38.092  ? 106 LEU   B CA   1 ? 1 
ATOM   1340 C C    . LEU   A 1 94  ? 12.294 3.481   -0.004  1   40.591  ? 106 LEU   B C    1 ? 1 
ATOM   1341 O O    . LEU   A 1 94  ? 11.897 2.497   -0.685  1   42.243  ? 106 LEU   B O    1 ? 1 
ATOM   1342 C CB   . LEU   A 1 94  ? 12.732 5.291   -1.704  1   39.769  ? 106 LEU   B CB   1 ? 1 
ATOM   1343 C CG   . LEU   A 1 94  ? 11.65  6.304   -1.282  1   41.476  ? 106 LEU   B CG   1 ? 1 
ATOM   1344 C CD1  . LEU   A 1 94  ? 12.126 7.433   -0.327  1   42.362  ? 106 LEU   B CD1  1 ? 1 
ATOM   1345 C CD2  . LEU   A 1 94  ? 11.083 6.916   -2.532  1   47      ? 106 LEU   B CD2  1 ? 1 
ATOM   1346 H H    . LEU   A 1 94  ? 14.296 3.109   -1.818  1   39.823  ? 106 LEU   B H    1 c 1 
ATOM   1347 H HA   . LEU   A 1 94  ? 13.669 5.034   0.138   1   38.244  ? 106 LEU   B HA   1 c 1 
ATOM   1348 H HB2  . LEU   A 1 94  ? 13.464 5.784   -2.142  1   41.035  ? 106 LEU   B HB2  1 c 1 
ATOM   1349 H HB3  . LEU   A 1 94  ? 12.343 4.682   -2.374  1   40.627  ? 106 LEU   B HB3  1 c 1 
ATOM   1350 H HG   . LEU   A 1 94  ? 10.921 5.807   -0.829  1   41.296  ? 106 LEU   B HG   1 c 1 
ATOM   1351 H HD11 . LEU   A 1 94  ? 12.467 7.042   0.495   1   40.94   ? 106 LEU   B HD11 1 c 1 
ATOM   1352 H HD12 . LEU   A 1 94  ? 11.378 8.019   -0.119  1   42.71   ? 106 LEU   B HD12 1 c 1 
ATOM   1353 H HD13 . LEU   A 1 94  ? 12.83  7.948   -0.756  1   43.116  ? 106 LEU   B HD13 1 c 1 
ATOM   1354 H HD21 . LEU   A 1 94  ? 10.712 6.218   -3.097  1   46.333  ? 106 LEU   B HD21 1 c 1 
ATOM   1355 H HD22 . LEU   A 1 94  ? 11.787 7.381   -3.014  1   46.979  ? 106 LEU   B HD22 1 c 1 
ATOM   1356 H HD23 . LEU   A 1 94  ? 10.383 7.547   -2.296  1   46.587  ? 106 LEU   B HD23 1 c 1 
ATOM   1357 N N    . ILE   A 1 95  ? 11.833 3.783   1.214   1   34.904  ? 107 ILE   B N    1 ? 1 
ATOM   1358 C CA   . ILE   A 1 95  ? 11.151 2.816   2.061   1   35.442  ? 107 ILE   B CA   1 ? 1 
ATOM   1359 C C    . ILE   A 1 95  ? 9.86   3.383   2.644   1   38.884  ? 107 ILE   B C    1 ? 1 
ATOM   1360 O O    . ILE   A 1 95  ? 9.884  4.335   3.434   1   37.157  ? 107 ILE   B O    1 ? 1 
ATOM   1361 C CB   . ILE   A 1 95  ? 12.087 2.352   3.192   1   34.15   ? 107 ILE   B CB   1 ? 1 
ATOM   1362 C CG1  . ILE   A 1 95  ? 13.414 1.818   2.665   1   34.566  ? 107 ILE   B CG1  1 ? 1 
ATOM   1363 C CG2  . ILE   A 1 95  ? 11.404 1.327   4.096   1   36.514  ? 107 ILE   B CG2  1 ? 1 
ATOM   1364 C CD1  . ILE   A 1 95  ? 14.52  1.788   3.716   1   36.18   ? 107 ILE   B CD1  1 ? 1 
ATOM   1365 H H    . ILE   A 1 95  ? 11.945 4.633   1.529   1   36.473  ? 107 ILE   B H    1 c 1 
ATOM   1366 H HA   . ILE   A 1 95  ? 10.928 2.038   1.518   1   35.955  ? 107 ILE   B HA   1 c 1 
ATOM   1367 H HB   . ILE   A 1 95  ? 12.289 3.137   3.74    1   34.841  ? 107 ILE   B HB   1 c 1 
ATOM   1368 H HG12 . ILE   A 1 95  ? 13.276 0.91    2.327   1   34.894  ? 107 ILE   B HG12 1 c 1 
ATOM   1369 H HG13 . ILE   A 1 95  ? 13.709 2.375   1.918   1   35.276  ? 107 ILE   B HG13 1 c 1 
ATOM   1370 H HG21 . ILE   A 1 95  ? 12.057 0.936   4.7     1   35.53   ? 107 ILE   B HG21 1 c 1 
ATOM   1371 H HG22 . ILE   A 1 95  ? 11.008 0.625   3.552   1   36.093  ? 107 ILE   B HG22 1 c 1 
ATOM   1372 H HG23 . ILE   A 1 95  ? 10.708 1.762   4.617   1   36.113  ? 107 ILE   B HG23 1 c 1 
ATOM   1373 H HD11 . ILE   A 1 95  ? 14.592 2.667   4.134   1   35.915  ? 107 ILE   B HD11 1 c 1 
ATOM   1374 H HD12 . ILE   A 1 95  ? 15.368 1.562   3.29    1   35.901  ? 107 ILE   B HD12 1 c 1 
ATOM   1375 H HD13 . ILE   A 1 95  ? 14.312 1.122   4.398   1   35.493  ? 107 ILE   B HD13 1 c 1 
ATOM   1376 N N    . LYS   A 1 96  ? 8.735  2.723   2.305   1   37.993  ? 108 LYS   B N    1 ? 1 
ATOM   1377 C CA   . LYS   A 1 96  ? 7.447  3.045   2.885   1   40.443  ? 108 LYS   B CA   1 ? 1 
ATOM   1378 C C    . LYS   A 1 96  ? 7.352  2.491   4.306   1   39.827  ? 108 LYS   B C    1 ? 1 
ATOM   1379 O O    . LYS   A 1 96  ? 8.075  1.537   4.679   1   36.311  ? 108 LYS   B O    1 ? 1 
ATOM   1380 C CB   . LYS   A 1 96  ? 6.328  2.442   1.997   1   41.934  ? 108 LYS   B CB   1 ? 1 
ATOM   1381 C CG   . LYS   A 1 96  ? 6.17   2.984   0.588   1   45.955  ? 108 LYS   B CG   1 ? 1 
ATOM   1382 C CD   . LYS   A 1 96  ? 5.059  2.394   -0.312  1   50.427  ? 108 LYS   B CD   1 ? 1 
ATOM   1383 C CE   . LYS   A 1 96  ? 4.963  3.142   -1.636  1   48.51   ? 108 LYS   B CE   1 ? 1 
ATOM   1384 N NZ   . LYS   A 1 96  ? 4.1    2.315   -2.491  1   57.066  ? 108 LYS   B NZ   1 ? 1 
ATOM   1385 H H    . LYS   A 1 96  ? 8.782  2.049   1.689   1   38.907  ? 108 LYS   B H    1 c 1 
ATOM   1386 H HA   . LYS   A 1 96  ? 7.352  4.03    2.91    1   40.454  ? 108 LYS   B HA   1 c 1 
ATOM   1387 H HB2  . LYS   A 1 96  ? 6.487  1.476   1.929   1   42.508  ? 108 LYS   B HB2  1 c 1 
ATOM   1388 H HB3  . LYS   A 1 96  ? 5.473  2.561   2.46    1   43.693  ? 108 LYS   B HB3  1 c 1 
ATOM   1389 H HG2  . LYS   A 1 96  ? 6.022  3.952   0.657   1   46.017  ? 108 LYS   B HG2  1 c 1 
ATOM   1390 H HG3  . LYS   A 1 96  ? 7.029  2.865   0.127   1   44.997  ? 108 LYS   B HG3  1 c 1 
ATOM   1391 H HD2  . LYS   A 1 96  ? 5.251  1.448   -0.487  1   49.092  ? 108 LYS   B HD2  1 c 1 
ATOM   1392 H HD3  . LYS   A 1 96  ? 4.198  2.452   0.156   1   50.152  ? 108 LYS   B HD3  1 c 1 
ATOM   1393 H HE2  . LYS   A 1 96  ? 4.56   4.02    -1.508  1   51.19   ? 108 LYS   B HE2  1 c 1 
ATOM   1394 H HE3  . LYS   A 1 96  ? 5.84   3.244   -2.046  1   49.686  ? 108 LYS   B HE3  1 c 1 
ATOM   1395 H HZ1  . LYS   A 1 96  ? 3.255  2.322   -2.164  1   56.251  ? 108 LYS   B HZ1  1 c 1 
ATOM   1396 H HZ2  . LYS   A 1 96  ? 4.399  1.462   -2.51   1   54.597  ? 108 LYS   B HZ2  1 c 1 
ATOM   1397 H HZ3  . LYS   A 1 96  ? 4.091  2.653   -3.331  1   56.33   ? 108 LYS   B HZ3  1 c 1 
ATOM   1398 N N    . PRO   A 1 97  ? 6.452  3.061   5.164   1   41.529  ? 109 PRO   B N    1 ? 1 
ATOM   1399 C CA   . PRO   A 1 97  ? 6.45   2.765   6.586   1   41.309  ? 109 PRO   B CA   1 ? 1 
ATOM   1400 C C    . PRO   A 1 97  ? 6.264  1.291   6.954   1   44.548  ? 109 PRO   B C    1 ? 1 
ATOM   1401 O O    . PRO   A 1 97  ? 6.844  0.801   7.909   1   48.029  ? 109 PRO   B O    1 ? 1 
ATOM   1402 C CB   . PRO   A 1 97  ? 5.349  3.645   7.174   1   43.478  ? 109 PRO   B CB   1 ? 1 
ATOM   1403 C CG   . PRO   A 1 97  ? 4.833  4.5     6.083   1   44.898  ? 109 PRO   B CG   1 ? 1 
ATOM   1404 C CD   . PRO   A 1 97  ? 5.465  4.088   4.776   1   48.701  ? 109 PRO   B CD   1 ? 1 
ATOM   1405 H HA   . PRO   A 1 97  ? 7.304  3.066   6.961   1   41.077  ? 109 PRO   B HA   1 c 1 
ATOM   1406 H HB2  . PRO   A 1 97  ? 4.631  3.094   7.543   1   44.865  ? 109 PRO   B HB2  1 c 1 
ATOM   1407 H HB3  . PRO   A 1 97  ? 5.704  4.195   7.899   1   43.662  ? 109 PRO   B HB3  1 c 1 
ATOM   1408 H HG2  . PRO   A 1 97  ? 3.86   4.413   6.022   1   47.334  ? 109 PRO   B HG2  1 c 1 
ATOM   1409 H HG3  . PRO   A 1 97  ? 5.041  5.435   6.265   1   45.87   ? 109 PRO   B HG3  1 c 1 
ATOM   1410 H HD2  . PRO   A 1 97  ? 4.8    3.715   4.167   1   47.058  ? 109 PRO   B HD2  1 c 1 
ATOM   1411 H HD3  . PRO   A 1 97  ? 5.905  4.846   4.346   1   45.714  ? 109 PRO   B HD3  1 c 1 
ATOM   1412 N N    . GLU   A 1 98  ? 5.548  0.553   6.122   1   44.27   ? 110 GLU   B N    1 ? 1 
ATOM   1413 C CA   . GLU   A 1 98  ? 5.268  -0.859  6.35    1   48.083  ? 110 GLU   B CA   1 ? 1 
ATOM   1414 C C    . GLU   A 1 98  ? 6.543  -1.703  6.41    1   45.333  ? 110 GLU   B C    1 ? 1 
ATOM   1415 O O    . GLU   A 1 98  ? 6.502  -2.769  6.979   1   40.979  ? 110 GLU   B O    1 ? 1 
ATOM   1416 C CB   . GLU   A 1 98  ? 4.314  -1.335  5.238   1   48.905  ? 110 GLU   B CB   1 ? 1 
ATOM   1417 C CG   . GLU   A 1 98  ? 2.955  -0.651  5.293   1   55.731  ? 110 GLU   B CG   1 ? 1 
ATOM   1418 C CD   . GLU   A 1 98  ? 2.82   0.726   4.672   1   60.514  ? 110 GLU   B CD   1 ? 1 
ATOM   1419 O OE1  . GLU   A 1 98  ? 3.739  1.182   3.955   1   49.847  ? 110 GLU   B OE1  1 ? 1 
ATOM   1420 O OE2  . GLU   A 1 98  ? 1.746  1.312   4.94    1   67.353  ? 110 GLU   B OE2  1 ? 1 
ATOM   1421 H H    . GLU   A 1 98  ? 5.225  0.941   5.361   1   45.45   ? 110 GLU   B H    1 c 1 
ATOM   1422 H HA   . GLU   A 1 98  ? 4.8    -0.941  7.219   1   48.35   ? 110 GLU   B HA   1 c 1 
ATOM   1423 H HB2  . GLU   A 1 98  ? 4.731  -1.166  4.367   1   49.213  ? 110 GLU   B HB2  1 c 1 
ATOM   1424 H HB3  . GLU   A 1 98  ? 4.187  -2.302  5.325   1   51.149  ? 110 GLU   B HB3  1 c 1 
ATOM   1425 H HG2  . GLU   A 1 98  ? 2.3    -1.239  4.859   1   57.566  ? 110 GLU   B HG2  1 c 1 
ATOM   1426 H HG3  . GLU   A 1 98  ? 2.685  -0.582  6.233   1   56.355  ? 110 GLU   B HG3  1 c 1 
ATOM   1427 N N    . TYR   A 1 99  ? 7.641  -1.235  5.817   1   40.319  ? 111 TYR   B N    1 ? 1 
ATOM   1428 C CA   . TYR   A 1 99  ? 8.892  -1.954  5.783   1   39.625  ? 111 TYR   B CA   1 ? 1 
ATOM   1429 C C    . TYR   A 1 99  ? 9.937  -1.216  6.664   1   40.737  ? 111 TYR   B C    1 ? 1 
ATOM   1430 O O    . TYR   A 1 99  ? 11.12  -1.527  6.617   1   39.53   ? 111 TYR   B O    1 ? 1 
ATOM   1431 C CB   . TYR   A 1 99  ? 9.381  -2.121  4.345   1   36.331  ? 111 TYR   B CB   1 ? 1 
ATOM   1432 C CG   . TYR   A 1 99  ? 8.438  -3      3.506   1   40.107  ? 111 TYR   B CG   1 ? 1 
ATOM   1433 C CD1  . TYR   A 1 99  ? 7.288  -2.491  2.941   1   44.056  ? 111 TYR   B CD1  1 ? 1 
ATOM   1434 C CD2  . TYR   A 1 99  ? 8.667  -4.374  3.393   1   43.045  ? 111 TYR   B CD2  1 ? 1 
ATOM   1435 C CE1  . TYR   A 1 99  ? 6.398  -3.295  2.23    1   44.878  ? 111 TYR   B CE1  1 ? 1 
ATOM   1436 C CE2  . TYR   A 1 99  ? 7.792  -5.206  2.71    1   47.137  ? 111 TYR   B CE2  1 ? 1 
ATOM   1437 C CZ   . TYR   A 1 99  ? 6.659  -4.653  2.114   1   46.155  ? 111 TYR   B CZ   1 ? 1 
ATOM   1438 O OH   . TYR   A 1 99  ? 5.813  -5.458  1.448   1   47.991  ? 111 TYR   B OH   1 ? 1 
ATOM   1439 H H    . TYR   A 1 99  ? 7.601  -0.428  5.392   1   40.686  ? 111 TYR   B H    1 c 1 
ATOM   1440 H HA   . TYR   A 1 99  ? 8.746  -2.859  6.167   1   40.316  ? 111 TYR   B HA   1 c 1 
ATOM   1441 H HB2  . TYR   A 1 99  ? 9.451  -1.234  3.929   1   36.824  ? 111 TYR   B HB2  1 c 1 
ATOM   1442 H HB3  . TYR   A 1 99  ? 10.274 -2.53   4.359   1   36.916  ? 111 TYR   B HB3  1 c 1 
ATOM   1443 H HD1  . TYR   A 1 99  ? 7.107  -1.568  3.02    1   42.525  ? 111 TYR   B HD1  1 c 1 
ATOM   1444 H HD2  . TYR   A 1 99  ? 9.431  -4.749  3.802   1   42.445  ? 111 TYR   B HD2  1 c 1 
ATOM   1445 H HE1  . TYR   A 1 99  ? 5.629  -2.922  1.834   1   46.385  ? 111 TYR   B HE1  1 c 1 
ATOM   1446 H HE2  . TYR   A 1 99  ? 7.974  -6.126  2.625   1   47.187  ? 111 TYR   B HE2  1 c 1 
ATOM   1447 H HH   . TYR   A 1 99  ? 5.198  -4.996  1.073   0   30      ? 111 TYR   B HH   1 c 1 
ATOM   1448 N N    . ALA   A 1 100 ? 9.473  -0.275  7.497   1   40.865  ? 112 ALA   B N    1 ? 1 
ATOM   1449 C CA   . ALA   A 1 100 ? 10.343 0.466   8.399   1   40.251  ? 112 ALA   B CA   1 ? 1 
ATOM   1450 C C    . ALA   A 1 100 ? 9.763  0.455   9.8     1   38.002  ? 112 ALA   B C    1 ? 1 
ATOM   1451 O O    . ALA   A 1 100 ? 9.793  -0.584  10.475  1   39.613  ? 112 ALA   B O    1 ? 1 
ATOM   1452 C CB   . ALA   A 1 100 ? 10.54  1.857   7.811   1   38.274  ? 112 ALA   B CB   1 ? 1 
ATOM   1453 H H    . ALA   A 1 100 ? 8.579  -0.093  7.511   1   41.541  ? 112 ALA   B H    1 c 1 
ATOM   1454 H HA   . ALA   A 1 100 ? 11.225 0.005   8.432   1   38.944  ? 112 ALA   B HA   1 c 1 
ATOM   1455 H HB1  . ALA   A 1 100 ? 11.083 1.798   7.007   1   37.922  ? 112 ALA   B HB1  1 c 1 
ATOM   1456 H HB2  . ALA   A 1 100 ? 9.677  2.243   7.585   1   39.084  ? 112 ALA   B HB2  1 c 1 
ATOM   1457 H HB3  . ALA   A 1 100 ? 10.988 2.427   8.458   1   38.987  ? 112 ALA   B HB3  1 c 1 
ATOM   1458 N N    . TYR   A 1 101 ? 9.149  1.555   10.25   1   40.228  ? 113 TYR   B N    1 ? 1 
ATOM   1459 C CA   . TYR   A 1 101 ? 8.687  1.655   11.628  1   44.104  ? 113 TYR   B CA   1 ? 1 
ATOM   1460 C C    . TYR   A 1 101 ? 7.179  1.746   11.775  1   46.288  ? 113 TYR   B C    1 ? 1 
ATOM   1461 O O    . TYR   A 1 101 ? 6.698  1.871   12.901  1   42.927  ? 113 TYR   B O    1 ? 1 
ATOM   1462 C CB   . TYR   A 1 101 ? 9.388  2.835   12.294  1   47.567  ? 113 TYR   B CB   1 ? 1 
ATOM   1463 C CG   . TYR   A 1 101 ? 10.886 2.585   12.422  1   46.532  ? 113 TYR   B CG   1 ? 1 
ATOM   1464 C CD1  . TYR   A 1 101 ? 11.415 1.754   13.376  1   49.171  ? 113 TYR   B CD1  1 ? 1 
ATOM   1465 C CD2  . TYR   A 1 101 ? 11.758 3.078   11.47   1   46.859  ? 113 TYR   B CD2  1 ? 1 
ATOM   1466 C CE1  . TYR   A 1 101 ? 12.78  1.528   13.484  1   46.857  ? 113 TYR   B CE1  1 ? 1 
ATOM   1467 C CE2  . TYR   A 1 101 ? 13.116 2.858   11.545  1   45.997  ? 113 TYR   B CE2  1 ? 1 
ATOM   1468 C CZ   . TYR   A 1 101 ? 13.644 2.108   12.575  1   47.526  ? 113 TYR   B CZ   1 ? 1 
ATOM   1469 O OH   . TYR   A 1 101 ? 14.981 1.881   12.594  1   48.269  ? 113 TYR   B OH   1 ? 1 
ATOM   1470 H H    . TYR   A 1 101 ? 9.011  2.262   9.688   1   39.847  ? 113 TYR   B H    1 c 1 
ATOM   1471 H HA   . TYR   A 1 101 ? 8.979  0.835   12.102  1   44.942  ? 113 TYR   B HA   1 c 1 
ATOM   1472 H HB2  . TYR   A 1 101 ? 9.237  3.644   11.759  1   46.502  ? 113 TYR   B HB2  1 c 1 
ATOM   1473 H HB3  . TYR   A 1 101 ? 9.006  2.971   13.189  1   48.538  ? 113 TYR   B HB3  1 c 1 
ATOM   1474 H HD1  . TYR   A 1 101 ? 10.843 1.396   14.035  1   49.73   ? 113 TYR   B HD1  1 c 1 
ATOM   1475 H HD2  . TYR   A 1 101 ? 11.423 3.634   10.785  1   45.522  ? 113 TYR   B HD2  1 c 1 
ATOM   1476 H HE1  . TYR   A 1 101 ? 13.119 0.994   14.182  1   49.136  ? 113 TYR   B HE1  1 c 1 
ATOM   1477 H HE2  . TYR   A 1 101 ? 13.69  3.249   10.911  1   45.51   ? 113 TYR   B HE2  1 c 1 
ATOM   1478 H HH   . TYR   A 1 101 ? 15.16  1.356   13.274  0   30      ? 113 TYR   B HH   1 c 1 
ATOM   1479 N N    . GLY   A 1 102 ? 6.442  1.607   10.665  1   43.507  ? 114 GLY   B N    1 ? 1 
ATOM   1480 C CA   . GLY   A 1 102 ? 5.015  1.31    10.697  1   47.937  ? 114 GLY   B CA   1 ? 1 
ATOM   1481 C C    . GLY   A 1 102 ? 4.176  2.447   11.252  1   52.569  ? 114 GLY   B C    1 ? 1 
ATOM   1482 O O    . GLY   A 1 102 ? 4.629  3.593   11.292  1   50.432  ? 114 GLY   B O    1 ? 1 
ATOM   1483 H H    . GLY   A 1 102 ? 6.843  1.708   9.851   1   43.076  ? 114 GLY   B H    1 c 1 
ATOM   1484 H HA2  . GLY   A 1 102 ? 4.715  1.104   9.78    1   47.482  ? 114 GLY   B HA2  1 c 1 
ATOM   1485 H HA3  . GLY   A 1 102 ? 4.872  0.504   11.246  1   49.105  ? 114 GLY   B HA3  1 c 1 
ATOM   1486 N N    . SER   A 1 103 ? 2.963  2.102   11.724  1   55.123  ? 115 SER   B N    1 ? 1 
ATOM   1487 C CA   . SER   A 1 103 ? 2.06   3.138   12.185  1   57.513  ? 115 SER   B CA   1 ? 1 
ATOM   1488 C C    . SER   A 1 103 ? 2.532  3.643   13.535  1   56.632  ? 115 SER   B C    1 ? 1 
ATOM   1489 O O    . SER   A 1 103 ? 2.29   4.787   13.908  1   58.684  ? 115 SER   B O    1 ? 1 
ATOM   1490 C CB   . SER   A 1 103 ? 0.589  2.745   12.18   1   64.765  ? 115 SER   B CB   1 ? 1 
ATOM   1491 O OG   . SER   A 1 103 ? 0.414  1.443   12.681  1   70.583  ? 115 SER   B OG   1 ? 1 
ATOM   1492 H H    . SER   A 1 103 ? 2.703  1.226   11.756  1   55.93   ? 115 SER   B H    1 c 1 
ATOM   1493 H HA   . SER   A 1 103 ? 2.153  3.894   11.556  1   56.685  ? 115 SER   B HA   1 c 1 
ATOM   1494 H HB2  . SER   A 1 103 ? 0.083  3.375   12.727  1   66.731  ? 115 SER   B HB2  1 c 1 
ATOM   1495 H HB3  . SER   A 1 103 ? 0.246  2.789   11.268  1   64.291  ? 115 SER   B HB3  1 c 1 
ATOM   1496 H HG   . SER   A 1 103 ? -0.336 1.178   12.896  0   30      ? 115 SER   B HG   1 c 1 
ATOM   1497 N N    . ALA   A 1 104 ? 3.18   2.773   14.31   1   56.51   ? 116 ALA   B N    1 ? 1 
ATOM   1498 C CA   . ALA   A 1 104 ? 3.601  3.159   15.64   1   57.88   ? 116 ALA   B CA   1 ? 1 
ATOM   1499 C C    . ALA   A 1 104 ? 4.826  4.061   15.561  1   54.398  ? 116 ALA   B C    1 ? 1 
ATOM   1500 O O    . ALA   A 1 104 ? 5.055  4.866   16.466  1   56.543  ? 116 ALA   B O    1 ? 1 
ATOM   1501 C CB   . ALA   A 1 104 ? 3.897  1.947   16.48   1   59.18   ? 116 ALA   B CB   1 ? 1 
ATOM   1502 H H    . ALA   A 1 104 ? 3.355  1.927   14.013  1   55.657  ? 116 ALA   B H    1 c 1 
ATOM   1503 H HA   . ALA   A 1 104 ? 2.862  3.675   16.066  1   60.062  ? 116 ALA   B HA   1 c 1 
ATOM   1504 H HB1  . ALA   A 1 104 ? 3.098  1.398   16.555  1   60.954  ? 116 ALA   B HB1  1 c 1 
ATOM   1505 H HB2  . ALA   A 1 104 ? 4.606  1.427   16.066  1   57.14   ? 116 ALA   B HB2  1 c 1 
ATOM   1506 H HB3  . ALA   A 1 104 ? 4.179  2.225   17.368  1   60.876  ? 116 ALA   B HB3  1 c 1 
ATOM   1507 N N    . GLY   A 1 105 ? 5.645  3.858   14.537  1   52.053  ? 117 GLY   B N    1 ? 1 
ATOM   1508 C CA   . GLY   A 1 105 ? 6.893  4.599   14.45   1   52.358  ? 117 GLY   B CA   1 ? 1 
ATOM   1509 C C    . GLY   A 1 105 ? 7.833  4.179   15.571  1   53.411  ? 117 GLY   B C    1 ? 1 
ATOM   1510 O O    . GLY   A 1 105 ? 7.631  3.107   16.154  1   53.648  ? 117 GLY   B O    1 ? 1 
ATOM   1511 H H    . GLY   A 1 105 ? 5.436  3.252   13.885  1   51.093  ? 117 GLY   B H    1 c 1 
ATOM   1512 H HA2  . GLY   A 1 105 ? 7.315  4.427   13.578  1   49.782  ? 117 GLY   B HA2  1 c 1 
ATOM   1513 H HA3  . GLY   A 1 105 ? 6.705  5.565   14.515  1   52.733  ? 117 GLY   B HA3  1 c 1 
ATOM   1514 N N    . SER   A 1 106 ? 8.8    5.062   15.897  1   51.986  ? 118 SER   B N    1 ? 1 
ATOM   1515 C CA   . SER   A 1 106 ? 9.776  4.806   16.918  1   54.888  ? 118 SER   B CA   1 ? 1 
ATOM   1516 C C    . SER   A 1 106 ? 10.193 6.13    17.552  1   59.333  ? 118 SER   B C    1 ? 1 
ATOM   1517 O O    . SER   A 1 106 ? 11.302 6.64    17.342  1   58.528  ? 118 SER   B O    1 ? 1 
ATOM   1518 C CB   . SER   A 1 106 ? 10.943 4.022   16.381  1   52.591  ? 118 SER   B CB   1 ? 1 
ATOM   1519 O OG   . SER   A 1 106 ? 11.731 3.622   17.481  1   52.238  ? 118 SER   B OG   1 ? 1 
ATOM   1520 H H    . SER   A 1 106 ? 8.836  5.859   15.451  1   52.207  ? 118 SER   B H    1 c 1 
ATOM   1521 H HA   . SER   A 1 106 ? 9.342  4.258   17.621  1   56.749  ? 118 SER   B HA   1 c 1 
ATOM   1522 H HB2  . SER   A 1 106 ? 10.623 3.239   15.896  1   50.544  ? 118 SER   B HB2  1 c 1 
ATOM   1523 H HB3  . SER   A 1 106 ? 11.469 4.579   15.776  1   50.699  ? 118 SER   B HB3  1 c 1 
ATOM   1524 H HG   . SER   A 1 106 ? 12.446 3.193   17.2    0   30      ? 118 SER   B HG   1 c 1 
ATOM   1525 N N    . LEU   A 1 107 ? 9.276  6.627   18.382  1   61.062  ? 119 LEU   B N    1 ? 1 
ATOM   1526 C CA   . LEU   A 1 107 ? 9.29   7.983   18.867  1   67.178  ? 119 LEU   B CA   1 ? 1 
ATOM   1527 C C    . LEU   A 1 107 ? 10.419 8.193   19.876  1   70.234  ? 119 LEU   B C    1 ? 1 
ATOM   1528 O O    . LEU   A 1 107 ? 10.766 7.289   20.651  1   77.106  ? 119 LEU   B O    1 ? 1 
ATOM   1529 C CB   . LEU   A 1 107 ? 7.916  8.282   19.467  1   70.119  ? 119 LEU   B CB   1 ? 1 
ATOM   1530 C CG   . LEU   A 1 107 ? 6.79   8.447   18.425  1   73.352  ? 119 LEU   B CG   1 ? 1 
ATOM   1531 C CD1  . LEU   A 1 107 ? 5.477  8.694   19.157  1   78.722  ? 119 LEU   B CD1  1 ? 1 
ATOM   1532 C CD2  . LEU   A 1 107 ? 7.065  9.55    17.448  1   67.406  ? 119 LEU   B CD2  1 ? 1 
ATOM   1533 H H    . LEU   A 1 107 ? 8.601  6.078   18.66   1   62.825  ? 119 LEU   B H    1 c 1 
ATOM   1534 H HA   . LEU   A 1 107 ? 9.445  8.577   18.094  1   64.979  ? 119 LEU   B HA   1 c 1 
ATOM   1535 H HB2  . LEU   A 1 107 ? 7.674  7.547   20.078  1   72.413  ? 119 LEU   B HB2  1 c 1 
ATOM   1536 H HB3  . LEU   A 1 107 ? 7.98   9.112   19.993  1   73.794  ? 119 LEU   B HB3  1 c 1 
ATOM   1537 H HG   . LEU   A 1 107 ? 6.708  7.599   17.919  1   69.514  ? 119 LEU   B HG   1 c 1 
ATOM   1538 H HD11 . LEU   A 1 107 ? 5.221  7.884   19.625  1   79.046  ? 119 LEU   B HD11 1 c 1 
ATOM   1539 H HD12 . LEU   A 1 107 ? 4.785  8.93    18.516  1   77.446  ? 119 LEU   B HD12 1 c 1 
ATOM   1540 H HD13 . LEU   A 1 107 ? 5.592  9.42    19.793  1   80.882  ? 119 LEU   B HD13 1 c 1 
ATOM   1541 H HD21 . LEU   A 1 107 ? 7.789  9.288   16.855  1   66.123  ? 119 LEU   B HD21 1 c 1 
ATOM   1542 H HD22 . LEU   A 1 107 ? 7.318  10.356  17.93   1   70.883  ? 119 LEU   B HD22 1 c 1 
ATOM   1543 H HD23 . LEU   A 1 107 ? 6.267  9.726   16.922  1   68.302  ? 119 LEU   B HD23 1 c 1 
ATOM   1544 N N    . PRO   A 1 108 ? 11.005 9.412   19.951  1   71.476  ? 120 PRO   B N    1 ? 1 
ATOM   1545 C CA   . PRO   A 1 108 ? 10.665 10.546  19.099  1   69.191  ? 120 PRO   B CA   1 ? 1 
ATOM   1546 C C    . PRO   A 1 108 ? 11.46  10.601  17.798  1   64.852  ? 120 PRO   B C    1 ? 1 
ATOM   1547 O O    . PRO   A 1 108 ? 11.286 11.527  17.017  1   64.686  ? 120 PRO   B O    1 ? 1 
ATOM   1548 C CB   . PRO   A 1 108 ? 11.044 11.75   19.965  1   76.922  ? 120 PRO   B CB   1 ? 1 
ATOM   1549 C CG   . PRO   A 1 108 ? 12.29  11.214  20.648  1   78.374  ? 120 PRO   B CG   1 ? 1 
ATOM   1550 C CD   . PRO   A 1 108 ? 12.023 9.768   20.958  1   76.454  ? 120 PRO   B CD   1 ? 1 
ATOM   1551 H HA   . PRO   A 1 108 ? 9.704  10.555  18.911  1   69.479  ? 120 PRO   B HA   1 c 1 
ATOM   1552 H HB2  . PRO   A 1 108 ? 11.243 12.537  19.42   1   76.093  ? 120 PRO   B HB2  1 c 1 
ATOM   1553 H HB3  . PRO   A 1 108 ? 10.342 11.958  20.613  1   78.735  ? 120 PRO   B HB3  1 c 1 
ATOM   1554 H HG2  . PRO   A 1 108 ? 13.068 11.298  20.061  1   76.778  ? 120 PRO   B HG2  1 c 1 
ATOM   1555 H HG3  . PRO   A 1 108 ? 12.469 11.709  21.469  1   82.067  ? 120 PRO   B HG3  1 c 1 
ATOM   1556 H HD2  . PRO   A 1 108 ? 12.826 9.223   20.849  1   75.271  ? 120 PRO   B HD2  1 c 1 
ATOM   1557 H HD3  . PRO   A 1 108 ? 11.673 9.654   21.861  1   79.183  ? 120 PRO   B HD3  1 c 1 
ATOM   1558 N N    . LYS   A 1 109 ? 12.379 9.644   17.615  1   62.345  ? 121 LYS   B N    1 ? 1 
ATOM   1559 C CA   . LYS   A 1 109 ? 13.322 9.669   16.51   1   60.357  ? 121 LYS   B CA   1 ? 1 
ATOM   1560 C C    . LYS   A 1 109 ? 12.633 9.41    15.169  1   52.566  ? 121 LYS   B C    1 ? 1 
ATOM   1561 O O    . LYS   A 1 109 ? 12.943 10.068  14.197  1   51.359  ? 121 LYS   B O    1 ? 1 
ATOM   1562 C CB   . LYS   A 1 109 ? 14.394 8.6     16.714  1   60.045  ? 121 LYS   B CB   1 ? 1 
ATOM   1563 C CG   . LYS   A 1 109 ? 15.505 8.618   15.659  1   61.582  ? 121 LYS   B CG   1 ? 1 
ATOM   1564 C CD   . LYS   A 1 109 ? 16.612 7.617   15.971  1   66.914  ? 121 LYS   B CD   1 ? 1 
ATOM   1565 C CE   . LYS   A 1 109 ? 17.511 8.091   17.071  1   71.97   ? 121 LYS   B CE   1 ? 1 
ATOM   1566 N NZ   . LYS   A 1 109 ? 18.693 8.759   16.519  1   75.382  ? 121 LYS   B NZ   1 ? 1 
ATOM   1567 H H    . LYS   A 1 109 ? 12.419 8.945   18.203  1   63.221  ? 121 LYS   B H    1 c 1 
ATOM   1568 H HA   . LYS   A 1 109 ? 13.752 10.561  16.483  1   61.158  ? 121 LYS   B HA   1 c 1 
ATOM   1569 H HB2  . LYS   A 1 109 ? 14.798 8.724   17.599  1   63.521  ? 121 LYS   B HB2  1 c 1 
ATOM   1570 H HB3  . LYS   A 1 109 ? 13.967 7.717   16.702  1   59.218  ? 121 LYS   B HB3  1 c 1 
ATOM   1571 H HG2  . LYS   A 1 109 ? 15.117 8.407   14.783  1   59.23   ? 121 LYS   B HG2  1 c 1 
ATOM   1572 H HG3  . LYS   A 1 109 ? 15.888 9.522   15.617  1   63.471  ? 121 LYS   B HG3  1 c 1 
ATOM   1573 H HD2  . LYS   A 1 109 ? 16.207 6.762   16.233  1   64.921  ? 121 LYS   B HD2  1 c 1 
ATOM   1574 H HD3  . LYS   A 1 109 ? 17.146 7.465   15.161  1   64.19   ? 121 LYS   B HD3  1 c 1 
ATOM   1575 H HE2  . LYS   A 1 109 ? 17.038 8.715   17.65   1   74.171  ? 121 LYS   B HE2  1 c 1 
ATOM   1576 H HE3  . LYS   A 1 109 ? 17.797 7.332   17.61   1   73.006  ? 121 LYS   B HE3  1 c 1 
ATOM   1577 H HZ1  . LYS   A 1 109 ? 18.437 9.421   15.956  1   74.024  ? 121 LYS   B HZ1  1 c 1 
ATOM   1578 H HZ2  . LYS   A 1 109 ? 19.199 8.16    16.063  1   73.259  ? 121 LYS   B HZ2  1 c 1 
ATOM   1579 H HZ3  . LYS   A 1 109 ? 19.187 9.114   17.19   1   77.723  ? 121 LYS   B HZ3  1 c 1 
ATOM   1580 N N    . ILE   A 1 110 ? 11.704 8.449   15.105  1   51.691  ? 122 ILE   B N    1 ? 1 
ATOM   1581 C CA   . ILE   A 1 110 ? 10.977 8.146   13.869  1   45.951  ? 122 ILE   B CA   1 ? 1 
ATOM   1582 C C    . ILE   A 1 110 ? 9.491  8.401   14.07   1   48.567  ? 122 ILE   B C    1 ? 1 
ATOM   1583 O O    . ILE   A 1 110 ? 8.91   7.76    14.931  1   48.661  ? 122 ILE   B O    1 ? 1 
ATOM   1584 C CB   . ILE   A 1 110 ? 11.166 6.681   13.463  1   45.354  ? 122 ILE   B CB   1 ? 1 
ATOM   1585 C CG1  . ILE   A 1 110 ? 12.574 6.207   13.581  1   45.364  ? 122 ILE   B CG1  1 ? 1 
ATOM   1586 C CG2  . ILE   A 1 110 ? 10.621 6.441   12.056  1   43.391  ? 122 ILE   B CG2  1 ? 1 
ATOM   1587 C CD1  . ILE   A 1 110 ? 13.558 6.858   12.635  1   43.046  ? 122 ILE   B CD1  1 ? 1 
ATOM   1588 H H    . ILE   A 1 110 ? 11.517 7.96    15.854  1   51.959  ? 122 ILE   B H    1 c 1 
ATOM   1589 H HA   . ILE   A 1 110 ? 11.309 8.717   13.152  1   46.494  ? 122 ILE   B HA   1 c 1 
ATOM   1590 H HB   . ILE   A 1 110 ? 10.632 6.139   14.076  1   45.944  ? 122 ILE   B HB   1 c 1 
ATOM   1591 H HG12 . ILE   A 1 110 ? 12.879 6.358   14.499  1   46.931  ? 122 ILE   B HG12 1 c 1 
ATOM   1592 H HG13 . ILE   A 1 110 ? 12.587 5.241   13.423  1   43.807  ? 122 ILE   B HG13 1 c 1 
ATOM   1593 H HG21 . ILE   A 1 110 ? 10.876 5.555   11.756  1   42.033  ? 122 ILE   B HG21 1 c 1 
ATOM   1594 H HG22 . ILE   A 1 110 ? 10.987 7.104   11.447  1   42.893  ? 122 ILE   B HG22 1 c 1 
ATOM   1595 H HG23 . ILE   A 1 110 ? 9.652  6.51    12.064  1   43.715  ? 122 ILE   B HG23 1 c 1 
ATOM   1596 H HD11 . ILE   A 1 110 ? 13.347 6.609   11.715  1   41.695  ? 122 ILE   B HD11 1 c 1 
ATOM   1597 H HD12 . ILE   A 1 110 ? 14.46  6.556   12.851  1   43.867  ? 122 ILE   B HD12 1 c 1 
ATOM   1598 H HD13 . ILE   A 1 110 ? 13.511 7.828   12.726  1   44.772  ? 122 ILE   B HD13 1 c 1 
ATOM   1599 N N    . PRO   A 1 111 ? 8.796  9.305   13.327  1   48.505  ? 123 PRO   B N    1 ? 1 
ATOM   1600 C CA   . PRO   A 1 111 ? 7.377  9.492   13.58   1   52.102  ? 123 PRO   B CA   1 ? 1 
ATOM   1601 C C    . PRO   A 1 111 ? 6.554  8.332   13.02   1   51.041  ? 123 PRO   B C    1 ? 1 
ATOM   1602 O O    . PRO   A 1 111 ? 7.069  7.446   12.309  1   48.19   ? 123 PRO   B O    1 ? 1 
ATOM   1603 C CB   . PRO   A 1 111 ? 7.026  10.871  12.987  1   54.919  ? 123 PRO   B CB   1 ? 1 
ATOM   1604 C CG   . PRO   A 1 111 ? 8.264  11.313  12.196  1   54.558  ? 123 PRO   B CG   1 ? 1 
ATOM   1605 C CD   . PRO   A 1 111 ? 9.331  10.238  12.326  1   50.045  ? 123 PRO   B CD   1 ? 1 
ATOM   1606 H HA   . PRO   A 1 111 ? 7.234  9.537   14.548  1   54.151  ? 123 PRO   B HA   1 c 1 
ATOM   1607 H HB2  . PRO   A 1 111 ? 6.248  10.808  12.4    1   54.433  ? 123 PRO   B HB2  1 c 1 
ATOM   1608 H HB3  . PRO   A 1 111 ? 6.825  11.511  13.698  1   57.268  ? 123 PRO   B HB3  1 c 1 
ATOM   1609 H HG2  . PRO   A 1 111 ? 8.035  11.443  11.255  1   52.714  ? 123 PRO   B HG2  1 c 1 
ATOM   1610 H HG3  . PRO   A 1 111 ? 8.603  12.161  12.547  1   55.625  ? 123 PRO   B HG3  1 c 1 
ATOM   1611 H HD2  . PRO   A 1 111 ? 9.474  9.782   11.474  1   47.989  ? 123 PRO   B HD2  1 c 1 
ATOM   1612 H HD3  . PRO   A 1 111 ? 10.177 10.62   12.63   1   50.829  ? 123 PRO   B HD3  1 c 1 
ATOM   1613 N N    . SER   A 1 112 ? 5.273  8.341   13.38   1   55.111  ? 124 SER   B N    1 ? 1 
ATOM   1614 C CA   . SER   A 1 112 ? 4.318  7.422   12.786  1   56.235  ? 124 SER   B CA   1 ? 1 
ATOM   1615 C C    . SER   A 1 112 ? 4.314  7.594   11.273  1   54.46   ? 124 SER   B C    1 ? 1 
ATOM   1616 O O    . SER   A 1 112 ? 4.371  8.721   10.775  1   51.745  ? 124 SER   B O    1 ? 1 
ATOM   1617 C CB   . SER   A 1 112 ? 2.971  7.607   13.381  1   61.137  ? 124 SER   B CB   1 ? 1 
ATOM   1618 O OG   . SER   A 1 112 ? 2.542  8.938   13.239  1   71.599  ? 124 SER   B OG   1 ? 1 
ATOM   1619 H H    . SER   A 1 112 ? 4.984  8.935   14.013  1   57.15   ? 124 SER   B H    1 c 1 
ATOM   1620 H HA   . SER   A 1 112 ? 4.62   6.501   12.99   1   55.372  ? 124 SER   B HA   1 c 1 
ATOM   1621 H HB2  . SER   A 1 112 ? 2.337  7.015   12.936  1   62.471  ? 124 SER   B HB2  1 c 1 
ATOM   1622 H HB3  . SER   A 1 112 ? 2.999  7.372   14.328  1   64.043  ? 124 SER   B HB3  1 c 1 
ATOM   1623 H HG   . SER   A 1 112 ? 1.805  8.96    13.548  0   30      ? 124 SER   B HG   1 c 1 
ATOM   1624 N N    . ASN   A 1 113 ? 4.276  6.456   10.568  1   51.357  ? 125 ASN   B N    1 ? 1 
ATOM   1625 C CA   . ASN   A 1 113 ? 3.956  6.403   9.149   1   50.025  ? 125 ASN   B CA   1 ? 1 
ATOM   1626 C C    . ASN   A 1 113 ? 5.068  7.097   8.36    1   48.377  ? 125 ASN   B C    1 ? 1 
ATOM   1627 O O    . ASN   A 1 113 ? 4.773  7.758   7.361   1   45.544  ? 125 ASN   B O    1 ? 1 
ATOM   1628 C CB   . ASN   A 1 113 ? 2.568  6.967   8.884   1   54.567  ? 125 ASN   B CB   1 ? 1 
ATOM   1629 C CG   . ASN   A 1 113 ? 1.485  6.237   9.66    1   52.657  ? 125 ASN   B CG   1 ? 1 
ATOM   1630 O OD1  . ASN   A 1 113 ? 0.604  6.842   10.284  1   55.42   ? 125 ASN   B OD1  1 ? 1 
ATOM   1631 N ND2  . ASN   A 1 113 ? 1.453  4.93    9.533   1   51.461  ? 125 ASN   B ND2  1 ? 1 
ATOM   1632 H H    . ASN   A 1 113 ? 4.462  5.67    10.997  1   51.369  ? 125 ASN   B H    1 c 1 
ATOM   1633 H HA   . ASN   A 1 113 ? 3.945  5.458   8.879   1   49.662  ? 125 ASN   B HA   1 c 1 
ATOM   1634 H HB2  . ASN   A 1 113 ? 2.552  7.914   9.126   1   54.03   ? 125 ASN   B HB2  1 c 1 
ATOM   1635 H HB3  . ASN   A 1 113 ? 2.373  6.898   7.927   1   52.685  ? 125 ASN   B HB3  1 c 1 
ATOM   1636 H HD21 . ASN   A 1 113 ? 0.763  4.479   9.86    1   53.559  ? 125 ASN   B HD21 1 c 1 
ATOM   1637 H HD22 . ASN   A 1 113 ? 2.1    4.496   9.112   1   49.894  ? 125 ASN   B HD22 1 c 1 
ATOM   1638 N N    . ALA   A 1 114 ? 6.339  6.905   8.802   1   45.533  ? 126 ALA   B N    1 ? 1 
ATOM   1639 C CA   . ALA   A 1 114 ? 7.455  7.628   8.182   1   46.488  ? 126 ALA   B CA   1 ? 1 
ATOM   1640 C C    . ALA   A 1 114 ? 8.006  6.846   6.98    1   44.345  ? 126 ALA   B C    1 ? 1 
ATOM   1641 O O    . ALA   A 1 114 ? 8.174  5.616   7.041   1   39.247  ? 126 ALA   B O    1 ? 1 
ATOM   1642 C CB   . ALA   A 1 114 ? 8.526  7.892   9.209   1   45.057  ? 126 ALA   B CB   1 ? 1 
ATOM   1643 H H    . ALA   A 1 114 ? 6.508  6.316   9.48    1   46.252  ? 126 ALA   B H    1 c 1 
ATOM   1644 H HA   . ALA   A 1 114 ? 7.11   8.502   7.851   1   46.717  ? 126 ALA   B HA   1 c 1 
ATOM   1645 H HB1  . ALA   A 1 114 ? 8.158  8.422   9.936   1   47.174  ? 126 ALA   B HB1  1 c 1 
ATOM   1646 H HB2  . ALA   A 1 114 ? 8.856  7.049   9.562   1   44.911  ? 126 ALA   B HB2  1 c 1 
ATOM   1647 H HB3  . ALA   A 1 114 ? 9.261  8.377   8.798   1   45.303  ? 126 ALA   B HB3  1 c 1 
ATOM   1648 N N    . THR   A 1 115 ? 8.208  7.567   5.866   1   40.64   ? 127 THR   B N    1 ? 1 
ATOM   1649 C CA   . THR   A 1 115 ? 9.025  7.093   4.761   1   39.873  ? 127 THR   B CA   1 ? 1 
ATOM   1650 C C    . THR   A 1 115 ? 10.498 7.435   5.032   1   43.365  ? 127 THR   B C    1 ? 1 
ATOM   1651 O O    . THR   A 1 115 ? 10.804 8.546   5.467   1   40.023  ? 127 THR   B O    1 ? 1 
ATOM   1652 C CB   . THR   A 1 115 ? 8.503  7.727   3.472   1   42.641  ? 127 THR   B CB   1 ? 1 
ATOM   1653 O OG1  . THR   A 1 115 ? 7.169  7.249   3.3     1   39.767  ? 127 THR   B OG1  1 ? 1 
ATOM   1654 C CG2  . THR   A 1 115 ? 9.299  7.296   2.255   1   43.186  ? 127 THR   B CG2  1 ? 1 
ATOM   1655 H H    . THR   A 1 115 ? 7.816  8.39    5.795   1   42.825  ? 127 THR   B H    1 c 1 
ATOM   1656 H HA   . THR   A 1 115 ? 8.928  6.121   4.696   1   39.972  ? 127 THR   B HA   1 c 1 
ATOM   1657 H HB   . THR   A 1 115 ? 8.497  8.711   3.547   1   42.929  ? 127 THR   B HB   1 c 1 
ATOM   1658 H HG1  . THR   A 1 115 ? 7.17   6.409   3.24    0   30      ? 127 THR   B HG1  1 c 1 
ATOM   1659 H HG21 . THR   A 1 115 ? 8.952  7.746   1.466   1   43.975  ? 127 THR   B HG21 1 c 1 
ATOM   1660 H HG22 . THR   A 1 115 ? 9.219  6.336   2.138   1   42.093  ? 127 THR   B HG22 1 c 1 
ATOM   1661 H HG23 . THR   A 1 115 ? 10.234 7.532   2.374   1   42.609  ? 127 THR   B HG23 1 c 1 
ATOM   1662 N N    . LEU   A 1 116 ? 11.416 6.523   4.678   1   40.82   ? 128 LEU   B N    1 ? 1 
ATOM   1663 C CA   . LEU   A 1 116 ? 12.84  6.7     4.957   1   40.35   ? 128 LEU   B CA   1 ? 1 
ATOM   1664 C C    . LEU   A 1 116 ? 13.611 6.513   3.663   1   38.923  ? 128 LEU   B C    1 ? 1 
ATOM   1665 O O    . LEU   A 1 116 ? 13.195 5.738   2.794   1   35.068  ? 128 LEU   B O    1 ? 1 
ATOM   1666 C CB   . LEU   A 1 116 ? 13.472 5.706   5.949   1   39.412  ? 128 LEU   B CB   1 ? 1 
ATOM   1667 C CG   . LEU   A 1 116 ? 12.795 5.418   7.292   1   44.387  ? 128 LEU   B CG   1 ? 1 
ATOM   1668 C CD1  . LEU   A 1 116 ? 13.813 4.75    8.27    1   45.423  ? 128 LEU   B CD1  1 ? 1 
ATOM   1669 C CD2  . LEU   A 1 116 ? 12.129 6.544   7.911   1   47.739  ? 128 LEU   B CD2  1 ? 1 
ATOM   1670 H H    . LEU   A 1 116 ? 11.146 5.764   4.246   1   40.37   ? 128 LEU   B H    1 c 1 
ATOM   1671 H HA   . LEU   A 1 116 ? 12.987 7.624   5.284   1   41.217  ? 128 LEU   B HA   1 c 1 
ATOM   1672 H HB2  . LEU   A 1 116 ? 13.581 4.847   5.48    1   39.656  ? 128 LEU   B HB2  1 c 1 
ATOM   1673 H HB3  . LEU   A 1 116 ? 14.387 6.018   6.136   1   41.065  ? 128 LEU   B HB3  1 c 1 
ATOM   1674 H HG   . LEU   A 1 116 ? 12.091 4.741   7.119   1   43.377  ? 128 LEU   B HG   1 c 1 
ATOM   1675 H HD11 . LEU   A 1 116 ? 14.159 3.934   7.872   1   44.442  ? 128 LEU   B HD11 1 c 1 
ATOM   1676 H HD12 . LEU   A 1 116 ? 13.367 4.537   9.106   1   45.71   ? 128 LEU   B HD12 1 c 1 
ATOM   1677 H HD13 . LEU   A 1 116 ? 14.548 5.363   8.443   1   46.04   ? 128 LEU   B HD13 1 c 1 
ATOM   1678 H HD21 . LEU   A 1 116 ? 11.293 6.721   7.45    1   47.039  ? 128 LEU   B HD21 1 c 1 
ATOM   1679 H HD22 . LEU   A 1 116 ? 12.7   7.327   7.855   1   47.929  ? 128 LEU   B HD22 1 c 1 
ATOM   1680 H HD23 . LEU   A 1 116 ? 11.946 6.343   8.844   1   47.682  ? 128 LEU   B HD23 1 c 1 
ATOM   1681 N N    . PHE   A 1 117 ? 14.776 7.178   3.585   1   38.99   ? 129 PHE   B N    1 ? 1 
ATOM   1682 C CA   . PHE   A 1 117 ? 15.7   7.06    2.472   1   38.948  ? 129 PHE   B CA   1 ? 1 
ATOM   1683 C C    . PHE   A 1 117 ? 17.066 6.69    3.023   1   40.562  ? 129 PHE   B C    1 ? 1 
ATOM   1684 O O    . PHE   A 1 117 ? 17.499 7.306   4.02    1   40.615  ? 129 PHE   B O    1 ? 1 
ATOM   1685 C CB   . PHE   A 1 117 ? 15.765 8.356   1.68    1   41.527  ? 129 PHE   B CB   1 ? 1 
ATOM   1686 C CG   . PHE   A 1 117 ? 16.851 8.356   0.604   1   46.585  ? 129 PHE   B CG   1 ? 1 
ATOM   1687 C CD1  . PHE   A 1 117 ? 16.588 7.923   -0.691  1   48.31   ? 129 PHE   B CD1  1 ? 1 
ATOM   1688 C CD2  . PHE   A 1 117 ? 18.125 8.851   0.866   1   49.939  ? 129 PHE   B CD2  1 ? 1 
ATOM   1689 C CE1  . PHE   A 1 117 ? 17.573 7.911   -1.677  1   48.849  ? 129 PHE   B CE1  1 ? 1 
ATOM   1690 C CE2  . PHE   A 1 117 ? 19.116 8.824   -0.111  1   54.478  ? 129 PHE   B CE2  1 ? 1 
ATOM   1691 C CZ   . PHE   A 1 117 ? 18.845 8.345   -1.378  1   52.971  ? 129 PHE   B CZ   1 ? 1 
ATOM   1692 H H    . PHE   A 1 117 ? 15.002 7.737   4.272   1   39.868  ? 129 PHE   B H    1 c 1 
ATOM   1693 H HA   . PHE   A 1 117 ? 15.387 6.335   1.872   1   38.674  ? 129 PHE   B HA   1 c 1 
ATOM   1694 H HB2  . PHE   A 1 117 ? 14.892 8.507   1.254   1   42.108  ? 129 PHE   B HB2  1 c 1 
ATOM   1695 H HB3  . PHE   A 1 117 ? 15.932 9.097   2.304   1   43.104  ? 129 PHE   B HB3  1 c 1 
ATOM   1696 H HD1  . PHE   A 1 117 ? 15.728 7.591   -0.896  1   46.826  ? 129 PHE   B HD1  1 c 1 
ATOM   1697 H HD2  . PHE   A 1 117 ? 18.337 9.147   1.737   1   50.37   ? 129 PHE   B HD2  1 c 1 
ATOM   1698 H HE1  . PHE   A 1 117 ? 17.374 7.587   -2.541  1   50.185  ? 129 PHE   B HE1  1 c 1 
ATOM   1699 H HE2  . PHE   A 1 117 ? 19.981 9.142   0.094   1   54.961  ? 129 PHE   B HE2  1 c 1 
ATOM   1700 H HZ   . PHE   A 1 117 ? 19.511 8.366   -2.047  1   54.372  ? 129 PHE   B HZ   1 c 1 
ATOM   1701 N N    . PHE   A 1 118 ? 17.768 5.794   2.309   1   40.464  ? 130 PHE   B N    1 ? 1 
ATOM   1702 C CA   . PHE   A 1 118 ? 19.128 5.417   2.676   1   44.372  ? 130 PHE   B CA   1 ? 1 
ATOM   1703 C C    . PHE   A 1 118 ? 20.03  5.365   1.45    1   49.243  ? 130 PHE   B C    1 ? 1 
ATOM   1704 O O    . PHE   A 1 118 ? 19.617 4.893   0.38    1   47.329  ? 130 PHE   B O    1 ? 1 
ATOM   1705 C CB   . PHE   A 1 118 ? 19.285 4.035   3.325   1   41.601  ? 130 PHE   B CB   1 ? 1 
ATOM   1706 C CG   . PHE   A 1 118 ? 18.639 3.931   4.682   1   41.842  ? 130 PHE   B CG   1 ? 1 
ATOM   1707 C CD1  . PHE   A 1 118 ? 17.3   3.575   4.795   1   41.745  ? 130 PHE   B CD1  1 ? 1 
ATOM   1708 C CD2  . PHE   A 1 118 ? 19.366 4.19    5.842   1   44.291  ? 130 PHE   B CD2  1 ? 1 
ATOM   1709 C CE1  . PHE   A 1 118 ? 16.707 3.447   6.037   1   41.491  ? 130 PHE   B CE1  1 ? 1 
ATOM   1710 C CE2  . PHE   A 1 118 ? 18.773 4.038   7.062   1   42.485  ? 130 PHE   B CE2  1 ? 1 
ATOM   1711 C CZ   . PHE   A 1 118 ? 17.463 3.679   7.173   1   45.005  ? 130 PHE   B CZ   1 ? 1 
ATOM   1712 H H    . PHE   A 1 118 ? 17.389 5.409   1.572   1   40.682  ? 130 PHE   B H    1 c 1 
ATOM   1713 H HA   . PHE   A 1 118 ? 19.484 6.098   3.302   1   45.042  ? 130 PHE   B HA   1 c 1 
ATOM   1714 H HB2  . PHE   A 1 118 ? 18.886 3.362   2.73    1   41.407  ? 130 PHE   B HB2  1 c 1 
ATOM   1715 H HB3  . PHE   A 1 118 ? 20.243 3.835   3.413   1   43.284  ? 130 PHE   B HB3  1 c 1 
ATOM   1716 H HD1  . PHE   A 1 118 ? 16.798 3.399   4.016   1   40.836  ? 130 PHE   B HD1  1 c 1 
ATOM   1717 H HD2  . PHE   A 1 118 ? 20.281 4.415   5.784   1   45.071  ? 130 PHE   B HD2  1 c 1 
ATOM   1718 H HE1  . PHE   A 1 118 ? 15.799 3.199   6.109   1   41.257  ? 130 PHE   B HE1  1 c 1 
ATOM   1719 H HE2  . PHE   A 1 118 ? 19.274 4.212   7.844   1   45.019  ? 130 PHE   B HE2  1 c 1 
ATOM   1720 H HZ   . PHE   A 1 118 ? 17.063 3.612   8.025   1   43.614  ? 130 PHE   B HZ   1 c 1 
ATOM   1721 N N    . GLU   A 1 119 ? 21.277 5.815   1.633   1   46.642  ? 131 GLU   B N    1 ? 1 
ATOM   1722 C CA   . GLU   A 1 119 ? 22.386 5.405   0.783   1   50.708  ? 131 GLU   B CA   1 ? 1 
ATOM   1723 C C    . GLU   A 1 119 ? 23.168 4.345   1.567   1   54.505  ? 131 GLU   B C    1 ? 1 
ATOM   1724 O O    . GLU   A 1 119 ? 23.565 4.613   2.709   1   55.56   ? 131 GLU   B O    1 ? 1 
ATOM   1725 C CB   . GLU   A 1 119 ? 23.24  6.611   0.378   1   57.025  ? 131 GLU   B CB   1 ? 1 
ATOM   1726 C CG   . GLU   A 1 119 ? 24.427 6.223   -0.492  1   62.386  ? 131 GLU   B CG   1 ? 1 
ATOM   1727 C CD   . GLU   A 1 119 ? 25.186 7.452   -0.965  1   70.33   ? 131 GLU   B CD   1 ? 1 
ATOM   1728 O OE1  . GLU   A 1 119 ? 24.849 8.155   -1.985  1   68.513  ? 131 GLU   B OE1  1 ? 1 
ATOM   1729 O OE2  . GLU   A 1 119 ? 26.137 7.741   -0.185  1   71.227  ? 131 GLU   B OE2  1 ? 1 
ATOM   1730 H H    . GLU   A 1 119 ? 21.443 6.404   2.311   1   48.935  ? 131 GLU   B H    1 c 1 
ATOM   1731 H HA   . GLU   A 1 119 ? 22.018 4.991   -0.037  1   50.956  ? 131 GLU   B HA   1 c 1 
ATOM   1732 H HB2  . GLU   A 1 119 ? 22.678 7.249   -0.109  1   57.072  ? 131 GLU   B HB2  1 c 1 
ATOM   1733 H HB3  . GLU   A 1 119 ? 23.565 7.056   1.189   1   57.727  ? 131 GLU   B HB3  1 c 1 
ATOM   1734 H HG2  . GLU   A 1 119 ? 25.037 5.648   0.018   1   62.813  ? 131 GLU   B HG2  1 c 1 
ATOM   1735 H HG3  . GLU   A 1 119 ? 24.111 5.722   -1.274  1   61.947  ? 131 GLU   B HG3  1 c 1 
ATOM   1736 N N    . ILE   A 1 120 ? 23.412 3.177   0.951   1   53.949  ? 132 ILE   B N    1 ? 1 
ATOM   1737 C CA   . ILE   A 1 120 ? 24.112 2.082   1.602   1   49.24   ? 132 ILE   B CA   1 ? 1 
ATOM   1738 C C    . ILE   A 1 120 ? 25.289 1.635   0.753   1   54.414  ? 132 ILE   B C    1 ? 1 
ATOM   1739 O O    . ILE   A 1 120 ? 25.142 1.369   -0.432  1   51.535  ? 132 ILE   B O    1 ? 1 
ATOM   1740 C CB   . ILE   A 1 120 ? 23.173 0.905   1.884   1   49.06   ? 132 ILE   B CB   1 ? 1 
ATOM   1741 C CG1  . ILE   A 1 120 ? 21.963 1.313   2.732   1   45.131  ? 132 ILE   B CG1  1 ? 1 
ATOM   1742 C CG2  . ILE   A 1 120 ? 23.924 -0.256  2.544   1   49.113  ? 132 ILE   B CG2  1 ? 1 
ATOM   1743 C CD1  . ILE   A 1 120 ? 20.875 0.211   2.78    1   47.133  ? 132 ILE   B CD1  1 ? 1 
ATOM   1744 H H    . ILE   A 1 120 ? 23.13  3.062   0.089   1   52.728  ? 132 ILE   B H    1 c 1 
ATOM   1745 H HA   . ILE   A 1 120 ? 24.454 2.404   2.457   1   51.69   ? 132 ILE   B HA   1 c 1 
ATOM   1746 H HB   . ILE   A 1 120 ? 22.833 0.588   1.024   1   47.859  ? 132 ILE   B HB   1 c 1 
ATOM   1747 H HG12 . ILE   A 1 120 ? 22.263 1.506   3.644   1   46.791  ? 132 ILE   B HG12 1 c 1 
ATOM   1748 H HG13 . ILE   A 1 120 ? 21.572 2.13    2.362   1   46.256  ? 132 ILE   B HG13 1 c 1 
ATOM   1749 H HG21 . ILE   A 1 120 ? 23.308 -0.985  2.724   1   48.091  ? 132 ILE   B HG21 1 c 1 
ATOM   1750 H HG22 . ILE   A 1 120 ? 24.319 0.045   3.38    1   50.042  ? 132 ILE   B HG22 1 c 1 
ATOM   1751 H HG23 . ILE   A 1 120 ? 24.626 -0.571  1.952   1   50.893  ? 132 ILE   B HG23 1 c 1 
ATOM   1752 H HD11 . ILE   A 1 120 ? 20.682 -0.095  1.873   1   45.943  ? 132 ILE   B HD11 1 c 1 
ATOM   1753 H HD12 . ILE   A 1 120 ? 20.062 0.576   3.177   1   44.85   ? 132 ILE   B HD12 1 c 1 
ATOM   1754 H HD13 . ILE   A 1 120 ? 21.187 -0.542  3.316   1   46.145  ? 132 ILE   B HD13 1 c 1 
ATOM   1755 N N    . GLU   A 1 121 ? 26.464 1.549   1.406   1   57.364  ? 133 GLU   B N    1 ? 1 
ATOM   1756 C CA   . GLU   A 1 121 ? 27.61  0.867   0.839   1   59.297  ? 133 GLU   B CA   1 ? 1 
ATOM   1757 C C    . GLU   A 1 121 ? 27.813 -0.488  1.509   1   59.441  ? 133 GLU   B C    1 ? 1 
ATOM   1758 O O    . GLU   A 1 121 ? 27.997 -0.56   2.728   1   58.872  ? 133 GLU   B O    1 ? 1 
ATOM   1759 C CB   . GLU   A 1 121 ? 28.821 1.775   1.014   1   61.97   ? 133 GLU   B CB   1 ? 1 
ATOM   1760 C CG   . GLU   A 1 121 ? 30.084 1.113   0.481   1   65.343  ? 133 GLU   B CG   1 ? 1 
ATOM   1761 C CD   . GLU   A 1 121 ? 31.268 2.026   0.366   1   69.378  ? 133 GLU   B CD   1 ? 1 
ATOM   1762 O OE1  . GLU   A 1 121 ? 31.107 3.245   0.546   1   70.751  ? 133 GLU   B OE1  1 ? 1 
ATOM   1763 O OE2  . GLU   A 1 121 ? 32.322 1.491   0.031   1   71.128  ? 133 GLU   B OE2  1 ? 1 
ATOM   1764 H H    . GLU   A 1 121 ? 26.547 1.932   2.232   1   57.104  ? 133 GLU   B H    1 c 1 
ATOM   1765 H HA   . GLU   A 1 121 ? 27.451 0.731   -0.126  1   59.505  ? 133 GLU   B HA   1 c 1 
ATOM   1766 H HB2  . GLU   A 1 121 ? 28.658 2.618   0.542   1   62.666  ? 133 GLU   B HB2  1 c 1 
ATOM   1767 H HB3  . GLU   A 1 121 ? 28.933 1.979   1.966   1   62.244  ? 133 GLU   B HB3  1 c 1 
ATOM   1768 H HG2  . GLU   A 1 121 ? 30.326 0.368   1.07    1   65.275  ? 133 GLU   B HG2  1 c 1 
ATOM   1769 H HG3  . GLU   A 1 121 ? 29.895 0.738   -0.406  1   65.084  ? 133 GLU   B HG3  1 c 1 
ATOM   1770 N N    . LEU   A 1 122 ? 27.783 -1.566  0.718   1   62.459  ? 134 LEU   B N    1 ? 1 
ATOM   1771 C CA   . LEU   A 1 122 ? 28.094 -2.887  1.253   1   61.509  ? 134 LEU   B CA   1 ? 1 
ATOM   1772 C C    . LEU   A 1 122 ? 29.609 -3.1    1.24    1   66.506  ? 134 LEU   B C    1 ? 1 
ATOM   1773 O O    . LEU   A 1 122 ? 30.21  -3.252  0.172   1   71.073  ? 134 LEU   B O    1 ? 1 
ATOM   1774 C CB   . LEU   A 1 122 ? 27.354 -3.984  0.486   1   60.07   ? 134 LEU   B CB   1 ? 1 
ATOM   1775 C CG   . LEU   A 1 122 ? 27.585 -5.408  0.996   1   58.754  ? 134 LEU   B CG   1 ? 1 
ATOM   1776 C CD1  . LEU   A 1 122 ? 27.315 -5.522  2.497   1   57.112  ? 134 LEU   B CD1  1 ? 1 
ATOM   1777 C CD2  . LEU   A 1 122 ? 26.743 -6.395  0.225   1   58.525  ? 134 LEU   B CD2  1 ? 1 
ATOM   1778 H H    . LEU   A 1 122 ? 27.566 -1.482  -0.166  1   61.437  ? 134 LEU   B H    1 c 1 
ATOM   1779 H HA   . LEU   A 1 122 ? 27.791 -2.907  2.195   1   60.633  ? 134 LEU   B HA   1 c 1 
ATOM   1780 H HB2  . LEU   A 1 122 ? 26.389 -3.791  0.527   1   57.249  ? 134 LEU   B HB2  1 c 1 
ATOM   1781 H HB3  . LEU   A 1 122 ? 27.632 -3.942  -0.458  1   61.001  ? 134 LEU   B HB3  1 c 1 
ATOM   1782 H HG   . LEU   A 1 122 ? 28.536 -5.64   0.84    1   61.807  ? 134 LEU   B HG   1 c 1 
ATOM   1783 H HD11 . LEU   A 1 122 ? 28.011 -5.057  2.99    1   58.631  ? 134 LEU   B HD11 1 c 1 
ATOM   1784 H HD12 . LEU   A 1 122 ? 27.31  -6.459  2.754   1   57.84   ? 134 LEU   B HD12 1 c 1 
ATOM   1785 H HD13 . LEU   A 1 122 ? 26.452 -5.126  2.704   1   54.964  ? 134 LEU   B HD13 1 c 1 
ATOM   1786 H HD21 . LEU   A 1 122 ? 26.945 -6.326  -0.722  1   59.567  ? 134 LEU   B HD21 1 c 1 
ATOM   1787 H HD22 . LEU   A 1 122 ? 25.801 -6.2    0.368   1   56.118  ? 134 LEU   B HD22 1 c 1 
ATOM   1788 H HD23 . LEU   A 1 122 ? 26.936 -7.297  0.531   1   59.372  ? 134 LEU   B HD23 1 c 1 
ATOM   1789 N N    . LEU   A 1 123 ? 30.231 -3.088  2.429   1   67.182  ? 135 LEU   B N    1 ? 1 
ATOM   1790 C CA   . LEU   A 1 123 ? 31.688 -3.173  2.528   1   69.233  ? 135 LEU   B CA   1 ? 1 
ATOM   1791 C C    . LEU   A 1 123 ? 32.13  -4.633  2.441   1   71.918  ? 135 LEU   B C    1 ? 1 
ATOM   1792 O O    . LEU   A 1 123 ? 32.99  -4.979  1.636   1   74.718  ? 135 LEU   B O    1 ? 1 
ATOM   1793 C CB   . LEU   A 1 123 ? 32.164 -2.547  3.835   1   72.093  ? 135 LEU   B CB   1 ? 1 
ATOM   1794 C CG   . LEU   A 1 123 ? 31.742 -1.095  4.092   1   72.615  ? 135 LEU   B CG   1 ? 1 
ATOM   1795 C CD1  . LEU   A 1 123 ? 32.112 -0.656  5.507   1   75.686  ? 135 LEU   B CD1  1 ? 1 
ATOM   1796 C CD2  . LEU   A 1 123 ? 32.413 -0.164  3.079   1   73.592  ? 135 LEU   B CD2  1 ? 1 
ATOM   1797 H H    . LEU   A 1 123 ? 29.738 -3.028  3.196   1   65.139  ? 135 LEU   B H    1 c 1 
ATOM   1798 H HA   . LEU   A 1 123 ? 32.084 -2.677  1.767   1   71.739  ? 135 LEU   B HA   1 c 1 
ATOM   1799 H HB2  . LEU   A 1 123 ? 31.832 -3.101  4.578   1   71.066  ? 135 LEU   B HB2  1 c 1 
ATOM   1800 H HB3  . LEU   A 1 123 ? 33.148 -2.591  3.854   1   75.63   ? 135 LEU   B HB3  1 c 1 
ATOM   1801 H HG   . LEU   A 1 123 ? 30.759 -1.025  3.985   1   68.919  ? 135 LEU   B HG   1 c 1 
ATOM   1802 H HD11 . LEU   A 1 123 ? 31.696 -1.253  6.152   1   73.931  ? 135 LEU   B HD11 1 c 1 
ATOM   1803 H HD12 . LEU   A 1 123 ? 31.799 0.251   5.659   1   74.734  ? 135 LEU   B HD12 1 c 1 
ATOM   1804 H HD13 . LEU   A 1 123 ? 33.078 -0.686  5.615   1   78.851  ? 135 LEU   B HD13 1 c 1 
ATOM   1805 H HD21 . LEU   A 1 123 ? 32.164 -0.427  2.178   1   73.207  ? 135 LEU   B HD21 1 c 1 
ATOM   1806 H HD22 . LEU   A 1 123 ? 33.377 -0.223  3.179   1   77.603  ? 135 LEU   B HD22 1 c 1 
ATOM   1807 H HD23 . LEU   A 1 123 ? 32.127 0.751   3.239   1   73.619  ? 135 LEU   B HD23 1 c 1 
ATOM   1808 N N    . ASP   A 1 124 ? 31.54  -5.486  3.292   1   70.201  ? 136 ASP   B N    1 ? 1 
ATOM   1809 C CA   . ASP   A 1 124 ? 31.875 -6.905  3.314   1   72.563  ? 136 ASP   B CA   1 ? 1 
ATOM   1810 C C    . ASP   A 1 124 ? 30.755 -7.699  3.989   1   69.307  ? 136 ASP   B C    1 ? 1 
ATOM   1811 O O    . ASP   A 1 124 ? 29.908 -7.134  4.679   1   66.264  ? 136 ASP   B O    1 ? 1 
ATOM   1812 C CB   . ASP   A 1 124 ? 33.216 -7.148  3.997   1   78.492  ? 136 ASP   B CB   1 ? 1 
ATOM   1813 C CG   . ASP   A 1 124 ? 33.939 -8.43   3.6     1   83.14   ? 136 ASP   B CG   1 ? 1 
ATOM   1814 O OD1  . ASP   A 1 124 ? 33.386 -9.503  3.797   1   86.125  ? 136 ASP   B OD1  1 ? 1 
ATOM   1815 O OD2  . ASP   A 1 124 ? 35.056 -8.36   3.071   1   90.454  ? 136 ASP   B OD2  1 ? 1 
ATOM   1816 H H    . ASP   A 1 124 ? 30.912 -5.173  3.877   1   68.17   ? 136 ASP   B H    1 c 1 
ATOM   1817 H HA   . ASP   A 1 124 ? 31.955 -7.216  2.384   1   73.257  ? 136 ASP   B HA   1 c 1 
ATOM   1818 H HB2  . ASP   A 1 124 ? 33.812 -6.395  3.802   1   80.106  ? 136 ASP   B HB2  1 c 1 
ATOM   1819 H HB3  . ASP   A 1 124 ? 33.074 -7.17   4.967   1   78.141  ? 136 ASP   B HB3  1 c 1 
ATOM   1820 N N    . PHE   A 1 125 ? 30.747 -9.019  3.767   1   71.392  ? 137 PHE   B N    1 ? 1 
ATOM   1821 C CA   . PHE   A 1 125 ? 29.832 -9.928  4.453   1   72.842  ? 137 PHE   B CA   1 ? 1 
ATOM   1822 C C    . PHE   A 1 125 ? 30.521 -11.289 4.597   1   76.378  ? 137 PHE   B C    1 ? 1 
ATOM   1823 O O    . PHE   A 1 125 ? 31.112 -11.784 3.641   1   84.469  ? 137 PHE   B O    1 ? 1 
ATOM   1824 C CB   . PHE   A 1 125 ? 28.464 -10.025 3.752   1   69.974  ? 137 PHE   B CB   1 ? 1 
ATOM   1825 C CG   . PHE   A 1 125 ? 28.449 -10.521 2.304   1   71.254  ? 137 PHE   B CG   1 ? 1 
ATOM   1826 C CD1  . PHE   A 1 125 ? 28.618 -9.646  1.232   1   69.044  ? 137 PHE   B CD1  1 ? 1 
ATOM   1827 C CD2  . PHE   A 1 125 ? 28.262 -11.867 2.013   1   70.272  ? 137 PHE   B CD2  1 ? 1 
ATOM   1828 C CE1  . PHE   A 1 125 ? 28.598 -10.117 -0.075  1   70.572  ? 137 PHE   B CE1  1 ? 1 
ATOM   1829 C CE2  . PHE   A 1 125 ? 28.272 -12.33  0.709   1   71.61   ? 137 PHE   B CE2  1 ? 1 
ATOM   1830 C CZ   . PHE   A 1 125 ? 28.446 -11.465 -0.332  1   73.086  ? 137 PHE   B CZ   1 ? 1 
ATOM   1831 H H    . PHE   A 1 125 ? 31.33  -9.367  3.155   1   73.988  ? 137 PHE   B H    1 c 1 
ATOM   1832 H HA   . PHE   A 1 125 ? 29.679 -9.566  5.363   1   71.562  ? 137 PHE   B HA   1 c 1 
ATOM   1833 H HB2  . PHE   A 1 125 ? 27.892 -10.619 4.287   1   69.42   ? 137 PHE   B HB2  1 c 1 
ATOM   1834 H HB3  . PHE   A 1 125 ? 28.049 -9.134  3.776   1   67.758  ? 137 PHE   B HB3  1 c 1 
ATOM   1835 H HD1  . PHE   A 1 125 ? 28.738 -8.724  1.397   1   68.565  ? 137 PHE   B HD1  1 c 1 
ATOM   1836 H HD2  . PHE   A 1 125 ? 28.16  -12.482 2.722   1   71.497  ? 137 PHE   B HD2  1 c 1 
ATOM   1837 H HE1  . PHE   A 1 125 ? 28.723 -9.515  -0.791  1   70.819  ? 137 PHE   B HE1  1 c 1 
ATOM   1838 H HE2  . PHE   A 1 125 ? 28.149 -13.25  0.538   1   73.652  ? 137 PHE   B HE2  1 c 1 
ATOM   1839 H HZ   . PHE   A 1 125 ? 28.428 -11.781 -1.221  1   73.832  ? 137 PHE   B HZ   1 c 1 
ATOM   1840 N N    . LYS   A 1 126 ? 30.462 -11.866 5.807   1   76.781  ? 138 LYS   B N    1 ? 1 
ATOM   1841 C CA   . LYS   A 1 126 ? 31.119 -13.129 6.141   1   78.584  ? 138 LYS   B CA   1 ? 1 
ATOM   1842 C C    . LYS   A 1 126 ? 30.072 -14.101 6.698   1   76.495  ? 138 LYS   B C    1 ? 1 
ATOM   1843 O O    . LYS   A 1 126 ? 29.079 -13.707 7.303   1   69.453  ? 138 LYS   B O    1 ? 1 
ATOM   1844 C CB   . LYS   A 1 126 ? 32.286 -12.866 7.105   1   81.002  ? 138 LYS   B CB   1 ? 1 
ATOM   1845 H H    . LYS   A 1 126 ? 29.977 -11.45  6.461   1   74.694  ? 138 LYS   B H    1 c 1 
ATOM   1846 H HA   . LYS   A 1 126 ? 31.49  -13.517 5.308   1   80.076  ? 138 LYS   B HA   1 c 1 
ATOM   1847 H HB2  . LYS   A 1 126 ? 33.044 -12.992 6.617   0   30      ? 138 LYS   B HB2  1 c 1 
ATOM   1848 H HB3  . LYS   A 1 126 ? 31.798 -12.58  7.933   0   30      ? 138 LYS   B HB3  1 c 1 
ATOM   1849 N N    . GLY   A 1 127 ? 30.321 -15.398 6.496   1   82.525  ? 139 GLY   B N    1 ? 1 
ATOM   1850 C CA   . GLY   A 1 127 ? 29.384 -16.421 6.927   1   85.031  ? 139 GLY   B CA   1 ? 1 
ATOM   1851 C C    . GLY   A 1 127 ? 29.418 -16.583 8.441   1   87.295  ? 139 GLY   B C    1 ? 1 
ATOM   1852 O O    . GLY   A 1 127 ? 30.489 -16.511 9.038   1   90.223  ? 139 GLY   B O    1 ? 1 
ATOM   1853 H H    . GLY   A 1 127 ? 31.093 -15.652 6.078   1   84.763  ? 139 GLY   B H    1 c 1 
ATOM   1854 H HA2  . GLY   A 1 127 ? 28.474 -16.173 6.638   1   81.677  ? 139 GLY   B HA2  1 c 1 
ATOM   1855 H HA3  . GLY   A 1 127 ? 29.618 -17.277 6.498   1   87.109  ? 139 GLY   B HA3  1 c 1 
ATOM   1856 N N    . GLU   A 1 128 ? 28.233 -16.742 9.042   1   87.617  ? 140 GLU   B N    1 ? 1 
ATOM   1857 C CA   . GLU   A 1 128 ? 28.134 -17.307 10.377  1   92.148  ? 140 GLU   B CA   1 ? 1 
ATOM   1858 C C    . GLU   A 1 128 ? 29.156 -18.469 10.493  1   95.654  ? 140 GLU   B C    1 ? 1 
ATOM   1859 O O    . GLU   A 1 128 ? 29.577 -19.012 9.435   1   94.373  ? 140 GLU   B O    1 ? 1 
ATOM   1860 C CB   . GLU   A 1 128 ? 26.677 -17.682 10.677  1   92.442  ? 140 GLU   B CB   1 ? 1 
ATOM   1861 O OXT  . GLU   A 1 128 ? 29.535 -18.778 11.632  1   99.045  ? 140 GLU   B OXT  1 ? 1 
ATOM   1862 H H    . GLU   A 1 128 ? 27.469 -16.484 8.61    1   84.749  ? 140 GLU   B H    1 c 1 
ATOM   1863 H HA   . GLU   A 1 128 ? 28.399 -16.604 11.023  1   91.39   ? 140 GLU   B HA   1 c 1 
ATOM   1864 H HB2  . GLU   A 1 128 ? 26.87  -18.634 11.356  0   30      ? 140 GLU   B HB2  1 c 1 
ATOM   1865 H HB3  . GLU   A 1 128 ? 26.127 -17.239 10.38   0   30      ? 140 GLU   B HB3  1 c 1 
ATOM   1866 N N    . THR   B 1 5   ? 0.263  -3.379  43.766  1   78.349  ? 17  THR   A N    1 ? 2 
ATOM   1867 C CA   . THR   B 1 5   ? 1.478  -3.855  43.041  1   79.237  ? 17  THR   A CA   1 ? 2 
ATOM   1868 C C    . THR   B 1 5   ? 2.031  -2.753  42.112  1   77.981  ? 17  THR   A C    1 ? 2 
ATOM   1869 O O    . THR   B 1 5   ? 1.346  -1.781  41.774  1   76.004  ? 17  THR   A O    1 ? 2 
ATOM   1870 C CB   . THR   B 1 5   ? 1.225  -5.179  42.292  1   77.369  ? 17  THR   A CB   1 ? 2 
ATOM   1871 O OG1  . THR   B 1 5   ? 0.385  -4.919  41.171  1   75.801  ? 17  THR   A OG1  1 ? 2 
ATOM   1872 C CG2  . THR   B 1 5   ? 0.605  -6.273  43.15   1   75.128  ? 17  THR   A CG2  1 ? 2 
ATOM   1873 H H    . THR   B 1 5   ? 0.082  -3.933  44.454  1   80.197  ? 17  THR   A H    1 c 2 
ATOM   1874 H HA   . THR   B 1 5   ? 2.16   -4.033  43.72   1   78.562  ? 17  THR   A HA   1 c 2 
ATOM   1875 H HB   . THR   B 1 5   ? 2.091  -5.517  41.962  1   74.421  ? 17  THR   A HB   1 c 2 
ATOM   1876 H HG1  . THR   B 1 5   ? -0.38  -4.4    41.609  0   30      ? 17  THR   A HG1  1 c 2 
ATOM   1877 H HG21 . THR   B 1 5   ? 0.481  -7.074  42.613  1   74.064  ? 17  THR   A HG21 1 c 2 
ATOM   1878 H HG22 . THR   B 1 5   ? -0.257 -5.975  43.487  1   78.006  ? 17  THR   A HG22 1 c 2 
ATOM   1879 H HG23 . THR   B 1 5   ? 1.192  -6.474  43.896  1   76.234  ? 17  THR   A HG23 1 c 2 
ATOM   1880 N N    . VAL   B 1 6   ? 3.318  -2.918  41.742  1   75.248  ? 18  VAL   A N    1 ? 2 
ATOM   1881 C CA   . VAL   B 1 6   ? 4.079  -2.021  40.878  1   72.982  ? 18  VAL   A CA   1 ? 2 
ATOM   1882 C C    . VAL   B 1 6   ? 4.266  -2.761  39.552  1   71.069  ? 18  VAL   A C    1 ? 2 
ATOM   1883 O O    . VAL   B 1 6   ? 4.079  -3.98   39.477  1   69.586  ? 18  VAL   A O    1 ? 2 
ATOM   1884 C CB   . VAL   B 1 6   ? 5.443  -1.551  41.455  1   75.162  ? 18  VAL   A CB   1 ? 2 
ATOM   1885 C CG1  . VAL   B 1 6   ? 5.29   -0.522  42.581  1   76.265  ? 18  VAL   A CG1  1 ? 2 
ATOM   1886 C CG2  . VAL   B 1 6   ? 6.332  -2.711  41.928  1   77.518  ? 18  VAL   A CG2  1 ? 2 
ATOM   1887 H H    . VAL   B 1 6   ? 3.747  -3.663  42.053  1   73.689  ? 18  VAL   A H    1 c 2 
ATOM   1888 H HA   . VAL   B 1 6   ? 3.534  -1.229  40.709  1   75.772  ? 18  VAL   A HA   1 c 2 
ATOM   1889 H HB   . VAL   B 1 6   ? 5.922  -1.102  40.72   1   74.737  ? 18  VAL   A HB   1 c 2 
ATOM   1890 H HG11 . VAL   B 1 6   ? 4.822  -0.927  43.331  1   77.827  ? 18  VAL   A HG11 1 c 2 
ATOM   1891 H HG12 . VAL   B 1 6   ? 4.782  0.241   42.258  1   78.765  ? 18  VAL   A HG12 1 c 2 
ATOM   1892 H HG13 . VAL   B 1 6   ? 6.169  -0.225  42.872  1   77.92   ? 18  VAL   A HG13 1 c 2 
ATOM   1893 H HG21 . VAL   B 1 6   ? 7.175  -2.358  42.26   1   77.1    ? 18  VAL   A HG21 1 c 2 
ATOM   1894 H HG22 . VAL   B 1 6   ? 6.506  -3.313  41.184  1   73.75   ? 18  VAL   A HG22 1 c 2 
ATOM   1895 H HG23 . VAL   B 1 6   ? 5.884  -3.197  42.64   1   76.559  ? 18  VAL   A HG23 1 c 2 
ATOM   1896 N N    . THR   B 1 7   ? 4.563  -2.004  38.486  1   69.378  ? 19  THR   A N    1 ? 2 
ATOM   1897 C CA   . THR   B 1 7   ? 4.847  -2.586  37.173  1   69.341  ? 19  THR   A CA   1 ? 2 
ATOM   1898 C C    . THR   B 1 7   ? 6.194  -3.329  37.223  1   61.006  ? 19  THR   A C    1 ? 2 
ATOM   1899 O O    . THR   B 1 7   ? 6.281  -4.508  36.893  1   60.761  ? 19  THR   A O    1 ? 2 
ATOM   1900 C CB   . THR   B 1 7   ? 4.86   -1.504  36.08   1   70.45   ? 19  THR   A CB   1 ? 2 
ATOM   1901 O OG1  . THR   B 1 7   ? 3.821  -0.522  36.239  1   70.604  ? 19  THR   A OG1  1 ? 2 
ATOM   1902 C CG2  . THR   B 1 7   ? 4.86   -2.136  34.689  1   64.528  ? 19  THR   A CG2  1 ? 2 
ATOM   1903 H H    . THR   B 1 7   ? 4.59   -1.094  38.578  1   72.408  ? 19  THR   A H    1 c 2 
ATOM   1904 H HA   . THR   B 1 7   ? 4.14   -3.23   36.961  1   66.719  ? 19  THR   A HA   1 c 2 
ATOM   1905 H HB   . THR   B 1 7   ? 5.724  -1.032  36.156  1   69.753  ? 19  THR   A HB   1 c 2 
ATOM   1906 H HG1  . THR   B 1 7   ? 2.989  -0.93   36.192  0   30      ? 19  THR   A HG1  1 c 2 
ATOM   1907 H HG21 . THR   B 1 7   ? 4.795  -1.438  34.016  1   66.522  ? 19  THR   A HG21 1 c 2 
ATOM   1908 H HG22 . THR   B 1 7   ? 4.1    -2.736  34.605  1   64.824  ? 19  THR   A HG22 1 c 2 
ATOM   1909 H HG23 . THR   B 1 7   ? 5.683  -2.635  34.558  1   63.992  ? 19  THR   A HG23 1 c 2 
ATOM   1910 N N    . GLU   B 1 8   ? 7.248  -2.641  37.69   1   64.307  ? 20  GLU   A N    1 ? 2 
ATOM   1911 C CA   . GLU   B 1 8   ? 8.606  -3.168  37.745  1   64.047  ? 20  GLU   A CA   1 ? 2 
ATOM   1912 C C    . GLU   B 1 8   ? 8.806  -4.049  38.984  1   55.861  ? 20  GLU   A C    1 ? 2 
ATOM   1913 O O    . GLU   B 1 8   ? 9.763  -3.834  39.761  1   57.092  ? 20  GLU   A O    1 ? 2 
ATOM   1914 C CB   . GLU   B 1 8   ? 9.666  -2.057  37.772  1   71.331  ? 20  GLU   A CB   1 ? 2 
ATOM   1915 C CG   . GLU   B 1 8   ? 9.487  -0.947  36.733  1   80.216  ? 20  GLU   A CG   1 ? 2 
ATOM   1916 C CD   . GLU   B 1 8   ? 9.362  -1.335  35.261  1   79.896  ? 20  GLU   A CD   1 ? 2 
ATOM   1917 O OE1  . GLU   B 1 8   ? 9.618  -2.505  34.856  1   70.52   ? 20  GLU   A OE1  1 ? 2 
ATOM   1918 O OE2  . GLU   B 1 8   ? 8.959  -0.391  34.52   1   81.279  ? 20  GLU   A OE2  1 ? 2 
ATOM   1919 H H    . GLU   B 1 8   ? 7.106  -1.791  37.997  1   66.35   ? 20  GLU   A H    1 c 2 
ATOM   1920 H HA   . GLU   B 1 8   ? 8.755  -3.724  36.939  1   61.314  ? 20  GLU   A HA   1 c 2 
ATOM   1921 H HB2  . GLU   B 1 8   ? 9.671  -1.644  38.661  1   73.419  ? 20  GLU   A HB2  1 c 2 
ATOM   1922 H HB3  . GLU   B 1 8   ? 10.54  -2.456  37.624  1   70.983  ? 20  GLU   A HB3  1 c 2 
ATOM   1923 H HG2  . GLU   B 1 8   ? 8.687  -0.434  36.971  1   80.015  ? 20  GLU   A HG2  1 c 2 
ATOM   1924 H HG3  . GLU   B 1 8   ? 10.24  -0.328  36.813  1   80.272  ? 20  GLU   A HG3  1 c 2 
ATOM   1925 N N    . GLN   B 1 9   ? 7.895  -5.007  39.192  1   54.794  ? 21  GLN   A N    1 ? 2 
ATOM   1926 C CA   . GLN   B 1 9   ? 8.048  -6.043  40.237  1   61.183  ? 21  GLN   A CA   1 ? 2 
ATOM   1927 C C    . GLN   B 1 9   ? 8.521  -7.37   39.612  1   60.563  ? 21  GLN   A C    1 ? 2 
ATOM   1928 O O    . GLN   B 1 9   ? 8.384  -7.536  38.372  1   59.61   ? 21  GLN   A O    1 ? 2 
ATOM   1929 C CB   . GLN   B 1 9   ? 6.676  -6.438  40.775  1   64.494  ? 21  GLN   A CB   1 ? 2 
ATOM   1930 C CG   . GLN   B 1 9   ? 5.723  -6.851  39.64   1   62.453  ? 21  GLN   A CG   1 ? 2 
ATOM   1931 C CD   . GLN   B 1 9   ? 4.416  -7.412  40.121  1   73.96   ? 21  GLN   A CD   1 ? 2 
ATOM   1932 O OE1  . GLN   B 1 9   ? 4.206  -7.553  41.34   1   76.855  ? 21  GLN   A OE1  1 ? 2 
ATOM   1933 N NE2  . GLN   B 1 9   ? 3.535  -7.667  39.157  1   69.823  ? 21  GLN   A NE2  1 ? 2 
ATOM   1934 H H    . GLN   B 1 9   ? 7.158  -5.035  38.655  1   55.892  ? 21  GLN   A H    1 c 2 
ATOM   1935 H HA   . GLN   B 1 9   ? 8.669  -5.738  40.945  1   61.886  ? 21  GLN   A HA   1 c 2 
ATOM   1936 H HB2  . GLN   B 1 9   ? 6.774  -7.182  41.406  1   63.654  ? 21  GLN   A HB2  1 c 2 
ATOM   1937 H HB3  . GLN   B 1 9   ? 6.29   -5.679  41.261  1   65.697  ? 21  GLN   A HB3  1 c 2 
ATOM   1938 H HG2  . GLN   B 1 9   ? 5.533  -6.075  39.075  1   65.11   ? 21  GLN   A HG2  1 c 2 
ATOM   1939 H HG3  . GLN   B 1 9   ? 6.154  -7.527  39.079  1   63.092  ? 21  GLN   A HG3  1 c 2 
ATOM   1940 H HE21 . GLN   B 1 9   ? 2.738  -7.997  39.364  1   71.35   ? 21  GLN   A HE21 1 c 2 
ATOM   1941 H HE22 . GLN   B 1 9   ? 3.742  -7.508  38.309  1   69.795  ? 21  GLN   A HE22 1 c 2 
ATOM   1942 N N    . GLY   B 1 10  ? 8.957  -8.326  40.453  1   53.886  ? 22  GLY   A N    1 ? 2 
ATOM   1943 C CA   . GLY   B 1 10  ? 9.605  -9.511  39.929  1   53.754  ? 22  GLY   A CA   1 ? 2 
ATOM   1944 C C    . GLY   B 1 10  ? 11.128 -9.481  40.101  1   47.894  ? 22  GLY   A C    1 ? 2 
ATOM   1945 O O    . GLY   B 1 10  ? 11.742 -8.457  40.389  1   49.395  ? 22  GLY   A O    1 ? 2 
ATOM   1946 H H    . GLY   B 1 10  ? 8.851  -8.232  41.356  1   57.183  ? 22  GLY   A H    1 c 2 
ATOM   1947 H HA2  . GLY   B 1 10  ? 9.242  -10.301 40.394  1   51.785  ? 22  GLY   A HA2  1 c 2 
ATOM   1948 H HA3  . GLY   B 1 10  ? 9.388  -9.604  38.972  1   50.686  ? 22  GLY   A HA3  1 c 2 
ATOM   1949 N N    . GLU   B 1 11  ? 11.726 -10.666 39.993  1   47.882  ? 23  GLU   A N    1 ? 2 
ATOM   1950 C CA   . GLU   B 1 11  ? 13.159 -10.842 40.139  1   45.933  ? 23  GLU   A CA   1 ? 2 
ATOM   1951 C C    . GLU   B 1 11  ? 13.823 -10.535 38.803  1   44.347  ? 23  GLU   A C    1 ? 2 
ATOM   1952 O O    . GLU   B 1 11  ? 13.371 -11.009 37.759  1   43.604  ? 23  GLU   A O    1 ? 2 
ATOM   1953 C CB   . GLU   B 1 11  ? 13.397 -12.307 40.537  1   51.807  ? 23  GLU   A CB   1 ? 2 
ATOM   1954 C CG   . GLU   B 1 11  ? 14.846 -12.685 40.865  1   60.667  ? 23  GLU   A CG   1 ? 2 
ATOM   1955 C CD   . GLU   B 1 11  ? 15.081 -14.204 40.895  1   61.47   ? 23  GLU   A CD   1 ? 2 
ATOM   1956 O OE1  . GLU   B 1 11  ? 14.152 -15.028 40.73   1   71.095  ? 23  GLU   A OE1  1 ? 2 
ATOM   1957 O OE2  . GLU   B 1 11  ? 16.241 -14.574 41.009  1   61.722  ? 23  GLU   A OE2  1 ? 2 
ATOM   1958 H H    . GLU   B 1 11  ? 11.213 -11.402 39.816  1   46.362  ? 23  GLU   A H    1 c 2 
ATOM   1959 H HA   . GLU   B 1 11  ? 13.497 -10.228 40.84   1   48.795  ? 23  GLU   A HA   1 c 2 
ATOM   1960 H HB2  . GLU   B 1 11  ? 12.837 -12.518 41.309  1   52.477  ? 23  GLU   A HB2  1 c 2 
ATOM   1961 H HB3  . GLU   B 1 11  ? 13.101 -12.875 39.796  1   50.643  ? 23  GLU   A HB3  1 c 2 
ATOM   1962 H HG2  . GLU   B 1 11  ? 15.444 -12.288 40.197  1   58.742  ? 23  GLU   A HG2  1 c 2 
ATOM   1963 H HG3  . GLU   B 1 11  ? 15.085 -12.313 41.741  1   60.519  ? 23  GLU   A HG3  1 c 2 
ATOM   1964 N N    . ASP   B 1 12  ? 14.893 -9.741  38.851  1   43.646  ? 24  ASP   A N    1 ? 2 
ATOM   1965 C CA   . ASP   B 1 12  ? 15.678 -9.433  37.677  1   48.364  ? 24  ASP   A CA   1 ? 2 
ATOM   1966 C C    . ASP   B 1 12  ? 16.586 -10.634 37.423  1   49.05   ? 24  ASP   A C    1 ? 2 
ATOM   1967 O O    . ASP   B 1 12  ? 17.459 -10.941 38.248  1   44.423  ? 24  ASP   A O    1 ? 2 
ATOM   1968 C CB   . ASP   B 1 12  ? 16.489 -8.179  37.907  1   48.205  ? 24  ASP   A CB   1 ? 2 
ATOM   1969 C CG   . ASP   B 1 12  ? 17.369 -7.786  36.738  1   49.977  ? 24  ASP   A CG   1 ? 2 
ATOM   1970 O OD1  . ASP   B 1 12  ? 17.35  -8.505  35.732  1   45.674  ? 24  ASP   A OD1  1 ? 2 
ATOM   1971 O OD2  . ASP   B 1 12  ? 18.052 -6.758  36.858  1   47.82   ? 24  ASP   A OD2  1 ? 2 
ATOM   1972 H H    . ASP   B 1 12  ? 15.142 -9.377  39.652  1   46.684  ? 24  ASP   A H    1 c 2 
ATOM   1973 H HA   . ASP   B 1 12  ? 15.075 -9.305  36.913  1   45.902  ? 24  ASP   A HA   1 c 2 
ATOM   1974 H HB2  . ASP   B 1 12  ? 15.878 -7.436  38.095  1   49.403  ? 24  ASP   A HB2  1 c 2 
ATOM   1975 H HB3  . ASP   B 1 12  ? 17.06  -8.308  38.693  1   50.355  ? 24  ASP   A HB3  1 c 2 
ATOM   1976 N N    . ILE   B 1 13  ? 16.326 -11.338 36.313  1   44.608  ? 25  ILE   A N    1 ? 2 
ATOM   1977 C CA   . ILE   B 1 13  ? 17.074 -12.547 35.994  1   48.431  ? 25  ILE   A CA   1 ? 2 
ATOM   1978 C C    . ILE   B 1 13  ? 18.085 -12.288 34.875  1   45.155  ? 25  ILE   A C    1 ? 2 
ATOM   1979 O O    . ILE   B 1 13  ? 18.696 -13.248 34.404  1   46.927  ? 25  ILE   A O    1 ? 2 
ATOM   1980 C CB   . ILE   B 1 13  ? 16.144 -13.715 35.649  1   46.244  ? 25  ILE   A CB   1 ? 2 
ATOM   1981 C CG1  . ILE   B 1 13  ? 15.213 -13.356 34.472  1   46.813  ? 25  ILE   A CG1  1 ? 2 
ATOM   1982 C CG2  . ILE   B 1 13  ? 15.356 -14.213 36.872  1   51.309  ? 25  ILE   A CG2  1 ? 2 
ATOM   1983 C CD1  . ILE   B 1 13  ? 14.509 -14.577 33.919  1   48.194  ? 25  ILE   A CD1  1 ? 2 
ATOM   1984 H H    . ILE   B 1 13  ? 15.677 -11.052 35.736  1   45.17   ? 25  ILE   A H    1 c 2 
ATOM   1985 H HA   . ILE   B 1 13  ? 17.577 -12.803 36.79   1   47.924  ? 25  ILE   A HA   1 c 2 
ATOM   1986 H HB   . ILE   B 1 13  ? 16.709 -14.455 35.351  1   48.055  ? 25  ILE   A HB   1 c 2 
ATOM   1987 H HG12 . ILE   B 1 13  ? 14.542 -12.712 34.778  1   46.445  ? 25  ILE   A HG12 1 c 2 
ATOM   1988 H HG13 . ILE   B 1 13  ? 15.737 -12.938 33.76   1   46.994  ? 25  ILE   A HG13 1 c 2 
ATOM   1989 H HG21 . ILE   B 1 13  ? 14.867 -15.02  36.64   1   49.222  ? 25  ILE   A HG21 1 c 2 
ATOM   1990 H HG22 . ILE   B 1 13  ? 14.729 -13.527 37.157  1   49.494  ? 25  ILE   A HG22 1 c 2 
ATOM   1991 H HG23 . ILE   B 1 13  ? 15.972 -14.409 37.598  1   50.982  ? 25  ILE   A HG23 1 c 2 
ATOM   1992 H HD11 . ILE   B 1 13  ? 15.164 -15.283 33.762  1   48.063  ? 25  ILE   A HD11 1 c 2 
ATOM   1993 H HD12 . ILE   B 1 13  ? 14.071 -14.348 33.078  1   46.825  ? 25  ILE   A HD12 1 c 2 
ATOM   1994 H HD13 . ILE   B 1 13  ? 13.841 -14.891 34.557  1   47.326  ? 25  ILE   A HD13 1 c 2 
ATOM   1995 N N    . THR   B 1 14  ? 18.339 -11.018 34.546  1   47.951  ? 26  THR   A N    1 ? 2 
ATOM   1996 C CA   . THR   B 1 14  ? 19.403 -10.653 33.606  1   51.706  ? 26  THR   A CA   1 ? 2 
ATOM   1997 C C    . THR   B 1 14  ? 20.768 -10.844 34.258  1   54.532  ? 26  THR   A C    1 ? 2 
ATOM   1998 O O    . THR   B 1 14  ? 20.908 -10.685 35.465  1   55.34   ? 26  THR   A O    1 ? 2 
ATOM   1999 C CB   . THR   B 1 14  ? 19.254 -9.222  33.075  1   49.257  ? 26  THR   A CB   1 ? 2 
ATOM   2000 O OG1  . THR   B 1 14  ? 19.421 -8.215  34.067  1   49.504  ? 26  THR   A OG1  1 ? 2 
ATOM   2001 C CG2  . THR   B 1 14  ? 17.886 -8.964  32.451  1   52.651  ? 26  THR   A CG2  1 ? 2 
ATOM   2002 H H    . THR   B 1 14  ? 17.84  -10.35  34.92   1   47.912  ? 26  THR   A H    1 c 2 
ATOM   2003 H HA   . THR   B 1 14  ? 19.343 -11.263 32.839  1   50.09   ? 26  THR   A HA   1 c 2 
ATOM   2004 H HB   . THR   B 1 14  ? 19.933 -9.084  32.372  1   51.315  ? 26  THR   A HB   1 c 2 
ATOM   2005 H HG1  . THR   B 1 14  ? 18.834 -8.369  34.663  0   30      ? 26  THR   A HG1  1 c 2 
ATOM   2006 H HG21 . THR   B 1 14  ? 17.867 -8.072  32.067  1   51.597  ? 26  THR   A HG21 1 c 2 
ATOM   2007 H HG22 . THR   B 1 14  ? 17.198 -9.038  33.132  1   50.252  ? 26  THR   A HG22 1 c 2 
ATOM   2008 H HG23 . THR   B 1 14  ? 17.72  -9.619  31.752  1   50.108  ? 26  THR   A HG23 1 c 2 
ATOM   2009 N N    . SER   B 1 15  ? 21.767 -11.168 33.433  1   59.782  ? 27  SER   A N    1 ? 2 
ATOM   2010 C CA   . SER   B 1 15  ? 23.152 -11.241 33.856  1   65.101  ? 27  SER   A CA   1 ? 2 
ATOM   2011 C C    . SER   B 1 15  ? 23.691 -9.863  34.205  1   64.025  ? 27  SER   A C    1 ? 2 
ATOM   2012 O O    . SER   B 1 15  ? 24.501 -9.723  35.136  1   59.511  ? 27  SER   A O    1 ? 2 
ATOM   2013 C CB   . SER   B 1 15  ? 23.99  -11.906 32.812  1   71.419  ? 27  SER   A CB   1 ? 2 
ATOM   2014 O OG   . SER   B 1 15  ? 23.868 -13.311 32.995  1   76.748  ? 27  SER   A OG   1 ? 2 
ATOM   2015 H H    . SER   B 1 15  ? 21.57  -11.351 32.559  1   58.623  ? 27  SER   A H    1 c 2 
ATOM   2016 H HA   . SER   B 1 15  ? 23.188 -11.796 34.677  1   65.196  ? 27  SER   A HA   1 c 2 
ATOM   2017 H HB2  . SER   B 1 15  ? 23.677 -11.655 31.922  1   70.5    ? 27  SER   A HB2  1 c 2 
ATOM   2018 H HB3  . SER   B 1 15  ? 24.923 -11.636 32.911  1   73.559  ? 27  SER   A HB3  1 c 2 
ATOM   2019 H HG   . SER   B 1 15  ? 24.224 -13.651 32.37   0   30      ? 27  SER   A HG   1 c 2 
ATOM   2020 N N    . LYS   B 1 16  ? 23.227 -8.88   33.451  1   56.274  ? 28  LYS   A N    1 ? 2 
ATOM   2021 C CA   . LYS   B 1 16  ? 23.704 -7.508  33.565  1   61.599  ? 28  LYS   A CA   1 ? 2 
ATOM   2022 C C    . LYS   B 1 16  ? 23.002 -6.761  34.701  1   57.519  ? 28  LYS   A C    1 ? 2 
ATOM   2023 O O    . LYS   B 1 16  ? 23.426 -5.674  35.049  1   63.75   ? 28  LYS   A O    1 ? 2 
ATOM   2024 C CB   . LYS   B 1 16  ? 23.48  -6.727  32.261  1   67.169  ? 28  LYS   A CB   1 ? 2 
ATOM   2025 C CG   . LYS   B 1 16  ? 24.409 -7.029  31.071  1   72.107  ? 28  LYS   A CG   1 ? 2 
ATOM   2026 C CD   . LYS   B 1 16  ? 24.307 -6.051  29.897  1   66.735  ? 28  LYS   A CD   1 ? 2 
ATOM   2027 H H    . LYS   B 1 16  ? 22.586 -9.064  32.827  1   57.034  ? 28  LYS   A H    1 c 2 
ATOM   2028 H HA   . LYS   B 1 16  ? 24.677 -7.531  33.756  1   63.319  ? 28  LYS   A HA   1 c 2 
ATOM   2029 H HB2  . LYS   B 1 16  ? 22.556 -6.884  31.969  1   64.363  ? 28  LYS   A HB2  1 c 2 
ATOM   2030 H HB3  . LYS   B 1 16  ? 23.559 -5.771  32.466  1   67.79   ? 28  LYS   A HB3  1 c 2 
ATOM   2031 H HG2  . LYS   B 1 16  ? 25.336 -7.036  31.397  1   71.972  ? 28  LYS   A HG2  1 c 2 
ATOM   2032 H HG3  . LYS   B 1 16  ? 24.205 -7.933  30.745  1   68.452  ? 28  LYS   A HG3  1 c 2 
ATOM   2033 H HD2  . LYS   B 1 16  ? 25.221 -6.077  29.733  0   30      ? 28  LYS   A HD2  1 c 2 
ATOM   2034 H HD3  . LYS   B 1 16  ? 23.368 -5.994  29.638  0   30      ? 28  LYS   A HD3  1 c 2 
ATOM   2035 N N    . LYS   B 1 17  ? 21.908 -7.308  35.236  1   54.597  ? 29  LYS   A N    1 ? 2 
ATOM   2036 C CA   . LYS   B 1 17  ? 21.14  -6.687  36.316  1   57.116  ? 29  LYS   A CA   1 ? 2 
ATOM   2037 C C    . LYS   B 1 17  ? 20.653 -5.286  35.911  1   56.208  ? 29  LYS   A C    1 ? 2 
ATOM   2038 O O    . LYS   B 1 17  ? 20.847 -4.29   36.595  1   56.537  ? 29  LYS   A O    1 ? 2 
ATOM   2039 C CB   . LYS   B 1 17  ? 21.923 -6.751  37.638  1   61.563  ? 29  LYS   A CB   1 ? 2 
ATOM   2040 C CG   . LYS   B 1 17  ? 22.151 -8.166  38.153  1   64.235  ? 29  LYS   A CG   1 ? 2 
ATOM   2041 C CD   . LYS   B 1 17  ? 20.836 -8.836  38.542  1   63.727  ? 29  LYS   A CD   1 ? 2 
ATOM   2042 C CE   . LYS   B 1 17  ? 20.99  -10.126 39.332  1   71.894  ? 29  LYS   A CE   1 ? 2 
ATOM   2043 N NZ   . LYS   B 1 17  ? 20.816 -11.246 38.403  1   71.67   ? 29  LYS   A NZ   1 ? 2 
ATOM   2044 H H    . LYS   B 1 17  ? 21.613 -8.107  34.907  1   53.79   ? 29  LYS   A H    1 c 2 
ATOM   2045 H HA   . LYS   B 1 17  ? 20.333 -7.241  36.447  1   54.872  ? 29  LYS   A HA   1 c 2 
ATOM   2046 H HB2  . LYS   B 1 17  ? 22.795 -6.319  37.516  1   63.868  ? 29  LYS   A HB2  1 c 2 
ATOM   2047 H HB3  . LYS   B 1 17  ? 21.432 -6.247  38.322  1   62.275  ? 29  LYS   A HB3  1 c 2 
ATOM   2048 H HG2  . LYS   B 1 17  ? 22.593 -8.695  37.454  1   63.54   ? 29  LYS   A HG2  1 c 2 
ATOM   2049 H HG3  . LYS   B 1 17  ? 22.743 -8.13   38.936  1   65.959  ? 29  LYS   A HG3  1 c 2 
ATOM   2050 H HD2  . LYS   B 1 17  ? 20.308 -8.202  39.074  1   65.196  ? 29  LYS   A HD2  1 c 2 
ATOM   2051 H HD3  . LYS   B 1 17  ? 20.328 -9.026  37.723  1   63.106  ? 29  LYS   A HD3  1 c 2 
ATOM   2052 H HE2  . LYS   B 1 17  ? 21.874 -10.175 39.739  1   72.234  ? 29  LYS   A HE2  1 c 2 
ATOM   2053 H HE3  . LYS   B 1 17  ? 20.315 -10.176 40.032  1   69.989  ? 29  LYS   A HE3  1 c 2 
ATOM   2054 H HZ1  . LYS   B 1 17  ? 21.378 -11.154 37.698  1   71.329  ? 29  LYS   A HZ1  1 c 2 
ATOM   2055 H HZ2  . LYS   B 1 17  ? 19.961 -11.268 38.103  1   69.334  ? 29  LYS   A HZ2  1 c 2 
ATOM   2056 H HZ3  . LYS   B 1 17  ? 20.999 -12.025 38.827  1   71.517  ? 29  LYS   A HZ3  1 c 2 
ATOM   2057 N N    . ASP   B 1 18  ? 19.942 -5.218  34.802  1   59.927  ? 30  ASP   A N    1 ? 2 
ATOM   2058 C CA   . ASP   B 1 18  ? 19.419 -3.96   34.279  1   59.708  ? 30  ASP   A CA   1 ? 2 
ATOM   2059 C C    . ASP   B 1 18  ? 17.892 -3.91   34.35   1   67.165  ? 30  ASP   A C    1 ? 2 
ATOM   2060 O O    . ASP   B 1 18  ? 17.27  -3.105  33.655  1   61.772  ? 30  ASP   A O    1 ? 2 
ATOM   2061 C CB   . ASP   B 1 18  ? 19.864 -3.757  32.835  1   66.434  ? 30  ASP   A CB   1 ? 2 
ATOM   2062 C CG   . ASP   B 1 18  ? 19.478 -4.851  31.848  1   57.899  ? 30  ASP   A CG   1 ? 2 
ATOM   2063 O OD1  . ASP   B 1 18  ? 18.544 -5.634  32.135  1   57.472  ? 30  ASP   A OD1  1 ? 2 
ATOM   2064 O OD2  . ASP   B 1 18  ? 20.201 -4.974  30.845  1   56.278  ? 30  ASP   A OD2  1 ? 2 
ATOM   2065 H H    . ASP   B 1 18  ? 19.762 -5.989  34.345  1   56.66   ? 30  ASP   A H    1 c 2 
ATOM   2066 H HA   . ASP   B 1 18  ? 19.783 -3.219  34.815  1   64.634  ? 30  ASP   A HA   1 c 2 
ATOM   2067 H HB2  . ASP   B 1 18  ? 19.501 -2.909  32.506  1   64.225  ? 30  ASP   A HB2  1 c 2 
ATOM   2068 H HB3  . ASP   B 1 18  ? 20.841 -3.682  32.827  1   65.105  ? 30  ASP   A HB3  1 c 2 
ATOM   2069 N N    . ARG   B 1 19  ? 17.297 -4.819  35.145  1   57.045  ? 31  ARG   A N    1 ? 2 
ATOM   2070 C CA   . ARG   B 1 19  ? 15.861 -4.921  35.34   1   52.784  ? 31  ARG   A CA   1 ? 2 
ATOM   2071 C C    . ARG   B 1 19  ? 15.117 -5.053  34.012  1   51.446  ? 31  ARG   A C    1 ? 2 
ATOM   2072 O O    . ARG   B 1 19  ? 13.958 -4.653  33.926  1   55.433  ? 31  ARG   A O    1 ? 2 
ATOM   2073 C CB   . ARG   B 1 19  ? 15.255 -3.837  36.235  1   53.871  ? 31  ARG   A CB   1 ? 2 
ATOM   2074 C CG   . ARG   B 1 19  ? 16.026 -3.486  37.496  1   63.068  ? 31  ARG   A CG   1 ? 2 
ATOM   2075 C CD   . ARG   B 1 19  ? 15.187 -2.619  38.443  1   66.619  ? 31  ARG   A CD   1 ? 2 
ATOM   2076 N NE   . ARG   B 1 19  ? 14.389 -3.447  39.347  1   72.414  ? 31  ARG   A NE   1 ? 2 
ATOM   2077 C CZ   . ARG   B 1 19  ? 13.144 -3.877  39.19   1   78.731  ? 31  ARG   A CZ   1 ? 2 
ATOM   2078 N NH1  . ARG   B 1 19  ? 12.461 -3.505  38.127  1   81.846  ? 31  ARG   A NH1  1 ? 2 
ATOM   2079 N NH2  . ARG   B 1 19  ? 12.614 -4.72   40.072  1   80.129  ? 31  ARG   A NH2  1 ? 2 
ATOM   2080 H H    . ARG   B 1 19  ? 17.829 -5.406  35.598  1   58.227  ? 31  ARG   A H    1 c 2 
ATOM   2081 H HA   . ARG   B 1 19  ? 15.704 -5.767  35.83   1   52.226  ? 31  ARG   A HA   1 c 2 
ATOM   2082 H HB2  . ARG   B 1 19  ? 15.155 -3.021  35.7    1   56.412  ? 31  ARG   A HB2  1 c 2 
ATOM   2083 H HB3  . ARG   B 1 19  ? 14.356 -4.126  36.496  1   54.701  ? 31  ARG   A HB3  1 c 2 
ATOM   2084 H HG2  . ARG   B 1 19  ? 16.285 -4.313  37.959  1   61.14   ? 31  ARG   A HG2  1 c 2 
ATOM   2085 H HG3  . ARG   B 1 19  ? 16.844 -3      37.253  1   63.24   ? 31  ARG   A HG3  1 c 2 
ATOM   2086 H HD2  . ARG   B 1 19  ? 15.784 -2.05   38.971  1   70.05   ? 31  ARG   A HD2  1 c 2 
ATOM   2087 H HD3  . ARG   B 1 19  ? 14.598 -2.036  37.924  1   67.953  ? 31  ARG   A HD3  1 c 2 
ATOM   2088 H HE   . ARG   B 1 19  ? 14.78  -3.692  40.087  1   73.376  ? 31  ARG   A HE   1 c 2 
ATOM   2089 H HH11 . ARG   B 1 19  ? 12.704 -2.803  37.651  1   80.693  ? 31  ARG   A HH11 1 c 2 
ATOM   2090 H HH12 . ARG   B 1 19  ? 11.753 -3.975  37.9    1   78.521  ? 31  ARG   A HH12 1 c 2 
ATOM   2091 H HH21 . ARG   B 1 19  ? 13.136 -5.15   40.643  1   79.743  ? 31  ARG   A HH21 1 c 2 
ATOM   2092 H HH22 . ARG   B 1 19  ? 11.74  -4.849  40.085  1   78.948  ? 31  ARG   A HH22 1 c 2 
ATOM   2093 N N    . GLY   B 1 20  ? 15.755 -5.695  33.022  1   50.972  ? 32  GLY   A N    1 ? 2 
ATOM   2094 C CA   . GLY   B 1 20  ? 15.195 -5.812  31.701  1   48.397  ? 32  GLY   A CA   1 ? 2 
ATOM   2095 C C    . GLY   B 1 20  ? 14.332 -7.036  31.477  1   48.689  ? 32  GLY   A C    1 ? 2 
ATOM   2096 O O    . GLY   B 1 20  ? 13.557 -7.096  30.496  1   48.897  ? 32  GLY   A O    1 ? 2 
ATOM   2097 H H    . GLY   B 1 20  ? 16.565 -6.084  33.188  1   51.021  ? 32  GLY   A H    1 c 2 
ATOM   2098 H HA2  . GLY   B 1 20  ? 14.658 -5.005  31.514  1   49.902  ? 32  GLY   A HA2  1 c 2 
ATOM   2099 H HA3  . GLY   B 1 20  ? 15.936 -5.825  31.051  1   49.811  ? 32  GLY   A HA3  1 c 2 
ATOM   2100 N N    . VAL   B 1 21  ? 14.53  -8.065  32.32   1   47.12   ? 33  VAL   A N    1 ? 2 
ATOM   2101 C CA   . VAL   B 1 21  ? 13.741 -9.272  32.272  1   45.157  ? 33  VAL   A CA   1 ? 2 
ATOM   2102 C C    . VAL   B 1 21  ? 13.406 -9.537  33.732  1   49.139  ? 33  VAL   A C    1 ? 2 
ATOM   2103 O O    . VAL   B 1 21  ? 14.348 -9.756  34.493  1   39.342  ? 33  VAL   A O    1 ? 2 
ATOM   2104 C CB   . VAL   B 1 21  ? 14.365 -10.536 31.654  1   47.279  ? 33  VAL   A CB   1 ? 2 
ATOM   2105 C CG1  . VAL   B 1 21  ? 13.395 -11.723 31.622  1   49.494  ? 33  VAL   A CG1  1 ? 2 
ATOM   2106 C CG2  . VAL   B 1 21  ? 14.913 -10.319 30.279  1   50.051  ? 33  VAL   A CG2  1 ? 2 
ATOM   2107 H H    . VAL   B 1 21  ? 15.194 -8.005  32.944  1   48.112  ? 33  VAL   A H    1 c 2 
ATOM   2108 H HA   . VAL   B 1 21  ? 12.913 -9.078  31.795  1   45.898  ? 33  VAL   A HA   1 c 2 
ATOM   2109 H HB   . VAL   B 1 21  ? 15.122 -10.793 32.231  1   48.393  ? 33  VAL   A HB   1 c 2 
ATOM   2110 H HG11 . VAL   B 1 21  ? 12.579 -11.463 31.162  1   47.999  ? 33  VAL   A HG11 1 c 2 
ATOM   2111 H HG12 . VAL   B 1 21  ? 13.181 -11.995 32.53   1   48.444  ? 33  VAL   A HG12 1 c 2 
ATOM   2112 H HG13 . VAL   B 1 21  ? 13.807 -12.467 31.153  1   48.464  ? 33  VAL   A HG13 1 c 2 
ATOM   2113 H HG21 . VAL   B 1 21  ? 15.316 -11.142 29.955  1   49.303  ? 33  VAL   A HG21 1 c 2 
ATOM   2114 H HG22 . VAL   B 1 21  ? 15.587 -9.619  30.305  1   50.344  ? 33  VAL   A HG22 1 c 2 
ATOM   2115 H HG23 . VAL   B 1 21  ? 14.195 -10.053 29.681  1   48.893  ? 33  VAL   A HG23 1 c 2 
ATOM   2116 N N    . LEU   B 1 22  ? 12.109 -9.419  34.069  1   48.041  ? 34  LEU   A N    1 ? 2 
ATOM   2117 C CA   . LEU   B 1 22  ? 11.585 -9.557  35.407  1   48.391  ? 34  LEU   A CA   1 ? 2 
ATOM   2118 C C    . LEU   B 1 22  ? 10.64  -10.743 35.472  1   45.379  ? 34  LEU   A C    1 ? 2 
ATOM   2119 O O    . LEU   B 1 22  ? 9.704  -10.87  34.681  1   44.795  ? 34  LEU   A O    1 ? 2 
ATOM   2120 C CB   . LEU   B 1 22  ? 10.844 -8.303  35.846  1   50.771  ? 34  LEU   A CB   1 ? 2 
ATOM   2121 C CG   . LEU   B 1 22  ? 11.691 -7.03   35.898  1   60.372  ? 34  LEU   A CG   1 ? 2 
ATOM   2122 C CD1  . LEU   B 1 22  ? 10.81  -5.857  36.27   1   59.365  ? 34  LEU   A CD1  1 ? 2 
ATOM   2123 C CD2  . LEU   B 1 22  ? 12.886 -7.154  36.849  1   56.426  ? 34  LEU   A CD2  1 ? 2 
ATOM   2124 H H    . LEU   B 1 22  ? 11.512 -9.24   33.4    1   47.692  ? 34  LEU   A H    1 c 2 
ATOM   2125 H HA   . LEU   B 1 22  ? 12.341 -9.718  36.022  1   48.82   ? 34  LEU   A HA   1 c 2 
ATOM   2126 H HB2  . LEU   B 1 22  ? 10.095 -8.155  35.224  1   51.701  ? 34  LEU   A HB2  1 c 2 
ATOM   2127 H HB3  . LEU   B 1 22  ? 10.468 -8.465  36.742  1   52.603  ? 34  LEU   A HB3  1 c 2 
ATOM   2128 H HG   . LEU   B 1 22  ? 12.047 -6.863  34.988  1   57.05   ? 34  LEU   A HG   1 c 2 
ATOM   2129 H HD11 . LEU   B 1 22  ? 10.002 -5.872  35.73   1   59.455  ? 34  LEU   A HD11 1 c 2 
ATOM   2130 H HD12 . LEU   B 1 22  ? 11.29  -5.028  36.106  1   61.382  ? 34  LEU   A HD12 1 c 2 
ATOM   2131 H HD13 . LEU   B 1 22  ? 10.572 -5.913  37.211  1   60.874  ? 34  LEU   A HD13 1 c 2 
ATOM   2132 H HD21 . LEU   B 1 22  ? 13.54  -7.765  36.471  1   57.075  ? 34  LEU   A HD21 1 c 2 
ATOM   2133 H HD22 . LEU   B 1 22  ? 12.585 -7.494  37.709  1   58.096  ? 34  LEU   A HD22 1 c 2 
ATOM   2134 H HD23 . LEU   B 1 22  ? 13.295 -6.281  36.972  1   59.24   ? 34  LEU   A HD23 1 c 2 
ATOM   2135 N N    . LYS   B 1 23  ? 10.854 -11.592 36.497  1   46.17   ? 35  LYS   A N    1 ? 2 
ATOM   2136 C CA   . LYS   B 1 23  ? 10.152 -12.85  36.601  1   39.4    ? 35  LYS   A CA   1 ? 2 
ATOM   2137 C C    . LYS   B 1 23  ? 9.448  -12.959 37.955  1   41.826  ? 35  LYS   A C    1 ? 2 
ATOM   2138 O O    . LYS   B 1 23  ? 10.078 -12.625 38.977  1   39.076  ? 35  LYS   A O    1 ? 2 
ATOM   2139 C CB   . LYS   B 1 23  ? 11.167 -13.994 36.459  1   41.931  ? 35  LYS   A CB   1 ? 2 
ATOM   2140 C CG   . LYS   B 1 23  ? 10.591 -15.377 36.583  1   39.922  ? 35  LYS   A CG   1 ? 2 
ATOM   2141 C CD   . LYS   B 1 23  ? 11.611 -16.492 36.833  1   41.733  ? 35  LYS   A CD   1 ? 2 
ATOM   2142 C CE   . LYS   B 1 23  ? 10.94  -17.815 36.818  1   42.264  ? 35  LYS   A CE   1 ? 2 
ATOM   2143 N NZ   . LYS   B 1 23  ? 11.759 -18.952 37.229  1   45.68   ? 35  LYS   A NZ   1 ? 2 
ATOM   2144 H H    . LYS   B 1 23  ? 11.455 -11.37  37.149  1   45.402  ? 35  LYS   A H    1 c 2 
ATOM   2145 H HA   . LYS   B 1 23  ? 9.484  -12.906 35.876  1   40.603  ? 35  LYS   A HA   1 c 2 
ATOM   2146 H HB2  . LYS   B 1 23  ? 11.603 -13.919 35.583  1   40.413  ? 35  LYS   A HB2  1 c 2 
ATOM   2147 H HB3  . LYS   B 1 23  ? 11.859 -13.885 37.145  1   41.672  ? 35  LYS   A HB3  1 c 2 
ATOM   2148 H HG2  . LYS   B 1 23  ? 9.941  -15.38  37.317  1   41.029  ? 35  LYS   A HG2  1 c 2 
ATOM   2149 H HG3  . LYS   B 1 23  ? 10.1   -15.581 35.757  1   39.963  ? 35  LYS   A HG3  1 c 2 
ATOM   2150 H HD2  . LYS   B 1 23  ? 12.301 -16.468 36.135  1   41.349  ? 35  LYS   A HD2  1 c 2 
ATOM   2151 H HD3  . LYS   B 1 23  ? 12.041 -16.354 37.705  1   42.392  ? 35  LYS   A HD3  1 c 2 
ATOM   2152 H HE2  . LYS   B 1 23  ? 10.162 -17.773 37.402  1   42.916  ? 35  LYS   A HE2  1 c 2 
ATOM   2153 H HE3  . LYS   B 1 23  ? 10.615 -17.985 35.915  1   42.088  ? 35  LYS   A HE3  1 c 2 
ATOM   2154 H HZ1  . LYS   B 1 23  ? 12.086 -18.808 38.062  1   45.763  ? 35  LYS   A HZ1  1 c 2 
ATOM   2155 H HZ2  . LYS   B 1 23  ? 12.45  -19.056 36.653  1   45.031  ? 35  LYS   A HZ2  1 c 2 
ATOM   2156 H HZ3  . LYS   B 1 23  ? 11.257 -19.706 37.232  1   45.455  ? 35  LYS   A HZ3  1 c 2 
ATOM   2157 N N    . ILE   B 1 24  ? 8.202  -13.493 37.906  1   37.238  ? 36  ILE   A N    1 ? 2 
ATOM   2158 C CA   . ILE   B 1 24  ? 7.479  -14.009 39.042  1   42.715  ? 36  ILE   A CA   1 ? 2 
ATOM   2159 C C    . ILE   B 1 24  ? 7.076  -15.445 38.753  1   42.123  ? 36  ILE   A C    1 ? 2 
ATOM   2160 O O    . ILE   B 1 24  ? 6.52   -15.735 37.695  1   44.988  ? 36  ILE   A O    1 ? 2 
ATOM   2161 C CB   . ILE   B 1 24  ? 6.221  -13.174 39.376  1   44.891  ? 36  ILE   A CB   1 ? 2 
ATOM   2162 C CG1  . ILE   B 1 24  ? 6.56   -11.696 39.557  1   47.305  ? 36  ILE   A CG1  1 ? 2 
ATOM   2163 C CG2  . ILE   B 1 24  ? 5.512  -13.765 40.616  1   45.968  ? 36  ILE   A CG2  1 ? 2 
ATOM   2164 C CD1  . ILE   B 1 24  ? 5.327  -10.806 39.48   1   56.536  ? 36  ILE   A CD1  1 ? 2 
ATOM   2165 H H    . ILE   B 1 24  ? 7.786  -13.526 37.093  1   38.549  ? 36  ILE   A H    1 c 2 
ATOM   2166 H HA   . ILE   B 1 24  ? 8.071  -13.999 39.819  1   42.817  ? 36  ILE   A HA   1 c 2 
ATOM   2167 H HB   . ILE   B 1 24  ? 5.607  -13.246 38.618  1   44.281  ? 36  ILE   A HB   1 c 2 
ATOM   2168 H HG12 . ILE   B 1 24  ? 6.99   -11.572 40.428  1   49.563  ? 36  ILE   A HG12 1 c 2 
ATOM   2169 H HG13 . ILE   B 1 24  ? 7.193  -11.423 38.863  1   47.663  ? 36  ILE   A HG13 1 c 2 
ATOM   2170 H HG21 . ILE   B 1 24  ? 4.787  -13.179 40.89   1   47.107  ? 36  ILE   A HG21 1 c 2 
ATOM   2171 H HG22 . ILE   B 1 24  ? 6.149  -13.85  41.346  1   46.826  ? 36  ILE   A HG22 1 c 2 
ATOM   2172 H HG23 . ILE   B 1 24  ? 5.151  -14.641 40.401  1   45.971  ? 36  ILE   A HG23 1 c 2 
ATOM   2173 H HD11 . ILE   B 1 24  ? 4.869  -10.953 38.631  1   53.077  ? 36  ILE   A HD11 1 c 2 
ATOM   2174 H HD12 . ILE   B 1 24  ? 5.602  -9.872  39.542  1   54.503  ? 36  ILE   A HD12 1 c 2 
ATOM   2175 H HD13 . ILE   B 1 24  ? 4.719  -11.013 40.215  1   54.903  ? 36  ILE   A HD13 1 c 2 
ATOM   2176 N N    . VAL   B 1 25  ? 7.345  -16.333 39.722  1   43.856  ? 37  VAL   A N    1 ? 2 
ATOM   2177 C CA   . VAL   B 1 25  ? 6.84   -17.691 39.713  1   42.639  ? 37  VAL   A CA   1 ? 2 
ATOM   2178 C C    . VAL   B 1 25  ? 5.399  -17.661 40.199  1   44.497  ? 37  VAL   A C    1 ? 2 
ATOM   2179 O O    . VAL   B 1 25  ? 5.133  -17.167 41.286  1   45.911  ? 37  VAL   A O    1 ? 2 
ATOM   2180 C CB   . VAL   B 1 25  ? 7.74   -18.52  40.653  1   44.261  ? 37  VAL   A CB   1 ? 2 
ATOM   2181 C CG1  . VAL   B 1 25  ? 7.217  -19.916 40.858  1   47.651  ? 37  VAL   A CG1  1 ? 2 
ATOM   2182 C CG2  . VAL   B 1 25  ? 9.176  -18.59  40.135  1   46.286  ? 37  VAL   A CG2  1 ? 2 
ATOM   2183 H H    . VAL   B 1 25  ? 7.869  -16.07  40.424  1   43.955  ? 37  VAL   A H    1 c 2 
ATOM   2184 H HA   . VAL   B 1 25  ? 6.882  -18.053 38.807  1   42.446  ? 37  VAL   A HA   1 c 2 
ATOM   2185 H HB   . VAL   B 1 25  ? 7.75   -18.066 41.528  1   45.903  ? 37  VAL   A HB   1 c 2 
ATOM   2186 H HG11 . VAL   B 1 25  ? 7.048  -20.33  39.995  1   46.437  ? 37  VAL   A HG11 1 c 2 
ATOM   2187 H HG12 . VAL   B 1 25  ? 6.39   -19.883 41.367  1   47.866  ? 37  VAL   A HG12 1 c 2 
ATOM   2188 H HG13 . VAL   B 1 25  ? 7.874  -20.441 41.345  1   47.991  ? 37  VAL   A HG13 1 c 2 
ATOM   2189 H HG21 . VAL   B 1 25  ? 9.705  -19.157 40.721  1   46.598  ? 37  VAL   A HG21 1 c 2 
ATOM   2190 H HG22 . VAL   B 1 25  ? 9.56   -17.698 40.117  1   44.97   ? 37  VAL   A HG22 1 c 2 
ATOM   2191 H HG23 . VAL   B 1 25  ? 9.18   -18.962 39.237  1   44.76   ? 37  VAL   A HG23 1 c 2 
ATOM   2192 N N    . LYS   B 1 26  ? 4.46   -18.15  39.378  1   44.68   ? 38  LYS   A N    1 ? 2 
ATOM   2193 C CA   . LYS   B 1 26  ? 3.053  -18.122 39.744  1   45.681  ? 38  LYS   A CA   1 ? 2 
ATOM   2194 C C    . LYS   B 1 26  ? 2.571  -19.479 40.256  1   49.971  ? 38  LYS   A C    1 ? 2 
ATOM   2195 O O    . LYS   B 1 26  ? 1.742  -19.524 41.147  1   48.631  ? 38  LYS   A O    1 ? 2 
ATOM   2196 C CB   . LYS   B 1 26  ? 2.21   -17.626 38.57   1   46.28   ? 38  LYS   A CB   1 ? 2 
ATOM   2197 C CG   . LYS   B 1 26  ? 2.509  -16.229 38.205  1   43.83   ? 38  LYS   A CG   1 ? 2 
ATOM   2198 C CD   . LYS   B 1 26  ? 2.389  -15.2   39.318  1   44.843  ? 38  LYS   A CD   1 ? 2 
ATOM   2199 C CE   . LYS   B 1 26  ? 1.023  -15.068 39.816  1   47.502  ? 38  LYS   A CE   1 ? 2 
ATOM   2200 N NZ   . LYS   B 1 26  ? 0.943  -13.74  40.41   1   51.782  ? 38  LYS   A NZ   1 ? 2 
ATOM   2201 H H    . LYS   B 1 26  ? 4.702  -18.502 38.57   1   43.792  ? 38  LYS   A H    1 c 2 
ATOM   2202 H HA   . LYS   B 1 26  ? 2.942  -17.476 40.483  1   47.039  ? 38  LYS   A HA   1 c 2 
ATOM   2203 H HB2  . LYS   B 1 26  ? 2.364  -18.2   37.79   1   45.117  ? 38  LYS   A HB2  1 c 2 
ATOM   2204 H HB3  . LYS   B 1 26  ? 1.268  -17.694 38.819  1   46.905  ? 38  LYS   A HB3  1 c 2 
ATOM   2205 H HG2  . LYS   B 1 26  ? 3.424  -16.196 37.848  1   43.024  ? 38  LYS   A HG2  1 c 2 
ATOM   2206 H HG3  . LYS   B 1 26  ? 1.906  -15.972 37.476  1   44.024  ? 38  LYS   A HG3  1 c 2 
ATOM   2207 H HD2  . LYS   B 1 26  ? 2.979  -15.448 40.061  1   45.394  ? 38  LYS   A HD2  1 c 2 
ATOM   2208 H HD3  . LYS   B 1 26  ? 2.691  -14.331 38.974  1   44.423  ? 38  LYS   A HD3  1 c 2 
ATOM   2209 H HE2  . LYS   B 1 26  ? 0.381  -15.138 39.087  1   48.019  ? 38  LYS   A HE2  1 c 2 
ATOM   2210 H HE3  . LYS   B 1 26  ? 0.829  -15.746 40.487  1   49.175  ? 38  LYS   A HE3  1 c 2 
ATOM   2211 H HZ1  . LYS   B 1 26  ? 0.976  -13.106 39.763  1   49.97   ? 38  LYS   A HZ1  1 c 2 
ATOM   2212 H HZ2  . LYS   B 1 26  ? 1.63   -13.615 40.989  1   50.68   ? 38  LYS   A HZ2  1 c 2 
ATOM   2213 H HZ3  . LYS   B 1 26  ? 0.161  -13.659 40.861  1   52.215  ? 38  LYS   A HZ3  1 c 2 
ATOM   2214 N N    . ARG   B 1 27  ? 3.081  -20.564 39.669  1   49.765  ? 39  ARG   A N    1 ? 2 
ATOM   2215 C CA   . ARG   B 1 27  ? 2.834  -21.892 40.173  1   50.521  ? 39  ARG   A CA   1 ? 2 
ATOM   2216 C C    . ARG   B 1 27  ? 4.179  -22.594 40.197  1   51.218  ? 39  ARG   A C    1 ? 2 
ATOM   2217 O O    . ARG   B 1 27  ? 4.88   -22.632 39.187  1   52.309  ? 39  ARG   A O    1 ? 2 
ATOM   2218 C CB   . ARG   B 1 27  ? 1.771  -22.663 39.374  1   55.052  ? 39  ARG   A CB   1 ? 2 
ATOM   2219 C CG   . ARG   B 1 27  ? 1.402  -24.011 40.002  1   58.795  ? 39  ARG   A CG   1 ? 2 
ATOM   2220 C CD   . ARG   B 1 27  ? 0.535  -24.892 39.106  1   61.767  ? 39  ARG   A CD   1 ? 2 
ATOM   2221 N NE   . ARG   B 1 27  ? 1.257  -25.333 37.903  1   62.164  ? 39  ARG   A NE   1 ? 2 
ATOM   2222 C CZ   . ARG   B 1 27  ? 0.68   -25.718 36.762  1   61.021  ? 39  ARG   A CZ   1 ? 2 
ATOM   2223 N NH1  . ARG   B 1 27  ? -0.626 -25.594 36.624  1   60.313  ? 39  ARG   A NH1  1 ? 2 
ATOM   2224 N NH2  . ARG   B 1 27  ? 1.38   -26.221 35.754  1   61.195  ? 39  ARG   A NH2  1 ? 2 
ATOM   2225 H H    . ARG   B 1 27  ? 3.59   -20.469 38.916  1   48.167  ? 39  ARG   A H    1 c 2 
ATOM   2226 H HA   . ARG   B 1 27  ? 2.51   -21.813 41.106  1   52.839  ? 39  ARG   A HA   1 c 2 
ATOM   2227 H HB2  . ARG   B 1 27  ? 0.963  -22.112 39.306  1   54.516  ? 39  ARG   A HB2  1 c 2 
ATOM   2228 H HB3  . ARG   B 1 27  ? 2.107  -22.816 38.465  1   53.465  ? 39  ARG   A HB3  1 c 2 
ATOM   2229 H HG2  . ARG   B 1 27  ? 2.224  -24.5   40.222  1   59.103  ? 39  ARG   A HG2  1 c 2 
ATOM   2230 H HG3  . ARG   B 1 27  ? 0.922  -23.849 40.844  1   60.141  ? 39  ARG   A HG3  1 c 2 
ATOM   2231 H HD2  . ARG   B 1 27  ? 0.241  -25.677 39.612  1   63.918  ? 39  ARG   A HD2  1 c 2 
ATOM   2232 H HD3  . ARG   B 1 27  ? -0.261 -24.388 38.841  1   61.638  ? 39  ARG   A HD3  1 c 2 
ATOM   2233 H HE   . ARG   B 1 27  ? 2.127  -25.345 37.934  1   60.59   ? 39  ARG   A HE   1 c 2 
ATOM   2234 H HH11 . ARG   B 1 27  ? -1.168 -25.885 37.261  1   62.613  ? 39  ARG   A HH11 1 c 2 
ATOM   2235 H HH12 . ARG   B 1 27  ? -0.959 -25.231 35.89   1   60.317  ? 39  ARG   A HH12 1 c 2 
ATOM   2236 H HH21 . ARG   B 1 27  ? 2.263  -26.213 35.784  1   60.178  ? 39  ARG   A HH21 1 c 2 
ATOM   2237 H HH22 . ARG   B 1 27  ? 0.96   -26.562 35.054  1   61.801  ? 39  ARG   A HH22 1 c 2 
ATOM   2238 N N    . VAL   B 1 28  ? 4.544  -23.139 41.362  1   56.307  ? 40  VAL   A N    1 ? 2 
ATOM   2239 C CA   . VAL   B 1 28  ? 5.832  -23.779 41.543  1   59.187  ? 40  VAL   A CA   1 ? 2 
ATOM   2240 C C    . VAL   B 1 28  ? 5.804  -25.152 40.879  1   59.671  ? 40  VAL   A C    1 ? 2 
ATOM   2241 O O    . VAL   B 1 28  ? 4.809  -25.863 40.985  1   60.2    ? 40  VAL   A O    1 ? 2 
ATOM   2242 C CB   . VAL   B 1 28  ? 6.187  -23.869 43.037  1   64.572  ? 40  VAL   A CB   1 ? 2 
ATOM   2243 C CG1  . VAL   B 1 28  ? 7.5    -24.597 43.272  1   67.566  ? 40  VAL   A CG1  1 ? 2 
ATOM   2244 C CG2  . VAL   B 1 28  ? 6.24   -22.483 43.672  1   65.746  ? 40  VAL   A CG2  1 ? 2 
ATOM   2245 H H    . VAL   B 1 28  ? 3.963  -23.117 42.068  1   57.323  ? 40  VAL   A H    1 c 2 
ATOM   2246 H HA   . VAL   B 1 28  ? 6.509  -23.232 41.1    1   57.596  ? 40  VAL   A HA   1 c 2 
ATOM   2247 H HB   . VAL   B 1 28  ? 5.47   -24.381 43.479  1   66.325  ? 40  VAL   A HB   1 c 2 
ATOM   2248 H HG11 . VAL   B 1 28  ? 8.199  -24.19  42.734  1   65.599  ? 40  VAL   A HG11 1 c 2 
ATOM   2249 H HG12 . VAL   B 1 28  ? 7.405  -25.531 43.025  1   68.15   ? 40  VAL   A HG12 1 c 2 
ATOM   2250 H HG13 . VAL   B 1 28  ? 7.741  -24.537 44.212  1   68.279  ? 40  VAL   A HG13 1 c 2 
ATOM   2251 H HG21 . VAL   B 1 28  ? 6.546  -22.558 44.591  1   66.532  ? 40  VAL   A HG21 1 c 2 
ATOM   2252 H HG22 . VAL   B 1 28  ? 5.353  -22.085 43.659  1   64.893  ? 40  VAL   A HG22 1 c 2 
ATOM   2253 H HG23 . VAL   B 1 28  ? 6.854  -21.92  43.172  1   63.493  ? 40  VAL   A HG23 1 c 2 
ATOM   2254 N N    . GLY   B 1 29  ? 6.92   -25.49  40.21   1   59.185  ? 41  GLY   A N    1 ? 2 
ATOM   2255 C CA   . GLY   B 1 29  ? 7.114  -26.76  39.538  1   59.6    ? 41  GLY   A CA   1 ? 2 
ATOM   2256 C C    . GLY   B 1 29  ? 7.667  -27.778 40.531  1   65.088  ? 41  GLY   A C    1 ? 2 
ATOM   2257 O O    . GLY   B 1 29  ? 7.409  -27.645 41.718  1   65.418  ? 41  GLY   A O    1 ? 2 
ATOM   2258 H H    . GLY   B 1 29  ? 7.602  -24.882 40.176  1   57.707  ? 41  GLY   A H    1 c 2 
ATOM   2259 H HA2  . GLY   B 1 29  ? 6.254  -27.076 39.172  1   60.955  ? 41  GLY   A HA2  1 c 2 
ATOM   2260 H HA3  . GLY   B 1 29  ? 7.745  -26.641 38.791  1   59.431  ? 41  GLY   A HA3  1 c 2 
ATOM   2261 N N    . ASN   B 1 30  ? 8.412  -28.775 40.041  1   69.151  ? 42  ASN   A N    1 ? 2 
ATOM   2262 C CA   . ASN   B 1 30  ? 8.98   -29.829 40.88   1   73.805  ? 42  ASN   A CA   1 ? 2 
ATOM   2263 C C    . ASN   B 1 30  ? 10.277 -30.305 40.234  1   75.234  ? 42  ASN   A C    1 ? 2 
ATOM   2264 O O    . ASN   B 1 30  ? 10.541 -29.998 39.075  1   66.124  ? 42  ASN   A O    1 ? 2 
ATOM   2265 C CB   . ASN   B 1 30  ? 8.018  -31.002 41.016  1   80.949  ? 42  ASN   A CB   1 ? 2 
ATOM   2266 C CG   . ASN   B 1 30  ? 7.39   -31.306 39.681  1   88.097  ? 42  ASN   A CG   1 ? 2 
ATOM   2267 O OD1  . ASN   B 1 30  ? 6.205  -31.024 39.487  1   99.358  ? 42  ASN   A OD1  1 ? 2 
ATOM   2268 N ND2  . ASN   B 1 30  ? 8.188  -31.763 38.727  1   91.511  ? 42  ASN   A ND2  1 ? 2 
ATOM   2269 H H    . ASN   B 1 30  ? 8.578  -28.798 39.142  1   68.076  ? 42  ASN   A H    1 c 2 
ATOM   2270 H HA   . ASN   B 1 30  ? 9.165  -29.473 41.777  1   74.671  ? 42  ASN   A HA   1 c 2 
ATOM   2271 H HB2  . ASN   B 1 30  ? 8.499  -31.79  41.338  1   84.037  ? 42  ASN   A HB2  1 c 2 
ATOM   2272 H HB3  . ASN   B 1 30  ? 7.319  -30.78  41.663  1   81.898  ? 42  ASN   A HB3  1 c 2 
ATOM   2273 H HD21 . ASN   B 1 30  ? 8.127  -31.436 37.904  1   89.042  ? 42  ASN   A HD21 1 c 2 
ATOM   2274 H HD22 . ASN   B 1 30  ? 8.78   -32.398 38.912  1   92.437  ? 42  ASN   A HD22 1 c 2 
ATOM   2275 N N    . GLY   B 1 31  ? 11.046 -31.111 40.969  1   80.076  ? 43  GLY   A N    1 ? 2 
ATOM   2276 C CA   . GLY   B 1 31  ? 12.366 -31.511 40.527  1   81.988  ? 43  GLY   A CA   1 ? 2 
ATOM   2277 C C    . GLY   B 1 31  ? 13.35  -30.383 40.8    1   85.431  ? 43  GLY   A C    1 ? 2 
ATOM   2278 O O    . GLY   B 1 31  ? 12.958 -29.221 40.864  1   76.044  ? 43  GLY   A O    1 ? 2 
ATOM   2279 H H    . GLY   B 1 31  ? 10.738 -31.418 41.773  1   81.417  ? 43  GLY   A H    1 c 2 
ATOM   2280 H HA2  . GLY   B 1 31  ? 12.641 -32.324 41.013  1   85.993  ? 43  GLY   A HA2  1 c 2 
ATOM   2281 H HA3  . GLY   B 1 31  ? 12.346 -31.718 39.563  1   82.589  ? 43  GLY   A HA3  1 c 2 
ATOM   2282 N N    . GLU   B 1 32  ? 14.616 -30.764 40.997  1   96.671  ? 44  GLU   A N    1 ? 2 
ATOM   2283 C CA   . GLU   B 1 32  ? 15.697 -29.818 41.22   1   94.784  ? 44  GLU   A CA   1 ? 2 
ATOM   2284 C C    . GLU   B 1 32  ? 16.225 -29.307 39.876  1   84.769  ? 44  GLU   A C    1 ? 2 
ATOM   2285 O O    . GLU   B 1 32  ? 16.875 -28.27  39.85   1   86.543  ? 44  GLU   A O    1 ? 2 
ATOM   2286 C CB   . GLU   B 1 32  ? 16.775 -30.48  42.086  1   92.3    ? 44  GLU   A CB   1 ? 2 
ATOM   2287 H H    . GLU   B 1 32  ? 14.814 -31.657 40.983  1   96.55   ? 44  GLU   A H    1 c 2 
ATOM   2288 H HA   . GLU   B 1 32  ? 15.333 -29.046 41.724  1   90.414  ? 44  GLU   A HA   1 c 2 
ATOM   2289 H HB2  . GLU   B 1 32  ? 17.608 -30.217 41.71   0   30      ? 44  GLU   A HB2  1 c 2 
ATOM   2290 H HB3  . GLU   B 1 32  ? 16.275 -30.991 42.746  0   30      ? 44  GLU   A HB3  1 c 2 
ATOM   2291 N N    . GLU   B 1 33  ? 15.893 -29.99  38.767  1   78.141  ? 45  GLU   A N    1 ? 2 
ATOM   2292 C CA   . GLU   B 1 33  ? 16.549 -29.765 37.489  1   77.317  ? 45  GLU   A CA   1 ? 2 
ATOM   2293 C C    . GLU   B 1 33  ? 15.837 -28.635 36.745  1   67.751  ? 45  GLU   A C    1 ? 2 
ATOM   2294 O O    . GLU   B 1 33  ? 14.619 -28.626 36.635  1   59.198  ? 45  GLU   A O    1 ? 2 
ATOM   2295 C CB   . GLU   B 1 33  ? 16.586 -31.013 36.603  1   81.867  ? 45  GLU   A CB   1 ? 2 
ATOM   2296 C CG   . GLU   B 1 33  ? 16.992 -32.29  37.338  1   93.873  ? 45  GLU   A CG   1 ? 2 
ATOM   2297 C CD   . GLU   B 1 33  ? 15.921 -32.827 38.289  1   103.757 ? 45  GLU   A CD   1 ? 2 
ATOM   2298 O OE1  . GLU   B 1 33  ? 14.768 -32.312 38.215  1   102.823 ? 45  GLU   A OE1  1 ? 2 
ATOM   2299 O OE2  . GLU   B 1 33  ? 16.22  -33.721 39.129  1   107.19  ? 45  GLU   A OE2  1 ? 2 
ATOM   2300 H H    . GLU   B 1 33  ? 15.211 -30.596 38.804  1   80.939  ? 45  GLU   A H    1 c 2 
ATOM   2301 H HA   . GLU   B 1 33  ? 17.484 -29.487 37.666  1   77.175  ? 45  GLU   A HA   1 c 2 
ATOM   2302 H HB2  . GLU   B 1 33  ? 15.702 -31.142 36.2    1   82.263  ? 45  GLU   A HB2  1 c 2 
ATOM   2303 H HB3  . GLU   B 1 33  ? 17.224 -30.86  35.874  1   83.082  ? 45  GLU   A HB3  1 c 2 
ATOM   2304 H HG2  . GLU   B 1 33  ? 17.201 -32.986 36.679  1   95.895  ? 45  GLU   A HG2  1 c 2 
ATOM   2305 H HG3  . GLU   B 1 33  ? 17.807 -32.116 37.853  1   94.743  ? 45  GLU   A HG3  1 c 2 
ATOM   2306 N N    . THR   B 1 34  ? 16.613 -27.689 36.216  1   70.038  ? 46  THR   A N    1 ? 2 
ATOM   2307 C CA   . THR   B 1 34  ? 16.109 -26.75  35.218  1   62.806  ? 46  THR   A CA   1 ? 2 
ATOM   2308 C C    . THR   B 1 34  ? 16.72  -27.12  33.874  1   67.865  ? 46  THR   A C    1 ? 2 
ATOM   2309 O O    . THR   B 1 34  ? 17.748 -27.766 33.828  1   70.393  ? 46  THR   A O    1 ? 2 
ATOM   2310 C CB   . THR   B 1 34  ? 16.505 -25.333 35.605  1   67.971  ? 46  THR   A CB   1 ? 2 
ATOM   2311 O OG1  . THR   B 1 34  ? 17.928 -25.325 35.619  1   63.17   ? 46  THR   A OG1  1 ? 2 
ATOM   2312 C CG2  . THR   B 1 34  ? 15.94  -24.93  36.949  1   70.726  ? 46  THR   A CG2  1 ? 2 
ATOM   2313 H H    . THR   B 1 34  ? 17.485 -27.62  36.484  1   69.216  ? 46  THR   A H    1 c 2 
ATOM   2314 H HA   . THR   B 1 34  ? 15.132 -26.816 35.17   1   64.655  ? 46  THR   A HA   1 c 2 
ATOM   2315 H HB   . THR   B 1 34  ? 16.181 -24.703 34.917  1   63.894  ? 46  THR   A HB   1 c 2 
ATOM   2316 H HG1  . THR   B 1 34  ? 18.246 -25.932 36.23   0   30      ? 46  THR   A HG1  1 c 2 
ATOM   2317 H HG21 . THR   B 1 34  ? 16.169 -24.003 37.132  1   68.508  ? 46  THR   A HG21 1 c 2 
ATOM   2318 H HG22 . THR   B 1 34  ? 16.314 -25.498 37.643  1   71.564  ? 46  THR   A HG22 1 c 2 
ATOM   2319 H HG23 . THR   B 1 34  ? 14.973 -25.027 36.937  1   68.906  ? 46  THR   A HG23 1 c 2 
ATOM   2320 N N    . PRO   B 1 35  ? 16.153 -26.707 32.726  1   68.908  ? 47  PRO   A N    1 ? 2 
ATOM   2321 C CA   . PRO   B 1 35  ? 16.751 -27.07  31.452  1   71.837  ? 47  PRO   A CA   1 ? 2 
ATOM   2322 C C    . PRO   B 1 35  ? 18.2   -26.592 31.316  1   76.087  ? 47  PRO   A C    1 ? 2 
ATOM   2323 O O    . PRO   B 1 35  ? 18.511 -25.45  31.69   1   66.042  ? 47  PRO   A O    1 ? 2 
ATOM   2324 C CB   . PRO   B 1 35  ? 15.821 -26.399 30.455  1   67.398  ? 47  PRO   A CB   1 ? 2 
ATOM   2325 C CG   . PRO   B 1 35  ? 14.542 -26.066 31.187  1   64.424  ? 47  PRO   A CG   1 ? 2 
ATOM   2326 C CD   . PRO   B 1 35  ? 14.944 -25.87  32.608  1   65.155  ? 47  PRO   A CD   1 ? 2 
ATOM   2327 H HA   . PRO   B 1 35  ? 16.712 -28.043 31.338  1   73.941  ? 47  PRO   A HA   1 c 2 
ATOM   2328 H HB2  . PRO   B 1 35  ? 16.228 -25.587 30.106  1   66.529  ? 47  PRO   A HB2  1 c 2 
ATOM   2329 H HB3  . PRO   B 1 35  ? 15.639 -26.994 29.702  1   68.906  ? 47  PRO   A HB3  1 c 2 
ATOM   2330 H HG2  . PRO   B 1 35  ? 14.139 -25.251 30.829  1   62.92   ? 47  PRO   A HG2  1 c 2 
ATOM   2331 H HG3  . PRO   B 1 35  ? 13.897 -26.797 31.11   1   65.793  ? 47  PRO   A HG3  1 c 2 
ATOM   2332 H HD2  . PRO   B 1 35  ? 15.149 -24.934 32.796  1   63.572  ? 47  PRO   A HD2  1 c 2 
ATOM   2333 H HD3  . PRO   B 1 35  ? 14.248 -26.179 33.215  1   65.076  ? 47  PRO   A HD3  1 c 2 
ATOM   2334 N N    . MET   B 1 36  ? 19.063 -27.474 30.775  1   80.84   ? 48  MET   A N    1 ? 2 
ATOM   2335 C CA   . MET   B 1 36  ? 20.404 -27.096 30.326  1   80.016  ? 48  MET   A CA   1 ? 2 
ATOM   2336 C C    . MET   B 1 36  ? 20.291 -26.524 28.906  1   76.505  ? 48  MET   A C    1 ? 2 
ATOM   2337 O O    . MET   B 1 36  ? 19.412 -26.894 28.125  1   74.355  ? 48  MET   A O    1 ? 2 
ATOM   2338 C CB   . MET   B 1 36  ? 21.397 -28.269 30.262  1   82.35   ? 48  MET   A CB   1 ? 2 
ATOM   2339 C CG   . MET   B 1 36  ? 21.712 -29.053 31.554  1   82.67   ? 48  MET   A CG   1 ? 2 
ATOM   2340 S SD   . MET   B 1 36  ? 22.509 -28.139 32.895  1   82.989  ? 48  MET   A SD   1 ? 2 
ATOM   2341 C CE   . MET   B 1 36  ? 21.178 -27.49  33.918  1   78.961  ? 48  MET   A CE   1 ? 2 
ATOM   2342 H H    . MET   B 1 36  ? 18.805 -28.346 30.683  1   81.578  ? 48  MET   A H    1 c 2 
ATOM   2343 H HA   . MET   B 1 36  ? 20.755 -26.394 30.931  1   78.501  ? 48  MET   A HA   1 c 2 
ATOM   2344 H HB2  . MET   B 1 36  ? 21.058 -28.908 29.599  1   83.521  ? 48  MET   A HB2  1 c 2 
ATOM   2345 H HB3  . MET   B 1 36  ? 22.244 -27.92  29.911  1   83.253  ? 48  MET   A HB3  1 c 2 
ATOM   2346 H HG2  . MET   B 1 36  ? 20.875 -29.423 31.9    1   82.697  ? 48  MET   A HG2  1 c 2 
ATOM   2347 H HG3  . MET   B 1 36  ? 22.287 -29.809 31.323  1   86.431  ? 48  MET   A HG3  1 c 2 
ATOM   2348 H HE1  . MET   B 1 36  ? 21.556 -27.051 34.702  1   78.942  ? 48  MET   A HE1  1 c 2 
ATOM   2349 H HE2  . MET   B 1 36  ? 20.659 -26.844 33.404  1   76.562  ? 48  MET   A HE2  1 c 2 
ATOM   2350 H HE3  . MET   B 1 36  ? 20.599 -28.221 34.201  1   79.705  ? 48  MET   A HE3  1 c 2 
ATOM   2351 N N    . ILE   B 1 37  ? 21.207 -25.617 28.563  1   74.343  ? 49  ILE   A N    1 ? 2 
ATOM   2352 C CA   . ILE   B 1 37  ? 21.284 -25.064 27.216  1   75.892  ? 49  ILE   A CA   1 ? 2 
ATOM   2353 C C    . ILE   B 1 37  ? 21.422 -26.197 26.188  1   75.229  ? 49  ILE   A C    1 ? 2 
ATOM   2354 O O    . ILE   B 1 37  ? 22.245 -27.106 26.351  1   78.833  ? 49  ILE   A O    1 ? 2 
ATOM   2355 C CB   . ILE   B 1 37  ? 22.478 -24.096 27.219  1   81.265  ? 49  ILE   A CB   1 ? 2 
ATOM   2356 C CG1  . ILE   B 1 37  ? 22.534 -23.173 26.028  1   82.748  ? 49  ILE   A CG1  1 ? 2 
ATOM   2357 C CG2  . ILE   B 1 37  ? 23.776 -24.879 27.364  1   94.659  ? 49  ILE   A CG2  1 ? 2 
ATOM   2358 C CD1  . ILE   B 1 37  ? 23.425 -21.964 26.27   1   81.52   ? 49  ILE   A CD1  1 ? 2 
ATOM   2359 H H    . ILE   B 1 37  ? 21.8   -25.326 29.195  1   75.816  ? 49  ILE   A H    1 c 2 
ATOM   2360 H HA   . ILE   B 1 37  ? 20.467 -24.561 27.034  1   73.299  ? 49  ILE   A HA   1 c 2 
ATOM   2361 H HB   . ILE   B 1 37  ? 22.389 -23.532 28.013  1   80.661  ? 49  ILE   A HB   1 c 2 
ATOM   2362 H HG12 . ILE   B 1 37  ? 22.868 -23.668 25.253  1   84.111  ? 49  ILE   A HG12 1 c 2 
ATOM   2363 H HG13 . ILE   B 1 37  ? 21.628 -22.865 25.825  1   79.749  ? 49  ILE   A HG13 1 c 2 
ATOM   2364 H HG21 . ILE   B 1 37  ? 24.478 -24.284 27.675  1   91.842  ? 49  ILE   A HG21 1 c 2 
ATOM   2365 H HG22 . ILE   B 1 37  ? 24.025 -25.253 26.504  1   93.193  ? 49  ILE   A HG22 1 c 2 
ATOM   2366 H HG23 . ILE   B 1 37  ? 23.659 -25.599 28.005  1   92.067  ? 49  ILE   A HG23 1 c 2 
ATOM   2367 H HD11 . ILE   B 1 37  ? 23.2   -21.554 27.126  1   80.254  ? 49  ILE   A HD11 1 c 2 
ATOM   2368 H HD12 . ILE   B 1 37  ? 23.292 -21.313 25.555  1   81.115  ? 49  ILE   A HD12 1 c 2 
ATOM   2369 H HD13 . ILE   B 1 37  ? 24.36  -22.245 26.282  1   84.299  ? 49  ILE   A HD13 1 c 2 
ATOM   2370 N N    . GLY   B 1 38  ? 20.602 -26.18  25.13   1   69.095  ? 50  GLY   A N    1 ? 2 
ATOM   2371 C CA   . GLY   B 1 38  ? 20.635 -27.265 24.158  1   69.65   ? 50  GLY   A CA   1 ? 2 
ATOM   2372 C C    . GLY   B 1 38  ? 19.398 -28.162 24.204  1   68.506  ? 50  GLY   A C    1 ? 2 
ATOM   2373 O O    . GLY   B 1 38  ? 19.096 -28.837 23.218  1   67.631  ? 50  GLY   A O    1 ? 2 
ATOM   2374 H H    . GLY   B 1 38  ? 20.018 -25.487 25.01   1   67.412  ? 50  GLY   A H    1 c 2 
ATOM   2375 H HA2  . GLY   B 1 38  ? 20.714 -26.875 23.256  1   70.217  ? 50  GLY   A HA2  1 c 2 
ATOM   2376 H HA3  . GLY   B 1 38  ? 21.437 -27.815 24.314  1   72.726  ? 50  GLY   A HA3  1 c 2 
ATOM   2377 N N    . ASP   B 1 39  ? 18.699 -28.168 25.347  1   66.47   ? 51  ASP   A N    1 ? 2 
ATOM   2378 C CA   . ASP   B 1 39  ? 17.557 -29.047 25.551  1   66.534  ? 51  ASP   A CA   1 ? 2 
ATOM   2379 C C    . ASP   B 1 39  ? 16.414 -28.688 24.599  1   64.957  ? 51  ASP   A C    1 ? 2 
ATOM   2380 O O    . ASP   B 1 39  ? 16.245 -27.528 24.21   1   60.879  ? 51  ASP   A O    1 ? 2 
ATOM   2381 C CB   . ASP   B 1 39  ? 17.091 -29.002 26.996  1   67.568  ? 51  ASP   A CB   1 ? 2 
ATOM   2382 C CG   . ASP   B 1 39  ? 17.999 -29.683 28.013  1   69.967  ? 51  ASP   A CG   1 ? 2 
ATOM   2383 O OD1  . ASP   B 1 39  ? 18.955 -30.328 27.579  1   75.055  ? 51  ASP   A OD1  1 ? 2 
ATOM   2384 O OD2  . ASP   B 1 39  ? 17.74  -29.571 29.234  1   68.386  ? 51  ASP   A OD2  1 ? 2 
ATOM   2385 H H    . ASP   B 1 39  ? 18.945 -27.607 26.026  1   64.943  ? 51  ASP   A H    1 c 2 
ATOM   2386 H HA   . ASP   B 1 39  ? 17.844 -29.968 25.356  1   70.129  ? 51  ASP   A HA   1 c 2 
ATOM   2387 H HB2  . ASP   B 1 39  ? 16.99  -28.064 27.262  1   64.261  ? 51  ASP   A HB2  1 c 2 
ATOM   2388 H HB3  . ASP   B 1 39  ? 16.209 -29.424 27.053  1   66.901  ? 51  ASP   A HB3  1 c 2 
ATOM   2389 N N    . LYS   B 1 40  ? 15.627 -29.707 24.22   1   67.26   ? 52  LYS   A N    1 ? 2 
ATOM   2390 C CA   . LYS   B 1 40  ? 14.342 -29.503 23.564  1   66.89   ? 52  LYS   A CA   1 ? 2 
ATOM   2391 C C    . LYS   B 1 40  ? 13.321 -29.201 24.654  1   66.226  ? 52  LYS   A C    1 ? 2 
ATOM   2392 O O    . LYS   B 1 40  ? 13.093 -30.014 25.542  1   69.719  ? 52  LYS   A O    1 ? 2 
ATOM   2393 C CB   . LYS   B 1 40  ? 13.788 -30.67  22.734  1   69.543  ? 52  LYS   A CB   1 ? 2 
ATOM   2394 H H    . LYS   B 1 40  ? 15.905 -30.563 24.379  1   69.914  ? 52  LYS   A H    1 c 2 
ATOM   2395 H HA   . LYS   B 1 40  ? 14.419 -28.713 22.971  1   65.613  ? 52  LYS   A HA   1 c 2 
ATOM   2396 H HB2  . LYS   B 1 40  ? 14.648 -31.182 22.454  0   30      ? 52  LYS   A HB2  1 c 2 
ATOM   2397 H HB3  . LYS   B 1 40  ? 12.892 -30.678 22.799  0   30      ? 52  LYS   A HB3  1 c 2 
ATOM   2398 N N    . VAL   B 1 41  ? 12.729 -28.007 24.588  1   67.776  ? 53  VAL   A N    1 ? 2 
ATOM   2399 C CA   . VAL   B 1 41  ? 11.862 -27.519 25.657  1   64.469  ? 53  VAL   A CA   1 ? 2 
ATOM   2400 C C    . VAL   B 1 41  ? 10.44  -27.387 25.132  1   61.755  ? 53  VAL   A C    1 ? 2 
ATOM   2401 O O    . VAL   B 1 41  ? 10.238 -26.869 24.033  1   61.734  ? 53  VAL   A O    1 ? 2 
ATOM   2402 C CB   . VAL   B 1 41  ? 12.434 -26.179 26.139  1   64.79   ? 53  VAL   A CB   1 ? 2 
ATOM   2403 C CG1  . VAL   B 1 41  ? 11.55  -25.527 27.183  1   66.069  ? 53  VAL   A CG1  1 ? 2 
ATOM   2404 C CG2  . VAL   B 1 41  ? 13.866 -26.343 26.651  1   62.529  ? 53  VAL   A CG2  1 ? 2 
ATOM   2405 H H    . VAL   B 1 41  ? 12.864 -27.477 23.855  1   65.818  ? 53  VAL   A H    1 c 2 
ATOM   2406 H HA   . VAL   B 1 41  ? 11.875 -28.156 26.397  1   65.661  ? 53  VAL   A HA   1 c 2 
ATOM   2407 H HB   . VAL   B 1 41  ? 12.464 -25.579 25.357  1   63.563  ? 53  VAL   A HB   1 c 2 
ATOM   2408 H HG11 . VAL   B 1 41  ? 11.34  -26.173 27.877  1   65.522  ? 53  VAL   A HG11 1 c 2 
ATOM   2409 H HG12 . VAL   B 1 41  ? 10.727 -25.218 26.769  1   64.118  ? 53  VAL   A HG12 1 c 2 
ATOM   2410 H HG13 . VAL   B 1 41  ? 12.017 -24.774 27.574  1   63.255  ? 53  VAL   A HG13 1 c 2 
ATOM   2411 H HG21 . VAL   B 1 41  ? 14.155 -25.519 27.079  1   61.721  ? 53  VAL   A HG21 1 c 2 
ATOM   2412 H HG22 . VAL   B 1 41  ? 14.457 -26.543 25.907  1   64.827  ? 53  VAL   A HG22 1 c 2 
ATOM   2413 H HG23 . VAL   B 1 41  ? 13.9   -27.07  27.296  1   64.647  ? 53  VAL   A HG23 1 c 2 
ATOM   2414 N N    . TYR   B 1 42  ? 9.469  -27.827 25.946  1   63.342  ? 54  TYR   A N    1 ? 2 
ATOM   2415 C CA   . TYR   B 1 42  ? 8.066  -27.843 25.555  1   63.421  ? 54  TYR   A CA   1 ? 2 
ATOM   2416 C C    . TYR   B 1 42  ? 7.273  -26.92  26.494  1   59.992  ? 54  TYR   A C    1 ? 2 
ATOM   2417 O O    . TYR   B 1 42  ? 7.272  -27.135 27.7    1   52.514  ? 54  TYR   A O    1 ? 2 
ATOM   2418 C CB   . TYR   B 1 42  ? 7.512  -29.277 25.598  1   70.466  ? 54  TYR   A CB   1 ? 2 
ATOM   2419 C CG   . TYR   B 1 42  ? 8.189  -30.38  24.789  1   73.242  ? 54  TYR   A CG   1 ? 2 
ATOM   2420 C CD1  . TYR   B 1 42  ? 9.48   -30.8   25.08   1   76.793  ? 54  TYR   A CD1  1 ? 2 
ATOM   2421 C CD2  . TYR   B 1 42  ? 7.505  -31.072 23.788  1   77.695  ? 54  TYR   A CD2  1 ? 2 
ATOM   2422 C CE1  . TYR   B 1 42  ? 10.09  -31.823 24.372  1   79.279  ? 54  TYR   A CE1  1 ? 2 
ATOM   2423 C CE2  . TYR   B 1 42  ? 8.089  -32.126 23.098  1   79.499  ? 54  TYR   A CE2  1 ? 2 
ATOM   2424 C CZ   . TYR   B 1 42  ? 9.389  -32.498 23.39   1   82.642  ? 54  TYR   A CZ   1 ? 2 
ATOM   2425 O OH   . TYR   B 1 42  ? 10.017 -33.517 22.737  1   90.221  ? 54  TYR   A OH   1 ? 2 
ATOM   2426 H H    . TYR   B 1 42  ? 9.691  -28.127 26.781  1   63.133  ? 54  TYR   A H    1 c 2 
ATOM   2427 H HA   . TYR   B 1 42  ? 7.987  -27.5   24.626  1   63.9    ? 54  TYR   A HA   1 c 2 
ATOM   2428 H HB2  . TYR   B 1 42  ? 7.502  -29.56  26.54   1   69.388  ? 54  TYR   A HB2  1 c 2 
ATOM   2429 H HB3  . TYR   B 1 42  ? 6.57   -29.235 25.32   1   69.745  ? 54  TYR   A HB3  1 c 2 
ATOM   2430 H HD1  . TYR   B 1 42  ? 9.968  -30.356 25.754  1   74.103  ? 54  TYR   A HD1  1 c 2 
ATOM   2431 H HD2  . TYR   B 1 42  ? 6.612  -30.834 23.591  1   76.563  ? 54  TYR   A HD2  1 c 2 
ATOM   2432 H HE1  . TYR   B 1 42  ? 10.969 -32.085 24.585  1   80.543  ? 54  TYR   A HE1  1 c 2 
ATOM   2433 H HE2  . TYR   B 1 42  ? 7.612  -32.569 22.417  1   82.776  ? 54  TYR   A HE2  1 c 2 
ATOM   2434 H HH   . TYR   B 1 42  ? 10.734 -33.561 22.915  0   30      ? 54  TYR   A HH   1 c 2 
ATOM   2435 N N    . VAL   B 1 43  ? 6.603  -25.886 25.95   1   57.415  ? 55  VAL   A N    1 ? 2 
ATOM   2436 C CA   . VAL   B 1 43  ? 5.846  -24.974 26.801  1   55.244  ? 55  VAL   A CA   1 ? 2 
ATOM   2437 C C    . VAL   B 1 43  ? 4.449  -24.745 26.245  1   52.471  ? 55  VAL   A C    1 ? 2 
ATOM   2438 O O    . VAL   B 1 43  ? 4.206  -24.969 25.059  1   59.328  ? 55  VAL   A O    1 ? 2 
ATOM   2439 C CB   . VAL   B 1 43  ? 6.527  -23.604 27.006  1   48.755  ? 55  VAL   A CB   1 ? 2 
ATOM   2440 C CG1  . VAL   B 1 43  ? 7.987  -23.759 27.428  1   49.915  ? 55  VAL   A CG1  1 ? 2 
ATOM   2441 C CG2  . VAL   B 1 43  ? 6.396  -22.738 25.763  1   50.798  ? 55  VAL   A CG2  1 ? 2 
ATOM   2442 H H    . VAL   B 1 43  ? 6.618  -25.749 25.046  1   58.063  ? 55  VAL   A H    1 c 2 
ATOM   2443 H HA   . VAL   B 1 43  ? 5.751  -25.393 27.675  1   54.2    ? 55  VAL   A HA   1 c 2 
ATOM   2444 H HB   . VAL   B 1 43  ? 6.05   -23.148 27.737  1   49.207  ? 55  VAL   A HB   1 c 2 
ATOM   2445 H HG11 . VAL   B 1 43  ? 8.49   -24.185 26.714  1   50.625  ? 55  VAL   A HG11 1 c 2 
ATOM   2446 H HG12 . VAL   B 1 43  ? 8.037  -24.307 28.23   1   50.062  ? 55  VAL   A HG12 1 c 2 
ATOM   2447 H HG13 . VAL   B 1 43  ? 8.367  -22.884 27.612  1   47.994  ? 55  VAL   A HG13 1 c 2 
ATOM   2448 H HG21 . VAL   B 1 43  ? 6.97   -21.961 25.851  1   48.652  ? 55  VAL   A HG21 1 c 2 
ATOM   2449 H HG22 . VAL   B 1 43  ? 5.474  -22.445 25.663  1   49.974  ? 55  VAL   A HG22 1 c 2 
ATOM   2450 H HG23 . VAL   B 1 43  ? 6.66   -23.249 24.98   1   51.323  ? 55  VAL   A HG23 1 c 2 
ATOM   2451 N N    . HIS   B 1 44  ? 3.569  -24.232 27.121  1   50.801  ? 56  HIS   A N    1 ? 2 
ATOM   2452 C CA   . HIS   B 1 44  ? 2.405  -23.449 26.719  1   50.181  ? 56  HIS   A CA   1 ? 2 
ATOM   2453 C C    . HIS   B 1 44  ? 2.604  -22.004 27.182  1   45.927  ? 56  HIS   A C    1 ? 2 
ATOM   2454 O O    . HIS   B 1 44  ? 3.269  -21.762 28.178  1   47.303  ? 56  HIS   A O    1 ? 2 
ATOM   2455 C CB   . HIS   B 1 44  ? 1.113  -24.054 27.278  1   56.032  ? 56  HIS   A CB   1 ? 2 
ATOM   2456 C CG   . HIS   B 1 44  ? 0.44   -25.074 26.41   1   58.554  ? 56  HIS   A CG   1 ? 2 
ATOM   2457 N ND1  . HIS   B 1 44  ? 0.078  -24.805 25.107  1   58.171  ? 56  HIS   A ND1  1 ? 2 
ATOM   2458 C CD2  . HIS   B 1 44  ? 0.013  -26.321 26.672  1   56.365  ? 56  HIS   A CD2  1 ? 2 
ATOM   2459 C CE1  . HIS   B 1 44  ? -0.55  -25.864 24.6    1   62.931  ? 56  HIS   A CE1  1 ? 2 
ATOM   2460 N NE2  . HIS   B 1 44  ? -0.592 -26.798 25.537  1   60.363  ? 56  HIS   A NE2  1 ? 2 
ATOM   2461 H H    . HIS   B 1 44  ? 3.702  -24.381 28.013  1   50.666  ? 56  HIS   A H    1 c 2 
ATOM   2462 H HA   . HIS   B 1 44  ? 2.357  -23.453 25.733  1   51.39   ? 56  HIS   A HA   1 c 2 
ATOM   2463 H HB2  . HIS   B 1 44  ? 1.315  -24.466 28.146  1   55.026  ? 56  HIS   A HB2  1 c 2 
ATOM   2464 H HB3  . HIS   B 1 44  ? 0.479  -23.325 27.451  1   54.365  ? 56  HIS   A HB3  1 c 2 
ATOM   2465 H HD1  . HIS   B 1 44  ? 0.193  -24.006 24.664  0   30      ? 56  HIS   A HD1  1 c 2 
ATOM   2466 H HD2  . HIS   B 1 44  ? 0.105  -26.786 27.48   1   58.212  ? 56  HIS   A HD2  1 c 2 
ATOM   2467 H HE1  . HIS   B 1 44  ? -0.88  -25.945 23.721  1   63.059  ? 56  HIS   A HE1  1 c 2 
ATOM   2468 H HE2  . HIS   B 1 44  ? -0.942 -27.57  25.411  0   30      ? 56  HIS   A HE2  1 c 2 
ATOM   2469 N N    . TYR   B 1 45  ? 2.071  -21.036 26.426  1   48.279  ? 57  TYR   A N    1 ? 2 
ATOM   2470 C CA   . TYR   B 1 45  ? 2.287  -19.628 26.727  1   47.176  ? 57  TYR   A CA   1 ? 2 
ATOM   2471 C C    . TYR   B 1 45  ? 1.08   -18.811 26.298  1   51.209  ? 57  TYR   A C    1 ? 2 
ATOM   2472 O O    . TYR   B 1 45  ? 0.344  -19.204 25.405  1   51.687  ? 57  TYR   A O    1 ? 2 
ATOM   2473 C CB   . TYR   B 1 45  ? 3.546  -19.053 26.069  1   44.772  ? 57  TYR   A CB   1 ? 2 
ATOM   2474 C CG   . TYR   B 1 45  ? 3.446  -18.837 24.562  1   48.024  ? 57  TYR   A CG   1 ? 2 
ATOM   2475 C CD1  . TYR   B 1 45  ? 2.936  -17.658 24.034  1   43.894  ? 57  TYR   A CD1  1 ? 2 
ATOM   2476 C CD2  . TYR   B 1 45  ? 3.844  -19.818 23.658  1   50.859  ? 57  TYR   A CD2  1 ? 2 
ATOM   2477 C CE1  . TYR   B 1 45  ? 2.796  -17.484 22.666  1   48.781  ? 57  TYR   A CE1  1 ? 2 
ATOM   2478 C CE2  . TYR   B 1 45  ? 3.776  -19.615 22.288  1   48.192  ? 57  TYR   A CE2  1 ? 2 
ATOM   2479 C CZ   . TYR   B 1 45  ? 3.254  -18.446 21.787  1   46.729  ? 57  TYR   A CZ   1 ? 2 
ATOM   2480 O OH   . TYR   B 1 45  ? 3.155  -18.219 20.45   1   54.591  ? 57  TYR   A OH   1 ? 2 
ATOM   2481 H H    . TYR   B 1 45  ? 1.558  -21.261 25.703  1   49.039  ? 57  TYR   A H    1 c 2 
ATOM   2482 H HA   . TYR   B 1 45  ? 2.386  -19.54  27.709  1   46.759  ? 57  TYR   A HA   1 c 2 
ATOM   2483 H HB2  . TYR   B 1 45  ? 3.753  -18.193 26.498  1   44.45   ? 57  TYR   A HB2  1 c 2 
ATOM   2484 H HB3  . TYR   B 1 45  ? 4.295  -19.663 26.251  1   45.528  ? 57  TYR   A HB3  1 c 2 
ATOM   2485 H HD1  . TYR   B 1 45  ? 2.622  -16.986 24.618  1   45.019  ? 57  TYR   A HD1  1 c 2 
ATOM   2486 H HD2  . TYR   B 1 45  ? 4.221  -20.619 23.985  1   49.889  ? 57  TYR   A HD2  1 c 2 
ATOM   2487 H HE1  . TYR   B 1 45  ? 2.468  -16.667 22.334  1   47.314  ? 57  TYR   A HE1  1 c 2 
ATOM   2488 H HE2  . TYR   B 1 45  ? 4.063  -20.291 21.697  1   50.002  ? 57  TYR   A HE2  1 c 2 
ATOM   2489 H HH   . TYR   B 1 45  ? 2.761  -17.48  20.298  0   30      ? 57  TYR   A HH   1 c 2 
ATOM   2490 N N    . LYS   B 1 46  ? 0.896  -17.688 26.983  1   48.679  ? 58  LYS   A N    1 ? 2 
ATOM   2491 C CA   . LYS   B 1 46  ? -0.005 -16.613 26.588  1   52.013  ? 58  LYS   A CA   1 ? 2 
ATOM   2492 C C    . LYS   B 1 46  ? 0.847  -15.352 26.618  1   49.091  ? 58  LYS   A C    1 ? 2 
ATOM   2493 O O    . LYS   B 1 46  ? 1.554  -15.114 27.585  1   45.71   ? 58  LYS   A O    1 ? 2 
ATOM   2494 C CB   . LYS   B 1 46  ? -1.187 -16.546 27.555  1   54.302  ? 58  LYS   A CB   1 ? 2 
ATOM   2495 C CG   . LYS   B 1 46  ? -1.919 -17.868 27.648  1   58.161  ? 58  LYS   A CG   1 ? 2 
ATOM   2496 C CD   . LYS   B 1 46  ? -2.917 -17.972 28.783  1   60.722  ? 58  LYS   A CD   1 ? 2 
ATOM   2497 C CE   . LYS   B 1 46  ? -3.502 -19.343 28.963  1   61.84   ? 58  LYS   A CE   1 ? 2 
ATOM   2498 N NZ   . LYS   B 1 46  ? -4.611 -19.264 29.927  1   64.779  ? 58  LYS   A NZ   1 ? 2 
ATOM   2499 H H    . LYS   B 1 46  ? 1.363  -17.583 27.762  1   48.695  ? 58  LYS   A H    1 c 2 
ATOM   2500 H HA   . LYS   B 1 46  ? -0.323 -16.779 25.664  1   52.351  ? 58  LYS   A HA   1 c 2 
ATOM   2501 H HB2  . LYS   B 1 46  ? -0.864 -16.297 28.447  1   53.656  ? 58  LYS   A HB2  1 c 2 
ATOM   2502 H HB3  . LYS   B 1 46  ? -1.815 -15.855 27.253  1   55.258  ? 58  LYS   A HB3  1 c 2 
ATOM   2503 H HG2  . LYS   B 1 46  ? -2.39  -18.019 26.799  1   59.144  ? 58  LYS   A HG2  1 c 2 
ATOM   2504 H HG3  . LYS   B 1 46  ? -1.257 -18.584 27.748  1   57.401  ? 58  LYS   A HG3  1 c 2 
ATOM   2505 H HD2  . LYS   B 1 46  ? -2.472 -17.706 29.617  1   59.174  ? 58  LYS   A HD2  1 c 2 
ATOM   2506 H HD3  . LYS   B 1 46  ? -3.646 -17.335 28.62   1   61.129  ? 58  LYS   A HD3  1 c 2 
ATOM   2507 H HE2  . LYS   B 1 46  ? -3.835 -19.68  28.112  1   63.456  ? 58  LYS   A HE2  1 c 2 
ATOM   2508 H HE3  . LYS   B 1 46  ? -2.823 -19.956 29.298  1   61.659  ? 58  LYS   A HE3  1 c 2 
ATOM   2509 H HZ1  . LYS   B 1 46  ? -5.266 -18.731 29.599  1   65.305  ? 58  LYS   A HZ1  1 c 2 
ATOM   2510 H HZ2  . LYS   B 1 46  ? -4.313 -18.923 30.711  1   63.527  ? 58  LYS   A HZ2  1 c 2 
ATOM   2511 H HZ3  . LYS   B 1 46  ? -4.948 -20.092 30.073  1   65.806  ? 58  LYS   A HZ3  1 c 2 
ATOM   2512 N N    . GLY   B 1 47  ? 0.949  -14.675 25.48   1   45.862  ? 59  GLY   A N    1 ? 2 
ATOM   2513 C CA   . GLY   B 1 47  ? 1.769  -13.489 25.413  1   45.347  ? 59  GLY   A CA   1 ? 2 
ATOM   2514 C C    . GLY   B 1 47  ? 0.951  -12.306 24.93   1   48.086  ? 59  GLY   A C    1 ? 2 
ATOM   2515 O O    . GLY   B 1 47  ? -0.128 -12.45  24.343  1   48.678  ? 59  GLY   A O    1 ? 2 
ATOM   2516 H H    . GLY   B 1 47  ? 0.501  -14.953 24.734  1   47.892  ? 59  GLY   A H    1 c 2 
ATOM   2517 H HA2  . GLY   B 1 47  ? 2.14   -13.294 26.302  1   44.736  ? 59  GLY   A HA2  1 c 2 
ATOM   2518 H HA3  . GLY   B 1 47  ? 2.52   -13.648 24.794  1   45.251  ? 59  GLY   A HA3  1 c 2 
ATOM   2519 N N    . LYS   B 1 48  ? 1.457  -11.116 25.214  1   46.418  ? 60  LYS   A N    1 ? 2 
ATOM   2520 C CA   . LYS   B 1 48  ? 0.826  -9.906  24.707  1   49.876  ? 60  LYS   A CA   1 ? 2 
ATOM   2521 C C    . LYS   B 1 48  ? 1.866  -8.793  24.695  1   49.692  ? 60  LYS   A C    1 ? 2 
ATOM   2522 O O    . LYS   B 1 48  ? 2.913  -8.87   25.354  1   47.808  ? 60  LYS   A O    1 ? 2 
ATOM   2523 C CB   . LYS   B 1 48  ? -0.393 -9.563  25.579  1   54.266  ? 60  LYS   A CB   1 ? 2 
ATOM   2524 C CG   . LYS   B 1 48  ? -0.156 -9.469  27.092  1   60.507  ? 60  LYS   A CG   1 ? 2 
ATOM   2525 C CD   . LYS   B 1 48  ? -1.323 -8.955  27.93   1   66.122  ? 60  LYS   A CD   1 ? 2 
ATOM   2526 C CE   . LYS   B 1 48  ? -1.43  -7.456  27.775  1   76.704  ? 60  LYS   A CE   1 ? 2 
ATOM   2527 N NZ   . LYS   B 1 48  ? -2.707 -6.786  28.086  1   82.421  ? 60  LYS   A NZ   1 ? 2 
ATOM   2528 H H    . LYS   B 1 48  ? 2.207  -11.047 25.732  1   46.114  ? 60  LYS   A H    1 c 2 
ATOM   2529 H HA   . LYS   B 1 48  ? 0.529  -10.074 23.778  1   50.979  ? 60  LYS   A HA   1 c 2 
ATOM   2530 H HB2  . LYS   B 1 48  ? -0.753 -8.703  25.272  1   56.429  ? 60  LYS   A HB2  1 c 2 
ATOM   2531 H HB3  . LYS   B 1 48  ? -1.084 -10.24  25.421  1   55.613  ? 60  LYS   A HB3  1 c 2 
ATOM   2532 H HG2  . LYS   B 1 48  ? 0.09   -10.363 27.417  1   58.54   ? 60  LYS   A HG2  1 c 2 
ATOM   2533 H HG3  . LYS   B 1 48  ? 0.618  -8.884  27.244  1   58.995  ? 60  LYS   A HG3  1 c 2 
ATOM   2534 H HD2  . LYS   B 1 48  ? -2.158 -9.376  27.63   1   68.146  ? 60  LYS   A HD2  1 c 2 
ATOM   2535 H HD3  . LYS   B 1 48  ? -1.176 -9.177  28.876  1   66.579  ? 60  LYS   A HD3  1 c 2 
ATOM   2536 H HE2  . LYS   B 1 48  ? -0.74  -7.052  28.331  1   74.387  ? 60  LYS   A HE2  1 c 2 
ATOM   2537 H HE3  . LYS   B 1 48  ? -1.21  -7.236  26.854  1   74.787  ? 60  LYS   A HE3  1 c 2 
ATOM   2538 H HZ1  . LYS   B 1 48  ? -2.903 -6.892  28.964  1   81.587  ? 60  LYS   A HZ1  1 c 2 
ATOM   2539 H HZ2  . LYS   B 1 48  ? -3.371 -7.148  27.586  1   82.306  ? 60  LYS   A HZ2  1 c 2 
ATOM   2540 H HZ3  . LYS   B 1 48  ? -2.642 -5.902  27.899  1   82.471  ? 60  LYS   A HZ3  1 c 2 
ATOM   2541 N N    . LEU   B 1 49  ? 1.573  -7.744  23.936  1   52.08   ? 61  LEU   A N    1 ? 2 
ATOM   2542 C CA   . LEU   B 1 49  ? 2.226  -6.453  24.113  1   50.873  ? 61  LEU   A CA   1 ? 2 
ATOM   2543 C C    . LEU   B 1 49  ? 1.668  -5.856  25.404  1   53.128  ? 61  LEU   A C    1 ? 2 
ATOM   2544 O O    . LEU   B 1 49  ? 0.513  -6.091  25.728  1   54.394  ? 61  LEU   A O    1 ? 2 
ATOM   2545 C CB   . LEU   B 1 49  ? 1.874  -5.542  22.921  1   51.481  ? 61  LEU   A CB   1 ? 2 
ATOM   2546 C CG   . LEU   B 1 49  ? 2.179  -6.093  21.523  1   50.7    ? 61  LEU   A CG   1 ? 2 
ATOM   2547 C CD1  . LEU   B 1 49  ? 1.765  -5.107  20.416  1   58.342  ? 61  LEU   A CD1  1 ? 2 
ATOM   2548 C CD2  . LEU   B 1 49  ? 3.656  -6.401  21.35   1   47.488  ? 61  LEU   A CD2  1 ? 2 
ATOM   2549 H H    . LEU   B 1 49  ? 0.932  -7.828  23.291  1   52.538  ? 61  LEU   A H    1 c 2 
ATOM   2550 H HA   . LEU   B 1 49  ? 3.207  -6.576  24.179  1   50.118  ? 61  LEU   A HA   1 c 2 
ATOM   2551 H HB2  . LEU   B 1 49  ? 0.911  -5.34   22.968  1   52.965  ? 61  LEU   A HB2  1 c 2 
ATOM   2552 H HB3  . LEU   B 1 49  ? 2.359  -4.692  23.032  1   52.187  ? 61  LEU   A HB3  1 c 2 
ATOM   2553 H HG   . LEU   B 1 49  ? 1.668  -6.933  21.397  1   51.16   ? 61  LEU   A HG   1 c 2 
ATOM   2554 H HD11 . LEU   B 1 49  ? 0.805  -4.956  20.457  1   58.03   ? 61  LEU   A HD11 1 c 2 
ATOM   2555 H HD12 . LEU   B 1 49  ? 1.995  -5.477  19.547  1   57.099  ? 61  LEU   A HD12 1 c 2 
ATOM   2556 H HD13 . LEU   B 1 49  ? 2.23   -4.263  20.541  1   57.366  ? 61  LEU   A HD13 1 c 2 
ATOM   2557 H HD21 . LEU   B 1 49  ? 3.901  -7.146  21.922  1   46.625  ? 61  LEU   A HD21 1 c 2 
ATOM   2558 H HD22 . LEU   B 1 49  ? 4.182  -5.62   21.593  1   48.317  ? 61  LEU   A HD22 1 c 2 
ATOM   2559 H HD23 . LEU   B 1 49  ? 3.833  -6.635  20.423  1   48.688  ? 61  LEU   A HD23 1 c 2 
ATOM   2560 N N    . SER   B 1 50  ? 2.425  -5.006  26.097  1   61.055  ? 62  SER   A N    1 ? 2 
ATOM   2561 C CA   . SER   B 1 50  ? 1.885  -4.35   27.284  1   64.291  ? 62  SER   A CA   1 ? 2 
ATOM   2562 C C    . SER   B 1 50  ? 0.752  -3.379  26.948  1   73.559  ? 62  SER   A C    1 ? 2 
ATOM   2563 O O    . SER   B 1 50  ? -0.143 -3.156  27.765  1   82.389  ? 62  SER   A O    1 ? 2 
ATOM   2564 C CB   . SER   B 1 50  ? 2.986  -3.655  28.025  1   70.531  ? 62  SER   A CB   1 ? 2 
ATOM   2565 O OG   . SER   B 1 50  ? 4.101  -4.528  28.174  1   74.15   ? 62  SER   A OG   1 ? 2 
ATOM   2566 H H    . SER   B 1 50  ? 3.282  -4.83   25.834  1   59.042  ? 62  SER   A H    1 c 2 
ATOM   2567 H HA   . SER   B 1 50  ? 1.515  -5.053  27.876  1   65.197  ? 62  SER   A HA   1 c 2 
ATOM   2568 H HB2  . SER   B 1 50  ? 3.258  -2.858  27.532  1   71.5    ? 62  SER   A HB2  1 c 2 
ATOM   2569 H HB3  . SER   B 1 50  ? 2.664  -3.381  28.905  1   70.984  ? 62  SER   A HB3  1 c 2 
ATOM   2570 H HG   . SER   B 1 50  ? 4.735  -4.148  28.621  0   30      ? 62  SER   A HG   1 c 2 
ATOM   2571 N N    . ASN   B 1 51  ? 0.75   -2.818  25.73   1   66.229  ? 63  ASN   A N    1 ? 2 
ATOM   2572 C CA   . ASN   B 1 51  ? -0.264 -1.854  25.355  1   73.867  ? 63  ASN   A CA   1 ? 2 
ATOM   2573 C C    . ASN   B 1 51  ? -1.623 -2.522  25.093  1   77.116  ? 63  ASN   A C    1 ? 2 
ATOM   2574 O O    . ASN   B 1 51  ? -2.587 -1.804  24.799  1   70.644  ? 63  ASN   A O    1 ? 2 
ATOM   2575 C CB   . ASN   B 1 51  ? 0.202  -1.025  24.16   1   76.926  ? 63  ASN   A CB   1 ? 2 
ATOM   2576 C CG   . ASN   B 1 51  ? 0.217  -1.808  22.866  1   74.059  ? 63  ASN   A CG   1 ? 2 
ATOM   2577 O OD1  . ASN   B 1 51  ? -0.088 -3.009  22.828  1   72.704  ? 63  ASN   A OD1  1 ? 2 
ATOM   2578 N ND2  . ASN   B 1 51  ? 0.617  -1.146  21.79   1   74.428  ? 63  ASN   A ND2  1 ? 2 
ATOM   2579 H H    . ASN   B 1 51  ? 1.401  -3.035  25.127  1   68.233  ? 63  ASN   A H    1 c 2 
ATOM   2580 H HA   . ASN   B 1 51  ? -0.377 -1.23   26.108  1   74.819  ? 63  ASN   A HA   1 c 2 
ATOM   2581 H HB2  . ASN   B 1 51  ? -0.391 -0.254  24.058  1   78.532  ? 63  ASN   A HB2  1 c 2 
ATOM   2582 H HB3  . ASN   B 1 51  ? 1.103  -0.689  24.338  1   75.58   ? 63  ASN   A HB3  1 c 2 
ATOM   2583 H HD21 . ASN   B 1 51  ? 0.607  -1.544  20.998  1   74.8    ? 63  ASN   A HD21 1 c 2 
ATOM   2584 H HD22 . ASN   B 1 51  ? 0.894  -0.306  21.862  1   76.144  ? 63  ASN   A HD22 1 c 2 
ATOM   2585 N N    . GLY   B 1 52  ? -1.695 -3.87   25.161  1   77.611  ? 64  GLY   A N    1 ? 2 
ATOM   2586 C CA   . GLY   B 1 52  ? -2.952 -4.609  25.058  1   81.005  ? 64  GLY   A CA   1 ? 2 
ATOM   2587 C C    . GLY   B 1 52  ? -3.523 -4.67   23.634  1   86.391  ? 64  GLY   A C    1 ? 2 
ATOM   2588 O O    . GLY   B 1 52  ? -4.71  -4.985  23.455  1   89.525  ? 64  GLY   A O    1 ? 2 
ATOM   2589 H H    . GLY   B 1 52  ? -0.923 -4.349  25.254  1   75.438  ? 64  GLY   A H    1 c 2 
ATOM   2590 H HA2  . GLY   B 1 52  ? -2.805 -5.527  25.386  1   79.511  ? 64  GLY   A HA2  1 c 2 
ATOM   2591 H HA3  . GLY   B 1 52  ? -3.615 -4.185  25.652  1   82.723  ? 64  GLY   A HA3  1 c 2 
ATOM   2592 N N    . LYS   B 1 53  ? -2.679 -4.402  22.618  1   81.269  ? 65  LYS   A N    1 ? 2 
ATOM   2593 C CA   . LYS   B 1 53  ? -3.16  -4.296  21.24   1   79.294  ? 65  LYS   A CA   1 ? 2 
ATOM   2594 C C    . LYS   B 1 53  ? -2.957 -5.627  20.497  1   73.414  ? 65  LYS   A C    1 ? 2 
ATOM   2595 O O    . LYS   B 1 53  ? -3.579 -5.845  19.465  1   75.401  ? 65  LYS   A O    1 ? 2 
ATOM   2596 C CB   . LYS   B 1 53  ? -2.579 -3.074  20.507  1   71.167  ? 65  LYS   A CB   1 ? 2 
ATOM   2597 H H    . LYS   B 1 53  ? -1.788 -4.287  22.786  1   79.789  ? 65  LYS   A H    1 c 2 
ATOM   2598 H HA   . LYS   B 1 53  ? -4.137 -4.137  21.281  1   79.278  ? 65  LYS   A HA   1 c 2 
ATOM   2599 H HB2  . LYS   B 1 53  ? -1.636 -3.127  20.58   0   30      ? 65  LYS   A HB2  1 c 2 
ATOM   2600 H HB3  . LYS   B 1 53  ? -3.349 -2.517  20.198  0   30      ? 65  LYS   A HB3  1 c 2 
ATOM   2601 N N    . LYS   B 1 54  ? -2.124 -6.54   21.027  1   70.849  ? 66  LYS   A N    1 ? 2 
ATOM   2602 C CA   . LYS   B 1 54  ? -1.951 -7.86   20.427  1   68.025  ? 66  LYS   A CA   1 ? 2 
ATOM   2603 C C    . LYS   B 1 54  ? -1.768 -8.905  21.529  1   64.155  ? 66  LYS   A C    1 ? 2 
ATOM   2604 O O    . LYS   B 1 54  ? -1.061 -8.67   22.511  1   58.253  ? 66  LYS   A O    1 ? 2 
ATOM   2605 C CB   . LYS   B 1 54  ? -0.786 -7.927  19.422  1   63.953  ? 66  LYS   A CB   1 ? 2 
ATOM   2606 H H    . LYS   B 1 54  ? -1.646 -6.333  21.778  1   69.19   ? 66  LYS   A H    1 c 2 
ATOM   2607 H HA   . LYS   B 1 54  ? -2.781 -8.08   19.933  1   69.085  ? 66  LYS   A HA   1 c 2 
ATOM   2608 H HB2  . LYS   B 1 54  ? 0.025  -7.828  19.994  0   30      ? 66  LYS   A HB2  1 c 2 
ATOM   2609 H HB3  . LYS   B 1 54  ? -1.161 -7.873  18.563  0   30      ? 66  LYS   A HB3  1 c 2 
ATOM   2610 N N    . PHE   B 1 55  ? -2.385 -10.073 21.29   1   57.603  ? 67  PHE   A N    1 ? 2 
ATOM   2611 C CA   . PHE   B 1 55  ? -2.304 -11.263 22.123  1   63.627  ? 67  PHE   A CA   1 ? 2 
ATOM   2612 C C    . PHE   B 1 55  ? -1.967 -12.455 21.249  1   61.174  ? 67  PHE   A C    1 ? 2 
ATOM   2613 O O    . PHE   B 1 55  ? -2.313 -12.494 20.073  1   70.195  ? 67  PHE   A O    1 ? 2 
ATOM   2614 C CB   . PHE   B 1 55  ? -3.65  -11.619 22.753  1   62.543  ? 67  PHE   A CB   1 ? 2 
ATOM   2615 C CG   . PHE   B 1 55  ? -4.167 -10.408 23.507  1   68.304  ? 67  PHE   A CG   1 ? 2 
ATOM   2616 C CD1  . PHE   B 1 55  ? -4.801 -9.369  22.835  1   68.559  ? 67  PHE   A CD1  1 ? 2 
ATOM   2617 C CD2  . PHE   B 1 55  ? -3.966 -10.278 24.878  1   68.667  ? 67  PHE   A CD2  1 ? 2 
ATOM   2618 C CE1  . PHE   B 1 55  ? -5.267 -8.26   23.523  1   69.278  ? 67  PHE   A CE1  1 ? 2 
ATOM   2619 C CE2  . PHE   B 1 55  ? -4.451 -9.164  25.557  1   70.993  ? 67  PHE   A CE2  1 ? 2 
ATOM   2620 C CZ   . PHE   B 1 55  ? -5.075 -8.145  24.871  1   68.517  ? 67  PHE   A CZ   1 ? 2 
ATOM   2621 H H    . PHE   B 1 55  ? -2.901 -10.127 20.537  1   62.539  ? 67  PHE   A H    1 c 2 
ATOM   2622 H HA   . PHE   B 1 55  ? -1.615 -11.144 22.826  1   59.374  ? 67  PHE   A HA   1 c 2 
ATOM   2623 H HB2  . PHE   B 1 55  ? -4.288 -11.867 22.046  1   65.992  ? 67  PHE   A HB2  1 c 2 
ATOM   2624 H HB3  . PHE   B 1 55  ? -3.532 -12.372 23.373  1   63.387  ? 67  PHE   A HB3  1 c 2 
ATOM   2625 H HD1  . PHE   B 1 55  ? -4.937 -9.433  21.903  1   69.952  ? 67  PHE   A HD1  1 c 2 
ATOM   2626 H HD2  . PHE   B 1 55  ? -3.537 -10.97  25.356  1   67.033  ? 67  PHE   A HD2  1 c 2 
ATOM   2627 H HE1  . PHE   B 1 55  ? -5.703 -7.568  23.052  1   71.443  ? 67  PHE   A HE1  1 c 2 
ATOM   2628 H HE2  . PHE   B 1 55  ? -4.316 -9.088  26.488  1   68.852  ? 67  PHE   A HE2  1 c 2 
ATOM   2629 H HZ   . PHE   B 1 55  ? -5.398 -7.389  25.334  1   70.644  ? 67  PHE   A HZ   1 c 2 
ATOM   2630 N N    . ASP   B 1 56  ? -1.296 -13.422 21.833  1   53.504  ? 68  ASP   A N    1 ? 2 
ATOM   2631 C CA   . ASP   B 1 56  ? -0.91  -14.603 21.093  1   56.614  ? 68  ASP   A CA   1 ? 2 
ATOM   2632 C C    . ASP   B 1 56  ? -0.796 -15.717 22.111  1   52.999  ? 68  ASP   A C    1 ? 2 
ATOM   2633 O O    . ASP   B 1 56  ? -0.149 -15.523 23.125  1   47.904  ? 68  ASP   A O    1 ? 2 
ATOM   2634 C CB   . ASP   B 1 56  ? 0.411  -14.414 20.358  1   51.747  ? 68  ASP   A CB   1 ? 2 
ATOM   2635 C CG   . ASP   B 1 56  ? 0.968  -15.693 19.741  1   58.549  ? 68  ASP   A CG   1 ? 2 
ATOM   2636 O OD1  . ASP   B 1 56  ? 0.228  -16.342 18.957  1   65.387  ? 68  ASP   A OD1  1 ? 2 
ATOM   2637 O OD2  . ASP   B 1 56  ? 2.102  -16.066 20.079  1   60.761  ? 68  ASP   A OD2  1 ? 2 
ATOM   2638 H H    . ASP   B 1 56  ? -1.066 -13.353 22.715  1   54.314  ? 68  ASP   A H    1 c 2 
ATOM   2639 H HA   . ASP   B 1 56  ? -1.621 -14.824 20.448  1   56.754  ? 68  ASP   A HA   1 c 2 
ATOM   2640 H HB2  . ASP   B 1 56  ? 0.287  -13.755 19.643  1   54.921  ? 68  ASP   A HB2  1 c 2 
ATOM   2641 H HB3  . ASP   B 1 56  ? 1.074  -14.059 20.987  1   52.407  ? 68  ASP   A HB3  1 c 2 
ATOM   2642 N N    . SER   B 1 57  ? -1.408 -16.863 21.848  1   55.926  ? 69  SER   A N    1 ? 2 
ATOM   2643 C CA   . SER   B 1 57  ? -1.286 -17.979 22.783  1   58.785  ? 69  SER   A CA   1 ? 2 
ATOM   2644 C C    . SER   B 1 57  ? -1.003 -19.271 22.021  1   60.205  ? 69  SER   A C    1 ? 2 
ATOM   2645 O O    . SER   B 1 57  ? -1.572 -19.491 20.947  1   62.394  ? 69  SER   A O    1 ? 2 
ATOM   2646 C CB   . SER   B 1 57  ? -2.529 -18.133 23.619  1   60.719  ? 69  SER   A CB   1 ? 2 
ATOM   2647 O OG   . SER   B 1 57  ? -2.574 -19.443 24.175  1   61.977  ? 69  SER   A OG   1 ? 2 
ATOM   2648 H H    . SER   B 1 57  ? -1.905 -16.964 21.087  1   57.996  ? 69  SER   A H    1 c 2 
ATOM   2649 H HA   . SER   B 1 57  ? -0.522 -17.801 23.386  1   56.335  ? 69  SER   A HA   1 c 2 
ATOM   2650 H HB2  . SER   B 1 57  ? -2.525 -17.471 24.337  1   59.603  ? 69  SER   A HB2  1 c 2 
ATOM   2651 H HB3  . SER   B 1 57  ? -3.318 -17.985 23.063  1   62.38   ? 69  SER   A HB3  1 c 2 
ATOM   2652 H HG   . SER   B 1 57  ? -3.272 -19.465 24.679  0   30      ? 69  SER   A HG   1 c 2 
ATOM   2653 N N    . SER   B 1 58  ? -0.168 -20.13  22.612  1   52.892  ? 70  SER   A N    1 ? 2 
ATOM   2654 C CA   . SER   B 1 58  ? 0.088  -21.444 22.053  1   57.811  ? 70  SER   A CA   1 ? 2 
ATOM   2655 C C    . SER   B 1 58  ? -1.235 -22.202 21.906  1   66.42   ? 70  SER   A C    1 ? 2 
ATOM   2656 O O    . SER   B 1 58  ? -1.387 -23.001 20.986  1   73.197  ? 70  SER   A O    1 ? 2 
ATOM   2657 C CB   . SER   B 1 58  ? 1.061  -22.204 22.917  1   59.4    ? 70  SER   A CB   1 ? 2 
ATOM   2658 O OG   . SER   B 1 58  ? 0.609  -22.268 24.264  1   57.042  ? 70  SER   A OG   1 ? 2 
ATOM   2659 H H    . SER   B 1 58  ? 0.255  -19.889 23.386  1   53.537  ? 70  SER   A H    1 c 2 
ATOM   2660 H HA   . SER   B 1 58  ? 0.485  -21.329 21.153  1   59.053  ? 70  SER   A HA   1 c 2 
ATOM   2661 H HB2  . SER   B 1 58  ? 1.165  -23.109 22.567  1   60.061  ? 70  SER   A HB2  1 c 2 
ATOM   2662 H HB3  . SER   B 1 58  ? 1.931  -21.765 22.887  1   56.907  ? 70  SER   A HB3  1 c 2 
ATOM   2663 H HG   . SER   B 1 58  ? 1.161  -22.667 24.673  0   30      ? 70  SER   A HG   1 c 2 
ATOM   2664 N N    . HIS   B 1 59  ? -2.196 -21.931 22.806  1   61.029  ? 71  HIS   A N    1 ? 2 
ATOM   2665 C CA   . HIS   B 1 59  ? -3.47  -22.634 22.807  1   68.032  ? 71  HIS   A CA   1 ? 2 
ATOM   2666 C C    . HIS   B 1 59  ? -4.288 -22.338 21.557  1   73.602  ? 71  HIS   A C    1 ? 2 
ATOM   2667 O O    . HIS   B 1 59  ? -5.027 -23.207 21.094  1   69.517  ? 71  HIS   A O    1 ? 2 
ATOM   2668 C CB   . HIS   B 1 59  ? -4.257 -22.332 24.082  1   65.758  ? 71  HIS   A CB   1 ? 2 
ATOM   2669 C CG   . HIS   B 1 59  ? -3.647 -23.017 25.26   1   66.621  ? 71  HIS   A CG   1 ? 2 
ATOM   2670 N ND1  . HIS   B 1 59  ? -2.973 -22.345 26.255  1   62.864  ? 71  HIS   A ND1  1 ? 2 
ATOM   2671 C CD2  . HIS   B 1 59  ? -3.654 -24.313 25.607  1   70.501  ? 71  HIS   A CD2  1 ? 2 
ATOM   2672 C CE1  . HIS   B 1 59  ? -2.561 -23.21  27.16   1   67.733  ? 71  HIS   A CE1  1 ? 2 
ATOM   2673 N NE2  . HIS   B 1 59  ? -2.962 -24.415 26.785  1   74.363  ? 71  HIS   A NE2  1 ? 2 
ATOM   2674 H H    . HIS   B 1 59  ? -2.043 -21.303 23.452  1   61.349  ? 71  HIS   A H    1 c 2 
ATOM   2675 H HA   . HIS   B 1 59  ? -3.262 -23.601 22.807  1   68.636  ? 71  HIS   A HA   1 c 2 
ATOM   2676 H HB2  . HIS   B 1 59  ? -4.264 -21.363 24.236  1   65.205  ? 71  HIS   A HB2  1 c 2 
ATOM   2677 H HB3  . HIS   B 1 59  ? -5.182 -22.643 23.969  1   68.963  ? 71  HIS   A HB3  1 c 2 
ATOM   2678 H HD1  . HIS   B 1 59  ? -2.808 -21.416 26.261  0   30      ? 71  HIS   A HD1  1 c 2 
ATOM   2679 H HD2  . HIS   B 1 59  ? -4.038 -25.022 25.13   1   73.502  ? 71  HIS   A HD2  1 c 2 
ATOM   2680 H HE1  . HIS   B 1 59  ? -2.07  -23.008 27.932  1   66.066  ? 71  HIS   A HE1  1 c 2 
ATOM   2681 H HE2  . HIS   B 1 59  ? -2.784 -25.082 27.285  0   30      ? 71  HIS   A HE2  1 c 2 
ATOM   2682 N N    . ASP   B 1 60  ? -4.137 -21.122 21.016  1   76.602  ? 72  ASP   A N    1 ? 2 
ATOM   2683 C CA   . ASP   B 1 60  ? -4.709 -20.75  19.724  1   86.062  ? 72  ASP   A CA   1 ? 2 
ATOM   2684 C C    . ASP   B 1 60  ? -4.41  -21.81  18.661  1   87.256  ? 72  ASP   A C    1 ? 2 
ATOM   2685 O O    . ASP   B 1 60  ? -5.231 -22.035 17.785  1   91.047  ? 72  ASP   A O    1 ? 2 
ATOM   2686 C CB   . ASP   B 1 60  ? -4.155 -19.425 19.204  1   80.886  ? 72  ASP   A CB   1 ? 2 
ATOM   2687 C CG   . ASP   B 1 60  ? -4.399 -18.209 20.085  1   76.738  ? 72  ASP   A CG   1 ? 2 
ATOM   2688 O OD1  . ASP   B 1 60  ? -5.484 -18.152 20.702  1   80.805  ? 72  ASP   A OD1  1 ? 2 
ATOM   2689 O OD2  . ASP   B 1 60  ? -3.516 -17.323 20.113  1   71.956  ? 72  ASP   A OD2  1 ? 2 
ATOM   2690 H H    . ASP   B 1 60  ? -3.659 -20.493 21.476  1   74.699  ? 72  ASP   A H    1 c 2 
ATOM   2691 H HA   . ASP   B 1 60  ? -5.684 -20.669 19.826  1   85.413  ? 72  ASP   A HA   1 c 2 
ATOM   2692 H HB2  . ASP   B 1 60  ? -3.19  -19.518 19.065  1   79.608  ? 72  ASP   A HB2  1 c 2 
ATOM   2693 H HB3  . ASP   B 1 60  ? -4.562 -19.244 18.332  1   82.966  ? 72  ASP   A HB3  1 c 2 
ATOM   2694 N N    . ARG   B 1 61  ? -3.211 -22.407 18.72   1   84.526  ? 73  ARG   A N    1 ? 2 
ATOM   2695 C CA   . ARG   B 1 61  ? -2.765 -23.401 17.76   1   86.117  ? 73  ARG   A CA   1 ? 2 
ATOM   2696 C C    . ARG   B 1 61  ? -3.114 -24.819 18.238  1   93.356  ? 73  ARG   A C    1 ? 2 
ATOM   2697 O O    . ARG   B 1 61  ? -2.792 -25.789 17.558  1   93.995  ? 73  ARG   A O    1 ? 2 
ATOM   2698 C CB   . ARG   B 1 61  ? -1.26  -23.183 17.551  1   82.72   ? 73  ARG   A CB   1 ? 2 
ATOM   2699 H H    . ARG   B 1 61  ? -2.639 -22.17  19.392  1   82.205  ? 73  ARG   A H    1 c 2 
ATOM   2700 H HA   . ARG   B 1 61  ? -3.228 -23.236 16.9    1   88.919  ? 73  ARG   A HA   1 c 2 
ATOM   2701 H HB2  . ARG   B 1 61  ? -0.812 -23.777 18.141  0   30      ? 73  ARG   A HB2  1 c 2 
ATOM   2702 H HB3  . ARG   B 1 61  ? -1.181 -22.647 16.712  0   30      ? 73  ARG   A HB3  1 c 2 
ATOM   2703 N N    . ASN   B 1 62  ? -3.77  -24.955 19.404  1   89.37   ? 74  ASN   A N    1 ? 2 
ATOM   2704 C CA   . ASN   B 1 62  ? -4.051 -26.252 20      1   90.314  ? 74  ASN   A CA   1 ? 2 
ATOM   2705 C C    . ASN   B 1 62  ? -2.817 -27.166 19.929  1   88.554  ? 74  ASN   A C    1 ? 2 
ATOM   2706 O O    . ASN   B 1 62  ? -2.93  -28.35  19.628  1   92.742  ? 74  ASN   A O    1 ? 2 
ATOM   2707 C CB   . ASN   B 1 62  ? -5.306 -26.877 19.379  1   93.089  ? 74  ASN   A CB   1 ? 2 
ATOM   2708 H H    . ASN   B 1 62  ? -4.059 -24.209 19.841  1   88.258  ? 74  ASN   A H    1 c 2 
ATOM   2709 H HA   . ASN   B 1 62  ? -4.25  -26.1   20.952  1   88.586  ? 74  ASN   A HA   1 c 2 
ATOM   2710 H HB2  . ASN   B 1 62  ? -5.03  -27.565 18.677  0   30      ? 74  ASN   A HB2  1 c 2 
ATOM   2711 H HB3  . ASN   B 1 62  ? -6.098 -26.503 19.746  0   30      ? 74  ASN   A HB3  1 c 2 
ATOM   2712 N N    . GLU   B 1 63  ? -1.623 -26.646 20.242  1   86.175  ? 75  GLU   A N    1 ? 2 
ATOM   2713 C CA   . GLU   B 1 63  ? -0.442 -27.499 20.331  1   88.36   ? 75  GLU   A CA   1 ? 2 
ATOM   2714 C C    . GLU   B 1 63  ? 0.627  -26.826 21.187  1   82.082  ? 75  GLU   A C    1 ? 2 
ATOM   2715 O O    . GLU   B 1 63  ? 0.72   -25.603 21.175  1   80.476  ? 75  GLU   A O    1 ? 2 
ATOM   2716 C CB   . GLU   B 1 63  ? 0.145  -27.83  18.957  1   87.603  ? 75  GLU   A CB   1 ? 2 
ATOM   2717 H H    . GLU   B 1 63  ? -1.542 -25.751 20.411  1   84.125  ? 75  GLU   A H    1 c 2 
ATOM   2718 H HA   . GLU   B 1 63  ? -0.709 -28.346 20.768  1   88.721  ? 75  GLU   A HA   1 c 2 
ATOM   2719 H HB2  . GLU   B 1 63  ? 1.092  -27.851 19.036  0   30      ? 75  GLU   A HB2  1 c 2 
ATOM   2720 H HB3  . GLU   B 1 63  ? -0.63  -28.026 18.365  0   30      ? 75  GLU   A HB3  1 c 2 
ATOM   2721 N N    . PRO   B 1 64  ? 1.46   -27.587 21.946  1   80.323  ? 76  PRO   A N    1 ? 2 
ATOM   2722 C CA   . PRO   B 1 64  ? 2.594  -26.996 22.648  1   75.056  ? 76  PRO   A CA   1 ? 2 
ATOM   2723 C C    . PRO   B 1 64  ? 3.539  -26.282 21.694  1   71.625  ? 76  PRO   A C    1 ? 2 
ATOM   2724 O O    . PRO   B 1 64  ? 3.653  -26.677 20.539  1   72.561  ? 76  PRO   A O    1 ? 2 
ATOM   2725 C CB   . PRO   B 1 64  ? 3.308  -28.178 23.288  1   78.246  ? 76  PRO   A CB   1 ? 2 
ATOM   2726 C CG   . PRO   B 1 64  ? 2.243  -29.259 23.366  1   80.289  ? 76  PRO   A CG   1 ? 2 
ATOM   2727 C CD   . PRO   B 1 64  ? 1.352  -29.041 22.162  1   83.503  ? 76  PRO   A CD   1 ? 2 
ATOM   2728 H HA   . PRO   B 1 64  ? 2.274  -26.374 23.335  1   73.444  ? 76  PRO   A HA   1 c 2 
ATOM   2729 H HB2  . PRO   B 1 64  ? 4.062  -28.471 22.74   1   78.348  ? 76  PRO   A HB2  1 c 2 
ATOM   2730 H HB3  . PRO   B 1 64  ? 3.635  -27.947 24.18   1   75.828  ? 76  PRO   A HB3  1 c 2 
ATOM   2731 H HG2  . PRO   B 1 64  ? 2.648  -30.148 23.335  1   83.033  ? 76  PRO   A HG2  1 c 2 
ATOM   2732 H HG3  . PRO   B 1 64  ? 1.726  -29.178 24.192  1   80.36   ? 76  PRO   A HG3  1 c 2 
ATOM   2733 H HD2  . PRO   B 1 64  ? 1.676  -29.534 21.383  1   85.201  ? 76  PRO   A HD2  1 c 2 
ATOM   2734 H HD3  . PRO   B 1 64  ? 0.43   -29.299 22.352  1   84.667  ? 76  PRO   A HD3  1 c 2 
ATOM   2735 N N    . PHE   B 1 65  ? 4.194  -25.229 22.189  1   67.701  ? 77  PHE   A N    1 ? 2 
ATOM   2736 C CA   . PHE   B 1 65  ? 5.293  -24.585 21.498  1   64.321  ? 77  PHE   A CA   1 ? 2 
ATOM   2737 C C    . PHE   B 1 65  ? 6.612  -25.238 21.906  1   63.665  ? 77  PHE   A C    1 ? 2 
ATOM   2738 O O    . PHE   B 1 65  ? 6.889  -25.34  23.093  1   57.622  ? 77  PHE   A O    1 ? 2 
ATOM   2739 C CB   . PHE   B 1 65  ? 5.257  -23.114 21.9    1   61.274  ? 77  PHE   A CB   1 ? 2 
ATOM   2740 C CG   . PHE   B 1 65  ? 6.296  -22.288 21.169  1   60.316  ? 77  PHE   A CG   1 ? 2 
ATOM   2741 C CD1  . PHE   B 1 65  ? 6.034  -21.79  19.9    1   62.927  ? 77  PHE   A CD1  1 ? 2 
ATOM   2742 C CD2  . PHE   B 1 65  ? 7.522  -22.01  21.752  1   58.421  ? 77  PHE   A CD2  1 ? 2 
ATOM   2743 C CE1  . PHE   B 1 65  ? 6.981  -21.036 19.235  1   62.188  ? 77  PHE   A CE1  1 ? 2 
ATOM   2744 C CE2  . PHE   B 1 65  ? 8.457  -21.24  21.085  1   55.312  ? 77  PHE   A CE2  1 ? 2 
ATOM   2745 C CZ   . PHE   B 1 65  ? 8.173  -20.741 19.843  1   54.571  ? 77  PHE   A CZ   1 ? 2 
ATOM   2746 H H    . PHE   B 1 65  ? 3.94   -24.899 23.002  1   65.935  ? 77  PHE   A H    1 c 2 
ATOM   2747 H HA   . PHE   B 1 65  ? 5.164  -24.665 20.515  1   66.117  ? 77  PHE   A HA   1 c 2 
ATOM   2748 H HB2  . PHE   B 1 65  ? 4.363  -22.755 21.704  1   61.364  ? 77  PHE   A HB2  1 c 2 
ATOM   2749 H HB3  . PHE   B 1 65  ? 5.414  -23.047 22.868  1   59.982  ? 77  PHE   A HB3  1 c 2 
ATOM   2750 H HD1  . PHE   B 1 65  ? 5.205  -21.973 19.488  1   63.583  ? 77  PHE   A HD1  1 c 2 
ATOM   2751 H HD2  . PHE   B 1 65  ? 7.711  -22.333 22.619  1   57.329  ? 77  PHE   A HD2  1 c 2 
ATOM   2752 H HE1  . PHE   B 1 65  ? 6.791  -20.692 18.376  1   61.592  ? 77  PHE   A HE1  1 c 2 
ATOM   2753 H HE2  . PHE   B 1 65  ? 9.286  -21.049 21.492  1   54.866  ? 77  PHE   A HE2  1 c 2 
ATOM   2754 H HZ   . PHE   B 1 65  ? 8.823  -20.235 19.381  1   56.443  ? 77  PHE   A HZ   1 c 2 
ATOM   2755 N N    . VAL   B 1 66  ? 7.412  -25.667 20.919  1   65.536  ? 78  VAL   A N    1 ? 2 
ATOM   2756 C CA   . VAL   B 1 66  ? 8.663  -26.356 21.19   1   69.952  ? 78  VAL   A CA   1 ? 2 
ATOM   2757 C C    . VAL   B 1 66  ? 9.825  -25.541 20.629  1   68.32   ? 78  VAL   A C    1 ? 2 
ATOM   2758 O O    . VAL   B 1 66  ? 9.674  -24.926 19.58   1   71.905  ? 78  VAL   A O    1 ? 2 
ATOM   2759 C CB   . VAL   B 1 66  ? 8.64   -27.774 20.588  1   71.322  ? 78  VAL   A CB   1 ? 2 
ATOM   2760 C CG1  . VAL   B 1 66  ? 9.89   -28.557 20.989  1   71.128  ? 78  VAL   A CG1  1 ? 2 
ATOM   2761 C CG2  . VAL   B 1 66  ? 7.364  -28.534 20.961  1   75.958  ? 78  VAL   A CG2  1 ? 2 
ATOM   2762 H H    . VAL   B 1 66  ? 7.169  -25.524 20.049  1   67.262  ? 78  VAL   A H    1 c 2 
ATOM   2763 H HA   . VAL   B 1 66  ? 8.773  -26.432 22.155  1   67.48   ? 78  VAL   A HA   1 c 2 
ATOM   2764 H HB   . VAL   B 1 66  ? 8.652  -27.672 19.607  1   73.267  ? 78  VAL   A HB   1 c 2 
ATOM   2765 H HG11 . VAL   B 1 66  ? 9.999  -28.524 21.954  1   70.293  ? 78  VAL   A HG11 1 c 2 
ATOM   2766 H HG12 . VAL   B 1 66  ? 10.671 -28.167 20.563  1   71.493  ? 78  VAL   A HG12 1 c 2 
ATOM   2767 H HG13 . VAL   B 1 66  ? 9.798  -29.482 20.707  1   74.468  ? 78  VAL   A HG13 1 c 2 
ATOM   2768 H HG21 . VAL   B 1 66  ? 7.418  -29.444 20.623  1   77.813  ? 78  VAL   A HG21 1 c 2 
ATOM   2769 H HG22 . VAL   B 1 66  ? 6.593  -28.09  20.569  1   74.55   ? 78  VAL   A HG22 1 c 2 
ATOM   2770 H HG23 . VAL   B 1 66  ? 7.269  -28.554 21.928  1   73.761  ? 78  VAL   A HG23 1 c 2 
ATOM   2771 N N    . PHE   B 1 67  ? 10.971 -25.537 21.332  1   67.949  ? 79  PHE   A N    1 ? 2 
ATOM   2772 C CA   . PHE   B 1 67  ? 12.179 -24.86  20.87   1   62.939  ? 79  PHE   A CA   1 ? 2 
ATOM   2773 C C    . PHE   B 1 67  ? 13.407 -25.375 21.637  1   66.443  ? 79  PHE   A C    1 ? 2 
ATOM   2774 O O    . PHE   B 1 67  ? 13.27  -26.011 22.693  1   63.756  ? 79  PHE   A O    1 ? 2 
ATOM   2775 C CB   . PHE   B 1 67  ? 12     -23.348 21.034  1   57.739  ? 79  PHE   A CB   1 ? 2 
ATOM   2776 C CG   . PHE   B 1 67  ? 12.171 -22.843 22.459  1   53.041  ? 79  PHE   A CG   1 ? 2 
ATOM   2777 C CD1  . PHE   B 1 67  ? 11.147 -22.972 23.392  1   55.648  ? 79  PHE   A CD1  1 ? 2 
ATOM   2778 C CD2  . PHE   B 1 67  ? 13.37  -22.286 22.88   1   52.296  ? 79  PHE   A CD2  1 ? 2 
ATOM   2779 C CE1  . PHE   B 1 67  ? 11.326 -22.536 24.702  1   50.123  ? 79  PHE   A CE1  1 ? 2 
ATOM   2780 C CE2  . PHE   B 1 67  ? 13.542 -21.869 24.19   1   52.608  ? 79  PHE   A CE2  1 ? 2 
ATOM   2781 C CZ   . PHE   B 1 67  ? 12.521 -21.995 25.098  1   51.336  ? 79  PHE   A CZ   1 ? 2 
ATOM   2782 H H    . PHE   B 1 67  ? 10.997 -25.976 22.134  1   66.681  ? 79  PHE   A H    1 c 2 
ATOM   2783 H HA   . PHE   B 1 67  ? 12.302 -25.061 19.904  1   65.778  ? 79  PHE   A HA   1 c 2 
ATOM   2784 H HB2  . PHE   B 1 67  ? 12.654 -22.894 20.458  1   58.046  ? 79  PHE   A HB2  1 c 2 
ATOM   2785 H HB3  . PHE   B 1 67  ? 11.104 -23.101 20.717  1   57.355  ? 79  PHE   A HB3  1 c 2 
ATOM   2786 H HD1  . PHE   B 1 67  ? 10.324 -23.355 23.133  1   54.451  ? 79  PHE   A HD1  1 c 2 
ATOM   2787 H HD2  . PHE   B 1 67  ? 14.084 -22.207 22.268  1   53.935  ? 79  PHE   A HD2  1 c 2 
ATOM   2788 H HE1  . PHE   B 1 67  ? 10.622 -22.623 25.325  1   50.736  ? 79  PHE   A HE1  1 c 2 
ATOM   2789 H HE2  . PHE   B 1 67  ? 14.362 -21.484 24.455  1   51.958  ? 79  PHE   A HE2  1 c 2 
ATOM   2790 H HZ   . PHE   B 1 67  ? 12.634 -21.691 25.984  1   49.917  ? 79  PHE   A HZ   1 c 2 
ATOM   2791 N N    . SER   B 1 68  ? 14.604 -25.083 21.101  1   66.816  ? 80  SER   A N    1 ? 2 
ATOM   2792 C CA   . SER   B 1 68  ? 15.859 -25.534 21.686  1   67.413  ? 80  SER   A CA   1 ? 2 
ATOM   2793 C C    . SER   B 1 68  ? 16.49  -24.393 22.464  1   66.245  ? 80  SER   A C    1 ? 2 
ATOM   2794 O O    . SER   B 1 68  ? 16.777 -23.32  21.922  1   70.213  ? 80  SER   A O    1 ? 2 
ATOM   2795 C CB   . SER   B 1 68  ? 16.832 -26.069 20.66   1   75.738  ? 80  SER   A CB   1 ? 2 
ATOM   2796 O OG   . SER   B 1 68  ? 16.561 -27.419 20.321  1   78.016  ? 80  SER   A OG   1 ? 2 
ATOM   2797 H H    . SER   B 1 68  ? 14.635 -24.581 20.338  1   66.906  ? 80  SER   A H    1 c 2 
ATOM   2798 H HA   . SER   B 1 68  ? 15.653 -26.263 22.319  1   69.111  ? 80  SER   A HA   1 c 2 
ATOM   2799 H HB2  . SER   B 1 68  ? 16.782 -25.519 19.855  1   74.291  ? 80  SER   A HB2  1 c 2 
ATOM   2800 H HB3  . SER   B 1 68  ? 17.74  -26.003 21.013  1   74.899  ? 80  SER   A HB3  1 c 2 
ATOM   2801 H HG   . SER   B 1 68  ? 16.898 -27.656 19.616  0   30      ? 80  SER   A HG   1 c 2 
ATOM   2802 N N    . LEU   B 1 69  ? 16.688 -24.65  23.753  1   64.938  ? 81  LEU   A N    1 ? 2 
ATOM   2803 C CA   . LEU   B 1 69  ? 17.074 -23.611 24.682  1   59.62   ? 81  LEU   A CA   1 ? 2 
ATOM   2804 C C    . LEU   B 1 69  ? 18.463 -23.07  24.347  1   60.455  ? 81  LEU   A C    1 ? 2 
ATOM   2805 O O    . LEU   B 1 69  ? 19.393 -23.815 24.083  1   62.569  ? 81  LEU   A O    1 ? 2 
ATOM   2806 C CB   . LEU   B 1 69  ? 17.021 -24.168 26.097  1   60.965  ? 81  LEU   A CB   1 ? 2 
ATOM   2807 C CG   . LEU   B 1 69  ? 17.198 -23.129 27.204  1   61.821  ? 81  LEU   A CG   1 ? 2 
ATOM   2808 C CD1  . LEU   B 1 69  ? 15.958 -22.258 27.323  1   57.513  ? 81  LEU   A CD1  1 ? 2 
ATOM   2809 C CD2  . LEU   B 1 69  ? 17.485 -23.868 28.506  1   65.647  ? 81  LEU   A CD2  1 ? 2 
ATOM   2810 H H    . LEU   B 1 69  ? 16.586 -25.504 24.064  1   65.632  ? 81  LEU   A H    1 c 2 
ATOM   2811 H HA   . LEU   B 1 69  ? 16.42  -22.872 24.601  1   58.536  ? 81  LEU   A HA   1 c 2 
ATOM   2812 H HB2  . LEU   B 1 69  ? 16.152 -24.614 26.222  1   61.033  ? 81  LEU   A HB2  1 c 2 
ATOM   2813 H HB3  . LEU   B 1 69  ? 17.729 -24.847 26.188  1   63.435  ? 81  LEU   A HB3  1 c 2 
ATOM   2814 H HG   . LEU   B 1 69  ? 17.975 -22.554 26.984  1   61.66   ? 81  LEU   A HG   1 c 2 
ATOM   2815 H HD11 . LEU   B 1 69  ? 15.845 -21.739 26.51   1   57.502  ? 81  LEU   A HD11 1 c 2 
ATOM   2816 H HD12 . LEU   B 1 69  ? 16.057 -21.655 28.079  1   56.841  ? 81  LEU   A HD12 1 c 2 
ATOM   2817 H HD13 . LEU   B 1 69  ? 15.177 -22.821 27.459  1   57.917  ? 81  LEU   A HD13 1 c 2 
ATOM   2818 H HD21 . LEU   B 1 69  ? 18.335 -24.332 28.436  1   66.71   ? 81  LEU   A HD21 1 c 2 
ATOM   2819 H HD22 . LEU   B 1 69  ? 16.778 -24.511 28.669  1   64.951  ? 81  LEU   A HD22 1 c 2 
ATOM   2820 H HD23 . LEU   B 1 69  ? 17.521 -23.232 29.24   1   63.405  ? 81  LEU   A HD23 1 c 2 
ATOM   2821 N N    . GLY   B 1 70  ? 18.579 -21.74  24.347  1   62.238  ? 82  GLY   A N    1 ? 2 
ATOM   2822 C CA   . GLY   B 1 70  ? 19.862 -21.075 24.172  1   66.149  ? 82  GLY   A CA   1 ? 2 
ATOM   2823 C C    . GLY   B 1 70  ? 20.39  -21.179 22.743  1   70.757  ? 82  GLY   A C    1 ? 2 
ATOM   2824 O O    . GLY   B 1 70  ? 21.525 -20.793 22.49   1   76.532  ? 82  GLY   A O    1 ? 2 
ATOM   2825 H H    . GLY   B 1 70  ? 17.833 -21.228 24.465  1   59.964  ? 82  GLY   A H    1 c 2 
ATOM   2826 H HA2  . GLY   B 1 70  ? 19.765 -20.125 24.414  1   64.34   ? 82  GLY   A HA2  1 c 2 
ATOM   2827 H HA3  . GLY   B 1 70  ? 20.514 -21.475 24.789  1   67.051  ? 82  GLY   A HA3  1 c 2 
ATOM   2828 N N    . LYS   B 1 71  ? 19.551 -21.637 21.797  1   70.893  ? 83  LYS   A N    1 ? 2 
ATOM   2829 C CA   . LYS   B 1 71  ? 19.975 -21.769 20.416  1   74.634  ? 83  LYS   A CA   1 ? 2 
ATOM   2830 C C    . LYS   B 1 71  ? 19.392 -20.611 19.606  1   75.762  ? 83  LYS   A C    1 ? 2 
ATOM   2831 O O    . LYS   B 1 71  ? 19.301 -20.72  18.388  1   79.851  ? 83  LYS   A O    1 ? 2 
ATOM   2832 C CB   . LYS   B 1 71  ? 19.677 -23.175 19.872  1   74.974  ? 83  LYS   A CB   1 ? 2 
ATOM   2833 H H    . LYS   B 1 71  ? 18.69  -21.851 22.015  1   69.813  ? 83  LYS   A H    1 c 2 
ATOM   2834 H HA   . LYS   B 1 71  ? 20.961 -21.672 20.394  1   76.042  ? 83  LYS   A HA   1 c 2 
ATOM   2835 H HB2  . LYS   B 1 71  ? 20.548 -23.548 19.725  0   30      ? 83  LYS   A HB2  1 c 2 
ATOM   2836 H HB3  . LYS   B 1 71  ? 18.719 -23.236 19.844  0   30      ? 83  LYS   A HB3  1 c 2 
ATOM   2837 N N    . GLY   B 1 72  ? 18.959 -19.53  20.291  1   74.258  ? 84  GLY   A N    1 ? 2 
ATOM   2838 C CA   . GLY   B 1 72  ? 18.515 -18.281 19.676  1   73.174  ? 84  GLY   A CA   1 ? 2 
ATOM   2839 C C    . GLY   B 1 72  ? 17.247 -18.369 18.806  1   68.934  ? 84  GLY   A C    1 ? 2 
ATOM   2840 O O    . GLY   B 1 72  ? 17.017 -17.508 17.955  1   63.502  ? 84  GLY   A O    1 ? 2 
ATOM   2841 H H    . GLY   B 1 72  ? 18.935 -19.58  21.202  1   72.657  ? 84  GLY   A H    1 c 2 
ATOM   2842 H HA2  . GLY   B 1 72  ? 18.358 -17.624 20.394  1   70.5    ? 84  GLY   A HA2  1 c 2 
ATOM   2843 H HA3  . GLY   B 1 72  ? 19.252 -17.933 19.121  1   73.839  ? 84  GLY   A HA3  1 c 2 
ATOM   2844 N N    . GLN   B 1 73  ? 16.403 -19.374 19.042  1   62.05   ? 85  GLN   A N    1 ? 2 
ATOM   2845 C CA   . GLN   B 1 73  ? 15.195 -19.59  18.256  1   64.997  ? 85  GLN   A CA   1 ? 2 
ATOM   2846 C C    . GLN   B 1 73  ? 14.028 -18.739 18.761  1   61.571  ? 85  GLN   A C    1 ? 2 
ATOM   2847 O O    . GLN   B 1 73  ? 12.993 -18.609 18.109  1   69.026  ? 85  GLN   A O    1 ? 2 
ATOM   2848 C CB   . GLN   B 1 73  ? 14.827 -21.072 18.314  1   69.217  ? 85  GLN   A CB   1 ? 2 
ATOM   2849 C CG   . GLN   B 1 73  ? 15.932 -22.001 17.827  1   75.094  ? 85  GLN   A CG   1 ? 2 
ATOM   2850 C CD   . GLN   B 1 73  ? 15.509 -23.451 17.9    1   73.78   ? 85  GLN   A CD   1 ? 2 
ATOM   2851 O OE1  . GLN   B 1 73  ? 14.527 -23.807 18.559  1   73.345  ? 85  GLN   A OE1  1 ? 2 
ATOM   2852 N NE2  . GLN   B 1 73  ? 16.277 -24.317 17.266  1   76.297  ? 85  GLN   A NE2  1 ? 2 
ATOM   2853 H H    . GLN   B 1 73  ? 16.579 -19.947 19.732  1   64.19   ? 85  GLN   A H    1 c 2 
ATOM   2854 H HA   . GLN   B 1 73  ? 15.385 -19.346 17.314  1   66.273  ? 85  GLN   A HA   1 c 2 
ATOM   2855 H HB2  . GLN   B 1 73  ? 14.604 -21.301 19.241  1   67.825  ? 85  GLN   A HB2  1 c 2 
ATOM   2856 H HB3  . GLN   B 1 73  ? 14.025 -21.218 17.77   1   69.562  ? 85  GLN   A HB3  1 c 2 
ATOM   2857 H HG2  . GLN   B 1 73  ? 16.162 -21.779 16.899  1   75.242  ? 85  GLN   A HG2  1 c 2 
ATOM   2858 H HG3  . GLN   B 1 73  ? 16.735 -21.874 18.376  1   73.474  ? 85  GLN   A HG3  1 c 2 
ATOM   2859 H HE21 . GLN   B 1 73  ? 16.105 -25.185 17.325  1   78.089  ? 85  GLN   A HE21 1 c 2 
ATOM   2860 H HE22 . GLN   B 1 73  ? 16.963 -24.032 16.782  1   77.8    ? 85  GLN   A HE22 1 c 2 
ATOM   2861 N N    . VAL   B 1 74  ? 14.224 -18.123 19.926  1   51.546  ? 86  VAL   A N    1 ? 2 
ATOM   2862 C CA   . VAL   B 1 74  ? 13.229 -17.309 20.583  1   50.103  ? 86  VAL   A CA   1 ? 2 
ATOM   2863 C C    . VAL   B 1 74  ? 13.968 -16.065 21.015  1   47.135  ? 86  VAL   A C    1 ? 2 
ATOM   2864 O O    . VAL   B 1 74  ? 15.184 -16.029 20.909  1   50.271  ? 86  VAL   A O    1 ? 2 
ATOM   2865 C CB   . VAL   B 1 74  ? 12.632 -18.07  21.786  1   45.808  ? 86  VAL   A CB   1 ? 2 
ATOM   2866 C CG1  . VAL   B 1 74  ? 11.748 -19.214 21.327  1   49.765  ? 86  VAL   A CG1  1 ? 2 
ATOM   2867 C CG2  . VAL   B 1 74  ? 13.717 -18.631 22.679  1   45.507  ? 86  VAL   A CG2  1 ? 2 
ATOM   2868 H H    . VAL   B 1 74  ? 15.034 -18.221 20.339  1   53.742  ? 86  VAL   A H    1 c 2 
ATOM   2869 H HA   . VAL   B 1 74  ? 12.523 -17.073 19.952  1   49.271  ? 86  VAL   A HA   1 c 2 
ATOM   2870 H HB   . VAL   B 1 74  ? 12.087 -17.433 22.305  1   45.399  ? 86  VAL   A HB   1 c 2 
ATOM   2871 H HG11 . VAL   B 1 74  ? 12.273 -19.842 20.804  1   50.538  ? 86  VAL   A HG11 1 c 2 
ATOM   2872 H HG12 . VAL   B 1 74  ? 11.023 -18.866 20.781  1   48.949  ? 86  VAL   A HG12 1 c 2 
ATOM   2873 H HG13 . VAL   B 1 74  ? 11.378 -19.669 22.102  1   48.343  ? 86  VAL   A HG13 1 c 2 
ATOM   2874 H HG21 . VAL   B 1 74  ? 13.313 -19.015 23.475  1   45.014  ? 86  VAL   A HG21 1 c 2 
ATOM   2875 H HG22 . VAL   B 1 74  ? 14.327 -17.921 22.939  1   45.288  ? 86  VAL   A HG22 1 c 2 
ATOM   2876 H HG23 . VAL   B 1 74  ? 14.208 -19.321 22.203  1   47.318  ? 86  VAL   A HG23 1 c 2 
ATOM   2877 N N    . ILE   B 1 75  ? 13.234 -15.098 21.549  1   46.012  ? 87  ILE   A N    1 ? 2 
ATOM   2878 C CA   . ILE   B 1 75  ? 13.868 -13.896 22.043  1   47.358  ? 87  ILE   A CA   1 ? 2 
ATOM   2879 C C    . ILE   B 1 75  ? 14.759 -14.245 23.25   1   51.589  ? 87  ILE   A C    1 ? 2 
ATOM   2880 O O    . ILE   B 1 75  ? 14.51  -15.227 23.972  1   47.122  ? 87  ILE   A O    1 ? 2 
ATOM   2881 C CB   . ILE   B 1 75  ? 12.806 -12.832 22.379  1   47.462  ? 87  ILE   A CB   1 ? 2 
ATOM   2882 C CG1  . ILE   B 1 75  ? 11.725 -13.366 23.323  1   45.362  ? 87  ILE   A CG1  1 ? 2 
ATOM   2883 C CG2  . ILE   B 1 75  ? 12.195 -12.27  21.099  1   47.543  ? 87  ILE   A CG2  1 ? 2 
ATOM   2884 C CD1  . ILE   B 1 75  ? 10.833 -12.284 23.906  1   50.283  ? 87  ILE   A CD1  1 ? 2 
ATOM   2885 H H    . ILE   B 1 75  ? 12.326 -15.183 21.592  1   45.809  ? 87  ILE   A H    1 c 2 
ATOM   2886 H HA   . ILE   B 1 75  ? 14.438 -13.54  21.334  1   49.139  ? 87  ILE   A HA   1 c 2 
ATOM   2887 H HB   . ILE   B 1 75  ? 13.26  -12.1   22.838  1   46.786  ? 87  ILE   A HB   1 c 2 
ATOM   2888 H HG12 . ILE   B 1 75  ? 11.164 -14.002 22.835  1   46.988  ? 87  ILE   A HG12 1 c 2 
ATOM   2889 H HG13 . ILE   B 1 75  ? 12.155 -13.848 24.058  1   46.347  ? 87  ILE   A HG13 1 c 2 
ATOM   2890 H HG21 . ILE   B 1 75  ? 11.598 -11.534 21.316  1   47.483  ? 87  ILE   A HG21 1 c 2 
ATOM   2891 H HG22 . ILE   B 1 75  ? 11.694 -12.967 20.644  1   48.12   ? 87  ILE   A HG22 1 c 2 
ATOM   2892 H HG23 . ILE   B 1 75  ? 12.902 -11.948 20.514  1   48.937  ? 87  ILE   A HG23 1 c 2 
ATOM   2893 H HD11 . ILE   B 1 75  ? 11.385 -11.591 24.315  1   48.497  ? 87  ILE   A HD11 1 c 2 
ATOM   2894 H HD12 . ILE   B 1 75  ? 10.249 -12.675 24.583  1   47.799  ? 87  ILE   A HD12 1 c 2 
ATOM   2895 H HD13 . ILE   B 1 75  ? 10.289 -11.89  23.198  1   48.962  ? 87  ILE   A HD13 1 c 2 
ATOM   2896 N N    . LYS   B 1 76  ? 15.81  -13.437 23.416  1   46.537  ? 88  LYS   A N    1 ? 2 
ATOM   2897 C CA   . LYS   B 1 76  ? 16.787 -13.565 24.499  1   48.746  ? 88  LYS   A CA   1 ? 2 
ATOM   2898 C C    . LYS   B 1 76  ? 16.085 -13.815 25.841  1   43.849  ? 88  LYS   A C    1 ? 2 
ATOM   2899 O O    . LYS   B 1 76  ? 16.476 -14.745 26.55   1   44.868  ? 88  LYS   A O    1 ? 2 
ATOM   2900 C CB   . LYS   B 1 76  ? 17.67  -12.302 24.429  1   50.562  ? 88  LYS   A CB   1 ? 2 
ATOM   2901 H H    . LYS   B 1 76  ? 15.925 -12.76  22.813  1   48.921  ? 88  LYS   A H    1 c 2 
ATOM   2902 H HA   . LYS   B 1 76  ? 17.361 -14.349 24.301  1   48.788  ? 88  LYS   A HA   1 c 2 
ATOM   2903 H HB2  . LYS   B 1 76  ? 18.528 -12.467 24.503  0   30      ? 88  LYS   A HB2  1 c 2 
ATOM   2904 H HB3  . LYS   B 1 76  ? 16.963 -11.464 24.504  0   30      ? 88  LYS   A HB3  1 c 2 
ATOM   2905 N N    . ALA   B 1 77  ? 15.047 -13.023 26.183  1   41.281  ? 89  ALA   A N    1 ? 2 
ATOM   2906 C CA   . ALA   B 1 77  ? 14.333 -13.192 27.439  1   39.797  ? 89  ALA   A CA   1 ? 2 
ATOM   2907 C C    . ALA   B 1 77  ? 13.792 -14.603 27.637  1   40.816  ? 89  ALA   A C    1 ? 2 
ATOM   2908 O O    . ALA   B 1 77  ? 13.702 -15.046 28.778  1   38.766  ? 89  ALA   A O    1 ? 2 
ATOM   2909 C CB   . ALA   B 1 77  ? 13.202 -12.216 27.6    1   39.853  ? 89  ALA   A CB   1 ? 2 
ATOM   2910 H H    . ALA   B 1 77  ? 14.782 -12.361 25.611  1   41.697  ? 89  ALA   A H    1 c 2 
ATOM   2911 H HA   . ALA   B 1 77  ? 14.989 -13.024 28.172  1   40.581  ? 89  ALA   A HA   1 c 2 
ATOM   2912 H HB1  . ALA   B 1 77  ? 13.549 -11.308 27.591  1   40.113  ? 89  ALA   A HB1  1 c 2 
ATOM   2913 H HB2  . ALA   B 1 77  ? 12.571 -12.325 26.868  1   39.519  ? 89  ALA   A HB2  1 c 2 
ATOM   2914 H HB3  . ALA   B 1 77  ? 12.746 -12.377 28.443  1   39.095  ? 89  ALA   A HB3  1 c 2 
ATOM   2915 N N    . TRP   B 1 78  ? 13.373 -15.282 26.563  1   41.293  ? 90  TRP   A N    1 ? 2 
ATOM   2916 C CA   . TRP   B 1 78  ? 12.924 -16.656 26.718  1   43.791  ? 90  TRP   A CA   1 ? 2 
ATOM   2917 C C    . TRP   B 1 78  ? 14.08  -17.591 27.029  1   48.033  ? 90  TRP   A C    1 ? 2 
ATOM   2918 O O    . TRP   B 1 78  ? 13.934 -18.502 27.867  1   42.945  ? 90  TRP   A O    1 ? 2 
ATOM   2919 C CB   . TRP   B 1 78  ? 12.147 -17.148 25.503  1   46.401  ? 90  TRP   A CB   1 ? 2 
ATOM   2920 C CG   . TRP   B 1 78  ? 10.672 -16.904 25.561  1   45.837  ? 90  TRP   A CG   1 ? 2 
ATOM   2921 C CD1  . TRP   B 1 78  ? 10.003 -15.76  25.88   1   44.345  ? 90  TRP   A CD1  1 ? 2 
ATOM   2922 C CD2  . TRP   B 1 78  ? 9.661  -17.908 25.325  1   45.814  ? 90  TRP   A CD2  1 ? 2 
ATOM   2923 N NE1  . TRP   B 1 78  ? 8.652  -15.97  25.794  1   44.655  ? 90  TRP   A NE1  1 ? 2 
ATOM   2924 C CE2  . TRP   B 1 78  ? 8.407  -17.28  25.493  1   41.921  ? 90  TRP   A CE2  1 ? 2 
ATOM   2925 C CE3  . TRP   B 1 78  ? 9.701  -19.265 24.999  1   47.778  ? 90  TRP   A CE3  1 ? 2 
ATOM   2926 C CZ2  . TRP   B 1 78  ? 7.192  -17.956 25.328  1   40.712  ? 90  TRP   A CZ2  1 ? 2 
ATOM   2927 C CZ3  . TRP   B 1 78  ? 8.504  -19.942 24.88   1   48.405  ? 90  TRP   A CZ3  1 ? 2 
ATOM   2928 C CH2  . TRP   B 1 78  ? 7.27   -19.276 24.974  1   42.527  ? 90  TRP   A CH2  1 ? 2 
ATOM   2929 H H    . TRP   B 1 78  ? 13.363 -14.891 25.737  1   42.165  ? 90  TRP   A H    1 c 2 
ATOM   2930 H HA   . TRP   B 1 78  ? 12.302 -16.68  27.494  1   43.511  ? 90  TRP   A HA   1 c 2 
ATOM   2931 H HB2  . TRP   B 1 78  ? 12.507 -16.71  24.703  1   46.398  ? 90  TRP   A HB2  1 c 2 
ATOM   2932 H HB3  . TRP   B 1 78  ? 12.302 -18.111 25.404  1   46.776  ? 90  TRP   A HB3  1 c 2 
ATOM   2933 H HD1  . TRP   B 1 78  ? 10.403 -14.925 26.061  1   44.209  ? 90  TRP   A HD1  1 c 2 
ATOM   2934 H HE1  . TRP   B 1 78  ? 8.044  -15.373 25.96   1   43.385  ? 90  TRP   A HE1  1 c 2 
ATOM   2935 H HE3  . TRP   B 1 78  ? 10.524 -19.713 24.901  1   48.255  ? 90  TRP   A HE3  1 c 2 
ATOM   2936 H HZ2  . TRP   B 1 78  ? 6.364  -17.517 25.425  1   41.199  ? 90  TRP   A HZ2  1 c 2 
ATOM   2937 H HZ3  . TRP   B 1 78  ? 8.516  -20.851 24.632  1   48.338  ? 90  TRP   A HZ3  1 c 2 
ATOM   2938 H HH2  . TRP   B 1 78  ? 6.475  -19.772 24.889  1   44.371  ? 90  TRP   A HH2  1 c 2 
ATOM   2939 N N    . ASP   B 1 79  ? 15.204 -17.424 26.321  1   44.407  ? 91  ASP   A N    1 ? 2 
ATOM   2940 C CA   . ASP   B 1 79  ? 16.341 -18.293 26.535  1   46.146  ? 91  ASP   A CA   1 ? 2 
ATOM   2941 C C    . ASP   B 1 79  ? 16.828 -18.103 27.973  1   46.8    ? 91  ASP   A C    1 ? 2 
ATOM   2942 O O    . ASP   B 1 79  ? 17.148 -19.067 28.656  1   48.052  ? 91  ASP   A O    1 ? 2 
ATOM   2943 C CB   . ASP   B 1 79  ? 17.443 -18.015 25.524  1   48.297  ? 91  ASP   A CB   1 ? 2 
ATOM   2944 C CG   . ASP   B 1 79  ? 17.333 -18.738 24.187  1   49.116  ? 91  ASP   A CG   1 ? 2 
ATOM   2945 O OD1  . ASP   B 1 79  ? 16.652 -19.79  24.153  1   55.017  ? 91  ASP   A OD1  1 ? 2 
ATOM   2946 O OD2  . ASP   B 1 79  ? 17.952 -18.262 23.205  1   52.774  ? 91  ASP   A OD2  1 ? 2 
ATOM   2947 H H    . ASP   B 1 79  ? 15.257 -16.764 25.691  1   45.492  ? 91  ASP   A H    1 c 2 
ATOM   2948 H HA   . ASP   B 1 79  ? 16.044 -19.224 26.427  1   47.012  ? 91  ASP   A HA   1 c 2 
ATOM   2949 H HB2  . ASP   B 1 79  ? 17.472 -17.052 25.345  1   47.496  ? 91  ASP   A HB2  1 c 2 
ATOM   2950 H HB3  . ASP   B 1 79  ? 18.302 -18.265 25.925  1   49.113  ? 91  ASP   A HB3  1 c 2 
ATOM   2951 N N    . ILE   B 1 80  ? 16.79  -16.863 28.463  1   48.662  ? 92  ILE   A N    1 ? 2 
ATOM   2952 C CA   . ILE   B 1 80  ? 17.194 -16.568 29.83   1   49.767  ? 92  ILE   A CA   1 ? 2 
ATOM   2953 C C    . ILE   B 1 80  ? 16.148 -17.107 30.789  1   44.306  ? 92  ILE   A C    1 ? 2 
ATOM   2954 O O    . ILE   B 1 80  ? 16.48  -17.809 31.727  1   42.566  ? 92  ILE   A O    1 ? 2 
ATOM   2955 C CB   . ILE   B 1 80  ? 17.43  -15.059 30.011  1   52.897  ? 92  ILE   A CB   1 ? 2 
ATOM   2956 C CG1  . ILE   B 1 80  ? 18.687 -14.607 29.274  1   55.952  ? 92  ILE   A CG1  1 ? 2 
ATOM   2957 C CG2  . ILE   B 1 80  ? 17.503 -14.69  31.485  1   60.161  ? 92  ILE   A CG2  1 ? 2 
ATOM   2958 C CD1  . ILE   B 1 80  ? 18.677 -13.11  29.031  1   58.907  ? 92  ILE   A CD1  1 ? 2 
ATOM   2959 H H    . ILE   B 1 80  ? 16.513 -16.175 27.928  1   47.702  ? 92  ILE   A H    1 c 2 
ATOM   2960 H HA   . ILE   B 1 80  ? 18.038 -17.029 30.005  1   50.477  ? 92  ILE   A HA   1 c 2 
ATOM   2961 H HB   . ILE   B 1 80  ? 16.667 -14.588 29.62   1   52.76   ? 92  ILE   A HB   1 c 2 
ATOM   2962 H HG12 . ILE   B 1 80  ? 19.475 -14.843 29.805  1   57.455  ? 92  ILE   A HG12 1 c 2 
ATOM   2963 H HG13 . ILE   B 1 80  ? 18.745 -15.073 28.415  1   56.619  ? 92  ILE   A HG13 1 c 2 
ATOM   2964 H HG21 . ILE   B 1 80  ? 17.808 -13.772 31.578  1   58.146  ? 92  ILE   A HG21 1 c 2 
ATOM   2965 H HG22 . ILE   B 1 80  ? 18.126 -15.282 31.938  1   58.807  ? 92  ILE   A HG22 1 c 2 
ATOM   2966 H HG23 . ILE   B 1 80  ? 16.624 -14.777 31.889  1   56.8    ? 92  ILE   A HG23 1 c 2 
ATOM   2967 H HD11 . ILE   B 1 80  ? 17.862 -12.863 28.554  1   56.98   ? 92  ILE   A HD11 1 c 2 
ATOM   2968 H HD12 . ILE   B 1 80  ? 19.453 -12.864 28.494  1   59.244  ? 92  ILE   A HD12 1 c 2 
ATOM   2969 H HD13 . ILE   B 1 80  ? 18.71  -12.635 29.882  1   58      ? 92  ILE   A HD13 1 c 2 
ATOM   2970 N N    . GLY   B 1 81  ? 14.883 -16.81  30.541  1   39.066  ? 93  GLY   A N    1 ? 2 
ATOM   2971 C CA   . GLY   B 1 81  ? 13.829 -17.072 31.499  1   40.043  ? 93  GLY   A CA   1 ? 2 
ATOM   2972 C C    . GLY   B 1 81  ? 13.467 -18.543 31.673  1   40.573  ? 93  GLY   A C    1 ? 2 
ATOM   2973 O O    . GLY   B 1 81  ? 13.254 -19.031 32.79   1   42.769  ? 93  GLY   A O    1 ? 2 
ATOM   2974 H H    . GLY   B 1 81  ? 14.663 -16.425 29.742  1   40.081  ? 93  GLY   A H    1 c 2 
ATOM   2975 H HA2  . GLY   B 1 81  ? 14.104 -16.71  32.37   1   39.833  ? 93  GLY   A HA2  1 c 2 
ATOM   2976 H HA3  . GLY   B 1 81  ? 13.024 -16.577 31.217  1   38.802  ? 93  GLY   A HA3  1 c 2 
ATOM   2977 N N    . VAL   B 1 82  ? 13.364 -19.244 30.551  1   39.168  ? 94  VAL   A N    1 ? 2 
ATOM   2978 C CA   . VAL   B 1 82  ? 12.969 -20.63  30.59   1   43.765  ? 94  VAL   A CA   1 ? 2 
ATOM   2979 C C    . VAL   B 1 82  ? 14.094 -21.466 31.221  1   44.71   ? 94  VAL   A C    1 ? 2 
ATOM   2980 O O    . VAL   B 1 82  ? 13.771 -22.466 31.875  1   44.879  ? 94  VAL   A O    1 ? 2 
ATOM   2981 C CB   . VAL   B 1 82  ? 12.501 -21.136 29.214  1   41.981  ? 94  VAL   A CB   1 ? 2 
ATOM   2982 C CG1  . VAL   B 1 82  ? 12.297 -22.649 29.193  1   52.885  ? 94  VAL   A CG1  1 ? 2 
ATOM   2983 C CG2  . VAL   B 1 82  ? 11.201 -20.48  28.825  1   45.39   ? 94  VAL   A CG2  1 ? 2 
ATOM   2984 H H    . VAL   B 1 82  ? 13.539 -18.852 29.744  1   40.246  ? 94  VAL   A H    1 c 2 
ATOM   2985 H HA   . VAL   B 1 82  ? 12.2   -20.689 31.189  1   42.12   ? 94  VAL   A HA   1 c 2 
ATOM   2986 H HB   . VAL   B 1 82  ? 13.192 -20.898 28.553  1   45.06   ? 94  VAL   A HB   1 c 2 
ATOM   2987 H HG11 . VAL   B 1 82  ? 11.775 -22.917 29.968  1   49.911  ? 94  VAL   A HG11 1 c 2 
ATOM   2988 H HG12 . VAL   B 1 82  ? 13.16  -23.096 29.213  1   51.122  ? 94  VAL   A HG12 1 c 2 
ATOM   2989 H HG13 . VAL   B 1 82  ? 11.823 -22.899 28.383  1   50.407  ? 94  VAL   A HG13 1 c 2 
ATOM   2990 H HG21 . VAL   B 1 82  ? 10.924 -20.799 27.949  1   44.5    ? 94  VAL   A HG21 1 c 2 
ATOM   2991 H HG22 . VAL   B 1 82  ? 11.32  -19.516 28.794  1   42.927  ? 94  VAL   A HG22 1 c 2 
ATOM   2992 H HG23 . VAL   B 1 82  ? 10.517 -20.7   29.48   1   43.758  ? 94  VAL   A HG23 1 c 2 
ATOM   2993 N N    . ALA   B 1 83  ? 15.382 -21.037 31.098  1   44.087  ? 95  ALA   A N    1 ? 2 
ATOM   2994 C CA   . ALA   B 1 83  ? 16.47  -21.757 31.738  1   43.79   ? 95  ALA   A CA   1 ? 2 
ATOM   2995 C C    . ALA   B 1 83  ? 16.312 -21.767 33.249  1   46.384  ? 95  ALA   A C    1 ? 2 
ATOM   2996 O O    . ALA   B 1 83  ? 16.939 -22.577 33.889  1   48.896  ? 95  ALA   A O    1 ? 2 
ATOM   2997 C CB   . ALA   B 1 83  ? 17.872 -21.237 31.392  1   48.561  ? 95  ALA   A CB   1 ? 2 
ATOM   2998 H H    . ALA   B 1 83  ? 15.572 -20.293 30.603  1   43.175  ? 95  ALA   A H    1 c 2 
ATOM   2999 H HA   . ALA   B 1 83  ? 16.413 -22.704 31.431  1   46.618  ? 95  ALA   A HA   1 c 2 
ATOM   3000 H HB1  . ALA   B 1 83  ? 18.005 -21.267 30.43   1   47.758  ? 95  ALA   A HB1  1 c 2 
ATOM   3001 H HB2  . ALA   B 1 83  ? 17.965 -20.319 31.699  1   46.494  ? 95  ALA   A HB2  1 c 2 
ATOM   3002 H HB3  . ALA   B 1 83  ? 18.543 -21.79  31.826  1   49.071  ? 95  ALA   A HB3  1 c 2 
ATOM   3003 N N    . THR   B 1 84  ? 15.548 -20.818 33.812  1   47.739  ? 96  THR   A N    1 ? 2 
ATOM   3004 C CA   . THR   B 1 84  ? 15.351 -20.745 35.246  1   47.905  ? 96  THR   A CA   1 ? 2 
ATOM   3005 C C    . THR   B 1 84  ? 14.165 -21.599 35.681  1   46.969  ? 96  THR   A C    1 ? 2 
ATOM   3006 O O    . THR   B 1 84  ? 13.937 -21.696 36.868  1   44.142  ? 96  THR   A O    1 ? 2 
ATOM   3007 C CB   . THR   B 1 84  ? 15.154 -19.292 35.71   1   48.05   ? 96  THR   A CB   1 ? 2 
ATOM   3008 O OG1  . THR   B 1 84  ? 13.855 -18.83  35.345  1   43.285  ? 96  THR   A OG1  1 ? 2 
ATOM   3009 C CG2  . THR   B 1 84  ? 16.234 -18.361 35.184  1   47.671  ? 96  THR   A CG2  1 ? 2 
ATOM   3010 H H    . THR   B 1 84  ? 15.149 -20.187 33.284  1   45.675  ? 96  THR   A H    1 c 2 
ATOM   3011 H HA   . THR   B 1 84  ? 16.158 -21.095 35.682  1   49.39   ? 96  THR   A HA   1 c 2 
ATOM   3012 H HB   . THR   B 1 84  ? 15.22  -19.28  36.695  1   47.739  ? 96  THR   A HB   1 c 2 
ATOM   3013 H HG1  . THR   B 1 84  ? 13.76  -18.86  34.556  0   30      ? 96  THR   A HG1  1 c 2 
ATOM   3014 H HG21 . THR   B 1 84  ? 16.151 -17.493 35.613  1   47.389  ? 96  THR   A HG21 1 c 2 
ATOM   3015 H HG22 . THR   B 1 84  ? 16.133 -18.257 34.224  1   47.134  ? 96  THR   A HG22 1 c 2 
ATOM   3016 H HG23 . THR   B 1 84  ? 17.109 -18.736 35.378  1   49.164  ? 96  THR   A HG23 1 c 2 
ATOM   3017 N N    . MET   B 1 85  ? 13.364 -22.17  34.774  1   47.244  ? 97  MET   A N    1 ? 2 
ATOM   3018 C CA   . MET   B 1 85  ? 12.088 -22.73  35.214  1   47.275  ? 97  MET   A CA   1 ? 2 
ATOM   3019 C C    . MET   B 1 85  ? 12.196 -24.227 35.487  1   48.515  ? 97  MET   A C    1 ? 2 
ATOM   3020 O O    . MET   B 1 85  ? 13.043 -24.927 34.944  1   47.533  ? 97  MET   A O    1 ? 2 
ATOM   3021 C CB   . MET   B 1 85  ? 10.994 -22.49  34.169  1   45.416  ? 97  MET   A CB   1 ? 2 
ATOM   3022 C CG   . MET   B 1 85  ? 10.702 -20.999 33.982  1   41.893  ? 97  MET   A CG   1 ? 2 
ATOM   3023 S SD   . MET   B 1 85  ? 9.484  -20.792 32.666  1   44.499  ? 97  MET   A SD   1 ? 2 
ATOM   3024 C CE   . MET   B 1 85  ? 7.999  -21.447 33.442  1   46.884  ? 97  MET   A CE   1 ? 2 
ATOM   3025 H H    . MET   B 1 85  ? 13.602 -22.221 33.894  1   46.971  ? 97  MET   A H    1 c 2 
ATOM   3026 H HA   . MET   B 1 85  ? 11.827 -22.281 36.057  1   46.648  ? 97  MET   A HA   1 c 2 
ATOM   3027 H HB2  . MET   B 1 85  ? 11.278 -22.876 33.314  1   45.627  ? 97  MET   A HB2  1 c 2 
ATOM   3028 H HB3  . MET   B 1 85  ? 10.175 -22.949 34.454  1   45.766  ? 97  MET   A HB3  1 c 2 
ATOM   3029 H HG2  . MET   B 1 85  ? 10.353 -20.619 34.811  1   42.708  ? 97  MET   A HG2  1 c 2 
ATOM   3030 H HG3  . MET   B 1 85  ? 11.521 -20.526 33.744  1   42.574  ? 97  MET   A HG3  1 c 2 
ATOM   3031 H HE1  . MET   B 1 85  ? 7.258  -21.403 32.81   1   46.405  ? 97  MET   A HE1  1 c 2 
ATOM   3032 H HE2  . MET   B 1 85  ? 8.147  -22.375 33.7    1   47.71   ? 97  MET   A HE2  1 c 2 
ATOM   3033 H HE3  . MET   B 1 85  ? 7.785  -20.918 34.233  1   46.153  ? 97  MET   A HE3  1 c 2 
ATOM   3034 N N    . LYS   B 1 86  ? 11.302 -24.713 36.342  1   50.045  ? 98  LYS   A N    1 ? 2 
ATOM   3035 C CA   . LYS   B 1 86  ? 11.222 -26.13  36.663  1   55.479  ? 98  LYS   A CA   1 ? 2 
ATOM   3036 C C    . LYS   B 1 86  ? 10.015 -26.727 35.955  1   53.515  ? 98  LYS   A C    1 ? 2 
ATOM   3037 O O    . LYS   B 1 86  ? 9.119  -26.001 35.526  1   49.702  ? 98  LYS   A O    1 ? 2 
ATOM   3038 C CB   . LYS   B 1 86  ? 11.22  -26.338 38.175  1   57.676  ? 98  LYS   A CB   1 ? 2 
ATOM   3039 C CG   . LYS   B 1 86  ? 12.53  -26.006 38.836  1   64.042  ? 98  LYS   A CG   1 ? 2 
ATOM   3040 C CD   . LYS   B 1 86  ? 12.489 -26.022 40.357  1   76.827  ? 98  LYS   A CD   1 ? 2 
ATOM   3041 C CE   . LYS   B 1 86  ? 13.864 -25.994 40.937  1   82.46   ? 98  LYS   A CE   1 ? 2 
ATOM   3042 N NZ   . LYS   B 1 86  ? 14.524 -24.759 40.5    1   85.327  ? 98  LYS   A NZ   1 ? 2 
ATOM   3043 H H    . LYS   B 1 86  ? 10.714 -24.141 36.745  1   49.569  ? 98  LYS   A H    1 c 2 
ATOM   3044 H HA   . LYS   B 1 86  ? 12.033 -26.573 36.307  1   55.592  ? 98  LYS   A HA   1 c 2 
ATOM   3045 H HB2  . LYS   B 1 86  ? 10.518 -25.778 38.572  1   57.788  ? 98  LYS   A HB2  1 c 2 
ATOM   3046 H HB3  . LYS   B 1 86  ? 11.001 -27.275 38.367  1   60.718  ? 98  LYS   A HB3  1 c 2 
ATOM   3047 H HG2  . LYS   B 1 86  ? 13.205 -26.65  38.529  1   66.35   ? 98  LYS   A HG2  1 c 2 
ATOM   3048 H HG3  . LYS   B 1 86  ? 12.811 -25.115 38.534  1   63.253  ? 98  LYS   A HG3  1 c 2 
ATOM   3049 H HD2  . LYS   B 1 86  ? 11.986 -25.242 40.678  1   73.616  ? 98  LYS   A HD2  1 c 2 
ATOM   3050 H HD3  . LYS   B 1 86  ? 12.028 -26.832 40.659  1   76.614  ? 98  LYS   A HD3  1 c 2 
ATOM   3051 H HE2  . LYS   B 1 86  ? 13.821 -26.014 41.91   1   83.742  ? 98  LYS   A HE2  1 c 2 
ATOM   3052 H HE3  . LYS   B 1 86  ? 14.377 -26.762 40.628  1   84.104  ? 98  LYS   A HE3  1 c 2 
ATOM   3053 H HZ1  . LYS   B 1 86  ? 13.935 -24.069 40.494  1   81.962  ? 98  LYS   A HZ1  1 c 2 
ATOM   3054 H HZ2  . LYS   B 1 86  ? 14.867 -24.866 39.668  1   83.057  ? 98  LYS   A HZ2  1 c 2 
ATOM   3055 H HZ3  . LYS   B 1 86  ? 15.199 -24.561 41.07   1   84.563  ? 98  LYS   A HZ3  1 c 2 
ATOM   3056 N N    . LYS   B 1 87  ? 10.043 -28.048 35.777  1   54.027  ? 99  LYS   A N    1 ? 2 
ATOM   3057 C CA   . LYS   B 1 87  ? 8.976  -28.731 35.069  1   63.896  ? 99  LYS   A CA   1 ? 2 
ATOM   3058 C C    . LYS   B 1 87  ? 7.66   -28.496 35.812  1   65.811  ? 99  LYS   A C    1 ? 2 
ATOM   3059 O O    . LYS   B 1 87  ? 7.606  -28.531 37.037  1   59.079  ? 99  LYS   A O    1 ? 2 
ATOM   3060 C CB   . LYS   B 1 87  ? 9.271  -30.224 34.905  1   70.848  ? 99  LYS   A CB   1 ? 2 
ATOM   3061 C CG   . LYS   B 1 87  ? 8.24   -31.002 34.097  1   79.445  ? 99  LYS   A CG   1 ? 2 
ATOM   3062 C CD   . LYS   B 1 87  ? 8.86   -32.271 33.502  1   92.673  ? 99  LYS   A CD   1 ? 2 
ATOM   3063 C CE   . LYS   B 1 87  ? 7.976  -33.486 33.479  1   100.732 ? 99  LYS   A CE   1 ? 2 
ATOM   3064 N NZ   . LYS   B 1 87  ? 6.672  -33.24  32.855  1   103.705 ? 99  LYS   A NZ   1 ? 2 
ATOM   3065 H H    . LYS   B 1 87  ? 10.742 -28.536 36.106  1   57.881  ? 99  LYS   A H    1 c 2 
ATOM   3066 H HA   . LYS   B 1 87  ? 8.904  -28.33  34.166  1   61.579  ? 99  LYS   A HA   1 c 2 
ATOM   3067 H HB2  . LYS   B 1 87  ? 10.144 -30.321 34.468  1   71.962  ? 99  LYS   A HB2  1 c 2 
ATOM   3068 H HB3  . LYS   B 1 87  ? 9.337  -30.63  35.795  1   72.949  ? 99  LYS   A HB3  1 c 2 
ATOM   3069 H HG2  . LYS   B 1 87  ? 7.49   -31.245 34.682  1   80.742  ? 99  LYS   A HG2  1 c 2 
ATOM   3070 H HG3  . LYS   B 1 87  ? 7.902  -30.43  33.375  1   78.052  ? 99  LYS   A HG3  1 c 2 
ATOM   3071 H HD2  . LYS   B 1 87  ? 9.141  -32.072 32.584  1   90.391  ? 99  LYS   A HD2  1 c 2 
ATOM   3072 H HD3  . LYS   B 1 87  ? 9.672  -32.488 34.01   1   91.808  ? 99  LYS   A HD3  1 c 2 
ATOM   3073 H HE2  . LYS   B 1 87  ? 8.425  -34.201 32.994  1   102.802 ? 99  LYS   A HE2  1 c 2 
ATOM   3074 H HE3  . LYS   B 1 87  ? 7.831  -33.79  34.393  1   101.637 ? 99  LYS   A HE3  1 c 2 
ATOM   3075 H HZ1  . LYS   B 1 87  ? 6.781  -32.778 32.084  1   101.046 ? 99  LYS   A HZ1  1 c 2 
ATOM   3076 H HZ2  . LYS   B 1 87  ? 6.147  -32.761 33.418  1   101.042 ? 99  LYS   A HZ2  1 c 2 
ATOM   3077 H HZ3  . LYS   B 1 87  ? 6.266  -34.03  32.674  1   105.137 ? 99  LYS   A HZ3  1 c 2 
ATOM   3078 N N    . GLY   B 1 88  ? 6.624  -28.126 35.059  1   62.49   ? 100 GLY   A N    1 ? 2 
ATOM   3079 C CA   . GLY   B 1 88  ? 5.332  -27.824 35.654  1   58.444  ? 100 GLY   A CA   1 ? 2 
ATOM   3080 C C    . GLY   B 1 88  ? 5.25   -26.41  36.23   1   55.211  ? 100 GLY   A C    1 ? 2 
ATOM   3081 O O    . GLY   B 1 88  ? 4.191  -26.044 36.702  1   59.674  ? 100 GLY   A O    1 ? 2 
ATOM   3082 H H    . GLY   B 1 88  ? 6.72   -28.063 34.152  1   61.603  ? 100 GLY   A H    1 c 2 
ATOM   3083 H HA2  . GLY   B 1 88  ? 4.635  -27.933 34.966  1   59.539  ? 100 GLY   A HA2  1 c 2 
ATOM   3084 H HA3  . GLY   B 1 88  ? 5.149  -28.477 36.37   1   61.147  ? 100 GLY   A HA3  1 c 2 
ATOM   3085 N N    . GLU   B 1 89  ? 6.322  -25.605 36.191  1   55.598  ? 101 GLU   A N    1 ? 2 
ATOM   3086 C CA   . GLU   B 1 89  ? 6.274  -24.228 36.683  1   54.982  ? 101 GLU   A CA   1 ? 2 
ATOM   3087 C C    . GLU   B 1 89  ? 5.45   -23.366 35.724  1   50.43   ? 101 GLU   A C    1 ? 2 
ATOM   3088 O O    . GLU   B 1 89  ? 5.503  -23.545 34.495  1   52.778  ? 101 GLU   A O    1 ? 2 
ATOM   3089 C CB   . GLU   B 1 89  ? 7.686  -23.654 36.842  1   55.384  ? 101 GLU   A CB   1 ? 2 
ATOM   3090 C CG   . GLU   B 1 89  ? 7.79   -22.262 37.465  1   50.82   ? 101 GLU   A CG   1 ? 2 
ATOM   3091 C CD   . GLU   B 1 89  ? 9.24   -21.844 37.608  1   48.695  ? 101 GLU   A CD   1 ? 2 
ATOM   3092 O OE1  . GLU   B 1 89  ? 10.135 -22.631 38.08   1   49.643  ? 101 GLU   A OE1  1 ? 2 
ATOM   3093 O OE2  . GLU   B 1 89  ? 9.501  -20.716 37.157  1   48.202  ? 101 GLU   A OE2  1 ? 2 
ATOM   3094 H H    . GLU   B 1 89  ? 7.107  -25.917 35.843  1   55.592  ? 101 GLU   A H    1 c 2 
ATOM   3095 H HA   . GLU   B 1 89  ? 5.833  -24.232 37.569  1   55.124  ? 101 GLU   A HA   1 c 2 
ATOM   3096 H HB2  . GLU   B 1 89  ? 8.21   -24.274 37.391  1   55.51   ? 101 GLU   A HB2  1 c 2 
ATOM   3097 H HB3  . GLU   B 1 89  ? 8.105  -23.617 35.957  1   53.617  ? 101 GLU   A HB3  1 c 2 
ATOM   3098 H HG2  . GLU   B 1 89  ? 7.322  -21.611 36.898  1   49.929  ? 101 GLU   A HG2  1 c 2 
ATOM   3099 H HG3  . GLU   B 1 89  ? 7.368  -22.265 38.35   1   51.854  ? 101 GLU   A HG3  1 c 2 
ATOM   3100 N N    . ILE   B 1 90  ? 4.631  -22.475 36.3    1   50.946  ? 102 ILE   A N    1 ? 2 
ATOM   3101 C CA   . ILE   B 1 90  ? 4.117  -21.327 35.557  1   47.895  ? 102 ILE   A CA   1 ? 2 
ATOM   3102 C C    . ILE   B 1 90  ? 4.782  -20.071 36.078  1   47.497  ? 102 ILE   A C    1 ? 2 
ATOM   3103 O O    . ILE   B 1 90  ? 4.722  -19.778 37.274  1   46.886  ? 102 ILE   A O    1 ? 2 
ATOM   3104 C CB   . ILE   B 1 90  ? 2.586  -21.225 35.615  1   49.785  ? 102 ILE   A CB   1 ? 2 
ATOM   3105 C CG1  . ILE   B 1 90  ? 1.933  -22.548 35.152  1   55.652  ? 102 ILE   A CG1  1 ? 2 
ATOM   3106 C CG2  . ILE   B 1 90  ? 2.049  -20.015 34.846  1   45.948  ? 102 ILE   A CG2  1 ? 2 
ATOM   3107 C CD1  . ILE   B 1 90  ? 0.423  -22.615 35.301  1   55.341  ? 102 ILE   A CD1  1 ? 2 
ATOM   3108 H H    . ILE   B 1 90  ? 4.384  -22.584 37.174  1   51.257  ? 102 ILE   A H    1 c 2 
ATOM   3109 H HA   . ILE   B 1 90  ? 4.368  -21.44  34.625  1   48.011  ? 102 ILE   A HA   1 c 2 
ATOM   3110 H HB   . ILE   B 1 90  ? 2.344  -21.101 36.554  1   50.43   ? 102 ILE   A HB   1 c 2 
ATOM   3111 H HG12 . ILE   B 1 90  ? 2.157  -22.69  34.21   1   53.822  ? 102 ILE   A HG12 1 c 2 
ATOM   3112 H HG13 . ILE   B 1 90  ? 2.325  -23.284 35.663  1   55.155  ? 102 ILE   A HG13 1 c 2 
ATOM   3113 H HG21 . ILE   B 1 90  ? 1.081  -19.98  34.924  1   47.756  ? 102 ILE   A HG21 1 c 2 
ATOM   3114 H HG22 . ILE   B 1 90  ? 2.293  -20.09  33.908  1   46.183  ? 102 ILE   A HG22 1 c 2 
ATOM   3115 H HG23 . ILE   B 1 90  ? 2.428  -19.199 35.212  1   45.869  ? 102 ILE   A HG23 1 c 2 
ATOM   3116 H HD11 . ILE   B 1 90  ? 0.178  -22.464 36.234  1   56.527  ? 102 ILE   A HD11 1 c 2 
ATOM   3117 H HD12 . ILE   B 1 90  ? 0.113  -23.496 35.023  1   57.382  ? 102 ILE   A HD12 1 c 2 
ATOM   3118 H HD13 . ILE   B 1 90  ? 0.003  -21.935 34.742  1   55.247  ? 102 ILE   A HD13 1 c 2 
ATOM   3119 N N    . ALA   B 1 91  ? 5.314  -19.292 35.122  1   41.354  ? 103 ALA   A N    1 ? 2 
ATOM   3120 C CA   . ALA   B 1 91  ? 6.015  -18.061 35.445  1   41.94   ? 103 ALA   A CA   1 ? 2 
ATOM   3121 C C    . ALA   B 1 91  ? 5.483  -16.946 34.546  1   39.817  ? 103 ALA   A C    1 ? 2 
ATOM   3122 O O    . ALA   B 1 91  ? 4.959  -17.223 33.442  1   41.267  ? 103 ALA   A O    1 ? 2 
ATOM   3123 C CB   . ALA   B 1 91  ? 7.522  -18.213 35.241  1   40.577  ? 103 ALA   A CB   1 ? 2 
ATOM   3124 H H    . ALA   B 1 91  ? 5.235  -19.536 34.245  1   42.636  ? 103 ALA   A H    1 c 2 
ATOM   3125 H HA   . ALA   B 1 91  ? 5.829  -17.823 36.394  1   41.804  ? 103 ALA   A HA   1 c 2 
ATOM   3126 H HB1  . ALA   B 1 91  ? 7.862  -18.911 35.826  1   41.615  ? 103 ALA   A HB1  1 c 2 
ATOM   3127 H HB2  . ALA   B 1 91  ? 7.704  -18.452 34.316  1   40.53   ? 103 ALA   A HB2  1 c 2 
ATOM   3128 H HB3  . ALA   B 1 91  ? 7.967  -17.375 35.449  1   40.409  ? 103 ALA   A HB3  1 c 2 
ATOM   3129 N N    . HIS   B 1 92  ? 5.599  -15.73  35.072  1   40.203  ? 104 HIS   A N    1 ? 2 
ATOM   3130 C CA   . HIS   B 1 92  ? 5.343  -14.485 34.359  1   40.794  ? 104 HIS   A CA   1 ? 2 
ATOM   3131 C C    . HIS   B 1 92  ? 6.663  -13.766 34.113  1   39.774  ? 104 HIS   A C    1 ? 2 
ATOM   3132 O O    . HIS   B 1 92  ? 7.483  -13.618 35.024  1   40.599  ? 104 HIS   A O    1 ? 2 
ATOM   3133 C CB   . HIS   B 1 92  ? 4.419  -13.601 35.203  1   38.61   ? 104 HIS   A CB   1 ? 2 
ATOM   3134 C CG   . HIS   B 1 92  ? 3.027  -14.059 35.232  1   39.686  ? 104 HIS   A CG   1 ? 2 
ATOM   3135 N ND1  . HIS   B 1 92  ? 2.05   -13.391 35.919  1   44.045  ? 104 HIS   A ND1  1 ? 2 
ATOM   3136 C CD2  . HIS   B 1 92  ? 2.459  -15.163 34.756  1   44.236  ? 104 HIS   A CD2  1 ? 2 
ATOM   3137 C CE1  . HIS   B 1 92  ? 0.9    -14.027 35.771  1   45.752  ? 104 HIS   A CE1  1 ? 2 
ATOM   3138 N NE2  . HIS   B 1 92  ? 1.123  -15.106 35.057  1   48.192  ? 104 HIS   A NE2  1 ? 2 
ATOM   3139 H H    . HIS   B 1 92  ? 5.861  -15.669 35.945  1   40.688  ? 104 HIS   A H    1 c 2 
ATOM   3140 H HA   . HIS   B 1 92  ? 4.92   -14.686 33.491  1   39.79   ? 104 HIS   A HA   1 c 2 
ATOM   3141 H HB2  . HIS   B 1 92  ? 4.763  -13.573 36.122  1   39.727  ? 104 HIS   A HB2  1 c 2 
ATOM   3142 H HB3  . HIS   B 1 92  ? 4.445  -12.687 34.846  1   39.267  ? 104 HIS   A HB3  1 c 2 
ATOM   3143 H HD1  . HIS   B 1 92  ? 2.122  -12.667 36.376  0   30      ? 104 HIS   A HD1  1 c 2 
ATOM   3144 H HD2  . HIS   B 1 92  ? 2.867  -15.821 34.23   1   43.214  ? 104 HIS   A HD2  1 c 2 
ATOM   3145 H HE1  . HIS   B 1 92  ? 0.072  -13.764 36.134  1   47.535  ? 104 HIS   A HE1  1 c 2 
ATOM   3146 H HE2  . HIS   B 1 92  ? 0.493  -15.724 34.81   0   30      ? 104 HIS   A HE2  1 c 2 
ATOM   3147 N N    . LEU   B 1 93  ? 6.832  -13.247 32.881  1   39.014  ? 105 LEU   A N    1 ? 2 
ATOM   3148 C CA   . LEU   B 1 93  ? 8.029  -12.549 32.479  1   38.933  ? 105 LEU   A CA   1 ? 2 
ATOM   3149 C C    . LEU   B 1 93  ? 7.615  -11.203 31.876  1   39.859  ? 105 LEU   A C    1 ? 2 
ATOM   3150 O O    . LEU   B 1 93  ? 6.706  -11.187 31.044  1   41.8    ? 105 LEU   A O    1 ? 2 
ATOM   3151 C CB   . LEU   B 1 93  ? 8.743  -13.375 31.419  1   40.09   ? 105 LEU   A CB   1 ? 2 
ATOM   3152 C CG   . LEU   B 1 93  ? 9.432  -14.674 31.809  1   42.505  ? 105 LEU   A CG   1 ? 2 
ATOM   3153 C CD1  . LEU   B 1 93  ? 10.094 -15.207 30.549  1   47.085  ? 105 LEU   A CD1  1 ? 2 
ATOM   3154 C CD2  . LEU   B 1 93  ? 10.4   -14.453 32.936  1   40.716  ? 105 LEU   A CD2  1 ? 2 
ATOM   3155 H H    . LEU   B 1 93  ? 6.159  -13.338 32.269  1   39.163  ? 105 LEU   A H    1 c 2 
ATOM   3156 H HA   . LEU   B 1 93  ? 8.615  -12.411 33.261  1   39.573  ? 105 LEU   A HA   1 c 2 
ATOM   3157 H HB2  . LEU   B 1 93  ? 8.088  -13.582 30.713  1   40.268  ? 105 LEU   A HB2  1 c 2 
ATOM   3158 H HB3  . LEU   B 1 93  ? 9.416  -12.794 30.994  1   40.343  ? 105 LEU   A HB3  1 c 2 
ATOM   3159 H HG   . LEU   B 1 93  ? 8.742  -15.322 32.104  1   42.558  ? 105 LEU   A HG   1 c 2 
ATOM   3160 H HD11 . LEU   B 1 93  ? 9.422  -15.343 29.86   1   45.615  ? 105 LEU   A HD11 1 c 2 
ATOM   3161 H HD12 . LEU   B 1 93  ? 10.531 -16.053 30.744  1   46.031  ? 105 LEU   A HD12 1 c 2 
ATOM   3162 H HD13 . LEU   B 1 93  ? 10.755 -14.568 30.233  1   45.681  ? 105 LEU   A HD13 1 c 2 
ATOM   3163 H HD21 . LEU   B 1 93  ? 9.91   -14.254 33.751  1   41.514  ? 105 LEU   A HD21 1 c 2 
ATOM   3164 H HD22 . LEU   B 1 93  ? 10.986 -13.708 32.72   1   41.418  ? 105 LEU   A HD22 1 c 2 
ATOM   3165 H HD23 . LEU   B 1 93  ? 10.933 -15.255 33.068  1   41.645  ? 105 LEU   A HD23 1 c 2 
ATOM   3166 N N    . LEU   B 1 94  ? 8.164  -10.108 32.412  1   40.662  ? 106 LEU   A N    1 ? 2 
ATOM   3167 C CA   . LEU   B 1 94  ? 7.974  -8.772  31.841  1   44.391  ? 106 LEU   A CA   1 ? 2 
ATOM   3168 C C    . LEU   B 1 94  ? 9.323  -8.368  31.271  1   44.783  ? 106 LEU   A C    1 ? 2 
ATOM   3169 O O    . LEU   B 1 94  ? 10.372 -8.429  31.959  1   43.07   ? 106 LEU   A O    1 ? 2 
ATOM   3170 C CB   . LEU   B 1 94  ? 7.456  -7.79   32.884  1   46.757  ? 106 LEU   A CB   1 ? 2 
ATOM   3171 C CG   . LEU   B 1 94  ? 7.182  -6.349  32.418  1   48.868  ? 106 LEU   A CG   1 ? 2 
ATOM   3172 C CD1  . LEU   B 1 94  ? 5.957  -6.329  31.527  1   50.665  ? 106 LEU   A CD1  1 ? 2 
ATOM   3173 C CD2  . LEU   B 1 94  ? 7.062  -5.389  33.616  1   51.266  ? 106 LEU   A CD2  1 ? 2 
ATOM   3174 H H    . LEU   B 1 94  ? 8.678  -10.191 33.164  1   41.406  ? 106 LEU   A H    1 c 2 
ATOM   3175 H HA   . LEU   B 1 94  ? 7.318  -8.836  31.102  1   43.918  ? 106 LEU   A HA   1 c 2 
ATOM   3176 H HB2  . LEU   B 1 94  ? 6.622  -8.156  33.258  1   46.698  ? 106 LEU   A HB2  1 c 2 
ATOM   3177 H HB3  . LEU   B 1 94  ? 8.11   -7.756  33.62   1   46.911  ? 106 LEU   A HB3  1 c 2 
ATOM   3178 H HG   . LEU   B 1 94  ? 7.955  -6.051  31.873  1   49.175  ? 106 LEU   A HG   1 c 2 
ATOM   3179 H HD11 . LEU   B 1 94  ? 6.123  -6.864  30.733  1   49.269  ? 106 LEU   A HD11 1 c 2 
ATOM   3180 H HD12 . LEU   B 1 94  ? 5.762  -5.414  31.264  1   51.39   ? 106 LEU   A HD12 1 c 2 
ATOM   3181 H HD13 . LEU   B 1 94  ? 5.197  -6.696  32.01   1   50.232  ? 106 LEU   A HD13 1 c 2 
ATOM   3182 H HD21 . LEU   B 1 94  ? 7.884  -5.411  34.134  1   51.173  ? 106 LEU   A HD21 1 c 2 
ATOM   3183 H HD22 . LEU   B 1 94  ? 6.318  -5.662  34.179  1   51.296  ? 106 LEU   A HD22 1 c 2 
ATOM   3184 H HD23 . LEU   B 1 94  ? 6.908  -4.485  33.294  1   52.331  ? 106 LEU   A HD23 1 c 2 
ATOM   3185 N N    . ILE   B 1 95  ? 9.267  -8.008  29.992  1   41.383  ? 107 ILE   A N    1 ? 2 
ATOM   3186 C CA   . ILE   B 1 95  ? 10.426 -8.004  29.122  1   39.3    ? 107 ILE   A CA   1 ? 2 
ATOM   3187 C C    . ILE   B 1 95  ? 10.509 -6.645  28.443  1   43.988  ? 107 ILE   A C    1 ? 2 
ATOM   3188 O O    . ILE   B 1 95  ? 9.6    -6.281  27.68   1   42.181  ? 107 ILE   A O    1 ? 2 
ATOM   3189 C CB   . ILE   B 1 95  ? 10.302 -9.129  28.096  1   37.775  ? 107 ILE   A CB   1 ? 2 
ATOM   3190 C CG1  . ILE   B 1 95  ? 10.09  -10.51  28.759  1   38.989  ? 107 ILE   A CG1  1 ? 2 
ATOM   3191 C CG2  . ILE   B 1 95  ? 11.507 -9.133  27.158  1   39.177  ? 107 ILE   A CG2  1 ? 2 
ATOM   3192 C CD1  . ILE   B 1 95  ? 9.627  -11.616 27.815  1   40.888  ? 107 ILE   A CD1  1 ? 2 
ATOM   3193 H H    . ILE   B 1 95  ? 8.464  -7.744  29.644  1   41.958  ? 107 ILE   A H    1 c 2 
ATOM   3194 H HA   . ILE   B 1 95  ? 11.23  -8.15   29.657  1   40.322  ? 107 ILE   A HA   1 c 2 
ATOM   3195 H HB   . ILE   B 1 95  ? 9.509  -8.944  27.555  1   38.623  ? 107 ILE   A HB   1 c 2 
ATOM   3196 H HG12 . ILE   B 1 95  ? 10.932 -10.788 29.173  1   38.966  ? 107 ILE   A HG12 1 c 2 
ATOM   3197 H HG13 . ILE   B 1 95  ? 9.427  -10.418 29.471  1   38.872  ? 107 ILE   A HG13 1 c 2 
ATOM   3198 H HG21 . ILE   B 1 95  ? 11.483 -9.926  26.598  1   38.687  ? 107 ILE   A HG21 1 c 2 
ATOM   3199 H HG22 . ILE   B 1 95  ? 12.326 -9.132  27.681  1   39.146  ? 107 ILE   A HG22 1 c 2 
ATOM   3200 H HG23 . ILE   B 1 95  ? 11.484 -8.342  26.594  1   39.764  ? 107 ILE   A HG23 1 c 2 
ATOM   3201 H HD11 . ILE   B 1 95  ? 8.843  -11.311 27.319  1   40.44   ? 107 ILE   A HD11 1 c 2 
ATOM   3202 H HD12 . ILE   B 1 95  ? 9.394  -12.411 28.331  1   39.867  ? 107 ILE   A HD12 1 c 2 
ATOM   3203 H HD13 . ILE   B 1 95  ? 10.34  -11.836 27.187  1   40.447  ? 107 ILE   A HD13 1 c 2 
ATOM   3204 N N    . LYS   B 1 96  ? 11.624 -5.958  28.687  1   45.982  ? 108 LYS   A N    1 ? 2 
ATOM   3205 C CA   . LYS   B 1 96  ? 11.931 -4.714  27.985  1   49.28   ? 108 LYS   A CA   1 ? 2 
ATOM   3206 C C    . LYS   B 1 96  ? 12.422 -5.033  26.578  1   44.616  ? 108 LYS   A C    1 ? 2 
ATOM   3207 O O    . LYS   B 1 96  ? 12.914 -6.111  26.286  1   44.479  ? 108 LYS   A O    1 ? 2 
ATOM   3208 C CB   . LYS   B 1 96  ? 12.961 -3.959  28.833  1   49.541  ? 108 LYS   A CB   1 ? 2 
ATOM   3209 C CG   . LYS   B 1 96  ? 12.446 -3.375  30.158  1   57.809  ? 108 LYS   A CG   1 ? 2 
ATOM   3210 C CD   . LYS   B 1 96  ? 11.216 -2.448  30.106  1   61.857  ? 108 LYS   A CD   1 ? 2 
ATOM   3211 C CE   . LYS   B 1 96  ? 10.647 -2.119  31.477  1   59.744  ? 108 LYS   A CE   1 ? 2 
ATOM   3212 N NZ   . LYS   B 1 96  ? 10.151 -3.346  32.158  1   52.701  ? 108 LYS   A NZ   1 ? 2 
ATOM   3213 H H    . LYS   B 1 96  ? 12.217 -6.271  29.309  1   45.864  ? 108 LYS   A H    1 c 2 
ATOM   3214 H HA   . LYS   B 1 96  ? 11.102 -4.178  27.92   1   48.422  ? 108 LYS   A HA   1 c 2 
ATOM   3215 H HB2  . LYS   B 1 96  ? 13.702 -4.569  29.036  1   50.917  ? 108 LYS   A HB2  1 c 2 
ATOM   3216 H HB3  . LYS   B 1 96  ? 13.326 -3.224  28.299  1   52.831  ? 108 LYS   A HB3  1 c 2 
ATOM   3217 H HG2  . LYS   B 1 96  ? 12.239 -4.127  30.753  1   55.341  ? 108 LYS   A HG2  1 c 2 
ATOM   3218 H HG3  . LYS   B 1 96  ? 13.185 -2.881  30.574  1   57.834  ? 108 LYS   A HG3  1 c 2 
ATOM   3219 H HD2  . LYS   B 1 96  ? 11.47  -1.611  29.659  1   62.095  ? 108 LYS   A HD2  1 c 2 
ATOM   3220 H HD3  . LYS   B 1 96  ? 10.516 -2.874  29.568  1   59.37   ? 108 LYS   A HD3  1 c 2 
ATOM   3221 H HE2  . LYS   B 1 96  ? 11.337 -1.706  32.027  1   60.303  ? 108 LYS   A HE2  1 c 2 
ATOM   3222 H HE3  . LYS   B 1 96  ? 9.91   -1.492  31.391  1   60.247  ? 108 LYS   A HE3  1 c 2 
ATOM   3223 H HZ1  . LYS   B 1 96  ? 10.846 -3.801  32.521  1   53.716  ? 108 LYS   A HZ1  1 c 2 
ATOM   3224 H HZ2  . LYS   B 1 96  ? 9.722  -3.879  31.564  1   53.09   ? 108 LYS   A HZ2  1 c 2 
ATOM   3225 H HZ3  . LYS   B 1 96  ? 9.575  -3.115  32.819  1   54.801  ? 108 LYS   A HZ3  1 c 2 
ATOM   3226 N N    . PRO   B 1 97  ? 12.383 -4.043  25.64   1   47.585  ? 109 PRO   A N    1 ? 2 
ATOM   3227 C CA   . PRO   B 1 97  ? 12.664 -4.323  24.229  1   47.296  ? 109 PRO   A CA   1 ? 2 
ATOM   3228 C C    . PRO   B 1 97  ? 14.053 -4.899  23.96   1   46.541  ? 109 PRO   A C    1 ? 2 
ATOM   3229 O O    . PRO   B 1 97  ? 14.209 -5.698  23.06   1   45.303  ? 109 PRO   A O    1 ? 2 
ATOM   3230 C CB   . PRO   B 1 97  ? 12.398 -2.991  23.526  1   46.612  ? 109 PRO   A CB   1 ? 2 
ATOM   3231 C CG   . PRO   B 1 97  ? 12.492 -1.938  24.635  1   52.956  ? 109 PRO   A CG   1 ? 2 
ATOM   3232 C CD   . PRO   B 1 97  ? 11.944 -2.664  25.886  1   51.915  ? 109 PRO   A CD   1 ? 2 
ATOM   3233 H HA   . PRO   B 1 97  ? 11.999 -4.968  23.907  1   45.674  ? 109 PRO   A HA   1 c 2 
ATOM   3234 H HB2  . PRO   B 1 97  ? 13.064 -2.824  22.831  1   49.503  ? 109 PRO   A HB2  1 c 2 
ATOM   3235 H HB3  . PRO   B 1 97  ? 11.511 -2.986  23.117  1   48.316  ? 109 PRO   A HB3  1 c 2 
ATOM   3236 H HG2  . PRO   B 1 97  ? 13.419 -1.657  24.775  1   52.878  ? 109 PRO   A HG2  1 c 2 
ATOM   3237 H HG3  . PRO   B 1 97  ? 11.949 -1.153  24.423  1   53.281  ? 109 PRO   A HG3  1 c 2 
ATOM   3238 H HD2  . PRO   B 1 97  ? 12.335 -2.308  26.704  1   51.649  ? 109 PRO   A HD2  1 c 2 
ATOM   3239 H HD3  . PRO   B 1 97  ? 10.97  -2.61   25.936  1   50.851  ? 109 PRO   A HD3  1 c 2 
ATOM   3240 N N    . GLU   B 1 98  ? 15.041 -4.532  24.785  1   50.059  ? 110 GLU   A N    1 ? 2 
ATOM   3241 C CA   . GLU   B 1 98  ? 16.416 -4.965  24.598  1   55.912  ? 110 GLU   A CA   1 ? 2 
ATOM   3242 C C    . GLU   B 1 98  ? 16.561 -6.497  24.686  1   56.692  ? 110 GLU   A C    1 ? 2 
ATOM   3243 O O    . GLU   B 1 98  ? 17.553 -7.056  24.207  1   51.003  ? 110 GLU   A O    1 ? 2 
ATOM   3244 C CB   . GLU   B 1 98  ? 17.292 -4.254  25.635  1   56.108  ? 110 GLU   A CB   1 ? 2 
ATOM   3245 C CG   . GLU   B 1 98  ? 17.308 -2.731  25.551  1   66.321  ? 110 GLU   A CG   1 ? 2 
ATOM   3246 C CD   . GLU   B 1 98  ? 16.136 -1.904  26.086  1   67.074  ? 110 GLU   A CD   1 ? 2 
ATOM   3247 O OE1  . GLU   B 1 98  ? 15.279 -2.424  26.817  1   59.256  ? 110 GLU   A OE1  1 ? 2 
ATOM   3248 O OE2  . GLU   B 1 98  ? 16.069 -0.7    25.726  1   66.383  ? 110 GLU   A OE2  1 ? 2 
ATOM   3249 H H    . GLU   B 1 98  ? 14.843 -4      25.501  1   50.75   ? 110 GLU   A H    1 c 2 
ATOM   3250 H HA   . GLU   B 1 98  ? 16.708 -4.677  23.696  1   56.349  ? 110 GLU   A HA   1 c 2 
ATOM   3251 H HB2  . GLU   B 1 98  ? 16.983 -4.509  26.53   1   56.955  ? 110 GLU   A HB2  1 c 2 
ATOM   3252 H HB3  . GLU   B 1 98  ? 18.213 -4.576  25.538  1   58.771  ? 110 GLU   A HB3  1 c 2 
ATOM   3253 H HG2  . GLU   B 1 98  ? 18.116 -2.418  26.012  1   65.889  ? 110 GLU   A HG2  1 c 2 
ATOM   3254 H HG3  . GLU   B 1 98  ? 17.428 -2.487  24.609  1   65.575  ? 110 GLU   A HG3  1 c 2 
ATOM   3255 N N    . TYR   B 1 99  ? 15.578 -7.188  25.291  1   52.607  ? 111 TYR   A N    1 ? 2 
ATOM   3256 C CA   . TYR   B 1 99  ? 15.601 -8.64   25.42   1   49.13   ? 111 TYR   A CA   1 ? 2 
ATOM   3257 C C    . TYR   B 1 99  ? 14.477 -9.264  24.587  1   49.222  ? 111 TYR   A C    1 ? 2 
ATOM   3258 O O    . TYR   B 1 99  ? 14.114 -10.435 24.771  1   43.322  ? 111 TYR   A O    1 ? 2 
ATOM   3259 C CB   . TYR   B 1 99  ? 15.5   -8.972  26.922  1   49.191  ? 111 TYR   A CB   1 ? 2 
ATOM   3260 C CG   . TYR   B 1 99  ? 16.727 -8.473  27.687  1   47.462  ? 111 TYR   A CG   1 ? 2 
ATOM   3261 C CD1  . TYR   B 1 99  ? 17.85  -9.286  27.802  1   56.24   ? 111 TYR   A CD1  1 ? 2 
ATOM   3262 C CD2  . TYR   B 1 99  ? 16.78  -7.219  28.283  1   46.326  ? 111 TYR   A CD2  1 ? 2 
ATOM   3263 C CE1  . TYR   B 1 99  ? 18.996 -8.866  28.464  1   54.292  ? 111 TYR   A CE1  1 ? 2 
ATOM   3264 C CE2  . TYR   B 1 99  ? 17.924 -6.791  28.969  1   50.03   ? 111 TYR   A CE2  1 ? 2 
ATOM   3265 C CZ   . TYR   B 1 99  ? 19.032 -7.621  29.057  1   54.318  ? 111 TYR   A CZ   1 ? 2 
ATOM   3266 O OH   . TYR   B 1 99  ? 20.201 -7.272  29.69   1   54.37   ? 111 TYR   A OH   1 ? 2 
ATOM   3267 H H    . TYR   B 1 99  ? 14.875 -6.734  25.656  1   52.053  ? 111 TYR   A H    1 c 2 
ATOM   3268 H HA   . TYR   B 1 99  ? 16.471 -8.979  25.08   1   50.765  ? 111 TYR   A HA   1 c 2 
ATOM   3269 H HB2  . TYR   B 1 99  ? 14.693 -8.548  27.29   1   47.682  ? 111 TYR   A HB2  1 c 2 
ATOM   3270 H HB3  . TYR   B 1 99  ? 15.424 -9.946  27.031  1   47.44   ? 111 TYR   A HB3  1 c 2 
ATOM   3271 H HD1  . TYR   B 1 99  ? 17.843 -10.138 27.396  1   52.86   ? 111 TYR   A HD1  1 c 2 
ATOM   3272 H HD2  . TYR   B 1 99  ? 16.033 -6.645  28.227  1   47.221  ? 111 TYR   A HD2  1 c 2 
ATOM   3273 H HE1  . TYR   B 1 99  ? 19.744 -9.436  28.522  1   55.459  ? 111 TYR   A HE1  1 c 2 
ATOM   3274 H HE2  . TYR   B 1 99  ? 17.946 -5.936  29.362  1   51.408  ? 111 TYR   A HE2  1 c 2 
ATOM   3275 H HH   . TYR   B 1 99  ? 20.751 -7.886  29.615  0   30      ? 111 TYR   A HH   1 c 2 
ATOM   3276 N N    . ALA   B 1 100 ? 13.927 -8.479  23.654  1   44.424  ? 112 ALA   A N    1 ? 2 
ATOM   3277 C CA   . ALA   B 1 100 ? 12.85  -8.924  22.787  1   43.457  ? 112 ALA   A CA   1 ? 2 
ATOM   3278 C C    . ALA   B 1 100 ? 13.147 -8.512  21.343  1   48.259  ? 112 ALA   A C    1 ? 2 
ATOM   3279 O O    . ALA   B 1 100 ? 14.048 -9.109  20.739  1   49.126  ? 112 ALA   A O    1 ? 2 
ATOM   3280 C CB   . ALA   B 1 100 ? 11.513 -8.405  23.311  1   40.067  ? 112 ALA   A CB   1 ? 2 
ATOM   3281 H H    . ALA   B 1 100 ? 14.246 -7.631  23.543  1   46.631  ? 112 ALA   A H    1 c 2 
ATOM   3282 H HA   . ALA   B 1 100 ? 12.829 -9.918  22.813  1   43.044  ? 112 ALA   A HA   1 c 2 
ATOM   3283 H HB1  . ALA   B 1 100 ? 11.299 -8.845  24.15   1   39.815  ? 112 ALA   A HB1  1 c 2 
ATOM   3284 H HB2  . ALA   B 1 100 ? 11.569 -7.446  23.459  1   41.559  ? 112 ALA   A HB2  1 c 2 
ATOM   3285 H HB3  . ALA   B 1 100 ? 10.812 -8.591  22.664  1   41.042  ? 112 ALA   A HB3  1 c 2 
ATOM   3286 N N    . TYR   B 1 101 ? 12.438 -7.5    20.794  1   46.564  ? 113 TYR   A N    1 ? 2 
ATOM   3287 C CA   . TYR   B 1 101 ? 12.655 -7.167  19.383  1   48.78   ? 113 TYR   A CA   1 ? 2 
ATOM   3288 C C    . TYR   B 1 101 ? 13.309 -5.803  19.169  1   50.256  ? 113 TYR   A C    1 ? 2 
ATOM   3289 O O    . TYR   B 1 101 ? 13.391 -5.349  18.034  1   53.788  ? 113 TYR   A O    1 ? 2 
ATOM   3290 C CB   . TYR   B 1 101 ? 11.304 -7.249  18.653  1   48.592  ? 113 TYR   A CB   1 ? 2 
ATOM   3291 C CG   . TYR   B 1 101 ? 10.732 -8.659  18.736  1   47.621  ? 113 TYR   A CG   1 ? 2 
ATOM   3292 C CD1  . TYR   B 1 101 ? 11.194 -9.647  17.873  1   48.421  ? 113 TYR   A CD1  1 ? 2 
ATOM   3293 C CD2  . TYR   B 1 101 ? 9.835  -9.035  19.72   1   47.766  ? 113 TYR   A CD2  1 ? 2 
ATOM   3294 C CE1  . TYR   B 1 101 ? 10.706 -10.941 17.913  1   46.66   ? 113 TYR   A CE1  1 ? 2 
ATOM   3295 C CE2  . TYR   B 1 101 ? 9.34   -10.333 19.784  1   45.939  ? 113 TYR   A CE2  1 ? 2 
ATOM   3296 C CZ   . TYR   B 1 101 ? 9.759  -11.279 18.864  1   45.985  ? 113 TYR   A CZ   1 ? 2 
ATOM   3297 O OH   . TYR   B 1 101 ? 9.312  -12.561 18.927  1   47.705  ? 113 TYR   A OH   1 ? 2 
ATOM   3298 H H    . TYR   B 1 101 ? 11.832 -7.024  21.283  1   46.77   ? 113 TYR   A H    1 c 2 
ATOM   3299 H HA   . TYR   B 1 101 ? 13.253 -7.856  18.99   1   48.882  ? 113 TYR   A HA   1 c 2 
ATOM   3300 H HB2  . TYR   B 1 101 ? 10.676 -6.616  19.068  1   48.708  ? 113 TYR   A HB2  1 c 2 
ATOM   3301 H HB3  . TYR   B 1 101 ? 11.431 -7.003  17.71   1   50.387  ? 113 TYR   A HB3  1 c 2 
ATOM   3302 H HD1  . TYR   B 1 101 ? 11.812 -9.413  17.198  1   49.573  ? 113 TYR   A HD1  1 c 2 
ATOM   3303 H HD2  . TYR   B 1 101 ? 9.518  -8.389  20.33   1   46.691  ? 113 TYR   A HD2  1 c 2 
ATOM   3304 H HE1  . TYR   B 1 101 ? 11.008 -11.584 17.294  1   48.087  ? 113 TYR   A HE1  1 c 2 
ATOM   3305 H HE2  . TYR   B 1 101 ? 8.703  -10.564 20.437  1   45.129  ? 113 TYR   A HE2  1 c 2 
ATOM   3306 H HH   . TYR   B 1 101 ? 9.736  -13.073 18.299  0   30      ? 113 TYR   A HH   1 c 2 
ATOM   3307 N N    . GLY   B 1 102 ? 13.68  -5.13   20.255  1   50.567  ? 114 GLY   A N    1 ? 2 
ATOM   3308 C CA   . GLY   B 1 102 ? 14.613 -4.013  20.172  1   56.173  ? 114 GLY   A CA   1 ? 2 
ATOM   3309 C C    . GLY   B 1 102 ? 13.961 -2.778  19.554  1   57.809  ? 114 GLY   A C    1 ? 2 
ATOM   3310 O O    . GLY   B 1 102 ? 12.733 -2.698  19.387  1   52.61   ? 114 GLY   A O    1 ? 2 
ATOM   3311 H H    . GLY   B 1 102 ? 13.341 -5.36   21.071  1   49.745  ? 114 GLY   A H    1 c 2 
ATOM   3312 H HA2  . GLY   B 1 102 ? 14.937 -3.796  21.078  1   54.848  ? 114 GLY   A HA2  1 c 2 
ATOM   3313 H HA3  . GLY   B 1 102 ? 15.39  -4.282  19.628  1   56.147  ? 114 GLY   A HA3  1 c 2 
ATOM   3314 N N    . SER   B 1 103 ? 14.813 -1.83   19.174  1   57.661  ? 115 SER   A N    1 ? 2 
ATOM   3315 C CA   . SER   B 1 103 ? 14.315 -0.599  18.595  1   63.823  ? 115 SER   A CA   1 ? 2 
ATOM   3316 C C    . SER   B 1 103 ? 13.817 -0.857  17.165  1   60.036  ? 115 SER   A C    1 ? 2 
ATOM   3317 O O    . SER   B 1 103 ? 12.938 -0.147  16.664  1   64.381  ? 115 SER   A O    1 ? 2 
ATOM   3318 C CB   . SER   B 1 103 ? 15.379 0.481   18.702  1   70.041  ? 115 SER   A CB   1 ? 2 
ATOM   3319 O OG   . SER   B 1 103 ? 16.656 0.03    18.263  1   71.736  ? 115 SER   A OG   1 ? 2 
ATOM   3320 H H    . SER   B 1 103 ? 15.713 -1.948  19.275  1   59.618  ? 115 SER   A H    1 c 2 
ATOM   3321 H HA   . SER   B 1 103 ? 13.536 -0.309  19.131  1   62.081  ? 115 SER   A HA   1 c 2 
ATOM   3322 H HB2  . SER   B 1 103 ? 15.108 1.25    18.165  1   71.573  ? 115 SER   A HB2  1 c 2 
ATOM   3323 H HB3  . SER   B 1 103 ? 15.444 0.773   19.631  1   69.043  ? 115 SER   A HB3  1 c 2 
ATOM   3324 H HG   . SER   B 1 103 ? 17.226 0.625   18.196  0   30      ? 115 SER   A HG   1 c 2 
ATOM   3325 N N    . ALA   B 1 104 ? 14.39  -1.87   16.502  1   56.35   ? 116 ALA   A N    1 ? 2 
ATOM   3326 C CA   . ALA   B 1 104 ? 13.946 -2.335  15.206  1   58.737  ? 116 ALA   A CA   1 ? 2 
ATOM   3327 C C    . ALA   B 1 104 ? 12.53  -2.886  15.205  1   59.207  ? 116 ALA   A C    1 ? 2 
ATOM   3328 O O    . ALA   B 1 104 ? 11.837 -2.777  14.184  1   57.362  ? 116 ALA   A O    1 ? 2 
ATOM   3329 C CB   . ALA   B 1 104 ? 14.899 -3.363  14.664  1   60.175  ? 116 ALA   A CB   1 ? 2 
ATOM   3330 H H    . ALA   B 1 104 ? 15.108 -2.287  16.883  1   56.819  ? 116 ALA   A H    1 c 2 
ATOM   3331 H HA   . ALA   B 1 104 ? 13.958 -1.55   14.592  1   61.504  ? 116 ALA   A HA   1 c 2 
ATOM   3332 H HB1  . ALA   B 1 104 ? 15.793 -2.985  14.613  1   61.239  ? 116 ALA   A HB1  1 c 2 
ATOM   3333 H HB2  . ALA   B 1 104 ? 14.912 -4.138  15.25   1   57.689  ? 116 ALA   A HB2  1 c 2 
ATOM   3334 H HB3  . ALA   B 1 104 ? 14.615 -3.636  13.776  1   60.814  ? 116 ALA   A HB3  1 c 2 
ATOM   3335 N N    . GLY   B 1 105 ? 12.148 -3.555  16.292  1   54.086  ? 117 GLY   A N    1 ? 2 
ATOM   3336 C CA   . GLY   B 1 105 ? 10.854 -4.215  16.386  1   50.976  ? 117 GLY   A CA   1 ? 2 
ATOM   3337 C C    . GLY   B 1 105 ? 10.781 -5.36   15.393  1   51.624  ? 117 GLY   A C    1 ? 2 
ATOM   3338 O O    . GLY   B 1 105 ? 11.791 -5.783  14.839  1   51.335  ? 117 GLY   A O    1 ? 2 
ATOM   3339 H H    . GLY   B 1 105 ? 12.716 -3.608  17.006  1   53.29   ? 117 GLY   A H    1 c 2 
ATOM   3340 H HA2  . GLY   B 1 105 ? 10.728 -4.558  17.299  1   49.645  ? 117 GLY   A HA2  1 c 2 
ATOM   3341 H HA3  . GLY   B 1 105 ? 10.139 -3.563  16.198  1   52.512  ? 117 GLY   A HA3  1 c 2 
ATOM   3342 N N    . SER   B 1 106 ? 9.56   -5.826  15.164  1   52.117  ? 118 SER   A N    1 ? 2 
ATOM   3343 C CA   . SER   B 1 106 ? 9.311  -6.935  14.259  1   53.579  ? 118 SER   A CA   1 ? 2 
ATOM   3344 C C    . SER   B 1 106 ? 7.92   -6.797  13.652  1   54.929  ? 118 SER   A C    1 ? 2 
ATOM   3345 O O    . SER   B 1 106 ? 7      -7.55   13.957  1   53.247  ? 118 SER   A O    1 ? 2 
ATOM   3346 C CB   . SER   B 1 106 ? 9.458  -8.265  14.973  1   53.872  ? 118 SER   A CB   1 ? 2 
ATOM   3347 O OG   . SER   B 1 106 ? 9.413  -9.309  14.018  1   56.779  ? 118 SER   A OG   1 ? 2 
ATOM   3348 H H    . SER   B 1 106 ? 8.849  -5.437  15.587  1   51.8    ? 118 SER   A H    1 c 2 
ATOM   3349 H HA   . SER   B 1 106 ? 9.976  -6.896  13.525  1   55.367  ? 118 SER   A HA   1 c 2 
ATOM   3350 H HB2  . SER   B 1 106 ? 10.309 -8.29   15.449  1   52.895  ? 118 SER   A HB2  1 c 2 
ATOM   3351 H HB3  . SER   B 1 106 ? 8.735  -8.375  15.619  1   52.373  ? 118 SER   A HB3  1 c 2 
ATOM   3352 H HG   . SER   B 1 106 ? 9.487  -10.097 14.48   0   30      ? 118 SER   A HG   1 c 2 
ATOM   3353 N N    . LEU   B 1 107 ? 7.799  -5.827  12.739  1   57.698  ? 119 LEU   A N    1 ? 2 
ATOM   3354 C CA   . LEU   B 1 107 ? 6.535  -5.491  12.122  1   61.31   ? 119 LEU   A CA   1 ? 2 
ATOM   3355 C C    . LEU   B 1 107 ? 6.055  -6.631  11.222  1   63.776  ? 119 LEU   A C    1 ? 2 
ATOM   3356 O O    . LEU   B 1 107 ? 6.874  -7.287  10.572  1   64.023  ? 119 LEU   A O    1 ? 2 
ATOM   3357 C CB   . LEU   B 1 107 ? 6.705  -4.192  11.321  1   65.797  ? 119 LEU   A CB   1 ? 2 
ATOM   3358 C CG   . LEU   B 1 107 ? 6.818  -2.905  12.145  1   65.23   ? 119 LEU   A CG   1 ? 2 
ATOM   3359 C CD1  . LEU   B 1 107 ? 6.858  -1.715  11.245  1   70.188  ? 119 LEU   A CD1  1 ? 2 
ATOM   3360 C CD2  . LEU   B 1 107 ? 5.694  -2.719  13.154  1   64.794  ? 119 LEU   A CD2  1 ? 2 
ATOM   3361 H H    . LEU   B 1 107 ? 8.544  -5.358  12.494  1   59.032  ? 119 LEU   A H    1 c 2 
ATOM   3362 H HA   . LEU   B 1 107 ? 5.872  -5.351  12.84   1   60.351  ? 119 LEU   A HA   1 c 2 
ATOM   3363 H HB2  . LEU   B 1 107 ? 7.513  -4.277  10.764  1   66.302  ? 119 LEU   A HB2  1 c 2 
ATOM   3364 H HB3  . LEU   B 1 107 ? 5.935  -4.104  10.713  1   67.145  ? 119 LEU   A HB3  1 c 2 
ATOM   3365 H HG   . LEU   B 1 107 ? 7.672  -2.938  12.647  1   64.519  ? 119 LEU   A HG   1 c 2 
ATOM   3366 H HD11 . LEU   B 1 107 ? 7.516  -1.86   10.545  1   70.916  ? 119 LEU   A HD11 1 c 2 
ATOM   3367 H HD12 . LEU   B 1 107 ? 7.1    -0.929  11.76   1   69.982  ? 119 LEU   A HD12 1 c 2 
ATOM   3368 H HD13 . LEU   B 1 107 ? 5.982  -1.582  10.843  1   71.24   ? 119 LEU   A HD13 1 c 2 
ATOM   3369 H HD21 . LEU   B 1 107 ? 5.791  -3.365  13.873  1   62.105  ? 119 LEU   A HD21 1 c 2 
ATOM   3370 H HD22 . LEU   B 1 107 ? 4.837  -2.852  12.714  1   65.65   ? 119 LEU   A HD22 1 c 2 
ATOM   3371 H HD23 . LEU   B 1 107 ? 5.732  -1.82   13.522  1   65.26   ? 119 LEU   A HD23 1 c 2 
ATOM   3372 N N    . PRO   B 1 108 ? 4.722  -6.839  11.058  1   64.265  ? 120 PRO   A N    1 ? 2 
ATOM   3373 C CA   . PRO   B 1 108 ? 3.688  -6.003  11.664  1   62.722  ? 120 PRO   A CA   1 ? 2 
ATOM   3374 C C    . PRO   B 1 108 ? 3.262  -6.431  13.055  1   60.305  ? 120 PRO   A C    1 ? 2 
ATOM   3375 O O    . PRO   B 1 108 ? 2.457  -5.748  13.66   1   66.547  ? 120 PRO   A O    1 ? 2 
ATOM   3376 C CB   . PRO   B 1 108 ? 2.484  -6.205  10.746  1   66.781  ? 120 PRO   A CB   1 ? 2 
ATOM   3377 C CG   . PRO   B 1 108 ? 2.658  -7.652  10.323  1   66.492  ? 120 PRO   A CG   1 ? 2 
ATOM   3378 C CD   . PRO   B 1 108 ? 4.155  -7.873  10.178  1   65.464  ? 120 PRO   A CD   1 ? 2 
ATOM   3379 H HA   . PRO   B 1 108 ? 3.965  -5.063  11.665  1   64.184  ? 120 PRO   A HA   1 c 2 
ATOM   3380 H HB2  . PRO   B 1 108 ? 1.643  -6.073  11.224  1   66.414  ? 120 PRO   A HB2  1 c 2 
ATOM   3381 H HB3  . PRO   B 1 108 ? 2.523  -5.605  9.976   1   68.915  ? 120 PRO   A HB3  1 c 2 
ATOM   3382 H HG2  . PRO   B 1 108 ? 2.288  -8.256  10.998  1   64.796  ? 120 PRO   A HG2  1 c 2 
ATOM   3383 H HG3  . PRO   B 1 108 ? 2.205  -7.82   9.473   1   68.825  ? 120 PRO   A HG3  1 c 2 
ATOM   3384 H HD2  . PRO   B 1 108 ? 4.415  -8.766  10.479  1   64.152  ? 120 PRO   A HD2  1 c 2 
ATOM   3385 H HD3  . PRO   B 1 108 ? 4.447  -7.743  9.255   1   67.753  ? 120 PRO   A HD3  1 c 2 
ATOM   3386 N N    . LYS   B 1 109 ? 3.807  -7.535  13.551  1   57.754  ? 121 LYS   A N    1 ? 2 
ATOM   3387 C CA   . LYS   B 1 109 ? 3.427  -8.07   14.851  1   58.887  ? 121 LYS   A CA   1 ? 2 
ATOM   3388 C C    . LYS   B 1 109 ? 3.867  -7.153  15.995  1   55.406  ? 121 LYS   A C    1 ? 2 
ATOM   3389 O O    . LYS   B 1 109 ? 3.098  -6.858  16.891  1   56.013  ? 121 LYS   A O    1 ? 2 
ATOM   3390 C CB   . LYS   B 1 109 ? 3.995  -9.483  15.02   1   54.598  ? 121 LYS   A CB   1 ? 2 
ATOM   3391 H H    . LYS   B 1 109 ? 4.442  -7.978  13.065  1   58.82   ? 121 LYS   A H    1 c 2 
ATOM   3392 H HA   . LYS   B 1 109 ? 2.438  -8.137  14.874  1   58.031  ? 121 LYS   A HA   1 c 2 
ATOM   3393 H HB2  . LYS   B 1 109 ? 4.851  -9.422  15.027  0   30      ? 121 LYS   A HB2  1 c 2 
ATOM   3394 H HB3  . LYS   B 1 109 ? 3.096  -10.03  15.104  0   30      ? 121 LYS   A HB3  1 c 2 
ATOM   3395 N N    . ILE   B 1 110 ? 5.123  -6.707  16.001  1   54.938  ? 122 ILE   A N    1 ? 2 
ATOM   3396 C CA   . ILE   B 1 110 ? 5.714  -6.054  17.159  1   52.266  ? 122 ILE   A CA   1 ? 2 
ATOM   3397 C C    . ILE   B 1 110 ? 6.207  -4.651  16.772  1   54.056  ? 122 ILE   A C    1 ? 2 
ATOM   3398 O O    . ILE   B 1 110 ? 7.071  -4.546  15.908  1   55.167  ? 122 ILE   A O    1 ? 2 
ATOM   3399 C CB   . ILE   B 1 110 ? 6.924  -6.878  17.663  1   50.41   ? 122 ILE   A CB   1 ? 2 
ATOM   3400 C CG1  . ILE   B 1 110 ? 6.609  -8.36   17.712  1   54.929  ? 122 ILE   A CG1  1 ? 2 
ATOM   3401 C CG2  . ILE   B 1 110 ? 7.415  -6.346  18.991  1   49.051  ? 122 ILE   A CG2  1 ? 2 
ATOM   3402 C CD1  . ILE   B 1 110 ? 5.569  -8.74   18.759  1   53.537  ? 122 ILE   A CD1  1 ? 2 
ATOM   3403 H H    . ILE   B 1 110 ? 5.635  -6.815  15.252  1   55.598  ? 122 ILE   A H    1 c 2 
ATOM   3404 H HA   . ILE   B 1 110 ? 5.052  -5.984  17.872  1   51.882  ? 122 ILE   A HA   1 c 2 
ATOM   3405 H HB   . ILE   B 1 110 ? 7.646  -6.76   17.016  1   52.262  ? 122 ILE   A HB   1 c 2 
ATOM   3406 H HG12 . ILE   B 1 110 ? 6.292  -8.647  16.832  1   54.737  ? 122 ILE   A HG12 1 c 2 
ATOM   3407 H HG13 . ILE   B 1 110 ? 7.437  -8.848  17.903  1   52.673  ? 122 ILE   A HG13 1 c 2 
ATOM   3408 H HG21 . ILE   B 1 110 ? 8.059  -6.965  19.37   1   47.843  ? 122 ILE   A HG21 1 c 2 
ATOM   3409 H HG22 . ILE   B 1 110 ? 6.665  -6.248  19.601  1   48.6    ? 122 ILE   A HG22 1 c 2 
ATOM   3410 H HG23 . ILE   B 1 110 ? 7.84   -5.482  18.86   1   50.076  ? 122 ILE   A HG23 1 c 2 
ATOM   3411 H HD11 . ILE   B 1 110 ? 5.923  -8.575  19.653  1   52.277  ? 122 ILE   A HD11 1 c 2 
ATOM   3412 H HD12 . ILE   B 1 110 ? 5.353  -9.687  18.667  1   53.175  ? 122 ILE   A HD12 1 c 2 
ATOM   3413 H HD13 . ILE   B 1 110 ? 4.759  -8.211  18.629  1   54.438  ? 122 ILE   A HD13 1 c 2 
ATOM   3414 N N    . PRO   B 1 111 ? 5.754  -3.534  17.392  1   53.996  ? 123 PRO   A N    1 ? 2 
ATOM   3415 C CA   . PRO   B 1 111 ? 6.315  -2.226  17.054  1   55.42   ? 123 PRO   A CA   1 ? 2 
ATOM   3416 C C    . PRO   B 1 111 ? 7.714  -2.006  17.627  1   53.415  ? 123 PRO   A C    1 ? 2 
ATOM   3417 O O    . PRO   B 1 111 ? 8.217  -2.822  18.403  1   50.478  ? 123 PRO   A O    1 ? 2 
ATOM   3418 C CB   . PRO   B 1 111 ? 5.296  -1.245  17.621  1   57.142  ? 123 PRO   A CB   1 ? 2 
ATOM   3419 C CG   . PRO   B 1 111 ? 4.71   -1.967  18.8    1   55.394  ? 123 PRO   A CG   1 ? 2 
ATOM   3420 C CD   . PRO   B 1 111 ? 4.722  -3.447  18.448  1   53.49   ? 123 PRO   A CD   1 ? 2 
ATOM   3421 H HA   . PRO   B 1 111 ? 6.346  -2.129  16.08   1   57.099  ? 123 PRO   A HA   1 c 2 
ATOM   3422 H HB2  . PRO   B 1 111 ? 5.729  -0.414  17.9    1   58.237  ? 123 PRO   A HB2  1 c 2 
ATOM   3423 H HB3  . PRO   B 1 111 ? 4.607  -1.038  16.96   1   58.979  ? 123 PRO   A HB3  1 c 2 
ATOM   3424 H HG2  . PRO   B 1 111 ? 5.243  -1.805  19.604  1   54.244  ? 123 PRO   A HG2  1 c 2 
ATOM   3425 H HG3  . PRO   B 1 111 ? 3.794  -1.666  18.968  1   56.193  ? 123 PRO   A HG3  1 c 2 
ATOM   3426 H HD2  . PRO   B 1 111 ? 4.969  -3.994  19.219  1   51.476  ? 123 PRO   A HD2  1 c 2 
ATOM   3427 H HD3  . PRO   B 1 111 ? 3.854  -3.74   18.109  1   54.014  ? 123 PRO   A HD3  1 c 2 
ATOM   3428 N N    . SER   B 1 112 ? 8.374  -0.936  17.182  1   54.221  ? 124 SER   A N    1 ? 2 
ATOM   3429 C CA   . SER   B 1 112 ? 9.636  -0.511  17.782  1   55.918  ? 124 SER   A CA   1 ? 2 
ATOM   3430 C C    . SER   B 1 112 ? 9.49   -0.367  19.295  1   52.429  ? 124 SER   A C    1 ? 2 
ATOM   3431 O O    . SER   B 1 112 ? 8.508  0.18    19.775  1   53.674  ? 124 SER   A O    1 ? 2 
ATOM   3432 C CB   . SER   B 1 112 ? 10.097 0.786   17.164  1   58.233  ? 124 SER   A CB   1 ? 2 
ATOM   3433 O OG   . SER   B 1 112 ? 11.217 1.328   17.862  1   57.587  ? 124 SER   A OG   1 ? 2 
ATOM   3434 H H    . SER   B 1 112 ? 8.031  -0.455  16.485  1   57.005  ? 124 SER   A H    1 c 2 
ATOM   3435 H HA   . SER   B 1 112 ? 10.316 -1.208  17.597  1   54.047  ? 124 SER   A HA   1 c 2 
ATOM   3436 H HB2  . SER   B 1 112 ? 10.342 0.628   16.232  1   59.33   ? 124 SER   A HB2  1 c 2 
ATOM   3437 H HB3  . SER   B 1 112 ? 9.364  1.428   17.181  1   59.573  ? 124 SER   A HB3  1 c 2 
ATOM   3438 H HG   . SER   B 1 112 ? 11.505 1.945   17.609  0   30      ? 124 SER   A HG   1 c 2 
ATOM   3439 N N    . ASN   B 1 113 ? 10.498 -0.829  20.037  1   55.185  ? 125 ASN   A N    1 ? 2 
ATOM   3440 C CA   . ASN   B 1 113 ? 10.663 -0.519  21.443  1   55.721  ? 125 ASN   A CA   1 ? 2 
ATOM   3441 C C    . ASN   B 1 113 ? 9.519  -1.083  22.285  1   55.513  ? 125 ASN   A C    1 ? 2 
ATOM   3442 O O    . ASN   B 1 113 ? 9.094  -0.425  23.242  1   54.602  ? 125 ASN   A O    1 ? 2 
ATOM   3443 C CB   . ASN   B 1 113 ? 10.841 0.979   21.675  1   57.405  ? 125 ASN   A CB   1 ? 2 
ATOM   3444 C CG   . ASN   B 1 113 ? 12.263 1.405   21.441  1   60.947  ? 125 ASN   A CG   1 ? 2 
ATOM   3445 O OD1  . ASN   B 1 113 ? 13.168 0.575   21.35   1   65.695  ? 125 ASN   A OD1  1 ? 2 
ATOM   3446 N ND2  . ASN   B 1 113 ? 12.465 2.692   21.208  1   68.701  ? 125 ASN   A ND2  1 ? 2 
ATOM   3447 H H    . ASN   B 1 113 ? 11.119 -1.37   19.641  1   53.876  ? 125 ASN   A H    1 c 2 
ATOM   3448 H HA   . ASN   B 1 113 ? 11.488 -0.959  21.746  1   54.648  ? 125 ASN   A HA   1 c 2 
ATOM   3449 H HB2  . ASN   B 1 113 ? 10.253 1.477   21.074  1   59.666  ? 125 ASN   A HB2  1 c 2 
ATOM   3450 H HB3  . ASN   B 1 113 ? 10.592 1.199   22.594  1   57.857  ? 125 ASN   A HB3  1 c 2 
ATOM   3451 H HD21 . ASN   B 1 113 ? 13.262 2.973   20.938  1   68.679  ? 125 ASN   A HD21 1 c 2 
ATOM   3452 H HD22 . ASN   B 1 113 ? 11.804 3.273   21.322  1   68.35   ? 125 ASN   A HD22 1 c 2 
ATOM   3453 N N    . ALA   B 1 114 ? 9.028  -2.289  21.939  1   49.176  ? 126 ALA   A N    1 ? 2 
ATOM   3454 C CA   . ALA   B 1 114 ? 7.858  -2.826  22.628  1   48.428  ? 126 ALA   A CA   1 ? 2 
ATOM   3455 C C    . ALA   B 1 114 ? 8.325  -3.604  23.865  1   45.073  ? 126 ALA   A C    1 ? 2 
ATOM   3456 O O    . ALA   B 1 114 ? 9.281  -4.363  23.797  1   45.378  ? 126 ALA   A O    1 ? 2 
ATOM   3457 C CB   . ALA   B 1 114 ? 7.026  -3.719  21.717  1   46.598  ? 126 ALA   A CB   1 ? 2 
ATOM   3458 H H    . ALA   B 1 114 ? 9.427  -2.781  21.279  1   50.102  ? 126 ALA   A H    1 c 2 
ATOM   3459 H HA   . ALA   B 1 114 ? 7.295  -2.062  22.932  1   49.137  ? 126 ALA   A HA   1 c 2 
ATOM   3460 H HB1  . ALA   B 1 114 ? 6.724  -3.21   20.947  1   48.621  ? 126 ALA   A HB1  1 c 2 
ATOM   3461 H HB2  . ALA   B 1 114 ? 7.565  -4.47   21.414  1   46.064  ? 126 ALA   A HB2  1 c 2 
ATOM   3462 H HB3  . ALA   B 1 114 ? 6.254  -4.054  22.203  1   46.328  ? 126 ALA   A HB3  1 c 2 
ATOM   3463 N N    . THR   B 1 115 ? 7.601  -3.407  24.965  1   50.459  ? 127 THR   A N    1 ? 2 
ATOM   3464 C CA   . THR   B 1 115 ? 7.628  -4.268  26.131  1   45.811  ? 127 THR   A CA   1 ? 2 
ATOM   3465 C C    . THR   B 1 115 ? 6.627  -5.403  25.947  1   45.117  ? 127 THR   A C    1 ? 2 
ATOM   3466 O O    . THR   B 1 115 ? 5.489  -5.183  25.523  1   46.354  ? 127 THR   A O    1 ? 2 
ATOM   3467 C CB   . THR   B 1 115 ? 7.307  -3.405  27.35   1   47.28   ? 127 THR   A CB   1 ? 2 
ATOM   3468 O OG1  . THR   B 1 115 ? 8.355  -2.453  27.445  1   44.461  ? 127 THR   A OG1  1 ? 2 
ATOM   3469 C CG2  . THR   B 1 115 ? 7.343  -4.207  28.659  1   48.913  ? 127 THR   A CG2  1 ? 2 
ATOM   3470 H H    . THR   B 1 115 ? 7.048  -2.68   24.987  1   49.677  ? 127 THR   A H    1 c 2 
ATOM   3471 H HA   . THR   B 1 115 ? 8.529  -4.64   26.23   1   45.772  ? 127 THR   A HA   1 c 2 
ATOM   3472 H HB   . THR   B 1 115 ? 6.44   -2.946  27.243  1   47.898  ? 127 THR   A HB   1 c 2 
ATOM   3473 H HG1  . THR   B 1 115 ? 9.091  -2.86   27.569  0   30      ? 127 THR   A HG1  1 c 2 
ATOM   3474 H HG21 . THR   B 1 115 ? 7.073  -3.635  29.397  1   48.956  ? 127 THR   A HG21 1 c 2 
ATOM   3475 H HG22 . THR   B 1 115 ? 8.244  -4.532  28.817  1   47.306  ? 127 THR   A HG22 1 c 2 
ATOM   3476 H HG23 . THR   B 1 115 ? 6.733  -4.962  28.598  1   47.127  ? 127 THR   A HG23 1 c 2 
ATOM   3477 N N    . LEU   B 1 116 ? 7.031  -6.638  26.352  1   44.189  ? 128 LEU   A N    1 ? 2 
ATOM   3478 C CA   . LEU   B 1 116 ? 6.198  -7.817  26.192  1   41.643  ? 128 LEU   A CA   1 ? 2 
ATOM   3479 C C    . LEU   B 1 116 ? 5.972  -8.46   27.56   1   41.766  ? 128 LEU   A C    1 ? 2 
ATOM   3480 O O    . LEU   B 1 116 ? 6.819  -8.361  28.447  1   41.977  ? 128 LEU   A O    1 ? 2 
ATOM   3481 C CB   . LEU   B 1 116 ? 6.837  -8.885  25.309  1   44.454  ? 128 LEU   A CB   1 ? 2 
ATOM   3482 C CG   . LEU   B 1 116 ? 7.278  -8.521  23.881  1   53.629  ? 128 LEU   A CG   1 ? 2 
ATOM   3483 C CD1  . LEU   B 1 116 ? 7.342  -9.801  23.06   1   54.065  ? 128 LEU   A CD1  1 ? 2 
ATOM   3484 C CD2  . LEU   B 1 116 ? 6.434  -7.506  23.219  1   52.007  ? 128 LEU   A CD2  1 ? 2 
ATOM   3485 H H    . LEU   B 1 116 ? 7.854  -6.733  26.739  1   43.158  ? 128 LEU   A H    1 c 2 
ATOM   3486 H HA   . LEU   B 1 116 ? 5.325  -7.548  25.809  1   43.621  ? 128 LEU   A HA   1 c 2 
ATOM   3487 H HB2  . LEU   B 1 116 ? 7.625  -9.234  25.787  1   44.555  ? 128 LEU   A HB2  1 c 2 
ATOM   3488 H HB3  . LEU   B 1 116 ? 6.205  -9.638  25.249  1   45.058  ? 128 LEU   A HB3  1 c 2 
ATOM   3489 H HG   . LEU   B 1 116 ? 8.198  -8.154  23.933  1   51.582  ? 128 LEU   A HG   1 c 2 
ATOM   3490 H HD11 . LEU   B 1 116 ? 7.955  -10.427 23.481  1   53.071  ? 128 LEU   A HD11 1 c 2 
ATOM   3491 H HD12 . LEU   B 1 116 ? 7.657  -9.595  22.164  1   54.597  ? 128 LEU   A HD12 1 c 2 
ATOM   3492 H HD13 . LEU   B 1 116 ? 6.457  -10.199 23.008  1   53.875  ? 128 LEU   A HD13 1 c 2 
ATOM   3493 H HD21 . LEU   B 1 116 ? 6.655  -6.625  23.562  1   53.35   ? 128 LEU   A HD21 1 c 2 
ATOM   3494 H HD22 . LEU   B 1 116 ? 5.498  -7.697  23.396  1   52.914  ? 128 LEU   A HD22 1 c 2 
ATOM   3495 H HD23 . LEU   B 1 116 ? 6.592  -7.525  22.26   1   53.676  ? 128 LEU   A HD23 1 c 2 
ATOM   3496 N N    . PHE   B 1 117 ? 4.846  -9.16   27.662  1   42.491  ? 129 PHE   A N    1 ? 2 
ATOM   3497 C CA   . PHE   B 1 117 ? 4.522  -9.971  28.817  1   40.957  ? 129 PHE   A CA   1 ? 2 
ATOM   3498 C C    . PHE   B 1 117 ? 4.184  -11.366 28.315  1   40.438  ? 129 PHE   A C    1 ? 2 
ATOM   3499 O O    . PHE   B 1 117 ? 3.419  -11.531 27.335  1   41.953  ? 129 PHE   A O    1 ? 2 
ATOM   3500 C CB   . PHE   B 1 117 ? 3.343  -9.327  29.548  1   45.278  ? 129 PHE   A CB   1 ? 2 
ATOM   3501 C CG   . PHE   B 1 117 ? 2.749  -10.24  30.61   1   51.099  ? 129 PHE   A CG   1 ? 2 
ATOM   3502 C CD1  . PHE   B 1 117 ? 1.764  -11.183 30.278  1   52.177  ? 129 PHE   A CD1  1 ? 2 
ATOM   3503 C CD2  . PHE   B 1 117 ? 3.186  -10.178 31.924  1   46.928  ? 129 PHE   A CD2  1 ? 2 
ATOM   3504 C CE1  . PHE   B 1 117 ? 1.2    -11.994 31.25   1   54.238  ? 129 PHE   A CE1  1 ? 2 
ATOM   3505 C CE2  . PHE   B 1 117 ? 2.604  -10.984 32.901  1   48.89   ? 129 PHE   A CE2  1 ? 2 
ATOM   3506 C CZ   . PHE   B 1 117 ? 1.659  -11.924 32.554  1   53.445  ? 129 PHE   A CZ   1 ? 2 
ATOM   3507 H H    . PHE   B 1 117 ? 4.246  -9.13   26.973  1   42.686  ? 129 PHE   A H    1 c 2 
ATOM   3508 H HA   . PHE   B 1 117 ? 5.305  -10.013 29.423  1   41.14   ? 129 PHE   A HA   1 c 2 
ATOM   3509 H HB2  . PHE   B 1 117 ? 3.65   -8.495  29.972  1   46.193  ? 129 PHE   A HB2  1 c 2 
ATOM   3510 H HB3  . PHE   B 1 117 ? 2.648  -9.102  28.89   1   46.568  ? 129 PHE   A HB3  1 c 2 
ATOM   3511 H HD1  . PHE   B 1 117 ? 1.458  -11.24  29.387  1   52.58   ? 129 PHE   A HD1  1 c 2 
ATOM   3512 H HD2  . PHE   B 1 117 ? 3.839  -9.542  32.169  1   48.255  ? 129 PHE   A HD2  1 c 2 
ATOM   3513 H HE1  . PHE   B 1 117 ? 0.544  -12.629 31.012  1   54.142  ? 129 PHE   A HE1  1 c 2 
ATOM   3514 H HE2  . PHE   B 1 117 ? 2.916  -10.939 33.791  1   49.601  ? 129 PHE   A HE2  1 c 2 
ATOM   3515 H HZ   . PHE   B 1 117 ? 1.277  -12.476 33.218  1   52.968  ? 129 PHE   A HZ   1 c 2 
ATOM   3516 N N    . PHE   B 1 118 ? 4.626  -12.369 29.09   1   41.641  ? 130 PHE   A N    1 ? 2 
ATOM   3517 C CA   . PHE   B 1 118 ? 4.258  -13.749 28.85   1   38.283  ? 130 PHE   A CA   1 ? 2 
ATOM   3518 C C    . PHE   B 1 118 ? 3.948  -14.436 30.165  1   42.767  ? 130 PHE   A C    1 ? 2 
ATOM   3519 O O    . PHE   B 1 118 ? 4.614  -14.183 31.175  1   38.413  ? 130 PHE   A O    1 ? 2 
ATOM   3520 C CB   . PHE   B 1 118 ? 5.344  -14.624 28.229  1   38.91   ? 130 PHE   A CB   1 ? 2 
ATOM   3521 C CG   . PHE   B 1 118 ? 5.769  -14.21  26.836  1   41.035  ? 130 PHE   A CG   1 ? 2 
ATOM   3522 C CD1  . PHE   B 1 118 ? 6.702  -13.197 26.665  1   42.233  ? 130 PHE   A CD1  1 ? 2 
ATOM   3523 C CD2  . PHE   B 1 118 ? 5.165  -14.79  25.722  1   40.392  ? 130 PHE   A CD2  1 ? 2 
ATOM   3524 C CE1  . PHE   B 1 118 ? 7.073  -12.813 25.409  1   45.131  ? 130 PHE   A CE1  1 ? 2 
ATOM   3525 C CE2  . PHE   B 1 118 ? 5.546  -14.386 24.468  1   42.786  ? 130 PHE   A CE2  1 ? 2 
ATOM   3526 C CZ   . PHE   B 1 118 ? 6.463  -13.375 24.314  1   40.238  ? 130 PHE   A CZ   1 ? 2 
ATOM   3527 H H    . PHE   B 1 118 ? 5.179  -12.18  29.793  1   40.041  ? 130 PHE   A H    1 c 2 
ATOM   3528 H HA   . PHE   B 1 118 ? 3.454  -13.773 28.27   1   40.646  ? 130 PHE   A HA   1 c 2 
ATOM   3529 H HB2  . PHE   B 1 118 ? 6.132  -14.606 28.818  1   38.621  ? 130 PHE   A HB2  1 c 2 
ATOM   3530 H HB3  . PHE   B 1 118 ? 5.017  -15.55  28.197  1   39.502  ? 130 PHE   A HB3  1 c 2 
ATOM   3531 H HD1  . PHE   B 1 118 ? 7.102  -12.797 27.42   1   41.933  ? 130 PHE   A HD1  1 c 2 
ATOM   3532 H HD2  . PHE   B 1 118 ? 4.518  -15.469 25.831  1   41.682  ? 130 PHE   A HD2  1 c 2 
ATOM   3533 H HE1  . PHE   B 1 118 ? 7.711  -12.126 25.295  1   43.117  ? 130 PHE   A HE1  1 c 2 
ATOM   3534 H HE2  . PHE   B 1 118 ? 5.146  -14.777 23.707  1   42.74   ? 130 PHE   A HE2  1 c 2 
ATOM   3535 H HZ   . PHE   B 1 118 ? 6.733  -13.117 23.447  1   42.629  ? 130 PHE   A HZ   1 c 2 
ATOM   3536 N N    . GLU   B 1 119 ? 2.928  -15.281 30.09   1   43.589  ? 131 GLU   A N    1 ? 2 
ATOM   3537 C CA   . GLU   B 1 119 ? 2.74   -16.371 31.025  1   47.269  ? 131 GLU   A CA   1 ? 2 
ATOM   3538 C C    . GLU   B 1 119 ? 3.221  -17.631 30.319  1   50.206  ? 131 GLU   A C    1 ? 2 
ATOM   3539 O O    . GLU   B 1 119 ? 2.766  -17.925 29.202  1   47.454  ? 131 GLU   A O    1 ? 2 
ATOM   3540 C CB   . GLU   B 1 119 ? 1.285  -16.499 31.458  1   47.089  ? 131 GLU   A CB   1 ? 2 
ATOM   3541 C CG   . GLU   B 1 119 ? 1.069  -17.662 32.421  1   56.071  ? 131 GLU   A CG   1 ? 2 
ATOM   3542 C CD   . GLU   B 1 119 ? -0.331 -17.701 32.993  1   53.409  ? 131 GLU   A CD   1 ? 2 
ATOM   3543 O OE1  . GLU   B 1 119 ? -0.578 -17.069 34.012  1   56.216  ? 131 GLU   A OE1  1 ? 2 
ATOM   3544 O OE2  . GLU   B 1 119 ? -1.181 -18.303 32.346  1   58.364  ? 131 GLU   A OE2  1 ? 2 
ATOM   3545 H H    . GLU   B 1 119 ? 2.31   -15.17  29.425  1   44.815  ? 131 GLU   A H    1 c 2 
ATOM   3546 H HA   . GLU   B 1 119 ? 3.303  -16.207 31.822  1   46.264  ? 131 GLU   A HA   1 c 2 
ATOM   3547 H HB2  . GLU   B 1 119 ? 1.007  -15.664 31.889  1   49.236  ? 131 GLU   A HB2  1 c 2 
ATOM   3548 H HB3  . GLU   B 1 119 ? 0.726  -16.626 30.663  1   49.774  ? 131 GLU   A HB3  1 c 2 
ATOM   3549 H HG2  . GLU   B 1 119 ? 1.239  -18.507 31.952  1   53.439  ? 131 GLU   A HG2  1 c 2 
ATOM   3550 H HG3  . GLU   B 1 119 ? 1.71   -17.593 33.16   1   52.493  ? 131 GLU   A HG3  1 c 2 
ATOM   3551 N N    . ILE   B 1 120 ? 4.106  -18.371 31.004  1   47.696  ? 132 ILE   A N    1 ? 2 
ATOM   3552 C CA   . ILE   B 1 120 ? 4.758  -19.538 30.427  1   47.065  ? 132 ILE   A CA   1 ? 2 
ATOM   3553 C C    . ILE   B 1 120 ? 4.581  -20.704 31.395  1   47.533  ? 132 ILE   A C    1 ? 2 
ATOM   3554 O O    . ILE   B 1 120 ? 4.868  -20.578 32.581  1   46.449  ? 132 ILE   A O    1 ? 2 
ATOM   3555 C CB   . ILE   B 1 120 ? 6.256  -19.308 30.177  1   44.681  ? 132 ILE   A CB   1 ? 2 
ATOM   3556 C CG1  . ILE   B 1 120 ? 6.548  -18.018 29.416  1   45.813  ? 132 ILE   A CG1  1 ? 2 
ATOM   3557 C CG2  . ILE   B 1 120 ? 6.854  -20.546 29.511  1   46.469  ? 132 ILE   A CG2  1 ? 2 
ATOM   3558 C CD1  . ILE   B 1 120 ? 7.992  -17.861 28.965  1   46.057  ? 132 ILE   A CD1  1 ? 2 
ATOM   3559 H H    . ILE   B 1 120 ? 4.308  -18.14  31.865  1   47.701  ? 132 ILE   A H    1 c 2 
ATOM   3560 H HA   . ILE   B 1 120 ? 4.328  -19.756 29.578  1   47.4    ? 132 ILE   A HA   1 c 2 
ATOM   3561 H HB   . ILE   B 1 120 ? 6.681  -19.22  31.054  1   45.219  ? 132 ILE   A HB   1 c 2 
ATOM   3562 H HG12 . ILE   B 1 120 ? 5.969  -17.986 28.626  1   45.792  ? 132 ILE   A HG12 1 c 2 
ATOM   3563 H HG13 . ILE   B 1 120 ? 6.314  -17.258 29.986  1   44.956  ? 132 ILE   A HG13 1 c 2 
ATOM   3564 H HG21 . ILE   B 1 120 ? 7.816  -20.44  29.425  1   46.036  ? 132 ILE   A HG21 1 c 2 
ATOM   3565 H HG22 . ILE   B 1 120 ? 6.462  -20.662 28.629  1   46.761  ? 132 ILE   A HG22 1 c 2 
ATOM   3566 H HG23 . ILE   B 1 120 ? 6.668  -21.332 30.051  1   47.167  ? 132 ILE   A HG23 1 c 2 
ATOM   3567 H HD11 . ILE   B 1 120 ? 8.587  -17.993 29.728  1   45.799  ? 132 ILE   A HD11 1 c 2 
ATOM   3568 H HD12 . ILE   B 1 120 ? 8.122  -16.963 28.606  1   45.41   ? 132 ILE   A HD12 1 c 2 
ATOM   3569 H HD13 . ILE   B 1 120 ? 8.202  -18.517 28.274  1   46.532  ? 132 ILE   A HD13 1 c 2 
ATOM   3570 N N    . GLU   B 1 121 ? 4.076  -21.813 30.847  1   47.013  ? 133 GLU   A N    1 ? 2 
ATOM   3571 C CA   . GLU   B 1 121 ? 4.049  -23.077 31.555  1   47.837  ? 133 GLU   A CA   1 ? 2 
ATOM   3572 C C    . GLU   B 1 121 ? 5.119  -23.995 30.951  1   49.494  ? 133 GLU   A C    1 ? 2 
ATOM   3573 O O    . GLU   B 1 121 ? 5.049  -24.312 29.755  1   51.51   ? 133 GLU   A O    1 ? 2 
ATOM   3574 C CB   . GLU   B 1 121 ? 2.657  -23.681 31.438  1   47.009  ? 133 GLU   A CB   1 ? 2 
ATOM   3575 C CG   . GLU   B 1 121 ? 2.578  -25.047 32.121  1   51.725  ? 133 GLU   A CG   1 ? 2 
ATOM   3576 C CD   . GLU   B 1 121 ? 1.178  -25.582 32.282  1   59.176  ? 133 GLU   A CD   1 ? 2 
ATOM   3577 O OE1  . GLU   B 1 121 ? 0.208  -24.859 31.929  1   61.917  ? 133 GLU   A OE1  1 ? 2 
ATOM   3578 O OE2  . GLU   B 1 121 ? 1.079  -26.733 32.763  1   55.997  ? 133 GLU   A OE2  1 ? 2 
ATOM   3579 H H    . GLU   B 1 121 ? 3.734  -21.779 30      1   47.611  ? 133 GLU   A H    1 c 2 
ATOM   3580 H HA   . GLU   B 1 121 ? 4.255  -22.915 32.508  1   47.36   ? 133 GLU   A HA   1 c 2 
ATOM   3581 H HB2  . GLU   B 1 121 ? 2.011  -23.068 31.846  1   47.862  ? 133 GLU   A HB2  1 c 2 
ATOM   3582 H HB3  . GLU   B 1 121 ? 2.428  -23.774 30.49   1   48.561  ? 133 GLU   A HB3  1 c 2 
ATOM   3583 H HG2  . GLU   B 1 121 ? 3.098  -25.694 31.601  1   53.097  ? 133 GLU   A HG2  1 c 2 
ATOM   3584 H HG3  . GLU   B 1 121 ? 2.99   -24.983 33.009  1   51.931  ? 133 GLU   A HG3  1 c 2 
ATOM   3585 N N    . LEU   B 1 122 ? 6.089  -24.413 31.775  1   45.838  ? 134 LEU   A N    1 ? 2 
ATOM   3586 C CA   . LEU   B 1 122 ? 7.062  -25.395 31.343  1   51.764  ? 134 LEU   A CA   1 ? 2 
ATOM   3587 C C    . LEU   B 1 122 ? 6.482  -26.805 31.474  1   58.473  ? 134 LEU   A C    1 ? 2 
ATOM   3588 O O    . LEU   B 1 122 ? 6.294  -27.306 32.579  1   59.664  ? 134 LEU   A O    1 ? 2 
ATOM   3589 C CB   . LEU   B 1 122 ? 8.379  -25.258 32.1    1   51.342  ? 134 LEU   A CB   1 ? 2 
ATOM   3590 C CG   . LEU   B 1 122 ? 9.502  -26.224 31.657  1   51.616  ? 134 LEU   A CG   1 ? 2 
ATOM   3591 C CD1  . LEU   B 1 122 ? 9.725  -26.124 30.157  1   51.716  ? 134 LEU   A CD1  1 ? 2 
ATOM   3592 C CD2  . LEU   B 1 122 ? 10.786 -25.907 32.361  1   49.342  ? 134 LEU   A CD2  1 ? 2 
ATOM   3593 H H    . LEU   B 1 122 ? 6.144  -24.077 32.623  1   47.209  ? 134 LEU   A H    1 c 2 
ATOM   3594 H HA   . LEU   B 1 122 ? 7.239  -25.231 30.383  1   51.274  ? 134 LEU   A HA   1 c 2 
ATOM   3595 H HB2  . LEU   B 1 122 ? 8.702  -24.334 31.991  1   49.32   ? 134 LEU   A HB2  1 c 2 
ATOM   3596 H HB3  . LEU   B 1 122 ? 8.201  -25.406 33.057  1   51.323  ? 134 LEU   A HB3  1 c 2 
ATOM   3597 H HG   . LEU   B 1 122 ? 9.234  -27.152 31.881  1   53.461  ? 134 LEU   A HG   1 c 2 
ATOM   3598 H HD11 . LEU   B 1 122 ? 8.972  -26.519 29.687  1   52.541  ? 134 LEU   A HD11 1 c 2 
ATOM   3599 H HD12 . LEU   B 1 122 ? 10.538 -26.601 29.919  1   52.982  ? 134 LEU   A HD12 1 c 2 
ATOM   3600 H HD13 . LEU   B 1 122 ? 9.812  -25.19  29.902  1   49.959  ? 134 LEU   A HD13 1 c 2 
ATOM   3601 H HD21 . LEU   B 1 122 ? 10.654 -25.972 33.321  1   50.119  ? 134 LEU   A HD21 1 c 2 
ATOM   3602 H HD22 . LEU   B 1 122 ? 11.067 -25.005 32.134  1   48.299  ? 134 LEU   A HD22 1 c 2 
ATOM   3603 H HD23 . LEU   B 1 122 ? 11.472 -26.538 32.086  1   51.441  ? 134 LEU   A HD23 1 c 2 
ATOM   3604 N N    . LEU   B 1 123 ? 6.179  -27.445 30.337  1   60.247  ? 135 LEU   A N    1 ? 2 
ATOM   3605 C CA   . LEU   B 1 123 ? 5.514  -28.745 30.345  1   61.324  ? 135 LEU   A CA   1 ? 2 
ATOM   3606 C C    . LEU   B 1 123 ? 6.566  -29.842 30.509  1   66.554  ? 135 LEU   A C    1 ? 2 
ATOM   3607 O O    . LEU   B 1 123 ? 6.426  -30.724 31.361  1   70.402  ? 135 LEU   A O    1 ? 2 
ATOM   3608 C CB   . LEU   B 1 123 ? 4.717  -28.981 29.062  1   60.746  ? 135 LEU   A CB   1 ? 2 
ATOM   3609 C CG   . LEU   B 1 123 ? 3.704  -27.891 28.679  1   61.354  ? 135 LEU   A CG   1 ? 2 
ATOM   3610 C CD1  . LEU   B 1 123 ? 3.153  -28.142 27.28   1   64.799  ? 135 LEU   A CD1  1 ? 2 
ATOM   3611 C CD2  . LEU   B 1 123 ? 2.558  -27.787 29.675  1   66.214  ? 135 LEU   A CD2  1 ? 2 
ATOM   3612 H H    . LEU   B 1 123 ? 6.393  -27.064 29.534  1   58.923  ? 135 LEU   A H    1 c 2 
ATOM   3613 H HA   . LEU   B 1 123 ? 4.898  -28.779 31.12   1   62.144  ? 135 LEU   A HA   1 c 2 
ATOM   3614 H HB2  . LEU   B 1 123 ? 5.355  -29.085 28.319  1   62.03   ? 135 LEU   A HB2  1 c 2 
ATOM   3615 H HB3  . LEU   B 1 123 ? 4.233  -29.834 29.155  1   64.136  ? 135 LEU   A HB3  1 c 2 
ATOM   3616 H HG   . LEU   B 1 123 ? 4.178  -27.02  28.666  1   59.769  ? 135 LEU   A HG   1 c 2 
ATOM   3617 H HD11 . LEU   B 1 123 ? 3.885  -28.158 26.64   1   64.189  ? 135 LEU   A HD11 1 c 2 
ATOM   3618 H HD12 . LEU   B 1 123 ? 2.533  -27.434 27.044  1   63.225  ? 135 LEU   A HD12 1 c 2 
ATOM   3619 H HD13 . LEU   B 1 123 ? 2.69   -28.997 27.262  1   66.711  ? 135 LEU   A HD13 1 c 2 
ATOM   3620 H HD21 . LEU   B 1 123 ? 2.915  -27.662 30.57   1   63.921  ? 135 LEU   A HD21 1 c 2 
ATOM   3621 H HD22 . LEU   B 1 123 ? 2.031  -28.603 29.65   1   67.147  ? 135 LEU   A HD22 1 c 2 
ATOM   3622 H HD23 . LEU   B 1 123 ? 1.994  -27.031 29.444  1   63.668  ? 135 LEU   A HD23 1 c 2 
ATOM   3623 N N    . ASP   B 1 124 ? 7.606  -29.789 29.675  1   65.954  ? 136 ASP   A N    1 ? 2 
ATOM   3624 C CA   . ASP   B 1 124 ? 8.642  -30.806 29.68   1   70.933  ? 136 ASP   A CA   1 ? 2 
ATOM   3625 C C    . ASP   B 1 124 ? 9.912  -30.282 29.013  1   73.566  ? 136 ASP   A C    1 ? 2 
ATOM   3626 O O    . ASP   B 1 124 ? 9.886  -29.287 28.268  1   66.232  ? 136 ASP   A O    1 ? 2 
ATOM   3627 C CB   . ASP   B 1 124 ? 8.155  -32.07  28.999  1   74.933  ? 136 ASP   A CB   1 ? 2 
ATOM   3628 C CG   . ASP   B 1 124 ? 8.902  -33.319 29.435  1   83.956  ? 136 ASP   A CG   1 ? 2 
ATOM   3629 O OD1  . ASP   B 1 124 ? 9.77   -33.194 30.337  1   86.53   ? 136 ASP   A OD1  1 ? 2 
ATOM   3630 O OD2  . ASP   B 1 124 ? 8.643  -34.368 28.837  1   83.507  ? 136 ASP   A OD2  1 ? 2 
ATOM   3631 H H    . ASP   B 1 124 ? 7.669  -29.099 29.079  1   65.015  ? 136 ASP   A H    1 c 2 
ATOM   3632 H HA   . ASP   B 1 124 ? 8.851  -31.02  30.616  1   71.625  ? 136 ASP   A HA   1 c 2 
ATOM   3633 H HB2  . ASP   B 1 124 ? 7.204  -32.2   29.193  1   76.428  ? 136 ASP   A HB2  1 c 2 
ATOM   3634 H HB3  . ASP   B 1 124 ? 8.255  -31.973 28.029  1   76.269  ? 136 ASP   A HB3  1 c 2 
ATOM   3635 N N    . PHE   B 1 125 ? 11.025 -30.973 29.305  1   72.006  ? 137 PHE   A N    1 ? 2 
ATOM   3636 C CA   . PHE   B 1 125 ? 12.28  -30.734 28.616  1   68.365  ? 137 PHE   A CA   1 ? 2 
ATOM   3637 C C    . PHE   B 1 125 ? 13.064 -32.043 28.529  1   72.977  ? 137 PHE   A C    1 ? 2 
ATOM   3638 O O    . PHE   B 1 125 ? 13.137 -32.776 29.508  1   73.525  ? 137 PHE   A O    1 ? 2 
ATOM   3639 C CB   . PHE   B 1 125 ? 13.075 -29.6   29.264  1   63.763  ? 137 PHE   A CB   1 ? 2 
ATOM   3640 C CG   . PHE   B 1 125 ? 13.501 -29.757 30.715  1   65.309  ? 137 PHE   A CG   1 ? 2 
ATOM   3641 C CD1  . PHE   B 1 125 ? 12.679 -29.314 31.745  1   67.723  ? 137 PHE   A CD1  1 ? 2 
ATOM   3642 C CD2  . PHE   B 1 125 ? 14.753 -30.249 31.052  1   70.056  ? 137 PHE   A CD2  1 ? 2 
ATOM   3643 C CE1  . PHE   B 1 125 ? 13.095 -29.407 33.073  1   68.575  ? 137 PHE   A CE1  1 ? 2 
ATOM   3644 C CE2  . PHE   B 1 125 ? 15.161 -30.344 32.386  1   71.585  ? 137 PHE   A CE2  1 ? 2 
ATOM   3645 C CZ   . PHE   B 1 125 ? 14.333 -29.921 33.392  1   67.775  ? 137 PHE   A CZ   1 ? 2 
ATOM   3646 H H    . PHE   B 1 125 ? 11     -31.606 29.964  1   73.503  ? 137 PHE   A H    1 c 2 
ATOM   3647 H HA   . PHE   B 1 125 ? 12.06  -30.453 27.691  1   68.445  ? 137 PHE   A HA   1 c 2 
ATOM   3648 H HB2  . PHE   B 1 125 ? 13.883 -29.455 28.723  1   64.876  ? 137 PHE   A HB2  1 c 2 
ATOM   3649 H HB3  . PHE   B 1 125 ? 12.54  -28.779 29.19   1   62.038  ? 137 PHE   A HB3  1 c 2 
ATOM   3650 H HD1  . PHE   B 1 125 ? 11.83  -28.953 31.543  1   65.365  ? 137 PHE   A HD1  1 c 2 
ATOM   3651 H HD2  . PHE   B 1 125 ? 15.335 -30.538 30.367  1   71.186  ? 137 PHE   A HD2  1 c 2 
ATOM   3652 H HE1  . PHE   B 1 125 ? 12.517 -29.122 33.763  1   66.721  ? 137 PHE   A HE1  1 c 2 
ATOM   3653 H HE2  . PHE   B 1 125 ? 16.009 -30.702 32.593  1   72.717  ? 137 PHE   A HE2  1 c 2 
ATOM   3654 H HZ   . PHE   B 1 125 ? 14.602 -29.994 34.294  1   69.469  ? 137 PHE   A HZ   1 c 2 
ATOM   3655 N N    . LYS   B 1 126 ? 13.612 -32.32  27.335  1   77.047  ? 138 LYS   A N    1 ? 2 
ATOM   3656 C CA   . LYS   B 1 126 ? 14.414 -33.509 27.056  1   78.281  ? 138 LYS   A CA   1 ? 2 
ATOM   3657 C C    . LYS   B 1 126 ? 15.751 -33.059 26.456  1   80.429  ? 138 LYS   A C    1 ? 2 
ATOM   3658 O O    . LYS   B 1 126 ? 15.816 -32.071 25.731  1   77.818  ? 138 LYS   A O    1 ? 2 
ATOM   3659 C CB   . LYS   B 1 126 ? 13.638 -34.46  26.134  1   79.283  ? 138 LYS   A CB   1 ? 2 
ATOM   3660 H H    . LYS   B 1 126 ? 13.481 -31.725 26.653  1   74.263  ? 138 LYS   A H    1 c 2 
ATOM   3661 H HA   . LYS   B 1 126 ? 14.595 -33.975 27.911  1   79.969  ? 138 LYS   A HA   1 c 2 
ATOM   3662 H HB2  . LYS   B 1 126 ? 14.336 -34.845 25.569  0   30      ? 138 LYS   A HB2  1 c 2 
ATOM   3663 H HB3  . LYS   B 1 126 ? 12.742 -34.199 26.274  0   30      ? 138 LYS   A HB3  1 c 2 
ATOM   3664 N N    . GLY   B 1 127 ? 16.847 -33.744 26.778  1   84.741  ? 139 GLY   A N    1 ? 2 
ATOM   3665 C CA   . GLY   B 1 127 ? 18.16  -33.268 26.353  1   87.126  ? 139 GLY   A CA   1 ? 2 
ATOM   3666 C C    . GLY   B 1 127 ? 18.412 -33.583 24.878  1   92.368  ? 139 GLY   A C    1 ? 2 
ATOM   3667 O O    . GLY   B 1 127 ? 18.045 -34.668 24.442  1   94.541  ? 139 GLY   A O    1 ? 2 
ATOM   3668 H H    . GLY   B 1 127 ? 16.784 -34.515 27.265  1   87.044  ? 139 GLY   A H    1 c 2 
ATOM   3669 H HA2  . GLY   B 1 127 ? 18.215 -32.297 26.497  1   84.044  ? 139 GLY   A HA2  1 c 2 
ATOM   3670 H HA3  . GLY   B 1 127 ? 18.854 -33.698 26.905  1   89.22   ? 139 GLY   A HA3  1 c 2 
ATOM   3671 N N    . GLU   B 1 128 ? 19.059 -32.658 24.133  1   95.282  ? 140 GLU   A N    1 ? 2 
ATOM   3672 C CA   . GLU   B 1 128 ? 19.275 -32.823 22.697  1   96.963  ? 140 GLU   A CA   1 ? 2 
ATOM   3673 C C    . GLU   B 1 128 ? 19.77  -34.267 22.444  1   106.957 ? 140 GLU   A C    1 ? 2 
ATOM   3674 O O    . GLU   B 1 128 ? 20.744 -34.671 23.11   1   109.559 ? 140 GLU   A O    1 ? 2 
ATOM   3675 C CB   . GLU   B 1 128 ? 20.225 -31.777 22.099  1   94.414  ? 140 GLU   A CB   1 ? 2 
ATOM   3676 O OXT  . GLU   B 1 128 ? 19.131 -34.968 21.634  1   109.614 ? 140 GLU   A OXT  1 ? 2 
ATOM   3677 H H    . GLU   B 1 128 ? 19.375 -31.903 24.54   1   91.649  ? 140 GLU   A H    1 c 2 
ATOM   3678 H HA   . GLU   B 1 128 ? 18.398 -32.719 22.247  1   96.452  ? 140 GLU   A HA   1 c 2 
ATOM   3679 H HB2  . GLU   B 1 128 ? 21.368 -32.364 22.474  0   30      ? 140 GLU   A HB2  1 c 2 
ATOM   3680 H HB3  . GLU   B 1 128 ? 20.056 -31.217 21.833  0   30      ? 140 GLU   A HB3  1 c 2 
HETATM 3681 C CAK  . A1IN4 C 2 .   ? 17.809 7.308   12.073  1   46.402  ? 201 A1IN4 B CAK  1 ? 1 
HETATM 3682 C CAL  . A1IN4 C 2 .   ? 16.981 8.492   11.833  1   49.836  ? 201 A1IN4 B CAL  1 ? 1 
HETATM 3683 C CAM  . A1IN4 C 2 .   ? 17.122 8.887   10.311  1   47.774  ? 201 A1IN4 B CAM  1 ? 1 
HETATM 3684 C CAN  . A1IN4 C 2 .   ? 16.717 7.727   9.413   1   44.295  ? 201 A1IN4 B CAN  1 ? 1 
HETATM 3685 C CAO  . A1IN4 C 2 .   ? 17.446 6.383   9.745   1   42.517  ? 201 A1IN4 B CAO  1 ? 1 
HETATM 3686 C CAJ  . A1IN4 C 2 .   ? 17.363 6.144   11.251  1   43.948  ? 201 A1IN4 B CAJ  1 ? 1 
HETATM 3687 C CAI  . A1IN4 C 2 .   ? 18.147 4.904   11.656  1   43.571  ? 201 A1IN4 B CAI  1 ? 1 
HETATM 3688 C CAB  . A1IN4 C 2 .   ? 17.569 3.682   11.138  1   43.874  ? 201 A1IN4 B CAB  1 ? 1 
HETATM 3689 O OAA  . A1IN4 C 2 .   ? 16.329 3.526   10.924  1   43.314  ? 201 A1IN4 B OAA  1 ? 1 
HETATM 3690 N N    . A1IN4 C 2 .   ? 18.345 2.596   10.847  1   43.682  ? 201 A1IN4 B N    1 ? 1 
HETATM 3691 C CAH  . A1IN4 C 2 .   ? 19.787 2.579   11.149  1   45.721  ? 201 A1IN4 B CAH  1 ? 1 
HETATM 3692 C CAG  . A1IN4 C 2 .   ? 20.656 1.802   10.229  1   45.138  ? 201 A1IN4 B CAG  1 ? 1 
HETATM 3693 C CAF  . A1IN4 C 2 .   ? 20.152 0.423   10.043  1   43.973  ? 201 A1IN4 B CAF  1 ? 1 
HETATM 3694 C CB   . A1IN4 C 2 .   ? 18.772 0.525   9.379   1   40.194  ? 201 A1IN4 B CB   1 ? 1 
HETATM 3695 C CA   . A1IN4 C 2 .   ? 17.786 1.257   10.419  1   42.85   ? 201 A1IN4 B CA   1 ? 1 
HETATM 3696 C C    . A1IN4 C 2 .   ? 17.549 0.36    11.542  1   46.124  ? 201 A1IN4 B C    1 ? 1 
HETATM 3697 O O    . A1IN4 C 2 .   ? 17.036 -0.734  11.384  1   44.329  ? 201 A1IN4 B O    1 ? 1 
HETATM 3698 O OBB  . A1IN4 C 2 .   ? 17.855 0.863   12.753  1   46.173  ? 201 A1IN4 B OBB  1 ? 1 
HETATM 3699 C CBA  . A1IN4 C 2 .   ? 17.543 0.007   13.96   1   48.658  ? 201 A1IN4 B CBA  1 ? 1 
HETATM 3700 C CAZ  . A1IN4 C 2 .   ? 17.888 0.604   15.253  1   50.405  ? 201 A1IN4 B CAZ  1 ? 1 
HETATM 3701 C CAY  . A1IN4 C 2 .   ? 19.204 1.275   15.258  1   52.292  ? 201 A1IN4 B CAY  1 ? 1 
HETATM 3702 C CAX  . A1IN4 C 2 .   ? 19.634 1.68    16.733  1   57.061  ? 201 A1IN4 B CAX  1 ? 1 
HETATM 3703 C CAW  . A1IN4 C 2 .   ? 18.596 2.544   17.507  1   56.742  ? 201 A1IN4 B CAW  1 ? 1 
HETATM 3704 O OAV  . A1IN4 C 2 .   ? 18.66  4.049   17.271  1   55.013  ? 201 A1IN4 B OAV  1 ? 1 
HETATM 3705 C CAU  . A1IN4 C 2 .   ? 18.567 4.328   15.943  1   51.541  ? 201 A1IN4 B CAU  1 ? 1 
HETATM 3706 C CAR  . A1IN4 C 2 .   ? 19.69  4.614   15.176  1   51.326  ? 201 A1IN4 B CAR  1 ? 1 
HETATM 3707 O OAS  . A1IN4 C 2 .   ? 20.817 4.789   15.895  1   55.894  ? 201 A1IN4 B OAS  1 ? 1 
HETATM 3708 C CAT  . A1IN4 C 2 .   ? 22.088 4.809   15.155  1   56.34   ? 201 A1IN4 B CAT  1 ? 1 
HETATM 3709 C CAQ  . A1IN4 C 2 .   ? 19.583 4.887   13.792  1   47.526  ? 201 A1IN4 B CAQ  1 ? 1 
HETATM 3710 C CAP  . A1IN4 C 2 .   ? 18.331 4.73    13.123  1   46.45   ? 201 A1IN4 B CAP  1 ? 1 
HETATM 3711 C CBH  . A1IN4 C 2 .   ? 17.216 4.381   13.95   1   46.226  ? 201 A1IN4 B CBH  1 ? 1 
HETATM 3712 C CBE  . A1IN4 C 2 .   ? 17.323 4.169   15.333  1   50.234  ? 201 A1IN4 B CBE  1 ? 1 
HETATM 3713 O OBF  . A1IN4 C 2 .   ? 16.322 3.878   16.196  1   50.039  ? 201 A1IN4 B OBF  1 ? 1 
HETATM 3714 C CBG  . A1IN4 C 2 .   ? 15.033 4.064   15.636  1   53.157  ? 201 A1IN4 B CBG  1 ? 1 
HETATM 3715 H HAK  . A1IN4 C 2 .   ? 17.798 6.992   13.037  1   48.495  ? 201 A1IN4 B HAK  1 c 1 
HETATM 3716 H HB6  . A1IN4 C 2 .   ? 18.719 7.76    11.761  1   48.598  ? 201 A1IN4 B HB6  1 c 1 
HETATM 3717 H HAL  . A1IN4 C 2 .   ? 17.327 9.314   12.463  1   51.679  ? 201 A1IN4 B HAL  1 c 1 
HETATM 3718 H HB7  . A1IN4 C 2 .   ? 15.94  8.267   12.063  1   48.025  ? 201 A1IN4 B HB7  1 c 1 
HETATM 3719 H HAM  . A1IN4 C 2 .   ? 18.152 9.164   10.094  1   49.183  ? 201 A1IN4 B HAM  1 c 1 
HETATM 3720 H HB8  . A1IN4 C 2 .   ? 16.474 9.738   10.103  1   48.353  ? 201 A1IN4 B HB8  1 c 1 
HETATM 3721 H HAN  . A1IN4 C 2 .   ? 16.94  7.994   8.381   1   43.694  ? 201 A1IN4 B HAN  1 c 1 
HETATM 3722 H HB9  . A1IN4 C 2 .   ? 15.644 7.57    9.511   1   43.161  ? 201 A1IN4 B HB9  1 c 1 
HETATM 3723 H HCA  . A1IN4 C 2 .   ? 16.978 5.536   9.368   1   40.995  ? 201 A1IN4 B HCA  1 c 1 
HETATM 3724 H HAO  . A1IN4 C 2 .   ? 18.478 6.428   9.607   1   43.734  ? 201 A1IN4 B HAO  1 c 1 
HETATM 3725 H HAJ  . A1IN4 C 2 .   ? 16.315 5.973   11.494  1   43.028  ? 201 A1IN4 B HAJ  1 c 1 
HETATM 3726 H HAI  . A1IN4 C 2 .   ? 19.13  5.048   11.224  1   44.881  ? 201 A1IN4 B HAI  1 c 1 
HETATM 3727 H HAH  . A1IN4 C 2 .   ? 19.925 2.179   12.152  1   47.21   ? 201 A1IN4 B HAH  1 c 1 
HETATM 3728 H HB5  . A1IN4 C 2 .   ? 20.188 3.583   11.138  1   46.881  ? 201 A1IN4 B HB5  1 c 1 
HETATM 3729 H HAG  . A1IN4 C 2 .   ? 21.612 1.675   10.607  1   47.124  ? 201 A1IN4 B HAG  1 c 1 
HETATM 3730 H HB4  . A1IN4 C 2 .   ? 20.65  2.159   9.254   1   44.25   ? 201 A1IN4 B HB4  1 c 1 
HETATM 3731 H HAF  . A1IN4 C 2 .   ? 19.953 -0.13   10.912  1   44.384  ? 201 A1IN4 B HAF  1 c 1 
HETATM 3732 H HB3  . A1IN4 C 2 .   ? 20.67  -0.118  9.312   1   43.349  ? 201 A1IN4 B HB3  1 c 1 
HETATM 3733 H HB2  . A1IN4 C 2 .   ? 18.722 1.201   8.58    1   40.327  ? 201 A1IN4 B HB2  1 c 1 
HETATM 3734 H HB1  . A1IN4 C 2 .   ? 18.26  -0.351  9.217   1   40.298  ? 201 A1IN4 B HB1  1 c 1 
HETATM 3735 H HA   . A1IN4 C 2 .   ? 16.837 1.413   9.908   1   41.37   ? 201 A1IN4 B HA   1 c 1 
HETATM 3736 H HCH  . A1IN4 C 2 .   ? 16.516 -0.022  14.084  1   47.704  ? 201 A1IN4 B HCH  1 c 1 
HETATM 3737 H HBA  . A1IN4 C 2 .   ? 17.964 -1.002  14.029  1   48.725  ? 201 A1IN4 B HBA  1 c 1 
HETATM 3738 H HCG  . A1IN4 C 2 .   ? 17.234 1.314   15.591  1   51.097  ? 201 A1IN4 B HCG  1 c 1 
HETATM 3739 H HAZ  . A1IN4 C 2 .   ? 18.037 -0.297  15.886  1   52.297  ? 201 A1IN4 B HAZ  1 c 1 
HETATM 3740 H HCF  . A1IN4 C 2 .   ? 19.985 0.635   15.002  1   52.554  ? 201 A1IN4 B HCF  1 c 1 
HETATM 3741 H HAY  . A1IN4 C 2 .   ? 19.225 2.166   14.742  1   51.539  ? 201 A1IN4 B HAY  1 c 1 
HETATM 3742 H HCE  . A1IN4 C 2 .   ? 19.74  0.893   17.415  1   58.215  ? 201 A1IN4 B HCE  1 c 1 
HETATM 3743 H HAX  . A1IN4 C 2 .   ? 20.366 2.488   16.766  1   58.026  ? 201 A1IN4 B HAX  1 c 1 
HETATM 3744 H HCD  . A1IN4 C 2 .   ? 17.615 2.392   17.261  1   54.689  ? 201 A1IN4 B HCD  1 c 1 
HETATM 3745 H HAW  . A1IN4 C 2 .   ? 18.761 2.443   18.525  1   59.506  ? 201 A1IN4 B HAW  1 c 1 
HETATM 3746 H HCC  . A1IN4 C 2 .   ? 22.914 4.734   15.861  1   59.571  ? 201 A1IN4 B HCC  1 c 1 
HETATM 3747 H HAT  . A1IN4 C 2 .   ? 22.178 5.745   14.604  1   56.371  ? 201 A1IN4 B HAT  1 c 1 
HETATM 3748 H HCB  . A1IN4 C 2 .   ? 22.13  3.969   14.463  1   54.048  ? 201 A1IN4 B HCB  1 c 1 
HETATM 3749 H HAQ  . A1IN4 C 2 .   ? 20.463 5.12    13.207  1   48.652  ? 201 A1IN4 B HAQ  1 c 1 
HETATM 3750 H HBH  . A1IN4 C 2 .   ? 16.249 4.273   13.466  1   44.822  ? 201 A1IN4 B HBH  1 c 1 
HETATM 3751 H HCJ  . A1IN4 C 2 .   ? 14.292 3.967   16.43   1   52.998  ? 201 A1IN4 B HCJ  1 c 1 
HETATM 3752 H HBG  . A1IN4 C 2 .   ? 14.839 3.299   14.886  1   49.271  ? 201 A1IN4 B HBG  1 c 1 
HETATM 3753 H HCI  . A1IN4 C 2 .   ? 14.941 5.058   15.195  1   51.211  ? 201 A1IN4 B HCI  1 c 1 
HETATM 3754 C CAK  . A1IN4 D 2 .   ? 3.142  -12.202 19.379  1   47.368  ? 201 A1IN4 A CAK  1 ? 2 
HETATM 3755 C CAL  . A1IN4 D 2 .   ? 2.353  -10.986 19.778  1   49.326  ? 201 A1IN4 A CAL  1 ? 2 
HETATM 3756 C CAM  . A1IN4 D 2 .   ? 2.116  -10.726 21.277  1   48.031  ? 201 A1IN4 A CAM  1 ? 2 
HETATM 3757 C CAN  . A1IN4 D 2 .   ? 3.453  -10.968 22.067  1   48.203  ? 201 A1IN4 A CAN  1 ? 2 
HETATM 3758 C CAO  . A1IN4 D 2 .   ? 4.097  -12.305 21.726  1   45.649  ? 201 A1IN4 A CAO  1 ? 2 
HETATM 3759 C CAJ  . A1IN4 D 2 .   ? 4.405  -12.358 20.256  1   47.357  ? 201 A1IN4 A CAJ  1 ? 2 
HETATM 3760 C CAI  . A1IN4 D 2 .   ? 5.118  -13.705 19.887  1   45.032  ? 201 A1IN4 A CAI  1 ? 2 
HETATM 3761 C CAB  . A1IN4 D 2 .   ? 6.471  -13.798 20.441  1   47.266  ? 201 A1IN4 A CAB  1 ? 2 
HETATM 3762 O OAA  . A1IN4 D 2 .   ? 7.136  -12.752 20.603  1   46.959  ? 201 A1IN4 A OAA  1 ? 2 
HETATM 3763 N N    . A1IN4 D 2 .   ? 7.005  -15.023 20.832  1   41.521  ? 201 A1IN4 A N    1 ? 2 
HETATM 3764 C CAH  . A1IN4 D 2 .   ? 6.242  -16.294 20.459  1   42.714  ? 201 A1IN4 A CAH  1 ? 2 
HETATM 3765 C CAG  . A1IN4 D 2 .   ? 6.4    -17.302 21.546  1   45.137  ? 201 A1IN4 A CAG  1 ? 2 
HETATM 3766 C CAF  . A1IN4 D 2 .   ? 7.854  -17.686 21.596  1   43.499  ? 201 A1IN4 A CAF  1 ? 2 
HETATM 3767 C CB   . A1IN4 D 2 .   ? 8.565  -16.492 22.273  1   42.781  ? 201 A1IN4 A CB   1 ? 2 
HETATM 3768 C CA   . A1IN4 D 2 .   ? 8.441  -15.238 21.351  1   42.836  ? 201 A1IN4 A CA   1 ? 2 
HETATM 3769 C C    . A1IN4 D 2 .   ? 9.298  -15.394 20.249  1   44.489  ? 201 A1IN4 A C    1 ? 2 
HETATM 3770 O O    . A1IN4 D 2 .   ? 10.506 -15.517 20.353  1   41.056  ? 201 A1IN4 A O    1 ? 2 
HETATM 3771 O OBB  . A1IN4 D 2 .   ? 8.685  -15.399 19.023  1   43.925  ? 201 A1IN4 A OBB  1 ? 2 
HETATM 3772 C CBA  . A1IN4 D 2 .   ? 9.471  -15.882 17.914  1   52.164  ? 201 A1IN4 A CBA  1 ? 2 
HETATM 3773 C CAZ  . A1IN4 D 2 .   ? 8.557  -15.672 16.692  1   55.955  ? 201 A1IN4 A CAZ  1 ? 2 
HETATM 3774 C CAY  . A1IN4 D 2 .   ? 8.209  -17.055 16.094  1   54.959  ? 201 A1IN4 A CAY  1 ? 2 
HETATM 3775 C CAX  . A1IN4 D 2 .   ? 7.038  -17.107 15.088  1   58.134  ? 201 A1IN4 A CAX  1 ? 2 
HETATM 3776 C CAW  . A1IN4 D 2 .   ? 6.802  -15.782 14.196  1   58.17   ? 201 A1IN4 A CAW  1 ? 2 
HETATM 3777 O OAV  . A1IN4 D 2 .   ? 5.503  -15.117 14.514  1   60.339  ? 201 A1IN4 A OAV  1 ? 2 
HETATM 3778 C CAU  . A1IN4 D 2 .   ? 5.377  -14.729 15.814  1   56.011  ? 201 A1IN4 A CAU  1 ? 2 
HETATM 3779 C CAR  . A1IN4 D 2 .   ? 4.564  -15.484 16.628  1   52.996  ? 201 A1IN4 A CAR  1 ? 2 
HETATM 3780 O OAS  . A1IN4 D 2 .   ? 3.925  -16.509 15.974  1   58.711  ? 201 A1IN4 A OAS  1 ? 2 
HETATM 3781 C CAT  . A1IN4 D 2 .   ? 2.876  -17.209 16.695  1   61.65   ? 201 A1IN4 A CAT  1 ? 2 
HETATM 3782 C CAQ  . A1IN4 D 2 .   ? 4.438  -15.125 17.968  1   51.88   ? 201 A1IN4 A CAQ  1 ? 2 
HETATM 3783 C CAP  . A1IN4 D 2 .   ? 5.18   -14.036 18.479  1   53.92   ? 201 A1IN4 A CAP  1 ? 2 
HETATM 3784 C CBH  . A1IN4 D 2 .   ? 6.041  -13.319 17.594  1   48.929  ? 201 A1IN4 A CBH  1 ? 2 
HETATM 3785 C CBE  . A1IN4 D 2 .   ? 6.143  -13.655 16.267  1   56.199  ? 201 A1IN4 A CBE  1 ? 2 
HETATM 3786 O OBF  . A1IN4 D 2 .   ? 6.959  -13.01  15.302  1   55.357  ? 201 A1IN4 A OBF  1 ? 2 
HETATM 3787 C CBG  . A1IN4 D 2 .   ? 7.652  -11.833 15.739  1   57.193  ? 201 A1IN4 A CBG  1 ? 2 
HETATM 3788 H HAK  . A1IN4 D 2 .   ? 3.599  -12.056 18.452  1   49.159  ? 201 A1IN4 A HAK  1 c 2 
HETATM 3789 H HB6  . A1IN4 D 2 .   ? 2.734  -13.245 19.527  1   48.325  ? 201 A1IN4 A HB6  1 c 2 
HETATM 3790 H HAL  . A1IN4 D 2 .   ? 1.377  -11.056 19.302  1   50.567  ? 201 A1IN4 A HAL  1 c 2 
HETATM 3791 H HB7  . A1IN4 D 2 .   ? 2.864  -10.114 19.374  1   49.406  ? 201 A1IN4 A HB7  1 c 2 
HETATM 3792 H HAM  . A1IN4 D 2 .   ? 1.347  -11.404 21.647  1   48.621  ? 201 A1IN4 A HAM  1 c 2 
HETATM 3793 H HB8  . A1IN4 D 2 .   ? 1.792  -9.695  21.421  1   49.11   ? 201 A1IN4 A HB8  1 c 2 
HETATM 3794 H HAN  . A1IN4 D 2 .   ? 3.241  -10.947 23.134  1   46.443  ? 201 A1IN4 A HAN  1 c 2 
HETATM 3795 H HB9  . A1IN4 D 2 .   ? 4.154  -10.172 21.828  1   47.304  ? 201 A1IN4 A HB9  1 c 2 
HETATM 3796 H HCA  . A1IN4 D 2 .   ? 5.044  -12.404 22.131  1   45.124  ? 201 A1IN4 A HCA  1 c 2 
HETATM 3797 H HAO  . A1IN4 D 2 .   ? 3.484  -13.161 21.831  1   46.387  ? 201 A1IN4 A HAO  1 c 2 
HETATM 3798 H HAJ  . A1IN4 D 2 .   ? 5.072  -11.532 20.022  1   46.585  ? 201 A1IN4 A HAJ  1 c 2 
HETATM 3799 H HAI  . A1IN4 D 2 .   ? 4.51   -14.457 20.372  1   47.125  ? 201 A1IN4 A HAI  1 c 2 
HETATM 3800 H HAH  . A1IN4 D 2 .   ? 6.612  -16.7   19.518  1   44.798  ? 201 A1IN4 A HAH  1 c 2 
HETATM 3801 H HB5  . A1IN4 D 2 .   ? 5.181  -16.121 20.379  1   44.006  ? 201 A1IN4 A HB5  1 c 2 
HETATM 3802 H HAG  . A1IN4 D 2 .   ? 6.015  -18.281 21.337  1   45.228  ? 201 A1IN4 A HAG  1 c 2 
HETATM 3803 H HB4  . A1IN4 D 2 .   ? 6.225  -16.955 22.52   1   42.855  ? 201 A1IN4 A HB4  1 c 2 
HETATM 3804 H HAF  . A1IN4 D 2 .   ? 8.349  -17.739 20.675  1   45.109  ? 201 A1IN4 A HAF  1 c 2 
HETATM 3805 H HB3  . A1IN4 D 2 .   ? 8.089  -18.456 22.27   1   43.884  ? 201 A1IN4 A HB3  1 c 2 
HETATM 3806 H HB2  . A1IN4 D 2 .   ? 8.117  -16.121 23.13   1   41.522  ? 201 A1IN4 A HB2  1 c 2 
HETATM 3807 H HB1  . A1IN4 D 2 .   ? 9.587  -16.685 22.363  1   42.574  ? 201 A1IN4 A HB1  1 c 2 
HETATM 3808 H HA   . A1IN4 D 2 .   ? 8.752  -14.36  21.916  1   41.705  ? 201 A1IN4 A HA   1 c 2 
HETATM 3809 H HCH  . A1IN4 D 2 .   ? 10.304 -15.306 17.623  1   51.45   ? 201 A1IN4 A HCH  1 c 2 
HETATM 3810 H HBA  . A1IN4 D 2 .   ? 9.65   -16.933 17.879  1   51.846  ? 201 A1IN4 A HBA  1 c 2 
HETATM 3811 H HCG  . A1IN4 D 2 .   ? 7.617  -15.448 17.008  1   54.161  ? 201 A1IN4 A HCG  1 c 2 
HETATM 3812 H HAZ  . A1IN4 D 2 .   ? 8.909  -14.957 15.961  1   55.818  ? 201 A1IN4 A HAZ  1 c 2 
HETATM 3813 H HCF  . A1IN4 D 2 .   ? 8.967  -17.373 15.461  1   57.24   ? 201 A1IN4 A HCF  1 c 2 
HETATM 3814 H HAY  . A1IN4 D 2 .   ? 7.892  -17.819 16.762  1   55.232  ? 201 A1IN4 A HAY  1 c 2 
HETATM 3815 H HCE  . A1IN4 D 2 .   ? 7.323  -17.723 14.32   1   59.665  ? 201 A1IN4 A HCE  1 c 2 
HETATM 3816 H HAX  . A1IN4 D 2 .   ? 6.143  -17.465 15.469  1   57.513  ? 201 A1IN4 A HAX  1 c 2 
HETATM 3817 H HCD  . A1IN4 D 2 .   ? 7.434  -14.968 14.356  1   58.149  ? 201 A1IN4 A HCD  1 c 2 
HETATM 3818 H HAW  . A1IN4 D 2 .   ? 6.498  -15.934 13.2    1   61.257  ? 201 A1IN4 A HAW  1 c 2 
HETATM 3819 H HCC  . A1IN4 D 2 .   ? 2.404  -17.935 16.034  1   62.922  ? 201 A1IN4 A HCC  1 c 2 
HETATM 3820 H HAT  . A1IN4 D 2 .   ? 2.127  -16.495 17.038  1   60.342  ? 201 A1IN4 A HAT  1 c 2 
HETATM 3821 H HCB  . A1IN4 D 2 .   ? 3.304  -17.729 17.551  1   59.338  ? 201 A1IN4 A HCB  1 c 2 
HETATM 3822 H HAQ  . A1IN4 D 2 .   ? 3.807  -15.704 18.626  1   52.064  ? 201 A1IN4 A HAQ  1 c 2 
HETATM 3823 H HBH  . A1IN4 D 2 .   ? 6.613  -12.48  17.989  1   50.386  ? 201 A1IN4 A HBH  1 c 2 
HETATM 3824 H HCJ  . A1IN4 D 2 .   ? 8.176  -11.4   14.89   1   57.847  ? 201 A1IN4 A HCJ  1 c 2 
HETATM 3825 H HBG  . A1IN4 D 2 .   ? 8.376  -12.099 16.506  1   54.821  ? 201 A1IN4 A HBG  1 c 2 
HETATM 3826 H HCI  . A1IN4 D 2 .   ? 6.942  -11.105 16.133  1   55.864  ? 201 A1IN4 A HCI  1 c 2 
HETATM 3827 O O    . HOH   E 3 .   ? 5.38   8.059   4.638   1   49.969  ? 301 HOH   B O    1 ? ? 
HETATM 3828 O O    . HOH   E 3 .   ? 7.996  7.128   -3.993  1   45.105  ? 302 HOH   B O    1 ? ? 
HETATM 3829 O O    . HOH   E 3 .   ? 4.582  3.76    -5.093  1   47.446  ? 303 HOH   B O    1 ? ? 
HETATM 3830 O O    . HOH   E 3 .   ? 14.362 14.244  -4.067  1   52.251  ? 304 HOH   B O    1 ? ? 
HETATM 3831 O O    . HOH   E 3 .   ? 32.945 4.779   -0.189  1   56.103  ? 305 HOH   B O    1 ? ? 
HETATM 3832 O O    . HOH   E 3 .   ? 8.027  5.824   -10.875 1   50.982  ? 306 HOH   B O    1 ? ? 
HETATM 3833 O O    . HOH   E 3 .   ? 7.358  0.232   14.895  1   46.496  ? 307 HOH   B O    1 ? ? 
HETATM 3834 O O    . HOH   E 3 .   ? 18.784 8.228   -6.463  1   49.179  ? 308 HOH   B O    1 ? ? 
HETATM 3835 O O    . HOH   E 3 .   ? 9.837  -8.553  -0.103  1   50.141  ? 309 HOH   B O    1 ? ? 
HETATM 3836 O O    . HOH   E 3 .   ? 12.777 10.538  1.422   1   55.424  ? 310 HOH   B O    1 ? ? 
HETATM 3837 O O    . HOH   E 3 .   ? 7.007  4.852   11.013  1   40.26   ? 311 HOH   B O    1 ? ? 
HETATM 3838 O O    . HOH   E 3 .   ? 28.136 0.675   14.74   1   55.038  ? 312 HOH   B O    1 ? ? 
HETATM 3839 O O    . HOH   E 3 .   ? 8.76   4.393   9.463   1   44.869  ? 313 HOH   B O    1 ? ? 
HETATM 3840 O O    . HOH   E 3 .   ? 6.259  -2.429  -8.496  1   49.163  ? 314 HOH   B O    1 ? ? 
HETATM 3841 O O    . HOH   E 3 .   ? 34.412 4.325   10.027  1   56.076  ? 315 HOH   B O    1 ? ? 
HETATM 3842 O O    . HOH   E 3 .   ? 9.157  3.007   -1.399  1   39.524  ? 316 HOH   B O    1 ? ? 
HETATM 3843 O O    . HOH   E 3 .   ? 9.49   -1.336  13.189  1   49.485  ? 317 HOH   B O    1 ? ? 
HETATM 3844 O O    . HOH   E 3 .   ? 18.552 -8.374  10.793  1   47.042  ? 318 HOH   B O    1 ? ? 
HETATM 3845 O O    . HOH   E 3 .   ? 6.65   -7.841  0.1     1   46.229  ? 319 HOH   B O    1 ? ? 
HETATM 3846 O O    . HOH   E 3 .   ? 10.43  -3.237  9.559   1   39.073  ? 320 HOH   B O    1 ? ? 
HETATM 3847 O O    . HOH   E 3 .   ? 7.246  -0.421  -9.477  1   44.434  ? 321 HOH   B O    1 ? ? 
HETATM 3848 O O    . HOH   E 3 .   ? 13.502 5.628   19.12   1   53.988  ? 322 HOH   B O    1 ? ? 
HETATM 3849 O O    . HOH   E 3 .   ? 6.637  6.7     0.292   1   45.714  ? 323 HOH   B O    1 ? ? 
HETATM 3850 O O    . HOH   E 3 .   ? 2.866  5.607   19.106  1   60.872  ? 324 HOH   B O    1 ? ? 
HETATM 3851 O O    . HOH   E 3 .   ? 1.399  2.424   0       0.5 45.448  ? 325 HOH   B O    1 ? ? 
HETATM 3852 O O    . HOH   E 3 .   ? 16.781 -7.456  18.361  1   55.903  ? 326 HOH   B O    1 ? ? 
HETATM 3853 O O    . HOH   E 3 .   ? 8.79   11.35   8.256   1   47.067  ? 327 HOH   B O    1 ? ? 
HETATM 3854 O O    . HOH   E 3 .   ? 2.667  -1.663  10.133  1   49.905  ? 328 HOH   B O    1 ? ? 
HETATM 3855 O O    . HOH   E 3 .   ? 7.814  5.194   -1.654  1   47.751  ? 329 HOH   B O    1 ? ? 
HETATM 3856 O O    . HOH   E 3 .   ? 8.693  15.057  0       0.5 72.036  ? 330 HOH   B O    1 ? ? 
HETATM 3857 O O    . HOH   F 3 .   ? 2.949  -5.204  37.761  1   55.163  ? 301 HOH   A O    1 ? ? 
HETATM 3858 O O    . HOH   F 3 .   ? 3.747  -8.412  43.614  1   61.054  ? 302 HOH   A O    1 ? ? 
HETATM 3859 O O    . HOH   F 3 .   ? 22.393 -29.518 27.231  1   48.842  ? 303 HOH   A O    1 ? ? 
HETATM 3860 O O    . HOH   F 3 .   ? 16.694 -20.275 21.623  1   54.062  ? 304 HOH   A O    1 ? ? 
HETATM 3861 O O    . HOH   F 3 .   ? 10.458 -4.018  19.7    1   43.282  ? 305 HOH   A O    1 ? ? 
HETATM 3862 O O    . HOH   F 3 .   ? 10.052 -5.856  21.731  1   42.964  ? 306 HOH   A O    1 ? ? 
HETATM 3863 O O    . HOH   F 3 .   ? 9.008  -23.839 40.345  1   54.735  ? 307 HOH   A O    1 ? ? 
HETATM 3864 O O    . HOH   F 3 .   ? 11.368 -5.692  32.698  1   51.342  ? 308 HOH   A O    1 ? ? 
HETATM 3865 O O    . HOH   F 3 .   ? 16.497 -3.247  29.103  1   51.926  ? 309 HOH   A O    1 ? ? 
HETATM 3866 O O    . HOH   F 3 .   ? 10.243 -4.085  12.403  1   40.716  ? 310 HOH   A O    1 ? ? 
HETATM 3867 O O    . HOH   F 3 .   ? -1.846 -25.918 33.395  1   49.613  ? 311 HOH   A O    1 ? ? 
HETATM 3868 O O    . HOH   F 3 .   ? 10.05  -27.163 42.285  1   82.751  ? 312 HOH   A O    1 ? ? 
HETATM 3869 O O    . HOH   F 3 .   ? 12.65  -18.215 39.773  1   46.369  ? 313 HOH   A O    1 ? ? 
HETATM 3870 O O    . HOH   F 3 .   ? 15.901 -11.017 21.733  1   43.961  ? 314 HOH   A O    1 ? ? 
HETATM 3871 O O    . HOH   F 3 .   ? 19.313 -16.035 34.903  1   50.003  ? 315 HOH   A O    1 ? ? 
HETATM 3872 O O    . HOH   F 3 .   ? 0.57   -7.428  39.631  1   53.211  ? 316 HOH   A O    1 ? ? 
HETATM 3873 O O    . HOH   F 3 .   ? 12.772 -2.035  34.76   1   45.868  ? 317 HOH   A O    1 ? ? 
HETATM 3874 O O    . HOH   F 3 .   ? 16.828 -1.816  21.46   1   48.682  ? 318 HOH   A O    1 ? ? 
HETATM 3875 O O    . HOH   F 3 .   ? -2.689 -13.651 25.551  1   61.002  ? 319 HOH   A O    1 ? ? 
HETATM 3876 O O    . HOH   F 3 .   ? 4.329  -5.295  43.43   1   56.908  ? 320 HOH   A O    1 ? ? 
HETATM 3877 O O    . HOH   F 3 .   ? 8.729  -15.071 42.199  1   48.17   ? 321 HOH   A O    1 ? ? 
HETATM 3878 O O    . HOH   F 3 .   ? -3.509 -24.787 37.585  1   59.326  ? 322 HOH   A O    1 ? ? 
HETATM 3879 O O    . HOH   F 3 .   ? 12.51  -0.461  37.079  1   52.682  ? 323 HOH   A O    1 ? ? 
HETATM 3880 O O    . HOH   F 3 .   ? 1.894  -20.695 18.813  1   56.978  ? 324 HOH   A O    1 ? ? 
HETATM 3881 O O    . HOH   F 3 .   ? 0.29   -20.141 30.025  1   61.657  ? 325 HOH   A O    1 ? ? 
HETATM 3882 O O    . HOH   F 3 .   ? 5.221  -9.377  36.408  1   56.956  ? 326 HOH   A O    1 ? ? 
HETATM 3883 O O    . HOH   F 3 .   ? -1.352 -22.264 29.793  1   58.259  ? 327 HOH   A O    1 ? ? 
HETATM 3884 O O    . HOH   F 3 .   ? 13.742 -14.511 17.431  1   54.158  ? 328 HOH   A O    1 ? ? 
HETATM 3885 O O    . HOH   F 3 .   ? -0.753 -8.354  35.662  1   57.735  ? 329 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   ? 1.45071  0.521651 0.817822 0.0358667   0.119704    0.2743      13  GLY   B N    
2    C CA   . GLY   A 1   ? 1.46481  0.553969 0.896422 -0.00379724 0.151525    0.277511    13  GLY   B CA   
3    C C    . GLY   A 1   ? 1.3683   0.542674 0.826732 -0.00931945 0.131001    0.258344    13  GLY   B C    
4    O O    . GLY   A 1   ? 1.36269  0.555503 0.761555 0.0199858   0.11525     0.256901    13  GLY   B O    
5    H H1   . GLY   A 1   ? 1.51418  0.532731 0.871319 0.0383315   0.130498    0.283482    13  GLY   B H1   
6    H H2   . GLY   A 1   ? 1.40869  0.524812 0.801806 0.0338876   0.0899873   0.253603    13  GLY   B H2   
7    H H3   . GLY   A 1   ? 1.49049  0.557284 0.801675 0.0615371   0.118955    0.284017    13  GLY   B H3   
8    H HA2  . GLY   A 1   ? 1.51559  0.560487 0.915276 0.00113688  0.186604    0.301518    13  GLY   B HA2  
9    H HA3  . GLY   A 1   ? 1.43654  0.524238 0.927339 -0.0310376  0.152624    0.268861    13  GLY   B HA3  
10   N N    . ALA   A 2   ? 1.3146   0.540439 0.864733 -0.0462368  0.127211    0.242002    14  ALA   B N    
11   C CA   . ALA   A 2   ? 1.21471  0.507485 0.796801 -0.0538939  0.11954     0.23021     14  ALA   B CA   
12   C C    . ALA   A 2   ? 1.18406  0.525967 0.737765 -0.031959   0.0740382   0.211238    14  ALA   B C    
13   O O    . ALA   A 2   ? 1.15077  0.515648 0.679108 -0.0203275  0.0714692   0.207982    14  ALA   B O    
14   C CB   . ALA   A 2   ? 1.16572  0.504438 0.853357 -0.0933177  0.119197    0.218247    14  ALA   B CB   
15   H H    . ALA   A 2   ? 1.2995   0.516818 0.893188 -0.0661938  0.12825     0.237657    14  ALA   B H    
16   H HA   . ALA   A 2   ? 1.26337  0.537625 0.815733 -0.0460751  0.146598    0.243809    14  ALA   B HA   
17   H HB1  . ALA   A 2   ? 1.19494  0.506867 0.908059 -0.108868   0.148515    0.230252    14  ALA   B HB1  
18   H HB2  . ALA   A 2   ? 1.13313  0.488183 0.843548 -0.0996481  0.0926673   0.204188    14  ALA   B HB2  
19   H HB3  . ALA   A 2   ? 1.12244  0.501429 0.830362 -0.095751   0.116036    0.212666    14  ALA   B HB3  
20   N N    . PRO   A 3   ? 1.09908  0.459496 0.660581 -0.0266998  0.0388932   0.19699     15  PRO   B N    
21   C CA   . PRO   A 3   ? 1.11736  0.529245 0.662952 -0.00758725 0.00029067  0.182394    15  PRO   B CA   
22   C C    . PRO   A 3   ? 1.12416  0.516924 0.588002 0.0294254   -0.00719612 0.18965     15  PRO   B C    
23   O O    . PRO   A 3   ? 1.0651   0.501808 0.522543 0.0372302   -0.0289178  0.178755    15  PRO   B O    
24   C CB   . PRO   A 3   ? 1.09453  0.522285 0.663332 -0.00718269 -0.0251404  0.169301    15  PRO   B CB   
25   C CG   . PRO   A 3   ? 1.14394  0.536578 0.755082 -0.0351648  -0.00557881 0.169793    15  PRO   B CG   
26   C CD   . PRO   A 3   ? 1.17352  0.505694 0.760924 -0.0384064  0.0360011   0.192663    15  PRO   B CD   
27   H HA   . PRO   A 3   ? 1.04965  0.502678 0.629205 -0.0200772  -0.00570609 0.174703    15  PRO   B HA   
28   H HB2  . PRO   A 3   ? 1.13459  0.541643 0.662196 0.0163662   -0.0323764  0.172236    15  PRO   B HB2  
29   H HB3  . PRO   A 3   ? 1.048    0.526759 0.646773 -0.0127087  -0.0444574  0.158106    15  PRO   B HB3  
30   H HG2  . PRO   A 3   ? 1.14948  0.520391 0.751777 -0.0288971  -0.0134931  0.164562    15  PRO   B HG2  
31   H HG3  . PRO   A 3   ? 1.08232  0.512331 0.744086 -0.056072   -0.0110407  0.161144    15  PRO   B HG3  
32   H HD2  . PRO   A 3   ? 1.22481  0.507779 0.767916 -0.0215603  0.0440009   0.202903    15  PRO   B HD2  
33   H HD3  . PRO   A 3   ? 1.16345  0.491122 0.797019 -0.0634442  0.0514497   0.193447    15  PRO   B HD3  
34   N N    . ALA   A 4   ? 1.2051   0.532609 0.608711 0.0523765   0.00761688  0.207211    16  ALA   B N    
35   C CA   . ALA   A 4   ? 1.30605  0.613402 0.624888 0.092422    -0.00196863 0.216326    16  ALA   B CA   
36   C C    . ALA   A 4   ? 1.33777  0.638665 0.617671 0.0952272   0.0152449   0.2205      16  ALA   B C    
37   O O    . ALA   A 4   ? 1.29885  0.619112 0.529976 0.120008    -0.0100248  0.212255    16  ALA   B O    
38   C CB   . ALA   A 4   ? 1.40046  0.63011  0.661252 0.11808     0.0151279   0.239538    16  ALA   B CB   
39   H H    . ALA   A 4   ? 1.2354   0.528759 0.65013  0.0437777   0.0227909   0.213815    16  ALA   B H    
40   H HA   . ALA   A 4   ? 1.26618  0.617023 0.590806 0.103292    -0.0333223  0.203333    16  ALA   B HA   
41   H HB1  . ALA   A 4   ? 1.3844   0.61706  0.667365 0.118843    0.0027208   0.233327    16  ALA   B HB1  
42   H HB2  . ALA   A 4   ? 1.43394  0.620399 0.694424 0.104982    0.048007    0.253892    16  ALA   B HB2  
43   H HB3  . ALA   A 4   ? 1.44596  0.663981 0.647208 0.148173    0.0062134   0.246853    16  ALA   B HB3  
44   N N    . THR   A 5   ? 1.31999  0.593606 0.620792 0.0718075   0.0580813   0.231883    17  THR   B N    
45   C CA   . THR   A 5   ? 1.32249  0.589007 0.588658 0.0755631   0.0813595   0.2342      17  THR   B CA   
46   C C    . THR   A 5   ? 1.19621  0.532443 0.50364  0.064303    0.0488309   0.20438     17  THR   B C    
47   O O    . THR   A 5   ? 1.17804  0.515131 0.439766 0.0781469   0.04637     0.194747    17  THR   B O    
48   C CB   . THR   A 5   ? 1.3085   0.543817 0.610781 0.0504543   0.137395    0.252895    17  THR   B CB   
49   O OG1  . THR   A 5   ? 1.37337  0.534562 0.6324   0.0602068   0.174662    0.284589    17  THR   B OG1  
50   C CG2  . THR   A 5   ? 1.32341  0.55754  0.59859  0.0552898   0.166542    0.252864    17  THR   B CG2  
51   H H    . THR   A 5   ? 1.30988  0.569363 0.649089 0.0535676   0.0738071   0.237502    17  THR   B H    
52   H HA   . THR   A 5   ? 1.3785   0.614532 0.569644 0.103902    0.08169     0.243007    17  THR   B HA   
53   H HB   . THR   A 5   ? 1.2452   0.510594 0.62307  0.0234664   0.133632    0.244556    17  THR   B HB   
55   H HG21 . THR   A 5   ? 1.34698  0.56184  0.64637  0.0419135   0.205653    0.268223    17  THR   B HG21 
56   H HG22 . THR   A 5   ? 1.3907   0.598068 0.585735 0.0834295   0.165717    0.257453    17  THR   B HG22 
57   H HG23 . THR   A 5   ? 1.27061  0.549039 0.583949 0.0449287   0.147508    0.232829    17  THR   B HG23 
58   N N    . VAL   A 6   ? 1.12769  0.518001 0.518165 0.0398923   0.0245809   0.189426    18  VAL   B N    
59   C CA   . VAL   A 6   ? 1.08573  0.535572 0.518374 0.0283103   -0.00275872 0.166347    18  VAL   B CA   
60   C C    . VAL   A 6   ? 1.08435  0.562379 0.482334 0.0506323   -0.0473202  0.151832    18  VAL   B C    
61   O O    . VAL   A 6   ? 1.04207  0.535951 0.423179 0.0550209   -0.0633009  0.135154    18  VAL   B O    
62   C CB   . VAL   A 6   ? 0.978792 0.476147 0.508404 -0.00379359 -0.00888332 0.1599      18  VAL   B CB   
63   C CG1  . VAL   A 6   ? 0.952325 0.504181 0.521288 -0.0131128  -0.035836   0.141288    18  VAL   B CG1  
64   C CG2  . VAL   A 6   ? 0.950535 0.430677 0.523384 -0.0257027  0.0309458   0.171099    18  VAL   B CG2  
65   H H    . VAL   A 6   ? 1.11184  0.499454 0.531924 0.0303683   0.0260268   0.193851    18  VAL   B H    
66   H HA   . VAL   A 6   ? 1.0962   0.535494 0.514943 0.0282198   0.0133381   0.164525    18  VAL   B HA   
67   H HB   . VAL   A 6   ? 0.96831  0.471695 0.507631 -0.00296861 -0.0213772  0.161221    18  VAL   B HB   
68   H HG11 . VAL   A 6   ? 0.967595 0.507856 0.515682 -0.00913328 -0.0276508  0.136516    18  VAL   B HG11 
69   H HG12 . VAL   A 6   ? 0.934468 0.506756 0.4943   -0.00414962 -0.0617543  0.134873    18  VAL   B HG12 
70   H HG13 . VAL   A 6   ? 0.896849 0.473691 0.521667 -0.0313493  -0.0348176  0.14089     18  VAL   B HG13 
71   H HG21 . VAL   A 6   ? 0.911463 0.419507 0.540764 -0.0432834  0.0233368   0.167856    18  VAL   B HG21 
72   H HG22 . VAL   A 6   ? 1.0066   0.446868 0.552476 -0.0206169  0.0519228   0.184367    18  VAL   B HG22 
73   H HG23 . VAL   A 6   ? 0.964924 0.446698 0.53755  -0.0264422  0.0431956   0.168284    18  VAL   B HG23 
74   N N    . THR   A 7   ? 1.07011  0.553225 0.459278 0.0657481   -0.067146   0.15662     19  THR   B N    
75   C CA   . THR   A 7   ? 1.1331   0.63812  0.482191 0.0946694   -0.105184   0.148163    19  THR   B CA   
76   C C    . THR   A 7   ? 1.21319  0.682317 0.474297 0.120219    -0.105031   0.146922    19  THR   B C    
77   O O    . THR   A 7   ? 1.24823  0.751648 0.501233 0.126429    -0.138488   0.126007    19  THR   B O    
78   C CB   . THR   A 7   ? 1.17617  0.667461 0.506717 0.118278    -0.1128     0.160805    19  THR   B CB   
79   O OG1  . THR   A 7   ? 1.07548  0.610674 0.484343 0.0954814   -0.119068   0.153852    19  THR   B OG1  
80   C CG2  . THR   A 7   ? 1.23288  0.742755 0.514866 0.156398    -0.149658   0.156705    19  THR   B CG2  
81   H H    . THR   A 7   ? 1.07007  0.544153 0.48122  0.0585947   -0.0575631  0.164177    19  THR   B H    
82   H HA   . THR   A 7   ? 1.07882  0.632839 0.471395 0.0836051   -0.127299   0.133969    19  THR   B HA   
83   H HB   . THR   A 7   ? 1.2144   0.653309 0.513949 0.123394    -0.0870856  0.176562    19  THR   B HB   
85   H HG21 . THR   A 7   ? 1.23133  0.742631 0.516322 0.170618    -0.155869   0.162828    19  THR   B HG21 
86   H HG22 . THR   A 7   ? 1.19367  0.753043 0.506162 0.148982    -0.173731   0.140541    19  THR   B HG22 
87   H HG23 . THR   A 7   ? 1.29413  0.76541  0.512408 0.175106    -0.143207   0.164149    19  THR   B HG23 
88   N N    . GLU   A 8   ? 1.30874  0.708452 0.504885 0.133681    -0.0664878  0.168545    20  GLU   B N    
89   C CA   . GLU   A 8   ? 1.44451  0.802302 0.535496 0.167754    -0.0645823  0.172367    20  GLU   B CA   
90   C C    . GLU   A 8   ? 1.45153  0.809704 0.53056  0.157264    -0.0541823  0.153523    20  GLU   B C    
91   O O    . GLU   A 8   ? 1.48394  0.839631 0.494391 0.181345    -0.0795195  0.13686     20  GLU   B O    
92   C CB   . GLU   A 8   ? 1.5598   0.836852 0.577677 0.188919    -0.0197478  0.208114    20  GLU   B CB   
93   C CG   . GLU   A 8   ? 1.54723  0.80181  0.571214 0.200266    -0.0204544  0.229111    20  GLU   B CG   
94   C CD   . GLU   A 8   ? 1.66564  0.832747 0.640901 0.209119    0.0328165   0.267289    20  GLU   B CD   
95   O OE1  . GLU   A 8   ? 1.70393  0.824013 0.621946 0.215151    0.073871    0.284372    20  GLU   B OE1  
96   O OE2  . GLU   A 8   ? 1.7013   0.844216 0.696579 0.21095     0.0351073   0.280692    20  GLU   B OE2  
97   H H    . GLU   A 8   ? 1.30334  0.681015 0.520721 0.121425    -0.0401567  0.181752    20  GLU   B H    
98   H HA   . GLU   A 8   ? 1.45516  0.83414  0.522664 0.187976    -0.0999355  0.163844    20  GLU   B HA   
99   H HB2  . GLU   A 8   ? 1.543    0.801663 0.583799 0.169169    0.0162631   0.215845    20  GLU   B HB2  
100  H HB3  . GLU   A 8   ? 1.62468  0.87694  0.56408  0.216546    -0.0227448  0.211072    20  GLU   B HB3  
101  H HG2  . GLU   A 8   ? 1.58281  0.849207 0.572606 0.227126    -0.0516981  0.225892    20  GLU   B HG2  
102  H HG3  . GLU   A 8   ? 1.48585  0.771883 0.582434 0.176481    -0.026531   0.220657    20  GLU   B HG3  
103  N N    . GLN   A 9   ? 1.32759  0.683713 0.466004 0.125969    -0.0165651  0.156201    21  GLN   B N    
104  C CA   . GLN   A 9   ? 1.39792  0.736744 0.514463 0.123225    0.00900768  0.145243    21  GLN   B CA   
105  C C    . GLN   A 9   ? 1.2821   0.672779 0.49579  0.089443    -0.00386769 0.121302    21  GLN   B C    
106  O O    . GLN   A 9   ? 1.33965  0.720302 0.548772 0.0864011   0.0137111   0.10788     21  GLN   B O    
107  C CB   . GLN   A 9   ? 1.4673   0.756305 0.571682 0.120005    0.0756052   0.173108    21  GLN   B CB   
108  C CG   . GLN   A 9   ? 1.57484  0.806922 0.618868 0.14004     0.104778    0.20964     21  GLN   B CG   
109  C CD   . GLN   A 9   ? 1.76046  0.954806 0.675742 0.186851    0.087599    0.213071    21  GLN   B CD   
110  O OE1  . GLN   A 9   ? 1.85127  1.05873  0.716806 0.203364    0.0584523   0.185229    21  GLN   B OE1  
111  N NE2  . GLN   A 9   ? 1.88257  1.02641  0.741288 0.209592    0.10424     0.246475    21  GLN   B NE2  
112  H H    . GLN   A 9   ? 1.30596  0.671514 0.499703 0.107665    -0.00635524 0.1648      21  GLN   B H    
113  H HA   . GLN   A 9   ? 1.45125  0.777574 0.499466 0.14608     -0.00736681 0.133849    21  GLN   B HA   
114  H HB2  . GLN   A 9   ? 1.40478  0.715972 0.587449 0.0933254   0.087878    0.17477     21  GLN   B HB2  
115  H HB3  . GLN   A 9   ? 1.51588  0.787596 0.578755 0.130488    0.0905849   0.165662    21  GLN   B HB3  
116  H HG2  . GLN   A 9   ? 1.53909  0.783544 0.625019 0.129793    0.091912    0.215372    21  GLN   B HG2  
117  H HG3  . GLN   A 9   ? 1.60785  0.813444 0.656817 0.133186    0.149441    0.226916    21  GLN   B HG3  
118  H HE21 . GLN   A 9   ? 1.93543  1.05632  0.715473 0.240243    0.0933695   0.251409    21  GLN   B HE21 
119  H HE22 . GLN   A 9   ? 1.84554  0.976952 0.744826 0.194621    0.125331    0.26358     21  GLN   B HE22 
120  N N    . GLY   A 10  ? 1.1868   0.628826 0.484193 0.0672472   -0.0313002  0.117729    22  GLY   B N    
121  C CA   . GLY   A 10  ? 1.10517  0.590831 0.496473 0.0357842   -0.0361683  0.104922    22  GLY   B CA   
122  C C    . GLY   A 10  ? 1.09115  0.595863 0.480005 0.0351875   -0.068325   0.0741606   22  GLY   B C    
123  O O    . GLY   A 10  ? 1.07808  0.593265 0.427799 0.0503776   -0.106148   0.0597575   22  GLY   B O    
124  H H    . GLY   A 10  ? 1.18234  0.631657 0.475792 0.0740423   -0.0467463  0.124181    22  GLY   B H    
125  H HA2  . GLY   A 10  ? 1.09903  0.570615 0.509086 0.0271442   -0.00442182 0.112646    22  GLY   B HA2  
126  H HA3  . GLY   A 10  ? 1.04549  0.561401 0.485705 0.023717    -0.0493359  0.109309    22  GLY   B HA3  
127  N N    . GLU   A 11  ? 1.05788  0.568177 0.496617 0.0168998   -0.0545808  0.0639611   23  GLU   B N    
128  C CA   . GLU   A 11  ? 1.07478  0.597403 0.528078 0.0097593   -0.0828807  0.0340305   23  GLU   B CA   
129  C C    . GLU   A 11  ? 0.955359 0.536851 0.495913 -0.0146048  -0.114986   0.0339951   23  GLU   B C    
130  O O    . GLU   A 11  ? 0.869956 0.476611 0.475747 -0.0311804  -0.101253   0.0536496   23  GLU   B O    
131  C CB   . GLU   A 11  ? 1.14532  0.641515 0.61503  0.00480784  -0.048517   0.0274523   23  GLU   B CB   
132  C CG   . GLU   A 11  ? 1.23368  0.721018 0.705968 0.00046752  -0.0712211  -0.00723616 23  GLU   B CG   
133  C CD   . GLU   A 11  ? 1.32436  0.796213 0.844957 -0.0081559  -0.0411044  -0.0112743  23  GLU   B CD   
134  O OE1  . GLU   A 11  ? 1.2832   0.754286 0.83248  -0.00785128 0.00052614  0.0125302   23  GLU   B OE1  
135  O OE2  . GLU   A 11  ? 1.38119  0.844023 0.921158 -0.016463   -0.060774   -0.038189   23  GLU   B OE2  
136  H H    . GLU   A 11  ? 1.04535  0.550526 0.512777 0.00869455  -0.0267673  0.0761813   23  GLU   B H    
137  H HA   . GLU   A 11  ? 1.12756  0.636166 0.522225 0.025934    -0.101754   0.0193454   23  GLU   B HA   
138  H HB2  . GLU   A 11  ? 1.19608  0.658572 0.613414 0.0210562   -0.0211913  0.0330074   23  GLU   B HB2  
139  H HB3  . GLU   A 11  ? 1.0898   0.605949 0.622277 -0.0105725  -0.0351459  0.0415423   23  GLU   B HB3  
140  H HG2  . GLU   A 11  ? 1.20189  0.7204   0.713239 -0.0133505  -0.102292   -0.0133578  23  GLU   B HG2  
141  H HG3  . GLU   A 11  ? 1.30793  0.76707  0.709225 0.0185659   -0.0779849  -0.0236511  23  GLU   B HG3  
142  N N    . ASP   A 12  ? 0.917577 0.523027 0.461499 -0.0169918  -0.157119   0.0118872   24  ASP   B N    
143  C CA   . ASP   A 12  ? 0.847362 0.50995  0.477585 -0.0407364  -0.181926   0.0138964   24  ASP   B CA   
144  C C    . ASP   A 12  ? 0.848805 0.50689  0.538531 -0.0636608  -0.173031   0.00620362  24  ASP   B C    
145  O O    . ASP   A 12  ? 0.863078 0.496426 0.53608  -0.0651565  -0.186208   -0.0217872  24  ASP   B O    
146  C CB   . ASP   A 12  ? 0.888288 0.58604  0.516245 -0.0373923  -0.228283   -0.00449602 24  ASP   B CB   
147  C CG   . ASP   A 12  ? 0.819159 0.580951 0.542046 -0.0620982  -0.247434   0.00162944  24  ASP   B CG   
148  O OD1  . ASP   A 12  ? 0.7915   0.564844 0.573401 -0.080698   -0.226023   0.0197887   24  ASP   B OD1  
149  O OD2  . ASP   A 12  ? 0.812808 0.615693 0.551958 -0.0614675  -0.28308    -0.0103571  24  ASP   B OD2  
150  H H    . ASP   A 12  ? 0.984025 0.571238 0.476496 -0.00357726 -0.170343   -0.00444993 24  ASP   B H    
151  H HA   . ASP   A 12  ? 0.813558 0.494764 0.468003 -0.0432876  -0.172254   0.03371     24  ASP   B HA   
152  H HB2  . ASP   A 12  ? 0.900392 0.598403 0.487283 -0.0184641  -0.233306   0.00196102  24  ASP   B HB2  
153  H HB3  . ASP   A 12  ? 0.929195 0.60796  0.532309 -0.0357922  -0.241848   -0.0275381  24  ASP   B HB3  
154  N N    . ILE   A 13  ? 0.774081 0.452648 0.529389 -0.0791531  -0.152874   0.0297513   25  ILE   B N    
155  C CA   . ILE   A 13  ? 0.785162 0.455529 0.596323 -0.0959637  -0.141876   0.0282916   25  ILE   B CA   
156  C C    . ILE   A 13  ? 0.747417 0.462328 0.634762 -0.119108   -0.162454   0.0356846   25  ILE   B C    
157  O O    . ILE   A 13  ? 0.756594 0.469838 0.698205 -0.132753   -0.152034   0.0450948   25  ILE   B O    
158  C CB   . ILE   A 13  ? 0.750493 0.411307 0.581747 -0.093585   -0.104954   0.050191    25  ILE   B CB   
159  C CG1  . ILE   A 13  ? 0.702765 0.403949 0.562756 -0.0976457  -0.103293   0.0765839   25  ILE   B CG1  
160  C CG2  . ILE   A 13  ? 0.797382 0.41149  0.563582 -0.0732814  -0.0763086  0.0437491   25  ILE   B CG2  
161  C CD1  . ILE   A 13  ? 0.730337 0.43415  0.628763 -0.100188   -0.0761449  0.0956353   25  ILE   B CD1  
162  H H    . ILE   A 13  ? 0.750949 0.447441 0.514487 -0.0776654  -0.147507   0.0464202   25  ILE   B H    
163  H HA   . ILE   A 13  ? 0.826666 0.46616  0.612371 -0.0922955  -0.144113   0.00773842  25  ILE   B HA   
164  H HB   . ILE   A 13  ? 0.744693 0.402909 0.615235 -0.101998   -0.0998894  0.0511347   25  ILE   B HB   
165  H HG12 . ILE   A 13  ? 0.723558 0.420803 0.544456 -0.0878398  -0.104973   0.0765866   25  ILE   B HG12 
166  H HG13 . ILE   A 13  ? 0.683089 0.414256 0.576087 -0.10743    -0.11954    0.0811334   25  ILE   B HG13 
167  H HG21 . ILE   A 13  ? 0.786379 0.398432 0.578089 -0.0739731  -0.0529648  0.0556973   25  ILE   B HG21 
168  H HG22 . ILE   A 13  ? 0.809684 0.423193 0.538125 -0.0643238  -0.0774498  0.0480987   25  ILE   B HG22 
169  H HG23 . ILE   A 13  ? 0.847312 0.433798 0.584146 -0.0675189  -0.0793557  0.0237631   25  ILE   B HG23 
170  H HD11 . ILE   A 13  ? 0.709138 0.411127 0.640675 -0.105403   -0.0725619  0.0958526   25  ILE   B HD11 
171  H HD12 . ILE   A 13  ? 0.677848 0.409081 0.596734 -0.104537   -0.0812716  0.108745    25  ILE   B HD12 
172  H HD13 . ILE   A 13  ? 0.736906 0.417331 0.607688 -0.0913969  -0.0574241  0.0945185   25  ILE   B HD13 
173  N N    . THR   A 14  ? 0.734608 0.490382 0.6293   -0.122041   -0.189708   0.0339491   26  THR   B N    
174  C CA   . THR   A 14  ? 0.711979 0.510468 0.681534 -0.14511    -0.205493   0.0405061   26  THR   B CA   
175  C C    . THR   A 14  ? 0.731622 0.506235 0.719288 -0.161209   -0.22492    0.0107258   26  THR   B C    
176  O O    . THR   A 14  ? 0.754175 0.495112 0.685313 -0.150346   -0.239646   -0.0205801  26  THR   B O    
177  C CB   . THR   A 14  ? 0.671432 0.529405 0.65493  -0.142076   -0.223984   0.0497959   26  THR   B CB   
178  O OG1  . THR   A 14  ? 0.705201 0.563242 0.643549 -0.128762   -0.251754   0.0244648   26  THR   B OG1  
179  C CG2  . THR   A 14  ? 0.615444 0.489655 0.584597 -0.128034   -0.205037   0.0759457   26  THR   B CG2  
180  H H    . THR   A 14  ? 0.7486   0.506845 0.604162 -0.108855   -0.196888   0.0304706   26  THR   B H    
181  H HA   . THR   A 14  ? 0.67517  0.478262 0.678249 -0.15196    -0.189401   0.0593568   26  THR   B HA   
182  H HB   . THR   A 14  ? 0.652771 0.539908 0.690678 -0.158531   -0.229603   0.0562803   26  THR   B HB   
184  H HG21 . THR   A 14  ? 0.606729 0.515532 0.581614 -0.122932   -0.215329   0.0802412   26  THR   B HG21 
185  H HG22 . THR   A 14  ? 0.63691  0.480835 0.559695 -0.114763   -0.196305   0.0722724   26  THR   B HG22 
186  H HG23 . THR   A 14  ? 0.594369 0.47379  0.595108 -0.136625   -0.191327   0.0917336   26  THR   B HG23 
187  N N    . SER   A 15  ? 0.706719 0.495249 0.77078  -0.186514   -0.224161   0.0213681   27  SER   B N    
188  C CA   . SER   A 15  ? 0.772685 0.542452 0.873917 -0.209355   -0.244831   -0.00535839 27  SER   B CA   
189  C C    . SER   A 15  ? 0.77439  0.590977 0.891653 -0.21803    -0.283345   -0.0252662  27  SER   B C    
190  O O    . SER   A 15  ? 0.80303  0.598442 0.916801 -0.228167   -0.3127     -0.063934   27  SER   B O    
191  C CB   . SER   A 15  ? 0.775523 0.546411 0.958182 -0.233967   -0.228899   0.0196164   27  SER   B CB   
192  O OG   . SER   A 15  ? 0.737768 0.458678 0.904721 -0.222761   -0.199989   0.0296812   27  SER   B OG   
193  H H    . SER   A 15  ? 0.676293 0.484708 0.769949 -0.189783   -0.210071   0.0466619   27  SER   B H    
194  H HA   . SER   A 15  ? 0.814877 0.53732  0.876813 -0.201824   -0.244139   -0.0279222  27  SER   B HA   
195  H HB2  . SER   A 15  ? 0.717039 0.531591 0.929041 -0.236929   -0.222975   0.0460471   27  SER   B HB2  
196  H HB3  . SER   A 15  ? 0.790521 0.552522 1.00694  -0.252974   -0.243884   0.00298759  27  SER   B HB3  
198  N N    . LYS   A 16  ? 0.722032 0.603894 0.858945 -0.212525   -0.284464   -0.00053114 28  LYS   B N    
199  C CA   . LYS   A 16  ? 0.773365 0.714658 0.938607 -0.216987   -0.318923   -0.0137303  28  LYS   B CA   
200  C C    . LYS   A 16  ? 0.780753 0.71584  0.85986  -0.185477   -0.343135   -0.0377705  28  LYS   B C    
201  O O    . LYS   A 16  ? 0.762729 0.741521 0.857494 -0.184916   -0.379448   -0.056127   28  LYS   B O    
202  C CB   . LYS   A 16  ? 0.767626 0.782046 0.988707 -0.218631   -0.30579    0.0236445   28  LYS   B CB   
203  C CG   . LYS   A 16  ? 0.782248 0.823453 1.1008   -0.251615   -0.289985   0.0483177   28  LYS   B CG   
204  C CD   . LYS   A 16  ? 0.802136 0.930116 1.17922  -0.25257    -0.286721   0.0741953   28  LYS   B CD   
205  C CE   . LYS   A 16  ? 0.827412 0.969969 1.1941   -0.238191   -0.24987    0.115824    28  LYS   B CE   
206  N NZ   . LYS   A 16  ? 0.863996 1.0078   1.29796  -0.264583   -0.224772   0.145919    28  LYS   B NZ   
207  H H    . LYS   A 16  ? 0.696937 0.587894 0.831114 -0.204667   -0.263839   0.0242163   28  LYS   B H    
208  H HA   . LYS   A 16  ? 0.794517 0.734441 1.00215  -0.238885   -0.335709   -0.0313316  28  LYS   B HA   
209  H HB2  . LYS   A 16  ? 0.736718 0.743273 0.922103 -0.201434   -0.285776   0.0415742   28  LYS   B HB2  
210  H HB3  . LYS   A 16  ? 0.763445 0.818057 0.989162 -0.211733   -0.32654    0.0154483   28  LYS   B HB3  
211  H HG2  . LYS   A 16  ? 0.818533 0.845957 1.17036  -0.272571   -0.305102   0.0290346   28  LYS   B HG2  
212  H HG3  . LYS   A 16  ? 0.774927 0.788553 1.08571  -0.250644   -0.26532    0.0672362   28  LYS   B HG3  
213  H HD2  . LYS   A 16  ? 0.803836 0.958106 1.15932  -0.236685   -0.305689   0.0611194   28  LYS   B HD2  
214  H HD3  . LYS   A 16  ? 0.812024 0.963143 1.2582   -0.277877   -0.291229   0.0753963   28  LYS   B HD3  
215  H HE2  . LYS   A 16  ? 0.814874 0.918369 1.12458  -0.222439   -0.241636   0.115147    28  LYS   B HE2  
216  H HE3  . LYS   A 16  ? 0.80056  0.990372 1.17205  -0.225617   -0.250296   0.124329    28  LYS   B HE3  
217  H HZ1  . LYS   A 16  ? 0.871894 0.970845 1.30593  -0.275933   -0.225414   0.137064    28  LYS   B HZ1  
218  H HZ2  . LYS   A 16  ? 0.852263 1.03598  1.3433   -0.279831   -0.228124   0.150519    28  LYS   B HZ2  
219  H HZ3  . LYS   A 16  ? 0.83076  0.979375 1.24935  -0.253428   -0.204496   0.169702    28  LYS   B HZ3  
220  N N    . LYS   A 17  ? 0.77477  0.658579 0.767262 -0.158619   -0.322313   -0.0348489  29  LYS   B N    
221  C CA   . LYS   A 17  ? 0.833349 0.700056 0.733469 -0.125305   -0.337444   -0.0500563  29  LYS   B CA   
222  C C    . LYS   A 17  ? 0.779699 0.709249 0.687598 -0.107968   -0.351747   -0.0340593  29  LYS   B C    
223  O O    . LYS   A 17  ? 0.777624 0.729649 0.658685 -0.0910377  -0.387171   -0.0523006  29  LYS   B O    
224  C CB   . LYS   A 17  ? 0.95672  0.789644 0.81356  -0.123552   -0.371476   -0.0949049  29  LYS   B CB   
225  C CG   . LYS   A 17  ? 1.0402   0.797533 0.864438 -0.128568   -0.350977   -0.112535   29  LYS   B CG   
226  C CD   . LYS   A 17  ? 1.07705  0.785473 0.814849 -0.0982854  -0.312518   -0.0964309  29  LYS   B CD   
227  C CE   . LYS   A 17  ? 1.16313  0.799982 0.859619 -0.0948389  -0.29073    -0.116301   29  LYS   B CE   
228  N NZ   . LYS   A 17  ? 1.10404  0.733887 0.864452 -0.111489   -0.25298    -0.0904039  29  LYS   B NZ   
229  H H    . LYS   A 17  ? 0.765074 0.62422  0.757632 -0.160675   -0.296558   -0.0208495  29  LYS   B H    
230  H HA   . LYS   A 17  ? 0.834025 0.66423  0.688628 -0.111909   -0.311976   -0.0396388  29  LYS   B HA   
231  H HB2  . LYS   A 17  ? 0.95746  0.824363 0.868798 -0.141899   -0.39793    -0.108279   29  LYS   B HB2  
232  H HB3  . LYS   A 17  ? 0.988564 0.816015 0.782176 -0.0986134  -0.383278   -0.101342   29  LYS   B HB3  
233  H HG2  . LYS   A 17  ? 1.00371  0.762312 0.887822 -0.150031   -0.336324   -0.101944   29  LYS   B HG2  
234  H HG3  . LYS   A 17  ? 1.09528  0.834242 0.896654 -0.129278   -0.376753   -0.144921   29  LYS   B HG3  
235  H HD2  . LYS   A 17  ? 1.10698  0.815573 0.786924 -0.0762288  -0.324089   -0.100279   29  LYS   B HD2  
236  H HD3  . LYS   A 17  ? 1.02068  0.74492  0.787017 -0.10097    -0.288825   -0.0676758  29  LYS   B HD3  
237  H HE2  . LYS   A 17  ? 1.20003  0.823624 0.898716 -0.103586   -0.314451   -0.146117   29  LYS   B HE2  
238  H HE3  . LYS   A 17  ? 1.1917   0.799045 0.816359 -0.0710803  -0.277157   -0.116446   29  LYS   B HE3  
239  H HZ1  . LYS   A 17  ? 1.07172  0.729342 0.895649 -0.131819   -0.262626   -0.0849022  29  LYS   B HZ1  
240  H HZ2  . LYS   A 17  ? 1.07075  0.708895 0.824292 -0.102757   -0.232066   -0.0665906  29  LYS   B HZ2  
241  H HZ3  . LYS   A 17  ? 1.14007  0.729242 0.883953 -0.109191   -0.240662   -0.103326   29  LYS   B HZ3  
242  N N    . ASP   A 18  ? 0.703265 0.658385 0.641801 -0.107717   -0.323923   -0.00026526 30  ASP   B N    
243  C CA   . ASP   A 18  ? 0.69232  0.703934 0.64378  -0.0898611  -0.329522   0.0170372   30  ASP   B CA   
244  C C    . ASP   A 18  ? 0.690488 0.66625  0.569951 -0.0607458  -0.304968   0.0349097   30  ASP   B C    
245  O O    . ASP   A 18  ? 0.671872 0.681031 0.560851 -0.0461919  -0.299208   0.0525486   30  ASP   B O    
246  C CB   . ASP   A 18  ? 0.621727 0.694114 0.667791 -0.112436   -0.318219   0.0388083   30  ASP   B CB   
247  C CG   . ASP   A 18  ? 0.613615 0.664929 0.675316 -0.124939   -0.28005    0.0648226   30  ASP   B CG   
248  O OD1  . ASP   A 18  ? 0.573214 0.569743 0.578774 -0.114795   -0.260625   0.0680989   30  ASP   B OD1  
249  O OD2  . ASP   A 18  ? 0.579332 0.672086 0.712355 -0.144483   -0.269732   0.0832402   30  ASP   B OD2  
250  H H    . ASP   A 18  ? 0.689586 0.625123 0.639643 -0.117235   -0.300522   0.0117311   30  ASP   B H    
251  H HA   . ASP   A 18  ? 0.713337 0.747362 0.659616 -0.0807965  -0.357652   0.00206152  30  ASP   B HA   
252  H HB2  . ASP   A 18  ? 0.618349 0.730418 0.672593 -0.0980123  -0.322014   0.0477261   30  ASP   B HB2  
253  H HB3  . ASP   A 18  ? 0.639696 0.731798 0.734551 -0.132787   -0.333487   0.027584    30  ASP   B HB3  
254  N N    . ARG   A 19  ? 0.722198 0.628796 0.535746 -0.0539975  -0.287423   0.0302451   31  ARG   B N    
255  C CA   . ARG   A 19  ? 0.726293 0.590117 0.479047 -0.0331005  -0.260091   0.0470309   31  ARG   B CA   
256  C C    . ARG   A 19  ? 0.678582 0.561337 0.472199 -0.0413038  -0.236178   0.0711439   31  ARG   B C    
257  O O    . ARG   A 19  ? 0.663205 0.528154 0.421935 -0.0236574  -0.222668   0.0836584   31  ARG   B O    
258  C CB   . ARG   A 19  ? 0.771537 0.626125 0.45589  0.00272512  -0.274785   0.0467024   31  ARG   B CB   
259  C CG   . ARG   A 19  ? 0.821397 0.65304  0.448403 0.0161443   -0.300858   0.0222728   31  ARG   B CG   
260  C CD   . ARG   A 19  ? 0.895897 0.710426 0.440876 0.058143    -0.315472   0.0260197   31  ARG   B CD   
261  N NE   . ARG   A 19  ? 0.909714 0.676762 0.408274 0.0754423   -0.279581   0.052507    31  ARG   B NE   
262  C CZ   . ARG   A 19  ? 0.983182 0.678662 0.408318 0.0859578   -0.249426   0.0606696   31  ARG   B CZ   
263  N NH1  . ARG   A 19  ? 1.01054  0.671203 0.394494 0.0832556   -0.245237   0.0449172   31  ARG   B NH1  
264  N NH2  . ARG   A 19  ? 1.04872  0.702845 0.439677 0.100352    -0.219846   0.0852454   31  ARG   B NH2  
265  H H    . ARG   A 19  ? 0.745312 0.629681 0.553887 -0.0633582  -0.291616   0.015414    31  ARG   B H    
266  H HA   . ARG   A 19  ? 0.75035  0.571459 0.474144 -0.0353205  -0.245762   0.042682    31  ARG   B HA   
267  H HB2  . ARG   A 19  ? 0.749785 0.647573 0.462805 0.00845067  -0.288472   0.0506406   31  ARG   B HB2  
268  H HB3  . ARG   A 19  ? 0.775899 0.595633 0.423717 0.0133643   -0.253446   0.059095    31  ARG   B HB3  
269  H HG2  . ARG   A 19  ? 0.849896 0.639579 0.449625 0.0108494   -0.284843   0.0172848   31  ARG   B HG2  
270  H HG3  . ARG   A 19  ? 0.822802 0.690805 0.491199 0.00387234  -0.32557    0.00747892  31  ARG   B HG3  
271  H HD2  . ARG   A 19  ? 0.951097 0.739968 0.445746 0.0678513   -0.327221   0.011355    31  ARG   B HD2  
272  H HD3  . ARG   A 19  ? 0.885377 0.746937 0.459476 0.0652346   -0.339198   0.0245662   31  ARG   B HD3  
273  H HE   . ARG   A 19  ? 0.885665 0.671542 0.408073 0.0784999   -0.276133   0.0638299   31  ARG   B HE   
274  H HH11 . ARG   A 19  ? 0.993913 0.668272 0.414247 0.0636531   -0.249457   0.0316641   31  ARG   B HH11 
275  H HH12 . ARG   A 19  ? 1.07534  0.696724 0.393203 0.102347    -0.236887   0.0479486   31  ARG   B HH12 
276  H HH21 . ARG   A 19  ? 1.00625  0.677227 0.420024 0.103657    -0.22123    0.093973    31  ARG   B HH21 
277  H HH22 . ARG   A 19  ? 1.06932  0.678008 0.415901 0.106306    -0.197994   0.0924629   31  ARG   B HH22 
278  N N    . GLY   A 20  ? 0.626615 0.539626 0.490253 -0.0674712  -0.230886   0.0774512   32  GLY   B N    
279  C CA   . GLY   A 20  ? 0.568463 0.504533 0.464583 -0.0722196  -0.212853   0.0991696   32  GLY   B CA   
280  C C    . GLY   A 20  ? 0.563545 0.45474  0.439061 -0.0749529  -0.187073   0.1075      32  GLY   B C    
281  O O    . GLY   A 20  ? 0.565856 0.463125 0.441957 -0.0705523  -0.176275   0.120103    32  GLY   B O    
282  H H    . GLY   A 20  ? 0.630925 0.546523 0.51818  -0.0812869  -0.238659   0.068039    32  GLY   B H    
283  H HA2  . GLY   A 20  ? 0.569782 0.524025 0.455329 -0.0574177  -0.216608   0.103535    32  GLY   B HA2  
284  H HA3  . GLY   A 20  ? 0.549101 0.514536 0.493853 -0.0876074  -0.214078   0.104336    32  GLY   B HA3  
285  N N    . VAL   A 21  ? 0.57173  0.420741 0.431037 -0.0810788  -0.178629   0.0980101   33  VAL   B N    
286  C CA   . VAL   A 21  ? 0.639652 0.452317 0.490186 -0.0837034  -0.152835   0.105231    33  VAL   B CA   
287  C C    . VAL   A 21  ? 0.675003 0.436159 0.465555 -0.0713452  -0.144149   0.092447    33  VAL   B C    
288  O O    . VAL   A 21  ? 0.705318 0.452136 0.488228 -0.0738752  -0.151115   0.0762172   33  VAL   B O    
289  C CB   . VAL   A 21  ? 0.578989 0.398031 0.484715 -0.102277   -0.141992   0.112949    33  VAL   B CB   
290  C CG1  . VAL   A 21  ? 0.611681 0.406751 0.51803  -0.102184   -0.117951   0.121367    33  VAL   B CG1  
291  C CG2  . VAL   A 21  ? 0.570477 0.438789 0.528402 -0.112593   -0.150327   0.12815     33  VAL   B CG2  
292  H H    . VAL   A 21  ? 0.6111   0.455506 0.466713 -0.0831979  -0.189444   0.085486    33  VAL   B H    
293  H HA   . VAL   A 21  ? 0.604849 0.419908 0.448702 -0.0785145  -0.147154   0.113799    33  VAL   B HA   
294  H HB   . VAL   A 21  ? 0.616715 0.421388 0.523804 -0.106406   -0.144595   0.102271    33  VAL   B HB   
295  H HG11 . VAL   A 21  ? 0.590454 0.392831 0.490444 -0.0986283  -0.116999   0.127772    33  VAL   B HG11 
296  H HG12 . VAL   A 21  ? 0.631002 0.394454 0.508635 -0.09653    -0.107488   0.113785    33  VAL   B HG12 
297  H HG13 . VAL   A 21  ? 0.583314 0.387604 0.526624 -0.110633   -0.113651   0.128065    33  VAL   B HG13 
298  H HG21 . VAL   A 21  ? 0.550059 0.417458 0.537456 -0.121246   -0.142938   0.135587    33  VAL   B HG21 
299  H HG22 . VAL   A 21  ? 0.56272  0.449288 0.531231 -0.115546   -0.163165   0.123461    33  VAL   B HG22 
300  H HG23 . VAL   A 21  ? 0.54695  0.429204 0.498082 -0.106481   -0.149558   0.135648    33  VAL   B HG23 
301  N N    . LEU   A 22  ? 0.713287 0.44381  0.458087 -0.0571029  -0.128726   0.0995665   34  LEU   B N    
302  C CA   . LEU   A 22  ? 0.757718 0.435072 0.437644 -0.0422168  -0.111318   0.0950173   34  LEU   B CA   
303  C C    . LEU   A 22  ? 0.770292 0.420125 0.463373 -0.0496603  -0.0740298  0.107038    34  LEU   B C    
304  O O    . LEU   A 22  ? 0.742502 0.402691 0.467135 -0.0580383  -0.0657788  0.120088    34  LEU   B O    
305  C CB   . LEU   A 22  ? 0.810389 0.470425 0.428931 -0.0183983  -0.118641   0.0996402   34  LEU   B CB   
306  C CG   . LEU   A 22  ? 0.808893 0.502636 0.416198 -0.00567143 -0.157063   0.0879605   34  LEU   B CG   
307  C CD1  . LEU   A 22  ? 0.843392 0.522021 0.399856 0.0216311   -0.161417   0.0984169   34  LEU   B CD1  
308  C CD2  . LEU   A 22  ? 0.812215 0.493685 0.38742  -0.00153873 -0.172793   0.0656669   34  LEU   B CD2  
309  H H    . LEU   A 22  ? 0.687496 0.428467 0.440481 -0.0562355  -0.12756    0.10836     34  LEU   B H    
310  H HA   . LEU   A 22  ? 0.787906 0.458459 0.455264 -0.0410249  -0.118771   0.081632    34  LEU   B HA   
311  H HB2  . LEU   A 22  ? 0.786213 0.449082 0.418924 -0.0204051  -0.111582   0.110628    34  LEU   B HB2  
312  H HB3  . LEU   A 22  ? 0.854076 0.475354 0.424407 -0.00705083 -0.103497   0.100646    34  LEU   B HB3  
313  H HG   . LEU   A 22  ? 0.755424 0.489561 0.414404 -0.0181876  -0.168338   0.0879677   34  LEU   B HG   
314  H HD11 . LEU   A 22  ? 0.817197 0.500005 0.395832 0.0172166   -0.152061   0.108517    34  LEU   B HD11 
315  H HD12 . LEU   A 22  ? 0.847393 0.553675 0.402516 0.0316723   -0.186648   0.0915014   34  LEU   B HD12 
316  H HD13 . LEU   A 22  ? 0.893925 0.530078 0.397293 0.0346335   -0.147991   0.102118    34  LEU   B HD13 
317  H HD21 . LEU   A 22  ? 0.799752 0.493428 0.416202 -0.0193273  -0.172867   0.0587022   34  LEU   B HD21 
318  H HD22 . LEU   A 22  ? 0.871644 0.511674 0.395355 0.0100347   -0.156385   0.0663557   34  LEU   B HD22 
319  H HD23 . LEU   A 22  ? 0.837873 0.54007  0.40272  0.00827931  -0.199225   0.0573941   34  LEU   B HD23 
320  N N    . LYS   A 23  ? 0.809056 0.422484 0.472291 -0.043686   -0.0515584  0.101248    35  LYS   B N    
321  C CA   . LYS   A 23  ? 0.817261 0.413436 0.505718 -0.0503452  -0.0128074  0.112652    35  LYS   B CA   
322  C C    . LYS   A 23  ? 0.919625 0.46261  0.538071 -0.0319026  0.0213545   0.117012    35  LYS   B C    
323  O O    . LYS   A 23  ? 0.969736 0.486226 0.52131  -0.0136277  0.0159755   0.102454    35  LYS   B O    
324  C CB   . LYS   A 23  ? 0.824367 0.431521 0.558781 -0.0591218  -0.00826212 0.103246    35  LYS   B CB   
325  C CG   . LYS   A 23  ? 0.818956 0.423262 0.598787 -0.0644792  0.0288043   0.114265    35  LYS   B CG   
326  C CD   . LYS   A 23  ? 0.768717 0.385429 0.60026  -0.0691765  0.0300652   0.10703     35  LYS   B CD   
327  C CE   . LYS   A 23  ? 0.780256 0.400474 0.660501 -0.0693956  0.0676782   0.118999    35  LYS   B CE   
328  N NZ   . LYS   A 23  ? 0.811237 0.417188 0.707962 -0.0597264  0.0846718   0.108881    35  LYS   B NZ   
329  H H    . LYS   A 23  ? 0.84628  0.447045 0.47329  -0.0342681  -0.0605525  0.0890135   35  LYS   B H    
330  H HA   . LYS   A 23  ? 0.79365  0.404774 0.516728 -0.0599512  -0.0097782  0.123658    35  LYS   B HA   
331  H HB2  . LYS   A 23  ? 0.775971 0.413844 0.55074  -0.0696946  -0.0287462  0.102582    35  LYS   B HB2  
332  H HB3  . LYS   A 23  ? 0.857745 0.444336 0.553602 -0.0494798  -0.0115147  0.0892052   35  LYS   B HB3  
333  H HG2  . LYS   A 23  ? 0.85842  0.43217  0.599064 -0.053587   0.0534599   0.115615    35  LYS   B HG2  
334  H HG3  . LYS   A 23  ? 0.778989 0.402887 0.594896 -0.074379   0.0297892   0.126194    35  LYS   B HG3  
335  H HD2  . LYS   A 23  ? 0.735661 0.381345 0.605836 -0.079632   0.00847684  0.109625    35  LYS   B HD2  
336  H HD3  . LYS   A 23  ? 0.815361 0.408735 0.611096 -0.0604094  0.0275094   0.091849    35  LYS   B HD3  
337  H HE2  . LYS   A 23  ? 0.810044 0.411559 0.662718 -0.063838   0.0904767   0.12449     35  LYS   B HE2  
338  H HE3  . LYS   A 23  ? 0.734683 0.386968 0.667728 -0.0808828  0.0601805   0.129711    35  LYS   B HE3  
339  H HZ1  . LYS   A 23  ? 0.855788 0.43024  0.699788 -0.0484606  0.0897295   0.0958008   35  LYS   B HZ1  
340  H HZ2  . LYS   A 23  ? 0.783293 0.404272 0.711348 -0.065655   0.0661132   0.106775    35  LYS   B HZ2  
341  H HZ3  . LYS   A 23  ? 0.810528 0.423064 0.738971 -0.0579184  0.109154    0.117644    35  LYS   B HZ3  
342  N N    . ILE   A 24  ? 0.923749 0.452648 0.561323 -0.0377856  0.0568607   0.136545    36  ILE   B N    
343  C CA   . ILE   A 24  ? 0.977505 0.462859 0.575355 -0.0258214  0.104704    0.147362    36  ILE   B CA   
344  C C    . ILE   A 24  ? 0.956498 0.465795 0.642362 -0.0440107  0.135381    0.155859    36  ILE   B C    
345  O O    . ILE   A 24  ? 0.87115  0.413951 0.631617 -0.0654652  0.12757     0.163672    36  ILE   B O    
346  C CB   . ILE   A 24  ? 1.03898  0.482268 0.582335 -0.015881   0.124659    0.168078    36  ILE   B CB   
347  C CG1  . ILE   A 24  ? 1.09343  0.517809 0.551803 0.00782283  0.0910482   0.161488    36  ILE   B CG1  
348  C CG2  . ILE   A 24  ? 1.13052  0.529189 0.635549 -0.00407079 0.182948    0.185309    36  ILE   B CG2  
349  C CD1  . ILE   A 24  ? 1.1469   0.529287 0.558523 0.0191723   0.104623    0.1843      36  ILE   B CD1  
350  H H    . ILE   A 24  ? 0.88273  0.430991 0.562054 -0.0504389  0.0515756   0.143494    36  ILE   B H    
351  H HA   . ILE   A 24  ? 1.02354  0.491463 0.57481  -0.0110785  0.105235    0.135908    36  ILE   B HA   
352  H HB   . ILE   A 24  ? 1.00807  0.465143 0.5988   -0.0317542  0.122758    0.176229    36  ILE   B HB   
353  H HG12 . ILE   A 24  ? 1.13611  0.543089 0.540729 0.0246107   0.0922376   0.152567    36  ILE   B HG12 
354  H HG13 . ILE   A 24  ? 1.04084  0.498423 0.527995 0.00085607  0.0572907   0.150247    36  ILE   B HG13 
355  H HG21 . ILE   A 24  ? 1.16349  0.533392 0.640747 -0.00025409 0.197764    0.202129    36  ILE   B HG21 
356  H HG22 . ILE   A 24  ? 1.17193  0.552301 0.618686 0.014948    0.184929    0.175896    36  ILE   B HG22 
357  H HG23 . ILE   A 24  ? 1.10165  0.518765 0.668447 -0.0183114  0.204106    0.189265    36  ILE   B HG23 
358  H HD11 . ILE   A 24  ? 1.10729  0.502123 0.570707 0.00206399  0.103596    0.190323    36  ILE   B HD11 
359  H HD12 . ILE   A 24  ? 1.16641  0.543531 0.529575 0.0366636   0.0791954   0.179439    36  ILE   B HD12 
360  H HD13 . ILE   A 24  ? 1.20319  0.549678 0.580408 0.0274662   0.14006     0.198165    36  ILE   B HD13 
361  N N    . VAL   A 25  ? 0.985895 0.479873 0.661792 -0.0325802  0.168243    0.152187    37  VAL   B N    
362  C CA   . VAL   A 25  ? 0.963653 0.475633 0.714448 -0.0418035  0.209248    0.164353    37  VAL   B CA   
363  C C    . VAL   A 25  ? 1.0228   0.50784  0.762704 -0.0437563  0.254774    0.189748    37  VAL   B C    
364  O O    . VAL   A 25  ? 1.07891  0.513699 0.727655 -0.0216656  0.281972    0.196328    37  VAL   B O    
365  C CB   . VAL   A 25  ? 1.01054  0.505069 0.73482  -0.0207978  0.231909    0.149649    37  VAL   B CB   
366  C CG1  . VAL   A 25  ? 1.01039  0.521542 0.804096 -0.0213184  0.284033    0.1633      37  VAL   B CG1  
367  C CG2  . VAL   A 25  ? 0.980575 0.491158 0.717392 -0.0216193  0.18762     0.12462     37  VAL   B CG2  
368  H H    . VAL   A 25  ? 1.02512  0.497023 0.644255 -0.0166958  0.164745    0.140433    37  VAL   B H    
369  H HA   . VAL   A 25  ? 0.909266 0.459125 0.730515 -0.0581726  0.19279     0.164954    37  VAL   B HA   
370  H HB   . VAL   A 25  ? 1.07384  0.529778 0.717855 -0.00293618 0.243392    0.146941    37  VAL   B HB   
371  H HG11 . VAL   A 25  ? 0.954864 0.50595  0.828757 -0.0388563  0.273433    0.169166    37  VAL   B HG11 
372  H HG12 . VAL   A 25  ? 1.05468  0.546879 0.827144 -0.0178724  0.317828    0.1784      37  VAL   B HG12 
373  H HG13 . VAL   A 25  ? 1.03821  0.539437 0.818562 -0.00649811 0.294514    0.151201    37  VAL   B HG13 
374  H HG21 . VAL   A 25  ? 1.00941  0.506153 0.737722 -0.00940204 0.203701    0.114413    37  VAL   B HG21 
375  H HG22 . VAL   A 25  ? 0.989267 0.486738 0.675196 -0.0177667  0.160467    0.114594    37  VAL   B HG22 
376  H HG23 . VAL   A 25  ? 0.918155 0.465092 0.7232   -0.0375881  0.171206    0.129327    37  VAL   B HG23 
377  N N    . LYS   A 26  ? 0.982006 0.498321 0.813376 -0.0700455  0.262627    0.204147    38  LYS   B N    
378  C CA   . LYS   A 26  ? 1.03028  0.520333 0.868639 -0.0788789  0.306933    0.229189    38  LYS   B CA   
379  C C    . LYS   A 26  ? 1.05542  0.567351 0.967786 -0.0841253  0.362166    0.243081    38  LYS   B C    
380  O O    . LYS   A 26  ? 1.11826  0.595175 1.00438  -0.078326   0.416854    0.265182    38  LYS   B O    
381  C CB   . LYS   A 26  ? 0.988999 0.492377 0.875569 -0.105686   0.275881    0.231601    38  LYS   B CB   
382  C CG   . LYS   A 26  ? 1.00624  0.477244 0.807825 -0.0935017  0.236405    0.224282    38  LYS   B CG   
383  C CD   . LYS   A 26  ? 1.09976  0.503    0.788494 -0.0660748  0.265162    0.238866    38  LYS   B CD   
384  C CE   . LYS   A 26  ? 1.13961  0.50293  0.776155 -0.0611659  0.246796    0.246397    38  LYS   B CE   
385  N NZ   . LYS   A 26  ? 1.22433  0.519083 0.769667 -0.0378917  0.288451    0.271335    38  LYS   B NZ   
386  H H    . LYS   A 26  ? 0.925795 0.479733 0.817172 -0.0832982  0.239269    0.198181    38  LYS   B H    
387  H HA   . LYS   A 26  ? 1.09251  0.537896 0.848731 -0.0612509  0.320914    0.235182    38  LYS   B HA   
388  H HB2  . LYS   A 26  ? 0.931943 0.479738 0.884746 -0.119252   0.252194    0.222234    38  LYS   B HB2  
389  H HB3  . LYS   A 26  ? 1.01867  0.508724 0.93106  -0.117537   0.305373    0.247323    38  LYS   B HB3  
390  H HG2  . LYS   A 26  ? 0.969596 0.461277 0.760494 -0.0865565  0.205173    0.208684    38  LYS   B HG2  
391  H HG3  . LYS   A 26  ? 0.985241 0.460233 0.817627 -0.109171   0.222085    0.225552    38  LYS   B HG3  
392  H HD2  . LYS   A 26  ? 1.14387  0.530632 0.841442 -0.0677272  0.308537    0.255131    38  LYS   B HD2  
393  H HD3  . LYS   A 26  ? 1.11501  0.51485  0.752535 -0.0467878  0.255456    0.227965    38  LYS   B HD3  
394  H HE2  . LYS   A 26  ? 1.11035  0.484208 0.71687  -0.0506497  0.209756    0.232098    38  LYS   B HE2  
395  H HE3  . LYS   A 26  ? 1.10872  0.480024 0.801111 -0.0823722  0.243751    0.249308    38  LYS   B HE3  
396  H HZ1  . LYS   A 26  ? 1.25867  0.545872 0.74874  -0.0172074  0.29086     0.266881    38  LYS   B HZ1  
397  H HZ2  . LYS   A 26  ? 1.25475  0.538994 0.831599 -0.0492941  0.325822    0.287206    38  LYS   B HZ2  
398  H HZ3  . LYS   A 26  ? 1.2513   0.520015 0.761927 -0.0313004  0.275311    0.276162    38  LYS   B HZ3  
399  N N    . ARG   A 27  ? 1.01353  0.58395  1.01864  -0.0922388  0.351088    0.233084    39  ARG   B N    
400  C CA   . ARG   A 27  ? 1.0254   0.623747 1.10308  -0.0899364  0.402979    0.244354    39  ARG   B CA   
401  C C    . ARG   A 27  ? 1.00346  0.624201 1.09008  -0.069459   0.38954     0.224973    39  ARG   B C    
402  O O    . ARG   A 27  ? 0.992928 0.645219 1.11305  -0.0767679  0.338209    0.210694    39  ARG   B O    
403  C CB   . ARG   A 27  ? 0.975363 0.629899 1.18965  -0.124437   0.408359    0.257294    39  ARG   B CB   
404  C CG   . ARG   A 27  ? 1.00017  0.692321 1.30476  -0.123274   0.467593    0.273079    39  ARG   B CG   
405  C CD   . ARG   A 27  ? 0.939381 0.704737 1.39849  -0.159034   0.457819    0.279297    39  ARG   B CD   
406  N NE   . ARG   A 27  ? 0.879377 0.705887 1.40309  -0.159094   0.401851    0.261022    39  ARG   B NE   
407  C CZ   . ARG   A 27  ? 0.813736 0.699502 1.43882  -0.187048   0.35989     0.255941    39  ARG   B CZ   
408  N NH1  . ARG   A 27  ? 0.842345 0.735318 1.52722  -0.221233   0.367051    0.263627    39  ARG   B NH1  
409  N NH2  . ARG   A 27  ? 0.737873 0.671487 1.40124  -0.180699   0.310002    0.243013    39  ARG   B NH2  
410  H H    . ARG   A 27  ? 0.95663  0.551114 0.981423 -0.0977152  0.311481    0.220562    39  ARG   B H    
411  H HA   . ARG   A 27  ? 1.09088  0.653309 1.11834  -0.0767486  0.445284    0.256063    39  ARG   B HA   
412  H HB2  . ARG   A 27  ? 0.99641  0.628222 1.19969  -0.138832   0.411897    0.266562    39  ARG   B HB2  
413  H HB3  . ARG   A 27  ? 0.918979 0.609993 1.17799  -0.134121   0.366532    0.245622    39  ARG   B HB3  
414  H HG2  . ARG   A 27  ? 0.992811 0.696701 1.29449  -0.103313   0.469895    0.264239    39  ARG   B HG2  
415  H HG3  . ARG   A 27  ? 1.05956  0.716875 1.32547  -0.116846   0.513092    0.288427    39  ARG   B HG3  
416  H HD2  . ARG   A 27  ? 0.97086  0.75601  1.48561  -0.15986    0.503288    0.293415    39  ARG   B HD2  
417  H HD3  . ARG   A 27  ? 0.945616 0.696913 1.40603  -0.180525   0.443975    0.281924    39  ARG   B HD3  
418  H HE   . ARG   A 27  ? 0.86724  0.689087 1.35842  -0.138711   0.395255    0.253159    39  ARG   B HE   
419  H HH11 . ARG   A 27  ? 0.875145 0.758099 1.57838  -0.226775   0.410533    0.277793    39  ARG   B HH11 
420  H HH12 . ARG   A 27  ? 0.811009 0.717813 1.51836  -0.238631   0.328889    0.254282    39  ARG   B HH12 
421  H HH21 . ARG   A 27  ? 0.736692 0.65432  1.34889  -0.161919   0.297794    0.236482    39  ARG   B HH21 
422  H HH22 . ARG   A 27  ? 0.715202 0.695855 1.45496  -0.195121   0.288732    0.241435    39  ARG   B HH22 
423  N N    . VAL   A 28  ? 1.06703  0.664993 1.11691  -0.0415962  0.437807    0.224937    40  VAL   B N    
424  C CA   . VAL   A 28  ? 1.08904  0.68464  1.12078  -0.0173813  0.426359    0.202318    40  VAL   B CA   
425  C C    . VAL   A 28  ? 1.05112  0.713165 1.2158   -0.0223856  0.432231    0.206724    40  VAL   B C    
426  O O    . VAL   A 28  ? 1.04039  0.739904 1.28957  -0.0308447  0.473816    0.226837    40  VAL   B O    
427  C CB   . VAL   A 28  ? 1.20243  0.738724 1.12654  0.0192971   0.473239    0.194929    40  VAL   B CB   
428  C CG1  . VAL   A 28  ? 1.26702  0.814741 1.23375  0.0295984   0.551174    0.21815     40  VAL   B CG1  
429  C CG2  . VAL   A 28  ? 1.21231  0.729376 1.10028  0.0427662   0.451308    0.163369    40  VAL   B CG2  
430  H H    . VAL   A 28  ? 1.12247  0.702662 1.1564   -0.0368796  0.480567    0.239338    40  VAL   B H    
431  H HA   . VAL   A 28  ? 1.06095  0.649769 1.06349  -0.0205611  0.3819      0.188315    40  VAL   B HA   
432  H HB   . VAL   A 28  ? 1.23755  0.735981 1.08021  0.0223795   0.467382    0.195408    40  VAL   B HB   
433  H HG11 . VAL   A 28  ? 1.23654  0.821391 1.27978  0.03194     0.558812    0.216376    40  VAL   B HG11 
434  H HG12 . VAL   A 28  ? 1.25373  0.814627 1.25587  0.0101985   0.564001    0.238441    40  VAL   B HG12 
435  H HG13 . VAL   A 28  ? 1.3397   0.844322 1.22227  0.0543223   0.581538    0.214785    40  VAL   B HG13 
436  H HG21 . VAL   A 28  ? 1.28754  0.763123 1.09787  0.0665369   0.477357    0.154942    40  VAL   B HG21 
437  H HG22 . VAL   A 28  ? 1.18143  0.693524 1.04786  0.0340282   0.404469    0.150721    40  VAL   B HG22 
438  H HG23 . VAL   A 28  ? 1.18483  0.734818 1.14919  0.0434603   0.458347    0.164177    40  VAL   B HG23 
439  N N    . GLY   A 29  ? 1.02282  0.698869 1.20679  -0.0163749  0.390689    0.189477    41  GLY   B N    
440  C CA   . GLY   A 29  ? 1.00751  0.741448 1.30614  -0.0134281  0.388474    0.193541    41  GLY   B CA   
441  C C    . GLY   A 29  ? 1.04912  0.767632 1.34758  0.0219461   0.44089     0.18836     41  GLY   B C    
442  O O    . GLY   A 29  ? 1.12928  0.806585 1.35939  0.0398509   0.491877    0.18838     41  GLY   B O    
443  H H    . GLY   A 29  ? 1.02705  0.674811 1.15063  -0.0132713  0.362389    0.175792    41  GLY   B H    
444  H HA2  . GLY   A 29  ? 0.966008 0.743908 1.33976  -0.0301246  0.392775    0.207997    41  GLY   B HA2  
445  H HA3  . GLY   A 29  ? 0.95847  0.699036 1.26256  -0.0167702  0.347323    0.185454    41  GLY   B HA3  
446  N N    . ASN   A 30  ? 1.00191  0.751976 1.37425  0.0351486   0.429336    0.185279    42  ASN   B N    
447  C CA   . ASN   A 30  ? 1.06689  0.80192  1.44742  0.0728054   0.473436    0.177481    42  ASN   B CA   
448  C C    . ASN   A 30  ? 1.04781  0.775794 1.44868  0.0851379   0.432685    0.164526    42  ASN   B C    
449  O O    . ASN   A 30  ? 0.955995 0.709292 1.38773  0.0635842   0.377386    0.169569    42  ASN   B O    
450  C CB   . ASN   A 30  ? 1.1185   0.922783 1.61981  0.0783669   0.522349    0.20063     42  ASN   B CB   
451  C CG   . ASN   A 30  ? 1.05725  0.945294 1.68232  0.0483116   0.480387    0.21858     42  ASN   B CG   
452  O OD1  . ASN   A 30  ? 1.08491  1.00288  1.7662   0.0543798   0.440436    0.217897    42  ASN   B OD1  
453  N ND2  . ASN   A 30  ? 1.04717  0.969788 1.7125   0.0166568   0.4869      0.234263    42  ASN   B ND2  
454  H H    . ASN   A 30  ? 0.956071 0.736864 1.374    0.0219582   0.391887    0.188625    42  ASN   B H    
455  H HA   . ASN   A 30  ? 1.13858  0.822151 1.43369  0.0878086   0.498526    0.165783    42  ASN   B HA   
456  H HB2  . ASN   A 30  ? 1.13902  0.942289 1.6617   0.105345    0.544352    0.195899    42  ASN   B HB2  
457  H HB3  . ASN   A 30  ? 1.14666  0.942487 1.62493  0.0760662   0.56054     0.208453    42  ASN   B HB3  
458  H HD21 . ASN   A 30  ? 1.00053  0.976335 1.74699  0.00083668  0.467303    0.242962    42  ASN   B HD21 
459  H HD22 . ASN   A 30  ? 1.07542  0.966081 1.68606  0.0114844   0.509983    0.235769    42  ASN   B HD22 
460  N N    . GLY   A 31  ? 1.14142  0.832854 1.52613  0.121788    0.463876    0.149527    43  GLY   B N    
461  C CA   . GLY   A 31  ? 1.12785  0.78952  1.51506  0.135587    0.430897    0.135185    43  GLY   B CA   
462  C C    . GLY   A 31  ? 1.17711  0.761656 1.44473  0.126519    0.396635    0.10649     43  GLY   B C    
463  O O    . GLY   A 31  ? 1.19131  0.768183 1.39701  0.102873    0.378471    0.104853    43  GLY   B O    
464  H H    . GLY   A 31  ? 1.18033  0.861957 1.55118  0.139404    0.508865    0.148507    43  GLY   B H    
465  H HA2  . GLY   A 31  ? 1.18086  0.83011  1.58379  0.164173    0.462251    0.129608    43  GLY   B HA2  
466  H HA3  . GLY   A 31  ? 1.0767   0.781315 1.5309   0.123294    0.399941    0.150157    43  GLY   B HA3  
467  N N    . GLU   A 32  ? 1.26089  0.788073 1.50162  0.146872    0.389441    0.0831941   44  GLU   B N    
468  C CA   . GLU   A 32  ? 1.30827  0.766298 1.4571   0.136447    0.351623    0.0528656   44  GLU   B CA   
469  C C    . GLU   A 32  ? 1.23977  0.72341  1.43332  0.105203    0.292294    0.0673482   44  GLU   B C    
470  O O    . GLU   A 32  ? 1.26378  0.713128 1.39892  0.0855295   0.255027    0.0500618   44  GLU   B O    
471  C CB   . GLU   A 32  ? 1.38215  0.764294 1.49189  0.171099    0.373839    0.0197808   44  GLU   B CB   
472  H H    . GLU   A 32  ? 1.27244  0.804436 1.55956  0.168006    0.408655    0.0860388   44  GLU   B H    
473  H HA   . GLU   A 32  ? 1.31875  0.762561 1.40037  0.128914    0.352858    0.0443255   44  GLU   B HA   
476  N N    . GLU   A 33  ? 1.15088  0.698976 1.44824  0.101985    0.283418    0.0998789   45  GLU   B N    
477  C CA   . GLU   A 33  ? 1.06464  0.630444 1.40436  0.0835315   0.235521    0.116497    45  GLU   B CA   
478  C C    . GLU   A 33  ? 0.985802 0.596736 1.31483  0.0487555   0.200627    0.129918    45  GLU   B C    
479  O O    . GLU   A 33  ? 0.916106 0.576362 1.26576  0.0407317   0.211198    0.142735    45  GLU   B O    
480  C CB   . GLU   A 33  ? 1.03703  0.65023  1.4825   0.102765    0.239524    0.145508    45  GLU   B CB   
481  H H    . GLU   A 33  ? 1.14008  0.724059 1.48307  0.112627    0.308543    0.112897    45  GLU   B H    
482  H HA   . GLU   A 33  ? 1.10409  0.618908 1.40855  0.083102    0.223137    0.0997788   45  GLU   B HA   
485  N N    . THR   A 34  ? 0.967014 0.557704 1.26443  0.0278133   0.160899    0.125581    46  THR   B N    
486  C CA   . THR   A 34  ? 0.879249 0.513581 1.17247  -0.00050562 0.126722    0.139794    46  THR   B CA   
487  C C    . THR   A 34  ? 0.856897 0.520653 1.20745  -0.00607758 0.0965454   0.166096    46  THR   B C    
488  O O    . THR   A 34  ? 0.820022 0.452339 1.19343  0.00617081  0.0970212   0.169233    46  THR   B O    
489  C CB   . THR   A 34  ? 0.892717 0.490103 1.10305  -0.0180166  0.10721     0.116516    46  THR   B CB   
490  O OG1  . THR   A 34  ? 0.927023 0.476089 1.13086  -0.0182457  0.0933595   0.103175    46  THR   B OG1  
491  C CG2  . THR   A 34  ? 0.917155 0.484446 1.05616  -0.00888791 0.134311    0.0941608   46  THR   B CG2  
492  H H    . THR   A 34  ? 0.998088 0.546293 1.27791  0.0314701   0.156136    0.112881    46  THR   B H    
493  H HA   . THR   A 34  ? 0.862591 0.532321 1.17137  -0.00262807 0.136235    0.148426    46  THR   B HA   
494  H HB   . THR   A 34  ? 0.845337 0.473283 1.05772  -0.0342301  0.085376    0.127347    46  THR   B HB   
496  H HG21 . THR   A 34  ? 0.934471 0.48272  1.02235  -0.0182997  0.116984    0.0803337   46  THR   B HG21 
497  H HG22 . THR   A 34  ? 0.973022 0.508308 1.1031   0.00899058  0.157086    0.0816261   46  THR   B HG22 
498  H HG23 . THR   A 34  ? 0.900702 0.499028 1.05328  -0.0102681  0.146697    0.106635    46  THR   B HG23 
499  N N    . PRO   A 35  ? 0.809415 0.528816 1.17946  -0.0227886  0.0695065   0.186621    47  PRO   B N    
500  C CA   . PRO   A 35  ? 0.769263 0.513941 1.18106  -0.023144   0.0431107   0.213982    47  PRO   B CA   
501  C C    . PRO   A 35  ? 0.806737 0.502496 1.19229  -0.0322586  0.0293667   0.211467    47  PRO   B C    
502  O O    . PRO   A 35  ? 0.786667 0.457238 1.11972  -0.0500866  0.0216512   0.190707    47  PRO   B O    
503  C CB   . PRO   A 35  ? 0.704431 0.507755 1.11608  -0.0400248  0.0178383   0.226243    47  PRO   B CB   
504  C CG   . PRO   A 35  ? 0.761371 0.575494 1.1572   -0.0458014  0.0361568   0.209771    47  PRO   B CG   
505  C CD   . PRO   A 35  ? 0.804499 0.558344 1.15312  -0.038764   0.0650988   0.184643    47  PRO   B CD   
506  H HA   . PRO   A 35  ? 0.780444 0.537742 1.23809  -0.00605531 0.0514691   0.226103    47  PRO   B HA   
507  H HB2  . PRO   A 35  ? 0.712191 0.508284 1.09237  -0.0529744  0.00177995  0.225473    47  PRO   B HB2  
508  H HB3  . PRO   A 35  ? 0.705121 0.544137 1.15765  -0.0329514  0.00728168  0.245068    47  PRO   B HB3  
509  H HG2  . PRO   A 35  ? 0.722359 0.548894 1.09196  -0.0601275  0.0217702   0.207658    47  PRO   B HG2  
510  H HG3  . PRO   A 35  ? 0.735886 0.581795 1.17753  -0.0385451  0.0440373   0.217699    47  PRO   B HG3  
511  H HD2  . PRO   A 35  ? 0.801768 0.534731 1.10017  -0.0497667  0.0566172   0.17254     47  PRO   B HD2  
512  H HD3  . PRO   A 35  ? 0.807992 0.566218 1.16478  -0.0319553  0.0886544   0.180434    47  PRO   B HD3  
513  N N    . MET   A 36  ? 0.867761 0.5498   1.2946   -0.0191743  0.0274172   0.233117    48  MET   B N    
514  C CA   . MET   A 36  ? 0.921921 0.563983 1.34283  -0.0307704  0.0150242   0.241291    48  MET   B CA   
515  C C    . MET   A 36  ? 0.874837 0.56819  1.30558  -0.0409092  -0.0102072  0.276076    48  MET   B C    
516  O O    . MET   A 36  ? 0.822049 0.572702 1.27527  -0.0296854  -0.0194821  0.296543    48  MET   B O    
517  C CB   . MET   A 36  ? 1.08978  0.681518 1.54952  -0.00837625 0.030069    0.252089    48  MET   B CB   
518  C CG   . MET   A 36  ? 1.22885  0.755065 1.67562  0.00724578  0.0576098   0.21627     48  MET   B CG   
519  S SD   . MET   A 36  ? 1.27475  0.728509 1.65412  -0.0172549  0.0546925   0.165983    48  MET   B SD   
520  C CE   . MET   A 36  ? 1.26566  0.754011 1.58923  -0.017455   0.064088    0.13857     48  MET   B CE   
521  H H    . MET   A 36  ? 0.866692 0.565356 1.33092  -0.00166903 0.0352534   0.245055    48  MET   B H    
522  H HA   . MET   A 36  ? 0.943365 0.55763  1.32883  -0.0457611  0.0132663   0.218457    48  MET   B HA   
523  H HB2  . MET   A 36  ? 1.06624  0.69038  1.56126  0.00911386  0.0301651   0.275096    48  MET   B HB2  
524  H HB3  . MET   A 36  ? 1.09373  0.662351 1.55499  -0.0190235  0.0214195   0.262968    48  MET   B HB3  
525  H HG2  . MET   A 36  ? 1.19606  0.747123 1.64402  0.0189156   0.070527    0.209       48  MET   B HG2  
526  H HG3  . MET   A 36  ? 1.2454   0.743363 1.72209  0.0241099   0.0660483   0.227456    48  MET   B HG3  
527  H HE1  . MET   A 36  ? 1.29913  0.747327 1.58     -0.0212212  0.0659901   0.108647    48  MET   B HE1  
528  H HE2  . MET   A 36  ? 1.21193  0.742641 1.53009  -0.0323261  0.0484547   0.149748    48  MET   B HE2  
529  H HE3  . MET   A 36  ? 1.25998  0.763375 1.60153  0.00217006  0.0837101   0.143212    48  MET   B HE3  
530  N N    . ILE   A 37  ? 0.821006 0.495208 1.23695  -0.0613722  -0.0212596  0.282719    49  ILE   B N    
531  C CA   . ILE   A 37  ? 0.735731 0.452529 1.15544  -0.0671657  -0.0384131  0.318691    49  ILE   B CA   
532  C C    . ILE   A 37  ? 0.715238 0.445458 1.1742   -0.0396219  -0.0384532  0.358698    49  ILE   B C    
533  O O    . ILE   A 37  ? 0.724589 0.406475 1.21274  -0.0251027  -0.0246397  0.367926    49  ILE   B O    
534  C CB   . ILE   A 37  ? 0.7719   0.463069 1.18435  -0.0924015  -0.0419076  0.323954    49  ILE   B CB   
535  C CG1  . ILE   A 37  ? 0.766284 0.460591 1.14182  -0.116955   -0.0497835  0.287178    49  ILE   B CG1  
536  C CG2  . ILE   A 37  ? 0.751097 0.480881 1.16913  -0.091142   -0.050126   0.369772    49  ILE   B CG2  
537  C CD1  . ILE   A 37  ? 0.830677 0.497084 1.21627  -0.14374    -0.0529791  0.283996    49  ILE   B CD1  
538  H H    . ILE   A 37  ? 0.845913 0.480618 1.24969  -0.0715428  -0.0173363  0.264179    49  ILE   B H    
539  H HA   . ILE   A 37  ? 0.704535 0.461477 1.1061   -0.0709344  -0.0478877  0.314364    49  ILE   B HA   
540  H HB   . ILE   A 37  ? 0.809953 0.453831 1.24042  -0.0920175  -0.0324801  0.322324    49  ILE   B HB   
541  H HG12 . ILE   A 37  ? 0.734563 0.471746 1.09251  -0.118034   -0.0586614  0.291262    49  ILE   B HG12 
542  H HG13 . ILE   A 37  ? 0.778961 0.452494 1.14163  -0.11309    -0.0443291  0.260364    49  ILE   B HG13 
543  H HG21 . ILE   A 37  ? 0.762334 0.485042 1.17823  -0.109269   -0.050002   0.372399    49  ILE   B HG21 
544  H HG22 . ILE   A 37  ? 0.721907 0.496472 1.12272  -0.0860701  -0.0601206  0.37192     49  ILE   B HG22 
545  H HG23 . ILE   A 37  ? 0.782522 0.498732 1.22264  -0.0759894  -0.0449584  0.394482    49  ILE   B HG23 
546  H HD11 . ILE   A 37  ? 0.861068 0.481175 1.26719  -0.143706   -0.0449946  0.281946    49  ILE   B HD11 
547  H HD12 . ILE   A 37  ? 0.810719 0.47888  1.17444  -0.155432   -0.0601864  0.257065    49  ILE   B HD12 
548  H HD13 . ILE   A 37  ? 0.808631 0.50166  1.20338  -0.148798   -0.0556502  0.310759    49  ILE   B HD13 
549  N N    . GLY   A 38  ? 0.66057  0.45424  1.11674  -0.0304538  -0.0564163  0.38157     50  GLY   B N    
550  C CA   . GLY   A 38  ? 0.702424 0.517966 1.19     -0.00055682 -0.0635125  0.419576    50  GLY   B CA   
551  C C    . GLY   A 38  ? 0.693124 0.560416 1.20996  0.0186966   -0.0722986  0.410795    50  GLY   B C    
552  O O    . GLY   A 38  ? 0.732686 0.642719 1.27167  0.0426973   -0.0901224  0.438856    50  GLY   B O    
553  H H    . GLY   A 38  ? 0.640689 0.463428 1.07311  -0.0414264  -0.0659727  0.372448    50  GLY   B H    
554  H HA2  . GLY   A 38  ? 0.700659 0.538958 1.17153  -0.00074476 -0.0751709  0.442581    50  GLY   B HA2  
555  H HA3  . GLY   A 38  ? 0.739637 0.513423 1.24784  0.00883044  -0.0511822  0.430381    50  GLY   B HA3  
556  N N    . ASP   A 39  ? 0.646414 0.508094 1.16796  0.0101757   -0.0583499  0.373716    51  ASP   B N    
557  C CA   . ASP   A 39  ? 0.671789 0.579684 1.23595  0.0247857   -0.0584138  0.36491     51  ASP   B CA   
558  C C    . ASP   A 39  ? 0.614172 0.593545 1.17333  0.0178769   -0.0890367  0.367513    51  ASP   B C    
559  O O    . ASP   A 39  ? 0.599005 0.583562 1.10831  -0.00265234 -0.101654   0.360822    51  ASP   B O    
560  C CB   . ASP   A 39  ? 0.688316 0.570735 1.24788  0.0148997   -0.0307737  0.327363    51  ASP   B CB   
561  C CG   . ASP   A 39  ? 0.753689 0.569302 1.32282  0.029382    -8.6e-06    0.317016    51  ASP   B CG   
562  O OD1  . ASP   A 39  ? 0.772726 0.560572 1.36463  0.0481573   0.00056641  0.340473    51  ASP   B OD1  
563  O OD2  . ASP   A 39  ? 0.777955 0.565862 1.32726  0.0239962   0.0240307   0.285568    51  ASP   B OD2  
564  H H    . ASP   A 39  ? 0.663476 0.492812 1.16227  -0.00505217 -0.0478183  0.354065    51  ASP   B H    
565  H HA   . ASP   A 39  ? 0.686624 0.596038 1.28791  0.047446    -0.0559721  0.381913    51  ASP   B HA   
566  H HB2  . ASP   A 39  ? 0.671307 0.542818 1.18967  -0.00529244 -0.0326809  0.312192    51  ASP   B HB2  
567  H HB3  . ASP   A 39  ? 0.669406 0.590065 1.25834  0.0195663   -0.030261   0.322918    51  ASP   B HB3  
568  N N    . LYS   A 40  ? 0.63404  0.669402 1.24935  0.0363921   -0.101981   0.375039    52  LYS   B N    
569  C CA   . LYS   A 40  ? 0.596805 0.697483 1.21823  0.0266109   -0.131205   0.366168    52  LYS   B CA   
570  C C    . LYS   A 40  ? 0.576153 0.677222 1.209    0.00458856  -0.110549   0.332103    52  LYS   B C    
571  O O    . LYS   A 40  ? 0.598212 0.702293 1.28449  0.0135257   -0.085567   0.325454    52  LYS   B O    
572  C CB   . LYS   A 40  ? 0.636782 0.806654 1.32276  0.051612    -0.159662   0.383463    52  LYS   B CB   
573  C CG   . LYS   A 40  ? 0.692484 0.892388 1.34392  0.0656307   -0.200013   0.409517    52  LYS   B CG   
574  C CD   . LYS   A 40  ? 0.751733 1.03039  1.46218  0.088197    -0.238683   0.418607    52  LYS   B CD   
575  C CE   . LYS   A 40  ? 0.748653 1.07811  1.47269  0.0623252   -0.262975   0.384919    52  LYS   B CE   
576  N NZ   . LYS   A 40  ? 0.789608 1.19447  1.60844  0.0741057   -0.28685    0.380987    52  LYS   B NZ   
577  H H    . LYS   A 40  ? 0.645927 0.678552 1.29955  0.0556722   -0.0932794  0.384676    52  LYS   B H    
578  H HA   . LYS   A 40  ? 0.600781 0.70101  1.17592  0.0168737   -0.146166   0.368673    52  LYS   B HA   
579  H HB2  . LYS   A 40  ? 0.65528  0.816989 1.38002  0.0713433   -0.145934   0.394823    52  LYS   B HB2  
580  H HB3  . LYS   A 40  ? 0.617669 0.82284  1.33293  0.0410739   -0.165191   0.366038    52  LYS   B HB3  
581  H HG2  . LYS   A 40  ? 0.681499 0.880602 1.28644  0.0478564   -0.2094     0.398206    52  LYS   B HG2  
582  H HG3  . LYS   A 40  ? 0.720387 0.887811 1.35374  0.0789805   -0.191963   0.43241     52  LYS   B HG3  
583  H HD2  . LYS   A 40  ? 0.774042 1.06206  1.45758  0.105955    -0.260431   0.441693    52  LYS   B HD2  
584  H HD3  . LYS   A 40  ? 0.751622 1.03837  1.51986  0.103283    -0.226513   0.423744    52  LYS   B HD3  
585  H HE2  . LYS   A 40  ? 0.725358 1.02916  1.44384  0.0398995   -0.238973   0.364373    52  LYS   B HE2  
586  H HE3  . LYS   A 40  ? 0.759577 1.0967   1.43374  0.0590855   -0.287128   0.384891    52  LYS   B HE3  
587  H HZ1  . LYS   A 40  ? 0.77277  1.17346  1.63947  0.0818793   -0.262968   0.384366    52  LYS   B HZ1  
588  H HZ2  . LYS   A 40  ? 0.800848 1.2347   1.61963  0.0948938   -0.315744   0.397649    52  LYS   B HZ2  
589  H HZ3  . LYS   A 40  ? 0.759922 1.188    1.59166  0.0535735   -0.296988   0.358457    52  LYS   B HZ3  
590  N N    . VAL   A 41  ? 0.540491 0.640879 1.12414  -0.0209483  -0.119952   0.313627    53  VAL   B N    
591  C CA   . VAL   A 41  ? 0.559766 0.647377 1.13884  -0.0420173  -0.0978173  0.285844    53  VAL   B CA   
592  C C    . VAL   A 41  ? 0.519431 0.659342 1.12341  -0.0570279  -0.122074   0.27399     53  VAL   B C    
593  O O    . VAL   A 41  ? 0.580701 0.742527 1.15441  -0.0605843  -0.156805   0.275483    53  VAL   B O    
594  C CB   . VAL   A 41  ? 0.54167  0.573691 1.04081  -0.0576972  -0.0871267  0.273542    53  VAL   B CB   
595  C CG1  . VAL   A 41  ? 0.561474 0.572242 1.04006  -0.0753093  -0.0646849  0.248687    53  VAL   B CG1  
596  C CG2  . VAL   A 41  ? 0.575425 0.555652 1.05881  -0.0470529  -0.0681668  0.280998    53  VAL   B CG2  
597  H H    . VAL   A 41  ? 0.550617 0.657052 1.1006   -0.0234975  -0.139336   0.319894    53  VAL   B H    
598  H HA   . VAL   A 41  ? 0.553562 0.632828 1.1653   -0.0349601  -0.0738906  0.283317    53  VAL   B HA   
599  H HB   . VAL   A 41  ? 0.544161 0.58767  1.0142   -0.0624292  -0.108647   0.277459    53  VAL   B HB   
600  H HG11 . VAL   A 41  ? 0.563117 0.569572 1.07261  -0.0695666  -0.0422996  0.245934    53  VAL   B HG11 
601  H HG12 . VAL   A 41  ? 0.541837 0.577041 1.02408  -0.0854639  -0.0781406  0.243186    53  VAL   B HG12 
602  H HG13 . VAL   A 41  ? 0.558122 0.534198 0.988615 -0.0810242  -0.0586735  0.241514    53  VAL   B HG13 
603  H HG21 . VAL   A 41  ? 0.573996 0.523072 1.01448  -0.0582761  -0.0616311  0.269236    53  VAL   B HG21 
604  H HG22 . VAL   A 41  ? 0.579849 0.566628 1.06612  -0.0383389  -0.0819     0.299594    53  VAL   B HG22 
605  H HG23 . VAL   A 41  ? 0.586115 0.556801 1.09993  -0.0371124  -0.0487512  0.278654    53  VAL   B HG23 
606  N N    . TYR   A 42  ? 0.521138 0.675882 1.17718  -0.0665378  -0.100894   0.261027    54  TYR   B N    
607  C CA   . TYR   A 42  ? 0.511414 0.711867 1.20767  -0.086114   -0.120418   0.247321    54  TYR   B CA   
608  C C    . TYR   A 42  ? 0.48226  0.641047 1.14414  -0.111217   -0.0913507  0.227846    54  TYR   B C    
609  O O    . TYR   A 42  ? 0.525061 0.656262 1.19623  -0.109747   -0.0476529  0.226862    54  TYR   B O    
610  C CB   . TYR   A 42  ? 0.530605 0.795505 1.33879  -0.0772336  -0.120819   0.253699    54  TYR   B CB   
611  C CG   . TYR   A 42  ? 0.588644 0.898306 1.44111  -0.0456865  -0.147974   0.276388    54  TYR   B CG   
612  C CD1  . TYR   A 42  ? 0.621757 0.896802 1.45956  -0.0178191  -0.127535   0.296037    54  TYR   B CD1  
613  C CD2  . TYR   A 42  ? 0.609901 0.994335 1.52185  -0.0421113  -0.194544   0.277701    54  TYR   B CD2  
614  C CE1  . TYR   A 42  ? 0.689899 0.998091 1.5662   0.0144383   -0.14948    0.321009    54  TYR   B CE1  
615  C CE2  . TYR   A 42  ? 0.673286 1.099    1.62184  -0.00806317 -0.220739   0.301663    54  TYR   B CE2  
616  C CZ   . TYR   A 42  ? 0.700032 1.08563  1.6304   0.021419    -0.196024   0.325837    54  TYR   B CZ   
617  O OH   . TYR   A 42  ? 0.851878 1.26992  1.81534  0.0583795   -0.219131   0.35368     54  TYR   B OH   
618  H H    . TYR   A 42  ? 0.527434 0.661683 1.19565  -0.0612216  -0.0718065  0.260346    54  TYR   B H    
619  H HA   . TYR   A 42  ? 0.50808  0.724124 1.18023  -0.087839   -0.153272   0.246763    54  TYR   B HA   
620  H HB2  . TYR   A 42  ? 0.540923 0.790481 1.37113  -0.0758695  -0.0843437  0.253118    54  TYR   B HB2  
621  H HB3  . TYR   A 42  ? 0.533877 0.82914  1.37205  -0.0941642  -0.136743   0.242453    54  TYR   B HB3  
622  H HD1  . TYR   A 42  ? 0.631352 0.856167 1.42982  -0.0203345  -0.0994433  0.292061    54  TYR   B HD1  
623  H HD2  . TYR   A 42  ? 0.61134  1.01744  1.5373   -0.0623669  -0.210635   0.261615    54  TYR   B HD2  
624  H HE1  . TYR   A 42  ? 0.694736 0.971699 1.56037  0.032477    -0.133999   0.334239    54  TYR   B HE1  
625  H HE2  . TYR   A 42  ? 0.670689 1.14937  1.65573  -0.00431456 -0.256341   0.30122     54  TYR   B HE2  
627  N N    . VAL   A 43  ? 0.445248 0.595242 1.06247  -0.130526   -0.113333   0.213207    55  VAL   B N    
628  C CA   . VAL   A 43  ? 0.458795 0.563246 1.03888  -0.150362   -0.0865664  0.198883    55  VAL   B CA   
629  C C    . VAL   A 43  ? 0.505329 0.629761 1.11318  -0.175196   -0.108002   0.18248     55  VAL   B C    
630  O O    . VAL   A 43  ? 0.529788 0.695184 1.15477  -0.175934   -0.15229    0.176722    55  VAL   B O    
631  C CB   . VAL   A 43  ? 0.471039 0.518361 0.948936 -0.148027   -0.0830353  0.194701    55  VAL   B CB   
632  C CG1  . VAL   A 43  ? 0.449363 0.474494 0.899965 -0.128157   -0.0701668  0.206614    55  VAL   B CG1  
633  C CG2  . VAL   A 43  ? 0.469177 0.523643 0.900749 -0.152239   -0.123136   0.18658     55  VAL   B CG2  
634  H H    . VAL   A 43  ? 0.453315 0.623609 1.06012  -0.129013   -0.144757   0.212726    55  VAL   B H    
635  H HA   . VAL   A 43  ? 0.474235 0.569726 1.07967  -0.149461   -0.0544429  0.201873    55  VAL   B HA   
636  H HB   . VAL   A 43  ? 0.477755 0.494561 0.936947 -0.156533   -0.0602768  0.188448    55  VAL   B HB   
637  H HG11 . VAL   A 43  ? 0.448197 0.498329 0.914697 -0.118777   -0.0898782  0.216231    55  VAL   B HG11 
638  H HG12 . VAL   A 43  ? 0.463806 0.480357 0.938197 -0.123463   -0.0438257  0.208643    55  VAL   B HG12 
639  H HG13 . VAL   A 43  ? 0.458026 0.451517 0.852036 -0.128912   -0.0684204  0.202402    55  VAL   B HG13 
640  H HG21 . VAL   A 43  ? 0.469888 0.495359 0.845678 -0.148153   -0.119491   0.186343    55  VAL   B HG21 
641  H HG22 . VAL   A 43  ? 0.478046 0.532665 0.917652 -0.1661     -0.128461   0.17494     55  VAL   B HG22 
642  H HG23 . VAL   A 43  ? 0.464614 0.551782 0.913942 -0.143787   -0.146297   0.193282    55  VAL   B HG23 
643  N N    . HIS   A 44  ? 0.512604 0.599369 1.1127   -0.193905   -0.0769836  0.174613    56  HIS   B N    
644  C CA   . HIS   A 44  ? 0.570974 0.641132 1.15878  -0.217875   -0.0927545  0.156768    56  HIS   B CA   
645  C C    . HIS   A 44  ? 0.597202 0.597116 1.08035  -0.214214   -0.0782135  0.153329    56  HIS   B C    
646  O O    . HIS   A 44  ? 0.594612 0.559253 1.03689  -0.201952   -0.0445889  0.163446    56  HIS   B O    
647  C CB   . HIS   A 44  ? 0.615601 0.698602 1.2909   -0.244196   -0.0685628  0.154037    56  HIS   B CB   
648  C CG   . HIS   A 44  ? 0.617001 0.773271 1.39576  -0.258382   -0.105253   0.144706    56  HIS   B CG   
649  N ND1  . HIS   A 44  ? 0.604739 0.783433 1.37406  -0.264488   -0.162946   0.124266    56  HIS   B ND1  
650  C CD2  . HIS   A 44  ? 0.587631 0.802429 1.48216  -0.266263   -0.0933812  0.151448    56  HIS   B CD2  
651  C CE1  . HIS   A 44  ? 0.624918 0.873734 1.49992  -0.27649    -0.18967    0.117379    56  HIS   B CE1  
652  N NE2  . HIS   A 44  ? 0.592481 0.867347 1.55037  -0.27834    -0.147939   0.134667    56  HIS   B NE2  
653  H H    . HIS   A 44  ? 0.529304 0.596    1.12922  -0.190329   -0.0432323  0.181108    56  HIS   B H    
654  H HA   . HIS   A 44  ? 0.56577  0.662274 1.15571  -0.217777   -0.130379   0.148681    56  HIS   B HA   
655  H HB2  . HIS   A 44  ? 0.611476 0.69015  1.30532  -0.238307   -0.0323247  0.166437    56  HIS   B HB2  
656  H HB3  . HIS   A 44  ? 0.632726 0.676771 1.27831  -0.257843   -0.0611781  0.146556    56  HIS   B HB3  
658  H HD2  . HIS   A 44  ? 0.593771 0.810192 1.52011  -0.262641   -0.0551823  0.164442    56  HIS   B HD2  
659  H HE1  . HIS   A 44  ? 0.625219 0.902205 1.51314  -0.281341   -0.23205    0.101847    56  HIS   B HE1  
661  N N    . TYR   A 45  ? 0.600255 0.581041 1.03888  -0.221906   -0.106019   0.137152    57  TYR   B N    
662  C CA   . TYR   A 45  ? 0.591388 0.513296 0.935648 -0.213486   -0.0963412  0.13462     57  TYR   B CA   
663  C C    . TYR   A 45  ? 0.611682 0.501772 0.937129 -0.229122   -0.110139   0.115819    57  TYR   B C    
664  O O    . TYR   A 45  ? 0.579724 0.497809 0.949324 -0.243755   -0.141025   0.099584    57  TYR   B O    
665  C CB   . TYR   A 45  ? 0.544964 0.472886 0.825443 -0.190585   -0.11675    0.138334    57  TYR   B CB   
666  C CG   . TYR   A 45  ? 0.540733 0.497554 0.80492  -0.186319   -0.160836   0.12686     57  TYR   B CG   
667  C CD1  . TYR   A 45  ? 0.534918 0.548396 0.844229 -0.181913   -0.188883   0.130733    57  TYR   B CD1  
668  C CD2  . TYR   A 45  ? 0.521371 0.448531 0.722093 -0.182778   -0.174048   0.112309    57  TYR   B CD2  
669  C CE1  . TYR   A 45  ? 0.523079 0.561386 0.80584  -0.174096   -0.228718   0.120507    57  TYR   B CE1  
670  C CE2  . TYR   A 45  ? 0.546511 0.497454 0.726273 -0.17626    -0.211443   0.0989414   57  TYR   B CE2  
671  C CZ   . TYR   A 45  ? 0.543525 0.549925 0.758526 -0.171212   -0.238761   0.103567    57  TYR   B CZ   
672  O OH   . TYR   A 45  ? 0.554773 0.582726 0.734918 -0.160163   -0.275333   0.0909599   57  TYR   B OH   
673  H H    . TYR   A 45  ? 0.601879 0.607162 1.06925  -0.230814   -0.132211   0.126539    57  TYR   B H    
674  H HA   . TYR   A 45  ? 0.597493 0.491869 0.930708 -0.211787   -0.0642188  0.143207    57  TYR   B HA   
675  H HB2  . TYR   A 45  ? 0.558369 0.450741 0.786934 -0.184623   -0.104615   0.138556    57  TYR   B HB2  
676  H HB3  . TYR   A 45  ? 0.531137 0.477774 0.830043 -0.182298   -0.110486   0.149455    57  TYR   B HB3  
677  H HD1  . TYR   A 45  ? 0.512929 0.547445 0.86745  -0.181185   -0.180095   0.141278    57  TYR   B HD1  
678  H HD2  . TYR   A 45  ? 0.547417 0.436337 0.71829  -0.183464   -0.157073   0.110605    57  TYR   B HD2  
679  H HE1  . TYR   A 45  ? 0.524414 0.600452 0.83252  -0.168329   -0.248518   0.124987    57  TYR   B HE1  
680  H HE2  . TYR   A 45  ? 0.565428 0.494552 0.700291 -0.17106    -0.21762    0.0883034   57  TYR   B HE2  
682  N N    . LYS   A 46  ? 0.628159 0.456931 0.885661 -0.223678   -0.0884387  0.117223    58  LYS   B N    
683  C CA   . LYS   A 46  ? 0.668584 0.453457 0.881979 -0.227643   -0.101554   0.100645    58  LYS   B CA   
684  C C    . LYS   A 46  ? 0.691798 0.452891 0.814912 -0.200315   -0.104909   0.103258    58  LYS   B C    
685  O O    . LYS   A 46  ? 0.681477 0.42647  0.772424 -0.187128   -0.080517   0.118548    58  LYS   B O    
686  C CB   . LYS   A 46  ? 0.700266 0.430497 0.930372 -0.246735   -0.0663967  0.104875    58  LYS   B CB   
687  C CG   . LYS   A 46  ? 0.715415 0.475726 1.05165  -0.278259   -0.0603306  0.102706    58  LYS   B CG   
688  C CD   . LYS   A 46  ? 0.760025 0.461904 1.11009  -0.295903   -0.012651   0.116071    58  LYS   B CD   
689  C CE   . LYS   A 46  ? 0.783577 0.517207 1.24782  -0.327448   0.0083418   0.121623    58  LYS   B CE   
690  N NZ   . LYS   A 46  ? 0.84734  0.51629  1.31923  -0.345661   0.057452    0.137423    58  LYS   B NZ   
691  H H    . LYS   A 46  ? 0.629281 0.441454 0.865426 -0.215055   -0.0647516  0.128779    58  LYS   B H    
692  H HA   . LYS   A 46  ? 0.672099 0.479649 0.905477 -0.234292   -0.130626   0.0857604   58  LYS   B HA   
693  H HB2  . LYS   A 46  ? 0.709066 0.418051 0.913001 -0.237162   -0.0379145  0.120329    58  LYS   B HB2  
694  H HB3  . LYS   A 46  ? 0.73763  0.430545 0.933922 -0.247078   -0.0738613  0.0945562   58  LYS   B HB3  
695  H HG2  . LYS   A 46  ? 0.718758 0.494134 1.07837  -0.289414   -0.0910999  0.084117    58  LYS   B HG2  
696  H HG3  . LYS   A 46  ? 0.680087 0.482369 1.05311  -0.275004   -0.0558064  0.111865    58  LYS   B HG3  
697  H HD2  . LYS   A 46  ? 0.767571 0.446813 1.07296  -0.279557   0.014496    0.132533    58  LYS   B HD2  
698  H HD3  . LYS   A 46  ? 0.801295 0.460421 1.12276  -0.300651   -0.0198412  0.106048    58  LYS   B HD3  
699  H HE2  . LYS   A 46  ? 0.7768   0.539938 1.28989  -0.343615   -0.0233653  0.103382    58  LYS   B HE2  
700  H HE3  . LYS   A 46  ? 0.750304 0.521015 1.2403   -0.319514   0.021447    0.133489    58  LYS   B HE3  
701  H HZ1  . LYS   A 46  ? 0.879326 0.50934  1.32923  -0.352907   0.0457699   0.126494    58  LYS   B HZ1  
702  H HZ2  . LYS   A 46  ? 0.855925 0.497776 1.27754  -0.328469   0.0860868   0.154579    58  LYS   B HZ2  
703  H HZ3  . LYS   A 46  ? 0.851564 0.545416 1.40046  -0.366108   0.0717636   0.14163     58  LYS   B HZ3  
704  N N    . GLY   A 47  ? 0.69606  0.460243 0.78067  -0.190284   -0.13583    0.087287    59  GLY   B N    
705  C CA   . GLY   A 47  ? 0.702132 0.456049 0.714201 -0.163678   -0.137944   0.0910755   59  GLY   B CA   
706  C C    . GLY   A 47  ? 0.706479 0.416363 0.668512 -0.155044   -0.147774   0.0734847   59  GLY   B C    
707  O O    . GLY   A 47  ? 0.738647 0.437869 0.71931  -0.168776   -0.164527   0.0534572   59  GLY   B O    
708  H H    . GLY   A 47  ? 0.711132 0.485538 0.815222 -0.199143   -0.155631   0.0732395   59  GLY   B H    
709  H HA2  . GLY   A 47  ? 0.68495  0.422712 0.681862 -0.158089   -0.117441   0.103221    59  GLY   B HA2  
710  H HA3  . GLY   A 47  ? 0.662538 0.454817 0.674279 -0.155455   -0.15314    0.0931671   59  GLY   B HA3  
711  N N    . LYS   A 48  ? 0.683109 0.37134  0.584638 -0.130645   -0.140569   0.0789406   60  LYS   B N    
712  C CA   . LYS   A 48  ? 0.75455  0.404189 0.604645 -0.11359    -0.148857   0.0637793   60  LYS   B CA   
713  C C    . LYS   A 48  ? 0.739867 0.407988 0.54069  -0.0819761  -0.150505   0.0713884   60  LYS   B C    
714  O O    . LYS   A 48  ? 0.732658 0.427141 0.536282 -0.0769899  -0.142145   0.0882901   60  LYS   B O    
715  C CB   . LYS   A 48  ? 0.844613 0.416722 0.682093 -0.120013   -0.126916   0.064321    60  LYS   B CB   
716  C CG   . LYS   A 48  ? 0.857098 0.403463 0.67657  -0.113425   -0.0967925  0.0889025   60  LYS   B CG   
717  C CD   . LYS   A 48  ? 0.973551 0.437844 0.774311 -0.117255   -0.0706308  0.0959882   60  LYS   B CD   
718  C CE   . LYS   A 48  ? 1.05763  0.470877 0.799299 -0.090758   -0.0764278  0.0884591   60  LYS   B CE   
719  N NZ   . LYS   A 48  ? 1.18794  0.515885 0.910994 -0.093766   -0.0465603  0.102594    60  LYS   B NZ   
720  H H    . LYS   A 48  ? 0.67514  0.373809 0.568933 -0.123301   -0.130884   0.0917052   60  LYS   B H    
721  H HA   . LYS   A 48  ? 0.765129 0.426101 0.621551 -0.117266   -0.167788   0.0477597   60  LYS   B HA   
722  H HB2  . LYS   A 48  ? 0.874754 0.418177 0.676214 -0.105354   -0.132693   0.0542398   60  LYS   B HB2  
723  H HB3  . LYS   A 48  ? 0.852751 0.415751 0.728873 -0.142568   -0.12693    0.0574538   60  LYS   B HB3  
724  H HG2  . LYS   A 48  ? 0.833614 0.406374 0.686678 -0.12611    -0.0894651  0.0973031   60  LYS   B HG2  
725  H HG3  . LYS   A 48  ? 0.85307  0.411103 0.637912 -0.0919213  -0.100483   0.0936167   60  LYS   B HG3  
726  H HD2  . LYS   A 48  ? 0.983845 0.437184 0.825383 -0.141067   -0.0678166  0.0896142   60  LYS   B HD2  
727  H HD3  . LYS   A 48  ? 0.972214 0.426206 0.761824 -0.113575   -0.0504569  0.11334     60  LYS   B HD3  
728  H HE2  . LYS   A 48  ? 1.04735  0.478436 0.755263 -0.0668693  -0.0811448  0.0941274   60  LYS   B HE2  
729  H HE3  . LYS   A 48  ? 1.0689   0.485083 0.817405 -0.0937309  -0.0942674  0.0691317   60  LYS   B HE3  
730  H HZ1  . LYS   A 48  ? 1.16874  0.492743 0.876934 -0.0876164  -0.0297106  0.120819    60  LYS   B HZ1  
731  H HZ2  . LYS   A 48  ? 1.18354  0.496808 0.945288 -0.118745   -0.0407642  0.0978877   60  LYS   B HZ2  
732  H HZ3  . LYS   A 48  ? 1.2085   0.500885 0.895944 -0.0758938  -0.0499872  0.0984324   60  LYS   B HZ3  
733  N N    . LEU   A 49  ? 0.778187 0.430647 0.536943 -0.060422   -0.161      0.0567245   61  LEU   B N    
734  C CA   . LEU   A 49  ? 0.787678 0.458161 0.507191 -0.0283496  -0.160132   0.0634432   61  LEU   B CA   
735  C C    . LEU   A 49  ? 0.805271 0.418111 0.494088 -0.0155032  -0.143397   0.0719045   61  LEU   B C    
736  O O    . LEU   A 49  ? 0.822161 0.371168 0.506513 -0.0259848  -0.133824   0.066999    61  LEU   B O    
737  C CB   . LEU   A 49  ? 0.830871 0.50551  0.516596 -0.00593558 -0.174107   0.0435731   61  LEU   B CB   
738  C CG   . LEU   A 49  ? 0.880185 0.60374  0.578744 -0.0128868  -0.192395   0.0338551   61  LEU   B CG   
739  C CD1  . LEU   A 49  ? 0.925871 0.643419 0.576872 0.0133745   -0.203353   0.0108528   61  LEU   B CD1  
740  C CD2  . LEU   A 49  ? 0.855652 0.647283 0.577938 -0.0123462  -0.188911   0.0581511   61  LEU   B CD2  
741  H H    . LEU   A 49  ? 0.812577 0.44338  0.569493 -0.0653954  -0.169128   0.0408262   61  LEU   B H    
742  H HA   . LEU   A 49  ? 0.742309 0.456438 0.477111 -0.0287572  -0.160426   0.0753296   61  LEU   B HA   
743  H HB2  . LEU   A 49  ? 0.889362 0.513463 0.558881 -0.00521923 -0.17367    0.0303012   61  LEU   B HB2  
744  H HB3  . LEU   A 49  ? 0.839756 0.531206 0.505861 0.0165162   -0.170907   0.049652    61  LEU   B HB3  
745  H HG   . LEU   A 49  ? 0.87327  0.586505 0.597406 -0.0351272  -0.198596   0.0275997   61  LEU   B HG   
746  H HD11 . LEU   A 49  ? 0.973137 0.639925 0.610722 0.0112957   -0.206213   -0.00675709 61  LEU   B HD11 
747  H HD12 . LEU   A 49  ? 0.922671 0.672109 0.575798 0.0106436   -0.215229   0.00643542  61  LEU   B HD12 
748  H HD13 . LEU   A 49  ? 0.926304 0.658139 0.557367 0.0364453   -0.19526    0.0178399   61  LEU   B HD13 
749  H HD21 . LEU   A 49  ? 0.81538  0.609197 0.568597 -0.0309587  -0.185017   0.0678132   61  LEU   B HD21 
750  H HD22 . LEU   A 49  ? 0.836258 0.637255 0.546091 0.00382427  -0.181134   0.0663598   61  LEU   B HD22 
751  H HD23 . LEU   A 49  ? 0.840159 0.663776 0.560122 -0.00892903 -0.198045   0.0561923   61  LEU   B HD23 
752  N N    . SER   A 50  ? 0.830214 0.465001 0.499107 0.00740401  -0.140877   0.0851911   62  SER   B N    
753  C CA   . SER   A 50  ? 0.941079 0.524027 0.567553 0.030748    -0.130878   0.0930125   62  SER   B CA   
754  C C    . SER   A 50  ? 0.972971 0.502949 0.56213  0.0543639   -0.131585   0.079988    62  SER   B C    
755  O O    . SER   A 50  ? 1.08643  0.547499 0.644661 0.0644969   -0.118871   0.0872413   62  SER   B O    
756  C CB   . SER   A 50  ? 0.962056 0.588274 0.578046 0.0534437   -0.136771   0.104518    62  SER   B CB   
757  O OG   . SER   A 50  ? 1.04024  0.695657 0.685888 0.0299021   -0.134348   0.113176    62  SER   B OG   
758  H H    . SER   A 50  ? 0.795472 0.478258 0.478448 0.00881223  -0.1465     0.0898501   62  SER   B H    
759  H HA   . SER   A 50  ? 0.945461 0.493701 0.573623 0.0169742   -0.118594   0.100191    62  SER   B HA   
760  H HB2  . SER   A 50  ? 0.959833 0.627    0.582217 0.0652755   -0.145892   0.100026    62  SER   B HB2  
761  H HB3  . SER   A 50  ? 1.01514  0.607541 0.599768 0.0717476   -0.132775   0.110237    62  SER   B HB3  
763  N N    . ASN   A 51  ? 0.987469 0.541769 0.573986 0.0653635   -0.143866   0.0616819   63  ASN   B N    
764  C CA   . ASN   A 51  ? 1.08394  0.580718 0.631127 0.0907319   -0.143989   0.0445524   63  ASN   B CA   
765  C C    . ASN   A 51  ? 1.12288  0.538911 0.672549 0.0646485   -0.139959   0.029188    63  ASN   B C    
766  O O    . ASN   A 51  ? 1.17162  0.523259 0.689071 0.0820826   -0.139403   0.0124643   63  ASN   B O    
767  C CB   . ASN   A 51  ? 1.09888  0.643241 0.634315 0.114704    -0.155081   0.0275408   63  ASN   B CB   
768  C CG   . ASN   A 51  ? 1.13686  0.702006 0.688912 0.0895794   -0.167966   0.00783039  63  ASN   B CG   
769  O OD1  . ASN   A 51  ? 1.06885  0.621177 0.652955 0.0518859   -0.171523   0.00630055  63  ASN   B OD1  
770  N ND2  . ASN   A 51  ? 1.1694   0.768115 0.698386 0.113053    -0.175004   -0.00743327 63  ASN   B ND2  
771  H H    . ASN   A 51  ? 0.950086 0.554668 0.556263 0.0588765   -0.151167   0.0599398   63  ASN   B H    
772  H HA   . ASN   A 51  ? 1.10436  0.579576 0.628162 0.113472    -0.137955   0.0547335   63  ASN   B HA   
773  H HB2  . ASN   A 51  ? 1.15787  0.664288 0.66274  0.139231    -0.152993   0.0178309   63  ASN   B HB2  
774  H HB3  . ASN   A 51  ? 1.06644  0.666963 0.611789 0.125727    -0.155569   0.0395144   63  ASN   B HB3  
775  H HD21 . ASN   A 51  ? 1.16858  0.774708 0.697488 0.102824    -0.184645   -0.0208516  63  ASN   B HD21 
776  H HD22 . ASN   A 51  ? 1.16998  0.785178 0.68294  0.140264    -0.16971    -0.00394399 63  ASN   B HD22 
777  N N    . GLY   A 52  ? 1.09989  0.51777  0.692627 0.0233957   -0.136376   0.0339317   64  GLY   B N    
778  C CA   . GLY   A 52  ? 1.15271  0.499476 0.764356 -0.00664391 -0.129635   0.0232072   64  GLY   B CA   
779  C C    . GLY   A 52  ? 1.18571  0.531814 0.812206 -0.0225274  -0.153255   -0.0131707  64  GLY   B C    
780  O O    . GLY   A 52  ? 1.21503  0.503195 0.864241 -0.049767   -0.153374   -0.0289531  64  GLY   B O    
781  H H    . GLY   A 52  ? 1.04625  0.512233 0.661943 0.0131134   -0.137673   0.0438326   64  GLY   B H    
782  H HA2  . GLY   A 52  ? 1.12916  0.48502  0.772706 -0.0302453  -0.12027    0.0360595   64  GLY   B HA2  
783  H HA3  . GLY   A 52  ? 1.2097   0.496058 0.793657 0.00672924  -0.117979   0.0275192   64  GLY   B HA3  
784  N N    . LYS   A 53  ? 1.14224  0.55201  0.755441 -0.0057933  -0.17363    -0.0270426  65  LYS   B N    
785  C CA   . LYS   A 53  ? 1.23132  0.630657 0.828816 -0.004801   -0.197576   -0.0650756  65  LYS   B CA   
786  C C    . LYS   A 53  ? 1.17438  0.63495  0.817275 -0.0360086  -0.220261   -0.0742291  65  LYS   B C    
787  O O    . LYS   A 53  ? 1.21601  0.667374 0.851855 -0.0426574  -0.245893   -0.108562   65  LYS   B O    
788  C CB   . LYS   A 53  ? 1.25461  0.665005 0.790518 0.0439582   -0.200604   -0.0766274  65  LYS   B CB   
789  H H    . LYS   A 53  ? 1.10777  0.5677   0.719991 0.00548656  -0.172174   -0.0125227  65  LYS   B H    
790  H HA   . LYS   A 53  ? 1.27652  0.610976 0.873584 -0.0150845  -0.196235   -0.0791474  65  LYS   B HA   
793  N N    . LYS   A 54  ? 1.09791  0.617405 0.786104 -0.0537679  -0.213651   -0.0462232  66  LYS   B N    
794  C CA   . LYS   A 54  ? 1.02473  0.599069 0.760542 -0.0803042  -0.235261   -0.0521618  66  LYS   B CA   
795  C C    . LYS   A 54  ? 0.965661 0.55571  0.766861 -0.110626   -0.218271   -0.0262088  66  LYS   B C    
796  O O    . LYS   A 54  ? 0.923626 0.520342 0.721317 -0.102104   -0.193965   0.00232367  66  LYS   B O    
797  C CB   . LYS   A 54  ? 0.970795 0.622485 0.686267 -0.0594518  -0.249986   -0.0465906  66  LYS   B CB   
798  H H    . LYS   A 54  ? 1.05996  0.585126 0.748472 -0.0475968  -0.196918   -0.0241571  66  LYS   B H    
799  H HA   . LYS   A 54  ? 1.07158  0.620399 0.812837 -0.0926238  -0.251841   -0.0777037  66  LYS   B HA   
802  N N    . PHE   A 55  ? 0.905644 0.50406  0.766459 -0.144128   -0.232866   -0.0389891  67  PHE   B N    
803  C CA   . PHE   A 55  ? 0.88066  0.504132 0.814348 -0.172734   -0.217799   -0.0179703  67  PHE   B CA   
804  C C    . PHE   A 55  ? 0.878946 0.573265 0.862514 -0.185983   -0.248619   -0.025877   67  PHE   B C    
805  O O    . PHE   A 55  ? 0.913226 0.614805 0.891085 -0.188424   -0.283983   -0.0564317  67  PHE   B O    
806  C CB   . PHE   A 55  ? 0.922959 0.486801 0.902789 -0.204807   -0.200474   -0.0227206  67  PHE   B CB   
807  C CG   . PHE   A 55  ? 1.01026  0.490323 0.93303  -0.189102   -0.175492   -0.0183194  67  PHE   B CG   
808  C CD1  . PHE   A 55  ? 1.10157  0.52967  0.973785 -0.174287   -0.192002   -0.0469977  67  PHE   B CD1  
809  C CD2  . PHE   A 55  ? 1.03508  0.487668 0.946633 -0.183221   -0.136342   0.0146734   67  PHE   B CD2  
810  C CE1  . PHE   A 55  ? 1.20721  0.5556   1.02773  -0.154915   -0.168856   -0.0402911  67  PHE   B CE1  
811  C CE2  . PHE   A 55  ? 1.11161  0.487297 0.965956 -0.163578   -0.115776   0.0221092   67  PHE   B CE2  
812  C CZ   . PHE   A 55  ? 1.17512  0.498984 0.986859 -0.14887    -0.131609   -0.00373186 67  PHE   B CZ   
813  H H    . PHE   A 55  ? 0.961711 0.551432 0.819049 -0.148445   -0.254049   -0.0636259  67  PHE   B H    
814  H HA   . PHE   A 55  ? 0.845811 0.481087 0.770632 -0.162518   -0.19846    0.0052533   67  PHE   B HA   
815  H HB2  . PHE   A 55  ? 0.960888 0.523104 0.966141 -0.221088   -0.22282    -0.0465801  67  PHE   B HB2  
816  H HB3  . PHE   A 55  ? 0.902327 0.48384  0.925015 -0.218583   -0.182782   -0.00410172 67  PHE   B HB3  
817  H HD1  . PHE   A 55  ? 1.11937  0.563687 0.991149 -0.175989   -0.219208   -0.0716406  67  PHE   B HD1  
818  H HD2  . PHE   A 55  ? 0.992112 0.476115 0.93274  -0.190903   -0.124041   0.0317808   67  PHE   B HD2  
819  H HE1  . PHE   A 55  ? 1.23869  0.549009 1.02609  -0.143008   -0.179124   -0.0606489  67  PHE   B HE1  
820  H HE2  . PHE   A 55  ? 1.10798  0.465394 0.949314 -0.157568   -0.0911465  0.0447926   67  PHE   B HE2  
821  H HZ   . PHE   A 55  ? 1.22219  0.492716 0.995821 -0.132591   -0.117474   0.0029367   67  PHE   B HZ   
822  N N    . ASP   A 56  ? 0.796047 0.536075 0.831555 -0.195347   -0.235838   -0.00063382 68  ASP   B N    
823  C CA   . ASP   A 56  ? 0.799735 0.609817 0.882331 -0.20124    -0.263783   -0.001694   68  ASP   B CA   
824  C C    . ASP   A 56  ? 0.754355 0.588674 0.915238 -0.220463   -0.239446   0.0215652   68  ASP   B C    
825  O O    . ASP   A 56  ? 0.682971 0.501338 0.83165  -0.213305   -0.204228   0.0456905   68  ASP   B O    
826  C CB   . ASP   A 56  ? 0.780018 0.634839 0.813054 -0.170133   -0.274261   0.0122567   68  ASP   B CB   
827  C CG   . ASP   A 56  ? 0.749403 0.673777 0.826305 -0.169452   -0.294462   0.0246795   68  ASP   B CG   
828  O OD1  . ASP   A 56  ? 0.786419 0.736584 0.899478 -0.181338   -0.327876   0.00495768  68  ASP   B OD1  
829  O OD2  . ASP   A 56  ? 0.667764 0.617865 0.745897 -0.157266   -0.277754   0.0535051   68  ASP   B OD2  
830  H H    . ASP   A 56  ? 0.792374 0.518635 0.831828 -0.195819   -0.20956    0.0175667   68  ASP   B H    
831  H HA   . ASP   A 56  ? 0.827645 0.638592 0.925233 -0.212147   -0.28918    -0.0251459  68  ASP   B HA   
832  H HB2  . ASP   A 56  ? 0.807919 0.653379 0.794004 -0.156854   -0.289852   -0.00361647 68  ASP   B HB2  
833  H HB3  . ASP   A 56  ? 0.752798 0.598186 0.767233 -0.16069    -0.250683   0.0304092   68  ASP   B HB3  
834  N N    . SER   A 57  ? 0.751281 0.627543 0.991181 -0.241825   -0.259602   0.0129325   69  SER   B N    
835  C CA   . SER   A 57  ? 0.732097 0.637585 1.05415  -0.25712    -0.234282   0.0342747   69  SER   B CA   
836  C C    . SER   A 57  ? 0.721462 0.705596 1.10469  -0.256143   -0.267941   0.0343773   69  SER   B C    
837  O O    . SER   A 57  ? 0.797016 0.806273 1.19431  -0.262633   -0.312749   0.00846197  69  SER   B O    
838  C CB   . SER   A 57  ? 0.801685 0.671789 1.18418  -0.289954   -0.210416   0.028776    69  SER   B CB   
839  O OG   . SER   A 57  ? 0.837416 0.755339 1.3152   -0.304295   -0.192613   0.0453842   69  SER   B OG   
840  H H    . SER   A 57  ? 0.7797   0.668524 1.02316  -0.245577   -0.290249   -0.00755767 69  SER   B H    
841  H HA   . SER   A 57  ? 0.71116  0.60914  1.00877  -0.243922   -0.2089     0.0544759   69  SER   B HA   
842  H HB2  . SER   A 57  ? 0.818835 0.639972 1.16284  -0.286424   -0.181732   0.0376522   69  SER   B HB2  
843  H HB3  . SER   A 57  ? 0.84128  0.703731 1.23676  -0.30401    -0.234867   0.00528157  69  SER   B HB3  
845  N N    . SER   A 58  ? 0.663888 0.683557 1.0861   -0.247581   -0.246516   0.0620173   70  SER   B N    
846  C CA   . SER   A 58  ? 0.682431 0.775849 1.17528  -0.244186   -0.27268    0.0676567   70  SER   B CA   
847  C C    . SER   A 58  ? 0.734548 0.858031 1.32541  -0.2758     -0.292965   0.0462066   70  SER   B C    
848  O O    . SER   A 58  ? 0.8187   1.00276  1.45252  -0.274208   -0.339387   0.0347104   70  SER   B O    
849  C CB   . SER   A 58  ? 0.621776 0.73402  1.14522  -0.230686   -0.238419   0.0988574   70  SER   B CB   
850  O OG   . SER   A 58  ? 0.601715 0.682296 1.16004  -0.247126   -0.189644   0.106574    70  SER   B OG   
851  H H    . SER   A 58  ? 0.660748 0.656606 1.06343  -0.241848   -0.215595   0.0771179   70  SER   B H    
852  H HA   . SER   A 58  ? 0.680623 0.79225  1.13531  -0.22834    -0.302523   0.0637017   70  SER   B HA   
853  H HB2  . SER   A 58  ? 0.612471 0.773472 1.18826  -0.226907   -0.255406   0.103323    70  SER   B HB2  
854  H HB3  . SER   A 58  ? 0.608079 0.70526  1.07409  -0.212485   -0.232471   0.109707    70  SER   B HB3  
856  N N    . HIS   A 59  ? 0.737452 0.818705 1.36374  -0.304394   -0.259444   0.0414733   71  HIS   B N    
857  C CA   . HIS   A 59  ? 0.8089   0.917125 1.54533  -0.34121    -0.270561   0.0237771   71  HIS   B CA   
858  C C    . HIS   A 59  ? 0.856155 0.967008 1.58443  -0.354828   -0.331038   -0.0176777  71  HIS   B C    
859  O O    . HIS   A 59  ? 0.78403  0.950357 1.60735  -0.376982   -0.366423   -0.036766   71  HIS   B O    
860  C CB   . HIS   A 59  ? 0.809734 0.861893 1.57718  -0.368163   -0.213854   0.0334176   71  HIS   B CB   
861  C CG   . HIS   A 59  ? 0.794806 0.861026 1.59719  -0.358763   -0.158473   0.0685592   71  HIS   B CG   
862  N ND1  . HIS   A 59  ? 0.794847 0.804895 1.51376  -0.337738   -0.111983   0.0912399   71  HIS   B ND1  
863  C CD2  . HIS   A 59  ? 0.801257 0.933728 1.71329  -0.364914   -0.143931   0.0823431   71  HIS   B CD2  
864  C CE1  . HIS   A 59  ? 0.76575  0.800722 1.53465  -0.331576   -0.0696566  0.115664    71  HIS   B CE1  
865  N NE2  . HIS   A 59  ? 0.784584 0.894957 1.67232  -0.346376   -0.0860434  0.112075    71  HIS   B NE2  
866  H H    . HIS   A 59  ? 0.750355 0.785606 1.33372  -0.301091   -0.228135   0.050892    71  HIS   B H    
867  H HA   . HIS   A 59  ? 0.773328 0.938962 1.57641  -0.338949   -0.275335   0.0334583   71  HIS   B HA   
868  H HB2  . HIS   A 59  ? 0.837535 0.829857 1.53036  -0.363188   -0.203147   0.0307103   71  HIS   B HB2  
869  H HB3  . HIS   A 59  ? 0.844996 0.908379 1.68247  -0.396316   -0.224286   0.0183605   71  HIS   B HB3  
871  H HD2  . HIS   A 59  ? 0.794493 0.980278 1.78502  -0.377582   -0.169526   0.0725339   71  HIS   B HD2  
872  H HE1  . HIS   A 59  ? 0.771454 0.777694 1.49792  -0.317104   -0.0358711  0.131388    71  HIS   B HE1  
874  N N    . ASP   A 60  ? 0.96714  1.02134  1.58177  -0.338829   -0.344118   -0.0329894  72  ASP   B N    
875  C CA   . ASP   A 60  ? 1.05824  1.1095   1.63605  -0.34022    -0.402366   -0.074471   72  ASP   B CA   
876  C C    . ASP   A 60  ? 1.03543  1.17537  1.64796  -0.327579   -0.458879   -0.082701   72  ASP   B C    
877  O O    . ASP   A 60  ? 1.16079  1.32012  1.79533  -0.341552   -0.512356   -0.121156   72  ASP   B O    
878  C CB   . ASP   A 60  ? 1.08127  1.07861  1.52234  -0.308336   -0.403828   -0.0799131  72  ASP   B CB   
879  C CG   . ASP   A 60  ? 1.06178  0.970079 1.44941  -0.31101    -0.357274   -0.0739069  72  ASP   B CG   
880  O OD1  . ASP   A 60  ? 1.0331   0.899553 1.47464  -0.344444   -0.339867   -0.0836744  72  ASP   B OD1  
881  O OD2  . ASP   A 60  ? 1.01649  0.899507 1.3122   -0.279299   -0.339758   -0.0585602  72  ASP   B OD2  
882  H H    . ASP   A 60  ? 0.939593 0.955911 1.49662  -0.325036   -0.315384   -0.0179425  72  ASP   B H    
883  H HA   . ASP   A 60  ? 1.08538  1.1123   1.70376  -0.368606   -0.40621    -0.0952766  72  ASP   B HA   
884  H HB2  . ASP   A 60  ? 1.03616  1.0595   1.44316  -0.282912   -0.400257   -0.0589872  72  ASP   B HB2  
885  H HB3  . ASP   A 60  ? 1.11455  1.11112  1.5303   -0.307369   -0.442149   -0.109236   72  ASP   B HB3  
886  N N    . ARG   A 61  ? 0.989491 1.17776  1.59813  -0.298149   -0.449162   -0.0473523  73  ARG   B N    
887  C CA   . ARG   A 61  ? 0.933937 1.20276  1.56482  -0.277241   -0.498208   -0.0452526  73  ARG   B CA   
888  C C    . ARG   A 61  ? 0.846738 1.18764  1.62248  -0.296151   -0.499964   -0.0358252  73  ARG   B C    
889  O O    . ARG   A 61  ? 0.847615 1.26242  1.66029  -0.277608   -0.539207   -0.029912   73  ARG   B O    
890  C CB   . ARG   A 61  ? 0.846172 1.11533  1.38795  -0.233652   -0.482553   -0.00963295 73  ARG   B CB   
891  H H    . ARG   A 61  ? 0.941184 1.10816  1.52967  -0.289418   -0.410595   -0.023164   73  ARG   B H    
892  H HA   . ARG   A 61  ? 0.967528 1.24039  1.57276  -0.277946   -0.540973   -0.0744027  73  ARG   B HA   
895  N N    . ASN   A 62  ? 0.793617 1.11538  1.65221  -0.329905   -0.455165   -0.0314204  74  ASN   B N    
896  C CA   . ASN   A 62  ? 0.737595 1.12915  1.74179  -0.347785   -0.445315   -0.0195912  74  ASN   B CA   
897  C C    . ASN   A 62  ? 0.690169 1.13842  1.70535  -0.308312   -0.439372   0.0171052   74  ASN   B C    
898  O O    . ASN   A 62  ? 0.689687 1.22138  1.80494  -0.305173   -0.466736   0.0201728   74  ASN   B O    
899  C CB   . ASN   A 62  ? 0.79217  1.23858  1.89842  -0.381086   -0.503073   -0.0587628  74  ASN   B CB   
900  H H    . ASN   A 62  ? 0.805753 1.06955  1.62908  -0.340681   -0.427884   -0.0343933  74  ASN   B H    
901  H HA   . ASN   A 62  ? 0.73514  1.09487  1.76602  -0.364666   -0.39823    -0.00863223 74  ASN   B HA   
904  N N    . GLU   A 63  ? 0.700336 1.10382  1.61995  -0.277657   -0.403091   0.0457135   75  GLU   B N    
905  C CA   . GLU   A 63  ? 0.660053 1.10463  1.59594  -0.242859   -0.391751   0.0806825   75  GLU   B CA   
906  C C    . GLU   A 63  ? 0.586413 0.964877 1.43201  -0.222844   -0.339423   0.107058    75  GLU   B C    
907  O O    . GLU   A 63  ? 0.577153 0.893156 1.32323  -0.223597   -0.332842   0.0988421   75  GLU   B O    
908  C CB   . GLU   A 63  ? 0.700328 1.19903  1.60949  -0.210991   -0.453151   0.0822942   75  GLU   B CB   
909  C CG   . GLU   A 63  ? 0.753984 1.20567  1.52237  -0.19281    -0.475052   0.0748086   75  GLU   B CG   
910  C CD   . GLU   A 63  ? 0.781069 1.27815  1.50681  -0.153068   -0.521258   0.0895289   75  GLU   B CD   
911  O OE1  . GLU   A 63  ? 0.778993 1.23806  1.40296  -0.127088   -0.506391   0.110774    75  GLU   B OE1  
912  O OE2  . GLU   A 63  ? 0.774549 1.34524  1.57064  -0.147382   -0.569731   0.0825056   75  GLU   B OE2  
913  H H    . GLU   A 63  ? 0.693902 1.04086  1.54196  -0.278612   -0.385899   0.0429528   75  GLU   B H    
914  H HA   . GLU   A 63  ? 0.644774 1.12616  1.67265  -0.251304   -0.376424   0.0878639   75  GLU   B HA   
915  H HB2  . GLU   A 63  ? 0.681254 1.20228  1.60809  -0.188401   -0.44151    0.107937    75  GLU   B HB2  
916  H HB3  . GLU   A 63  ? 0.721434 1.26734  1.69102  -0.222415   -0.490761   0.063848    75  GLU   B HB3  
917  H HG2  . GLU   A 63  ? 0.776319 1.21183  1.52895  -0.211203   -0.494763   0.0462656   75  GLU   B HG2  
918  H HG3  . GLU   A 63  ? 0.727499 1.1314   1.44308  -0.187495   -0.437687   0.0889582   75  GLU   B HG3  
919  N N    . PRO   A 64  ? 0.549887 0.941263 1.42963  -0.20305    -0.303183   0.137087    76  PRO   B N    
920  C CA   . PRO   A 64  ? 0.538635 0.870102 1.33629  -0.184233   -0.261183   0.157882    76  PRO   B CA   
921  C C    . PRO   A 64  ? 0.535764 0.84509  1.22665  -0.162635   -0.288481   0.161998    76  PRO   B C    
922  O O    . PRO   A 64  ? 0.563581 0.914368 1.24802  -0.149337   -0.33655    0.159621    76  PRO   B O    
923  C CB   . PRO   A 64  ? 0.520586 0.883028 1.38195  -0.161502   -0.235934   0.1842      76  PRO   B CB   
924  C CG   . PRO   A 64  ? 0.548186 0.986447 1.54022  -0.172917   -0.249492   0.178694    76  PRO   B CG   
925  C CD   . PRO   A 64  ? 0.567041 1.03329  1.56724  -0.195173   -0.305041   0.150013    76  PRO   B CD   
926  H HA   . PRO   A 64  ? 0.535434 0.82422  1.31359  -0.199099   -0.230714   0.152735    76  PRO   B HA   
927  H HB2  . PRO   A 64  ? 0.525731 0.896467 1.35955  -0.138641   -0.252388   0.197384    76  PRO   B HB2  
928  H HB3  . PRO   A 64  ? 0.518667 0.843891 1.36582  -0.161754   -0.194664   0.190958    76  PRO   B HB3  
929  H HG2  . PRO   A 64  ? 0.537975 1.01521  1.5674   -0.150963   -0.259547   0.193215    76  PRO   B HG2  
930  H HG3  . PRO   A 64  ? 0.537952 0.967726 1.57186  -0.187095   -0.212586   0.178584    76  PRO   B HG3  
931  H HD2  . PRO   A 64  ? 0.570515 1.07892  1.57856  -0.179092   -0.34536    0.151553    76  PRO   B HD2  
932  H HD3  . PRO   A 64  ? 0.566795 1.05442  1.63955  -0.219009   -0.300223   0.138455    76  PRO   B HD3  
933  N N    . PHE   A 65  ? 0.520158 0.767124 1.12855  -0.158511   -0.257464   0.168449    77  PHE   B N    
934  C CA   . PHE   A 65  ? 0.556733 0.783943 1.07678  -0.137069   -0.268275   0.180497    77  PHE   B CA   
935  C C    . PHE   A 65  ? 0.549485 0.77651  1.0811   -0.114229   -0.246526   0.210717    77  PHE   B C    
936  O O    . PHE   A 65  ? 0.572235 0.769718 1.12083  -0.117219   -0.205838   0.215761    77  PHE   B O    
937  C CB   . PHE   A 65  ? 0.599344 0.764014 1.04076  -0.146844   -0.24521    0.170052    77  PHE   B CB   
938  C CG   . PHE   A 65  ? 0.595402 0.746179 0.95358  -0.128109   -0.254601   0.180743    77  PHE   B CG   
939  C CD1  . PHE   A 65  ? 0.637492 0.801618 0.946009 -0.121581   -0.28977    0.169099    77  PHE   B CD1  
940  C CD2  . PHE   A 65  ? 0.592463 0.717326 0.924349 -0.11734    -0.22718    0.201225    77  PHE   B CD2  
941  C CE1  . PHE   A 65  ? 0.6383   0.795288 0.87521  -0.102819   -0.291972   0.1828      77  PHE   B CE1  
942  C CE2  . PHE   A 65  ? 0.589393 0.708382 0.859693 -0.103363   -0.233028   0.213891    77  PHE   B CE2  
943  C CZ   . PHE   A 65  ? 0.659417 0.796886 0.883605 -0.0952021  -0.262596   0.207307    77  PHE   B CZ   
944  H H    . PHE   A 65  ? 0.524493 0.741181 1.13421  -0.169839   -0.227061   0.165838    77  PHE   B H    
945  H HA   . PHE   A 65  ? 0.575526 0.828532 1.08081  -0.130242   -0.303162   0.175971    77  PHE   B HA   
946  H HB2  . PHE   A 65  ? 0.600708 0.758601 1.04012  -0.161529   -0.254861   0.15078     77  PHE   B HB2  
947  H HB3  . PHE   A 65  ? 0.574536 0.714172 1.02368  -0.150395   -0.21318    0.175406    77  PHE   B HB3  
948  H HD1  . PHE   A 65  ? 0.649268 0.828404 0.974519 -0.12972    -0.311746   0.15137     77  PHE   B HD1  
949  H HD2  . PHE   A 65  ? 0.576547 0.689097 0.935684 -0.119617   -0.204313   0.206365    77  PHE   B HD2  
950  H HE1  . PHE   A 65  ? 0.673684 0.839793 0.87266  -0.0955348  -0.313199   0.174907    77  PHE   B HE1  
951  H HE2  . PHE   A 65  ? 0.593282 0.69543  0.853541 -0.0992754  -0.215577   0.226664    77  PHE   B HE2  
952  H HZ   . PHE   A 65  ? 0.644831 0.779583 0.827677 -0.0850198  -0.261644   0.21777     77  PHE   B HZ   
953  N N    . VAL   A 66  ? 0.559596 0.814968 1.07844  -0.0897555  -0.273065   0.230694    78  VAL   B N    
954  C CA   . VAL   A 66  ? 0.544937 0.798334 1.08354  -0.0665401  -0.256315   0.26102     78  VAL   B CA   
955  C C    . VAL   A 66  ? 0.571904 0.793849 1.02967  -0.0537441  -0.254787   0.279776    78  VAL   B C    
956  O O    . VAL   A 66  ? 0.599107 0.830218 0.999416 -0.0505517  -0.280367   0.277027    78  VAL   B O    
957  C CB   . VAL   A 66  ? 0.580312 0.896455 1.19021  -0.0459845  -0.285461   0.275242    78  VAL   B CB   
958  C CG1  . VAL   A 66  ? 0.580472 0.886889 1.2137   -0.0180931  -0.265896   0.308177    78  VAL   B CG1  
959  C CG2  . VAL   A 66  ? 0.555706 0.914972 1.25881  -0.0635712  -0.28918    0.254372    78  VAL   B CG2  
960  H H    . VAL   A 66  ? 0.573835 0.847022 1.06765  -0.0861679  -0.302144   0.225608    78  VAL   B H    
961  H HA   . VAL   A 66  ? 0.541763 0.771612 1.10063  -0.0722294  -0.225458   0.259751    78  VAL   B HA   
962  H HB   . VAL   A 66  ? 0.591923 0.929308 1.17165  -0.0377917  -0.317912   0.276757    78  VAL   B HB   
963  H HG11 . VAL   A 66  ? 0.569537 0.847518 1.21926  -0.0242176  -0.232813   0.305017    78  VAL   B HG11 
964  H HG12 . VAL   A 66  ? 0.59559  0.880886 1.17696  -0.00791822 -0.268025   0.323721    78  VAL   B HG12 
965  H HG13 . VAL   A 66  ? 0.593302 0.941847 1.27711  -0.0033334  -0.284028   0.316815    78  VAL   B HG13 
966  H HG21 . VAL   A 66  ? 0.56842  0.97166  1.32372  -0.0485254  -0.307086   0.26437     78  VAL   B HG21 
967  H HG22 . VAL   A 66  ? 0.564552 0.930912 1.25511  -0.080115   -0.308254   0.234166    78  VAL   B HG22 
968  H HG23 . VAL   A 66  ? 0.545052 0.88071  1.26916  -0.0726546  -0.254018   0.251591    78  VAL   B HG23 
969  N N    . PHE   A 67  ? 0.554117 0.734522 1.00599  -0.0491525  -0.221018   0.295228    79  PHE   B N    
970  C CA   . PHE   A 67  ? 0.541326 0.693986 0.9342   -0.0409514  -0.215634   0.3159      79  PHE   B CA   
971  C C    . PHE   A 67  ? 0.571723 0.686791 0.988319 -0.0323693  -0.186056   0.335205    79  PHE   B C    
972  O O    . PHE   A 67  ? 0.533206 0.635054 0.995789 -0.0335888  -0.164977   0.325948    79  PHE   B O    
973  C CB   . PHE   A 67  ? 0.568768 0.694077 0.898771 -0.0589089  -0.207835   0.297688    79  PHE   B CB   
974  C CG   . PHE   A 67  ? 0.510785 0.590459 0.841316 -0.0753404  -0.1749     0.281029    79  PHE   B CG   
975  C CD1  . PHE   A 67  ? 0.489415 0.563398 0.844394 -0.0885446  -0.163854   0.257469    79  PHE   B CD1  
976  C CD2  . PHE   A 67  ? 0.510197 0.55266  0.81693  -0.0770621  -0.155346   0.289992    79  PHE   B CD2  
977  C CE1  . PHE   A 67  ? 0.483539 0.513896 0.825515 -0.0982254  -0.133897   0.244428    79  PHE   B CE1  
978  C CE2  . PHE   A 67  ? 0.51284  0.514705 0.811325 -0.0893319  -0.131466   0.271066    79  PHE   B CE2  
979  C CZ   . PHE   A 67  ? 0.497888 0.492711 0.809509 -0.0967629  -0.120224   0.249914    79  PHE   B CZ   
980  H H    . PHE   A 67  ? 0.542694 0.711684 1.029    -0.0516528  -0.200552   0.292208    79  PHE   B H    
981  H HA   . PHE   A 67  ? 0.577392 0.755105 0.957211 -0.026831   -0.237544   0.33074     79  PHE   B HA   
982  H HB2  . PHE   A 67  ? 0.561755 0.682594 0.858069 -0.0523556  -0.208995   0.31304     79  PHE   B HB2  
983  H HB3  . PHE   A 67  ? 0.550057 0.692501 0.869386 -0.0645959  -0.224304   0.281495    79  PHE   B HB3  
984  H HD1  . PHE   A 67  ? 0.491177 0.591241 0.871176 -0.0907136  -0.17692    0.25078     79  PHE   B HD1  
985  H HD2  . PHE   A 67  ? 0.524836 0.56987  0.819511 -0.0702932  -0.159186   0.308329    79  PHE   B HD2  
986  H HE1  . PHE   A 67  ? 0.484459 0.509486 0.839721 -0.105542   -0.123058   0.232099    79  PHE   B HE1  
987  H HE2  . PHE   A 67  ? 0.514963 0.493597 0.800799 -0.0917165  -0.122326   0.274068    79  PHE   B HE2  
988  H HZ   . PHE   A 67  ? 0.500735 0.466633 0.798176 -0.101985   -0.103922   0.238523    79  PHE   B HZ   
989  N N    . SER   A 68  ? 0.545191 0.641278 0.930516 -0.0228592  -0.182948   0.362517    80  SER   B N    
990  C CA   . SER   A 68  ? 0.602558 0.654557 1.00975  -0.0161426  -0.157573   0.380645    80  SER   B CA   
991  C C    . SER   A 68  ? 0.581661 0.586966 0.955046 -0.0388619  -0.135646   0.365459    80  SER   B C    
992  O O    . SER   A 68  ? 0.57758  0.586108 0.907808 -0.047976   -0.140111   0.369701    80  SER   B O    
993  C CB   . SER   A 68  ? 0.637451 0.692511 1.04471  0.00816206  -0.165387   0.424105    80  SER   B CB   
994  O OG   . SER   A 68  ? 0.705863 0.794451 1.1616   0.0344851   -0.181282   0.437827    80  SER   B OG   
995  H H    . SER   A 68  ? 0.573529 0.682298 0.923626 -0.020732   -0.195572   0.369877    80  SER   B H    
996  H HA   . SER   A 68  ? 0.587952 0.636846 1.03438  -0.0120166  -0.148766   0.372713    80  SER   B HA   
997  H HB2  . SER   A 68  ? 0.657658 0.730112 1.0275   0.00902883  -0.177846   0.433493    80  SER   B HB2  
998  H HB3  . SER   A 68  ? 0.666289 0.682169 1.0772   0.00625097  -0.146638   0.434497    80  SER   B HB3  
1000 N N    . LEU   A 69  ? 0.561764 0.528773 0.954756 -0.0461306  -0.113064   0.344814    81  LEU   B N    
1001 C CA   . LEU   A 69  ? 0.575404 0.503277 0.935927 -0.0667484  -0.0987544  0.322441    81  LEU   B CA   
1002 C C    . LEU   A 69  ? 0.600506 0.500986 0.952001 -0.0726688  -0.0940908  0.342227    81  LEU   B C    
1003 O O    . LEU   A 69  ? 0.604661 0.485085 0.984072 -0.0606848  -0.0877767  0.368104    81  LEU   B O    
1004 C CB   . LEU   A 69  ? 0.638141 0.528798 1.01422  -0.0672102  -0.0763081  0.297172    81  LEU   B CB   
1005 C CG   . LEU   A 69  ? 0.664768 0.516564 0.999343 -0.0851957  -0.0665436  0.26863     81  LEU   B CG   
1006 C CD1  . LEU   A 69  ? 0.634995 0.50964  0.935866 -0.0948033  -0.0729889  0.250125    81  LEU   B CD1  
1007 C CD2  . LEU   A 69  ? 0.735977 0.536472 1.07562  -0.0802547  -0.043363   0.247869    81  LEU   B CD2  
1008 H H    . LEU   A 69  ? 0.576462 0.543107 1.00254  -0.0362066  -0.107047   0.34424     81  LEU   B H    
1009 H HA   . LEU   A 69  ? 0.562021 0.507182 0.895737 -0.0757345  -0.106937   0.31058     81  LEU   B HA   
1010 H HB2  . LEU   A 69  ? 0.617034 0.529324 1.0064   -0.0637083  -0.0762561  0.289445    81  LEU   B HB2  
1011 H HB3  . LEU   A 69  ? 0.654063 0.523959 1.05535  -0.0567132  -0.0674978  0.307165    81  LEU   B HB3  
1012 H HG   . LEU   A 69  ? 0.671529 0.515818 0.994987 -0.0929971  -0.0720736  0.275856    81  LEU   B HG   
1013 H HD11 . LEU   A 69  ? 0.619209 0.521346 0.910938 -0.0970997  -0.0877834  0.259903    81  LEU   B HD11 
1014 H HD12 . LEU   A 69  ? 0.641178 0.492399 0.913697 -0.10272    -0.0683291  0.233564    81  LEU   B HD12 
1015 H HD13 . LEU   A 69  ? 0.630881 0.514944 0.947683 -0.0897836  -0.0666065  0.245178    81  LEU   B HD13 
1016 H HD21 . LEU   A 69  ? 0.748069 0.526989 1.1081   -0.0744079  -0.0393632  0.258124    81  LEU   B HD21 
1017 H HD22 . LEU   A 69  ? 0.720913 0.530644 1.07485  -0.0715675  -0.0336896  0.243077    81  LEU   B HD22 
1018 H HD23 . LEU   A 69  ? 0.729472 0.508595 1.03707  -0.0903583  -0.0417961  0.228877    81  LEU   B HD23 
1019 N N    . GLY   A 70  ? 0.637317 0.541254 0.954064 -0.0902678  -0.0973291  0.333238    82  GLY   B N    
1020 C CA   . GLY   A 70  ? 0.705977 0.591033 1.02426  -0.1022     -0.0908353  0.349599    82  GLY   B CA   
1021 C C    . GLY   A 70  ? 0.799499 0.709833 1.11854  -0.0904941  -0.094029   0.39382     82  GLY   B C    
1022 O O    . GLY   A 70  ? 0.869778 0.760438 1.20279  -0.099072   -0.0823966  0.417046    82  GLY   B O    
1023 H H    . GLY   A 70  ? 0.612959 0.532387 0.908602 -0.0950001  -0.103027   0.317081    82  GLY   B H    
1024 H HA2  . GLY   A 70  ? 0.694631 0.585704 0.99328  -0.114853   -0.0930936  0.335115    82  GLY   B HA2  
1025 H HA3  . GLY   A 70  ? 0.729348 0.576839 1.06808  -0.105269   -0.0808814  0.345828    82  GLY   B HA3  
1026 N N    . LYS   A 71  ? 0.803759 0.754442 1.10995  -0.0702218  -0.109313   0.407069    83  LYS   B N    
1027 C CA   . LYS   A 71  ? 0.740721 0.710945 1.03867  -0.0513864  -0.11321    0.451572    83  LYS   B CA   
1028 C C    . LYS   A 71  ? 0.815614 0.83075  1.06226  -0.0496493  -0.124123   0.453849    83  LYS   B C    
1029 O O    . LYS   A 71  ? 0.808373 0.853104 1.02827  -0.0277708  -0.135963   0.480084    83  LYS   B O    
1030 C CB   . LYS   A 71  ? 0.790224 0.767051 1.11363  -0.0236485  -0.123689   0.470831    83  LYS   B CB   
1031 H H    . LYS   A 71  ? 0.754783 0.720828 1.05563  -0.0680104  -0.118079   0.38822     83  LYS   B H    
1032 H HA   . LYS   A 71  ? 0.802608 0.747234 1.11314  -0.0576058  -0.0986516  0.470056    83  LYS   B HA   
1035 N N    . GLY   A 72  ? 0.827939 0.847086 1.05647  -0.0689454  -0.120773   0.425577    84  GLY   B N    
1036 C CA   . GLY   A 72  ? 0.911216 0.966123 1.09377  -0.0663414  -0.123872   0.427904    84  GLY   B CA   
1037 C C    . GLY   A 72  ? 0.846476 0.934091 0.988152 -0.0522425  -0.148511   0.406899    84  GLY   B C    
1038 O O    . GLY   A 72  ? 0.938981 1.05447  1.03412  -0.0417105  -0.152871   0.411034    84  GLY   B O    
1039 H H    . GLY   A 72  ? 0.816607 0.81521  1.06008  -0.0817567  -0.116173   0.403887    84  GLY   B H    
1040 H HA2  . GLY   A 72  ? 0.860675 0.910464 1.04515  -0.0812321  -0.116386   0.41277     84  GLY   B HA2  
1041 H HA3  . GLY   A 72  ? 0.905445 0.967413 1.08133  -0.0585676  -0.115786   0.459119    84  GLY   B HA3  
1042 N N    . GLN   A 73  ? 0.688885 0.773619 0.849215 -0.0513793  -0.163912   0.384141    85  GLN   B N    
1043 C CA   . GLN   A 73  ? 0.678719 0.793687 0.811995 -0.0405397  -0.190739   0.366135    85  GLN   B CA   
1044 C C    . GLN   A 73  ? 0.623261 0.732445 0.736955 -0.0549777  -0.193947   0.325548    85  GLN   B C    
1045 O O    . GLN   A 73  ? 0.611955 0.739684 0.695429 -0.0488173  -0.214703   0.307508    85  GLN   B O    
1046 C CB   . GLN   A 73  ? 0.646913 0.769143 0.825104 -0.0320543  -0.205212   0.368515    85  GLN   B CB   
1047 C CG   . GLN   A 73  ? 0.719576 0.850005 0.904892 -0.00914691 -0.207459   0.412117    85  GLN   B CG   
1048 C CD   . GLN   A 73  ? 0.705724 0.84312  0.947423 0.00224937  -0.218272   0.416749    85  GLN   B CD   
1049 O OE1  . GLN   A 73  ? 0.712196 0.85781  0.990116 -0.00729767 -0.225463   0.387037    85  GLN   B OE1  
1050 N NE2  . GLN   A 73  ? 0.851961 0.986848 1.10375  0.0245296   -0.216943   0.457206    85  GLN   B NE2  
1051 H H    . GLN   A 73  ? 0.704015 0.767789 0.896164 -0.0582431  -0.15725    0.378449    85  GLN   B H    
1052 H HA   . GLN   A 73  ? 0.697831 0.832343 0.797387 -0.026935   -0.197332   0.381376    85  GLN   B HA   
1053 H HB2  . GLN   A 73  ? 0.642373 0.743512 0.85381  -0.042753   -0.193249   0.358257    85  GLN   B HB2  
1054 H HB3  . GLN   A 73  ? 0.661985 0.804589 0.83308  -0.0295464  -0.224995   0.351604    85  GLN   B HB3  
1055 H HG2  . GLN   A 73  ? 0.734371 0.888028 0.881897 0.00464135  -0.221466   0.421756    85  GLN   B HG2  
1056 H HG3  . GLN   A 73  ? 0.715091 0.82283  0.904772 -0.0133511  -0.187032   0.429965    85  GLN   B HG3  
1057 H HE21 . GLN   A 73  ? 0.820627 0.960634 1.10747  0.0349472   -0.222811   0.462803    85  GLN   B HE21 
1058 H HE22 . GLN   A 73  ? 0.838694 0.966491 1.0634   0.0300559   -0.208958   0.480262    85  GLN   B HE22 
1059 N N    . VAL   A 74  ? 0.521322 0.601533 0.647831 -0.0723212  -0.17524    0.310866    86  VAL   B N    
1060 C CA   . VAL   A 74  ? 0.508526 0.575102 0.617804 -0.0829467  -0.176078   0.276845    86  VAL   B CA   
1061 C C    . VAL   A 74  ? 0.490211 0.544993 0.583359 -0.0902376  -0.160555   0.274509    86  VAL   B C    
1062 O O    . VAL   A 74  ? 0.505162 0.561753 0.613219 -0.0924138  -0.149053   0.296121    86  VAL   B O    
1063 C CB   . VAL   A 74  ? 0.485896 0.528866 0.631568 -0.0937228  -0.170659   0.258819    86  VAL   B CB   
1064 C CG1  . VAL   A 74  ? 0.494849 0.560886 0.668066 -0.0887719  -0.188849   0.256221    86  VAL   B CG1  
1065 C CG2  . VAL   A 74  ? 0.473255 0.490752 0.653244 -0.0982812  -0.151497   0.26976     86  VAL   B CG2  
1066 H H    . VAL   A 74  ? 0.539376 0.605692 0.684297 -0.0768109  -0.162214   0.322777    86  VAL   B H    
1067 H HA   . VAL   A 74  ? 0.514614 0.595142 0.598685 -0.0770619  -0.189275   0.26785     86  VAL   B HA   
1068 H HB   . VAL   A 74  ? 0.480026 0.508479 0.608847 -0.100244   -0.167236   0.240465    86  VAL   B HB   
1069 H HG11 . VAL   A 74  ? 0.504158 0.585816 0.690884 -0.0789274  -0.194427   0.275505    86  VAL   B HG11 
1070 H HG12 . VAL   A 74  ? 0.501828 0.579106 0.652289 -0.0877075  -0.202964   0.244605    86  VAL   B HG12 
1071 H HG13 . VAL   A 74  ? 0.485396 0.539611 0.686545 -0.0957451  -0.180884   0.246809    86  VAL   B HG13 
1072 H HG21 . VAL   A 74  ? 0.47173  0.474304 0.668975 -0.102423   -0.144837   0.257812    86  VAL   B HG21 
1073 H HG22 . VAL   A 74  ? 0.475258 0.480802 0.642095 -0.103566   -0.143786   0.268559    86  VAL   B HG22 
1074 H HG23 . VAL   A 74  ? 0.487555 0.514535 0.685283 -0.0907954  -0.153507   0.289465    86  VAL   B HG23 
1075 N N    . ILE   A 75  ? 0.498543 0.541909 0.566074 -0.0938552  -0.161239   0.249272    87  ILE   B N    
1076 C CA   . ILE   A 75  ? 0.514784 0.55252  0.572199 -0.0984299  -0.151301   0.244153    87  ILE   B CA   
1077 C C    . ILE   A 75  ? 0.436737 0.447875 0.52609  -0.111909   -0.140789   0.242737    87  ILE   B C    
1078 O O    . ILE   A 75  ? 0.436909 0.42469  0.546055 -0.115836   -0.137328   0.238006    87  ILE   B O    
1079 C CB   . ILE   A 75  ? 0.485366 0.513633 0.504613 -0.0935263  -0.15589    0.219535    87  ILE   B CB   
1080 C CG1  . ILE   A 75  ? 0.538964 0.531905 0.559188 -0.100447   -0.156182   0.199566    87  ILE   B CG1  
1081 C CG2  . ILE   A 75  ? 0.553347 0.606221 0.535935 -0.0775717  -0.164738   0.219314    87  ILE   B CG2  
1082 C CD1  . ILE   A 75  ? 0.537403 0.506996 0.520123 -0.0959709  -0.156173   0.179196    87  ILE   B CD1  
1083 H H    . ILE   A 75  ? 0.501684 0.541172 0.55952  -0.0930268  -0.168975   0.235171    87  ILE   B H    
1084 H HA   . ILE   A 75  ? 0.496288 0.555735 0.550746 -0.0938265  -0.148688   0.259426    87  ILE   B HA   
1085 H HB   . ILE   A 75  ? 0.505696 0.53269  0.523181 -0.0951467  -0.151155   0.216811    87  ILE   B HB   
1086 H HG12 . ILE   A 75  ? 0.52617  0.524991 0.553803 -0.100011   -0.163019   0.19988     87  ILE   B HG12 
1087 H HG13 . ILE   A 75  ? 0.51691  0.495256 0.556848 -0.10751    -0.148461   0.200822    87  ILE   B HG13 
1088 H HG21 . ILE   A 75  ? 0.543629 0.585958 0.502654 -0.073043   -0.166279   0.203709    87  ILE   B HG21 
1089 H HG22 . ILE   A 75  ? 0.545608 0.60087  0.527577 -0.0757721  -0.17374    0.218966    87  ILE   B HG22 
1090 H HG23 . ILE   A 75  ? 0.541124 0.61724  0.523668 -0.0723917  -0.159609   0.234877    87  ILE   B HG23 
1091 H HD11 . ILE   A 75  ? 0.539765 0.50949  0.514601 -0.0936499  -0.152835   0.178966    87  ILE   B HD11 
1092 H HD12 . ILE   A 75  ? 0.54532  0.49014  0.531343 -0.10171    -0.151684   0.17091     87  ILE   B HD12 
1093 H HD13 . ILE   A 75  ? 0.551896 0.529867 0.514801 -0.0884361  -0.163633   0.174801    87  ILE   B HD13 
1094 N N    . LYS   A 76  ? 0.499811 0.518986 0.599148 -0.118233   -0.135614   0.248127    88  LYS   B N    
1095 C CA   . LYS   A 76  ? 0.507192 0.500352 0.633519 -0.132295   -0.130602   0.241233    88  LYS   B CA   
1096 C C    . LYS   A 76  ? 0.485689 0.440197 0.593543 -0.132835   -0.130602   0.214392    88  LYS   B C    
1097 O O    . LYS   A 76  ? 0.486385 0.410219 0.612423 -0.137731   -0.123557   0.210276    88  LYS   B O    
1098 C CB   . LYS   A 76  ? 0.551025 0.56715  0.69054  -0.140274   -0.131586   0.242248    88  LYS   B CB   
1099 H H    . LYS   A 76  ? 0.485828 0.528782 0.576068 -0.113567   -0.135785   0.254987    88  LYS   B H    
1100 H HA   . LYS   A 76  ? 0.515397 0.501616 0.666987 -0.135613   -0.125558   0.255446    88  LYS   B HA   
1103 N N    . ALA   A 77  ? 0.505913 0.45777  0.574689 -0.124964   -0.135132   0.198076    89  ALA   B N    
1104 C CA   . ALA   A 77  ? 0.533503 0.446643 0.576986 -0.123327   -0.130197   0.177817    89  ALA   B CA   
1105 C C    . ALA   A 77  ? 0.579131 0.473302 0.641453 -0.124457   -0.118452   0.180207    89  ALA   B C    
1106 O O    . ALA   A 77  ? 0.545711 0.405495 0.599221 -0.124283   -0.106371   0.168062    89  ALA   B O    
1107 C CB   . ALA   A 77  ? 0.517342 0.426471 0.518475 -0.113352   -0.134095   0.167147    89  ALA   B CB   
1108 H H    . ALA   A 77  ? 0.498624 0.470946 0.554282 -0.119117   -0.139542   0.200953    89  ALA   B H    
1109 H HA   . ALA   A 77  ? 0.546011 0.445585 0.588655 -0.127019   -0.130762   0.169398    89  ALA   B HA   
1110 H HB1  . ALA   A 77  ? 0.524034 0.447495 0.515691 -0.109767   -0.14127    0.165285    89  ALA   B HB1  
1111 H HB2  . ALA   A 77  ? 0.516841 0.436377 0.518182 -0.110825   -0.135406   0.171867    89  ALA   B HB2  
1112 H HB3  . ALA   A 77  ? 0.539285 0.419883 0.521788 -0.111778   -0.127833   0.157419    89  ALA   B HB3  
1113 N N    . TRP   A 78  ? 0.514566 0.43407  0.600381 -0.122785   -0.122172   0.195126    90  TRP   B N    
1114 C CA   . TRP   A 78  ? 0.507026 0.419801 0.623919 -0.122668   -0.113598   0.198119    90  TRP   B CA   
1115 C C    . TRP   A 78  ? 0.472078 0.372626 0.62299  -0.123023   -0.104712   0.207384    90  TRP   B C    
1116 O O    . TRP   A 78  ? 0.556167 0.434442 0.723661 -0.120729   -0.0894654  0.201323    90  TRP   B O    
1117 C CB   . TRP   A 78  ? 0.465465 0.411908 0.597828 -0.119309   -0.127024   0.207168    90  TRP   B CB   
1118 C CG   . TRP   A 78  ? 0.512994 0.452757 0.631471 -0.122528   -0.128471   0.19128     90  TRP   B CG   
1119 C CD1  . TRP   A 78  ? 0.527562 0.446702 0.602449 -0.122788   -0.127658   0.176965    90  TRP   B CD1  
1120 C CD2  . TRP   A 78  ? 0.487405 0.438547 0.643418 -0.126983   -0.130049   0.188542    90  TRP   B CD2  
1121 N NE1  . TRP   A 78  ? 0.497887 0.408198 0.578324 -0.128606   -0.127223   0.166821    90  TRP   B NE1  
1122 C CE2  . TRP   A 78  ? 0.51349  0.44595  0.647297 -0.133681   -0.129061   0.17236     90  TRP   B CE2  
1123 C CE3  . TRP   A 78  ? 0.501519 0.478576 0.712938 -0.125418   -0.133032   0.1987      90  TRP   B CE3  
1124 C CZ2  . TRP   A 78  ? 0.488271 0.426943 0.659155 -0.144207   -0.130324   0.164845    90  TRP   B CZ2  
1125 C CZ3  . TRP   A 78  ? 0.489493 0.482095 0.739397 -0.133158   -0.13715    0.190728    90  TRP   B CZ3  
1126 C CH2  . TRP   A 78  ? 0.492498 0.465455 0.72541  -0.14517    -0.134806   0.173343    90  TRP   B CH2  
1127 H H    . TRP   A 78  ? 0.515954 0.458581 0.598174 -0.1202     -0.130314   0.202856    90  TRP   B H    
1128 H HA   . TRP   A 78  ? 0.503739 0.395453 0.608777 -0.123409   -0.104269   0.186367    90  TRP   B HA   
1129 H HB2  . TRP   A 78  ? 0.47953  0.444993 0.600132 -0.116034   -0.136963   0.215005    90  TRP   B HB2  
1130 H HB3  . TRP   A 78  ? 0.48121  0.434979 0.645946 -0.117424   -0.12539    0.216183    90  TRP   B HB3  
1131 H HD1  . TRP   A 78  ? 0.518097 0.431759 0.566537 -0.119251   -0.128556   0.174971    90  TRP   B HD1  
1132 H HE1  . TRP   A 78  ? 0.524915 0.417575 0.581773 -0.129021   -0.125716   0.158507    90  TRP   B HE1  
1133 H HE3  . TRP   A 78  ? 0.489974 0.474895 0.715891 -0.119054   -0.132987   0.211279    90  TRP   B HE3  
1134 H HZ2  . TRP   A 78  ? 0.513644 0.433803 0.671399 -0.150385   -0.127981   0.154827    90  TRP   B HZ2  
1135 H HZ3  . TRP   A 78  ? 0.487317 0.503316 0.780279 -0.130714   -0.140818   0.197557    90  TRP   B HZ3  
1136 H HH2  . TRP   A 78  ? 0.496759 0.480858 0.764136 -0.153652   -0.137486   0.167886    90  TRP   B HH2  
1137 N N    . ASP   A 79  ? 0.45951  0.372681 0.6233   -0.124792   -0.110973   0.223669    91  ASP   B N    
1138 C CA   . ASP   A 79  ? 0.520441 0.411751 0.717809 -0.125833   -0.101994   0.232949    91  ASP   B CA   
1139 C C    . ASP   A 79  ? 0.592046 0.439161 0.774969 -0.131018   -0.0924213  0.207484    91  ASP   B C    
1140 O O    . ASP   A 79  ? 0.573965 0.390118 0.775016 -0.126373   -0.079165   0.202887    91  ASP   B O    
1141 C CB   . ASP   A 79  ? 0.550256 0.457264 0.76511  -0.129663   -0.106533   0.258141    91  ASP   B CB   
1142 C CG   . ASP   A 79  ? 0.585913 0.524831 0.81521  -0.117546   -0.11209    0.289349    91  ASP   B CG   
1143 O OD1  . ASP   A 79  ? 0.533177 0.476883 0.778018 -0.1068     -0.113733   0.291372    91  ASP   B OD1  
1144 O OD2  . ASP   A 79  ? 0.562742 0.523127 0.78903  -0.11776    -0.113954   0.312698    91  ASP   B OD2  
1145 H H    . ASP   A 79  ? 0.466083 0.399469 0.618447 -0.124906   -0.118934   0.229733    91  ASP   B H    
1146 H HA   . ASP   A 79  ? 0.525382 0.418556 0.744368 -0.118788   -0.0980399  0.239942    91  ASP   B HA   
1147 H HB2  . ASP   A 79  ? 0.545132 0.465418 0.742926 -0.134987   -0.111673   0.254585    91  ASP   B HB2  
1148 H HB3  . ASP   A 79  ? 0.570541 0.452195 0.80397  -0.134364   -0.100048   0.258506    91  ASP   B HB3  
1149 N N    . ILE   A 80  ? 0.584787 0.429884 0.731045 -0.136798   -0.100301   0.189896    92  ILE   B N    
1150 C CA   . ILE   A 80  ? 0.624611 0.430224 0.74356  -0.138522   -0.097488   0.16277     92  ILE   B CA   
1151 C C    . ILE   A 80  ? 0.589794 0.370246 0.681632 -0.127129   -0.0801544  0.150272    92  ILE   B C    
1152 O O    . ILE   A 80  ? 0.621067 0.364188 0.708801 -0.121756   -0.0656122  0.137328    92  ILE   B O    
1153 C CB   . ILE   A 80  ? 0.625598 0.44499  0.714395 -0.143447   -0.114948   0.150007    92  ILE   B CB   
1154 C CG1  . ILE   A 80  ? 0.655365 0.499738 0.781003 -0.15728    -0.126552   0.160738    92  ILE   B CG1  
1155 C CG2  . ILE   A 80  ? 0.659237 0.43965  0.700975 -0.138505   -0.116416   0.119776    92  ILE   B CG2  
1156 C CD1  . ILE   A 80  ? 0.65016  0.531009 0.761183 -0.158404   -0.142557   0.156347    92  ILE   B CD1  
1157 H H    . ILE   A 80  ? 0.572215 0.441607 0.708256 -0.137453   -0.10862    0.194604    92  ILE   B H    
1158 H HA   . ILE   A 80  ? 0.6321   0.418306 0.770716 -0.142503   -0.0950059  0.161118    92  ILE   B HA   
1159 H HB   . ILE   A 80  ? 0.612597 0.451685 0.686181 -0.138408   -0.117113   0.155156    92  ILE   B HB   
1160 H HG12 . ILE   A 80  ? 0.672585 0.493234 0.810991 -0.164733   -0.127585   0.150682    92  ILE   B HG12 
1161 H HG13 . ILE   A 80  ? 0.632542 0.493514 0.783158 -0.15768    -0.121773   0.1819      92  ILE   B HG13 
1162 H HG21 . ILE   A 80  ? 0.66552  0.457808 0.695606 -0.141216   -0.131337   0.11184     92  ILE   B HG21 
1163 H HG22 . ILE   A 80  ? 0.686365 0.440013 0.736903 -0.140815   -0.111833   0.111042    92  ILE   B HG22 
1164 H HG23 . ILE   A 80  ? 0.665334 0.435285 0.679024 -0.129022   -0.106907   0.117309    92  ILE   B HG23 
1165 H HD11 . ILE   A 80  ? 0.629403 0.527889 0.723856 -0.149507   -0.141069   0.163886    92  ILE   B HD11 
1166 H HD12 . ILE   A 80  ? 0.643933 0.54567  0.787466 -0.168446   -0.14613    0.166415    92  ILE   B HD12 
1167 H HD13 . ILE   A 80  ? 0.666827 0.532838 0.753403 -0.156711   -0.150448   0.136199    92  ILE   B HD13 
1168 N N    . GLY   A 81  ? 0.553604 0.352149 0.629494 -0.123221   -0.0785333  0.154779    93  GLY   B N    
1169 C CA   . GLY   A 81  ? 0.57918  0.35199  0.627806 -0.115631   -0.0586187  0.14492     93  GLY   B CA   
1170 C C    . GLY   A 81  ? 0.630227 0.399975 0.720989 -0.110864   -0.0359815  0.152061    93  GLY   B C    
1171 O O    . GLY   A 81  ? 0.619714 0.358706 0.694129 -0.102535   -0.0110055  0.142448    93  GLY   B O    
1172 H H    . GLY   A 81  ? 0.537384 0.3623   0.619224 -0.125387   -0.0884975  0.16425     93  GLY   B H    
1173 H HA2  . GLY   A 81  ? 0.617945 0.364021 0.632071 -0.111924   -0.0559532  0.130827    93  GLY   B HA2  
1174 H HA3  . GLY   A 81  ? 0.577727 0.361156 0.612863 -0.115951   -0.0616313  0.147476    93  GLY   B HA3  
1175 N N    . VAL   A 82  ? 0.584949 0.391699 0.729235 -0.113178   -0.0440538  0.17054     94  VAL   B N    
1176 C CA   . VAL   A 82  ? 0.557056 0.373792 0.751566 -0.106639   -0.0267693  0.178761    94  VAL   B CA   
1177 C C    . VAL   A 82  ? 0.604108 0.390272 0.813553 -0.0965225  -0.0121495  0.175451    94  VAL   B C    
1178 O O    . VAL   A 82  ? 0.593609 0.371022 0.826857 -0.0855655  0.0136924   0.173688    94  VAL   B O    
1179 C CB   . VAL   A 82  ? 0.597825 0.465603 0.840315 -0.108528   -0.0462449  0.197596    94  VAL   B CB   
1180 C CG1  . VAL   A 82  ? 0.596494 0.485289 0.904701 -0.0992227  -0.0335261  0.20739     94  VAL   B CG1  
1181 C CG2  . VAL   A 82  ? 0.566612 0.453771 0.790324 -0.118002   -0.0591066  0.193292    94  VAL   B CG2  
1182 H H    . VAL   A 82  ? 0.562579 0.390278 0.711282 -0.117088   -0.0604668  0.178294    94  VAL   B H    
1183 H HA   . VAL   A 82  ? 0.588668 0.397125 0.774559 -0.106049   -0.0112492  0.172985    94  VAL   B HA   
1184 H HB   . VAL   A 82  ? 0.573185 0.447811 0.816104 -0.108169   -0.0599661  0.206179    94  VAL   B HB   
1185 H HG11 . VAL   A 82  ? 0.609118 0.487196 0.919844 -0.098962   -0.0133507  0.199676    94  VAL   B HG11 
1186 H HG12 . VAL   A 82  ? 0.607623 0.486213 0.930527 -0.0907946  -0.0296628  0.213086    94  VAL   B HG12 
1187 H HG13 . VAL   A 82  ? 0.579896 0.503403 0.91373  -0.100846   -0.0493135  0.215791    94  VAL   B HG13 
1188 H HG21 . VAL   A 82  ? 0.557142 0.475426 0.807529 -0.118309   -0.0737098  0.201588    94  VAL   B HG21 
1189 H HG22 . VAL   A 82  ? 0.569963 0.448457 0.755953 -0.120547   -0.0680021  0.188866    94  VAL   B HG22 
1190 H HG23 . VAL   A 82  ? 0.581438 0.457265 0.804318 -0.120223   -0.0435574  0.186513    94  VAL   B HG23 
1191 N N    . ALA   A 83  ? 0.606194 0.373324 0.804018 -0.100209   -0.0255522  0.172988    95  ALA   B N    
1192 C CA   . ALA   A 83  ? 0.652102 0.376093 0.858233 -0.0921746  -0.0125634  0.163663    95  ALA   B CA   
1193 C C    . ALA   A 83  ? 0.709435 0.388564 0.867906 -0.082934   0.0101635   0.136222    95  ALA   B C    
1194 O O    . ALA   A 83  ? 0.797408 0.439538 0.96151  -0.0697937  0.0290179   0.125455    95  ALA   B O    
1195 C CB   . ALA   A 83  ? 0.666102 0.371732 0.871357 -0.103481   -0.0307021  0.162415    95  ALA   B CB   
1196 H H    . ALA   A 83  ? 0.593432 0.373803 0.780848 -0.108124   -0.042104   0.176701    95  ALA   B H    
1197 H HA   . ALA   A 83  ? 0.651404 0.384979 0.898212 -0.0830782  -0.00430713 0.176351    95  ALA   B HA   
1198 H HB1  . ALA   A 83  ? 0.64214  0.37482  0.872594 -0.107588   -0.0415319  0.182655    95  ALA   B HB1  
1199 H HB2  . ALA   A 83  ? 0.670181 0.369461 0.840984 -0.111446   -0.0399928  0.148309    95  ALA   B HB2  
1200 H HB3  . ALA   A 83  ? 0.69896  0.371781 0.914105 -0.0982182  -0.0218548  0.155658    95  ALA   B HB3  
1201 N N    . THR   A 84  ? 0.766946 0.444585 0.872496 -0.0861183  0.0099256   0.125343    96  THR   B N    
1202 C CA   . THR   A 84  ? 0.843484 0.476917 0.890146 -0.0732318  0.0329144   0.102892    96  THR   B CA   
1203 C C    . THR   A 84  ? 0.850357 0.491096 0.913587 -0.0613592  0.0704318   0.112505    96  THR   B C    
1204 O O    . THR   A 84  ? 0.87135  0.475938 0.886597 -0.0467732  0.0985664   0.098996    96  THR   B O    
1205 C CB   . THR   A 84  ? 0.856869 0.478947 0.831727 -0.0772927  0.0160179   0.0889122   96  THR   B CB   
1206 O OG1  . THR   A 84  ? 0.824615 0.47482  0.79718  -0.081293   0.0189803   0.105089    96  THR   B OG1  
1207 C CG2  . THR   A 84  ? 0.856468 0.487431 0.831112 -0.0916588  -0.0215522  0.0817597   96  THR   B CG2  
1208 H H    . THR   A 84  ? 0.727152 0.428815 0.828644 -0.0942493  -0.00402482 0.132401    96  THR   B H    
1209 H HA   . THR   A 84  ? 0.873399 0.476744 0.914925 -0.0674845  0.0360575   0.0897142   96  THR   B HA   
1210 H HB   . THR   A 84  ? 0.909302 0.497123 0.837954 -0.0660884  0.0287417   0.0728358   96  THR   B HB   
1212 H HG21 . THR   A 84  ? 0.86869  0.492451 0.798193 -0.0904576  -0.0320864  0.0706767   96  THR   B HG21 
1213 H HG22 . THR   A 84  ? 0.807222 0.471869 0.817279 -0.100639   -0.0321554  0.0986706   96  THR   B HG22 
1214 H HG23 . THR   A 84  ? 0.875056 0.485392 0.860467 -0.092344   -0.0239197  0.071591    96  THR   B HG23 
1215 N N    . MET   A 85  ? 0.800622 0.489162 0.931538 -0.0667327  0.0723459   0.135261    97  MET   B N    
1216 C CA   . MET   A 85  ? 0.811939 0.514217 0.963909 -0.0622385  0.105892    0.143767    97  MET   B CA   
1217 C C    . MET   A 85  ? 0.823381 0.532027 1.03424  -0.0448611  0.136866    0.148524    97  MET   B C    
1218 O O    . MET   A 85  ? 0.740925 0.45568  0.994023 -0.0377588  0.125638    0.152393    97  MET   B O    
1219 C CB   . MET   A 85  ? 0.732835 0.483878 0.925132 -0.0799397  0.088876    0.160153    97  MET   B CB   
1220 C CG   . MET   A 85  ? 0.739851 0.480063 0.871633 -0.091373   0.0659957   0.155019    97  MET   B CG   
1221 S SD   . MET   A 85  ? 0.717109 0.50403  0.889897 -0.110114   0.0442968   0.167648    97  MET   B SD   
1222 C CE   . MET   A 85  ? 0.749743 0.535613 0.955918 -0.114122   0.0872196   0.174212    97  MET   B CE   
1223 H H    . MET   A 85  ? 0.768742 0.481984 0.933551 -0.0732408  0.0532248   0.145496    97  MET   B H    
1224 H HA   . MET   A 85  ? 0.840021 0.512825 0.938325 -0.0576319  0.121229    0.134692    97  MET   B HA   
1225 H HB2  . MET   A 85  ? 0.711711 0.491951 0.948005 -0.0826164  0.0705266   0.168682    97  MET   B HB2  
1226 H HB3  . MET   A 85  ? 0.749253 0.51074  0.966938 -0.0798755  0.111616    0.165828    97  MET   B HB3  
1227 H HG2  . MET   A 85  ? 0.774663 0.485413 0.86055  -0.0865841  0.083272    0.148842    97  MET   B HG2  
1228 H HG3  . MET   A 85  ? 0.734068 0.468472 0.84636  -0.0918842  0.0452061   0.149726    97  MET   B HG3  
1229 H HE1  . MET   A 85  ? 0.72904  0.537235 0.964364 -0.12671    0.0763278   0.178127    97  MET   B HE1  
1230 H HE2  . MET   A 85  ? 0.751329 0.549662 0.998991 -0.107594   0.104077    0.177856    97  MET   B HE2  
1231 H HE3  . MET   A 85  ? 0.782099 0.532655 0.937315 -0.109722   0.10534     0.170752    97  MET   B HE3  
1232 N N    . LYS   A 86  ? 0.823758 0.530892 1.03974  -0.0361611  0.179576    0.151076    98  LYS   B N    
1233 C CA   . LYS   A 86  ? 0.836636 0.560148 1.11854  -0.0169864  0.215133    0.157516    98  LYS   B CA   
1234 C C    . LYS   A 86  ? 0.797065 0.590644 1.17551  -0.0298665  0.217801    0.179449    98  LYS   B C    
1235 O O    . LYS   A 86  ? 0.737016 0.548692 1.11186  -0.0528073  0.201514    0.184953    98  LYS   B O    
1236 C CB   . LYS   A 86  ? 0.903701 0.577467 1.12452  0.00516558  0.26556     0.143934    98  LYS   B CB   
1237 H H    . LYS   A 86  ? 0.8422   0.53874  1.02221  -0.0411891  0.188582    0.150457    98  LYS   B H    
1238 H HA   . LYS   A 86  ? 0.833196 0.554139 1.13579  -0.00899484 0.202257    0.155812    98  LYS   B HA   
1241 N N    . LYS   A 87  ? 0.784077 0.617173 1.25167  -0.0145372  0.23384     0.189983    99  LYS   B N    
1242 C CA   . LYS   A 87  ? 0.732402 0.64172  1.30745  -0.0253319  0.231834    0.208003    99  LYS   B CA   
1243 C C    . LYS   A 87  ? 0.778322 0.690453 1.35266  -0.0412357  0.268412    0.211436    99  LYS   B C    
1244 O O    . LYS   A 87  ? 0.887225 0.759683 1.41681  -0.0267534  0.317953    0.207609    99  LYS   B O    
1245 C CB   . LYS   A 87  ? 0.706914 0.66003  1.37994  0.0001824   0.248624    0.218705    99  LYS   B CB   
1246 H H    . LYS   A 87  ? 0.809407 0.621287 1.27237  0.0041464   0.245041    0.184513    99  LYS   B H    
1247 H HA   . LYS   A 87  ? 0.696052 0.627804 1.28131  -0.0397208  0.193117    0.211565    99  LYS   B HA   
1250 N N    . GLY   A 88  ? 0.729436 0.679454 1.34189  -0.070616   0.243768    0.217882    100 GLY   B N    
1251 C CA   . GLY   A 88  ? 0.791995 0.739768 1.41253  -0.0897787  0.278255    0.224089    100 GLY   B CA   
1252 C C    . GLY   A 88  ? 0.810382 0.685466 1.3091   -0.0956438  0.284598    0.217162    100 GLY   B C    
1253 O O    . GLY   A 88  ? 0.828453 0.688499 1.32096  -0.109306   0.316701    0.225936    100 GLY   B O    
1254 H H    . GLY   A 88  ? 0.705564 0.680195 1.33783  -0.0785943  0.205497    0.218443    100 GLY   B H    
1255 H HA2  . GLY   A 88  ? 0.749489 0.738153 1.42941  -0.109634   0.257405    0.227992    100 GLY   B HA2  
1256 H HA3  . GLY   A 88  ? 0.806711 0.762439 1.46009  -0.0786431  0.320239    0.230387    100 GLY   B HA3  
1257 N N    . GLU   A 89  ? 0.817146 0.649378 1.22543  -0.0856546  0.25378     0.203449    101 GLU   B N    
1258 C CA   . GLU   A 89  ? 0.839578 0.612664 1.13835  -0.088727   0.2506      0.196498    101 GLU   B CA   
1259 C C    . GLU   A 89  ? 0.790891 0.577451 1.09698  -0.115875   0.215425    0.19908     101 GLU   B C    
1260 O O    . GLU   A 89  ? 0.668918 0.500481 1.0301   -0.127837   0.174492    0.197848    101 GLU   B O    
1261 C CB   . GLU   A 89  ? 0.849208 0.582218 1.06563  -0.0717622  0.226223    0.179124    101 GLU   B CB   
1262 C CG   . GLU   A 89  ? 0.887155 0.562911 0.989129 -0.0679614  0.222139    0.169876    101 GLU   B CG   
1263 C CD   . GLU   A 89  ? 0.896472 0.54399  0.938257 -0.0555195  0.192441    0.149493    101 GLU   B CD   
1264 O OE1  . GLU   A 89  ? 0.937665 0.57145  0.9825   -0.0386216  0.205506    0.139059    101 GLU   B OE1  
1265 O OE2  . GLU   A 89  ? 0.865769 0.506975 0.865256 -0.0638938  0.154753    0.143454    101 GLU   B OE2  
1266 H H    . GLU   A 89  ? 0.795455 0.636629 1.21366  -0.0766612  0.234241    0.199287    101 GLU   B H    
1267 H HA   . GLU   A 89  ? 0.883765 0.632257 1.15719  -0.0826358  0.289702    0.20135     101 GLU   B HA   
1268 H HB2  . GLU   A 89  ? 0.873726 0.596898 1.09135  -0.0548341  0.246719    0.174926    101 GLU   B HB2  
1269 H HB3  . GLU   A 89  ? 0.806796 0.562249 1.04628  -0.0785246  0.190742    0.177435    101 GLU   B HB3  
1270 H HG2  . GLU   A 89  ? 0.866021 0.548681 0.965606 -0.0822883  0.202829    0.173934    101 GLU   B HG2  
1271 H HG3  . GLU   A 89  ? 0.937331 0.586893 1.00669  -0.0583632  0.257929    0.173052    101 GLU   B HG3  
1272 N N    . ILE   A 90  ? 0.825668 0.570252 1.07457  -0.122818   0.233993    0.20351     102 ILE   B N    
1273 C CA   . ILE   A 90  ? 0.825602 0.558967 1.04538  -0.139903   0.198999    0.200506    102 ILE   B CA   
1274 C C    . ILE   A 90  ? 0.837418 0.515824 0.939077 -0.12268    0.188091    0.192225    102 ILE   B C    
1275 O O    . ILE   A 90  ? 0.868786 0.500276 0.901956 -0.10665    0.222796    0.196277    102 ILE   B O    
1276 C CB   . ILE   A 90  ? 0.833593 0.560209 1.08977  -0.16294    0.221656    0.21251     102 ILE   B CB   
1277 C CG1  . ILE   A 90  ? 0.845215 0.635434 1.23191  -0.182482   0.229956    0.218381    102 ILE   B CG1  
1278 C CG2  . ILE   A 90  ? 0.782    0.487516 1.00154  -0.176396   0.184561    0.205712    102 ILE   B CG2  
1279 C CD1  . ILE   A 90  ? 0.844549 0.627343 1.28295  -0.20946    0.260916    0.23078     102 ILE   B CD1  
1280 H H    . ILE   A 90  ? 0.874212 0.594148 1.0993   -0.114438   0.271111    0.2094      102 ILE   B H    
1281 H HA   . ILE   A 90  ? 0.77134  0.53751  1.02504  -0.146662   0.164742    0.195049    102 ILE   B HA   
1282 H HB   . ILE   A 90  ? 0.882874 0.574116 1.10065  -0.154832   0.258803    0.221535    102 ILE   B HB   
1283 H HG12 . ILE   A 90  ? 0.78574  0.610382 1.20612  -0.189505   0.190967    0.209848    102 ILE   B HG12 
1284 H HG13 . ILE   A 90  ? 0.832277 0.637324 1.24168  -0.169751   0.253146    0.222425    102 ILE   B HG13 
1285 H HG21 . ILE   A 90  ? 0.816196 0.512365 1.06272  -0.192317   0.199492    0.212327    102 ILE   B HG21 
1286 H HG22 . ILE   A 90  ? 0.752366 0.4905   0.999081 -0.181678   0.14843     0.196417    102 ILE   B HG22 
1287 H HG23 . ILE   A 90  ? 0.81596  0.484014 0.957832 -0.162445   0.182464    0.203964    102 ILE   B HG23 
1288 H HD11 . ILE   A 90  ? 0.901539 0.647897 1.30204  -0.201202   0.302676    0.242735    102 ILE   B HD11 
1289 H HD12 . ILE   A 90  ? 0.835962 0.666711 1.36517  -0.221817   0.263934    0.232906    102 ILE   B HD12 
1290 H HD13 . ILE   A 90  ? 0.85241  0.618529 1.27301  -0.22229    0.236665    0.224935    102 ILE   B HD13 
1291 N N    . ALA   A 91  ? 0.777362 0.465892 0.858127 -0.125607   0.13965     0.18181     103 ALA   B N    
1292 C CA   . ALA   A 91  ? 0.803298 0.45604  0.790588 -0.111243   0.11988     0.172576    103 ALA   B CA   
1293 C C    . ALA   A 91  ? 0.797629 0.449946 0.769081 -0.120796   0.0892099   0.17151     103 ALA   B C    
1294 O O    . ALA   A 91  ? 0.779067 0.46571  0.810788 -0.137967   0.0705736   0.171543    103 ALA   B O    
1295 C CB   . ALA   A 91  ? 0.790242 0.458953 0.773294 -0.101975   0.0944491   0.160066    103 ALA   B CB   
1296 H H    . ALA   A 91  ? 0.746268 0.468696 0.875059 -0.1362     0.117776    0.180679    103 ALA   B H    
1297 H HA   . ALA   A 91  ? 0.854618 0.470909 0.791626 -0.100094   0.144798    0.175415    103 ALA   B HA   
1298 H HB1  . ALA   A 91  ? 0.804491 0.466969 0.794085 -0.0939639  0.114839    0.158728    103 ALA   B HB1  
1299 H HB2  . ALA   A 91  ? 0.743869 0.446511 0.772401 -0.110928   0.072932    0.160793    103 ALA   B HB2  
1300 H HB3  . ALA   A 91  ? 0.799004 0.449384 0.728042 -0.0944409  0.0795564   0.152793    103 ALA   B HB3  
1301 N N    . HIS   A 92  ? 0.798956 0.410815 0.686009 -0.106195   0.0844561   0.169378    104 HIS   B N    
1302 C CA   . HIS   A 92  ? 0.77973  0.386514 0.634432 -0.104705   0.053879    0.165677    104 HIS   B CA   
1303 C C    . HIS   A 92  ? 0.760222 0.387634 0.585615 -0.0928749  0.0184599   0.153302    104 HIS   B C    
1304 O O    . HIS   A 92  ? 0.841959 0.455376 0.627235 -0.0794612  0.0209163   0.146909    104 HIS   B O    
1305 C CB   . HIS   A 92  ? 0.868285 0.416094 0.65422  -0.0925518  0.0760519   0.175906    104 HIS   B CB   
1306 C CG   . HIS   A 92  ? 0.903775 0.431222 0.729455 -0.110492   0.106946    0.189487    104 HIS   B CG   
1307 N ND1  . HIS   A 92  ? 0.975822 0.444549 0.752055 -0.103958   0.131682    0.204214    104 HIS   B ND1  
1308 C CD2  . HIS   A 92  ? 0.879808 0.438182 0.795126 -0.135539   0.117124    0.19138     104 HIS   B CD2  
1309 C CE1  . HIS   A 92  ? 1.01075  0.47262  0.849352 -0.128353   0.158196    0.21439     104 HIS   B CE1  
1310 N NE2  . HIS   A 92  ? 0.93613  0.456904 0.862786 -0.148332   0.146671    0.204702    104 HIS   B NE2  
1311 H H    . HIS   A 92  ? 0.842501 0.428273 0.687346 -0.0936026  0.101834    0.170051    104 HIS   B H    
1312 H HA   . HIS   A 92  ? 0.759964 0.387995 0.658592 -0.118353   0.042978    0.165285    104 HIS   B HA   
1313 H HB2  . HIS   A 92  ? 0.901387 0.4281   0.644835 -0.0787091  0.091267    0.177507    104 HIS   B HB2  
1314 H HB3  . HIS   A 92  ? 0.866913 0.409159 0.62197  -0.0849127  0.0547253   0.172311    104 HIS   B HB3  
1316 H HD2  . HIS   A 92  ? 0.838719 0.43781  0.802778 -0.142978   0.104555    0.185169    104 HIS   B HD2  
1317 H HE1  . HIS   A 92  ? 1.04991  0.471597 0.874712 -0.131129   0.180254    0.226951    104 HIS   B HE1  
1319 N N    . LEU   A 93  ? 0.722832 0.385697 0.572919 -0.0988541  -0.0134869  0.148935    105 LEU   B N    
1320 C CA   . LEU   A 93  ? 0.698581 0.388735 0.535767 -0.0913733  -0.0438697  0.141122    105 LEU   B CA   
1321 C C    . LEU   A 93  ? 0.739278 0.429005 0.545125 -0.0819333  -0.0628142  0.139645    105 LEU   B C    
1322 O O    . LEU   A 93  ? 0.681668 0.37594  0.508104 -0.0893029  -0.0660453  0.140892    105 LEU   B O    
1323 C CB   . LEU   A 93  ? 0.671281 0.410404 0.570097 -0.10336    -0.0596324  0.142049    105 LEU   B CB   
1324 C CG   . LEU   A 93  ? 0.634336 0.378638 0.57263  -0.108823   -0.0452748  0.143799    105 LEU   B CG   
1325 C CD1  . LEU   A 93  ? 0.581769 0.37088  0.574477 -0.116433   -0.0635481  0.15014     105 LEU   B CD1  
1326 C CD2  . LEU   A 93  ? 0.705358 0.421425 0.604272 -0.0986871  -0.0387123  0.133801    105 LEU   B CD2  
1327 H H    . LEU   A 93  ? 0.709311 0.380607 0.587358 -0.108416   -0.0154182  0.150962    105 LEU   B H    
1328 H HA   . LEU   A 93  ? 0.730068 0.406207 0.537201 -0.082647   -0.0417455  0.136677    105 LEU   B HA   
1329 H HB2  . LEU   A 93  ? 0.642942 0.396156 0.56544  -0.109999   -0.0641542  0.144963    105 LEU   B HB2  
1330 H HB3  . LEU   A 93  ? 0.646163 0.402177 0.536967 -0.0995033  -0.076984   0.139283    105 LEU   B HB3  
1331 H HG   . LEU   A 93  ? 0.653596 0.389355 0.609357 -0.112772   -0.0271164  0.147773    105 LEU   B HG   
1332 H HD11 . LEU   A 93  ? 0.569226 0.376071 0.582466 -0.121127   -0.0693445  0.154463    105 LEU   B HD11 
1333 H HD12 . LEU   A 93  ? 0.584286 0.372837 0.601946 -0.11734    -0.0540607  0.151991    105 LEU   B HD12 
1334 H HD13 . LEU   A 93  ? 0.576466 0.375902 0.557547 -0.114408   -0.0783172  0.148532    105 LEU   B HD13 
1335 H HD21 . LEU   A 93  ? 0.729249 0.415654 0.590788 -0.0913666  -0.023843   0.132436    105 LEU   B HD21 
1336 H HD22 . LEU   A 93  ? 0.689173 0.414165 0.573322 -0.0963281  -0.0576509  0.128615    105 LEU   B HD22 
1337 H HD23 . LEU   A 93  ? 0.691063 0.409044 0.616451 -0.100863   -0.0305764  0.133493    105 LEU   B HD23 
1338 N N    . LEU   A 94  ? 0.656846 0.344084 0.417125 -0.0646904  -0.0777312  0.134553    106 LEU   B N    
1339 C CA   . LEU   A 94  ? 0.669495 0.368946 0.408889 -0.0508433  -0.0978148  0.13291     106 LEU   B CA   
1340 C C    . LEU   A 94  ? 0.67337  0.427993 0.440927 -0.051766   -0.122045   0.128184    106 LEU   B C    
1341 O O    . LEU   A 94  ? 0.691619 0.45412  0.459308 -0.0528821  -0.128945   0.122075    106 LEU   B O    
1342 C CB   . LEU   A 94  ? 0.727967 0.38508  0.397997 -0.026498   -0.0955248  0.134312    106 LEU   B CB   
1343 C CG   . LEU   A 94  ? 0.756083 0.418032 0.401786 -0.00527189 -0.112533   0.1342      106 LEU   B CG   
1344 C CD1  . LEU   A 94  ? 0.770361 0.412847 0.426367 -0.00921783 -0.104918   0.136222    106 LEU   B CD1  
1345 C CD2  . LEU   A 94  ? 0.862753 0.484427 0.438623 0.0226589   -0.112533   0.138327    106 LEU   B CD2  
1346 H H    . LEU   A 94  ? 0.697047 0.376065 0.439992 -0.0602313  -0.0759203  0.130921    106 LEU   B H    
1347 H HA   . LEU   A 94  ? 0.666503 0.366164 0.420414 -0.0557282  -0.0963901  0.13467     106 LEU   B HA   
1348 H HB2  . LEU   A 94  ? 0.762095 0.381012 0.41602  -0.0278687  -0.0749703  0.140566    106 LEU   B HB2  
1349 H HB3  . LEU   A 94  ? 0.743067 0.403931 0.396628 -0.0207426  -0.101911   0.129634    106 LEU   B HB3  
1350 H HG   . LEU   A 94  ? 0.732343 0.437286 0.39943  -0.0042547  -0.130151   0.129387    106 LEU   B HG   
1351 H HD11 . LEU   A 94  ? 0.729771 0.400473 0.425292 -0.0244274  -0.108342   0.132953    106 LEU   B HD11 
1352 H HD12 . LEU   A 94  ? 0.780812 0.424169 0.417795 0.0080595   -0.114829   0.134867    106 LEU   B HD12 
1353 H HD13 . LEU   A 94  ? 0.798622 0.398947 0.440632 -0.0129448  -0.0869262  0.141648    106 LEU   B HD13 
1354 H HD21 . LEU   A 94  ? 0.85242  0.488494 0.41952  0.0260518   -0.122553   0.132935    106 LEU   B HD21 
1355 H HD22 . LEU   A 94  ? 0.88506  0.462295 0.437648 0.0220811   -0.0916071  0.146102    106 LEU   B HD22 
1356 H HD23 . LEU   A 94  ? 0.86095  0.486086 0.423039 0.0393177   -0.123404   0.138927    106 LEU   B HD23 
1357 N N    . ILE   A 95  ? 0.58239  0.371981 0.371809 -0.0509609  -0.133535   0.130166    107 ILE   B N    
1358 C CA   . ILE   A 95  ? 0.556767 0.40203  0.387839 -0.0576273  -0.146914   0.132779    107 ILE   B CA   
1359 C C    . ILE   A 95  ? 0.591484 0.470749 0.415192 -0.0399374  -0.1601     0.132706    107 ILE   B C    
1360 O O    . ILE   A 95  ? 0.575111 0.451706 0.384975 -0.0297465  -0.158677   0.132554    107 ILE   B O    
1361 C CB   . ILE   A 95  ? 0.520589 0.384165 0.392779 -0.0736902  -0.141918   0.140389    107 ILE   B CB   
1362 C CG1  . ILE   A 95  ? 0.528656 0.36598  0.418706 -0.0878754  -0.127266   0.141494    107 ILE   B CG1  
1363 C CG2  . ILE   A 95  ? 0.520474 0.435897 0.430982 -0.0790395  -0.150298   0.149891    107 ILE   B CG2  
1364 C CD1  . ILE   A 95  ? 0.532374 0.383965 0.458336 -0.0986069  -0.125497   0.147543    107 ILE   B CD1  
1365 H H    . ILE   A 95  ? 0.611278 0.387163 0.387368 -0.0454085  -0.131246   0.130355    107 ILE   B H    
1366 H HA   . ILE   A 95  ? 0.558959 0.408838 0.398322 -0.0622922  -0.150004   0.130415    107 ILE   B HA   
1367 H HB   . ILE   A 95  ? 0.534214 0.393203 0.39638  -0.0693793  -0.142133   0.139245    107 ILE   B HB   
1368 H HG12 . ILE   A 95  ? 0.526084 0.369369 0.430374 -0.0925793  -0.127467   0.141979    107 ILE   B HG12 
1369 H HG13 . ILE   A 95  ? 0.557149 0.36148  0.421683 -0.0841059  -0.118225   0.137599    107 ILE   B HG13 
1370 H HG21 . ILE   A 95  ? 0.498233 0.421362 0.430402 -0.0870786  -0.147434   0.156634    107 ILE   B HG21 
1371 H HG22 . ILE   A 95  ? 0.510173 0.429636 0.431559 -0.0834887  -0.152563   0.148805    107 ILE   B HG22 
1372 H HG23 . ILE   A 95  ? 0.510999 0.447224 0.413889 -0.0691576  -0.155519   0.150893    107 ILE   B HG23 
1373 H HD11 . ILE   A 95  ? 0.535078 0.381636 0.44791  -0.0951767  -0.128689   0.143952    107 ILE   B HD11 
1374 H HD12 . ILE   A 95  ? 0.529143 0.36545  0.469481 -0.105517   -0.114572   0.148096    107 ILE   B HD12 
1375 H HD13 . ILE   A 95  ? 0.506527 0.387564 0.454474 -0.100914   -0.132383   0.154372    107 ILE   B HD13 
1376 N N    . LYS   A 96  ? 0.562948 0.477895 0.402729 -0.0370848  -0.173215   0.131167    108 LYS   B N    
1377 C CA   . LYS   A 96  ? 0.574151 0.537324 0.425179 -0.0211741  -0.183219   0.133427    108 LYS   B CA   
1378 C C    . LYS   A 96  ? 0.536921 0.546441 0.429894 -0.0308461  -0.176809   0.14583     108 LYS   B C    
1379 O O    . LYS   A 96  ? 0.48245  0.493157 0.404041 -0.0518489  -0.17051    0.15363     108 LYS   B O    
1380 C CB   . LYS   A 96  ? 0.577491 0.570473 0.445347 -0.0191488  -0.20167    0.126721    108 LYS   B CB   
1381 C CG   . LYS   A 96  ? 0.658438 0.61352  0.474136 -0.00152894 -0.213278   0.115254    108 LYS   B CG   
1382 C CD   . LYS   A 96  ? 0.699154 0.687673 0.529159 0.00182896  -0.240488   0.103314    108 LYS   B CD   
1383 C CE   . LYS   A 96  ? 0.712819 0.658728 0.471596 0.0284808   -0.252597   0.0947629   108 LYS   B CE   
1384 N NZ   . LYS   A 96  ? 0.805137 0.782646 0.58046  0.0253371   -0.283755   0.0778487   108 LYS   B NZ   
1385 H H    . LYS   A 96  ? 0.573799 0.483897 0.42059  -0.0454013  -0.175783   0.127647    108 LYS   B H    
1386 H HA   . LYS   A 96  ? 0.59041  0.536427 0.410219 -0.00370745 -0.182163   0.13117     108 LYS   B HA   
1387 H HB2  . LYS   A 96  ? 0.572232 0.573182 0.469699 -0.0381229  -0.202319   0.126809    108 LYS   B HB2  
1388 H HB3  . LYS   A 96  ? 0.578952 0.613669 0.467504 -0.010523   -0.206563   0.130073    108 LYS   B HB3  
1389 H HG2  . LYS   A 96  ? 0.673216 0.615684 0.459553 0.0183306   -0.211392   0.117291    108 LYS   B HG2  
1390 H HG3  . LYS   A 96  ? 0.667114 0.581185 0.461389 -0.00926652 -0.204361   0.113298    108 LYS   B HG3  
1391 H HD2  . LYS   A 96  ? 0.673289 0.664099 0.5279   -0.0184346  -0.242784   0.098349    108 LYS   B HD2  
1392 H HD3  . LYS   A 96  ? 0.668976 0.705455 0.531119 0.00772104  -0.248314   0.106211    108 LYS   B HD3  
1393 H HE2  . LYS   A 96  ? 0.752138 0.700685 0.492165 0.0508016   -0.254153   0.0997718   108 LYS   B HE2  
1394 H HE3  . LYS   A 96  ? 0.755998 0.652718 0.479117 0.0256591   -0.239035   0.0951899   108 LYS   B HE3  
1395 H HZ1  . LYS   A 96  ? 0.766741 0.79264  0.577899 0.0295153   -0.296416   0.0782505   108 LYS   B HZ1  
1396 H HZ2  . LYS   A 96  ? 0.766418 0.742679 0.565338 0.00370127  -0.282346   0.0722306   108 LYS   B HZ2  
1397 H HZ3  . LYS   A 96  ? 0.821025 0.771406 0.547842 0.0417138   -0.292492   0.0721333   108 LYS   B HZ3  
1398 N N    . PRO   A 97  ? 0.544894 0.593609 0.439422 -0.0118462  -0.176071   0.150097    109 PRO   B N    
1399 C CA   . PRO   A 97  ? 0.523644 0.608441 0.437466 -0.0137088  -0.165535   0.163313    109 PRO   B CA   
1400 C C    . PRO   A 97  ? 0.532811 0.656704 0.50309  -0.036798   -0.160619   0.180563    109 PRO   B C    
1401 O O    . PRO   A 97  ? 0.572191 0.702489 0.550209 -0.0445145  -0.151402   0.194549    109 PRO   B O    
1402 C CB   . PRO   A 97  ? 0.543765 0.662872 0.445334 0.0161243   -0.162723   0.162734    109 PRO   B CB   
1403 C CG   . PRO   A 97  ? 0.577278 0.674829 0.453811 0.035456    -0.174056   0.149609    109 PRO   B CG   
1404 C CD   . PRO   A 97  ? 0.64187  0.696894 0.511656 0.017634    -0.183552   0.142863    109 PRO   B CD   
1405 H HA   . PRO   A 97  ? 0.536505 0.594379 0.429873 -0.015691   -0.162413   0.161211    109 PRO   B HA   
1406 H HB2  . PRO   A 97  ? 0.533897 0.700408 0.470372 0.0145427   -0.158321   0.173426    109 PRO   B HB2  
1407 H HB3  . PRO   A 97  ? 0.558925 0.666168 0.433848 0.0257841   -0.15738    0.160659    109 PRO   B HB3  
1408 H HG2  . PRO   A 97  ? 0.586326 0.72576  0.486377 0.0454458   -0.17729    0.152382    109 PRO   B HG2  
1409 H HG3  . PRO   A 97  ? 0.611737 0.68001  0.451107 0.0519856   -0.171744   0.142748    109 PRO   B HG3  
1410 H HD2  . PRO   A 97  ? 0.607427 0.684583 0.495983 0.0174939   -0.193594   0.141253    109 PRO   B HD2  
1411 H HD3  . PRO   A 97  ? 0.631849 0.642165 0.462916 0.0267239   -0.183523   0.136081    109 PRO   B HD3  
1412 N N    . GLU   A 98  ? 0.510327 0.653072 0.51864  -0.0488104  -0.168936   0.178667    110 GLU   B N    
1413 C CA   . GLU   A 98  ? 0.528569 0.700724 0.59766  -0.0739167  -0.164356   0.193524    110 GLU   B CA   
1414 C C    . GLU   A 98  ? 0.506451 0.637935 0.578049 -0.0932255  -0.158596   0.199542    110 GLU   B C    
1415 O O    . GLU   A 98  ? 0.431651 0.580084 0.545262 -0.109168   -0.149201   0.21871     110 GLU   B O    
1416 C CB   . GLU   A 98  ? 0.520604 0.711304 0.626268 -0.0839556  -0.182066   0.180272    110 GLU   B CB   
1417 C CG   . GLU   A 98  ? 0.582473 0.830433 0.704621 -0.0638233  -0.188459   0.178635    110 GLU   B CG   
1418 C CD   . GLU   A 98  ? 0.669347 0.896731 0.733173 -0.0317469  -0.20058    0.162038    110 GLU   B CD   
1419 O OE1  . GLU   A 98  ? 0.574121 0.737738 0.582119 -0.0277041  -0.205548   0.149734    110 GLU   B OE1  
1420 O OE2  . GLU   A 98  ? 0.73379  1.0118   0.813516 -0.00973518 -0.2019     0.164424    110 GLU   B OE2  
1421 H H    . GLU   A 98  ? 0.532329 0.666636 0.527943 -0.0412419  -0.17897    0.167037    110 GLU   B H    
1422 H HA   . GLU   A 98  ? 0.513573 0.722881 0.600634 -0.0698865  -0.153529   0.208669    110 GLU   B HA   
1423 H HB2  . GLU   A 98  ? 0.546457 0.699653 0.623744 -0.0831976  -0.192389   0.164798    110 GLU   B HB2  
1424 H HB3  . GLU   A 98  ? 0.530853 0.732985 0.679607 -0.104157   -0.179645   0.187748    110 GLU   B HB3  
1425 H HG2  . GLU   A 98  ? 0.582243 0.856831 0.748176 -0.0766087  -0.19893    0.174981    110 GLU   B HG2  
1426 H HG3  . GLU   A 98  ? 0.575485 0.85481  0.710947 -0.0581186  -0.173147   0.194224    110 GLU   B HG3  
1427 N N    . TYR   A 99  ? 0.47374  0.55306  0.505149 -0.0905524  -0.161929   0.185624    111 TYR   B N    
1428 C CA   . TYR   A 99  ? 0.473957 0.519102 0.512494 -0.104455   -0.156013   0.189799    111 TYR   B CA   
1429 C C    . TYR   A 99  ? 0.500976 0.535525 0.511329 -0.0945209  -0.151314   0.194432    111 TYR   B C    
1430 O O    . TYR   A 99  ? 0.492478 0.501771 0.507692 -0.101614   -0.148324   0.195608    111 TYR   B O    
1431 C CB   . TYR   A 99  ? 0.45255  0.451293 0.476576 -0.110431   -0.160758   0.169983    111 TYR   B CB   
1432 C CG   . TYR   A 99  ? 0.488485 0.495056 0.540357 -0.122434   -0.171824   0.159968    111 TYR   B CG   
1433 C CD1  . TYR   A 99  ? 0.533762 0.562846 0.577328 -0.113491   -0.187438   0.147431    111 TYR   B CD1  
1434 C CD2  . TYR   A 99  ? 0.516133 0.510407 0.608974 -0.142545   -0.168737   0.163247    111 TYR   B CD2  
1435 C CE1  . TYR   A 99  ? 0.528272 0.571968 0.604907 -0.126641   -0.203956   0.134746    111 TYR   B CE1  
1436 C CE2  . TYR   A 99  ? 0.555618 0.555219 0.680165 -0.157588   -0.182044   0.150235    111 TYR   B CE2  
1437 C CZ   . TYR   A 99  ? 0.536418 0.563457 0.653819 -0.150913   -0.201736   0.134301    111 TYR   B CZ   
1438 O OH   . TYR   A 99  ? 0.544092 0.581164 0.698169 -0.16761    -0.220562   0.117652    111 TYR   B OH   
1439 H H    . TYR   A 99  ? 0.493351 0.558406 0.494141 -0.0786847  -0.166782   0.174058    111 TYR   B H    
1440 H HA   . TYR   A 99  ? 0.466202 0.5264   0.53924  -0.115533   -0.15159    0.203175    111 TYR   B HA   
1441 H HB2  . TYR   A 99  ? 0.475746 0.458542 0.464865 -0.0990366  -0.163196   0.159877    111 TYR   B HB2  
1442 H HB3  . TYR   A 99  ? 0.465036 0.442665 0.494934 -0.11667    -0.154077   0.17303     111 TYR   B HB3  
1443 H HD1  . TYR   A 99  ? 0.521878 0.55601  0.537859 -0.0975014  -0.188757   0.146132    111 TYR   B HD1  
1444 H HD2  . TYR   A 99  ? 0.510139 0.491362 0.611201 -0.145792   -0.158633   0.173733    111 TYR   B HD2  
1445 H HE1  . TYR   A 99  ? 0.541888 0.60561  0.61494  -0.118859   -0.217821   0.125589    111 TYR   B HE1  
1446 H HE2  . TYR   A 99  ? 0.552556 0.53637  0.703972 -0.171511   -0.179569   0.150732    111 TYR   B HE2  
1448 N N    . ALA   A 100 ? 0.50361  0.56054  0.488516 -0.0773327  -0.151899   0.195383    112 ALA   B N    
1449 C CA   . ALA   A 100 ? 0.508361 0.556409 0.464574 -0.0682177  -0.153303   0.193776    112 ALA   B CA   
1450 C C    . ALA   A 100 ? 0.468173 0.558823 0.416914 -0.0546456  -0.149066   0.209079    112 ALA   B C    
1451 O O    . ALA   A 100 ? 0.472119 0.586767 0.446235 -0.0607909  -0.142392   0.232428    112 ALA   B O    
1452 C CB   . ALA   A 100 ? 0.509082 0.520289 0.424868 -0.0578493  -0.157971   0.171575    112 ALA   B CB   
1453 H H    . ALA   A 100 ? 0.504261 0.583414 0.490697 -0.0704371  -0.152337   0.195448    112 ALA   B H    
1454 H HA   . ALA   A 100 ? 0.491411 0.527336 0.460954 -0.0777204  -0.153367   0.197703    112 ALA   B HA   
1455 H HB1  . ALA   A 100 ? 0.513039 0.496146 0.43166  -0.0665168  -0.157032   0.165819    112 ALA   B HB1  
1456 H HB2  . ALA   A 100 ? 0.520199 0.53972  0.425102 -0.0471665  -0.158427   0.167852    112 ALA   B HB2  
1457 H HB3  . ALA   A 100 ? 0.525756 0.531773 0.423812 -0.0523243  -0.160932   0.167176    112 ALA   B HB3  
1458 N N    . TYR   A 101 ? 0.505884 0.604948 0.41765  -0.0332362  -0.14953    0.19864     113 TYR   B N    
1459 C CA   . TYR   A 101 ? 0.549621 0.685344 0.440768 -0.0147931  -0.142324   0.210628    113 TYR   B CA   
1460 C C    . TYR   A 101 ? 0.559417 0.739121 0.460196 0.00053473  -0.128577   0.218787    113 TYR   B C    
1461 O O    . TYR   A 101 ? 0.51286  0.725295 0.392873 0.0199462   -0.11634    0.229943    113 TYR   B O    
1462 C CB   . TYR   A 101 ? 0.620452 0.729573 0.457313 0.00078949  -0.153671   0.189085    113 TYR   B CB   
1463 C CG   . TYR   A 101 ? 0.613488 0.698452 0.456054 -0.0152398  -0.167881   0.185693    113 TYR   B CG   
1464 C CD1  . TYR   A 101 ? 0.637446 0.746124 0.484692 -0.0155828  -0.170693   0.205151    113 TYR   B CD1  
1465 C CD2  . TYR   A 101 ? 0.629199 0.670678 0.480537 -0.0300576  -0.176119   0.167225    113 TYR   B CD2  
1466 C CE1  . TYR   A 101 ? 0.608249 0.703217 0.46887  -0.0270707  -0.186659   0.202148    113 TYR   B CE1  
1467 C CE2  . TYR   A 101 ? 0.616319 0.644889 0.486473 -0.0447917  -0.187137   0.164589    113 TYR   B CE2  
1468 C CZ   . TYR   A 101 ? 0.623657 0.681607 0.500519 -0.0426158  -0.195118   0.18024     113 TYR   B CZ   
1469 O OH   . TYR   A 101 ? 0.625691 0.678024 0.530301 -0.0549855  -0.208314   0.177738    113 TYR   B OH   
1470 H H    . TYR   A 101 ? 0.512935 0.592389 0.408675 -0.0277561  -0.153061   0.184165    113 TYR   B H    
1471 H HA   . TYR   A 101 ? 0.550261 0.699734 0.457594 -0.0221149  -0.138739   0.22848     113 TYR   B HA   
1472 H HB2  . TYR   A 101 ? 0.619805 0.705249 0.441807 0.00615554  -0.156835   0.171946    113 TYR   B HB2  
1473 H HB3  . TYR   A 101 ? 0.632991 0.764557 0.446681 0.0171496   -0.148738   0.193964    113 TYR   B HB3  
1474 H HD1  . TYR   A 101 ? 0.638011 0.77455  0.476963 -0.00502575 -0.161658   0.221367    113 TYR   B HD1  
1475 H HD2  . TYR   A 101 ? 0.621446 0.642833 0.465349 -0.02825    -0.173415   0.156798    113 TYR   B HD2  
1476 H HE1  . TYR   A 101 ? 0.631451 0.744052 0.491435 -0.0231305  -0.190788   0.216363    113 TYR   B HE1  
1477 H HE2  . TYR   A 101 ? 0.616459 0.617571 0.495127 -0.0547112  -0.189005   0.153088    113 TYR   B HE2  
1479 N N    . GLY   A 102 ? 0.511052 0.696602 0.445407 -0.00709581 -0.130316   0.214465    114 GLY   B N    
1480 C CA   . GLY   A 102 ? 0.535435 0.777392 0.50856  -0.00100745 -0.118984   0.226888    114 GLY   B CA   
1481 C C    . GLY   A 102 ? 0.597047 0.862496 0.537854 0.03411     -0.111166   0.219273    114 GLY   B C    
1482 O O    . GLY   A 102 ? 0.602169 0.826495 0.487515 0.0527331   -0.119196   0.197786    114 GLY   B O    
1483 H H    . GLY   A 102 ? 0.515744 0.671103 0.449858 -0.0159294  -0.139484   0.203004    114 GLY   B H    
1484 H HA2  . GLY   A 102 ? 0.521719 0.761765 0.520624 -0.0111458  -0.12722    0.220541    114 GLY   B HA2  
1485 H HA3  . GLY   A 102 ? 0.532632 0.800965 0.532174 -0.00985999 -0.107497   0.24754     114 GLY   B HA3  
1486 N N    . SER   A 103 ? 0.594364 0.925668 0.574409 0.0429951   -0.0927128  0.237795    115 SER   B N    
1487 C CA   . SER   A 103 ? 0.622997 0.982769 0.579473 0.0808091   -0.0817395  0.230865    115 SER   B CA   
1488 C C    . SER   A 103 ? 0.638273 0.985595 0.527879 0.104299    -0.0686101  0.230992    115 SER   B C    
1489 O O    . SER   A 103 ? 0.685043 1.02035  0.524326 0.138419    -0.0659853  0.212554    115 SER   B O    
1490 C CB   . SER   A 103 ? 0.664552 1.10519  0.69105  0.0861441   -0.0652422  0.248267    115 SER   B CB   
1491 O OG   . SER   A 103 ? 0.706622 1.18714  0.78806  0.06002     -0.0465547  0.279671    115 SER   B OG   
1492 H H    . SER   A 103 ? 0.581091 0.938923 0.605081 0.0258536   -0.0855268  0.254906    115 SER   B H    
1493 H HA   . SER   A 103 ? 0.63051  0.959107 0.564154 0.0905306   -0.095866   0.211009    115 SER   B HA   
1494 H HB2  . SER   A 103 ? 0.688844 1.15093  0.69572  0.114741    -0.0519473  0.247244    115 SER   B HB2  
1495 H HB3  . SER   A 103 ? 0.648021 1.09194  0.702817 0.0804636   -0.080558   0.238652    115 SER   B HB3  
1497 N N    . ALA   A 104 ? 0.637518 0.986689 0.52292  0.089163    -0.0609992  0.251564    116 ALA   B N    
1498 C CA   . ALA   A 104 ? 0.680222 1.02272  0.496221 0.113672    -0.0521601  0.252015    116 ALA   B CA   
1499 C C    . ALA   A 104 ? 0.679656 0.952494 0.434712 0.11571     -0.0805121  0.218025    116 ALA   B C    
1500 O O    . ALA   A 104 ? 0.734916 0.991258 0.422201 0.142575    -0.0819041  0.20106     116 ALA   B O    
1501 C CB   . ALA   A 104 ? 0.685127 1.05145  0.511972 0.100936    -0.0369647  0.288191    116 ALA   B CB   
1502 H H    . ALA   A 104 ? 0.612649 0.965968 0.536079 0.0651665   -0.0622714  0.265099    116 ALA   B H    
1503 H HA   . ALA   A 104 ? 0.704798 1.07249  0.504804 0.140046    -0.0369824  0.25038     116 ALA   B HA   
1504 H HB1  . ALA   A 104 ? 0.679021 1.08835  0.548584 0.0979      -0.0160974  0.311015    116 ALA   B HB1  
1505 H HB2  . ALA   A 104 ? 0.661362 1.00346  0.506224 0.077505    -0.0510386  0.289989    116 ALA   B HB2  
1506 H HB3  . ALA   A 104 ? 0.725933 1.08808  0.499007 0.120278    -0.0334922  0.287659    116 ALA   B HB3  
1507 N N    . GLY   A 105 ? 0.654594 0.88782  0.435364 0.0862858   -0.101643   0.20862     117 GLY   B N    
1508 C CA   . GLY   A 105 ? 0.692361 0.864885 0.432137 0.0815038   -0.125451   0.180832    117 GLY   B CA   
1509 C C    . GLY   A 105 ? 0.715177 0.888801 0.425389 0.0803958   -0.132894   0.187737    117 GLY   B C    
1510 O O    . GLY   A 105 ? 0.699074 0.912239 0.427077 0.0777134   -0.118865   0.220054    117 GLY   B O    
1511 H H    . GLY   A 105 ? 0.623806 0.868028 0.449473 0.0686749   -0.10062    0.218971    117 GLY   B H    
1512 H HA2  . GLY   A 105 ? 0.658413 0.808569 0.424492 0.0614325   -0.134528   0.177411    117 GLY   B HA2  
1513 H HA3  . GLY   A 105 ? 0.715092 0.867607 0.420919 0.100012    -0.127987   0.160623    117 GLY   B HA3  
1514 N N    . SER   A 106 ? 0.726494 0.857057 0.391692 0.0841598   -0.155391   0.157695    118 SER   B N    
1515 C CA   . SER   A 106 ? 0.773011 0.904774 0.407712 0.0852055   -0.172042   0.157433    118 SER   B CA   
1516 C C    . SER   A 106 ? 0.863637 0.95784  0.432918 0.103495    -0.192401   0.116148    118 SER   B C    
1517 O O    . SER   A 106 ? 0.865278 0.920793 0.437725 0.0860654   -0.219069   0.0903076   118 SER   B O    
1518 C CB   . SER   A 106 ? 0.730823 0.852643 0.414744 0.0534372   -0.187492   0.166644    118 SER   B CB   
1519 O OG   . SER   A 106 ? 0.730186 0.867217 0.3874   0.0604677   -0.203752   0.173351    118 SER   B OG   
1520 H H    . SER   A 106 ? 0.743024 0.842492 0.398116 0.0861332   -0.161616   0.136521    118 SER   B H    
1521 H HA   . SER   A 106 ? 0.789246 0.955164 0.411787 0.0980496   -0.15874    0.179087    118 SER   B HA   
1522 H HB2  . SER   A 106 ? 0.686297 0.824065 0.410071 0.0422117   -0.174338   0.188641    118 SER   B HB2  
1523 H HB3  . SER   A 106 ? 0.714549 0.803711 0.408069 0.0412528   -0.199171   0.146111    118 SER   B HB3  
1525 N N    . LEU   A 107 ? 0.899469 1.00799  0.412598 0.139082    -0.17764    0.110734    119 LEU   B N    
1526 C CA   . LEU   A 107 ? 1.01271  1.07941  0.460324 0.162866    -0.189918   0.0680231   119 LEU   B CA   
1527 C C    . LEU   A 107 ? 1.07338  1.12386  0.47133  0.164136    -0.223885   0.0436337   119 LEU   B C    
1528 O O    . LEU   A 107 ? 1.15174  1.24033  0.537591 0.167213    -0.228644   0.0668693   119 LEU   B O    
1529 C CB   . LEU   A 107 ? 1.05453  1.14969  0.459997 0.204907    -0.158624   0.07355     119 LEU   B CB   
1530 C CG   . LEU   A 107 ? 1.07544  1.18186  0.529742 0.208176    -0.133908   0.084911    119 LEU   B CG   
1531 C CD1  . LEU   A 107 ? 1.14126  1.28818  0.561631 0.252673    -0.101142   0.092146    119 LEU   B CD1  
1532 C CD2  . LEU   A 107 ? 1.02036  1.06093  0.479841 0.200521    -0.149527   0.0530855   119 LEU   B CD2  
1533 H H    . LEU   A 107 ? 0.908145 1.05354  0.42539  0.149359    -0.15724    0.135041    119 LEU   B H    
1534 H HA   . LEU   A 107 ? 0.990865 1.02071  0.457331 0.151217    -0.19608    0.0511787   119 LEU   B HA   
1535 H HB2  . LEU   A 107 ? 1.07211  1.20867  0.470604 0.213047    -0.145391   0.0991082   119 LEU   B HB2  
1536 H HB3  . LEU   A 107 ? 1.12889  1.19551  0.479442 0.225191    -0.167235   0.0439768   119 LEU   B HB3  
1537 H HG   . LEU   A 107 ? 0.999794 1.13417  0.507235 0.18744     -0.127282   0.111547    119 LEU   B HG   
1538 H HD11 . LEU   A 107 ? 1.12724  1.31962  0.556536 0.253748    -0.0854364  0.120233    119 LEU   B HD11 
1539 H HD12 . LEU   A 107 ? 1.11264  1.26646  0.563504 0.257922    -0.0898007  0.0948497   119 LEU   B HD12 
1540 H HD13 . LEU   A 107 ? 1.1975   1.3179   0.55776  0.275581    -0.106755   0.0662461   119 LEU   B HD13 
1541 H HD21 . LEU   A 107 ? 0.999005 1.02231  0.491043 0.171343    -0.163342   0.0549245   119 LEU   B HD21 
1542 H HD22 . LEU   A 107 ? 1.09265  1.09693  0.503663 0.215096    -0.159859   0.0245721   119 LEU   B HD22 
1543 H HD23 . LEU   A 107 ? 1.02209  1.07232  0.50076  0.211166    -0.134955   0.0595379   119 LEU   B HD23 
1544 N N    . PRO   A 108 ? 1.11925  1.11181  0.484691 0.163741    -0.250387   -0.00460497 120 PRO   B N    
1545 C CA   . PRO   A 108 ? 1.1067   1.04303  0.479223 0.162974    -0.244649   -0.030482   120 PRO   B CA   
1546 C C    . PRO   A 108 ? 1.03872  0.941712 0.483646 0.120747    -0.253624   -0.0296387  120 PRO   B C    
1547 O O    . PRO   A 108 ? 1.05241  0.902498 0.502852 0.118504    -0.248524   -0.0464242  120 PRO   B O    
1548 C CB   . PRO   A 108 ? 1.24632  1.13021  0.546166 0.180925    -0.270188   -0.0831723  120 PRO   B CB   
1549 C CG   . PRO   A 108 ? 1.25801  1.16098  0.558871 0.161205    -0.306952   -0.0890769  120 PRO   B CG   
1550 C CD   . PRO   A 108 ? 1.20401  1.18075  0.520157 0.166085    -0.289836   -0.0378411  120 PRO   B CD   
1551 H HA   . PRO   A 108 ? 1.10626  1.05724  0.476377 0.181493    -0.219775   -0.0173102  120 PRO   B HA   
1552 H HB2  . PRO   A 108 ? 1.24902  1.08245  0.559718 0.170689    -0.276115   -0.105081   120 PRO   B HB2  
1553 H HB3  . PRO   A 108 ? 1.28384  1.17675  0.530973 0.213989    -0.257627   -0.0880016  120 PRO   B HB3  
1554 H HG2  . PRO   A 108 ? 1.22811  1.1116   0.577509 0.130287    -0.322245   -0.0953354  120 PRO   B HG2  
1555 H HG3  . PRO   A 108 ? 1.32887  1.21615  0.573147 0.177598    -0.325566   -0.118671   120 PRO   B HG3  
1556 H HD2  . PRO   A 108 ? 1.17229  1.16266  0.524983 0.143589    -0.306799   -0.0283307  120 PRO   B HD2  
1557 H HD3  . PRO   A 108 ? 1.25064  1.24796  0.509998 0.1939      -0.286338   -0.0363642  120 PRO   B HD3  
1558 N N    . LYS   A 109 ? 0.98087  0.911637 0.476323 0.0907652   -0.265854   -0.00989264 121 LYS   B N    
1559 C CA   . LYS   A 109 ? 0.943276 0.845669 0.504364 0.0521158   -0.27347    -0.0106441  121 LYS   B CA   
1560 C C    . LYS   A 109 ? 0.832715 0.731018 0.433533 0.0452328   -0.244706   0.0143784   121 LYS   B C    
1561 O O    . LYS   A 109 ? 0.826653 0.676434 0.448306 0.029447    -0.242089   0.00437216  121 LYS   B O    
1562 C CB   . LYS   A 109 ? 0.911319 0.85318  0.516935 0.0294248   -0.290396   0.00693674  121 LYS   B CB   
1563 C CG   . LYS   A 109 ? 0.914769 0.833225 0.591854 -0.00885783 -0.296065   0.00510051  121 LYS   B CG   
1564 C CD   . LYS   A 109 ? 0.952629 0.913863 0.67595  -0.0253647  -0.314762   0.0198013   121 LYS   B CD   
1565 C CE   . LYS   A 109 ? 1.02136  0.987507 0.725654 -0.0250408  -0.355747   -0.0113548  121 LYS   B CE   
1566 N NZ   . LYS   A 109 ? 1.05417  0.991865 0.818128 -0.0591636  -0.372531   -0.0359336  121 LYS   B NZ   
1567 H H    . LYS   A 109 ? 0.981843 0.950251 0.470002 0.0965011   -0.267498   0.00596882  121 LYS   B H    
1568 H HA   . LYS   A 109 ? 0.971143 0.829911 0.522683 0.0459477   -0.286732   -0.0393752  121 LYS   B HA   
1569 H HB2  . LYS   A 109 ? 0.96225  0.911871 0.539378 0.0367063   -0.311891   -0.00809125 121 LYS   B HB2  
1570 H HB3  . LYS   A 109 ? 0.885254 0.863177 0.501593 0.0345613   -0.275773   0.0360391   121 LYS   B HB3  
1571 H HG2  . LYS   A 109 ? 0.879702 0.791806 0.578961 -0.0140502  -0.275042   0.0213555   121 LYS   B HG2  
1572 H HG3  . LYS   A 109 ? 0.95315  0.833265 0.625189 -0.0164671  -0.307336   -0.0218879  121 LYS   B HG3  
1573 H HD2  . LYS   A 109 ? 0.917762 0.913246 0.635709 -0.0139238  -0.305727   0.0450338   121 LYS   B HD2  
1574 H HD3  . LYS   A 109 ? 0.904251 0.856951 0.677725 -0.0467175  -0.308701   0.025863    121 LYS   B HD3  
1575 H HE2  . LYS   A 109 ? 1.07283  1.02294  0.722377 -0.00716755 -0.361464   -0.0311183  121 LYS   B HE2  
1576 H HE3  . LYS   A 109 ? 1.02059  1.0256   0.72769  -0.019055   -0.36649    0.00389639  121 LYS   B HE3  
1577 H HZ1  . LYS   A 109 ? 1.05066  0.948782 0.813124 -0.0650697  -0.359327   -0.0456259  121 LYS   B HZ1  
1578 H HZ2  . LYS   A 109 ? 1.0041   0.961053 0.81837  -0.0733899  -0.367772   -0.0183394  121 LYS   B HZ2  
1579 H HZ3  . LYS   A 109 ? 1.08643  1.02657  0.840133 -0.0599223  -0.400449   -0.0589515  121 LYS   B HZ3  
1580 N N    . ILE   A 110 ? 0.801365 0.749782 0.41286  0.0566099   -0.223692   0.0471861   122 ILE   B N    
1581 C CA   . ILE   A 110 ? 0.715836 0.66667  0.363419 0.051429    -0.202776   0.0671178   122 ILE   B CA   
1582 C C    . ILE   A 110 ? 0.749867 0.724262 0.371186 0.0847937   -0.183829   0.0727206   122 ILE   B C    
1583 O O    . ILE   A 110 ? 0.736942 0.762775 0.349195 0.0999795   -0.173701   0.0897963   122 ILE   B O    
1584 C CB   . ILE   A 110 ? 0.676518 0.668508 0.378219 0.0302396   -0.1962     0.0996252   122 ILE   B CB   
1585 C CG1  . ILE   A 110 ? 0.668496 0.656731 0.398409 0.00557247  -0.212996   0.0994816   122 ILE   B CG1  
1586 C CG2  . ILE   A 110 ? 0.642833 0.627118 0.378706 0.0209417   -0.182453   0.111083    122 ILE   B CG2  
1587 C CD1  . ILE   A 110 ? 0.647603 0.585951 0.401993 -0.0176618  -0.219492   0.0819122   122 ILE   B CD1  
1588 H H    . ILE   A 110 ? 0.798586 0.780761 0.39486  0.0675916   -0.223106   0.0573598   122 ILE   B H    
1589 H HA   . ILE   A 110 ? 0.733664 0.644217 0.38867  0.0413875   -0.204908   0.0558916   122 ILE   B HA   
1590 H HB   . ILE   A 110 ? 0.673393 0.703082 0.369173 0.0417222   -0.188928   0.114789    122 ILE   B HB   
1591 H HG12 . ILE   A 110 ? 0.69391  0.690304 0.398945 0.0136507   -0.225665   0.091134    122 ILE   B HG12 
1592 H HG13 . ILE   A 110 ? 0.630294 0.644163 0.390006 -0.00272222 -0.206846   0.121097    122 ILE   B HG13 
1593 H HG21 . ILE   A 110 ? 0.609078 0.609791 0.378176 0.00550016  -0.180266   0.126594    122 ILE   B HG21 
1594 H HG22 . ILE   A 110 ? 0.651271 0.595361 0.383098 0.0152984   -0.185454   0.0977205   122 ILE   B HG22 
1595 H HG23 . ILE   A 110 ? 0.643443 0.646139 0.3714   0.0372498   -0.17303    0.116069    122 ILE   B HG23 
1596 H HD11 . ILE   A 110 ? 0.626085 0.556853 0.401269 -0.0249138  -0.207087   0.0919541   122 ILE   B HD11 
1597 H HD12 . ILE   A 110 ? 0.648361 0.593206 0.425182 -0.031342   -0.230905   0.0814136   122 ILE   B HD12 
1598 H HD13 . ILE   A 110 ? 0.688915 0.595665 0.416547 -0.0110272  -0.223976   0.0614333   122 ILE   B HD13 
1599 N N    . PRO   A 111 ? 0.763312 0.705869 0.373772 0.100208    -0.176079   0.0622394   123 PRO   B N    
1600 C CA   . PRO   A 111 ? 0.802162 0.779641 0.397839 0.135285    -0.158311   0.0689092   123 PRO   B CA   
1601 C C    . PRO   A 111 ? 0.748992 0.789376 0.400939 0.127172    -0.14475    0.101677    123 PRO   B C    
1602 O O    . PRO   A 111 ? 0.697026 0.741842 0.392116 0.0957849   -0.149646   0.116019    123 PRO   B O    
1603 C CB   . PRO   A 111 ? 0.867579 0.785414 0.433682 0.156927    -0.158333   0.0466287   123 PRO   B CB   
1604 C CG   . PRO   A 111 ? 0.883928 0.732229 0.456811 0.126056    -0.172638   0.0338916   123 PRO   B CG   
1605 C CD   . PRO   A 111 ? 0.806466 0.679189 0.415841 0.0892428   -0.182138   0.0453717   123 PRO   B CD   
1606 H HA   . PRO   A 111 ? 0.832029 0.826914 0.398564 0.151393    -0.155673   0.0647775   123 PRO   B HA   
1607 H HB2  . PRO   A 111 ? 0.849317 0.785789 0.43309  0.167594    -0.149832   0.0581381   123 PRO   B HB2  
1608 H HB3  . PRO   A 111 ? 0.914759 0.819643 0.441526 0.179788    -0.157182   0.0299223   123 PRO   B HB3  
1609 H HG2  . PRO   A 111 ? 0.861504 0.693875 0.447506 0.124806    -0.168423   0.0412414   123 PRO   B HG2  
1610 H HG3  . PRO   A 111 ? 0.922755 0.7264   0.464346 0.132471    -0.179091   0.0114608   123 PRO   B HG3  
1611 H HD2  . PRO   A 111 ? 0.769464 0.643575 0.410318 0.072669    -0.17915    0.0588317   123 PRO   B HD2  
1612 H HD3  . PRO   A 111 ? 0.829722 0.671813 0.429746 0.0776468   -0.194078   0.0288975   123 PRO   B HD3  
1613 N N    . SER   A 112 ? 0.783373 0.873031 0.437546 0.156042    -0.127113   0.111578    124 SER   B N    
1614 C CA   . SER   A 112 ? 0.756622 0.907084 0.472979 0.148991    -0.116335   0.137747    124 SER   B CA   
1615 C C    . SER   A 112 ? 0.736171 0.856609 0.476446 0.136604    -0.129595   0.132963    124 SER   B C    
1616 O O    . SER   A 112 ? 0.730865 0.79887  0.436331 0.15376     -0.136269   0.114332    124 SER   B O    
1617 C CB   . SER   A 112 ? 0.797579 1.00658  0.51875  0.183911    -0.0946911  0.146325    124 SER   B CB   
1618 O OG   . SER   A 112 ? 0.954457 1.13003  0.63596  0.219894    -0.0954841  0.12342     124 SER   B OG   
1619 H H    . SER   A 112 ? 0.822008 0.908523 0.440915 0.180569    -0.121699   0.100685    124 SER   B H    
1620 H HA   . SER   A 112 ? 0.730011 0.902814 0.471069 0.128306    -0.114621   0.153735    124 SER   B HA   
1621 H HB2  . SER   A 112 ? 0.783606 1.03516  0.554866 0.176178    -0.08999    0.162177    124 SER   B HB2  
1622 H HB3  . SER   A 112 ? 0.833368 1.06296  0.537021 0.190835    -0.0834504  0.152997    124 SER   B HB3  
1624 N N    . ASN   A 113 ? 0.669436 0.817902 0.464011 0.107883    -0.132822   0.150047    125 ASN   B N    
1625 C CA   . ASN   A 113 ? 0.647926 0.786683 0.466098 0.101032    -0.144681   0.14812     125 ASN   B CA   
1626 C C    . ASN   A 113 ? 0.667674 0.724481 0.445964 0.0924497   -0.155604   0.132254    125 ASN   B C    
1627 O O    . ASN   A 113 ? 0.647385 0.674344 0.408727 0.106165    -0.16249    0.125631    125 ASN   B O    
1628 C CB   . ASN   A 113 ? 0.688745 0.866455 0.518111 0.134254    -0.143145   0.147597    125 ASN   B CB   
1629 C CG   . ASN   A 113 ? 0.617165 0.883766 0.499804 0.139236    -0.126928   0.16638     125 ASN   B CG   
1630 O OD1  . ASN   A 113 ? 0.641681 0.944228 0.519796 0.173759    -0.112968   0.166878    125 ASN   B OD1  
1631 N ND2  . ASN   A 113 ? 0.570671 0.874301 0.510319 0.106023    -0.126445   0.182873    125 ASN   B ND2  
1632 H H    . ASN   A 113 ? 0.655041 0.82721  0.469523 0.0930881   -0.128074   0.162844    125 ASN   B H    
1633 H HA   . ASN   A 113 ? 0.622667 0.785207 0.479065 0.0794855   -0.146101   0.158925    125 ASN   B HA   
1634 H HB2  . ASN   A 113 ? 0.704261 0.854028 0.494617 0.158196    -0.140825   0.136652    125 ASN   B HB2  
1635 H HB3  . ASN   A 113 ? 0.66255  0.834964 0.504269 0.130566    -0.154793   0.146023    125 ASN   B HB3  
1636 H HD21 . ASN   A 113 ? 0.566537 0.922571 0.545879 0.105996    -0.116421   0.195543    125 ASN   B HD21 
1637 H HD22 . ASN   A 113 ? 0.55963  0.835547 0.500556 0.0838824   -0.13494    0.181592    125 ASN   B HD22 
1638 N N    . ALA   A 114 ? 0.645935 0.670634 0.413492 0.0702745   -0.156394   0.129033    126 ALA   B N    
1639 C CA   . ALA   A 114 ? 0.691834 0.643244 0.431252 0.0599505   -0.161859   0.115294    126 ALA   B CA   
1640 C C    . ALA   A 114 ? 0.661187 0.597965 0.425774 0.03395     -0.163999   0.122653    126 ALA   B C    
1641 O O    . ALA   A 114 ? 0.572457 0.543008 0.375731 0.0133297   -0.163659   0.134261    126 ALA   B O    
1642 C CB   . ALA   A 114 ? 0.68604  0.616492 0.409425 0.0502859   -0.164745   0.104913    126 ALA   B CB   
1643 H H    . ALA   A 114 ? 0.642044 0.69244  0.422897 0.0618071   -0.153044   0.136822    126 ALA   B H    
1644 H HA   . ALA   A 114 ? 0.712559 0.636563 0.425922 0.0787537   -0.161967   0.107422    126 ALA   B HA   
1645 H HB1  . ALA   A 114 ? 0.719409 0.654232 0.418747 0.069261    -0.163888   0.0970934   126 ALA   B HB1  
1646 H HB2  . ALA   A 114 ? 0.66734  0.625075 0.413999 0.0354852   -0.16528    0.114504    126 ALA   B HB2  
1647 H HB3  . ALA   A 114 ? 0.707371 0.592533 0.421405 0.0407739   -0.167301   0.0961617   126 ALA   B HB3  
1648 N N    . THR   A 115 ? 0.641006 0.524227 0.378887 0.0388755   -0.164024   0.116919    127 THR   B N    
1649 C CA   . THR   A 115 ? 0.639721 0.491398 0.383866 0.0176609   -0.161039   0.120364    127 THR   B CA   
1650 C C    . THR   A 115 ? 0.697782 0.507113 0.442772 -0.00275889 -0.154044   0.11522     127 THR   B C    
1651 O O    . THR   A 115 ? 0.675653 0.448092 0.396944 0.00411918  -0.153183   0.104776    127 THR   B O    
1652 C CB   . THR   A 115 ? 0.698863 0.514852 0.406448 0.0371382   -0.16195    0.120364    127 THR   B CB   
1653 O OG1  . THR   A 115 ? 0.639061 0.510043 0.361878 0.0525746   -0.17424    0.123263    127 THR   B OG1  
1654 C CG2  . THR   A 115 ? 0.720527 0.499792 0.420563 0.021096    -0.154789   0.123944    127 THR   B CG2  
1655 H H    . THR   A 115 ? 0.683671 0.547717 0.395773 0.0583441   -0.164019   0.111753    127 THR   B H    
1656 H HA   . THR   A 115 ? 0.620909 0.504322 0.393517 0.00571584  -0.163067   0.126342    127 THR   B HA   
1657 H HB   . THR   A 115 ? 0.723318 0.505374 0.40242  0.0517107   -0.158965   0.116479    127 THR   B HB   
1659 H HG21 . THR   A 115 ? 0.749298 0.504086 0.417476 0.0369012   -0.15561    0.125229    127 THR   B HG21 
1660 H HG22 . THR   A 115 ? 0.688241 0.497346 0.413739 0.00944636  -0.158814   0.125528    127 THR   B HG22 
1661 H HG23 . THR   A 115 ? 0.722686 0.47247  0.423794 0.00798383  -0.144709   0.123442    127 THR   B HG23 
1662 N N    . LEU   A 116 ? 0.654746 0.466046 0.430169 -0.0273588  -0.149089   0.120959    128 LEU   B N    
1663 C CA   . LEU   A 116 ? 0.650511 0.437877 0.444724 -0.0482392  -0.143637   0.117444    128 LEU   B CA   
1664 C C    . LEU   A 116 ? 0.643552 0.394334 0.440995 -0.0602598  -0.12695    0.122943    128 LEU   B C    
1665 O O    . LEU   A 116 ? 0.593835 0.35152  0.387073 -0.0573233  -0.123891   0.12861     128 LEU   B O    
1666 C CB   . LEU   A 116 ? 0.609388 0.441405 0.446677 -0.064053   -0.150854   0.121721    128 LEU   B CB   
1667 C CG   . LEU   A 116 ? 0.656551 0.536802 0.493139 -0.0531291  -0.163113   0.123615    128 LEU   B CG   
1668 C CD1  . LEU   A 116 ? 0.649999 0.557312 0.518539 -0.0668675  -0.171497   0.127935    128 LEU   B CD1  
1669 C CD2  . LEU   A 116 ? 0.71543  0.586089 0.51234  -0.0321689  -0.168332   0.111075    128 LEU   B CD2  
1670 H H    . LEU   A 116 ? 0.638858 0.468139 0.426897 -0.0308048  -0.149572   0.126329    128 LEU   B H    
1671 H HA   . LEU   A 116 ? 0.675492 0.437725 0.452852 -0.0438063  -0.144839   0.108948    128 LEU   B HA   
1672 H HB2  . LEU   A 116 ? 0.602329 0.445203 0.459226 -0.0715399  -0.146257   0.129701    128 LEU   B HB2  
1673 H HB3  . LEU   A 116 ? 0.631059 0.448124 0.481083 -0.0753598  -0.150443   0.116877    128 LEU   B HB3  
1674 H HG   . LEU   A 116 ? 0.632694 0.538183 0.477259 -0.0495658  -0.161401   0.132869    128 LEU   B HG   
1675 H HD11 . LEU   A 116 ? 0.625953 0.540729 0.521898 -0.0771977  -0.16662    0.137584    128 LEU   B HD11 
1676 H HD12 . LEU   A 116 ? 0.646478 0.582694 0.507611 -0.0576836  -0.177099   0.131943    128 LEU   B HD12 
1677 H HD13 . LEU   A 116 ? 0.664343 0.552061 0.532895 -0.0729588  -0.176108   0.117223    128 LEU   B HD13 
1678 H HD21 . LEU   A 116 ? 0.711644 0.58155  0.49409  -0.0190737  -0.164786   0.11289     128 LEU   B HD21 
1679 H HD22 . LEU   A 116 ? 0.733307 0.568205 0.519588 -0.0357507  -0.16926    0.0998377   128 LEU   B HD22 
1680 H HD23 . LEU   A 116 ? 0.705494 0.605406 0.500793 -0.0263639  -0.174064   0.111972    128 LEU   B HD23 
1681 N N    . PHE   A 117 ? 0.652841 0.367197 0.461415 -0.0749509  -0.115834   0.120029    129 PHE   B N    
1682 C CA   . PHE   A 117 ? 0.660177 0.342037 0.477633 -0.0870797  -0.0924095  0.127777    129 PHE   B CA   
1683 C C    . PHE   A 117 ? 0.653291 0.355316 0.53255  -0.111749   -0.0895361  0.126983    129 PHE   B C    
1684 O O    . PHE   A 117 ? 0.645345 0.353033 0.544825 -0.120895   -0.103079   0.116555    129 PHE   B O    
1685 C CB   . PHE   A 117 ? 0.728413 0.343987 0.505455 -0.0799877  -0.0749363  0.13042     129 PHE   B CB   
1686 C CG   . PHE   A 117 ? 0.800865 0.381105 0.588045 -0.0931665  -0.0427577  0.14211     129 PHE   B CG   
1687 C CD1  . PHE   A 117 ? 0.842956 0.403294 0.589318 -0.0792548  -0.0258107  0.152519    129 PHE   B CD1  
1688 C CD2  . PHE   A 117 ? 0.831402 0.39821  0.667839 -0.11826    -0.0285117  0.141983    129 PHE   B CD2  
1689 C CE1  . PHE   A 117 ? 0.859802 0.388005 0.608235 -0.087036   0.00956592  0.164805    129 PHE   B CE1  
1690 C CE2  . PHE   A 117 ? 0.891627 0.433225 0.745056 -0.129686   0.00721623  0.155838    129 PHE   B CE2  
1691 C CZ   . PHE   A 117 ? 0.895151 0.416405 0.701084 -0.112507   0.0290738   0.168422    129 PHE   B CZ   
1692 H H    . PHE   A 117 ? 0.663976 0.374543 0.476267 -0.0775943  -0.122417   0.112401    129 PHE   B H    
1693 H HA   . PHE   A 117 ? 0.656018 0.346972 0.466452 -0.0823137  -0.0892862  0.132654    129 PHE   B HA   
1694 H HB2  . PHE   A 117 ? 0.752174 0.358209 0.489535 -0.0608647  -0.078238   0.132549    129 PHE   B HB2  
1695 H HB3  . PHE   A 117 ? 0.750965 0.353949 0.532835 -0.0838242  -0.0804947  0.122955    129 PHE   B HB3  
1696 H HD1  . PHE   A 117 ? 0.830022 0.401665 0.547491 -0.0637982  -0.0386324  0.150472    129 PHE   B HD1  
1697 H HD2  . PHE   A 117 ? 0.823878 0.403722 0.686232 -0.127888   -0.04348    0.131817    129 PHE   B HD2  
1698 H HE1  . PHE   A 117 ? 0.893384 0.407443 0.605968 -0.074751   0.0201606   0.170047    129 PHE   B HE1  
1699 H HE2  . PHE   A 117 ? 0.883871 0.423124 0.781285 -0.148684   0.0168403   0.155985    129 PHE   B HE2  
1700 H HZ   . PHE   A 117 ? 0.917386 0.419478 0.729011 -0.117534   0.0570477   0.17876     129 PHE   B HZ   
1701 N N    . PHE   A 118 ? 0.640726 0.349306 0.54741  -0.120219   -0.072114   0.135761    130 PHE   B N    
1702 C CA   . PHE   A 118 ? 0.660122 0.392029 0.633788 -0.140194   -0.0665599  0.137406    130 PHE   B CA   
1703 C C    . PHE   A 118 ? 0.726853 0.430235 0.713934 -0.146727   -0.0300535  0.147068    130 PHE   B C    
1704 O O    . PHE   A 118 ? 0.723061 0.405077 0.670157 -0.133416   -0.0132624  0.152658    130 PHE   B O    
1705 C CB   . PHE   A 118 ? 0.593966 0.379239 0.60743  -0.14092    -0.0804699  0.14137     130 PHE   B CB   
1706 C CG   . PHE   A 118 ? 0.586419 0.408156 0.595219 -0.135233   -0.111511   0.1371      130 PHE   B CG   
1707 C CD1  . PHE   A 118 ? 0.595041 0.425941 0.565122 -0.12018    -0.120708   0.139145    130 PHE   B CD1  
1708 C CD2  . PHE   A 118 ? 0.596635 0.446436 0.639803 -0.143833   -0.131329   0.130956    130 PHE   B CD2  
1709 C CE1  . PHE   A 118 ? 0.581832 0.448129 0.54652  -0.112836   -0.14179    0.139224    130 PHE   B CE1  
1710 C CE2  . PHE   A 118 ? 0.568751 0.450134 0.595362 -0.133861   -0.156464   0.128823    130 PHE   B CE2  
1711 C CZ   . PHE   A 118 ? 0.611444 0.50026  0.598287 -0.11806    -0.158372   0.134656    130 PHE   B CZ   
1712 H H    . PHE   A 118 ? 0.654299 0.353584 0.537836 -0.111778   -0.0642151  0.139784    130 PHE   B H    
1713 H HA   . PHE   A 118 ? 0.66333  0.394942 0.653132 -0.148941   -0.0756185  0.13046     130 PHE   B HA   
1714 H HB2  . PHE   A 118 ? 0.597862 0.379519 0.595897 -0.133524   -0.0730609  0.145632    130 PHE   B HB2  
1715 H HB3  . PHE   A 118 ? 0.595839 0.394344 0.654411 -0.151289   -0.0745524  0.143666    130 PHE   B HB3  
1716 H HD1  . PHE   A 118 ? 0.595923 0.411051 0.544603 -0.114552   -0.111953   0.140838    130 PHE   B HD1  
1717 H HD2  . PHE   A 118 ? 0.594586 0.444494 0.673423 -0.155781   -0.127383   0.128715    130 PHE   B HD2  
1718 H HE1  . PHE   A 118 ? 0.581674 0.458351 0.527552 -0.103647   -0.144904   0.142333    130 PHE   B HE1  
1719 H HE2  . PHE   A 118 ? 0.589262 0.488911 0.632356 -0.137525   -0.172396   0.123121    130 PHE   B HE2  
1720 H HZ   . PHE   A 118 ? 0.590531 0.50145  0.565165 -0.110227   -0.171451   0.135041    130 PHE   B HZ   
1721 N N    . GLU   A 119 ? 0.67302  0.380142 0.719023 -0.166921   -0.0183313  0.147912    131 GLU   B N    
1722 C CA   . GLU   A 119 ? 0.710481 0.417373 0.79883  -0.174674   0.0172232   0.159146    131 GLU   B CA   
1723 C C    . GLU   A 119 ? 0.712711 0.482223 0.875998 -0.181024   0.0024515   0.158371    131 GLU   B C    
1724 O O    . GLU   A 119 ? 0.69944  0.503683 0.9079   -0.193312   -0.0260186  0.150106    131 GLU   B O    
1725 C CB   . GLU   A 119 ? 0.792989 0.465795 0.907892 -0.193409   0.0449954   0.1645      131 GLU   B CB   
1726 C CG   . GLU   A 119 ? 0.841716 0.520793 1.00788  -0.200694   0.0889502   0.179105    131 GLU   B CG   
1727 C CD   . GLU   A 119 ? 0.945637 0.587136 1.13946  -0.221312   0.123129    0.189294    131 GLU   B CD   
1728 O OE1  . GLU   A 119 ? 0.965638 0.542635 1.09492  -0.212443   0.156459    0.203551    131 GLU   B OE1  
1729 O OE2  . GLU   A 119 ? 0.913398 0.593069 1.19985  -0.248027   0.111723    0.182367    131 GLU   B OE2  
1730 H H    . GLU   A 119 ? 0.695137 0.406506 0.757681 -0.175969   -0.0327072  0.140353    131 GLU   B H    
1731 H HA   . GLU   A 119 ? 0.732996 0.420889 0.782196 -0.161292   0.0328172   0.164377    131 GLU   B HA   
1732 H HB2  . GLU   A 119 ? 0.826273 0.455071 0.887128 -0.185638   0.0538779   0.167548    131 GLU   B HB2  
1733 H HB3  . GLU   A 119 ? 0.78378  0.472871 0.936714 -0.207975   0.0259412   0.155529    131 GLU   B HB3  
1734 H HG2  . GLU   A 119 ? 0.811893 0.53649  1.03822  -0.207533   0.0794405   0.176426    131 GLU   B HG2  
1735 H HG3  . GLU   A 119 ? 0.856119 0.518366 0.979217 -0.184131   0.106445    0.185308    131 GLU   B HG3  
1736 N N    . ILE   A 120 ? 0.698858 0.479056 0.871895 -0.170223   0.0207116   0.16593     132 ILE   B N    
1737 C CA   . ILE   A 120 ? 0.599227 0.432372 0.839311 -0.169862   0.00932716  0.16884     132 ILE   B CA   
1738 C C    . ILE   A 120 ? 0.6454   0.484279 0.937786 -0.169562   0.0495174   0.178051    132 ILE   B C    
1739 O O    . ILE   A 120 ? 0.635862 0.436866 0.885348 -0.157304   0.0833074   0.181494    132 ILE   B O    
1740 C CB   . ILE   A 120 ? 0.605159 0.446692 0.812216 -0.153495   -0.0104445  0.168871    132 ILE   B CB   
1741 C CG1  . ILE   A 120 ? 0.570583 0.413755 0.730451 -0.151542   -0.0444366  0.162582    132 ILE   B CG1  
1742 C CG2  . ILE   A 120 ? 0.568154 0.456079 0.841839 -0.149268   -0.0196658  0.176605    132 ILE   B CG2  
1743 C CD1  . ILE   A 120 ? 0.606054 0.451438 0.73336  -0.138592   -0.0560201  0.164913    132 ILE   B CD1  
1744 H H    . ILE   A 120 ? 0.706221 0.457119 0.840081 -0.160867   0.0404823   0.168991    132 ILE   B H    
1745 H HA   . ILE   A 120 ? 0.608854 0.46984  0.885294 -0.179735   -0.0117084  0.165314    132 ILE   B HA   
1746 H HB   . ILE   A 120 ? 0.611099 0.42447  0.782844 -0.144812   0.00715029  0.168753    132 ILE   B HB   
1747 H HG12 . ILE   A 120 ? 0.57284  0.444095 0.760921 -0.157142   -0.0639501  0.161388    132 ILE   B HG12 
1748 H HG13 . ILE   A 120 ? 0.606511 0.421297 0.729716 -0.152521   -0.0392808  0.158171    132 ILE   B HG13 
1749 H HG21 . ILE   A 120 ? 0.562102 0.449648 0.815485 -0.140566   -0.0300545  0.178453    132 ILE   B HG21 
1750 H HG22 . ILE   A 120 ? 0.558296 0.476812 0.86625  -0.156269   -0.0390448  0.176417    132 ILE   B HG22 
1751 H HG23 . ILE   A 120 ? 0.581483 0.468266 0.883938 -0.146914   0.00438532  0.180273    132 ILE   B HG23 
1752 H HD11 . ILE   A 120 ? 0.607065 0.426986 0.711565 -0.133312   -0.0394962  0.1633      132 ILE   B HD11 
1753 H HD12 . ILE   A 120 ? 0.58728  0.433048 0.683761 -0.136573   -0.0717293  0.161752    132 ILE   B HD12 
1754 H HD13 . ILE   A 120 ? 0.5736   0.444875 0.734822 -0.137213   -0.0638561  0.171212    132 ILE   B HD13 
1755 N N    . GLU   A 121 ? 0.634255 0.5251   1.02021  -0.180763   0.0438932   0.181004    133 GLU   B N    
1756 C CA   . GLU   A 121 ? 0.628175 0.543205 1.08162  -0.175388   0.0778469   0.190818    133 GLU   B CA   
1757 C C    . GLU   A 121 ? 0.60327  0.560443 1.09475  -0.158759   0.0565113   0.194439    133 GLU   B C    
1758 O O    . GLU   A 121 ? 0.56721  0.570428 1.09921  -0.163045   0.0160295   0.193593    133 GLU   B O    
1759 C CB   . GLU   A 121 ? 0.620662 0.56877  1.16514  -0.199711   0.0886922   0.193266    133 GLU   B CB   
1760 C CG   . GLU   A 121 ? 0.62201  0.608032 1.2527   -0.193103   0.126667    0.205158    133 GLU   B CG   
1761 C CD   . GLU   A 121 ? 0.630524 0.647446 1.35807  -0.219458   0.149928    0.210351    133 GLU   B CD   
1762 O OE1  . GLU   A 121 ? 0.657906 0.652295 1.37801  -0.245044   0.141642    0.204439    133 GLU   B OE1  
1763 O OE2  . GLU   A 121 ? 0.610664 0.670524 1.42134  -0.213152   0.180024    0.220713    133 GLU   B OE2  
1764 H H    . GLU   A 121 ? 0.615882 0.529396 1.02441  -0.190524   0.0173006   0.175877    133 GLU   B H    
1765 H HA   . GLU   A 121 ? 0.655555 0.535361 1.06999  -0.165963   0.109253    0.193816    133 GLU   B HA   
1766 H HB2  . GLU   A 121 ? 0.650483 0.563293 1.16725  -0.20989    0.105824    0.193426    133 GLU   B HB2  
1767 H HB3  . GLU   A 121 ? 0.602909 0.58304  1.17905  -0.209221   0.053381    0.186647    133 GLU   B HB3  
1768 H HG2  . GLU   A 121 ? 0.596135 0.620529 1.26347  -0.183573   0.10557     0.205511    133 GLU   B HG2  
1769 H HG3  . GLU   A 121 ? 0.643806 0.596831 1.23228  -0.178302   0.159018    0.209768    133 GLU   B HG3  
1770 N N    . LEU   A 122 ? 0.654252 0.591052 1.12787  -0.137525   0.0833567   0.198295    134 LEU   B N    
1771 C CA   . LEU   A 122 ? 0.617822 0.585535 1.1337   -0.119514   0.0701102   0.204729    134 LEU   B CA   
1772 C C    . LEU   A 122 ? 0.627917 0.648271 1.25075  -0.115657   0.090743    0.214085    134 LEU   B C    
1773 O O    . LEU   A 122 ? 0.68553  0.692015 1.32292  -0.106642   0.139178    0.216586    134 LEU   B O    
1774 C CB   . LEU   A 122 ? 0.637536 0.554696 1.09014  -0.099054   0.0855142   0.20063     134 LEU   B CB   
1775 C CG   . LEU   A 122 ? 0.602795 0.53608  1.09351  -0.079307   0.0747043   0.208683    134 LEU   B CG   
1776 C CD1  . LEU   A 122 ? 0.561364 0.535221 1.0734   -0.0837441  0.0259556   0.218794    134 LEU   B CD1  
1777 C CD2  . LEU   A 122 ? 0.641713 0.514787 1.06719  -0.0650427  0.086593    0.19893     134 LEU   B CD2  
1778 H H    . LEU   A 122 ? 0.667499 0.567504 1.09934  -0.13276    0.109928    0.196618    134 LEU   B H    
1779 H HA   . LEU   A 122 ? 0.598662 0.587697 1.11743  -0.122886   0.0350631   0.205614    134 LEU   B HA   
1780 H HB2  . LEU   A 122 ? 0.629877 0.521609 1.02373  -0.103497   0.0698903   0.194556    134 LEU   B HB2  
1781 H HB3  . LEU   A 122 ? 0.661383 0.554937 1.10144  -0.093376   0.119726    0.197943    134 LEU   B HB3  
1782 H HG   . LEU   A 122 ? 0.614497 0.57141  1.16248  -0.0708949  0.0933681   0.214254    134 LEU   B HG   
1783 H HD11 . LEU   A 122 ? 0.550018 0.565473 1.11222  -0.0895929  0.016441    0.222798    134 LEU   B HD11 
1784 H HD12 . LEU   A 122 ? 0.566839 0.539959 1.09085  -0.0699398  0.021101    0.226372    134 LEU   B HD12 
1785 H HD13 . LEU   A 122 ? 0.555818 0.514082 1.01847  -0.0931814  0.00972882  0.213898    134 LEU   B HD13 
1786 H HD21 . LEU   A 122 ? 0.670338 0.517389 1.07554  -0.05914    0.116866    0.191394    134 LEU   B HD21 
1787 H HD22 . LEU   A 122 ? 0.633429 0.488657 1.01013  -0.0734788  0.0679025   0.193785    134 LEU   B HD22 
1788 H HD23 . LEU   A 122 ? 0.641795 0.519352 1.09472  -0.0526486  0.0824555   0.204958    134 LEU   B HD23 
1789 N N    . LEU   A 123 ? 0.590167 0.674689 1.28777  -0.12043    0.0538298   0.219106    135 LEU   B N    
1790 C CA   . LEU   A 123 ? 0.555439 0.704959 1.37014  -0.11868    0.0655465   0.227151    135 LEU   B CA   
1791 C C    . LEU   A 123 ? 0.573686 0.736153 1.42271  -0.0846502  0.0773734   0.238811    135 LEU   B C    
1792 O O    . LEU   A 123 ? 0.588103 0.761217 1.48964  -0.0711841  0.12172     0.243879    135 LEU   B O    
1793 C CB   . LEU   A 123 ? 0.548661 0.763505 1.42704  -0.135938   0.0139029   0.224022    135 LEU   B CB   
1794 C CG   . LEU   A 123 ? 0.571314 0.76929  1.41843  -0.168876   -0.00407779 0.208613    135 LEU   B CG   
1795 C CD1  . LEU   A 123 ? 0.574278 0.831984 1.46947  -0.180656   -0.0642349  0.199573    135 LEU   B CD1  
1796 C CD2  . LEU   A 123 ? 0.572604 0.760824 1.46272  -0.191055   0.0436752   0.207986    135 LEU   B CD2  
1797 H H    . LEU   A 123 ? 0.569533 0.660136 1.24533  -0.123548   0.0200641   0.217405    135 LEU   B H    
1798 H HA   . LEU   A 123 ? 0.584647 0.725886 1.41523  -0.127169   0.100707    0.226625    135 LEU   B HA   
1799 H HB2  . LEU   A 123 ? 0.538238 0.762747 1.39919  -0.123451   -0.0177004  0.227583    135 LEU   B HB2  
1800 H HB3  . LEU   A 123 ? 0.548852 0.811948 1.51281  -0.13571    0.0208292   0.228567    135 LEU   B HB3  
1801 H HG   . LEU   A 123 ? 0.567953 0.718844 1.33181  -0.167052   -0.00691597 0.204757    135 LEU   B HG   
1802 H HD11 . LEU   A 123 ? 0.5608   0.823763 1.42446  -0.164397   -0.0911621  0.20352     135 LEU   B HD11 
1803 H HD12 . LEU   A 123 ? 0.576859 0.816081 1.4466   -0.200238   -0.0750109  0.187207    135 LEU   B HD12 
1804 H HD13 . LEU   A 123 ? 0.568431 0.876964 1.55059  -0.183689   -0.0650651  0.201963    135 LEU   B HD13 
1805 H HD21 . LEU   A 123 ? 0.594519 0.743026 1.44398  -0.180698   0.0813433   0.213324    135 LEU   B HD21 
1806 H HD22 . LEU   A 123 ? 0.576602 0.815758 1.55621  -0.194326   0.0479612   0.212041    135 LEU   B HD22 
1807 H HD23 . LEU   A 123 ? 0.585947 0.756247 1.455    -0.211389   0.0327654   0.198753    135 LEU   B HD23 
1808 N N    . ASP   A 124 ? 0.562936 0.722096 1.38229  -0.069093   0.0402868   0.244739    136 ASP   B N    
1809 C CA   . ASP   A 124 ? 0.583014 0.743643 1.43039  -0.0354536  0.0480233   0.257748    136 ASP   B CA   
1810 C C    . ASP   A 124 ? 0.5776   0.700925 1.35481  -0.0260443  0.0170732   0.263997    136 ASP   B C    
1811 O O    . ASP   A 124 ? 0.557648 0.676844 1.28324  -0.0431692  -0.0159058  0.260935    136 ASP   B O    
1812 C CB   . ASP   A 124 ? 0.59038  0.835492 1.55645  -0.0215483  0.0331561   0.271311    136 ASP   B CB   
1813 C CG   . ASP   A 124 ? 0.630563 0.879501 1.64889  0.0169852   0.0620088   0.284051    136 ASP   B CG   
1814 O OD1  . ASP   A 124 ? 0.696564 0.903483 1.67229  0.0393195   0.0550688   0.29227     136 ASP   B OD1  
1815 O OD2  . ASP   A 124 ? 0.68001  0.971943 1.7849   0.0252706   0.094655    0.286192    136 ASP   B OD2  
1816 H H    . ASP   A 124 ? 0.551995 0.705622 1.33252  -0.0788222  0.0113158   0.241764    136 ASP   B H    
1817 H HA   . ASP   A 124 ? 0.606732 0.734942 1.44176  -0.0261747  0.0859515   0.253872    136 ASP   B HA   
1818 H HB2  . ASP   A 124 ? 0.583922 0.861762 1.59799  -0.0371697  0.0425456   0.266354    136 ASP   B HB2  
1819 H HB3  . ASP   A 124 ? 0.577019 0.847554 1.54443  -0.0214499  -0.00751475 0.276984    136 ASP   B HB3  
1820 N N    . PHE   A 125 ? 0.613993 0.707099 1.39147  0.0017441   0.0315557   0.273166    137 PHE   B N    
1821 C CA   . PHE   A 125 ? 0.659039 0.71892  1.3897   0.0112624   0.00674718  0.285261    137 PHE   B CA   
1822 C C    . PHE   A 125 ? 0.686109 0.745793 1.47011  0.047449    0.015521    0.304017    137 PHE   B C    
1823 O O    . PHE   A 125 ? 0.786723 0.825715 1.59698  0.0650747   0.0549314   0.296748    137 PHE   B O    
1824 C CB   . PHE   A 125 ? 0.679469 0.663336 1.3159   -0.00266755 0.0183039   0.269308    137 PHE   B CB   
1825 C CG   . PHE   A 125 ? 0.724552 0.647998 1.33477  0.00669786  0.062728    0.250549    137 PHE   B CG   
1826 C CD1  . PHE   A 125 ? 0.707848 0.620411 1.29509  -0.00360622 0.0927502   0.231831    137 PHE   B CD1  
1827 C CD2  . PHE   A 125 ? 0.731883 0.603513 1.33463  0.0275025   0.075182    0.251362    137 PHE   B CD2  
1828 C CE1  . PHE   A 125 ? 0.758652 0.61433  1.30843  0.00982275  0.132718    0.213999    137 PHE   B CE1  
1829 C CE2  . PHE   A 125 ? 0.778724 0.591921 1.35019  0.0388808   0.113085    0.228942    137 PHE   B CE2  
1830 C CZ   . PHE   A 125 ? 0.809453 0.616614 1.35087  0.0317477   0.141514    0.21        137 PHE   B CZ   
1831 H H    . PHE   A 125 ? 0.63738  0.727847 1.44598  0.0152679   0.0601358   0.272213    137 PHE   B H    
1832 H HA   . PHE   A 125 ? 0.632633 0.723919 1.36248  0.004173    -0.0256885  0.292978    137 PHE   B HA   
1833 H HB2  . PHE   A 125 ? 0.684239 0.65228  1.30112  0.00115418  0.00200848  0.27974     137 PHE   B HB2  
1834 H HB3  . PHE   A 125 ? 0.659711 0.648899 1.26587  -0.0222078  0.00937451  0.260431    137 PHE   B HB3  
1835 H HD1  . PHE   A 125 ? 0.690348 0.631203 1.2836   -0.0188645  0.0862306   0.231359    137 PHE   B HD1  
1836 H HD2  . PHE   A 125 ? 0.741354 0.615484 1.35971  0.0353804   0.0580113   0.267376    137 PHE   B HD2  
1837 H HE1  . PHE   A 125 ? 0.771349 0.6192   1.30026  0.00517566  0.154749    0.204425    137 PHE   B HE1  
1838 H HE2  . PHE   A 125 ? 0.819189 0.593091 1.38614  0.0526003   0.119716    0.226808    137 PHE   B HE2  
1839 H HZ   . PHE   A 125 ? 0.842987 0.608668 1.35364  0.0419592   0.167025    0.194183    137 PHE   B HZ   
1840 N N    . LYS   A 126 ? 0.679864 0.761277 1.47618  0.0618149   -0.0197768  0.329493    138 LYS   B N    
1841 C CA   . LYS   A 126 ? 0.685181 0.767885 1.53275  0.100242    -0.0175903  0.353877    138 LYS   B CA   
1842 C C    . LYS   A 126 ? 0.697257 0.720688 1.48851  0.105983    -0.0294837  0.373115    138 LYS   B C    
1843 O O    . LYS   A 126 ? 0.629456 0.646388 1.36304  0.0844561   -0.0525176  0.376471    138 LYS   B O    
1844 C CB   . LYS   A 126 ? 0.656772 0.833434 1.5875   0.117219    -0.0494577  0.372125    138 LYS   B CB   
1845 H H    . LYS   A 126 ? 0.658704 0.752606 1.42671  0.0491587   -0.0455804  0.33303     138 LYS   B H    
1846 H HA   . LYS   A 126 ? 0.705914 0.76476  1.57185  0.111985    0.0146697   0.344872    138 LYS   B HA   
1849 N N    . GLY   A 127 ? 0.781197 0.760019 1.59434  0.136442    -0.0104944  0.387105    139 GLY   B N    
1850 C CA   . GLY   A 127 ? 0.849037 0.76203  1.61972  0.140325    -0.0148119  0.407282    139 GLY   B CA   
1851 C C    . GLY   A 127 ? 0.861834 0.817218 1.63776  0.155091    -0.0531756  0.448528    139 GLY   B C    
1852 O O    . GLY   A 127 ? 0.85789  0.879484 1.69069  0.181692    -0.0721712  0.46566     139 GLY   B O    
1853 H H    . GLY   A 127 ? 0.791498 0.779629 1.64948  0.155256    0.00718567  0.384499    139 GLY   B H    
1854 H HA2  . GLY   A 127 ? 0.83431  0.714471 1.55458  0.114765    -0.0122153  0.392657    139 GLY   B HA2  
1855 H HA3  . GLY   A 127 ? 0.883823 0.754392 1.67154  0.159779    0.00606925  0.408644    139 GLY   B HA3  
1856 N N    . GLU   A 128 ? 0.897023 0.819168 1.61284  0.137796    -0.0646857  0.463539    140 GLU   B N    
1857 C CA   . GLU   A 128 ? 0.95327  0.886923 1.66101  0.159563    -0.0888211  0.510327    140 GLU   B CA   
1858 C C    . GLU   A 128 ? 0.98184  0.903282 1.74928  0.206889    -0.0811298  0.538696    140 GLU   B C    
1859 O O    . GLU   A 128 ? 0.968332 0.847334 1.77008  0.216704    -0.0491965  0.51891     140 GLU   B O    
1860 C CB   . GLU   A 128 ? 0.996845 0.872709 1.64282  0.136186    -0.0828442  0.524041    140 GLU   B CB   
1861 O OXT  . GLU   A 128 ? 1.01085  0.966435 1.78596  0.236649    -0.107456   0.579291    140 GLU   B OXT  
1862 H H    . GLU   A 128 ? 0.882494 0.776065 1.56151  0.113036    -0.0563899  0.445523    140 GLU   B H    
1863 H HA   . GLU   A 128 ? 0.924444 0.917709 1.63025  0.15998     -0.114968   0.514012    140 GLU   B HA   
1866 N N    . THR   B 5   ? 1.19815  0.901828 0.876908 0.220674    0.0627715   -0.0542603  17  THR   A N    
1867 C CA   . THR   B 5   ? 1.20628  0.909555 0.894808 0.182391    0.0364086   -0.0340292  17  THR   A CA   
1868 C C    . THR   B 5   ? 1.21019  0.857241 0.895502 0.174483    0.00591145  -0.0357638  17  THR   A C    
1869 O O    . THR   B 5   ? 1.19461  0.80878  0.884433 0.199378    0.00466278  -0.0464596  17  THR   A O    
1870 C CB   . THR   B 5   ? 1.14     0.910955 0.888732 0.169494    0.0453843   -0.00788983 17  THR   A CB   
1871 O OG1  . THR   B 5   ? 1.09772  0.885071 0.897297 0.182587    0.043988    -0.00240033 17  THR   A OG1  
1872 C CG2  . THR   B 5   ? 1.09212  0.914813 0.84759  0.174607    0.076039    -0.00228206 17  THR   A CG2  
1873 H H    . THR   B 5   ? 1.2159   0.946099 0.885131 0.222227    0.0797086   -0.0542288  17  THR   A H    
1874 H HA   . THR   B 5   ? 1.2127   0.90645  0.865838 0.169       0.0326546   -0.0366141  17  THR   A HA   
1875 H HB   . THR   B 5   ? 1.10321  0.872719 0.851731 0.146749    0.0306115   0.00308824  17  THR   A HB   
1877 H HG21 . THR   B 5   ? 1.0547   0.912006 0.847377 0.164018    0.0793687   0.0133233   17  THR   A HG21 
1878 H HG22 . THR   B 5   ? 1.12492  0.956049 0.882897 0.196874    0.092647    -0.0122854  17  THR   A HG22 
1879 H HG23 . THR   B 5   ? 1.12119  0.934443 0.840899 0.165813    0.0757671   -0.00354566 17  THR   A HG23 
1880 N N    . VAL   B 6   ? 1.18172  0.818832 0.858533 0.139624    -0.0183158  -0.0231812  18  VAL   A N    
1881 C CA   . VAL   B 6   ? 1.16999  0.760624 0.842357 0.121588    -0.0480582  -0.0188129  18  VAL   A CA   
1882 C C    . VAL   B 6   ? 1.1116   0.749758 0.83894  0.105362    -0.0540576  0.00821564  18  VAL   A C    
1883 O O    . VAL   B 6   ? 1.06311  0.759582 0.821249 0.102464    -0.0388577  0.0202274   18  VAL   A O    
1884 C CB   . VAL   B 6   ? 1.22887  0.777163 0.849789 0.0914172   -0.0716824  -0.0253864  18  VAL   A CB   
1885 C CG1  . VAL   B 6   ? 1.2859   0.768102 0.843731 0.104974    -0.0721272  -0.0572508  18  VAL   A CG1  
1886 C CG2  . VAL   B 6   ? 1.24226  0.840877 0.862173 0.0680226   -0.0710815  -0.0116528  18  VAL   A CG2  
1887 H H    . VAL   B 6   ? 1.1536   0.817568 0.828684 0.126273    -0.0152191  -0.0152475  18  VAL   A H    
1888 H HA   . VAL   B 6   ? 1.21735  0.774954 0.886693 0.13977     -0.0489155  -0.028187   18  VAL   A HA   
1889 H HB   . VAL   B 6   ? 1.22741  0.756157 0.856079 0.0761516   -0.0898327  -0.016871   18  VAL   A HB   
1890 H HG11 . VAL   B 6   ? 1.3027   0.80507  0.8493   0.120339    -0.05323    -0.0659487  18  VAL   A HG11 
1891 H HG12 . VAL   B 6   ? 1.32976  0.774721 0.888223 0.121267    -0.0734563  -0.0653171  18  VAL   A HG12 
1892 H HG13 . VAL   B 6   ? 1.32535  0.782602 0.85266  0.0819072   -0.0899409  -0.0607777  18  VAL   A HG13 
1893 H HG21 . VAL   B 6   ? 1.25427  0.830551 0.844639 0.0489402   -0.0879785  -0.0151457  18  VAL   A HG21 
1894 H HG22 . VAL   B 6   ? 1.17076  0.804042 0.827369 0.0592815   -0.0717354  0.00640109  18  VAL   A HG22 
1895 H HG23 . VAL   B 6   ? 1.22626  0.844694 0.837933 0.0812104   -0.0533045  -0.0169238  18  VAL   A HG23 
1896 N N    . THR   B 7   ? 1.09628  0.706058 0.833707 0.0958215   -0.0751867  0.0173106   19  THR   A N    
1897 C CA   . THR   B 7   ? 1.06784  0.718601 0.848218 0.0785752   -0.0827405  0.0411922   19  THR   A CA   
1898 C C    . THR   B 7   ? 0.95561  0.631247 0.731101 0.0458149   -0.0909844  0.0529691   19  THR   A C    
1899 O O    . THR   B 7   ? 0.924764 0.653693 0.730178 0.0399311   -0.0805466  0.0648448   19  THR   A O    
1900 C CB   . THR   B 7   ? 1.09318  0.705377 0.878233 0.0762581   -0.103362   0.0502597   19  THR   A CB   
1901 O OG1  . THR   B 7   ? 1.11162  0.681492 0.889528 0.109197    -0.100394   0.0375809   19  THR   A OG1  
1902 C CG2  . THR   B 7   ? 0.987039 0.649186 0.815562 0.0649158   -0.106838   0.0728902   19  THR   A CG2  
1903 H H    . THR   B 7   ? 1.15825  0.720092 0.872844 0.100029    -0.084836   0.00835724  19  THR   A H    
1904 H HA   . THR   B 7   ? 1.01189  0.701561 0.821584 0.0903153   -0.0684949  0.0446102   19  THR   A HA   
1905 H HB   . THR   B 7   ? 1.10276  0.683869 0.86368  0.0564133   -0.118559   0.0512981   19  THR   A HB   
1907 H HG21 . THR   B 7   ? 1.01961  0.658612 0.849315 0.0651136   -0.119296   0.0803287   19  THR   A HG21 
1908 H HG22 . THR   B 7   ? 0.970334 0.668657 0.82401  0.0789246   -0.0929981  0.0723232   19  THR   A HG22 
1909 H HG23 . THR   B 7   ? 0.973738 0.655052 0.802614 0.0433555   -0.110472   0.0805431   19  THR   A HG23 
1910 N N    . GLU   B 8   ? 1.02317  0.659644 0.760566 0.0249597   -0.109858   0.0488541   20  GLU   A N    
1911 C CA   . GLU   B 8   ? 1.01197  0.674878 0.746634 -0.00555132 -0.121156   0.061458    20  GLU   A CA   
1912 C C    . GLU   B 8   ? 0.90511  0.594367 0.623004 -0.00213073 -0.108659   0.0557308   20  GLU   A C    
1913 O O    . GLU   B 8   ? 0.935261 0.613807 0.620174 -0.0203016  -0.122728   0.052528    20  GLU   A O    
1914 C CB   . GLU   B 8   ? 1.13007  0.746843 0.83333  -0.0338441  -0.148764   0.0610753   20  GLU   A CB   
1915 C CG   . GLU   B 8   ? 1.256    0.828563 0.963272 -0.0384373  -0.163427   0.067325    20  GLU   A CG   
1916 C CD   . GLU   B 8   ? 1.22401  0.836177 0.975479 -0.0409884  -0.161722   0.0902532   20  GLU   A CD   
1917 O OE1  . GLU   B 8   ? 1.07368  0.749736 0.856023 -0.0447144  -0.150924   0.102068    20  GLU   A OE1  
1918 O OE2  . GLU   B 8   ? 1.25518  0.827167 1.00587  -0.0374351  -0.171796   0.0953741   20  GLU   A OE2  
1919 H H    . GLU   B 8   ? 1.07226  0.663906 0.784845 0.0302407   -0.116298   0.0373773   20  GLU   A H    
1920 H HA   . GLU   B 8   ? 0.955646 0.653164 0.72083  -0.0114052  -0.119271   0.0758611   20  GLU   A HA   
1921 H HB2  . GLU   B 8   ? 1.17824  0.763773 0.84758  -0.0317022  -0.151425   0.0454496   20  GLU   A HB2  
1922 H HB3  . GLU   B 8   ? 1.11305  0.759293 0.824668 -0.0537239  -0.15572    0.0731104   20  GLU   A HB3  
1923 H HG2  . GLU   B 8   ? 1.26923  0.806311 0.964665 -0.0175131  -0.158644   0.0543951   20  GLU   A HG2  
1924 H HG3  . GLU   B 8   ? 1.27259  0.817553 0.959835 -0.0608937  -0.180731   0.0684317   20  GLU   A HG3  
1925 N N    . GLN   B 9   ? 0.873119 0.596775 0.612022 0.0192662   -0.0836934  0.0557267   21  GLN   A N    
1926 C CA   . GLN   B 9   ? 0.947273 0.701752 0.675642 0.022229    -0.0693466  0.0577169   21  GLN   A CA   
1927 C C    . GLN   B 9   ? 0.908875 0.715169 0.677078 0.0134481   -0.0630352  0.0794455   21  GLN   A C    
1928 O O    . GLN   B 9   ? 0.879689 0.70077  0.684445 0.0103051   -0.0637927  0.0878921   21  GLN   A O    
1929 C CB   . GLN   B 9   ? 0.984138 0.748859 0.717469 0.0495088   -0.0417615  0.0484457   21  GLN   A CB   
1930 C CG   . GLN   B 9   ? 0.931923 0.723444 0.717544 0.0594947   -0.0300833  0.0558262   21  GLN   A CG   
1931 C CD   . GLN   B 9   ? 1.06421  0.88089  0.865027 0.0812381   -0.00228212 0.0511553   21  GLN   A CD   
1932 O OE1  . GLN   B 9   ? 1.11142  0.926759 0.881966 0.0904412   0.0117246   0.0435777   21  GLN   A OE1  
1933 N NE2  . GLN   B 9   ? 0.988269 0.830346 0.834326 0.0880113   0.00468317  0.0559282   21  GLN   A NE2  
1934 H H    . GLN   B 9   ? 0.877666 0.607116 0.638863 0.0312258   -0.0757981  0.0562455   21  GLN   A H    
1935 H HA   . GLN   B 9   ? 0.97195  0.711561 0.667881 0.0131419   -0.0795857  0.0528201   21  GLN   A HA   
1936 H HB2  . GLN   B 9   ? 0.968374 0.754245 0.695947 0.0499112   -0.0315925  0.0532891   21  GLN   A HB2  
1937 H HB3  . GLN   B 9   ? 1.0182   0.752427 0.725561 0.0601749   -0.0414348  0.0329221   21  GLN   A HB3  
1938 H HG2  . GLN   B 9   ? 0.971503 0.741857 0.760517 0.0621397   -0.0396681  0.0517932   21  GLN   A HG2  
1939 H HG3  . GLN   B 9   ? 0.924566 0.740192 0.732464 0.0479806   -0.0319225  0.0687292   21  GLN   A HG3  
1940 H HE21 . GLN   B 9   ? 0.996159 0.858214 0.8566   0.0987791   0.0204538   0.0544028   21  GLN   A HE21 
1941 H HE22 . GLN   B 9   ? 0.983005 0.824352 0.844533 0.0808495   -0.00675389 0.0610442   21  GLN   A HE22 
1942 N N    . GLY   B 10  ? 0.818831 0.650169 0.578419 0.0126649   -0.0551478  0.087772    22  GLY   A N    
1943 C CA   . GLY   B 10  ? 0.793218 0.663922 0.585274 0.0057746   -0.0515664  0.107687    22  GLY   A CA   
1944 C C    . GLY   B 10  ? 0.717706 0.602314 0.499747 -0.0124958  -0.0722704  0.119478    22  GLY   A C    
1945 O O    . GLY   B 10  ? 0.752731 0.616847 0.507194 -0.0268516  -0.0933577  0.112907    22  GLY   A O    
1946 H H    . GLY   B 10  ? 0.872826 0.695195 0.604654 0.0176442   -0.0518471  0.0811522   22  GLY   A H    
1947 H HA2  . GLY   B 10  ? 0.762963 0.646742 0.557898 0.0146539   -0.0361725  0.111837    22  GLY   A HA2  
1948 H HA3  . GLY   B 10  ? 0.742864 0.620591 0.562378 0.00482297  -0.0499871  0.110179    22  GLY   A HA3  
1949 N N    . GLU   B 11  ? 0.697911 0.6184   0.502974 -0.0113483  -0.0656939  0.137403    23  GLU   A N    
1950 C CA   . GLU   B 11  ? 0.663683 0.612025 0.469544 -0.0239141  -0.0825167  0.152609    23  GLU   A CA   
1951 C C    . GLU   B 11  ? 0.627953 0.592479 0.464545 -0.0377742  -0.0927579  0.158469    23  GLU   A C    
1952 O O    . GLU   B 11  ? 0.606258 0.577521 0.472959 -0.0315067  -0.0795785  0.159218    23  GLU   A O    
1953 C CB   . GLU   B 11  ? 0.723568 0.700598 0.544271 -0.00996996 -0.0675388  0.170546    23  GLU   A CB   
1954 C CG   . GLU   B 11  ? 0.821719 0.836596 0.646756 -0.015376   -0.0827893  0.190221    23  GLU   A CG   
1955 C CD   . GLU   B 11  ? 0.815656 0.854042 0.665888 0.00322919  -0.0660675  0.210219    23  GLU   A CD   
1956 O OE1  . GLU   B 11  ? 0.939411 0.961178 0.800708 0.0165858   -0.0429243  0.209001    23  GLU   A OE1  
1957 O OE2  . GLU   B 11  ? 0.802836 0.87709  0.665219 0.00394147  -0.0767987  0.227988    23  GLU   A OE2  
1958 H H    . GLU   B 11  ? 0.67026  0.598671 0.49261  -0.00180506 -0.0500233  0.140559    23  GLU   A H    
1959 H HA   . GLU   B 11  ? 0.712978 0.651272 0.489725 -0.0318587  -0.0960391  0.14801     23  GLU   A HA   
1960 H HB2  . GLU   B 11  ? 0.742116 0.708027 0.543757 -0.00152613 -0.0582944  0.168002    23  GLU   A HB2  
1961 H HB3  . GLU   B 11  ? 0.697963 0.680379 0.54586  -0.00421392 -0.0553762  0.172843    23  GLU   A HB3  
1962 H HG2  . GLU   B 11  ? 0.787883 0.816025 0.628032 -0.026557   -0.0936768  0.191802    23  GLU   A HG2  
1963 H HG3  . GLU   B 11  ? 0.830508 0.842641 0.626308 -0.020138   -0.0938227  0.18926     23  GLU   A HG3  
1964 N N    . ASP   B 12  ? 0.619542 0.592326 0.446475 -0.058885   -0.116455   0.162723    24  ASP   A N    
1965 C CA   . ASP   B 12  ? 0.662279 0.658641 0.516677 -0.0753405  -0.126013   0.172402    24  ASP   A CA   
1966 C C    . ASP   B 12  ? 0.641407 0.693119 0.529154 -0.0674441  -0.118212   0.191562    24  ASP   A C    
1967 O O    . ASP   B 12  ? 0.574591 0.655064 0.458199 -0.0687877  -0.127715   0.203209    24  ASP   A O    
1968 C CB   . ASP   B 12  ? 0.670596 0.657156 0.503825 -0.104182   -0.153776   0.171762    24  ASP   A CB   
1969 C CG   . ASP   B 12  ? 0.67407  0.68984  0.534973 -0.125906   -0.163693   0.185526    24  ASP   A CG   
1970 O OD1  . ASP   B 12  ? 0.598845 0.643852 0.492705 -0.115589   -0.14785    0.193691    24  ASP   A OD1  
1971 O OD2  . ASP   B 12  ? 0.654202 0.661916 0.500828 -0.154511   -0.186822   0.187297    24  ASP   A OD2  
1972 H H    . ASP   B 12  ? 0.669115 0.634064 0.470583 -0.0646539  -0.12697    0.159689    24  ASP   A H    
1973 H HA   . ASP   B 12  ? 0.632019 0.61527  0.49679  -0.0721405  -0.118645   0.167426    24  ASP   A HA   
1974 H HB2  . ASP   B 12  ? 0.707619 0.652007 0.517468 -0.106096   -0.157583   0.15817     24  ASP   A HB2  
1975 H HB3  . ASP   B 12  ? 0.696493 0.698467 0.518306 -0.108314   -0.162582   0.175898    24  ASP   A HB3  
1976 N N    . ILE   B 13  ? 0.570374 0.635439 0.489095 -0.0567723  -0.100682   0.193787    25  ILE   A N    
1977 C CA   . ILE   B 13  ? 0.593896 0.702762 0.543504 -0.0432154  -0.0888828  0.208282    25  ILE   A CA   
1978 C C    . ILE   B 13  ? 0.529518 0.680693 0.505461 -0.056465   -0.0943687  0.218175    25  ILE   A C    
1979 O O    . ILE   B 13  ? 0.53014  0.71882  0.534048 -0.0422412  -0.0816636  0.227676    25  ILE   A O    
1980 C CB   . ILE   B 13  ? 0.567276 0.66025  0.529539 -0.0208071  -0.0630755  0.202163    25  ILE   A CB   
1981 C CG1  . ILE   B 13  ? 0.579404 0.652044 0.547236 -0.0257559  -0.0563447  0.187901    25  ILE   A CG1  
1982 C CG2  . ILE   B 13  ? 0.647646 0.712745 0.589117 -0.0074647  -0.0545361  0.199793    25  ILE   A CG2  
1983 C CD1  . ILE   B 13  ? 0.593361 0.659416 0.57836  -0.00951196 -0.033409   0.181801    25  ILE   A CD1  
1984 H H    . ILE   B 13  ? 0.583625 0.629484 0.503148 -0.0573016  -0.0963892  0.185571    25  ILE   A H    
1985 H HA   . ILE   B 13  ? 0.584401 0.707573 0.528902 -0.0398955  -0.0942215  0.21676     25  ILE   A HA   
1986 H HB   . ILE   B 13  ? 0.575499 0.693112 0.557253 -0.0116812  -0.0557345  0.210568    25  ILE   A HB   
1987 H HG12 . ILE   B 13  ? 0.589117 0.635515 0.540064 -0.0300765  -0.0612493  0.179598    25  ILE   A HG12 
1988 H HG13 . ILE   B 13  ? 0.573099 0.663323 0.549122 -0.0361831  -0.0629299  0.191215    25  ILE   A HG13 
1989 H HG21 . ILE   B 13  ? 0.62007  0.677535 0.572615 0.00399575  -0.0385583  0.198355    25  ILE   A HG21 
1990 H HG22 . ILE   B 13  ? 0.638914 0.680126 0.561489 -0.0133653  -0.0588719  0.189727    25  ILE   A HG22 
1991 H HG23 . ILE   B 13  ? 0.640636 0.720393 0.576046 -0.004776   -0.0606216  0.21039     25  ILE   A HG23 
1992 H HD11 . ILE   B 13  ? 0.580394 0.666502 0.579286 -0.00158604 -0.0271705  0.189119    25  ILE   A HD11 
1993 H HD12 . ILE   B 13  ? 0.575901 0.63769  0.565553 -0.0144221  -0.0317338  0.17408     25  ILE   A HD12 
1994 H HD13 . ILE   B 13  ? 0.591676 0.637813 0.568666 -0.0024847  -0.0266401  0.17847     25  ILE   A HD13 
1995 N N    . THR   B 14  ? 0.570026 0.715905 0.535977 -0.0829872  -0.1128     0.217568    26  THR   A N    
1996 C CA   . THR   B 14  ? 0.59444  0.786674 0.583466 -0.101255   -0.119451   0.231206    26  THR   A CA   
1997 C C    . THR   B 14  ? 0.606097 0.855003 0.610883 -0.107278   -0.131605   0.249135    26  THR   A C    
1998 O O    . THR   B 14  ? 0.625585 0.866165 0.61091  -0.110344   -0.145913   0.24949     26  THR   A O    
1999 C CB   . THR   B 14  ? 0.578155 0.742672 0.550733 -0.130803   -0.136196   0.228972    26  THR   A CB   
2000 O OG1  . THR   B 14  ? 0.600353 0.736014 0.544571 -0.151556   -0.159913   0.226008    26  THR   A OG1  
2001 C CG2  . THR   B 14  ? 0.642807 0.755979 0.601723 -0.122461   -0.12716    0.213989    26  THR   A CG2  
2002 H H    . THR   B 14  ? 0.588283 0.700083 0.532067 -0.0901876  -0.120898   0.209006    26  THR   A H    
2003 H HA   . THR   B 14  ? 0.562916 0.770744 0.569537 -0.0897166  -0.104128   0.231538    26  THR   A HA   
2004 H HB   . THR   B 14  ? 0.586935 0.786168 0.576646 -0.14271    -0.137365   0.24004     26  THR   A HB   
2006 H HG21 . THR   B 14  ? 0.638067 0.734482 0.587896 -0.139697   -0.138101   0.215742    26  THR   A HG21 
2007 H HG22 . THR   B 14  ? 0.627951 0.709868 0.571542 -0.111552   -0.125331   0.203417    26  THR   A HG22 
2008 H HG23 . THR   B 14  ? 0.599868 0.729561 0.574435 -0.1108     -0.112454   0.213791    26  THR   A HG23 
2009 N N    . SER   B 15  ? 0.640164 0.95132  0.679948 -0.108717   -0.125844   0.264111    27  SER   A N    
2010 C CA   . SER   B 15  ? 0.676278 1.05665  0.740611 -0.116729   -0.13847    0.284443    27  SER   A CA   
2011 C C    . SER   B 15  ? 0.666739 1.04913  0.716802 -0.159564   -0.168735   0.289773    27  SER   A C    
2012 O O    . SER   B 15  ? 0.597549 1.01396  0.649616 -0.171331   -0.188851   0.300284    27  SER   A O    
2013 C CB   . SER   B 15  ? 0.719623 1.16762  0.826355 -0.10477    -0.120781   0.297392    27  SER   A CB   
2014 O OG   . SER   B 15  ? 0.780792 1.2337   0.901574 -0.0635582  -0.0993799  0.296285    27  SER   A OG   
2015 H H    . SER   B 15  ? 0.621472 0.935272 0.670646 -0.104129   -0.113246   0.261558    27  SER   A H    
2016 H HA   . SER   B 15  ? 0.677887 1.05985  0.739419 -0.100967   -0.139054   0.286441    27  SER   A HA   
2017 H HB2  . SER   B 15  ? 0.712065 1.14928  0.817327 -0.110957   -0.112605   0.292077    27  SER   A HB2  
2018 H HB3  . SER   B 15  ? 0.723619 1.22251  0.848792 -0.118633   -0.131903   0.312074    27  SER   A HB3  
2020 N N    . LYS   B 16  ? 0.586481 0.930564 0.621119 -0.182822   -0.172738   0.283091    28  LYS   A N    
2021 C CA   . LYS   B 16  ? 0.661894 0.996333 0.682257 -0.227126   -0.20006    0.288355    28  LYS   A CA   
2022 C C    . LYS   B 16  ? 0.651456 0.910363 0.623635 -0.236329   -0.219015   0.26967     28  LYS   A C    
2023 O O    . LYS   B 16  ? 0.742102 0.983983 0.696138 -0.272889   -0.244511   0.270492    28  LYS   A O    
2024 C CB   . LYS   B 16  ? 0.738209 1.05536  0.758544 -0.247463   -0.196585   0.292055    28  LYS   A CB   
2025 C CG   . LYS   B 16  ? 0.760388 1.15751  0.821832 -0.253738   -0.183246   0.313115    28  LYS   A CG   
2026 C CD   . LYS   B 16  ? 0.70012  1.0811   0.75442  -0.282753   -0.185179   0.321984    28  LYS   A CD   
2027 H H    . LYS   B 16  ? 0.604438 0.925802 0.636789 -0.171417   -0.158599   0.275627    28  LYS   A H    
2028 H HA   . LYS   B 16  ? 0.658448 1.04789  0.699496 -0.239852   -0.209552   0.302731    28  LYS   A HA   
2029 H HB2  . LYS   B 16  ? 0.72096  0.996618 0.727919 -0.230025   -0.184897   0.279894    28  LYS   A HB2  
2030 H HB3  . LYS   B 16  ? 0.761652 1.05013  0.763925 -0.275334   -0.215307   0.292277    28  LYS   A HB3  
2031 H HG2  . LYS   B 16  ? 0.734802 1.18368  0.816108 -0.266203   -0.192345   0.32603     28  LYS   A HG2  
2032 H HG3  . LYS   B 16  ? 0.704164 1.11806  0.778651 -0.224779   -0.163011   0.309399    28  LYS   A HG3  
2035 N N    . LYS   B 17  ? 0.63754  0.849217 0.587673 -0.204833   -0.205592   0.25199     29  LYS   A N    
2036 C CA   . LYS   B 17  ? 0.708464 0.850777 0.610906 -0.206785   -0.217655   0.231775    29  LYS   A CA   
2037 C C    . LYS   B 17  ? 0.728215 0.804078 0.603352 -0.231854   -0.230818   0.221249    29  LYS   A C    
2038 O O    . LYS   B 17  ? 0.755934 0.793694 0.598507 -0.25769    -0.254203   0.212834    29  LYS   A O    
2039 C CB   . LYS   B 17  ? 0.760751 0.929329 0.649046 -0.216457   -0.237763   0.235098    29  LYS   A CB   
2040 C CG   . LYS   B 17  ? 0.771291 0.98959  0.679752 -0.183569   -0.223364   0.245881    29  LYS   A CG   
2041 C CD   . LYS   B 17  ? 0.788417 0.957235 0.675699 -0.149028   -0.200667   0.230435    29  LYS   A CD   
2042 C CE   . LYS   B 17  ? 0.878715 1.07971  0.773233 -0.119929   -0.190016   0.241644    29  LYS   A CE   
2043 N NZ   . LYS   B 17  ? 0.855891 1.07755  0.78969  -0.0928322  -0.162677   0.249641    29  LYS   A NZ   
2044 H H    . LYS   B 17  ? 0.618567 0.841752 0.58347  -0.181159   -0.187106   0.252022    29  LYS   A H    
2045 H HA   . LYS   B 17  ? 0.68916  0.809996 0.585717 -0.181125   -0.201609   0.222522    29  LYS   A HA   
2046 H HB2  . LYS   B 17  ? 0.775362 0.975999 0.675337 -0.242371   -0.253807   0.246108    29  LYS   A HB2  
2047 H HB3  . LYS   B 17  ? 0.798031 0.918283 0.649851 -0.220009   -0.245995   0.219662    29  LYS   A HB3  
2048 H HG2  . LYS   B 17  ? 0.736092 0.998141 0.680004 -0.176338   -0.213051   0.259018    29  LYS   A HG2  
2049 H HG3  . LYS   B 17  ? 0.788189 1.02938  0.688575 -0.192487   -0.239363   0.251126    29  LYS   A HG3  
2050 H HD2  . LYS   B 17  ? 0.833856 0.95678  0.686516 -0.155714   -0.208094   0.215522    29  LYS   A HD2  
2051 H HD3  . LYS   B 17  ? 0.779578 0.937042 0.681132 -0.139146   -0.184821   0.227549    29  LYS   A HD3  
2052 H HE2  . LYS   B 17  ? 0.866923 1.10911  0.768523 -0.128245   -0.204493   0.254279    29  LYS   A HE2  
2053 H HE3  . LYS   B 17  ? 0.875789 1.04217  0.74131  -0.110688   -0.186541   0.231349    29  LYS   A HE3  
2054 H HZ1  . LYS   B 17  ? 0.833326 1.08531  0.791547 -0.100653   -0.163841   0.257169    29  LYS   A HZ1  
2055 H HZ2  . LYS   B 17  ? 0.840739 1.02644  0.7672   -0.0851707  -0.150146   0.238059    29  LYS   A HZ2  
2056 H HZ3  . LYS   B 17  ? 0.8455   1.08574  0.786096 -0.0757021  -0.156875   0.258736    29  LYS   A HZ3  
2057 N N    . ASP   B 18  ? 0.778789 0.834372 0.663783 -0.222317   -0.215878   0.220631    30  ASP   A N    
2058 C CA   . ASP   B 18  ? 0.80469  0.796619 0.667313 -0.240299   -0.226538   0.215256    30  ASP   A CA   
2059 C C    . ASP   B 18  ? 0.927217 0.856141 0.76861  -0.210071   -0.213261   0.194931    30  ASP   A C    
2060 O O    . ASP   B 18  ? 0.8773   0.760443 0.709301 -0.213313   -0.215978   0.193485    30  ASP   A O    
2061 C CB   . ASP   B 18  ? 0.869902 0.894107 0.76017  -0.256903   -0.223215   0.23594     30  ASP   A CB   
2062 C CG   . ASP   B 18  ? 0.738478 0.803269 0.658135 -0.228489   -0.196139   0.240169    30  ASP   A CG   
2063 O OD1  . ASP   B 18  ? 0.738947 0.788662 0.656079 -0.195567   -0.179637   0.225173    30  ASP   A OD1  
2064 O OD2  . ASP   B 18  ? 0.692201 0.808807 0.637311 -0.241214   -0.191266   0.258468    30  ASP   A OD2  
2065 H H    . ASP   B 18  ? 0.722238 0.802996 0.627591 -0.20336    -0.198894   0.223961    30  ASP   A H    
2066 H HA   . ASP   B 18  ? 0.881635 0.850308 0.723854 -0.262522   -0.245351   0.212342    30  ASP   A HA   
2067 H HB2  . ASP   B 18  ? 0.862681 0.841078 0.736487 -0.268341   -0.23123    0.234732    30  ASP   A HB2  
2068 H HB3  . ASP   B 18  ? 0.834656 0.900111 0.738942 -0.278431   -0.232221   0.249297    30  ASP   A HB3  
2069 N N    . ARG   B 19  ? 0.799069 0.731802 0.636563 -0.18007    -0.198083   0.182537    31  ARG   A N    
2070 C CA   . ARG   B 19  ? 0.764694 0.652743 0.588116 -0.150645   -0.18289    0.16441     31  ARG   A CA   
2071 C C    . ARG   B 19  ? 0.739618 0.628967 0.586142 -0.139273   -0.169767   0.168884    31  ARG   A C    
2072 O O    . ARG   B 19  ? 0.807986 0.654564 0.643657 -0.122993   -0.164889   0.156884    31  ARG   A O    
2073 C CB   . ARG   B 19  ? 0.817335 0.633461 0.596062 -0.151258   -0.19455    0.143868    31  ARG   A CB   
2074 C CG   . ARG   B 19  ? 0.947577 0.7553   0.693428 -0.169206   -0.212826   0.136583    31  ARG   A CG   
2075 C CD   . ARG   B 19  ? 1.03404  0.766926 0.730263 -0.159781   -0.216794   0.109399    31  ARG   A CD   
2076 N NE   . ARG   B 19  ? 1.10841  0.849175 0.793804 -0.12809    -0.19607    0.0971073   31  ARG   A NE   
2077 C CZ   . ARG   B 19  ? 1.18714  0.921042 0.883239 -0.09619    -0.172095   0.0899243   31  ARG   A CZ   
2078 N NH1  . ARG   B 19  ? 1.22554  0.941706 0.942549 -0.0883377  -0.167154   0.092007    31  ARG   A NH1  
2079 N NH2  . ARG   B 19  ? 1.20182  0.952829 0.889875 -0.0740695  -0.153714   0.0838056   31  ARG   A NH2  
2080 H H    . ARG   B 19  ? 0.799851 0.767498 0.64503  -0.178366   -0.197197   0.187236    31  ARG   A H    
2081 H HA   . ARG   B 19  ? 0.749255 0.657512 0.577595 -0.133913   -0.170953   0.16192     31  ARG   A HA   
2082 H HB2  . ARG   B 19  ? 0.861636 0.64669  0.635067 -0.161914   -0.203469   0.145009    31  ARG   A HB2  
2083 H HB3  . ARG   B 19  ? 0.834124 0.63579  0.608477 -0.127947   -0.180798   0.132974    31  ARG   A HB3  
2084 H HG2  . ARG   B 19  ? 0.908002 0.753519 0.661521 -0.160928   -0.20613    0.140506    31  ARG   A HG2  
2085 H HG3  . ARG   B 19  ? 0.946762 0.761399 0.694652 -0.195786   -0.229239   0.145773    31  ARG   A HG3  
2086 H HD2  . ARG   B 19  ? 1.09138  0.807228 0.76297  -0.180869   -0.234842   0.104592    31  ARG   A HD2  
2087 H HD3  . ARG   B 19  ? 1.06392  0.759492 0.758503 -0.154652   -0.215573   0.105116    31  ARG   A HD3  
2088 H HE   . ARG   B 19  ? 1.12115  0.875146 0.791645 -0.131789   -0.200149   0.0954716   31  ARG   A HE   
2089 H HH11 . ARG   B 19  ? 1.21903  0.913303 0.93363  -0.101917   -0.179592   0.0948233   31  ARG   A HH11 
2090 H HH12 . ARG   B 19  ? 1.17423  0.901658 0.907554 -0.0699403  -0.151747   0.0914991   31  ARG   A HH12 
2091 H HH21 . ARG   B 19  ? 1.19198  0.96532  0.872582 -0.0788046  -0.156343   0.0881922   31  ARG   A HH21 
2092 H HH22 . ARG   B 19  ? 1.18911  0.930757 0.879801 -0.0550465  -0.138994   0.0767054   31  ARG   A HH22 
2093 N N    . GLY   B 20  ? 0.704923 0.648549 0.583247 -0.144857   -0.162799   0.185271    32  GLY   A N    
2094 C CA   . GLY   B 20  ? 0.664301 0.614992 0.559565 -0.138634   -0.152979   0.19001     32  GLY   A CA   
2095 C C    . GLY   B 20  ? 0.65603  0.624885 0.569056 -0.110441   -0.129829   0.181255    32  GLY   A C    
2096 O O    . GLY   B 20  ? 0.656465 0.623399 0.577999 -0.103076   -0.123171   0.179968    32  GLY   A O    
2097 H H    . GLY   B 20  ? 0.690218 0.669355 0.579003 -0.15176    -0.164051   0.193318    32  GLY   A H    
2098 H HA2  . GLY   B 20  ? 0.700915 0.612792 0.582341 -0.140941   -0.160577   0.18705     32  GLY   A HA2  
2099 H HA3  . GLY   B 20  ? 0.667367 0.649692 0.575545 -0.152892   -0.155117   0.203182    32  GLY   A HA3  
2100 N N    . VAL   B 21  ? 0.627077 0.616838 0.546435 -0.0970278  -0.118567   0.177534    33  VAL   A N    
2101 C CA   . VAL   B 21  ? 0.594028 0.593533 0.528217 -0.0737421  -0.0969644  0.169601    33  VAL   A CA   
2102 C C    . VAL   B 21  ? 0.65632  0.636832 0.573918 -0.0615893  -0.0934787  0.161702    33  VAL   A C    
2103 O O    . VAL   B 21  ? 0.527932 0.526179 0.440717 -0.0660766  -0.0991661  0.169212    33  VAL   A O    
2104 C CB   . VAL   B 21  ? 0.596842 0.642208 0.557354 -0.06715    -0.081689   0.176414    33  VAL   A CB   
2105 C CG1  . VAL   B 21  ? 0.622868 0.663275 0.5944   -0.0467595  -0.0607774  0.165718    33  VAL   A CG1  
2106 C CG2  . VAL   B 21  ? 0.61853  0.692012 0.591149 -0.0798016  -0.0833376  0.184921    33  VAL   A CG2  
2107 H H    . VAL   B 21  ? 0.638878 0.636463 0.552679 -0.103993   -0.125544   0.181213    33  VAL   A H    
2108 H HA   . VAL   B 21  ? 0.608388 0.592401 0.543139 -0.0689792  -0.0942309  0.163672    33  VAL   A HA   
2109 H HB   . VAL   B 21  ? 0.604783 0.666994 0.566938 -0.0677286  -0.0836959  0.183037    33  VAL   A HB   
2110 H HG11 . VAL   B 21  ? 0.608916 0.635278 0.579531 -0.0462202  -0.0601295  0.158858    33  VAL   A HG11 
2111 H HG12 . VAL   B 21  ? 0.615493 0.644613 0.580553 -0.0389159  -0.0574163  0.16357     33  VAL   A HG12 
2112 H HG13 . VAL   B 21  ? 0.597658 0.660541 0.583214 -0.0427296  -0.0515862  0.168335    33  VAL   A HG13 
2113 H HG21 . VAL   B 21  ? 0.595039 0.695956 0.582281 -0.0728101  -0.0720037  0.1868      33  VAL   A HG21 
2114 H HG22 . VAL   B 21  ? 0.62175  0.701325 0.58977  -0.0953041  -0.0959156  0.193951    33  VAL   A HG22 
2115 H HG23 . VAL   B 21  ? 0.609659 0.668705 0.579343 -0.0796762  -0.0830533  0.180017    33  VAL   A HG23 
2116 N N    . LEU   B 22  ? 0.655594 0.605332 0.564394 -0.0475691  -0.0855899  0.148399    34  LEU   A N    
2117 C CA   . LEU   B 22  ? 0.673107 0.603692 0.561832 -0.035246   -0.079306   0.139744    34  LEU   A CA   
2118 C C    . LEU   B 22  ? 0.625524 0.566525 0.532128 -0.0178118  -0.0559391  0.136518    34  LEU   A C    
2119 O O    . LEU   B 22  ? 0.612052 0.553307 0.536657 -0.0126724  -0.0479428  0.131006    34  LEU   A O    
2120 C CB   . LEU   B 22  ? 0.727062 0.613043 0.58897  -0.0329286  -0.0879598  0.12616     34  LEU   A CB   
2121 C CG   . LEU   B 22  ? 0.865081 0.725665 0.703096 -0.0535303  -0.112605   0.127145    34  LEU   A CG   
2122 C CD1  . LEU   B 22  ? 0.87962  0.685431 0.690549 -0.0454448  -0.118044   0.110904    34  LEU   A CD1  
2123 C CD2  . LEU   B 22  ? 0.816218 0.691147 0.636566 -0.0672723  -0.1238     0.132555    34  LEU   A CD2  
2124 H H    . LEU   B 22  ? 0.650622 0.59461  0.566856 -0.0454074  -0.0836415  0.145293    34  LEU   A H    
2125 H HA   . LEU   B 22  ? 0.67823  0.6186   0.558105 -0.0397126  -0.0842135  0.145264    34  LEU   A HA   
2126 H HB2  . LEU   B 22  ? 0.736812 0.617142 0.61046  -0.0265929  -0.083717   0.122692    34  LEU   A HB2  
2127 H HB3  . LEU   B 22  ? 0.758045 0.635189 0.60543  -0.0232021  -0.0808765  0.119473    34  LEU   A HB3  
2128 H HG   . LEU   B 22  ? 0.814561 0.685887 0.667209 -0.0640841  -0.118512   0.135844    34  LEU   A HG   
2129 H HD11 . LEU   B 22  ? 0.876512 0.680383 0.70211  -0.0336564  -0.110268   0.108932    34  LEU   A HD11 
2130 H HD12 . LEU   B 22  ? 0.916882 0.700544 0.714797 -0.0602425  -0.134084   0.112217    34  LEU   A HD12 
2131 H HD13 . LEU   B 22  ? 0.908909 0.703722 0.700318 -0.036904   -0.113186   0.101375    34  LEU   A HD13 
2132 H HD21 . LEU   B 22  ? 0.805856 0.716111 0.646608 -0.0721209  -0.122341   0.144692    34  LEU   A HD21 
2133 H HD22 . LEU   B 22  ? 0.843193 0.71452  0.64967  -0.0564266  -0.116414   0.126555    34  LEU   A HD22 
2134 H HD23 . LEU   B 22  ? 0.865067 0.718485 0.667298 -0.0821731  -0.140091   0.130368    34  LEU   A HD23 
2135 N N    . LYS   B 23  ? 0.635183 0.58418  0.534874 -0.0102064  -0.0462171  0.141225    35  LYS   A N    
2136 C CA   . LYS   B 23  ? 0.540992 0.498178 0.457849 0.00180091  -0.0241161  0.142668    35  LYS   A CA   
2137 C C    . LYS   B 23  ? 0.583735 0.52746  0.478004 0.0119996   -0.0133378  0.139526    35  LYS   A C    
2138 O O    . LYS   B 23  ? 0.56039  0.499516 0.424822 0.0108812   -0.0222983  0.142681    35  LYS   A O    
2139 C CB   . LYS   B 23  ? 0.560241 0.540508 0.492453 0.00319937  -0.0193607  0.157062    35  LYS   A CB   
2140 C CG   . LYS   B 23  ? 0.530114 0.509088 0.477641 0.0135636   0.00259675  0.160508    35  LYS   A CG   
2141 C CD   . LYS   B 23  ? 0.546304 0.537877 0.501477 0.0215466   0.00769377  0.176856    35  LYS   A CD   
2142 C CE   . LYS   B 23  ? 0.55291  0.530594 0.522351 0.0293085   0.0293316   0.179039    35  LYS   A CE   
2143 N NZ   . LYS   B 23  ? 0.594288 0.573053 0.568309 0.0419118   0.0364927   0.19666     35  LYS   A NZ   
2144 H H    . LYS   B 23  ? 0.631256 0.579681 0.514138 -0.0138879  -0.0544632  0.144547    35  LYS   A H    
2145 H HA   . LYS   B 23  ? 0.550866 0.508114 0.483742 0.00245783  -0.018892   0.137054    35  LYS   A HA   
2146 H HB2  . LYS   B 23  ? 0.532667 0.524543 0.478302 -0.002326   -0.0241278  0.158025    35  LYS   A HB2  
2147 H HB3  . LYS   B 23  ? 0.559999 0.545155 0.478181 0.00244406  -0.02694    0.164231    35  LYS   A HB3  
2148 H HG2  . LYS   B 23  ? 0.551413 0.519911 0.487586 0.0174272   0.00926392  0.15875     35  LYS   A HG2  
2149 H HG3  . LYS   B 23  ? 0.525071 0.50407  0.489252 0.0115991   0.00805346  0.1538      35  LYS   A HG3  
2150 H HD2  . LYS   B 23  ? 0.532651 0.53888  0.499561 0.0193164   0.00221841  0.178462    35  LYS   A HD2  
2151 H HD3  . LYS   B 23  ? 0.559259 0.55366  0.497776 0.0237878   0.00184515  0.185049    35  LYS   A HD3  
2152 H HE2  . LYS   B 23  ? 0.5677   0.534728 0.528186 0.0291632   0.0357348   0.177154    35  LYS   A HE2  
2153 H HE3  . LYS   B 23  ? 0.545843 0.522439 0.530856 0.0256806   0.0333577   0.170072    35  LYS   A HE3  
2154 H HZ1  . LYS   B 23  ? 0.599018 0.581881 0.557879 0.0451207   0.0313772   0.206401    35  LYS   A HZ1  
2155 H HZ2  . LYS   B 23  ? 0.578242 0.56929  0.56345  0.0442031   0.0329086   0.197832    35  LYS   A HZ2  
2156 H HZ3  . LYS   B 23  ? 0.594402 0.557681 0.574989 0.0446258   0.0496338   0.197348    35  LYS   A HZ3  
2157 N N    . ILE   B 24  ? 0.520685 0.463945 0.430262 0.019743    0.00571512  0.134513    36  ILE   A N    
2158 C CA   . ILE   B 24  ? 0.594839 0.535943 0.492197 0.0286778   0.0236035   0.136434    36  ILE   A CA   
2159 C C    . ILE   B 24  ? 0.5747   0.5256   0.500198 0.0283276   0.0426115   0.145695    36  ILE   A C    
2160 O O    . ILE   B 24  ? 0.59903  0.555985 0.55432  0.0236048   0.0464391   0.139826    36  ILE   A O    
2161 C CB   . ILE   B 24  ? 0.627372 0.560837 0.517458 0.0373176   0.0306076   0.121462    36  ILE   A CB   
2162 C CG1  . ILE   B 24  ? 0.675481 0.585977 0.53591  0.0382921   0.0114175   0.109153    36  ILE   A CG1  
2163 C CG2  . ILE   B 24  ? 0.643981 0.582806 0.519806 0.0457504   0.0527675   0.125627    36  ILE   A CG2  
2164 C CD1  . ILE   B 24  ? 0.794828 0.69551  0.657779 0.0513733   0.016833    0.0934376   36  ILE   A CD1  
2165 H H    . ILE   B 24  ? 0.529409 0.476757 0.458538 0.0178884   0.00725941  0.130472    36  ILE   A H    
2166 H HA   . ILE   B 24  ? 0.60453  0.54322  0.479114 0.0295427   0.019513    0.142238    36  ILE   A HA   
2167 H HB   . ILE   B 24  ? 0.608691 0.549628 0.524168 0.0367363   0.0340973   0.117704    36  ILE   A HB   
2168 H HG12 . ILE   B 24  ? 0.716088 0.619245 0.547821 0.0388161   0.00882856  0.109828    36  ILE   A HG12 
2169 H HG13 . ILE   B 24  ? 0.67846  0.587108 0.545423 0.0297793   -0.00268684 0.111183    36  ILE   A HG13 
2170 H HG21 . ILE   B 24  ? 0.661146 0.598044 0.530656 0.0534881   0.0579894   0.115436    36  ILE   A HG21 
2171 H HG22 . ILE   B 24  ? 0.664877 0.599018 0.515262 0.0457223   0.0493903   0.131791    36  ILE   A HG22 
2172 H HG23 . ILE   B 24  ? 0.633067 0.582683 0.530926 0.0431408   0.0650975   0.132914    36  ILE   A HG23 
2173 H HD11 . ILE   B 24  ? 0.737479 0.649662 0.629535 0.0506593   0.0182795   0.0940819   36  ILE   A HD11 
2174 H HD12 . ILE   B 24  ? 0.783168 0.661647 0.626037 0.0518128   0.00371549  0.085619    36  ILE   A HD12 
2175 H HD13 . ILE   B 24  ? 0.774984 0.680725 0.630363 0.0603698   0.0318652   0.0909427   36  ILE   A HD13 
2176 N N    . VAL   B 25  ? 0.601297 0.550912 0.514102 0.0322659   0.0534357   0.160601    37  VAL   A N    
2177 C CA   . VAL   B 25  ? 0.579664 0.52775  0.512689 0.0312002   0.0736568   0.171028    37  VAL   A CA   
2178 C C    . VAL   B 25  ? 0.600097 0.553799 0.53678  0.0309413   0.091925    0.16608     37  VAL   A C    
2179 O O    . VAL   B 25  ? 0.626886 0.582566 0.534944 0.0377379   0.0966395   0.166541    37  VAL   A O    
2180 C CB   . VAL   B 25  ? 0.608391 0.550969 0.522338 0.0374324   0.0761518   0.193186    37  VAL   A CB   
2181 C CG1  . VAL   B 25  ? 0.650707 0.581193 0.578635 0.0362873   0.0978574   0.207747    37  VAL   A CG1  
2182 C CG2  . VAL   B 25  ? 0.630745 0.578638 0.549261 0.0401269   0.0592091   0.199547    37  VAL   A CG2  
2183 H H    . VAL   B 25  ? 0.610982 0.55898  0.50013  0.0348153   0.0470963   0.165128    37  VAL   A H    
2184 H HA   . VAL   B 25  ? 0.569762 0.517833 0.525155 0.0267816   0.0731154   0.167727    37  VAL   A HA   
2185 H HB   . VAL   B 25  ? 0.637365 0.581944 0.52481  0.0407606   0.0741863   0.195146    37  VAL   A HB   
2186 H HG11 . VAL   B 25  ? 0.628889 0.554462 0.581052 0.0313843   0.10066     0.201938    37  VAL   A HG11 
2187 H HG12 . VAL   B 25  ? 0.654361 0.58717  0.577173 0.0341013   0.109363    0.207625    37  VAL   A HG12 
2188 H HG13 . VAL   B 25  ? 0.660353 0.585408 0.577679 0.0422495   0.0975598   0.22362     37  VAL   A HG13 
2189 H HG21 . VAL   B 25  ? 0.637942 0.584959 0.547601 0.0463027   0.0606699   0.215211    37  VAL   A HG21 
2190 H HG22 . VAL   B 25  ? 0.615384 0.570565 0.522716 0.0379797   0.0447542   0.192885    37  VAL   A HG22 
2191 H HG23 . VAL   B 25  ? 0.604337 0.550546 0.545786 0.0378091   0.0615369   0.19509     37  VAL   A HG23 
2192 N N    . LYS   B 26  ? 0.588448 0.549031 0.56014  0.022555    0.101942    0.160121    38  LYS   A N    
2193 C CA   . LYS   B 26  ? 0.591089 0.568858 0.575709 0.0208769   0.11937     0.156626    38  LYS   A CA   
2194 C C    . LYS   B 26  ? 0.643026 0.617856 0.637805 0.0112708   0.141706    0.173541    38  LYS   A C    
2195 O O    . LYS   B 26  ? 0.622791 0.612443 0.612535 0.0119976   0.159514    0.179698    38  LYS   A O    
2196 C CB   . LYS   B 26  ? 0.581346 0.577379 0.599692 0.0160441   0.113247    0.14022     38  LYS   A CB   
2197 C CG   . LYS   B 26  ? 0.554886 0.549561 0.560877 0.0261496   0.0937126   0.127366    38  LYS   A CG   
2198 C CD   . LYS   B 26  ? 0.580062 0.57058  0.553187 0.0417258   0.0950463   0.122713    38  LYS   A CD   
2199 C CE   . LYS   B 26  ? 0.601043 0.616131 0.587689 0.0494266   0.11434     0.118735    38  LYS   A CE   
2200 N NZ   . LYS   B 26  ? 0.668619 0.673424 0.625449 0.0681196   0.109398    0.10572     38  LYS   A NZ   
2201 H H    . LYS   B 26  ? 0.572787 0.530219 0.560895 0.0173473   0.0977198   0.1579      38  LYS   A H    
2202 H HA   . LYS   B 26  ? 0.614391 0.59556  0.577299 0.029689    0.120532    0.154669    38  LYS   A HA   
2203 H HB2  . LYS   B 26  ? 0.562195 0.554332 0.597697 0.0066824   0.110301    0.139616    38  LYS   A HB2  
2204 H HB3  . LYS   B 26  ? 0.578909 0.592373 0.61088  0.0148852   0.125585    0.139623    38  LYS   A HB3  
2205 H HG2  . LYS   B 26  ? 0.551794 0.533923 0.548995 0.0241228   0.0815636   0.128756    38  LYS   A HG2  
2206 H HG3  . LYS   B 26  ? 0.545506 0.553482 0.573708 0.0240737   0.090313    0.119789    38  LYS   A HG3  
2207 H HD2  . LYS   B 26  ? 0.598747 0.57865  0.547371 0.0427766   0.0970908   0.130356    38  LYS   A HD2  
2208 H HD3  . LYS   B 26  ? 0.5805   0.562045 0.545321 0.0460134   0.080205    0.114594    38  LYS   A HD3  
2209 H HE2  . LYS   B 26  ? 0.591425 0.623849 0.609241 0.0455231   0.114467    0.11521     38  LYS   A HE2  
2210 H HE3  . LYS   B 26  ? 0.621651 0.642377 0.604414 0.0464785   0.129859    0.128119    38  LYS   A HE3  
2211 H HZ1  . LYS   B 26  ? 0.645184 0.644509 0.608954 0.0708882   0.0962977   0.0982627   38  LYS   A HZ1  
2212 H HZ2  . LYS   B 26  ? 0.670787 0.658078 0.596745 0.0693462   0.105219    0.107305    38  LYS   A HZ2  
2213 H HZ3  . LYS   B 26  ? 0.66722  0.68829  0.628432 0.0760289   0.123738    0.103346    38  LYS   A HZ3  
2214 N N    . ARG   B 27  ? 0.642807 0.596866 0.651154 0.00244548  0.141719    0.180809    39  ARG   A N    
2215 C CA   . ARG   B 27  ? 0.656624 0.5936   0.669352 -0.00684948 0.160691    0.199769    39  ARG   A CA   
2216 C C    . ARG   B 27  ? 0.680973 0.586441 0.678637 0.00156248  0.153938    0.213205    39  ARG   A C    
2217 O O    . ARG   B 27  ? 0.694223 0.590833 0.702451 0.00353342  0.14124     0.202708    39  ARG   A O    
2218 C CB   . ARG   B 27  ? 0.700122 0.639623 0.751979 -0.0286284  0.171154    0.193372    39  ARG   A CB   
2219 C CG   . ARG   B 27  ? 0.75407  0.67054  0.80932  -0.0426991  0.192354    0.215252    39  ARG   A CG   
2220 C CD   . ARG   B 27  ? 0.781637 0.691134 0.874095 -0.0697127  0.198924    0.207298    39  ARG   A CD   
2221 N NE   . ARG   B 27  ? 0.795208 0.673014 0.89371  -0.071272   0.185535    0.192222    39  ARG   A NE   
2222 C CZ   . ARG   B 27  ? 0.772201 0.64885  0.897477 -0.0921334  0.18157     0.173354    39  ARG   A CZ   
2223 N NH1  . ARG   B 27  ? 0.741324 0.654875 0.895435 -0.113102   0.186449    0.167827    39  ARG   A NH1  
2224 N NH2  . ARG   B 27  ? 0.786114 0.629547 0.909487 -0.0921496  0.172802    0.159285    39  ARG   A NH2  
2225 H H    . ARG   B 27  ? 0.62244  0.570907 0.636775 0.00244173  0.130088    0.173629    39  ARG   A H    
2226 H HA   . ARG   B 27  ? 0.688323 0.633432 0.685894 -0.00393383 0.171096    0.209612    39  ARG   A HA   
2227 H HB2  . ARG   B 27  ? 0.679728 0.647078 0.744535 -0.0315258  0.173054    0.184839    39  ARG   A HB2  
2228 H HB3  . ARG   B 27  ? 0.679879 0.609018 0.742519 -0.0318383  0.161548    0.183128    39  ARG   A HB3  
2229 H HG2  . ARG   B 27  ? 0.772674 0.661059 0.811926 -0.0353055  0.190872    0.226564    39  ARG   A HG2  
2230 H HG3  . ARG   B 27  ? 0.768382 0.701451 0.815269 -0.0419785  0.203725    0.225177    39  ARG   A HG3  
2231 H HD2  . ARG   B 27  ? 0.813681 0.707841 0.907065 -0.0804589  0.213215    0.223052    39  ARG   A HD2  
2232 H HD3  . ARG   B 27  ? 0.762533 0.705603 0.873824 -0.0763819  0.198398    0.196662    39  ARG   A HD3  
2233 H HE   . ARG   B 27  ? 0.786368 0.646867 0.868915 -0.0575762  0.179862    0.195327    39  ARG   A HE   
2234 H HH11 . ARG   B 27  ? 0.766405 0.686428 0.926166 -0.121788   0.199341    0.180372    39  ARG   A HH11 
2235 H HH12 . ARG   B 27  ? 0.729612 0.6639   0.898241 -0.118618   0.176801    0.152608    39  ARG   A HH12 
2236 H HH21 . ARG   B 27  ? 0.783957 0.610933 0.891592 -0.0761804  0.168947    0.16221     39  ARG   A HH21 
2237 H HH22 . ARG   B 27  ? 0.790311 0.629997 0.927864 -0.108028   0.171049    0.146583    39  ARG   A HH22 
2238 N N    . VAL   B 28  ? 0.758061 0.650726 0.730623 0.00836791  0.162899    0.237883    40  VAL   A N    
2239 C CA   . VAL   B 28  ? 0.807032 0.675817 0.766    0.0214392   0.155994    0.255236    40  VAL   A CA   
2240 C C    . VAL   B 28  ? 0.818059 0.648557 0.800596 0.0143779   0.166623    0.260699    40  VAL   A C    
2241 O O    . VAL   B 28  ? 0.825167 0.641745 0.820403 -0.00269778 0.18396     0.265882    40  VAL   A O    
2242 C CB   . VAL   B 28  ? 0.88723  0.757745 0.808483 0.0317571   0.15986     0.282024    40  VAL   A CB   
2243 C CG1  . VAL   B 28  ? 0.934975 0.786099 0.846115 0.0480159   0.151737    0.304736    40  VAL   A CG1  
2244 C CG2  . VAL   B 28  ? 0.901535 0.803204 0.793309 0.0377654   0.148367    0.27093     40  VAL   A CG2  
2245 H H    . VAL   B 28  ? 0.770801 0.672383 0.734816 0.00566826  0.173919    0.245247    40  VAL   A H    
2246 H HA   . VAL   B 28  ? 0.784339 0.661599 0.742463 0.0284548   0.14109     0.245579    40  VAL   A HA   
2247 H HB   . VAL   B 28  ? 0.911469 0.775668 0.832899 0.0235387   0.176082    0.29276     40  VAL   A HB   
2248 H HG11 . VAL   B 28  ? 0.905191 0.765176 0.82211  0.0545571   0.137387    0.294564    40  VAL   A HG11 
2249 H HG12 . VAL   B 28  ? 0.946679 0.771002 0.871713 0.0458528   0.161612    0.313529    40  VAL   A HG12 
2250 H HG13 . VAL   B 28  ? 0.950613 0.808277 0.835389 0.0543726   0.150936    0.321283    40  VAL   A HG13 
2251 H HG21 . VAL   B 28  ? 0.920175 0.823399 0.784342 0.0439595   0.148991    0.286866    40  VAL   A HG21 
2252 H HG22 . VAL   B 28  ? 0.884927 0.798509 0.782208 0.0310932   0.156373    0.259539    40  VAL   A HG22 
2253 H HG23 . VAL   B 28  ? 0.870179 0.777917 0.764337 0.0419648   0.132337    0.259372    40  VAL   A HG23 
2254 N N    . GLY   B 29  ? 0.815564 0.62989  0.803298 0.0274392   0.15646     0.258891    41  GLY   A N    
2255 C CA   . GLY   B 29  ? 0.829969 0.600153 0.834394 0.0269771   0.165387    0.260337    41  GLY   A CA   
2256 C C    . GLY   B 29  ? 0.915953 0.652641 0.904455 0.0412587   0.174282    0.294856    41  GLY   A C    
2257 O O    . GLY   B 29  ? 0.92373  0.671215 0.890659 0.0409979   0.178869    0.316777    41  GLY   A O    
2258 H H    . GLY   B 29  ? 0.793563 0.625419 0.773623 0.0374687   0.143737    0.256002    41  GLY   A H    
2259 H HA2  . GLY   B 29  ? 0.846072 0.605697 0.864262 0.00954786  0.174014    0.251115    41  GLY   A HA2  
2260 H HA3  . GLY   B 29  ? 0.824726 0.597046 0.836339 0.0349229   0.156868    0.248324    41  GLY   A HA3  
2261 N N    . ASN   B 30  ? 0.978065 0.674201 0.975149 0.0554544   0.177149    0.299724    42  ASN   A N    
2262 C CA   . ASN   B 30  ? 1.0541   0.711387 1.03878  0.0732355   0.184917    0.334928    42  ASN   A CA   
2263 C C    . ASN   B 30  ? 1.07398  0.715651 1.06891  0.102861    0.178884    0.333964    42  ASN   A C    
2264 O O    . ASN   B 30  ? 0.949441 0.602373 0.960585 0.103671    0.173657    0.30431     42  ASN   A O    
2265 C CB   . ASN   B 30  ? 1.16246  0.761655 1.15156  0.0533244   0.205519    0.345502    42  ASN   A CB   
2266 C CG   . ASN   B 30  ? 1.25301  0.827832 1.26643  0.0326223   0.210079    0.310302    42  ASN   A CG   
2267 O OD1  . ASN   B 30  ? 1.387    0.977272 1.41089  0.0021748   0.214851    0.295747    42  ASN   A OD1  
2268 N ND2  . ASN   B 30  ? 1.30263  0.849414 1.32496  0.0498625   0.207293    0.294326    42  ASN   A ND2  
2269 H H    . ASN   B 30  ? 0.961481 0.653355 0.971739 0.0555544   0.174389    0.280633    42  ASN   A H    
2270 H HA   . ASN   B 30  ? 1.06365  0.743311 1.03019  0.0793297   0.180623    0.35339     42  ASN   A HA   
2271 H HB2  . ASN   B 30  ? 1.21545  0.778676 1.19891  0.0677712   0.210134    0.366637    42  ASN   A HB2  
2272 H HB3  . ASN   B 30  ? 1.17238  0.786186 1.15317  0.0386751   0.211086    0.354873    42  ASN   A HB3  
2273 H HD21 . ASN   B 30  ? 1.26395  0.823637 1.29559  0.044458    0.202548    0.269444    42  ASN   A HD21 
2274 H HD22 . ASN   B 30  ? 1.326    0.841814 1.34439  0.0678151   0.210714    0.308819    42  ASN   A HD22 
2275 N N    . GLY   B 31  ? 1.14693  0.762882 1.13272  0.128209    0.181246    0.367851    43  GLY   A N    
2276 C CA   . GLY   B 31  ? 1.16826  0.780898 1.16602  0.163231    0.175733    0.372048    43  GLY   A CA   
2277 C C    . GLY   B 31  ? 1.18751  0.87585  1.18261  0.177373    0.153987    0.375599    43  GLY   A C    
2278 O O    . GLY   B 31  ? 1.05627  0.789506 1.04355  0.157094    0.143546    0.360212    43  GLY   A O    
2279 H H    . GLY   B 31  ? 1.17288  0.775457 1.14514  0.124651    0.186776    0.390226    43  GLY   A H    
2280 H HA2  . GLY   B 31  ? 1.23199  0.810243 1.22511  0.178808    0.181732    0.397024    43  GLY   A HA2  
2281 H HA3  . GLY   B 31  ? 1.17672  0.772411 1.18887  0.162007    0.180288    0.348092    43  GLY   A HA3  
2282 N N    . GLU   B 32  ? 1.3235   1.02371  1.32586  0.212297    0.147141    0.397543    44  GLU   A N    
2283 C CA   . GLU   B 32  ? 1.27388  1.04855  1.2789   0.225145    0.12505     0.403534    44  GLU   A CA   
2284 C C    . GLU   B 32  ? 1.12788  0.933925 1.15902  0.227225    0.121653    0.37101     44  GLU   A C    
2285 O O    . GLU   B 32  ? 1.12779  0.998013 1.16243  0.224442    0.103366    0.367409    44  GLU   A O    
2286 C CB   . GLU   B 32  ? 1.2399   1.02262  1.24447  0.261046    0.118252    0.445726    44  GLU   A CB   
2287 H H    . GLU   B 32  ? 1.33354  0.994195 1.34074  0.228499    0.156337    0.409567    44  GLU   A H    
2288 H HA   . GLU   B 32  ? 1.21542  1.01631  1.20357  0.207184    0.116336    0.40232     44  GLU   A HA   
2291 N N    . GLU   B 33  ? 1.05434  0.81466  1.10002  0.228074    0.138932    0.34653     45  GLU   A N    
2292 C CA   . GLU   B 33  ? 1.02781  0.814344 1.09553  0.237632    0.139613    0.320281    45  GLU   A CA   
2293 C C    . GLU   B 33  ? 0.898756 0.712662 0.962798 0.202779    0.132892    0.287694    45  GLU   A C    
2294 O O    . GLU   B 33  ? 0.804962 0.585778 0.858504 0.175965    0.13916     0.272514    45  GLU   A O    
2295 C CB   . GLU   B 33  ? 1.10273  0.826342 1.18149  0.256804    0.161115    0.305749    45  GLU   A CB   
2296 C CG   . GLU   B 33  ? 1.27222  0.943266 1.35124  0.289898    0.171168    0.338042    45  GLU   A CG   
2297 C CD   . GLU   B 33  ? 1.42461  1.03624  1.48145  0.269851    0.177214    0.357231    45  GLU   A CD   
2298 O OE1  . GLU   B 33  ? 1.41773  1.026    1.46306  0.230264    0.177251    0.339085    45  GLU   A OE1  
2299 O OE2  . GLU   B 33  ? 1.48249  1.056    1.53422  0.293464    0.181798    0.392728    45  GLU   A OE2  
2300 H H    . GLU   B 33  ? 1.10779  0.819936 1.1476   0.220381    0.150714    0.345397    45  GLU   A H    
2301 H HA   . GLU   B 33  ? 1.00794  0.839107 1.08526  0.254923    0.129755    0.333368    45  GLU   A HA   
2302 H HB2  . GLU   B 33  ? 1.12173  0.8105   1.19338  0.234947    0.168509    0.286265    45  GLU   A HB2  
2303 H HB3  . GLU   B 33  ? 1.10455  0.855247 1.19693  0.26931     0.161534    0.292926    45  GLU   A HB3  
2304 H HG2  . GLU   B 33  ? 1.30686  0.942496 1.39422  0.30648     0.183927    0.325742    45  GLU   A HG2  
2305 H HG3  . GLU   B 33  ? 1.26761  0.978892 1.3533   0.310133    0.161366    0.36072     45  GLU   A HG3  
2306 N N    . THR   B 34  ? 0.903162 0.779864 0.978103 0.203331    0.119892    0.279158    46  THR   A N    
2307 C CA   . THR   B 34  ? 0.804837 0.702219 0.8793   0.176554    0.115395    0.248399    46  THR   A CA   
2308 C C    . THR   B 34  ? 0.861329 0.764797 0.952452 0.190968    0.126145    0.228078    46  THR   A C    
2309 O O    . THR   B 34  ? 0.885223 0.797719 0.991659 0.222979    0.132803    0.239833    46  THR   A O    
2310 C CB   . THR   B 34  ? 0.851168 0.810401 0.921026 0.162367    0.0927541   0.254726    46  THR   A CB   
2311 O OG1  . THR   B 34  ? 0.767981 0.776189 0.856008 0.185447    0.0858963   0.271285    46  THR   A OG1  
2312 C CG2  . THR   B 34  ? 0.895461 0.849238 0.942583 0.150308    0.0831646   0.271138    46  THR   A CG2  
2313 H H    . THR   B 34  ? 0.879151 0.788167 0.962559 0.220187    0.113102    0.294546    46  THR   A H    
2314 H HA   . THR   B 34  ? 0.841487 0.708298 0.906812 0.158894    0.120259    0.237403    46  THR   A HA   
2315 H HB   . THR   B 34  ? 0.79609  0.76611  0.865468 0.145767    0.089615    0.236334    46  THR   A HB   
2317 H HG21 . THR   B 34  ? 0.85805  0.845328 0.899612 0.140028    0.0685796   0.271125    46  THR   A HG21 
2318 H HG22 . THR   B 34  ? 0.90867  0.856263 0.954164 0.166247    0.0844963   0.291746    46  THR   A HG22 
2319 H HG23 . THR   B 34  ? 0.885242 0.808867 0.924009 0.136857    0.0903793   0.261292    46  THR   A HG23 
2320 N N    . PRO   B 35  ? 0.875424 0.779251 0.963509 0.17027     0.128361    0.197655    47  PRO   A N    
2321 C CA   . PRO   B 35  ? 0.906724 0.818524 1.00423  0.184421    0.140217    0.177388    47  PRO   A CA   
2322 C C    . PRO   B 35  ? 0.930549 0.913253 1.04717  0.204705    0.134421    0.191624    47  PRO   A C    
2323 O O    . PRO   B 35  ? 0.784966 0.820767 0.903551 0.189455    0.115296    0.204321    47  PRO   A O    
2324 C CB   . PRO   B 35  ? 0.853975 0.767181 0.939657 0.152269    0.136427    0.14856     47  PRO   A CB   
2325 C CG   . PRO   B 35  ? 0.828518 0.716494 0.902801 0.125619    0.128297    0.151138    47  PRO   A CG   
2326 C CD   . PRO   B 35  ? 0.833274 0.734219 0.908117 0.135237    0.119656    0.18274     47  PRO   A CD   
2327 H HA   . PRO   B 35  ? 0.947456 0.81681  1.04516  0.199206    0.154138    0.172977    47  PRO   A HA   
2328 H HB2  . PRO   B 35  ? 0.827086 0.785066 0.915638 0.146507    0.127568    0.148475    47  PRO   A HB2  
2329 H HB3  . PRO   B 35  ? 0.882925 0.769958 0.965236 0.15484     0.14805     0.129333    47  PRO   A HB3  
2330 H HG2  . PRO   B 35  ? 0.803787 0.71295  0.873933 0.106987    0.118952    0.142201    47  PRO   A HG2  
2331 H HG3  . PRO   B 35  ? 0.861718 0.70597  0.932139 0.121609    0.138013    0.142213    47  PRO   A HG3  
2332 H HD2  . PRO   B 35  ? 0.801324 0.739478 0.874661 0.126754    0.106177    0.188047    47  PRO   A HD2  
2333 H HD3  . PRO   B 35  ? 0.844715 0.715205 0.912658 0.128399    0.122553    0.187938    47  PRO   A HD3  
2334 N N    . MET   B 36  ? 0.986009 0.968423 1.11712  0.238525    0.151552    0.188571    48  MET   A N    
2335 C CA   . MET   B 36  ? 0.942629 1.00064  1.09696  0.257676    0.15132     0.19663     48  MET   A CA   
2336 C C    . MET   B 36  ? 0.892213 0.975474 1.03914  0.239449    0.156382    0.167793    48  MET   A C    
2337 O O    . MET   B 36  ? 0.888205 0.922159 1.0148   0.227469    0.166587    0.138612    48  MET   A O    
2338 C CB   . MET   B 36  ? 0.966542 1.02046  1.14193  0.307025    0.170676    0.204474    48  MET   A CB   
2339 C CG   . MET   B 36  ? 0.97564  1.00479  1.16065  0.335665    0.168468    0.237303    48  MET   A CG   
2340 S SD   . MET   B 36  ? 0.947569 1.05688  1.14876  0.331978    0.138945    0.280478    48  MET   A SD   
2341 C CE   . MET   B 36  ? 0.92195  0.990224 1.08798  0.288473    0.12018     0.284337    48  MET   A CE   
2342 H H    . MET   B 36  ? 1.01295  0.94664  1.13998  0.250243    0.164523    0.18123     48  MET   A H    
2343 H HA   . MET   B 36  ? 0.907215 1.0072   1.06825  0.2497      0.135184    0.215729    48  MET   A HA   
2344 H HB2  . MET   B 36  ? 0.999343 1.00917  1.1649   0.313348    0.186656    0.182093    48  MET   A HB2  
2345 H HB3  . MET   B 36  ? 0.952108 1.0659   1.14525  0.316829    0.170677    0.209156    48  MET   A HB3  
2346 H HG2  . MET   B 36  ? 1.0016   0.971606 1.16891  0.324956    0.169971    0.234105    48  MET   A HG2  
2347 H HG3  . MET   B 36  ? 1.02136  1.04315  1.21948  0.36879     0.182821    0.238276    48  MET   A HG3  
2348 H HE1  . MET   B 36  ? 0.909283 1.01265  1.0775   0.286181    0.104254    0.305491    48  MET   A HE1  
2349 H HE2  . MET   B 36  ? 0.894245 0.964751 1.05002  0.262209    0.117154    0.265443    48  MET   A HE2  
2350 H HE3  . MET   B 36  ? 0.954598 0.964534 1.10931  0.293788    0.129321    0.284382    48  MET   A HE3  
2351 N N    . ILE   B 37  ? 0.832783 0.996355 0.99557  0.235351    0.148323    0.177567    49  ILE   A N    
2352 C CA   . ILE   B 37  ? 0.843513 1.04071  0.999313 0.220467    0.15416     0.156538    49  ILE   A CA   
2353 C C    . ILE   B 37  ? 0.846662 1.0148   0.996894 0.248551    0.183038    0.129206    49  ILE   A C    
2354 O O    . ILE   B 37  ? 0.885259 1.05529  1.05474  0.289402    0.199388    0.135649    49  ILE   A O    
2355 C CB   . ILE   B 37  ? 0.871806 1.16327  1.05262  0.216615    0.143161    0.179841    49  ILE   A CB   
2356 C CG1  . ILE   B 37  ? 0.879324 1.21384  1.05089  0.190622    0.142504    0.168234    49  ILE   A CG1  
2357 C CG2  . ILE   B 37  ? 1.01562  1.35057  1.23044  0.26075     0.158149    0.195132    49  ILE   A CG2  
2358 C CD1  . ILE   B 37  ? 0.830119 1.24527  1.02201  0.170716    0.123697    0.195235    49  ILE   A CD1  
2359 H H    . ILE   B 37  ? 0.834464 1.03415  1.01205  0.240299    0.138323    0.199129    49  ILE   A H    
2360 H HA   . ILE   B 37  ? 0.823178 1.00103  0.96081  0.193576    0.145378    0.146459    49  ILE   A HA   
2361 H HB   . ILE   B 37  ? 0.861495 1.15977  1.04349  0.20184     0.124919    0.196017    49  ILE   A HB   
2362 H HG12 . ILE   B 37  ? 0.892836 1.23729  1.0657   0.207556    0.161063    0.155308    49  ILE   A HG12 
2363 H HG13 . ILE   B 37  ? 0.860619 1.15965  1.00983  0.168604    0.13604     0.155564    49  ILE   A HG13 
2364 H HG21 . ILE   B 37  ? 0.953723 1.3479   1.18796  0.255895    0.146601    0.215369    49  ILE   A HG21 
2365 H HG22 . ILE   B 37  ? 0.994418 1.33695  1.20954  0.27478     0.176349    0.179611    49  ILE   A HG22 
2366 H HG23 . ILE   B 37  ? 0.994718 1.29182  1.21157  0.280106    0.161041    0.200758    49  ILE   A HG23 
2367 H HD11 . ILE   B 37  ? 0.818175 1.22252  1.00858  0.157998    0.105911    0.207597    49  ILE   A HD11 
2368 H HD12 . ILE   B 37  ? 0.823005 1.25484  1.00417  0.149409    0.121354    0.189247    49  ILE   A HD12 
2369 H HD13 . ILE   B 37  ? 0.841563 1.30312  1.05829  0.19134     0.131544    0.206608    49  ILE   A HD13 
2370 N N    . GLY   B 38  ? 0.788394 0.926582 0.910321 0.228585    0.189192    0.0975387   50  GLY   A N    
2371 C CA   . GLY   B 38  ? 0.812634 0.913398 0.920362 0.25186     0.215633    0.065855    50  GLY   A CA   
2372 C C    . GLY   B 38  ? 0.839186 0.84207  0.921667 0.242729    0.219688    0.0415981   50  GLY   A C    
2373 O O    . GLY   B 38  ? 0.848821 0.813259 0.907606 0.246054    0.235888    0.00706293  50  GLY   A O    
2374 H H    . GLY   B 38  ? 0.770231 0.910804 0.880309 0.200719    0.176356    0.0950793   50  GLY   A H    
2375 H HA2  . GLY   B 38  ? 0.813632 0.944039 0.910268 0.241914    0.219279    0.0523454   50  GLY   A HA2  
2376 H HA3  . GLY   B 38  ? 0.841885 0.95425  0.967111 0.284221    0.228262    0.0731742   50  GLY   A HA3  
2377 N N    . ASP   B 39  ? 0.824706 0.789843 0.911007 0.229535    0.205288    0.0594064   51  ASP   A N    
2378 C CA   . ASP   B 39  ? 0.860853 0.737591 0.929545 0.218521    0.209195    0.0429035   51  ASP   A CA   
2379 C C    . ASP   B 39  ? 0.854371 0.716988 0.896702 0.179891    0.202585    0.0122953   51  ASP   A C    
2380 O O    . ASP   B 39  ? 0.785836 0.7024   0.824895 0.155784    0.187356    0.0147651   51  ASP   A O    
2381 C CB   . ASP   B 39  ? 0.878136 0.732278 0.956851 0.210855    0.196053    0.0726328   51  ASP   A CB   
2382 C CG   . ASP   B 39  ? 0.904186 0.751165 1.00308  0.2494      0.202495    0.102424    51  ASP   A CG   
2383 O OD1  . ASP   B 39  ? 0.96373  0.815583 1.07242  0.286183    0.219376    0.0982464   51  ASP   A OD1  
2384 O OD2  . ASP   B 39  ? 0.885371 0.723872 0.989132 0.244201    0.190962    0.130196    51  ASP   A OD2  
2385 H H    . ASP   B 39  ? 0.790414 0.78702  0.890095 0.226112    0.192945    0.0826516   51  ASP   A H    
2386 H HA   . ASP   B 39  ? 0.919357 0.759186 0.98605  0.242204    0.225601    0.0323145   51  ASP   A HA   
2387 H HB2  . ASP   B 39  ? 0.821636 0.716291 0.903697 0.193307    0.180744    0.0846244   51  ASP   A HB2  
2388 H HB3  . ASP   B 39  ? 0.890454 0.69391  0.957559 0.195528    0.197194    0.0616699   51  ASP   A HB3  
2389 N N    . LYS   B 40  ? 0.914792 0.702709 0.93806  0.173424    0.212894    -0.0157456  52  LYS   A N    
2390 C CA   . LYS   B 40  ? 0.923602 0.692381 0.925526 0.133059    0.202651    -0.0410945  52  LYS   A CA   
2391 C C    . LYS   B 40  ? 0.916451 0.669724 0.930111 0.107655    0.186918    -0.0202834  52  LYS   A C    
2392 O O    . LYS   B 40  ? 0.976208 0.675826 0.996956 0.114308    0.193404    -0.00885785 52  LYS   A O    
2393 C CB   . LYS   B 40  ? 0.990163 0.686367 0.965792 0.127575    0.216312    -0.0814153  52  LYS   A CB   
2394 H H    . LYS   B 40  ? 0.961563 0.709085 0.985775 0.194568    0.225999    -0.0186886  52  LYS   A H    
2395 H HA   . LYS   B 40  ? 0.893155 0.710144 0.889701 0.122363    0.194984    -0.0444805  52  LYS   A HA   
2398 N N    . VAL   B 41  ? 0.919527 0.721099 0.934542 0.0803398   0.167301    -0.0138214  53  VAL   A N    
2399 C CA   . VAL   B 41  ? 0.873601 0.674891 0.901045 0.0610465   0.153619    0.007426    53  VAL   A CA   
2400 C C    . VAL   B 41  ? 0.845049 0.636447 0.864904 0.0248464   0.143687    -0.0125577  53  VAL   A C    
2401 O O    . VAL   B 41  ? 0.839137 0.660276 0.846208 0.0111409   0.135669    -0.031025   53  VAL   A O    
2402 C CB   . VAL   B 41  ? 0.852684 0.718472 0.890559 0.0642947   0.138833    0.0337084   53  VAL   A CB   
2403 C CG1  . VAL   B 41  ? 0.865146 0.734466 0.91071  0.0465704   0.125341    0.0518      53  VAL   A CG1  
2404 C CG2  . VAL   B 41  ? 0.813737 0.698782 0.86328  0.0977317   0.146447    0.0544428   53  VAL   A CG2  
2405 H H    . VAL   B 41  ? 0.886191 0.721293 0.893297 0.0746413   0.163025    -0.0226394  53  VAL   A H    
2406 H HA   . VAL   B 41  ? 0.898096 0.665073 0.931665 0.0702438   0.160741    0.0179947   53  VAL   A HA   
2407 H HB   . VAL   B 41  ? 0.829231 0.725709 0.860159 0.0555243   0.132617    0.0245261   53  VAL   A HB   
2408 H HG11 . VAL   B 41  ? 0.86785  0.704446 0.917237 0.0506909   0.132152    0.0590472   53  VAL   A HG11 
2409 H HG12 . VAL   B 41  ? 0.840539 0.713157 0.882514 0.0268338   0.118456    0.040498    53  VAL   A HG12 
2410 H HG13 . VAL   B 41  ? 0.81737  0.718986 0.867029 0.0510375   0.116999    0.0676794   53  VAL   A HG13 
2411 H HG21 . VAL   B 41  ? 0.78924  0.710722 0.845144 0.0955582   0.135292    0.0715801   53  VAL   A HG21 
2412 H HG22 . VAL   B 41  ? 0.840242 0.736587 0.886302 0.109231    0.154615    0.0431732   53  VAL   A HG22 
2413 H HG23 . VAL   B 41  ? 0.850415 0.701349 0.90451  0.109666    0.154085    0.0623571   53  VAL   A HG23 
2414 N N    . TYR   B 42  ? 0.873869 0.629948 0.902897 0.00915812  0.143718    -0.00569983 54  TYR   A N    
2415 C CA   . TYR   B 42  ? 0.876793 0.626839 0.906083 -0.025965   0.135091    -0.0224025  54  TYR   A CA   
2416 C C    . TYR   B 42  ? 0.815987 0.600154 0.863275 -0.0388192  0.122906    0.00090538  54  TYR   A C    
2417 O O    . TYR   B 42  ? 0.72354  0.491304 0.780454 -0.0313447  0.12928     0.0237631   54  TYR   A O    
2418 C CB   . TYR   B 42  ? 0.991229 0.66893  1.01724  -0.0378077  0.148223    -0.0376344  54  TYR   A CB   
2419 C CG   . TYR   B 42  ? 1.05114  0.675553 1.05616  -0.0232123  0.163528    -0.0644189  54  TYR   A CG   
2420 C CD1  . TYR   B 42  ? 1.10281  0.709282 1.10571  0.0164162   0.17841     -0.0539543  54  TYR   A CD1  
2421 C CD2  . TYR   B 42  ? 1.12532  0.714068 1.11265  -0.0484447  0.163524    -0.100895   54  TYR   A CD2  
2422 C CE1  . TYR   B 42  ? 1.15762  0.712719 1.1419   0.0351684   0.195077    -0.079493   54  TYR   A CE1  
2423 C CE2  . TYR   B 42  ? 1.17581  0.705637 1.13916  -0.0338194  0.179317    -0.129107   54  TYR   A CE2  
2424 C CZ   . TYR   B 42  ? 1.22205  0.73383  1.18412  0.0104602   0.196502    -0.118558   54  TYR   A CZ   
2425 O OH   . TYR   B 42  ? 1.34502  0.798579 1.28438  0.0319345   0.214687    -0.146458   54  TYR   A OH   
2426 H H    . TYR   B 42  ? 0.874548 0.613377 0.910837 0.020317    0.149228    0.0113451   54  TYR   A H    
2427 H HA   . TYR   B 42  ? 0.878766 0.651121 0.898015 -0.0341554  0.128296    -0.0390846  54  TYR   A HA   
2428 H HB2  . TYR   B 42  ? 0.980891 0.638844 1.01669  -0.0320405  0.154052    -0.0179803  54  TYR   A HB2  
2429 H HB3  . TYR   B 42  ? 0.979758 0.661568 1.00866  -0.0640357  0.140718    -0.0482148  54  TYR   A HB3  
2430 H HD1  . TYR   B 42  ? 1.05629  0.688688 1.0706   0.0320409   0.176867    -0.0296222  54  TYR   A HD1  
2431 H HD2  . TYR   B 42  ? 1.1045   0.70863  1.09589  -0.0759482  0.152428    -0.107223   54  TYR   A HD2  
2432 H HE1  . TYR   B 42  ? 1.17523  0.723361 1.16168  0.0650446   0.205424    -0.0707206  54  TYR   A HE1  
2433 H HE2  . TYR   B 42  ? 1.23096  0.735346 1.17879  -0.0529852  0.178069    -0.156043   54  TYR   A HE2  
2435 N N    . VAL   B 43  ? 0.76674  0.5982   0.816563 -0.0558596  0.105933    -0.00423341 55  VAL   A N    
2436 C CA   . VAL   B 43  ? 0.723436 0.585934 0.789665 -0.0631834  0.0961583   0.0150706   55  VAL   A CA   
2437 C C    . VAL   B 43  ? 0.677171 0.561814 0.754684 -0.091449   0.0847315   0.00191856  55  VAL   A C    
2438 O O    . VAL   B 43  ? 0.765933 0.654272 0.833994 -0.105643   0.0783553   -0.0211339  55  VAL   A O    
2439 C CB   . VAL   B 43  ? 0.628109 0.533226 0.691121 -0.0479512  0.0843162   0.0316942   55  VAL   A CB   
2440 C CG1  . VAL   B 43  ? 0.647977 0.545334 0.703244 -0.0221885  0.0922268   0.0448097   55  VAL   A CG1  
2441 C CG2  . VAL   B 43  ? 0.644228 0.586579 0.699298 -0.0571337  0.0685653   0.0196045   55  VAL   A CG2  
2442 H H    . VAL   B 43  ? 0.774014 0.617913 0.814219 -0.0614439  0.10083     -0.0196231  55  VAL   A H    
2443 H HA   . VAL   B 43  ? 0.715012 0.556618 0.787737 -0.0601231  0.104684    0.027141    55  VAL   A HA   
2444 H HB   . VAL   B 43  ? 0.627704 0.542545 0.699404 -0.0497635  0.0811426   0.0436509   55  VAL   A HB   
2445 H HG11 . VAL   B 43  ? 0.661699 0.552461 0.709349 -0.0174645  0.0971012   0.0330747   55  VAL   A HG11 
2446 H HG12 . VAL   B 43  ? 0.656302 0.530317 0.715504 -0.0158415  0.100941    0.0546722   55  VAL   A HG12 
2447 H HG13 . VAL   B 43  ? 0.615275 0.538986 0.6693   -0.0168639  0.0835154   0.0555966   55  VAL   A HG13 
2448 H HG21 . VAL   B 43  ? 0.611743 0.57395  0.662877 -0.0479191  0.0624327   0.0305052   55  VAL   A HG21 
2449 H HG22 . VAL   B 43  ? 0.626576 0.582142 0.690064 -0.0704444  0.0607696   0.0168214   55  VAL   A HG22 
2450 H HG23 . VAL   B 43  ? 0.657199 0.59087  0.701955 -0.0589676  0.0722898   0.00448749  55  VAL   A HG23 
2451 N N    . HIS   B 44  ? 0.642531 0.548055 0.739617 -0.0975988  0.0817503   0.017412    56  HIS   A N    
2452 C CA   . HIS   B 44  ? 0.614202 0.564904 0.727541 -0.11378    0.0665257   0.0136948   56  HIS   A CA   
2453 C C    . HIS   B 44  ? 0.548813 0.533707 0.662508 -0.0957383  0.0563033   0.0311515   56  HIS   A C    
2454 O O    . HIS   B 44  ? 0.572281 0.545402 0.679614 -0.0781756  0.0632202   0.0473591   56  HIS   A O    
2455 C CB   . HIS   B 44  ? 0.679362 0.630675 0.818935 -0.13573    0.0731374   0.0152631   56  HIS   A CB   
2456 C CG   . HIS   B 44  ? 0.714644 0.651403 0.858741 -0.165786   0.0717791   -0.00741383 56  HIS   A CG   
2457 N ND1  . HIS   B 44  ? 0.701808 0.667116 0.841327 -0.180251   0.0538868   -0.0273635  56  HIS   A ND1  
2458 C CD2  . HIS   B 44  ? 0.697932 0.594569 0.849121 -0.186881   0.0843285   -0.0128706  56  HIS   A CD2  
2459 C CE1  . HIS   B 44  ? 0.767939 0.712401 0.910768 -0.21031    0.0546107   -0.0472223  56  HIS   A CE1  
2460 N NE2  . HIS   B 44  ? 0.747789 0.647231 0.898515 -0.215442   0.0734002   -0.0388494  56  HIS   A NE2  
2461 H H    . HIS   B 44  ? 0.643981 0.536732 0.744357 -0.0898363  0.0900189   0.0313498   56  HIS   A H    
2462 H HA   . HIS   B 44  ? 0.628984 0.588558 0.73506  -0.122257   0.0580772   -0.00121137 56  HIS   A HA   
2463 H HB2  . HIS   B 44  ? 0.674335 0.601957 0.814442 -0.129776   0.085938    0.0269518   56  HIS   A HB2  
2464 H HB3  . HIS   B 44  ? 0.641458 0.628548 0.795621 -0.136309   0.065934    0.0217592   56  HIS   A HB3  
2466 H HD2  . HIS   B 44  ? 0.729059 0.599409 0.88333  -0.184036   0.0974684   -0.00067118 56  HIS   A HD2  
2467 H HE1  . HIS   B 44  ? 0.766908 0.724271 0.904762 -0.226015   0.0431998   -0.0641138  56  HIS   A HE1  
2469 N N    . TYR   B 45  ? 0.564019 0.588205 0.682161 -0.100061   0.0383483   0.0277338   57  TYR   A N    
2470 C CA   . TYR   B 45  ? 0.543832 0.590106 0.65852  -0.0833407  0.0272104   0.0423873   57  TYR   A CA   
2471 C C    . TYR   B 45  ? 0.574884 0.662085 0.708753 -0.089099   0.0117242   0.0423351   57  TYR   A C    
2472 O O    . TYR   B 45  ? 0.570953 0.677994 0.71493  -0.107007   0.00398591  0.0299806   57  TYR   A O    
2473 C CB   . TYR   B 45  ? 0.522362 0.566935 0.611834 -0.0734472  0.019233    0.0443183   57  TYR   A CB   
2474 C CG   . TYR   B 45  ? 0.559447 0.626295 0.638952 -0.0845832  0.00500505  0.0326491   57  TYR   A CG   
2475 C CD1  . TYR   B 45  ? 0.496263 0.593913 0.57759  -0.0844929  -0.0142934  0.0398815   57  TYR   A CD1  
2476 C CD2  . TYR   B 45  ? 0.604085 0.659258 0.669085 -0.093951   0.0109384   0.014382    57  TYR   A CD2  
2477 C CE1  . TYR   B 45  ? 0.554525 0.675345 0.623586 -0.0954198  -0.0283779  0.0321009   57  TYR   A CE1  
2478 C CE2  . TYR   B 45  ? 0.568112 0.645922 0.617054 -0.104466   -0.00170044 0.00307455  57  TYR   A CE2  
2479 C CZ   . TYR   B 45  ? 0.537371 0.65029  0.58783  -0.106205   -0.0220755  0.0134486   57  TYR   A CZ   
2480 O OH   . TYR   B 45  ? 0.634816 0.772986 0.666412 -0.116867   -0.0360256  0.00591528  57  TYR   A OH   
2481 H H    . TYR   B 45  ? 0.56852  0.603905 0.690847 -0.113982   0.0321687   0.0162596   57  TYR   A H    
2482 H HA   . TYR   B 45  ? 0.541108 0.577694 0.657841 -0.0741262  0.0350931   0.0527424   57  TYR   A HA   
2483 H HB2  . TYR   B 45  ? 0.51742  0.567369 0.604105 -0.0634685  0.0137406   0.0556606   57  TYR   A HB2  
2484 H HB3  . TYR   B 45  ? 0.541785 0.565473 0.622591 -0.0690121  0.0293771   0.0434447   57  TYR   A HB3  
2485 H HD1  . TYR   B 45  ? 0.506005 0.608226 0.596286 -0.076452   -0.0178748  0.0502238   57  TYR   A HD1  
2486 H HD2  . TYR   B 45  ? 0.600828 0.630737 0.663979 -0.0916139  0.0241303   0.00980452  57  TYR   A HD2  
2487 H HE1  . TYR   B 45  ? 0.52923  0.669385 0.599115 -0.0938204  -0.042078   0.040115    57  TYR   A HE1  
2488 H HE2  . TYR   B 45  ? 0.598792 0.666778 0.634279 -0.109847   0.00367692  -0.0116504  57  TYR   A HE2  
2490 N N    . LYS   B 46  ? 0.537688 0.636191 0.675716 -0.0726558  0.00705617  0.0559041   58  LYS   A N    
2491 C CA   . LYS   B 46  ? 0.563188 0.697106 0.715961 -0.0677013  -0.0094341  0.0601008   58  LYS   A CA   
2492 C C    . LYS   B 46  ? 0.53845  0.658943 0.66785  -0.0504587  -0.0203228  0.0711682   58  LYS   A C    
2493 O O    . LYS   B 46  ? 0.50887  0.603525 0.624395 -0.0391677  -0.0122482  0.0777662   58  LYS   A O    
2494 C CB   . LYS   B 46  ? 0.574982 0.730089 0.758145 -0.0626308  -0.00012166 0.0646636   58  LYS   A CB   
2495 C CG   . LYS   B 46  ? 0.613098 0.777344 0.819415 -0.0850648  0.012627    0.0566732   58  LYS   A CG   
2496 C CD   . LYS   B 46  ? 0.62899  0.814193 0.863977 -0.0821439  0.028453    0.0641702   58  LYS   A CD   
2497 C CE   . LYS   B 46  ? 0.635963 0.822336 0.891334 -0.109069   0.0427851   0.0597505   58  LYS   A CE   
2498 N NZ   . LYS   B 46  ? 0.649989 0.873147 0.938159 -0.107084   0.0570029   0.0695629   58  LYS   A NZ   
2499 H H    . LYS   B 46  ? 0.546126 0.627664 0.676398 -0.0627339  0.0144711   0.0628796   58  LYS   A H    
2500 H HA   . LYS   B 46  ? 0.560306 0.712093 0.716683 -0.0791447  -0.0191067  0.0532589   58  LYS   A HA   
2501 H HB2  . LYS   B 46  ? 0.575362 0.713198 0.750135 -0.0503735  0.00864393  0.0708812   58  LYS   A HB2  
2502 H HB3  . LYS   B 46  ? 0.574064 0.755335 0.770142 -0.0567383  -0.0109853  0.0674628   58  LYS   A HB3  
2503 H HG2  . LYS   B 46  ? 0.614699 0.801194 0.831327 -0.0979932  0.00197685  0.0496293   58  LYS   A HG2  
2504 H HG3  . LYS   B 46  ? 0.618428 0.752642 0.809911 -0.0908851  0.0212553   0.0532822   58  LYS   A HG3  
2505 H HD2  . LYS   B 46  ? 0.620707 0.785948 0.841672 -0.0678473  0.037481    0.0709442   58  LYS   A HD2  
2506 H HD3  . LYS   B 46  ? 0.616373 0.835869 0.870391 -0.0757422  0.0205776   0.0664608   58  LYS   A HD3  
2507 H HE2  . LYS   B 46  ? 0.648627 0.849187 0.913232 -0.126013   0.0328929   0.0506011   58  LYS   A HE2  
2508 H HE3  . LYS   B 46  ? 0.652031 0.801229 0.889494 -0.111381   0.0528824   0.0600439   58  LYS   A HE3  
2509 H HZ1  . LYS   B 46  ? 0.637474 0.898158 0.945656 -0.103565   0.0479182   0.0694729   58  LYS   A HZ1  
2510 H HZ2  . LYS   B 46  ? 0.642524 0.852666 0.918536 -0.0908626  0.0660444   0.0767335   58  LYS   A HZ2  
2511 H HZ3  . LYS   B 46  ? 0.659064 0.881699 0.959559 -0.125621   0.0662053   0.0689599   58  LYS   A HZ3  
2512 N N    . GLY   B 47  ? 0.495878 0.630721 0.615966 -0.0526635  -0.0390286  0.0732686   59  GLY   A N    
2513 C CA   . GLY   B 47  ? 0.502218 0.620989 0.599766 -0.0415905  -0.0502859  0.0857399   59  GLY   A CA   
2514 C C    . GLY   B 47  ? 0.528046 0.665133 0.63387  -0.0320716  -0.0694121  0.0953043   59  GLY   A C    
2515 O O    . GLY   B 47  ? 0.516504 0.68871  0.644346 -0.0357664  -0.0772285  0.0924685   59  GLY   A O    
2516 H H    . GLY   B 47  ? 0.512816 0.667391 0.639489 -0.0627243  -0.0454063  0.0675879   59  GLY   A H    
2517 H HA2  . GLY   B 47  ? 0.502938 0.601734 0.595102 -0.0330901  -0.0432082  0.0893799   59  GLY   A HA2  
2518 H HA3  . GLY   B 47  ? 0.507616 0.622866 0.588862 -0.0488952  -0.0526051  0.0850892   59  GLY   A HA3  
2519 N N    . LYS   B 48  ? 0.520882 0.632987 0.609788 -0.0195666  -0.0780227  0.107584    60  LYS   A N    
2520 C CA   . LYS   B 48  ? 0.561517 0.679851 0.653708 -0.00746346 -0.0972877  0.119814    60  LYS   A CA   
2521 C C    . LYS   B 48  ? 0.582335 0.661748 0.643975 -0.00498947 -0.107716   0.133433    60  LYS   A C    
2522 O O    . LYS   B 48  ? 0.573521 0.625638 0.617318 -0.00975124 -0.0994115  0.132174    60  LYS   A O    
2523 C CB   . LYS   B 48  ? 0.604714 0.7323   0.724843 0.0138205   -0.0922704  0.117995    60  LYS   A CB   
2524 C CG   . LYS   B 48  ? 0.696526 0.792262 0.810204 0.0265125   -0.074866   0.112582    60  LYS   A CG   
2525 C CD   . LYS   B 48  ? 0.756862 0.862223 0.893245 0.0517978   -0.0679609  0.11067     60  LYS   A CD   
2526 C CE   . LYS   B 48  ? 0.903943 0.981584 1.02886  0.0737463   -0.084503   0.120415    60  LYS   A CE   
2527 N NZ   . LYS   B 48  ? 0.961061 1.05713  1.11344  0.103923    -0.0837246  0.121398    60  LYS   A NZ   
2528 H H    . LYS   B 48  ? 0.529283 0.618643 0.6042   -0.0186717  -0.0726359  0.108943    60  LYS   A H    
2529 H HA   . LYS   B 48  ? 0.565914 0.709319 0.66173  -0.0155808  -0.10654    0.120809    60  LYS   A HA   
2530 H HB2  . LYS   B 48  ? 0.63171  0.758924 0.753429 0.0256457   -0.1051     0.127058    60  LYS   A HB2  
2531 H HB3  . LYS   B 48  ? 0.603879 0.763048 0.74611  0.0083232   -0.0880941  0.111774    60  LYS   A HB3  
2532 H HG2  . LYS   B 48  ? 0.67011  0.769056 0.785085 0.0162503   -0.0621657  0.105684    60  LYS   A HG2  
2533 H HG3  . LYS   B 48  ? 0.695831 0.759831 0.785896 0.0277143   -0.0797856  0.117137    60  LYS   A HG3  
2534 H HD2  . LYS   B 48  ? 0.760621 0.904163 0.924468 0.0504473   -0.0667317  0.109168    60  LYS   A HD2  
2535 H HD3  . LYS   B 48  ? 0.769201 0.860728 0.899761 0.0555202   -0.0537187  0.104968    60  LYS   A HD3  
2536 H HE2  . LYS   B 48  ? 0.895923 0.934622 0.995826 0.0756746   -0.0828209  0.119242    60  LYS   A HE2  
2537 H HE3  . LYS   B 48  ? 0.880335 0.961197 1.00003  0.0658621   -0.0993003  0.12878     60  LYS   A HE3  
2538 H HZ1  . LYS   B 48  ? 0.951256 1.04316  1.10552  0.112995    -0.0691328  0.11374     60  LYS   A HZ1  
2539 H HZ2  . LYS   B 48  ? 0.937234 1.0744   1.11562  0.101577    -0.0864001  0.123343    60  LYS   A HZ2  
2540 H HZ3  . LYS   B 48  ? 0.97348  1.04501  1.11503  0.116299    -0.095045   0.128074    60  LYS   A HZ3  
2541 N N    . LEU   B 49  ? 0.614876 0.692696 0.671211 0.00113741  -0.127456   0.148552    61  LEU   A N    
2542 C CA   . LEU   B 49  ? 0.623037 0.654903 0.654989 0.00654586  -0.138896   0.163276    61  LEU   A CA   
2543 C C    . LEU   B 49  ? 0.659702 0.660357 0.698577 0.0307043   -0.13271    0.156806    61  LEU   A C    
2544 O O    . LEU   B 49  ? 0.658146 0.683658 0.724901 0.0476029   -0.126333   0.149389    61  LEU   A O    
2545 C CB   . LEU   B 49  ? 0.630955 0.668148 0.656948 0.00886684  -0.161782   0.183876    61  LEU   A CB   
2546 C CG   . LEU   B 49  ? 0.611164 0.687803 0.627408 -0.0127086  -0.16878    0.1898      61  LEU   A CG   
2547 C CD1  . LEU   B 49  ? 0.709304 0.791097 0.716332 -0.00856982 -0.193089   0.214531    61  LEU   A CD1  
2548 C CD2  . LEU   B 49  ? 0.582385 0.649317 0.572614 -0.0351597  -0.160972   0.190771    61  LEU   A CD2  
2549 H H    . LEU   B 49  ? 0.607784 0.712724 0.675714 0.0013063   -0.134905   0.150522    61  LEU   A H    
2550 H HA   . LEU   B 49  ? 0.623519 0.642331 0.638408 -0.00654959 -0.13556    0.164151    61  LEU   A HA   
2551 H HB2  . LEU   B 49  ? 0.639333 0.688711 0.684377 0.0252262   -0.165663   0.184042    61  LEU   A HB2  
2552 H HB3  . LEU   B 49  ? 0.657916 0.658814 0.666122 0.00987413  -0.16927    0.194714    61  LEU   A HB3  
2553 H HG   . LEU   B 49  ? 0.600824 0.709798 0.633215 -0.015114   -0.162604   0.177344    61  LEU   A HG   
2554 H HD11 . LEU   B 49  ? 0.694054 0.789672 0.721161 0.00722872  -0.198745   0.214836    61  LEU   A HD11 
2555 H HD12 . LEU   B 49  ? 0.688327 0.796488 0.684693 -0.0232636  -0.196623   0.217372    61  LEU   A HD12 
2556 H HD13 . LEU   B 49  ? 0.714411 0.759664 0.705568 -0.00703336 -0.199443   0.227779    61  LEU   A HD13 
2557 H HD21 . LEU   B 49  ? 0.568407 0.637956 0.565162 -0.0374053  -0.146451   0.176324    61  LEU   A HD21 
2558 H HD22 . LEU   B 49  ? 0.607921 0.643372 0.58454  -0.0356842  -0.166242   0.201933    61  LEU   A HD22 
2559 H HD23 . LEU   B 49  ? 0.592795 0.683684 0.573448 -0.0467111  -0.165148   0.195147    61  LEU   A HD23 
2560 N N    . SER   B 50  ? 0.786135 0.734355 0.799305 0.032494    -0.135502   0.159627    62  SER   A N    
2561 C CA   . SER   B 50  ? 0.839169 0.752531 0.851071 0.0571141   -0.129867   0.150453    62  SER   A CA   
2562 C C    . SER   B 50  ? 0.954134 0.860968 0.979821 0.0849265   -0.141416   0.158567    62  SER   A C    
2563 O O    . SER   B 50  ? 1.06223  0.966239 1.10194  0.112179    -0.131459   0.148009    62  SER   A O    
2564 C CB   . SER   B 50  ? 0.948984 0.805305 0.925582 0.0486574   -0.133405   0.149566    62  SER   A CB   
2565 O OG   . SER   B 50  ? 0.992582 0.864071 0.960705 0.0239305   -0.125806   0.146989    62  SER   A OG   
2566 H H    . SER   B 50  ? 0.77103  0.705787 0.766491 0.0177207   -0.140759   0.166519    62  SER   A H    
2567 H HA   . SER   B 50  ? 0.839255 0.773025 0.864892 0.0616834   -0.115022   0.138687    62  SER   A HA   
2568 H HB2  . SER   B 50  ? 0.974297 0.804678 0.937698 0.0450272   -0.147864   0.161575    62  SER   A HB2  
2569 H HB3  . SER   B 50  ? 0.963392 0.798154 0.935529 0.0638785   -0.126869   0.139179    62  SER   A HB3  
2571 N N    . ASN   B 51  ? 0.861527 0.770545 0.884319 0.0804609   -0.161595   0.178834    63  ASN   A N    
2572 C CA   . ASN   B 51  ? 0.956534 0.857787 0.992272 0.109425    -0.175273   0.191209    63  ASN   A CA   
2573 C C    . ASN   B 51  ? 0.958826 0.931245 1.03997  0.125825    -0.170495   0.18729     63  ASN   A C    
2574 O O    . ASN   B 51  ? 0.867966 0.847678 0.968503 0.154341    -0.181369   0.198347    63  ASN   A O    
2575 C CB   . ASN   B 51  ? 1.00955  0.888954 1.02432  0.0983807   -0.199479   0.218564    63  ASN   A CB   
2576 C CG   . ASN   B 51  ? 0.949565 0.891851 0.972506 0.0764852   -0.206801   0.229066    63  ASN   A CG   
2577 O OD1  . ASN   B 51  ? 0.906791 0.904654 0.950965 0.0675152   -0.194633   0.213832    63  ASN   A OD1  
2578 N ND2  . ASN   B 51  ? 0.96526  0.895689 0.966972 0.0653879   -0.226434   0.254943    63  ASN   A ND2  
2579 H H    . ASN   B 51  ? 0.888137 0.804307 0.900113 0.0601292   -0.166658   0.186125    63  ASN   A H    
2580 H HA   . ASN   B 51  ? 0.984745 0.845679 1.01235  0.126915    -0.172063   0.185151    63  ASN   A HA   
2581 H HB2  . ASN   B 51  ? 1.03452  0.895394 1.05394  0.120728    -0.208966   0.227943    63  ASN   A HB2  
2582 H HB3  . ASN   B 51  ? 1.01437  0.854297 1.00305  0.0832554   -0.201404   0.221018    63  ASN   A HB3  
2583 H HD21 . ASN   B 51  ? 0.957618 0.924406 0.960041 0.0534948   -0.231417   0.26121     63  ASN   A HD21 
2584 H HD22 . ASN   B 51  ? 1.00761  0.892741 0.992773 0.0690786   -0.23449    0.266175    63  ASN   A HD22 
2585 N N    . GLY   B 52  ? 0.941745 0.966164 1.04096  0.107347    -0.155783   0.173397    64  GLY   A N    
2586 C CA   . GLY   B 52  ? 0.946918 1.03988  1.09102  0.115843    -0.149595   0.167321    64  GLY   A CA   
2587 C C    . GLY   B 52  ? 0.992622 1.13662  1.15323  0.109502    -0.17133    0.182817    64  GLY   A C    
2588 O O    . GLY   B 52  ? 0.998693 1.20236  1.20048  0.120157    -0.17299    0.182337    64  GLY   A O    
2589 H H    . GLY   B 52  ? 0.921975 0.938702 1.00563  0.087787    -0.149921   0.168278    64  GLY   A H    
2590 H HA2  . GLY   B 52  ? 0.92045  1.03098  1.06963  0.100874    -0.135752   0.155146    64  GLY   A HA2  
2591 H HA3  . GLY   B 52  ? 0.964243 1.05515  1.12371  0.14071     -0.144166   0.164706    64  GLY   A HA3  
2592 N N    . LYS   B 53  ? 0.944103 1.07108  1.07265  0.0901369   -0.188033   0.197179    65  LYS   A N    
2593 C CA   . LYS   B 53  ? 0.902672 1.07336  1.0368   0.08524     -0.211376   0.214765    65  LYS   A CA   
2594 C C    . LYS   B 53  ? 0.812478 1.03195  0.944954 0.0510202   -0.208519   0.202088    65  LYS   A C    
2595 O O    . LYS   B 53  ? 0.817237 1.0881   0.95955  0.0440898   -0.225474   0.208965    65  LYS   A O    
2596 C CB   . LYS   B 53  ? 0.825888 0.952265 0.92586  0.0885872   -0.232688   0.242397    65  LYS   A CB   
2597 H H    . LYS   B 53  ? 0.946127 1.03699  1.04849  0.0791661   -0.184859   0.196721    65  LYS   A H    
2598 H HA   . LYS   B 53  ? 0.882437 1.08328  1.0465   0.104386    -0.215761   0.217567    65  LYS   A HA   
2601 N N    . LYS   B 54  ? 0.789647 0.993076 0.909201 0.0308092   -0.187712   0.182706    66  LYS   A N    
2602 C CA   . LYS   B 54  ? 0.742634 0.981999 0.859996 0.00194442  -0.181812   0.16659     66  LYS   A CA   
2603 C C    . LYS   B 54  ? 0.692875 0.92242  0.822315 -0.00452898 -0.155072   0.144061    66  LYS   A C    
2604 O O    . LYS   B 54  ? 0.636855 0.822442 0.754043 0.00270285  -0.141517   0.142263    66  LYS   A O    
2605 C CB   . LYS   B 54  ? 0.708899 0.937339 0.783677 -0.0202997  -0.187618   0.172235    66  LYS   A CB   
2606 H H    . LYS   B 54  ? 0.783563 0.951059 0.894285 0.0357942   -0.177417   0.179298    66  LYS   A H    
2607 H HA   . LYS   B 54  ? 0.735696 1.01677  0.872445 0.0009127   -0.191375   0.166551    66  LYS   A HA   
2610 N N    . PHE   B 55  ? 0.589347 0.859598 0.739702 -0.0211194  -0.149717   0.128066    67  PHE   A N    
2611 C CA   . PHE   B 55  ? 0.663911 0.928091 0.825549 -0.0324342  -0.125859   0.10867     67  PHE   A CA   
2612 C C    . PHE   B 55  ? 0.633493 0.909921 0.780925 -0.0612773  -0.124379   0.0925906   67  PHE   A C    
2613 O O    . PHE   B 55  ? 0.738668 1.04796  0.880478 -0.0733772  -0.142389   0.0925292   67  PHE   A O    
2614 C CB   . PHE   B 55  ? 0.621806 0.924549 0.829983 -0.0268319  -0.119179   0.103673    67  PHE   A CB   
2615 C CG   . PHE   B 55  ? 0.691287 0.988734 0.915232 0.00661207  -0.120528   0.117259    67  PHE   A CG   
2616 C CD1  . PHE   B 55  ? 0.683277 1.00394  0.917709 0.0246491   -0.143057   0.133596    67  PHE   A CD1  
2617 C CD2  . PHE   B 55  ? 0.706946 0.971782 0.930317 0.021967    -0.0995464  0.11373     67  PHE   A CD2  
2618 C CE1  . PHE   B 55  ? 0.692273 1.0004   0.939571 0.0594201   -0.142877   0.144074    67  PHE   A CE1  
2619 C CE2  . PHE   B 55  ? 0.736389 0.991809 0.969226 0.0545039   -0.0994088  0.121869    67  PHE   A CE2  
2620 C CZ   . PHE   B 55  ? 0.69511  0.968428 0.939793 0.0743026   -0.120552   0.136308    67  PHE   A CZ   
2621 H H    . PHE   B 55  ? 0.638711 0.941656 0.795816 -0.0268358  -0.162916   0.130282    67  PHE   A H    
2622 H HA   . PHE   B 55  ? 0.626194 0.855206 0.774549 -0.0265949  -0.114437   0.108722    67  PHE   A HA   
2623 H HB2  . PHE   B 55  ? 0.647872 0.989046 0.870477 -0.0368087  -0.130805   0.102234    67  PHE   A HB2  
2624 H HB3  . PHE   B 55  ? 0.634363 0.92708  0.846956 -0.0347337  -0.102247   0.0935202   67  PHE   A HB3  
2625 H HD1  . PHE   B 55  ? 0.693719 1.03844  0.925717 0.014253    -0.158561   0.137439    67  PHE   A HD1  
2626 H HD2  . PHE   B 55  ? 0.693863 0.943359 0.909733 0.0111118   -0.085129   0.10528     67  PHE   A HD2  
2627 H HE1  . PHE   B 55  ? 0.712496 1.03425  0.967774 0.0738388   -0.158431   0.156476    67  PHE   A HE1  
2628 H HE2  . PHE   B 55  ? 0.718088 0.951628 0.94635  0.064243    -0.0849554  0.117585    67  PHE   A HE2  
2629 H HZ   . PHE   B 55  ? 0.723873 0.986063 0.974229 0.0989521   -0.119592   0.140815    67  PHE   A HZ   
2630 N N    . ASP   B 56  ? 0.548516 0.796657 0.687718 -0.0707891  -0.103183   0.0787078   68  ASP   A N    
2631 C CA   . ASP   B 56  ? 0.593345 0.841438 0.716276 -0.0944546  -0.0982824  0.0601751   68  ASP   A CA   
2632 C C    . ASP   B 56  ? 0.552271 0.774627 0.686823 -0.0995797  -0.0738849  0.0475664   68  ASP   A C    
2633 O O    . ASP   B 56  ? 0.49969  0.690836 0.629607 -0.0854676  -0.0603054  0.0546313   68  ASP   A O    
2634 C CB   . ASP   B 56  ? 0.552217 0.780306 0.633643 -0.0967619  -0.0995842  0.0621439   68  ASP   A CB   
2635 C CG   . ASP   B 56  ? 0.648171 0.867325 0.709081 -0.115052   -0.0882816  0.0394361   68  ASP   A CG   
2636 O OD1  . ASP   B 56  ? 0.726115 0.969307 0.788968 -0.133368   -0.0963422  0.0236135   68  ASP   A OD1  
2637 O OD2  . ASP   B 56  ? 0.692016 0.880379 0.736264 -0.110486   -0.0716306  0.0364963   68  ASP   A OD2  
2638 H H    . ASP   B 56  ? 0.564914 0.791606 0.707148 -0.0613636  -0.091476   0.0805537   68  ASP   A H    
2639 H HA   . ASP   B 56  ? 0.581845 0.860501 0.714044 -0.105566   -0.109227   0.0548892   68  ASP   A HA   
2640 H HB2  . ASP   B 56  ? 0.589565 0.835223 0.661942 -0.0961441  -0.115463   0.0715713   68  ASP   A HB2  
2641 H HB3  . ASP   B 56  ? 0.570803 0.77429  0.64612  -0.0860783  -0.0919745  0.0699821   68  ASP   A HB3  
2642 N N    . SER   B 57  ? 0.581408 0.814751 0.728758 -0.121126   -0.0696477  0.0301456   69  SER   A N    
2643 C CA   . SER   B 57  ? 0.625167 0.827174 0.781232 -0.127623   -0.046286   0.0211413   69  SER   A CA   
2644 C C    . SER   B 57  ? 0.655549 0.838107 0.793869 -0.15089    -0.0412362  -0.00223675 69  SER   A C    
2645 O O    . SER   B 57  ? 0.67518  0.88477  0.810756 -0.170197   -0.0567064  -0.0152729  69  SER   A O    
2646 C CB   . SER   B 57  ? 0.627292 0.854589 0.825156 -0.130965   -0.040784   0.0255396   69  SER   A CB   
2647 O OG   . SER   B 57  ? 0.650091 0.850191 0.854556 -0.147844   -0.021377   0.015344    69  SER   A OG   
2648 H H    . SER   B 57  ? 0.598371 0.857235 0.747961 -0.133012   -0.0819432  0.0243853   69  SER   A H    
2649 H HA   . SER   B 57  ? 0.607012 0.782121 0.751328 -0.114163   -0.0364388  0.0279509   69  SER   A HA   
2650 H HB2  . SER   B 57  ? 0.611303 0.837901 0.815427 -0.112946   -0.0370516  0.037861    69  SER   A HB2  
2651 H HB3  . SER   B 57  ? 0.630656 0.894796 0.844711 -0.139589   -0.0542364  0.0239031   69  SER   A HB3  
2653 N N    . SER   B 58  ? 0.583005 0.717838 0.708794 -0.148139   -0.0201678  -0.00776392 70  SER   A N    
2654 C CA   . SER   B 58  ? 0.661246 0.764732 0.770575 -0.166351   -0.0114451  -0.0315211  70  SER   A CA   
2655 C C    . SER   B 58  ? 0.756584 0.87554  0.891515 -0.196402   -0.0161028  -0.044451   70  SER   A C    
2656 O O    . SER   B 58  ? 0.850661 0.960329 0.970179 -0.219238   -0.0209632  -0.0686043  70  SER   A O    
2657 C CB   . SER   B 58  ? 0.702361 0.752371 0.802214 -0.153617   0.0122275   -0.0296912  70  SER   A CB   
2658 O OG   . SER   B 58  ? 0.666042 0.709365 0.791916 -0.14909    0.0235053   -0.0132708  70  SER   A OG   
2659 H H    . SER   B 58  ? 0.595898 0.715839 0.722431 -0.133672   -0.0113933  0.00343581  70  SER   A H    
2660 H HA   . SER   B 58  ? 0.682766 0.791562 0.769423 -0.167912   -0.0189712  -0.0402972  70  SER   A HA   
2661 H HB2  . SER   B 58  ? 0.722677 0.746776 0.812604 -0.164457   0.0187289   -0.0461079  70  SER   A HB2  
2662 H HB3  . SER   B 58  ? 0.677378 0.72328  0.761532 -0.137335   0.0134948   -0.023053   70  SER   A HB3  
2664 N N    . HIS   B 59  ? 0.666622 0.812046 0.84015  -0.197479   -0.014557   -0.0291174  71  HIS   A N    
2665 C CA   . HIS   B 59  ? 0.73679  0.905373 0.942753 -0.228209   -0.0173216  -0.0370098  71  HIS   A CA   
2666 C C    . HIS   B 59  ? 0.787285 1.01032  0.998931 -0.247836   -0.0446596  -0.0482252  71  HIS   A C    
2667 O O    . HIS   B 59  ? 0.729437 0.96033  0.951557 -0.282107   -0.0508106  -0.0657821  71  HIS   A O    
2668 C CB   . HIS   B 59  ? 0.685931 0.879826 0.932749 -0.221358   -0.00640662 -0.0155652  71  HIS   A CB   
2669 C CG   . HIS   B 59  ? 0.717567 0.856516 0.957217 -0.213833   0.0200925   -0.00757478 71  HIS   A CG   
2670 N ND1  . HIS   B 59  ? 0.677512 0.802857 0.908173 -0.182439   0.0312526   0.0110974   71  HIS   A ND1  
2671 C CD2  . HIS   B 59  ? 0.781754 0.875835 1.02113  -0.234767   0.0360511   -0.0142872  71  HIS   A CD2  
2672 C CE1  . HIS   B 59  ? 0.756725 0.835727 0.98108  -0.183002   0.0524498   0.0168033   71  HIS   A CE1  
2673 N NE2  . HIS   B 59  ? 0.846258 0.902919 1.07629  -0.213586   0.0564034   0.00282705  71  HIS   A NE2  
2674 H H    . HIS   B 59  ? 0.667063 0.817095 0.846833 -0.17921    -0.0109368  -0.0136029  71  HIS   A H    
2675 H HA   . HIS   B 59  ? 0.760592 0.890502 0.956751 -0.242354   -0.00725331 -0.0495758  71  HIS   A HA   
2676 H HB2  . HIS   B 59  ? 0.669177 0.88793  0.920385 -0.20084    -0.0123782  -0.00312814 71  HIS   A HB2  
2677 H HB3  . HIS   B 59  ? 0.707775 0.931534 0.980957 -0.242431   -0.0110934  -0.0187941  71  HIS   A HB3  
2679 H HD2  . HIS   B 59  ? 0.821057 0.907873 1.0638   -0.259776   0.0330765   -0.0280492  71  HIS   A HD2  
2680 H HE1  . HIS   B 59  ? 0.743677 0.806946 0.95958  -0.165563   0.06209     0.0288828   71  HIS   A HE1  
2682 N N    . ASP   B 60  ? 0.816452 1.07478  1.01929  -0.227619   -0.0621865  -0.0370133  72  ASP   A N    
2683 C CA   . ASP   B 60  ? 0.9211   1.22959  1.11928  -0.241548   -0.0905358  -0.0441845  72  ASP   A CA   
2684 C C    . ASP   B 60  ? 0.957194 1.23948  1.11867  -0.270245   -0.0944561  -0.0756831  72  ASP   A C    
2685 O O    . ASP   B 60  ? 0.990631 1.31258  1.15617  -0.297219   -0.11569    -0.0888504  72  ASP   A O    
2686 C CB   . ASP   B 60  ? 0.857224 1.18276  1.03333  -0.214355   -0.104933   -0.0274665  72  ASP   A CB   
2687 C CG   . ASP   B 60  ? 0.789173 1.13387  0.992649 -0.183339   -0.104657   0.00084095  72  ASP   A CG   
2688 O OD1  . ASP   B 60  ? 0.813396 1.19464  1.0622   -0.184348   -0.104322   0.00850098  72  ASP   A OD1  
2689 O OD2  . ASP   B 60  ? 0.743662 1.06781  0.922543 -0.159435   -0.104786   0.0142075   72  ASP   A OD2  
2690 H H    . ASP   B 60  ? 0.796638 1.04656  0.995016 -0.204897   -0.057022   -0.0234009  72  ASP   A H    
2691 H HA   . ASP   B 60  ? 0.887641 1.23806  1.11961  -0.251171   -0.0990542  -0.039404   72  ASP   A HA   
2692 H HB2  . ASP   B 60  ? 0.8634   1.15336  1.008    -0.207124   -0.0965036  -0.0318596  72  ASP   A HB2  
2693 H HB3  . ASP   B 60  ? 0.873886 1.23321  1.04525  -0.224747   -0.124216   -0.0310655  72  ASP   A HB3  
2694 N N    . ARG   B 61  ? 0.956463 1.17441  1.08073  -0.262208   -0.0747869  -0.0879571  73  ARG   A N    
2695 C CA   . ARG   B 61  ? 1.00227  1.18465  1.08512  -0.281997   -0.0734805  -0.120665   73  ARG   A CA   
2696 C C    . ARG   B 61  ? 1.10667  1.24011  1.20034  -0.308054   -0.0581827  -0.140213   73  ARG   A C    
2697 O O    . ARG   B 61  ? 1.14066  1.23072  1.19999  -0.325126   -0.0543342  -0.171148   73  ARG   A O    
2698 C CB   . ARG   B 61  ? 0.985365 1.13158  1.02603  -0.253888   -0.0593874  -0.120575   73  ARG   A CB   
2699 H H    . ARG   B 61  ? 0.934253 1.13048  1.05868  -0.242096   -0.0615305  -0.0756956  73  ARG   A H    
2700 H HA   . ARG   B 61  ? 1.02895  1.24597  1.10358  -0.296708   -0.0927987  -0.12905    73  ARG   A HA   
2703 N N    . ASN   B 62  ? 1.04006  1.17689  1.1787   -0.311488   -0.0483186  -0.122466   74  ASN   A N    
2704 C CA   . ASN   B 62  ? 1.06536  1.15072  1.21543  -0.335748   -0.0314557  -0.133596   74  ASN   A CA   
2705 C C    . ASN   B 62  ? 1.08632  1.08545  1.19288  -0.324556   -0.0105439  -0.152026   74  ASN   A C    
2706 O O    . ASN   B 62  ? 1.16166  1.1087   1.25343  -0.350746   -0.00528267 -0.17803    74  ASN   A O    
2707 C CB   . ASN   B 62  ? 1.08463  1.19912  1.25319  -0.383886   -0.0499272  -0.152964   74  ASN   A CB   
2708 H H    . ASN   B 62  ? 1.00664  1.17823  1.16852  -0.298356   -0.0517165  -0.102198   74  ASN   A H    
2709 H HA   . ASN   B 62  ? 1.03304  1.12262  1.2102   -0.327223   -0.0209144  -0.113515   74  ASN   A HA   
2712 N N    . GLU   B 63  ? 1.06829  1.05016  1.1558   -0.285131   0.0019758   -0.138376   75  GLU   A N    
2713 C CA   . GLU   B 63  ? 1.13142  1.03896  1.18688  -0.268295   0.0240545   -0.150674   75  GLU   A CA   
2714 C C    . GLU   B 63  ? 1.05246  0.957369 1.10893  -0.226991   0.0376684   -0.122594   75  GLU   A C    
2715 O O    . GLU   B 63  ? 1.01289  0.969437 1.07537  -0.21153    0.0263413   -0.104293   75  GLU   A O    
2716 C CB   . GLU   B 63  ? 1.1432   1.03439  1.15093  -0.27077    0.0196744   -0.184369   75  GLU   A CB   
2717 H H    . GLU   B 63  ? 1.02779  1.04498  1.1236   -0.268315   -0.00347269 -0.120829   75  GLU   A H    
2718 H HA   . GLU   B 63  ? 1.14643  1.01432  1.21023  -0.282043   0.0339857   -0.155074   75  GLU   A HA   
2721 N N    . PRO   B 64  ? 1.05242  0.89686  1.10262  -0.208666   0.0605314   -0.11757    76  PRO   A N    
2722 C CA   . PRO   B 64  ? 0.98607  0.832008 1.03371  -0.170971   0.0707506   -0.0933799  76  PRO   A CA   
2723 C C    . PRO   B 64  ? 0.942343 0.816163 0.962931 -0.152665   0.0646379   -0.0998195  76  PRO   A C    
2724 O O    . PRO   B 64  ? 0.965585 0.832457 0.958949 -0.161932   0.061979    -0.127716   76  PRO   A O    
2725 C CB   . PRO   B 64  ? 1.05284  0.826912 1.09325  -0.157344   0.0938621   -0.0935206  76  PRO   A CB   
2726 C CG   . PRO   B 64  ? 1.08867  0.822769 1.13916  -0.19213    0.0964772   -0.107347   76  PRO   A CG   
2727 C CD   . PRO   B 64  ? 1.11874  0.889904 1.1641   -0.223806   0.0759067   -0.133269   76  PRO   A CD   
2728 H HA   . PRO   B 64  ? 0.950114 0.822701 1.01772  -0.167418   0.0673188   -0.0728555  76  PRO   A HA   
2729 H HB2  . PRO   B 64  ? 1.06771  0.822581 1.08655  -0.144485   0.0997775   -0.107093   76  PRO   A HB2  
2730 H HB3  . PRO   B 64  ? 1.01846  0.79291  1.06973  -0.140998   0.100225    -0.0709302  76  PRO   A HB3  
2731 H HG2  . PRO   B 64  ? 1.1463   0.82547  1.1831   -0.188479   0.108718    -0.118084   76  PRO   A HG2  
2732 H HG3  . PRO   B 64  ? 1.07942  0.821303 1.15257  -0.198293   0.0983624   -0.08848    76  PRO   A HG3  
2733 H HD2  . PRO   B 64  ? 1.1576   0.902301 1.17733  -0.22651    0.0772362   -0.157693   76  PRO   A HD2  
2734 H HD3  . PRO   B 64  ? 1.12567  0.901298 1.18999  -0.249561   0.0713202   -0.133453   76  PRO   A HD3  
2735 N N    . PHE   B 65  ? 0.880214 0.785654 0.90648  -0.129152   0.0625021   -0.0740886  77  PHE   A N    
2736 C CA   . PHE   B 65  ? 0.83693  0.766073 0.840906 -0.110528   0.0609549   -0.0730772  77  PHE   A CA   
2737 C C    . PHE   B 65  ? 0.843067 0.737015 0.838884 -0.0830346  0.0822232   -0.0702578  77  PHE   A C    
2738 O O    . PHE   B 65  ? 0.766374 0.643712 0.779274 -0.0691505  0.0903691   -0.0492446  77  PHE   A O    
2739 C CB   . PHE   B 65  ? 0.778131 0.754801 0.795184 -0.103465   0.0462249   -0.0455696  77  PHE   A CB   
2740 C CG   . PHE   B 65  ? 0.762705 0.769776 0.759238 -0.090789   0.0418237   -0.0396831  77  PHE   A CG   
2741 C CD1  . PHE   B 65  ? 0.791374 0.831288 0.76829  -0.103618   0.0274894   -0.049646   77  PHE   A CD1  
2742 C CD2  . PHE   B 65  ? 0.738484 0.745528 0.735716 -0.0682964  0.0512117   -0.0220277  77  PHE   A CD2  
2743 C CE1  . PHE   B 65  ? 0.778794 0.847905 0.736146 -0.0947242  0.0250589   -0.0408106  77  PHE   A CE1  
2744 C CE2  . PHE   B 65  ? 0.69311  0.733337 0.675173 -0.061184   0.0475878   -0.0142677  77  PHE   A CE2  
2745 C CZ   . PHE   B 65  ? 0.680521 0.750399 0.642543 -0.0747692  0.035432    -0.022653   77  PHE   A CZ   
2746 H H    . PHE   B 65  ? 0.849393 0.762118 0.893726 -0.125989   0.0622231   -0.0563951  77  PHE   A H    
2747 H HA   . PHE   B 65  ? 0.86254  0.800913 0.848698 -0.120892   0.055239    -0.0912603  77  PHE   A HA   
2748 H HB2  . PHE   B 65  ? 0.769394 0.767018 0.795146 -0.117933   0.0335701   -0.0462726  77  PHE   A HB2  
2749 H HB3  . PHE   B 65  ? 0.760574 0.727292 0.79117  -0.0933886  0.0520099   -0.029844   77  PHE   A HB3  
2750 H HD1  . PHE   B 65  ? 0.798222 0.842679 0.77497  -0.119658   0.0190586   -0.061291   77  PHE   A HD1  
2751 H HD2  . PHE   B 65  ? 0.727424 0.714669 0.736144 -0.0591873  0.0594258   -0.0137439  77  PHE   A HD2  
2752 H HE1  . PHE   B 65  ? 0.76895  0.860702 0.71057  -0.103823   0.0152889   -0.0454063  77  PHE   A HE1  
2753 H HE2  . PHE   B 65  ? 0.684754 0.729562 0.670334 -0.0481215  0.0529764   -0.00160239 77  PHE   A HE2  
2754 H HZ   . PHE   B 65  ? 0.700367 0.793138 0.651074 -0.0712499  0.0342471   -0.015592   77  PHE   A HZ   
2755 N N    . VAL   B 66  ? 0.877945 0.764953 0.847185 -0.0737538  0.0911942   -0.0908514  78  VAL   A N    
2756 C CA   . VAL   B 66  ? 0.945006 0.80342  0.90943  -0.0437236  0.112613    -0.0899979  78  VAL   A CA   
2757 C C    . VAL   B 66  ? 0.911066 0.819597 0.865186 -0.0254805  0.113413    -0.0811256  78  VAL   A C    
2758 O O    . VAL   B 66  ? 0.950539 0.895775 0.885734 -0.0383663  0.103029    -0.0905477  78  VAL   A O    
2759 C CB   . VAL   B 66  ? 0.989486 0.78764  0.932769 -0.0444696  0.128467    -0.124639   78  VAL   A CB   
2760 C CG1  . VAL   B 66  ? 0.998404 0.762213 0.941932 -0.00713054 0.152086    -0.1211     78  VAL   A CG1  
2761 C CG2  . VAL   B 66  ? 1.06069  0.812432 1.01293  -0.0730408  0.124647    -0.134912   78  VAL   A CG2  
2762 H H    . VAL   B 66  ? 0.89969  0.802669 0.853302 -0.0852208  0.08404     -0.105547   78  VAL   A H    
2763 H HA   . VAL   B 66  ? 0.912151 0.757819 0.89396  -0.0346804  0.116398    -0.071712   78  VAL   A HA   
2764 H HB   . VAL   B 66  ? 1.0161   0.82996  0.937751 -0.0511842  0.12554     -0.143746   78  VAL   A HB   
2765 H HG11 . VAL   B 66  ? 0.983283 0.740829 0.946686 0.00155153  0.153276    -0.0982214  78  VAL   A HG11 
2766 H HG12 . VAL   B 66  ? 0.994316 0.791135 0.930946 0.00812436  0.1556      -0.119509   78  VAL   A HG12 
2767 H HG13 . VAL   B 66  ? 1.06098  0.776916 0.991561 -0.00699357 0.162379    -0.142801   78  VAL   A HG13 
2768 H HG21 . VAL   B 66  ? 1.10431  0.810544 1.04168  -0.0734951  0.134876    -0.156774   78  VAL   A HG21 
2769 H HG22 . VAL   B 66  ? 1.03385  0.812492 0.986201 -0.0955711  0.109742    -0.139886   78  VAL   A HG22 
2770 H HG23 . VAL   B 66  ? 1.02945  0.771122 1.00201  -0.0687142  0.126915    -0.114082   78  VAL   A HG23 
2771 N N    . PHE   B 67  ? 0.900211 0.813969 0.867563 0.00275919  0.124891    -0.0607154  79  PHE   A N    
2772 C CA   . PHE   B 67  ? 0.820959 0.786174 0.784266 0.0191194   0.128097    -0.0499845  79  PHE   A CA   
2773 C C    . PHE   B 67  ? 0.86123  0.821191 0.842129 0.0530428   0.145081    -0.0343739  79  PHE   A C    
2774 O O    . PHE   B 67  ? 0.835579 0.754962 0.831879 0.0626244   0.14967     -0.0245114  79  PHE   A O    
2775 C CB   . PHE   B 67  ? 0.735714 0.751224 0.706869 0.00371076  0.106089    -0.0248349  79  PHE   A CB   
2776 C CG   . PHE   B 67  ? 0.667093 0.68443  0.663782 0.0103497   0.0991316   0.00554102  79  PHE   A CG   
2777 C CD1  . PHE   B 67  ? 0.706532 0.692901 0.714931 0.00061366  0.0927563   0.010251    79  PHE   A CD1  
2778 C CD2  . PHE   B 67  ? 0.642141 0.694799 0.65007  0.0253845   0.0997055   0.0287084   79  PHE   A CD2  
2779 C CE1  . PHE   B 67  ? 0.630597 0.618541 0.65531  0.00762856  0.0878088   0.0358105   79  PHE   A CE1  
2780 C CE2  . PHE   B 67  ? 0.640149 0.693014 0.665704 0.0299447   0.0919069   0.0535419   79  PHE   A CE2  
2781 C CZ   . PHE   B 67  ? 0.633623 0.652354 0.664563 0.0220354   0.0864337   0.0561564   79  PHE   A CZ   
2782 H H    . PHE   B 67  ? 0.888775 0.77583  0.868969 0.0110773   0.130519    -0.0518813  79  PHE   A H    
2783 H HA   . PHE   B 67  ? 0.861675 0.833009 0.804583 0.017697    0.133475    -0.0695591  79  PHE   A HA   
2784 H HB2  . PHE   B 67  ? 0.730657 0.780756 0.694083 0.00713867  0.106979    -0.0214325  79  PHE   A HB2  
2785 H HB3  . PHE   B 67  ? 0.733468 0.747528 0.698234 -0.0152007  0.0946862   -0.0322205  79  PHE   A HB3  
2786 H HD1  . PHE   B 67  ? 0.699263 0.665946 0.703677 -0.0117329  0.0918917   -0.00414199 79  PHE   A HD1  
2787 H HD2  . PHE   B 67  ? 0.655838 0.734712 0.658744 0.0317722   0.105557    0.0271809   79  PHE   A HD2  
2788 H HE1  . PHE   B 67  ? 0.64236  0.612119 0.67327  0.00143225  0.0853376   0.0388801   79  PHE   A HE1  
2789 H HE2  . PHE   B 67  ? 0.620595 0.699923 0.653635 0.0375047   0.0903481   0.0686354   79  PHE   A HE2  
2790 H HZ   . PHE   B 67  ? 0.612745 0.632484 0.651401 0.0251379   0.081501    0.0719803   79  PHE   A HZ   
2791 N N    . SER   B 68  ? 0.850828 0.85736  0.830511 0.0708838   0.154078    -0.0295607  80  SER   A N    
2792 C CA   . SER   B 68  ? 0.848089 0.864889 0.848403 0.10552     0.169601    -0.0140018  80  SER   A CA   
2793 C C    . SER   B 68  ? 0.807006 0.87932  0.830701 0.103426    0.154522    0.0225806   80  SER   A C    
2794 O O    . SER   B 68  ? 0.840622 0.966479 0.860677 0.0884093   0.144444    0.0316094   80  SER   A O    
2795 C CB   . SER   B 68  ? 0.950475 0.987573 0.939633 0.130019    0.192555    -0.0325025  80  SER   A CB   
2796 O OG   . SER   B 68  ? 1.00747  0.977264 0.979512 0.144692    0.211272    -0.0643993  80  SER   A OG   
2797 H H    . SER   B 68  ? 0.846345 0.882807 0.812966 0.061004    0.150274    -0.0347873  80  SER   A H    
2798 H HA   . SER   B 68  ? 0.881971 0.854961 0.888964 0.115005    0.174894    -0.0142001  80  SER   A HA   
2799 H HB2  . SER   B 68  ? 0.926709 0.995543 0.900461 0.116012    0.188889    -0.0393084  80  SER   A HB2  
2800 H HB3  . SER   B 68  ? 0.923146 0.991006 0.931668 0.150086    0.198491    -0.0151361  80  SER   A HB3  
2802 N N    . LEU   B 69  ? 0.789071 0.844441 0.833846 0.116734    0.152284    0.0438632   81  LEU   A N    
2803 C CA   . LEU   B 69  ? 0.702719 0.797901 0.764655 0.109655    0.134153    0.0755187   81  LEU   A CA   
2804 C C    . LEU   B 69  ? 0.684319 0.851328 0.761362 0.120696    0.136499    0.0913138   81  LEU   A C    
2805 O O    . LEU   B 69  ? 0.701684 0.885254 0.790383 0.150105    0.15544     0.0893058   81  LEU   A O    
2806 C CB   . LEU   B 69  ? 0.726484 0.787839 0.802051 0.123629    0.133169    0.093167    81  LEU   A CB   
2807 C CG   . LEU   B 69  ? 0.724323 0.815242 0.809349 0.112514    0.112101    0.121571    81  LEU   A CG   
2808 C CD1  . LEU   B 69  ? 0.680302 0.754469 0.750468 0.0813221   0.0955866   0.116606    81  LEU   A CD1  
2809 C CD2  . LEU   B 69  ? 0.776563 0.844682 0.873042 0.134163    0.114995    0.141067    81  LEU   A CD2  
2810 H H    . LEU   B 69  ? 0.810379 0.826598 0.856735 0.130074    0.16197     0.0384537   81  LEU   A H    
2811 H HA   . LEU   B 69  ? 0.691032 0.788638 0.74443  0.0867311   0.120345    0.0754077   81  LEU   A HA   
2812 H HB2  . LEU   B 69  ? 0.745263 0.761772 0.811956 0.116274    0.134911    0.082421    81  LEU   A HB2  
2813 H HB3  . LEU   B 69  ? 0.754269 0.816022 0.839948 0.14836     0.145486    0.0964976   81  LEU   A HB3  
2814 H HG   . LEU   B 69  ? 0.704167 0.84156  0.797078 0.11263     0.107629    0.1311      81  LEU   A HG   
2815 H HD11 . LEU   B 69  ? 0.676617 0.768467 0.73973  0.0688489   0.0919383   0.108014    81  LEU   A HD11 
2816 H HD12 . LEU   B 69  ? 0.666981 0.752825 0.739896 0.0762102   0.0836022   0.132166    81  LEU   A HD12 
2817 H HD13 . LEU   B 69  ? 0.700321 0.735152 0.765116 0.0792293   0.100673    0.106888    81  LEU   A HD13 
2818 H HD21 . LEU   B 69  ? 0.780201 0.86528  0.889188 0.156328    0.123892    0.14693     81  LEU   A HD21 
2819 H HD22 . LEU   B 69  ? 0.785589 0.807356 0.874907 0.134211    0.121669    0.132694    81  LEU   A HD22 
2820 H HD23 . LEU   B 69  ? 0.742665 0.826092 0.840338 0.12568     0.101168    0.156629    81  LEU   A HD23 
2821 N N    . GLY   B 70  ? 0.692319 0.902318 0.770127 0.0961958   0.117272    0.107604    82  GLY   A N    
2822 C CA   . GLY   B 70  ? 0.711695 0.994277 0.807406 0.0980488   0.115594    0.127946    82  GLY   A CA   
2823 C C    . GLY   B 70  ? 0.75963  1.08146  0.847373 0.102306    0.133313    0.114309    82  GLY   A C    
2824 O O    . GLY   B 70  ? 0.804227 1.1934   0.910252 0.106424    0.137593    0.130662    82  GLY   A O    
2825 H H    . GLY   B 70  ? 0.672488 0.865667 0.740197 0.0772488   0.104819    0.106507    82  GLY   A H    
2826 H HA2  . GLY   B 70  ? 0.684457 0.981302 0.778882 0.0769088   0.0983527   0.14055     82  GLY   A HA2  
2827 H HA3  . GLY   B 70  ? 0.71271  1.0075   0.82743  0.117069    0.11956     0.139859    82  GLY   A HA3  
2828 N N    . LYS   B 71  ? 0.783197 1.06817  0.842248 0.0980416   0.142604    0.0848784   83  LYS   A N    
2829 C CA   . LYS   B 71  ? 0.824687 1.14394  0.867133 0.101791    0.160319    0.068597    83  LYS   A CA   
2830 C C    . LYS   B 71  ? 0.841161 1.17865  0.858804 0.065449    0.143503    0.0709127   83  LYS   A C    
2831 O O    . LYS   B 71  ? 0.897623 1.24816  0.888199 0.0614865   0.154243    0.05262     83  LYS   A O    
2832 C CB   . LYS   B 71  ? 0.851532 1.12119  0.875942 0.126024    0.184173    0.0329993   83  LYS   A CB   
2833 H H    . LYS   B 71  ? 0.787898 1.02818  0.836508 0.0912711   0.137343    0.0748415   83  LYS   A H    
2834 H HA   . LYS   B 71  ? 0.820227 1.18821  0.880818 0.113626    0.168219    0.0819361   83  LYS   A HA   
2837 N N    . GLY   B 72  ? 0.821428 1.15512  0.844916 0.0406005   0.117137    0.0925777   84  GLY   A N    
2838 C CA   . GLY   B 72  ? 0.808526 1.15846  0.813304 0.00851098  0.0983266   0.102886    84  GLY   A CA   
2839 C C    . GLY   B 72  ? 0.777192 1.09316  0.748813 -0.00504689 0.0932845   0.0796713   84  GLY   A C    
2840 O O    . GLY   B 72  ? 0.707964 1.04575  0.659076 -0.0262514  0.0826899   0.0866451   84  GLY   A O    
2841 H H    . GLY   B 72  ? 0.801538 1.11908  0.840032 0.0450724   0.110684    0.101483    84  GLY   A H    
2842 H HA2  . GLY   B 72  ? 0.774208 1.11628  0.788204 -0.00251892 0.0817041   0.118647    84  GLY   A HA2  
2843 H HA3  . GLY   B 72  ? 0.801619 1.19716  0.806758 0.0052061   0.103946    0.112523    84  GLY   A HA3  
2844 N N    . GLN   B 73  ? 0.70904  0.972584 0.675979 0.00476838  0.0986546   0.0547744   85  GLN   A N    
2845 C CA   . GLN   B 73  ? 0.764917 1.00051  0.704162 -0.00939023 0.0928197   0.030893    85  GLN   A CA   
2846 C C    . GLN   B 73  ? 0.727502 0.941729 0.670194 -0.0299219  0.0665101   0.041971    85  GLN   A C    
2847 O O    . GLN   B 73  ? 0.831077 1.03603  0.755577 -0.0452744  0.0553257   0.029898    85  GLN   A O    
2848 C CB   . GLN   B 73  ? 0.835861 1.0231   0.770973 0.00671146  0.110038    -0.00049484 85  GLN   A CB   
2849 C CG   . GLN   B 73  ? 0.90757  1.10724  0.838431 0.0337252   0.138555    -0.0152285  85  GLN   A CG   
2850 C CD   . GLN   B 73  ? 0.914298 1.05133  0.837688 0.0487545   0.154268    -0.0470661  85  GLN   A CD   
2851 O OE1  . GLN   B 73  ? 0.923325 1.01044  0.852999 0.039331    0.144836    -0.0520924  85  GLN   A OE1  
2852 N NE2  . GLN   B 73  ? 0.950171 1.08766  0.861113 0.0731746   0.179943    -0.0680963  85  GLN   A NE2  
2853 H H    . GLN   B 73  ? 0.737174 0.982508 0.719251 0.0194983   0.105279    0.0537614   85  GLN   A H    
2854 H HA   . GLN   B 73  ? 0.778415 1.04145  0.698216 -0.0160029  0.0952036   0.0276118   85  GLN   A HA   
2855 H HB2  . GLN   B 73  ? 0.821229 0.981513 0.774283 0.0117735   0.107546    0.00513351  85  GLN   A HB2  
2856 H HB3  . GLN   B 73  ? 0.85156  1.02311  0.76837  -0.00578985 0.10471     -0.0172351  85  GLN   A HB3  
2857 H HG2  . GLN   B 73  ? 0.906306 1.13539  0.817142 0.0288551   0.142764    -0.0213518  85  GLN   A HG2  
2858 H HG3  . GLN   B 73  ? 0.872835 1.09342  0.82542  0.0468709   0.143155    0.0027259   85  GLN   A HG3  
2859 H HE21 . GLN   B 73  ? 0.988474 1.08407  0.894496 0.0837227   0.190117    -0.0867448  85  GLN   A HE21 
2860 H HE22 . GLN   B 73  ? 0.956608 1.13556  0.863891 0.0793591   0.187693    -0.0636682  85  GLN   A HE22 
2861 N N    . VAL   B 74  ? 0.594105 0.804465 0.559937 -0.0290604  0.0562618   0.065235    86  VAL   A N    
2862 C CA   . VAL   B 74  ? 0.581259 0.769987 0.55245  -0.0421637  0.0348311   0.075653    86  VAL   A CA   
2863 C C    . VAL   B 74  ? 0.53356  0.745496 0.511874 -0.049631   0.0218911   0.104607    86  VAL   A C    
2864 O O    . VAL   B 74  ? 0.560089 0.805668 0.544313 -0.0453173  0.0304485   0.115588    86  VAL   A O    
2865 C CB   . VAL   B 74  ? 0.53519  0.681771 0.523533 -0.0318304  0.0390128   0.0686296   86  VAL   A CB   
2866 C CG1  . VAL   B 74  ? 0.597305 0.715246 0.578275 -0.0321528  0.0484643   0.0406068   86  VAL   A CG1  
2867 C CG2  . VAL   B 74  ? 0.52558  0.672747 0.530734 -0.0123245  0.05222     0.077704    86  VAL   A CG2  
2868 H H    . VAL   B 74  ? 0.613493 0.83656  0.591889 -0.0188193  0.063282    0.0744354   86  VAL   A H    
2869 H HA   . VAL   B 74  ? 0.575131 0.763429 0.533519 -0.05291    0.0267001   0.0693412   86  VAL   A HA   
2870 H HB   . VAL   B 74  ? 0.531436 0.66917  0.524333 -0.0384587  0.0261993   0.0775379   86  VAL   A HB   
2871 H HG11 . VAL   B 74  ? 0.608398 0.730042 0.581758 -0.0244654  0.0616356   0.0293793   86  VAL   A HG11 
2872 H HG12 . VAL   B 74  ? 0.588597 0.710696 0.560549 -0.0450362  0.0381429   0.0355438   86  VAL   A HG12 
2873 H HG13 . VAL   B 74  ? 0.584213 0.676078 0.576538 -0.0276975  0.0514955   0.0391414   86  VAL   A HG13 
2874 H HG21 . VAL   B 74  ? 0.525453 0.64602  0.538864 -0.00735362 0.0533489   0.0768954   86  VAL   A HG21 
2875 H HG22 . VAL   B 74  ? 0.513896 0.68288  0.523961 -0.0147445  0.0452313   0.0947678   86  VAL   A HG22 
2876 H HG23 . VAL   B 74  ? 0.547395 0.700516 0.54996  -0.00218895 0.0663927   0.0678799   86  VAL   A HG23 
2877 N N    . ILE   B 75  ? 0.525271 0.718355 0.504636 -0.06011    0.00212436  0.115855    87  ILE   A N    
2878 C CA   . ILE   B 75  ? 0.538179 0.740423 0.520787 -0.069827   -0.0121006  0.140613    87  ILE   A CA   
2879 C C    . ILE   B 75  ? 0.585113 0.788743 0.586305 -0.0587109  -0.00590825 0.14776     87  ILE   A C    
2880 O O    . ILE   B 75  ? 0.532165 0.715147 0.543094 -0.0427141  0.00489401  0.136424    87  ILE   A O    
2881 C CB   . ILE   B 75  ? 0.551402 0.723583 0.528352 -0.0787973  -0.0332082  0.14715     87  ILE   A CB   
2882 C CG1  . ILE   B 75  ? 0.5328   0.67075  0.519996 -0.0672378  -0.0312526  0.13304     87  ILE   A CG1  
2883 C CG2  . ILE   B 75  ? 0.555054 0.737279 0.514066 -0.0905029  -0.0433923  0.149335    87  ILE   A CG2  
2884 C CD1  . ILE   B 75  ? 0.604576 0.715798 0.590136 -0.0698234  -0.0488227  0.140063    87  ILE   A CD1  
2885 H H    . ILE   B 75  ? 0.529522 0.70355  0.507459 -0.061446   -0.00250464 0.107405    87  ILE   A H    
2886 H HA   . ILE   B 75  ? 0.554217 0.783172 0.529687 -0.0779219  -0.0121204  0.149104    87  ILE   A HA   
2887 H HB   . ILE   B 75  ? 0.543265 0.713279 0.521096 -0.0847326  -0.0420252  0.161203    87  ILE   A HB   
2888 H HG12 . ILE   B 75  ? 0.553621 0.691674 0.540037 -0.0652404  -0.0252432  0.119553    87  ILE   A HG12 
2889 H HG13 . ILE   B 75  ? 0.543826 0.67753  0.539628 -0.0592499  -0.023278   0.132324    87  ILE   A HG13 
2890 H HG21 . ILE   B 75  ? 0.560955 0.724941 0.518254 -0.0935918  -0.0570721  0.156036    87  ILE   A HG21 
2891 H HG22 . ILE   B 75  ? 0.562472 0.746984 0.518886 -0.0867187  -0.0367808  0.134053    87  ILE   A HG22 
2892 H HG23 . ILE   B 75  ? 0.567615 0.773    0.518751 -0.098757   -0.0430547  0.15995     87  ILE   A HG23 
2893 H HD11 . ILE   B 75  ? 0.584476 0.691395 0.566812 -0.0741338  -0.0562541  0.152024    87  ILE   A HD11 
2894 H HD12 . ILE   B 75  ? 0.57579  0.671074 0.569291 -0.0618236  -0.0445823  0.131968    87  ILE   A HD12 
2895 H HD13 . ILE   B 75  ? 0.588875 0.703273 0.568187 -0.0748315  -0.0568233  0.140912    87  ILE   A HD13 
2896 N N    . LYS   B 76  ? 0.510767 0.741177 0.516236 -0.0693958  -0.0138364  0.168563    88  LYS   A N    
2897 C CA   . LYS   B 76  ? 0.528446 0.772311 0.551374 -0.0633546  -0.0135055  0.179865    88  LYS   A CA   
2898 C C    . LYS   B 76  ? 0.480195 0.681282 0.504582 -0.0530405  -0.0178616  0.173647    88  LYS   A C    
2899 O O    . LYS   B 76  ? 0.48808  0.691624 0.525076 -0.0355178  -0.00698306 0.172203    88  LYS   A O    
2900 C CB   . LYS   B 76  ? 0.542508 0.813347 0.565275 -0.0874175  -0.0296506  0.203337    88  LYS   A CB   
2901 H H    . LYS   B 76  ? 0.539746 0.782292 0.536752 -0.0826517  -0.0208589  0.177288    88  LYS   A H    
2902 H HA   . LYS   B 76  ? 0.517878 0.78486  0.550976 -0.0508199  0.0011444   0.176712    88  LYS   A HA   
2905 N N    . ALA   B 77  ? 0.464656 0.627995 0.475851 -0.0614187  -0.0321311  0.17098     89  ALA   A N    
2906 C CA   . ALA   B 77  ? 0.458282 0.585767 0.468047 -0.0519187  -0.0339061  0.165052    89  ALA   A CA   
2907 C C    . ALA   B 77  ? 0.472336 0.587636 0.490841 -0.0336049  -0.0148319  0.151018    89  ALA   A C    
2908 O O    . ALA   B 77  ? 0.451059 0.550047 0.471834 -0.0234744  -0.011226   0.152257    89  ALA   A O    
2909 C CB   . ALA   B 77  ? 0.474871 0.568043 0.471321 -0.058624   -0.047486   0.161439    89  ALA   A CB   
2910 H H    . ALA   B 77  ? 0.473464 0.634761 0.476057 -0.0721804  -0.0401637  0.173659    89  ALA   A H    
2911 H HA   . ALA   B 77  ? 0.46561  0.599148 0.477153 -0.0526192  -0.0387058  0.173828    89  ALA   A HA   
2912 H HB1  . ALA   B 77  ? 0.481102 0.572974 0.47003  -0.0700765  -0.0602024  0.170623    89  ALA   A HB1  
2913 H HB2  . ALA   B 77  ? 0.471088 0.563244 0.467202 -0.0587202  -0.0451168  0.154793    89  ALA   A HB2  
2914 H HB3  . ALA   B 77  ? 0.472124 0.545809 0.46751  -0.051094   -0.0459286  0.156928    89  ALA   A HB3  
2915 N N    . TRP   B 78  ? 0.4767   0.59575  0.496497 -0.031462   -0.00366615 0.137714    90  TRP   A N    
2916 C CA   . TRP   B 78  ? 0.51218  0.612659 0.539019 -0.0176979  0.0140417   0.123731    90  TRP   A CA   
2917 C C    . TRP   B 78  ? 0.557977 0.671442 0.595632 -0.00069578 0.0280111   0.12909     90  TRP   A C    
2918 O O    . TRP   B 78  ? 0.499445 0.589211 0.543074 0.0128965   0.0379856   0.128597    90  TRP   A O    
2919 C CB   . TRP   B 78  ? 0.548079 0.645136 0.56981  -0.0227764  0.0202052   0.104739    90  TRP   A CB   
2920 C CG   . TRP   B 78  ? 0.547916 0.624841 0.568849 -0.0313244  0.0126592   0.0962283   90  TRP   A CG   
2921 C CD1  . TRP   B 78  ? 0.530916 0.604401 0.549606 -0.0381423  -0.00340118 0.103857    90  TRP   A CD1  
2922 C CD2  . TRP   B 78  ? 0.552275 0.610667 0.577769 -0.0330174  0.0220004   0.0780033   90  TRP   A CD2  
2923 N NE1  . TRP   B 78  ? 0.536106 0.599441 0.561137 -0.0415306  -0.00408248 0.092802    90  TRP   A NE1  
2924 C CE2  . TRP   B 78  ? 0.502418 0.557811 0.532587 -0.0413155  0.0105272   0.0774371   90  TRP   A CE2  
2925 C CE3  . TRP   B 78  ? 0.582263 0.624366 0.608706 -0.0287259  0.0387145   0.0619442   90  TRP   A CE3  
2926 C CZ2  . TRP   B 78  ? 0.486782 0.533584 0.526489 -0.0487524  0.0141828   0.0630699   90  TRP   A CZ2  
2927 C CZ3  . TRP   B 78  ? 0.595039 0.617678 0.626471 -0.0384383  0.0417387   0.0464542   90  TRP   A CZ3  
2928 C CH2  . TRP   B 78  ? 0.515212 0.546124 0.554508 -0.0503327  0.0287435   0.0474021   90  TRP   A CH2  
2929 H H    . TRP   B 78  ? 0.485533 0.616669 0.49989  -0.0397311  -0.00754019 0.137357    90  TRP   A H    
2930 H HA   . TRP   B 78  ? 0.515498 0.594745 0.542973 -0.0159549  0.0126269   0.123373    90  TRP   A HA   
2931 H HB2  . TRP   B 78  ? 0.543102 0.661489 0.558327 -0.0292502  0.016289    0.106578    90  TRP   A HB2  
2932 H HB3  . TRP   B 78  ? 0.554143 0.643882 0.579231 -0.0139364  0.03363     0.0960081   90  TRP   A HB3  
2933 H HD1  . TRP   B 78  ? 0.529249 0.607444 0.543063 -0.0407758  -0.0130757  0.114823    90  TRP   A HD1  
2934 H HE1  . TRP   B 78  ? 0.520131 0.581567 0.54674  -0.0431399  -0.0122522  0.0952896   90  TRP   A HE1  
2935 H HE3  . TRP   B 78  ? 0.58843  0.631889 0.613159 -0.019419   0.0477641   0.0619352   90  TRP   A HE3  
2936 H HZ2  . TRP   B 78  ? 0.488961 0.540937 0.535484 -0.0528254  0.00670849  0.063903    90  TRP   A HZ2  
2937 H HZ3  . TRP   B 78  ? 0.600316 0.606147 0.630151 -0.0377404  0.0522253   0.0342522   90  TRP   A HZ3  
2938 H HH2  . TRP   B 78  ? 0.538823 0.562241 0.584839 -0.0585201  0.0308345   0.0376297   90  TRP   A HH2  
2939 N N    . ASP   B 79  ? 0.497693 0.650453 0.539115 -1.525e-05  0.0302042   0.135571    91  ASP   A N    
2940 C CA   . ASP   B 79  ? 0.507688 0.681306 0.56433  0.0205941   0.0442451   0.141646    91  ASP   A CA   
2941 C C    . ASP   B 79  ? 0.512419 0.688031 0.577737 0.0259892   0.0347157   0.161008    91  ASP   A C    
2942 O O    . ASP   B 79  ? 0.528042 0.694536 0.603192 0.0468006   0.0449087   0.165404    91  ASP   A O    
2943 C CB   . ASP   B 79  ? 0.515437 0.742182 0.577462 0.0192996   0.0488741   0.146968    91  ASP   A CB   
2944 C CG   . ASP   B 79  ? 0.527937 0.757597 0.580659 0.0260906   0.0672406   0.125858    91  ASP   A CG   
2945 O OD1  . ASP   B 79  ? 0.618386 0.806226 0.665764 0.0377167   0.0795342   0.106245    91  ASP   A OD1  
2946 O OD2  . ASP   B 79  ? 0.561027 0.834233 0.609923 0.018377    0.0695544   0.129148    91  ASP   A OD2  
2947 H H    . ASP   B 79  ? 0.508181 0.676761 0.54354  -0.011724   0.0233903   0.137364    91  ASP   A H    
2948 H HA   . ASP   B 79  ? 0.525846 0.677412 0.58297  0.0324542   0.0573559   0.129838    91  ASP   A HA   
2949 H HB2  . ASP   B 79  ? 0.5023   0.743374 0.55897  0.00162416  0.0357814   0.155199    91  ASP   A HB2  
2950 H HB3  . ASP   B 79  ? 0.513007 0.763201 0.589844 0.0311176   0.0526229   0.157872    91  ASP   A HB3  
2951 N N    . ILE   B 80  ? 0.536798 0.717767 0.594371 0.0069311   0.0141534   0.171823    92  ILE   A N    
2952 C CA   . ILE   B 80  ? 0.550379 0.732248 0.608293 0.00787096  0.00202326  0.187111    92  ILE   A CA   
2953 C C    . ILE   B 80  ? 0.500246 0.635243 0.547925 0.0165572   0.00660245  0.180764    92  ILE   A C    
2954 O O    . ILE   B 80  ? 0.477992 0.609712 0.529613 0.0318949   0.0109748   0.190514    92  ILE   A O    
2955 C CB   . ILE   B 80  ? 0.590045 0.782587 0.637228 -0.0175192  -0.0213358  0.196234    92  ILE   A CB   
2956 C CG1  . ILE   B 80  ? 0.605353 0.853358 0.667206 -0.0284337  -0.0254587  0.209556    92  ILE   A CG1  
2957 C CG2  . ILE   B 80  ? 0.690161 0.869393 0.7263   -0.0195941  -0.0355653  0.204532    92  ILE   A CG2  
2958 C CD1  . ILE   B 80  ? 0.648258 0.89376  0.69619  -0.0588171  -0.0463035  0.21567     92  ILE   A CD1  
2959 H H    . ILE   B 80  ? 0.526755 0.709188 0.576524 -0.00712355 0.00696936  0.16937     92  ILE   A H    
2960 H HA   . ILE   B 80  ? 0.546327 0.753829 0.617755 0.0193583   0.00641987  0.196364    92  ILE   A HA   
2961 H HB   . ILE   B 80  ? 0.599243 0.770084 0.635313 -0.0266473  -0.0245715  0.187759    92  ILE   A HB   
2962 H HG12 . ILE   B 80  ? 0.611572 0.88584  0.685606 -0.0223733  -0.0271808  0.220606    92  ILE   A HG12 
2963 H HG13 . ILE   B 80  ? 0.607415 0.86803  0.675829 -0.0217229  -0.0123937  0.204014    92  ILE   A HG13 
2964 H HG21 . ILE   B 80  ? 0.664631 0.850668 0.693979 -0.036365   -0.0506521  0.209714    92  ILE   A HG21 
2965 H HG22 . ILE   B 80  ? 0.663246 0.861349 0.709785 -0.0078075  -0.0320979  0.213274    92  ILE   A HG22 
2966 H HG23 . ILE   B 80  ? 0.662761 0.808285 0.687111 -0.0161004  -0.033183   0.19615     92  ILE   A HG23 
2967 H HD11 . ILE   B 80  ? 0.636563 0.855661 0.672745 -0.0625364  -0.0457481  0.20637     92  ILE   A HD11 
2968 H HD12 . ILE   B 80  ? 0.636593 0.919523 0.69487  -0.0678592  -0.047221   0.225444    92  ILE   A HD12 
2969 H HD13 . ILE   B 80  ? 0.643787 0.876407 0.683532 -0.0658605  -0.0594588  0.219634    92  ILE   A HD13 
2970 N N    . GLY   B 81  ? 0.448416 0.551428 0.484468 0.00735072  0.00622717  0.166675    93  GLY   A N    
2971 C CA   . GLY   B 81  ? 0.475872 0.542642 0.502937 0.0109742   0.00958661  0.162637    93  GLY   A CA   
2972 C C    . GLY   B 81  ? 0.487318 0.531624 0.522642 0.0263321   0.029682    0.15888     93  GLY   A C    
2973 O O    . GLY   B 81  ? 0.522719 0.54885  0.553463 0.034547    0.0343864   0.167321    93  GLY   A O    
2974 H H    . GLY   B 81  ? 0.460394 0.567708 0.494798 -0.00136492 0.00399497  0.160454    93  GLY   A H    
2975 H HA2  . GLY   B 81  ? 0.475382 0.543231 0.494859 0.0108397   0.00157816  0.17157     93  GLY   A HA2  
2976 H HA3  . GLY   B 81  ? 0.466002 0.520806 0.48749  0.00229903  0.00592675  0.154069    93  GLY   A HA3  
2977 N N    . VAL   B 82  ? 0.467475 0.509326 0.511395 0.0286421   0.0415607   0.145852    94  VAL   A N    
2978 C CA   . VAL   B 82  ? 0.534398 0.544592 0.583885 0.0397085   0.0600647   0.13917     94  VAL   A CA   
2979 C C    . VAL   B 82  ? 0.542709 0.556004 0.600075 0.0628053   0.0680759   0.155536    94  VAL   A C    
2980 O O    . VAL   B 82  ? 0.556198 0.535007 0.614007 0.0730596   0.0797808   0.160289    94  VAL   A O    
2981 C CB   . VAL   B 82  ? 0.514325 0.515638 0.565124 0.0337548   0.0690388   0.116483    94  VAL   A CB   
2982 C CG1  . VAL   B 82  ? 0.664584 0.625598 0.719195 0.0447537   0.088365    0.107789    94  VAL   A CG1  
2983 C CG2  . VAL   B 82  ? 0.56045  0.557664 0.606491 0.0131877   0.0602172   0.10442     94  VAL   A CG2  
2984 H H    . VAL   B 82  ? 0.475693 0.533625 0.519858 0.0222843   0.0379792   0.140767    94  VAL   A H    
2985 H HA   . VAL   B 82  ? 0.521279 0.511927 0.567171 0.0354523   0.0609637   0.139591    94  VAL   A HA   
2986 H HB   . VAL   B 82  ? 0.545092 0.570463 0.596523 0.035901    0.0676326   0.11534     94  VAL   A HB   
2987 H HG11 . VAL   B 82  ? 0.633855 0.573683 0.688844 0.0434244   0.0906057   0.113979    94  VAL   A HG11 
2988 H HG12 . VAL   B 82  ? 0.639565 0.604515 0.698337 0.0610646   0.0949318   0.113412    94  VAL   A HG12 
2989 H HG13 . VAL   B 82  ? 0.637115 0.589173 0.688954 0.0365261   0.0918265   0.0907288   94  VAL   A HG13 
2990 H HG21 . VAL   B 82  ? 0.550366 0.545011 0.595418 0.00804725  0.0639037   0.0902392   94  VAL   A HG21 
2991 H HG22 . VAL   B 82  ? 0.524078 0.540599 0.566365 0.00734297  0.0480794   0.109769    94  VAL   A HG22 
2992 H HG23 . VAL   B 82  ? 0.545371 0.524222 0.593001 0.0110712   0.0628543   0.106005    94  VAL   A HG23 
2993 N N    . ALA   B 83  ? 0.517839 0.574342 0.58292  0.0703314   0.0609371   0.167384    95  ALA   A N    
2994 C CA   . ALA   B 83  ? 0.505617 0.575364 0.582827 0.0948017   0.0659098   0.186185    95  ALA   A CA   
2995 C C    . ALA   B 83  ? 0.546055 0.602553 0.613767 0.0975898   0.0583833   0.205254    95  ALA   A C    
2996 O O    . ALA   B 83  ? 0.575787 0.631316 0.650731 0.11953     0.0636587   0.2225      95  ALA   A O    
2997 C CB   . ALA   B 83  ? 0.540363 0.671612 0.63314  0.100061    0.0582472   0.197969    95  ALA   A CB   
2998 H H    . ALA   B 83  ? 0.49887  0.578569 0.562996 0.0598507   0.0526856   0.164983    95  ALA   A H    
2999 H HA   . ALA   B 83  ? 0.547495 0.594316 0.629454 0.108239    0.0807293   0.17992     95  ALA   A HA   
3000 H HB1  . ALA   B 83  ? 0.525148 0.667271 0.622168 0.099418    0.065111    0.186753    95  ALA   A HB1  
3001 H HB2  . ALA   B 83  ? 0.509651 0.659851 0.597065 0.0848369   0.0428656   0.204185    95  ALA   A HB2  
3002 H HB3  . ALA   B 83  ? 0.539567 0.681539 0.643367 0.1189      0.0618787   0.211052    95  ALA   A HB3  
3003 N N    . THR   B 84  ? 0.571375 0.621091 0.621391 0.0774447   0.0456723   0.203157    96  THR   A N    
3004 C CA   . THR   B 84  ? 0.582399 0.621653 0.616133 0.0788083   0.0394479   0.218593    96  THR   A CA   
3005 C C    . THR   B 84  ? 0.588877 0.580529 0.615194 0.0802237   0.0557756   0.215563    96  THR   A C    
3006 O O    . THR   B 84  ? 0.5617   0.543274 0.572207 0.0826588   0.0548862   0.229757    96  THR   A O    
3007 C CB   . THR   B 84  ? 0.586155 0.638911 0.600624 0.0587436   0.0194584   0.215895    96  THR   A CB   
3008 O OG1  . THR   B 84  ? 0.536985 0.564127 0.543512 0.0447751   0.0228703   0.197267    96  THR   A OG1  
3009 C CG2  . THR   B 84  ? 0.564362 0.660402 0.58652  0.0493246   0.00238531  0.218691    96  THR   A CG2  
3010 H H    . THR   B 84  ? 0.545595 0.5977   0.592161 0.0636422   0.0410263   0.191836    96  THR   A H    
3011 H HA   . THR   B 84  ? 0.594172 0.649356 0.633053 0.0920892   0.0374242   0.234144    96  THR   A HA   
3012 H HB   . THR   B 84  ? 0.587294 0.638154 0.588427 0.0616319   0.0149393   0.226655    96  THR   A HB   
3014 H HG21 . THR   B 84  ? 0.565344 0.66274  0.572463 0.0368102   -0.0110115  0.218035    96  THR   A HG21 
3015 H HG22 . THR   B 84  ? 0.553432 0.6527   0.584732 0.0446865   0.00621047  0.208609    96  THR   A HG22 
3016 H HG23 . THR   B 84  ? 0.571812 0.691719 0.604479 0.0599527   0.00100432  0.23182     96  THR   A HG23 
3017 N N    . MET   B 85  ? 0.598413 0.563013 0.63363  0.0753355   0.069796    0.197604    97  MET   A N    
3018 C CA   . MET   B 85  ? 0.613343 0.539871 0.643033 0.0674869   0.0822376   0.194462    97  MET   A CA   
3019 C C    . MET   B 85  ? 0.639961 0.528372 0.675031 0.0824148   0.0996314   0.205619    97  MET   A C    
3020 O O    . MET   B 85  ? 0.625405 0.509068 0.671553 0.0997633   0.10542     0.206351    97  MET   A O    
3021 C CB   . MET   B 85  ? 0.589942 0.509168 0.626496 0.048692    0.0849212   0.169532    97  MET   A CB   
3022 C CG   . MET   B 85  ? 0.538027 0.485771 0.567959 0.0356466   0.0681609   0.161407    97  MET   A CG   
3023 S SD   . MET   B 85  ? 0.567967 0.514067 0.608742 0.0173306   0.0688947   0.136292    97  MET   A SD   
3024 C CE   . MET   B 85  ? 0.604554 0.526556 0.650262 0.00840873  0.0831972   0.136666    97  MET   A CE   
3025 H H    . MET   B 85  ? 0.589573 0.561267 0.633851 0.0755493   0.071612    0.187529    97  MET   A H    
3026 H HA   . MET   B 85  ? 0.608207 0.538854 0.625364 0.0639716   0.0773347   0.202441    97  MET   A HA   
3027 H HB2  . MET   B 85  ? 0.590788 0.507439 0.63541  0.0511868   0.0887482   0.159981    97  MET   A HB2  
3028 H HB3  . MET   B 85  ? 0.601345 0.499204 0.638354 0.0425776   0.0938593   0.168603    97  MET   A HB3  
3029 H HG2  . MET   B 85  ? 0.551865 0.498983 0.571871 0.0339884   0.0657179   0.167637    97  MET   A HG2  
3030 H HG3  . MET   B 85  ? 0.540138 0.508236 0.56923  0.038794    0.0589291   0.164168    97  MET   A HG3  
3031 H HE1  . MET   B 85  ? 0.594541 0.51941  0.649225 -0.00254542 0.0830416   0.12426     97  MET   A HE1  
3032 H HE2  . MET   B 85  ? 0.621453 0.5225   0.668798 0.0126304   0.0938719   0.142539    97  MET   A HE2  
3033 H HE3  . MET   B 85  ? 0.595818 0.524225 0.633543 0.00983047  0.0805941   0.144021    97  MET   A HE3  
3034 N N    . LYS   B 86  ? 0.671731 0.531287 0.698456 0.0760647   0.109317    0.215029    98  LYS   A N    
3035 C CA   . LYS   B 86  ? 0.755378 0.567971 0.78459  0.0855827   0.12626     0.228126    98  LYS   A CA   
3036 C C    . LYS   B 86  ? 0.739295 0.516315 0.777705 0.0645946   0.139248    0.208026    98  LYS   A C    
3037 O O    . LYS   B 86  ? 0.683422 0.479584 0.725462 0.0438066   0.134642    0.189987    98  LYS   A O    
3038 C CB   . LYS   B 86  ? 0.790996 0.598149 0.802293 0.0921782   0.127822    0.258939    98  LYS   A CB   
3039 C CG   . LYS   B 86  ? 0.863339 0.703471 0.866506 0.11381     0.113545    0.28034     98  LYS   A CG   
3040 C CD   . LYS   B 86  ? 1.03292  0.875793 1.01037  0.117492    0.111283    0.309413    98  LYS   A CD   
3041 C CE   . LYS   B 86  ? 1.09558  0.96881  1.06871  0.140646    0.0964773   0.333429    98  LYS   A CE   
3042 N NZ   . LYS   B 86  ? 1.11349  1.03778  1.09078  0.135021    0.0764086   0.318151    98  LYS   A NZ   
3043 H H    . LYS   B 86  ? 0.665374 0.533778 0.684247 0.0654093   0.105957    0.213923    98  LYS   A H    
3044 H HA   . LYS   B 86  ? 0.755787 0.564493 0.79198  0.102075    0.127587    0.230326    98  LYS   A HA   
3045 H HB2  . LYS   B 86  ? 0.791685 0.60977  0.79424  0.0783834   0.126376    0.256372    98  LYS   A HB2  
3046 H HB3  . LYS   B 86  ? 0.841231 0.612075 0.853686 0.0949646   0.140017    0.268505    98  LYS   A HB3  
3047 H HG2  . LYS   B 86  ? 0.89223  0.722494 0.906269 0.130649    0.116939    0.285965    98  LYS   A HG2  
3048 H HG3  . LYS   B 86  ? 0.842182 0.715155 0.846001 0.109198    0.101296    0.269713    98  LYS   A HG3  
3049 H HD2  . LYS   B 86  ? 0.990972 0.850417 0.955666 0.104057    0.106419    0.3023      98  LYS   A HD2  
3050 H HD3  . LYS   B 86  ? 1.04225  0.851192 1.01752  0.117391    0.124522    0.320158    98  LYS   A HD3  
3051 H HE2  . LYS   B 86  ? 1.11777  0.993217 1.07083  0.142228    0.0940904   0.352058    98  LYS   A HE2  
3052 H HE3  . LYS   B 86  ? 1.11651  0.975012 1.10406  0.157457    0.102036    0.341145    98  LYS   A HE3  
3053 H HZ1  . LYS   B 86  ? 1.07248  1.0012   1.0405   0.119011    0.0736631   0.304525    98  LYS   A HZ1  
3054 H HZ2  . LYS   B 86  ? 1.07717  1.00529  1.07332  0.139479    0.077821    0.308037    98  LYS   A HZ2  
3055 H HZ3  . LYS   B 86  ? 1.09819  1.04683  1.068    0.142804    0.0648669   0.333079    98  LYS   A HZ3  
3056 N N    . LYS   B 87  ? 0.761608 0.486525 0.804633 0.0706301   0.154048    0.210729    99  LYS   A N    
3057 C CA   . LYS   B 87  ? 0.896723 0.583246 0.947792 0.0471876   0.16489     0.190326    99  LYS   A CA   
3058 C C    . LYS   B 87  ? 0.918753 0.611923 0.96985  0.0211956   0.168616    0.197742    99  LYS   A C    
3059 O O    . LYS   B 87  ? 0.836864 0.530788 0.877096 0.0256454   0.172676    0.224909    99  LYS   A O    
3060 C CB   . LYS   B 87  ? 1.00757  0.625205 1.05912  0.0581601   0.180345    0.193692    99  LYS   A CB   
3061 C CG   . LYS   B 87  ? 1.13005  0.70113  1.18735  0.0299764   0.189763    0.168925    99  LYS   A CG   
3062 C CD   . LYS   B 87  ? 1.3216   0.824122 1.37544  0.0471728   0.201905    0.15939     99  LYS   A CD   
3063 C CE   . LYS   B 87  ? 1.4494   0.875665 1.5023   0.0230029   0.215366    0.155196    99  LYS   A CE   
3064 N NZ   . LYS   B 87  ? 1.47987  0.919612 1.54083  -0.0204002  0.211063    0.129818    99  LYS   A NZ   
3065 H H    . LYS   B 87  ? 0.815409 0.527377 0.856445 0.0894018   0.156738    0.22565     99  LYS   A H    
3066 H HA   . LYS   B 87  ? 0.86009  0.563475 0.916157 0.0403918   0.159281    0.168388    99  LYS   A HA   
3067 H HB2  . LYS   B 87  ? 1.02078  0.640173 1.07328  0.0786332   0.179107    0.189261    99  LYS   A HB2  
3068 H HB3  . LYS   B 87  ? 1.04206  0.641586 1.08808  0.0649861   0.18552     0.218066    99  LYS   A HB3  
3069 H HG2  . LYS   B 87  ? 1.15059  0.708308 1.20894  0.0130187   0.195112    0.18031     99  LYS   A HG2  
3070 H HG3  . LYS   B 87  ? 1.10162  0.700814 1.16318  0.0168794   0.182445    0.147553    99  LYS   A HG3  
3071 H HD2  . LYS   B 87  ? 1.28866  0.803029 1.34278  0.050439    0.198595    0.135874    99  LYS   A HD2  
3072 H HD3  . LYS   B 87  ? 1.31358  0.810126 1.36458  0.0736955   0.204069    0.179229    99  LYS   A HD3  
3073 H HE2  . LYS   B 87  ? 1.4922   0.87338  1.54043  0.0360531   0.222177    0.14434     99  LYS   A HE2  
3074 H HE3  . LYS   B 87  ? 1.46693  0.876652 1.51814  0.0231866   0.22063     0.1818      99  LYS   A HE3  
3075 H HZ1  . LYS   B 87  ? 1.4372   0.903664 1.49841  -0.0207726  0.203748    0.108416    99  LYS   A HZ1  
3076 H HZ2  . LYS   B 87  ? 1.4337   0.905137 1.5003   -0.0325888  0.208242    0.142634    99  LYS   A HZ2  
3077 H HZ3  . LYS   B 87  ? 1.5146   0.90541  1.57471  -0.0352113  0.21832     0.122997    99  LYS   A HZ3  
3078 N N    . GLY   B 88  ? 0.867479 0.576268 0.930576 -0.0046376  0.166031    0.173788    100 GLY   A N    
3079 C CA   . GLY   B 88  ? 0.807566 0.535471 0.877569 -0.0278628  0.170357    0.178848    100 GLY   A CA   
3080 C C    . GLY   B 88  ? 0.750393 0.533896 0.813472 -0.0214308  0.159564    0.1831      100 GLY   A C    
3081 O O    . GLY   B 88  ? 0.797176 0.603445 0.866719 -0.0358372  0.164298    0.185281    100 GLY   A O    
3082 H H    . GLY   B 88  ? 0.854025 0.564994 0.921619 -0.00720058 0.161653    0.154476    100 GLY   A H    
3083 H HA2  . GLY   B 88  ? 0.817022 0.545392 0.899799 -0.0465915  0.170223    0.161609    100 GLY   A HA2  
3084 H HA3  . GLY   B 88  ? 0.851321 0.554138 0.917845 -0.0302455  0.181365    0.196756    100 GLY   A HA3  
3085 N N    . GLU   B 89  ? 0.752003 0.557639 0.802817 -0.00098805 0.14572     0.183465    101 GLU   A N    
3086 C CA   . GLU   B 89  ? 0.733556 0.581586 0.773932 0.00319118  0.133844    0.183997    101 GLU   A CA   
3087 C C    . GLU   B 89  ? 0.661465 0.537628 0.717029 -0.0107656  0.124897    0.160166    101 GLU   A C    
3088 O O    . GLU   B 89  ? 0.688223 0.561586 0.755527 -0.017424   0.119937    0.142409    101 GLU   A O    
3089 C CB   . GLU   B 89  ? 0.739212 0.601057 0.76407  0.0234407   0.119587    0.191238    101 GLU   A CB   
3090 C CG   . GLU   B 89  ? 0.67642  0.570701 0.6838   0.0265344   0.105716    0.191954    101 GLU   A CG   
3091 C CD   . GLU   B 89  ? 0.648815 0.557277 0.644084 0.040917    0.0905377   0.200767    101 GLU   A CD   
3092 O OE1  . GLU   B 89  ? 0.665237 0.564414 0.656545 0.0551993   0.0931343   0.219825    101 GLU   A OE1  
3093 O OE2  . GLU   B 89  ? 0.635955 0.566795 0.628716 0.0373728   0.07496     0.189314    101 GLU   A OE2  
3094 H H    . GLU   B 89  ? 0.756583 0.550016 0.805641 0.010237    0.143734    0.182942    101 GLU   A H    
3095 H HA   . GLU   B 89  ? 0.737164 0.587109 0.770199 0.001496    0.140909    0.196153    101 GLU   A HA   
3096 H HB2  . GLU   B 89  ? 0.748356 0.594514 0.766253 0.033655    0.124435    0.207423    101 GLU   A HB2  
3097 H HB3  . GLU   B 89  ? 0.713347 0.577783 0.746078 0.0248067   0.114103    0.179821    101 GLU   A HB3  
3098 H HG2  . GLU   B 89  ? 0.658367 0.56597  0.67274  0.0189811   0.100095    0.177248    101 GLU   A HG2  
3099 H HG3  . GLU   B 89  ? 0.693473 0.586887 0.689841 0.0261884   0.112011    0.201515    101 GLU   A HG3  
3100 N N    . ILE   B 90  ? 0.659477 0.562653 0.713569 -0.0139246  0.123902    0.160192    102 ILE   A N    
3101 C CA   . ILE   B 90  ? 0.607637 0.541111 0.671053 -0.0176618  0.110572    0.142638    102 ILE   A CA   
3102 C C    . ILE   B 90  ? 0.606085 0.5522   0.646397 -0.00296704 0.0971232   0.145426    102 ILE   A C    
3103 O O    . ILE   B 90  ? 0.604167 0.551577 0.625692 0.00461514  0.102149    0.155769    102 ILE   A O    
3104 C CB   . ILE   B 90  ? 0.616667 0.572795 0.70213  -0.0308179  0.118893    0.13722     102 ILE   A CB   
3105 C CG1  . ILE   B 90  ? 0.688403 0.629498 0.796607 -0.0521234  0.13099     0.134932    102 ILE   A CG1  
3106 C CG2  . ILE   B 90  ? 0.5538   0.541599 0.6504   -0.0298268  0.103638    0.12211     102 ILE   A CG2  
3107 C CD1  . ILE   B 90  ? 0.66514  0.636297 0.801263 -0.0693941  0.140714    0.133629    102 ILE   A CD1  
3108 H H    . ILE   B 90  ? 0.666333 0.568558 0.712658 -0.0123299  0.132176    0.171875    102 ILE   A H    
3109 H HA   . ILE   B 90  ? 0.607441 0.538839 0.677935 -0.021379   0.104115    0.132655    102 ILE   A HA   
3110 H HB   . ILE   B 90  ? 0.626269 0.58659  0.703239 -0.0260335  0.127226    0.146916    102 ILE   A HB   
3111 H HG12 . ILE   B 90  ? 0.665238 0.601178 0.778575 -0.0569649  0.123025    0.123037    102 ILE   A HG12 
3112 H HG13 . ILE   B 90  ? 0.693755 0.609016 0.792866 -0.0506312  0.140326    0.14652     102 ILE   A HG13 
3113 H HG21 . ILE   B 90  ? 0.56449  0.571656 0.678375 -0.0359912  0.109349    0.120207    102 ILE   A HG21 
3114 H HG22 . ILE   B 90  ? 0.555514 0.541727 0.65749  -0.0349178  0.0948304   0.113386    102 ILE   A HG22 
3115 H HG23 . ILE   B 90  ? 0.557267 0.547722 0.637827 -0.0178006  0.0968445   0.123744    102 ILE   A HG23 
3116 H HD11 . ILE   B 90  ? 0.67951  0.658591 0.809663 -0.0639124  0.150579    0.145062    102 ILE   A HD11 
3117 H HD12 . ILE   B 90  ? 0.69152  0.6487   0.840035 -0.08593    0.147132    0.132626    102 ILE   A HD12 
3118 H HD13 . ILE   B 90  ? 0.65111  0.649016 0.798996 -0.069733   0.130784    0.12287     102 ILE   A HD13 
3119 N N    . ALA   B 91  ? 0.525098 0.480644 0.565507 -0.00188616 0.0799154   0.134851    103 ALA   A N    
3120 C CA   . ALA   B 91  ? 0.537374 0.499556 0.556586 0.00681983  0.0642158   0.136234    103 ALA   A CA   
3121 C C    . ALA   B 91  ? 0.503134 0.479472 0.530241 0.00317217  0.0506163   0.123061    103 ALA   A C    
3122 O O    . ALA   B 91  ? 0.511575 0.497158 0.559238 -0.00569316 0.0497004   0.114039    103 ALA   A O    
3123 C CB   . ALA   B 91  ? 0.524307 0.483483 0.533943 0.0115277   0.0552552   0.143806    103 ALA   A CB   
3124 H H    . ALA   B 91  ? 0.536854 0.493745 0.589366 -0.00829226 0.0777769   0.126767    103 ALA   A H    
3125 H HA   . ALA   B 91  ? 0.540692 0.501254 0.54642  0.0118971   0.0680536   0.141415    103 ALA   A HA   
3126 H HB1  . ALA   B 91  ? 0.54175  0.49237  0.547071 0.0164716   0.0629109   0.154036    103 ALA   A HB1  
3127 H HB2  . ALA   B 91  ? 0.519    0.480964 0.540007 0.00773838  0.0535331   0.137956    103 ALA   A HB2  
3128 H HB3  . ALA   B 91  ? 0.52481  0.489231 0.52132  0.0134142   0.0436217   0.144781    103 ALA   A HB3  
3129 N N    . HIS   B 92  ? 0.514918 0.489726 0.522895 0.00998824  0.0398394   0.12241     104 HIS   A N    
3130 C CA   . HIS   B 92  ? 0.521072 0.499576 0.529355 0.010045    0.0238138   0.114341    104 HIS   A CA   
3131 C C    . HIS   B 92  ? 0.517047 0.487771 0.506414 0.00667308  0.00592816  0.118837    104 HIS   A C    
3132 O O    . HIS   B 92  ? 0.537663 0.499576 0.50532  0.00878326  0.00266707  0.125085    104 HIS   A O    
3133 C CB   . HIS   B 92  ? 0.497658 0.472373 0.496976 0.0215491   0.0265034   0.108976    104 HIS   A CB   
3134 C CG   . HIS   B 92  ? 0.495792 0.490685 0.521419 0.0237351   0.041982    0.105184    104 HIS   A CG   
3135 N ND1  . HIS   B 92  ? 0.549078 0.550334 0.574091 0.0374121   0.0492493   0.0999752   104 HIS   A ND1  
3136 C CD2  . HIS   B 92  ? 0.538618 0.550216 0.591938 0.0130986   0.0529526   0.105919    104 HIS   A CD2  
3137 C CE1  . HIS   B 92  ? 0.55017  0.580497 0.607708 0.0344247   0.0633504   0.0995832   104 HIS   A CE1  
3138 N NE2  . HIS   B 92  ? 0.573923 0.608844 0.648325 0.0172049   0.0645004   0.102886    104 HIS   A NE2  
3139 H H    . HIS   B 92  ? 0.528728 0.496885 0.520342 0.0149677   0.0422367   0.127562    104 HIS   A H    
3140 H HA   . HIS   B 92  ? 0.498882 0.487947 0.525025 0.0048077   0.0230171   0.110101    104 HIS   A HA   
3141 H HB2  . HIS   B 92  ? 0.521748 0.486603 0.501105 0.0257773   0.0298425   0.111974    104 HIS   A HB2  
3142 H HB3  . HIS   B 92  ? 0.509729 0.478509 0.50372  0.023767    0.0140424   0.105317    104 HIS   A HB3  
3144 H HD2  . HIS   B 92  ? 0.524671 0.533762 0.583495 0.00418069  0.0523528   0.107131    104 HIS   A HD2  
3145 H HE1  . HIS   B 92  ? 0.564487 0.610158 0.631475 0.0430541   0.0717306   0.0969838   104 HIS   A HE1  
3147 N N    . LEU   B 93  ? 0.50265  0.480161 0.499543 -0.00046708 -0.00695975 0.116842    105 LEU   A N    
3148 C CA   . LEU   B 93  ? 0.506535 0.482576 0.49015  -0.00816118 -0.0231352  0.12335     105 LEU   A CA   
3149 C C    . LEU   B 93  ? 0.52363  0.489203 0.501621 -0.0104102  -0.0393503  0.121372    105 LEU   A C    
3150 O O    . LEU   B 93  ? 0.539708 0.514959 0.533552 -0.00903681 -0.0392297  0.117268    105 LEU   A O    
3151 C CB   . LEU   B 93  ? 0.509887 0.506337 0.507023 -0.0152436  -0.0199773  0.12632     105 LEU   A CB   
3152 C CG   . LEU   B 93  ? 0.536542 0.538984 0.539484 -0.0104897  -0.00593106 0.130672    105 LEU   A CG   
3153 C CD1  . LEU   B 93  ? 0.584862 0.605895 0.598258 -0.014933   -0.00371536 0.129573    105 LEU   A CD1  
3154 C CD2  . LEU   B 93  ? 0.519731 0.520128 0.507177 -0.00728862 -0.0111867  0.141654    105 LEU   A CD2  
3155 H H    . LEU   B 93  ? 0.497096 0.482886 0.508036 -0.00174902 -0.00562879 0.112327    105 LEU   A H    
3156 H HA   . LEU   B 93  ? 0.521733 0.490781 0.491076 -0.00722809 -0.0254297  0.127449    105 LEU   A HA   
3157 H HB2  . LEU   B 93  ? 0.506404 0.508913 0.514691 -0.0168754  -0.0174347  0.120451    105 LEU   A HB2  
3158 H HB3  . LEU   B 93  ? 0.513537 0.51466  0.504664 -0.0218244  -0.0307267  0.131284    105 LEU   A HB3  
3159 H HG   . LEU   B 93  ? 0.537083 0.533115 0.54682  -0.00652355 0.00535902  0.126728    105 LEU   A HG   
3160 H HD11 . LEU   B 93  ? 0.563741 0.585891 0.583537 -0.0182899  -0.00176064 0.121389    105 LEU   A HD11 
3161 H HD12 . LEU   B 93  ? 0.569554 0.591736 0.587681 -0.00902515 0.00597042  0.13173     105 LEU   A HD12 
3162 H HD13 . LEU   B 93  ? 0.565401 0.596701 0.573557 -0.0202593  -0.0137335  0.135049    105 LEU   A HD13 
3163 H HD21 . LEU   B 93  ? 0.537302 0.525028 0.515013 -0.00342971 -0.00976625 0.140269    105 LEU   A HD21 
3164 H HD22 . LEU   B 93  ? 0.529005 0.534799 0.509873 -0.0140924  -0.023693   0.145231    105 LEU   A HD22 
3165 H HD23 . LEU   B 93  ? 0.527309 0.534564 0.520439 -0.00253698 -0.00379365 0.146967    105 LEU   A HD23 
3166 N N    . LEU   B 94  ? 0.549112 0.492064 0.5038   -0.0130252  -0.0532865  0.124053    106 LEU   A N    
3167 C CA   . LEU   B 94  ? 0.606352 0.528505 0.551789 -0.0161999  -0.0705201  0.125403    106 LEU   A CA   
3168 C C    . LEU   B 94  ? 0.612512 0.53936  0.54967  -0.0359108  -0.0847296  0.137708    106 LEU   A C    
3169 O O    . LEU   B 94  ? 0.594003 0.522646 0.519818 -0.044434   -0.0882436  0.141982    106 LEU   A O    
3170 C CB   . LEU   B 94  ? 0.656432 0.54054  0.57958  -0.00465699 -0.074564   0.116607    106 LEU   A CB   
3171 C CG   . LEU   B 94  ? 0.699096 0.547682 0.609969 -0.00357035 -0.0920886  0.117623    106 LEU   A CG   
3172 C CD1  . LEU   B 94  ? 0.708664 0.571924 0.644459 0.00992946  -0.0893901  0.117907    106 LEU   A CD1  
3173 C CD2  . LEU   B 94  ? 0.756234 0.556862 0.634784 0.00568589  -0.0965315  0.105648    106 LEU   A CD2  
3174 H H    . LEU   B 94  ? 0.564093 0.502158 0.506992 -0.0134836  -0.0528639  0.125475    106 LEU   A H    
3175 H HA   . LEU   B 94  ? 0.592232 0.524484 0.551973 -0.0132299  -0.0694972  0.124706    106 LEU   A HA   
3176 H HB2  . LEU   B 94  ? 0.65106  0.540755 0.582505 0.00821188  -0.062467   0.10983     106 LEU   A HB2  
3177 H HB3  . LEU   B 94  ? 0.666928 0.542281 0.573198 -0.00931719 -0.076611   0.116318    106 LEU   A HB3  
3178 H HG   . LEU   B 94  ? 0.704763 0.552396 0.611254 -0.0191298  -0.103368   0.126983    106 LEU   A HG   
3179 H HD11 . LEU   B 94  ? 0.677336 0.567185 0.627478 0.00124299  -0.0888886  0.124064    106 LEU   A HD11 
3180 H HD12 . LEU   B 94  ? 0.728729 0.567215 0.656657 0.0135621   -0.100572   0.120358    106 LEU   A HD12 
3181 H HD13 . LEU   B 94  ? 0.697174 0.569164 0.642231 0.0235048   -0.0772727  0.109967    106 LEU   A HD13 
3182 H HD21 . LEU   B 94  ? 0.762341 0.557519 0.62449  -0.00589861 -0.100879   0.106093    106 LEU   A HD21 
3183 H HD22 . LEU   B 94  ? 0.754337 0.55872  0.635966 0.0216809   -0.0838045  0.0966925   106 LEU   A HD22 
3184 H HD23 . LEU   B 94  ? 0.781977 0.554005 0.652361 0.00707411  -0.107702   0.106561    106 LEU   A HD23 
3185 N N    . ILE   B 95  ? 0.56399  0.499836 0.508523 -0.0436332  -0.092507   0.144991    107 ILE   A N    
3186 C CA   . ILE   B 95  ? 0.529419 0.488756 0.47503  -0.0623243  -0.0986556  0.158243    107 ILE   A CA   
3187 C C    . ILE   B 95  ? 0.601133 0.537222 0.53298  -0.0748406  -0.117872   0.169986    107 ILE   A C    
3188 O O    . ILE   B 95  ? 0.579363 0.509109 0.514224 -0.068176   -0.121934   0.171309    107 ILE   A O    
3189 C CB   . ILE   B 95  ? 0.490959 0.488792 0.455527 -0.0605525  -0.0853809  0.156318    107 ILE   A CB   
3190 C CG1  . ILE   B 95  ? 0.498153 0.507375 0.475881 -0.0478842  -0.065961   0.145245    107 ILE   A CG1  
3191 C CG2  . ILE   B 95  ? 0.49858  0.526832 0.463149 -0.0771054  -0.0879987  0.169232    107 ILE   A CG2  
3192 C CD1  . ILE   B 95  ? 0.509362 0.541619 0.502588 -0.0452457  -0.0529911  0.137017    107 ILE   A CD1  
3193 H H    . ILE   B 95  ? 0.571763 0.501719 0.520733 -0.0366009  -0.0938165  0.142529    107 ILE   A H    
3194 H HA   . ILE   B 95  ? 0.541829 0.506564 0.483666 -0.0680226  -0.098826   0.161056    107 ILE   A HA   
3195 H HB   . ILE   B 95  ? 0.501558 0.496846 0.469084 -0.0569135  -0.08765    0.154053    107 ILE   A HB   
3196 H HG12 . ILE   B 95  ? 0.495649 0.512715 0.472183 -0.0501153  -0.0637151  0.149502    107 ILE   A HG12 
3197 H HG13 . ILE   B 95  ? 0.502956 0.495008 0.478977 -0.0392846  -0.0640006  0.139381    107 ILE   A HG13 
3198 H HG21 . ILE   B 95  ? 0.481993 0.532518 0.455427 -0.0740488  -0.0775804  0.164883    107 ILE   A HG21 
3199 H HG22 . ILE   B 95  ? 0.496956 0.530229 0.46018  -0.0820264  -0.088917   0.173991    107 ILE   A HG22 
3200 H HG23 . ILE   B 95  ? 0.510815 0.532481 0.467546 -0.0859021  -0.0989377  0.177545    107 ILE   A HG23 
3201 H HD11 . ILE   B 95  ? 0.503623 0.534204 0.498722 -0.0450651  -0.0576049  0.134227    107 ILE   A HD11 
3202 H HD12 . ILE   B 95  ? 0.494604 0.525152 0.49499  -0.0379964  -0.0415499  0.130679    107 ILE   A HD12 
3203 H HD13 . ILE   B 95  ? 0.497709 0.548093 0.490986 -0.0513042  -0.0516479  0.140878    107 ILE   A HD13 
3204 N N    . LYS   B 96  ? 0.633935 0.560829 0.552357 -0.0943822  -0.130222   0.180561    108 LYS   A N    
3205 C CA   . LYS   B 96  ? 0.687992 0.591731 0.592677 -0.112925   -0.148512   0.196435    108 LYS   A CA   
3206 C C    . LYS   B 96  ? 0.610277 0.559308 0.525608 -0.125901   -0.145404   0.211906    108 LYS   A C    
3207 O O    . LYS   B 96  ? 0.587527 0.58429  0.518194 -0.124699   -0.130757   0.20982     108 LYS   A O    
3208 C CB   . LYS   B 96  ? 0.704961 0.584997 0.592383 -0.133907   -0.162648   0.200854    108 LYS   A CB   
3209 C CG   . LYS   B 96  ? 0.83576  0.659987 0.70072  -0.122969   -0.168668   0.183705    108 LYS   A CG   
3210 C CD   . LYS   B 96  ? 0.910764 0.677526 0.762005 -0.104927   -0.174451   0.176719    108 LYS   A CD   
3211 C CE   . LYS   B 96  ? 0.906454 0.627565 0.735975 -0.0872418  -0.172996   0.154645    108 LYS   A CE   
3212 N NZ   . LYS   B 96  ? 0.800314 0.558129 0.643973 -0.0662686  -0.151857   0.14108     108 LYS   A NZ   
3213 H H    . LYS   B 96  ? 0.629651 0.565281 0.547678 -0.0975534  -0.127909   0.179149    108 LYS   A H    
3214 H HA   . LYS   B 96  ? 0.689192 0.562836 0.58778  -0.102664   -0.153362   0.193589    108 LYS   A HA   
3215 H HB2  . LYS   B 96  ? 0.707826 0.622187 0.604587 -0.139969   -0.15724    0.202691    108 LYS   A HB2  
3216 H HB3  . LYS   B 96  ? 0.75264  0.621701 0.632998 -0.151131   -0.174044   0.21417     108 LYS   A HB3  
3217 H HG2  . LYS   B 96  ? 0.797322 0.63725  0.668151 -0.109408   -0.157135   0.173187    108 LYS   A HG2  
3218 H HG3  . LYS   B 96  ? 0.844778 0.655732 0.696903 -0.140995   -0.179956   0.186911    108 LYS   A HG3  
3219 H HD2  . LYS   B 96  ? 0.925725 0.666881 0.766717 -0.118911   -0.187759   0.18782     108 LYS   A HD2  
3220 H HD3  . LYS   B 96  ? 0.867854 0.653514 0.734421 -0.090262   -0.165835   0.176467    108 LYS   A HD3  
3221 H HE2  . LYS   B 96  ? 0.92603  0.627763 0.737463 -0.103051   -0.182816   0.153158    108 LYS   A HE2  
3222 H HE3  . LYS   B 96  ? 0.926919 0.612719 0.749484 -0.0739172  -0.176118   0.150917    108 LYS   A HE3  
3223 H HZ1  . LYS   B 96  ? 0.806305 0.584846 0.64983  -0.0760379  -0.150518   0.142395    108 LYS   A HZ1  
3224 H HZ2  . LYS   B 96  ? 0.789679 0.574367 0.653148 -0.0582851  -0.143373   0.144256    108 LYS   A HZ2  
3225 H HZ3  . LYS   B 96  ? 0.83913  0.571812 0.671234 -0.0517465  -0.148609   0.128701    108 LYS   A HZ3  
3226 N N    . PRO   B 97  ? 0.656974 0.59018  0.560878 -0.139347   -0.159204   0.229588    109 PRO   A N    
3227 C CA   . PRO   B 97  ? 0.637204 0.61461  0.545231 -0.149542   -0.155057   0.24398     109 PRO   A CA   
3228 C C    . PRO   B 97  ? 0.606326 0.638052 0.523983 -0.167399   -0.145288   0.252457    109 PRO   A C    
3229 O O    . PRO   B 97  ? 0.572652 0.651104 0.497534 -0.164876   -0.131664   0.252111    109 PRO   A O    
3230 C CB   . PRO   B 97  ? 0.647141 0.587402 0.536484 -0.161341   -0.174237   0.265258    109 PRO   A CB   
3231 C CG   . PRO   B 97  ? 0.753943 0.62914  0.628991 -0.166409   -0.18919    0.263785    109 PRO   A CG   
3232 C CD   . PRO   B 97  ? 0.740095 0.60858  0.623868 -0.14161    -0.177993   0.235614    109 PRO   A CD   
3233 H HA   . PRO   B 97  ? 0.608923 0.602028 0.524458 -0.13487    -0.146522   0.23425     109 PRO   A HA   
3234 H HB2  . PRO   B 97  ? 0.677486 0.640228 0.563165 -0.179668   -0.175624   0.281589    109 PRO   A HB2  
3235 H HB3  . PRO   B 97  ? 0.670684 0.605176 0.559939 -0.147174   -0.175543   0.263121    109 PRO   A HB3  
3236 H HG2  . PRO   B 97  ? 0.752998 0.63175  0.624373 -0.188159   -0.193813   0.273009    109 PRO   A HG2  
3237 H HG3  . PRO   B 97  ? 0.774708 0.611133 0.638579 -0.162788   -0.200218   0.270725    109 PRO   A HG3  
3238 H HD2  . PRO   B 97  ? 0.747977 0.591625 0.622841 -0.148129   -0.183447   0.231371    109 PRO   A HD2  
3239 H HD3  . PRO   B 97  ? 0.732173 0.582933 0.617012 -0.122073   -0.177223   0.227622    109 PRO   A HD3  
3240 N N    . GLU   B 98  ? 0.651983 0.67983  0.570187 -0.183795   -0.151918   0.258056    110 GLU   A N    
3241 C CA   . GLU   B 98  ? 0.701566 0.788185 0.634668 -0.200506   -0.144347   0.269399    110 GLU   A CA   
3242 C C    . GLU   B 98  ? 0.688797 0.822579 0.642646 -0.177444   -0.121291   0.25372     110 GLU   A C    
3243 O O    . GLU   B 98  ? 0.592474 0.783908 0.561506 -0.182455   -0.109284   0.261633    110 GLU   A O    
3244 C CB   . GLU   B 98  ? 0.710008 0.781105 0.640747 -0.222383   -0.16005    0.276257    110 GLU   A CB   
3245 C CG   . GLU   B 98  ? 0.864956 0.881738 0.773204 -0.249742   -0.183284   0.291841    110 GLU   A CG   
3246 C CD   . GLU   B 98  ? 0.910783 0.843159 0.794562 -0.236818   -0.196462   0.27968     110 GLU   A CD   
3247 O OE1  . GLU   B 98  ? 0.818024 0.73177  0.701654 -0.207705   -0.189056   0.256828    110 GLU   A OE1  
3248 O OE2  . GLU   B 98  ? 0.924497 0.808515 0.789223 -0.255562   -0.21348    0.294956    110 GLU   A OE2  
3249 H H    . GLU   B 98  ? 0.676429 0.66594  0.585888 -0.184054   -0.161567   0.254113    110 GLU   A H    
3250 H HA   . GLU   B 98  ? 0.701562 0.807663 0.631793 -0.213989   -0.144736   0.284273    110 GLU   A HA   
3251 H HB2  . GLU   B 98  ? 0.727772 0.779079 0.657192 -0.208967   -0.15999    0.261674    110 GLU   A HB2  
3252 H HB3  . GLU   B 98  ? 0.723316 0.841072 0.66864  -0.232537   -0.155142   0.284774    110 GLU   A HB3  
3253 H HG2  . GLU   B 98  ? 0.856466 0.880214 0.766789 -0.269931   -0.191699   0.298425    110 GLU   A HG2  
3254 H HG3  . GLU   B 98  ? 0.850927 0.882738 0.757896 -0.260489   -0.182641   0.307293    110 GLU   A HG3  
3255 N N    . TYR   B 99  ? 0.64477  0.753997 0.600068 -0.151597   -0.113814   0.232296    111 TYR   A N    
3256 C CA   . TYR   B 99  ? 0.585147 0.724303 0.557255 -0.130071   -0.0927429  0.217656    111 TYR   A CA   
3257 C C    . TYR   B 99  ? 0.588534 0.723312 0.558359 -0.115429   -0.0824519  0.2034      111 TYR   A C    
3258 O O    . TYR   B 99  ? 0.508832 0.648595 0.488597 -0.0973421  -0.0666598  0.187013    111 TYR   A O    
3259 C CB   . TYR   B 99  ? 0.592496 0.708981 0.567552 -0.117584   -0.0931296  0.207748    111 TYR   A CB   
3260 C CG   . TYR   B 99  ? 0.564809 0.696466 0.542054 -0.134451   -0.105013   0.221238    111 TYR   A CG   
3261 C CD1  . TYR   B 99  ? 0.651044 0.836146 0.649659 -0.130963   -0.0951313  0.228196    111 TYR   A CD1  
3262 C CD2  . TYR   B 99  ? 0.569118 0.663124 0.527937 -0.153518   -0.126624   0.226533    111 TYR   A CD2  
3263 C CE1  . TYR   B 99  ? 0.615487 0.826433 0.620934 -0.147993   -0.107946   0.242243    111 TYR   A CE1  
3264 C CE2  . TYR   B 99  ? 0.609714 0.721007 0.570192 -0.173849   -0.139985   0.237633    111 TYR   A CE2  
3265 C CZ   . TYR   B 99  ? 0.634418 0.809249 0.620168 -0.171977   -0.131419   0.246528    111 TYR   A CZ   
3266 O OH   . TYR   B 99  ? 0.622155 0.828038 0.615623 -0.192679   -0.145774   0.259547    111 TYR   A OH   
3267 H H    . TYR   B 99  ? 0.653621 0.724878 0.59928  -0.147367   -0.121726   0.227214    111 TYR   A H    
3268 H HA   . TYR   B 99  ? 0.589476 0.767812 0.571533 -0.1345     -0.0855714  0.224707    111 TYR   A HA   
3269 H HB2  . TYR   B 99  ? 0.589123 0.668961 0.553608 -0.113742   -0.0996218  0.201273    111 TYR   A HB2  
3270 H HB3  . TYR   B 99  ? 0.562614 0.692046 0.547862 -0.102499   -0.0792733  0.199262    111 TYR   A HB3  
3271 H HD1  . TYR   B 99  ? 0.597776 0.80344  0.607228 -0.116649   -0.0798153  0.223385    111 TYR   A HD1  
3272 H HD2  . TYR   B 99  ? 0.597848 0.653604 0.54273  -0.152844   -0.132963   0.222086    111 TYR   A HD2  
3273 H HE1  . TYR   B 99  ? 0.610414 0.862914 0.633858 -0.143048   -0.101156   0.248261    111 TYR   A HE1  
3274 H HE2  . TYR   B 99  ? 0.642601 0.723086 0.58758  -0.188705   -0.155355   0.239061    111 TYR   A HE2  
3276 N N    . ALA   B 100 ? 0.535656 0.660592 0.491646 -0.124959   -0.0928928  0.211005    112 ALA   A N    
3277 C CA   . ALA   B 100 ? 0.524173 0.650617 0.476383 -0.11533    -0.0884566  0.199679    112 ALA   A CA   
3278 C C    . ALA   B 100 ? 0.580382 0.7352   0.518033 -0.130503   -0.0917589  0.21427     112 ALA   A C    
3279 O O    . ALA   B 100 ? 0.57664  0.774189 0.515731 -0.134617   -0.0775782  0.215299    112 ALA   A O    
3280 C CB   . ALA   B 100 ? 0.496195 0.57965  0.44652  -0.104824   -0.0998558  0.193227    112 ALA   A CB   
3281 H H    . ALA   B 100 ? 0.568648 0.686236 0.516884 -0.139001   -0.10424    0.224812    112 ALA   A H    
3282 H HA   . ALA   B 100 ? 0.511397 0.651978 0.472099 -0.105175   -0.0744816  0.186296    112 ALA   A HA   
3283 H HB1  . ALA   B 100 ? 0.493923 0.566303 0.452547 -0.0945257  -0.0937955  0.182509    112 ALA   A HB1  
3284 H HB2  . ALA   B 100 ? 0.525224 0.58683  0.46701  -0.111836   -0.112885   0.204701    112 ALA   A HB2  
3285 H HB3  . ALA   B 100 ? 0.506773 0.596592 0.456032 -0.101089   -0.100003   0.188657    112 ALA   A HB3  
3286 N N    . TYR   B 101 ? 0.570998 0.704374 0.493829 -0.137082   -0.109299   0.227061    113 TYR   A N    
3287 C CA   . TYR   B 101 ? 0.595502 0.757942 0.499962 -0.15139    -0.1123     0.243232    113 TYR   A CA   
3288 C C    . TYR   B 101 ? 0.623047 0.772221 0.514225 -0.174337   -0.128054   0.274797    113 TYR   A C    
3289 O O    . TYR   B 101 ? 0.66803  0.835223 0.540448 -0.187572   -0.13305    0.293825    113 TYR   A O    
3290 C CB   . TYR   B 101 ? 0.597401 0.755594 0.493275 -0.141607   -0.120197   0.236081    113 TYR   A CB   
3291 C CG   . TYR   B 101 ? 0.575949 0.749552 0.483876 -0.126233   -0.10441    0.205128    113 TYR   A CG   
3292 C CD1  . TYR   B 101 ? 0.575926 0.788858 0.474989 -0.128687   -0.0878219  0.192652    113 TYR   A CD1  
3293 C CD2  . TYR   B 101 ? 0.580195 0.727562 0.507123 -0.110436   -0.10372    0.188083    113 TYR   A CD2  
3294 C CE1  . TYR   B 101 ? 0.549552 0.767038 0.456275 -0.117367   -0.073944   0.163509    113 TYR   A CE1  
3295 C CE2  . TYR   B 101 ? 0.549919 0.707804 0.487748 -0.101218   -0.0893789  0.162343    113 TYR   A CE2  
3296 C CZ   . TYR   B 101 ? 0.5438   0.732587 0.470847 -0.105507   -0.0757201  0.149659    113 TYR   A CZ   
3297 O OH   . TYR   B 101 ? 0.562824 0.751942 0.497808 -0.098577   -0.0620366  0.123255    113 TYR   A OH   
3298 H H    . TYR   B 101 ? 0.584038 0.685808 0.507192 -0.131621   -0.118871   0.226562    113 TYR   A H    
3299 H HA   . TYR   B 101 ? 0.584775 0.782079 0.490422 -0.152731   -0.0980321  0.238005    113 TYR   A HA   
3300 H HB2  . TYR   B 101 ? 0.608808 0.735043 0.506842 -0.136287   -0.132813   0.240469    113 TYR   A HB2  
3301 H HB3  . TYR   B 101 ? 0.618918 0.79671  0.498829 -0.151297   -0.12347    0.248015    113 TYR   A HB3  
3302 H HD1  . TYR   B 101 ? 0.587556 0.822947 0.473056 -0.138817   -0.0860486  0.204115    113 TYR   A HD1  
3303 H HD2  . TYR   B 101 ? 0.573919 0.694832 0.505288 -0.10648    -0.112941   0.194167    113 TYR   A HD2  
3304 H HE1  . TYR   B 101 ? 0.563647 0.802564 0.460894 -0.118363   -0.0628302  0.153179    113 TYR   A HE1  
3305 H HE2  . TYR   B 101 ? 0.540366 0.682801 0.49152  -0.0925171  -0.0885806  0.153172    113 TYR   A HE2  
3307 N N    . GLY   B 102 ? 0.636918 0.75007  0.534314 -0.180159   -0.137305   0.280275    114 GLY   A N    
3308 C CA   . GLY   B 102 ? 0.714085 0.818096 0.60213  -0.208505   -0.149519   0.308276    114 GLY   A CA   
3309 C C    . GLY   B 102 ? 0.756567 0.81747  0.622436 -0.216424   -0.170119   0.330698    114 GLY   A C    
3310 O O    . GLY   B 102 ? 0.700708 0.736264 0.561967 -0.196038   -0.177194   0.323623    114 GLY   A O    
3311 H H    . GLY   B 102 ? 0.630289 0.723308 0.536478 -0.167894   -0.136399   0.266246    114 GLY   A H    
3312 H HA2  . GLY   B 102 ? 0.701998 0.78549  0.596474 -0.211573   -0.153615   0.305129    114 GLY   A HA2  
3313 H HA3  . GLY   B 102 ? 0.698772 0.846072 0.588483 -0.22025    -0.140208   0.316714    114 GLY   A HA3  
3314 N N    . SER   B 103 ? 0.760071 0.816653 0.614125 -0.246825   -0.179715   0.360463    115 SER   A N    
3315 C CA   . SER   B 103 ? 0.861789 0.870351 0.69283  -0.256055   -0.200039   0.387056    115 SER   A CA   
3316 C C    . SER   B 103 ? 0.805886 0.853428 0.621766 -0.251539   -0.197026   0.399115    115 SER   A C    
3317 O O    . SER   B 103 ? 0.878052 0.890477 0.67765  -0.244012   -0.21348    0.414518    115 SER   A O    
3318 C CB   . SER   B 103 ? 0.951101 0.936627 0.773514 -0.293984   -0.211788   0.415852    115 SER   A CB   
3319 O OG   . SER   B 103 ? 0.944972 1.00333  0.777342 -0.318985   -0.19677    0.427318    115 SER   A OG   
3320 H H    . SER   B 103 ? 0.77326  0.857383 0.634567 -0.262176   -0.173724   0.365689    115 SER   A H    
3321 H HA   . SER   B 103 ? 0.855217 0.817759 0.685808 -0.239059   -0.208915   0.377175    115 SER   A HA   
3322 H HB2  . SER   B 103 ? 0.986016 0.942178 0.791271 -0.301594   -0.223899   0.437246    115 SER   A HB2  
3323 H HB3  . SER   B 103 ? 0.949764 0.897245 0.776312 -0.294321   -0.218534   0.406133    115 SER   A HB3  
3325 N N    . ALA   B 104 ? 0.73372  0.854277 0.553046 -0.254815   -0.176361   0.392014    116 ALA   A N    
3326 C CA   . ALA   B 104 ? 0.755617 0.919493 0.556644 -0.249579   -0.170772   0.394709    116 ALA   A CA   
3327 C C    . ALA   B 104 ? 0.764466 0.916715 0.568428 -0.219319   -0.175257   0.370107    116 ALA   A C    
3328 O O    . ALA   B 104 ? 0.743275 0.909209 0.527023 -0.216291   -0.183888   0.38017     116 ALA   A O    
3329 C CB   . ALA   B 104 ? 0.748098 0.986537 0.551756 -0.255901   -0.144755   0.385128    116 ALA   A CB   
3330 H H    . ALA   B 104 ? 0.727286 0.871727 0.559836 -0.260114   -0.16534    0.384573    116 ALA   A H    
3331 H HA   . ALA   B 104 ? 0.800295 0.953985 0.582578 -0.263458   -0.181982   0.421947    116 ALA   A HA   
3332 H HB1  . ALA   B 104 ? 0.756219 1.00989  0.560689 -0.27604    -0.141821   0.403316    116 ALA   A HB1  
3333 H HB2  . ALA   B 104 ? 0.708292 0.953792 0.529828 -0.241648   -0.133939   0.360254    116 ALA   A HB2  
3334 H HB3  . ALA   B 104 ? 0.753075 1.01828  0.539317 -0.25381    -0.141358   0.385785    116 ALA   A HB3  
3335 N N    . GLY   B 105 ? 0.696585 0.83292  0.5255   -0.199131   -0.168505   0.338988    117 GLY   A N    
3336 C CA   . GLY   B 105 ? 0.654843 0.788736 0.493278 -0.173534   -0.169567   0.314017    117 GLY   A CA   
3337 C C    . GLY   B 105 ? 0.647049 0.838022 0.47639  -0.172459   -0.155272   0.29745     117 GLY   A C    
3338 O O    . GLY   B 105 ? 0.633394 0.864671 0.452437 -0.185621   -0.139553   0.299376    117 GLY   A O    
3339 H H    . GLY   B 105 ? 0.684952 0.814145 0.525674 -0.202691   -0.163208   0.334185    117 GLY   A H    
3340 H HA2  . GLY   B 105 ? 0.637356 0.755307 0.493612 -0.162693   -0.164236   0.296339    117 GLY   A HA2  
3341 H HA3  . GLY   B 105 ? 0.684068 0.794517 0.516625 -0.167966   -0.185235   0.325662    117 GLY   A HA3  
3342 N N    . SER   B 106 ? 0.650761 0.845743 0.483695 -0.156965   -0.161181   0.280736    118 SER   A N    
3343 C CA   . SER   B 106 ? 0.658005 0.898629 0.479109 -0.156941   -0.150821   0.259543    118 SER   A CA   
3344 C C    . SER   B 106 ? 0.674719 0.921352 0.490988 -0.149259   -0.170916   0.259899    118 SER   A C    
3345 O O    . SER   B 106 ? 0.64596  0.896158 0.481023 -0.137768   -0.170201   0.234402    118 SER   A O    
3346 C CB   . SER   B 106 ? 0.653124 0.898464 0.495288 -0.14689    -0.128767   0.223739    118 SER   A CB   
3347 O OG   . SER   B 106 ? 0.683494 0.966246 0.507604 -0.149843   -0.117246   0.202255    118 SER   A OG   
3348 H H    . SER   B 106 ? 0.652097 0.820932 0.495135 -0.14652    -0.172262   0.281885    118 SER   A H    
3349 H HA   . SER   B 106 ? 0.679013 0.945113 0.479559 -0.169304   -0.145485   0.269647    118 SER   A HA   
3350 H HB2  . SER   B 106 ? 0.63965  0.881713 0.488423 -0.149346   -0.118288   0.225953    118 SER   A HB2  
3351 H HB3  . SER   B 106 ? 0.634691 0.859947 0.495303 -0.136005   -0.133032   0.213694    118 SER   A HB3  
3353 N N    . LEU   B 107 ? 0.716431 0.968531 0.507307 -0.157529   -0.189549   0.29198     119 LEU   A N    
3354 C CA   . LEU   B 107 ? 0.760482 1.02204  0.546985 -0.149206   -0.213287   0.300992    119 LEU   A CA   
3355 C C    . LEU   B 107 ? 0.779748 1.09197  0.551464 -0.154054   -0.20988    0.274586    119 LEU   A C    
3356 O O    . LEU   B 107 ? 0.782131 1.12322  0.527233 -0.167643   -0.192811   0.263275    119 LEU   A O    
3357 C CB   . LEU   B 107 ? 0.829658 1.08297  0.587363 -0.158098   -0.233109   0.346351    119 LEU   A CB   
3358 C CG   . LEU   B 107 ? 0.83916  1.02959  0.609705 -0.151645   -0.244548   0.373287    119 LEU   A CG   
3359 C CD1  . LEU   B 107 ? 0.915903 1.09489  0.656023 -0.160555   -0.265426   0.419185    119 LEU   A CD1  
3360 C CD2  . LEU   B 107 ? 0.832859 0.989342 0.63966  -0.123863   -0.253936   0.360717    119 LEU   A CD2  
3361 H H    . LEU   B 107 ? 0.738226 0.989995 0.514719 -0.169087   -0.187721   0.310605    119 LEU   A H    
3362 H HA   . LEU   B 107 ? 0.747321 0.986467 0.559289 -0.134647   -0.219167   0.295474    119 LEU   A HA   
3363 H HB2  . LEU   B 107 ? 0.837175 1.11041  0.571596 -0.173937   -0.223807   0.353485    119 LEU   A HB2  
3364 H HB3  . LEU   B 107 ? 0.843318 1.11464  0.593233 -0.153578   -0.248488   0.352655    119 LEU   A HB3  
3365 H HG   . LEU   B 107 ? 0.833499 1.01054  0.607375 -0.160578   -0.231279   0.369951    119 LEU   A HG   
3366 H HD11 . LEU   B 107 ? 0.923881 1.13112  0.639503 -0.17852    -0.25852    0.427863    119 LEU   A HD11 
3367 H HD12 . LEU   B 107 ? 0.926893 1.06052  0.671602 -0.160233   -0.27041    0.434983    119 LEU   A HD12 
3368 H HD13 . LEU   B 107 ? 0.926157 1.11493  0.665718 -0.148856   -0.281021   0.425335    119 LEU   A HD13 
3369 H HD21 . LEU   B 107 ? 0.792946 0.948347 0.618405 -0.120017   -0.239555   0.335413    119 LEU   A HD21 
3370 H HD22 . LEU   B 107 ? 0.835158 1.0142   0.645057 -0.114579   -0.265104   0.359935    119 LEU   A HD22 
3371 H HD23 . LEU   B 107 ? 0.852483 0.966726 0.660363 -0.119114   -0.262948   0.37913     119 LEU   A HD23 
3372 N N    . PRO   B 108 ? 0.776148 1.10396  0.561657 -0.144344   -0.22732    0.265381    120 PRO   A N    
3373 C CA   . PRO   B 108 ? 0.754217 1.05816  0.570781 -0.124485   -0.247631   0.281577    120 PRO   A CA   
3374 C C    . PRO   B 108 ? 0.717303 0.995353 0.57865  -0.108648   -0.235739   0.257142    120 PRO   A C    
3375 O O    . PRO   B 108 ? 0.79411  1.0522   0.68218  -0.0890997  -0.248058   0.267819    120 PRO   A O    
3376 C CB   . PRO   B 108 ? 0.791084 1.14208  0.604212 -0.123354   -0.270335   0.281246    120 PRO   A CB   
3377 C CG   . PRO   B 108 ? 0.780577 1.16569  0.580139 -0.140174   -0.253914   0.241803    120 PRO   A CG   
3378 C CD   . PRO   B 108 ? 0.78119  1.15544  0.550712 -0.153299   -0.229254   0.239242    120 PRO   A CD   
3379 H HA   . PRO   B 108 ? 0.78332  1.06336  0.592004 -0.122509   -0.255814   0.308719    120 PRO   A HA   
3380 H HB2  . PRO   B 108 ? 0.777204 1.12559  0.620623 -0.108787   -0.279143   0.279716    120 PRO   A HB2  
3381 H HB3  . PRO   B 108 ? 0.822926 1.1844   0.611122 -0.127428   -0.284626   0.306172    120 PRO   A HB3  
3382 H HG2  . PRO   B 108 ? 0.75166  1.13106  0.57924  -0.135168   -0.245688   0.219245    120 PRO   A HG2  
3383 H HG3  . PRO   B 108 ? 0.804705 1.22415  0.586189 -0.14754    -0.267155   0.241495    120 PRO   A HG3  
3384 H HD2  . PRO   B 108 ? 0.762708 1.13649  0.538267 -0.155837   -0.211513   0.211484    120 PRO   A HD2  
3385 H HD3  . PRO   B 108 ? 0.813899 1.21116  0.549257 -0.164131   -0.233364   0.249751    120 PRO   A HD3  
3386 N N    . LYS   B 109 ? 0.68284  0.960917 0.55064  -0.115202   -0.211167   0.226182    121 LYS   A N    
3387 C CA   . LYS   B 109 ? 0.691539 0.948372 0.597534 -0.102604   -0.198065   0.203811    121 LYS   A CA   
3388 C C    . LYS   B 109 ? 0.659964 0.866815 0.578381 -0.0901495  -0.19514    0.218594    121 LYS   A C    
3389 O O    . LYS   B 109 ? 0.664613 0.852558 0.611071 -0.0722443  -0.198012   0.216298    121 LYS   A O    
3390 C CB   . LYS   B 109 ? 0.635177 0.899531 0.539767 -0.112629   -0.173118   0.171011    121 LYS   A CB   
3391 H H    . LYS   B 109 ? 0.698705 0.990528 0.545663 -0.127022   -0.201576   0.219522    121 LYS   A H    
3392 H HA   . LYS   B 109 ? 0.669729 0.940817 0.594366 -0.0953399  -0.207913   0.199919    121 LYS   A HA   
3395 N N    . ILE   B 110 ? 0.667748 0.854712 0.564942 -0.100645   -0.188677   0.23249     122 ILE   A N    
3396 C CA   . ILE   B 110 ? 0.646753 0.786622 0.5525   -0.0950692  -0.183972   0.239388    122 ILE   A CA   
3397 C C    . ILE   B 110 ? 0.686205 0.797958 0.569717 -0.102272   -0.200449   0.274511    122 ILE   A C    
3398 O O    . ILE   B 110 ? 0.702395 0.833075 0.560631 -0.121826   -0.199355   0.289724    122 ILE   A O    
3399 C CB   . ILE   B 110 ? 0.622494 0.765327 0.527518 -0.105254   -0.160749   0.223878    122 ILE   A CB   
3400 C CG1  . ILE   B 110 ? 0.666653 0.835952 0.584463 -0.102613   -0.143867   0.192462    122 ILE   A CG1  
3401 C CG2  . ILE   B 110 ? 0.616357 0.715657 0.531703 -0.100058   -0.157568   0.226317    122 ILE   A CG2  
3402 C CD1  . ILE   B 110 ? 0.643724 0.79831  0.592114 -0.0863509  -0.140984   0.175426    122 ILE   A CD1  
3403 H H    . ILE   B 110 ? 0.676911 0.882578 0.553    -0.112915   -0.187307   0.237593    122 ILE   A H    
3404 H HA   . ILE   B 110 ? 0.640565 0.764791 0.56592  -0.0807015  -0.18515    0.232116    122 ILE   A HA   
3405 H HB   . ILE   B 110 ? 0.647345 0.804316 0.534056 -0.118238   -0.159523   0.234577    122 ILE   A HB   
3406 H HG12 . ILE   B 110 ? 0.659076 0.854212 0.566484 -0.107923   -0.147829   0.189677    122 ILE   A HG12 
3407 H HG13 . ILE   B 110 ? 0.637949 0.810162 0.553238 -0.107304   -0.129819   0.185748    122 ILE   A HG13 
3408 H HG21 . ILE   B 110 ? 0.597579 0.703521 0.516701 -0.10363    -0.143713   0.215724    122 ILE   A HG21 
3409 H HG22 . ILE   B 110 ? 0.611416 0.69406  0.541116 -0.08618    -0.160277   0.21945     122 ILE   A HG22 
3410 H HG23 . ILE   B 110 ? 0.639359 0.720985 0.542315 -0.107276   -0.166853   0.245516    122 ILE   A HG23 
3411 H HD11 . ILE   B 110 ? 0.633481 0.764075 0.588744 -0.0813004  -0.135049   0.175397    122 ILE   A HD11 
3412 H HD12 . ILE   B 110 ? 0.631731 0.80234  0.586345 -0.0882544  -0.131465   0.157379    122 ILE   A HD12 
3413 H HD13 . ILE   B 110 ? 0.653177 0.807455 0.607773 -0.0792476  -0.154309   0.182913    122 ILE   A HD13 
3414 N N    . PRO   B 111 ? 0.699503 0.76269  0.589391 -0.0879917  -0.214425   0.288929    123 PRO   A N    
3415 C CA   . PRO   B 111 ? 0.7381   0.76327  0.604327 -0.0984049  -0.229576   0.322634    123 PRO   A CA   
3416 C C    . PRO   B 111 ? 0.723894 0.725171 0.580479 -0.119629   -0.219812   0.32605     123 PRO   A C    
3417 O O    . PRO   B 111 ? 0.678659 0.690736 0.548543 -0.121276   -0.202139   0.302484    123 PRO   A O    
3418 C CB   . PRO   B 111 ? 0.772404 0.748419 0.650329 -0.0717099  -0.245381   0.330296    123 PRO   A CB   
3419 C CG   . PRO   B 111 ? 0.739932 0.716957 0.647815 -0.0521481  -0.230757   0.296876    123 PRO   A CG   
3420 C CD   . PRO   B 111 ? 0.691737 0.730999 0.609631 -0.0614515  -0.214855   0.273916    123 PRO   A CD   
3421 H HA   . PRO   B 111 ? 0.756913 0.805575 0.607027 -0.107401   -0.236622   0.338281    123 PRO   A HA   
3422 H HB2  . PRO   B 111 ? 0.805064 0.736252 0.671433 -0.0761353  -0.25153    0.344201    123 PRO   A HB2  
3423 H HB3  . PRO   B 111 ? 0.790816 0.781715 0.668416 -0.0629647  -0.257603   0.342079    123 PRO   A HB3  
3424 H HG2  . PRO   B 111 ? 0.73633  0.682329 0.642382 -0.0549744  -0.224138   0.290379    123 PRO   A HG2  
3425 H HG3  . PRO   B 111 ? 0.747938 0.717601 0.669542 -0.0312541  -0.237895   0.296842    123 PRO   A HG3  
3426 H HD2  . PRO   B 111 ? 0.663987 0.699795 0.592076 -0.0607694  -0.200798   0.255687    123 PRO   A HD2  
3427 H HD3  . PRO   B 111 ? 0.685458 0.751228 0.615616 -0.0517135  -0.219461   0.269483    123 PRO   A HD3  
3428 N N    . SER   B 112 ? 0.750929 0.724586 0.584621 -0.138208   -0.232056   0.358013    124 SER   A N    
3429 C CA   . SER   B 112 ? 0.783251 0.730739 0.610657 -0.161524   -0.227867   0.364963    124 SER   A CA   
3430 C C    . SER   B 112 ? 0.750523 0.648808 0.592737 -0.147489   -0.225979   0.342733    124 SER   A C    
3431 O O    . SER   B 112 ? 0.779706 0.633565 0.626111 -0.123338   -0.235778   0.338345    124 SER   A O    
3432 C CB   . SER   B 112 ? 0.833151 0.74436  0.635095 -0.183058   -0.24528    0.404717    124 SER   A CB   
3433 O OG   . SER   B 112 ? 0.836995 0.71567  0.635371 -0.208299   -0.245217   0.411171    124 SER   A OG   
3434 H H    . SER   B 112 ? 0.790674 0.762655 0.612615 -0.137759   -0.244144   0.37724     124 SER   A H    
3435 H HA   . SER   B 112 ? 0.745145 0.733852 0.574526 -0.173593   -0.214299   0.358282    124 SER   A HA   
3436 H HB2  . SER   B 112 ? 0.838443 0.787247 0.62859  -0.195085   -0.243737   0.419195    124 SER   A HB2  
3437 H HB3  . SER   B 112 ? 0.864017 0.736805 0.662691 -0.168224   -0.258865   0.413029    124 SER   A HB3  
3439 N N    . ASN   B 113 ? 0.779661 0.688694 0.628426 -0.161837   -0.213386   0.329925    125 ASN   A N    
3440 C CA   . ASN   B 113 ? 0.801162 0.662222 0.653744 -0.157584   -0.214367   0.314274    125 ASN   A CA   
3441 C C    . ASN   B 113 ? 0.795487 0.648834 0.664917 -0.123476   -0.206653   0.285239    125 ASN   A C    
3442 O O    . ASN   B 113 ? 0.804065 0.601451 0.669102 -0.109707   -0.212879   0.27625     125 ASN   A O    
3443 C CB   . ASN   B 113 ? 0.854671 0.640509 0.685966 -0.16976    -0.234776   0.333931    125 ASN   A CB   
3444 C CG   . ASN   B 113 ? 0.901027 0.693187 0.721506 -0.210916   -0.238787   0.355642    125 ASN   A CG   
3445 O OD1  . ASN   B 113 ? 0.93655  0.790477 0.769097 -0.226178   -0.224773   0.352394    125 ASN   A OD1  
3446 N ND2  . ASN   B 113 ? 1.02616  0.758868 0.825304 -0.22959    -0.257542   0.381317    125 ASN   A ND2  
3447 H H    . ASN   B 113 ? 0.748891 0.699212 0.598933 -0.1742     -0.203852   0.331001    125 ASN   A H    
3448 H HA   . ASN   B 113 ? 0.778201 0.662589 0.63559  -0.17087    -0.205802   0.309337    125 ASN   A HA   
3449 H HB2  . ASN   B 113 ? 0.891205 0.660418 0.715429 -0.161856   -0.244294   0.348026    125 ASN   A HB2  
3450 H HB3  . ASN   B 113 ? 0.873124 0.620928 0.704234 -0.158579   -0.23629    0.318736    125 ASN   A HB3  
3451 H HD21 . ASN   B 113 ? 1.02526  0.765475 0.818761 -0.256624   -0.260385   0.397974    125 ASN   A HD21 
3452 H HD22 . ASN   B 113 ? 1.04038  0.725205 0.831395 -0.215054   -0.267006   0.382445    125 ASN   A HD22 
3453 N N    . ALA   B 114 ? 0.691141 0.599154 0.578168 -0.111204   -0.192346   0.270008    126 ALA   A N    
3454 C CA   . ALA   B 114 ? 0.675655 0.582765 0.581615 -0.0823883  -0.184831   0.246508    126 ALA   A CA   
3455 C C    . ALA   B 114 ? 0.629346 0.539087 0.544121 -0.0807802  -0.168672   0.224462    126 ALA   A C    
3456 O O    . ALA   B 114 ? 0.621351 0.564278 0.538514 -0.0955251  -0.158003   0.222416    126 ALA   A O    
3457 C CB   . ALA   B 114 ? 0.630299 0.589621 0.55061  -0.0737501  -0.179719   0.240647    126 ALA   A CB   
3458 H H    . ALA   B 114 ? 0.690409 0.636003 0.577224 -0.121712   -0.18673    0.273941    126 ALA   A H    
3459 H HA   . ALA   B 114 ? 0.698329 0.567537 0.601097 -0.0697049  -0.194171   0.249316    126 ALA   A HA   
3460 H HB1  . ALA   B 114 ? 0.658145 0.618061 0.571186 -0.0743258  -0.191522   0.255999    126 ALA   A HB1  
3461 H HB2  . ALA   B 114 ? 0.612657 0.603979 0.533604 -0.0846439  -0.169798   0.235804    126 ALA   A HB2  
3462 H HB3  . ALA   B 114 ? 0.621347 0.582088 0.556836 -0.0571872  -0.174797   0.226517    126 ALA   A HB3  
3463 N N    . THR   B 115 ? 0.707002 0.584068 0.626147 -0.0601119  -0.166512   0.20932     127 THR   A N    
3464 C CA   . THR   B 115 ? 0.642579 0.527085 0.570938 -0.0517943  -0.150012   0.188171    127 THR   A CA   
3465 C C    . THR   B 115 ? 0.611807 0.537195 0.56524  -0.0367096  -0.135733   0.174694    127 THR   A C    
3466 O O    . THR   B 115 ? 0.621638 0.552613 0.58698  -0.0217375  -0.140389   0.175163    127 THR   A O    
3467 C CB   . THR   B 115 ? 0.684262 0.513208 0.598954 -0.0380635  -0.154295   0.179022    127 THR   A CB   
3468 O OG1  . THR   B 115 ? 0.669262 0.460506 0.559532 -0.0595655  -0.169001   0.19067     127 THR   A OG1  
3469 C CG2  . THR   B 115 ? 0.702002 0.53698  0.619504 -0.0298394  -0.137795   0.159453    127 THR   A CG2  
3470 H H    . THR   B 115 ? 0.708055 0.556368 0.623081 -0.0495678  -0.17542    0.213271    127 THR   A H    
3471 H HA   . THR   B 115 ? 0.638541 0.536709 0.563896 -0.0659576  -0.145972   0.189484    127 THR   A HA   
3472 H HB   . THR   B 115 ? 0.695935 0.509831 0.614144 -0.0215401  -0.158231   0.178714    127 THR   A HB   
3474 H HG21 . THR   B 115 ? 0.718073 0.518527 0.623489 -0.0199639  -0.13993    0.152131    127 THR   A HG21 
3475 H HG22 . THR   B 115 ? 0.679606 0.525341 0.59248  -0.0447074  -0.13646    0.161698    127 THR   A HG22 
3476 H HG23 . THR   B 115 ? 0.664186 0.527076 0.599341 -0.0197371  -0.12661    0.152783    127 THR   A HG23 
3477 N N    . LEU   B 116 ? 0.587648 0.540624 0.550701 -0.0403945  -0.118623   0.162981    128 LEU   A N    
3478 C CA   . LEU   B 116 ? 0.536824 0.523302 0.52213  -0.032354   -0.104614   0.149976    128 LEU   A CA   
3479 C C    . LEU   B 116 ? 0.538695 0.517209 0.531015 -0.021412   -0.0885874  0.13634     128 LEU   A C    
3480 O O    . LEU   B 116 ? 0.552176 0.512305 0.530467 -0.0243942  -0.0864406  0.136649    128 LEU   A O    
3481 C CB   . LEU   B 116 ? 0.559444 0.581815 0.547789 -0.0463438  -0.0962727  0.148303    128 LEU   A CB   
3482 C CG   . LEU   B 116 ? 0.673281 0.714686 0.649674 -0.0605816  -0.107149   0.161338    128 LEU   A CG   
3483 C CD1  . LEU   B 116 ? 0.664912 0.742754 0.646538 -0.0666109  -0.0947333  0.14957     128 LEU   A CD1  
3484 C CD2  . LEU   B 116 ? 0.656273 0.690499 0.629241 -0.0563877  -0.125222   0.173041    128 LEU   A CD2  
3485 H H    . LEU   B 116 ? 0.578256 0.527642 0.533919 -0.0487104  -0.116432   0.164003    128 LEU   A H    
3486 H HA   . LEU   B 116 ? 0.557511 0.54877  0.551136 -0.0244846  -0.110095   0.150621    128 LEU   A HA   
3487 H HB2  . LEU   B 116 ? 0.56248  0.583116 0.547292 -0.0500555  -0.0891655  0.147287    128 LEU   A HB2  
3488 H HB3  . LEU   B 116 ? 0.557525 0.595167 0.559317 -0.0421826  -0.0880616  0.138118    128 LEU   A HB3  
3489 H HG   . LEU   B 116 ? 0.653072 0.688297 0.618504 -0.0695783  -0.109647   0.170472    128 LEU   A HG   
3490 H HD11 . LEU   B 116 ? 0.651096 0.73048  0.634869 -0.0670092  -0.0830811  0.14395     128 LEU   A HD11 
3491 H HD12 . LEU   B 116 ? 0.670442 0.762931 0.641068 -0.0754874  -0.100094   0.157035    128 LEU   A HD12 
3492 H HD13 . LEU   B 116 ? 0.656437 0.741174 0.649378 -0.0612703  -0.0930829  0.140207    128 LEU   A HD13 
3493 H HD21 . LEU   B 116 ? 0.685723 0.691866 0.649454 -0.0555435  -0.133774   0.182462    128 LEU   A HD21 
3494 H HD22 . LEU   B 116 ? 0.661644 0.700236 0.6486   -0.0452476  -0.124117   0.165258    128 LEU   A HD22 
3495 H HD23 . LEU   B 116 ? 0.673385 0.727071 0.638984 -0.0654108  -0.12983    0.17975     128 LEU   A HD23 
3496 N N    . PHE   B 117 ? 0.534202 0.531994 0.548264 -0.0115838  -0.0781063  0.126199    129 PHE   A N    
3497 C CA   . PHE   B 117 ? 0.51189  0.509766 0.534535 -0.00391303 -0.0599355  0.115942    129 PHE   A CA   
3498 C C    . PHE   B 117 ? 0.488628 0.516474 0.531345 -0.0120022  -0.0473992  0.108649    129 PHE   A C    
3499 O O    . PHE   B 117 ? 0.494559 0.546878 0.552571 -0.0160937  -0.0526467  0.106161    129 PHE   A O    
3500 C CB   . PHE   B 117 ? 0.566783 0.556174 0.597387 0.0156339   -0.0580361  0.11141     129 PHE   A CB   
3501 C CG   . PHE   B 117 ? 0.632646 0.633024 0.675857 0.0222293   -0.0366791  0.102785    129 PHE   A CG   
3502 C CD1  . PHE   B 117 ? 0.624324 0.659859 0.698312 0.0190405   -0.0263053  0.0983438   129 PHE   A CD1  
3503 C CD2  . PHE   B 117 ? 0.594523 0.571503 0.617034 0.0284025   -0.0277352  0.100343    129 PHE   A CD2  
3504 C CE1  . PHE   B 117 ? 0.643171 0.688514 0.729115 0.0218617   -0.00597962 0.0940236   129 PHE   A CE1  
3505 C CE2  . PHE   B 117 ? 0.612757 0.601112 0.643729 0.0340306   -0.00725761 0.0959711   129 PHE   A CE2  
3506 C CZ   . PHE   B 117 ? 0.648587 0.670165 0.711911 0.0296948   0.00447634  0.0941965   129 PHE   A CZ   
3507 H H    . PHE   B 117 ? 0.528091 0.541613 0.552167 -0.0109529  -0.0828986  0.126998    129 PHE   A H    
3508 H HA   . PHE   B 117 ? 0.523376 0.507327 0.532424 -0.00639709 -0.0572811  0.117244    129 PHE   A HA   
3509 H HB2  . PHE   B 117 ? 0.593293 0.555469 0.606349 0.0208864   -0.0646712  0.113359    129 PHE   A HB2  
3510 H HB3  . PHE   B 117 ? 0.573492 0.577936 0.617927 0.0190859   -0.0643069  0.112946    129 PHE   A HB3  
3511 H HD1  . PHE   B 117 ? 0.619485 0.672839 0.705486 0.0135297   -0.0338295  0.0989869   129 PHE   A HD1  
3512 H HD2  . PHE   B 117 ? 0.626144 0.579825 0.627494 0.0280398   -0.0361519  0.102189    129 PHE   A HD2  
3513 H HE1  . PHE   B 117 ? 0.626922 0.695549 0.734685 0.0162737   0.00035154  0.0917235   129 PHE   A HE1  
3514 H HE2  . PHE   B 117 ? 0.63253  0.606336 0.645761 0.0380625   -0.00174648 0.0951606   129 PHE   A HE2  
3515 H HZ   . PHE   B 117 ? 0.638096 0.667114 0.707317 0.0311901   0.0189264   0.0933553   129 PHE   A HZ   
3516 N N    . PHE   B 118 ? 0.50545  0.528899 0.547817 -0.0135121  -0.0312697  0.10496     130 PHE   A N    
3517 C CA   . PHE   B 118 ? 0.452309 0.490586 0.511683 -0.0206794  -0.0171117  0.0969783   130 PHE   A CA   
3518 C C    . PHE   B 118 ? 0.510637 0.539368 0.574947 -0.0146643  0.00070959  0.0962291   130 PHE   A C    
3519 O O    . PHE   B 118 ? 0.467294 0.478173 0.514055 -0.00739126 0.00333986  0.10214     130 PHE   A O    
3520 C CB   . PHE   B 118 ? 0.462718 0.501109 0.514576 -0.029685   -0.0124329  0.0954408   130 PHE   A CB   
3521 C CG   . PHE   B 118 ? 0.487415 0.54078  0.530959 -0.0383096  -0.025374   0.0960449   130 PHE   A CG   
3522 C CD1  . PHE   B 118 ? 0.509282 0.559376 0.536    -0.0390597  -0.0374293  0.107951    130 PHE   A CD1  
3523 C CD2  . PHE   B 118 ? 0.470755 0.542455 0.521499 -0.0481166  -0.0263343  0.0852981   130 PHE   A CD2  
3524 C CE1  . PHE   B 118 ? 0.543703 0.610059 0.561025 -0.0483194  -0.0475383  0.111858    130 PHE   A CE1  
3525 C CE2  . PHE   B 118 ? 0.500126 0.588039 0.53749  -0.0558491  -0.0376988  0.0869969   130 PHE   A CE2  
3526 C CZ   . PHE   B 118 ? 0.473887 0.559955 0.495025 -0.0552938  -0.0476042  0.101769    130 PHE   A CZ   
3527 H H    . PHE   B 118 ? 0.49425  0.502882 0.524253 -0.0104186  -0.0298805  0.108032    130 PHE   A H    
3528 H HA   . PHE   B 118 ? 0.472211 0.526877 0.545265 -0.0236672  -0.0205263  0.09286     130 PHE   A HA   
3529 H HB2  . PHE   B 118 ? 0.466041 0.493527 0.50787  -0.0258509  -0.00979511 0.101082    130 PHE   A HB2  
3530 H HB3  . PHE   B 118 ? 0.466484 0.506252 0.528177 -0.0333518  -0.00212972 0.088714    130 PHE   A HB3  
3531 H HD1  . PHE   B 118 ? 0.511876 0.549053 0.532351 -0.0348738  -0.0385095  0.113751    130 PHE   A HD1  
3532 H HD2  . PHE   B 118 ? 0.482452 0.55588  0.545412 -0.0509639  -0.0193216  0.0771079   130 PHE   A HD2  
3533 H HE1  . PHE   B 118 ? 0.522318 0.586829 0.529085 -0.0513162  -0.0552658  0.121846    130 PHE   A HE1  
3534 H HE2  . PHE   B 118 ? 0.49484  0.595924 0.533175 -0.0631739  -0.0393014  0.0786073   130 PHE   A HE2  
3535 H HZ   . PHE   B 118 ? 0.503281 0.602148 0.514267 -0.0616823  -0.0541262  0.104866    130 PHE   A HZ   
3536 N N    . GLU   B 119 ? 0.508632 0.551885 0.595677 -0.0204547  0.0113345   0.0899381   131 GLU   A N    
3537 C CA   . GLU   B 119 ? 0.556184 0.590644 0.649186 -0.0222424  0.0310732   0.0910918   131 GLU   A CA   
3538 C C    . GLU   B 119 ? 0.595667 0.62089  0.691054 -0.0349232  0.0371806   0.0855027   131 GLU   A C    
3539 O O    . GLU   B 119 ? 0.552513 0.591441 0.659072 -0.0473617  0.0314841   0.0749532   131 GLU   A O    
3540 C CB   . GLU   B 119 ? 0.538065 0.594568 0.656518 -0.0233718  0.0405691   0.0892641   131 GLU   A CB   
3541 C CG   . GLU   B 119 ? 0.65346  0.70003  0.776961 -0.0290911  0.0623126   0.094243    131 GLU   A CG   
3542 C CD   . GLU   B 119 ? 0.601313 0.677128 0.750873 -0.0307011  0.07445     0.095612    131 GLU   A CD   
3543 O OE1  . GLU   B 119 ? 0.638176 0.718309 0.779459 -0.0152755  0.0817917   0.10071     131 GLU   A OE1  
3544 O OE2  . GLU   B 119 ? 0.647066 0.745194 0.825296 -0.0479034  0.0754438   0.0902419   131 GLU   A OE2  
3545 H H    . GLU   B 119 ? 0.514395 0.574436 0.613923 -0.0248017  0.00540904  0.0859743   131 GLU   A H    
3546 H HA   . GLU   B 119 ? 0.553387 0.573468 0.630967 -0.0144264  0.0342699   0.0973239   131 GLU   A HA   
3547 H HB2  . GLU   B 119 ? 0.564694 0.625829 0.680227 -0.0117354  0.0377546   0.0913476   131 GLU   A HB2  
3548 H HB3  . GLU   B 119 ? 0.560517 0.635196 0.695478 -0.0321595  0.0351043   0.0835287   131 GLU   A HB3  
3549 H HG2  . GLU   B 119 ? 0.62143  0.659612 0.749392 -0.0406317  0.0651805   0.0910382   131 GLU   A HG2  
3550 H HG3  . GLU   B 119 ? 0.620292 0.649475 0.724722 -0.0206324  0.066307    0.100899    131 GLU   A HG3  
3551 N N    . ILE   B 120 ? 0.575869 0.57718  0.659181 -0.0303119  0.0484525   0.0922493   132 ILE   A N    
3552 C CA   . ILE   B 120 ? 0.574175 0.558029 0.656043 -0.0354409  0.0559086   0.087138    132 ILE   A CA   
3553 C C    . ILE   B 120 ? 0.587159 0.545877 0.673006 -0.0358325  0.0747541   0.0944464   132 ILE   A C    
3554 O O    . ILE   B 120 ? 0.579037 0.530808 0.654988 -0.0251464  0.0802011   0.109135    132 ILE   A O    
3555 C CB   . ILE   B 120 ? 0.550891 0.531276 0.61549  -0.0249897  0.0503488   0.0921764   132 ILE   A CB   
3556 C CG1  . ILE   B 120 ? 0.560331 0.562968 0.617368 -0.0260548  0.0319211   0.0914631   132 ILE   A CG1  
3557 C CG2  . ILE   B 120 ? 0.579368 0.542342 0.643894 -0.0253647  0.0609487   0.0840192   132 ILE   A CG2  
3558 C CD1  . ILE   B 120 ? 0.565314 0.574227 0.610413 -0.0211097  0.0276935   0.0965769   132 ILE   A CD1  
3559 H H    . ILE   B 120 ? 0.580803 0.576001 0.655613 -0.022351   0.0515271   0.100218    132 ILE   A H    
3560 H HA   . ILE   B 120 ? 0.573511 0.564397 0.663092 -0.0456008  0.0529949   0.076304    132 ILE   A HA   
3561 H HB   . ILE   B 120 ? 0.562202 0.536058 0.61987  -0.0164891  0.0528573   0.102952    132 ILE   A HB   
3562 H HG12 . ILE   B 120 ? 0.554822 0.567215 0.617837 -0.034241   0.0277492   0.08258     132 ILE   A HG12 
3563 H HG13 . ILE   B 120 ? 0.549639 0.554752 0.603724 -0.0225444  0.026294    0.097207    132 ILE   A HG13 
3564 H HG21 . ILE   B 120 ? 0.575351 0.541463 0.632355 -0.0166016  0.0594451   0.0887516   132 ILE   A HG21 
3565 H HG22 . ILE   B 120 ? 0.580255 0.548724 0.647739 -0.034866   0.058212    0.0714426   132 ILE   A HG22 
3566 H HG23 . ILE   B 120 ? 0.593576 0.536624 0.661923 -0.0246283  0.0721239   0.0867165   132 ILE   A HG23 
3567 H HD11 . ILE   B 120 ? 0.565411 0.567966 0.606778 -0.0133143  0.0311914   0.10568     132 ILE   A HD11 
3568 H HD12 . ILE   B 120 ? 0.554869 0.575962 0.594528 -0.0239902  0.0158201   0.0991732   132 ILE   A HD12 
3569 H HD13 . ILE   B 120 ? 0.570989 0.579546 0.61748  -0.0229538  0.0333574   0.0887693   132 ILE   A HD13 
3570 N N    . GLU   B 121 ? 0.581636 0.525374 0.679262 -0.0502997  0.0833921   0.0840467   133 GLU   A N    
3571 C CA   . GLU   B 121 ? 0.603213 0.511801 0.702574 -0.0529164  0.101273    0.0917852   133 GLU   A CA   
3572 C C    . GLU   B 121 ? 0.638933 0.514029 0.727571 -0.0455462  0.106114    0.0855252   133 GLU   A C    
3573 O O    . GLU   B 121 ? 0.665447 0.537024 0.754666 -0.0554459  0.102667    0.0650867   133 GLU   A O    
3574 C CB   . GLU   B 121 ? 0.584646 0.495439 0.706034 -0.0773484  0.108066    0.0847683   133 GLU   A CB   
3575 C CG   . GLU   B 121 ? 0.658695 0.525379 0.781229 -0.084845   0.12699     0.0947128   133 GLU   A CG   
3576 C CD   . GLU   B 121 ? 0.742571 0.616372 0.889461 -0.112808   0.135289    0.0940147   133 GLU   A CD   
3577 O OE1  . GLU   B 121 ? 0.75476  0.676229 0.921561 -0.123771   0.126383    0.0862858   133 GLU   A OE1  
3578 O OE2  . GLU   B 121 ? 0.716045 0.548188 0.863405 -0.123425   0.150506    0.10318     133 GLU   A OE2  
3579 H H    . GLU   B 121 ? 0.584014 0.537701 0.687283 -0.0598144  0.0772805   0.072041    133 GLU   A H    
3580 H HA   . GLU   B 121 ? 0.600031 0.506605 0.692822 -0.0432151  0.105612    0.106428    133 GLU   A HA   
3581 H HB2  . GLU   B 121 ? 0.583685 0.520907 0.713934 -0.0783802  0.106391    0.0895604   133 GLU   A HB2  
3582 H HB3  . GLU   B 121 ? 0.600898 0.517025 0.727156 -0.0881449  0.101302    0.0693977   133 GLU   A HB3  
3583 H HG2  . GLU   B 121 ? 0.687995 0.525768 0.803667 -0.0842176  0.128749    0.086756    133 GLU   A HG2  
3584 H HG3  . GLU   B 121 ? 0.666741 0.526789 0.779607 -0.0716038  0.132648    0.111153    133 GLU   A HG3  
3585 N N    . LEU   B 122 ? 0.603517 0.456658 0.681448 -0.0266512  0.114039    0.102792    134 LEU   A N    
3586 C CA   . LEU   B 122 ? 0.691792 0.511504 0.7635   -0.0140211  0.122147    0.0992544   134 LEU   A CA   
3587 C C    . LEU   B 122 ? 0.792698 0.559898 0.869121 -0.0253294  0.138129    0.0969191   134 LEU   A C    
3588 O O    . LEU   B 122 ? 0.81513  0.560229 0.891619 -0.0236317  0.148166    0.118091    134 LEU   A O    
3589 C CB   . LEU   B 122 ? 0.688068 0.512128 0.750556 0.0128379   0.121774    0.120558    134 LEU   A CB   
3590 C CG   . LEU   B 122 ? 0.701193 0.498333 0.761642 0.0337177   0.131103    0.118886    134 LEU   A CG   
3591 C CD1  . LEU   B 122 ? 0.699144 0.5074   0.75844  0.0301477   0.128448    0.0917295   134 LEU   A CD1  
3592 C CD2  . LEU   B 122 ? 0.665845 0.485544 0.723366 0.0592364   0.126575    0.141712    134 LEU   A CD2  
3593 H H    . LEU   B 122 ? 0.619815 0.480046 0.693861 -0.0202387  0.114282    0.116984    134 LEU   A H    
3594 H HA   . LEU   B 122 ? 0.68285  0.512162 0.753179 -0.0163297  0.116947    0.0833756   134 LEU   A HA   
3595 H HB2  . LEU   B 122 ? 0.652701 0.508847 0.712371 0.0155106   0.110601    0.121131    134 LEU   A HB2  
3596 H HB3  . LEU   B 122 ? 0.691319 0.507    0.751706 0.0149091   0.12603     0.136729    134 LEU   A HB3  
3597 H HG   . LEU   B 122 ? 0.737341 0.495302 0.798618 0.0329278   0.142214    0.120782    134 LEU   A HG   
3598 H HD11 . LEU   B 122 ? 0.715727 0.504944 0.775636 0.0144028   0.131537    0.0763583   134 LEU   A HD11 
3599 H HD12 . LEU   B 122 ? 0.718843 0.517549 0.776694 0.0473377   0.134926    0.0911934   134 LEU   A HD12 
3600 H HD13 . LEU   B 122 ? 0.665058 0.509684 0.723488 0.0263422   0.11724     0.0906183   134 LEU   A HD13 
3601 H HD21 . LEU   B 122 ? 0.678852 0.492348 0.733091 0.0613986   0.12752     0.159011    134 LEU   A HD21 
3602 H HD22 . LEU   B 122 ? 0.641025 0.496503 0.697616 0.057424    0.115425    0.139907    134 LEU   A HD22 
3603 H HD23 . LEU   B 122 ? 0.69634  0.502267 0.755925 0.0751735   0.133559    0.141487    134 LEU   A HD23 
3604 N N    . LEU   B 123 ? 0.822283 0.567253 0.899581 -0.0392558  0.140055    0.0711239   135 LEU   A N    
3605 C CA   . LEU   B 123 ? 0.853244 0.542668 0.934133 -0.0572928  0.15296     0.0647639   135 LEU   A CA   
3606 C C    . LEU   B 123 ? 0.942875 0.573693 1.01217  -0.0326761  0.166907    0.0705648   135 LEU   A C    
3607 O O    . LEU   B 123 ? 1.00699  0.591058 1.07692  -0.0325873  0.179284    0.0891604   135 LEU   A O    
3608 C CB   . LEU   B 123 ? 0.84588  0.533302 0.928885 -0.0854673  0.14691     0.03176     135 LEU   A CB   
3609 C CG   . LEU   B 123 ? 0.827868 0.578493 0.924811 -0.106274   0.130496    0.0249404   135 LEU   A CG   
3610 C CD1  . LEU   B 123 ? 0.872034 0.624447 0.9656   -0.130573   0.12122     -0.00792539 135 LEU   A CD1  
3611 C CD2  . LEU   B 123 ? 0.876403 0.644198 0.995211 -0.124279   0.133998    0.0430088   135 LEU   A CD2  
3612 H H    . LEU   B 123 ? 0.800614 0.563911 0.874283 -0.0389303  0.132876    0.0569566   135 LEU   A H    
3613 H HA   . LEU   B 123 ? 0.860564 0.551092 0.949517 -0.0671861  0.156636    0.0795129   135 LEU   A HA   
3614 H HB2  . LEU   B 123 ? 0.86858  0.548667 0.939592 -0.0749589  0.146089    0.016806    135 LEU   A HB2  
3615 H HB3  . LEU   B 123 ? 0.90071  0.549484 0.986665 -0.101056   0.154748    0.0284588   135 LEU   A HB3  
3616 H HG   . LEU   B 123 ? 0.798108 0.581654 0.891172 -0.091067   0.122862    0.0305698   135 LEU   A HG   
3617 H HD11 . LEU   B 123 ? 0.87191  0.617666 0.9493   -0.118026   0.120388    -0.0196267  135 LEU   A HD11 
3618 H HD12 . LEU   B 123 ? 0.834353 0.62978  0.938126 -0.141251   0.10962     -0.00953089 135 LEU   A HD12 
3619 H HD13 . LEU   B 123 ? 0.906793 0.624658 1.00325  -0.148216   0.127502    -0.0153716  135 LEU   A HD13 
3620 H HD21 . LEU   B 123 ? 0.849152 0.614247 0.96532  -0.109235   0.140199    0.0629868   135 LEU   A HD21 
3621 H HD22 . LEU   B 123 ? 0.895678 0.635097 1.02051  -0.143488   0.140563    0.0382741   135 LEU   A HD22 
3622 H HD23 . LEU   B 123 ? 0.826372 0.63729  0.955421 -0.13169    0.123721    0.0396993   135 LEU   A HD23 
3623 N N    . ASP   B 124 ? 0.937304 0.572066 0.996589 -0.0107937  0.165771    0.0560536   136 ASP   A N    
3624 C CA   . ASP   B 124 ? 1.01998  0.603995 1.07114  0.01833     0.179822    0.0583454   136 ASP   A CA   
3625 C C    . ASP   B 124 ? 1.04186  0.664887 1.08841  0.0474041   0.176942    0.051761    136 ASP   A C    
3626 O O    . ASP   B 124 ? 0.931593 0.608477 0.976463 0.0382585   0.164808    0.0386722   136 ASP   A O    
3627 C CB   . ASP   B 124 ? 1.09785  0.608699 1.14057  0.00334005  0.191148    0.032331    136 ASP   A CB   
3628 C CG   . ASP   B 124 ? 1.2388   0.675615 1.27552  0.0315471   0.208584    0.043525    136 ASP   A CG   
3629 O OD1  . ASP   B 124 ? 1.26502  0.715739 1.30699  0.0630245   0.210659    0.0755338   136 ASP   A OD1  
3630 O OD2  . ASP   B 124 ? 1.2601   0.626951 1.28584  0.0227308   0.218493    0.0196217   136 ASP   A OD2  
3631 H H    . ASP   B 124 ? 0.913683 0.584943 0.971658 -0.0130832  0.156671    0.0451647   136 ASP   A H    
3632 H HA   . ASP   B 124 ? 1.03178  0.60378  1.08587  0.0294883   0.184125    0.0829641   136 ASP   A HA   
3633 H HB2  . ASP   B 124 ? 1.11817  0.619395 1.16634  -0.0239036  0.189527    0.0319475   136 ASP   A HB2  
3634 H HB3  . ASP   B 124 ? 1.11475  0.633752 1.14936  0.00076935  0.188583    0.00709618  136 ASP   A HB3  
3635 N N    . PHE   B 125 ? 1.03085  0.628003 1.07707  0.083067    0.188655    0.0638656   137 PHE   A N    
3636 C CA   . PHE   B 125 ? 0.973442 0.604913 1.01921  0.112876    0.191045    0.0568138   137 PHE   A CA   
3637 C C    . PHE   B 125 ? 1.05275  0.624019 1.096    0.147415    0.21072     0.0539575   137 PHE   A C    
3638 O O    . PHE   B 125 ? 1.0731   0.59963  1.12088  0.161128    0.217314    0.0785685   137 PHE   A O    
3639 C CB   . PHE   B 125 ? 0.886869 0.591603 0.944232 0.126025    0.177986    0.084977    137 PHE   A CB   
3640 C CG   . PHE   B 125 ? 0.9046   0.606602 0.970254 0.144213    0.176675    0.123435    137 PHE   A CG   
3641 C CD1  . PHE   B 125 ? 0.934637 0.640276 0.998245 0.123275    0.167675    0.14189     137 PHE   A CD1  
3642 C CD2  . PHE   B 125 ? 0.960251 0.666225 1.03533  0.183456    0.183364    0.142249    137 PHE   A CD2  
3643 C CE1  . PHE   B 125 ? 0.944285 0.65232  1.00893  0.139147    0.165399    0.177165    137 PHE   A CE1  
3644 C CE2  . PHE   B 125 ? 0.976351 0.68694  1.05661  0.19956     0.178702    0.179864    137 PHE   A CE2  
3645 C CZ   . PHE   B 125 ? 0.930871 0.641349 1.0029   0.176197    0.1694      0.19681     137 PHE   A CZ   
3646 H H    . PHE   B 125 ? 1.06177  0.62165  1.10936  0.0895498   0.19562     0.0786307   137 PHE   A H    
3647 H HA   . PHE   B 125 ? 0.972015 0.61826  1.01032  0.100229    0.188351    0.0331624   137 PHE   A HA   
3648 H HB2  . PHE   B 125 ? 0.891373 0.622857 0.950753 0.142787    0.180266    0.07966     137 PHE   A HB2  
3649 H HB3  . PHE   B 125 ? 0.855192 0.590473 0.911493 0.104507    0.166369    0.0823945   137 PHE   A HB3  
3650 H HD1  . PHE   B 125 ? 0.904757 0.613318 0.965484 0.0989937   0.163352    0.130553    137 PHE   A HD1  
3651 H HD2  . PHE   B 125 ? 0.973148 0.680701 1.0509   0.200456    0.191281    0.129763    137 PHE   A HD2  
3652 H HE1  . PHE   B 125 ? 0.921589 0.631972 0.981551 0.125168    0.161067    0.188127    137 PHE   A HE1  
3653 H HE2  . PHE   B 125 ? 0.985977 0.702223 1.07472  0.227491    0.182184    0.19378     137 PHE   A HE2  
3654 H HZ   . PHE   B 125 ? 0.951433 0.665333 1.02275  0.186476    0.166215    0.221895    137 PHE   A HZ   
3655 N N    . LYS   B 126 ? 1.10816  0.677471 1.14179  0.161983    0.22065     0.023762    138 LYS   A N    
3656 C CA   . LYS   B 126 ? 1.14378  0.657265 1.17327  0.200381    0.241701    0.0141679   138 LYS   A CA   
3657 C C    . LYS   B 126 ? 1.14562  0.726749 1.18358  0.235418    0.247224    0.0125802   138 LYS   A C    
3658 O O    . LYS   B 126 ? 1.09125  0.739417 1.12605  0.21998     0.238388    0.00125002  138 LYS   A O    
3659 C CB   . LYS   B 126 ? 1.19163  0.624878 1.19587  0.181585    0.25238     -0.0281278  138 LYS   A CB   
3660 H H    . LYS   B 126 ? 1.06289  0.667683 1.09107  0.148536    0.214552    0.00831754  138 LYS   A H    
3661 H HA   . LYS   B 126 ? 1.17171  0.657054 1.20971  0.215577    0.244992    0.03825     138 LYS   A HA   
3664 N N    . GLY   B 127 ? 1.19953  0.769338 1.25089  0.283289    0.261662    0.0275697   139 GLY   A N    
3665 C CA   . GLY   B 127 ? 1.19763  0.847089 1.26567  0.316726    0.266858    0.0327928   139 GLY   A CA   
3666 C C    . GLY   B 127 ? 1.27252  0.916649 1.32041  0.32653     0.285217    -0.0113886  139 GLY   A C    
3667 O O    . GLY   B 127 ? 1.33638  0.89328  1.36247  0.333209    0.300998    -0.040554   139 GLY   A O    
3668 H H    . GLY   B 127 ? 1.24713  0.761368 1.2988   0.295608    0.268481    0.0360525   139 GLY   A H    
3669 H HA2  . GLY   B 127 ? 1.13476  0.847459 1.21106  0.300429    0.252351    0.0457339   139 GLY   A HA2  
3670 H HA3  . GLY   B 127 ? 1.21969  0.866274 1.30399  0.349606    0.272868    0.0536589   139 GLY   A HA3  
3671 N N    . GLU   B 128 ? 1.27767  1.0123   1.3303   0.326913    0.283788    -0.0158636  140 GLU   A N    
3672 C CA   . GLU   B 128 ? 1.30486  1.04641  1.33287  0.332739    0.30112     -0.0570607  140 GLU   A CA   
3673 C C    . GLU   B 128 ? 1.45936  1.12503  1.47949  0.379829    0.330041    -0.0787058  140 GLU   A C    
3674 O O    . GLU   B 128 ? 1.47827  1.15561  1.52887  0.425749    0.339637    -0.0516016  140 GLU   A O    
3675 C CB   . GLU   B 128 ? 1.23053  1.08495  1.27183  0.338411    0.30107     -0.0483798  140 GLU   A CB   
3676 O OXT  . GLU   B 128 ? 1.52972  1.12224  1.51288  0.368983    0.340679    -0.121659   140 GLU   A OXT  
3677 H H    . GLU   B 128 ? 1.2064   0.999492 1.27636  0.322338    0.271772    0.00782663  140 GLU   A H    
3678 H HA   . GLU   B 128 ? 1.31487  1.03071  1.31915  0.300253    0.294319    -0.0784335  140 GLU   A HA   
3681 C CAK  . A1IN4 C .   ? 0.660255 0.558668 0.544126 -0.094921   -0.258357   0.0501831   201 A1IN4 B CAK  
3682 C CAL  . A1IN4 C .   ? 0.736759 0.585001 0.57178  -0.083381   -0.249947   0.032938    201 A1IN4 B CAL  
3683 C CAM  . A1IN4 C .   ? 0.718992 0.51953  0.576677 -0.0984902  -0.22331    0.040227    201 A1IN4 B CAM  
3684 C CAN  . A1IN4 C .   ? 0.661369 0.485697 0.535946 -0.0966513  -0.202224   0.0696568   201 A1IN4 B CAN  
3685 C CAO  . A1IN4 C .   ? 0.605204 0.482245 0.528016 -0.106602   -0.208637   0.0860851   201 A1IN4 B CAO  
3686 C CAJ  . A1IN4 C .   ? 0.616044 0.533704 0.520058 -0.0936052  -0.234316   0.0815126   201 A1IN4 B CAJ  
3687 C CAI  . A1IN4 C .   ? 0.580736 0.545435 0.529339 -0.0992098  -0.243189   0.0999128   201 A1IN4 B CAI  
3688 C CAB  . A1IN4 C .   ? 0.575007 0.556623 0.535369 -0.0946983  -0.223467   0.127914    201 A1IN4 B CAB  
3689 O OAA  . A1IN4 C .   ? 0.578815 0.558683 0.508246 -0.0825991  -0.210001   0.136367    201 A1IN4 B OAA  
3690 N N    . A1IN4 C .   ? 0.549113 0.549878 0.560739 -0.103462   -0.219125   0.145473    201 A1IN4 B N    
3691 C CAH  . A1IN4 C .   ? 0.552411 0.570919 0.613874 -0.114583   -0.235587   0.140096    201 A1IN4 B CAH  
3692 C CAG  . A1IN4 C .   ? 0.524    0.544111 0.646914 -0.125993   -0.2183     0.152596    201 A1IN4 B CAG  
3693 C CAF  . A1IN4 C .   ? 0.504824 0.534594 0.631364 -0.116087   -0.204451   0.178278    201 A1IN4 B CAF  
3694 C CB   . A1IN4 C .   ? 0.481564 0.482925 0.562716 -0.112997   -0.186498   0.17809     201 A1IN4 B CB   
3695 C CA   . A1IN4 C .   ? 0.530443 0.54212  0.555557 -0.0997782  -0.201608   0.171329    201 A1IN4 B CA   
3696 C C    . A1IN4 C .   ? 0.561355 0.609987 0.581171 -0.0864229  -0.211047   0.192752    201 A1IN4 B C    
3697 O O    . A1IN4 C .   ? 0.532179 0.587743 0.564396 -0.0844517  -0.197643   0.215195    201 A1IN4 B O    
3698 O OBB  . A1IN4 C .   ? 0.563328 0.633048 0.557983 -0.0758059  -0.234947   0.185415    201 A1IN4 B OBB  
3699 C CBA  . A1IN4 C .   ? 0.590021 0.695052 0.563704 -0.0566876  -0.241917   0.21152     201 A1IN4 B CBA  
3700 C CAZ  . A1IN4 C .   ? 0.618996 0.744589 0.551557 -0.0411108  -0.270656   0.199832    201 A1IN4 B CAZ  
3701 C CAY  . A1IN4 C .   ? 0.63291  0.758366 0.595593 -0.0530246  -0.298114   0.173407    201 A1IN4 B CAY  
3702 C CAX  . A1IN4 C .   ? 0.698822 0.851776 0.617442 -0.0345032  -0.337121   0.160376    201 A1IN4 B CAX  
3703 C CAW  . A1IN4 C .   ? 0.727201 0.8688   0.559951 -0.0152628  -0.338856   0.142975    201 A1IN4 B CAW  
3704 O OAV  . A1IN4 C .   ? 0.723291 0.827252 0.539706 -0.0265042  -0.350128   0.0973053   201 A1IN4 B OAV  
3705 C CAU  . A1IN4 C .   ? 0.676116 0.747012 0.535177 -0.0487088  -0.325531   0.0944065   201 A1IN4 B CAU  
3706 C CAR  . A1IN4 C .   ? 0.655238 0.713826 0.581087 -0.076252   -0.331516   0.0814994   201 A1IN4 B CAR  
3707 O OAS  . A1IN4 C .   ? 0.697022 0.779982 0.646717 -0.0816407  -0.368539   0.0646058   201 A1IN4 B OAS  
3708 C CAT  . A1IN4 C .   ? 0.671059 0.759409 0.710201 -0.109993   -0.371742   0.0597402   201 A1IN4 B CAT  
3709 C CAQ  . A1IN4 C .   ? 0.608735 0.63024  0.566801 -0.0949659  -0.302028   0.0822679   201 A1IN4 B CAQ  
3710 C CAP  . A1IN4 C .   ? 0.611839 0.613611 0.539423 -0.0856823  -0.271564   0.0965601   201 A1IN4 B CAP  
3711 C CBH  . A1IN4 C .   ? 0.619712 0.643071 0.493599 -0.0602956  -0.269426   0.108806    201 A1IN4 B CBH  
3712 C CBE  . A1IN4 C .   ? 0.670962 0.727285 0.510416 -0.0419572  -0.291992   0.109955    201 A1IN4 B CBE  
3713 O OBF  . A1IN4 C .   ? 0.679456 0.757365 0.464441 -0.0158318  -0.285147   0.12414     201 A1IN4 B OBF  
3714 C CBG  . A1IN4 C .   ? 0.728749 0.794102 0.496856 -0.00892291 -0.256467   0.12995     201 A1IN4 B CBG  
3715 H HAK  . A1IN4 C .   ? 0.681834 0.611131 0.549638 -0.0840946  -0.275538   0.0493816   201 A1IN4 B HAK  
3716 H HB6  . A1IN4 C .   ? 0.682166 0.56248  0.601846 -0.115065   -0.262574   0.0386901   201 A1IN4 B HB6  
3717 H HAL  . A1IN4 C .   ? 0.771499 0.600561 0.591504 -0.0848807  -0.268511   0.00715443  201 A1IN4 B HAL  
3718 H HB7  . A1IN4 C .   ? 0.721314 0.583664 0.519749 -0.0614744  -0.242883   0.0415587   201 A1IN4 B HB7  
3719 H HAM  . A1IN4 C .   ? 0.728008 0.515104 0.625626 -0.120825   -0.225944   0.0330494   201 A1IN4 B HAM  
3720 H HB8  . A1IN4 C .   ? 0.751923 0.513434 0.571849 -0.0864791  -0.21683    0.0310432   201 A1IN4 B HB8  
3721 H HAN  . A1IN4 C .   ? 0.661423 0.452568 0.546178 -0.105772   -0.184926   0.0736897   201 A1IN4 B HAN  
3722 H HB9  . A1IN4 C .   ? 0.654472 0.489356 0.496099 -0.0772895  -0.198502   0.0757272   201 A1IN4 B HB9  
3723 H HCA  . A1IN4 C .   ? 0.579261 0.472771 0.50561  -0.101682   -0.19759    0.103485    201 A1IN4 B HCA  
3724 H HAO  . A1IN4 C .   ? 0.607643 0.483398 0.570669 -0.123756   -0.211325   0.0824213   201 A1IN4 B HAO  
3725 H HAJ  . A1IN4 C .   ? 0.612866 0.54072  0.481291 -0.0754149  -0.228717   0.0887809   201 A1IN4 B HAJ  
3726 H HAI  . A1IN4 C .   ? 0.585357 0.542532 0.577394 -0.11689    -0.243855   0.0945725   201 A1IN4 B HAI  
3727 H HAH  . A1IN4 C .   ? 0.562505 0.61284  0.618419 -0.103943   -0.254802   0.146677    201 A1IN4 B HAH  
3728 H HB5  . A1IN4 C .   ? 0.572537 0.573935 0.634774 -0.124042   -0.24368    0.119029    201 A1IN4 B HB5  
3729 H HAG  . A1IN4 C .   ? 0.527666 0.572149 0.690674 -0.129905   -0.232128   0.151848    201 A1IN4 B HAG  
3730 H HB4  . A1IN4 C .   ? 0.521518 0.511585 0.64819  -0.135045   -0.19883    0.147342    201 A1IN4 B HB4  
3731 H HAF  . A1IN4 C .   ? 0.504698 0.559567 0.622126 -0.104648   -0.216547   0.191394    201 A1IN4 B HAF  
3732 H HB3  . A1IN4 C .   ? 0.486964 0.510519 0.649585 -0.121431   -0.189523   0.184451    201 A1IN4 B HB3  
3733 H HB2  . A1IN4 C .   ? 0.495844 0.468385 0.567995 -0.119621   -0.175825   0.165794    201 A1IN4 B HB2  
3734 H HB1  . A1IN4 C .   ? 0.481227 0.485802 0.564105 -0.109219   -0.1777     0.192471    201 A1IN4 B HB1  
3735 H HA   . A1IN4 C .   ? 0.524896 0.521259 0.525697 -0.0968548  -0.189708   0.170282    201 A1IN4 B HA   
3736 H HCH  . A1IN4 C .   ? 0.587194 0.693176 0.532164 -0.0491332  -0.229212   0.218739    201 A1IN4 B HCH  
3737 H HBA  . A1IN4 C .   ? 0.576244 0.694291 0.58079  -0.0556582  -0.240065   0.233861    201 A1IN4 B HBA  
3738 H HCG  . A1IN4 C .   ? 0.644893 0.764114 0.532438 -0.0324698  -0.270952   0.186545    201 A1IN4 B HCG  
3739 H HAZ  . A1IN4 C .   ? 0.634311 0.78423  0.568493 -0.0293564  -0.27406    0.225796    201 A1IN4 B HAZ  
3740 H HCF  . A1IN4 C .   ? 0.615846 0.753549 0.627432 -0.0592232  -0.300214   0.184906    201 A1IN4 B HCF  
3741 H HAY  . A1IN4 C .   ? 0.631641 0.73149  0.595119 -0.0650184  -0.29643    0.149655    201 A1IN4 B HAY  
3742 H HCE  . A1IN4 C .   ? 0.707477 0.887527 0.616897 -0.018544   -0.344334   0.183802    201 A1IN4 B HCE  
3743 H HAX  . A1IN4 C .   ? 0.707905 0.855763 0.641045 -0.0457298  -0.359796   0.130972    201 A1IN4 B HAX  
3744 H HCD  . A1IN4 C .   ? 0.710352 0.84388  0.523693 -0.00955454 -0.312835   0.155871    201 A1IN4 B HCD  
3745 H HAW  . A1IN4 C .   ? 0.767234 0.931061 0.562676 0.00301902  -0.359694   0.144328    201 A1IN4 B HAW  
3746 H HCC  . A1IN4 C .   ? 0.693382 0.815282 0.754753 -0.109914   -0.404679   0.0509985   201 A1IN4 B HCC  
3747 H HAT  . A1IN4 C .   ? 0.680309 0.7319   0.729645 -0.127631   -0.364914   0.0386198   201 A1IN4 B HAT  
3748 H HCB  . A1IN4 C .   ? 0.627912 0.723646 0.702036 -0.112371   -0.347869   0.0858873   201 A1IN4 B HCB  
3749 H HAQ  . A1IN4 C .   ? 0.608971 0.621514 0.61806  -0.115388   -0.301672   0.0749136   201 A1IN4 B HAQ  
3750 H HBH  . A1IN4 C .   ? 0.609252 0.624824 0.468957 -0.0541804  -0.248535   0.11857     201 A1IN4 B HBH  
3751 H HCJ  . A1IN4 C .   ? 0.734029 0.819671 0.459984 0.0128317   -0.250685   0.138599    201 A1IN4 B HCJ  
3752 H HBG  . A1IN4 C .   ? 0.665006 0.735201 0.471881 -0.0197264  -0.239303   0.150957    201 A1IN4 B HBG  
3753 H HCI  . A1IN4 C .   ? 0.718928 0.750492 0.476375 -0.0123508  -0.257036   0.105375    201 A1IN4 B HCI  
3754 C CAK  . A1IN4 D .   ? 0.531603 0.72815  0.540009 -0.0856618  -0.11308    0.103365    201 A1IN4 A CAK  
3755 C CAL  . A1IN4 D .   ? 0.552229 0.74547  0.57647  -0.070711   -0.129141   0.122083    201 A1IN4 A CAL  
3756 C CAM  . A1IN4 D .   ? 0.537848 0.703201 0.583923 -0.0538797  -0.119241   0.122383    201 A1IN4 A CAM  
3757 C CAN  . A1IN4 D .   ? 0.555805 0.68867  0.587028 -0.0551692  -0.102685   0.120559    201 A1IN4 A CAN  
3758 C CAO  . A1IN4 D .   ? 0.523121 0.664162 0.547174 -0.0679383  -0.086754   0.10397     201 A1IN4 A CAO  
3759 C CAJ  . A1IN4 D .   ? 0.544004 0.709638 0.545713 -0.0811538  -0.0951498  0.104264    201 A1IN4 A CAJ  
3760 C CAI  . A1IN4 D .   ? 0.51733  0.685784 0.507905 -0.089995   -0.0765451  0.0839353   201 A1IN4 A CAI  
3761 C CAB  . A1IN4 D .   ? 0.553485 0.705609 0.536801 -0.0848461  -0.0622774  0.0889988   201 A1IN4 A CAB  
3762 O OAA  . A1IN4 D .   ? 0.553561 0.70152  0.529165 -0.0832887  -0.0699196  0.10924     201 A1IN4 A OAA  
3763 N N    . A1IN4 D .   ? 0.48343  0.623874 0.470313 -0.0816594  -0.0415506  0.0730603   201 A1IN4 A N    
3764 C CAH  . A1IN4 D .   ? 0.49793  0.636215 0.488775 -0.0884211  -0.0334602  0.047564    201 A1IN4 A CAH  
3765 C CAG  . A1IN4 D .   ? 0.533299 0.642098 0.539587 -0.0804998  -0.0147042  0.039377    201 A1IN4 A CAG  
3766 C CAF  . A1IN4 D .   ? 0.518154 0.621205 0.513399 -0.0703149  0.0003722   0.0411363   201 A1IN4 A CAF  
3767 C CB   . A1IN4 D .   ? 0.506086 0.615582 0.503799 -0.0636709  -0.00778321 0.066626    201 A1IN4 A CB   
3768 C CA   . A1IN4 D .   ? 0.503455 0.636987 0.487143 -0.0736274  -0.0271233  0.0793135   201 A1IN4 A CA   
3769 C C    . A1IN4 D .   ? 0.523204 0.68016  0.48702  -0.0781563  -0.0218588  0.0770273   201 A1IN4 A C    
3770 O O    . A1IN4 D .   ? 0.477339 0.643396 0.439221 -0.0725301  -0.0107943  0.083189    201 A1IN4 A O    
3771 O OBB  . A1IN4 D .   ? 0.515798 0.690884 0.462253 -0.0891773  -0.0299546  0.0678895   201 A1IN4 A OBB  
3772 C CBA  . A1IN4 D .   ? 0.620909 0.818234 0.542843 -0.0921345  -0.0187642  0.0578798   201 A1IN4 A CBA  
3773 C CAZ  . A1IN4 D .   ? 0.669588 0.886776 0.569685 -0.106596   -0.0343138  0.050936    201 A1IN4 A CAZ  
3774 C CAY  . A1IN4 D .   ? 0.663757 0.873981 0.550463 -0.110166   -0.022231   0.0155053   201 A1IN4 A CAY  
3775 C CAX  . A1IN4 D .   ? 0.704056 0.931226 0.573553 -0.127345   -0.0403085  0.00213986  201 A1IN4 A CAX  
3776 C CAW  . A1IN4 D .   ? 0.698493 0.962852 0.548869 -0.136432   -0.064345   0.0280185   201 A1IN4 A CAW  
3777 O OAV  . A1IN4 D .   ? 0.716862 0.984912 0.590832 -0.139502   -0.0886628  0.0408057   201 A1IN4 A OAV  
3778 C CAU  . A1IN4 D .   ? 0.658534 0.902377 0.567266 -0.127417   -0.0871892  0.054092    201 A1IN4 A CAU  
3779 C CAR  . A1IN4 D .   ? 0.616465 0.842959 0.554169 -0.126206   -0.0822106  0.0379406   201 A1IN4 A CAR  
3780 O OAS  . A1IN4 D .   ? 0.688877 0.923048 0.618814 -0.140612   -0.0822733  0.010515    201 A1IN4 A OAS  
3781 C CAT  . A1IN4 D .   ? 0.718956 0.942159 0.681316 -0.145776   -0.0810712  -0.00280864 201 A1IN4 A CAT  
3782 C CAQ  . A1IN4 D .   ? 0.59968  0.803832 0.567702 -0.113352   -0.0785275  0.0502862   201 A1IN4 A CAQ  
3783 C CAP  . A1IN4 D .   ? 0.62918  0.823446 0.596094 -0.102808   -0.0810658  0.0752499   201 A1IN4 A CAP  
3784 C CBH  . A1IN4 D .   ? 0.570223 0.779742 0.509121 -0.107526   -0.0870194  0.0908662   201 A1IN4 A CBH  
3785 C CBE  . A1IN4 D .   ? 0.662827 0.899285 0.573184 -0.119189   -0.0890632  0.0820075   201 A1IN4 A CBE  
3786 O OBF  . A1IN4 D .   ? 0.655291 0.913335 0.534695 -0.125954   -0.0927052  0.0985595   201 A1IN4 A OBF  
3787 C CBG  . A1IN4 D .   ? 0.681006 0.929067 0.563005 -0.123145   -0.0980614  0.128941    201 A1IN4 A CBG  
3788 H HAK  . A1IN4 D .   ? 0.557817 0.766814 0.543197 -0.0938615  -0.118769   0.10762     201 A1IN4 A HAK  
3789 H HB6  . A1IN4 D .   ? 0.538109 0.739474 0.558555 -0.0913817  -0.103038   0.0841693   201 A1IN4 A HB6  
3790 H HAL  . A1IN4 D .   ? 0.554464 0.775436 0.591421 -0.0719964  -0.140077   0.120017    201 A1IN4 A HAL  
3791 H HB7  . A1IN4 D .   ? 0.562032 0.747552 0.567607 -0.0700947  -0.139247   0.139436    201 A1IN4 A HB7  
3792 H HAM  . A1IN4 D .   ? 0.53344  0.71192  0.602014 -0.0534559  -0.112134   0.110167    201 A1IN4 A HAM  
3793 H HB8  . A1IN4 D .   ? 0.5537   0.710075 0.60219  -0.0415748  -0.130967   0.136593    201 A1IN4 A HB8  
3794 H HAN  . A1IN4 D .   ? 0.535046 0.65106  0.578521 -0.0450046  -0.0948175  0.118074    201 A1IN4 A HAN  
3795 H HB9  . A1IN4 D .   ? 0.554399 0.675308 0.567646 -0.0564027  -0.110556   0.134631    201 A1IN4 A HB9  
3796 H HCA  . A1IN4 D .   ? 0.52443  0.650397 0.539684 -0.0671995  -0.0777949  0.105929    201 A1IN4 A HCA  
3797 H HAO  . A1IN4 D .   ? 0.525151 0.673963 0.563382 -0.0709833  -0.0794404  0.089843    201 A1IN4 A HAO  
3798 H HAJ  . A1IN4 D .   ? 0.541054 0.701859 0.527121 -0.0814362  -0.102073   0.12048     201 A1IN4 A HAJ  
3799 H HAI  . A1IN4 D .   ? 0.540138 0.702556 0.547834 -0.0896405  -0.0689149  0.0704303   201 A1IN4 A HAI  
3800 H HAH  . A1IN4 D .   ? 0.527033 0.676206 0.498889 -0.0942074  -0.0301042  0.0368788   201 A1IN4 A HAH  
3801 H HB5  . A1IN4 D .   ? 0.508097 0.654403 0.509546 -0.0937927  -0.044244   0.0457095   201 A1IN4 A HB5  
3802 H HAG  . A1IN4 D .   ? 0.537304 0.636195 0.544978 -0.0863735  -0.00685957 0.0215862   201 A1IN4 A HAG  
3803 H HB4  . A1IN4 D .   ? 0.503205 0.601762 0.523334 -0.0737493  -0.0150995  0.0499637   201 A1IN4 A HB4  
3804 H HAF  . A1IN4 D .   ? 0.539055 0.657521 0.517371 -0.0732073  0.00181824  0.0359893   201 A1IN4 A HAF  
3805 H HB3  . A1IN4 D .   ? 0.527273 0.609291 0.530811 -0.0626164  0.0137065   0.0368541   201 A1IN4 A HB3  
3806 H HB2  . A1IN4 D .   ? 0.490322 0.588022 0.499297 -0.0605452  -0.0122925  0.073859    201 A1IN4 A HB2  
3807 H HB1  . A1IN4 D .   ? 0.50331  0.616488 0.497835 -0.0573437  0.00102871  0.0706881   201 A1IN4 A HB1  
3808 H HA   . A1IN4 D .   ? 0.489784 0.618946 0.475861 -0.0713258  -0.0347488  0.096052    201 A1IN4 A HA   
3809 H HCH  . A1IN4 D .   ? 0.608474 0.824925 0.52147  -0.0933079  -0.0184047  0.0731282   201 A1IN4 A HCH  
3810 H HBA  . A1IN4 D .   ? 0.620724 0.807875 0.541312 -0.0867338  -0.00307027 0.0379268   201 A1IN4 A HBA  
3811 H HCG  . A1IN4 D .   ? 0.644968 0.854432 0.558475 -0.10897    -0.0466119  0.0523875   201 A1IN4 A HCG  
3812 H HAZ  . A1IN4 D .   ? 0.666231 0.90701  0.547594 -0.112842   -0.0416608  0.0653303   201 A1IN4 A HAZ  
3813 H HCF  . A1IN4 D .   ? 0.695639 0.917667 0.561554 -0.108273   -0.0102098  0.00787548  201 A1IN4 A HCF  
3814 H HAY  . A1IN4 D .   ? 0.670409 0.85419  0.573965 -0.10608    -0.0140603  0.002114    201 A1IN4 A HAY  
3815 H HCE  . A1IN4 D .   ? 0.730053 0.962704 0.574254 -0.131152   -0.0316809  -0.0169408  201 A1IN4 A HCE  
3816 H HAX  . A1IN4 D .   ? 0.694441 0.909282 0.581503 -0.131659   -0.0458086  -0.0072281  201 A1IN4 A HAX  
3817 H HCD  . A1IN4 D .   ? 0.696428 0.965926 0.547041 -0.132013   -0.0655077  0.051529    201 A1IN4 A HCD  
3818 H HAW  . A1IN4 D .   ? 0.739393 1.02437  0.563716 -0.147099   -0.0715129  0.0180411   201 A1IN4 A HAW  
3819 H HCC  . A1IN4 D .   ? 0.735859 0.966659 0.688214 -0.161428   -0.0842968  -0.0240625  201 A1IN4 A HCC  
3820 H HAT  . A1IN4 D .   ? 0.689876 0.928131 0.674706 -0.142182   -0.094695   0.0128501   201 A1IN4 A HAT  
3821 H HCB  . A1IN4 D .   ? 0.695856 0.88909  0.669612 -0.138029   -0.0632653  -0.006745   201 A1IN4 A HCB  
3822 H HAQ  . A1IN4 D .   ? 0.598278 0.791626 0.588299 -0.113065   -0.0730255  0.0400776   201 A1IN4 A HAQ  
3823 H HBH  . A1IN4 D .   ? 0.592054 0.791745 0.530649 -0.103316   -0.0900033  0.110265    201 A1IN4 A HBH  
3824 H HCJ  . A1IN4 D .   ? 0.690694 0.95894  0.548304 -0.13171    -0.101015   0.142268    201 A1IN4 A HCJ  
3825 H HBG  . A1IN4 D .   ? 0.651769 0.885653 0.545518 -0.1174     -0.0838679  0.126508    201 A1IN4 A HBG  
3826 H HCI  . A1IN4 D .   ? 0.663997 0.899227 0.559338 -0.118764   -0.11349    0.14155     201 A1IN4 A HCI  
# 
