data_9GQ9
# 
_entry.id   9GQ9 
# 
_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   9GQ9         pdb_00009gq9 10.2210/pdb9gq9/pdb 
WWPDB D_1292141301 ?            ?                   
# 
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                        9GQ9 
_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},14~{E})-2-cyclohexyl-20,23-dimethoxy-11,18-dioxa-4-azatricyclo[17.2.2.0^{4,9}]tricosa-1(22),14,19(23),20-tetraene-3,10-dione
;
485.612   2  ?       ?                    ? ? 
3 water       nat water 18.015    52 ?       ?                    ? ? 
# 
_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},14~{E})-2-cyclohexyl-20,23-dimethoxy-11,18-dioxa-4-azatricyclo[17.2.2.0^{4,9}]tricosa-1(22),14,19(23),20-tetraene-3,10-dione
;
A1IN3 
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 
A1IN3 non-polymer         . 
;(2~{S},9~{S},14~{E})-2-cyclohexyl-20,23-dimethoxy-11,18-dioxa-4-azatricyclo[17.2.2.0^{4,9}]tricosa-1(22),14,19(23),20-tetraene-3,10-dione
;
? 'C28 H39 N O6'   485.612 
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        A1IN3 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IN3 
_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 A1IN3 1  201 201 A1IN3 PDB B . 
D 2 A1IN3 1  201 201 A1IN3 PDB A . 
E 3 HOH   1  301 46  HOH   HOH B . 
E 3 HOH   2  302 48  HOH   HOH B . 
E 3 HOH   3  303 54  HOH   HOH B . 
E 3 HOH   4  304 1   HOH   HOH B . 
E 3 HOH   5  305 5   HOH   HOH B . 
E 3 HOH   6  306 34  HOH   HOH B . 
E 3 HOH   7  307 44  HOH   HOH B . 
E 3 HOH   8  308 13  HOH   HOH B . 
E 3 HOH   9  309 32  HOH   HOH B . 
E 3 HOH   10 310 33  HOH   HOH B . 
E 3 HOH   11 311 25  HOH   HOH B . 
E 3 HOH   12 312 20  HOH   HOH B . 
E 3 HOH   13 313 21  HOH   HOH B . 
E 3 HOH   14 314 28  HOH   HOH B . 
E 3 HOH   15 315 4   HOH   HOH B . 
E 3 HOH   16 316 3   HOH   HOH B . 
E 3 HOH   17 317 36  HOH   HOH B . 
E 3 HOH   18 318 9   HOH   HOH B . 
E 3 HOH   19 319 49  HOH   HOH B . 
E 3 HOH   20 320 23  HOH   HOH B . 
E 3 HOH   21 321 19  HOH   HOH B . 
E 3 HOH   22 322 22  HOH   HOH B . 
E 3 HOH   23 323 17  HOH   HOH B . 
E 3 HOH   24 324 52  HOH   HOH B . 
E 3 HOH   25 325 47  HOH   HOH B . 
E 3 HOH   26 326 42  HOH   HOH B . 
E 3 HOH   27 327 39  HOH   HOH B . 
E 3 HOH   28 328 41  HOH   HOH B . 
E 3 HOH   29 329 43  HOH   HOH B . 
E 3 HOH   30 330 51  HOH   HOH B . 
E 3 HOH   31 331 45  HOH   HOH B . 
F 3 HOH   1  301 50  HOH   HOH A . 
F 3 HOH   2  302 37  HOH   HOH A . 
F 3 HOH   3  303 31  HOH   HOH A . 
F 3 HOH   4  304 53  HOH   HOH A . 
F 3 HOH   5  305 10  HOH   HOH A . 
F 3 HOH   6  306 11  HOH   HOH A . 
F 3 HOH   7  307 12  HOH   HOH A . 
F 3 HOH   8  308 6   HOH   HOH A . 
F 3 HOH   9  309 8   HOH   HOH A . 
F 3 HOH   10 310 29  HOH   HOH A . 
F 3 HOH   11 311 55  HOH   HOH A . 
F 3 HOH   12 312 16  HOH   HOH A . 
F 3 HOH   13 313 26  HOH   HOH A . 
F 3 HOH   14 314 24  HOH   HOH A . 
F 3 HOH   15 315 15  HOH   HOH A . 
F 3 HOH   16 316 18  HOH   HOH A . 
F 3 HOH   17 317 30  HOH   HOH A . 
F 3 HOH   18 318 27  HOH   HOH A . 
F 3 HOH   19 319 35  HOH   HOH A . 
F 3 HOH   20 320 38  HOH   HOH A . 
F 3 HOH   21 321 40  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 52  ? CD  ? A LYS 40  CD  
10  1 Y 1 B LYS 52  ? CE  ? A LYS 40  CE  
11  1 Y 1 B LYS 52  ? NZ  ? A LYS 40  NZ  
12  1 Y 1 B LYS 60  ? NZ  ? A LYS 48  NZ  
13  1 Y 1 B LYS 65  ? CG  ? A LYS 53  CG  
14  1 Y 1 B LYS 65  ? CD  ? A LYS 53  CD  
15  1 Y 1 B LYS 65  ? CE  ? A LYS 53  CE  
16  1 Y 1 B LYS 65  ? NZ  ? A LYS 53  NZ  
17  1 Y 1 B LYS 66  ? CG  ? A LYS 54  CG  
18  1 Y 1 B LYS 66  ? CD  ? A LYS 54  CD  
19  1 Y 1 B LYS 66  ? CE  ? A LYS 54  CE  
20  1 Y 1 B LYS 66  ? NZ  ? A LYS 54  NZ  
21  1 Y 1 B ASP 72  ? CG  ? A ASP 60  CG  
22  1 Y 1 B ASP 72  ? OD1 ? A ASP 60  OD1 
23  1 Y 1 B ASP 72  ? OD2 ? A ASP 60  OD2 
24  1 Y 1 B ARG 73  ? CG  ? A ARG 61  CG  
25  1 Y 1 B ARG 73  ? CD  ? A ARG 61  CD  
26  1 Y 1 B ARG 73  ? NE  ? A ARG 61  NE  
27  1 Y 1 B ARG 73  ? CZ  ? A ARG 61  CZ  
28  1 Y 1 B ARG 73  ? NH1 ? A ARG 61  NH1 
29  1 Y 1 B ARG 73  ? NH2 ? A ARG 61  NH2 
30  1 Y 1 B ASN 74  ? CG  ? A ASN 62  CG  
31  1 Y 1 B ASN 74  ? OD1 ? A ASN 62  OD1 
32  1 Y 1 B ASN 74  ? ND2 ? A ASN 62  ND2 
33  1 Y 1 B LYS 83  ? CG  ? A LYS 71  CG  
34  1 Y 1 B LYS 83  ? CD  ? A LYS 71  CD  
35  1 Y 1 B LYS 83  ? CE  ? A LYS 71  CE  
36  1 Y 1 B LYS 83  ? NZ  ? A LYS 71  NZ  
37  1 Y 1 B LYS 88  ? CG  ? A LYS 76  CG  
38  1 Y 1 B LYS 88  ? CD  ? A LYS 76  CD  
39  1 Y 1 B LYS 88  ? CE  ? A LYS 76  CE  
40  1 Y 1 B LYS 88  ? NZ  ? A LYS 76  NZ  
41  1 Y 1 B LYS 98  ? CG  ? A LYS 86  CG  
42  1 Y 1 B LYS 98  ? CD  ? A LYS 86  CD  
43  1 Y 1 B LYS 98  ? CE  ? A LYS 86  CE  
44  1 Y 1 B LYS 98  ? NZ  ? A LYS 86  NZ  
45  1 Y 1 B LYS 99  ? CG  ? A LYS 87  CG  
46  1 Y 1 B LYS 99  ? CD  ? A LYS 87  CD  
47  1 Y 1 B LYS 99  ? CE  ? A LYS 87  CE  
48  1 Y 1 B LYS 99  ? NZ  ? A LYS 87  NZ  
49  1 Y 1 B LYS 121 ? CG  ? A LYS 109 CG  
50  1 Y 1 B LYS 121 ? CD  ? A LYS 109 CD  
51  1 Y 1 B LYS 121 ? CE  ? A LYS 109 CE  
52  1 Y 1 B LYS 121 ? NZ  ? A LYS 109 NZ  
53  1 Y 1 B LYS 138 ? CG  ? A LYS 126 CG  
54  1 Y 1 B LYS 138 ? CD  ? A LYS 126 CD  
55  1 Y 1 B LYS 138 ? CE  ? A LYS 126 CE  
56  1 Y 1 B LYS 138 ? NZ  ? A LYS 126 NZ  
57  1 Y 1 B GLU 140 ? CG  ? A GLU 128 CG  
58  1 Y 1 B GLU 140 ? CD  ? A GLU 128 CD  
59  1 Y 1 B GLU 140 ? OE1 ? A GLU 128 OE1 
60  1 Y 1 B GLU 140 ? OE2 ? A GLU 128 OE2 
61  1 Y 1 A GLU 20  ? CG  ? B GLU 8   CG  
62  1 Y 1 A GLU 20  ? CD  ? B GLU 8   CD  
63  1 Y 1 A GLU 20  ? OE1 ? B GLU 8   OE1 
64  1 Y 1 A GLU 20  ? OE2 ? B GLU 8   OE2 
65  1 Y 1 A LYS 28  ? CD  ? B LYS 16  CD  
66  1 Y 1 A LYS 28  ? CE  ? B LYS 16  CE  
67  1 Y 1 A LYS 28  ? NZ  ? B LYS 16  NZ  
68  1 Y 1 A GLU 44  ? CG  ? B GLU 32  CG  
69  1 Y 1 A GLU 44  ? CD  ? B GLU 32  CD  
70  1 Y 1 A GLU 44  ? OE1 ? B GLU 32  OE1 
71  1 Y 1 A GLU 44  ? OE2 ? B GLU 32  OE2 
72  1 Y 1 A LYS 52  ? CG  ? B LYS 40  CG  
73  1 Y 1 A LYS 52  ? CD  ? B LYS 40  CD  
74  1 Y 1 A LYS 52  ? CE  ? B LYS 40  CE  
75  1 Y 1 A LYS 52  ? NZ  ? B LYS 40  NZ  
76  1 Y 1 A LYS 65  ? CG  ? B LYS 53  CG  
77  1 Y 1 A LYS 65  ? CD  ? B LYS 53  CD  
78  1 Y 1 A LYS 65  ? CE  ? B LYS 53  CE  
79  1 Y 1 A LYS 65  ? NZ  ? B LYS 53  NZ  
80  1 Y 1 A LYS 66  ? CG  ? B LYS 54  CG  
81  1 Y 1 A LYS 66  ? CD  ? B LYS 54  CD  
82  1 Y 1 A LYS 66  ? CE  ? B LYS 54  CE  
83  1 Y 1 A LYS 66  ? NZ  ? B LYS 54  NZ  
84  1 Y 1 A ASN 74  ? CG  ? B ASN 62  CG  
85  1 Y 1 A ASN 74  ? OD1 ? B ASN 62  OD1 
86  1 Y 1 A ASN 74  ? ND2 ? B ASN 62  ND2 
87  1 Y 1 A GLU 75  ? CG  ? B GLU 63  CG  
88  1 Y 1 A GLU 75  ? CD  ? B GLU 63  CD  
89  1 Y 1 A GLU 75  ? OE1 ? B GLU 63  OE1 
90  1 Y 1 A GLU 75  ? OE2 ? B GLU 63  OE2 
91  1 Y 1 A LYS 83  ? CG  ? B LYS 71  CG  
92  1 Y 1 A LYS 83  ? CD  ? B LYS 71  CD  
93  1 Y 1 A LYS 83  ? CE  ? B LYS 71  CE  
94  1 Y 1 A LYS 83  ? NZ  ? B LYS 71  NZ  
95  1 Y 1 A LYS 88  ? CG  ? B LYS 76  CG  
96  1 Y 1 A LYS 88  ? CD  ? B LYS 76  CD  
97  1 Y 1 A LYS 88  ? CE  ? B LYS 76  CE  
98  1 Y 1 A LYS 88  ? NZ  ? B LYS 76  NZ  
99  1 Y 1 A LYS 138 ? CG  ? B LYS 126 CG  
100 1 Y 1 A LYS 138 ? CD  ? B LYS 126 CD  
101 1 Y 1 A LYS 138 ? CE  ? B LYS 126 CE  
102 1 Y 1 A LYS 138 ? NZ  ? B LYS 126 NZ  
103 1 Y 1 A GLU 140 ? CG  ? B GLU 128 CG  
104 1 Y 1 A GLU 140 ? CD  ? B GLU 128 CD  
105 1 Y 1 A GLU 140 ? OE1 ? B GLU 128 OE1 
106 1 Y 1 A GLU 140 ? OE2 ? B GLU 128 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? '5.8.0430 (refmacat 0.4.82)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoXDS ? ? ? .                            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                            4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GQ9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.886 
_cell.length_a_esd                 ? 
_cell.length_b                     48.886 
_cell.length_b_esd                 ? 
_cell.length_c                     194.679 
_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                         9GQ9 
_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                   9GQ9 
_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             2.40 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.70 
_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                                       9GQ9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               48.67 
_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                                     19232 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          33.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.05 
_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                                0.034 
_reflns.pdbx_Rpim_I_all                                0.014 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.031 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
8.94 48.67 ? 85.8 ? ? ? ? 281  ? ? ? ? ? ? ? ? ? ? ? 8.4  0.78 ? ? 0.019 0.008 ? 1 ? 1.000 ? ? 98.9  ? 0.017 ? ? ? ? ? ? ? ? ? 
2.00 2.05  ? 4.9  ? ? ? ? 1412 ? ? ? ? ? ? ? ? ? ? ? 11.3 1.05 ? ? 0.539 0.220 ? 2 ? 0.932 ? ? 100.0 ? 0.492 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.343 
_refine.aniso_B[1][2]                            -0.172 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            -0.343 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            1.113 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               57.763 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.952 
_refine.correlation_coeff_Fo_to_Fc_free          0.916 
_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                                 9GQ9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.000 
_refine.ls_d_res_low                             41.404 
_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                     19153 
_refine.ls_number_reflns_R_free                  1011 
_refine.ls_number_reflns_R_work                  18142 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.849 
_refine.ls_percent_reflns_R_free                 5.279 
_refine.ls_R_factor_all                          0.241 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2799 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2386 
_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                       0.213 
_refine.pdbx_overall_ESU_R_Free                  0.188 
_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                             14.708 
_refine.overall_SU_ML                            0.187 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.000 
_refine_hist.d_res_low                        41.404 
_refine_hist.number_atoms_solvent             52 
_refine_hist.number_atoms_total               1969 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1847 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.012  1962 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.016  1798 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.787  1.849  2660 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.211  1.813  4180 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 8.200  5.000  250  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 5.484  5.000  5    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 12.530 10.000 291  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.331 10.000 69   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.080  0.200  295  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 1.816  0.200  30   ? r_chiral_restr_other           ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  2252 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  408  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.204  0.200  371  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.200  0.200  1691 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.180  0.200  1014 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.090  0.200  1008 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.154  0.200  65   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.157  0.200  4    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.166  0.200  16   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.103  0.200  2    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 2.496  2.642  1012 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.495  2.641  1012 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.551  4.738  1258 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.550  4.737  1259 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 2.520  2.737  950  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.519  2.737  951  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.643  4.967  1402 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.642  4.966  1403 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.794  24.193 2150 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.794  24.150 2145 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.107  0.050  3385 ? 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 ? ? 0.10713 ? 0.05009 1 'Local ncs' ? B ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.10713 ? 0.05009 2 'Local ncs' ? A ? ? ? 1 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.000 2.052  1407 . 79 1328 100.0000 . 0.338 . . 0.335 . . . . . 0.312 . 20 . 0.921 0.877 0.395 
'X-RAY DIFFRACTION' 2.052 2.108  1333 . 57 1276 100.0000 . 0.323 . . 0.322 . . . . . 0.292 . 20 . 0.925 0.924 0.343 
'X-RAY DIFFRACTION' 2.108 2.169  1302 . 72 1230 100.0000 . 0.313 . . 0.310 . . . . . 0.283 . 20 . 0.931 0.911 0.373 
'X-RAY DIFFRACTION' 2.169 2.235  1299 . 38 1252 99.3072  . 0.334 . . 0.333 . . . . . 0.294 . 20 . 0.931 0.925 0.364 
'X-RAY DIFFRACTION' 2.235 2.309  1216 . 83 1124 99.2599  . 0.331 . . 0.326 . . . . . 0.291 . 20 . 0.930 0.900 0.411 
'X-RAY DIFFRACTION' 2.309 2.389  1200 . 66 1134 100.0000 . 0.293 . . 0.288 . . . . . 0.259 . 20 . 0.948 0.918 0.371 
'X-RAY DIFFRACTION' 2.389 2.479  1172 . 75 1097 100.0000 . 0.283 . . 0.278 . . . . . 0.247 . 20 . 0.953 0.930 0.351 
'X-RAY DIFFRACTION' 2.479 2.580  1119 . 62 1057 100.0000 . 0.256 . . 0.257 . . . . . 0.232 . 20 . 0.958 0.966 0.239 
'X-RAY DIFFRACTION' 2.580 2.694  1081 . 37 1044 100.0000 . 0.267 . . 0.263 . . . . . 0.238 . 20 . 0.955 0.913 0.412 
'X-RAY DIFFRACTION' 2.694 2.825  1031 . 57 974  100.0000 . 0.311 . . 0.309 . . . . . 0.284 . 20 . 0.935 0.932 0.340 
'X-RAY DIFFRACTION' 2.825 2.977  965  . 56 909  100.0000 . 0.274 . . 0.273 . . . . . 0.262 . 20 . 0.949 0.955 0.278 
'X-RAY DIFFRACTION' 2.977 3.157  954  . 57 897  100.0000 . 0.260 . . 0.260 . . . . . 0.255 . 20 . 0.957 0.954 0.258 
'X-RAY DIFFRACTION' 3.157 3.373  881  . 68 813  100.0000 . 0.262 . . 0.263 . . . . . 0.261 . 20 . 0.959 0.960 0.249 
'X-RAY DIFFRACTION' 3.373 3.642  829  . 50 777  99.7587  . 0.248 . . 0.245 . . . . . 0.249 . 20 . 0.970 0.954 0.296 
'X-RAY DIFFRACTION' 3.642 3.986  769  . 28 739  99.7399  . 0.221 . . 0.221 . . . . . 0.229 . 20 . 0.976 0.970 0.222 
'X-RAY DIFFRACTION' 3.986 4.451  729  . 38 690  99.8628  . 0.168 . . 0.167 . . . . . 0.185 . 20 . 0.985 0.976 0.195 
'X-RAY DIFFRACTION' 4.451 5.130  604  . 30 574  100.0000 . 0.153 . . 0.151 . . . . . 0.176 . 20 . 0.986 0.978 0.183 
'X-RAY DIFFRACTION' 5.130 6.259  566  . 31 535  100.0000 . 0.219 . . 0.217 . . . . . 0.244 . 20 . 0.973 0.965 0.248 
'X-RAY DIFFRACTION' 6.259 8.752  437  . 12 425  100.0000 . 0.238 . . 0.238 . . . . . 0.280 . 20 . 0.965 0.955 0.258 
'X-RAY DIFFRACTION' 8.752 41.404 286  . 15 267  98.6014  . 0.244 . . 0.234 . . . . . 0.288 . 20 . 0.954 0.901 0.410 
# 
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                     9GQ9 
_struct.title                        'The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog p5(2,2)-(Z)' 
_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        9GQ9 
_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 9GQ9 B 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
2 1 9GQ9 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 9GQ9 GLY B 1  ? UNP Q13451 ?   ?   'expression tag'      13  1  
1 9GQ9 ALA B 2  ? UNP Q13451 ?   ?   'expression tag'      14  2  
1 9GQ9 PRO B 3  ? UNP Q13451 ?   ?   'expression tag'      15  3  
1 9GQ9 THR B 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  4  
1 9GQ9 ALA B 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 5  
1 9GQ9 ILE B 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 6  
2 9GQ9 GLY A 1  ? UNP Q13451 ?   ?   'expression tag'      13  7  
2 9GQ9 ALA A 2  ? UNP Q13451 ?   ?   'expression tag'      14  8  
2 9GQ9 PRO A 3  ? UNP Q13451 ?   ?   'expression tag'      15  9  
2 9GQ9 THR A 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  10 
2 9GQ9 ALA A 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 11 
2 9GQ9 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 -3.73 
2 LEU 107 B . ? LEU 119 A PRO 108 B ? PRO 120 A 1 -0.29 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ASP A 12  ? GLU B 23  ASP B 24  
AA1 2 VAL A 21  ? ARG A 27  ? VAL B 33  ARG B 39  
AA1 3 ILE A 90  ? ILE A 95  ? ILE B 102 ILE B 107 
AA1 4 LEU A 116 ? LYS A 126 ? LEU B 128 LYS B 138 
AA1 5 LYS A 40  ? LEU A 49  ? LYS B 52  LEU B 61  
AA1 6 PHE A 55  ? SER A 57  ? PHE B 67  SER B 69  
AA2 1 GLU A 11  ? ASP A 12  ? GLU B 23  ASP B 24  
AA2 2 VAL A 21  ? ARG A 27  ? VAL B 33  ARG B 39  
AA2 3 ILE A 90  ? ILE A 95  ? ILE B 102 ILE B 107 
AA2 4 LEU A 116 ? LYS A 126 ? LEU B 128 LYS B 138 
AA2 5 LYS A 40  ? LEU A 49  ? LYS B 52  LEU B 61  
AA2 6 PHE A 65  ? SER A 68  ? PHE B 77  SER B 80  
AA3 1 GLU B 11  ? ASP B 12  ? GLU A 23  ASP A 24  
AA3 2 VAL B 21  ? ARG B 27  ? VAL A 33  ARG A 39  
AA3 3 ILE B 90  ? ILE B 95  ? ILE A 102 ILE A 107 
AA3 4 LEU B 116 ? LYS B 126 ? LEU A 128 LYS A 138 
AA3 5 LYS B 40  ? LEU B 49  ? LYS A 52  LEU A 61  
AA3 6 PHE B 55  ? SER B 57  ? PHE A 67  SER A 69  
AA4 1 GLU B 11  ? ASP B 12  ? GLU A 23  ASP A 24  
AA4 2 VAL B 21  ? ARG B 27  ? VAL A 33  ARG A 39  
AA4 3 ILE B 90  ? ILE B 95  ? ILE A 102 ILE A 107 
AA4 4 LEU B 116 ? LYS B 126 ? LEU A 128 LYS A 138 
AA4 5 LYS B 40  ? LEU B 49  ? LYS A 52  LEU A 61  
AA4 6 PHE B 65  ? SER B 68  ? PHE A 77  SER A 80  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 11  ? N GLU B 23  O LYS A 23  ? O LYS B 35  
AA1 2 3 N ILE A 24  ? N ILE B 36  O HIS A 92  ? O HIS B 104 
AA1 3 4 N ALA A 91  ? N ALA B 103 O ILE A 120 ? O ILE B 132 
AA1 4 5 O GLU A 121 ? O GLU B 133 N HIS A 44  ? N HIS B 56  
AA1 5 6 N GLY A 47  ? N GLY B 59  O ASP A 56  ? O ASP B 68  
AA2 1 2 N GLU A 11  ? N GLU B 23  O LYS A 23  ? O LYS B 35  
AA2 2 3 N ILE A 24  ? N ILE B 36  O HIS A 92  ? O HIS B 104 
AA2 3 4 N ALA A 91  ? N ALA B 103 O ILE A 120 ? O ILE B 132 
AA2 4 5 O GLU A 121 ? O GLU B 133 N HIS A 44  ? N HIS B 56  
AA2 5 6 N VAL A 41  ? N VAL B 53  O PHE A 67  ? O PHE B 79  
AA3 1 2 N GLU B 11  ? N GLU A 23  O LYS B 23  ? O LYS A 35  
AA3 2 3 N ILE B 24  ? N ILE A 36  O HIS B 92  ? O HIS A 104 
AA3 3 4 N ALA B 91  ? N ALA A 103 O ILE B 120 ? O ILE A 132 
AA3 4 5 O GLU B 121 ? O GLU A 133 N HIS B 44  ? N HIS A 56  
AA3 5 6 N GLY B 47  ? N GLY A 59  O ASP B 56  ? O ASP A 68  
AA4 1 2 N GLU B 11  ? N GLU A 23  O LYS B 23  ? O LYS A 35  
AA4 2 3 N ILE B 24  ? N ILE A 36  O HIS B 92  ? O HIS A 104 
AA4 3 4 N ALA B 91  ? N ALA A 103 O ILE B 120 ? O ILE A 132 
AA4 4 5 O GLU B 121 ? O GLU A 133 N HIS B 44  ? N HIS A 56  
AA4 5 6 N VAL B 41  ? N VAL A 53  O PHE B 67  ? O PHE A 79  
# 
_pdbx_entry_details.entry_id                   9GQ9 
_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  ? ? 1.50 
2 1 OD2 A ASP 30 ? ? HH  A TYR 111 ? ? 1.58 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA B 112 ? ? -128.77 -104.98 
2 1 SER B 118 ? ? -150.86 70.73   
3 1 ASN A 74  ? ? 39.33   48.82   
4 1 ALA A 112 ? ? -134.68 -108.83 
5 1 SER A 118 ? ? -155.49 67.72   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     327 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 -18.3761 -0.4054 3.3818  0.2926 ? -0.1368 ? 0.0700  ? 0.1158 ? -0.1502 ? 0.3245 ? 6.3077 ? -1.7636 
? 0.9960  ? 6.4815 ? -0.1835 ? 6.0528 ? 0.0288  ? -0.3123 ? 0.2512 ? -0.5792 ? -0.0726 ? 0.9783  ? 0.3289  ? -0.1912 ? 0.0438 ? 
2 'X-RAY DIFFRACTION' ? refined -8.9148  16.0064 28.2978 0.1137 ? -0.0347 ? -0.0146 ? 0.1796 ? -0.1018 ? 0.1716 ? 5.2020 ? 0.3786  
? -0.2907 ? 3.6549 ? 0.8494  ? 6.6019 ? -0.3869 ? 0.3157  ? 0.3441 ? 0.0130  ? 0.0076  ? -0.2839 ? -0.2020 ? -0.1621 ? 0.3793 ? 
# 
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 
A1IN3 CAK  C N N 1   
A1IN3 CAL  C N N 2   
A1IN3 CAM  C N N 3   
A1IN3 CAN  C N N 4   
A1IN3 CAO  C N N 5   
A1IN3 CAJ  C N N 6   
A1IN3 CAI  C N S 7   
A1IN3 CAB  C N N 8   
A1IN3 OAA  O N N 9   
A1IN3 N    N N N 10  
A1IN3 CAH  C N N 11  
A1IN3 CAG  C N N 12  
A1IN3 CAF  C N N 13  
A1IN3 CB   C N N 14  
A1IN3 CA   C N S 15  
A1IN3 C    C N N 16  
A1IN3 O    O N N 17  
A1IN3 OBC  O N N 18  
A1IN3 CBB  C N N 19  
A1IN3 CBA  C N N 20  
A1IN3 CAZ  C N N 21  
A1IN3 CAY  C N N 22  
A1IN3 CAX  C N N 23  
A1IN3 CAW  C N N 24  
A1IN3 OAV  O N N 25  
A1IN3 CAU  C Y N 26  
A1IN3 CAR  C Y N 27  
A1IN3 OAS  O N N 28  
A1IN3 CAT  C N N 29  
A1IN3 CAQ  C Y N 30  
A1IN3 CAP  C Y N 31  
A1IN3 CBI  C Y N 32  
A1IN3 CBF  C Y N 33  
A1IN3 OBG  O N N 34  
A1IN3 CBH  C N N 35  
A1IN3 HAK  H N N 36  
A1IN3 HB6  H N N 37  
A1IN3 HAL  H N N 38  
A1IN3 HB7  H N N 39  
A1IN3 HAM  H N N 40  
A1IN3 HB8  H N N 41  
A1IN3 HAN  H N N 42  
A1IN3 HB9  H N N 43  
A1IN3 HCA  H N N 44  
A1IN3 HAO  H N N 45  
A1IN3 HAJ  H N N 46  
A1IN3 HAI  H N N 47  
A1IN3 HAH  H N N 48  
A1IN3 HB5  H N N 49  
A1IN3 HAG  H N N 50  
A1IN3 HB4  H N N 51  
A1IN3 HAF  H N N 52  
A1IN3 HB3  H N N 53  
A1IN3 HB2  H N N 54  
A1IN3 HB1  H N N 55  
A1IN3 HA   H N N 56  
A1IN3 HCG  H N N 57  
A1IN3 HBB  H N N 58  
A1IN3 HCF  H N N 59  
A1IN3 HBA  H N N 60  
A1IN3 HAZ  H N N 61  
A1IN3 HAY  H N N 62  
A1IN3 HCE  H N N 63  
A1IN3 HAX  H N N 64  
A1IN3 HCD  H N N 65  
A1IN3 HAW  H N N 66  
A1IN3 HCC  H N N 67  
A1IN3 HAT  H N N 68  
A1IN3 HCB  H N N 69  
A1IN3 HAQ  H N N 70  
A1IN3 HBI  H N N 71  
A1IN3 HCI  H N N 72  
A1IN3 HBH  H N N 73  
A1IN3 HCH  H N N 74  
ALA   N    N N N 75  
ALA   CA   C N S 76  
ALA   C    C N N 77  
ALA   O    O N N 78  
ALA   CB   C N N 79  
ALA   OXT  O N N 80  
ALA   H    H N N 81  
ALA   H2   H N N 82  
ALA   HA   H N N 83  
ALA   HB1  H N N 84  
ALA   HB2  H N N 85  
ALA   HB3  H N N 86  
ALA   HXT  H N N 87  
ARG   N    N N N 88  
ARG   CA   C N S 89  
ARG   C    C N N 90  
ARG   O    O N N 91  
ARG   CB   C N N 92  
ARG   CG   C N N 93  
ARG   CD   C N N 94  
ARG   NE   N N N 95  
ARG   CZ   C N N 96  
ARG   NH1  N N N 97  
ARG   NH2  N N N 98  
ARG   OXT  O N N 99  
ARG   H    H N N 100 
ARG   H2   H N N 101 
ARG   HA   H N N 102 
ARG   HB2  H N N 103 
ARG   HB3  H N N 104 
ARG   HG2  H N N 105 
ARG   HG3  H N N 106 
ARG   HD2  H N N 107 
ARG   HD3  H N N 108 
ARG   HE   H N N 109 
ARG   HH11 H N N 110 
ARG   HH12 H N N 111 
ARG   HH21 H N N 112 
ARG   HH22 H N N 113 
ARG   HXT  H N N 114 
ASN   N    N N N 115 
ASN   CA   C N S 116 
ASN   C    C N N 117 
ASN   O    O N N 118 
ASN   CB   C N N 119 
ASN   CG   C N N 120 
ASN   OD1  O N N 121 
ASN   ND2  N N N 122 
ASN   OXT  O N N 123 
ASN   H    H N N 124 
ASN   H2   H N N 125 
ASN   HA   H N N 126 
ASN   HB2  H N N 127 
ASN   HB3  H N N 128 
ASN   HD21 H N N 129 
ASN   HD22 H N N 130 
ASN   HXT  H N N 131 
ASP   N    N N N 132 
ASP   CA   C N S 133 
ASP   C    C N N 134 
ASP   O    O N N 135 
ASP   CB   C N N 136 
ASP   CG   C N N 137 
ASP   OD1  O N N 138 
ASP   OD2  O N N 139 
ASP   OXT  O N N 140 
ASP   H    H N N 141 
ASP   H2   H N N 142 
ASP   HA   H N N 143 
ASP   HB2  H N N 144 
ASP   HB3  H N N 145 
ASP   HD2  H N N 146 
ASP   HXT  H N N 147 
CYS   N    N N N 148 
CYS   CA   C N R 149 
CYS   C    C N N 150 
CYS   O    O N N 151 
CYS   CB   C N N 152 
CYS   SG   S N N 153 
CYS   OXT  O N N 154 
CYS   H    H N N 155 
CYS   H2   H N N 156 
CYS   HA   H N N 157 
CYS   HB2  H N N 158 
CYS   HB3  H N N 159 
CYS   HG   H N N 160 
CYS   HXT  H N N 161 
GLN   N    N N N 162 
GLN   CA   C N S 163 
GLN   C    C N N 164 
GLN   O    O N N 165 
GLN   CB   C N N 166 
GLN   CG   C N N 167 
GLN   CD   C N N 168 
GLN   OE1  O N N 169 
GLN   NE2  N N N 170 
GLN   OXT  O N N 171 
GLN   H    H N N 172 
GLN   H2   H N N 173 
GLN   HA   H N N 174 
GLN   HB2  H N N 175 
GLN   HB3  H N N 176 
GLN   HG2  H N N 177 
GLN   HG3  H N N 178 
GLN   HE21 H N N 179 
GLN   HE22 H N N 180 
GLN   HXT  H N N 181 
GLU   N    N N N 182 
GLU   CA   C N S 183 
GLU   C    C N N 184 
GLU   O    O N N 185 
GLU   CB   C N N 186 
GLU   CG   C N N 187 
GLU   CD   C N N 188 
GLU   OE1  O N N 189 
GLU   OE2  O N N 190 
GLU   OXT  O N N 191 
GLU   H    H N N 192 
GLU   H2   H N N 193 
GLU   HA   H N N 194 
GLU   HB2  H N N 195 
GLU   HB3  H N N 196 
GLU   HG2  H N N 197 
GLU   HG3  H N N 198 
GLU   HE2  H N N 199 
GLU   HXT  H N N 200 
GLY   N    N N N 201 
GLY   CA   C N N 202 
GLY   C    C N N 203 
GLY   O    O N N 204 
GLY   OXT  O N N 205 
GLY   H    H N N 206 
GLY   H2   H N N 207 
GLY   HA2  H N N 208 
GLY   HA3  H N N 209 
GLY   HXT  H N N 210 
HIS   N    N N N 211 
HIS   CA   C N S 212 
HIS   C    C N N 213 
HIS   O    O N N 214 
HIS   CB   C N N 215 
HIS   CG   C Y N 216 
HIS   ND1  N Y N 217 
HIS   CD2  C Y N 218 
HIS   CE1  C Y N 219 
HIS   NE2  N Y N 220 
HIS   OXT  O N N 221 
HIS   H    H N N 222 
HIS   H2   H N N 223 
HIS   HA   H N N 224 
HIS   HB2  H N N 225 
HIS   HB3  H N N 226 
HIS   HD1  H N N 227 
HIS   HD2  H N N 228 
HIS   HE1  H N N 229 
HIS   HE2  H N N 230 
HIS   HXT  H N N 231 
HOH   O    O N N 232 
HOH   H1   H N N 233 
HOH   H2   H N N 234 
ILE   N    N N N 235 
ILE   CA   C N S 236 
ILE   C    C N N 237 
ILE   O    O N N 238 
ILE   CB   C N S 239 
ILE   CG1  C N N 240 
ILE   CG2  C N N 241 
ILE   CD1  C N N 242 
ILE   OXT  O N N 243 
ILE   H    H N N 244 
ILE   H2   H N N 245 
ILE   HA   H N N 246 
ILE   HB   H N N 247 
ILE   HG12 H N N 248 
ILE   HG13 H N N 249 
ILE   HG21 H N N 250 
ILE   HG22 H N N 251 
ILE   HG23 H N N 252 
ILE   HD11 H N N 253 
ILE   HD12 H N N 254 
ILE   HD13 H N N 255 
ILE   HXT  H N N 256 
LEU   N    N N N 257 
LEU   CA   C N S 258 
LEU   C    C N N 259 
LEU   O    O N N 260 
LEU   CB   C N N 261 
LEU   CG   C N N 262 
LEU   CD1  C N N 263 
LEU   CD2  C N N 264 
LEU   OXT  O N N 265 
LEU   H    H N N 266 
LEU   H2   H N N 267 
LEU   HA   H N N 268 
LEU   HB2  H N N 269 
LEU   HB3  H N N 270 
LEU   HG   H N N 271 
LEU   HD11 H N N 272 
LEU   HD12 H N N 273 
LEU   HD13 H N N 274 
LEU   HD21 H N N 275 
LEU   HD22 H N N 276 
LEU   HD23 H N N 277 
LEU   HXT  H N N 278 
LYS   N    N N N 279 
LYS   CA   C N S 280 
LYS   C    C N N 281 
LYS   O    O N N 282 
LYS   CB   C N N 283 
LYS   CG   C N N 284 
LYS   CD   C N N 285 
LYS   CE   C N N 286 
LYS   NZ   N N N 287 
LYS   OXT  O N N 288 
LYS   H    H N N 289 
LYS   H2   H N N 290 
LYS   HA   H N N 291 
LYS   HB2  H N N 292 
LYS   HB3  H N N 293 
LYS   HG2  H N N 294 
LYS   HG3  H N N 295 
LYS   HD2  H N N 296 
LYS   HD3  H N N 297 
LYS   HE2  H N N 298 
LYS   HE3  H N N 299 
LYS   HZ1  H N N 300 
LYS   HZ2  H N N 301 
LYS   HZ3  H N N 302 
LYS   HXT  H N N 303 
MET   N    N N N 304 
MET   CA   C N S 305 
MET   C    C N N 306 
MET   O    O N N 307 
MET   CB   C N N 308 
MET   CG   C N N 309 
MET   SD   S N N 310 
MET   CE   C N N 311 
MET   OXT  O N N 312 
MET   H    H N N 313 
MET   H2   H N N 314 
MET   HA   H N N 315 
MET   HB2  H N N 316 
MET   HB3  H N N 317 
MET   HG2  H N N 318 
MET   HG3  H N N 319 
MET   HE1  H N N 320 
MET   HE2  H N N 321 
MET   HE3  H N N 322 
MET   HXT  H N N 323 
PHE   N    N N N 324 
PHE   CA   C N S 325 
PHE   C    C N N 326 
PHE   O    O N N 327 
PHE   CB   C N N 328 
PHE   CG   C Y N 329 
PHE   CD1  C Y N 330 
PHE   CD2  C Y N 331 
PHE   CE1  C Y N 332 
PHE   CE2  C Y N 333 
PHE   CZ   C Y N 334 
PHE   OXT  O N N 335 
PHE   H    H N N 336 
PHE   H2   H N N 337 
PHE   HA   H N N 338 
PHE   HB2  H N N 339 
PHE   HB3  H N N 340 
PHE   HD1  H N N 341 
PHE   HD2  H N N 342 
PHE   HE1  H N N 343 
PHE   HE2  H N N 344 
PHE   HZ   H N N 345 
PHE   HXT  H N N 346 
PRO   N    N N N 347 
PRO   CA   C N S 348 
PRO   C    C N N 349 
PRO   O    O N N 350 
PRO   CB   C N N 351 
PRO   CG   C N N 352 
PRO   CD   C N N 353 
PRO   OXT  O N N 354 
PRO   H    H N N 355 
PRO   HA   H N N 356 
PRO   HB2  H N N 357 
PRO   HB3  H N N 358 
PRO   HG2  H N N 359 
PRO   HG3  H N N 360 
PRO   HD2  H N N 361 
PRO   HD3  H N N 362 
PRO   HXT  H N N 363 
SER   N    N N N 364 
SER   CA   C N S 365 
SER   C    C N N 366 
SER   O    O N N 367 
SER   CB   C N N 368 
SER   OG   O N N 369 
SER   OXT  O N N 370 
SER   H    H N N 371 
SER   H2   H N N 372 
SER   HA   H N N 373 
SER   HB2  H N N 374 
SER   HB3  H N N 375 
SER   HG   H N N 376 
SER   HXT  H N N 377 
THR   N    N N N 378 
THR   CA   C N S 379 
THR   C    C N N 380 
THR   O    O N N 381 
THR   CB   C N R 382 
THR   OG1  O N N 383 
THR   CG2  C N N 384 
THR   OXT  O N N 385 
THR   H    H N N 386 
THR   H2   H N N 387 
THR   HA   H N N 388 
THR   HB   H N N 389 
THR   HG1  H N N 390 
THR   HG21 H N N 391 
THR   HG22 H N N 392 
THR   HG23 H N N 393 
THR   HXT  H N N 394 
TRP   N    N N N 395 
TRP   CA   C N S 396 
TRP   C    C N N 397 
TRP   O    O N N 398 
TRP   CB   C N N 399 
TRP   CG   C Y N 400 
TRP   CD1  C Y N 401 
TRP   CD2  C Y N 402 
TRP   NE1  N Y N 403 
TRP   CE2  C Y N 404 
TRP   CE3  C Y N 405 
TRP   CZ2  C Y N 406 
TRP   CZ3  C Y N 407 
TRP   CH2  C Y N 408 
TRP   OXT  O N N 409 
TRP   H    H N N 410 
TRP   H2   H N N 411 
TRP   HA   H N N 412 
TRP   HB2  H N N 413 
TRP   HB3  H N N 414 
TRP   HD1  H N N 415 
TRP   HE1  H N N 416 
TRP   HE3  H N N 417 
TRP   HZ2  H N N 418 
TRP   HZ3  H N N 419 
TRP   HH2  H N N 420 
TRP   HXT  H N N 421 
TYR   N    N N N 422 
TYR   CA   C N S 423 
TYR   C    C N N 424 
TYR   O    O N N 425 
TYR   CB   C N N 426 
TYR   CG   C Y N 427 
TYR   CD1  C Y N 428 
TYR   CD2  C Y N 429 
TYR   CE1  C Y N 430 
TYR   CE2  C Y N 431 
TYR   CZ   C Y N 432 
TYR   OH   O N N 433 
TYR   OXT  O N N 434 
TYR   H    H N N 435 
TYR   H2   H N N 436 
TYR   HA   H N N 437 
TYR   HB2  H N N 438 
TYR   HB3  H N N 439 
TYR   HD1  H N N 440 
TYR   HD2  H N N 441 
TYR   HE1  H N N 442 
TYR   HE2  H N N 443 
TYR   HH   H N N 444 
TYR   HXT  H N N 445 
VAL   N    N N N 446 
VAL   CA   C N S 447 
VAL   C    C N N 448 
VAL   O    O N N 449 
VAL   CB   C N N 450 
VAL   CG1  C N N 451 
VAL   CG2  C N N 452 
VAL   OXT  O N N 453 
VAL   H    H N N 454 
VAL   H2   H N N 455 
VAL   HA   H N N 456 
VAL   HB   H N N 457 
VAL   HG11 H N N 458 
VAL   HG12 H N N 459 
VAL   HG13 H N N 460 
VAL   HG21 H N N 461 
VAL   HG22 H N N 462 
VAL   HG23 H N N 463 
VAL   HXT  H N N 464 
# 
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 
A1IN3 CAW OAV  sing N N 1   
A1IN3 CAW CAX  sing N N 2   
A1IN3 OAV CAU  sing N N 3   
A1IN3 CAX CAY  sing N N 4   
A1IN3 CAY CAZ  doub N E 5   
A1IN3 OAS CAT  sing N N 6   
A1IN3 OAS CAR  sing N N 7   
A1IN3 CAU CAR  doub Y N 8   
A1IN3 CAU CBF  sing Y N 9   
A1IN3 OBG CBF  sing N N 10  
A1IN3 OBG CBH  sing N N 11  
A1IN3 CAZ CBA  sing N N 12  
A1IN3 CAR CAQ  sing Y N 13  
A1IN3 CBF CBI  doub Y N 14  
A1IN3 CBA CBB  sing N N 15  
A1IN3 CAQ CAP  doub Y N 16  
A1IN3 CBB OBC  sing N N 17  
A1IN3 CBI CAP  sing Y N 18  
A1IN3 CAP CAI  sing N N 19  
A1IN3 OBC C    sing N N 20  
A1IN3 CAK CAL  sing N N 21  
A1IN3 CAK CAJ  sing N N 22  
A1IN3 CAL CAM  sing N N 23  
A1IN3 CAI CAJ  sing N N 24  
A1IN3 CAI CAB  sing N N 25  
A1IN3 CAJ CAO  sing N N 26  
A1IN3 C   O    doub N N 27  
A1IN3 C   CA   sing N N 28  
A1IN3 CAH N    sing N N 29  
A1IN3 CAH CAG  sing N N 30  
A1IN3 CAB OAA  doub N N 31  
A1IN3 CAB N    sing N N 32  
A1IN3 N   CA   sing N N 33  
A1IN3 CAM CAN  sing N N 34  
A1IN3 CA  CB   sing N N 35  
A1IN3 CAG CAF  sing N N 36  
A1IN3 CAF CB   sing N N 37  
A1IN3 CAO CAN  sing N N 38  
A1IN3 CAK HAK  sing N N 39  
A1IN3 CAK HB6  sing N N 40  
A1IN3 CAL HAL  sing N N 41  
A1IN3 CAL HB7  sing N N 42  
A1IN3 CAM HAM  sing N N 43  
A1IN3 CAM HB8  sing N N 44  
A1IN3 CAN HAN  sing N N 45  
A1IN3 CAN HB9  sing N N 46  
A1IN3 CAO HCA  sing N N 47  
A1IN3 CAO HAO  sing N N 48  
A1IN3 CAJ HAJ  sing N N 49  
A1IN3 CAI HAI  sing N N 50  
A1IN3 CAH HAH  sing N N 51  
A1IN3 CAH HB5  sing N N 52  
A1IN3 CAG HAG  sing N N 53  
A1IN3 CAG HB4  sing N N 54  
A1IN3 CAF HAF  sing N N 55  
A1IN3 CAF HB3  sing N N 56  
A1IN3 CB  HB2  sing N N 57  
A1IN3 CB  HB1  sing N N 58  
A1IN3 CA  HA   sing N N 59  
A1IN3 CBB HCG  sing N N 60  
A1IN3 CBB HBB  sing N N 61  
A1IN3 CBA HCF  sing N N 62  
A1IN3 CBA HBA  sing N N 63  
A1IN3 CAZ HAZ  sing N N 64  
A1IN3 CAY HAY  sing N N 65  
A1IN3 CAX HCE  sing N N 66  
A1IN3 CAX HAX  sing N N 67  
A1IN3 CAW HCD  sing N N 68  
A1IN3 CAW HAW  sing N N 69  
A1IN3 CAT HCC  sing N N 70  
A1IN3 CAT HAT  sing N N 71  
A1IN3 CAT HCB  sing N N 72  
A1IN3 CAQ HAQ  sing N N 73  
A1IN3 CBI HBI  sing N N 74  
A1IN3 CBH HCI  sing N N 75  
A1IN3 CBH HBH  sing N N 76  
A1IN3 CBH HCH  sing N N 77  
ALA   N   CA   sing N N 78  
ALA   N   H    sing N N 79  
ALA   N   H2   sing N N 80  
ALA   CA  C    sing N N 81  
ALA   CA  CB   sing N N 82  
ALA   CA  HA   sing N N 83  
ALA   C   O    doub N N 84  
ALA   C   OXT  sing N N 85  
ALA   CB  HB1  sing N N 86  
ALA   CB  HB2  sing N N 87  
ALA   CB  HB3  sing N N 88  
ALA   OXT HXT  sing N N 89  
ARG   N   CA   sing N N 90  
ARG   N   H    sing N N 91  
ARG   N   H2   sing N N 92  
ARG   CA  C    sing N N 93  
ARG   CA  CB   sing N N 94  
ARG   CA  HA   sing N N 95  
ARG   C   O    doub N N 96  
ARG   C   OXT  sing N N 97  
ARG   CB  CG   sing N N 98  
ARG   CB  HB2  sing N N 99  
ARG   CB  HB3  sing N N 100 
ARG   CG  CD   sing N N 101 
ARG   CG  HG2  sing N N 102 
ARG   CG  HG3  sing N N 103 
ARG   CD  NE   sing N N 104 
ARG   CD  HD2  sing N N 105 
ARG   CD  HD3  sing N N 106 
ARG   NE  CZ   sing N N 107 
ARG   NE  HE   sing N N 108 
ARG   CZ  NH1  sing N N 109 
ARG   CZ  NH2  doub N N 110 
ARG   NH1 HH11 sing N N 111 
ARG   NH1 HH12 sing N N 112 
ARG   NH2 HH21 sing N N 113 
ARG   NH2 HH22 sing N N 114 
ARG   OXT HXT  sing N N 115 
ASN   N   CA   sing N N 116 
ASN   N   H    sing N N 117 
ASN   N   H2   sing N N 118 
ASN   CA  C    sing N N 119 
ASN   CA  CB   sing N N 120 
ASN   CA  HA   sing N N 121 
ASN   C   O    doub N N 122 
ASN   C   OXT  sing N N 123 
ASN   CB  CG   sing N N 124 
ASN   CB  HB2  sing N N 125 
ASN   CB  HB3  sing N N 126 
ASN   CG  OD1  doub N N 127 
ASN   CG  ND2  sing N N 128 
ASN   ND2 HD21 sing N N 129 
ASN   ND2 HD22 sing N N 130 
ASN   OXT HXT  sing N N 131 
ASP   N   CA   sing N N 132 
ASP   N   H    sing N N 133 
ASP   N   H2   sing N N 134 
ASP   CA  C    sing N N 135 
ASP   CA  CB   sing N N 136 
ASP   CA  HA   sing N N 137 
ASP   C   O    doub N N 138 
ASP   C   OXT  sing N N 139 
ASP   CB  CG   sing N N 140 
ASP   CB  HB2  sing N N 141 
ASP   CB  HB3  sing N N 142 
ASP   CG  OD1  doub N N 143 
ASP   CG  OD2  sing N N 144 
ASP   OD2 HD2  sing N N 145 
ASP   OXT HXT  sing N N 146 
CYS   N   CA   sing N N 147 
CYS   N   H    sing N N 148 
CYS   N   H2   sing N N 149 
CYS   CA  C    sing N N 150 
CYS   CA  CB   sing N N 151 
CYS   CA  HA   sing N N 152 
CYS   C   O    doub N N 153 
CYS   C   OXT  sing N N 154 
CYS   CB  SG   sing N N 155 
CYS   CB  HB2  sing N N 156 
CYS   CB  HB3  sing N N 157 
CYS   SG  HG   sing N N 158 
CYS   OXT HXT  sing N N 159 
GLN   N   CA   sing N N 160 
GLN   N   H    sing N N 161 
GLN   N   H2   sing N N 162 
GLN   CA  C    sing N N 163 
GLN   CA  CB   sing N N 164 
GLN   CA  HA   sing N N 165 
GLN   C   O    doub N N 166 
GLN   C   OXT  sing N N 167 
GLN   CB  CG   sing N N 168 
GLN   CB  HB2  sing N N 169 
GLN   CB  HB3  sing N N 170 
GLN   CG  CD   sing N N 171 
GLN   CG  HG2  sing N N 172 
GLN   CG  HG3  sing N N 173 
GLN   CD  OE1  doub N N 174 
GLN   CD  NE2  sing N N 175 
GLN   NE2 HE21 sing N N 176 
GLN   NE2 HE22 sing N N 177 
GLN   OXT HXT  sing N N 178 
GLU   N   CA   sing N N 179 
GLU   N   H    sing N N 180 
GLU   N   H2   sing N N 181 
GLU   CA  C    sing N N 182 
GLU   CA  CB   sing N N 183 
GLU   CA  HA   sing N N 184 
GLU   C   O    doub N N 185 
GLU   C   OXT  sing N N 186 
GLU   CB  CG   sing N N 187 
GLU   CB  HB2  sing N N 188 
GLU   CB  HB3  sing N N 189 
GLU   CG  CD   sing N N 190 
GLU   CG  HG2  sing N N 191 
GLU   CG  HG3  sing N N 192 
GLU   CD  OE1  doub N N 193 
GLU   CD  OE2  sing N N 194 
GLU   OE2 HE2  sing N N 195 
GLU   OXT HXT  sing N N 196 
GLY   N   CA   sing N N 197 
GLY   N   H    sing N N 198 
GLY   N   H2   sing N N 199 
GLY   CA  C    sing N N 200 
GLY   CA  HA2  sing N N 201 
GLY   CA  HA3  sing N N 202 
GLY   C   O    doub N N 203 
GLY   C   OXT  sing N N 204 
GLY   OXT HXT  sing N N 205 
HIS   N   CA   sing N N 206 
HIS   N   H    sing N N 207 
HIS   N   H2   sing N N 208 
HIS   CA  C    sing N N 209 
HIS   CA  CB   sing N N 210 
HIS   CA  HA   sing N N 211 
HIS   C   O    doub N N 212 
HIS   C   OXT  sing N N 213 
HIS   CB  CG   sing N N 214 
HIS   CB  HB2  sing N N 215 
HIS   CB  HB3  sing N N 216 
HIS   CG  ND1  sing Y N 217 
HIS   CG  CD2  doub Y N 218 
HIS   ND1 CE1  doub Y N 219 
HIS   ND1 HD1  sing N N 220 
HIS   CD2 NE2  sing Y N 221 
HIS   CD2 HD2  sing N N 222 
HIS   CE1 NE2  sing Y N 223 
HIS   CE1 HE1  sing N N 224 
HIS   NE2 HE2  sing N N 225 
HIS   OXT HXT  sing N N 226 
HOH   O   H1   sing N N 227 
HOH   O   H2   sing N N 228 
ILE   N   CA   sing N N 229 
ILE   N   H    sing N N 230 
ILE   N   H2   sing N N 231 
ILE   CA  C    sing N N 232 
ILE   CA  CB   sing N N 233 
ILE   CA  HA   sing N N 234 
ILE   C   O    doub N N 235 
ILE   C   OXT  sing N N 236 
ILE   CB  CG1  sing N N 237 
ILE   CB  CG2  sing N N 238 
ILE   CB  HB   sing N N 239 
ILE   CG1 CD1  sing N N 240 
ILE   CG1 HG12 sing N N 241 
ILE   CG1 HG13 sing N N 242 
ILE   CG2 HG21 sing N N 243 
ILE   CG2 HG22 sing N N 244 
ILE   CG2 HG23 sing N N 245 
ILE   CD1 HD11 sing N N 246 
ILE   CD1 HD12 sing N N 247 
ILE   CD1 HD13 sing N N 248 
ILE   OXT HXT  sing N N 249 
LEU   N   CA   sing N N 250 
LEU   N   H    sing N N 251 
LEU   N   H2   sing N N 252 
LEU   CA  C    sing N N 253 
LEU   CA  CB   sing N N 254 
LEU   CA  HA   sing N N 255 
LEU   C   O    doub N N 256 
LEU   C   OXT  sing N N 257 
LEU   CB  CG   sing N N 258 
LEU   CB  HB2  sing N N 259 
LEU   CB  HB3  sing N N 260 
LEU   CG  CD1  sing N N 261 
LEU   CG  CD2  sing N N 262 
LEU   CG  HG   sing N N 263 
LEU   CD1 HD11 sing N N 264 
LEU   CD1 HD12 sing N N 265 
LEU   CD1 HD13 sing N N 266 
LEU   CD2 HD21 sing N N 267 
LEU   CD2 HD22 sing N N 268 
LEU   CD2 HD23 sing N N 269 
LEU   OXT HXT  sing N N 270 
LYS   N   CA   sing N N 271 
LYS   N   H    sing N N 272 
LYS   N   H2   sing N N 273 
LYS   CA  C    sing N N 274 
LYS   CA  CB   sing N N 275 
LYS   CA  HA   sing N N 276 
LYS   C   O    doub N N 277 
LYS   C   OXT  sing N N 278 
LYS   CB  CG   sing N N 279 
LYS   CB  HB2  sing N N 280 
LYS   CB  HB3  sing N N 281 
LYS   CG  CD   sing N N 282 
LYS   CG  HG2  sing N N 283 
LYS   CG  HG3  sing N N 284 
LYS   CD  CE   sing N N 285 
LYS   CD  HD2  sing N N 286 
LYS   CD  HD3  sing N N 287 
LYS   CE  NZ   sing N N 288 
LYS   CE  HE2  sing N N 289 
LYS   CE  HE3  sing N N 290 
LYS   NZ  HZ1  sing N N 291 
LYS   NZ  HZ2  sing N N 292 
LYS   NZ  HZ3  sing N N 293 
LYS   OXT HXT  sing N N 294 
MET   N   CA   sing N N 295 
MET   N   H    sing N N 296 
MET   N   H2   sing N N 297 
MET   CA  C    sing N N 298 
MET   CA  CB   sing N N 299 
MET   CA  HA   sing N N 300 
MET   C   O    doub N N 301 
MET   C   OXT  sing N N 302 
MET   CB  CG   sing N N 303 
MET   CB  HB2  sing N N 304 
MET   CB  HB3  sing N N 305 
MET   CG  SD   sing N N 306 
MET   CG  HG2  sing N N 307 
MET   CG  HG3  sing N N 308 
MET   SD  CE   sing N N 309 
MET   CE  HE1  sing N N 310 
MET   CE  HE2  sing N N 311 
MET   CE  HE3  sing N N 312 
MET   OXT HXT  sing N N 313 
PHE   N   CA   sing N N 314 
PHE   N   H    sing N N 315 
PHE   N   H2   sing N N 316 
PHE   CA  C    sing N N 317 
PHE   CA  CB   sing N N 318 
PHE   CA  HA   sing N N 319 
PHE   C   O    doub N N 320 
PHE   C   OXT  sing N N 321 
PHE   CB  CG   sing N N 322 
PHE   CB  HB2  sing N N 323 
PHE   CB  HB3  sing N N 324 
PHE   CG  CD1  doub Y N 325 
PHE   CG  CD2  sing Y N 326 
PHE   CD1 CE1  sing Y N 327 
PHE   CD1 HD1  sing N N 328 
PHE   CD2 CE2  doub Y N 329 
PHE   CD2 HD2  sing N N 330 
PHE   CE1 CZ   doub Y N 331 
PHE   CE1 HE1  sing N N 332 
PHE   CE2 CZ   sing Y N 333 
PHE   CE2 HE2  sing N N 334 
PHE   CZ  HZ   sing N N 335 
PHE   OXT HXT  sing N N 336 
PRO   N   CA   sing N N 337 
PRO   N   CD   sing N N 338 
PRO   N   H    sing N N 339 
PRO   CA  C    sing N N 340 
PRO   CA  CB   sing N N 341 
PRO   CA  HA   sing N N 342 
PRO   C   O    doub N N 343 
PRO   C   OXT  sing N N 344 
PRO   CB  CG   sing N N 345 
PRO   CB  HB2  sing N N 346 
PRO   CB  HB3  sing N N 347 
PRO   CG  CD   sing N N 348 
PRO   CG  HG2  sing N N 349 
PRO   CG  HG3  sing N N 350 
PRO   CD  HD2  sing N N 351 
PRO   CD  HD3  sing N N 352 
PRO   OXT HXT  sing N N 353 
SER   N   CA   sing N N 354 
SER   N   H    sing N N 355 
SER   N   H2   sing N N 356 
SER   CA  C    sing N N 357 
SER   CA  CB   sing N N 358 
SER   CA  HA   sing N N 359 
SER   C   O    doub N N 360 
SER   C   OXT  sing N N 361 
SER   CB  OG   sing N N 362 
SER   CB  HB2  sing N N 363 
SER   CB  HB3  sing N N 364 
SER   OG  HG   sing N N 365 
SER   OXT HXT  sing N N 366 
THR   N   CA   sing N N 367 
THR   N   H    sing N N 368 
THR   N   H2   sing N N 369 
THR   CA  C    sing N N 370 
THR   CA  CB   sing N N 371 
THR   CA  HA   sing N N 372 
THR   C   O    doub N N 373 
THR   C   OXT  sing N N 374 
THR   CB  OG1  sing N N 375 
THR   CB  CG2  sing N N 376 
THR   CB  HB   sing N N 377 
THR   OG1 HG1  sing N N 378 
THR   CG2 HG21 sing N N 379 
THR   CG2 HG22 sing N N 380 
THR   CG2 HG23 sing N N 381 
THR   OXT HXT  sing N N 382 
TRP   N   CA   sing N N 383 
TRP   N   H    sing N N 384 
TRP   N   H2   sing N N 385 
TRP   CA  C    sing N N 386 
TRP   CA  CB   sing N N 387 
TRP   CA  HA   sing N N 388 
TRP   C   O    doub N N 389 
TRP   C   OXT  sing N N 390 
TRP   CB  CG   sing N N 391 
TRP   CB  HB2  sing N N 392 
TRP   CB  HB3  sing N N 393 
TRP   CG  CD1  doub Y N 394 
TRP   CG  CD2  sing Y N 395 
TRP   CD1 NE1  sing Y N 396 
TRP   CD1 HD1  sing N N 397 
TRP   CD2 CE2  doub Y N 398 
TRP   CD2 CE3  sing Y N 399 
TRP   NE1 CE2  sing Y N 400 
TRP   NE1 HE1  sing N N 401 
TRP   CE2 CZ2  sing Y N 402 
TRP   CE3 CZ3  doub Y N 403 
TRP   CE3 HE3  sing N N 404 
TRP   CZ2 CH2  doub Y N 405 
TRP   CZ2 HZ2  sing N N 406 
TRP   CZ3 CH2  sing Y N 407 
TRP   CZ3 HZ3  sing N N 408 
TRP   CH2 HH2  sing N N 409 
TRP   OXT HXT  sing N N 410 
TYR   N   CA   sing N N 411 
TYR   N   H    sing N N 412 
TYR   N   H2   sing N N 413 
TYR   CA  C    sing N N 414 
TYR   CA  CB   sing N N 415 
TYR   CA  HA   sing N N 416 
TYR   C   O    doub N N 417 
TYR   C   OXT  sing N N 418 
TYR   CB  CG   sing N N 419 
TYR   CB  HB2  sing N N 420 
TYR   CB  HB3  sing N N 421 
TYR   CG  CD1  doub Y N 422 
TYR   CG  CD2  sing Y N 423 
TYR   CD1 CE1  sing Y N 424 
TYR   CD1 HD1  sing N N 425 
TYR   CD2 CE2  doub Y N 426 
TYR   CD2 HD2  sing N N 427 
TYR   CE1 CZ   doub Y N 428 
TYR   CE1 HE1  sing N N 429 
TYR   CE2 CZ   sing Y N 430 
TYR   CE2 HE2  sing N N 431 
TYR   CZ  OH   sing N N 432 
TYR   OH  HH   sing N N 433 
TYR   OXT HXT  sing N N 434 
VAL   N   CA   sing N N 435 
VAL   N   H    sing N N 436 
VAL   N   H2   sing N N 437 
VAL   CA  C    sing N N 438 
VAL   CA  CB   sing N N 439 
VAL   CA  HA   sing N N 440 
VAL   C   O    doub N N 441 
VAL   C   OXT  sing N N 442 
VAL   CB  CG1  sing N N 443 
VAL   CB  CG2  sing N N 444 
VAL   CB  HB   sing N N 445 
VAL   CG1 HG11 sing N N 446 
VAL   CG1 HG12 sing N N 447 
VAL   CG1 HG13 sing N N 448 
VAL   CG2 HG21 sing N N 449 
VAL   CG2 HG22 sing N N 450 
VAL   CG2 HG23 sing N N 451 
VAL   OXT HXT  sing N N 452 
# 
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                    9GQ9 
_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]   0.020456 
_atom_sites.fract_transf_matrix[1][2]   0.011810 
_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]   0.023620 
_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]   0.005137 
_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   ? -15.704 -15.34  -5.775  1   77.85   ? 13  GLY   B N    1 ? 1 
ATOM   2    C CA   . GLY   A 1 1   ? -17.046 -14.743 -5.89   1   77.747  ? 13  GLY   B CA   1 ? 1 
ATOM   3    C C    . GLY   A 1 1   ? -16.972 -13.239 -5.702  1   74.077  ? 13  GLY   B C    1 ? 1 
ATOM   4    O O    . GLY   A 1 1   ? -16.057 -12.583 -6.195  1   70.312  ? 13  GLY   B O    1 ? 1 
ATOM   5    H H1   . GLY   A 1 1   ? -15.758 -16.239 -5.864  1   80.914  ? 13  GLY   B H1   1 c 1 
ATOM   6    H H2   . GLY   A 1 1   ? -15.346 -15.146 -4.967  1   75.34   ? 13  GLY   B H2   1 c 1 
ATOM   7    H H3   . GLY   A 1 1   ? -15.163 -15.013 -6.422  1   78.021  ? 13  GLY   B H3   1 c 1 
ATOM   8    H HA2  . GLY   A 1 1   ? -17.419 -14.95  -6.779  1   81.001  ? 13  GLY   B HA2  1 c 1 
ATOM   9    H HA3  . GLY   A 1 1   ? -17.637 -15.139 -5.207  1   78.349  ? 13  GLY   B HA3  1 c 1 
ATOM   10   N N    . ALA   A 1 2   ? -17.91  -12.721 -4.913  1   74.253  ? 14  ALA   B N    1 ? 1 
ATOM   11   C CA   . ALA   A 1 2   ? -18.183 -11.298 -4.853  1   69.032  ? 14  ALA   B CA   1 ? 1 
ATOM   12   C C    . ALA   A 1 2   ? -16.927 -10.465 -4.565  1   66.552  ? 14  ALA   B C    1 ? 1 
ATOM   13   O O    . ALA   A 1 2   ? -16.737 -9.417  -5.21   1   64.189  ? 14  ALA   B O    1 ? 1 
ATOM   14   C CB   . ALA   A 1 2   ? -19.271 -11.061 -3.837  1   68.506  ? 14  ALA   B CB   1 ? 1 
ATOM   15   H H    . ALA   A 1 2   ? -18.399 -13.28  -4.381  1   74.295  ? 14  ALA   B H    1 c 1 
ATOM   16   H HA   . ALA   A 1 2   ? -18.525 -11.022 -5.748  1   71.384  ? 14  ALA   B HA   1 c 1 
ATOM   17   H HB1  . ALA   A 1 2   ? -20.101 -11.457 -4.15   1   71.109  ? 14  ALA   B HB1  1 c 1 
ATOM   18   H HB2  . ALA   A 1 2   ? -19.025 -11.465 -2.989  1   67.569  ? 14  ALA   B HB2  1 c 1 
ATOM   19   H HB3  . ALA   A 1 2   ? -19.399 -10.106 -3.712  1   66.314  ? 14  ALA   B HB3  1 c 1 
ATOM   20   N N    . PRO   A 1 3   ? -16.062 -10.855 -3.59   1   63.298  ? 15  PRO   B N    1 ? 1 
ATOM   21   C CA   . PRO   A 1 3   ? -14.832 -10.117 -3.298  1   64.854  ? 15  PRO   B CA   1 ? 1 
ATOM   22   C C    . PRO   A 1 3   ? -13.802 -10.126 -4.431  1   64.8    ? 15  PRO   B C    1 ? 1 
ATOM   23   O O    . PRO   A 1 3   ? -13.16  -9.102  -4.712  1   59.53   ? 15  PRO   B O    1 ? 1 
ATOM   24   C CB   . PRO   A 1 3   ? -14.24  -10.776 -2.043  1   62.877  ? 15  PRO   B CB   1 ? 1 
ATOM   25   C CG   . PRO   A 1 3   ? -15.39  -11.602 -1.507  1   66.002  ? 15  PRO   B CG   1 ? 1 
ATOM   26   C CD   . PRO   A 1 3   ? -16.233 -11.999 -2.689  1   67.657  ? 15  PRO   B CD   1 ? 1 
ATOM   27   H HA   . PRO   A 1 3   ? -15.063 -9.189  -3.087  1   61.551  ? 15  PRO   B HA   1 c 1 
ATOM   28   H HB2  . PRO   A 1 3   ? -13.477 -11.343 -2.27   1   64.64   ? 15  PRO   B HB2  1 c 1 
ATOM   29   H HB3  . PRO   A 1 3   ? -13.958 -10.103 -1.394  1   61.089  ? 15  PRO   B HB3  1 c 1 
ATOM   30   H HG2  . PRO   A 1 3   ? -15.055 -12.399 -1.049  1   66.306  ? 15  PRO   B HG2  1 c 1 
ATOM   31   H HG3  . PRO   A 1 3   ? -15.92  -11.08  -0.872  1   63.772  ? 15  PRO   B HG3  1 c 1 
ATOM   32   H HD2  . PRO   A 1 3   ? -15.905 -12.821 -3.101  1   69.586  ? 15  PRO   B HD2  1 c 1 
ATOM   33   H HD3  . PRO   A 1 3   ? -17.166 -12.112 -2.434  1   67.987  ? 15  PRO   B HD3  1 c 1 
ATOM   34   N N    . ALA   A 1 4   ? -13.633 -11.288 -5.053  1   64.733  ? 16  ALA   B N    1 ? 1 
ATOM   35   C CA   . ALA   A 1 4   ? -12.745 -11.413 -6.197  1   68.494  ? 16  ALA   B CA   1 ? 1 
ATOM   36   C C    . ALA   A 1 4   ? -13.202 -10.53  -7.366  1   70.487  ? 16  ALA   B C    1 ? 1 
ATOM   37   O O    . ALA   A 1 4   ? -12.368 -9.904  -8.018  1   68.242  ? 16  ALA   B O    1 ? 1 
ATOM   38   C CB   . ALA   A 1 4   ? -12.658 -12.861 -6.599  1   71.547  ? 16  ALA   B CB   1 ? 1 
ATOM   39   H H    . ALA   A 1 4   ? -14.078 -12.03  -4.756  1   67.022  ? 16  ALA   B H    1 c 1 
ATOM   40   H HA   . ALA   A 1 4   ? -11.839 -11.105 -5.916  1   66.925  ? 16  ALA   B HA   1 c 1 
ATOM   41   H HB1  . ALA   A 1 4   ? -12.35  -13.392 -5.846  1   71.401  ? 16  ALA   B HB1  1 c 1 
ATOM   42   H HB2  . ALA   A 1 4   ? -13.534 -13.177 -6.877  1   73.543  ? 16  ALA   B HB2  1 c 1 
ATOM   43   H HB3  . ALA   A 1 4   ? -12.033 -12.959 -7.337  1   73.945  ? 16  ALA   B HB3  1 c 1 
ATOM   44   N N    . THR   A 1 5   ? -14.52  -10.489 -7.631  1   69.991  ? 17  THR   B N    1 ? 1 
ATOM   45   C CA   . THR   A 1 5   ? -15.09  -9.592  -8.633  1   67.535  ? 17  THR   B CA   1 ? 1 
ATOM   46   C C    . THR   A 1 5   ? -14.725 -8.146  -8.291  1   61.333  ? 17  THR   B C    1 ? 1 
ATOM   47   O O    . THR   A 1 5   ? -14.58  -7.327  -9.193  1   58.5    ? 17  THR   B O    1 ? 1 
ATOM   48   C CB   . THR   A 1 5   ? -16.609 -9.78   -8.775  1   68.516  ? 17  THR   B CB   1 ? 1 
ATOM   49   O OG1  . THR   A 1 5   ? -16.847 -11.045 -9.392  1   71.724  ? 17  THR   B OG1  1 ? 1 
ATOM   50   C CG2  . THR   A 1 5   ? -17.28  -8.739  -9.666  1   68.656  ? 17  THR   B CG2  1 ? 1 
ATOM   51   H H    . THR   A 1 5   ? -15.082 -11.045 -7.173  1   69.682  ? 17  THR   B H    1 c 1 
ATOM   52   H HA   . THR   A 1 5   ? -14.678 -9.812  -9.497  1   70.281  ? 17  THR   B HA   1 c 1 
ATOM   53   H HB   . THR   A 1 5   ? -17.031 -9.767  -7.883  1   66.117  ? 17  THR   B HB   1 c 1 
ATOM   54   H HG1  . THR   A 1 5   ? -16.233 -11.172 -10.217 0   30      ? 17  THR   B HG1  1 c 1 
ATOM   55   H HG21 . THR   A 1 5   ? -18.168 -9.048  -9.913  1   71.114  ? 17  THR   B HG21 1 c 1 
ATOM   56   H HG22 . THR   A 1 5   ? -16.749 -8.608  -10.469 1   70.755  ? 17  THR   B HG22 1 c 1 
ATOM   57   H HG23 . THR   A 1 5   ? -17.354 -7.899  -9.185  1   66.238  ? 17  THR   B HG23 1 c 1 
ATOM   58   N N    . VAL   A 1 6   ? -14.561 -7.832  -7      1   57.288  ? 18  VAL   B N    1 ? 1 
ATOM   59   C CA   . VAL   A 1 6   ? -14.279 -6.463  -6.608  1   56.553  ? 18  VAL   B CA   1 ? 1 
ATOM   60   C C    . VAL   A 1 6   ? -12.804 -6.152  -6.845  1   56.287  ? 18  VAL   B C    1 ? 1 
ATOM   61   O O    . VAL   A 1 6   ? -12.51  -5.101  -7.41   1   53.239  ? 18  VAL   B O    1 ? 1 
ATOM   62   C CB   . VAL   A 1 6   ? -14.734 -6.098  -5.191  1   51.956  ? 18  VAL   B CB   1 ? 1 
ATOM   63   C CG1  . VAL   A 1 6   ? -14.319 -4.681  -4.825  1   52.299  ? 18  VAL   B CG1  1 ? 1 
ATOM   64   C CG2  . VAL   A 1 6   ? -16.241 -6.255  -5.063  1   50.925  ? 18  VAL   B CG2  1 ? 1 
ATOM   65   H H    . VAL   A 1 6   ? -14.652 -8.47   -6.354  1   57.396  ? 18  VAL   B H    1 c 1 
ATOM   66   H HA   . VAL   A 1 6   ? -14.785 -5.89   -7.213  1   56.755  ? 18  VAL   B HA   1 c 1 
ATOM   67   H HB   . VAL   A 1 6   ? -14.298 -6.724  -4.567  1   51.641  ? 18  VAL   B HB   1 c 1 
ATOM   68   H HG11 . VAL   A 1 6   ? -14.592 -4.07   -5.53   1   52.561  ? 18  VAL   B HG11 1 c 1 
ATOM   69   H HG12 . VAL   A 1 6   ? -13.354 -4.64   -4.717  1   51.098  ? 18  VAL   B HG12 1 c 1 
ATOM   70   H HG13 . VAL   A 1 6   ? -14.747 -4.423  -3.991  1   49.812  ? 18  VAL   B HG13 1 c 1 
ATOM   71   H HG21 . VAL   A 1 6   ? -16.503 -6.131  -4.135  1   49.705  ? 18  VAL   B HG21 1 c 1 
ATOM   72   H HG22 . VAL   A 1 6   ? -16.503 -7.141  -5.356  1   53.408  ? 18  VAL   B HG22 1 c 1 
ATOM   73   H HG23 . VAL   A 1 6   ? -16.685 -5.589  -5.615  1   52.149  ? 18  VAL   B HG23 1 c 1 
ATOM   74   N N    . THR   A 1 7   ? -11.898 -7.059  -6.443  1   55.071  ? 19  THR   B N    1 ? 1 
ATOM   75   C CA   . THR   A 1 7   ? -10.507 -7.011  -6.881  1   58.809  ? 19  THR   B CA   1 ? 1 
ATOM   76   C C    . THR   A 1 7   ? -10.441 -6.788  -8.398  1   61.818  ? 19  THR   B C    1 ? 1 
ATOM   77   O O    . THR   A 1 7   ? -9.71   -5.923  -8.844  1   65.647  ? 19  THR   B O    1 ? 1 
ATOM   78   C CB   . THR   A 1 7   ? -9.783  -8.299  -6.497  1   61.734  ? 19  THR   B CB   1 ? 1 
ATOM   79   O OG1  . THR   A 1 7   ? -9.755  -8.264  -5.073  1   57.146  ? 19  THR   B OG1  1 ? 1 
ATOM   80   C CG2  . THR   A 1 7   ? -8.434  -8.47   -7.19   1   64.742  ? 19  THR   B CG2  1 ? 1 
ATOM   81   H H    . THR   A 1 7   ? -12.156 -7.725  -5.872  1   55.415  ? 19  THR   B H    1 c 1 
ATOM   82   H HA   . THR   A 1 7   ? -10.067 -6.257  -6.431  1   56.839  ? 19  THR   B HA   1 c 1 
ATOM   83   H HB   . THR   A 1 7   ? -10.345 -9.061  -6.775  1   62.695  ? 19  THR   B HB   1 c 1 
ATOM   84   H HG1  . THR   A 1 7   ? -9.229  -7.452  -4.848  0   30      ? 19  THR   B HG1  1 c 1 
ATOM   85   H HG21 . THR   A 1 7   ? -7.944  -9.197  -6.769  1   65.168  ? 19  THR   B HG21 1 c 1 
ATOM   86   H HG22 . THR   A 1 7   ? -7.922  -7.648  -7.112  1   63.904  ? 19  THR   B HG22 1 c 1 
ATOM   87   H HG23 . THR   A 1 7   ? -8.573  -8.678  -8.129  1   67.423  ? 19  THR   B HG23 1 c 1 
ATOM   88   N N    . GLU   A 1 8   ? -11.27  -7.492  -9.17   1   64.713  ? 20  GLU   B N    1 ? 1 
ATOM   89   C CA   . GLU   A 1 8   ? -11.131 -7.522  -10.619 1   70.537  ? 20  GLU   B CA   1 ? 1 
ATOM   90   C C    . GLU   A 1 8   ? -11.692 -6.259  -11.275 1   70.752  ? 20  GLU   B C    1 ? 1 
ATOM   91   O O    . GLU   A 1 8   ? -11.068 -5.722  -12.181 1   71.248  ? 20  GLU   B O    1 ? 1 
ATOM   92   C CB   . GLU   A 1 8   ? -11.854 -8.741  -11.194 1   75.439  ? 20  GLU   B CB   1 ? 1 
ATOM   93   C CG   . GLU   A 1 8   ? -11.344 -10.071 -10.656 1   76.419  ? 20  GLU   B CG   1 ? 1 
ATOM   94   C CD   . GLU   A 1 8   ? -12.188 -11.27  -11.067 1   80.839  ? 20  GLU   B CD   1 ? 1 
ATOM   95   O OE1  . GLU   A 1 8   ? -13.006 -11.153 -12.02  1   82.811  ? 20  GLU   B OE1  1 ? 1 
ATOM   96   O OE2  . GLU   A 1 8   ? -12.025 -12.326 -10.406 1   82.985  ? 20  GLU   B OE2  1 ? 1 
ATOM   97   H H    . GLU   A 1 8   ? -11.942 -7.976  -8.784  1   64.325  ? 20  GLU   B H    1 c 1 
ATOM   98   H HA   . GLU   A 1 8   ? -10.167 -7.592  -10.839 1   71.803  ? 20  GLU   B HA   1 c 1 
ATOM   99   H HB2  . GLU   A 1 8   ? -12.81  -8.664  -10.993 1   74.269  ? 20  GLU   B HB2  1 c 1 
ATOM   100  H HB3  . GLU   A 1 8   ? -11.753 -8.736  -12.168 1   78.602  ? 20  GLU   B HB3  1 c 1 
ATOM   101  H HG2  . GLU   A 1 8   ? -10.428 -10.213 -10.979 1   78.219  ? 20  GLU   B HG2  1 c 1 
ATOM   102  H HG3  . GLU   A 1 8   ? -11.305 -10.033 -9.682  1   73.378  ? 20  GLU   B HG3  1 c 1 
ATOM   103  N N    . GLN   A 1 9   ? -12.891 -5.832  -10.859 1   66.743  ? 21  GLN   B N    1 ? 1 
ATOM   104  C CA   . GLN   A 1 9   ? -13.66  -4.836  -11.599 1   70.905  ? 21  GLN   B CA   1 ? 1 
ATOM   105  C C    . GLN   A 1 9   ? -13.922 -3.614  -10.718 1   65.191  ? 21  GLN   B C    1 ? 1 
ATOM   106  O O    . GLN   A 1 9   ? -14.62  -2.704  -11.135 1   66.749  ? 21  GLN   B O    1 ? 1 
ATOM   107  C CB   . GLN   A 1 9   ? -15.037 -5.324  -12.078 1   75.694  ? 21  GLN   B CB   1 ? 1 
ATOM   108  C CG   . GLN   A 1 9   ? -15.077 -6.766  -12.579 1   81.315  ? 21  GLN   B CG   1 ? 1 
ATOM   109  C CD   . GLN   A 1 9   ? -14.082 -7.016  -13.68  1   91.288  ? 21  GLN   B CD   1 ? 1 
ATOM   110  O OE1  . GLN   A 1 9   ? -13.608 -6.074  -14.322 1   98.34   ? 21  GLN   B OE1  1 ? 1 
ATOM   111  N NE2  . GLN   A 1 9   ? -13.784 -8.284  -13.936 1   99.281  ? 21  GLN   B NE2  1 ? 1 
ATOM   112  H H    . GLN   A 1 9   ? -13.252 -6.189  -10.099 1   65.72   ? 21  GLN   B H    1 c 1 
ATOM   113  H HA   . GLN   A 1 9   ? -13.131 -4.547  -12.384 1   73.038  ? 21  GLN   B HA   1 c 1 
ATOM   114  H HB2  . GLN   A 1 9   ? -15.673 -5.233  -11.338 1   73.122  ? 21  GLN   B HB2  1 c 1 
ATOM   115  H HB3  . GLN   A 1 9   ? -15.339 -4.732  -12.798 1   77.723  ? 21  GLN   B HB3  1 c 1 
ATOM   116  H HG2  . GLN   A 1 9   ? -14.887 -7.375  -11.834 1   80.079  ? 21  GLN   B HG2  1 c 1 
ATOM   117  H HG3  . GLN   A 1 9   ? -15.978 -6.969  -12.91  1   83.87   ? 21  GLN   B HG3  1 c 1 
ATOM   118  H HE21 . GLN   A 1 9   ? -13.321 -8.489  -14.664 1   100.767 ? 21  GLN   B HE21 1 c 1 
ATOM   119  H HE22 . GLN   A 1 9   ? -14.049 -8.925  -13.383 1   96.397  ? 21  GLN   B HE22 1 c 1 
ATOM   120  N N    . GLY   A 1 10  ? -13.379 -3.591  -9.497  1   62.16   ? 22  GLY   B N    1 ? 1 
ATOM   121  C CA   . GLY   A 1 10  ? -13.731 -2.556  -8.528  1   58.075  ? 22  GLY   B CA   1 ? 1 
ATOM   122  C C    . GLY   A 1 10  ? -13.123 -1.218  -8.917  1   57.747  ? 22  GLY   B C    1 ? 1 
ATOM   123  O O    . GLY   A 1 10  ? -11.962 -1.182  -9.289  1   57.502  ? 22  GLY   B O    1 ? 1 
ATOM   124  H H    . GLY   A 1 10  ? -12.76  -4.22   -9.261  1   61.573  ? 22  GLY   B H    1 c 1 
ATOM   125  H HA2  . GLY   A 1 10  ? -14.71  -2.475  -8.483  1   57.943  ? 22  GLY   B HA2  1 c 1 
ATOM   126  H HA3  . GLY   A 1 10  ? -13.406 -2.819  -7.636  1   55.702  ? 22  GLY   B HA3  1 c 1 
ATOM   127  N N    . GLU   A 1 11  ? -13.892 -0.128  -8.723  1   57.531  ? 23  GLU   B N    1 ? 1 
ATOM   128  C CA   . GLU   A 1 11  ? -13.389 1.227   -8.844  1   57.953  ? 23  GLU   B CA   1 ? 1 
ATOM   129  C C    . GLU   A 1 11  ? -12.593 1.574   -7.586  1   53.335  ? 23  GLU   B C    1 ? 1 
ATOM   130  O O    . GLU   A 1 11  ? -13.068 1.353   -6.469  1   50.978  ? 23  GLU   B O    1 ? 1 
ATOM   131  C CB   . GLU   A 1 11  ? -14.638 2.07    -9.129  1   62.787  ? 23  GLU   B CB   1 ? 1 
ATOM   132  C CG   . GLU   A 1 11  ? -14.404 3.533   -9.495  1   67.161  ? 23  GLU   B CG   1 ? 1 
ATOM   133  C CD   . GLU   A 1 11  ? -15.592 4.484   -9.264  1   72.806  ? 23  GLU   B CD   1 ? 1 
ATOM   134  O OE1  . GLU   A 1 11  ? -16.652 4.138   -8.671  1   74.07   ? 23  GLU   B OE1  1 ? 1 
ATOM   135  O OE2  . GLU   A 1 11  ? -15.441 5.649   -9.678  1   78.912  ? 23  GLU   B OE2  1 ? 1 
ATOM   136  H H    . GLU   A 1 11  ? -14.771 -0.247  -8.499  1   56.884  ? 23  GLU   B H    1 c 1 
ATOM   137  H HA   . GLU   A 1 11  ? -12.786 1.269   -9.63   1   60.713  ? 23  GLU   B HA   1 c 1 
ATOM   138  H HB2  . GLU   A 1 11  ? -15.131 1.653   -9.866  1   64.398  ? 23  GLU   B HB2  1 c 1 
ATOM   139  H HB3  . GLU   A 1 11  ? -15.214 2.043   -8.337  1   60.307  ? 23  GLU   B HB3  1 c 1 
ATOM   140  H HG2  . GLU   A 1 11  ? -13.641 3.867   -8.977  1   66.553  ? 23  GLU   B HG2  1 c 1 
ATOM   141  H HG3  . GLU   A 1 11  ? -14.153 3.582   -10.442 1   70.649  ? 23  GLU   B HG3  1 c 1 
ATOM   142  N N    . ASP   A 1 12  ? -11.385 2.121   -7.754  1   51.782  ? 24  ASP   B N    1 ? 1 
ATOM   143  C CA   . ASP   A 1 12  ? -10.601 2.597   -6.625  1   50.322  ? 24  ASP   B CA   1 ? 1 
ATOM   144  C C    . ASP   A 1 12  ? -11.137 3.961   -6.227  1   50.28   ? 24  ASP   B C    1 ? 1 
ATOM   145  O O    . ASP   A 1 12  ? -10.954 4.897   -6.979  1   50.649  ? 24  ASP   B O    1 ? 1 
ATOM   146  C CB   . ASP   A 1 12  ? -9.115  2.711   -6.937  1   52.627  ? 24  ASP   B CB   1 ? 1 
ATOM   147  C CG   . ASP   A 1 12  ? -8.246  3.158   -5.763  1   51.364  ? 24  ASP   B CG   1 ? 1 
ATOM   148  O OD1  . ASP   A 1 12  ? -8.808  3.522   -4.699  1   49.706  ? 24  ASP   B OD1  1 ? 1 
ATOM   149  O OD2  . ASP   A 1 12  ? -7.005  3.137   -5.89   1   50.114  ? 24  ASP   B OD2  1 ? 1 
ATOM   150  H H    . ASP   A 1 12  ? -11.039 2.2     -8.597  1   55.155  ? 24  ASP   B H    1 c 1 
ATOM   151  H HA   . ASP   A 1 12  ? -10.717 1.975   -5.873  1   48.051  ? 24  ASP   B HA   1 c 1 
ATOM   152  H HB2  . ASP   A 1 12  ? -8.792  1.837   -7.238  1   53.134  ? 24  ASP   B HB2  1 c 1 
ATOM   153  H HB3  . ASP   A 1 12  ? -8.989  3.347   -7.672  1   55.187  ? 24  ASP   B HB3  1 c 1 
ATOM   154  N N    . ILE   A 1 13  ? -11.797 4.065   -5.061  1   48.761  ? 25  ILE   B N    1 ? 1 
ATOM   155  C CA   . ILE   A 1 13  ? -12.42  5.329   -4.659  1   49.987  ? 25  ILE   B CA   1 ? 1 
ATOM   156  C C    . ILE   A 1 13  ? -11.596 6.084   -3.615  1   50.526  ? 25  ILE   B C    1 ? 1 
ATOM   157  O O    . ILE   A 1 13  ? -12.075 7.073   -3.065  1   51.903  ? 25  ILE   B O    1 ? 1 
ATOM   158  C CB   . ILE   A 1 13  ? -13.861 5.083   -4.175  1   47.221  ? 25  ILE   B CB   1 ? 1 
ATOM   159  C CG1  . ILE   A 1 13  ? -13.924 4.179   -2.974  1   44.613  ? 25  ILE   B CG1  1 ? 1 
ATOM   160  C CG2  . ILE   A 1 13  ? -14.723 4.517   -5.3    1   48.041  ? 25  ILE   B CG2  1 ? 1 
ATOM   161  C CD1  . ILE   A 1 13  ? -15.318 4.079   -2.39   1   45.841  ? 25  ILE   B CD1  1 ? 1 
ATOM   162  H H    . ILE   A 1 13  ? -11.847 3.344   -4.502  1   46.825  ? 25  ILE   B H    1 c 1 
ATOM   163  H HA   . ILE   A 1 13  ? -12.476 5.896   -5.452  1   52.042  ? 25  ILE   B HA   1 c 1 
ATOM   164  H HB   . ILE   A 1 13  ? -14.239 5.947   -3.915  1   47.922  ? 25  ILE   B HB   1 c 1 
ATOM   165  H HG12 . ILE   A 1 13  ? -13.625 3.283   -3.233  1   44.644  ? 25  ILE   B HG12 1 c 1 
ATOM   166  H HG13 . ILE   A 1 13  ? -13.315 4.515   -2.286  1   44.322  ? 25  ILE   B HG13 1 c 1 
ATOM   167  H HG21 . ILE   A 1 13  ? -15.661 4.562   -5.05   1   47.981  ? 25  ILE   B HG21 1 c 1 
ATOM   168  H HG22 . ILE   A 1 13  ? -14.478 3.591   -5.465  1   47.782  ? 25  ILE   B HG22 1 c 1 
ATOM   169  H HG23 . ILE   A 1 13  ? -14.583 5.036   -6.11   1   50.557  ? 25  ILE   B HG23 1 c 1 
ATOM   170  H HD11 . ILE   A 1 13  ? -15.696 4.974   -2.294  1   46.008  ? 25  ILE   B HD11 1 c 1 
ATOM   171  H HD12 . ILE   A 1 13  ? -15.271 3.652   -1.514  1   43.611  ? 25  ILE   B HD12 1 c 1 
ATOM   172  H HD13 . ILE   A 1 13  ? -15.888 3.548   -2.977  1   45.794  ? 25  ILE   B HD13 1 c 1 
ATOM   173  N N    . THR   A 1 14  ? -10.349 5.683   -3.354  1   50.467  ? 26  THR   B N    1 ? 1 
ATOM   174  C CA   . THR   A 1 14  ? -9.473  6.477   -2.486  1   49.45   ? 26  THR   B CA   1 ? 1 
ATOM   175  C C    . THR   A 1 14  ? -8.938  7.695   -3.24   1   51.553  ? 26  THR   B C    1 ? 1 
ATOM   176  O O    . THR   A 1 14  ? -8.794  7.673   -4.463  1   52.872  ? 26  THR   B O    1 ? 1 
ATOM   177  C CB   . THR   A 1 14  ? -8.285  5.681   -1.941  1   49.122  ? 26  THR   B CB   1 ? 1 
ATOM   178  O OG1  . THR   A 1 14  ? -7.443  5.249   -3.019  1   51.03   ? 26  THR   B OG1  1 ? 1 
ATOM   179  C CG2  . THR   A 1 14  ? -8.717  4.471   -1.146  1   44.901  ? 26  THR   B CG2  1 ? 1 
ATOM   180  H H    . THR   A 1 14  ? -10.03  4.906   -3.715  1   49.982  ? 26  THR   B H    1 c 1 
ATOM   181  H HA   . THR   A 1 14  ? -10.005 6.789   -1.724  1   48.452  ? 26  THR   B HA   1 c 1 
ATOM   182  H HB   . THR   A 1 14  ? -7.761  6.265   -1.345  1   49.572  ? 26  THR   B HB   1 c 1 
ATOM   183  H HG1  . THR   A 1 14  ? -7.993  4.814   -3.56   0   30      ? 26  THR   B HG1  1 c 1 
ATOM   184  H HG21 . THR   A 1 14  ? -7.933  3.993   -0.828  1   45.116  ? 26  THR   B HG21 1 c 1 
ATOM   185  H HG22 . THR   A 1 14  ? -9.246  3.884   -1.71   1   44.782  ? 26  THR   B HG22 1 c 1 
ATOM   186  H HG23 . THR   A 1 14  ? -9.251  4.756   -0.386  1   44.052  ? 26  THR   B HG23 1 c 1 
ATOM   187  N N    . SER   A 1 15  ? -8.59   8.735   -2.469  1   50.721  ? 27  SER   B N    1 ? 1 
ATOM   188  C CA   . SER   A 1 15  ? -7.996  9.942   -2.996  1   55.741  ? 27  SER   B CA   1 ? 1 
ATOM   189  C C    . SER   A 1 15  ? -6.554  9.701   -3.424  1   57.459  ? 27  SER   B C    1 ? 1 
ATOM   190  O O    . SER   A 1 15  ? -6.07   10.317  -4.39   1   60.858  ? 27  SER   B O    1 ? 1 
ATOM   191  C CB   . SER   A 1 15  ? -8.062  11.046  -1.965  1   57.445  ? 27  SER   B CB   1 ? 1 
ATOM   192  O OG   . SER   A 1 15  ? -9.416  11.428  -1.814  1   54.913  ? 27  SER   B OG   1 ? 1 
ATOM   193  H H    . SER   A 1 15  ? -8.732  8.679   -1.568  1   49.781  ? 27  SER   B H    1 c 1 
ATOM   194  H HA   . SER   A 1 15  ? -8.515  10.223  -3.792  1   56.936  ? 27  SER   B HA   1 c 1 
ATOM   195  H HB2  . SER   A 1 15  ? -7.71   10.725  -1.113  1   55.414  ? 27  SER   B HB2  1 c 1 
ATOM   196  H HB3  . SER   A 1 15  ? -7.53   11.808  -2.26   1   60.051  ? 27  SER   B HB3  1 c 1 
ATOM   197  H HG   . SER   A 1 15  ? -9.342  12.04   -1.06   0   30      ? 27  SER   B HG   1 c 1 
ATOM   198  N N    . LYS   A 1 16  ? -5.887  8.812   -2.679  1   55.248  ? 28  LYS   B N    1 ? 1 
ATOM   199  C CA   . LYS   A 1 16  ? -4.485  8.503   -2.889  1   61.492  ? 28  LYS   B CA   1 ? 1 
ATOM   200  C C    . LYS   A 1 16  ? -4.313  7.456   -3.984  1   59.943  ? 28  LYS   B C    1 ? 1 
ATOM   201  O O    . LYS   A 1 16  ? -3.2    7.239   -4.424  1   61.481  ? 28  LYS   B O    1 ? 1 
ATOM   202  C CB   . LYS   A 1 16  ? -3.852  8.017   -1.585  1   63.555  ? 28  LYS   B CB   1 ? 1 
ATOM   203  C CG   . LYS   A 1 16  ? -3.581  9.129   -0.59   1   68.244  ? 28  LYS   B CG   1 ? 1 
ATOM   204  C CD   . LYS   A 1 16  ? -2.573  8.759   0.491   1   72.083  ? 28  LYS   B CD   1 ? 1 
ATOM   205  C CE   . LYS   A 1 16  ? -3.187  7.947   1.581   1   71.978  ? 28  LYS   B CE   1 ? 1 
ATOM   206  N NZ   . LYS   A 1 16  ? -2.503  8.236   2.84    1   76.834  ? 28  LYS   B NZ   1 ? 1 
ATOM   207  H H    . LYS   A 1 16  ? -6.328  8.382   -2.003  1   53.449  ? 28  LYS   B H    1 c 1 
ATOM   208  H HA   . LYS   A 1 16  ? -4.022  9.332   -3.172  1   64.223  ? 28  LYS   B HA   1 c 1 
ATOM   209  H HB2  . LYS   A 1 16  ? -4.446  7.359   -1.166  1   60.209  ? 28  LYS   B HB2  1 c 1 
ATOM   210  H HB3  . LYS   A 1 16  ? -3.005  7.568   -1.79   1   64.591  ? 28  LYS   B HB3  1 c 1 
ATOM   211  H HG2  . LYS   A 1 16  ? -3.249  9.912   -1.08   1   71.416  ? 28  LYS   B HG2  1 c 1 
ATOM   212  H HG3  . LYS   A 1 16  ? -4.43   9.382   -0.165  1   66.548  ? 28  LYS   B HG3  1 c 1 
ATOM   213  H HD2  . LYS   A 1 16  ? -1.838  8.248   0.085   1   73.246  ? 28  LYS   B HD2  1 c 1 
ATOM   214  H HD3  . LYS   A 1 16  ? -2.196  9.582   0.873   1   74.581  ? 28  LYS   B HD3  1 c 1 
ATOM   215  H HE2  . LYS   A 1 16  ? -4.133  8.16    1.675   1   70.015  ? 28  LYS   B HE2  1 c 1 
ATOM   216  H HE3  . LYS   A 1 16  ? -3.101  6.998   1.378   1   70.326  ? 28  LYS   B HE3  1 c 1 
ATOM   217  H HZ1  . LYS   A 1 16  ? -2.643  9.1     3.076   1   77.04   ? 28  LYS   B HZ1  1 c 1 
ATOM   218  H HZ2  . LYS   A 1 16  ? -1.613  8.094   2.747   1   77.585  ? 28  LYS   B HZ2  1 c 1 
ATOM   219  H HZ3  . LYS   A 1 16  ? -2.823  7.696   3.493   1   73.494  ? 28  LYS   B HZ3  1 c 1 
ATOM   220  N N    . LYS   A 1 17  ? -5.411  6.813   -4.413  1   56.066  ? 29  LYS   B N    1 ? 1 
ATOM   221  C CA   . LYS   A 1 17  ? -5.372  5.815   -5.473  1   57.346  ? 29  LYS   B CA   1 ? 1 
ATOM   222  C C    . LYS   A 1 17  ? -4.41   4.682   -5.104  1   55.992  ? 29  LYS   B C    1 ? 1 
ATOM   223  O O    . LYS   A 1 17  ? -3.548  4.279   -5.901  1   56.888  ? 29  LYS   B O    1 ? 1 
ATOM   224  C CB   . LYS   A 1 17  ? -4.994  6.456   -6.806  1   63.649  ? 29  LYS   B CB   1 ? 1 
ATOM   225  C CG   . LYS   A 1 17  ? -6.053  7.393   -7.327  1   67.172  ? 29  LYS   B CG   1 ? 1 
ATOM   226  C CD   . LYS   A 1 17  ? -7.264  6.603   -7.802  1   66.113  ? 29  LYS   B CD   1 ? 1 
ATOM   227  C CE   . LYS   A 1 17  ? -8.326  7.507   -8.316  1   69.24   ? 29  LYS   B CE   1 ? 1 
ATOM   228  N NZ   . LYS   A 1 17  ? -9.111  7.907   -7.145  1   66.685  ? 29  LYS   B NZ   1 ? 1 
ATOM   229  H H    . LYS   A 1 17  ? -6.216  6.995   -4.02   1   54.627  ? 29  LYS   B H    1 c 1 
ATOM   230  H HA   . LYS   A 1 17  ? -6.277  5.43    -5.556  1   55.412  ? 29  LYS   B HA   1 c 1 
ATOM   231  H HB2  . LYS   A 1 17  ? -4.155  6.952   -6.705  1   66.182  ? 29  LYS   B HB2  1 c 1 
ATOM   232  H HB3  . LYS   A 1 17  ? -4.849  5.75    -7.471  1   64.777  ? 29  LYS   B HB3  1 c 1 
ATOM   233  H HG2  . LYS   A 1 17  ? -6.32   8.011   -6.612  1   65.633  ? 29  LYS   B HG2  1 c 1 
ATOM   234  H HG3  . LYS   A 1 17  ? -5.685  7.914   -8.073  1   70.444  ? 29  LYS   B HG3  1 c 1 
ATOM   235  H HD2  . LYS   A 1 17  ? -6.989  5.99    -8.519  1   67.711  ? 29  LYS   B HD2  1 c 1 
ATOM   236  H HD3  . LYS   A 1 17  ? -7.624  6.069   -7.062  1   62.924  ? 29  LYS   B HD3  1 c 1 
ATOM   237  H HE2  . LYS   A 1 17  ? -7.939  8.293   -8.741  1   72.173  ? 29  LYS   B HE2  1 c 1 
ATOM   238  H HE3  . LYS   A 1 17  ? -8.896  7.041   -8.953  1   69.301  ? 29  LYS   B HE3  1 c 1 
ATOM   239  H HZ1  . LYS   A 1 17  ? -8.576  8.27    -6.511  1   66.129  ? 29  LYS   B HZ1  1 c 1 
ATOM   240  H HZ2  . LYS   A 1 17  ? -9.541  7.189   -6.797  1   63.781  ? 29  LYS   B HZ2  1 c 1 
ATOM   241  H HZ3  . LYS   A 1 17  ? -9.727  8.523   -7.393  1   67.477  ? 29  LYS   B HZ3  1 c 1 
ATOM   242  N N    . ASP   A 1 18  ? -4.608  4.15    -3.901  1   50.327  ? 30  ASP   B N    1 ? 1 
ATOM   243  C CA   . ASP   A 1 18  ? -3.793  3.074   -3.353  1   49.818  ? 30  ASP   B CA   1 ? 1 
ATOM   244  C C    . ASP   A 1 18  ? -4.587  1.775   -3.311  1   46.154  ? 30  ASP   B C    1 ? 1 
ATOM   245  O O    . ASP   A 1 18  ? -4.212  0.864   -2.604  1   44.748  ? 30  ASP   B O    1 ? 1 
ATOM   246  C CB   . ASP   A 1 18  ? -3.252  3.45    -1.984  1   49.402  ? 30  ASP   B CB   1 ? 1 
ATOM   247  C CG   . ASP   A 1 18  ? -4.319  3.802   -0.954  1   47.099  ? 30  ASP   B CG   1 ? 1 
ATOM   248  O OD1  . ASP   A 1 18  ? -5.479  3.411   -1.151  1   42.131  ? 30  ASP   B OD1  1 ? 1 
ATOM   249  O OD2  . ASP   A 1 18  ? -3.977  4.497   0.027   1   50.789  ? 30  ASP   B OD2  1 ? 1 
ATOM   250  H H    . ASP   A 1 18  ? -5.298  4.468   -3.393  1   49.001  ? 30  ASP   B H    1 c 1 
ATOM   251  H HA   . ASP   A 1 18  ? -3.017  2.941   -3.944  1   52.373  ? 30  ASP   B HA   1 c 1 
ATOM   252  H HB2  . ASP   A 1 18  ? -2.717  2.708   -1.633  1   49.387  ? 30  ASP   B HB2  1 c 1 
ATOM   253  H HB3  . ASP   A 1 18  ? -2.66   4.225   -2.085  1   51.933  ? 30  ASP   B HB3  1 c 1 
ATOM   254  N N    . ARG   A 1 19  ? -5.698  1.703   -4.056  1   46.683  ? 31  ARG   B N    1 ? 1 
ATOM   255  C CA   . ARG   A 1 19  ? -6.605  0.553   -4.056  1   44.477  ? 31  ARG   B CA   1 ? 1 
ATOM   256  C C    . ARG   A 1 19  ? -6.992  0.127   -2.644  1   43.045  ? 31  ARG   B C    1 ? 1 
ATOM   257  O O    . ARG   A 1 19  ? -7.283  -1.057  -2.416  1   41.594  ? 31  ARG   B O    1 ? 1 
ATOM   258  C CB   . ARG   A 1 19  ? -6.067  -0.646  -4.856  1   46.667  ? 31  ARG   B CB   1 ? 1 
ATOM   259  C CG   . ARG   A 1 19  ? -5.855  -0.313  -6.326  1   49.246  ? 31  ARG   B CG   1 ? 1 
ATOM   260  C CD   . ARG   A 1 19  ? -5.217  -1.521  -7.058  1   52.08   ? 31  ARG   B CD   1 ? 1 
ATOM   261  N NE   . ARG   A 1 19  ? -6.009  -2.743  -6.908  1   50.541  ? 31  ARG   B NE   1 ? 1 
ATOM   262  C CZ   . ARG   A 1 19  ? -7.067  -3.071  -7.666  1   53.324  ? 31  ARG   B CZ   1 ? 1 
ATOM   263  N NH1  . ARG   A 1 19  ? -7.517  -2.282  -8.623  1   55.478  ? 31  ARG   B NH1  1 ? 1 
ATOM   264  N NH2  . ARG   A 1 19  ? -7.68   -4.238  -7.521  1   55.564  ? 31  ARG   B NH2  1 ? 1 
ATOM   265  H H    . ARG   A 1 19  ? -5.9    2.405   -4.605  1   47.705  ? 31  ARG   B H    1 c 1 
ATOM   266  H HA   . ARG   A 1 19  ? -7.437  0.837   -4.511  1   44.775  ? 31  ARG   B HA   1 c 1 
ATOM   267  H HB2  . ARG   A 1 19  ? -5.212  -0.931  -4.471  1   46.961  ? 31  ARG   B HB2  1 c 1 
ATOM   268  H HB3  . ARG   A 1 19  ? -6.697  -1.394  -4.784  1   45.232  ? 31  ARG   B HB3  1 c 1 
ATOM   269  H HG2  . ARG   A 1 19  ? -6.718  -0.099  -6.743  1   49.438  ? 31  ARG   B HG2  1 c 1 
ATOM   270  H HG3  . ARG   A 1 19  ? -5.263  0.466   -6.408  1   51.035  ? 31  ARG   B HG3  1 c 1 
ATOM   271  H HD2  . ARG   A 1 19  ? -5.126  -1.31   -8.009  1   54.823  ? 31  ARG   B HD2  1 c 1 
ATOM   272  H HD3  . ARG   A 1 19  ? -4.319  -1.675  -6.698  1   52.738  ? 31  ARG   B HD3  1 c 1 
ATOM   273  H HE   . ARG   A 1 19  ? -5.778  -3.301  -6.279  1   50.011  ? 31  ARG   B HE   1 c 1 
ATOM   274  H HH11 . ARG   A 1 19  ? -7.552  -1.407  -8.497  1   54.89   ? 31  ARG   B HH11 1 c 1 
ATOM   275  H HH12 . ARG   A 1 19  ? -7.786  -2.634  -9.39   1   57.442  ? 31  ARG   B HH12 1 c 1 
ATOM   276  H HH21 . ARG   A 1 19  ? -7.308  -4.872  -7.03   1   54.096  ? 31  ARG   B HH21 1 c 1 
ATOM   277  H HH22 . ARG   A 1 19  ? -8.459  -4.379  -7.915  1   54.903  ? 31  ARG   B HH22 1 c 1 
ATOM   278  N N    . GLY   A 1 20  ? -7.08   1.107   -1.72   1   41.445  ? 32  GLY   B N    1 ? 1 
ATOM   279  C CA   . GLY   A 1 20  ? -7.365  0.783   -0.331  1   38.093  ? 32  GLY   B CA   1 ? 1 
ATOM   280  C C    . GLY   A 1 20  ? -8.852  0.51    -0.109  1   36.01   ? 32  GLY   B C    1 ? 1 
ATOM   281  O O    . GLY   A 1 20  ? -9.224  -0.253  0.793   1   36.761  ? 32  GLY   B O    1 ? 1 
ATOM   282  H H    . GLY   A 1 20  ? -6.981  1.982   -1.962  1   42.336  ? 32  GLY   B H    1 c 1 
ATOM   283  H HA2  . GLY   A 1 20  ? -6.843  -0.008  -0.068  1   38.396  ? 32  GLY   B HA2  1 c 1 
ATOM   284  H HA3  . GLY   A 1 20  ? -7.081  1.535   0.238   1   38.446  ? 32  GLY   B HA3  1 c 1 
ATOM   285  N N    . VAL   A 1 21  ? -9.68   1.135   -0.948  1   36.761  ? 33  VAL   B N    1 ? 1 
ATOM   286  C CA   . VAL   A 1 21  ? -11.122 0.967   -0.92   1   39.996  ? 33  VAL   B CA   1 ? 1 
ATOM   287  C C    . VAL   A 1 21  ? -11.554 0.782   -2.363  1   40.19   ? 33  VAL   B C    1 ? 1 
ATOM   288  O O    . VAL   A 1 21  ? -11.382 1.702   -3.16   1   43.881  ? 33  VAL   B O    1 ? 1 
ATOM   289  C CB   . VAL   A 1 21  ? -11.916 2.127   -0.254  1   38.531  ? 33  VAL   B CB   1 ? 1 
ATOM   290  C CG1  . VAL   A 1 21  ? -13.369 1.715   -0.133  1   39.71   ? 33  VAL   B CG1  1 ? 1 
ATOM   291  C CG2  . VAL   A 1 21  ? -11.339 2.545   1.095   1   38.918  ? 33  VAL   B CG2  1 ? 1 
ATOM   292  H H    . VAL   A 1 21  ? -9.326  1.698   -1.573  1   39.07   ? 33  VAL   B H    1 c 1 
ATOM   293  H HA   . VAL   A 1 21  ? -11.322 0.145   -0.433  1   37.722  ? 33  VAL   B HA   1 c 1 
ATOM   294  H HB   . VAL   A 1 21  ? -11.867 2.903   -0.86   1   40.485  ? 33  VAL   B HB   1 c 1 
ATOM   295  H HG11 . VAL   A 1 21  ? -13.429 0.871   0.345   1   38.328  ? 33  VAL   B HG11 1 c 1 
ATOM   296  H HG12 . VAL   A 1 21  ? -13.755 1.613   -1.019  1   40.085  ? 33  VAL   B HG12 1 c 1 
ATOM   297  H HG13 . VAL   A 1 21  ? -13.86  2.398   0.355   1   39.034  ? 33  VAL   B HG13 1 c 1 
ATOM   298  H HG21 . VAL   A 1 21  ? -11.876 3.263   1.47    1   38.602  ? 33  VAL   B HG21 1 c 1 
ATOM   299  H HG22 . VAL   A 1 21  ? -10.425 2.855   0.976   1   39.384  ? 33  VAL   B HG22 1 c 1 
ATOM   300  H HG23 . VAL   A 1 21  ? -11.346 1.785   1.701   1   37.621  ? 33  VAL   B HG23 1 c 1 
ATOM   301  N N    . LEU   A 1 22  ? -12.037 -0.423  -2.693  1   40.177  ? 34  LEU   B N    1 ? 1 
ATOM   302  C CA   . LEU   A 1 22  ? -12.523 -0.769  -4.019  1   41.582  ? 34  LEU   B CA   1 ? 1 
ATOM   303  C C    . LEU   A 1 22  ? -14.033 -0.983  -3.985  1   42.514  ? 34  LEU   B C    1 ? 1 
ATOM   304  O O    . LEU   A 1 22  ? -14.54  -1.652  -3.071  1   40.059  ? 34  LEU   B O    1 ? 1 
ATOM   305  C CB   . LEU   A 1 22  ? -11.804 -2.039  -4.485  1   44.752  ? 34  LEU   B CB   1 ? 1 
ATOM   306  C CG   . LEU   A 1 22  ? -10.288 -1.92   -4.68   1   45.2    ? 34  LEU   B CG   1 ? 1 
ATOM   307  C CD1  . LEU   A 1 22  ? -9.642  -3.293  -4.858  1   47.407  ? 34  LEU   B CD1  1 ? 1 
ATOM   308  C CD2  . LEU   A 1 22  ? -10.056 -1.017  -5.858  1   45.77   ? 34  LEU   B CD2  1 ? 1 
ATOM   309  H H    . LEU   A 1 22  ? -12.064 -1.069  -2.047  1   39.035  ? 34  LEU   B H    1 c 1 
ATOM   310  H HA   . LEU   A 1 22  ? -12.316 -0.027  -4.636  1   43.588  ? 34  LEU   B HA   1 c 1 
ATOM   311  H HB2  . LEU   A 1 22  ? -11.977 -2.749  -3.825  1   43.052  ? 34  LEU   B HB2  1 c 1 
ATOM   312  H HB3  . LEU   A 1 22  ? -12.206 -2.325  -5.338  1   45.834  ? 34  LEU   B HB3  1 c 1 
ATOM   313  H HG   . LEU   A 1 22  ? -9.9    -1.492  -3.874  1   43.721  ? 34  LEU   B HG   1 c 1 
ATOM   314  H HD11 . LEU   A 1 22  ? -9.81   -3.836  -4.069  1   45.672  ? 34  LEU   B HD11 1 c 1 
ATOM   315  H HD12 . LEU   A 1 22  ? -8.683  -3.188  -4.979  1   48.119  ? 34  LEU   B HD12 1 c 1 
ATOM   316  H HD13 . LEU   A 1 22  ? -10.02  -3.732  -5.638  1   48.74   ? 34  LEU   B HD13 1 c 1 
ATOM   317  H HD21 . LEU   A 1 22  ? -10.356 -0.12   -5.645  1   45.785  ? 34  LEU   B HD21 1 c 1 
ATOM   318  H HD22 . LEU   A 1 22  ? -10.55  -1.35   -6.627  1   47.863  ? 34  LEU   B HD22 1 c 1 
ATOM   319  H HD23 . LEU   A 1 22  ? -9.108  -0.997  -6.069  1   47.639  ? 34  LEU   B HD23 1 c 1 
ATOM   320  N N    . LYS   A 1 23  ? -14.726 -0.488  -5.023  1   45.783  ? 35  LYS   B N    1 ? 1 
ATOM   321  C CA   . LYS   A 1 23  ? -16.181 -0.474  -5.04   1   47.518  ? 35  LYS   B CA   1 ? 1 
ATOM   322  C C    . LYS   A 1 23  ? -16.744 -0.998  -6.351  1   54.176  ? 35  LYS   B C    1 ? 1 
ATOM   323  O O    . LYS   A 1 23  ? -16.265 -0.599  -7.406  1   58.025  ? 35  LYS   B O    1 ? 1 
ATOM   324  C CB   . LYS   A 1 23  ? -16.685 0.962   -4.931  1   49.216  ? 35  LYS   B CB   1 ? 1 
ATOM   325  C CG   . LYS   A 1 23  ? -18.188 1.088   -4.804  1   50.552  ? 35  LYS   B CG   1 ? 1 
ATOM   326  C CD   . LYS   A 1 23  ? -18.708 2.519   -4.82   1   50.213  ? 35  LYS   B CD   1 ? 1 
ATOM   327  C CE   . LYS   A 1 23  ? -20.155 2.569   -4.483  1   50.305  ? 35  LYS   B CE   1 ? 1 
ATOM   328  N NZ   . LYS   A 1 23  ? -20.808 3.788   -4.929  1   53.108  ? 35  LYS   B NZ   1 ? 1 
ATOM   329  H H    . LYS   A 1 23  ? -14.275 -0.151  -5.743  1   47.178  ? 35  LYS   B H    1 c 1 
ATOM   330  H HA   . LYS   A 1 23  ? -16.522 -1.015  -4.289  1   46.934  ? 35  LYS   B HA   1 c 1 
ATOM   331  H HB2  . LYS   A 1 23  ? -16.271 1.383   -4.147  1   47.389  ? 35  LYS   B HB2  1 c 1 
ATOM   332  H HB3  . LYS   A 1 23  ? -16.397 1.462   -5.724  1   50.619  ? 35  LYS   B HB3  1 c 1 
ATOM   333  H HG2  . LYS   A 1 23  ? -18.607 0.593   -5.54   1   51.921  ? 35  LYS   B HG2  1 c 1 
ATOM   334  H HG3  . LYS   A 1 23  ? -18.464 0.66    -3.964  1   48.781  ? 35  LYS   B HG3  1 c 1 
ATOM   335  H HD2  . LYS   A 1 23  ? -18.205 3.057   -4.17   1   48.945  ? 35  LYS   B HD2  1 c 1 
ATOM   336  H HD3  . LYS   A 1 23  ? -18.572 2.904   -5.714  1   52.163  ? 35  LYS   B HD3  1 c 1 
ATOM   337  H HE2  . LYS   A 1 23  ? -20.606 1.807   -4.889  1   51.675  ? 35  LYS   B HE2  1 c 1 
ATOM   338  H HE3  . LYS   A 1 23  ? -20.258 2.496   -3.517  1   49.046  ? 35  LYS   B HE3  1 c 1 
ATOM   339  H HZ1  . LYS   A 1 23  ? -20.79  3.831   -5.834  1   54.784  ? 35  LYS   B HZ1  1 c 1 
ATOM   340  H HZ2  . LYS   A 1 23  ? -20.378 4.509   -4.589  1   52.35   ? 35  LYS   B HZ2  1 c 1 
ATOM   341  H HZ3  . LYS   A 1 23  ? -21.669 3.795   -4.648  1   53.684  ? 35  LYS   B HZ3  1 c 1 
ATOM   342  N N    . ILE   A 1 24  ? -17.807 -1.828  -6.261  1   53.521  ? 36  ILE   B N    1 ? 1 
ATOM   343  C CA   . ILE   A 1 24  ? -18.724 -2.065  -7.37   1   54.89   ? 36  ILE   B CA   1 ? 1 
ATOM   344  C C    . ILE   A 1 24  ? -20.137 -1.736  -6.899  1   54.508  ? 36  ILE   B C    1 ? 1 
ATOM   345  O O    . ILE   A 1 24  ? -20.54  -2.115  -5.8    1   52.705  ? 36  ILE   B O    1 ? 1 
ATOM   346  C CB   . ILE   A 1 24  ? -18.618 -3.504  -7.891  1   57.654  ? 36  ILE   B CB   1 ? 1 
ATOM   347  C CG1  . ILE   A 1 24  ? -17.224 -3.784  -8.421  1   58.888  ? 36  ILE   B CG1  1 ? 1 
ATOM   348  C CG2  . ILE   A 1 24  ? -19.672 -3.813  -8.961  1   62.442  ? 36  ILE   B CG2  1 ? 1 
ATOM   349  C CD1  . ILE   A 1 24  ? -16.982 -5.236  -8.751  1   60.204  ? 36  ILE   B CD1  1 ? 1 
ATOM   350  H H    . ILE   A 1 24  ? -17.959 -2.264  -5.473  1   51.928  ? 36  ILE   B H    1 c 1 
ATOM   351  H HA   . ILE   A 1 24  ? -18.49  -1.459  -8.099  1   56.675  ? 36  ILE   B HA   1 c 1 
ATOM   352  H HB   . ILE   A 1 24  ? -18.774 -4.105  -7.136  1   56.532  ? 36  ILE   B HB   1 c 1 
ATOM   353  H HG12 . ILE   A 1 24  ? -17.079 -3.248  -9.228  1   60.295  ? 36  ILE   B HG12 1 c 1 
ATOM   354  H HG13 . ILE   A 1 24  ? -16.569 -3.502  -7.751  1   56.139  ? 36  ILE   B HG13 1 c 1 
ATOM   355  H HG21 . ILE   A 1 24  ? -19.581 -4.734  -9.255  1   63.835  ? 36  ILE   B HG21 1 c 1 
ATOM   356  H HG22 . ILE   A 1 24  ? -19.55  -3.219  -9.72   1   63.845  ? 36  ILE   B HG22 1 c 1 
ATOM   357  H HG23 . ILE   A 1 24  ? -20.561 -3.683  -8.592  1   62.33   ? 36  ILE   B HG23 1 c 1 
ATOM   358  H HD11 . ILE   A 1 24  ? -17.162 -5.787  -7.966  1   59.029  ? 36  ILE   B HD11 1 c 1 
ATOM   359  H HD12 . ILE   A 1 24  ? -16.05  -5.345  -9.016  1   60.671  ? 36  ILE   B HD12 1 c 1 
ATOM   360  H HD13 . ILE   A 1 24  ? -17.559 -5.518  -9.485  1   63.252  ? 36  ILE   B HD13 1 c 1 
ATOM   361  N N    . VAL   A 1 25  ? -20.856 -0.982  -7.734  1   55.788  ? 37  VAL   B N    1 ? 1 
ATOM   362  C CA   . VAL   A 1 25  ? -22.288 -0.801  -7.619  1   58.07   ? 37  VAL   B CA   1 ? 1 
ATOM   363  C C    . VAL   A 1 25  ? -22.985 -2.058  -8.14   1   62.761  ? 37  VAL   B C    1 ? 1 
ATOM   364  O O    . VAL   A 1 25  ? -22.79  -2.45   -9.29   1   65.134  ? 37  VAL   B O    1 ? 1 
ATOM   365  C CB   . VAL   A 1 25  ? -22.641 0.452   -8.439  1   60.92   ? 37  VAL   B CB   1 ? 1 
ATOM   366  C CG1  . VAL   A 1 25  ? -24.147 0.673   -8.581  1   63.776  ? 37  VAL   B CG1  1 ? 1 
ATOM   367  C CG2  . VAL   A 1 25  ? -21.944 1.687   -7.864  1   59.534  ? 37  VAL   B CG2  1 ? 1 
ATOM   368  H H    . VAL   A 1 25  ? -20.422 -0.567  -8.423  1   57.339  ? 37  VAL   B H    1 c 1 
ATOM   369  H HA   . VAL   A 1 25  ? -22.523 -0.655  -6.682  1   56.547  ? 37  VAL   B HA   1 c 1 
ATOM   370  H HB   . VAL   A 1 25  ? -22.283 0.311   -9.347  1   62.843  ? 37  VAL   B HB   1 c 1 
ATOM   371  H HG11 . VAL   A 1 25  ? -24.559 0.675   -7.7    1   62.508  ? 37  VAL   B HG11 1 c 1 
ATOM   372  H HG12 . VAL   A 1 25  ? -24.533 -0.041  -9.116  1   66.186  ? 37  VAL   B HG12 1 c 1 
ATOM   373  H HG13 . VAL   A 1 25  ? -24.311 1.526   -9.016  1   65.378  ? 37  VAL   B HG13 1 c 1 
ATOM   374  H HG21 . VAL   A 1 25  ? -22.293 2.486   -8.293  1   61.05   ? 37  VAL   B HG21 1 c 1 
ATOM   375  H HG22 . VAL   A 1 25  ? -20.988 1.627   -8.024  1   58.177  ? 37  VAL   B HG22 1 c 1 
ATOM   376  H HG23 . VAL   A 1 25  ? -22.109 1.737   -6.908  1   57.187  ? 37  VAL   B HG23 1 c 1 
ATOM   377  N N    . LYS   A 1 26  ? -23.788 -2.705  -7.285  1   63.059  ? 38  LYS   B N    1 ? 1 
ATOM   378  C CA   . LYS   A 1 26  ? -24.499 -3.914  -7.676  1   66.357  ? 38  LYS   B CA   1 ? 1 
ATOM   379  C C    . LYS   A 1 26  ? -25.97  -3.629  -7.985  1   71.072  ? 38  LYS   B C    1 ? 1 
ATOM   380  O O    . LYS   A 1 26  ? -26.531 -4.257  -8.865  1   73.355  ? 38  LYS   B O    1 ? 1 
ATOM   381  C CB   . LYS   A 1 26  ? -24.243 -4.952  -6.586  1   64.812  ? 38  LYS   B CB   1 ? 1 
ATOM   382  C CG   . LYS   A 1 26  ? -22.796 -5.479  -6.564  1   61.322  ? 38  LYS   B CG   1 ? 1 
ATOM   383  C CD   . LYS   A 1 26  ? -22.5   -6.128  -7.914  1   66.06   ? 38  LYS   B CD   1 ? 1 
ATOM   384  C CE   . LYS   A 1 26  ? -21.651 -7.345  -7.892  1   65.087  ? 38  LYS   B CE   1 ? 1 
ATOM   385  N NZ   . LYS   A 1 26  ? -21.576 -7.907  -9.234  1   68.395  ? 38  LYS   B NZ   1 ? 1 
ATOM   386  H H    . LYS   A 1 26  ? -23.891 -2.388  -6.434  1   60.982  ? 38  LYS   B H    1 c 1 
ATOM   387  H HA   . LYS   A 1 26  ? -24.087 -4.251  -8.509  1   68.123  ? 38  LYS   B HA   1 c 1 
ATOM   388  H HB2  . LYS   A 1 26  ? -24.444 -4.553  -5.712  1   62.62   ? 38  LYS   B HB2  1 c 1 
ATOM   389  H HB3  . LYS   A 1 26  ? -24.851 -5.71   -6.717  1   67.104  ? 38  LYS   B HB3  1 c 1 
ATOM   390  H HG2  . LYS   A 1 26  ? -22.176 -4.734  -6.406  1   59.474  ? 38  LYS   B HG2  1 c 1 
ATOM   391  H HG3  . LYS   A 1 26  ? -22.699 -6.14   -5.845  1   60.972  ? 38  LYS   B HG3  1 c 1 
ATOM   392  H HD2  . LYS   A 1 26  ? -23.353 -6.358  -8.342  1   68.58   ? 38  LYS   B HD2  1 c 1 
ATOM   393  H HD3  . LYS   A 1 26  ? -22.067 -5.458  -8.486  1   65.315  ? 38  LYS   B HD3  1 c 1 
ATOM   394  H HE2  . LYS   A 1 26  ? -20.755 -7.111  -7.593  1   62.649  ? 38  LYS   B HE2  1 c 1 
ATOM   395  H HE3  . LYS   A 1 26  ? -22.024 -8.005  -7.282  1   65.373  ? 38  LYS   B HE3  1 c 1 
ATOM   396  H HZ1  . LYS   A 1 26  ? -21.263 -7.284  -9.813  1   68.852  ? 38  LYS   B HZ1  1 c 1 
ATOM   397  H HZ2  . LYS   A 1 26  ? -22.4   -8.175  -9.501  1   71.444  ? 38  LYS   B HZ2  1 c 1 
ATOM   398  H HZ3  . LYS   A 1 26  ? -21.018 -8.62   -9.235  1   69.03   ? 38  LYS   B HZ3  1 c 1 
ATOM   399  N N    . ARG   A 1 27  ? -26.59  -2.65   -7.313  1   71.748  ? 39  ARG   B N    1 ? 1 
ATOM   400  C CA   . ARG   A 1 27  ? -27.921 -2.197  -7.69   1   74.427  ? 39  ARG   B CA   1 ? 1 
ATOM   401  C C    . ARG   A 1 27  ? -27.943 -0.675  -7.62   1   74.087  ? 39  ARG   B C    1 ? 1 
ATOM   402  O O    . ARG   A 1 27  ? -27.519 -0.095  -6.632  1   73.704  ? 39  ARG   B O    1 ? 1 
ATOM   403  C CB   . ARG   A 1 27  ? -29.015 -2.796  -6.797  1   75.256  ? 39  ARG   B CB   1 ? 1 
ATOM   404  C CG   . ARG   A 1 27  ? -30.44  -2.543  -7.286  1   79.74   ? 39  ARG   B CG   1 ? 1 
ATOM   405  C CD   . ARG   A 1 27  ? -31.49  -2.93   -6.245  1   81.366  ? 39  ARG   B CD   1 ? 1 
ATOM   406  N NE   . ARG   A 1 27  ? -31.473 -2.023  -5.081  1   79.343  ? 39  ARG   B NE   1 ? 1 
ATOM   407  C CZ   . ARG   A 1 27  ? -31.964 -2.31   -3.867  1   79.272  ? 39  ARG   B CZ   1 ? 1 
ATOM   408  N NH1  . ARG   A 1 27  ? -32.48  -3.506  -3.604  1   82.698  ? 39  ARG   B NH1  1 ? 1 
ATOM   409  N NH2  . ARG   A 1 27  ? -31.914 -1.419  -2.897  1   76.363  ? 39  ARG   B NH2  1 ? 1 
ATOM   410  H H    . ARG   A 1 27  ? -26.179 -2.263  -6.594  1   68.037  ? 39  ARG   B H    1 c 1 
ATOM   411  H HA   . ARG   A 1 27  ? -28.092 -2.472  -8.627  1   77.673  ? 39  ARG   B HA   1 c 1 
ATOM   412  H HB2  . ARG   A 1 27  ? -28.872 -3.764  -6.733  1   75.575  ? 39  ARG   B HB2  1 c 1 
ATOM   413  H HB3  . ARG   A 1 27  ? -28.922 -2.422  -5.895  1   72.748  ? 39  ARG   B HB3  1 c 1 
ATOM   414  H HG2  . ARG   A 1 27  ? -30.545 -1.592  -7.506  1   80.048  ? 39  ARG   B HG2  1 c 1 
ATOM   415  H HG3  . ARG   A 1 27  ? -30.597 -3.062  -8.105  1   82.842  ? 39  ARG   B HG3  1 c 1 
ATOM   416  H HD2  . ARG   A 1 27  ? -32.378 -2.908  -6.657  1   85.774  ? 39  ARG   B HD2  1 c 1 
ATOM   417  H HD3  . ARG   A 1 27  ? -31.319 -3.845  -5.944  1   81.414  ? 39  ARG   B HD3  1 c 1 
ATOM   418  H HE   . ARG   A 1 27  ? -31.115 -1.236  -5.19   1   77.427  ? 39  ARG   B HE   1 c 1 
ATOM   419  H HH11 . ARG   A 1 27  ? -32.935 -3.94   -4.225  1   85.708  ? 39  ARG   B HH11 1 c 1 
ATOM   420  H HH12 . ARG   A 1 27  ? -32.375 -3.861  -2.802  1   81.381  ? 39  ARG   B HH12 1 c 1 
ATOM   421  H HH21 . ARG   A 1 27  ? -31.347 -0.743  -2.949  1   74.183  ? 39  ARG   B HH21 1 c 1 
ATOM   422  H HH22 . ARG   A 1 27  ? -32.447 -1.501  -2.197  1   77.786  ? 39  ARG   B HH22 1 c 1 
ATOM   423  N N    . VAL   A 1 28  ? -28.412 -0.039  -8.687  1   78.781  ? 40  VAL   B N    1 ? 1 
ATOM   424  C CA   . VAL   A 1 28  ? -28.306 1.398   -8.831  1   79.617  ? 40  VAL   B CA   1 ? 1 
ATOM   425  C C    . VAL   A 1 28  ? -29.376 2.042   -7.955  1   83.809  ? 40  VAL   B C    1 ? 1 
ATOM   426  O O    . VAL   A 1 28  ? -30.511 1.566   -7.918  1   89.309  ? 40  VAL   B O    1 ? 1 
ATOM   427  C CB   . VAL   A 1 28  ? -28.429 1.823   -10.307 1   82.342  ? 40  VAL   B CB   1 ? 1 
ATOM   428  C CG1  . VAL   A 1 28  ? -29.826 1.58    -10.853 1   88.076  ? 40  VAL   B CG1  1 ? 1 
ATOM   429  C CG2  . VAL   A 1 28  ? -28.019 3.277   -10.509 1   81.619  ? 40  VAL   B CG2  1 ? 1 
ATOM   430  H H    . VAL   A 1 28  ? -28.814 -0.52   -9.352  1   81.836  ? 40  VAL   B H    1 c 1 
ATOM   431  H HA   . VAL   A 1 28  ? -27.428 1.674   -8.505  1   76.498  ? 40  VAL   B HA   1 c 1 
ATOM   432  H HB   . VAL   A 1 28  ? -27.804 1.261   -10.823 1   82.352  ? 40  VAL   B HB   1 c 1 
ATOM   433  H HG11 . VAL   A 1 28  ? -30.448 2.212   -10.454 1   88.931  ? 40  VAL   B HG11 1 c 1 
ATOM   434  H HG12 . VAL   A 1 28  ? -30.107 0.674   -10.645 1   88.487  ? 40  VAL   B HG12 1 c 1 
ATOM   435  H HG13 . VAL   A 1 28  ? -29.819 1.702   -11.816 1   91.024  ? 40  VAL   B HG13 1 c 1 
ATOM   436  H HG21 . VAL   A 1 28  ? -28.046 3.493   -11.456 1   84.787  ? 40  VAL   B HG21 1 c 1 
ATOM   437  H HG22 . VAL   A 1 28  ? -27.117 3.41    -10.172 1   78.502  ? 40  VAL   B HG22 1 c 1 
ATOM   438  H HG23 . VAL   A 1 28  ? -28.632 3.858   -10.028 1   82.352  ? 40  VAL   B HG23 1 c 1 
ATOM   439  N N    . GLY   A 1 29  ? -28.97  3.108   -7.25   1   85.198  ? 41  GLY   B N    1 ? 1 
ATOM   440  C CA   . GLY   A 1 29  ? -29.87  3.994   -6.526  1   87.673  ? 41  GLY   B CA   1 ? 1 
ATOM   441  C C    . GLY   A 1 29  ? -30.578 4.98    -7.459  1   91.06   ? 41  GLY   B C    1 ? 1 
ATOM   442  O O    . GLY   A 1 29  ? -30.672 4.761   -8.661  1   94.344  ? 41  GLY   B O    1 ? 1 
ATOM   443  H H    . GLY   A 1 29  ? -28.075 3.292   -7.22   1   81.733  ? 41  GLY   B H    1 c 1 
ATOM   444  H HA2  . GLY   A 1 29  ? -30.541 3.452   -6.049  1   87.974  ? 41  GLY   B HA2  1 c 1 
ATOM   445  H HA3  . GLY   A 1 29  ? -29.35  4.494   -5.853  1   84.347  ? 41  GLY   B HA3  1 c 1 
ATOM   446  N N    . ASN   A 1 30  ? -31.074 6.076   -6.882  1   91.478  ? 42  ASN   B N    1 ? 1 
ATOM   447  C CA   . ASN   A 1 30  ? -31.752 7.137   -7.611  1   95.129  ? 42  ASN   B CA   1 ? 1 
ATOM   448  C C    . ASN   A 1 30  ? -31.429 8.462   -6.926  1   93.141  ? 42  ASN   B C    1 ? 1 
ATOM   449  O O    . ASN   A 1 30  ? -30.908 8.469   -5.819  1   86.569  ? 42  ASN   B O    1 ? 1 
ATOM   450  C CB   . ASN   A 1 30  ? -33.25  6.876   -7.627  1   102.691 ? 42  ASN   B CB   1 ? 1 
ATOM   451  C CG   . ASN   A 1 30  ? -33.72  6.419   -6.268  1   103.09  ? 42  ASN   B CG   1 ? 1 
ATOM   452  O OD1  . ASN   A 1 30  ? -33.855 7.244   -5.36   1   103.935 ? 42  ASN   B OD1  1 ? 1 
ATOM   453  N ND2  . ASN   A 1 30  ? -33.935 5.122   -6.09   1   103.681 ? 42  ASN   B ND2  1 ? 1 
ATOM   454  H H    . ASN   A 1 30  ? -30.977 6.169   -5.978  1   89.324  ? 42  ASN   B H    1 c 1 
ATOM   455  H HA   . ASN   A 1 30  ? -31.428 7.155   -8.54   1   96.775  ? 42  ASN   B HA   1 c 1 
ATOM   456  H HB2  . ASN   A 1 30  ? -33.723 7.695   -7.877  1   105.601 ? 42  ASN   B HB2  1 c 1 
ATOM   457  H HB3  . ASN   A 1 30  ? -33.455 6.188   -8.292  1   104.259 ? 42  ASN   B HB3  1 c 1 
ATOM   458  H HD21 . ASN   A 1 30  ? -34.321 4.837   -5.342  1   103.359 ? 42  ASN   B HD21 1 c 1 
ATOM   459  H HD22 . ASN   A 1 30  ? -33.693 4.539   -6.713  1   103.341 ? 42  ASN   B HD22 1 c 1 
ATOM   460  N N    . GLY   A 1 31  ? -31.787 9.583   -7.554  1   96.735  ? 43  GLY   B N    1 ? 1 
ATOM   461  C CA   . GLY   A 1 31  ? -31.414 10.893  -7.053  1   95.268  ? 43  GLY   B CA   1 ? 1 
ATOM   462  C C    . GLY   A 1 31  ? -29.989 11.208  -7.489  1   93.81   ? 43  GLY   B C    1 ? 1 
ATOM   463  O O    . GLY   A 1 31  ? -29.167 10.306  -7.611  1   91.96   ? 43  GLY   B O    1 ? 1 
ATOM   464  H H    . GLY   A 1 31  ? -32.279 9.529   -8.323  1   99.952  ? 43  GLY   B H    1 c 1 
ATOM   465  H HA2  . GLY   A 1 31  ? -32.034 11.571  -7.413  1   99.926  ? 43  GLY   B HA2  1 c 1 
ATOM   466  H HA3  . GLY   A 1 31  ? -31.477 10.905  -6.069  1   94.088  ? 43  GLY   B HA3  1 c 1 
ATOM   467  N N    . GLU   A 1 32  ? -29.718 12.487  -7.751  1   98.323  ? 44  GLU   B N    1 ? 1 
ATOM   468  C CA   . GLU   A 1 32  ? -28.395 12.939  -8.158  1   97.524  ? 44  GLU   B CA   1 ? 1 
ATOM   469  C C    . GLU   A 1 32  ? -27.456 12.964  -6.944  1   92.946  ? 44  GLU   B C    1 ? 1 
ATOM   470  O O    . GLU   A 1 32  ? -26.236 12.874  -7.091  1   89.847  ? 44  GLU   B O    1 ? 1 
ATOM   471  C CB   . GLU   A 1 32  ? -28.536 14.306  -8.839  1   101.854 ? 44  GLU   B CB   1 ? 1 
ATOM   472  H H    . GLU   A 1 32  ? -30.386 13.106  -7.668  1   101.004 ? 44  GLU   B H    1 c 1 
ATOM   473  H HA   . GLU   A 1 32  ? -28.037 12.295  -8.821  1   96.587  ? 44  GLU   B HA   1 c 1 
ATOM   474  H HB2  . GLU   A 1 32  ? -27.64  14.568  -9.149  0   30      ? 44  GLU   B HB2  1 c 1 
ATOM   475  H HB3  . GLU   A 1 32  ? -29.489 14.424  -9.073  0   30      ? 44  GLU   B HB3  1 c 1 
ATOM   476  N N    . GLU   A 1 33  ? -28.035 13.032  -5.735  1   90.756  ? 45  GLU   B N    1 ? 1 
ATOM   477  C CA   . GLU   A 1 33  ? -27.334 13.521  -4.558  1   86.334  ? 45  GLU   B CA   1 ? 1 
ATOM   478  C C    . GLU   A 1 33  ? -26.785 12.363  -3.722  1   81.339  ? 45  GLU   B C    1 ? 1 
ATOM   479  O O    . GLU   A 1 33  ? -27.459 11.363  -3.474  1   75.777  ? 45  GLU   B O    1 ? 1 
ATOM   480  C CB   . GLU   A 1 33  ? -28.286 14.419  -3.763  1   88.021  ? 45  GLU   B CB   1 ? 1 
ATOM   481  H H    . GLU   A 1 33  ? -28.901 12.757  -5.64   1   92.054  ? 45  GLU   B H    1 c 1 
ATOM   482  H HA   . GLU   A 1 33  ? -26.574 14.078  -4.862  1   86.632  ? 45  GLU   B HA   1 c 1 
ATOM   483  H HB2  . GLU   A 1 33  ? -27.73  15.065  -3.311  0   30      ? 45  GLU   B HB2  1 c 1 
ATOM   484  H HB3  . GLU   A 1 33  ? -29.216 14.234  -4.051  0   30      ? 45  GLU   B HB3  1 c 1 
ATOM   485  N N    . THR   A 1 34  ? -25.525 12.507  -3.303  1   78.764  ? 46  THR   B N    1 ? 1 
ATOM   486  C CA   . THR   A 1 34  ? -24.913 11.55   -2.403  1   73.128  ? 46  THR   B CA   1 ? 1 
ATOM   487  C C    . THR   A 1 34  ? -24.865 12.198  -1.031  1   73.891  ? 46  THR   B C    1 ? 1 
ATOM   488  O O    . THR   A 1 34  ? -24.946 13.404  -0.929  1   74.958  ? 46  THR   B O    1 ? 1 
ATOM   489  C CB   . THR   A 1 34  ? -23.513 11.201  -2.885  1   70.5    ? 46  THR   B CB   1 ? 1 
ATOM   490  O OG1  . THR   A 1 34  ? -22.839 12.461  -2.92   1   70.335  ? 46  THR   B OG1  1 ? 1 
ATOM   491  C CG2  . THR   A 1 34  ? -23.521 10.463  -4.211  1   69.704  ? 46  THR   B CG2  1 ? 1 
ATOM   492  H H    . THR   A 1 34  ? -25.032 13.223  -3.586  1   79.529  ? 46  THR   B H    1 c 1 
ATOM   493  H HA   . THR   A 1 34  ? -25.46  10.737  -2.369  1   72.961  ? 46  THR   B HA   1 c 1 
ATOM   494  H HB   . THR   A 1 34  ? -23.083 10.623  -2.211  1   67.112  ? 46  THR   B HB   1 c 1 
ATOM   495  H HG1  . THR   A 1 34  ? -23.366 13.027  -3.556  0   30      ? 46  THR   B HG1  1 c 1 
ATOM   496  H HG21 . THR   A 1 34  ? -22.608 10.248  -4.468  1   68.696  ? 46  THR   B HG21 1 c 1 
ATOM   497  H HG22 . THR   A 1 34  ? -23.924 11.025  -4.894  1   73.111  ? 46  THR   B HG22 1 c 1 
ATOM   498  H HG23 . THR   A 1 34  ? -24.034 9.642   -4.123  1   69.361  ? 46  THR   B HG23 1 c 1 
ATOM   499  N N    . PRO   A 1 35  ? -24.722 11.44   0.073   1   72.742  ? 47  PRO   B N    1 ? 1 
ATOM   500  C CA   . PRO   A 1 35  ? -24.594 12.058  1.38    1   72.292  ? 47  PRO   B CA   1 ? 1 
ATOM   501  C C    . PRO   A 1 35  ? -23.416 13.033  1.479   1   72.395  ? 47  PRO   B C    1 ? 1 
ATOM   502  O O    . PRO   A 1 35  ? -22.371 12.788  0.883   1   67.285  ? 47  PRO   B O    1 ? 1 
ATOM   503  C CB   . PRO   A 1 35  ? -24.402 10.873  2.312   1   68.253  ? 47  PRO   B CB   1 ? 1 
ATOM   504  C CG   . PRO   A 1 35  ? -24.894 9.669   1.55    1   69.864  ? 47  PRO   B CG   1 ? 1 
ATOM   505  C CD   . PRO   A 1 35  ? -24.676 9.973   0.104   1   71.045  ? 47  PRO   B CD   1 ? 1 
ATOM   506  H HA   . PRO   A 1 35  ? -25.427 12.523  1.603   1   74.877  ? 47  PRO   B HA   1 c 1 
ATOM   507  H HB2  . PRO   A 1 35  ? -23.462 10.769  2.543   1   67      ? 47  PRO   B HB2  1 c 1 
ATOM   508  H HB3  . PRO   A 1 35  ? -24.914 10.994  3.135   1   70.064  ? 47  PRO   B HB3  1 c 1 
ATOM   509  H HG2  . PRO   A 1 35  ? -24.393 8.87    1.809   1   66.832  ? 47  PRO   B HG2  1 c 1 
ATOM   510  H HG3  . PRO   A 1 35  ? -25.843 9.514   1.726   1   70.997  ? 47  PRO   B HG3  1 c 1 
ATOM   511  H HD2  . PRO   A 1 35  ? -23.809 9.645   -0.205  1   68.67   ? 47  PRO   B HD2  1 c 1 
ATOM   512  H HD3  . PRO   A 1 35  ? -25.384 9.592   -0.446  1   71.844  ? 47  PRO   B HD3  1 c 1 
ATOM   513  N N    . MET   A 1 36  ? -23.616 14.143  2.206   1   77.237  ? 48  MET   B N    1 ? 1 
ATOM   514  C CA   . MET   A 1 36  ? -22.546 15.054  2.588   1   80.388  ? 48  MET   B CA   1 ? 1 
ATOM   515  C C    . MET   A 1 36  ? -22.052 14.669  3.99    1   77.841  ? 48  MET   B C    1 ? 1 
ATOM   516  O O    . MET   A 1 36  ? -22.777 14.025  4.756   1   77.46   ? 48  MET   B O    1 ? 1 
ATOM   517  C CB   . MET   A 1 36  ? -23.043 16.507  2.6     1   91.464  ? 48  MET   B CB   1 ? 1 
ATOM   518  C CG   . MET   A 1 36  ? -23.534 17.084  1.259   1   97.168  ? 48  MET   B CG   1 ? 1 
ATOM   519  S SD   . MET   A 1 36  ? -22.289 17.326  -0.037  1   98.623  ? 48  MET   B SD   1 ? 1 
ATOM   520  C CE   . MET   A 1 36  ? -22.395 15.834  -1.032  1   94.032  ? 48  MET   B CE   1 ? 1 
ATOM   521  H H    . MET   A 1 36  ? -24.466 14.341  2.475   1   79.204  ? 48  MET   B H    1 c 1 
ATOM   522  H HA   . MET   A 1 36  ? -21.799 14.962  1.943   1   79.62   ? 48  MET   B HA   1 c 1 
ATOM   523  H HB2  . MET   A 1 36  ? -23.776 16.571  3.249   1   91.788  ? 48  MET   B HB2  1 c 1 
ATOM   524  H HB3  . MET   A 1 36  ? -22.314 17.074  2.93    1   91.211  ? 48  MET   B HB3  1 c 1 
ATOM   525  H HG2  . MET   A 1 36  ? -24.225 16.491  0.902   1   96.268  ? 48  MET   B HG2  1 c 1 
ATOM   526  H HG3  . MET   A 1 36  ? -23.958 17.949  1.431   1   100.297 ? 48  MET   B HG3  1 c 1 
ATOM   527  H HE1  . MET   A 1 36  ? -21.969 15.99   -1.894  1   95.153  ? 48  MET   B HE1  1 c 1 
ATOM   528  H HE2  . MET   A 1 36  ? -21.944 15.103  -0.57   1   91.04   ? 48  MET   B HE2  1 c 1 
ATOM   529  H HE3  . MET   A 1 36  ? -23.332 15.603  -1.171  1   95.074  ? 48  MET   B HE3  1 c 1 
ATOM   530  N N    . ILE   A 1 37  ? -20.819 15.069  4.339   1   73.108  ? 49  ILE   B N    1 ? 1 
ATOM   531  C CA   . ILE   A 1 37  ? -20.299 14.911  5.694   1   71.209  ? 49  ILE   B CA   1 ? 1 
ATOM   532  C C    . ILE   A 1 37  ? -21.293 15.544  6.683   1   70.291  ? 49  ILE   B C    1 ? 1 
ATOM   533  O O    . ILE   A 1 37  ? -21.732 16.657  6.46    1   68.556  ? 49  ILE   B O    1 ? 1 
ATOM   534  C CB   . ILE   A 1 37  ? -18.911 15.572  5.846   1   76.534  ? 49  ILE   B CB   1 ? 1 
ATOM   535  C CG1  . ILE   A 1 37  ? -17.858 15.031  4.848   1   78.201  ? 49  ILE   B CG1  1 ? 1 
ATOM   536  C CG2  . ILE   A 1 37  ? -18.419 15.487  7.298   1   74.982  ? 49  ILE   B CG2  1 ? 1 
ATOM   537  C CD1  . ILE   A 1 37  ? -16.891 14.011  5.424   1   81.134  ? 49  ILE   B CD1  1 ? 1 
ATOM   538  H H    . ILE   A 1 37  ? -20.291 15.468  3.709   1   74.633  ? 49  ILE   B H    1 c 1 
ATOM   539  H HA   . ILE   A 1 37  ? -20.217 13.958  5.889   1   68.517  ? 49  ILE   B HA   1 c 1 
ATOM   540  H HB   . ILE   A 1 37  ? -19.028 16.521  5.642   1   79.099  ? 49  ILE   B HB   1 c 1 
ATOM   541  H HG12 . ILE   A 1 37  ? -18.324 14.622  4.091   1   77.426  ? 49  ILE   B HG12 1 c 1 
ATOM   542  H HG13 . ILE   A 1 37  ? -17.341 15.788  4.503   1   80.567  ? 49  ILE   B HG13 1 c 1 
ATOM   543  H HG21 . ILE   A 1 37  ? -17.491 15.772  7.347   1   75.923  ? 49  ILE   B HG21 1 c 1 
ATOM   544  H HG22 . ILE   A 1 37  ? -18.493 14.572  7.615   1   73      ? 49  ILE   B HG22 1 c 1 
ATOM   545  H HG23 . ILE   A 1 37  ? -18.96  16.066  7.86    1   78.024  ? 49  ILE   B HG23 1 c 1 
ATOM   546  H HD11 . ILE   A 1 37  ? -16.305 14.429  6.083   1   80.16   ? 49  ILE   B HD11 1 c 1 
ATOM   547  H HD12 . ILE   A 1 37  ? -16.35  13.642  4.7     1   77.789  ? 49  ILE   B HD12 1 c 1 
ATOM   548  H HD13 . ILE   A 1 37  ? -17.395 13.29   5.847   1   77.311  ? 49  ILE   B HD13 1 c 1 
ATOM   549  N N    . GLY   A 1 38  ? -21.642 14.815  7.752   1   67.127  ? 50  GLY   B N    1 ? 1 
ATOM   550  C CA   . GLY   A 1 38  ? -22.552 15.299  8.768   1   72.207  ? 50  GLY   B CA   1 ? 1 
ATOM   551  C C    . GLY   A 1 38  ? -23.913 14.605  8.739   1   72.279  ? 50  GLY   B C    1 ? 1 
ATOM   552  O O    . GLY   A 1 38  ? -24.634 14.628  9.744   1   77.925  ? 50  GLY   B O    1 ? 1 
ATOM   553  H H    . GLY   A 1 38  ? -21.294 13.975  7.846   1   65.295  ? 50  GLY   B H    1 c 1 
ATOM   554  H HA2  . GLY   A 1 38  ? -22.139 15.16   9.653   1   71.689  ? 50  GLY   B HA2  1 c 1 
ATOM   555  H HA3  . GLY   A 1 38  ? -22.681 16.269  8.65    1   74.796  ? 50  GLY   B HA3  1 c 1 
ATOM   556  N N    . ASP   A 1 39  ? -24.309 14.101  7.573   1   67.447  ? 51  ASP   B N    1 ? 1 
ATOM   557  C CA   . ASP   A 1 39  ? -25.623 13.501  7.397   1   71.185  ? 51  ASP   B CA   1 ? 1 
ATOM   558  C C    . ASP   A 1 39  ? -25.815 12.312  8.347   1   68.137  ? 51  ASP   B C    1 ? 1 
ATOM   559  O O    . ASP   A 1 39  ? -24.866 11.603  8.666   1   64.154  ? 51  ASP   B O    1 ? 1 
ATOM   560  C CB   . ASP   A 1 39  ? -25.843 13.099  5.937   1   70.86   ? 51  ASP   B CB   1 ? 1 
ATOM   561  C CG   . ASP   A 1 39  ? -25.976 14.26   4.954   1   73.655  ? 51  ASP   B CG   1 ? 1 
ATOM   562  O OD1  . ASP   A 1 39  ? -26.054 15.402  5.42    1   75.145  ? 51  ASP   B OD1  1 ? 1 
ATOM   563  O OD2  . ASP   A 1 39  ? -25.993 14.019  3.729   1   73.555  ? 51  ASP   B OD2  1 ? 1 
ATOM   564  H H    . ASP   A 1 39  ? -23.743 14.132  6.856   1   67.373  ? 51  ASP   B H    1 c 1 
ATOM   565  H HA   . ASP   A 1 39  ? -26.298 14.182  7.619   1   73.975  ? 51  ASP   B HA   1 c 1 
ATOM   566  H HB2  . ASP   A 1 39  ? -25.092 12.539  5.649   1   67.541  ? 51  ASP   B HB2  1 c 1 
ATOM   567  H HB3  . ASP   A 1 39  ? -26.659 12.559  5.88    1   71.2    ? 51  ASP   B HB3  1 c 1 
ATOM   568  N N    . LYS   A 1 40  ? -27.062 12.112  8.8     1   71.882  ? 52  LYS   B N    1 ? 1 
ATOM   569  C CA   . LYS   A 1 40  ? -27.472 10.892  9.484   1   71.591  ? 52  LYS   B CA   1 ? 1 
ATOM   570  C C    . LYS   A 1 40  ? -27.847 9.878   8.4     1   70.911  ? 52  LYS   B C    1 ? 1 
ATOM   571  O O    . LYS   A 1 40  ? -28.766 10.129  7.632   1   74.216  ? 52  LYS   B O    1 ? 1 
ATOM   572  C CB   . LYS   A 1 40  ? -28.62  11.199  10.466  1   76.057  ? 52  LYS   B CB   1 ? 1 
ATOM   573  C CG   . LYS   A 1 40  ? -29.171 10.097  11.368  1   76.615  ? 52  LYS   B CG   1 ? 1 
ATOM   574  H H    . LYS   A 1 40  ? -27.686 12.768  8.676   1   74.762  ? 52  LYS   B H    1 c 1 
ATOM   575  H HA   . LYS   A 1 40  ? -26.699 10.544  9.998   1   69.583  ? 52  LYS   B HA   1 c 1 
ATOM   576  H HB2  . LYS   A 1 40  ? -28.319 11.93   11.047  1   77.571  ? 52  LYS   B HB2  1 c 1 
ATOM   577  H HB3  . LYS   A 1 40  ? -29.369 11.547  9.938   1   78.31   ? 52  LYS   B HB3  1 c 1 
ATOM   578  H HG2  . LYS   A 1 40  ? -28.426 9.723   11.841  0   30      ? 52  LYS   B HG2  1 c 1 
ATOM   579  H HG3  . LYS   A 1 40  ? -30.178 10.203  11.424  0   30      ? 52  LYS   B HG3  1 c 1 
ATOM   580  N N    . VAL   A 1 41  ? -27.14  8.742   8.368   1   66.439  ? 53  VAL   B N    1 ? 1 
ATOM   581  C CA   . VAL   A 1 41  ? -27.21  7.77    7.29    1   67.469  ? 53  VAL   B CA   1 ? 1 
ATOM   582  C C    . VAL   A 1 41  ? -27.75  6.437   7.819   1   65.682  ? 53  VAL   B C    1 ? 1 
ATOM   583  O O    . VAL   A 1 41  ? -27.318 5.945   8.857   1   66.634  ? 53  VAL   B O    1 ? 1 
ATOM   584  C CB   . VAL   A 1 41  ? -25.785 7.624   6.72    1   64.44   ? 53  VAL   B CB   1 ? 1 
ATOM   585  C CG1  . VAL   A 1 41  ? -25.679 6.556   5.644   1   63.138  ? 53  VAL   B CG1  1 ? 1 
ATOM   586  C CG2  . VAL   A 1 41  ? -25.264 8.951   6.177   1   68.23   ? 53  VAL   B CG2  1 ? 1 
ATOM   587  H H    . VAL   A 1 41  ? -26.581 8.562   9.068   1   66.236  ? 53  VAL   B H    1 c 1 
ATOM   588  H HA   . VAL   A 1 41  ? -27.803 8.106   6.591   1   68.209  ? 53  VAL   B HA   1 c 1 
ATOM   589  H HB   . VAL   A 1 41  ? -25.2   7.356   7.467   1   63.724  ? 53  VAL   B HB   1 c 1 
ATOM   590  H HG11 . VAL   A 1 41  ? -26.369 6.7     4.975   1   64.519  ? 53  VAL   B HG11 1 c 1 
ATOM   591  H HG12 . VAL   A 1 41  ? -25.794 5.677   6.043   1   62.397  ? 53  VAL   B HG12 1 c 1 
ATOM   592  H HG13 . VAL   A 1 41  ? -24.807 6.606   5.223   1   60.792  ? 53  VAL   B HG13 1 c 1 
ATOM   593  H HG21 . VAL   A 1 41  ? -24.428 8.803   5.703   1   64.902  ? 53  VAL   B HG21 1 c 1 
ATOM   594  H HG22 . VAL   A 1 41  ? -25.112 9.567   6.913   1   68.178  ? 53  VAL   B HG22 1 c 1 
ATOM   595  H HG23 . VAL   A 1 41  ? -25.918 9.331   5.566   1   69.036  ? 53  VAL   B HG23 1 c 1 
ATOM   596  N N    . TYR   A 1 42  ? -28.693 5.852   7.088   1   67.005  ? 54  TYR   B N    1 ? 1 
ATOM   597  C CA   . TYR   A 1 42  ? -29.313 4.587   7.46    1   68.804  ? 54  TYR   B CA   1 ? 1 
ATOM   598  C C    . TYR   A 1 42  ? -28.956 3.534   6.399   1   64.48   ? 54  TYR   B C    1 ? 1 
ATOM   599  O O    . TYR   A 1 42  ? -29.228 3.758   5.225   1   66.894  ? 54  TYR   B O    1 ? 1 
ATOM   600  C CB   . TYR   A 1 42  ? -30.837 4.765   7.586   1   74.803  ? 54  TYR   B CB   1 ? 1 
ATOM   601  C CG   . TYR   A 1 42  ? -31.347 5.837   8.551   1   79.833  ? 54  TYR   B CG   1 ? 1 
ATOM   602  C CD1  . TYR   A 1 42  ? -31.216 7.192   8.252   1   80.947  ? 54  TYR   B CD1  1 ? 1 
ATOM   603  C CD2  . TYR   A 1 42  ? -31.998 5.504   9.734   1   84.579  ? 54  TYR   B CD2  1 ? 1 
ATOM   604  C CE1  . TYR   A 1 42  ? -31.677 8.177   9.114   1   86.667  ? 54  TYR   B CE1  1 ? 1 
ATOM   605  C CE2  . TYR   A 1 42  ? -32.468 6.482   10.603  1   90.024  ? 54  TYR   B CE2  1 ? 1 
ATOM   606  C CZ   . TYR   A 1 42  ? -32.293 7.822   10.299  1   90.55   ? 54  TYR   B CZ   1 ? 1 
ATOM   607  O OH   . TYR   A 1 42  ? -32.738 8.793   11.144  1   98.464  ? 54  TYR   B OH   1 ? 1 
ATOM   608  H H    . TYR   A 1 42  ? -28.965 6.257   6.315   1   67.955  ? 54  TYR   B H    1 c 1 
ATOM   609  H HA   . TYR   A 1 42  ? -28.952 4.295   8.338   1   67.889  ? 54  TYR   B HA   1 c 1 
ATOM   610  H HB2  . TYR   A 1 42  ? -31.192 4.963   6.692   1   75.708  ? 54  TYR   B HB2  1 c 1 
ATOM   611  H HB3  . TYR   A 1 42  ? -31.22  3.901   7.857   1   76.161  ? 54  TYR   B HB3  1 c 1 
ATOM   612  H HD1  . TYR   A 1 42  ? -30.782 7.448   7.454   1   79.329  ? 54  TYR   B HD1  1 c 1 
ATOM   613  H HD2  . TYR   A 1 42  ? -32.108 4.595   9.961   1   84.78   ? 54  TYR   B HD2  1 c 1 
ATOM   614  H HE1  . TYR   A 1 42  ? -31.557 9.087   8.9     1   86.875  ? 54  TYR   B HE1  1 c 1 
ATOM   615  H HE2  . TYR   A 1 42  ? -32.885 6.234   11.41   1   92.334  ? 54  TYR   B HE2  1 c 1 
ATOM   616  H HH   . TYR   A 1 42  ? -32.535 9.619   10.767  0   30      ? 54  TYR   B HH   1 c 1 
ATOM   617  N N    . VAL   A 1 43  ? -28.328 2.411   6.795   1   60.481  ? 55  VAL   B N    1 ? 1 
ATOM   618  C CA   . VAL   A 1 43  ? -27.98  1.357   5.845   1   58.885  ? 55  VAL   B CA   1 ? 1 
ATOM   619  C C    . VAL   A 1 43  ? -28.374 -0.021  6.377   1   60.839  ? 55  VAL   B C    1 ? 1 
ATOM   620  O O    . VAL   A 1 43  ? -28.491 -0.189  7.582   1   62.906  ? 55  VAL   B O    1 ? 1 
ATOM   621  C CB   . VAL   A 1 43  ? -26.485 1.298   5.512   1   54.089  ? 55  VAL   B CB   1 ? 1 
ATOM   622  C CG1  . VAL   A 1 43  ? -25.935 2.664   5.082   1   52.582  ? 55  VAL   B CG1  1 ? 1 
ATOM   623  C CG2  . VAL   A 1 43  ? -25.702 0.717   6.688   1   53.009  ? 55  VAL   B CG2  1 ? 1 
ATOM   624  H H    . VAL   A 1 43  ? -28.112 2.3     7.677   1   60.934  ? 55  VAL   B H    1 c 1 
ATOM   625  H HA   . VAL   A 1 43  ? -28.473 1.517   5.019   1   60.127  ? 55  VAL   B HA   1 c 1 
ATOM   626  H HB   . VAL   A 1 43  ? -26.38  0.68    4.753   1   53.776  ? 55  VAL   B HB   1 c 1 
ATOM   627  H HG11 . VAL   A 1 43  ? -25.997 3.289   5.824   1   53.301  ? 55  VAL   B HG11 1 c 1 
ATOM   628  H HG12 . VAL   A 1 43  ? -26.453 3.001   4.332   1   54.022  ? 55  VAL   B HG12 1 c 1 
ATOM   629  H HG13 . VAL   A 1 43  ? -25.005 2.571   4.816   1   50.303  ? 55  VAL   B HG13 1 c 1 
ATOM   630  H HG21 . VAL   A 1 43  ? -24.754 0.835   6.53    1   50.391  ? 55  VAL   B HG21 1 c 1 
ATOM   631  H HG22 . VAL   A 1 43  ? -25.896 -0.231  6.777   1   53.561  ? 55  VAL   B HG22 1 c 1 
ATOM   632  H HG23 . VAL   A 1 43  ? -25.953 1.178   7.507   1   54.036  ? 55  VAL   B HG23 1 c 1 
ATOM   633  N N    . HIS   A 1 44  ? -28.453 -1.003  5.466   1   60.352  ? 56  HIS   B N    1 ? 1 
ATOM   634  C CA   . HIS   A 1 44  ? -28.304 -2.415  5.802   1   64.533  ? 56  HIS   B CA   1 ? 1 
ATOM   635  C C    . HIS   A 1 44  ? -26.982 -2.905  5.227   1   61.305  ? 56  HIS   B C    1 ? 1 
ATOM   636  O O    . HIS   A 1 44  ? -26.56  -2.407  4.196   1   61.421  ? 56  HIS   B O    1 ? 1 
ATOM   637  C CB   . HIS   A 1 44  ? -29.466 -3.26   5.267   1   69.635  ? 56  HIS   B CB   1 ? 1 
ATOM   638  C CG   . HIS   A 1 44  ? -30.616 -3.374  6.207   1   75.961  ? 56  HIS   B CG   1 ? 1 
ATOM   639  N ND1  . HIS   A 1 44  ? -30.472 -3.827  7.506   1   76.406  ? 56  HIS   B ND1  1 ? 1 
ATOM   640  C CD2  . HIS   A 1 44  ? -31.926 -3.133  6.025   1   79.656  ? 56  HIS   B CD2  1 ? 1 
ATOM   641  C CE1  . HIS   A 1 44  ? -31.659 -3.824  8.083   1   82.058  ? 56  HIS   B CE1  1 ? 1 
ATOM   642  N NE2  . HIS   A 1 44  ? -32.548 -3.398  7.207   1   82.909  ? 56  HIS   B NE2  1 ? 1 
ATOM   643  H H    . HIS   A 1 44  ? -28.609 -0.78   4.593   1   61.482  ? 56  HIS   B H    1 c 1 
ATOM   644  H HA   . HIS   A 1 44  ? -28.265 -2.5    6.785   1   64.437  ? 56  HIS   B HA   1 c 1 
ATOM   645  H HB2  . HIS   A 1 44  ? -29.782 -2.862  4.426   1   70.366  ? 56  HIS   B HB2  1 c 1 
ATOM   646  H HB3  . HIS   A 1 44  ? -29.133 -4.161  5.063   1   69.592  ? 56  HIS   B HB3  1 c 1 
ATOM   647  H HD1  . HIS   A 1 44  ? -29.694 -4.068  7.951   0   30      ? 56  HIS   B HD1  1 c 1 
ATOM   648  H HD2  . HIS   A 1 44  ? -32.337 -2.809  5.248   1   80.79   ? 56  HIS   B HD2  1 c 1 
ATOM   649  H HE1  . HIS   A 1 44  ? -31.837 -4.081  8.972   1   83.433  ? 56  HIS   B HE1  1 c 1 
ATOM   650  H HE2  . HIS   A 1 44  ? -33.383 -3.297  7.421   0   30      ? 56  HIS   B HE2  1 c 1 
ATOM   651  N N    . TYR   A 1 45  ? -26.331 -3.858  5.903   1   58.495  ? 57  TYR   B N    1 ? 1 
ATOM   652  C CA   . TYR   A 1 45  ? -25.043 -4.332  5.428   1   54.41   ? 57  TYR   B CA   1 ? 1 
ATOM   653  C C    . TYR   A 1 45  ? -24.83  -5.785  5.819   1   56.172  ? 57  TYR   B C    1 ? 1 
ATOM   654  O O    . TYR   A 1 45  ? -25.45  -6.287  6.765   1   56.573  ? 57  TYR   B O    1 ? 1 
ATOM   655  C CB   . TYR   A 1 45  ? -23.887 -3.481  5.94    1   48.763  ? 57  TYR   B CB   1 ? 1 
ATOM   656  C CG   . TYR   A 1 45  ? -23.566 -3.719  7.403   1   49.24   ? 57  TYR   B CG   1 ? 1 
ATOM   657  C CD1  . TYR   A 1 45  ? -24.274 -3.061  8.416   1   51.931  ? 57  TYR   B CD1  1 ? 1 
ATOM   658  C CD2  . TYR   A 1 45  ? -22.612 -4.649  7.775   1   46.699  ? 57  TYR   B CD2  1 ? 1 
ATOM   659  C CE1  . TYR   A 1 45  ? -24     -3.291  9.754   1   50.273  ? 57  TYR   B CE1  1 ? 1 
ATOM   660  C CE2  . TYR   A 1 45  ? -22.362 -4.92   9.111   1   48.491  ? 57  TYR   B CE2  1 ? 1 
ATOM   661  C CZ   . TYR   A 1 45  ? -23.051 -4.235  10.097  1   49.521  ? 57  TYR   B CZ   1 ? 1 
ATOM   662  O OH   . TYR   A 1 45  ? -22.774 -4.519  11.395  1   49.77   ? 57  TYR   B OH   1 ? 1 
ATOM   663  H H    . TYR   A 1 45  ? -26.691 -4.216  6.663   1   60.494  ? 57  TYR   B H    1 c 1 
ATOM   664  H HA   . TYR   A 1 45  ? -25.048 -4.279  4.439   1   54.122  ? 57  TYR   B HA   1 c 1 
ATOM   665  H HB2  . TYR   A 1 45  ? -23.089 -3.68   5.401   1   47.535  ? 57  TYR   B HB2  1 c 1 
ATOM   666  H HB3  . TYR   A 1 45  ? -24.114 -2.534  5.812   1   49.087  ? 57  TYR   B HB3  1 c 1 
ATOM   667  H HD1  . TYR   A 1 45  ? -24.927 -2.42   8.183   1   52.062  ? 57  TYR   B HD1  1 c 1 
ATOM   668  H HD2  . TYR   A 1 45  ? -22.147 -5.131  7.11    1   46.409  ? 57  TYR   B HD2  1 c 1 
ATOM   669  H HE1  . TYR   A 1 45  ? -24.484 -2.839  10.425  1   52.542  ? 57  TYR   B HE1  1 c 1 
ATOM   670  H HE2  . TYR   A 1 45  ? -21.703 -5.549  9.348   1   47.729  ? 57  TYR   B HE2  1 c 1 
ATOM   671  H HH   . TYR   A 1 45  ? -23.198 -4.029  11.908  0   30      ? 57  TYR   B HH   1 c 1 
ATOM   672  N N    . LYS   A 1 46  ? -23.975 -6.445  5.023   1   53.67   ? 58  LYS   B N    1 ? 1 
ATOM   673  C CA   . LYS   A 1 46  ? -23.433 -7.75   5.342   1   53.355  ? 58  LYS   B CA   1 ? 1 
ATOM   674  C C    . LYS   A 1 46  ? -21.925 -7.595  5.244   1   51.29   ? 58  LYS   B C    1 ? 1 
ATOM   675  O O    . LYS   A 1 46  ? -21.429 -7.033  4.262   1   49.074  ? 58  LYS   B O    1 ? 1 
ATOM   676  C CB   . LYS   A 1 46  ? -24.02  -8.805  4.403   1   55.237  ? 58  LYS   B CB   1 ? 1 
ATOM   677  C CG   . LYS   A 1 46  ? -25.54  -8.952  4.5     1   59.508  ? 58  LYS   B CG   1 ? 1 
ATOM   678  C CD   . LYS   A 1 46  ? -26.088 -9.899  3.437   1   62.465  ? 58  LYS   B CD   1 ? 1 
ATOM   679  C CE   . LYS   A 1 46  ? -27.558 -9.849  3.201   1   66.662  ? 58  LYS   B CE   1 ? 1 
ATOM   680  N NZ   . LYS   A 1 46  ? -27.983 -10.756 2.117   1   70.427  ? 58  LYS   B NZ   1 ? 1 
ATOM   681  H H    . LYS   A 1 46  ? -23.723 -6.055  4.236   1   52.475  ? 58  LYS   B H    1 c 1 
ATOM   682  H HA   . LYS   A 1 46  ? -23.675 -7.975  6.276   1   54.843  ? 58  LYS   B HA   1 c 1 
ATOM   683  H HB2  . LYS   A 1 46  ? -23.786 -8.572  3.48    1   54.575  ? 58  LYS   B HB2  1 c 1 
ATOM   684  H HB3  . LYS   A 1 46  ? -23.609 -9.673  4.606   1   56.243  ? 58  LYS   B HB3  1 c 1 
ATOM   685  H HG2  . LYS   A 1 46  ? -25.771 -9.293  5.391   1   60.857  ? 58  LYS   B HG2  1 c 1 
ATOM   686  H HG3  . LYS   A 1 46  ? -25.953 -8.068  4.391   1   58.886  ? 58  LYS   B HG3  1 c 1 
ATOM   687  H HD2  . LYS   A 1 46  ? -25.634 -9.701  2.59    1   61.039  ? 58  LYS   B HD2  1 c 1 
ATOM   688  H HD3  . LYS   A 1 46  ? -25.844 -10.817 3.687   1   63.89   ? 58  LYS   B HD3  1 c 1 
ATOM   689  H HE2  . LYS   A 1 46  ? -28.024 -10.095 4.02    1   68.707  ? 58  LYS   B HE2  1 c 1 
ATOM   690  H HE3  . LYS   A 1 46  ? -27.815 -8.938  2.97    1   65.646  ? 58  LYS   B HE3  1 c 1 
ATOM   691  H HZ1  . LYS   A 1 46  ? -27.861 -11.617 2.372   1   72.068  ? 58  LYS   B HZ1  1 c 1 
ATOM   692  H HZ2  . LYS   A 1 46  ? -27.494 -10.594 1.372   1   68.812  ? 58  LYS   B HZ2  1 c 1 
ATOM   693  H HZ3  . LYS   A 1 46  ? -28.86  -10.622 1.933   1   73.126  ? 58  LYS   B HZ3  1 c 1 
ATOM   694  N N    . GLY   A 1 47  ? -21.202 -7.993  6.293   1   50.389  ? 59  GLY   B N    1 ? 1 
ATOM   695  C CA   . GLY   A 1 47  ? -19.764 -7.778  6.315   1   47.313  ? 59  GLY   B CA   1 ? 1 
ATOM   696  C C    . GLY   A 1 47  ? -19.065 -9.093  6.643   1   46.423  ? 59  GLY   B C    1 ? 1 
ATOM   697  O O    . GLY   A 1 47  ? -19.643 -9.933  7.308   1   49.753  ? 59  GLY   B O    1 ? 1 
ATOM   698  H H    . GLY   A 1 47  ? -21.605 -8.406  7.002   1   52.228  ? 59  GLY   B H    1 c 1 
ATOM   699  H HA2  . GLY   A 1 47  ? -19.463 -7.448  5.439   1   45.641  ? 59  GLY   B HA2  1 c 1 
ATOM   700  H HA3  . GLY   A 1 47  ? -19.543 -7.101  6.996   1   45.791  ? 59  GLY   B HA3  1 c 1 
ATOM   701  N N    . LYS   A 1 48  ? -17.815 -9.242  6.216   1   42.892  ? 60  LYS   B N    1 ? 1 
ATOM   702  C CA   . LYS   A 1 48  ? -17.012 -10.377 6.619   1   45.239  ? 60  LYS   B CA   1 ? 1 
ATOM   703  C C    . LYS   A 1 48  ? -15.531 -10.039 6.506   1   42.569  ? 60  LYS   B C    1 ? 1 
ATOM   704  O O    . LYS   A 1 48  ? -15.133 -9.108  5.821   1   42.264  ? 60  LYS   B O    1 ? 1 
ATOM   705  C CB   . LYS   A 1 48  ? -17.329 -11.603 5.755   1   51.146  ? 60  LYS   B CB   1 ? 1 
ATOM   706  C CG   . LYS   A 1 48  ? -17.094 -11.463 4.264   1   52.639  ? 60  LYS   B CG   1 ? 1 
ATOM   707  C CD   . LYS   A 1 48  ? -17.068 -12.814 3.524   1   58.609  ? 60  LYS   B CD   1 ? 1 
ATOM   708  C CE   . LYS   A 1 48  ? -16.504 -12.657 2.133   1   59.808  ? 60  LYS   B CE   1 ? 1 
ATOM   709  H H    . LYS   A 1 48  ? -17.451 -8.617  5.657   1   41.943  ? 60  LYS   B H    1 c 1 
ATOM   710  H HA   . LYS   A 1 48  ? -17.218 -10.584 7.565   1   46.604  ? 60  LYS   B HA   1 c 1 
ATOM   711  H HB2  . LYS   A 1 48  ? -16.789 -12.355 6.08    1   52.044  ? 60  LYS   B HB2  1 c 1 
ATOM   712  H HB3  . LYS   A 1 48  ? -18.272 -11.839 5.893   1   52.646  ? 60  LYS   B HB3  1 c 1 
ATOM   713  H HG2  . LYS   A 1 48  ? -17.805 -10.901 3.885   1   52.39   ? 60  LYS   B HG2  1 c 1 
ATOM   714  H HG3  . LYS   A 1 48  ? -16.237 -11.003 4.123   1   50.798  ? 60  LYS   B HG3  1 c 1 
ATOM   715  H HD2  . LYS   A 1 48  ? -16.517 -13.454 4.027   1   59.2    ? 60  LYS   B HD2  1 c 1 
ATOM   716  H HD3  . LYS   A 1 48  ? -17.981 -13.17  3.464   1   60.406  ? 60  LYS   B HD3  1 c 1 
ATOM   717  H HE2  . LYS   A 1 48  ? -14.894 -12.728 2.812   0   30      ? 60  LYS   B HE2  1 c 1 
ATOM   718  H HE3  . LYS   A 1 48  ? -16.162 -12.779 1.484   0   30      ? 60  LYS   B HE3  1 c 1 
ATOM   719  N N    . LEU   A 1 49  ? -14.724 -10.835 7.189   1   43.549  ? 61  LEU   B N    1 ? 1 
ATOM   720  C CA   . LEU   A 1 49  ? -13.282 -10.761 7.082   1   43.816  ? 61  LEU   B CA   1 ? 1 
ATOM   721  C C    . LEU   A 1 49  ? -12.943 -11.536 5.823   1   44.155  ? 61  LEU   B C    1 ? 1 
ATOM   722  O O    . LEU   A 1 49  ? -13.647 -12.49  5.523   1   42.789  ? 61  LEU   B O    1 ? 1 
ATOM   723  C CB   . LEU   A 1 49  ? -12.615 -11.4   8.301   1   46.801  ? 61  LEU   B CB   1 ? 1 
ATOM   724  C CG   . LEU   A 1 49  ? -13.042 -10.835 9.663   1   50.252  ? 61  LEU   B CG   1 ? 1 
ATOM   725  C CD1  . LEU   A 1 49  ? -12.424 -11.609 10.815  1   52.889  ? 61  LEU   B CD1  1 ? 1 
ATOM   726  C CD2  . LEU   A 1 49  ? -12.682 -9.377  9.712   1   49.421  ? 61  LEU   B CD2  1 ? 1 
ATOM   727  H H    . LEU   A 1 49  ? -15.088 -11.461 7.746   1   45.825  ? 61  LEU   B H    1 c 1 
ATOM   728  H HA   . LEU   A 1 49  ? -13.001 -9.815  6.99    1   41.81   ? 61  LEU   B HA   1 c 1 
ATOM   729  H HB2  . LEU   A 1 49  ? -12.816 -12.363 8.289   1   49.401  ? 61  LEU   B HB2  1 c 1 
ATOM   730  H HB3  . LEU   A 1 49  ? -11.64  -11.293 8.21    1   46.757  ? 61  LEU   B HB3  1 c 1 
ATOM   731  H HG   . LEU   A 1 49  ? -14.028 -10.912 9.737   1   50.582  ? 61  LEU   B HG   1 c 1 
ATOM   732  H HD11 . LEU   A 1 49  ? -12.586 -12.559 10.693  1   54.85   ? 61  LEU   B HD11 1 c 1 
ATOM   733  H HD12 . LEU   A 1 49  ? -12.823 -11.319 11.653  1   53.422  ? 61  LEU   B HD12 1 c 1 
ATOM   734  H HD13 . LEU   A 1 49  ? -11.466 -11.445 10.84   1   52.264  ? 61  LEU   B HD13 1 c 1 
ATOM   735  H HD21 . LEU   A 1 49  ? -13.284 -8.876  9.136   1   47.612  ? 61  LEU   B HD21 1 c 1 
ATOM   736  H HD22 . LEU   A 1 49  ? -11.767 -9.255  9.408   1   48.113  ? 61  LEU   B HD22 1 c 1 
ATOM   737  H HD23 . LEU   A 1 49  ? -12.766 -9.052  10.624  1   49.232  ? 61  LEU   B HD23 1 c 1 
ATOM   738  N N    . SER   A 1 50  ? -11.875 -11.145 5.134   1   44.992  ? 62  SER   B N    1 ? 1 
ATOM   739  C CA   . SER   A 1 50  ? -11.302 -11.965 4.062   1   52.584  ? 62  SER   B CA   1 ? 1 
ATOM   740  C C    . SER   A 1 50  ? -10.933 -13.365 4.521   1   53.352  ? 62  SER   B C    1 ? 1 
ATOM   741  O O    . SER   A 1 50  ? -11.028 -14.26  3.71    1   62.521  ? 62  SER   B O    1 ? 1 
ATOM   742  C CB   . SER   A 1 50  ? -10.091 -11.335 3.457   1   52.93   ? 62  SER   B CB   1 ? 1 
ATOM   743  O OG   . SER   A 1 50  ? -10.461 -10.055 2.999   1   62.201  ? 62  SER   B OG   1 ? 1 
ATOM   744  H H    . SER   A 1 50  ? -11.483 -10.343 5.332   1   44.094  ? 62  SER   B H    1 c 1 
ATOM   745  H HA   . SER   A 1 50  ? -11.988 -12.052 3.354   1   51.739  ? 62  SER   B HA   1 c 1 
ATOM   746  H HB2  . SER   A 1 50  ? -9.386  -11.259 4.128   1   54.853  ? 62  SER   B HB2  1 c 1 
ATOM   747  H HB3  . SER   A 1 50  ? -9.77   -11.878 2.712   1   56.535  ? 62  SER   B HB3  1 c 1 
ATOM   748  H HG   . SER   A 1 50  ? -9.84   -9.915  2.212   0   30      ? 62  SER   B HG   1 c 1 
ATOM   749  N N    . ASN   A 1 51  ? -10.577 -13.57  5.799   1   57.814  ? 63  ASN   B N    1 ? 1 
ATOM   750  C CA   . ASN   A 1 51  ? -10.19  -14.893 6.27    1   62.207  ? 63  ASN   B CA   1 ? 1 
ATOM   751  C C    . ASN   A 1 51  ? -11.403 -15.823 6.393   1   64.055  ? 63  ASN   B C    1 ? 1 
ATOM   752  O O    . ASN   A 1 51  ? -11.233 -16.987 6.724   1   66.666  ? 63  ASN   B O    1 ? 1 
ATOM   753  C CB   . ASN   A 1 51  ? -9.372  -14.832 7.555   1   63.881  ? 63  ASN   B CB   1 ? 1 
ATOM   754  C CG   . ASN   A 1 51  ? -10.201 -14.532 8.785   1   66.64   ? 63  ASN   B CG   1 ? 1 
ATOM   755  O OD1  . ASN   A 1 51  ? -11.423 -14.339 8.7     1   65.057  ? 63  ASN   B OD1  1 ? 1 
ATOM   756  N ND2  . ASN   A 1 51  ? -9.559  -14.521 9.946   1   68.034  ? 63  ASN   B ND2  1 ? 1 
ATOM   757  H H    . ASN   A 1 51  ? -10.564 -12.87  6.387   1   55.339  ? 63  ASN   B H    1 c 1 
ATOM   758  H HA   . ASN   A 1 51  ? -9.599  -15.281 5.585   1   63.199  ? 63  ASN   B HA   1 c 1 
ATOM   759  H HB2  . ASN   A 1 51  ? -8.918  -15.688 7.682   1   66.775  ? 63  ASN   B HB2  1 c 1 
ATOM   760  H HB3  . ASN   A 1 51  ? -8.686  -14.141 7.461   1   62.647  ? 63  ASN   B HB3  1 c 1 
ATOM   761  H HD21 . ASN   A 1 51  ? -9.98   -14.255 10.68   1   67.878  ? 63  ASN   B HD21 1 c 1 
ATOM   762  H HD22 . ASN   A 1 51  ? -8.712  -14.779 9.988   1   68.83   ? 63  ASN   B HD22 1 c 1 
ATOM   763  N N    . GLY   A 1 52  ? -12.62  -15.303 6.179   1   64.311  ? 64  GLY   B N    1 ? 1 
ATOM   764  C CA   . GLY   A 1 52  ? -13.82  -16.134 6.128   1   67.602  ? 64  GLY   B CA   1 ? 1 
ATOM   765  C C    . GLY   A 1 52  ? -14.288 -16.658 7.497   1   70.605  ? 64  GLY   B C    1 ? 1 
ATOM   766  O O    . GLY   A 1 52  ? -15.087 -17.587 7.56    1   78.274  ? 64  GLY   B O    1 ? 1 
ATOM   767  H H    . GLY   A 1 52  ? -12.713 -14.4   6.085   1   61.404  ? 64  GLY   B H    1 c 1 
ATOM   768  H HA2  . GLY   A 1 52  ? -14.548 -15.606 5.722   1   66.53   ? 64  GLY   B HA2  1 c 1 
ATOM   769  H HA3  . GLY   A 1 52  ? -13.645 -16.901 5.534   1   69.855  ? 64  GLY   B HA3  1 c 1 
ATOM   770  N N    . LYS   A 1 53  ? -13.802 -16.085 8.604   1   68.969  ? 65  LYS   B N    1 ? 1 
ATOM   771  C CA   . LYS   A 1 53  ? -14.044 -16.656 9.927   1   72.634  ? 65  LYS   B CA   1 ? 1 
ATOM   772  C C    . LYS   A 1 53  ? -15.065 -15.824 10.722  1   70.47   ? 65  LYS   B C    1 ? 1 
ATOM   773  O O    . LYS   A 1 53  ? -15.542 -16.284 11.758  1   74.162  ? 65  LYS   B O    1 ? 1 
ATOM   774  C CB   . LYS   A 1 53  ? -12.706 -16.911 10.647  1   71.843  ? 65  LYS   B CB   1 ? 1 
ATOM   775  H H    . LYS   A 1 53  ? -13.309 -15.318 8.537   1   66.494  ? 65  LYS   B H    1 c 1 
ATOM   776  H HA   . LYS   A 1 53  ? -14.447 -17.551 9.794   1   75.119  ? 65  LYS   B HA   1 c 1 
ATOM   777  H HB2  . LYS   A 1 53  ? -11.998 -16.723 9.937   0   30      ? 65  LYS   B HB2  1 c 1 
ATOM   778  H HB3  . LYS   A 1 53  ? -12.903 -17.48  11.373  0   30      ? 65  LYS   B HB3  1 c 1 
ATOM   779  N N    . LYS   A 1 54  ? -15.418 -14.613 10.264  1   67.506  ? 66  LYS   B N    1 ? 1 
ATOM   780  C CA   . LYS   A 1 54  ? -16.429 -13.799 10.942  1   65.32   ? 66  LYS   B CA   1 ? 1 
ATOM   781  C C    . LYS   A 1 54  ? -17.346 -13.153 9.902   1   62.449  ? 66  LYS   B C    1 ? 1 
ATOM   782  O O    . LYS   A 1 54  ? -16.866 -12.67  8.874   1   59.027  ? 66  LYS   B O    1 ? 1 
ATOM   783  C CB   . LYS   A 1 54  ? -15.826 -12.733 11.87   1   60.752  ? 66  LYS   B CB   1 ? 1 
ATOM   784  H H    . LYS   A 1 54  ? -15.018 -14.279 9.514   1   64.862  ? 66  LYS   B H    1 c 1 
ATOM   785  H HA   . LYS   A 1 54  ? -16.98  -14.401 11.502  1   67.997  ? 66  LYS   B HA   1 c 1 
ATOM   786  H HB2  . LYS   A 1 54  ? -14.869 -12.848 11.94   0   30      ? 66  LYS   B HB2  1 c 1 
ATOM   787  H HB3  . LYS   A 1 54  ? -16.593 -12.351 12.422  0   30      ? 66  LYS   B HB3  1 c 1 
ATOM   788  N N    . PHE   A 1 55  ? -18.658 -13.185 10.181  1   60.864  ? 67  PHE   B N    1 ? 1 
ATOM   789  C CA   . PHE   A 1 55  ? -19.69  -12.544 9.376   1   61.071  ? 67  PHE   B CA   1 ? 1 
ATOM   790  C C    . PHE   A 1 55  ? -20.645 -11.778 10.279  1   63.334  ? 67  PHE   B C    1 ? 1 
ATOM   791  O O    . PHE   A 1 55  ? -21.003 -12.235 11.366  1   67.171  ? 67  PHE   B O    1 ? 1 
ATOM   792  C CB   . PHE   A 1 55  ? -20.589 -13.501 8.603   1   64.347  ? 67  PHE   B CB   1 ? 1 
ATOM   793  C CG   . PHE   A 1 55  ? -19.736 -14.544 7.921   1   68.965  ? 67  PHE   B CG   1 ? 1 
ATOM   794  C CD1  . PHE   A 1 55  ? -19.164 -15.59  8.648   1   74.062  ? 67  PHE   B CD1  1 ? 1 
ATOM   795  C CD2  . PHE   A 1 55  ? -19.483 -14.454 6.56    1   70.832  ? 67  PHE   B CD2  1 ? 1 
ATOM   796  C CE1  . PHE   A 1 55  ? -18.368 -16.535 8.015   1   79.522  ? 67  PHE   B CE1  1 ? 1 
ATOM   797  C CE2  . PHE   A 1 55  ? -18.703 -15.416 5.924   1   74.441  ? 67  PHE   B CE2  1 ? 1 
ATOM   798  C CZ   . PHE   A 1 55  ? -18.14  -16.45  6.65    1   77.729  ? 67  PHE   B CZ   1 ? 1 
ATOM   799  H H    . PHE   A 1 55  ? -18.925 -13.641 10.927  1   64.546  ? 67  PHE   B H    1 c 1 
ATOM   800  H HA   . PHE   A 1 55  ? -19.262 -11.914 8.741   1   58.265  ? 67  PHE   B HA   1 c 1 
ATOM   801  H HB2  . PHE   A 1 55  ? -21.211 -13.94  9.225   1   68.275  ? 67  PHE   B HB2  1 c 1 
ATOM   802  H HB3  . PHE   A 1 55  ? -21.098 -12.998 7.93    1   64.451  ? 67  PHE   B HB3  1 c 1 
ATOM   803  H HD1  . PHE   A 1 55  ? -19.32  -15.654 9.577   1   75.663  ? 67  PHE   B HD1  1 c 1 
ATOM   804  H HD2  . PHE   A 1 55  ? -19.868 -13.753 6.058   1   69.019  ? 67  PHE   B HD2  1 c 1 
ATOM   805  H HE1  . PHE   A 1 55  ? -17.994 -17.245 8.512   1   80.414  ? 67  PHE   B HE1  1 c 1 
ATOM   806  H HE2  . PHE   A 1 55  ? -18.54  -15.35  4.996   1   73.411  ? 67  PHE   B HE2  1 c 1 
ATOM   807  H HZ   . PHE   A 1 55  ? -17.602 -17.094 6.218   1   78.753  ? 67  PHE   B HZ   1 c 1 
ATOM   808  N N    . ASP   A 1 56  ? -21.121 -10.653 9.775   1   60.384  ? 68  ASP   B N    1 ? 1 
ATOM   809  C CA   . ASP   A 1 56  ? -21.952 -9.782  10.575  1   63.208  ? 68  ASP   B CA   1 ? 1 
ATOM   810  C C    . ASP   A 1 56  ? -22.943 -9.113  9.639   1   61.007  ? 68  ASP   B C    1 ? 1 
ATOM   811  O O    . ASP   A 1 56  ? -22.554 -8.637  8.589   1   53.513  ? 68  ASP   B O    1 ? 1 
ATOM   812  C CB   . ASP   A 1 56  ? -21.083 -8.752  11.288  1   64.146  ? 68  ASP   B CB   1 ? 1 
ATOM   813  C CG   . ASP   A 1 56  ? -21.829 -7.611  11.967  1   66.237  ? 68  ASP   B CG   1 ? 1 
ATOM   814  O OD1  . ASP   A 1 56  ? -22.723 -7.907  12.775  1   71.151  ? 68  ASP   B OD1  1 ? 1 
ATOM   815  O OD2  . ASP   A 1 56  ? -21.501 -6.447  11.673  1   61.447  ? 68  ASP   B OD2  1 ? 1 
ATOM   816  H H    . ASP   A 1 56  ? -20.928 -10.419 8.913   1   59.241  ? 68  ASP   B H    1 c 1 
ATOM   817  H HA   . ASP   A 1 56  ? -22.441 -10.32  11.237  1   66.112  ? 68  ASP   B HA   1 c 1 
ATOM   818  H HB2  . ASP   A 1 56  ? -20.548 -9.213  11.968  1   64.338  ? 68  ASP   B HB2  1 c 1 
ATOM   819  H HB3  . ASP   A 1 56  ? -20.466 -8.365  10.633  1   60.752  ? 68  ASP   B HB3  1 c 1 
ATOM   820  N N    . SER   A 1 57  ? -24.205 -9.044  10.044  1   64.095  ? 69  SER   B N    1 ? 1 
ATOM   821  C CA   . SER   A 1 57  ? -25.216 -8.389  9.244   1   67.68   ? 69  SER   B CA   1 ? 1 
ATOM   822  C C    . SER   A 1 57  ? -26.057 -7.483  10.125  1   71.389  ? 69  SER   B C    1 ? 1 
ATOM   823  O O    . SER   A 1 57  ? -26.386 -7.837  11.257  1   77.207  ? 69  SER   B O    1 ? 1 
ATOM   824  C CB   . SER   A 1 57  ? -26.092 -9.375  8.545   1   74.558  ? 69  SER   B CB   1 ? 1 
ATOM   825  O OG   . SER   A 1 57  ? -27.152 -8.684  7.899   1   82.262  ? 69  SER   B OG   1 ? 1 
ATOM   826  H H    . SER   A 1 57  ? -24.446 -9.416  10.844  1   67.257  ? 69  SER   B H    1 c 1 
ATOM   827  H HA   . SER   A 1 57  ? -24.765 -7.831  8.564   1   64.984  ? 69  SER   B HA   1 c 1 
ATOM   828  H HB2  . SER   A 1 57  ? -25.569 -9.869  7.885   1   74.139  ? 69  SER   B HB2  1 c 1 
ATOM   829  H HB3  . SER   A 1 57  ? -26.457 -10.008 9.193   1   78.254  ? 69  SER   B HB3  1 c 1 
ATOM   830  H HG   . SER   A 1 57  ? -27.741 -9.414  7.609   0   30      ? 69  SER   B HG   1 c 1 
ATOM   831  N N    . SER   A 1 58  ? -26.454 -6.338  9.57    1   70.433  ? 70  SER   B N    1 ? 1 
ATOM   832  C CA   . SER   A 1 58  ? -27.401 -5.477  10.253  1   72.552  ? 70  SER   B CA   1 ? 1 
ATOM   833  C C    . SER   A 1 58  ? -28.654 -6.288  10.583  1   79.185  ? 70  SER   B C    1 ? 1 
ATOM   834  O O    . SER   A 1 58  ? -29.186 -6.174  11.689  1   85.351  ? 70  SER   B O    1 ? 1 
ATOM   835  C CB   . SER   A 1 58  ? -27.705 -4.253  9.444   1   68.44   ? 70  SER   B CB   1 ? 1 
ATOM   836  O OG   . SER   A 1 58  ? -28.015 -4.621  8.111   1   66.602  ? 70  SER   B OG   1 ? 1 
ATOM   837  H H    . SER   A 1 58  ? -26.132 -6.088  8.752   1   68.054  ? 70  SER   B H    1 c 1 
ATOM   838  H HA   . SER   A 1 58  ? -26.99  -5.189  11.107  1   71.832  ? 70  SER   B HA   1 c 1 
ATOM   839  H HB2  . SER   A 1 58  ? -28.462 -3.78   9.838   1   70.969  ? 70  SER   B HB2  1 c 1 
ATOM   840  H HB3  . SER   A 1 58  ? -26.931 -3.659  9.448   1   65.567  ? 70  SER   B HB3  1 c 1 
ATOM   841  H HG   . SER   A 1 58  ? -28.175 -3.975  7.667   0   30      ? 70  SER   B HG   1 c 1 
ATOM   842  N N    . HIS   A 1 59  ? -29.076 -7.144  9.639   1   79.812  ? 71  HIS   B N    1 ? 1 
ATOM   843  C CA   . HIS   A 1 59  ? -30.287 -7.954  9.773   1   87.967  ? 71  HIS   B CA   1 ? 1 
ATOM   844  C C    . HIS   A 1 59  ? -30.273 -8.843  11.022  1   91.136  ? 71  HIS   B C    1 ? 1 
ATOM   845  O O    . HIS   A 1 59  ? -31.319 -9.131  11.589  1   91.549  ? 71  HIS   B O    1 ? 1 
ATOM   846  C CB   . HIS   A 1 59  ? -30.505 -8.802  8.515   1   88.386  ? 71  HIS   B CB   1 ? 1 
ATOM   847  C CG   . HIS   A 1 59  ? -30.714 -8.011  7.265   1   86.79   ? 71  HIS   B CG   1 ? 1 
ATOM   848  N ND1  . HIS   A 1 59  ? -31.895 -7.352  6.991   1   89.95   ? 71  HIS   B ND1  1 ? 1 
ATOM   849  C CD2  . HIS   A 1 59  ? -29.89  -7.749  6.232   1   83.646  ? 71  HIS   B CD2  1 ? 1 
ATOM   850  C CE1  . HIS   A 1 59  ? -31.783 -6.729  5.823   1   88.749  ? 71  HIS   B CE1  1 ? 1 
ATOM   851  N NE2  . HIS   A 1 59  ? -30.575 -6.965  5.34    1   84.38   ? 71  HIS   B NE2  1 ? 1 
ATOM   852  H H    . HIS   A 1 59  ? -28.589 -7.222  8.87    1   78.111  ? 71  HIS   B H    1 c 1 
ATOM   853  H HA   . HIS   A 1 59  ? -31.048 -7.327  9.854   1   89.255  ? 71  HIS   B HA   1 c 1 
ATOM   854  H HB2  . HIS   A 1 59  ? -29.726 -9.387  8.393   1   86.81   ? 71  HIS   B HB2  1 c 1 
ATOM   855  H HB3  . HIS   A 1 59  ? -31.287 -9.379  8.659   1   93.042  ? 71  HIS   B HB3  1 c 1 
ATOM   856  H HD1  . HIS   A 1 59  ? -32.669 -7.461  7.47    0   30      ? 71  HIS   B HD1  1 c 1 
ATOM   857  H HD2  . HIS   A 1 59  ? -29.013 -8.06   6.124   1   80.819  ? 71  HIS   B HD2  1 c 1 
ATOM   858  H HE1  . HIS   A 1 59  ? -32.455 -6.215  5.408   1   90.221  ? 71  HIS   B HE1  1 c 1 
ATOM   859  H HE2  . HIS   A 1 59  ? -30.195 -6.606  4.689   0   30      ? 71  HIS   B HE2  1 c 1 
ATOM   860  N N    . ASP   A 1 60  ? -29.077 -9.27   11.448  1   92.776  ? 72  ASP   B N    1 ? 1 
ATOM   861  C CA   . ASP   A 1 60  ? -28.88  -10.012 12.689  1   97.016  ? 72  ASP   B CA   1 ? 1 
ATOM   862  C C    . ASP   A 1 60  ? -29.476 -9.276  13.89   1   98.325  ? 72  ASP   B C    1 ? 1 
ATOM   863  O O    . ASP   A 1 60  ? -29.762 -9.9    14.896  1   101.223 ? 72  ASP   B O    1 ? 1 
ATOM   864  C CB   . ASP   A 1 60  ? -27.403 -10.268 12.956  1   93.617  ? 72  ASP   B CB   1 ? 1 
ATOM   865  H H    . ASP   A 1 60  ? -28.345 -9.101  10.927  1   88.086  ? 72  ASP   B H    1 c 1 
ATOM   866  H HA   . ASP   A 1 60  ? -29.329 -10.883 12.601  1   100.118 ? 72  ASP   B HA   1 c 1 
ATOM   867  H HB2  . ASP   A 1 60  ? -26.875 -9.715  12.342  0   30      ? 72  ASP   B HB2  1 c 1 
ATOM   868  H HB3  . ASP   A 1 60  ? -27.303 -10.784 13.797  0   30      ? 72  ASP   B HB3  1 c 1 
ATOM   869  N N    . ARG   A 1 61  ? -29.589 -7.944  13.804  1   97.013  ? 73  ARG   B N    1 ? 1 
ATOM   870  C CA   . ARG   A 1 61  ? -30.125 -7.108  14.872  1   97.608  ? 73  ARG   B CA   1 ? 1 
ATOM   871  C C    . ARG   A 1 61  ? -31.556 -6.656  14.545  1   98.053  ? 73  ARG   B C    1 ? 1 
ATOM   872  O O    . ARG   A 1 61  ? -32.102 -5.8    15.232  1   100.533 ? 73  ARG   B O    1 ? 1 
ATOM   873  C CB   . ARG   A 1 61  ? -29.148 -5.929  15.056  1   91.139  ? 73  ARG   B CB   1 ? 1 
ATOM   874  H H    . ARG   A 1 61  ? -29.296 -7.531  13.045  1   92.845  ? 73  ARG   B H    1 c 1 
ATOM   875  H HA   . ARG   A 1 61  ? -30.144 -7.636  15.709  1   100.041 ? 73  ARG   B HA   1 c 1 
ATOM   876  H HB2  . ARG   A 1 61  ? -28.3   -6.277  15.161  0   30      ? 73  ARG   B HB2  1 c 1 
ATOM   877  H HB3  . ARG   A 1 61  ? -29.761 -5.163  15.446  0   30      ? 73  ARG   B HB3  1 c 1 
ATOM   878  N N    . ASN   A 1 62  ? -32.155 -7.225  13.488  1   96.223  ? 74  ASN   B N    1 ? 1 
ATOM   879  C CA   . ASN   A 1 62  ? -33.492 -6.878  13.023  1   97.978  ? 74  ASN   B CA   1 ? 1 
ATOM   880  C C    . ASN   A 1 62  ? -33.7   -5.362  13.059  1   96.845  ? 74  ASN   B C    1 ? 1 
ATOM   881  O O    . ASN   A 1 62  ? -34.723 -4.905  13.543  1   104.333 ? 74  ASN   B O    1 ? 1 
ATOM   882  C CB   . ASN   A 1 62  ? -34.571 -7.676  13.77   1   104.291 ? 74  ASN   B CB   1 ? 1 
ATOM   883  H H    . ASN   A 1 62  ? -31.706 -7.877  13.034  1   94.908  ? 74  ASN   B H    1 c 1 
ATOM   884  H HA   . ASN   A 1 62  ? -33.548 -7.151  12.08   1   97.164  ? 74  ASN   B HA   1 c 1 
ATOM   885  H HB2  . ASN   A 1 62  ? -34.067 -8.449  14.208  0   30      ? 74  ASN   B HB2  1 c 1 
ATOM   886  H HB3  . ASN   A 1 62  ? -35.405 -7.468  13.395  0   30      ? 74  ASN   B HB3  1 c 1 
ATOM   887  N N    . GLU   A 1 63  ? -32.742 -4.567  12.542  1   93.728  ? 75  GLU   B N    1 ? 1 
ATOM   888  C CA   . GLU   A 1 63  ? -32.934 -3.124  12.422  1   91.963  ? 75  GLU   B CA   1 ? 1 
ATOM   889  C C    . GLU   A 1 63  ? -31.792 -2.489  11.621  1   83.491  ? 75  GLU   B C    1 ? 1 
ATOM   890  O O    . GLU   A 1 63  ? -30.664 -2.983  11.638  1   79.083  ? 75  GLU   B O    1 ? 1 
ATOM   891  C CB   . GLU   A 1 63  ? -33.024 -2.437  13.788  1   95.301  ? 75  GLU   B CB   1 ? 1 
ATOM   892  C CG   . GLU   A 1 63  ? -31.693 -2.411  14.535  1   92.467  ? 75  GLU   B CG   1 ? 1 
ATOM   893  C CD   . GLU   A 1 63  ? -31.686 -1.482  15.731  1   94.183  ? 75  GLU   B CD   1 ? 1 
ATOM   894  O OE1  . GLU   A 1 63  ? -30.558 -1.051  16.077  1   91.364  ? 75  GLU   B OE1  1 ? 1 
ATOM   895  O OE2  . GLU   A 1 63  ? -32.772 -1.185  16.286  1   97.166  ? 75  GLU   B OE2  1 ? 1 
ATOM   896  H H    . GLU   A 1 63  ? -31.955 -4.934  12.255  1   89.472  ? 75  GLU   B H    1 c 1 
ATOM   897  H HA   . GLU   A 1 63  ? -33.784 -2.97   11.942  1   94.655  ? 75  GLU   B HA   1 c 1 
ATOM   898  H HB2  . GLU   A 1 63  ? -33.33  -1.516  13.658  1   95.614  ? 75  GLU   B HB2  1 c 1 
ATOM   899  H HB3  . GLU   A 1 63  ? -33.689 -2.897  14.339  1   99.792  ? 75  GLU   B HB3  1 c 1 
ATOM   900  H HG2  . GLU   A 1 63  ? -31.479 -3.317  14.842  1   92.793  ? 75  GLU   B HG2  1 c 1 
ATOM   901  H HG3  . GLU   A 1 63  ? -30.982 -2.129  13.924  1   87.764  ? 75  GLU   B HG3  1 c 1 
ATOM   902  N N    . PRO   A 1 64  ? -32.03  -1.364  10.9    1   81.564  ? 76  PRO   B N    1 ? 1 
ATOM   903  C CA   . PRO   A 1 64  ? -30.968 -0.696  10.161  1   76.183  ? 76  PRO   B CA   1 ? 1 
ATOM   904  C C    . PRO   A 1 64  ? -29.793 -0.307  11.05   1   72.601  ? 76  PRO   B C    1 ? 1 
ATOM   905  O O    . PRO   A 1 64  ? -29.951 -0.143  12.255  1   74.187  ? 76  PRO   B O    1 ? 1 
ATOM   906  C CB   . PRO   A 1 64  ? -31.6   0.576   9.603   1   76.55   ? 76  PRO   B CB   1 ? 1 
ATOM   907  C CG   . PRO   A 1 64  ? -33.091 0.412   9.772   1   84.616  ? 76  PRO   B CG   1 ? 1 
ATOM   908  C CD   . PRO   A 1 64  ? -33.328 -0.675  10.789  1   87.697  ? 76  PRO   B CD   1 ? 1 
ATOM   909  H HA   . PRO   A 1 64  ? -30.66  -1.272  9.43    1   74.159  ? 76  PRO   B HA   1 c 1 
ATOM   910  H HB2  . PRO   A 1 64  ? -31.285 1.362   10.091  1   76.49   ? 76  PRO   B HB2  1 c 1 
ATOM   911  H HB3  . PRO   A 1 64  ? -31.372 0.689   8.66    1   75.214  ? 76  PRO   B HB3  1 c 1 
ATOM   912  H HG2  . PRO   A 1 64  ? -33.492 1.25    10.078  1   86.096  ? 76  PRO   B HG2  1 c 1 
ATOM   913  H HG3  . PRO   A 1 64  ? -33.504 0.168   8.92    1   84.974  ? 76  PRO   B HG3  1 c 1 
ATOM   914  H HD2  . PRO   A 1 64  ? -33.592 -0.298  11.651  1   89.65   ? 76  PRO   B HD2  1 c 1 
ATOM   915  H HD3  . PRO   A 1 64  ? -34.021 -1.293  10.485  1   90.224  ? 76  PRO   B HD3  1 c 1 
ATOM   916  N N    . PHE   A 1 65  ? -28.631 -0.147  10.424  1   67.689  ? 77  PHE   B N    1 ? 1 
ATOM   917  C CA   . PHE   A 1 65  ? -27.454 0.442   11.027  1   67.735  ? 77  PHE   B CA   1 ? 1 
ATOM   918  C C    . PHE   A 1 65  ? -27.426 1.932   10.686  1   69.354  ? 77  PHE   B C    1 ? 1 
ATOM   919  O O    . PHE   A 1 65  ? -27.497 2.311   9.512   1   70.399  ? 77  PHE   B O    1 ? 1 
ATOM   920  C CB   . PHE   A 1 65  ? -26.209 -0.282  10.5    1   65.195  ? 77  PHE   B CB   1 ? 1 
ATOM   921  C CG   . PHE   A 1 65  ? -24.925 0.233   11.12   1   63.096  ? 77  PHE   B CG   1 ? 1 
ATOM   922  C CD1  . PHE   A 1 65  ? -24.502 -0.22   12.37   1   66.04   ? 77  PHE   B CD1  1 ? 1 
ATOM   923  C CD2  . PHE   A 1 65  ? -24.164 1.197   10.47   1   61.394  ? 77  PHE   B CD2  1 ? 1 
ATOM   924  C CE1  . PHE   A 1 65  ? -23.35  0.28    12.95   1   63.631  ? 77  PHE   B CE1  1 ? 1 
ATOM   925  C CE2  . PHE   A 1 65  ? -23.016 1.695   11.055  1   57.972  ? 77  PHE   B CE2  1 ? 1 
ATOM   926  C CZ   . PHE   A 1 65  ? -22.606 1.234   12.286  1   61.475  ? 77  PHE   B CZ   1 ? 1 
ATOM   927  H H    . PHE   A 1 65  ? -28.569 -0.426  9.556   1   67.155  ? 77  PHE   B H    1 c 1 
ATOM   928  H HA   . PHE   A 1 65  ? -27.501 0.329   12.014  1   69.476  ? 77  PHE   B HA   1 c 1 
ATOM   929  H HB2  . PHE   A 1 65  ? -26.296 -1.242  10.691  1   65.762  ? 77  PHE   B HB2  1 c 1 
ATOM   930  H HB3  . PHE   A 1 65  ? -26.165 -0.164  9.525   1   63.578  ? 77  PHE   B HB3  1 c 1 
ATOM   931  H HD1  . PHE   A 1 65  ? -25.015 -0.867  12.828  1   67.645  ? 77  PHE   B HD1  1 c 1 
ATOM   932  H HD2  . PHE   A 1 65  ? -24.443 1.524   9.629   1   60.41   ? 77  PHE   B HD2  1 c 1 
ATOM   933  H HE1  . PHE   A 1 65  ? -23.068 -0.04   13.792  1   64.864  ? 77  PHE   B HE1  1 c 1 
ATOM   934  H HE2  . PHE   A 1 65  ? -22.501 2.343   10.6    1   57.528  ? 77  PHE   B HE2  1 c 1 
ATOM   935  H HZ   . PHE   A 1 65  ? -21.813 1.567   12.674  1   59.923  ? 77  PHE   B HZ   1 c 1 
ATOM   936  N N    . VAL   A 1 66  ? -27.333 2.769   11.729  1   71.101  ? 78  VAL   B N    1 ? 1 
ATOM   937  C CA   . VAL   A 1 66  ? -27.4   4.211   11.575  1   69.358  ? 78  VAL   B CA   1 ? 1 
ATOM   938  C C    . VAL   A 1 66  ? -26.1   4.818   12.079  1   66.004  ? 78  VAL   B C    1 ? 1 
ATOM   939  O O    . VAL   A 1 66  ? -25.533 4.354   13.065  1   67.365  ? 78  VAL   B O    1 ? 1 
ATOM   940  C CB   . VAL   A 1 66  ? -28.608 4.76    12.335  1   76.62   ? 78  VAL   B CB   1 ? 1 
ATOM   941  C CG1  . VAL   A 1 66  ? -28.774 6.254   12.097  1   79.182  ? 78  VAL   B CG1  1 ? 1 
ATOM   942  C CG2  . VAL   A 1 66  ? -29.886 3.995   11.992  1   79.32   ? 78  VAL   B CG2  1 ? 1 
ATOM   943  H H    . VAL   A 1 66  ? -27.221 2.425   12.569  1   71.462  ? 78  VAL   B H    1 c 1 
ATOM   944  H HA   . VAL   A 1 66  ? -27.502 4.422   10.63   1   68.953  ? 78  VAL   B HA   1 c 1 
ATOM   945  H HB   . VAL   A 1 66  ? -28.429 4.628   13.296  1   77.51   ? 78  VAL   B HB   1 c 1 
ATOM   946  H HG11 . VAL   A 1 66  ? -28.81  6.429   11.142  1   77.541  ? 78  VAL   B HG11 1 c 1 
ATOM   947  H HG12 . VAL   A 1 66  ? -28.022 6.732   12.486  1   77.695  ? 78  VAL   B HG12 1 c 1 
ATOM   948  H HG13 . VAL   A 1 66  ? -29.598 6.558   12.513  1   82.484  ? 78  VAL   B HG13 1 c 1 
ATOM   949  H HG21 . VAL   A 1 66  ? -30.651 4.445   12.389  1   83.049  ? 78  VAL   B HG21 1 c 1 
ATOM   950  H HG22 . VAL   A 1 66  ? -29.828 3.089   12.341  1   79.489  ? 78  VAL   B HG22 1 c 1 
ATOM   951  H HG23 . VAL   A 1 66  ? -29.996 3.962   11.027  1   78.24   ? 78  VAL   B HG23 1 c 1 
ATOM   952  N N    . PHE   A 1 67  ? -25.598 5.823   11.363  1   62.114  ? 79  PHE   B N    1 ? 1 
ATOM   953  C CA   . PHE   A 1 67  ? -24.382 6.494   11.786  1   59.625  ? 79  PHE   B CA   1 ? 1 
ATOM   954  C C    . PHE   A 1 67  ? -24.318 7.864   11.118  1   62.318  ? 79  PHE   B C    1 ? 1 
ATOM   955  O O    . PHE   A 1 67  ? -25.037 8.117   10.146  1   61.842  ? 79  PHE   B O    1 ? 1 
ATOM   956  C CB   . PHE   A 1 67  ? -23.143 5.668   11.463  1   56.775  ? 79  PHE   B CB   1 ? 1 
ATOM   957  C CG   . PHE   A 1 67  ? -22.765 5.653   9.986   1   53.269  ? 79  PHE   B CG   1 ? 1 
ATOM   958  C CD1  . PHE   A 1 67  ? -23.422 4.819   9.084   1   51.535  ? 79  PHE   B CD1  1 ? 1 
ATOM   959  C CD2  . PHE   A 1 67  ? -21.725 6.454   9.515   1   51.412  ? 79  PHE   B CD2  1 ? 1 
ATOM   960  C CE1  . PHE   A 1 67  ? -23.065 4.801   7.749   1   50      ? 79  PHE   B CE1  1 ? 1 
ATOM   961  C CE2  . PHE   A 1 67  ? -21.377 6.434   8.168   1   48.135  ? 79  PHE   B CE2  1 ? 1 
ATOM   962  C CZ   . PHE   A 1 67  ? -22.047 5.633   7.293   1   48.286  ? 79  PHE   B CZ   1 ? 1 
ATOM   963  H H    . PHE   A 1 67  ? -26.017 6.097   10.598  1   62.686  ? 79  PHE   B H    1 c 1 
ATOM   964  H HA   . PHE   A 1 67  ? -24.423 6.627   12.771  1   62.351  ? 79  PHE   B HA   1 c 1 
ATOM   965  H HB2  . PHE   A 1 67  ? -22.387 6.027   11.979  1   56.068  ? 79  PHE   B HB2  1 c 1 
ATOM   966  H HB3  . PHE   A 1 67  ? -23.295 4.744   11.76   1   56.268  ? 79  PHE   B HB3  1 c 1 
ATOM   967  H HD1  . PHE   A 1 67  ? -24.124 4.266   9.389   1   53.282  ? 79  PHE   B HD1  1 c 1 
ATOM   968  H HD2  . PHE   A 1 67  ? -21.266 7.025   10.111  1   51.834  ? 79  PHE   B HD2  1 c 1 
ATOM   969  H HE1  . PHE   A 1 67  ? -23.528 4.244   7.144   1   49.921  ? 79  PHE   B HE1  1 c 1 
ATOM   970  H HE2  . PHE   A 1 67  ? -20.681 6.99    7.857   1   48.098  ? 79  PHE   B HE2  1 c 1 
ATOM   971  H HZ   . PHE   A 1 67  ? -21.797 5.616   6.383   1   47.31   ? 79  PHE   B HZ   1 c 1 
ATOM   972  N N    . SER   A 1 68  ? -23.47  8.745   11.666  1   59.681  ? 80  SER   B N    1 ? 1 
ATOM   973  C CA   . SER   A 1 68  ? -23.337 10.097  11.142  1   64.161  ? 80  SER   B CA   1 ? 1 
ATOM   974  C C    . SER   A 1 68  ? -22.089 10.141  10.267  1   60.212  ? 80  SER   B C    1 ? 1 
ATOM   975  O O    . SER   A 1 68  ? -20.996 9.821   10.735  1   58.717  ? 80  SER   B O    1 ? 1 
ATOM   976  C CB   . SER   A 1 68  ? -23.305 11.147  12.228  1   67.23   ? 80  SER   B CB   1 ? 1 
ATOM   977  O OG   . SER   A 1 68  ? -24.621 11.512  12.645  1   74.746  ? 80  SER   B OG   1 ? 1 
ATOM   978  H H    . SER   A 1 68  ? -22.961 8.496   12.384  1   60.892  ? 80  SER   B H    1 c 1 
ATOM   979  H HA   . SER   A 1 68  ? -24.121 10.279  10.568  1   64.359  ? 80  SER   B HA   1 c 1 
ATOM   980  H HB2  . SER   A 1 68  ? -22.809 10.802  12.994  1   67.904  ? 80  SER   B HB2  1 c 1 
ATOM   981  H HB3  . SER   A 1 68  ? -22.84  11.939  11.898  1   68.496  ? 80  SER   B HB3  1 c 1 
ATOM   982  H HG   . SER   A 1 68  ? -24.598 12.2    13.063  0   30      ? 80  SER   B HG   1 c 1 
ATOM   983  N N    . LEU   A 1 69  ? -22.283 10.481  8.986   1   58.661  ? 81  LEU   B N    1 ? 1 
ATOM   984  C CA   . LEU   A 1 69  ? -21.238 10.332  7.993   1   57.619  ? 81  LEU   B CA   1 ? 1 
ATOM   985  C C    . LEU   A 1 69  ? -20.11  11.317  8.269   1   57.751  ? 81  LEU   B C    1 ? 1 
ATOM   986  O O    . LEU   A 1 69  ? -20.357 12.502  8.489   1   56.689  ? 81  LEU   B O    1 ? 1 
ATOM   987  C CB   . LEU   A 1 69  ? -21.794 10.563  6.595   1   60.368  ? 81  LEU   B CB   1 ? 1 
ATOM   988  C CG   . LEU   A 1 69  ? -20.809 10.28   5.456   1   60.487  ? 81  LEU   B CG   1 ? 1 
ATOM   989  C CD1  . LEU   A 1 69  ? -20.538 8.792   5.307   1   55.757  ? 81  LEU   B CD1  1 ? 1 
ATOM   990  C CD2  . LEU   A 1 69  ? -21.367 10.755  4.147   1   66.921  ? 81  LEU   B CD2  1 ? 1 
ATOM   991  H H    . LEU   A 1 69  ? -23.091 10.821  8.727   1   61.15   ? 81  LEU   B H    1 c 1 
ATOM   992  H HA   . LEU   A 1 69  ? -20.883 9.41    8.055   1   55.404  ? 81  LEU   B HA   1 c 1 
ATOM   993  H HB2  . LEU   A 1 69  ? -22.583 9.985   6.477   1   60.456  ? 81  LEU   B HB2  1 c 1 
ATOM   994  H HB3  . LEU   A 1 69  ? -22.088 11.501  6.529   1   62.784  ? 81  LEU   B HB3  1 c 1 
ATOM   995  H HG   . LEU   A 1 69  ? -19.956 10.753  5.636   1   60.511  ? 81  LEU   B HG   1 c 1 
ATOM   996  H HD11 . LEU   A 1 69  ? -20.095 8.46    6.105   1   55.259  ? 81  LEU   B HD11 1 c 1 
ATOM   997  H HD12 . LEU   A 1 69  ? -19.966 8.641   4.535   1   55.208  ? 81  LEU   B HD12 1 c 1 
ATOM   998  H HD13 . LEU   A 1 69  ? -21.378 8.319   5.183   1   56.563  ? 81  LEU   B HD13 1 c 1 
ATOM   999  H HD21 . LEU   A 1 69  ? -21.591 11.699  4.211   1   67.638  ? 81  LEU   B HD21 1 c 1 
ATOM   1000 H HD22 . LEU   A 1 69  ? -22.166 10.246  3.937   1   65.429  ? 81  LEU   B HD22 1 c 1 
ATOM   1001 H HD23 . LEU   A 1 69  ? -20.707 10.626  3.446   1   64.173  ? 81  LEU   B HD23 1 c 1 
ATOM   1002 N N    . GLY   A 1 70  ? -18.882 10.798  8.254   1   58.291  ? 82  GLY   B N    1 ? 1 
ATOM   1003 C CA   . GLY   A 1 70  ? -17.704 11.645  8.376   1   62.333  ? 82  GLY   B CA   1 ? 1 
ATOM   1004 C C    . GLY   A 1 70  ? -17.419 12.023  9.82    1   69.686  ? 82  GLY   B C    1 ? 1 
ATOM   1005 O O    . GLY   A 1 70  ? -16.51  12.81   10.047  1   76.298  ? 82  GLY   B O    1 ? 1 
ATOM   1006 H H    . GLY   A 1 70  ? -18.773 9.895   8.17    1   56.079  ? 82  GLY   B H    1 c 1 
ATOM   1007 H HA2  . GLY   A 1 70  ? -16.926 11.168  8.003   1   60.769  ? 82  GLY   B HA2  1 c 1 
ATOM   1008 H HA3  . GLY   A 1 70  ? -17.839 12.461  7.845   1   64.317  ? 82  GLY   B HA3  1 c 1 
ATOM   1009 N N    . LYS   A 1 71  ? -18.215 11.514  10.78   1   69.311  ? 83  LYS   B N    1 ? 1 
ATOM   1010 C CA   . LYS   A 1 71  ? -18.112 11.949  12.169  1   71.241  ? 83  LYS   B CA   1 ? 1 
ATOM   1011 C C    . LYS   A 1 71  ? -17.373 10.875  12.971  1   74.328  ? 83  LYS   B C    1 ? 1 
ATOM   1012 O O    . LYS   A 1 71  ? -17.596 10.75   14.173  1   79.972  ? 83  LYS   B O    1 ? 1 
ATOM   1013 C CB   . LYS   A 1 71  ? -19.496 12.309  12.723  1   69.544  ? 83  LYS   B CB   1 ? 1 
ATOM   1014 H H    . LYS   A 1 71  ? -18.82  10.864  10.569  1   67.888  ? 83  LYS   B H    1 c 1 
ATOM   1015 H HA   . LYS   A 1 71  ? -17.565 12.774  12.193  1   73.037  ? 83  LYS   B HA   1 c 1 
ATOM   1016 H HB2  . LYS   A 1 71  ? -19.329 12.9    13.476  0   30      ? 83  LYS   B HB2  1 c 1 
ATOM   1017 H HB3  . LYS   A 1 71  ? -20.15  11.911  12.134  0   30      ? 83  LYS   B HB3  1 c 1 
ATOM   1018 N N    . GLY   A 1 72  ? -16.543 10.084  12.274  1   76.138  ? 84  GLY   B N    1 ? 1 
ATOM   1019 C CA   . GLY   A 1 72  ? -15.685 9.036   12.829  1   80.238  ? 84  GLY   B CA   1 ? 1 
ATOM   1020 C C    . GLY   A 1 72  ? -16.399 7.994   13.701  1   71.83   ? 84  GLY   B C    1 ? 1 
ATOM   1021 O O    . GLY   A 1 72  ? -15.864 7.561   14.717  1   79.701  ? 84  GLY   B O    1 ? 1 
ATOM   1022 H H    . GLY   A 1 72  ? -16.504 10.211  11.371  1   74.718  ? 84  GLY   B H    1 c 1 
ATOM   1023 H HA2  . GLY   A 1 72  ? -15.242 8.572   12.08   1   74.618  ? 84  GLY   B HA2  1 c 1 
ATOM   1024 H HA3  . GLY   A 1 72  ? -14.978 9.467   13.365  1   78.368  ? 84  GLY   B HA3  1 c 1 
ATOM   1025 N N    . GLN   A 1 73  ? -17.613 7.595   13.333  1   61.839  ? 85  GLN   B N    1 ? 1 
ATOM   1026 C CA   . GLN   A 1 73  ? -18.308 6.525   14.039  1   60.423  ? 85  GLN   B CA   1 ? 1 
ATOM   1027 C C    . GLN   A 1 73  ? -18.027 5.156   13.41   1   53.872  ? 85  GLN   B C    1 ? 1 
ATOM   1028 O O    . GLN   A 1 73  ? -18.292 4.128   14.027  1   51.58   ? 85  GLN   B O    1 ? 1 
ATOM   1029 C CB   . GLN   A 1 73  ? -19.793 6.87    14.045  1   61.73   ? 85  GLN   B CB   1 ? 1 
ATOM   1030 C CG   . GLN   A 1 73  ? -20.091 8.036   14.975  1   67.082  ? 85  GLN   B CG   1 ? 1 
ATOM   1031 C CD   . GLN   A 1 73  ? -21.423 8.685   14.717  1   68.488  ? 85  GLN   B CD   1 ? 1 
ATOM   1032 O OE1  . GLN   A 1 73  ? -22.31  8.119   14.076  1   69.049  ? 85  GLN   B OE1  1 ? 1 
ATOM   1033 N NE2  . GLN   A 1 73  ? -21.563 9.878   15.261  1   78.244  ? 85  GLN   B NE2  1 ? 1 
ATOM   1034 H H    . GLN   A 1 73  ? -18.023 7.995   12.621  1   63.192  ? 85  GLN   B H    1 c 1 
ATOM   1035 H HA   . GLN   A 1 73  ? -17.991 6.51    14.978  1   61.674  ? 85  GLN   B HA   1 c 1 
ATOM   1036 H HB2  . GLN   A 1 73  ? -20.075 7.099   13.134  1   61.223  ? 85  GLN   B HB2  1 c 1 
ATOM   1037 H HB3  . GLN   A 1 73  ? -20.306 6.086   14.333  1   62.509  ? 85  GLN   B HB3  1 c 1 
ATOM   1038 H HG2  . GLN   A 1 73  ? -20.071 7.72    15.903  1   68.142  ? 85  GLN   B HG2  1 c 1 
ATOM   1039 H HG3  . GLN   A 1 73  ? -19.389 8.714   14.878  1   66.611  ? 85  GLN   B HG3  1 c 1 
ATOM   1040 H HE21 . GLN   A 1 73  ? -22.361 10.267  15.267  1   78.209  ? 85  GLN   B HE21 1 c 1 
ATOM   1041 H HE22 . GLN   A 1 73  ? -20.867 10.292  15.622  1   76.693  ? 85  GLN   B HE22 1 c 1 
ATOM   1042 N N    . VAL   A 1 74  ? -17.457 5.154   12.209  1   47.092  ? 86  VAL   B N    1 ? 1 
ATOM   1043 C CA   . VAL   A 1 74  ? -17.255 3.931   11.439  1   44.398  ? 86  VAL   B CA   1 ? 1 
ATOM   1044 C C    . VAL   A 1 74  ? -15.838 3.983   10.879  1   41.286  ? 86  VAL   B C    1 ? 1 
ATOM   1045 O O    . VAL   A 1 74  ? -15.191 4.999   10.956  1   43.163  ? 86  VAL   B O    1 ? 1 
ATOM   1046 C CB   . VAL   A 1 74  ? -18.27  3.793   10.288  1   42.909  ? 86  VAL   B CB   1 ? 1 
ATOM   1047 C CG1  . VAL   A 1 74  ? -19.691 3.539   10.824  1   45.928  ? 86  VAL   B CG1  1 ? 1 
ATOM   1048 C CG2  . VAL   A 1 74  ? -18.26  5.022   9.387   1   43      ? 86  VAL   B CG2  1 ? 1 
ATOM   1049 H H    . VAL   A 1 74  ? -17.178 5.945   11.847  1   48.305  ? 86  VAL   B H    1 c 1 
ATOM   1050 H HA   . VAL   A 1 74  ? -17.336 3.161   12.033  1   44.4    ? 86  VAL   B HA   1 c 1 
ATOM   1051 H HB   . VAL   A 1 74  ? -18.001 3.013   9.749   1   41.789  ? 86  VAL   B HB   1 c 1 
ATOM   1052 H HG11 . VAL   A 1 74  ? -19.967 4.287   11.38   1   47.413  ? 86  VAL   B HG11 1 c 1 
ATOM   1053 H HG12 . VAL   A 1 74  ? -19.698 2.724   11.352  1   45.914  ? 86  VAL   B HG12 1 c 1 
ATOM   1054 H HG13 . VAL   A 1 74  ? -20.308 3.447   10.078  1   45.561  ? 86  VAL   B HG13 1 c 1 
ATOM   1055 H HG21 . VAL   A 1 74  ? -18.914 4.908   8.678   1   42.936  ? 86  VAL   B HG21 1 c 1 
ATOM   1056 H HG22 . VAL   A 1 74  ? -17.378 5.134   8.995   1   41.962  ? 86  VAL   B HG22 1 c 1 
ATOM   1057 H HG23 . VAL   A 1 74  ? -18.485 5.811   9.908   1   44.676  ? 86  VAL   B HG23 1 c 1 
ATOM   1058 N N    . ILE   A 1 75  ? -15.366 2.889   10.332  1   42.187  ? 87  ILE   B N    1 ? 1 
ATOM   1059 C CA   . ILE   A 1 75  ? -14.067 2.861   9.676   1   41.602  ? 87  ILE   B CA   1 ? 1 
ATOM   1060 C C    . ILE   A 1 75  ? -14.028 3.829   8.497   1   37.471  ? 87  ILE   B C    1 ? 1 
ATOM   1061 O O    . ILE   A 1 75  ? -15.059 4.174   7.904   1   37.198  ? 87  ILE   B O    1 ? 1 
ATOM   1062 C CB   . ILE   A 1 75  ? -13.701 1.438   9.279   1   39.606  ? 87  ILE   B CB   1 ? 1 
ATOM   1063 C CG1  . ILE   A 1 75  ? -14.743 0.822   8.353   1   43.398  ? 87  ILE   B CG1  1 ? 1 
ATOM   1064 C CG2  . ILE   A 1 75  ? -13.467 0.603   10.526  1   42.381  ? 87  ILE   B CG2  1 ? 1 
ATOM   1065 C CD1  . ILE   A 1 75  ? -14.269 -0.443  7.67    1   42.119  ? 87  ILE   B CD1  1 ? 1 
ATOM   1066 H H    . ILE   A 1 75  ? -15.862 2.123   10.371  1   41.565  ? 87  ILE   B H    1 c 1 
ATOM   1067 H HA   . ILE   A 1 75  ? -13.405 3.162   10.329  1   41.396  ? 87  ILE   B HA   1 c 1 
ATOM   1068 H HB   . ILE   A 1 75  ? -12.858 1.48    8.786   1   40.351  ? 87  ILE   B HB   1 c 1 
ATOM   1069 H HG12 . ILE   A 1 75  ? -15.546 0.615   8.872   1   42.872  ? 87  ILE   B HG12 1 c 1 
ATOM   1070 H HG13 . ILE   A 1 75  ? -14.988 1.477   7.668   1   41.984  ? 87  ILE   B HG13 1 c 1 
ATOM   1071 H HG21 . ILE   A 1 75  ? -13.14  -0.276  10.273  1   41.331  ? 87  ILE   B HG21 1 c 1 
ATOM   1072 H HG22 . ILE   A 1 75  ? -14.3   0.508   11.017  1   42.587  ? 87  ILE   B HG22 1 c 1 
ATOM   1073 H HG23 . ILE   A 1 75  ? -12.808 1.04    11.092  1   42.567  ? 87  ILE   B HG23 1 c 1 
ATOM   1074 H HD11 . ILE   A 1 75  ? -13.435 -0.265  7.195   1   41.826  ? 87  ILE   B HD11 1 c 1 
ATOM   1075 H HD12 . ILE   A 1 75  ? -14.946 -0.741  7.033   1   42.18   ? 87  ILE   B HD12 1 c 1 
ATOM   1076 H HD13 . ILE   A 1 75  ? -14.121 -1.141  8.335   1   42.607  ? 87  ILE   B HD13 1 c 1 
ATOM   1077 N N    . LYS   A 1 76  ? -12.8   4.287   8.213   1   41.321  ? 88  LYS   B N    1 ? 1 
ATOM   1078 C CA   . LYS   A 1 76  ? -12.559 5.316   7.214   1   40.819  ? 88  LYS   B CA   1 ? 1 
ATOM   1079 C C    . LYS   A 1 76  ? -13.2   4.894   5.895   1   36.935  ? 88  LYS   B C    1 ? 1 
ATOM   1080 O O    . LYS   A 1 76  ? -13.795 5.72    5.218   1   39.49   ? 88  LYS   B O    1 ? 1 
ATOM   1081 C CB   . LYS   A 1 76  ? -11.049 5.584   7.1     1   44.773  ? 88  LYS   B CB   1 ? 1 
ATOM   1082 H H    . LYS   A 1 76  ? -12.084 3.937   8.661   1   40.255  ? 88  LYS   B H    1 c 1 
ATOM   1083 H HA   . LYS   A 1 76  ? -12.999 6.149   7.521   1   42.178  ? 88  LYS   B HA   1 c 1 
ATOM   1084 H HB2  . LYS   A 1 76  ? -10.612 4.811   7.352   0   30      ? 88  LYS   B HB2  1 c 1 
ATOM   1085 H HB3  . LYS   A 1 76  ? -10.948 6.538   6.752   0   30      ? 88  LYS   B HB3  1 c 1 
ATOM   1086 N N    . ALA   A 1 77  ? -13.095 3.613   5.538   1   37.401  ? 89  ALA   B N    1 ? 1 
ATOM   1087 C CA   . ALA   A 1 77  ? -13.604 3.118   4.259   1   39.635  ? 89  ALA   B CA   1 ? 1 
ATOM   1088 C C    . ALA   A 1 77  ? -15.107 3.312   4.122   1   41.872  ? 89  ALA   B C    1 ? 1 
ATOM   1089 O O    . ALA   A 1 77  ? -15.61  3.429   3.003   1   38.946  ? 89  ALA   B O    1 ? 1 
ATOM   1090 C CB   . ALA   A 1 77  ? -13.282 1.67    4.063   1   39.1    ? 89  ALA   B CB   1 ? 1 
ATOM   1091 H H    . ALA   A 1 77  ? -12.682 3.024   6.102   1   37.186  ? 89  ALA   B H    1 c 1 
ATOM   1092 H HA   . ALA   A 1 77  ? -13.163 3.643   3.535   1   40.066  ? 89  ALA   B HA   1 c 1 
ATOM   1093 H HB1  . ALA   A 1 77  ? -12.318 1.545   4.067   1   38.982  ? 89  ALA   B HB1  1 c 1 
ATOM   1094 H HB2  . ALA   A 1 77  ? -13.676 1.147   4.781   1   38.704  ? 89  ALA   B HB2  1 c 1 
ATOM   1095 H HB3  . ALA   A 1 77  ? -13.64  1.367   3.211   1   39.067  ? 89  ALA   B HB3  1 c 1 
ATOM   1096 N N    . TRP   A 1 78  ? -15.834 3.288   5.255   1   41.398  ? 90  TRP   B N    1 ? 1 
ATOM   1097 C CA   . TRP   A 1 78  ? -17.264 3.557   5.2     1   40.744  ? 90  TRP   B CA   1 ? 1 
ATOM   1098 C C    . TRP   A 1 78  ? -17.534 5.03    4.953   1   41.175  ? 90  TRP   B C    1 ? 1 
ATOM   1099 O O    . TRP   A 1 78  ? -18.419 5.364   4.174   1   45.789  ? 90  TRP   B O    1 ? 1 
ATOM   1100 C CB   . TRP   A 1 78  ? -17.979 3.034   6.46    1   40.637  ? 90  TRP   B CB   1 ? 1 
ATOM   1101 C CG   . TRP   A 1 78  ? -18.493 1.639   6.313   1   39.589  ? 90  TRP   B CG   1 ? 1 
ATOM   1102 C CD1  . TRP   A 1 78  ? -17.816 0.532   5.86    1   40.937  ? 90  TRP   B CD1  1 ? 1 
ATOM   1103 C CD2  . TRP   A 1 78  ? -19.85  1.2     6.543   1   40.117  ? 90  TRP   B CD2  1 ? 1 
ATOM   1104 N NE1  . TRP   A 1 78  ? -18.646 -0.558  5.847   1   36.433  ? 90  TRP   B NE1  1 ? 1 
ATOM   1105 C CE2  . TRP   A 1 78  ? -19.899 -0.175  6.24    1   39.647  ? 90  TRP   B CE2  1 ? 1 
ATOM   1106 C CE3  . TRP   A 1 78  ? -21.015 1.833   6.972   1   42.501  ? 90  TRP   B CE3  1 ? 1 
ATOM   1107 C CZ2  . TRP   A 1 78  ? -21.065 -0.922  6.376   1   41.601  ? 90  TRP   B CZ2  1 ? 1 
ATOM   1108 C CZ3  . TRP   A 1 78  ? -22.166 1.09    7.105   1   43.411  ? 90  TRP   B CZ3  1 ? 1 
ATOM   1109 C CH2  . TRP   A 1 78  ? -22.189 -0.263  6.795   1   42.621  ? 90  TRP   B CH2  1 ? 1 
ATOM   1110 H H    . TRP   A 1 78  ? -15.442 3.097   6.057   1   40.884  ? 90  TRP   B H    1 c 1 
ATOM   1111 H HA   . TRP   A 1 78  ? -17.631 3.053   4.424   1   40.664  ? 90  TRP   B HA   1 c 1 
ATOM   1112 H HB2  . TRP   A 1 78  ? -17.354 3.066   7.214   1   40.409  ? 90  TRP   B HB2  1 c 1 
ATOM   1113 H HB3  . TRP   A 1 78  ? -18.732 3.63    6.663   1   41.831  ? 90  TRP   B HB3  1 c 1 
ATOM   1114 H HD1  . TRP   A 1 78  ? -16.9   0.507   5.634   1   38.125  ? 90  TRP   B HD1  1 c 1 
ATOM   1115 H HE1  . TRP   A 1 78  ? -18.417 -1.359  5.605   1   37.8    ? 90  TRP   B HE1  1 c 1 
ATOM   1116 H HE3  . TRP   A 1 78  ? -21.008 2.75    7.185   1   42.663  ? 90  TRP   B HE3  1 c 1 
ATOM   1117 H HZ2  . TRP   A 1 78  ? -21.084 -1.84   6.166   1   41.622  ? 90  TRP   B HZ2  1 c 1 
ATOM   1118 H HZ3  . TRP   A 1 78  ? -22.957 1.513   7.394   1   45.275  ? 90  TRP   B HZ3  1 c 1 
ATOM   1119 H HH2  . TRP   A 1 78  ? -22.992 -0.743  6.891   1   44.802  ? 90  TRP   B HH2  1 c 1 
ATOM   1120 N N    . ASP   A 1 79  ? -16.796 5.915   5.633   1   40.013  ? 91  ASP   B N    1 ? 1 
ATOM   1121 C CA   . ASP   A 1 79  ? -16.977 7.343   5.424   1   44.05   ? 91  ASP   B CA   1 ? 1 
ATOM   1122 C C    . ASP   A 1 79  ? -16.717 7.656   3.951   1   47.17   ? 91  ASP   B C    1 ? 1 
ATOM   1123 O O    . ASP   A 1 79  ? -17.464 8.412   3.351   1   48.051  ? 91  ASP   B O    1 ? 1 
ATOM   1124 C CB   . ASP   A 1 79  ? -16.155 8.163   6.4     1   45.117  ? 91  ASP   B CB   1 ? 1 
ATOM   1125 C CG   . ASP   A 1 79  ? -16.731 8.332   7.811   1   47.605  ? 91  ASP   B CG   1 ? 1 
ATOM   1126 O OD1  . ASP   A 1 79  ? -17.922 8.144   7.996   1   49.606  ? 91  ASP   B OD1  1 ? 1 
ATOM   1127 O OD2  . ASP   A 1 79  ? -15.982 8.66    8.739   1   48.116  ? 91  ASP   B OD2  1 ? 1 
ATOM   1128 H H    . ASP   A 1 79  ? -16.176 5.626   6.24    1   40.374  ? 91  ASP   B H    1 c 1 
ATOM   1129 H HA   . ASP   A 1 79  ? -17.92  7.554   5.61    1   45.17   ? 91  ASP   B HA   1 c 1 
ATOM   1130 H HB2  . ASP   A 1 79  ? -15.27  7.752   6.484   1   44.427  ? 91  ASP   B HB2  1 c 1 
ATOM   1131 H HB3  . ASP   A 1 79  ? -16.03  9.058   6.022   1   46.841  ? 91  ASP   B HB3  1 c 1 
ATOM   1132 N N    . ILE   A 1 80  ? -15.662 7.058   3.368   1   45.393  ? 92  ILE   B N    1 ? 1 
ATOM   1133 C CA   . ILE   A 1 80  ? -15.33  7.267   1.962   1   46.634  ? 92  ILE   B CA   1 ? 1 
ATOM   1134 C C    . ILE   A 1 80  ? -16.402 6.624   1.086   1   42.4    ? 92  ILE   B C    1 ? 1 
ATOM   1135 O O    . ILE   A 1 80  ? -16.919 7.256   0.182   1   46.121  ? 92  ILE   B O    1 ? 1 
ATOM   1136 C CB   . ILE   A 1 80  ? -13.938 6.694   1.621   1   47.566  ? 92  ILE   B CB   1 ? 1 
ATOM   1137 C CG1  . ILE   A 1 80  ? -12.82  7.43    2.323   1   50.809  ? 92  ILE   B CG1  1 ? 1 
ATOM   1138 C CG2  . ILE   A 1 80  ? -13.713 6.659   0.104   1   50.2    ? 92  ILE   B CG2  1 ? 1 
ATOM   1139 C CD1  . ILE   A 1 80  ? -11.522 6.637   2.373   1   51.243  ? 92  ILE   B CD1  1 ? 1 
ATOM   1140 H H    . ILE   A 1 80  ? -15.13  6.506   3.866   1   44.542  ? 92  ILE   B H    1 c 1 
ATOM   1141 H HA   . ILE   A 1 80  ? -15.319 8.228   1.786   1   47.651  ? 92  ILE   B HA   1 c 1 
ATOM   1142 H HB   . ILE   A 1 80  ? -13.92  5.77    1.94    1   46.467  ? 92  ILE   B HB   1 c 1 
ATOM   1143 H HG12 . ILE   A 1 80  ? -12.657 8.276   1.859   1   52.28   ? 92  ILE   B HG12 1 c 1 
ATOM   1144 H HG13 . ILE   A 1 80  ? -13.1   7.637   3.238   1   50.346  ? 92  ILE   B HG13 1 c 1 
ATOM   1145 H HG21 . ILE   A 1 80  ? -12.784 6.447   -0.085  1   49.865  ? 92  ILE   B HG21 1 c 1 
ATOM   1146 H HG22 . ILE   A 1 80  ? -13.928 7.527   -0.277  1   51.46   ? 92  ILE   B HG22 1 c 1 
ATOM   1147 H HG23 . ILE   A 1 80  ? -14.283 5.981   -0.297  1   49.176  ? 92  ILE   B HG23 1 c 1 
ATOM   1148 H HD11 . ILE   A 1 80  ? -11.682 5.779   2.809   1   49.361  ? 92  ILE   B HD11 1 c 1 
ATOM   1149 H HD12 . ILE   A 1 80  ? -10.856 7.138   2.881   1   51.812  ? 92  ILE   B HD12 1 c 1 
ATOM   1150 H HD13 . ILE   A 1 80  ? -11.189 6.483   1.469   1   51.392  ? 92  ILE   B HD13 1 c 1 
ATOM   1151 N N    . GLY   A 1 81  ? -16.762 5.368   1.375   1   41.353  ? 93  GLY   B N    1 ? 1 
ATOM   1152 C CA   . GLY   A 1 81  ? -17.573 4.595   0.457   1   42.305  ? 93  GLY   B CA   1 ? 1 
ATOM   1153 C C    . GLY   A 1 81  ? -19.038 5.018   0.417   1   46.778  ? 93  GLY   B C    1 ? 1 
ATOM   1154 O O    . GLY   A 1 81  ? -19.658 5.084   -0.642  1   47.423  ? 93  GLY   B O    1 ? 1 
ATOM   1155 H H    . GLY   A 1 81  ? -16.493 4.985   2.159   1   40.385  ? 93  GLY   B H    1 c 1 
ATOM   1156 H HA2  . GLY   A 1 81  ? -17.192 4.677   -0.448  1   43.434  ? 93  GLY   B HA2  1 c 1 
ATOM   1157 H HA3  . GLY   A 1 81  ? -17.521 3.645   0.715   1   41.713  ? 93  GLY   B HA3  1 c 1 
ATOM   1158 N N    . VAL   A 1 82  ? -19.617 5.266   1.602   1   46.9    ? 94  VAL   B N    1 ? 1 
ATOM   1159 C CA   . VAL   A 1 82  ? -21.029 5.567   1.666   1   45.378  ? 94  VAL   B CA   1 ? 1 
ATOM   1160 C C    . VAL   A 1 82  ? -21.26  6.973   1.11    1   47.928  ? 94  VAL   B C    1 ? 1 
ATOM   1161 O O    . VAL   A 1 82  ? -22.34  7.223   0.577   1   46.844  ? 94  VAL   B O    1 ? 1 
ATOM   1162 C CB   . VAL   A 1 82  ? -21.526 5.375   3.108   1   48.585  ? 94  VAL   B CB   1 ? 1 
ATOM   1163 C CG1  . VAL   A 1 82  ? -22.949 5.901   3.318   1   51.924  ? 94  VAL   B CG1  1 ? 1 
ATOM   1164 C CG2  . VAL   A 1 82  ? -21.429 3.905   3.509   1   47.525  ? 94  VAL   B CG2  1 ? 1 
ATOM   1165 H H    . VAL   A 1 82  ? -19.126 5.244   2.372   1   45.055  ? 94  VAL   B H    1 c 1 
ATOM   1166 H HA   . VAL   A 1 82  ? -21.503 4.93    1.096   1   47.114  ? 94  VAL   B HA   1 c 1 
ATOM   1167 H HB   . VAL   A 1 82  ? -20.926 5.891   3.695   1   47.658  ? 94  VAL   B HB   1 c 1 
ATOM   1168 H HG11 . VAL   A 1 82  ? -23.524 5.58    2.602   1   52.713  ? 94  VAL   B HG11 1 c 1 
ATOM   1169 H HG12 . VAL   A 1 82  ? -22.942 6.873   3.317   1   52.88   ? 94  VAL   B HG12 1 c 1 
ATOM   1170 H HG13 . VAL   A 1 82  ? -23.288 5.582   4.17    1   52.061  ? 94  VAL   B HG13 1 c 1 
ATOM   1171 H HG21 . VAL   A 1 82  ? -21.774 3.791   4.411   1   47.825  ? 94  VAL   B HG21 1 c 1 
ATOM   1172 H HG22 . VAL   A 1 82  ? -20.501 3.62    3.48    1   45.838  ? 94  VAL   B HG22 1 c 1 
ATOM   1173 H HG23 . VAL   A 1 82  ? -21.952 3.366   2.893   1   48.044  ? 94  VAL   B HG23 1 c 1 
ATOM   1174 N N    . ALA   A 1 83  ? -20.252 7.87    1.186   1   47.705  ? 95  ALA   B N    1 ? 1 
ATOM   1175 C CA   . ALA   A 1 83  ? -20.364 9.176   0.556   1   51.811  ? 95  ALA   B CA   1 ? 1 
ATOM   1176 C C    . ALA   A 1 83  ? -20.526 9.074   -0.955  1   53.73   ? 95  ALA   B C    1 ? 1 
ATOM   1177 O O    . ALA   A 1 83  ? -20.94  10.046  -1.562  1   60.709  ? 95  ALA   B O    1 ? 1 
ATOM   1178 C CB   . ALA   A 1 83  ? -19.189 10.09   0.849   1   53.378  ? 95  ALA   B CB   1 ? 1 
ATOM   1179 H H    . ALA   A 1 83  ? -19.49  7.664   1.647   1   46.645  ? 95  ALA   B H    1 c 1 
ATOM   1180 H HA   . ALA   A 1 83  ? -21.188 9.608   0.915   1   53.357  ? 95  ALA   B HA   1 c 1 
ATOM   1181 H HB1  . ALA   A 1 83  ? -19.093 10.203  1.809   1   52.593  ? 95  ALA   B HB1  1 c 1 
ATOM   1182 H HB2  . ALA   A 1 83  ? -18.375 9.7     0.488   1   51.855  ? 95  ALA   B HB2  1 c 1 
ATOM   1183 H HB3  . ALA   A 1 83  ? -19.339 10.958  0.437   1   55.257  ? 95  ALA   B HB3  1 c 1 
ATOM   1184 N N    . THR   A 1 84  ? -20.149 7.959   -1.575  1   56.866  ? 96  THR   B N    1 ? 1 
ATOM   1185 C CA   . THR   A 1 84  ? -20.289 7.811   -3.023  1   58.74   ? 96  THR   B CA   1 ? 1 
ATOM   1186 C C    . THR   A 1 84  ? -21.655 7.239   -3.404  1   60.334  ? 96  THR   B C    1 ? 1 
ATOM   1187 O O    . THR   A 1 84  ? -21.931 7.131   -4.589  1   61      ? 96  THR   B O    1 ? 1 
ATOM   1188 C CB   . THR   A 1 84  ? -19.183 6.932   -3.616  1   57.011  ? 96  THR   B CB   1 ? 1 
ATOM   1189 O OG1  . THR   A 1 84  ? -19.433 5.589   -3.195  1   53.623  ? 96  THR   B OG1  1 ? 1 
ATOM   1190 C CG2  . THR   A 1 84  ? -17.787 7.39    -3.21   1   55.791  ? 96  THR   B CG2  1 ? 1 
ATOM   1191 H H    . THR   A 1 84  ? -19.776 7.276   -1.097  1   53.583  ? 96  THR   B H    1 c 1 
ATOM   1192 H HA   . THR   A 1 84  ? -20.209 8.703   -3.426  1   60.613  ? 96  THR   B HA   1 c 1 
ATOM   1193 H HB   . THR   A 1 84  ? -19.241 6.972   -4.601  1   58.595  ? 96  THR   B HB   1 c 1 
ATOM   1194 H HG1  . THR   A 1 84  ? -19.41  5.607   -2.378  0   30      ? 96  THR   B HG1  1 c 1 
ATOM   1195 H HG21 . THR   A 1 84  ? -17.122 6.857   -3.677  1   55.446  ? 96  THR   B HG21 1 c 1 
ATOM   1196 H HG22 . THR   A 1 84  ? -17.675 7.279   -2.252  1   54.137  ? 96  THR   B HG22 1 c 1 
ATOM   1197 H HG23 . THR   A 1 84  ? -17.672 8.327   -3.443  1   57.591  ? 96  THR   B HG23 1 c 1 
ATOM   1198 N N    . MET   A 1 85  ? -22.501 6.853   -2.435  1   59.546  ? 97  MET   B N    1 ? 1 
ATOM   1199 C CA   . MET   A 1 85  ? -23.667 6.039   -2.756  1   61.058  ? 97  MET   B CA   1 ? 1 
ATOM   1200 C C    . MET   A 1 85  ? -24.937 6.886   -2.856  1   62.583  ? 97  MET   B C    1 ? 1 
ATOM   1201 O O    . MET   A 1 85  ? -25.064 7.946   -2.235  1   60.93   ? 97  MET   B O    1 ? 1 
ATOM   1202 C CB   . MET   A 1 85  ? -23.867 4.942   -1.714  1   59.161  ? 97  MET   B CB   1 ? 1 
ATOM   1203 C CG   . MET   A 1 85  ? -22.763 3.922   -1.673  1   57.014  ? 97  MET   B CG   1 ? 1 
ATOM   1204 S SD   . MET   A 1 85  ? -23.024 2.727   -0.353  1   56.43   ? 97  MET   B SD   1 ? 1 
ATOM   1205 C CE   . MET   A 1 85  ? -24.416 1.823   -1.024  1   59.113  ? 97  MET   B CE   1 ? 1 
ATOM   1206 H H    . MET   A 1 85  ? -22.356 7.1     -1.568  1   58.497  ? 97  MET   B H    1 c 1 
ATOM   1207 H HA   . MET   A 1 85  ? -23.511 5.615   -3.637  1   61.246  ? 97  MET   B HA   1 c 1 
ATOM   1208 H HB2  . MET   A 1 85  ? -23.944 5.361   -0.83   1   58.842  ? 97  MET   B HB2  1 c 1 
ATOM   1209 H HB3  . MET   A 1 85  ? -24.715 4.486   -1.902  1   60.902  ? 97  MET   B HB3  1 c 1 
ATOM   1210 H HG2  . MET   A 1 85  ? -22.722 3.449   -2.526  1   57.693  ? 97  MET   B HG2  1 c 1 
ATOM   1211 H HG3  . MET   A 1 85  ? -21.908 4.37    -1.533  1   55.704  ? 97  MET   B HG3  1 c 1 
ATOM   1212 H HE1  . MET   A 1 85  ? -24.648 1.092   -0.421  1   59.01   ? 97  MET   B HE1  1 c 1 
ATOM   1213 H HE2  . MET   A 1 85  ? -25.18  2.422   -1.114  1   61.147  ? 97  MET   B HE2  1 c 1 
ATOM   1214 H HE3  . MET   A 1 85  ? -24.178 1.462   -1.898  1   59.654  ? 97  MET   B HE3  1 c 1 
ATOM   1215 N N    . LYS   A 1 86  ? -25.89  6.387   -3.657  1   62.269  ? 98  LYS   B N    1 ? 1 
ATOM   1216 C CA   . LYS   A 1 86  ? -27.166 7.06    -3.856  1   65.267  ? 98  LYS   B CA   1 ? 1 
ATOM   1217 C C    . LYS   A 1 86  ? -28.224 6.287   -3.066  1   67.54   ? 98  LYS   B C    1 ? 1 
ATOM   1218 O O    . LYS   A 1 86  ? -27.978 5.137   -2.685  1   66.951  ? 98  LYS   B O    1 ? 1 
ATOM   1219 C CB   . LYS   A 1 86  ? -27.436 7.16    -5.359  1   66.67   ? 98  LYS   B CB   1 ? 1 
ATOM   1220 H H    . LYS   A 1 86  ? -25.741 5.593   -4.086  1   62.312  ? 98  LYS   B H    1 c 1 
ATOM   1221 H HA   . LYS   A 1 86  ? -27.102 7.977   -3.485  1   65.786  ? 98  LYS   B HA   1 c 1 
ATOM   1222 H HB2  . LYS   A 1 86  ? -26.619 7.208   -5.859  0   30      ? 98  LYS   B HB2  1 c 1 
ATOM   1223 H HB3  . LYS   A 1 86  ? -28.44  7.176   -5.487  0   30      ? 98  LYS   B HB3  1 c 1 
ATOM   1224 N N    . LYS   A 1 87  ? -29.379 6.922   -2.808  1   70.877  ? 99  LYS   B N    1 ? 1 
ATOM   1225 C CA   . LYS   A 1 87  ? -30.477 6.29    -2.081  1   72.769  ? 99  LYS   B CA   1 ? 1 
ATOM   1226 C C    . LYS   A 1 87  ? -30.907 5.03    -2.837  1   75.382  ? 99  LYS   B C    1 ? 1 
ATOM   1227 O O    . LYS   A 1 87  ? -31.037 5.044   -4.053  1   78.358  ? 99  LYS   B O    1 ? 1 
ATOM   1228 C CB   . LYS   A 1 87  ? -31.652 7.249   -1.822  1   75.642  ? 99  LYS   B CB   1 ? 1 
ATOM   1229 H H    . LYS   A 1 87  ? -29.484 7.783   -3.097  1   72.58   ? 99  LYS   B H    1 c 1 
ATOM   1230 H HA   . LYS   A 1 87  ? -30.127 6.011   -1.197  1   70.375  ? 99  LYS   B HA   1 c 1 
ATOM   1231 H HB2  . LYS   A 1 87  ? -31.312 8.21    -1.747  0   30      ? 99  LYS   B HB2  1 c 1 
ATOM   1232 H HB3  . LYS   A 1 87  ? -32.502 6.81    -2.025  0   30      ? 99  LYS   B HB3  1 c 1 
ATOM   1233 N N    . GLY   A 1 88  ? -31.028 3.915   -2.117  1   74.171  ? 100 GLY   B N    1 ? 1 
ATOM   1234 C CA   . GLY   A 1 88  ? -31.448 2.662   -2.716  1   77.28   ? 100 GLY   B CA   1 ? 1 
ATOM   1235 C C    . GLY   A 1 88  ? -30.315 1.886   -3.392  1   73.982  ? 100 GLY   B C    1 ? 1 
ATOM   1236 O O    . GLY   A 1 88  ? -30.557 0.782   -3.885  1   74.875  ? 100 GLY   B O    1 ? 1 
ATOM   1237 H H    . GLY   A 1 88  ? -30.845 3.935   -1.221  1   72.896  ? 100 GLY   B H    1 c 1 
ATOM   1238 H HA2  . GLY   A 1 88  ? -31.849 2.098   -2.014  1   77.44   ? 100 GLY   B HA2  1 c 1 
ATOM   1239 H HA3  . GLY   A 1 88  ? -32.152 2.85    -3.382  1   80.342  ? 100 GLY   B HA3  1 c 1 
ATOM   1240 N N    . GLU   A 1 89  ? -29.091 2.44    -3.391  1   71.204  ? 101 GLU   B N    1 ? 1 
ATOM   1241 C CA   . GLU   A 1 89  ? -27.948 1.766   -3.995  1   67.542  ? 101 GLU   B CA   1 ? 1 
ATOM   1242 C C    . GLU   A 1 89  ? -27.511 0.597   -3.113  1   64.398  ? 101 GLU   B C    1 ? 1 
ATOM   1243 O O    . GLU   A 1 89  ? -27.504 0.73    -1.887  1   57.258  ? 101 GLU   B O    1 ? 1 
ATOM   1244 C CB   . GLU   A 1 89  ? -26.804 2.753   -4.21   1   65.725  ? 101 GLU   B CB   1 ? 1 
ATOM   1245 C CG   . GLU   A 1 89  ? -25.614 2.206   -4.996  1   64.296  ? 101 GLU   B CG   1 ? 1 
ATOM   1246 C CD   . GLU   A 1 89  ? -24.494 3.213   -5.182  1   60.304  ? 101 GLU   B CD   1 ? 1 
ATOM   1247 O OE1  . GLU   A 1 89  ? -24.709 4.356   -5.646  1   63.574  ? 101 GLU   B OE1  1 ? 1 
ATOM   1248 O OE2  . GLU   A 1 89  ? -23.359 2.824   -4.837  1   57.027  ? 101 GLU   B OE2  1 ? 1 
ATOM   1249 H H    . GLU   A 1 89  ? -28.961 3.254   -2.997  1   69.922  ? 101 GLU   B H    1 c 1 
ATOM   1250 H HA   . GLU   A 1 89  ? -28.228 1.414   -4.876  1   70.058  ? 101 GLU   B HA   1 c 1 
ATOM   1251 H HB2  . GLU   A 1 89  ? -27.152 3.538   -4.683  1   67.597  ? 101 GLU   B HB2  1 c 1 
ATOM   1252 H HB3  . GLU   A 1 89  ? -26.482 3.054   -3.335  1   63.517  ? 101 GLU   B HB3  1 c 1 
ATOM   1253 H HG2  . GLU   A 1 89  ? -25.254 1.421   -4.531  1   61.923  ? 101 GLU   B HG2  1 c 1 
ATOM   1254 H HG3  . GLU   A 1 89  ? -25.921 1.914   -5.881  1   66.095  ? 101 GLU   B HG3  1 c 1 
ATOM   1255 N N    . ILE   A 1 90  ? -27.237 -0.564  -3.745  1   65.615  ? 102 ILE   B N    1 ? 1 
ATOM   1256 C CA   . ILE   A 1 90  ? -26.421 -1.603  -3.116  1   64.445  ? 102 ILE   B CA   1 ? 1 
ATOM   1257 C C    . ILE   A 1 90  ? -25.037 -1.614  -3.765  1   60.686  ? 102 ILE   B C    1 ? 1 
ATOM   1258 O O    . ILE   A 1 90  ? -24.934 -1.698  -4.985  1   60.207  ? 102 ILE   B O    1 ? 1 
ATOM   1259 C CB   . ILE   A 1 90  ? -27.062 -2.999  -3.148  1   65.298  ? 102 ILE   B CB   1 ? 1 
ATOM   1260 C CG1  . ILE   A 1 90  ? -28.482 -2.969  -2.559  1   70.912  ? 102 ILE   B CG1  1 ? 1 
ATOM   1261 C CG2  . ILE   A 1 90  ? -26.168 -4.024  -2.438  1   61.09   ? 102 ILE   B CG2  1 ? 1 
ATOM   1262 C CD1  . ILE   A 1 90  ? -29.317 -4.191  -2.86   1   72.843  ? 102 ILE   B CD1  1 ? 1 
ATOM   1263 H H    . ILE   A 1 90  ? -27.566 -0.71   -4.585  1   68.117  ? 102 ILE   B H    1 c 1 
ATOM   1264 H HA   . ILE   A 1 90  ? -26.31  -1.359  -2.182  1   61.754  ? 102 ILE   B HA   1 c 1 
ATOM   1265 H HB   . ILE   A 1 90  ? -27.138 -3.268  -4.085  1   67.607  ? 102 ILE   B HB   1 c 1 
ATOM   1266 H HG12 . ILE   A 1 90  ? -28.414 -2.87   -1.587  1   68.338  ? 102 ILE   B HG12 1 c 1 
ATOM   1267 H HG13 . ILE   A 1 90  ? -28.948 -2.181  -2.905  1   71.092  ? 102 ILE   B HG13 1 c 1 
ATOM   1268 H HG21 . ILE   A 1 90  ? -26.635 -4.873  -2.368  1   63.727  ? 102 ILE   B HG21 1 c 1 
ATOM   1269 H HG22 . ILE   A 1 90  ? -25.949 -3.704  -1.547  1   59.59   ? 102 ILE   B HG22 1 c 1 
ATOM   1270 H HG23 . ILE   A 1 90  ? -25.348 -4.151  -2.944  1   60.328  ? 102 ILE   B HG23 1 c 1 
ATOM   1271 H HD11 . ILE   A 1 90  ? -29.495 -4.237  -3.818  1   75.544  ? 102 ILE   B HD11 1 c 1 
ATOM   1272 H HD12 . ILE   A 1 90  ? -30.162 -4.13   -2.376  1   75.62   ? 102 ILE   B HD12 1 c 1 
ATOM   1273 H HD13 . ILE   A 1 90  ? -28.843 -4.996  -2.58   1   72.556  ? 102 ILE   B HD13 1 c 1 
ATOM   1274 N N    . ALA   A 1 91  ? -24     -1.565  -2.919  1   56.452  ? 103 ALA   B N    1 ? 1 
ATOM   1275 C CA   . ALA   A 1 91  ? -22.613 -1.574  -3.357  1   55.333  ? 103 ALA   B CA   1 ? 1 
ATOM   1276 C C    . ALA   A 1 91  ? -21.832 -2.658  -2.614  1   53.509  ? 103 ALA   B C    1 ? 1 
ATOM   1277 O O    . ALA   A 1 91  ? -22.204 -3.051  -1.507  1   57.479  ? 103 ALA   B O    1 ? 1 
ATOM   1278 C CB   . ALA   A 1 91  ? -22     -0.195  -3.151  1   56.737  ? 103 ALA   B CB   1 ? 1 
ATOM   1279 H H    . ALA   A 1 91  ? -24.167 -1.524  -2.022  1   55.953  ? 103 ALA   B H    1 c 1 
ATOM   1280 H HA   . ALA   A 1 91  ? -22.596 -1.793  -4.328  1   57.342  ? 103 ALA   B HA   1 c 1 
ATOM   1281 H HB1  . ALA   A 1 91  ? -22.486 0.461   -3.679  1   57.355  ? 103 ALA   B HB1  1 c 1 
ATOM   1282 H HB2  . ALA   A 1 91  ? -22.051 0.048   -2.211  1   54.458  ? 103 ALA   B HB2  1 c 1 
ATOM   1283 H HB3  . ALA   A 1 91  ? -21.069 -0.206  -3.43   1   54.696  ? 103 ALA   B HB3  1 c 1 
ATOM   1284 N N    . HIS   A 1 92  ? -20.776 -3.16   -3.271  1   53.179  ? 104 HIS   B N    1 ? 1 
ATOM   1285 C CA   . HIS   A 1 92  ? -19.751 -4.01   -2.678  1   50.992  ? 104 HIS   B CA   1 ? 1 
ATOM   1286 C C    . HIS   A 1 92  ? -18.462 -3.206  -2.474  1   48.403  ? 104 HIS   B C    1 ? 1 
ATOM   1287 O O    . HIS   A 1 92  ? -18.047 -2.488  -3.372  1   51.205  ? 104 HIS   B O    1 ? 1 
ATOM   1288 C CB   . HIS   A 1 92  ? -19.499 -5.224  -3.564  1   54.803  ? 104 HIS   B CB   1 ? 1 
ATOM   1289 C CG   . HIS   A 1 92  ? -20.62  -6.212  -3.56   1   57.228  ? 104 HIS   B CG   1 ? 1 
ATOM   1290 N ND1  . HIS   A 1 92  ? -20.585 -7.37   -4.279  1   60.221  ? 104 HIS   B ND1  1 ? 1 
ATOM   1291 C CD2  . HIS   A 1 92  ? -21.781 -6.232  -2.895  1   57.928  ? 104 HIS   B CD2  1 ? 1 
ATOM   1292 C CE1  . HIS   A 1 92  ? -21.697 -8.042  -4.075  1   63.433  ? 104 HIS   B CE1  1 ? 1 
ATOM   1293 N NE2  . HIS   A 1 92  ? -22.437 -7.37   -3.232  1   61.627  ? 104 HIS   B NE2  1 ? 1 
ATOM   1294 H H    . HIS   A 1 92  ? -20.692 -2.956  -4.158  1   54.279  ? 104 HIS   B H    1 c 1 
ATOM   1295 H HA   . HIS   A 1 92  ? -20.072 -4.317  -1.798  1   50.844  ? 104 HIS   B HA   1 c 1 
ATOM   1296 H HB2  . HIS   A 1 92  ? -19.349 -4.917  -4.484  1   55.435  ? 104 HIS   B HB2  1 c 1 
ATOM   1297 H HB3  . HIS   A 1 92  ? -18.68  -5.672  -3.259  1   53.265  ? 104 HIS   B HB3  1 c 1 
ATOM   1298 H HD1  . HIS   A 1 92  ? -19.904 -7.54   -4.836  0   30      ? 104 HIS   B HD1  1 c 1 
ATOM   1299 H HD2  . HIS   A 1 92  ? -22.097 -5.573  -2.309  1   56.987  ? 104 HIS   B HD2  1 c 1 
ATOM   1300 H HE1  . HIS   A 1 92  ? -21.916 -8.871  -4.463  1   65.705  ? 104 HIS   B HE1  1 c 1 
ATOM   1301 H HE2  . HIS   A 1 92  ? -23.188 -7.597  -2.921  0   30      ? 104 HIS   B HE2  1 c 1 
ATOM   1302 N N    . LEU   A 1 93  ? -17.873 -3.307  -1.271  1   46.578  ? 105 LEU   B N    1 ? 1 
ATOM   1303 C CA   . LEU   A 1 93  ? -16.634 -2.632  -0.888  1   44.225  ? 105 LEU   B CA   1 ? 1 
ATOM   1304 C C    . LEU   A 1 93  ? -15.628 -3.695  -0.439  1   42.717  ? 105 LEU   B C    1 ? 1 
ATOM   1305 O O    . LEU   A 1 93  ? -15.965 -4.523  0.427   1   39.388  ? 105 LEU   B O    1 ? 1 
ATOM   1306 C CB   . LEU   A 1 93  ? -16.817 -1.636  0.262   1   43.948  ? 105 LEU   B CB   1 ? 1 
ATOM   1307 C CG   . LEU   A 1 93  ? -17.659 -0.382  0.01    1   44.381  ? 105 LEU   B CG   1 ? 1 
ATOM   1308 C CD1  . LEU   A 1 93  ? -17.628 0.497   1.28    1   40.205  ? 105 LEU   B CD1  1 ? 1 
ATOM   1309 C CD2  . LEU   A 1 93  ? -17.195 0.426   -1.176  1   45.913  ? 105 LEU   B CD2  1 ? 1 
ATOM   1310 H H    . LEU   A 1 93  ? -18.275 -3.837  -0.644  1   46.467  ? 105 LEU   B H    1 c 1 
ATOM   1311 H HA   . LEU   A 1 93  ? -16.275 -2.16   -1.676  1   44.761  ? 105 LEU   B HA   1 c 1 
ATOM   1312 H HB2  . LEU   A 1 93  ? -17.215 -2.122  1.021   1   43.463  ? 105 LEU   B HB2  1 c 1 
ATOM   1313 H HB3  . LEU   A 1 93  ? -15.922 -1.347  0.556   1   42.691  ? 105 LEU   B HB3  1 c 1 
ATOM   1314 H HG   . LEU   A 1 93  ? -18.597 -0.663  -0.152  1   45.028  ? 105 LEU   B HG   1 c 1 
ATOM   1315 H HD11 . LEU   A 1 93  ? -18.001 0       2.028   1   40.928  ? 105 LEU   B HD11 1 c 1 
ATOM   1316 H HD12 . LEU   A 1 93  ? -18.154 1.301   1.132   1   41.812  ? 105 LEU   B HD12 1 c 1 
ATOM   1317 H HD13 . LEU   A 1 93  ? -16.71  0.744   1.482   1   40.271  ? 105 LEU   B HD13 1 c 1 
ATOM   1318 H HD21 . LEU   A 1 93  ? -17.334 -0.083  -1.992  1   46.822  ? 105 LEU   B HD21 1 c 1 
ATOM   1319 H HD22 . LEU   A 1 93  ? -16.25  0.631   -1.08   1   45.029  ? 105 LEU   B HD22 1 c 1 
ATOM   1320 H HD23 . LEU   A 1 93  ? -17.702 1.255   -1.223  1   46.326  ? 105 LEU   B HD23 1 c 1 
ATOM   1321 N N    . LEU   A 1 94  ? -14.423 -3.676  -1.028  1   37.087  ? 106 LEU   B N    1 ? 1 
ATOM   1322 C CA   . LEU   A 1 94  ? -13.289 -4.437  -0.535  1   36.892  ? 106 LEU   B CA   1 ? 1 
ATOM   1323 C C    . LEU   A 1 94  ? -12.238 -3.474  0.015   1   38.006  ? 106 LEU   B C    1 ? 1 
ATOM   1324 O O    . LEU   A 1 94  ? -11.806 -2.5    -0.661  1   42.463  ? 106 LEU   B O    1 ? 1 
ATOM   1325 C CB   . LEU   A 1 94  ? -12.71  -5.319  -1.649  1   40.066  ? 106 LEU   B CB   1 ? 1 
ATOM   1326 C CG   . LEU   A 1 94  ? -11.574 -6.258  -1.233  1   41.728  ? 106 LEU   B CG   1 ? 1 
ATOM   1327 C CD1  . LEU   A 1 94  ? -12.049 -7.346  -0.266  1   41.779  ? 106 LEU   B CD1  1 ? 1 
ATOM   1328 C CD2  . LEU   A 1 94  ? -10.972 -6.872  -2.477  1   49.261  ? 106 LEU   B CD2  1 ? 1 
ATOM   1329 H H    . LEU   A 1 94  ? -14.308 -3.164  -1.777  1   39.063  ? 106 LEU   B H    1 c 1 
ATOM   1330 H HA   . LEU   A 1 94  ? -13.601 -5.017  0.204   1   37.233  ? 106 LEU   B HA   1 c 1 
ATOM   1331 H HB2  . LEU   A 1 94  ? -13.442 -5.862  -2.022  1   41.191  ? 106 LEU   B HB2  1 c 1 
ATOM   1332 H HB3  . LEU   A 1 94  ? -12.38  -4.729  -2.366  1   40.699  ? 106 LEU   B HB3  1 c 1 
ATOM   1333 H HG   . LEU   A 1 94  ? -10.873 -5.722  -0.781  1   41.418  ? 106 LEU   B HG   1 c 1 
ATOM   1334 H HD11 . LEU   A 1 94  ? -12.361 -6.936  0.558   1   40.367  ? 106 LEU   B HD11 1 c 1 
ATOM   1335 H HD12 . LEU   A 1 94  ? -11.311 -7.948  -0.067  1   42.434  ? 106 LEU   B HD12 1 c 1 
ATOM   1336 H HD13 . LEU   A 1 94  ? -12.775 -7.848  -0.672  1   42.916  ? 106 LEU   B HD13 1 c 1 
ATOM   1337 H HD21 . LEU   A 1 94  ? -10.614 -6.17   -3.046  1   47.958  ? 106 LEU   B HD21 1 c 1 
ATOM   1338 H HD22 . LEU   A 1 94  ? -11.657 -7.363  -2.962  1   48.893  ? 106 LEU   B HD22 1 c 1 
ATOM   1339 H HD23 . LEU   A 1 94  ? -10.257 -7.48   -2.226  1   48.297  ? 106 LEU   B HD23 1 c 1 
ATOM   1340 N N    . ILE   A 1 95  ? -11.796 -3.76   1.233   1   34.227  ? 107 ILE   B N    1 ? 1 
ATOM   1341 C CA   . ILE   A 1 95  ? -11.115 -2.772  2.047   1   34.487  ? 107 ILE   B CA   1 ? 1 
ATOM   1342 C C    . ILE   A 1 95  ? -9.816  -3.328  2.63    1   35.653  ? 107 ILE   B C    1 ? 1 
ATOM   1343 O O    . ILE   A 1 95  ? -9.841  -4.259  3.44    1   33.85   ? 107 ILE   B O    1 ? 1 
ATOM   1344 C CB   . ILE   A 1 95  ? -12.055 -2.301  3.176   1   33.629  ? 107 ILE   B CB   1 ? 1 
ATOM   1345 C CG1  . ILE   A 1 95  ? -13.366 -1.74   2.642   1   34.675  ? 107 ILE   B CG1  1 ? 1 
ATOM   1346 C CG2  . ILE   A 1 95  ? -11.374 -1.277  4.064   1   35.457  ? 107 ILE   B CG2  1 ? 1 
ATOM   1347 C CD1  . ILE   A 1 95  ? -14.5   -1.768  3.646   1   35.568  ? 107 ILE   B CD1  1 ? 1 
ATOM   1348 H H    . ILE   A 1 95  ? -11.915 -4.601  1.571   1   35.386  ? 107 ILE   B H    1 c 1 
ATOM   1349 H HA   . ILE   A 1 95  ? -10.902 -2.003  1.487   1   34.738  ? 107 ILE   B HA   1 c 1 
ATOM   1350 H HB   . ILE   A 1 95  ? -12.269 -3.08   3.727   1   34.24   ? 107 ILE   B HB   1 c 1 
ATOM   1351 H HG12 . ILE   A 1 95  ? -13.219 -0.815  2.358   1   34.74   ? 107 ILE   B HG12 1 c 1 
ATOM   1352 H HG13 . ILE   A 1 95  ? -13.635 -2.254  1.855   1   35.266  ? 107 ILE   B HG13 1 c 1 
ATOM   1353 H HG21 . ILE   A 1 95  ? -12.027 -0.878  4.663   1   34.559  ? 107 ILE   B HG21 1 c 1 
ATOM   1354 H HG22 . ILE   A 1 95  ? -10.975 -0.582  3.514   1   35.121  ? 107 ILE   B HG22 1 c 1 
ATOM   1355 H HG23 . ILE   A 1 95  ? -10.68  -1.709  4.59    1   34.995  ? 107 ILE   B HG23 1 c 1 
ATOM   1356 H HD11 . ILE   A 1 95  ? -14.581 -2.665  4.021   1   35.497  ? 107 ILE   B HD11 1 c 1 
ATOM   1357 H HD12 . ILE   A 1 95  ? -15.335 -1.526  3.202   1   35.687  ? 107 ILE   B HD12 1 c 1 
ATOM   1358 H HD13 . ILE   A 1 95  ? -14.32  -1.132  4.364   1   34.968  ? 107 ILE   B HD13 1 c 1 
ATOM   1359 N N    . LYS   A 1 96  ? -8.7    -2.645  2.319   1   36.699  ? 108 LYS   B N    1 ? 1 
ATOM   1360 C CA   . LYS   A 1 96  ? -7.401  -2.94   2.902   1   38.522  ? 108 LYS   B CA   1 ? 1 
ATOM   1361 C C    . LYS   A 1 96  ? -7.332  -2.401  4.326   1   38.848  ? 108 LYS   B C    1 ? 1 
ATOM   1362 O O    . LYS   A 1 96  ? -8.065  -1.458  4.681   1   37.186  ? 108 LYS   B O    1 ? 1 
ATOM   1363 C CB   . LYS   A 1 96  ? -6.28   -2.345  2.028   1   39.365  ? 108 LYS   B CB   1 ? 1 
ATOM   1364 C CG   . LYS   A 1 96  ? -6.178  -2.908  0.63    1   42.413  ? 108 LYS   B CG   1 ? 1 
ATOM   1365 C CD   . LYS   A 1 96  ? -5.117  -2.318  -0.331  1   44.415  ? 108 LYS   B CD   1 ? 1 
ATOM   1366 C CE   . LYS   A 1 96  ? -4.986  -3.146  -1.582  1   45.847  ? 108 LYS   B CE   1 ? 1 
ATOM   1367 N NZ   . LYS   A 1 96  ? -4.203  -2.37   -2.529  1   50.923  ? 108 LYS   B NZ   1 ? 1 
ATOM   1368 H H    . LYS   A 1 96  ? -8.757  -1.964  1.712   1   37.042  ? 108 LYS   B H    1 c 1 
ATOM   1369 H HA   . LYS   A 1 96  ? -7.293  -3.924  2.927   1   38.823  ? 108 LYS   B HA   1 c 1 
ATOM   1370 H HB2  . LYS   A 1 96  ? -6.423  -1.377  1.959   1   39.788  ? 108 LYS   B HB2  1 c 1 
ATOM   1371 H HB3  . LYS   A 1 96  ? -5.421  -2.483  2.478   1   40.935  ? 108 LYS   B HB3  1 c 1 
ATOM   1372 H HG2  . LYS   A 1 96  ? -6.012  -3.872  0.711   1   42.486  ? 108 LYS   B HG2  1 c 1 
ATOM   1373 H HG3  . LYS   A 1 96  ? -7.058  -2.81   0.206   1   41.312  ? 108 LYS   B HG3  1 c 1 
ATOM   1374 H HD2  . LYS   A 1 96  ? -5.369  -1.403  -0.572  1   44.262  ? 108 LYS   B HD2  1 c 1 
ATOM   1375 H HD3  . LYS   A 1 96  ? -4.248  -2.287  0.127   1   45.299  ? 108 LYS   B HD3  1 c 1 
ATOM   1376 H HE2  . LYS   A 1 96  ? -4.532  -3.987  -1.391  1   47.285  ? 108 LYS   B HE2  1 c 1 
ATOM   1377 H HE3  . LYS   A 1 96  ? -5.863  -3.334  -1.96   1   45.906  ? 108 LYS   B HE3  1 c 1 
ATOM   1378 H HZ1  . LYS   A 1 96  ? -3.335  -2.36   -2.27   1   51.351  ? 108 LYS   B HZ1  1 c 1 
ATOM   1379 H HZ2  . LYS   A 1 96  ? -4.509  -1.519  -2.567  1   49.588  ? 108 LYS   B HZ2  1 c 1 
ATOM   1380 H HZ3  . LYS   A 1 96  ? -4.262  -2.745  -3.351  1   51.501  ? 108 LYS   B HZ3  1 c 1 
ATOM   1381 N N    . PRO   A 1 97  ? -6.438  -2.971  5.189   1   40.723  ? 109 PRO   B N    1 ? 1 
ATOM   1382 C CA   . PRO   A 1 97  ? -6.417  -2.67   6.613   1   41.245  ? 109 PRO   B CA   1 ? 1 
ATOM   1383 C C    . PRO   A 1 97  ? -6.242  -1.195  6.966   1   43.918  ? 109 PRO   B C    1 ? 1 
ATOM   1384 O O    . PRO   A 1 97  ? -6.78   -0.704  7.957   1   45.405  ? 109 PRO   B O    1 ? 1 
ATOM   1385 C CB   . PRO   A 1 97  ? -5.292  -3.521  7.195   1   43.063  ? 109 PRO   B CB   1 ? 1 
ATOM   1386 C CG   . PRO   A 1 97  ? -4.69   -4.3    6.084   1   43.703  ? 109 PRO   B CG   1 ? 1 
ATOM   1387 C CD   . PRO   A 1 97  ? -5.486  -4.035  4.814   1   45.601  ? 109 PRO   B CD   1 ? 1 
ATOM   1388 H HA   . PRO   A 1 97  ? -7.261  -2.98   7.004   1   40.756  ? 109 PRO   B HA   1 c 1 
ATOM   1389 H HB2  . PRO   A 1 97  ? -4.617  -2.954  7.616   1   44.019  ? 109 PRO   B HB2  1 c 1 
ATOM   1390 H HB3  . PRO   A 1 97  ? -5.642  -4.123  7.88    1   43.011  ? 109 PRO   B HB3  1 c 1 
ATOM   1391 H HG2  . PRO   A 1 97  ? -3.758  -4.035  5.953   1   45.828  ? 109 PRO   B HG2  1 c 1 
ATOM   1392 H HG3  . PRO   A 1 97  ? -4.707  -5.254  6.293   1   44.902  ? 109 PRO   B HG3  1 c 1 
ATOM   1393 H HD2  . PRO   A 1 97  ? -4.901  -3.736  4.094   1   44.927  ? 109 PRO   B HD2  1 c 1 
ATOM   1394 H HD3  . PRO   A 1 97  ? -5.963  -4.837  4.527   1   43.862  ? 109 PRO   B HD3  1 c 1 
ATOM   1395 N N    . GLU   A 1 98  ? -5.531  -0.468  6.113   1   43.563  ? 110 GLU   B N    1 ? 1 
ATOM   1396 C CA   . GLU   A 1 98  ? -5.28   0.955   6.326   1   45.893  ? 110 GLU   B CA   1 ? 1 
ATOM   1397 C C    . GLU   A 1 98  ? -6.572  1.777   6.416   1   40.484  ? 110 GLU   B C    1 ? 1 
ATOM   1398 O O    . GLU   A 1 98  ? -6.554  2.815   7.037   1   39.521  ? 110 GLU   B O    1 ? 1 
ATOM   1399 C CB   . GLU   A 1 98  ? -4.375  1.431   5.183   1   47.926  ? 110 GLU   B CB   1 ? 1 
ATOM   1400 C CG   . GLU   A 1 98  ? -2.976  0.826   5.226   1   55.521  ? 110 GLU   B CG   1 ? 1 
ATOM   1401 C CD   . GLU   A 1 98  ? -2.769  -0.6    4.743   1   60.876  ? 110 GLU   B CD   1 ? 1 
ATOM   1402 O OE1  . GLU   A 1 98  ? -3.638  -1.177  4.024   1   51.34   ? 110 GLU   B OE1  1 ? 1 
ATOM   1403 O OE2  . GLU   A 1 98  ? -1.691  -1.119  5.149   1   66.943  ? 110 GLU   B OE2  1 ? 1 
ATOM   1404 H H    . GLU   A 1 98  ? -5.196  -0.865  5.362   1   44.612  ? 110 GLU   B H    1 c 1 
ATOM   1405 H HA   . GLU   A 1 98  ? -4.787  1.056   7.18    1   45.96   ? 110 GLU   B HA   1 c 1 
ATOM   1406 H HB2  . GLU   A 1 98  ? -4.798  1.205   4.329   1   48.25   ? 110 GLU   B HB2  1 c 1 
ATOM   1407 H HB3  . GLU   A 1 98  ? -4.298  2.407   5.229   1   49.864  ? 110 GLU   B HB3  1 c 1 
ATOM   1408 H HG2  . GLU   A 1 98  ? -2.381  1.403   4.702   1   57.068  ? 110 GLU   B HG2  1 c 1 
ATOM   1409 H HG3  . GLU   A 1 98  ? -2.655  0.873   6.152   1   56.017  ? 110 GLU   B HG3  1 c 1 
ATOM   1410 N N    . TYR   A 1 99  ? -7.655  1.331   5.785   1   37.296  ? 111 TYR   B N    1 ? 1 
ATOM   1411 C CA   . TYR   A 1 99  ? -8.915  2.029   5.79    1   38.118  ? 111 TYR   B CA   1 ? 1 
ATOM   1412 C C    . TYR   A 1 99  ? -9.93   1.292   6.708   1   38.991  ? 111 TYR   B C    1 ? 1 
ATOM   1413 O O    . TYR   A 1 99  ? -11.114 1.578   6.668   1   38.527  ? 111 TYR   B O    1 ? 1 
ATOM   1414 C CB   . TYR   A 1 99  ? -9.372  2.193   4.343   1   35.295  ? 111 TYR   B CB   1 ? 1 
ATOM   1415 C CG   . TYR   A 1 99  ? -8.436  3.068   3.499   1   38.764  ? 111 TYR   B CG   1 ? 1 
ATOM   1416 C CD1  . TYR   A 1 99  ? -7.263  2.587   2.959   1   38.124  ? 111 TYR   B CD1  1 ? 1 
ATOM   1417 C CD2  . TYR   A 1 99  ? -8.669  4.437   3.374   1   41.09   ? 111 TYR   B CD2  1 ? 1 
ATOM   1418 C CE1  . TYR   A 1 99  ? -6.394  3.405   2.238   1   41.18   ? 111 TYR   B CE1  1 ? 1 
ATOM   1419 C CE2  . TYR   A 1 99  ? -7.833  5.265   2.653   1   43.542  ? 111 TYR   B CE2  1 ? 1 
ATOM   1420 C CZ   . TYR   A 1 99  ? -6.675  4.747   2.093   1   43.077  ? 111 TYR   B CZ   1 ? 1 
ATOM   1421 O OH   . TYR   A 1 99  ? -5.892  5.573   1.372   1   46.018  ? 111 TYR   B OH   1 ? 1 
ATOM   1422 H H    . TYR   A 1 99  ? -7.598  0.55    5.314   1   37.736  ? 111 TYR   B H    1 c 1 
ATOM   1423 H HA   . TYR   A 1 99  ? -8.766  2.936   6.165   1   38.483  ? 111 TYR   B HA   1 c 1 
ATOM   1424 H HB2  . TYR   A 1 99  ? -9.434  1.302   3.931   1   35.748  ? 111 TYR   B HB2  1 c 1 
ATOM   1425 H HB3  . TYR   A 1 99  ? -10.269 2.593   4.342   1   35.939  ? 111 TYR   B HB3  1 c 1 
ATOM   1426 H HD1  . TYR   A 1 99  ? -7.058  1.67    3.05    1   38.247  ? 111 TYR   B HD1  1 c 1 
ATOM   1427 H HD2  . TYR   A 1 99  ? -9.456  4.801   3.749   1   40.376  ? 111 TYR   B HD2  1 c 1 
ATOM   1428 H HE1  . TYR   A 1 99  ? -5.62   3.042   1.843   1   42.305  ? 111 TYR   B HE1  1 c 1 
ATOM   1429 H HE2  . TYR   A 1 99  ? -8.039  6.178   2.553   1   44.185  ? 111 TYR   B HE2  1 c 1 
ATOM   1430 H HH   . TYR   A 1 99  ? -5.173  5.189   1.019   0   30      ? 111 TYR   B HH   1 c 1 
ATOM   1431 N N    . ALA   A 1 100 ? -9.462  0.34    7.528   1   39.183  ? 112 ALA   B N    1 ? 1 
ATOM   1432 C CA   . ALA   A 1 100 ? -10.321 -0.41   8.431   1   36.715  ? 112 ALA   B CA   1 ? 1 
ATOM   1433 C C    . ALA   A 1 100 ? -9.737  -0.362  9.838   1   36.502  ? 112 ALA   B C    1 ? 1 
ATOM   1434 O O    . ALA   A 1 100 ? -9.793  0.693   10.486  1   35.542  ? 112 ALA   B O    1 ? 1 
ATOM   1435 C CB   . ALA   A 1 100 ? -10.511 -1.819  7.884   1   37.996  ? 112 ALA   B CB   1 ? 1 
ATOM   1436 H H    . ALA   A 1 100 ? -8.568  0.156   7.531   1   39.212  ? 112 ALA   B H    1 c 1 
ATOM   1437 H HA   . ALA   A 1 100 ? -11.208 0.04    8.458   1   36.939  ? 112 ALA   B HA   1 c 1 
ATOM   1438 H HB1  . ALA   A 1 100 ? -11.052 -1.785  7.078   1   36.891  ? 112 ALA   B HB1  1 c 1 
ATOM   1439 H HB2  . ALA   A 1 100 ? -9.645  -2.208  7.673   1   37.811  ? 112 ALA   B HB2  1 c 1 
ATOM   1440 H HB3  . ALA   A 1 100 ? -10.959 -2.37   8.548   1   37.806  ? 112 ALA   B HB3  1 c 1 
ATOM   1441 N N    . TYR   A 1 101 ? -9.125  -1.454  10.318  1   39.015  ? 113 TYR   B N    1 ? 1 
ATOM   1442 C CA   . TYR   A 1 101 ? -8.651  -1.522  11.699  1   40.269  ? 113 TYR   B CA   1 ? 1 
ATOM   1443 C C    . TYR   A 1 101 ? -7.142  -1.653  11.817  1   43.699  ? 113 TYR   B C    1 ? 1 
ATOM   1444 O O    . TYR   A 1 101 ? -6.622  -1.861  12.914  1   42.778  ? 113 TYR   B O    1 ? 1 
ATOM   1445 C CB   . TYR   A 1 101 ? -9.327  -2.702  12.39   1   42.464  ? 113 TYR   B CB   1 ? 1 
ATOM   1446 C CG   . TYR   A 1 101 ? -10.833 -2.514  12.482  1   39.666  ? 113 TYR   B CG   1 ? 1 
ATOM   1447 C CD1  . TYR   A 1 101 ? -11.403 -1.706  13.428  1   42.362  ? 113 TYR   B CD1  1 ? 1 
ATOM   1448 C CD2  . TYR   A 1 101 ? -11.683 -3.071  11.545  1   38.166  ? 113 TYR   B CD2  1 ? 1 
ATOM   1449 C CE1  . TYR   A 1 101 ? -12.774 -1.526  13.508  1   41.591  ? 113 TYR   B CE1  1 ? 1 
ATOM   1450 C CE2  . TYR   A 1 101 ? -13.045 -2.869  11.583  1   38.584  ? 113 TYR   B CE2  1 ? 1 
ATOM   1451 C CZ   . TYR   A 1 101 ? -13.613 -2.15   12.61   1   39.809  ? 113 TYR   B CZ   1 ? 1 
ATOM   1452 O OH   . TYR   A 1 101 ? -14.954 -1.946  12.656  1   40.435  ? 113 TYR   B OH   1 ? 1 
ATOM   1453 H H    . TYR   A 1 101 ? -8.997  -2.178  9.775   1   38.085  ? 113 TYR   B H    1 c 1 
ATOM   1454 H HA   . TYR   A 1 101 ? -8.928  -0.694  12.166  1   41.648  ? 113 TYR   B HA   1 c 1 
ATOM   1455 H HB2  . TYR   A 1 101 ? -9.132  -3.522  11.885  1   41.316  ? 113 TYR   B HB2  1 c 1 
ATOM   1456 H HB3  . TYR   A 1 101 ? -8.959  -2.796  13.296  1   43.198  ? 113 TYR   B HB3  1 c 1 
ATOM   1457 H HD1  . TYR   A 1 101 ? -10.852 -1.314  14.086  1   43.035  ? 113 TYR   B HD1  1 c 1 
ATOM   1458 H HD2  . TYR   A 1 101 ? -11.32  -3.606  10.857  1   37.747  ? 113 TYR   B HD2  1 c 1 
ATOM   1459 H HE1  . TYR   A 1 101 ? -13.138 -1.002  14.201  1   42.933  ? 113 TYR   B HE1  1 c 1 
ATOM   1460 H HE2  . TYR   A 1 101 ? -13.6   -3.305  10.959  1   38.048  ? 113 TYR   B HE2  1 c 1 
ATOM   1461 H HH   . TYR   A 1 101 ? -15.114 -1.419  13.381  0   30      ? 113 TYR   B HH   1 c 1 
ATOM   1462 N N    . GLY   A 1 102 ? -6.437  -1.523  10.688  1   41.81   ? 114 GLY   B N    1 ? 1 
ATOM   1463 C CA   . GLY   A 1 102 ? -5.012  -1.261  10.714  1   46.374  ? 114 GLY   B CA   1 ? 1 
ATOM   1464 C C    . GLY   A 1 102 ? -4.191  -2.412  11.288  1   48.664  ? 114 GLY   B C    1 ? 1 
ATOM   1465 O O    . GLY   A 1 102 ? -4.653  -3.558  11.39   1   46.599  ? 114 GLY   B O    1 ? 1 
ATOM   1466 H H    . GLY   A 1 102 ? -6.853  -1.607  9.879   1   41.392  ? 114 GLY   B H    1 c 1 
ATOM   1467 H HA2  . GLY   A 1 102 ? -4.708  -1.076  9.794   1   45.44   ? 114 GLY   B HA2  1 c 1 
ATOM   1468 H HA3  . GLY   A 1 102 ? -4.85   -0.45   11.25   1   46.846  ? 114 GLY   B HA3  1 c 1 
ATOM   1469 N N    . SER   A 1 103 ? -2.97   -2.071  11.722  1   50.703  ? 115 SER   B N    1 ? 1 
ATOM   1470 C CA   . SER   A 1 103 ? -2.093  -3.13   12.162  1   52.196  ? 115 SER   B CA   1 ? 1 
ATOM   1471 C C    . SER   A 1 103 ? -2.509  -3.575  13.552  1   52.038  ? 115 SER   B C    1 ? 1 
ATOM   1472 O O    . SER   A 1 103 ? -2.278  -4.72   13.92   1   55.996  ? 115 SER   B O    1 ? 1 
ATOM   1473 C CB   . SER   A 1 103 ? -0.636  -2.812  11.992  1   55.52   ? 115 SER   B CB   1 ? 1 
ATOM   1474 O OG   . SER   A 1 103 ? -0.079  -2.034  13.025  1   57.326  ? 115 SER   B OG   1 ? 1 
ATOM   1475 H H    . SER   A 1 103 ? -2.691  -1.201  11.742  1   51.339  ? 115 SER   B H    1 c 1 
ATOM   1476 H HA   . SER   A 1 103 ? -2.274  -3.899  11.572  1   51.214  ? 115 SER   B HA   1 c 1 
ATOM   1477 H HB2  . SER   A 1 103 ? -0.14   -3.651  11.933  1   56.344  ? 115 SER   B HB2  1 c 1 
ATOM   1478 H HB3  . SER   A 1 103 ? -0.515  -2.344  11.145  1   54.514  ? 115 SER   B HB3  1 c 1 
ATOM   1479 H HG   . SER   A 1 103 ? 0.713   -1.92   12.87   0   30      ? 115 SER   B HG   1 c 1 
ATOM   1480 N N    . ALA   A 1 104 ? -3.167  -2.698  14.321  1   53.536  ? 116 ALA   B N    1 ? 1 
ATOM   1481 C CA   . ALA   A 1 104 ? -3.582  -3.055  15.668  1   52.99   ? 116 ALA   B CA   1 ? 1 
ATOM   1482 C C    . ALA   A 1 104 ? -4.788  -3.985  15.621  1   51.094  ? 116 ALA   B C    1 ? 1 
ATOM   1483 O O    . ALA   A 1 104 ? -4.996  -4.771  16.55   1   53.686  ? 116 ALA   B O    1 ? 1 
ATOM   1484 C CB   . ALA   A 1 104 ? -3.926  -1.836  16.482  1   56.24   ? 116 ALA   B CB   1 ? 1 
ATOM   1485 H H    . ALA   A 1 104 ? -3.353  -1.86   14.007  1   51.781  ? 116 ALA   B H    1 c 1 
ATOM   1486 H HA   . ALA   A 1 104 ? -2.831  -3.539  16.111  1   56.062  ? 116 ALA   B HA   1 c 1 
ATOM   1487 H HB1  . ALA   A 1 104 ? -3.147  -1.26   16.554  1   57.136  ? 116 ALA   B HB1  1 c 1 
ATOM   1488 H HB2  . ALA   A 1 104 ? -4.648  -1.348  16.051  1   53.619  ? 116 ALA   B HB2  1 c 1 
ATOM   1489 H HB3  . ALA   A 1 104 ? -4.209  -2.106  17.372  1   57.172  ? 116 ALA   B HB3  1 c 1 
ATOM   1490 N N    . GLY   A 1 105 ? -5.628  -3.799  14.604  1   47.629  ? 117 GLY   B N    1 ? 1 
ATOM   1491 C CA   . GLY   A 1 105 ? -6.865  -4.553  14.517  1   46.974  ? 117 GLY   B CA   1 ? 1 
ATOM   1492 C C    . GLY   A 1 105 ? -7.8    -4.13   15.643  1   48.152  ? 117 GLY   B C    1 ? 1 
ATOM   1493 O O    . GLY   A 1 105 ? -7.659  -3.016  16.143  1   47.742  ? 117 GLY   B O    1 ? 1 
ATOM   1494 H H    . GLY   A 1 105 ? -5.434  -3.188  13.953  1   46.757  ? 117 GLY   B H    1 c 1 
ATOM   1495 H HA2  . GLY   A 1 105 ? -7.291  -4.386  13.645  1   44.907  ? 117 GLY   B HA2  1 c 1 
ATOM   1496 H HA3  . GLY   A 1 105 ? -6.668  -5.517  14.586  1   47.775  ? 117 GLY   B HA3  1 c 1 
ATOM   1497 N N    . SER   A 1 106 ? -8.761  -5.016  15.971  1   46.865  ? 118 SER   B N    1 ? 1 
ATOM   1498 C CA   . SER   A 1 106 ? -9.765  -4.756  16.965  1   49.757  ? 118 SER   B CA   1 ? 1 
ATOM   1499 C C    . SER   A 1 106 ? -10.164 -6.088  17.573  1   53.633  ? 118 SER   B C    1 ? 1 
ATOM   1500 O O    . SER   A 1 106 ? -11.276 -6.592  17.358  1   52.932  ? 118 SER   B O    1 ? 1 
ATOM   1501 C CB   . SER   A 1 106 ? -10.932 -4.006  16.403  1   47.411  ? 118 SER   B CB   1 ? 1 
ATOM   1502 O OG   . SER   A 1 106 ? -11.753 -3.672  17.495  1   48.227  ? 118 SER   B OG   1 ? 1 
ATOM   1503 H H    . SER   A 1 106 ? -8.774  -5.823  15.543  1   47.295  ? 118 SER   B H    1 c 1 
ATOM   1504 H HA   . SER   A 1 106 ? -9.357  -4.203  17.679  1   51.28   ? 118 SER   B HA   1 c 1 
ATOM   1505 H HB2  . SER   A 1 106 ? -10.625 -3.197  15.952  1   45.759  ? 118 SER   B HB2  1 c 1 
ATOM   1506 H HB3  . SER   A 1 106 ? -11.42  -4.566  15.771  1   45.989  ? 118 SER   B HB3  1 c 1 
ATOM   1507 H HG   . SER   A 1 106 ? -12.437 -3.314  17.222  0   30      ? 118 SER   B HG   1 c 1 
ATOM   1508 N N    . LEU   A 1 107 ? -9.212  -6.617  18.343  1   55.725  ? 119 LEU   B N    1 ? 1 
ATOM   1509 C CA   . LEU   A 1 107 ? -9.267  -7.976  18.826  1   60.641  ? 119 LEU   B CA   1 ? 1 
ATOM   1510 C C    . LEU   A 1 107 ? -10.367 -8.146  19.868  1   64.776  ? 119 LEU   B C    1 ? 1 
ATOM   1511 O O    . LEU   A 1 107 ? -10.657 -7.239  20.65   1   72.68   ? 119 LEU   B O    1 ? 1 
ATOM   1512 C CB   . LEU   A 1 107 ? -7.877  -8.315  19.358  1   63.572  ? 119 LEU   B CB   1 ? 1 
ATOM   1513 C CG   . LEU   A 1 107 ? -6.833  -8.512  18.239  1   65.414  ? 119 LEU   B CG   1 ? 1 
ATOM   1514 C CD1  . LEU   A 1 107 ? -5.414  -8.712  18.745  1   70.144  ? 119 LEU   B CD1  1 ? 1 
ATOM   1515 C CD2  . LEU   A 1 107 ? -7.248  -9.678  17.407  1   63.121  ? 119 LEU   B CD2  1 ? 1 
ATOM   1516 H H    . LEU   A 1 107 ? -8.496  -6.1    18.576  1   56.8    ? 119 LEU   B H    1 c 1 
ATOM   1517 H HA   . LEU   A 1 107 ? -9.473  -8.557  18.056  1   59.137  ? 119 LEU   B HA   1 c 1 
ATOM   1518 H HB2  . LEU   A 1 107 ? -7.577  -7.586  19.948  1   65.26   ? 119 LEU   B HB2  1 c 1 
ATOM   1519 H HB3  . LEU   A 1 107 ? -7.937  -9.146  19.884  1   66.94   ? 119 LEU   B HB3  1 c 1 
ATOM   1520 H HG   . LEU   A 1 107 ? -6.842  -7.705  17.662  1   62.174  ? 119 LEU   B HG   1 c 1 
ATOM   1521 H HD11 . LEU   A 1 107 ? -5.154  -7.952  19.292  1   70.427  ? 119 LEU   B HD11 1 c 1 
ATOM   1522 H HD12 . LEU   A 1 107 ? -4.807  -8.789  17.989  1   68.391  ? 119 LEU   B HD12 1 c 1 
ATOM   1523 H HD13 . LEU   A 1 107 ? -5.371  -9.524  19.278  1   72.207  ? 119 LEU   B HD13 1 c 1 
ATOM   1524 H HD21 . LEU   A 1 107 ? -7.985  -9.421  16.828  1   61.255  ? 119 LEU   B HD21 1 c 1 
ATOM   1525 H HD22 . LEU   A 1 107 ? -7.529  -10.408 17.984  1   65.975  ? 119 LEU   B HD22 1 c 1 
ATOM   1526 H HD23 . LEU   A 1 107 ? -6.499  -9.97   16.86   1   63.303  ? 119 LEU   B HD23 1 c 1 
ATOM   1527 N N    . PRO   A 1 108 ? -11     -9.337  19.946  1   66.068  ? 120 PRO   B N    1 ? 1 
ATOM   1528 C CA   . PRO   A 1 108 ? -10.744 -10.447 19.036  1   62.997  ? 120 PRO   B CA   1 ? 1 
ATOM   1529 C C    . PRO   A 1 108 ? -11.577 -10.467 17.757  1   57.987  ? 120 PRO   B C    1 ? 1 
ATOM   1530 O O    . PRO   A 1 108 ? -11.395 -11.382 16.97   1   58.864  ? 120 PRO   B O    1 ? 1 
ATOM   1531 C CB   . PRO   A 1 108 ? -11.139 -11.656 19.875  1   69.123  ? 120 PRO   B CB   1 ? 1 
ATOM   1532 C CG   . PRO   A 1 108 ? -12.323 -11.109 20.647  1   71.438  ? 120 PRO   B CG   1 ? 1 
ATOM   1533 C CD   . PRO   A 1 108 ? -11.968 -9.689  20.999  1   70.227  ? 120 PRO   B CD   1 ? 1 
ATOM   1534 H HA   . PRO   A 1 108 ? -9.791  -10.493 18.818  1   62.842  ? 120 PRO   B HA   1 c 1 
ATOM   1535 H HB2  . PRO   A 1 108 ? -11.399 -12.413 19.314  1   68.965  ? 120 PRO   B HB2  1 c 1 
ATOM   1536 H HB3  . PRO   A 1 108 ? -10.416 -11.922 20.476  1   71.238  ? 120 PRO   B HB3  1 c 1 
ATOM   1537 H HG2  . PRO   A 1 108 ? -13.134 -11.132 20.1    1   70.116  ? 120 PRO   B HG2  1 c 1 
ATOM   1538 H HG3  . PRO   A 1 108 ? -12.477 -11.631 21.454  1   75.121  ? 120 PRO   B HG3  1 c 1 
ATOM   1539 H HD2  . PRO   A 1 108 ? -12.75  -9.105  20.964  1   69.364  ? 120 PRO   B HD2  1 c 1 
ATOM   1540 H HD3  . PRO   A 1 108 ? -11.557 -9.631  21.883  1   72.842  ? 120 PRO   B HD3  1 c 1 
ATOM   1541 N N    . LYS   A 1 109 ? -12.503 -9.509  17.548  1   55.718  ? 121 LYS   B N    1 ? 1 
ATOM   1542 C CA   . LYS   A 1 109 ? -13.385 -9.544  16.373  1   53.597  ? 121 LYS   B CA   1 ? 1 
ATOM   1543 C C    . LYS   A 1 109 ? -12.594 -9.345  15.072  1   47.621  ? 121 LYS   B C    1 ? 1 
ATOM   1544 O O    . LYS   A 1 109 ? -12.816 -10.034 14.094  1   45.097  ? 121 LYS   B O    1 ? 1 
ATOM   1545 C CB   . LYS   A 1 109 ? -14.585 -8.582  16.454  1   50.729  ? 121 LYS   B CB   1 ? 1 
ATOM   1546 H H    . LYS   A 1 109 ? -12.587 -8.822  18.144  1   56.377  ? 121 LYS   B H    1 c 1 
ATOM   1547 H HA   . LYS   A 1 109 ? -13.777 -10.454 16.334  1   54.423  ? 121 LYS   B HA   1 c 1 
ATOM   1548 H HB2  . LYS   A 1 109 ? -14.251 -7.699  16.678  0   30      ? 121 LYS   B HB2  1 c 1 
ATOM   1549 H HB3  . LYS   A 1 109 ? -15.424 -9.127  16.476  0   30      ? 121 LYS   B HB3  1 c 1 
ATOM   1550 N N    . ILE   A 1 110 ? -11.66  -8.398  15.042  1   47.819  ? 122 ILE   B N    1 ? 1 
ATOM   1551 C CA   . ILE   A 1 110 ? -10.891 -8.112  13.844  1   44.35   ? 122 ILE   B CA   1 ? 1 
ATOM   1552 C C    . ILE   A 1 110 ? -9.416  -8.399  14.092  1   46.114  ? 122 ILE   B C    1 ? 1 
ATOM   1553 O O    . ILE   A 1 110 ? -8.823  -7.716  14.914  1   45.082  ? 122 ILE   B O    1 ? 1 
ATOM   1554 C CB   . ILE   A 1 110 ? -11.05  -6.639  13.44   1   43.385  ? 122 ILE   B CB   1 ? 1 
ATOM   1555 C CG1  . ILE   A 1 110 ? -12.467 -6.146  13.62   1   44.086  ? 122 ILE   B CG1  1 ? 1 
ATOM   1556 C CG2  . ILE   A 1 110 ? -10.535 -6.45   12.006  1   42.032  ? 122 ILE   B CG2  1 ? 1 
ATOM   1557 C CD1  . ILE   A 1 110 ? -13.487 -6.823  12.728  1   43.04   ? 122 ILE   B CD1  1 ? 1 
ATOM   1558 H H    . ILE   A 1 110 ? -11.497 -7.907  15.796  1   48.083  ? 122 ILE   B H    1 c 1 
ATOM   1559 H HA   . ILE   A 1 110 ? -11.211 -8.673  13.114  1   44.437  ? 122 ILE   B HA   1 c 1 
ATOM   1560 H HB   . ILE   A 1 110 ? -10.481 -6.107  14.03   1   43.949  ? 122 ILE   B HB   1 c 1 
ATOM   1561 H HG12 . ILE   A 1 110 ? -12.731 -6.276  14.553  1   45.651  ? 122 ILE   B HG12 1 c 1 
ATOM   1562 H HG13 . ILE   A 1 110 ? -12.486 -5.184  13.438  1   42.558  ? 122 ILE   B HG13 1 c 1 
ATOM   1563 H HG21 . ILE   A 1 110 ? -10.706 -5.541  11.716  1   40.456  ? 122 ILE   B HG21 1 c 1 
ATOM   1564 H HG22 . ILE   A 1 110 ? -10.991 -7.069  11.411  1   41.545  ? 122 ILE   B HG22 1 c 1 
ATOM   1565 H HG23 . ILE   A 1 110 ? -9.578  -6.622  11.976  1   42.137  ? 122 ILE   B HG23 1 c 1 
ATOM   1566 H HD11 . ILE   A 1 110 ? -13.314 -6.59   11.797  1   41.502  ? 122 ILE   B HD11 1 c 1 
ATOM   1567 H HD12 . ILE   A 1 110 ? -14.381 -6.519  12.976  1   43.716  ? 122 ILE   B HD12 1 c 1 
ATOM   1568 H HD13 . ILE   A 1 110 ? -13.435 -7.791  12.834  1   44.544  ? 122 ILE   B HD13 1 c 1 
ATOM   1569 N N    . PRO   A 1 111 ? -8.74   -9.3    13.332  1   45.98   ? 123 PRO   B N    1 ? 1 
ATOM   1570 C CA   . PRO   A 1 111 ? -7.321  -9.525  13.57   1   48.571  ? 123 PRO   B CA   1 ? 1 
ATOM   1571 C C    . PRO   A 1 111 ? -6.487  -8.354  13.057  1   47.78   ? 123 PRO   B C    1 ? 1 
ATOM   1572 O O    . PRO   A 1 111 ? -6.984  -7.479  12.335  1   45.85   ? 123 PRO   B O    1 ? 1 
ATOM   1573 C CB   . PRO   A 1 111 ? -7.01   -10.889 12.903  1   49.975  ? 123 PRO   B CB   1 ? 1 
ATOM   1574 C CG   . PRO   A 1 111 ? -8.222  -11.222 12.028  1   48.405  ? 123 PRO   B CG   1 ? 1 
ATOM   1575 C CD   . PRO   A 1 111 ? -9.31   -10.175 12.292  1   45.845  ? 123 PRO   B CD   1 ? 1 
ATOM   1576 H HA   . PRO   A 1 111 ? -7.174  -9.616  14.535  1   50.479  ? 123 PRO   B HA   1 c 1 
ATOM   1577 H HB2  . PRO   A 1 111 ? -6.2    -10.831 12.36   1   49.759  ? 123 PRO   B HB2  1 c 1 
ATOM   1578 H HB3  . PRO   A 1 111 ? -6.875  -11.58  13.581  1   52.4    ? 123 PRO   B HB3  1 c 1 
ATOM   1579 H HG2  . PRO   A 1 111 ? -7.97   -11.21  11.083  1   47.265  ? 123 PRO   B HG2  1 c 1 
ATOM   1580 H HG3  . PRO   A 1 111 ? -8.559  -12.114 12.243  1   50.227  ? 123 PRO   B HG3  1 c 1 
ATOM   1581 H HD2  . PRO   A 1 111 ? -9.509  -9.663  11.484  1   43.946  ? 123 PRO   B HD2  1 c 1 
ATOM   1582 H HD3  . PRO   A 1 111 ? -10.131 -10.598 12.612  1   46.967  ? 123 PRO   B HD3  1 c 1 
ATOM   1583 N N    . SER   A 1 112 ? -5.209  -8.361  13.425  1   50.933  ? 124 SER   B N    1 ? 1 
ATOM   1584 C CA   . SER   A 1 112 ? -4.251  -7.431  12.851  1   51.059  ? 124 SER   B CA   1 ? 1 
ATOM   1585 C C    . SER   A 1 112 ? -4.232  -7.567  11.325  1   51.002  ? 124 SER   B C    1 ? 1 
ATOM   1586 O O    . SER   A 1 112 ? -4.29   -8.677  10.799  1   49.643  ? 124 SER   B O    1 ? 1 
ATOM   1587 C CB   . SER   A 1 112 ? -2.91   -7.665  13.447  1   54.889  ? 124 SER   B CB   1 ? 1 
ATOM   1588 O OG   . SER   A 1 112 ? -2.399  -8.899  12.997  1   64.003  ? 124 SER   B OG   1 ? 1 
ATOM   1589 H H    . SER   A 1 112 ? -4.923  -8.964  14.05   1   52.967  ? 124 SER   B H    1 c 1 
ATOM   1590 H HA   . SER   A 1 112 ? -4.54   -6.512  13.08   1   50.386  ? 124 SER   B HA   1 c 1 
ATOM   1591 H HB2  . SER   A 1 112 ? -2.306  -6.948  13.182  1   56.268  ? 124 SER   B HB2  1 c 1 
ATOM   1592 H HB3  . SER   A 1 112 ? -2.98   -7.672  14.421  1   57.792  ? 124 SER   B HB3  1 c 1 
ATOM   1593 H HG   . SER   A 1 112 ? -1.612  -9.117  13.318  0   30      ? 124 SER   B HG   1 c 1 
ATOM   1594 N N    . ASN   A 1 113 ? -4.191  -6.411  10.647  1   47.819  ? 125 ASN   B N    1 ? 1 
ATOM   1595 C CA   . ASN   A 1 113 ? -3.928  -6.305  9.222   1   47.349  ? 125 ASN   B CA   1 ? 1 
ATOM   1596 C C    . ASN   A 1 113 ? -5.042  -7.01   8.43    1   45.16   ? 125 ASN   B C    1 ? 1 
ATOM   1597 O O    . ASN   A 1 113 ? -4.758  -7.671  7.438   1   39.901  ? 125 ASN   B O    1 ? 1 
ATOM   1598 C CB   . ASN   A 1 113 ? -2.519  -6.819  8.903   1   51.763  ? 125 ASN   B CB   1 ? 1 
ATOM   1599 C CG   . ASN   A 1 113 ? -1.396  -6.156  9.694   1   51.891  ? 125 ASN   B CG   1 ? 1 
ATOM   1600 O OD1  . ASN   A 1 113 ? -0.533  -6.825  10.272  1   51.674  ? 125 ASN   B OD1  1 ? 1 
ATOM   1601 N ND2  . ASN   A 1 113 ? -1.322  -4.839  9.667   1   50.113  ? 125 ASN   B ND2  1 ? 1 
ATOM   1602 H H    . ASN   A 1 113 ? -4.339  -5.637  11.11   1   47.911  ? 125 ASN   B H    1 c 1 
ATOM   1603 H HA   . ASN   A 1 113 ? -3.949  -5.352  8.985   1   46.562  ? 125 ASN   B HA   1 c 1 
ATOM   1604 H HB2  . ASN   A 1 113 ? -2.492  -7.782  9.071   1   51.931  ? 125 ASN   B HB2  1 c 1 
ATOM   1605 H HB3  . ASN   A 1 113 ? -2.348  -6.683  7.95    1   50.517  ? 125 ASN   B HB3  1 c 1 
ATOM   1606 H HD21 . ASN   A 1 113 ? -0.544  -4.442  9.818   1   52.15   ? 125 ASN   B HD21 1 c 1 
ATOM   1607 H HD22 . ASN   A 1 113 ? -2.037  -4.351  9.478   1   48.689  ? 125 ASN   B HD22 1 c 1 
ATOM   1608 N N    . ALA   A 1 114 ? -6.31   -6.883  8.871   1   43.71   ? 126 ALA   B N    1 ? 1 
ATOM   1609 C CA   . ALA   A 1 114 ? -7.415  -7.574  8.199   1   44.548  ? 126 ALA   B CA   1 ? 1 
ATOM   1610 C C    . ALA   A 1 114 ? -7.943  -6.779  6.993   1   42.019  ? 126 ALA   B C    1 ? 1 
ATOM   1611 O O    . ALA   A 1 114 ? -8.123  -5.558  7.058   1   34.428  ? 126 ALA   B O    1 ? 1 
ATOM   1612 C CB   . ALA   A 1 114 ? -8.528  -7.873  9.194   1   43.801  ? 126 ALA   B CB   1 ? 1 
ATOM   1613 H H    . ALA   A 1 114 ? -6.491  -6.354  9.594   1   43.913  ? 126 ALA   B H    1 c 1 
ATOM   1614 H HA   . ALA   A 1 114 ? -7.064  -8.442  7.858   1   45.04   ? 126 ALA   B HA   1 c 1 
ATOM   1615 H HB1  . ALA   A 1 114 ? -8.181  -8.422  9.918   1   45.601  ? 126 ALA   B HB1  1 c 1 
ATOM   1616 H HB2  . ALA   A 1 114 ? -8.872  -7.041  9.56    1   43.267  ? 126 ALA   B HB2  1 c 1 
ATOM   1617 H HB3  . ALA   A 1 114 ? -9.248  -8.349  8.747   1   44.011  ? 126 ALA   B HB3  1 c 1 
ATOM   1618 N N    . THR   A 1 115 ? -8.167  -7.502  5.882   1   38.019  ? 127 THR   B N    1 ? 1 
ATOM   1619 C CA   . THR   A 1 115 ? -8.981  -7.034  4.772   1   37.712  ? 127 THR   B CA   1 ? 1 
ATOM   1620 C C    . THR   A 1 115 ? -10.447 -7.372  5.034   1   38.592  ? 127 THR   B C    1 ? 1 
ATOM   1621 O O    . THR   A 1 115 ? -10.758 -8.459  5.491   1   39.01   ? 127 THR   B O    1 ? 1 
ATOM   1622 C CB   . THR   A 1 115 ? -8.458  -7.668  3.481   1   40.046  ? 127 THR   B CB   1 ? 1 
ATOM   1623 O OG1  . THR   A 1 115 ? -7.156  -7.111  3.3     1   38.905  ? 127 THR   B OG1  1 ? 1 
ATOM   1624 C CG2  . THR   A 1 115 ? -9.245  -7.266  2.248   1   41.144  ? 127 THR   B CG2  1 ? 1 
ATOM   1625 H H    . THR   A 1 115 ? -7.788  -8.331  5.817   1   40.54   ? 127 THR   B H    1 c 1 
ATOM   1626 H HA   . THR   A 1 115 ? -8.884  -6.061  4.705   1   37.01   ? 127 THR   B HA   1 c 1 
ATOM   1627 H HB   . THR   A 1 115 ? -8.398  -8.649  3.563   1   41.173  ? 127 THR   B HB   1 c 1 
ATOM   1628 H HG1  . THR   A 1 115 ? -7.095  -6.293  3.286   0   30      ? 127 THR   B HG1  1 c 1 
ATOM   1629 H HG21 . THR   A 1 115 ? -8.879  -7.719  1.47    1   42.061  ? 127 THR   B HG21 1 c 1 
ATOM   1630 H HG22 . THR   A 1 115 ? -9.182  -6.306  2.121   1   39.784  ? 127 THR   B HG22 1 c 1 
ATOM   1631 H HG23 . THR   A 1 115 ? -10.177 -7.517  2.358   1   40.556  ? 127 THR   B HG23 1 c 1 
ATOM   1632 N N    . LEU   A 1 116 ? -11.364 -6.444  4.734   1   39.872  ? 128 LEU   B N    1 ? 1 
ATOM   1633 C CA   . LEU   A 1 116 ? -12.783 -6.655  4.99    1   38.247  ? 128 LEU   B CA   1 ? 1 
ATOM   1634 C C    . LEU   A 1 116 ? -13.551 -6.489  3.686   1   37.694  ? 128 LEU   B C    1 ? 1 
ATOM   1635 O O    . LEU   A 1 116 ? -13.147 -5.704  2.832   1   34.264  ? 128 LEU   B O    1 ? 1 
ATOM   1636 C CB   . LEU   A 1 116 ? -13.414 -5.69   6       1   39.402  ? 128 LEU   B CB   1 ? 1 
ATOM   1637 C CG   . LEU   A 1 116 ? -12.644 -5.325  7.281   1   41.174  ? 128 LEU   B CG   1 ? 1 
ATOM   1638 C CD1  . LEU   A 1 116 ? -13.651 -4.66   8.246   1   42.465  ? 128 LEU   B CD1  1 ? 1 
ATOM   1639 C CD2  . LEU   A 1 116 ? -11.968 -6.452  7.927   1   43.171  ? 128 LEU   B CD2  1 ? 1 
ATOM   1640 H H    . LEU   A 1 116 ? -11.098 -5.655  4.356   1   38.106  ? 128 LEU   B H    1 c 1 
ATOM   1641 H HA   . LEU   A 1 116 ? -12.908 -7.583  5.311   1   39.946  ? 128 LEU   B HA   1 c 1 
ATOM   1642 H HB2  . LEU   A 1 116 ? -13.62  -4.852  5.525   1   38.561  ? 128 LEU   B HB2  1 c 1 
ATOM   1643 H HB3  . LEU   A 1 116 ? -14.284 -6.067  6.267   1   40.125  ? 128 LEU   B HB3  1 c 1 
ATOM   1644 H HG   . LEU   A 1 116 ? -11.956 -4.651  7.045   1   40.468  ? 128 LEU   B HG   1 c 1 
ATOM   1645 H HD11 . LEU   A 1 116 ? -14.06  -3.893  7.811   1   41.467  ? 128 LEU   B HD11 1 c 1 
ATOM   1646 H HD12 . LEU   A 1 116 ? -13.186 -4.367  9.047   1   42.34   ? 128 LEU   B HD12 1 c 1 
ATOM   1647 H HD13 . LEU   A 1 116 ? -14.341 -5.3    8.489   1   43.099  ? 128 LEU   B HD13 1 c 1 
ATOM   1648 H HD21 . LEU   A 1 116 ? -11.15  -6.659  7.448   1   42.92   ? 128 LEU   B HD21 1 c 1 
ATOM   1649 H HD22 . LEU   A 1 116 ? -12.552 -7.227  7.917   1   43.92   ? 128 LEU   B HD22 1 c 1 
ATOM   1650 H HD23 . LEU   A 1 116 ? -11.753 -6.22   8.846   1   43.327  ? 128 LEU   B HD23 1 c 1 
ATOM   1651 N N    . PHE   A 1 117 ? -14.689 -7.19   3.597   1   38.796  ? 129 PHE   B N    1 ? 1 
ATOM   1652 C CA   . PHE   A 1 117 ? -15.639 -7.072  2.499   1   40.424  ? 129 PHE   B CA   1 ? 1 
ATOM   1653 C C    . PHE   A 1 117 ? -16.983 -6.693  3.113   1   40.482  ? 129 PHE   B C    1 ? 1 
ATOM   1654 O O    . PHE   A 1 117 ? -17.39  -7.293  4.11    1   41.824  ? 129 PHE   B O    1 ? 1 
ATOM   1655 C CB   . PHE   A 1 117 ? -15.733 -8.354  1.676   1   43.635  ? 129 PHE   B CB   1 ? 1 
ATOM   1656 C CG   . PHE   A 1 117 ? -16.847 -8.378  0.632   1   46.58   ? 129 PHE   B CG   1 ? 1 
ATOM   1657 C CD1  . PHE   A 1 117 ? -16.634 -7.913  -0.656  1   46.29   ? 129 PHE   B CD1  1 ? 1 
ATOM   1658 C CD2  . PHE   A 1 117 ? -18.107 -8.879  0.94    1   51.431  ? 129 PHE   B CD2  1 ? 1 
ATOM   1659 C CE1  . PHE   A 1 117 ? -17.646 -7.916  -1.601  1   48.98   ? 129 PHE   B CE1  1 ? 1 
ATOM   1660 C CE2  . PHE   A 1 117 ? -19.127 -8.89   -0.007  1   54.131  ? 129 PHE   B CE2  1 ? 1 
ATOM   1661 C CZ   . PHE   A 1 117 ? -18.901 -8.391  -1.274  1   53.391  ? 129 PHE   B CZ   1 ? 1 
ATOM   1662 H H    . PHE   A 1 117 ? -14.884 -7.78   4.267   1   39.822  ? 129 PHE   B H    1 c 1 
ATOM   1663 H HA   . PHE   A 1 117 ? -15.342 -6.337  1.904   1   39.557  ? 129 PHE   B HA   1 c 1 
ATOM   1664 H HB2  . PHE   A 1 117 ? -14.873 -8.492  1.221   1   43.687  ? 129 PHE   B HB2  1 c 1 
ATOM   1665 H HB3  . PHE   A 1 117 ? -15.865 -9.107  2.293   1   44.683  ? 129 PHE   B HB3  1 c 1 
ATOM   1666 H HD1  . PHE   A 1 117 ? -15.788 -7.564  -0.886  1   45.711  ? 129 PHE   B HD1  1 c 1 
ATOM   1667 H HD2  . PHE   A 1 117 ? -18.276 -9.2    1.811   1   50.982  ? 129 PHE   B HD2  1 c 1 
ATOM   1668 H HE1  . PHE   A 1 117 ? -17.48  -7.584  -2.469  1   49.998  ? 129 PHE   B HE1  1 c 1 
ATOM   1669 H HE2  . PHE   A 1 117 ? -19.979 -9.224  0.224   1   55.391  ? 129 PHE   B HE2  1 c 1 
ATOM   1670 H HZ   . PHE   A 1 117 ? -19.585 -8.415  -1.923  1   54.791  ? 129 PHE   B HZ   1 c 1 
ATOM   1671 N N    . PHE   A 1 118 ? -17.7   -5.788  2.443   1   40.357  ? 130 PHE   B N    1 ? 1 
ATOM   1672 C CA   . PHE   A 1 118 ? -19.064 -5.436  2.806   1   43.846  ? 130 PHE   B CA   1 ? 1 
ATOM   1673 C C    . PHE   A 1 118 ? -19.955 -5.391  1.577   1   46.4    ? 130 PHE   B C    1 ? 1 
ATOM   1674 O O    . PHE   A 1 118 ? -19.534 -4.928  0.513   1   45.002  ? 130 PHE   B O    1 ? 1 
ATOM   1675 C CB   . PHE   A 1 118 ? -19.273 -4.05   3.429   1   40.771  ? 130 PHE   B CB   1 ? 1 
ATOM   1676 C CG   . PHE   A 1 118 ? -18.606 -3.92   4.774   1   39.617  ? 130 PHE   B CG   1 ? 1 
ATOM   1677 C CD1  . PHE   A 1 118 ? -17.251 -3.623  4.859   1   39.395  ? 130 PHE   B CD1  1 ? 1 
ATOM   1678 C CD2  . PHE   A 1 118 ? -19.329 -4.099  5.943   1   43.027  ? 130 PHE   B CD2  1 ? 1 
ATOM   1679 C CE1  . PHE   A 1 118 ? -16.635 -3.499  6.083   1   38.265  ? 130 PHE   B CE1  1 ? 1 
ATOM   1680 C CE2  . PHE   A 1 118 ? -18.71  -3.962  7.157   1   42.58   ? 130 PHE   B CE2  1 ? 1 
ATOM   1681 C CZ   . PHE   A 1 118 ? -17.371 -3.665  7.226   1   42.643  ? 130 PHE   B CZ   1 ? 1 
ATOM   1682 H H    . PHE   A 1 118 ? -17.321 -5.37   1.724   1   40.441  ? 130 PHE   B H    1 c 1 
ATOM   1683 H HA   . PHE   A 1 118 ? -19.413 -6.121  3.431   1   44.229  ? 130 PHE   B HA   1 c 1 
ATOM   1684 H HB2  . PHE   A 1 118 ? -18.906 -3.37   2.821   1   40.37   ? 130 PHE   B HB2  1 c 1 
ATOM   1685 H HB3  . PHE   A 1 118 ? -20.237 -3.889  3.532   1   42.433  ? 130 PHE   B HB3  1 c 1 
ATOM   1686 H HD1  . PHE   A 1 118 ? -16.751 -3.503  4.067   1   38.411  ? 130 PHE   B HD1  1 c 1 
ATOM   1687 H HD2  . PHE   A 1 118 ? -20.252 -4.295  5.9     1   44.049  ? 130 PHE   B HD2  1 c 1 
ATOM   1688 H HE1  . PHE   A 1 118 ? -15.715 -3.293  6.134   1   38.303  ? 130 PHE   B HE1  1 c 1 
ATOM   1689 H HE2  . PHE   A 1 118 ? -19.206 -4.082  7.951   1   44.198  ? 130 PHE   B HE2  1 c 1 
ATOM   1690 H HZ   . PHE   A 1 118 ? -16.953 -3.584  8.068   1   41.413  ? 130 PHE   B HZ   1 c 1 
ATOM   1691 N N    . GLU   A 1 119 ? -21.207 -5.819  1.775   1   46.961  ? 131 GLU   B N    1 ? 1 
ATOM   1692 C CA   . GLU   A 1 119 ? -22.296 -5.397  0.912   1   51.991  ? 131 GLU   B CA   1 ? 1 
ATOM   1693 C C    . GLU   A 1 119 ? -23.083 -4.342  1.68    1   54.295  ? 131 GLU   B C    1 ? 1 
ATOM   1694 O O    . GLU   A 1 119 ? -23.489 -4.611  2.808   1   58.337  ? 131 GLU   B O    1 ? 1 
ATOM   1695 C CB   . GLU   A 1 119 ? -23.173 -6.596  0.541   1   56.773  ? 131 GLU   B CB   1 ? 1 
ATOM   1696 C CG   . GLU   A 1 119 ? -24.325 -6.23   -0.385  1   61.664  ? 131 GLU   B CG   1 ? 1 
ATOM   1697 C CD   . GLU   A 1 119 ? -25.113 -7.458  -0.799  1   69.188  ? 131 GLU   B CD   1 ? 1 
ATOM   1698 O OE1  . GLU   A 1 119 ? -24.871 -8.084  -1.886  1   69.348  ? 131 GLU   B OE1  1 ? 1 
ATOM   1699 O OE2  . GLU   A 1 119 ? -25.991 -7.787  0.051   1   69.078  ? 131 GLU   B OE2  1 ? 1 
ATOM   1700 H H    . GLU   A 1 119 ? -21.387 -6.392  2.465   1   48.768  ? 131 GLU   B H    1 c 1 
ATOM   1701 H HA   . GLU   A 1 119 ? -21.919 -4.995  0.09    1   51.493  ? 131 GLU   B HA   1 c 1 
ATOM   1702 H HB2  . GLU   A 1 119 ? -22.614 -7.273  0.106   1   57.141  ? 131 GLU   B HB2  1 c 1 
ATOM   1703 H HB3  . GLU   A 1 119 ? -23.534 -6.989  1.363   1   57.774  ? 131 GLU   B HB3  1 c 1 
ATOM   1704 H HG2  . GLU   A 1 119 ? -24.928 -5.605  0.071   1   62.114  ? 131 GLU   B HG2  1 c 1 
ATOM   1705 H HG3  . GLU   A 1 119 ? -23.976 -5.79   -1.187  1   61.293  ? 131 GLU   B HG3  1 c 1 
ATOM   1706 N N    . ILE   A 1 120 ? -23.301 -3.167  1.077   1   56.266  ? 132 ILE   B N    1 ? 1 
ATOM   1707 C CA   . ILE   A 1 120 ? -24.027 -2.092  1.736   1   51.7    ? 132 ILE   B CA   1 ? 1 
ATOM   1708 C C    . ILE   A 1 120 ? -25.241 -1.687  0.906   1   55.329  ? 132 ILE   B C    1 ? 1 
ATOM   1709 O O    . ILE   A 1 120 ? -25.14  -1.451  -0.289  1   52.325  ? 132 ILE   B O    1 ? 1 
ATOM   1710 C CB   . ILE   A 1 120 ? -23.124 -0.886  2.036   1   50.824  ? 132 ILE   B CB   1 ? 1 
ATOM   1711 C CG1  . ILE   A 1 120 ? -21.865 -1.279  2.837   1   46.178  ? 132 ILE   B CG1  1 ? 1 
ATOM   1712 C CG2  . ILE   A 1 120 ? -23.918 0.201   2.772   1   50.187  ? 132 ILE   B CG2  1 ? 1 
ATOM   1713 C CD1  . ILE   A 1 120 ? -20.802 -0.172  2.899   1   46.523  ? 132 ILE   B CD1  1 ? 1 
ATOM   1714 H H    . ILE   A 1 120 ? -22.989 -3.032  0.228   1   54.357  ? 132 ILE   B H    1 c 1 
ATOM   1715 H HA   . ILE   A 1 120 ? -24.352 -2.433  2.592   1   53.652  ? 132 ILE   B HA   1 c 1 
ATOM   1716 H HB   . ILE   A 1 120 ? -22.828 -0.516  1.181   1   49.542  ? 132 ILE   B HB   1 c 1 
ATOM   1717 H HG12 . ILE   A 1 120 ? -22.132 -1.512  3.749   1   47.536  ? 132 ILE   B HG12 1 c 1 
ATOM   1718 H HG13 . ILE   A 1 120 ? -21.466 -2.074  2.429   1   46.963  ? 132 ILE   B HG13 1 c 1 
ATOM   1719 H HG21 . ILE   A 1 120 ? -23.327 0.934   3.01    1   49.395  ? 132 ILE   B HG21 1 c 1 
ATOM   1720 H HG22 . ILE   A 1 120 ? -24.309 -0.172  3.58    1   51.468  ? 132 ILE   B HG22 1 c 1 
ATOM   1721 H HG23 . ILE   A 1 120 ? -24.626 0.535   2.196   1   52.441  ? 132 ILE   B HG23 1 c 1 
ATOM   1722 H HD11 . ILE   A 1 120 ? -20.603 0.139   1.996   1   45.835  ? 132 ILE   B HD11 1 c 1 
ATOM   1723 H HD12 . ILE   A 1 120 ? -19.989 -0.526  3.306   1   44.524  ? 132 ILE   B HD12 1 c 1 
ATOM   1724 H HD13 . ILE   A 1 120 ? -21.132 0.575   3.434   1   46.156  ? 132 ILE   B HD13 1 c 1 
ATOM   1725 N N    . GLU   A 1 121 ? -26.406 -1.622  1.578   1   58.495  ? 133 GLU   B N    1 ? 1 
ATOM   1726 C CA   . GLU   A 1 121 ? -27.581 -0.957  1.039   1   61.598  ? 133 GLU   B CA   1 ? 1 
ATOM   1727 C C    . GLU   A 1 121 ? -27.804 0.393   1.719   1   62.481  ? 133 GLU   B C    1 ? 1 
ATOM   1728 O O    . GLU   A 1 121 ? -28.053 0.435   2.92    1   62.271  ? 133 GLU   B O    1 ? 1 
ATOM   1729 C CB   . GLU   A 1 121 ? -28.798 -1.849  1.243   1   65.003  ? 133 GLU   B CB   1 ? 1 
ATOM   1730 C CG   . GLU   A 1 121 ? -30.071 -1.182  0.728   1   69.519  ? 133 GLU   B CG   1 ? 1 
ATOM   1731 C CD   . GLU   A 1 121 ? -31.203 -2.131  0.451   1   72.282  ? 133 GLU   B CD   1 ? 1 
ATOM   1732 O OE1  . GLU   A 1 121 ? -31.042 -3.359  0.629   1   73.095  ? 133 GLU   B OE1  1 ? 1 
ATOM   1733 O OE2  . GLU   A 1 121 ? -32.233 -1.592  0.027   1   74.256  ? 133 GLU   B OE2  1 ? 1 
ATOM   1734 H H    . GLU   A 1 121 ? -26.466 -2.012  2.402   1   58.375  ? 133 GLU   B H    1 c 1 
ATOM   1735 H HA   . GLU   A 1 121 ? -27.449 -0.815  0.069   1   61.855  ? 133 GLU   B HA   1 c 1 
ATOM   1736 H HB2  . GLU   A 1 121 ? -28.651 -2.697  0.775   1   65.675  ? 133 GLU   B HB2  1 c 1 
ATOM   1737 H HB3  . GLU   A 1 121 ? -28.893 -2.045  2.199   1   65.291  ? 133 GLU   B HB3  1 c 1 
ATOM   1738 H HG2  . GLU   A 1 121 ? -30.374 -0.524  1.387   1   69.327  ? 133 GLU   B HG2  1 c 1 
ATOM   1739 H HG3  . GLU   A 1 121 ? -29.863 -0.697  -0.099  1   68.563  ? 133 GLU   B HG3  1 c 1 
ATOM   1740 N N    . LEU   A 1 122 ? -27.732 1.481   0.943   1   64.2    ? 134 LEU   B N    1 ? 1 
ATOM   1741 C CA   . LEU   A 1 122 ? -28.063 2.815   1.433   1   66.161  ? 134 LEU   B CA   1 ? 1 
ATOM   1742 C C    . LEU   A 1 122 ? -29.577 3.037   1.404   1   72.503  ? 134 LEU   B C    1 ? 1 
ATOM   1743 O O    . LEU   A 1 122 ? -30.153 3.294   0.346   1   76.673  ? 134 LEU   B O    1 ? 1 
ATOM   1744 C CB   . LEU   A 1 122 ? -27.331 3.897   0.637   1   64.944  ? 134 LEU   B CB   1 ? 1 
ATOM   1745 C CG   . LEU   A 1 122 ? -27.575 5.34    1.094   1   64.847  ? 134 LEU   B CG   1 ? 1 
ATOM   1746 C CD1  . LEU   A 1 122 ? -27.305 5.489   2.591   1   63.704  ? 134 LEU   B CD1  1 ? 1 
ATOM   1747 C CD2  . LEU   A 1 122 ? -26.742 6.347   0.322   1   63.181  ? 134 LEU   B CD2  1 ? 1 
ATOM   1748 H H    . LEU   A 1 122 ? -27.464 1.391   0.074   1   63.837  ? 134 LEU   B H    1 c 1 
ATOM   1749 H HA   . LEU   A 1 122 ? -27.766 2.867   2.376   1   64.935  ? 134 LEU   B HA   1 c 1 
ATOM   1750 H HB2  . LEU   A 1 122 ? -26.364 3.714   0.688   1   61.971  ? 134 LEU   B HB2  1 c 1 
ATOM   1751 H HB3  . LEU   A 1 122 ? -27.6   3.82    -0.307  1   66.042  ? 134 LEU   B HB3  1 c 1 
ATOM   1752 H HG   . LEU   A 1 122 ? -28.53  5.555   0.935   1   67.912  ? 134 LEU   B HG   1 c 1 
ATOM   1753 H HD11 . LEU   A 1 122 ? -28.011 5.051   3.095   1   65.219  ? 134 LEU   B HD11 1 c 1 
ATOM   1754 H HD12 . LEU   A 1 122 ? -27.281 6.432   2.824   1   64.462  ? 134 LEU   B HD12 1 c 1 
ATOM   1755 H HD13 . LEU   A 1 122 ? -26.451 5.081   2.81    1   61.076  ? 134 LEU   B HD13 1 c 1 
ATOM   1756 H HD21 . LEU   A 1 122 ? -26.926 6.263   -0.627  1   64.566  ? 134 LEU   B HD21 1 c 1 
ATOM   1757 H HD22 . LEU   A 1 122 ? -25.798 6.18    0.484   1   60.862  ? 134 LEU   B HD22 1 c 1 
ATOM   1758 H HD23 . LEU   A 1 122 ? -26.965 7.246   0.615   1   64.799  ? 134 LEU   B HD23 1 c 1 
ATOM   1759 N N    . LEU   A 1 123 ? -30.209 2.965   2.583   1   73.345  ? 135 LEU   B N    1 ? 1 
ATOM   1760 C CA   . LEU   A 1 123 ? -31.661 3.044   2.691   1   76.665  ? 135 LEU   B CA   1 ? 1 
ATOM   1761 C C    . LEU   A 1 123 ? -32.114 4.501   2.588   1   79.177  ? 135 LEU   B C    1 ? 1 
ATOM   1762 O O    . LEU   A 1 123 ? -32.941 4.835   1.742   1   80.13   ? 135 LEU   B O    1 ? 1 
ATOM   1763 C CB   . LEU   A 1 123 ? -32.127 2.425   4.009   1   78.203  ? 135 LEU   B CB   1 ? 1 
ATOM   1764 C CG   . LEU   A 1 123 ? -31.706 0.977   4.291   1   77.057  ? 135 LEU   B CG   1 ? 1 
ATOM   1765 C CD1  . LEU   A 1 123 ? -32.078 0.589   5.716   1   79.024  ? 135 LEU   B CD1  1 ? 1 
ATOM   1766 C CD2  . LEU   A 1 123 ? -32.349 -0.015  3.334   1   78.57   ? 135 LEU   B CD2  1 ? 1 
ATOM   1767 H H    . LEU   A 1 123 ? -29.718 2.868   3.348   1   71.345  ? 135 LEU   B H    1 c 1 
ATOM   1768 H HA   . LEU   A 1 123 ? -32.058 2.538   1.938   1   78.6    ? 135 LEU   B HA   1 c 1 
ATOM   1769 H HB2  . LEU   A 1 123 ? -31.795 2.989   4.745   1   77.281  ? 135 LEU   B HB2  1 c 1 
ATOM   1770 H HB3  . LEU   A 1 123 ? -33.11  2.47    4.035   1   82.102  ? 135 LEU   B HB3  1 c 1 
ATOM   1771 H HG   . LEU   A 1 123 ? -30.721 0.911   4.196   1   73.224  ? 135 LEU   B HG   1 c 1 
ATOM   1772 H HD11 . LEU   A 1 123 ? -31.66  1.206   6.34    1   77.606  ? 135 LEU   B HD11 1 c 1 
ATOM   1773 H HD12 . LEU   A 1 123 ? -31.77  -0.314  5.899   1   78.216  ? 135 LEU   B HD12 1 c 1 
ATOM   1774 H HD13 . LEU   A 1 123 ? -33.044 0.629   5.823   1   82.844  ? 135 LEU   B HD13 1 c 1 
ATOM   1775 H HD21 . LEU   A 1 123 ? -32.242 0.295   2.419   1   78.48   ? 135 LEU   B HD21 1 c 1 
ATOM   1776 H HD22 . LEU   A 1 123 ? -33.295 -0.094  3.54    1   82.688  ? 135 LEU   B HD22 1 c 1 
ATOM   1777 H HD23 . LEU   A 1 123 ? -31.924 -0.884  3.432   1   77.673  ? 135 LEU   B HD23 1 c 1 
ATOM   1778 N N    . ASP   A 1 124 ? -31.56  5.363   3.46    1   77.279  ? 136 ASP   B N    1 ? 1 
ATOM   1779 C CA   . ASP   A 1 124 ? -31.943 6.769   3.532   1   80.253  ? 136 ASP   B CA   1 ? 1 
ATOM   1780 C C    . ASP   A 1 124 ? -30.809 7.569   4.172   1   76.872  ? 136 ASP   B C    1 ? 1 
ATOM   1781 O O    . ASP   A 1 124 ? -29.942 6.994   4.825   1   72.97   ? 136 ASP   B O    1 ? 1 
ATOM   1782 C CB   . ASP   A 1 124 ? -33.235 6.945   4.322   1   86.975  ? 136 ASP   B CB   1 ? 1 
ATOM   1783 C CG   . ASP   A 1 124 ? -34.027 8.221   4.061   1   93.212  ? 136 ASP   B CG   1 ? 1 
ATOM   1784 O OD1  . ASP   A 1 124 ? -34.888 8.228   3.157   1   97.107  ? 136 ASP   B OD1  1 ? 1 
ATOM   1785 O OD2  . ASP   A 1 124 ? -33.776 9.216   4.757   1   99.394  ? 136 ASP   B OD2  1 ? 1 
ATOM   1786 H H    . ASP   A 1 124 ? -30.919 5.057   4.036   1   75.037  ? 136 ASP   B H    1 c 1 
ATOM   1787 H HA   . ASP   A 1 124 ? -32.087 7.101   2.617   1   81.294  ? 136 ASP   B HA   1 c 1 
ATOM   1788 H HB2  . ASP   A 1 124 ? -33.824 6.186   4.128   1   88.59   ? 136 ASP   B HB2  1 c 1 
ATOM   1789 H HB3  . ASP   A 1 124 ? -33.022 6.916   5.279   1   86.417  ? 136 ASP   B HB3  1 c 1 
ATOM   1790 N N    . PHE   A 1 125 ? -30.832 8.896   3.981   1   78.497  ? 137 PHE   B N    1 ? 1 
ATOM   1791 C CA   . PHE   A 1 125 ? -29.948 9.806   4.695   1   78.972  ? 137 PHE   B CA   1 ? 1 
ATOM   1792 C C    . PHE   A 1 125 ? -30.612 11.18   4.806   1   83.358  ? 137 PHE   B C    1 ? 1 
ATOM   1793 O O    . PHE   A 1 125 ? -31.164 11.679  3.828   1   88.47   ? 137 PHE   B O    1 ? 1 
ATOM   1794 C CB   . PHE   A 1 125 ? -28.568 9.941   4.042   1   76.377  ? 137 PHE   B CB   1 ? 1 
ATOM   1795 C CG   . PHE   A 1 125 ? -28.547 10.463  2.608   1   78.332  ? 137 PHE   B CG   1 ? 1 
ATOM   1796 C CD1  . PHE   A 1 125 ? -28.708 9.606   1.524   1   74.561  ? 137 PHE   B CD1  1 ? 1 
ATOM   1797 C CD2  . PHE   A 1 125 ? -28.36  11.82   2.343   1   79.218  ? 137 PHE   B CD2  1 ? 1 
ATOM   1798 C CE1  . PHE   A 1 125 ? -28.684 10.101  0.23    1   76.423  ? 137 PHE   B CE1  1 ? 1 
ATOM   1799 C CE2  . PHE   A 1 125 ? -28.348 12.306  1.043   1   79.235  ? 137 PHE   B CE2  1 ? 1 
ATOM   1800 C CZ   . PHE   A 1 125 ? -28.503 11.448  -0.007  1   79.297  ? 137 PHE   B CZ   1 ? 1 
ATOM   1801 H H    . PHE   A 1 125 ? -31.421 9.246   3.375   1   81.422  ? 137 PHE   B H    1 c 1 
ATOM   1802 H HA   . PHE   A 1 125 ? -29.821 9.448   5.611   1   78.096  ? 137 PHE   B HA   1 c 1 
ATOM   1803 H HB2  . PHE   A 1 125 ? -28.024 10.541  4.599   1   75.897  ? 137 PHE   B HB2  1 c 1 
ATOM   1804 H HB3  . PHE   A 1 125 ? -28.134 9.059   4.059   1   73.637  ? 137 PHE   B HB3  1 c 1 
ATOM   1805 H HD1  . PHE   A 1 125 ? -28.831 8.682   1.673   1   74.237  ? 137 PHE   B HD1  1 c 1 
ATOM   1806 H HD2  . PHE   A 1 125 ? -28.254 12.42   3.064   1   79.978  ? 137 PHE   B HD2  1 c 1 
ATOM   1807 H HE1  . PHE   A 1 125 ? -28.795 9.509   -0.497  1   76.421  ? 137 PHE   B HE1  1 c 1 
ATOM   1808 H HE2  . PHE   A 1 125 ? -28.221 13.228  0.886   1   81.583  ? 137 PHE   B HE2  1 c 1 
ATOM   1809 H HZ   . PHE   A 1 125 ? -28.491 11.776  -0.892  1   80.328  ? 137 PHE   B HZ   1 c 1 
ATOM   1810 N N    . LYS   A 1 126 ? -30.521 11.779  6.005   1   82.872  ? 138 LYS   B N    1 ? 1 
ATOM   1811 C CA   . LYS   A 1 126 ? -31.145 13.061  6.328   1   86.481  ? 138 LYS   B CA   1 ? 1 
ATOM   1812 C C    . LYS   A 1 126 ? -30.063 14.016  6.849   1   83.883  ? 138 LYS   B C    1 ? 1 
ATOM   1813 O O    . LYS   A 1 126 ? -29.013 13.598  7.334   1   78.561  ? 138 LYS   B O    1 ? 1 
ATOM   1814 C CB   . LYS   A 1 126 ? -32.325 12.862  7.299   1   88.3    ? 138 LYS   B CB   1 ? 1 
ATOM   1815 H H    . LYS   A 1 126 ? -30.037 11.364  6.66    1   81.014  ? 138 LYS   B H    1 c 1 
ATOM   1816 H HA   . LYS   A 1 126 ? -31.51  13.444  5.49    1   87.629  ? 138 LYS   B HA   1 c 1 
ATOM   1817 H HB2  . LYS   A 1 126 ? -32.017 12.692  8.17    0   30      ? 138 LYS   B HB2  1 c 1 
ATOM   1818 H HB3  . LYS   A 1 126 ? -33.231 13.008  6.798   0   30      ? 138 LYS   B HB3  1 c 1 
ATOM   1819 N N    . GLY   A 1 127 ? -30.319 15.322  6.723   1   88.484  ? 139 GLY   B N    1 ? 1 
ATOM   1820 C CA   . GLY   A 1 127 ? -29.403 16.327  7.236   1   89.763  ? 139 GLY   B CA   1 ? 1 
ATOM   1821 C C    . GLY   A 1 127 ? -29.443 16.389  8.76    1   92.337  ? 139 GLY   B C    1 ? 1 
ATOM   1822 O O    . GLY   A 1 127 ? -30.486 16.149  9.364   1   93.884  ? 139 GLY   B O    1 ? 1 
ATOM   1823 H H    . GLY   A 1 127 ? -31.088 15.594  6.311   1   91.453  ? 139 GLY   B H    1 c 1 
ATOM   1824 H HA2  . GLY   A 1 127 ? -28.488 16.115  6.935   1   86.358  ? 139 GLY   B HA2  1 c 1 
ATOM   1825 H HA3  . GLY   A 1 127 ? -29.649 17.206  6.864   1   92.858  ? 139 GLY   B HA3  1 c 1 
ATOM   1826 N N    . GLU   A 1 128 ? -28.288 16.682  9.373   1   91.954  ? 140 GLU   B N    1 ? 1 
ATOM   1827 C CA   . GLU   A 1 128 ? -28.278 17.28   10.703  1   96.516  ? 140 GLU   B CA   1 ? 1 
ATOM   1828 C C    . GLU   A 1 128 ? -29.141 18.567  10.658  1   102.289 ? 140 GLU   B C    1 ? 1 
ATOM   1829 O O    . GLU   A 1 128 ? -29.425 19.038  9.528   1   102.974 ? 140 GLU   B O    1 ? 1 
ATOM   1830 C CB   . GLU   A 1 128 ? -26.837 17.479  11.186  1   93.74   ? 140 GLU   B CB   1 ? 1 
ATOM   1831 O OXT  . GLU   A 1 128 ? -29.539 19.046  11.743  1   106.963 ? 140 GLU   B OXT  1 ? 1 
ATOM   1832 H H    . GLU   A 1 128 ? -27.494 16.504  8.956   1   88.746  ? 140 GLU   B H    1 c 1 
ATOM   1833 H HA   . GLU   A 1 128 ? -28.714 16.643  11.324  1   96.247  ? 140 GLU   B HA   1 c 1 
ATOM   1834 H HB2  . GLU   A 1 128 ? -26.171 17.178  10.489  0   30      ? 140 GLU   B HB2  1 c 1 
ATOM   1835 H HB3  . GLU   A 1 128 ? -26.821 17.869  12.085  0   30      ? 140 GLU   B HB3  1 c 1 
ATOM   1836 N N    . THR   B 1 5   ? -0.397  3.426   44.008  1   89.401  ? 17  THR   A N    1 ? 2 
ATOM   1837 C CA   . THR   B 1 5   ? -1.608  3.909   43.291  1   88.889  ? 17  THR   A CA   1 ? 2 
ATOM   1838 C C    . THR   B 1 5   ? -2.085  2.836   42.303  1   90.168  ? 17  THR   A C    1 ? 2 
ATOM   1839 O O    . THR   B 1 5   ? -1.366  1.875   42.024  1   87.575  ? 17  THR   A O    1 ? 2 
ATOM   1840 C CB   . THR   B 1 5   ? -1.34   5.247   42.589  1   83.612  ? 17  THR   A CB   1 ? 2 
ATOM   1841 O OG1  . THR   B 1 5   ? -0.513  4.976   41.463  1   85.367  ? 17  THR   A OG1  1 ? 2 
ATOM   1842 C CG2  . THR   B 1 5   ? -0.652  6.281   43.463  1   82.242  ? 17  THR   A CG2  1 ? 2 
ATOM   1843 H H    . THR   B 1 5   ? -0.222  3.966   44.709  1   91.268  ? 17  THR   A H    1 c 2 
ATOM   1844 H HA   . THR   B 1 5   ? -2.316  4.051   43.957  1   88.204  ? 17  THR   A HA   1 c 2 
ATOM   1845 H HB   . THR   B 1 5   ? -2.197  5.623   42.275  1   81.427  ? 17  THR   A HB   1 c 2 
ATOM   1846 H HG1  . THR   B 1 5   ? 0.304   4.76    41.909  0   30      ? 17  THR   A HG1  1 c 2 
ATOM   1847 H HG21 . THR   B 1 5   ? -0.587  7.122   42.979  1   80.808  ? 17  THR   A HG21 1 c 2 
ATOM   1848 H HG22 . THR   B 1 5   ? 0.24    5.973   43.694  1   85.422  ? 17  THR   A HG22 1 c 2 
ATOM   1849 H HG23 . THR   B 1 5   ? -1.168  6.416   44.275  1   83.635  ? 17  THR   A HG23 1 c 2 
ATOM   1850 N N    . VAL   B 1 6   ? -3.316  3.033   41.786  1   93.249  ? 18  VAL   A N    1 ? 2 
ATOM   1851 C CA   . VAL   B 1 6   ? -4.043  2.098   40.928  1   90.229  ? 18  VAL   A CA   1 ? 2 
ATOM   1852 C C    . VAL   B 1 6   ? -4.357  2.81    39.607  1   86.28   ? 18  VAL   A C    1 ? 2 
ATOM   1853 O O    . VAL   B 1 6   ? -4.519  4.029   39.579  1   92.071  ? 18  VAL   A O    1 ? 2 
ATOM   1854 C CB   . VAL   B 1 6   ? -5.344  1.541   41.573  1   92.846  ? 18  VAL   A CB   1 ? 2 
ATOM   1855 C CG1  . VAL   B 1 6   ? -5.074  0.589   42.74   1   91.515  ? 18  VAL   A CG1  1 ? 2 
ATOM   1856 C CG2  . VAL   B 1 6   ? -6.31   2.642   42.017  1   92.445  ? 18  VAL   A CG2  1 ? 2 
ATOM   1857 H H    . VAL   B 1 6   ? -3.731  3.821   41.99   1   89.263  ? 18  VAL   A H    1 c 2 
ATOM   1858 H HA   . VAL   B 1 6   ? -3.454  1.343   40.735  1   93.043  ? 18  VAL   A HA   1 c 2 
ATOM   1859 H HB   . VAL   B 1 6   ? -5.804  1.017   40.875  1   91.434  ? 18  VAL   A HB   1 c 2 
ATOM   1860 H HG11 . VAL   B 1 6   ? -4.595  1.061   43.441  1   93.933  ? 18  VAL   A HG11 1 c 2 
ATOM   1861 H HG12 . VAL   B 1 6   ? -4.538  -0.161  42.431  1   95.196  ? 18  VAL   A HG12 1 c 2 
ATOM   1862 H HG13 . VAL   B 1 6   ? -5.918  0.259   43.091  1   94.187  ? 18  VAL   A HG13 1 c 2 
ATOM   1863 H HG21 . VAL   B 1 6   ? -7.097  2.238   42.422  1   92.941  ? 18  VAL   A HG21 1 c 2 
ATOM   1864 H HG22 . VAL   B 1 6   ? -6.58   3.17    41.248  1   88.979  ? 18  VAL   A HG22 1 c 2 
ATOM   1865 H HG23 . VAL   B 1 6   ? -5.873  3.216   42.668  1   92.071  ? 18  VAL   A HG23 1 c 2 
ATOM   1866 N N    . THR   B 1 7   ? -4.455  2.036   38.516  1   79.085  ? 19  THR   A N    1 ? 2 
ATOM   1867 C CA   . THR   B 1 7   ? -4.741  2.574   37.186  1   74.656  ? 19  THR   A CA   1 ? 2 
ATOM   1868 C C    . THR   B 1 7   ? -6.093  3.306   37.196  1   67.325  ? 19  THR   A C    1 ? 2 
ATOM   1869 O O    . THR   B 1 7   ? -6.191  4.464   36.821  1   68.468  ? 19  THR   A O    1 ? 2 
ATOM   1870 C CB   . THR   B 1 7   ? -4.743  1.457   36.129  1   72.209  ? 19  THR   A CB   1 ? 2 
ATOM   1871 O OG1  . THR   B 1 7   ? -3.669  0.527   36.294  1   74.305  ? 19  THR   A OG1  1 ? 2 
ATOM   1872 C CG2  . THR   B 1 7   ? -4.74   2.016   34.712  1   65.511  ? 19  THR   A CG2  1 ? 2 
ATOM   1873 H H    . THR   B 1 7   ? -4.341  1.134   38.605  1   82.867  ? 19  THR   A H    1 c 2 
ATOM   1874 H HA   . THR   B 1 7   ? -4.037  3.218   36.956  1   72.353  ? 19  THR   A HA   1 c 2 
ATOM   1875 H HB   . THR   B 1 7   ? -5.589  0.958   36.227  1   72.371  ? 19  THR   A HB   1 c 2 
ATOM   1876 H HG1  . THR   B 1 7   ? -2.847  1.233   36.284  0   30      ? 19  THR   A HG1  1 c 2 
ATOM   1877 H HG21 . THR   B 1 7   ? -4.615  1.291   34.077  1   67.957  ? 19  THR   A HG21 1 c 2 
ATOM   1878 H HG22 . THR   B 1 7   ? -4.015  2.657   34.617  1   65.882  ? 19  THR   A HG22 1 c 2 
ATOM   1879 H HG23 . THR   B 1 7   ? -5.587  2.459   34.535  1   64.836  ? 19  THR   A HG23 1 c 2 
ATOM   1880 N N    . GLU   B 1 8   ? -7.158  2.615   37.617  1   68.725  ? 20  GLU   A N    1 ? 2 
ATOM   1881 C CA   . GLU   B 1 8   ? -8.491  3.19    37.709  1   66.59   ? 20  GLU   A CA   1 ? 2 
ATOM   1882 C C    . GLU   B 1 8   ? -8.632  3.999   39.005  1   62.992  ? 20  GLU   A C    1 ? 2 
ATOM   1883 O O    . GLU   B 1 8   ? -9.512  3.722   39.831  1   68.539  ? 20  GLU   A O    1 ? 2 
ATOM   1884 C CB   . GLU   B 1 8   ? -9.538  2.073   37.626  1   69.508  ? 20  GLU   A CB   1 ? 2 
ATOM   1885 H H    . GLU   B 1 8   ? -7.043  1.743   37.863  1   71.009  ? 20  GLU   A H    1 c 2 
ATOM   1886 H HA   . GLU   B 1 8   ? -8.622  3.801   36.939  1   64.01   ? 20  GLU   A HA   1 c 2 
ATOM   1887 H HB2  . GLU   B 1 8   ? -8.994  1.278   37.346  0   30      ? 20  GLU   A HB2  1 c 2 
ATOM   1888 H HB3  . GLU   B 1 8   ? -10.406 2.472   37.518  0   30      ? 20  GLU   A HB3  1 c 2 
ATOM   1889 N N    . GLN   B 1 9   ? -7.752  4.979   39.205  1   59.316  ? 21  GLN   A N    1 ? 2 
ATOM   1890 C CA   . GLN   B 1 9   ? -7.933  5.999   40.241  1   67.487  ? 21  GLN   A CA   1 ? 2 
ATOM   1891 C C    . GLN   B 1 9   ? -8.405  7.336   39.631  1   63.763  ? 21  GLN   A C    1 ? 2 
ATOM   1892 O O    . GLN   B 1 9   ? -8.238  7.561   38.408  1   54.639  ? 21  GLN   A O    1 ? 2 
ATOM   1893 C CB   . GLN   B 1 9   ? -6.575  6.293   40.858  1   71.224  ? 21  GLN   A CB   1 ? 2 
ATOM   1894 C CG   . GLN   B 1 9   ? -5.62   6.93    39.843  1   67.823  ? 21  GLN   A CG   1 ? 2 
ATOM   1895 C CD   . GLN   B 1 9   ? -4.335  7.397   40.472  1   75.286  ? 21  GLN   A CD   1 ? 2 
ATOM   1896 O OE1  . GLN   B 1 9   ? -4.191  7.396   41.71   1   74.473  ? 21  GLN   A OE1  1 ? 2 
ATOM   1897 N NE2  . GLN   B 1 9   ? -3.406  7.773   39.6    1   72.549  ? 21  GLN   A NE2  1 ? 2 
ATOM   1898 H H    . GLN   B 1 9   ? -7.015  5.028   38.668  1   61.408  ? 21  GLN   A H    1 c 2 
ATOM   1899 H HA   . GLN   B 1 9   ? -8.581  5.681   40.92   1   67.363  ? 21  GLN   A HA   1 c 2 
ATOM   1900 H HB2  . GLN   B 1 9   ? -6.693  6.899   41.619  1   70.659  ? 21  GLN   A HB2  1 c 2 
ATOM   1901 H HB3  . GLN   B 1 9   ? -6.184  5.459   41.192  1   72.584  ? 21  GLN   A HB3  1 c 2 
ATOM   1902 H HG2  . GLN   B 1 9   ? -5.41   6.284   39.138  1   69.476  ? 21  GLN   A HG2  1 c 2 
ATOM   1903 H HG3  . GLN   B 1 9   ? -6.053  7.7     39.424  1   67.301  ? 21  GLN   A HG3  1 c 2 
ATOM   1904 H HE21 . GLN   B 1 9   ? -2.594  7.986   39.885  1   74.24   ? 21  GLN   A HE21 1 c 2 
ATOM   1905 H HE22 . GLN   B 1 9   ? -3.597  7.811   38.734  1   71.606  ? 21  GLN   A HE22 1 c 2 
ATOM   1906 N N    . GLY   B 1 10  ? -8.92   8.234   40.494  1   56.295  ? 22  GLY   A N    1 ? 2 
ATOM   1907 C CA   . GLY   B 1 10  ? -9.511  9.473   40.032  1   51.786  ? 22  GLY   A CA   1 ? 2 
ATOM   1908 C C    . GLY   B 1 10  ? -11.04  9.48    40.136  1   46.175  ? 22  GLY   A C    1 ? 2 
ATOM   1909 O O    . GLY   B 1 10  ? -11.685 8.479   40.415  1   46.743  ? 22  GLY   A O    1 ? 2 
ATOM   1910 H H    . GLY   B 1 10  ? -8.898  8.061   41.392  1   59.069  ? 22  GLY   A H    1 c 2 
ATOM   1911 H HA2  . GLY   B 1 10  ? -9.147  10.216  40.57   1   51.166  ? 22  GLY   A HA2  1 c 2 
ATOM   1912 H HA3  . GLY   B 1 10  ? -9.249  9.628   39.095  1   49.588  ? 22  GLY   A HA3  1 c 2 
ATOM   1913 N N    . GLU   B 1 11  ? -11.603 10.682  40.023  1   45.787  ? 23  GLU   A N    1 ? 2 
ATOM   1914 C CA   . GLU   B 1 11  ? -13.036 10.909  40.176  1   44.193  ? 23  GLU   A CA   1 ? 2 
ATOM   1915 C C    . GLU   B 1 11  ? -13.738 10.562  38.857  1   42.845  ? 23  GLU   A C    1 ? 2 
ATOM   1916 O O    . GLU   B 1 11  ? -13.304 10.977  37.799  1   40.628  ? 23  GLU   A O    1 ? 2 
ATOM   1917 C CB   . GLU   B 1 11  ? -13.203 12.368  40.623  1   50.162  ? 23  GLU   A CB   1 ? 2 
ATOM   1918 C CG   . GLU   B 1 11  ? -14.538 12.981  40.208  1   55.744  ? 23  GLU   A CG   1 ? 2 
ATOM   1919 C CD   . GLU   B 1 11  ? -14.788 14.396  40.692  1   62.328  ? 23  GLU   A CD   1 ? 2 
ATOM   1920 O OE1  . GLU   B 1 11  ? -13.859 15.24   40.699  1   70.164  ? 23  GLU   A OE1  1 ? 2 
ATOM   1921 O OE2  . GLU   B 1 11  ? -15.956 14.625  41.028  1   57.598  ? 23  GLU   A OE2  1 ? 2 
ATOM   1922 H H    . GLU   B 1 11  ? -11.066 11.398  39.832  1   44.468  ? 23  GLU   A H    1 c 2 
ATOM   1923 H HA   . GLU   B 1 11  ? -13.375 10.313  40.891  1   47.17   ? 23  GLU   A HA   1 c 2 
ATOM   1924 H HB2  . GLU   B 1 11  ? -13.125 12.415  41.595  1   51.292  ? 23  GLU   A HB2  1 c 2 
ATOM   1925 H HB3  . GLU   B 1 11  ? -12.48  12.907  40.239  1   48.732  ? 23  GLU   A HB3  1 c 2 
ATOM   1926 H HG2  . GLU   B 1 11  ? -14.594 12.98   39.232  1   54.156  ? 23  GLU   A HG2  1 c 2 
ATOM   1927 H HG3  . GLU   B 1 11  ? -15.263 12.409  40.54   1   56.726  ? 23  GLU   A HG3  1 c 2 
ATOM   1928 N N    . ASP   B 1 12  ? -14.795 9.753   38.924  1   41.397  ? 24  ASP   A N    1 ? 2 
ATOM   1929 C CA   . ASP   B 1 12  ? -15.614 9.438   37.78   1   44.438  ? 24  ASP   A CA   1 ? 2 
ATOM   1930 C C    . ASP   B 1 12  ? -16.517 10.631  37.498  1   46.515  ? 24  ASP   A C    1 ? 2 
ATOM   1931 O O    . ASP   B 1 12  ? -17.411 10.913  38.291  1   42.338  ? 24  ASP   A O    1 ? 2 
ATOM   1932 C CB   . ASP   B 1 12  ? -16.446 8.201   38.033  1   45.154  ? 24  ASP   A CB   1 ? 2 
ATOM   1933 C CG   . ASP   B 1 12  ? -17.31  7.783   36.86   1   45.932  ? 24  ASP   A CG   1 ? 2 
ATOM   1934 O OD1  . ASP   B 1 12  ? -17.281 8.497   35.844  1   45.867  ? 24  ASP   A OD1  1 ? 2 
ATOM   1935 O OD2  . ASP   B 1 12  ? -17.964 6.719   36.967  1   43.988  ? 24  ASP   A OD2  1 ? 2 
ATOM   1936 H H    . ASP   B 1 12  ? -15.014 9.382   39.73   1   44.413  ? 24  ASP   A H    1 c 2 
ATOM   1937 H HA   . ASP   B 1 12  ? -15.03  9.28    37.006  1   42.692  ? 24  ASP   A HA   1 c 2 
ATOM   1938 H HB2  . ASP   B 1 12  ? -15.847 7.458   38.253  1   46.166  ? 24  ASP   A HB2  1 c 2 
ATOM   1939 H HB3  . ASP   B 1 12  ? -17.028 8.358   38.806  1   47.049  ? 24  ASP   A HB3  1 c 2 
ATOM   1940 N N    . ILE   B 1 13  ? -16.25  11.333  36.383  1   41.133  ? 25  ILE   A N    1 ? 2 
ATOM   1941 C CA   . ILE   B 1 13  ? -16.985 12.544  36.076  1   43.854  ? 25  ILE   A CA   1 ? 2 
ATOM   1942 C C    . ILE   B 1 13  ? -18.009 12.295  34.976  1   41.715  ? 25  ILE   A C    1 ? 2 
ATOM   1943 O O    . ILE   B 1 13  ? -18.592 13.252  34.493  1   43.961  ? 25  ILE   A O    1 ? 2 
ATOM   1944 C CB   . ILE   B 1 13  ? -16.055 13.707  35.726  1   44.523  ? 25  ILE   A CB   1 ? 2 
ATOM   1945 C CG1  . ILE   B 1 13  ? -15.176 13.404  34.519  1   42.363  ? 25  ILE   A CG1  1 ? 2 
ATOM   1946 C CG2  . ILE   B 1 13  ? -15.222 14.132  36.947  1   48.789  ? 25  ILE   A CG2  1 ? 2 
ATOM   1947 C CD1  . ILE   B 1 13  ? -14.439 14.633  34.025  1   42.076  ? 25  ILE   A CD1  1 ? 2 
ATOM   1948 H H    . ILE   B 1 13  ? -15.608 11.041  35.802  1   41.575  ? 25  ILE   A H    1 c 2 
ATOM   1949 H HA   . ILE   B 1 13  ? -17.478 12.802  36.879  1   44.457  ? 25  ILE   A HA   1 c 2 
ATOM   1950 H HB   . ILE   B 1 13  ? -16.62  14.467  35.485  1   45.154  ? 25  ILE   A HB   1 c 2 
ATOM   1951 H HG12 . ILE   B 1 13  ? -14.523 12.717  34.763  1   42.233  ? 25  ILE   A HG12 1 c 2 
ATOM   1952 H HG13 . ILE   B 1 13  ? -15.733 13.053  33.795  1   42.683  ? 25  ILE   A HG13 1 c 2 
ATOM   1953 H HG21 . ILE   B 1 13  ? -14.801 14.99   36.773  1   47.15   ? 25  ILE   A HG21 1 c 2 
ATOM   1954 H HG22 . ILE   B 1 13  ? -14.535 13.466  37.118  1   47.197  ? 25  ILE   A HG22 1 c 2 
ATOM   1955 H HG23 . ILE   B 1 13  ? -15.8   14.208  37.724  1   48.871  ? 25  ILE   A HG23 1 c 2 
ATOM   1956 H HD11 . ILE   B 1 13  ? -15.071 15.37   33.92   1   42.572  ? 25  ILE   A HD11 1 c 2 
ATOM   1957 H HD12 . ILE   B 1 13  ? -14.022 14.439  33.164  1   41.187  ? 25  ILE   A HD12 1 c 2 
ATOM   1958 H HD13 . ILE   B 1 13  ? -13.749 14.887  34.667  1   41.898  ? 25  ILE   A HD13 1 c 2 
ATOM   1959 N N    . THR   B 1 14  ? -18.294 11.041  34.639  1   45.102  ? 26  THR   A N    1 ? 2 
ATOM   1960 C CA   . THR   B 1 14  ? -19.375 10.737  33.7    1   49.154  ? 26  THR   A CA   1 ? 2 
ATOM   1961 C C    . THR   B 1 14  ? -20.731 10.869  34.384  1   53.787  ? 26  THR   A C    1 ? 2 
ATOM   1962 O O    . THR   B 1 14  ? -20.859 10.631  35.582  1   52.507  ? 26  THR   A O    1 ? 2 
ATOM   1963 C CB   . THR   B 1 14  ? -19.258 9.343   33.079  1   46.645  ? 26  THR   A CB   1 ? 2 
ATOM   1964 O OG1  . THR   B 1 14  ? -19.417 8.317   34.053  1   46.021  ? 26  THR   A OG1  1 ? 2 
ATOM   1965 C CG2  . THR   B 1 14  ? -17.922 9.137   32.387  1   45.532  ? 26  THR   A CG2  1 ? 2 
ATOM   1966 H H    . THR   B 1 14  ? -17.812 10.352  34.995  1   44.972  ? 26  THR   A H    1 c 2 
ATOM   1967 H HA   . THR   B 1 14  ? -19.333 11.394  32.972  1   47.671  ? 26  THR   A HA   1 c 2 
ATOM   1968 H HB   . THR   B 1 14  ? -19.967 9.246   32.399  1   47.784  ? 26  THR   A HB   1 c 2 
ATOM   1969 H HG1  . THR   B 1 14  ? -18.738 8.472   34.691  0   30      ? 26  THR   A HG1  1 c 2 
ATOM   1970 H HG21 . THR   B 1 14  ? -17.886 8.243   32.009  1   45.918  ? 26  THR   A HG21 1 c 2 
ATOM   1971 H HG22 . THR   B 1 14  ? -17.202 9.244   33.03   1   44.566  ? 26  THR   A HG22 1 c 2 
ATOM   1972 H HG23 . THR   B 1 14  ? -17.82  9.792   31.676  1   44.451  ? 26  THR   A HG23 1 c 2 
ATOM   1973 N N    . SER   B 1 15  ? -21.759 11.138  33.576  1   56.046  ? 27  SER   A N    1 ? 2 
ATOM   1974 C CA   . SER   B 1 15  ? -23.115 11.231  34.064  1   59.949  ? 27  SER   A CA   1 ? 2 
ATOM   1975 C C    . SER   B 1 15  ? -23.681 9.851   34.38   1   60.548  ? 27  SER   A C    1 ? 2 
ATOM   1976 O O    . SER   B 1 15  ? -24.491 9.699   35.311  1   56.326  ? 27  SER   A O    1 ? 2 
ATOM   1977 C CB   . SER   B 1 15  ? -23.953 12      33.1    1   67.193  ? 27  SER   A CB   1 ? 2 
ATOM   1978 O OG   . SER   B 1 15  ? -23.741 13.386  33.352  1   69.818  ? 27  SER   A OG   1 ? 2 
ATOM   1979 H H    . SER   B 1 15  ? -21.603 11.263  32.684  1   55.349  ? 27  SER   A H    1 c 2 
ATOM   1980 H HA   . SER   B 1 15  ? -23.09  11.741  34.913  1   60.816  ? 27  SER   A HA   1 c 2 
ATOM   1981 H HB2  . SER   B 1 15  ? -23.695 11.783  32.184  1   65.484  ? 27  SER   A HB2  1 c 2 
ATOM   1982 H HB3  . SER   B 1 15  ? -24.895 11.778  33.227  1   68.716  ? 27  SER   A HB3  1 c 2 
ATOM   1983 H HG   . SER   B 1 15  ? -24.172 13.721  32.694  0   30      ? 27  SER   A HG   1 c 2 
ATOM   1984 N N    . LYS   B 1 16  ? -23.216 8.864   33.622  1   53.46   ? 28  LYS   A N    1 ? 2 
ATOM   1985 C CA   . LYS   B 1 16  ? -23.69  7.49    33.715  1   59.349  ? 28  LYS   A CA   1 ? 2 
ATOM   1986 C C    . LYS   B 1 16  ? -22.966 6.742   34.837  1   55.398  ? 28  LYS   A C    1 ? 2 
ATOM   1987 O O    . LYS   B 1 16  ? -23.329 5.607   35.128  1   58.489  ? 28  LYS   A O    1 ? 2 
ATOM   1988 C CB   . LYS   B 1 16  ? -23.417 6.847   32.34   1   60.293  ? 28  LYS   A CB   1 ? 2 
ATOM   1989 C CG   . LYS   B 1 16  ? -24.212 5.647   31.835  1   70.532  ? 28  LYS   A CG   1 ? 2 
ATOM   1990 H H    . LYS   B 1 16  ? -22.564 9.053   33.01   1   53.953  ? 28  LYS   A H    1 c 2 
ATOM   1991 H HA   . LYS   B 1 16  ? -24.664 7.496   33.898  1   60.525  ? 28  LYS   A HA   1 c 2 
ATOM   1992 H HB2  . LYS   B 1 16  ? -23.517 7.556   31.669  1   60.589  ? 28  LYS   A HB2  1 c 2 
ATOM   1993 H HB3  . LYS   B 1 16  ? -22.47  6.588   32.331  1   59.698  ? 28  LYS   A HB3  1 c 2 
ATOM   1994 H HG2  . LYS   B 1 16  ? -23.852 4.786   31.775  0   30      ? 28  LYS   A HG2  1 c 2 
ATOM   1995 H HG3  . LYS   B 1 16  ? -25.353 5.846   32.086  0   30      ? 28  LYS   A HG3  1 c 2 
ATOM   1996 N N    . LYS   B 1 17  ? -21.878 7.319   35.35   1   52.958  ? 29  LYS   A N    1 ? 2 
ATOM   1997 C CA   . LYS   B 1 17  ? -21.053 6.696   36.382  1   56.116  ? 29  LYS   A CA   1 ? 2 
ATOM   1998 C C    . LYS   B 1 17  ? -20.552 5.309   35.962  1   55.439  ? 29  LYS   A C    1 ? 2 
ATOM   1999 O O    . LYS   B 1 17  ? -20.699 4.326   36.684  1   51.763  ? 29  LYS   A O    1 ? 2 
ATOM   2000 C CB   . LYS   B 1 17  ? -21.827 6.643   37.702  1   59.765  ? 29  LYS   A CB   1 ? 2 
ATOM   2001 C CG   . LYS   B 1 17  ? -22.172 8.003   38.256  1   62.23   ? 29  LYS   A CG   1 ? 2 
ATOM   2002 C CD   . LYS   B 1 17  ? -20.952 8.879   38.521  1   62.046  ? 29  LYS   A CD   1 ? 2 
ATOM   2003 C CE   . LYS   B 1 17  ? -21.353 10.025  39.389  1   70.271  ? 29  LYS   A CE   1 ? 2 
ATOM   2004 N NZ   . LYS   B 1 17  ? -20.301 11.028  39.462  1   71.444  ? 29  LYS   A NZ   1 ? 2 
ATOM   2005 H H    . LYS   B 1 17  ? -21.624 8.139   35.038  1   52.055  ? 29  LYS   A H    1 c 2 
ATOM   2006 H HA   . LYS   B 1 17  ? -20.263 7.272   36.519  1   53.45   ? 29  LYS   A HA   1 c 2 
ATOM   2007 H HB2  . LYS   B 1 17  ? -22.658 6.139   37.57   1   62.329  ? 29  LYS   A HB2  1 c 2 
ATOM   2008 H HB3  . LYS   B 1 17  ? -21.289 6.165   38.367  1   60.568  ? 29  LYS   A HB3  1 c 2 
ATOM   2009 H HG2  . LYS   B 1 17  ? -22.764 8.46    37.621  1   62.117  ? 29  LYS   A HG2  1 c 2 
ATOM   2010 H HG3  . LYS   B 1 17  ? -22.668 7.881   39.095  1   64.349  ? 29  LYS   A HG3  1 c 2 
ATOM   2011 H HD2  . LYS   B 1 17  ? -20.256 8.353   38.973  1   62.833  ? 29  LYS   A HD2  1 c 2 
ATOM   2012 H HD3  . LYS   B 1 17  ? -20.595 9.221   37.674  1   60.944  ? 29  LYS   A HD3  1 c 2 
ATOM   2013 H HE2  . LYS   B 1 17  ? -22.161 10.437  39.034  1   69.997  ? 29  LYS   A HE2  1 c 2 
ATOM   2014 H HE3  . LYS   B 1 17  ? -21.546 9.701   40.288  1   71.071  ? 29  LYS   A HE3  1 c 2 
ATOM   2015 H HZ1  . LYS   B 1 17  ? -20.23  11.456  38.667  1   68.977  ? 29  LYS   A HZ1  1 c 2 
ATOM   2016 H HZ2  . LYS   B 1 17  ? -19.51  10.631  39.658  1   69.467  ? 29  LYS   A HZ2  1 c 2 
ATOM   2017 H HZ3  . LYS   B 1 17  ? -20.498 11.631  40.109  1   71.238  ? 29  LYS   A HZ3  1 c 2 
ATOM   2018 N N    . ASP   B 1 18  ? -19.91  5.249   34.793  1   58.607  ? 30  ASP   A N    1 ? 2 
ATOM   2019 C CA   . ASP   B 1 18  ? -19.375 4.009   34.248  1   59.087  ? 30  ASP   A CA   1 ? 2 
ATOM   2020 C C    . ASP   B 1 18  ? -17.846 4.003   34.318  1   62.7    ? 30  ASP   A C    1 ? 2 
ATOM   2021 O O    . ASP   B 1 18  ? -17.203 3.21    33.621  1   57.867  ? 30  ASP   A O    1 ? 2 
ATOM   2022 C CB   . ASP   B 1 18  ? -19.784 3.825   32.79   1   61.548  ? 30  ASP   A CB   1 ? 2 
ATOM   2023 C CG   . ASP   B 1 18  ? -19.42  4.97    31.854  1   55.445  ? 30  ASP   A CG   1 ? 2 
ATOM   2024 O OD1  . ASP   B 1 18  ? -18.468 5.738   32.157  1   56.074  ? 30  ASP   A OD1  1 ? 2 
ATOM   2025 O OD2  . ASP   B 1 18  ? -20.188 5.193   30.917  1   50.679  ? 30  ASP   A OD2  1 ? 2 
ATOM   2026 H H    . ASP   B 1 18  ? -19.795 6.02    34.316  1   55.514  ? 30  ASP   A H    1 c 2 
ATOM   2027 H HA   . ASP   B 1 18  ? -19.722 3.253   34.772  1   62.737  ? 30  ASP   A HA   1 c 2 
ATOM   2028 H HB2  . ASP   B 1 18  ? -19.38  3.003   32.442  1   61.013  ? 30  ASP   A HB2  1 c 2 
ATOM   2029 H HB3  . ASP   B 1 18  ? -20.757 3.711   32.759  1   61.999  ? 30  ASP   A HB3  1 c 2 
ATOM   2030 N N    . ARG   B 1 19  ? -17.27  4.895   35.141  1   54.54   ? 31  ARG   A N    1 ? 2 
ATOM   2031 C CA   . ARG   B 1 19  ? -15.83  4.973   35.34   1   51.819  ? 31  ARG   A CA   1 ? 2 
ATOM   2032 C C    . ARG   B 1 19  ? -15.087 5.081   34.011  1   50.777  ? 31  ARG   A C    1 ? 2 
ATOM   2033 O O    . ARG   B 1 19  ? -13.918 4.685   33.947  1   51.911  ? 31  ARG   A O    1 ? 2 
ATOM   2034 C CB   . ARG   B 1 19  ? -15.233 3.878   36.236  1   54.731  ? 31  ARG   A CB   1 ? 2 
ATOM   2035 C CG   . ARG   B 1 19  ? -15.945 3.803   37.577  1   63.994  ? 31  ARG   A CG   1 ? 2 
ATOM   2036 C CD   . ARG   B 1 19  ? -15.388 2.824   38.592  1   72.035  ? 31  ARG   A CD   1 ? 2 
ATOM   2037 N NE   . ARG   B 1 19  ? -13.922 2.802   38.669  1   80.631  ? 31  ARG   A NE   1 ? 2 
ATOM   2038 C CZ   . ARG   B 1 19  ? -13.148 3.669   39.311  1   88.813  ? 31  ARG   A CZ   1 ? 2 
ATOM   2039 N NH1  . ARG   B 1 19  ? -13.661 4.706   39.952  1   83.82   ? 31  ARG   A NH1  1 ? 2 
ATOM   2040 N NH2  . ARG   B 1 19  ? -11.847 3.476   39.316  1   94.17   ? 31  ARG   A NH2  1 ? 2 
ATOM   2041 H H    . ARG   B 1 19  ? -17.801 5.476   35.603  1   55.706  ? 31  ARG   A H    1 c 2 
ATOM   2042 H HA   . ARG   B 1 19  ? -15.658 5.819   35.824  1   51.242  ? 31  ARG   A HA   1 c 2 
ATOM   2043 H HB2  . ARG   B 1 19  ? -15.307 3.011   35.783  1   57.378  ? 31  ARG   A HB2  1 c 2 
ATOM   2044 H HB3  . ARG   B 1 19  ? -14.282 4.064   36.387  1   55.243  ? 31  ARG   A HB3  1 c 2 
ATOM   2045 H HG2  . ARG   B 1 19  ? -15.942 4.699   37.979  1   62.303  ? 31  ARG   A HG2  1 c 2 
ATOM   2046 H HG3  . ARG   B 1 19  ? -16.886 3.574   37.415  1   64.522  ? 31  ARG   A HG3  1 c 2 
ATOM   2047 H HD2  . ARG   B 1 19  ? -15.75  3.048   39.474  1   73.989  ? 31  ARG   A HD2  1 c 2 
ATOM   2048 H HD3  . ARG   B 1 19  ? -15.707 1.927   38.364  1   74.719  ? 31  ARG   A HD3  1 c 2 
ATOM   2049 H HE   . ARG   B 1 19  ? -13.515 2.155   38.251  1   80.974  ? 31  ARG   A HE   1 c 2 
ATOM   2050 H HH11 . ARG   B 1 19  ? -14.476 4.991   39.765  1   84.225  ? 31  ARG   A HH11 1 c 2 
ATOM   2051 H HH12 . ARG   B 1 19  ? -13.179 5.118   40.569  1   85.014  ? 31  ARG   A HH12 1 c 2 
ATOM   2052 H HH21 . ARG   B 1 19  ? -11.51  2.755   39.7    1   94.19   ? 31  ARG   A HH21 1 c 2 
ATOM   2053 H HH22 . ARG   B 1 19  ? -11.322 4.079   38.941  1   90.221  ? 31  ARG   A HH22 1 c 2 
ATOM   2054 N N    . GLY   B 1 20  ? -15.716 5.747   33.021  1   50.345  ? 32  GLY   A N    1 ? 2 
ATOM   2055 C CA   . GLY   B 1 20  ? -15.164 5.886   31.689  1   49.287  ? 32  GLY   A CA   1 ? 2 
ATOM   2056 C C    . GLY   B 1 20  ? -14.311 7.132   31.471  1   50.436  ? 32  GLY   A C    1 ? 2 
ATOM   2057 O O    . GLY   B 1 20  ? -13.511 7.172   30.518  1   44.469  ? 32  GLY   A O    1 ? 2 
ATOM   2058 H H    . GLY   B 1 20  ? -16.52  6.144   33.198  1   50.584  ? 32  GLY   A H    1 c 2 
ATOM   2059 H HA2  . GLY   B 1 20  ? -14.619 5.089   31.491  1   50.689  ? 32  GLY   A HA2  1 c 2 
ATOM   2060 H HA3  . GLY   B 1 20  ? -15.91  5.897   31.045  1   50.481  ? 32  GLY   A HA3  1 c 2 
ATOM   2061 N N    . VAL   B 1 21  ? -14.545 8.18    32.291  1   46.581  ? 33  VAL   A N    1 ? 2 
ATOM   2062 C CA   . VAL   B 1 21  ? -13.696 9.355   32.324  1   42.048  ? 33  VAL   A CA   1 ? 2 
ATOM   2063 C C    . VAL   B 1 21  ? -13.336 9.562   33.787  1   44.834  ? 33  VAL   A C    1 ? 2 
ATOM   2064 O O    . VAL   B 1 21  ? -14.253 9.804   34.577  1   37.068  ? 33  VAL   A O    1 ? 2 
ATOM   2065 C CB   . VAL   B 1 21  ? -14.268 10.659  31.733  1   42.41   ? 33  VAL   A CB   1 ? 2 
ATOM   2066 C CG1  . VAL   B 1 21  ? -13.234 11.781  31.724  1   44.265  ? 33  VAL   A CG1  1 ? 2 
ATOM   2067 C CG2  . VAL   B 1 21  ? -14.809 10.5    30.332  1   46.127  ? 33  VAL   A CG2  1 ? 2 
ATOM   2068 H H    . VAL   B 1 21  ? -15.267 8.15    32.851  1   47.367  ? 33  VAL   A H    1 c 2 
ATOM   2069 H HA   . VAL   B 1 21  ? -12.876 9.145   31.838  1   42.832  ? 33  VAL   A HA   1 c 2 
ATOM   2070 H HB   . VAL   B 1 21  ? -15.014 10.939  32.313  1   43.942  ? 33  VAL   A HB   1 c 2 
ATOM   2071 H HG11 . VAL   B 1 21  ? -12.442 11.489  31.243  1   42.962  ? 33  VAL   A HG11 1 c 2 
ATOM   2072 H HG12 . VAL   B 1 21  ? -12.992 12.01   32.637  1   43.437  ? 33  VAL   A HG12 1 c 2 
ATOM   2073 H HG13 . VAL   B 1 21  ? -13.608 12.564  31.285  1   43.304  ? 33  VAL   A HG13 1 c 2 
ATOM   2074 H HG21 . VAL   B 1 21  ? -15.175 11.348  30.027  1   44.982  ? 33  VAL   A HG21 1 c 2 
ATOM   2075 H HG22 . VAL   B 1 21  ? -15.509 9.827   30.328  1   46.071  ? 33  VAL   A HG22 1 c 2 
ATOM   2076 H HG23 . VAL   B 1 21  ? -14.092 10.224  29.736  1   44.663  ? 33  VAL   A HG23 1 c 2 
ATOM   2077 N N    . LEU   B 1 22  ? -12.036 9.399   34.104  1   44.558  ? 34  LEU   A N    1 ? 2 
ATOM   2078 C CA   . LEU   B 1 22  ? -11.505 9.535   35.447  1   45.995  ? 34  LEU   A CA   1 ? 2 
ATOM   2079 C C    . LEU   B 1 22  ? -10.595 10.748  35.517  1   43.271  ? 34  LEU   A C    1 ? 2 
ATOM   2080 O O    . LEU   B 1 22  ? -9.723  10.942  34.668  1   41.113  ? 34  LEU   A O    1 ? 2 
ATOM   2081 C CB   . LEU   B 1 22  ? -10.759 8.28    35.864  1   49.551  ? 34  LEU   A CB   1 ? 2 
ATOM   2082 C CG   . LEU   B 1 22  ? -11.611 7.009   35.933  1   57.509  ? 34  LEU   A CG   1 ? 2 
ATOM   2083 C CD1  . LEU   B 1 22  ? -10.735 5.795   36.219  1   58.763  ? 34  LEU   A CD1  1 ? 2 
ATOM   2084 C CD2  . LEU   B 1 22  ? -12.746 7.14    36.954  1   56.106  ? 34  LEU   A CD2  1 ? 2 
ATOM   2085 H H    . LEU   B 1 22  ? -11.451 9.19    33.434  1   44.314  ? 34  LEU   A H    1 c 2 
ATOM   2086 H HA   . LEU   B 1 22  ? -12.262 9.677   36.064  1   46.435  ? 34  LEU   A HA   1 c 2 
ATOM   2087 H HB2  . LEU   B 1 22  ? -10.026 8.13    35.224  1   49.921  ? 34  LEU   A HB2  1 c 2 
ATOM   2088 H HB3  . LEU   B 1 22  ? -10.361 8.438   36.751  1   50.973  ? 34  LEU   A HB3  1 c 2 
ATOM   2089 H HG   . LEU   B 1 22  ? -12.026 6.874   35.043  1   55.2    ? 34  LEU   A HG   1 c 2 
ATOM   2090 H HD11 . LEU   B 1 22  ? -10.129 5.649   35.474  1   58.442  ? 34  LEU   A HD11 1 c 2 
ATOM   2091 H HD12 . LEU   B 1 22  ? -11.297 5.01    36.337  1   60.376  ? 34  LEU   A HD12 1 c 2 
ATOM   2092 H HD13 . LEU   B 1 22  ? -10.221 5.948   37.029  1   59.515  ? 34  LEU   A HD13 1 c 2 
ATOM   2093 H HD21 . LEU   B 1 22  ? -13.385 7.805   36.649  1   55.826  ? 34  LEU   A HD21 1 c 2 
ATOM   2094 H HD22 . LEU   B 1 22  ? -12.382 7.412   37.813  1   57.276  ? 34  LEU   A HD22 1 c 2 
ATOM   2095 H HD23 . LEU   B 1 22  ? -13.196 6.284   37.051  1   58.274  ? 34  LEU   A HD23 1 c 2 
ATOM   2096 N N    . LYS   B 1 23  ? -10.81  11.576  36.555  1   41.718  ? 35  LYS   A N    1 ? 2 
ATOM   2097 C CA   . LYS   B 1 23  ? -10.127 12.85   36.656  1   38.705  ? 35  LYS   A CA   1 ? 2 
ATOM   2098 C C    . LYS   B 1 23  ? -9.391  12.973  37.99   1   40.163  ? 35  LYS   A C    1 ? 2 
ATOM   2099 O O    . LYS   B 1 23  ? -9.971  12.65   39.032  1   38.567  ? 35  LYS   A O    1 ? 2 
ATOM   2100 C CB   . LYS   B 1 23  ? -11.167 13.977  36.6    1   40.346  ? 35  LYS   A CB   1 ? 2 
ATOM   2101 C CG   . LYS   B 1 23  ? -10.567 15.376  36.636  1   37.62   ? 35  LYS   A CG   1 ? 2 
ATOM   2102 C CD   . LYS   B 1 23  ? -11.577 16.498  36.907  1   39.875  ? 35  LYS   A CD   1 ? 2 
ATOM   2103 C CE   . LYS   B 1 23  ? -10.843 17.802  36.897  1   42.693  ? 35  LYS   A CE   1 ? 2 
ATOM   2104 N NZ   . LYS   B 1 23  ? -11.614 18.997  37.263  1   45.028  ? 35  LYS   A NZ   1 ? 2 
ATOM   2105 H H    . LYS   B 1 23  ? -11.395 11.335  37.215  1   42.493  ? 35  LYS   A H    1 c 2 
ATOM   2106 H HA   . LYS   B 1 23  ? -9.487  12.938  35.91   1   38.827  ? 35  LYS   A HA   1 c 2 
ATOM   2107 H HB2  . LYS   B 1 23  ? -11.691 13.884  35.776  1   38.703  ? 35  LYS   A HB2  1 c 2 
ATOM   2108 H HB3  . LYS   B 1 23  ? -11.781 13.881  37.358  1   40.171  ? 35  LYS   A HB3  1 c 2 
ATOM   2109 H HG2  . LYS   B 1 23  ? -9.875  15.403  37.331  1   39.192  ? 35  LYS   A HG2  1 c 2 
ATOM   2110 H HG3  . LYS   B 1 23  ? -10.128 15.546  35.774  1   37.846  ? 35  LYS   A HG3  1 c 2 
ATOM   2111 H HD2  . LYS   B 1 23  ? -12.268 16.503  36.209  1   39.681  ? 35  LYS   A HD2  1 c 2 
ATOM   2112 H HD3  . LYS   B 1 23  ? -12     16.364  37.783  1   40.985  ? 35  LYS   A HD3  1 c 2 
ATOM   2113 H HE2  . LYS   B 1 23  ? -10.085 17.733  37.505  1   42.743  ? 35  LYS   A HE2  1 c 2 
ATOM   2114 H HE3  . LYS   B 1 23  ? -10.48  17.939  36.003  1   41.634  ? 35  LYS   A HE3  1 c 2 
ATOM   2115 H HZ1  . LYS   B 1 23  ? -11.866 18.946  38.132  1   45.679  ? 35  LYS   A HZ1  1 c 2 
ATOM   2116 H HZ2  . LYS   B 1 23  ? -12.353 19.056  36.742  1   44.626  ? 35  LYS   A HZ2  1 c 2 
ATOM   2117 H HZ3  . LYS   B 1 23  ? -11.107 19.738  37.143  1   45.278  ? 35  LYS   A HZ3  1 c 2 
ATOM   2118 N N    . ILE   B 1 24  ? -8.184  13.547  37.912  1   37.391  ? 36  ILE   A N    1 ? 2 
ATOM   2119 C CA   . ILE   B 1 24  ? -7.436  14.018  39.051  1   40.978  ? 36  ILE   A CA   1 ? 2 
ATOM   2120 C C    . ILE   B 1 24  ? -7.013  15.457  38.786  1   41.11   ? 36  ILE   A C    1 ? 2 
ATOM   2121 O O    . ILE   B 1 24  ? -6.504  15.772  37.713  1   43.661  ? 36  ILE   A O    1 ? 2 
ATOM   2122 C CB   . ILE   B 1 24  ? -6.202  13.145  39.342  1   44.1    ? 36  ILE   A CB   1 ? 2 
ATOM   2123 C CG1  . ILE   B 1 24  ? -6.527  11.661  39.41   1   45.252  ? 36  ILE   A CG1  1 ? 2 
ATOM   2124 C CG2  . ILE   B 1 24  ? -5.512  13.659  40.619  1   45.689  ? 36  ILE   A CG2  1 ? 2 
ATOM   2125 C CD1  . ILE   B 1 24  ? -5.279  10.779  39.312  1   49.718  ? 36  ILE   A CD1  1 ? 2 
ATOM   2126 H H    . ILE   B 1 24  ? -7.806  13.644  37.085  1   37.754  ? 36  ILE   A H    1 c 2 
ATOM   2127 H HA   . ILE   B 1 24  ? -8.019  14      39.835  1   41.755  ? 36  ILE   A HA   1 c 2 
ATOM   2128 H HB   . ILE   B 1 24  ? -5.576  13.27   38.601  1   43.193  ? 36  ILE   A HB   1 c 2 
ATOM   2129 H HG12 . ILE   B 1 24  ? -6.986  11.474  40.254  1   46.819  ? 36  ILE   A HG12 1 c 2 
ATOM   2130 H HG13 . ILE   B 1 24  ? -7.134  11.432  38.678  1   44.558  ? 36  ILE   A HG13 1 c 2 
ATOM   2131 H HG21 . ILE   B 1 24  ? -4.786  13.06   40.863  1   46.985  ? 36  ILE   A HG21 1 c 2 
ATOM   2132 H HG22 . ILE   B 1 24  ? -6.157  13.695  41.346  1   46.567  ? 36  ILE   A HG22 1 c 2 
ATOM   2133 H HG23 . ILE   B 1 24  ? -5.153  14.549  40.463  1   45.87   ? 36  ILE   A HG23 1 c 2 
ATOM   2134 H HD11 . ILE   B 1 24  ? -4.732  11.065  38.556  1   48.004  ? 36  ILE   A HD11 1 c 2 
ATOM   2135 H HD12 . ILE   B 1 24  ? -5.547  9.85    39.184  1   49.132  ? 36  ILE   A HD12 1 c 2 
ATOM   2136 H HD13 . ILE   B 1 24  ? -4.758  10.854  40.135  1   50.288  ? 36  ILE   A HD13 1 c 2 
ATOM   2137 N N    . VAL   B 1 25  ? -7.274  16.333  39.762  1   41.007  ? 37  VAL   A N    1 ? 2 
ATOM   2138 C CA   . VAL   B 1 25  ? -6.767  17.691  39.774  1   41.004  ? 37  VAL   A CA   1 ? 2 
ATOM   2139 C C    . VAL   B 1 25  ? -5.322  17.652  40.257  1   43.26   ? 37  VAL   A C    1 ? 2 
ATOM   2140 O O    . VAL   B 1 25  ? -5.044  17.158  41.35   1   46.068  ? 37  VAL   A O    1 ? 2 
ATOM   2141 C CB   . VAL   B 1 25  ? -7.671  18.52   40.71   1   43.145  ? 37  VAL   A CB   1 ? 2 
ATOM   2142 C CG1  . VAL   B 1 25  ? -7.222  19.957  40.778  1   44.069  ? 37  VAL   A CG1  1 ? 2 
ATOM   2143 C CG2  . VAL   B 1 25  ? -9.133  18.481  40.285  1   44.49   ? 37  VAL   A CG2  1 ? 2 
ATOM   2144 H H    . VAL   B 1 25  ? -7.788  16.058  40.466  1   41.85   ? 37  VAL   A H    1 c 2 
ATOM   2145 H HA   . VAL   B 1 25  ? -6.805  18.061  38.871  1   40.565  ? 37  VAL   A HA   1 c 2 
ATOM   2146 H HB   . VAL   B 1 25  ? -7.599  18.13   41.613  1   44.416  ? 37  VAL   A HB   1 c 2 
ATOM   2147 H HG11 . VAL   B 1 25  ? -7.188  20.329  39.88   1   43.468  ? 37  VAL   A HG11 1 c 2 
ATOM   2148 H HG12 . VAL   B 1 25  ? -6.339  20.004  41.181  1   45.37   ? 37  VAL   A HG12 1 c 2 
ATOM   2149 H HG13 . VAL   B 1 25  ? -7.849  20.469  41.316  1   45.437  ? 37  VAL   A HG13 1 c 2 
ATOM   2150 H HG21 . VAL   B 1 25  ? -9.654  19.069  40.857  1   45.034  ? 37  VAL   A HG21 1 c 2 
ATOM   2151 H HG22 . VAL   B 1 25  ? -9.473  17.574  40.362  1   43.182  ? 37  VAL   A HG22 1 c 2 
ATOM   2152 H HG23 . VAL   B 1 25  ? -9.211  18.778  39.363  1   42.81   ? 37  VAL   A HG23 1 c 2 
ATOM   2153 N N    . LYS   B 1 26  ? -4.385  18.145  39.441  1   43.881  ? 38  LYS   A N    1 ? 2 
ATOM   2154 C CA   . LYS   B 1 26  ? -2.972  18.135  39.801  1   45.009  ? 38  LYS   A CA   1 ? 2 
ATOM   2155 C C    . LYS   B 1 26  ? -2.467  19.509  40.253  1   47.799  ? 38  LYS   A C    1 ? 2 
ATOM   2156 O O    . LYS   B 1 26  ? -1.482  19.578  40.966  1   48.813  ? 38  LYS   A O    1 ? 2 
ATOM   2157 C CB   . LYS   B 1 26  ? -2.113  17.644  38.637  1   44.804  ? 38  LYS   A CB   1 ? 2 
ATOM   2158 C CG   . LYS   B 1 26  ? -2.5    16.297  38.148  1   42.351  ? 38  LYS   A CG   1 ? 2 
ATOM   2159 C CD   . LYS   B 1 26  ? -2.365  15.216  39.209  1   44.094  ? 38  LYS   A CD   1 ? 2 
ATOM   2160 C CE   . LYS   B 1 26  ? -0.971  15.027  39.645  1   47.427  ? 38  LYS   A CE   1 ? 2 
ATOM   2161 N NZ   . LYS   B 1 26  ? -0.941  13.828  40.468  1   49.929  ? 38  LYS   A NZ   1 ? 2 
ATOM   2162 H H    . LYS   B 1 26  ? -4.631  18.493  38.632  1   42.603  ? 38  LYS   A H    1 c 2 
ATOM   2163 H HA   . LYS   B 1 26  ? -2.85   17.508  40.556  1   46.15   ? 38  LYS   A HA   1 c 2 
ATOM   2164 H HB2  . LYS   B 1 26  ? -2.19   18.28   37.894  1   44.002  ? 38  LYS   A HB2  1 c 2 
ATOM   2165 H HB3  . LYS   B 1 26  ? -1.173  17.622  38.917  1   46.111  ? 38  LYS   A HB3  1 c 2 
ATOM   2166 H HG2  . LYS   B 1 26  ? -3.43   16.329  37.835  1   41.265  ? 38  LYS   A HG2  1 c 2 
ATOM   2167 H HG3  . LYS   B 1 26  ? -1.932  16.069  37.385  1   42.492  ? 38  LYS   A HG3  1 c 2 
ATOM   2168 H HD2  . LYS   B 1 26  ? -2.918  15.445  39.986  1   44.616  ? 38  LYS   A HD2  1 c 2 
ATOM   2169 H HD3  . LYS   B 1 26  ? -2.703  14.37   38.84   1   43.229  ? 38  LYS   A HD3  1 c 2 
ATOM   2170 H HE2  . LYS   B 1 26  ? -0.386  14.912  38.875  1   47.364  ? 38  LYS   A HE2  1 c 2 
ATOM   2171 H HE3  . LYS   B 1 26  ? -0.665  15.789  40.169  1   48.84   ? 38  LYS   A HE3  1 c 2 
ATOM   2172 H HZ1  . LYS   B 1 26  ? -1.203  13.108  39.984  1   48.538  ? 38  LYS   A HZ1  1 c 2 
ATOM   2173 H HZ2  . LYS   B 1 26  ? -1.494  13.927  41.179  1   49.808  ? 38  LYS   A HZ2  1 c 2 
ATOM   2174 H HZ3  . LYS   B 1 26  ? -0.098  13.689  40.769  1   51.327  ? 38  LYS   A HZ3  1 c 2 
ATOM   2175 N N    . ARG   B 1 27  ? -3.066  20.588  39.755  1   49.142  ? 39  ARG   A N    1 ? 2 
ATOM   2176 C CA   . ARG   B 1 27  ? -2.794  21.921  40.256  1   50.08   ? 39  ARG   A CA   1 ? 2 
ATOM   2177 C C    . ARG   B 1 27  ? -4.125  22.656  40.285  1   51.635  ? 39  ARG   A C    1 ? 2 
ATOM   2178 O O    . ARG   B 1 27  ? -4.836  22.689  39.284  1   51.671  ? 39  ARG   A O    1 ? 2 
ATOM   2179 C CB   . ARG   B 1 27  ? -1.764  22.706  39.43   1   53.989  ? 39  ARG   A CB   1 ? 2 
ATOM   2180 C CG   . ARG   B 1 27  ? -1.347  24.043  40.043  1   55.746  ? 39  ARG   A CG   1 ? 2 
ATOM   2181 C CD   . ARG   B 1 27  ? -0.494  24.894  39.116  1   58.902  ? 39  ARG   A CD   1 ? 2 
ATOM   2182 N NE   . ARG   B 1 27  ? -1.231  25.297  37.911  1   58.496  ? 39  ARG   A NE   1 ? 2 
ATOM   2183 C CZ   . ARG   B 1 27  ? -0.688  25.742  36.767  1   60.131  ? 39  ARG   A CZ   1 ? 2 
ATOM   2184 N NH1  . ARG   B 1 27  ? 0.617   25.689  36.577  1   61.481  ? 39  ARG   A NH1  1 ? 2 
ATOM   2185 N NH2  . ARG   B 1 27  ? -1.441  26.22   35.789  1   60.147  ? 39  ARG   A NH2  1 ? 2 
ATOM   2186 H H    . ARG   B 1 27  ? -3.656  20.493  39.063  1   46.74   ? 39  ARG   A H    1 c 2 
ATOM   2187 H HA   . ARG   B 1 27  ? -2.457  21.842  41.184  1   52.83   ? 39  ARG   A HA   1 c 2 
ATOM   2188 H HB2  . ARG   B 1 27  ? -0.964  22.15   39.316  1   53.069  ? 39  ARG   A HB2  1 c 2 
ATOM   2189 H HB3  . ARG   B 1 27  ? -2.139  22.873  38.539  1   51.711  ? 39  ARG   A HB3  1 c 2 
ATOM   2190 H HG2  . ARG   B 1 27  ? -2.151  24.55   40.286  1   56.717  ? 39  ARG   A HG2  1 c 2 
ATOM   2191 H HG3  . ARG   B 1 27  ? -0.843  23.872  40.869  1   58.026  ? 39  ARG   A HG3  1 c 2 
ATOM   2192 H HD2  . ARG   B 1 27  ? -0.197  25.695  39.595  1   61.5    ? 39  ARG   A HD2  1 c 2 
ATOM   2193 H HD3  . ARG   B 1 27  ? 0.3     24.386  38.854  1   58.79   ? 39  ARG   A HD3  1 c 2 
ATOM   2194 H HE   . ARG   B 1 27  ? -2.101  25.244  37.938  1   57.25   ? 39  ARG   A HE   1 c 2 
ATOM   2195 H HH11 . ARG   B 1 27  ? 1.169   25.92   37.228  1   63.584  ? 39  ARG   A HH11 1 c 2 
ATOM   2196 H HH12 . ARG   B 1 27  ? 0.935   25.43   35.794  1   61.004  ? 39  ARG   A HH12 1 c 2 
ATOM   2197 H HH21 . ARG   B 1 27  ? -2.304  26.031  35.766  1   58.384  ? 39  ARG   A HH21 1 c 2 
ATOM   2198 H HH22 . ARG   B 1 27  ? -1.078  26.724  35.16   1   61.178  ? 39  ARG   A HH22 1 c 2 
ATOM   2199 N N    . VAL   B 1 28  ? -4.467  23.22   41.448  1   56.527  ? 40  VAL   A N    1 ? 2 
ATOM   2200 C CA   . VAL   B 1 28  ? -5.756  23.858  41.649  1   59.637  ? 40  VAL   A CA   1 ? 2 
ATOM   2201 C C    . VAL   B 1 28  ? -5.748  25.195  40.908  1   60.879  ? 40  VAL   A C    1 ? 2 
ATOM   2202 O O    . VAL   B 1 28  ? -4.766  25.949  41.005  1   63.821  ? 40  VAL   A O    1 ? 2 
ATOM   2203 C CB   . VAL   B 1 28  ? -6.051  24.01   43.156  1   66.275  ? 40  VAL   A CB   1 ? 2 
ATOM   2204 C CG1  . VAL   B 1 28  ? -7.249  24.904  43.448  1   70.406  ? 40  VAL   A CG1  1 ? 2 
ATOM   2205 C CG2  . VAL   B 1 28  ? -6.249  22.657  43.83   1   65.098  ? 40  VAL   A CG2  1 ? 2 
ATOM   2206 H H    . VAL   B 1 28  ? -3.872  23.208  42.142  1   58.078  ? 40  VAL   A H    1 c 2 
ATOM   2207 H HA   . VAL   B 1 28  ? -6.445  23.287  41.256  1   57.712  ? 40  VAL   A HA   1 c 2 
ATOM   2208 H HB   . VAL   B 1 28  ? -5.259  24.433  43.565  1   67.9    ? 40  VAL   A HB   1 c 2 
ATOM   2209 H HG11 . VAL   B 1 28  ? -7.969  24.696  42.829  1   67.9    ? 40  VAL   A HG11 1 c 2 
ATOM   2210 H HG12 . VAL   B 1 28  ? -6.992  25.834  43.346  1   71.409  ? 40  VAL   A HG12 1 c 2 
ATOM   2211 H HG13 . VAL   B 1 28  ? -7.553  24.753  44.359  1   70.853  ? 40  VAL   A HG13 1 c 2 
ATOM   2212 H HG21 . VAL   B 1 28  ? -6.427  22.787  44.777  1   67.018  ? 40  VAL   A HG21 1 c 2 
ATOM   2213 H HG22 . VAL   B 1 28  ? -5.445  22.121  43.724  1   64.598  ? 40  VAL   A HG22 1 c 2 
ATOM   2214 H HG23 . VAL   B 1 28  ? -7      22.196  43.421  1   63.27   ? 40  VAL   A HG23 1 c 2 
ATOM   2215 N N    . GLY   B 1 29  ? -6.845  25.45   40.17   1   60.706  ? 41  GLY   A N    1 ? 2 
ATOM   2216 C CA   . GLY   B 1 29  ? -7.128  26.737  39.554  1   64.022  ? 41  GLY   A CA   1 ? 2 
ATOM   2217 C C    . GLY   B 1 29  ? -7.694  27.728  40.58   1   70.403  ? 41  GLY   A C    1 ? 2 
ATOM   2218 O O    . GLY   B 1 29  ? -7.545  27.542  41.783  1   68.394  ? 41  GLY   A O    1 ? 2 
ATOM   2219 H H    . GLY   B 1 29  ? -7.451  24.776  40.047  1   58.987  ? 41  GLY   A H    1 c 2 
ATOM   2220 H HA2  . GLY   B 1 29  ? -6.298  27.1    39.164  1   65.07   ? 41  GLY   A HA2  1 c 2 
ATOM   2221 H HA3  . GLY   B 1 29  ? -7.778  26.608  38.825  1   62.953  ? 41  GLY   A HA3  1 c 2 
ATOM   2222 N N    . ASN   B 1 30  ? -8.37   28.775  40.093  1   73.858  ? 42  ASN   A N    1 ? 2 
ATOM   2223 C CA   . ASN   B 1 30  ? -8.941  29.811  40.944  1   77.786  ? 42  ASN   A CA   1 ? 2 
ATOM   2224 C C    . ASN   B 1 30  ? -10.235 30.294  40.295  1   76.775  ? 42  ASN   A C    1 ? 2 
ATOM   2225 O O    . ASN   B 1 30  ? -10.483 30.011  39.13   1   68.675  ? 42  ASN   A O    1 ? 2 
ATOM   2226 C CB   . ASN   B 1 30  ? -7.957  30.961  41.115  1   83.374  ? 42  ASN   A CB   1 ? 2 
ATOM   2227 C CG   . ASN   B 1 30  ? -7.284  31.256  39.797  1   90.948  ? 42  ASN   A CG   1 ? 2 
ATOM   2228 O OD1  . ASN   B 1 30  ? -6.073  31.056  39.671  1   97.984  ? 42  ASN   A OD1  1 ? 2 
ATOM   2229 N ND2  . ASN   B 1 30  ? -8.057  31.627  38.782  1   94.616  ? 42  ASN   A ND2  1 ? 2 
ATOM   2230 H H    . ASN   B 1 30  ? -8.485  28.841  39.188  1   72.593  ? 42  ASN   A H    1 c 2 
ATOM   2231 H HA   . ASN   B 1 30  ? -9.137  29.434  41.831  1   77.883  ? 42  ASN   A HA   1 c 2 
ATOM   2232 H HB2  . ASN   B 1 30  ? -8.431  31.758  41.427  1   87.538  ? 42  ASN   A HB2  1 c 2 
ATOM   2233 H HB3  . ASN   B 1 30  ? -7.283  30.72   41.781  1   85.124  ? 42  ASN   A HB3  1 c 2 
ATOM   2234 H HD21 . ASN   B 1 30  ? -7.966  31.234  37.991  1   91.31   ? 42  ASN   A HD21 1 c 2 
ATOM   2235 H HD22 . ASN   B 1 30  ? -8.66   32.268  38.895  1   95.492  ? 42  ASN   A HD22 1 c 2 
ATOM   2236 N N    . GLY   B 1 31  ? -11.022 31.068  41.037  1   82.149  ? 43  GLY   A N    1 ? 2 
ATOM   2237 C CA   . GLY   B 1 31  ? -12.319 31.51   40.562  1   84.662  ? 43  GLY   A CA   1 ? 2 
ATOM   2238 C C    . GLY   B 1 31  ? -13.336 30.41   40.82   1   86.847  ? 43  GLY   A C    1 ? 2 
ATOM   2239 O O    . GLY   B 1 31  ? -12.984 29.237  40.811  1   82.548  ? 43  GLY   A O    1 ? 2 
ATOM   2240 H H    . GLY   B 1 31  ? -10.743 31.331  41.867  1   83.898  ? 43  GLY   A H    1 c 2 
ATOM   2241 H HA2  . GLY   B 1 31  ? -12.581 32.333  41.038  1   88.931  ? 43  GLY   A HA2  1 c 2 
ATOM   2242 H HA3  . GLY   B 1 31  ? -12.272 31.71   39.597  1   84.82   ? 43  GLY   A HA3  1 c 2 
ATOM   2243 N N    . GLU   B 1 32  ? -14.583 30.807  41.081  1   97.686  ? 44  GLU   A N    1 ? 2 
ATOM   2244 C CA   . GLU   B 1 32  ? -15.642 29.868  41.418  1   96.338  ? 44  GLU   A CA   1 ? 2 
ATOM   2245 C C    . GLU   B 1 32  ? -16.135 29.177  40.145  1   89.741  ? 44  GLU   A C    1 ? 2 
ATOM   2246 O O    . GLU   B 1 32  ? -16.684 28.075  40.214  1   93.007  ? 44  GLU   A O    1 ? 2 
ATOM   2247 C CB   . GLU   B 1 32  ? -16.757 30.594  42.18   1   98.782  ? 44  GLU   A CB   1 ? 2 
ATOM   2248 H H    . GLU   B 1 32  ? -14.782 31.699  41.041  1   98.416  ? 44  GLU   A H    1 c 2 
ATOM   2249 H HA   . GLU   B 1 32  ? -15.261 29.177  42.019  1   93.656  ? 44  GLU   A HA   1 c 2 
ATOM   2250 H HB2  . GLU   B 1 32  ? -16.283 31.219  42.938  0   30      ? 44  GLU   A HB2  1 c 2 
ATOM   2251 H HB3  . GLU   B 1 32  ? -17.583 30.322  41.962  0   30      ? 44  GLU   A HB3  1 c 2 
ATOM   2252 N N    . GLU   B 1 33  ? -15.883 29.794  38.982  1   81.703  ? 45  GLU   A N    1 ? 2 
ATOM   2253 C CA   . GLU   B 1 33  ? -16.625 29.462  37.78   1   81.818  ? 45  GLU   A CA   1 ? 2 
ATOM   2254 C C    . GLU   B 1 33  ? -15.853 28.495  36.882  1   71.36   ? 45  GLU   A C    1 ? 2 
ATOM   2255 O O    . GLU   B 1 33  ? -14.658 28.631  36.64   1   62.651  ? 45  GLU   A O    1 ? 2 
ATOM   2256 C CB   . GLU   B 1 33  ? -17.004 30.738  37.036  1   91.541  ? 45  GLU   A CB   1 ? 2 
ATOM   2257 C CG   . GLU   B 1 33  ? -15.811 31.614  36.673  1   97.527  ? 45  GLU   A CG   1 ? 2 
ATOM   2258 C CD   . GLU   B 1 33  ? -16.314 32.963  36.204  1   105.704 ? 45  GLU   A CD   1 ? 2 
ATOM   2259 O OE1  . GLU   B 1 33  ? -17.134 33.568  36.933  1   108.588 ? 45  GLU   A OE1  1 ? 2 
ATOM   2260 O OE2  . GLU   B 1 33  ? -15.894 33.389  35.107  1   107.923 ? 45  GLU   A OE2  1 ? 2 
ATOM   2261 H H    . GLU   B 1 33  ? -15.225 30.426  38.937  1   85.36   ? 45  GLU   A H    1 c 2 
ATOM   2262 H HA   . GLU   B 1 33  ? -17.469 29.022  38.056  1   81.409  ? 45  GLU   A HA   1 c 2 
ATOM   2263 H HB2  . GLU   B 1 33  ? -17.477 30.492  36.214  1   90.428  ? 45  GLU   A HB2  1 c 2 
ATOM   2264 H HB3  . GLU   B 1 33  ? -17.625 31.25   37.595  1   94.12   ? 45  GLU   A HB3  1 c 2 
ATOM   2265 H HG2  . GLU   B 1 33  ? -15.231 31.739  37.452  1   97.288  ? 45  GLU   A HG2  1 c 2 
ATOM   2266 H HG3  . GLU   B 1 33  ? -15.294 31.192  35.954  1   94.46   ? 45  GLU   A HG3  1 c 2 
ATOM   2267 N N    . THR   B 1 34  ? -16.584 27.514  36.364  1   70.545  ? 46  THR   A N    1 ? 2 
ATOM   2268 C CA   . THR   B 1 34  ? -16.083 26.653  35.312  1   63.873  ? 46  THR   A CA   1 ? 2 
ATOM   2269 C C    . THR   B 1 34  ? -16.681 27.133  33.998  1   68.063  ? 46  THR   A C    1 ? 2 
ATOM   2270 O O    . THR   B 1 34  ? -17.679 27.833  34.005  1   73.704  ? 46  THR   A O    1 ? 2 
ATOM   2271 C CB   . THR   B 1 34  ? -16.5   25.221  35.62   1   63.959  ? 46  THR   A CB   1 ? 2 
ATOM   2272 O OG1  . THR   B 1 34  ? -17.92  25.26   35.65   1   59.309  ? 46  THR   A OG1  1 ? 2 
ATOM   2273 C CG2  . THR   B 1 34  ? -15.919 24.711  36.926  1   61.318  ? 46  THR   A CG2  1 ? 2 
ATOM   2274 H H    . THR   B 1 34  ? -17.43  27.372  36.679  1   70.442  ? 46  THR   A H    1 c 2 
ATOM   2275 H HA   . THR   B 1 34  ? -15.104 26.71   35.277  1   64.636  ? 46  THR   A HA   1 c 2 
ATOM   2276 H HB   . THR   B 1 34  ? -16.204 24.632  34.886  1   59.749  ? 46  THR   A HB   1 c 2 
ATOM   2277 H HG1  . THR   B 1 34  ? -18.187 25.909  36.349  0   30      ? 46  THR   A HG1  1 c 2 
ATOM   2278 H HG21 . THR   B 1 34  ? -16.178 23.783  37.055  1   60.387  ? 46  THR   A HG21 1 c 2 
ATOM   2279 H HG22 . THR   B 1 34  ? -16.257 25.245  37.664  1   63.978  ? 46  THR   A HG22 1 c 2 
ATOM   2280 H HG23 . THR   B 1 34  ? -14.95  24.775  36.897  1   61.017  ? 46  THR   A HG23 1 c 2 
ATOM   2281 N N    . PRO   B 1 35  ? -16.119 26.774  32.829  1   68.536  ? 47  PRO   A N    1 ? 2 
ATOM   2282 C CA   . PRO   B 1 35  ? -16.731 27.152  31.565  1   73.074  ? 47  PRO   A CA   1 ? 2 
ATOM   2283 C C    . PRO   B 1 35  ? -18.171 26.65   31.427  1   78.773  ? 47  PRO   A C    1 ? 2 
ATOM   2284 O O    . PRO   B 1 35  ? -18.503 25.555  31.909  1   73.925  ? 47  PRO   A O    1 ? 2 
ATOM   2285 C CB   . PRO   B 1 35  ? -15.82  26.496  30.536  1   71.023  ? 47  PRO   A CB   1 ? 2 
ATOM   2286 C CG   . PRO   B 1 35  ? -14.53  26.137  31.241  1   66.053  ? 47  PRO   A CG   1 ? 2 
ATOM   2287 C CD   . PRO   B 1 35  ? -14.902 25.955  32.676  1   67.169  ? 47  PRO   A CD   1 ? 2 
ATOM   2288 H HA   . PRO   B 1 35  ? -16.705 28.127  31.466  1   76.03   ? 47  PRO   A HA   1 c 2 
ATOM   2289 H HB2  . PRO   B 1 35  ? -16.241 25.697  30.174  1   68.739  ? 47  PRO   A HB2  1 c 2 
ATOM   2290 H HB3  . PRO   B 1 35  ? -15.645 27.108  29.795  1   71.745  ? 47  PRO   A HB3  1 c 2 
ATOM   2291 H HG2  . PRO   B 1 35  ? -14.154 25.311  30.877  1   64.694  ? 47  PRO   A HG2  1 c 2 
ATOM   2292 H HG3  . PRO   B 1 35  ? -13.871 26.852  31.146  1   68.163  ? 47  PRO   A HG3  1 c 2 
ATOM   2293 H HD2  . PRO   B 1 35  ? -15.089 25.017  32.878  1   64.468  ? 47  PRO   A HD2  1 c 2 
ATOM   2294 H HD3  . PRO   B 1 35  ? -14.194 26.277  33.263  1   66.539  ? 47  PRO   A HD3  1 c 2 
ATOM   2295 N N    . MET   B 1 36  ? -19.004 27.468  30.763  1   83.083  ? 48  MET   A N    1 ? 2 
ATOM   2296 C CA   . MET   B 1 36  ? -20.343 27.075  30.332  1   80.408  ? 48  MET   A CA   1 ? 2 
ATOM   2297 C C    . MET   B 1 36  ? -20.238 26.481  28.924  1   76.34   ? 48  MET   A C    1 ? 2 
ATOM   2298 O O    . MET   B 1 36  ? -19.292 26.778  28.187  1   71.609  ? 48  MET   A O    1 ? 2 
ATOM   2299 C CB   . MET   B 1 36  ? -21.313 28.268  30.279  1   86.821  ? 48  MET   A CB   1 ? 2 
ATOM   2300 C CG   . MET   B 1 36  ? -21.461 29.107  31.563  1   87.659  ? 48  MET   A CG   1 ? 2 
ATOM   2301 S SD   . MET   B 1 36  ? -22.395 28.293  32.875  1   84.344  ? 48  MET   A SD   1 ? 2 
ATOM   2302 C CE   . MET   B 1 36  ? -21.181 27.453  33.907  1   81.186  ? 48  MET   A CE   1 ? 2 
ATOM   2303 H H    . MET   B 1 36  ? -18.723 28.317  30.572  1   83.708  ? 48  MET   A H    1 c 2 
ATOM   2304 H HA   . MET   B 1 36  ? -20.691 26.386  30.953  1   79.617  ? 48  MET   A HA   1 c 2 
ATOM   2305 H HB2  . MET   B 1 36  ? -21.021 28.863  29.555  1   87.478  ? 48  MET   A HB2  1 c 2 
ATOM   2306 H HB3  . MET   B 1 36  ? -22.198 27.926  30.031  1   87.04   ? 48  MET   A HB3  1 c 2 
ATOM   2307 H HG2  . MET   B 1 36  ? -20.572 29.325  31.906  1   86.428  ? 48  MET   A HG2  1 c 2 
ATOM   2308 H HG3  . MET   B 1 36  ? -21.907 29.949  31.343  1   91.026  ? 48  MET   A HG3  1 c 2 
ATOM   2309 H HE1  . MET   B 1 36  ? -21.631 27.039  34.667  1   80.91   ? 48  MET   A HE1  1 c 2 
ATOM   2310 H HE2  . MET   B 1 36  ? -20.729 26.765  33.384  1   78.032  ? 48  MET   A HE2  1 c 2 
ATOM   2311 H HE3  . MET   B 1 36  ? -20.526 28.099  34.23   1   81.452  ? 48  MET   A HE3  1 c 2 
ATOM   2312 N N    . ILE   B 1 37  ? -21.221 25.644  28.553  1   73.538  ? 49  ILE   A N    1 ? 2 
ATOM   2313 C CA   . ILE   B 1 37  ? -21.301 25.098  27.203  1   71.097  ? 49  ILE   A CA   1 ? 2 
ATOM   2314 C C    . ILE   B 1 37  ? -21.356 26.273  26.226  1   73.676  ? 49  ILE   A C    1 ? 2 
ATOM   2315 O O    . ILE   B 1 37  ? -22.147 27.192  26.44   1   74.489  ? 49  ILE   A O    1 ? 2 
ATOM   2316 C CB   . ILE   B 1 37  ? -22.544 24.192  27.06   1   76.152  ? 49  ILE   A CB   1 ? 2 
ATOM   2317 C CG1  . ILE   B 1 37  ? -22.632 23.023  28.095  1   76.825  ? 49  ILE   A CG1  1 ? 2 
ATOM   2318 C CG2  . ILE   B 1 37  ? -22.705 23.707  25.619  1   75.588  ? 49  ILE   A CG2  1 ? 2 
ATOM   2319 C CD1  . ILE   B 1 37  ? -21.322 22.531  28.715  1   76.613  ? 49  ILE   A CD1  1 ? 2 
ATOM   2320 H H    . ILE   B 1 37  ? -21.863 25.413  29.161  1   74.391  ? 49  ILE   A H    1 c 2 
ATOM   2321 H HA   . ILE   B 1 37  ? -20.499 24.569  27.026  1   69.423  ? 49  ILE   A HA   1 c 2 
ATOM   2322 H HB   . ILE   B 1 37  ? -23.315 24.766  27.24   1   78.591  ? 49  ILE   A HB   1 c 2 
ATOM   2323 H HG12 . ILE   B 1 37  ? -23.221 23.309  28.823  1   78.395  ? 49  ILE   A HG12 1 c 2 
ATOM   2324 H HG13 . ILE   B 1 37  ? -23.064 22.261  27.659  1   76.549  ? 49  ILE   A HG13 1 c 2 
ATOM   2325 H HG21 . ILE   B 1 37  ? -23.407 23.037  25.576  1   76.165  ? 49  ILE   A HG21 1 c 2 
ATOM   2326 H HG22 . ILE   B 1 37  ? -21.87  23.318  25.311  1   73.544  ? 49  ILE   A HG22 1 c 2 
ATOM   2327 H HG23 . ILE   B 1 37  ? -22.941 24.455  25.045  1   78.486  ? 49  ILE   A HG23 1 c 2 
ATOM   2328 H HD11 . ILE   B 1 37  ? -20.683 22.323  28.007  1   74.158  ? 49  ILE   A HD11 1 c 2 
ATOM   2329 H HD12 . ILE   B 1 37  ? -21.495 21.727  29.241  1   74.244  ? 49  ILE   A HD12 1 c 2 
ATOM   2330 H HD13 . ILE   B 1 37  ? -20.948 23.221  29.296  1   75.704  ? 49  ILE   A HD13 1 c 2 
ATOM   2331 N N    . GLY   B 1 38  ? -20.517 26.26   25.174  1   68.631  ? 50  GLY   A N    1 ? 2 
ATOM   2332 C CA   . GLY   B 1 38  ? -20.491 27.353  24.211  1   71.266  ? 50  GLY   A CA   1 ? 2 
ATOM   2333 C C    . GLY   B 1 38  ? -19.256 28.253  24.317  1   70.857  ? 50  GLY   A C    1 ? 2 
ATOM   2334 O O    . GLY   B 1 38  ? -18.915 28.94   23.357  1   70.845  ? 50  GLY   A O    1 ? 2 
ATOM   2335 H H    . GLY   B 1 38  ? -19.949 25.554  25.058  1   66.707  ? 50  GLY   A H    1 c 2 
ATOM   2336 H HA2  . GLY   B 1 38  ? -20.529 26.969  23.304  1   71.443  ? 50  GLY   A HA2  1 c 2 
ATOM   2337 H HA3  . GLY   B 1 38  ? -21.3   27.903  24.331  1   74.44   ? 50  GLY   A HA3  1 c 2 
ATOM   2338 N N    . ASP   B 1 39  ? -18.603 28.278  25.487  1   68.775  ? 51  ASP   A N    1 ? 2 
ATOM   2339 C CA   . ASP   B 1 39  ? -17.424 29.107  25.694  1   69.363  ? 51  ASP   A CA   1 ? 2 
ATOM   2340 C C    . ASP   B 1 39  ? -16.313 28.741  24.702  1   68.87   ? 51  ASP   A C    1 ? 2 
ATOM   2341 O O    . ASP   B 1 39  ? -16.174 27.584  24.295  1   66.766  ? 51  ASP   A O    1 ? 2 
ATOM   2342 C CB   . ASP   B 1 39  ? -16.966 29.035  27.146  1   68.836  ? 51  ASP   A CB   1 ? 2 
ATOM   2343 C CG   . ASP   B 1 39  ? -17.887 29.702  28.164  1   70.992  ? 51  ASP   A CG   1 ? 2 
ATOM   2344 O OD1  . ASP   B 1 39  ? -18.837 30.357  27.734  1   75.828  ? 51  ASP   A OD1  1 ? 2 
ATOM   2345 O OD2  . ASP   B 1 39  ? -17.659 29.563  29.39   1   68.167  ? 51  ASP   A OD2  1 ? 2 
ATOM   2346 H H    . ASP   B 1 39  ? -18.905 27.766  26.181  1   67.262  ? 51  ASP   A H    1 c 2 
ATOM   2347 H HA   . ASP   B 1 39  ? -17.682 30.041  25.525  1   73.326  ? 51  ASP   A HA   1 c 2 
ATOM   2348 H HB2  . ASP   B 1 39  ? -16.869 28.092  27.397  1   65.319  ? 51  ASP   A HB2  1 c 2 
ATOM   2349 H HB3  . ASP   B 1 39  ? -16.083 29.455  27.216  1   68.542  ? 51  ASP   A HB3  1 c 2 
ATOM   2350 N N    . LYS   B 1 40  ? -15.528 29.754  24.3    1   73.866  ? 52  LYS   A N    1 ? 2 
ATOM   2351 C CA   . LYS   B 1 40  ? -14.255 29.549  23.616  1   74.115  ? 52  LYS   A CA   1 ? 2 
ATOM   2352 C C    . LYS   B 1 40  ? -13.203 29.298  24.693  1   73.381  ? 52  LYS   A C    1 ? 2 
ATOM   2353 O O    . LYS   B 1 40  ? -12.974 30.146  25.559  1   77.514  ? 52  LYS   A O    1 ? 2 
ATOM   2354 C CB   . LYS   B 1 40  ? -13.832 30.705  22.695  1   77.584  ? 52  LYS   A CB   1 ? 2 
ATOM   2355 H H    . LYS   B 1 40  ? -15.801 30.611  24.461  1   76.491  ? 52  LYS   A H    1 c 2 
ATOM   2356 H HA   . LYS   B 1 40  ? -14.334 28.735  23.057  1   72.22   ? 52  LYS   A HA   1 c 2 
ATOM   2357 H HB2  . LYS   B 1 40  ? -12.901 30.794  22.629  0   30      ? 52  LYS   A HB2  1 c 2 
ATOM   2358 H HB3  . LYS   B 1 40  ? -14.696 31.174  22.33   0   30      ? 52  LYS   A HB3  1 c 2 
ATOM   2359 N N    . VAL   B 1 41  ? -12.584 28.111  24.635  1   71.158  ? 53  VAL   A N    1 ? 2 
ATOM   2360 C CA   . VAL   B 1 41  ? -11.715 27.612  25.692  1   66.321  ? 53  VAL   A CA   1 ? 2 
ATOM   2361 C C    . VAL   B 1 41  ? -10.297 27.48   25.155  1   64.417  ? 53  VAL   A C    1 ? 2 
ATOM   2362 O O    . VAL   B 1 41  ? -10.091 26.963  24.06   1   66.642  ? 53  VAL   A O    1 ? 2 
ATOM   2363 C CB   . VAL   B 1 41  ? -12.296 26.264  26.152  1   64.648  ? 53  VAL   A CB   1 ? 2 
ATOM   2364 C CG1  . VAL   B 1 41  ? -11.402 25.548  27.146  1   64.369  ? 53  VAL   A CG1  1 ? 2 
ATOM   2365 C CG2  . VAL   B 1 41  ? -13.696 26.433  26.731  1   64.36   ? 53  VAL   A CG2  1 ? 2 
ATOM   2366 H H    . VAL   B 1 41  ? -12.708 27.588  23.896  1   69.601  ? 53  VAL   A H    1 c 2 
ATOM   2367 H HA   . VAL   B 1 41  ? -11.723 28.238  26.441  1   67.948  ? 53  VAL   A HA   1 c 2 
ATOM   2368 H HB   . VAL   B 1 41  ? -12.37  25.693  25.352  1   63.782  ? 53  VAL   A HB   1 c 2 
ATOM   2369 H HG11 . VAL   B 1 41  ? -11.176 26.152  27.874  1   64.388  ? 53  VAL   A HG11 1 c 2 
ATOM   2370 H HG12 . VAL   B 1 41  ? -10.587 25.256  26.704  1   62.787  ? 53  VAL   A HG12 1 c 2 
ATOM   2371 H HG13 . VAL   B 1 41  ? -11.868 24.776  27.502  1   61.617  ? 53  VAL   A HG13 1 c 2 
ATOM   2372 H HG21 . VAL   B 1 41  ? -13.986 25.595  27.131  1   62.62   ? 53  VAL   A HG21 1 c 2 
ATOM   2373 H HG22 . VAL   B 1 41  ? -14.314 26.682  26.023  1   66.318  ? 53  VAL   A HG22 1 c 2 
ATOM   2374 H HG23 . VAL   B 1 41  ? -13.686 27.128  27.41   1   66.067  ? 53  VAL   A HG23 1 c 2 
ATOM   2375 N N    . TYR   B 1 42  ? -9.331  27.954  25.944  1   66.302  ? 54  TYR   A N    1 ? 2 
ATOM   2376 C CA   . TYR   B 1 42  ? -7.925  27.908  25.572  1   67.033  ? 54  TYR   A CA   1 ? 2 
ATOM   2377 C C    . TYR   B 1 42  ? -7.188  26.991  26.555  1   62.62   ? 54  TYR   A C    1 ? 2 
ATOM   2378 O O    . TYR   B 1 42  ? -7.241  27.229  27.765  1   54.682  ? 54  TYR   A O    1 ? 2 
ATOM   2379 C CB   . TYR   B 1 42  ? -7.332  29.324  25.609  1   73.146  ? 54  TYR   A CB   1 ? 2 
ATOM   2380 C CG   . TYR   B 1 42  ? -7.975  30.405  24.748  1   75.048  ? 54  TYR   A CG   1 ? 2 
ATOM   2381 C CD1  . TYR   B 1 42  ? -9.243  30.898  25.024  1   77.993  ? 54  TYR   A CD1  1 ? 2 
ATOM   2382 C CD2  . TYR   B 1 42  ? -7.266  30.997  23.705  1   79.158  ? 54  TYR   A CD2  1 ? 2 
ATOM   2383 C CE1  . TYR   B 1 42  ? -9.808  31.905  24.254  1   83.293  ? 54  TYR   A CE1  1 ? 2 
ATOM   2384 C CE2  . TYR   B 1 42  ? -7.806  32.019  22.944  1   83.331  ? 54  TYR   A CE2  1 ? 2 
ATOM   2385 C CZ   . TYR   B 1 42  ? -9.08   32.48   23.223  1   87.091  ? 54  TYR   A CZ   1 ? 2 
ATOM   2386 O OH   . TYR   B 1 42  ? -9.615  33.481  22.457  1   95.461  ? 54  TYR   A OH   1 ? 2 
ATOM   2387 H H    . TYR   B 1 42  ? -9.556  28.321  26.75   1   66.555  ? 54  TYR   A H    1 c 2 
ATOM   2388 H HA   . TYR   B 1 42  ? -7.839  27.543  24.653  1   66.788  ? 54  TYR   A HA   1 c 2 
ATOM   2389 H HB2  . TYR   B 1 42  ? -7.348  29.63   26.543  1   72.353  ? 54  TYR   A HB2  1 c 2 
ATOM   2390 H HB3  . TYR   B 1 42  ? -6.384  29.257  25.357  1   72.54   ? 54  TYR   A HB3  1 c 2 
ATOM   2391 H HD1  . TYR   B 1 42  ? -9.743  30.522  25.73   1   75.996  ? 54  TYR   A HD1  1 c 2 
ATOM   2392 H HD2  . TYR   B 1 42  ? -6.391  30.698  23.515  1   78.476  ? 54  TYR   A HD2  1 c 2 
ATOM   2393 H HE1  . TYR   B 1 42  ? -10.674 32.22   24.451  1   84.307  ? 54  TYR   A HE1  1 c 2 
ATOM   2394 H HE2  . TYR   B 1 42  ? -7.313  32.394  22.235  1   86.369  ? 54  TYR   A HE2  1 c 2 
ATOM   2395 H HH   . TYR   B 1 42  ? -10.55  33.628  22.761  0   30      ? 54  TYR   A HH   1 c 2 
ATOM   2396 N N    . VAL   B 1 43  ? -6.51   25.944  26.039  1   58.911  ? 55  VAL   A N    1 ? 2 
ATOM   2397 C CA   . VAL   B 1 43  ? -5.76   25.037  26.903  1   55.005  ? 55  VAL   A CA   1 ? 2 
ATOM   2398 C C    . VAL   B 1 43  ? -4.38   24.767  26.323  1   54.069  ? 55  VAL   A C    1 ? 2 
ATOM   2399 O O    . VAL   B 1 43  ? -4.173  24.931  25.128  1   60.468  ? 55  VAL   A O    1 ? 2 
ATOM   2400 C CB   . VAL   B 1 43  ? -6.464  23.683  27.099  1   50.333  ? 55  VAL   A CB   1 ? 2 
ATOM   2401 C CG1  . VAL   B 1 43  ? -7.906  23.847  27.575  1   49.254  ? 55  VAL   A CG1  1 ? 2 
ATOM   2402 C CG2  . VAL   B 1 43  ? -6.393  22.84   25.828  1   50.824  ? 55  VAL   A CG2  1 ? 2 
ATOM   2403 H H    . VAL   B 1 43  ? -6.515  25.796  25.137  1   59.332  ? 55  VAL   A H    1 c 2 
ATOM   2404 H HA   . VAL   B 1 43  ? -5.652  25.46   27.774  1   55.279  ? 55  VAL   A HA   1 c 2 
ATOM   2405 H HB   . VAL   B 1 43  ? -5.971  23.2    27.801  1   49.679  ? 55  VAL   A HB   1 c 2 
ATOM   2406 H HG11 . VAL   B 1 43  ? -8.428  24.293  26.887  1   50.707  ? 55  VAL   A HG11 1 c 2 
ATOM   2407 H HG12 . VAL   B 1 43  ? -7.921  24.379  28.388  1   50.198  ? 55  VAL   A HG12 1 c 2 
ATOM   2408 H HG13 . VAL   B 1 43  ? -8.29   22.973  27.755  1   47.638  ? 55  VAL   A HG13 1 c 2 
ATOM   2409 H HG21 . VAL   B 1 43  ? -6.95   22.053  25.934  1   48.727  ? 55  VAL   A HG21 1 c 2 
ATOM   2410 H HG22 . VAL   B 1 43  ? -5.475  22.563  25.667  1   50.562  ? 55  VAL   A HG22 1 c 2 
ATOM   2411 H HG23 . VAL   B 1 43  ? -6.711  23.362  25.072  1   51.854  ? 55  VAL   A HG23 1 c 2 
ATOM   2412 N N    . HIS   B 1 44  ? -3.481  24.257  27.176  1   54.114  ? 56  HIS   A N    1 ? 2 
ATOM   2413 C CA   . HIS   B 1 44  ? -2.336  23.461  26.751  1   51.73   ? 56  HIS   A CA   1 ? 2 
ATOM   2414 C C    . HIS   B 1 44  ? -2.581  22.03   27.207  1   47.357  ? 56  HIS   A C    1 ? 2 
ATOM   2415 O O    . HIS   B 1 44  ? -3.248  21.816  28.211  1   47.692  ? 56  HIS   A O    1 ? 2 
ATOM   2416 C CB   . HIS   B 1 44  ? -1.035  24.018  27.34   1   58.22   ? 56  HIS   A CB   1 ? 2 
ATOM   2417 C CG   . HIS   B 1 44  ? -0.362  25.05   26.502  1   59.902  ? 56  HIS   A CG   1 ? 2 
ATOM   2418 N ND1  . HIS   B 1 44  ? -0.007  24.783  25.199  1   63.202  ? 56  HIS   A ND1  1 ? 2 
ATOM   2419 C CD2  . HIS   B 1 44  ? 0.05    26.297  26.754  1   61.137  ? 56  HIS   A CD2  1 ? 2 
ATOM   2420 C CE1  . HIS   B 1 44  ? 0.611   25.842  24.686  1   65.575  ? 56  HIS   A CE1  1 ? 2 
ATOM   2421 N NE2  . HIS   B 1 44  ? 0.646   26.778  25.615  1   64.809  ? 56  HIS   A NE2  1 ? 2 
ATOM   2422 H H    . HIS   B 1 44  ? -3.589  24.415  28.07   1   53.23   ? 56  HIS   A H    1 c 2 
ATOM   2423 H HA   . HIS   B 1 44  ? -2.287  23.471  25.765  1   53.374  ? 56  HIS   A HA   1 c 2 
ATOM   2424 H HB2  . HIS   B 1 44  ? -1.232  24.406  28.22   1   56.935  ? 56  HIS   A HB2  1 c 2 
ATOM   2425 H HB3  . HIS   B 1 44  ? -0.412  23.273  27.483  1   56.169  ? 56  HIS   A HB3  1 c 2 
ATOM   2426 H HD1  . HIS   B 1 44  ? -0.164  24.032  24.714  0   30      ? 56  HIS   A HD1  1 c 2 
ATOM   2427 H HD2  . HIS   B 1 44  ? -0.045  26.765  27.56   1   62.405  ? 56  HIS   A HD2  1 c 2 
ATOM   2428 H HE1  . HIS   B 1 44  ? 0.939   25.921  23.807  1   66.853  ? 56  HIS   A HE1  1 c 2 
ATOM   2429 H HE2  . HIS   B 1 44  ? 0.989   27.571  25.477  0   30      ? 56  HIS   A HE2  1 c 2 
ATOM   2430 N N    . TYR   B 1 45  ? -2.075  21.05   26.454  1   48.497  ? 57  TYR   A N    1 ? 2 
ATOM   2431 C CA   . TYR   B 1 45  ? -2.297  19.656  26.797  1   46.211  ? 57  TYR   A CA   1 ? 2 
ATOM   2432 C C    . TYR   B 1 45  ? -1.117  18.798  26.351  1   49.201  ? 57  TYR   A C    1 ? 2 
ATOM   2433 O O    . TYR   B 1 45  ? -0.417  19.118  25.402  1   52.93   ? 57  TYR   A O    1 ? 2 
ATOM   2434 C CB   . TYR   B 1 45  ? -3.587  19.129  26.179  1   44.593  ? 57  TYR   A CB   1 ? 2 
ATOM   2435 C CG   . TYR   B 1 45  ? -3.472  18.878  24.682  1   46.164  ? 57  TYR   A CG   1 ? 2 
ATOM   2436 C CD1  . TYR   B 1 45  ? -2.969  17.687  24.185  1   42.65   ? 57  TYR   A CD1  1 ? 2 
ATOM   2437 C CD2  . TYR   B 1 45  ? -3.816  19.862  23.762  1   50.366  ? 57  TYR   A CD2  1 ? 2 
ATOM   2438 C CE1  . TYR   B 1 45  ? -2.803  17.492  22.824  1   49.051  ? 57  TYR   A CE1  1 ? 2 
ATOM   2439 C CE2  . TYR   B 1 45  ? -3.7    19.652  22.398  1   51.763  ? 57  TYR   A CE2  1 ? 2 
ATOM   2440 C CZ   . TYR   B 1 45  ? -3.205  18.459  21.923  1   49.329  ? 57  TYR   A CZ   1 ? 2 
ATOM   2441 O OH   . TYR   B 1 45  ? -3.06   18.256  20.585  1   53.945  ? 57  TYR   A OH   1 ? 2 
ATOM   2442 H H    . TYR   B 1 45  ? -1.581  21.253  25.712  1   49.489  ? 57  TYR   A H    1 c 2 
ATOM   2443 H HA   . TYR   B 1 45  ? -2.374  19.591  27.783  1   46.035  ? 57  TYR   A HA   1 c 2 
ATOM   2444 H HB2  . TYR   B 1 45  ? -3.831  18.289  26.627  1   43.417  ? 57  TYR   A HB2  1 c 2 
ATOM   2445 H HB3  . TYR   B 1 45  ? -4.304  19.782  26.341  1   44.757  ? 57  TYR   A HB3  1 c 2 
ATOM   2446 H HD1  . TYR   B 1 45  ? -2.695  17.012  24.786  1   43.894  ? 57  TYR   A HD1  1 c 2 
ATOM   2447 H HD2  . TYR   B 1 45  ? -4.17   20.681  24.072  1   50.219  ? 57  TYR   A HD2  1 c 2 
ATOM   2448 H HE1  . TYR   B 1 45  ? -2.479  16.667  22.508  1   47.663  ? 57  TYR   A HE1  1 c 2 
ATOM   2449 H HE2  . TYR   B 1 45  ? -3.952  20.329  21.794  1   52.563  ? 57  TYR   A HE2  1 c 2 
ATOM   2450 H HH   . TYR   B 1 45  ? -2.654  17.506  20.49   0   30      ? 57  TYR   A HH   1 c 2 
ATOM   2451 N N    . LYS   B 1 46  ? -0.9    17.711  27.084  1   47.664  ? 58  LYS   A N    1 ? 2 
ATOM   2452 C CA   . LYS   B 1 46  ? -0.028  16.62   26.677  1   51.683  ? 58  LYS   A CA   1 ? 2 
ATOM   2453 C C    . LYS   B 1 46  ? -0.918  15.384  26.666  1   48.349  ? 58  LYS   A C    1 ? 2 
ATOM   2454 O O    . LYS   B 1 46  ? -1.668  15.168  27.607  1   46.625  ? 58  LYS   A O    1 ? 2 
ATOM   2455 C CB   . LYS   B 1 46  ? 1.17    16.566  27.631  1   55.877  ? 58  LYS   A CB   1 ? 2 
ATOM   2456 C CG   . LYS   B 1 46  ? 1.904   17.906  27.756  1   61.699  ? 58  LYS   A CG   1 ? 2 
ATOM   2457 C CD   . LYS   B 1 46  ? 2.917   18.017  28.887  1   66.906  ? 58  LYS   A CD   1 ? 2 
ATOM   2458 C CE   . LYS   B 1 46  ? 3.505   19.4    29.066  1   68.502  ? 58  LYS   A CE   1 ? 2 
ATOM   2459 N NZ   . LYS   B 1 46  ? 4.653   19.37   29.988  1   74.328  ? 58  LYS   A NZ   1 ? 2 
ATOM   2460 H H    . LYS   B 1 46  ? -1.32   17.644  27.893  1   47.528  ? 58  LYS   A H    1 c 2 
ATOM   2461 H HA   . LYS   B 1 46  ? 0.295   16.795  25.757  1   52.225  ? 58  LYS   A HA   1 c 2 
ATOM   2462 H HB2  . LYS   B 1 46  ? 0.859   16.293  28.521  1   55.117  ? 58  LYS   A HB2  1 c 2 
ATOM   2463 H HB3  . LYS   B 1 46  ? 1.803   15.888  27.312  1   56.972  ? 58  LYS   A HB3  1 c 2 
ATOM   2464 H HG2  . LYS   B 1 46  ? 2.364   18.082  26.906  1   62.915  ? 58  LYS   A HG2  1 c 2 
ATOM   2465 H HG3  . LYS   B 1 46  ? 1.234   18.613  27.873  1   60.826  ? 58  LYS   A HG3  1 c 2 
ATOM   2466 H HD2  . LYS   B 1 46  ? 2.482   17.747  29.725  1   64.727  ? 58  LYS   A HD2  1 c 2 
ATOM   2467 H HD3  . LYS   B 1 46  ? 3.647   17.383  28.716  1   67      ? 58  LYS   A HD3  1 c 2 
ATOM   2468 H HE2  . LYS   B 1 46  ? 3.798   19.747  28.204  1   70.678  ? 58  LYS   A HE2  1 c 2 
ATOM   2469 H HE3  . LYS   B 1 46  ? 2.826   20      29.422  1   68.684  ? 58  LYS   A HE3  1 c 2 
ATOM   2470 H HZ1  . LYS   B 1 46  ? 5.326   18.885  29.624  1   74.401  ? 58  LYS   A HZ1  1 c 2 
ATOM   2471 H HZ2  . LYS   B 1 46  ? 4.406   18.992  30.774  1   72.333  ? 58  LYS   A HZ2  1 c 2 
ATOM   2472 H HZ3  . LYS   B 1 46  ? 4.944   20.214  30.143  1   74.878  ? 58  LYS   A HZ3  1 c 2 
ATOM   2473 N N    . GLY   B 1 47  ? -0.974  14.686  25.53   1   43.816  ? 59  GLY   A N    1 ? 2 
ATOM   2474 C CA   . GLY   B 1 47  ? -1.837  13.533  25.396  1   42.595  ? 59  GLY   A CA   1 ? 2 
ATOM   2475 C C    . GLY   B 1 47  ? -1.03   12.329  24.937  1   45.425  ? 59  GLY   A C    1 ? 2 
ATOM   2476 O O    . GLY   B 1 47  ? 0.058   12.463  24.386  1   46.994  ? 59  GLY   A O    1 ? 2 
ATOM   2477 H H    . GLY   B 1 47  ? -0.456  14.936  24.819  1   46.263  ? 59  GLY   A H    1 c 2 
ATOM   2478 H HA2  . GLY   B 1 47  ? -2.265  13.338  26.26   1   41.922  ? 59  GLY   A HA2  1 c 2 
ATOM   2479 H HA3  . GLY   B 1 47  ? -2.546  13.731  24.739  1   42.487  ? 59  GLY   A HA3  1 c 2 
ATOM   2480 N N    . LYS   B 1 48  ? -1.56   11.137  25.174  1   45.057  ? 60  LYS   A N    1 ? 2 
ATOM   2481 C CA   . LYS   B 1 48  ? -0.92   9.926   24.689  1   46.496  ? 60  LYS   A CA   1 ? 2 
ATOM   2482 C C    . LYS   B 1 48  ? -1.943  8.807   24.715  1   48.246  ? 60  LYS   A C    1 ? 2 
ATOM   2483 O O    . LYS   B 1 48  ? -2.96   8.894   25.426  1   48.62   ? 60  LYS   A O    1 ? 2 
ATOM   2484 C CB   . LYS   B 1 48  ? 0.302   9.52    25.521  1   52.015  ? 60  LYS   A CB   1 ? 2 
ATOM   2485 C CG   . LYS   B 1 48  ? 0.062   9.35    27.018  1   58.649  ? 60  LYS   A CG   1 ? 2 
ATOM   2486 C CD   . LYS   B 1 48  ? 1.233   8.842   27.848  1   65.564  ? 60  LYS   A CD   1 ? 2 
ATOM   2487 C CE   . LYS   B 1 48  ? 1.142   7.365   28.12   1   74.934  ? 60  LYS   A CE   1 ? 2 
ATOM   2488 N NZ   . LYS   B 1 48  ? 2.397   6.73    28.559  1   80.962  ? 60  LYS   A NZ   1 ? 2 
ATOM   2489 H H    . LYS   B 1 48  ? -2.339  11.071  25.648  1   43.682  ? 60  LYS   A H    1 c 2 
ATOM   2490 H HA   . LYS   B 1 48  ? -0.639  10.076  23.752  1   48.724  ? 60  LYS   A HA   1 c 2 
ATOM   2491 H HB2  . LYS   B 1 48  ? 0.649   8.673   25.169  1   54.144  ? 60  LYS   A HB2  1 c 2 
ATOM   2492 H HB3  . LYS   B 1 48  ? 1       10.198  25.398  1   53.413  ? 60  LYS   A HB3  1 c 2 
ATOM   2493 H HG2  . LYS   B 1 48  ? -0.218  10.22   27.379  1   56.517  ? 60  LYS   A HG2  1 c 2 
ATOM   2494 H HG3  . LYS   B 1 48  ? -0.694  8.735   27.138  1   57.119  ? 60  LYS   A HG3  1 c 2 
ATOM   2495 H HD2  . LYS   B 1 48  ? 2.069   9.029   27.369  1   67.627  ? 60  LYS   A HD2  1 c 2 
ATOM   2496 H HD3  . LYS   B 1 48  ? 1.255   9.326   28.702  1   65.631  ? 60  LYS   A HD3  1 c 2 
ATOM   2497 H HE2  . LYS   B 1 48  ? 0.466   7.216   28.806  1   72.471  ? 60  LYS   A HE2  1 c 2 
ATOM   2498 H HE3  . LYS   B 1 48  ? 0.842   6.916   27.312  1   73.492  ? 60  LYS   A HE3  1 c 2 
ATOM   2499 H HZ1  . LYS   B 1 48  ? 2.691   7.128   29.318  1   80.148  ? 60  LYS   A HZ1  1 c 2 
ATOM   2500 H HZ2  . LYS   B 1 48  ? 3.026   6.817   27.914  1   81.33   ? 60  LYS   A HZ2  1 c 2 
ATOM   2501 H HZ3  . LYS   B 1 48  ? 2.254   5.851   28.721  1   81.01   ? 60  LYS   A HZ3  1 c 2 
ATOM   2502 N N    . LEU   B 1 49  ? -1.671  7.764   23.933  1   49.247  ? 61  LEU   A N    1 ? 2 
ATOM   2503 C CA   . LEU   B 1 49  ? -2.319  6.471   24.093  1   50.527  ? 61  LEU   A CA   1 ? 2 
ATOM   2504 C C    . LEU   B 1 49  ? -1.766  5.859   25.381  1   55.009  ? 61  LEU   A C    1 ? 2 
ATOM   2505 O O    . LEU   B 1 49  ? -0.589  6.063   25.685  1   58.166  ? 61  LEU   A O    1 ? 2 
ATOM   2506 C CB   . LEU   B 1 49  ? -1.996  5.558   22.899  1   51.272  ? 61  LEU   A CB   1 ? 2 
ATOM   2507 C CG   . LEU   B 1 49  ? -2.355  6.088   21.508  1   49.783  ? 61  LEU   A CG   1 ? 2 
ATOM   2508 C CD1  . LEU   B 1 49  ? -1.877  5.114   20.395  1   56.68   ? 61  LEU   A CD1  1 ? 2 
ATOM   2509 C CD2  . LEU   B 1 49  ? -3.836  6.322   21.355  1   46.616  ? 61  LEU   A CD2  1 ? 2 
ATOM   2510 H H    . LEU   B 1 49  ? -1.045  7.86    23.274  1   50.847  ? 61  LEU   A H    1 c 2 
ATOM   2511 H HA   . LEU   B 1 49  ? -3.298  6.601   24.169  1   49.357  ? 61  LEU   A HA   1 c 2 
ATOM   2512 H HB2  . LEU   B 1 49  ? -1.03   5.369   22.915  1   52.979  ? 61  LEU   A HB2  1 c 2 
ATOM   2513 H HB3  . LEU   B 1 49  ? -2.464  4.702   23.034  1   51.912  ? 61  LEU   A HB3  1 c 2 
ATOM   2514 H HG   . LEU   B 1 49  ? -1.892  6.955   21.376  1   50.108  ? 61  LEU   A HG   1 c 2 
ATOM   2515 H HD11 . LEU   B 1 49  ? -0.916  4.988   20.463  1   56.997  ? 61  LEU   A HD11 1 c 2 
ATOM   2516 H HD12 . LEU   B 1 49  ? -2.093  5.486   19.523  1   55.85   ? 61  LEU   A HD12 1 c 2 
ATOM   2517 H HD13 . LEU   B 1 49  ? -2.323  4.257   20.499  1   56.226  ? 61  LEU   A HD13 1 c 2 
ATOM   2518 H HD21 . LEU   B 1 49  ? -4.107  7.059   21.924  1   45.382  ? 61  LEU   A HD21 1 c 2 
ATOM   2519 H HD22 . LEU   B 1 49  ? -4.321  5.519   21.611  1   47.407  ? 61  LEU   A HD22 1 c 2 
ATOM   2520 H HD23 . LEU   B 1 49  ? -4.037  6.539   20.429  1   47.725  ? 61  LEU   A HD23 1 c 2 
ATOM   2521 N N    . SER   B 1 50  ? -2.577  5.062   26.084  1   59.171  ? 62  SER   A N    1 ? 2 
ATOM   2522 C CA   . SER   B 1 50  ? -2.105  4.351   27.263  1   66.782  ? 62  SER   A CA   1 ? 2 
ATOM   2523 C C    . SER   B 1 50  ? -0.943  3.404   26.944  1   75.499  ? 62  SER   A C    1 ? 2 
ATOM   2524 O O    . SER   B 1 50  ? -0.056  3.193   27.774  1   81.608  ? 62  SER   A O    1 ? 2 
ATOM   2525 C CB   . SER   B 1 50  ? -3.248  3.621   27.915  1   72.345  ? 62  SER   A CB   1 ? 2 
ATOM   2526 O OG   . SER   B 1 50  ? -4.048  4.541   28.65   1   75.951  ? 62  SER   A OG   1 ? 2 
ATOM   2527 H H    . SER   B 1 50  ? -3.446  4.958   25.821  1   58.676  ? 62  SER   A H    1 c 2 
ATOM   2528 H HA   . SER   B 1 50  ? -1.772  5.028   27.906  1   66.633  ? 62  SER   A HA   1 c 2 
ATOM   2529 H HB2  . SER   B 1 50  ? -3.793  3.188   27.229  1   72.557  ? 62  SER   A HB2  1 c 2 
ATOM   2530 H HB3  . SER   B 1 50  ? -2.899  2.933   28.515  1   73.995  ? 62  SER   A HB3  1 c 2 
ATOM   2531 H HG   . SER   B 1 50  ? -3.794  3.749   29.832  0   30      ? 62  SER   A HG   1 c 2 
ATOM   2532 N N    . ASN   B 1 51  ? -0.922  2.849   25.723  1   71.78   ? 63  ASN   A N    1 ? 2 
ATOM   2533 C CA   . ASN   B 1 51  ? 0.085   1.878   25.337  1   78.244  ? 63  ASN   A CA   1 ? 2 
ATOM   2534 C C    . ASN   B 1 51  ? 1.442   2.543   25.079  1   80.554  ? 63  ASN   A C    1 ? 2 
ATOM   2535 O O    . ASN   B 1 51  ? 2.401   1.837   24.753  1   81.011  ? 63  ASN   A O    1 ? 2 
ATOM   2536 C CB   . ASN   B 1 51  ? -0.386  1.059   24.138  1   79.294  ? 63  ASN   A CB   1 ? 2 
ATOM   2537 C CG   . ASN   B 1 51  ? -0.37   1.836   22.841  1   80.23   ? 63  ASN   A CG   1 ? 2 
ATOM   2538 O OD1  . ASN   B 1 51  ? -0.009  3.024   22.803  1   75.766  ? 63  ASN   A OD1  1 ? 2 
ATOM   2539 N ND2  . ASN   B 1 51  ? -0.777  1.177   21.765  1   80.248  ? 63  ASN   A ND2  1 ? 2 
ATOM   2540 H H    . ASN   B 1 51  ? -1.567  3.077   25.117  1   72.348  ? 63  ASN   A H    1 c 2 
ATOM   2541 H HA   . ASN   B 1 51  ? 0.197   1.249   26.086  1   79.151  ? 63  ASN   A HA   1 c 2 
ATOM   2542 H HB2  . ASN   B 1 51  ? 0.188   0.273   24.044  1   82.721  ? 63  ASN   A HB2  1 c 2 
ATOM   2543 H HB3  . ASN   B 1 51  ? -1.297  0.745   24.307  1   79.096  ? 63  ASN   A HB3  1 c 2 
ATOM   2544 H HD21 . ASN   B 1 51  ? -0.7    1.55    20.963  1   80.883  ? 63  ASN   A HD21 1 c 2 
ATOM   2545 H HD22 . ASN   B 1 51  ? -1.126  0.365   21.846  1   82.087  ? 63  ASN   A HD22 1 c 2 
ATOM   2546 N N    . GLY   B 1 52  ? 1.508   3.884   25.169  1   79.155  ? 64  GLY   A N    1 ? 2 
ATOM   2547 C CA   . GLY   B 1 52  ? 2.756   4.636   25.083  1   80.446  ? 64  GLY   A CA   1 ? 2 
ATOM   2548 C C    . GLY   B 1 52  ? 3.383   4.656   23.681  1   83.331  ? 64  GLY   A C    1 ? 2 
ATOM   2549 O O    . GLY   B 1 52  ? 4.59    4.889   23.554  1   85.794  ? 64  GLY   A O    1 ? 2 
ATOM   2550 H H    . GLY   B 1 52  ? 0.733   4.356   25.266  1   76.462  ? 64  GLY   A H    1 c 2 
ATOM   2551 H HA2  . GLY   B 1 52  ? 2.584   5.564   25.37   1   78.603  ? 64  GLY   A HA2  1 c 2 
ATOM   2552 H HA3  . GLY   B 1 52  ? 3.402   4.245   25.718  1   82.336  ? 64  GLY   A HA3  1 c 2 
ATOM   2553 N N    . LYS   B 1 53  ? 2.575   4.457   22.622  1   79.378  ? 65  LYS   A N    1 ? 2 
ATOM   2554 C CA   . LYS   B 1 53  ? 3.118   4.363   21.263  1   80.456  ? 65  LYS   A CA   1 ? 2 
ATOM   2555 C C    . LYS   B 1 53  ? 2.943   5.678   20.483  1   78.281  ? 65  LYS   A C    1 ? 2 
ATOM   2556 O O    . LYS   B 1 53  ? 3.607   5.872   19.472  1   78.266  ? 65  LYS   A O    1 ? 2 
ATOM   2557 C CB   . LYS   B 1 53  ? 2.555   3.134   20.532  1   74.798  ? 65  LYS   A CB   1 ? 2 
ATOM   2558 H H    . LYS   B 1 53  ? 1.673   4.38    22.746  1   78.026  ? 65  LYS   A H    1 c 2 
ATOM   2559 H HA   . LYS   B 1 53  ? 4.092   4.203   21.343  1   81.52   ? 65  LYS   A HA   1 c 2 
ATOM   2560 H HB2  . LYS   B 1 53  ? 3.545   2.647   20.305  0   30      ? 65  LYS   A HB2  1 c 2 
ATOM   2561 H HB3  . LYS   B 1 53  ? 1.773   3.141   20.573  0   30      ? 65  LYS   A HB3  1 c 2 
ATOM   2562 N N    . LYS   B 1 54  ? 2.079   6.598   20.956  1   78.176  ? 66  LYS   A N    1 ? 2 
ATOM   2563 C CA   . LYS   B 1 54  ? 1.957   7.938   20.387  1   74.881  ? 66  LYS   A CA   1 ? 2 
ATOM   2564 C C    . LYS   B 1 54  ? 1.807   8.956   21.524  1   70.666  ? 66  LYS   A C    1 ? 2 
ATOM   2565 O O    . LYS   B 1 54  ? 1.168   8.671   22.54   1   68.309  ? 66  LYS   A O    1 ? 2 
ATOM   2566 C CB   . LYS   B 1 54  ? 0.791   8.045   19.386  1   71.941  ? 66  LYS   A CB   1 ? 2 
ATOM   2567 H H    . LYS   B 1 54  ? 1.537   6.376   21.657  1   75.297  ? 66  LYS   A H    1 c 2 
ATOM   2568 H HA   . LYS   B 1 54  ? 2.795   8.142   19.9    1   76.577  ? 66  LYS   A HA   1 c 2 
ATOM   2569 H HB2  . LYS   B 1 54  ? 1.069   8.025   18.462  0   30      ? 66  LYS   A HB2  1 c 2 
ATOM   2570 H HB3  . LYS   B 1 54  ? -0.087  7.97    19.916  0   30      ? 66  LYS   A HB3  1 c 2 
ATOM   2571 N N    . PHE   B 1 55  ? 2.386   10.149  21.301  1   64.899  ? 67  PHE   A N    1 ? 2 
ATOM   2572 C CA   . PHE   B 1 55  ? 2.297   11.318  22.165  1   65.384  ? 67  PHE   A CA   1 ? 2 
ATOM   2573 C C    . PHE   B 1 55  ? 2.012   12.547  21.321  1   63.687  ? 67  PHE   A C    1 ? 2 
ATOM   2574 O O    . PHE   B 1 55  ? 2.477   12.659  20.197  1   74.369  ? 67  PHE   A O    1 ? 2 
ATOM   2575 C CB   . PHE   B 1 55  ? 3.607   11.658  22.876  1   64.453  ? 67  PHE   A CB   1 ? 2 
ATOM   2576 C CG   . PHE   B 1 55  ? 4.129   10.407  23.552  1   69.692  ? 67  PHE   A CG   1 ? 2 
ATOM   2577 C CD1  . PHE   B 1 55  ? 4.795   9.441   22.809  1   71.342  ? 67  PHE   A CD1  1 ? 2 
ATOM   2578 C CD2  . PHE   B 1 55  ? 3.889   10.163  24.906  1   72.629  ? 67  PHE   A CD2  1 ? 2 
ATOM   2579 C CE1  . PHE   B 1 55  ? 5.255   8.282   23.417  1   76.398  ? 67  PHE   A CE1  1 ? 2 
ATOM   2580 C CE2  . PHE   B 1 55  ? 4.347   8.992   25.504  1   72.766  ? 67  PHE   A CE2  1 ? 2 
ATOM   2581 C CZ   . PHE   B 1 55  ? 5.016   8.051   24.757  1   71.708  ? 67  PHE   A CZ   1 ? 2 
ATOM   2582 H H    . PHE   B 1 55  ? 2.883   10.233  20.539  1   68.745  ? 67  PHE   A H    1 c 2 
ATOM   2583 H HA   . PHE   B 1 55  ? 1.574   11.19   22.832  1   62.048  ? 67  PHE   A HA   1 c 2 
ATOM   2584 H HB2  . PHE   B 1 55  ? 4.264   11.977  22.218  1   67.992  ? 67  PHE   A HB2  1 c 2 
ATOM   2585 H HB3  . PHE   B 1 55  ? 3.443   12.356  23.548  1   64.849  ? 67  PHE   A HB3  1 c 2 
ATOM   2586 H HD1  . PHE   B 1 55  ? 4.957   9.587   21.891  1   73.56   ? 67  PHE   A HD1  1 c 2 
ATOM   2587 H HD2  . PHE   B 1 55  ? 3.422   10.802  25.421  1   69.459  ? 67  PHE   A HD2  1 c 2 
ATOM   2588 H HE1  . PHE   B 1 55  ? 5.717   7.638   22.905  1   77.03   ? 67  PHE   A HE1  1 c 2 
ATOM   2589 H HE2  . PHE   B 1 55  ? 4.192   8.842   26.422  1   71.443  ? 67  PHE   A HE2  1 c 2 
ATOM   2590 H HZ   . PHE   B 1 55  ? 5.337   7.263   25.167  1   74.829  ? 67  PHE   A HZ   1 c 2 
ATOM   2591 N N    . ASP   B 1 56  ? 1.27    13.481  21.881  1   55.693  ? 68  ASP   A N    1 ? 2 
ATOM   2592 C CA   . ASP   B 1 56  ? 0.868   14.666  21.156  1   56.532  ? 68  ASP   A CA   1 ? 2 
ATOM   2593 C C    . ASP   B 1 56  ? 0.769   15.786  22.182  1   54.661  ? 68  ASP   A C    1 ? 2 
ATOM   2594 O O    . ASP   B 1 56  ? 0.124   15.606  23.195  1   45.95   ? 68  ASP   A O    1 ? 2 
ATOM   2595 C CB   . ASP   B 1 56  ? -0.47   14.486  20.444  1   52.802  ? 68  ASP   A CB   1 ? 2 
ATOM   2596 C CG   . ASP   B 1 56  ? -1.029  15.756  19.805  1   58.102  ? 68  ASP   A CG   1 ? 2 
ATOM   2597 O OD1  . ASP   B 1 56  ? -0.285  16.413  19.026  1   66.646  ? 68  ASP   A OD1  1 ? 2 
ATOM   2598 O OD2  . ASP   B 1 56  ? -2.184  16.129  20.107  1   58.109  ? 68  ASP   A OD2  1 ? 2 
ATOM   2599 H H    . ASP   B 1 56  ? 1       13.381  22.749  1   55.814  ? 68  ASP   A H    1 c 2 
ATOM   2600 H HA   . ASP   B 1 56  ? 1.563   14.892  20.498  1   58.032  ? 68  ASP   A HA   1 c 2 
ATOM   2601 H HB2  . ASP   B 1 56  ? -0.365  13.811  19.742  1   55.366  ? 68  ASP   A HB2  1 c 2 
ATOM   2602 H HB3  . ASP   B 1 56  ? -1.128  14.151  21.089  1   52.562  ? 68  ASP   A HB3  1 c 2 
ATOM   2603 N N    . SER   B 1 57  ? 1.379   16.933  21.911  1   56.283  ? 69  SER   A N    1 ? 2 
ATOM   2604 C CA   . SER   B 1 57  ? 1.277   18.046  22.841  1   61.786  ? 69  SER   A CA   1 ? 2 
ATOM   2605 C C    . SER   B 1 57  ? 0.939   19.323  22.079  1   62.728  ? 69  SER   A C    1 ? 2 
ATOM   2606 O O    . SER   B 1 57  ? 1.395   19.519  20.951  1   67.034  ? 69  SER   A O    1 ? 2 
ATOM   2607 C CB   . SER   B 1 57  ? 2.545   18.217  23.643  1   64.111  ? 69  SER   A CB   1 ? 2 
ATOM   2608 O OG   . SER   B 1 57  ? 2.488   19.432  24.379  1   69.162  ? 69  SER   A OG   1 ? 2 
ATOM   2609 H H    . SER   B 1 57  ? 1.863   17.031  21.142  1   59.539  ? 69  SER   A H    1 c 2 
ATOM   2610 H HA   . SER   B 1 57  ? 0.536   17.858  23.469  1   58.365  ? 69  SER   A HA   1 c 2 
ATOM   2611 H HB2  . SER   B 1 57  ? 2.647   17.466  24.257  1   64.049  ? 69  SER   A HB2  1 c 2 
ATOM   2612 H HB3  . SER   B 1 57  ? 3.312   18.234  23.04   1   67.154  ? 69  SER   A HB3  1 c 2 
ATOM   2613 H HG   . SER   B 1 57  ? 3.266   19.568  24.798  0   30      ? 69  SER   A HG   1 c 2 
ATOM   2614 N N    . SER   B 1 58  ? 0.158   20.197  22.711  1   58.339  ? 70  SER   A N    1 ? 2 
ATOM   2615 C CA   . SER   B 1 58  ? -0.079  21.51   22.144  1   62.142  ? 70  SER   A CA   1 ? 2 
ATOM   2616 C C    . SER   B 1 58  ? 1.269   22.19   21.894  1   69.767  ? 70  SER   A C    1 ? 2 
ATOM   2617 O O    . SER   B 1 58  ? 1.47    22.804  20.844  1   78.901  ? 70  SER   A O    1 ? 2 
ATOM   2618 C CB   . SER   B 1 58  ? -0.965  22.323  23.044  1   60.736  ? 70  SER   A CB   1 ? 2 
ATOM   2619 O OG   . SER   B 1 58  ? -0.484  22.298  24.38   1   59.466  ? 70  SER   A OG   1 ? 2 
ATOM   2620 H H    . SER   B 1 58  ? -0.234  19.975  23.507  1   57.837  ? 70  SER   A H    1 c 2 
ATOM   2621 H HA   . SER   B 1 58  ? -0.536  21.393  21.272  1   62.678  ? 70  SER   A HA   1 c 2 
ATOM   2622 H HB2  . SER   B 1 58  ? -0.992  23.245  22.725  1   62.703  ? 70  SER   A HB2  1 c 2 
ATOM   2623 H HB3  . SER   B 1 58  ? -1.871  21.963  23.018  1   58.958  ? 70  SER   A HB3  1 c 2 
ATOM   2624 H HG   . SER   B 1 58  ? -0.975  22.725  24.874  0   30      ? 70  SER   A HG   1 c 2 
ATOM   2625 N N    . HIS   B 1 59  ? 2.201   22.011  22.848  1   68.449  ? 71  HIS   A N    1 ? 2 
ATOM   2626 C CA   . HIS   B 1 59  ? 3.511   22.642  22.824  1   73.028  ? 71  HIS   A CA   1 ? 2 
ATOM   2627 C C    . HIS   B 1 59  ? 4.302   22.276  21.57   1   76.398  ? 71  HIS   A C    1 ? 2 
ATOM   2628 O O    . HIS   B 1 59  ? 5.115   23.073  21.115  1   74.752  ? 71  HIS   A O    1 ? 2 
ATOM   2629 C CB   . HIS   B 1 59  ? 4.305   22.281  24.087  1   72.467  ? 71  HIS   A CB   1 ? 2 
ATOM   2630 C CG   . HIS   B 1 59  ? 3.686   22.791  25.352  1   71.339  ? 71  HIS   A CG   1 ? 2 
ATOM   2631 N ND1  . HIS   B 1 59  ? 3.676   24.121  25.721  1   75.205  ? 71  HIS   A ND1  1 ? 2 
ATOM   2632 C CD2  . HIS   B 1 59  ? 3.071   22.125  26.336  1   67.941  ? 71  HIS   A CD2  1 ? 2 
ATOM   2633 C CE1  . HIS   B 1 59  ? 3.06    24.243  26.887  1   75.14   ? 71  HIS   A CE1  1 ? 2 
ATOM   2634 N NE2  . HIS   B 1 59  ? 2.683   23.034  27.276  1   68.731  ? 71  HIS   A NE2  1 ? 2 
ATOM   2635 H H    . HIS   B 1 59  ? 1.999   21.471  23.557  1   66.994  ? 71  HIS   A H    1 c 2 
ATOM   2636 H HA   . HIS   B 1 59  ? 3.367   23.62   22.819  1   74.446  ? 71  HIS   A HA   1 c 2 
ATOM   2637 H HB2  . HIS   B 1 59  ? 4.383   21.304  24.142  1   71.259  ? 71  HIS   A HB2  1 c 2 
ATOM   2638 H HB3  . HIS   B 1 59  ? 5.211   22.651  24.006  1   75.443  ? 71  HIS   A HB3  1 c 2 
ATOM   2639 H HD1  . HIS   B 1 59  ? 4.181   24.781  25.287  0   30      ? 71  HIS   A HD1  1 c 2 
ATOM   2640 H HD2  . HIS   B 1 59  ? 2.92    21.201  26.376  1   66.454  ? 71  HIS   A HD2  1 c 2 
ATOM   2641 H HE1  . HIS   B 1 59  ? 2.917   25.047  27.356  1   75.101  ? 71  HIS   A HE1  1 c 2 
ATOM   2642 H HE2  . HIS   B 1 59  ? 2.176   22.908  27.927  0   30      ? 71  HIS   A HE2  1 c 2 
ATOM   2643 N N    . ASP   B 1 60  ? 4.067   21.075  21.026  1   79.693  ? 72  ASP   A N    1 ? 2 
ATOM   2644 C CA   . ASP   B 1 60  ? 4.639   20.638  19.755  1   86.812  ? 72  ASP   A CA   1 ? 2 
ATOM   2645 C C    . ASP   B 1 60  ? 4.401   21.658  18.641  1   89.271  ? 72  ASP   A C    1 ? 2 
ATOM   2646 O O    . ASP   B 1 60  ? 5.166   21.695  17.684  1   96.069  ? 72  ASP   A O    1 ? 2 
ATOM   2647 C CB   . ASP   B 1 60  ? 4.013   19.338  19.257  1   82.169  ? 72  ASP   A CB   1 ? 2 
ATOM   2648 C CG   . ASP   B 1 60  ? 4.289   18.091  20.077  1   77.689  ? 72  ASP   A CG   1 ? 2 
ATOM   2649 O OD1  . ASP   B 1 60  ? 5.352   18.038  20.73   1   81.129  ? 72  ASP   A OD1  1 ? 2 
ATOM   2650 O OD2  . ASP   B 1 60  ? 3.433   17.195  20.058  1   69.116  ? 72  ASP   A OD2  1 ? 2 
ATOM   2651 H H    . ASP   B 1 60  ? 3.531   20.49   21.479  1   76.723  ? 72  ASP   A H    1 c 2 
ATOM   2652 H HA   . ASP   B 1 60  ? 5.607   20.51   19.872  1   87.298  ? 72  ASP   A HA   1 c 2 
ATOM   2653 H HB2  . ASP   B 1 60  ? 3.044   19.46   19.195  1   80.188  ? 72  ASP   A HB2  1 c 2 
ATOM   2654 H HB3  . ASP   B 1 60  ? 4.344   19.168  18.35   1   84.056  ? 72  ASP   A HB3  1 c 2 
ATOM   2655 N N    . ARG   B 1 61  ? 3.305   22.423  18.739  1   88.142  ? 73  ARG   A N    1 ? 2 
ATOM   2656 C CA   . ARG   B 1 61  ? 2.945   23.409  17.736  1   90.806  ? 73  ARG   A CA   1 ? 2 
ATOM   2657 C C    . ARG   B 1 61  ? 3.254   24.828  18.226  1   95.973  ? 73  ARG   A C    1 ? 2 
ATOM   2658 O O    . ARG   B 1 61  ? 2.879   25.796  17.566  1   99.04   ? 73  ARG   A O    1 ? 2 
ATOM   2659 C CB   . ARG   B 1 61  ? 1.455   23.23   17.422  1   89.757  ? 73  ARG   A CB   1 ? 2 
ATOM   2660 C CG   . ARG   B 1 61  ? 1.083   21.925  16.732  1   87.1    ? 73  ARG   A CG   1 ? 2 
ATOM   2661 C CD   . ARG   B 1 61  ? -0.404  21.898  16.365  1   83.456  ? 73  ARG   A CD   1 ? 2 
ATOM   2662 N NE   . ARG   B 1 61  ? -1.31   21.863  17.524  1   82.643  ? 73  ARG   A NE   1 ? 2 
ATOM   2663 C CZ   . ARG   B 1 61  ? -1.526  20.826  18.352  1   75.116  ? 73  ARG   A CZ   1 ? 2 
ATOM   2664 N NH1  . ARG   B 1 61  ? -0.784  19.724  18.281  1   76.407  ? 73  ARG   A NH1  1 ? 2 
ATOM   2665 N NH2  . ARG   B 1 61  ? -2.493  20.885  19.256  1   67.642  ? 73  ARG   A NH2  1 ? 2 
ATOM   2666 H H    . ARG   B 1 61  ? 2.744   22.307  19.451  1   85.468  ? 73  ARG   A H    1 c 2 
ATOM   2667 H HA   . ARG   B 1 61  ? 3.47    23.234  16.914  1   93.819  ? 73  ARG   A HA   1 c 2 
ATOM   2668 H HB2  . ARG   B 1 61  ? 0.951   23.293  18.261  1   86.931  ? 73  ARG   A HB2  1 c 2 
ATOM   2669 H HB3  . ARG   B 1 61  ? 1.169   23.974  16.851  1   91.334  ? 73  ARG   A HB3  1 c 2 
ATOM   2670 H HG2  . ARG   B 1 61  ? 1.619   21.823  15.915  1   89.225  ? 73  ARG   A HG2  1 c 2 
ATOM   2671 H HG3  . ARG   B 1 61  ? 1.284   21.171  17.329  1   84.789  ? 73  ARG   A HG3  1 c 2 
ATOM   2672 H HD2  . ARG   B 1 61  ? -0.607  22.691  15.827  1   86.791  ? 73  ARG   A HD2  1 c 2 
ATOM   2673 H HD3  . ARG   B 1 61  ? -0.572  21.112  15.806  1   84.132  ? 73  ARG   A HD3  1 c 2 
ATOM   2674 H HE   . ARG   B 1 61  ? -1.755  22.593  17.696  1   81.33   ? 73  ARG   A HE   1 c 2 
ATOM   2675 H HH11 . ARG   B 1 61  ? -0.313  19.547  17.555  1   77.607  ? 73  ARG   A HH11 1 c 2 
ATOM   2676 H HH12 . ARG   B 1 61  ? -0.768  19.164  18.967  1   73.977  ? 73  ARG   A HH12 1 c 2 
ATOM   2677 H HH21 . ARG   B 1 61  ? -2.775  21.671  19.549  1   69.637  ? 73  ARG   A HH21 1 c 2 
ATOM   2678 H HH22 . ARG   B 1 61  ? -2.854  20.139  19.563  1   67.162  ? 73  ARG   A HH22 1 c 2 
ATOM   2679 N N    . ASN   B 1 62  ? 3.942   24.955  19.374  1   91.86   ? 74  ASN   A N    1 ? 2 
ATOM   2680 C CA   . ASN   B 1 62  ? 4.202   26.235  20.02   1   92.572  ? 74  ASN   A CA   1 ? 2 
ATOM   2681 C C    . ASN   B 1 62  ? 2.974   27.153  19.922  1   91.366  ? 74  ASN   A C    1 ? 2 
ATOM   2682 O O    . ASN   B 1 62  ? 3.107   28.318  19.552  1   94.698  ? 74  ASN   A O    1 ? 2 
ATOM   2683 C CB   . ASN   B 1 62  ? 5.489   26.873  19.481  1   93.929  ? 74  ASN   A CB   1 ? 2 
ATOM   2684 H H    . ASN   B 1 62  ? 4.278   24.204  19.767  1   90.768  ? 74  ASN   A H    1 c 2 
ATOM   2685 H HA   . ASN   B 1 62  ? 4.355   26.054  20.975  1   90.418  ? 74  ASN   A HA   1 c 2 
ATOM   2686 H HB2  . ASN   B 1 62  ? 6.25    26.28   20.021  0   30      ? 74  ASN   A HB2  1 c 2 
ATOM   2687 H HB3  . ASN   B 1 62  ? 5.316   27.551  19.058  0   30      ? 74  ASN   A HB3  1 c 2 
ATOM   2688 N N    . GLU   B 1 63  ? 1.778   26.645  20.265  1   85.379  ? 75  GLU   A N    1 ? 2 
ATOM   2689 C CA   . GLU   B 1 63  ? 0.586   27.489  20.323  1   87.333  ? 75  GLU   A CA   1 ? 2 
ATOM   2690 C C    . GLU   B 1 63  ? -0.501  26.817  21.162  1   82.274  ? 75  GLU   A C    1 ? 2 
ATOM   2691 O O    . GLU   B 1 63  ? -0.643  25.598  21.108  1   80.705  ? 75  GLU   A O    1 ? 2 
ATOM   2692 C CB   . GLU   B 1 63  ? 0.03    27.833  18.937  1   87.7    ? 75  GLU   A CB   1 ? 2 
ATOM   2693 H H    . GLU   B 1 63  ? 1.703   25.757  20.47   1   83.671  ? 75  GLU   A H    1 c 2 
ATOM   2694 H HA   . GLU   B 1 63  ? 0.84    28.337  20.763  1   88.659  ? 75  GLU   A HA   1 c 2 
ATOM   2695 H HB2  . GLU   B 1 63  ? 0.782   27.743  18.193  0   30      ? 75  GLU   A HB2  1 c 2 
ATOM   2696 H HB3  . GLU   B 1 63  ? -0.951  27.644  18.85   0   30      ? 75  GLU   A HB3  1 c 2 
ATOM   2697 N N    . PRO   B 1 64  ? -1.3    27.575  21.959  1   80.76   ? 76  PRO   A N    1 ? 2 
ATOM   2698 C CA   . PRO   B 1 64  ? -2.403  26.974  22.702  1   74.899  ? 76  PRO   A CA   1 ? 2 
ATOM   2699 C C    . PRO   B 1 64  ? -3.417  26.316  21.78   1   73.435  ? 76  PRO   A C    1 ? 2 
ATOM   2700 O O    . PRO   B 1 64  ? -3.553  26.716  20.624  1   75.992  ? 76  PRO   A O    1 ? 2 
ATOM   2701 C CB   . PRO   B 1 64  ? -3.067  28.117  23.451  1   77.742  ? 76  PRO   A CB   1 ? 2 
ATOM   2702 C CG   . PRO   B 1 64  ? -2.071  29.261  23.385  1   84.69   ? 76  PRO   A CG   1 ? 2 
ATOM   2703 C CD   . PRO   B 1 64  ? -1.183  29.027  22.178  1   86.576  ? 76  PRO   A CD   1 ? 2 
ATOM   2704 H HA   . PRO   B 1 64  ? -2.052  26.315  23.337  1   73.516  ? 76  PRO   A HA   1 c 2 
ATOM   2705 H HB2  . PRO   B 1 64  ? -3.91   28.369  23.026  1   78.419  ? 76  PRO   A HB2  1 c 2 
ATOM   2706 H HB3  . PRO   B 1 64  ? -3.246  27.867  24.378  1   76.155  ? 76  PRO   A HB3  1 c 2 
ATOM   2707 H HG2  . PRO   B 1 64  ? -2.539  30.115  23.297  1   86.385  ? 76  PRO   A HG2  1 c 2 
ATOM   2708 H HG3  . PRO   B 1 64  ? -1.531  29.289  24.199  1   83.987  ? 76  PRO   A HG3  1 c 2 
ATOM   2709 H HD2  . PRO   B 1 64  ? -1.5    29.522  21.398  1   88.308  ? 76  PRO   A HD2  1 c 2 
ATOM   2710 H HD3  . PRO   B 1 64  ? -0.258  29.277  22.366  1   87.904  ? 76  PRO   A HD3  1 c 2 
ATOM   2711 N N    . PHE   B 1 65  ? -4.114  25.309  22.317  1   69.977  ? 77  PHE   A N    1 ? 2 
ATOM   2712 C CA   . PHE   B 1 65  ? -5.219  24.666  21.638  1   65.469  ? 77  PHE   A CA   1 ? 2 
ATOM   2713 C C    . PHE   B 1 65  ? -6.529  25.333  22.061  1   66.828  ? 77  PHE   A C    1 ? 2 
ATOM   2714 O O    . PHE   B 1 65  ? -6.818  25.462  23.246  1   62.207  ? 77  PHE   A O    1 ? 2 
ATOM   2715 C CB   . PHE   B 1 65  ? -5.179  23.184  21.985  1   62.337  ? 77  PHE   A CB   1 ? 2 
ATOM   2716 C CG   . PHE   B 1 65  ? -6.266  22.376  21.296  1   61.173  ? 77  PHE   A CG   1 ? 2 
ATOM   2717 C CD1  . PHE   B 1 65  ? -6.055  21.857  20.027  1   64.663  ? 77  PHE   A CD1  1 ? 2 
ATOM   2718 C CD2  . PHE   B 1 65  ? -7.479  22.116  21.924  1   59.454  ? 77  PHE   A CD2  1 ? 2 
ATOM   2719 C CE1  . PHE   B 1 65  ? -7.031  21.1    19.397  1   61.114  ? 77  PHE   A CE1  1 ? 2 
ATOM   2720 C CE2  . PHE   B 1 65  ? -8.453  21.365  21.282  1   58.4    ? 77  PHE   A CE2  1 ? 2 
ATOM   2721 C CZ   . PHE   B 1 65  ? -8.215  20.847  20.028  1   57.824  ? 77  PHE   A CZ   1 ? 2 
ATOM   2722 H H    . PHE   B 1 65  ? -3.886  25.013  23.151  1   67.706  ? 77  PHE   A H    1 c 2 
ATOM   2723 H HA   . PHE   B 1 65  ? -5.1    24.769  20.657  1   68.021  ? 77  PHE   A HA   1 c 2 
ATOM   2724 H HB2  . PHE   B 1 65  ? -4.301  22.825  21.728  1   62.557  ? 77  PHE   A HB2  1 c 2 
ATOM   2725 H HB3  . PHE   B 1 65  ? -5.276  23.087  22.958  1   60.879  ? 77  PHE   A HB3  1 c 2 
ATOM   2726 H HD1  . PHE   B 1 65  ? -5.232  22.016  19.591  1   64.763  ? 77  PHE   A HD1  1 c 2 
ATOM   2727 H HD2  . PHE   B 1 65  ? -7.641  22.458  22.789  1   58.866  ? 77  PHE   A HD2  1 c 2 
ATOM   2728 H HE1  . PHE   B 1 65  ? -6.873  20.754  18.533  1   62.321  ? 77  PHE   A HE1  1 c 2 
ATOM   2729 H HE2  . PHE   B 1 65  ? -9.274  21.192  21.716  1   57.25   ? 77  PHE   A HE2  1 c 2 
ATOM   2730 H HZ   . PHE   B 1 65  ? -8.884  20.344  19.591  1   58.469  ? 77  PHE   A HZ   1 c 2 
ATOM   2731 N N    . VAL   B 1 66  ? -7.307  25.762  21.063  1   68.765  ? 78  VAL   A N    1 ? 2 
ATOM   2732 C CA   . VAL   B 1 66  ? -8.556  26.46   21.289  1   73.268  ? 78  VAL   A CA   1 ? 2 
ATOM   2733 C C    . VAL   B 1 66  ? -9.689  25.636  20.689  1   71.738  ? 78  VAL   A C    1 ? 2 
ATOM   2734 O O    . VAL   B 1 66  ? -9.527  25.039  19.63   1   73.412  ? 78  VAL   A O    1 ? 2 
ATOM   2735 C CB   . VAL   B 1 66  ? -8.489  27.862  20.655  1   78.572  ? 78  VAL   A CB   1 ? 2 
ATOM   2736 C CG1  . VAL   B 1 66  ? -9.753  28.663  20.949  1   79.24   ? 78  VAL   A CG1  1 ? 2 
ATOM   2737 C CG2  . VAL   B 1 66  ? -7.237  28.623  21.09   1   81.467  ? 78  VAL   A CG2  1 ? 2 
ATOM   2738 H H    . VAL   B 1 66  ? -7.045  25.609  20.201  1   70.503  ? 78  VAL   A H    1 c 2 
ATOM   2739 H HA   . VAL   B 1 66  ? -8.699  26.552  22.247  1   71.476  ? 78  VAL   A HA   1 c 2 
ATOM   2740 H HB   . VAL   B 1 66  ? -8.437  27.735  19.679  1   79.62   ? 78  VAL   A HB   1 c 2 
ATOM   2741 H HG11 . VAL   B 1 66  ? -9.914  28.677  21.907  1   78.309  ? 78  VAL   A HG11 1 c 2 
ATOM   2742 H HG12 . VAL   B 1 66  ? -10.511 28.253  20.5    1   79.232  ? 78  VAL   A HG12 1 c 2 
ATOM   2743 H HG13 . VAL   B 1 66  ? -9.642  29.573  20.626  1   82.911  ? 78  VAL   A HG13 1 c 2 
ATOM   2744 H HG21 . VAL   B 1 66  ? -7.274  29.532  20.746  1   84.404  ? 78  VAL   A HG21 1 c 2 
ATOM   2745 H HG22 . VAL   B 1 66  ? -6.447  28.179  20.739  1   80.587  ? 78  VAL   A HG22 1 c 2 
ATOM   2746 H HG23 . VAL   B 1 66  ? -7.191  28.646  22.06   1   79.824  ? 78  VAL   A HG23 1 c 2 
ATOM   2747 N N    . PHE   B 1 67  ? -10.833 25.605  21.378  1   69.582  ? 79  PHE   A N    1 ? 2 
ATOM   2748 C CA   . PHE   B 1 67  ? -12.023 24.942  20.873  1   64.994  ? 79  PHE   A CA   1 ? 2 
ATOM   2749 C C    . PHE   B 1 67  ? -13.252 25.5    21.602  1   68.752  ? 79  PHE   A C    1 ? 2 
ATOM   2750 O O    . PHE   B 1 67  ? -13.115 26.154  22.65   1   67.554  ? 79  PHE   A O    1 ? 2 
ATOM   2751 C CB   . PHE   B 1 67  ? -11.872 23.428  21.055  1   58.879  ? 79  PHE   A CB   1 ? 2 
ATOM   2752 C CG   . PHE   B 1 67  ? -12.066 22.943  22.486  1   56.057  ? 79  PHE   A CG   1 ? 2 
ATOM   2753 C CD1  . PHE   B 1 67  ? -11.04  23.056  23.425  1   55.344  ? 79  PHE   A CD1  1 ? 2 
ATOM   2754 C CD2  . PHE   B 1 67  ? -13.268 22.389  22.904  1   54.742  ? 79  PHE   A CD2  1 ? 2 
ATOM   2755 C CE1  . PHE   B 1 67  ? -11.227 22.646  24.732  1   50.513  ? 79  PHE   A CE1  1 ? 2 
ATOM   2756 C CE2  . PHE   B 1 67  ? -13.442 21.989  24.22   1   51.954  ? 79  PHE   A CE2  1 ? 2 
ATOM   2757 C CZ   . PHE   B 1 67  ? -12.428 22.128  25.128  1   51.22   ? 79  PHE   A CZ   1 ? 2 
ATOM   2758 H H    . PHE   B 1 67  ? -10.871 26.012  22.196  1   68.823  ? 79  PHE   A H    1 c 2 
ATOM   2759 H HA   . PHE   B 1 67  ? -12.111 25.139  19.903  1   67.835  ? 79  PHE   A HA   1 c 2 
ATOM   2760 H HB2  . PHE   B 1 67  ? -12.529 22.98   20.477  1   59.713  ? 79  PHE   A HB2  1 c 2 
ATOM   2761 H HB3  . PHE   B 1 67  ? -10.977 23.163  20.75   1   59.057  ? 79  PHE   A HB3  1 c 2 
ATOM   2762 H HD1  . PHE   B 1 67  ? -10.215 23.436  23.168  1   55.344  ? 79  PHE   A HD1  1 c 2 
ATOM   2763 H HD2  . PHE   B 1 67  ? -13.983 22.312  22.293  1   55.77   ? 79  PHE   A HD2  1 c 2 
ATOM   2764 H HE1  . PHE   B 1 67  ? -10.524 22.734  25.356  1   50.96   ? 79  PHE   A HE1  1 c 2 
ATOM   2765 H HE2  . PHE   B 1 67  ? -14.267 21.617  24.491  1   51.994  ? 79  PHE   A HE2  1 c 2 
ATOM   2766 H HZ   . PHE   B 1 67  ? -12.543 21.827  26.015  1   49.666  ? 79  PHE   A HZ   1 c 2 
ATOM   2767 N N    . SER   B 1 68  ? -14.442 25.21   21.049  1   65.325  ? 80  SER   A N    1 ? 2 
ATOM   2768 C CA   . SER   B 1 68  ? -15.698 25.678  21.618  1   67.173  ? 80  SER   A CA   1 ? 2 
ATOM   2769 C C    . SER   B 1 68  ? -16.339 24.564  22.432  1   62.217  ? 80  SER   A C    1 ? 2 
ATOM   2770 O O    . SER   B 1 68  ? -16.602 23.487  21.903  1   62.222  ? 80  SER   A O    1 ? 2 
ATOM   2771 C CB   . SER   B 1 68  ? -16.64  26.168  20.543  1   72.564  ? 80  SER   A CB   1 ? 2 
ATOM   2772 O OG   . SER   B 1 68  ? -16.418 27.542  20.263  1   76.907  ? 80  SER   A OG   1 ? 2 
ATOM   2773 H H    . SER   B 1 68  ? -14.467 24.7    20.292  1   66.389  ? 80  SER   A H    1 c 2 
ATOM   2774 H HA   . SER   B 1 68  ? -15.5   26.434  22.224  1   67.908  ? 80  SER   A HA   1 c 2 
ATOM   2775 H HB2  . SER   B 1 68  ? -16.505 25.645  19.73   1   72.131  ? 80  SER   A HB2  1 c 2 
ATOM   2776 H HB3  . SER   B 1 68  ? -17.562 26.042  20.837  1   72.764  ? 80  SER   A HB3  1 c 2 
ATOM   2777 H HG   . SER   B 1 68  ? -17     27.902  19.873  0   30      ? 80  SER   A HG   1 c 2 
ATOM   2778 N N    . LEU   B 1 69  ? -16.559 24.829  23.723  1   62.36   ? 81  LEU   A N    1 ? 2 
ATOM   2779 C CA   . LEU   B 1 69  ? -16.898 23.777  24.671  1   58.268  ? 81  LEU   A CA   1 ? 2 
ATOM   2780 C C    . LEU   B 1 69  ? -18.303 23.261  24.392  1   60.242  ? 81  LEU   A C    1 ? 2 
ATOM   2781 O O    . LEU   B 1 69  ? -19.234 24.04   24.252  1   65.594  ? 81  LEU   A O    1 ? 2 
ATOM   2782 C CB   . LEU   B 1 69  ? -16.817 24.286  26.101  1   57.643  ? 81  LEU   A CB   1 ? 2 
ATOM   2783 C CG   . LEU   B 1 69  ? -17.008 23.226  27.188  1   58.635  ? 81  LEU   A CG   1 ? 2 
ATOM   2784 C CD1  . LEU   B 1 69  ? -15.846 22.238  27.234  1   53.687  ? 81  LEU   A CD1  1 ? 2 
ATOM   2785 C CD2  . LEU   B 1 69  ? -17.168 23.93   28.527  1   59.629  ? 81  LEU   A CD2  1 ? 2 
ATOM   2786 H H    . LEU   B 1 69  ? -16.501 25.691  24.023  1   63.54   ? 81  LEU   A H    1 c 2 
ATOM   2787 H HA   . LEU   B 1 69  ? -16.254 23.035  24.552  1   56.523  ? 81  LEU   A HA   1 c 2 
ATOM   2788 H HB2  . LEU   B 1 69  ? -15.935 24.706  26.227  1   58.365  ? 81  LEU   A HB2  1 c 2 
ATOM   2789 H HB3  . LEU   B 1 69  ? -17.503 24.982  26.219  1   60.916  ? 81  LEU   A HB3  1 c 2 
ATOM   2790 H HG   . LEU   B 1 69  ? -17.841 22.723  26.997  1   57.883  ? 81  LEU   A HG   1 c 2 
ATOM   2791 H HD11 . LEU   B 1 69  ? -15.805 21.743  26.399  1   53.79   ? 81  LEU   A HD11 1 c 2 
ATOM   2792 H HD12 . LEU   B 1 69  ? -15.977 21.617  27.971  1   52.928  ? 81  LEU   A HD12 1 c 2 
ATOM   2793 H HD13 . LEU   B 1 69  ? -15.013 22.721  27.364  1   54.141  ? 81  LEU   A HD13 1 c 2 
ATOM   2794 H HD21 . LEU   B 1 69  ? -17.93  24.533  28.49   1   61.935  ? 81  LEU   A HD21 1 c 2 
ATOM   2795 H HD22 . LEU   B 1 69  ? -16.364 24.436  28.72   1   59.693  ? 81  LEU   A HD22 1 c 2 
ATOM   2796 H HD23 . LEU   B 1 69  ? -17.311 23.271  29.226  1   58.217  ? 81  LEU   A HD23 1 c 2 
ATOM   2797 N N    . GLY   B 1 70  ? -18.446 21.938  24.345  1   63.474  ? 82  GLY   A N    1 ? 2 
ATOM   2798 C CA   . GLY   B 1 70  ? -19.748 21.309  24.19   1   68.097  ? 82  GLY   A CA   1 ? 2 
ATOM   2799 C C    . GLY   B 1 70  ? -20.27  21.37   22.753  1   74.429  ? 82  GLY   A C    1 ? 2 
ATOM   2800 O O    . GLY   B 1 70  ? -21.395 20.959  22.503  1   83.795  ? 82  GLY   A O    1 ? 2 
ATOM   2801 H H    . GLY   B 1 70  ? -17.707 21.406  24.413  1   60.621  ? 82  GLY   A H    1 c 2 
ATOM   2802 H HA2  . GLY   B 1 70  ? -19.681 20.366  24.471  1   66.114  ? 82  GLY   A HA2  1 c 2 
ATOM   2803 H HA3  . GLY   B 1 70  ? -20.391 21.753  24.789  1   69.236  ? 82  GLY   A HA3  1 c 2 
ATOM   2804 N N    . LYS   B 1 71  ? -19.44  21.842  21.808  1   73.467  ? 83  LYS   A N    1 ? 2 
ATOM   2805 C CA   . LYS   B 1 71  ? -19.832 21.932  20.416  1   77.664  ? 83  LYS   A CA   1 ? 2 
ATOM   2806 C C    . LYS   B 1 71  ? -19.277 20.726  19.66   1   78.369  ? 83  LYS   A C    1 ? 2 
ATOM   2807 O O    . LYS   B 1 71  ? -19.197 20.774  18.436  1   85.89   ? 83  LYS   A O    1 ? 2 
ATOM   2808 C CB   . LYS   B 1 71  ? -19.398 23.279  19.825  1   81.132  ? 83  LYS   A CB   1 ? 2 
ATOM   2809 H H    . LYS   B 1 71  ? -18.594 22.099  22.04   1   72.767  ? 83  LYS   A H    1 c 2 
ATOM   2810 H HA   . LYS   B 1 71  ? -20.821 21.893  20.37   1   79.822  ? 83  LYS   A HA   1 c 2 
ATOM   2811 H HB2  . LYS   B 1 71  ? -18.553 23.398  19.803  0   30      ? 83  LYS   A HB2  1 c 2 
ATOM   2812 H HB3  . LYS   B 1 71  ? -20.359 23.802  19.635  0   30      ? 83  LYS   A HB3  1 c 2 
ATOM   2813 N N    . GLY   B 1 72  ? -18.891 19.667  20.402  1   73.521  ? 84  GLY   A N    1 ? 2 
ATOM   2814 C CA   . GLY   B 1 72  ? -18.361 18.414  19.871  1   70.747  ? 84  GLY   A CA   1 ? 2 
ATOM   2815 C C    . GLY   B 1 72  ? -17.2   18.563  18.874  1   68.18   ? 84  GLY   A C    1 ? 2 
ATOM   2816 O O    . GLY   B 1 72  ? -17.123 17.809  17.91   1   67.372  ? 84  GLY   A O    1 ? 2 
ATOM   2817 H H    . GLY   B 1 72  ? -18.965 19.734  21.31   1   72.469  ? 84  GLY   A H    1 c 2 
ATOM   2818 H HA2  . GLY   B 1 72  ? -18.06  17.86   20.628  1   68.24   ? 84  GLY   A HA2  1 c 2 
ATOM   2819 H HA3  . GLY   B 1 72  ? -19.098 17.931  19.428  1   71.726  ? 84  GLY   A HA3  1 c 2 
ATOM   2820 N N    . GLN   B 1 73  ? -16.275 19.495  19.12   1   63.087  ? 85  GLN   A N    1 ? 2 
ATOM   2821 C CA   . GLN   B 1 73  ? -15.097 19.667  18.28   1   63.962  ? 85  GLN   A CA   1 ? 2 
ATOM   2822 C C    . GLN   B 1 73  ? -13.938 18.797  18.774  1   59.787  ? 85  GLN   A C    1 ? 2 
ATOM   2823 O O    . GLN   B 1 73  ? -12.948 18.574  18.084  1   66.902  ? 85  GLN   A O    1 ? 2 
ATOM   2824 C CB   . GLN   B 1 73  ? -14.668 21.133  18.291  1   66.632  ? 85  GLN   A CB   1 ? 2 
ATOM   2825 C CG   . GLN   B 1 73  ? -15.705 22.098  17.727  1   71.507  ? 85  GLN   A CG   1 ? 2 
ATOM   2826 C CD   . GLN   B 1 73  ? -15.293 23.544  17.909  1   69.877  ? 85  GLN   A CD   1 ? 2 
ATOM   2827 O OE1  . GLN   B 1 73  ? -14.359 23.873  18.646  1   67.64   ? 85  GLN   A OE1  1 ? 2 
ATOM   2828 N NE2  . GLN   B 1 73  ? -16.012 24.446  17.268  1   72.754  ? 85  GLN   A NE2  1 ? 2 
ATOM   2829 H H    . GLN   B 1 73  ? -16.384 20.049  19.839  1   64.003  ? 85  GLN   A H    1 c 2 
ATOM   2830 H HA   . GLN   B 1 73  ? -15.325 19.404  17.352  1   65.433  ? 85  GLN   A HA   1 c 2 
ATOM   2831 H HB2  . GLN   B 1 73  ? -14.466 21.389  19.215  1   65.3    ? 85  GLN   A HB2  1 c 2 
ATOM   2832 H HB3  . GLN   B 1 73  ? -13.841 21.22   17.773  1   67.055  ? 85  GLN   A HB3  1 c 2 
ATOM   2833 H HG2  . GLN   B 1 73  ? -15.83  21.919  16.77   1   72.059  ? 85  GLN   A HG2  1 c 2 
ATOM   2834 H HG3  . GLN   B 1 73  ? -16.565 21.953  18.176  1   70.262  ? 85  GLN   A HG3  1 c 2 
ATOM   2835 H HE21 . GLN   B 1 73  ? -15.816 25.307  17.348  1   74.767  ? 85  GLN   A HE21 1 c 2 
ATOM   2836 H HE22 . GLN   B 1 73  ? -16.691 24.191  16.756  1   74.413  ? 85  GLN   A HE22 1 c 2 
ATOM   2837 N N    . VAL   B 1 74  ? -14.096 18.264  19.979  1   50.242  ? 86  VAL   A N    1 ? 2 
ATOM   2838 C CA   . VAL   B 1 74  ? -13.13  17.399  20.62   1   47.45   ? 86  VAL   A CA   1 ? 2 
ATOM   2839 C C    . VAL   B 1 74  ? -13.885 16.161  21.064  1   44.194  ? 86  VAL   A C    1 ? 2 
ATOM   2840 O O    . VAL   B 1 74  ? -15.096 16.128  20.955  1   43.718  ? 86  VAL   A O    1 ? 2 
ATOM   2841 C CB   . VAL   B 1 74  ? -12.516 18.158  21.808  1   46.385  ? 86  VAL   A CB   1 ? 2 
ATOM   2842 C CG1  . VAL   B 1 74  ? -11.659 19.315  21.309  1   50.006  ? 86  VAL   A CG1  1 ? 2 
ATOM   2843 C CG2  . VAL   B 1 74  ? -13.603 18.68   22.753  1   45.479  ? 86  VAL   A CG2  1 ? 2 
ATOM   2844 H H    . VAL   B 1 74  ? -14.868 18.445  20.432  1   52.032  ? 86  VAL   A H    1 c 2 
ATOM   2845 H HA   . VAL   B 1 74  ? -12.431 17.152  19.985  1   47.52   ? 86  VAL   A HA   1 c 2 
ATOM   2846 H HB   . VAL   B 1 74  ? -11.942 17.527  22.301  1   45.038  ? 86  VAL   A HB   1 c 2 
ATOM   2847 H HG11 . VAL   B 1 74  ? -12.221 19.963  20.851  1   51.119  ? 86  VAL   A HG11 1 c 2 
ATOM   2848 H HG12 . VAL   B 1 74  ? -10.986 18.979  20.693  1   49.595  ? 86  VAL   A HG12 1 c 2 
ATOM   2849 H HG13 . VAL   B 1 74  ? -11.221 19.744  22.063  1   48.813  ? 86  VAL   A HG13 1 c 2 
ATOM   2850 H HG21 . VAL   B 1 74  ? -13.187 19.075  23.536  1   45.161  ? 86  VAL   A HG21 1 c 2 
ATOM   2851 H HG22 . VAL   B 1 74  ? -14.178 17.947  23.029  1   45.159  ? 86  VAL   A HG22 1 c 2 
ATOM   2852 H HG23 . VAL   B 1 74  ? -14.135 19.354  22.299  1   47.634  ? 86  VAL   A HG23 1 c 2 
ATOM   2853 N N    . ILE   B 1 75  ? -13.16  15.173  21.573  1   41.729  ? 87  ILE   A N    1 ? 2 
ATOM   2854 C CA   . ILE   B 1 75  ? -13.799 13.961  22.041  1   43.508  ? 87  ILE   A CA   1 ? 2 
ATOM   2855 C C    . ILE   B 1 75  ? -14.659 14.289  23.272  1   45.135  ? 87  ILE   A C    1 ? 2 
ATOM   2856 O O    . ILE   B 1 75  ? -14.44  15.282  23.962  1   42.298  ? 87  ILE   A O    1 ? 2 
ATOM   2857 C CB   . ILE   B 1 75  ? -12.743 12.894  22.369  1   44.941  ? 87  ILE   A CB   1 ? 2 
ATOM   2858 C CG1  . ILE   B 1 75  ? -11.682 13.419  23.346  1   44.035  ? 87  ILE   A CG1  1 ? 2 
ATOM   2859 C CG2  . ILE   B 1 75  ? -12.116 12.34   21.102  1   45.394  ? 87  ILE   A CG2  1 ? 2 
ATOM   2860 C CD1  . ILE   B 1 75  ? -10.91  12.308  24.035  1   48.727  ? 87  ILE   A CD1  1 ? 2 
ATOM   2861 H H    . ILE   B 1 75  ? -12.251 15.251  21.618  1   42.046  ? 87  ILE   A H    1 c 2 
ATOM   2862 H HA   . ILE   B 1 75  ? -14.379 13.619  21.332  1   45.062  ? 87  ILE   A HA   1 c 2 
ATOM   2863 H HB   . ILE   B 1 75  ? -13.206 12.158  22.814  1   44.17   ? 87  ILE   A HB   1 c 2 
ATOM   2864 H HG12 . ILE   B 1 75  ? -11.05  13.984  22.857  1   45.38   ? 87  ILE   A HG12 1 c 2 
ATOM   2865 H HG13 . ILE   B 1 75  ? -12.117 13.971  24.027  1   44.645  ? 87  ILE   A HG13 1 c 2 
ATOM   2866 H HG21 . ILE   B 1 75  ? -11.484 11.637  21.33   1   45.261  ? 87  ILE   A HG21 1 c 2 
ATOM   2867 H HG22 . ILE   B 1 75  ? -11.651 13.051  20.631  1   46.059  ? 87  ILE   A HG22 1 c 2 
ATOM   2868 H HG23 . ILE   B 1 75  ? -12.81  11.974  20.529  1   46.753  ? 87  ILE   A HG23 1 c 2 
ATOM   2869 H HD11 . ILE   B 1 75  ? -11.531 11.728  24.514  1   46.867  ? 87  ILE   A HD11 1 c 2 
ATOM   2870 H HD12 . ILE   B 1 75  ? -10.277 12.697  24.669  1   46.337  ? 87  ILE   A HD12 1 c 2 
ATOM   2871 H HD13 . ILE   B 1 75  ? -10.422 11.784  23.372  1   47.53   ? 87  ILE   A HD13 1 c 2 
ATOM   2872 N N    . LYS   B 1 76  ? -15.628 13.415  23.519  1   42.579  ? 88  LYS   A N    1 ? 2 
ATOM   2873 C CA   . LYS   B 1 76  ? -16.662 13.622  24.52   1   43.17   ? 88  LYS   A CA   1 ? 2 
ATOM   2874 C C    . LYS   B 1 76  ? -16.014 13.879  25.879  1   42.555  ? 88  LYS   A C    1 ? 2 
ATOM   2875 O O    . LYS   B 1 76  ? -16.467 14.768  26.598  1   42.106  ? 88  LYS   A O    1 ? 2 
ATOM   2876 C CB   . LYS   B 1 76  ? -17.588 12.402  24.443  1   45.889  ? 88  LYS   A CB   1 ? 2 
ATOM   2877 H H    . LYS   B 1 76  ? -15.644 12.641  23.033  1   43.816  ? 88  LYS   A H    1 c 2 
ATOM   2878 H HA   . LYS   B 1 76  ? -17.181 14.426  24.265  1   44.597  ? 88  LYS   A HA   1 c 2 
ATOM   2879 H HB2  . LYS   B 1 76  ? -16.999 11.605  24.437  0   30      ? 88  LYS   A HB2  1 c 2 
ATOM   2880 H HB3  . LYS   B 1 76  ? -18.52  12.671  24.491  0   30      ? 88  LYS   A HB3  1 c 2 
ATOM   2881 N N    . ALA   B 1 77  ? -14.96  13.113  26.214  1   39.904  ? 89  ALA   A N    1 ? 2 
ATOM   2882 C CA   . ALA   B 1 77  ? -14.277 13.243  27.489  1   40.442  ? 89  ALA   A CA   1 ? 2 
ATOM   2883 C C    . ALA   B 1 77  ? -13.735 14.648  27.715  1   40.906  ? 89  ALA   A C    1 ? 2 
ATOM   2884 O O    . ALA   B 1 77  ? -13.643 15.065  28.874  1   36.082  ? 89  ALA   A O    1 ? 2 
ATOM   2885 C CB   . ALA   B 1 77  ? -13.132 12.268  27.623  1   38.093  ? 89  ALA   A CB   1 ? 2 
ATOM   2886 H H    . ALA   B 1 77  ? -14.663 12.482  25.622  1   40.715  ? 89  ALA   A H    1 c 2 
ATOM   2887 H HA   . ALA   B 1 77  ? -14.94  13.055  28.209  1   40.23   ? 89  ALA   A HA   1 c 2 
ATOM   2888 H HB1  . ALA   B 1 77  ? -13.47  11.358  27.582  1   39.038  ? 89  ALA   A HB1  1 c 2 
ATOM   2889 H HB2  . ALA   B 1 77  ? -12.498 12.407  26.899  1   38.518  ? 89  ALA   A HB2  1 c 2 
ATOM   2890 H HB3  . ALA   B 1 77  ? -12.682 12.406  28.474  1   38.083  ? 89  ALA   A HB3  1 c 2 
ATOM   2891 N N    . TRP   B 1 78  ? -13.323 15.337  26.644  1   39.422  ? 90  TRP   A N    1 ? 2 
ATOM   2892 C CA   . TRP   B 1 78  ? -12.86  16.707  26.8    1   42.194  ? 90  TRP   A CA   1 ? 2 
ATOM   2893 C C    . TRP   B 1 78  ? -14.015 17.651  27.117  1   44.236  ? 90  TRP   A C    1 ? 2 
ATOM   2894 O O    . TRP   B 1 78  ? -13.892 18.538  27.983  1   41.18   ? 90  TRP   A O    1 ? 2 
ATOM   2895 C CB   . TRP   B 1 78  ? -12.104 17.183  25.554  1   44.979  ? 90  TRP   A CB   1 ? 2 
ATOM   2896 C CG   . TRP   B 1 78  ? -10.624 16.962  25.618  1   44.421  ? 90  TRP   A CG   1 ? 2 
ATOM   2897 C CD1  . TRP   B 1 78  ? -9.97   15.805  25.907  1   42.766  ? 90  TRP   A CD1  1 ? 2 
ATOM   2898 C CD2  . TRP   B 1 78  ? -9.608  17.97   25.425  1   43.277  ? 90  TRP   A CD2  1 ? 2 
ATOM   2899 N NE1  . TRP   B 1 78  ? -8.623  16.01   25.892  1   44.125  ? 90  TRP   A NE1  1 ? 2 
ATOM   2900 C CE2  . TRP   B 1 78  ? -8.369  17.331  25.62   1   42.179  ? 90  TRP   A CE2  1 ? 2 
ATOM   2901 C CE3  . TRP   B 1 78  ? -9.633  19.335  25.119  1   45.094  ? 90  TRP   A CE3  1 ? 2 
ATOM   2902 C CZ2  . TRP   B 1 78  ? -7.154  18      25.489  1   39.372  ? 90  TRP   A CZ2  1 ? 2 
ATOM   2903 C CZ3  . TRP   B 1 78  ? -8.432  20.005  25.015  1   43.904  ? 90  TRP   A CZ3  1 ? 2 
ATOM   2904 C CH2  . TRP   B 1 78  ? -7.212  19.327  25.153  1   42.849  ? 90  TRP   A CH2  1 ? 2 
ATOM   2905 H H    . TRP   B 1 78  ? -13.323 14.952  25.815  1   40.79   ? 90  TRP   A H    1 c 2 
ATOM   2906 H HA   . TRP   B 1 78  ? -12.225 16.729  27.566  1   41.53   ? 90  TRP   A HA   1 c 2 
ATOM   2907 H HB2  . TRP   B 1 78  ? -12.461 16.716  24.77   1   44.862  ? 90  TRP   A HB2  1 c 2 
ATOM   2908 H HB3  . TRP   B 1 78  ? -12.273 18.142  25.434  1   45.484  ? 90  TRP   A HB3  1 c 2 
ATOM   2909 H HD1  . TRP   B 1 78  ? -10.381 14.973  26.084  1   42.733  ? 90  TRP   A HD1  1 c 2 
ATOM   2910 H HE1  . TRP   B 1 78  ? -8.023  15.403  26.048  1   42.728  ? 90  TRP   A HE1  1 c 2 
ATOM   2911 H HE3  . TRP   B 1 78  ? -10.451 19.786  24.995  1   45.255  ? 90  TRP   A HE3  1 c 2 
ATOM   2912 H HZ2  . TRP   B 1 78  ? -6.332  17.554  25.603  1   40.61   ? 90  TRP   A HZ2  1 c 2 
ATOM   2913 H HZ3  . TRP   B 1 78  ? -8.43   20.919  24.789  1   45.775  ? 90  TRP   A HZ3  1 c 2 
ATOM   2914 H HH2  . TRP   B 1 78  ? -6.41   19.815  25.091  1   43.519  ? 90  TRP   A HH2  1 c 2 
ATOM   2915 N N    . ASP   B 1 79  ? -15.123 17.523  26.375  1   42.61   ? 91  ASP   A N    1 ? 2 
ATOM   2916 C CA   . ASP   B 1 79  ? -16.266 18.376  26.638  1   42.455  ? 91  ASP   A CA   1 ? 2 
ATOM   2917 C C    . ASP   B 1 79  ? -16.732 18.195  28.084  1   44.329  ? 91  ASP   A C    1 ? 2 
ATOM   2918 O O    . ASP   B 1 79  ? -17.023 19.173  28.768  1   47.865  ? 91  ASP   A O    1 ? 2 
ATOM   2919 C CB   . ASP   B 1 79  ? -17.371 18.119  25.627  1   45.834  ? 91  ASP   A CB   1 ? 2 
ATOM   2920 C CG   . ASP   B 1 79  ? -17.24  18.882  24.317  1   47.743  ? 91  ASP   A CG   1 ? 2 
ATOM   2921 O OD1  . ASP   B 1 79  ? -16.459 19.863  24.271  1   53.009  ? 91  ASP   A OD1  1 ? 2 
ATOM   2922 O OD2  . ASP   B 1 79  ? -17.911 18.495  23.365  1   49.984  ? 91  ASP   A OD2  1 ? 2 
ATOM   2923 H H    . ASP   B 1 79  ? -15.163 16.908  25.7    1   42.776  ? 91  ASP   A H    1 c 2 
ATOM   2924 H HA   . ASP   B 1 79  ? -15.977 19.309  26.529  1   44.361  ? 91  ASP   A HA   1 c 2 
ATOM   2925 H HB2  . ASP   B 1 79  ? -17.401 17.162  25.421  1   44.832  ? 91  ASP   A HB2  1 c 2 
ATOM   2926 H HB3  . ASP   B 1 79  ? -18.23  18.364  26.031  1   46.645  ? 91  ASP   A HB3  1 c 2 
ATOM   2927 N N    . ILE   B 1 80  ? -16.741 16.955  28.582  1   46      ? 92  ILE   A N    1 ? 2 
ATOM   2928 C CA   . ILE   B 1 80  ? -17.152 16.692  29.953  1   46.192  ? 92  ILE   A CA   1 ? 2 
ATOM   2929 C C    . ILE   B 1 80  ? -16.096 17.205  30.913  1   41.62   ? 92  ILE   A C    1 ? 2 
ATOM   2930 O O    . ILE   B 1 80  ? -16.416 17.895  31.88   1   41.445  ? 92  ILE   A O    1 ? 2 
ATOM   2931 C CB   . ILE   B 1 80  ? -17.442 15.2    30.168  1   50.006  ? 92  ILE   A CB   1 ? 2 
ATOM   2932 C CG1  . ILE   B 1 80  ? -18.691 14.757  29.38   1   52.265  ? 92  ILE   A CG1  1 ? 2 
ATOM   2933 C CG2  . ILE   B 1 80  ? -17.604 14.908  31.657  1   57.186  ? 92  ILE   A CG2  1 ? 2 
ATOM   2934 C CD1  . ILE   B 1 80  ? -18.748 13.25   29.214  1   55.629  ? 92  ILE   A CD1  1 ? 2 
ATOM   2935 H H    . ILE   B 1 80  ? -16.491 16.253  28.053  1   44.752  ? 92  ILE   A H    1 c 2 
ATOM   2936 H HA   . ILE   B 1 80  ? -17.979 17.184  30.12   1   47.524  ? 92  ILE   A HA   1 c 2 
ATOM   2937 H HB   . ILE   B 1 80  ? -16.677 14.69   29.836  1   49.385  ? 92  ILE   A HB   1 c 2 
ATOM   2938 H HG12 . ILE   B 1 80  ? -19.493 15.059  29.853  1   54.171  ? 92  ILE   A HG12 1 c 2 
ATOM   2939 H HG13 . ILE   B 1 80  ? -18.681 15.178  28.496  1   53.16   ? 92  ILE   A HG13 1 c 2 
ATOM   2940 H HG21 . ILE   B 1 80  ? -17.947 14.007  31.778  1   55.23   ? 92  ILE   A HG21 1 c 2 
ATOM   2941 H HG22 . ILE   B 1 80  ? -18.226 15.544  32.048  1   56.078  ? 92  ILE   A HG22 1 c 2 
ATOM   2942 H HG23 . ILE   B 1 80  ? -16.743 14.984  32.102  1   53.954  ? 92  ILE   A HG23 1 c 2 
ATOM   2943 H HD11 . ILE   B 1 80  ? -17.927 12.94   28.786  1   53.461  ? 92  ILE   A HD11 1 c 2 
ATOM   2944 H HD12 . ILE   B 1 80  ? -19.512 13.014  28.655  1   55.85   ? 92  ILE   A HD12 1 c 2 
ATOM   2945 H HD13 . ILE   B 1 80  ? -18.84  12.822  30.085  1   54.65   ? 92  ILE   A HD13 1 c 2 
ATOM   2946 N N    . GLY   B 1 81  ? -14.836 16.904  30.626  1   38.284  ? 93  GLY   A N    1 ? 2 
ATOM   2947 C CA   . GLY   B 1 81  ? -13.743 17.142  31.547  1   38.454  ? 93  GLY   A CA   1 ? 2 
ATOM   2948 C C    . GLY   B 1 81  ? -13.382 18.615  31.74   1   39.295  ? 93  GLY   A C    1 ? 2 
ATOM   2949 O O    . GLY   B 1 81  ? -13.206 19.093  32.865  1   38.082  ? 93  GLY   A O    1 ? 2 
ATOM   2950 H H    . GLY   B 1 81  ? -14.645 16.526  29.816  1   38.592  ? 93  GLY   A H    1 c 2 
ATOM   2951 H HA2  . GLY   B 1 81  ? -13.982 16.757  32.42   1   38.366  ? 93  GLY   A HA2  1 c 2 
ATOM   2952 H HA3  . GLY   B 1 81  ? -12.948 16.658  31.22   1   37.393  ? 93  GLY   A HA3  1 c 2 
ATOM   2953 N N    . VAL   B 1 82  ? -13.268 19.327  30.626  1   38.148  ? 94  VAL   A N    1 ? 2 
ATOM   2954 C CA   . VAL   B 1 82  ? -12.901 20.719  30.667  1   40.748  ? 94  VAL   A CA   1 ? 2 
ATOM   2955 C C    . VAL   B 1 82  ? -14.016 21.564  31.294  1   44.039  ? 94  VAL   A C    1 ? 2 
ATOM   2956 O O    . VAL   B 1 82  ? -13.711 22.586  31.93   1   41.078  ? 94  VAL   A O    1 ? 2 
ATOM   2957 C CB   . VAL   B 1 82  ? -12.46  21.209  29.279  1   40.258  ? 94  VAL   A CB   1 ? 2 
ATOM   2958 C CG1  . VAL   B 1 82  ? -12.188 22.704  29.266  1   49.817  ? 94  VAL   A CG1  1 ? 2 
ATOM   2959 C CG2  . VAL   B 1 82  ? -11.209 20.498  28.846  1   41.02   ? 94  VAL   A CG2  1 ? 2 
ATOM   2960 H H    . VAL   B 1 82  ? -13.423 18.933  29.816  1   38.543  ? 94  VAL   A H    1 c 2 
ATOM   2961 H HA   . VAL   B 1 82  ? -12.124 20.792  31.254  1   40.305  ? 94  VAL   A HA   1 c 2 
ATOM   2962 H HB   . VAL   B 1 82  ? -13.185 21.008  28.642  1   42.363  ? 94  VAL   A HB   1 c 2 
ATOM   2963 H HG11 . VAL   B 1 82  ? -11.635 22.94   30.03   1   47.503  ? 94  VAL   A HG11 1 c 2 
ATOM   2964 H HG12 . VAL   B 1 82  ? -13.028 23.19   29.312  1   48.765  ? 94  VAL   A HG12 1 c 2 
ATOM   2965 H HG13 . VAL   B 1 82  ? -11.724 22.94   28.447  1   47.957  ? 94  VAL   A HG13 1 c 2 
ATOM   2966 H HG21 . VAL   B 1 82  ? -10.935 20.823  27.972  1   41.047  ? 94  VAL   A HG21 1 c 2 
ATOM   2967 H HG22 . VAL   B 1 82  ? -11.378 19.542  28.796  1   39.198  ? 94  VAL   A HG22 1 c 2 
ATOM   2968 H HG23 . VAL   B 1 82  ? -10.5   20.667  29.49   1   40.278  ? 94  VAL   A HG23 1 c 2 
ATOM   2969 N N    . ALA   B 1 83  ? -15.287 21.129  31.16   1   43.374  ? 95  ALA   A N    1 ? 2 
ATOM   2970 C CA   . ALA   B 1 83  ? -16.372 21.831  31.82   1   44.507  ? 95  ALA   A CA   1 ? 2 
ATOM   2971 C C    . ALA   B 1 83  ? -16.253 21.785  33.337  1   45.302  ? 95  ALA   A C    1 ? 2 
ATOM   2972 O O    . ALA   B 1 83  ? -16.932 22.542  33.982  1   49.16   ? 95  ALA   A O    1 ? 2 
ATOM   2973 C CB   . ALA   B 1 83  ? -17.75  21.319  31.412  1   48.108  ? 95  ALA   A CB   1 ? 2 
ATOM   2974 H H    . ALA   B 1 83  ? -15.474 20.396  30.648  1   42.519  ? 95  ALA   A H    1 c 2 
ATOM   2975 H HA   . ALA   B 1 83  ? -16.31  22.789  31.55   1   46.846  ? 95  ALA   A HA   1 c 2 
ATOM   2976 H HB1  . ALA   B 1 83  ? -17.844 21.365  30.446  1   47.543  ? 95  ALA   A HB1  1 c 2 
ATOM   2977 H HB2  . ALA   B 1 83  ? -17.855 20.397  31.702  1   46.136  ? 95  ALA   A HB2  1 c 2 
ATOM   2978 H HB3  . ALA   B 1 83  ? -18.438 21.866  31.828  1   49.154  ? 95  ALA   A HB3  1 c 2 
ATOM   2979 N N    . THR   B 1 84  ? -15.465 20.867  33.908  1   46.303  ? 96  THR   A N    1 ? 2 
ATOM   2980 C CA   . THR   B 1 84  ? -15.296 20.777  35.347  1   45.055  ? 96  THR   A CA   1 ? 2 
ATOM   2981 C C    . THR   B 1 84  ? -14.118 21.632  35.811  1   47.491  ? 96  THR   A C    1 ? 2 
ATOM   2982 O O    . THR   B 1 84  ? -13.865 21.668  36.998  1   43.901  ? 96  THR   A O    1 ? 2 
ATOM   2983 C CB   . THR   B 1 84  ? -15.072 19.324  35.798  1   43.151  ? 96  THR   A CB   1 ? 2 
ATOM   2984 O OG1  . THR   B 1 84  ? -13.782 18.888  35.374  1   40.122  ? 96  THR   A OG1  1 ? 2 
ATOM   2985 C CG2  . THR   B 1 84  ? -16.121 18.353  35.296  1   43.704  ? 96  THR   A CG2  1 ? 2 
ATOM   2986 H H    . THR   B 1 84  ? -15.03  20.261  33.381  1   43.72   ? 96  THR   A H    1 c 2 
ATOM   2987 H HA   . THR   B 1 84  ? -16.114 21.11   35.777  1   47.224  ? 96  THR   A HA   1 c 2 
ATOM   2988 H HB   . THR   B 1 84  ? -15.101 19.301  36.784  1   43.855  ? 96  THR   A HB   1 c 2 
ATOM   2989 H HG1  . THR   B 1 84  ? -13.866 18.952  34.494  0   30      ? 96  THR   A HG1  1 c 2 
ATOM   2990 H HG21 . THR   B 1 84  ? -15.954 17.472  35.673  1   42.83   ? 96  THR   A HG21 1 c 2 
ATOM   2991 H HG22 . THR   B 1 84  ? -16.08  18.302  34.328  1   42.808  ? 96  THR   A HG22 1 c 2 
ATOM   2992 H HG23 . THR   B 1 84  ? -17.003 18.658  35.567  1   44.914  ? 96  THR   A HG23 1 c 2 
ATOM   2993 N N    . MET   B 1 85  ? -13.337 22.242  34.906  1   48.201  ? 97  MET   A N    1 ? 2 
ATOM   2994 C CA   . MET   B 1 85  ? -12.045 22.799  35.299  1   47.923  ? 97  MET   A CA   1 ? 2 
ATOM   2995 C C    . MET   B 1 85  ? -12.129 24.311  35.526  1   48.197  ? 97  MET   A C    1 ? 2 
ATOM   2996 O O    . MET   B 1 85  ? -12.942 25.003  34.933  1   46.615  ? 97  MET   A O    1 ? 2 
ATOM   2997 C CB   . MET   B 1 85  ? -10.976 22.532  34.234  1   46.313  ? 97  MET   A CB   1 ? 2 
ATOM   2998 C CG   . MET   B 1 85  ? -10.666 21.039  34.056  1   43.17   ? 97  MET   A CG   1 ? 2 
ATOM   2999 S SD   . MET   B 1 85  ? -9.496  20.801  32.708  1   43.824  ? 97  MET   A SD   1 ? 2 
ATOM   3000 C CE   . MET   B 1 85  ? -8.021  21.534  33.442  1   45.947  ? 97  MET   A CE   1 ? 2 
ATOM   3001 H H    . MET   B 1 85  ? -13.61  22.319  34.038  1   47.66   ? 97  MET   A H    1 c 2 
ATOM   3002 H HA   . MET   B 1 85  ? -11.767 22.371  36.147  1   47.22   ? 97  MET   A HA   1 c 2 
ATOM   3003 H HB2  . MET   B 1 85  ? -11.283 22.9    33.379  1   46.572  ? 97  MET   A HB2  1 c 2 
ATOM   3004 H HB3  . MET   B 1 85  ? -10.155 23.003  34.488  1   46.995  ? 97  MET   A HB3  1 c 2 
ATOM   3005 H HG2  . MET   B 1 85  ? -10.286 20.679  34.879  1   43.5    ? 97  MET   A HG2  1 c 2 
ATOM   3006 H HG3  . MET   B 1 85  ? -11.488 20.553  33.859  1   43.069  ? 97  MET   A HG3  1 c 2 
ATOM   3007 H HE1  . MET   B 1 85  ? -7.275  21.449  32.822  1   45.653  ? 97  MET   A HE1  1 c 2 
ATOM   3008 H HE2  . MET   B 1 85  ? -8.182  22.478  33.624  1   47.265  ? 97  MET   A HE2  1 c 2 
ATOM   3009 H HE3  . MET   B 1 85  ? -7.809  21.072  34.274  1   45.543  ? 97  MET   A HE3  1 c 2 
ATOM   3010 N N    . LYS   B 1 86  ? -11.233 24.813  36.366  1   50.664  ? 98  LYS   A N    1 ? 2 
ATOM   3011 C CA   . LYS   B 1 86  ? -11.17  26.229  36.694  1   57.961  ? 98  LYS   A CA   1 ? 2 
ATOM   3012 C C    . LYS   B 1 86  ? -9.944  26.811  36.005  1   56.083  ? 98  LYS   A C    1 ? 2 
ATOM   3013 O O    . LYS   B 1 86  ? -9.05   26.064  35.605  1   49.41   ? 98  LYS   A O    1 ? 2 
ATOM   3014 C CB   . LYS   B 1 86  ? -11.084 26.43   38.205  1   61.854  ? 98  LYS   A CB   1 ? 2 
ATOM   3015 C CG   . LYS   B 1 86  ? -12.037 25.636  39.058  1   66.534  ? 98  LYS   A CG   1 ? 2 
ATOM   3016 C CD   . LYS   B 1 86  ? -13.387 26.306  39.27   1   77.251  ? 98  LYS   A CD   1 ? 2 
ATOM   3017 C CE   . LYS   B 1 86  ? -14.263 25.453  40.123  1   82.462  ? 98  LYS   A CE   1 ? 2 
ATOM   3018 N NZ   . LYS   B 1 86  ? -13.579 25.098  41.368  1   86.915  ? 98  LYS   A NZ   1 ? 2 
ATOM   3019 H H    . LYS   B 1 86  ? -10.627 24.25   36.754  1   50.232  ? 98  LYS   A H    1 c 2 
ATOM   3020 H HA   . LYS   B 1 86  ? -11.982 26.679  36.346  1   58.06   ? 98  LYS   A HA   1 c 2 
ATOM   3021 H HB2  . LYS   B 1 86  ? -10.17  26.214  38.49   1   62.084  ? 98  LYS   A HB2  1 c 2 
ATOM   3022 H HB3  . LYS   B 1 86  ? -11.229 27.382  38.394  1   65.098  ? 98  LYS   A HB3  1 c 2 
ATOM   3023 H HG2  . LYS   B 1 86  ? -12.178 24.759  38.641  1   64.629  ? 98  LYS   A HG2  1 c 2 
ATOM   3024 H HG3  . LYS   B 1 86  ? -11.613 25.485  39.93   1   67.695  ? 98  LYS   A HG3  1 c 2 
ATOM   3025 H HD2  . LYS   B 1 86  ? -13.257 27.175  39.704  1   78.916  ? 98  LYS   A HD2  1 c 2 
ATOM   3026 H HD3  . LYS   B 1 86  ? -13.821 26.451  38.401  1   76.115  ? 98  LYS   A HD3  1 c 2 
ATOM   3027 H HE2  . LYS   B 1 86  ? -15.086 25.93   40.334  1   84.062  ? 98  LYS   A HE2  1 c 2 
ATOM   3028 H HE3  . LYS   B 1 86  ? -14.495 24.637  39.644  1   79.942  ? 98  LYS   A HE3  1 c 2 
ATOM   3029 H HZ1  . LYS   B 1 86  ? -13.074 25.792  41.66   1   86.857  ? 98  LYS   A HZ1  1 c 2 
ATOM   3030 H HZ2  . LYS   B 1 86  ? -13.053 24.371  41.243  1   83.366  ? 98  LYS   A HZ2  1 c 2 
ATOM   3031 H HZ3  . LYS   B 1 86  ? -14.196 24.903  42.002  1   86.476  ? 98  LYS   A HZ3  1 c 2 
ATOM   3032 N N    . LYS   B 1 87  ? -9.919  28.142  35.856  1   60.454  ? 99  LYS   A N    1 ? 2 
ATOM   3033 C CA   . LYS   B 1 87  ? -8.798  28.814  35.217  1   67.185  ? 99  LYS   A CA   1 ? 2 
ATOM   3034 C C    . LYS   B 1 87  ? -7.514  28.498  35.989  1   66.89   ? 99  LYS   A C    1 ? 2 
ATOM   3035 O O    . LYS   B 1 87  ? -7.475  28.498  37.221  1   62.877  ? 99  LYS   A O    1 ? 2 
ATOM   3036 C CB   . LYS   B 1 87  ? -9.071  30.314  35.07   1   76.271  ? 99  LYS   A CB   1 ? 2 
ATOM   3037 C CG   . LYS   B 1 87  ? -8.074  31.133  34.25   1   82.816  ? 99  LYS   A CG   1 ? 2 
ATOM   3038 C CD   . LYS   B 1 87  ? -8.723  32.432  33.765  1   94.639  ? 99  LYS   A CD   1 ? 2 
ATOM   3039 C CE   . LYS   B 1 87  ? -7.841  33.648  33.671  1   105.438 ? 99  LYS   A CE   1 ? 2 
ATOM   3040 N NZ   . LYS   B 1 87  ? -6.704  33.456  32.769  1   108.344 ? 99  LYS   A NZ   1 ? 2 
ATOM   3041 H H    . LYS   B 1 87  ? -10.62  28.643  36.161  1   63.029  ? 99  LYS   A H    1 c 2 
ATOM   3042 H HA   . LYS   B 1 87  ? -8.708  28.44   34.303  1   65.371  ? 99  LYS   A HA   1 c 2 
ATOM   3043 H HB2  . LYS   B 1 87  ? -9.958  30.421  34.664  1   76.351  ? 99  LYS   A HB2  1 c 2 
ATOM   3044 H HB3  . LYS   B 1 87  ? -9.115  30.705  35.969  1   77.822  ? 99  LYS   A HB3  1 c 2 
ATOM   3045 H HG2  . LYS   B 1 87  ? -7.292  31.341  34.805  1   84.499  ? 99  LYS   A HG2  1 c 2 
ATOM   3046 H HG3  . LYS   B 1 87  ? -7.783  30.602  33.479  1   81.435  ? 99  LYS   A HG3  1 c 2 
ATOM   3047 H HD2  . LYS   B 1 87  ? -9.112  32.262  32.88   1   93.264  ? 99  LYS   A HD2  1 c 2 
ATOM   3048 H HD3  . LYS   B 1 87  ? -9.472  32.641  34.365  1   94.876  ? 99  LYS   A HD3  1 c 2 
ATOM   3049 H HE2  . LYS   B 1 87  ? -8.368  34.404  33.355  1   107.47  ? 99  LYS   A HE2  1 c 2 
ATOM   3050 H HE3  . LYS   B 1 87  ? -7.504  33.868  34.558  1   105.911 ? 99  LYS   A HE3  1 c 2 
ATOM   3051 H HZ1  . LYS   B 1 87  ? -6.998  33.162  31.964  1   105.878 ? 99  LYS   A HZ1  1 c 2 
ATOM   3052 H HZ2  . LYS   B 1 87  ? -6.132  32.847  33.118  1   105.213 ? 99  LYS   A HZ2  1 c 2 
ATOM   3053 H HZ3  . LYS   B 1 87  ? -6.267  34.242  32.656  1   110.374 ? 99  LYS   A HZ3  1 c 2 
ATOM   3054 N N    . GLY   B 1 88  ? -6.482  28.117  35.236  1   64.086  ? 100 GLY   A N    1 ? 2 
ATOM   3055 C CA   . GLY   B 1 88  ? -5.186  27.809  35.814  1   61.416  ? 100 GLY   A CA   1 ? 2 
ATOM   3056 C C    . GLY   B 1 88  ? -5.093  26.388  36.366  1   56.945  ? 100 GLY   A C    1 ? 2 
ATOM   3057 O O    . GLY   B 1 88  ? -4.022  25.999  36.805  1   59.128  ? 100 GLY   A O    1 ? 2 
ATOM   3058 H H    . GLY   B 1 88  ? -6.586  28.047  34.33   1   63.135  ? 100 GLY   A H    1 c 2 
ATOM   3059 H HA2  . GLY   B 1 88  ? -4.495  27.933  35.122  1   62.196  ? 100 GLY   A HA2  1 c 2 
ATOM   3060 H HA3  . GLY   B 1 88  ? -5      28.452  36.539  1   64.133  ? 100 GLY   A HA3  1 c 2 
ATOM   3061 N N    . GLU   B 1 89  ? -6.185  25.608  36.318  1   56.115  ? 101 GLU   A N    1 ? 2 
ATOM   3062 C CA   . GLU   B 1 89  ? -6.179  24.228  36.784  1   53.794  ? 101 GLU   A CA   1 ? 2 
ATOM   3063 C C    . GLU   B 1 89  ? -5.383  23.378  35.793  1   51.937  ? 101 GLU   A C    1 ? 2 
ATOM   3064 O O    . GLU   B 1 89  ? -5.503  23.554  34.567  1   52.694  ? 101 GLU   A O    1 ? 2 
ATOM   3065 C CB   . GLU   B 1 89  ? -7.612  23.703  36.918  1   54.44   ? 101 GLU   A CB   1 ? 2 
ATOM   3066 C CG   . GLU   B 1 89  ? -7.759  22.313  37.539  1   47.474  ? 101 GLU   A CG   1 ? 2 
ATOM   3067 C CD   . GLU   B 1 89  ? -9.214  21.876  37.668  1   45.132  ? 101 GLU   A CD   1 ? 2 
ATOM   3068 O OE1  . GLU   B 1 89  ? -10.126 22.609  38.191  1   47.1    ? 101 GLU   A OE1  1 ? 2 
ATOM   3069 O OE2  . GLU   B 1 89  ? -9.474  20.739  37.199  1   42.265  ? 101 GLU   A OE2  1 ? 2 
ATOM   3070 H H    . GLU   B 1 89  ? -6.961  25.946  35.974  1   55.953  ? 101 GLU   A H    1 c 2 
ATOM   3071 H HA   . GLU   B 1 89  ? -5.738  24.199  37.667  1   55.089  ? 101 GLU   A HA   1 c 2 
ATOM   3072 H HB2  . GLU   B 1 89  ? -8.125  24.337  37.462  1   54.189  ? 101 GLU   A HB2  1 c 2 
ATOM   3073 H HB3  . GLU   B 1 89  ? -8.019  23.681  36.027  1   51.797  ? 101 GLU   A HB3  1 c 2 
ATOM   3074 H HG2  . GLU   B 1 89  ? -7.281  21.659  36.986  1   46.844  ? 101 GLU   A HG2  1 c 2 
ATOM   3075 H HG3  . GLU   B 1 89  ? -7.35   22.312  38.43   1   49.223  ? 101 GLU   A HG3  1 c 2 
ATOM   3076 N N    . ILE   B 1 90  ? -4.523  22.501  36.344  1   51.225  ? 102 ILE   A N    1 ? 2 
ATOM   3077 C CA   . ILE   B 1 90  ? -4.016  21.361  35.585  1   48.53   ? 102 ILE   A CA   1 ? 2 
ATOM   3078 C C    . ILE   B 1 90  ? -4.697  20.102  36.096  1   47.84   ? 102 ILE   A C    1 ? 2 
ATOM   3079 O O    . ILE   B 1 90  ? -4.663  19.838  37.302  1   44.295  ? 102 ILE   A O    1 ? 2 
ATOM   3080 C CB   . ILE   B 1 90  ? -2.483  21.235  35.643  1   51.056  ? 102 ILE   A CB   1 ? 2 
ATOM   3081 C CG1  . ILE   B 1 90  ? -1.799  22.523  35.139  1   53.294  ? 102 ILE   A CG1  1 ? 2 
ATOM   3082 C CG2  . ILE   B 1 90  ? -2.003  19.992  34.882  1   46.378  ? 102 ILE   A CG2  1 ? 2 
ATOM   3083 C CD1  . ILE   B 1 90  ? -0.319  22.64   35.461  1   55.131  ? 102 ILE   A CD1  1 ? 2 
ATOM   3084 H H    . ILE   B 1 90  ? -4.247  22.616  37.208  1   52.269  ? 102 ILE   A H    1 c 2 
ATOM   3085 H HA   . ILE   B 1 90  ? -4.267  21.487  34.654  1   48.382  ? 102 ILE   A HA   1 c 2 
ATOM   3086 H HB   . ILE   B 1 90  ? -2.234  21.121  36.582  1   51.095  ? 102 ILE   A HB   1 c 2 
ATOM   3087 H HG12 . ILE   B 1 90  ? -1.909  22.571  34.167  1   52.548  ? 102 ILE   A HG12 1 c 2 
ATOM   3088 H HG13 . ILE   B 1 90  ? -2.261  23.294  35.526  1   54.151  ? 102 ILE   A HG13 1 c 2 
ATOM   3089 H HG21 . ILE   B 1 90  ? -1.035  20.005  34.812  1   48.561  ? 102 ILE   A HG21 1 c 2 
ATOM   3090 H HG22 . ILE   B 1 90  ? -2.391  19.987  33.991  1   46.296  ? 102 ILE   A HG22 1 c 2 
ATOM   3091 H HG23 . ILE   B 1 90  ? -2.278  19.191  35.358  1   46.435  ? 102 ILE   A HG23 1 c 2 
ATOM   3092 H HD11 . ILE   B 1 90  ? -0.198  22.676  36.429  1   56.281  ? 102 ILE   A HD11 1 c 2 
ATOM   3093 H HD12 . ILE   B 1 90  ? 0.034   23.456  35.06   1   56.947  ? 102 ILE   A HD12 1 c 2 
ATOM   3094 H HD13 . ILE   B 1 90  ? 0.162   21.871  35.103  1   54.613  ? 102 ILE   A HD13 1 c 2 
ATOM   3095 N N    . ALA   B 1 91  ? -5.286  19.34   35.144  1   40.097  ? 103 ALA   A N    1 ? 2 
ATOM   3096 C CA   . ALA   B 1 91  ? -5.964  18.099  35.478  1   40.509  ? 103 ALA   A CA   1 ? 2 
ATOM   3097 C C    . ALA   B 1 91  ? -5.437  16.967  34.593  1   38.496  ? 103 ALA   A C    1 ? 2 
ATOM   3098 O O    . ALA   B 1 91  ? -4.908  17.204  33.507  1   40.153  ? 103 ALA   A O    1 ? 2 
ATOM   3099 C CB   . ALA   B 1 91  ? -7.485  18.255  35.331  1   37.93   ? 103 ALA   A CB   1 ? 2 
ATOM   3100 H H    . ALA   B 1 91  ? -5.259  19.606  34.27   1   41.584  ? 103 ALA   A H    1 c 2 
ATOM   3101 H HA   . ALA   B 1 91  ? -5.754  17.875  36.424  1   40.411  ? 103 ALA   A HA   1 c 2 
ATOM   3102 H HB1  . ALA   B 1 91  ? -7.803  18.946  35.936  1   39.404  ? 103 ALA   A HB1  1 c 2 
ATOM   3103 H HB2  . ALA   B 1 91  ? -7.701  18.504  34.417  1   38.018  ? 103 ALA   A HB2  1 c 2 
ATOM   3104 H HB3  . ALA   B 1 91  ? -7.922  17.414  35.547  1   37.84   ? 103 ALA   A HB3  1 c 2 
ATOM   3105 N N    . HIS   B 1 92  ? -5.559  15.753  35.113  1   40.428  ? 104 HIS   A N    1 ? 2 
ATOM   3106 C CA   . HIS   B 1 92  ? -5.291  14.516  34.406  1   38.454  ? 104 HIS   A CA   1 ? 2 
ATOM   3107 C C    . HIS   B 1 92  ? -6.622  13.81   34.173  1   38.56   ? 104 HIS   A C    1 ? 2 
ATOM   3108 O O    . HIS   B 1 92  ? -7.436  13.694  35.099  1   37.116  ? 104 HIS   A O    1 ? 2 
ATOM   3109 C CB   . HIS   B 1 92  ? -4.352  13.609  35.218  1   37.571  ? 104 HIS   A CB   1 ? 2 
ATOM   3110 C CG   . HIS   B 1 92  ? -2.954  14.087  35.284  1   39.933  ? 104 HIS   A CG   1 ? 2 
ATOM   3111 N ND1  . HIS   B 1 92  ? -1.983  13.402  35.955  1   41.558  ? 104 HIS   A ND1  1 ? 2 
ATOM   3112 C CD2  . HIS   B 1 92  ? -2.381  15.198  34.831  1   42.356  ? 104 HIS   A CD2  1 ? 2 
ATOM   3113 C CE1  . HIS   B 1 92  ? -0.836  14.048  35.846  1   45.216  ? 104 HIS   A CE1  1 ? 2 
ATOM   3114 N NE2  . HIS   B 1 92  ? -1.054  15.168  35.183  1   45.998  ? 104 HIS   A NE2  1 ? 2 
ATOM   3115 H H    . HIS   B 1 92  ? -5.835  15.69   35.982  1   40.006  ? 104 HIS   A H    1 c 2 
ATOM   3116 H HA   . HIS   B 1 92  ? -4.882  14.723  33.534  1   38.365  ? 104 HIS   A HA   1 c 2 
ATOM   3117 H HB2  . HIS   B 1 92  ? -4.704  13.531  36.132  1   38.71   ? 104 HIS   A HB2  1 c 2 
ATOM   3118 H HB3  . HIS   B 1 92  ? -4.361  12.711  34.82   1   38.112  ? 104 HIS   A HB3  1 c 2 
ATOM   3119 H HD1  . HIS   B 1 92  ? -2.044  12.729  36.438  0   30      ? 104 HIS   A HD1  1 c 2 
ATOM   3120 H HD2  . HIS   B 1 92  ? -2.797  15.875  34.336  1   41.646  ? 104 HIS   A HD2  1 c 2 
ATOM   3121 H HE1  . HIS   B 1 92  ? -0.015  13.779  36.222  1   46.637  ? 104 HIS   A HE1  1 c 2 
ATOM   3122 H HE2  . HIS   B 1 92  ? -0.452  15.842  34.907  0   30      ? 104 HIS   A HE2  1 c 2 
ATOM   3123 N N    . LEU   B 1 93  ? -6.795  13.301  32.938  1   36.156  ? 105 LEU   A N    1 ? 2 
ATOM   3124 C CA   . LEU   B 1 93  ? -7.977  12.58   32.514  1   36.3    ? 105 LEU   A CA   1 ? 2 
ATOM   3125 C C    . LEU   B 1 93  ? -7.526  11.238  31.944  1   38.459  ? 105 LEU   A C    1 ? 2 
ATOM   3126 O O    . LEU   B 1 93  ? -6.579  11.202  31.142  1   41.294  ? 105 LEU   A O    1 ? 2 
ATOM   3127 C CB   . LEU   B 1 93  ? -8.708  13.38   31.439  1   36.271  ? 105 LEU   A CB   1 ? 2 
ATOM   3128 C CG   . LEU   B 1 93  ? -9.421  14.682  31.807  1   39.662  ? 105 LEU   A CG   1 ? 2 
ATOM   3129 C CD1  . LEU   B 1 93  ? -10.114 15.269  30.591  1   40.533  ? 105 LEU   A CD1  1 ? 2 
ATOM   3130 C CD2  . LEU   B 1 93  ? -10.414 14.461  32.918  1   40.552  ? 105 LEU   A CD2  1 ? 2 
ATOM   3131 H H    . LEU   B 1 93  ? -6.126  13.417  32.327  1   36.845  ? 105 LEU   A H    1 c 2 
ATOM   3132 H HA   . LEU   B 1 93  ? -8.57   12.436  33.29   1   36.867  ? 105 LEU   A HA   1 c 2 
ATOM   3133 H HB2  . LEU   B 1 93  ? -8.059  13.585  30.727  1   36.888  ? 105 LEU   A HB2  1 c 2 
ATOM   3134 H HB3  . LEU   B 1 93  ? -9.373  12.783  31.024  1   36.756  ? 105 LEU   A HB3  1 c 2 
ATOM   3135 H HG   . LEU   B 1 93  ? -8.741  15.331  32.122  1   39.61   ? 105 LEU   A HG   1 c 2 
ATOM   3136 H HD11 . LEU   B 1 93  ? -9.467  15.394  29.877  1   40.3    ? 105 LEU   A HD11 1 c 2 
ATOM   3137 H HD12 . LEU   B 1 93  ? -10.509 16.126  30.824  1   40.684  ? 105 LEU   A HD12 1 c 2 
ATOM   3138 H HD13 . LEU   B 1 93  ? -10.813 14.663  30.291  1   40.175  ? 105 LEU   A HD13 1 c 2 
ATOM   3139 H HD21 . LEU   B 1 93  ? -9.944  14.224  33.734  1   40.644  ? 105 LEU   A HD21 1 c 2 
ATOM   3140 H HD22 . LEU   B 1 93  ? -11.021 13.742  32.674  1   40.308  ? 105 LEU   A HD22 1 c 2 
ATOM   3141 H HD23 . LEU   B 1 93  ? -10.923 15.276  33.064  1   40.696  ? 105 LEU   A HD23 1 c 2 
ATOM   3142 N N    . LEU   B 1 94  ? -8.11   10.143  32.451  1   40.112  ? 106 LEU   A N    1 ? 2 
ATOM   3143 C CA   . LEU   B 1 94  ? -7.934  8.807   31.874  1   39.921  ? 106 LEU   A CA   1 ? 2 
ATOM   3144 C C    . LEU   B 1 94  ? -9.27   8.382   31.284  1   40.704  ? 106 LEU   A C    1 ? 2 
ATOM   3145 O O    . LEU   B 1 94  ? -10.338 8.393   31.946  1   42.53   ? 106 LEU   A O    1 ? 2 
ATOM   3146 C CB   . LEU   B 1 94  ? -7.438  7.806   32.904  1   41.462  ? 106 LEU   A CB   1 ? 2 
ATOM   3147 C CG   . LEU   B 1 94  ? -7.218  6.369   32.42   1   45.926  ? 106 LEU   A CG   1 ? 2 
ATOM   3148 C CD1  . LEU   B 1 94  ? -5.959  6.345   31.571  1   46.763  ? 106 LEU   A CD1  1 ? 2 
ATOM   3149 C CD2  . LEU   B 1 94  ? -7.186  5.401   33.601  1   46.715  ? 106 LEU   A CD2  1 ? 2 
ATOM   3150 H H    . LEU   B 1 94  ? -8.64   10.228  33.191  1   39.712  ? 106 LEU   A H    1 c 2 
ATOM   3151 H HA   . LEU   B 1 94  ? -7.27   8.87    31.142  1   40.272  ? 106 LEU   A HA   1 c 2 
ATOM   3152 H HB2  . LEU   B 1 94  ? -6.589  8.143   33.272  1   42.367  ? 106 LEU   A HB2  1 c 2 
ATOM   3153 H HB3  . LEU   B 1 94  ? -8.086  7.786   33.645  1   42.294  ? 106 LEU   A HB3  1 c 2 
ATOM   3154 H HG   . LEU   B 1 94  ? -7.981  6.115   31.841  1   45.031  ? 106 LEU   A HG   1 c 2 
ATOM   3155 H HD11 . LEU   B 1 94  ? -6.081  6.912   30.791  1   45.554  ? 106 LEU   A HD11 1 c 2 
ATOM   3156 H HD12 . LEU   B 1 94  ? -5.78   5.435   31.283  1   48.001  ? 106 LEU   A HD12 1 c 2 
ATOM   3157 H HD13 . LEU   B 1 94  ? -5.207  6.672   32.094  1   46.912  ? 106 LEU   A HD13 1 c 2 
ATOM   3158 H HD21 . LEU   B 1 94  ? -8.033  5.439   34.075  1   47.014  ? 106 LEU   A HD21 1 c 2 
ATOM   3159 H HD22 . LEU   B 1 94  ? -6.466  5.649   34.205  1   47.628  ? 106 LEU   A HD22 1 c 2 
ATOM   3160 H HD23 . LEU   B 1 94  ? -7.037  4.497   33.276  1   48.508  ? 106 LEU   A HD23 1 c 2 
ATOM   3161 N N    . ILE   B 1 95  ? -9.204  8.034   30.008  1   38.23   ? 107 ILE   A N    1 ? 2 
ATOM   3162 C CA   . ILE   B 1 95  ? -10.386 8.045   29.164  1   37.01   ? 107 ILE   A CA   1 ? 2 
ATOM   3163 C C    . ILE   B 1 95  ? -10.507 6.694   28.467  1   43.072  ? 107 ILE   A C    1 ? 2 
ATOM   3164 O O    . ILE   B 1 95  ? -9.614  6.319   27.693  1   37.844  ? 107 ILE   A O    1 ? 2 
ATOM   3165 C CB   . ILE   B 1 95  ? -10.277 9.184   28.146  1   36.13   ? 107 ILE   A CB   1 ? 2 
ATOM   3166 C CG1  . ILE   B 1 95  ? -10.088 10.548  28.833  1   37.377  ? 107 ILE   A CG1  1 ? 2 
ATOM   3167 C CG2  . ILE   B 1 95  ? -11.496 9.173   27.24   1   36.391  ? 107 ILE   A CG2  1 ? 2 
ATOM   3168 C CD1  . ILE   B 1 95  ? -9.542  11.621  27.918  1   40.023  ? 107 ILE   A CD1  1 ? 2 
ATOM   3169 H H    . ILE   B 1 95  ? -8.405  7.773   29.647  1   39.004  ? 107 ILE   A H    1 c 2 
ATOM   3170 H HA   . ILE   B 1 95  ? -11.175 8.193   29.718  1   38.052  ? 107 ILE   A HA   1 c 2 
ATOM   3171 H HB   . ILE   B 1 95  ? -9.488  9.016   27.593  1   36.759  ? 107 ILE   A HB   1 c 2 
ATOM   3172 H HG12 . ILE   B 1 95  ? -10.951 10.845  29.186  1   37.389  ? 107 ILE   A HG12 1 c 2 
ATOM   3173 H HG13 . ILE   B 1 95  ? -9.476  10.443  29.588  1   37.48   ? 107 ILE   A HG13 1 c 2 
ATOM   3174 H HG21 . ILE   B 1 95  ? -11.508 9.981   26.699  1   36.178  ? 107 ILE   A HG21 1 c 2 
ATOM   3175 H HG22 . ILE   B 1 95  ? -12.303 9.136   27.78   1   36.61   ? 107 ILE   A HG22 1 c 2 
ATOM   3176 H HG23 . ILE   B 1 95  ? -11.464 8.397   26.655  1   37.362  ? 107 ILE   A HG23 1 c 2 
ATOM   3177 H HD11 . ILE   B 1 95  ? -8.741  11.287  27.471  1   39.423  ? 107 ILE   A HD11 1 c 2 
ATOM   3178 H HD12 . ILE   B 1 95  ? -9.315  12.414  28.44   1   38.798  ? 107 ILE   A HD12 1 c 2 
ATOM   3179 H HD13 . ILE   B 1 95  ? -10.212 11.855  27.248  1   39.244  ? 107 ILE   A HD13 1 c 2 
ATOM   3180 N N    . LYS   B 1 96  ? -11.617 6.008   28.723  1   42.781  ? 108 LYS   A N    1 ? 2 
ATOM   3181 C CA   . LYS   B 1 96  ? -11.963 4.78    28.012  1   47.528  ? 108 LYS   A CA   1 ? 2 
ATOM   3182 C C    . LYS   B 1 96  ? -12.459 5.115   26.611  1   43.015  ? 108 LYS   A C    1 ? 2 
ATOM   3183 O O    . LYS   B 1 96  ? -12.958 6.207   26.374  1   42.873  ? 108 LYS   A O    1 ? 2 
ATOM   3184 C CB   . LYS   B 1 96  ? -13.031 4.04    28.832  1   47.356  ? 108 LYS   A CB   1 ? 2 
ATOM   3185 C CG   . LYS   B 1 96  ? -12.488 3.419   30.113  1   58.128  ? 108 LYS   A CG   1 ? 2 
ATOM   3186 C CD   . LYS   B 1 96  ? -11.274 2.473   29.979  1   63.41   ? 108 LYS   A CD   1 ? 2 
ATOM   3187 C CE   . LYS   B 1 96  ? -10.807 1.984   31.345  1   65.44   ? 108 LYS   A CE   1 ? 2 
ATOM   3188 N NZ   . LYS   B 1 96  ? -10.229 3.094   32.137  1   62.074  ? 108 LYS   A NZ   1 ? 2 
ATOM   3189 H H    . LYS   B 1 96  ? -12.186 6.312   29.37   1   43.392  ? 108 LYS   A H    1 c 2 
ATOM   3190 H HA   . LYS   B 1 96  ? -11.15  4.223   27.938  1   46.638  ? 108 LYS   A HA   1 c 2 
ATOM   3191 H HB2  . LYS   B 1 96  ? -13.747 4.669   29.067  1   49.064  ? 108 LYS   A HB2  1 c 2 
ATOM   3192 H HB3  . LYS   B 1 96  ? -13.424 3.331   28.282  1   51.251  ? 108 LYS   A HB3  1 c 2 
ATOM   3193 H HG2  . LYS   B 1 96  ? -12.245 4.15    30.72   1   55.113  ? 108 LYS   A HG2  1 c 2 
ATOM   3194 H HG3  . LYS   B 1 96  ? -13.219 2.922   30.54   1   57.706  ? 108 LYS   A HG3  1 c 2 
ATOM   3195 H HD2  . LYS   B 1 96  ? -11.523 1.701   29.426  1   64.304  ? 108 LYS   A HD2  1 c 2 
ATOM   3196 H HD3  . LYS   B 1 96  ? -10.535 2.945   29.538  1   61.416  ? 108 LYS   A HD3  1 c 2 
ATOM   3197 H HE2  . LYS   B 1 96  ? -11.561 1.605   31.831  1   66.101  ? 108 LYS   A HE2  1 c 2 
ATOM   3198 H HE3  . LYS   B 1 96  ? -10.135 1.287   31.233  1   66.46   ? 108 LYS   A HE3  1 c 2 
ATOM   3199 H HZ1  . LYS   B 1 96  ? -10.89  3.621   32.462  1   61.585  ? 108 LYS   A HZ1  1 c 2 
ATOM   3200 H HZ2  . LYS   B 1 96  ? -9.677  3.592   31.618  1   61.308  ? 108 LYS   A HZ2  1 c 2 
ATOM   3201 H HZ3  . LYS   B 1 96  ? -9.756  2.756   32.831  1   63.503  ? 108 LYS   A HZ3  1 c 2 
ATOM   3202 N N    . PRO   B 1 97  ? -12.413 4.14    25.667  1   49.402  ? 109 PRO   A N    1 ? 2 
ATOM   3203 C CA   . PRO   B 1 97  ? -12.708 4.409   24.253  1   45.875  ? 109 PRO   A CA   1 ? 2 
ATOM   3204 C C    . PRO   B 1 97  ? -14.094 4.976   23.979  1   43.713  ? 109 PRO   A C    1 ? 2 
ATOM   3205 O O    . PRO   B 1 97  ? -14.267 5.736   23.044  1   46.233  ? 109 PRO   A O    1 ? 2 
ATOM   3206 C CB   . PRO   B 1 97  ? -12.489 3.079   23.532  1   48.73   ? 109 PRO   A CB   1 ? 2 
ATOM   3207 C CG   . PRO   B 1 97  ? -12.196 2.041   24.593  1   54.543  ? 109 PRO   A CG   1 ? 2 
ATOM   3208 C CD   . PRO   B 1 97  ? -11.937 2.767   25.911  1   51.222  ? 109 PRO   A CD   1 ? 2 
ATOM   3209 H HA   . PRO   B 1 97  ? -12.043 5.047   23.917  1   45.169  ? 109 PRO   A HA   1 c 2 
ATOM   3210 H HB2  . PRO   B 1 97  ? -13.284 2.83    23.021  1   50.952  ? 109 PRO   A HB2  1 c 2 
ATOM   3211 H HB3  . PRO   B 1 97  ? -11.741 3.149   22.908  1   49.807  ? 109 PRO   A HB3  1 c 2 
ATOM   3212 H HG2  . PRO   B 1 97  ? -12.957 1.434   24.69   1   54.721  ? 109 PRO   A HG2  1 c 2 
ATOM   3213 H HG3  . PRO   B 1 97  ? -11.414 1.512   24.343  1   54.183  ? 109 PRO   A HG3  1 c 2 
ATOM   3214 H HD2  . PRO   B 1 97  ? -12.433 2.352   26.641  1   52.257  ? 109 PRO   A HD2  1 c 2 
ATOM   3215 H HD3  . PRO   B 1 97  ? -10.985 2.767   26.131  1   51.216  ? 109 PRO   A HD3  1 c 2 
ATOM   3216 N N    . GLU   B 1 98  ? -15.076 4.617   24.801  1   46.523  ? 110 GLU   A N    1 ? 2 
ATOM   3217 C CA   . GLU   B 1 98  ? -16.438 5.097   24.636  1   50.093  ? 110 GLU   A CA   1 ? 2 
ATOM   3218 C C    . GLU   B 1 98  ? -16.541 6.632   24.72   1   51.127  ? 110 GLU   A C    1 ? 2 
ATOM   3219 O O    . GLU   B 1 98  ? -17.493 7.208   24.193  1   50.823  ? 110 GLU   A O    1 ? 2 
ATOM   3220 C CB   . GLU   B 1 98  ? -17.306 4.405   25.693  1   52.377  ? 110 GLU   A CB   1 ? 2 
ATOM   3221 C CG   . GLU   B 1 98  ? -17.371 2.887   25.55   1   60.3    ? 110 GLU   A CG   1 ? 2 
ATOM   3222 C CD   . GLU   B 1 98  ? -16.205 2.006   26.033  1   62.702  ? 110 GLU   A CD   1 ? 2 
ATOM   3223 O OE1  . GLU   B 1 98  ? -15.343 2.45    26.811  1   52.507  ? 110 GLU   A OE1  1 ? 2 
ATOM   3224 O OE2  . GLU   B 1 98  ? -16.142 0.818   25.607  1   63.456  ? 110 GLU   A OE2  1 ? 2 
ATOM   3225 H H    . GLU   B 1 98  ? -14.887 4.063   25.502  1   47.116  ? 110 GLU   A H    1 c 2 
ATOM   3226 H HA   . GLU   B 1 98  ? -16.756 4.814   23.741  1   51.613  ? 110 GLU   A HA   1 c 2 
ATOM   3227 H HB2  . GLU   B 1 98  ? -16.953 4.623   26.581  1   52.065  ? 110 GLU   A HB2  1 c 2 
ATOM   3228 H HB3  . GLU   B 1 98  ? -18.215 4.766   25.638  1   53.893  ? 110 GLU   A HB3  1 c 2 
ATOM   3229 H HG2  . GLU   B 1 98  ? -18.179 2.579   26.014  1   60.909  ? 110 GLU   A HG2  1 c 2 
ATOM   3230 H HG3  . GLU   B 1 98  ? -17.515 2.683   24.601  1   60.645  ? 110 GLU   A HG3  1 c 2 
ATOM   3231 N N    . TYR   B 1 99  ? -15.575 7.302   25.381  1   49.347  ? 111 TYR   A N    1 ? 2 
ATOM   3232 C CA   . TYR   B 1 99  ? -15.568 8.755   25.487  1   47.78   ? 111 TYR   A CA   1 ? 2 
ATOM   3233 C C    . TYR   B 1 99  ? -14.454 9.353   24.619  1   44.569  ? 111 TYR   A C    1 ? 2 
ATOM   3234 O O    . TYR   B 1 99  ? -14.065 10.513  24.782  1   40.536  ? 111 TYR   A O    1 ? 2 
ATOM   3235 C CB   . TYR   B 1 99  ? -15.488 9.104   26.982  1   45.743  ? 111 TYR   A CB   1 ? 2 
ATOM   3236 C CG   . TYR   B 1 99  ? -16.729 8.628   27.73   1   47.118  ? 111 TYR   A CG   1 ? 2 
ATOM   3237 C CD1  . TYR   B 1 99  ? -16.815 7.344   28.255  1   46.577  ? 111 TYR   A CD1  1 ? 2 
ATOM   3238 C CD2  . TYR   B 1 99  ? -17.835 9.463   27.894  1   53.366  ? 111 TYR   A CD2  1 ? 2 
ATOM   3239 C CE1  . TYR   B 1 99  ? -17.955 6.914   28.921  1   48.3    ? 111 TYR   A CE1  1 ? 2 
ATOM   3240 C CE2  . TYR   B 1 99  ? -18.974 9.042   28.558  1   52.16   ? 111 TYR   A CE2  1 ? 2 
ATOM   3241 C CZ   . TYR   B 1 99  ? -19.041 7.756   29.055  1   51.882  ? 111 TYR   A CZ   1 ? 2 
ATOM   3242 O OH   . TYR   B 1 99  ? -20.178 7.396   29.723  1   52.323  ? 111 TYR   A OH   1 ? 2 
ATOM   3243 H H    . TYR   B 1 99  ? -14.907 6.833   25.792  1   48.788  ? 111 TYR   A H    1 c 2 
ATOM   3244 H HA   . TYR   B 1 99  ? -16.436 9.094   25.144  1   48.032  ? 111 TYR   A HA   1 c 2 
ATOM   3245 H HB2  . TYR   B 1 99  ? -14.691 8.676   27.368  1   45.443  ? 111 TYR   A HB2  1 c 2 
ATOM   3246 H HB3  . TYR   B 1 99  ? -15.403 10.078  27.079  1   45.138  ? 111 TYR   A HB3  1 c 2 
ATOM   3247 H HD1  . TYR   B 1 99  ? -16.087 6.752   28.155  1   46.954  ? 111 TYR   A HD1  1 c 2 
ATOM   3248 H HD2  . TYR   B 1 99  ? -17.806 10.338  27.543  1   50.75   ? 111 TYR   A HD2  1 c 2 
ATOM   3249 H HE1  . TYR   B 1 99  ? -17.994 6.04    29.27   1   50.167  ? 111 TYR   A HE1  1 c 2 
ATOM   3250 H HE2  . TYR   B 1 99  ? -19.708 9.624   28.656  1   53.095  ? 111 TYR   A HE2  1 c 2 
ATOM   3251 H HH   . TYR   B 1 99  ? -20.136 6.519   30.065  0   30      ? 111 TYR   A HH   1 c 2 
ATOM   3252 N N    . ALA   B 1 100 ? -13.916 8.553   23.694  1   44.111  ? 112 ALA   A N    1 ? 2 
ATOM   3253 C CA   . ALA   B 1 100 ? -12.833 8.996   22.831  1   39.985  ? 112 ALA   A CA   1 ? 2 
ATOM   3254 C C    . ALA   B 1 100 ? -13.158 8.563   21.402  1   43.597  ? 112 ALA   A C    1 ? 2 
ATOM   3255 O O    . ALA   B 1 100 ? -14.098 9.125   20.832  1   44.938  ? 112 ALA   A O    1 ? 2 
ATOM   3256 C CB   . ALA   B 1 100 ? -11.488 8.492   23.351  1   36.345  ? 112 ALA   A CB   1 ? 2 
ATOM   3257 H H    . ALA   B 1 100 ? -14.239 7.705   23.588  1   44.609  ? 112 ALA   A H    1 c 2 
ATOM   3258 H HA   . ALA   B 1 100 ? -12.819 9.99    22.844  1   39.804  ? 112 ALA   A HA   1 c 2 
ATOM   3259 H HB1  . ALA   B 1 100 ? -11.272 8.941   24.185  1   36.089  ? 112 ALA   A HB1  1 c 2 
ATOM   3260 H HB2  . ALA   B 1 100 ? -11.534 7.534   23.505  1   37.991  ? 112 ALA   A HB2  1 c 2 
ATOM   3261 H HB3  . ALA   B 1 100 ? -10.793 8.68    22.697  1   37.53   ? 112 ALA   A HB3  1 c 2 
ATOM   3262 N N    . TYR   B 1 101 ? -12.438 7.565   20.838  1   44.769  ? 113 TYR   A N    1 ? 2 
ATOM   3263 C CA   . TYR   B 1 101 ? -12.645 7.235   19.418  1   47.575  ? 113 TYR   A CA   1 ? 2 
ATOM   3264 C C    . TYR   B 1 101 ? -13.285 5.869   19.181  1   49.359  ? 113 TYR   A C    1 ? 2 
ATOM   3265 O O    . TYR   B 1 101 ? -13.407 5.408   18.036  1   50.713  ? 113 TYR   A O    1 ? 2 
ATOM   3266 C CB   . TYR   B 1 101 ? -11.304 7.336   18.686  1   47.663  ? 113 TYR   A CB   1 ? 2 
ATOM   3267 C CG   . TYR   B 1 101 ? -10.749 8.752   18.744  1   46.579  ? 113 TYR   A CG   1 ? 2 
ATOM   3268 C CD1  . TYR   B 1 101 ? -11.231 9.727   17.882  1   47.929  ? 113 TYR   A CD1  1 ? 2 
ATOM   3269 C CD2  . TYR   B 1 101 ? -9.806  9.142   19.69   1   48.027  ? 113 TYR   A CD2  1 ? 2 
ATOM   3270 C CE1  . TYR   B 1 101 ? -10.746 11.023  17.898  1   47.762  ? 113 TYR   A CE1  1 ? 2 
ATOM   3271 C CE2  . TYR   B 1 101 ? -9.316  10.442  19.725  1   46.433  ? 113 TYR   A CE2  1 ? 2 
ATOM   3272 C CZ   . TYR   B 1 101 ? -9.775  11.385  18.811  1   48.323  ? 113 TYR   A CZ   1 ? 2 
ATOM   3273 O OH   . TYR   B 1 101 ? -9.349  12.689  18.802  1   45.039  ? 113 TYR   A OH   1 ? 2 
ATOM   3274 H H    . TYR   B 1 101 ? -11.827 7.093   21.325  1   44.433  ? 113 TYR   A H    1 c 2 
ATOM   3275 H HA   . TYR   B 1 101 ? -13.25  7.921   19.029  1   47.576  ? 113 TYR   A HA   1 c 2 
ATOM   3276 H HB2  . TYR   B 1 101 ? -10.664 6.718   19.105  1   47.714  ? 113 TYR   A HB2  1 c 2 
ATOM   3277 H HB3  . TYR   B 1 101 ? -11.43  7.075   17.747  1   49.624  ? 113 TYR   A HB3  1 c 2 
ATOM   3278 H HD1  . TYR   B 1 101 ? -11.871 9.487   17.231  1   49.445  ? 113 TYR   A HD1  1 c 2 
ATOM   3279 H HD2  . TYR   B 1 101 ? -9.468  8.504   20.299  1   46.647  ? 113 TYR   A HD2  1 c 2 
ATOM   3280 H HE1  . TYR   B 1 101 ? -11.072 11.657  17.282  1   49.152  ? 113 TYR   A HE1  1 c 2 
ATOM   3281 H HE2  . TYR   B 1 101 ? -8.659  10.682  20.356  1   45.875  ? 113 TYR   A HE2  1 c 2 
ATOM   3282 H HH   . TYR   B 1 101 ? -9.688  13.154  18.235  0   30      ? 113 TYR   A HH   1 c 2 
ATOM   3283 N N    . GLY   B 1 102 ? -13.674 5.21    20.263  1   48.846  ? 114 GLY   A N    1 ? 2 
ATOM   3284 C CA   . GLY   B 1 102 ? -14.653 4.14    20.159  1   53.424  ? 114 GLY   A CA   1 ? 2 
ATOM   3285 C C    . GLY   B 1 102 ? -14.051 2.88    19.545  1   55.216  ? 114 GLY   A C    1 ? 2 
ATOM   3286 O O    . GLY   B 1 102 ? -12.831 2.739   19.402  1   50.94   ? 114 GLY   A O    1 ? 2 
ATOM   3287 H H    . GLY   B 1 102 ? -13.323 5.414   21.081  1   47.83   ? 114 GLY   A H    1 c 2 
ATOM   3288 H HA2  . GLY   B 1 102 ? -15     3.934   21.059  1   52.242  ? 114 GLY   A HA2  1 c 2 
ATOM   3289 H HA3  . GLY   B 1 102 ? -15.409 4.447   19.605  1   53.632  ? 114 GLY   A HA3  1 c 2 
ATOM   3290 N N    . SER   B 1 103 ? -14.939 1.967   19.149  1   58.474  ? 115 SER   A N    1 ? 2 
ATOM   3291 C CA   . SER   B 1 103 ? -14.464 0.721   18.587  1   60.924  ? 115 SER   A CA   1 ? 2 
ATOM   3292 C C    . SER   B 1 103 ? -13.907 0.965   17.179  1   58.187  ? 115 SER   A C    1 ? 2 
ATOM   3293 O O    . SER   B 1 103 ? -13.002 0.25    16.745  1   62.237  ? 115 SER   A O    1 ? 2 
ATOM   3294 C CB   . SER   B 1 103 ? -15.552 -0.318  18.665  1   65.388  ? 115 SER   A CB   1 ? 2 
ATOM   3295 O OG   . SER   B 1 103 ? -16.732 0.129   18.013  1   65.932  ? 115 SER   A OG   1 ? 2 
ATOM   3296 H H    . SER   B 1 103 ? -15.837 2.12    19.226  1   58.684  ? 115 SER   A H    1 c 2 
ATOM   3297 H HA   . SER   B 1 103 ? -13.713 0.407   19.149  1   59.884  ? 115 SER   A HA   1 c 2 
ATOM   3298 H HB2  . SER   B 1 103 ? -15.241 -1.143  18.246  1   67.355  ? 115 SER   A HB2  1 c 2 
ATOM   3299 H HB3  . SER   B 1 103 ? -15.751 -0.508  19.602  1   64.309  ? 115 SER   A HB3  1 c 2 
ATOM   3300 H HG   . SER   B 1 103 ? -17.302 -0.349  18.193  0   30      ? 115 SER   A HG   1 c 2 
ATOM   3301 N N    . ALA   B 1 104 ? -14.396 2.013   16.501  1   56.049  ? 116 ALA   A N    1 ? 2 
ATOM   3302 C CA   . ALA   B 1 104 ? -13.921 2.401   15.189  1   59.026  ? 116 ALA   A CA   1 ? 2 
ATOM   3303 C C    . ALA   B 1 104 ? -12.511 2.954   15.227  1   56.46   ? 116 ALA   A C    1 ? 2 
ATOM   3304 O O    . ALA   B 1 104 ? -11.822 2.876   14.228  1   56.369  ? 116 ALA   A O    1 ? 2 
ATOM   3305 C CB   . ALA   B 1 104 ? -14.839 3.409   14.533  1   60.318  ? 116 ALA   A CB   1 ? 2 
ATOM   3306 H H    . ALA   B 1 104 ? -15.07  2.503   16.876  1   55.811  ? 116 ALA   A H    1 c 2 
ATOM   3307 H HA   . ALA   B 1 104 ? -13.905 1.58    14.623  1   61.496  ? 116 ALA   A HA   1 c 2 
ATOM   3308 H HB1  . ALA   B 1 104 ? -15.737 3.043   14.473  1   61.582  ? 116 ALA   A HB1  1 c 2 
ATOM   3309 H HB2  . ALA   B 1 104 ? -14.86  4.225   15.062  1   57.645  ? 116 ALA   A HB2  1 c 2 
ATOM   3310 H HB3  . ALA   B 1 104 ? -14.515 3.614   13.64   1   61.322  ? 116 ALA   A HB3  1 c 2 
ATOM   3311 N N    . GLY   B 1 105 ? -12.157 3.662   16.303  1   52.541  ? 117 GLY   A N    1 ? 2 
ATOM   3312 C CA   . GLY   B 1 105 ? -10.873 4.344   16.396  1   49.037  ? 117 GLY   A CA   1 ? 2 
ATOM   3313 C C    . GLY   B 1 105 ? -10.793 5.447   15.353  1   50.474  ? 117 GLY   A C    1 ? 2 
ATOM   3314 O O    . GLY   B 1 105 ? -11.806 5.892   14.841  1   49.587  ? 117 GLY   A O    1 ? 2 
ATOM   3315 H H    . GLY   B 1 105 ? -12.739 3.73    17.005  1   51.132  ? 117 GLY   A H    1 c 2 
ATOM   3316 H HA2  . GLY   B 1 105 ? -10.772 4.729   17.297  1   47.609  ? 117 GLY   A HA2  1 c 2 
ATOM   3317 H HA3  . GLY   B 1 105 ? -10.146 3.694   16.253  1   50.923  ? 117 GLY   A HA3  1 c 2 
ATOM   3318 N N    . SER   B 1 106 ? -9.576  5.881   15.058  1   51.523  ? 118 SER   A N    1 ? 2 
ATOM   3319 C CA   . SER   B 1 106 ? -9.35   7.037   14.221  1   52.846  ? 118 SER   A CA   1 ? 2 
ATOM   3320 C C    . SER   B 1 106 ? -7.973  6.9     13.604  1   55.26   ? 118 SER   A C    1 ? 2 
ATOM   3321 O O    . SER   B 1 106 ? -7.047  7.633   13.93   1   51.883  ? 118 SER   A O    1 ? 2 
ATOM   3322 C CB   . SER   B 1 106 ? -9.45   8.345   14.985  1   50.715  ? 118 SER   A CB   1 ? 2 
ATOM   3323 O OG   . SER   B 1 106 ? -9.439  9.371   14.004  1   54.921  ? 118 SER   A OG   1 ? 2 
ATOM   3324 H H    . SER   B 1 106 ? -8.852  5.438   15.398  1   51.359  ? 118 SER   A H    1 c 2 
ATOM   3325 H HA   . SER   B 1 106 ? -10.023 7.04    13.492  1   54.538  ? 118 SER   A HA   1 c 2 
ATOM   3326 H HB2  . SER   B 1 106 ? -10.281 8.374   15.495  1   50.189  ? 118 SER   A HB2  1 c 2 
ATOM   3327 H HB3  . SER   B 1 106 ? -8.691  8.445   15.591  1   49.938  ? 118 SER   A HB3  1 c 2 
ATOM   3328 H HG   . SER   B 1 106 ? -9.37   10.137  14.337  0   30      ? 118 SER   A HG   1 c 2 
ATOM   3329 N N    . LEU   B 1 107 ? -7.866  5.905   12.728  1   59.197  ? 119 LEU   A N    1 ? 2 
ATOM   3330 C CA   . LEU   B 1 107 ? -6.614  5.546   12.107  1   60.496  ? 119 LEU   A CA   1 ? 2 
ATOM   3331 C C    . LEU   B 1 107 ? -6.155  6.654   11.164  1   61.965  ? 119 LEU   A C    1 ? 2 
ATOM   3332 O O    . LEU   B 1 107 ? -6.981  7.314   10.53   1   61.238  ? 119 LEU   A O    1 ? 2 
ATOM   3333 C CB   . LEU   B 1 107 ? -6.788  4.223   11.349  1   64.842  ? 119 LEU   A CB   1 ? 2 
ATOM   3334 C CG   . LEU   B 1 107 ? -6.827  2.962   12.217  1   64.336  ? 119 LEU   A CG   1 ? 2 
ATOM   3335 C CD1  . LEU   B 1 107 ? -6.78   1.775   11.301  1   70.053  ? 119 LEU   A CD1  1 ? 2 
ATOM   3336 C CD2  . LEU   B 1 107 ? -5.706  2.873   13.23   1   62.922  ? 119 LEU   A CD2  1 ? 2 
ATOM   3337 H H    . LEU   B 1 107 ? -8.614  5.428   12.509  1   59.69   ? 119 LEU   A H    1 c 2 
ATOM   3338 H HA   . LEU   B 1 107 ? -5.942  5.433   12.821  1   59.658  ? 119 LEU   A HA   1 c 2 
ATOM   3339 H HB2  . LEU   B 1 107 ? -7.624  4.271   10.831  1   65.513  ? 119 LEU   A HB2  1 c 2 
ATOM   3340 H HB3  . LEU   B 1 107 ? -6.045  4.136   10.708  1   66.739  ? 119 LEU   A HB3  1 c 2 
ATOM   3341 H HG   . LEU   B 1 107 ? -7.689  2.949   12.706  1   63.358  ? 119 LEU   A HG   1 c 2 
ATOM   3342 H HD11 . LEU   B 1 107 ? -7.501  1.835   10.653  1   70.84   ? 119 LEU   A HD11 1 c 2 
ATOM   3343 H HD12 . LEU   B 1 107 ? -6.88   0.962   11.821  1   69.987  ? 119 LEU   A HD12 1 c 2 
ATOM   3344 H HD13 . LEU   B 1 107 ? -5.928  1.758   10.834  1   71.318  ? 119 LEU   A HD13 1 c 2 
ATOM   3345 H HD21 . LEU   B 1 107 ? -5.838  3.54    13.924  1   60.118  ? 119 LEU   A HD21 1 c 2 
ATOM   3346 H HD22 . LEU   B 1 107 ? -4.854  3.031   12.788  1   64.209  ? 119 LEU   A HD22 1 c 2 
ATOM   3347 H HD23 . LEU   B 1 107 ? -5.7    1.988   13.633  1   63.682  ? 119 LEU   A HD23 1 c 2 
ATOM   3348 N N    . PRO   B 1 108 ? -4.823  6.843   10.983  1   63.141  ? 120 PRO   A N    1 ? 2 
ATOM   3349 C CA   . PRO   B 1 108 ? -3.811  6.034   11.658  1   62.4    ? 120 PRO   A CA   1 ? 2 
ATOM   3350 C C    . PRO   B 1 108 ? -3.394  6.477   13.061  1   59.361  ? 120 PRO   A C    1 ? 2 
ATOM   3351 O O    . PRO   B 1 108 ? -2.637  5.765   13.684  1   62.189  ? 120 PRO   A O    1 ? 2 
ATOM   3352 C CB   . PRO   B 1 108 ? -2.597  6.175   10.749  1   66.933  ? 120 PRO   A CB   1 ? 2 
ATOM   3353 C CG   . PRO   B 1 108 ? -2.76   7.582   10.2    1   66.042  ? 120 PRO   A CG   1 ? 2 
ATOM   3354 C CD   . PRO   B 1 108 ? -4.245  7.817   10.05   1   64.38   ? 120 PRO   A CD   1 ? 2 
ATOM   3355 H HA   . PRO   B 1 108 ? -4.094  5.097   11.678  1   63.734  ? 120 PRO   A HA   1 c 2 
ATOM   3356 H HB2  . PRO   B 1 108 ? -1.764  6.085   11.251  1   66.333  ? 120 PRO   A HB2  1 c 2 
ATOM   3357 H HB3  . PRO   B 1 108 ? -2.617  5.512   10.031  1   69.198  ? 120 PRO   A HB3  1 c 2 
ATOM   3358 H HG2  . PRO   B 1 108 ? -2.373  8.237   10.815  1   64.359  ? 120 PRO   A HG2  1 c 2 
ATOM   3359 H HG3  . PRO   B 1 108 ? -2.313  7.667   9.334   1   68.928  ? 120 PRO   A HG3  1 c 2 
ATOM   3360 H HD2  . PRO   B 1 108 ? -4.49   8.729   10.303  1   63.095  ? 120 PRO   A HD2  1 c 2 
ATOM   3361 H HD3  . PRO   B 1 108 ? -4.544  7.643   9.137   1   67.124  ? 120 PRO   A HD3  1 c 2 
ATOM   3362 N N    . LYS   B 1 109 ? -3.877  7.595   13.588  1   59.303  ? 121 LYS   A N    1 ? 2 
ATOM   3363 C CA   . LYS   B 1 109 ? -3.432  8.045   14.917  1   59.211  ? 121 LYS   A CA   1 ? 2 
ATOM   3364 C C    . LYS   B 1 109 ? -3.905  7.132   16.055  1   56.478  ? 121 LYS   A C    1 ? 2 
ATOM   3365 O O    . LYS   B 1 109 ? -3.149  6.768   16.94   1   57.686  ? 121 LYS   A O    1 ? 2 
ATOM   3366 C CB   . LYS   B 1 109 ? -3.822  9.502   15.192  1   58.119  ? 121 LYS   A CB   1 ? 2 
ATOM   3367 C CG   . LYS   B 1 109 ? -2.925  10.451  14.393  1   65.73   ? 121 LYS   A CG   1 ? 2 
ATOM   3368 C CD   . LYS   B 1 109 ? -3.091  11.942  14.669  1   67.582  ? 121 LYS   A CD   1 ? 2 
ATOM   3369 C CE   . LYS   B 1 109 ? -2.253  12.669  13.666  1   72.056  ? 121 LYS   A CE   1 ? 2 
ATOM   3370 N NZ   . LYS   B 1 109 ? -2.619  14.079  13.612  1   74.579  ? 121 LYS   A NZ   1 ? 2 
ATOM   3371 H H    . LYS   B 1 109 ? -4.49   8.094   13.13   1   59.287  ? 121 LYS   A H    1 c 2 
ATOM   3372 H HA   . LYS   B 1 109 ? -2.441  8.018   14.917  1   59.777  ? 121 LYS   A HA   1 c 2 
ATOM   3373 H HB2  . LYS   B 1 109 ? -4.757  9.649   14.936  1   58.687  ? 121 LYS   A HB2  1 c 2 
ATOM   3374 H HB3  . LYS   B 1 109 ? -3.727  9.697   16.149  1   57.155  ? 121 LYS   A HB3  1 c 2 
ATOM   3375 H HG2  . LYS   B 1 109 ? -1.99   10.206  14.569  1   65.777  ? 121 LYS   A HG2  1 c 2 
ATOM   3376 H HG3  . LYS   B 1 109 ? -3.09   10.289  13.438  1   67.075  ? 121 LYS   A HG3  1 c 2 
ATOM   3377 H HD2  . LYS   B 1 109 ? -4.033  12.203  14.568  1   66.502  ? 121 LYS   A HD2  1 c 2 
ATOM   3378 H HD3  . LYS   B 1 109 ? -2.783  12.156  15.577  1   65.624  ? 121 LYS   A HD3  1 c 2 
ATOM   3379 H HE2  . LYS   B 1 109 ? -1.313  12.592  13.906  1   72.936  ? 121 LYS   A HE2  1 c 2 
ATOM   3380 H HE3  . LYS   B 1 109 ? -2.376  12.28   12.781  1   74.192  ? 121 LYS   A HE3  1 c 2 
ATOM   3381 H HZ1  . LYS   B 1 109 ? -2.505  14.456  14.427  1   72.048  ? 121 LYS   A HZ1  1 c 2 
ATOM   3382 H HZ2  . LYS   B 1 109 ? -3.485  14.164  13.362  1   73.364  ? 121 LYS   A HZ2  1 c 2 
ATOM   3383 H HZ3  . LYS   B 1 109 ? -2.094  14.508  13.011  1   75.872  ? 121 LYS   A HZ3  1 c 2 
ATOM   3384 N N    . ILE   B 1 110 ? -5.176  6.76    16.065  1   54.61   ? 122 ILE   A N    1 ? 2 
ATOM   3385 C CA   . ILE   B 1 110 ? -5.769  6.104   17.215  1   52.253  ? 122 ILE   A CA   1 ? 2 
ATOM   3386 C C    . ILE   B 1 110 ? -6.252  4.709   16.83   1   51.952  ? 122 ILE   A C    1 ? 2 
ATOM   3387 O O    . ILE   B 1 110 ? -7.124  4.608   15.976  1   52.233  ? 122 ILE   A O    1 ? 2 
ATOM   3388 C CB   . ILE   B 1 110 ? -6.966  6.934   17.708  1   49.289  ? 122 ILE   A CB   1 ? 2 
ATOM   3389 C CG1  . ILE   B 1 110 ? -6.638  8.411   17.724  1   53.606  ? 122 ILE   A CG1  1 ? 2 
ATOM   3390 C CG2  . ILE   B 1 110 ? -7.45   6.417   19.049  1   49.071  ? 122 ILE   A CG2  1 ? 2 
ATOM   3391 C CD1  . ILE   B 1 110 ? -5.499  8.788   18.668  1   53.142  ? 122 ILE   A CD1  1 ? 2 
ATOM   3392 H H    . ILE   B 1 110 ? -5.697  6.92    15.331  1   55.612  ? 122 ILE   A H    1 c 2 
ATOM   3393 H HA   . ILE   B 1 110 ? -5.111  6.038   17.931  1   51.225  ? 122 ILE   A HA   1 c 2 
ATOM   3394 H HB   . ILE   B 1 110 ? -7.693  6.808   17.066  1   51.547  ? 122 ILE   A HB   1 c 2 
ATOM   3395 H HG12 . ILE   B 1 110 ? -6.403  8.694   16.817  1   53.806  ? 122 ILE   A HG12 1 c 2 
ATOM   3396 H HG13 . ILE   B 1 110 ? -7.44   8.905   17.99   1   51.203  ? 122 ILE   A HG13 1 c 2 
ATOM   3397 H HG21 . ILE   B 1 110 ? -8.132  7.011   19.399  1   47.268  ? 122 ILE   A HG21 1 c 2 
ATOM   3398 H HG22 . ILE   B 1 110 ? -6.705  6.379   19.672  1   48.162  ? 122 ILE   A HG22 1 c 2 
ATOM   3399 H HG23 . ILE   B 1 110 ? -7.825  5.527   18.941  1   49.772  ? 122 ILE   A HG23 1 c 2 
ATOM   3400 H HD11 . ILE   B 1 110 ? -5.75   8.572   19.586  1   51.499  ? 122 ILE   A HD11 1 c 2 
ATOM   3401 H HD12 . ILE   B 1 110 ? -5.333  9.746   18.596  1   52.432  ? 122 ILE   A HD12 1 c 2 
ATOM   3402 H HD13 . ILE   B 1 110 ? -4.688  8.302   18.433  1   54.159  ? 122 ILE   A HD13 1 c 2 
ATOM   3403 N N    . PRO   B 1 111 ? -5.784  3.612   17.478  1   53.042  ? 123 PRO   A N    1 ? 2 
ATOM   3404 C CA   . PRO   B 1 111 ? -6.298  2.288   17.155  1   55.672  ? 123 PRO   A CA   1 ? 2 
ATOM   3405 C C    . PRO   B 1 111 ? -7.718  2.098   17.669  1   52.281  ? 123 PRO   A C    1 ? 2 
ATOM   3406 O O    . PRO   B 1 111 ? -8.22   2.911   18.449  1   50.308  ? 123 PRO   A O    1 ? 2 
ATOM   3407 C CB   . PRO   B 1 111 ? -5.281  1.32    17.767  1   57.364  ? 123 PRO   A CB   1 ? 2 
ATOM   3408 C CG   . PRO   B 1 111 ? -4.441  2.123   18.752  1   53.878  ? 123 PRO   A CG   1 ? 2 
ATOM   3409 C CD   . PRO   B 1 111 ? -4.743  3.581   18.521  1   52.819  ? 123 PRO   A CD   1 ? 2 
ATOM   3410 H HA   . PRO   B 1 111 ? -6.294  2.173   16.181  1   57.131  ? 123 PRO   A HA   1 c 2 
ATOM   3411 H HB2  . PRO   B 1 111 ? -5.738  0.587   18.226  1   57.719  ? 123 PRO   A HB2  1 c 2 
ATOM   3412 H HB3  . PRO   B 1 111 ? -4.715  0.933   17.071  1   59.535  ? 123 PRO   A HB3  1 c 2 
ATOM   3413 H HG2  . PRO   B 1 111 ? -4.663  1.875   19.671  1   53.535  ? 123 PRO   A HG2  1 c 2 
ATOM   3414 H HG3  . PRO   B 1 111 ? -3.489  1.95    18.607  1   55.946  ? 123 PRO   A HG3  1 c 2 
ATOM   3415 H HD2  . PRO   B 1 111 ? -5.07   4.002   19.34   1   50.169  ? 123 PRO   A HD2  1 c 2 
ATOM   3416 H HD3  . PRO   B 1 111 ? -3.945  4.056   18.218  1   52.684  ? 123 PRO   A HD3  1 c 2 
ATOM   3417 N N    . SER   B 1 112 ? -8.38   1.046   17.19   1   53.087  ? 124 SER   A N    1 ? 2 
ATOM   3418 C CA   . SER   B 1 112 ? -9.653  0.62    17.76   1   54.946  ? 124 SER   A CA   1 ? 2 
ATOM   3419 C C    . SER   B 1 112 ? -9.533  0.473   19.28   1   52.63   ? 124 SER   A C    1 ? 2 
ATOM   3420 O O    . SER   B 1 112 ? -8.556  -0.069  19.778  1   55.502  ? 124 SER   A O    1 ? 2 
ATOM   3421 C CB   . SER   B 1 112 ? -10.113 -0.667  17.127  1   57.605  ? 124 SER   A CB   1 ? 2 
ATOM   3422 O OG   . SER   B 1 112 ? -11.167 -1.265  17.874  1   57.268  ? 124 SER   A OG   1 ? 2 
ATOM   3423 H H    . SER   B 1 112 ? -8.031  0.577   16.487  1   56.346  ? 124 SER   A H    1 c 2 
ATOM   3424 H HA   . SER   B 1 112 ? -10.325 1.321   17.566  1   53.026  ? 124 SER   A HA   1 c 2 
ATOM   3425 H HB2  . SER   B 1 112 ? -10.421 -0.487  16.219  1   58.848  ? 124 SER   A HB2  1 c 2 
ATOM   3426 H HB3  . SER   B 1 112 ? -9.362  -1.287  17.076  1   59.405  ? 124 SER   A HB3  1 c 2 
ATOM   3427 H HG   . SER   B 1 112 ? -11.459 -1.945  17.611  0   30      ? 124 SER   A HG   1 c 2 
ATOM   3428 N N    . ASN   B 1 113 ? -10.544 0.941   19.997  1   54.543  ? 125 ASN   A N    1 ? 2 
ATOM   3429 C CA   . ASN   B 1 113 ? -10.724 0.665   21.414  1   54.34   ? 125 ASN   A CA   1 ? 2 
ATOM   3430 C C    . ASN   B 1 113 ? -9.566  1.216   22.251  1   52.087  ? 125 ASN   A C    1 ? 2 
ATOM   3431 O O    . ASN   B 1 113 ? -9.155  0.571   23.212  1   51.782  ? 125 ASN   A O    1 ? 2 
ATOM   3432 C CB   . ASN   B 1 113 ? -10.955 -0.829  21.647  1   59.197  ? 125 ASN   A CB   1 ? 2 
ATOM   3433 C CG   . ASN   B 1 113 ? -12.385 -1.223  21.381  1   63.913  ? 125 ASN   A CG   1 ? 2 
ATOM   3434 O OD1  . ASN   B 1 113 ? -13.284 -0.381  21.358  1   66.72   ? 125 ASN   A OD1  1 ? 2 
ATOM   3435 N ND2  . ASN   B 1 113 ? -12.616 -2.501  21.152  1   73.949  ? 125 ASN   A ND2  1 ? 2 
ATOM   3436 H H    . ASN   B 1 113 ? -11.163 1.47    19.582  1   53.154  ? 125 ASN   A H    1 c 2 
ATOM   3437 H HA   . ASN   B 1 113 ? -11.539 1.132   21.703  1   53.304  ? 125 ASN   A HA   1 c 2 
ATOM   3438 H HB2  . ASN   B 1 113 ? -10.366 -1.345  21.062  1   61.402  ? 125 ASN   A HB2  1 c 2 
ATOM   3439 H HB3  . ASN   B 1 113 ? -10.732 -1.051  22.572  1   59.181  ? 125 ASN   A HB3  1 c 2 
ATOM   3440 H HD21 . ASN   B 1 113 ? -13.418 -2.762  20.875  1   73.336  ? 125 ASN   A HD21 1 c 2 
ATOM   3441 H HD22 . ASN   B 1 113 ? -11.972 -3.098  21.276  1   73.191  ? 125 ASN   A HD22 1 c 2 
ATOM   3442 N N    . ALA   B 1 114 ? -9.032  2.402   21.902  1   49.015  ? 126 ALA   A N    1 ? 2 
ATOM   3443 C CA   . ALA   B 1 114 ? -7.875  2.937   22.625  1   47.23   ? 126 ALA   A CA   1 ? 2 
ATOM   3444 C C    . ALA   B 1 114 ? -8.338  3.684   23.875  1   41.695  ? 126 ALA   A C    1 ? 2 
ATOM   3445 O O    . ALA   B 1 114 ? -9.296  4.437   23.829  1   39.127  ? 126 ALA   A O    1 ? 2 
ATOM   3446 C CB   . ALA   B 1 114 ? -7.042  3.85    21.75   1   45.076  ? 126 ALA   A CB   1 ? 2 
ATOM   3447 H H    . ALA   B 1 114 ? -9.393  2.884   21.214  1   48.914  ? 126 ALA   A H    1 c 2 
ATOM   3448 H HA   . ALA   B 1 114 ? -7.309  2.169   22.913  1   47.942  ? 126 ALA   A HA   1 c 2 
ATOM   3449 H HB1  . ALA   B 1 114 ? -6.705  3.352   20.986  1   47.431  ? 126 ALA   A HB1  1 c 2 
ATOM   3450 H HB2  . ALA   B 1 114 ? -7.589  4.589   21.435  1   44.449  ? 126 ALA   A HB2  1 c 2 
ATOM   3451 H HB3  . ALA   B 1 114 ? -6.293  4.199   22.261  1   44.85   ? 126 ALA   A HB3  1 c 2 
ATOM   3452 N N    . THR   B 1 115 ? -7.61   3.47    24.974  1   48.378  ? 127 THR   A N    1 ? 2 
ATOM   3453 C CA   . THR   B 1 115 ? -7.632  4.333   26.155  1   43.687  ? 127 THR   A CA   1 ? 2 
ATOM   3454 C C    . THR   B 1 115 ? -6.627  5.458   25.962  1   43.756  ? 127 THR   A C    1 ? 2 
ATOM   3455 O O    . THR   B 1 115 ? -5.498  5.225   25.523  1   43.458  ? 127 THR   A O    1 ? 2 
ATOM   3456 C CB   . THR   B 1 115 ? -7.293  3.496   27.391  1   44.242  ? 127 THR   A CB   1 ? 2 
ATOM   3457 O OG1  . THR   B 1 115 ? -8.379  2.59    27.476  1   44.502  ? 127 THR   A OG1  1 ? 2 
ATOM   3458 C CG2  . THR   B 1 115 ? -7.305  4.283   28.705  1   45.868  ? 127 THR   A CG2  1 ? 2 
ATOM   3459 H H    . THR   B 1 115 ? -7.064  2.738   24.992  1   47.586  ? 127 THR   A H    1 c 2 
ATOM   3460 H HA   . THR   B 1 115 ? -8.53   4.709   26.257  1   43.229  ? 127 THR   A HA   1 c 2 
ATOM   3461 H HB   . THR   B 1 115 ? -6.446  3.004   27.273  1   46.098  ? 127 THR   A HB   1 c 2 
ATOM   3462 H HG1  . THR   B 1 115 ? -9.142  3.16    27.625  0   30      ? 127 THR   A HG1  1 c 2 
ATOM   3463 H HG21 . THR   B 1 115 ? -7.061  3.693   29.438  1   46.065  ? 127 THR   A HG21 1 c 2 
ATOM   3464 H HG22 . THR   B 1 115 ? -8.194  4.64    28.862  1   43.923  ? 127 THR   A HG22 1 c 2 
ATOM   3465 H HG23 . THR   B 1 115 ? -6.667  5.014   28.655  1   44.053  ? 127 THR   A HG23 1 c 2 
ATOM   3466 N N    . LEU   B 1 116 ? -7.021  6.687   26.354  1   39.426  ? 128 LEU   A N    1 ? 2 
ATOM   3467 C CA   . LEU   B 1 116 ? -6.172  7.852   26.21   1   39.805  ? 128 LEU   A CA   1 ? 2 
ATOM   3468 C C    . LEU   B 1 116 ? -5.937  8.471   27.592  1   38.914  ? 128 LEU   A C    1 ? 2 
ATOM   3469 O O    . LEU   B 1 116 ? -6.801  8.396   28.474  1   38.673  ? 128 LEU   A O    1 ? 2 
ATOM   3470 C CB   . LEU   B 1 116 ? -6.778  8.924   25.316  1   42.07   ? 128 LEU   A CB   1 ? 2 
ATOM   3471 C CG   . LEU   B 1 116 ? -7.307  8.529   23.929  1   51.184  ? 128 LEU   A CG   1 ? 2 
ATOM   3472 C CD1  . LEU   B 1 116 ? -7.398  9.77    23.042  1   52.919  ? 128 LEU   A CD1  1 ? 2 
ATOM   3473 C CD2  . LEU   B 1 116 ? -6.498  7.488   23.264  1   47.13   ? 128 LEU   A CD2  1 ? 2 
ATOM   3474 H H    . LEU   B 1 116 ? -7.85   6.793   26.724  1   39.615  ? 128 LEU   A H    1 c 2 
ATOM   3475 H HA   . LEU   B 1 116 ? -5.301  7.567   25.835  1   41.197  ? 128 LEU   A HA   1 c 2 
ATOM   3476 H HB2  . LEU   B 1 116 ? -7.517  9.347   25.811  1   41.999  ? 128 LEU   A HB2  1 c 2 
ATOM   3477 H HB3  . LEU   B 1 116 ? -6.099  9.627   25.192  1   42.94   ? 128 LEU   A HB3  1 c 2 
ATOM   3478 H HG   . LEU   B 1 116 ? -8.225  8.171   24.044  1   48.609  ? 128 LEU   A HG   1 c 2 
ATOM   3479 H HD11 . LEU   B 1 116 ? -7.952  10.44   23.477  1   51.352  ? 128 LEU   A HD11 1 c 2 
ATOM   3480 H HD12 . LEU   B 1 116 ? -7.793  9.531   22.188  1   53.077  ? 128 LEU   A HD12 1 c 2 
ATOM   3481 H HD13 . LEU   B 1 116 ? -6.508  10.132  22.896  1   52.573  ? 128 LEU   A HD13 1 c 2 
ATOM   3482 H HD21 . LEU   B 1 116 ? -6.715  6.619   23.637  1   49.224  ? 128 LEU   A HD21 1 c 2 
ATOM   3483 H HD22 . LEU   B 1 116 ? -5.555  7.674   23.403  1   48.982  ? 128 LEU   A HD22 1 c 2 
ATOM   3484 H HD23 . LEU   B 1 116 ? -6.69   7.485   22.311  1   49.632  ? 128 LEU   A HD23 1 c 2 
ATOM   3485 N N    . PHE   B 1 117 ? -4.774  9.095   27.741  1   39.34   ? 129 PHE   A N    1 ? 2 
ATOM   3486 C CA   . PHE   B 1 117 ? -4.464  9.929   28.887  1   38.066  ? 129 PHE   A CA   1 ? 2 
ATOM   3487 C C    . PHE   B 1 117 ? -4.161  11.335  28.385  1   39.876  ? 129 PHE   A C    1 ? 2 
ATOM   3488 O O    . PHE   B 1 117 ? -3.399  11.505  27.411  1   40.241  ? 129 PHE   A O    1 ? 2 
ATOM   3489 C CB   . PHE   B 1 117 ? -3.267  9.342   29.633  1   41.75   ? 129 PHE   A CB   1 ? 2 
ATOM   3490 C CG   . PHE   B 1 117 ? -2.7    10.252  30.718  1   48.338  ? 129 PHE   A CG   1 ? 2 
ATOM   3491 C CD1  . PHE   B 1 117 ? -1.702  11.183  30.417  1   49.5    ? 129 PHE   A CD1  1 ? 2 
ATOM   3492 C CD2  . PHE   B 1 117 ? -3.186  10.202  32.02   1   46.556  ? 129 PHE   A CD2  1 ? 2 
ATOM   3493 C CE1  . PHE   B 1 117 ? -1.185  12.01   31.409  1   51.867  ? 129 PHE   A CE1  1 ? 2 
ATOM   3494 C CE2  . PHE   B 1 117 ? -2.643  11.008  33.019  1   47.366  ? 129 PHE   A CE2  1 ? 2 
ATOM   3495 C CZ   . PHE   B 1 117 ? -1.679  11.931  32.703  1   52.679  ? 129 PHE   A CZ   1 ? 2 
ATOM   3496 H H    . PHE   B 1 117 ? -4.136  8.997   27.093  1   39.972  ? 129 PHE   A H    1 c 2 
ATOM   3497 H HA   . PHE   B 1 117 ? -5.247  9.956   29.495  1   38.309  ? 129 PHE   A HA   1 c 2 
ATOM   3498 H HB2  . PHE   B 1 117 ? -3.542  8.492   30.043  1   43.081  ? 129 PHE   A HB2  1 c 2 
ATOM   3499 H HB3  . PHE   B 1 117 ? -2.559  9.146   28.98   1   43.571  ? 129 PHE   A HB3  1 c 2 
ATOM   3500 H HD1  . PHE   B 1 117 ? -1.369  11.242  29.536  1   50.119  ? 129 PHE   A HD1  1 c 2 
ATOM   3501 H HD2  . PHE   B 1 117 ? -3.851  9.57    32.243  1   46.856  ? 129 PHE   A HD2  1 c 2 
ATOM   3502 H HE1  . PHE   B 1 117 ? -0.509  12.634  31.197  1   52.358  ? 129 PHE   A HE1  1 c 2 
ATOM   3503 H HE2  . PHE   B 1 117 ? -2.986  10.965  33.898  1   48.466  ? 129 PHE   A HE2  1 c 2 
ATOM   3504 H HZ   . PHE   B 1 117 ? -1.323  12.488  33.377  1   51.857  ? 129 PHE   A HZ   1 c 2 
ATOM   3505 N N    . PHE   B 1 118 ? -4.657  12.339  29.136  1   37.945  ? 130 PHE   A N    1 ? 2 
ATOM   3506 C CA   . PHE   B 1 118 ? -4.275  13.723  28.898  1   37.427  ? 130 PHE   A CA   1 ? 2 
ATOM   3507 C C    . PHE   B 1 118 ? -3.946  14.437  30.191  1   39.463  ? 130 PHE   A C    1 ? 2 
ATOM   3508 O O    . PHE   B 1 118 ? -4.577  14.179  31.224  1   38.243  ? 130 PHE   A O    1 ? 2 
ATOM   3509 C CB   . PHE   B 1 118 ? -5.355  14.62   28.295  1   36.308  ? 130 PHE   A CB   1 ? 2 
ATOM   3510 C CG   . PHE   B 1 118 ? -5.771  14.215  26.897  1   38.52   ? 130 PHE   A CG   1 ? 2 
ATOM   3511 C CD1  . PHE   B 1 118 ? -6.657  13.169  26.706  1   39.023  ? 130 PHE   A CD1  1 ? 2 
ATOM   3512 C CD2  . PHE   B 1 118 ? -5.236  14.867  25.784  1   40.642  ? 130 PHE   A CD2  1 ? 2 
ATOM   3513 C CE1  . PHE   B 1 118 ? -7.027  12.786  25.435  1   41.205  ? 130 PHE   A CE1  1 ? 2 
ATOM   3514 C CE2  . PHE   B 1 118 ? -5.634  14.489  24.507  1   41.203  ? 130 PHE   A CE2  1 ? 2 
ATOM   3515 C CZ   . PHE   B 1 118 ? -6.495  13.435  24.337  1   40.045  ? 130 PHE   A CZ   1 ? 2 
ATOM   3516 H H    . PHE   B 1 118 ? -5.245  12.153  29.81   1   37.567  ? 130 PHE   A H    1 c 2 
ATOM   3517 H HA   . PHE   B 1 118 ? -3.478  13.739  28.308  1   38.727  ? 130 PHE   A HA   1 c 2 
ATOM   3518 H HB2  . PHE   B 1 118 ? -6.144  14.597  28.88   1   36.267  ? 130 PHE   A HB2  1 c 2 
ATOM   3519 H HB3  . PHE   B 1 118 ? -5.02   15.544  28.271  1   37.447  ? 130 PHE   A HB3  1 c 2 
ATOM   3520 H HD1  . PHE   B 1 118 ? -7.008  12.715  27.455  1   38.727  ? 130 PHE   A HD1  1 c 2 
ATOM   3521 H HD2  . PHE   B 1 118 ? -4.635  15.585  25.902  1   41.05   ? 130 PHE   A HD2  1 c 2 
ATOM   3522 H HE1  . PHE   B 1 118 ? -7.633  12.072  25.315  1   40.215  ? 130 PHE   A HE1  1 c 2 
ATOM   3523 H HE2  . PHE   B 1 118 ? -5.272  14.928  23.754  1   42.041  ? 130 PHE   A HE2  1 c 2 
ATOM   3524 H HZ   . PHE   B 1 118 ? -6.763  13.183  23.469  1   41.285  ? 130 PHE   A HZ   1 c 2 
ATOM   3525 N N    . GLU   B 1 119 ? -2.987  15.348  30.076  1   40.758  ? 131 GLU   A N    1 ? 2 
ATOM   3526 C CA   . GLU   B 1 119 ? -2.788  16.387  31.063  1   46.753  ? 131 GLU   A CA   1 ? 2 
ATOM   3527 C C    . GLU   B 1 119 ? -3.251  17.669  30.401  1   47.147  ? 131 GLU   A C    1 ? 2 
ATOM   3528 O O    . GLU   B 1 119 ? -2.777  18      29.314  1   46.732  ? 131 GLU   A O    1 ? 2 
ATOM   3529 C CB   . GLU   B 1 119 ? -1.335  16.504  31.5    1   47.097  ? 131 GLU   A CB   1 ? 2 
ATOM   3530 C CG   . GLU   B 1 119 ? -1.092  17.609  32.517  1   53.053  ? 131 GLU   A CG   1 ? 2 
ATOM   3531 C CD   . GLU   B 1 119 ? 0.352   17.65   32.965  1   53.246  ? 131 GLU   A CD   1 ? 2 
ATOM   3532 O OE1  . GLU   B 1 119 ? 0.633   17.107  34.04   1   50.465  ? 131 GLU   A OE1  1 ? 2 
ATOM   3533 O OE2  . GLU   B 1 119 ? 1.17    18.254  32.236  1   56.92   ? 131 GLU   A OE2  1 ? 2 
ATOM   3534 H H    . GLU   B 1 119 ? -2.43   15.321  29.352  1   42.458  ? 131 GLU   A H    1 c 2 
ATOM   3535 H HA   . GLU   B 1 119 ? -3.356  16.197  31.849  1   44.761  ? 131 GLU   A HA   1 c 2 
ATOM   3536 H HB2  . GLU   B 1 119 ? -1.052  15.648  31.886  1   48.602  ? 131 GLU   A HB2  1 c 2 
ATOM   3537 H HB3  . GLU   B 1 119 ? -0.781  16.672  30.709  1   49.229  ? 131 GLU   A HB3  1 c 2 
ATOM   3538 H HG2  . GLU   B 1 119 ? -1.324  18.475  32.121  1   51.636  ? 131 GLU   A HG2  1 c 2 
ATOM   3539 H HG3  . GLU   B 1 119 ? -1.664  17.467  33.299  1   50.726  ? 131 GLU   A HG3  1 c 2 
ATOM   3540 N N    . ILE   B 1 120 ? -4.168  18.378  31.069  1   47.021  ? 132 ILE   A N    1 ? 2 
ATOM   3541 C CA   . ILE   B 1 120 ? -4.778  19.564  30.489  1   46.683  ? 132 ILE   A CA   1 ? 2 
ATOM   3542 C C    . ILE   B 1 120 ? -4.565  20.736  31.44   1   47.152  ? 132 ILE   A C    1 ? 2 
ATOM   3543 O O    . ILE   B 1 120 ? -4.857  20.639  32.632  1   42.912  ? 132 ILE   A O    1 ? 2 
ATOM   3544 C CB   . ILE   B 1 120 ? -6.277  19.369  30.196  1   44.234  ? 132 ILE   A CB   1 ? 2 
ATOM   3545 C CG1  . ILE   B 1 120 ? -6.56   18.084  29.408  1   42.778  ? 132 ILE   A CG1  1 ? 2 
ATOM   3546 C CG2  . ILE   B 1 120 ? -6.822  20.64   29.522  1   45.69   ? 132 ILE   A CG2  1 ? 2 
ATOM   3547 C CD1  . ILE   B 1 120 ? -8.023  17.861  29.04   1   42.115  ? 132 ILE   A CD1  1 ? 2 
ATOM   3548 H H    . ILE   B 1 120 ? -4.418  18.119  31.909  1   46.45   ? 132 ILE   A H    1 c 2 
ATOM   3549 H HA   . ILE   B 1 120 ? -4.328  19.763  29.646  1   47.022  ? 132 ILE   A HA   1 c 2 
ATOM   3550 H HB   . ILE   B 1 120 ? -6.73   19.281  31.059  1   44.153  ? 132 ILE   A HB   1 c 2 
ATOM   3551 H HG12 . ILE   B 1 120 ? -6.031  18.102  28.585  1   43.268  ? 132 ILE   A HG12 1 c 2 
ATOM   3552 H HG13 . ILE   B 1 120 ? -6.256  17.32   29.939  1   42.326  ? 132 ILE   A HG13 1 c 2 
ATOM   3553 H HG21 . ILE   B 1 120 ? -7.77   20.532  29.339  1   45.21   ? 132 ILE   A HG21 1 c 2 
ATOM   3554 H HG22 . ILE   B 1 120 ? -6.348  20.793  28.687  1   46.275  ? 132 ILE   A HG22 1 c 2 
ATOM   3555 H HG23 . ILE   B 1 120 ? -6.694  21.403  30.109  1   46.728  ? 132 ILE   A HG23 1 c 2 
ATOM   3556 H HD11 . ILE   B 1 120 ? -8.583  17.986  29.83   1   41.992  ? 132 ILE   A HD11 1 c 2 
ATOM   3557 H HD12 . ILE   B 1 120 ? -8.137  16.953  28.702  1   41.472  ? 132 ILE   A HD12 1 c 2 
ATOM   3558 H HD13 . ILE   B 1 120 ? -8.29   18.497  28.35   1   42.8    ? 132 ILE   A HD13 1 c 2 
ATOM   3559 N N    . GLU   B 1 121 ? -4.011  21.813  30.87   1   47.302  ? 133 GLU   A N    1 ? 2 
ATOM   3560 C CA   . GLU   B 1 121 ? -3.936  23.094  31.55   1   48.224  ? 133 GLU   A CA   1 ? 2 
ATOM   3561 C C    . GLU   B 1 121 ? -4.982  24.046  30.953  1   50.442  ? 133 GLU   A C    1 ? 2 
ATOM   3562 O O    . GLU   B 1 121 ? -4.886  24.411  29.767  1   52.695  ? 133 GLU   A O    1 ? 2 
ATOM   3563 C CB   . GLU   B 1 121 ? -2.536  23.668  31.402  1   49.048  ? 133 GLU   A CB   1 ? 2 
ATOM   3564 C CG   . GLU   B 1 121 ? -2.445  25.052  32.033  1   53.86   ? 133 GLU   A CG   1 ? 2 
ATOM   3565 C CD   . GLU   B 1 121 ? -1.047  25.51   32.365  1   60.714  ? 133 GLU   A CD   1 ? 2 
ATOM   3566 O OE1  . GLU   B 1 121 ? -0.075  24.761  32.121  1   63.384  ? 133 GLU   A OE1  1 ? 2 
ATOM   3567 O OE2  . GLU   B 1 121 ? -0.961  26.627  32.901  1   61.962  ? 133 GLU   A OE2  1 ? 2 
ATOM   3568 H H    . GLU   B 1 121 ? -3.665  21.745  30.027  1   47.7    ? 133 GLU   A H    1 c 2 
ATOM   3569 H HA   . GLU   B 1 121 ? -4.129  22.958  32.51   1   48.18   ? 133 GLU   A HA   1 c 2 
ATOM   3570 H HB2  . GLU   B 1 121 ? -1.897  23.06   31.83   1   49.621  ? 133 GLU   A HB2  1 c 2 
ATOM   3571 H HB3  . GLU   B 1 121 ? -2.311  23.722  30.45   1   50.183  ? 133 GLU   A HB3  1 c 2 
ATOM   3572 H HG2  . GLU   B 1 121 ? -2.846  25.705  31.423  1   55.305  ? 133 GLU   A HG2  1 c 2 
ATOM   3573 H HG3  . GLU   B 1 121 ? -2.976  25.06   32.858  1   53.926  ? 133 GLU   A HG3  1 c 2 
ATOM   3574 N N    . LEU   B 1 122 ? -5.981  24.416  31.776  1   48.092  ? 134 LEU   A N    1 ? 2 
ATOM   3575 C CA   . LEU   B 1 122 ? -6.985  25.389  31.383  1   52.634  ? 134 LEU   A CA   1 ? 2 
ATOM   3576 C C    . LEU   B 1 122 ? -6.435  26.807  31.563  1   59.16   ? 134 LEU   A C    1 ? 2 
ATOM   3577 O O    . LEU   B 1 122 ? -6.372  27.325  32.677  1   65.356  ? 134 LEU   A O    1 ? 2 
ATOM   3578 C CB   . LEU   B 1 122 ? -8.301  25.208  32.137  1   51.38   ? 134 LEU   A CB   1 ? 2 
ATOM   3579 C CG   . LEU   B 1 122 ? -9.422  26.204  31.773  1   52.48   ? 134 LEU   A CG   1 ? 2 
ATOM   3580 C CD1  . LEU   B 1 122 ? -9.685  26.173  30.281  1   54.182  ? 134 LEU   A CD1  1 ? 2 
ATOM   3581 C CD2  . LEU   B 1 122 ? -10.719 25.937  32.495  1   50.037  ? 134 LEU   A CD2  1 ? 2 
ATOM   3582 H H    . LEU   B 1 122 ? -6.035  24.043  32.609  1   48.71   ? 134 LEU   A H    1 c 2 
ATOM   3583 H HA   . LEU   B 1 122 ? -7.161  25.255  30.419  1   52.15   ? 134 LEU   A HA   1 c 2 
ATOM   3584 H HB2  . LEU   B 1 122 ? -8.629  24.295  31.967  1   49.279  ? 134 LEU   A HB2  1 c 2 
ATOM   3585 H HB3  . LEU   B 1 122 ? -8.116  25.286  33.101  1   51.713  ? 134 LEU   A HB3  1 c 2 
ATOM   3586 H HG   . LEU   B 1 122 ? -9.119  27.117  32.015  1   54.872  ? 134 LEU   A HG   1 c 2 
ATOM   3587 H HD11 . LEU   B 1 122 ? -8.942  26.585  29.809  1   54.753  ? 134 LEU   A HD11 1 c 2 
ATOM   3588 H HD12 . LEU   B 1 122 ? -10.501 26.662  30.084  1   55.023  ? 134 LEU   A HD12 1 c 2 
ATOM   3589 H HD13 . LEU   B 1 122 ? -9.782  25.251  29.987  1   51.582  ? 134 LEU   A HD13 1 c 2 
ATOM   3590 H HD21 . LEU   B 1 122 ? -10.566 25.951  33.453  1   50.862  ? 134 LEU   A HD21 1 c 2 
ATOM   3591 H HD22 . LEU   B 1 122 ? -11.061 25.066  32.235  1   48.713  ? 134 LEU   A HD22 1 c 2 
ATOM   3592 H HD23 . LEU   B 1 122 ? -11.368 26.622  32.262  1   52.441  ? 134 LEU   A HD23 1 c 2 
ATOM   3593 N N    . LEU   B 1 123 ? -6.063  27.443  30.445  1   62.29   ? 135 LEU   A N    1 ? 2 
ATOM   3594 C CA   . LEU   B 1 123 ? -5.423  28.749  30.471  1   66.572  ? 135 LEU   A CA   1 ? 2 
ATOM   3595 C C    . LEU   B 1 123 ? -6.483  29.835  30.682  1   72.536  ? 135 LEU   A C    1 ? 2 
ATOM   3596 O O    . LEU   B 1 123 ? -6.365  30.652  31.6    1   72.452  ? 135 LEU   A O    1 ? 2 
ATOM   3597 C CB   . LEU   B 1 123 ? -4.67   28.962  29.158  1   67.441  ? 135 LEU   A CB   1 ? 2 
ATOM   3598 C CG   . LEU   B 1 123 ? -3.602  27.924  28.782  1   66.933  ? 135 LEU   A CG   1 ? 2 
ATOM   3599 C CD1  . LEU   B 1 123 ? -3.098  28.215  27.37   1   69.8    ? 135 LEU   A CD1  1 ? 2 
ATOM   3600 C CD2  . LEU   B 1 123 ? -2.419  27.867  29.751  1   69.393  ? 135 LEU   A CD2  1 ? 2 
ATOM   3601 H H    . LEU   B 1 123 ? -6.22   27.05   29.635  1   61.046  ? 135 LEU   A H    1 c 2 
ATOM   3602 H HA   . LEU   B 1 123 ? -4.782  28.774  31.226  1   67.445  ? 135 LEU   A HA   1 c 2 
ATOM   3603 H HB2  . LEU   B 1 123 ? -5.332  28.999  28.43   1   67.82   ? 135 LEU   A HB2  1 c 2 
ATOM   3604 H HB3  . LEU   B 1 123 ? -4.238  29.847  29.196  1   70.855  ? 135 LEU   A HB3  1 c 2 
ATOM   3605 H HG   . LEU   B 1 123 ? -4.031  27.03   28.772  1   64.397  ? 135 LEU   A HG   1 c 2 
ATOM   3606 H HD11 . LEU   B 1 123 ? -3.847  28.214  26.751  1   69.165  ? 135 LEU   A HD11 1 c 2 
ATOM   3607 H HD12 . LEU   B 1 123 ? -2.459  27.532  27.106  1   68.426  ? 135 LEU   A HD12 1 c 2 
ATOM   3608 H HD13 . LEU   B 1 123 ? -2.666  29.086  27.352  1   72.455  ? 135 LEU   A HD13 1 c 2 
ATOM   3609 H HD21 . LEU   B 1 123 ? -2.748  27.784  30.661  1   68.095  ? 135 LEU   A HD21 1 c 2 
ATOM   3610 H HD22 . LEU   B 1 123 ? -1.895  28.681  29.671  1   71.743  ? 135 LEU   A HD22 1 c 2 
ATOM   3611 H HD23 . LEU   B 1 123 ? -1.861  27.101  29.538  1   67.56   ? 135 LEU   A HD23 1 c 2 
ATOM   3612 N N    . ASP   B 1 124 ? -7.507  29.844  29.816  1   72.386  ? 136 ASP   A N    1 ? 2 
ATOM   3613 C CA   . ASP   B 1 124 ? -8.499  30.914  29.787  1   76.574  ? 136 ASP   A CA   1 ? 2 
ATOM   3614 C C    . ASP   B 1 124 ? -9.755  30.42   29.072  1   76.318  ? 136 ASP   A C    1 ? 2 
ATOM   3615 O O    . ASP   B 1 124 ? -9.711  29.414  28.349  1   70.545  ? 136 ASP   A O    1 ? 2 
ATOM   3616 C CB   . ASP   B 1 124 ? -7.963  32.162  29.101  1   79.953  ? 136 ASP   A CB   1 ? 2 
ATOM   3617 C CG   . ASP   B 1 124 ? -8.612  33.465  29.546  1   89.299  ? 136 ASP   A CG   1 ? 2 
ATOM   3618 O OD1  . ASP   B 1 124 ? -9.379  33.433  30.535  1   94.322  ? 136 ASP   A OD1  1 ? 2 
ATOM   3619 O OD2  . ASP   B 1 124 ? -8.356  34.5    28.897  1   91.192  ? 136 ASP   A OD2  1 ? 2 
ATOM   3620 H H    . ASP   B 1 124 ? -7.586  29.16   29.214  1   70.599  ? 136 ASP   A H    1 c 2 
ATOM   3621 H HA   . ASP   B 1 124 ? -8.735  31.138  30.715  1   76.947  ? 136 ASP   A HA   1 c 2 
ATOM   3622 H HB2  . ASP   B 1 124 ? -7      32.231  29.272  1   81.693  ? 136 ASP   A HB2  1 c 2 
ATOM   3623 H HB3  . ASP   B 1 124 ? -8.088  32.074  28.133  1   81.382  ? 136 ASP   A HB3  1 c 2 
ATOM   3624 N N    . PHE   B 1 125 ? -10.875 31.126  29.306  1   77.422  ? 137 PHE   A N    1 ? 2 
ATOM   3625 C CA   . PHE   B 1 125 ? -12.113 30.861  28.586  1   73.996  ? 137 PHE   A CA   1 ? 2 
ATOM   3626 C C    . PHE   B 1 125 ? -12.977 32.119  28.535  1   76.468  ? 137 PHE   A C    1 ? 2 
ATOM   3627 O O    . PHE   B 1 125 ? -13.121 32.812  29.535  1   79.601  ? 137 PHE   A O    1 ? 2 
ATOM   3628 C CB   . PHE   B 1 125 ? -12.925 29.705  29.173  1   67.242  ? 137 PHE   A CB   1 ? 2 
ATOM   3629 C CG   . PHE   B 1 125 ? -13.36  29.852  30.623  1   67.866  ? 137 PHE   A CG   1 ? 2 
ATOM   3630 C CD1  . PHE   B 1 125 ? -12.542 29.404  31.648  1   68.043  ? 137 PHE   A CD1  1 ? 2 
ATOM   3631 C CD2  . PHE   B 1 125 ? -14.605 30.366  30.959  1   71.604  ? 137 PHE   A CD2  1 ? 2 
ATOM   3632 C CE1  . PHE   B 1 125 ? -12.968 29.469  32.97   1   70.874  ? 137 PHE   A CE1  1 ? 2 
ATOM   3633 C CE2  . PHE   B 1 125 ? -15.019 30.442  32.287  1   73.638  ? 137 PHE   A CE2  1 ? 2 
ATOM   3634 C CZ   . PHE   B 1 125 ? -14.204 29.993  33.289  1   69.334  ? 137 PHE   A CZ   1 ? 2 
ATOM   3635 H H    . PHE   B 1 125 ? -10.866 31.785  29.938  1   79.008  ? 137 PHE   A H    1 c 2 
ATOM   3636 H HA   . PHE   B 1 125 ? -11.871 30.619  27.655  1   73.111  ? 137 PHE   A HA   1 c 2 
ATOM   3637 H HB2  . PHE   B 1 125 ? -13.728 29.584  28.618  1   68.417  ? 137 PHE   A HB2  1 c 2 
ATOM   3638 H HB3  . PHE   B 1 125 ? -12.391 28.884  29.09   1   65.248  ? 137 PHE   A HB3  1 c 2 
ATOM   3639 H HD1  . PHE   B 1 125 ? -11.702 29.024  31.443  1   66.48   ? 137 PHE   A HD1  1 c 2 
ATOM   3640 H HD2  . PHE   B 1 125 ? -15.182 30.664  30.275  1   73.301  ? 137 PHE   A HD2  1 c 2 
ATOM   3641 H HE1  . PHE   B 1 125 ? -12.394 29.173  33.658  1   68.259  ? 137 PHE   A HE1  1 c 2 
ATOM   3642 H HE2  . PHE   B 1 125 ? -15.864 30.807  32.495  1   74.826  ? 137 PHE   A HE2  1 c 2 
ATOM   3643 H HZ   . PHE   B 1 125 ? -14.474 30.062  34.19   1   71.586  ? 137 PHE   A HZ   1 c 2 
ATOM   3644 N N    . LYS   B 1 126 ? -13.567 32.37   27.358  1   77.247  ? 138 LYS   A N    1 ? 2 
ATOM   3645 C CA   . LYS   B 1 126 ? -14.391 33.54   27.087  1   81.208  ? 138 LYS   A CA   1 ? 2 
ATOM   3646 C C    . LYS   B 1 126 ? -15.755 33.074  26.582  1   81.094  ? 138 LYS   A C    1 ? 2 
ATOM   3647 O O    . LYS   B 1 126 ? -15.832 32.084  25.869  1   76.017  ? 138 LYS   A O    1 ? 2 
ATOM   3648 C CB   . LYS   B 1 126 ? -13.686 34.405  26.035  1   82.629  ? 138 LYS   A CB   1 ? 2 
ATOM   3649 H H    . LYS   B 1 126 ? -13.45  31.766  26.681  1   75.473  ? 138 LYS   A H    1 c 2 
ATOM   3650 H HA   . LYS   B 1 126 ? -14.51  34.055  27.926  1   82.635  ? 138 LYS   A HA   1 c 2 
ATOM   3651 H HB2  . LYS   B 1 126 ? -12.693 34.448  26.334  0   30      ? 138 LYS   A HB2  1 c 2 
ATOM   3652 H HB3  . LYS   B 1 126 ? -14.318 35.082  25.691  0   30      ? 138 LYS   A HB3  1 c 2 
ATOM   3653 N N    . GLY   B 1 127 ? -16.831 33.779  26.942  1   86.829  ? 139 GLY   A N    1 ? 2 
ATOM   3654 C CA   . GLY   B 1 127 ? -18.158 33.378  26.501  1   88.315  ? 139 GLY   A CA   1 ? 2 
ATOM   3655 C C    . GLY   B 1 127 ? -18.394 33.826  25.061  1   93.185  ? 139 GLY   A C    1 ? 2 
ATOM   3656 O O    . GLY   B 1 127 ? -18.155 34.991  24.767  1   98.56   ? 139 GLY   A O    1 ? 2 
ATOM   3657 H H    . GLY   B 1 127 ? -16.739 34.521  27.468  1   88.969  ? 139 GLY   A H    1 c 2 
ATOM   3658 H HA2  . GLY   B 1 127 ? -18.243 32.401  26.565  1   84.763  ? 139 GLY   A HA2  1 c 2 
ATOM   3659 H HA3  . GLY   B 1 127 ? -18.834 33.786  27.091  1   90.616  ? 139 GLY   A HA3  1 c 2 
ATOM   3660 N N    . GLU   B 1 128 ? -18.895 32.92   24.193  1   92.27   ? 140 GLU   A N    1 ? 2 
ATOM   3661 C CA   . GLU   B 1 128 ? -19.061 33.195  22.766  1   94.313  ? 140 GLU   A CA   1 ? 2 
ATOM   3662 C C    . GLU   B 1 128 ? -19.499 34.666  22.567  1   102.82  ? 140 GLU   A C    1 ? 2 
ATOM   3663 O O    . GLU   B 1 128 ? -20.305 35.171  23.397  1   105.492 ? 140 GLU   A O    1 ? 2 
ATOM   3664 C CB   . GLU   B 1 128 ? -20.006 32.213  22.06   1   90.599  ? 140 GLU   A CB   1 ? 2 
ATOM   3665 O OXT  . GLU   B 1 128 ? -18.986 35.279  21.606  1   106.268 ? 140 GLU   A OXT  1 ? 2 
ATOM   3666 H H    . GLU   B 1 128 ? -19.141 32.098  24.51   1   88.755  ? 140 GLU   A H    1 c 2 
ATOM   3667 H HA   . GLU   B 1 128 ? -18.175 33.089  22.342  1   93.212  ? 140 GLU   A HA   1 c 2 
ATOM   3668 H HB2  . GLU   B 1 128 ? -19.728 31.48   21.767  0   30      ? 140 GLU   A HB2  1 c 2 
ATOM   3669 H HB3  . GLU   B 1 128 ? -21.154 32.48   22.41   0   30      ? 140 GLU   A HB3  1 c 2 
HETATM 3670 C CAK  . A1IN3 C 2 .   ? -17.644 -7.324  12.131  1   45.422  ? 201 A1IN3 B CAK  1 ? 1 
HETATM 3671 C CAL  . A1IN3 C 2 .   ? -16.778 -8.447  11.764  1   47.742  ? 201 A1IN3 B CAL  1 ? 1 
HETATM 3672 C CAM  . A1IN3 C 2 .   ? -16.89  -8.712  10.236  1   45.321  ? 201 A1IN3 B CAM  1 ? 1 
HETATM 3673 C CAN  . A1IN3 C 2 .   ? -16.517 -7.429  9.542   1   43.12   ? 201 A1IN3 B CAN  1 ? 1 
HETATM 3674 C CAO  . A1IN3 C 2 .   ? -17.521 -6.322  9.87    1   42.193  ? 201 A1IN3 B CAO  1 ? 1 
HETATM 3675 C CAJ  . A1IN3 C 2 .   ? -17.339 -6.08   11.346  1   42.201  ? 201 A1IN3 B CAJ  1 ? 1 
HETATM 3676 C CAI  . A1IN3 C 2 .   ? -18.153 -4.855  11.761  1   42.405  ? 201 A1IN3 B CAI  1 ? 1 
HETATM 3677 C CAB  . A1IN3 C 2 .   ? -17.599 -3.626  11.237  1   41.24   ? 201 A1IN3 B CAB  1 ? 1 
HETATM 3678 O OAA  . A1IN3 C 2 .   ? -16.363 -3.481  11.087  1   39.705  ? 201 A1IN3 B OAA  1 ? 1 
HETATM 3679 N N    . A1IN3 C 2 .   ? -18.371 -2.568  10.871  1   41.602  ? 201 A1IN3 B N    1 ? 1 
HETATM 3680 C CAH  . A1IN3 C 2 .   ? -19.852 -2.503  11.199  1   44.136  ? 201 A1IN3 B CAH  1 ? 1 
HETATM 3681 C CAG  . A1IN3 C 2 .   ? -20.644 -1.797  10.247  1   44.123  ? 201 A1IN3 B CAG  1 ? 1 
HETATM 3682 C CAF  . A1IN3 C 2 .   ? -20.065 -0.456  10.1    1   43.056  ? 201 A1IN3 B CAF  1 ? 1 
HETATM 3683 C CB   . A1IN3 C 2 .   ? -18.658 -0.542  9.448   1   39.948  ? 201 A1IN3 B CB   1 ? 1 
HETATM 3684 C CA   . A1IN3 C 2 .   ? -17.739 -1.278  10.464  1   40.418  ? 201 A1IN3 B CA   1 ? 1 
HETATM 3685 C C    . A1IN3 C 2 .   ? -17.472 -0.406  11.582  1   43.038  ? 201 A1IN3 B C    1 ? 1 
HETATM 3686 O O    . A1IN3 C 2 .   ? -17.01  0.721   11.401  1   42.553  ? 201 A1IN3 B O    1 ? 1 
HETATM 3687 O OBC  . A1IN3 C 2 .   ? -17.616 -0.976  12.787  1   46.532  ? 201 A1IN3 B OBC  1 ? 1 
HETATM 3688 C CBB  . A1IN3 C 2 .   ? -17.326 -0.108  13.88   1   49.065  ? 201 A1IN3 B CBB  1 ? 1 
HETATM 3689 C CBA  . A1IN3 C 2 .   ? -18.007 -0.441  15.09   1   50.252  ? 201 A1IN3 B CBA  1 ? 1 
HETATM 3690 C CAZ  . A1IN3 C 2 .   ? -19.238 -1.126  15.009  1   54.129  ? 201 A1IN3 B CAZ  1 ? 1 
HETATM 3691 C CAY  . A1IN3 C 2 .   ? -19.732 -1.799  16.135  1   57.252  ? 201 A1IN3 B CAY  1 ? 1 
HETATM 3692 C CAX  . A1IN3 C 2 .   ? -18.991 -1.896  17.286  1   56.422  ? 201 A1IN3 B CAX  1 ? 1 
HETATM 3693 C CAW  . A1IN3 C 2 .   ? -19.328 -3.16   17.963  1   59.568  ? 201 A1IN3 B CAW  1 ? 1 
HETATM 3694 O OAV  . A1IN3 C 2 .   ? -18.523 -4.291  17.362  1   54.5    ? 201 A1IN3 B OAV  1 ? 1 
HETATM 3695 C CAU  . A1IN3 C 2 .   ? -18.528 -4.478  16.006  1   51.677  ? 201 A1IN3 B CAU  1 ? 1 
HETATM 3696 C CAR  . A1IN3 C 2 .   ? -17.335 -4.229  15.372  1   49.85   ? 201 A1IN3 B CAR  1 ? 1 
HETATM 3697 O OAS  . A1IN3 C 2 .   ? -16.375 -3.823  16.179  1   53.267  ? 201 A1IN3 B OAS  1 ? 1 
HETATM 3698 C CAT  . A1IN3 C 2 .   ? -15.21  -4.623  16.231  1   58.605  ? 201 A1IN3 B CAT  1 ? 1 
HETATM 3699 C CAQ  . A1IN3 C 2 .   ? -17.167 -4.327  13.996  1   46.141  ? 201 A1IN3 B CAQ  1 ? 1 
HETATM 3700 C CAP  . A1IN3 C 2 .   ? -18.267 -4.744  13.214  1   45.986  ? 201 A1IN3 B CAP  1 ? 1 
HETATM 3701 C CBI  . A1IN3 C 2 .   ? -19.497 -5.015  13.882  1   47.539  ? 201 A1IN3 B CBI  1 ? 1 
HETATM 3702 C CBF  . A1IN3 C 2 .   ? -19.62  -4.869  15.279  1   51.306  ? 201 A1IN3 B CBF  1 ? 1 
HETATM 3703 O OBG  . A1IN3 C 2 .   ? -20.727 -5.154  15.991  1   57.924  ? 201 A1IN3 B OBG  1 ? 1 
HETATM 3704 C CBH  . A1IN3 C 2 .   ? -21.989 -5.211  15.312  1   58.372  ? 201 A1IN3 B CBH  1 ? 1 
HETATM 3705 H HAK  . A1IN3 C 2 .   ? -17.558 -7.047  13.106  1   46.979  ? 201 A1IN3 B HAK  1 c 1 
HETATM 3706 H HB6  . A1IN3 C 2 .   ? -18.562 -7.817  11.888  1   47.62   ? 201 A1IN3 B HB6  1 c 1 
HETATM 3707 H HAL  . A1IN3 C 2 .   ? -17.093 -9.338  12.312  1   49.675  ? 201 A1IN3 B HAL  1 c 1 
HETATM 3708 H HB7  . A1IN3 C 2 .   ? -15.747 -8.214  12.019  1   45.955  ? 201 A1IN3 B HB7  1 c 1 
HETATM 3709 H HAM  . A1IN3 C 2 .   ? -17.91  -8.994  9.975   1   47.162  ? 201 A1IN3 B HAM  1 c 1 
HETATM 3710 H HB8  . A1IN3 C 2 .   ? -16.201 -9.505  9.946   1   46.05   ? 201 A1IN3 B HB8  1 c 1 
HETATM 3711 H HAN  . A1IN3 C 2 .   ? -16.518 -7.598  8.465   1   42.036  ? 201 A1IN3 B HAN  1 c 1 
HETATM 3712 H HB9  . A1IN3 C 2 .   ? -15.516 -7.128  9.851   1   41.707  ? 201 A1IN3 B HB9  1 c 1 
HETATM 3713 H HCA  . A1IN3 C 2 .   ? -17.315 -5.39   9.455   1   40.407  ? 201 A1IN3 B HCA  1 c 1 
HETATM 3714 H HAO  . A1IN3 C 2 .   ? -18.523 -6.637  9.835   1   43.684  ? 201 A1IN3 B HAO  1 c 1 
HETATM 3715 H HAJ  . A1IN3 C 2 .   ? -16.288 -5.856  11.526  1   41.361  ? 201 A1IN3 B HAJ  1 c 1 
HETATM 3716 H HAI  . A1IN3 C 2 .   ? -19.145 -5.01   11.35   1   43.821  ? 201 A1IN3 B HAI  1 c 1 
HETATM 3717 H HAH  . A1IN3 C 2 .   ? -19.972 -2.017  12.161  1   45.611  ? 201 A1IN3 B HAH  1 c 1 
HETATM 3718 H HB5  . A1IN3 C 2 .   ? -20.273 -3.497  11.268  1   45.542  ? 201 A1IN3 B HB5  1 c 1 
HETATM 3719 H HAG  . A1IN3 C 2 .   ? -21.624 -1.651  10.564  1   46.231  ? 201 A1IN3 B HAG  1 c 1 
HETATM 3720 H HB4  . A1IN3 C 2 .   ? -20.578 -2.171  9.276   1   43.141  ? 201 A1IN3 B HB4  1 c 1 
HETATM 3721 H HAF  . A1IN3 C 2 .   ? -19.882 0.061   10.989  1   43.678  ? 201 A1IN3 B HAF  1 c 1 
HETATM 3722 H HB3  . A1IN3 C 2 .   ? -20.563 0.12    9.387   1   42.828  ? 201 A1IN3 B HB3  1 c 1 
HETATM 3723 H HB2  . A1IN3 C 2 .   ? -18.594 -1.204  8.638   1   39.402  ? 201 A1IN3 B HB2  1 c 1 
HETATM 3724 H HB1  . A1IN3 C 2 .   ? -18.142 0.336   9.311   1   39.405  ? 201 A1IN3 B HB1  1 c 1 
HETATM 3725 H HA   . A1IN3 C 2 .   ? -16.796 -1.479  9.956   1   39.075  ? 201 A1IN3 B HA   1 c 1 
HETATM 3726 H HCG  . A1IN3 C 2 .   ? -16.342 -0.242  14.196  1   48.017  ? 201 A1IN3 B HCG  1 c 1 
HETATM 3727 H HBB  . A1IN3 C 2 .   ? -17.575 0.964   13.796  1   48.598  ? 201 A1IN3 B HBB  1 c 1 
HETATM 3728 H HCF  . A1IN3 C 2 .   ? -17.42  -1.034  15.671  1   51.914  ? 201 A1IN3 B HCF  1 c 1 
HETATM 3729 H HBA  . A1IN3 C 2 .   ? -18.271 0.529   15.536  1   52.607  ? 201 A1IN3 B HBA  1 c 1 
HETATM 3730 H HAZ  . A1IN3 C 2 .   ? -19.851 -1.051  14.115  1   52.529  ? 201 A1IN3 B HAZ  1 c 1 
HETATM 3731 H HAY  . A1IN3 C 2 .   ? -20.696 -2.304  16.059  1   58.31   ? 201 A1IN3 B HAY  1 c 1 
HETATM 3732 H HCE  . A1IN3 C 2 .   ? -17.975 -2.034  17.148  1   55.346  ? 201 A1IN3 B HCE  1 c 1 
HETATM 3733 H HAX  . A1IN3 C 2 .   ? -19.201 -1.045  17.94   1   58.898  ? 201 A1IN3 B HAX  1 c 1 
HETATM 3734 H HCD  . A1IN3 C 2 .   ? -18.938 -3.278  18.933  1   60.974  ? 201 A1IN3 B HCD  1 c 1 
HETATM 3735 H HAW  . A1IN3 C 2 .   ? -20.305 -3.502  17.821  1   60.249  ? 201 A1IN3 B HAW  1 c 1 
HETATM 3736 H HCC  . A1IN3 C 2 .   ? -14.538 -4.227  16.994  1   57.806  ? 201 A1IN3 B HCC  1 c 1 
HETATM 3737 H HAT  . A1IN3 C 2 .   ? -14.703 -4.613  15.267  1   54.143  ? 201 A1IN3 B HAT  1 c 1 
HETATM 3738 H HCB  . A1IN3 C 2 .   ? -15.484 -5.646  16.49   1   58.39   ? 201 A1IN3 B HCB  1 c 1 
HETATM 3739 H HAQ  . A1IN3 C 2 .   ? -16.205 -4.091  13.546  1   44.275  ? 201 A1IN3 B HAQ  1 c 1 
HETATM 3740 H HBI  . A1IN3 C 2 .   ? -20.349 -5.336  13.3    1   48.922  ? 201 A1IN3 B HBI  1 c 1 
HETATM 3741 H HCI  . A1IN3 C 2 .   ? -22.792 -5.239  16.048  1   62.045  ? 201 A1IN3 B HCI  1 c 1 
HETATM 3742 H HBH  . A1IN3 C 2 .   ? -22.035 -6.11   14.698  1   58.32   ? 201 A1IN3 B HBH  1 c 1 
HETATM 3743 H HCH  . A1IN3 C 2 .   ? -22.11  -4.33   14.681  1   56.493  ? 201 A1IN3 B HCH  1 c 1 
HETATM 3744 C CAK  . A1IN3 D 2 .   ? -3.183  12.294  19.293  1   48.63   ? 201 A1IN3 A CAK  1 ? 2 
HETATM 3745 C CAL  . A1IN3 D 2 .   ? -2.556  11.019  19.708  1   49.462  ? 201 A1IN3 A CAL  1 ? 2 
HETATM 3746 C CAM  . A1IN3 D 2 .   ? -2.243  10.914  21.183  1   47.954  ? 201 A1IN3 A CAM  1 ? 2 
HETATM 3747 C CAN  . A1IN3 D 2 .   ? -3.554  11.084  21.968  1   46.26   ? 201 A1IN3 A CAN  1 ? 2 
HETATM 3748 C CAO  . A1IN3 D 2 .   ? -4.203  12.364  21.655  1   45.116  ? 201 A1IN3 A CAO  1 ? 2 
HETATM 3749 C CAJ  . A1IN3 D 2 .   ? -4.473  12.498  20.157  1   46.034  ? 201 A1IN3 A CAJ  1 ? 2 
HETATM 3750 C CAI  . A1IN3 D 2 .   ? -5.146  13.886  19.859  1   44.325  ? 201 A1IN3 A CAI  1 ? 2 
HETATM 3751 C CAB  . A1IN3 D 2 .   ? -6.474  13.932  20.446  1   43.493  ? 201 A1IN3 A CAB  1 ? 2 
HETATM 3752 O OAA  . A1IN3 D 2 .   ? -7.117  12.866  20.618  1   40.847  ? 201 A1IN3 A OAA  1 ? 2 
HETATM 3753 N N    . A1IN3 D 2 .   ? -6.998  15.149  20.856  1   40.145  ? 201 A1IN3 A N    1 ? 2 
HETATM 3754 C CAH  . A1IN3 D 2 .   ? -6.286  16.453  20.491  1   43.001  ? 201 A1IN3 A CAH  1 ? 2 
HETATM 3755 C CAG  . A1IN3 D 2 .   ? -6.531  17.542  21.475  1   42.867  ? 201 A1IN3 A CAG  1 ? 2 
HETATM 3756 C CAF  . A1IN3 D 2 .   ? -7.979  17.76   21.688  1   42.3    ? 201 A1IN3 A CAF  1 ? 2 
HETATM 3757 C CB   . A1IN3 D 2 .   ? -8.494  16.555  22.43   1   40.398  ? 201 A1IN3 A CB   1 ? 2 
HETATM 3758 C CA   . A1IN3 D 2 .   ? -8.411  15.301  21.428  1   40.197  ? 201 A1IN3 A CA   1 ? 2 
HETATM 3759 C C    . A1IN3 D 2 .   ? -9.301  15.429  20.306  1   43.703  ? 201 A1IN3 A C    1 ? 2 
HETATM 3760 O O    . A1IN3 D 2 .   ? -10.508 15.53   20.432  1   42.551  ? 201 A1IN3 A O    1 ? 2 
HETATM 3761 O OBC  . A1IN3 D 2 .   ? -8.721  15.361  19.045  1   44.661  ? 201 A1IN3 A OBC  1 ? 2 
HETATM 3762 C CBB  . A1IN3 D 2 .   ? -9.556  15.978  18.003  1   49.732  ? 201 A1IN3 A CBB  1 ? 2 
HETATM 3763 C CBA  . A1IN3 D 2 .   ? -8.712  15.785  16.756  1   51.484  ? 201 A1IN3 A CBA  1 ? 2 
HETATM 3764 C CAZ  . A1IN3 D 2 .   ? -8.02   17.024  16.42   1   52.861  ? 201 A1IN3 A CAZ  1 ? 2 
HETATM 3765 C CAY  . A1IN3 D 2 .   ? -7.139  17.19   15.339  1   54.168  ? 201 A1IN3 A CAY  1 ? 2 
HETATM 3766 C CAX  . A1IN3 D 2 .   ? -7.067  16.179  14.364  1   55.948  ? 201 A1IN3 A CAX  1 ? 2 
HETATM 3767 C CAW  . A1IN3 D 2 .   ? -5.694  16.105  13.744  1   56.423  ? 201 A1IN3 A CAW  1 ? 2 
HETATM 3768 O OAV  . A1IN3 D 2 .   ? -5.164  14.903  14.323  1   56.966  ? 201 A1IN3 A OAV  1 ? 2 
HETATM 3769 C CAU  . A1IN3 D 2 .   ? -5.154  14.679  15.698  1   53.374  ? 201 A1IN3 A CAU  1 ? 2 
HETATM 3770 C CAR  . A1IN3 D 2 .   ? -6.02   13.716  16.239  1   53.335  ? 201 A1IN3 A CAR  1 ? 2 
HETATM 3771 O OAS  . A1IN3 D 2 .   ? -6.871  13.098  15.343  1   55.418  ? 201 A1IN3 A OAS  1 ? 2 
HETATM 3772 C CAT  . A1IN3 D 2 .   ? -7.586  11.951  15.78   1   53.369  ? 201 A1IN3 A CAT  1 ? 2 
HETATM 3773 C CAQ  . A1IN3 D 2 .   ? -6.034  13.463  17.594  1   46.221  ? 201 A1IN3 A CAQ  1 ? 2 
HETATM 3774 C CAP  . A1IN3 D 2 .   ? -5.167  14.177  18.447  1   50.262  ? 201 A1IN3 A CAP  1 ? 2 
HETATM 3775 C CBI  . A1IN3 D 2 .   ? -4.294  15.127  17.873  1   51.28   ? 201 A1IN3 A CBI  1 ? 2 
HETATM 3776 C CBF  . A1IN3 D 2 .   ? -4.292  15.396  16.5    1   51.469  ? 201 A1IN3 A CBF  1 ? 2 
HETATM 3777 O OBG  . A1IN3 D 2 .   ? -3.478  16.301  15.856  1   56.403  ? 201 A1IN3 A OBG  1 ? 2 
HETATM 3778 C CBH  . A1IN3 D 2 .   ? -2.829  17.354  16.622  1   53.963  ? 201 A1IN3 A CBH  1 ? 2 
HETATM 3779 H HAK  . A1IN3 D 2 .   ? -3.611  12.209  18.341  1   49.742  ? 201 A1IN3 A HAK  1 c 2 
HETATM 3780 H HB6  . A1IN3 D 2 .   ? -2.722  13.302  19.497  1   48.854  ? 201 A1IN3 A HB6  1 c 2 
HETATM 3781 H HAL  . A1IN3 D 2 .   ? -1.625  10.902  19.153  1   51.347  ? 201 A1IN3 A HAL  1 c 2 
HETATM 3782 H HB7  . A1IN3 D 2 .   ? -3.22   10.202  19.441  1   49.407  ? 201 A1IN3 A HB7  1 c 2 
HETATM 3783 H HAM  . A1IN3 D 2 .   ? -1.538  11.697  21.466  1   48.401  ? 201 A1IN3 A HAM  1 c 2 
HETATM 3784 H HB8  . A1IN3 D 2 .   ? -1.81   9.936   21.397  1   48.887  ? 201 A1IN3 A HB8  1 c 2 
HETATM 3785 H HAN  . A1IN3 D 2 .   ? -3.339  11.048  23.035  1   45.135  ? 201 A1IN3 A HAN  1 c 2 
HETATM 3786 H HB9  . A1IN3 D 2 .   ? -4.233  10.271  21.712  1   45.989  ? 201 A1IN3 A HB9  1 c 2 
HETATM 3787 H HCA  . A1IN3 D 2 .   ? -5.154  12.417  22.056  1   43.807  ? 201 A1IN3 A HCA  1 c 2 
HETATM 3788 H HAO  . A1IN3 D 2 .   ? -3.617  13.222  21.835  1   45.326  ? 201 A1IN3 A HAO  1 c 2 
HETATM 3789 H HAJ  . A1IN3 D 2 .   ? -5.167  11.709  19.873  1   45.863  ? 201 A1IN3 A HAJ  1 c 2 
HETATM 3790 H HAI  . A1IN3 D 2 .   ? -4.515  14.618  20.35   1   45.41   ? 201 A1IN3 A HAI  1 c 2 
HETATM 3791 H HAH  . A1IN3 D 2 .   ? -6.631  16.787  19.514  1   44.319  ? 201 A1IN3 A HAH  1 c 2 
HETATM 3792 H HB5  . A1IN3 D 2 .   ? -5.214  16.317  20.45   1   43.464  ? 201 A1IN3 A HB5  1 c 2 
HETATM 3793 H HAG  . A1IN3 D 2 .   ? -6.269  18.525  21.145  1   44.275  ? 201 A1IN3 A HAG  1 c 2 
HETATM 3794 H HB4  . A1IN3 D 2 .   ? -6.205  17.323  22.442  1   41.604  ? 201 A1IN3 A HB4  1 c 2 
HETATM 3795 H HAF  . A1IN3 D 2 .   ? -8.564  17.729  20.822  1   43.307  ? 201 A1IN3 A HAF  1 c 2 
HETATM 3796 H HB3  . A1IN3 D 2 .   ? -8.222  18.526  22.363  1   42.209  ? 201 A1IN3 A HB3  1 c 2 
HETATM 3797 H HB2  . A1IN3 D 2 .   ? -7.914  16.207  23.219  1   39.313  ? 201 A1IN3 A HB2  1 c 2 
HETATM 3798 H HB1  . A1IN3 D 2 .   ? -9.509  16.689  22.642  1   40.037  ? 201 A1IN3 A HB1  1 c 2 
HETATM 3799 H HA   . A1IN3 D 2 .   ? -8.673  14.4    21.983  1   39.446  ? 201 A1IN3 A HA   1 c 2 
HETATM 3800 H HCG  . A1IN3 D 2 .   ? -10.425 15.455  17.712  1   49.275  ? 201 A1IN3 A HCG  1 c 2 
HETATM 3801 H HBB  . A1IN3 D 2 .   ? -9.692  17.039  18.027  1   49.733  ? 201 A1IN3 A HBB  1 c 2 
HETATM 3802 H HCF  . A1IN3 D 2 .   ? -7.894  15.264  17.043  1   50.76   ? 201 A1IN3 A HCF  1 c 2 
HETATM 3803 H HBA  . A1IN3 D 2 .   ? -9.143  15.226  15.945  1   52.735  ? 201 A1IN3 A HBA  1 c 2 
HETATM 3804 H HAZ  . A1IN3 D 2 .   ? -8.048  17.84   17.142  1   51.981  ? 201 A1IN3 A HAZ  1 c 2 
HETATM 3805 H HAY  . A1IN3 D 2 .   ? -6.652  18.151  15.17   1   56.03   ? 201 A1IN3 A HAY  1 c 2 
HETATM 3806 H HCE  . A1IN3 D 2 .   ? -7.205  15.253  14.77   1   54.041  ? 201 A1IN3 A HCE  1 c 2 
HETATM 3807 H HAX  . A1IN3 D 2 .   ? -7.696  16.258  13.545  1   57.262  ? 201 A1IN3 A HAX  1 c 2 
HETATM 3808 H HCD  . A1IN3 D 2 .   ? -5.611  15.739  12.742  1   59.468  ? 201 A1IN3 A HCD  1 c 2 
HETATM 3809 H HAW  . A1IN3 D 2 .   ? -4.918  16.723  14.111  1   57.387  ? 201 A1IN3 A HAW  1 c 2 
HETATM 3810 H HCC  . A1IN3 D 2 .   ? -8.049  11.475  14.915  1   55.313  ? 201 A1IN3 A HCC  1 c 2 
HETATM 3811 H HAT  . A1IN3 D 2 .   ? -8.365  12.25   16.475  1   51.996  ? 201 A1IN3 A HAT  1 c 2 
HETATM 3812 H HCB  . A1IN3 D 2 .   ? -6.909  11.24   16.255  1   53.003  ? 201 A1IN3 A HCB  1 c 2 
HETATM 3813 H HAQ  . A1IN3 D 2 .   ? -6.71   12.723  18.015  1   47.099  ? 201 A1IN3 A HAQ  1 c 2 
HETATM 3814 H HBI  . A1IN3 D 2 .   ? -3.615  15.666  18.514  1   50.742  ? 201 A1IN3 A HBI  1 c 2 
HETATM 3815 H HCI  . A1IN3 D 2 .   ? -2.38   18.076  15.94   1   57.177  ? 201 A1IN3 A HCI  1 c 2 
HETATM 3816 H HBH  . A1IN3 D 2 .   ? -2.054  16.92   17.249  1   54.04   ? 201 A1IN3 A HBH  1 c 2 
HETATM 3817 H HCH  . A1IN3 D 2 .   ? -3.566  17.856  17.248  1   53.209  ? 201 A1IN3 A HCH  1 c 2 
HETATM 3818 O O    . HOH   E 3 .   ? -5.388  -8.093  4.545   1   43.443  ? 301 HOH   B O    1 ? ? 
HETATM 3819 O O    . HOH   E 3 .   ? -7.951  -7.096  -3.941  1   45.247  ? 302 HOH   B O    1 ? ? 
HETATM 3820 O O    . HOH   E 3 .   ? -19.022 -8.115  -6.163  1   57.696  ? 303 HOH   B O    1 ? ? 
HETATM 3821 O O    . HOH   E 3 .   ? -6.909  -4.87   11.05   1   36.317  ? 304 HOH   B O    1 ? ? 
HETATM 3822 O O    . HOH   E 3 .   ? -7.960  -5.789  -10.812 1   44.382  ? 305 HOH   B O    1 ? ? 
HETATM 3823 O O    . HOH   E 3 .   ? -18.738 8.439   10.723  1   46.164  ? 306 HOH   B O    1 ? ? 
HETATM 3824 O O    . HOH   E 3 .   ? -4.526  -3.875  -5.029  1   44.635  ? 307 HOH   B O    1 ? ? 
HETATM 3825 O O    . HOH   E 3 .   ? -33.18  -4.805  -0.113  1   51.74   ? 308 HOH   B O    1 ? ? 
HETATM 3826 O O    . HOH   E 3 .   ? -9.993  8.646   -0.157  1   53.726  ? 309 HOH   B O    1 ? ? 
HETATM 3827 O O    . HOH   E 3 .   ? -8.553  -4.357  9.461   1   40.498  ? 310 HOH   B O    1 ? ? 
HETATM 3828 O O    . HOH   E 3 .   ? -7.405  -0.268  14.978  1   46.473  ? 311 HOH   B O    1 ? ? 
HETATM 3829 O O    . HOH   E 3 .   ? -10.441 3.224   9.69    1   35.702  ? 312 HOH   B O    1 ? ? 
HETATM 3830 O O    . HOH   E 3 .   ? -7.091  0.328   -9.37   1   45.46   ? 313 HOH   B O    1 ? ? 
HETATM 3831 O O    . HOH   E 3 .   ? -6.288  2.397   -8.441  1   43.294  ? 314 HOH   B O    1 ? ? 
HETATM 3832 O O    . HOH   E 3 .   ? -9.2    -3.004  -1.438  1   41.687  ? 315 HOH   B O    1 ? ? 
HETATM 3833 O O    . HOH   E 3 .   ? -6.758  7.9     0.054   1   43.925  ? 316 HOH   B O    1 ? ? 
HETATM 3834 O O    . HOH   E 3 .   ? -9.394  1.377   13.265  1   54.944  ? 317 HOH   B O    1 ? ? 
HETATM 3835 O O    . HOH   E 3 .   ? -6.586  -6.49   0.483   1   50.061  ? 318 HOH   B O    1 ? ? 
HETATM 3836 O O    . HOH   E 3 .   ? -12.93  -10.682 1.456   1   53.449  ? 319 HOH   B O    1 ? ? 
HETATM 3837 O O    . HOH   E 3 .   ? -13.451 -5.582  19.158  1   49.516  ? 320 HOH   B O    1 ? ? 
HETATM 3838 O O    . HOH   E 3 .   ? -1.945  -1.183  8.148   1   66.272  ? 321 HOH   B O    1 ? ? 
HETATM 3839 O O    . HOH   E 3 .   ? -2.956  -5.79   18.766  1   65.118  ? 322 HOH   B O    1 ? ? 
HETATM 3840 O O    . HOH   E 3 .   ? -26.939 -5.889  2.477   1   61.185  ? 323 HOH   B O    1 ? ? 
HETATM 3841 O O    . HOH   E 3 .   ? -5.27   7.488   4.36    1   53.62   ? 324 HOH   B O    1 ? ? 
HETATM 3842 O O    . HOH   E 3 .   ? -34.692 -4.205  9.898   1   57.526  ? 325 HOH   B O    1 ? ? 
HETATM 3843 O O    . HOH   E 3 .   ? -16.91  7.519   18.295  1   53.426  ? 326 HOH   B O    1 ? ? 
HETATM 3844 O O    . HOH   E 3 .   ? -1.369  -2.371  0       0.5 42.332  ? 327 HOH   B O    1 ? ? 
HETATM 3845 O O    . HOH   E 3 .   ? -8.819  -11.175 8.236   1   46.679  ? 328 HOH   B O    1 ? ? 
HETATM 3846 O O    . HOH   E 3 .   ? -2.627  1.544   10.112  1   48.061  ? 329 HOH   B O    1 ? ? 
HETATM 3847 O O    . HOH   E 3 .   ? -7.726  -5.131  -1.515  1   45.402  ? 330 HOH   B O    1 ? ? 
HETATM 3848 O O    . HOH   E 3 .   ? -2.926  5.939   6.805   1   46.789  ? 331 HOH   B O    1 ? ? 
HETATM 3849 O O    . HOH   F 3 .   ? -22.402 29.486  27.242  1   45.043  ? 301 HOH   A O    1 ? ? 
HETATM 3850 O O    . HOH   F 3 .   ? -16.53  20.387  21.727  1   55.013  ? 302 HOH   A O    1 ? ? 
HETATM 3851 O O    . HOH   F 3 .   ? -18.992 21.178  15.868  1   61.184  ? 303 HOH   A O    1 ? ? 
HETATM 3852 O O    . HOH   F 3 .   ? -10.133 5.852   21.778  1   47.289  ? 304 HOH   A O    1 ? ? 
HETATM 3853 O O    . HOH   F 3 .   ? -10.334 4.058   19.761  1   41.855  ? 305 HOH   A O    1 ? ? 
HETATM 3854 O O    . HOH   F 3 .   ? -2.932  5.413   37.824  1   47.395  ? 306 HOH   A O    1 ? ? 
HETATM 3855 O O    . HOH   F 3 .   ? -11.532 5.481   41.521  1   57.246  ? 307 HOH   A O    1 ? ? 
HETATM 3856 O O    . HOH   F 3 .   ? -9.095  23.701  40.502  1   55.648  ? 308 HOH   A O    1 ? ? 
HETATM 3857 O O    . HOH   F 3 .   ? 2.093   25.875  33.511  1   48.247  ? 309 HOH   A O    1 ? ? 
HETATM 3858 O O    . HOH   F 3 .   ? -11.384 5.877   32.618  1   45.467  ? 310 HOH   A O    1 ? ? 
HETATM 3859 O O    . HOH   F 3 .   ? -12.682 2.22    34.821  1   47.435  ? 311 HOH   A O    1 ? ? 
HETATM 3860 O O    . HOH   F 3 .   ? -0.527  7.323   39.685  1   54.053  ? 312 HOH   A O    1 ? ? 
HETATM 3861 O O    . HOH   F 3 .   ? -10.401 4.398   12.137  1   44.888  ? 313 HOH   A O    1 ? ? 
HETATM 3862 O O    . HOH   F 3 .   ? -4.066  5.875   35.333  1   60.704  ? 314 HOH   A O    1 ? ? 
HETATM 3863 O O    . HOH   F 3 .   ? -16.848 1.959   21.45   1   45.546  ? 315 HOH   A O    1 ? ? 
HETATM 3864 O O    . HOH   F 3 .   ? -20.145 7.38    26.177  1   68.884  ? 316 HOH   A O    1 ? ? 
HETATM 3865 O O    . HOH   F 3 .   ? -16.161 33.11   21.012  1   72.821  ? 317 HOH   A O    1 ? ? 
HETATM 3866 O O    . HOH   F 3 .   ? -20.698 4.622   26.902  1   62.623  ? 318 HOH   A O    1 ? ? 
HETATM 3867 O O    . HOH   F 3 .   ? -13.619 14.433  17.426  1   49.936  ? 319 HOH   A O    1 ? ? 
HETATM 3868 O O    . HOH   F 3 .   ? -0.034  9.04    35.615  1   58.4    ? 320 HOH   A O    1 ? ? 
HETATM 3869 O O    . HOH   F 3 .   ? -0.837  7.214   32.958  1   57.21   ? 321 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   ? 1.58371  0.529685 0.844533 0.00632053  -0.146059   -0.284527   13  GLY   B N    
2    C CA   . GLY   A 1   ? 1.5525   0.52597  0.875553 -0.0382795  -0.179492   -0.283162   13  GLY   B CA   
3    C C    . GLY   A 1   ? 1.45957  0.533652 0.821374 -0.0419164  -0.153983   -0.260049   13  GLY   B C    
4    O O    . GLY   A 1   ? 1.41981  0.521772 0.729965 -0.00925291 -0.129113   -0.25752    13  GLY   B O    
5    H H1   . GLY   A 1   ? 1.65192  0.5323   0.890153 0.00983408  -0.161885   -0.298506   13  GLY   B H1   
6    H H2   . GLY   A 1   ? 1.52591  0.513992 0.822666 0.00468307  -0.11768    -0.262988   13  GLY   B H2   
7    H H3   . GLY   A 1   ? 1.60101  0.553552 0.809892 0.0335823   -0.137989   -0.292971   13  GLY   B H3   
8    H HA2  . GLY   A 1   ? 1.62209  0.551269 0.904297 -0.0354165  -0.213631   -0.30731    13  GLY   B HA2  
9    H HA3  . GLY   A 1   ? 1.5425   0.510822 0.923564 -0.0681168  -0.186072   -0.273743   13  GLY   B HA3  
10   N N    . ALA   A 2   ? 1.41168  0.540268 0.869335 -0.0818279  -0.156639   -0.241666   14  ALA   B N    
11   C CA   . ALA   A 2   ? 1.30413  0.513335 0.805439 -0.0898937  -0.146759   -0.22645    14  ALA   B CA   
12   C C    . ALA   A 2   ? 1.26173  0.524435 0.742495 -0.0623409  -0.0985315  -0.209286   14  ALA   B C    
13   O O    . ALA   A 2   ? 1.2284   0.521023 0.689472 -0.0511349  -0.0953823  -0.205591   14  ALA   B O    
14   C CB   . ALA   A 2   ? 1.24468  0.503697 0.854556 -0.131376   -0.148585   -0.210593   14  ALA   B CB   
15   H H    . ALA   A 2   ? 1.40368  0.517478 0.901722 -0.104074   -0.163809   -0.238071   14  ALA   B H    
16   H HA   . ALA   A 2   ? 1.34849  0.542798 0.820961 -0.0857738  -0.173683   -0.23908    14  ALA   B HA   
17   H HB1  . ALA   A 2   ? 1.27969  0.513188 0.908932 -0.150448   -0.181675   -0.221395   14  ALA   B HB1  
18   H HB2  . ALA   A 2   ? 1.22368  0.488664 0.854982 -0.136484   -0.125989   -0.198685   14  ALA   B HB2  
19   H HB3  . ALA   A 2   ? 1.18937  0.500924 0.829322 -0.133325   -0.139331   -0.201323   14  ALA   B HB3  
20   N N    . PRO   A 3   ? 1.21246  0.490854 0.701718 -0.0523928  -0.0620022  -0.196312   15  PRO   B N    
21   C CA   . PRO   A 3   ? 1.21704  0.551175 0.695953 -0.0286422  -0.0205161  -0.182438   15  PRO   B CA   
22   C C    . PRO   A 3   ? 1.25236  0.564606 0.645141 0.0105956   -0.0110742  -0.192698   15  PRO   B C    
23   O O    . PRO   A 3   ? 1.17085  0.532476 0.558526 0.0209369   0.0118995   -0.181513   15  PRO   B O    
24   C CB   . PRO   A 3   ? 1.17993  0.526611 0.682506 -0.0248761  0.00571739  -0.169578   15  PRO   B CB   
25   C CG   . PRO   A 3   ? 1.21868  0.527981 0.761124 -0.0565072  -0.0171369  -0.168634   15  PRO   B CG   
26   C CD   . PRO   A 3   ? 1.27058  0.516126 0.783964 -0.0648073  -0.060501   -0.191545   15  PRO   B CD   
27   H HA   . PRO   A 3   ? 1.14659  0.527937 0.664121 -0.0411207  -0.0146756  -0.173089   15  PRO   B HA   
28   H HB2  . PRO   A 3   ? 1.22573  0.546622 0.683676 0.00105073  0.0140214   -0.174655   15  PRO   B HB2  
29   H HB3  . PRO   A 3   ? 1.12689  0.529635 0.664587 -0.0289217  0.0262681   -0.156971   15  PRO   B HB3  
30   H HG2  . PRO   A 3   ? 1.23513  0.517617 0.76659  -0.0490187  -0.00986951 -0.164306   15  PRO   B HG2  
31   H HG3  . PRO   A 3   ? 1.15744  0.510563 0.755058 -0.0784249  -0.0119299  -0.157621   15  PRO   B HG3  
32   H HD2  . PRO   A 3   ? 1.33066  0.518548 0.79475  -0.0481629  -0.0691675  -0.20409    15  PRO   B HD2  
33   H HD3  . PRO   A 3   ? 1.25961  0.504167 0.819432 -0.0933287  -0.0775006  -0.189673   15  PRO   B HD3  
34   N N    . ALA   A 4   ? 1.29857  0.535991 0.624983 0.0324776   -0.0266277  -0.213544   16  ALA   B N    
35   C CA   . ALA   A 4   ? 1.38491  0.597163 0.620396 0.0742882   -0.0172245  -0.227411   16  ALA   B CA   
36   C C    . ALA   A 4   ? 1.42243  0.636169 0.619593 0.0728589   -0.0354296  -0.230983   16  ALA   B C    
37   O O    . ALA   A 4   ? 1.39956  0.641594 0.551729 0.0978385   -0.00858329 -0.222794   16  ALA   B O    
38   C CB   . ALA   A 4   ? 1.4751   0.596182 0.647186 0.0978264   -0.0365844  -0.25492    16  ALA   B CB   
39   H H    . ALA   A 4   ? 1.33651  0.536358 0.67366  0.0217926   -0.0424459  -0.219511   16  ALA   B H    
40   H HA   . ALA   A 4   ? 1.34876  0.605014 0.589069 0.0904061   0.0158215   -0.215156   16  ALA   B HA   
41   H HB1  . ALA   A 4   ? 1.46621  0.58472  0.661961 0.100251    -0.0246553  -0.248807   16  ALA   B HB1  
42   H HB2  . ALA   A 4   ? 1.51545  0.592818 0.686018 0.0795696   -0.0712552  -0.268279   16  ALA   B HB2  
43   H HB3  . ALA   A 4   ? 1.53136  0.638255 0.63994  0.12981     -0.0270609  -0.265821   16  ALA   B HB3  
44   N N    . THR   A 5   ? 1.41886  0.604685 0.635808 0.0440459   -0.0809342  -0.240635   17  THR   B N    
45   C CA   . THR   A 5   ? 1.39569  0.58585  0.584493 0.0415297   -0.104815   -0.240186   17  THR   B CA   
46   C C    . THR   A 5   ? 1.27503  0.544371 0.51098  0.0340373   -0.0713999  -0.207945   17  THR   B C    
47   O O    . THR   A 5   ? 1.25225  0.52839  0.442094 0.046573    -0.0701375  -0.198383   17  THR   B O    
48   C CB   . THR   A 5   ? 1.40504  0.566643 0.631614 0.00923382  -0.161853   -0.254496   17  THR   B CB   
49   O OG1  . THR   A 5   ? 1.49459  0.571494 0.659092 0.0190156   -0.197787   -0.288539   17  THR   B OG1  
50   C CG2  . THR   A 5   ? 1.40708  0.582886 0.618666 0.00680107  -0.190307   -0.249286   17  THR   B CG2  
51   H H    . THR   A 5   ? 1.41081  0.575335 0.661447 0.0257039   -0.098235   -0.246345   17  THR   B H    
52   H HA   . THR   A 5   ? 1.46727  0.625606 0.577474 0.0684395   -0.106051   -0.251927   17  THR   B HA   
53   H HB   . THR   A 5   ? 1.34013  0.528728 0.643288 -0.0162107  -0.158954   -0.245243   17  THR   B HB   
55   H HG21 . THR   A 5   ? 1.44275  0.593412 0.665853 -0.00768703 -0.231514   -0.264205   17  THR   B HG21 
56   H HG22 . THR   A 5   ? 1.46493  0.623704 0.599741 0.033034    -0.184125   -0.251528   17  THR   B HG22 
57   H HG23 . THR   A 5   ? 1.34106  0.567604 0.608082 -0.00550282 -0.174163   -0.228474   17  THR   B HG23 
58   N N    . VAL   A 6   ? 1.17666  0.500891 0.499131 0.0143907   -0.0451564  -0.191086   18  VAL   B N    
59   C CA   . VAL   A 6   ? 1.12815  0.519619 0.500992 0.0041581   -0.0190485  -0.165928   18  VAL   B CA   
60   C C    . VAL   A 6   ? 1.12773  0.548322 0.462588 0.0303116   0.0259058   -0.152996   18  VAL   B C    
61   O O    . VAL   A 6   ? 1.08547  0.529136 0.408243 0.032508    0.0388434   -0.135151   18  VAL   B O    
62   C CB   . VAL   A 6   ? 1.01941  0.460461 0.494211 -0.0255086  -0.0113339  -0.156711   18  VAL   B CB   
63   C CG1  . VAL   A 6   ? 0.988974 0.489949 0.508199 -0.0326345  0.0142841   -0.136534   18  VAL   B CG1  
64   C CG2  . VAL   A 6   ? 0.995764 0.421688 0.517472 -0.0518392  -0.0517326  -0.1657     18  VAL   B CG2  
65   H H    . VAL   A 6   ? 1.17177  0.488404 0.520609 0.00698169  -0.0451506  -0.195693   18  VAL   B H    
66   H HA   . VAL   A 6   ? 1.13615  0.521635 0.498637 0.0005893   -0.0373176  -0.163015   18  VAL   B HA   
67   H HB   . VAL   A 6   ? 1.01216  0.455968 0.494011 -0.0219518  0.00347604  -0.158588   18  VAL   B HB   
68   H HG11 . VAL   A 6   ? 1.00069  0.493448 0.502926 -0.0315588  0.0027529   -0.131492   18  VAL   B HG11 
69   H HG12 . VAL   A 6   ? 0.971908 0.491742 0.47783  -0.0206972  0.041194    -0.13048    18  VAL   B HG12 
70   H HG13 . VAL   A 6   ? 0.928732 0.456675 0.507227 -0.0498114  0.0146445   -0.13482    18  VAL   B HG13 
71   H HG21 . VAL   A 6   ? 0.949732 0.407505 0.531313 -0.0679292  -0.0426148  -0.160402   18  VAL   B HG21 
72   H HG22 . VAL   A 6   ? 1.05044  0.43398  0.544849 -0.0500497  -0.0708785  -0.179281   18  VAL   B HG22 
73   H HG23 . VAL   A 6   ? 1.01102  0.438863 0.531547 -0.0538646  -0.0678661  -0.162983   18  VAL   B HG23 
74   N N    . THR   A 7   ? 1.11776  0.537536 0.437166 0.050243    0.0489731   -0.159829   19  THR   B N    
75   C CA   . THR   A 7   ? 1.17109  0.616107 0.447288 0.0819393   0.0887038   -0.152385   19  THR   B CA   
76   C C    . THR   A 7   ? 1.25075  0.663085 0.434964 0.10421     0.0853564   -0.153723   19  THR   B C    
77   O O    . THR   A 7   ? 1.2893   0.74201  0.462964 0.11097     0.116642    -0.131918   19  THR   B O    
78   C CB   . THR   A 7   ? 1.22125  0.647899 0.476474 0.109517    0.100815    -0.167082   19  THR   B CB   
79   O OG1  . THR   A 7   ? 1.12171  0.590235 0.45933  0.0889342   0.108098    -0.157674   19  THR   B OG1  
80   C CG2  . THR   A 7   ? 1.2716   0.717492 0.470792 0.151644    0.138529    -0.165849   19  THR   B CG2  
81   H H    . THR   A 7   ? 1.12044  0.525475 0.459595 0.0445244   0.0403087   -0.167955   19  THR   B H    
82   H HA   . THR   A 7   ? 1.11362  0.61093  0.435085 0.0720532   0.110422    -0.135814   19  THR   B HA   
83   H HB   . THR   A 7   ? 1.26367  0.632789 0.485667 0.113153    0.074963    -0.184748   19  THR   B HB   
85   H HG21 . THR   A 7   ? 1.27703  0.720736 0.478336 0.169118    0.147213    -0.172902   19  THR   B HG21 
86   H HG22 . THR   A 7   ? 1.23289  0.733621 0.461542 0.145521    0.162452    -0.14743    19  THR   B HG22 
87   H HG23 . THR   A 7   ? 1.34096  0.747344 0.473481 0.168112    0.130104    -0.1763     19  THR   B HG23 
88   N N    . GLU   A 8   ? 1.33275  0.672885 0.453181 0.111962    0.045226    -0.177541   20  GLU   B N    
89   C CA   . GLU   A 8   ? 1.45597  0.756835 0.467287 0.142037    0.0402681   -0.184959   20  GLU   B CA   
90   C C    . GLU   A 8   ? 1.45715  0.770093 0.461002 0.126987    0.027941    -0.162038   20  GLU   B C    
91   O O    . GLU   A 8   ? 1.48207  0.804465 0.420577 0.148113    0.0532275   -0.144811   20  GLU   B O    
92   C CB   . GLU   A 8   ? 1.5697   0.783284 0.513342 0.155116    -0.00638514 -0.224083   20  GLU   B CB   
93   C CG   . GLU   A 8   ? 1.59403  0.775701 0.53384  0.173991    0.00137653  -0.247204   20  GLU   B CG   
94   C CD   . GLU   A 8   ? 1.69806  0.784155 0.589296 0.176724    -0.0512169  -0.286917   20  GLU   B CD   
95   O OE1  . GLU   A 8   ? 1.75533  0.799293 0.591824 0.174075    -0.0933568  -0.302704   20  GLU   B OE1  
96   O OE2  . GLU   A 8   ? 1.73021  0.782131 0.640695 0.18071     -0.0524172  -0.301345   20  GLU   B OE2  
97   H H    . GLU   A 8   ? 1.32836  0.643118 0.472593 0.0979988   0.0196798   -0.189893   20  GLU   B H    
98   H HA   . GLU   A 8   ? 1.47519  0.79629  0.456709 0.166397    0.0752322   -0.17977    20  GLU   B HA   
99   H HB2  . GLU   A 8   ? 1.54749  0.747113 0.527285 0.129239    -0.0409471  -0.228166   20  GLU   B HB2  
100  H HB3  . GLU   A 8   ? 1.64515  0.832746 0.508606 0.17759     -0.0106063  -0.231006   20  GLU   B HB3  
101  H HG2  . GLU   A 8   ? 1.62752  0.81989  0.524555 0.205094    0.0325465   -0.247045   20  GLU   B HG2  
102  H HG3  . GLU   A 8   ? 1.52058  0.733726 0.533706 0.15525     0.0113932   -0.23598    20  GLU   B HG3  
103  N N    . GLN   A 9   ? 1.38604  0.696367 0.453509 0.0933661   -0.0108694  -0.160901   21  GLN   B N    
104  C CA   . GLN   A 9   ? 1.44677  0.749809 0.497479 0.0851318   -0.0379212  -0.145457   21  GLN   B CA   
105  C C    . GLN   A 9   ? 1.32073  0.678707 0.47754  0.0533452   -0.0275463  -0.118248   21  GLN   B C    
106  O O    . GLN   A 9   ? 1.33964  0.694095 0.502431 0.0450229   -0.0507259  -0.10303    21  GLN   B O    
107  C CB   . GLN   A 9   ? 1.53165  0.781141 0.563242 0.0778927   -0.104279   -0.17153    21  GLN   B CB   
108  C CG   . GLN   A 9   ? 1.64999  0.834055 0.605545 0.0983814   -0.129216   -0.211366   21  GLN   B CG   
109  C CD   . GLN   A 9   ? 1.82753  0.98508  0.655907 0.142969    -0.103833   -0.215559   21  GLN   B CD   
110  O OE1  . GLN   A 9   ? 1.92344  1.10491  0.708129 0.156306    -0.0780989  -0.186384   21  GLN   B OE1  
111  N NE2  . GLN   A 9   ? 1.9673   1.07202  0.732897 0.167533    -0.110343   -0.251233   21  GLN   B NE2  
112  H H    . GLN   A 9   ? 1.35377  0.667171 0.476125 0.0768924   -0.0208945  -0.169366   21  GLN   B H    
113  H HA   . GLN   A 9   ? 1.49729  0.796111 0.481686 0.105362    -0.0209263  -0.133933   21  GLN   B HA   
114  H HB2  . GLN   A 9   ? 1.46689  0.733796 0.577611 0.0528465   -0.118709   -0.172545   21  GLN   B HB2  
115  H HB3  . GLN   A 9   ? 1.57283  0.813175 0.567102 0.0836333   -0.12001    -0.161091   21  GLN   B HB3  
116  H HG2  . GLN   A 9   ? 1.6195   0.806884 0.616244 0.0911838   -0.118271   -0.220328   21  GLN   B HG2  
117  H HG3  . GLN   A 9   ? 1.69451  0.848197 0.643955 0.0900943   -0.174742   -0.22705    21  GLN   B HG3  
118  H HE21 . GLN   A 9   ? 2.02072  1.10422  0.703748 0.196798    -0.100721   -0.259003   21  GLN   B HE21 
119  H HE22 . GLN   A 9   ? 1.92309  1.01173  0.727826 0.155595    -0.123761   -0.26707    21  GLN   B HE22 
120  N N    . GLY   A 10  ? 1.23967  0.645164 0.476971 0.0384903   0.00424847  -0.113906   22  GLY   B N    
121  C CA   . GLY   A 10  ? 1.139    0.590332 0.477259 0.00919357  0.00876309  -0.0981306  22  GLY   B CA   
122  C C    . GLY   A 10  ? 1.12691  0.602717 0.464499 0.00812672  0.035513    -0.0654071  22  GLY   B C    
123  O O    . GLY   A 10  ? 1.13145  0.623094 0.430265 0.0227593   0.0739604   -0.0518137  22  GLY   B O    
124  H H    . GLY   A 10  ? 1.23461  0.643638 0.461241 0.0490156   0.0229433   -0.121812   22  GLY   B H    
125  H HA2  . GLY   A 10  ? 1.13328  0.572084 0.496219 -0.00222009 -0.0232079  -0.104805   22  GLY   B HA2  
126  H HA3  . GLY   A 10  ? 1.08473  0.562786 0.468914 0.00159716  0.0254652   -0.102565   22  GLY   B HA3  
127  N N    . GLU   A 11  ? 1.10396  0.586212 0.495757 -0.0103304  0.0174253   -0.0524106  23  GLU   B N    
128  C CA   . GLU   A 11  ? 1.0963   0.596749 0.508911 -0.0184915  0.0410642   -0.0203742  23  GLU   B CA   
129  C C    . GLU   A 11  ? 0.991706 0.546719 0.488044 -0.0371716  0.0757207   -0.0199992  23  GLU   B C    
130  O O    . GLU   A 11  ? 0.932483 0.508666 0.495794 -0.0504902  0.0660722   -0.0400042  23  GLU   B O    
131  C CB   . GLU   A 11  ? 1.1588   0.634159 0.592648 -0.0247485  0.00010649  -0.0130107  23  GLU   B CB   
132  C CG   . GLU   A 11  ? 1.21303  0.682647 0.656152 -0.0304176  0.0118982   0.0234242   23  GLU   B CG   
133  C CD   . GLU   A 11  ? 1.26864  0.725893 0.771776 -0.0381614  -0.0243531  0.0265629   23  GLU   B CD   
134  O OE1  . GLU   A 11  ? 1.26353  0.730763 0.820028 -0.0423167  -0.055821   0.0003419   23  GLU   B OE1  
135  O OE2  . GLU   A 11  ? 1.35297  0.791053 0.854282 -0.0396825  -0.0188876  0.0584329   23  GLU   B OE2  
136  H H    . GLU   A 11  ? 1.0893   0.563168 0.508856 -0.0179973  -0.0109296  -0.0641003  23  GLU   B H    
137  H HA   . GLU   A 11  ? 1.15486  0.645121 0.506837 -0.0049967  0.0578273   -0.00538202 23  GLU   B HA   
138  H HB2  . GLU   A 11  ? 1.20758  0.651924 0.587316 -0.0118111  -0.0260975  -0.0186265  23  GLU   B HB2  
139  H HB3  . GLU   A 11  ? 1.10097  0.592297 0.598116 -0.0369238  -0.0124599  -0.0277819  23  GLU   B HB3  
140  H HG2  . GLU   A 11  ? 1.18435  0.681411 0.662929 -0.0415351  0.0429593   0.0306372   23  GLU   B HG2  
141  H HG3  . GLU   A 11  ? 1.28877  0.734433 0.66114  -0.0166981  0.0147229   0.0406634   23  GLU   B HG3  
142  N N    . ASP   A 12  ? 0.964299 0.545453 0.457715 -0.0387009  0.115741    0.00304133  24  ASP   B N    
143  C CA   . ASP   A 12  ? 0.900615 0.535102 0.476272 -0.0584986  0.142644    0.00309926  24  ASP   B CA   
144  C C    . ASP   A 12  ? 0.880269 0.50974  0.520404 -0.081236   0.130269    0.0133534   24  ASP   B C    
145  O O    . ASP   A 12  ? 0.897215 0.506196 0.521004 -0.0854827  0.137328    0.0433085   24  ASP   B O    
146  C CB   . ASP   A 12  ? 0.920912 0.593148 0.485545 -0.0554662  0.18798     0.0235641   24  ASP   B CB   
147  C CG   . ASP   A 12  ? 0.854765 0.587913 0.508929 -0.0769643  0.209837    0.0201281   24  ASP   B CG   
148  O OD1  . ASP   A 12  ? 0.809988 0.550325 0.528273 -0.0940356  0.190619    0.00230566  24  ASP   B OD1  
149  O OD2  . ASP   A 12  ? 0.821641 0.599458 0.482994 -0.0755039  0.245441    0.0334643   24  ASP   B OD2  
150  H H    . ASP   A 12  ? 1.02961  0.596962 0.469085 -0.0275592  0.126106    0.0190273   24  ASP   B H    
151  H HA   . ASP   A 12  ? 0.858355 0.508386 0.458964 -0.0588779  0.137794    -0.0178002  24  ASP   B HA   
152  H HB2  . ASP   A 12  ? 0.941876 0.614935 0.462035 -0.0361284  0.195972    0.0157057   24  ASP   B HB2  
153  H HB3  . ASP   A 12  ? 0.966485 0.623749 0.506604 -0.0569574  0.196044    0.0479421   24  ASP   B HB3  
154  N N    . ILE   A 13  ? 0.832835 0.477837 0.542005 -0.093511   0.113408    -0.0104606  25  ILE   B N    
155  C CA   . ILE   A 13  ? 0.831927 0.466562 0.600791 -0.108851   0.0988364   -0.00741805 25  ILE   B CA   
156  C C    . ILE   A 13  ? 0.802199 0.475297 0.642252 -0.129848   0.120176    -0.0124497  25  ILE   B C    
157  O O    . ILE   A 13  ? 0.804432 0.468728 0.698919 -0.141225   0.108145    -0.0188887  25  ILE   B O    
158  C CB   . ILE   A 13  ? 0.790565 0.415841 0.587764 -0.104938   0.0642716   -0.0311174  25  ILE   B CB   
159  C CG1  . ILE   A 13  ? 0.733439 0.397831 0.563812 -0.107933   0.0692567   -0.0597691  25  ILE   B CG1  
160  C CG2  . ILE   A 13  ? 0.83515  0.420246 0.56994  -0.087943   0.0345854   -0.0261663  25  ILE   B CG2  
161  C CD1  . ILE   A 13  ? 0.733881 0.400528 0.607331 -0.108375   0.0430618   -0.0791961  25  ILE   B CD1  
162  H H    . ILE   A 13  ? 0.800078 0.46133  0.517714 -0.0907488  0.112255    -0.0285321  25  ILE   B H    
163  H HA   . ILE   A 13  ? 0.876028 0.481989 0.619352 -0.106925   0.0958311   0.0143739   25  ILE   B HA   
164  H HB   . ILE   A 13  ? 0.788203 0.407473 0.625149 -0.111217   0.0563271   -0.0301997  25  ILE   B HB   
165  H HG12 . ILE   A 13  ? 0.746946 0.41094  0.538365 -0.100018   0.0741381   -0.0612916  25  ILE   B HG12 
166  H HG13 . ILE   A 13  ? 0.710034 0.40096  0.573036 -0.116863   0.0859581   -0.0638783  25  ILE   B HG13 
167  H HG21 . ILE   A 13  ? 0.825293 0.4079   0.589855 -0.0878691  0.0116079   -0.0374887  25  ILE   B HG21 
168  H HG22 . ILE   A 13  ? 0.843394 0.43046  0.541643 -0.0809629  0.0386623   -0.0332178  25  ILE   B HG22 
169  H HG23 . ILE   A 13  ? 0.886602 0.446358 0.587992 -0.083433   0.0335347   -0.00486091 25  ILE   B HG23 
170  H HD11 . ILE   A 13  ? 0.726856 0.388121 0.633135 -0.111165   0.0356136   -0.0775534  25  ILE   B HD11 
171  H HD12 . ILE   A 13  ? 0.688316 0.38261  0.586112 -0.112356   0.0517058   -0.0938241  25  ILE   B HD12 
172  H HD13 . ILE   A 13  ? 0.749203 0.396146 0.594603 -0.10128    0.0249677   -0.0786542  25  ILE   B HD13 
173  N N    . THR   A 14  ? 0.786545 0.501916 0.629055 -0.13369    0.149325    -0.0112618  26  THR   B N    
174  C CA   . THR   A 14  ? 0.738128 0.491502 0.649263 -0.156199   0.165019    -0.0151986  26  THR   B CA   
175  C C    . THR   A 14  ? 0.768178 0.500173 0.690445 -0.174102   0.17823     0.0186906   26  THR   B C    
176  O O    . THR   A 14  ? 0.812623 0.518879 0.677384 -0.165694   0.189105    0.0504192   26  THR   B O    
177  C CB   . THR   A 14  ? 0.710559 0.524794 0.631067 -0.154032   0.188289    -0.0240842  26  THR   B CB   
178  O OG1  . THR   A 14  ? 0.748487 0.570217 0.620192 -0.142939   0.214179    0.00185056  26  THR   B OG1  
179  C CG2  . THR   A 14  ? 0.656062 0.48598  0.563976 -0.137203   0.177397    -0.0518651  26  THR   B CG2  
180  H H    . THR   A 14  ? 0.791489 0.513009 0.594593 -0.121463   0.157926    -0.00947817 26  THR   B H    
181  H HA   . THR   A 14  ? 0.713097 0.466544 0.661302 -0.161549   0.150588    -0.034259   26  THR   B HA   
182  H HB   . THR   A 14  ? 0.690934 0.531288 0.661287 -0.170605   0.193372    -0.0289405  26  THR   B HB   
184  H HG21 . THR   A 14  ? 0.64517  0.511359 0.557667 -0.133107   0.190813    -0.0552596  26  THR   B HG21 
185  H HG22 . THR   A 14  ? 0.678689 0.480769 0.542051 -0.123423   0.169955    -0.0491983  26  THR   B HG22 
186  H HG23 . THR   A 14  ? 0.634313 0.465286 0.574166 -0.143768   0.16414     -0.0684816  26  THR   B HG23 
187  N N    . SER   A 15  ? 0.730148 0.472324 0.724711 -0.199369   0.178032    0.0115408   27  SER   B N    
188  C CA   . SER   A 15  ? 0.791815 0.512707 0.813378 -0.223965   0.190976    0.0434487   27  SER   B CA   
189  C C    . SER   A 15  ? 0.795824 0.567793 0.81956  -0.235006   0.228784    0.068051    27  SER   B C    
190  O O    . SER   A 15  ? 0.849074 0.602781 0.860478 -0.247437   0.250198    0.110433    27  SER   B O    
191  C CB   . SER   A 15  ? 0.78969  0.502265 0.890677 -0.247875   0.175334    0.0208651   27  SER   B CB   
192  O OG   . SER   A 15  ? 0.775989 0.437088 0.873365 -0.233775   0.145274    0.00610732  27  SER   B OG   
193  H H    . SER   A 15  ? 0.701027 0.46213  0.72829  -0.201753   0.169034    -0.0145857  27  SER   B H    
194  H HA   . SER   A 15  ? 0.833922 0.509821 0.819578 -0.216866   0.184887    0.0651125   27  SER   B HA   
195  H HB2  . SER   A 15  ? 0.740323 0.495177 0.869987 -0.251063   0.175448    -0.0051957  27  SER   B HB2  
196  H HB3  . SER   A 15  ? 0.818459 0.518946 0.94425  -0.268462   0.185252    0.0420399   27  SER   B HB3  
198  N N    . LYS   A 16  ? 0.73981  0.578054 0.781305 -0.228902   0.237567    0.043154    28  LYS   B N    
199  C CA   . LYS   A 16  ? 0.790809 0.69493  0.850681 -0.235399   0.27199     0.0594226   28  LYS   B CA   
200  C C    . LYS   A 16  ? 0.798243 0.705747 0.773568 -0.203321   0.294999    0.0793439   28  LYS   B C    
201  O O    . LYS   A 16  ? 0.798685 0.757682 0.779627 -0.203065   0.329824    0.0995593   28  LYS   B O    
202  C CB   . LYS   A 16  ? 0.775217 0.74889  0.890676 -0.237528   0.266311    0.0232163   28  LYS   B CB   
203  C CG   . LYS   A 16  ? 0.801431 0.786772 1.00476  -0.27289    0.250107    0.00466991  28  LYS   B CG   
204  C CD   . LYS   A 16  ? 0.802984 0.871824 1.06402  -0.27845    0.248828    -0.0220017  28  LYS   B CD   
205  C CE   . LYS   A 16  ? 0.806626 0.883142 1.04506  -0.253795   0.224407    -0.0619765  28  LYS   B CE   
206  N NZ   . LYS   A 16  ? 0.827569 0.959756 1.13204  -0.269627   0.208097    -0.0933322  28  LYS   B NZ   
207  H H    . LYS   A 16  ? 0.714138 0.558606 0.75806  -0.219192   0.221686    0.0160189   28  LYS   B H    
208  H HA   . LYS   A 16  ? 0.814972 0.717203 0.90802  -0.25909    0.284062    0.0817264   28  LYS   B HA   
209  H HB2  . LYS   A 16  ? 0.744444 0.710196 0.833036 -0.218394   0.250806    0.00126181  28  LYS   B HB2  
210  H HB3  . LYS   A 16  ? 0.771418 0.792499 0.890253 -0.232532   0.287935    0.0325854   28  LYS   B HB3  
211  H HG2  . LYS   A 16  ? 0.837751 0.810309 1.06542  -0.294961   0.260977    0.0287238   28  LYS   B HG2  
212  H HG3  . LYS   A 16  ? 0.793963 0.741311 0.993261 -0.270531   0.227445    -0.0141008  28  LYS   B HG3  
213  H HD2  . LYS   A 16  ? 0.804838 0.916316 1.06187  -0.270832   0.270834    -0.00650293 28  LYS   B HD2  
214  H HD3  . LYS   A 16  ? 0.812199 0.889859 1.13167  -0.306078   0.242394    -0.0271359  28  LYS   B HD3  
215  H HE2  . LYS   A 16  ? 0.804746 0.833094 1.02241  -0.249941   0.209341    -0.0709443  28  LYS   B HE2  
216  H HE3  . LYS   A 16  ? 0.793063 0.886094 0.992914 -0.230052   0.233668    -0.0584354  28  LYS   B HE3  
217  H HZ1  . LYS   A 16  ? 0.826292 0.937098 1.16376  -0.290567   0.196591    -0.101309   28  LYS   B HZ1  
218  H HZ2  . LYS   A 16  ? 0.81158  0.99268  1.14361  -0.274647   0.220398    -0.084648   28  LYS   B HZ2  
219  H HZ3  . LYS   A 16  ? 0.78924  0.928917 1.07426  -0.252864   0.196122    -0.114132   28  LYS   B HZ3  
220  N N    . LYS   A 17  ? 0.791478 0.646717 0.692045 -0.175881   0.274767    0.0711677   29  LYS   B N    
221  C CA   . LYS   A 17  ? 0.841442 0.686075 0.651355 -0.143061   0.289296    0.0828319   29  LYS   B CA   
222  C C    . LYS   A 17  ? 0.801899 0.711083 0.614447 -0.123467   0.310287    0.0667252   29  LYS   B C    
223  O O    . LYS   A 17  ? 0.81524  0.753138 0.593091 -0.106927   0.344733    0.0859679   29  LYS   B O    
224  C CB   . LYS   A 17  ? 0.942548 0.766603 0.709217 -0.146225   0.316797    0.129671    29  LYS   B CB   
225  C CG   . LYS   A 17  ? 1.02019  0.768619 0.763417 -0.154684   0.291233    0.148294    29  LYS   B CG   
226  C CD   . LYS   A 17  ? 1.05152  0.747618 0.712842 -0.123114   0.257722    0.131134    29  LYS   B CD   
227  C CE   . LYS   A 17  ? 1.12008  0.7483   0.762424 -0.126673   0.228178    0.149159    29  LYS   B CE   
228  N NZ   . LYS   A 17  ? 1.06363  0.686833 0.783264 -0.140869   0.19602     0.118167    29  LYS   B NZ   
229  H H    . LYS   A 17  ? 0.780576 0.606745 0.688266 -0.177329   0.250081    0.0558221   29  LYS   B H    
230  H HA   . LYS   A 17  ? 0.842651 0.648285 0.614469 -0.129148   0.265397    0.0697012   29  LYS   B HA   
231  H HB2  . LYS   A 17  ? 0.94602  0.807911 0.760698 -0.165576   0.340382    0.145532    29  LYS   B HB2  
232  H HB3  . LYS   A 17  ? 0.977902 0.801622 0.681702 -0.121759   0.329405    0.13405     29  LYS   B HB3  
233  H HG2  . LYS   A 17  ? 0.982814 0.725823 0.785115 -0.174088   0.274922    0.137498    29  LYS   B HG2  
234  H HG3  . LYS   A 17  ? 1.0713   0.810142 0.795103 -0.160937   0.311838    0.182727    29  LYS   B HG3  
235  H HD2  . LYS   A 17  ? 1.09241  0.789602 0.690705 -0.102798   0.272167    0.138652    29  LYS   B HD2  
236  H HD3  . LYS   A 17  ? 1.00035  0.706927 0.683561 -0.119042   0.240087    0.100003    29  LYS   B HD3  
237  H HE2  . LYS   A 17  ? 1.1591   0.77737  0.80576  -0.13982    0.244634    0.180983    29  LYS   B HE2  
238  H HE3  . LYS   A 17  ? 1.15263  0.750829 0.729661 -0.105509   0.212699    0.148334    29  LYS   B HE3  
239  H HZ1  . LYS   A 17  ? 1.02846  0.679569 0.804572 -0.158948   0.207802    0.11397     29  LYS   B HZ1  
240  H HZ2  . LYS   A 17  ? 1.02681  0.656799 0.739771 -0.129259   0.181343    0.0925642   29  LYS   B HZ2  
241  H HZ3  . LYS   A 17  ? 1.08705  0.671832 0.80494  -0.142331   0.178273    0.128492    29  LYS   B HZ3  
242  N N    . ASP   A 18  ? 0.711073 0.64104  0.560067 -0.121325   0.289595    0.0321108   30  ASP   B N    
243  C CA   . ASP   A 18  ? 0.68347  0.669316 0.540064 -0.1004     0.301485    0.0150717   30  ASP   B CA   
244  C C    . ASP   A 18  ? 0.672497 0.617495 0.463646 -0.0692195  0.281442    -0.00734592 30  ASP   B C    
245  O O    . ASP   A 18  ? 0.642471 0.61676  0.441003 -0.0521689  0.280608    -0.0252667  30  ASP   B O    
246  C CB   . ASP   A 18  ? 0.629076 0.67298  0.574978 -0.121452   0.293806    -0.00312041 30  ASP   B CB   
247  C CG   . ASP   A 18  ? 0.602546 0.61504  0.571963 -0.135523   0.258397    -0.0287742  30  ASP   B CG   
248  O OD1  . ASP   A 18  ? 0.574623 0.530623 0.495525 -0.123754   0.239492    -0.0360339  30  ASP   B OD1  
249  O OD2  . ASP   A 18  ? 0.61466  0.662126 0.652958 -0.158289   0.249935    -0.042382   30  ASP   B OD2  
250  H H    . ASP   A 18  ? 0.695373 0.602975 0.563451 -0.131439   0.267121    0.0194604   30  ASP   B H    
251  H HA   . ASP   A 18  ? 0.71021  0.723824 0.555917 -0.0916338  0.328313    0.0312139   30  ASP   B HA   
252  H HB2  . ASP   A 18  ? 0.615881 0.696546 0.564039 -0.104412   0.299597    -0.0126687  30  ASP   B HB2  
253  H HB3  . ASP   A 18  ? 0.637608 0.708226 0.627394 -0.142487   0.30695     0.0111444   30  ASP   B HB3  
254  N N    . ARG   A 19  ? 0.722667 0.598191 0.452872 -0.0629239  0.26235     -0.00541739 31  ARG   B N    
255  C CA   . ARG   A 19  ? 0.728221 0.55716  0.404536 -0.0412765  0.237481    -0.0269949  31  ARG   B CA   
256  C C    . ARG   A 19  ? 0.689353 0.533637 0.412516 -0.047858   0.218757    -0.0514489  31  ARG   B C    
257  O O    . ARG   A 19  ? 0.688365 0.512555 0.379472 -0.0289476  0.208518    -0.0667067  31  ARG   B O    
258  C CB   . ARG   A 19  ? 0.784106 0.603021 0.386017 -0.00421914 0.253102    -0.0295209  31  ARG   B CB   
259  C CG   . ARG   A 19  ? 0.846639 0.64314  0.381346 0.00754985  0.271171    -0.00656123 31  ARG   B CG   
260  C CD   . ARG   A 19  ? 0.909747 0.700711 0.368341 0.0502877   0.290459    -0.0149634  31  ARG   B CD   
261  N NE   . ARG   A 19  ? 0.924027 0.658475 0.337812 0.0691596   0.258194    -0.0452888  31  ARG   B NE   
262  C CZ   . ARG   A 19  ? 1.00642  0.6685   0.351155 0.0758105   0.226755    -0.0557048  31  ARG   B CZ   
263  N NH1  . ARG   A 19  ? 1.05599  0.691468 0.360464 0.0696005   0.220621    -0.0381106  31  ARG   B NH1  
264  N NH2  . ARG   A 19  ? 1.06227  0.674434 0.37448  0.0896952   0.198563    -0.0834543  31  ARG   B NH2  
265  H H    . ARG   A 19  ? 0.744481 0.600169 0.467939 -0.0733316  0.26343     0.0108557   31  ARG   B H    
266  H HA   . ARG   A 19  ? 0.753811 0.540615 0.406815 -0.045679   0.219972    -0.0240905  31  ARG   B HA   
267  H HB2  . ARG   A 19  ? 0.765298 0.628222 0.390773 0.00377993  0.271273    -0.0309693  31  ARG   B HB2  
268  H HB3  . ARG   A 19  ? 0.787778 0.570685 0.360163 0.00623576  0.233168    -0.045428   31  ARG   B HB3  
269  H HG2  . ARG   A 19  ? 0.874064 0.624866 0.379506 0.00315926  0.24935     -0.00574006 31  ARG   B HG2  
270  H HG3  . ARG   A 19  ? 0.847085 0.677531 0.414476 -0.00633365 0.292308    0.0130499   31  ARG   B HG3  
271  H HD2  . ARG   A 19  ? 0.966694 0.742352 0.373964 0.0597287   0.302542    -0.00093438 31  ARG   B HD2  
272  H HD3  . ARG   A 19  ? 0.890243 0.731895 0.381675 0.0567341   0.313676    -0.0133596  31  ARG   B HD3  
273  H HE   . ARG   A 19  ? 0.905611 0.653814 0.340774 0.0755919   0.257898    -0.0570144  31  ARG   B HE   
274  H HH11 . ARG   A 19  ? 1.03027  0.683422 0.371874 0.0495659   0.224585    -0.0211917  31  ARG   B HH11 
275  H HH12 . ARG   A 19  ? 1.11567  0.713028 0.353828 0.0864384   0.211088    -0.0434568  31  ARG   B HH12 
276  H HH21 . ARG   A 19  ? 1.03642  0.658509 0.360475 0.100145    0.204484    -0.0933183  31  ARG   B HH21 
277  H HH22 . ARG   A 19  ? 1.07913  0.647372 0.359564 0.0879179   0.172857    -0.0913859  31  ARG   B HH22 
278  N N    . GLY   A 20  ? 0.636433 0.508315 0.429987 -0.0745601  0.212926    -0.0550161  32  GLY   B N    
279  C CA   . GLY   A 20  ? 0.574123 0.467431 0.405822 -0.0788709  0.199499    -0.0768322  32  GLY   B CA   
280  C C    . GLY   A 20  ? 0.567228 0.414312 0.386664 -0.0815792  0.173028    -0.0888014  32  GLY   B C    
281  O O    . GLY   A 20  ? 0.573731 0.425486 0.397546 -0.0769926  0.165152    -0.102484   32  GLY   B O    
282  H H    . GLY   A 20  ? 0.640137 0.51414  0.454284 -0.0892971  0.217127    -0.0438729  32  GLY   B H    
283  H HA2  . GLY   A 20  ? 0.575431 0.487461 0.395984 -0.0634517  0.206531    -0.0809707  32  GLY   B HA2  
284  H HA3  . GLY   A 20  ? 0.553239 0.475468 0.43206  -0.0949395  0.200976    -0.0794597  32  GLY   B HA3  
285  N N    . VAL   A 21  ? 0.594949 0.400673 0.401125 -0.0886639  0.159997    -0.0805973  33  VAL   B N    
286  C CA   . VAL   A 21  ? 0.649005 0.41782  0.452854 -0.091474   0.133149    -0.0899943  33  VAL   B CA   
287  C C    . VAL   A 21  ? 0.688462 0.406977 0.431583 -0.0806408  0.120702    -0.0783852  33  VAL   B C    
288  O O    . VAL   A 21  ? 0.742614 0.448774 0.475873 -0.0838955  0.123995    -0.0605071  33  VAL   B O    
289  C CB   . VAL   A 21  ? 0.607952 0.383645 0.472422 -0.109424   0.120991    -0.0973166  33  VAL   B CB   
290  C CG1  . VAL   A 21  ? 0.628272 0.381787 0.498754 -0.109027   0.0968128   -0.107758   33  VAL   B CG1  
291  C CG2  . VAL   A 21  ? 0.579347 0.403748 0.495608 -0.119176   0.132887    -0.111256   33  VAL   B CG2  
292  H H    . VAL   A 21  ? 0.627119 0.429783 0.427576 -0.0916759  0.168037    -0.0670612  33  VAL   B H    
293  H HA   . VAL   A 21  ? 0.621198 0.391878 0.420172 -0.0862434  0.129945    -0.0996796  33  VAL   B HA   
294  H HB   . VAL   A 21  ? 0.637562 0.398577 0.502098 -0.113692   0.120001    -0.0856938  33  VAL   B HB   
295  H HG11 . VAL   A 21  ? 0.609981 0.371468 0.474837 -0.10584    0.0986945   -0.114971   33  VAL   B HG11 
296  H HG12 . VAL   A 21  ? 0.653029 0.375757 0.49428  -0.104153   0.0841814   -0.100485   33  VAL   B HG12 
297  H HG13 . VAL   A 21  ? 0.603204 0.366113 0.513781 -0.116443   0.0916747   -0.114387   33  VAL   B HG13 
298  H HG21 . VAL   A 21  ? 0.564635 0.388253 0.513821 -0.127339   0.12496     -0.118838   33  VAL   B HG21 
299  H HG22 . VAL   A 21  ? 0.577975 0.419774 0.49865  -0.122059   0.145723    -0.1045     33  VAL   B HG22 
300  H HG23 . VAL   A 21  ? 0.559706 0.398495 0.471222 -0.113538   0.134754    -0.119609   33  VAL   B HG23 
301  N N    . LEU   A 22  ? 0.713598 0.400729 0.412205 -0.0675564  0.10632     -0.087878   34  LEU   B N    
302  C CA   . LEU   A 22  ? 0.770779 0.406423 0.402712 -0.0547754  0.0870404   -0.0844881  34  LEU   B CA   
303  C C    . LEU   A 22  ? 0.785648 0.394184 0.435518 -0.0639458  0.0491728   -0.0965964  34  LEU   B C    
304  O O    . LEU   A 22  ? 0.739104 0.357735 0.425208 -0.0725581  0.0432438   -0.110082   34  LEU   B O    
305  C CB   . LEU   A 22  ? 0.839209 0.45632  0.404833 -0.0308112  0.0974768   -0.0911997  34  LEU   B CB   
306  C CG   . LEU   A 22  ? 0.838933 0.491011 0.387459 -0.0163553  0.13664     -0.0786519  34  LEU   B CG   
307  C CD1  . LEU   A 22  ? 0.889072 0.527085 0.385103 0.0124558   0.146514    -0.0910293  34  LEU   B CD1  
308  C CD2  . LEU   A 22  ? 0.862298 0.503824 0.372913 -0.0135178  0.14538     -0.056677   34  LEU   B CD2  
309  H H    . LEU   A 22  ? 0.692804 0.388781 0.401559 -0.0666573  0.107088    -0.0974955  34  LEU   B H    
310  H HA   . LEU   A 22  ? 0.801939 0.433373 0.420817 -0.0545     0.0916316   -0.0700964  34  LEU   B HA   
311  H HB2  . LEU   A 22  ? 0.812272 0.430293 0.393211 -0.0319255  0.0933784   -0.102752   34  LEU   B HB2  
312  H HB3  . LEU   A 22  ? 0.881986 0.460744 0.398743 -0.0216369  0.0807364   -0.0936735  34  LEU   B HB3  
313  H HG   . LEU   A 22  ? 0.789306 0.481595 0.390283 -0.0278871  0.1494      -0.0761174  34  LEU   B HG   
314  H HD11 . LEU   A 22  ? 0.85766  0.498964 0.378687 0.00939488  0.140608    -0.101058   34  LEU   B HD11 
315  H HD12 . LEU   A 22  ? 0.889376 0.557552 0.381371 0.0231811   0.172587    -0.0827722  34  LEU   B HD12 
316  H HD13 . LEU   A 22  ? 0.938428 0.533356 0.380112 0.024258    0.132181    -0.0972356  34  LEU   B HD13 
317  H HD21 . LEU   A 22  ? 0.846353 0.49673  0.396527 -0.0310696  0.141009    -0.0477336  34  LEU   B HD21 
318  H HD22 . LEU   A 22  ? 0.920015 0.521126 0.377426 -0.00268399 0.12815     -0.0601584  34  LEU   B HD22 
319  H HD23 . LEU   A 22  ? 0.881668 0.547639 0.380754 -0.00419835 0.172593    -0.0472487  34  LEU   B HD23 
320  N N    . LYS   A 23  ? 0.84726  0.422936 0.469332 -0.0608676  0.0236096   -0.0896587  35  LYS   B N    
321  C CA   . LYS   A 23  ? 0.863    0.424927 0.517521 -0.0699879  -0.0154295  -0.0993789  35  LYS   B CA   
322  C C    . LYS   A 23  ? 0.987892 0.498733 0.571819 -0.056921   -0.0513385  -0.103648   35  LYS   B C    
323  O O    . LYS   A 23  ? 1.06728  0.554018 0.583389 -0.0411037  -0.0489622  -0.0891834  35  LYS   B O    
324  C CB   . LYS   A 23  ? 0.862074 0.438947 0.568965 -0.0776767  -0.0220664  -0.0874921  35  LYS   B CB   
325  C CG   . LYS   A 23  ? 0.860618 0.439669 0.620443 -0.0844515  -0.0593489  -0.097643   35  LYS   B CG   
326  C CD   . LYS   A 23  ? 0.838633 0.424264 0.644953 -0.0839854  -0.0692255  -0.0864885  35  LYS   B CD   
327  C CE   . LYS   A 23  ? 0.810309 0.415144 0.685913 -0.0881213  -0.100503   -0.0995131  35  LYS   B CE   
328  N NZ   . LYS   A 23  ? 0.840351 0.435728 0.741785 -0.0779056  -0.123569   -0.0881818  35  LYS   B NZ   
329  H H    . LYS   A 23  ? 0.881879 0.446091 0.464574 -0.0521156  0.0306101   -0.0774043  35  LYS   B H    
330  H HA   . LYS   A 23  ? 0.839163 0.414905 0.529224 -0.0787645  -0.0165811  -0.110958   35  LYS   B HA   
331  H HB2  . LYS   A 23  ? 0.816059 0.421813 0.562679 -0.0851638  -0.00042949 -0.0868669  35  LYS   B HB2  
332  H HB3  . LYS   A 23  ? 0.899288 0.456562 0.567457 -0.0695643  -0.0225361  -0.072711   35  LYS   B HB3  
333  H HG2  . LYS   A 23  ? 0.898999 0.451346 0.622411 -0.0786945  -0.0845255  -0.101028   35  LYS   B HG2  
334  H HG3  . LYS   A 23  ? 0.816068 0.419015 0.618356 -0.0940531  -0.054025   -0.10929    35  LYS   B HG3  
335  H HD2  . LYS   A 23  ? 0.806288 0.411695 0.641694 -0.0892662  -0.0452281  -0.0844715  35  LYS   B HD2  
336  H HD3  . LYS   A 23  ? 0.887591 0.444819 0.649551 -0.0744363  -0.0787852  -0.0720433  35  LYS   B HD3  
337  H HE2  . LYS   A 23  ? 0.837474 0.430936 0.694986 -0.0883762  -0.122149   -0.106465   35  LYS   B HE2  
338  H HE3  . LYS   A 23  ? 0.766941 0.404155 0.692424 -0.0969333  -0.084729   -0.109538   35  LYS   B HE3  
339  H HZ1  . LYS   A 23  ? 0.888001 0.453158 0.740376 -0.0688702  -0.140722   -0.0774652  35  LYS   B HZ1  
340  H HZ2  . LYS   A 23  ? 0.824376 0.423502 0.741179 -0.0783514  -0.104883   -0.0821504  35  LYS   B HZ2  
341  H HZ3  . LYS   A 23  ? 0.824348 0.439618 0.775786 -0.0791     -0.140195   -0.0975343  35  LYS   B HZ3  
342  N N    . ILE   A 24  ? 0.977784 0.474486 0.581275 -0.0653536  -0.0856597  -0.122626   36  ILE   B N    
343  C CA   . ILE   A 24  ? 1.02177  0.4784   0.58541  -0.0591232  -0.134526   -0.130813   36  ILE   B CA   
344  C C    . ILE   A 24  ? 0.977053 0.461129 0.632865 -0.0776129  -0.166785   -0.136547   36  ILE   B C    
345  O O    . ILE   A 24  ? 0.918185 0.435409 0.648942 -0.0966084  -0.156981   -0.144444   36  ILE   B O    
346  C CB   . ILE   A 24  ? 1.09523  0.503765 0.591591 -0.0513039  -0.151255   -0.152703   36  ILE   B CB   
347  C CG1  . ILE   A 24  ? 1.14832  0.535529 0.55361  -0.0257451  -0.116845   -0.148103   36  ILE   B CG1  
348  C CG2  . ILE   A 24  ? 1.18119  0.549021 0.642287 -0.0482637  -0.210931   -0.1681     36  ILE   B CG2  
349  C CD1  . ILE   A 24  ? 1.2026   0.539916 0.544963 -0.0132671  -0.126621   -0.173291   36  ILE   B CD1  
350  H H    . ILE   A 24  ? 0.938382 0.452096 0.582532 -0.076248   -0.0790689  -0.130242   36  ILE   B H    
351  H HA   . ILE   A 24  ? 1.06298  0.506425 0.583982 -0.0465257  -0.13634    -0.118233   36  ILE   B HA   
352  H HB   . ILE   A 24  ? 1.06382  0.482195 0.601936 -0.0645841  -0.14605    -0.16126    36  ILE   B HB   
353  H HG12 . ILE   A 24  ? 1.18621  0.5614   0.543344 -0.0125696  -0.120671   -0.137878   36  ILE   B HG12 
354  H HG13 . ILE   A 24  ? 1.09294  0.512174 0.527924 -0.0286221  -0.0824389  -0.137775   36  ILE   B HG13 
355  H HG21 . ILE   A 24  ? 1.22482  0.557404 0.643217 -0.0439351  -0.222278   -0.185251   36  ILE   B HG21 
356  H HG22 . ILE   A 24  ? 1.21849  0.574892 0.632428 -0.0333378  -0.217606   -0.157791   36  ILE   B HG22 
357  H HG23 . ILE   A 24  ? 1.15035  0.539009 0.678904 -0.0648903  -0.232082   -0.17128    36  ILE   B HG23 
358  H HD11 . ILE   A 24  ? 1.16986  0.514035 0.558956 -0.0272413  -0.124149   -0.180476   36  ILE   B HD11 
359  H HD12 . ILE   A 24  ? 1.22696  0.559602 0.518654 0.00590852  -0.0996084  -0.16954    36  ILE   B HD12 
360  H HD13 . ILE   A 24  ? 1.26549  0.567395 0.570409 -0.0092562  -0.162401   -0.186228   36  ILE   B HD13 
361  N N    . VAL   A 25  ? 0.998867 0.472798 0.648039 -0.0691991  -0.202774   -0.129683   37  VAL   B N    
362  C CA   . VAL   A 25  ? 0.993851 0.491176 0.721352 -0.0800877  -0.244725   -0.137882   37  VAL   B CA   
363  C C    . VAL   A 25  ? 1.06882  0.537999 0.77782  -0.088369   -0.289228   -0.161632   37  VAL   B C    
364  O O    . VAL   A 25  ? 1.14784  0.56555  0.761414 -0.0722333  -0.316591   -0.168437   37  VAL   B O    
365  C CB   . VAL   A 25  ? 1.03752  0.526479 0.750699 -0.06164    -0.269298   -0.119376   37  VAL   B CB   
366  C CG1  . VAL   A 25  ? 1.04105  0.554096 0.828041 -0.0646443  -0.322263   -0.127652   37  VAL   B CG1  
367  C CG2  . VAL   A 25  ? 1.00494  0.512998 0.744091 -0.0581345  -0.226147   -0.0974149  37  VAL   B CG2  
368  H H    . VAL   A 25  ? 1.04416  0.497208 0.637238 -0.0547665  -0.200957   -0.118      37  VAL   B H    
369  H HA   . VAL   A 25  ? 0.937777 0.473195 0.737538 -0.0927533  -0.227528   -0.139084   37  VAL   B HA   
370  H HB   . VAL   A 25  ? 1.10205  0.55289  0.73281  -0.0477153  -0.280326   -0.115398   37  VAL   B HB   
371  H HG11 . VAL   A 25  ? 0.984452 0.538031 0.852554 -0.0783058  -0.310842   -0.133721   37  VAL   B HG11 
372  H HG12 . VAL   A 25  ? 1.0862   0.580939 0.847613 -0.0665065  -0.355131   -0.141014   37  VAL   B HG12 
373  H HG13 . VAL   A 25  ? 1.06573  0.572854 0.845474 -0.0502153  -0.335102   -0.113423   37  VAL   B HG13 
374  H HG21 . VAL   A 25  ? 1.02572  0.526602 0.767295 -0.0477201  -0.243776   -0.0849753  37  VAL   B HG21 
375  H HG22 . VAL   A 25  ? 1.01112  0.502734 0.696602 -0.0539092  -0.199009   -0.0892358  37  VAL   B HG22 
376  H HG23 . VAL   A 25  ? 0.940714 0.483995 0.748152 -0.0701455  -0.208951   -0.10425    37  VAL   B HG23 
377  N N    . LYS   A 26  ? 1.03195  0.533357 0.830651 -0.114337   -0.295708   -0.174601   38  LYS   B N    
378  C CA   . LYS   A 26  ? 1.08281  0.556987 0.88147  -0.130074   -0.339277   -0.197308   38  LYS   B CA   
379  C C    . LYS   A 26  ? 1.10518  0.612147 0.983074 -0.140531   -0.394676   -0.204323   38  LYS   B C    
380  O O    . LYS   A 26  ? 1.15463  0.628339 1.0042   -0.143469   -0.449345   -0.223095   38  LYS   B O    
381  C CB   . LYS   A 26  ? 1.04915  0.528636 0.884777 -0.153389   -0.305883   -0.202077   38  LYS   B CB   
382  C CG   . LYS   A 26  ? 1.05044  0.486356 0.79317  -0.13692    -0.266159   -0.200575   38  LYS   B CG   
383  C CD   . LYS   A 26  ? 1.17234  0.534537 0.803122 -0.117597   -0.301041   -0.218959   38  LYS   B CD   
384  C CE   . LYS   A 26  ? 1.20018  0.507796 0.765042 -0.110796   -0.284613   -0.232239   38  LYS   B CE   
385  N NZ   . LYS   A 26  ? 1.30049  0.537945 0.760268 -0.0902366  -0.324788   -0.256147   38  LYS   B NZ   
386  H H    . LYS   A 26  ? 0.971737 0.512211 0.833071 -0.123286   -0.272002   -0.16899    38  LYS   B H    
387  H HA   . LYS   A 26  ? 1.14956  0.575734 0.863055 -0.115886   -0.354136   -0.204534   38  LYS   B HA   
388  H HB2  . LYS   A 26  ? 0.982441 0.509571 0.887248 -0.163053   -0.281388   -0.192445   38  LYS   B HB2  
389  H HB3  . LYS   A 26  ? 1.07603  0.541622 0.93198  -0.169799   -0.334857   -0.215425   38  LYS   B HB3  
390  H HG2  . LYS   A 26  ? 1.0253   0.479254 0.755193 -0.12389    -0.23723    -0.186979   38  LYS   B HG2  
391  H HG3  . LYS   A 26  ? 1.03651  0.47474  0.805425 -0.150633   -0.24831    -0.20178    38  LYS   B HG3  
392  H HD2  . LYS   A 26  ? 1.20134  0.554421 0.849973 -0.127432   -0.344052   -0.231503   38  LYS   B HD2  
393  H HD3  . LYS   A 26  ? 1.18134  0.53916  0.761185 -0.0968851  -0.296117   -0.210422   38  LYS   B HD3  
394  H HE2  . LYS   A 26  ? 1.17386  0.49146  0.715051 -0.0972963  -0.245315   -0.220621   38  LYS   B HE2  
395  H HE3  . LYS   A 26  ? 1.18739  0.495159 0.801323 -0.1319     -0.2864     -0.236871   38  LYS   B HE3  
396  H HZ1  . LYS   A 26  ? 1.32186  0.56037  0.733849 -0.0707075  -0.322125   -0.249064   38  LYS   B HZ1  
397  H HZ2  . LYS   A 26  ? 1.33488  0.561921 0.817738 -0.104089   -0.364803   -0.269298   38  LYS   B HZ2  
398  H HZ3  . LYS   A 26  ? 1.33453  0.536618 0.751689 -0.0820274  -0.313167   -0.265524   38  LYS   B HZ3  
399  N N    . ARG   A 27  ? 1.05934  0.631822 1.03496  -0.142757   -0.383949   -0.19168    39  ARG   B N    
400  C CA   . ARG   A 27  ? 1.055    0.665959 1.10691  -0.143605   -0.436329   -0.19586    39  ARG   B CA   
401  C C    . ARG   A 27  ? 1.03352  0.673088 1.10837  -0.117935   -0.42406    -0.176242   39  ARG   B C    
402  O O    . ARG   A 27  ? 1.00621  0.675755 1.11846  -0.11754    -0.372467   -0.165923   39  ARG   B O    
403  C CB   . ARG   A 27  ? 1.00005  0.674285 1.18504  -0.177806   -0.44077    -0.205005   39  ARG   B CB   
404  C CG   . ARG   A 27  ? 1.01208  0.732522 1.28517  -0.181062   -0.502713   -0.213238   39  ARG   B CG   
405  C CD   . ARG   A 27  ? 0.954794 0.758046 1.37868  -0.214465   -0.492376   -0.215689   39  ARG   B CD   
406  N NE   . ARG   A 27  ? 0.88443  0.751905 1.37835  -0.205096   -0.434651   -0.200676   39  ARG   B NE   
407  C CZ   . ARG   A 27  ? 0.825927 0.761987 1.42406  -0.229215   -0.395061   -0.196867   39  ARG   B CZ   
408  N NH1  . ARG   A 27  ? 0.847488 0.796013 1.49865  -0.269159   -0.402586   -0.201444   39  ARG   B NH1  
409  N NH2  . ARG   A 27  ? 0.756177 0.744288 1.40099  -0.21378    -0.34614    -0.18809    39  ARG   B NH2  
410  H H    . ARG   A 27  ? 0.9979   0.592724 0.994472 -0.142201   -0.344234   -0.181781   39  ARG   B H    
411  H HA   . ARG   A 27  ? 1.12524  0.700834 1.12512  -0.136837   -0.478848   -0.204989   39  ARG   B HA   
412  H HB2  . ARG   A 27  ? 1.0182   0.666806 1.18651  -0.196097   -0.441197   -0.21429    39  ARG   B HB2  
413  H HB3  . ARG   A 27  ? 0.938832 0.65209  1.17318  -0.180479   -0.400098   -0.195751   39  ARG   B HB3  
414  H HG2  . ARG   A 27  ? 1.01047  0.744734 1.28625  -0.157844   -0.508384   -0.204024   39  ARG   B HG2  
415  H HG3  . ARG   A 27  ? 1.07817  0.761728 1.30773  -0.183118   -0.546475   -0.22599    39  ARG   B HG3  
416  H HD2  . ARG   A 27  ? 0.982442 0.814385 1.4622   -0.218519   -0.537193   -0.223144   39  ARG   B HD2  
417  H HD3  . ARG   A 27  ? 0.9627   0.748142 1.38253  -0.238517   -0.480807   -0.220428   39  ARG   B HD3  
418  H HE   . ARG   A 27  ? 0.873405 0.732302 1.33615  -0.181578   -0.425167   -0.193993   39  ARG   B HE   
419  H HH11 . ARG   A 27  ? 0.885931 0.823472 1.54713  -0.280601   -0.445927   -0.210815   39  ARG   B HH11 
420  H HH12 . ARG   A 27  ? 0.816133 0.782982 1.49299  -0.284821   -0.364908   -0.194577   39  ARG   B HH12 
421  H HH21 . ARG   A 27  ? 0.751486 0.718139 1.349    -0.191732   -0.332699   -0.184399   39  ARG   B HH21 
422  H HH22 . ARG   A 27  ? 0.729619 0.773394 1.45248  -0.225661   -0.326717   -0.186479   39  ARG   B HH22 
423  N N    . VAL   A 28  ? 1.10799  0.731513 1.1538   -0.0949661  -0.474232   -0.171687   40  VAL   B N    
424  C CA   . VAL   A 28  ? 1.11798  0.744875 1.16224  -0.0665559  -0.466992   -0.149377   40  VAL   B CA   
425  C C    . VAL   A 28  ? 1.0974   0.801953 1.28501  -0.0684926  -0.467032   -0.151229   40  VAL   B C    
426  O O    . VAL   A 28  ? 1.12261  0.874643 1.39609  -0.08166    -0.504757   -0.1659     40  VAL   B O    
427  C CB   . VAL   A 28  ? 1.19959  0.776625 1.15241  -0.0378909  -0.521504   -0.139178   40  VAL   B CB   
428  C CG1  . VAL   A 28  ? 1.24195  0.849398 1.25513  -0.0376915  -0.595869   -0.154656   40  VAL   B CG1  
429  C CG2  . VAL   A 28  ? 1.20557  0.763821 1.13178  -0.00923459 -0.50474    -0.108178   40  VAL   B CG2  
430  H H    . VAL   A 28  ? 1.15936  0.766065 1.18397  -0.0967018  -0.516197   -0.182663   40  VAL   B H    
431  H HA   . VAL   A 28  ? 1.09583  0.706474 1.10426  -0.063756   -0.424427   -0.139211   40  VAL   B HA   
432  H HB   . VAL   A 28  ? 1.2443   0.776951 1.10776  -0.0375848  -0.51994    -0.142376   40  VAL   B HB   
433  H HG11 . VAL   A 28  ? 1.20977  0.861639 1.30756  -0.0321728  -0.59961    -0.14988    40  VAL   B HG11 
434  H HG12 . VAL   A 28  ? 1.23316  0.853561 1.27537  -0.060536   -0.604782   -0.17384    40  VAL   B HG12 
435  H HG13 . VAL   A 28  ? 1.31666  0.886555 1.25527  -0.0195264  -0.631882   -0.15015    40  VAL   B HG13 
436  H HG21 . VAL   A 28  ? 1.28018  0.80305  1.1383   0.0091005   -0.536826   -0.0981451  40  VAL   B HG21 
437  H HG22 . VAL   A 28  ? 1.18272  0.724462 1.07555  -0.0124533  -0.459484   -0.0994216  40  VAL   B HG22 
438  H HG23 . VAL   A 28  ? 1.17371  0.770819 1.18446  -0.00558774 -0.507667   -0.106857   40  VAL   B HG23 
439  N N    . GLY   A 29  ? 1.10209  0.8195   1.31554  -0.0554187  -0.423529   -0.137975   41  GLY   B N    
440  C CA   . GLY   A 29  ? 1.0728   0.853341 1.40502  -0.0442525  -0.420966   -0.139428   41  GLY   B CA   
441  C C    . GLY   A 29  ? 1.11705  0.887219 1.45559  -0.0105572  -0.474805   -0.127263   41  GLY   B C    
442  O O    . GLY   A 29  ? 1.19664  0.925451 1.46255  -0.00102683 -0.524767   -0.121333   41  GLY   B O    
443  H H    . GLY   A 29  ? 1.08878  0.773528 1.24318  -0.052588   -0.394146   -0.129087   41  GLY   B H    
444  H HA2  . GLY   A 29  ? 1.03541  0.865717 1.44149  -0.0602887  -0.423892   -0.152244   41  GLY   B HA2  
445  H HA3  . GLY   A 29  ? 1.02833  0.810448 1.36601  -0.0416077  -0.37999    -0.135754   41  GLY   B HA3  
446  N N    . ASN   A 30  ? 1.08279  0.888332 1.50463  0.0109039   -0.465064   -0.124427   42  ASN   B N    
447  C CA   . ASN   A 30  ? 1.12661  0.922199 1.56567  0.0485247   -0.512272   -0.110529   42  ASN   B CA   
448  C C    . ASN   A 30  ? 1.09605  0.879484 1.56339  0.0712707   -0.474187   -0.102054   42  ASN   B C    
449  O O    . ASN   A 30  ? 0.998544 0.799962 1.49072  0.0563924   -0.417584   -0.11366    42  ASN   B O    
450  C CB   . ASN   A 30  ? 1.15534  1.03216  1.71427  0.0528532   -0.560519   -0.126227   42  ASN   B CB   
451  C CG   . ASN   A 30  ? 1.09137  1.05582  1.76976  0.0297197   -0.516885   -0.147833   42  ASN   B CG   
452  O OD1  . ASN   A 30  ? 1.06864  1.06614  1.81428  0.0467825   -0.48011    -0.151705   42  ASN   B OD1  
453  N ND2  . ASN   A 30  ? 1.08055  1.078    1.78087  -0.00835191 -0.517755   -0.161502   42  ASN   B ND2  
454  H H    . ASN   A 30  ? 1.03027  0.865513 1.49812  0.0038406   -0.427231   -0.131938   42  ASN   B H    
455  H HA   . ASN   A 30  ? 1.19341  0.936328 1.54726  0.0567919   -0.53809    -0.0964223  42  ASN   B HA   
456  H HB2  . ASN   A 30  ? 1.18109  1.06129  1.76997  0.0819623   -0.584602   -0.118265   42  ASN   B HB2  
457  H HB3  . ASN   A 30  ? 1.18739  1.05727  1.7167   0.0425688   -0.597304   -0.129662   42  ASN   B HB3  
458  H HD21 . ASN   A 30  ? 1.03296  1.086    1.80822  -0.0220939  -0.495266   -0.170863   42  ASN   B HD21 
459  H HD22 . ASN   A 30  ? 1.1085   1.0704   1.7476   -0.0198435  -0.540174   -0.160989   42  ASN   B HD22 
460  N N    . GLY   A 31  ? 1.1526   0.904227 1.61866  0.108718    -0.508572   -0.0833937  43  GLY   B N    
461  C CA   . GLY   A 31  ? 1.14043  0.858521 1.62081  0.131183    -0.478681   -0.0742128  43  GLY   B CA   
462  C C    . GLY   A 31  ? 1.19363  0.820617 1.55009  0.121245    -0.45087    -0.0480098  43  GLY   B C    
463  O O    . GLY   A 31  ? 1.19862  0.812645 1.48281  0.0920565   -0.428892   -0.048298   43  GLY   B O    
464  H H    . GLY   A 31  ? 1.19862  0.945863 1.65323  0.121056    -0.55403    -0.0763348  43  GLY   B H    
465  H HA2  . GLY   A 31  ? 1.19063  0.904859 1.70125  0.160503    -0.511505   -0.0658535  43  GLY   B HA2  
466  H HA3  . GLY   A 31  ? 1.09115  0.850189 1.63356  0.124241    -0.444339   -0.0934624  43  GLY   B HA3  
467  N N    . GLU   A 32  ? 1.27851  0.842531 1.6148   0.146347    -0.452586   -0.0238656  44  GLU   B N    
468  C CA   . GLU   A 32  ? 1.33031  0.811243 1.56391  0.135438    -0.423926   0.00617028  44  GLU   B CA   
469  C C    . GLU   A 32  ? 1.26172  0.753033 1.51677  0.107861    -0.359982   -0.0135416  44  GLU   B C    
470  O O    . GLU   A 32  ? 1.261    0.711762 1.44101  0.0854474   -0.327247   0.0021969   44  GLU   B O    
471  C CB   . GLU   A 32  ? 1.41579  0.82351  1.6307   0.169864    -0.451092   0.0417769   44  GLU   B CB   
472  H H    . GLU   A 32  ? 1.29055  0.864179 1.68297  0.170904    -0.471732   -0.0253365  44  GLU   B H    
473  H HA   . GLU   A 32  ? 1.34765  0.814007 1.5082   0.124247    -0.430909   0.0169287   44  GLU   B HA   
476  N N    . GLU   A 33  ? 1.1791   0.732262 1.53696  0.110532    -0.342404   -0.049123   45  GLU   B N    
477  C CA   . GLU   A 33  ? 1.11388  0.665902 1.5005   0.0986      -0.292687   -0.0685602  45  GLU   B CA   
478  C C    . GLU   A 33  ? 1.03445  0.640256 1.41582  0.0642596   -0.252317   -0.0921123  45  GLU   B C    
479  O O    . GLU   A 33  ? 0.930447 0.601514 1.34721  0.0567726   -0.257599   -0.108944   45  GLU   B O    
480  C CB   . GLU   A 33  ? 1.09165  0.670904 1.58186  0.130553    -0.297416   -0.0933691  45  GLU   B CB   
481  H H    . GLU   A 33  ? 1.16213  0.762058 1.57344  0.120429    -0.362397   -0.0623941  45  GLU   B H    
482  H HA   . GLU   A 33  ? 1.15304  0.646541 1.49205  0.0944247   -0.283728   -0.0487521  45  GLU   B HA   
485  N N    . THR   A 34  ? 1.02603  0.602229 1.36443  0.0423573   -0.213196   -0.0907163  46  THR   B N    
486  C CA   . THR   A 34  ? 0.940935 0.56325  1.27434  0.0147187   -0.174492   -0.111992   46  THR   B CA   
487  C C    . THR   A 34  ? 0.922096 0.568497 1.31691  0.0185288   -0.144528   -0.143659   46  THR   B C    
488  O O    . THR   A 34  ? 0.939642 0.547546 1.36088  0.0367495   -0.150361   -0.145824   46  THR   B O    
489  C CB   . THR   A 34  ? 0.950484 0.532992 1.19521  -0.00937659 -0.15399    -0.0905388  46  THR   B CB   
490  O OG1  . THR   A 34  ? 0.969282 0.495264 1.20785  -0.00736553 -0.145065   -0.0773596  46  THR   B OG1  
491  C CG2  . THR   A 34  ? 0.972686 0.532172 1.14357  -0.00984507 -0.18001    -0.0644657  46  THR   B CG2  
492  H H    . THR   A 34  ? 1.06063  0.587    1.3741   0.0446705   -0.21167    -0.0749083  46  THR   B H    
493  H HA   . THR   A 34  ? 0.919842 0.583574 1.26875  0.011402    -0.181981   -0.119975   46  THR   B HA   
494  H HB   . THR   A 34  ? 0.897157 0.510188 1.1426   -0.0248482  -0.128812   -0.105457   46  THR   B HB   
496  H HG21 . THR   A 34  ? 0.984709 0.523859 1.10155  -0.0227073  -0.162203   -0.0522461  46  THR   B HG21 
497  H HG22 . THR   A 34  ? 1.02846  0.557316 1.19211  0.00653453  -0.20632    -0.0478817  46  THR   B HG22 
498  H HG23 . THR   A 34  ? 0.95204  0.547342 1.13604  -0.0127053  -0.188761   -0.0768877  46  THR   B HG23 
499  N N    . PRO   A 35  ? 0.881593 0.586729 1.29554  0.00351287  -0.112543   -0.169621   47  PRO   B N    
500  C CA   . PRO   A 35  ? 0.855072 0.580453 1.31123  0.009365    -0.0842764  -0.202058   47  PRO   B CA   
501  C C    . PRO   A 35  ? 0.887781 0.550377 1.31252  0.0009383   -0.0731575  -0.200453   47  PRO   B C    
502  O O    . PRO   A 35  ? 0.854155 0.483503 1.21885  -0.0213712  -0.0683785  -0.176349   47  PRO   B O    
503  C CB   . PRO   A 35  ? 0.783953 0.573325 1.23602  -0.0100087  -0.0531952  -0.218053   47  PRO   B CB   
504  C CG   . PRO   A 35  ? 0.801777 0.61292  1.23983  -0.0208071  -0.0705939  -0.198781   47  PRO   B CG   
505  C CD   . PRO   A 35  ? 0.853922 0.601575 1.2439   -0.0177391  -0.103896   -0.168506   47  PRO   B CD   
506  H HA   . PRO   A 35  ? 0.865135 0.606706 1.37316  0.0310603   -0.0930733  -0.214579   47  PRO   B HA   
507  H HB2  . PRO   A 35  ? 0.785416 0.560599 1.19966  -0.0251926  -0.0367695  -0.217803   47  PRO   B HB2  
508  H HB3  . PRO   A 35  ? 0.779323 0.607877 1.27493  0.00059992  -0.040239   -0.240177   47  PRO   B HB3  
509  H HG2  . PRO   A 35  ? 0.768751 0.593503 1.17708  -0.0383844  -0.0539631  -0.198      47  PRO   B HG2  
510  H HG3  . PRO   A 35  ? 0.785953 0.636864 1.27475  -0.0113309  -0.0776689  -0.206563   47  PRO   B HG3  
511  H HD2  . PRO   A 35  ? 0.850565 0.573507 1.18508  -0.0326009  -0.0955073  -0.156381   47  PRO   B HD2  
512  H HD3  . PRO   A 35  ? 0.856535 0.615628 1.25757  -0.013013   -0.127657   -0.161488   47  PRO   B HD3  
513  N N    . MET   A 36  ? 0.939347 0.586409 1.4089   0.0194458   -0.0697862  -0.226983   48  MET   B N    
514  C CA   . MET   A 36  ? 1.00162  0.596122 1.45664  0.00748091  -0.0586199  -0.236187   48  MET   B CA   
515  C C    . MET   A 36  ? 0.951227 0.597156 1.40922  -0.00345263 -0.027104   -0.274914   48  MET   B C    
516  O O    . MET   A 36  ? 0.91555  0.629659 1.39792  0.00805788  -0.013155   -0.296807   48  MET   B O    
517  C CB   . MET   A 36  ? 1.14682  0.682978 1.64543  0.0358267   -0.0774471  -0.247672   48  MET   B CB   
518  C CG   . MET   A 36  ? 1.24116  0.715791 1.735    0.0525148   -0.112416   -0.207064   48  MET   B CG   
519  S SD   . MET   A 36  ? 1.31162  0.704729 1.73088  0.0209675   -0.117935   -0.150684   48  MET   B SD   
520  C CE   . MET   A 36  ? 1.25779  0.696669 1.61833  0.010135    -0.123129   -0.118201   48  MET   B CE   
521  H H    . MET   A 36  ? 0.941771 0.612206 1.4554   0.0406604   -0.0755978  -0.241377   48  MET   B H    
522  H HA   . MET   A 36  ? 1.01591  0.579163 1.43011  -0.0115723  -0.0597537  -0.21003    48  MET   B HA   
523  H HB2  . MET   A 36  ? 1.12544  0.697615 1.66448  0.0573396   -0.0738334  -0.275309   48  MET   B HB2  
524  H HB3  . MET   A 36  ? 1.15749  0.658608 1.64952  0.0241888   -0.0702311  -0.257244   48  MET   B HB3  
525  H HG2  . MET   A 36  ? 1.21559  0.726873 1.7153   0.0623332   -0.123115   -0.198629   48  MET   B HG2  
526  H HG3  . MET   A 36  ? 1.27935  0.723324 1.80815  0.0752585   -0.123288   -0.219377   48  MET   B HG3  
527  H HE1  . MET   A 36  ? 1.30054  0.696607 1.61825  0.00283729  -0.129939   -0.0848182  48  MET   B HE1  
528  H HE2  . MET   A 36  ? 1.21044  0.690005 1.55866  -0.00756953 -0.10241    -0.130492   48  MET   B HE2  
529  H HE3  . MET   A 36  ? 1.25474  0.71927  1.63835  0.0302081   -0.14075    -0.122297   48  MET   B HE3  
530  N N    . ILE   A 37  ? 0.909122 0.525237 1.34341  -0.0261232  -0.0163018  -0.281986   49  ILE   B N    
531  C CA   . ILE   A 37  ? 0.871767 0.528288 1.30557  -0.0327043  0.00623438  -0.322068   49  ILE   B CA   
532  C C    . ILE   A 37  ? 0.838621 0.513118 1.31898  0.00192531  0.00883638  -0.367139   49  ILE   B C    
533  O O    . ILE   A 37  ? 0.823579 0.444707 1.33655  0.0225568   -0.00879831 -0.375579   49  ILE   B O    
534  C CB   . ILE   A 37  ? 0.958954 0.571744 1.37726  -0.0599402  0.00694872  -0.326645   49  ILE   B CB   
535  C CG1  . ILE   A 37  ? 0.997801 0.598404 1.37508  -0.0917206  0.00980738  -0.281129   49  ILE   B CG1  
536  C CG2  . ILE   A 37  ? 0.926192 0.580629 1.34216  -0.0626199  0.0225614   -0.37372    49  ILE   B CG2  
537  C CD1  . ILE   A 37  ? 1.02618  0.684006 1.37253  -0.112301   0.0300273   -0.286246   49  ILE   B CD1  
538  H H    . ILE   A 37  ? 0.948911 0.519252 1.36757  -0.0377565  -0.0242431  -0.260648   49  ILE   B H    
539  H HA   . ILE   A 37  ? 0.828833 0.531534 1.24298  -0.040614   0.0190774   -0.317726   49  ILE   B HA   
540  H HB   . ILE   A 37  ? 1.00163  0.562693 1.44109  -0.0533367  -0.00640029 -0.329678   49  ILE   B HB   
541  H HG12 . ILE   A 37  ? 0.992368 0.592169 1.35729  -0.0856168  0.00432706  -0.255316   49  ILE   B HG12 
542  H HG13 . ILE   A 37  ? 1.04177  0.594548 1.42487  -0.103632   0.00280872  -0.271607   49  ILE   B HG13 
543  H HG21 . ILE   A 37  ? 0.947031 0.582211 1.35548  -0.0834846  0.0208081   -0.374676   49  ILE   B HG21 
544  H HG22 . ILE   A 37  ? 0.889842 0.596163 1.28767  -0.0629192  0.0361133   -0.37267    49  ILE   B HG22 
545  H HG23 . ILE   A 37  ? 0.958971 0.607178 1.39842  -0.0421425  0.0199923   -0.403976   49  ILE   B HG23 
546  H HD11 . ILE   A 37  ? 1.01075  0.668383 1.36658  -0.12112    0.0321003   -0.309073   49  ILE   B HD11 
547  H HD12 . ILE   A 37  ? 0.993803 0.64569  1.31612  -0.126759   0.0326098   -0.256552   49  ILE   B HD12 
548  H HD13 . ILE   A 37  ? 0.965289 0.666222 1.30596  -0.10129    0.0378311   -0.295659   49  ILE   B HD13 
549  N N    . GLY   A 38  ? 0.773857 0.522309 1.25434  0.0103615   0.0325416   -0.393544   50  GLY   B N    
550  C CA   . GLY   A 38  ? 0.815582 0.594622 1.33335  0.0454797   0.0434364   -0.437226   50  GLY   B CA   
551  C C    . GLY   A 38  ? 0.780753 0.628467 1.33705  0.0666884   0.0531947   -0.428778   50  GLY   B C    
552  O O    . GLY   A 38  ? 0.825557 0.727881 1.40735  0.0925748   0.0753304   -0.461429   50  GLY   B O    
553  H H    . GLY   A 38  ? 0.748637 0.529376 1.20288  -0.00522441 0.0437791   -0.382659   50  GLY   B H    
554  H HA2  . GLY   A 38  ? 0.807798 0.610635 1.30543  0.0424466   0.0588589   -0.461983   50  GLY   B HA2  
555  H HA3  . GLY   A 38  ? 0.857057 0.588329 1.39654  0.059935    0.0292928   -0.45022    50  GLY   B HA3  
556  N N    . ASP   A 39  ? 0.717965 0.56192  1.2828   0.0580377   0.035166    -0.387262   51  ASP   B N    
557  C CA   . ASP   A 39  ? 0.727751 0.634703 1.34225  0.0738993   0.03605     -0.377573   51  ASP   B CA   
558  C C    . ASP   A 39  ? 0.663143 0.654366 1.27138  0.0629889   0.0714674   -0.383447   51  ASP   B C    
559  O O    . ASP   A 39  ? 0.630953 0.623754 1.18284  0.0364763   0.0856907   -0.376752   51  ASP   B O    
560  C CB   . ASP   A 39  ? 0.733258 0.614726 1.34437  0.0617779   0.00403126  -0.333648   51  ASP   B CB   
561  C CG   . ASP   A 39  ? 0.789747 0.595396 1.41342  0.080158    -0.0316554  -0.320883   51  ASP   B CG   
562  O OD1  . ASP   A 39  ? 0.811089 0.584063 1.46003  0.104857    -0.0323981  -0.347865   51  ASP   B OD1  
563  O OD2  . ASP   A 39  ? 0.805665 0.580453 1.40864  0.0712582   -0.0593193  -0.284066   51  ASP   B OD2  
564  H H    . ASP   A 39  ? 0.739215 0.541673 1.27898  0.0414205   0.0211559   -0.364614   51  ASP   B H    
565  H HA   . ASP   A 39  ? 0.747373 0.658596 1.40473  0.102192    0.0333903   -0.396604   51  ASP   B HA   
566  H HB2  . ASP   A 39  ? 0.711624 0.578638 1.27601  0.0365761   0.00572713  -0.31635    51  ASP   B HB2  
567  H HB3  . ASP   A 39  ? 0.710045 0.640258 1.35498  0.0667586   0.00397124  -0.328441   51  ASP   B HB3  
568  N N    . LYS   A 40  ? 0.665941 0.729038 1.3362   0.084909    0.0864474   -0.393576   52  LYS   B N    
569  C CA   . LYS   A 40  ? 0.633075 0.777752 1.3093   0.0713172   0.118854    -0.386157   52  LYS   B CA   
570  C C    . LYS   A 40  ? 0.617151 0.769847 1.30728  0.045621    0.0967008   -0.345592   52  LYS   B C    
571  O O    . LYS   A 40  ? 0.63649  0.797484 1.3859   0.058694    0.070366    -0.336789   52  LYS   B O    
572  C CB   . LYS   A 40  ? 0.641912 0.86447  1.38343  0.105665    0.149251    -0.414436   52  LYS   B CB   
573  C CG   . LYS   A 40  ? 0.613179 0.928513 1.36933  0.0956457   0.192491    -0.407045   52  LYS   B CG   
574  H H    . LYS   A 40  ? 0.688543 0.750249 1.40181  0.109391    0.0768555   -0.403961   52  LYS   B H    
575  H HA   . LYS   A 40  ? 0.626225 0.766188 1.25144  0.0568119   0.134476    -0.389146   52  LYS   B HA   
576  H HB2  . LYS   A 40  ? 0.672868 0.876818 1.39767  0.12432     0.157495    -0.443605   52  LYS   B HB2  
577  H HB3  . LYS   A 40  ? 0.649599 0.879463 1.44636  0.121494    0.131862    -0.41133    52  LYS   B HB3  
580  N N    . VAL   A 41  ? 0.580014 0.729313 1.21504  0.0119892   0.105018    -0.323869   53  VAL   B N    
581  C CA   . VAL   A 41  ? 0.600879 0.735702 1.22693  -0.0142098  0.0800395   -0.290189   53  VAL   B CA   
582  C C    . VAL   A 41  ? 0.550214 0.749028 1.19639  -0.0353049  0.104373    -0.276483   53  VAL   B C    
583  O O    . VAL   A 41  ? 0.564986 0.788393 1.17842  -0.042597   0.140322    -0.280191   53  VAL   B O    
584  C CB   . VAL   A 41  ? 0.615526 0.677941 1.15496  -0.0333096  0.0681708   -0.276798   53  VAL   B CB   
585  C CG1  . VAL   A 41  ? 0.61642  0.655606 1.12694  -0.05737    0.0452636   -0.246677   53  VAL   B CG1  
586  C CG2  . VAL   A 41  ? 0.689528 0.687457 1.21545  -0.0180891  0.0466325   -0.284203   53  VAL   B CG2  
587  H H    . VAL   A 41  ? 0.587647 0.742203 1.1868   0.00702594  0.126227    -0.332113   53  VAL   B H    
588  H HA   . VAL   A 41  ? 0.600151 0.728832 1.26266  -0.00478786 0.0548152   -0.285376   53  VAL   B HA   
589  H HB   . VAL   A 41  ? 0.613708 0.685921 1.12159  -0.0395612  0.0914063   -0.283637   53  VAL   B HB   
590  H HG11 . VAL   A 41  ? 0.623032 0.661712 1.16669  -0.0516248  0.0214514   -0.240677   53  VAL   B HG11 
591  H HG12 . VAL   A 41  ? 0.597694 0.666027 1.10708  -0.0708427  0.060417    -0.241152   53  VAL   B HG12 
592  H HG13 . VAL   A 41  ? 0.618398 0.613441 1.07796  -0.0640918  0.0386362   -0.239332   53  VAL   B HG13 
593  H HG21 . VAL   A 41  ? 0.676502 0.635054 1.15444  -0.0320536  0.0396778   -0.271211   53  VAL   B HG21 
594  H HG22 . VAL   A 41  ? 0.685336 0.687958 1.21716  -0.00591814 0.0611906   -0.306402   53  VAL   B HG22 
595  H HG23 . VAL   A 41  ? 0.690894 0.681576 1.25058  -0.00619854 0.0249367   -0.279235   53  VAL   B HG23 
596  N N    . TYR   A 42  ? 0.540965 0.764045 1.24087  -0.0461675  0.0820892   -0.259124   54  TYR   B N    
597  C CA   . TYR   A 42  ? 0.53406  0.812912 1.26726  -0.0719113  0.100368    -0.242502   54  TYR   B CA   
598  C C    . TYR   A 42  ? 0.50989  0.738105 1.20194  -0.102648   0.0677947   -0.218428   54  TYR   B C    
599  O O    . TYR   A 42  ? 0.547617 0.744638 1.24942  -0.0999329  0.0232956   -0.214102   54  TYR   B O    
600  C CB   . TYR   A 42  ? 0.543682 0.905618 1.39287  -0.0607516  0.101713    -0.246575   54  TYR   B CB   
601  C CG   . TYR   A 42  ? 0.573146 0.989412 1.47073  -0.0224479  0.133228    -0.274322   54  TYR   B CG   
602  C CD1  . TYR   A 42  ? 0.600346 0.978073 1.49719  0.0135042   0.112896    -0.296881   54  TYR   B CD1  
603  C CD2  . TYR   A 42  ? 0.588752 1.09223  1.53262  -0.0202343  0.183756    -0.277575   54  TYR   B CD2  
604  C CE1  . TYR   A 42  ? 0.645666 1.06389  1.58338  0.0526034   0.139306    -0.327393   54  TYR   B CE1  
605  C CE2  . TYR   A 42  ? 0.628649 1.18172  1.61012  0.0201978   0.214263    -0.307212   54  TYR   B CE2  
606  C CZ   . TYR   A 42  ? 0.651842 1.15941  1.62924  0.0579313   0.190598    -0.33512    54  TYR   B CZ   
607  O OH   . TYR   A 42  ? 0.727925 1.27487  1.73838  0.101505    0.218393    -0.369336   54  TYR   B OH   
608  H H    . TYR   A 42  ? 0.553899 0.756606 1.27146  -0.0382344  0.0525783   -0.256835   54  TYR   B H    
609  H HA   . TYR   A 42  ? 0.525907 0.821223 1.23234  -0.0757883  0.133528    -0.244426   54  TYR   B HA   
610  H HB2  . TYR   A 42  ? 0.552072 0.898258 1.42621  -0.0578576  0.0648394   -0.243005   54  TYR   B HB2  
611  H HB3  . TYR   A 42  ? 0.540147 0.939321 1.41431  -0.0823283  0.116013    -0.233045   54  TYR   B HB3  
612  H HD1  . TYR   A 42  ? 0.610162 0.929263 1.47472  0.0120149   0.081348    -0.29128    54  TYR   B HD1  
613  H HD2  . TYR   A 42  ? 0.582482 1.10985  1.52891  -0.0457481  0.199141    -0.259107   54  TYR   B HD2  
614  H HE1  . TYR   A 42  ? 0.660935 1.04362  1.59628  0.0763892   0.123612    -0.34267    54  TYR   B HE1  
615  H HE2  . TYR   A 42  ? 0.629198 1.24342  1.63564  0.0227451   0.25202     -0.308312   54  TYR   B HE2  
617  N N    . VAL   A 43  ? 0.481101 0.696111 1.12079  -0.127877   0.0879969   -0.203873   55  VAL   B N    
618  C CA   . VAL   A 43  ? 0.492768 0.654794 1.08981  -0.153359   0.0588725   -0.185681   55  VAL   B CA   
619  C C    . VAL   A 43  ? 0.501856 0.690923 1.11884  -0.184338   0.0786401   -0.167392   55  VAL   B C    
620  O O    . VAL   A 43  ? 0.50723  0.744368 1.13855  -0.185466   0.122882    -0.164164   55  VAL   B O    
621  C CB   . VAL   A 43  ? 0.491382 0.580217 0.983548 -0.151511   0.0559984   -0.183465   55  VAL   B CB   
622  C CG1  . VAL   A 43  ? 0.490744 0.547524 0.959605 -0.126369   0.0427951   -0.196671   55  VAL   B CG1  
623  C CG2  . VAL   A 43  ? 0.489702 0.587855 0.936542 -0.157497   0.0979979   -0.179267   55  VAL   B CG2  
624  H H    . VAL   A 43  ? 0.483465 0.720645 1.11109  -0.126978   0.11975     -0.206061   55  VAL   B H    
625  H HA   . VAL   A 43  ? 0.502195 0.656426 1.12593  -0.152197   0.0262843   -0.185676   55  VAL   B HA   
626  H HB   . VAL   A 43  ? 0.506993 0.561008 0.975232 -0.163508   0.0331882   -0.174365   55  VAL   B HB   
627  H HG11 . VAL   A 43  ? 0.483954 0.568261 0.972968 -0.113696   0.0629921   -0.209117   55  VAL   B HG11 
628  H HG12 . VAL   A 43  ? 0.503281 0.552145 0.99717  -0.120905   0.0150819   -0.196095   55  VAL   B HG12 
629  H HG13 . VAL   A 43  ? 0.495344 0.511391 0.904559 -0.128199   0.0415576   -0.192761   55  VAL   B HG13 
630  H HG21 . VAL   A 43  ? 0.487678 0.548953 0.878009 -0.152679   0.096446    -0.180519   55  VAL   B HG21 
631  H HG22 . VAL   A 43  ? 0.495584 0.595614 0.943873 -0.175228   0.102042    -0.165931   55  VAL   B HG22 
632  H HG23 . VAL   A 43  ? 0.480644 0.619444 0.953026 -0.147373   0.121509    -0.188454   55  VAL   B HG23 
633  N N    . HIS   A 44  ? 0.513645 0.661253 1.11822  -0.208365   0.0455426   -0.155324   56  HIS   B N    
634  C CA   . HIS   A 44  ? 0.578896 0.709668 1.1634   -0.238609   0.0591915   -0.136164   56  HIS   B CA   
635  C C    . HIS   A 44  ? 0.602968 0.647288 1.07905  -0.236207   0.0458721   -0.13405    56  HIS   B C    
636  O O    . HIS   A 44  ? 0.632329 0.63276  1.06863  -0.221918   0.0135911   -0.144021   56  HIS   B O    
637  C CB   . HIS   A 44  ? 0.611981 0.759877 1.27396  -0.270303   0.0307242   -0.127343   56  HIS   B CB   
638  C CG   . HIS   A 44  ? 0.626166 0.866313 1.39371  -0.285339   0.0633596   -0.117131   56  HIS   B CG   
639  N ND1  . HIS   A 44  ? 0.623254 0.895292 1.38453  -0.293682   0.11922     -0.099503   56  HIS   B ND1  
640  C CD2  . HIS   A 44  ? 0.610823 0.922317 1.49341  -0.29298    0.0491243   -0.119835   56  HIS   B CD2  
641  C CE1  . HIS   A 44  ? 0.629742 0.990843 1.49723  -0.306069   0.142709    -0.091045   56  HIS   B CE1  
642  N NE2  . HIS   A 44  ? 0.604258 0.993881 1.55204  -0.305747   0.100922    -0.104182   56  HIS   B NE2  
643  H H    . HIS   A 44  ? 0.534895 0.660015 1.14111  -0.204714   0.0117876   -0.159665   56  HIS   B H    
644  H HA   . HIS   A 44  ? 0.564967 0.728805 1.15456  -0.238882   0.0964601   -0.130223   56  HIS   B HA   
645  H HB2  . HIS   A 44  ? 0.618502 0.758264 1.29681  -0.263571   -0.00534342 -0.137411   56  HIS   B HB2  
646  H HB3  . HIS   A 44  ? 0.638647 0.741648 1.2639   -0.28799    0.0234732   -0.118339   56  HIS   B HB3  
648  H HD2  . HIS   A 44  ? 0.615165 0.926749 1.52775  -0.288234   0.0115468   -0.129901   56  HIS   B HD2  
649  H HE1  . HIS   A 44  ? 0.629058 1.02927  1.51176  -0.312734   0.18305     -0.0769364  56  HIS   B HE1  
651  N N    . TYR   A 45  ? 0.590553 0.613083 1.01892  -0.247249   0.0726291   -0.119183   57  TYR   B N    
652  C CA   . TYR   A 45  ? 0.595822 0.544558 0.926944 -0.239532   0.063672    -0.118084   57  TYR   B CA   
653  C C    . TYR   A 45  ? 0.638565 0.552999 0.9427   -0.260086   0.0751427   -0.0981318  57  TYR   B C    
654  O O    . TYR   A 45  ? 0.616075 0.568806 0.964631 -0.278337   0.102905    -0.0807912  57  TYR   B O    
655  C CB   . TYR   A 45  ? 0.541518 0.493369 0.817874 -0.212613   0.0870014   -0.126275   57  TYR   B CB   
656  C CG   . TYR   A 45  ? 0.539298 0.526892 0.804688 -0.210715   0.131115    -0.116736   57  TYR   B CG   
657  C CD1  . TYR   A 45  ? 0.532118 0.590096 0.850929 -0.206138   0.159795    -0.121405   57  TYR   B CD1  
658  C CD2  . TYR   A 45  ? 0.54107  0.492705 0.740584 -0.210484   0.143576    -0.102625   57  TYR   B CD2  
659  C CE1  . TYR   A 45  ? 0.507642 0.598109 0.804387 -0.201721   0.199895    -0.112517   57  TYR   B CE1  
660  C CE2  . TYR   A 45  ? 0.558905 0.541834 0.74168  -0.207045   0.180488    -0.0904595  57  TYR   B CE2  
661  C CZ   . TYR   A 45  ? 0.534108 0.586245 0.761216 -0.203178   0.208732    -0.0952937  57  TYR   B CZ   
662  O OH   . TYR   A 45  ? 0.537907 0.618631 0.734505 -0.196893   0.244552    -0.0829624  57  TYR   B OH   
663  H H    . TYR   A 45  ? 0.595547 0.650628 1.05233  -0.257995   0.0973679   -0.108513   57  TYR   B H    
664  H HA   . TYR   A 45  ? 0.60784  0.523022 0.925546 -0.237841   0.0317281   -0.125255   57  TYR   B HA   
665  H HB2  . TYR   A 45  ? 0.559164 0.466497 0.780451 -0.206138   0.0759062   -0.127005   57  TYR   B HB2  
666  H HB3  . TYR   A 45  ? 0.530043 0.503751 0.831281 -0.201322   0.0822843   -0.1379     57  TYR   B HB3  
667  H HD1  . TYR   A 45  ? 0.509253 0.592968 0.875906 -0.202809   0.151578    -0.131647   57  TYR   B HD1  
668  H HD2  . TYR   A 45  ? 0.564883 0.469755 0.728682 -0.210799   0.126194    -0.100819   57  TYR   B HD2  
669  H HE1  . TYR   A 45  ? 0.510124 0.648497 0.83775  -0.196052   0.220634    -0.117539   57  TYR   B HE1  
670  H HE2  . TYR   A 45  ? 0.572965 0.530149 0.710375 -0.204294   0.186259    -0.0796109  57  TYR   B HE2  
672  N N    . LYS   A 46  ? 0.656355 0.495687 0.887158 -0.255446   0.053503    -0.0998173  58  LYS   B N    
673  C CA   . LYS   A 46  ? 0.684826 0.473499 0.868914 -0.264094   0.0631083   -0.0833134  58  LYS   B CA   
674  C C    . LYS   A 46  ? 0.699077 0.454547 0.795154 -0.233383   0.0709069   -0.0886361  58  LYS   B C    
675  O O    . LYS   A 46  ? 0.68966  0.422903 0.752031 -0.216551   0.0498577   -0.104797   58  LYS   B O    
676  C CB   . LYS   A 46  ? 0.725405 0.454595 0.918753 -0.288208   0.0245048   -0.0845793  58  LYS   B CB   
677  C CG   . LYS   A 46  ? 0.730063 0.50349  1.02748  -0.323129   0.0142474   -0.0789354  58  LYS   B CG   
678  C CD   . LYS   A 46  ? 0.785017 0.496118 1.09227  -0.348035   -0.0348956  -0.0875624  58  LYS   B CD   
679  C CE   . LYS   A 46  ? 0.785286 0.54547  1.20208  -0.380172   -0.0595373  -0.0897005  58  LYS   B CE   
680  N NZ   . LYS   A 46  ? 0.855191 0.547962 1.27274  -0.403502   -0.115125   -0.104076   58  LYS   B NZ   
681  H H    . LYS   A 46  ? 0.65612  0.473777 0.863901 -0.24442    0.0322279   -0.111489   58  LYS   B H    
682  H HA   . LYS   A 46  ? 0.68593  0.504998 0.892853 -0.272886   0.0902204   -0.068294   58  LYS   B HA   
683  H HB2  . LYS   A 46  ? 0.736642 0.436583 0.900372 -0.276997   -0.00213274 -0.100216   58  LYS   B HB2  
684  H HB3  . LYS   A 46  ? 0.76372  0.450694 0.922545 -0.291682   0.0303794   -0.0741665  58  LYS   B HB3  
685  H HG2  . LYS   A 46  ? 0.729869 0.528793 1.05364  -0.336113   0.0431384   -0.0602616  58  LYS   B HG2  
686  H HG3  . LYS   A 46  ? 0.694057 0.514264 1.02909  -0.31613    0.0108187   -0.0884211  58  LYS   B HG3  
687  H HD2  . LYS   A 46  ? 0.796308 0.469979 1.05293  -0.330278   -0.0597744  -0.104593   58  LYS   B HD2  
688  H HD3  . LYS   A 46  ? 0.825164 0.492779 1.1096   -0.359133   -0.0286123  -0.0758975  58  LYS   B HD3  
689  H HE2  . LYS   A 46  ? 0.780677 0.579755 1.25013  -0.39938    -0.0323493  -0.0709903  58  LYS   B HE2  
690  H HE3  . LYS   A 46  ? 0.750391 0.553006 1.19086  -0.36635    -0.0664058  -0.100451   58  LYS   B HE3  
691  H HZ1  . LYS   A 46  ? 0.892756 0.546058 1.29946  -0.419546   -0.109273   -0.0934987  58  LYS   B HZ1  
692  H HZ2  . LYS   A 46  ? 0.867919 0.520644 1.22598  -0.383576   -0.137741   -0.120709   58  LYS   B HZ2  
693  H HZ3  . LYS   A 46  ? 0.853462 0.583394 1.34159  -0.421295   -0.133689   -0.107391   58  LYS   B HZ3  
694  N N    . GLY   A 47  ? 0.696958 0.458014 0.759571 -0.224771   0.102534    -0.0735053  59  GLY   B N    
695  C CA   . GLY   A 47  ? 0.685741 0.432503 0.679442 -0.19518    0.110536    -0.0787174  59  GLY   B CA   
696  C C    . GLY   A 47  ? 0.709296 0.404451 0.650108 -0.189354   0.117384    -0.0610344  59  GLY   B C    
697  O O    . GLY   A 47  ? 0.748493 0.434855 0.707029 -0.207911   0.128395    -0.0397325  59  GLY   B O    
698  H H    . GLY   A 47  ? 0.708022 0.484368 0.79202  -0.237204   0.119018    -0.058647   59  GLY   B H    
699  H HA2  . GLY   A 47  ? 0.677159 0.404193 0.65278  -0.186324   0.0926723   -0.0915962  59  GLY   B HA2  
700  H HA3  . GLY   A 47  ? 0.649415 0.440352 0.65008  -0.186765   0.128922    -0.0806929  59  GLY   B HA3  
701  N N    . LYS   A 48  ? 0.695381 0.359565 0.57476  -0.162351   0.113259    -0.0675192  60  LYS   B N    
702  C CA   . LYS   A 48  ? 0.756523 0.377292 0.585053 -0.147353   0.120859    -0.0516226  60  LYS   B CA   
703  C C    . LYS   A 48  ? 0.73493  0.366948 0.51554  -0.112022   0.126595    -0.0603916  60  LYS   B C    
704  O O    . LYS   A 48  ? 0.723402 0.377889 0.504556 -0.103227   0.121069    -0.0782825  60  LYS   B O    
705  C CB   . LYS   A 48  ? 0.867134 0.40056  0.675629 -0.155956   0.0959953   -0.0511849  60  LYS   B CB   
706  C CG   . LYS   A 48  ? 0.909299 0.402362 0.688372 -0.144401   0.0676041   -0.0772435  60  LYS   B CG   
707  C CD   . LYS   A 48  ? 1.03145  0.427136 0.76828  -0.14159    0.0436448   -0.0820483  60  LYS   B CD   
708  C CE   . LYS   A 48  ? 1.07609  0.43651  0.759818 -0.116871   0.0229055   -0.109036   60  LYS   B CE   
709  H H    . LYS   A 48  ? 0.683901 0.355204 0.554531 -0.151953   0.106178    -0.0810054  60  LYS   B H    
710  H HA   . LYS   A 48  ? 0.763552 0.404624 0.602565 -0.153605   0.1383      -0.0349871  60  LYS   B HA   
711  H HB2  . LYS   A 48  ? 0.900326 0.40161  0.675491 -0.14353    0.101815    -0.0396101  60  LYS   B HB2  
712  H HB3  . LYS   A 48  ? 0.874045 0.405045 0.721228 -0.181972   0.0921998   -0.0439967  60  LYS   B HB3  
713  H HG2  . LYS   A 48  ? 0.888464 0.400819 0.70129  -0.159898   0.0562666   -0.0858243  60  LYS   B HG2  
714  H HG3  . LYS   A 48  ? 0.88872  0.400234 0.64114  -0.121628   0.0752978   -0.0837096  60  LYS   B HG3  
715  H HD2  . LYS   A 48  ? 1.0548   0.42845  0.766097 -0.128519   0.055051    -0.0697513  60  LYS   B HD2  
716  H HD3  . LYS   A 48  ? 1.04982  0.42629  0.819033 -0.16834    0.0300611   -0.0796778  60  LYS   B HD3  
719  N N    . LEU   A 49  ? 0.765091 0.381872 0.507689 -0.0922106  0.137636    -0.0445928  61  LEU   B N    
720  C CA   . LEU   A 49  ? 0.778011 0.405629 0.481174 -0.0567678  0.141131    -0.0506716  61  LEU   B CA   
721  C C    . LEU   A 49  ? 0.819162 0.37486  0.483659 -0.0414048  0.123683    -0.0607945  61  LEU   B C    
722  O O    . LEU   A 49  ? 0.826996 0.314931 0.483876 -0.0543831  0.110292    -0.0559093  61  LEU   B O    
723  C CB   . LEU   A 49  ? 0.82124  0.45867  0.498331 -0.0373683  0.155041    -0.0288005  61  LEU   B CB   
724  C CG   . LEU   A 49  ? 0.836501 0.536551 0.536278 -0.0501094  0.17302     -0.0174457  61  LEU   B CG   
725  C CD1  . LEU   A 49  ? 0.883245 0.582776 0.543534 -0.0283122  0.183025    0.00838303  61  LEU   B CD1  
726  C CD2  . LEU   A 49  ? 0.79286  0.565702 0.519212 -0.0488227  0.175738    -0.041405   61  LEU   B CD2  
727  H H    . LEU   A 49  ? 0.799113 0.399428 0.542612 -0.100755   0.14316     -0.0277954  61  LEU   B H    
728  H HA   . LEU   A 49  ? 0.732454 0.405292 0.450839 -0.0549078  0.14428     -0.0627094  61  LEU   B HA   
729  H HB2  . LEU   A 49  ? 0.878223 0.461752 0.537024 -0.0373204  0.151075    -0.0155913  61  LEU   B HB2  
730  H HB3  . LEU   A 49  ? 0.821417 0.474867 0.480255 -0.013068   0.155513    -0.0345161  61  LEU   B HB3  
731  H HG   . LEU   A 49  ? 0.835703 0.526834 0.559359 -0.074057   0.175557    -0.0113003  61  LEU   B HG   
732  H HD11 . LEU   A 49  ? 0.932807 0.576127 0.5751   -0.0279529  0.179787    0.0242871   61  LEU   B HD11 
733  H HD12 . LEU   A 49  ? 0.875761 0.609782 0.544267 -0.0374737  0.195247    0.0164187   61  LEU   B HD12 
734  H HD13 . LEU   A 49  ? 0.873609 0.594267 0.517901 -0.00453848 0.179824    0.00137091  61  LEU   B HD13 
735  H HD21 . LEU   A 49  ? 0.761118 0.533531 0.514407 -0.0651629  0.170893    -0.0526187  61  LEU   B HD21 
736  H HD22 . LEU   A 49  ? 0.778198 0.55915  0.490745 -0.0301463  0.171511    -0.0491721  61  LEU   B HD22 
737  H HD23 . LEU   A 49  ? 0.776059 0.587599 0.506934 -0.0499434  0.186053    -0.0378686  61  LEU   B HD23 
738  N N    . SER   A 50  ? 0.83232  0.403598 0.473554 -0.0144107  0.124947    -0.0749076  62  SER   B N    
739  C CA   . SER   A 50  ? 0.966152 0.47438  0.557422 0.0123539   0.114876    -0.0852772  62  SER   B CA   
740  C C    . SER   A 50  ? 1.0073   0.45635  0.563488 0.0342072   0.113676    -0.0717805  62  SER   B C    
741  O O    . SER   A 50  ? 1.16207  0.531962 0.681494 0.0447929   0.0986088   -0.0816161  62  SER   B O    
742  C CB   . SER   A 50  ? 0.961218 0.511939 0.537959 0.040785    0.125891    -0.0965047  62  SER   B CB   
743  O OG   . SER   A 50  ? 1.05462  0.647501 0.66124  0.0192505   0.125985    -0.104972   62  SER   B OG   
744  H H    . SER   A 50  ? 0.798371 0.421418 0.455576 -0.0121663  0.133282    -0.0786828  62  SER   B H    
745  H HA   . SER   A 50  ? 0.968745 0.4399   0.557186 -0.00168633 0.100305    -0.0944266  62  SER   B HA   
746  H HB2  . SER   A 50  ? 0.96998  0.560352 0.553834 0.0546089   0.137247    -0.0891725  62  SER   B HB2  
747  H HB3  . SER   A 50  ? 1.03254  0.54221  0.573305 0.0604024   0.121374    -0.104719   62  SER   B HB3  
749  N N    . ASN   A 51  ? 1.05132  0.530915 0.61442  0.0414483   0.12656     -0.0499187  63  ASN   B N    
750  C CA   . ASN   A 51  ? 1.13945  0.557963 0.666176 0.0658451   0.124573    -0.0318091  63  ASN   B CA   
751  C C    . ASN   A 51  ? 1.18949  0.526172 0.71815  0.0342596   0.11329     -0.0171676  63  ASN   B C    
752  O O    . ASN   A 51  ? 1.25566  0.522991 0.754355 0.0491698   0.109423    0.00063023  63  ASN   B O    
753  C CB   . ASN   A 51  ? 1.14184  0.617865 0.667482 0.087809    0.138288    -0.0109553  63  ASN   B CB   
754  C CG   . ASN   A 51  ? 1.15731  0.667283 0.70744  0.0563859   0.148261    0.011347    63  ASN   B CG   
755  O OD1  . ASN   A 51  ? 1.13183  0.629549 0.710495 0.0164383   0.148012    0.0123903   63  ASN   B OD1  
756  N ND2  . ASN   A 51  ? 1.16379  0.719196 0.701973 0.0763286   0.156881    0.0293993   63  ASN   B ND2  
757  H H    . ASN   A 51  ? 0.992653 0.529596 0.580385 0.0328219   0.13559     -0.0463317  63  ASN   B H    
758  H HA   . ASN   A 51  ? 1.17158  0.559583 0.670099 0.0923291   0.119787    -0.0436648  63  ASN   B HA   
759  H HB2  . ASN   A 51  ? 1.20206  0.636396 0.698688 0.113095    0.135219    -0.00096918 63  ASN   B HB2  
760  H HB3  . ASN   A 51  ? 1.10341  0.637756 0.63914  0.100866    0.143422    -0.0222364  63  ASN   B HB3  
761  H HD21 . ASN   A 51  ? 1.14957  0.732381 0.697099 0.0611547   0.164703    0.0403112   63  ASN   B HD21 
762  H HD22 . ASN   A 51  ? 1.17842  0.738413 0.698393 0.106185    0.154259    0.030048    63  ASN   B HD22 
763  N N    . GLY   A 52  ? 1.17551  0.522602 0.745416 -0.00968406 0.107877    -0.0222949  64  GLY   B N    
764  C CA   . GLY   A 52  ? 1.23517  0.511775 0.821624 -0.045659   0.0944837   -0.0115522  64  GLY   B CA   
765  C C    . GLY   A 52  ? 1.26756  0.545024 0.870072 -0.0645158  0.112104    0.0289182   64  GLY   B C    
766  O O    . GLY   A 52  ? 1.38417  0.592485 0.997389 -0.0916674  0.104078    0.0458447   64  GLY   B O    
767  H H    . GLY   A 52  ? 1.11291  0.514299 0.70585  -0.0181056  0.112141    -0.0320506  64  GLY   B H    
768  H HA2  . GLY   A 52  ? 1.20486  0.499975 0.823009 -0.070783   0.0871757   -0.0231101  64  GLY   B HA2  
769  H HA3  . GLY   A 52  ? 1.29728  0.503532 0.85336  -0.0334923  0.0796311   -0.0197879  64  GLY   B HA3  
770  N N    . LYS   A 53  ? 1.22151  0.575095 0.823902 -0.051441   0.135727    0.0455905   65  LYS   B N    
771  C CA   . LYS   A 53  ? 1.27063  0.622067 0.867047 -0.0588082  0.154735    0.0873042   65  LYS   B CA   
772  C C    . LYS   A 53  ? 1.20056  0.629918 0.847058 -0.0948767  0.176337    0.0979114   65  LYS   B C    
773  O O    . LYS   A 53  ? 1.24741  0.676673 0.893729 -0.109375   0.196388    0.134976    65  LYS   B O    
774  C CB   . LYS   A 53  ? 1.2737   0.638154 0.817864 -0.00999909 0.161319    0.101121    65  LYS   B CB   
775  H H    . LYS   A 53  ? 1.17179  0.578928 0.77576  -0.0378234  0.139595    0.0309915   65  LYS   B H    
776  H HA   . LYS   A 53  ? 1.32705  0.607925 0.919213 -0.0712935  0.147555    0.101264    65  LYS   B HA   
779  N N    . LYS   A 54  ? 1.12765  0.622119 0.815136 -0.107297   0.174541    0.0677631   66  LYS   B N    
780  C CA   . LYS   A 54  ? 1.05858  0.625833 0.797453 -0.136481   0.194618    0.07258     66  LYS   B CA   
781  C C    . LYS   A 54  ? 0.999444 0.577569 0.795774 -0.163534   0.177877    0.0449766   66  LYS   B C    
782  O O    . LYS   A 54  ? 0.961533 0.532462 0.748763 -0.149351   0.157436    0.0151355   66  LYS   B O    
783  C CB   . LYS   A 54  ? 0.975328 0.630557 0.702406 -0.11465    0.213029    0.0652346   66  LYS   B CB   
784  H H    . LYS   A 54  ? 1.0962   0.589411 0.778855 -0.0955576  0.161501    0.0442569   66  LYS   B H    
785  H HA   . LYS   A 54  ? 1.09582  0.6464   0.841361 -0.153567   0.206737    0.0998106   66  LYS   B HA   
788  N N    . PHE   A 55  ? 0.953306 0.550646 0.808619 -0.201184   0.187275    0.058173    67  PHE   B N    
789  C CA   . PHE   A 55  ? 0.925846 0.547425 0.847134 -0.227226   0.171251    0.0360017   67  PHE   B CA   
790  C C    . PHE   A 55  ? 0.905337 0.61444  0.886627 -0.244974   0.200141    0.0442181   67  PHE   B C    
791  O O    . PHE   A 55  ? 0.946093 0.67397  0.932113 -0.256061   0.230787    0.0765302   67  PHE   B O    
792  C CB   . PHE   A 55  ? 0.977711 0.533736 0.933451 -0.261368   0.146061    0.0404667   67  PHE   B CB   
793  C CG   . PHE   A 55  ? 1.09148  0.547294 0.981581 -0.243364   0.122375    0.0367891   67  PHE   B CG   
794  C CD1  . PHE   A 55  ? 1.18871  0.59265  1.03265  -0.232553   0.13643     0.0674454   67  PHE   B CD1  
795  C CD2  . PHE   A 55  ? 1.13641  0.549531 1.00535  -0.232287   0.0869237   0.00268351  67  PHE   B CD2  
796  C CE1  . PHE   A 55  ? 1.30908  0.61866  1.09374  -0.209703   0.114525    0.0609572   67  PHE   B CE1  
797  C CE2  . PHE   A 55  ? 1.23407  0.555333 1.039    -0.210396   0.0675021   -0.00492091 67  PHE   B CE2  
798  C CZ   . PHE   A 55  ? 1.30607  0.575418 1.07187  -0.198048   0.0811184   0.0226202   67  PHE   B CZ   
799  H H    . PHE   A 55  ? 0.999568 0.5974   0.85548  -0.210388   0.204976    0.084091    67  PHE   B H    
800  H HA   . PHE   A 55  ? 0.891397 0.520587 0.80181  -0.211628   0.157278    0.0114374   67  PHE   B HA   
801  H HB2  . PHE   A 55  ? 1.01535  0.577974 1.00082  -0.284084   0.162102    0.0651764   67  PHE   B HB2  
802  H HB3  . PHE   A 55  ? 0.961784 0.534165 0.952914 -0.271311   0.12859     0.0204948   67  PHE   B HB3  
803  H HD1  . PHE   A 55  ? 1.19736  0.629488 1.048    -0.238366   0.161141    0.0929296   67  PHE   B HD1  
804  H HD2  . PHE   A 55  ? 1.09384  0.538605 0.989971 -0.238182   0.0759864   -0.0152311  67  PHE   B HD2  
805  H HE1  . PHE   A 55  ? 1.34312  0.614512 1.09774  -0.20023    0.122703    0.0828834   67  PHE   B HE1  
806  H HE2  . PHE   A 55  ? 1.23677  0.530656 1.02184  -0.200929   0.045375    -0.028897   67  PHE   B HE2  
807  H HZ   . PHE   A 55  ? 1.35445  0.560172 1.07763  -0.179463   0.0679095   0.0158159   67  PHE   B HZ   
808  N N    . ASP   A 56  ? 0.836083 0.594919 0.863307 -0.246905   0.190485    0.0163436   68  ASP   B N    
809  C CA   . ASP   A 56  ? 0.824508 0.66959  0.907501 -0.254419   0.217579    0.0164327   68  ASP   B CA   
810  C C    . ASP   A 56  ? 0.764352 0.632698 0.92093  -0.270411   0.19338     -0.00614707 68  ASP   B C    
811  O O    . ASP   A 56  ? 0.68327  0.525622 0.824348 -0.258151   0.162302    -0.0311583  68  ASP   B O    
812  C CB   . ASP   A 56  ? 0.833494 0.727006 0.876746 -0.221125   0.235093    0.00071742  68  ASP   B CB   
813  C CG   . ASP   A 56  ? 0.815252 0.793094 0.908363 -0.219283   0.258161    -0.0125401  68  ASP   B CG   
814  O OD1  . ASP   A 56  ? 0.852449 0.869831 0.981129 -0.235264   0.287965    0.00899357  68  ASP   B OD1  
815  O OD2  . ASP   A 56  ? 0.745858 0.746876 0.841977 -0.201229   0.247468    -0.0435023  68  ASP   B OD2  
816  H H    . ASP   A 56  ? 0.830438 0.568016 0.852418 -0.2414     0.167001    -0.00290954 68  ASP   B H    
817  H HA   . ASP   A 56  ? 0.852639 0.707523 0.951797 -0.270169   0.238403    0.0411305   68  ASP   B HA   
818  H HB2  . ASP   A 56  ? 0.853075 0.738315 0.85316  -0.21146    0.249763    0.0171601   68  ASP   B HB2  
819  H HB3  . ASP   A 56  ? 0.803385 0.678825 0.826085 -0.207308   0.215508    -0.0185022  68  ASP   B HB3  
820  N N    . SER   A 57  ? 0.758662 0.68154  0.99512  -0.295205   0.209211    0.00449532  69  SER   B N    
821  C CA   . SER   A 57  ? 0.766581 0.72265  1.08228  -0.307304   0.184945    -0.0155984  69  SER   B CA   
822  C C    . SER   A 57  ? 0.759073 0.81281  1.14058  -0.30388    0.218986    -0.0174294  69  SER   B C    
823  O O    . SER   A 57  ? 0.815338 0.909663 1.2085   -0.312241   0.261317    0.00754544  69  SER   B O    
824  C CB   . SER   A 57  ? 0.847465 0.769129 1.21626  -0.345321   0.157744    -0.00486348 69  SER   B CB   
825  O OG   . SER   A 57  ? 0.900326 0.870336 1.35491  -0.354968   0.134051    -0.0231787  69  SER   B OG   
826  H H    . SER   A 57  ? 0.78997  0.732616 1.03289  -0.303758   0.236232    0.0260822   69  SER   B H    
827  H HA   . SER   A 57  ? 0.746393 0.684752 1.03796  -0.290333   0.162487    -0.0369906  69  SER   B HA   
828  H HB2  . SER   A 57  ? 0.878958 0.735188 1.20282  -0.343407   0.132504    -0.0101116  69  SER   B HB2  
829  H HB3  . SER   A 57  ? 0.884168 0.815125 1.27402  -0.364785   0.1804      0.0199189   69  SER   B HB3  
831  N N    . SER   A 58  ? 0.720847 0.810164 1.1451   -0.290101   0.200583    -0.0457836  70  SER   B N    
832  C CA   . SER   A 58  ? 0.692306 0.873048 1.19127  -0.283884   0.228197    -0.0522503  70  SER   B CA   
833  C C    . SER   A 58  ? 0.731568 0.957687 1.31941  -0.320539   0.245573    -0.025152   70  SER   B C    
834  O O    . SER   A 58  ? 0.774516 1.07235  1.39607  -0.320264   0.293501    -0.0113341  70  SER   B O    
835  C CB   . SER   A 58  ? 0.621923 0.819904 1.1586   -0.264329   0.197862    -0.0837589  70  SER   B CB   
836  O OG   . SER   A 58  ? 0.606429 0.759909 1.16423  -0.28101    0.147454    -0.0871821  70  SER   B OG   
837  H H    . SER   A 58  ? 0.708366 0.763662 1.11372  -0.282541   0.171106    -0.0607468  70  SER   B H    
838  H HA   . SER   A 58  ? 0.68769  0.889736 1.15184  -0.26733    0.258055    -0.0520426  70  SER   B HA   
839  H HB2  . SER   A 58  ? 0.613564 0.872472 1.21047  -0.260763   0.214056    -0.0876987  70  SER   B HB2  
840  H HB3  . SER   A 58  ? 0.608974 0.787784 1.0945   -0.242184   0.196232    -0.0980588  70  SER   B HB3  
842  N N    . HIS   A 59  ? 0.742719 0.925263 1.3645   -0.352791   0.207452    -0.0173367  71  HIS   B N    
843  C CA   . HIS   A 59  ? 0.800251 1.02101  1.52107  -0.395916   0.21456     0.00755611  71  HIS   B CA   
844  C C    . HIS   A 59  ? 0.841269 1.07366  1.54783  -0.415023   0.269249    0.0492292   71  HIS   B C    
845  O O    . HIS   A 59  ? 0.793428 1.0955   1.58953  -0.442631   0.300328    0.0734297   71  HIS   B O    
846  C CB   . HIS   A 59  ? 0.823495 0.973346 1.56144  -0.426802   0.156217    0.0038611   71  HIS   B CB   
847  C CG   . HIS   A 59  ? 0.798639 0.943256 1.55573  -0.411118   0.101236    -0.0313225  71  HIS   B CG   
848  N ND1  . HIS   A 59  ? 0.774563 1.00017  1.64296  -0.415068   0.0866642   -0.042481   71  HIS   B ND1  
849  C CD2  . HIS   A 59  ? 0.809986 0.881159 1.48703  -0.388552   0.0591373   -0.0550969  71  HIS   B CD2  
850  C CE1  . HIS   A 59  ? 0.775666 0.970621 1.62575  -0.395226   0.0338432   -0.0705994  71  HIS   B CE1  
851  N NE2  . HIS   A 59  ? 0.79098  0.891918 1.52316  -0.38027    0.0183598   -0.0776594  71  HIS   B NE2  
852  H H    . HIS   A 59  ? 0.752724 0.879796 1.33535  -0.34832    0.174998    -0.0288772  71  HIS   B H    
853  H HA   . HIS   A 59  ? 0.769598 1.0595   1.56218  -0.392372   0.220743    -0.0008201  71  HIS   B HA   
854  H HB2  . HIS   A 59  ? 0.851745 0.930431 1.5162   -0.425786   0.149479    0.00894846  71  HIS   B HB2  
855  H HB3  . HIS   A 59  ? 0.850921 1.02544  1.6588   -0.459458   0.160981    0.0214566   71  HIS   B HB3  
857  H HD2  . HIS   A 59  ? 0.820184 0.831968 1.41861  -0.379116   0.0578098   -0.0550462  71  HIS   B HD2  
858  H HE1  . HIS   A 59  ? 0.76063  0.995703 1.67165  -0.391238   0.0116183   -0.0821243  71  HIS   B HE1  
860  N N    . ASP   A 60  ? 0.921207 1.08815  1.51572  -0.398949   0.28154     0.0600016   72  ASP   B N    
861  C CA   . ASP   A 60  ? 0.986332 1.15689  1.54294  -0.40686    0.332634    0.101168    72  ASP   B CA   
862  C C    . ASP   A 60  ? 0.954939 1.23473  1.54622  -0.392725   0.390497    0.108085    72  ASP   B C    
863  O O    . ASP   A 60  ? 0.983092 1.28905  1.57387  -0.408199   0.438125    0.148508    72  ASP   B O    
864  C CB   . ASP   A 60  ? 1.01076  1.10785  1.43841  -0.377236   0.331638    0.1027      72  ASP   B CB   
865  H H    . ASP   A 60  ? 0.896509 1.01492  1.43544  -0.381401   0.256285    0.042247    72  ASP   B H    
866  H HA   . ASP   A 60  ? 1.02102  1.17018  1.61282  -0.440609   0.330963    0.125675    72  ASP   B HA   
869  N N    . ARG   A 61  ? 0.912922 1.24962  1.52352  -0.35962    0.387545    0.0689011   73  ARG   B N    
870  C CA   . ARG   A 61  ? 0.877682 1.31504  1.51594  -0.337069   0.439018    0.0642312   73  ARG   B CA   
871  C C    . ARG   A 61  ? 0.807603 1.33303  1.58493  -0.350993   0.440485    0.0559984   73  ARG   B C    
872  O O    . ARG   A 61  ? 0.797151 1.41088  1.61179  -0.325987   0.477515    0.0426269   73  ARG   B O    
873  C CB   . ARG   A 61  ? 0.825517 1.25439  1.38297  -0.286802   0.432193    0.0228811   73  ARG   B CB   
874  H H    . ARG   A 61  ? 0.872528 1.18045  1.47469  -0.348697   0.352009    0.0433852   73  ARG   B H    
875  H HA   . ARG   A 61  ? 0.911523 1.36268  1.52691  -0.34453    0.477094    0.0940786   73  ARG   B HA   
878  N N    . ASN   A 62  ? 0.766494 1.26889  1.62065  -0.388099   0.397616    0.0610684   74  ASN   B N    
879  C CA   . ASN   A 62  ? 0.714502 1.2988   1.70941  -0.403518   0.386586    0.0528057   74  ASN   B CA   
880  C C    . ASN   A 62  ? 0.671317 1.31899  1.68936  -0.354466   0.388445    0.0113002   74  ASN   B C    
881  O O    . ASN   A 62  ? 0.699265 1.45183  1.8131   -0.348406   0.421679    0.0109581   74  ASN   B O    
882  C CB   . ASN   A 62  ? 0.736395 1.3983   1.8279   -0.445103   0.43567     0.0969409   74  ASN   B CB   
883  H H    . ASN   A 62  ? 0.785439 1.21799  1.60264  -0.403643   0.37224     0.0690005   74  ASN   B H    
884  H HA   . ASN   A 62  ? 0.712226 1.25296  1.72661  -0.420332   0.339421    0.0452147   74  ASN   B HA   
887  N N    . GLU   A 63  ? 0.68059  1.26509  1.61556  -0.318773   0.353946    -0.0231921  75  GLU   B N    
888  C CA   . GLU   A 63  ? 0.636219 1.26205  1.5959   -0.274663   0.346489    -0.0627486  75  GLU   B CA   
889  C C    . GLU   A 63  ? 0.58995  1.12434  1.45799  -0.249491   0.300151    -0.0912688  75  GLU   B C    
890  O O    . GLU   A 63  ? 0.593075 1.05199  1.35972  -0.253163   0.295339    -0.0838227  75  GLU   B O    
891  C CB   . GLU   A 63  ? 0.658927 1.35741  1.60467  -0.240708   0.409522    -0.0709191  75  GLU   B CB   
892  C CG   . GLU   A 63  ? 0.68806  1.32968  1.49557  -0.220631   0.428868    -0.0743688  75  GLU   B CG   
893  C CD   . GLU   A 63  ? 0.69903  1.40055  1.47895  -0.17803    0.47706     -0.0973725  75  GLU   B CD   
894  O OE1  . GLU   A 63  ? 0.714871 1.36602  1.39052  -0.153159   0.472944    -0.117516   75  GLU   B OE1  
895  O OE2  . GLU   A 63  ? 0.677286 1.47509  1.5395   -0.16884    0.516337    -0.0975884  75  GLU   B OE2  
896  H H    . GLU   A 63  ? 0.674    1.18748  1.53804  -0.322168   0.335222    -0.0210378  75  GLU   B H    
897  H HA   . GLU   A 63  ? 0.626889 1.29401  1.67556  -0.281777   0.329046    -0.0667092  75  GLU   B HA   
898  H HB2  . GLU   A 63  ? 0.641308 1.37023  1.62135  -0.213339   0.402785    -0.0975084  75  GLU   B HB2  
899  H HB3  . GLU   A 63  ? 0.679398 1.43652  1.67573  -0.257191   0.444858    -0.0484432  75  GLU   B HB3  
900  H HG2  . GLU   A 63  ? 0.708692 1.33126  1.48576  -0.243575   0.443667    -0.0451758  75  GLU   B HG2  
901  H HG3  . GLU   A 63  ? 0.664759 1.24459  1.42527  -0.212058   0.39302     -0.0908019  75  GLU   B HG3  
902  N N    . PRO   A 64  ? 0.55251  1.09189  1.45468  -0.22194    0.266118    -0.122241   76  PRO   B N    
903  C CA   . PRO   A 64  ? 0.539531 0.99607  1.35901  -0.199993   0.227885    -0.144242   76  PRO   B CA   
904  C C    . PRO   A 64  ? 0.53682  0.966147 1.25555  -0.176839   0.257986    -0.154976   76  PRO   B C    
905  O O    . PRO   A 64  ? 0.539015 1.02334  1.25641  -0.163782   0.306104    -0.156716   76  PRO   B O    
906  C CB   . PRO   A 64  ? 0.51368  0.997796 1.39708  -0.169312   0.201866    -0.171342   76  PRO   B CB   
907  C CG   . PRO   A 64  ? 0.539853 1.12177  1.5534   -0.178948   0.213459    -0.163575   76  PRO   B CG   
908  C CD   . PRO   A 64  ? 0.560258 1.18719  1.58465  -0.209049   0.264879    -0.134478   76  PRO   B CD   
909  H HA   . PRO   A 64  ? 0.539975 0.943914 1.33382  -0.218372   0.197989    -0.135249   76  PRO   B HA   
910  H HB2  . PRO   A 64  ? 0.519649 1.00832  1.37829  -0.142229   0.218523    -0.189294   76  PRO   B HB2  
911  H HB3  . PRO   A 64  ? 0.518428 0.953806 1.38556  -0.17036    0.161217    -0.174781   76  PRO   B HB3  
912  H HG2  . PRO   A 64  ? 0.531368 1.15685  1.58305  -0.150712   0.225551    -0.180967   76  PRO   B HG2  
913  H HG3  . PRO   A 64  ? 0.533897 1.10714  1.58759  -0.193465   0.175565    -0.159215   76  PRO   B HG3  
914  H HD2  . PRO   A 64  ? 0.560845 1.24355  1.60188  -0.191416   0.305375    -0.139561   76  PRO   B HD2  
915  H HD3  . PRO   A 64  ? 0.561112 1.21482  1.65217  -0.236375   0.255143    -0.118528   76  PRO   B HD3  
916  N N    . PHE   A 65  ? 0.529044 0.877481 1.16535  -0.171196   0.228228    -0.162895   77  PHE   B N    
917  C CA   . PHE   A 65  ? 0.567124 0.887408 1.11908  -0.148233   0.242301    -0.17962    77  PHE   B CA   
918  C C    . PHE   A 65  ? 0.584382 0.898335 1.15243  -0.117389   0.22345     -0.212433   77  PHE   B C    
919  O O    . PHE   A 65  ? 0.604858 0.880696 1.18929  -0.116936   0.182345    -0.215196   77  PHE   B O    
920  C CB   . PHE   A 65  ? 0.589644 0.83211  1.05537  -0.161602   0.221946    -0.16656    77  PHE   B CB   
921  C CG   . PHE   A 65  ? 0.596911 0.817232 0.983213 -0.141788   0.233246    -0.182012   77  PHE   B CG   
922  C CD1  . PHE   A 65  ? 0.641863 0.885768 0.981586 -0.13822    0.269326    -0.174891   77  PHE   B CD1  
923  C CD2  . PHE   A 65  ? 0.597598 0.776322 0.958769 -0.127437   0.20671     -0.202453   77  PHE   B CD2  
924  C CE1  . PHE   A 65  ? 0.638308 0.868293 0.911104 -0.119925   0.273366    -0.192634   77  PHE   B CE1  
925  C CE2  . PHE   A 65  ? 0.578384 0.743606 0.880679 -0.113574   0.214371    -0.218266   77  PHE   B CE2  
926  C CZ   . PHE   A 65  ? 0.62798  0.820331 0.887446 -0.109498   0.244924    -0.215643   77  PHE   B CZ   
927  H H    . PHE   A 65  ? 0.535438 0.846249 1.16991  -0.182792   0.196678    -0.157888   77  PHE   B H    
928  H HA   . PHE   A 65  ? 0.580237 0.936995 1.12254  -0.143337   0.277244    -0.177789   77  PHE   B HA   
929  H HB2  . PHE   A 65  ? 0.599341 0.840547 1.05875  -0.180168   0.231933    -0.145374   77  PHE   B HB2  
930  H HB3  . PHE   A 65  ? 0.57933  0.786994 1.04935  -0.164753   0.189818    -0.168561   77  PHE   B HB3  
931  H HD1  . PHE   A 65  ? 0.648204 0.918974 1.00304  -0.148731   0.290193    -0.157094   77  PHE   B HD1  
932  H HD2  . PHE   A 65  ? 0.582712 0.743496 0.96911  -0.127966   0.182703    -0.204681   77  PHE   B HD2  
933  H HE1  . PHE   A 65  ? 0.660304 0.90672  0.897527 -0.11571    0.294643    -0.187692   77  PHE   B HE1  
934  H HE2  . PHE   A 65  ? 0.585722 0.723121 0.876968 -0.107546   0.197285    -0.229783   77  PHE   B HE2  
935  H HZ   . PHE   A 65  ? 0.623568 0.808814 0.844411 -0.100204   0.245788    -0.228084   77  PHE   B HZ   
936  N N    . VAL   A 66  ? 0.598501 0.945663 1.15735  -0.0903737  0.253048    -0.237131   78  VAL   B N    
937  C CA   . VAL   A 66  ? 0.572011 0.911222 1.15204  -0.0592611  0.238941    -0.270615   78  VAL   B CA   
938  C C    . VAL   A 66  ? 0.570615 0.867265 1.06997  -0.0465933  0.241226    -0.292543   78  VAL   B C    
939  O O    . VAL   A 66  ? 0.601212 0.912691 1.04565  -0.0481403  0.268814    -0.291893   78  VAL   B O    
940  C CB   . VAL   A 66  ? 0.612153 1.0315   1.26757  -0.0345223  0.268963    -0.288178   78  VAL   B CB   
941  C CG1  . VAL   A 66  ? 0.640749 1.04302  1.3248   0.00140809  0.250104    -0.323572   78  VAL   B CG1  
942  C CG2  . VAL   A 66  ? 0.596243 1.07518  1.34239  -0.0532335  0.271753    -0.262779   78  VAL   B CG2  
943  H H    . VAL   A 66  ? 0.60258  0.974508 1.13816  -0.0905114  0.282116    -0.233347   78  VAL   B H    
944  H HA   . VAL   A 66  ? 0.570593 0.879652 1.16966  -0.062197   0.207418    -0.26718    78  VAL   B HA   
945  H HB   . VAL   A 66  ? 0.624708 1.07058  1.24973  -0.028489   0.301443    -0.293516   78  VAL   B HB   
946  H HG11 . VAL   A 66  ? 0.626088 0.993445 1.32666  -0.00322713 0.216415    -0.316573   78  VAL   B HG11 
947  H HG12 . VAL   A 66  ? 0.649119 1.02116  1.28177  0.0115758   0.252919    -0.341921   78  VAL   B HG12 
948  H HG13 . VAL   A 66  ? 0.647004 1.10258  1.38445  0.0197148   0.268429    -0.334734   78  VAL   B HG13 
949  H HG21 . VAL   A 66  ? 0.606836 1.1402   1.40845  -0.0342803  0.28943     -0.275191   78  VAL   B HG21 
950  H HG22 . VAL   A 66  ? 0.599394 1.09167  1.32914  -0.0746314  0.290551    -0.241594   78  VAL   B HG22 
951  H HG23 . VAL   A 66  ? 0.585711 1.03527  1.35177  -0.0624338  0.236406    -0.255367   78  VAL   B HG23 
952  N N    . PHE   A 67  ? 0.541956 0.783838 1.03426  -0.0361797  0.209453    -0.309052   79  PHE   B N    
953  C CA   . PHE   A 67  ? 0.543771 0.74689  0.974822 -0.0284123  0.207341    -0.331658   79  PHE   B CA   
954  C C    . PHE   A 67  ? 0.585721 0.740801 1.04128  -0.0123275  0.178231    -0.352368   79  PHE   B C    
955  O O    . PHE   A 67  ? 0.567757 0.710061 1.07191  -0.00935546 0.155032    -0.341099   79  PHE   B O    
956  C CB   . PHE   A 67  ? 0.543182 0.70764  0.906386 -0.0527361  0.198292    -0.309502   79  PHE   B CB   
957  C CG   . PHE   A 67  ? 0.519374 0.625535 0.879061 -0.06729    0.162874    -0.289354   79  PHE   B CG   
958  C CD1  . PHE   A 67  ? 0.490994 0.594282 0.872813 -0.0817407  0.148965    -0.262256   79  PHE   B CD1  
959  C CD2  . PHE   A 67  ? 0.52246  0.577247 0.853727 -0.0675609  0.144006    -0.297386   79  PHE   B CD2  
960  C CE1  . PHE   A 67  ? 0.495157 0.544691 0.859942 -0.0908251  0.117134    -0.246068   79  PHE   B CE1  
961  C CE2  . PHE   A 67  ? 0.501324 0.506189 0.82141  -0.0788374  0.117313    -0.275428   79  PHE   B CE2  
962  C CZ   . PHE   A 67  ? 0.500563 0.502141 0.831939 -0.0876332  0.103908    -0.251321   79  PHE   B CZ   
963  H H    . PHE   A 67  ? 0.541939 0.77043  1.06941  -0.0348865  0.187854    -0.305098   79  PHE   B H    
964  H HA   . PHE   A 67  ? 0.57151  0.806538 0.991023 -0.0157311  0.231307    -0.349164   79  PHE   B HA   
965  H HB2  . PHE   A 67  ? 0.54893  0.704422 0.876986 -0.0476296  0.2018      -0.32573    79  PHE   B HB2  
966  H HB3  . PHE   A 67  ? 0.53242  0.720413 0.885107 -0.0629154  0.213523    -0.292047   79  PHE   B HB3  
967  H HD1  . PHE   A 67  ? 0.492651 0.631291 0.900518 -0.0855543  0.161194    -0.255297   79  PHE   B HD1  
968  H HD2  . PHE   A 67  ? 0.531706 0.586274 0.851483 -0.0603761  0.149703    -0.317702   79  PHE   B HD2  
969  H HE1  . PHE   A 67  ? 0.491399 0.537506 0.867846 -0.0994149  0.104563    -0.231433   79  PHE   B HE1  
970  H HE2  . PHE   A 67  ? 0.516771 0.489936 0.82078  -0.0805121  0.1081      -0.2777     79  PHE   B HE2  
971  H HZ   . PHE   A 67  ? 0.505104 0.472068 0.820385 -0.0928284  0.0857822   -0.237898   79  PHE   B HZ   
972  N N    . SER   A 68  ? 0.572797 0.699753 0.995051 -0.00204962 0.177341    -0.382374   80  SER   B N    
973  C CA   . SER   A 68  ? 0.640807 0.712203 1.08482  0.0112865   0.151258    -0.401851   80  SER   B CA   
974  C C    . SER   A 68  ? 0.625264 0.633753 1.02875  -0.0140244  0.127153    -0.382279   80  SER   B C    
975  O O    . SER   A 68  ? 0.623018 0.630125 0.977824 -0.0284408  0.13377     -0.385332   80  SER   B O    
976  C CB   . SER   A 68  ? 0.678884 0.75248  1.12308  0.0382362   0.162063    -0.450782   80  SER   B CB   
977  O OG   . SER   A 68  ? 0.740594 0.858765 1.24064  0.0707188   0.177872    -0.469827   80  SER   B OG   
978  H H    . SER   A 68  ? 0.595834 0.736381 0.981393 -0.00398526 0.191692    -0.390453   80  SER   B H    
979  H HA   . SER   A 68  ? 0.628736 0.700647 1.11595  0.0196247   0.140882    -0.393694   80  SER   B HA   
980  H HB2  . SER   A 68  ? 0.693582 0.787645 1.0988   0.0343975   0.177273    -0.460471   80  SER   B HB2  
981  H HB3  . SER   A 68  ? 0.712034 0.73496  1.15554  0.0382409   0.142455    -0.461017   80  SER   B HB3  
983  N N    . LEU   A 69  ? 0.613992 0.577017 1.03784  -0.0178351  0.100196    -0.359527   81  LEU   B N    
984  C CA   . LEU   A 69  ? 0.63049  0.543394 1.01536  -0.0417571  0.0831671   -0.331635   81  LEU   B CA   
985  C C    . LEU   A 69  ? 0.651584 0.522612 1.02008  -0.048164   0.078217    -0.350523   81  LEU   B C    
986  O O    . LEU   A 69  ? 0.63816  0.479112 1.03664  -0.0324707  0.0692283   -0.375699   81  LEU   B O    
987  C CB   . LEU   A 69  ? 0.672141 0.545933 1.07562  -0.0395758  0.0557629   -0.30351    81  LEU   B CB   
988  C CG   . LEU   A 69  ? 0.705317 0.532674 1.06024  -0.0615772  0.0428641   -0.269865   81  LEU   B CG   
989  C CD1  . LEU   A 69  ? 0.648817 0.504894 0.964814 -0.0777228  0.0527361   -0.250674   81  LEU   B CD1  
990  C CD2  . LEU   A 69  ? 0.798507 0.580824 1.16336  -0.0535527  0.0139016   -0.245238   81  LEU   B CD2  
991  H H    . LEU   A 69  ? 0.631977 0.597504 1.09395  -0.00334645 0.0928933   -0.360955   81  LEU   B H    
992  H HA   . LEU   A 69  ? 0.605461 0.538237 0.961385 -0.0550847  0.0924946   -0.318196   81  LEU   B HA   
993  H HB2  . LEU   A 69  ? 0.656826 0.561035 1.07919  -0.0355803  0.0556994   -0.295977   81  LEU   B HB2  
994  H HB3  . LEU   A 69  ? 0.702045 0.551041 1.1324   -0.0251619  0.0454814   -0.314765   81  LEU   B HB3  
995  H HG   . LEU   A 69  ? 0.717618 0.523724 1.05779  -0.0696058  0.0463142   -0.27571    81  LEU   B HG   
996  H HD11 . LEU   A 69  ? 0.638259 0.5197   0.94164  -0.0822837  0.0700605   -0.262254   81  LEU   B HD11 
997  H HD12 . LEU   A 69  ? 0.661909 0.489071 0.946687 -0.0873298  0.0452215   -0.231044   81  LEU   B HD12 
998  H HD13 . LEU   A 69  ? 0.645745 0.522777 0.980609 -0.0730598  0.0487084   -0.246437   81  LEU   B HD13 
999  H HD21 . LEU   A 69  ? 0.806705 0.565485 1.19773  -0.0410752  0.00607384  -0.255386   81  LEU   B HD21 
1000 H HD22 . LEU   A 69  ? 0.766455 0.572358 1.1472   -0.0475381  0.00716631  -0.240022   81  LEU   B HD22 
1001 H HD23 . LEU   A 69  ? 0.785541 0.538561 1.11417  -0.0658954  0.00905001  -0.224079   81  LEU   B HD23 
1002 N N    . GLY   A 70  ? 0.673032 0.542991 0.998758 -0.0710793  0.0828993   -0.338891   82  GLY   B N    
1003 C CA   . GLY   A 70  ? 0.738036 0.573469 1.05685  -0.0850804  0.0754195   -0.351322   82  GLY   B CA   
1004 C C    . GLY   A 70  ? 0.82304  0.684858 1.13987  -0.0770005  0.0836464   -0.397596   82  GLY   B C    
1005 O O    . GLY   A 70  ? 0.91486  0.749362 1.23476  -0.0893965  0.0729419   -0.415895   82  GLY   B O    
1006 H H    . GLY   A 70  ? 0.644804 0.536949 0.949001 -0.0783031  0.0903162   -0.323088   82  GLY   B H    
1007 H HA2  . GLY   A 70  ? 0.726154 0.562039 1.02075  -0.101696   0.0769675   -0.331711   82  GLY   B HA2  
1008 H HA3  . GLY   A 70  ? 0.770606 0.563138 1.11002  -0.0834841  0.0620443   -0.34828    82  GLY   B HA3  
1009 N N    . LYS   A 71  ? 0.802401 0.716163 1.11493  -0.0566885  0.101867    -0.416743   83  LYS   B N    
1010 C CA   . LYS   A 71  ? 0.822496 0.760253 1.12409  -0.0413803  0.110059    -0.46432    83  LYS   B CA   
1011 C C    . LYS   A 71  ? 0.86168  0.850462 1.11198  -0.0496016  0.12454     -0.461173   83  LYS   B C    
1012 O O    . LYS   A 71  ? 0.927884 0.956656 1.15402  -0.0316679  0.139664    -0.489835   83  LYS   B O    
1013 C CB   . LYS   A 71  ? 0.783911 0.743907 1.11452  -0.00762405 0.123428    -0.489516   83  LYS   B CB   
1014 H H    . LYS   A 71  ? 0.776511 0.712007 1.0909   -0.0527767  0.109789    -0.399409   83  LYS   B H    
1015 H HA   . LYS   A 71  ? 0.854371 0.757124 1.16359  -0.0469631  0.0953768   -0.48267    83  LYS   B HA   
1018 N N    . GLY   A 72  ? 0.891751 0.878619 1.12252  -0.0726373  0.120835    -0.424566   84  GLY   B N    
1019 C CA   . GLY   A 72  ? 0.945908 0.97233  1.13042  -0.0798669  0.129428    -0.414506   84  GLY   B CA   
1020 C C    . GLY   A 72  ? 0.8327   0.909634 0.986876 -0.0639687  0.154784    -0.409431   84  GLY   B C    
1021 O O    . GLY   A 72  ? 0.935193 1.0462   1.04688  -0.0579692  0.161711    -0.420553   84  GLY   B O    
1022 H H    . GLY   A 72  ? 0.878362 0.836229 1.12434  -0.0822691  0.11213     -0.404023   84  GLY   B H    
1023 H HA2  . GLY   A 72  ? 0.879553 0.895782 1.05981  -0.0933479  0.126027    -0.386474   84  GLY   B HA2  
1024 H HA3  . GLY   A 72  ? 0.924082 0.953261 1.10029  -0.0823591  0.120829    -0.437613   84  GLY   B HA3  
1025 N N    . GLN   A 73  ? 0.696144 0.780018 0.873423 -0.0577018  0.167982    -0.391009   85  GLN   B N    
1026 C CA   . GLN   A 73  ? 0.669365 0.800002 0.826449 -0.049666   0.195106    -0.376691   85  GLN   B CA   
1027 C C    . GLN   A 73  ? 0.595127 0.721365 0.730382 -0.0668505  0.196906    -0.332188   85  GLN   B C    
1028 O O    . GLN   A 73  ? 0.564944 0.721004 0.673854 -0.0653071  0.217445    -0.314451   85  GLN   B O    
1029 C CB   . GLN   A 73  ? 0.663305 0.811825 0.870316 -0.0350962  0.20848     -0.383402   85  GLN   B CB   
1030 C CG   . GLN   A 73  ? 0.724421 0.884732 0.939657 -0.00933468 0.214246    -0.432065   85  GLN   B CG   
1031 C CD   . GLN   A 73  ? 0.718431 0.886401 0.997388 0.00922679  0.21965     -0.442898   85  GLN   B CD   
1032 O OE1  . GLN   A 73  ? 0.706818 0.890706 1.02604  0.00338118  0.224492    -0.413372   85  GLN   B OE1  
1033 N NE2  . GLN   A 73  ? 0.841763 0.999504 1.13166  0.0335721   0.216773    -0.488507   85  GLN   B NE2  
1034 H H    . GLN   A 73  ? 0.710964 0.770649 0.919397 -0.0593712  0.159388    -0.385722   85  GLN   B H    
1035 H HA   . GLN   A 73  ? 0.687872 0.841993 0.813471 -0.0406651  0.203496    -0.393577   85  GLN   B HA   
1036 H HB2  . GLN   A 73  ? 0.654762 0.777219 0.894196 -0.0410727  0.194384    -0.372704   85  GLN   B HB2  
1037 H HB3  . GLN   A 73  ? 0.664325 0.843358 0.86737  -0.0353566  0.227206    -0.366319   85  GLN   B HB3  
1038 H HG2  . GLN   A 73  ? 0.737472 0.931646 0.919985 6.659e-05   0.232506    -0.440887   85  GLN   B HG2  
1039 H HG3  . GLN   A 73  ? 0.730749 0.859993 0.940185 -0.0120902  0.195589    -0.450238   85  GLN   B HG3  
1040 H HE21 . GLN   A 73  ? 0.825792 0.994237 1.15155  0.050287    0.22301     -0.49882    85  GLN   B HE21 
1041 H HE22 . GLN   A 73  ? 0.837026 0.976887 1.10009  0.0339355   0.207616    -0.510123   85  GLN   B HE22 
1042 N N    . VAL   A 74  ? 0.520648 0.606218 0.662418 -0.0817538  0.176487    -0.314369   86  VAL   B N    
1043 C CA   . VAL   A 74  ? 0.498179 0.569185 0.619563 -0.0941821  0.175164    -0.277303   86  VAL   B CA   
1044 C C    . VAL   A 74  ? 0.47448  0.522541 0.571661 -0.102315   0.16078     -0.271513   86  VAL   B C    
1045 O O    . VAL   A 74  ? 0.496381 0.538624 0.605007 -0.103772   0.150635    -0.292198   86  VAL   B O    
1046 C CB   . VAL   A 74  ? 0.475374 0.522233 0.632743 -0.100885   0.165469    -0.259091   86  VAL   B CB   
1047 C CG1  . VAL   A 74  ? 0.4895   0.572522 0.683039 -0.0956248  0.181841    -0.259594   86  VAL   B CG1  
1048 C CG2  . VAL   A 74  ? 0.478376 0.489674 0.665743 -0.100632   0.144407    -0.26865    86  VAL   B CG2  
1049 H H    . VAL   A 74  ? 0.538061 0.601878 0.695426 -0.0835352  0.163398    -0.325824   86  VAL   B H    
1050 H HA   . VAL   A 74  ? 0.498538 0.590558 0.597907 -0.0920534  0.188855    -0.268358   86  VAL   B HA   
1051 H HB   . VAL   A 74  ? 0.473333 0.504037 0.610433 -0.108665   0.161558    -0.238662   86  VAL   B HB   
1052 H HG11 . VAL   A 74  ? 0.49654  0.59729  0.707655 -0.0842379  0.187936    -0.281443   86  VAL   B HG11 
1053 H HG12 . VAL   A 74  ? 0.490038 0.591373 0.663109 -0.0981826  0.196553    -0.248267   86  VAL   B HG12 
1054 H HG13 . VAL   A 74  ? 0.480001 0.55077  0.700337 -0.100569   0.17138     -0.249108   86  VAL   B HG13 
1055 H HG21 . VAL   A 74  ? 0.475723 0.473844 0.681819 -0.102539   0.135672    -0.256827   86  VAL   B HG21 
1056 H HG22 . VAL   A 74  ? 0.478274 0.469765 0.646313 -0.10671    0.137079    -0.263967   86  VAL   B HG22 
1057 H HG23 . VAL   A 74  ? 0.489882 0.510623 0.696961 -0.091799   0.1466      -0.290654   86  VAL   B HG23 
1058 N N    . ILE   A 75  ? 0.499701 0.535758 0.567467 -0.10742    0.160761    -0.244212   87  ILE   B N    
1059 C CA   . ILE   A 75  ? 0.502999 0.52448  0.553208 -0.112287   0.151534    -0.235586   87  ILE   B CA   
1060 C C    . ILE   A 75  ? 0.45344  0.439872 0.530416 -0.121366   0.138141    -0.233776   87  ILE   B C    
1061 O O    . ILE   A 75  ? 0.450057 0.413484 0.549803 -0.122102   0.131564    -0.230844   87  ILE   B O    
1062 C CB   . ILE   A 75  ? 0.494132 0.505012 0.505706 -0.109735   0.155655    -0.208446   87  ILE   B CB   
1063 C CG1  . ILE   A 75  ? 0.552659 0.528963 0.567319 -0.11479    0.151616    -0.190617   87  ILE   B CG1  
1064 C CG2  . ILE   A 75  ? 0.529245 0.571297 0.509744 -0.099418   0.167614    -0.206863   87  ILE   B CG2  
1065 C CD1  . ILE   A 75  ? 0.559243 0.50744  0.533659 -0.11185    0.150035    -0.168686   87  ILE   B CD1  
1066 H H    . ILE   A 75  ? 0.493943 0.531475 0.553861 -0.107438   0.167583    -0.230601   87  ILE   B H    
1067 H HA   . ILE   A 75  ? 0.494785 0.537714 0.540364 -0.109875   0.151557    -0.249384   87  ILE   B HA   
1068 H HB   . ILE   A 75  ? 0.508188 0.513142 0.511831 -0.110501   0.151525    -0.203676   87  ILE   B HB   
1069 H HG12 . ILE   A 75  ? 0.538382 0.526409 0.564141 -0.115206   0.157894    -0.191849   87  ILE   B HG12 
1070 H HG13 . ILE   A 75  ? 0.53405  0.49354  0.567608 -0.118948   0.142483    -0.193072   87  ILE   B HG13 
1071 H HG21 . ILE   A 75  ? 0.528078 0.558227 0.484078 -0.0960233  0.16877     -0.189817   87  ILE   B HG21 
1072 H HG22 . ILE   A 75  ? 0.527076 0.577432 0.513607 -0.0990758  0.175649    -0.208401   87  ILE   B HG22 
1073 H HG23 . ILE   A 75  ? 0.524567 0.589943 0.502858 -0.0956175  0.165694    -0.220851   87  ILE   B HG23 
1074 H HD11 . ILE   A 75  ? 0.560921 0.504084 0.524176 -0.109113   0.147461    -0.167196   87  ILE   B HD11 
1075 H HD12 . ILE   A 75  ? 0.567253 0.490591 0.544822 -0.116519   0.14304     -0.161447   87  ILE   B HD12 
1076 H HD13 . ILE   A 75  ? 0.567839 0.526983 0.524042 -0.106964   0.158106    -0.163499   87  ILE   B HD13 
1077 N N    . LYS   A 76  ? 0.502166 0.488925 0.578914 -0.128057   0.134092    -0.233952   88  LYS   B N    
1078 C CA   . LYS   A 76  ? 0.498707 0.453268 0.598943 -0.139209   0.125128    -0.228463   88  LYS   B CA   
1079 C C    . LYS   A 76  ? 0.467988 0.38354  0.55183  -0.137765   0.120926    -0.202319   88  LYS   B C    
1080 O O    . LYS   A 76  ? 0.504744 0.387779 0.607922 -0.140343   0.110434    -0.198745   88  LYS   B O    
1081 C CB   . LYS   A 76  ? 0.541688 0.513499 0.645967 -0.149633   0.126869    -0.225341   88  LYS   B CB   
1082 H H    . LYS   A 76  ? 0.485703 0.495031 0.548777 -0.125879   0.137434    -0.235597   88  LYS   B H    
1083 H HA   . LYS   A 76  ? 0.509499 0.457471 0.635607 -0.140224   0.119763    -0.2449     88  LYS   B HA   
1086 N N    . ALA   A 77  ? 0.486977 0.401652 0.532445 -0.131573   0.125903    -0.185568   89  ALA   B N    
1087 C CA   . ALA   A 77  ? 0.536856 0.4121   0.556998 -0.129132   0.11764     -0.165351   89  ALA   B CA   
1088 C C    . ALA   A 77  ? 0.56238  0.421869 0.606706 -0.128398   0.103566    -0.169345   89  ALA   B C    
1089 O O    . ALA   A 77  ? 0.54004  0.364769 0.574965 -0.127365   0.0882673   -0.156792   89  ALA   B O    
1090 C CB   . ALA   A 77  ? 0.546092 0.417887 0.521654 -0.120889   0.123048    -0.154044   89  ALA   B CB   
1091 H H    . ALA   A 77  ? 0.481456 0.417886 0.513575 -0.127588   0.132829    -0.187729   89  ALA   B H    
1092 H HA   . ALA   A 77  ? 0.54899  0.407933 0.565405 -0.132435   0.116164    -0.156018   89  ALA   B HA   
1093 H HB1  . ALA   A 77  ? 0.544665 0.429069 0.507396 -0.118132   0.131672    -0.15067    89  ALA   B HB1  
1094 H HB2  . ALA   A 77  ? 0.535619 0.420713 0.51425  -0.119269   0.125677    -0.159479   89  ALA   B HB2  
1095 H HB3  . ALA   A 77  ? 0.561857 0.404537 0.51799  -0.118953   0.114805    -0.144656   89  ALA   B HB3  
1096 N N    . TRP   A 78  ? 0.536398 0.426183 0.610346 -0.126837   0.108899    -0.185992   90  TRP   B N    
1097 C CA   . TRP   A 78  ? 0.515731 0.404661 0.627686 -0.124735   0.0983545   -0.191001   90  TRP   B CA   
1098 C C    . TRP   A 78  ? 0.514307 0.388087 0.662052 -0.121252   0.0874743   -0.200669   90  TRP   B C    
1099 O O    . TRP   A 78  ? 0.573512 0.42596  0.740286 -0.117061   0.0690846   -0.194016   90  TRP   B O    
1100 C CB   . TRP   A 78  ? 0.493061 0.424885 0.626075 -0.122821   0.113875    -0.202179   90  TRP   B CB   
1101 C CG   . TRP   A 78  ? 0.485056 0.415075 0.604054 -0.128988   0.114508    -0.185805   90  TRP   B CG   
1102 C CD1  . TRP   A 78  ? 0.526626 0.431459 0.597335 -0.131931   0.113425    -0.17004    90  TRP   B CD1  
1103 C CD2  . TRP   A 78  ? 0.471058 0.421846 0.631348 -0.134014   0.114461    -0.183617   90  TRP   B CD2  
1104 N NE1  . TRP   A 78  ? 0.469353 0.369482 0.545441 -0.140155   0.110881    -0.159601   90  TRP   B NE1  
1105 C CE2  . TRP   A 78  ? 0.480304 0.411495 0.614613 -0.144399   0.111561    -0.165949   90  TRP   B CE2  
1106 C CE3  . TRP   A 78  ? 0.469199 0.45513  0.690529 -0.130099   0.117205    -0.195215   90  TRP   B CE3  
1107 C CZ2  . TRP   A 78  ? 0.487635 0.43337  0.659645 -0.157072   0.110615    -0.157812   90  TRP   B CZ2  
1108 C CZ3  . TRP   A 78  ? 0.459035 0.470057 0.720323 -0.139825   0.119348    -0.186373   90  TRP   B CZ3  
1109 C CH2  . TRP   A 78  ? 0.463315 0.453743 0.70234  -0.15617    0.115133    -0.16694    90  TRP   B CH2  
1110 H H    . TRP   A 78  ? 0.522937 0.437031 0.593426 -0.125748   0.119569    -0.193645   90  TRP   B H    
1111 H HA   . TRP   A 78  ? 0.525637 0.394006 0.625416 -0.125993   0.0871601   -0.178606   90  TRP   B HA   
1112 H HB2  . TRP   A 78  ? 0.487926 0.43844  0.60899  -0.12101    0.126103    -0.210347   90  TRP   B HB2  
1113 H HB3  . TRP   A 78  ? 0.49242  0.43525  0.661732 -0.118717   0.111679    -0.212511   90  TRP   B HB3  
1114 H HD1  . TRP   A 78  ? 0.504568 0.398383 0.545614 -0.128635   0.115111    -0.167221   90  TRP   B HD1  
1115 H HE1  . TRP   A 78  ? 0.502229 0.382255 0.551731 -0.142249   0.10882     -0.150672   90  TRP   B HE1  
1116 H HE3  . TRP   A 78  ? 0.463057 0.456728 0.701223 -0.120871   0.118242    -0.209201   90  TRP   B HE3  
1117 H HZ2  . TRP   A 78  ? 0.500073 0.425782 0.655583 -0.165895   0.106709    -0.146738   90  TRP   B HZ2  
1118 H HZ3  . TRP   A 78  ? 0.456817 0.498733 0.764692 -0.135632   0.123192    -0.193919   90  TRP   B HZ3  
1119 H HH2  . TRP   A 78  ? 0.473808 0.48147  0.747    -0.166401   0.115816    -0.160439   90  TRP   B HH2  
1120 N N    . ASP   A 79  ? 0.493183 0.375358 0.651762 -0.122244   0.0953939   -0.217362   91  ASP   B N    
1121 C CA   . ASP   A 79  ? 0.541898 0.397431 0.734369 -0.11968    0.0840029   -0.227064   91  ASP   B CA   
1122 C C    . ASP   A 79  ? 0.604023 0.410522 0.777704 -0.124578   0.0695604   -0.198345   91  ASP   B C    
1123 O O    . ASP   A 79  ? 0.618368 0.393955 0.813385 -0.117045   0.0525283   -0.193218   91  ASP   B O    
1124 C CB   . ASP   A 79  ? 0.547247 0.414179 0.752829 -0.123566   0.0912552   -0.252845   91  ASP   B CB   
1125 C CG   . ASP   A 79  ? 0.559399 0.464156 0.785237 -0.110714   0.1008      -0.287627   91  ASP   B CG   
1126 O OD1  . ASP   A 79  ? 0.572518 0.493194 0.819103 -0.0977454  0.103393    -0.291803   91  ASP   B OD1  
1127 O OD2  . ASP   A 79  ? 0.561669 0.483945 0.782594 -0.112916   0.105715    -0.311506   91  ASP   B OD2  
1128 H H    . ASP   A 79  ? 0.495483 0.397812 0.640726 -0.12435    0.105982    -0.223304   91  ASP   B H    
1129 H HA   . ASP   A 79  ? 0.544913 0.40646  0.76487  -0.11032    0.0795937   -0.235894   91  ASP   B HA   
1130 H HB2  . ASP   A 79  ? 0.542056 0.420604 0.725375 -0.131694   0.097988    -0.247502   91  ASP   B HB2  
1131 H HB3  . ASP   A 79  ? 0.573812 0.410212 0.795716 -0.126429   0.0822254   -0.252847   91  ASP   B HB3  
1132 N N    . ILE   A 80  ? 0.597605 0.398823 0.728293 -0.133714   0.0773177   -0.178494   92  ILE   B N    
1133 C CA   . ILE   A 80  ? 0.637698 0.396735 0.737458 -0.136319   0.0697389   -0.148707   92  ILE   B CA   
1134 C C    . ILE   A 80  ? 0.597713 0.337335 0.67596  -0.125398   0.0507491   -0.136544   92  ILE   B C    
1135 O O    . ILE   A 80  ? 0.657996 0.360547 0.733833 -0.11952    0.0320125   -0.121822   92  ILE   B O    
1136 C CB   . ILE   A 80  ? 0.659078 0.428712 0.71951  -0.14435    0.0880097   -0.13326    92  ILE   B CB   
1137 C CG1  . ILE   A 80  ? 0.682872 0.47414  0.773489 -0.158787   0.101026    -0.142921   92  ILE   B CG1  
1138 C CG2  . ILE   A 80  ? 0.721277 0.451814 0.734291 -0.141845   0.0849358   -0.100927   92  ILE   B CG2  
1139 C CD1  . ILE   A 80  ? 0.684246 0.511244 0.751525 -0.162435   0.119919    -0.135572   92  ILE   B CD1  
1140 H H    . ILE   A 80  ? 0.58264  0.408556 0.701199 -0.136323   0.0885981   -0.183243   92  ILE   B H    
1141 H HA   . ILE   A 80  ? 0.651646 0.388046 0.770835 -0.138868   0.0643134   -0.146412   92  ILE   B HA   
1142 H HB   . ILE   A 80  ? 0.643577 0.434129 0.687819 -0.140071   0.093147    -0.138447   92  ILE   B HB   
1143 H HG12 . ILE   A 80  ? 0.706288 0.471545 0.808551 -0.166175   0.0981689   -0.132215   92  ILE   B HG12 
1144 H HG13 . ILE   A 80  ? 0.662371 0.470839 0.779696 -0.158001   0.0988715   -0.165599   92  ILE   B HG13 
1145 H HG21 . ILE   A 80  ? 0.719339 0.460857 0.714437 -0.146069   0.100168    -0.0915396  92  ILE   B HG21 
1146 H HG22 . ILE   A 80  ? 0.742106 0.445687 0.767443 -0.144131   0.0770514   -0.0920186  92  ILE   B HG22 
1147 H HG23 . ILE   A 80  ? 0.719896 0.441344 0.707212 -0.13275    0.0753902   -0.0984463  92  ILE   B HG23 
1148 H HD11 . ILE   A 80  ? 0.658796 0.505286 0.711402 -0.153781   0.121804    -0.143844   92  ILE   B HD11 
1149 H HD12 . ILE   A 80  ? 0.67597  0.522008 0.770628 -0.173013   0.124497    -0.144159   92  ILE   B HD12 
1150 H HD13 . ILE   A 80  ? 0.70005  0.51218  0.740427 -0.161762   0.125221    -0.114119   92  ILE   B HD13 
1151 N N    . GLY   A 81  ? 0.58148  0.344088 0.64567  -0.123118   0.0524945   -0.142581   93  GLY   B N    
1152 C CA   . GLY   A 81  ? 0.608885 0.350771 0.647738 -0.117491   0.0315202   -0.13235    93  GLY   B CA   
1153 C C    . GLY   A 81  ? 0.648302 0.392622 0.736433 -0.110955   0.00729014  -0.139306   93  GLY   B C    
1154 O O    . GLY   A 81  ? 0.670798 0.386286 0.744786 -0.104093   -0.0201828  -0.127425   93  GLY   B O    
1155 H H    . GLY   A 81  ? 0.558336 0.347794 0.628304 -0.125673   0.0654307   -0.15319    93  GLY   B H    
1156 H HA2  . GLY   A 81  ? 0.645104 0.358662 0.646511 -0.115189   0.0264737   -0.116938   93  GLY   B HA2  
1157 H HA3  . GLY   A 81  ? 0.602087 0.356371 0.626458 -0.119422   0.0371653   -0.135744   93  GLY   B HA3  
1158 N N    . VAL   A 82  ? 0.617225 0.401552 0.763201 -0.110407   0.0172485   -0.159636   94  VAL   B N    
1159 C CA   . VAL   A 82  ? 0.572975 0.374479 0.776693 -0.101686   -0.00111377 -0.16776    94  VAL   B CA   
1160 C C    . VAL   A 82  ? 0.609579 0.378594 0.83289  -0.0882139  -0.0191595  -0.163578   94  VAL   B C    
1161 O O    . VAL   A 82  ? 0.586041 0.352866 0.840966 -0.0763245  -0.0463903  -0.160657   94  VAL   B O    
1162 C CB   . VAL   A 82  ? 0.578008 0.436391 0.831626 -0.102081   0.0219849   -0.189264   94  VAL   B CB   
1163 C CG1  . VAL   A 82  ? 0.585263 0.474467 0.913163 -0.0889076  0.0101959   -0.200512   94  VAL   B CG1  
1164 C CG2  . VAL   A 82  ? 0.564674 0.444754 0.796288 -0.115755   0.0357276   -0.184737   94  VAL   B CG2  
1165 H H    . VAL   A 82  ? 0.586281 0.390194 0.735393 -0.113934   0.0358025   -0.16875    94  VAL   B H    
1166 H HA   . VAL   A 82  ? 0.599519 0.395947 0.794632 -0.103483   -0.0173242  -0.160493   94  VAL   B HA   
1167 H HB   . VAL   A 82  ? 0.566122 0.427499 0.817158 -0.100738   0.0372964   -0.198906   94  VAL   B HB   
1168 H HG11 . VAL   A 82  ? 0.595205 0.47802  0.929621 -0.089552   -0.0115017  -0.19088    94  VAL   B HG11 
1169 H HG12 . VAL   A 82  ? 0.596628 0.47244  0.940124 -0.0775416  0.00625887  -0.206992   94  VAL   B HG12 
1170 H HG13 . VAL   A 82  ? 0.564928 0.494332 0.918805 -0.0902557  0.0281018   -0.210798   94  VAL   B HG13 
1171 H HG21 . VAL   A 82  ? 0.546923 0.463343 0.806863 -0.11581    0.052138    -0.194547   94  VAL   B HG21 
1172 H HG22 . VAL   A 82  ? 0.562546 0.427679 0.751394 -0.119881   0.0448857   -0.179845   94  VAL   B HG22 
1173 H HG23 . VAL   A 82  ? 0.573935 0.445525 0.806005 -0.119596   0.018466    -0.176611   94  VAL   B HG23 
1174 N N    . ALA   A 83  ? 0.62116  0.363033 0.828396 -0.09065    -0.00692193 -0.16127    95  ALA   B N    
1175 C CA   . ALA   A 83  ? 0.684813 0.380542 0.903217 -0.0804107  -0.0242029  -0.150597   95  ALA   B CA   
1176 C C    . ALA   A 83  ? 0.739356 0.391535 0.910604 -0.0752044  -0.0507265  -0.119128   95  ALA   B C    
1177 O O    . ALA   A 83  ? 0.837126 0.45108  1.01845  -0.0617977  -0.0719944  -0.105958   95  ALA   B O    
1178 C CB   . ALA   A 83  ? 0.715469 0.38524  0.927429 -0.0910131  -0.0069691  -0.15049    95  ALA   B CB   
1179 H H    . ALA   A 83  ? 0.609619 0.361339 0.801332 -0.0994141  0.0114294   -0.165595   95  ALA   B H    
1180 H HA   . ALA   A 83  ? 0.684855 0.392919 0.949549 -0.0679101  -0.0324683  -0.163996   95  ALA   B HA   
1181 H HB1  . ALA   A 83  ? 0.688341 0.383652 0.926291 -0.0925552  0.00611538  -0.173371   95  ALA   B HB1  
1182 H HB2  . ALA   A 83  ? 0.711297 0.374977 0.88397  -0.102401   0.00267495  -0.136373   95  ALA   B HB2  
1183 H HB3  . ALA   A 83  ? 0.747947 0.381566 0.969996 -0.0847272  -0.0191989  -0.141636   95  ALA   B HB3  
1184 N N    . THR   A 84  ? 0.798536 0.45014  0.911973 -0.0828819  -0.0502288  -0.107015   96  THR   B N    
1185 C CA   . THR   A 84  ? 0.855917 0.465442 0.910509 -0.0747218  -0.0763786  -0.0807915  96  THR   B CA   
1186 C C    . THR   A 84  ? 0.864545 0.488145 0.939722 -0.064196   -0.113408   -0.0880273  96  THR   B C    
1187 O O    . THR   A 84  ? 0.900327 0.490456 0.926929 -0.0542911  -0.143433   -0.0707404  96  THR   B O    
1188 C CB   . THR   A 84  ? 0.864924 0.461621 0.839625 -0.083291   -0.0591446  -0.0672538  96  THR   B CB   
1189 O OG1  . THR   A 84  ? 0.81191  0.440001 0.785506 -0.0887104  -0.0576641  -0.0859945  96  THR   B OG1  
1190 C CG2  . THR   A 84  ? 0.851718 0.44973  0.81837  -0.0962874  -0.0220906  -0.0603299  96  THR   B CG2  
1191 H H    . THR   A 84  ? 0.751647 0.426797 0.857481 -0.0915177  -0.033855   -0.115666   96  THR   B H    
1192 H HA   . THR   A 84  ? 0.890952 0.46923  0.942821 -0.0687633  -0.0827414  -0.0661292  96  THR   B HA   
1193 H HB   . THR   A 84  ? 0.910656 0.475959 0.839729 -0.0753326  -0.0751453  -0.0495924  96  THR   B HB   
1195 H HG21 . THR   A 84  ? 0.865431 0.45809  0.783192 -0.0980133  -0.0112627  -0.0501601  96  THR   B HG21 
1196 H HG22 . THR   A 84  ? 0.808269 0.437253 0.811447 -0.103013   -0.00830206 -0.0789583  96  THR   B HG22 
1197 H HG23 . THR   A 84  ? 0.879846 0.453635 0.854731 -0.0957185  -0.0237012  -0.047427   96  THR   B HG23 
1198 N N    . MET   A 85  ? 0.813773 0.489395 0.959309 -0.0667935  -0.111944   -0.112497   97  MET   B N    
1199 C CA   . MET   A 85  ? 0.816595 0.51584  0.987476 -0.0655766  -0.143547   -0.119355   97  MET   B CA   
1200 C C    . MET   A 85  ? 0.806115 0.522212 1.04955  -0.0461354  -0.174584   -0.122585   97  MET   B C    
1201 O O    . MET   A 85  ? 0.766345 0.4899   1.05883  -0.0338458  -0.162721   -0.129134   97  MET   B O    
1202 C CB   . MET   A 85  ? 0.763659 0.513868 0.970315 -0.0832576  -0.121575   -0.138023   97  MET   B CB   
1203 C CG   . MET   A 85  ? 0.764895 0.49831  0.903056 -0.0978026  -0.0984733  -0.135067   97  MET   B CG   
1204 S SD   . MET   A 85  ? 0.726102 0.511812 0.906162 -0.11666    -0.0717268  -0.150365   97  MET   B SD   
1205 C CE   . MET   A 85  ? 0.745704 0.539697 0.960619 -0.125521   -0.114892   -0.152741   97  MET   B CE   
1206 H H    . MET   A 85  ? 0.78183  0.479946 0.960861 -0.0700336  -0.0910928  -0.124833   97  MET   B H    
1207 H HA   . MET   A 85  ? 0.846836 0.51702  0.963199 -0.0651949  -0.161076   -0.108713   97  MET   B HA   
1208 H HB2  . MET   A 85  ? 0.735413 0.514267 0.986043 -0.0820661  -0.10129    -0.148375   97  MET   B HB2  
1209 H HB3  . MET   A 85  ? 0.769836 0.538105 1.00607  -0.0851143  -0.143363   -0.142029   97  MET   B HB3  
1210 H HG2  . MET   A 85  ? 0.797991 0.503126 0.890971 -0.0971994  -0.117864   -0.12817    97  MET   B HG2  
1211 H HG3  . MET   A 85  ? 0.761023 0.481409 0.874058 -0.0965134  -0.0785291  -0.130469   97  MET   B HG3  
1212 H HE1  . MET   A 85  ? 0.728389 0.546037 0.967698 -0.1391     -0.102939   -0.156914   97  MET   B HE1  
1213 H HE2  . MET   A 85  ? 0.748793 0.562305 1.01221  -0.117765   -0.131224   -0.154939   97  MET   B HE2  
1214 H HE3  . MET   A 85  ? 0.782869 0.538584 0.945123 -0.124341   -0.134935   -0.147901   97  MET   B HE3  
1215 N N    . LYS   A 86  ? 0.797507 0.519458 1.04898  -0.0416252  -0.217801   -0.120472   98  LYS   B N    
1216 C CA   . LYS   A 86  ? 0.802436 0.549115 1.12831  -0.0204165  -0.254213   -0.122921   98  LYS   B CA   
1217 C C    . LYS   A 86  ? 0.773536 0.59893  1.19374  -0.0324334  -0.253496   -0.144141   98  LYS   B C    
1218 O O    . LYS   A 86  ? 0.764766 0.606663 1.17242  -0.0583171  -0.235421   -0.150951   98  LYS   B O    
1219 C CB   . LYS   A 86  ? 0.855473 0.555071 1.12263  -0.00522199 -0.307174   -0.103163   98  LYS   B CB   
1220 H H    . LYS   A 86  ? 0.815076 0.52623  1.02628  -0.0511502  -0.22652    -0.118921   98  LYS   B H    
1221 H HA   . LYS   A 86  ? 0.801956 0.544339 1.15326  -0.00745057 -0.242281   -0.122993   98  LYS   B HA   
1224 N N    . LYS   A 87  ? 0.767347 0.641424 1.28422  -0.0129592  -0.270734   -0.152446   99  LYS   B N    
1225 C CA   . LYS   A 87  ? 0.727803 0.688345 1.34876  -0.0237044  -0.267297   -0.168911   99  LYS   B CA   
1226 C C    . LYS   A 87  ? 0.762801 0.72794  1.37345  -0.0478982  -0.305141   -0.166769   99  LYS   B C    
1227 O O    . LYS   A 87  ? 0.829602 0.75374  1.39389  -0.0388552  -0.355603   -0.157672   99  LYS   B O    
1228 C CB   . LYS   A 87  ? 0.709638 0.725409 1.43902  0.00763782  -0.282161   -0.177588   99  LYS   B CB   
1229 H H    . LYS   A 87  ? 0.794659 0.648259 1.3148   0.00828663  -0.28391    -0.146368   99  LYS   B H    
1230 H HA   . LYS   A 87  ? 0.688574 0.669555 1.31579  -0.036444   -0.227379   -0.176535   99  LYS   B HA   
1233 N N    . GLY   A 88  ? 0.723504 0.729169 1.36548  -0.0794029  -0.280116   -0.174661   100 GLY   B N    
1234 C CA   . GLY   A 88  ? 0.763377 0.768708 1.40419  -0.107086   -0.315039   -0.176189   100 GLY   B CA   
1235 C C    . GLY   A 88  ? 0.792219 0.713932 1.30482  -0.119913   -0.31837    -0.171158   100 GLY   B C    
1236 O O    . GLY   A 88  ? 0.81279  0.72016  1.31195  -0.142491   -0.347288   -0.176581   100 GLY   B O    
1237 H H    . GLY   A 88  ? 0.691794 0.722963 1.35496  -0.0839126  -0.241071   -0.179133   100 GLY   B H    
1238 H HA2  . GLY   A 88  ? 0.729754 0.782638 1.42996  -0.126626   -0.29528    -0.180696   100 GLY   B HA2  
1239 H HA3  . GLY   A 88  ? 0.788597 0.804477 1.45956  -0.0977492  -0.358445   -0.176977   100 GLY   B HA3  
1240 N N    . GLU   A 89  ? 0.803938 0.67296  1.22853  -0.105941   -0.288396   -0.16253    101 GLU   B N    
1241 C CA   . GLU   A 89  ? 0.820249 0.618959 1.12708  -0.112764   -0.284381   -0.157439   101 GLU   B CA   
1242 C C    . GLU   A 89  ? 0.777857 0.585874 1.0831   -0.140203   -0.246969   -0.163184   101 GLU   B C    
1243 O O    . GLU   A 89  ? 0.653926 0.508324 1.01328  -0.146627   -0.204102   -0.16462    101 GLU   B O    
1244 C CB   . GLU   A 89  ? 0.837671 0.590465 1.0691   -0.0920701  -0.260637   -0.143614   101 GLU   B CB   
1245 C CG   . GLU   A 89  ? 0.882066 0.56877  0.992131 -0.0923448  -0.255881   -0.135716   101 GLU   B CG   
1246 C CD   . GLU   A 89  ? 0.862937 0.514666 0.913692 -0.0768688  -0.228546   -0.118002   101 GLU   B CD   
1247 O OE1  . GLU   A 89  ? 0.907986 0.545094 0.962458 -0.0581995  -0.244405   -0.104421   101 GLU   B OE1  
1248 O OE2  . GLU   A 89  ? 0.841515 0.48034  0.844913 -0.0845213  -0.190436   -0.11635    101 GLU   B OE2  
1249 H H    . GLU   A 89  ? 0.778888 0.657577 1.22027  -0.0917053  -0.269573   -0.160549   101 GLU   B H    
1250 H HA   . GLU   A 89  ? 0.869839 0.644264 1.14777  -0.112157   -0.323637   -0.158739   101 GLU   B HA   
1251 H HB2  . GLU   A 89  ? 0.860741 0.607299 1.10035  -0.0746709  -0.282914   -0.137239   101 GLU   B HB2  
1252 H HB3  . GLU   A 89  ? 0.794036 0.568272 1.05105  -0.0941205  -0.224615   -0.145477   101 GLU   B HB3  
1253 H HG2  . GLU   A 89  ? 0.853561 0.543727 0.9555   -0.106882   -0.23513    -0.142041   101 GLU   B HG2  
1254 H HG3  . GLU   A 89  ? 0.924206 0.586622 1.00047  -0.0881074  -0.292126   -0.135912   101 GLU   B HG3  
1255 N N    . ILE   A 90  ? 0.829156 0.591448 1.07246  -0.154138   -0.266614   -0.167336   102 ILE   B N    
1256 C CA   . ILE   A 90  ? 0.833615 0.576375 1.03863  -0.171187   -0.230364   -0.16799    102 ILE   B CA   
1257 C C    . ILE   A 90  ? 0.847667 0.525545 0.932569 -0.153921   -0.218602   -0.163026   102 ILE   B C    
1258 O O    . ILE   A 90  ? 0.880883 0.510609 0.896089 -0.141816   -0.253953   -0.165041   102 ILE   B O    
1259 C CB   . ILE   A 90  ? 0.837715 0.57401  1.0693   -0.200495   -0.253009   -0.177003   102 ILE   B CB   
1260 C CG1  . ILE   A 90  ? 0.839423 0.651912 1.20299  -0.220458   -0.263096   -0.178619   102 ILE   B CG1  
1261 C CG2  . ILE   A 90  ? 0.807837 0.516489 0.996829 -0.213308   -0.213588   -0.173631   102 ILE   B CG2  
1262 C CD1  . ILE   A 90  ? 0.852016 0.658643 1.25706  -0.253334   -0.300377   -0.187216   102 ILE   B CD1  
1263 H H    . ILE   A 90  ? 0.874964 0.615548 1.09763  -0.150948   -0.304922   -0.170667   102 ILE   B H    
1264 H HA   . ILE   A 90  ? 0.77574  0.553117 1.01751  -0.173919   -0.195679   -0.164786   102 ILE   B HA   
1265 H HB   . ILE   A 90  ? 0.894048 0.591844 1.08288  -0.196966   -0.289867   -0.183941   102 ILE   B HB   
1266 H HG12 . ILE   A 90  ? 0.782524 0.631367 1.18265  -0.225323   -0.223968   -0.172522   102 ILE   B HG12 
1267 H HG13 . ILE   A 90  ? 0.825082 0.659368 1.21674  -0.206062   -0.283009   -0.179611   102 ILE   B HG13 
1268 H HG21 . ILE   A 90  ? 0.834292 0.537863 1.04919  -0.234134   -0.22617    -0.177241   102 ILE   B HG21 
1269 H HG22 . ILE   A 90  ? 0.76885  0.511252 0.984049 -0.212771   -0.176978   -0.166464   102 ILE   B HG22 
1270 H HG23 . ILE   A 90  ? 0.840149 0.502211 0.949846 -0.200112   -0.213069   -0.174763   102 ILE   B HG23 
1271 H HD11 . ILE   A 90  ? 0.906832 0.682636 1.28085  -0.247545   -0.344073   -0.196478   102 ILE   B HD11 
1272 H HD12 . ILE   A 90  ? 0.836997 0.70207  1.33414  -0.267166   -0.298655   -0.185136   102 ILE   B HD12 
1273 H HD13 . ILE   A 90  ? 0.869824 0.644955 1.242    -0.266405   -0.283398   -0.185671   102 ILE   B HD13 
1274 N N    . ALA   A 91  ? 0.799605 0.482318 0.862997 -0.152313   -0.16881    -0.156973   103 ALA   B N    
1275 C CA   . ALA   A 91  ? 0.832365 0.470655 0.799365 -0.137098   -0.148914   -0.150831   103 ALA   B CA   
1276 C C    . ALA   A 91  ? 0.819913 0.450361 0.762816 -0.145701   -0.1169     -0.152682   103 ALA   B C    
1277 O O    . ALA   A 91  ? 0.838592 0.504845 0.840499 -0.161957   -0.0980721  -0.153104   103 ALA   B O    
1278 C CB   . ALA   A 91  ? 0.844247 0.498394 0.813094 -0.122805   -0.124233   -0.139612   103 ALA   B CB   
1279 H H    . ALA   A 91  ? 0.764711 0.483842 0.877404 -0.160451   -0.146311   -0.156731   103 ALA   B H    
1280 H HA   . ALA   A 91  ? 0.887659 0.488339 0.802727 -0.1295     -0.174866   -0.152638   103 ALA   B HA   
1281 H HB1  . ALA   A 91  ? 0.849777 0.5008   0.828641 -0.115193   -0.146384   -0.136254   103 ALA   B HB1  
1282 H HB2  . ALA   A 91  ? 0.787573 0.477107 0.804479 -0.128578   -0.101975   -0.141503   103 ALA   B HB2  
1283 H HB3  . ALA   A 91  ? 0.844794 0.476128 0.757273 -0.115115   -0.109072   -0.133865   103 ALA   B HB3  
1284 N N    . HIS   A 92  ? 0.861451 0.44451  0.714604 -0.131792   -0.111194   -0.15233    104 HIS   B N    
1285 C CA   . HIS   A 92  ? 0.848837 0.421313 0.667307 -0.129302   -0.0788621  -0.15159    104 HIS   B CA   
1286 C C    . HIS   A 92  ? 0.819013 0.409981 0.610095 -0.113407   -0.0423352  -0.14112    104 HIS   B C    
1287 O O    . HIS   A 92  ? 0.872989 0.449446 0.623113 -0.0998045  -0.0459194  -0.134581   104 HIS   B O    
1288 C CB   . HIS   A 92  ? 0.943756 0.451422 0.687092 -0.121429   -0.0994445  -0.16253    104 HIS   B CB   
1289 C CG   . HIS   A 92  ? 0.970284 0.456345 0.747772 -0.143601   -0.133086   -0.174232   104 HIS   B CG   
1290 N ND1  . HIS   A 92  ? 1.04963  0.4694   0.769086 -0.140797   -0.158977   -0.18978    104 HIS   B ND1  
1291 C CD2  . HIS   A 92  ? 0.936476 0.459783 0.804741 -0.170261   -0.143342   -0.172897   104 HIS   B CD2  
1292 C CE1  . HIS   A 92  ? 1.07292  0.487019 0.850243 -0.169206   -0.187512   -0.197008   104 HIS   B CE1  
1293 N NE2  . HIS   A 92  ? 0.996285 0.477971 0.867277 -0.187872   -0.176247   -0.184897   104 HIS   B NE2  
1294 H H    . HIS   A 92  ? 0.89852  0.455372 0.708444 -0.120804   -0.128605   -0.152154   104 HIS   B H    
1295 H HA   . HIS   A 92  ? 0.823576 0.420056 0.688225 -0.14264    -0.0678208  -0.151063   104 HIS   B HA   
1296 H HB2  . HIS   A 92  ? 0.974711 0.460125 0.671449 -0.108079   -0.113577   -0.163985   104 HIS   B HB2  
1297 H HB3  . HIS   A 92  ? 0.936594 0.436223 0.651003 -0.113173   -0.0763858  -0.160766   104 HIS   B HB3  
1299 H HD2  . HIS   A 92  ? 0.891049 0.461054 0.813141 -0.175706   -0.130245   -0.16589    104 HIS   B HD2  
1300 H HE1  . HIS   A 92  ? 1.12376  0.49265  0.880074 -0.175144   -0.211487   -0.209569   104 HIS   B HE1  
1302 N N    . LEU   A 93  ? 0.775703 0.401116 0.592921 -0.116866   -0.00872522 -0.138052   105 LEU   B N    
1303 C CA   . LEU   A 93  ? 0.740728 0.392771 0.546857 -0.106477   0.023559    -0.131061   105 LEU   B CA   
1304 C C    . LEU   A 93  ? 0.735596 0.381897 0.505569 -0.0963767  0.0445672   -0.130746   105 LEU   B C    
1305 O O    . LEU   A 93  ? 0.685612 0.335392 0.475554 -0.104433   0.0479012   -0.132122   105 LEU   B O    
1306 C CB   . LEU   A 93  ? 0.696897 0.402151 0.570774 -0.116285   0.0399807   -0.131834   105 LEU   B CB   
1307 C CG   . LEU   A 93  ? 0.684152 0.399685 0.602448 -0.120501   0.0244528   -0.132577   105 LEU   B CG   
1308 C CD1  . LEU   A 93  ? 0.596168 0.359762 0.571669 -0.125185   0.0452596   -0.139633   105 LEU   B CD1  
1309 C CD2  . LEU   A 93  ? 0.726026 0.412907 0.60554  -0.11073    0.0162706   -0.121773   105 LEU   B CD2  
1310 H H    . LEU   A 93  ? 0.762332 0.396284 0.606905 -0.127041   -0.00702711 -0.140048   105 LEU   B H    
1311 H HA   . LEU   A 93  ? 0.762226 0.400406 0.538094 -0.0978724  0.0207952   -0.126385   105 LEU   B HA   
1312 H HB2  . LEU   A 93  ? 0.677388 0.397595 0.576422 -0.123682   0.0443064   -0.134953   105 LEU   B HB2  
1313 H HB3  . LEU   A 93  ? 0.67858  0.399587 0.543903 -0.111163   0.0588999   -0.129424   105 LEU   B HB3  
1314 H HG   . LEU   A 93  ? 0.687421 0.397863 0.625586 -0.125887   0.00542242  -0.135872   105 LEU   B HG   
1315 H HD11 . LEU   A 93  ? 0.591617 0.375032 0.588428 -0.13038    0.051789    -0.144304   105 LEU   B HD11 
1316 H HD12 . LEU   A 93  ? 0.605894 0.372349 0.610421 -0.125016   0.0355177   -0.141396   105 LEU   B HD12 
1317 H HD13 . LEU   A 93  ? 0.599571 0.370351 0.560177 -0.122165   0.0609997   -0.138093   105 LEU   B HD13 
1318 H HD21 . LEU   A 93  ? 0.760871 0.417426 0.600724 -0.105599   0.00061126  -0.119753   105 LEU   B HD21 
1319 H HD22 . LEU   A 93  ? 0.718218 0.411824 0.580861 -0.107531   0.0357843   -0.117039   105 LEU   B HD22 
1320 H HD23 . LEU   A 93  ? 0.719247 0.411041 0.629907 -0.112108   0.00707278  -0.120938   105 LEU   B HD23 
1321 N N    . LEU   A 94  ? 0.683608 0.322633 0.402908 -0.0776345  0.0596343   -0.126387   106 LEU   B N    
1322 C CA   . LEU   A 94  ? 0.68595  0.334244 0.381539 -0.0621984  0.0826517   -0.125114   106 LEU   B CA   
1323 C C    . LEU   A 94  ? 0.671856 0.376934 0.395247 -0.0607766  0.108788    -0.118582   106 LEU   B C    
1324 O O    . LEU   A 94  ? 0.725719 0.441012 0.446676 -0.0607601  0.115249    -0.111457   106 LEU   B O    
1325 C CB   . LEU   A 94  ? 0.767419 0.367672 0.387222 -0.0377984  0.0798604   -0.128669   106 LEU   B CB   
1326 C CG   . LEU   A 94  ? 0.795839 0.399853 0.389794 -0.0143724  0.100764    -0.128759   106 LEU   B CG   
1327 C CD1  . LEU   A 94  ? 0.79873  0.381946 0.40675  -0.0201354  0.0932807   -0.130839   106 LEU   B CD1  
1328 C CD2  . LEU   A 94  ? 0.930874 0.492291 0.448544 0.0150874   0.10175     -0.13517    106 LEU   B CD2  
1329 H H    . LEU   A 94  ? 0.718101 0.348131 0.417988 -0.0730948  0.055845    -0.122814   106 LEU   B H    
1330 H HA   . LEU   A 94  ? 0.684252 0.333559 0.396875 -0.0678834  0.0820482   -0.126827   106 LEU   B HA   
1331 H HB2  . LEU   A 94  ? 0.800063 0.360801 0.404203 -0.0414054  0.0582769   -0.135869   106 LEU   B HB2  
1332 H HB3  . LEU   A 94  ? 0.781212 0.38404  0.381136 -0.0316668  0.0840375   -0.124332   106 LEU   B HB3  
1333 H HG   . LEU   A 94  ? 0.768772 0.418521 0.386395 -0.0128181  0.119569    -0.122415   106 LEU   B HG   
1334 H HD11 . LEU   A 94  ? 0.755276 0.371346 0.407144 -0.0358458  0.0971639   -0.126192   106 LEU   B HD11 
1335 H HD12 . LEU   A 94  ? 0.81479  0.395262 0.402265 -0.00146154 0.104323    -0.129873   106 LEU   B HD12 
1336 H HD13 . LEU   A 94  ? 0.832548 0.371972 0.426106 -0.0262318  0.073473    -0.137134   106 LEU   B HD13 
1337 H HD21 . LEU   A 94  ? 0.911801 0.490718 0.419681 0.0185781   0.111213    -0.129418   106 LEU   B HD21 
1338 H HD22 . LEU   A 94  ? 0.95077  0.4646   0.442355 0.0133126   0.0797679   -0.144366   106 LEU   B HD22 
1339 H HD23 . LEU   A 94  ? 0.922414 0.486455 0.426203 0.033469    0.11476     -0.136058   106 LEU   B HD23 
1340 N N    . ILE   A 95  ? 0.603818 0.344313 0.352357 -0.060307   0.122547    -0.119641   107 ILE   B N    
1341 C CA   . ILE   A 95  ? 0.573616 0.371916 0.364818 -0.0665544  0.137899    -0.119808   107 ILE   B CA   
1342 C C    . ILE   A 95  ? 0.580105 0.412168 0.362377 -0.0486659  0.154765    -0.117827   107 ILE   B C    
1343 O O    . ILE   A 95  ? 0.560838 0.391242 0.334054 -0.0402628  0.15472     -0.11784    107 ILE   B O    
1344 C CB   . ILE   A 95  ? 0.539182 0.359764 0.378818 -0.0842118  0.132788    -0.127558   107 ILE   B CB   
1345 C CG1  . ILE   A 95  ? 0.553632 0.350116 0.413747 -0.0980938  0.114963    -0.130013   107 ILE   B CG1  
1346 C CG2  . ILE   A 95  ? 0.531676 0.405474 0.410036 -0.0897055  0.143633    -0.134732   107 ILE   B CG2  
1347 C CD1  . ILE   A 95  ? 0.545516 0.359075 0.446817 -0.109999   0.111927    -0.136656   107 ILE   B CD1  
1348 H H    . ILE   A 95  ? 0.627122 0.35323  0.364145 -0.0558563  0.120653    -0.120455   107 ILE   B H    
1349 H HA   . ILE   A 95  ? 0.57377  0.37611  0.370018 -0.0702715  0.139816    -0.116695   107 ILE   B HA   
1350 H HB   . ILE   A 95  ? 0.550489 0.367311 0.383147 -0.0815391  0.133376    -0.126939   107 ILE   B HB   
1351 H HG12 . ILE   A 95  ? 0.547004 0.351027 0.421933 -0.101918   0.115002    -0.130107   107 ILE   B HG12 
1352 H HG13 . ILE   A 95  ? 0.582025 0.343901 0.414016 -0.0944254  0.10454     -0.126716   107 ILE   B HG13 
1353 H HG21 . ILE   A 95  ? 0.508101 0.39229  0.412712 -0.0984645  0.140519    -0.142188   107 ILE   B HG21 
1354 H HG22 . ILE   A 95  ? 0.52443  0.400615 0.409378 -0.0928234  0.145233    -0.132576   107 ILE   B HG22 
1355 H HG23 . ILE   A 95  ? 0.521345 0.416285 0.392025 -0.0808668  0.15127     -0.134441   107 ILE   B HG23 
1356 H HD11 . ILE   A 95  ? 0.550904 0.358493 0.439318 -0.10827    0.114764    -0.133279   107 ILE   B HD11 
1357 H HD12 . ILE   A 95  ? 0.546737 0.346172 0.463036 -0.116416   0.09872     -0.137711   107 ILE   B HD12 
1358 H HD13 . ILE   A 95  ? 0.519096 0.364376 0.445145 -0.112212   0.120458    -0.143028   107 ILE   B HD13 
1359 N N    . LYS   A 96  ? 0.577081 0.44616  0.371158 -0.0450335  0.168936    -0.114051   108 LYS   B N    
1360 C CA   . LYS   A 96  ? 0.580207 0.499366 0.384103 -0.0293682  0.182733    -0.113187   108 LYS   B CA   
1361 C C    . LYS   A 96  ? 0.553131 0.520457 0.402453 -0.0418068  0.178707    -0.122864   108 LYS   B C    
1362 O O    . LYS   A 96  ? 0.521473 0.490078 0.401347 -0.0637044  0.17122     -0.131113   108 LYS   B O    
1363 C CB   . LYS   A 96  ? 0.577668 0.528102 0.389903 -0.0255305  0.200731    -0.104295   108 LYS   B CB   
1364 C CG   . LYS   A 96  ? 0.649124 0.558501 0.403893 -0.00599053 0.209319    -0.0958497  108 LYS   B CG   
1365 C CD   . LYS   A 96  ? 0.662389 0.605336 0.419827 -0.00145973 0.234802    -0.0816176  108 LYS   B CD   
1366 C CE   . LYS   A 96  ? 0.718703 0.620825 0.402459 0.0284116   0.244987    -0.0778322  108 LYS   B CE   
1367 N NZ   . LYS   A 96  ? 0.772155 0.705208 0.457488 0.0267295   0.272389    -0.0592949  108 LYS   B NZ   
1368 H H    . LYS   A 96  ? 0.581272 0.44582  0.380326 -0.0530443  0.169525    -0.110573   108 LYS   B H    
1369 H HA   . LYS   A 96  ? 0.600001 0.50116  0.37395  -0.011371   0.182678    -0.111832   108 LYS   B HA   
1370 H HB2  . LYS   A 96  ? 0.570415 0.530123 0.411213 -0.045084   0.199962    -0.103425   108 LYS   B HB2  
1371 H HB3  . LYS   A 96  ? 0.577385 0.570462 0.407484 -0.0165086  0.208344    -0.104688   108 LYS   B HB3  
1372 H HG2  . LYS   A 96  ? 0.66373  0.559782 0.390778 0.0148078   0.20923     -0.0989773  108 LYS   B HG2  
1373 H HG3  . LYS   A 96  ? 0.655576 0.522698 0.391401 -0.0143482  0.197409    -0.0966288  108 LYS   B HG3  
1374 H HD2  . LYS   A 96  ? 0.65447  0.596371 0.430899 -0.0221195  0.23405     -0.0754179  108 LYS   B HD2  
1375 H HD3  . LYS   A 96  ? 0.645767 0.639896 0.435479 0.00287796  0.24561     -0.0809386  108 LYS   B HD3  
1376 H HE2  . LYS   A 96  ? 0.739787 0.647649 0.409162 0.0516538   0.249516    -0.0832959  108 LYS   B HE2  
1377 H HE3  . LYS   A 96  ? 0.748208 0.598186 0.397826 0.0260539   0.229027    -0.0819091  108 LYS   B HE3  
1378 H HZ1  . LYS   A 96  ? 0.750802 0.734026 0.466285 0.0324534   0.288422    -0.0560307  108 LYS   B HZ1  
1379 H HZ2  . LYS   A 96  ? 0.747867 0.680317 0.455947 0.0036797   0.268683    -0.0522059  108 LYS   B HZ2  
1380 H HZ3  . LYS   A 96  ? 0.806695 0.710012 0.440082 0.0436299   0.277656    -0.057343   108 LYS   B HZ3  
1381 N N    . PRO   A 97  ? 0.562436 0.57058  0.414268 -0.0244441  0.181788    -0.12388    109 PRO   B N    
1382 C CA   . PRO   A 97  ? 0.54711  0.596064 0.423952 -0.0303016  0.174215    -0.134642   109 PRO   B CA   
1383 C C    . PRO   A 97  ? 0.550344 0.638567 0.479755 -0.0548874  0.170036    -0.149551   109 PRO   B C    
1384 O O    . PRO   A 97  ? 0.560961 0.660301 0.503905 -0.0651108  0.161538    -0.164475   109 PRO   B O    
1385 C CB   . PRO   A 97  ? 0.560932 0.647686 0.427578 -0.00228694 0.175367    -0.130118   109 PRO   B CB   
1386 C CG   . PRO   A 97  ? 0.584284 0.651203 0.42504  0.0208958   0.186488    -0.118354   109 PRO   B CG   
1387 C CD   . PRO   A 97  ? 0.632923 0.644294 0.455426 0.00726215  0.190634    -0.115339   109 PRO   B CD   
1388 H HA   . PRO   A 97  ? 0.554228 0.57786  0.416471 -0.0332991  0.169958    -0.134943   109 PRO   B HA   
1389 H HB2  . PRO   A 97  ? 0.546092 0.681916 0.444526 -0.00608657 0.172784    -0.137529   109 PRO   B HB2  
1390 H HB3  . PRO   A 97  ? 0.571422 0.646422 0.416386 0.0057871   0.170816    -0.127716   109 PRO   B HB3  
1391 H HG2  . PRO   A 97  ? 0.588204 0.69975  0.453301 0.026856    0.192362    -0.118402   109 PRO   B HG2  
1392 H HG3  . PRO   A 97  ? 0.616996 0.661959 0.427111 0.0405446   0.184711    -0.112677   109 PRO   B HG3  
1393 H HD2  . PRO   A 97  ? 0.617348 0.643237 0.44643  0.0098977   0.200686    -0.111849   109 PRO   B HD2  
1394 H HD3  . PRO   A 97  ? 0.638579 0.603394 0.424588 0.0174023   0.187939    -0.1118     109 PRO   B HD3  
1395 N N    . GLU   A 98  ? 0.531195 0.635432 0.488576 -0.064673   0.177336    -0.145266   110 GLU   B N    
1396 C CA   . GLU   A 98  ? 0.533373 0.664873 0.54546  -0.0914669  0.172431    -0.157325   110 GLU   B CA   
1397 C C    . GLU   A 98  ? 0.476888 0.565903 0.49543  -0.109703   0.163376    -0.16776    110 GLU   B C    
1398 O O    . GLU   A 98  ? 0.44636  0.551658 0.503609 -0.126564   0.15413     -0.186212   110 GLU   B O    
1399 C CB   . GLU   A 98  ? 0.546404 0.692647 0.581928 -0.0995958  0.187749    -0.140796   110 GLU   B CB   
1400 C CG   . GLU   A 98  ? 0.61695  0.825684 0.666928 -0.0816175  0.197999    -0.13431    110 GLU   B CG   
1401 C CD   . GLU   A 98  ? 0.707084 0.902305 0.703634 -0.0449863  0.209386    -0.121603   110 GLU   B CD   
1402 O OE1  . GLU   A 98  ? 0.626377 0.756017 0.568284 -0.0354442  0.212153    -0.114304   110 GLU   B OE1  
1403 O OE2  . GLU   A 98  ? 0.758749 1.01179  0.772996 -0.0249623  0.211969    -0.121621   110 GLU   B OE2  
1404 H H    . GLU   A 98  ? 0.552722 0.648236 0.494096 -0.0546722  0.186369    -0.13399    110 GLU   B H    
1405 H HA   . GLU   A 98  ? 0.5146   0.685876 0.545802 -0.0907366  0.165166    -0.169239   110 GLU   B HA   
1406 H HB2  . GLU   A 98  ? 0.573315 0.680934 0.579044 -0.0952957  0.194758    -0.128431   110 GLU   B HB2  
1407 H HB3  . GLU   A 98  ? 0.556242 0.709524 0.62882  -0.120955   0.184344    -0.145869   110 GLU   B HB3  
1408 H HG2  . GLU   A 98  ? 0.618588 0.849382 0.700343 -0.0941782  0.208147    -0.126193   110 GLU   B HG2  
1409 H HG3  . GLU   A 98  ? 0.604238 0.848832 0.675302 -0.0815093  0.186353    -0.147647   110 GLU   B HG3  
1410 N N    . TYR   A 99  ? 0.465312 0.501621 0.450137 -0.105146   0.16386     -0.158194   111 TYR   B N    
1411 C CA   . TYR   A 99  ? 0.483167 0.485384 0.479765 -0.11751    0.154875    -0.166293   111 TYR   B CA   
1412 C C    . TYR   A 99  ? 0.501559 0.499299 0.480624 -0.108921   0.151525    -0.174461   111 TYR   B C    
1413 O O    . TYR   A 99  ? 0.500518 0.474448 0.488871 -0.114463   0.146355    -0.178677   111 TYR   B O    
1414 C CB   . TYR   A 99  ? 0.468893 0.423173 0.448965 -0.120545   0.154942    -0.148085   111 TYR   B CB   
1415 C CG   . TYR   A 99  ? 0.505042 0.464575 0.503223 -0.131988   0.163438    -0.134845   111 TYR   B CG   
1416 C CD1  . TYR   A 99  ? 0.493233 0.4776   0.477699 -0.123647   0.179686    -0.120117   111 TYR   B CD1  
1417 C CD2  . TYR   A 99  ? 0.52676  0.47105  0.563423 -0.151616   0.157122    -0.137189   111 TYR   B CD2  
1418 C CE1  . TYR   A 99  ? 0.519437 0.517468 0.52775  -0.137363   0.193006    -0.103988   111 TYR   B CE1  
1419 C CE2  . TYR   A 99  ? 0.550292 0.496289 0.60783  -0.16687    0.166919    -0.120053   111 TYR   B CE2  
1420 C CZ   . TYR   A 99  ? 0.538011 0.515466 0.583239 -0.161639   0.186819    -0.102048   111 TYR   B CZ   
1421 O OH   . TYR   A 99  ? 0.564891 0.548654 0.634945 -0.179358   0.201258    -0.0806851  111 TYR   B OH   
1422 H H    . TYR   A 99  ? 0.485617 0.507403 0.440776 -0.0927902  0.168705    -0.147082   111 TYR   B H    
1423 H HA   . TYR   A 99  ? 0.472381 0.488395 0.501411 -0.129172   0.150775    -0.178414   111 TYR   B HA   
1424 H HB2  . TYR   A 99  ? 0.49104  0.430169 0.437052 -0.108767   0.157353    -0.139074   111 TYR   B HB2  
1425 H HB3  . TYR   A 99  ? 0.48102  0.413881 0.470616 -0.125883   0.146533    -0.152921   111 TYR   B HB3  
1426 H HD1  . TYR   A 99  ? 0.500806 0.492551 0.459865 -0.107606   0.183338    -0.119428   111 TYR   B HD1  
1427 H HD2  . TYR   A 99  ? 0.518661 0.448041 0.567413 -0.154073   0.146741    -0.148947   111 TYR   B HD2  
1428 H HE1  . TYR   A 99  ? 0.528953 0.549169 0.529277 -0.129701   0.207278    -0.0931486  111 TYR   B HE1  
1429 H HE2  . TYR   A 99  ? 0.556595 0.483455 0.638775 -0.18036    0.161482    -0.119733   111 TYR   B HE2  
1431 N N    . ALA   A 100 ? 0.50317  0.526233 0.45936  -0.0946655  0.155506    -0.17366    112 ALA   B N    
1432 C CA   . ALA   A 100 ? 0.479463 0.499535 0.416001 -0.0880686  0.157323    -0.174123   112 ALA   B CA   
1433 C C    . ALA   A 100 ? 0.461593 0.530016 0.395302 -0.0798589  0.15723     -0.187394   112 ALA   B C    
1434 O O    . ALA   A 100 ? 0.432671 0.525288 0.39247  -0.0877802  0.152273    -0.210653   112 ALA   B O    
1435 C CB   . ALA   A 100 ? 0.521285 0.504364 0.418018 -0.0768934  0.160242    -0.152954   112 ALA   B CB   
1436 H H    . ALA   A 100 ? 0.497278 0.541471 0.45111  -0.0884789  0.157812    -0.170803   112 ALA   B H    
1437 H HA   . ALA   A 100 ? 0.480642 0.489714 0.433142 -0.0965754  0.155696    -0.180353   112 ALA   B HA   
1438 H HB1  . ALA   A 100 ? 0.517367 0.469625 0.414714 -0.0830277  0.156758    -0.148796   112 ALA   B HB1  
1439 H HB2  . ALA   A 100 ? 0.521631 0.511051 0.403972 -0.0658634  0.162047    -0.147214   112 ALA   B HB2  
1440 H HB3  . ALA   A 100 ? 0.522964 0.505599 0.407907 -0.0739681  0.163114    -0.149479   112 ALA   B HB3  
1441 N N    . TYR   A 101 ? 0.500894 0.581192 0.400316 -0.061567   0.159619    -0.174738   113 TYR   B N    
1442 C CA   . TYR   A 101 ? 0.506831 0.631425 0.391766 -0.04961    0.156105    -0.184417   113 TYR   B CA   
1443 C C    . TYR   A 101 ? 0.535279 0.701353 0.423735 -0.0358596  0.146753    -0.185435   113 TYR   B C    
1444 O O    . TYR   A 101 ? 0.51691  0.721114 0.387348 -0.0211923  0.138477    -0.191166   113 TYR   B O    
1445 C CB   . TYR   A 101 ? 0.555535 0.662035 0.395853 -0.0374084  0.165588    -0.164537   113 TYR   B CB   
1446 C CG   . TYR   A 101 ? 0.52424  0.608833 0.374052 -0.052518   0.176471    -0.164918   113 TYR   B CG   
1447 C CD1  . TYR   A 101 ? 0.545341 0.659784 0.404455 -0.0558614  0.181029    -0.185541   113 TYR   B CD1  
1448 C CD2  . TYR   A 101 ? 0.519313 0.556444 0.374383 -0.0627189  0.180367    -0.148292   113 TYR   B CD2  
1449 C CE1  . TYR   A 101 ? 0.532866 0.63784  0.40958  -0.0662798  0.193858    -0.185906   113 TYR   B CE1  
1450 C CE2  . TYR   A 101 ? 0.520168 0.548009 0.397849 -0.077197   0.187962    -0.14893    113 TYR   B CE2  
1451 C CZ   . TYR   A 101 ? 0.519001 0.584323 0.409225 -0.0779161  0.19755     -0.165381   113 TYR   B CZ   
1452 O OH   . TYR   A 101 ? 0.516472 0.58269  0.437199 -0.0889224  0.20791     -0.16603    113 TYR   B OH   
1453 H H    . TYR   A 101 ? 0.5024   0.560676 0.383992 -0.054406   0.162079    -0.16007    113 TYR   B H    
1454 H HA   . TYR   A 101 ? 0.513264 0.65367  0.415514 -0.0580324  0.153163    -0.203482   113 TYR   B HA   
1455 H HB2  . TYR   A 101 ? 0.554925 0.636259 0.378641 -0.0296858  0.167128    -0.14696    113 TYR   B HB2  
1456 H HB3  . TYR   A 101 ? 0.561315 0.696452 0.383577 -0.0263907  0.162987    -0.167985   113 TYR   B HB3  
1457 H HD1  . TYR   A 101 ? 0.546073 0.690687 0.398374 -0.0489064  0.175375    -0.200373   113 TYR   B HD1  
1458 H HD2  . TYR   A 101 ? 0.52574  0.538284 0.370171 -0.0587949  0.176639    -0.137617   113 TYR   B HD2  
1459 H HE1  . TYR   A 101 ? 0.541028 0.669103 0.421139 -0.0643824  0.199451    -0.201179   113 TYR   B HE1  
1460 H HE2  . TYR   A 101 ? 0.52157  0.519361 0.404739 -0.0848162  0.186963    -0.138051   113 TYR   B HE2  
1462 N N    . GLY   A 102 ? 0.50432  0.667981 0.416278 -0.0390259  0.148231    -0.17912    114 GLY   B N    
1463 C CA   . GLY   A 102 ? 0.533989 0.752651 0.475361 -0.0333556  0.1408      -0.184592   114 GLY   B CA   
1464 C C    . GLY   A 102 ? 0.563842 0.809279 0.475881 -0.00111001 0.13635     -0.172249   114 GLY   B C    
1465 O O    . GLY   A 102 ? 0.566896 0.773109 0.430529 0.017675    0.142241    -0.153364   114 GLY   B O    
1466 H H    . GLY   A 102 ? 0.510799 0.6408   0.421121 -0.0445349  0.154418    -0.170707   114 GLY   B H    
1467 H HA2  . GLY   A 102 ? 0.518145 0.73068  0.477679 -0.0391759  0.147437    -0.178048   114 GLY   B HA2  
1468 H HA3  . GLY   A 102 ? 0.522223 0.768957 0.48875  -0.0449402  0.131149    -0.203425   114 GLY   B HA3  
1469 N N    . SER   A 103 ? 0.555716 0.868878 0.501877 0.00456931  0.12291     -0.18324    115 SER   B N    
1470 C CA   . SER   A 103 ? 0.571578 0.915012 0.496608 0.0399701   0.116001    -0.170245   115 SER   B CA   
1471 C C    . SER   A 103 ? 0.586439 0.929668 0.461112 0.0551842   0.103316    -0.171207   115 SER   B C    
1472 O O    . SER   A 103 ? 0.653875 0.987735 0.485998 0.0869883   0.101479    -0.150534   115 SER   B O    
1473 C CB   . SER   A 103 ? 0.568613 0.988975 0.551903 0.0454698   0.107117    -0.176394   115 SER   B CB   
1474 O OG   . SER   A 103 ? 0.55905  1.04364  0.575439 0.0359694   0.0809332   -0.201376   115 SER   B OG   
1475 H H    . SER   A 103 ? 0.542301 0.881733 0.526619 -0.0130364  0.116655    -0.198347   115 SER   B H    
1476 H HA   . SER   A 103 ? 0.580081 0.885707 0.480126 0.0531555   0.127932    -0.152793   115 SER   B HA   
1477 H HB2  . SER   A 103 ? 0.58112  1.00974  0.549965 0.0731609   0.108308    -0.162766   115 SER   B HB2  
1478 H HB3  . SER   A 103 ? 0.545688 0.964601 0.560989 0.0293924   0.118695    -0.175628   115 SER   B HB3  
1480 N N    . ALA   A 104 ? 0.604217 0.952266 0.47766  0.03513     0.096434    -0.193605   116 ALA   B N    
1481 C CA   . ALA   A 104 ? 0.614506 0.966794 0.432087 0.0508416   0.088662    -0.194332   116 ALA   B CA   
1482 C C    . ALA   A 104 ? 0.630339 0.915432 0.395583 0.0551349   0.11125     -0.166346   116 ALA   B C    
1483 O O    . ALA   A 104 ? 0.683997 0.962782 0.393028 0.0756727   0.111701    -0.148867   116 ALA   B O    
1484 C CB   . ALA   A 104 ? 0.643945 1.02124  0.471687 0.0322238   0.0769478   -0.23075    116 ALA   B CB   
1485 H H    . ALA   A 104 ? 0.571378 0.919323 0.476727 0.0130812   0.0973599   -0.208396   116 ALA   B H    
1486 H HA   . ALA   A 104 ? 0.647424 1.03022  0.452452 0.073125    0.0757615   -0.188274   116 ALA   B HA   
1487 H HB1  . ALA   A 104 ? 0.629729 1.04796  0.493212 0.0270177   0.0595305   -0.249475   116 ALA   B HB1  
1488 H HB2  . ALA   A 104 ? 0.61545  0.963552 0.458266 0.0131624   0.0887802   -0.236586   116 ALA   B HB2  
1489 H HB3  . ALA   A 104 ? 0.669271 1.05045  0.45257  0.045355    0.0744251   -0.230321   116 ALA   B HB3  
1490 N N    . GLY   A 105 ? 0.595529 0.833034 0.381114 0.0330453   0.128261    -0.162713   117 GLY   B N    
1491 C CA   . GLY   A 105 ? 0.618092 0.79671  0.370015 0.0291764   0.14673     -0.140208   117 GLY   B CA   
1492 C C    . GLY   A 105 ? 0.636023 0.826476 0.367071 0.0220479   0.153708    -0.149769   117 GLY   B C    
1493 O O    . GLY   A 105 ? 0.611151 0.84121  0.361608 0.0147181   0.144257    -0.181657   117 GLY   B O    
1494 H H    . GLY   A 105 ? 0.570435 0.813114 0.39299  0.0193329   0.12737     -0.173617   117 GLY   B H    
1495 H HA2  . GLY   A 105 ? 0.594291 0.74442  0.36755  0.0145436   0.153291    -0.14011    117 GLY   B HA2  
1496 H HA3  . GLY   A 105 ? 0.644513 0.804217 0.366494 0.04658     0.14815     -0.118588   117 GLY   B HA3  
1497 N N    . SER   A 106 ? 0.64405  0.79776  0.33885  0.023215    0.171541    -0.122502   118 SER   B N    
1498 C CA   . SER   A 106 ? 0.683394 0.849459 0.357673 0.0177704   0.187251    -0.12503    118 SER   B CA   
1499 C C    . SER   A 106 ? 0.760164 0.897282 0.38036  0.0294875   0.202818    -0.0827909  118 SER   B C    
1500 O O    . SER   A 106 ? 0.761353 0.862458 0.387377 0.0126903   0.223373    -0.0609932  118 SER   B O    
1501 C CB   . SER   A 106 ? 0.642762 0.795804 0.362854 -0.00828435 0.199867    -0.139546   118 SER   B CB   
1502 O OG   . SER   A 106 ? 0.650588 0.830285 0.351538 -0.00699717 0.216944    -0.146532   118 SER   B OG   
1503 H H    . SER   A 106 ? 0.664413 0.78425  0.348338 0.0275469   0.174938    -0.101233   118 SER   B H    
1504 H HA   . SER   A 106 ? 0.693447 0.898075 0.356883 0.0262633   0.178364    -0.144627   118 SER   B HA   
1505 H HB2  . SER   A 106 ? 0.607518 0.770882 0.360216 -0.015199   0.189012    -0.16245    118 SER   B HB2  
1506 H HB3  . SER   A 106 ? 0.633739 0.750854 0.362791 -0.0173464  0.206827    -0.121022   118 SER   B HB3  
1508 N N    . LEU   A 107 ? 0.796787 0.952039 0.368474 0.0579259   0.1904      -0.0709544  119 LEU   B N    
1509 C CA   . LEU   A 107 ? 0.889874 1.00828  0.405924 0.0748241   0.199257    -0.0253274  119 LEU   B CA   
1510 C C    . LEU   A 107 ? 0.954194 1.07554  0.431464 0.0683597   0.227607    -0.00494358 119 LEU   B C    
1511 O O    . LEU   A 107 ? 1.04088  1.21168  0.508962 0.0683248   0.23362     -0.0305273  119 LEU   B O    
1512 C CB   . LEU   A 107 ? 0.92991  1.07603  0.409524 0.111311    0.173325    -0.0221254  119 LEU   B CB   
1513 C CG   . LEU   A 107 ? 0.942895 1.08046  0.462085 0.121076    0.153854    -0.0293524  119 LEU   B CG   
1514 C CD1  . LEU   A 107 ? 0.993681 1.17651  0.494971 0.158149    0.125959    -0.0309937  119 LEU   B CD1  
1515 C CD2  . LEU   A 107 ? 0.942048 1.0001   0.456178 0.119035    0.165759    0.00311258  119 LEU   B CD2  
1516 H H    . LEU   A 107 ? 0.797314 0.98851  0.372304 0.0671283   0.17416     -0.0917028  119 LEU   B H    
1517 H HA   . LEU   A 107 ? 0.880842 0.953932 0.412181 0.0670197   0.202866    -0.00993727 119 LEU   B HA   
1518 H HB2  . LEU   A 107 ? 0.936753 1.13106  0.41177  0.116204    0.163253    -0.0463049  119 LEU   B HB2  
1519 H HB3  . LEU   A 107 ? 0.995335 1.11922  0.428851 0.125881    0.178833    0.00931258  119 LEU   B HB3  
1520 H HG   . LEU   A 107 ? 0.881133 1.03583  0.445378 0.10371     0.151645    -0.0558884  119 LEU   B HG   
1521 H HD11 . LEU   A 107 ? 0.979206 1.21226  0.484428 0.157528    0.114712    -0.0547647  119 LEU   B HD11 
1522 H HD12 . LEU   A 107 ? 0.960823 1.14371  0.494024 0.16339     0.118227    -0.0363689  119 LEU   B HD12 
1523 H HD13 . LEU   A 107 ? 1.04217  1.20442  0.496941 0.178146    0.126337    -0.00284914 119 LEU   B HD13 
1524 H HD21 . LEU   A 107 ? 0.916198 0.953285 0.45793  0.09422     0.176793    -0.00340503 119 LEU   B HD21 
1525 H HD22 . LEU   A 107 ? 1.00071  1.03237  0.47368  0.127647    0.173017    0.0315581   119 LEU   B HD22 
1526 H HD23 . LEU   A 107 ? 0.942755 0.995316 0.467149 0.134578    0.154452    0.00209505  119 LEU   B HD23 
1527 N N    . PRO   A 108 ? 0.9969   1.06482  0.44855  0.0635531   0.247433    0.0425412   120 PRO   B N    
1528 C CA   . PRO   A 108 ? 0.97911  0.976738 0.437741 0.0643527   0.239292    0.0692699   120 PRO   B CA   
1529 C C    . PRO   A 108 ? 0.909595 0.863656 0.429984 0.0309796   0.244627    0.0626735   120 PRO   B C    
1530 O O    . PRO   A 108 ? 0.94162  0.832031 0.462904 0.0324982   0.235992    0.0793509   120 PRO   B O    
1531 C CB   . PRO   A 108 ? 1.0902   1.04619  0.489973 0.0712766   0.257861    0.124181    120 PRO   B CB   
1532 C CG   . PRO   A 108 ? 1.10605  1.10095  0.507299 0.0493314   0.290561    0.12607     120 PRO   B CG   
1533 C CD   . PRO   A 108 ? 1.06187  1.134    0.47243  0.0583113   0.280119    0.0740574   120 PRO   B CD   
1534 H HA   . PRO   A 108 ? 0.976938 0.979958 0.430803 0.0845038   0.21893     0.0603888   120 PRO   B HA   
1535 H HB2  . PRO   A 108 ? 1.10379  1.00269  0.513855 0.061555    0.259912    0.144758    120 PRO   B HB2  
1536 H HB3  . PRO   A 108 ? 1.12877  1.09475  0.483191 0.098861    0.247312    0.134693    120 PRO   B HB3  
1537 H HG2  . PRO   A 108 ? 1.08122  1.05703  0.525825 0.0224136   0.302772    0.127615    120 PRO   B HG2  
1538 H HG3  . PRO   A 108 ? 1.17027  1.16005  0.523931 0.0576578   0.305067    0.158117    120 PRO   B HG3  
1539 H HD2  . PRO   A 108 ? 1.03385  1.1262   0.475457 0.0397104   0.295953    0.0592389   120 PRO   B HD2  
1540 H HD3  . PRO   A 108 ? 1.10224  1.20286  0.462557 0.0798393   0.277521    0.0765517   120 PRO   B HD3  
1541 N N    . LYS   A 109 ? 0.854696 0.839024 0.423327 0.00406313  0.25646     0.0380779   121 LYS   B N    
1542 C CA   . LYS   A 109 ? 0.821537 0.76762  0.447291 -0.0265504  0.257605    0.033649    121 LYS   B CA   
1543 C C    . LYS   A 109 ? 0.745892 0.669312 0.394184 -0.0209178  0.231684    0.00969358  121 LYS   B C    
1544 O O    . LYS   A 109 ? 0.729996 0.594225 0.389267 -0.0302592  0.224281    0.0182933   121 LYS   B O    
1545 C CB   . LYS   A 109 ? 0.754921 0.741704 0.430858 -0.0517309  0.274664    0.0149419   121 LYS   B CB   
1546 H H    . LYS   A 109 ? 0.849349 0.878268 0.414469 0.00664061  0.262003    0.0226518   121 LYS   B H    
1547 H HA   . LYS   A 109 ? 0.849628 0.752087 0.466111 -0.0343661  0.264494    0.0623716   121 LYS   B HA   
1550 N N    . ILE   A 110 ? 0.730561 0.701052 0.385297 -0.00622552 0.218122    -0.0208637  122 ILE   B N    
1551 C CA   . ILE   A 110 ? 0.68248  0.642241 0.360368 -0.0017729  0.200189    -0.040368   122 ILE   B CA   
1552 C C    . ILE   A 110 ? 0.707206 0.687525 0.357388 0.0313121   0.186649    -0.0396746  122 ILE   B C    
1553 O O    . ILE   A 110 ? 0.675479 0.71505  0.322393 0.0416863   0.18082     -0.054782   122 ILE   B O    
1554 C CB   . ILE   A 110 ? 0.640845 0.640767 0.366834 -0.0179589  0.196354    -0.0753891  122 ILE   B CB   
1555 C CG1  . ILE   A 110 ? 0.638427 0.642732 0.393921 -0.0425413  0.210039    -0.0796852  122 ILE   B CG1  
1556 C CG2  . ILE   A 110 ? 0.624021 0.600636 0.372353 -0.0194944  0.184122    -0.0862194  122 ILE   B CG2  
1557 C CD1  . ILE   A 110 ? 0.636777 0.586941 0.411599 -0.0626873  0.211917    -0.0637285  122 ILE   B CD1  
1558 H H    . ILE   A 110 ? 0.723695 0.735017 0.368226 0.00056632  0.220671    -0.0296997  122 ILE   B H    
1559 H HA   . ILE   A 110 ? 0.697779 0.61131  0.379314 -0.00871919 0.198864    -0.0311831  122 ILE   B HA   
1560 H HB   . ILE   A 110 ? 0.635506 0.676602 0.357747 -0.00859391 0.192373    -0.0884352  122 ILE   B HB   
1561 H HG12 . ILE   A 110 ? 0.658057 0.681433 0.395042 -0.0390513  0.221429    -0.0718402  122 ILE   B HG12 
1562 H HG13 . ILE   A 110 ? 0.602063 0.629902 0.385059 -0.0484214  0.205981    -0.10234    122 ILE   B HG13 
1563 H HG21 . ILE   A 110 ? 0.58823  0.582708 0.366192 -0.0313008  0.182133    -0.103905   122 ILE   B HG21 
1564 H HG22 . ILE   A 110 ? 0.63401  0.566478 0.378027 -0.0250557  0.184407    -0.0749958  122 ILE   B HG22 
1565 H HG23 . ILE   A 110 ? 0.625456 0.613596 0.361972 -0.00220296 0.178024    -0.0863456  122 ILE   B HG23 
1566 H HD11 . ILE   A 110 ? 0.617967 0.551117 0.407798 -0.0657063  0.200438    -0.0740377  122 ILE   B HD11 
1567 H HD12 . ILE   A 110 ? 0.632892 0.596643 0.431485 -0.07673    0.221623    -0.0652057  122 ILE   B HD12 
1568 H HD13 . ILE   A 110 ? 0.674832 0.593497 0.424138 -0.0583417  0.214017    -0.0419928  122 ILE   B HD13 
1569 N N    . PRO   A 111 ? 0.724402 0.66255  0.360075 0.0502064   0.178624    -0.0280345  123 PRO   B N    
1570 C CA   . PRO   A 111 ? 0.751567 0.721804 0.372111 0.0853302   0.166009    -0.0284335  123 PRO   B CA   
1571 C C    . PRO   A 111 ? 0.705681 0.737284 0.372449 0.0825437   0.157744    -0.0599447  123 PRO   B C    
1572 O O    . PRO   A 111 ? 0.66889  0.701345 0.371841 0.0558444   0.161822    -0.0780357  123 PRO   B O    
1573 C CB   . PRO   A 111 ? 0.802569 0.702005 0.394233 0.108665    0.163451    -0.00697058 123 PRO   B CB   
1574 C CG   . PRO   A 111 ? 0.804303 0.632155 0.402696 0.0794483   0.17062     -0.00354183 123 PRO   B CG   
1575 C CD   . PRO   A 111 ? 0.750006 0.609803 0.382094 0.0418798   0.179574    -0.0159993  123 PRO   B CD   
1576 H HA   . PRO   A 111 ? 0.775523 0.769253 0.373212 0.0959155   0.164592    -0.0201599  123 PRO   B HA   
1577 H HB2  . PRO   A 111 ? 0.791231 0.705624 0.393778 0.125245    0.157644    -0.0170995  123 PRO   B HB2  
1578 H HB3  . PRO   A 111 ? 0.848893 0.734022 0.408052 0.125569    0.16223     0.0137454   123 PRO   B HB3  
1579 H HG2  . PRO   A 111 ? 0.79232  0.603546 0.399998 0.0826633   0.166825    -0.0151498  123 PRO   B HG2  
1580 H HG3  . PRO   A 111 ? 0.85242  0.630906 0.425084 0.0825475   0.172388    0.0178642   123 PRO   B HG3  
1581 H HD2  . PRO   A 111 ? 0.717943 0.576003 0.375815 0.0286978   0.1774      -0.0322236  123 PRO   B HD2  
1582 H HD3  . PRO   A 111 ? 0.775917 0.607861 0.400744 0.0280839   0.187041    -0.00017412 123 PRO   B HD3  
1583 N N    . SER   A 112 ? 0.727941 0.810704 0.396564 0.110149    0.145117    -0.0637173  124 SER   B N    
1584 C CA   . SER   A 112 ? 0.692839 0.834098 0.413063 0.107551    0.138506    -0.0876982  124 SER   B CA   
1585 C C    . SER   A 112 ? 0.69954  0.802383 0.43591  0.103517    0.149291    -0.0878602  124 SER   B C    
1586 O O    . SER   A 112 ? 0.712521 0.757753 0.415943 0.12323     0.153599    -0.0715163  124 SER   B O    
1587 C CB   . SER   A 112 ? 0.719801 0.921823 0.443896 0.140488    0.122253    -0.0872677  124 SER   B CB   
1588 O OG   . SER   A 112 ? 0.855297 1.02217  0.55435  0.176041    0.124132    -0.0661128  124 SER   B OG   
1589 H H    . SER   A 112 ? 0.763348 0.846144 0.402996 0.130687    0.140253    -0.0494639  124 SER   B H    
1590 H HA   . SER   A 112 ? 0.668239 0.835159 0.411031 0.0859086   0.137312    -0.104544   124 SER   B HA   
1591 H HB2  . SER   A 112 ? 0.707291 0.956809 0.473815 0.133449    0.117844    -0.103729   124 SER   B HB2  
1592 H HB3  . SER   A 112 ? 0.757941 0.977512 0.460373 0.145669    0.113754    -0.0855869  124 SER   B HB3  
1594 N N    . ASN   A 113 ? 0.635091 0.764773 0.417049 0.0781329   0.152762    -0.106626   125 ASN   B N    
1595 C CA   . ASN   A 113 ? 0.629968 0.742262 0.426832 0.0764164   0.163397    -0.107607   125 ASN   B CA   
1596 C C    . ASN   A 113 ? 0.64449  0.668835 0.402561 0.0709145   0.16938     -0.0981196  125 ASN   B C    
1597 O O    . ASN   A 113 ? 0.597007 0.585568 0.333463 0.0891533   0.175072    -0.0934092  125 ASN   B O    
1598 C CB   . ASN   A 113 ? 0.669351 0.821816 0.475605 0.111275    0.165582    -0.103023   125 ASN   B CB   
1599 C CG   . ASN   A 113 ? 0.622794 0.870552 0.47828  0.114734    0.154211    -0.113369   125 ASN   B CG   
1600 O OD1  . ASN   A 113 ? 0.609322 0.892963 0.461107 0.148406    0.144588    -0.107178   125 ASN   B OD1  
1601 N ND2  . ASN   A 113 ? 0.569207 0.859214 0.475632 0.0813361   0.152438    -0.129666   125 ASN   B ND2  
1602 H H    . ASN   A 113 ? 0.620146 0.778423 0.421843 0.061767    0.148524    -0.11891    125 ASN   B H    
1603 H HA   . ASN   A 113 ? 0.601353 0.73682  0.430964 0.0550812   0.164629    -0.118678   125 ASN   B HA   
1604 H HB2  . ASN   A 113 ? 0.692763 0.815261 0.465122 0.135315    0.163772    -0.0920196  125 ASN   B HB2  
1605 H HB3  . ASN   A 113 ? 0.653511 0.798443 0.467449 0.110082    0.176147    -0.103845   125 ASN   B HB3  
1606 H HD21 . ASN   A 113 ? 0.563976 0.909349 0.508128 0.0813555   0.147617    -0.135983   125 ASN   B HD21 
1607 H HD22 . ASN   A 113 ? 0.560678 0.823003 0.466294 0.0589748   0.155395    -0.134155   125 ASN   B HD22 
1608 N N    . ALA   A 114 ? 0.639208 0.631507 0.390051 0.0469045   0.167333    -0.0972714  126 ALA   B N    
1609 C CA   . ALA   A 114 ? 0.684352 0.599294 0.408967 0.0375495   0.168       -0.0891068  126 ALA   B CA   
1610 C C    . ALA   A 114 ? 0.651994 0.549536 0.394985 0.0159161   0.168133    -0.100195   126 ALA   B C    
1611 O O    . ALA   A 114 ? 0.531562 0.464943 0.311592 -0.00486933 0.168388    -0.1114     126 ALA   B O    
1612 C CB   . ALA   A 114 ? 0.683508 0.580392 0.400319 0.0218734   0.168213    -0.0792038  126 ALA   B CB   
1613 H H    . ALA   A 114 ? 0.627487 0.648788 0.392232 0.036298    0.165035    -0.103066   126 ALA   B H    
1614 H HA   . ALA   A 114 ? 0.70993  0.593665 0.407702 0.0580017   0.167689    -0.0815377  126 ALA   B HA   
1615 H HB1  . ALA   A 114 ? 0.710811 0.613573 0.408249 0.037394    0.168381    -0.068549   126 ALA   B HB1  
1616 H HB2  . ALA   A 114 ? 0.658267 0.586343 0.399352 0.00570729  0.169528    -0.0886601  126 ALA   B HB2  
1617 H HB3  . ALA   A 114 ? 0.70541  0.554198 0.412612 0.0130571   0.167041    -0.0736306  126 ALA   B HB3  
1618 N N    . THR   A 115 ? 0.632054 0.468856 0.343624 0.0237956   0.165623    -0.0975071  127 THR   B N    
1619 C CA   . THR   A 115 ? 0.639211 0.441564 0.352127 0.00485056  0.159729    -0.104339   127 THR   B CA   
1620 C C    . THR   A 115 ? 0.662378 0.423671 0.380262 -0.0184028  0.148838    -0.10152    127 THR   B C    
1621 O O    . THR   A 115 ? 0.686425 0.411253 0.384531 -0.0142508  0.146257    -0.091423   127 THR   B O    
1622 C CB   . THR   A 115 ? 0.697385 0.457676 0.366508 0.0282198   0.160293    -0.106389   127 THR   B CB   
1623 O OG1  . THR   A 115 ? 0.659112 0.477569 0.341537 0.0442795   0.175831    -0.10684    127 THR   B OG1  
1624 C CG2  . THR   A 115 ? 0.729025 0.449471 0.384781 0.0138329   0.150194    -0.113002   127 THR   B CG2  
1625 H H    . THR   A 115 ? 0.680146 0.494503 0.365693 0.043809    0.165749    -0.0921148  127 THR   B H    
1626 H HA   . THR   A 115 ? 0.609962 0.446261 0.349983 -0.00661114 0.162512    -0.109497   127 THR   B HA   
1627 H HB   . THR   A 115 ? 0.732684 0.457588 0.374127 0.0437418   0.157302    -0.103271   127 THR   B HB   
1629 H HG21 . THR   A 115 ? 0.761753 0.455    0.381376 0.0319483   0.151237    -0.115795   127 THR   B HG21 
1630 H HG22 . THR   A 115 ? 0.692912 0.445514 0.373182 0.00226946  0.154291    -0.113622   127 THR   B HG22 
1631 H HG23 . THR   A 115 ? 0.730944 0.420765 0.38922  -0.00093298 0.137807    -0.113694   127 THR   B HG23 
1632 N N    . LEU   A 116 ? 0.666064 0.433642 0.415258 -0.0430855  0.142489    -0.108459   128 LEU   B N    
1633 C CA   . LEU   A 116 ? 0.645937 0.391254 0.416026 -0.0661404  0.133354    -0.106183   128 LEU   B CA   
1634 C C    . LEU   A 116 ? 0.6534   0.357976 0.420808 -0.0764635  0.114041    -0.113391   128 LEU   B C    
1635 O O    . LEU   A 116 ? 0.610382 0.320745 0.370756 -0.071243   0.111968    -0.119202   128 LEU   B O    
1636 C CB   . LEU   A 116 ? 0.626693 0.424735 0.445671 -0.0835214  0.140993    -0.109751   128 LEU   B CB   
1637 C CG   . LEU   A 116 ? 0.629024 0.48248  0.452935 -0.074159   0.156187    -0.11068    128 LEU   B CG   
1638 C CD1  . LEU   A 116 ? 0.620757 0.509786 0.482949 -0.0903069  0.163272    -0.116153   128 LEU   B CD1  
1639 C CD2  . LEU   A 116 ? 0.669422 0.514409 0.45648  -0.0556993  0.162267    -0.0964352  128 LEU   B CD2  
1640 H H    . LEU   A 116 ? 0.633019 0.420724 0.394129 -0.0452981  0.144075    -0.11367    128 LEU   B H    
1641 H HA   . LEU   A 116 ? 0.681508 0.400872 0.435382 -0.0632492  0.133239    -0.0977034  128 LEU   B HA   
1642 H HB2  . LEU   A 116 ? 0.606661 0.413606 0.444893 -0.0901746  0.135984    -0.117998   128 LEU   B HB2  
1643 H HB3  . LEU   A 116 ? 0.635365 0.421971 0.467242 -0.0957817  0.139112    -0.10471    128 LEU   B HB3  
1644 H HG   . LEU   A 116 ? 0.611024 0.486079 0.440482 -0.0692026  0.156502    -0.118775   128 LEU   B HG   
1645 H HD11 . LEU   A 116 ? 0.598149 0.491286 0.486105 -0.099001   0.157845    -0.125938   128 LEU   B HD11 
1646 H HD12 . LEU   A 116 ? 0.608435 0.53144  0.468852 -0.0835955  0.170593    -0.12029    128 LEU   B HD12 
1647 H HD13 . LEU   A 116 ? 0.633845 0.507551 0.496162 -0.0973597  0.165819    -0.105823   128 LEU   B HD13 
1648 H HD21 . LEU   A 116 ? 0.674776 0.512755 0.443241 -0.0405713  0.160391    -0.0969684  128 LEU   B HD21 
1649 H HD22 . LEU   A 116 ? 0.693769 0.50393  0.471052 -0.0607539  0.160641    -0.0859498  128 LEU   B HD22 
1650 H HD23 . LEU   A 116 ? 0.658181 0.538961 0.44907  -0.0525052  0.169252    -0.0966211  128 LEU   B HD23 
1651 N N    . PHE   A 117 ? 0.676761 0.343995 0.453311 -0.0930389  0.0993452   -0.111107   129 PHE   B N    
1652 C CA   . PHE   A 117 ? 0.706796 0.340322 0.488801 -0.105829   0.0734641   -0.11954    129 PHE   B CA   
1653 C C    . PHE   A 117 ? 0.675125 0.339155 0.523847 -0.132637   0.0694384   -0.117493   129 PHE   B C    
1654 O O    . PHE   A 117 ? 0.681089 0.355654 0.552372 -0.14422    0.081442    -0.106574   129 PHE   B O    
1655 C CB   . PHE   A 117 ? 0.788088 0.346717 0.523141 -0.100522   0.0532599   -0.123625   129 PHE   B CB   
1656 C CG   . PHE   A 117 ? 0.835154 0.357819 0.576846 -0.116378   0.0184822   -0.134999   129 PHE   B CG   
1657 C CD1  . PHE   A 117 ? 0.852666 0.354012 0.552114 -0.10229    0.00182388  -0.146289   129 PHE   B CD1  
1658 C CD2  . PHE   A 117 ? 0.88321  0.396818 0.67412  -0.14553    0.00174718  -0.132831   129 PHE   B CD2  
1659 C CE1  . PHE   A 117 ? 0.896613 0.367316 0.597102 -0.113907   -0.0354932  -0.157498   129 PHE   B CE1  
1660 C CE2  . PHE   A 117 ? 0.921202 0.409466 0.726071 -0.16047    -0.0359151  -0.145244   129 PHE   B CE2  
1661 C CZ   . PHE   A 117 ? 0.935125 0.401351 0.692138 -0.143214   -0.057112   -0.158766   129 PHE   B CZ   
1662 H H    . PHE   A 117 ? 0.689441 0.353184 0.47044  -0.0972203  0.104659    -0.103022   129 PHE   B H    
1663 H HA   . PHE   A 117 ? 0.695314 0.337835 0.46985  -0.0993363  0.0714307   -0.124588   129 PHE   B HA   
1664 H HB2  . PHE   A 117 ? 0.807764 0.351883 0.500268 -0.0794328  0.0579024   -0.126932   129 PHE   B HB2  
1665 H HB3  . PHE   A 117 ? 0.804421 0.34956  0.543775 -0.105591   0.0575937   -0.115889   129 PHE   B HB3  
1666 H HD1  . PHE   A 117 ? 0.85184  0.362937 0.522027 -0.0844938  0.0160306   -0.145205   129 PHE   B HD1  
1667 H HD2  . PHE   A 117 ? 0.863782 0.392224 0.681067 -0.155701   0.0159314   -0.121876   129 PHE   B HD2  
1668 H HE1  . PHE   A 117 ? 0.926636 0.382447 0.590631 -0.102013   -0.0464722  -0.163373   129 PHE   B HE1  
1669 H HE2  . PHE   A 117 ? 0.922635 0.411627 0.770345 -0.182431   -0.0471771  -0.143315   129 PHE   B HE2  
1670 H HZ   . PHE   A 117 ? 0.957223 0.405683 0.718909 -0.151338   -0.0862284  -0.167786   129 PHE   B HZ   
1671 N N    . PHE   A 118 ? 0.660274 0.335092 0.538013 -0.140512   0.0521457   -0.125792   130 PHE   B N    
1672 C CA   . PHE   A 118 ? 0.670918 0.376612 0.618424 -0.161915   0.0442928   -0.126329   130 PHE   B CA   
1673 C C    . PHE   A 118 ? 0.7102   0.386347 0.666434 -0.169555   0.00606217  -0.134584   130 PHE   B C    
1674 O O    . PHE   A 118 ? 0.715113 0.365644 0.629116 -0.155001   -0.00956371 -0.140349   130 PHE   B O    
1675 C CB   . PHE   A 118 ? 0.595847 0.361646 0.591634 -0.160312   0.0586422   -0.130945   130 PHE   B CB   
1676 C CG   . PHE   A 118 ? 0.568102 0.373711 0.563438 -0.154269   0.0918146   -0.127763   130 PHE   B CG   
1677 C CD1  . PHE   A 118 ? 0.578565 0.385875 0.532374 -0.137429   0.103736    -0.129616   130 PHE   B CD1  
1678 C CD2  . PHE   A 118 ? 0.584398 0.429885 0.62053  -0.164876   0.110596    -0.122594   130 PHE   B CD2  
1679 C CE1  . PHE   A 118 ? 0.552108 0.397814 0.503965 -0.1309     0.127107    -0.129554   130 PHE   B CE1  
1680 C CE2  . PHE   A 118 ? 0.571347 0.451746 0.594764 -0.155845   0.13778     -0.121175   130 PHE   B CE2  
1681 C CZ   . PHE   A 118 ? 0.586746 0.465935 0.567552 -0.138797   0.142687    -0.126156   130 PHE   B CZ   
1682 H H    . PHE   A 118 ? 0.672828 0.336971 0.526775 -0.130695   0.0454873   -0.130105   130 PHE   B H    
1683 H HA   . PHE   A 118 ? 0.669693 0.377488 0.633301 -0.172973   0.051838    -0.118915   130 PHE   B HA   
1684 H HB2  . PHE   A 118 ? 0.598012 0.357131 0.578724 -0.151031   0.051581    -0.135493   130 PHE   B HB2  
1685 H HB3  . PHE   A 118 ? 0.595033 0.379516 0.637715 -0.171503   0.0514213   -0.13231    130 PHE   B HB3  
1686 H HD1  . PHE   A 118 ? 0.58243  0.367215 0.509805 -0.130241   0.0952292   -0.130892   130 PHE   B HD1  
1687 H HD2  . PHE   A 118 ? 0.583144 0.434749 0.65576  -0.177799   0.104628    -0.120055   130 PHE   B HD2  
1688 H HE1  . PHE   A 118 ? 0.557751 0.409356 0.48824  -0.12066    0.132327    -0.1317     130 PHE   B HE1  
1689 H HE2  . PHE   A 118 ? 0.575597 0.483664 0.620075 -0.161256   0.152801    -0.116569   130 PHE   B HE2  
1690 H HZ   . PHE   A 118 ? 0.565693 0.470237 0.537578 -0.132325   0.157227    -0.126728   130 PHE   B HZ   
1691 N N    . GLU   A 119 ? 0.694195 0.380965 0.709155 -0.192817   -0.00805723 -0.133427   131 GLU   B N    
1692 C CA   . GLU   A 119 ? 0.743624 0.433568 0.798222 -0.201246   -0.0449216  -0.142195   131 GLU   B CA   
1693 C C    . GLU   A 119 ? 0.721054 0.483978 0.857934 -0.205015   -0.030794   -0.141132   131 GLU   B C    
1694 O O    . GLU   A 119 ? 0.742333 0.546988 0.927216 -0.218121   -0.0040568  -0.133342   131 GLU   B O    
1695 C CB   . GLU   A 119 ? 0.808328 0.465137 0.883632 -0.225855   -0.0750188  -0.144529   131 GLU   B CB   
1696 C CG   . GLU   A 119 ? 0.852704 0.517367 0.972895 -0.234633   -0.121208   -0.155695   131 GLU   B CG   
1697 C CD   . GLU   A 119 ? 0.953277 0.580967 1.09457  -0.262507   -0.156844   -0.161912   131 GLU   B CD   
1698 O OE1  . GLU   A 119 ? 1.00144  0.558183 1.07527  -0.257125   -0.193568   -0.177026   131 GLU   B OE1  
1699 O OE2  . GLU   A 119 ? 0.907278 0.580558 1.13682  -0.29094    -0.144914   -0.151377   131 GLU   B OE2  
1700 H H    . GLU   A 119 ? 0.70866  0.402942 0.741369 -0.203759   0.00516813  -0.125693   131 GLU   B H    
1701 H HA   . GLU   A 119 ? 0.758545 0.425191 0.772752 -0.186918   -0.0592816  -0.147578   131 GLU   B HA   
1702 H HB2  . GLU   A 119 ? 0.849269 0.454561 0.86727  -0.220153   -0.0824342  -0.147836   131 GLU   B HB2  
1703 H HB3  . GLU   A 119 ? 0.799382 0.479655 0.916112 -0.241831   -0.0576637  -0.135255   131 GLU   B HB3  
1704 H HG2  . GLU   A 119 ? 0.819669 0.537455 1.00294  -0.23887    -0.113593   -0.152613   131 GLU   B HG2  
1705 H HG3  . GLU   A 119 ? 0.871024 0.512531 0.945295 -0.217218   -0.137437   -0.162278   131 GLU   B HG3  
1706 N N    . ILE   A 120 ? 0.73771  0.513054 0.887105 -0.191187   -0.0473438  -0.14786    132 ILE   B N    
1707 C CA   . ILE   A 120 ? 0.633741 0.471578 0.859033 -0.187806   -0.0360515  -0.15089    132 ILE   B CA   
1708 C C    . ILE   A 120 ? 0.657228 0.507317 0.937709 -0.189077   -0.0776083  -0.156194   132 ILE   B C    
1709 O O    . ILE   A 120 ? 0.647168 0.455348 0.885603 -0.178704   -0.112615   -0.158122   132 ILE   B O    
1710 C CB   . ILE   A 120 ? 0.628718 0.473253 0.829102 -0.166727   -0.0140165  -0.154013   132 ILE   B CB   
1711 C CG1  . ILE   A 120 ? 0.588752 0.428009 0.73779  -0.164254   0.0212153   -0.150435   132 ILE   B CG1  
1712 C CG2  . ILE   A 120 ? 0.575801 0.477843 0.853247 -0.159472   -0.00302131 -0.16246    132 ILE   B CG2  
1713 C CD1  . ILE   A 120 ? 0.603459 0.4405   0.72372  -0.148076   0.0349089   -0.154507   132 ILE   B CD1  
1714 H H    . ILE   A 120 ? 0.738668 0.480543 0.846117 -0.181816   -0.0657489  -0.150261   132 ILE   B H    
1715 H HA   . ILE   A 120 ? 0.635624 0.505968 0.896947 -0.198297   -0.0154977  -0.147734   132 ILE   B HA   
1716 H HB   . ILE   A 120 ? 0.633902 0.447305 0.801146 -0.157659   -0.0320834  -0.153433   132 ILE   B HB   
1717 H HG12 . ILE   A 120 ? 0.585738 0.457318 0.7631   -0.170392   0.0409094   -0.149805   132 ILE   B HG12 
1718 H HG13 . ILE   A 120 ? 0.623997 0.429417 0.730957 -0.16717    0.0151191   -0.14571    132 ILE   B HG13 
1719 H HG21 . ILE   A 120 ? 0.571414 0.472224 0.833158 -0.148097   0.00967607  -0.166565   132 ILE   B HG21 
1720 H HG22 . ILE   A 120 ? 0.56911  0.506204 0.880254 -0.16783    0.0156756   -0.162266   132 ILE   B HG22 
1721 H HG23 . ILE   A 120 ? 0.593053 0.497785 0.901683 -0.156654   -0.0276574  -0.164228   132 ILE   B HG23 
1722 H HD11 . ILE   A 120 ? 0.612648 0.420491 0.708369 -0.142494   0.0179522   -0.151883   132 ILE   B HD11 
1723 H HD12 . ILE   A 120 ? 0.589512 0.424371 0.677812 -0.146736   0.0521473   -0.152333   132 ILE   B HD12 
1724 H HD13 . ILE   A 120 ? 0.575996 0.442713 0.735022 -0.144486   0.0428609   -0.16175    132 ILE   B HD13 
1725 N N    . GLU   A 121 ? 0.644242 0.557829 1.02046  -0.200227   -0.0724438  -0.157364   133 GLU   B N    
1726 C CA   . GLU   A 121 ? 0.647831 0.595313 1.0973   -0.194622   -0.106593   -0.163373   133 GLU   B CA   
1727 C C    . GLU   A 121 ? 0.626244 0.622951 1.12478  -0.171294   -0.0839347  -0.169558   133 GLU   B C    
1728 O O    . GLU   A 121 ? 0.58948  0.641185 1.13533  -0.17405    -0.0443098  -0.171258   133 GLU   B O    
1729 C CB   . GLU   A 121 ? 0.647078 0.638969 1.18377  -0.223301   -0.118644   -0.161356   133 GLU   B CB   
1730 C CG   . GLU   A 121 ? 0.657518 0.698836 1.28505  -0.215955   -0.156407   -0.168278   133 GLU   B CG   
1731 C CD   . GLU   A 121 ? 0.655878 0.727631 1.36289  -0.24783    -0.188365   -0.16796    133 GLU   B CD   
1732 O OE1  . GLU   A 121 ? 0.680393 0.725763 1.3711   -0.27893    -0.182242   -0.161759   133 GLU   B OE1  
1733 O OE2  . GLU   A 121 ? 0.638062 0.757841 1.42547  -0.240086   -0.222343   -0.17403    133 GLU   B OE2  
1734 H H    . GLU   A 121 ? 0.627243 0.566352 1.02438  -0.210335   -0.0461004  -0.153225   133 GLU   B H    
1735 H HA   . GLU   A 121 ? 0.67687  0.585305 1.08804  -0.186663   -0.138508   -0.164861   133 GLU   B HA   
1736 H HB2  . GLU   A 121 ? 0.679898 0.631871 1.18358  -0.238309   -0.136796   -0.159937   133 GLU   B HB2  
1737 H HB3  . GLU   A 121 ? 0.627963 0.656796 1.19599  -0.231752   -0.0834964  -0.156397   133 GLU   B HB3  
1738 H HG2  . GLU   A 121 ? 0.62232  0.712754 1.29905  -0.204339   -0.132786   -0.169973   133 GLU   B HG2  
1739 H HG3  . GLU   A 121 ? 0.670271 0.676561 1.25826  -0.199201   -0.185196   -0.171682   133 GLU   B HG3  
1740 N N    . LEU   A 122 ? 0.661188 0.633739 1.14437  -0.14688    -0.109406   -0.172636   134 LEU   B N    
1741 C CA   . LEU   A 122 ? 0.657495 0.664568 1.19175  -0.121664   -0.0973698  -0.181147   134 LEU   B CA   
1742 C C    . LEU   A 122 ? 0.679336 0.751797 1.32365  -0.116277   -0.119438   -0.186505   134 LEU   B C    
1743 O O    . LEU   A 122 ? 0.731712 0.791059 1.39046  -0.106883   -0.168129   -0.184027   134 LEU   B O    
1744 C CB   . LEU   A 122 ? 0.682296 0.628911 1.15638  -0.098927   -0.114181   -0.177482   134 LEU   B CB   
1745 C CG   . LEU   A 122 ? 0.660315 0.623204 1.18037  -0.0713557  -0.105127   -0.187479   134 LEU   B CG   
1746 C CD1  . LEU   A 122 ? 0.624164 0.629127 1.16718  -0.0714764  -0.054359   -0.203305   134 LEU   B CD1  
1747 C CD2  . LEU   A 122 ? 0.683579 0.576141 1.14087  -0.0554493  -0.118708   -0.177822   134 LEU   B CD2  
1748 H H    . LEU   A 122 ? 0.686418 0.616096 1.12299  -0.144691   -0.135077   -0.168978   134 LEU   B H    
1749 H HA   . LEU   A 122 ? 0.633004 0.662498 1.17174  -0.122384   -0.0613977  -0.185801   134 LEU   B HA   
1750 H HB2  . LEU   A 122 ? 0.676023 0.590113 1.08849  -0.104199   -0.0976798  -0.173682   134 LEU   B HB2  
1751 H HB3  . LEU   A 122 ? 0.708775 0.631535 1.16898  -0.0966466  -0.14941    -0.17115    134 LEU   B HB3  
1752 H HG   . LEU   A 122 ? 0.668456 0.662488 1.24939  -0.0619349  -0.124615   -0.190463   134 LEU   B HG   
1753 H HD11 . LEU   A 122 ? 0.60911  0.665072 1.20385  -0.0770983  -0.0444495  -0.207453   134 LEU   B HD11 
1754 H HD12 . LEU   A 122 ? 0.630115 0.631264 1.18788  -0.053166   -0.0498953  -0.212452   134 LEU   B HD12 
1755 H HD13 . LEU   A 122 ? 0.615272 0.599763 1.10559  -0.0832442  -0.0369233  -0.200206   134 LEU   B HD13 
1756 H HD21 . LEU   A 122 ? 0.71715  0.583323 1.15274  -0.0528758  -0.150235   -0.166559   134 LEU   B HD21 
1757 H HD22 . LEU   A 122 ? 0.679613 0.547985 1.08487  -0.0647232  -0.0988857  -0.175061   134 LEU   B HD22 
1758 H HD23 . LEU   A 122 ? 0.691049 0.588908 1.1821   -0.0381945  -0.115713   -0.18509    134 LEU   B HD23 
1759 N N    . LEU   A 123 ? 0.63915  0.786878 1.36075  -0.119581   -0.0825866  -0.193242   135 LEU   B N    
1760 C CA   . LEU   A 123 ? 0.614631 0.842725 1.45556  -0.116872   -0.0948942  -0.197303   135 LEU   B CA   
1761 C C    . LEU   A 123 ? 0.626318 0.870147 1.51188  -0.0751057  -0.106713   -0.209597   135 LEU   B C    
1762 O O    . LEU   A 123 ? 0.617138 0.87346  1.55397  -0.0618524  -0.153238   -0.208726   135 LEU   B O    
1763 C CB   . LEU   A 123 ? 0.58767  0.893463 1.49023  -0.134474   -0.0432217  -0.196274   135 LEU   B CB   
1764 C CG   . LEU   A 123 ? 0.592495 0.880009 1.45532  -0.174906   -0.0259184  -0.180309   135 LEU   B CG   
1765 C CD1  . LEU   A 123 ? 0.576144 0.938025 1.48839  -0.185773   0.0334431   -0.17456    135 LEU   B CD1  
1766 C CD2  . LEU   A 123 ? 0.603665 0.882353 1.49927  -0.205679   -0.0732574  -0.171516   135 LEU   B CD2  
1767 H H    . LEU   A 123 ? 0.619476 0.772076 1.31922  -0.122586   -0.0479832  -0.194954   135 LEU   B H    
1768 H HA   . LEU   A 123 ? 0.63756  0.858445 1.49044  -0.130055   -0.130857   -0.191857   135 LEU   B HA   
1769 H HB2  . LEU   A 123 ? 0.577124 0.892435 1.46678  -0.117559   -0.0106014  -0.204707   135 LEU   B HB2  
1770 H HB3  . LEU   A 123 ? 0.588286 0.953758 1.57744  -0.133562   -0.0506945  -0.197769   135 LEU   B HB3  
1771 H HG   . LEU   A 123 ? 0.591255 0.82097  1.36993  -0.173574   -0.0216023  -0.179043   135 LEU   B HG   
1772 H HD11 . LEU   A 123 ? 0.565735 0.931497 1.45143  -0.165159   0.0612381   -0.183565   135 LEU   B HD11 
1773 H HD12 . LEU   A 123 ? 0.582235 0.925015 1.4646   -0.210266   0.0440516   -0.161572   135 LEU   B HD12 
1774 H HD13 . LEU   A 123 ? 0.574482 0.999173 1.57404  -0.187982   0.0329621   -0.174479   135 LEU   B HD13 
1775 H HD21 . LEU   A 123 ? 0.624997 0.86432  1.49258  -0.19496    -0.112394   -0.175992   135 LEU   B HD21 
1776 H HD22 . LEU   A 123 ? 0.604575 0.947382 1.58979  -0.21302    -0.0733639  -0.170641   135 LEU   B HD22 
1777 H HD23 . LEU   A 123 ? 0.615987 0.864033 1.47121  -0.228242   -0.065078   -0.162647   135 LEU   B HD23 
1778 N N    . ASP   A 124 ? 0.610764 0.850263 1.47521  -0.0530127  -0.0674966  -0.222388   136 ASP   B N    
1779 C CA   . ASP   A 124 ? 0.632258 0.878603 1.53841  -0.0111553  -0.0731878  -0.237691   136 ASP   B CA   
1780 C C    . ASP   A 124 ? 0.630011 0.82524  1.46555  0.00258898  -0.042028   -0.250608   136 ASP   B C    
1781 O O    . ASP   A 124 ? 0.603618 0.788342 1.38057  -0.0180219  -0.00883353 -0.250347   136 ASP   B O    
1782 C CB   . ASP   A 124 ? 0.642055 0.993162 1.66945  0.00544368  -0.052493   -0.251091   136 ASP   B CB   
1783 C CG   . ASP   A 124 ? 0.692018 1.06004  1.78958  0.0524346   -0.0760748  -0.264752   136 ASP   B CG   
1784 O OD1  . ASP   A 124 ? 0.714622 1.10333  1.87167  0.0596208   -0.123968   -0.256026   136 ASP   B OD1  
1785 O OD2  . ASP   A 124 ? 0.775995 1.13308  1.86743  0.0838169   -0.0498127  -0.285644   136 ASP   B OD2  
1786 H H    . ASP   A 124 ? 0.599786 0.829363 1.42192  -0.0636989  -0.0380056  -0.222721   136 ASP   B H    
1787 H HA   . ASP   A 124 ? 0.657901 0.87193  1.55898  -0.00141527 -0.112586   -0.230886   136 ASP   B HA   
1788 H HB2  . ASP   A 124 ? 0.634392 1.02582  1.70581  -0.0146755  -0.0625355  -0.241539   136 ASP   B HB2  
1789 H HB3  . ASP   A 124 ? 0.628427 1.00419  1.65085  0.00553386  -0.0104765  -0.260414   136 ASP   B HB3  
1790 N N    . PHE   A 125 ? 0.658481 0.820627 1.50342  0.0375474   -0.056184   -0.261952   137 PHE   B N    
1791 C CA   . PHE   A 125 ? 0.692946 0.813721 1.49393  0.0521743   -0.029465   -0.281039   137 PHE   B CA   
1792 C C    . PHE   A 125 ? 0.728985 0.848306 1.58993  0.0974696   -0.0396862  -0.301363   137 PHE   B C    
1793 O O    . PHE   A 125 ? 0.7919   0.888172 1.68139  0.116261    -0.0821154  -0.288994   137 PHE   B O    
1794 C CB   . PHE   A 125 ? 0.724278 0.752214 1.4255   0.0350976   -0.0414402  -0.26584    137 PHE   B CB   
1795 C CG   . PHE   A 125 ? 0.779144 0.739944 1.45718  0.0435394   -0.0895768  -0.242477   137 PHE   B CG   
1796 C CD1  . PHE   A 125 ? 0.742984 0.694487 1.39552  0.0263879   -0.121332   -0.217555   137 PHE   B CD1  
1797 C CD2  . PHE   A 125 ? 0.810947 0.71207  1.4869   0.0696642   -0.104064   -0.245141   137 PHE   B CD2  
1798 C CE1  . PHE   A 125 ? 0.798129 0.688484 1.4171   0.0377447   -0.16455    -0.195288   137 PHE   B CE1  
1799 C CE2  . PHE   A 125 ? 0.841869 0.679074 1.48963  0.078792    -0.146095   -0.217749   137 PHE   B CE2  
1800 C CZ   . PHE   A 125 ? 0.854327 0.688817 1.46979  0.0639502   -0.175443   -0.192419   137 PHE   B CZ   
1801 H H    . PHE   A 125 ? 0.68342  0.846227 1.56403  0.0525812   -0.0858881  -0.257829   137 PHE   B H    
1802 H HA   . PHE   A 125 ? 0.669983 0.827303 1.47002  0.0450624   0.00519659  -0.292267   137 PHE   B HA   
1803 H HB2  . PHE   A 125 ? 0.731189 0.738548 1.414    0.0423582   -0.0240382  -0.280893   137 PHE   B HB2  
1804 H HB3  . PHE   A 125 ? 0.700562 0.732233 1.36509  0.0103534   -0.0319868  -0.25599    137 PHE   B HB3  
1805 H HD1  . PHE   A 125 ? 0.72737  0.711462 1.38185  0.00751622  -0.113947   -0.215902   137 PHE   B HD1  
1806 H HD2  . PHE   A 125 ? 0.815054 0.716649 1.5071   0.0820361   -0.0854995  -0.265561   137 PHE   B HD2  
1807 H HE1  . PHE   A 125 ? 0.808112 0.691846 1.40369  0.0278821   -0.187317   -0.18145    137 PHE   B HE1  
1808 H HE2  . PHE   A 125 ? 0.886926 0.679196 1.53368  0.0956573   -0.154846   -0.216633   137 PHE   B HE2  
1809 H HZ   . PHE   A 125 ? 0.890823 0.682021 1.47923  0.07205     -0.203931   -0.173207   137 PHE   B HZ   
1810 N N    . LYS   A 126 ? 0.71213  0.851505 1.58511  0.117466    -0.00221389 -0.333689   138 LYS   B N    
1811 C CA   . LYS   A 126 ? 0.739067 0.877933 1.66889  0.165396    -0.00475616 -0.361468   138 LYS   B CA   
1812 C C    . LYS   A 126 ? 0.752437 0.813799 1.62095  0.172701    0.00673547  -0.385503   138 LYS   B C    
1813 O O    . LYS   A 126 ? 0.713807 0.757267 1.5139   0.143972    0.0283882   -0.38803    138 LYS   B O    
1814 C CB   . LYS   A 126 ? 0.694936 0.946142 1.71391  0.188709    0.0292724   -0.383737   138 LYS   B CB   
1815 H H    . LYS   A 126 ? 0.695159 0.846916 1.53608  0.102336    0.0253928   -0.339989   138 LYS   B H    
1816 H HA   . LYS   A 126 ? 0.754977 0.868128 1.70641  0.178393    -0.0394371  -0.348326   138 LYS   B HA   
1819 N N    . GLY   A 127 ? 0.817684 0.829793 1.71452  0.211651    -0.0117873  -0.403332   139 GLY   B N    
1820 C CA   . GLY   A 127 ? 0.874601 0.809168 1.7268   0.218962    -0.0054275  -0.430888   139 GLY   B CA   
1821 C C    . GLY   A 127 ? 0.888514 0.87596  1.7439   0.235079    0.0393536   -0.478851   139 GLY   B C    
1822 O O    . GLY   A 127 ? 0.858514 0.934856 1.77379  0.261231    0.0632916   -0.495196   139 GLY   B O    
1823 H H    . GLY   A 127 ? 0.833901 0.859601 1.7813   0.234282    -0.0306574  -0.398721   139 GLY   B H    
1824 H HA2  . GLY   A 127 ? 0.864915 0.7557   1.66058  0.188556    -0.00995371 -0.414766   139 GLY   B HA2  
1825 H HA3  . GLY   A 127 ? 0.921904 0.809617 1.79666  0.244419    -0.027569   -0.434188   139 GLY   B HA3  
1826 N N    . GLU   A 128 ? 0.922193 0.859615 1.71202  0.218592    0.0507456   -0.500367   140 GLU   B N    
1827 C CA   . GLU   A 128 ? 0.976894 0.927792 1.76247  0.247385    0.0787352   -0.556241   140 GLU   B CA   
1828 C C    . GLU   A 128 ? 1.03994  0.958503 1.88807  0.30306     0.0631367   -0.585971   140 GLU   B C    
1829 O O    . GLU   A 128 ? 1.05616  0.921443 1.93493  0.310166    0.0253352   -0.556993   140 GLU   B O    
1830 C CB   . GLU   A 128 ? 0.98733  0.878578 1.69579  0.218192    0.0798111   -0.573635   140 GLU   B CB   
1831 O OXT  . GLU   A 128 ? 1.08472  1.03278  1.94663  0.341663    0.0890624   -0.636768   140 GLU   B OXT  
1832 H H    . GLU   A 128 ? 0.909488 0.805855 1.65661  0.189761    0.040155    -0.481214   140 GLU   B H    
1833 H HA   . GLU   A 128 ? 0.94471  0.972279 1.73994  0.251158    0.107678    -0.562445   140 GLU   B HA   
1836 N N    . THR   B 5   ? 1.29054  1.08202  1.02427  0.247033    -0.111684   0.109085    17  THR   A N    
1837 C CA   . THR   B 5   ? 1.28611  1.0684   1.02289  0.204805    -0.0816009  0.082929    17  THR   A CA   
1838 C C    . THR   B 5   ? 1.32296  1.04124  1.06177  0.199759    -0.0451335  0.0849938   17  THR   A C    
1839 O O    . THR   B 5   ? 1.29776  0.98281  1.04689  0.230017    -0.0430395  0.100856    17  THR   A O    
1840 C CB   . THR   B 5   ? 1.1747   1.02799  0.97417  0.188541    -0.0923702  0.050702    17  THR   A CB   
1841 O OG1  . THR   B 5   ? 1.17156  1.03999  1.03202  0.202991    -0.0873611  0.0456283   17  THR   A OG1  
1842 C CG2  . THR   B 5   ? 1.13443  1.04944  0.940941 0.193645    -0.130533   0.0447078   17  THR   A CG2  
1843 H H    . THR   B 5   ? 1.30764  1.13127  1.02887  0.247443    -0.132791   0.108936    17  THR   A H    
1844 H HA   . THR   B 5   ? 1.29614  1.06636  0.988861 0.189737    -0.0782304  0.0853542   17  THR   A HA   
1845 H HB   . THR   B 5   ? 1.15043  0.998629 0.944795 0.163385    -0.07634    0.0358939   17  THR   A HB   
1847 H HG21 . THR   B 5   ? 1.09271  1.04209  0.935548 0.179021    -0.13378    0.0244581   17  THR   A HG21 
1848 H HG22 . THR   B 5   ? 1.16504  1.096    0.984625 0.218189    -0.148417   0.0572909   17  THR   A HG22 
1849 H HG23 . THR   B 5   ? 1.17058  1.07551  0.931656 0.186434    -0.133845   0.0477512   17  THR   A HG23 
1850 N N    . VAL   B 6   ? 1.36979  1.07377  1.09947  0.161869    -0.017386   0.0663154   18  VAL   A N    
1851 C CA   . VAL   B 6   ? 1.3535   0.99879  1.07601  0.145111    0.0185028   0.0626032   18  VAL   A CA   
1852 C C    . VAL   B 6   ? 1.27186  0.958942 1.04746  0.122545    0.0300239   0.0294831   18  VAL   A C    
1853 O O    . VAL   B 6   ? 1.31844  1.06361  1.11625  0.109596    0.0169455   0.0124148   18  VAL   A O    
1854 C CB   . VAL   B 6   ? 1.42624  1.01843  1.08304  0.116035    0.0424702   0.0729401   18  VAL   A CB   
1855 C CG1  . VAL   B 6   ? 1.45044  0.982072 1.04466  0.136696    0.0374066   0.112047    18  VAL   A CG1  
1856 C CG2  . VAL   B 6   ? 1.40794  1.05044  1.0541   0.0865599   0.0414081   0.0550227   18  VAL   A CG2  
1857 H H    . VAL   B 6   ? 1.30916  1.04451  1.0379   0.145389    -0.0221632  0.053621    18  VAL   A H    
1858 H HA   . VAL   B 6   ? 1.39813  1.0119   1.12519  0.167134    0.0202621   0.0742844   18  VAL   A HA   
1859 H HB   . VAL   B 6   ? 1.4174   0.978567 1.0781   0.100876    0.0653208   0.0650881   18  VAL   A HB   
1860 H HG11 . VAL   B 6   ? 1.47247  1.03638  1.06017  0.152424    0.013352    0.119949    18  VAL   A HG11 
1861 H HG12 . VAL   B 6   ? 1.50804  1.00068  1.1083   0.156966    0.0401617   0.123101    18  VAL   A HG12 
1862 H HG13 . VAL   B 6   ? 1.50835  1.00829  1.06204  0.11382     0.0555079   0.118114    18  VAL   A HG13 
1863 H HG21 . VAL   B 6   ? 1.43678  1.0507   1.04388  0.0683921   0.0583932   0.0617381   18  VAL   A HG21 
1864 H HG22 . VAL   B 6   ? 1.34227  1.01477  1.02375  0.0734152   0.046331    0.0329523   18  VAL   A HG22 
1865 H HG23 . VAL   B 6   ? 1.39406  1.06756  1.03665  0.0993549   0.0190767   0.0584506   18  VAL   A HG23 
1866 N N    . THR   B 7   ? 1.18691  0.839702 0.978257 0.118098    0.0545167   0.0205707   19  THR   A N    
1867 C CA   . THR   B 7   ? 1.10438  0.793555 0.938649 0.0975934   0.0664146   -0.00824476 19  THR   A CA   
1868 C C    . THR   B 7   ? 1.00843  0.720651 0.828968 0.0601405   0.0745142   -0.0238656  19  THR   A C    
1869 O O    . THR   B 7   ? 0.994105 0.762581 0.844798 0.0513091   0.0633359   -0.039524   19  THR   A O    
1870 C CB   . THR   B 7   ? 1.08808  0.728065 0.927476 0.0968858   0.0937263   -0.0167985  19  THR   A CB   
1871 O OG1  . THR   B 7   ? 1.12709  0.727644 0.96852  0.135814    0.0907918   -7.806e-05  19  THR   A OG1  
1872 C CG2  . THR   B 7   ? 0.972849 0.659264 0.857001 0.0827599   0.101791    -0.044425   19  THR   A CG2  
1873 H H    . THR   B 7   ? 1.25794  0.860847 1.0298   0.128403    0.0639713   0.0329323   19  THR   A H    
1874 H HA   . THR   B 7   ? 1.04876  0.782297 0.91802  0.109086    0.0509318   -0.0129652  19  THR   A HA   
1875 H HB   . THR   B 7   ? 1.11335  0.714898 0.921516 0.0763927   0.110548    -0.0171143  19  THR   A HB   
1877 H HG21 . THR   B 7   ? 1.01289  0.669712 0.899447 0.0856517   0.117881    -0.051302   19  THR   A HG21 
1878 H HG22 . THR   B 7   ? 0.952612 0.682905 0.867696 0.0961897   0.0861229   -0.044737   19  THR   A HG22 
1879 H HG23 . THR   B 7   ? 0.960922 0.663337 0.839199 0.0572142   0.106632    -0.0549522  19  THR   A HG23 
1880 N N    . GLU   B 8   ? 1.05574  0.723964 0.831529 0.0379817   0.0950487   -0.0192778  20  GLU   A N    
1881 C CA   . GLU   B 8   ? 1.0232   0.719086 0.787846 0.00478245  0.104825    -0.034206   20  GLU   A CA   
1882 C C    . GLU   B 8   ? 0.975866 0.700166 0.717384 0.00982937  0.0865295   -0.0261263  20  GLU   A C    
1883 O O    . GLU   B 8   ? 1.06551  0.774384 0.764273 -0.00726324 0.09924     -0.0196972  20  GLU   A O    
1884 C CB   . GLU   B 8   ? 1.08915  0.732817 0.819033 -0.0251781  0.136543    -0.0342641  20  GLU   A CB   
1885 H H    . GLU   B 8   ? 1.10873  0.728369 0.860916 0.044077    0.10374     -0.00601201 20  GLU   A H    
1886 H HA   . GLU   B 8   ? 0.967781 0.700503 0.763787 -0.00218949 0.103006    -0.051373   20  GLU   A HA   
1889 N N    . GLN   B 9   ? 0.90665  0.672748 0.674343 0.0311199   0.0579883   -0.0277168  21  GLN   A N    
1890 C CA   . GLN   B 9   ? 1.00329  0.805076 0.755834 0.032693    0.0392944   -0.0309702  21  GLN   A CA   
1891 C C    . GLN   B 9   ? 0.926121 0.78023  0.716342 0.0212892   0.0327961   -0.0576745  21  GLN   A C    
1892 O O    . GLN   B 9   ? 0.792079 0.660316 0.623637 0.0176818   0.0354368   -0.0682233  21  GLN   A O    
1893 C CB   . GLN   B 9   ? 1.044    0.858655 0.803538 0.0619862   0.00818576  -0.0182982  21  GLN   A CB   
1894 C CG   . GLN   B 9   ? 0.96841  0.81862  0.789919 0.0714037   -0.00608678 -0.0295319  21  GLN   A CG   
1895 C CD   . GLN   B 9   ? 1.04811  0.927651 0.884751 0.0945477   -0.0386634  -0.0220931  21  GLN   A CD   
1896 O OE1  . GLN   B 9   ? 1.05106  0.929004 0.849552 0.104328    -0.0548342  -0.0110434  21  GLN   A OE1  
1897 N NE2  . GLN   B 9   ? 0.984741 0.895556 0.87625  0.101251    -0.047553   -0.0285426  21  GLN   A NE2  
1898 H H    . GLN   B 9   ? 0.921087 0.694722 0.717432 0.0436793   0.0505829   -0.0286915  21  GLN   A H    
1899 H HA   . GLN   B 9   ? 1.01948  0.805621 0.734375 0.0230265   0.04965     -0.0250884  21  GLN   A HA   
1900 H HB2  . GLN   B 9   ? 1.0359   0.869762 0.779059 0.0620564   -0.0041788  -0.0214434  21  GLN   A HB2  
1901 H HB3  . GLN   B 9   ? 1.07892  0.861219 0.817734 0.0745365   0.00941118  0.00051446  21  GLN   A HB3  
1902 H HG2  . GLN   B 9   ? 0.990677 0.82305  0.826032 0.0742276   0.00597326  -0.0265506  21  GLN   A HG2  
1903 H HG3  . GLN   B 9   ? 0.947715 0.822135 0.787268 0.058286    -0.00547402 -0.0457531  21  GLN   A HG3  
1904 H HE21 . GLN   B 9   ? 0.99376  0.926584 0.90044  0.113773    -0.0659102  -0.0247501  21  GLN   A HE21 
1905 H HE22 . GLN   B 9   ? 0.965199 0.877703 0.877815 0.0922599   -0.0349353  -0.0367004  21  GLN   A HE22 
1906 N N    . GLY   B 10  ? 0.828455 0.70873  0.601766 0.0184497   0.0233889   -0.0677435  22  GLY   A N    
1907 C CA   . GLY   B 10  ? 0.748507 0.66802  0.55109  0.0109848   0.0184686   -0.0919473  22  GLY   A CA   
1908 C C    . GLY   B 10  ? 0.678195 0.611296 0.464941 -0.00787487 0.04093     -0.105559   22  GLY   A C    
1909 O O    . GLY   B 10  ? 0.702129 0.615231 0.458648 -0.0222752  0.063898    -0.0972352  22  GLY   A O    
1910 H H    . GLY   B 10  ? 0.877227 0.748807 0.618326 0.0226862   0.0200599   -0.0592582  22  GLY   A H    
1911 H HA2  . GLY   B 10  ? 0.736074 0.669629 0.538386 0.0197213   0.00035394  -0.0968121  22  GLY   A HA2  
1912 H HA3  . GLY   B 10  ? 0.707773 0.63366  0.542675 0.010218    0.017479    -0.0954965  22  GLY   A HA3  
1913 N N    . GLU   B 11  ? 0.654788 0.623286 0.461622 -0.0068088  0.0331842   -0.126886   23  GLU   A N    
1914 C CA   . GLU   B 11  ? 0.626991 0.624206 0.427953 -0.0186256  0.0508754   -0.143958   23  GLU   A CA   
1915 C C    . GLU   B 11  ? 0.594992 0.606313 0.426621 -0.0341492  0.0664517   -0.149666   23  GLU   A C    
1916 O O    . GLU   B 11  ? 0.554257 0.569693 0.419741 -0.0293844  0.0554093   -0.151119   23  GLU   A O    
1917 C CB   . GLU   B 11  ? 0.690502 0.714235 0.501174 -0.00360486 0.0328063   -0.164904   23  GLU   A CB   
1918 C CG   . GLU   B 11  ? 0.740514 0.8044   0.57309  -0.00613834 0.0437203   -0.186839   23  GLU   A CG   
1919 C CD   . GLU   B 11  ? 0.815588 0.897163 0.655428 0.0129879   0.0282549   -0.209789   23  GLU   A CD   
1920 O OE1  . GLU   B 11  ? 0.918278 0.979914 0.767722 0.0255782   0.00349551  -0.211296   23  GLU   A OE1  
1921 O OE2  . GLU   B 11  ? 0.744581 0.861215 0.582683 0.0139877   0.0428164   -0.227748   23  GLU   A OE2  
1922 H H    . GLU   B 11  ? 0.629117 0.60468  0.455784 0.00227323  0.0162863   -0.131165   23  GLU   A H    
1923 H HA   . GLU   B 11  ? 0.678148 0.667393 0.446701 -0.025918   0.0638392   -0.13804    23  GLU   A HA   
1924 H HB2  . GLU   B 11  ? 0.715506 0.736346 0.49702  0.00048576  0.0303478   -0.165513   23  GLU   A HB2  
1925 H HB3  . GLU   B 11  ? 0.667536 0.685146 0.498914 0.00492063  0.0152994   -0.164287   23  GLU   A HB3  
1926 H HG2  . GLU   B 11  ? 0.709898 0.778433 0.569338 -0.00944253 0.0435389   -0.185621   23  GLU   A HG2  
1927 H HG3  . GLU   B 11  ? 0.754504 0.830284 0.570539 -0.0176181  0.0627617   -0.188004   23  GLU   A HG3  
1928 N N    . ASP   B 12  ? 0.578635 0.598595 0.395659 -0.0557389  0.0925578   -0.152383   24  ASP   A N    
1929 C CA   . ASP   B 12  ? 0.600355 0.644003 0.444071 -0.0741518  0.106493    -0.162583   24  ASP   A CA   
1930 C C    . ASP   B 12  ? 0.597218 0.698457 0.4717   -0.0654147  0.0986985   -0.18431    24  ASP   A C    
1931 O O    . ASP   B 12  ? 0.536369 0.670224 0.402059 -0.0663509  0.108054    -0.196688   24  ASP   A O    
1932 C CB   . ASP   B 12  ? 0.620345 0.656051 0.439236 -0.104585   0.1367      -0.160106   24  ASP   A CB   
1933 C CG   . ASP   B 12  ? 0.61176  0.675986 0.457448 -0.129059   0.15058     -0.174112   24  ASP   A CG   
1934 O OD1  . ASP   B 12  ? 0.589507 0.682753 0.470491 -0.118731   0.13532     -0.183981   24  ASP   A OD1  
1935 O OD2  . ASP   B 12  ? 0.596438 0.650582 0.424318 -0.160221   0.17611     -0.173883   24  ASP   A OD2  
1936 H H    . ASP   B 12  ? 0.628961 0.641488 0.417051 -0.0608843  0.101942    -0.147816   24  ASP   A H    
1937 H HA   . ASP   B 12  ? 0.578612 0.606788 0.436706 -0.0722587  0.100744    -0.157519   24  ASP   A HA   
1938 H HB2  . ASP   B 12  ? 0.655437 0.646666 0.452012 -0.106823   0.140765    -0.14449    24  ASP   A HB2  
1939 H HB3  . ASP   B 12  ? 0.642722 0.697913 0.446997 -0.107853   0.144322    -0.164731   24  ASP   A HB3  
1940 N N    . ILE   B 13  ? 0.513848 0.626441 0.422564 -0.0548623  0.0819483   -0.187668   25  ILE   A N    
1941 C CA   . ILE   B 13  ? 0.52411  0.681141 0.460992 -0.0395203  0.0700494   -0.203886   25  ILE   A CA   
1942 C C    . ILE   B 13  ? 0.473257 0.676199 0.43554  -0.0537022  0.0787018   -0.213525   25  ILE   A C    
1943 O O    . ILE   B 13  ? 0.480274 0.720926 0.469109 -0.0377527  0.0660615   -0.223472   25  ILE   A O    
1944 C CB   . ILE   B 13  ? 0.533979 0.670879 0.486798 -0.0164795  0.0427342   -0.199137   25  ILE   A CB   
1945 C CG1  . ILE   B 13  ? 0.509168 0.62562  0.474823 -0.0230249  0.0370906   -0.184597   25  ILE   A CG1  
1946 C CG2  . ILE   B 13  ? 0.605839 0.711503 0.536406 -0.00329814 0.0312547   -0.196971   25  ILE   A CG2  
1947 C CD1  . ILE   B 13  ? 0.503213 0.607665 0.487805 -0.00619656 0.0130553   -0.179398   25  ILE   A CD1  
1948 H H    . ILE   B 13  ? 0.524965 0.616478 0.438216 -0.0565085  0.0785251   -0.178979   25  ILE   A H    
1949 H HA   . ILE   B 13  ? 0.529499 0.702206 0.457465 -0.0347463  0.074301    -0.21289    25  ILE   A HA   
1950 H HB   . ILE   B 13  ? 0.528191 0.689499 0.497963 -0.00556713 0.0357614   -0.208747   25  ILE   A HB   
1951 H HG12 . ILE   B 13  ? 0.520867 0.611248 0.472554 -0.0291381  0.0422545   -0.175438   25  ILE   A HG12 
1952 H HG13 . ILE   B 13  ? 0.503295 0.640635 0.477834 -0.0334091  0.0450223   -0.187773   25  ILE   A HG13 
1953 H HG21 . ILE   B 13  ? 0.583745 0.680998 0.526757 0.00907736  0.0144934   -0.198131   25  ILE   A HG21 
1954 H HG22 . ILE   B 13  ? 0.598514 0.679725 0.515025 -0.00987088 0.0337994   -0.184925   25  ILE   A HG22 
1955 H HG23 . ILE   B 13  ? 0.606591 0.726367 0.523907 -0.00103988 0.0380653   -0.207019   25  ILE   A HG23 
1956 H HD11 . ILE   B 13  ? 0.499762 0.62275  0.495025 0.00374977  0.00659794  -0.187526   25  ILE   A HD11 
1957 H HD12 . ILE   B 13  ? 0.490487 0.590802 0.483641 -0.0122014  0.0124588   -0.171079   25  ILE   A HD12 
1958 H HD13 . ILE   B 13  ? 0.510832 0.593327 0.487769 0.00014224  0.00485146  -0.176413   25  ILE   A HD13 
1959 N N    . THR   B 14  ? 0.519993 0.720619 0.473065 -0.0829045  0.0992984   -0.211985   26  THR   A N    
1960 C CA   . THR   B 14  ? 0.546187 0.799592 0.521862 -0.101851   0.107811    -0.225782   26  THR   A CA   
1961 C C    . THR   B 14  ? 0.580999 0.89634  0.566317 -0.107863   0.121113    -0.243609   26  THR   A C    
1962 O O    . THR   B 14  ? 0.575735 0.881622 0.53767  -0.111911   0.135389    -0.243285   26  THR   A O    
1963 C CB   . THR   B 14  ? 0.527293 0.755199 0.489816 -0.135371   0.126291    -0.223386   26  THR   A CB   
1964 O OG1  . THR   B 14  ? 0.539318 0.737706 0.471567 -0.157755   0.150406    -0.219454   26  THR   A OG1  
1965 C CG2  . THR   B 14  ? 0.533699 0.70712  0.489194 -0.127622   0.116978    -0.208898   26  THR   A CG2  
1966 H H    . THR   B 14  ? 0.537216 0.702319 0.469211 -0.0916259  0.107654    -0.202744   26  THR   A H    
1967 H HA   . THR   B 14  ? 0.515563 0.785281 0.510427 -0.088688   0.0923147   -0.226716   26  THR   A HA   
1968 H HB   . THR   B 14  ? 0.522704 0.790991 0.501871 -0.148106   0.128633    -0.234945   26  THR   A HB   
1970 H HG21 . THR   B 14  ? 0.547712 0.702832 0.494121 -0.147195   0.129946    -0.210293   26  THR   A HG21 
1971 H HG22 . THR   B 14  ? 0.537109 0.676467 0.479746 -0.114623   0.112763    -0.197844   26  THR   A HG22 
1972 H HG23 . THR   B 14  ? 0.507942 0.700252 0.480731 -0.116149   0.102572    -0.209771   26  THR   A HG23 
1973 N N    . SER   B 15  ? 0.575456 0.9597   0.594352 -0.111091   0.118048    -0.259026   27  SER   A N    
1974 C CA   . SER   B 15  ? 0.592934 1.0532   0.631656 -0.117408   0.131449    -0.278898   27  SER   A CA   
1975 C C    . SER   B 15  ? 0.603238 1.07073  0.626586 -0.165166   0.163463    -0.283593   27  SER   A C    
1976 O O    . SER   B 15  ? 0.537145 1.04396  0.559035 -0.176953   0.183982    -0.293745   27  SER   A O    
1977 C CB   . SER   B 15  ? 0.645362 1.18008  0.727577 -0.10076    0.11377     -0.292012   27  SER   A CB   
1978 O OG   . SER   B 15  ? 0.676369 1.20681  0.769603 -0.0543527  0.0913141   -0.290806   27  SER   A OG   
1979 H H    . SER   B 15  ? 0.56168  0.949428 0.591898 -0.109014   0.107097    -0.257083   27  SER   A H    
1980 H HA   . SER   B 15  ? 0.607205 1.06438  0.639153 -0.0996354  0.131258    -0.280493   27  SER   A HA   
1981 H HB2  . SER   B 15  ? 0.625643 1.1522   0.710245 -0.108478   0.105752    -0.287009   27  SER   A HB2  
1982 H HB3  . SER   B 15  ? 0.639164 1.233    0.738738 -0.113614   0.125495    -0.306535   27  SER   A HB3  
1984 N N    . LYS   B 16  ? 0.532261 0.95724  0.541748 -0.192865   0.169098    -0.276452   28  LYS   A N    
1985 C CA   . LYS   B 16  ? 0.615119 1.03142  0.608444 -0.242482   0.19856     -0.280921   28  LYS   A CA   
1986 C C    . LYS   B 16  ? 0.609406 0.942076 0.55338  -0.251489   0.216657    -0.260549   28  LYS   A C    
1987 O O    . LYS   B 16  ? 0.663167 0.973673 0.585463 -0.292299   0.243662    -0.259517   28  LYS   A O    
1988 C CB   . LYS   B 16  ? 0.631698 1.03019  0.628989 -0.262548   0.193926    -0.284943   28  LYS   A CB   
1989 C CG   . LYS   B 16  ? 0.754742 1.17176  0.753375 -0.316626   0.216398    -0.302177   28  LYS   A CG   
1990 H H    . LYS   B 16  ? 0.54773  0.9453   0.55695  -0.180981   0.154793    -0.269113   28  LYS   A H    
1991 H HA   . LYS   B 16  ? 0.603131 1.08154  0.614981 -0.25645    0.208805    -0.295252   28  LYS   A HA   
1992 H HB2  . LYS   B 16  ? 0.614927 1.05141  0.635751 -0.24361    0.174786    -0.290027   28  LYS   A HB2  
1993 H HB3  . LYS   B 16  ? 0.653849 0.986013 0.628397 -0.255212   0.191813    -0.270876   28  LYS   A HB3  
1996 N N    . LYS   B 17  ? 0.601972 0.883214 0.526963 -0.215446   0.200086    -0.243078   29  LYS   A N    
1997 C CA   . LYS   B 17  ? 0.68374  0.887628 0.560781 -0.216132   0.210086    -0.220628   29  LYS   A CA   
1998 C C    . LYS   B 17  ? 0.708037 0.838883 0.559495 -0.244125   0.225301    -0.208748   29  LYS   A C    
1999 O O    . LYS   B 17  ? 0.687721 0.776255 0.502787 -0.270269   0.249125    -0.197324   29  LYS   A O    
2000 C CB   . LYS   B 17  ? 0.72819  0.958846 0.583749 -0.22788    0.231013    -0.222016   29  LYS   A CB   
2001 C CG   . LYS   B 17  ? 0.733394 1.02316  0.607908 -0.193969   0.217002    -0.235557   29  LYS   A CG   
2002 C CD   . LYS   B 17  ? 0.749057 0.994948 0.613455 -0.152006   0.188068    -0.224423   29  LYS   A CD   
2003 C CE   . LYS   B 17  ? 0.837329 1.12686  0.705777 -0.125043   0.181605    -0.239508   29  LYS   A CE   
2004 N NZ   . LYS   B 17  ? 0.863488 1.1191   0.731955 -0.0881167  0.151194    -0.23534    29  LYS   A NZ   
2005 H H    . LYS   B 17  ? 0.580184 0.875259 0.522411 -0.189527   0.180682    -0.244631   29  LYS   A H    
2006 H HA   . LYS   B 17  ? 0.658621 0.839663 0.532569 -0.187707   0.192016    -0.212038   29  LYS   A HA   
2007 H HB2  . LYS   B 17  ? 0.747954 1.00937  0.610915 -0.257835   0.249545    -0.231656   29  LYS   A HB2  
2008 H HB3  . LYS   B 17  ? 0.768415 0.945695 0.587195 -0.229656   0.237289    -0.204559   29  LYS   A HB3  
2009 H HG2  . LYS   B 17  ? 0.701956 1.0453   0.61292  -0.190405   0.21096     -0.251557   29  LYS   A HG2  
2010 H HG3  . LYS   B 17  ? 0.759732 1.06765  0.617574 -0.203694   0.233636    -0.237624   29  LYS   A HG3  
2011 H HD2  . LYS   B 17  ? 0.787753 0.980124 0.619502 -0.154649   0.190416    -0.207174   29  LYS   A HD2  
2012 H HD3  . LYS   B 17  ? 0.728375 0.971453 0.615774 -0.140393   0.171492    -0.225451   29  LYS   A HD3  
2013 H HE2  . LYS   B 17  ? 0.804694 1.15025  0.704642 -0.122977   0.182932    -0.25653    29  LYS   A HE2  
2014 H HE3  . LYS   B 17  ? 0.858114 1.14502  0.697236 -0.134698   0.19718     -0.236538   29  LYS   A HE3  
2015 H HZ1  . LYS   B 17  ? 0.820105 1.0844   0.716308 -0.0784033  0.137753    -0.23905    29  LYS   A HZ1  
2016 H HZ2  . LYS   B 17  ? 0.861736 1.07064  0.707051 -0.0894911  0.147636    -0.219629   29  LYS   A HZ2  
2017 H HZ3  . LYS   B 17  ? 0.856791 1.12961  0.720301 -0.0737617  0.149164    -0.245121   29  LYS   A HZ3  
2018 N N    . ASP   B 18  ? 0.749466 0.860382 0.616953 -0.23667    0.211852    -0.210744   30  ASP   A N    
2019 C CA   . ASP   B 18  ? 0.785744 0.826392 0.6329   -0.257021   0.224985    -0.205026   30  ASP   A CA   
2020 C C    . ASP   B 18  ? 0.859188 0.831921 0.691187 -0.223006   0.210129    -0.183902   30  ASP   A C    
2021 O O    . ASP   B 18  ? 0.817454 0.738498 0.642718 -0.226981   0.215225    -0.182414   30  ASP   A O    
2022 C CB   . ASP   B 18  ? 0.796835 0.870236 0.671478 -0.276299   0.223946    -0.227671   30  ASP   A CB   
2023 C CG   . ASP   B 18  ? 0.693694 0.812019 0.600927 -0.245198   0.19558     -0.233105   30  ASP   A CG   
2024 O OD1  . ASP   B 18  ? 0.707861 0.807366 0.615333 -0.20852    0.176943    -0.217338   30  ASP   A OD1  
2025 O OD2  . ASP   B 18  ? 0.604455 0.784078 0.537036 -0.258577   0.191067    -0.252499   30  ASP   A OD2  
2026 H H    . ASP   B 18  ? 0.692674 0.833329 0.583268 -0.217446   0.194483    -0.216167   30  ASP   A H    
2027 H HA   . ASP   B 18  ? 0.848186 0.863262 0.672277 -0.280927   0.244757    -0.200778   30  ASP   A HA   
2028 H HB2  . ASP   B 18  ? 0.81235  0.834271 0.671588 -0.288163   0.233376    -0.22628    30  ASP   A HB2  
2029 H HB3  . ASP   B 18  ? 0.784214 0.902184 0.669266 -0.300947   0.233952    -0.241563   30  ASP   A HB3  
2030 N N    . ARG   B 19  ? 0.755183 0.732835 0.584247 -0.189712   0.191794    -0.170764   31  ARG   A N    
2031 C CA   . ARG   B 19  ? 0.740407 0.668296 0.560179 -0.15792    0.175377    -0.151428   31  ARG   A CA   
2032 C C    . ARG   B 19  ? 0.718786 0.644454 0.566051 -0.147486   0.164658    -0.157387   31  ARG   A C    
2033 O O    . ARG   B 19  ? 0.750872 0.629537 0.591979 -0.129439   0.16003     -0.144017   31  ARG   A O    
2034 C CB   . ARG   B 19  ? 0.817496 0.668973 0.593066 -0.157913   0.187271    -0.127671   31  ARG   A CB   
2035 C CG   . ARG   B 19  ? 0.945062 0.800613 0.685816 -0.16987    0.199152    -0.1189     31  ARG   A CG   
2036 C CD   . ARG   B 19  ? 1.08956  0.869568 0.777883 -0.167358   0.208145    -0.0893445  31  ARG   A CD   
2037 N NE   . ARG   B 19  ? 1.21304  0.951755 0.898815 -0.12968    0.186281    -0.070708   31  ARG   A NE   
2038 C CZ   . ARG   B 19  ? 1.30937  1.06835  0.99678  -0.0978984  0.15998     -0.0627683  31  ARG   A CZ   
2039 N NH1  . ARG   B 19  ? 1.22772  1.04094  0.91614  -0.0958595  0.151401    -0.0731659  31  ARG   A NH1  
2040 N NH2  . ARG   B 19  ? 1.38761  1.11357  1.07685  -0.0679628  0.142467    -0.0465189  31  ARG   A NH2  
2041 H H    . ARG   B 19  ? 0.755419 0.771616 0.589526 -0.187172   0.189447    -0.175693   31  ARG   A H    
2042 H HA   . ARG   B 19  ? 0.723947 0.67418  0.548852 -0.138944   0.160475    -0.149127   31  ARG   A HA   
2043 H HB2  . ARG   B 19  ? 0.864647 0.682522 0.632932 -0.174664   0.202027    -0.129173   31  ARG   A HB2  
2044 H HB3  . ARG   B 19  ? 0.830562 0.662441 0.605981 -0.132994   0.172633    -0.116104   31  ARG   A HB3  
2045 H HG2  . ARG   B 19  ? 0.908796 0.800717 0.657708 -0.153777   0.18522     -0.12208    31  ARG   A HG2  
2046 H HG3  . ARG   B 19  ? 0.943015 0.821624 0.686886 -0.196653   0.215445    -0.130808   31  ARG   A HG3  
2047 H HD2  . ARG   B 19  ? 1.11673  0.911034 0.7835   -0.169793   0.210988    -0.0839628  31  ARG   A HD2  
2048 H HD3  . ARG   B 19  ? 1.13991  0.884377 0.814712 -0.190422   0.227403    -0.0876547  31  ARG   A HD3  
2049 H HE   . ARG   B 19  ? 1.23096  0.930239 0.915443 -0.128345   0.190895    -0.0657196  31  ARG   A HE   
2050 H HH11 . ARG   B 19  ? 1.21784  1.06474  0.917586 -0.11098    0.160159    -0.088114   31  ARG   A HH11 
2051 H HH12 . ARG   B 19  ? 1.24509  1.06173  0.923333 -0.0784282  0.136516    -0.0663265  31  ARG   A HH12 
2052 H HH21 . ARG   B 19  ? 1.41147  1.09285  1.07449  -0.0629678  0.146652    -0.0289523  31  ARG   A HH21 
2053 H HH22 . ARG   B 19  ? 1.32014  1.0703   1.03755  -0.0528499  0.12659     -0.0529374  31  ARG   A HH22 
2054 N N    . GLY   B 20  ? 0.683744 0.667317 0.561817 -0.154147   0.158276    -0.175933   32  GLY   A N    
2055 C CA   . GLY   B 20  ? 0.66122  0.651348 0.560108 -0.148899   0.150403    -0.182282   32  GLY   A CA   
2056 C C    . GLY   B 20  ? 0.661831 0.671707 0.582818 -0.118328   0.124735    -0.173937   32  GLY   A C    
2057 O O    . GLY   B 20  ? 0.584096 0.588672 0.516865 -0.111319   0.120074    -0.17283    32  GLY   A O    
2058 H H    . GLY   B 20  ? 0.671352 0.693972 0.556624 -0.161021   0.158653    -0.184286   32  GLY   A H    
2059 H HA2  . GLY   B 20  ? 0.696935 0.644662 0.584346 -0.151529   0.159784    -0.178978   32  GLY   A HA2  
2060 H HA3  . GLY   B 20  ? 0.661724 0.685593 0.570731 -0.165324   0.15409     -0.196567   32  GLY   A HA3  
2061 N N    . VAL   B 21  ? 0.602768 0.637774 0.529323 -0.103004   0.109791    -0.170655   33  VAL   A N    
2062 C CA   . VAL   B 21  ? 0.537855 0.578865 0.480914 -0.0773669  0.0859468   -0.162214   33  VAL   A CA   
2063 C C    . VAL   B 21  ? 0.585837 0.606565 0.511103 -0.0634614  0.0793468   -0.15333    33  VAL   A C    
2064 O O    . VAL   B 21  ? 0.484401 0.524591 0.399424 -0.0665384  0.0832143   -0.160822   33  VAL   A O    
2065 C CB   . VAL   B 21  ? 0.518928 0.606286 0.486166 -0.0693646  0.0693811   -0.169632   33  VAL   A CB   
2066 C CG1  . VAL   B 21  ? 0.541019 0.618846 0.521996 -0.0484358  0.0469974   -0.158941   33  VAL   A CG1  
2067 C CG2  . VAL   B 21  ? 0.551952 0.669585 0.531082 -0.0833417  0.0734075   -0.17814    33  VAL   A CG2  
2068 H H    . VAL   B 21  ? 0.610737 0.658845 0.53016  -0.110253   0.11578     -0.175205   33  VAL   A H    
2069 H HA   . VAL   B 21  ? 0.552015 0.575791 0.499627 -0.0733512  0.0845064   -0.15621    33  VAL   A HA   
2070 H HB   . VAL   B 21  ? 0.532763 0.638706 0.498137 -0.0684276  0.0698156   -0.176396   33  VAL   A HB   
2071 H HG11 . VAL   B 21  ? 0.528334 0.591555 0.512476 -0.0493125  0.0479552   -0.152053   33  VAL   A HG11 
2072 H HG12 . VAL   B 21  ? 0.537095 0.602502 0.510801 -0.0397379  0.0415809   -0.156687   33  VAL   A HG12 
2073 H HG13 . VAL   B 21  ? 0.517534 0.616821 0.510985 -0.0435633  0.037336    -0.161658   33  VAL   A HG13 
2074 H HG21 . VAL   B 21  ? 0.524064 0.668848 0.516196 -0.0749875  0.0611241   -0.17972    33  VAL   A HG21 
2075 H HG22 . VAL   B 21  ? 0.550217 0.677408 0.522847 -0.0997389  0.0868474   -0.1874     33  VAL   A HG22 
2076 H HG23 . VAL   B 21  ? 0.538728 0.640189 0.518074 -0.0845347  0.0747909   -0.173205   33  VAL   A HG23 
2077 N N    . LEU   B 22  ? 0.594419 0.582522 0.516068 -0.0490539  0.0706249   -0.139014   34  LEU   A N    
2078 C CA   . LEU   B 22  ? 0.625186 0.595426 0.526976 -0.0349454  0.0604114   -0.129282   34  LEU   A CA   
2079 C C    . LEU   B 22  ? 0.579376 0.561822 0.502915 -0.0175008  0.0341754   -0.127833   34  LEU   A C    
2080 O O    . LEU   B 22  ? 0.542983 0.527285 0.491843 -0.013692   0.0270541   -0.123253   34  LEU   A O    
2081 C CB   . LEU   B 22  ? 0.692933 0.617935 0.571854 -0.0316487  0.0693952   -0.11294    34  LEU   A CB   
2082 C CG   . LEU   B 22  ? 0.812474 0.709518 0.663094 -0.0528154  0.0969107   -0.112311   34  LEU   A CG   
2083 C CD1  . LEU   B 22  ? 0.854833 0.694217 0.683671 -0.0438141  0.103868    -0.0934847  34  LEU   A CD1  
2084 C CD2  . LEU   B 22  ? 0.798677 0.710563 0.622546 -0.0654151  0.105749    -0.116558   34  LEU   A CD2  
2085 H H    . LEU   B 22  ? 0.590121 0.570969 0.522634 -0.0477427  0.0706996   -0.135922   34  LEU   A H    
2086 H HA   . LEU   B 22  ? 0.63197  0.612638 0.519709 -0.0392588  0.0645933   -0.134958   34  LEU   A HA   
2087 H HB2  . LEU   B 22  ? 0.69396  0.612899 0.5899   -0.0256678  0.0666804   -0.109586   34  LEU   A HB2  
2088 H HB3  . LEU   B 22  ? 0.71801  0.635829 0.582905 -0.0205586  0.0591725   -0.105237   34  LEU   A HB3  
2089 H HG   . LEU   B 22  ? 0.774822 0.682869 0.639668 -0.0654825  0.105787    -0.12269    34  LEU   A HG   
2090 H HD11 . LEU   B 22  ? 0.84573  0.680627 0.694175 -0.0372088  0.102491    -0.0946132  34  LEU   A HD11 
2091 H HD12 . LEU   B 22  ? 0.890902 0.705083 0.698023 -0.059311   0.121747    -0.092086   34  LEU   A HD12 
2092 H HD13 . LEU   B 22  ? 0.870784 0.703199 0.687303 -0.0288056  0.0918386   -0.0819316  34  LEU   A HD13 
2093 H HD21 . LEU   B 22  ? 0.777029 0.725909 0.618185 -0.0699982  0.103789    -0.130379   34  LEU   A HD21 
2094 H HD22 . LEU   B 22  ? 0.820236 0.727273 0.62872  -0.0529228  0.0954873   -0.108806   34  LEU   A HD22 
2095 H HD23 . LEU   B 22  ? 0.839788 0.730159 0.644202 -0.0815411  0.124044    -0.113647   34  LEU   A HD23 
2096 N N    . LYS   B 23  ? 0.560525 0.551789 0.472774 -0.00925016 0.0212505   -0.133654   35  LYS   A N    
2097 C CA   . LYS   B 23  ? 0.51321  0.512673 0.444726 0.00216861  -0.00345429 -0.137376   35  LYS   A CA   
2098 C C    . LYS   B 23  ? 0.54238  0.531307 0.452324 0.0128062   -0.0190365  -0.133987   35  LYS   A C    
2099 O O    . LYS   B 23  ? 0.535067 0.520629 0.409665 0.0132861   -0.0123097  -0.136466   35  LYS   A O    
2100 C CB   . LYS   B 23  ? 0.524603 0.544628 0.463745 0.0041835   -0.00769815 -0.154671   35  LYS   A CB   
2101 C CG   . LYS   B 23  ? 0.485331 0.501609 0.442457 0.0135465   -0.0321014  -0.160164   35  LYS   A CG   
2102 C CD   . LYS   B 23  ? 0.510575 0.536083 0.468399 0.023136    -0.0375678  -0.17917    35  LYS   A CD   
2103 C CE   . LYS   B 23  ? 0.54759  0.553925 0.520627 0.0291712   -0.0611927  -0.183136   35  LYS   A CE   
2104 N NZ   . LYS   B 23  ? 0.579014 0.580337 0.551494 0.0433447   -0.0696949  -0.203165   35  LYS   A NZ   
2105 H H    . LYS   B 23  ? 0.57754  0.568552 0.468438 -0.0122725  0.0289714   -0.136394   35  LYS   A H    
2106 H HA   . LYS   B 23  ? 0.507595 0.50716  0.460503 0.00178095  -0.00773014 -0.131907   35  LYS   A HA   
2107 H HB2  . LYS   B 23  ? 0.495862 0.527497 0.447168 -0.001688   0.00053925  -0.156216   35  LYS   A HB2  
2108 H HB3  . LYS   B 23  ? 0.527451 0.552121 0.446752 0.00505028  -0.00177863 -0.161711   35  LYS   A HB3  
2109 H HG2  . LYS   B 23  ? 0.511212 0.518338 0.459586 0.0168417   -0.041883   -0.158294   35  LYS   A HG2  
2110 H HG3  . LYS   B 23  ? 0.481557 0.497233 0.459177 0.0101498   -0.0353846  -0.153173   35  LYS   A HG3  
2111 H HD2  . LYS   B 23  ? 0.499829 0.539345 0.468521 0.0219267   -0.0301274  -0.180427   35  LYS   A HD2  
2112 H HD3  . LYS   B 23  ? 0.530079 0.559896 0.467272 0.0264755   -0.033018   -0.187965   35  LYS   A HD3  
2113 H HE2  . LYS   B 23  ? 0.55369  0.551385 0.518957 0.0278058   -0.0695084  -0.181826   35  LYS   A HE2  
2114 H HE3  . LYS   B 23  ? 0.528775 0.532424 0.520702 0.0241478   -0.0636118  -0.172983   35  LYS   A HE3  
2115 H HZ1  . LYS   B 23  ? 0.592324 0.596862 0.546408 0.0479577   -0.0678293  -0.214482   35  LYS   A HZ1  
2116 H HZ2  . LYS   B 23  ? 0.567036 0.580837 0.547719 0.047264    -0.0630604  -0.204338   35  LYS   A HZ2  
2117 H HZ3  . LYS   B 23  ? 0.58525  0.567905 0.567203 0.0439828   -0.0833486  -0.203679   35  LYS   A HZ3  
2118 N N    . ILE   B 24  ? 0.499526 0.489758 0.431404 0.0188358   -0.0400178  -0.130092   36  ILE   A N    
2119 C CA   . ILE   B 24  ? 0.548915 0.539732 0.468342 0.0270971   -0.062231   -0.132373   36  ILE   A CA   
2120 C C    . ILE   B 24  ? 0.538784 0.536473 0.486746 0.0243506   -0.082801   -0.144937   36  ILE   A C    
2121 O O    . ILE   B 24  ? 0.557908 0.559985 0.541016 0.0179575   -0.0843708  -0.139377   36  ILE   A O    
2122 C CB   . ILE   B 24  ? 0.588987 0.577715 0.508908 0.0357936   -0.0699912  -0.114012   36  ILE   A CB   
2123 C CG1  . ILE   B 24  ? 0.61976  0.586643 0.512963 0.0388771   -0.0482488  -0.0980122  36  ILE   A CG1  
2124 C CG2  . ILE   B 24  ? 0.611725 0.609714 0.514516 0.0434772   -0.0966646  -0.118316   36  ILE   A CG2  
2125 C CD1  . ILE   B 24  ? 0.673861 0.635723 0.579458 0.0532379   -0.0538551  -0.0790839  36  ILE   A CD1  
2126 H H    . ILE   B 24  ? 0.494783 0.488827 0.450858 0.0159413   -0.0402578  -0.126513   36  ILE   A H    
2127 H HA   . ILE   B 24  ? 0.568936 0.557594 0.459952 0.0289033   -0.0594645  -0.138549   36  ILE   A HA   
2128 H HB   . ILE   B 24  ? 0.564304 0.561235 0.515602 0.0342634   -0.0730951  -0.110573   36  ILE   A HB   
2129 H HG12 . ILE   B 24  ? 0.65344  0.612726 0.512747 0.0398757   -0.0460706  -0.0977573  36  ILE   A HG12 
2130 H HG13 . ILE   B 24  ? 0.610058 0.572762 0.510177 0.0305062   -0.0316018  -0.100553   36  ILE   A HG13 
2131 H HG21 . ILE   B 24  ? 0.627735 0.628086 0.52939  0.0518899   -0.102831   -0.10544    36  ILE   A HG21 
2132 H HG22 . ILE   B 24  ? 0.635525 0.627912 0.505885 0.0440577   -0.0937221  -0.124503   36  ILE   A HG22 
2133 H HG23 . ILE   B 24  ? 0.603376 0.611497 0.527977 0.0390585   -0.110495   -0.128326   36  ILE   A HG23 
2134 H HD11 . ILE   B 24  ? 0.635644 0.61201  0.576278 0.0522386   -0.0571334  -0.0809641  36  ILE   A HD11 
2135 H HD12 . ILE   B 24  ? 0.678931 0.618483 0.569368 0.0544285   -0.0375677  -0.0699632  36  ILE   A HD12 
2136 H HD13 . ILE   B 24  ? 0.683291 0.650681 0.576761 0.0626204   -0.0703266  -0.0746141  36  ILE   A HD13 
2137 N N    . VAL   B 25  ? 0.544637 0.539776 0.473658 0.0276862   -0.0965333  -0.162752   37  VAL   A N    
2138 C CA   . VAL   B 25  ? 0.539662 0.529823 0.488465 0.0237236   -0.118534   -0.176849   37  VAL   A CA   
2139 C C    . VAL   B 25  ? 0.560741 0.56316  0.519788 0.0206359   -0.140515   -0.17138    37  VAL   A C    
2140 O O    . VAL   B 25  ? 0.603529 0.614075 0.532777 0.0279209   -0.148834   -0.171041   37  VAL   A O    
2141 C CB   . VAL   B 25  ? 0.57959  0.56016  0.499578 0.0306771   -0.122261   -0.202806   37  VAL   A CB   
2142 C CG1  . VAL   B 25  ? 0.592146 0.554419 0.527866 0.026136    -0.144409   -0.221054   37  VAL   A CG1  
2143 C CG2  . VAL   B 25  ? 0.597464 0.579961 0.512977 0.0368269   -0.100329   -0.208879   37  VAL   A CG2  
2144 H H    . VAL   B 25  ? 0.564953 0.559534 0.465626 0.0315668   -0.0910506  -0.167066   37  VAL   A H    
2145 H HA   . VAL   B 25  ? 0.527225 0.51369  0.500377 0.0187218   -0.115808   -0.173709   37  VAL   A HA   
2146 H HB   . VAL   B 25  ? 0.603064 0.589427 0.495102 0.0343228   -0.124432   -0.205051   37  VAL   A HB   
2147 H HG11 . VAL   B 25  ? 0.57879  0.53261  0.540174 0.0214597   -0.143129   -0.214834   37  VAL   A HG11 
2148 H HG12 . VAL   B 25  ? 0.606373 0.573598 0.543865 0.020416    -0.15945    -0.220885   37  VAL   A HG12 
2149 H HG13 . VAL   B 25  ? 0.618343 0.571968 0.536103 0.0331459   -0.144811   -0.239679   37  VAL   A HG13 
2150 H HG21 . VAL   B 25  ? 0.610142 0.589327 0.511618 0.0436095   -0.10263    -0.227149   37  VAL   A HG21 
2151 H HG22 . VAL   B 25  ? 0.582122 0.574534 0.484046 0.0363333   -0.0855751  -0.200017   37  VAL   A HG22 
2152 H HG23 . VAL   B 25  ? 0.569193 0.547949 0.509458 0.0343459   -0.0988062  -0.203863   37  VAL   A HG23 
2153 N N    . LYS   B 26  ? 0.552342 0.561498 0.553449 0.00926271  -0.150021   -0.165699   38  LYS   A N    
2154 C CA   . LYS   B 26  ? 0.551294 0.585577 0.573256 0.00440846  -0.171048   -0.16181    38  LYS   A CA   
2155 C C    . LYS   B 26  ? 0.584954 0.614072 0.617105 -0.0108583  -0.196235   -0.182725   38  LYS   A C    
2156 O O    . LYS   B 26  ? 0.587338 0.64177  0.625552 -0.0150924  -0.218464   -0.187495   38  LYS   A O    
2157 C CB   . LYS   B 26  ? 0.526534 0.582987 0.592844 -0.00087792 -0.162531   -0.142451   38  LYS   A CB   
2158 C CG   . LYS   B 26  ? 0.498811 0.55428  0.556067 0.0124948   -0.138316   -0.125847   38  LYS   A CG   
2159 C CD   . LYS   B 26  ? 0.530418 0.588903 0.556041 0.0310519   -0.141446   -0.117959   38  LYS   A CD   
2160 C CE   . LYS   B 26  ? 0.553126 0.646602 0.602288 0.0377672   -0.163125   -0.111482   38  LYS   A CE   
2161 N NZ   . LYS   B 26  ? 0.598095 0.686142 0.612847 0.060145    -0.16279    -0.0969106  38  LYS   A NZ   
2162 H H    . LYS   B 26  ? 0.533174 0.534638 0.550916 0.00384005  -0.143092   -0.163715   38  LYS   A H    
2163 H HA   . LYS   B 26  ? 0.570075 0.613322 0.570094 0.0145437   -0.174922   -0.158754   38  LYS   A HA   
2164 H HB2  . LYS   B 26  ? 0.51289  0.56124  0.597762 -0.0124954  -0.159036   -0.1435     38  LYS   A HB2  
2165 H HB3  . LYS   B 26  ? 0.529142 0.609824 0.613032 -0.00270148 -0.1767     -0.140809   38  LYS   A HB3  
2166 H HG2  . LYS   B 26  ? 0.495949 0.533077 0.538847 0.0117685   -0.124863   -0.128542   38  LYS   A HG2  
2167 H HG3  . LYS   B 26  ? 0.486168 0.556323 0.572025 0.00940335  -0.132557   -0.117006   38  LYS   A HG3  
2168 H HD2  . LYS   B 26  ? 0.551299 0.598156 0.545734 0.032792    -0.146034   -0.126748   38  LYS   A HD2  
2169 H HD3  . LYS   B 26  ? 0.525293 0.573846 0.543361 0.0374704   -0.123694   -0.108064   38  LYS   A HD3  
2170 H HE2  . LYS   B 26  ? 0.534923 0.645463 0.619212 0.0352159   -0.158416   -0.105304   38  LYS   A HE2  
2171 H HE3  . LYS   B 26  ? 0.566963 0.670653 0.618093 0.0302791   -0.182204   -0.122871   38  LYS   A HE3  
2172 H HZ1  . LYS   B 26  ? 0.58576  0.659826 0.598622 0.0659115   -0.14481    -0.0873016  38  LYS   A HZ1  
2173 H HZ2  . LYS   B 26  ? 0.612911 0.686949 0.592622 0.0609577   -0.165464   -0.101935   38  LYS   A HZ2  
2174 H HZ3  . LYS   B 26  ? 0.602868 0.715435 0.631878 0.0677099   -0.177999   -0.0921253  38  LYS   A HZ3  
2175 N N    . ARG   B 27  ? 0.611113 0.607583 0.648495 -0.0198026  -0.193763   -0.194133   39  ARG   A N    
2176 C CA   . ARG   B 27  ? 0.630082 0.604346 0.6684   -0.033811   -0.215231   -0.217879   39  ARG   A CA   
2177 C C    . ARG   B 27  ? 0.672555 0.603247 0.686092 -0.023058   -0.206628   -0.234559   39  ARG   A C    
2178 O O    . ARG   B 27  ? 0.674631 0.590703 0.697917 -0.0181512  -0.189777   -0.222425   39  ARG   A O    
2179 C CB   . ARG   B 27  ? 0.664304 0.638396 0.748642 -0.0609506  -0.224672   -0.211859   39  ARG   A CB   
2180 C CG   . ARG   B 27  ? 0.695552 0.642077 0.780455 -0.0813387  -0.248643   -0.238513   39  ARG   A CG   
2181 C CD   . ARG   B 27  ? 0.724606 0.660804 0.852593 -0.113688   -0.252981   -0.230033   39  ARG   A CD   
2182 N NE   . ARG   B 27  ? 0.732152 0.626716 0.863716 -0.112316   -0.234079   -0.213133   39  ARG   A NE   
2183 C CZ   . ARG   B 27  ? 0.744586 0.632385 0.907746 -0.136459   -0.227623   -0.192921   39  ARG   A CZ   
2184 N NH1  . ARG   B 27  ? 0.73456  0.665177 0.936268 -0.164086   -0.233746   -0.185977   39  ARG   A NH1  
2185 N NH2  . ARG   B 27  ? 0.761579 0.605709 0.918031 -0.132823   -0.214553   -0.178053   39  ARG   A NH2  
2186 H H    . ARG   B 27  ? 0.583351 0.569066 0.623474 -0.0168567  -0.178747   -0.186912   39  ARG   A H    
2187 H HA   . ARG   B 27  ? 0.665819 0.653422 0.688071 -0.0322784  -0.2292     -0.22887    39  ARG   A HA   
2188 H HB2  . ARG   B 27  ? 0.633732 0.643852 0.738808 -0.0650365  -0.226938   -0.200414   39  ARG   A HB2  
2189 H HB3  . ARG   B 27  ? 0.637717 0.594953 0.732097 -0.0625685  -0.211674   -0.200967   39  ARG   A HB3  
2190 H HG2  . ARG   B 27  ? 0.727844 0.637945 0.789186 -0.072694   -0.246884   -0.25279    39  ARG   A HG2  
2191 H HG3  . ARG   B 27  ? 0.718685 0.689398 0.796639 -0.0827388  -0.263603   -0.249082   39  ARG   A HG3  
2192 H HD2  . ARG   B 27  ? 0.764298 0.681214 0.891191 -0.129009   -0.269018   -0.24896    39  ARG   A HD2  
2193 H HD3  . ARG   B 27  ? 0.700217 0.678824 0.854716 -0.121578   -0.252997   -0.217038   39  ARG   A HD3  
2194 H HE   . ARG   B 27  ? 0.730027 0.604875 0.840324 -0.0943983  -0.226506   -0.215745   39  ARG   A HE   
2195 H HH11 . ARG   B 27  ? 0.754998 0.69766  0.963246 -0.175484   -0.249231   -0.200482   39  ARG   A HH11 
2196 H HH12 . ARG   B 27  ? 0.715307 0.665659 0.936921 -0.171439   -0.222221   -0.167777   39  ARG   A HH12 
2197 H HH21 . ARG   B 27  ? 0.749906 0.581579 0.886831 -0.111764   -0.207481   -0.178672   39  ARG   A HH21 
2198 H HH22 . ARG   B 27  ? 0.774574 0.604066 0.945853 -0.151694   -0.213239   -0.166827   39  ARG   A HH22 
2199 N N    . VAL   B 28  ? 0.750655 0.665687 0.731444 -0.0171492  -0.218546   -0.263745   40  VAL   A N    
2200 C CA   . VAL   B 28  ? 0.809227 0.690461 0.766227 -0.00049311 -0.209498   -0.284288   40  VAL   A CA   
2201 C C    . VAL   B 28  ? 0.833921 0.66476  0.814425 -0.0098108  -0.216808   -0.290571   40  VAL   A C    
2202 O O    . VAL   B 28  ? 0.872046 0.685158 0.867711 -0.0328074  -0.236199   -0.298683   40  VAL   A O    
2203 C CB   . VAL   B 28  ? 0.907701 0.791245 0.819206 0.00909156  -0.217997   -0.316076   40  VAL   A CB   
2204 C CG1  . VAL   B 28  ? 0.978216 0.826864 0.870013 0.0272431   -0.210773   -0.345707   40  VAL   A CG1  
2205 C CG2  . VAL   B 28  ? 0.889279 0.814773 0.769361 0.0197582   -0.206835   -0.303503   40  VAL   A CG2  
2206 H H    . VAL   B 28  ? 0.768174 0.696991 0.741532 -0.0226786  -0.232932   -0.272317   40  VAL   A H    
2207 H HA   . VAL   B 28  ? 0.782364 0.67352  0.736894 0.0108194   -0.192181   -0.272505   40  VAL   A HA   
2208 H HB   . VAL   B 28  ? 0.928445 0.809418 0.842014 -0.00439172 -0.236837   -0.326976   40  VAL   A HB   
2209 H HG11 . VAL   B 28  ? 0.943069 0.792825 0.844012 0.0381123   -0.194977   -0.334544   40  VAL   A HG11 
2210 H HG12 . VAL   B 28  ? 0.998911 0.813518 0.900789 0.0202188   -0.222778   -0.359211   40  VAL   A HG12 
2211 H HG13 . VAL   B 28  ? 0.990737 0.850941 0.85041  0.0353638   -0.209793   -0.362902   40  VAL   A HG13 
2212 H HG21 . VAL   B 28  ? 0.923612 0.851547 0.77121  0.0246523   -0.211865   -0.322735   40  VAL   A HG21 
2213 H HG22 . VAL   B 28  ? 0.872271 0.817852 0.764325 0.0119754   -0.213556   -0.28657    40  VAL   A HG22 
2214 H HG23 . VAL   B 28  ? 0.864958 0.794488 0.744511 0.0291898   -0.187768   -0.293123   40  VAL   A HG23 
2215 N N    . GLY   B 29  ? 0.837975 0.647402 0.821168 0.00735202  -0.201686   -0.285337   41  GLY   A N    
2216 C CA   . GLY   B 29  ? 0.895246 0.646838 0.890456 0.00820186  -0.207624   -0.290317   41  GLY   A CA   
2217 C C    . GLY   B 29  ? 0.998585 0.708923 0.96748  0.0236953   -0.216742   -0.331139   41  GLY   A C    
2218 O O    . GLY   B 29  ? 0.976229 0.703896 0.918548 0.0242137   -0.222797   -0.356639   41  GLY   A O    
2219 H H    . GLY   B 29  ? 0.8108   0.642813 0.78764  0.0194474   -0.187595   -0.277561   41  GLY   A H    
2220 H HA2  . GLY   B 29  ? 0.907184 0.6447   0.92049  -0.0130234  -0.216772   -0.281072   41  GLY   A HA2  
2221 H HA3  . GLY   B 29  ? 0.879086 0.631673 0.88117  0.0199761   -0.19621    -0.27614    41  GLY   A HA3  
2222 N N    . ASN   B 30  ? 1.05932  0.714107 1.03286  0.0390174   -0.217507   -0.337379   42  ASN   A N    
2223 C CA   . ASN   B 30  ? 1.13267  0.73868  1.08417  0.0582739   -0.224615   -0.378519   42  ASN   A CA   
2224 C C    . ASN   B 30  ? 1.12582  0.707492 1.08377  0.0950333   -0.214256   -0.375946   42  ASN   A C    
2225 O O    . ASN   B 30  ? 1.01245  0.605497 0.991407 0.0978427   -0.207142   -0.34092    42  ASN   A O    
2226 C CB   . ASN   B 30  ? 1.22486  0.763683 1.17927  0.0309587   -0.246401   -0.394011   42  ASN   A CB   
2227 C CG   . ASN   B 30  ? 1.31944  0.830655 1.3055   0.00595817  -0.249551   -0.354914   42  ASN   A CG   
2228 O OD1  . ASN   B 30  ? 1.39703  0.926227 1.39969  -0.0315332  -0.258018   -0.342156   42  ASN   A OD1  
2229 N ND2  . ASN   B 30  ? 1.37342  0.852932 1.36861  0.0268559   -0.241732   -0.333011   42  ASN   A ND2  
2230 H H    . ASN   B 30  ? 1.04072  0.686888 1.03059  0.0391603   -0.213404   -0.315212   42  ASN   A H    
2231 H HA   . ASN   B 30  ? 1.13152  0.766011 1.06166  0.0652857   -0.221709   -0.398622   42  ASN   A HA   
2232 H HB2  . ASN   B 30  ? 1.29701  0.789352 1.23969  0.0467066   -0.249722   -0.418457   42  ASN   A HB2  
2233 H HB3  . ASN   B 30  ? 1.24254  0.802918 1.18885  0.012896    -0.254821   -0.405794   42  ASN   A HB3  
2234 H HD21 . ASN   B 30  ? 1.32023  0.819905 1.32923  0.0212033   -0.235475   -0.304355   42  ASN   A HD21 
2235 H HD22 . ASN   B 30  ? 1.40079  0.839906 1.38758  0.0475364   -0.243312   -0.347354   42  ASN   A HD22 
2236 N N    . GLY   B 31  ? 1.21068  0.759847 1.15076  0.124243    -0.214809   -0.414506   43  GLY   A N    
2237 C CA   . GLY   B 31  ? 1.24362  0.780496 1.19264  0.166762    -0.205934   -0.416584   43  GLY   A CA   
2238 C C    . GLY   B 31  ? 1.24268  0.86786  1.18926  0.187534    -0.183969   -0.417977   43  GLY   A C    
2239 O O    . GLY   B 31  ? 1.1692   0.852964 1.11427  0.165619    -0.175292   -0.398226   43  GLY   A O    
2240 H H    . GLY   B 31  ? 1.24284  0.779762 1.16514  0.118808    -0.221246   -0.44149    43  GLY   A H    
2241 H HA2  . GLY   B 31  ? 1.316    0.808166 1.2548   0.1833      -0.21116    -0.445352   43  GLY   A HA2  
2242 H HA3  . GLY   B 31  ? 1.24655  0.763055 1.21318  0.165141    -0.208977   -0.38875    43  GLY   A HA3  
2243 N N    . GLU   B 32  ? 1.37719  1.01024  1.32421  0.229549    -0.174444   -0.442891   44  GLU   A N    
2244 C CA   . GLU   B 32  ? 1.33137  1.05123  1.27781  0.247301    -0.151367   -0.449724   44  GLU   A CA   
2245 C C    . GLU   B 32  ? 1.22243  0.988128 1.19921  0.248703    -0.143835   -0.40945    44  GLU   A C    
2246 O O    . GLU   B 32  ? 1.238    1.07942  1.21641  0.244371    -0.125016   -0.403179   44  GLU   A O    
2247 C CB   . GLU   B 32  ? 1.36416  1.08435  1.30475  0.291535    -0.142916   -0.494944   44  GLU   A CB   
2248 H H    . GLU   B 32  ? 1.40244  0.985439 1.35149  0.247521    -0.182011   -0.456238   44  GLU   A H    
2249 H HA   . GLU   B 32  ? 1.2933   1.04374  1.22147  0.227276    -0.145793   -0.452288   44  GLU   A HA   
2252 N N    . GLU   B 33  ? 1.13     0.847679 1.12668  0.250172    -0.158528   -0.381304   45  GLU   A N    
2253 C CA   . GLU   B 33  ? 1.10976  0.866451 1.13251  0.263894    -0.154516   -0.351483   45  GLU   A CA   
2254 C C    . GLU   B 33  ? 0.967414 0.748832 0.995123 0.225068    -0.152534   -0.311134   45  GLU   A C    
2255 O O    . GLU   B 33  ? 0.873281 0.611554 0.895608 0.194776    -0.162653   -0.29417    45  GLU   A O    
2256 C CB   . GLU   B 33  ? 1.24971  0.942477 1.28596  0.296819    -0.171175   -0.344136   45  GLU   A CB   
2257 C CG   . GLU   B 33  ? 1.36132  0.95632  1.38795  0.273275    -0.190189   -0.327434   45  GLU   A CG   
2258 C CD   . GLU   B 33  ? 1.48876  1.00658  1.52093  0.311908    -0.205305   -0.326138   45  GLU   A CD   
2259 O OE1  . GLU   B 33  ? 1.5292   1.03538  1.56128  0.353307    -0.203934   -0.36346    45  GLU   A OE1  
2260 O OE2  . GLU   B 33  ? 1.53201  1.00167  1.56688  0.301834    -0.217327   -0.287141   45  GLU   A OE2  
2261 H H    . GLU   B 33  ? 1.19685  0.857488 1.18894  0.240581    -0.171442   -0.380304   45  GLU   A H    
2262 H HA   . GLU   B 33  ? 1.08416  0.896953 1.11204  0.279557    -0.141336   -0.364184   45  GLU   A HA   
2263 H HB2  . GLU   B 33  ? 1.22018  0.94385  1.27182  0.305497    -0.170459   -0.322619   45  GLU   A HB2  
2264 H HB3  . GLU   B 33  ? 1.28468  0.970704 1.32077  0.326696    -0.169853   -0.371965   45  GLU   A HB3  
2265 H HG2  . GLU   B 33  ? 1.37078  0.942714 1.383    0.257576    -0.191761   -0.347497   45  GLU   A HG2  
2266 H HG3  . GLU   B 33  ? 1.31801  0.922282 1.34877  0.248616    -0.191064   -0.297353   45  GLU   A HG3  
2267 N N    . THR   B 34  ? 0.92827  0.783569 0.968559 0.226199    -0.13828    -0.298266   46  THR   A N    
2268 C CA   . THR   B 34  ? 0.833608 0.712807 0.880449 0.197164    -0.135257   -0.262466   46  THR   A CA   
2269 C C    . THR   B 34  ? 0.881003 0.759587 0.945488 0.21637     -0.144706   -0.238706   46  THR   A C    
2270 O O    . THR   B 34  ? 0.947889 0.829087 1.02346  0.254717    -0.150041   -0.251223   46  THR   A O    
2271 C CB   . THR   B 34  ? 0.810242 0.765362 0.854565 0.182574    -0.113367   -0.26627    46  THR   A CB   
2272 O OG1  . THR   B 34  ? 0.72905  0.736137 0.788299 0.212042    -0.10518    -0.282473   46  THR   A OG1  
2273 C CG2  . THR   B 34  ? 0.785009 0.73969  0.805123 0.165774    -0.105317   -0.284411   46  THR   A CG2  
2274 H H    . THR   B 34  ? 0.912585 0.806164 0.95773  0.24482     -0.129374   -0.314171   46  THR   A H    
2275 H HA   . THR   B 34  ? 0.856641 0.702575 0.896642 0.175289    -0.141243   -0.252336   46  THR   A HA   
2276 H HB   . THR   B 34  ? 0.750801 0.720097 0.799287 0.16476     -0.110635   -0.244941   46  THR   A HB   
2278 H HG21 . THR   B 34  ? 0.760613 0.756866 0.77697  0.155457    -0.0909587  -0.282597   46  THR   A HG21 
2279 H HG22 . THR   B 34  ? 0.824089 0.769598 0.837188 0.182663    -0.106377   -0.30781    46  THR   A HG22 
2280 H HG23 . THR   B 34  ? 0.793724 0.716553 0.808075 0.14839     -0.113542   -0.274533   46  THR   A HG23 
2281 N N    . PRO   B 35  ? 0.886156 0.765232 0.95265  0.193232    -0.147281   -0.204097   47  PRO   A N    
2282 C CA   . PRO   B 35  ? 0.937919 0.824311 1.01427  0.211021    -0.15701    -0.179507   47  PRO   A CA   
2283 C C    . PRO   B 35  ? 0.976948 0.945429 1.07064  0.236156    -0.149747   -0.191605   47  PRO   A C    
2284 O O    . PRO   B 35  ? 0.893849 0.924596 0.99038  0.221598    -0.131131   -0.207446   47  PRO   A O    
2285 C CB   . PRO   B 35  ? 0.912305 0.803981 0.982245 0.173749    -0.153521   -0.147189   47  PRO   A CB   
2286 C CG   . PRO   B 35  ? 0.860734 0.726818 0.922161 0.140511    -0.147202   -0.152416   47  PRO   A CG   
2287 C CD   . PRO   B 35  ? 0.87139  0.750763 0.929972 0.151642    -0.140446   -0.188204   47  PRO   A CD   
2288 H HA   . PRO   B 35  ? 0.993001 0.827995 1.06779  0.22781     -0.170164   -0.175659   47  PRO   A HA   
2289 H HB2  . PRO   B 35  ? 0.864149 0.809354 0.938249 0.168656    -0.144506   -0.145241   47  PRO   A HB2  
2290 H HB3  . PRO   B 35  ? 0.933189 0.792782 1        0.176668    -0.164274   -0.125923   47  PRO   A HB3  
2291 H HG2  . PRO   B 35  ? 0.834201 0.728787 0.895073 0.119495    -0.137782   -0.142433   47  PRO   A HG2  
2292 H HG3  . PRO   B 35  ? 0.905718 0.720624 0.963557 0.133843    -0.156874   -0.143521   47  PRO   A HG3  
2293 H HD2  . PRO   B 35  ? 0.822388 0.746708 0.880379 0.142586    -0.127391   -0.193345   47  PRO   A HD2  
2294 H HD3  . PRO   B 35  ? 0.877583 0.72124  0.929361 0.142067    -0.145005   -0.195574   47  PRO   A HD3  
2295 N N    . MET   B 36  ? 1.02793  0.995401 1.13343  0.273202    -0.165173   -0.182695   48  MET   A N    
2296 C CA   . MET   B 36  ? 0.957388 1.01232  1.08541  0.296805    -0.163531   -0.188172   48  MET   A CA   
2297 C C    . MET   B 36  ? 0.896156 0.984614 1.01981  0.27523     -0.167557   -0.155243   48  MET   A C    
2298 O O    . MET   B 36  ? 0.861323 0.894058 0.965441 0.256791    -0.175838   -0.125094   48  MET   A O    
2299 C CB   . MET   B 36  ? 1.03662  1.08032  1.18187  0.354095    -0.181478   -0.194247   48  MET   A CB   
2300 C CG   . MET   B 36  ? 1.06164  1.06002  1.20897  0.384017    -0.179945   -0.22935    48  MET   A CG   
2301 S SD   . MET   B 36  ? 0.982209 1.07516  1.14732  0.388822    -0.152859   -0.277677   48  MET   A SD   
2302 C CE   . MET   B 36  ? 0.962243 1.0274   1.09503  0.334783    -0.13343    -0.288215   48  MET   A CE   
2303 H H    . MET   B 36  ? 1.05685  0.967024 1.15665  0.284347    -0.178057   -0.172448   48  MET   A H    
2304 H HA   . MET   B 36  ? 0.92912  1.0323   1.06368  0.288938    -0.148008   -0.209346   48  MET   A HA   
2305 H HB2  . MET   B 36  ? 1.06313  1.06118  1.19945  0.360462    -0.196862   -0.168615   48  MET   A HB2  
2306 H HB3  . MET   B 36  ? 1.0095   1.1238   1.17384  0.368072    -0.179966   -0.199799   48  MET   A HB3  
2307 H HG2  . MET   B 36  ? 1.07287  1.00951  1.20151  0.364509    -0.180065   -0.22817    48  MET   A HG2  
2308 H HG3  . MET   B 36  ? 1.10972  1.08375  1.26512  0.420761    -0.19394    -0.227075   48  MET   A HG3  
2309 H HE1  . MET   B 36  ? 0.943444 1.05193  1.07885  0.335491    -0.118094   -0.311909   48  MET   A HE1  
2310 H HE2  . MET   B 36  ? 0.920599 0.996891 1.04736  0.30466     -0.13046    -0.268249   48  MET   A HE2  
2311 H HE3  . MET   B 36  ? 0.993264 0.99006  1.11146  0.335439    -0.141529   -0.290235   48  MET   A HE3  
2312 N N    . ILE   B 37  ? 0.823251 1.00641  0.964453 0.275176    -0.160654   -0.163069   49  ILE   A N    
2313 C CA   . ILE   B 37  ? 0.780317 1.0049   0.916131 0.257866    -0.166031   -0.13793    49  ILE   A CA   
2314 C C    . ILE   B 37  ? 0.829753 1.01231  0.957284 0.28885     -0.193696   -0.105599   49  ILE   A C    
2315 O O    . ILE   B 37  ? 0.835666 1.01465  0.979906 0.336263    -0.208988   -0.111333   49  ILE   A O    
2316 C CB   . ILE   B 37  ? 0.798556 1.1353   0.959577 0.257429    -0.157754   -0.157903   49  ILE   A CB   
2317 C CG1  . ILE   B 37  ? 0.79223  1.16774  0.959009 0.226511    -0.128138   -0.188554   49  ILE   A CG1  
2318 C CG2  . ILE   B 37  ? 0.778768 1.16154  0.931689 0.241375    -0.16694    -0.135635   49  ILE   A CG2  
2319 C CD1  . ILE   B 37  ? 0.8203   1.13011  0.960545 0.191578    -0.112236   -0.18646    49  ILE   A CD1  
2320 H H    . ILE   B 37  ? 0.815177 1.0399   0.971438 0.284765    -0.152057   -0.185967   49  ILE   A H    
2321 H HA   . ILE   B 37  ? 0.77073  0.976534 0.890477 0.225684    -0.157036   -0.129169   49  ILE   A HA   
2322 H HB   . ILE   B 37  ? 0.815639 1.1745   0.99597  0.291873    -0.16713    -0.166694   49  ILE   A HB   
2323 H HG12 . ILE   B 37  ? 0.800404 1.19482  0.983414 0.247799    -0.125139   -0.208228   49  ILE   A HG12 
2324 H HG13 . ILE   B 37  ? 0.767524 1.20037  0.940625 0.209087    -0.121845   -0.19193    49  ILE   A HG13 
2325 H HG21 . ILE   B 37  ? 0.757432 1.21054  0.925951 0.233503    -0.159975   -0.151244   49  ILE   A HG21 
2326 H HG22 . ILE   B 37  ? 0.770272 1.12196  0.902103 0.212501    -0.160031   -0.12365    49  ILE   A HG22 
2327 H HG23 . ILE   B 37  ? 0.818641 1.19259  0.970876 0.267606    -0.186616   -0.118367   49  ILE   A HG23 
2328 H HD11 . ILE   B 37  ? 0.800813 1.09001  0.926833 0.17319     -0.114709   -0.167587   49  ILE   A HD11 
2329 H HD12 . ILE   B 37  ? 0.779883 1.11934  0.921712 0.173415    -0.0948455  -0.202089   49  ILE   A HD12 
2330 H HD13 . ILE   B 37  ? 0.826834 1.0871   0.962488 0.205735    -0.116972   -0.188729   49  ILE   A HD13 
2331 N N    . GLY   B 38  ? 0.78619  0.935034 0.886453 0.264034    -0.199144   -0.0712386  50  GLY   A N    
2332 C CA   . GLY   B 38  ? 0.841091 0.942241 0.924435 0.288641    -0.224085   -0.0340075  50  GLY   A CA   
2333 C C    . GLY   B 38  ? 0.882036 0.868749 0.941466 0.276803    -0.227263   -0.0120093  50  GLY   A C    
2334 O O    . GLY   B 38  ? 0.905696 0.84558  0.940504 0.278879    -0.241878   0.0267495   50  GLY   A O    
2335 H H    . GLY   B 38  ? 0.762972 0.917953 0.853646 0.231533    -0.186301   -0.070396   50  GLY   A H    
2336 H HA2  . GLY   B 38  ? 0.835987 0.970887 0.907653 0.275902    -0.227037   -0.0169891  50  GLY   A HA2  
2337 H HA3  . GLY   B 38  ? 0.872266 0.985376 0.97072  0.326696    -0.236986   -0.0390194  50  GLY   A HA3  
2338 N N    . ASP   B 39  ? 0.868338 0.81137  0.933445 0.263099    -0.214334   -0.0361586  51  ASP   A N    
2339 C CA   . ASP   B 39  ? 0.915449 0.756902 0.963138 0.246583    -0.217238   -0.0214831  51  ASP   A CA   
2340 C C    . ASP   B 39  ? 0.92055  0.75081  0.945373 0.201553    -0.210343   0.0117226   51  ASP   A C    
2341 O O    . ASP   B 39  ? 0.872032 0.768438 0.896327 0.174856    -0.195538   0.00948569  51  ASP   A O    
2342 C CB   . ASP   B 39  ? 0.913714 0.730027 0.971726 0.237125    -0.205485   -0.0580127  51  ASP   A CB   
2343 C CG   . ASP   B 39  ? 0.939261 0.744843 1.01327  0.282345    -0.211818   -0.0906834  51  ASP   A CG   
2344 O OD1  . ASP   B 39  ? 0.997292 0.805432 1.07841  0.325478    -0.227261   -0.0831582  51  ASP   A OD1  
2345 O OD2  . ASP   B 39  ? 0.904553 0.702503 0.982992 0.276485    -0.201413   -0.124282   51  ASP   A OD2  
2346 H H    . ASP   B 39  ? 0.83224  0.811612 0.911811 0.262625    -0.203699   -0.0626818  51  ASP   A H    
2347 H HA   . ASP   B 39  ? 0.982748 0.777374 1.02592  0.273136    -0.232538   -0.00926956 51  ASP   A HA   
2348 H HB2  . ASP   B 39  ? 0.851025 0.716548 0.914255 0.217381    -0.191159   -0.0712146  51  ASP   A HB2  
2349 H HB3  . ASP   B 39  ? 0.932892 0.690926 0.980459 0.218217    -0.206734   -0.0485721  51  ASP   A HB3  
2350 N N    . LYS   B 40  ? 1.01915  0.763059 1.02436  0.192692    -0.219734   0.0418936   52  LYS   A N    
2351 C CA   . LYS   B 40  ? 1.03464  0.759455 1.02194  0.14521     -0.20895    0.068629    52  LYS   A CA   
2352 C C    . LYS   B 40  ? 1.02753  0.731076 1.02955  0.114561    -0.195383   0.0432081   52  LYS   A C    
2353 O O    . LYS   B 40  ? 1.10034  0.737488 1.10735  0.121627    -0.203218   0.0296343   52  LYS   A O    
2354 C CB   . LYS   B 40  ? 1.11457  0.76015  1.07311  0.141783    -0.222054   0.114707    52  LYS   A CB   
2355 H H    . LYS   B 40  ? 1.0693   0.76421  1.07281  0.216839    -0.232382   0.0454656   52  LYS   A H    
2356 H HA   . LYS   B 40  ? 0.99207  0.775732 0.97623  0.133152    -0.200467   0.0720808   52  LYS   A HA   
2359 N N    . VAL   B 41  ? 0.978016 0.739511 0.98615  0.0824313   -0.176117   0.0353028   53  VAL   A N    
2360 C CA   . VAL   B 41  ? 0.910604 0.674166 0.935108 0.0591903   -0.164372   0.0091909   53  VAL   A CA   
2361 C C    . VAL   B 41  ? 0.890091 0.644802 0.912645 0.0160774   -0.153632   0.0298263   53  VAL   A C    
2362 O O    . VAL   B 41  ? 0.909889 0.700471 0.921722 0.00051239  -0.143501   0.0512867   53  VAL   A O    
2363 C CB   . VAL   B 41  ? 0.859988 0.700757 0.895599 0.0645049   -0.150677   -0.0185484  53  VAL   A CB   
2364 C CG1  . VAL   B 41  ? 0.849174 0.699875 0.896675 0.0424131   -0.138489   -0.0402533  53  VAL   A CG1  
2365 C CG2  . VAL   B 41  ? 0.84807  0.706873 0.890443 0.104233    -0.158711   -0.0407628  53  VAL   A CG2  
2366 H H    . VAL   B 41  ? 0.947541 0.748646 0.948318 0.0760658   -0.170791   0.0466706   53  VAL   A H    
2367 H HA   . VAL   B 41  ? 0.943397 0.666002 0.972311 0.0690729   -0.172437   -0.00392334 53  VAL   A HA   
2368 H HB   . VAL   B 41  ? 0.8388   0.716184 0.868435 0.0560629   -0.143758   -0.00692951 53  VAL   A HB   
2369 H HG11 . VAL   B 41  ? 0.860815 0.674146 0.911503 0.0458129   -0.14608    -0.0504278  53  VAL   A HG11 
2370 H HG12 . VAL   B 41  ? 0.8273   0.683311 0.874992 0.0191987   -0.131146   -0.0278387  53  VAL   A HG12 
2371 H HG13 . VAL   B 41  ? 0.80007  0.689955 0.851153 0.048285    -0.130605   -0.056535   53  VAL   A HG13 
2372 H HG21 . VAL   B 41  ? 0.809047 0.712111 0.858133 0.102434    -0.14825    -0.058834   53  VAL   A HG21 
2373 H HG22 . VAL   B 41  ? 0.871279 0.739999 0.908499 0.119519    -0.166196   -0.026929   53  VAL   A HG22 
2374 H HG23 . VAL   B 41  ? 0.882491 0.700195 0.927549 0.116059    -0.166505   -0.0512542  53  VAL   A HG23 
2375 N N    . TYR   B 42  ? 0.924263 0.636784 0.958131 -0.00352621 -0.155633   0.020506    54  TYR   A N    
2376 C CA   . TYR   B 42  ? 0.931689 0.642675 0.972603 -0.0456447  -0.145664   0.0363154   54  TYR   A CA   
2377 C C    . TYR   B 42  ? 0.853913 0.606925 0.918428 -0.0592787  -0.136551   0.00788056  54  TYR   A C    
2378 O O    . TYR   B 42  ? 0.75764  0.490292 0.829726 -0.0500207  -0.146134   -0.0189675  54  TYR   A O    
2379 C CB   . TYR   B 42  ? 1.03875  0.665115 1.07536  -0.0622797  -0.157999   0.0516951   54  TYR   A CB   
2380 C CG   . TYR   B 42  ? 1.09291  0.656407 1.10215  -0.0467169  -0.170139   0.0840884   54  TYR   A CG   
2381 C CD1  . TYR   B 42  ? 1.1431   0.677655 1.14264  -0.00077833 -0.18593    0.0755351   54  TYR   A CD1  
2382 C CD2  . TYR   B 42  ? 1.16149  0.691564 1.15458  -0.0777373  -0.165937   0.124369    54  TYR   A CD2  
2383 C CE1  . TYR   B 42  ? 1.23882  0.712447 1.21349  0.0188995   -0.199737   0.107596    54  TYR   A CE1  
2384 C CE2  . TYR   B 42  ? 1.2469   0.709993 1.20932  -0.0631168  -0.178475   0.159004    54  TYR   A CE2  
2385 C CZ   . TYR   B 42  ? 1.30783  0.74008  1.26114  -0.0123221  -0.197002   0.151118    54  TYR   A CZ   
2386 O OH   . TYR   B 42  ? 1.44662  0.811175 1.36928  0.00774615  -0.211669   0.188147    54  TYR   A OH   
2387 H H    . TYR   B 42  ? 0.934201 0.621952 0.972634 0.00929342  -0.163418   0.0020542   54  TYR   A H    
2388 H HA   . TYR   B 42  ? 0.922089 0.660866 0.954675 -0.0547436  -0.136576   0.0553764   54  TYR   A HA   
2389 H HB2  . TYR   B 42  ? 1.03435  0.635715 1.07903  -0.0556444  -0.166223   0.028973    54  TYR   A HB2  
2390 H HB3  . TYR   B 42  ? 1.0257   0.659986 1.07049  -0.0932932  -0.149817   0.0615167   54  TYR   A HB3  
2391 H HD1  . TYR   B 42  ? 1.10601  0.665534 1.11595  0.0188768   -0.186963   0.0483803   54  TYR   A HD1  
2392 H HD2  . TYR   B 42  ? 1.14172  0.695615 1.14438  -0.10908    -0.153943   0.129224    54  TYR   A HD2  
2393 H HE1  . TYR   B 42  ? 1.25745  0.716562 1.22927  0.0538188   -0.210831   0.100532    54  TYR   A HE1  
2394 H HE2  . TYR   B 42  ? 1.29792  0.738029 1.24568  -0.0864662  -0.174187   0.188603    54  TYR   A HE2  
2396 N N    . VAL   B 43  ? 0.784602 0.59557  0.858191 -0.0786871  -0.118497   0.0134191   55  VAL   A N    
2397 C CA   . VAL   B 43  ? 0.714765 0.564741 0.810418 -0.0874043  -0.111171   -0.00888495 55  VAL   A CA   
2398 C C    . VAL   B 43  ? 0.686677 0.566099 0.801598 -0.120626   -0.0979829  0.00525741  55  VAL   A C    
2399 O O    . VAL   B 43  ? 0.768799 0.653793 0.874905 -0.135632   -0.087875   0.0306533   55  VAL   A O    
2400 C CB   . VAL   B 43  ? 0.640044 0.540645 0.73173  -0.0678259  -0.0996119  -0.0254108  55  VAL   A CB   
2401 C CG1  . VAL   B 43  ? 0.635305 0.524087 0.712023 -0.0366937  -0.108487   -0.0398324  55  VAL   A CG1  
2402 C CG2  . VAL   B 43  ? 0.633924 0.577625 0.719522 -0.0767364  -0.0807651  -0.0101421  55  VAL   A CG2  
2403 H H    . VAL   B 43  ? 0.78797  0.613705 0.852652 -0.0848425  -0.110996   0.0312429   55  VAL   A H    
2404 H HA   . VAL   B 43  ? 0.724492 0.550204 0.825639 -0.0851262  -0.12198    -0.0232785  55  VAL   A HA   
2405 H HB   . VAL   B 43  ? 0.622803 0.538379 0.726383 -0.0708188  -0.0977634  -0.0387548  55  VAL   A HB   
2406 H HG11 . VAL   B 43  ? 0.660781 0.538803 0.727061 -0.0301685  -0.112033   -0.0265315  55  VAL   A HG11 
2407 H HG12 . VAL   B 43  ? 0.655588 0.517184 0.734513 -0.0306606  -0.118931   -0.0519883  55  VAL   A HG12 
2408 H HG13 . VAL   B 43  ? 0.604626 0.525405 0.67999  -0.029464   -0.0998768  -0.0506832  55  VAL   A HG13 
2409 H HG21 . VAL   B 43  ? 0.600902 0.568798 0.681713 -0.065257   -0.0743983  -0.0215293  55  VAL   A HG21 
2410 H HG22 . VAL   B 43  ? 0.620643 0.581092 0.719376 -0.0933451  -0.0723347  -0.00637733 55  VAL   A HG22 
2411 H HG23 . VAL   B 43  ? 0.655623 0.586529 0.728066 -0.0773976  -0.0833486  0.00643665  55  VAL   A HG23 
2412 N N    . HIS   B 44  ? 0.669493 0.576555 0.810024 -0.129298   -0.0972955  -0.0120454  56  HIS   A N    
2413 C CA   . HIS   B 44  ? 0.612545 0.575061 0.777897 -0.14796    -0.0805364  -0.00724389 56  HIS   A CA   
2414 C C    . HIS   B 44  ? 0.542965 0.546693 0.709692 -0.125558   -0.0712026  -0.0251542  56  HIS   A C    
2415 O O    . HIS   B 44  ? 0.555154 0.545355 0.711588 -0.105119   -0.0811918  -0.0430355  56  HIS   A O    
2416 C CB   . HIS   B 44  ? 0.682341 0.649042 0.880724 -0.174731   -0.0892836  -0.011193   56  HIS   A CB   
2417 C CG   . HIS   B 44  ? 0.707838 0.655223 0.912939 -0.210082   -0.0861372  0.0124366   56  HIS   A CG   
2418 N ND1  . HIS   B 44  ? 0.739391 0.71879  0.943219 -0.225653   -0.0640221  0.035374    56  HIS   A ND1  
2419 C CD2  . HIS   B 44  ? 0.737596 0.637042 0.948277 -0.235784   -0.0998143  0.0169      56  HIS   A CD2  
2420 C CE1  . HIS   B 44  ? 0.776626 0.7303   0.984641 -0.261005   -0.0634263  0.056387    56  HIS   A CE1  
2421 N NE2  . HIS   B 44  ? 0.782844 0.683861 0.99573  -0.268397   -0.0854203  0.0457025   56  HIS   A NE2  
2422 H H    . HIS   B 44  ? 0.662387 0.555149 0.804959 -0.121463   -0.108182   -0.0280013  56  HIS   A H    
2423 H HA   . HIS   B 44  ? 0.632661 0.604034 0.791257 -0.157296   -0.0691632  0.00978093  56  HIS   A HA   
2424 H HB2  . HIS   B 44  ? 0.675558 0.616009 0.87171  -0.168413   -0.104791   -0.0252789  56  HIS   A HB2  
2425 H HB3  . HIS   B 44  ? 0.634844 0.645964 0.853373 -0.175317   -0.082015   -0.0173506  56  HIS   A HB3  
2427 H HD2  . HIS   B 44  ? 0.763764 0.632523 0.97481  -0.233574   -0.115559   0.00242565  56  HIS   A HD2  
2428 H HE1  . HIS   B 44  ? 0.789071 0.757032 0.994018 -0.278617   -0.0490921  0.0753682   56  HIS   A HE1  
2430 N N    . TYR   B 45  ? 0.538725 0.588987 0.714962 -0.129435   -0.0503458  -0.020484   57  TYR   A N    
2431 C CA   . TYR   B 45  ? 0.50121  0.578908 0.675681 -0.108945   -0.0396469  -0.035731   57  TYR   A CA   
2432 C C    . TYR   B 45  ? 0.513277 0.640591 0.715535 -0.115347   -0.0214926  -0.0349865  57  TYR   A C    
2433 O O    . TYR   B 45  ? 0.548748 0.698524 0.763815 -0.135507   -0.00976682 -0.0217605  57  TYR   A O    
2434 C CB   . TYR   B 45  ? 0.493265 0.565463 0.635619 -0.095532   -0.0301275  -0.0369932  57  TYR   A CB   
2435 C CG   . TYR   B 45  ? 0.507905 0.604524 0.641579 -0.107765   -0.0108661  -0.0238629  57  TYR   A CG   
2436 C CD1  . TYR   B 45  ? 0.448986 0.582046 0.589472 -0.106973   0.0111901   -0.0312197  57  TYR   A CD1  
2437 C CD2  . TYR   B 45  ? 0.572365 0.653206 0.68811  -0.119335   -0.0147339  -0.00370418 57  TYR   A CD2  
2438 C CE1  . TYR   B 45  ? 0.52535  0.683668 0.654682 -0.119382   0.0300998   -0.0225786  57  TYR   A CE1  
2439 C CE2  . TYR   B 45  ? 0.586617 0.692788 0.687335 -0.131688   0.00254043  0.00930866  57  TYR   A CE2  
2440 C CZ   . TYR   B 45  ? 0.540016 0.687519 0.646753 -0.132654   0.0257321   -0.0021101  57  TYR   A CZ   
2441 O OH   . TYR   B 45  ? 0.595362 0.770584 0.683732 -0.145577   0.0443077   0.00710245  57  TYR   A OH   
2442 H H    . TYR   B 45  ? 0.545035 0.607669 0.727637 -0.145364   -0.04171    -0.00784116 57  TYR   A H    
2443 H HA   . TYR   B 45  ? 0.501523 0.569813 0.67778  -0.0990478  -0.0507537  -0.0471741  57  TYR   A HA   
2444 H HB2  . TYR   B 45  ? 0.476975 0.556504 0.616154 -0.083172   -0.0255499  -0.0489131  57  TYR   A HB2  
2445 H HB3  . TYR   B 45  ? 0.508581 0.554674 0.637313 -0.0908783  -0.0415165  -0.0357495  57  TYR   A HB3  
2446 H HD1  . TYR   B 45  ? 0.45873  0.598517 0.610514 -0.0972992  0.0135381   -0.0423494  57  TYR   A HD1  
2447 H HD2  . TYR   B 45  ? 0.58231  0.632876 0.692898 -0.117403   -0.0295518  0.00127108  57  TYR   A HD2  
2448 H HE1  . TYR   B 45  ? 0.498938 0.679831 0.632189 -0.1171     0.0459543   -0.0310149  57  TYR   A HE1  
2449 H HE2  . TYR   B 45  ? 0.606398 0.699993 0.690762 -0.138622   -0.00143295 0.0257747   57  TYR   A HE2  
2451 N N    . LYS   B 46  ? 0.485525 0.629197 0.696293 -0.0964644  -0.0188477  -0.0488384  58  LYS   A N    
2452 C CA   . LYS   B 46  ? 0.514929 0.701035 0.747773 -0.0903583  0.00054187  -0.0520775  58  LYS   A CA   
2453 C C    . LYS   B 46  ? 0.487142 0.658183 0.691713 -0.0696359  0.0133582   -0.0628211  58  LYS   A C    
2454 O O    . LYS   B 46  ? 0.481259 0.623795 0.666489 -0.0565511  0.00247922  -0.0698488  58  LYS   A O    
2455 C CB   . LYS   B 46  ? 0.545271 0.760507 0.81731  -0.0863449  -0.012169   -0.0563363  58  LYS   A CB   
2456 C CG   . LYS   B 46  ? 0.607377 0.831561 0.905359 -0.113982   -0.0277586  -0.0490831  58  LYS   A CG   
2457 C CD   . LYS   B 46  ? 0.651653 0.90505  0.985406 -0.112841   -0.0482374  -0.0569446  58  LYS   A CD   
2458 C CE   . LYS   B 46  ? 0.664729 0.917982 1.02003  -0.146182   -0.0650351  -0.0538561  58  LYS   A CE   
2459 N NZ   . LYS   B 46  ? 0.708213 1.01004  1.10589  -0.148042   -0.0831411  -0.0634765  58  LYS   A NZ   
2460 H H    . LYS   B 46  ? 0.492959 0.618761 0.694144 -0.0853902  -0.0294523  -0.0564495  58  LYS   A H    
2461 H HA   . LYS   B 46  ? 0.513752 0.718293 0.752272 -0.103654   0.0130772   -0.0446047  58  LYS   A HA   
2462 H HB2  . LYS   B 46  ? 0.544696 0.74307  0.806445 -0.0718769  -0.0234784  -0.0630142  58  LYS   A HB2  
2463 H HB3  . LYS   B 46  ? 0.542156 0.789181 0.833329 -0.0799064  0.00084932  -0.0580578  58  LYS   A HB3  
2464 H HG2  . LYS   B 46  ? 0.610642 0.857838 0.922011 -0.12927    -0.0144755  -0.041101   58  LYS   A HG2  
2465 H HG3  . LYS   B 46  ? 0.615809 0.802971 0.892328 -0.120254   -0.0375785  -0.0468289  58  LYS   A HG3  
2466 H HD2  . LYS   B 46  ? 0.636562 0.869563 0.953191 -0.0962597  -0.0599968  -0.0643125  58  LYS   A HD2  
2467 H HD3  . LYS   B 46  ? 0.630163 0.925305 0.990212 -0.105694   -0.0391052  -0.0579409  58  LYS   A HD3  
2468 H HE2  . LYS   B 46  ? 0.684995 0.950149 1.05031  -0.165473   -0.0522429  -0.043805   58  LYS   A HE2  
2469 H HE3  . LYS   B 46  ? 0.690178 0.898973 1.02054  -0.14847    -0.0769191  -0.0558345  58  LYS   A HE3  
2470 H HZ1  . LYS   B 46  ? 0.684732 1.03187  1.1103   -0.145718   -0.072182   -0.0615333  58  LYS   A HZ1  
2471 H HZ2  . LYS   B 46  ? 0.690213 0.982713 1.0754   -0.128967   -0.0946433  -0.0711855  58  LYS   A HZ2  
2472 H HZ3  . LYS   B 46  ? 0.713065 1.0105   1.12144  -0.170675   -0.0941053  -0.0640386  58  LYS   A HZ3  
2473 N N    . GLY   B 47  ? 0.42711  0.614033 0.623671 -0.0712946  0.037269    -0.0646936  59  GLY   A N    
2474 C CA   . GLY   B 47  ? 0.426901 0.595949 0.595549 -0.0583441  0.0509243   -0.0772834  59  GLY   A CA   
2475 C C    . GLY   B 47  ? 0.450676 0.641298 0.633986 -0.0469796  0.0740446   -0.0869351  59  GLY   A C    
2476 O O    . GLY   B 47  ? 0.447644 0.677471 0.660457 -0.0514264  0.0836691   -0.0836943  59  GLY   A O    
2477 H H    . GLY   B 47  ? 0.446859 0.656339 0.654589 -0.0826165  0.0459528   -0.0589885  59  GLY   A H    
2478 H HA2  . GLY   B 47  ? 0.428479 0.575911 0.588471 -0.048505   0.0413987   -0.0812193  59  GLY   A HA2  
2479 H HA3  . GLY   B 47  ? 0.434176 0.598213 0.581936 -0.0669842  0.0548758   -0.0763566  59  GLY   A HA3  
2480 N N    . LYS   B 48  ? 0.461516 0.625458 0.624985 -0.0322958  0.0844636   -0.0997819  60  LYS   A N    
2481 C CA   . LYS   B 48  ? 0.474358 0.645838 0.646453 -0.0180755  0.108094    -0.112143   60  LYS   A CA   
2482 C C    . LYS   B 48  ? 0.523584 0.650365 0.659178 -0.0135812  0.12021     -0.126659   60  LYS   A C    
2483 O O    . LYS   B 48  ? 0.546337 0.642635 0.658378 -0.0175883  0.108276    -0.124918   60  LYS   A O    
2484 C CB   . LYS   B 48  ? 0.52695  0.712913 0.73646  0.00646226  0.102606    -0.109296   60  LYS   A CB   
2485 C CG   . LYS   B 48  ? 0.624648 0.777442 0.826287 0.0222659   0.0809216   -0.102983   60  LYS   A CG   
2486 C CD   . LYS   B 48  ? 0.696022 0.864961 0.930141 0.0508844   0.0723019   -0.0986325  60  LYS   A CD   
2487 C CE   . LYS   B 48  ? 0.83505  0.96069  1.05141  0.0783518   0.0858215   -0.104264   60  LYS   A CE   
2488 N NZ   . LYS   B 48  ? 0.89193  1.03978  1.14446  0.112972    0.0824576   -0.100779   60  LYS   A NZ   
2489 H H    . LYS   B 48  ? 0.458954 0.597799 0.60297  -0.0312939  0.0776713   -0.101511   60  LYS   A H    
2490 H HA   . LYS   B 48  ? 0.49271  0.689775 0.668813 -0.0277573  0.120741    -0.113971   60  LYS   A HA   
2491 H HB2  . LYS   B 48  ? 0.552362 0.738714 0.766161 0.0194347   0.119353    -0.118687   60  LYS   A HB2  
2492 H HB3  . LYS   B 48  ? 0.523876 0.745311 0.760256 -0.00013897 0.0972054   -0.102457   60  LYS   A HB3  
2493 H HG2  . LYS   B 48  ? 0.597891 0.752404 0.797077 0.0105295   0.0647823   -0.0962516  60  LYS   A HG2  
2494 H HG3  . LYS   B 48  ? 0.626732 0.743563 0.799949 0.0246247   0.0872985   -0.108272   60  LYS   A HG3  
2495 H HD2  . LYS   B 48  ? 0.697683 0.907924 0.963904 0.0512748   0.0773755   -0.0993341  60  LYS   A HD2  
2496 H HD3  . LYS   B 48  ? 0.696537 0.864992 0.932148 0.0512606   0.0518868   -0.0911001  60  LYS   A HD3  
2497 H HE2  . LYS   B 48  ? 0.825298 0.914465 1.01379  0.0782932   0.0779609   -0.100316   60  LYS   A HE2  
2498 H HE3  . LYS   B 48  ? 0.824306 0.939032 1.02904  0.0733732   0.105714    -0.114804   60  LYS   A HE3  
2499 H HZ1  . LYS   B 48  ? 0.873717 1.03509  1.13644  0.11727     0.0624973   -0.091608   60  LYS   A HZ1  
2500 H HZ2  . LYS   B 48  ? 0.874691 1.0602   1.15526  0.113734    0.092057    -0.106009   60  LYS   A HZ2  
2501 H HZ3  . LYS   B 48  ? 0.909924 1.02149  1.14661  0.129814    0.0905823   -0.102769   60  LYS   A HZ3  
2502 N N    . LEU   B 49  ? 0.538574 0.662568 0.670024 -0.00709276 0.1455      -0.143002   61  LEU   A N    
2503 C CA   . LEU   B 49  ? 0.581267 0.654131 0.684413 -0.00016378 0.159511    -0.158768   61  LEU   A CA   
2504 C C    . LEU   B 49  ? 0.644321 0.686101 0.759665 0.0282095   0.150877    -0.149967   61  LEU   A C    
2505 O O    . LEU   B 49  ? 0.661857 0.734071 0.814099 0.0476035   0.143959    -0.14122    61  LEU   A O    
2506 C CB   . LEU   B 49  ? 0.59182  0.667196 0.689104 0.00154787  0.189338    -0.181792   61  LEU   A CB   
2507 C CG   . LEU   B 49  ? 0.565409 0.679397 0.646721 -0.0245901  0.199406    -0.190397   61  LEU   A CG   
2508 C CD1  . LEU   B 49  ? 0.653474 0.772143 0.727948 -0.0197919  0.231127    -0.217604   61  LEU   A CD1  
2509 C CD2  . LEU   B 49  ? 0.542338 0.641961 0.586911 -0.0495262  0.190737    -0.193507   61  LEU   A CD2  
2510 H H    . LEU   B 49  ? 0.544006 0.697605 0.690338 -0.00789931 0.155449    -0.14527    61  LEU   A H    
2511 H HA   . LEU   B 49  ? 0.579494 0.636829 0.659    -0.0146978  0.154803    -0.160139   61  LEU   A HA   
2512 H HB2  . LEU   B 49  ? 0.599421 0.690681 0.722863 0.019646    0.19469     -0.181273   61  LEU   A HB2  
2513 H HB3  . LEU   B 49  ? 0.620555 0.654555 0.697327 0.00373958  0.198281    -0.193193   61  LEU   A HB3  
2514 H HG   . LEU   B 49  ? 0.551389 0.70159  0.650883 -0.0285291  0.191288    -0.176621   61  LEU   A HG   
2515 H HD11 . LEU   B 49  ? 0.642725 0.777957 0.744964 -0.00170609 0.237397    -0.216383   61  LEU   A HD11 
2516 H HD12 . LEU   B 49  ? 0.638288 0.784901 0.69885  -0.0371375  0.23652     -0.221737   61  LEU   A HD12 
2517 H HD13 . LEU   B 49  ? 0.667707 0.745335 0.723295 -0.0175475  0.239636    -0.232508   61  LEU   A HD13 
2518 H HD21 . LEU   B 49  ? 0.523593 0.627224 0.573496 -0.0519945  0.172172    -0.177751   61  LEU   A HD21 
2519 H HD22 . LEU   B 49  ? 0.569603 0.633345 0.598295 -0.0490291  0.197276    -0.205535   61  LEU   A HD22 
2520 H HD23 . LEU   B 49  ? 0.552677 0.676543 0.584098 -0.0636551  0.197189    -0.199664   61  LEU   A HD23 
2521 N N    . SER   B 50  ? 0.726416 0.711229 0.810587 0.0299195   0.152343    -0.152005   62  SER   A N    
2522 C CA   . SER   B 50  ? 0.835122 0.782064 0.920242 0.057807    0.145551    -0.140571   62  SER   A CA   
2523 C C    . SER   B 50  ? 0.93977  0.881085 1.04778  0.0897581   0.160862    -0.147271   62  SER   A C    
2524 O O    . SER   B 50  ? 1.00971  0.952207 1.1388   0.120665    0.148434    -0.133269   62  SER   A O    
2525 C CB   . SER   B 50  ? 0.941129 0.824885 0.982771 0.0478022   0.150002    -0.140889   62  SER   A CB   
2526 O OG   . SER   B 50  ? 0.986345 0.883016 1.01642  0.0311384   0.130678    -0.130155   62  SER   A OG   
2527 H H    . SER   B 50  ? 0.732641 0.703191 0.793591 0.0125925   0.157567    -0.159684   62  SER   A H    
2528 H HA   . SER   B 50  ? 0.820784 0.790181 0.920783 0.0629516   0.126508    -0.127048   62  SER   A HA   
2529 H HB2  . SER   B 50  ? 0.954217 0.82273  0.9799   0.0328944   0.166161    -0.156144   62  SER   A HB2  
2530 H HB3  . SER   B 50  ? 0.975165 0.824525 1.01179  0.0673535   0.150769    -0.133913   62  SER   A HB3  
2532 N N    . ASN   B 51  ? 0.894093 0.834395 0.998842 0.0845721   0.1872      -0.170297   63  ASN   A N    
2533 C CA   . ASN   B 51  ? 0.972419 0.903448 1.09706  0.117329    0.206214    -0.182592   63  ASN   A CA   
2534 C C    . ASN   B 51  ? 0.956198 0.967883 1.1366   0.135302    0.201113    -0.177444   63  ASN   A C    
2535 O O    . ASN   B 51  ? 0.94993  0.97088  1.15724  0.167094    0.216606    -0.188381   63  ASN   A O    
2536 C CB   . ASN   B 51  ? 1.0043   0.906017 1.10251  0.104003    0.237415    -0.214054   63  ASN   A CB   
2537 C CG   . ASN   B 51  ? 0.991413 0.960284 1.09667  0.0786768   0.247262    -0.227808   63  ASN   A CG   
2538 O OD1  . ASN   B 51  ? 0.904988 0.938085 1.03567  0.0694033   0.231922    -0.211585   63  ASN   A OD1  
2539 N ND2  . ASN   B 51  ? 1.00652  0.957627 1.08491  0.0651179   0.272832    -0.257639   63  ASN   A ND2  
2540 H H    . ASN   B 51  ? 0.904604 0.850874 0.993428 0.0611318   0.193368    -0.179749   63  ASN   A H    
2541 H HA   . ASN   B 51  ? 1.00031  0.888694 1.11838  0.137959    0.202301    -0.174381   63  ASN   A HA   
2542 H HB2  . ASN   B 51  ? 1.0525   0.931745 1.15876  0.129419    0.250477    -0.223211   63  ASN   A HB2  
2543 H HB3  . ASN   B 51  ? 1.02726  0.885341 1.09267  0.0865072   0.238934    -0.217298   63  ASN   A HB3  
2544 H HD21 . ASN   B 51  ? 1.00114  0.991574 1.08048  0.0525947   0.280276    -0.266087   63  ASN   A HD21 
2545 H HD22 . ASN   B 51  ? 1.05406  0.95313  1.11173  0.0674443   0.282488    -0.269384   63  ASN   A HD22 
2546 N N    . GLY   B 52  ? 0.913055 0.982738 1.11172  0.113895    0.181637    -0.163029   64  GLY   A N    
2547 C CA   . GLY   B 52  ? 0.885137 1.03311  1.13834  0.122602    0.173802    -0.155217   64  GLY   A CA   
2548 C C    . GLY   B 52  ? 0.896718 1.09815  1.17133  0.116982    0.201799    -0.173246   64  GLY   A C    
2549 O O    . GLY   B 52  ? 0.888912 1.15596  1.21491  0.131679    0.20398     -0.171853   64  GLY   A O    
2550 H H    . GLY   B 52  ? 0.889509 0.949368 1.06635  0.0917407   0.173582    -0.158723   64  GLY   A H    
2551 H HA2  . GLY   B 52  ? 0.853982 1.0225   1.11007  0.104151    0.15651     -0.143115   64  GLY   A HA2  
2552 H HA3  . GLY   B 52  ? 0.9017   1.05054  1.17615  0.150495    0.166291    -0.149429   64  GLY   A HA3  
2553 N N    . LYS   B 53  ? 0.865964 1.0482   1.10183  0.0935329   0.222988    -0.19067    65  LYS   A N    
2554 C CA   . LYS   B 53  ? 0.860501 1.09036  1.10611  0.0883906   0.252645    -0.210306   65  LYS   A CA   
2555 C C    . LYS   B 53  ? 0.816582 1.10028  1.05745  0.0486018   0.249767    -0.199025   65  LYS   A C    
2556 O O    . LYS   B 53  ? 0.7928   1.13277  1.04818  0.0414277   0.271406    -0.207265   65  LYS   A O    
2557 C CB   . LYS   B 53  ? 0.819891 0.996468 1.02563  0.0930511   0.280558    -0.24137    65  LYS   A CB   
2558 H H    . LYS   B 53  ? 0.87317  1.01594  1.07554  0.0799476   0.218966    -0.191049   65  LYS   A H    
2559 H HA   . LYS   B 53  ? 0.849455 1.11406  1.13388  0.110666    0.257519    -0.211431   65  LYS   A HA   
2562 N N    . LYS   B 54  ? 0.828064 1.09423  1.04803  0.0241673   0.223975    -0.17915    66  LYS   A N    
2563 C CA   . LYS   B 54  ? 0.774129 1.08021  0.990791 -0.00902589 0.216188    -0.162152   66  LYS   A CA   
2564 C C    . LYS   B 54  ? 0.719166 1.01651  0.949302 -0.0153673  0.182009    -0.137575   66  LYS   A C    
2565 O O    . LYS   B 54  ? 0.709699 0.959729 0.926017 -0.00447559 0.164844    -0.13566    66  LYS   A O    
2566 C CB   . LYS   B 54  ? 0.760202 1.05036  0.922856 -0.0352122  0.223903    -0.169175   66  LYS   A CB   
2567 H H    . LYS   B 54  ? 0.809763 1.03537  1.01582  0.029205    0.21151     -0.175922   66  LYS   A H    
2568 H HA   . LYS   B 54  ? 0.771599 1.1244   1.01356  -0.0102689  0.228257    -0.162115   66  LYS   A HA   
2571 N N    . PHE   B 55  ? 0.623562 0.965175 0.877123 -0.0358896  0.174481    -0.120043   67  PHE   A N    
2572 C CA   . PHE   B 55  ? 0.628385 0.963264 0.892652 -0.0486805  0.144124    -0.0994755  67  PHE   A CA   
2573 C C    . PHE   B 55  ? 0.60875  0.95524  0.855831 -0.0825049  0.14266     -0.0827012  67  PHE   A C    
2574 O O    . PHE   B 55  ? 0.731072 1.11613  0.978461 -0.0972548  0.164694    -0.0815609  67  PHE   A O    
2575 C CB   . PHE   B 55  ? 0.582736 0.961981 0.9042   -0.0420054  0.133445    -0.0929559  67  PHE   A CB   
2576 C CG   . PHE   B 55  ? 0.642092 1.02062  0.985258 -0.00328161 0.136663    -0.106379   67  PHE   A CG   
2577 C CD1  . PHE   B 55  ? 0.64726  1.05567  1.00774  0.0154871   0.16571     -0.12256    67  PHE   A CD1  
2578 C CD2  . PHE   B 55  ? 0.692335 1.03487  1.03236  0.0164256   0.111712    -0.102818   67  PHE   A CD2  
2579 C CE1  . PHE   B 55  ? 0.708583 1.10704  1.08717  0.0560185   0.167944    -0.133146   67  PHE   A CE1  
2580 C CE2  . PHE   B 55  ? 0.692267 1.02665  1.04585  0.0543193   0.113808    -0.110279   67  PHE   A CE2  
2581 C CZ   . PHE   B 55  ? 0.66422  1.02274  1.03761  0.0754804   0.141225    -0.124763   67  PHE   A CZ   
2582 H H    . PHE   B 55  ? 0.657522 1.0346   0.919863 -0.0436552  0.190765    -0.122059   67  PHE   A H    
2583 H HA   . PHE   B 55  ? 0.605717 0.901053 0.850783 -0.0419472  0.130322    -0.0998342  67  PHE   A HA   
2584 H HB2  . PHE   B 55  ? 0.606599 1.02865  0.948142 -0.0547935  0.146122    -0.0903354  67  PHE   A HB2  
2585 H HB3  . PHE   B 55  ? 0.591721 0.957455 0.914781 -0.0498866  0.111777    -0.0830334  67  PHE   A HB3  
2586 H HD1  . PHE   B 55  ? 0.666833 1.102    1.02609  0.00184773  0.184123    -0.126085   67  PHE   A HD1  
2587 H HD2  . PHE   B 55  ? 0.663146 0.985914 0.990083 0.00493392  0.0934467   -0.0947217  67  PHE   A HD2  
2588 H HE1  . PHE   B 55  ? 0.70616  1.12291  1.09774  0.071401    0.188258    -0.145818   67  PHE   A HE1  
2589 H HE2  . PHE   B 55  ? 0.685676 0.995948 1.0329   0.0668168   0.0966641   -0.105292   67  PHE   A HE2  
2590 H HZ   . PHE   B 55  ? 0.704006 1.05243  1.08675  0.104253    0.141943    -0.12881    67  PHE   A HZ   
2591 N N    . ASP   B 56  ? 0.52463  0.836326 0.755121 -0.0932901  0.117179    -0.0689384  68  ASP   A N    
2592 C CA   . ASP   B 56  ? 0.544036 0.851425 0.752484 -0.120589   0.11211     -0.0497017  68  ASP   A CA   
2593 C C    . ASP   B 56  ? 0.526068 0.805211 0.745571 -0.127022   0.0819718   -0.0365583  68  ASP   A C    
2594 O O    . ASP   B 56  ? 0.429657 0.674926 0.641292 -0.11067    0.0646288   -0.0441447  68  ASP   A O    
2595 C CB   . ASP   B 56  ? 0.522826 0.804038 0.679354 -0.122355   0.114802    -0.0521614  68  ASP   A CB   
2596 C CG   . ASP   B 56  ? 0.603272 0.871913 0.732417 -0.143548   0.103311    -0.0280704  68  ASP   A CG   
2597 O OD1  . ASP   B 56  ? 0.701245 0.995677 0.835317 -0.165151   0.113496    -0.010778   68  ASP   A OD1  
2598 O OD2  . ASP   B 56  ? 0.623511 0.856844 0.727505 -0.138046   0.0842655   -0.0248795  68  ASP   A OD2  
2599 H H    . ASP   B 56  ? 0.533699 0.821823 0.765164 -0.0820074  0.102545    -0.0712321  68  ASP   A H    
2600 H HA   . ASP   B 56  ? 0.547675 0.888632 0.768637 -0.133937   0.125627    -0.043748   68  ASP   A HA   
2601 H HB2  . ASP   B 56  ? 0.552112 0.851867 0.699664 -0.121237   0.134374    -0.062559   68  ASP   A HB2  
2602 H HB3  . ASP   B 56  ? 0.531788 0.785911 0.679408 -0.109679   0.104744    -0.0603392  68  ASP   A HB3  
2603 N N    . SER   B 57  ? 0.537933 0.828233 0.772323 -0.152712   0.0773485   -0.0180731  69  SER   A N    
2604 C CA   . SER   B 57  ? 0.616835 0.872237 0.858532 -0.16106    0.0491964   -0.00921885 69  SER   A CA   
2605 C C    . SER   B 57  ? 0.646134 0.874104 0.863134 -0.187078   0.0448787   0.0152969   69  SER   A C    
2606 O O    . SER   B 57  ? 0.693378 0.948103 0.905523 -0.20806    0.0642838   0.0299629   69  SER   A O    
2607 C CB   . SER   B 57  ? 0.61798  0.90655  0.911384 -0.167232   0.0414545   -0.0134297  69  SER   A CB   
2608 O OG   . SER   B 57  ? 0.692991 0.945437 0.9894   -0.182891   0.0157368   -0.00643747 69  SER   A OG   
2609 H H    . SER   B 57  ? 0.568536 0.886506 0.807158 -0.16649    0.092642    -0.0116123  69  SER   A H    
2610 H HA   . SER   B 57  ? 0.588499 0.814274 0.814815 -0.144922   0.0370027   -0.0170844  69  SER   A HA   
2611 H HB2  . SER   B 57  ? 0.610568 0.908034 0.914957 -0.14653    0.0391378   -0.0266556  69  SER   A HB2  
2612 H HB3  . SER   B 57  ? 0.636726 0.964318 0.950487 -0.18125    0.0565611   -0.00862869 69  SER   A HB3  
2614 N N    . SER   B 58  ? 0.614667 0.787608 0.81435  -0.184379   0.020068    0.0202342   70  SER   A N    
2615 C CA   . SER   B 58  ? 0.682636 0.817142 0.861326 -0.205878   0.0121583   0.0456462   70  SER   A CA   
2616 C C    . SER   B 58  ? 0.760941 0.918025 0.971856 -0.241934   0.0198035   0.0595707   70  SER   A C    
2617 O O    . SER   B 58  ? 0.88299  1.03795  1.07695  -0.267315   0.0317344   0.0849505   70  SER   A O    
2618 C CB   . SER   B 58  ? 0.690473 0.762427 0.854776 -0.193068   -0.0156792  0.0430546   70  SER   A CB   
2619 O OG   . SER   B 58  ? 0.664683 0.735431 0.859314 -0.188398   -0.0301048  0.0232128   70  SER   A OG   
2620 H H    . SER   B 58  ? 0.613531 0.770789 0.813206 -0.168061   0.00848284  0.00788657  70  SER   A H    
2621 H HA   . SER   B 58  ? 0.697525 0.834717 0.849238 -0.205709   0.0216592   0.0554057   70  SER   A HA   
2622 H HB2  . SER   B 58  ? 0.729308 0.770075 0.883051 -0.207284   -0.0216403  0.0604148   70  SER   A HB2  
2623 H HB3  . SER   B 58  ? 0.678006 0.741333 0.820794 -0.173453   -0.0179467  0.0373722   70  SER   A HB3  
2625 N N    . HIS   B 59  ? 0.71937  0.904871 0.976517 -0.244856   0.0136782   0.0430727   71  HIS   A N    
2626 C CA   . HIS   B 59  ? 0.753142 0.970001 1.05157  -0.281075   0.0177037   0.0506646   71  HIS   A CA   
2627 C C    . HIS   B 59  ? 0.771069 1.05117  1.08052  -0.301028   0.0509174   0.062909    71  HIS   A C    
2628 O O    . HIS   B 59  ? 0.739647 1.03438  1.06619  -0.340514   0.0596879   0.0803426   71  HIS   A O    
2629 C CB   . HIS   B 59  ? 0.717986 0.970234 1.0652   -0.273468   0.00318281  0.0266639   71  HIS   A CB   
2630 C CG   . HIS   B 59  ? 0.726971 0.921424 1.06217  -0.260958   -0.0284141  0.0137151   71  HIS   A CG   
2631 N ND1  . HIS   B 59  ? 0.795579 0.935518 1.12633  -0.286649   -0.0472635  0.0193626   71  HIS   A ND1  
2632 C CD2  . HIS   B 59  ? 0.691463 0.873983 1.01599  -0.226096   -0.04237    -0.00594625 71  HIS   A CD2  
2633 C CE1  . HIS   B 59  ? 0.81234  0.912475 1.13017  -0.265237   -0.0715054  0.00033472  71  HIS   A CE1  
2634 N NE2  . HIS   B 59  ? 0.723317 0.851611 1.03652  -0.2292     -0.0683573  -0.0137471  71  HIS   A NE2  
2635 H H    . HIS   B 59  ? 0.698307 0.885832 0.961347 -0.223977   0.00599997  0.0265254   71  HIS   A H    
2636 H HA   . HIS   B 59  ? 0.789696 0.962674 1.07624  -0.299406   0.007329    0.0637164   71  HIS   A HA   
2637 H HB2  . HIS   B 59  ? 0.688152 0.975284 1.04408  -0.251232   0.0117976   0.0151007   71  HIS   A HB2  
2638 H HB3  . HIS   B 59  ? 0.734398 1.01846  1.11364  -0.299293   0.00697952  0.0304455   71  HIS   A HB3  
2640 H HD2  . HIS   B 59  ? 0.665935 0.870244 0.988761 -0.204018   -0.0347915  -0.0133834  71  HIS   A HD2  
2641 H HE1  . HIS   B 59  ? 0.828307 0.885514 1.13969  -0.274642   -0.087216   -0.00310188 71  HIS   A HE1  
2643 N N    . ASP   B 60  ? 0.804288 1.12082  1.10287  -0.275789   0.070825    0.0520663   72  ASP   A N    
2644 C CA   . ASP   B 60  ? 0.875293 1.24959  1.17357  -0.289305   0.105178    0.0591574   72  ASP   A CA   
2645 C C    . ASP   B 60  ? 0.929459 1.27627  1.18615  -0.32267    0.113787    0.0927739   72  ASP   A C    
2646 O O    . ASP   B 60  ? 0.996977 1.39391  1.2593   -0.348716   0.1417      0.104625    72  ASP   A O    
2647 C CB   . ASP   B 60  ? 0.820506 1.20952  1.09201  -0.256727   0.121456    0.0418754   72  ASP   A CB   
2648 C CG   . ASP   B 60  ? 0.74358  1.16001  1.04823  -0.221648   0.121601    0.0117488   72  ASP   A CG   
2649 O OD1  . ASP   B 60  ? 0.754884 1.21349  1.11414  -0.222826   0.118759    0.00403798  72  ASP   A OD1  
2650 O OD2  . ASP   B 60  ? 0.652066 1.04694  0.927096 -0.194408   0.12357     -0.00266651 72  ASP   A OD2  
2651 H H    . ASP   B 60  ? 0.773605 1.07786  1.06364  -0.249678   0.0635532   0.0381934   72  ASP   A H    
2652 H HA   . ASP   B 60  ? 0.850796 1.27493  1.1912   -0.299179   0.114163    0.0534408   72  ASP   A HA   
2653 H HB2  . ASP   B 60  ? 0.822503 1.16795  1.05631  -0.247753   0.110883    0.0460276   72  ASP   A HB2  
2654 H HB3  . ASP   B 60  ? 0.835236 1.2584   1.10011  -0.268042   0.144322    0.0467566   72  ASP   A HB3  
2655 N N    . ARG   B 61  ? 0.955761 1.2251   1.16813  -0.318448   0.0910507   0.108319    73  ARG   A N    
2656 C CA   . ARG   B 61  ? 1.01817  1.24857  1.18349  -0.343191   0.0940244   0.144579    73  ARG   A CA   
2657 C C    . ARG   B 61  ? 1.09996  1.27177  1.2748   -0.373421   0.0754071   0.165042    73  ARG   A C    
2658 O O    . ARG   B 61  ? 1.17075  1.28856  1.30377  -0.391405   0.07212     0.198731    73  ARG   A O    
2659 C CB   . ARG   B 61  ? 1.03783  1.22535  1.14716  -0.312217   0.0808064   0.14757     73  ARG   A CB   
2660 C CG   . ARG   B 61  ? 0.993781 1.23183  1.08378  -0.291117   0.100523    0.1291      73  ARG   A CG   
2661 C CD   . ARG   B 61  ? 0.977662 1.17937  1.01393  -0.267515   0.0847788   0.134013    73  ARG   A CD   
2662 N NE   . ARG   B 61  ? 0.978396 1.13843  1.02324  -0.237685   0.0571968   0.116095    73  ARG   A NE   
2663 C CZ   . ARG   B 61  ? 0.870221 1.04634  0.937514 -0.213379   0.0560877   0.0825697   73  ARG   A CZ   
2664 N NH1  . ARG   B 61  ? 0.861507 1.08886  0.952773 -0.211949   0.0788602   0.0613755   73  ARG   A NH1  
2665 N NH2  . ARG   B 61  ? 0.788709 0.928101 0.853264 -0.189335   0.0332414   0.0707533   73  ARG   A NH2  
2666 H H    . ARG   B 61  ? 0.932269 1.17262  1.14251  -0.297392   0.0732363   0.0963848   73  ARG   A H    
2667 H HA   . ARG   B 61  ? 1.0432   1.31562  1.20587  -0.360432   0.117569    0.153188    73  ARG   A HA   
2668 H HB2  . ARG   B 61  ? 1.01084  1.16576  1.1264   -0.293321   0.0605282   0.135509    73  ARG   A HB2  
2669 H HB3  . ARG   B 61  ? 1.07941  1.23436  1.1565   -0.324996   0.0776505   0.17401     73  ARG   A HB3  
2670 H HG2  . ARG   B 61  ? 1.01064  1.28503  1.09446  -0.30891    0.122315    0.137847    73  ARG   A HG2  
2671 H HG3  . ARG   B 61  ? 0.947404 1.20816  1.06602  -0.275308   0.102347    0.103944    73  ARG   A HG3  
2672 H HD2  . ARG   B 61  ? 1.03808  1.21372  1.04585  -0.279994   0.0799607   0.161142    73  ARG   A HD2  
2673 H HD3  . ARG   B 61  ? 0.979848 1.2155   1.00128  -0.260641   0.099091    0.12268     73  ARG   A HD3  
2674 H HE   . ARG   B 61  ? 0.979173 1.09903  1.01196  -0.235554   0.0406995   0.129014    73  ARG   A HE   
2675 H HH11 . ARG   B 61  ? 0.867916 1.12539  0.955397 -0.22407    0.0967874   0.0657423   73  ARG   A HH11 
2676 H HH12 . ARG   B 61  ? 0.823465 1.05379  0.933548 -0.197563   0.0762944   0.042914    73  ARG   A HH12 
2677 H HH21 . ARG   B 61  ? 0.827278 0.931091 0.887539 -0.188834   0.0175084   0.0812284   73  ARG   A HH21 
2678 H HH22 . ARG   B 61  ? 0.778348 0.928465 0.845018 -0.174178   0.034779    0.0520641   73  ARG   A HH22 
2679 N N    . ASN   B 62  ? 1.02782  1.20751  1.25496  -0.379324   0.0623711   0.144819    74  ASN   A N    
2680 C CA   . ASN   B 62  ? 1.0532   1.17261  1.2915   -0.407321   0.0417253   0.154582    74  ASN   A CA   
2681 C C    . ASN   B 62  ? 1.09053  1.10818  1.27277  -0.394857   0.0205007   0.175165    74  ASN   A C    
2682 O O    . ASN   B 62  ? 1.1586   1.11754  1.32195  -0.426591   0.0176766   0.204495    74  ASN   A O    
2683 C CB   . ASN   B 62  ? 1.04955  1.20281  1.31653  -0.463531   0.0617446   0.174046    74  ASN   A CB   
2684 H H    . ASN   B 62  ? 0.989377 1.2138   1.24558  -0.365559   0.0661869   0.123354    74  ASN   A H    
2685 H HA   . ASN   B 62  ? 1.01443  1.13955  1.2815   -0.396416   0.0274197   0.1316      74  ASN   A HA   
2688 N N    . GLU   B 63  ? 1.03039  1.02623  1.18741  -0.348467   0.00569732  0.160252    75  GLU   A N    
2689 C CA   . GLU   B 63  ? 1.09881  1.00706  1.21238  -0.328843   -0.0171273  0.174311    75  GLU   A CA   
2690 C C    . GLU   B 63  ? 1.03725  0.941975 1.14683  -0.280416   -0.0339274  0.144105    75  GLU   A C    
2691 O O    . GLU   B 63  ? 0.995187 0.959885 1.11133  -0.261024   -0.0222166  0.125539    75  GLU   A O    
2692 C CB   . GLU   B 63  ? 1.12813  1.01625  1.18782  -0.331937   -0.00822873 0.213256    75  GLU   A CB   
2693 H H    . GLU   B 63  ? 0.991208 1.02827  1.15965  -0.328474   0.0102879   0.140811    75  GLU   A H    
2694 H HA   . GLU   B 63  ? 1.12863  0.990132 1.2499   -0.345318   -0.028705   0.178104    75  GLU   A HA   
2697 N N    . PRO   B 64  ? 1.04549  0.879382 1.14362  -0.260234   -0.0597361  0.137192    76  PRO   A N    
2698 C CA   . PRO   B 64  ? 0.972578 0.808433 1.06481  -0.216393   -0.0724312  0.110187    76  PRO   A CA   
2699 C C    . PRO   B 64  ? 0.95589  0.818705 1.01559  -0.192      -0.0652353  0.119276    76  PRO   A C    
2700 O O    . PRO   B 64  ? 1.00157  0.854748 1.03102  -0.201792   -0.0597031  0.150997    76  PRO   A O    
2701 C CB   . PRO   B 64  ? 1.04017  0.792684 1.12098  -0.201695   -0.0978037  0.106568    76  PRO   A CB   
2702 C CG   . PRO   B 64  ? 1.1419   0.844597 1.23135  -0.243275   -0.100151   0.124246    76  PRO   A CG   
2703 C CD   . PRO   B 64  ? 1.15052  0.898431 1.24055  -0.279232   -0.0756303  0.153245    76  PRO   A CD   
2704 H HA   . PRO   B 64  ? 0.935194 0.80663  1.05146  -0.213287   -0.0697377  0.0879365   76  PRO   A HA   
2705 H HB2  . PRO   B 64  ? 1.06531  0.793931 1.12032  -0.182333   -0.103578   0.118661    76  PRO   A HB2  
2706 H HB3  . PRO   B 64  ? 1.01452  0.770676 1.10835  -0.186728   -0.105877   0.0806685   76  PRO   A HB3  
2707 H HG2  . PRO   B 64  ? 1.19161  0.830395 1.26023  -0.23747    -0.11172    0.136936    76  PRO   A HG2  
2708 H HG3  . PRO   B 64  ? 1.12318  0.829919 1.23801  -0.253551   -0.105218   0.103837    76  PRO   A HG3  
2709 H HD2  . PRO   B 64  ? 1.1929   0.908994 1.2534   -0.282107   -0.0745761  0.180946    76  PRO   A HD2  
2710 H HD3  . PRO   B 64  ? 1.15703  0.911738 1.27121  -0.309928   -0.0712691  0.152306    76  PRO   A HD3  
2711 N N    . PHE   B 65  ? 0.899192 0.796227 0.963391 -0.16292    -0.0657321  0.0914107   77  PHE   A N    
2712 C CA   . PHE   B 65  ? 0.84222  0.765935 0.879381 -0.139814   -0.0626032  0.0920071   77  PHE   A CA   
2713 C C    . PHE   B 65  ? 0.879151 0.759468 0.900527 -0.107607   -0.0856716  0.0894874   77  PHE   A C    
2714 O O    . PHE   B 65  ? 0.822267 0.682078 0.859243 -0.0914485  -0.0971909  0.0657606   77  PHE   A O    
2715 C CB   . PHE   B 65  ? 0.777787 0.759975 0.830765 -0.131629   -0.0476611  0.0629469   77  PHE   A CB   
2716 C CG   . PHE   B 65  ? 0.760269 0.775864 0.788181 -0.114652   -0.0422567  0.0576983   77  PHE   A CG   
2717 C CD1  . PHE   B 65  ? 0.798138 0.852127 0.806637 -0.128556   -0.0244166  0.0689673   77  PHE   A CD1  
2718 C CD2  . PHE   B 65  ? 0.740117 0.754406 0.764448 -0.0876143  -0.0537962  0.0387503   77  PHE   A CD2  
2719 C CE1  . PHE   B 65  ? 0.749939 0.837254 0.734858 -0.116979   -0.0208464  0.0600363   77  PHE   A CE1  
2720 C CE2  . PHE   B 65  ? 0.720557 0.772398 0.725991 -0.0776256  -0.0491832  0.0317307   77  PHE   A CE2  
2721 C CZ   . PHE   B 65  ? 0.708157 0.795196 0.693701 -0.0930583  -0.0337709  0.0413669   77  PHE   A CZ   
2722 H H    . PHE   B 65  ? 0.861176 0.765778 0.945582 -0.159101   -0.0683566  0.0712253   77  PHE   A H    
2723 H HA   . PHE   B 65  ? 0.877656 0.810412 0.896422 -0.151523   -0.0546461  0.113072    77  PHE   A HA   
2724 H HB2  . PHE   B 65  ? 0.767616 0.775816 0.83344  -0.149022   -0.033471   0.0643093   77  PHE   A HB2  
2725 H HB3  . PHE   B 65  ? 0.757534 0.730423 0.825175 -0.121029   -0.055311   0.0447962   77  PHE   A HB3  
2726 H HD1  . PHE   B 65  ? 0.796394 0.856606 0.807697 -0.147536   -0.014101   0.0811856   77  PHE   A HD1  
2727 H HD2  . PHE   B 65  ? 0.736983 0.727627 0.772017 -0.0775662  -0.0643671  0.029411    77  PHE   A HD2  
2728 H HE1  . PHE   B 65  ? 0.761912 0.875296 0.73071  -0.127248   -0.00883814 0.065424    77  PHE   A HE1  
2729 H HE2  . PHE   B 65  ? 0.70424  0.760481 0.710526 -0.0616989  -0.0559476  0.0184147   77  PHE   A HE2  
2730 H HZ   . PHE   B 65  ? 0.71217  0.825495 0.683876 -0.0882186  -0.0318614  0.034348    77  PHE   A HZ   
2731 N N    . VAL   B 66  ? 0.917476 0.788385 0.906902 -0.0969275  -0.0923113  0.114221    78  VAL   A N    
2732 C CA   . VAL   B 66  ? 0.990469 0.826326 0.967063 -0.0620249  -0.114782   0.115617    78  VAL   A CA   
2733 C C    . VAL   B 66  ? 0.956305 0.851154 0.918249 -0.0407794  -0.114254   0.109163    78  VAL   A C    
2734 O O    . VAL   B 66  ? 0.969448 0.907091 0.912797 -0.0559104  -0.101473   0.121064    78  VAL   A O    
2735 C CB   . VAL   B 66  ? 1.08947  0.854844 1.04108  -0.064977   -0.12848    0.154839    78  VAL   A CB   
2736 C CG1  . VAL   B 66  ? 1.11499  0.838392 1.05738  -0.0216058  -0.153429   0.155454    78  VAL   A CG1  
2737 C CG2  . VAL   B 66  ? 1.13951  0.850477 1.10538  -0.0981887  -0.125475   0.161962    78  VAL   A CG2  
2738 H H    . VAL   B 66  ? 0.937908 0.828007 0.912876 -0.110562   -0.0826548  0.130777    78  VAL   A H    
2739 H HA   . VAL   B 66  ? 0.967369 0.787565 0.960809 -0.0507695  -0.121195   0.094747    78  VAL   A HA   
2740 H HB   . VAL   B 66  ? 1.10332  0.888528 1.03336  -0.0745012  -0.122317   0.176788    78  VAL   A HB   
2741 H HG11 . VAL   B 66  ? 1.1001   0.813231 1.06206  -0.00976722 -0.157693   0.129794    78  VAL   A HG11 
2742 H HG12 . VAL   B 66  ? 1.10493  0.867949 1.03759  -0.00413736 -0.156054   0.155947    78  VAL   A HG12 
2743 H HG13 . VAL   B 66  ? 1.1852   0.853359 1.11168  -0.022868   -0.162351   0.180573    78  VAL   A HG13 
2744 H HG21 . VAL   B 66  ? 1.2005   0.857734 1.14873  -0.0995749  -0.134511   0.186429    78  VAL   A HG21 
2745 H HG22 . VAL   B 66  ? 1.11572  0.858848 1.08737  -0.124688   -0.109472   0.166031    78  VAL   A HG22 
2746 H HG23 . VAL   B 66  ? 1.11582  0.814724 1.10239  -0.0920598  -0.13049    0.137439    78  VAL   A HG23 
2747 N N    . PHE   B 67  ? 0.923888 0.824993 0.89493  -0.00761336 -0.127313   0.0876207   79  PHE   A N    
2748 C CA   . PHE   B 67  ? 0.848993 0.809274 0.811214 0.0117559   -0.130086   0.0795605   79  PHE   A CA   
2749 C C    . PHE   B 67  ? 0.895908 0.846188 0.870174 0.05212     -0.149759   0.0653977   79  PHE   A C    
2750 O O    . PHE   B 67  ? 0.89209  0.792992 0.881676 0.0631672   -0.156317   0.0534949   79  PHE   A O    
2751 C CB   . PHE   B 67  ? 0.747475 0.768376 0.721284 -0.00475489 -0.108169   0.0506929   79  PHE   A CB   
2752 C CG   . PHE   B 67  ? 0.702016 0.725022 0.702865 0.00439443  -0.104315   0.0161957   79  PHE   A CG   
2753 C CD1  . PHE   B 67  ? 0.699073 0.687572 0.716192 -0.00769659 -0.0992481  0.00826591  79  PHE   A CD1  
2754 C CD2  . PHE   B 67  ? 0.669163 0.732807 0.677983 0.0232248   -0.105969   -0.00771036 79  PHE   A CD2  
2755 C CE1  . PHE   B 67  ? 0.631686 0.622038 0.665538 0.00133087  -0.0972103  -0.0204098  79  PHE   A CE1  
2756 C CE2  . PHE   B 67  ? 0.627641 0.691493 0.654894 0.0296003   -0.1006     -0.0358955  79  PHE   A CE2  
2757 C CZ   . PHE   B 67  ? 0.628211 0.65331  0.664614 0.0198658   -0.0968667  -0.0411284  79  PHE   A CZ   
2758 H H    . PHE   B 67  ? 0.92004  0.790903 0.904014 0.0020538   -0.134286   0.076104    79  PHE   A H    
2759 H HA   . PHE   B 67  ? 0.890228 0.857228 0.829983 0.00890537  -0.133322   0.102694    79  PHE   A HA   
2760 H HB2  . PHE   B 67  ? 0.748096 0.809089 0.711652 -0.00031326 -0.108277   0.0486216   79  PHE   A HB2  
2761 H HB3  . PHE   B 67  ? 0.750558 0.771463 0.721886 -0.0272408  -0.0953055  0.0571434   79  PHE   A HB3  
2762 H HD1  . PHE   B 67  ? 0.707026 0.672996 0.72279  -0.022921   -0.0977085  0.0230528   79  PHE   A HD1  
2763 H HD2  . PHE   B 67  ? 0.674842 0.768343 0.67581  0.0310106   -0.111054   -0.00421872 79  PHE   A HD2  
2764 H HE1  . PHE   B 67  ? 0.641064 0.611234 0.68395  -0.00648924 -0.096004   -0.0253604  79  PHE   A HE1  
2765 H HE2  . PHE   B 67  ? 0.616296 0.710278 0.648943 0.0397073   -0.0997036  -0.0513552  79  PHE   A HE2  
2766 H HZ   . PHE   B 67  ? 0.605292 0.632234 0.649569 0.0240418   -0.093556   -0.0591335  79  PHE   A HZ   
2767 N N    . SER   B 68  ? 0.836493 0.840362 0.805181 0.0734281   -0.158498   0.0634817   80  SER   A N    
2768 C CA   . SER   B 68  ? 0.851483 0.864239 0.836553 0.114812    -0.175914   0.0490528   80  SER   A CA   
2769 C C    . SER   B 68  ? 0.759205 0.835587 0.769177 0.114818    -0.162547   0.00829083  80  SER   A C    
2770 O O    . SER   B 68  ? 0.739311 0.878873 0.745978 0.0974174   -0.151398   -0.00083772 80  SER   A O    
2771 C CB   . SER   B 68  ? 0.917199 0.954648 0.885272 0.141291    -0.19729    0.0738865   80  SER   A CB   
2772 O OG   . SER   B 68  ? 1.00456  0.962503 0.955049 0.159497    -0.215806   0.10822     80  SER   A OG   
2773 H H    . SER   B 68  ? 0.842339 0.882295 0.797839 0.0616769   -0.153263   0.0698292   80  SER   A H    
2774 H HA   . SER   B 68  ? 0.876524 0.836088 0.867569 0.125987    -0.182456   0.0491964   80  SER   A HA   
2775 H HB2  . SER   B 68  ? 0.905905 0.977477 0.857252 0.123126    -0.19197    0.0833979   80  SER   A HB2  
2776 H HB3  . SER   B 68  ? 0.901093 0.977505 0.886093 0.164228    -0.203897   0.0565698   80  SER   A HB3  
2778 N N    . LEU   B 69  ? 0.760869 0.816431 0.792102 0.131558    -0.162363   -0.0165006  81  LEU   A N    
2779 C CA   . LEU   B 69  ? 0.687753 0.789131 0.737036 0.123688    -0.144952   -0.052043   81  LEU   A CA   
2780 C C    . LEU   B 69  ? 0.681137 0.864248 0.743521 0.139225    -0.147205   -0.0669744  81  LEU   A C    
2781 O O    . LEU   B 69  ? 0.741034 0.937735 0.813493 0.175075    -0.165638   -0.0641327  81  LEU   A O    
2782 C CB   . LEU   B 69  ? 0.688942 0.750019 0.751202 0.13857     -0.144954   -0.0738278  81  LEU   A CB   
2783 C CG   . LEU   B 69  ? 0.685588 0.784003 0.758266 0.12701     -0.125267   -0.105942   81  LEU   A CG   
2784 C CD1  . LEU   B 69  ? 0.628917 0.71921  0.691737 0.089267    -0.107826   -0.103343   81  LEU   A CD1  
2785 C CD2  . LEU   B 69  ? 0.706603 0.772052 0.786957 0.149259    -0.128902   -0.128034   81  LEU   A CD2  
2786 H H    . LEU   B 69  ? 0.790866 0.800514 0.822838 0.147715    -0.172822   -0.0110699  81  LEU   A H    
2787 H HA   . LEU   B 69  ? 0.665541 0.773222 0.70884  0.0968203   -0.131005   -0.052711   81  LEU   A HA   
2788 H HB2  . LEU   B 69  ? 0.717455 0.72766  0.772484 0.128107    -0.146484   -0.0641438  81  LEU   A HB2  
2789 H HB3  . LEU   B 69  ? 0.729421 0.786327 0.798769 0.167461    -0.157253   -0.0762541  81  LEU   A HB3  
2790 H HG   . LEU   B 69  ? 0.655754 0.807535 0.736012 0.130976    -0.12143    -0.115064   81  LEU   A HG   
2791 H HD11 . LEU   B 69  ? 0.624211 0.738117 0.681455 0.0761751   -0.103502   -0.0935576  81  LEU   A HD11 
2792 H HD12 . LEU   B 69  ? 0.612802 0.719331 0.678883 0.0842543   -0.0966839  -0.121005   81  LEU   A HD12 
2793 H HD13 . LEU   B 69  ? 0.650826 0.696859 0.709444 0.0836428   -0.11208    -0.0942013  81  LEU   A HD13 
2794 H HD21 . LEU   B 69  ? 0.730695 0.803066 0.819489 0.176506    -0.13889    -0.131516   81  LEU   A HD21 
2795 H HD22 . LEU   B 69  ? 0.726976 0.740783 0.800291 0.143444    -0.133803   -0.12105    81  LEU   A HD22 
2796 H HD23 . LEU   B 69  ? 0.67979  0.769479 0.762694 0.141806    -0.116125   -0.146293   81  LEU   A HD23 
2797 N N    . GLY   B 70  ? 0.703387 0.9406   0.767717 0.112185    -0.128359   -0.0842665  82  GLY   A N    
2798 C CA   . GLY   B 70  ? 0.728591 1.04958  0.809185 0.117226    -0.127147   -0.103886   82  GLY   A CA   
2799 C C    . GLY   B 70  ? 0.796706 1.16433  0.86692  0.120179    -0.143035   -0.0862391  82  GLY   A C    
2800 O O    . GLY   B 70  ? 0.883896 1.32965  0.970293 0.125082    -0.146951   -0.101734   82  GLY   A O    
2801 H H    . GLY   B 70  ? 0.675263 0.896538 0.731519 0.0892512   -0.115737   -0.0844239  82  GLY   A H    
2802 H HA2  . GLY   B 70  ? 0.69672  1.03716  0.778138 0.0940873   -0.109781   -0.119335   82  GLY   A HA2  
2803 H HA3  . GLY   B 70  ? 0.733734 1.06526  0.831639 0.141266    -0.132775   -0.115215   82  GLY   A HA3  
2804 N N    . LYS   B 71  ? 0.808005 1.1334   0.849997 0.113914    -0.151406   -0.0543335  83  LYS   A N    
2805 C CA   . LYS   B 71  ? 0.85437  1.22013  0.876387 0.115611    -0.167145   -0.0338791  83  LYS   A CA   
2806 C C    . LYS   B 71  ? 0.862189 1.25359  0.8619   0.0722176   -0.14762    -0.039712   83  LYS   A C    
2807 O O    . LYS   B 71  ? 0.960865 1.37083  0.931727 0.0648847   -0.156153   -0.0198851  83  LYS   A O    
2808 C CB   . LYS   B 71  ? 0.926556 1.23002  0.926073 0.137973    -0.188559   0.00730646  83  LYS   A CB   
2809 H H    . LYS   B 71  ? 0.819425 1.09215  0.853232 0.106698    -0.146702   -0.0451064  83  LYS   A H    
2810 H HA   . LYS   B 71  ? 0.858244 1.27855  0.896069 0.131591    -0.176888   -0.0446946  83  LYS   A HA   
2813 N N    . GLY   B 72  ? 0.798276 1.18695  0.808225 0.0456565   -0.121479   -0.0666116  84  GLY   A N    
2814 C CA   . GLY   B 72  ? 0.76383  1.16776  0.756463 0.00733979  -0.0992661  -0.0789961  84  GLY   A CA   
2815 C C    . GLY   B 72  ? 0.753191 1.12418  0.713159 -0.00846291 -0.0948318  -0.0536375  84  GLY   A C    
2816 O O    . GLY   B 72  ? 0.739439 1.1435   0.676891 -0.0311567  -0.0860242  -0.0594085  84  GLY   A O    
2817 H H    . GLY   B 72  ? 0.784138 1.15793  0.811444 0.0533505   -0.117222   -0.0779797  84  GLY   A H    
2818 H HA2  . GLY   B 72  ? 0.734486 1.12116  0.737163 -0.00332231 -0.0831368  -0.0944393  84  GLY   A HA2  
2819 H HA3  . GLY   B 72  ? 0.758546 1.2156   0.751098 0.00078244  -0.101357   -0.0916854  84  GLY   A HA3  
2820 N N    . GLN   B 73  ? 0.710687 1.01849  0.667849 0.00015943  -0.0985895  -0.0284846  85  GLN   A N    
2821 C CA   . GLN   B 73  ? 0.740116 1.01932  0.670831 -0.018312   -0.0903892  -0.00425123 85  GLN   A CA   
2822 C C    . GLN   B 73  ? 0.691857 0.948324 0.631439 -0.0422075  -0.0628784  -0.0195213  85  GLN   A C    
2823 O O    . GLN   B 73  ? 0.7895   1.03967  0.712803 -0.0617672  -0.0484186  -0.00952339 85  GLN   A O    
2824 C CB   . GLN   B 73  ? 0.794913 1.01658  0.720203 -0.00161368 -0.107609   0.0311563   85  GLN   A CB   
2825 C CG   . GLN   B 73  ? 0.857055 1.08986  0.77002  0.0282532   -0.136922   0.0532011   85  GLN   A CG   
2826 C CD   . GLN   B 73  ? 0.863016 1.0207   0.771306 0.0459052   -0.152722   0.0861574   85  GLN   A CD   
2827 O OE1  . GLN   B 73  ? 0.849366 0.950433 0.770231 0.0360048   -0.143629   0.0866291   85  GLN   A OE1  
2828 N NE2  . GLN   B 73  ? 0.906578 1.0608   0.796937 0.0731744   -0.178307   0.113655    85  GLN   A NE2  
2829 H H    . GLN   B 73  ? 0.72535  1.00859  0.697898 0.0166702   -0.105722   -0.0275205  85  GLN   A H    
2830 H HA   . GLN   B 73  ? 0.754609 1.06749  0.664059 -0.0264227  -0.091387   -0.00067219 85  GLN   A HA   
2831 H HB2  . GLN   B 73  ? 0.781957 0.971751 0.727391 0.00552089  -0.107289   0.0243019   85  GLN   A HB2  
2832 H HB3  . GLN   B 73  ? 0.811176 1.01607  0.72054  -0.0179113  -0.0993643  0.0470624   85  GLN   A HB3  
2833 H HG2  . GLN   B 73  ? 0.86215  1.12509  0.750662 0.0206038   -0.139105   0.0635388   85  GLN   A HG2  
2834 H HG3  . GLN   B 73  ? 0.825753 1.08659  0.757307 0.0444243   -0.144043   0.035266    85  GLN   A HG3  
2835 H HE21 . GLN   B 73  ? 0.950477 1.05448  0.835853 0.08436     -0.188004   0.133854    85  GLN   A HE21 
2836 H HE22 . GLN   B 73  ? 0.914366 1.11567  0.797326 0.0806325   -0.186485   0.112136    85  GLN   A HE22 
2837 N N    . VAL   B 74  ? 0.564925 0.813928 0.530129 -0.0389702  -0.0551421  -0.0442471  86  VAL   A N    
2838 C CA   . VAL   B 74  ? 0.533127 0.760954 0.508816 -0.0544436  -0.0328509  -0.0588157  86  VAL   A CA   
2839 C C    . VAL   B 74  ? 0.480533 0.736529 0.462091 -0.061631   -0.0200742  -0.0902032  86  VAL   A C    
2840 O O    . VAL   B 74  ? 0.461402 0.755457 0.444225 -0.0560047  -0.0292891  -0.100357   86  VAL   A O    
2841 C CB   . VAL   B 74  ? 0.529113 0.70822  0.525095 -0.0425911  -0.039652   -0.0522262  86  VAL   A CB   
2842 C CG1  . VAL   B 74  ? 0.588119 0.733998 0.577889 -0.0441487  -0.0490182  -0.0217406  86  VAL   A CG1  
2843 C CG2  . VAL   B 74  ? 0.513296 0.69175  0.522943 -0.0190848  -0.0551026  -0.0623201  86  VAL   A CG2  
2844 H H    . VAL   B 74  ? 0.580491 0.839946 0.556551 -0.0250959  -0.0644831  -0.0518831  86  VAL   A H    
2845 H HA   . VAL   B 74  ? 0.53754  0.76568  0.502341 -0.0677594  -0.022529   -0.0527985  86  VAL   A HA   
2846 H HB   . VAL   B 74  ? 0.512408 0.682722 0.516126 -0.0503974  -0.0268082  -0.0625157  86  VAL   A HB   
2847 H HG11 . VAL   B 74  ? 0.604891 0.752803 0.584579 -0.0342359  -0.062691   -0.00892149 86  VAL   A HG11 
2848 H HG12 . VAL   B 74  ? 0.583103 0.736233 0.565039 -0.0595579  -0.0371797  -0.0161688  86  VAL   A HG12 
2849 H HG13 . VAL   B 74  ? 0.578691 0.694244 0.581742 -0.0402851  -0.0528795  -0.0208082  86  VAL   A HG13 
2850 H HG21 . VAL   B 74  ? 0.516289 0.663836 0.535782 -0.0134347  -0.0579892  -0.0621216  86  VAL   A HG21 
2851 H HG22 . VAL   B 74  ? 0.4998   0.703076 0.512973 -0.0215216  -0.0476258  -0.0805277  86  VAL   A HG22 
2852 H HG23 . VAL   B 74  ? 0.540059 0.72509  0.544713 -0.00724754 -0.0691983  -0.0513122  86  VAL   A HG23 
2853 N N    . ILE   B 75  ? 0.454056 0.691116 0.440334 -0.0738353  0.00065097  -0.104167   87  ILE   A N    
2854 C CA   . ILE   B 75  ? 0.471865 0.721664 0.459586 -0.0841781  0.0152454   -0.131043   87  ILE   A CA   
2855 C C    . ILE   B 75  ? 0.486846 0.736922 0.49115  -0.0699627  0.00622399  -0.138159   87  ILE   A C    
2856 O O    . ILE   B 75  ? 0.454992 0.682066 0.470065 -0.0514232  -0.00742365 -0.126111   87  ILE   A O    
2857 C CB   . ILE   B 75  ? 0.500936 0.718578 0.488027 -0.0946064  0.0380477   -0.139698   87  ILE   A CB   
2858 C CG1  . ILE   B 75  ? 0.496906 0.676046 0.500173 -0.0811733  0.0338171   -0.125663   87  ILE   A CG1  
2859 C CG2  . ILE   B 75  ? 0.508801 0.736915 0.479061 -0.109284   0.0524229   -0.142453   87  ILE   A CG2  
2860 C CD1  . ILE   B 75  ? 0.564654 0.715539 0.571224 -0.0836034  0.0518748   -0.135252   87  ILE   A CD1  
2861 H H    . ILE   B 75  ? 0.464448 0.680006 0.453098 -0.0759634  0.00581143  -0.0960715  87  ILE   A H    
2862 H HA   . ILE   B 75  ? 0.484777 0.765137 0.462253 -0.0936042  0.0164795   -0.139455   87  ILE   A HA   
2863 H HB   . ILE   B 75  ? 0.491644 0.708375 0.478252 -0.100682   0.0468164   -0.154919   87  ILE   A HB   
2864 H HG12 . ILE   B 75  ? 0.514222 0.691527 0.518494 -0.0804252  0.0296888   -0.111835   87  ILE   A HG12 
2865 H HG13 . ILE   B 75  ? 0.50359  0.678755 0.513959 -0.0710154  0.0223131   -0.123612   87  ILE   A HG13 
2866 H HG21 . ILE   B 75  ? 0.513193 0.721061 0.485471 -0.112215   0.0670902   -0.149627   87  ILE   A HG21 
2867 H HG22 . ILE   B 75  ? 0.516856 0.747666 0.485514 -0.105826   0.0456417   -0.125982   87  ILE   A HG22 
2868 H HG23 . ILE   B 75  ? 0.521618 0.774949 0.479816 -0.119363   0.0541128   -0.154159   87  ILE   A HG23 
2869 H HD11 . ILE   B 75  ? 0.543493 0.691596 0.545648 -0.0866708  0.0573049   -0.146955   87  ILE   A HD11 
2870 H HD12 . ILE   B 75  ? 0.536483 0.670051 0.554044 -0.0746144  0.0459436   -0.126473   87  ILE   A HD12 
2871 H HD13 . ILE   B 75  ? 0.550506 0.703433 0.551995 -0.0907608  0.0639483   -0.138566   87  ILE   A HD13 
2872 N N    . LYS   B 76  ? 0.445291 0.722237 0.45028  -0.0816784  0.0160411   -0.160101   88  LYS   A N    
2873 C CA   . LYS   B 76  ? 0.44154  0.737236 0.461475 -0.0721685  0.0114882   -0.170624   88  LYS   A CA   
2874 C C    . LYS   B 76  ? 0.447471 0.696995 0.472428 -0.0594073  0.0132157   -0.165663   88  LYS   A C    
2875 O O    . LYS   B 76  ? 0.436795 0.68999  0.473056 -0.0392942  0.00058705  -0.164904   88  LYS   A O    
2876 C CB   . LYS   B 76  ? 0.465399 0.795279 0.482881 -0.0980272  0.0282702   -0.195224   88  LYS   A CB   
2877 H H    . LYS   B 76  ? 0.46144  0.746336 0.457044 -0.0978907  0.027465    -0.17015    88  LYS   A H    
2878 H HA   . LYS   B 76  ? 0.449319 0.768666 0.476498 -0.0578845  -0.00440568 -0.165061   88  LYS   A HA   
2881 N N    . ALA   B 77  ? 0.430585 0.63904  0.446552 -0.068878   0.0277116   -0.163604   89  ALA   A N    
2882 C CA   . ALA   B 77  ? 0.449909 0.619582 0.467115 -0.0581229  0.0274916   -0.158796   89  ALA   A CA   
2883 C C    . ALA   B 77  ? 0.457817 0.61133  0.485097 -0.038105   0.00633943  -0.144627   89  ALA   A C    
2884 O O    . ALA   B 77  ? 0.402253 0.53749  0.431212 -0.0263764  0.00039224  -0.146808   89  ALA   A O    
2885 C CB   . ALA   B 77  ? 0.434981 0.568502 0.443876 -0.0662909  0.0421051   -0.155416   89  ALA   A CB   
2886 H H    . ALA   B 77  ? 0.444049 0.650455 0.452462 -0.0812514  0.037382    -0.16601    89  ALA   A H    
2887 H HA   . ALA   B 77  ? 0.444901 0.622432 0.461232 -0.0580715  0.0314685   -0.167996   89  ALA   A HA   
2888 H HB1  . ALA   B 77  ? 0.449862 0.583328 0.450063 -0.0788054  0.0562614   -0.164857   89  ALA   A HB1  
2889 H HB2  . ALA   B 77  ? 0.440111 0.571876 0.451526 -0.0671862  0.0407356   -0.14839    89  ALA   A HB2  
2890 H HB3  . ALA   B 77  ? 0.441653 0.554248 0.451075 -0.0577901  0.0388384   -0.151133   89  ALA   A HB3  
2891 N N    . TRP   B 78  ? 0.437348 0.593208 0.467303 -0.0368959  -0.00366846 -0.130403   90  TRP   A N    
2892 C CA   . TRP   B 78  ? 0.47772  0.610054 0.515411 -0.0221993  -0.0230451  -0.116029   90  TRP   A CA   
2893 C C    . TRP   B 78  ? 0.497746 0.642016 0.540999 -0.00175715 -0.0384672  -0.121      90  TRP   A C    
2894 O O    . TRP   B 78  ? 0.466502 0.583144 0.515024 0.0136408   -0.0503145  -0.122147   90  TRP   A O    
2895 C CB   . TRP   B 78  ? 0.515285 0.643483 0.550232 -0.0297875  -0.0270067  -0.0957465  90  TRP   A CB   
2896 C CG   . TRP   B 78  ? 0.513488 0.619968 0.554345 -0.0405512  -0.0194725  -0.0876048  90  TRP   A CG   
2897 C CD1  . TRP   B 78  ? 0.492012 0.598259 0.534625 -0.0484847  -0.00253427 -0.0962292  90  TRP   A CD1  
2898 C CD2  . TRP   B 78  ? 0.50389  0.587354 0.55308  -0.0436743  -0.0293753  -0.0691067  90  TRP   A CD2  
2899 N NE1  . TRP   B 78  ? 0.508792 0.603378 0.564361 -0.0531322  -0.00203519 -0.0855754  90  TRP   A NE1  
2900 C CE2  . TRP   B 78  ? 0.486453 0.568991 0.547168 -0.0536513  -0.0176334  -0.0696232  90  TRP   A CE2  
2901 C CE3  . TRP   B 78  ? 0.534508 0.595906 0.582939 -0.039461   -0.0466314  -0.0519634  90  TRP   A CE3  
2902 C CZ2  . TRP   B 78  ? 0.449286 0.521569 0.525084 -0.0633562  -0.0216503  -0.0553769  90  TRP   A CZ2  
2903 C CZ3  . TRP   B 78  ? 0.523648 0.562602 0.581892 -0.0520616  -0.0497743  -0.0365901  90  TRP   A CZ3  
2904 C CH2  . TRP   B 78  ? 0.50122  0.552103 0.574729 -0.0659293  -0.0366434  -0.0389399  90  TRP   A CH2  
2905 H H    . TRP   B 78  ? 0.451782 0.621565 0.476494 -0.0466909  0.00219409  -0.129666   90  TRP   A H    
2906 H HA   . TRP   B 78  ? 0.475989 0.585304 0.516676 -0.0205975  -0.0232376  -0.116461   90  TRP   A HA   
2907 H HB2  . TRP   B 78  ? 0.50831  0.660806 0.535421 -0.0373964  -0.0206512  -0.0973795  90  TRP   A HB2  
2908 H HB3  . TRP   B 78  ? 0.52436  0.642957 0.560866 -0.0200236  -0.0410985  -0.0861545  90  TRP   A HB3  
2909 H HD1  . TRP   B 78  ? 0.491317 0.604421 0.527907 -0.0506696  0.00763384  -0.107696   90  TRP   A HD1  
2910 H HE1  . TRP   B 78  ? 0.489412 0.583917 0.550123 -0.0551775  0.00667663  -0.0884203  90  TRP   A HE1  
2911 H HE3  . TRP   B 78  ? 0.538616 0.600032 0.580835 -0.0284868  -0.0557868  -0.0508881  90  TRP   A HE3  
2912 H HZ2  . TRP   B 78  ? 0.458477 0.538377 0.546133 -0.068281   -0.0140501  -0.0566536  90  TRP   A HZ2  
2913 H HZ3  . TRP   B 78  ? 0.555491 0.572763 0.610973 -0.0517821  -0.0603977  -0.0237161  90  TRP   A HZ3  
2914 H HH2  . TRP   B 78  ? 0.509129 0.551342 0.593057 -0.0762044  -0.0389486  -0.0293903  90  TRP   A HH2  
2915 N N    . ASP   B 79  ? 0.462701 0.650321 0.505966 9.594e-05   -0.0398295  -0.12536    91  ASP   A N    
2916 C CA   . ASP   B 79  ? 0.450066 0.658704 0.504322 0.0247057   -0.054465   -0.131314   91  ASP   A CA   
2917 C C    . ASP   B 79  ? 0.470933 0.681401 0.531978 0.0324585   -0.0469786  -0.15258    91  ASP   A C    
2918 O O    . ASP   B 79  ? 0.517976 0.714281 0.586397 0.0565705   -0.0587978  -0.157362   91  ASP   A O    
2919 C CB   . ASP   B 79  ? 0.471975 0.740746 0.528754 0.0241586   -0.0577538  -0.134401   91  ASP   A CB   
2920 C CG   . ASP   B 79  ? 0.499457 0.768034 0.54654  0.0312936   -0.075152   -0.109958   91  ASP   A CG   
2921 O OD1  . ASP   B 79  ? 0.585072 0.802201 0.626832 0.0409597   -0.0863563  -0.0894011  91  ASP   A OD1  
2922 O OD2  . ASP   B 79  ? 0.512509 0.831598 0.555045 0.0248856   -0.0774859  -0.11126    91  ASP   A OD2  
2923 H H    . ASP   B 79  ? 0.460514 0.666915 0.497853 -0.0130525  -0.0321165  -0.125829   91  ASP   A H    
2924 H HA   . ASP   B 79  ? 0.482924 0.664801 0.537793 0.0376696   -0.0680794  -0.118989   91  ASP   A HA   
2925 H HB2  . ASP   B 79  ? 0.454728 0.742144 0.506523 0.00405558  -0.0438729  -0.14295    91  ASP   A HB2  
2926 H HB3  . ASP   B 79  ? 0.469479 0.76418  0.538623 0.0387191   -0.0621231  -0.145282   91  ASP   A HB3  
2927 N N    . ILE   B 80  ? 0.490644 0.712007 0.545147 0.0118573   -0.0262799  -0.164971   92  ILE   A N    
2928 C CA   . ILE   B 80  ? 0.492786 0.716413 0.545894 0.0150865   -0.0162286  -0.181878   92  ILE   A CA   
2929 C C    . ILE   B 80  ? 0.455555 0.625962 0.499861 0.0234071   -0.022815   -0.177252   92  ILE   A C    
2930 O O    . ILE   B 80  ? 0.455043 0.619705 0.499964 0.0412111   -0.0285846  -0.188735   92  ILE   A O    
2931 C CB   . ILE   B 80  ? 0.538555 0.779898 0.581534 -0.0122697  0.00824997  -0.19172    92  ILE   A CB   
2932 C CG1  . ILE   B 80  ? 0.541985 0.846601 0.597245 -0.0236249  0.0138571   -0.203538   92  ILE   A CG1  
2933 C CG2  . ILE   B 80  ? 0.636404 0.868296 0.668102 -0.0117619  0.0200405   -0.202347   92  ILE   A CG2  
2934 C CD1  . ILE   B 80  ? 0.588078 0.89518  0.630374 -0.0582257  0.0373503   -0.210785   92  ILE   A CD1  
2935 H H    . ILE   B 80  ? 0.47552  0.700969 0.523899 -0.00473964 -0.017543   -0.16254    92  ILE   A H    
2936 H HA   . ILE   B 80  ? 0.497229 0.747384 0.56109  0.0297614   -0.0213498  -0.190727   92  ILE   A HA   
2937 H HB   . ILE   B 80  ? 0.541764 0.758823 0.575823 -0.0242045  0.0129828   -0.183359   92  ILE   A HB   
2938 H HG12 . ILE   B 80  ? 0.552303 0.887537 0.618403 -0.0139316  0.01356     -0.214436   92  ILE   A HG12 
2939 H HG13 . ILE   B 80  ? 0.548106 0.862811 0.608933 -0.0180058  0.00197953  -0.196316   92  ILE   A HG13 
2940 H HG21 . ILE   B 80  ? 0.610004 0.853721 0.634779 -0.0297724  0.0361411   -0.207675   92  ILE   A HG21 
2941 H HG22 . ILE   B 80  ? 0.612638 0.864901 0.653166 0.00348966  0.0148963   -0.211421   92  ILE   A HG22 
2942 H HG23 . ILE   B 80  ? 0.611416 0.805816 0.632762 -0.00892697 0.0168464   -0.194948   92  ILE   A HG23 
2943 H HD11 . ILE   B 80  ? 0.574413 0.850291 0.606583 -0.0648521  0.0387248   -0.201745   92  ILE   A HD11 
2944 H HD12 . ILE   B 80  ? 0.573809 0.923334 0.6249   -0.0680183  0.0391237   -0.219846   92  ILE   A HD12 
2945 H HD13 . ILE   B 80  ? 0.581616 0.878733 0.616118 -0.0644287  0.0495351   -0.215838   92  ILE   A HD13 
2946 N N    . GLY   B 81  ? 0.426869 0.563299 0.464461 0.0110614   -0.0225329  -0.162806   93  GLY   A N    
2947 C CA   . GLY   B 81  ? 0.444583 0.540885 0.475626 0.0133286   -0.0282229  -0.159629   93  GLY   A CA   
2948 C C    . GLY   B 81  ? 0.462437 0.529671 0.500912 0.0294278   -0.0498034  -0.157265   93  GLY   A C    
2949 O O    . GLY   B 81  ? 0.455745 0.503256 0.48793  0.0385215   -0.0566974  -0.168297   93  GLY   A O    
2950 H H    . GLY   B 81  ? 0.428553 0.57122  0.46654  0.00083305  -0.0187648  -0.155768   93  GLY   A H    
2951 H HA2  . GLY   B 81  ? 0.44597  0.544336 0.467421 0.0136862   -0.0212599  -0.168961   93  GLY   A HA2  
2952 H HA3  . GLY   B 81  ? 0.435181 0.520541 0.465049 0.00257279  -0.024208   -0.150325   93  GLY   A HA3  
2953 N N    . VAL   B 82  ? 0.446829 0.507913 0.494715 0.031214    -0.0601702  -0.142813   94  VAL   A N    
2954 C CA   . VAL   B 82  ? 0.491134 0.513195 0.543928 0.0427138   -0.0795819  -0.137204   94  VAL   A CA   
2955 C C    . VAL   B 82  ? 0.532407 0.553933 0.586936 0.0701839   -0.0883031  -0.154676   94  VAL   A C    
2956 O O    . VAL   B 82  ? 0.509213 0.488873 0.56269  0.0811433   -0.101702   -0.161549   94  VAL   A O    
2957 C CB   . VAL   B 82  ? 0.487303 0.498612 0.543723 0.0349105   -0.0861788  -0.112182   94  VAL   A CB   
2958 C CG1  . VAL   B 82  ? 0.624584 0.585226 0.683014 0.045039    -0.105673   -0.103464   94  VAL   A CG1  
2959 C CG2  . VAL   B 82  ? 0.496229 0.50833  0.554016 0.0100172   -0.0760854  -0.0997733  94  VAL   A CG2  
2960 H H    . VAL   B 82  ? 0.44549  0.524663 0.494306 0.0240324   -0.05478    -0.13601    94  VAL   A H    
2961 H HA   . VAL   B 82  ? 0.493086 0.493881 0.544427 0.0366829   -0.0822957  -0.138868   94  VAL   A HA   
2962 H HB   . VAL   B 82  ? 0.50539  0.543268 0.56096  0.0392733   -0.0837201  -0.109783   94  VAL   A HB   
2963 H HG11 . VAL   B 82  ? 0.602628 0.540119 0.662156 0.0417356   -0.109314   -0.111504   94  VAL   A HG11 
2964 H HG12 . VAL   B 82  ? 0.611208 0.57185  0.669805 0.064695    -0.112377   -0.108831   94  VAL   A HG12 
2965 H HG13 . VAL   B 82  ? 0.604541 0.555378 0.662232 0.0348091   -0.10765    -0.0847559  94  VAL   A HG13 
2966 H HG21 . VAL   B 82  ? 0.497901 0.505884 0.555805 0.00368046  -0.0783507  -0.0840917  94  VAL   A HG21 
2967 H HG22 . VAL   B 82  ? 0.465811 0.502853 0.520699 0.00443119  -0.0633986  -0.105061   94  VAL   A HG22 
2968 H HG23 . VAL   B 82  ? 0.492052 0.484955 0.553367 0.00599952  -0.07974    -0.102632   94  VAL   A HG23 
2969 N N    . ALA   B 83  ? 0.506354 0.576408 0.565239 0.0806546   -0.0800005  -0.1651     95  ALA   A N    
2970 C CA   . ALA   B 83  ? 0.514489 0.596502 0.580064 0.109646    -0.0849088  -0.185374   95  ALA   A CA   
2971 C C    . ALA   B 83  ? 0.532315 0.602774 0.586166 0.112424    -0.0786941  -0.208468   95  ALA   A C    
2972 O O    . ALA   B 83  ? 0.580394 0.650094 0.637371 0.137759    -0.0831207  -0.228103   95  ALA   A O    
2973 C CB   . ALA   B 83  ? 0.532657 0.683813 0.611413 0.117626    -0.0762042  -0.194035   95  ALA   A CB   
2974 H H    . ALA   B 83  ? 0.486116 0.58416  0.545246 0.0693888   -0.0708804  -0.161027   95  ALA   A H    
2975 H HA   . ALA   B 83  ? 0.552826 0.605023 0.6221   0.124438    -0.0993546  -0.179417   95  ALA   A HA   
2976 H HB1  . ALA   B 83  ? 0.520571 0.681867 0.603971 0.116433    -0.0820525  -0.179999   95  ALA   A HB1  
2977 H HB2  . ALA   B 83  ? 0.500853 0.677067 0.575052 0.10109     -0.0610279  -0.200492   95  ALA   A HB2  
2978 H HB3  . ALA   B 83  ? 0.539549 0.701477 0.626583 0.140017    -0.0798998  -0.207724   95  ALA   A HB3  
2979 N N    . THR   B 84  ? 0.551701 0.617219 0.59037  0.0892516   -0.0680249  -0.206982   96  THR   A N    
2980 C CA   . THR   B 84  ? 0.545191 0.601635 0.565056 0.0907161   -0.0638071  -0.225616   96  THR   A CA   
2981 C C    . THR   B 84  ? 0.59646  0.598254 0.609723 0.0897883   -0.0822805  -0.225615   96  THR   A C    
2982 O O    . THR   B 84  ? 0.560431 0.552909 0.554709 0.0907999   -0.0831156  -0.241886   96  THR   A O    
2983 C CB   . THR   B 84  ? 0.52017  0.596761 0.522593 0.0684801   -0.0447832  -0.221307   96  THR   A CB   
2984 O OG1  . THR   B 84  ? 0.490648 0.541548 0.492274 0.051058    -0.0493165  -0.201218   96  THR   A OG1  
2985 C CG2  . THR   B 84  ? 0.508818 0.634623 0.517108 0.0593828   -0.0248917  -0.22147    96  THR   A CG2  
2986 H H    . THR   B 84  ? 0.517964 0.586782 0.556406 0.0732822   -0.0633482  -0.193832   96  THR   A H    
2987 H HA   . THR   B 84  ? 0.566693 0.639908 0.587714 0.106752    -0.061161   -0.242205   96  THR   A HA   
2988 H HB   . THR   B 84  ? 0.535231 0.60975  0.521296 0.0714936   -0.0419732  -0.233247   96  THR   A HB   
2990 H HG21 . THR   B 84  ? 0.501822 0.62994  0.495568 0.0451341   -0.0126048  -0.218753   96  THR   A HG21 
2991 H HG22 . THR   B 84  ? 0.491739 0.62207  0.512681 0.0550615   -0.0276728  -0.210638   96  THR   A HG22 
2992 H HG23 . THR   B 84  ? 0.513857 0.665268 0.527391 0.0714943   -0.0215203  -0.235716   96  THR   A HG23 
2993 N N    . MET   B 85  ? 0.612056 0.581038 0.638323 0.0832504   -0.0961576  -0.207155   97  MET   A N    
2994 C CA   . MET   B 85  ? 0.623722 0.549809 0.647308 0.0709841   -0.110988   -0.205298   97  MET   A CA   
2995 C C    . MET   B 85  ? 0.643318 0.519535 0.66843  0.0862343   -0.128789   -0.218459   97  MET   A C    
2996 O O    . MET   B 85  ? 0.623976 0.489832 0.657362 0.106234    -0.132478   -0.216914   97  MET   A O    
2997 C CB   . MET   B 85  ? 0.600405 0.521222 0.638049 0.0483009   -0.11246    -0.177615   97  MET   A CB   
2998 C CG   . MET   B 85  ? 0.548777 0.507068 0.58441  0.0340985   -0.0955388  -0.167159   97  MET   A CG   
2999 S SD   . MET   B 85  ? 0.550601 0.509458 0.605044 0.0121077   -0.0938632  -0.139321   97  MET   A SD   
3000 C CE   . MET   B 85  ? 0.583658 0.51463  0.64748  -0.00109378 -0.112104   -0.141662   97  MET   A CE   
3001 H H    . MET   B 85  ? 0.599518 0.575273 0.636058 0.0848637   -0.0963858  -0.195603   97  MET   A H    
3002 H HA   . MET   B 85  ? 0.616791 0.549673 0.62767  0.0666017   -0.108418   -0.214663   97  MET   A HA   
3003 H HB2  . MET   B 85  ? 0.602611 0.518845 0.648072 0.0517899   -0.114042   -0.166633   97  MET   A HB2  
3004 H HB3  . MET   B 85  ? 0.616401 0.512681 0.656506 0.0393106   -0.122962   -0.177664   97  MET   A HB3  
3005 H HG2  . MET   B 85  ? 0.555523 0.515295 0.581986 0.0315092   -0.0955478  -0.174209   97  MET   A HG2  
3006 H HG3  . MET   B 85  ? 0.540877 0.522327 0.573227 0.0395509   -0.0847458  -0.169273   97  MET   A HG3  
3007 H HE1  . MET   B 85  ? 0.573789 0.50965  0.651159 -0.0144977  -0.110688   -0.128029   97  MET   A HE1  
3008 H HE2  . MET   B 85  ? 0.609788 0.513519 0.672544 0.00285829  -0.123172   -0.148149   97  MET   A HE2  
3009 H HE3  . MET   B 85  ? 0.578083 0.517927 0.634403 0.00053158  -0.112389   -0.15067    97  MET   A HE3  
3010 N N    . LYS   B 86  ? 0.688275 0.531573 0.705147 0.076372    -0.141251   -0.231144   98  LYS   A N    
3011 C CA   . LYS   B 86  ? 0.800961 0.58554  0.815765 0.0857258   -0.158163   -0.248035   98  LYS   A CA   
3012 C C    . LYS   B 86  ? 0.786013 0.530126 0.814742 0.0586484   -0.171192   -0.227432   98  LYS   A C    
3013 O O    . LYS   B 86  ? 0.688962 0.460495 0.727887 0.0343697   -0.167123   -0.207635   98  LYS   A O    
3014 C CB   . LYS   B 86  ? 0.86016  0.63796  0.852061 0.0901008   -0.16303    -0.283318   98  LYS   A CB   
3015 C CG   . LYS   B 86  ? 0.909209 0.736763 0.882009 0.106888    -0.146228   -0.301585   98  LYS   A CG   
3016 C CD   . LYS   B 86  ? 1.04578  0.87183  1.01758  0.141807    -0.14059    -0.325829   98  LYS   A CD   
3017 C CE   . LYS   B 86  ? 1.09827  0.982699 1.05223  0.151532    -0.120212   -0.342742   98  LYS   A CE   
3018 N NZ   . LYS   B 86  ? 1.16486  1.05178  1.08575  0.136739    -0.121995   -0.357696   98  LYS   A NZ   
3019 H H    . LYS   B 86  ? 0.679916 0.536765 0.69191  0.0631094   -0.139863   -0.229954   98  LYS   A H    
3020 H HA   . LYS   B 86  ? 0.803771 0.579877 0.822351 0.106087    -0.157533   -0.249765   98  LYS   A HA   
3021 H HB2  . LYS   B 86  ? 0.863584 0.641817 0.853509 0.0700588   -0.169201   -0.280566   98  LYS   A HB2  
3022 H HB3  . LYS   B 86  ? 0.915676 0.652455 0.905289 0.100143    -0.172357   -0.298556   98  LYS   A HB3  
3023 H HG2  . LYS   B 86  ? 0.871727 0.734327 0.849538 0.101145    -0.134774   -0.284466   98  LYS   A HG2  
3024 H HG3  . LYS   B 86  ? 0.929009 0.759071 0.884013 0.0996779   -0.149419   -0.314935   98  LYS   A HG3  
3025 H HD2  . LYS   B 86  ? 1.08232  0.868666 1.04748  0.149182    -0.151192   -0.345129   98  LYS   A HD2  
3026 H HD3  . LYS   B 86  ? 1.02514  0.852157 1.01471  0.150822    -0.139501   -0.311407   98  LYS   A HD3  
3027 H HE2  . LYS   B 86  ? 1.11675  1.00494  1.07229  0.174655    -0.116232   -0.361751   98  LYS   A HE2  
3028 H HE3  . LYS   B 86  ? 1.05214  0.97151  1.01377  0.144481    -0.109081   -0.324897   98  LYS   A HE3  
3029 H HZ1  . LYS   B 86  ? 1.17768  1.02895  1.09353  0.134964    -0.135858   -0.369641   98  LYS   A HZ1  
3030 H HZ2  . LYS   B 86  ? 1.11578  1.01681  1.03496  0.119526    -0.120326   -0.339466   98  LYS   A HZ2  
3031 H HZ3  . LYS   B 86  ? 1.1562   1.06769  1.0618   0.146755    -0.110818   -0.373979   98  LYS   A HZ3  
3032 N N    . LYS   B 87  ? 0.863027 0.541196 0.892747 0.0630494   -0.185234   -0.232284   99  LYS   A N    
3033 C CA   . LYS   B 87  ? 0.958909 0.593151 1.00065  0.0326133   -0.195986   -0.212524   99  LYS   A CA   
3034 C C    . LYS   B 87  ? 0.948179 0.599443 0.993902 0.00094407  -0.202688   -0.223183   99  LYS   A C    
3035 O O    . LYS   B 87  ? 0.901064 0.556187 0.9318   0.00511899  -0.209208   -0.254546   99  LYS   A O    
3036 C CB   . LYS   B 87  ? 1.10442  0.652511 1.141    0.0433225   -0.209598   -0.218169   99  LYS   A CB   
3037 C CG   . LYS   B 87  ? 1.20299  0.694626 1.249    0.00979014  -0.21824    -0.192175   99  LYS   A CG   
3038 C CD   . LYS   B 87  ? 1.38503  0.789541 1.42129  0.031294    -0.227533   -0.18539    99  LYS   A CD   
3039 C CE   . LYS   B 87  ? 1.55254  0.86638  1.58726  0.00011296  -0.240463   -0.181451   99  LYS   A CE   
3040 N NZ   . LYS   B 87  ? 1.57979  0.907836 1.62895  -0.0465747  -0.235714   -0.14536    99  LYS   A NZ   
3041 H H    . LYS   B 87  ? 0.904293 0.563411 0.927108 0.0851462   -0.187246   -0.248348   99  LYS   A H    
3042 H HA   . LYS   B 87  ? 0.92657  0.579743 0.977495 0.0254889   -0.189133   -0.186479   99  LYS   A HA   
3043 H HB2  . LYS   B 87  ? 1.1065   0.653355 1.14113  0.0693125   -0.206225   -0.212536   99  LYS   A HB2  
3044 H HB3  . LYS   B 87  ? 1.13443  0.661218 1.16121  0.0491646   -0.216082   -0.246822   99  LYS   A HB3  
3045 H HG2  . LYS   B 87  ? 1.22743  0.707199 1.27594  -0.0132583  -0.22531    -0.205692   99  LYS   A HG2  
3046 H HG3  . LYS   B 87  ? 1.17161  0.695723 1.22681  -0.0032204  -0.210424   -0.166144   99  LYS   A HG3  
3047 H HD2  . LYS   B 87  ? 1.36303  0.779777 1.40081  0.0407464   -0.22252    -0.158929   99  LYS   A HD2  
3048 H HD3  . LYS   B 87  ? 1.39391  0.789154 1.42179  0.0606846   -0.229526   -0.209824   99  LYS   A HD3  
3049 H HE2  . LYS   B 87  ? 1.6007   0.856341 1.62634  0.0195659   -0.24563    -0.175384   99  LYS   A HE2  
3050 H HE3  . LYS   B 87  ? 1.56383  0.864234 1.59607  -0.00885484 -0.247012   -0.210767   99  LYS   A HE3  
3051 H HZ1  . LYS   B 87  ? 1.5421   0.889756 1.59103  -0.039108   -0.228661   -0.119604   99  LYS   A HZ1  
3052 H HZ2  . LYS   B 87  ? 1.52036  0.897031 1.58021  -0.064311   -0.232694   -0.153173   99  LYS   A HZ2  
3053 H HZ3  . LYS   B 87  ? 1.62548  0.895262 1.67295  -0.0657642  -0.242446   -0.141052   99  LYS   A HZ3  
3054 N N    . GLY   B 88  ? 0.898562 0.57178  0.964645 -0.0291042  -0.200011   -0.196328   100 GLY   A N    
3055 C CA   . GLY   B 88  ? 0.85133  0.551933 0.930253 -0.0583056  -0.207817   -0.202601   100 GLY   A CA   
3056 C C    . GLY   B 88  ? 0.772477 0.54305  0.848118 -0.0499815  -0.199183   -0.204768   100 GLY   A C    
3057 O O    . GLY   B 88  ? 0.785126 0.588041 0.873444 -0.0685287  -0.206587   -0.206565   100 GLY   A O    
3058 H H    . GLY   B 88  ? 0.883631 0.558783 0.956424 -0.0306751  -0.193248   -0.173982   100 GLY   A H    
3059 H HA2  . GLY   B 88  ? 0.85503  0.55614  0.952004 -0.0803209  -0.206911   -0.183656   100 GLY   A HA2  
3060 H HA3  . GLY   B 88  ? 0.897761 0.569299 0.969696 -0.0630852  -0.220565   -0.224445   100 GLY   A HA3  
3061 N N    . GLU   B 89  ? 0.759224 0.553541 0.819355 -0.0232144  -0.183947   -0.203133   101 GLU   A N    
3062 C CA   . GLU   B 89  ? 0.714459 0.562795 0.76666  -0.0163477  -0.173239   -0.201554   101 GLU   A CA   
3063 C C    . GLU   B 89  ? 0.671022 0.554492 0.747856 -0.0315634  -0.162716   -0.173363   101 GLU   A C    
3064 O O    . GLU   B 89  ? 0.678429 0.555506 0.768209 -0.0371756  -0.15405    -0.153565   101 GLU   A O    
3065 C CB   . GLU   B 89  ? 0.725501 0.58645  0.756508 0.0101344   -0.157587   -0.207915   101 GLU   A CB   
3066 C CG   . GLU   B 89  ? 0.628532 0.532349 0.642918 0.0158013   -0.144788   -0.207201   101 GLU   A CG   
3067 C CD   . GLU   B 89  ? 0.599864 0.518759 0.596199 0.0353018   -0.127426   -0.215056   101 GLU   A CD   
3068 O OE1  . GLU   B 89  ? 0.633318 0.539063 0.617198 0.0522939   -0.129006   -0.2373     101 GLU   A OE1  
3069 O OE2  . GLU   B 89  ? 0.55391  0.50128  0.550702 0.0331291   -0.110203   -0.200032   101 GLU   A OE2  
3070 H H    . GLU   B 89  ? 0.765252 0.540814 0.819876 -0.00933674 -0.180161   -0.202367   101 GLU   A H    
3071 H HA   . GLU   B 89  ? 0.73148  0.585782 0.775857 -0.019762   -0.182954   -0.215477   101 GLU   A HA   
3072 H HB2  . GLU   B 89  ? 0.733623 0.573208 0.752114 0.0213844   -0.163031   -0.226727   101 GLU   A HB2  
3073 H HB3  . GLU   B 89  ? 0.68902  0.550276 0.728742 0.0129029   -0.149642   -0.194178   101 GLU   A HB3  
3074 H HG2  . GLU   B 89  ? 0.610458 0.532152 0.637248 0.0074098   -0.138566   -0.189964   101 GLU   A HG2  
3075 H HG3  . GLU   B 89  ? 0.654135 0.559634 0.656488 0.0141618   -0.153733   -0.218721   101 GLU   A HG3  
3076 N N    . ILE   B 90  ? 0.647929 0.568603 0.729798 -0.0367075  -0.164554   -0.172134   102 ILE   A N    
3077 C CA   . ILE   B 90  ? 0.595264 0.554176 0.694484 -0.03973    -0.149386   -0.150573   102 ILE   A CA   
3078 C C    . ILE   B 90  ? 0.589006 0.565708 0.662984 -0.0203469  -0.135977   -0.151691   102 ILE   A C    
3079 O O    . ILE   B 90  ? 0.549727 0.530887 0.602396 -0.012102   -0.144576   -0.163586   102 ILE   A O    
3080 C CB   . ILE   B 90  ? 0.606317 0.596542 0.737031 -0.0570306  -0.159466   -0.144508   102 ILE   A CB   
3081 C CG1  . ILE   B 90  ? 0.63246  0.603807 0.788656 -0.0842453  -0.170597   -0.14309    102 ILE   A CG1  
3082 C CG2  . ILE   B 90  ? 0.528103 0.557401 0.676666 -0.0533944  -0.141238   -0.125721   102 ILE   A CG2  
3083 C CD1  . ILE   B 90  ? 0.632039 0.640078 0.822596 -0.105766   -0.185213   -0.144905   102 ILE   A CD1  
3084 H H    . ILE   B 90  ? 0.66355  0.585378 0.737064 -0.0367521  -0.175896   -0.185542   102 ILE   A H    
3085 H HA   . ILE   B 90  ? 0.592759 0.546098 0.699455 -0.0431379  -0.140105   -0.139303   102 ILE   A HA   
3086 H HB   . ILE   B 90  ? 0.60709  0.605275 0.728998 -0.0527938  -0.171175   -0.1554     102 ILE   A HB   
3087 H HG12 . ILE   B 90  ? 0.621333 0.589427 0.785824 -0.0896415  -0.158724   -0.128556   102 ILE   A HG12 
3088 H HG13 . ILE   B 90  ? 0.65989  0.596427 0.801156 -0.0835171  -0.179646   -0.155608   102 ILE   A HG13 
3089 H HG21 . ILE   B 90  ? 0.539096 0.592738 0.713277 -0.0635949  -0.146749   -0.122014   102 ILE   A HG21 
3090 H HG22 . ILE   B 90  ? 0.528715 0.551599 0.678733 -0.0555893  -0.128171   -0.116711   102 ILE   A HG22 
3091 H HG23 . ILE   B 90  ? 0.531869 0.568327 0.664118 -0.0385797  -0.136913   -0.127129   102 ILE   A HG23 
3092 H HD11 . ILE   B 90  ? 0.648898 0.660257 0.829278 -0.101579   -0.199775   -0.159936   102 ILE   A HD11 
3093 H HD12 . ILE   B 90  ? 0.655024 0.647928 0.86079  -0.126751   -0.189201   -0.142817   102 ILE   A HD12 
3094 H HD13 . ILE   B 90  ? 0.607423 0.652447 0.815164 -0.103175   -0.176186   -0.133653   102 ILE   A HD13 
3095 N N    . ALA   B 91  ? 0.487912 0.473622 0.561968 -0.0162348  -0.11487    -0.138827   103 ALA   A N    
3096 C CA   . ALA   B 91  ? 0.497177 0.493731 0.548235 -0.00394745 -0.0987315  -0.138456   103 ALA   A CA   
3097 C C    . ALA   B 91  ? 0.460574 0.475916 0.526177 -0.00704827 -0.0821926  -0.122274   103 ALA   A C    
3098 O O    . ALA   B 91  ? 0.470387 0.494487 0.560771 -0.0174972  -0.0785252  -0.112591   103 ALA   A O    
3099 C CB   . ALA   B 91  ? 0.473398 0.461848 0.505935 0.00408468  -0.0879684  -0.147125   103 ALA   A CB   
3100 H H    . ALA   B 91  ? 0.503034 0.486935 0.590049 -0.0231014  -0.110465   -0.13033    103 ALA   A H    
3101 H HA   . ALA   B 91  ? 0.499948 0.498117 0.537372 0.00121475  -0.105616   -0.144049   103 ALA   A HA   
3102 H HB1  . ALA   B 91  ? 0.498863 0.4758   0.52252  0.00920079  -0.0973001  -0.159508   103 ALA   A HB1  
3103 H HB2  . ALA   B 91  ? 0.470664 0.459138 0.51472  0.00038087  -0.0837919  -0.140964   103 ALA   A HB2  
3104 H HB3  . ALA   B 91  ? 0.47438  0.470849 0.492534 0.00778896  -0.0758964  -0.146894   103 ALA   A HB3  
3105 N N    . HIS   B 92  ? 0.490373 0.508401 0.537288 0.00211226  -0.0716463  -0.119864   104 HIS   A N    
3106 C CA   . HIS   B 92  ? 0.461406 0.485927 0.513738 0.0034718   -0.0526822  -0.109167   104 HIS   A CA   
3107 C C    . HIS   B 92  ? 0.474801 0.488607 0.501711 0.00224325  -0.032247   -0.113269   104 HIS   A C    
3108 O O    . HIS   B 92  ? 0.46869  0.473539 0.467999 0.00591851  -0.0311578  -0.12002    104 HIS   A O    
3109 C CB   . HIS   B 92  ? 0.450213 0.477648 0.499664 0.0162088   -0.0572863  -0.101496   104 HIS   A CB   
3110 C CG   . HIS   B 92  ? 0.460208 0.513205 0.543863 0.0163065   -0.0754745  -0.0978333  104 HIS   A CG   
3111 N ND1  . HIS   B 92  ? 0.474258 0.541114 0.56365  0.0312757   -0.0847913  -0.0903187  104 HIS   A ND1  
3112 C CD2  . HIS   B 92  ? 0.475436 0.544553 0.589344 0.00218979  -0.087114   -0.100427   104 HIS   A CD2  
3113 C CE1  . HIS   B 92  ? 0.496217 0.597123 0.624655 0.0256042   -0.101039   -0.09058    104 HIS   A CE1  
3114 N NE2  . HIS   B 92  ? 0.501617 0.601701 0.64439  0.00494399  -0.101882   -0.0968277  104 HIS   A NE2  
3115 H H    . HIS   B 92  ? 0.493601 0.505738 0.520724 0.00795612  -0.0760541  -0.125539   104 HIS   A H    
3116 H HA   . HIS   B 92  ? 0.449781 0.484383 0.523527 -0.00318179 -0.0498039  -0.104861   104 HIS   A HA   
3117 H HB2  . HIS   B 92  ? 0.476046 0.493722 0.501039 0.0215373   -0.0624248  -0.104344   104 HIS   A HB2  
3118 H HB3  . HIS   B 92  ? 0.459452 0.481997 0.506623 0.0197036   -0.0423804  -0.0961807  104 HIS   A HB3  
3120 H HD2  . HIS   B 92  ? 0.468297 0.529748 0.584305 -0.00801517 -0.0856171  -0.103236   104 HIS   A HD2  
3121 H HE1  . HIS   B 92  ? 0.502131 0.62467  0.645187 0.0346355   -0.111372   -0.086602   104 HIS   A HE1  
3123 N N    . LEU   B 93  ? 0.439405 0.458816 0.475526 -0.00516041 -0.0151575  -0.110498   105 LEU   A N    
3124 C CA   . LEU   B 93  ? 0.448458 0.464566 0.466206 -0.01195    0.00423016  -0.116559   105 LEU   A CA   
3125 C C    . LEU   B 93  ? 0.47954  0.485642 0.49609  -0.0133332  0.023417    -0.112782   105 LEU   A C    
3126 O O    . LEU   B 93  ? 0.504654 0.52101  0.543332 -0.0123697  0.0251667   -0.108246   105 LEU   A O    
3127 C CB   . LEU   B 93  ? 0.438916 0.472807 0.466406 -0.0203722  0.00367751  -0.120658   105 LEU   A CB   
3128 C CG   . LEU   B 93  ? 0.480364 0.518244 0.508365 -0.0153119  -0.0124122  -0.126467   105 LEU   A CG   
3129 C CD1  . LEU   B 93  ? 0.483277 0.537743 0.519041 -0.0197108  -0.0127066  -0.125553   105 LEU   A CD1  
3130 C CD2  . LEU   B 93  ? 0.498973 0.536071 0.505753 -0.0102514  -0.00880921 -0.138108   105 LEU   A CD2  
3131 H H    . LEU   B 93  ? 0.438852 0.467363 0.493725 -0.00761971 -0.0155898  -0.105761   105 LEU   A H    
3132 H HA   . LEU   B 93  ? 0.464054 0.473292 0.463428 -0.0100115  0.00514575  -0.120738   105 LEU   A HA   
3133 H HB2  . LEU   B 93  ? 0.439706 0.479717 0.48217  -0.0232862  0.00251545  -0.11467    105 LEU   A HB2  
3134 H HB3  . LEU   B 93  ? 0.446542 0.484703 0.465326 -0.0267968  0.016759    -0.125356   105 LEU   A HB3  
3135 H HG   . LEU   B 93  ? 0.479201 0.509789 0.51601  -0.0119365  -0.0256162  -0.12323    105 LEU   A HG   
3136 H HD11 . LEU   B 93  ? 0.476712 0.532291 0.522228 -0.0247129  -0.0131598  -0.116965   105 LEU   A HD11 
3137 H HD12 . LEU   B 93  ? 0.485247 0.537845 0.522731 -0.012764   -0.0239111  -0.128284   105 LEU   A HD12 
3138 H HD13 . LEU   B 93  ? 0.477151 0.543798 0.505534 -0.0244098  -0.00138049 -0.130883   105 LEU   A HD13 
3139 H HD21 . LEU   B 93  ? 0.506946 0.532488 0.504835 -0.00635982 -0.011634   -0.136719   105 LEU   A HD21 
3140 H HD22 . LEU   B 93  ? 0.496025 0.540435 0.495046 -0.0168537  0.00526303  -0.141197   105 LEU   A HD22 
3141 H HD23 . LEU   B 93  ? 0.498422 0.540366 0.507475 -0.00459836 -0.0173396  -0.144287   105 LEU   A HD23 
3142 N N    . LEU   B 94  ? 0.516852 0.50013  0.507109 -0.0150008  0.0383192   -0.114652   106 LEU   A N    
3143 C CA   . LEU   B 94  ? 0.524143 0.4852   0.50748  -0.0179768  0.0596011   -0.115048   106 LEU   A CA   
3144 C C    . LEU   B 94  ? 0.538459 0.501405 0.506691 -0.0391824  0.0770236   -0.128412   106 LEU   A C    
3145 O O    . LEU   B 94  ? 0.567159 0.531382 0.517387 -0.0483103  0.0799527   -0.133012   106 LEU   A O    
3146 C CB   . LEU   B 94  ? 0.562972 0.486255 0.526137 -0.00437049 0.0627722   -0.103967   106 LEU   A CB   
3147 C CG   . LEU   B 94  ? 0.635815 0.520416 0.588765 -0.00329497 0.0850675   -0.104231   106 LEU   A CG   
3148 C CD1  . LEU   B 94  ? 0.630269 0.530226 0.616286 0.0115921   0.0841387   -0.104065   106 LEU   A CD1  
3149 C CD2  . LEU   B 94  ? 0.673384 0.508985 0.592605 0.00670867  0.089052    -0.089887   106 LEU   A CD2  
3150 H H    . LEU   B 94  ? 0.518462 0.497268 0.493141 -0.0150324  0.0361219   -0.116209   106 LEU   A H    
3151 H HA   . LEU   B 94  ? 0.518914 0.49031  0.520933 -0.0154185  0.0602737   -0.114539   106 LEU   A HA   
3152 H HB2  . LEU   B 94  ? 0.567636 0.498694 0.543425 0.00950254  0.0487103   -0.0964191  106 LEU   A HB2  
3153 H HB3  . LEU   B 94  ? 0.583441 0.498224 0.525305 -0.00861191 0.0628369   -0.103289   106 LEU   A HB3  
3154 H HG   . LEU   B 94  ? 0.627393 0.51043  0.573159 -0.0204911  0.0984325   -0.115064   106 LEU   A HG   
3155 H HD11 . LEU   B 94  ? 0.600837 0.528444 0.601553 0.00170572  0.0841686   -0.111595   106 LEU   A HD11 
3156 H HD12 . LEU   B 94  ? 0.657003 0.529946 0.636876 0.0157434   0.0985141   -0.106211   106 LEU   A HD12 
3157 H HD13 . LEU   B 94  ? 0.62452  0.535024 0.622905 0.0266821   0.0695612   -0.0947458  106 LEU   A HD13 
3158 H HD21 . LEU   B 94  ? 0.68566  0.516761 0.583903 -0.00631033 0.0926403   -0.0910966  106 LEU   A HD21 
3159 H HD22 . LEU   B 94  ? 0.68145  0.522374 0.605838 0.024181    0.0738336   -0.0791947  106 LEU   A HD22 
3160 H HD23 . LEU   B 94  ? 0.709035 0.512677 0.621386 0.0084962   0.103322    -0.0901093  106 LEU   A HD23 
3161 N N    . ILE   B 95  ? 0.501673 0.472339 0.478551 -0.0483457  0.0887919   -0.136601   107 ILE   A N    
3162 C CA   . ILE   B 95  ? 0.480218 0.474055 0.451948 -0.0694316  0.0971566   -0.151282   107 ILE   A CA   
3163 C C    . ILE   B 95  ? 0.570217 0.53865  0.527657 -0.0840134  0.121073    -0.164009   107 ILE   A C    
3164 O O    . ILE   B 95  ? 0.504167 0.46475  0.468963 -0.0778701  0.128355    -0.166091   107 ILE   A O    
3165 C CB   . ILE   B 95  ? 0.449137 0.483271 0.44037  -0.0689685  0.0840912   -0.150286   107 ILE   A CB   
3166 C CG1  . ILE   B 95  ? 0.456481 0.502704 0.460981 -0.0551304  0.0606417   -0.139114   107 ILE   A CG1  
3167 C CG2  . ILE   B 95  ? 0.444262 0.50931  0.429119 -0.0877476  0.0890808   -0.164321   107 ILE   A CG2  
3168 C CD1  . ILE   B 95  ? 0.476825 0.544616 0.499253 -0.0531408  0.0483898   -0.130758   107 ILE   A CD1  
3169 H H    . ILE   B 95  ? 0.510308 0.475277 0.496394 -0.0410994  0.0915525   -0.134022   107 ILE   A H    
3170 H HA   . ILE   B 95  ? 0.494159 0.493759 0.457867 -0.0746479  0.0956072   -0.153765   107 ILE   A HA   
3171 H HB   . ILE   B 95  ? 0.45548  0.487224 0.453969 -0.0657516  0.0879633   -0.148053   107 ILE   A HB   
3172 H HG12 . ILE   B 95  ? 0.455093 0.511132 0.454405 -0.0572951  0.0570282   -0.143782   107 ILE   A HG12 
3173 H HG13 . ILE   B 95  ? 0.463408 0.4922   0.468448 -0.0455916  0.0570387   -0.132957   107 ILE   A HG13 
3174 H HG21 . ILE   B 95  ? 0.430738 0.519538 0.424335 -0.0851072  0.078226    -0.160183   107 ILE   A HG21 
3175 H HG22 . ILE   B 95  ? 0.447275 0.51715  0.426598 -0.0924592  0.0892476   -0.169044   107 ILE   A HG22 
3176 H HG23 . ILE   B 95  ? 0.461491 0.519391 0.438689 -0.0978811  0.102776    -0.173166   107 ILE   A HG23 
3177 H HD11 . ILE   B 95  ? 0.468027 0.533263 0.496618 -0.0531622  0.0549135   -0.127895   107 ILE   A HD11 
3178 H HD12 . ILE   B 95  ? 0.459354 0.5253   0.489477 -0.0453336  0.0343238   -0.124461   107 ILE   A HD12 
3179 H HD13 . ILE   B 95  ? 0.461857 0.548131 0.481119 -0.0600861  0.048296    -0.134494   107 ILE   A HD13 
3180 N N    . LYS   B 96  ? 0.576388 0.534478 0.514599 -0.104803   0.134228    -0.174701   108 LYS   A N    
3181 C CA   . LYS   B 96  ? 0.65025  0.582896 0.57269  -0.126555   0.157026    -0.192182   108 LYS   A CA   
3182 C C    . LYS   B 96  ? 0.574441 0.555126 0.504816 -0.14266    0.156145    -0.209811   108 LYS   A C    
3183 O O    . LYS   B 96  ? 0.550846 0.583412 0.49471  -0.141178   0.139147    -0.207241   108 LYS   A O    
3184 C CB   . LYS   B 96  ? 0.663007 0.57296  0.563348 -0.149457   0.17083     -0.196573   108 LYS   A CB   
3185 C CG   . LYS   B 96  ? 0.826326 0.675936 0.706351 -0.135697   0.175788    -0.177123   108 LYS   A CG   
3186 C CD   . LYS   B 96  ? 0.916583 0.703659 0.789042 -0.116635   0.184837    -0.170498   108 LYS   A CD   
3187 C CE   . LYS   B 96  ? 0.967731 0.701182 0.817512 -0.0988452  0.184005    -0.145916   108 LYS   A CE   
3188 N NZ   . LYS   B 96  ? 0.908568 0.67744  0.772517 -0.0729046  0.158386    -0.128562   108 LYS   A NZ   
3189 H H    . LYS   B 96  ? 0.582138 0.549633 0.516921 -0.107105   0.129684    -0.172438   108 LYS   A H    
3190 H HA   . LYS   B 96  ? 0.651105 0.550026 0.570912 -0.11577    0.163953    -0.189361   108 LYS   A HA   
3191 H HB2  . LYS   B 96  ? 0.66984  0.617711 0.576649 -0.154877   0.16298     -0.197794   108 LYS   A HB2  
3192 H HB3  . LYS   B 96  ? 0.719036 0.617847 0.610431 -0.169718   0.184959    -0.211483   108 LYS   A HB3  
3193 H HG2  . LYS   B 96  ? 0.780189 0.646763 0.66708  -0.119447   0.161025    -0.165115   108 LYS   A HG2  
3194 H HG3  . LYS   B 96  ? 0.831385 0.66659  0.694576 -0.154836   0.187313    -0.179737   108 LYS   A HG3  
3195 H HD2  . LYS   B 96  ? 0.939453 0.701834 0.801982 -0.132711   0.200884    -0.184203   108 LYS   A HD2  
3196 H HD3  . LYS   B 96  ? 0.87825  0.685339 0.769957 -0.0992239  0.175224    -0.1689     108 LYS   A HD3  
3197 H HE2  . LYS   B 96  ? 0.988613 0.705332 0.817589 -0.11778    0.193832    -0.145222   108 LYS   A HE2  
3198 H HE3  . LYS   B 96  ? 0.996432 0.687657 0.841088 -0.0860385  0.19079     -0.142426   108 LYS   A HE3  
3199 H HZ1  . LYS   B 96  ? 0.893893 0.689866 0.7562   -0.0828596  0.153945    -0.130316   108 LYS   A HZ1  
3200 H HZ2  . LYS   B 96  ? 0.88293  0.677174 0.769336 -0.0615849  0.149287    -0.131109   108 LYS   A HZ2  
3201 H HZ3  . LYS   B 96  ? 0.941128 0.679405 0.792303 -0.0584429  0.15605     -0.113961   108 LYS   A HZ3  
3202 N N    . PRO   B 97  ? 0.665671 0.627684 0.583711 -0.158714   0.174461    -0.22938    109 PRO   A N    
3203 C CA   . PRO   B 97  ? 0.605054 0.613726 0.524277 -0.172515   0.172994    -0.246245   109 PRO   A CA   
3204 C C    . PRO   B 97  ? 0.556393 0.625577 0.478926 -0.192855   0.161611    -0.2552     109 PRO   A C    
3205 O O    . PRO   B 97  ? 0.569538 0.689802 0.497286 -0.192287   0.148453    -0.25615    109 PRO   A O    
3206 C CB   . PRO   B 97  ? 0.661651 0.628794 0.561088 -0.188075   0.197581    -0.270708   109 PRO   A CB   
3207 C CG   . PRO   B 97  ? 0.764868 0.655112 0.652418 -0.183331   0.212809    -0.265277   109 PRO   A CG   
3208 C CD   . PRO   B 97  ? 0.718923 0.608784 0.618503 -0.159983   0.19644     -0.235222   109 PRO   A CD   
3209 H HA   . PRO   B 97  ? 0.586956 0.612518 0.516748 -0.15671    0.164147    -0.236294   109 PRO   A HA   
3210 H HB2  . PRO   B 97  ? 0.686297 0.672773 0.576878 -0.212081   0.201348    -0.288662   109 PRO   A HB2  
3211 H HB3  . PRO   B 97  ? 0.67336  0.643576 0.575486 -0.176832   0.199747    -0.271996   109 PRO   A HB3  
3212 H HG2  . PRO   B 97  ? 0.776851 0.651451 0.650827 -0.20736    0.22293     -0.277775   109 PRO   A HG2  
3213 H HG3  . PRO   B 97  ? 0.772661 0.629084 0.656971 -0.171295   0.222967    -0.268699   109 PRO   A HG3  
3214 H HD2  . PRO   B 97  ? 0.744183 0.609255 0.632107 -0.16976    0.202044    -0.232598   109 PRO   A HD2  
3215 H HD3  . PRO   B 97  ? 0.723392 0.593146 0.629428 -0.136814   0.194573    -0.223701   109 PRO   A HD3  
3216 N N    . GLU   B 98  ? 0.593704 0.660533 0.513413 -0.209762   0.16667     -0.260244   110 GLU   A N    
3217 C CA   . GLU   B 98  ? 0.613198 0.74692  0.543185 -0.227255   0.156837    -0.270809   110 GLU   A CA   
3218 C C    . GLU   B 98  ? 0.60221  0.786819 0.55356  -0.200136   0.129987    -0.252878   110 GLU   A C    
3219 O O    . GLU   B 98  ? 0.573243 0.821986 0.53581  -0.205427   0.116673    -0.260226   110 GLU   A O    
3220 C CB   . GLU   B 98  ? 0.648807 0.767467 0.573827 -0.249445   0.1716      -0.276769   110 GLU   A CB   
3221 C CG   . GLU   B 98  ? 0.776077 0.837823 0.677233 -0.282093   0.198605    -0.295275   110 GLU   A CG   
3222 C CD   . GLU   B 98  ? 0.84538  0.811629 0.725365 -0.268588   0.214534    -0.283827   110 GLU   A CD   
3223 O OE1  . GLU   B 98  ? 0.723436 0.665002 0.606588 -0.235426   0.205999    -0.258559   110 GLU   A OE1  
3224 O OE2  . GLU   B 98  ? 0.879159 0.79301  0.738887 -0.290877   0.235361    -0.302012   110 GLU   A OE2  
3225 H H    . GLU   B 98  ? 0.617887 0.642641 0.52965  -0.209677   0.176661    -0.256156   110 GLU   A H    
3226 H HA   . GLU   B 98  ? 0.626851 0.782517 0.551681 -0.244248   0.159321    -0.287397   110 GLU   A HA   
3227 H HB2  . GLU   B 98  ? 0.652879 0.747505 0.577858 -0.2329     0.169981    -0.260608   110 GLU   A HB2  
3228 H HB3  . GLU   B 98  ? 0.646424 0.817746 0.583523 -0.259339   0.165143    -0.284322   110 GLU   A HB3  
3229 H HG2  . GLU   B 98  ? 0.780829 0.852045 0.681393 -0.303756   0.206512    -0.301594   110 GLU   A HG2  
3230 H HG3  . GLU   B 98  ? 0.775078 0.855305 0.673854 -0.295669   0.199475    -0.31252    110 GLU   A HG3  
3231 N N    . TYR   B 99  ? 0.587238 0.743061 0.544663 -0.17073    0.120769    -0.230117   111 TYR   A N    
3232 C CA   . TYR   B 99  ? 0.550965 0.738708 0.525735 -0.14601    0.096465    -0.213954   111 TYR   A CA   
3233 C C    . TYR   B 99  ? 0.511883 0.693576 0.487953 -0.131907   0.0874389   -0.200002   111 TYR   A C    
3234 O O    . TYR   B 99  ? 0.455599 0.641386 0.4432   -0.111636   0.0694889   -0.182303   111 TYR   A O    
3235 C CB   . TYR   B 99  ? 0.531284 0.696229 0.510509 -0.130123   0.0930792   -0.203216   111 TYR   A CB   
3236 C CG   . TYR   B 99  ? 0.542604 0.727659 0.520011 -0.147158   0.10393     -0.216832   111 TYR   A CG   
3237 C CD1  . TYR   B 99  ? 0.554709 0.701713 0.513277 -0.169211   0.127243    -0.22333    111 TYR   A CD1  
3238 C CD2  . TYR   B 99  ? 0.596435 0.839511 0.591715 -0.141251   0.0921112   -0.222876   111 TYR   A CD2  
3239 C CE1  . TYR   B 99  ? 0.570168 0.738488 0.526515 -0.190554   0.140144    -0.234431   111 TYR   A CE1  
3240 C CE2  . TYR   B 99  ? 0.569998 0.843498 0.568358 -0.158568   0.104646    -0.236869   111 TYR   A CE2  
3241 C CZ   . TYR   B 99  ? 0.585107 0.822776 0.563394 -0.186644   0.129722    -0.242473   111 TYR   A CZ   
3242 O OH   . TYR   B 99  ? 0.578256 0.849966 0.559815 -0.207878   0.144148    -0.254738   111 TYR   A OH   
3243 H H    . TYR   B 99  ? 0.596514 0.710221 0.546995 -0.166211   0.12945     -0.225084   111 TYR   A H    
3244 H HA   . TYR   B 99  ? 0.537481 0.768691 0.518831 -0.150941   0.0889375   -0.220838   111 TYR   A HA   
3245 H HB2  . TYR   B 99  ? 0.543338 0.668179 0.515106 -0.125938   0.0998446   -0.196694   111 TYR   A HB2  
3246 H HB3  . TYR   B 99  ? 0.515654 0.693865 0.505515 -0.113111   0.0772644   -0.194129   111 TYR   A HB3  
3247 H HD1  . TYR   B 99  ? 0.57718  0.682601 0.524275 -0.16991    0.135247    -0.219675   111 TYR   A HD1  
3248 H HD2  . TYR   B 99  ? 0.553042 0.815904 0.559337 -0.124655   0.0758504   -0.21716    111 TYR   A HD2  
3249 H HE1  . TYR   B 99  ? 0.609778 0.746019 0.550312 -0.207698   0.156826    -0.236509   111 TYR   A HE1  
3250 H HE2  . TYR   B 99  ? 0.561578 0.879977 0.575821 -0.151587   0.096883    -0.24226    111 TYR   A HE2  
3252 N N    . ALA   B 100 ? 0.514296 0.68423  0.47749  -0.144344   0.101901    -0.209212   112 ALA   A N    
3253 C CA   . ALA   B 100 ? 0.462052 0.63199  0.42521  -0.134897   0.0991485   -0.197734   112 ALA   A CA   
3254 C C    . ALA   B 100 ? 0.503728 0.704188 0.448566 -0.154254   0.106468    -0.214395   112 ALA   A C    
3255 O O    . ALA   B 100 ? 0.505896 0.753808 0.447732 -0.159993   0.0918358   -0.215613   112 ALA   A O    
3256 C CB   . ALA   B 100 ? 0.429916 0.552899 0.398136 -0.122653   0.11108     -0.191101   112 ALA   A CB   
3257 H H    . ALA   B 100 ? 0.52639  0.688527 0.480025 -0.160259   0.115068    -0.224159   112 ALA   A H    
3258 H HA   . ALA   B 100 ? 0.45164  0.637237 0.423488 -0.12357    0.0831088   -0.183138   112 ALA   A HA   
3259 H HB1  . ALA   B 100 ? 0.426942 0.53867  0.405587 -0.110203   0.102066    -0.179217   112 ALA   A HB1  
3260 H HB2  . ALA   B 100 ? 0.461699 0.560624 0.421163 -0.130059   0.125831    -0.203383   112 ALA   A HB2  
3261 H HB3  . ALA   B 100 ? 0.442269 0.571724 0.41196  -0.119567   0.112867    -0.186708   112 ALA   A HB3  
3262 N N    . TYR   B 101 ? 0.531076 0.707141 0.462802 -0.162534   0.12804     -0.229027   113 TYR   A N    
3263 C CA   . TYR   B 101 ? 0.563721 0.77106  0.472853 -0.18073    0.134909    -0.247157   113 TYR   A CA   
3264 C C    . TYR   B 101 ? 0.597309 0.789813 0.488291 -0.207299   0.153978    -0.282028   113 TYR   A C    
3265 O O    . TYR   B 101 ? 0.615404 0.827922 0.483526 -0.225103   0.162481    -0.304238   113 TYR   A O    
3266 C CB   . TYR   B 101 ? 0.567906 0.769751 0.473308 -0.170736   0.145563    -0.240123   113 TYR   A CB   
3267 C CG   . TYR   B 101 ? 0.543079 0.763034 0.463663 -0.153429   0.126739    -0.206204   113 TYR   A CG   
3268 C CD1  . TYR   B 101 ? 0.550051 0.813559 0.457478 -0.157328   0.109436    -0.19247    113 TYR   A CD1  
3269 C CD2  . TYR   B 101 ? 0.562207 0.753981 0.508628 -0.134341   0.124064    -0.187264   113 TYR   A CD2  
3270 C CE1  . TYR   B 101 ? 0.542948 0.811632 0.460171 -0.144441   0.093314    -0.160345   113 TYR   A CE1  
3271 C CE2  . TYR   B 101 ? 0.533647 0.737393 0.493216 -0.124353   0.107348    -0.15906    113 TYR   A CE2  
3272 C CZ   . TYR   B 101 ? 0.551563 0.788837 0.49564  -0.130207   0.0932785   -0.145008   113 TYR   A CZ   
3273 O OH   . TYR   B 101 ? 0.506738 0.745207 0.459315 -0.122956   0.0772849   -0.115545   113 TYR   A OH   
3274 H H    . TYR   B 101 ? 0.537166 0.678314 0.472789 -0.155717   0.138115    -0.228625   113 TYR   A H    
3275 H HA   . TYR   B 101 ? 0.551337 0.797815 0.458509 -0.182737   0.119181    -0.240938   113 TYR   A HA   
3276 H HB2  . TYR   B 101 ? 0.578325 0.744596 0.489987 -0.163931   0.159331    -0.244855   113 TYR   A HB2  
3277 H HB3  . TYR   B 101 ? 0.592316 0.81468  0.478483 -0.183241   0.151881    -0.253917   113 TYR   A HB3  
3278 H HD1  . TYR   B 101 ? 0.566901 0.855408 0.456367 -0.169731   0.108725    -0.205022   113 TYR   A HD1  
3279 H HD2  . TYR   B 101 ? 0.551726 0.714848 0.505789 -0.128946   0.133516    -0.193769   113 TYR   A HD2  
3280 H HE1  . TYR   B 101 ? 0.556757 0.849423 0.46138  -0.146208   0.0817946   -0.148881   113 TYR   A HE1  
3281 H HE2  . TYR   B 101 ? 0.525984 0.713466 0.503591 -0.114157   0.105178    -0.14898    113 TYR   A HE2  
3283 N N    . GLY   B 102 ? 0.601348 0.755699 0.498868 -0.212363   0.161713    -0.287437   114 GLY   A N    
3284 C CA   . GLY   B 102 ? 0.666318 0.814218 0.549347 -0.24512    0.174938    -0.317787   114 GLY   A CA   
3285 C C    . GLY   B 102 ? 0.713193 0.811183 0.573584 -0.25697    0.201365    -0.344616   114 GLY   A C    
3286 O O    . GLY   B 102 ? 0.670038 0.735077 0.530381 -0.234731   0.211639    -0.338516   114 GLY   A O    
3287 H H    . GLY   B 102 ? 0.59209  0.723569 0.50165  -0.197269   0.159219    -0.27211    114 GLY   A H    
3288 H HA2  . GLY   B 102 ? 0.655781 0.783368 0.545813 -0.247368   0.177032    -0.313869   114 GLY   A HA2  
3289 H HA3  . GLY   B 102 ? 0.653163 0.850742 0.533873 -0.258325   0.164507    -0.325739   114 GLY   A HA3  
3290 N N    . SER   B 103 ? 0.760891 0.857103 0.603755 -0.293017   0.212623    -0.377401   115 SER   A N    
3291 C CA   . SER   B 103 ? 0.819034 0.858358 0.637461 -0.305915   0.238942    -0.408244   115 SER   A CA   
3292 C C    . SER   B 103 ? 0.777197 0.854718 0.578945 -0.30194    0.239719    -0.422063   115 SER   A C    
3293 O O    . SER   B 103 ? 0.848092 0.88055  0.636095 -0.293211   0.261334    -0.438822   115 SER   A O    
3294 C CB   . SER   B 103 ? 0.88743  0.905555 0.691456 -0.349795   0.251531    -0.439817   115 SER   A CB   
3295 O OG   . SER   B 103 ? 0.865175 0.969771 0.670177 -0.378338   0.234215    -0.454587   115 SER   A OG   
3296 H H    . SER   B 103 ? 0.750637 0.881361 0.597709 -0.309744   0.204171    -0.382079   115 SER   A H    
3297 H HA   . SER   B 103 ? 0.822296 0.808323 0.64471  -0.286377   0.248915    -0.397669   115 SER   A HA   
3298 H HB2  . SER   B 103 ? 0.932867 0.907912 0.718421 -0.35879    0.269174    -0.462827   115 SER   A HB2  
3299 H HB3  . SER   B 103 ? 0.881556 0.868305 0.693574 -0.350286   0.254623    -0.427774   115 SER   A HB3  
3301 N N    . ALA   B 104 ? 0.722441 0.882438 0.524743 -0.30437    0.216456    -0.412358   116 ALA   A N    
3302 C CA   . ALA   B 104 ? 0.752702 0.956295 0.533721 -0.301415   0.214946    -0.418141   116 ALA   A CA   
3303 C C    . ALA   B 104 ? 0.721332 0.910081 0.513828 -0.265979   0.220096    -0.39102    116 ALA   A C    
3304 O O    . ALA   B 104 ? 0.722108 0.9249   0.494775 -0.263845   0.232267    -0.402159   116 ALA   A O    
3305 C CB   . ALA   B 104 ? 0.741598 1.03266  0.517564 -0.310424   0.185979    -0.408094   116 ALA   A CB   
3306 H H    . ALA   B 104 ? 0.705129 0.895332 0.520087 -0.307511   0.201134    -0.401052   116 ALA   A H    
3307 H HA   . ALA   B 104 ? 0.79686  0.983457 0.556254 -0.31823    0.231037    -0.449145   116 ALA   A HA   
3308 H HB1  . ALA   B 104 ? 0.752711 1.0624   0.524712 -0.333895   0.18223     -0.427519   116 ALA   A HB1  
3309 H HB2  . ALA   B 104 ? 0.696802 1.0004   0.493031 -0.29273    0.170674    -0.37924    116 ALA   A HB2  
3310 H HB3  . ALA   B 104 ? 0.752324 1.06948  0.508154 -0.310148   0.186133    -0.411089   116 ALA   A HB3  
3311 N N    . GLY   B 105 ? 0.665817 0.84074  0.489761 -0.240922   0.20826     -0.355283   117 GLY   A N    
3312 C CA   . GLY   B 105 ? 0.61644  0.78912  0.457633 -0.211276   0.208774    -0.327625   117 GLY   A CA   
3313 C C    . GLY   B 105 ? 0.617535 0.853895 0.446342 -0.212105   0.194865    -0.310947   117 GLY   A C    
3314 O O    . GLY   B 105 ? 0.596466 0.878177 0.409452 -0.227454   0.176987    -0.311464   117 GLY   A O    
3315 H H    . GLY   B 105 ? 0.646036 0.815507 0.481237 -0.243937   0.199791    -0.349145   117 GLY   A H    
3316 H HA2  . GLY   B 105 ? 0.595986 0.754147 0.458803 -0.197581   0.199376    -0.30696    117 GLY   A HA2  
3317 H HA3  . GLY   B 105 ? 0.650719 0.794504 0.489606 -0.204651   0.227944    -0.340387   117 GLY   A HA3  
3318 N N    . SER   B 106 ? 0.626614 0.86779  0.463222 -0.19546    0.203073    -0.294548   118 SER   A N    
3319 C CA   . SER   B 106 ? 0.630379 0.921917 0.455616 -0.195772   0.191053    -0.269323   118 SER   A CA   
3320 C C    . SER   B 106 ? 0.659149 0.956072 0.484401 -0.188035   0.215718    -0.270771   118 SER   A C    
3321 O O    . SER   B 106 ? 0.606611 0.906641 0.458056 -0.17386    0.214053    -0.242859   118 SER   A O    
3322 C CB   . SER   B 106 ? 0.593555 0.889338 0.444044 -0.182022   0.164018    -0.228826   118 SER   A CB   
3323 O OG   . SER   B 106 ? 0.639905 0.978283 0.468544 -0.187072   0.152458    -0.205791   118 SER   A OG   
3324 H H    . SER   B 106 ? 0.629775 0.842069 0.479576 -0.18378    0.216966    -0.298276   118 SER   A H    
3325 H HA   . SER   B 106 ? 0.650872 0.971816 0.449516 -0.210877   0.185652    -0.279215   118 SER   A HA   
3326 H HB2  . SER   B 106 ? 0.586614 0.878455 0.441879 -0.18363    0.150852    -0.230121   118 SER   A HB2  
3327 H HB3  . SER   B 106 ? 0.58294  0.85711  0.45737  -0.168838   0.168301    -0.218212   118 SER   A HB3  
3329 N N    . LEU   B 107 ? 0.717562 1.01714  0.514514 -0.198982   0.240004    -0.307664   119 LEU   A N    
3330 C CA   . LEU   B 107 ? 0.7314   1.03899  0.528193 -0.19035    0.269437    -0.319229   119 LEU   A CA   
3331 C C    . LEU   B 107 ? 0.73645  1.10159  0.516339 -0.197243   0.266919    -0.291657   119 LEU   A C    
3332 O O    . LEU   B 107 ? 0.727381 1.12568  0.473725 -0.213614   0.247638    -0.278669   119 LEU   A O    
3333 C CB   . LEU   B 107 ? 0.802221 1.09586  0.565622 -0.201979   0.295436    -0.370769   119 LEU   A CB   
3334 C CG   . LEU   B 107 ? 0.814134 1.03576  0.594584 -0.192012   0.308614    -0.398588   119 LEU   A CG   
3335 C CD1  . LEU   B 107 ? 0.903429 1.10938  0.648887 -0.20256    0.337809    -0.450336   119 LEU   A CD1  
3336 C CD2  . LEU   B 107 ? 0.791383 0.97928  0.620102 -0.158372   0.315974    -0.380995   119 LEU   A CD2  
3337 H H    . LEU   B 107 ? 0.730726 1.0289   0.508342 -0.212778   0.238642    -0.328319   119 LEU   A H    
3338 H HA   . LEU   B 107 ? 0.717921 1.00149  0.547312 -0.172468   0.274672    -0.312019   119 LEU   A HA   
3339 H HB2  . LEU   B 107 ? 0.813901 1.12793  0.54737  -0.221434   0.285589    -0.379744   119 LEU   A HB2  
3340 H HB3  . LEU   B 107 ? 0.822152 1.13545  0.578172 -0.198236   0.314578    -0.378802   119 LEU   A HB3  
3341 H HG   . LEU   B 107 ? 0.806982 1.01361  0.586729 -0.202142   0.292703    -0.396002   119 LEU   A HG   
3342 H HD11 . LEU   B 107 ? 0.915276 1.1474   0.628912 -0.225493   0.331222    -0.462671   119 LEU   A HD11 
3343 H HD12 . LEU   B 107 ? 0.918027 1.07096  0.67018  -0.198247   0.345798    -0.467622   119 LEU   A HD12 
3344 H HD13 . LEU   B 107 ? 0.913271 1.13601  0.660474 -0.190892   0.355535    -0.454975   119 LEU   A HD13 
3345 H HD21 . LEU   B 107 ? 0.748391 0.938472 0.597342 -0.153781   0.296361    -0.352353   119 LEU   A HD21 
3346 H HD22 . LEU   B 107 ? 0.796812 1.01013  0.632708 -0.148424   0.32943     -0.379619   119 LEU   A HD22 
3347 H HD23 . LEU   B 107 ? 0.815952 0.955754 0.647908 -0.151257   0.326721    -0.400056   119 LEU   A HD23 
3348 N N    . PRO   B 108 ? 0.738892 1.12056  0.539603 -0.185824   0.287695    -0.28242    120 PRO   A N    
3349 C CA   . PRO   B 108 ? 0.725473 1.07745  0.56801  -0.16173    0.309362    -0.298741   120 PRO   A CA   
3350 C C    . PRO   B 108 ? 0.67805  1.00306  0.574347 -0.141635   0.291903    -0.270068   120 PRO   A C    
3351 O O    . PRO   B 108 ? 0.710919 1.01138  0.640578 -0.118752   0.305382    -0.282033   120 PRO   A O    
3352 C CB   . PRO   B 108 ? 0.765982 1.16745  0.609704 -0.160184   0.338197    -0.300673   120 PRO   A CB   
3353 C CG   . PRO   B 108 ? 0.746894 1.19201  0.570392 -0.180664   0.320781    -0.259301   120 PRO   A CG   
3354 C CD   . PRO   B 108 ? 0.742801 1.17754  0.525804 -0.196752   0.2924      -0.255979   120 PRO   A CD   
3355 H HA   . PRO   B 108 ? 0.755147 1.0786   0.587841 -0.159876   0.319579    -0.328793   120 PRO   A HA   
3356 H HB2  . PRO   B 108 ? 0.746317 1.14504  0.628975 -0.1427     0.346483    -0.296776   120 PRO   A HB2  
3357 H HB3  . PRO   B 108 ? 0.801417 1.20962  0.61816  -0.16468    0.357635    -0.330563   120 PRO   A HB3  
3358 H HG2  . PRO   B 108 ? 0.715507 1.15852  0.571304 -0.174783   0.309603    -0.232222   120 PRO   A HG2  
3359 H HG3  . PRO   B 108 ? 0.777818 1.25969  0.581453 -0.189301   0.338892    -0.262518   120 PRO   A HG3  
3360 H HD2  . PRO   B 108 ? 0.723922 1.16169  0.511698 -0.19957    0.270974    -0.224108   120 PRO   A HD2  
3361 H HD3  . PRO   B 108 ? 0.783001 1.24188  0.525514 -0.210395   0.299647    -0.269825   120 PRO   A HD3  
3362 N N    . LYS   B 109 ? 0.674107 1.00121  0.577928 -0.147401   0.261688    -0.234606   121 LYS   A N    
3363 C CA   . LYS   B 109 ? 0.664846 0.968898 0.615996 -0.129966   0.245204    -0.210988   121 LYS   A CA   
3364 C C    . LYS   B 109 ? 0.644718 0.893418 0.607788 -0.115142   0.239869    -0.226522   121 LYS   A C    
3365 O O    . LYS   B 109 ? 0.655457 0.882896 0.65344  -0.0933605  0.242676    -0.224849   121 LYS   A O    
3366 C CB   . LYS   B 109 ? 0.647055 0.960692 0.60051  -0.139304   0.215466    -0.172507   121 LYS   A CB   
3367 C CG   . LYS   B 109 ? 0.728347 1.0855   0.683581 -0.151041   0.222976    -0.148454   121 LYS   A CG   
3368 C CD   . LYS   B 109 ? 0.750992 1.1061   0.710719 -0.159828   0.196033    -0.108233   121 LYS   A CD   
3369 C CE   . LYS   B 109 ? 0.797233 1.19262  0.747961 -0.177901   0.210387    -0.0872942  121 LYS   A CE   
3370 N NZ   . LYS   B 109 ? 0.837272 1.22181  0.774583 -0.190374   0.185884    -0.0481172  121 LYS   A NZ   
3371 H H    . LYS   B 109 ? 0.67708  1.01989  0.555659 -0.161239   0.250398    -0.225529   121 LYS   A H    
3372 H HA   . LYS   B 109 ? 0.65865  0.978059 0.634555 -0.120771   0.258087    -0.209162   121 LYS   A HA   
3373 H HB2  . LYS   B 109 ? 0.663536 0.975796 0.590494 -0.14868    0.20404     -0.172803   121 LYS   A HB2  
3374 H HB3  . LYS   B 109 ? 0.633211 0.925773 0.612652 -0.128785   0.202838    -0.162795   121 LYS   A HB3  
3375 H HG2  . LYS   B 109 ? 0.716141 1.08326  0.699829 -0.142669   0.237012    -0.152433   121 LYS   A HG2  
3376 H HG3  . LYS   B 109 ? 0.748629 1.12757  0.672331 -0.162136   0.234574    -0.156756   121 LYS   A HG3  
3377 H HD2  . LYS   B 109 ? 0.748604 1.09406  0.684107 -0.163568   0.180291    -0.103687   121 LYS   A HD2  
3378 H HD3  . LYS   B 109 ? 0.721328 1.05924  0.712862 -0.150506   0.186202    -0.101137   121 LYS   A HD3  
3379 H HE2  . LYS   B 109 ? 0.793209 1.20174  0.776274 -0.174597   0.222412    -0.0880612  121 LYS   A HE2  
3380 H HE3  . LYS   B 109 ? 0.82726  1.24398  0.747727 -0.185276   0.22518     -0.0990158  121 LYS   A HE3  
3381 H HZ1  . LYS   B 109 ? 0.803298 1.16686  0.767319 -0.184304   0.172489    -0.0395803  121 LYS   A HZ1  
3382 H HZ2  . LYS   B 109 ? 0.833847 1.21086  0.74279  -0.190922   0.17396     -0.0467853  121 LYS   A HZ2  
3383 H HZ3  . LYS   B 109 ? 0.849008 1.25486  0.778925 -0.203655   0.195903    -0.0335012  121 LYS   A HZ3  
3384 N N    . ILE   B 110 ? 0.637928 0.865374 0.571611 -0.127856   0.231392    -0.240143   122 ILE   A N    
3385 C CA   . ILE   B 110 ? 0.622557 0.798826 0.564009 -0.120373   0.224101    -0.247182   122 ILE   A CA   
3386 C C    . ILE   B 110 ? 0.638709 0.781966 0.55325  -0.129041   0.245138    -0.28594    122 ILE   A C    
3387 O O    . ILE   B 110 ? 0.646782 0.809788 0.528047 -0.1527     0.245455    -0.303164   122 ILE   A O    
3388 C CB   . ILE   B 110 ? 0.585428 0.766783 0.520551 -0.131373   0.195519    -0.229652   122 ILE   A CB   
3389 C CG1  . ILE   B 110 ? 0.624884 0.837165 0.574749 -0.128476   0.175532    -0.195284   122 ILE   A CG1  
3390 C CG2  . ILE   B 110 ? 0.59459  0.729124 0.540745 -0.123651   0.188939    -0.23106    122 ILE   A CG2  
3391 C CD1  . ILE   B 110 ? 0.609721 0.810199 0.599239 -0.10925    0.171732    -0.176427   122 ILE   A CD1  
3392 H H    . ILE   B 110 ? 0.652454 0.900595 0.559942 -0.142851   0.230198    -0.244771   122 ILE   A H    
3393 H HA   . ILE   B 110 ? 0.606378 0.766382 0.573576 -0.103178   0.224017    -0.238546   122 ILE   A HA   
3394 H HB   . ILE   B 110 ? 0.617274 0.813304 0.527984 -0.147007   0.195546    -0.241842   122 ILE   A HB   
3395 H HG12 . ILE   B 110 ? 0.622295 0.862875 0.559219 -0.136451   0.181259    -0.193266   122 ILE   A HG12 
3396 H HG13 . ILE   B 110 ? 0.595487 0.809582 0.540416 -0.132566   0.158209    -0.186893   122 ILE   A HG13 
3397 H HG21 . ILE   B 110 ? 0.568937 0.711931 0.515119 -0.128032   0.171924    -0.220074   122 ILE   A HG21 
3398 H HG22 . ILE   B 110 ? 0.581555 0.699876 0.548504 -0.107198   0.189872    -0.221934   122 ILE   A HG22 
3399 H HG23 . ILE   B 110 ? 0.615664 0.72837  0.547059 -0.131064   0.201069    -0.252181   122 ILE   A HG23 
3400 H HD11 . ILE   B 110 ? 0.594851 0.768609 0.593252 -0.101179   0.16422     -0.176283   122 ILE   A HD11 
3401 H HD12 . ILE   B 110 ? 0.592766 0.810475 0.588924 -0.111971   0.159719    -0.156429   122 ILE   A HD12 
3402 H HD13 . ILE   B 110 ? 0.618252 0.822115 0.617414 -0.102571   0.188361    -0.184627   122 ILE   A HD13 
3403 N N    . PRO   B 111 ? 0.666833 0.755891 0.592635 -0.111411   0.260773    -0.30037    123 PRO   A N    
3404 C CA   . PRO   B 111 ? 0.724824 0.768261 0.622211 -0.122679   0.280925    -0.337736   123 PRO   A CA   
3405 C C    . PRO   B 111 ? 0.695564 0.716014 0.574854 -0.147389   0.267817    -0.341523   123 PRO   A C    
3406 O O    . PRO   B 111 ? 0.661425 0.696056 0.554008 -0.148096   0.244476    -0.314843   123 PRO   A O    
3407 C CB   . PRO   B 111 ? 0.758042 0.746022 0.675516 -0.0906292  0.298873    -0.344146   123 PRO   A CB   
3408 C CG   . PRO   B 111 ? 0.69442  0.69901  0.653699 -0.0638651  0.281161    -0.306619   123 PRO   A CG   
3409 C CD   . PRO   B 111 ? 0.658531 0.725796 0.622553 -0.0799652  0.258721    -0.281656   123 PRO   A CD   
3410 H HA   . PRO   B 111 ? 0.741772 0.808682 0.620253 -0.133589   0.292066    -0.356138   123 PRO   A HA   
3411 H HB2  . PRO   B 111 ? 0.783372 0.720241 0.689463 -0.0940824  0.302678    -0.353764   123 PRO   A HB2  
3412 H HB3  . PRO   B 111 ? 0.784404 0.778769 0.698883 -0.0838617  0.317384    -0.362795   123 PRO   A HB3  
3413 H HG2  . PRO   B 111 ? 0.701426 0.668287 0.664367 -0.0571079  0.273174    -0.297094   123 PRO   A HG2  
3414 H HG3  . PRO   B 111 ? 0.711506 0.724268 0.689932 -0.0434399  0.292149    -0.308682   123 PRO   A HG3  
3415 H HD2  . PRO   B 111 ? 0.624941 0.683791 0.597457 -0.0787647  0.240994    -0.263369   123 PRO   A HD2  
3416 H HD3  . PRO   B 111 ? 0.639419 0.740916 0.621426 -0.0713363  0.260946    -0.272703   123 PRO   A HD3  
3417 N N    . SER   B 112 ? 0.726111 0.715446 0.575521 -0.169788   0.283903    -0.377499   124 SER   A N    
3418 C CA   . SER   B 112 ? 0.763095 0.725139 0.599473 -0.196178   0.277484    -0.385329   124 SER   A CA   
3419 C C    . SER   B 112 ? 0.744634 0.654311 0.600752 -0.178204   0.271738    -0.359569   124 SER   A C    
3420 O O    . SER   B 112 ? 0.793929 0.653999 0.660879 -0.149793   0.283087    -0.353844   124 SER   A O    
3421 C CB   . SER   B 112 ? 0.821557 0.741313 0.625874 -0.222153   0.300359    -0.43016    124 SER   A CB   
3422 O OG   . SER   B 112 ? 0.83358  0.712434 0.629916 -0.248019   0.299623    -0.436364   124 SER   A OG   
3423 H H    . SER   B 112 ? 0.77256  0.758748 0.60957  -0.170297   0.300236    -0.399181   124 SER   A H    
3424 H HA   . SER   B 112 ? 0.72354  0.73289  0.55832  -0.210148   0.261054    -0.377819   124 SER   A HA   
3425 H HB2  . SER   B 112 ? 0.828652 0.79051  0.616785 -0.238931   0.299386    -0.446341   124 SER   A HB2  
3426 H HB3  . SER   B 112 ? 0.858142 0.73689  0.662091 -0.205266   0.31764     -0.440327   124 SER   A HB3  
3428 N N    . ASN   B 113 ? 0.76267  0.687717 0.622014 -0.193596   0.254164    -0.345031   125 ASN   A N    
3429 C CA   . ASN   B 113 ? 0.774391 0.650104 0.640178 -0.186545   0.251404    -0.326002   125 ASN   A CA   
3430 C C    . ASN   B 113 ? 0.739788 0.608116 0.631178 -0.146359   0.241085    -0.293486   125 ASN   A C    
3431 O O    . ASN   B 113 ? 0.756112 0.564531 0.646838 -0.129606   0.246812    -0.282521   125 ASN   A O    
3432 C CB   . ASN   B 113 ? 0.871809 0.663838 0.713577 -0.201497   0.275732    -0.347892   125 ASN   A CB   
3433 C CG   . ASN   B 113 ? 0.934552 0.736636 0.757201 -0.248942   0.279625    -0.372241   125 ASN   A CG   
3434 O OD1  . ASN   B 113 ? 0.944022 0.815062 0.775964 -0.265222   0.261573    -0.366811   125 ASN   A OD1  
3435 N ND2  . ASN   B 113 ? 1.09228  0.827493 0.889949 -0.271733   0.302991    -0.401045   125 ASN   A ND2  
3436 H H    . ASN   B 113 ? 0.730667 0.70181  0.587131 -0.208545   0.243447    -0.346907   125 ASN   A H    
3437 H HA   . ASN   B 113 ? 0.751016 0.65551  0.618796 -0.200671   0.239316    -0.319925   125 ASN   A HA   
3438 H HB2  . ASN   B 113 ? 0.909221 0.678966 0.74481  -0.193577   0.289574    -0.363944   125 ASN   A HB2  
3439 H HB3  . ASN   B 113 ? 0.884257 0.635706 0.728655 -0.188038   0.275748    -0.330409   125 ASN   A HB3  
3440 H HD21 . ASN   B 113 ? 1.08469  0.829871 0.871872 -0.303034   0.306104    -0.419548   125 ASN   A HD21 
3441 H HD22 . ASN   B 113 ? 1.10311  0.782815 0.89498  -0.255793   0.315365    -0.402481   125 ASN   A HD22 
3442 N N    . ALA   B 114 ? 0.673955 0.602052 0.586339 -0.132256   0.225041    -0.277113   126 ALA   A N    
3443 C CA   . ALA   B 114 ? 0.642038 0.570433 0.58205  -0.0988762  0.214764    -0.250302   126 ALA   A CA   
3444 C C    . ALA   B 114 ? 0.56783  0.500349 0.516046 -0.0954858  0.192682    -0.225553   126 ALA   A C    
3445 O O    . ALA   B 114 ? 0.524272 0.492725 0.469643 -0.112166   0.17939     -0.223396   126 ALA   A O    
3446 C CB   . ALA   B 114 ? 0.589568 0.574777 0.548319 -0.0901608  0.210003    -0.243809   126 ALA   A CB   
3447 H H    . ALA   B 114 ? 0.660221 0.629117 0.569154 -0.144666   0.219896    -0.282235   126 ALA   A H    
3448 H HA   . ALA   B 114 ? 0.664772 0.551738 0.605051 -0.0840661  0.226171    -0.253106   126 ALA   A HA   
3449 H HB1  . ALA   B 114 ? 0.621761 0.606276 0.574107 -0.0909319  0.225941    -0.260598   126 ALA   A HB1  
3450 H HB2  . ALA   B 114 ? 0.571055 0.591205 0.526581 -0.103206   0.198563    -0.239272   126 ALA   A HB2  
3451 H HB3  . ALA   B 114 ? 0.578686 0.56697  0.558426 -0.0712675  0.202766    -0.227454   126 ALA   A HB3  
3452 N N    . THR   B 115 ? 0.660542 0.558943 0.618646 -0.07083    0.188515    -0.208016   127 THR   A N    
3453 C CA   . THR   B 115 ? 0.593932 0.503335 0.562654 -0.0603322  0.165955    -0.184038   127 THR   A CA   
3454 C C    . THR   B 115 ? 0.569115 0.524334 0.569062 -0.0443467  0.1499      -0.169981   127 THR   A C    
3455 O O    . THR   B 115 ? 0.557086 0.518619 0.575494 -0.0282453  0.157306    -0.170687   127 THR   A O    
3456 C CB   . THR   B 115 ? 0.623666 0.475502 0.581839 -0.042724   0.168366    -0.17185    127 THR   A CB   
3457 O OG1  . THR   B 115 ? 0.650746 0.462155 0.577985 -0.0668982  0.18458     -0.184316   127 THR   A OG1  
3458 C CG2  . THR   B 115 ? 0.639998 0.501281 0.601512 -0.0321996  0.145774    -0.149802   127 THR   A CG2  
3459 H H    . THR   B 115 ? 0.661566 0.528038 0.618452 -0.0588558  0.199893    -0.212029   127 THR   A H    
3460 H HA   . THR   B 115 ? 0.585889 0.510052 0.546547 -0.0760577  0.160195    -0.185632   127 THR   A HA   
3461 H HB   . THR   B 115 ? 0.650268 0.484797 0.616453 -0.0246282  0.174801    -0.171466   127 THR   A HB   
3463 H HG21 . THR   B 115 ? 0.658347 0.483163 0.608754 -0.0206747  0.147526    -0.140896   127 THR   A HG21 
3464 H HG22 . THR   B 115 ? 0.614379 0.487971 0.566507 -0.0483942  0.142546    -0.152388   127 THR   A HG22 
3465 H HG23 . THR   B 115 ? 0.599602 0.49149  0.582739 -0.0210217  0.133056    -0.142784   127 THR   A HG23 
3466 N N    . LEU   B 116 ? 0.50142  0.487635 0.508958 -0.0486211  0.128528    -0.157742   128 LEU   A N    
3467 C CA   . LEU   B 116 ? 0.484872 0.507919 0.519603 -0.0403236  0.112593    -0.144057   128 LEU   A CA   
3468 C C    . LEU   B 116 ? 0.472885 0.489389 0.516285 -0.027321   0.0911519   -0.128796   128 LEU   A C    
3469 O O    . LEU   B 116 ? 0.482556 0.480008 0.506851 -0.029905   0.086188    -0.128691   128 LEU   A O    
3470 C CB   . LEU   B 116 ? 0.501564 0.561813 0.535105 -0.0569082  0.104433    -0.143143   128 LEU   A CB   
3471 C CG   . LEU   B 116 ? 0.617168 0.694208 0.63339  -0.0743283  0.120081    -0.158559   128 LEU   A CG   
3472 C CD1  . LEU   B 116 ? 0.625121 0.741674 0.643902 -0.0829995  0.108121    -0.147421   128 LEU   A CD1  
3473 C CD2  . LEU   B 116 ? 0.568902 0.636726 0.585099 -0.0704412  0.143278    -0.171918   128 LEU   A CD2  
3474 H H    . LEU   B 116 ? 0.508946 0.491755 0.504501 -0.0576309  0.12467     -0.15886    128 LEU   A H    
3475 H HA   . LEU   B 116 ? 0.496273 0.524534 0.544475 -0.0317767  0.120337    -0.144754   128 LEU   A HA   
3476 H HB2  . LEU   B 116 ? 0.503252 0.562307 0.53022  -0.0599403  0.0937374   -0.140865   128 LEU   A HB2  
3477 H HB3  . LEU   B 116 ? 0.500952 0.578873 0.551684 -0.0530594  0.0964173   -0.132946   128 LEU   A HB3  
3478 H HG   . LEU   B 116 ? 0.592534 0.661322 0.593059 -0.0835156  0.122232    -0.167802   128 LEU   A HG   
3479 H HD11 . LEU   B 116 ? 0.604485 0.723048 0.623603 -0.082508   0.0930995   -0.140142   128 LEU   A HD11 
3480 H HD12 . LEU   B 116 ? 0.627517 0.75787  0.631312 -0.0940197  0.116029    -0.156738   128 LEU   A HD12 
3481 H HD13 . LEU   B 116 ? 0.612575 0.738355 0.646602 -0.078096   0.107681    -0.13819    128 LEU   A HD13 
3482 H HD21 . LEU   B 116 ? 0.609099 0.645772 0.615409 -0.068602   0.15243     -0.181249   128 LEU   A HD21 
3483 H HD22 . LEU   B 116 ? 0.583595 0.657936 0.619564 -0.0581418  0.142222    -0.163541   128 LEU   A HD22 
3484 H HD23 . LEU   B 116 ? 0.597676 0.684608 0.603509 -0.0818469  0.150736    -0.180401   128 LEU   A HD23 
3485 N N    . PHE   B 117 ? 0.461714 0.499422 0.533616 -0.0160907  0.0794558   -0.117988   129 PHE   A N    
3486 C CA   . PHE   B 117 ? 0.441101 0.482214 0.523021 -0.0081669  0.055647    -0.10675    129 PHE   A CA   
3487 C C    . PHE   B 117 ? 0.446727 0.519059 0.549303 -0.0192617  0.0420063   -0.100458   129 PHE   A C    
3488 O O    . PHE   B 117 ? 0.43586  0.534443 0.558666 -0.0247582  0.0499901   -0.0981055  129 PHE   A O    
3489 C CB   . PHE   B 117 ? 0.483144 0.521121 0.582035 0.0139631   0.0513802   -0.0999009  129 PHE   A CB   
3490 C CG   . PHE   B 117 ? 0.556847 0.609655 0.670113 0.0201423   0.0242544   -0.0907966  129 PHE   A CG   
3491 C CD1  . PHE   B 117 ? 0.54613  0.638248 0.69638  0.0151434   0.0125998   -0.0867765  129 PHE   A CD1  
3492 C CD2  . PHE   B 117 ? 0.550819 0.579849 0.638256 0.027028    0.0113945   -0.087868   129 PHE   A CD2  
3493 C CE1  . PHE   B 117 ? 0.567585 0.672628 0.730504 0.0165019   -0.0131401  -0.0826519  129 PHE   A CE1  
3494 C CE2  . PHE   B 117 ? 0.553123 0.59697  0.649599 0.0317845   -0.0141931  -0.0836461  129 PHE   A CE2  
3495 C CZ   . PHE   B 117 ? 0.595502 0.676011 0.730034 0.025504    -0.0273167  -0.0826249  129 PHE   A CZ   
3496 H H    . PHE   B 117 ? 0.459839 0.513067 0.545848 -0.0147097  0.0870592   -0.119221   129 PHE   A H    
3497 H HA   . PHE   B 117 ? 0.455841 0.481025 0.518703 -0.0102527  0.0512895   -0.108108   129 PHE   A HA   
3498 H HB2  . PHE   B 117 ? 0.515785 0.525012 0.596082 0.021556    0.0586076   -0.100911   129 PHE   A HB2  
3499 H HB3  . PHE   B 117 ? 0.493755 0.549374 0.612359 0.0173599   0.0598132   -0.101187   129 PHE   A HB3  
3500 H HD1  . PHE   B 117 ? 0.542594 0.653334 0.708347 0.00881994  0.022869    -0.0877061  129 PHE   A HD1  
3501 H HD2  . PHE   B 117 ? 0.571567 0.574876 0.633881 0.0275791   0.0208252   -0.0893616  129 PHE   A HD2  
3502 H HE1  . PHE   B 117 ? 0.556336 0.687592 0.745449 0.00931791  -0.0203933  -0.0807737  129 PHE   A HE1  
3503 H HE2  . PHE   B 117 ? 0.579152 0.60839  0.65395  0.0362932   -0.0220062  -0.0826707  129 PHE   A HE2  
3504 H HZ   . PHE   B 117 ? 0.579886 0.670081 0.72037  0.0258578   -0.0452745  -0.0822661  129 PHE   A HZ   
3505 N N    . PHE   B 118 ? 0.425902 0.49271  0.523132 -0.021786   0.0221232   -0.09749    130 PHE   A N    
3506 C CA   . PHE   B 118 ? 0.408353 0.489954 0.523745 -0.0312709  0.00633661  -0.0900683  130 PHE   A CA   
3507 C C    . PHE   B 118 ? 0.434865 0.508472 0.556078 -0.0256426  -0.0167656  -0.0895356  130 PHE   A C    
3508 O O    . PHE   B 118 ? 0.432736 0.488011 0.532302 -0.0162955  -0.0221851  -0.0955767  130 PHE   A O    
3509 C CB   . PHE   B 118 ? 0.400537 0.477706 0.501294 -0.0412635  0.00203146  -0.0892235  130 PHE   A CB   
3510 C CG   . PHE   B 118 ? 0.427011 0.518679 0.517895 -0.0507565  0.0195764   -0.0894485  130 PHE   A CG   
3511 C CD1  . PHE   B 118 ? 0.441395 0.52972  0.511578 -0.0503778  0.0342645   -0.101598   130 PHE   A CD1  
3512 C CD2  . PHE   B 118 ? 0.44502  0.554385 0.544813 -0.0631358  0.0218883   -0.077905   130 PHE   A CD2  
3513 C CE1  . PHE   B 118 ? 0.467441 0.572187 0.525989 -0.0611101  0.0486257   -0.10577    130 PHE   A CE1  
3514 C CE2  . PHE   B 118 ? 0.451898 0.577969 0.535672 -0.0720258  0.0371214   -0.0790478  130 PHE   A CE2  
3515 C CZ   . PHE   B 118 ? 0.444147 0.569352 0.508038 -0.0704452  0.0496614   -0.0947466  130 PHE   A CZ   
3516 H H    . PHE   B 118 ? 0.431781 0.482971 0.512627 -0.017992   0.0193881   -0.100713   130 PHE   A H    
3517 H HA   . PHE   B 118 ? 0.412427 0.512507 0.546518 -0.0353999  0.0116057   -0.0856434  130 PHE   A HA   
3518 H HB2  . PHE   B 118 ? 0.409046 0.473962 0.494969 -0.0361335  -0.00202501 -0.0952882  130 PHE   A HB2  
3519 H HB3  . PHE   B 118 ? 0.4113   0.488769 0.522756 -0.04632    -0.00952804 -0.0827648  130 PHE   A HB3  
3520 H HD1  . PHE   B 118 ? 0.444686 0.519663 0.507087 -0.044652   0.0345798   -0.107516   130 PHE   A HD1  
3521 H HD2  . PHE   B 118 ? 0.445163 0.555185 0.559361 -0.0672488  0.0129943   -0.0693786  130 PHE   A HD2  
3522 H HE1  . PHE   B 118 ? 0.460202 0.562568 0.505223 -0.0637998  0.0581528   -0.116313   130 PHE   A HE1  
3523 H HE2  . PHE   B 118 ? 0.457725 0.596419 0.54321  -0.0810725  0.039559    -0.0696247  130 PHE   A HE2  
3524 H HZ   . PHE   B 118 ? 0.459481 0.597995 0.511168 -0.0778882  0.0588556   -0.0979143  130 PHE   A HZ   
3525 N N    . GLU   B 119 ? 0.437071 0.526187 0.585369 -0.034891   -0.0288176  -0.0833717  131 GLU   A N    
3526 C CA   . GLU   B 119 ? 0.514926 0.594071 0.667422 -0.0374514  -0.0529372  -0.0862396  131 GLU   A CA   
3527 C C    . GLU   B 119 ? 0.525943 0.588875 0.676535 -0.0521475  -0.0587502  -0.0818718  131 GLU   A C    
3528 O O    . GLU   B 119 ? 0.511432 0.587259 0.676925 -0.0669838  -0.0509201  -0.0704678  131 GLU   A O    
3529 C CB   . GLU   B 119 ? 0.498423 0.606162 0.684875 -0.0405805  -0.0647096  -0.0840831  131 GLU   A CB   
3530 C CG   . GLU   B 119 ? 0.576304 0.673856 0.765621 -0.0480069  -0.0912375  -0.091449   131 GLU   A CG   
3531 C CD   . GLU   B 119 ? 0.553068 0.690528 0.779528 -0.0532119  -0.104929   -0.0914295  131 GLU   A CD   
3532 O OE1  . GLU   B 119 ? 0.516429 0.664049 0.736943 -0.0370104  -0.117471   -0.0965341  131 GLU   A OE1  
3533 O OE2  . GLU   B 119 ? 0.580412 0.741486 0.840797 -0.0746431  -0.103373   -0.0854496  131 GLU   A OE2  
3534 H H    . GLU   B 119 ? 0.447324 0.554227 0.611664 -0.0415966  -0.0209613  -0.0784346  131 GLU   A H    
3535 H HA   . GLU   B 119 ? 0.501243 0.565426 0.634026 -0.0278265  -0.0576577  -0.0929458  131 GLU   A HA   
3536 H HB2  . GLU   B 119 ? 0.514195 0.631396 0.701052 -0.0271251  -0.061686   -0.0848143  131 GLU   A HB2  
3537 H HB3  . GLU   B 119 ? 0.512147 0.638853 0.719468 -0.0514977  -0.0575379  -0.0777693  131 GLU   A HB3  
3538 H HG2  . GLU   B 119 ? 0.563416 0.645602 0.752919 -0.0608442  -0.0941464  -0.09013    131 GLU   A HG2  
3539 H HG3  . GLU   B 119 ? 0.560294 0.640888 0.726156 -0.0371261  -0.097189   -0.0987225  131 GLU   A HG3  
3540 N N    . ILE   B 120 ? 0.540776 0.574632 0.671189 -0.0463371  -0.0716348  -0.0903505  132 ILE   A N    
3541 C CA   . ILE   B 120 ? 0.546713 0.555814 0.67123  -0.0526183  -0.0782747  -0.0856047  132 ILE   A CA   
3542 C C    . ILE   B 120 ? 0.561772 0.541476 0.688316 -0.0553051  -0.100632   -0.0951181  132 ILE   A C    
3543 O O    . ILE   B 120 ? 0.514736 0.487553 0.62819  -0.0432408  -0.109489   -0.111741   132 ILE   A O    
3544 C CB   . ILE   B 120 ? 0.526013 0.528622 0.626055 -0.0389246  -0.0711432  -0.0897334  132 ILE   A CB   
3545 C CG1  . ILE   B 120 ? 0.500476 0.530345 0.594556 -0.0389783  -0.0494488  -0.087012   132 ILE   A CG1  
3546 C CG2  . ILE   B 120 ? 0.554374 0.531433 0.650217 -0.0400487  -0.0809209  -0.0807766  132 ILE   A CG2  
3547 C CD1  . ILE   B 120 ? 0.496802 0.531812 0.57156  -0.030822   -0.0431571  -0.0927539  132 ILE   A CD1  
3548 H H    . ILE   B 120 ? 0.538987 0.567754 0.658158 -0.0367811  -0.0761441  -0.0990093  132 ILE   A H    
3549 H HA   . ILE   B 120 ? 0.544911 0.561388 0.680334 -0.064657   -0.0731789  -0.0737685  132 ILE   A HA   
3550 H HB   . ILE   B 120 ? 0.530551 0.52667  0.620394 -0.0286258  -0.0754738  -0.101711   132 ILE   A HB   
3551 H HG12 . ILE   B 120 ? 0.500378 0.540264 0.603357 -0.0489557  -0.0436289  -0.0768606  132 ILE   A HG12 
3552 H HG13 . ILE   B 120 ? 0.492356 0.528994 0.586844 -0.0354442  -0.044492   -0.0922677  132 ILE   A HG13 
3553 H HG21 . ILE   B 120 ? 0.551204 0.531346 0.635209 -0.0294094  -0.0782069  -0.0838646  132 ILE   A HG21 
3554 H HG22 . ILE   B 120 ? 0.558088 0.539607 0.660534 -0.0521458  -0.0768478  -0.0667903  132 ILE   A HG22 
3555 H HG23 . ILE   B 120 ? 0.574914 0.528057 0.672494 -0.0390796  -0.0939525  -0.0859478  132 ILE   A HG23 
3556 H HD11 . ILE   B 120 ? 0.500115 0.52769  0.567705 -0.0214472  -0.0484621  -0.102818   132 ILE   A HD11 
3557 H HD12 . ILE   B 120 ? 0.485181 0.535093 0.555455 -0.033424   -0.0294979  -0.0948101  132 ILE   A HD12 
3558 H HD13 . ILE   B 120 ? 0.506566 0.53913  0.580503 -0.0326216  -0.0474104  -0.084823   132 ILE   A HD13 
3559 N N    . GLU   B 121 ? 0.5652   0.526508 0.705535 -0.0739205  -0.108111   -0.0844413  133 GLU   A N    
3560 C CA   . GLU   B 121 ? 0.591384 0.510414 0.730512 -0.0798338  -0.128449   -0.0942155  133 GLU   A CA   
3561 C C    . GLU   B 121 ? 0.640531 0.514362 0.761666 -0.0711195  -0.131456   -0.0874044  133 GLU   A C    
3562 O O    . GLU   B 121 ? 0.671056 0.537071 0.794058 -0.0829149  -0.125376   -0.0643071  133 GLU   A O    
3563 C CB   . GLU   B 121 ? 0.59034  0.514619 0.758638 -0.110501   -0.135383   -0.0871481  133 GLU   A CB   
3564 C CG   . GLU   B 121 ? 0.670162 0.540738 0.835522 -0.122226   -0.156205   -0.0992269  133 GLU   A CG   
3565 C CD   . GLU   B 121 ? 0.74231  0.626298 0.938234 -0.154963   -0.167491   -0.103048   133 GLU   A CD   
3566 O OE1  . GLU   B 121 ? 0.746719 0.690167 0.971433 -0.166298   -0.159621   -0.0954257  133 GLU   A OE1  
3567 O OE2  . GLU   B 121 ? 0.775678 0.611014 0.967569 -0.16817    -0.184563   -0.116464   133 GLU   A OE2  
3568 H H    . GLU   B 121 ? 0.563348 0.536564 0.712483 -0.084528   -0.0993943  -0.0710263  133 GLU   A H    
3569 H HA   . GLU   B 121 ? 0.594222 0.511646 0.724758 -0.0692221  -0.135737   -0.110737   133 GLU   A HA   
3570 H HB2  . GLU   B 121 ? 0.581767 0.539805 0.763813 -0.111937   -0.135567   -0.0924018  133 GLU   A HB2  
3571 H HB3  . GLU   B 121 ? 0.600172 0.530863 0.775682 -0.122122   -0.125433   -0.0698798  133 GLU   A HB3  
3572 H HG2  . GLU   B 121 ? 0.70287  0.538728 0.859749 -0.124399   -0.155257   -0.0883796  133 GLU   A HG2  
3573 H HG3  . GLU   B 121 ? 0.68035  0.538507 0.830082 -0.105791   -0.16388    -0.117006   133 GLU   A HG3  
3574 N N    . LEU   B 122 ? 0.625641 0.473468 0.728174 -0.0482605  -0.140336   -0.10695    134 LEU   A N    
3575 C CA   . LEU   B 122 ? 0.70216  0.506534 0.791153 -0.0322422  -0.146644   -0.103904   134 LEU   A CA   
3576 C C    . LEU   B 122 ? 0.805063 0.54578  0.896953 -0.0465206  -0.163499   -0.104753   134 LEU   A C    
3577 O O    . LEU   B 122 ? 0.894091 0.60755  0.981594 -0.0430916  -0.17617    -0.13076    134 LEU   A O    
3578 C CB   . LEU   B 122 ? 0.689934 0.499554 0.762717 2.575e-05   -0.146437   -0.12652    134 LEU   A CB   
3579 C CG   . LEU   B 122 ? 0.719339 0.491394 0.783259 0.0252902   -0.154198   -0.12579    134 LEU   A CG   
3580 C CD1  . LEU   B 122 ? 0.737745 0.518912 0.802003 0.0235496   -0.149086   -0.0943087  134 LEU   A CD1  
3581 C CD2  . LEU   B 122 ? 0.683828 0.478468 0.738875 0.0570057   -0.150495   -0.150214   134 LEU   A CD2  
3582 H H    . LEU   B 122 ? 0.631226 0.49034  0.72918  -0.04097    -0.142251   -0.12244    134 LEU   A H    
3583 H HA   . LEU   B 122 ? 0.693132 0.506628 0.781689 -0.0340149  -0.139333   -0.0851259  134 LEU   A HA   
3584 H HB2  . LEU   B 122 ? 0.651056 0.499062 0.722249 0.00427376  -0.134683   -0.124661   134 LEU   A HB2  
3585 H HB3  . LEU   B 122 ? 0.697322 0.500877 0.766663 0.00128904  -0.1523     -0.145387   134 LEU   A HB3  
3586 H HG   . LEU   B 122 ? 0.76535  0.490954 0.828583 0.0221664   -0.165642   -0.129611   134 LEU   A HG   
3587 H HD11 . LEU   B 122 ? 0.75149  0.509877 0.819002 0.00462348  -0.151864   -0.0781258  134 LEU   A HD11 
3588 H HD12 . LEU   B 122 ? 0.755003 0.521812 0.81382  0.0445557   -0.154591   -0.0937815  134 LEU   A HD12 
3589 H HD13 . LEU   B 122 ? 0.689767 0.514796 0.755324 0.0201865   -0.137511   -0.0910762  134 LEU   A HD13 
3590 H HD21 . LEU   B 122 ? 0.697432 0.487541 0.747558 0.0579739   -0.152892   -0.170199   134 LEU   A HD21 
3591 H HD22 . LEU   B 122 ? 0.652602 0.490061 0.708209 0.0575849   -0.139045   -0.146469   134 LEU   A HD22 
3592 H HD23 . LEU   B 122 ? 0.722257 0.494622 0.775648 0.0756031   -0.156761   -0.150135   134 LEU   A HD23 
3593 N N    . LEU   B 123 ? 0.85257  0.566313 0.947836 -0.064323   -0.162832   -0.0764198  135 LEU   A N    
3594 C CA   . LEU   B 123 ? 0.928105 0.575327 1.02598  -0.0864932  -0.175969   -0.0721306  135 LEU   A CA   
3595 C C    . LEU   B 123 ? 1.03438  0.609738 1.11192  -0.0574456  -0.188949   -0.0802642  135 LEU   A C    
3596 O O    . LEU   B 123 ? 1.0516   0.575257 1.12598  -0.0579893  -0.202578   -0.105075   135 LEU   A O    
3597 C CB   . LEU   B 123 ? 0.937251 0.583345 1.04185  -0.117807   -0.166808   -0.0348575  135 LEU   A CB   
3598 C CG   . LEU   B 123 ? 0.897921 0.618847 1.02637  -0.14358    -0.150854   -0.026366   135 LEU   A CG   
3599 C CD1  . LEU   B 123 ? 0.935069 0.654487 1.06253  -0.170365   -0.138354   0.0110165   135 LEU   A CD1  
3600 C CD2  . LEU   B 123 ? 0.912661 0.655034 1.06891  -0.168289   -0.158054   -0.047039   135 LEU   A CD2  
3601 H H    . LEU   B 123 ? 0.829972 0.565871 0.923638 -0.0641804  -0.153366   -0.0590419  135 LEU   A H    
3602 H HA   . LEU   B 123 ? 0.934546 0.585495 1.04256  -0.100264   -0.181897   -0.0892004  135 LEU   A HA   
3603 H HB2  . LEU   B 123 ? 0.948939 0.588723 1.03918  -0.103293   -0.163198   -0.0179186  135 LEU   A HB2  
3604 H HB3  . LEU   B 123 ? 0.996182 0.594029 1.10196  -0.136109   -0.174773   -0.0312489  135 LEU   A HB3  
3605 H HG   . LEU   B 123 ? 0.853111 0.615001 0.978667 -0.125616   -0.142799   -0.0312208  135 LEU   A HG   
3606 H HD11 . LEU   B 123 ? 0.936455 0.647299 1.0442   -0.153732   -0.135611   0.0244919   135 LEU   A HD11 
3607 H HD12 . LEU   B 123 ? 0.895251 0.665865 1.03876  -0.183626   -0.126337   0.0142103   135 LEU   A HD12 
3608 H HD13 . LEU   B 123 ? 0.982302 0.658937 1.11174  -0.191138   -0.144834   0.0180194   135 LEU   A HD13 
3609 H HD21 . LEU   B 123 ? 0.899445 0.637409 1.05045  -0.152243   -0.167194   -0.0698319  135 LEU   A HD21 
3610 H HD22 . LEU   B 123 ? 0.95158  0.660258 1.11406  -0.192338   -0.164012   -0.0418007  135 LEU   A HD22 
3611 H HD23 . LEU   B 123 ? 0.866321 0.661783 1.03889  -0.176152   -0.14775    -0.0429921  135 LEU   A HD23 
3612 N N    . ASP   B 124 ? 1.03733  0.611492 1.1015   -0.0307935  -0.185492   -0.0608515  136 ASP   A N    
3613 C CA   . ASP   B 124 ? 1.1179   0.625328 1.16622  0.00173926  -0.198311   -0.0616489  136 ASP   A CA   
3614 C C    . ASP   B 124 ? 1.10307  0.652762 1.1439   0.0375033   -0.19376    -0.049378   136 ASP   A C    
3615 O O    . ASP   B 124 ? 1.0072   0.622597 1.05058  0.0277878   -0.180724   -0.0337467  136 ASP   A O    
3616 C CB   . ASP   B 124 ? 1.19237  0.61383  1.23165  -0.0187801  -0.207145   -0.0335329  136 ASP   A CB   
3617 C CG   . ASP   B 124 ? 1.34718  0.673209 1.37257  0.00958974  -0.223917   -0.0461466  136 ASP   A CG   
3618 O OD1  . ASP   B 124 ? 1.4086   0.740655 1.43455  0.0436183   -0.22821    -0.083496   136 ASP   A OD1  
3619 O OD2  . ASP   B 124 ? 1.40276  0.647006 1.41513  -0.00193719 -0.231186   -0.0184352  136 ASP   A OD2  
3620 H H    . ASP   B 124 ? 0.999839 0.61738  1.06521  -0.0318635  -0.175508   -0.0472117  136 ASP   A H    
3621 H HA   . ASP   B 124 ? 1.12799  0.619817 1.17584  0.0148571   -0.204295   -0.0899751  136 ASP   A HA   
3622 H HB2  . ASP   B 124 ? 1.21293  0.629382 1.26165  -0.0523268  -0.205775   -0.0344068  136 ASP   A HB2  
3623 H HB3  . ASP   B 124 ? 1.2098   0.640443 1.24189  -0.0197965  -0.202733   -0.00412373 136 ASP   A HB3  
3624 N N    . PHE   B 125 ? 1.13113  0.645988 1.16455  0.0795618   -0.204844   -0.060054   137 PHE   A N    
3625 C CA   . PHE   B 125 ? 1.07551  0.630334 1.10565  0.115512    -0.205226   -0.0477977  137 PHE   A CA   
3626 C C    . PHE   B 125 ? 1.13261  0.618068 1.15476  0.157882    -0.222798   -0.0454751  137 PHE   A C    
3627 O O    . PHE   B 125 ? 1.18856  0.623721 1.21221  0.174981    -0.229641   -0.0758331  137 PHE   A O    
3628 C CB   . PHE   B 125 ? 0.9568   0.599648 0.998429 0.132646    -0.193562   -0.0763288  137 PHE   A CB   
3629 C CG   . PHE   B 125 ? 0.964576 0.60289  1.01115  0.153772    -0.194034   -0.120226   137 PHE   A CG   
3630 C CD1  . PHE   B 125 ? 0.964335 0.609688 1.01128  0.128374    -0.187551   -0.143289   137 PHE   A CD1  
3631 C CD2  . PHE   B 125 ? 1.01102  0.648206 1.06141  0.200512    -0.200171   -0.139074   137 PHE   A CD2  
3632 C CE1  . PHE   B 125 ? 1.00012  0.64842  1.04436  0.146595    -0.186637   -0.183281   137 PHE   A CE1  
3633 C CE2  . PHE   B 125 ? 1.03465  0.676354 1.08689  0.219103    -0.196659   -0.18176    137 PHE   A CE2  
3634 C CZ   . PHE   B 125 ? 0.98088  0.626831 1.02666  0.190791    -0.189587   -0.203429   137 PHE   A CZ   
3635 H H    . PHE   B 125 ? 1.16745  0.635366 1.19912  0.0866093   -0.212703   -0.0770626  137 PHE   A H    
3636 H HA   . PHE   B 125 ? 1.0608   0.631579 1.08552  0.100786    -0.201662   -0.0199811  137 PHE   A HA   
3637 H HB2  . PHE   B 125 ? 0.962056 0.633627 1.00386  0.153525    -0.195071   -0.0674666  137 PHE   A HB2  
3638 H HB3  . PHE   B 125 ? 0.917652 0.599191 0.962275 0.107783    -0.182642   -0.0738338  137 PHE   A HB3  
3639 H HD1  . PHE   B 125 ? 0.941556 0.594445 0.989919 0.0995549   -0.183577   -0.131764   137 PHE   A HD1  
3640 H HD2  . PHE   B 125 ? 1.03221  0.669128 1.08377  0.220998    -0.206628   -0.122984   137 PHE   A HD2  
3641 H HE1  . PHE   B 125 ? 0.966281 0.620007 1.00724  0.129469    -0.184076   -0.197124   137 PHE   A HE1  
3642 H HE2  . PHE   B 125 ? 1.0471   0.691671 1.10426  0.252344    -0.199358   -0.195775   137 PHE   A HE2  
3643 H HZ   . PHE   B 125 ? 1.00961  0.658477 1.05186  0.20257     -0.187242   -0.231945   137 PHE   A HZ   
3644 N N    . LYS   B 126 ? 1.14574  0.631631 1.15768  0.177011    -0.230381   -0.0101931  138 LYS   A N    
3645 C CA   . LYS   B 126 ? 1.22082  0.640894 1.22381  0.222422    -0.249326   0.0016457   138 LYS   A CA   
3646 C C    . LYS   B 126 ? 1.18959  0.69008  1.20152  0.265969    -0.253687   0.00412002  138 LYS   A C    
3647 O O    . LYS   B 126 ? 1.09821  0.679736 1.11035  0.249238    -0.245126   0.0177268   138 LYS   A O    
3648 C CB   . LYS   B 126 ? 1.27522  0.61216  1.25215  0.201022    -0.257944   0.0512551   138 LYS   A CB   
3649 H H    . LYS   B 126 ? 1.10938  0.639596 1.11864  0.162353    -0.223954   0.00749284  138 LYS   A H    
3650 H HA   . LYS   B 126 ? 1.25088  0.630252 1.25864  0.237728    -0.253262   -0.0247341  138 LYS   A HA   
3653 N N    . GLY   B 127 ? 1.26529  0.747306 1.28653  0.321774    -0.266951   -0.0114632  139 GLY   A N    
3654 C CA   . GLY   B 127 ? 1.24968  0.819211 1.28669  0.364266    -0.272865   -0.0117944  139 GLY   A CA   
3655 C C    . GLY   B 127 ? 1.32369  0.877326 1.3396   0.378388    -0.291151   0.0409379   139 GLY   A C    
3656 O O    . GLY   B 127 ? 1.4336   0.882265 1.42897  0.392994    -0.306457   0.0674597   139 GLY   A O    
3657 H H    . GLY   B 127 ? 1.3149   0.731335 1.33417  0.333833    -0.272465   -0.0235393  139 GLY   A H    
3658 H HA2  . GLY   B 127 ? 1.1755   0.822529 1.22258  0.34655     -0.260218   -0.0237068  139 GLY   A HA2  
3659 H HA3  . GLY   B 127 ? 1.27585  0.84024  1.3269   0.401761    -0.277605   -0.0354615  139 GLY   A HA3  
3660 N N    . GLU   B 128 ? 1.27781  0.932298 1.29574  0.374353    -0.290176   0.0551597   140 GLU   A N    
3661 C CA   . GLU   B 128 ? 1.31304  0.966683 1.30376  0.381748    -0.307198   0.106207    140 GLU   A CA   
3662 C C    . GLU   B 128 ? 1.45755  1.01353  1.43563  0.434482    -0.333499   0.131672    140 GLU   A C    
3663 O O    . GLU   B 128 ? 1.48558  1.03191  1.49071  0.484887    -0.34099    0.10034     140 GLU   A O    
3664 C CB   . GLU   B 128 ? 1.21897  1.0024   1.22099  0.391172    -0.309873   0.1052      140 GLU   A CB   
3665 O OXT  . GLU   B 128 ? 1.53705  1.02415  1.47651  0.423308    -0.34417    0.182289    140 GLU   A OXT  
3666 H H    . GLU   B 128 ? 1.20412  0.929487 1.23867  0.365495    -0.278542   0.0317958   140 GLU   A H    
3667 H HA   . GLU   B 128 ? 1.31567  0.941323 1.28464  0.342588    -0.299692   0.127365    140 GLU   A HA   
3670 C CAK  . A1IN3 C .   ? 0.634866 0.557491 0.533479 -0.13946    0.234196    -0.037981   201 A1IN3 B CAK  
3671 C CAL  . A1IN3 C .   ? 0.700948 0.56308  0.549943 -0.129098   0.222221    -0.0212706  201 A1IN3 B CAL  
3672 C CAM  . A1IN3 C .   ? 0.684908 0.490598 0.54647  -0.138004   0.194432    -0.0316296  201 A1IN3 B CAM  
3673 C CAN  . A1IN3 C .   ? 0.642689 0.475755 0.519911 -0.129806   0.18218     -0.0619061  201 A1IN3 B CAN  
3674 C CAO  . A1IN3 C .   ? 0.594114 0.481019 0.528027 -0.143161   0.190285    -0.0753434  201 A1IN3 B CAO  
3675 C CAJ  . A1IN3 C .   ? 0.581527 0.519701 0.502208 -0.13316    0.216446    -0.0713849  201 A1IN3 B CAJ  
3676 C CAI  . A1IN3 C .   ? 0.549114 0.543309 0.51878  -0.137104   0.226847    -0.0918598  201 A1IN3 B CAI  
3677 C CAB  . A1IN3 C .   ? 0.528151 0.531418 0.507382 -0.127275   0.211326    -0.120877   201 A1IN3 B CAB  
3678 O OAA  . A1IN3 C .   ? 0.523391 0.517681 0.467537 -0.113932   0.202276    -0.127547   201 A1IN3 B OAA  
3679 N N    . A1IN3 C .   ? 0.509475 0.531007 0.54021  -0.132044   0.20568     -0.140108   201 A1IN3 B N    
3680 C CAH  . A1IN3 C .   ? 0.5121   0.565762 0.599094 -0.143354   0.219152    -0.137247   201 A1IN3 B CAH  
3681 C CAG  . A1IN3 C .   ? 0.494971 0.544861 0.636633 -0.149179   0.199751    -0.149328   201 A1IN3 B CAG  
3682 C CAF  . A1IN3 C .   ? 0.48076  0.533432 0.621747 -0.133979   0.190205    -0.175834   201 A1IN3 B CAF  
3683 C CB   . A1IN3 C .   ? 0.472435 0.48395  0.561443 -0.130107   0.174547    -0.17407    201 A1IN3 B CB   
3684 C CA   . A1IN3 C .   ? 0.491417 0.515312 0.528975 -0.122786   0.191776    -0.165866   201 A1IN3 B CA   
3685 C C    . A1IN3 C .   ? 0.511308 0.577019 0.54694  -0.110459   0.204487    -0.188203   201 A1IN3 B C    
3686 O O    . A1IN3 C .   ? 0.500888 0.567433 0.548497 -0.105589   0.19346     -0.211364   201 A1IN3 B O    
3687 O OBC  . A1IN3 C .   ? 0.553521 0.649777 0.564696 -0.104726   0.227098    -0.180389   201 A1IN3 B OBC  
3688 C CBB  . A1IN3 C .   ? 0.576733 0.711956 0.575575 -0.0894329  0.236277    -0.207438   201 A1IN3 B CBB  
3689 C CBA  . A1IN3 C .   ? 0.583139 0.758157 0.568067 -0.0822563  0.265312    -0.202085   201 A1IN3 B CBA  
3690 C CAZ  . A1IN3 C .   ? 0.618651 0.801364 0.636628 -0.0952591  0.284073    -0.177265   201 A1IN3 B CAZ  
3691 C CAY  . A1IN3 C .   ? 0.654712 0.871441 0.649177 -0.092373   0.317395    -0.157112   201 A1IN3 B CAY  
3692 C CAX  . A1IN3 C .   ? 0.660273 0.896942 0.586578 -0.0735823  0.328847    -0.159533   201 A1IN3 B CAX  
3693 C CAW  . A1IN3 C .   ? 0.709682 0.950619 0.602994 -0.0793164  0.356567    -0.115547   201 A1IN3 B CAW  
3694 O OAV  . A1IN3 C .   ? 0.674723 0.858436 0.537589 -0.0878092  0.336848    -0.0849101  201 A1IN3 B OAV  
3695 C CAU  . A1IN3 C .   ? 0.640813 0.778963 0.543727 -0.104652   0.31138     -0.0836297  201 A1IN3 B CAU  
3696 C CAR  . A1IN3 C .   ? 0.634056 0.744434 0.515602 -0.0948622  0.281996    -0.0995375  201 A1IN3 B CAR  
3697 O OAS  . A1IN3 C .   ? 0.684171 0.819463 0.520274 -0.0735153  0.279371    -0.115169   201 A1IN3 B OAS  
3698 C CAT  . A1IN3 C .   ? 0.776638 0.888401 0.561673 -0.0608653  0.266621    -0.0983177  201 A1IN3 B CAT  
3699 C CAQ  . A1IN3 C .   ? 0.593547 0.659114 0.500505 -0.105842   0.257068    -0.101151   201 A1IN3 B CAQ  
3700 C CAP  . A1IN3 C .   ? 0.583479 0.626358 0.537408 -0.128276   0.25521     -0.0881636  201 A1IN3 B CAP  
3701 C CBI  . A1IN3 C .   ? 0.581818 0.656111 0.568322 -0.14156    0.281641    -0.0723924  201 A1IN3 B CBI  
3702 C CBF  . A1IN3 C .   ? 0.621304 0.745257 0.582836 -0.129398   0.313092    -0.0687838  201 A1IN3 B CBF  
3703 O OBG  . A1IN3 C .   ? 0.683659 0.845199 0.672004 -0.140171   0.345975    -0.0496618  201 A1IN3 B OBG  
3704 C CBH  . A1IN3 C .   ? 0.65908  0.828923 0.729867 -0.165262   0.346328    -0.0443184  201 A1IN3 B CBH  
3705 H HAK  . A1IN3 C .   ? 0.646059 0.607388 0.531548 -0.130734   0.251929    -0.0367437  201 A1IN3 B HAK  
3706 H HB6  . A1IN3 C .   ? 0.657426 0.564357 0.587549 -0.160401   0.235512    -0.0250475  201 A1IN3 B HB6  
3707 H HAL  . A1IN3 C .   ? 0.735849 0.579419 0.57216  -0.135941   0.234413    0.00568238  201 A1IN3 B HAL  
3708 H HB7  . A1IN3 C .   ? 0.685358 0.560212 0.500519 -0.106888   0.22012     -0.0285905  201 A1IN3 B HB7  
3709 H HAM  . A1IN3 C .   ? 0.700366 0.493523 0.598067 -0.161114   0.191714    -0.0253633  201 A1IN3 B HAM  
3710 H HB8  . A1IN3 C .   ? 0.722449 0.482638 0.544603 -0.125613   0.186297    -0.0235883  201 A1IN3 B HB8  
3711 H HAN  . A1IN3 C .   ? 0.642585 0.436909 0.517687 -0.132274   0.16348     -0.0681692  201 A1IN3 B HAN  
3712 H HB9  . A1IN3 C .   ? 0.627741 0.479109 0.477843 -0.110598   0.185304    -0.0678387  201 A1IN3 B HB9  
3713 H HCA  . A1IN3 C .   ? 0.562383 0.463985 0.508906 -0.138112   0.181998    -0.0943112  201 A1IN3 B HCA  
3714 H HAO  . A1IN3 C .   ? 0.602537 0.487246 0.570017 -0.161356   0.191953    -0.0667448  201 A1IN3 B HAO  
3715 H HAJ  . A1IN3 C .   ? 0.579841 0.524293 0.467394 -0.115253   0.213451    -0.0789942  201 A1IN3 B HAJ  
3716 H HAI  . A1IN3 C .   ? 0.554615 0.544432 0.565952 -0.15392    0.224631    -0.0866833  201 A1IN3 B HAI  
3717 H HAH  . A1IN3 C .   ? 0.516658 0.61104  0.605297 -0.133762   0.238488    -0.147484   201 A1IN3 B HAH  
3718 H HB5  . A1IN3 C .   ? 0.533193 0.576425 0.620758 -0.155965   0.225669    -0.114882   201 A1IN3 B HB5  
3719 H HAG  . A1IN3 C .   ? 0.495429 0.578482 0.682666 -0.153508   0.210276    -0.149931   201 A1IN3 B HAG  
3720 H HB4  . A1IN3 C .   ? 0.496919 0.508283 0.633951 -0.156736   0.178861    -0.142449   201 A1IN3 B HB4  
3721 H HAF  . A1IN3 C .   ? 0.480454 0.563008 0.616097 -0.123291   0.205209    -0.189871   201 A1IN3 B HAF  
3722 H HB3  . A1IN3 C .   ? 0.469099 0.513773 0.644379 -0.135091   0.174493    -0.182884   201 A1IN3 B HB3  
3723 H HB2  . A1IN3 C .   ? 0.481276 0.458882 0.556942 -0.136748   0.162037    -0.160572   201 A1IN3 B HB2  
3724 H HB1  . A1IN3 C .   ? 0.465851 0.47633  0.555043 -0.123697   0.168101    -0.18886    201 A1IN3 B HB1  
3725 H HA   . A1IN3 C .   ? 0.492463 0.491999 0.500206 -0.119362   0.181512    -0.162327   201 A1IN3 B HA   
3726 H HCG  . A1IN3 C .   ? 0.57561  0.711412 0.537396 -0.082232   0.230737    -0.209216   201 A1IN3 B HCG  
3727 H HBB  . A1IN3 C .   ? 0.557971 0.700872 0.587644 -0.0860001  0.23076     -0.233179   201 A1IN3 B HBB  
3728 H HCF  . A1IN3 C .   ? 0.618346 0.797001 0.557145 -0.0759453  0.270502    -0.190277   201 A1IN3 B HCF  
3729 H HBA  . A1IN3 C .   ? 0.599573 0.799513 0.599755 -0.072064   0.269433    -0.230813   201 A1IN3 B HBA  
3730 H HAZ  . A1IN3 C .   ? 0.587977 0.755058 0.652808 -0.107534   0.273286    -0.174481   201 A1IN3 B HAZ  
3731 H HAY  . A1IN3 C .   ? 0.652988 0.879597 0.682946 -0.106367   0.333136    -0.136416   201 A1IN3 B HAY  
3732 H HCE  . A1IN3 C .   ? 0.665516 0.880189 0.55719  -0.0684183  0.309875    -0.160923   201 A1IN3 B HCE  
3733 H HAX  . A1IN3 C .   ? 0.67999  0.951922 0.605952 -0.0587358  0.338943    -0.187636   201 A1IN3 B HAX  
3734 H HCD  . A1IN3 C .   ? 0.739419 1.0001   0.577219 -0.0632752  0.369221    -0.112813   201 A1IN3 B HCD  
3735 H HAW  . A1IN3 C .   ? 0.701498 0.951329 0.636343 -0.094805   0.373598    -0.0976298  201 A1IN3 B HAW  
3736 H HCC  . A1IN3 C .   ? 0.767179 0.908928 0.520253 -0.0437635  0.263376    -0.112961   201 A1IN3 B HCC  
3737 H HAT  . A1IN3 C .   ? 0.724518 0.808531 0.52415  -0.0640538  0.247304    -0.103188   201 A1IN3 B HAT  
3738 H HCB  . A1IN3 C .   ? 0.787941 0.879872 0.550745 -0.063621   0.278958    -0.0657209  201 A1IN3 B HCB  
3739 H HAQ  . A1IN3 C .   ? 0.580012 0.631625 0.470592 -0.0970034  0.239319    -0.112284   201 A1IN3 B HAQ  
3740 H HBI  . A1IN3 C .   ? 0.588285 0.651067 0.619457 -0.161001   0.277643    -0.0631358  201 A1IN3 B HBI  
3741 H HCI  . A1IN3 C .   ? 0.682264 0.898707 0.776472 -0.169337   0.377914    -0.0330832  201 A1IN3 B HCI  
3742 H HBH  . A1IN3 C .   ? 0.671866 0.796306 0.747731 -0.183874   0.333096    -0.0227416  201 A1IN3 B HBH  
3743 H HCH  . A1IN3 C .   ? 0.621682 0.797397 0.727413 -0.160897   0.327811    -0.0728031  201 A1IN3 B HCH  
3744 C CAK  . A1IN3 D .   ? 0.512325 0.760002 0.575373 -0.110275   0.135377    -0.0965933  201 A1IN3 A CAK  
3745 C CAL  . A1IN3 D .   ? 0.51843  0.760633 0.600279 -0.0930306  0.152945    -0.118334   201 A1IN3 A CAL  
3746 C CAM  . A1IN3 D .   ? 0.49801  0.715266 0.608767 -0.0746116  0.137759    -0.115299   201 A1IN3 A CAM  
3747 C CAN  . A1IN3 D .   ? 0.495988 0.676929 0.584764 -0.0741954  0.118033    -0.114565   201 A1IN3 A CAN  
3748 C CAO  . A1IN3 D .   ? 0.483787 0.670647 0.559772 -0.0881632  0.100298    -0.0976343  201 A1IN3 A CAO  
3749 C CAJ  . A1IN3 D .   ? 0.49536  0.708788 0.544915 -0.104522   0.112224    -0.0966243  201 A1IN3 A CAJ  
3750 C CAI  . A1IN3 D .   ? 0.478927 0.691979 0.513233 -0.114042   0.0904875   -0.0733918  201 A1IN3 A CAI  
3751 C CAB  . A1IN3 D .   ? 0.479059 0.673277 0.500208 -0.106565   0.073757    -0.0794024  201 A1IN3 A CAB  
3752 O OAA  . A1IN3 D .   ? 0.450115 0.640598 0.46128  -0.103958   0.0825835   -0.101509   201 A1IN3 A OAA  
3753 N N    . A1IN3 D .   ? 0.441401 0.620654 0.463255 -0.102454   0.0495271   -0.0620039  201 A1IN3 A N    
3754 C CAH  . A1IN3 D .   ? 0.477401 0.651622 0.504824 -0.110839   0.0402551   -0.0341951  201 A1IN3 A CAH  
3755 C CAG  . A1IN3 D .   ? 0.483025 0.623208 0.522526 -0.101743   0.0161617   -0.0240224  201 A1IN3 A CAG  
3756 C CAF  . A1IN3 D .   ? 0.483512 0.616653 0.507057 -0.0874553  0.00070372  -0.0291384  201 A1IN3 A CAF  
3757 C CB   . A1IN3 D .   ? 0.455535 0.596376 0.483032 -0.0798229  0.00948126  -0.0560997  201 A1IN3 A CB   
3758 C CA   . A1IN3 D .   ? 0.448057 0.618547 0.460711 -0.0918261  0.0331027   -0.0693251  201 A1IN3 A CA   
3759 C C    . A1IN3 D .   ? 0.492632 0.689137 0.478754 -0.09742    0.0299667   -0.0665555  201 A1IN3 A C    
3760 O O    . A1IN3 D .   ? 0.477108 0.683591 0.456062 -0.090344   0.0177854   -0.0727874  201 A1IN3 A O    
3761 O OBC  . A1IN3 D .   ? 0.503506 0.721377 0.472027 -0.111534   0.0425075   -0.058254   201 A1IN3 A OBC  
3762 C CBB  . A1IN3 D .   ? 0.570305 0.810237 0.509033 -0.113978   0.0296012   -0.0441544  201 A1IN3 A CBB  
3763 C CBA  . A1IN3 D .   ? 0.592206 0.854622 0.509338 -0.131619   0.0483811   -0.0367719  201 A1IN3 A CBA  
3764 C CAZ  . A1IN3 D .   ? 0.615504 0.863342 0.529647 -0.136541   0.0411854   -0.00147247 201 A1IN3 A CAZ  
3765 C CAY  . A1IN3 D .   ? 0.632153 0.899015 0.526955 -0.155034   0.0578784   0.0146651   201 A1IN3 A CAY  
3766 C CAX  . A1IN3 D .   ? 0.649805 0.956416 0.519547 -0.166155   0.0801691   -0.00529283 201 A1IN3 A CAX  
3767 C CAW  . A1IN3 D .   ? 0.648785 0.974379 0.520672 -0.183052   0.107557    0.00112983  201 A1IN3 A CAW  
3768 O OAV  . A1IN3 D .   ? 0.644146 0.973523 0.54678  -0.176396   0.127693    -0.0334148  201 A1IN3 A OAV  
3769 C CAU  . A1IN3 D .   ? 0.59568  0.894208 0.538068 -0.160478   0.118252    -0.0442881  201 A1IN3 A CAU  
3770 C CAR  . A1IN3 D .   ? 0.599258 0.886235 0.541001 -0.149331   0.115894    -0.0726435  201 A1IN3 A CAR  
3771 O OAS  . A1IN3 D .   ? 0.630714 0.939502 0.535418 -0.156927   0.121047    -0.0901338  201 A1IN3 A OAS  
3772 C CAT  . A1IN3 D .   ? 0.608279 0.90654  0.512947 -0.153087   0.125776    -0.122747   201 A1IN3 A CAT  
3773 C CAQ  . A1IN3 D .   ? 0.508704 0.76536  0.482126 -0.134623   0.107924    -0.0810843  201 A1IN3 A CAQ  
3774 C CAP  . A1IN3 D .   ? 0.553845 0.794491 0.561401 -0.129461   0.0995011   -0.0643013  201 A1IN3 A CAP  
3775 C CBI  . A1IN3 D .   ? 0.560591 0.814986 0.572821 -0.142896   0.101461    -0.0393675  201 A1IN3 A CBI  
3776 C CBF  . A1IN3 D .   ? 0.565054 0.846363 0.544173 -0.159079   0.111806    -0.027366   201 A1IN3 A CBF  
3777 O OBG  . A1IN3 D .   ? 0.623907 0.918069 0.601092 -0.17695    0.117157    -1.957e-05  201 A1IN3 A OBG  
3778 C CBH  . A1IN3 D .   ? 0.590382 0.860681 0.599274 -0.181945   0.103414    0.0215992   201 A1IN3 A CBH  
3779 H HAK  . A1IN3 D .   ? 0.531124 0.792538 0.566301 -0.120641   0.143514    -0.100072   201 A1IN3 A HAK  
3780 H HB6  . A1IN3 D .   ? 0.508117 0.760601 0.587522 -0.116244   0.123476    -0.0761559  201 A1IN3 A HB6  
3781 H HAL  . A1IN3 D .   ? 0.527498 0.79928  0.624193 -0.0939925  0.169576    -0.119882   201 A1IN3 A HAL  
3782 H HB7  . A1IN3 D .   ? 0.530237 0.758552 0.588469 -0.0923472  0.162114    -0.136453   201 A1IN3 A HB7  
3783 H HAM  . A1IN3 D .   ? 0.489903 0.72321  0.62592  -0.077032   0.128109    -0.100446   201 A1IN3 A HAM  
3784 H HB8  . A1IN3 D .   ? 0.508829 0.71935  0.62929  -0.0595835  0.150663    -0.129043   201 A1IN3 A HB8  
3785 H HAN  . A1IN3 D .   ? 0.482224 0.646331 0.586375 -0.0621078  0.107202    -0.11173    201 A1IN3 A HAN  
3786 H HB9  . A1IN3 D .   ? 0.504261 0.672128 0.570967 -0.0750976  0.128298    -0.130228   201 A1IN3 A HB9  
3787 H HCA  . A1IN3 D .   ? 0.477589 0.647448 0.539412 -0.0864853  0.0898158   -0.100417   201 A1IN3 A HCA  
3788 H HAO  . A1IN3 D .   ? 0.478334 0.671824 0.572038 -0.0913602  0.0904946   -0.0824233  201 A1IN3 A HAO  
3789 H HAJ  . A1IN3 D .   ? 0.501489 0.710845 0.530263 -0.105249   0.120536    -0.113837   201 A1IN3 A HAJ  
3790 H HAI  . A1IN3 D .   ? 0.487759 0.694089 0.54354  -0.113887   0.0811295   -0.0592164  201 A1IN3 A HAI  
3791 H HAH  . A1IN3 D .   ? 0.497672 0.684451 0.501791 -0.118089   0.0400052   -0.0229405  201 A1IN3 A HAH  
3792 H HB5  . A1IN3 D .   ? 0.474606 0.657391 0.519436 -0.117616   0.0516341   -0.0321338  201 A1IN3 A HB5  
3793 H HAG  . A1IN3 D .   ? 0.505691 0.633691 0.54285  -0.108748   0.0078151   -0.00389789 201 A1IN3 A HAG  
3794 H HB4  . A1IN3 D .   ? 0.464414 0.593524 0.522827 -0.095395   0.0140246   -0.0336814  201 A1IN3 A HB4  
3795 H HAF  . A1IN3 D .   ? 0.497081 0.64812  0.500263 -0.0897385  0.00115918  -0.0251651  201 A1IN3 A HAF  
3796 H HB3  . A1IN3 D .   ? 0.488223 0.596862 0.518672 -0.0781865  -0.015205   -0.024885   201 A1IN3 A HB3  
3797 H HB2  . A1IN3 D .   ? 0.440338 0.570089 0.483285 -0.0772284  0.0132299   -0.0630059  201 A1IN3 A HB2  
3798 H HB1  . A1IN3 D .   ? 0.452597 0.595369 0.473267 -0.0712708  0.00015131  -0.0615299  201 A1IN3 A HB1  
3799 H HA   . A1IN3 D .   ? 0.438882 0.605892 0.454004 -0.0886876  0.0410882   -0.0874361  201 A1IN3 A HA   
3800 H HCG  . A1IN3 D .   ? 0.561427 0.823858 0.486933 -0.114808   0.0286682   -0.0591746  201 A1IN3 A HCG  
3801 H HBB  . A1IN3 D .   ? 0.575521 0.801098 0.512993 -0.107308   0.0124119   -0.0218723  201 A1IN3 A HBB  
3802 H HCF  . A1IN3 D .   ? 0.579101 0.836572 0.512971 -0.134692   0.064451    -0.0464986  201 A1IN3 A HCF  
3803 H HBA  . A1IN3 D .   ? 0.606903 0.897595 0.499186 -0.139235   0.0551449   -0.0484179  201 A1IN3 A HBA  
3804 H HAZ  . A1IN3 D .   ? 0.609092 0.826265 0.539672 -0.127617   0.0250504   0.0118267   201 A1IN3 A HAZ  
3805 H HAY  . A1IN3 D .   ? 0.661563 0.912618 0.554692 -0.161825   0.0527194   0.0429052   201 A1IN3 A HAY  
3806 H HCE  . A1IN3 D .   ? 0.620763 0.929677 0.502887 -0.161407   0.0887338   -0.0331197  201 A1IN3 A HCE  
3807 H HAX  . A1IN3 D .   ? 0.671196 0.998033 0.506477 -0.169911   0.0745167   -0.00056387 201 A1IN3 A HAX  
3808 H HCD  . A1IN3 D .   ? 0.687181 1.04366  0.528688 -0.194009   0.122764    -0.00374424 201 A1IN3 A HCD  
3809 H HAW  . A1IN3 D .   ? 0.657889 0.969535 0.553002 -0.187188   0.107915    0.0184181   201 A1IN3 A HAW  
3810 H HCC  . A1IN3 D .   ? 0.635371 0.955814 0.510469 -0.163847   0.132791    -0.138101   201 A1IN3 A HCC  
3811 H HAT  . A1IN3 D .   ? 0.592826 0.87768  0.50511  -0.14625    0.107151    -0.119004   201 A1IN3 A HAT  
3812 H HCB  . A1IN3 D .   ? 0.602168 0.884687 0.527027 -0.147013   0.141391    -0.136724   201 A1IN3 A HCB  
3813 H HAQ  . A1IN3 D .   ? 0.524409 0.770342 0.494807 -0.129053   0.107944    -0.100614   201 A1IN3 A HAQ  
3814 H HBI  . A1IN3 D .   ? 0.547827 0.792309 0.587816 -0.142833   0.0948661   -0.0289584  201 A1IN3 A HBI  
3815 H HCI  . A1IN3 D .   ? 0.632235 0.910074 0.630139 -0.200414   0.10829     0.0451281   201 A1IN3 A HCI  
3816 H HBH  . A1IN3 D .   ? 0.576357 0.85564  0.621286 -0.177776   0.111276    0.00855806  201 A1IN3 A HBH  
3817 H HCH  . A1IN3 D .   ? 0.592807 0.829341 0.599555 -0.171862   0.0804861   0.0266852   201 A1IN3 A HCH  
# 
