data_9GQB
# 
_entry.id   9GQB 
# 
_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   9GQB         pdb_00009gqb 10.2210/pdb9gqb/pdb 
WWPDB D_1292141289 ?            ?                   
# 
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                        9GQB 
_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~{S},15~{S})-2-cyclohexyl-19,22-dimethoxy-14,15-bis(oxidanyl)-11,17-dioxa-4-azatricyclo[16.2.2.0^{4,9}]docosa-1(21),18(22),19-triene-3,10-dione
;
505.600   2  ?       ?                    ? ? 
3 water       nat water 18.015    65 ?       ?                    ? ? 
# 
_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~{S},15~{S})-2-cyclohexyl-19,22-dimethoxy-14,15-bis(oxidanyl)-11,17-dioxa-4-azatricyclo[16.2.2.0^{4,9}]docosa-1(21),18(22),19-triene-3,10-dione
;
A1IN8 
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 
A1IN8 non-polymer         . 
;(2~{S},9~{S},14~{S},15~{S})-2-cyclohexyl-19,22-dimethoxy-14,15-bis(oxidanyl)-11,17-dioxa-4-azatricyclo[16.2.2.0^{4,9}]docosa-1(21),18(22),19-triene-3,10-dione
;
? 'C27 H39 N O8'   505.600 
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        A1IN8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IN8 
_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 A1IN8 1  201 201 A1IN8 DRG B . 
D 2 A1IN8 1  201 201 A1IN8 DRG A . 
E 3 HOH   1  301 42  HOH   HOH B . 
E 3 HOH   2  302 60  HOH   HOH B . 
E 3 HOH   3  303 19  HOH   HOH B . 
E 3 HOH   4  304 26  HOH   HOH B . 
E 3 HOH   5  305 44  HOH   HOH B . 
E 3 HOH   6  306 36  HOH   HOH B . 
E 3 HOH   7  307 2   HOH   HOH B . 
E 3 HOH   8  308 14  HOH   HOH B . 
E 3 HOH   9  309 7   HOH   HOH B . 
E 3 HOH   10 310 38  HOH   HOH B . 
E 3 HOH   11 311 22  HOH   HOH B . 
E 3 HOH   12 312 45  HOH   HOH B . 
E 3 HOH   13 313 23  HOH   HOH B . 
E 3 HOH   14 314 13  HOH   HOH B . 
E 3 HOH   15 315 18  HOH   HOH B . 
E 3 HOH   16 316 40  HOH   HOH B . 
E 3 HOH   17 317 9   HOH   HOH B . 
E 3 HOH   18 318 17  HOH   HOH B . 
E 3 HOH   19 319 12  HOH   HOH B . 
E 3 HOH   20 320 3   HOH   HOH B . 
E 3 HOH   21 321 16  HOH   HOH B . 
E 3 HOH   22 322 59  HOH   HOH B . 
E 3 HOH   23 323 43  HOH   HOH B . 
E 3 HOH   24 324 64  HOH   HOH B . 
E 3 HOH   25 325 41  HOH   HOH B . 
E 3 HOH   26 326 54  HOH   HOH B . 
E 3 HOH   27 327 65  HOH   HOH B . 
E 3 HOH   28 328 56  HOH   HOH B . 
E 3 HOH   29 329 58  HOH   HOH B . 
E 3 HOH   30 330 67  HOH   HOH B . 
F 3 HOH   1  301 53  HOH   HOH A . 
F 3 HOH   2  302 57  HOH   HOH A . 
F 3 HOH   3  303 20  HOH   HOH A . 
F 3 HOH   4  304 46  HOH   HOH A . 
F 3 HOH   5  305 37  HOH   HOH A . 
F 3 HOH   6  306 1   HOH   HOH A . 
F 3 HOH   7  307 29  HOH   HOH A . 
F 3 HOH   8  308 11  HOH   HOH A . 
F 3 HOH   9  309 8   HOH   HOH A . 
F 3 HOH   10 310 15  HOH   HOH A . 
F 3 HOH   11 311 4   HOH   HOH A . 
F 3 HOH   12 312 21  HOH   HOH A . 
F 3 HOH   13 313 34  HOH   HOH A . 
F 3 HOH   14 314 52  HOH   HOH A . 
F 3 HOH   15 315 35  HOH   HOH A . 
F 3 HOH   16 316 32  HOH   HOH A . 
F 3 HOH   17 317 31  HOH   HOH A . 
F 3 HOH   18 318 39  HOH   HOH A . 
F 3 HOH   19 319 27  HOH   HOH A . 
F 3 HOH   20 320 28  HOH   HOH A . 
F 3 HOH   21 321 5   HOH   HOH A . 
F 3 HOH   22 322 33  HOH   HOH A . 
F 3 HOH   23 323 24  HOH   HOH A . 
F 3 HOH   24 324 30  HOH   HOH A . 
F 3 HOH   25 325 63  HOH   HOH A . 
F 3 HOH   26 326 49  HOH   HOH A . 
F 3 HOH   27 327 10  HOH   HOH A . 
F 3 HOH   28 328 50  HOH   HOH A . 
F 3 HOH   29 329 48  HOH   HOH A . 
F 3 HOH   30 330 55  HOH   HOH A . 
F 3 HOH   31 331 47  HOH   HOH A . 
F 3 HOH   32 332 62  HOH   HOH A . 
F 3 HOH   33 333 25  HOH   HOH A . 
F 3 HOH   34 334 51  HOH   HOH A . 
F 3 HOH   35 335 61  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 B GLU 44  ? CG  ? A GLU 32  CG  
2   1 Y 1 B GLU 44  ? CD  ? A GLU 32  CD  
3   1 Y 1 B GLU 44  ? OE1 ? A GLU 32  OE1 
4   1 Y 1 B GLU 44  ? OE2 ? A GLU 32  OE2 
5   1 Y 1 B GLU 45  ? CG  ? A GLU 33  CG  
6   1 Y 1 B GLU 45  ? CD  ? A GLU 33  CD  
7   1 Y 1 B GLU 45  ? OE1 ? A GLU 33  OE1 
8   1 Y 1 B GLU 45  ? OE2 ? A GLU 33  OE2 
9   1 Y 1 B LYS 65  ? CG  ? A LYS 53  CG  
10  1 Y 1 B LYS 65  ? CD  ? A LYS 53  CD  
11  1 Y 1 B LYS 65  ? CE  ? A LYS 53  CE  
12  1 Y 1 B LYS 65  ? NZ  ? A LYS 53  NZ  
13  1 Y 1 B LYS 66  ? CG  ? A LYS 54  CG  
14  1 Y 1 B LYS 66  ? CD  ? A LYS 54  CD  
15  1 Y 1 B LYS 66  ? CE  ? A LYS 54  CE  
16  1 Y 1 B LYS 66  ? NZ  ? A LYS 54  NZ  
17  1 Y 1 B ARG 73  ? CG  ? A ARG 61  CG  
18  1 Y 1 B ARG 73  ? CD  ? A ARG 61  CD  
19  1 Y 1 B ARG 73  ? NE  ? A ARG 61  NE  
20  1 Y 1 B ARG 73  ? CZ  ? A ARG 61  CZ  
21  1 Y 1 B ARG 73  ? NH1 ? A ARG 61  NH1 
22  1 Y 1 B ARG 73  ? NH2 ? A ARG 61  NH2 
23  1 Y 1 B ASN 74  ? CG  ? A ASN 62  CG  
24  1 Y 1 B ASN 74  ? OD1 ? A ASN 62  OD1 
25  1 Y 1 B ASN 74  ? ND2 ? A ASN 62  ND2 
26  1 Y 1 B LYS 83  ? CG  ? A LYS 71  CG  
27  1 Y 1 B LYS 83  ? CD  ? A LYS 71  CD  
28  1 Y 1 B LYS 83  ? CE  ? A LYS 71  CE  
29  1 Y 1 B LYS 83  ? NZ  ? A LYS 71  NZ  
30  1 Y 1 B LYS 88  ? CG  ? A LYS 76  CG  
31  1 Y 1 B LYS 88  ? CD  ? A LYS 76  CD  
32  1 Y 1 B LYS 88  ? CE  ? A LYS 76  CE  
33  1 Y 1 B LYS 88  ? NZ  ? A LYS 76  NZ  
34  1 Y 1 B LYS 98  ? CG  ? A LYS 86  CG  
35  1 Y 1 B LYS 98  ? CD  ? A LYS 86  CD  
36  1 Y 1 B LYS 98  ? CE  ? A LYS 86  CE  
37  1 Y 1 B LYS 98  ? NZ  ? A LYS 86  NZ  
38  1 Y 1 B LYS 99  ? CG  ? A LYS 87  CG  
39  1 Y 1 B LYS 99  ? CD  ? A LYS 87  CD  
40  1 Y 1 B LYS 99  ? CE  ? A LYS 87  CE  
41  1 Y 1 B LYS 99  ? NZ  ? A LYS 87  NZ  
42  1 Y 1 B LYS 121 ? CG  ? A LYS 109 CG  
43  1 Y 1 B LYS 121 ? CD  ? A LYS 109 CD  
44  1 Y 1 B LYS 121 ? CE  ? A LYS 109 CE  
45  1 Y 1 B LYS 121 ? NZ  ? A LYS 109 NZ  
46  1 Y 1 B LYS 138 ? CG  ? A LYS 126 CG  
47  1 Y 1 B LYS 138 ? CD  ? A LYS 126 CD  
48  1 Y 1 B LYS 138 ? CE  ? A LYS 126 CE  
49  1 Y 1 B LYS 138 ? NZ  ? A LYS 126 NZ  
50  1 Y 1 B GLU 140 ? CG  ? A GLU 128 CG  
51  1 Y 1 B GLU 140 ? CD  ? A GLU 128 CD  
52  1 Y 1 B GLU 140 ? OE1 ? A GLU 128 OE1 
53  1 Y 1 B GLU 140 ? OE2 ? A GLU 128 OE2 
54  1 Y 1 A GLU 44  ? CG  ? B GLU 32  CG  
55  1 Y 1 A GLU 44  ? CD  ? B GLU 32  CD  
56  1 Y 1 A GLU 44  ? OE1 ? B GLU 32  OE1 
57  1 Y 1 A GLU 44  ? OE2 ? B GLU 32  OE2 
58  1 Y 1 A LYS 52  ? CG  ? B LYS 40  CG  
59  1 Y 1 A LYS 52  ? CD  ? B LYS 40  CD  
60  1 Y 1 A LYS 52  ? CE  ? B LYS 40  CE  
61  1 Y 1 A LYS 52  ? NZ  ? B LYS 40  NZ  
62  1 Y 1 A LYS 65  ? CG  ? B LYS 53  CG  
63  1 Y 1 A LYS 65  ? CD  ? B LYS 53  CD  
64  1 Y 1 A LYS 65  ? CE  ? B LYS 53  CE  
65  1 Y 1 A LYS 65  ? NZ  ? B LYS 53  NZ  
66  1 Y 1 A LYS 66  ? CG  ? B LYS 54  CG  
67  1 Y 1 A LYS 66  ? CD  ? B LYS 54  CD  
68  1 Y 1 A LYS 66  ? CE  ? B LYS 54  CE  
69  1 Y 1 A LYS 66  ? NZ  ? B LYS 54  NZ  
70  1 Y 1 A ARG 73  ? CG  ? B ARG 61  CG  
71  1 Y 1 A ARG 73  ? CD  ? B ARG 61  CD  
72  1 Y 1 A ARG 73  ? NE  ? B ARG 61  NE  
73  1 Y 1 A ARG 73  ? CZ  ? B ARG 61  CZ  
74  1 Y 1 A ARG 73  ? NH1 ? B ARG 61  NH1 
75  1 Y 1 A ARG 73  ? NH2 ? B ARG 61  NH2 
76  1 Y 1 A ASN 74  ? CG  ? B ASN 62  CG  
77  1 Y 1 A ASN 74  ? OD1 ? B ASN 62  OD1 
78  1 Y 1 A ASN 74  ? ND2 ? B ASN 62  ND2 
79  1 Y 1 A GLU 75  ? CG  ? B GLU 63  CG  
80  1 Y 1 A GLU 75  ? CD  ? B GLU 63  CD  
81  1 Y 1 A GLU 75  ? OE1 ? B GLU 63  OE1 
82  1 Y 1 A GLU 75  ? OE2 ? B GLU 63  OE2 
83  1 Y 1 A LYS 83  ? CG  ? B LYS 71  CG  
84  1 Y 1 A LYS 83  ? CD  ? B LYS 71  CD  
85  1 Y 1 A LYS 83  ? CE  ? B LYS 71  CE  
86  1 Y 1 A LYS 83  ? NZ  ? B LYS 71  NZ  
87  1 Y 1 A LYS 88  ? CG  ? B LYS 76  CG  
88  1 Y 1 A LYS 88  ? CD  ? B LYS 76  CD  
89  1 Y 1 A LYS 88  ? CE  ? B LYS 76  CE  
90  1 Y 1 A LYS 88  ? NZ  ? B LYS 76  NZ  
91  1 Y 1 A LYS 121 ? CG  ? B LYS 109 CG  
92  1 Y 1 A LYS 121 ? CD  ? B LYS 109 CD  
93  1 Y 1 A LYS 121 ? CE  ? B LYS 109 CE  
94  1 Y 1 A LYS 121 ? NZ  ? B LYS 109 NZ  
95  1 Y 1 A LYS 138 ? CG  ? B LYS 126 CG  
96  1 Y 1 A LYS 138 ? CD  ? B LYS 126 CD  
97  1 Y 1 A LYS 138 ? CE  ? B LYS 126 CE  
98  1 Y 1 A LYS 138 ? NZ  ? B LYS 126 NZ  
99  1 Y 1 A GLU 140 ? CG  ? B GLU 128 CG  
100 1 Y 1 A GLU 140 ? CD  ? B GLU 128 CD  
101 1 Y 1 A GLU 140 ? OE1 ? B GLU 128 OE1 
102 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                     9GQB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.191 
_cell.length_a_esd                 ? 
_cell.length_b                     48.191 
_cell.length_b_esd                 ? 
_cell.length_c                     191.561 
_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                         9GQB 
_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                   9GQB 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.35 
_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    '24% 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                                       9GQB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.00 
_reflns.d_resolution_low                               47.89 
_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                                     18383 
_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                                10.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.0 
_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                                0.053 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.048 
_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 47.89 ? 54.7 ? ? ? ? 271  ? ? ? ? ? ? ? ? ? ? ? 8.3  0.94 ? ? 0.031 0.013 ? 1 ? 1.000 ? ? 98.8  ? 0.028 ? ? ? ? ? ? ? ? ? 
2.00 2.05  ? 4.6  ? ? ? ? 1296 ? ? ? ? ? ? ? ? ? ? ? 11.2 1.03 ? ? 0.579 0.238 ? 2 ? 0.918 ? ? 100.0 ? 0.527 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.547 
_refine.aniso_B[1][2]                            -0.273 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -0.547 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            1.774 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               49.966 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.937 
_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                                 9GQB 
_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                             41.769 
_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                     18324 
_refine.ls_number_reflns_R_free                  867 
_refine.ls_number_reflns_R_work                  17457 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.935 
_refine.ls_percent_reflns_R_free                 4.731 
_refine.ls_R_factor_all                          0.221 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2709 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2187 
_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                       0.203 
_refine.pdbx_overall_ESU_R_Free                  0.186 
_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                             11.938 
_refine.overall_SU_ML                            0.161 
_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                        41.769 
_refine_hist.number_atoms_solvent             65 
_refine_hist.number_atoms_total               1988 
_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        1851 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.015  0.012  1968 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1801 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 2.430  1.820  2671 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 0.797  1.738  4193 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 8.337  5.000  250  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 27.037 14.375 16   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 13.325 10.000 294  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 16.963 10.000 70   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.121  0.200  299  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  2245 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  399  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.214  0.200  372  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.211  0.200  1677 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.190  0.200  1017 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.097  0.200  1036 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.176  0.200  76   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.212  0.200  3    ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.168  0.200  14   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.192  0.200  42   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.308  0.200  1    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 3.560  2.608  1006 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.540  2.608  1006 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 4.479  4.662  1254 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 4.478  4.664  1255 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 4.153  2.748  962  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 4.151  2.748  963  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 5.439  4.956  1417 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.437  4.955  1418 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 7.281  25.220 2163 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 7.279  25.198 2160 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.122  0.050  3361 ? 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 ? ? 0.12161 ? 0.05007 1 'Local ncs' ? B ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.12161 ? 0.05007 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  1288 . 75 1213 100.0000 . 0.265 . . 0.261 . . . . . 0.248 . 20 . 0.954 0.916 0.350 
'X-RAY DIFFRACTION' 2.052 2.108  1297 . 65 1232 100.0000 . 0.297 . . 0.293 . . . . . 0.277 . 20 . 0.940 0.921 0.363 
'X-RAY DIFFRACTION' 2.108 2.169  1259 . 58 1201 100.0000 . 0.289 . . 0.286 . . . . . 0.265 . 20 . 0.943 0.912 0.344 
'X-RAY DIFFRACTION' 2.169 2.235  1209 . 52 1157 100.0000 . 0.282 . . 0.279 . . . . . 0.259 . 20 . 0.945 0.922 0.338 
'X-RAY DIFFRACTION' 2.235 2.309  1208 . 60 1148 100.0000 . 0.248 . . 0.246 . . . . . 0.229 . 20 . 0.960 0.934 0.295 
'X-RAY DIFFRACTION' 2.309 2.389  1137 . 48 1089 100.0000 . 0.255 . . 0.255 . . . . . 0.231 . 20 . 0.960 0.962 0.240 
'X-RAY DIFFRACTION' 2.389 2.479  1103 . 48 1055 100.0000 . 0.234 . . 0.229 . . . . . 0.206 . 20 . 0.967 0.922 0.343 
'X-RAY DIFFRACTION' 2.479 2.580  1073 . 48 1025 100.0000 . 0.243 . . 0.239 . . . . . 0.222 . 20 . 0.964 0.938 0.328 
'X-RAY DIFFRACTION' 2.580 2.694  1053 . 50 1003 100.0000 . 0.228 . . 0.223 . . . . . 0.208 . 20 . 0.970 0.952 0.347 
'X-RAY DIFFRACTION' 2.694 2.825  987  . 53 934  100.0000 . 0.227 . . 0.221 . . . . . 0.211 . 20 . 0.971 0.942 0.340 
'X-RAY DIFFRACTION' 2.825 2.977  937  . 37 900  100.0000 . 0.224 . . 0.221 . . . . . 0.213 . 20 . 0.968 0.941 0.305 
'X-RAY DIFFRACTION' 2.977 3.157  896  . 33 860  99.6652  . 0.242 . . 0.239 . . . . . 0.235 . 20 . 0.961 0.929 0.313 
'X-RAY DIFFRACTION' 3.157 3.374  840  . 47 793  100.0000 . 0.227 . . 0.224 . . . . . 0.227 . 20 . 0.970 0.955 0.277 
'X-RAY DIFFRACTION' 3.374 3.642  810  . 29 781  100.0000 . 0.238 . . 0.237 . . . . . 0.245 . 20 . 0.971 0.966 0.254 
'X-RAY DIFFRACTION' 3.642 3.986  741  . 30 711  100.0000 . 0.221 . . 0.219 . . . . . 0.231 . 20 . 0.972 0.962 0.263 
'X-RAY DIFFRACTION' 3.986 4.452  671  . 31 637  99.5529  . 0.183 . . 0.180 . . . . . 0.200 . 20 . 0.982 0.961 0.251 
'X-RAY DIFFRACTION' 4.452 5.131  597  . 34 563  100.0000 . 0.139 . . 0.137 . . . . . 0.165 . 20 . 0.989 0.988 0.159 
'X-RAY DIFFRACTION' 5.131 6.260  524  . 36 488  100.0000 . 0.213 . . 0.208 . . . . . 0.239 . 20 . 0.976 0.963 0.278 
'X-RAY DIFFRACTION' 6.260 8.756  426  . 18 407  99.7653  . 0.231 . . 0.231 . . . . . 0.277 . 20 . 0.972 0.969 0.242 
'X-RAY DIFFRACTION' 8.756 41.769 279  . 15 260  98.5663  . 0.212 . . 0.211 . . . . . 0.271 . 20 . 0.973 0.960 0.239 
# 
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                     9GQB 
_struct.title                        'The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog p5(2,1)-Diol-II' 
_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        9GQB 
_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 9GQB B 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
2 1 9GQB 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 9GQB GLY B 1  ? UNP Q13451 ?   ?   'expression tag'      13  1  
1 9GQB ALA B 2  ? UNP Q13451 ?   ?   'expression tag'      14  2  
1 9GQB PRO B 3  ? UNP Q13451 ?   ?   'expression tag'      15  3  
1 9GQB THR B 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  4  
1 9GQB ALA B 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 5  
1 9GQB ILE B 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 6  
2 9GQB GLY A 1  ? UNP Q13451 ?   ?   'expression tag'      13  7  
2 9GQB ALA A 2  ? UNP Q13451 ?   ?   'expression tag'      14  8  
2 9GQB PRO A 3  ? UNP Q13451 ?   ?   'expression tag'      15  9  
2 9GQB THR A 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  10 
2 9GQB ALA A 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 11 
2 9GQB 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 ILE A 75 ? ALA A 83  ? ILE B 87  ALA B 95  1 ? 9  
HELX_P HELX_P3 AA3 PRO A 97 ? ALA A 100 ? PRO B 109 ALA B 112 5 ? 4  
HELX_P HELX_P4 AA4 ILE B 75 ? ALA B 83  ? ILE A 87  ALA A 95  1 ? 9  
HELX_P HELX_P5 AA5 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 -4.12 
2 LEU 107 B . ? LEU 119 A PRO 108 B ? PRO 120 A 1 0.94  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ASP A 12  ? GLU B 23  ASP B 24  
AA1 2 VAL A 21  ? ARG A 27  ? VAL B 33  ARG B 39  
AA1 3 ILE A 90  ? ILE A 95  ? ILE B 102 ILE B 107 
AA1 4 LEU A 116 ? LYS A 126 ? LEU B 128 LYS B 138 
AA1 5 LYS A 40  ? LEU A 49  ? LYS B 52  LEU B 61  
AA1 6 PHE A 55  ? SER A 57  ? PHE B 67  SER B 69  
AA2 1 GLU A 11  ? ASP A 12  ? GLU B 23  ASP B 24  
AA2 2 VAL A 21  ? ARG A 27  ? VAL B 33  ARG B 39  
AA2 3 ILE A 90  ? ILE A 95  ? ILE B 102 ILE B 107 
AA2 4 LEU A 116 ? LYS A 126 ? LEU B 128 LYS B 138 
AA2 5 LYS A 40  ? LEU A 49  ? LYS B 52  LEU B 61  
AA2 6 PHE A 65  ? SER A 68  ? PHE B 77  SER B 80  
AA3 1 GLU B 11  ? ASP B 12  ? GLU A 23  ASP A 24  
AA3 2 VAL B 21  ? ARG B 27  ? VAL A 33  ARG A 39  
AA3 3 ILE B 90  ? ILE B 95  ? ILE A 102 ILE A 107 
AA3 4 LEU B 116 ? LYS B 126 ? LEU A 128 LYS A 138 
AA3 5 LYS B 40  ? LEU B 49  ? LYS A 52  LEU A 61  
AA3 6 PHE B 55  ? SER B 57  ? PHE A 67  SER A 69  
AA4 1 GLU B 11  ? ASP B 12  ? GLU A 23  ASP A 24  
AA4 2 VAL B 21  ? ARG B 27  ? VAL A 33  ARG A 39  
AA4 3 ILE B 90  ? ILE B 95  ? ILE A 102 ILE A 107 
AA4 4 LEU B 116 ? LYS B 126 ? LEU A 128 LYS A 138 
AA4 5 LYS B 40  ? LEU B 49  ? LYS A 52  LEU A 61  
AA4 6 PHE B 65  ? SER B 68  ? PHE A 77  SER A 80  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 11  ? N GLU B 23  O LYS A 23  ? O LYS B 35  
AA1 2 3 N LYS A 26  ? N LYS B 38  O ILE A 90  ? O ILE B 102 
AA1 3 4 N ILE A 95  ? N ILE B 107 O LEU A 116 ? O LEU B 128 
AA1 4 5 O LYS A 126 ? O LYS B 138 N LYS A 40  ? N LYS B 52  
AA1 5 6 N GLY A 47  ? N GLY B 59  O ASP A 56  ? O ASP B 68  
AA2 1 2 N GLU A 11  ? N GLU B 23  O LYS A 23  ? O LYS B 35  
AA2 2 3 N LYS A 26  ? N LYS B 38  O ILE A 90  ? O ILE B 102 
AA2 3 4 N ILE A 95  ? N ILE B 107 O LEU A 116 ? O LEU B 128 
AA2 4 5 O LYS A 126 ? O LYS B 138 N LYS A 40  ? N LYS B 52  
AA2 5 6 N VAL A 43  ? N VAL B 55  O PHE A 65  ? O PHE B 77  
AA3 1 2 N GLU B 11  ? N GLU A 23  O LYS B 23  ? O LYS A 35  
AA3 2 3 N ILE B 24  ? N ILE A 36  O HIS B 92  ? O HIS A 104 
AA3 3 4 N ILE B 95  ? N ILE A 107 O LEU B 116 ? O LEU A 128 
AA3 4 5 O ASP B 124 ? O ASP A 136 N TYR B 42  ? N TYR A 54  
AA3 5 6 N GLY B 47  ? N GLY A 59  O ASP B 56  ? O ASP A 68  
AA4 1 2 N GLU B 11  ? N GLU A 23  O LYS B 23  ? O LYS A 35  
AA4 2 3 N ILE B 24  ? N ILE A 36  O HIS B 92  ? O HIS A 104 
AA4 3 4 N ILE B 95  ? N ILE A 107 O LEU B 116 ? O LEU A 128 
AA4 4 5 O ASP B 124 ? O ASP A 136 N TYR B 42  ? N TYR A 54  
AA4 5 6 N VAL B 43  ? N VAL A 55  O PHE B 65  ? O PHE A 77  
# 
_pdbx_entry_details.entry_id                   9GQB 
_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 H    B GLY 41  ? ? O   B HOH 302 ? ? 1.34 
2 1 H    A GLY 41  ? ? O   A HOH 301 ? ? 1.39 
3 1 HH12 A ARG 31  ? ? O   A HOH 302 ? ? 1.54 
4 1 HH   A TYR 57  ? ? OD2 A ASP 68  ? ? 1.58 
5 1 OG   B SER 115 ? ? O   B HOH 301 ? ? 2.11 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             133 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             133 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.178 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.074 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N  B LYS 99  ? ? CA B LYS 99  ? ? CB  B LYS 99  ? ? 122.54 110.60 11.94  1.80 N 
2 1 CG B GLU 131 ? ? CD B GLU 131 ? ? OE1 B GLU 131 ? ? 131.29 118.30 12.99  2.00 N 
3 1 CG A GLU 20  ? ? CD A GLU 20  ? ? OE2 A GLU 20  ? ? 105.67 118.30 -12.63 2.00 N 
4 1 NE A ARG 31  ? ? CZ A ARG 31  ? ? NH1 A ARG 31  ? ? 124.51 120.30 4.21   0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG B 73  ? ? -62.86  0.61    
2 1 ASN B 74  ? ? 38.32   58.62   
3 1 GLU B 75  ? ? 178.14  151.93  
4 1 ALA B 112 ? ? -132.35 -105.39 
5 1 GLU A 20  ? ? -80.70  45.16   
6 1 ARG A 73  ? ? -63.25  0.46    
7 1 ALA A 112 ? ? -128.55 -108.02 
8 1 SER A 118 ? ? -153.73 66.57   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    139 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLU 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    140 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.91 
# 
_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     324 
_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 18.4768 0.9950   3.3743  0.1926 ? -0.0910 ? 0.0047 ? 0.0645 ? -0.0060 ? 0.0418 ? 5.5319 ? -2.3538 
? -0.1822 ? 7.2911 ? -0.5674 ? 3.0720 ? -0.3217 ? -0.0916 ? 0.0578  ? -0.1907 ? 0.2842 ? -0.4676 ? -0.4132 ? 0.0996  ? 0.0375 ? 
2 'X-RAY DIFFRACTION' ? refined 8.9742  -15.5546 28.1165 0.4912 ? 0.0625  ? 0.0514 ? 0.0101 ? 0.0118  ? 0.0815 ? 3.0297 ? 0.5595  
? -0.8747 ? 4.4381 ? -1.3908 ? 3.3818 ? -0.1857 ? -0.0567 ? -0.4508 ? 0.4575  ? 0.1175 ? 0.0167  ? 0.3154  ? -0.0092 ? 0.0683 ? 
# 
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 
A1IN8 C4   C Y N 1   
A1IN8 C14  C N N 2   
A1IN8 C5   C Y N 3   
A1IN8 C6   C Y N 4   
A1IN8 C11  C N S 5   
A1IN8 C7   C N N 6   
A1IN8 C8   C Y N 7   
A1IN8 C9   C N N 8   
A1IN8 C10  C N S 9   
A1IN8 C12  C N N 10  
A1IN8 C13  C N N 11  
A1IN8 N1   N N N 12  
A1IN8 C3   C Y N 13  
A1IN8 C1   C N N 14  
A1IN8 O1   O N N 15  
A1IN8 C2   C Y N 16  
A1IN8 O2   O N N 17  
A1IN8 O3   O N N 18  
A1IN8 O4   O N N 19  
A1IN8 O5   O N N 20  
A1IN8 O6   O N N 21  
A1IN8 O7   O N N 22  
A1IN8 C15  C N S 23  
A1IN8 C16  C N N 24  
A1IN8 C17  C N N 25  
A1IN8 C18  C N N 26  
A1IN8 C19  C N N 27  
A1IN8 C20  C N N 28  
A1IN8 O8   O N N 29  
A1IN8 C21  C N S 30  
A1IN8 C22  C N N 31  
A1IN8 C23  C N N 32  
A1IN8 C24  C N N 33  
A1IN8 C25  C N N 34  
A1IN8 C26  C N N 35  
A1IN8 C27  C N N 36  
A1IN8 H5   H N N 37  
A1IN8 H13  H N N 38  
A1IN8 H7   H N N 39  
A1IN8 H8   H N N 40  
A1IN8 H6   H N N 41  
A1IN8 H10  H N N 42  
A1IN8 H9   H N N 43  
A1IN8 H11  H N N 44  
A1IN8 H15  H N N 45  
A1IN8 H16  H N N 46  
A1IN8 H17  H N N 47  
A1IN8 H18  H N N 48  
A1IN8 H4   H N N 49  
A1IN8 H2   H N N 50  
A1IN8 H3   H N N 51  
A1IN8 H1   H N N 52  
A1IN8 H12  H N N 53  
A1IN8 H14  H N N 54  
A1IN8 H19  H N N 55  
A1IN8 H20  H N N 56  
A1IN8 H21  H N N 57  
A1IN8 H23  H N N 58  
A1IN8 H22  H N N 59  
A1IN8 H25  H N N 60  
A1IN8 H24  H N N 61  
A1IN8 H27  H N N 62  
A1IN8 H26  H N N 63  
A1IN8 H28  H N N 64  
A1IN8 H29  H N N 65  
A1IN8 H30  H N N 66  
A1IN8 H31  H N N 67  
A1IN8 H33  H N N 68  
A1IN8 H32  H N N 69  
A1IN8 H35  H N N 70  
A1IN8 H34  H N N 71  
A1IN8 H37  H N N 72  
A1IN8 H36  H N N 73  
A1IN8 H38  H N N 74  
A1IN8 H39  H N N 75  
ALA   N    N N N 76  
ALA   CA   C N S 77  
ALA   C    C N N 78  
ALA   O    O N N 79  
ALA   CB   C N N 80  
ALA   OXT  O N N 81  
ALA   H    H N N 82  
ALA   H2   H N N 83  
ALA   HA   H N N 84  
ALA   HB1  H N N 85  
ALA   HB2  H N N 86  
ALA   HB3  H N N 87  
ALA   HXT  H N N 88  
ARG   N    N N N 89  
ARG   CA   C N S 90  
ARG   C    C N N 91  
ARG   O    O N N 92  
ARG   CB   C N N 93  
ARG   CG   C N N 94  
ARG   CD   C N N 95  
ARG   NE   N N N 96  
ARG   CZ   C N N 97  
ARG   NH1  N N N 98  
ARG   NH2  N N N 99  
ARG   OXT  O N N 100 
ARG   H    H N N 101 
ARG   H2   H N N 102 
ARG   HA   H N N 103 
ARG   HB2  H N N 104 
ARG   HB3  H N N 105 
ARG   HG2  H N N 106 
ARG   HG3  H N N 107 
ARG   HD2  H N N 108 
ARG   HD3  H N N 109 
ARG   HE   H N N 110 
ARG   HH11 H N N 111 
ARG   HH12 H N N 112 
ARG   HH21 H N N 113 
ARG   HH22 H N N 114 
ARG   HXT  H N N 115 
ASN   N    N N N 116 
ASN   CA   C N S 117 
ASN   C    C N N 118 
ASN   O    O N N 119 
ASN   CB   C N N 120 
ASN   CG   C N N 121 
ASN   OD1  O N N 122 
ASN   ND2  N N N 123 
ASN   OXT  O N N 124 
ASN   H    H N N 125 
ASN   H2   H N N 126 
ASN   HA   H N N 127 
ASN   HB2  H N N 128 
ASN   HB3  H N N 129 
ASN   HD21 H N N 130 
ASN   HD22 H N N 131 
ASN   HXT  H N N 132 
ASP   N    N N N 133 
ASP   CA   C N S 134 
ASP   C    C N N 135 
ASP   O    O N N 136 
ASP   CB   C N N 137 
ASP   CG   C N N 138 
ASP   OD1  O N N 139 
ASP   OD2  O N N 140 
ASP   OXT  O N N 141 
ASP   H    H N N 142 
ASP   H2   H N N 143 
ASP   HA   H N N 144 
ASP   HB2  H N N 145 
ASP   HB3  H N N 146 
ASP   HD2  H N N 147 
ASP   HXT  H N N 148 
CYS   N    N N N 149 
CYS   CA   C N R 150 
CYS   C    C N N 151 
CYS   O    O N N 152 
CYS   CB   C N N 153 
CYS   SG   S N N 154 
CYS   OXT  O N N 155 
CYS   H    H N N 156 
CYS   H2   H N N 157 
CYS   HA   H N N 158 
CYS   HB2  H N N 159 
CYS   HB3  H N N 160 
CYS   HG   H N N 161 
CYS   HXT  H N N 162 
GLN   N    N N N 163 
GLN   CA   C N S 164 
GLN   C    C N N 165 
GLN   O    O N N 166 
GLN   CB   C N N 167 
GLN   CG   C N N 168 
GLN   CD   C N N 169 
GLN   OE1  O N N 170 
GLN   NE2  N N N 171 
GLN   OXT  O N N 172 
GLN   H    H N N 173 
GLN   H2   H N N 174 
GLN   HA   H N N 175 
GLN   HB2  H N N 176 
GLN   HB3  H N N 177 
GLN   HG2  H N N 178 
GLN   HG3  H N N 179 
GLN   HE21 H N N 180 
GLN   HE22 H N N 181 
GLN   HXT  H N N 182 
GLU   N    N N N 183 
GLU   CA   C N S 184 
GLU   C    C N N 185 
GLU   O    O N N 186 
GLU   CB   C N N 187 
GLU   CG   C N N 188 
GLU   CD   C N N 189 
GLU   OE1  O N N 190 
GLU   OE2  O N N 191 
GLU   OXT  O N N 192 
GLU   H    H N N 193 
GLU   H2   H N N 194 
GLU   HA   H N N 195 
GLU   HB2  H N N 196 
GLU   HB3  H N N 197 
GLU   HG2  H N N 198 
GLU   HG3  H N N 199 
GLU   HE2  H N N 200 
GLU   HXT  H N N 201 
GLY   N    N N N 202 
GLY   CA   C N N 203 
GLY   C    C N N 204 
GLY   O    O N N 205 
GLY   OXT  O N N 206 
GLY   H    H N N 207 
GLY   H2   H N N 208 
GLY   HA2  H N N 209 
GLY   HA3  H N N 210 
GLY   HXT  H N N 211 
HIS   N    N N N 212 
HIS   CA   C N S 213 
HIS   C    C N N 214 
HIS   O    O N N 215 
HIS   CB   C N N 216 
HIS   CG   C Y N 217 
HIS   ND1  N Y N 218 
HIS   CD2  C Y N 219 
HIS   CE1  C Y N 220 
HIS   NE2  N Y N 221 
HIS   OXT  O N N 222 
HIS   H    H N N 223 
HIS   H2   H N N 224 
HIS   HA   H N N 225 
HIS   HB2  H N N 226 
HIS   HB3  H N N 227 
HIS   HD1  H N N 228 
HIS   HD2  H N N 229 
HIS   HE1  H N N 230 
HIS   HE2  H N N 231 
HIS   HXT  H N N 232 
HOH   O    O N N 233 
HOH   H1   H N N 234 
HOH   H2   H N N 235 
ILE   N    N N N 236 
ILE   CA   C N S 237 
ILE   C    C N N 238 
ILE   O    O N N 239 
ILE   CB   C N S 240 
ILE   CG1  C N N 241 
ILE   CG2  C N N 242 
ILE   CD1  C N N 243 
ILE   OXT  O N N 244 
ILE   H    H N N 245 
ILE   H2   H N N 246 
ILE   HA   H N N 247 
ILE   HB   H N N 248 
ILE   HG12 H N N 249 
ILE   HG13 H N N 250 
ILE   HG21 H N N 251 
ILE   HG22 H N N 252 
ILE   HG23 H N N 253 
ILE   HD11 H N N 254 
ILE   HD12 H N N 255 
ILE   HD13 H N N 256 
ILE   HXT  H N N 257 
LEU   N    N N N 258 
LEU   CA   C N S 259 
LEU   C    C N N 260 
LEU   O    O N N 261 
LEU   CB   C N N 262 
LEU   CG   C N N 263 
LEU   CD1  C N N 264 
LEU   CD2  C N N 265 
LEU   OXT  O N N 266 
LEU   H    H N N 267 
LEU   H2   H N N 268 
LEU   HA   H N N 269 
LEU   HB2  H N N 270 
LEU   HB3  H N N 271 
LEU   HG   H N N 272 
LEU   HD11 H N N 273 
LEU   HD12 H N N 274 
LEU   HD13 H N N 275 
LEU   HD21 H N N 276 
LEU   HD22 H N N 277 
LEU   HD23 H N N 278 
LEU   HXT  H N N 279 
LYS   N    N N N 280 
LYS   CA   C N S 281 
LYS   C    C N N 282 
LYS   O    O N N 283 
LYS   CB   C N N 284 
LYS   CG   C N N 285 
LYS   CD   C N N 286 
LYS   CE   C N N 287 
LYS   NZ   N N N 288 
LYS   OXT  O N N 289 
LYS   H    H N N 290 
LYS   H2   H N N 291 
LYS   HA   H N N 292 
LYS   HB2  H N N 293 
LYS   HB3  H N N 294 
LYS   HG2  H N N 295 
LYS   HG3  H N N 296 
LYS   HD2  H N N 297 
LYS   HD3  H N N 298 
LYS   HE2  H N N 299 
LYS   HE3  H N N 300 
LYS   HZ1  H N N 301 
LYS   HZ2  H N N 302 
LYS   HZ3  H N N 303 
LYS   HXT  H N N 304 
MET   N    N N N 305 
MET   CA   C N S 306 
MET   C    C N N 307 
MET   O    O N N 308 
MET   CB   C N N 309 
MET   CG   C N N 310 
MET   SD   S N N 311 
MET   CE   C N N 312 
MET   OXT  O N N 313 
MET   H    H N N 314 
MET   H2   H N N 315 
MET   HA   H N N 316 
MET   HB2  H N N 317 
MET   HB3  H N N 318 
MET   HG2  H N N 319 
MET   HG3  H N N 320 
MET   HE1  H N N 321 
MET   HE2  H N N 322 
MET   HE3  H N N 323 
MET   HXT  H N N 324 
PHE   N    N N N 325 
PHE   CA   C N S 326 
PHE   C    C N N 327 
PHE   O    O N N 328 
PHE   CB   C N N 329 
PHE   CG   C Y N 330 
PHE   CD1  C Y N 331 
PHE   CD2  C Y N 332 
PHE   CE1  C Y N 333 
PHE   CE2  C Y N 334 
PHE   CZ   C Y N 335 
PHE   OXT  O N N 336 
PHE   H    H N N 337 
PHE   H2   H N N 338 
PHE   HA   H N N 339 
PHE   HB2  H N N 340 
PHE   HB3  H N N 341 
PHE   HD1  H N N 342 
PHE   HD2  H N N 343 
PHE   HE1  H N N 344 
PHE   HE2  H N N 345 
PHE   HZ   H N N 346 
PHE   HXT  H N N 347 
PRO   N    N N N 348 
PRO   CA   C N S 349 
PRO   C    C N N 350 
PRO   O    O N N 351 
PRO   CB   C N N 352 
PRO   CG   C N N 353 
PRO   CD   C N N 354 
PRO   OXT  O N N 355 
PRO   H    H N N 356 
PRO   HA   H N N 357 
PRO   HB2  H N N 358 
PRO   HB3  H N N 359 
PRO   HG2  H N N 360 
PRO   HG3  H N N 361 
PRO   HD2  H N N 362 
PRO   HD3  H N N 363 
PRO   HXT  H N N 364 
SER   N    N N N 365 
SER   CA   C N S 366 
SER   C    C N N 367 
SER   O    O N N 368 
SER   CB   C N N 369 
SER   OG   O N N 370 
SER   OXT  O N N 371 
SER   H    H N N 372 
SER   H2   H N N 373 
SER   HA   H N N 374 
SER   HB2  H N N 375 
SER   HB3  H N N 376 
SER   HG   H N N 377 
SER   HXT  H N N 378 
THR   N    N N N 379 
THR   CA   C N S 380 
THR   C    C N N 381 
THR   O    O N N 382 
THR   CB   C N R 383 
THR   OG1  O N N 384 
THR   CG2  C N N 385 
THR   OXT  O N N 386 
THR   H    H N N 387 
THR   H2   H N N 388 
THR   HA   H N N 389 
THR   HB   H N N 390 
THR   HG1  H N N 391 
THR   HG21 H N N 392 
THR   HG22 H N N 393 
THR   HG23 H N N 394 
THR   HXT  H N N 395 
TRP   N    N N N 396 
TRP   CA   C N S 397 
TRP   C    C N N 398 
TRP   O    O N N 399 
TRP   CB   C N N 400 
TRP   CG   C Y N 401 
TRP   CD1  C Y N 402 
TRP   CD2  C Y N 403 
TRP   NE1  N Y N 404 
TRP   CE2  C Y N 405 
TRP   CE3  C Y N 406 
TRP   CZ2  C Y N 407 
TRP   CZ3  C Y N 408 
TRP   CH2  C Y N 409 
TRP   OXT  O N N 410 
TRP   H    H N N 411 
TRP   H2   H N N 412 
TRP   HA   H N N 413 
TRP   HB2  H N N 414 
TRP   HB3  H N N 415 
TRP   HD1  H N N 416 
TRP   HE1  H N N 417 
TRP   HE3  H N N 418 
TRP   HZ2  H N N 419 
TRP   HZ3  H N N 420 
TRP   HH2  H N N 421 
TRP   HXT  H N N 422 
TYR   N    N N N 423 
TYR   CA   C N S 424 
TYR   C    C N N 425 
TYR   O    O N N 426 
TYR   CB   C N N 427 
TYR   CG   C Y N 428 
TYR   CD1  C Y N 429 
TYR   CD2  C Y N 430 
TYR   CE1  C Y N 431 
TYR   CE2  C Y N 432 
TYR   CZ   C Y N 433 
TYR   OH   O N N 434 
TYR   OXT  O N N 435 
TYR   H    H N N 436 
TYR   H2   H N N 437 
TYR   HA   H N N 438 
TYR   HB2  H N N 439 
TYR   HB3  H N N 440 
TYR   HD1  H N N 441 
TYR   HD2  H N N 442 
TYR   HE1  H N N 443 
TYR   HE2  H N N 444 
TYR   HH   H N N 445 
TYR   HXT  H N N 446 
VAL   N    N N N 447 
VAL   CA   C N S 448 
VAL   C    C N N 449 
VAL   O    O N N 450 
VAL   CB   C N N 451 
VAL   CG1  C N N 452 
VAL   CG2  C N N 453 
VAL   OXT  O N N 454 
VAL   H    H N N 455 
VAL   H2   H N N 456 
VAL   HA   H N N 457 
VAL   HB   H N N 458 
VAL   HG11 H N N 459 
VAL   HG12 H N N 460 
VAL   HG13 H N N 461 
VAL   HG21 H N N 462 
VAL   HG22 H N N 463 
VAL   HG23 H N N 464 
VAL   HXT  H N N 465 
# 
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 
A1IN8 O4  C10  sing N N 1   
A1IN8 C10 C9   sing N N 2   
A1IN8 C10 C11  sing N N 3   
A1IN8 C9  O3   sing N N 4   
A1IN8 O3  C8   sing N N 5   
A1IN8 O5  C11  sing N N 6   
A1IN8 C11 C12  sing N N 7   
A1IN8 O2  C7   sing N N 8   
A1IN8 O2  C6   sing N N 9   
A1IN8 C8  C6   doub Y N 10  
A1IN8 C8  C2   sing Y N 11  
A1IN8 O1  C2   sing N N 12  
A1IN8 O1  C1   sing N N 13  
A1IN8 C6  C5   sing Y N 14  
A1IN8 C2  C3   doub Y N 15  
A1IN8 C12 C13  sing N N 16  
A1IN8 C5  C4   doub Y N 17  
A1IN8 C13 O6   sing N N 18  
A1IN8 C3  C4   sing Y N 19  
A1IN8 C4  C21  sing N N 20  
A1IN8 O6  C14  sing N N 21  
A1IN8 C27 C26  sing N N 22  
A1IN8 C27 C22  sing N N 23  
A1IN8 C26 C25  sing N N 24  
A1IN8 C21 C22  sing N N 25  
A1IN8 C21 C20  sing N N 26  
A1IN8 C14 O7   doub N N 27  
A1IN8 C14 C15  sing N N 28  
A1IN8 C22 C23  sing N N 29  
A1IN8 C20 O8   doub N N 30  
A1IN8 C20 N1   sing N N 31  
A1IN8 C19 N1   sing N N 32  
A1IN8 C19 C18  sing N N 33  
A1IN8 N1  C15  sing N N 34  
A1IN8 C25 C24  sing N N 35  
A1IN8 C15 C16  sing N N 36  
A1IN8 C18 C17  sing N N 37  
A1IN8 C17 C16  sing N N 38  
A1IN8 C23 C24  sing N N 39  
A1IN8 C5  H5   sing N N 40  
A1IN8 C11 H13  sing N N 41  
A1IN8 C7  H7   sing N N 42  
A1IN8 C7  H8   sing N N 43  
A1IN8 C7  H6   sing N N 44  
A1IN8 C9  H10  sing N N 45  
A1IN8 C9  H9   sing N N 46  
A1IN8 C10 H11  sing N N 47  
A1IN8 C12 H15  sing N N 48  
A1IN8 C12 H16  sing N N 49  
A1IN8 C13 H17  sing N N 50  
A1IN8 C13 H18  sing N N 51  
A1IN8 C3  H4   sing N N 52  
A1IN8 C1  H2   sing N N 53  
A1IN8 C1  H3   sing N N 54  
A1IN8 C1  H1   sing N N 55  
A1IN8 O4  H12  sing N N 56  
A1IN8 O5  H14  sing N N 57  
A1IN8 C15 H19  sing N N 58  
A1IN8 C16 H20  sing N N 59  
A1IN8 C16 H21  sing N N 60  
A1IN8 C17 H23  sing N N 61  
A1IN8 C17 H22  sing N N 62  
A1IN8 C18 H25  sing N N 63  
A1IN8 C18 H24  sing N N 64  
A1IN8 C19 H27  sing N N 65  
A1IN8 C19 H26  sing N N 66  
A1IN8 C21 H28  sing N N 67  
A1IN8 C22 H29  sing N N 68  
A1IN8 C23 H30  sing N N 69  
A1IN8 C23 H31  sing N N 70  
A1IN8 C24 H33  sing N N 71  
A1IN8 C24 H32  sing N N 72  
A1IN8 C25 H35  sing N N 73  
A1IN8 C25 H34  sing N N 74  
A1IN8 C26 H37  sing N N 75  
A1IN8 C26 H36  sing N N 76  
A1IN8 C27 H38  sing N N 77  
A1IN8 C27 H39  sing N N 78  
ALA   N   CA   sing N N 79  
ALA   N   H    sing N N 80  
ALA   N   H2   sing N N 81  
ALA   CA  C    sing N N 82  
ALA   CA  CB   sing N N 83  
ALA   CA  HA   sing N N 84  
ALA   C   O    doub N N 85  
ALA   C   OXT  sing N N 86  
ALA   CB  HB1  sing N N 87  
ALA   CB  HB2  sing N N 88  
ALA   CB  HB3  sing N N 89  
ALA   OXT HXT  sing N N 90  
ARG   N   CA   sing N N 91  
ARG   N   H    sing N N 92  
ARG   N   H2   sing N N 93  
ARG   CA  C    sing N N 94  
ARG   CA  CB   sing N N 95  
ARG   CA  HA   sing N N 96  
ARG   C   O    doub N N 97  
ARG   C   OXT  sing N N 98  
ARG   CB  CG   sing N N 99  
ARG   CB  HB2  sing N N 100 
ARG   CB  HB3  sing N N 101 
ARG   CG  CD   sing N N 102 
ARG   CG  HG2  sing N N 103 
ARG   CG  HG3  sing N N 104 
ARG   CD  NE   sing N N 105 
ARG   CD  HD2  sing N N 106 
ARG   CD  HD3  sing N N 107 
ARG   NE  CZ   sing N N 108 
ARG   NE  HE   sing N N 109 
ARG   CZ  NH1  sing N N 110 
ARG   CZ  NH2  doub N N 111 
ARG   NH1 HH11 sing N N 112 
ARG   NH1 HH12 sing N N 113 
ARG   NH2 HH21 sing N N 114 
ARG   NH2 HH22 sing N N 115 
ARG   OXT HXT  sing N N 116 
ASN   N   CA   sing N N 117 
ASN   N   H    sing N N 118 
ASN   N   H2   sing N N 119 
ASN   CA  C    sing N N 120 
ASN   CA  CB   sing N N 121 
ASN   CA  HA   sing N N 122 
ASN   C   O    doub N N 123 
ASN   C   OXT  sing N N 124 
ASN   CB  CG   sing N N 125 
ASN   CB  HB2  sing N N 126 
ASN   CB  HB3  sing N N 127 
ASN   CG  OD1  doub N N 128 
ASN   CG  ND2  sing N N 129 
ASN   ND2 HD21 sing N N 130 
ASN   ND2 HD22 sing N N 131 
ASN   OXT HXT  sing N N 132 
ASP   N   CA   sing N N 133 
ASP   N   H    sing N N 134 
ASP   N   H2   sing N N 135 
ASP   CA  C    sing N N 136 
ASP   CA  CB   sing N N 137 
ASP   CA  HA   sing N N 138 
ASP   C   O    doub N N 139 
ASP   C   OXT  sing N N 140 
ASP   CB  CG   sing N N 141 
ASP   CB  HB2  sing N N 142 
ASP   CB  HB3  sing N N 143 
ASP   CG  OD1  doub N N 144 
ASP   CG  OD2  sing N N 145 
ASP   OD2 HD2  sing N N 146 
ASP   OXT HXT  sing N N 147 
CYS   N   CA   sing N N 148 
CYS   N   H    sing N N 149 
CYS   N   H2   sing N N 150 
CYS   CA  C    sing N N 151 
CYS   CA  CB   sing N N 152 
CYS   CA  HA   sing N N 153 
CYS   C   O    doub N N 154 
CYS   C   OXT  sing N N 155 
CYS   CB  SG   sing N N 156 
CYS   CB  HB2  sing N N 157 
CYS   CB  HB3  sing N N 158 
CYS   SG  HG   sing N N 159 
CYS   OXT HXT  sing N N 160 
GLN   N   CA   sing N N 161 
GLN   N   H    sing N N 162 
GLN   N   H2   sing N N 163 
GLN   CA  C    sing N N 164 
GLN   CA  CB   sing N N 165 
GLN   CA  HA   sing N N 166 
GLN   C   O    doub N N 167 
GLN   C   OXT  sing N N 168 
GLN   CB  CG   sing N N 169 
GLN   CB  HB2  sing N N 170 
GLN   CB  HB3  sing N N 171 
GLN   CG  CD   sing N N 172 
GLN   CG  HG2  sing N N 173 
GLN   CG  HG3  sing N N 174 
GLN   CD  OE1  doub N N 175 
GLN   CD  NE2  sing N N 176 
GLN   NE2 HE21 sing N N 177 
GLN   NE2 HE22 sing N N 178 
GLN   OXT HXT  sing N N 179 
GLU   N   CA   sing N N 180 
GLU   N   H    sing N N 181 
GLU   N   H2   sing N N 182 
GLU   CA  C    sing N N 183 
GLU   CA  CB   sing N N 184 
GLU   CA  HA   sing N N 185 
GLU   C   O    doub N N 186 
GLU   C   OXT  sing N N 187 
GLU   CB  CG   sing N N 188 
GLU   CB  HB2  sing N N 189 
GLU   CB  HB3  sing N N 190 
GLU   CG  CD   sing N N 191 
GLU   CG  HG2  sing N N 192 
GLU   CG  HG3  sing N N 193 
GLU   CD  OE1  doub N N 194 
GLU   CD  OE2  sing N N 195 
GLU   OE2 HE2  sing N N 196 
GLU   OXT HXT  sing N N 197 
GLY   N   CA   sing N N 198 
GLY   N   H    sing N N 199 
GLY   N   H2   sing N N 200 
GLY   CA  C    sing N N 201 
GLY   CA  HA2  sing N N 202 
GLY   CA  HA3  sing N N 203 
GLY   C   O    doub N N 204 
GLY   C   OXT  sing N N 205 
GLY   OXT HXT  sing N N 206 
HIS   N   CA   sing N N 207 
HIS   N   H    sing N N 208 
HIS   N   H2   sing N N 209 
HIS   CA  C    sing N N 210 
HIS   CA  CB   sing N N 211 
HIS   CA  HA   sing N N 212 
HIS   C   O    doub N N 213 
HIS   C   OXT  sing N N 214 
HIS   CB  CG   sing N N 215 
HIS   CB  HB2  sing N N 216 
HIS   CB  HB3  sing N N 217 
HIS   CG  ND1  sing Y N 218 
HIS   CG  CD2  doub Y N 219 
HIS   ND1 CE1  doub Y N 220 
HIS   ND1 HD1  sing N N 221 
HIS   CD2 NE2  sing Y N 222 
HIS   CD2 HD2  sing N N 223 
HIS   CE1 NE2  sing Y N 224 
HIS   CE1 HE1  sing N N 225 
HIS   NE2 HE2  sing N N 226 
HIS   OXT HXT  sing N N 227 
HOH   O   H1   sing N N 228 
HOH   O   H2   sing N N 229 
ILE   N   CA   sing N N 230 
ILE   N   H    sing N N 231 
ILE   N   H2   sing N N 232 
ILE   CA  C    sing N N 233 
ILE   CA  CB   sing N N 234 
ILE   CA  HA   sing N N 235 
ILE   C   O    doub N N 236 
ILE   C   OXT  sing N N 237 
ILE   CB  CG1  sing N N 238 
ILE   CB  CG2  sing N N 239 
ILE   CB  HB   sing N N 240 
ILE   CG1 CD1  sing N N 241 
ILE   CG1 HG12 sing N N 242 
ILE   CG1 HG13 sing N N 243 
ILE   CG2 HG21 sing N N 244 
ILE   CG2 HG22 sing N N 245 
ILE   CG2 HG23 sing N N 246 
ILE   CD1 HD11 sing N N 247 
ILE   CD1 HD12 sing N N 248 
ILE   CD1 HD13 sing N N 249 
ILE   OXT HXT  sing N N 250 
LEU   N   CA   sing N N 251 
LEU   N   H    sing N N 252 
LEU   N   H2   sing N N 253 
LEU   CA  C    sing N N 254 
LEU   CA  CB   sing N N 255 
LEU   CA  HA   sing N N 256 
LEU   C   O    doub N N 257 
LEU   C   OXT  sing N N 258 
LEU   CB  CG   sing N N 259 
LEU   CB  HB2  sing N N 260 
LEU   CB  HB3  sing N N 261 
LEU   CG  CD1  sing N N 262 
LEU   CG  CD2  sing N N 263 
LEU   CG  HG   sing N N 264 
LEU   CD1 HD11 sing N N 265 
LEU   CD1 HD12 sing N N 266 
LEU   CD1 HD13 sing N N 267 
LEU   CD2 HD21 sing N N 268 
LEU   CD2 HD22 sing N N 269 
LEU   CD2 HD23 sing N N 270 
LEU   OXT HXT  sing N N 271 
LYS   N   CA   sing N N 272 
LYS   N   H    sing N N 273 
LYS   N   H2   sing N N 274 
LYS   CA  C    sing N N 275 
LYS   CA  CB   sing N N 276 
LYS   CA  HA   sing N N 277 
LYS   C   O    doub N N 278 
LYS   C   OXT  sing N N 279 
LYS   CB  CG   sing N N 280 
LYS   CB  HB2  sing N N 281 
LYS   CB  HB3  sing N N 282 
LYS   CG  CD   sing N N 283 
LYS   CG  HG2  sing N N 284 
LYS   CG  HG3  sing N N 285 
LYS   CD  CE   sing N N 286 
LYS   CD  HD2  sing N N 287 
LYS   CD  HD3  sing N N 288 
LYS   CE  NZ   sing N N 289 
LYS   CE  HE2  sing N N 290 
LYS   CE  HE3  sing N N 291 
LYS   NZ  HZ1  sing N N 292 
LYS   NZ  HZ2  sing N N 293 
LYS   NZ  HZ3  sing N N 294 
LYS   OXT HXT  sing N N 295 
MET   N   CA   sing N N 296 
MET   N   H    sing N N 297 
MET   N   H2   sing N N 298 
MET   CA  C    sing N N 299 
MET   CA  CB   sing N N 300 
MET   CA  HA   sing N N 301 
MET   C   O    doub N N 302 
MET   C   OXT  sing N N 303 
MET   CB  CG   sing N N 304 
MET   CB  HB2  sing N N 305 
MET   CB  HB3  sing N N 306 
MET   CG  SD   sing N N 307 
MET   CG  HG2  sing N N 308 
MET   CG  HG3  sing N N 309 
MET   SD  CE   sing N N 310 
MET   CE  HE1  sing N N 311 
MET   CE  HE2  sing N N 312 
MET   CE  HE3  sing N N 313 
MET   OXT HXT  sing N N 314 
PHE   N   CA   sing N N 315 
PHE   N   H    sing N N 316 
PHE   N   H2   sing N N 317 
PHE   CA  C    sing N N 318 
PHE   CA  CB   sing N N 319 
PHE   CA  HA   sing N N 320 
PHE   C   O    doub N N 321 
PHE   C   OXT  sing N N 322 
PHE   CB  CG   sing N N 323 
PHE   CB  HB2  sing N N 324 
PHE   CB  HB3  sing N N 325 
PHE   CG  CD1  doub Y N 326 
PHE   CG  CD2  sing Y N 327 
PHE   CD1 CE1  sing Y N 328 
PHE   CD1 HD1  sing N N 329 
PHE   CD2 CE2  doub Y N 330 
PHE   CD2 HD2  sing N N 331 
PHE   CE1 CZ   doub Y N 332 
PHE   CE1 HE1  sing N N 333 
PHE   CE2 CZ   sing Y N 334 
PHE   CE2 HE2  sing N N 335 
PHE   CZ  HZ   sing N N 336 
PHE   OXT HXT  sing N N 337 
PRO   N   CA   sing N N 338 
PRO   N   CD   sing N N 339 
PRO   N   H    sing N N 340 
PRO   CA  C    sing N N 341 
PRO   CA  CB   sing N N 342 
PRO   CA  HA   sing N N 343 
PRO   C   O    doub N N 344 
PRO   C   OXT  sing N N 345 
PRO   CB  CG   sing N N 346 
PRO   CB  HB2  sing N N 347 
PRO   CB  HB3  sing N N 348 
PRO   CG  CD   sing N N 349 
PRO   CG  HG2  sing N N 350 
PRO   CG  HG3  sing N N 351 
PRO   CD  HD2  sing N N 352 
PRO   CD  HD3  sing N N 353 
PRO   OXT HXT  sing N N 354 
SER   N   CA   sing N N 355 
SER   N   H    sing N N 356 
SER   N   H2   sing N N 357 
SER   CA  C    sing N N 358 
SER   CA  CB   sing N N 359 
SER   CA  HA   sing N N 360 
SER   C   O    doub N N 361 
SER   C   OXT  sing N N 362 
SER   CB  OG   sing N N 363 
SER   CB  HB2  sing N N 364 
SER   CB  HB3  sing N N 365 
SER   OG  HG   sing N N 366 
SER   OXT HXT  sing N N 367 
THR   N   CA   sing N N 368 
THR   N   H    sing N N 369 
THR   N   H2   sing N N 370 
THR   CA  C    sing N N 371 
THR   CA  CB   sing N N 372 
THR   CA  HA   sing N N 373 
THR   C   O    doub N N 374 
THR   C   OXT  sing N N 375 
THR   CB  OG1  sing N N 376 
THR   CB  CG2  sing N N 377 
THR   CB  HB   sing N N 378 
THR   OG1 HG1  sing N N 379 
THR   CG2 HG21 sing N N 380 
THR   CG2 HG22 sing N N 381 
THR   CG2 HG23 sing N N 382 
THR   OXT HXT  sing N N 383 
TRP   N   CA   sing N N 384 
TRP   N   H    sing N N 385 
TRP   N   H2   sing N N 386 
TRP   CA  C    sing N N 387 
TRP   CA  CB   sing N N 388 
TRP   CA  HA   sing N N 389 
TRP   C   O    doub N N 390 
TRP   C   OXT  sing N N 391 
TRP   CB  CG   sing N N 392 
TRP   CB  HB2  sing N N 393 
TRP   CB  HB3  sing N N 394 
TRP   CG  CD1  doub Y N 395 
TRP   CG  CD2  sing Y N 396 
TRP   CD1 NE1  sing Y N 397 
TRP   CD1 HD1  sing N N 398 
TRP   CD2 CE2  doub Y N 399 
TRP   CD2 CE3  sing Y N 400 
TRP   NE1 CE2  sing Y N 401 
TRP   NE1 HE1  sing N N 402 
TRP   CE2 CZ2  sing Y N 403 
TRP   CE3 CZ3  doub Y N 404 
TRP   CE3 HE3  sing N N 405 
TRP   CZ2 CH2  doub Y N 406 
TRP   CZ2 HZ2  sing N N 407 
TRP   CZ3 CH2  sing Y N 408 
TRP   CZ3 HZ3  sing N N 409 
TRP   CH2 HH2  sing N N 410 
TRP   OXT HXT  sing N N 411 
TYR   N   CA   sing N N 412 
TYR   N   H    sing N N 413 
TYR   N   H2   sing N N 414 
TYR   CA  C    sing N N 415 
TYR   CA  CB   sing N N 416 
TYR   CA  HA   sing N N 417 
TYR   C   O    doub N N 418 
TYR   C   OXT  sing N N 419 
TYR   CB  CG   sing N N 420 
TYR   CB  HB2  sing N N 421 
TYR   CB  HB3  sing N N 422 
TYR   CG  CD1  doub Y N 423 
TYR   CG  CD2  sing Y N 424 
TYR   CD1 CE1  sing Y N 425 
TYR   CD1 HD1  sing N N 426 
TYR   CD2 CE2  doub Y N 427 
TYR   CD2 HD2  sing N N 428 
TYR   CE1 CZ   doub Y N 429 
TYR   CE1 HE1  sing N N 430 
TYR   CE2 CZ   sing Y N 431 
TYR   CE2 HE2  sing N N 432 
TYR   CZ  OH   sing N N 433 
TYR   OH  HH   sing N N 434 
TYR   OXT HXT  sing N N 435 
VAL   N   CA   sing N N 436 
VAL   N   H    sing N N 437 
VAL   N   H2   sing N N 438 
VAL   CA  C    sing N N 439 
VAL   CA  CB   sing N N 440 
VAL   CA  HA   sing N N 441 
VAL   C   O    doub N N 442 
VAL   C   OXT  sing N N 443 
VAL   CB  CG1  sing N N 444 
VAL   CB  CG2  sing N N 445 
VAL   CB  HB   sing N N 446 
VAL   CG1 HG11 sing N N 447 
VAL   CG1 HG12 sing N N 448 
VAL   CG1 HG13 sing N N 449 
VAL   CG2 HG21 sing N N 450 
VAL   CG2 HG22 sing N N 451 
VAL   CG2 HG23 sing N N 452 
VAL   OXT HXT  sing N N 453 
# 
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                    9GQB 
_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]   0.020751 
_atom_sites.fract_transf_matrix[1][2]   0.011980 
_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]   0.023961 
_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]   0.005220 
_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   ? 15.822 15.755  -6.941  1   67.195  ? 13  GLY   B N    1 ? 1 
ATOM   2    C CA   . GLY   A 1 1   ? 16.838 15.234  -6.03   1   63.561  ? 13  GLY   B CA   1 ? 1 
ATOM   3    C C    . GLY   A 1 1   ? 16.846 13.706  -6.095  1   60.656  ? 13  GLY   B C    1 ? 1 
ATOM   4    O O    . GLY   A 1 1   ? 16.174 13.099  -6.927  1   68.196  ? 13  GLY   B O    1 ? 1 
ATOM   5    H H1   . GLY   A 1 1   ? 15.833 16.659  -6.931  1   68.878  ? 13  GLY   B H1   1 c 1 
ATOM   6    H H2   . GLY   A 1 1   ? 15.001 15.47   -6.685  1   65.169  ? 13  GLY   B H2   1 c 1 
ATOM   7    H H3   . GLY   A 1 1   ? 15.982 15.469  -7.784  1   68.06   ? 13  GLY   B H3   1 c 1 
ATOM   8    H HA2  . GLY   A 1 1   ? 17.719 15.581  -6.29   1   65.957  ? 13  GLY   B HA2  1 c 1 
ATOM   9    H HA3  . GLY   A 1 1   ? 16.643 15.532  -5.111  1   62.798  ? 13  GLY   B HA3  1 c 1 
ATOM   10   N N    . ALA   A 1 2   ? 17.686 13.132  -5.254  1   54.946  ? 14  ALA   B N    1 ? 1 
ATOM   11   C CA   . ALA   A 1 2   ? 17.935 11.713  -5.217  1   61.254  ? 14  ALA   B CA   1 ? 1 
ATOM   12   C C    . ALA   A 1 2   ? 16.659 10.951  -4.87   1   61.523  ? 14  ALA   B C    1 ? 1 
ATOM   13   O O    . ALA   A 1 2   ? 16.409 9.943   -5.522  1   59.074  ? 14  ALA   B O    1 ? 1 
ATOM   14   C CB   . ALA   A 1 2   ? 19.045 11.405  -4.249  1   59.126  ? 14  ALA   B CB   1 ? 1 
ATOM   15   H H    . ALA   A 1 2   ? 18.139 13.664  -4.665  1   58.214  ? 14  ALA   B H    1 c 1 
ATOM   16   H HA   . ALA   A 1 2   ? 18.22  11.43   -6.13   1   61.075  ? 14  ALA   B HA   1 c 1 
ATOM   17   H HB1  . ALA   A 1 2   ? 19.854 11.87   -4.521  1   61.565  ? 14  ALA   B HB1  1 c 1 
ATOM   18   H HB2  . ALA   A 1 2   ? 18.794 11.694  -3.357  1   58.38   ? 14  ALA   B HB2  1 c 1 
ATOM   19   H HB3  . ALA   A 1 2   ? 19.213 10.448  -4.239  1   57.874  ? 14  ALA   B HB3  1 c 1 
ATOM   20   N N    . PRO   A 1 3   ? 15.844 11.378  -3.865  1   53.79   ? 15  PRO   B N    1 ? 1 
ATOM   21   C CA   . PRO   A 1 3   ? 14.623 10.676  -3.485  1   53.046  ? 15  PRO   B CA   1 ? 1 
ATOM   22   C C    . PRO   A 1 3   ? 13.583 10.734  -4.599  1   60.126  ? 15  PRO   B C    1 ? 1 
ATOM   23   O O    . PRO   A 1 3   ? 12.959 9.753   -4.897  1   51.11   ? 15  PRO   B O    1 ? 1 
ATOM   24   C CB   . PRO   A 1 3   ? 14.096 11.426  -2.256  1   50.749  ? 15  PRO   B CB   1 ? 1 
ATOM   25   C CG   . PRO   A 1 3   ? 15.369 12.009  -1.737  1   51.636  ? 15  PRO   B CG   1 ? 1 
ATOM   26   C CD   . PRO   A 1 3   ? 16.071 12.528  -3      1   58.013  ? 15  PRO   B CD   1 ? 1 
ATOM   27   H HA   . PRO   A 1 3   ? 14.827 9.744   -3.261  1   51.689  ? 15  PRO   B HA   1 c 1 
ATOM   28   H HB2  . PRO   A 1 3   ? 13.46  12.124  -2.507  1   52.594  ? 15  PRO   B HB2  1 c 1 
ATOM   29   H HB3  . PRO   A 1 3   ? 13.692 10.815  -1.61   1   49.422  ? 15  PRO   B HB3  1 c 1 
ATOM   30   H HG2  . PRO   A 1 3   ? 15.194 12.739  -1.111  1   53.026  ? 15  PRO   B HG2  1 c 1 
ATOM   31   H HG3  . PRO   A 1 3   ? 15.912 11.329  -1.292  1   50.922  ? 15  PRO   B HG3  1 c 1 
ATOM   32   H HD2  . PRO   A 1 3   ? 15.646 13.332  -3.354  1   58.287  ? 15  PRO   B HD2  1 c 1 
ATOM   33   H HD3  . PRO   A 1 3   ? 17.019 12.688  -2.848  1   57.065  ? 15  PRO   B HD3  1 c 1 
ATOM   34   N N    . ALA   A 1 4   ? 13.462 11.859  -5.299  1   55.504  ? 16  ALA   B N    1 ? 1 
ATOM   35   C CA   . ALA   A 1 4   ? 12.508 11.957  -6.384  1   57.653  ? 16  ALA   B CA   1 ? 1 
ATOM   36   C C    . ALA   A 1 4   ? 12.921 11.064  -7.557  1   61.322  ? 16  ALA   B C    1 ? 1 
ATOM   37   O O    . ALA   A 1 4   ? 12.101 10.432  -8.232  1   64.215  ? 16  ALA   B O    1 ? 1 
ATOM   38   C CB   . ALA   A 1 4   ? 12.377 13.405  -6.819  1   64.883  ? 16  ALA   B CB   1 ? 1 
ATOM   39   H H    . ALA   A 1 4   ? 13.979 12.584  -5.094  1   58.115  ? 16  ALA   B H    1 c 1 
ATOM   40   H HA   . ALA   A 1 4   ? 11.624 11.639  -6.05   1   57.801  ? 16  ALA   B HA   1 c 1 
ATOM   41   H HB1  . ALA   A 1 4   ? 12.058 13.943  -6.075  1   63.315  ? 16  ALA   B HB1  1 c 1 
ATOM   42   H HB2  . ALA   A 1 4   ? 13.242 13.74   -7.11   1   64.983  ? 16  ALA   B HB2  1 c 1 
ATOM   43   H HB3  . ALA   A 1 4   ? 11.745 13.47   -7.555  1   65.504  ? 16  ALA   B HB3  1 c 1 
ATOM   44   N N    . THR   A 1 5   ? 14.217 10.997  -7.831  1   58.677  ? 17  THR   B N    1 ? 1 
ATOM   45   C CA   . THR   A 1 5   ? 14.682 10.073  -8.852  1   56.821  ? 17  THR   B CA   1 ? 1 
ATOM   46   C C    . THR   A 1 5   ? 14.257 8.654   -8.463  1   53.423  ? 17  THR   B C    1 ? 1 
ATOM   47   O O    . THR   A 1 5   ? 13.764 7.94    -9.317  1   48.778  ? 17  THR   B O    1 ? 1 
ATOM   48   C CB   . THR   A 1 5   ? 16.196 10.207  -9.039  1   58.432  ? 17  THR   B CB   1 ? 1 
ATOM   49   O OG1  . THR   A 1 5   ? 16.377 11.528  -9.551  1   64.975  ? 17  THR   B OG1  1 ? 1 
ATOM   50   C CG2  . THR   A 1 5   ? 16.794 9.138   -9.939  1   57.544  ? 17  THR   B CG2  1 ? 1 
ATOM   51   H H    . THR   A 1 5   ? 14.818 11.527  -7.392  1   58.661  ? 17  THR   B H    1 c 1 
ATOM   52   H HA   . THR   A 1 5   ? 14.245 10.308  -9.7    1   59.895  ? 17  THR   B HA   1 c 1 
ATOM   53   H HB   . THR   A 1 5   ? 16.633 10.145  -8.156  1   56.492  ? 17  THR   B HB   1 c 1 
ATOM   54   H HG1  . THR   A 1 5   ? 15.937 11.518  -10.344 0   30      ? 17  THR   B HG1  1 c 1 
ATOM   55   H HG21 . THR   A 1 5   ? 17.722 9.356   -10.128 1   59.516  ? 17  THR   B HG21 1 c 1 
ATOM   56   H HG22 . THR   A 1 5   ? 16.295 9.099   -10.773 1   60.224  ? 17  THR   B HG22 1 c 1 
ATOM   57   H HG23 . THR   A 1 5   ? 16.75  8.276   -9.496  1   55.802  ? 17  THR   B HG23 1 c 1 
ATOM   58   N N    . VAL   A 1 6   ? 14.312 8.293   -7.165  1   48.257  ? 18  VAL   B N    1 ? 1 
ATOM   59   C CA   . VAL   A 1 6   ? 14.011 6.927   -6.733  1   48.594  ? 18  VAL   B CA   1 ? 1 
ATOM   60   C C    . VAL   A 1 6   ? 12.523 6.633   -6.882  1   48.636  ? 18  VAL   B C    1 ? 1 
ATOM   61   O O    . VAL   A 1 6   ? 12.159 5.556   -7.318  1   47.604  ? 18  VAL   B O    1 ? 1 
ATOM   62   C CB   . VAL   A 1 6   ? 14.476 6.604   -5.314  1   41.932  ? 18  VAL   B CB   1 ? 1 
ATOM   63   C CG1  . VAL   A 1 6   ? 14.298 5.113   -5.004  1   42.836  ? 18  VAL   B CG1  1 ? 1 
ATOM   64   C CG2  . VAL   A 1 6   ? 15.946 6.974   -5.201  1   52.498  ? 18  VAL   B CG2  1 ? 1 
ATOM   65   H H    . VAL   A 1 6   ? 14.542 8.914   -6.536  1   48.907  ? 18  VAL   B H    1 c 1 
ATOM   66   H HA   . VAL   A 1 6   ? 14.487 6.325   -7.335  1   48.07   ? 18  VAL   B HA   1 c 1 
ATOM   67   H HB   . VAL   A 1 6   ? 13.945 7.145   -4.684  1   44.161  ? 18  VAL   B HB   1 c 1 
ATOM   68   H HG11 . VAL   A 1 6   ? 14.689 4.584   -5.72   1   42.933  ? 18  VAL   B HG11 1 c 1 
ATOM   69   H HG12 . VAL   A 1 6   ? 13.352 4.906   -4.929  1   41.806  ? 18  VAL   B HG12 1 c 1 
ATOM   70   H HG13 . VAL   A 1 6   ? 14.742 4.9     -4.166  1   40.424  ? 18  VAL   B HG13 1 c 1 
ATOM   71   H HG21 . VAL   A 1 6   ? 16.323 6.568   -4.402  1   47.288  ? 18  VAL   B HG21 1 c 1 
ATOM   72   H HG22 . VAL   A 1 6   ? 16.036 7.936   -5.144  1   50.059  ? 18  VAL   B HG22 1 c 1 
ATOM   73   H HG23 . VAL   A 1 6   ? 16.425 6.65    -5.983  1   50.306  ? 18  VAL   B HG23 1 c 1 
ATOM   74   N N    . THR   A 1 7   ? 11.689 7.635   -6.603  1   53.578  ? 19  THR   B N    1 ? 1 
ATOM   75   C CA   . THR   A 1 7   ? 10.247 7.51    -6.767  1   56.757  ? 19  THR   B CA   1 ? 1 
ATOM   76   C C    . THR   A 1 7   ? 9.92   7.115   -8.198  1   61.816  ? 19  THR   B C    1 ? 1 
ATOM   77   O O    . THR   A 1 7   ? 9.118  6.213   -8.37   1   69.28   ? 19  THR   B O    1 ? 1 
ATOM   78   C CB   . THR   A 1 7   ? 9.536  8.808   -6.412  1   61.301  ? 19  THR   B CB   1 ? 1 
ATOM   79   O OG1  . THR   A 1 7   ? 9.716  8.88    -5.008  1   52.318  ? 19  THR   B OG1  1 ? 1 
ATOM   80   C CG2  . THR   A 1 7   ? 8.046  8.817   -6.722  1   63.854  ? 19  THR   B CG2  1 ? 1 
ATOM   81   H H    . THR   A 1 7   ? 12.026 8.423   -6.287  1   52.996  ? 19  THR   B H    1 c 1 
ATOM   82   H HA   . THR   A 1 7   ? 9.928  6.803   -6.164  1   55.632  ? 19  THR   B HA   1 c 1 
ATOM   83   H HB   . THR   A 1 7   ? 9.98   9.575   -6.846  1   60.95   ? 19  THR   B HB   1 c 1 
ATOM   84   H HG1  . THR   A 1 7   ? 9.29   8.155   -4.612  0   30      ? 19  THR   B HG1  1 c 1 
ATOM   85   H HG21 . THR   A 1 7   ? 7.626  9.571   -6.274  1   63.936  ? 19  THR   B HG21 1 c 1 
ATOM   86   H HG22 . THR   A 1 7   ? 7.644  7.99    -6.406  1   62.595  ? 19  THR   B HG22 1 c 1 
ATOM   87   H HG23 . THR   A 1 7   ? 7.912  8.897   -7.681  1   65.988  ? 19  THR   B HG23 1 c 1 
ATOM   88   N N    . GLU   A 1 8   ? 10.577 7.767   -9.162  1   61.578  ? 20  GLU   B N    1 ? 1 
ATOM   89   C CA   . GLU   A 1 8   ? 10.163 7.758   -10.546 1   75.438  ? 20  GLU   B CA   1 ? 1 
ATOM   90   C C    . GLU   A 1 8   ? 10.823 6.613   -11.287 1   72.456  ? 20  GLU   B C    1 ? 1 
ATOM   91   O O    . GLU   A 1 8   ? 10.159 6.051   -12.127 1   69.554  ? 20  GLU   B O    1 ? 1 
ATOM   92   C CB   . GLU   A 1 8   ? 10.432 9.068   -11.296 1   80.542  ? 20  GLU   B CB   1 ? 1 
ATOM   93   C CG   . GLU   A 1 8   ? 9.805  10.286  -10.62  1   79.63   ? 20  GLU   B CG   1 ? 1 
ATOM   94   C CD   . GLU   A 1 8   ? 10.063 11.582  -11.381 1   89.591  ? 20  GLU   B CD   1 ? 1 
ATOM   95   O OE1  . GLU   A 1 8   ? 10.315 11.534  -12.628 1   88.334  ? 20  GLU   B OE1  1 ? 1 
ATOM   96   O OE2  . GLU   A 1 8   ? 10.008 12.645  -10.724 1   80.293  ? 20  GLU   B OE2  1 ? 1 
ATOM   97   H H    . GLU   A 1 8   ? 11.321 8.248   -8.939  1   63.726  ? 20  GLU   B H    1 c 1 
ATOM   98   H HA   . GLU   A 1 8   ? 9.183  7.608   -10.566 1   73.493  ? 20  GLU   B HA   1 c 1 
ATOM   99   H HB2  . GLU   A 1 8   ? 11.401 9.201   -11.362 1   79.892  ? 20  GLU   B HB2  1 c 1 
ATOM   100  H HB3  . GLU   A 1 8   ? 10.079 8.987   -12.206 1   82.986  ? 20  GLU   B HB3  1 c 1 
ATOM   101  H HG2  . GLU   A 1 8   ? 8.835  10.151  -10.549 1   81.384  ? 20  GLU   B HG2  1 c 1 
ATOM   102  H HG3  . GLU   A 1 8   ? 10.163 10.375  -9.713  1   78.325  ? 20  GLU   B HG3  1 c 1 
ATOM   103  N N    . GLN   A 1 9   ? 12.076 6.252   -10.98  1   68.719  ? 21  GLN   B N    1 ? 1 
ATOM   104  C CA   . GLN   A 1 9   ? 12.764 5.249   -11.787 1   74.829  ? 21  GLN   B CA   1 ? 1 
ATOM   105  C C    . GLN   A 1 9   ? 13.219 4.051   -10.95  1   62.015  ? 21  GLN   B C    1 ? 1 
ATOM   106  O O    . GLN   A 1 9   ? 13.794 3.122   -11.514 1   76.96   ? 21  GLN   B O    1 ? 1 
ATOM   107  C CB   . GLN   A 1 9   ? 14.05  5.695   -12.498 1   83.022  ? 21  GLN   B CB   1 ? 1 
ATOM   108  C CG   . GLN   A 1 9   ? 14.351 7.183   -12.377 1   90.394  ? 21  GLN   B CG   1 ? 1 
ATOM   109  C CD   . GLN   A 1 9   ? 14.332 7.915   -13.678 1   91.473  ? 21  GLN   B CD   1 ? 1 
ATOM   110  O OE1  . GLN   A 1 9   ? 14.669 7.336   -14.712 1   97.828  ? 21  GLN   B OE1  1 ? 1 
ATOM   111  N NE2  . GLN   A 1 9   ? 14.032 9.206   -13.61  1   98.45   ? 21  GLN   B NE2  1 ? 1 
ATOM   112  H H    . GLN   A 1 9   ? 12.505 6.629   -10.266 1   68.196  ? 21  GLN   B H    1 c 1 
ATOM   113  H HA   . GLN   A 1 9   ? 12.137 4.921   -12.479 1   75.2    ? 21  GLN   B HA   1 c 1 
ATOM   114  H HB2  . GLN   A 1 9   ? 14.807 5.197   -12.125 1   81.254  ? 21  GLN   B HB2  1 c 1 
ATOM   115  H HB3  . GLN   A 1 9   ? 13.979 5.457   -13.445 1   86.085  ? 21  GLN   B HB3  1 c 1 
ATOM   116  H HG2  . GLN   A 1 9   ? 13.7   7.602   -11.781 1   85.823  ? 21  GLN   B HG2  1 c 1 
ATOM   117  H HG3  . GLN   A 1 9   ? 15.238 7.297   -11.972 1   86.671  ? 21  GLN   B HG3  1 c 1 
ATOM   118  H HE21 . GLN   A 1 9   ? 13.554 9.581   -14.256 1   99.402  ? 21  GLN   B HE21 1 c 1 
ATOM   119  H HE22 . GLN   A 1 9   ? 14.307 9.69    -12.92  1   94.878  ? 21  GLN   B HE22 1 c 1 
ATOM   120  N N    . GLY   A 1 10  ? 13.006 4.036   -9.63   1   56.066  ? 22  GLY   B N    1 ? 1 
ATOM   121  C CA   . GLY   A 1 10  ? 13.576 2.973   -8.816  1   49.001  ? 22  GLY   B CA   1 ? 1 
ATOM   122  C C    . GLY   A 1 10  ? 12.722 1.701   -8.884  1   49.352  ? 22  GLY   B C    1 ? 1 
ATOM   123  O O    . GLY   A 1 10  ? 11.521 1.772   -9.136  1   46.364  ? 22  GLY   B O    1 ? 1 
ATOM   124  H H    . GLY   A 1 10  ? 12.496 4.681   -9.231  1   55.122  ? 22  GLY   B H    1 c 1 
ATOM   125  H HA2  . GLY   A 1 10  ? 14.489 2.777   -9.13   1   50.721  ? 22  GLY   B HA2  1 c 1 
ATOM   126  H HA3  . GLY   A 1 10  ? 13.636 3.28    -7.881  1   47.822  ? 22  GLY   B HA3  1 c 1 
ATOM   127  N N    . GLU   A 1 11  ? 13.396 0.555   -8.741  1   54.402  ? 23  GLU   B N    1 ? 1 
ATOM   128  C CA   . GLU   A 1 11  ? 12.79  -0.773  -8.728  1   48.948  ? 23  GLU   B CA   1 ? 1 
ATOM   129  C C    . GLU   A 1 11  ? 12.078 -1.053  -7.4    1   45.971  ? 23  GLU   B C    1 ? 1 
ATOM   130  O O    . GLU   A 1 11  ? 12.651 -0.793  -6.299  1   42.773  ? 23  GLU   B O    1 ? 1 
ATOM   131  C CB   . GLU   A 1 11  ? 13.949 -1.744  -8.961  1   55.321  ? 23  GLU   B CB   1 ? 1 
ATOM   132  C CG   . GLU   A 1 11  ? 13.483 -3.192  -9.076  1   72.167  ? 23  GLU   B CG   1 ? 1 
ATOM   133  C CD   . GLU   A 1 11  ? 14.532 -4.282  -9.296  1   82.995  ? 23  GLU   B CD   1 ? 1 
ATOM   134  O OE1  . GLU   A 1 11  ? 15.694 -3.972  -9.708  1   79.463  ? 23  GLU   B OE1  1 ? 1 
ATOM   135  O OE2  . GLU   A 1 11  ? 14.148 -5.471  -9.044  1   83.576  ? 23  GLU   B OE2  1 ? 1 
ATOM   136  H H    . GLU   A 1 11  ? 14.303 0.608   -8.64   1   51.058  ? 23  GLU   B H    1 c 1 
ATOM   137  H HA   . GLU   A 1 11  ? 12.141 -0.835  -9.474  1   53.305  ? 23  GLU   B HA   1 c 1 
ATOM   138  H HB2  . GLU   A 1 11  ? 14.417 -1.489  -9.784  1   58.787  ? 23  GLU   B HB2  1 c 1 
ATOM   139  H HB3  . GLU   A 1 11  ? 14.584 -1.666  -8.218  1   54.583  ? 23  GLU   B HB3  1 c 1 
ATOM   140  H HG2  . GLU   A 1 11  ? 12.991 -3.42   -8.258  1   67.955  ? 23  GLU   B HG2  1 c 1 
ATOM   141  H HG3  . GLU   A 1 11  ? 12.836 -3.248  -9.811  1   72.262  ? 23  GLU   B HG3  1 c 1 
ATOM   142  N N    . ASP   A 1 12  ? 10.835 -1.614  -7.509  1   45.905  ? 24  ASP   B N    1 ? 1 
ATOM   143  C CA   . ASP   A 1 12  ? 10.038 -2.062  -6.36   1   42.364  ? 24  ASP   B CA   1 ? 1 
ATOM   144  C C    . ASP   A 1 12  ? 10.613 -3.405  -5.981  1   43.513  ? 24  ASP   B C    1 ? 1 
ATOM   145  O O    . ASP   A 1 12  ? 10.451 -4.33   -6.778  1   46.103  ? 24  ASP   B O    1 ? 1 
ATOM   146  C CB   . ASP   A 1 12  ? 8.546  -2.198  -6.685  1   43.352  ? 24  ASP   B CB   1 ? 1 
ATOM   147  C CG   . ASP   A 1 12  ? 7.685  -2.599  -5.5    1   41.409  ? 24  ASP   B CG   1 ? 1 
ATOM   148  O OD1  . ASP   A 1 12  ? 8.254  -2.998  -4.474  1   40.44   ? 24  ASP   B OD1  1 ? 1 
ATOM   149  O OD2  . ASP   A 1 12  ? 6.427  -2.479  -5.573  1   44.101  ? 24  ASP   B OD2  1 ? 1 
ATOM   150  H H    . ASP   A 1 12  ? 10.477 -1.716  -8.344  1   48.231  ? 24  ASP   B H    1 c 1 
ATOM   151  H HA   . ASP   A 1 12  ? 10.164 -1.434  -5.618  1   40.898  ? 24  ASP   B HA   1 c 1 
ATOM   152  H HB2  . ASP   A 1 12  ? 8.219  -1.337  -7.021  1   44.301  ? 24  ASP   B HB2  1 c 1 
ATOM   153  H HB3  . ASP   A 1 12  ? 8.426  -2.863  -7.394  1   45.632  ? 24  ASP   B HB3  1 c 1 
ATOM   154  N N    . ILE   A 1 13  ? 11.346 -3.489  -4.88   1   37.782  ? 25  ILE   B N    1 ? 1 
ATOM   155  C CA   . ILE   A 1 13  ? 11.947 -4.747  -4.46   1   41.737  ? 25  ILE   B CA   1 ? 1 
ATOM   156  C C    . ILE   A 1 13  ? 11.168 -5.43   -3.34   1   37.929  ? 25  ILE   B C    1 ? 1 
ATOM   157  O O    . ILE   A 1 13  ? 11.653 -6.381  -2.751  1   39.712  ? 25  ILE   B O    1 ? 1 
ATOM   158  C CB   . ILE   A 1 13  ? 13.44  -4.631  -4.114  1   37.084  ? 25  ILE   B CB   1 ? 1 
ATOM   159  C CG1  . ILE   A 1 13  ? 13.635 -3.66   -2.99   1   38.563  ? 25  ILE   B CG1  1 ? 1 
ATOM   160  C CG2  . ILE   A 1 13  ? 14.269 -4.22   -5.335  1   42.171  ? 25  ILE   B CG2  1 ? 1 
ATOM   161  C CD1  . ILE   A 1 13  ? 15.031 -3.556  -2.421  1   36.947  ? 25  ILE   B CD1  1 ? 1 
ATOM   162  H H    . ILE   A 1 13  ? 11.468 -2.745  -4.364  1   38.063  ? 25  ILE   B H    1 c 1 
ATOM   163  H HA   . ILE   A 1 13  ? 11.897 -5.346  -5.229  1   41.575  ? 25  ILE   B HA   1 c 1 
ATOM   164  H HB   . ILE   A 1 13  ? 13.754 -5.507  -3.815  1   38.844  ? 25  ILE   B HB   1 c 1 
ATOM   165  H HG12 . ILE   A 1 13  ? 13.37  -2.771  -3.304  1   37.742  ? 25  ILE   B HG12 1 c 1 
ATOM   166  H HG13 . ILE   A 1 13  ? 13.027 -3.904  -2.263  1   36.956  ? 25  ILE   B HG13 1 c 1 
ATOM   167  H HG21 . ILE   A 1 13  ? 15.215 -4.255  -5.116  1   40.401  ? 25  ILE   B HG21 1 c 1 
ATOM   168  H HG22 . ILE   A 1 13  ? 14.033 -3.314  -5.599  1   41.286  ? 25  ILE   B HG22 1 c 1 
ATOM   169  H HG23 . ILE   A 1 13  ? 14.087 -4.827  -6.072  1   43.011  ? 25  ILE   B HG23 1 c 1 
ATOM   170  H HD11 . ILE   A 1 13  ? 15.358 -4.447  -2.192  1   37.036  ? 25  ILE   B HD11 1 c 1 
ATOM   171  H HD12 . ILE   A 1 13  ? 15.014 -3.002  -1.617  1   35.841  ? 25  ILE   B HD12 1 c 1 
ATOM   172  H HD13 . ILE   A 1 13  ? 15.627 -3.152  -3.079  1   37.692  ? 25  ILE   B HD13 1 c 1 
ATOM   173  N N    . THR   A 1 14  ? 9.93   -5.034  -3.072  1   43.746  ? 26  THR   B N    1 ? 1 
ATOM   174  C CA   . THR   A 1 14  ? 9.126  -5.759  -2.077  1   39.298  ? 26  THR   B CA   1 ? 1 
ATOM   175  C C    . THR   A 1 14  ? 8.525  -6.998  -2.738  1   46.556  ? 26  THR   B C    1 ? 1 
ATOM   176  O O    . THR   A 1 14  ? 8.255  -6.981  -3.956  1   45.081  ? 26  THR   B O    1 ? 1 
ATOM   177  C CB   . THR   A 1 14  ? 8.022  -4.874  -1.52   1   37.09   ? 26  THR   B CB   1 ? 1 
ATOM   178  O OG1  . THR   A 1 14  ? 7.177  -4.453  -2.615  1   36.955  ? 26  THR   B OG1  1 ? 1 
ATOM   179  C CG2  . THR   A 1 14  ? 8.527  -3.581  -0.894  1   36.446  ? 26  THR   B CG2  1 ? 1 
ATOM   180  H H    . THR   A 1 14  ? 9.567  -4.314  -3.502  1   41.787  ? 26  THR   B H    1 c 1 
ATOM   181  H HA   . THR   A 1 14  ? 9.71   -6.038  -1.339  1   39.023  ? 26  THR   B HA   1 c 1 
ATOM   182  H HB   . THR   A 1 14  ? 7.484  -5.373  -0.861  1   37.844  ? 26  THR   B HB   1 c 1 
ATOM   183  H HG1  . THR   A 1 14  ? 7.647  -4.013  -3.232  0   30      ? 26  THR   B HG1  1 c 1 
ATOM   184  H HG21 . THR   A 1 14  ? 7.775  -3.066  -0.56   1   36.347  ? 26  THR   B HG21 1 c 1 
ATOM   185  H HG22 . THR   A 1 14  ? 9.004  -3.062  -1.562  1   35.83   ? 26  THR   B HG22 1 c 1 
ATOM   186  H HG23 . THR   A 1 14  ? 9.127  -3.79   -0.158  1   34.609  ? 26  THR   B HG23 1 c 1 
ATOM   187  N N    . SER   A 1 15  ? 8.199  -7.996  -1.916  1   43.37   ? 27  SER   B N    1 ? 1 
ATOM   188  C CA   . SER   A 1 15  ? 7.544  -9.188  -2.441  1   48.026  ? 27  SER   B CA   1 ? 1 
ATOM   189  C C    . SER   A 1 15  ? 6.126  -8.876  -2.903  1   47.319  ? 27  SER   B C    1 ? 1 
ATOM   190  O O    . SER   A 1 15  ? 5.684  -9.325  -3.933  1   51.589  ? 27  SER   B O    1 ? 1 
ATOM   191  C CB   . SER   A 1 15  ? 7.503  -10.268 -1.427  1   48.304  ? 27  SER   B CB   1 ? 1 
ATOM   192  O OG   . SER   A 1 15  ? 8.807  -10.543 -0.955  1   46.594  ? 27  SER   B OG   1 ? 1 
ATOM   193  H H    . SER   A 1 15  ? 8.382  -7.938  -1.023  1   43.065  ? 27  SER   B H    1 c 1 
ATOM   194  H HA   . SER   A 1 15  ? 8.063  -9.51   -3.222  1   47.871  ? 27  SER   B HA   1 c 1 
ATOM   195  H HB2  . SER   A 1 15  ? 6.937  -9.991  -0.681  1   48.156  ? 27  SER   B HB2  1 c 1 
ATOM   196  H HB3  . SER   A 1 15  ? 7.12   -11.072 -1.822  1   50.932  ? 27  SER   B HB3  1 c 1 
ATOM   197  H HG   . SER   A 1 15  ? 8.815  -11.14  -0.387  0   30      ? 27  SER   B HG   1 c 1 
ATOM   198  N N    . LYS   A 1 16  ? 5.426  -8.084  -2.115  1   51.924  ? 28  LYS   B N    1 ? 1 
ATOM   199  C CA   . LYS   A 1 16  ? 4.031  -7.796  -2.345  1   53.997  ? 28  LYS   B CA   1 ? 1 
ATOM   200  C C    . LYS   A 1 16  ? 3.861  -6.757  -3.45   1   51.571  ? 28  LYS   B C    1 ? 1 
ATOM   201  O O    . LYS   A 1 16  ? 2.733  -6.526  -3.885  1   49.959  ? 28  LYS   B O    1 ? 1 
ATOM   202  C CB   . LYS   A 1 16  ? 3.468  -7.229  -1.043  1   56.025  ? 28  LYS   B CB   1 ? 1 
ATOM   203  C CG   . LYS   A 1 16  ? 3.442  -8.151  0.154   1   57.648  ? 28  LYS   B CG   1 ? 1 
ATOM   204  C CD   . LYS   A 1 16  ? 2.87   -7.438  1.377   1   64.894  ? 28  LYS   B CD   1 ? 1 
ATOM   205  C CE   . LYS   A 1 16  ? 3.612  -7.726  2.655   1   75.332  ? 28  LYS   B CE   1 ? 1 
ATOM   206  N NZ   . LYS   A 1 16  ? 3.429  -9.111  3.093   1   80.252  ? 28  LYS   B NZ   1 ? 1 
ATOM   207  H H    . LYS   A 1 16  ? 5.835  -7.704  -1.392  1   48.17   ? 28  LYS   B H    1 c 1 
ATOM   208  H HA   . LYS   A 1 16  ? 3.561  -8.632  -2.594  1   56.672  ? 28  LYS   B HA   1 c 1 
ATOM   209  H HB2  . LYS   A 1 16  ? 3.994  -6.436  -0.804  1   53.199  ? 28  LYS   B HB2  1 c 1 
ATOM   210  H HB3  . LYS   A 1 16  ? 2.55   -6.928  -1.213  1   57.488  ? 28  LYS   B HB3  1 c 1 
ATOM   211  H HG2  . LYS   A 1 16  ? 2.888  -8.934  -0.057  1   61.612  ? 28  LYS   B HG2  1 c 1 
ATOM   212  H HG3  . LYS   A 1 16  ? 4.355  -8.457  0.346   1   57.28   ? 28  LYS   B HG3  1 c 1 
ATOM   213  H HD2  . LYS   A 1 16  ? 2.882  -6.47   1.216   1   64.1    ? 28  LYS   B HD2  1 c 1 
ATOM   214  H HD3  . LYS   A 1 16  ? 1.933  -7.708  1.487   1   68.007  ? 28  LYS   B HD3  1 c 1 
ATOM   215  H HE2  . LYS   A 1 16  ? 4.563  -7.56   2.524   1   70.369  ? 28  LYS   B HE2  1 c 1 
ATOM   216  H HE3  . LYS   A 1 16  ? 3.296  -7.128  3.356   1   72.482  ? 28  LYS   B HE3  1 c 1 
ATOM   217  H HZ1  . LYS   A 1 16  ? 3.758  -9.681  2.47    1   79.611  ? 28  LYS   B HZ1  1 c 1 
ATOM   218  H HZ2  . LYS   A 1 16  ? 2.546  -9.279  3.212   1   81.756  ? 28  LYS   B HZ2  1 c 1 
ATOM   219  H HZ3  . LYS   A 1 16  ? 3.865  -9.245  3.876   1   78.414  ? 28  LYS   B HZ3  1 c 1 
ATOM   220  N N    . LYS   A 1 17  ? 4.983  -6.184  -3.911  1   51.302  ? 29  LYS   B N    1 ? 1 
ATOM   221  C CA   . LYS   A 1 17  ? 4.975  -5.167  -4.955  1   54.931  ? 29  LYS   B CA   1 ? 1 
ATOM   222  C C    . LYS   A 1 17  ? 4.042  -4.04   -4.534  1   49.707  ? 29  LYS   B C    1 ? 1 
ATOM   223  O O    . LYS   A 1 17  ? 3.183  -3.673  -5.295  1   51.985  ? 29  LYS   B O    1 ? 1 
ATOM   224  C CB   . LYS   A 1 17  ? 4.501  -5.648  -6.349  1   56.771  ? 29  LYS   B CB   1 ? 1 
ATOM   225  C CG   . LYS   A 1 17  ? 5.413  -6.619  -7.037  1   58.852  ? 29  LYS   B CG   1 ? 1 
ATOM   226  C CD   . LYS   A 1 17  ? 6.859  -6.145  -7.053  1   55.248  ? 29  LYS   B CD   1 ? 1 
ATOM   227  C CE   . LYS   A 1 17  ? 7.746  -7.022  -7.881  1   61.226  ? 29  LYS   B CE   1 ? 1 
ATOM   228  N NZ   . LYS   A 1 17  ? 9.111  -6.871  -7.373  1   59.356  ? 29  LYS   B NZ   1 ? 1 
ATOM   229  H H    . LYS   A 1 17  ? 5.788  -6.422  -3.55   1   49.51   ? 29  LYS   B H    1 c 1 
ATOM   230  H HA   . LYS   A 1 17  ? 5.888  -4.8    -5.033  1   50.889  ? 29  LYS   B HA   1 c 1 
ATOM   231  H HB2  . LYS   A 1 17  ? 3.619  -6.069  -6.256  1   59.675  ? 29  LYS   B HB2  1 c 1 
ATOM   232  H HB3  . LYS   A 1 17  ? 4.395  -4.867  -6.933  1   58.236  ? 29  LYS   B HB3  1 c 1 
ATOM   233  H HG2  . LYS   A 1 17  ? 5.36   -7.484  -6.575  1   58.595  ? 29  LYS   B HG2  1 c 1 
ATOM   234  H HG3  . LYS   A 1 17  ? 5.103  -6.745  -7.96   1   61.479  ? 29  LYS   B HG3  1 c 1 
ATOM   235  H HD2  . LYS   A 1 17  ? 6.892  -5.23   -7.407  1   56.169  ? 29  LYS   B HD2  1 c 1 
ATOM   236  H HD3  . LYS   A 1 17  ? 7.2    -6.126  -6.134  1   53.694  ? 29  LYS   B HD3  1 c 1 
ATOM   237  H HE2  . LYS   A 1 17  ? 7.471  -7.953  -7.807  1   61.915  ? 29  LYS   B HE2  1 c 1 
ATOM   238  H HE3  . LYS   A 1 17  ? 7.713  -6.753  -8.816  1   62.673  ? 29  LYS   B HE3  1 c 1 
ATOM   239  H HZ1  . LYS   A 1 17  ? 9.176  -7.24   -6.547  1   57.234  ? 29  LYS   B HZ1  1 c 1 
ATOM   240  H HZ2  . LYS   A 1 17  ? 9.33   -5.993  -7.326  1   57.503  ? 29  LYS   B HZ2  1 c 1 
ATOM   241  H HZ3  . LYS   A 1 17  ? 9.69   -7.291  -7.929  1   59.919  ? 29  LYS   B HZ3  1 c 1 
ATOM   242  N N    . ASP   A 1 18  ? 4.252  -3.487  -3.346  1   46.769  ? 30  ASP   B N    1 ? 1 
ATOM   243  C CA   . ASP   A 1 18  ? 3.436  -2.401  -2.861  1   46.445  ? 30  ASP   B CA   1 ? 1 
ATOM   244  C C    . ASP   A 1 18  ? 4.27   -1.12   -2.844  1   45.499  ? 30  ASP   B C    1 ? 1 
ATOM   245  O O    . ASP   A 1 18  ? 3.826  -0.177  -2.2    1   44.728  ? 30  ASP   B O    1 ? 1 
ATOM   246  C CB   . ASP   A 1 18  ? 2.957  -2.724  -1.462  1   46.659  ? 30  ASP   B CB   1 ? 1 
ATOM   247  C CG   . ASP   A 1 18  ? 4.089  -2.996  -0.48   1   42.528  ? 30  ASP   B CG   1 ? 1 
ATOM   248  O OD1  . ASP   A 1 18  ? 5.275  -2.507  -0.717  1   39.365  ? 30  ASP   B OD1  1 ? 1 
ATOM   249  O OD2  . ASP   A 1 18  ? 3.786  -3.661  0.539   1   41.784  ? 30  ASP   B OD2  1 ? 1 
ATOM   250  H H    . ASP   A 1 18  ? 4.939  -3.791  -2.825  1   44.814  ? 30  ASP   B H    1 c 1 
ATOM   251  H HA   . ASP   A 1 18  ? 2.663  -2.281  -3.458  1   49.458  ? 30  ASP   B HA   1 c 1 
ATOM   252  H HB2  . ASP   A 1 18  ? 2.416  -1.981  -1.12   1   46.612  ? 30  ASP   B HB2  1 c 1 
ATOM   253  H HB3  . ASP   A 1 18  ? 2.386  -3.519  -1.5    1   48.237  ? 30  ASP   B HB3  1 c 1 
ATOM   254  N N    . ARG   A 1 19  ? 5.405  -1.103  -3.568  1   43.507  ? 31  ARG   B N    1 ? 1 
ATOM   255  C CA   . ARG   A 1 19  ? 6.299  0.06    -3.679  1   44.023  ? 31  ARG   B CA   1 ? 1 
ATOM   256  C C    . ARG   A 1 19  ? 6.836  0.542   -2.31   1   43.7    ? 31  ARG   B C    1 ? 1 
ATOM   257  O O    . ARG   A 1 19  ? 7.396  1.63    -2.176  1   39.266  ? 31  ARG   B O    1 ? 1 
ATOM   258  C CB   . ARG   A 1 19  ? 5.615  1.177   -4.479  1   48.302  ? 31  ARG   B CB   1 ? 1 
ATOM   259  C CG   . ARG   A 1 19  ? 5.273  0.789   -5.92   1   48.644  ? 31  ARG   B CG   1 ? 1 
ATOM   260  C CD   . ARG   A 1 19  ? 4.695  1.888   -6.763  1   56.988  ? 31  ARG   B CD   1 ? 1 
ATOM   261  N NE   . ARG   A 1 19  ? 5.531  3.102   -6.67   1   55.926  ? 31  ARG   B NE   1 ? 1 
ATOM   262  C CZ   . ARG   A 1 19  ? 6.577  3.436   -7.429  1   54.01   ? 31  ARG   B CZ   1 ? 1 
ATOM   263  N NH1  . ARG   A 1 19  ? 7.087  2.627   -8.298  1   56.874  ? 31  ARG   B NH1  1 ? 1 
ATOM   264  N NH2  . ARG   A 1 19  ? 7.18   4.611   -7.319  1   62.044  ? 31  ARG   B NH2  1 ? 1 
ATOM   265  H H    . ARG   A 1 19  ? 5.635  -1.858  -4.026  1   44.863  ? 31  ARG   B H    1 c 1 
ATOM   266  H HA   . ARG   A 1 19  ? 7.082  -0.222  -4.214  1   44.109  ? 31  ARG   B HA   1 c 1 
ATOM   267  H HB2  . ARG   A 1 19  ? 4.787  1.431   -4.024  1   47.909  ? 31  ARG   B HB2  1 c 1 
ATOM   268  H HB3  . ARG   A 1 19  ? 6.202  1.963   -4.492  1   46.245  ? 31  ARG   B HB3  1 c 1 
ATOM   269  H HG2  . ARG   A 1 19  ? 6.087  0.457   -6.357  1   50.173  ? 31  ARG   B HG2  1 c 1 
ATOM   270  H HG3  . ARG   A 1 19  ? 4.634  0.043   -5.901  1   51.798  ? 31  ARG   B HG3  1 c 1 
ATOM   271  H HD2  . ARG   A 1 19  ? 4.645  1.598   -7.696  1   57.957  ? 31  ARG   B HD2  1 c 1 
ATOM   272  H HD3  . ARG   A 1 19  ? 3.788  2.095   -6.456  1   56.67   ? 31  ARG   B HD3  1 c 1 
ATOM   273  H HE   . ARG   A 1 19  ? 5.32   3.671   -6.045  1   54.496  ? 31  ARG   B HE   1 c 1 
ATOM   274  H HH11 . ARG   A 1 19  ? 7.034  1.753   -8.17   1   56.087  ? 31  ARG   B HH11 1 c 1 
ATOM   275  H HH12 . ARG   A 1 19  ? 7.49   2.948   -9.018  1   57.845  ? 31  ARG   B HH12 1 c 1 
ATOM   276  H HH21 . ARG   A 1 19  ? 6.807  5.251   -6.836  1   58.711  ? 31  ARG   B HH21 1 c 1 
ATOM   277  H HH22 . ARG   A 1 19  ? 7.952  4.755   -7.725  1   59.095  ? 31  ARG   B HH22 1 c 1 
ATOM   278  N N    . GLY   A 1 20  ? 6.85   -0.306  -1.288  1   38.181  ? 32  GLY   B N    1 ? 1 
ATOM   279  C CA   . GLY   A 1 20  ? 7.269  0.135   0.036   1   34.983  ? 32  GLY   B CA   1 ? 1 
ATOM   280  C C    . GLY   A 1 20  ? 8.794  0.305   0.154   1   33.593  ? 32  GLY   B C    1 ? 1 
ATOM   281  O O    . GLY   A 1 20  ? 9.258  0.925   1.073   1   33.055  ? 32  GLY   B O    1 ? 1 
ATOM   282  H H    . GLY   A 1 20  ? 6.612  -1.179  -1.411  1   39.602  ? 32  GLY   B H    1 c 1 
ATOM   283  H HA2  . GLY   A 1 20  ? 6.832  0.988   0.242   1   35.916  ? 32  GLY   B HA2  1 c 1 
ATOM   284  H HA3  . GLY   A 1 20  ? 6.963  -0.524  0.699   1   35.506  ? 32  GLY   B HA3  1 c 1 
ATOM   285  N N    . VAL   A 1 21  ? 9.56   -0.333  -0.729  1   34.406  ? 33  VAL   B N    1 ? 1 
ATOM   286  C CA   . VAL   A 1 21  ? 11.001 -0.218  -0.752  1   32.773  ? 33  VAL   B CA   1 ? 1 
ATOM   287  C C    . VAL   A 1 21  ? 11.421 -0.117  -2.219  1   32.423  ? 33  VAL   B C    1 ? 1 
ATOM   288  O O    . VAL   A 1 21  ? 11.24  -1.075  -2.955  1   34.9    ? 33  VAL   B O    1 ? 1 
ATOM   289  C CB   . VAL   A 1 21  ? 11.731 -1.38   -0.095  1   35.67   ? 33  VAL   B CB   1 ? 1 
ATOM   290  C CG1  . VAL   A 1 21  ? 13.229 -1.13   -0.13   1   28.199  ? 33  VAL   B CG1  1 ? 1 
ATOM   291  C CG2  . VAL   A 1 21  ? 11.187 -1.636  1.324   1   39.207  ? 33  VAL   B CG2  1 ? 1 
ATOM   292  H H    . VAL   A 1 21  ? 9.16   -0.868  -1.352  1   35.296  ? 33  VAL   B H    1 c 1 
ATOM   293  H HA   . VAL   A 1 21  ? 11.255 0.607   -0.296  1   32.535  ? 33  VAL   B HA   1 c 1 
ATOM   294  H HB   . VAL   A 1 21  ? 11.547 -2.184  -0.636  1   34.966  ? 33  VAL   B HB   1 c 1 
ATOM   295  H HG11 . VAL   A 1 21  ? 13.419 -0.244  0.221   1   29.587  ? 33  VAL   B HG11 1 c 1 
ATOM   296  H HG12 . VAL   A 1 21  ? 13.551 -1.191  -1.045  1   30.69   ? 33  VAL   B HG12 1 c 1 
ATOM   297  H HG13 . VAL   A 1 21  ? 13.681 -1.797  0.415   1   29.427  ? 33  VAL   B HG13 1 c 1 
ATOM   298  H HG21 . VAL   A 1 21  ? 11.734 -2.308  1.765   1   37.467  ? 33  VAL   B HG21 1 c 1 
ATOM   299  H HG22 . VAL   A 1 21  ? 10.27  -1.953  1.269   1   38.798  ? 33  VAL   B HG22 1 c 1 
ATOM   300  H HG23 . VAL   A 1 21  ? 11.214 -0.811  1.836   1   37.524  ? 33  VAL   B HG23 1 c 1 
ATOM   301  N N    . LEU   A 1 22  ? 11.968 1.067   -2.603  1   31.843  ? 34  LEU   B N    1 ? 1 
ATOM   302  C CA   . LEU   A 1 22  ? 12.402 1.357   -3.957  1   33.806  ? 34  LEU   B CA   1 ? 1 
ATOM   303  C C    . LEU   A 1 22  ? 13.92  1.548   -3.971  1   34.514  ? 34  LEU   B C    1 ? 1 
ATOM   304  O O    . LEU   A 1 22  ? 14.527 2.17    -3.067  1   33.861  ? 34  LEU   B O    1 ? 1 
ATOM   305  C CB   . LEU   A 1 22  ? 11.611 2.549   -4.487  1   34.872  ? 34  LEU   B CB   1 ? 1 
ATOM   306  C CG   . LEU   A 1 22  ? 10.104 2.395   -4.504  1   39.74   ? 34  LEU   B CG   1 ? 1 
ATOM   307  C CD1  . LEU   A 1 22  ? 9.501  3.745   -4.694  1   41.133  ? 34  LEU   B CD1  1 ? 1 
ATOM   308  C CD2  . LEU   A 1 22  ? 9.615  1.391   -5.581  1   39.871  ? 34  LEU   B CD2  1 ? 1 
ATOM   309  H H    . LEU   A 1 22  ? 12.071 1.72    -1.972  1   31.366  ? 34  LEU   B H    1 c 1 
ATOM   310  H HA   . LEU   A 1 22  ? 12.19  0.571   -4.514  1   34.908  ? 34  LEU   B HA   1 c 1 
ATOM   311  H HB2  . LEU   A 1 22  ? 11.838 3.334   -3.937  1   35.139  ? 34  LEU   B HB2  1 c 1 
ATOM   312  H HB3  . LEU   A 1 22  ? 11.914 2.734   -5.405  1   37.379  ? 34  LEU   B HB3  1 c 1 
ATOM   313  H HG   . LEU   A 1 22  ? 9.817  2.056   -3.617  1   37.323  ? 34  LEU   B HG   1 c 1 
ATOM   314  H HD11 . LEU   A 1 22  ? 9.727  4.313   -3.938  1   39.869  ? 34  LEU   B HD11 1 c 1 
ATOM   315  H HD12 . LEU   A 1 22  ? 8.535  3.664   -4.758  1   42.112  ? 34  LEU   B HD12 1 c 1 
ATOM   316  H HD13 . LEU   A 1 22  ? 9.846  4.144   -5.511  1   42.448  ? 34  LEU   B HD13 1 c 1 
ATOM   317  H HD21 . LEU   A 1 22  ? 9.966  0.51    -5.382  1   39.73   ? 34  LEU   B HD21 1 c 1 
ATOM   318  H HD22 . LEU   A 1 22  ? 9.928  1.674   -6.456  1   41.99   ? 34  LEU   B HD22 1 c 1 
ATOM   319  H HD23 . LEU   A 1 22  ? 8.643  1.36    -5.58   1   41.478  ? 34  LEU   B HD23 1 c 1 
ATOM   320  N N    . LYS   A 1 23  ? 14.547 1.034   -5.032  1   37.409  ? 35  LYS   B N    1 ? 1 
ATOM   321  C CA   . LYS   A 1 23  ? 16     0.963   -5.094  1   33.858  ? 35  LYS   B CA   1 ? 1 
ATOM   322  C C    . LYS   A 1 23  ? 16.532 1.475   -6.408  1   38.497  ? 35  LYS   B C    1 ? 1 
ATOM   323  O O    . LYS   A 1 23  ? 16.026 1.049   -7.459  1   42.475  ? 35  LYS   B O    1 ? 1 
ATOM   324  C CB   . LYS   A 1 23  ? 16.507 -0.48   -5.142  1   35.443  ? 35  LYS   B CB   1 ? 1 
ATOM   325  C CG   . LYS   A 1 23  ? 18.006 -0.596  -4.82   1   34.365  ? 35  LYS   B CG   1 ? 1 
ATOM   326  C CD   . LYS   A 1 23  ? 18.522 -2.039  -4.913  1   35.862  ? 35  LYS   B CD   1 ? 1 
ATOM   327  C CE   . LYS   A 1 23  ? 19.983 -2.214  -4.592  1   38.461  ? 35  LYS   B CE   1 ? 1 
ATOM   328  N NZ   . LYS   A 1 23  ? 20.589 -3.496  -5.035  1   39.292  ? 35  LYS   B NZ   1 ? 1 
ATOM   329  H H    . LYS   A 1 23  ? 14.059 0.724   -5.741  1   37.607  ? 35  LYS   B H    1 c 1 
ATOM   330  H HA   . LYS   A 1 23  ? 16.397 1.463   -4.341  1   34.062  ? 35  LYS   B HA   1 c 1 
ATOM   331  H HB2  . LYS   A 1 23  ? 16.005 -1.014  -4.489  1   33.64   ? 35  LYS   B HB2  1 c 1 
ATOM   332  H HB3  . LYS   A 1 23  ? 16.343 -0.861  -6.03   1   36.586  ? 35  LYS   B HB3  1 c 1 
ATOM   333  H HG2  . LYS   A 1 23  ? 18.51  -0.036  -5.447  1   36.291  ? 35  LYS   B HG2  1 c 1 
ATOM   334  H HG3  . LYS   A 1 23  ? 18.164 -0.256  -3.915  1   33.426  ? 35  LYS   B HG3  1 c 1 
ATOM   335  H HD2  . LYS   A 1 23  ? 17.996 -2.595  -4.298  1   34.937  ? 35  LYS   B HD2  1 c 1 
ATOM   336  H HD3  . LYS   A 1 23  ? 18.356 -2.373  -5.819  1   37.93   ? 35  LYS   B HD3  1 c 1 
ATOM   337  H HE2  . LYS   A 1 23  ? 20.479 -1.484  -5.005  1   38.865  ? 35  LYS   B HE2  1 c 1 
ATOM   338  H HE3  . LYS   A 1 23  ? 20.1   -2.137  -3.629  1   36.245  ? 35  LYS   B HE3  1 c 1 
ATOM   339  H HZ1  . LYS   A 1 23  ? 20.455 -3.608  -5.924  1   41.106  ? 35  LYS   B HZ1  1 c 1 
ATOM   340  H HZ2  . LYS   A 1 23  ? 20.207 -4.184  -4.587  1   38.55   ? 35  LYS   B HZ2  1 c 1 
ATOM   341  H HZ3  . LYS   A 1 23  ? 21.479 -3.488  -4.866  1   39.797  ? 35  LYS   B HZ3  1 c 1 
ATOM   342  N N    . ILE   A 1 24  ? 17.603 2.31    -6.36   1   39.522  ? 36  ILE   B N    1 ? 1 
ATOM   343  C CA   . ILE   A 1 24  ? 18.452 2.492   -7.547  1   46.535  ? 36  ILE   B CA   1 ? 1 
ATOM   344  C C    . ILE   A 1 24  ? 19.881 2.135   -7.148  1   43.603  ? 36  ILE   B C    1 ? 1 
ATOM   345  O O    . ILE   A 1 24  ? 20.348 2.588   -6.13   1   37.705  ? 36  ILE   B O    1 ? 1 
ATOM   346  C CB   . ILE   A 1 24  ? 18.33  3.939   -8.035  1   48.226  ? 36  ILE   B CB   1 ? 1 
ATOM   347  C CG1  . ILE   A 1 24  ? 16.922 4.168   -8.393  1   49.891  ? 36  ILE   B CG1  1 ? 1 
ATOM   348  C CG2  . ILE   A 1 24  ? 19.277 4.296   -9.196  1   54.611  ? 36  ILE   B CG2  1 ? 1 
ATOM   349  C CD1  . ILE   A 1 24  ? 16.654 5.496   -9.03   1   54.761  ? 36  ILE   B CD1  1 ? 1 
ATOM   350  H H    . ILE   A 1 24  ? 17.801 2.764   -5.592  1   38.968  ? 36  ILE   B H    1 c 1 
ATOM   351  H HA   . ILE   A 1 24  ? 18.154 1.889   -8.255  1   46.395  ? 36  ILE   B HA   1 c 1 
ATOM   352  H HB   . ILE   A 1 24  ? 18.544 4.525   -7.282  1   47.811  ? 36  ILE   B HB   1 c 1 
ATOM   353  H HG12 . ILE   A 1 24  ? 16.638 3.464   -9.01   1   51.085  ? 36  ILE   B HG12 1 c 1 
ATOM   354  H HG13 . ILE   A 1 24  ? 16.376 4.096   -7.584  1   47.868  ? 36  ILE   B HG13 1 c 1 
ATOM   355  H HG21 . ILE   A 1 24  ? 19.291 5.26    -9.323  1   55.026  ? 36  ILE   B HG21 1 c 1 
ATOM   356  H HG22 . ILE   A 1 24  ? 18.967 3.868   -10.012 1   55.508  ? 36  ILE   B HG22 1 c 1 
ATOM   357  H HG23 . ILE   A 1 24  ? 20.176 3.988   -8.993  1   53.721  ? 36  ILE   B HG23 1 c 1 
ATOM   358  H HD11 . ILE   A 1 24  ? 17.052 6.203   -8.487  1   53.463  ? 36  ILE   B HD11 1 c 1 
ATOM   359  H HD12 . ILE   A 1 24  ? 15.691 5.638   -9.091  1   54.046  ? 36  ILE   B HD12 1 c 1 
ATOM   360  H HD13 . ILE   A 1 24  ? 17.039 5.521   -9.926  1   56.625  ? 36  ILE   B HD13 1 c 1 
ATOM   361  N N    . VAL   A 1 25  ? 20.587 1.361   -7.961  1   43.952  ? 37  VAL   B N    1 ? 1 
ATOM   362  C CA   . VAL   A 1 25  ? 22.013 1.121   -7.789  1   44.169  ? 37  VAL   B CA   1 ? 1 
ATOM   363  C C    . VAL   A 1 25  ? 22.736 2.371   -8.281  1   51.945  ? 37  VAL   B C    1 ? 1 
ATOM   364  O O    . VAL   A 1 25  ? 22.581 2.73    -9.44   1   48.281  ? 37  VAL   B O    1 ? 1 
ATOM   365  C CB   . VAL   A 1 25  ? 22.439 -0.123  -8.588  1   48.295  ? 37  VAL   B CB   1 ? 1 
ATOM   366  C CG1  . VAL   A 1 25  ? 23.949 -0.318  -8.713  1   52.071  ? 37  VAL   B CG1  1 ? 1 
ATOM   367  C CG2  . VAL   A 1 25  ? 21.723 -1.36   -8.097  1   45.811  ? 37  VAL   B CG2  1 ? 1 
ATOM   368  H H    . VAL   A 1 25  ? 20.162 0.963   -8.665  1   45.52   ? 37  VAL   B H    1 c 1 
ATOM   369  H HA   . VAL   A 1 25  ? 22.207 0.981   -6.842  1   43.525  ? 37  VAL   B HA   1 c 1 
ATOM   370  H HB   . VAL   A 1 25  ? 22.117 0.022   -9.509  1   50.249  ? 37  VAL   B HB   1 c 1 
ATOM   371  H HG11 . VAL   A 1 25  ? 24.355 -0.286  -7.83   1   49.949  ? 37  VAL   B HG11 1 c 1 
ATOM   372  H HG12 . VAL   A 1 25  ? 24.326 0.386   -9.267  1   53.833  ? 37  VAL   B HG12 1 c 1 
ATOM   373  H HG13 . VAL   A 1 25  ? 24.133 -1.181  -9.122  1   52.625  ? 37  VAL   B HG13 1 c 1 
ATOM   374  H HG21 . VAL   A 1 25  ? 22.056 -2.139  -8.574  1   47.345  ? 37  VAL   B HG21 1 c 1 
ATOM   375  H HG22 . VAL   A 1 25  ? 20.768 -1.269  -8.256  1   45.453  ? 37  VAL   B HG22 1 c 1 
ATOM   376  H HG23 . VAL   A 1 25  ? 21.883 -1.471  -7.145  1   43.77   ? 37  VAL   B HG23 1 c 1 
ATOM   377  N N    . LYS   A 1 26  ? 23.543 3.01    -7.428  1   49.459  ? 38  LYS   B N    1 ? 1 
ATOM   378  C CA   . LYS   A 1 26  ? 24.256 4.197   -7.899  1   51.3    ? 38  LYS   B CA   1 ? 1 
ATOM   379  C C    . LYS   A 1 26  ? 25.707 3.882   -8.204  1   53.156  ? 38  LYS   B C    1 ? 1 
ATOM   380  O O    . LYS   A 1 26  ? 26.278 4.546   -9.003  1   54.943  ? 38  LYS   B O    1 ? 1 
ATOM   381  C CB   . LYS   A 1 26  ? 24.188 5.27    -6.796  1   49.469  ? 38  LYS   B CB   1 ? 1 
ATOM   382  C CG   . LYS   A 1 26  ? 22.8   5.728   -6.427  1   47.776  ? 38  LYS   B CG   1 ? 1 
ATOM   383  C CD   . LYS   A 1 26  ? 21.905 6.18    -7.563  1   48.156  ? 38  LYS   B CD   1 ? 1 
ATOM   384  C CE   . LYS   A 1 26  ? 22.444 7.364   -8.121  1   50.221  ? 38  LYS   B CE   1 ? 1 
ATOM   385  N NZ   . LYS   A 1 26  ? 21.541 7.972   -9.089  1   56.187  ? 38  LYS   B NZ   1 ? 1 
ATOM   386  H H    . LYS   A 1 26  ? 23.653 2.721   -6.569  1   47.586  ? 38  LYS   B H    1 c 1 
ATOM   387  H HA   . LYS   A 1 26  ? 23.82  4.535   -8.721  1   52.956  ? 38  LYS   B HA   1 c 1 
ATOM   388  H HB2  . LYS   A 1 26  ? 24.619 4.914   -5.99   1   48.348  ? 38  LYS   B HB2  1 c 1 
ATOM   389  H HB3  . LYS   A 1 26  ? 24.705 6.05    -7.087  1   52.103  ? 38  LYS   B HB3  1 c 1 
ATOM   390  H HG2  . LYS   A 1 26  ? 22.354 4.991   -5.956  1   44.94   ? 38  LYS   B HG2  1 c 1 
ATOM   391  H HG3  . LYS   A 1 26  ? 22.886 6.466   -5.785  1   46.997  ? 38  LYS   B HG3  1 c 1 
ATOM   392  H HD2  . LYS   A 1 26  ? 21.853 5.484   -8.253  1   48.935  ? 38  LYS   B HD2  1 c 1 
ATOM   393  H HD3  . LYS   A 1 26  ? 21.001 6.36    -7.222  1   46.499  ? 38  LYS   B HD3  1 c 1 
ATOM   394  H HE2  . LYS   A 1 26  ? 22.625 8.01    -7.414  1   50.978  ? 38  LYS   B HE2  1 c 1 
ATOM   395  H HE3  . LYS   A 1 26  ? 23.286 7.162   -8.567  1   53.474  ? 38  LYS   B HE3  1 c 1 
ATOM   396  H HZ1  . LYS   A 1 26  ? 20.757 8.186   -8.688  1   53.224  ? 38  LYS   B HZ1  1 c 1 
ATOM   397  H HZ2  . LYS   A 1 26  ? 21.381 7.393   -9.766  1   55.705  ? 38  LYS   B HZ2  1 c 1 
ATOM   398  H HZ3  . LYS   A 1 26  ? 21.916 8.725   -9.425  1   57.357  ? 38  LYS   B HZ3  1 c 1 
ATOM   399  N N    . ARG   A 1 27  ? 26.37  2.927   -7.543  1   50.56   ? 39  ARG   B N    1 ? 1 
ATOM   400  C CA   . ARG   A 1 27  ? 27.708 2.522   -7.995  1   55.665  ? 39  ARG   B CA   1 ? 1 
ATOM   401  C C    . ARG   A 1 27  ? 27.743 0.997   -7.997  1   52.696  ? 39  ARG   B C    1 ? 1 
ATOM   402  O O    . ARG   A 1 27  ? 27.31  0.399   -7.038  1   51.539  ? 39  ARG   B O    1 ? 1 
ATOM   403  C CB   . ARG   A 1 27  ? 28.889 3.109   -7.2    1   57.911  ? 39  ARG   B CB   1 ? 1 
ATOM   404  C CG   . ARG   A 1 27  ? 30.281 2.784   -7.732  1   65.991  ? 39  ARG   B CG   1 ? 1 
ATOM   405  C CD   . ARG   A 1 27  ? 31.386 3.323   -6.788  1   72.852  ? 39  ARG   B CD   1 ? 1 
ATOM   406  N NE   . ARG   A 1 27  ? 31.356 2.486   -5.578  1   75.819  ? 39  ARG   B NE   1 ? 1 
ATOM   407  C CZ   . ARG   A 1 27  ? 31.921 2.749   -4.402  1   72.803  ? 39  ARG   B CZ   1 ? 1 
ATOM   408  N NH1  . ARG   A 1 27  ? 32.634 3.869   -4.235  1   73.064  ? 39  ARG   B NH1  1 ? 1 
ATOM   409  N NH2  . ARG   A 1 27  ? 31.8   1.85    -3.427  1   64.546  ? 39  ARG   B NH2  1 ? 1 
ATOM   410  H H    . ARG   A 1 27  ? 26.001 2.526   -6.809  1   48.638  ? 39  ARG   B H    1 c 1 
ATOM   411  H HA   . ARG   A 1 27  ? 27.815 2.823   -8.933  1   57.918  ? 39  ARG   B HA   1 c 1 
ATOM   412  H HB2  . ARG   A 1 27  ? 28.787 4.084   -7.175  1   59.301  ? 39  ARG   B HB2  1 c 1 
ATOM   413  H HB3  . ARG   A 1 27  ? 28.826 2.785   -6.276  1   56.152  ? 39  ARG   B HB3  1 c 1 
ATOM   414  H HG2  . ARG   A 1 27  ? 30.38  1.811   -7.822  1   65.7    ? 39  ARG   B HG2  1 c 1 
ATOM   415  H HG3  . ARG   A 1 27  ? 30.392 3.187   -8.62   1   69.005  ? 39  ARG   B HG3  1 c 1 
ATOM   416  H HD2  . ARG   A 1 27  ? 32.266 3.26    -7.213  1   76.217  ? 39  ARG   B HD2  1 c 1 
ATOM   417  H HD3  . ARG   A 1 27  ? 31.212 4.256   -6.55   1   73.076  ? 39  ARG   B HD3  1 c 1 
ATOM   418  H HE   . ARG   A 1 27  ? 30.923 1.731   -5.632  1   71.539  ? 39  ARG   B HE   1 c 1 
ATOM   419  H HH11 . ARG   A 1 27  ? 32.999 4.275   -4.931  1   76.688  ? 39  ARG   B HH11 1 c 1 
ATOM   420  H HH12 . ARG   A 1 27  ? 32.739 4.199   -3.421  1   73.441  ? 39  ARG   B HH12 1 c 1 
ATOM   421  H HH21 . ARG   A 1 27  ? 31.154 1.247   -3.455  1   63.935  ? 39  ARG   B HH21 1 c 1 
ATOM   422  H HH22 . ARG   A 1 27  ? 32.37  1.861   -2.751  1   66.748  ? 39  ARG   B HH22 1 c 1 
ATOM   423  N N    . VAL   A 1 28  ? 28.138 0.363   -9.1    1   55.104  ? 40  VAL   B N    1 ? 1 
ATOM   424  C CA   . VAL   A 1 28  ? 28.007 -1.08   -9.204  1   56.999  ? 40  VAL   B CA   1 ? 1 
ATOM   425  C C    . VAL   A 1 28  ? 29.15  -1.704  -8.419  1   56.917  ? 40  VAL   B C    1 ? 1 
ATOM   426  O O    . VAL   A 1 28  ? 30.277 -1.193  -8.429  1   58.26   ? 40  VAL   B O    1 ? 1 
ATOM   427  C CB   . VAL   A 1 28  ? 28.072 -1.419  -10.71  1   66.713  ? 40  VAL   B CB   1 ? 1 
ATOM   428  C CG1  . VAL   A 1 28  ? 28.57  -2.844  -10.978 1   64.839  ? 40  VAL   B CG1  1 ? 1 
ATOM   429  C CG2  . VAL   A 1 28  ? 26.697 -1.145  -11.316 1   68.095  ? 40  VAL   B CG2  1 ? 1 
ATOM   430  H H    . VAL   A 1 28  ? 28.5   0.834   -9.795  1   58.895  ? 40  VAL   B H    1 c 1 
ATOM   431  H HA   . VAL   A 1 28  ? 27.148 -1.362  -8.834  1   54.72   ? 40  VAL   B HA   1 c 1 
ATOM   432  H HB   . VAL   A 1 28  ? 28.716 -0.798  -11.125 1   68.032  ? 40  VAL   B HB   1 c 1 
ATOM   433  H HG11 . VAL   A 1 28  ? 28.106 -3.467  -10.392 1   63.033  ? 40  VAL   B HG11 1 c 1 
ATOM   434  H HG12 . VAL   A 1 28  ? 29.526 -2.894  -10.812 1   67.277  ? 40  VAL   B HG12 1 c 1 
ATOM   435  H HG13 . VAL   A 1 28  ? 28.392 -3.08   -11.904 1   68.299  ? 40  VAL   B HG13 1 c 1 
ATOM   436  H HG21 . VAL   A 1 28  ? 26.7   -1.398  -12.254 1   70.398  ? 40  VAL   B HG21 1 c 1 
ATOM   437  H HG22 . VAL   A 1 28  ? 26.491 -0.198  -11.237 1   67.172  ? 40  VAL   B HG22 1 c 1 
ATOM   438  H HG23 . VAL   A 1 28  ? 26.024 -1.663  -10.844 1   64.691  ? 40  VAL   B HG23 1 c 1 
ATOM   439  N N    . GLY   A 1 29  ? 28.825 -2.781  -7.72   1   62.649  ? 41  GLY   B N    1 ? 1 
ATOM   440  C CA   . GLY   A 1 29  ? 29.78  -3.516  -6.905  1   64.767  ? 41  GLY   B CA   1 ? 1 
ATOM   441  C C    . GLY   A 1 29  ? 30.588 -4.464  -7.778  1   67.07   ? 41  GLY   B C    1 ? 1 
ATOM   442  O O    . GLY   A 1 29  ? 30.67  -4.277  -8.978  1   72.946  ? 41  GLY   B O    1 ? 1 
ATOM   443  H H    . GLY   A 1 29  ? 27.962 -3.079  -7.748  1   59.134  ? 41  GLY   B H    1 c 1 
ATOM   444  H HA2  . GLY   A 1 29  ? 30.383 -2.882  -6.451  1   64.312  ? 41  GLY   B HA2  1 c 1 
ATOM   445  H HA3  . GLY   A 1 29  ? 29.295 -4.028  -6.216  1   61.361  ? 41  GLY   B HA3  1 c 1 
ATOM   446  N N    . ASN   A 1 30  ? 31.131 -5.514  -7.172  1   72.062  ? 42  ASN   B N    1 ? 1 
ATOM   447  C CA   . ASN   A 1 30  ? 31.927 -6.478  -7.91   1   80.378  ? 42  ASN   B CA   1 ? 1 
ATOM   448  C C    . ASN   A 1 30  ? 31.588 -7.86   -7.371  1   76.63   ? 42  ASN   B C    1 ? 1 
ATOM   449  O O    . ASN   A 1 30  ? 31.208 -7.985  -6.212  1   71.352  ? 42  ASN   B O    1 ? 1 
ATOM   450  C CB   . ASN   A 1 30  ? 33.406 -6.141  -7.792  1   88.445  ? 42  ASN   B CB   1 ? 1 
ATOM   451  C CG   . ASN   A 1 30  ? 33.781 -6.06   -6.334  1   90.473  ? 42  ASN   B CG   1 ? 1 
ATOM   452  O OD1  . ASN   A 1 30  ? 33.848 -7.096  -5.666  1   98.009  ? 42  ASN   B OD1  1 ? 1 
ATOM   453  N ND2  . ASN   A 1 30  ? 33.952 -4.859  -5.796  1   89.694  ? 42  ASN   B ND2  1 ? 1 
ATOM   454  H H    . ASN   A 1 30  ? 31     -5.638  -6.275  1   69.468  ? 42  ASN   B H    1 c 1 
ATOM   455  H HA   . ASN   A 1 30  ? 31.681 -6.436  -8.861  1   81.585  ? 42  ASN   B HA   1 c 1 
ATOM   456  H HB2  . ASN   A 1 30  ? 33.939 -6.834  -8.231  1   90.935  ? 42  ASN   B HB2  1 c 1 
ATOM   457  H HB3  . ASN   A 1 30  ? 33.588 -5.285  -8.226  1   89.951  ? 42  ASN   B HB3  1 c 1 
ATOM   458  H HD21 . ASN   A 1 30  ? 34.293 -4.785  -4.98   1   89.244  ? 42  ASN   B HD21 1 c 1 
ATOM   459  H HD22 . ASN   A 1 30  ? 33.724 -4.13   -6.249  1   90.1    ? 42  ASN   B HD22 1 c 1 
ATOM   460  N N    . GLY   A 1 31  ? 31.744 -8.875  -8.233  1   84.766  ? 43  GLY   B N    1 ? 1 
ATOM   461  C CA   . GLY   A 1 31  ? 31.344 -10.245 -7.932  1   82.328  ? 43  GLY   B CA   1 ? 1 
ATOM   462  C C    . GLY   A 1 31  ? 29.85  -10.472 -8.162  1   77.266  ? 43  GLY   B C    1 ? 1 
ATOM   463  O O    . GLY   A 1 31  ? 29.096 -9.551  -8.422  1   81.317  ? 43  GLY   B O    1 ? 1 
ATOM   464  H H    . GLY   A 1 31  ? 32.122 -8.704  -9.047  1   85.996  ? 43  GLY   B H    1 c 1 
ATOM   465  H HA2  . GLY   A 1 31  ? 31.86  -10.861 -8.503  1   85.157  ? 43  GLY   B HA2  1 c 1 
ATOM   466  H HA3  . GLY   A 1 31  ? 31.566 -10.446 -6.992  1   80.441  ? 43  GLY   B HA3  1 c 1 
ATOM   467  N N    . GLU   A 1 32  ? 29.433 -11.726 -8.092  1   78.363  ? 44  GLU   B N    1 ? 1 
ATOM   468  C CA   . GLU   A 1 32  ? 28.034 -12.054 -8.244  1   73.228  ? 44  GLU   B CA   1 ? 1 
ATOM   469  C C    . GLU   A 1 32  ? 27.437 -12.237 -6.84   1   64.924  ? 44  GLU   B C    1 ? 1 
ATOM   470  O O    . GLU   A 1 32  ? 26.25  -12.138 -6.683  1   59.286  ? 44  GLU   B O    1 ? 1 
ATOM   471  C CB   . GLU   A 1 32  ? 27.982 -13.207 -9.264  1   75.51   ? 44  GLU   B CB   1 ? 1 
ATOM   472  H H    . GLU   A 1 32  ? 30.036 -12.397 -7.944  1   78.726  ? 44  GLU   B H    1 c 1 
ATOM   473  H HA   . GLU   A 1 32  ? 27.58  -11.281 -8.664  1   72.364  ? 44  GLU   B HA   1 c 1 
ATOM   474  H HB2  . GLU   A 1 32  ? 28.936 -13.652 -9.283  0   30      ? 44  GLU   B HB2  1 c 1 
ATOM   475  H HB3  . GLU   A 1 32  ? 27.081 -13.582 -9.235  0   30      ? 44  GLU   B HB3  1 c 1 
ATOM   476  N N    . GLU   A 1 33  ? 28.217 -12.489 -5.779  1   66.063  ? 45  GLU   B N    1 ? 1 
ATOM   477  C CA   . GLU   A 1 33  ? 27.611 -12.872 -4.498  1   60.294  ? 45  GLU   B CA   1 ? 1 
ATOM   478  C C    . GLU   A 1 33  ? 26.896 -11.673 -3.856  1   57.848  ? 45  GLU   B C    1 ? 1 
ATOM   479  O O    . GLU   A 1 33  ? 27.399 -10.552 -3.803  1   50.982  ? 45  GLU   B O    1 ? 1 
ATOM   480  C CB   . GLU   A 1 33  ? 28.643 -13.535 -3.574  1   61.447  ? 45  GLU   B CB   1 ? 1 
ATOM   481  H H    . GLU   A 1 33  ? 29.126 -12.421 -5.844  1   66.618  ? 45  GLU   B H    1 c 1 
ATOM   482  H HA   . GLU   A 1 33  ? 26.925 -13.562 -4.689  1   61.276  ? 45  GLU   B HA   1 c 1 
ATOM   483  H HB2  . GLU   A 1 33  ? 29.508 -13.336 -3.856  0   30      ? 45  GLU   B HB2  1 c 1 
ATOM   484  H HB3  . GLU   A 1 33  ? 28.104 -14.018 -2.851  0   30      ? 45  GLU   B HB3  1 c 1 
ATOM   485  N N    . THR   A 1 34  ? 25.705 -11.917 -3.301  1   53.152  ? 46  THR   B N    1 ? 1 
ATOM   486  C CA   . THR   A 1 34  ? 25.027 -10.991 -2.416  1   48.217  ? 46  THR   B CA   1 ? 1 
ATOM   487  C C    . THR   A 1 34  ? 24.8   -11.674 -1.076  1   52.362  ? 46  THR   B C    1 ? 1 
ATOM   488  O O    . THR   A 1 34  ? 24.971 -12.848 -0.918  1   51.276  ? 46  THR   B O    1 ? 1 
ATOM   489  C CB   . THR   A 1 34  ? 23.71  -10.577 -3.018  1   48.599  ? 46  THR   B CB   1 ? 1 
ATOM   490  O OG1  . THR   A 1 34  ? 23.091 -11.856 -3.133  1   44.501  ? 46  THR   B OG1  1 ? 1 
ATOM   491  C CG2  . THR   A 1 34  ? 23.894 -9.931  -4.375  1   46.697  ? 46  THR   B CG2  1 ? 1 
ATOM   492  H H    . THR   A 1 34  ? 25.292 -12.71  -3.489  1   54.085  ? 46  THR   B H    1 c 1 
ATOM   493  H HA   . THR   A 1 34  ? 25.588 -10.196 -2.288  1   49.438  ? 46  THR   B HA   1 c 1 
ATOM   494  H HB   . THR   A 1 34  ? 23.195 -9.999  -2.407  1   44.66   ? 46  THR   B HB   1 c 1 
ATOM   495  H HG1  . THR   A 1 34  ? 23.529 -12.346 -3.691  0   30      ? 46  THR   B HG1  1 c 1 
ATOM   496  H HG21 . THR   A 1 34  ? 23.046 -9.568  -4.679  1   47.151  ? 46  THR   B HG21 1 c 1 
ATOM   497  H HG22 . THR   A 1 34  ? 24.208 -10.595 -5.012  1   49.873  ? 46  THR   B HG22 1 c 1 
ATOM   498  H HG23 . THR   A 1 34  ? 24.547 -9.214  -4.308  1   47.632  ? 46  THR   B HG23 1 c 1 
ATOM   499  N N    . PRO   A 1 35  ? 24.574 -10.96  0.009   1   47.26   ? 47  PRO   B N    1 ? 1 
ATOM   500  C CA   . PRO   A 1 35  ? 24.602 -11.642 1.297   1   43.898  ? 47  PRO   B CA   1 ? 1 
ATOM   501  C C    . PRO   A 1 35  ? 23.401 -12.537 1.503   1   39.906  ? 47  PRO   B C    1 ? 1 
ATOM   502  O O    . PRO   A 1 35  ? 22.316 -12.152 1.122   1   43.57   ? 47  PRO   B O    1 ? 1 
ATOM   503  C CB   . PRO   A 1 35  ? 24.553 -10.515 2.311   1   38.569  ? 47  PRO   B CB   1 ? 1 
ATOM   504  C CG   . PRO   A 1 35  ? 24.263 -9.287  1.492   1   42.037  ? 47  PRO   B CG   1 ? 1 
ATOM   505  C CD   . PRO   A 1 35  ? 24.553 -9.5    0.071   1   42.931  ? 47  PRO   B CD   1 ? 1 
ATOM   506  H HA   . PRO   A 1 35  ? 25.432 -12.154 1.392   1   44.488  ? 47  PRO   B HA   1 c 1 
ATOM   507  H HB2  . PRO   A 1 35  ? 23.857 -10.671 2.973   1   39.621  ? 47  PRO   B HB2  1 c 1 
ATOM   508  H HB3  . PRO   A 1 35  ? 25.41  -10.428 2.773   1   41.095  ? 47  PRO   B HB3  1 c 1 
ATOM   509  H HG2  . PRO   A 1 35  ? 23.323 -9.042  1.596   1   39.604  ? 47  PRO   B HG2  1 c 1 
ATOM   510  H HG3  . PRO   A 1 35  ? 24.8   -8.54   1.822   1   40.722  ? 47  PRO   B HG3  1 c 1 
ATOM   511  H HD2  . PRO   A 1 35  ? 23.852 -9.133  -0.5    1   43.147  ? 47  PRO   B HD2  1 c 1 
ATOM   512  H HD3  . PRO   A 1 35  ? 25.418 -9.124  -0.183  1   44.69   ? 47  PRO   B HD3  1 c 1 
ATOM   513  N N    . MET   A 1 36  ? 23.648 -13.647 2.189   1   41.813  ? 48  MET   B N    1 ? 1 
ATOM   514  C CA   . MET   A 1 36  ? 22.61  -14.546 2.656   1   40.844  ? 48  MET   B CA   1 ? 1 
ATOM   515  C C    . MET   A 1 36  ? 22.162 -14.136 4.072   1   39.995  ? 48  MET   B C    1 ? 1 
ATOM   516  O O    . MET   A 1 36  ? 22.894 -13.483 4.855   1   40.445  ? 48  MET   B O    1 ? 1 
ATOM   517  C CB   . MET   A 1 36  ? 23.216 -15.943 2.717   1   45.891  ? 48  MET   B CB   1 ? 1 
ATOM   518  C CG   . MET   A 1 36  ? 23.82  -16.507 1.44    1   52.278  ? 48  MET   B CG   1 ? 1 
ATOM   519  S SD   . MET   A 1 36  ? 22.571 -17.107 0.279   1   58.596  ? 48  MET   B SD   1 ? 1 
ATOM   520  C CE   . MET   A 1 36  ? 22.217 -15.808 -0.908  1   61.307  ? 48  MET   B CE   1 ? 1 
ATOM   521  H H    . MET   A 1 36  ? 24.517 -13.858 2.379   1   42.459  ? 48  MET   B H    1 c 1 
ATOM   522  H HA   . MET   A 1 36  ? 21.842 -14.525 2.029   1   41.411  ? 48  MET   B HA   1 c 1 
ATOM   523  H HB2  . MET   A 1 36  ? 23.914 -15.937 3.406   1   46.501  ? 48  MET   B HB2  1 c 1 
ATOM   524  H HB3  . MET   A 1 36  ? 22.517 -16.56  3.022   1   46.807  ? 48  MET   B HB3  1 c 1 
ATOM   525  H HG2  . MET   A 1 36  ? 24.351 -15.816 0.998   1   51.534  ? 48  MET   B HG2  1 c 1 
ATOM   526  H HG3  . MET   A 1 36  ? 24.418 -17.247 1.665   1   53.728  ? 48  MET   B HG3  1 c 1 
ATOM   527  H HE1  . MET   A 1 36  ? 21.637 -16.161 -1.607  1   61.444  ? 48  MET   B HE1  1 c 1 
ATOM   528  H HE2  . MET   A 1 36  ? 21.777 -15.064 -0.456  1   58.247  ? 48  MET   B HE2  1 c 1 
ATOM   529  H HE3  . MET   A 1 36  ? 23.051 -15.498 -1.307  1   60.623  ? 48  MET   B HE3  1 c 1 
ATOM   530  N N    . ILE   A 1 37  ? 20.95  -14.533 4.434   1   38.365  ? 49  ILE   B N    1 ? 1 
ATOM   531  C CA   . ILE   A 1 37  ? 20.473 -14.35  5.79    1   37.738  ? 49  ILE   B CA   1 ? 1 
ATOM   532  C C    . ILE   A 1 37  ? 21.443 -15.031 6.734   1   36.522  ? 49  ILE   B C    1 ? 1 
ATOM   533  O O    . ILE   A 1 37  ? 21.857 -16.193 6.551   1   39.063  ? 49  ILE   B O    1 ? 1 
ATOM   534  C CB   . ILE   A 1 37  ? 19.016 -14.841 5.974   1   44.033  ? 49  ILE   B CB   1 ? 1 
ATOM   535  C CG1  . ILE   A 1 37  ? 18.028 -13.924 5.203   1   43.621  ? 49  ILE   B CG1  1 ? 1 
ATOM   536  C CG2  . ILE   A 1 37  ? 18.622 -14.907 7.461   1   43.652  ? 49  ILE   B CG2  1 ? 1 
ATOM   537  C CD1  . ILE   A 1 37  ? 16.584 -14.381 5.268   1   51.648  ? 49  ILE   B CD1  1 ? 1 
ATOM   538  H H    . ILE   A 1 37  ? 20.401 -14.931 3.821   1   39.304  ? 49  ILE   B H    1 c 1 
ATOM   539  H HA   . ILE   A 1 37  ? 20.486 -13.392 5.98    1   36.71   ? 49  ILE   B HA   1 c 1 
ATOM   540  H HB   . ILE   A 1 37  ? 18.949 -15.742 5.598   1   44.379  ? 49  ILE   B HB   1 c 1 
ATOM   541  H HG12 . ILE   A 1 37  ? 18.089 -13.019 5.571   1   43.416  ? 49  ILE   B HG12 1 c 1 
ATOM   542  H HG13 . ILE   A 1 37  ? 18.304 -13.885 4.265   1   44.547  ? 49  ILE   B HG13 1 c 1 
ATOM   543  H HG21 . ILE   A 1 37  ? 17.691 -15.169 7.543   1   44.671  ? 49  ILE   B HG21 1 c 1 
ATOM   544  H HG22 . ILE   A 1 37  ? 18.747 -14.033 7.869   1   42.734  ? 49  ILE   B HG22 1 c 1 
ATOM   545  H HG23 . ILE   A 1 37  ? 19.179 -15.558 7.919   1   45.368  ? 49  ILE   B HG23 1 c 1 
ATOM   546  H HD11 . ILE   A 1 37  ? 16.535 -15.34  5.09    1   51.148  ? 49  ILE   B HD11 1 c 1 
ATOM   547  H HD12 . ILE   A 1 37  ? 16.069 -13.901 4.593   1   48.733  ? 49  ILE   B HD12 1 c 1 
ATOM   548  H HD13 . ILE   A 1 37  ? 16.213 -14.195 6.15    1   49.385  ? 49  ILE   B HD13 1 c 1 
ATOM   549  N N    . GLY   A 1 38  ? 21.794 -14.292 7.771   1   37.411  ? 50  GLY   B N    1 ? 1 
ATOM   550  C CA   . GLY   A 1 38  ? 22.675 -14.802 8.822   1   40.148  ? 50  GLY   B CA   1 ? 1 
ATOM   551  C C    . GLY   A 1 38  ? 24.082 -14.222 8.672   1   40.169  ? 50  GLY   B C    1 ? 1 
ATOM   552  O O    . GLY   A 1 38  ? 24.936 -14.435 9.514   1   41.322  ? 50  GLY   B O    1 ? 1 
ATOM   553  H H    . GLY   A 1 38  ? 21.478 -13.437 7.841   1   35.908  ? 50  GLY   B H    1 c 1 
ATOM   554  H HA2  . GLY   A 1 38  ? 22.306 -14.555 9.702   1   40.247  ? 50  GLY   B HA2  1 c 1 
ATOM   555  H HA3  . GLY   A 1 38  ? 22.714 -15.786 8.773   1   41.526  ? 50  GLY   B HA3  1 c 1 
ATOM   556  N N    . ASP   A 1 39  ? 24.399 -13.746 7.475   1   39.483  ? 51  ASP   B N    1 ? 1 
ATOM   557  C CA   . ASP   A 1 39  ? 25.712 -13.209 7.223   1   43.779  ? 51  ASP   B CA   1 ? 1 
ATOM   558  C C    . ASP   A 1 39  ? 25.927 -11.933 8.036   1   44.121  ? 51  ASP   B C    1 ? 1 
ATOM   559  O O    . ASP   A 1 39  ? 25.007 -11.146 8.288   1   42.568  ? 51  ASP   B O    1 ? 1 
ATOM   560  C CB   . ASP   A 1 39  ? 25.954 -12.822 5.768   1   42.968  ? 51  ASP   B CB   1 ? 1 
ATOM   561  C CG   . ASP   A 1 39  ? 26.139 -13.979 4.805   1   48.387  ? 51  ASP   B CG   1 ? 1 
ATOM   562  O OD1  . ASP   A 1 39  ? 26.18  -15.167 5.31    1   48.591  ? 51  ASP   B OD1  1 ? 1 
ATOM   563  O OD2  . ASP   A 1 39  ? 26.095 -13.699 3.572   1   49.178  ? 51  ASP   B OD2  1 ? 1 
ATOM   564  H H    . ASP   A 1 39  ? 23.788 -13.757 6.796   1   39.183  ? 51  ASP   B H    1 c 1 
ATOM   565  H HA   . ASP   A 1 39  ? 26.381 -13.878 7.49    1   44.998  ? 51  ASP   B HA   1 c 1 
ATOM   566  H HB2  . ASP   A 1 39  ? 25.196 -12.285 5.457   1   42.21   ? 51  ASP   B HB2  1 c 1 
ATOM   567  H HB3  . ASP   A 1 39  ? 26.757 -12.262 5.719   1   44.25   ? 51  ASP   B HB3  1 c 1 
ATOM   568  N N    . LYS   A 1 40  ? 27.198 -11.736 8.397   1   45.452  ? 52  LYS   B N    1 ? 1 
ATOM   569  C CA   . LYS   A 1 40  ? 27.651 -10.5   9.047   1   48.397  ? 52  LYS   B CA   1 ? 1 
ATOM   570  C C    . LYS   A 1 40  ? 27.897 -9.471  7.952   1   41.964  ? 52  LYS   B C    1 ? 1 
ATOM   571  O O    . LYS   A 1 40  ? 28.56  -9.778  7       1   44.384  ? 52  LYS   B O    1 ? 1 
ATOM   572  C CB   . LYS   A 1 40  ? 28.923 -10.782 9.878   1   48.618  ? 52  LYS   B CB   1 ? 1 
ATOM   573  C CG   . LYS   A 1 40  ? 29.096 -9.745  10.96   1   53.919  ? 52  LYS   B CG   1 ? 1 
ATOM   574  C CD   . LYS   A 1 40  ? 30.216 -10.02  11.948  1   64.693  ? 52  LYS   B CD   1 ? 1 
ATOM   575  C CE   . LYS   A 1 40  ? 30.692 -8.723  12.526  1   71.527  ? 52  LYS   B CE   1 ? 1 
ATOM   576  N NZ   . LYS   A 1 40  ? 31.994 -8.778  13.177  1   78.206  ? 52  LYS   B NZ   1 ? 1 
ATOM   577  H H    . LYS   A 1 40  ? 27.813 -12.393 8.235   1   47.588  ? 52  LYS   B H    1 c 1 
ATOM   578  H HA   . LYS   A 1 40  ? 26.932 -10.174 9.645   1   45.605  ? 52  LYS   B HA   1 c 1 
ATOM   579  H HB2  . LYS   A 1 40  ? 28.857 -11.669 10.292  1   51.309  ? 52  LYS   B HB2  1 c 1 
ATOM   580  H HB3  . LYS   A 1 40  ? 29.711 -10.772 9.293   1   51.038  ? 52  LYS   B HB3  1 c 1 
ATOM   581  H HG2  . LYS   A 1 40  ? 29.259 -8.878  10.527  1   53.648  ? 52  LYS   B HG2  1 c 1 
ATOM   582  H HG3  . LYS   A 1 40  ? 28.251 -9.671  11.455  1   53.378  ? 52  LYS   B HG3  1 c 1 
ATOM   583  H HD2  . LYS   A 1 40  ? 29.888 -10.6   12.67   1   65.015  ? 52  LYS   B HD2  1 c 1 
ATOM   584  H HD3  . LYS   A 1 40  ? 30.961 -10.468 11.491  1   65.261  ? 52  LYS   B HD3  1 c 1 
ATOM   585  H HE2  . LYS   A 1 40  ? 30.749 -8.068  11.808  1   68.978  ? 52  LYS   B HE2  1 c 1 
ATOM   586  H HE3  . LYS   A 1 40  ? 30.034 -8.401  13.168  1   70.284  ? 52  LYS   B HE3  1 c 1 
ATOM   587  H HZ1  . LYS   A 1 40  ? 32.622 -9.06   12.589  1   78.01   ? 52  LYS   B HZ1  1 c 1 
ATOM   588  H HZ2  . LYS   A 1 40  ? 31.961 -9.352  13.878  1   78.918  ? 52  LYS   B HZ2  1 c 1 
ATOM   589  H HZ3  . LYS   A 1 40  ? 32.219 -7.954  13.48   1   78.356  ? 52  LYS   B HZ3  1 c 1 
ATOM   590  N N    . VAL   A 1 41  ? 27.29  -8.28   8.048   1   49.749  ? 53  VAL   B N    1 ? 1 
ATOM   591  C CA   . VAL   A 1 41  ? 27.345 -7.292  6.97    1   44.492  ? 53  VAL   B CA   1 ? 1 
ATOM   592  C C    . VAL   A 1 41  ? 27.929 -6.003  7.518   1   46.82   ? 53  VAL   B C    1 ? 1 
ATOM   593  O O    . VAL   A 1 41  ? 27.553 -5.59   8.614   1   46.241  ? 53  VAL   B O    1 ? 1 
ATOM   594  C CB   . VAL   A 1 41  ? 25.904 -7.082  6.472   1   41.59   ? 53  VAL   B CB   1 ? 1 
ATOM   595  C CG1  . VAL   A 1 41  ? 25.764 -5.941  5.52    1   48.578  ? 53  VAL   B CG1  1 ? 1 
ATOM   596  C CG2  . VAL   A 1 41  ? 25.367 -8.334  5.787   1   41.092  ? 53  VAL   B CG2  1 ? 1 
ATOM   597  H H    . VAL   A 1 41  ? 26.828 -8.073  8.809   1   46.076  ? 53  VAL   B H    1 c 1 
ATOM   598  H HA   . VAL   A 1 41  ? 27.901 -7.626  6.24    1   46.045  ? 53  VAL   B HA   1 c 1 
ATOM   599  H HB   . VAL   A 1 41  ? 25.344 -6.897  7.262   1   42.579  ? 53  VAL   B HB   1 c 1 
ATOM   600  H HG11 . VAL   A 1 41  ? 26.393 -6.051  4.788   1   46.611  ? 53  VAL   B HG11 1 c 1 
ATOM   601  H HG12 . VAL   A 1 41  ? 25.947 -5.105  5.981   1   46.121  ? 53  VAL   B HG12 1 c 1 
ATOM   602  H HG13 . VAL   A 1 41  ? 24.86  -5.922  5.169   1   44.45   ? 53  VAL   B HG13 1 c 1 
ATOM   603  H HG21 . VAL   A 1 41  ? 24.473 -8.162  5.447   1   39.87   ? 53  VAL   B HG21 1 c 1 
ATOM   604  H HG22 . VAL   A 1 41  ? 25.332 -9.065  6.427   1   41.815  ? 53  VAL   B HG22 1 c 1 
ATOM   605  H HG23 . VAL   A 1 41  ? 25.952 -8.578  5.051   1   41.877  ? 53  VAL   B HG23 1 c 1 
ATOM   606  N N    . TYR   A 1 42  ? 28.818 -5.355  6.745   1   45.546  ? 54  TYR   B N    1 ? 1 
ATOM   607  C CA   . TYR   A 1 42  ? 29.431 -4.114  7.162   1   43.844  ? 54  TYR   B CA   1 ? 1 
ATOM   608  C C    . TYR   A 1 42  ? 29.084 -3.033  6.138   1   42.019  ? 54  TYR   B C    1 ? 1 
ATOM   609  O O    . TYR   A 1 42  ? 29.315 -3.221  4.959   1   37.851  ? 54  TYR   B O    1 ? 1 
ATOM   610  C CB   . TYR   A 1 42  ? 30.965 -4.247  7.176   1   52.935  ? 54  TYR   B CB   1 ? 1 
ATOM   611  C CG   . TYR   A 1 42  ? 31.53  -5.369  8.026   1   55.946  ? 54  TYR   B CG   1 ? 1 
ATOM   612  C CD1  . TYR   A 1 42  ? 31.377 -6.717  7.699   1   54.129  ? 54  TYR   B CD1  1 ? 1 
ATOM   613  C CD2  . TYR   A 1 42  ? 32.226 -5.055  9.166   1   63.14   ? 54  TYR   B CD2  1 ? 1 
ATOM   614  C CE1  . TYR   A 1 42  ? 31.85  -7.726  8.523   1   61.513  ? 54  TYR   B CE1  1 ? 1 
ATOM   615  C CE2  . TYR   A 1 42  ? 32.732 -6.046  9.986   1   71.725  ? 54  TYR   B CE2  1 ? 1 
ATOM   616  C CZ   . TYR   A 1 42  ? 32.552 -7.383  9.666   1   66.179  ? 54  TYR   B CZ   1 ? 1 
ATOM   617  O OH   . TYR   A 1 42  ? 33.144 -8.221  10.558  1   62.148  ? 54  TYR   B OH   1 ? 1 
ATOM   618  H H    . TYR   A 1 42  ? 29.044 -5.704  5.931   1   45.389  ? 54  TYR   B H    1 c 1 
ATOM   619  H HA   . TYR   A 1 42  ? 29.104 -3.852  8.062   1   45.296  ? 54  TYR   B HA   1 c 1 
ATOM   620  H HB2  . TYR   A 1 42  ? 31.27  -4.376  6.25    1   51.889  ? 54  TYR   B HB2  1 c 1 
ATOM   621  H HB3  . TYR   A 1 42  ? 31.343 -3.395  7.488   1   53.247  ? 54  TYR   B HB3  1 c 1 
ATOM   622  H HD1  . TYR   A 1 42  ? 30.882 -6.95   6.93    1   54.008  ? 54  TYR   B HD1  1 c 1 
ATOM   623  H HD2  . TYR   A 1 42  ? 32.345 -4.149  9.405   1   64.096  ? 54  TYR   B HD2  1 c 1 
ATOM   624  H HE1  . TYR   A 1 42  ? 31.743 -8.63   8.282   1   60.321  ? 54  TYR   B HE1  1 c 1 
ATOM   625  H HE2  . TYR   A 1 42  ? 33.21  -5.812  10.763  1   71.118  ? 54  TYR   B HE2  1 c 1 
ATOM   626  H HH   . TYR   A 1 42  ? 32.928 -9.187  10.095  0   30      ? 54  TYR   B HH   1 c 1 
ATOM   627  N N    . VAL   A 1 43  ? 28.536 -1.878  6.586   1   40.904  ? 55  VAL   B N    1 ? 1 
ATOM   628  C CA   . VAL   A 1 43  ? 28.119 -0.885  5.619   1   40.736  ? 55  VAL   B CA   1 ? 1 
ATOM   629  C C    . VAL   A 1 43  ? 28.569 0.499   6.106   1   40.764  ? 55  VAL   B C    1 ? 1 
ATOM   630  O O    . VAL   A 1 43  ? 28.845 0.694   7.296   1   45.261  ? 55  VAL   B O    1 ? 1 
ATOM   631  C CB   . VAL   A 1 43  ? 26.61  -0.849  5.345   1   35.778  ? 55  VAL   B CB   1 ? 1 
ATOM   632  C CG1  . VAL   A 1 43  ? 25.968 -2.228  5.114   1   38.151  ? 55  VAL   B CG1  1 ? 1 
ATOM   633  C CG2  . VAL   A 1 43  ? 25.808 -0.276  6.514   1   41.008  ? 55  VAL   B CG2  1 ? 1 
ATOM   634  H H    . VAL   A 1 43  ? 28.427 -1.72   7.479   1   41.645  ? 55  VAL   B H    1 c 1 
ATOM   635  H HA   . VAL   A 1 43  ? 28.575 -1.07   4.777   1   40.502  ? 55  VAL   B HA   1 c 1 
ATOM   636  H HB   . VAL   A 1 43  ? 26.459 -0.287  4.55    1   37.702  ? 55  VAL   B HB   1 c 1 
ATOM   637  H HG11 . VAL   A 1 43  ? 26.046 -2.763  5.921   1   37.21   ? 55  VAL   B HG11 1 c 1 
ATOM   638  H HG12 . VAL   A 1 43  ? 26.422 -2.679  4.382   1   37.405  ? 55  VAL   B HG12 1 c 1 
ATOM   639  H HG13 . VAL   A 1 43  ? 25.028 -2.117  4.89    1   35.412  ? 55  VAL   B HG13 1 c 1 
ATOM   640  H HG21 . VAL   A 1 43  ? 24.863 -0.289  6.294   1   37.386  ? 55  VAL   B HG21 1 c 1 
ATOM   641  H HG22 . VAL   A 1 43  ? 26.084 0.639   6.685   1   40.249  ? 55  VAL   B HG22 1 c 1 
ATOM   642  H HG23 . VAL   A 1 43  ? 25.962 -0.814  7.309   1   39.594  ? 55  VAL   B HG23 1 c 1 
ATOM   643  N N    . HIS   A 1 44  ? 28.503 1.455   5.187   1   38.172  ? 56  HIS   B N    1 ? 1 
ATOM   644  C CA   . HIS   A 1 44  ? 28.467 2.86    5.527   1   43.46   ? 56  HIS   B CA   1 ? 1 
ATOM   645  C C    . HIS   A 1 44  ? 27.119 3.337   5.005   1   39.752  ? 56  HIS   B C    1 ? 1 
ATOM   646  O O    . HIS   A 1 44  ? 26.6   2.776   4.056   1   40.888  ? 56  HIS   B O    1 ? 1 
ATOM   647  C CB   . HIS   A 1 44  ? 29.623 3.634   4.881   1   53.519  ? 56  HIS   B CB   1 ? 1 
ATOM   648  C CG   . HIS   A 1 44  ? 30.803 3.754   5.817   1   56.861  ? 56  HIS   B CG   1 ? 1 
ATOM   649  N ND1  . HIS   A 1 44  ? 30.666 4.197   7.121   1   56.793  ? 56  HIS   B ND1  1 ? 1 
ATOM   650  C CD2  . HIS   A 1 44  ? 32.076 3.373   5.672   1   60.828  ? 56  HIS   B CD2  1 ? 1 
ATOM   651  C CE1  . HIS   A 1 44  ? 31.828 4.118   7.733   1   64.672  ? 56  HIS   B CE1  1 ? 1 
ATOM   652  N NE2  . HIS   A 1 44  ? 32.704 3.627   6.855   1   66.512  ? 56  HIS   B NE2  1 ? 1 
ATOM   653  H H    . HIS   A 1 44  ? 28.481 1.219   4.304   1   39.249  ? 56  HIS   B H    1 c 1 
ATOM   654  H HA   . HIS   A 1 44  ? 28.481 2.963   6.508   1   44.125  ? 56  HIS   B HA   1 c 1 
ATOM   655  H HB2  . HIS   A 1 44  ? 29.904 3.166   4.065   1   51.708  ? 56  HIS   B HB2  1 c 1 
ATOM   656  H HB3  . HIS   A 1 44  ? 29.311 4.533   4.638   1   52.071  ? 56  HIS   B HB3  1 c 1 
ATOM   657  H HD1  . HIS   A 1 44  ? 29.911 4.477   7.535   0   30      ? 56  HIS   B HD1  1 c 1 
ATOM   658  H HD2  . HIS   A 1 44  ? 32.474 3.018   4.902   1   61.63   ? 56  HIS   B HD2  1 c 1 
ATOM   659  H HE1  . HIS   A 1 44  ? 32.016 4.394   8.614   1   65.53   ? 56  HIS   B HE1  1 c 1 
ATOM   660  H HE2  . HIS   A 1 44  ? 33.588 3.613   7.116   0   30      ? 56  HIS   B HE2  1 c 1 
ATOM   661  N N    . TYR   A 1 45  ? 26.53  4.346   5.61    1   40.516  ? 57  TYR   B N    1 ? 1 
ATOM   662  C CA   . TYR   A 1 45  ? 25.248 4.837   5.095   1   38.85   ? 57  TYR   B CA   1 ? 1 
ATOM   663  C C    . TYR   A 1 45  ? 25.076 6.314   5.448   1   37.008  ? 57  TYR   B C    1 ? 1 
ATOM   664  O O    . TYR   A 1 45  ? 25.631 6.788   6.423   1   42.259  ? 57  TYR   B O    1 ? 1 
ATOM   665  C CB   . TYR   A 1 45  ? 24.097 4.008   5.694   1   37.484  ? 57  TYR   B CB   1 ? 1 
ATOM   666  C CG   . TYR   A 1 45  ? 23.828 4.219   7.192   1   36.683  ? 57  TYR   B CG   1 ? 1 
ATOM   667  C CD1  . TYR   A 1 45  ? 24.585 3.584   8.174   1   37.935  ? 57  TYR   B CD1  1 ? 1 
ATOM   668  C CD2  . TYR   A 1 45  ? 22.901 5.15    7.61    1   33.211  ? 57  TYR   B CD2  1 ? 1 
ATOM   669  C CE1  . TYR   A 1 45  ? 24.406 3.849   9.526   1   42.492  ? 57  TYR   B CE1  1 ? 1 
ATOM   670  C CE2  . TYR   A 1 45  ? 22.75  5.475   8.933   1   37.251  ? 57  TYR   B CE2  1 ? 1 
ATOM   671  C CZ   . TYR   A 1 45  ? 23.421 4.747   9.904   1   39.264  ? 57  TYR   B CZ   1 ? 1 
ATOM   672  O OH   . TYR   A 1 45  ? 23.141 5.093   11.155  1   47.135  ? 57  TYR   B OH   1 ? 1 
ATOM   673  H H    . TYR   A 1 45  ? 26.908 4.74    6.343   1   42.07   ? 57  TYR   B H    1 c 1 
ATOM   674  H HA   . TYR   A 1 45  ? 25.239 4.737   4.11    1   38.083  ? 57  TYR   B HA   1 c 1 
ATOM   675  H HB2  . TYR   A 1 45  ? 23.276 4.219   5.197   1   35.635  ? 57  TYR   B HB2  1 c 1 
ATOM   676  H HB3  . TYR   A 1 45  ? 24.293 3.056   5.543   1   36.106  ? 57  TYR   B HB3  1 c 1 
ATOM   677  H HD1  . TYR   A 1 45  ? 25.233 2.948   7.915   1   38.826  ? 57  TYR   B HD1  1 c 1 
ATOM   678  H HD2  . TYR   A 1 45  ? 22.42  5.639   6.962   1   34.087  ? 57  TYR   B HD2  1 c 1 
ATOM   679  H HE1  . TYR   A 1 45  ? 24.889 3.369   10.176  1   42.061  ? 57  TYR   B HE1  1 c 1 
ATOM   680  H HE2  . TYR   A 1 45  ? 22.067 6.07    9.188   1   37.032  ? 57  TYR   B HE2  1 c 1 
ATOM   681  H HH   . TYR   A 1 45  ? 23.669 4.607   11.715  0   30      ? 57  TYR   B HH   1 c 1 
ATOM   682  N N    . LYS   A 1 46  ? 24.183 6.964   4.727   1   35.411  ? 58  LYS   B N    1 ? 1 
ATOM   683  C CA   . LYS   A 1 46  ? 23.606 8.232   5.074   1   38.104  ? 58  LYS   B CA   1 ? 1 
ATOM   684  C C    . LYS   A 1 46  ? 22.115 8.029   5.008   1   35.551  ? 58  LYS   B C    1 ? 1 
ATOM   685  O O    . LYS   A 1 46  ? 21.599 7.448   4.056   1   38.741  ? 58  LYS   B O    1 ? 1 
ATOM   686  C CB   . LYS   A 1 46  ? 24.021 9.403   4.146   1   41.754  ? 58  LYS   B CB   1 ? 1 
ATOM   687  C CG   . LYS   A 1 46  ? 25.46  9.618   4.057   1   48.02   ? 58  LYS   B CG   1 ? 1 
ATOM   688  C CD   . LYS   A 1 46  ? 25.867 10.537  2.905   1   53.528  ? 58  LYS   B CD   1 ? 1 
ATOM   689  C CE   . LYS   A 1 46  ? 27.301 10.603  2.585   1   57.85   ? 58  LYS   B CE   1 ? 1 
ATOM   690  N NZ   . LYS   A 1 46  ? 27.568 11.811  1.776   1   62.15   ? 58  LYS   B NZ   1 ? 1 
ATOM   691  H H    . LYS   A 1 46  ? 23.913 6.578   3.943   1   34.845  ? 58  LYS   B H    1 c 1 
ATOM   692  H HA   . LYS   A 1 46  ? 23.859 8.451   6.006   1   39.3    ? 58  LYS   B HA   1 c 1 
ATOM   693  H HB2  . LYS   A 1 46  ? 23.675 9.226   3.246   1   41.275  ? 58  LYS   B HB2  1 c 1 
ATOM   694  H HB3  . LYS   A 1 46  ? 23.602 10.229  4.471   1   43.077  ? 58  LYS   B HB3  1 c 1 
ATOM   695  H HG2  . LYS   A 1 46  ? 25.772 10.006  4.903   1   49.392  ? 58  LYS   B HG2  1 c 1 
ATOM   696  H HG3  . LYS   A 1 46  ? 25.901 8.749   3.943   1   47.056  ? 58  LYS   B HG3  1 c 1 
ATOM   697  H HD2  . LYS   A 1 46  ? 25.393 10.237  2.103   1   51.55   ? 58  LYS   B HD2  1 c 1 
ATOM   698  H HD3  . LYS   A 1 46  ? 25.549 11.444  3.107   1   54.275  ? 58  LYS   B HD3  1 c 1 
ATOM   699  H HE2  . LYS   A 1 46  ? 27.825 10.642  3.405   1   59.111  ? 58  LYS   B HE2  1 c 1 
ATOM   700  H HE3  . LYS   A 1 46  ? 27.567 9.813   2.082   1   56.94   ? 58  LYS   B HE3  1 c 1 
ATOM   701  H HZ1  . LYS   A 1 46  ? 27.484 12.55   2.292   1   63.24   ? 58  LYS   B HZ1  1 c 1 
ATOM   702  H HZ2  . LYS   A 1 46  ? 26.981 11.859  1.087   1   60.828  ? 58  LYS   B HZ2  1 c 1 
ATOM   703  H HZ3  . LYS   A 1 46  ? 28.409 11.772  1.446   1   64.001  ? 58  LYS   B HZ3  1 c 1 
ATOM   704  N N    . GLY   A 1 47  ? 21.398 8.662   5.923   1   40.227  ? 59  GLY   B N    1 ? 1 
ATOM   705  C CA   . GLY   A 1 47  ? 19.963 8.561   5.884   1   40.747  ? 59  GLY   B CA   1 ? 1 
ATOM   706  C C    . GLY   A 1 47  ? 19.282 9.821   6.372   1   36.632  ? 59  GLY   B C    1 ? 1 
ATOM   707  O O    . GLY   A 1 47  ? 19.877 10.611  7.059   1   37.857  ? 59  GLY   B O    1 ? 1 
ATOM   708  H H    . GLY   A 1 47  ? 21.801 9.158   6.577   1   41.286  ? 59  GLY   B H    1 c 1 
ATOM   709  H HA2  . GLY   A 1 47  ? 19.679 8.376   4.961   1   37.714  ? 59  GLY   B HA2  1 c 1 
ATOM   710  H HA3  . GLY   A 1 47  ? 19.682 7.8     6.445   1   37.616  ? 59  GLY   B HA3  1 c 1 
ATOM   711  N N    . LYS   A 1 48  ? 18.039 9.976   5.937   1   35.497  ? 60  LYS   B N    1 ? 1 
ATOM   712  C CA   . LYS   A 1 48  ? 17.247 11.126  6.264   1   42.022  ? 60  LYS   B CA   1 ? 1 
ATOM   713  C C    . LYS   A 1 48  ? 15.764 10.783  6.261   1   46.078  ? 60  LYS   B C    1 ? 1 
ATOM   714  O O    . LYS   A 1 48  ? 15.353 9.762   5.706   1   40.952  ? 60  LYS   B O    1 ? 1 
ATOM   715  C CB   . LYS   A 1 48  ? 17.535 12.314  5.342   1   47.614  ? 60  LYS   B CB   1 ? 1 
ATOM   716  C CG   . LYS   A 1 48  ? 16.962 12.206  3.983   1   53.301  ? 60  LYS   B CG   1 ? 1 
ATOM   717  C CD   . LYS   A 1 48  ? 17.57  13.247  3.023   1   54.38   ? 60  LYS   B CD   1 ? 1 
ATOM   718  C CE   . LYS   A 1 48  ? 16.909 14.584  3.16    1   70.373  ? 60  LYS   B CE   1 ? 1 
ATOM   719  N NZ   . LYS   A 1 48  ? 15.79  14.814  2.224   1   73.526  ? 60  LYS   B NZ   1 ? 1 
ATOM   720  H H    . LYS   A 1 48  ? 17.669 9.327   5.41    1   35.066  ? 60  LYS   B H    1 c 1 
ATOM   721  H HA   . LYS   A 1 48  ? 17.489 11.402  7.182   1   43.756  ? 60  LYS   B HA   1 c 1 
ATOM   722  H HB2  . LYS   A 1 48  ? 17.184 13.128  5.762   1   49.812  ? 60  LYS   B HB2  1 c 1 
ATOM   723  H HB3  . LYS   A 1 48  ? 18.507 12.417  5.261   1   49.231  ? 60  LYS   B HB3  1 c 1 
ATOM   724  H HG2  . LYS   A 1 48  ? 17.132 11.304  3.636   1   49.614  ? 60  LYS   B HG2  1 c 1 
ATOM   725  H HG3  . LYS   A 1 48  ? 15.99  12.341  4.034   1   50.99   ? 60  LYS   B HG3  1 c 1 
ATOM   726  H HD2  . LYS   A 1 48  ? 18.529 13.341  3.209   1   58.457  ? 60  LYS   B HD2  1 c 1 
ATOM   727  H HD3  . LYS   A 1 48  ? 17.467 12.931  2.099   1   56.944  ? 60  LYS   B HD3  1 c 1 
ATOM   728  H HE2  . LYS   A 1 48  ? 16.577 14.685  4.07    1   67.244  ? 60  LYS   B HE2  1 c 1 
ATOM   729  H HE3  . LYS   A 1 48  ? 17.577 15.276  3.013   1   69.607  ? 60  LYS   B HE3  1 c 1 
ATOM   730  H HZ1  . LYS   A 1 48  ? 15.128 14.216  2.384   1   70.784  ? 60  LYS   B HZ1  1 c 1 
ATOM   731  H HZ2  . LYS   A 1 48  ? 16.079 14.718  1.371   1   72.604  ? 60  LYS   B HZ2  1 c 1 
ATOM   732  H HZ3  . LYS   A 1 48  ? 15.467 15.653  2.336   1   74.166  ? 60  LYS   B HZ3  1 c 1 
ATOM   733  N N    . LEU   A 1 49  ? 15.013 11.609  6.999   1   43.212  ? 61  LEU   B N    1 ? 1 
ATOM   734  C CA   . LEU   A 1 49  ? 13.571 11.588  7.053   1   44.574  ? 61  LEU   B CA   1 ? 1 
ATOM   735  C C    . LEU   A 1 49  ? 13.117 12.292  5.82    1   44.34   ? 61  LEU   B C    1 ? 1 
ATOM   736  O O    . LEU   A 1 49  ? 13.764 13.246  5.482   1   43.679  ? 61  LEU   B O    1 ? 1 
ATOM   737  C CB   . LEU   A 1 49  ? 13.009 12.303  8.283   1   44.773  ? 61  LEU   B CB   1 ? 1 
ATOM   738  C CG   . LEU   A 1 49  ? 13.342 11.696  9.636   1   47.611  ? 61  LEU   B CG   1 ? 1 
ATOM   739  C CD1  . LEU   A 1 49  ? 12.726 12.496  10.789  1   55.77   ? 61  LEU   B CD1  1 ? 1 
ATOM   740  C CD2  . LEU   A 1 49  ? 12.81  10.283  9.63    1   46.222  ? 61  LEU   B CD2  1 ? 1 
ATOM   741  H H    . LEU   A 1 49  ? 15.445 12.233  7.508   1   46.297  ? 61  LEU   B H    1 c 1 
ATOM   742  H HA   . LEU   A 1 49  ? 13.258 10.649  7.032   1   42.182  ? 61  LEU   B HA   1 c 1 
ATOM   743  H HB2  . LEU   A 1 49  ? 13.34  13.23   8.273   1   47.6    ? 61  LEU   B HB2  1 c 1 
ATOM   744  H HB3  . LEU   A 1 49  ? 12.029 12.342  8.194   1   45.8    ? 61  LEU   B HB3  1 c 1 
ATOM   745  H HG   . LEU   A 1 49  ? 14.328 11.672  9.745   1   48.462  ? 61  LEU   B HG   1 c 1 
ATOM   746  H HD11 . LEU   A 1 49  ? 13.096 13.394  10.795  1   55.933  ? 61  LEU   B HD11 1 c 1 
ATOM   747  H HD12 . LEU   A 1 49  ? 12.928 12.058  11.633  1   54.696  ? 61  LEU   B HD12 1 c 1 
ATOM   748  H HD13 . LEU   A 1 49  ? 11.762 12.544  10.673  1   54.099  ? 61  LEU   B HD13 1 c 1 
ATOM   749  H HD21 . LEU   A 1 49  ? 13.403 9.715   9.111   1   44.36   ? 61  LEU   B HD21 1 c 1 
ATOM   750  H HD22 . LEU   A 1 49  ? 11.921 10.269  9.235   1   45.496  ? 61  LEU   B HD22 1 c 1 
ATOM   751  H HD23 . LEU   A 1 49  ? 12.763 9.95    10.542  1   46.67   ? 61  LEU   B HD23 1 c 1 
ATOM   752  N N    . SER   A 1 50  ? 12.003 11.87   5.203   1   48.15   ? 62  SER   B N    1 ? 1 
ATOM   753  C CA   . SER   A 1 50  ? 11.439 12.666  4.102   1   51.489  ? 62  SER   B CA   1 ? 1 
ATOM   754  C C    . SER   A 1 50  ? 10.984 14.03   4.583   1   46.878  ? 62  SER   B C    1 ? 1 
ATOM   755  O O    . SER   A 1 50  ? 10.885 14.903  3.78    1   56.268  ? 62  SER   B O    1 ? 1 
ATOM   756  C CB   . SER   A 1 50  ? 10.272 12      3.342   1   53.202  ? 62  SER   B CB   1 ? 1 
ATOM   757  O OG   . SER   A 1 50  ? 9.342  11.394  4.214   1   66.123  ? 62  SER   B OG   1 ? 1 
ATOM   758  H H    . SER   A 1 50  ? 11.591 11.095  5.46    1   46.211  ? 62  SER   B H    1 c 1 
ATOM   759  H HA   . SER   A 1 50  ? 12.168 12.816  3.45    1   50.111  ? 62  SER   B HA   1 c 1 
ATOM   760  H HB2  . SER   A 1 50  ? 9.815  12.672  2.801   1   56.698  ? 62  SER   B HB2  1 c 1 
ATOM   761  H HB3  . SER   A 1 50  ? 10.628 11.323  2.738   1   54.313  ? 62  SER   B HB3  1 c 1 
ATOM   762  H HG   . SER   A 1 50  ? 8.687  11.167  4.029   0   30      ? 62  SER   B HG   1 c 1 
ATOM   763  N N    . ASN   A 1 51  ? 10.684 14.268  5.874   1   47.846  ? 63  ASN   B N    1 ? 1 
ATOM   764  C CA   . ASN   A 1 51  ? 10.333 15.647  6.262   1   51.188  ? 63  ASN   B CA   1 ? 1 
ATOM   765  C C    . ASN   A 1 51  ? 11.538 16.609  6.302   1   53.213  ? 63  ASN   B C    1 ? 1 
ATOM   766  O O    . ASN   A 1 51  ? 11.344 17.797  6.61    1   56.934  ? 63  ASN   B O    1 ? 1 
ATOM   767  C CB   . ASN   A 1 51  ? 9.529  15.663  7.56    1   54.924  ? 63  ASN   B CB   1 ? 1 
ATOM   768  C CG   . ASN   A 1 51  ? 10.366 15.275  8.756   1   58.649  ? 63  ASN   B CG   1 ? 1 
ATOM   769  O OD1  . ASN   A 1 51  ? 11.598 15.16   8.671   1   60.685  ? 63  ASN   B OD1  1 ? 1 
ATOM   770  N ND2  . ASN   A 1 51  ? 9.723  15.141  9.907   1   62.854  ? 63  ASN   B ND2  1 ? 1 
ATOM   771  H H    . ASN   A 1 51  ? 10.683 13.6    6.497   1   47.039  ? 63  ASN   B H    1 c 1 
ATOM   772  H HA   . ASN   A 1 51  ? 9.727  15.992  5.568   1   52.209  ? 63  ASN   B HA   1 c 1 
ATOM   773  H HB2  . ASN   A 1 51  ? 9.165  16.56   7.701   1   57.386  ? 63  ASN   B HB2  1 c 1 
ATOM   774  H HB3  . ASN   A 1 51  ? 8.779  15.041  7.48    1   54.107  ? 63  ASN   B HB3  1 c 1 
ATOM   775  H HD21 . ASN   A 1 51  ? 10.18  15.004  10.655  1   62.566  ? 63  ASN   B HD21 1 c 1 
ATOM   776  H HD22 . ASN   A 1 51  ? 8.838  15.188  9.93    1   62.436  ? 63  ASN   B HD22 1 c 1 
ATOM   777  N N    . GLY   A 1 52  ? 12.78  16.135  6.058   1   53.499  ? 64  GLY   B N    1 ? 1 
ATOM   778  C CA   . GLY   A 1 52  ? 13.98  16.966  6.105   1   62.191  ? 64  GLY   B CA   1 ? 1 
ATOM   779  C C    . GLY   A 1 52  ? 14.402 17.408  7.523   1   69.97   ? 64  GLY   B C    1 ? 1 
ATOM   780  O O    . GLY   A 1 52  ? 15.329 18.206  7.632   1   67.727  ? 64  GLY   B O    1 ? 1 
ATOM   781  H H    . GLY   A 1 52  ? 12.882 15.248  5.865   1   52.299  ? 64  GLY   B H    1 c 1 
ATOM   782  H HA2  . GLY   A 1 52  ? 14.722 16.465  5.693   1   60.462  ? 64  GLY   B HA2  1 c 1 
ATOM   783  H HA3  . GLY   A 1 52  ? 13.825 17.769  5.554   1   63.252  ? 64  GLY   B HA3  1 c 1 
ATOM   784  N N    . LYS   A 1 53  ? 13.757 16.919  8.607   1   71.121  ? 65  LYS   B N    1 ? 1 
ATOM   785  C CA   . LYS   A 1 53  ? 14.078 17.402  9.95    1   73.194  ? 65  LYS   B CA   1 ? 1 
ATOM   786  C C    . LYS   A 1 53  ? 15.214 16.559  10.58   1   70.528  ? 65  LYS   B C    1 ? 1 
ATOM   787  O O    . LYS   A 1 53  ? 15.799 16.996  11.552  1   77.928  ? 65  LYS   B O    1 ? 1 
ATOM   788  C CB   . LYS   A 1 53  ? 12.822 17.636  10.813  1   68.669  ? 65  LYS   B CB   1 ? 1 
ATOM   789  H H    . LYS   A 1 53  ? 13.123 16.268  8.509   1   68.359  ? 65  LYS   B H    1 c 1 
ATOM   790  H HA   . LYS   A 1 53  ? 14.451 18.313  9.839   1   74.21   ? 65  LYS   B HA   1 c 1 
ATOM   791  H HB2  . LYS   A 1 53  ? 13.185 17.821  11.7    0   30      ? 65  LYS   B HB2  1 c 1 
ATOM   792  H HB3  . LYS   A 1 53  ? 12.12  17.515  10.208  0   30      ? 65  LYS   B HB3  1 c 1 
ATOM   793  N N    . LYS   A 1 54  ? 15.649 15.418  10.033  1   63.394  ? 66  LYS   B N    1 ? 1 
ATOM   794  C CA   . LYS   A 1 54  ? 16.701 14.635  10.7    1   59.06   ? 66  LYS   B CA   1 ? 1 
ATOM   795  C C    . LYS   A 1 54  ? 17.552 13.855  9.692   1   57.963  ? 66  LYS   B C    1 ? 1 
ATOM   796  O O    . LYS   A 1 54  ? 17.004 13.234  8.767   1   54.621  ? 66  LYS   B O    1 ? 1 
ATOM   797  C CB   . LYS   A 1 54  ? 16.089 13.729  11.776  1   55.451  ? 66  LYS   B CB   1 ? 1 
ATOM   798  H H    . LYS   A 1 54  ? 15.297 15.118  9.244   1   61.339  ? 66  LYS   B H    1 c 1 
ATOM   799  H HA   . LYS   A 1 54  ? 17.3   15.272  11.166  1   62.308  ? 66  LYS   B HA   1 c 1 
ATOM   800  H HB2  . LYS   A 1 54  ? 16.86  13.357  12.256  0   30      ? 66  LYS   B HB2  1 c 1 
ATOM   801  H HB3  . LYS   A 1 54  ? 15.149 13.822  11.699  0   30      ? 66  LYS   B HB3  1 c 1 
ATOM   802  N N    . PHE   A 1 55  ? 18.881 13.915  9.889   1   54.555  ? 67  PHE   B N    1 ? 1 
ATOM   803  C CA   . PHE   A 1 55  ? 19.91  13.247  9.094   1   55.829  ? 67  PHE   B CA   1 ? 1 
ATOM   804  C C    . PHE   A 1 55  ? 20.868 12.434  9.969   1   59.894  ? 67  PHE   B C    1 ? 1 
ATOM   805  O O    . PHE   A 1 55  ? 21.203 12.85   11.066  1   62.117  ? 67  PHE   B O    1 ? 1 
ATOM   806  C CB   . PHE   A 1 55  ? 20.796 14.266  8.375   1   62.29   ? 67  PHE   B CB   1 ? 1 
ATOM   807  C CG   . PHE   A 1 55  ? 19.974 15.28   7.599   1   74.337  ? 67  PHE   B CG   1 ? 1 
ATOM   808  C CD1  . PHE   A 1 55  ? 19.308 16.332  8.247   1   82.89   ? 67  PHE   B CD1  1 ? 1 
ATOM   809  C CD2  . PHE   A 1 55  ? 19.886 15.204  6.207   1   81.081  ? 67  PHE   B CD2  1 ? 1 
ATOM   810  C CE1  . PHE   A 1 55  ? 18.547 17.251  7.518   1   84.583  ? 67  PHE   B CE1  1 ? 1 
ATOM   811  C CE2  . PHE   A 1 55  ? 19.128 16.136  5.484   1   81.539  ? 67  PHE   B CE2  1 ? 1 
ATOM   812  C CZ   . PHE   A 1 55  ? 18.453 17.144  6.139   1   81.859  ? 67  PHE   B CZ   1 ? 1 
ATOM   813  H H    . PHE   A 1 55  ? 19.17  14.423  10.592  1   58.843  ? 67  PHE   B H    1 c 1 
ATOM   814  H HA   . PHE   A 1 55  ? 19.479 12.652  8.427   1   53.912  ? 67  PHE   B HA   1 c 1 
ATOM   815  H HB2  . PHE   A 1 55  ? 21.346 14.737  9.04    1   66.397  ? 67  PHE   B HB2  1 c 1 
ATOM   816  H HB3  . PHE   A 1 55  ? 21.392 13.789  7.756   1   62.932  ? 67  PHE   B HB3  1 c 1 
ATOM   817  H HD1  . PHE   A 1 55  ? 19.352 16.403  9.187   1   82.664  ? 67  PHE   B HD1  1 c 1 
ATOM   818  H HD2  . PHE   A 1 55  ? 20.329 14.507  5.751   1   77.313  ? 67  PHE   B HD2  1 c 1 
ATOM   819  H HE1  . PHE   A 1 55  ? 18.096 17.947  7.968   1   85.843  ? 67  PHE   B HE1  1 c 1 
ATOM   820  H HE2  . PHE   A 1 55  ? 19.068 16.063  4.545   1   80.414  ? 67  PHE   B HE2  1 c 1 
ATOM   821  H HZ   . PHE   A 1 55  ? 17.954 17.778  5.648   1   83.421  ? 67  PHE   B HZ   1 c 1 
ATOM   822  N N    . ASP   A 1 56  ? 21.392 11.308  9.466   1   53.152  ? 68  ASP   B N    1 ? 1 
ATOM   823  C CA   . ASP   A 1 56  ? 22.171 10.373  10.266  1   56.76   ? 68  ASP   B CA   1 ? 1 
ATOM   824  C C    . ASP   A 1 56  ? 23.161 9.72    9.317   1   57.642  ? 68  ASP   B C    1 ? 1 
ATOM   825  O O    . ASP   A 1 56  ? 22.741 9.267   8.273   1   55.57   ? 68  ASP   B O    1 ? 1 
ATOM   826  C CB   . ASP   A 1 56  ? 21.309 9.277   10.891  1   56.323  ? 68  ASP   B CB   1 ? 1 
ATOM   827  C CG   . ASP   A 1 56  ? 22.069 8.103   11.534  1   59.833  ? 68  ASP   B CG   1 ? 1 
ATOM   828  O OD1  . ASP   A 1 56  ? 23.061 8.372   12.226  1   64.215  ? 68  ASP   B OD1  1 ? 1 
ATOM   829  O OD2  . ASP   A 1 56  ? 21.67  6.908   11.386  1   49.318  ? 68  ASP   B OD2  1 ? 1 
ATOM   830  H H    . ASP   A 1 56  ? 21.254 11.116  8.583   1   53.282  ? 68  ASP   B H    1 c 1 
ATOM   831  H HA   . ASP   A 1 56  ? 22.658 10.868  10.962  1   59.558  ? 68  ASP   B HA   1 c 1 
ATOM   832  H HB2  . ASP   A 1 56  ? 20.748 9.688   11.582  1   57.593  ? 68  ASP   B HB2  1 c 1 
ATOM   833  H HB3  . ASP   A 1 56  ? 20.717 8.914   10.2    1   54.151  ? 68  ASP   B HB3  1 c 1 
ATOM   834  N N    . SER   A 1 57  ? 24.438 9.663   9.678   1   62.83   ? 69  SER   B N    1 ? 1 
ATOM   835  C CA   . SER   A 1 57  ? 25.432 8.974   8.874   1   64.306  ? 69  SER   B CA   1 ? 1 
ATOM   836  C C    . SER   A 1 57  ? 26.345 8.165   9.784   1   67.01   ? 69  SER   B C    1 ? 1 
ATOM   837  O O    . SER   A 1 57  ? 26.793 8.726   10.796  1   70.249  ? 69  SER   B O    1 ? 1 
ATOM   838  C CB   . SER   A 1 57  ? 26.245 9.996   8.128   1   73.369  ? 69  SER   B CB   1 ? 1 
ATOM   839  O OG   . SER   A 1 57  ? 27.356 9.384   7.491   1   82.501  ? 69  SER   B OG   1 ? 1 
ATOM   840  H H    . SER   A 1 57  ? 24.704 10.07   10.452  1   64.908  ? 69  SER   B H    1 c 1 
ATOM   841  H HA   . SER   A 1 57  ? 24.981 8.371   8.233   1   62.334  ? 69  SER   B HA   1 c 1 
ATOM   842  H HB2  . SER   A 1 57  ? 25.683 10.429  7.458   1   72.746  ? 69  SER   B HB2  1 c 1 
ATOM   843  H HB3  . SER   A 1 57  ? 26.56  10.677  8.751   1   76.443  ? 69  SER   B HB3  1 c 1 
ATOM   844  H HG   . SER   A 1 57  ? 27.76  9.802   6.952   0   30      ? 69  SER   B HG   1 c 1 
ATOM   845  N N    . SER   A 1 58  ? 26.678 6.938   9.349   1   61.246  ? 70  SER   B N    1 ? 1 
ATOM   846  C CA   . SER   A 1 58  ? 27.703 6.116   9.988   1   63.301  ? 70  SER   B CA   1 ? 1 
ATOM   847  C C    . SER   A 1 58  ? 29.037 6.835   10.135  1   69.695  ? 70  SER   B C    1 ? 1 
ATOM   848  O O    . SER   A 1 58  ? 29.817 6.5     11.039  1   71.809  ? 70  SER   B O    1 ? 1 
ATOM   849  C CB   . SER   A 1 58  ? 27.989 4.801   9.287   1   50.256  ? 70  SER   B CB   1 ? 1 
ATOM   850  O OG   . SER   A 1 58  ? 28.217 4.95    7.892   1   46.194  ? 70  SER   B OG   1 ? 1 
ATOM   851  H H    . SER   A 1 58  ? 26.245 6.599   8.62    1   59.86   ? 70  SER   B H    1 c 1 
ATOM   852  H HA   . SER   A 1 58  ? 27.381 5.904   10.901  1   61.439  ? 70  SER   B HA   1 c 1 
ATOM   853  H HB2  . SER   A 1 58  ? 28.772 4.386   9.696   1   53.331  ? 70  SER   B HB2  1 c 1 
ATOM   854  H HB3  . SER   A 1 58  ? 27.232 4.2     9.423   1   49.196  ? 70  SER   B HB3  1 c 1 
ATOM   855  H HG   . SER   A 1 58  ? 28.311 4.16    7.615   0   30      ? 70  SER   B HG   1 c 1 
ATOM   856  N N    . HIS   A 1 59  ? 29.345 7.73    9.198   1   75.315  ? 71  HIS   B N    1 ? 1 
ATOM   857  C CA   . HIS   A 1 59  ? 30.622 8.431   9.264   1   89.934  ? 71  HIS   B CA   1 ? 1 
ATOM   858  C C    . HIS   A 1 59  ? 30.716 9.371   10.477  1   102.365 ? 71  HIS   B C    1 ? 1 
ATOM   859  O O    . HIS   A 1 59  ? 31.821 9.691   10.919  1   103.77  ? 71  HIS   B O    1 ? 1 
ATOM   860  C CB   . HIS   A 1 59  ? 30.905 9.152   7.948   1   91.951  ? 71  HIS   B CB   1 ? 1 
ATOM   861  C CG   . HIS   A 1 59  ? 30.946 8.243   6.773   1   91.301  ? 71  HIS   B CG   1 ? 1 
ATOM   862  N ND1  . HIS   A 1 59  ? 32.05  7.492   6.413   1   103.376 ? 71  HIS   B ND1  1 ? 1 
ATOM   863  C CD2  . HIS   A 1 59  ? 29.997 7.977   5.867   1   86.605  ? 71  HIS   B CD2  1 ? 1 
ATOM   864  C CE1  . HIS   A 1 59  ? 31.764 6.805   5.309   1   95.465  ? 71  HIS   B CE1  1 ? 1 
ATOM   865  N NE2  . HIS   A 1 59  ? 30.53  7.104   4.951   1   91.947  ? 71  HIS   B NE2  1 ? 1 
ATOM   866  H H    . HIS   A 1 59  ? 28.772 7.902   8.508   1   74.207  ? 71  HIS   B H    1 c 1 
ATOM   867  H HA   . HIS   A 1 59  ? 31.321 7.738   9.368   1   90.107  ? 71  HIS   B HA   1 c 1 
ATOM   868  H HB2  . HIS   A 1 59  ? 30.209 9.829   7.803   1   91.44   ? 71  HIS   B HB2  1 c 1 
ATOM   869  H HB3  . HIS   A 1 59  ? 31.767 9.616   8.022   1   95.778  ? 71  HIS   B HB3  1 c 1 
ATOM   870  H HD1  . HIS   A 1 59  ? 32.757 7.451   6.849   0   30      ? 71  HIS   B HD1  1 c 1 
ATOM   871  H HD2  . HIS   A 1 59  ? 29.138 8.348   5.831   1   86.554  ? 71  HIS   B HD2  1 c 1 
ATOM   872  H HE1  . HIS   A 1 59  ? 32.345 6.216   4.858   1   97.01   ? 71  HIS   B HE1  1 c 1 
ATOM   873  H HE2  . HIS   A 1 59  ? 30.118 6.819   4.178   0   30      ? 71  HIS   B HE2  1 c 1 
ATOM   874  N N    . ASP   A 1 60  ? 29.572 9.818   11.02   1   103.678 ? 72  ASP   B N    1 ? 1 
ATOM   875  C CA   . ASP   A 1 60  ? 29.559 10.481  12.316  1   109.717 ? 72  ASP   B CA   1 ? 1 
ATOM   876  C C    . ASP   A 1 60  ? 30.323 9.605   13.303  1   111.22  ? 72  ASP   B C    1 ? 1 
ATOM   877  O O    . ASP   A 1 60  ? 31.356 10.024  13.808  1   129.191 ? 72  ASP   B O    1 ? 1 
ATOM   878  C CB   . ASP   A 1 60  ? 28.149 10.819  12.781  1   102.026 ? 72  ASP   B CB   1 ? 1 
ATOM   879  C CG   . ASP   A 1 60  ? 27.385 11.746  11.838  1   102.862 ? 72  ASP   B CG   1 ? 1 
ATOM   880  O OD1  . ASP   A 1 60  ? 28.1   12.509  11.113  1   92.549  ? 72  ASP   B OD1  1 ? 1 
ATOM   881  O OD2  . ASP   A 1 60  ? 26.09  11.662  11.785  1   84.66   ? 72  ASP   B OD2  1 ? 1 
ATOM   882  H H    . ASP   A 1 60  ? 28.784 9.713   10.568  1   100.073 ? 72  ASP   B H    1 c 1 
ATOM   883  H HA   . ASP   A 1 60  ? 30.046 11.332  12.225  1   111.2   ? 72  ASP   B HA   1 c 1 
ATOM   884  H HB2  . ASP   A 1 60  ? 27.638 9.989   12.885  1   100.785 ? 72  ASP   B HB2  1 c 1 
ATOM   885  H HB3  . ASP   A 1 60  ? 28.202 11.252  13.658  1   106.697 ? 72  ASP   B HB3  1 c 1 
ATOM   886  N N    . ARG   A 1 61  ? 29.862 8.36    13.502  1   107.162 ? 73  ARG   B N    1 ? 1 
ATOM   887  C CA   . ARG   A 1 61  ? 30.513 7.426   14.422  1   102.448 ? 73  ARG   B CA   1 ? 1 
ATOM   888  C C    . ARG   A 1 61  ? 31.952 7.09    13.974  1   102.662 ? 73  ARG   B C    1 ? 1 
ATOM   889  O O    . ARG   A 1 61  ? 32.636 6.333   14.661  1   109.972 ? 73  ARG   B O    1 ? 1 
ATOM   890  C CB   . ARG   A 1 61  ? 29.606 6.191   14.618  1   79.881  ? 73  ARG   B CB   1 ? 1 
ATOM   891  H H    . ARG   A 1 61  ? 29.117 8.085   13.048  1   102.104 ? 73  ARG   B H    1 c 1 
ATOM   892  H HA   . ARG   A 1 61  ? 30.576 7.875   15.303  1   102.314 ? 73  ARG   B HA   1 c 1 
ATOM   893  H HB2  . ARG   A 1 61  ? 30.238 5.444   14.68   0   30      ? 73  ARG   B HB2  1 c 1 
ATOM   894  H HB3  . ARG   A 1 61  ? 28.748 6.541   14.506  0   30      ? 73  ARG   B HB3  1 c 1 
ATOM   895  N N    . ASN   A 1 62  ? 32.444 7.665   12.854  1   99.213  ? 74  ASN   B N    1 ? 1 
ATOM   896  C CA   . ASN   A 1 62  ? 33.685 7.267   12.193  1   98.212  ? 74  ASN   B CA   1 ? 1 
ATOM   897  C C    . ASN   A 1 62  ? 33.831 5.739   12.246  1   92.632  ? 74  ASN   B C    1 ? 1 
ATOM   898  O O    . ASN   A 1 62  ? 34.769 5.235   12.863  1   91.073  ? 74  ASN   B O    1 ? 1 
ATOM   899  C CB   . ASN   A 1 62  ? 34.891 8.059   12.731  1   93.211  ? 74  ASN   B CB   1 ? 1 
ATOM   900  H H    . ASN   A 1 62  ? 31.972 8.35    12.479  1   98.841  ? 74  ASN   B H    1 c 1 
ATOM   901  H HA   . ASN   A 1 62  ? 33.595 7.511   11.244  1   94.22   ? 74  ASN   B HA   1 c 1 
ATOM   902  H HB2  . ASN   A 1 62  ? 35.665 7.629   12.326  0   30      ? 74  ASN   B HB2  1 c 1 
ATOM   903  H HB3  . ASN   A 1 62  ? 34.455 8.794   13.094  0   30      ? 74  ASN   B HB3  1 c 1 
ATOM   904  N N    . GLU   A 1 63  ? 32.874 4.961   11.698  1   84.497  ? 75  GLU   B N    1 ? 1 
ATOM   905  C CA   . GLU   A 1 63  ? 33.133 3.524   11.578  1   76.821  ? 75  GLU   B CA   1 ? 1 
ATOM   906  C C    . GLU   A 1 63  ? 31.931 2.832   10.987  1   68.273  ? 75  GLU   B C    1 ? 1 
ATOM   907  O O    . GLU   A 1 63  ? 30.79  3.298   11.14   1   65.804  ? 75  GLU   B O    1 ? 1 
ATOM   908  C CB   . GLU   A 1 63  ? 33.454 2.703   12.84   1   79.692  ? 75  GLU   B CB   1 ? 1 
ATOM   909  C CG   . GLU   A 1 63  ? 32.316 2.667   13.866  1   79.155  ? 75  GLU   B CG   1 ? 1 
ATOM   910  C CD   . GLU   A 1 63  ? 32.857 3.019   15.247  1   90.236  ? 75  GLU   B CD   1 ? 1 
ATOM   911  O OE1  . GLU   A 1 63  ? 33.916 2.442   15.589  1   91.875  ? 75  GLU   B OE1  1 ? 1 
ATOM   912  O OE2  . GLU   A 1 63  ? 32.272 3.877   15.961  1   89.211  ? 75  GLU   B OE2  1 ? 1 
ATOM   913  H H    . GLU   A 1 63  ? 32.081 5.313   11.41   1   81.309  ? 75  GLU   B H    1 c 1 
ATOM   914  H HA   . GLU   A 1 63  ? 33.892 3.417   10.955  1   78.564  ? 75  GLU   B HA   1 c 1 
ATOM   915  H HB2  . GLU   A 1 63  ? 33.653 1.782   12.582  1   78.555  ? 75  GLU   B HB2  1 c 1 
ATOM   916  H HB3  . GLU   A 1 63  ? 34.259 3.069   13.258  1   83.681  ? 75  GLU   B HB3  1 c 1 
ATOM   917  H HG2  . GLU   A 1 63  ? 31.622 3.314   13.619  1   78.48   ? 75  GLU   B HG2  1 c 1 
ATOM   918  H HG3  . GLU   A 1 63  ? 31.919 1.77    13.892  1   78.033  ? 75  GLU   B HG3  1 c 1 
ATOM   919  N N    . PRO   A 1 64  ? 32.188 1.701   10.289  1   63.081  ? 76  PRO   B N    1 ? 1 
ATOM   920  C CA   . PRO   A 1 64  ? 31.141 0.987   9.59    1   54.718  ? 76  PRO   B CA   1 ? 1 
ATOM   921  C C    . PRO   A 1 64  ? 30.05  0.568   10.549  1   50.952  ? 76  PRO   B C    1 ? 1 
ATOM   922  O O    . PRO   A 1 64  ? 30.315 0.371   11.733  1   61.663  ? 76  PRO   B O    1 ? 1 
ATOM   923  C CB   . PRO   A 1 64  ? 31.829 -0.268  9.07    1   54.932  ? 76  PRO   B CB   1 ? 1 
ATOM   924  C CG   . PRO   A 1 64  ? 33.283 0.158   8.971   1   62.253  ? 76  PRO   B CG   1 ? 1 
ATOM   925  C CD   . PRO   A 1 64  ? 33.492 1.03    10.159  1   67.844  ? 76  PRO   B CD   1 ? 1 
ATOM   926  H HA   . PRO   A 1 64  ? 30.779 1.532   8.86    1   53.82   ? 76  PRO   B HA   1 c 1 
ATOM   927  H HB2  . PRO   A 1 64  ? 31.724 -1.013  9.694   1   55.421  ? 76  PRO   B HB2  1 c 1 
ATOM   928  H HB3  . PRO   A 1 64  ? 31.477 -0.526  8.197   1   53.594  ? 76  PRO   B HB3  1 c 1 
ATOM   929  H HG2  . PRO   A 1 64  ? 33.879 -0.617  9.001   1   63.336  ? 76  PRO   B HG2  1 c 1 
ATOM   930  H HG3  . PRO   A 1 64  ? 33.447 0.654   8.144   1   62.279  ? 76  PRO   B HG3  1 c 1 
ATOM   931  H HD2  . PRO   A 1 64  ? 33.697 0.503   10.954  1   68.071  ? 76  PRO   B HD2  1 c 1 
ATOM   932  H HD3  . PRO   A 1 64  ? 34.208 1.674   10.001  1   69.621  ? 76  PRO   B HD3  1 c 1 
ATOM   933  N N    . PHE   A 1 65  ? 28.835 0.519   10.028  1   50.071  ? 77  PHE   B N    1 ? 1 
ATOM   934  C CA   . PHE   A 1 65  ? 27.709 -0.084  10.698  1   48.011  ? 77  PHE   B CA   1 ? 1 
ATOM   935  C C    . PHE   A 1 65  ? 27.656 -1.564  10.341  1   40.723  ? 77  PHE   B C    1 ? 1 
ATOM   936  O O    . PHE   A 1 65  ? 27.684 -1.941  9.211   1   40.505  ? 77  PHE   B O    1 ? 1 
ATOM   937  C CB   . PHE   A 1 65  ? 26.48  0.701   10.268  1   44.632  ? 77  PHE   B CB   1 ? 1 
ATOM   938  C CG   . PHE   A 1 65  ? 25.21  0.223   10.936  1   44.567  ? 77  PHE   B CG   1 ? 1 
ATOM   939  C CD1  . PHE   A 1 65  ? 24.86  0.696   12.206  1   51.419  ? 77  PHE   B CD1  1 ? 1 
ATOM   940  C CD2  . PHE   A 1 65  ? 24.334 -0.657  10.298  1   40.748  ? 77  PHE   B CD2  1 ? 1 
ATOM   941  C CE1  . PHE   A 1 65  ? 23.678 0.308   12.828  1   46.303  ? 77  PHE   B CE1  1 ? 1 
ATOM   942  C CE2  . PHE   A 1 65  ? 23.209 -1.114  10.98   1   43.835  ? 77  PHE   B CE2  1 ? 1 
ATOM   943  C CZ   . PHE   A 1 65  ? 22.876 -0.641  12.218  1   46.391  ? 77  PHE   B CZ   1 ? 1 
ATOM   944  H H    . PHE   A 1 65  ? 28.701 0.882   9.2     1   48.364  ? 77  PHE   B H    1 c 1 
ATOM   945  H HA   . PHE   A 1 65  ? 27.826 0.014   11.68   1   48.504  ? 77  PHE   B HA   1 c 1 
ATOM   946  H HB2  . PHE   A 1 65  ? 26.619 1.649   10.484  1   46.54   ? 77  PHE   B HB2  1 c 1 
ATOM   947  H HB3  . PHE   A 1 65  ? 26.379 0.619   9.293   1   43.733  ? 77  PHE   B HB3  1 c 1 
ATOM   948  H HD1  . PHE   A 1 65  ? 25.42  1.326   12.63   1   51.29   ? 77  PHE   B HD1  1 c 1 
ATOM   949  H HD2  . PHE   A 1 65  ? 24.565 -1.028  9.461   1   41.017  ? 77  PHE   B HD2  1 c 1 
ATOM   950  H HE1  . PHE   A 1 65  ? 23.475 0.616   13.697  1   49.435  ? 77  PHE   B HE1  1 c 1 
ATOM   951  H HE2  . PHE   A 1 65  ? 22.627 -1.72   10.549  1   41.544  ? 77  PHE   B HE2  1 c 1 
ATOM   952  H HZ   . PHE   A 1 65  ? 22.076 -0.921  12.632  1   45.209  ? 77  PHE   B HZ   1 c 1 
ATOM   953  N N    . VAL   A 1 66  ? 27.542 -2.403  11.354  1   45.205  ? 78  VAL   B N    1 ? 1 
ATOM   954  C CA   . VAL   A 1 66  ? 27.764 -3.833  11.317  1   44.761  ? 78  VAL   B CA   1 ? 1 
ATOM   955  C C    . VAL   A 1 66  ? 26.492 -4.417  11.903  1   44.956  ? 78  VAL   B C    1 ? 1 
ATOM   956  O O    . VAL   A 1 66  ? 25.951 -3.888  12.887  1   46.296  ? 78  VAL   B O    1 ? 1 
ATOM   957  C CB   . VAL   A 1 66  ? 28.969 -4.322  12.132  1   50.115  ? 78  VAL   B CB   1 ? 1 
ATOM   958  C CG1  . VAL   A 1 66  ? 29.362 -5.735  11.742  1   51.302  ? 78  VAL   B CG1  1 ? 1 
ATOM   959  C CG2  . VAL   A 1 66  ? 30.183 -3.39   12.027  1   54.758  ? 78  VAL   B CG2  1 ? 1 
ATOM   960  H H    . VAL   A 1 66  ? 27.297 -2.044  12.158  1   45.238  ? 78  VAL   B H    1 c 1 
ATOM   961  H HA   . VAL   A 1 66  ? 27.86  -4.12   10.392  1   44.291  ? 78  VAL   B HA   1 c 1 
ATOM   962  H HB   . VAL   A 1 66  ? 28.691 -4.34   13.079  1   51.441  ? 78  VAL   B HB   1 c 1 
ATOM   963  H HG11 . VAL   A 1 66  ? 29.539 -5.772  10.787  1   49.93   ? 78  VAL   B HG11 1 c 1 
ATOM   964  H HG12 . VAL   A 1 66  ? 28.64  -6.347  11.961  1   49.923  ? 78  VAL   B HG12 1 c 1 
ATOM   965  H HG13 . VAL   A 1 66  ? 30.162 -5.992  12.229  1   53.656  ? 78  VAL   B HG13 1 c 1 
ATOM   966  H HG21 . VAL   A 1 66  ? 30.93  -3.774  12.516  1   56.677  ? 78  VAL   B HG21 1 c 1 
ATOM   967  H HG22 . VAL   A 1 66  ? 29.962 -2.523  12.405  1   54.661  ? 78  VAL   B HG22 1 c 1 
ATOM   968  H HG23 . VAL   A 1 66  ? 30.429 -3.283  11.093  1   53.316  ? 78  VAL   B HG23 1 c 1 
ATOM   969  N N    . PHE   A 1 67  ? 25.98  -5.457  11.233  1   45.45   ? 79  PHE   B N    1 ? 1 
ATOM   970  C CA   . PHE   A 1 67  ? 24.718 -6.059  11.607  1   41.529  ? 79  PHE   B CA   1 ? 1 
ATOM   971  C C    . PHE   A 1 67  ? 24.557 -7.386  10.882  1   43.256  ? 79  PHE   B C    1 ? 1 
ATOM   972  O O    . PHE   A 1 67  ? 25.287 -7.662  9.967   1   39.201  ? 79  PHE   B O    1 ? 1 
ATOM   973  C CB   . PHE   A 1 67  ? 23.463 -5.224  11.397  1   39.334  ? 79  PHE   B CB   1 ? 1 
ATOM   974  C CG   . PHE   A 1 67  ? 23.005 -5.084  9.95    1   36.828  ? 79  PHE   B CG   1 ? 1 
ATOM   975  C CD1  . PHE   A 1 67  ? 23.644 -4.216  9.091   1   35.422  ? 79  PHE   B CD1  1 ? 1 
ATOM   976  C CD2  . PHE   A 1 67  ? 21.928 -5.812  9.478   1   32.757  ? 79  PHE   B CD2  1 ? 1 
ATOM   977  C CE1  . PHE   A 1 67  ? 23.255 -4.105  7.771   1   35.784  ? 79  PHE   B CE1  1 ? 1 
ATOM   978  C CE2  . PHE   A 1 67  ? 21.531 -5.689  8.166   1   30.926  ? 79  PHE   B CE2  1 ? 1 
ATOM   979  C CZ   . PHE   A 1 67  ? 22.236 -4.924  7.298   1   33.797  ? 79  PHE   B CZ   1 ? 1 
ATOM   980  H H    . PHE   A 1 67  ? 26.437 -5.8    10.519  1   43.947  ? 79  PHE   B H    1 c 1 
ATOM   981  H HA   . PHE   A 1 67  ? 24.773 -6.261  12.579  1   44.197  ? 79  PHE   B HA   1 c 1 
ATOM   982  H HB2  . PHE   A 1 67  ? 22.734 -5.626  11.919  1   39.509  ? 79  PHE   B HB2  1 c 1 
ATOM   983  H HB3  . PHE   A 1 67  ? 23.623 -4.326  11.764  1   40.055  ? 79  PHE   B HB3  1 c 1 
ATOM   984  H HD1  . PHE   A 1 67  ? 24.389 -3.724  9.4     1   37.396  ? 79  PHE   B HD1  1 c 1 
ATOM   985  H HD2  . PHE   A 1 67  ? 21.479 -6.411  10.053  1   33.895  ? 79  PHE   B HD2  1 c 1 
ATOM   986  H HE1  . PHE   A 1 67  ? 23.725 -3.537  7.181   1   35.217  ? 79  PHE   B HE1  1 c 1 
ATOM   987  H HE2  . PHE   A 1 67  ? 20.82  -6.221  7.845   1   31.15   ? 79  PHE   B HE2  1 c 1 
ATOM   988  H HZ   . PHE   A 1 67  ? 21.919 -4.81   6.416   1   32.315  ? 79  PHE   B HZ   1 c 1 
ATOM   989  N N    . SER   A 1 68  ? 23.697 -8.238  11.433  1   38.692  ? 80  SER   B N    1 ? 1 
ATOM   990  C CA   . SER   A 1 68  ? 23.531 -9.608  10.963  1   44.995  ? 80  SER   B CA   1 ? 1 
ATOM   991  C C    . SER   A 1 68  ? 22.235 -9.597  10.143  1   39.046  ? 80  SER   B C    1 ? 1 
ATOM   992  O O    . SER   A 1 68  ? 21.184 -9.151  10.602  1   39.962  ? 80  SER   B O    1 ? 1 
ATOM   993  C CB   . SER   A 1 68  ? 23.454 -10.603 12.101  1   44.401  ? 80  SER   B CB   1 ? 1 
ATOM   994  O OG   . SER   A 1 68  ? 24.749 -10.858 12.589  1   61.035  ? 80  SER   B OG   1 ? 1 
ATOM   995  H H    . SER   A 1 68  ? 23.187 -7.956  12.138  1   41.576  ? 80  SER   B H    1 c 1 
ATOM   996  H HA   . SER   A 1 68  ? 24.29  -9.844  10.374  1   42.555  ? 80  SER   B HA   1 c 1 
ATOM   997  H HB2  . SER   A 1 68  ? 22.898 -10.24  12.817  1   48.335  ? 80  SER   B HB2  1 c 1 
ATOM   998  H HB3  . SER   A 1 68  ? 23.052 -11.434 11.783  1   47.898  ? 80  SER   B HB3  1 c 1 
ATOM   999  H HG   . SER   A 1 68  ? 24.709 -11.338 13.256  0   30      ? 80  SER   B HG   1 c 1 
ATOM   1000 N N    . LEU   A 1 69  ? 22.386 -9.946  8.867   1   35.447  ? 81  LEU   B N    1 ? 1 
ATOM   1001 C CA   . LEU   A 1 69  ? 21.301 -9.776  7.928   1   32.865  ? 81  LEU   B CA   1 ? 1 
ATOM   1002 C C    . LEU   A 1 69  ? 20.184 -10.768 8.209   1   32.22   ? 81  LEU   B C    1 ? 1 
ATOM   1003 O O    . LEU   A 1 69  ? 20.4   -11.961 8.443   1   29.709  ? 81  LEU   B O    1 ? 1 
ATOM   1004 C CB   . LEU   A 1 69  ? 21.82  -10.016 6.529   1   35.503  ? 81  LEU   B CB   1 ? 1 
ATOM   1005 C CG   . LEU   A 1 69  ? 20.885 -9.669  5.376   1   39.725  ? 81  LEU   B CG   1 ? 1 
ATOM   1006 C CD1  . LEU   A 1 69  ? 20.672 -8.24   5.187   1   37.156  ? 81  LEU   B CD1  1 ? 1 
ATOM   1007 C CD2  . LEU   A 1 69  ? 21.567 -10.249 4.119   1   47.073  ? 81  LEU   B CD2  1 ? 1 
ATOM   1008 H H    . LEU   A 1 69  ? 23.176 -10.301 8.577   1   36.634  ? 81  LEU   B H    1 c 1 
ATOM   1009 H HA   . LEU   A 1 69  ? 20.956 -8.85   8.001   1   32.466  ? 81  LEU   B HA   1 c 1 
ATOM   1010 H HB2  . LEU   A 1 69  ? 22.65  -9.496  6.42    1   36.012  ? 81  LEU   B HB2  1 c 1 
ATOM   1011 H HB3  . LEU   A 1 69  ? 22.065 -10.968 6.456   1   37.056  ? 81  LEU   B HB3  1 c 1 
ATOM   1012 H HG   . LEU   A 1 69  ? 20.013 -10.121 5.514   1   39.451  ? 81  LEU   B HG   1 c 1 
ATOM   1013 H HD11 . LEU   A 1 69  ? 20.265 -7.863  5.985   1   37.214  ? 81  LEU   B HD11 1 c 1 
ATOM   1014 H HD12 . LEU   A 1 69  ? 20.084 -8.097  4.427   1   37.017  ? 81  LEU   B HD12 1 c 1 
ATOM   1015 H HD13 . LEU   A 1 69  ? 21.525 -7.803  5.023   1   37.705  ? 81  LEU   B HD13 1 c 1 
ATOM   1016 H HD21 . LEU   A 1 69  ? 21.738 -11.197 4.246   1   45.865  ? 81  LEU   B HD21 1 c 1 
ATOM   1017 H HD22 . LEU   A 1 69  ? 22.406 -9.786  3.969   1   44.965  ? 81  LEU   B HD22 1 c 1 
ATOM   1018 H HD23 . LEU   A 1 69  ? 20.988 -10.126 3.349   1   44.529  ? 81  LEU   B HD23 1 c 1 
ATOM   1019 N N    . GLY   A 1 70  ? 19.005 -10.201 8.24    1   32.702  ? 82  GLY   B N    1 ? 1 
ATOM   1020 C CA   . GLY   A 1 70  ? 17.775 -10.932 8.398   1   39.624  ? 82  GLY   B CA   1 ? 1 
ATOM   1021 C C    . GLY   A 1 70  ? 17.438 -11.197 9.86    1   44.766  ? 82  GLY   B C    1 ? 1 
ATOM   1022 O O    . GLY   A 1 70  ? 16.576 -12.031 10.077  1   49.457  ? 82  GLY   B O    1 ? 1 
ATOM   1023 H H    . GLY   A 1 70  ? 18.956 -9.293  8.159   1   32.623  ? 82  GLY   B H    1 c 1 
ATOM   1024 H HA2  . GLY   A 1 70  ? 17.043 -10.421 7.982   1   37.777  ? 82  GLY   B HA2  1 c 1 
ATOM   1025 H HA3  . GLY   A 1 70  ? 17.849 -11.791 7.919   1   39.261  ? 82  GLY   B HA3  1 c 1 
ATOM   1026 N N    . LYS   A 1 71  ? 18.214 -10.661 10.827  1   43.851  ? 83  LYS   B N    1 ? 1 
ATOM   1027 C CA   . LYS   A 1 71  ? 18.129 -11.075 12.239  1   42.683  ? 83  LYS   B CA   1 ? 1 
ATOM   1028 C C    . LYS   A 1 71  ? 17.329 -10.04  13.021  1   53.598  ? 83  LYS   B C    1 ? 1 
ATOM   1029 O O    . LYS   A 1 71  ? 17.537 -9.924  14.231  1   63.346  ? 83  LYS   B O    1 ? 1 
ATOM   1030 C CB   . LYS   A 1 71  ? 19.485 -11.3   12.931  1   42.292  ? 83  LYS   B CB   1 ? 1 
ATOM   1031 H H    . LYS   A 1 71  ? 18.811 -10.006 10.603  1   42.227  ? 83  LYS   B H    1 c 1 
ATOM   1032 H HA   . LYS   A 1 71  ? 17.635 -11.933 12.277  1   45.87   ? 83  LYS   B HA   1 c 1 
ATOM   1033 H HB2  . LYS   A 1 71  ? 20.206 -11.07  12.201  0   30      ? 83  LYS   B HB2  1 c 1 
ATOM   1034 H HB3  . LYS   A 1 71  ? 19.393 -11.494 13.818  0   30      ? 83  LYS   B HB3  1 c 1 
ATOM   1035 N N    . GLY   A 1 72  ? 16.488 -9.286  12.315  1   57.184  ? 84  GLY   B N    1 ? 1 
ATOM   1036 C CA   . GLY   A 1 72  ? 15.607 -8.254  12.828  1   60.979  ? 84  GLY   B CA   1 ? 1 
ATOM   1037 C C    . GLY   A 1 72  ? 16.322 -7.145  13.612  1   61.89   ? 84  GLY   B C    1 ? 1 
ATOM   1038 O O    . GLY   A 1 72  ? 15.662 -6.442  14.373  1   58.566  ? 84  GLY   B O    1 ? 1 
ATOM   1039 H H    . GLY   A 1 72  ? 16.461 -9.432  11.414  1   55.008  ? 84  GLY   B H    1 c 1 
ATOM   1040 H HA2  . GLY   A 1 72  ? 15.123 -7.85   12.07   1   58.699  ? 84  GLY   B HA2  1 c 1 
ATOM   1041 H HA3  . GLY   A 1 72  ? 14.936 -8.678  13.414  1   61.845  ? 84  GLY   B HA3  1 c 1 
ATOM   1042 N N    . GLN   A 1 73  ? 17.622 -6.929  13.383  1   47.801  ? 85  GLN   B N    1 ? 1 
ATOM   1043 C CA   . GLN   A 1 73  ? 18.368 -5.877  14.069  1   45.498  ? 85  GLN   B CA   1 ? 1 
ATOM   1044 C C    . GLN   A 1 73  ? 18.281 -4.541  13.362  1   39.237  ? 85  GLN   B C    1 ? 1 
ATOM   1045 O O    . GLN   A 1 73  ? 18.533 -3.506  13.94   1   39.119  ? 85  GLN   B O    1 ? 1 
ATOM   1046 C CB   . GLN   A 1 73  ? 19.853 -6.175  14.184  1   43.098  ? 85  GLN   B CB   1 ? 1 
ATOM   1047 C CG   . GLN   A 1 73  ? 20.116 -7.543  14.778  1   49.698  ? 85  GLN   B CG   1 ? 1 
ATOM   1048 C CD   . GLN   A 1 73  ? 21.538 -7.969  14.529  1   54.713  ? 85  GLN   B CD   1 ? 1 
ATOM   1049 O OE1  . GLN   A 1 73  ? 22.336 -7.34   13.8    1   52.481  ? 85  GLN   B OE1  1 ? 1 
ATOM   1050 N NE2  . GLN   A 1 73  ? 21.824 -9.093  15.126  1   54.106  ? 85  GLN   B NE2  1 ? 1 
ATOM   1051 H H    . GLN   A 1 73  ? 18.057 -7.438  12.762  1   49.091  ? 85  GLN   B H    1 c 1 
ATOM   1052 H HA   . GLN   A 1 73  ? 17.998 -5.775  14.983  1   46.529  ? 85  GLN   B HA   1 c 1 
ATOM   1053 H HB2  . GLN   A 1 73  ? 20.258 -6.126  13.292  1   43.303  ? 85  GLN   B HB2  1 c 1 
ATOM   1054 H HB3  . GLN   A 1 73  ? 20.276 -5.492  14.746  1   46.009  ? 85  GLN   B HB3  1 c 1 
ATOM   1055 H HG2  . GLN   A 1 73  ? 19.948 -7.52   15.745  1   51.667  ? 85  GLN   B HG2  1 c 1 
ATOM   1056 H HG3  . GLN   A 1 73  ? 19.509 -8.201  14.38   1   48.932  ? 85  GLN   B HG3  1 c 1 
ATOM   1057 H HE21 . GLN   A 1 73  ? 22.654 -9.404  15.104  1   55.792  ? 85  GLN   B HE21 1 c 1 
ATOM   1058 H HE22 . GLN   A 1 73  ? 21.192 -9.547  15.555  1   55.822  ? 85  GLN   B HE22 1 c 1 
ATOM   1059 N N    . VAL   A 1 74  ? 17.751 -4.523  12.167  1   32.342  ? 86  VAL   B N    1 ? 1 
ATOM   1060 C CA   . VAL   A 1 74  ? 17.497 -3.269  11.463  1   32.582  ? 86  VAL   B CA   1 ? 1 
ATOM   1061 C C    . VAL   A 1 74  ? 16.08  -3.312  10.919  1   29.957  ? 86  VAL   B C    1 ? 1 
ATOM   1062 O O    . VAL   A 1 74  ? 15.504 -4.37   10.958  1   32.766  ? 86  VAL   B O    1 ? 1 
ATOM   1063 C CB   . VAL   A 1 74  ? 18.445 -3.113  10.261  1   31.867  ? 86  VAL   B CB   1 ? 1 
ATOM   1064 C CG1  . VAL   A 1 74  ? 19.843 -2.807  10.744  1   35.001  ? 86  VAL   B CG1  1 ? 1 
ATOM   1065 C CG2  . VAL   A 1 74  ? 18.436 -4.404  9.439   1   29.494  ? 86  VAL   B CG2  1 ? 1 
ATOM   1066 H H    . VAL   A 1 74  ? 17.523 -5.309  11.761  1   33.492  ? 86  VAL   B H    1 c 1 
ATOM   1067 H HA   . VAL   A 1 74  ? 17.598 -2.513  12.071  1   33.037  ? 86  VAL   B HA   1 c 1 
ATOM   1068 H HB   . VAL   A 1 74  ? 18.12  -2.365  9.707   1   30.875  ? 86  VAL   B HB   1 c 1 
ATOM   1069 H HG11 . VAL   A 1 74  ? 20.153 -3.527  11.318  1   35.478  ? 86  VAL   B HG11 1 c 1 
ATOM   1070 H HG12 . VAL   A 1 74  ? 19.839 -1.974  11.244  1   35.244  ? 86  VAL   B HG12 1 c 1 
ATOM   1071 H HG13 . VAL   A 1 74  ? 20.439 -2.724  9.981   1   33.851  ? 86  VAL   B HG13 1 c 1 
ATOM   1072 H HG21 . VAL   A 1 74  ? 18.947 -4.27   8.623   1   29.27   ? 86  VAL   B HG21 1 c 1 
ATOM   1073 H HG22 . VAL   A 1 74  ? 17.522 -4.642  9.21    1   29.543  ? 86  VAL   B HG22 1 c 1 
ATOM   1074 H HG23 . VAL   A 1 74  ? 18.839 -5.123  9.954   1   30.895  ? 86  VAL   B HG23 1 c 1 
ATOM   1075 N N    . ILE   A 1 75  ? 15.595 -2.208  10.378  1   28.05   ? 87  ILE   B N    1 ? 1 
ATOM   1076 C CA   . ILE   A 1 75  ? 14.268 -2.169  9.78    1   29.358  ? 87  ILE   B CA   1 ? 1 
ATOM   1077 C C    . ILE   A 1 75  ? 14.185 -3.177  8.628   1   28.191  ? 87  ILE   B C    1 ? 1 
ATOM   1078 O O    . ILE   A 1 75  ? 15.252 -3.417  8       1   25.839  ? 87  ILE   B O    1 ? 1 
ATOM   1079 C CB   . ILE   A 1 75  ? 13.887 -0.742  9.348   1   29.712  ? 87  ILE   B CB   1 ? 1 
ATOM   1080 C CG1  . ILE   A 1 75  ? 14.942 -0.092  8.404   1   30.118  ? 87  ILE   B CG1  1 ? 1 
ATOM   1081 C CG2  . ILE   A 1 75  ? 13.627 0.134   10.517  1   33.284  ? 87  ILE   B CG2  1 ? 1 
ATOM   1082 C CD1  . ILE   A 1 75  ? 14.523 1.268   7.791   1   33.523  ? 87  ILE   B CD1  1 ? 1 
ATOM   1083 H H    . ILE   A 1 75  ? 16.096 -1.445  10.396  1   28.836  ? 87  ILE   B H    1 c 1 
ATOM   1084 H HA   . ILE   A 1 75  ? 13.631 -2.449  10.465  1   30.244  ? 87  ILE   B HA   1 c 1 
ATOM   1085 H HB   . ILE   A 1 75  ? 13.053 -0.808  8.843   1   29.964  ? 87  ILE   B HB   1 c 1 
ATOM   1086 H HG12 . ILE   A 1 75  ? 15.772 0.04    8.906   1   30.955  ? 87  ILE   B HG12 1 c 1 
ATOM   1087 H HG13 . ILE   A 1 75  ? 15.133 -0.715  7.674   1   29.755  ? 87  ILE   B HG13 1 c 1 
ATOM   1088 H HG21 . ILE   A 1 75  ? 13.244 0.976   10.218  1   32.64   ? 87  ILE   B HG21 1 c 1 
ATOM   1089 H HG22 . ILE   A 1 75  ? 14.461 0.308   10.986  1   33.196  ? 87  ILE   B HG22 1 c 1 
ATOM   1090 H HG23 . ILE   A 1 75  ? 13.004 -0.304  11.121  1   33.678  ? 87  ILE   B HG23 1 c 1 
ATOM   1091 H HD11 . ILE   A 1 75  ? 13.66  1.175   7.345   1   32.234  ? 87  ILE   B HD11 1 c 1 
ATOM   1092 H HD12 . ILE   A 1 75  ? 15.194 1.551   7.14    1   32.034  ? 87  ILE   B HD12 1 c 1 
ATOM   1093 H HD13 . ILE   A 1 75  ? 14.453 1.941   8.494   1   33.326  ? 87  ILE   B HD13 1 c 1 
ATOM   1094 N N    . LYS   A 1 76  ? 12.933 -3.622  8.32    1   32.471  ? 88  LYS   B N    1 ? 1 
ATOM   1095 C CA   . LYS   A 1 76  ? 12.642 -4.631  7.281   1   29.937  ? 88  LYS   B CA   1 ? 1 
ATOM   1096 C C    . LYS   A 1 76  ? 13.316 -4.212  5.983   1   32.419  ? 88  LYS   B C    1 ? 1 
ATOM   1097 O O    . LYS   A 1 76  ? 13.873 -5.043  5.296   1   30.422  ? 88  LYS   B O    1 ? 1 
ATOM   1098 C CB   . LYS   A 1 76  ? 11.12  -4.913  7.08    1   32.686  ? 88  LYS   B CB   1 ? 1 
ATOM   1099 H H    . LYS   A 1 76  ? 12.228 -3.272  8.786   1   31.654  ? 88  LYS   B H    1 c 1 
ATOM   1100 H HA   . LYS   A 1 76  ? 13.056 -5.483  7.571   1   31.752  ? 88  LYS   B HA   1 c 1 
ATOM   1101 H HB2  . LYS   A 1 76  ? 11.069 -5.796  6.707   0   30      ? 88  LYS   B HB2  1 c 1 
ATOM   1102 H HB3  . LYS   A 1 76  ? 10.675 -4.178  7.532   0   30      ? 88  LYS   B HB3  1 c 1 
ATOM   1103 N N    . ALA   A 1 77  ? 13.211 -2.927  5.625   1   28.815  ? 89  ALA   B N    1 ? 1 
ATOM   1104 C CA   . ALA   A 1 77  ? 13.691 -2.425  4.339   1   29.09   ? 89  ALA   B CA   1 ? 1 
ATOM   1105 C C    . ALA   A 1 77  ? 15.17  -2.638  4.178   1   29.611  ? 89  ALA   B C    1 ? 1 
ATOM   1106 O O    . ALA   A 1 77  ? 15.61  -2.84   3.064   1   27.462  ? 89  ALA   B O    1 ? 1 
ATOM   1107 C CB   . ALA   A 1 77  ? 13.381 -0.968  4.154   1   30.373  ? 89  ALA   B CB   1 ? 1 
ATOM   1108 H H    . ALA   A 1 77  ? 12.818 -2.337  6.202   1   29.966  ? 89  ALA   B H    1 c 1 
ATOM   1109 H HA   . ALA   A 1 77  ? 13.23  -2.941  3.621   1   29.668  ? 89  ALA   B HA   1 c 1 
ATOM   1110 H HB1  . ALA   A 1 77  ? 12.422 -0.826  4.215   1   30.406  ? 89  ALA   B HB1  1 c 1 
ATOM   1111 H HB2  . ALA   A 1 77  ? 13.826 -0.448  4.844   1   29.894  ? 89  ALA   B HB2  1 c 1 
ATOM   1112 H HB3  . ALA   A 1 77  ? 13.693 -0.676  3.281   1   29.889  ? 89  ALA   B HB3  1 c 1 
ATOM   1113 N N    . TRP   A 1 78  ? 15.929 -2.701  5.309   1   28.662  ? 90  TRP   B N    1 ? 1 
ATOM   1114 C CA   . TRP   A 1 78  ? 17.35  -2.941  5.209   1   29.246  ? 90  TRP   B CA   1 ? 1 
ATOM   1115 C C    . TRP   A 1 78  ? 17.6   -4.431  4.978   1   30.348  ? 90  TRP   B C    1 ? 1 
ATOM   1116 O O    . TRP   A 1 78  ? 18.477 -4.793  4.215   1   33.399  ? 90  TRP   B O    1 ? 1 
ATOM   1117 C CB   . TRP   A 1 78  ? 18.128 -2.396  6.404   1   24.974  ? 90  TRP   B CB   1 ? 1 
ATOM   1118 C CG   . TRP   A 1 78  ? 18.569 -0.997  6.243   1   28.577  ? 90  TRP   B CG   1 ? 1 
ATOM   1119 C CD1  . TRP   A 1 78  ? 17.877 0.131   5.869   1   27.004  ? 90  TRP   B CD1  1 ? 1 
ATOM   1120 C CD2  . TRP   A 1 78  ? 19.921 -0.583  6.464   1   27.576  ? 90  TRP   B CD2  1 ? 1 
ATOM   1121 N NE1  . TRP   A 1 78  ? 18.71  1.213   5.852   1   28.097  ? 90  TRP   B NE1  1 ? 1 
ATOM   1122 C CE2  . TRP   A 1 78  ? 19.969 0.805   6.198   1   33.92   ? 90  TRP   B CE2  1 ? 1 
ATOM   1123 C CE3  . TRP   A 1 78  ? 21.066 -1.23   6.867   1   25.526  ? 90  TRP   B CE3  1 ? 1 
ATOM   1124 C CZ2  . TRP   A 1 78  ? 21.14  1.527   6.341   1   31.411  ? 90  TRP   B CZ2  1 ? 1 
ATOM   1125 C CZ3  . TRP   A 1 78  ? 22.239 -0.543  6.971   1   29.144  ? 90  TRP   B CZ3  1 ? 1 
ATOM   1126 C CH2  . TRP   A 1 78  ? 22.25  0.844   6.778   1   34.073  ? 90  TRP   B CH2  1 ? 1 
ATOM   1127 H H    . TRP   A 1 78  ? 15.552 -2.575  6.132   1   29.231  ? 90  TRP   B H    1 c 1 
ATOM   1128 H HA   . TRP   A 1 78  ? 17.676 -2.457  4.403   1   28.181  ? 90  TRP   B HA   1 c 1 
ATOM   1129 H HB2  . TRP   A 1 78  ? 17.562 -2.459  7.203   1   27.063  ? 90  TRP   B HB2  1 c 1 
ATOM   1130 H HB3  . TRP   A 1 78  ? 18.915 -2.963  6.549   1   27.16   ? 90  TRP   B HB3  1 c 1 
ATOM   1131 H HD1  . TRP   A 1 78  ? 16.96  0.161   5.647   1   27      ? 90  TRP   B HD1  1 c 1 
ATOM   1132 H HE1  . TRP   A 1 78  ? 18.484 2.02    5.636   1   29.308  ? 90  TRP   B HE1  1 c 1 
ATOM   1133 H HE3  . TRP   A 1 78  ? 21.047 -2.158  7.03    1   26.716  ? 90  TRP   B HE3  1 c 1 
ATOM   1134 H HZ2  . TRP   A 1 78  ? 21.165 2.455   6.183   1   33.152  ? 90  TRP   B HZ2  1 c 1 
ATOM   1135 H HZ3  . TRP   A 1 78  ? 23.017 -0.984  7.268   1   30.515  ? 90  TRP   B HZ3  1 c 1 
ATOM   1136 H HH2  . TRP   A 1 78  ? 23.067 1.305   6.845   1   33.899  ? 90  TRP   B HH2  1 c 1 
ATOM   1137 N N    . ASP   A 1 79  ? 16.876 -5.282  5.671   1   30.344  ? 91  ASP   B N    1 ? 1 
ATOM   1138 C CA   . ASP   A 1 79  ? 17.04  -6.717  5.499   1   33.217  ? 91  ASP   B CA   1 ? 1 
ATOM   1139 C C    . ASP   A 1 79  ? 16.715 -7.068  4.037   1   35.694  ? 91  ASP   B C    1 ? 1 
ATOM   1140 O O    . ASP   A 1 79  ? 17.348 -7.896  3.402   1   31.6    ? 91  ASP   B O    1 ? 1 
ATOM   1141 C CB   . ASP   A 1 79  ? 16.167 -7.406  6.545   1   31.893  ? 91  ASP   B CB   1 ? 1 
ATOM   1142 C CG   . ASP   A 1 79  ? 16.788 -7.707  7.908   1   32.497  ? 91  ASP   B CG   1 ? 1 
ATOM   1143 O OD1  . ASP   A 1 79  ? 18.004 -7.663  8.051   1   32.668  ? 91  ASP   B OD1  1 ? 1 
ATOM   1144 O OD2  . ASP   A 1 79  ? 16.038 -7.976  8.843   1   39.731  ? 91  ASP   B OD2  1 ? 1 
ATOM   1145 H H    . ASP   A 1 79  ? 16.268 -4.971  6.279   1   30.986  ? 91  ASP   B H    1 c 1 
ATOM   1146 H HA   . ASP   A 1 79  ? 17.98  -6.945  5.674   1   33.012  ? 91  ASP   B HA   1 c 1 
ATOM   1147 H HB2  . ASP   A 1 79  ? 15.363 -6.866  6.696   1   32.151  ? 91  ASP   B HB2  1 c 1 
ATOM   1148 H HB3  . ASP   A 1 79  ? 15.872 -8.262  6.168   1   32.952  ? 91  ASP   B HB3  1 c 1 
ATOM   1149 N N    . ILE   A 1 80  ? 15.72  -6.391  3.474   1   32.705  ? 92  ILE   B N    1 ? 1 
ATOM   1150 C CA   . ILE   A 1 80  ? 15.321 -6.613  2.102   1   34.284  ? 92  ILE   B CA   1 ? 1 
ATOM   1151 C C    . ILE   A 1 80  ? 16.319 -5.988  1.136   1   37.596  ? 92  ILE   B C    1 ? 1 
ATOM   1152 O O    . ILE   A 1 80  ? 16.789 -6.686  0.221   1   29.196  ? 92  ILE   B O    1 ? 1 
ATOM   1153 C CB   . ILE   A 1 80  ? 13.887 -6.096  1.871   1   31.597  ? 92  ILE   B CB   1 ? 1 
ATOM   1154 C CG1  . ILE   A 1 80  ? 12.892 -6.967  2.615   1   41.586  ? 92  ILE   B CG1  1 ? 1 
ATOM   1155 C CG2  . ILE   A 1 80  ? 13.607 -6.007  0.38    1   39.61   ? 92  ILE   B CG2  1 ? 1 
ATOM   1156 C CD1  . ILE   A 1 80  ? 11.535 -6.283  2.704   1   38.62   ? 92  ILE   B CD1  1 ? 1 
ATOM   1157 H H    . ILE   A 1 80  ? 15.262 -5.774  3.969   1   33.143  ? 92  ILE   B H    1 c 1 
ATOM   1158 H HA   . ILE   A 1 80  ? 15.316 -7.577  1.945   1   34.958  ? 92  ILE   B HA   1 c 1 
ATOM   1159 H HB   . ILE   A 1 80  ? 13.831 -5.194  2.243   1   34.185  ? 92  ILE   B HB   1 c 1 
ATOM   1160 H HG12 . ILE   A 1 80  ? 12.795 -7.821  2.147   1   39.549  ? 92  ILE   B HG12 1 c 1 
ATOM   1161 H HG13 . ILE   A 1 80  ? 13.225 -7.144  3.518   1   38.167  ? 92  ILE   B HG13 1 c 1 
ATOM   1162 H HG21 . ILE   A 1 80  ? 12.666 -5.816  0.234   1   37.934  ? 92  ILE   B HG21 1 c 1 
ATOM   1163 H HG22 . ILE   A 1 80  ? 13.833 -6.851  -0.045  1   38.257  ? 92  ILE   B HG22 1 c 1 
ATOM   1164 H HG23 . ILE   A 1 80  ? 14.14  -5.296  -0.013  1   36.922  ? 92  ILE   B HG23 1 c 1 
ATOM   1165 H HD11 . ILE   A 1 80  ? 11.642 -5.391  3.084   1   38.679  ? 92  ILE   B HD11 1 c 1 
ATOM   1166 H HD12 . ILE   A 1 80  ? 10.945 -6.81   3.276   1   40.473  ? 92  ILE   B HD12 1 c 1 
ATOM   1167 H HD13 . ILE   A 1 80  ? 11.141 -6.211  1.814   1   40.246  ? 92  ILE   B HD13 1 c 1 
ATOM   1168 N N    . GLY   A 1 81  ? 16.71  -4.728  1.375   1   29.707  ? 93  GLY   B N    1 ? 1 
ATOM   1169 C CA   . GLY   A 1 81  ? 17.484 -3.998  0.375   1   33.021  ? 93  GLY   B CA   1 ? 1 
ATOM   1170 C C    . GLY   A 1 81  ? 18.978 -4.367  0.384   1   34.355  ? 93  GLY   B C    1 ? 1 
ATOM   1171 O O    . GLY   A 1 81  ? 19.529 -4.627  -0.674  1   37.127  ? 93  GLY   B O    1 ? 1 
ATOM   1172 H H    . GLY   A 1 81  ? 16.493 -4.317  2.162   1   31.337  ? 93  GLY   B H    1 c 1 
ATOM   1173 H HA2  . GLY   A 1 81  ? 17.108 -4.184  -0.518  1   33.271  ? 93  GLY   B HA2  1 c 1 
ATOM   1174 H HA3  . GLY   A 1 81  ? 17.388 -3.032  0.544   1   32.093  ? 93  GLY   B HA3  1 c 1 
ATOM   1175 N N    . VAL   A 1 82  ? 19.573 -4.615  1.572   1   32.062  ? 94  VAL   B N    1 ? 1 
ATOM   1176 C CA   . VAL   A 1 82  ? 20.971 -5.01   1.656   1   31.884  ? 94  VAL   B CA   1 ? 1 
ATOM   1177 C C    . VAL   A 1 82  ? 21.22  -6.401  1.12    1   32.608  ? 94  VAL   B C    1 ? 1 
ATOM   1178 O O    . VAL   A 1 82  ? 22.28  -6.665  0.496   1   33.055  ? 94  VAL   B O    1 ? 1 
ATOM   1179 C CB   . VAL   A 1 82  ? 21.571 -4.831  3.043   1   34.95   ? 94  VAL   B CB   1 ? 1 
ATOM   1180 C CG1  . VAL   A 1 82  ? 23.015 -5.311  3.108   1   41.56   ? 94  VAL   B CG1  1 ? 1 
ATOM   1181 C CG2  . VAL   A 1 82  ? 21.489 -3.357  3.351   1   32.511  ? 94  VAL   B CG2  1 ? 1 
ATOM   1182 H H    . VAL   A 1 82  ? 19.089 -4.536  2.343   1   31.674  ? 94  VAL   B H    1 c 1 
ATOM   1183 H HA   . VAL   A 1 82  ? 21.459 -4.402  1.067   1   33.155  ? 94  VAL   B HA   1 c 1 
ATOM   1184 H HB   . VAL   A 1 82  ? 21.021 -5.338  3.685   1   34.431  ? 94  VAL   B HB   1 c 1 
ATOM   1185 H HG11 . VAL   A 1 82  ? 23.49  -5.021  2.311   1   40.548  ? 94  VAL   B HG11 1 c 1 
ATOM   1186 H HG12 . VAL   A 1 82  ? 23.035 -6.281  3.163   1   40.21   ? 94  VAL   B HG12 1 c 1 
ATOM   1187 H HG13 . VAL   A 1 82  ? 23.444 -4.935  3.894   1   40.161  ? 94  VAL   B HG13 1 c 1 
ATOM   1188 H HG21 . VAL   A 1 82  ? 21.903 -3.183  4.213   1   33.474  ? 94  VAL   B HG21 1 c 1 
ATOM   1189 H HG22 . VAL   A 1 82  ? 20.558 -3.08   3.381   1   32.362  ? 94  VAL   B HG22 1 c 1 
ATOM   1190 H HG23 . VAL   A 1 82  ? 21.954 -2.853  2.662   1   33.65   ? 94  VAL   B HG23 1 c 1 
ATOM   1191 N N    . ALA   A 1 83  ? 20.183 -7.236  1.18    1   35.605  ? 95  ALA   B N    1 ? 1 
ATOM   1192 C CA   . ALA   A 1 83  ? 20.317 -8.565  0.662   1   34.878  ? 95  ALA   B CA   1 ? 1 
ATOM   1193 C C    . ALA   A 1 83  ? 20.444 -8.546  -0.855  1   39.176  ? 95  ALA   B C    1 ? 1 
ATOM   1194 O O    . ALA   A 1 83  ? 20.891 -9.542  -1.43   1   36.142  ? 95  ALA   B O    1 ? 1 
ATOM   1195 C CB   . ALA   A 1 83  ? 19.159 -9.47   1.095   1   39.927  ? 95  ALA   B CB   1 ? 1 
ATOM   1196 H H    . ALA   A 1 83  ? 19.392 -6.978  1.558   1   33.622  ? 95  ALA   B H    1 c 1 
ATOM   1197 H HA   . ALA   A 1 83  ? 21.161 -8.946  1.028   1   37.139  ? 95  ALA   B HA   1 c 1 
ATOM   1198 H HB1  . ALA   A 1 83  ? 19.12  -9.51   2.066   1   37.919  ? 95  ALA   B HB1  1 c 1 
ATOM   1199 H HB2  . ALA   A 1 83  ? 18.321 -9.113  0.755   1   38.132  ? 95  ALA   B HB2  1 c 1 
ATOM   1200 H HB3  . ALA   A 1 83  ? 19.293 -10.365 0.742   1   39.627  ? 95  ALA   B HB3  1 c 1 
ATOM   1201 N N    . THR   A 1 84  ? 20.021 -7.466  -1.505  1   32.088  ? 96  THR   B N    1 ? 1 
ATOM   1202 C CA   . THR   A 1 84  ? 20.14  -7.391  -2.983  1   37.365  ? 96  THR   B CA   1 ? 1 
ATOM   1203 C C    . THR   A 1 84  ? 21.497 -6.806  -3.425  1   40.82   ? 96  THR   B C    1 ? 1 
ATOM   1204 O O    . THR   A 1 84  ? 21.747 -6.662  -4.638  1   35.059  ? 96  THR   B O    1 ? 1 
ATOM   1205 C CB   . THR   A 1 84  ? 19.024 -6.52   -3.601  1   37.018  ? 96  THR   B CB   1 ? 1 
ATOM   1206 O OG1  . THR   A 1 84  ? 19.175 -5.121  -3.22   1   35.567  ? 96  THR   B OG1  1 ? 1 
ATOM   1207 C CG2  . THR   A 1 84  ? 17.636 -6.969  -3.23   1   38.142  ? 96  THR   B CG2  1 ? 1 
ATOM   1208 H H    . THR   A 1 84  ? 19.637 -6.771  -1.054  1   33.195  ? 96  THR   B H    1 c 1 
ATOM   1209 H HA   . THR   A 1 84  ? 20.058 -8.299  -3.346  1   38.276  ? 96  THR   B HA   1 c 1 
ATOM   1210 H HB   . THR   A 1 84  ? 19.097 -6.584  -4.583  1   39.033  ? 96  THR   B HB   1 c 1 
ATOM   1211 H HG1  . THR   A 1 84  ? 19.248 -5.084  -2.369  0   30      ? 96  THR   B HG1  1 c 1 
ATOM   1212 H HG21 . THR   A 1 84  ? 16.982 -6.397  -3.666  1   37.88   ? 96  THR   B HG21 1 c 1 
ATOM   1213 H HG22 . THR   A 1 84  ? 17.522 -6.915  -2.267  1   36.17   ? 96  THR   B HG22 1 c 1 
ATOM   1214 H HG23 . THR   A 1 84  ? 17.504 -7.888  -3.52   1   38.833  ? 96  THR   B HG23 1 c 1 
ATOM   1215 N N    . MET   A 1 85  ? 22.361 -6.38   -2.495  1   40.177  ? 97  MET   B N    1 ? 1 
ATOM   1216 C CA   . MET   A 1 85  ? 23.538 -5.617  -2.908  1   41.437  ? 97  MET   B CA   1 ? 1 
ATOM   1217 C C    . MET   A 1 85  ? 24.757 -6.521  -3.072  1   40.06   ? 97  MET   B C    1 ? 1 
ATOM   1218 O O    . MET   A 1 85  ? 24.905 -7.524  -2.385  1   39.056  ? 97  MET   B O    1 ? 1 
ATOM   1219 C CB   . MET   A 1 85  ? 23.844 -4.527  -1.85   1   41.681  ? 97  MET   B CB   1 ? 1 
ATOM   1220 C CG   . MET   A 1 85  ? 22.768 -3.471  -1.752  1   41.378  ? 97  MET   B CG   1 ? 1 
ATOM   1221 S SD   . MET   A 1 85  ? 22.964 -2.163  -0.517  1   36.185  ? 97  MET   B SD   1 ? 1 
ATOM   1222 C CE   . MET   A 1 85  ? 24.432 -1.313  -1.165  1   42.737  ? 97  MET   B CE   1 ? 1 
ATOM   1223 H H    . MET   A 1 85  ? 22.228 -6.56   -1.61   1   38.877  ? 97  MET   B H    1 c 1 
ATOM   1224 H HA   . MET   A 1 85  ? 23.344 -5.183  -3.776  1   41.944  ? 97  MET   B HA   1 c 1 
ATOM   1225 H HB2  . MET   A 1 85  ? 23.95  -4.958  -0.976  1   40.783  ? 97  MET   B HB2  1 c 1 
ATOM   1226 H HB3  . MET   A 1 85  ? 24.696 -4.097  -2.079  1   42.846  ? 97  MET   B HB3  1 c 1 
ATOM   1227 H HG2  . MET   A 1 85  ? 22.683 -3.041  -2.623  1   41.189  ? 97  MET   B HG2  1 c 1 
ATOM   1228 H HG3  . MET   A 1 85  ? 21.919 -3.919  -1.573  1   39.257  ? 97  MET   B HG3  1 c 1 
ATOM   1229 H HE1  . MET   A 1 85  ? 24.709 -0.622  -0.537  1   41.7    ? 97  MET   B HE1  1 c 1 
ATOM   1230 H HE2  . MET   A 1 85  ? 25.156 -1.956  -1.279  1   42.708  ? 97  MET   B HE2  1 c 1 
ATOM   1231 H HE3  . MET   A 1 85  ? 24.219 -0.907  -2.026  1   42.498  ? 97  MET   B HE3  1 c 1 
ATOM   1232 N N    . LYS   A 1 86  ? 25.695 -6.089  -3.939  1   44.344  ? 98  LYS   B N    1 ? 1 
ATOM   1233 C CA   . LYS   A 1 86  ? 27.032 -6.665  -4.106  1   43.845  ? 98  LYS   B CA   1 ? 1 
ATOM   1234 C C    . LYS   A 1 86  ? 28.081 -5.875  -3.304  1   46.674  ? 98  LYS   B C    1 ? 1 
ATOM   1235 O O    . LYS   A 1 86  ? 27.872 -4.688  -3.097  1   45.666  ? 98  LYS   B O    1 ? 1 
ATOM   1236 C CB   . LYS   A 1 86  ? 27.397 -6.714  -5.619  1   45.776  ? 98  LYS   B CB   1 ? 1 
ATOM   1237 H H    . LYS   A 1 86  ? 25.479 -5.373  -4.464  1   43.56   ? 98  LYS   B H    1 c 1 
ATOM   1238 H HA   . LYS   A 1 86  ? 27.013 -7.595  -3.764  1   44.371  ? 98  LYS   B HA   1 c 1 
ATOM   1239 H HB2  . LYS   A 1 86  ? 28.361 -6.729  -5.706  0   30      ? 98  LYS   B HB2  1 c 1 
ATOM   1240 H HB3  . LYS   A 1 86  ? 26.554 -6.731  -6.141  0   30      ? 98  LYS   B HB3  1 c 1 
ATOM   1241 N N    . LYS   A 1 87  ? 29.222 -6.54   -2.921  1   44.713  ? 99  LYS   B N    1 ? 1 
ATOM   1242 C CA   . LYS   A 1 87  ? 30.378 -5.983  -2.226  1   45.803  ? 99  LYS   B CA   1 ? 1 
ATOM   1243 C C    . LYS   A 1 87  ? 30.832 -4.789  -3.067  1   46.694  ? 99  LYS   B C    1 ? 1 
ATOM   1244 O O    . LYS   A 1 87  ? 31     -4.957  -4.261  1   47.048  ? 99  LYS   B O    1 ? 1 
ATOM   1245 C CB   . LYS   A 1 87  ? 31.698 -6.776  -2.033  1   43.52   ? 99  LYS   B CB   1 ? 1 
ATOM   1246 H H    . LYS   A 1 87  ? 29.258 -7.43   -3.126  1   46.096  ? 99  LYS   B H    1 c 1 
ATOM   1247 H HA   . LYS   A 1 87  ? 30.076 -5.654  -1.341  1   42.851  ? 99  LYS   B HA   1 c 1 
ATOM   1248 H HB2  . LYS   A 1 87  ? 32.39  -6.272  -2.244  0   30      ? 99  LYS   B HB2  1 c 1 
ATOM   1249 H HB3  . LYS   A 1 87  ? 31.333 -7.773  -1.952  0   30      ? 99  LYS   B HB3  1 c 1 
ATOM   1250 N N    . GLY   A 1 88  ? 30.888 -3.591  -2.464  1   48.83   ? 100 GLY   B N    1 ? 1 
ATOM   1251 C CA   . GLY   A 1 88  ? 31.339 -2.397  -3.175  1   47.949  ? 100 GLY   B CA   1 ? 1 
ATOM   1252 C C    . GLY   A 1 88  ? 30.194 -1.564  -3.774  1   48.399  ? 100 GLY   B C    1 ? 1 
ATOM   1253 O O    . GLY   A 1 88  ? 30.42  -0.442  -4.292  1   50.505  ? 100 GLY   B O    1 ? 1 
ATOM   1254 H H    . GLY   A 1 88  ? 30.639 -3.515  -1.588  1   45.747  ? 100 GLY   B H    1 c 1 
ATOM   1255 H HA2  . GLY   A 1 88  ? 31.851 -1.835  -2.547  1   49.832  ? 100 GLY   B HA2  1 c 1 
ATOM   1256 H HA3  . GLY   A 1 88  ? 31.953 -2.669  -3.897  1   51.664  ? 100 GLY   B HA3  1 c 1 
ATOM   1257 N N    . GLU   A 1 89  ? 28.967 -2.086  -3.723  1   45.398  ? 101 GLU   B N    1 ? 1 
ATOM   1258 C CA   . GLU   A 1 89  ? 27.822 -1.407  -4.333  1   47.824  ? 101 GLU   B CA   1 ? 1 
ATOM   1259 C C    . GLU   A 1 89  ? 27.399 -0.205  -3.466  1   48.912  ? 101 GLU   B C    1 ? 1 
ATOM   1260 O O    . GLU   A 1 89  ? 27.433 -0.303  -2.216  1   43.87   ? 101 GLU   B O    1 ? 1 
ATOM   1261 C CB   . GLU   A 1 89  ? 26.682 -2.439  -4.521  1   45.57   ? 101 GLU   B CB   1 ? 1 
ATOM   1262 C CG   . GLU   A 1 89  ? 25.451 -1.843  -5.223  1   44.39   ? 101 GLU   B CG   1 ? 1 
ATOM   1263 C CD   . GLU   A 1 89  ? 24.297 -2.844  -5.365  1   42.708  ? 101 GLU   B CD   1 ? 1 
ATOM   1264 O OE1  . GLU   A 1 89  ? 24.539 -4.026  -5.812  1   44.177  ? 101 GLU   B OE1  1 ? 1 
ATOM   1265 O OE2  . GLU   A 1 89  ? 23.141 -2.497  -4.932  1   38.209  ? 101 GLU   B OE2  1 ? 1 
ATOM   1266 H H    . GLU   A 1 89  ? 28.829 -2.881  -3.294  1   44.961  ? 101 GLU   B H    1 c 1 
ATOM   1267 H HA   . GLU   A 1 89  ? 28.098 -1.077  -5.224  1   49.725  ? 101 GLU   B HA   1 c 1 
ATOM   1268 H HB2  . GLU   A 1 89  ? 27.019 -3.195  -5.045  1   46.895  ? 101 GLU   B HB2  1 c 1 
ATOM   1269 H HB3  . GLU   A 1 89  ? 26.412 -2.777  -3.642  1   43.533  ? 101 GLU   B HB3  1 c 1 
ATOM   1270 H HG2  . GLU   A 1 89  ? 25.131 -1.068  -4.714  1   43.276  ? 101 GLU   B HG2  1 c 1 
ATOM   1271 H HG3  . GLU   A 1 89  ? 25.709 -1.532  -6.116  1   46.7    ? 101 GLU   B HG3  1 c 1 
ATOM   1272 N N    . ILE   A 1 90  ? 26.984 0.894   -4.139  1   45.788  ? 102 ILE   B N    1 ? 1 
ATOM   1273 C CA   . ILE   A 1 90  ? 26.259 1.998   -3.506  1   49.523  ? 102 ILE   B CA   1 ? 1 
ATOM   1274 C C    . ILE   A 1 90  ? 24.868 2.024   -4.113  1   47.659  ? 102 ILE   B C    1 ? 1 
ATOM   1275 O O    . ILE   A 1 90  ? 24.733 2.111   -5.322  1   45.993  ? 102 ILE   B O    1 ? 1 
ATOM   1276 C CB   . ILE   A 1 90  ? 26.905 3.403   -3.649  1   51.271  ? 102 ILE   B CB   1 ? 1 
ATOM   1277 C CG1  . ILE   A 1 90  ? 28.331 3.434   -3.042  1   52.187  ? 102 ILE   B CG1  1 ? 1 
ATOM   1278 C CG2  . ILE   A 1 90  ? 25.96  4.459   -3.044  1   49.058  ? 102 ILE   B CG2  1 ? 1 
ATOM   1279 C CD1  . ILE   A 1 90  ? 29.09  4.761   -3.127  1   59.958  ? 102 ILE   B CD1  1 ? 1 
ATOM   1280 H H    . ILE   A 1 90  ? 27.165 0.954   -5.033  1   49.714  ? 102 ILE   B H    1 c 1 
ATOM   1281 H HA   . ILE   A 1 90  ? 26.178 1.801   -2.556  1   46.412  ? 102 ILE   B HA   1 c 1 
ATOM   1282 H HB   . ILE   A 1 90  ? 26.989 3.592   -4.605  1   52.963  ? 102 ILE   B HB   1 c 1 
ATOM   1283 H HG12 . ILE   A 1 90  ? 28.264 3.181   -2.099  1   51.738  ? 102 ILE   B HG12 1 c 1 
ATOM   1284 H HG13 . ILE   A 1 90  ? 28.867 2.747   -3.489  1   54.497  ? 102 ILE   B HG13 1 c 1 
ATOM   1285 H HG21 . ILE   A 1 90  ? 26.412 5.318   -3.002  1   51.133  ? 102 ILE   B HG21 1 c 1 
ATOM   1286 H HG22 . ILE   A 1 90  ? 25.7   4.189   -2.147  1   47.34   ? 102 ILE   B HG22 1 c 1 
ATOM   1287 H HG23 . ILE   A 1 90  ? 25.165 4.544   -3.597  1   48.703  ? 102 ILE   B HG23 1 c 1 
ATOM   1288 H HD11 . ILE   A 1 90  ? 29.185 5.019   -4.064  1   60.545  ? 102 ILE   B HD11 1 c 1 
ATOM   1289 H HD12 . ILE   A 1 90  ? 29.975 4.653   -2.731  1   60.142  ? 102 ILE   B HD12 1 c 1 
ATOM   1290 H HD13 . ILE   A 1 90  ? 28.604 5.457   -2.647  1   57.736  ? 102 ILE   B HD13 1 c 1 
ATOM   1291 N N    . ALA   A 1 91  ? 23.869 2.008   -3.247  1   36.919  ? 103 ALA   B N    1 ? 1 
ATOM   1292 C CA   . ALA   A 1 91  ? 22.468 2.077   -3.666  1   39.876  ? 103 ALA   B CA   1 ? 1 
ATOM   1293 C C    . ALA   A 1 91  ? 21.732 3.182   -2.932  1   35.272  ? 103 ALA   B C    1 ? 1 
ATOM   1294 O O    . ALA   A 1 91  ? 22.071 3.509   -1.8    1   37.83   ? 103 ALA   B O    1 ? 1 
ATOM   1295 C CB   . ALA   A 1 91  ? 21.757 0.803   -3.411  1   37.731  ? 103 ALA   B CB   1 ? 1 
ATOM   1296 H H    . ALA   A 1 91  ? 24.054 1.953   -2.353  1   38.602  ? 103 ALA   B H    1 c 1 
ATOM   1297 H HA   . ALA   A 1 91  ? 22.44  2.278   -4.64   1   39.992  ? 103 ALA   B HA   1 c 1 
ATOM   1298 H HB1  . ALA   A 1 91  ? 22.193 0.083   -3.898  1   38.696  ? 103 ALA   B HB1  1 c 1 
ATOM   1299 H HB2  . ALA   A 1 91  ? 21.773 0.603   -2.46   1   36.39   ? 103 ALA   B HB2  1 c 1 
ATOM   1300 H HB3  . ALA   A 1 91  ? 20.834 0.877   -3.708  1   37.372  ? 103 ALA   B HB3  1 c 1 
ATOM   1301 N N    . HIS   A 1 92  ? 20.651 3.634   -3.555  1   35.472  ? 104 HIS   B N    1 ? 1 
ATOM   1302 C CA   . HIS   A 1 92  ? 19.673 4.491   -2.911  1   33.956  ? 104 HIS   B CA   1 ? 1 
ATOM   1303 C C    . HIS   A 1 92  ? 18.345 3.756   -2.66   1   33.473  ? 104 HIS   B C    1 ? 1 
ATOM   1304 O O    . HIS   A 1 92  ? 17.811 3.127   -3.528  1   35.937  ? 104 HIS   B O    1 ? 1 
ATOM   1305 C CB   . HIS   A 1 92  ? 19.39  5.713   -3.801  1   36.055  ? 104 HIS   B CB   1 ? 1 
ATOM   1306 C CG   . HIS   A 1 92  ? 20.464 6.737   -3.837  1   38.337  ? 104 HIS   B CG   1 ? 1 
ATOM   1307 N ND1  . HIS   A 1 92  ? 20.459 7.868   -4.597  1   45.842  ? 104 HIS   B ND1  1 ? 1 
ATOM   1308 C CD2  . HIS   A 1 92  ? 21.567 6.774   -3.16   1   38.442  ? 104 HIS   B CD2  1 ? 1 
ATOM   1309 C CE1  . HIS   A 1 92  ? 21.595 8.517   -4.404  1   45.939  ? 104 HIS   B CE1  1 ? 1 
ATOM   1310 N NE2  . HIS   A 1 92  ? 22.271 7.852   -3.49   1   39.302  ? 104 HIS   B NE2  1 ? 1 
ATOM   1311 H H    . HIS   A 1 92  ? 20.512 3.398   -4.427  1   36.441  ? 104 HIS   B H    1 c 1 
ATOM   1312 H HA   . HIS   A 1 92  ? 20.033 4.794   -2.045  1   33.809  ? 104 HIS   B HA   1 c 1 
ATOM   1313 H HB2  . HIS   A 1 92  ? 19.225 5.398   -4.716  1   37.125  ? 104 HIS   B HB2  1 c 1 
ATOM   1314 H HB3  . HIS   A 1 92  ? 18.561 6.139   -3.49   1   35.46   ? 104 HIS   B HB3  1 c 1 
ATOM   1315 H HD1  . HIS   A 1 92  ? 19.778 8.138   -5.047  0   30      ? 104 HIS   B HD1  1 c 1 
ATOM   1316 H HD2  . HIS   A 1 92  ? 21.854 6.128   -2.546  1   36.854  ? 104 HIS   B HD2  1 c 1 
ATOM   1317 H HE1  . HIS   A 1 92  ? 21.843 9.338   -4.793  1   47.228  ? 104 HIS   B HE1  1 c 1 
ATOM   1318 H HE2  . HIS   A 1 92  ? 23.116 8.023   -3.229  0   30      ? 104 HIS   B HE2  1 c 1 
ATOM   1319 N N    . LEU   A 1 93  ? 17.84  3.773   -1.421  1   31.513  ? 105 LEU   B N    1 ? 1 
ATOM   1320 C CA   . LEU   A 1 93  ? 16.586 3.179   -1.023  1   30.713  ? 105 LEU   B CA   1 ? 1 
ATOM   1321 C C    . LEU   A 1 93  ? 15.657 4.265   -0.502  1   30.886  ? 105 LEU   B C    1 ? 1 
ATOM   1322 O O    . LEU   A 1 93  ? 16.035 5.108   0.333   1   28.424  ? 105 LEU   B O    1 ? 1 
ATOM   1323 C CB   . LEU   A 1 93  ? 16.787 2.174   0.082   1   29.069  ? 105 LEU   B CB   1 ? 1 
ATOM   1324 C CG   . LEU   A 1 93  ? 17.645 0.95    -0.162  1   33.413  ? 105 LEU   B CG   1 ? 1 
ATOM   1325 C CD1  . LEU   A 1 93  ? 17.612 0.073   1.126   1   37.456  ? 105 LEU   B CD1  1 ? 1 
ATOM   1326 C CD2  . LEU   A 1 93  ? 17.277 0.172   -1.368  1   32.383  ? 105 LEU   B CD2  1 ? 1 
ATOM   1327 H H    . LEU   A 1 93  ? 18.328 4.194   -0.774  1   31.632  ? 105 LEU   B H    1 c 1 
ATOM   1328 H HA   . LEU   A 1 93  ? 16.177 2.737   -1.802  1   31.124  ? 105 LEU   B HA   1 c 1 
ATOM   1329 H HB2  . LEU   A 1 93  ? 17.163 2.654   0.856   1   29.913  ? 105 LEU   B HB2  1 c 1 
ATOM   1330 H HB3  . LEU   A 1 93  ? 15.897 1.865   0.369   1   29.593  ? 105 LEU   B HB3  1 c 1 
ATOM   1331 H HG   . LEU   A 1 93  ? 18.58  1.258   -0.285  1   33.651  ? 105 LEU   B HG   1 c 1 
ATOM   1332 H HD11 . LEU   A 1 93  ? 17.978 0.578   1.872   1   35.757  ? 105 LEU   B HD11 1 c 1 
ATOM   1333 H HD12 . LEU   A 1 93  ? 18.143 -0.729  0.987   1   35.939  ? 105 LEU   B HD12 1 c 1 
ATOM   1334 H HD13 . LEU   A 1 93  ? 16.695 -0.177  1.325   1   35.391  ? 105 LEU   B HD13 1 c 1 
ATOM   1335 H HD21 . LEU   A 1 93  ? 17.348 0.739   -2.153  1   33.936  ? 105 LEU   B HD21 1 c 1 
ATOM   1336 H HD22 . LEU   A 1 93  ? 16.363 -0.147  -1.282  1   32.573  ? 105 LEU   B HD22 1 c 1 
ATOM   1337 H HD23 . LEU   A 1 93  ? 17.876 -0.587  -1.461  1   33.05   ? 105 LEU   B HD23 1 c 1 
ATOM   1338 N N    . LEU   A 1 94  ? 14.431 4.244   -1.038  1   30.594  ? 106 LEU   B N    1 ? 1 
ATOM   1339 C CA   . LEU   A 1 94  ? 13.358 5.072   -0.517  1   30.679  ? 106 LEU   B CA   1 ? 1 
ATOM   1340 C C    . LEU   A 1 94  ? 12.278 4.157   0.045   1   34.901  ? 106 LEU   B C    1 ? 1 
ATOM   1341 O O    . LEU   A 1 94  ? 11.886 3.234   -0.628  1   33.072  ? 106 LEU   B O    1 ? 1 
ATOM   1342 C CB   . LEU   A 1 94  ? 12.832 5.951   -1.627  1   33.778  ? 106 LEU   B CB   1 ? 1 
ATOM   1343 C CG   . LEU   A 1 94  ? 11.57  6.721   -1.272  1   34.578  ? 106 LEU   B CG   1 ? 1 
ATOM   1344 C CD1  . LEU   A 1 94  ? 12.018 7.842   -0.349  1   44.373  ? 106 LEU   B CD1  1 ? 1 
ATOM   1345 C CD2  . LEU   A 1 94  ? 10.934 7.288   -2.484  1   43.77   ? 106 LEU   B CD2  1 ? 1 
ATOM   1346 H H    . LEU   A 1 94  ? 14.259 3.7     -1.752  1   31.144  ? 106 LEU   B H    1 c 1 
ATOM   1347 H HA   . LEU   A 1 94  ? 13.716 5.638   0.212   1   31.69   ? 106 LEU   B HA   1 c 1 
ATOM   1348 H HB2  . LEU   A 1 94  ? 13.536 6.593   -1.878  1   34.356  ? 106 LEU   B HB2  1 c 1 
ATOM   1349 H HB3  . LEU   A 1 94  ? 12.642 5.382   -2.409  1   34.078  ? 106 LEU   B HB3  1 c 1 
ATOM   1350 H HG   . LEU   A 1 94  ? 10.933 6.125   -0.8    1   36.674  ? 106 LEU   B HG   1 c 1 
ATOM   1351 H HD11 . LEU   A 1 94  ? 12.377 7.466   0.472   1   39.818  ? 106 LEU   B HD11 1 c 1 
ATOM   1352 H HD12 . LEU   A 1 94  ? 11.258 8.409   -0.137  1   41.783  ? 106 LEU   B HD12 1 c 1 
ATOM   1353 H HD13 . LEU   A 1 94  ? 12.703 8.373   -0.788  1   41.789  ? 106 LEU   B HD13 1 c 1 
ATOM   1354 H HD21 . LEU   A 1 94  ? 10.648 6.566   -3.069  1   41.711  ? 106 LEU   B HD21 1 c 1 
ATOM   1355 H HD22 . LEU   A 1 94  ? 11.572 7.851   -2.953  1   42.33   ? 106 LEU   B HD22 1 c 1 
ATOM   1356 H HD23 . LEU   A 1 94  ? 10.161 7.819   -2.227  1   42.079  ? 106 LEU   B HD23 1 c 1 
ATOM   1357 N N    . ILE   A 1 95  ? 11.85  4.392   1.292   1   36.081  ? 107 ILE   B N    1 ? 1 
ATOM   1358 C CA   . ILE   A 1 95  ? 11.173 3.433   2.13    1   30.455  ? 107 ILE   B CA   1 ? 1 
ATOM   1359 C C    . ILE   A 1 95  ? 9.907  4.013   2.783   1   31.874  ? 107 ILE   B C    1 ? 1 
ATOM   1360 O O    . ILE   A 1 95  ? 9.975  4.996   3.493   1   30.886  ? 107 ILE   B O    1 ? 1 
ATOM   1361 C CB   . ILE   A 1 95  ? 12.135 3.06    3.245   1   29.732  ? 107 ILE   B CB   1 ? 1 
ATOM   1362 C CG1  . ILE   A 1 95  ? 13.377 2.38    2.675   1   30.381  ? 107 ILE   B CG1  1 ? 1 
ATOM   1363 C CG2  . ILE   A 1 95  ? 11.449 2.15    4.277   1   35.581  ? 107 ILE   B CG2  1 ? 1 
ATOM   1364 C CD1  . ILE   A 1 95  ? 14.603 2.493   3.566   1   31.104  ? 107 ILE   B CD1  1 ? 1 
ATOM   1365 H H    . ILE   A 1 95  ? 11.995 5.226   1.638   1   34.713  ? 107 ILE   B H    1 c 1 
ATOM   1366 H HA   . ILE   A 1 95  ? 10.95  2.638   1.612   1   31.519  ? 107 ILE   B HA   1 c 1 
ATOM   1367 H HB   . ILE   A 1 95  ? 12.415 3.882   3.695   1   31.214  ? 107 ILE   B HB   1 c 1 
ATOM   1368 H HG12 . ILE   A 1 95  ? 13.179 1.432   2.531   1   30.094  ? 107 ILE   B HG12 1 c 1 
ATOM   1369 H HG13 . ILE   A 1 95  ? 13.589 2.774   1.805   1   30.737  ? 107 ILE   B HG13 1 c 1 
ATOM   1370 H HG21 . ILE   A 1 95  ? 12.122 1.738   4.844   1   33.252  ? 107 ILE   B HG21 1 c 1 
ATOM   1371 H HG22 . ILE   A 1 95  ? 10.947 1.456   3.817   1   33.81   ? 107 ILE   B HG22 1 c 1 
ATOM   1372 H HG23 . ILE   A 1 95  ? 10.844 2.675   4.827   1   34.284  ? 107 ILE   B HG23 1 c 1 
ATOM   1373 H HD11 . ILE   A 1 95  ? 14.723 3.422   3.836   1   31.293  ? 107 ILE   B HD11 1 c 1 
ATOM   1374 H HD12 . ILE   A 1 95  ? 15.393 2.193   3.078   1   30.695  ? 107 ILE   B HD12 1 c 1 
ATOM   1375 H HD13 . ILE   A 1 95  ? 14.483 1.938   4.36    1   30.577  ? 107 ILE   B HD13 1 c 1 
ATOM   1376 N N    . LYS   A 1 96  ? 8.756  3.388   2.515   1   33.403  ? 108 LYS   B N    1 ? 1 
ATOM   1377 C CA   . LYS   A 1 96  ? 7.509  3.748   3.142   1   31.566  ? 108 LYS   B CA   1 ? 1 
ATOM   1378 C C    . LYS   A 1 96  ? 7.53   3.239   4.579   1   35.153  ? 108 LYS   B C    1 ? 1 
ATOM   1379 O O    . LYS   A 1 96  ? 8.183  2.227   4.88    1   30.773  ? 108 LYS   B O    1 ? 1 
ATOM   1380 C CB   . LYS   A 1 96  ? 6.363  3.194   2.306   1   33.305  ? 108 LYS   B CB   1 ? 1 
ATOM   1381 C CG   . LYS   A 1 96  ? 6.184  3.88    0.899   1   39.7    ? 108 LYS   B CG   1 ? 1 
ATOM   1382 C CD   . LYS   A 1 96  ? 5.146  3.153   0.031   1   48.316  ? 108 LYS   B CD   1 ? 1 
ATOM   1383 C CE   . LYS   A 1 96  ? 4.987  3.702   -1.405  1   48.747  ? 108 LYS   B CE   1 ? 1 
ATOM   1384 N NZ   . LYS   A 1 96  ? 4.071  2.756   -2.055  1   59.119  ? 108 LYS   B NZ   1 ? 1 
ATOM   1385 H H    . LYS   A 1 96  ? 8.757  2.702   1.91    1   32.412  ? 108 LYS   B H    1 c 1 
ATOM   1386 H HA   . LYS   A 1 96  ? 7.443  4.736   3.153   1   33.423  ? 108 LYS   B HA   1 c 1 
ATOM   1387 H HB2  . LYS   A 1 96  ? 6.51   2.234   2.167   1   33.979  ? 108 LYS   B HB2  1 c 1 
ATOM   1388 H HB3  . LYS   A 1 96  ? 5.527  3.295   2.808   1   35.496  ? 108 LYS   B HB3  1 c 1 
ATOM   1389 H HG2  . LYS   A 1 96  ? 5.9    4.81    1.034   1   40.517  ? 108 LYS   B HG2  1 c 1 
ATOM   1390 H HG3  . LYS   A 1 96  ? 7.049  3.885   0.436   1   38.899  ? 108 LYS   B HG3  1 c 1 
ATOM   1391 H HD2  . LYS   A 1 96  ? 5.386  2.205   -0.019  1   45.866  ? 108 LYS   B HD2  1 c 1 
ATOM   1392 H HD3  . LYS   A 1 96  ? 4.276  3.206   0.483   1   47.549  ? 108 LYS   B HD3  1 c 1 
ATOM   1393 H HE2  . LYS   A 1 96  ? 4.596  4.594   -1.397  1   51.715  ? 108 LYS   B HE2  1 c 1 
ATOM   1394 H HE3  . LYS   A 1 96  ? 5.84   3.72    -1.873  1   49.963  ? 108 LYS   B HE3  1 c 1 
ATOM   1395 H HZ1  . LYS   A 1 96  ? 3.267  2.777   -1.637  1   57.242  ? 108 LYS   B HZ1  1 c 1 
ATOM   1396 H HZ2  . LYS   A 1 96  ? 4.401  1.915   -2.011  1   55.391  ? 108 LYS   B HZ2  1 c 1 
ATOM   1397 H HZ3  . LYS   A 1 96  ? 3.955  2.996   -2.92   1   57.572  ? 108 LYS   B HZ3  1 c 1 
ATOM   1398 N N    . PRO   A 1 97  ? 6.715  3.857   5.458   1   37.603  ? 109 PRO   B N    1 ? 1 
ATOM   1399 C CA   . PRO   A 1 97  ? 6.706  3.508   6.873   1   37.801  ? 109 PRO   B CA   1 ? 1 
ATOM   1400 C C    . PRO   A 1 97  ? 6.488  2.033   7.182   1   35.195  ? 109 PRO   B C    1 ? 1 
ATOM   1401 O O    . PRO   A 1 97  ? 7.077  1.533   8.122   1   38.577  ? 109 PRO   B O    1 ? 1 
ATOM   1402 C CB   . PRO   A 1 97  ? 5.558  4.324   7.475   1   38.602  ? 109 PRO   B CB   1 ? 1 
ATOM   1403 C CG   . PRO   A 1 97  ? 4.853  4.949   6.295   1   40.724  ? 109 PRO   B CG   1 ? 1 
ATOM   1404 C CD   . PRO   A 1 97  ? 5.802  4.963   5.137   1   38.577  ? 109 PRO   B CD   1 ? 1 
ATOM   1405 H HA   . PRO   A 1 97  ? 7.55   3.798   7.277   1   36.392  ? 109 PRO   B HA   1 c 1 
ATOM   1406 H HB2  . PRO   A 1 97  ? 4.948  3.75    7.978   1   40.382  ? 109 PRO   B HB2  1 c 1 
ATOM   1407 H HB3  . PRO   A 1 97  ? 5.904  5.012   8.075   1   39.603  ? 109 PRO   B HB3  1 c 1 
ATOM   1408 H HG2  . PRO   A 1 97  ? 4.054  4.433   6.066   1   41.307  ? 109 PRO   B HG2  1 c 1 
ATOM   1409 H HG3  . PRO   A 1 97  ? 4.575  5.862   6.511   1   41.374  ? 109 PRO   B HG3  1 c 1 
ATOM   1410 H HD2  . PRO   A 1 97  ? 5.335  4.803   4.297   1   39.175  ? 109 PRO   B HD2  1 c 1 
ATOM   1411 H HD3  . PRO   A 1 97  ? 6.287  5.81    5.083   1   38.598  ? 109 PRO   B HD3  1 c 1 
ATOM   1412 N N    . GLU   A 1 98  ? 5.713  1.326   6.371   1   41.926  ? 110 GLU   B N    1 ? 1 
ATOM   1413 C CA   . GLU   A 1 98  ? 5.398  -0.086  6.663   1   42.348  ? 110 GLU   B CA   1 ? 1 
ATOM   1414 C C    . GLU   A 1 98  ? 6.675  -0.917  6.694   1   41.867  ? 110 GLU   B C    1 ? 1 
ATOM   1415 O O    . GLU   A 1 98  ? 6.684  -1.993  7.262   1   36.098  ? 110 GLU   B O    1 ? 1 
ATOM   1416 C CB   . GLU   A 1 98  ? 4.389  -0.643  5.678   1   46.961  ? 110 GLU   B CB   1 ? 1 
ATOM   1417 C CG   . GLU   A 1 98  ? 3.053  0.112   5.722   1   50.04   ? 110 GLU   B CG   1 ? 1 
ATOM   1418 C CD   . GLU   A 1 98  ? 2.924  1.572   5.179   1   55.936  ? 110 GLU   B CD   1 ? 1 
ATOM   1419 O OE1  . GLU   A 1 98  ? 3.731  1.992   4.298   1   43.258  ? 110 GLU   B OE1  1 ? 1 
ATOM   1420 O OE2  . GLU   A 1 98  ? 2.017  2.342   5.688   1   57.405  ? 110 GLU   B OE2  1 ? 1 
ATOM   1421 H H    . GLU   A 1 98  ? 5.379  1.709   5.612   1   40.554  ? 110 GLU   B H    1 c 1 
ATOM   1422 H HA   . GLU   A 1 98  ? 4.988  -0.124  7.565   1   44.498  ? 110 GLU   B HA   1 c 1 
ATOM   1423 H HB2  . GLU   A 1 98  ? 4.763  -0.587  4.774   1   45.436  ? 110 GLU   B HB2  1 c 1 
ATOM   1424 H HB3  . GLU   A 1 98  ? 4.235  -1.589  5.881   1   47.069  ? 110 GLU   B HB3  1 c 1 
ATOM   1425 H HG2  . GLU   A 1 98  ? 2.391  -0.431  5.244   1   52.59   ? 110 GLU   B HG2  1 c 1 
ATOM   1426 H HG3  . GLU   A 1 98  ? 2.754  0.127   6.657   1   52.175  ? 110 GLU   B HG3  1 c 1 
ATOM   1427 N N    . TYR   A 1 99  ? 7.733  -0.448  6.015   1   35.591  ? 111 TYR   B N    1 ? 1 
ATOM   1428 C CA   . TYR   A 1 99  ? 8.998  -1.143  5.943   1   32.703  ? 111 TYR   B CA   1 ? 1 
ATOM   1429 C C    . TYR   A 1 99  ? 10.076 -0.479  6.798   1   33.953  ? 111 TYR   B C    1 ? 1 
ATOM   1430 O O    . TYR   A 1 99  ? 11.276 -0.847  6.737   1   31.703  ? 111 TYR   B O    1 ? 1 
ATOM   1431 C CB   . TYR   A 1 99  ? 9.445  -1.325  4.481   1   31.589  ? 111 TYR   B CB   1 ? 1 
ATOM   1432 C CG   . TYR   A 1 99  ? 8.556  -2.229  3.661   1   32.157  ? 111 TYR   B CG   1 ? 1 
ATOM   1433 C CD1  . TYR   A 1 99  ? 7.371  -1.751  3.145   1   33.893  ? 111 TYR   B CD1  1 ? 1 
ATOM   1434 C CD2  . TYR   A 1 99  ? 8.789  -3.603  3.595   1   37.566  ? 111 TYR   B CD2  1 ? 1 
ATOM   1435 C CE1  . TYR   A 1 99  ? 6.502  -2.582  2.469   1   37.915  ? 111 TYR   B CE1  1 ? 1 
ATOM   1436 C CE2  . TYR   A 1 99  ? 7.883  -4.459  3.018   1   36.787  ? 111 TYR   B CE2  1 ? 1 
ATOM   1437 C CZ   . TYR   A 1 99  ? 6.804  -3.931  2.364   1   34.782  ? 111 TYR   B CZ   1 ? 1 
ATOM   1438 O OH   . TYR   A 1 99  ? 5.853  -4.69   1.821   1   41.445  ? 111 TYR   B OH   1 ? 1 
ATOM   1439 H H    . TYR   A 1 99  ? 7.65   0.337   5.555   1   36.092  ? 111 TYR   B H    1 c 1 
ATOM   1440 H HA   . TYR   A 1 99  ? 8.854  -2.053  6.315   1   33.862  ? 111 TYR   B HA   1 c 1 
ATOM   1441 H HB2  . TYR   A 1 99  ? 9.478  -0.441  4.054   1   31.298  ? 111 TYR   B HB2  1 c 1 
ATOM   1442 H HB3  . TYR   A 1 99  ? 10.355 -1.694  4.478   1   30.693  ? 111 TYR   B HB3  1 c 1 
ATOM   1443 H HD1  . TYR   A 1 99  ? 7.19   -0.825  3.181   1   34.313  ? 111 TYR   B HD1  1 c 1 
ATOM   1444 H HD2  . TYR   A 1 99  ? 9.551  -3.962  4.021   1   34.872  ? 111 TYR   B HD2  1 c 1 
ATOM   1445 H HE1  . TYR   A 1 99  ? 5.712  -2.239  2.086   1   37.87   ? 111 TYR   B HE1  1 c 1 
ATOM   1446 H HE2  . TYR   A 1 99  ? 8.084  -5.375  2.933   1   36.931  ? 111 TYR   B HE2  1 c 1 
ATOM   1447 H HH   . TYR   A 1 99  ? 5.196  -4.232  1.426   0   30      ? 111 TYR   B HH   1 c 1 
ATOM   1448 N N    . ALA   A 1 100 ? 9.63   0.448   7.657   1   32.997  ? 112 ALA   B N    1 ? 1 
ATOM   1449 C CA   . ALA   A 1 100 ? 10.52  1.188   8.529   1   34.13   ? 112 ALA   B CA   1 ? 1 
ATOM   1450 C C    . ALA   A 1 100 ? 10.006 1.212   9.971   1   34.799  ? 112 ALA   B C    1 ? 1 
ATOM   1451 O O    . ALA   A 1 100 ? 10.081 0.176   10.643  1   33.889  ? 112 ALA   B O    1 ? 1 
ATOM   1452 C CB   . ALA   A 1 100 ? 10.732 2.555   7.944   1   32.67   ? 112 ALA   B CB   1 ? 1 
ATOM   1453 H H    . ALA   A 1 100 ? 8.734  0.617   7.709   1   34.672  ? 112 ALA   B H    1 c 1 
ATOM   1454 H HA   . ALA   A 1 100 ? 11.396 0.717   8.537   1   32.737  ? 112 ALA   B HA   1 c 1 
ATOM   1455 H HB1  . ALA   A 1 100 ? 11.254 2.483   7.128   1   32.061  ? 112 ALA   B HB1  1 c 1 
ATOM   1456 H HB2  . ALA   A 1 100 ? 9.873  2.962   7.739   1   33.679  ? 112 ALA   B HB2  1 c 1 
ATOM   1457 H HB3  . ALA   A 1 100 ? 11.21  3.114   8.58    1   33.493  ? 112 ALA   B HB3  1 c 1 
ATOM   1458 N N    . TYR   A 1 101 ? 9.461  2.351   10.439  1   31.407  ? 113 TYR   B N    1 ? 1 
ATOM   1459 C CA   . TYR   A 1 101 ? 9.061  2.511   11.833  1   37.856  ? 113 TYR   B CA   1 ? 1 
ATOM   1460 C C    . TYR   A 1 101 ? 7.556  2.618   12.036  1   39.681  ? 113 TYR   B C    1 ? 1 
ATOM   1461 O O    . TYR   A 1 101 ? 7.139  2.739   13.176  1   39.603  ? 113 TYR   B O    1 ? 1 
ATOM   1462 C CB   . TYR   A 1 101 ? 9.744  3.689   12.529  1   36.609  ? 113 TYR   B CB   1 ? 1 
ATOM   1463 C CG   . TYR   A 1 101 ? 11.233 3.422   12.612  1   33.436  ? 113 TYR   B CG   1 ? 1 
ATOM   1464 C CD1  . TYR   A 1 101 ? 11.77  2.593   13.577  1   36.164  ? 113 TYR   B CD1  1 ? 1 
ATOM   1465 C CD2  . TYR   A 1 101 ? 12.095 3.898   11.648  1   35.422  ? 113 TYR   B CD2  1 ? 1 
ATOM   1466 C CE1  . TYR   A 1 101 ? 13.136 2.377   13.653  1   32.116  ? 113 TYR   B CE1  1 ? 1 
ATOM   1467 C CE2  . TYR   A 1 101 ? 13.465 3.642   11.675  1   34.12   ? 113 TYR   B CE2  1 ? 1 
ATOM   1468 C CZ   . TYR   A 1 101 ? 14.007 2.87    12.682  1   33.485  ? 113 TYR   B CZ   1 ? 1 
ATOM   1469 O OH   . TYR   A 1 101 ? 15.409 2.699   12.692  1   32.144  ? 113 TYR   B OH   1 ? 1 
ATOM   1470 H H    . TYR   A 1 101 ? 9.329  3.052   9.868   1   33.074  ? 113 TYR   B H    1 c 1 
ATOM   1471 H HA   . TYR   A 1 101 ? 9.354  1.692   12.31   1   36.893  ? 113 TYR   B HA   1 c 1 
ATOM   1472 H HB2  . TYR   A 1 101 ? 9.586  4.508   12.012  1   36.449  ? 113 TYR   B HB2  1 c 1 
ATOM   1473 H HB3  . TYR   A 1 101 ? 9.377  3.793   13.434  1   38.693  ? 113 TYR   B HB3  1 c 1 
ATOM   1474 H HD1  . TYR   A 1 101 ? 11.212 2.258   14.261  1   36.499  ? 113 TYR   B HD1  1 c 1 
ATOM   1475 H HD2  . TYR   A 1 101 ? 11.749 4.433   10.953  1   33.732  ? 113 TYR   B HD2  1 c 1 
ATOM   1476 H HE1  . TYR   A 1 101 ? 13.479 1.839   14.347  1   34.733  ? 113 TYR   B HE1  1 c 1 
ATOM   1477 H HE2  . TYR   A 1 101 ? 14.027 4.023   11.023  1   32.975  ? 113 TYR   B HE2  1 c 1 
ATOM   1478 H HH   . TYR   A 1 101 ? 15.547 2.177   13.416  0   30      ? 113 TYR   B HH   1 c 1 
ATOM   1479 N N    . GLY   A 1 102 ? 6.774  2.509   10.961  1   38.702  ? 114 GLY   B N    1 ? 1 
ATOM   1480 C CA   . GLY   A 1 102 ? 5.356  2.241   11.031  1   41.123  ? 114 GLY   B CA   1 ? 1 
ATOM   1481 C C    . GLY   A 1 102 ? 4.574  3.439   11.536  1   47.646  ? 114 GLY   B C    1 ? 1 
ATOM   1482 O O    . GLY   A 1 102 ? 5.093  4.573   11.565  1   42.478  ? 114 GLY   B O    1 ? 1 
ATOM   1483 H H    . GLY   A 1 102 ? 7.147  2.617   10.134  1   37.202  ? 114 GLY   B H    1 c 1 
ATOM   1484 H HA2  . GLY   A 1 102 ? 5.032  1.992   10.134  1   41.19   ? 114 GLY   B HA2  1 c 1 
ATOM   1485 H HA3  . GLY   A 1 102 ? 5.206  1.473   11.631  1   42.993  ? 114 GLY   B HA3  1 c 1 
ATOM   1486 N N    . SER   A 1 103 ? 3.324  3.113   11.875  1   48.621  ? 115 SER   B N    1 ? 1 
ATOM   1487 C CA   . SER   A 1 103 ? 2.372  4.041   12.412  1   55.964  ? 115 SER   B CA   1 ? 1 
ATOM   1488 C C    . SER   A 1 103 ? 2.842  4.595   13.736  1   57.761  ? 115 SER   B C    1 ? 1 
ATOM   1489 O O    . SER   A 1 103 ? 2.588  5.75    14.047  1   58.178  ? 115 SER   B O    1 ? 1 
ATOM   1490 C CB   . SER   A 1 103 ? 1.011  3.397   12.568  1   62.254  ? 115 SER   B CB   1 ? 1 
ATOM   1491 O OG   . SER   A 1 103 ? 0.443  3.299   11.264  1   66.861  ? 115 SER   B OG   1 ? 1 
ATOM   1492 H H    . SER   A 1 103 ? 3.058  2.246   11.757  1   50.169  ? 115 SER   B H    1 c 1 
ATOM   1493 H HA   . SER   A 1 103 ? 2.289  4.794   11.78   1   54.952  ? 115 SER   B HA   1 c 1 
ATOM   1494 H HB2  . SER   A 1 103 ? 1.103  2.508   12.961  1   63.01   ? 115 SER   B HB2  1 c 1 
ATOM   1495 H HB3  . SER   A 1 103 ? 0.443  3.947   13.14   1   65.122  ? 115 SER   B HB3  1 c 1 
ATOM   1496 H HG   . SER   A 1 103 ? -0.365 2.986   11.294  0   30      ? 115 SER   B HG   1 c 1 
ATOM   1497 N N    . ALA   A 1 104 ? 3.485  3.751   14.54   1   60.672  ? 116 ALA   B N    1 ? 1 
ATOM   1498 C CA   . ALA   A 1 104 ? 3.871  4.157   15.882  1   62.379  ? 116 ALA   B CA   1 ? 1 
ATOM   1499 C C    . ALA   A 1 104 ? 5.091  5.071   15.827  1   55.453  ? 116 ALA   B C    1 ? 1 
ATOM   1500 O O    . ALA   A 1 104 ? 5.365  5.848   16.74   1   54.946  ? 116 ALA   B O    1 ? 1 
ATOM   1501 C CB   . ALA   A 1 104 ? 4.167  2.913   16.739  1   62.524  ? 116 ALA   B CB   1 ? 1 
ATOM   1502 H H    . ALA   A 1 104 ? 3.681  2.905   14.257  1   58.482  ? 116 ALA   B H    1 c 1 
ATOM   1503 H HA   . ALA   A 1 104 ? 3.116  4.664   16.29   1   63.959  ? 116 ALA   B HA   1 c 1 
ATOM   1504 H HB1  . ALA   A 1 104 ? 3.371  2.357   16.792  1   64.3    ? 116 ALA   B HB1  1 c 1 
ATOM   1505 H HB2  . ALA   A 1 104 ? 4.889  2.402   16.335  1   60.437  ? 116 ALA   B HB2  1 c 1 
ATOM   1506 H HB3  . ALA   A 1 104 ? 4.428  3.187   17.634  1   64.912  ? 116 ALA   B HB3  1 c 1 
ATOM   1507 N N    . GLY   A 1 105 ? 5.897  4.899   14.8    1   54.286  ? 117 GLY   B N    1 ? 1 
ATOM   1508 C CA   . GLY   A 1 105 ? 7.155  5.628   14.708  1   53.006  ? 117 GLY   B CA   1 ? 1 
ATOM   1509 C C    . GLY   A 1 105 ? 8.107  5.193   15.814  1   57.153  ? 117 GLY   B C    1 ? 1 
ATOM   1510 O O    . GLY   A 1 105 ? 7.979  4.083   16.343  1   55.261  ? 117 GLY   B O    1 ? 1 
ATOM   1511 H H    . GLY   A 1 105 ? 5.678  4.31    14.137  1   52.264  ? 117 GLY   B H    1 c 1 
ATOM   1512 H HA2  . GLY   A 1 105 ? 7.567  5.456   13.832  1   51.199  ? 117 GLY   B HA2  1 c 1 
ATOM   1513 H HA3  . GLY   A 1 105 ? 6.979  6.596   14.781  1   54.716  ? 117 GLY   B HA3  1 c 1 
ATOM   1514 N N    . SER   A 1 106 ? 9.137  6.008   16.028  1   50.912  ? 118 SER   B N    1 ? 1 
ATOM   1515 C CA   . SER   A 1 106 ? 10.091 5.721   17.065  1   56.273  ? 118 SER   B CA   1 ? 1 
ATOM   1516 C C    . SER   A 1 106 ? 10.349 7.058   17.719  1   60.951  ? 118 SER   B C    1 ? 1 
ATOM   1517 O O    . SER   A 1 106 ? 11.393 7.665   17.493  1   57.705  ? 118 SER   B O    1 ? 1 
ATOM   1518 C CB   . SER   A 1 106 ? 11.349 5.004   16.602  1   53.186  ? 118 SER   B CB   1 ? 1 
ATOM   1519 O OG   . SER   A 1 106 ? 12.013 4.353   17.686  1   50.045  ? 118 SER   B OG   1 ? 1 
ATOM   1520 H H    . SER   A 1 106 ? 9.24   6.759   15.517  1   52.513  ? 118 SER   B H    1 c 1 
ATOM   1521 H HA   . SER   A 1 106 ? 9.647  5.141   17.734  1   57.52   ? 118 SER   B HA   1 c 1 
ATOM   1522 H HB2  . SER   A 1 106 ? 11.108 4.341   15.927  1   49.782  ? 118 SER   B HB2  1 c 1 
ATOM   1523 H HB3  . SER   A 1 106 ? 11.956 5.647   16.189  1   51.177  ? 118 SER   B HB3  1 c 1 
ATOM   1524 H HG   . SER   A 1 106 ? 12.671 4.046   17.436  0   30      ? 118 SER   B HG   1 c 1 
ATOM   1525 N N    . LEU   A 1 107 ? 9.306  7.412   18.492  1   65.899  ? 119 LEU   B N    1 ? 1 
ATOM   1526 C CA   . LEU   A 1 107 ? 8.969  8.754   18.911  1   78.365  ? 119 LEU   B CA   1 ? 1 
ATOM   1527 C C    . LEU   A 1 107 ? 10.02  9.21    19.92   1   84.77   ? 119 LEU   B C    1 ? 1 
ATOM   1528 O O    . LEU   A 1 107 ? 10.199 8.53    20.94   1   80.174  ? 119 LEU   B O    1 ? 1 
ATOM   1529 C CB   . LEU   A 1 107 ? 7.572  8.77    19.576  1   81.318  ? 119 LEU   B CB   1 ? 1 
ATOM   1530 C CG   . LEU   A 1 107 ? 6.264  8.886   18.752  1   74.998  ? 119 LEU   B CG   1 ? 1 
ATOM   1531 C CD1  . LEU   A 1 107 ? 5.007  9.129   19.676  1   73.402  ? 119 LEU   B CD1  1 ? 1 
ATOM   1532 C CD2  . LEU   A 1 107 ? 6.342  9.981   17.684  1   65.992  ? 119 LEU   B CD2  1 ? 1 
ATOM   1533 H H    . LEU   A 1 107 ? 8.761  6.738   18.782  1   68.026  ? 119 LEU   B H    1 c 1 
ATOM   1534 H HA   . LEU   A 1 107 ? 8.976  9.343   18.121  1   75.048  ? 119 LEU   B HA   1 c 1 
ATOM   1535 H HB2  . LEU   A 1 107 ? 7.502  7.962   20.133  1   81.097  ? 119 LEU   B HB2  1 c 1 
ATOM   1536 H HB3  . LEU   A 1 107 ? 7.571  9.51    20.227  1   83.309  ? 119 LEU   B HB3  1 c 1 
ATOM   1537 H HG   . LEU   A 1 107 ? 6.126  8.023   18.282  1   70.907  ? 119 LEU   B HG   1 c 1 
ATOM   1538 H HD11 . LEU   A 1 107 ? 4.803  8.313   20.16   1   76.08   ? 119 LEU   B HD11 1 c 1 
ATOM   1539 H HD12 . LEU   A 1 107 ? 4.243  9.376   19.126  1   74.704  ? 119 LEU   B HD12 1 c 1 
ATOM   1540 H HD13 . LEU   A 1 107 ? 5.197  9.844   20.307  1   77.863  ? 119 LEU   B HD13 1 c 1 
ATOM   1541 H HD21 . LEU   A 1 107 ? 7.071  9.787   17.071  1   65.249  ? 119 LEU   B HD21 1 c 1 
ATOM   1542 H HD22 . LEU   A 1 107 ? 6.499  10.84   18.111  1   70.235  ? 119 LEU   B HD22 1 c 1 
ATOM   1543 H HD23 . LEU   A 1 107 ? 5.506  10.013  17.19   1   67.565  ? 119 LEU   B HD23 1 c 1 
ATOM   1544 N N    . PRO   A 1 108 ? 10.598 10.429  19.795  1   87.555  ? 120 PRO   B N    1 ? 1 
ATOM   1545 C CA   . PRO   A 1 108 ? 10.335 11.327  18.678  1   83.026  ? 120 PRO   B CA   1 ? 1 
ATOM   1546 C C    . PRO   A 1 108 ? 11.406 11.334  17.599  1   77.89   ? 120 PRO   B C    1 ? 1 
ATOM   1547 O O    . PRO   A 1 108 ? 11.24  12.037  16.616  1   76.747  ? 120 PRO   B O    1 ? 1 
ATOM   1548 C CB   . PRO   A 1 108 ? 10.272 12.694  19.342  1   91.974  ? 120 PRO   B CB   1 ? 1 
ATOM   1549 C CG   . PRO   A 1 108 ? 11.266 12.555  20.494  1   100.936 ? 120 PRO   B CG   1 ? 1 
ATOM   1550 C CD   . PRO   A 1 108 ? 11.378 11.085  20.851  1   94.838  ? 120 PRO   B CD   1 ? 1 
ATOM   1551 H HA   . PRO   A 1 108 ? 9.467  11.123  18.279  1   82.753  ? 120 PRO   B HA   1 c 1 
ATOM   1552 H HB2  . PRO   A 1 108 ? 10.542 13.402  18.726  1   91.355  ? 120 PRO   B HB2  1 c 1 
ATOM   1553 H HB3  . PRO   A 1 108 ? 9.372  12.881  19.675  1   93.946  ? 120 PRO   B HB3  1 c 1 
ATOM   1554 H HG2  . PRO   A 1 108 ? 12.142 12.901  20.228  1   98.196  ? 120 PRO   B HG2  1 c 1 
ATOM   1555 H HG3  . PRO   A 1 108 ? 10.959 13.065  21.27   1   102.39  ? 120 PRO   B HG3  1 c 1 
ATOM   1556 H HD2  . PRO   A 1 108 ? 12.306 10.782  20.841  1   94.395  ? 120 PRO   B HD2  1 c 1 
ATOM   1557 H HD3  . PRO   A 1 108 ? 10.989 10.907  21.724  1   98.071  ? 120 PRO   B HD3  1 c 1 
ATOM   1558 N N    . LYS   A 1 109 ? 12.484 10.551  17.764  1   73.958  ? 121 LYS   B N    1 ? 1 
ATOM   1559 C CA   . LYS   A 1 109 ? 13.484 10.267  16.71   1   66.025  ? 121 LYS   B CA   1 ? 1 
ATOM   1560 C C    . LYS   A 1 109 ? 12.922 10.146  15.264  1   60.416  ? 121 LYS   B C    1 ? 1 
ATOM   1561 O O    . LYS   A 1 109 ? 13.334 10.726  14.223  1   52.436  ? 121 LYS   B O    1 ? 1 
ATOM   1562 C CB   . LYS   A 1 109 ? 13.975 8.839   17.059  1   55.309  ? 121 LYS   B CB   1 ? 1 
ATOM   1563 H H    . LYS   A 1 109 ? 12.615 10.172  18.585  1   75.471  ? 121 LYS   B H    1 c 1 
ATOM   1564 H HA   . LYS   A 1 109 ? 14.216 10.934  16.749  1   65.911  ? 121 LYS   B HA   1 c 1 
ATOM   1565 H HB2  . LYS   A 1 109 ? 15.308 9.468   16.951  0   30      ? 121 LYS   B HB2  1 c 1 
ATOM   1566 H HB3  . LYS   A 1 109 ? 13.784 8.448   17.25   0   30      ? 121 LYS   B HB3  1 c 1 
ATOM   1567 N N    . ILE   A 1 110 ? 11.954 9.249   15.169  1   56.197  ? 122 ILE   B N    1 ? 1 
ATOM   1568 C CA   . ILE   A 1 110 ? 11.316 8.993   13.906  1   49.592  ? 122 ILE   B CA   1 ? 1 
ATOM   1569 C C    . ILE   A 1 110 ? 9.859  9.301   14.12   1   48.997  ? 122 ILE   B C    1 ? 1 
ATOM   1570 O O    . ILE   A 1 110 ? 9.184  8.612   14.897  1   51.395  ? 122 ILE   B O    1 ? 1 
ATOM   1571 C CB   . ILE   A 1 110 ? 11.469 7.521   13.483  1   44.527  ? 122 ILE   B CB   1 ? 1 
ATOM   1572 C CG1  . ILE   A 1 110 ? 12.889 7.03    13.516  1   42.171  ? 122 ILE   B CG1  1 ? 1 
ATOM   1573 C CG2  . ILE   A 1 110 ? 10.785 7.294   12.132  1   46.303  ? 122 ILE   B CG2  1 ? 1 
ATOM   1574 C CD1  . ILE   A 1 110 ? 13.841 7.559   12.465  1   37.485  ? 122 ILE   B CD1  1 ? 1 
ATOM   1575 H H    . ILE   A 1 110 ? 11.671 8.793   15.909  1   57.218  ? 122 ILE   B H    1 c 1 
ATOM   1576 H HA   . ILE   A 1 110 ? 11.686 9.574   13.217  1   48.679  ? 122 ILE   B HA   1 c 1 
ATOM   1577 H HB   . ILE   A 1 110 ? 10.98  6.988   14.139  1   46.373  ? 122 ILE   B HB   1 c 1 
ATOM   1578 H HG12 . ILE   A 1 110 ? 13.263 7.241   14.395  1   43.811  ? 122 ILE   B HG12 1 c 1 
ATOM   1579 H HG13 . ILE   A 1 110 ? 12.87  6.054   13.439  1   40.502  ? 122 ILE   B HG13 1 c 1 
ATOM   1580 H HG21 . ILE   A 1 110 ? 11.027 6.419   11.789  1   43.221  ? 122 ILE   B HG21 1 c 1 
ATOM   1581 H HG22 . ILE   A 1 110 ? 11.071 7.977   11.503  1   44.512  ? 122 ILE   B HG22 1 c 1 
ATOM   1582 H HG23 . ILE   A 1 110 ? 9.821  7.34    12.241  1   45.686  ? 122 ILE   B HG23 1 c 1 
ATOM   1583 H HD11 . ILE   A 1 110 ? 13.567 7.245   11.583  1   36.509  ? 122 ILE   B HD11 1 c 1 
ATOM   1584 H HD12 . ILE   A 1 110 ? 14.743 7.241   12.656  1   38.433  ? 122 ILE   B HD12 1 c 1 
ATOM   1585 H HD13 . ILE   A 1 110 ? 13.832 8.535   12.479  1   39.7    ? 122 ILE   B HD13 1 c 1 
ATOM   1586 N N    . PRO   A 1 111 ? 9.281  10.279  13.393  1   49.371  ? 123 PRO   B N    1 ? 1 
ATOM   1587 C CA   . PRO   A 1 111 ? 7.872  10.555  13.605  1   49.127  ? 123 PRO   B CA   1 ? 1 
ATOM   1588 C C    . PRO   A 1 111 ? 7.018  9.41    13.083  1   46.057  ? 123 PRO   B C    1 ? 1 
ATOM   1589 O O    . PRO   A 1 111 ? 7.469  8.505   12.355  1   44.567  ? 123 PRO   B O    1 ? 1 
ATOM   1590 C CB   . PRO   A 1 111 ? 7.652  11.917  12.922  1   52.329  ? 123 PRO   B CB   1 ? 1 
ATOM   1591 C CG   . PRO   A 1 111 ? 8.768  12.069  11.959  1   48.745  ? 123 PRO   B CG   1 ? 1 
ATOM   1592 C CD   . PRO   A 1 111 ? 9.903  11.101  12.352  1   47.242  ? 123 PRO   B CD   1 ? 1 
ATOM   1593 H HA   . PRO   A 1 111 ? 7.71   10.659  14.566  1   52.052  ? 123 PRO   B HA   1 c 1 
ATOM   1594 H HB2  . PRO   A 1 111 ? 6.791  11.936  12.46   1   51.436  ? 123 PRO   B HB2  1 c 1 
ATOM   1595 H HB3  . PRO   A 1 111 ? 7.664  12.639  13.581  1   54.03   ? 123 PRO   B HB3  1 c 1 
ATOM   1596 H HG2  . PRO   A 1 111 ? 8.459  11.867  11.053  1   47.411  ? 123 PRO   B HG2  1 c 1 
ATOM   1597 H HG3  . PRO   A 1 111 ? 9.098  12.989  11.969  1   50.451  ? 123 PRO   B HG3  1 c 1 
ATOM   1598 H HD2  . PRO   A 1 111 ? 10.183 10.55   11.595  1   45.173  ? 123 PRO   B HD2  1 c 1 
ATOM   1599 H HD3  . PRO   A 1 111 ? 10.676 11.583  12.705  1   48.613  ? 123 PRO   B HD3  1 c 1 
ATOM   1600 N N    . SER   A 1 112 ? 5.768  9.479   13.492  1   46.096  ? 124 SER   B N    1 ? 1 
ATOM   1601 C CA   . SER   A 1 112 ? 4.726  8.604   13.039  1   47.165  ? 124 SER   B CA   1 ? 1 
ATOM   1602 C C    . SER   A 1 112 ? 4.67   8.609   11.517  1   45.341  ? 124 SER   B C    1 ? 1 
ATOM   1603 O O    . SER   A 1 112 ? 4.611  9.691   10.919  1   43.727  ? 124 SER   B O    1 ? 1 
ATOM   1604 C CB   . SER   A 1 112 ? 3.496  9.152   13.645  1   53.315  ? 124 SER   B CB   1 ? 1 
ATOM   1605 O OG   . SER   A 1 112 ? 2.42   8.286   13.403  1   61.747  ? 124 SER   B OG   1 ? 1 
ATOM   1606 H H    . SER   A 1 112 ? 5.551  10.128  14.098  1   49.449  ? 124 SER   B H    1 c 1 
ATOM   1607 H HA   . SER   A 1 112 ? 4.892  7.686   13.373  1   46.949  ? 124 SER   B HA   1 c 1 
ATOM   1608 H HB2  . SER   A 1 112 ? 3.621  9.253   14.609  1   56.243  ? 124 SER   B HB2  1 c 1 
ATOM   1609 H HB3  . SER   A 1 112 ? 3.305  10.03   13.263  1   54.817  ? 124 SER   B HB3  1 c 1 
ATOM   1610 H HG   . SER   A 1 112 ? 1.588  8.406   13.552  0   30      ? 124 SER   B HG   1 c 1 
ATOM   1611 N N    . ASN   A 1 113 ? 4.67   7.423   10.908  1   44.99   ? 125 ASN   B N    1 ? 1 
ATOM   1612 C CA   . ASN   A 1 113 ? 4.441  7.217   9.496   1   44.607  ? 125 ASN   B CA   1 ? 1 
ATOM   1613 C C    . ASN   A 1 113 ? 5.441  7.955   8.628   1   43.227  ? 125 ASN   B C    1 ? 1 
ATOM   1614 O O    . ASN   A 1 113 ? 5.069  8.409   7.553   1   40.312  ? 125 ASN   B O    1 ? 1 
ATOM   1615 C CB   . ASN   A 1 113 ? 3.038  7.655   9.092   1   49.206  ? 125 ASN   B CB   1 ? 1 
ATOM   1616 C CG   . ASN   A 1 113 ? 1.995  6.752   9.707   1   46.459  ? 125 ASN   B CG   1 ? 1 
ATOM   1617 O OD1  . ASN   A 1 113 ? 1.024  7.24    10.26   1   52.538  ? 125 ASN   B OD1  1 ? 1 
ATOM   1618 N ND2  . ASN   A 1 113 ? 2.042  5.468   9.412   1   48.315  ? 125 ASN   B ND2  1 ? 1 
ATOM   1619 H H    . ASN   A 1 113 ? 4.828  6.683   11.421  1   44.758  ? 125 ASN   B H    1 c 1 
ATOM   1620 H HA   . ASN   A 1 113 ? 4.519  6.256   9.311   1   43.752  ? 125 ASN   B HA   1 c 1 
ATOM   1621 H HB2  . ASN   A 1 113 ? 2.884  8.576   9.382   1   48.85   ? 125 ASN   B HB2  1 c 1 
ATOM   1622 H HB3  . ASN   A 1 113 ? 2.953  7.623   8.118   1   46.611  ? 125 ASN   B HB3  1 c 1 
ATOM   1623 H HD21 . ASN   A 1 113 ? 1.424  4.919   9.736   1   48.817  ? 125 ASN   B HD21 1 c 1 
ATOM   1624 H HD22 . ASN   A 1 113 ? 2.676  5.151   8.88    1   45.388  ? 125 ASN   B HD22 1 c 1 
ATOM   1625 N N    . ALA   A 1 114 ? 6.721  7.894   9.026   1   40.607  ? 126 ALA   B N    1 ? 1 
ATOM   1626 C CA   . ALA   A 1 114 ? 7.785  8.544   8.304   1   40.4    ? 126 ALA   B CA   1 ? 1 
ATOM   1627 C C    . ALA   A 1 114 ? 8.253  7.764   7.066   1   35.726  ? 126 ALA   B C    1 ? 1 
ATOM   1628 O O    . ALA   A 1 114 ? 8.449  6.582   7.117   1   35.584  ? 126 ALA   B O    1 ? 1 
ATOM   1629 C CB   . ALA   A 1 114 ? 8.9    8.739   9.24    1   40.167  ? 126 ALA   B CB   1 ? 1 
ATOM   1630 H H    . ALA   A 1 114 ? 6.931  7.417   9.777   1   41.325  ? 126 ALA   B H    1 c 1 
ATOM   1631 H HA   . ALA   A 1 114 ? 7.456  9.436   8.004   1   40.704  ? 126 ALA   B HA   1 c 1 
ATOM   1632 H HB1  . ALA   A 1 114 ? 8.598  9.257   10.004  1   42.124  ? 126 ALA   B HB1  1 c 1 
ATOM   1633 H HB2  . ALA   A 1 114 ? 9.226  7.876   9.545   1   39.444  ? 126 ALA   B HB2  1 c 1 
ATOM   1634 H HB3  . ALA   A 1 114 ? 9.621  9.215   8.794   1   39.895  ? 126 ALA   B HB3  1 c 1 
ATOM   1635 N N    . THR   A 1 115 ? 8.375  8.431   5.907   1   31.038  ? 127 THR   B N    1 ? 1 
ATOM   1636 C CA   . THR   A 1 115 ? 9.186  7.909   4.831   1   30.719  ? 127 THR   B CA   1 ? 1 
ATOM   1637 C C    . THR   A 1 115 ? 10.671 8.198   5.047   1   29.466  ? 127 THR   B C    1 ? 1 
ATOM   1638 O O    . THR   A 1 115 ? 11.065 9.326   5.344   1   29.117  ? 127 THR   B O    1 ? 1 
ATOM   1639 C CB   . THR   A 1 115 ? 8.697  8.487   3.521   1   31.404  ? 127 THR   B CB   1 ? 1 
ATOM   1640 O OG1  . THR   A 1 115 ? 7.484  7.848   3.222   1   34.44   ? 127 THR   B OG1  1 ? 1 
ATOM   1641 C CG2  . THR   A 1 115 ? 9.511  8.08    2.32    1   33.002  ? 127 THR   B CG2  1 ? 1 
ATOM   1642 H H    . THR   A 1 115 ? 7.941  9.227   5.793   1   33.62   ? 127 THR   B H    1 c 1 
ATOM   1643 H HA   . THR   A 1 115 ? 9.059  6.938   4.799   1   29.532  ? 127 THR   B HA   1 c 1 
ATOM   1644 H HB   . THR   A 1 115 ? 8.567  9.464   3.565   1   33.737  ? 127 THR   B HB   1 c 1 
ATOM   1645 H HG1  . THR   A 1 115 ? 7.584  6.956   3.188   0   30      ? 127 THR   B HG1  1 c 1 
ATOM   1646 H HG21 . THR   A 1 115 ? 9.077  8.399   1.511   1   33.178  ? 127 THR   B HG21 1 c 1 
ATOM   1647 H HG22 . THR   A 1 115 ? 9.582  7.113   2.286   1   31.234  ? 127 THR   B HG22 1 c 1 
ATOM   1648 H HG23 . THR   A 1 115 ? 10.4   8.468   2.381   1   32.077  ? 127 THR   B HG23 1 c 1 
ATOM   1649 N N    . LEU   A 1 116 ? 11.497 7.209   4.772   1   29.072  ? 128 LEU   B N    1 ? 1 
ATOM   1650 C CA   . LEU   A 1 116 ? 12.941 7.302   4.935   1   30.447  ? 128 LEU   B CA   1 ? 1 
ATOM   1651 C C    . LEU   A 1 116 ? 13.67  7.134   3.602   1   30.662  ? 128 LEU   B C    1 ? 1 
ATOM   1652 O O    . LEU   A 1 116 ? 13.224 6.419   2.723   1   29.285  ? 128 LEU   B O    1 ? 1 
ATOM   1653 C CB   . LEU   A 1 116 ? 13.517 6.258   5.877   1   28.693  ? 128 LEU   B CB   1 ? 1 
ATOM   1654 C CG   . LEU   A 1 116 ? 12.875 6.097   7.267   1   31.316  ? 128 LEU   B CG   1 ? 1 
ATOM   1655 C CD1  . LEU   A 1 116 ? 13.841 5.401   8.25    1   32.257  ? 128 LEU   B CD1  1 ? 1 
ATOM   1656 C CD2  . LEU   A 1 116 ? 12.356 7.263   7.855   1   35.323  ? 128 LEU   B CD2  1 ? 1 
ATOM   1657 H H    . LEU   A 1 116 ? 11.149 6.423   4.46    1   28.461  ? 128 LEU   B H    1 c 1 
ATOM   1658 H HA   . LEU   A 1 116 ? 13.153 8.201   5.29    1   31.192  ? 128 LEU   B HA   1 c 1 
ATOM   1659 H HB2  . LEU   A 1 116 ? 13.478 5.386   5.421   1   28.326  ? 128 LEU   B HB2  1 c 1 
ATOM   1660 H HB3  . LEU   A 1 116 ? 14.472 6.463   6.004   1   29.585  ? 128 LEU   B HB3  1 c 1 
ATOM   1661 H HG   . LEU   A 1 116 ? 12.105 5.482   7.156   1   31.11   ? 128 LEU   B HG   1 c 1 
ATOM   1662 H HD11 . LEU   A 1 116 ? 14.116 4.544   7.882   1   30.914  ? 128 LEU   B HD11 1 c 1 
ATOM   1663 H HD12 . LEU   A 1 116 ? 13.395 5.258   9.101   1   32.789  ? 128 LEU   B HD12 1 c 1 
ATOM   1664 H HD13 . LEU   A 1 116 ? 14.625 5.959   8.386   1   32.666  ? 128 LEU   B HD13 1 c 1 
ATOM   1665 H HD21 . LEU   A 1 116 ? 11.519 7.5     7.425   1   34.719  ? 128 LEU   B HD21 1 c 1 
ATOM   1666 H HD22 . LEU   A 1 116 ? 12.992 7.989   7.747   1   35.274  ? 128 LEU   B HD22 1 c 1 
ATOM   1667 H HD23 . LEU   A 1 116 ? 12.198 7.11    8.802   1   35.386  ? 128 LEU   B HD23 1 c 1 
ATOM   1668 N N    . PHE   A 1 117 ? 14.845 7.799   3.526   1   31.995  ? 129 PHE   B N    1 ? 1 
ATOM   1669 C CA   . PHE   A 1 117 ? 15.764 7.741   2.428   1   30.695  ? 129 PHE   B CA   1 ? 1 
ATOM   1670 C C    . PHE   A 1 117 ? 17.112 7.307   2.958   1   28.983  ? 129 PHE   B C    1 ? 1 
ATOM   1671 O O    . PHE   A 1 117 ? 17.559 7.867   3.902   1   32.398  ? 129 PHE   B O    1 ? 1 
ATOM   1672 C CB   . PHE   A 1 117 ? 15.792 9.048   1.663   1   37.106  ? 129 PHE   B CB   1 ? 1 
ATOM   1673 C CG   . PHE   A 1 117 ? 16.708 8.971   0.454   1   41.859  ? 129 PHE   B CG   1 ? 1 
ATOM   1674 C CD1  . PHE   A 1 117 ? 18.054 9.341   0.56    1   41.488  ? 129 PHE   B CD1  1 ? 1 
ATOM   1675 C CD2  . PHE   A 1 117 ? 16.213 8.526   -0.796  1   36.328  ? 129 PHE   B CD2  1 ? 1 
ATOM   1676 C CE1  . PHE   A 1 117 ? 18.884 9.286   -0.556  1   47.893  ? 129 PHE   B CE1  1 ? 1 
ATOM   1677 C CE2  . PHE   A 1 117 ? 17.087 8.36    -1.866  1   42.638  ? 129 PHE   B CE2  1 ? 1 
ATOM   1678 C CZ   . PHE   A 1 117 ? 18.416 8.764   -1.748  1   45.631  ? 129 PHE   B CZ   1 ? 1 
ATOM   1679 H H    . PHE   A 1 117 ? 15.073 8.33    4.234   1   32.244  ? 129 PHE   B H    1 c 1 
ATOM   1680 H HA   . PHE   A 1 117 ? 15.443 7.039   1.806   1   30.663  ? 129 PHE   B HA   1 c 1 
ATOM   1681 H HB2  . PHE   A 1 117 ? 14.88  9.263   1.366   1   36.95   ? 129 PHE   B HB2  1 c 1 
ATOM   1682 H HB3  . PHE   A 1 117 ? 16.104 9.762   2.262   1   37.841  ? 129 PHE   B HB3  1 c 1 
ATOM   1683 H HD1  . PHE   A 1 117 ? 18.384 9.678   1.378   1   43.31   ? 129 PHE   B HD1  1 c 1 
ATOM   1684 H HD2  . PHE   A 1 117 ? 15.324 8.216   -0.863  1   38.061  ? 129 PHE   B HD2  1 c 1 
ATOM   1685 H HE1  . PHE   A 1 117 ? 19.793 9.518   -0.472  1   47.234  ? 129 PHE   B HE1  1 c 1 
ATOM   1686 H HE2  . PHE   A 1 117 ? 16.757 8.069   -2.7    1   42.265  ? 129 PHE   B HE2  1 c 1 
ATOM   1687 H HZ   . PHE   A 1 117 ? 18.987 8.722   -2.497  1   46.83   ? 129 PHE   B HZ   1 c 1 
ATOM   1688 N N    . PHE   A 1 118 ? 17.745 6.328   2.283   1   30.532  ? 130 PHE   B N    1 ? 1 
ATOM   1689 C CA   . PHE   A 1 118 ? 19.152 6.07    2.527   1   30.102  ? 130 PHE   B CA   1 ? 1 
ATOM   1690 C C    . PHE   A 1 118 ? 20.004 5.976   1.245   1   33.196  ? 130 PHE   B C    1 ? 1 
ATOM   1691 O O    . PHE   A 1 118 ? 19.542 5.463   0.212   1   34.003  ? 130 PHE   B O    1 ? 1 
ATOM   1692 C CB   . PHE   A 1 118 ? 19.375 4.719   3.219   1   34.095  ? 130 PHE   B CB   1 ? 1 
ATOM   1693 C CG   . PHE   A 1 118 ? 18.745 4.579   4.613   1   30.188  ? 130 PHE   B CG   1 ? 1 
ATOM   1694 C CD1  . PHE   A 1 118 ? 17.412 4.235   4.76    1   30.591  ? 130 PHE   B CD1  1 ? 1 
ATOM   1695 C CD2  . PHE   A 1 118 ? 19.497 4.865   5.742   1   34.669  ? 130 PHE   B CD2  1 ? 1 
ATOM   1696 C CE1  . PHE   A 1 118 ? 16.862 4.044   6.036   1   31.41   ? 130 PHE   B CE1  1 ? 1 
ATOM   1697 C CE2  . PHE   A 1 118 ? 18.952 4.622   6.985   1   35.159  ? 130 PHE   B CE2  1 ? 1 
ATOM   1698 C CZ   . PHE   A 1 118 ? 17.602 4.335   7.131   1   30.991  ? 130 PHE   B CZ   1 ? 1 
ATOM   1699 H H    . PHE   A 1 118 ? 17.295 5.821   1.669   1   29.154  ? 130 PHE   B H    1 c 1 
ATOM   1700 H HA   . PHE   A 1 118 ? 19.514 6.789   3.105   1   32.632  ? 130 PHE   B HA   1 c 1 
ATOM   1701 H HB2  . PHE   A 1 118 ? 19.012 4.012   2.639   1   31.13   ? 130 PHE   B HB2  1 c 1 
ATOM   1702 H HB3  . PHE   A 1 118 ? 20.343 4.567   3.297   1   32.655  ? 130 PHE   B HB3  1 c 1 
ATOM   1703 H HD1  . PHE   A 1 118 ? 16.893 4.054   3.994   1   29.996  ? 130 PHE   B HD1  1 c 1 
ATOM   1704 H HD2  . PHE   A 1 118 ? 20.416 5.068   5.658   1   34.985  ? 130 PHE   B HD2  1 c 1 
ATOM   1705 H HE1  . PHE   A 1 118 ? 15.949 3.82    6.127   1   30.445  ? 130 PHE   B HE1  1 c 1 
ATOM   1706 H HE2  . PHE   A 1 118 ? 19.46  4.829   7.753   1   35.443  ? 130 PHE   B HE2  1 c 1 
ATOM   1707 H HZ   . PHE   A 1 118 ? 17.237 4.21    7.993   1   32.48   ? 130 PHE   B HZ   1 c 1 
ATOM   1708 N N    . GLU   A 1 119 ? 21.285 6.27    1.46    1   31.891  ? 131 GLU   B N    1 ? 1 
ATOM   1709 C CA   . GLU   A 1 119 ? 22.412 5.955   0.579   1   36.768  ? 131 GLU   B CA   1 ? 1 
ATOM   1710 C C    . GLU   A 1 119 ? 23.247 4.952   1.377   1   35.945  ? 131 GLU   B C    1 ? 1 
ATOM   1711 O O    . GLU   A 1 119 ? 23.853 5.274   2.403   1   42.634  ? 131 GLU   B O    1 ? 1 
ATOM   1712 C CB   . GLU   A 1 119 ? 23.197 7.171   0.114   1   41.021  ? 131 GLU   B CB   1 ? 1 
ATOM   1713 C CG   . GLU   A 1 119 ? 24.349 6.892   -0.848  1   49.38   ? 131 GLU   B CG   1 ? 1 
ATOM   1714 C CD   . GLU   A 1 119 ? 24.977 8.15    -1.438  1   49.951  ? 131 GLU   B CD   1 ? 1 
ATOM   1715 O OE1  . GLU   A 1 119 ? 24.623 8.887   -2.412  1   48.494  ? 131 GLU   B OE1  1 ? 1 
ATOM   1716 O OE2  . GLU   A 1 119 ? 25.894 8.478   -0.686  1   54.125  ? 131 GLU   B OE2  1 ? 1 
ATOM   1717 H H    . GLU   A 1 119 ? 21.481 6.716   2.233   1   33.846  ? 131 GLU   B H    1 c 1 
ATOM   1718 H HA   . GLU   A 1 119 ? 22.055 5.501   -0.225  1   35.757  ? 131 GLU   B HA   1 c 1 
ATOM   1719 H HB2  . GLU   A 1 119 ? 22.577 7.791   -0.324  1   42.307  ? 131 GLU   B HB2  1 c 1 
ATOM   1720 H HB3  . GLU   A 1 119 ? 23.561 7.624   0.902   1   42.763  ? 131 GLU   B HB3  1 c 1 
ATOM   1721 H HG2  . GLU   A 1 119 ? 25.045 6.386   -0.376  1   47.25   ? 131 GLU   B HG2  1 c 1 
ATOM   1722 H HG3  . GLU   A 1 119 ? 24.023 6.332   -1.584  1   46.497  ? 131 GLU   B HG3  1 c 1 
ATOM   1723 N N    . ILE   A 1 120 ? 23.303 3.743   0.859   1   33.736  ? 132 ILE   B N    1 ? 1 
ATOM   1724 C CA   . ILE   A 1 120 ? 24.068 2.697   1.496   1   34.685  ? 132 ILE   B CA   1 ? 1 
ATOM   1725 C C    . ILE   A 1 120 ? 25.215 2.192   0.653   1   35.646  ? 132 ILE   B C    1 ? 1 
ATOM   1726 O O    . ILE   A 1 120 ? 24.967 1.854   -0.509  1   38.132  ? 132 ILE   B O    1 ? 1 
ATOM   1727 C CB   . ILE   A 1 120 ? 23.12  1.523   1.713   1   33.028  ? 132 ILE   B CB   1 ? 1 
ATOM   1728 C CG1  . ILE   A 1 120 ? 21.887 1.93    2.481   1   29.442  ? 132 ILE   B CG1  1 ? 1 
ATOM   1729 C CG2  . ILE   A 1 120 ? 23.967 0.434   2.393   1   32.672  ? 132 ILE   B CG2  1 ? 1 
ATOM   1730 C CD1  . ILE   A 1 120 ? 20.886 0.804   2.735   1   32.799  ? 132 ILE   B CD1  1 ? 1 
ATOM   1731 H H    . ILE   A 1 120 ? 22.856 3.556   0.084   1   34.005  ? 132 ILE   B H    1 c 1 
ATOM   1732 H HA   . ILE   A 1 120 ? 24.402 3.008   2.359   1   34.943  ? 132 ILE   B HA   1 c 1 
ATOM   1733 H HB   . ILE   A 1 120 ? 22.837 1.192   0.837   1   32.253  ? 132 ILE   B HB   1 c 1 
ATOM   1734 H HG12 . ILE   A 1 120 ? 22.166 2.299   3.344   1   31.429  ? 132 ILE   B HG12 1 c 1 
ATOM   1735 H HG13 . ILE   A 1 120 ? 21.432 2.642   1.988   1   31.145  ? 132 ILE   B HG13 1 c 1 
ATOM   1736 H HG21 . ILE   A 1 120 ? 23.388 -0.269  2.73    1   31.662  ? 132 ILE   B HG21 1 c 1 
ATOM   1737 H HG22 . ILE   A 1 120 ? 24.465 0.821   3.133   1   33.653  ? 132 ILE   B HG22 1 c 1 
ATOM   1738 H HG23 . ILE   A 1 120 ? 24.589 0.052   1.752   1   33.782  ? 132 ILE   B HG23 1 c 1 
ATOM   1739 H HD11 . ILE   A 1 120 ? 20.639 0.39    1.886   1   31.018  ? 132 ILE   B HD11 1 c 1 
ATOM   1740 H HD12 . ILE   A 1 120 ? 20.088 1.171   3.159   1   30.593  ? 132 ILE   B HD12 1 c 1 
ATOM   1741 H HD13 . ILE   A 1 120 ? 21.282 0.131   3.321   1   31.119  ? 132 ILE   B HD13 1 c 1 
ATOM   1742 N N    . GLU   A 1 121 ? 26.401 2.002   1.281   1   37.851  ? 133 GLU   B N    1 ? 1 
ATOM   1743 C CA   . GLU   A 1 121 ? 27.504 1.311   0.635   1   39.775  ? 133 GLU   B CA   1 ? 1 
ATOM   1744 C C    . GLU   A 1 121 ? 27.77  0.001   1.353   1   39.45   ? 133 GLU   B C    1 ? 1 
ATOM   1745 O O    . GLU   A 1 121 ? 28.08  -0.016  2.555   1   44.045  ? 133 GLU   B O    1 ? 1 
ATOM   1746 C CB   . GLU   A 1 121 ? 28.759 2.173   0.583   1   43.287  ? 133 GLU   B CB   1 ? 1 
ATOM   1747 C CG   . GLU   A 1 121 ? 29.948 1.532   -0.151  1   44.762  ? 133 GLU   B CG   1 ? 1 
ATOM   1748 C CD   . GLU   A 1 121 ? 31.194 2.433   -0.111  1   49.447  ? 133 GLU   B CD   1 ? 1 
ATOM   1749 O OE1  . GLU   A 1 121 ? 31.108 3.636   0.112   1   49.107  ? 133 GLU   B OE1  1 ? 1 
ATOM   1750 O OE2  . GLU   A 1 121 ? 32.289 1.926   -0.379  1   49.425  ? 133 GLU   B OE2  1 ? 1 
ATOM   1751 H H    . GLU   A 1 121 ? 26.515 2.314   2.133   1   37.855  ? 133 GLU   B H    1 c 1 
ATOM   1752 H HA   . GLU   A 1 121 ? 27.24  1.111   -0.295  1   39.94   ? 133 GLU   B HA   1 c 1 
ATOM   1753 H HB2  . GLU   A 1 121 ? 28.537 3.021   0.147   1   43.67   ? 133 GLU   B HB2  1 c 1 
ATOM   1754 H HB3  . GLU   A 1 121 ? 29.036 2.375   1.501   1   43.347  ? 133 GLU   B HB3  1 c 1 
ATOM   1755 H HG2  . GLU   A 1 121 ? 30.166 0.672   0.266   1   44.674  ? 133 GLU   B HG2  1 c 1 
ATOM   1756 H HG3  . GLU   A 1 121 ? 29.704 1.367   -1.086  1   45.262  ? 133 GLU   B HG3  1 c 1 
ATOM   1757 N N    . LEU   A 1 122 ? 27.696 -1.083  0.603   1   44.753  ? 134 LEU   B N    1 ? 1 
ATOM   1758 C CA   . LEU   A 1 122 ? 28     -2.395  1.166   1   43.6    ? 134 LEU   B CA   1 ? 1 
ATOM   1759 C C    . LEU   A 1 122 ? 29.494 -2.669  1.126   1   49.556  ? 134 LEU   B C    1 ? 1 
ATOM   1760 O O    . LEU   A 1 122 ? 30.093 -2.743  0.061   1   50.991  ? 134 LEU   B O    1 ? 1 
ATOM   1761 C CB   . LEU   A 1 122 ? 27.284 -3.469  0.368   1   41.522  ? 134 LEU   B CB   1 ? 1 
ATOM   1762 C CG   . LEU   A 1 122 ? 27.519 -4.882  0.901   1   40.629  ? 134 LEU   B CG   1 ? 1 
ATOM   1763 C CD1  . LEU   A 1 122 ? 27.269 -5.037  2.393   1   39.579  ? 134 LEU   B CD1  1 ? 1 
ATOM   1764 C CD2  . LEU   A 1 122 ? 26.632 -5.885  0.105   1   40.028  ? 134 LEU   B CD2  1 ? 1 
ATOM   1765 H H    . LEU   A 1 122 ? 27.454 -1.02   -0.276  1   43.216  ? 134 LEU   B H    1 c 1 
ATOM   1766 H HA   . LEU   A 1 122 ? 27.687 -2.418  2.105   1   43.036  ? 134 LEU   B HA   1 c 1 
ATOM   1767 H HB2  . LEU   A 1 122 ? 26.317 -3.28   0.388   1   39.877  ? 134 LEU   B HB2  1 c 1 
ATOM   1768 H HB3  . LEU   A 1 122 ? 27.596 -3.427  -0.565  1   42.896  ? 134 LEU   B HB3  1 c 1 
ATOM   1769 H HG   . LEU   A 1 122 ? 28.466 -5.121  0.728   1   42.763  ? 134 LEU   B HG   1 c 1 
ATOM   1770 H HD11 . LEU   A 1 122 ? 27.971 -4.586  2.89    1   40.721  ? 134 LEU   B HD11 1 c 1 
ATOM   1771 H HD12 . LEU   A 1 122 ? 27.265 -5.981  2.624   1   39.668  ? 134 LEU   B HD12 1 c 1 
ATOM   1772 H HD13 . LEU   A 1 122 ? 26.409 -4.645  2.621   1   38.026  ? 134 LEU   B HD13 1 c 1 
ATOM   1773 H HD21 . LEU   A 1 122 ? 26.756 -5.745  -0.848  1   41.007  ? 134 LEU   B HD21 1 c 1 
ATOM   1774 H HD22 . LEU   A 1 122 ? 25.698 -5.744  0.333   1   38.356  ? 134 LEU   B HD22 1 c 1 
ATOM   1775 H HD23 . LEU   A 1 122 ? 26.885 -6.795  0.333   1   40.479  ? 134 LEU   B HD23 1 c 1 
ATOM   1776 N N    . LEU   A 1 123 ? 30.146 -2.744  2.288   1   52.744  ? 135 LEU   B N    1 ? 1 
ATOM   1777 C CA   . LEU   A 1 123 ? 31.605 -2.793  2.266   1   54.77   ? 135 LEU   B CA   1 ? 1 
ATOM   1778 C C    . LEU   A 1 123 ? 32.05  -4.251  2.132   1   62.063  ? 135 LEU   B C    1 ? 1 
ATOM   1779 O O    . LEU   A 1 123 ? 32.971 -4.593  1.373   1   58.344  ? 135 LEU   B O    1 ? 1 
ATOM   1780 C CB   . LEU   A 1 123 ? 32.124 -2.166  3.551   1   55.915  ? 135 LEU   B CB   1 ? 1 
ATOM   1781 C CG   . LEU   A 1 123 ? 31.675 -0.725  3.828   1   61.732  ? 135 LEU   B CG   1 ? 1 
ATOM   1782 C CD1  . LEU   A 1 123 ? 32.081 -0.28   5.25    1   71.899  ? 135 LEU   B CD1  1 ? 1 
ATOM   1783 C CD2  . LEU   A 1 123 ? 32.258 0.226   2.804   1   65.486  ? 135 LEU   B CD2  1 ? 1 
ATOM   1784 H H    . LEU   A 1 123 ? 29.698 -2.761  3.084   1   50.63   ? 135 LEU   B H    1 c 1 
ATOM   1785 H HA   . LEU   A 1 123 ? 31.937 -2.277  1.488   1   57.528  ? 135 LEU   B HA   1 c 1 
ATOM   1786 H HB2  . LEU   A 1 123 ? 31.838 -2.731  4.305   1   56.185  ? 135 LEU   B HB2  1 c 1 
ATOM   1787 H HB3  . LEU   A 1 123 ? 33.108 -2.184  3.525   1   59.951  ? 135 LEU   B HB3  1 c 1 
ATOM   1788 H HG   . LEU   A 1 123 ? 30.687 -0.687  3.761   1   59.426  ? 135 LEU   B HG   1 c 1 
ATOM   1789 H HD11 . LEU   A 1 123 ? 31.724 -0.908  5.9     1   67.886  ? 135 LEU   B HD11 1 c 1 
ATOM   1790 H HD12 . LEU   A 1 123 ? 31.723 0.606   5.427   1   68.949  ? 135 LEU   B HD12 1 c 1 
ATOM   1791 H HD13 . LEU   A 1 123 ? 33.05  -0.258  5.32    1   71.947  ? 135 LEU   B HD13 1 c 1 
ATOM   1792 H HD21 . LEU   A 1 123 ? 31.917 0.006   1.921   1   64.116  ? 135 LEU   B HD21 1 c 1 
ATOM   1793 H HD22 . LEU   A 1 123 ? 33.226 0.148   2.805   1   67.757  ? 135 LEU   B HD22 1 c 1 
ATOM   1794 H HD23 . LEU   A 1 123 ? 32.008 1.138   3.028   1   65.151  ? 135 LEU   B HD23 1 c 1 
ATOM   1795 N N    . ASP   A 1 124 ? 31.385 -5.14   2.883   1   57.178  ? 136 ASP   B N    1 ? 1 
ATOM   1796 C CA   . ASP   A 1 124 ? 31.869 -6.519  3.032   1   54.702  ? 136 ASP   B CA   1 ? 1 
ATOM   1797 C C    . ASP   A 1 124 ? 30.745 -7.32   3.703   1   53.881  ? 136 ASP   B C    1 ? 1 
ATOM   1798 O O    . ASP   A 1 124 ? 29.93  -6.697  4.375   1   44.962  ? 136 ASP   B O    1 ? 1 
ATOM   1799 C CB   . ASP   A 1 124 ? 33.093 -6.543  3.938   1   55.946  ? 136 ASP   B CB   1 ? 1 
ATOM   1800 C CG   . ASP   A 1 124 ? 34.006 -7.754  3.812   1   57.035  ? 136 ASP   B CG   1 ? 1 
ATOM   1801 O OD1  . ASP   A 1 124 ? 33.609 -8.722  3.163   1   54.74   ? 136 ASP   B OD1  1 ? 1 
ATOM   1802 O OD2  . ASP   A 1 124 ? 35.155 -7.678  4.282   1   70.642  ? 136 ASP   B OD2  1 ? 1 
ATOM   1803 H H    . ASP   A 1 124 ? 30.62  -4.889  3.316   1   55.031  ? 136 ASP   B H    1 c 1 
ATOM   1804 H HA   . ASP   A 1 124 ? 32.065 -6.894  2.144   1   56.114  ? 136 ASP   B HA   1 c 1 
ATOM   1805 H HB2  . ASP   A 1 124 ? 33.635 -5.748  3.756   1   57.543  ? 136 ASP   B HB2  1 c 1 
ATOM   1806 H HB3  . ASP   A 1 124 ? 32.795 -6.488  4.87    1   55.309  ? 136 ASP   B HB3  1 c 1 
ATOM   1807 N N    . PHE   A 1 125 ? 30.691 -8.644  3.507   1   50.654  ? 137 PHE   B N    1 ? 1 
ATOM   1808 C CA   . PHE   A 1 125 ? 29.836 -9.519  4.326   1   48.073  ? 137 PHE   B CA   1 ? 1 
ATOM   1809 C C    . PHE   A 1 125 ? 30.538 -10.855 4.522   1   50.969  ? 137 PHE   B C    1 ? 1 
ATOM   1810 O O    . PHE   A 1 125 ? 31.258 -11.29  3.631   1   54.296  ? 137 PHE   B O    1 ? 1 
ATOM   1811 C CB   . PHE   A 1 125 ? 28.473 -9.73   3.674   1   49.788  ? 137 PHE   B CB   1 ? 1 
ATOM   1812 C CG   . PHE   A 1 125 ? 28.471 -10.177 2.213   1   47.351  ? 137 PHE   B CG   1 ? 1 
ATOM   1813 C CD1  . PHE   A 1 125 ? 28.444 -9.226  1.192   1   45.648  ? 137 PHE   B CD1  1 ? 1 
ATOM   1814 C CD2  . PHE   A 1 125 ? 28.312 -11.513 1.864   1   49.173  ? 137 PHE   B CD2  1 ? 1 
ATOM   1815 C CE1  . PHE   A 1 125 ? 28.463 -9.623  -0.132  1   49.84   ? 137 PHE   B CE1  1 ? 1 
ATOM   1816 C CE2  . PHE   A 1 125 ? 28.313 -11.907 0.518   1   52.654  ? 137 PHE   B CE2  1 ? 1 
ATOM   1817 C CZ   . PHE   A 1 125 ? 28.376 -10.947 -0.471  1   54.118  ? 137 PHE   B CZ   1 ? 1 
ATOM   1818 H H    . PHE   A 1 125 ? 31.2   -9.018  2.846   1   52.625  ? 137 PHE   B H    1 c 1 
ATOM   1819 H HA   . PHE   A 1 125 ? 29.705 -9.092  5.211   1   48.717  ? 137 PHE   B HA   1 c 1 
ATOM   1820 H HB2  . PHE   A 1 125 ? 27.983 -10.398 4.203   1   47.667  ? 137 PHE   B HB2  1 c 1 
ATOM   1821 H HB3  . PHE   A 1 125 ? 27.971 -8.888  3.741   1   46.658  ? 137 PHE   B HB3  1 c 1 
ATOM   1822 H HD1  . PHE   A 1 125 ? 28.543 -8.312  1.406   1   46.288  ? 137 PHE   B HD1  1 c 1 
ATOM   1823 H HD2  . PHE   A 1 125 ? 28.306 -12.17  2.541   1   49.854  ? 137 PHE   B HD2  1 c 1 
ATOM   1824 H HE1  . PHE   A 1 125 ? 28.489 -8.969  -0.812  1   50.084  ? 137 PHE   B HE1  1 c 1 
ATOM   1825 H HE2  . PHE   A 1 125 ? 28.251 -12.822 0.292   1   53.44   ? 137 PHE   B HE2  1 c 1 
ATOM   1826 H HZ   . PHE   A 1 125 ? 28.344 -11.202 -1.379  1   54.078  ? 137 PHE   B HZ   1 c 1 
ATOM   1827 N N    . LYS   A 1 126 ? 30.398 -11.454 5.709   1   50.783  ? 138 LYS   B N    1 ? 1 
ATOM   1828 C CA   . LYS   A 1 126 ? 31.085 -12.706 6.035   1   53.745  ? 138 LYS   B CA   1 ? 1 
ATOM   1829 C C    . LYS   A 1 126 ? 30.007 -13.728 6.469   1   46.813  ? 138 LYS   B C    1 ? 1 
ATOM   1830 O O    . LYS   A 1 126 ? 29.066 -13.404 7.154   1   45.059  ? 138 LYS   B O    1 ? 1 
ATOM   1831 C CB   . LYS   A 1 126 ? 32.161 -12.353 7.074   1   50.196  ? 138 LYS   B CB   1 ? 1 
ATOM   1832 H H    . LYS   A 1 126 ? 29.855 -11.074 6.339   1   49.808  ? 138 LYS   B H    1 c 1 
ATOM   1833 H HA   . LYS   A 1 126 ? 31.531 -13.045 5.219   1   52.386  ? 138 LYS   B HA   1 c 1 
ATOM   1834 H HB2  . LYS   A 1 126 ? 33.042 -12.512 6.679   0   30      ? 138 LYS   B HB2  1 c 1 
ATOM   1835 H HB3  . LYS   A 1 126 ? 31.716 -12.207 7.945   0   30      ? 138 LYS   B HB3  1 c 1 
ATOM   1836 N N    . GLY   A 1 127 ? 30.161 -14.978 6.086   1   54.788  ? 139 GLY   B N    1 ? 1 
ATOM   1837 C CA   . GLY   A 1 127 ? 29.515 -16.101 6.749   1   54.069  ? 139 GLY   B CA   1 ? 1 
ATOM   1838 C C    . GLY   A 1 127 ? 29.5   -15.933 8.265   1   60.472  ? 139 GLY   B C    1 ? 1 
ATOM   1839 O O    . GLY   A 1 127 ? 30.533 -15.63  8.849   1   69.031  ? 139 GLY   B O    1 ? 1 
ATOM   1840 H H    . GLY   A 1 127 ? 30.698 -15.152 5.367   1   53.864  ? 139 GLY   B H    1 c 1 
ATOM   1841 H HA2  . GLY   A 1 127 ? 28.591 -16.185 6.415   1   54.129  ? 139 GLY   B HA2  1 c 1 
ATOM   1842 H HA3  . GLY   A 1 127 ? 29.999 -16.927 6.516   1   57.601  ? 139 GLY   B HA3  1 c 1 
ATOM   1843 N N    . GLU   A 1 128 ? 28.312 -16.019 8.88    1   62.039  ? 140 GLU   B N    1 ? 1 
ATOM   1844 C CA   . GLU   A 1 128 ? 28.195 -16.512 10.243  1   71.648  ? 140 GLU   B CA   1 ? 1 
ATOM   1845 C C    . GLU   A 1 128 ? 29.261 -17.631 10.452  1   78.369  ? 140 GLU   B C    1 ? 1 
ATOM   1846 O O    . GLU   A 1 128 ? 29.675 -18.318 9.479   1   80.247  ? 140 GLU   B O    1 ? 1 
ATOM   1847 C CB   . GLU   A 1 128 ? 26.763 -16.956 10.612  1   71.579  ? 140 GLU   B CB   1 ? 1 
ATOM   1848 O OXT  . GLU   A 1 128 ? 29.663 -17.789 11.598  1   89.157  ? 140 GLU   B OXT  1 ? 1 
ATOM   1849 H H    . GLU   A 1 128 ? 27.557 -15.757 8.436   1   60.937  ? 140 GLU   B H    1 c 1 
ATOM   1850 H HA   . GLU   A 1 128 ? 28.427 -15.762 10.85   1   70.657  ? 140 GLU   B HA   1 c 1 
ATOM   1851 H HB2  . GLU   A 1 128 ? 26.845 -17.724 11.2    0   30      ? 140 GLU   B HB2  1 c 1 
ATOM   1852 H HB3  . GLU   A 1 128 ? 26.117 -16.392 10.132  0   30      ? 140 GLU   B HB3  1 c 1 
ATOM   1853 N N    . THR   B 1 5   ? 0.376  -3.541  43.512  1   71.401  ? 17  THR   A N    1 ? 2 
ATOM   1854 C CA   . THR   B 1 5   ? 1.55   -4.01   42.755  1   70.749  ? 17  THR   A CA   1 ? 2 
ATOM   1855 C C    . THR   B 1 5   ? 2.124  -2.887  41.869  1   73.263  ? 17  THR   A C    1 ? 2 
ATOM   1856 O O    . THR   B 1 5   ? 1.437  -1.926  41.498  1   71.799  ? 17  THR   A O    1 ? 2 
ATOM   1857 C CB   . THR   B 1 5   ? 1.101  -5.216  41.913  1   76.389  ? 17  THR   A CB   1 ? 2 
ATOM   1858 O OG1  . THR   B 1 5   ? 0.936  -6.313  42.809  1   74.65   ? 17  THR   A OG1  1 ? 2 
ATOM   1859 C CG2  . THR   B 1 5   ? 2.053  -5.637  40.797  1   74.259  ? 17  THR   A CG2  1 ? 2 
ATOM   1860 H H    . THR   B 1 5   ? 0.032  -4.223  43.992  1   73.188  ? 17  THR   A H    1 c 2 
ATOM   1861 H HA   . THR   B 1 5   ? 2.238  -4.304  43.391  1   73.035  ? 17  THR   A HA   1 c 2 
ATOM   1862 H HB   . THR   B 1 5   ? 0.228  -5.008  41.502  1   74.362  ? 17  THR   A HB   1 c 2 
ATOM   1863 H HG1  . THR   B 1 5   ? 1.616  -6.487  43.1    0   30      ? 17  THR   A HG1  1 c 2 
ATOM   1864 H HG21 . THR   B 1 5   ? 1.803  -6.519  40.474  1   72.82   ? 17  THR   A HG21 1 c 2 
ATOM   1865 H HG22 . THR   B 1 5   ? 2.96   -5.663  41.139  1   73.847  ? 17  THR   A HG22 1 c 2 
ATOM   1866 H HG23 . THR   B 1 5   ? 2      -4.999  40.065  1   72.747  ? 17  THR   A HG23 1 c 2 
ATOM   1867 N N    . VAL   B 1 6   ? 3.409  -3.071  41.488  1   75.584  ? 18  VAL   A N    1 ? 2 
ATOM   1868 C CA   . VAL   B 1 6   ? 4.179  -2.211  40.593  1   71.597  ? 18  VAL   A CA   1 ? 2 
ATOM   1869 C C    . VAL   B 1 6   ? 4.386  -3.007  39.294  1   66.551  ? 18  VAL   A C    1 ? 2 
ATOM   1870 O O    . VAL   B 1 6   ? 4.412  -4.256  39.282  1   66.603  ? 18  VAL   A O    1 ? 2 
ATOM   1871 C CB   . VAL   B 1 6   ? 5.537  -1.683  41.158  1   67.806  ? 18  VAL   A CB   1 ? 2 
ATOM   1872 C CG1  . VAL   B 1 6   ? 5.379  -0.719  42.335  1   71.548  ? 18  VAL   A CG1  1 ? 2 
ATOM   1873 C CG2  . VAL   B 1 6   ? 6.51   -2.799  41.589  1   72.34   ? 18  VAL   A CG2  1 ? 2 
ATOM   1874 H H    . VAL   B 1 6   ? 3.84   -3.798  41.835  1   73.784  ? 18  VAL   A H    1 c 2 
ATOM   1875 H HA   . VAL   B 1 6   ? 3.626  -1.434  40.382  1   71.37   ? 18  VAL   A HA   1 c 2 
ATOM   1876 H HB   . VAL   B 1 6   ? 5.973  -1.184  40.43   1   68.247  ? 18  VAL   A HB   1 c 2 
ATOM   1877 H HG11 . VAL   B 1 6   ? 4.993  -1.192  43.092  1   73.112  ? 18  VAL   A HG11 1 c 2 
ATOM   1878 H HG12 . VAL   B 1 6   ? 4.794  0.013   42.079  1   72.129  ? 18  VAL   A HG12 1 c 2 
ATOM   1879 H HG13 . VAL   B 1 6   ? 6.249  -0.365  42.584  1   72.358  ? 18  VAL   A HG13 1 c 2 
ATOM   1880 H HG21 . VAL   B 1 6   ? 7.261  -2.41   42.068  1   72.131  ? 18  VAL   A HG21 1 c 2 
ATOM   1881 H HG22 . VAL   B 1 6   ? 6.839  -3.264  40.801  1   68.537  ? 18  VAL   A HG22 1 c 2 
ATOM   1882 H HG23 . VAL   B 1 6   ? 6.049  -3.428  42.167  1   71.753  ? 18  VAL   A HG23 1 c 2 
ATOM   1883 N N    . THR   B 1 7   ? 4.509  -2.243  38.203  1   57.605  ? 19  THR   A N    1 ? 2 
ATOM   1884 C CA   . THR   B 1 7   ? 4.806  -2.779  36.873  1   58.085  ? 19  THR   A CA   1 ? 2 
ATOM   1885 C C    . THR   B 1 7   ? 6.148  -3.508  36.94   1   52.97   ? 19  THR   A C    1 ? 2 
ATOM   1886 O O    . THR   B 1 7   ? 6.184  -4.674  36.65   1   64.749  ? 19  THR   A O    1 ? 2 
ATOM   1887 C CB   . THR   B 1 7   ? 4.906  -1.658  35.822  1   55.982  ? 19  THR   A CB   1 ? 2 
ATOM   1888 O OG1  . THR   B 1 7   ? 3.74   -0.851  35.843  1   62.14   ? 19  THR   A OG1  1 ? 2 
ATOM   1889 C CG2  . THR   B 1 7   ? 5.18   -2.21   34.435  1   49.251  ? 19  THR   A CG2  1 ? 2 
ATOM   1890 H H    . THR   B 1 7   ? 4.403  -1.339  38.29   1   61.221  ? 19  THR   A H    1 c 2 
ATOM   1891 H HA   . THR   B 1 7   ? 4.1    -3.41   36.613  1   55.887  ? 19  THR   A HA   1 c 2 
ATOM   1892 H HB   . THR   B 1 7   ? 5.676  -1.088  36.059  1   56.761  ? 19  THR   A HB   1 c 2 
ATOM   1893 H HG1  . THR   B 1 7   ? 2.95   -1.379  35.754  0   30      ? 19  THR   A HG1  1 c 2 
ATOM   1894 H HG21 . THR   B 1 7   ? 5.065  -1.504  33.777  1   50.087  ? 19  THR   A HG21 1 c 2 
ATOM   1895 H HG22 . THR   B 1 7   ? 4.558  -2.933  34.245  1   49.852  ? 19  THR   A HG22 1 c 2 
ATOM   1896 H HG23 . THR   B 1 7   ? 6.091  -2.547  34.391  1   49.587  ? 19  THR   A HG23 1 c 2 
ATOM   1897 N N    . GLU   B 1 8   ? 7.189  -2.8    37.448  1   54.692  ? 20  GLU   A N    1 ? 2 
ATOM   1898 C CA   . GLU   B 1 8   ? 8.585  -3.2    37.468  1   54.088  ? 20  GLU   A CA   1 ? 2 
ATOM   1899 C C    . GLU   B 1 8   ? 8.842  -4.159  38.626  1   53.698  ? 20  GLU   A C    1 ? 2 
ATOM   1900 O O    . GLU   B 1 8   ? 9.725  -3.929  39.486  1   57.377  ? 20  GLU   A O    1 ? 2 
ATOM   1901 C CB   . GLU   B 1 8   ? 9.527  -2      37.474  1   60.276  ? 20  GLU   A CB   1 ? 2 
ATOM   1902 C CG   . GLU   B 1 8   ? 9.304  -1.1    36.267  1   63.648  ? 20  GLU   A CG   1 ? 2 
ATOM   1903 C CD   . GLU   B 1 8   ? 9.578  -1.614  34.867  1   58.372  ? 20  GLU   A CD   1 ? 2 
ATOM   1904 O OE1  . GLU   B 1 8   ? 10.371 -2.578  34.499  1   49.731  ? 20  GLU   A OE1  1 ? 2 
ATOM   1905 O OE2  . GLU   B 1 8   ? 8.998  -0.809  34.089  1   61.166  ? 20  GLU   A OE2  1 ? 2 
ATOM   1906 H H    . GLU   B 1 8   ? 6.99   -1.987  37.815  1   56.11   ? 20  GLU   A H    1 c 2 
ATOM   1907 H HA   . GLU   B 1 8   ? 8.761  -3.698  36.629  1   52.769  ? 20  GLU   A HA   1 c 2 
ATOM   1908 H HB2  . GLU   B 1 8   ? 9.407  -1.496  38.305  1   62.062  ? 20  GLU   A HB2  1 c 2 
ATOM   1909 H HB3  . GLU   B 1 8   ? 10.448 -2.32   37.443  1   59.73   ? 20  GLU   A HB3  1 c 2 
ATOM   1910 H HG2  . GLU   B 1 8   ? 8.372  -0.795  36.289  1   62.239  ? 20  GLU   A HG2  1 c 2 
ATOM   1911 H HG3  . GLU   B 1 8   ? 9.851  -0.295  36.391  1   62.967  ? 20  GLU   A HG3  1 c 2 
ATOM   1912 N N    . GLN   B 1 9   ? 7.914  -5.126  38.754  1   55.683  ? 21  GLN   A N    1 ? 2 
ATOM   1913 C CA   . GLN   B 1 9   ? 7.965  -6.083  39.868  1   58.641  ? 21  GLN   A CA   1 ? 2 
ATOM   1914 C C    . GLN   B 1 9   ? 8.443  -7.409  39.3    1   56.391  ? 21  GLN   A C    1 ? 2 
ATOM   1915 O O    . GLN   B 1 9   ? 8.492  -7.604  38.086  1   59.14   ? 21  GLN   A O    1 ? 2 
ATOM   1916 C CB   . GLN   B 1 9   ? 6.553  -6.251  40.423  1   70.037  ? 21  GLN   A CB   1 ? 2 
ATOM   1917 C CG   . GLN   B 1 9   ? 5.545  -6.856  39.433  1   72.815  ? 21  GLN   A CG   1 ? 2 
ATOM   1918 C CD   . GLN   B 1 9   ? 4.479  -7.65   40.174  1   71.795  ? 21  GLN   A CD   1 ? 2 
ATOM   1919 O OE1  . GLN   B 1 9   ? 4.524  -7.73   41.404  1   71.213  ? 21  GLN   A OE1  1 ? 2 
ATOM   1920 N NE2  . GLN   B 1 9   ? 3.622  -8.361  39.439  1   67.4    ? 21  GLN   A NE2  1 ? 2 
ATOM   1921 H H    . GLN   B 1 9   ? 7.258  -5.216  38.125  1   54.288  ? 21  GLN   A H    1 c 2 
ATOM   1922 H HA   . GLN   B 1 9   ? 8.593  -5.76   40.563  1   61.498  ? 21  GLN   A HA   1 c 2 
ATOM   1923 H HB2  . GLN   B 1 9   ? 6.606  -6.825  41.215  1   69.806  ? 21  GLN   A HB2  1 c 2 
ATOM   1924 H HB3  . GLN   B 1 9   ? 6.225  -5.378  40.714  1   69.606  ? 21  GLN   A HB3  1 c 2 
ATOM   1925 H HG2  . GLN   B 1 9   ? 5.122  -6.145  38.912  1   70.511  ? 21  GLN   A HG2  1 c 2 
ATOM   1926 H HG3  . GLN   B 1 9   ? 6.008  -7.451  38.808  1   69.233  ? 21  GLN   A HG3  1 c 2 
ATOM   1927 H HE21 . GLN   B 1 9   ? 2.928  -8.755  39.827  1   69.4    ? 21  GLN   A HE21 1 c 2 
ATOM   1928 H HE22 . GLN   B 1 9   ? 3.745  -8.439  38.564  1   66.618  ? 21  GLN   A HE22 1 c 2 
ATOM   1929 N N    . GLY   B 1 10  ? 8.769  -8.345  40.166  1   60.742  ? 22  GLY   A N    1 ? 2 
ATOM   1930 C CA   . GLY   B 1 10  ? 9.368  -9.544  39.683  1   51.304  ? 22  GLY   A CA   1 ? 2 
ATOM   1931 C C    . GLY   B 1 10  ? 10.865 -9.418  39.794  1   52.435  ? 22  GLY   A C    1 ? 2 
ATOM   1932 O O    . GLY   B 1 10  ? 11.395 -8.353  40.087  1   55.148  ? 22  GLY   A O    1 ? 2 
ATOM   1933 H H    . GLY   B 1 10  ? 8.618  -8.236  41.061  1   59.905  ? 22  GLY   A H    1 c 2 
ATOM   1934 H HA2  . GLY   B 1 10  ? 9.054  -10.308 40.222  1   54.141  ? 22  GLY   A HA2  1 c 2 
ATOM   1935 H HA3  . GLY   B 1 10  ? 9.109  -9.699  38.745  1   51.392  ? 22  GLY   A HA3  1 c 2 
ATOM   1936 N N    . GLU   B 1 11  ? 11.523 -10.567 39.633  1   51.929  ? 23  GLU   A N    1 ? 2 
ATOM   1937 C CA   . GLU   B 1 11  ? 12.943 -10.733 39.842  1   52.745  ? 23  GLU   A CA   1 ? 2 
ATOM   1938 C C    . GLU   B 1 11  ? 13.644 -10.355 38.54   1   53.237  ? 23  GLU   A C    1 ? 2 
ATOM   1939 O O    . GLU   B 1 11  ? 13.172 -10.753 37.453  1   47.678  ? 23  GLU   A O    1 ? 2 
ATOM   1940 C CB   . GLU   B 1 11  ? 13.166 -12.194 40.226  1   55.5    ? 23  GLU   A CB   1 ? 2 
ATOM   1941 C CG   . GLU   B 1 11  ? 14.645 -12.581 40.316  1   60.177  ? 23  GLU   A CG   1 ? 2 
ATOM   1942 C CD   . GLU   B 1 11  ? 14.972 -14.045 40.551  1   64.785  ? 23  GLU   A CD   1 ? 2 
ATOM   1943 O OE1  . GLU   B 1 11  ? 14.085 -14.817 40.966  1   61.529  ? 23  GLU   A OE1  1 ? 2 
ATOM   1944 O OE2  . GLU   B 1 11  ? 16.158 -14.375 40.363  1   70.986  ? 23  GLU   A OE2  1 ? 2 
ATOM   1945 H H    . GLU   B 1 11  ? 11.043 -11.298 39.368  1   51.253  ? 23  GLU   A H    1 c 2 
ATOM   1946 H HA   . GLU   B 1 11  ? 13.237 -10.131 40.572  1   55.34   ? 23  GLU   A HA   1 c 2 
ATOM   1947 H HB2  . GLU   B 1 11  ? 12.747 -12.364 41.09   1   57.386  ? 23  GLU   A HB2  1 c 2 
ATOM   1948 H HB3  . GLU   B 1 11  ? 12.729 -12.768 39.564  1   54.287  ? 23  GLU   A HB3  1 c 2 
ATOM   1949 H HG2  . GLU   B 1 11  ? 15.088 -12.309 39.484  1   58.764  ? 23  GLU   A HG2  1 c 2 
ATOM   1950 H HG3  . GLU   B 1 11  ? 15.059 -12.061 41.037  1   61.954  ? 23  GLU   A HG3  1 c 2 
ATOM   1951 N N    . ASP   B 1 12  ? 14.758 -9.612  38.686  1   52.683  ? 24  ASP   A N    1 ? 2 
ATOM   1952 C CA   . ASP   B 1 12  ? 15.596 -9.23   37.59   1   55.313  ? 24  ASP   A CA   1 ? 2 
ATOM   1953 C C    . ASP   B 1 12  ? 16.427 -10.458 37.267  1   53.943  ? 24  ASP   A C    1 ? 2 
ATOM   1954 O O    . ASP   B 1 12  ? 17.291 -10.778 38.059  1   50.716  ? 24  ASP   A O    1 ? 2 
ATOM   1955 C CB   . ASP   B 1 12  ? 16.457 -8.008  37.883  1   52.834  ? 24  ASP   A CB   1 ? 2 
ATOM   1956 C CG   . ASP   B 1 12  ? 17.271 -7.56   36.677  1   53.889  ? 24  ASP   A CG   1 ? 2 
ATOM   1957 O OD1  . ASP   B 1 12  ? 17.244 -8.3    35.658  1   50.462  ? 24  ASP   A OD1  1 ? 2 
ATOM   1958 O OD2  . ASP   B 1 12  ? 17.9   -6.496  36.723  1   51.101  ? 24  ASP   A OD2  1 ? 2 
ATOM   1959 H H    . ASP   B 1 12  ? 14.994 -9.337  39.525  1   55.821  ? 24  ASP   A H    1 c 2 
ATOM   1960 H HA   . ASP   B 1 12  ? 15.025 -9.025  36.819  1   51.559  ? 24  ASP   A HA   1 c 2 
ATOM   1961 H HB2  . ASP   B 1 12  ? 15.876 -7.268  38.158  1   54.504  ? 24  ASP   A HB2  1 c 2 
ATOM   1962 H HB3  . ASP   B 1 12  ? 17.07  -8.208  38.621  1   56.333  ? 24  ASP   A HB3  1 c 2 
ATOM   1963 N N    . ILE   B 1 13  ? 16.175 -11.11  36.119  1   47.68   ? 25  ILE   A N    1 ? 2 
ATOM   1964 C CA   . ILE   B 1 13  ? 16.924 -12.318 35.782  1   54.352  ? 25  ILE   A CA   1 ? 2 
ATOM   1965 C C    . ILE   B 1 13  ? 17.906 -12.045 34.648  1   55.584  ? 25  ILE   A C    1 ? 2 
ATOM   1966 O O    . ILE   B 1 13  ? 18.44  -12.969 34.029  1   50.845  ? 25  ILE   A O    1 ? 2 
ATOM   1967 C CB   . ILE   B 1 13  ? 15.998 -13.49  35.433  1   50.822  ? 25  ILE   A CB   1 ? 2 
ATOM   1968 C CG1  . ILE   B 1 13  ? 15.119 -13.209 34.221  1   48.428  ? 25  ILE   A CG1  1 ? 2 
ATOM   1969 C CG2  . ILE   B 1 13  ? 15.147 -13.933 36.618  1   57.18   ? 25  ILE   A CG2  1 ? 2 
ATOM   1970 C CD1  . ILE   B 1 13  ? 14.258 -14.411 33.871  1   55.55   ? 25  ILE   A CD1  1 ? 2 
ATOM   1971 H H    . ILE   B 1 13  ? 15.542 -10.796 35.539  1   48.445  ? 25  ILE   A H    1 c 2 
ATOM   1972 H HA   . ILE   B 1 13  ? 17.442 -12.579 36.567  1   54.767  ? 25  ILE   A HA   1 c 2 
ATOM   1973 H HB   . ILE   B 1 13  ? 16.57  -14.245 35.197  1   52.852  ? 25  ILE   A HB   1 c 2 
ATOM   1974 H HG12 . ILE   B 1 13  ? 14.54  -12.443 34.411  1   49.477  ? 25  ILE   A HG12 1 c 2 
ATOM   1975 H HG13 . ILE   B 1 13  ? 15.685 -12.984 33.454  1   49.37   ? 25  ILE   A HG13 1 c 2 
ATOM   1976 H HG21 . ILE   B 1 13  ? 14.749 -14.799 36.433  1   55.38   ? 25  ILE   A HG21 1 c 2 
ATOM   1977 H HG22 . ILE   B 1 13  ? 14.444 -13.281 36.776  1   55.038  ? 25  ILE   A HG22 1 c 2 
ATOM   1978 H HG23 . ILE   B 1 13  ? 15.706 -14     37.411  1   57.432  ? 25  ILE   A HG23 1 c 2 
ATOM   1979 H HD11 . ILE   B 1 13  ? 14.805 -15.219 33.88   1   53.897  ? 25  ILE   A HD11 1 c 2 
ATOM   1980 H HD12 . ILE   B 1 13  ? 13.879 -14.287 32.98   1   51.654  ? 25  ILE   A HD12 1 c 2 
ATOM   1981 H HD13 . ILE   B 1 13  ? 13.533 -14.503 34.518  1   53.432  ? 25  ILE   A HD13 1 c 2 
ATOM   1982 N N    . THR   B 1 14  ? 18.22  -10.793 34.403  1   47.466  ? 26  THR   A N    1 ? 2 
ATOM   1983 C CA   . THR   B 1 14  ? 19.184 -10.437 33.362  1   46.839  ? 26  THR   A CA   1 ? 2 
ATOM   1984 C C    . THR   B 1 14  ? 20.549 -10.526 34.018  1   56.228  ? 26  THR   A C    1 ? 2 
ATOM   1985 O O    . THR   B 1 14  ? 20.702 -10.298 35.239  1   56.171  ? 26  THR   A O    1 ? 2 
ATOM   1986 C CB   . THR   B 1 14  ? 18.953 -9.016  32.794  1   44.465  ? 26  THR   A CB   1 ? 2 
ATOM   1987 O OG1  . THR   B 1 14  ? 19.093 -8.054  33.833  1   47.041  ? 26  THR   A OG1  1 ? 2 
ATOM   1988 C CG2  . THR   B 1 14  ? 17.628 -8.772  32.06   1   39.507  ? 26  THR   A CG2  1 ? 2 
ATOM   1989 H H    . THR   B 1 14  ? 17.835 -10.124 34.89   1   49.301  ? 26  THR   A H    1 c 2 
ATOM   1990 H HA   . THR   B 1 14  ? 19.127 -11.089 32.63   1   46.971  ? 26  THR   A HA   1 c 2 
ATOM   1991 H HB   . THR   B 1 14  ? 19.666 -8.851  32.131  1   44.405  ? 26  THR   A HB   1 c 2 
ATOM   1992 H HG1  . THR   B 1 14  ? 18.518 -8.226  34.451  0   30      ? 26  THR   A HG1  1 c 2 
ATOM   1993 H HG21 . THR   B 1 14  ? 17.584 -7.848  31.764  1   39.877  ? 26  THR   A HG21 1 c 2 
ATOM   1994 H HG22 . THR   B 1 14  ? 16.887 -8.955  32.661  1   40.24   ? 26  THR   A HG22 1 c 2 
ATOM   1995 H HG23 . THR   B 1 14  ? 17.572 -9.361  31.289  1   39.284  ? 26  THR   A HG23 1 c 2 
ATOM   1996 N N    . SER   B 1 15  ? 21.541 -10.82  33.195  1   56.272  ? 27  SER   A N    1 ? 2 
ATOM   1997 C CA   . SER   B 1 15  ? 22.934 -10.864 33.59   1   62.678  ? 27  SER   A CA   1 ? 2 
ATOM   1998 C C    . SER   B 1 15  ? 23.413 -9.468  33.978  1   62.081  ? 27  SER   A C    1 ? 2 
ATOM   1999 O O    . SER   B 1 15  ? 24.128 -9.297  34.945  1   63.43   ? 27  SER   A O    1 ? 2 
ATOM   2000 C CB   . SER   B 1 15  ? 23.724 -11.388 32.41   1   65.22   ? 27  SER   A CB   1 ? 2 
ATOM   2001 O OG   . SER   B 1 15  ? 23.348 -12.746 32.254  1   70.448  ? 27  SER   A OG   1 ? 2 
ATOM   2002 H H    . SER   B 1 15  ? 21.336 -11.005 32.323  1   55.674  ? 27  SER   A H    1 c 2 
ATOM   2003 H HA   . SER   B 1 15  ? 23.039 -11.477 34.362  1   63.556  ? 27  SER   A HA   1 c 2 
ATOM   2004 H HB2  . SER   B 1 15  ? 23.506 -10.881 31.605  1   64.269  ? 27  SER   A HB2  1 c 2 
ATOM   2005 H HB3  . SER   B 1 15  ? 24.681 -11.321 32.59   1   67.871  ? 27  SER   A HB3  1 c 2 
ATOM   2006 H HG   . SER   B 1 15  ? 23.816 -13.022 31.522  0   30      ? 27  SER   A HG   1 c 2 
ATOM   2007 N N    . LYS   B 1 16  ? 23.025 -8.468  33.209  1   54.405  ? 28  LYS   A N    1 ? 2 
ATOM   2008 C CA   . LYS   B 1 16  ? 23.524 -7.111  33.411  1   62.764  ? 28  LYS   A CA   1 ? 2 
ATOM   2009 C C    . LYS   B 1 16  ? 22.819 -6.414  34.577  1   60.002  ? 28  LYS   A C    1 ? 2 
ATOM   2010 O O    . LYS   B 1 16  ? 23.226 -5.322  34.997  1   61.538  ? 28  LYS   A O    1 ? 2 
ATOM   2011 C CB   . LYS   B 1 16  ? 23.324 -6.302  32.135  1   67.585  ? 28  LYS   A CB   1 ? 2 
ATOM   2012 C CG   . LYS   B 1 16  ? 24.253 -6.761  30.993  1   74.276  ? 28  LYS   A CG   1 ? 2 
ATOM   2013 C CD   . LYS   B 1 16  ? 23.91  -6.197  29.618  1   68.299  ? 28  LYS   A CD   1 ? 2 
ATOM   2014 C CE   . LYS   B 1 16  ? 24.42  -4.806  29.423  1   76.997  ? 28  LYS   A CE   1 ? 2 
ATOM   2015 N NZ   . LYS   B 1 16  ? 23.99  -4.284  28.115  1   77.612  ? 28  LYS   A NZ   1 ? 2 
ATOM   2016 H H    . LYS   B 1 16  ? 22.435 -8.624  32.529  1   55.416  ? 28  LYS   A H    1 c 2 
ATOM   2017 H HA   . LYS   B 1 16  ? 24.494 -7.159  33.608  1   63.782  ? 28  LYS   A HA   1 c 2 
ATOM   2018 H HB2  . LYS   B 1 16  ? 22.393 -6.388  31.84   1   65.137  ? 28  LYS   A HB2  1 c 2 
ATOM   2019 H HB3  . LYS   B 1 16  ? 23.498 -5.355  32.322  1   67.897  ? 28  LYS   A HB3  1 c 2 
ATOM   2020 H HG2  . LYS   B 1 16  ? 25.172 -6.502  31.22   1   73.9    ? 28  LYS   A HG2  1 c 2 
ATOM   2021 H HG3  . LYS   B 1 16  ? 24.226 -7.741  30.946  1   71.517  ? 28  LYS   A HG3  1 c 2 
ATOM   2022 H HD2  . LYS   B 1 16  ? 24.295 -6.779  28.928  1   70.767  ? 28  LYS   A HD2  1 c 2 
ATOM   2023 H HD3  . LYS   B 1 16  ? 22.934 -6.198  29.506  1   69.074  ? 28  LYS   A HD3  1 c 2 
ATOM   2024 H HE2  . LYS   B 1 16  ? 24.075 -4.227  30.126  1   76.046  ? 28  LYS   A HE2  1 c 2 
ATOM   2025 H HE3  . LYS   B 1 16  ? 25.393 -4.799  29.467  1   77.581  ? 28  LYS   A HE3  1 c 2 
ATOM   2026 H HZ1  . LYS   B 1 16  ? 23.087 -4.335  28.046  1   75.099  ? 28  LYS   A HZ1  1 c 2 
ATOM   2027 H HZ2  . LYS   B 1 16  ? 24.366 -4.771  27.451  1   76.728  ? 28  LYS   A HZ2  1 c 2 
ATOM   2028 H HZ3  . LYS   B 1 16  ? 24.244 -3.419  28.032  1   77.476  ? 28  LYS   A HZ3  1 c 2 
ATOM   2029 N N    . LYS   B 1 17  ? 21.773 -7.064  35.089  1   55.59   ? 29  LYS   A N    1 ? 2 
ATOM   2030 C CA   . LYS   B 1 17  ? 20.928 -6.53   36.142  1   56.66   ? 29  LYS   A CA   1 ? 2 
ATOM   2031 C C    . LYS   B 1 17  ? 20.476 -5.118  35.748  1   57.085  ? 29  LYS   A C    1 ? 2 
ATOM   2032 O O    . LYS   B 1 17  ? 20.773 -4.17   36.485  1   55.027  ? 29  LYS   A O    1 ? 2 
ATOM   2033 C CB   . LYS   B 1 17  ? 21.647 -6.417  37.493  1   61.514  ? 29  LYS   A CB   1 ? 2 
ATOM   2034 C CG   . LYS   B 1 17  ? 22.024 -7.766  38.122  1   64.547  ? 29  LYS   A CG   1 ? 2 
ATOM   2035 C CD   . LYS   B 1 17  ? 20.883 -8.777  38.09   1   65.902  ? 29  LYS   A CD   1 ? 2 
ATOM   2036 C CE   . LYS   B 1 17  ? 21.38  -10.148 38.546  1   84.023  ? 29  LYS   A CE   1 ? 2 
ATOM   2037 N NZ   . LYS   B 1 17  ? 20.782 -11.249 37.765  1   83.445  ? 29  LYS   A NZ   1 ? 2 
ATOM   2038 H H    . LYS   B 1 17  ? 21.56  -7.885  34.752  1   55.495  ? 29  LYS   A H    1 c 2 
ATOM   2039 H HA   . LYS   B 1 17  ? 20.131 -7.105  36.226  1   55.911  ? 29  LYS   A HA   1 c 2 
ATOM   2040 H HB2  . LYS   B 1 17  ? 22.465 -5.889  37.378  1   62.89   ? 29  LYS   A HB2  1 c 2 
ATOM   2041 H HB3  . LYS   B 1 17  ? 21.067 -5.937  38.122  1   62.082  ? 29  LYS   A HB3  1 c 2 
ATOM   2042 H HG2  . LYS   B 1 17  ? 22.794 -8.134  37.637  1   65.32   ? 29  LYS   A HG2  1 c 2 
ATOM   2043 H HG3  . LYS   B 1 17  ? 22.295 -7.615  39.053  1   67.389  ? 29  LYS   A HG3  1 c 2 
ATOM   2044 H HD2  . LYS   B 1 17  ? 20.164 -8.477  38.687  1   68.369  ? 29  LYS   A HD2  1 c 2 
ATOM   2045 H HD3  . LYS   B 1 17  ? 20.525 -8.851  37.182  1   65.903  ? 29  LYS   A HD3  1 c 2 
ATOM   2046 H HE2  . LYS   B 1 17  ? 22.348 -10.195 38.459  1   81.244  ? 29  LYS   A HE2  1 c 2 
ATOM   2047 H HE3  . LYS   B 1 17  ? 21.157 -10.272 39.486  1   81.556  ? 29  LYS   A HE3  1 c 2 
ATOM   2048 H HZ1  . LYS   B 1 17  ? 21.024 -11.176 36.895  1   81.524  ? 29  LYS   A HZ1  1 c 2 
ATOM   2049 H HZ2  . LYS   B 1 17  ? 19.878 -11.211 37.826  1   81.611  ? 29  LYS   A HZ2  1 c 2 
ATOM   2050 H HZ3  . LYS   B 1 17  ? 21.068 -12.045 38.089  1   84.073  ? 29  LYS   A HZ3  1 c 2 
ATOM   2051 N N    . ASP   B 1 18  ? 19.825 -4.999  34.58   1   54.198  ? 30  ASP   A N    1 ? 2 
ATOM   2052 C CA   . ASP   B 1 18  ? 19.279 -3.733  34.123  1   49.095  ? 30  ASP   A CA   1 ? 2 
ATOM   2053 C C    . ASP   B 1 18  ? 17.77  -3.814  34.183  1   48.973  ? 30  ASP   A C    1 ? 2 
ATOM   2054 O O    . ASP   B 1 18  ? 17.092 -3.023  33.549  1   46.868  ? 30  ASP   A O    1 ? 2 
ATOM   2055 C CB   . ASP   B 1 18  ? 19.676 -3.491  32.69   1   50.876  ? 30  ASP   A CB   1 ? 2 
ATOM   2056 C CG   . ASP   B 1 18  ? 19.286 -4.589  31.706  1   44.453  ? 30  ASP   A CG   1 ? 2 
ATOM   2057 O OD1  . ASP   B 1 18  ? 18.395 -5.442  32.035  1   45.313  ? 30  ASP   A OD1  1 ? 2 
ATOM   2058 O OD2  . ASP   B 1 18  ? 19.95  -4.63   30.649  1   43.409  ? 30  ASP   A OD2  1 ? 2 
ATOM   2059 H H    . ASP   B 1 18  ? 19.715 -5.74   34.056  1   51.84   ? 30  ASP   A H    1 c 2 
ATOM   2060 H HA   . ASP   B 1 18  ? 19.599 -3.006  34.704  1   52.554  ? 30  ASP   A HA   1 c 2 
ATOM   2061 H HB2  . ASP   B 1 18  ? 19.284 -2.647  32.383  1   48.669  ? 30  ASP   A HB2  1 c 2 
ATOM   2062 H HB3  . ASP   B 1 18  ? 20.651 -3.392  32.656  1   50.391  ? 30  ASP   A HB3  1 c 2 
ATOM   2063 N N    . ARG   B 1 19  ? 17.212 -4.829  34.86   1   45.849  ? 31  ARG   A N    1 ? 2 
ATOM   2064 C CA   . ARG   B 1 19  ? 15.764 -4.952  35.008  1   44.351  ? 31  ARG   A CA   1 ? 2 
ATOM   2065 C C    . ARG   B 1 19  ? 15.043 -4.971  33.653  1   43.903  ? 31  ARG   A C    1 ? 2 
ATOM   2066 O O    . ARG   B 1 19  ? 13.86  -4.691  33.599  1   43.77   ? 31  ARG   A O    1 ? 2 
ATOM   2067 C CB   . ARG   B 1 19  ? 15.333 -3.795  35.93   1   51.03   ? 31  ARG   A CB   1 ? 2 
ATOM   2068 C CG   . ARG   B 1 19  ? 15.844 -4.065  37.345  1   55.061  ? 31  ARG   A CG   1 ? 2 
ATOM   2069 C CD   . ARG   B 1 19  ? 15.692 -2.902  38.222  1   57.276  ? 31  ARG   A CD   1 ? 2 
ATOM   2070 N NE   . ARG   B 1 19  ? 14.259 -2.639  38.353  1   57.109  ? 31  ARG   A NE   1 ? 2 
ATOM   2071 C CZ   . ARG   B 1 19  ? 13.386 -3.423  38.969  1   56.613  ? 31  ARG   A CZ   1 ? 2 
ATOM   2072 N NH1  . ARG   B 1 19  ? 13.707 -4.381  39.796  1   58.921  ? 31  ARG   A NH1  1 ? 2 
ATOM   2073 N NH2  . ARG   B 1 19  ? 12.121 -3.195  38.816  1   62.258  ? 31  ARG   A NH2  1 ? 2 
ATOM   2074 H H    . ARG   B 1 19  ? 17.745 -5.461  35.245  1   47.517  ? 31  ARG   A H    1 c 2 
ATOM   2075 H HA   . ARG   B 1 19  ? 15.573 -5.805  35.472  1   45.905  ? 31  ARG   A HA   1 c 2 
ATOM   2076 H HB2  . ARG   B 1 19  ? 15.694 -2.944  35.605  1   50.399  ? 31  ARG   A HB2  1 c 2 
ATOM   2077 H HB3  . ARG   B 1 19  ? 14.355 -3.733  35.946  1   49.58   ? 31  ARG   A HB3  1 c 2 
ATOM   2078 H HG2  . ARG   B 1 19  ? 15.358 -4.827  37.727  1   54.627  ? 31  ARG   A HG2  1 c 2 
ATOM   2079 H HG3  . ARG   B 1 19  ? 16.795 -4.304  37.305  1   55.322  ? 31  ARG   A HG3  1 c 2 
ATOM   2080 H HD2  . ARG   B 1 19  ? 16.077 -3.083  39.103  1   59.5    ? 31  ARG   A HD2  1 c 2 
ATOM   2081 H HD3  . ARG   B 1 19  ? 16.137 -2.12   37.836  1   57.654  ? 31  ARG   A HD3  1 c 2 
ATOM   2082 H HE   . ARG   B 1 19  ? 13.952 -1.905  37.998  1   56.595  ? 31  ARG   A HE   1 c 2 
ATOM   2083 H HH11 . ARG   B 1 19  ? 14.519 -4.73   39.786  1   58.96   ? 31  ARG   A HH11 1 c 2 
ATOM   2084 H HH12 . ARG   B 1 19  ? 13.108 -4.679  40.374  1   59.537  ? 31  ARG   A HH12 1 c 2 
ATOM   2085 H HH21 . ARG   B 1 19  ? 11.781 -2.429  39.098  1   61.246  ? 31  ARG   A HH21 1 c 2 
ATOM   2086 H HH22 . ARG   B 1 19  ? 11.609 -3.814  38.449  1   58.709  ? 31  ARG   A HH22 1 c 2 
ATOM   2087 N N    . GLY   B 1 20  ? 15.687 -5.494  32.598  1   41.413  ? 32  GLY   A N    1 ? 2 
ATOM   2088 C CA   . GLY   B 1 20  ? 15.029 -5.622  31.301  1   43.553  ? 32  GLY   A CA   1 ? 2 
ATOM   2089 C C    . GLY   B 1 20  ? 14.108 -6.845  31.177  1   44.003  ? 32  GLY   A C    1 ? 2 
ATOM   2090 O O    . GLY   B 1 20  ? 13.29  -6.938  30.243  1   41.164  ? 32  GLY   A O    1 ? 2 
ATOM   2091 H H    . GLY   B 1 20  ? 16.547 -5.789  32.688  1   43.348  ? 32  GLY   A H    1 c 2 
ATOM   2092 H HA2  . GLY   B 1 20  ? 14.504 -4.806  31.132  1   42.505  ? 32  GLY   A HA2  1 c 2 
ATOM   2093 H HA3  . GLY   B 1 20  ? 15.724 -5.674  30.604  1   42.47   ? 32  GLY   A HA3  1 c 2 
ATOM   2094 N N    . VAL   B 1 21  ? 14.29  -7.82   32.073  1   40.214  ? 33  VAL   A N    1 ? 2 
ATOM   2095 C CA   . VAL   B 1 21  ? 13.465 -8.991  32.119  1   41.711  ? 33  VAL   A CA   1 ? 2 
ATOM   2096 C C    . VAL   B 1 21  ? 13.156 -9.299  33.572  1   41.939  ? 33  VAL   A C    1 ? 2 
ATOM   2097 O O    . VAL   B 1 21  ? 14.082 -9.636  34.317  1   44.215  ? 33  VAL   A O    1 ? 2 
ATOM   2098 C CB   . VAL   B 1 21  ? 14.065 -10.252 31.452  1   37.916  ? 33  VAL   A CB   1 ? 2 
ATOM   2099 C CG1  . VAL   B 1 21  ? 13.088 -11.376 31.49   1   36.605  ? 33  VAL   A CG1  1 ? 2 
ATOM   2100 C CG2  . VAL   B 1 21  ? 14.472 -10.025 29.987  1   38.624  ? 33  VAL   A CG2  1 ? 2 
ATOM   2101 H H    . VAL   B 1 21  ? 14.968 -7.742  32.68   1   42.886  ? 33  VAL   A H    1 c 2 
ATOM   2102 H HA   . VAL   B 1 21  ? 12.626 -8.785  31.666  1   39.53   ? 33  VAL   A HA   1 c 2 
ATOM   2103 H HB   . VAL   B 1 21  ? 14.866 -10.51  31.966  1   39.808  ? 33  VAL   A HB   1 c 2 
ATOM   2104 H HG11 . VAL   B 1 21  ? 12.245 -11.086 31.104  1   36.088  ? 33  VAL   A HG11 1 c 2 
ATOM   2105 H HG12 . VAL   B 1 21  ? 12.944 -11.654 32.41   1   37.911  ? 33  VAL   A HG12 1 c 2 
ATOM   2106 H HG13 . VAL   B 1 21  ? 13.436 -12.126 30.979  1   36.823  ? 33  VAL   A HG13 1 c 2 
ATOM   2107 H HG21 . VAL   B 1 21  ? 14.837 -10.847 29.62   1   38.112  ? 33  VAL   A HG21 1 c 2 
ATOM   2108 H HG22 . VAL   B 1 21  ? 15.146 -9.325  29.942  1   38.383  ? 33  VAL   A HG22 1 c 2 
ATOM   2109 H HG23 . VAL   B 1 21  ? 13.694 -9.757  29.471  1   37.103  ? 33  VAL   A HG23 1 c 2 
ATOM   2110 N N    . LEU   B 1 22  ? 11.862 -9.249  33.897  1   43.782  ? 34  LEU   A N    1 ? 2 
ATOM   2111 C CA   . LEU   B 1 22  ? 11.393 -9.366  35.266  1   44.582  ? 34  LEU   A CA   1 ? 2 
ATOM   2112 C C    . LEU   B 1 22  ? 10.428 -10.547 35.314  1   40.762  ? 34  LEU   A C    1 ? 2 
ATOM   2113 O O    . LEU   B 1 22  ? 9.615  -10.712 34.449  1   39.297  ? 34  LEU   A O    1 ? 2 
ATOM   2114 C CB   . LEU   B 1 22  ? 10.805 -8.047  35.812  1   48.497  ? 34  LEU   A CB   1 ? 2 
ATOM   2115 C CG   . LEU   B 1 22  ? 11.737 -6.833  35.793  1   51.09   ? 34  LEU   A CG   1 ? 2 
ATOM   2116 C CD1  . LEU   B 1 22  ? 11.126 -5.53   36.268  1   52.269  ? 34  LEU   A CD1  1 ? 2 
ATOM   2117 C CD2  . LEU   B 1 22  ? 12.896 -7.013  36.724  1   50.962  ? 34  LEU   A CD2  1 ? 2 
ATOM   2118 H H    . LEU   B 1 22  ? 11.242 -9.139  33.235  1   41.984  ? 34  LEU   A H    1 c 2 
ATOM   2119 H HA   . LEU   B 1 22  ? 12.17  -9.605  35.822  1   45.696  ? 34  LEU   A HA   1 c 2 
ATOM   2120 H HB2  . LEU   B 1 22  ? 10.001 -7.829  35.287  1   47.297  ? 34  LEU   A HB2  1 c 2 
ATOM   2121 H HB3  . LEU   B 1 22  ? 10.521 -8.203  36.741  1   49.667  ? 34  LEU   A HB3  1 c 2 
ATOM   2122 H HG   . LEU   B 1 22  ? 12.083 -6.709  34.872  1   49.1    ? 34  LEU   A HG   1 c 2 
ATOM   2123 H HD11 . LEU   B 1 22  ? 10.355 -5.315  35.717  1   51.266  ? 34  LEU   A HD11 1 c 2 
ATOM   2124 H HD12 . LEU   B 1 22  ? 11.781 -4.815  36.197  1   52.679  ? 34  LEU   A HD12 1 c 2 
ATOM   2125 H HD13 . LEU   B 1 22  ? 10.845 -5.622  37.193  1   53.726  ? 34  LEU   A HD13 1 c 2 
ATOM   2126 H HD21 . LEU   B 1 22  ? 13.421 -7.778  36.441  1   51.123  ? 34  LEU   A HD21 1 c 2 
ATOM   2127 H HD22 . LEU   B 1 22  ? 12.568 -7.163  37.627  1   53.007  ? 34  LEU   A HD22 1 c 2 
ATOM   2128 H HD23 . LEU   B 1 22  ? 13.455 -6.218  36.711  1   52.172  ? 34  LEU   A HD23 1 c 2 
ATOM   2129 N N    . LYS   B 1 23  ? 10.601 -11.499 36.271  1   45.947  ? 35  LYS   A N    1 ? 2 
ATOM   2130 C CA   . LYS   B 1 23  ? 9.881  -12.771 36.227  1   40.374  ? 35  LYS   A CA   1 ? 2 
ATOM   2131 C C    . LYS   B 1 23  ? 9.169  -12.966 37.549  1   43.014  ? 35  LYS   A C    1 ? 2 
ATOM   2132 O O    . LYS   B 1 23  ? 9.78   -12.717 38.561  1   49.088  ? 35  LYS   A O    1 ? 2 
ATOM   2133 C CB   . LYS   B 1 23  ? 10.895 -13.904 36.143  1   45.789  ? 35  LYS   A CB   1 ? 2 
ATOM   2134 C CG   . LYS   B 1 23  ? 10.351 -15.342 36.253  1   43.658  ? 35  LYS   A CG   1 ? 2 
ATOM   2135 C CD   . LYS   B 1 23  ? 11.345 -16.455 36.601  1   46.66   ? 35  LYS   A CD   1 ? 2 
ATOM   2136 C CE   . LYS   B 1 23  ? 10.671 -17.796 36.351  1   46.64   ? 35  LYS   A CE   1 ? 2 
ATOM   2137 N NZ   . LYS   B 1 23  ? 11.393 -19.004 36.832  1   46.715  ? 35  LYS   A NZ   1 ? 2 
ATOM   2138 H H    . LYS   B 1 23  ? 11.179 -11.343 36.961  1   44.987  ? 35  LYS   A H    1 c 2 
ATOM   2139 H HA   . LYS   B 1 23  ? 9.244  -12.779 35.475  1   41.15   ? 35  LYS   A HA   1 c 2 
ATOM   2140 H HB2  . LYS   B 1 23  ? 11.368 -13.825 35.288  1   42.821  ? 35  LYS   A HB2  1 c 2 
ATOM   2141 H HB3  . LYS   B 1 23  ? 11.557 -13.775 36.855  1   45.213  ? 35  LYS   A HB3  1 c 2 
ATOM   2142 H HG2  . LYS   B 1 23  ? 9.64   -15.349 36.928  1   45.455  ? 35  LYS   A HG2  1 c 2 
ATOM   2143 H HG3  . LYS   B 1 23  ? 9.927  -15.567 35.396  1   43.414  ? 35  LYS   A HG3  1 c 2 
ATOM   2144 H HD2  . LYS   B 1 23  ? 12.145 -16.378 36.037  1   45.709  ? 35  LYS   A HD2  1 c 2 
ATOM   2145 H HD3  . LYS   B 1 23  ? 11.606 -16.388 37.546  1   47.775  ? 35  LYS   A HD3  1 c 2 
ATOM   2146 H HE2  . LYS   B 1 23  ? 9.793  -17.782 36.774  1   46.614  ? 35  LYS   A HE2  1 c 2 
ATOM   2147 H HE3  . LYS   B 1 23  ? 10.526 -17.891 35.393  1   44.969  ? 35  LYS   A HE3  1 c 2 
ATOM   2148 H HZ1  . LYS   B 1 23  ? 11.542 -18.938 37.723  1   48.655  ? 35  LYS   A HZ1  1 c 2 
ATOM   2149 H HZ2  . LYS   B 1 23  ? 12.187 -19.076 36.402  1   47.113  ? 35  LYS   A HZ2  1 c 2 
ATOM   2150 H HZ3  . LYS   B 1 23  ? 10.898 -19.743 36.666  1   47.53   ? 35  LYS   A HZ3  1 c 2 
ATOM   2151 N N    . ILE   B 1 24  ? 7.963  -13.504 37.539  1   46.126  ? 36  ILE   A N    1 ? 2 
ATOM   2152 C CA   . ILE   B 1 24  ? 7.306  -14.001 38.743  1   47.001  ? 36  ILE   A CA   1 ? 2 
ATOM   2153 C C    . ILE   B 1 24  ? 6.83   -15.407 38.44   1   47.425  ? 36  ILE   A C    1 ? 2 
ATOM   2154 O O    . ILE   B 1 24  ? 6.207  -15.636 37.383  1   42.631  ? 36  ILE   A O    1 ? 2 
ATOM   2155 C CB   . ILE   B 1 24  ? 6.092  -13.104 39.102  1   48.497  ? 36  ILE   A CB   1 ? 2 
ATOM   2156 C CG1  . ILE   B 1 24  ? 6.526  -11.662 39.102  1   55.39   ? 36  ILE   A CG1  1 ? 2 
ATOM   2157 C CG2  . ILE   B 1 24  ? 5.401  -13.527 40.41   1   49.8    ? 36  ILE   A CG2  1 ? 2 
ATOM   2158 C CD1  . ILE   B 1 24  ? 5.515  -10.727 38.485  1   60.286  ? 36  ILE   A CD1  1 ? 2 
ATOM   2159 H H    . ILE   B 1 24  ? 7.517  -13.567 36.744  1   43.829  ? 36  ILE   A H    1 c 2 
ATOM   2160 H HA   . ILE   B 1 24  ? 7.939  -14.015 39.487  1   48.753  ? 36  ILE   A HA   1 c 2 
ATOM   2161 H HB   . ILE   B 1 24  ? 5.437  -13.206 38.383  1   48.273  ? 36  ILE   A HB   1 c 2 
ATOM   2162 H HG12 . ILE   B 1 24  ? 6.685  -11.383 40.027  1   56.326  ? 36  ILE   A HG12 1 c 2 
ATOM   2163 H HG13 . ILE   B 1 24  ? 7.369  -11.575 38.617  1   53.484  ? 36  ILE   A HG13 1 c 2 
ATOM   2164 H HG21 . ILE   B 1 24  ? 4.655  -12.932 40.591  1   50.751  ? 36  ILE   A HG21 1 c 2 
ATOM   2165 H HG22 . ILE   B 1 24  ? 6.036  -13.479 41.144  1   51.494  ? 36  ILE   A HG22 1 c 2 
ATOM   2166 H HG23 . ILE   B 1 24  ? 5.073  -14.438 40.327  1   50.416  ? 36  ILE   A HG23 1 c 2 
ATOM   2167 H HD11 . ILE   B 1 24  ? 5.451  -10.902 37.527  1   56.873  ? 36  ILE   A HD11 1 c 2 
ATOM   2168 H HD12 . ILE   B 1 24  ? 5.797  -9.803  38.626  1   58.807  ? 36  ILE   A HD12 1 c 2 
ATOM   2169 H HD13 . ILE   B 1 24  ? 4.642  -10.866 38.899  1   59.588  ? 36  ILE   A HD13 1 c 2 
ATOM   2170 N N    . VAL   B 1 25  ? 7.103  -16.326 39.382  1   46.418  ? 37  VAL   A N    1 ? 2 
ATOM   2171 C CA   . VAL   B 1 25  ? 6.605  -17.681 39.382  1   47.603  ? 37  VAL   A CA   1 ? 2 
ATOM   2172 C C    . VAL   B 1 25  ? 5.159  -17.63  39.83   1   50.297  ? 37  VAL   A C    1 ? 2 
ATOM   2173 O O    . VAL   B 1 25  ? 4.912  -17.178 40.924  1   53.272  ? 37  VAL   A O    1 ? 2 
ATOM   2174 C CB   . VAL   B 1 25  ? 7.441  -18.54  40.373  1   50.993  ? 37  VAL   A CB   1 ? 2 
ATOM   2175 C CG1  . VAL   B 1 25  ? 6.867  -19.942 40.513  1   50.372  ? 37  VAL   A CG1  1 ? 2 
ATOM   2176 C CG2  . VAL   B 1 25  ? 8.905  -18.57  39.912  1   51.204  ? 37  VAL   A CG2  1 ? 2 
ATOM   2177 H H    . VAL   B 1 25  ? 7.635  -16.071 40.079  1   48.355  ? 37  VAL   A H    1 c 2 
ATOM   2178 H HA   . VAL   B 1 25  ? 6.665  -18.055 38.482  1   46.767  ? 37  VAL   A HA   1 c 2 
ATOM   2179 H HB   . VAL   B 1 25  ? 7.402  -18.099 41.254  1   51.957  ? 37  VAL   A HB   1 c 2 
ATOM   2180 H HG11 . VAL   B 1 25  ? 6.684  -20.308 39.631  1   49.731  ? 37  VAL   A HG11 1 c 2 
ATOM   2181 H HG12 . VAL   B 1 25  ? 6.043  -19.908 41.027  1   51.984  ? 37  VAL   A HG12 1 c 2 
ATOM   2182 H HG13 . VAL   B 1 25  ? 7.508  -20.511 40.972  1   52.298  ? 37  VAL   A HG13 1 c 2 
ATOM   2183 H HG21 . VAL   B 1 25  ? 9.405  -19.2   40.459  1   52.507  ? 37  VAL   A HG21 1 c 2 
ATOM   2184 H HG22 . VAL   B 1 25  ? 9.295  -17.685 40.004  1   50.518  ? 37  VAL   A HG22 1 c 2 
ATOM   2185 H HG23 . VAL   B 1 25  ? 8.947  -18.846 38.981  1   49.504  ? 37  VAL   A HG23 1 c 2 
ATOM   2186 N N    . LYS   B 1 26  ? 4.224  -18.161 39.056  1   50.735  ? 38  LYS   A N    1 ? 2 
ATOM   2187 C CA   . LYS   B 1 26  ? 2.819  -18.11  39.407  1   55.235  ? 38  LYS   A CA   1 ? 2 
ATOM   2188 C C    . LYS   B 1 26  ? 2.309  -19.487 39.786  1   53.556  ? 38  LYS   A C    1 ? 2 
ATOM   2189 O O    . LYS   B 1 26  ? 1.349  -19.6   40.556  1   52.273  ? 38  LYS   A O    1 ? 2 
ATOM   2190 C CB   . LYS   B 1 26  ? 1.955  -17.568 38.261  1   52.972  ? 38  LYS   A CB   1 ? 2 
ATOM   2191 C CG   . LYS   B 1 26  ? 2.37   -16.177 37.852  1   57.037  ? 38  LYS   A CG   1 ? 2 
ATOM   2192 C CD   . LYS   B 1 26  ? 2.304  -15.153 38.978  1   56.245  ? 38  LYS   A CD   1 ? 2 
ATOM   2193 C CE   . LYS   B 1 26  ? 1.067  -15.218 39.828  1   57.445  ? 38  LYS   A CE   1 ? 2 
ATOM   2194 N NZ   . LYS   B 1 26  ? 0.741  -13.846 40.22   1   60.371  ? 38  LYS   A NZ   1 ? 2 
ATOM   2195 H H    . LYS   B 1 26  ? 4.468  -18.56  38.271  1   50.065  ? 38  LYS   A H    1 c 2 
ATOM   2196 H HA   . LYS   B 1 26  ? 2.712  -17.516 40.19   1   54.872  ? 38  LYS   A HA   1 c 2 
ATOM   2197 H HB2  . LYS   B 1 26  ? 2.037  -18.163 37.486  1   53.526  ? 38  LYS   A HB2  1 c 2 
ATOM   2198 H HB3  . LYS   B 1 26  ? 1.014  -17.557 38.537  1   55.516  ? 38  LYS   A HB3  1 c 2 
ATOM   2199 H HG2  . LYS   B 1 26  ? 3.288  -16.213 37.506  1   53.946  ? 38  LYS   A HG2  1 c 2 
ATOM   2200 H HG3  . LYS   B 1 26  ? 1.787  -15.884 37.123  1   54.272  ? 38  LYS   A HG3  1 c 2 
ATOM   2201 H HD2  . LYS   B 1 26  ? 3.089  -15.275 39.556  1   56.858  ? 38  LYS   A HD2  1 c 2 
ATOM   2202 H HD3  . LYS   B 1 26  ? 2.372  -14.256 38.583  1   55.425  ? 38  LYS   A HD3  1 c 2 
ATOM   2203 H HE2  . LYS   B 1 26  ? 0.322  -15.593 39.327  1   58.172  ? 38  LYS   A HE2  1 c 2 
ATOM   2204 H HE3  . LYS   B 1 26  ? 1.224  -15.758 40.624  1   59.728  ? 38  LYS   A HE3  1 c 2 
ATOM   2205 H HZ1  . LYS   B 1 26  ? 0.492  -13.366 39.493  1   58.481  ? 38  LYS   A HZ1  1 c 2 
ATOM   2206 H HZ2  . LYS   B 1 26  ? 1.461  -13.454 40.607  1   59.69   ? 38  LYS   A HZ2  1 c 2 
ATOM   2207 H HZ3  . LYS   B 1 26  ? 0.057  -13.856 40.814  1   61.405  ? 38  LYS   A HZ3  1 c 2 
ATOM   2208 N N    . ARG   B 1 27  ? 2.847  -20.561 39.194  1   54.867  ? 39  ARG   A N    1 ? 2 
ATOM   2209 C CA   . ARG   B 1 27  ? 2.549  -21.889 39.725  1   59.756  ? 39  ARG   A CA   1 ? 2 
ATOM   2210 C C    . ARG   B 1 27  ? 3.868  -22.645 39.749  1   59.576  ? 39  ARG   A C    1 ? 2 
ATOM   2211 O O    . ARG   B 1 27  ? 4.611  -22.638 38.772  1   54.737  ? 39  ARG   A O    1 ? 2 
ATOM   2212 C CB   . ARG   B 1 27  ? 1.513  -22.719 38.96   1   62.433  ? 39  ARG   A CB   1 ? 2 
ATOM   2213 C CG   . ARG   B 1 27  ? 1.131  -24.078 39.522  1   66.125  ? 39  ARG   A CG   1 ? 2 
ATOM   2214 C CD   . ARG   B 1 27  ? 0.239  -24.941 38.636  1   66.414  ? 39  ARG   A CD   1 ? 2 
ATOM   2215 N NE   . ARG   B 1 27  ? 0.966  -25.259 37.398  1   66.185  ? 39  ARG   A NE   1 ? 2 
ATOM   2216 C CZ   . ARG   B 1 27  ? 0.466  -25.613 36.221  1   64.99   ? 39  ARG   A CZ   1 ? 2 
ATOM   2217 N NH1  . ARG   B 1 27  ? -0.814 -25.475 36.001  1   67.453  ? 39  ARG   A NH1  1 ? 2 
ATOM   2218 N NH2  . ARG   B 1 27  ? 1.24   -26.091 35.246  1   62.641  ? 39  ARG   A NH2  1 ? 2 
ATOM   2219 H H    . ARG   B 1 27  ? 3.385  -20.476 38.46   1   53.45   ? 39  ARG   A H    1 c 2 
ATOM   2220 H HA   . ARG   B 1 27  ? 2.232  -21.787 40.658  1   61.148  ? 39  ARG   A HA   1 c 2 
ATOM   2221 H HB2  . ARG   B 1 27  ? 0.696  -22.182 38.886  1   62.053  ? 39  ARG   A HB2  1 c 2 
ATOM   2222 H HB3  . ARG   B 1 27  ? 1.852  -22.852 38.049  1   60.689  ? 39  ARG   A HB3  1 c 2 
ATOM   2223 H HG2  . ARG   B 1 27  ? 1.953  -24.581 39.714  1   66.196  ? 39  ARG   A HG2  1 c 2 
ATOM   2224 H HG3  . ARG   B 1 27  ? 0.676  -23.943 40.381  1   67.407  ? 39  ARG   A HG3  1 c 2 
ATOM   2225 H HD2  . ARG   B 1 27  ? 0.001  -25.769 39.1    1   68.873  ? 39  ARG   A HD2  1 c 2 
ATOM   2226 H HD3  . ARG   B 1 27  ? -0.583 -24.454 38.423  1   66.698  ? 39  ARG   A HD3  1 c 2 
ATOM   2227 H HE   . ARG   B 1 27  ? 1.836  -25.21  37.436  1   64.918  ? 39  ARG   A HE   1 c 2 
ATOM   2228 H HH11 . ARG   B 1 27  ? -1.297 -24.91  36.48   1   67.13   ? 39  ARG   A HH11 1 c 2 
ATOM   2229 H HH12 . ARG   B 1 27  ? -1.199 -25.953 35.362  1   67.366  ? 39  ARG   A HH12 1 c 2 
ATOM   2230 H HH21 . ARG   B 1 27  ? 2.118  -26.003 35.299  1   62.342  ? 39  ARG   A HH21 1 c 2 
ATOM   2231 H HH22 . ARG   B 1 27  ? 0.874  -26.495 34.549  1   63.405  ? 39  ARG   A HH22 1 c 2 
ATOM   2232 N N    . VAL   B 1 28  ? 4.2    -23.201 40.918  1   61.467  ? 40  VAL   A N    1 ? 2 
ATOM   2233 C CA   . VAL   B 1 28  ? 5.498  -23.793 41.135  1   63.236  ? 40  VAL   A CA   1 ? 2 
ATOM   2234 C C    . VAL   B 1 28  ? 5.499  -25.129 40.405  1   65.049  ? 40  VAL   A C    1 ? 2 
ATOM   2235 O O    . VAL   B 1 28  ? 4.515  -25.856 40.411  1   67.338  ? 40  VAL   A O    1 ? 2 
ATOM   2236 C CB   . VAL   B 1 28  ? 5.81   -23.952 42.628  1   70.133  ? 40  VAL   A CB   1 ? 2 
ATOM   2237 C CG1  . VAL   B 1 28  ? 7.121  -24.679 42.821  1   72.194  ? 40  VAL   A CG1  1 ? 2 
ATOM   2238 C CG2  . VAL   B 1 28  ? 5.814  -22.614 43.35   1   65.907  ? 40  VAL   A CG2  1 ? 2 
ATOM   2239 H H    . VAL   B 1 28  ? 3.591  -23.214 41.599  1   63.385  ? 40  VAL   A H    1 c 2 
ATOM   2240 H HA   . VAL   B 1 28  ? 6.173  -23.213 40.736  1   62.548  ? 40  VAL   A HA   1 c 2 
ATOM   2241 H HB   . VAL   B 1 28  ? 5.094  -24.507 43.019  1   70.294  ? 40  VAL   A HB   1 c 2 
ATOM   2242 H HG11 . VAL   B 1 28  ? 7.785  -24.321 42.209  1   70.363  ? 40  VAL   A HG11 1 c 2 
ATOM   2243 H HG12 . VAL   B 1 28  ? 6.998  -25.625 42.648  1   72.878  ? 40  VAL   A HG12 1 c 2 
ATOM   2244 H HG13 . VAL   B 1 28  ? 7.428  -24.557 43.736  1   73.653  ? 40  VAL   A HG13 1 c 2 
ATOM   2245 H HG21 . VAL   B 1 28  ? 6.022  -22.752 44.29   1   69.231  ? 40  VAL   A HG21 1 c 2 
ATOM   2246 H HG22 . VAL   B 1 28  ? 4.939  -22.198 43.271  1   66.634  ? 40  VAL   A HG22 1 c 2 
ATOM   2247 H HG23 . VAL   B 1 28  ? 6.485  -22.033 42.954  1   65.572  ? 40  VAL   A HG23 1 c 2 
ATOM   2248 N N    . GLY   B 1 29  ? 6.602  -25.434 39.728  1   68.051  ? 41  GLY   A N    1 ? 2 
ATOM   2249 C CA   . GLY   B 1 29  ? 6.75   -26.703 39.038  1   69.092  ? 41  GLY   A CA   1 ? 2 
ATOM   2250 C C    . GLY   B 1 29  ? 7.323  -27.704 40.015  1   74.335  ? 41  GLY   A C    1 ? 2 
ATOM   2251 O O    . GLY   B 1 29  ? 7.104  -27.576 41.219  1   75.79   ? 41  GLY   A O    1 ? 2 
ATOM   2252 H H    . GLY   B 1 29  ? 7.288  -24.831 39.691  1   66.308  ? 41  GLY   A H    1 c 2 
ATOM   2253 H HA2  . GLY   B 1 29  ? 5.875  -27.012 38.707  1   69.556  ? 41  GLY   A HA2  1 c 2 
ATOM   2254 H HA3  . GLY   B 1 29  ? 7.357  -26.593 38.269  1   68.188  ? 41  GLY   A HA3  1 c 2 
ATOM   2255 N N    . ASN   B 1 30  ? 8.034  -28.692 39.486  1   70.923  ? 42  ASN   A N    1 ? 2 
ATOM   2256 C CA   . ASN   B 1 30  ? 8.573  -29.736 40.337  1   81.051  ? 42  ASN   A CA   1 ? 2 
ATOM   2257 C C    . ASN   B 1 30  ? 9.846  -30.246 39.691  1   78.637  ? 42  ASN   A C    1 ? 2 
ATOM   2258 O O    . ASN   B 1 30  ? 10.101 -29.966 38.513  1   67.63   ? 42  ASN   A O    1 ? 2 
ATOM   2259 C CB   . ASN   B 1 30  ? 7.625  -30.916 40.523  1   85.296  ? 42  ASN   A CB   1 ? 2 
ATOM   2260 C CG   . ASN   B 1 30  ? 7.043  -31.243 39.182  1   87.433  ? 42  ASN   A CG   1 ? 2 
ATOM   2261 O OD1  . ASN   B 1 30  ? 5.838  -31.069 38.996  1   94.378  ? 42  ASN   A OD1  1 ? 2 
ATOM   2262 N ND2  . ASN   B 1 30  ? 7.905  -31.509 38.211  1   88.1    ? 42  ASN   A ND2  1 ? 2 
ATOM   2263 H H    . ASN   B 1 30  ? 8.189  -28.719 38.585  1   72.166  ? 42  ASN   A H    1 c 2 
ATOM   2264 H HA   . ASN   B 1 30  ? 8.781  -29.363 41.223  1   80.269  ? 42  ASN   A HA   1 c 2 
ATOM   2265 H HB2  . ASN   B 1 30  ? 8.108  -31.69  40.876  1   87.725  ? 42  ASN   A HB2  1 c 2 
ATOM   2266 H HB3  . ASN   B 1 30  ? 6.911  -30.677 41.147  1   86.162  ? 42  ASN   A HB3  1 c 2 
ATOM   2267 H HD21 . ASN   B 1 30  ? 7.989  -30.949 37.527  1   85.603  ? 42  ASN   A HD21 1 c 2 
ATOM   2268 H HD22 . ASN   B 1 30  ? 8.393  -32.25  38.244  1   89.323  ? 42  ASN   A HD22 1 c 2 
ATOM   2269 N N    . GLY   B 1 31  ? 10.601 -31.016 40.488  1   76.707  ? 43  GLY   A N    1 ? 2 
ATOM   2270 C CA   . GLY   B 1 31  ? 11.896 -31.52  40.072  1   82.144  ? 43  GLY   A CA   1 ? 2 
ATOM   2271 C C    . GLY   B 1 31  ? 13.001 -30.5   40.351  1   83.15   ? 43  GLY   A C    1 ? 2 
ATOM   2272 O O    . GLY   B 1 31  ? 12.735 -29.318 40.58   1   86.062  ? 43  GLY   A O    1 ? 2 
ATOM   2273 H H    . GLY   B 1 31  ? 10.299 -31.226 41.325  1   80.626  ? 43  GLY   A H    1 c 2 
ATOM   2274 H HA2  . GLY   B 1 31  ? 12.089 -32.356 40.559  1   84.167  ? 43  GLY   A HA2  1 c 2 
ATOM   2275 H HA3  . GLY   B 1 31  ? 11.872 -31.728 39.109  1   80.362  ? 43  GLY   A HA3  1 c 2 
ATOM   2276 N N    . GLU   B 1 32  ? 14.247 -30.999 40.287  1   90.355  ? 44  GLU   A N    1 ? 2 
ATOM   2277 C CA   . GLU   B 1 32  ? 15.421 -30.197 40.575  1   84.878  ? 44  GLU   A CA   1 ? 2 
ATOM   2278 C C    . GLU   B 1 32  ? 15.901 -29.512 39.28   1   77.305  ? 44  GLU   A C    1 ? 2 
ATOM   2279 O O    . GLU   B 1 32  ? 16.419 -28.421 39.381  1   73.634  ? 44  GLU   A O    1 ? 2 
ATOM   2280 C CB   . GLU   B 1 32  ? 16.382 -31.095 41.369  1   86.92   ? 44  GLU   A CB   1 ? 2 
ATOM   2281 H H    . GLU   B 1 32  ? 14.361 -31.872 40.042  1   89.129  ? 44  GLU   A H    1 c 2 
ATOM   2282 H HA   . GLU   B 1 32  ? 15.145 -29.477 41.199  1   83.927  ? 44  GLU   A HA   1 c 2 
ATOM   2283 H HB2  . GLU   B 1 32  ? 17.238 -30.599 41.101  0   30      ? 44  GLU   A HB2  1 c 2 
ATOM   2284 H HB3  . GLU   B 1 32  ? 15.825 -31.47  41.934  0   30      ? 44  GLU   A HB3  1 c 2 
ATOM   2285 N N    . GLU   B 1 33  ? 15.631 -30.083 38.087  1   73.196  ? 45  GLU   A N    1 ? 2 
ATOM   2286 C CA   . GLU   B 1 33  ? 16.335 -29.719 36.872  1   75.134  ? 45  GLU   A CA   1 ? 2 
ATOM   2287 C C    . GLU   B 1 33  ? 15.525 -28.691 36.072  1   71.004  ? 45  GLU   A C    1 ? 2 
ATOM   2288 O O    . GLU   B 1 33  ? 14.305 -28.705 36.042  1   67.531  ? 45  GLU   A O    1 ? 2 
ATOM   2289 C CB   . GLU   B 1 33  ? 16.928 -30.849 36.019  1   82.456  ? 45  GLU   A CB   1 ? 2 
ATOM   2290 C CG   . GLU   B 1 33  ? 16.091 -32.092 35.677  1   83.809  ? 45  GLU   A CG   1 ? 2 
ATOM   2291 C CD   . GLU   B 1 33  ? 15.423 -32.806 36.845  1   90.13   ? 45  GLU   A CD   1 ? 2 
ATOM   2292 O OE1  . GLU   B 1 33  ? 15.994 -33.719 37.478  1   97.256  ? 45  GLU   A OE1  1 ? 2 
ATOM   2293 O OE2  . GLU   B 1 33  ? 14.288 -32.38  37.148  1   93.34   ? 45  GLU   A OE2  1 ? 2 
ATOM   2294 H H    . GLU   B 1 33  ? 14.965 -30.705 38.036  1   75.418  ? 45  GLU   A H    1 c 2 
ATOM   2295 H HA   . GLU   B 1 33  ? 17.148 -29.238 37.17   1   75.67   ? 45  GLU   A HA   1 c 2 
ATOM   2296 H HB2  . GLU   B 1 33  ? 17.215 -30.462 35.165  1   79.671  ? 45  GLU   A HB2  1 c 2 
ATOM   2297 H HB3  . GLU   B 1 33  ? 17.733 -31.175 36.473  1   83.443  ? 45  GLU   A HB3  1 c 2 
ATOM   2298 H HG2  . GLU   B 1 33  ? 15.392 -31.831 35.04   1   82.727  ? 45  GLU   A HG2  1 c 2 
ATOM   2299 H HG3  . GLU   B 1 33  ? 16.668 -32.738 35.217  1   86.404  ? 45  GLU   A HG3  1 c 2 
ATOM   2300 N N    . THR   B 1 34  ? 16.257 -27.779 35.44   1   67.242  ? 46  THR   A N    1 ? 2 
ATOM   2301 C CA   . THR   B 1 34  ? 15.705 -26.852 34.471  1   67.095  ? 46  THR   A CA   1 ? 2 
ATOM   2302 C C    . THR   B 1 34  ? 16.343 -27.109 33.102  1   68.486  ? 46  THR   A C    1 ? 2 
ATOM   2303 O O    . THR   B 1 34  ? 17.368 -27.739 32.955  1   62.716  ? 46  THR   A O    1 ? 2 
ATOM   2304 C CB   . THR   B 1 34  ? 16.052 -25.455 34.933  1   67.541  ? 46  THR   A CB   1 ? 2 
ATOM   2305 O OG1  . THR   B 1 34  ? 17.463 -25.564 35.027  1   63.747  ? 46  THR   A OG1  1 ? 2 
ATOM   2306 C CG2  . THR   B 1 34  ? 15.385 -25.08  36.238  1   74.549  ? 46  THR   A CG2  1 ? 2 
ATOM   2307 H H    . THR   B 1 34  ? 17.151 -27.729 35.623  1   69.608  ? 46  THR   A H    1 c 2 
ATOM   2308 H HA   . THR   B 1 34  ? 14.731 -26.958 34.42   1   66.274  ? 46  THR   A HA   1 c 2 
ATOM   2309 H HB   . THR   B 1 34  ? 15.817 -24.795 34.24   1   64.971  ? 46  THR   A HB   1 c 2 
ATOM   2310 H HG1  . THR   B 1 34  ? 17.69  -26.089 35.682  0   30      ? 46  THR   A HG1  1 c 2 
ATOM   2311 H HG21 . THR   B 1 34  ? 15.605 -24.16  36.462  1   71.495  ? 46  THR   A HG21 1 c 2 
ATOM   2312 H HG22 . THR   B 1 34  ? 15.698 -25.669 36.945  1   74.529  ? 46  THR   A HG22 1 c 2 
ATOM   2313 H HG23 . THR   B 1 34  ? 14.423 -25.168 36.148  1   71.307  ? 46  THR   A HG23 1 c 2 
ATOM   2314 N N    . PRO   B 1 35  ? 15.798 -26.607 32.003  1   69.366  ? 47  PRO   A N    1 ? 2 
ATOM   2315 C CA   . PRO   B 1 35  ? 16.448 -26.853 30.733  1   73.728  ? 47  PRO   A CA   1 ? 2 
ATOM   2316 C C    . PRO   B 1 35  ? 17.841 -26.224 30.594  1   80.54   ? 47  PRO   A C    1 ? 2 
ATOM   2317 O O    . PRO   B 1 35  ? 18.017 -25.061 30.967  1   74.75   ? 47  PRO   A O    1 ? 2 
ATOM   2318 C CB   . PRO   B 1 35  ? 15.455 -26.294 29.747  1   70.92   ? 47  PRO   A CB   1 ? 2 
ATOM   2319 C CG   . PRO   B 1 35  ? 14.456 -25.45  30.496  1   63.434  ? 47  PRO   A CG   1 ? 2 
ATOM   2320 C CD   . PRO   B 1 35  ? 14.569 -25.806 31.938  1   68.327  ? 47  PRO   A CD   1 ? 2 
ATOM   2321 H HA   . PRO   B 1 35  ? 16.516 -27.821 30.594  1   75.521  ? 47  PRO   A HA   1 c 2 
ATOM   2322 H HB2  . PRO   B 1 35  ? 15.911 -25.757 29.071  1   68.6    ? 47  PRO   A HB2  1 c 2 
ATOM   2323 H HB3  . PRO   B 1 35  ? 14.997 -27.021 29.281  1   70.325  ? 47  PRO   A HB3  1 c 2 
ATOM   2324 H HG2  . PRO   B 1 35  ? 14.648 -24.5   30.368  1   63.806  ? 47  PRO   A HG2  1 c 2 
ATOM   2325 H HG3  . PRO   B 1 35  ? 13.549 -25.628 30.175  1   64.808  ? 47  PRO   A HG3  1 c 2 
ATOM   2326 H HD2  . PRO   B 1 35  ? 14.646 -25.007 32.491  1   66.349  ? 47  PRO   A HD2  1 c 2 
ATOM   2327 H HD3  . PRO   B 1 35  ? 13.799 -26.33  32.235  1   67.758  ? 47  PRO   A HD3  1 c 2 
ATOM   2328 N N    . MET   B 1 36  ? 18.789 -27.045 30.082  1   76.062  ? 48  MET   A N    1 ? 2 
ATOM   2329 C CA   . MET   B 1 36  ? 20.093 -26.661 29.549  1   73.728  ? 48  MET   A CA   1 ? 2 
ATOM   2330 C C    . MET   B 1 36  ? 19.931 -26.084 28.124  1   72.499  ? 48  MET   A C    1 ? 2 
ATOM   2331 O O    . MET   B 1 36  ? 18.977 -26.406 27.37   1   63.359  ? 48  MET   A O    1 ? 2 
ATOM   2332 C CB   . MET   B 1 36  ? 21.021 -27.882 29.384  1   84.366  ? 48  MET   A CB   1 ? 2 
ATOM   2333 C CG   . MET   B 1 36  ? 21.394 -28.724 30.622  1   85.08   ? 48  MET   A CG   1 ? 2 
ATOM   2334 S SD   . MET   B 1 36  ? 22.527 -27.963 31.811  1   88.953  ? 48  MET   A SD   1 ? 2 
ATOM   2335 C CE   . MET   B 1 36  ? 21.414 -27.328 33.082  1   82.157  ? 48  MET   A CE   1 ? 2 
ATOM   2336 H H    . MET   B 1 36  ? 18.59  -27.937 30.07   1   78.338  ? 48  MET   A H    1 c 2 
ATOM   2337 H HA   . MET   B 1 36  ? 20.507 -25.986 30.145  1   75.329  ? 48  MET   A HA   1 c 2 
ATOM   2338 H HB2  . MET   B 1 36  ? 20.604 -28.482 28.73   1   82.415  ? 48  MET   A HB2  1 c 2 
ATOM   2339 H HB3  . MET   B 1 36  ? 21.856 -27.562 28.98   1   82.664  ? 48  MET   A HB3  1 c 2 
ATOM   2340 H HG2  . MET   B 1 36  ? 20.571 -28.956 31.097  1   85.58   ? 48  MET   A HG2  1 c 2 
ATOM   2341 H HG3  . MET   B 1 36  ? 21.797 -29.562 30.316  1   88.426  ? 48  MET   A HG3  1 c 2 
ATOM   2342 H HE1  . MET   B 1 36  ? 21.936 -27.013 33.843  1   84.379  ? 48  MET   A HE1  1 c 2 
ATOM   2343 H HE2  . MET   B 1 36  ? 20.892 -26.589 32.718  1   80.666  ? 48  MET   A HE2  1 c 2 
ATOM   2344 H HE3  . MET   B 1 36  ? 20.813 -28.039 33.372  1   83.938  ? 48  MET   A HE3  1 c 2 
ATOM   2345 N N    . ILE   B 1 37  ? 20.859 -25.183 27.74   1   70.081  ? 49  ILE   A N    1 ? 2 
ATOM   2346 C CA   . ILE   B 1 37  ? 20.914 -24.743 26.347  1   69.482  ? 49  ILE   A CA   1 ? 2 
ATOM   2347 C C    . ILE   B 1 37  ? 21.037 -25.972 25.439  1   67.189  ? 49  ILE   A C    1 ? 2 
ATOM   2348 O O    . ILE   B 1 37  ? 21.883 -26.845 25.636  1   63.531  ? 49  ILE   A O    1 ? 2 
ATOM   2349 C CB   . ILE   B 1 37  ? 22.072 -23.752 26.11   1   73.922  ? 49  ILE   A CB   1 ? 2 
ATOM   2350 C CG1  . ILE   B 1 37  ? 21.779 -22.4   26.77   1   75.124  ? 49  ILE   A CG1  1 ? 2 
ATOM   2351 C CG2  . ILE   B 1 37  ? 22.367 -23.564 24.614  1   71.345  ? 49  ILE   A CG2  1 ? 2 
ATOM   2352 C CD1  . ILE   B 1 37  ? 23.006 -21.533 26.882  1   75.613  ? 49  ILE   A CD1  1 ? 2 
ATOM   2353 H H    . ILE   B 1 37  ? 21.456 -24.845 28.344  1   71.364  ? 49  ILE   A H    1 c 2 
ATOM   2354 H HA   . ILE   B 1 37  ? 20.076 -24.286 26.139  1   66.863  ? 49  ILE   A HA   1 c 2 
ATOM   2355 H HB   . ILE   B 1 37  ? 22.873 -24.123 26.531  1   75.368  ? 49  ILE   A HB   1 c 2 
ATOM   2356 H HG12 . ILE   B 1 37  ? 21.101 -21.928 26.244  1   72.217  ? 49  ILE   A HG12 1 c 2 
ATOM   2357 H HG13 . ILE   B 1 37  ? 21.414 -22.553 27.666  1   74.094  ? 49  ILE   A HG13 1 c 2 
ATOM   2358 H HG21 . ILE   B 1 37  ? 23.053 -22.887 24.497  1   72.129  ? 49  ILE   A HG21 1 c 2 
ATOM   2359 H HG22 . ILE   B 1 37  ? 21.558 -23.283 24.155  1   70.214  ? 49  ILE   A HG22 1 c 2 
ATOM   2360 H HG23 . ILE   B 1 37  ? 22.679 -24.402 24.232  1   74.025  ? 49  ILE   A HG23 1 c 2 
ATOM   2361 H HD11 . ILE   B 1 37  ? 23.706 -22.009 27.367  1   77.878  ? 49  ILE   A HD11 1 c 2 
ATOM   2362 H HD12 . ILE   B 1 37  ? 22.768 -20.722 27.367  1   74.323  ? 49  ILE   A HD12 1 c 2 
ATOM   2363 H HD13 . ILE   B 1 37  ? 23.331 -21.293 25.994  1   75.559  ? 49  ILE   A HD13 1 c 2 
ATOM   2364 N N    . GLY   B 1 38  ? 20.205 -26.012 24.406  1   63.071  ? 50  GLY   A N    1 ? 2 
ATOM   2365 C CA   . GLY   B 1 38  ? 20.301 -27.085 23.432  1   63.225  ? 50  GLY   A CA   1 ? 2 
ATOM   2366 C C    . GLY   B 1 38  ? 19.155 -28.068 23.582  1   66.07   ? 50  GLY   A C    1 ? 2 
ATOM   2367 O O    . GLY   B 1 38  ? 18.847 -28.797 22.651  1   69.458  ? 50  GLY   A O    1 ? 2 
ATOM   2368 H H    . GLY   B 1 38  ? 19.568 -25.365 24.299  1   61.182  ? 50  GLY   A H    1 c 2 
ATOM   2369 H HA2  . GLY   B 1 38  ? 20.286 -26.699 22.525  1   63.653  ? 50  GLY   A HA2  1 c 2 
ATOM   2370 H HA3  . GLY   B 1 38  ? 21.159 -27.558 23.545  1   66.53   ? 50  GLY   A HA3  1 c 2 
ATOM   2371 N N    . ASP   B 1 39  ? 18.498 -28.033 24.741  1   66.229  ? 51  ASP   A N    1 ? 2 
ATOM   2372 C CA   . ASP   B 1 39  ? 17.331 -28.864 24.949  1   64.249  ? 51  ASP   A CA   1 ? 2 
ATOM   2373 C C    . ASP   B 1 39  ? 16.189 -28.421 24.034  1   60.924  ? 51  ASP   A C    1 ? 2 
ATOM   2374 O O    . ASP   B 1 39  ? 16.024 -27.224 23.781  1   58.361  ? 51  ASP   A O    1 ? 2 
ATOM   2375 C CB   . ASP   B 1 39  ? 16.86  -28.789 26.392  1   65.42   ? 51  ASP   A CB   1 ? 2 
ATOM   2376 C CG   . ASP   B 1 39  ? 17.744 -29.457 27.436  1   65.746  ? 51  ASP   A CG   1 ? 2 
ATOM   2377 O OD1  . ASP   B 1 39  ? 18.624 -30.257 27.068  1   67.784  ? 51  ASP   A OD1  1 ? 2 
ATOM   2378 O OD2  . ASP   B 1 39  ? 17.493 -29.186 28.638  1   65.531  ? 51  ASP   A OD2  1 ? 2 
ATOM   2379 H H    . ASP   B 1 39  ? 18.782 -27.489 25.417  1   64.548  ? 51  ASP   A H    1 c 2 
ATOM   2380 H HA   . ASP   B 1 39  ? 17.568 -29.794 24.741  1   67.268  ? 51  ASP   A HA   1 c 2 
ATOM   2381 H HB2  . ASP   B 1 39  ? 16.767 -27.845 26.638  1   62.378  ? 51  ASP   A HB2  1 c 2 
ATOM   2382 H HB3  . ASP   B 1 39  ? 15.971 -29.199 26.451  1   64.447  ? 51  ASP   A HB3  1 c 2 
ATOM   2383 N N    . LYS   B 1 40  ? 15.401 -29.41  23.572  1   63.4    ? 52  LYS   A N    1 ? 2 
ATOM   2384 C CA   . LYS   B 1 40  ? 14.13  -29.122 22.933  1   62.107  ? 52  LYS   A CA   1 ? 2 
ATOM   2385 C C    . LYS   B 1 40  ? 13.11  -28.905 24.05   1   62.803  ? 52  LYS   A C    1 ? 2 
ATOM   2386 O O    . LYS   B 1 40  ? 13.062 -29.653 25.006  1   70.542  ? 52  LYS   A O    1 ? 2 
ATOM   2387 C CB   . LYS   B 1 40  ? 13.634 -30.126 21.892  1   60.684  ? 52  LYS   A CB   1 ? 2 
ATOM   2388 H H    . LYS   B 1 40  ? 15.666 -30.28  23.66   1   65.444  ? 52  LYS   A H    1 c 2 
ATOM   2389 H HA   . LYS   B 1 40  ? 14.23  -28.263 22.451  1   60.032  ? 52  LYS   A HA   1 c 2 
ATOM   2390 H HB2  . LYS   B 1 40  ? 14.507 -30.705 21.679  0   30      ? 52  LYS   A HB2  1 c 2 
ATOM   2391 H HB3  . LYS   B 1 40  ? 12.716 -30.319 21.991  0   30      ? 52  LYS   A HB3  1 c 2 
ATOM   2392 N N    . VAL   B 1 41  ? 12.328 -27.838 23.943  1   58.822  ? 53  VAL   A N    1 ? 2 
ATOM   2393 C CA   . VAL   B 1 41  ? 11.489 -27.333 25.021  1   54.857  ? 53  VAL   A CA   1 ? 2 
ATOM   2394 C C    . VAL   B 1 41  ? 10.072 -27.208 24.483  1   54.725  ? 53  VAL   A C    1 ? 2 
ATOM   2395 O O    . VAL   B 1 41  ? 9.872  -26.715 23.37   1   52.643  ? 53  VAL   A O    1 ? 2 
ATOM   2396 C CB   . VAL   B 1 41  ? 12.008 -25.968 25.5    1   56.86   ? 53  VAL   A CB   1 ? 2 
ATOM   2397 C CG1  . VAL   B 1 41  ? 11.053 -25.355 26.482  1   58.688  ? 53  VAL   A CG1  1 ? 2 
ATOM   2398 C CG2  . VAL   B 1 41  ? 13.353 -26.12  26.18   1   60.364  ? 53  VAL   A CG2  1 ? 2 
ATOM   2399 H H    . VAL   B 1 41  ? 12.312 -27.394 23.145  1   57.847  ? 53  VAL   A H    1 c 2 
ATOM   2400 H HA   . VAL   B 1 41  ? 11.501 -27.964 25.766  1   57.391  ? 53  VAL   A HA   1 c 2 
ATOM   2401 H HB   . VAL   B 1 41  ? 12.098 -25.38  24.713  1   55.992  ? 53  VAL   A HB   1 c 2 
ATOM   2402 H HG11 . VAL   B 1 41  ? 10.83  -26.008 27.166  1   58.732  ? 53  VAL   A HG11 1 c 2 
ATOM   2403 H HG12 . VAL   B 1 41  ? 10.244 -25.079 26.022  1   56.865  ? 53  VAL   A HG12 1 c 2 
ATOM   2404 H HG13 . VAL   B 1 41  ? 11.467 -24.582 26.897  1   56.402  ? 53  VAL   A HG13 1 c 2 
ATOM   2405 H HG21 . VAL   B 1 41  ? 13.645 -25.257 26.521  1   58.234  ? 53  VAL   A HG21 1 c 2 
ATOM   2406 H HG22 . VAL   B 1 41  ? 14.006 -26.451 25.54   1   60.594  ? 53  VAL   A HG22 1 c 2 
ATOM   2407 H HG23 . VAL   B 1 41  ? 13.276 -26.749 26.917  1   60.811  ? 53  VAL   A HG23 1 c 2 
ATOM   2408 N N    . TYR   B 1 42  ? 9.086  -27.641 25.28   1   53.052  ? 54  TYR   A N    1 ? 2 
ATOM   2409 C CA   . TYR   B 1 42  ? 7.699  -27.583 24.865  1   52.825  ? 54  TYR   A CA   1 ? 2 
ATOM   2410 C C    . TYR   B 1 42  ? 6.953  -26.698 25.864  1   50.633  ? 54  TYR   A C    1 ? 2 
ATOM   2411 O O    . TYR   B 1 42  ? 7.04   -26.951 27.074  1   49.07   ? 54  TYR   A O    1 ? 2 
ATOM   2412 C CB   . TYR   B 1 42  ? 7.079  -28.98  24.848  1   56.804  ? 54  TYR   A CB   1 ? 2 
ATOM   2413 C CG   . TYR   B 1 42  ? 7.81   -30.063 24.053  1   60.948  ? 54  TYR   A CG   1 ? 2 
ATOM   2414 C CD1  . TYR   B 1 42  ? 9.028  -30.572 24.46   1   62.48   ? 54  TYR   A CD1  1 ? 2 
ATOM   2415 C CD2  . TYR   B 1 42  ? 7.259  -30.577 22.893  1   69.011  ? 54  TYR   A CD2  1 ? 2 
ATOM   2416 C CE1  . TYR   B 1 42  ? 9.667  -31.588 23.747  1   70.71   ? 54  TYR   A CE1  1 ? 2 
ATOM   2417 C CE2  . TYR   B 1 42  ? 7.874  -31.601 22.176  1   70.123  ? 54  TYR   A CE2  1 ? 2 
ATOM   2418 C CZ   . TYR   B 1 42  ? 9.091  -32.096 22.597  1   72.777  ? 54  TYR   A CZ   1 ? 2 
ATOM   2419 O OH   . TYR   B 1 42  ? 9.69   -33.073 21.851  1   84.465  ? 54  TYR   A OH   1 ? 2 
ATOM   2420 H H    . TYR   B 1 42  ? 9.286  -27.982 26.104  1   54.191  ? 54  TYR   A H    1 c 2 
ATOM   2421 H HA   . TYR   B 1 42  ? 7.639  -27.185 23.958  1   52.506  ? 54  TYR   A HA   1 c 2 
ATOM   2422 H HB2  . TYR   B 1 42  ? 6.996  -29.286 25.778  1   57.408  ? 54  TYR   A HB2  1 c 2 
ATOM   2423 H HB3  . TYR   B 1 42  ? 6.165  -28.9   24.494  1   57.149  ? 54  TYR   A HB3  1 c 2 
ATOM   2424 H HD1  . TYR   B 1 42  ? 9.426  -30.245 25.251  1   62.676  ? 54  TYR   A HD1  1 c 2 
ATOM   2425 H HD2  . TYR   B 1 42  ? 6.42   -30.257 22.603  1   66.562  ? 54  TYR   A HD2  1 c 2 
ATOM   2426 H HE1  . TYR   B 1 42  ? 10.498 -31.919 24.041  1   70.292  ? 54  TYR   A HE1  1 c 2 
ATOM   2427 H HE2  . TYR   B 1 42  ? 7.479  -31.929 21.386  1   72.271  ? 54  TYR   A HE2  1 c 2 
ATOM   2428 H HH   . TYR   B 1 42  ? 10.425 -33.217 22.248  0   30      ? 54  TYR   A HH   1 c 2 
ATOM   2429 N N    . VAL   B 1 43  ? 6.207  -25.7   25.367  1   52.439  ? 55  VAL   A N    1 ? 2 
ATOM   2430 C CA   . VAL   B 1 43  ? 5.499  -24.785 26.257  1   51.549  ? 55  VAL   A CA   1 ? 2 
ATOM   2431 C C    . VAL   B 1 43  ? 4.101  -24.509 25.721  1   50.198  ? 55  VAL   A C    1 ? 2 
ATOM   2432 O O    . VAL   B 1 43  ? 3.795  -24.799 24.552  1   57.776  ? 55  VAL   A O    1 ? 2 
ATOM   2433 C CB   . VAL   B 1 43  ? 6.243  -23.458 26.449  1   53.147  ? 55  VAL   A CB   1 ? 2 
ATOM   2434 C CG1  . VAL   B 1 43  ? 7.709  -23.611 26.844  1   51.761  ? 55  VAL   A CG1  1 ? 2 
ATOM   2435 C CG2  . VAL   B 1 43  ? 6.157  -22.602 25.186  1   57.732  ? 55  VAL   A CG2  1 ? 2 
ATOM   2436 H H    . VAL   B 1 43  ? 6.136  -25.587 24.463  1   51.636  ? 55  VAL   A H    1 c 2 
ATOM   2437 H HA   . VAL   B 1 43  ? 5.411  -25.214 27.127  1   52.548  ? 55  VAL   A HA   1 c 2 
ATOM   2438 H HB   . VAL   B 1 43  ? 5.786  -22.969 27.172  1   52.563  ? 55  VAL   A HB   1 c 2 
ATOM   2439 H HG11 . VAL   B 1 43  ? 8.197  -24.037 26.121  1   52.683  ? 55  VAL   A HG11 1 c 2 
ATOM   2440 H HG12 . VAL   B 1 43  ? 7.774  -24.158 27.645  1   53.126  ? 55  VAL   A HG12 1 c 2 
ATOM   2441 H HG13 . VAL   B 1 43  ? 8.092  -22.735 27.02   1   50.834  ? 55  VAL   A HG13 1 c 2 
ATOM   2442 H HG21 . VAL   B 1 43  ? 6.782  -21.861 25.254  1   54.405  ? 55  VAL   A HG21 1 c 2 
ATOM   2443 H HG22 . VAL   B 1 43  ? 5.256  -22.254 25.087  1   55.658  ? 55  VAL   A HG22 1 c 2 
ATOM   2444 H HG23 . VAL   B 1 43  ? 6.382  -23.143 24.41   1   56.633  ? 55  VAL   A HG23 1 c 2 
ATOM   2445 N N    . HIS   B 1 44  ? 3.244  -23.927 26.587  1   46.459  ? 56  HIS   A N    1 ? 2 
ATOM   2446 C CA   . HIS   B 1 44  ? 2.064  -23.206 26.175  1   45.067  ? 56  HIS   A CA   1 ? 2 
ATOM   2447 C C    . HIS   B 1 44  ? 2.351  -21.759 26.575  1   45.286  ? 56  HIS   A C    1 ? 2 
ATOM   2448 O O    . HIS   B 1 44  ? 3.153  -21.532 27.486  1   42.661  ? 56  HIS   A O    1 ? 2 
ATOM   2449 C CB   . HIS   B 1 44  ? 0.791  -23.731 26.856  1   50.13   ? 56  HIS   A CB   1 ? 2 
ATOM   2450 C CG   . HIS   B 1 44  ? 0.084  -24.721 25.964  1   60.672  ? 56  HIS   A CG   1 ? 2 
ATOM   2451 N ND1  . HIS   B 1 44  ? -0.218 -24.447 24.631  1   62.101  ? 56  HIS   A ND1  1 ? 2 
ATOM   2452 C CD2  . HIS   B 1 44  ? -0.342 -25.96  26.206  1   59.802  ? 56  HIS   A CD2  1 ? 2 
ATOM   2453 C CE1  . HIS   B 1 44  ? -0.844 -25.48  24.102  1   64.74   ? 56  HIS   A CE1  1 ? 2 
ATOM   2454 N NE2  . HIS   B 1 44  ? -0.941 -26.407 25.043  1   62.667  ? 56  HIS   A NE2  1 ? 2 
ATOM   2455 H H    . HIS   B 1 44  ? 3.419  -23.992 27.482  1   47.029  ? 56  HIS   A H    1 c 2 
ATOM   2456 H HA   . HIS   B 1 44  ? 1.978  -23.251 25.193  1   46.715  ? 56  HIS   A HA   1 c 2 
ATOM   2457 H HB2  . HIS   B 1 44  ? 1.035  -24.169 27.7    1   51.477  ? 56  HIS   A HB2  1 c 2 
ATOM   2458 H HB3  . HIS   B 1 44  ? 0.191  -22.977 27.044  1   50.529  ? 56  HIS   A HB3  1 c 2 
ATOM   2459 H HD1  . HIS   B 1 44  ? -0.024 -23.7   24.169  0   30      ? 56  HIS   A HD1  1 c 2 
ATOM   2460 H HD2  . HIS   B 1 44  ? -0.293 -26.427 27.016  1   61.518  ? 56  HIS   A HD2  1 c 2 
ATOM   2461 H HE1  . HIS   B 1 44  ? -1.159 -25.55  23.217  1   64.733  ? 56  HIS   A HE1  1 c 2 
ATOM   2462 H HE2  . HIS   B 1 44  ? -1.32  -27.199 24.897  0   30      ? 56  HIS   A HE2  1 c 2 
ATOM   2463 N N    . TYR   B 1 45  ? 1.697  -20.79  25.919  1   44.541  ? 57  TYR   A N    1 ? 2 
ATOM   2464 C CA   . TYR   B 1 45  ? 1.949  -19.398 26.286  1   43.382  ? 57  TYR   A CA   1 ? 2 
ATOM   2465 C C    . TYR   B 1 45  ? 0.735  -18.54  25.904  1   44.194  ? 57  TYR   A C    1 ? 2 
ATOM   2466 O O    . TYR   B 1 45  ? -0.075 -18.868 24.999  1   44.338  ? 57  TYR   A O    1 ? 2 
ATOM   2467 C CB   . TYR   B 1 45  ? 3.305  -18.927 25.707  1   40.356  ? 57  TYR   A CB   1 ? 2 
ATOM   2468 C CG   . TYR   B 1 45  ? 3.23   -18.583 24.226  1   41.873  ? 57  TYR   A CG   1 ? 2 
ATOM   2469 C CD1  . TYR   B 1 45  ? 2.81   -17.329 23.764  1   37.487  ? 57  TYR   A CD1  1 ? 2 
ATOM   2470 C CD2  . TYR   B 1 45  ? 3.558  -19.543 23.282  1   42.354  ? 57  TYR   A CD2  1 ? 2 
ATOM   2471 C CE1  . TYR   B 1 45  ? 2.696  -17.092 22.401  1   40.153  ? 57  TYR   A CE1  1 ? 2 
ATOM   2472 C CE2  . TYR   B 1 45  ? 3.491  -19.299 21.926  1   41.09   ? 57  TYR   A CE2  1 ? 2 
ATOM   2473 C CZ   . TYR   B 1 45  ? 3.062  -18.072 21.485  1   43.789  ? 57  TYR   A CZ   1 ? 2 
ATOM   2474 O OH   . TYR   B 1 45  ? 3.008  -17.85  20.154  1   44.333  ? 57  TYR   A OH   1 ? 2 
ATOM   2475 H H    . TYR   B 1 45  ? 1.105  -20.988 25.252  1   45.544  ? 57  TYR   A H    1 c 2 
ATOM   2476 H HA   . TYR   B 1 45  ? 2.028  -19.369 27.273  1   43.154  ? 57  TYR   A HA   1 c 2 
ATOM   2477 H HB2  . TYR   B 1 45  ? 3.601  -18.133 26.205  1   40.07   ? 57  TYR   A HB2  1 c 2 
ATOM   2478 H HB3  . TYR   B 1 45  ? 3.972  -19.637 25.838  1   41.364  ? 57  TYR   A HB3  1 c 2 
ATOM   2479 H HD1  . TYR   B 1 45  ? 2.548  -16.663 24.379  1   38.411  ? 57  TYR   A HD1  1 c 2 
ATOM   2480 H HD2  . TYR   B 1 45  ? 3.85   -20.391 23.576  1   42.847  ? 57  TYR   A HD2  1 c 2 
ATOM   2481 H HE1  . TYR   B 1 45  ? 2.427  -16.244 22.096  1   39.775  ? 57  TYR   A HE1  1 c 2 
ATOM   2482 H HE2  . TYR   B 1 45  ? 3.727  -19.969 21.308  1   43.154  ? 57  TYR   A HE2  1 c 2 
ATOM   2483 H HH   . TYR   B 1 45  ? 2.744  -17.027 19.995  0   30      ? 57  TYR   A HH   1 c 2 
ATOM   2484 N N    . LYS   B 1 46  ? 0.628  -17.424 26.625  1   43.423  ? 58  LYS   A N    1 ? 2 
ATOM   2485 C CA   . LYS   B 1 46  ? -0.205 -16.307 26.25   1   42.36   ? 58  LYS   A CA   1 ? 2 
ATOM   2486 C C    . LYS   B 1 46  ? 0.717  -15.101 26.263  1   42.361  ? 58  LYS   A C    1 ? 2 
ATOM   2487 O O    . LYS   B 1 46  ? 1.416  -14.845 27.221  1   40.752  ? 58  LYS   A O    1 ? 2 
ATOM   2488 C CB   . LYS   B 1 46  ? -1.394 -16.12  27.183  1   46.966  ? 58  LYS   A CB   1 ? 2 
ATOM   2489 C CG   . LYS   B 1 46  ? -2.151 -17.394 27.427  1   49.007  ? 58  LYS   A CG   1 ? 2 
ATOM   2490 C CD   . LYS   B 1 46  ? -3.203 -17.3   28.506  1   51.911  ? 58  LYS   A CD   1 ? 2 
ATOM   2491 C CE   . LYS   B 1 46  ? -3.666 -18.694 28.815  1   56.179  ? 58  LYS   A CE   1 ? 2 
ATOM   2492 N NZ   . LYS   B 1 46  ? -4.881 -18.649 29.615  1   57.9    ? 58  LYS   A NZ   1 ? 2 
ATOM   2493 H H    . LYS   B 1 46  ? 1.106  -17.361 27.401  1   42.747  ? 58  LYS   A H    1 c 2 
ATOM   2494 H HA   . LYS   B 1 46  ? -0.535 -16.452 25.327  1   43.948  ? 58  LYS   A HA   1 c 2 
ATOM   2495 H HB2  . LYS   B 1 46  ? -1.076 -15.773 28.044  1   45.804  ? 58  LYS   A HB2  1 c 2 
ATOM   2496 H HB3  . LYS   B 1 46  ? -2.006 -15.458 26.796  1   46.564  ? 58  LYS   A HB3  1 c 2 
ATOM   2497 H HG2  . LYS   B 1 46  ? -2.582 -17.664 26.587  1   49.998  ? 58  LYS   A HG2  1 c 2 
ATOM   2498 H HG3  . LYS   B 1 46  ? -1.511 -18.096 27.671  1   49.028  ? 58  LYS   A HG3  1 c 2 
ATOM   2499 H HD2  . LYS   B 1 46  ? -2.822 -16.892 29.314  1   51.572  ? 58  LYS   A HD2  1 c 2 
ATOM   2500 H HD3  . LYS   B 1 46  ? -3.961 -16.76  28.193  1   52.867  ? 58  LYS   A HD3  1 c 2 
ATOM   2501 H HE2  . LYS   B 1 46  ? -3.848 -19.174 27.986  1   56.03   ? 58  LYS   A HE2  1 c 2 
ATOM   2502 H HE3  . LYS   B 1 46  ? -2.975 -19.174 29.305  1   55.074  ? 58  LYS   A HE3  1 c 2 
ATOM   2503 H HZ1  . LYS   B 1 46  ? -5.529 -18.199 29.169  1   58.63   ? 58  LYS   A HZ1  1 c 2 
ATOM   2504 H HZ2  . LYS   B 1 46  ? -4.714 -18.229 30.401  1   57.752  ? 58  LYS   A HZ2  1 c 2 
ATOM   2505 H HZ3  . LYS   B 1 46  ? -5.167 -19.491 29.785  1   59.369  ? 58  LYS   A HZ3  1 c 2 
ATOM   2506 N N    . GLY   B 1 47  ? 0.758  -14.371 25.151  1   45.627  ? 59  GLY   A N    1 ? 2 
ATOM   2507 C CA   . GLY   B 1 47  ? 1.635  -13.215 25.022  1   36.702  ? 59  GLY   A CA   1 ? 2 
ATOM   2508 C C    . GLY   B 1 47  ? 0.842  -12.004 24.568  1   40.104  ? 59  GLY   A C    1 ? 2 
ATOM   2509 O O    . GLY   B 1 47  ? -0.206 -12.121 23.931  1   39.683  ? 59  GLY   A O    1 ? 2 
ATOM   2510 H H    . GLY   B 1 47  ? 0.221  -14.595 24.446  1   43.567  ? 59  GLY   A H    1 c 2 
ATOM   2511 H HA2  . GLY   B 1 47  ? 2.062  -13.028 25.888  1   38.566  ? 59  GLY   A HA2  1 c 2 
ATOM   2512 H HA3  . GLY   B 1 47  ? 2.343  -13.415 24.366  1   38.359  ? 59  GLY   A HA3  1 c 2 
ATOM   2513 N N    . LYS   B 1 48  ? 1.399  -10.819 24.881  1   39.779  ? 60  LYS   A N    1 ? 2 
ATOM   2514 C CA   . LYS   B 1 48  ? 0.747  -9.621  24.426  1   43.766  ? 60  LYS   A CA   1 ? 2 
ATOM   2515 C C    . LYS   B 1 48  ? 1.729  -8.463  24.495  1   41.229  ? 60  LYS   A C    1 ? 2 
ATOM   2516 O O    . LYS   B 1 48  ? 2.776  -8.577  25.11   1   36.907  ? 60  LYS   A O    1 ? 2 
ATOM   2517 C CB   . LYS   B 1 48  ? -0.51  -9.353  25.231  1   45.581  ? 60  LYS   A CB   1 ? 2 
ATOM   2518 C CG   . LYS   B 1 48  ? -0.14  -9.084  26.699  1   50.389  ? 60  LYS   A CG   1 ? 2 
ATOM   2519 C CD   . LYS   B 1 48  ? -1.322 -8.78   27.616  1   55.183  ? 60  LYS   A CD   1 ? 2 
ATOM   2520 C CE   . LYS   B 1 48  ? -1.805 -7.407  27.471  1   61.69   ? 60  LYS   A CE   1 ? 2 
ATOM   2521 N NZ   . LYS   B 1 48  ? -2.518 -6.975  28.677  1   80.23   ? 60  LYS   A NZ   1 ? 2 
ATOM   2522 H H    . LYS   B 1 48  ? 2.169  -10.767 25.371  1   39.606  ? 60  LYS   A H    1 c 2 
ATOM   2523 H HA   . LYS   B 1 48  ? 0.491  -9.754  23.479  1   43.098  ? 60  LYS   A HA   1 c 2 
ATOM   2524 H HB2  . LYS   B 1 48  ? -0.977 -8.571  24.868  1   47.118  ? 60  LYS   A HB2  1 c 2 
ATOM   2525 H HB3  . LYS   B 1 48  ? -1.114 -10.124 25.185  1   47.368  ? 60  LYS   A HB3  1 c 2 
ATOM   2526 H HG2  . LYS   B 1 48  ? 0.333  -9.87   27.048  1   49.335  ? 60  LYS   A HG2  1 c 2 
ATOM   2527 H HG3  . LYS   B 1 48  ? 0.484  -8.328  26.73   1   49.165  ? 60  LYS   A HG3  1 c 2 
ATOM   2528 H HD2  . LYS   B 1 48  ? -2.055 -9.4    27.41   1   56.739  ? 60  LYS   A HD2  1 c 2 
ATOM   2529 H HD3  . LYS   B 1 48  ? -1.051 -8.929  28.548  1   56.024  ? 60  LYS   A HD3  1 c 2 
ATOM   2530 H HE2  . LYS   B 1 48  ? -1.057 -6.803  27.316  1   62.408  ? 60  LYS   A HE2  1 c 2 
ATOM   2531 H HE3  . LYS   B 1 48  ? -2.408 -7.35   26.708  1   64.21   ? 60  LYS   A HE3  1 c 2 
ATOM   2532 H HZ1  . LYS   B 1 48  ? -1.947 -6.946  29.38   1   73.827  ? 60  LYS   A HZ1  1 c 2 
ATOM   2533 H HZ2  . LYS   B 1 48  ? -3.189 -7.555  28.863  1   75.266  ? 60  LYS   A HZ2  1 c 2 
ATOM   2534 H HZ3  . LYS   B 1 48  ? -2.868 -6.149  28.547  1   75.103  ? 60  LYS   A HZ3  1 c 2 
ATOM   2535 N N    . LEU   B 1 49  ? 1.399  -7.439  23.671  1   41.823  ? 61  LEU   A N    1 ? 2 
ATOM   2536 C CA   . LEU   B 1 49  ? 2.035  -6.15   23.742  1   42.919  ? 61  LEU   A CA   1 ? 2 
ATOM   2537 C C    . LEU   B 1 49  ? 1.428  -5.514  24.999  1   40.081  ? 61  LEU   A C    1 ? 2 
ATOM   2538 O O    . LEU   B 1 49  ? 0.241  -5.731  25.282  1   45.523  ? 61  LEU   A O    1 ? 2 
ATOM   2539 C CB   . LEU   B 1 49  ? 1.685  -5.296  22.529  1   39.407  ? 61  LEU   A CB   1 ? 2 
ATOM   2540 C CG   . LEU   B 1 49  ? 2.108  -5.816  21.165  1   43.421  ? 61  LEU   A CG   1 ? 2 
ATOM   2541 C CD1  . LEU   B 1 49  ? 1.682  -4.872  20.066  1   41.087  ? 61  LEU   A CD1  1 ? 2 
ATOM   2542 C CD2  . LEU   B 1 49  ? 3.608  -6.167  21.03   1   41.119  ? 61  LEU   A CD2  1 ? 2 
ATOM   2543 H H    . LEU   B 1 49  ? 0.746  -7.568  23.044  1   42.862  ? 61  LEU   A H    1 c 2 
ATOM   2544 H HA   . LEU   B 1 49  ? 3.016  -6.255  23.833  1   40.16   ? 61  LEU   A HA   1 c 2 
ATOM   2545 H HB2  . LEU   B 1 49  ? 0.709  -5.168  22.519  1   42.451  ? 61  LEU   A HB2  1 c 2 
ATOM   2546 H HB3  . LEU   B 1 49  ? 2.088  -4.407  22.657  1   41.18   ? 61  LEU   A HB3  1 c 2 
ATOM   2547 H HG   . LEU   B 1 49  ? 1.612  -6.661  21.013  1   42.194  ? 61  LEU   A HG   1 c 2 
ATOM   2548 H HD11 . LEU   B 1 49  ? 0.715  -4.77   20.081  1   43.236  ? 61  LEU   A HD11 1 c 2 
ATOM   2549 H HD12 . LEU   B 1 49  ? 1.955  -5.231  19.205  1   42.006  ? 61  LEU   A HD12 1 c 2 
ATOM   2550 H HD13 . LEU   B 1 49  ? 2.1    -4.005  20.201  1   41.811  ? 61  LEU   A HD13 1 c 2 
ATOM   2551 H HD21 . LEU   B 1 49  ? 3.825  -6.9    21.629  1   40.965  ? 61  LEU   A HD21 1 c 2 
ATOM   2552 H HD22 . LEU   B 1 49  ? 4.146  -5.391  21.261  1   40.996  ? 61  LEU   A HD22 1 c 2 
ATOM   2553 H HD23 . LEU   B 1 49  ? 3.799  -6.431  20.114  1   41.416  ? 61  LEU   A HD23 1 c 2 
ATOM   2554 N N    . SER   B 1 50  ? 2.213  -4.75   25.74   1   47.354  ? 62  SER   A N    1 ? 2 
ATOM   2555 C CA   . SER   B 1 50  ? 1.625  -4.002  26.87   1   52.081  ? 62  SER   A CA   1 ? 2 
ATOM   2556 C C    . SER   B 1 50  ? 0.581  -3.001  26.402  1   50.55   ? 62  SER   A C    1 ? 2 
ATOM   2557 O O    . SER   B 1 50  ? -0.345 -2.688  27.163  1   54.911  ? 62  SER   A O    1 ? 2 
ATOM   2558 C CB   . SER   B 1 50  ? 2.704  -3.385  27.706  1   45.694  ? 62  SER   A CB   1 ? 2 
ATOM   2559 O OG   . SER   B 1 50  ? 3.523  -4.516  28.041  1   58.149  ? 62  SER   A OG   1 ? 2 
ATOM   2560 H H    . SER   B 1 50  ? 3.106  -4.679  25.561  1   45.034  ? 62  SER   A H    1 c 2 
ATOM   2561 H HA   . SER   B 1 50  ? 1.156  -4.663  27.442  1   50.083  ? 62  SER   A HA   1 c 2 
ATOM   2562 H HB2  . SER   B 1 50  ? 3.21   -2.729  27.19   1   49.516  ? 62  SER   A HB2  1 c 2 
ATOM   2563 H HB3  . SER   B 1 50  ? 2.329  -2.977  28.51   1   51.005  ? 62  SER   A HB3  1 c 2 
ATOM   2564 H HG   . SER   B 1 50  ? 4.209  -4.012  28.464  0   30      ? 62  SER   A HG   1 c 2 
ATOM   2565 N N    . ASN   B 1 51  ? 0.655  -2.494  25.143  1   53.349  ? 63  ASN   A N    1 ? 2 
ATOM   2566 C CA   . ASN   B 1 51  ? -0.363 -1.528  24.735  1   47.922  ? 63  ASN   A CA   1 ? 2 
ATOM   2567 C C    . ASN   B 1 51  ? -1.74  -2.187  24.452  1   61.553  ? 63  ASN   A C    1 ? 2 
ATOM   2568 O O    . ASN   B 1 51  ? -2.662 -1.456  24.077  1   51.042  ? 63  ASN   A O    1 ? 2 
ATOM   2569 C CB   . ASN   B 1 51  ? 0.102  -0.696  23.578  1   50      ? 63  ASN   A CB   1 ? 2 
ATOM   2570 C CG   . ASN   B 1 51  ? 0.106  -1.485  22.285  1   51.263  ? 63  ASN   A CG   1 ? 2 
ATOM   2571 O OD1  . ASN   B 1 51  ? -0.425 -2.608  22.206  1   45.917  ? 63  ASN   A OD1  1 ? 2 
ATOM   2572 N ND2  . ASN   B 1 51  ? 0.751  -0.927  21.27   1   52.113  ? 63  ASN   A ND2  1 ? 2 
ATOM   2573 H H    . ASN   B 1 51  ? 1.322  -2.732  24.566  1   49.692  ? 63  ASN   A H    1 c 2 
ATOM   2574 H HA   . ASN   B 1 51  ? -0.492 -0.906  25.487  1   52.566  ? 63  ASN   A HA   1 c 2 
ATOM   2575 H HB2  . ASN   B 1 51  ? -0.487 0.079   23.48   1   51.325  ? 63  ASN   A HB2  1 c 2 
ATOM   2576 H HB3  . ASN   B 1 51  ? 1.006  -0.369  23.758  1   49.017  ? 63  ASN   A HB3  1 c 2 
ATOM   2577 H HD21 . ASN   B 1 51  ? 0.852  -1.374  20.511  1   51.382  ? 63  ASN   A HD21 1 c 2 
ATOM   2578 H HD22 . ASN   B 1 51  ? 1.081  -0.107  21.35   1   51.9    ? 63  ASN   A HD22 1 c 2 
ATOM   2579 N N    . GLY   B 1 52  ? -1.903 -3.541  24.6    1   56.823  ? 64  GLY   A N    1 ? 2 
ATOM   2580 C CA   . GLY   B 1 52  ? -3.177 -4.237  24.406  1   59.842  ? 64  GLY   A CA   1 ? 2 
ATOM   2581 C C    . GLY   B 1 52  ? -3.678 -4.29   22.95   1   63.82   ? 64  GLY   A C    1 ? 2 
ATOM   2582 O O    . GLY   B 1 52  ? -4.836 -4.653  22.704  1   67.292  ? 64  GLY   A O    1 ? 2 
ATOM   2583 H H    . GLY   B 1 52  ? -1.174 -4.045  24.819  1   56.716  ? 64  GLY   A H    1 c 2 
ATOM   2584 H HA2  . GLY   B 1 52  ? -3.081 -5.159  24.742  1   59.662  ? 64  GLY   A HA2  1 c 2 
ATOM   2585 H HA3  . GLY   B 1 52  ? -3.86  -3.793  24.961  1   61.691  ? 64  GLY   A HA3  1 c 2 
ATOM   2586 N N    . LYS   B 1 53  ? -2.831 -3.935  21.956  1   56.93   ? 65  LYS   A N    1 ? 2 
ATOM   2587 C CA   . LYS   B 1 53  ? -3.283 -3.886  20.565  1   53.348  ? 65  LYS   A CA   1 ? 2 
ATOM   2588 C C    . LYS   B 1 53  ? -2.981 -5.282  19.981  1   54.219  ? 65  LYS   A C    1 ? 2 
ATOM   2589 O O    . LYS   B 1 53  ? -3.434 -5.599  18.883  1   55.409  ? 65  LYS   A O    1 ? 2 
ATOM   2590 C CB   . LYS   B 1 53  ? -2.842 -2.63   19.737  1   46.572  ? 65  LYS   A CB   1 ? 2 
ATOM   2591 H H    . LYS   B 1 53  ? -1.962 -3.727  22.147  1   55.589  ? 65  LYS   A H    1 c 2 
ATOM   2592 H HA   . LYS   B 1 53  ? -4.27  -3.809  20.589  1   54.969  ? 65  LYS   A HA   1 c 2 
ATOM   2593 H HB2  . LYS   B 1 53  ? -1.792 -2.72   19.799  0   30      ? 65  LYS   A HB2  1 c 2 
ATOM   2594 H HB3  . LYS   B 1 53  ? -3.542 -2.193  19.461  0   30      ? 65  LYS   A HB3  1 c 2 
ATOM   2595 N N    . LYS   B 1 54  ? -2.283 -6.169  20.713  1   48.418  ? 66  LYS   A N    1 ? 2 
ATOM   2596 C CA   . LYS   B 1 54  ? -1.965 -7.478  20.136  1   48.826  ? 66  LYS   A CA   1 ? 2 
ATOM   2597 C C    . LYS   B 1 54  ? -1.81  -8.546  21.224  1   47.864  ? 66  LYS   A C    1 ? 2 
ATOM   2598 O O    . LYS   B 1 54  ? -1.124 -8.353  22.226  1   43.288  ? 66  LYS   A O    1 ? 2 
ATOM   2599 C CB   . LYS   B 1 54  ? -0.845 -7.465  19.075  1   44.735  ? 66  LYS   A CB   1 ? 2 
ATOM   2600 H H    . LYS   B 1 54  ? -1.996 -5.967  21.556  1   49.013  ? 66  LYS   A H    1 c 2 
ATOM   2601 H HA   . LYS   B 1 54  ? -2.764 -7.745  19.615  1   49.643  ? 66  LYS   A HA   1 c 2 
ATOM   2602 H HB2  . LYS   B 1 54  ? 0.007  -7.496  19.548  0   30      ? 66  LYS   A HB2  1 c 2 
ATOM   2603 H HB3  . LYS   B 1 54  ? -1.197 -7.491  18.133  0   30      ? 66  LYS   A HB3  1 c 2 
ATOM   2604 N N    . PHE   B 1 55  ? -2.471 -9.688  20.964  1   48.722  ? 67  PHE   A N    1 ? 2 
ATOM   2605 C CA   . PHE   B 1 55  ? -2.393 -10.916 21.759  1   54.885  ? 67  PHE   A CA   1 ? 2 
ATOM   2606 C C    . PHE   B 1 55  ? -2.076 -12.112 20.847  1   53.579  ? 67  PHE   A C    1 ? 2 
ATOM   2607 O O    . PHE   B 1 55  ? -2.432 -12.118 19.647  1   52.339  ? 67  PHE   A O    1 ? 2 
ATOM   2608 C CB   . PHE   B 1 55  ? -3.755 -11.272 22.342  1   54.264  ? 67  PHE   A CB   1 ? 2 
ATOM   2609 C CG   . PHE   B 1 55  ? -4.343 -10.085 23.091  1   64.285  ? 67  PHE   A CG   1 ? 2 
ATOM   2610 C CD1  . PHE   B 1 55  ? -4.957 -9.031  22.389  1   60.178  ? 67  PHE   A CD1  1 ? 2 
ATOM   2611 C CD2  . PHE   B 1 55  ? -4.285 -10.028 24.501  1   66.233  ? 67  PHE   A CD2  1 ? 2 
ATOM   2612 C CE1  . PHE   B 1 55  ? -5.55  -7.976  23.086  1   63.311  ? 67  PHE   A CE1  1 ? 2 
ATOM   2613 C CE2  . PHE   B 1 55  ? -4.824 -8.933  25.178  1   69.192  ? 67  PHE   A CE2  1 ? 2 
ATOM   2614 C CZ   . PHE   B 1 55  ? -5.43  -7.889  24.461  1   64.781  ? 67  PHE   A CZ   1 ? 2 
ATOM   2615 H H    . PHE   B 1 55  ? -3.013 -9.701  20.228  1   51.359  ? 67  PHE   A H    1 c 2 
ATOM   2616 H HA   . PHE   B 1 55  ? -1.715 -10.829 22.477  1   51.328  ? 67  PHE   A HA   1 c 2 
ATOM   2617 H HB2  . PHE   B 1 55  ? -4.361 -11.53  21.612  1   58.262  ? 67  PHE   A HB2  1 c 2 
ATOM   2618 H HB3  . PHE   B 1 55  ? -3.653 -12.03  22.958  1   56.816  ? 67  PHE   A HB3  1 c 2 
ATOM   2619 H HD1  . PHE   B 1 55  ? -5.032 -9.075  21.449  1   62.254  ? 67  PHE   A HD1  1 c 2 
ATOM   2620 H HD2  . PHE   B 1 55  ? -3.855 -10.717 24.983  1   65.323  ? 67  PHE   A HD2  1 c 2 
ATOM   2621 H HE1  . PHE   B 1 55  ? -5.942 -7.263  22.606  1   64.276  ? 67  PHE   A HE1  1 c 2 
ATOM   2622 H HE2  . PHE   B 1 55  ? -4.775 -8.892  26.119  1   67.27   ? 67  PHE   A HE2  1 c 2 
ATOM   2623 H HZ   . PHE   B 1 55  ? -5.819 -7.164  24.924  1   66.448  ? 67  PHE   A HZ   1 c 2 
ATOM   2624 N N    . ASP   B 1 56  ? -1.428 -13.106 21.429  1   44.012  ? 68  ASP   A N    1 ? 2 
ATOM   2625 C CA   . ASP   B 1 56  ? -0.949 -14.261 20.683  1   44.519  ? 68  ASP   A CA   1 ? 2 
ATOM   2626 C C    . ASP   B 1 56  ? -0.856 -15.401 21.677  1   42.486  ? 68  ASP   A C    1 ? 2 
ATOM   2627 O O    . ASP   B 1 56  ? -0.251 -15.229 22.731  1   41.032  ? 68  ASP   A O    1 ? 2 
ATOM   2628 C CB   . ASP   B 1 56  ? 0.471  -14.04  20.142  1   46.158  ? 68  ASP   A CB   1 ? 2 
ATOM   2629 C CG   . ASP   B 1 56  ? 1.135  -15.272 19.537  1   51.816  ? 68  ASP   A CG   1 ? 2 
ATOM   2630 O OD1  . ASP   B 1 56  ? 0.441  -15.947 18.786  1   47.235  ? 68  ASP   A OD1  1 ? 2 
ATOM   2631 O OD2  . ASP   B 1 56  ? 2.355  -15.51  19.759  1   49.19   ? 68  ASP   A OD2  1 ? 2 
ATOM   2632 H H    . ASP   B 1 56  ? -1.273 -13.069 22.329  1   45.407  ? 68  ASP   A H    1 c 2 
ATOM   2633 H HA   . ASP   B 1 56  ? -1.586 -14.484 19.967  1   46.13   ? 68  ASP   A HA   1 c 2 
ATOM   2634 H HB2  . ASP   B 1 56  ? 0.425  -13.349 19.449  1   46.431  ? 68  ASP   A HB2  1 c 2 
ATOM   2635 H HB3  . ASP   B 1 56  ? 1.04   -13.707 20.868  1   45.143  ? 68  ASP   A HB3  1 c 2 
ATOM   2636 N N    . SER   B 1 57  ? -1.448 -16.549 21.369  1   44.713  ? 69  SER   A N    1 ? 2 
ATOM   2637 C CA   . SER   B 1 57  ? -1.423 -17.645 22.309  1   48.603  ? 69  SER   A CA   1 ? 2 
ATOM   2638 C C    . SER   B 1 57  ? -1.238 -18.932 21.516  1   53.441  ? 69  SER   A C    1 ? 2 
ATOM   2639 O O    . SER   B 1 57  ? -1.973 -19.102 20.55   1   49.454  ? 69  SER   A O    1 ? 2 
ATOM   2640 C CB   . SER   B 1 57  ? -2.683 -17.72  23.114  1   48.162  ? 69  SER   A CB   1 ? 2 
ATOM   2641 O OG   . SER   B 1 57  ? -2.722 -18.927 23.866  1   47.338  ? 69  SER   A OG   1 ? 2 
ATOM   2642 H H    . SER   B 1 57  ? -1.873 -16.652 20.567  1   46.552  ? 69  SER   A H    1 c 2 
ATOM   2643 H HA   . SER   B 1 57  ? -0.653 -17.53  22.919  1   46.668  ? 69  SER   A HA   1 c 2 
ATOM   2644 H HB2  . SER   B 1 57  ? -2.727 -16.956 23.721  1   47.364  ? 69  SER   A HB2  1 c 2 
ATOM   2645 H HB3  . SER   B 1 57  ? -3.453 -17.682 22.516  1   49.568  ? 69  SER   A HB3  1 c 2 
ATOM   2646 H HG   . SER   B 1 57  ? -3.455 -18.942 24.31   0   30      ? 69  SER   A HG   1 c 2 
ATOM   2647 N N    . SER   B 1 58  ? -0.345 -19.812 22.007  1   48.021  ? 70  SER   A N    1 ? 2 
ATOM   2648 C CA   . SER   B 1 58  ? -0.218 -21.187 21.514  1   57.286  ? 70  SER   A CA   1 ? 2 
ATOM   2649 C C    . SER   B 1 58  ? -1.552 -21.929 21.461  1   57.052  ? 70  SER   A C    1 ? 2 
ATOM   2650 O O    . SER   B 1 58  ? -1.715 -22.845 20.622  1   61.175  ? 70  SER   A O    1 ? 2 
ATOM   2651 C CB   . SER   B 1 58  ? 0.781  -22.016 22.304  1   58.32   ? 70  SER   A CB   1 ? 2 
ATOM   2652 O OG   . SER   B 1 58  ? 0.457  -22.033 23.685  1   57.216  ? 70  SER   A OG   1 ? 2 
ATOM   2653 H H    . SER   B 1 58  ? 0.211  -19.541 22.679  1   49.426  ? 70  SER   A H    1 c 2 
ATOM   2654 H HA   . SER   B 1 58  ? 0.119  -21.13  20.584  1   55.465  ? 70  SER   A HA   1 c 2 
ATOM   2655 H HB2  . SER   B 1 58  ? 0.786  -22.929 21.961  1   59.264  ? 70  SER   A HB2  1 c 2 
ATOM   2656 H HB3  . SER   B 1 58  ? 1.674  -21.642 22.186  1   56.38   ? 70  SER   A HB3  1 c 2 
ATOM   2657 H HG   . SER   B 1 58  ? 1.061  -22.504 24.064  0   30      ? 70  SER   A HG   1 c 2 
ATOM   2658 N N    . HIS   B 1 59  ? -2.492 -21.582 22.348  1   55.855  ? 71  HIS   A N    1 ? 2 
ATOM   2659 C CA   . HIS   B 1 59  ? -3.764 -22.306 22.329  1   60.555  ? 71  HIS   A CA   1 ? 2 
ATOM   2660 C C    . HIS   B 1 59  ? -4.616 -21.963 21.095  1   64.42   ? 71  HIS   A C    1 ? 2 
ATOM   2661 O O    . HIS   B 1 59  ? -5.454 -22.76  20.694  1   68.6    ? 71  HIS   A O    1 ? 2 
ATOM   2662 C CB   . HIS   B 1 59  ? -4.549 -22.103 23.621  1   61.658  ? 71  HIS   A CB   1 ? 2 
ATOM   2663 C CG   . HIS   B 1 59  ? -3.788 -22.491 24.841  1   60.801  ? 71  HIS   A CG   1 ? 2 
ATOM   2664 N ND1  . HIS   B 1 59  ? -3.764 -23.782 25.328  1   68.263  ? 71  HIS   A ND1  1 ? 2 
ATOM   2665 C CD2  . HIS   B 1 59  ? -3.061 -21.75  25.672  1   59.037  ? 71  HIS   A CD2  1 ? 2 
ATOM   2666 C CE1  . HIS   B 1 59  ? -3.013 -23.795 26.421  1   68.22   ? 71  HIS   A CE1  1 ? 2 
ATOM   2667 N NE2  . HIS   B 1 59  ? -2.562 -22.562 26.627  1   62.072  ? 71  HIS   A NE2  1 ? 2 
ATOM   2668 H H    . HIS   B 1 59  ? -2.349 -20.924 22.965  1   55.256  ? 71  HIS   A H    1 c 2 
ATOM   2669 H HA   . HIS   B 1 59  ? -3.543 -23.269 22.28   1   61.798  ? 71  HIS   A HA   1 c 2 
ATOM   2670 H HB2  . HIS   B 1 59  ? -4.803 -21.156 23.691  1   60.747  ? 71  HIS   A HB2  1 c 2 
ATOM   2671 H HB3  . HIS   B 1 59  ? -5.374 -22.634 23.576  1   63.782  ? 71  HIS   A HB3  1 c 2 
ATOM   2672 H HD1  . HIS   B 1 59  ? -4.06  -24.421 24.943  0   30      ? 71  HIS   A HD1  1 c 2 
ATOM   2673 H HD2  . HIS   B 1 59  ? -2.887 -20.833 25.595  1   58.119  ? 71  HIS   A HD2  1 c 2 
ATOM   2674 H HE1  . HIS   B 1 59  ? -2.819 -24.551 26.947  1   67.779  ? 71  HIS   A HE1  1 c 2 
ATOM   2675 H HE2  . HIS   B 1 59  ? -2.068 -22.274 27.373  0   30      ? 71  HIS   A HE2  1 c 2 
ATOM   2676 N N    . ASP   B 1 60  ? -4.437 -20.772 20.512  1   60.863  ? 72  ASP   A N    1 ? 2 
ATOM   2677 C CA   . ASP   B 1 60  ? -4.961 -20.487 19.18   1   69.834  ? 72  ASP   A CA   1 ? 2 
ATOM   2678 C C    . ASP   B 1 60  ? -4.597 -21.661 18.272  1   77.319  ? 72  ASP   A C    1 ? 2 
ATOM   2679 O O    . ASP   B 1 60  ? -5.484 -22.346 17.803  1   92.451  ? 72  ASP   A O    1 ? 2 
ATOM   2680 C CB   . ASP   B 1 60  ? -4.439 -19.168 18.6    1   66.383  ? 72  ASP   A CB   1 ? 2 
ATOM   2681 C CG   . ASP   B 1 60  ? -4.699 -17.93  19.458  1   68.169  ? 72  ASP   A CG   1 ? 2 
ATOM   2682 O OD1  . ASP   B 1 60  ? -5.674 -17.978 20.222  1   71.574  ? 72  ASP   A OD1  1 ? 2 
ATOM   2683 O OD2  . ASP   B 1 60  ? -3.932 -16.917 19.376  1   60.847  ? 72  ASP   A OD2  1 ? 2 
ATOM   2684 H H    . ASP   B 1 60  ? -3.98  -20.118 20.957  1   60.954  ? 72  ASP   A H    1 c 2 
ATOM   2685 H HA   . ASP   B 1 60  ? -5.941 -20.43  19.24   1   70.805  ? 72  ASP   A HA   1 c 2 
ATOM   2686 H HB2  . ASP   B 1 60  ? -3.474 -19.242 18.453  1   66.004  ? 72  ASP   A HB2  1 c 2 
ATOM   2687 H HB3  . ASP   B 1 60  ? -4.863 -19.024 17.728  1   68.935  ? 72  ASP   A HB3  1 c 2 
ATOM   2688 N N    . ARG   B 1 61  ? -3.301 -21.942 18.08   1   79.174  ? 73  ARG   A N    1 ? 2 
ATOM   2689 C CA   . ARG   B 1 61  ? -2.864 -23.052 17.246  1   81.61   ? 73  ARG   A CA   1 ? 2 
ATOM   2690 C C    . ARG   B 1 61  ? -3.313 -24.423 17.796  1   78.346  ? 73  ARG   A C    1 ? 2 
ATOM   2691 O O    . ARG   B 1 61  ? -3.039 -25.437 17.174  1   83.532  ? 73  ARG   A O    1 ? 2 
ATOM   2692 C CB   . ARG   B 1 61  ? -1.353 -22.865 17.04   1   83.434  ? 73  ARG   A CB   1 ? 2 
ATOM   2693 H H    . ARG   B 1 61  ? -2.669 -21.424 18.492  1   76.09   ? 73  ARG   A H    1 c 2 
ATOM   2694 H HA   . ARG   B 1 61  ? -3.288 -22.939 16.357  1   82.766  ? 73  ARG   A HA   1 c 2 
ATOM   2695 H HB2  . ARG   B 1 61  ? -0.925 -23.503 17.811  0   30      ? 73  ARG   A HB2  1 c 2 
ATOM   2696 H HB3  . ARG   B 1 61  ? -1.189 -22.45  16.302  0   30      ? 73  ARG   A HB3  1 c 2 
ATOM   2697 N N    . ASN   B 1 62  ? -4.038 -24.479 18.93   1   77.693  ? 74  ASN   A N    1 ? 2 
ATOM   2698 C CA   . ASN   B 1 62  ? -4.447 -25.725 19.598  1   78.113  ? 74  ASN   A CA   1 ? 2 
ATOM   2699 C C    . ASN   B 1 62  ? -3.323 -26.785 19.603  1   77.022  ? 74  ASN   A C    1 ? 2 
ATOM   2700 O O    . ASN   B 1 62  ? -3.609 -27.966 19.45   1   74.429  ? 74  ASN   A O    1 ? 2 
ATOM   2701 C CB   . ASN   B 1 62  ? -5.78  -26.303 19.071  1   74.744  ? 74  ASN   A CB   1 ? 2 
ATOM   2702 H H    . ASN   B 1 62  ? -4.29  -23.694 19.319  1   76.222  ? 74  ASN   A H    1 c 2 
ATOM   2703 H HA   . ASN   B 1 62  ? -4.608 -25.493 20.54   1   75.731  ? 74  ASN   A HA   1 c 2 
ATOM   2704 H HB2  . ASN   B 1 62  ? -5.498 -26.952 18.531  0   30      ? 74  ASN   A HB2  1 c 2 
ATOM   2705 H HB3  . ASN   B 1 62  ? -6.406 -25.794 19.648  0   30      ? 74  ASN   A HB3  1 c 2 
ATOM   2706 N N    . GLU   B 1 63  ? -2.055 -26.407 19.859  1   72.884  ? 75  GLU   A N    1 ? 2 
ATOM   2707 C CA   . GLU   B 1 63  ? -0.965 -27.357 20.102  1   73.53   ? 75  GLU   A CA   1 ? 2 
ATOM   2708 C C    . GLU   B 1 63  ? 0.167  -26.603 20.811  1   68.339  ? 75  GLU   A C    1 ? 2 
ATOM   2709 O O    . GLU   B 1 63  ? 0.275  -25.404 20.593  1   56.589  ? 75  GLU   A O    1 ? 2 
ATOM   2710 C CB   . GLU   B 1 63  ? -0.451 -28.041 18.825  1   70.991  ? 75  GLU   A CB   1 ? 2 
ATOM   2711 H H    . GLU   B 1 63  ? -1.864 -25.513 19.891  1   71.364  ? 75  GLU   A H    1 c 2 
ATOM   2712 H HA   . GLU   B 1 63  ? -1.306 -28.058 20.711  1   73.579  ? 75  GLU   A HA   1 c 2 
ATOM   2713 H HB2  . GLU   B 1 63  ? 0.621  -27.849 18.853  0   30      ? 75  GLU   A HB2  1 c 2 
ATOM   2714 H HB3  . GLU   B 1 63  ? -1.127 -28.093 18.275  0   30      ? 75  GLU   A HB3  1 c 2 
ATOM   2715 N N    . PRO   B 1 64  ? 0.996  -27.283 21.66   1   66.847  ? 76  PRO   A N    1 ? 2 
ATOM   2716 C CA   . PRO   B 1 64  ? 2.152  -26.68  22.3    1   61.516  ? 76  PRO   A CA   1 ? 2 
ATOM   2717 C C    . PRO   B 1 64  ? 3.108  -26.045 21.305  1   59.255  ? 76  PRO   A C    1 ? 2 
ATOM   2718 O O    . PRO   B 1 64  ? 3.129  -26.469 20.161  1   57.557  ? 76  PRO   A O    1 ? 2 
ATOM   2719 C CB   . PRO   B 1 64  ? 2.904  -27.833 22.935  1   61.509  ? 76  PRO   A CB   1 ? 2 
ATOM   2720 C CG   . PRO   B 1 64  ? 1.889  -28.933 23.091  1   69.667  ? 76  PRO   A CG   1 ? 2 
ATOM   2721 C CD   . PRO   B 1 64  ? 0.893  -28.718 21.969  1   72.748  ? 76  PRO   A CD   1 ? 2 
ATOM   2722 H HA   . PRO   B 1 64  ? 1.869  -26.027 22.973  1   60.266  ? 76  PRO   A HA   1 c 2 
ATOM   2723 H HB2  . PRO   B 1 64  ? 3.642  -28.125 22.365  1   63.303  ? 76  PRO   A HB2  1 c 2 
ATOM   2724 H HB3  . PRO   B 1 64  ? 3.268  -27.572 23.803  1   61.791  ? 76  PRO   A HB3  1 c 2 
ATOM   2725 H HG2  . PRO   B 1 64  ? 2.312  -29.812 23.011  1   70.429  ? 76  PRO   A HG2  1 c 2 
ATOM   2726 H HG3  . PRO   B 1 64  ? 1.444  -28.875 23.961  1   68.683  ? 76  PRO   A HG3  1 c 2 
ATOM   2727 H HD2  . PRO   B 1 64  ? 1.122  -29.255 21.186  1   73.058  ? 76  PRO   A HD2  1 c 2 
ATOM   2728 H HD3  . PRO   B 1 64  ? -0.012 -28.944 22.258  1   72.823  ? 76  PRO   A HD3  1 c 2 
ATOM   2729 N N    . PHE   B 1 65  ? 3.83   -25.029 21.752  1   55.786  ? 77  PHE   A N    1 ? 2 
ATOM   2730 C CA   . PHE   B 1 65  ? 4.947  -24.407 21.064  1   56.614  ? 77  PHE   A CA   1 ? 2 
ATOM   2731 C C    . PHE   B 1 65  ? 6.265  -25.068 21.452  1   61.186  ? 77  PHE   A C    1 ? 2 
ATOM   2732 O O    . PHE   B 1 65  ? 6.558  -25.236 22.62   1   61.557  ? 77  PHE   A O    1 ? 2 
ATOM   2733 C CB   . PHE   B 1 65  ? 4.933  -22.939 21.417  1   50.979  ? 77  PHE   A CB   1 ? 2 
ATOM   2734 C CG   . PHE   B 1 65  ? 6.031  -22.103 20.758  1   54.088  ? 77  PHE   A CG   1 ? 2 
ATOM   2735 C CD1  . PHE   B 1 65  ? 5.917  -21.676 19.436  1   60.518  ? 77  PHE   A CD1  1 ? 2 
ATOM   2736 C CD2  . PHE   B 1 65  ? 7.183  -21.753 21.45   1   50.895  ? 77  PHE   A CD2  1 ? 2 
ATOM   2737 C CE1  . PHE   B 1 65  ? 6.925  -20.905 18.851  1   67.069  ? 77  PHE   A CE1  1 ? 2 
ATOM   2738 C CE2  . PHE   B 1 65  ? 8.202  -21.016 20.849  1   57.37   ? 77  PHE   A CE2  1 ? 2 
ATOM   2739 C CZ   . PHE   B 1 65  ? 8.072  -20.585 19.558  1   54.926  ? 77  PHE   A CZ   1 ? 2 
ATOM   2740 H H    . PHE   B 1 65  ? 3.604  -24.689 22.569  1   55.609  ? 77  PHE   A H    1 c 2 
ATOM   2741 H HA   . PHE   B 1 65  ? 4.812  -24.502 20.084  1   57.299  ? 77  PHE   A HA   1 c 2 
ATOM   2742 H HB2  . PHE   B 1 65  ? 4.06   -22.568 21.161  1   52.745  ? 77  PHE   A HB2  1 c 2 
ATOM   2743 H HB3  . PHE   B 1 65  ? 5.017  -22.854 22.392  1   51.98   ? 77  PHE   A HB3  1 c 2 
ATOM   2744 H HD1  . PHE   B 1 65  ? 5.14   -21.887 18.943  1   61.549  ? 77  PHE   A HD1  1 c 2 
ATOM   2745 H HD2  . PHE   B 1 65  ? 7.29   -22.047 22.341  1   53.046  ? 77  PHE   A HD2  1 c 2 
ATOM   2746 H HE1  . PHE   B 1 65  ? 6.835  -20.623 17.955  1   62.645  ? 77  PHE   A HE1  1 c 2 
ATOM   2747 H HE2  . PHE   B 1 65  ? 8.971  -20.788 21.346  1   54.261  ? 77  PHE   A HE2  1 c 2 
ATOM   2748 H HZ   . PHE   B 1 65  ? 8.754  -20.071 19.154  1   57.175  ? 77  PHE   A HZ   1 c 2 
ATOM   2749 N N    . VAL   B 1 66  ? 7.077  -25.385 20.428  1   68.142  ? 78  VAL   A N    1 ? 2 
ATOM   2750 C CA   . VAL   B 1 66  ? 8.327  -26.112 20.594  1   65.87   ? 78  VAL   A CA   1 ? 2 
ATOM   2751 C C    . VAL   B 1 66  ? 9.438  -25.213 20.073  1   57.517  ? 78  VAL   A C    1 ? 2 
ATOM   2752 O O    . VAL   B 1 66  ? 9.248  -24.558 19.073  1   68.494  ? 78  VAL   A O    1 ? 2 
ATOM   2753 C CB   . VAL   B 1 66  ? 8.344  -27.454 19.831  1   67.322  ? 78  VAL   A CB   1 ? 2 
ATOM   2754 C CG1  . VAL   B 1 66  ? 9.426  -28.387 20.377  1   64.192  ? 78  VAL   A CG1  1 ? 2 
ATOM   2755 C CG2  . VAL   B 1 66  ? 6.987  -28.155 19.859  1   77.173  ? 78  VAL   A CG2  1 ? 2 
ATOM   2756 H H    . VAL   B 1 66  ? 6.837  -25.129 19.584  1   65.922  ? 78  VAL   A H    1 c 2 
ATOM   2757 H HA   . VAL   B 1 66  ? 8.471  -26.283 21.542  1   64.277  ? 78  VAL   A HA   1 c 2 
ATOM   2758 H HB   . VAL   B 1 66  ? 8.561  -27.254 18.89   1   68.397  ? 78  VAL   A HB   1 c 2 
ATOM   2759 H HG11 . VAL   B 1 66  ? 9.282  -28.531 21.327  1   65.175  ? 78  VAL   A HG11 1 c 2 
ATOM   2760 H HG12 . VAL   B 1 66  ? 10.301 -27.985 20.24   1   64.805  ? 78  VAL   A HG12 1 c 2 
ATOM   2761 H HG13 . VAL   B 1 66  ? 9.386  -29.239 19.911  1   67.823  ? 78  VAL   A HG13 1 c 2 
ATOM   2762 H HG21 . VAL   B 1 66  ? 7.065  -29.031 19.446  1   76.811  ? 78  VAL   A HG21 1 c 2 
ATOM   2763 H HG22 . VAL   B 1 66  ? 6.336  -27.625 19.369  1   74.079  ? 78  VAL   A HG22 1 c 2 
ATOM   2764 H HG23 . VAL   B 1 66  ? 6.693  -28.258 20.78   1   74.179  ? 78  VAL   A HG23 1 c 2 
ATOM   2765 N N    . PHE   B 1 67  ? 10.594 -25.214 20.734  1   54.501  ? 79  PHE   A N    1 ? 2 
ATOM   2766 C CA   . PHE   B 1 67  ? 11.795 -24.561 20.239  1   52.258  ? 79  PHE   A CA   1 ? 2 
ATOM   2767 C C    . PHE   B 1 67  ? 13.009 -25.136 20.949  1   56.666  ? 79  PHE   A C    1 ? 2 
ATOM   2768 O O    . PHE   B 1 67  ? 12.86  -25.784 21.99   1   61.676  ? 79  PHE   A O    1 ? 2 
ATOM   2769 C CB   . PHE   B 1 67  ? 11.766 -23.049 20.468  1   46.637  ? 79  PHE   A CB   1 ? 2 
ATOM   2770 C CG   . PHE   B 1 67  ? 11.896 -22.568 21.915  1   48.56   ? 79  PHE   A CG   1 ? 2 
ATOM   2771 C CD1  . PHE   B 1 67  ? 10.892 -22.777 22.866  1   43.426  ? 79  PHE   A CD1  1 ? 2 
ATOM   2772 C CD2  . PHE   B 1 67  ? 13.049 -21.921 22.326  1   49.675  ? 79  PHE   A CD2  1 ? 2 
ATOM   2773 C CE1  . PHE   B 1 67  ? 11.059 -22.359 24.18   1   46.082  ? 79  PHE   A CE1  1 ? 2 
ATOM   2774 C CE2  . PHE   B 1 67  ? 13.162 -21.42  23.626  1   49.532  ? 79  PHE   A CE2  1 ? 2 
ATOM   2775 C CZ   . PHE   B 1 67  ? 12.168 -21.622 24.553  1   44.458  ? 79  PHE   A CZ   1 ? 2 
ATOM   2776 H H    . PHE   B 1 67  ? 10.636 -25.643 21.54   1   55.223  ? 79  PHE   A H    1 c 2 
ATOM   2777 H HA   . PHE   B 1 67  ? 11.878 -24.738 19.264  1   53.695  ? 79  PHE   A HA   1 c 2 
ATOM   2778 H HB2  . PHE   B 1 67  ? 12.492 -22.648 19.941  1   48.027  ? 79  PHE   A HB2  1 c 2 
ATOM   2779 H HB3  . PHE   B 1 67  ? 10.922 -22.702 20.102  1   47.563  ? 79  PHE   A HB3  1 c 2 
ATOM   2780 H HD1  . PHE   B 1 67  ? 10.113 -23.251 22.623  1   46.047  ? 79  PHE   A HD1  1 c 2 
ATOM   2781 H HD2  . PHE   B 1 67  ? 13.723 -21.729 21.693  1   49.538  ? 79  PHE   A HD2  1 c 2 
ATOM   2782 H HE1  . PHE   B 1 67  ? 10.357 -22.486 24.799  1   45.07   ? 79  PHE   A HE1  1 c 2 
ATOM   2783 H HE2  . PHE   B 1 67  ? 13.951 -20.968 23.881  1   47.794  ? 79  PHE   A HE2  1 c 2 
ATOM   2784 H HZ   . PHE   B 1 67  ? 12.279 -21.339 25.446  1   45.361  ? 79  PHE   A HZ   1 c 2 
ATOM   2785 N N    . SER   B 1 68  ? 14.193 -24.826 20.408  1   57.55   ? 80  SER   A N    1 ? 2 
ATOM   2786 C CA   . SER   B 1 68  ? 15.443 -25.316 20.961  1   62.15   ? 80  SER   A CA   1 ? 2 
ATOM   2787 C C    . SER   B 1 68  ? 16.074 -24.161 21.729  1   64.17   ? 80  SER   A C    1 ? 2 
ATOM   2788 O O    . SER   B 1 68  ? 16.247 -23.096 21.196  1   56.548  ? 80  SER   A O    1 ? 2 
ATOM   2789 C CB   . SER   B 1 68  ? 16.307 -25.857 19.852  1   70.39   ? 80  SER   A CB   1 ? 2 
ATOM   2790 O OG   . SER   B 1 68  ? 17.656 -26.064 20.253  1   77.231  ? 80  SER   A OG   1 ? 2 
ATOM   2791 H H    . SER   B 1 68  ? 14.22  -24.288 19.67   1   57.556  ? 80  SER   A H    1 c 2 
ATOM   2792 H HA   . SER   B 1 68  ? 15.244 -26.05  21.594  1   64.114  ? 80  SER   A HA   1 c 2 
ATOM   2793 H HB2  . SER   B 1 68  ? 15.933 -26.703 19.541  1   71.764  ? 80  SER   A HB2  1 c 2 
ATOM   2794 H HB3  . SER   B 1 68  ? 16.291 -25.232 19.103  1   69.347  ? 80  SER   A HB3  1 c 2 
ATOM   2795 H HG   . SER   B 1 68  ? 18.122 -26.318 19.598  0   30      ? 80  SER   A HG   1 c 2 
ATOM   2796 N N    . LEU   B 1 69  ? 16.339 -24.379 23.012  1   62.837  ? 81  LEU   A N    1 ? 2 
ATOM   2797 C CA   . LEU   B 1 69  ? 16.68  -23.318 23.934  1   54.473  ? 81  LEU   A CA   1 ? 2 
ATOM   2798 C C    . LEU   B 1 69  ? 18.077 -22.83  23.645  1   55.224  ? 81  LEU   A C    1 ? 2 
ATOM   2799 O O    . LEU   B 1 69  ? 19.007 -23.61  23.551  1   60.103  ? 81  LEU   A O    1 ? 2 
ATOM   2800 C CB   . LEU   B 1 69  ? 16.621 -23.78  25.38   1   51.477  ? 81  LEU   A CB   1 ? 2 
ATOM   2801 C CG   . LEU   B 1 69  ? 17.068 -22.786 26.456  1   45.717  ? 81  LEU   A CG   1 ? 2 
ATOM   2802 C CD1  . LEU   B 1 69  ? 15.938 -21.822 26.721  1   44.564  ? 81  LEU   A CD1  1 ? 2 
ATOM   2803 C CD2  . LEU   B 1 69  ? 17.509 -23.436 27.752  1   48.825  ? 81  LEU   A CD2  1 ? 2 
ATOM   2804 H H    . LEU   B 1 69  ? 16.31  -25.236 23.329  1   62.838  ? 81  LEU   A H    1 c 2 
ATOM   2805 H HA   . LEU   B 1 69  ? 16.039 -22.573 23.803  1   53.22   ? 81  LEU   A HA   1 c 2 
ATOM   2806 H HB2  . LEU   B 1 69  ? 15.694 -24.051 25.575  1   50.646  ? 81  LEU   A HB2  1 c 2 
ATOM   2807 H HB3  . LEU   B 1 69  ? 17.176 -24.59  25.462  1   53.041  ? 81  LEU   A HB3  1 c 2 
ATOM   2808 H HG   . LEU   B 1 69  ? 17.834 -22.267 26.103  1   47.017  ? 81  LEU   A HG   1 c 2 
ATOM   2809 H HD11 . LEU   B 1 69  ? 15.707 -21.358 25.899  1   43.138  ? 81  LEU   A HD11 1 c 2 
ATOM   2810 H HD12 . LEU   B 1 69  ? 16.214 -21.174 27.39   1   43.754  ? 81  LEU   A HD12 1 c 2 
ATOM   2811 H HD13 . LEU   B 1 69  ? 15.163 -22.31  27.046  1   44.343  ? 81  LEU   A HD13 1 c 2 
ATOM   2812 H HD21 . LEU   B 1 69  ? 18.361 -23.88  27.617  1   50.331  ? 81  LEU   A HD21 1 c 2 
ATOM   2813 H HD22 . LEU   B 1 69  ? 16.845 -24.087 28.031  1   49.054  ? 81  LEU   A HD22 1 c 2 
ATOM   2814 H HD23 . LEU   B 1 69  ? 17.605 -22.757 28.44   1   47.866  ? 81  LEU   A HD23 1 c 2 
ATOM   2815 N N    . GLY   B 1 70  ? 18.158 -21.511 23.542  1   54.364  ? 82  GLY   A N    1 ? 2 
ATOM   2816 C CA   . GLY   B 1 70  ? 19.423 -20.826 23.406  1   59.541  ? 82  GLY   A CA   1 ? 2 
ATOM   2817 C C    . GLY   B 1 70  ? 19.897 -20.779 21.954  1   60.004  ? 82  GLY   A C    1 ? 2 
ATOM   2818 O O    . GLY   B 1 70  ? 20.985 -20.279 21.765  1   63.806  ? 82  GLY   A O    1 ? 2 
ATOM   2819 H H    . GLY   B 1 70  ? 17.391 -21.014 23.554  1   53.48   ? 82  GLY   A H    1 c 2 
ATOM   2820 H HA2  . GLY   B 1 70  ? 19.331 -19.907 23.749  1   56.838  ? 82  GLY   A HA2  1 c 2 
ATOM   2821 H HA3  . GLY   B 1 70  ? 20.1   -21.286 23.956  1   59.796  ? 82  GLY   A HA3  1 c 2 
ATOM   2822 N N    . LYS   B 1 71  ? 19.107 -21.299 20.975  1   60.466  ? 83  LYS   A N    1 ? 2 
ATOM   2823 C CA   . LYS   B 1 71  ? 19.498 -21.41  19.573  1   58.722  ? 83  LYS   A CA   1 ? 2 
ATOM   2824 C C    . LYS   B 1 71  ? 18.959 -20.214 18.786  1   68.64   ? 83  LYS   A C    1 ? 2 
ATOM   2825 O O    . LYS   B 1 71  ? 18.763 -20.34  17.581  1   79.106  ? 83  LYS   A O    1 ? 2 
ATOM   2826 C CB   . LYS   B 1 71  ? 19.048 -22.718 18.901  1   62.783  ? 83  LYS   A CB   1 ? 2 
ATOM   2827 H H    . LYS   B 1 71  ? 18.27  -21.586 21.204  1   59.005  ? 83  LYS   A H    1 c 2 
ATOM   2828 H HA   . LYS   B 1 71  ? 20.488 -21.382 19.531  1   62.9    ? 83  LYS   A HA   1 c 2 
ATOM   2829 H HB2  . LYS   B 1 71  ? 19.638 -23.249 18.704  0   30      ? 83  LYS   A HB2  1 c 2 
ATOM   2830 H HB3  . LYS   B 1 71  ? 17.9   -22.654 18.982  0   30      ? 83  LYS   A HB3  1 c 2 
ATOM   2831 N N    . GLY   B 1 72  ? 18.692 -19.103 19.498  1   68.016  ? 84  GLY   A N    1 ? 2 
ATOM   2832 C CA   . GLY   B 1 72  ? 18.194 -17.831 18.994  1   65.317  ? 84  GLY   A CA   1 ? 2 
ATOM   2833 C C    . GLY   B 1 72  ? 16.985 -17.943 18.065  1   60.738  ? 84  GLY   A C    1 ? 2 
ATOM   2834 O O    . GLY   B 1 72  ? 16.774 -17.067 17.227  1   54.095  ? 84  GLY   A O    1 ? 2 
ATOM   2835 H H    . GLY   B 1 72  ? 18.842 -19.149 20.397  1   66.979  ? 84  GLY   A H    1 c 2 
ATOM   2836 H HA2  . GLY   B 1 72  ? 17.954 -17.263 19.764  1   63.247  ? 84  GLY   A HA2  1 c 2 
ATOM   2837 H HA3  . GLY   B 1 72  ? 18.926 -17.379 18.512  1   65.043  ? 84  GLY   A HA3  1 c 2 
ATOM   2838 N N    . GLN   B 1 73  ? 16.117 -18.933 18.295  1   53.061  ? 85  GLN   A N    1 ? 2 
ATOM   2839 C CA   . GLN   B 1 73  ? 14.857 -19.068 17.585  1   49.759  ? 85  GLN   A CA   1 ? 2 
ATOM   2840 C C    . GLN   B 1 73  ? 13.734 -18.254 18.209  1   51.728  ? 85  GLN   A C    1 ? 2 
ATOM   2841 O O    . GLN   B 1 73  ? 12.717 -17.987 17.561  1   44.57   ? 85  GLN   A O    1 ? 2 
ATOM   2842 C CB   . GLN   B 1 73  ? 14.428 -20.518 17.622  1   56.031  ? 85  GLN   A CB   1 ? 2 
ATOM   2843 C CG   . GLN   B 1 73  ? 15.451 -21.451 17.009  1   69.535  ? 85  GLN   A CG   1 ? 2 
ATOM   2844 C CD   . GLN   B 1 73  ? 15.12  -22.904 17.269  1   68.783  ? 85  GLN   A CD   1 ? 2 
ATOM   2845 O OE1  . GLN   B 1 73  ? 14.156 -23.259 17.969  1   64.711  ? 85  GLN   A OE1  1 ? 2 
ATOM   2846 N NE2  . GLN   B 1 73  ? 15.99  -23.751 16.743  1   70.531  ? 85  GLN   A NE2  1 ? 2 
ATOM   2847 H H    . GLN   B 1 73  ? 16.313 -19.545 18.945  1   54.898  ? 85  GLN   A H    1 c 2 
ATOM   2848 H HA   . GLN   B 1 73  ? 14.985 -18.782 16.645  1   52.406  ? 85  GLN   A HA   1 c 2 
ATOM   2849 H HB2  . GLN   B 1 73  ? 14.275 -20.778 18.555  1   56.729  ? 85  GLN   A HB2  1 c 2 
ATOM   2850 H HB3  . GLN   B 1 73  ? 13.579 -20.612 17.141  1   57.227  ? 85  GLN   A HB3  1 c 2 
ATOM   2851 H HG2  . GLN   B 1 73  ? 15.491 -21.3   16.041  1   66.85   ? 85  GLN   A HG2  1 c 2 
ATOM   2852 H HG3  . GLN   B 1 73  ? 16.337 -21.257 17.38   1   66.123  ? 85  GLN   A HG3  1 c 2 
ATOM   2853 H HE21 . GLN   B 1 73  ? 15.871 -24.624 16.843  1   72.244  ? 85  GLN   A HE21 1 c 2 
ATOM   2854 H HE22 . GLN   B 1 73  ? 16.689 -23.447 16.289  1   71.274  ? 85  GLN   A HE22 1 c 2 
ATOM   2855 N N    . VAL   B 1 74  ? 13.959 -17.756 19.434  1   46.555  ? 86  VAL   A N    1 ? 2 
ATOM   2856 C CA   . VAL   B 1 74  ? 13.002 -16.905 20.091  1   45.041  ? 86  VAL   A CA   1 ? 2 
ATOM   2857 C C    . VAL   B 1 74  ? 13.772 -15.709 20.643  1   39.355  ? 86  VAL   A C    1 ? 2 
ATOM   2858 O O    . VAL   B 1 74  ? 14.989 -15.719 20.648  1   41.396  ? 86  VAL   A O    1 ? 2 
ATOM   2859 C CB   . VAL   B 1 74  ? 12.361 -17.669 21.264  1   45.801  ? 86  VAL   A CB   1 ? 2 
ATOM   2860 C CG1  . VAL   B 1 74  ? 11.454 -18.757 20.764  1   46.579  ? 86  VAL   A CG1  1 ? 2 
ATOM   2861 C CG2  . VAL   B 1 74  ? 13.438 -18.217 22.19   1   47.831  ? 86  VAL   A CG2  1 ? 2 
ATOM   2862 H H    . VAL   B 1 74  ? 14.742 -17.951 19.862  1   47.95   ? 86  VAL   A H    1 c 2 
ATOM   2863 H HA   . VAL   B 1 74  ? 12.318 -16.608 19.462  1   43.992  ? 86  VAL   A HA   1 c 2 
ATOM   2864 H HB   . VAL   B 1 74  ? 11.816 -17.025 21.773  1   44.759  ? 86  VAL   A HB   1 c 2 
ATOM   2865 H HG11 . VAL   B 1 74  ? 11.968 -19.395 20.241  1   47.902  ? 86  VAL   A HG11 1 c 2 
ATOM   2866 H HG12 . VAL   B 1 74  ? 10.758 -18.37  20.207  1   46.399  ? 86  VAL   A HG12 1 c 2 
ATOM   2867 H HG13 . VAL   B 1 74  ? 11.047 -19.213 21.52   1   46.888  ? 86  VAL   A HG13 1 c 2 
ATOM   2868 H HG21 . VAL   B 1 74  ? 13.019 -18.614 22.972  1   47.473  ? 86  VAL   A HG21 1 c 2 
ATOM   2869 H HG22 . VAL   B 1 74  ? 14.027 -17.498 22.472  1   46.837  ? 86  VAL   A HG22 1 c 2 
ATOM   2870 H HG23 . VAL   B 1 74  ? 13.955 -18.896 21.725  1   48.607  ? 86  VAL   A HG23 1 c 2 
ATOM   2871 N N    . ILE   B 1 75  ? 13.062 -14.722 21.138  1   40.451  ? 87  ILE   A N    1 ? 2 
ATOM   2872 C CA   . ILE   B 1 75  ? 13.691 -13.522 21.708  1   42.022  ? 87  ILE   A CA   1 ? 2 
ATOM   2873 C C    . ILE   B 1 75  ? 14.592 -13.891 22.908  1   41.882  ? 87  ILE   A C    1 ? 2 
ATOM   2874 O O    . ILE   B 1 75  ? 14.392 -14.961 23.557  1   38.243  ? 87  ILE   A O    1 ? 2 
ATOM   2875 C CB   . ILE   B 1 75  ? 12.613 -12.5   22.13   1   39.467  ? 87  ILE   A CB   1 ? 2 
ATOM   2876 C CG1  . ILE   B 1 75  ? 11.508 -13.093 23.017  1   41.531  ? 87  ILE   A CG1  1 ? 2 
ATOM   2877 C CG2  . ILE   B 1 75  ? 12.026 -11.795 20.923  1   35.173  ? 87  ILE   A CG2  1 ? 2 
ATOM   2878 C CD1  . ILE   B 1 75  ? 10.438 -12.06  23.452  1   40.539  ? 87  ILE   A CD1  1 ? 2 
ATOM   2879 H H    . ILE   B 1 75  ? 12.15  -14.774 21.108  1   40.178  ? 87  ILE   A H    1 c 2 
ATOM   2880 H HA   . ILE   B 1 75  ? 14.248 -13.113 21.018  1   41.24   ? 87  ILE   A HA   1 c 2 
ATOM   2881 H HB   . ILE   B 1 75  ? 13.067 -11.819 22.664  1   39.03   ? 87  ILE   A HB   1 c 2 
ATOM   2882 H HG12 . ILE   B 1 75  ? 11.063 -13.816 22.532  1   41.358  ? 87  ILE   A HG12 1 c 2 
ATOM   2883 H HG13 . ILE   B 1 75  ? 11.918 -13.477 23.818  1   41.289  ? 87  ILE   A HG13 1 c 2 
ATOM   2884 H HG21 . ILE   B 1 75  ? 11.5   -11.032 21.213  1   35.827  ? 87  ILE   A HG21 1 c 2 
ATOM   2885 H HG22 . ILE   B 1 75  ? 11.457 -12.411 20.431  1   36.682  ? 87  ILE   A HG22 1 c 2 
ATOM   2886 H HG23 . ILE   B 1 75  ? 12.744 -11.487 20.344  1   36.528  ? 87  ILE   A HG23 1 c 2 
ATOM   2887 H HD11 . ILE   B 1 75  ? 10.879 -11.259 23.793  1   40.328  ? 87  ILE   A HD11 1 c 2 
ATOM   2888 H HD12 . ILE   B 1 75  ? 9.882  -12.447 24.155  1   40.804  ? 87  ILE   A HD12 1 c 2 
ATOM   2889 H HD13 . ILE   B 1 75  ? 9.876  -11.822 22.691  1   40.46   ? 87  ILE   A HD13 1 c 2 
ATOM   2890 N N    . LYS   B 1 76  ? 15.585 -13.008 23.163  1   39.814  ? 88  LYS   A N    1 ? 2 
ATOM   2891 C CA   . LYS   B 1 76  ? 16.559 -13.133 24.246  1   39.537  ? 88  LYS   A CA   1 ? 2 
ATOM   2892 C C    . LYS   B 1 76  ? 15.849 -13.505 25.556  1   36.47   ? 88  LYS   A C    1 ? 2 
ATOM   2893 O O    . LYS   B 1 76  ? 16.299 -14.423 26.25   1   40.079  ? 88  LYS   A O    1 ? 2 
ATOM   2894 C CB   . LYS   B 1 76  ? 17.549 -11.965 24.325  1   40.676  ? 88  LYS   A CB   1 ? 2 
ATOM   2895 H H    . LYS   B 1 76  ? 15.652 -12.279 22.616  1   39.669  ? 88  LYS   A H    1 c 2 
ATOM   2896 H HA   . LYS   B 1 76  ? 17.128 -13.912 24.017  1   40.308  ? 88  LYS   A HA   1 c 2 
ATOM   2897 H HB2  . LYS   B 1 76  ? 18.44  -12.335 24.358  0   30      ? 88  LYS   A HB2  1 c 2 
ATOM   2898 H HB3  . LYS   B 1 76  ? 16.978 -11.193 24.477  0   30      ? 88  LYS   A HB3  1 c 2 
ATOM   2899 N N    . ALA   B 1 77  ? 14.775 -12.8   25.888  1   38.965  ? 89  ALA   A N    1 ? 2 
ATOM   2900 C CA   . ALA   B 1 77  ? 14.109 -12.95  27.18   1   38.727  ? 89  ALA   A CA   1 ? 2 
ATOM   2901 C C    . ALA   B 1 77  ? 13.569 -14.373 27.356  1   36.043  ? 89  ALA   A C    1 ? 2 
ATOM   2902 O O    . ALA   B 1 77  ? 13.457 -14.852 28.502  1   34.076  ? 89  ALA   A O    1 ? 2 
ATOM   2903 C CB   . ALA   B 1 77  ? 13.008 -11.997 27.325  1   35.88   ? 89  ALA   A CB   1 ? 2 
ATOM   2904 H H    . ALA   B 1 77  ? 14.439 -12.194 25.291  1   37.29   ? 89  ALA   A H    1 c 2 
ATOM   2905 H HA   . ALA   B 1 77  ? 14.781 -12.782 27.897  1   38.538  ? 89  ALA   A HA   1 c 2 
ATOM   2906 H HB1  . ALA   B 1 77  ? 13.346 -11.09  27.236  1   36.256  ? 89  ALA   A HB1  1 c 2 
ATOM   2907 H HB2  . ALA   B 1 77  ? 12.342 -12.16  26.637  1   35.926  ? 89  ALA   A HB2  1 c 2 
ATOM   2908 H HB3  . ALA   B 1 77  ? 12.598 -12.101 28.2    1   36.802  ? 89  ALA   A HB3  1 c 2 
ATOM   2909 N N    . TRP   B 1 78  ? 13.234 -15.059 26.241  1   37.566  ? 90  TRP   A N    1 ? 2 
ATOM   2910 C CA   . TRP   B 1 78  ? 12.706 -16.421 26.326  1   37.246  ? 90  TRP   A CA   1 ? 2 
ATOM   2911 C C    . TRP   B 1 78  ? 13.838 -17.402 26.619  1   40.351  ? 90  TRP   A C    1 ? 2 
ATOM   2912 O O    . TRP   B 1 78  ? 13.695 -18.316 27.457  1   42.661  ? 90  TRP   A O    1 ? 2 
ATOM   2913 C CB   . TRP   B 1 78  ? 11.883 -16.815 25.12   1   35.232  ? 90  TRP   A CB   1 ? 2 
ATOM   2914 C CG   . TRP   B 1 78  ? 10.399 -16.605 25.222  1   34.937  ? 90  TRP   A CG   1 ? 2 
ATOM   2915 C CD1  . TRP   B 1 78  ? 9.698  -15.465 25.523  1   37.618  ? 90  TRP   A CD1  1 ? 2 
ATOM   2916 C CD2  . TRP   B 1 78  ? 9.398  -17.605 24.918  1   43.701  ? 90  TRP   A CD2  1 ? 2 
ATOM   2917 N NE1  . TRP   B 1 78  ? 8.359  -15.715 25.529  1   36.494  ? 90  TRP   A NE1  1 ? 2 
ATOM   2918 C CE2  . TRP   B 1 78  ? 8.141  -17.012 25.133  1   39.345  ? 90  TRP   A CE2  1 ? 2 
ATOM   2919 C CE3  . TRP   B 1 78  ? 9.451  -18.935 24.513  1   42.365  ? 90  TRP   A CE3  1 ? 2 
ATOM   2920 C CZ2  . TRP   B 1 78  ? 6.954  -17.715 24.968  1   36.877  ? 90  TRP   A CZ2  1 ? 2 
ATOM   2921 C CZ3  . TRP   B 1 78  ? 8.271  -19.626 24.345  1   40.914  ? 90  TRP   A CZ3  1 ? 2 
ATOM   2922 C CH2  . TRP   B 1 78  ? 7.035  -18.993 24.508  1   41.952  ? 90  TRP   A CH2  1 ? 2 
ATOM   2923 H H    . TRP   B 1 78  ? 13.323 -14.668 25.42   1   36.453  ? 90  TRP   A H    1 c 2 
ATOM   2924 H HA   . TRP   B 1 78  ? 12.092 -16.443 27.11   1   37.396  ? 90  TRP   A HA   1 c 2 
ATOM   2925 H HB2  . TRP   B 1 78  ? 12.215 -16.315 24.344  1   35.324  ? 90  TRP   A HB2  1 c 2 
ATOM   2926 H HB3  . TRP   B 1 78  ? 12.049 -17.763 24.932  1   36.737  ? 90  TRP   A HB3  1 c 2 
ATOM   2927 H HD1  . TRP   B 1 78  ? 10.087 -14.648 25.793  1   35.933  ? 90  TRP   A HD1  1 c 2 
ATOM   2928 H HE1  . TRP   B 1 78  ? 7.741  -15.131 25.705  1   36.933  ? 90  TRP   A HE1  1 c 2 
ATOM   2929 H HE3  . TRP   B 1 78  ? 10.28  -19.358 24.368  1   42.864  ? 90  TRP   A HE3  1 c 2 
ATOM   2930 H HZ2  . TRP   B 1 78  ? 6.12   -17.292 25.087  1   38.402  ? 90  TRP   A HZ2  1 c 2 
ATOM   2931 H HZ3  . TRP   B 1 78  ? 8.297  -20.52  24.046  1   42.992  ? 90  TRP   A HZ3  1 c 2 
ATOM   2932 H HH2  . TRP   B 1 78  ? 6.245  -19.494 24.403  1   41.526  ? 90  TRP   A HH2  1 c 2 
ATOM   2933 N N    . ASP   B 1 79  ? 14.988 -17.157 25.997  1   37.886  ? 91  ASP   A N    1 ? 2 
ATOM   2934 C CA   . ASP   B 1 79  ? 16.125 -18.026 26.225  1   44.913  ? 91  ASP   A CA   1 ? 2 
ATOM   2935 C C    . ASP   B 1 79  ? 16.516 -17.951 27.711  1   49.994  ? 91  ASP   A C    1 ? 2 
ATOM   2936 O O    . ASP   B 1 79  ? 16.926 -18.915 28.349  1   48.425  ? 91  ASP   A O    1 ? 2 
ATOM   2937 C CB   . ASP   B 1 79  ? 17.223 -17.702 25.236  1   42.938  ? 91  ASP   A CB   1 ? 2 
ATOM   2938 C CG   . ASP   B 1 79  ? 17.086 -18.348 23.846  1   45.052  ? 91  ASP   A CG   1 ? 2 
ATOM   2939 O OD1  . ASP   B 1 79  ? 16.417 -19.377 23.714  1   45.665  ? 91  ASP   A OD1  1 ? 2 
ATOM   2940 O OD2  . ASP   B 1 79  ? 17.692 -17.868 22.932  1   42.052  ? 91  ASP   A OD2  1 ? 2 
ATOM   2941 H H    . ASP   B 1 79  ? 15.065 -16.453 25.42   1   38.894  ? 91  ASP   A H    1 c 2 
ATOM   2942 H HA   . ASP   B 1 79  ? 15.84  -18.949 26.039  1   44.768  ? 91  ASP   A HA   1 c 2 
ATOM   2943 H HB2  . ASP   B 1 79  ? 17.268 -16.73  25.117  1   42.85   ? 91  ASP   A HB2  1 c 2 
ATOM   2944 H HB3  . ASP   B 1 79  ? 18.077 -17.993 25.617  1   45.164  ? 91  ASP   A HB3  1 c 2 
ATOM   2945 N N    . ILE   B 1 80  ? 16.41  -16.763 28.284  1   44.561  ? 92  ILE   A N    1 ? 2 
ATOM   2946 C CA   . ILE   B 1 80  ? 16.936 -16.531 29.617  1   48.131  ? 92  ILE   A CA   1 ? 2 
ATOM   2947 C C    . ILE   B 1 80  ? 15.899 -16.998 30.631  1   41.784  ? 92  ILE   A C    1 ? 2 
ATOM   2948 O O    . ILE   B 1 80  ? 16.212 -17.711 31.567  1   48.958  ? 92  ILE   A O    1 ? 2 
ATOM   2949 C CB   . ILE   B 1 80  ? 17.227 -15.036 29.789  1   55.079  ? 92  ILE   A CB   1 ? 2 
ATOM   2950 C CG1  . ILE   B 1 80  ? 18.377 -14.564 28.965  1   55.471  ? 92  ILE   A CG1  1 ? 2 
ATOM   2951 C CG2  . ILE   B 1 80  ? 17.443 -14.748 31.275  1   63.312  ? 92  ILE   A CG2  1 ? 2 
ATOM   2952 C CD1  . ILE   B 1 80  ? 18.449 -13.035 28.969  1   62.701  ? 92  ILE   A CD1  1 ? 2 
ATOM   2953 H H    . ILE   B 1 80  ? 16.017 -16.07  27.835  1   44.89   ? 92  ILE   A H    1 c 2 
ATOM   2954 H HA   . ILE   B 1 80  ? 17.763 -17.037 29.735  1   48.928  ? 92  ILE   A HA   1 c 2 
ATOM   2955 H HB   . ILE   B 1 80  ? 16.433 -14.543 29.502  1   53.34   ? 92  ILE   A HB   1 c 2 
ATOM   2956 H HG12 . ILE   B 1 80  ? 19.209 -14.931 29.328  1   58.625  ? 92  ILE   A HG12 1 c 2 
ATOM   2957 H HG13 . ILE   B 1 80  ? 18.272 -14.883 28.046  1   56.45   ? 92  ILE   A HG13 1 c 2 
ATOM   2958 H HG21 . ILE   B 1 80  ? 17.764 -13.84  31.392  1   61.07   ? 92  ILE   A HG21 1 c 2 
ATOM   2959 H HG22 . ILE   B 1 80  ? 18.099 -15.369 31.635  1   62.531  ? 92  ILE   A HG22 1 c 2 
ATOM   2960 H HG23 . ILE   B 1 80  ? 16.604 -14.852 31.755  1   60.667  ? 92  ILE   A HG23 1 c 2 
ATOM   2961 H HD11 . ILE   B 1 80  ? 17.589 -12.666 28.692  1   58.794  ? 92  ILE   A HD11 1 c 2 
ATOM   2962 H HD12 . ILE   B 1 80  ? 19.14  -12.747 28.342  1   60.37   ? 92  ILE   A HD12 1 c 2 
ATOM   2963 H HD13 . ILE   B 1 80  ? 18.669 -12.708 29.861  1   60.998  ? 92  ILE   A HD13 1 c 2 
ATOM   2964 N N    . GLY   B 1 81  ? 14.643 -16.687 30.343  1   39.96   ? 93  GLY   A N    1 ? 2 
ATOM   2965 C CA   . GLY   B 1 81  ? 13.56  -16.927 31.255  1   41.087  ? 93  GLY   A CA   1 ? 2 
ATOM   2966 C C    . GLY   B 1 81  ? 13.123 -18.383 31.325  1   40.755  ? 93  GLY   A C    1 ? 2 
ATOM   2967 O O    . GLY   B 1 81  ? 12.95  -18.893 32.436  1   41.419  ? 93  GLY   A O    1 ? 2 
ATOM   2968 H H    . GLY   B 1 81  ? 14.453 -16.3   29.537  1   39.292  ? 93  GLY   A H    1 c 2 
ATOM   2969 H HA2  . GLY   B 1 81  ? 13.834 -16.63  32.155  1   41.407  ? 93  GLY   A HA2  1 c 2 
ATOM   2970 H HA3  . GLY   B 1 81  ? 12.791 -16.374 30.982  1   39.462  ? 93  GLY   A HA3  1 c 2 
ATOM   2971 N N    . VAL   B 1 82  ? 13.107 -19.081 30.187  1   38.206  ? 94  VAL   A N    1 ? 2 
ATOM   2972 C CA   . VAL   B 1 82  ? 12.644 -20.449 30.202  1   39.524  ? 94  VAL   A CA   1 ? 2 
ATOM   2973 C C    . VAL   B 1 82  ? 13.72  -21.306 30.855  1   39.966  ? 94  VAL   A C    1 ? 2 
ATOM   2974 O O    . VAL   B 1 82  ? 13.422 -22.343 31.47   1   45.734  ? 94  VAL   A O    1 ? 2 
ATOM   2975 C CB   . VAL   B 1 82  ? 12.215 -20.987 28.804  1   44.628  ? 94  VAL   A CB   1 ? 2 
ATOM   2976 C CG1  . VAL   B 1 82  ? 11.936 -22.478 28.791  1   47.976  ? 94  VAL   A CG1  1 ? 2 
ATOM   2977 C CG2  . VAL   B 1 82  ? 10.969 -20.304 28.29   1   42.925  ? 94  VAL   A CG2  1 ? 2 
ATOM   2978 H H    . VAL   B 1 82  ? 13.38  -18.703 29.401  1   38.021  ? 94  VAL   A H    1 c 2 
ATOM   2979 H HA   . VAL   B 1 82  ? 11.855 -20.482 30.777  1   40.169  ? 94  VAL   A HA   1 c 2 
ATOM   2980 H HB   . VAL   B 1 82  ? 12.953 -20.803 28.177  1   43.584  ? 94  VAL   A HB   1 c 2 
ATOM   2981 H HG11 . VAL   B 1 82  ? 11.335 -22.702 29.521  1   47.963  ? 94  VAL   A HG11 1 c 2 
ATOM   2982 H HG12 . VAL   B 1 82  ? 12.769 -22.967 28.896  1   48.629  ? 94  VAL   A HG12 1 c 2 
ATOM   2983 H HG13 . VAL   B 1 82  ? 11.524 -22.722 27.946  1   47.42   ? 94  VAL   A HG13 1 c 2 
ATOM   2984 H HG21 . VAL   B 1 82  ? 10.766 -20.627 27.396  1   43.023  ? 94  VAL   A HG21 1 c 2 
ATOM   2985 H HG22 . VAL   B 1 82  ? 11.114 -19.343 28.26   1   41.898  ? 94  VAL   A HG22 1 c 2 
ATOM   2986 H HG23 . VAL   B 1 82  ? 10.223 -20.5   28.882  1   43.31   ? 94  VAL   A HG23 1 c 2 
ATOM   2987 N N    . ALA   B 1 83  ? 14.975 -20.916 30.699  1   40.786  ? 95  ALA   A N    1 ? 2 
ATOM   2988 C CA   . ALA   B 1 83  ? 16.111 -21.574 31.354  1   42.5    ? 95  ALA   A CA   1 ? 2 
ATOM   2989 C C    . ALA   B 1 83  ? 15.932 -21.626 32.865  1   47.97   ? 95  ALA   A C    1 ? 2 
ATOM   2990 O O    . ALA   B 1 83  ? 16.512 -22.508 33.509  1   53.015  ? 95  ALA   A O    1 ? 2 
ATOM   2991 C CB   . ALA   B 1 83  ? 17.442 -20.871 31.043  1   42.143  ? 95  ALA   A CB   1 ? 2 
ATOM   2992 H H    . ALA   B 1 83  ? 15.149 -20.208 30.146  1   39.408  ? 95  ALA   A H    1 c 2 
ATOM   2993 H HA   . ALA   B 1 83  ? 16.157 -22.511 31.018  1   44.281  ? 95  ALA   A HA   1 c 2 
ATOM   2994 H HB1  . ALA   B 1 83  ? 17.578 -20.839 30.081  1   41.746  ? 95  ALA   A HB1  1 c 2 
ATOM   2995 H HB2  . ALA   B 1 83  ? 17.425 -19.967 31.395  1   41.562  ? 95  ALA   A HB2  1 c 2 
ATOM   2996 H HB3  . ALA   B 1 83  ? 18.174 -21.362 31.453  1   44.177  ? 95  ALA   A HB3  1 c 2 
ATOM   2997 N N    . THR   B 1 84  ? 15.191 -20.666 33.451  1   50.683  ? 96  THR   A N    1 ? 2 
ATOM   2998 C CA   . THR   B 1 84  ? 15.04  -20.629 34.911  1   51.822  ? 96  THR   A CA   1 ? 2 
ATOM   2999 C C    . THR   B 1 84  ? 13.842 -21.452 35.365  1   51.616  ? 96  THR   A C    1 ? 2 
ATOM   3000 O O    . THR   B 1 84  ? 13.608 -21.544 36.542  1   54.908  ? 96  THR   A O    1 ? 2 
ATOM   3001 C CB   . THR   B 1 84  ? 14.848 -19.204 35.425  1   49.763  ? 96  THR   A CB   1 ? 2 
ATOM   3002 O OG1  . THR   B 1 84  ? 13.664 -18.587 34.906  1   43.515  ? 96  THR   A OG1  1 ? 2 
ATOM   3003 C CG2  . THR   B 1 84  ? 16.048 -18.318 35.176  1   55.973  ? 96  THR   A CG2  1 ? 2 
ATOM   3004 H H    . THR   B 1 84  ? 14.791 -20.018 32.946  1   47.798  ? 96  THR   A H    1 c 2 
ATOM   3005 H HA   . THR   B 1 84  ? 15.853 -21     35.32   1   53.24   ? 96  THR   A HA   1 c 2 
ATOM   3006 H HB   . THR   B 1 84  ? 14.754 -19.257 36.406  1   51.499  ? 96  THR   A HB   1 c 2 
ATOM   3007 H HG1  . THR   B 1 84  ? 13.567 -18.673 34.078  0   30      ? 96  THR   A HG1  1 c 2 
ATOM   3008 H HG21 . THR   B 1 84  ? 15.885 -17.437 35.551  1   53.555  ? 96  THR   A HG21 1 c 2 
ATOM   3009 H HG22 . THR   B 1 84  ? 16.199 -18.239 34.219  1   52.758  ? 96  THR   A HG22 1 c 2 
ATOM   3010 H HG23 . THR   B 1 84  ? 16.833 -18.708 35.595  1   55.691  ? 96  THR   A HG23 1 c 2 
ATOM   3011 N N    . MET   B 1 85  ? 13.036 -22.012 34.46   1   48.486  ? 97  MET   A N    1 ? 2 
ATOM   3012 C CA   . MET   B 1 85  ? 11.786 -22.658 34.843  1   48.084  ? 97  MET   A CA   1 ? 2 
ATOM   3013 C C    . MET   B 1 85  ? 11.92  -24.162 35.046  1   53.028  ? 97  MET   A C    1 ? 2 
ATOM   3014 O O    . MET   B 1 85  ? 12.766 -24.846 34.461  1   49.159  ? 97  MET   A O    1 ? 2 
ATOM   3015 C CB   . MET   B 1 85  ? 10.732 -22.38  33.75   1   46.554  ? 97  MET   A CB   1 ? 2 
ATOM   3016 C CG   . MET   B 1 85  ? 10.361 -20.921 33.626  1   44.402  ? 97  MET   A CG   1 ? 2 
ATOM   3017 S SD   . MET   B 1 85  ? 9.227  -20.623 32.245  1   46.167  ? 97  MET   A SD   1 ? 2 
ATOM   3018 C CE   . MET   B 1 85  ? 7.705  -21.402 32.811  1   45.778  ? 97  MET   A CE   1 ? 2 
ATOM   3019 H H    . MET   B 1 85  ? 13.267 -21.997 33.577  1   47.893  ? 97  MET   A H    1 c 2 
ATOM   3020 H HA   . MET   B 1 85  ? 11.481 -22.255 35.694  1   49.302  ? 97  MET   A HA   1 c 2 
ATOM   3021 H HB2  . MET   B 1 85  ? 11.082 -22.694 32.889  1   46.17   ? 97  MET   A HB2  1 c 2 
ATOM   3022 H HB3  . MET   B 1 85  ? 9.925  -22.898 33.953  1   47.111  ? 97  MET   A HB3  1 c 2 
ATOM   3023 H HG2  . MET   B 1 85  ? 9.938  -20.621 34.451  1   45.552  ? 97  MET   A HG2  1 c 2 
ATOM   3024 H HG3  . MET   B 1 85  ? 11.169 -20.39  33.491  1   44.597  ? 97  MET   A HG3  1 c 2 
ATOM   3025 H HE1  . MET   B 1 85  ? 7.019  -21.309 32.124  1   45.583  ? 97  MET   A HE1  1 c 2 
ATOM   3026 H HE2  . MET   B 1 85  ? 7.867  -22.348 32.98   1   47.496  ? 97  MET   A HE2  1 c 2 
ATOM   3027 H HE3  . MET   B 1 85  ? 7.405  -20.971 33.632  1   46.493  ? 97  MET   A HE3  1 c 2 
ATOM   3028 N N    . LYS   B 1 86  ? 11.045 -24.676 35.923  1   60.273  ? 98  LYS   A N    1 ? 2 
ATOM   3029 C CA   . LYS   B 1 86  ? 10.925 -26.09  36.238  1   61.401  ? 98  LYS   A CA   1 ? 2 
ATOM   3030 C C    . LYS   B 1 86  ? 9.754  -26.689 35.465  1   60.037  ? 98  LYS   A C    1 ? 2 
ATOM   3031 O O    . LYS   B 1 86  ? 8.821  -25.983 35.094  1   56.102  ? 98  LYS   A O    1 ? 2 
ATOM   3032 C CB   . LYS   B 1 86  ? 10.695 -26.335 37.731  1   69.503  ? 98  LYS   A CB   1 ? 2 
ATOM   3033 C CG   . LYS   B 1 86  ? 11.727 -25.864 38.729  1   73.214  ? 98  LYS   A CG   1 ? 2 
ATOM   3034 C CD   . LYS   B 1 86  ? 13.089 -26.51  38.548  1   79.193  ? 98  LYS   A CD   1 ? 2 
ATOM   3035 C CE   . LYS   B 1 86  ? 14.114 -25.859 39.428  1   83.881  ? 98  LYS   A CE   1 ? 2 
ATOM   3036 N NZ   . LYS   B 1 86  ? 13.676 -25.694 40.812  1   85.048  ? 98  LYS   A NZ   1 ? 2 
ATOM   3037 H H    . LYS   B 1 86  ? 10.483 -24.098 36.353  1   57.788  ? 98  LYS   A H    1 c 2 
ATOM   3038 H HA   . LYS   B 1 86  ? 11.758 -26.548 35.961  1   63.219  ? 98  LYS   A HA   1 c 2 
ATOM   3039 H HB2  . LYS   B 1 86  ? 9.842  -25.914 37.97   1   67.913  ? 98  LYS   A HB2  1 c 2 
ATOM   3040 H HB3  . LYS   B 1 86  ? 10.582 -27.301 37.858  1   70.291  ? 98  LYS   A HB3  1 c 2 
ATOM   3041 H HG2  . LYS   B 1 86  ? 11.821 -24.89  38.646  1   72.057  ? 98  LYS   A HG2  1 c 2 
ATOM   3042 H HG3  . LYS   B 1 86  ? 11.397 -26.059 39.633  1   75.231  ? 98  LYS   A HG3  1 c 2 
ATOM   3043 H HD2  . LYS   B 1 86  ? 13.029 -27.464 38.772  1   80.785  ? 98  LYS   A HD2  1 c 2 
ATOM   3044 H HD3  . LYS   B 1 86  ? 13.368 -26.431 37.612  1   77.423  ? 98  LYS   A HD3  1 c 2 
ATOM   3045 H HE2  . LYS   B 1 86  ? 14.93  -26.39  39.419  1   84.375  ? 98  LYS   A HE2  1 c 2 
ATOM   3046 H HE3  . LYS   B 1 86  ? 14.329 -24.981 39.065  1   81.139  ? 98  LYS   A HE3  1 c 2 
ATOM   3047 H HZ1  . LYS   B 1 86  ? 13.236 -26.437 41.088  1   86.427  ? 98  LYS   A HZ1  1 c 2 
ATOM   3048 H HZ2  . LYS   B 1 86  ? 13.128 -24.976 40.884  1   83.772  ? 98  LYS   A HZ2  1 c 2 
ATOM   3049 H HZ3  . LYS   B 1 86  ? 14.399 -25.566 41.343  1   86.641  ? 98  LYS   A HZ3  1 c 2 
ATOM   3050 N N    . LYS   B 1 87  ? 9.83   -28.002 35.191  1   59.181  ? 99  LYS   A N    1 ? 2 
ATOM   3051 C CA   . LYS   B 1 87  ? 8.762  -28.722 34.508  1   61.303  ? 99  LYS   A CA   1 ? 2 
ATOM   3052 C C    . LYS   B 1 87  ? 7.463  -28.567 35.289  1   65.526  ? 99  LYS   A C    1 ? 2 
ATOM   3053 O O    . LYS   B 1 87  ? 7.468  -28.719 36.527  1   66.265  ? 99  LYS   A O    1 ? 2 
ATOM   3054 C CB   . LYS   B 1 87  ? 9.046  -30.215 34.435  1   64.192  ? 99  LYS   A CB   1 ? 2 
ATOM   3055 C CG   . LYS   B 1 87  ? 8.029  -31.043 33.638  1   67.616  ? 99  LYS   A CG   1 ? 2 
ATOM   3056 C CD   . LYS   B 1 87  ? 8.436  -32.527 33.637  1   74.374  ? 99  LYS   A CD   1 ? 2 
ATOM   3057 C CE   . LYS   B 1 87  ? 7.49   -33.465 32.96   1   81.454  ? 99  LYS   A CE   1 ? 2 
ATOM   3058 N NZ   . LYS   B 1 87  ? 7.149  -32.859 31.677  1   76.688  ? 99  LYS   A NZ   1 ? 2 
ATOM   3059 H H    . LYS   B 1 87  ? 10.578 -28.465 35.441  1   61.683  ? 99  LYS   A H    1 c 2 
ATOM   3060 H HA   . LYS   B 1 87  ? 8.652  -28.347 33.598  1   60.068  ? 99  LYS   A HA   1 c 2 
ATOM   3061 H HB2  . LYS   B 1 87  ? 9.931  -30.343 34.031  1   64.894  ? 99  LYS   A HB2  1 c 2 
ATOM   3062 H HB3  . LYS   B 1 87  ? 9.084  -30.57  35.349  1   66.393  ? 99  LYS   A HB3  1 c 2 
ATOM   3063 H HG2  . LYS   B 1 87  ? 7.14   -30.947 34.044  1   67.871  ? 99  LYS   A HG2  1 c 2 
ATOM   3064 H HG3  . LYS   B 1 87  ? 7.995  -30.707 32.717  1   66.463  ? 99  LYS   A HG3  1 c 2 
ATOM   3065 H HD2  . LYS   B 1 87  ? 9.315  -32.603 33.205  1   74.761  ? 99  LYS   A HD2  1 c 2 
ATOM   3066 H HD3  . LYS   B 1 87  ? 8.549  -32.815 34.569  1   76.159  ? 99  LYS   A HD3  1 c 2 
ATOM   3067 H HE2  . LYS   B 1 87  ? 7.912  -34.33  32.813  1   81.611  ? 99  LYS   A HE2  1 c 2 
ATOM   3068 H HE3  . LYS   B 1 87  ? 6.685  -33.586 33.493  1   80.21   ? 99  LYS   A HE3  1 c 2 
ATOM   3069 H HZ1  . LYS   B 1 87  ? 7.89   -32.527 31.279  1   76.297  ? 99  LYS   A HZ1  1 c 2 
ATOM   3070 H HZ2  . LYS   B 1 87  ? 6.54   -32.197 31.792  1   75.886  ? 99  LYS   A HZ2  1 c 2 
ATOM   3071 H HZ3  . LYS   B 1 87  ? 6.789  -33.491 31.137  1   78.72   ? 99  LYS   A HZ3  1 c 2 
ATOM   3072 N N    . GLY   B 1 88  ? 6.399  -28.151 34.559  1   60.651  ? 100 GLY   A N    1 ? 2 
ATOM   3073 C CA   . GLY   B 1 88  ? 5.097  -27.838 35.149  1   59.611  ? 100 GLY   A CA   1 ? 2 
ATOM   3074 C C    . GLY   B 1 88  ? 4.964  -26.414 35.718  1   59.281  ? 100 GLY   A C    1 ? 2 
ATOM   3075 O O    . GLY   B 1 88  ? 3.899  -26.055 36.192  1   62.137  ? 100 GLY   A O    1 ? 2 
ATOM   3076 H H    . GLY   B 1 88  ? 6.494  -28.062 33.653  1   60.144  ? 100 GLY   A H    1 c 2 
ATOM   3077 H HA2  . GLY   B 1 88  ? 4.405  -27.97  34.46   1   60.093  ? 100 GLY   A HA2  1 c 2 
ATOM   3078 H HA3  . GLY   B 1 88  ? 4.918  -28.486 35.871  1   62.251  ? 100 GLY   A HA3  1 c 2 
ATOM   3079 N N    . GLU   B 1 89  ? 6.019  -25.593 35.675  1   55.031  ? 101 GLU   A N    1 ? 2 
ATOM   3080 C CA   . GLU   B 1 89  ? 5.986  -24.235 36.189  1   56.22   ? 101 GLU   A CA   1 ? 2 
ATOM   3081 C C    . GLU   B 1 89  ? 5.213  -23.309 35.225  1   54.288  ? 101 GLU   A C    1 ? 2 
ATOM   3082 O O    . GLU   B 1 89  ? 5.153  -23.526 33.987  1   45.967  ? 101 GLU   A O    1 ? 2 
ATOM   3083 C CB   . GLU   B 1 89  ? 7.422  -23.753 36.452  1   52.352  ? 101 GLU   A CB   1 ? 2 
ATOM   3084 C CG   . GLU   B 1 89  ? 7.52   -22.327 36.992  1   53.949  ? 101 GLU   A CG   1 ? 2 
ATOM   3085 C CD   . GLU   B 1 89  ? 8.934  -21.814 37.156  1   50.866  ? 101 GLU   A CD   1 ? 2 
ATOM   3086 O OE1  . GLU   B 1 89  ? 9.832  -22.566 37.687  1   53.815  ? 101 GLU   A OE1  1 ? 2 
ATOM   3087 O OE2  . GLU   B 1 89  ? 9.173  -20.651 36.723  1   52.763  ? 101 GLU   A OE2  1 ? 2 
ATOM   3088 H H    . GLU   B 1 89  ? 6.798  -25.893 35.303  1   56.176  ? 101 GLU   A H    1 c 2 
ATOM   3089 H HA   . GLU   B 1 89  ? 5.509  -24.251 37.056  1   56.344  ? 101 GLU   A HA   1 c 2 
ATOM   3090 H HB2  . GLU   B 1 89  ? 7.851  -24.367 37.083  1   55.44   ? 101 GLU   A HB2  1 c 2 
ATOM   3091 H HB3  . GLU   B 1 89  ? 7.923  -23.791 35.611  1   52.729  ? 101 GLU   A HB3  1 c 2 
ATOM   3092 H HG2  . GLU   B 1 89  ? 7.041  -21.722 36.388  1   51.207  ? 101 GLU   A HG2  1 c 2 
ATOM   3093 H HG3  . GLU   B 1 89  ? 7.074  -22.287 37.865  1   53.855  ? 101 GLU   A HG3  1 c 2 
ATOM   3094 N N    . ILE   B 1 90  ? 4.525  -22.312 35.842  1   54.66   ? 102 ILE   A N    1 ? 2 
ATOM   3095 C CA   . ILE   B 1 90  ? 3.925  -21.191 35.129  1   52.354  ? 102 ILE   A CA   1 ? 2 
ATOM   3096 C C    . ILE   B 1 90  ? 4.563  -19.93  35.676  1   52.77   ? 102 ILE   A C    1 ? 2 
ATOM   3097 O O    . ILE   B 1 90  ? 4.429  -19.645 36.888  1   51.828  ? 102 ILE   A O    1 ? 2 
ATOM   3098 C CB   . ILE   B 1 90  ? 2.387  -21.103 35.231  1   53.676  ? 102 ILE   A CB   1 ? 2 
ATOM   3099 C CG1  . ILE   B 1 90  ? 1.689  -22.313 34.612  1   60.221  ? 102 ILE   A CG1  1 ? 2 
ATOM   3100 C CG2  . ILE   B 1 90  ? 1.895  -19.793 34.57   1   49.461  ? 102 ILE   A CG2  1 ? 2 
ATOM   3101 C CD1  . ILE   B 1 90  ? 0.173  -22.404 34.765  1   64.16   ? 102 ILE   A CD1  1 ? 2 
ATOM   3102 H H    . ILE   B 1 90  ? 4.431  -22.343 36.75   1   55.578  ? 102 ILE   A H    1 c 2 
ATOM   3103 H HA   . ILE   B 1 90  ? 4.159  -21.272 34.187  1   51.605  ? 102 ILE   A HA   1 c 2 
ATOM   3104 H HB   . ILE   B 1 90  ? 2.15   -21.072 36.18   1   55.261  ? 102 ILE   A HB   1 c 2 
ATOM   3105 H HG12 . ILE   B 1 90  ? 1.898  -22.325 33.656  1   58.335  ? 102 ILE   A HG12 1 c 2 
ATOM   3106 H HG13 . ILE   B 1 90  ? 2.08   -23.12  35.003  1   60.477  ? 102 ILE   A HG13 1 c 2 
ATOM   3107 H HG21 . ILE   B 1 90  ? 0.924  -19.783 34.543  1   51.068  ? 102 ILE   A HG21 1 c 2 
ATOM   3108 H HG22 . ILE   B 1 90  ? 2.241  -19.736 33.663  1   48.98   ? 102 ILE   A HG22 1 c 2 
ATOM   3109 H HG23 . ILE   B 1 90  ? 2.207  -19.029 35.082  1   49.861  ? 102 ILE   A HG23 1 c 2 
ATOM   3110 H HD11 . ILE   B 1 90  ? -0.046 -22.537 35.706  1   64.775  ? 102 ILE   A HD11 1 c 2 
ATOM   3111 H HD12 . ILE   B 1 90  ? -0.158 -23.162 34.247  1   64.184  ? 102 ILE   A HD12 1 c 2 
ATOM   3112 H HD13 . ILE   B 1 90  ? -0.253 -21.586 34.445  1   62.498  ? 102 ILE   A HD13 1 c 2 
ATOM   3113 N N    . ALA   B 1 91  ? 5.218  -19.204 34.769  1   45.918  ? 103 ALA   A N    1 ? 2 
ATOM   3114 C CA   . ALA   B 1 91  ? 5.805  -17.923 35.098  1   44.778  ? 103 ALA   A CA   1 ? 2 
ATOM   3115 C C    . ALA   B 1 91  ? 5.307  -16.78  34.254  1   42.967  ? 103 ALA   A C    1 ? 2 
ATOM   3116 O O    . ALA   B 1 91  ? 4.941  -16.949 33.065  1   42.52   ? 103 ALA   A O    1 ? 2 
ATOM   3117 C CB   . ALA   B 1 91  ? 7.293  -17.995 35.006  1   45.837  ? 103 ALA   A CB   1 ? 2 
ATOM   3118 H H    . ALA   B 1 91  ? 5.303  -19.519 33.915  1   46.306  ? 103 ALA   A H    1 c 2 
ATOM   3119 H HA   . ALA   B 1 91  ? 5.565  -17.718 36.042  1   46.235  ? 103 ALA   A HA   1 c 2 
ATOM   3120 H HB1  . ALA   B 1 91  ? 7.623  -18.7   35.589  1   46.677  ? 103 ALA   A HB1  1 c 2 
ATOM   3121 H HB2  . ALA   B 1 91  ? 7.555  -18.187 34.09   1   44.464  ? 103 ALA   A HB2  1 c 2 
ATOM   3122 H HB3  . ALA   B 1 91  ? 7.68   -17.146 35.279  1   45.087  ? 103 ALA   A HB3  1 c 2 
ATOM   3123 N N    . HIS   B 1 92  ? 5.485  -15.577 34.811  1   47.913  ? 104 HIS   A N    1 ? 2 
ATOM   3124 C CA   . HIS   B 1 92  ? 5.186  -14.342 34.088  1   44.536  ? 104 HIS   A CA   1 ? 2 
ATOM   3125 C C    . HIS   B 1 92  ? 6.467  -13.559 33.795  1   45.115  ? 104 HIS   A C    1 ? 2 
ATOM   3126 O O    . HIS   B 1 92  ? 7.267  -13.284 34.707  1   45.357  ? 104 HIS   A O    1 ? 2 
ATOM   3127 C CB   . HIS   B 1 92  ? 4.171  -13.423 34.778  1   44.77   ? 104 HIS   A CB   1 ? 2 
ATOM   3128 C CG   . HIS   B 1 92  ? 2.781  -13.928 34.887  1   47.21   ? 104 HIS   A CG   1 ? 2 
ATOM   3129 N ND1  . HIS   B 1 92  ? 1.834  -13.339 35.694  1   45.649  ? 104 HIS   A ND1  1 ? 2 
ATOM   3130 C CD2  . HIS   B 1 92  ? 2.218  -15.021 34.419  1   50.833  ? 104 HIS   A CD2  1 ? 2 
ATOM   3131 C CE1  . HIS   B 1 92  ? 0.712  -14.022 35.65   1   47.216  ? 104 HIS   A CE1  1 ? 2 
ATOM   3132 N NE2  . HIS   B 1 92  ? 0.925  -15.051 34.91   1   51.925  ? 104 HIS   A NE2  1 ? 2 
ATOM   3133 H H    . HIS   B 1 92  ? 5.802  -15.519 35.667  1   47.056  ? 104 HIS   A H    1 c 2 
ATOM   3134 H HA   . HIS   B 1 92  ? 4.791  -14.605 33.223  1   44.328  ? 104 HIS   A HA   1 c 2 
ATOM   3135 H HB2  . HIS   B 1 92  ? 4.501  -13.226 35.681  1   46.191  ? 104 HIS   A HB2  1 c 2 
ATOM   3136 H HB3  . HIS   B 1 92  ? 4.154  -12.568 34.295  1   44.444  ? 104 HIS   A HB3  1 c 2 
ATOM   3137 H HD1  . HIS   B 1 92  ? 1.843  -12.548 36.058  0   30      ? 104 HIS   A HD1  1 c 2 
ATOM   3138 H HD2  . HIS   B 1 92  ? 2.608  -15.657 33.852  1   49.136  ? 104 HIS   A HD2  1 c 2 
ATOM   3139 H HE1  . HIS   B 1 92  ? -0.091 -13.812 36.095  1   49.679  ? 104 HIS   A HE1  1 c 2 
ATOM   3140 H HE2  . HIS   B 1 92  ? 0.35   -15.72  34.598  0   30      ? 104 HIS   A HE2  1 c 2 
ATOM   3141 N N    . LEU   B 1 93  ? 6.594  -13.074 32.531  1   38.619  ? 105 LEU   A N    1 ? 2 
ATOM   3142 C CA   . LEU   B 1 93  ? 7.761  -12.312 32.187  1   39.944  ? 105 LEU   A CA   1 ? 2 
ATOM   3143 C C    . LEU   B 1 93  ? 7.299  -10.947 31.71   1   42.705  ? 105 LEU   A C    1 ? 2 
ATOM   3144 O O    . LEU   B 1 93  ? 6.34   -10.854 30.939  1   43.884  ? 105 LEU   A O    1 ? 2 
ATOM   3145 C CB   . LEU   B 1 93  ? 8.666  -12.885 31.133  1   40.323  ? 105 LEU   A CB   1 ? 2 
ATOM   3146 C CG   . LEU   B 1 93  ? 9.163  -14.294 31.339  1   39.342  ? 105 LEU   A CG   1 ? 2 
ATOM   3147 C CD1  . LEU   B 1 93  ? 9.826  -14.948 30.144  1   40.728  ? 105 LEU   A CD1  1 ? 2 
ATOM   3148 C CD2  . LEU   B 1 93  ? 10.142 -14.263 32.48   1   42.707  ? 105 LEU   A CD2  1 ? 2 
ATOM   3149 H H    . LEU   B 1 93  ? 5.949  -13.225 31.901  1   39.868  ? 105 LEU   A H    1 c 2 
ATOM   3150 H HA   . LEU   B 1 93  ? 8.289  -12.182 33.011  1   41.145  ? 105 LEU   A HA   1 c 2 
ATOM   3151 H HB2  . LEU   B 1 93  ? 8.188  -12.852 30.273  1   38.934  ? 105 LEU   A HB2  1 c 2 
ATOM   3152 H HB3  . LEU   B 1 93  ? 9.447  -12.291 31.047  1   39.358  ? 105 LEU   A HB3  1 c 2 
ATOM   3153 H HG   . LEU   B 1 93  ? 8.393  -14.857 31.609  1   40.955  ? 105 LEU   A HG   1 c 2 
ATOM   3154 H HD11 . LEU   B 1 93  ? 9.194  -14.998 29.408  1   39.617  ? 105 LEU   A HD11 1 c 2 
ATOM   3155 H HD12 . LEU   B 1 93  ? 10.115 -15.844 30.383  1   40.933  ? 105 LEU   A HD12 1 c 2 
ATOM   3156 H HD13 . LEU   B 1 93  ? 10.597 -14.422 29.872  1   39.743  ? 105 LEU   A HD13 1 c 2 
ATOM   3157 H HD21 . LEU   B 1 93  ? 9.685  -13.998 33.295  1   42.726  ? 105 LEU   A HD21 1 c 2 
ATOM   3158 H HD22 . LEU   B 1 93  ? 10.85  -13.627 32.285  1   41.691  ? 105 LEU   A HD22 1 c 2 
ATOM   3159 H HD23 . LEU   B 1 93  ? 10.528 -15.147 32.6    1   42.708  ? 105 LEU   A HD23 1 c 2 
ATOM   3160 N N    . LEU   B 1 94  ? 7.976  -9.936  32.216  1   39.959  ? 106 LEU   A N    1 ? 2 
ATOM   3161 C CA   . LEU   B 1 94  ? 7.792  -8.583  31.665  1   41.809  ? 106 LEU   A CA   1 ? 2 
ATOM   3162 C C    . LEU   B 1 94  ? 9.112  -8.141  31.064  1   36.398  ? 106 LEU   A C    1 ? 2 
ATOM   3163 O O    . LEU   B 1 94  ? 10.127 -8.227  31.723  1   38.008  ? 106 LEU   A O    1 ? 2 
ATOM   3164 C CB   . LEU   B 1 94  ? 7.3    -7.611  32.714  1   45.979  ? 106 LEU   A CB   1 ? 2 
ATOM   3165 C CG   . LEU   B 1 94  ? 7.277  -6.147  32.27   1   40.695  ? 106 LEU   A CG   1 ? 2 
ATOM   3166 C CD1  . LEU   B 1 94  ? 6.104  -5.986  31.319  1   42.574  ? 106 LEU   A CD1  1 ? 2 
ATOM   3167 C CD2  . LEU   B 1 94  ? 7.232  -5.238  33.423  1   50.046  ? 106 LEU   A CD2  1 ? 2 
ATOM   3168 H H    . LEU   B 1 94  ? 8.56   -10.064 32.908  1   41.872  ? 106 LEU   A H    1 c 2 
ATOM   3169 H HA   . LEU   B 1 94  ? 7.121  -8.633  30.938  1   40.346  ? 106 LEU   A HA   1 c 2 
ATOM   3170 H HB2  . LEU   B 1 94  ? 6.389  -7.875  32.978  1   44.591  ? 106 LEU   A HB2  1 c 2 
ATOM   3171 H HB3  . LEU   B 1 94  ? 7.882  -7.69   33.504  1   44.944  ? 106 LEU   A HB3  1 c 2 
ATOM   3172 H HG   . LEU   B 1 94  ? 8.11   -5.958  31.766  1   42.682  ? 106 LEU   A HG   1 c 2 
ATOM   3173 H HD11 . LEU   B 1 94  ? 6.261  -6.508  30.515  1   40.803  ? 106 LEU   A HD11 1 c 2 
ATOM   3174 H HD12 . LEU   B 1 94  ? 6.007  -5.048  31.08   1   42.023  ? 106 LEU   A HD12 1 c 2 
ATOM   3175 H HD13 . LEU   B 1 94  ? 5.289  -6.293  31.751  1   42.571  ? 106 LEU   A HD13 1 c 2 
ATOM   3176 H HD21 . LEU   B 1 94  ? 8.036  -5.348  33.957  1   48.024  ? 106 LEU   A HD21 1 c 2 
ATOM   3177 H HD22 . LEU   B 1 94  ? 6.453  -5.444  33.967  1   48.396  ? 106 LEU   A HD22 1 c 2 
ATOM   3178 H HD23 . LEU   B 1 94  ? 7.174  -4.321  33.112  1   47.668  ? 106 LEU   A HD23 1 c 2 
ATOM   3179 N N    . ILE   B 1 95  ? 9.071  -7.773  29.784  1   40.312  ? 107 ILE   A N    1 ? 2 
ATOM   3180 C CA   . ILE   B 1 95  ? 10.247 -7.762  28.927  1   38.599  ? 107 ILE   A CA   1 ? 2 
ATOM   3181 C C    . ILE   B 1 95  ? 10.322 -6.405  28.231  1   40.031  ? 107 ILE   A C    1 ? 2 
ATOM   3182 O O    . ILE   B 1 95  ? 9.421  -6.095  27.476  1   37.92   ? 107 ILE   A O    1 ? 2 
ATOM   3183 C CB   . ILE   B 1 95  ? 10.083 -8.841  27.869  1   37.281  ? 107 ILE   A CB   1 ? 2 
ATOM   3184 C CG1  . ILE   B 1 95  ? 9.903  -10.235 28.534  1   40.087  ? 107 ILE   A CG1  1 ? 2 
ATOM   3185 C CG2  . ILE   B 1 95  ? 11.237 -8.747  26.871  1   32.971  ? 107 ILE   A CG2  1 ? 2 
ATOM   3186 C CD1  . ILE   B 1 95  ? 9.333  -11.281 27.569  1   38.801  ? 107 ILE   A CD1  1 ? 2 
ATOM   3187 H H    . ILE   B 1 95  ? 8.271  -7.51   29.426  1   38.641  ? 107 ILE   A H    1 c 2 
ATOM   3188 H HA   . ILE   B 1 95  ? 11.053 -7.925  29.452  1   39.445  ? 107 ILE   A HA   1 c 2 
ATOM   3189 H HB   . ILE   B 1 95  ? 9.258  -8.646  27.381  1   36.726  ? 107 ILE   A HB   1 c 2 
ATOM   3190 H HG12 . ILE   B 1 95  ? 10.77  -10.545 28.864  1   39.715  ? 107 ILE   A HG12 1 c 2 
ATOM   3191 H HG13 . ILE   B 1 95  ? 9.299  -10.152 29.299  1   39.827  ? 107 ILE   A HG13 1 c 2 
ATOM   3192 H HG21 . ILE   B 1 95  ? 11.279 -9.563  26.344  1   33.944  ? 107 ILE   A HG21 1 c 2 
ATOM   3193 H HG22 . ILE   B 1 95  ? 12.074 -8.631  27.35   1   34.531  ? 107 ILE   A HG22 1 c 2 
ATOM   3194 H HG23 . ILE   B 1 95  ? 11.098 -7.99   26.277  1   33.763  ? 107 ILE   A HG23 1 c 2 
ATOM   3195 H HD11 . ILE   B 1 95  ? 8.513  -10.937 27.168  1   38.834  ? 107 ILE   A HD11 1 c 2 
ATOM   3196 H HD12 . ILE   B 1 95  ? 9.136  -12.104 28.055  1   39.584  ? 107 ILE   A HD12 1 c 2 
ATOM   3197 H HD13 . ILE   B 1 95  ? 9.983  -11.468 26.865  1   38.772  ? 107 ILE   A HD13 1 c 2 
ATOM   3198 N N    . LYS   B 1 96  ? 11.422 -5.673  28.463  1   37.979  ? 108 LYS   A N    1 ? 2 
ATOM   3199 C CA   . LYS   B 1 96  ? 11.656 -4.415  27.824  1   36.498  ? 108 LYS   A CA   1 ? 2 
ATOM   3200 C C    . LYS   B 1 96  ? 12.145 -4.709  26.407  1   31.727  ? 108 LYS   A C    1 ? 2 
ATOM   3201 O O    . LYS   B 1 96  ? 12.646 -5.774  26.105  1   34.366  ? 108 LYS   A O    1 ? 2 
ATOM   3202 C CB   . LYS   B 1 96  ? 12.688 -3.632  28.642  1   34.386  ? 108 LYS   A CB   1 ? 2 
ATOM   3203 C CG   . LYS   B 1 96  ? 12.274 -3.299  30.11   1   41.327  ? 108 LYS   A CG   1 ? 2 
ATOM   3204 C CD   . LYS   B 1 96  ? 11.224 -2.196  30.186  1   38.71   ? 108 LYS   A CD   1 ? 2 
ATOM   3205 C CE   . LYS   B 1 96  ? 10.73  -1.799  31.539  1   46.259  ? 108 LYS   A CE   1 ? 2 
ATOM   3206 N NZ   . LYS   B 1 96  ? 10.146 -3.071  32.031  1   50.465  ? 108 LYS   A NZ   1 ? 2 
ATOM   3207 H H    . LYS   B 1 96  ? 12.048 -5.988  29.05   1   38.677  ? 108 LYS   A H    1 c 2 
ATOM   3208 H HA   . LYS   B 1 96  ? 10.803 -3.912  27.782  1   35.49   ? 108 LYS   A HA   1 c 2 
ATOM   3209 H HB2  . LYS   B 1 96  ? 13.518 -4.153  28.67   1   36.404  ? 108 LYS   A HB2  1 c 2 
ATOM   3210 H HB3  . LYS   B 1 96  ? 12.886 -2.79   28.183  1   36.416  ? 108 LYS   A HB3  1 c 2 
ATOM   3211 H HG2  . LYS   B 1 96  ? 11.924 -4.113  30.53   1   39.415  ? 108 LYS   A HG2  1 c 2 
ATOM   3212 H HG3  . LYS   B 1 96  ? 13.073 -3.019  30.607  1   40.305  ? 108 LYS   A HG3  1 c 2 
ATOM   3213 H HD2  . LYS   B 1 96  ? 11.597 -1.399  29.75   1   40.875  ? 108 LYS   A HD2  1 c 2 
ATOM   3214 H HD3  . LYS   B 1 96  ? 10.454 -2.472  29.642  1   39.909  ? 108 LYS   A HD3  1 c 2 
ATOM   3215 H HE2  . LYS   B 1 96  ? 11.459 -1.512  32.117  1   46.847  ? 108 LYS   A HE2  1 c 2 
ATOM   3216 H HE3  . LYS   B 1 96  ? 10.047 -1.107  31.484  1   46.249  ? 108 LYS   A HE3  1 c 2 
ATOM   3217 H HZ1  . LYS   B 1 96  ? 10.782 -3.561  32.453  1   49.134  ? 108 LYS   A HZ1  1 c 2 
ATOM   3218 H HZ2  . LYS   B 1 96  ? 9.794  -3.558  31.353  1   47.628  ? 108 LYS   A HZ2  1 c 2 
ATOM   3219 H HZ3  . LYS   B 1 96  ? 9.483  -2.89   32.618  1   49.783  ? 108 LYS   A HZ3  1 c 2 
ATOM   3220 N N    . PRO   B 1 97  ? 12.125 -3.714  25.516  1   36.353  ? 109 PRO   A N    1 ? 2 
ATOM   3221 C CA   . PRO   B 1 97  ? 12.489 -3.947  24.108  1   33.563  ? 109 PRO   A CA   1 ? 2 
ATOM   3222 C C    . PRO   B 1 97  ? 13.854 -4.548  23.887  1   35.273  ? 109 PRO   A C    1 ? 2 
ATOM   3223 O O    . PRO   B 1 97  ? 14.012 -5.363  22.993  1   32.85   ? 109 PRO   A O    1 ? 2 
ATOM   3224 C CB   . PRO   B 1 97  ? 12.428 -2.553  23.482  1   35.497  ? 109 PRO   A CB   1 ? 2 
ATOM   3225 C CG   . PRO   B 1 97  ? 12.33  -1.588  24.599  1   35.336  ? 109 PRO   A CG   1 ? 2 
ATOM   3226 C CD   . PRO   B 1 97  ? 11.694 -2.334  25.774  1   34.141  ? 109 PRO   A CD   1 ? 2 
ATOM   3227 H HA   . PRO   B 1 97  ? 11.812 -4.52   23.691  1   34.073  ? 109 PRO   A HA   1 c 2 
ATOM   3228 H HB2  . PRO   B 1 97  ? 13.227 -2.379  22.948  1   35.083  ? 109 PRO   A HB2  1 c 2 
ATOM   3229 H HB3  . PRO   B 1 97  ? 11.65  -2.478  22.896  1   34.645  ? 109 PRO   A HB3  1 c 2 
ATOM   3230 H HG2  . PRO   B 1 97  ? 13.215 -1.259  24.847  1   35.965  ? 109 PRO   A HG2  1 c 2 
ATOM   3231 H HG3  . PRO   B 1 97  ? 11.776 -0.824  24.344  1   35.627  ? 109 PRO   A HG3  1 c 2 
ATOM   3232 H HD2  . PRO   B 1 97  ? 12.034 -2.007  26.625  1   35.806  ? 109 PRO   A HD2  1 c 2 
ATOM   3233 H HD3  . PRO   B 1 97  ? 10.72  -2.262  25.761  1   34.99   ? 109 PRO   A HD3  1 c 2 
ATOM   3234 N N    . GLU   B 1 98  ? 14.813 -4.223  24.729  1   34.234  ? 110 GLU   A N    1 ? 2 
ATOM   3235 C CA   . GLU   B 1 98  ? 16.192 -4.661  24.524  1   36.867  ? 110 GLU   A CA   1 ? 2 
ATOM   3236 C C    . GLU   B 1 98  ? 16.297 -6.171  24.657  1   38.948  ? 110 GLU   A C    1 ? 2 
ATOM   3237 O O    . GLU   B 1 98  ? 17.236 -6.748  24.084  1   37.831  ? 110 GLU   A O    1 ? 2 
ATOM   3238 C CB   . GLU   B 1 98  ? 17.172 -4.001  25.515  1   47.563  ? 110 GLU   A CB   1 ? 2 
ATOM   3239 C CG   . GLU   B 1 98  ? 17.114 -2.466  25.441  1   51.768  ? 110 GLU   A CG   1 ? 2 
ATOM   3240 C CD   . GLU   B 1 98  ? 15.912 -1.632  25.909  1   51.848  ? 110 GLU   A CD   1 ? 2 
ATOM   3241 O OE1  . GLU   B 1 98  ? 15.228 -2.138  26.834  1   43.194  ? 110 GLU   A OE1  1 ? 2 
ATOM   3242 O OE2  . GLU   B 1 98  ? 15.612 -0.522  25.335  1   47.843  ? 110 GLU   A OE2  1 ? 2 
ATOM   3243 H H    . GLU   B 1 98  ? 14.613 -3.727  25.469  1   35.695  ? 110 GLU   A H    1 c 2 
ATOM   3244 H HA   . GLU   B 1 98  ? 16.462 -4.408  23.604  1   38.261  ? 110 GLU   A HA   1 c 2 
ATOM   3245 H HB2  . GLU   B 1 98  ? 16.952 -4.294  26.424  1   46.169  ? 110 GLU   A HB2  1 c 2 
ATOM   3246 H HB3  . GLU   B 1 98  ? 18.082 -4.304  25.314  1   46.538  ? 110 GLU   A HB3  1 c 2 
ATOM   3247 H HG2  . GLU   B 1 98  ? 17.894 -2.127  25.93   1   52.126  ? 110 GLU   A HG2  1 c 2 
ATOM   3248 H HG3  . GLU   B 1 98  ? 17.276 -2.22   24.506  1   50.747  ? 110 GLU   A HG3  1 c 2 
ATOM   3249 N N    . TYR   B 1 99  ? 15.296 -6.809  25.301  1   36.682  ? 111 TYR   A N    1 ? 2 
ATOM   3250 C CA   . TYR   B 1 99  ? 15.32  -8.275  25.403  1   40.455  ? 111 TYR   A CA   1 ? 2 
ATOM   3251 C C    . TYR   B 1 99  ? 14.282 -8.899  24.497  1   32.657  ? 111 TYR   A C    1 ? 2 
ATOM   3252 O O    . TYR   B 1 99  ? 14     -10.099 24.58   1   34.001  ? 111 TYR   A O    1 ? 2 
ATOM   3253 C CB   . TYR   B 1 99  ? 15.219 -8.615  26.921  1   38.399  ? 111 TYR   A CB   1 ? 2 
ATOM   3254 C CG   . TYR   B 1 99  ? 16.536 -8.173  27.574  1   40.51   ? 111 TYR   A CG   1 ? 2 
ATOM   3255 C CD1  . TYR   B 1 99  ? 17.605 -9.059  27.654  1   40.116  ? 111 TYR   A CD1  1 ? 2 
ATOM   3256 C CD2  . TYR   B 1 99  ? 16.684 -6.872  28.107  1   46.727  ? 111 TYR   A CD2  1 ? 2 
ATOM   3257 C CE1  . TYR   B 1 99  ? 18.746 -8.712  28.349  1   46.311  ? 111 TYR   A CE1  1 ? 2 
ATOM   3258 C CE2  . TYR   B 1 99  ? 17.847 -6.477  28.73   1   44.748  ? 111 TYR   A CE2  1 ? 2 
ATOM   3259 C CZ   . TYR   B 1 99  ? 18.867 -7.419  28.862  1   48.216  ? 111 TYR   A CZ   1 ? 2 
ATOM   3260 O OH   . TYR   B 1 99  ? 20.01  -7.093  29.527  1   42.956  ? 111 TYR   A OH   1 ? 2 
ATOM   3261 H H    . TYR   B 1 99  ? 14.618 -6.342  25.698  1   37.63   ? 111 TYR   A H    1 c 2 
ATOM   3262 H HA   . TYR   B 1 99  ? 16.21  -8.586  25.09   1   38.349  ? 111 TYR   A HA   1 c 2 
ATOM   3263 H HB2  . TYR   B 1 99  ? 14.465 -8.125  27.32   1   38.885  ? 111 TYR   A HB2  1 c 2 
ATOM   3264 H HB3  . TYR   B 1 99  ? 15.096 -9.583  27.035  1   39.229  ? 111 TYR   A HB3  1 c 2 
ATOM   3265 H HD1  . TYR   B 1 99  ? 17.498 -9.947  27.35   1   41.366  ? 111 TYR   A HD1  1 c 2 
ATOM   3266 H HD2  . TYR   B 1 99  ? 15.968 -6.261  28.038  1   43.863  ? 111 TYR   A HD2  1 c 2 
ATOM   3267 H HE1  . TYR   B 1 99  ? 19.462 -9.32   28.424  1   46.409  ? 111 TYR   A HE1  1 c 2 
ATOM   3268 H HE2  . TYR   B 1 99  ? 17.926 -5.622  29.116  1   46.605  ? 111 TYR   A HE2  1 c 2 
ATOM   3269 H HH   . TYR   B 1 99  ? 20.556 -7.767  29.538  0   30      ? 111 TYR   A HH   1 c 2 
ATOM   3270 N N    . ALA   B 1 100 ? 13.698 -8.07   23.619  1   35.51   ? 112 ALA   A N    1 ? 2 
ATOM   3271 C CA   . ALA   B 1 100 ? 12.717 -8.558  22.652  1   36.087  ? 112 ALA   A CA   1 ? 2 
ATOM   3272 C C    . ALA   B 1 100 ? 13.065 -8.122  21.223  1   32.569  ? 112 ALA   A C    1 ? 2 
ATOM   3273 O O    . ALA   B 1 100 ? 13.942 -8.745  20.657  1   37.193  ? 112 ALA   A O    1 ? 2 
ATOM   3274 C CB   . ALA   B 1 100 ? 11.323 -8.133  23.067  1   37.595  ? 112 ALA   A CB   1 ? 2 
ATOM   3275 H H    . ALA   B 1 100 ? 13.916 -7.184  23.612  1   34.973  ? 112 ALA   A H    1 c 2 
ATOM   3276 H HA   . ALA   B 1 100 ? 12.749 -9.552  22.667  1   35.677  ? 112 ALA   A HA   1 c 2 
ATOM   3277 H HB1  . ALA   B 1 100 ? 11.08  -8.579  23.896  1   37.114  ? 112 ALA   A HB1  1 c 2 
ATOM   3278 H HB2  . ALA   B 1 100 ? 11.301 -7.171  23.204  1   36.976  ? 112 ALA   A HB2  1 c 2 
ATOM   3279 H HB3  . ALA   B 1 100 ? 10.685 -8.375  22.375  1   36.928  ? 112 ALA   A HB3  1 c 2 
ATOM   3280 N N    . TYR   B 1 101 ? 12.318 -7.17   20.617  1   33.787  ? 113 TYR   A N    1 ? 2 
ATOM   3281 C CA   . TYR   B 1 101 ? 12.507 -6.769  19.22   1   32.125  ? 113 TYR   A CA   1 ? 2 
ATOM   3282 C C    . TYR   B 1 101 ? 13.138 -5.378  19.048  1   33.927  ? 113 TYR   A C    1 ? 2 
ATOM   3283 O O    . TYR   B 1 101 ? 13.274 -4.952  17.969  1   31.408  ? 113 TYR   A O    1 ? 2 
ATOM   3284 C CB   . TYR   B 1 101 ? 11.146 -6.771  18.539  1   30.967  ? 113 TYR   A CB   1 ? 2 
ATOM   3285 C CG   . TYR   B 1 101 ? 10.594 -8.183  18.526  1   30.566  ? 113 TYR   A CG   1 ? 2 
ATOM   3286 C CD1  . TYR   B 1 101 ? 10.985 -9.109  17.604  1   35.293  ? 113 TYR   A CD1  1 ? 2 
ATOM   3287 C CD2  . TYR   B 1 101 ? 9.766  -8.62   19.573  1   31.193  ? 113 TYR   A CD2  1 ? 2 
ATOM   3288 C CE1  . TYR   B 1 101 ? 10.472 -10.402 17.617  1   38.013  ? 113 TYR   A CE1  1 ? 2 
ATOM   3289 C CE2  . TYR   B 1 101 ? 9.212  -9.879  19.568  1   32.805  ? 113 TYR   A CE2  1 ? 2 
ATOM   3290 C CZ   . TYR   B 1 101 ? 9.575  -10.793 18.598  1   30.388  ? 113 TYR   A CZ   1 ? 2 
ATOM   3291 O OH   . TYR   B 1 101 ? 9.062  -12.115 18.676  1   34.057  ? 113 TYR   A OH   1 ? 2 
ATOM   3292 H H    . TYR   B 1 101 ? 11.669 -6.745  21.099  1   32.887  ? 113 TYR   A H    1 c 2 
ATOM   3293 H HA   . TYR   B 1 101 ? 13.087 -7.439  18.77   1   32.916  ? 113 TYR   A HA   1 c 2 
ATOM   3294 H HB2  . TYR   B 1 101 ? 10.534 -6.181  19.033  1   30.964  ? 113 TYR   A HB2  1 c 2 
ATOM   3295 H HB3  . TYR   B 1 101 ? 11.242 -6.446  17.616  1   31.597  ? 113 TYR   A HB3  1 c 2 
ATOM   3296 H HD1  . TYR   B 1 101 ? 11.565 -8.85   16.906  1   35.099  ? 113 TYR   A HD1  1 c 2 
ATOM   3297 H HD2  . TYR   B 1 101 ? 9.473  -7.995  20.217  1   31.023  ? 113 TYR   A HD2  1 c 2 
ATOM   3298 H HE1  . TYR   B 1 101 ? 10.725 -11.013 16.946  1   36.255  ? 113 TYR   A HE1  1 c 2 
ATOM   3299 H HE2  . TYR   B 1 101 ? 8.634  -10.141 20.263  1   31.785  ? 113 TYR   A HE2  1 c 2 
ATOM   3300 H HH   . TYR   B 1 101 ? 9.384  -12.625 18.018  0   30      ? 113 TYR   A HH   1 c 2 
ATOM   3301 N N    . GLY   B 1 102 ? 13.55  -4.717  20.121  1   37.377  ? 114 GLY   A N    1 ? 2 
ATOM   3302 C CA   . GLY   B 1 102 ? 14.39  -3.507  20.121  1   34.929  ? 114 GLY   A CA   1 ? 2 
ATOM   3303 C C    . GLY   B 1 102 ? 13.753 -2.295  19.48   1   37.537  ? 114 GLY   A C    1 ? 2 
ATOM   3304 O O    . GLY   B 1 102 ? 12.511 -2.189  19.223  1   37.389  ? 114 GLY   A O    1 ? 2 
ATOM   3305 H H    . GLY   B 1 102 ? 13.287 -5.039  20.935  1   35.483  ? 114 GLY   A H    1 c 2 
ATOM   3306 H HA2  . GLY   B 1 102 ? 14.622 -3.289  21.054  1   36.238  ? 114 GLY   A HA2  1 c 2 
ATOM   3307 H HA3  . GLY   B 1 102 ? 15.231 -3.715  19.65   1   36.564  ? 114 GLY   A HA3  1 c 2 
ATOM   3308 N N    . SER   B 1 103 ? 14.675 -1.409  19.11   1   36.943  ? 115 SER   A N    1 ? 2 
ATOM   3309 C CA   . SER   B 1 103 ? 14.229 -0.162  18.547  1   40.412  ? 115 SER   A CA   1 ? 2 
ATOM   3310 C C    . SER   B 1 103 ? 13.79  -0.419  17.106  1   33.823  ? 115 SER   A C    1 ? 2 
ATOM   3311 O O    . SER   B 1 103 ? 12.957 0.322   16.61   1   34      ? 115 SER   A O    1 ? 2 
ATOM   3312 C CB   . SER   B 1 103 ? 15.302 0.905   18.758  1   40.539  ? 115 SER   A CB   1 ? 2 
ATOM   3313 O OG   . SER   B 1 103 ? 16.406 0.611   17.916  1   52.186  ? 115 SER   A OG   1 ? 2 
ATOM   3314 H H    . SER   B 1 103 ? 15.569 -1.576  19.208  1   38.222  ? 115 SER   A H    1 c 2 
ATOM   3315 H HA   . SER   B 1 103 ? 13.427 0.123   19.052  1   38.115  ? 115 SER   A HA   1 c 2 
ATOM   3316 H HB2  . SER   B 1 103 ? 14.941 1.784   18.537  1   43.633  ? 115 SER   A HB2  1 c 2 
ATOM   3317 H HB3  . SER   B 1 103 ? 15.587 0.906   19.691  1   43.104  ? 115 SER   A HB3  1 c 2 
ATOM   3318 H HG   . SER   B 1 103 ? 16.969 1.263   18.04   0   30      ? 115 SER   A HG   1 c 2 
ATOM   3319 N N    . ALA   B 1 104 ? 14.312 -1.454  16.409  1   34.513  ? 116 ALA   A N    1 ? 2 
ATOM   3320 C CA   . ALA   B 1 104 ? 13.84  -1.73   15.047  1   37.347  ? 116 ALA   A CA   1 ? 2 
ATOM   3321 C C    . ALA   B 1 104 ? 12.416 -2.293  14.989  1   34.294  ? 116 ALA   A C    1 ? 2 
ATOM   3322 O O    . ALA   B 1 104 ? 11.71  -2.199  13.978  1   34.205  ? 116 ALA   A O    1 ? 2 
ATOM   3323 C CB   . ALA   B 1 104 ? 14.804 -2.707  14.346  1   45.053  ? 116 ALA   A CB   1 ? 2 
ATOM   3324 H H    . ALA   B 1 104 ? 14.962 -1.981  16.776  1   34.744  ? 116 ALA   A H    1 c 2 
ATOM   3325 H HA   . ALA   B 1 104 ? 13.846 -0.869  14.544  1   38.204  ? 116 ALA   A HA   1 c 2 
ATOM   3326 H HB1  . ALA   B 1 104 ? 15.703 -2.338  14.347  1   43.284  ? 116 ALA   A HB1  1 c 2 
ATOM   3327 H HB2  . ALA   B 1 104 ? 14.806 -3.559  14.815  1   42.303  ? 116 ALA   A HB2  1 c 2 
ATOM   3328 H HB3  . ALA   B 1 104 ? 14.517 -2.847  13.428  1   43.431  ? 116 ALA   A HB3  1 c 2 
ATOM   3329 N N    . GLY   B 1 105 ? 12.065 -3.003  16.023  1   35.11   ? 117 GLY   A N    1 ? 2 
ATOM   3330 C CA   . GLY   B 1 105 ? 10.801 -3.713  16.133  1   34.603  ? 117 GLY   A CA   1 ? 2 
ATOM   3331 C C    . GLY   B 1 105 ? 10.739 -4.895  15.159  1   34.888  ? 117 GLY   A C    1 ? 2 
ATOM   3332 O O    . GLY   B 1 105 ? 11.765 -5.381  14.772  1   35.278  ? 117 GLY   A O    1 ? 2 
ATOM   3333 H H    . GLY   B 1 105 ? 12.649 -3.068  16.722  1   34.235  ? 117 GLY   A H    1 c 2 
ATOM   3334 H HA2  . GLY   B 1 105 ? 10.694 -4.041  17.056  1   34.002  ? 117 GLY   A HA2  1 c 2 
ATOM   3335 H HA3  . GLY   B 1 105 ? 10.062 -3.088  15.943  1   34.984  ? 117 GLY   A HA3  1 c 2 
ATOM   3336 N N    . SER   B 1 106 ? 9.516  -5.336  14.824  1   35.949  ? 118 SER   A N    1 ? 2 
ATOM   3337 C CA   . SER   B 1 106 ? 9.259  -6.449  13.916  1   38.559  ? 118 SER   A CA   1 ? 2 
ATOM   3338 C C    . SER   B 1 106 ? 7.876  -6.238  13.284  1   39.792  ? 118 SER   A C    1 ? 2 
ATOM   3339 O O    . SER   B 1 106 ? 6.902  -6.876  13.61   1   38.972  ? 118 SER   A O    1 ? 2 
ATOM   3340 C CB   . SER   B 1 106 ? 9.321  -7.844  14.583  1   36.58   ? 118 SER   A CB   1 ? 2 
ATOM   3341 O OG   . SER   B 1 106 ? 9.475  -8.842  13.579  1   37.364  ? 118 SER   A OG   1 ? 2 
ATOM   3342 H H    . SER   B 1 106 ? 8.795  -4.913  15.193  1   36.082  ? 118 SER   A H    1 c 2 
ATOM   3343 H HA   . SER   B 1 106 ? 9.936  -6.419  13.192  1   38.557  ? 118 SER   A HA   1 c 2 
ATOM   3344 H HB2  . SER   B 1 106 ? 10.078 -7.878  15.197  1   36.08   ? 118 SER   A HB2  1 c 2 
ATOM   3345 H HB3  . SER   B 1 106 ? 8.503  -8.007  15.088  1   36.579  ? 118 SER   A HB3  1 c 2 
ATOM   3346 H HG   . SER   B 1 106 ? 9.561  -9.566  13.934  0   30      ? 118 SER   A HG   1 c 2 
ATOM   3347 N N    . LEU   B 1 107 ? 7.791  -5.204  12.49   1   39.323  ? 119 LEU   A N    1 ? 2 
ATOM   3348 C CA   . LEU   B 1 107 ? 6.583  -4.795  11.819  1   46.638  ? 119 LEU   A CA   1 ? 2 
ATOM   3349 C C    . LEU   B 1 107 ? 6.153  -5.884  10.84   1   48.879  ? 119 LEU   A C    1 ? 2 
ATOM   3350 O O    . LEU   B 1 107 ? 6.99   -6.472  10.122  1   50.733  ? 119 LEU   A O    1 ? 2 
ATOM   3351 C CB   . LEU   B 1 107 ? 6.787  -3.468  11.066  1   41.86   ? 119 LEU   A CB   1 ? 2 
ATOM   3352 C CG   . LEU   B 1 107 ? 7.052  -2.262  11.987  1   42.352  ? 119 LEU   A CG   1 ? 2 
ATOM   3353 C CD1  . LEU   B 1 107 ? 7.305  -1.118  11.02   1   47.5    ? 119 LEU   A CD1  1 ? 2 
ATOM   3354 C CD2  . LEU   B 1 107 ? 5.887  -1.918  12.934  1   44.417  ? 119 LEU   A CD2  1 ? 2 
ATOM   3355 H H    . LEU   B 1 107 ? 8.547  -4.709  12.348  1   40.706  ? 119 LEU   A H    1 c 2 
ATOM   3356 H HA   . LEU   B 1 107 ? 5.883  -4.677  12.505  1   44.043  ? 119 LEU   A HA   1 c 2 
ATOM   3357 H HB2  . LEU   B 1 107 ? 7.554  -3.573  10.456  1   43.812  ? 119 LEU   A HB2  1 c 2 
ATOM   3358 H HB3  . LEU   B 1 107 ? 5.982  -3.284  10.529  1   44.825  ? 119 LEU   A HB3  1 c 2 
ATOM   3359 H HG   . LEU   B 1 107 ? 7.871  -2.433  12.518  1   42.049  ? 119 LEU   A HG   1 c 2 
ATOM   3360 H HD11 . LEU   B 1 107 ? 8.045  -1.345  10.433  1   46.526  ? 119 LEU   A HD11 1 c 2 
ATOM   3361 H HD12 . LEU   B 1 107 ? 7.525  -0.313  11.52   1   45.945  ? 119 LEU   A HD12 1 c 2 
ATOM   3362 H HD13 . LEU   B 1 107 ? 6.508  -0.959  10.488  1   47.584  ? 119 LEU   A HD13 1 c 2 
ATOM   3363 H HD21 . LEU   B 1 107 ? 5.79   -2.62   13.599  1   42.887  ? 119 LEU   A HD21 1 c 2 
ATOM   3364 H HD22 . LEU   B 1 107 ? 5.064  -1.842  12.422  1   45.026  ? 119 LEU   A HD22 1 c 2 
ATOM   3365 H HD23 . LEU   B 1 107 ? 6.068  -1.074  13.38   1   43.585  ? 119 LEU   A HD23 1 c 2 
ATOM   3366 N N    . PRO   B 1 108 ? 4.829  -6.048  10.684  1   49.607  ? 120 PRO   A N    1 ? 2 
ATOM   3367 C CA   . PRO   B 1 108 ? 3.838  -5.235  11.379  1   47.976  ? 120 PRO   A CA   1 ? 2 
ATOM   3368 C C    . PRO   B 1 108 ? 3.369  -5.74   12.743  1   45.185  ? 120 PRO   A C    1 ? 2 
ATOM   3369 O O    . PRO   B 1 108 ? 2.615  -5.029  13.389  1   44.536  ? 120 PRO   A O    1 ? 2 
ATOM   3370 C CB   . PRO   B 1 108 ? 2.634  -5.295  10.449  1   59.31   ? 120 PRO   A CB   1 ? 2 
ATOM   3371 C CG   . PRO   B 1 108 ? 2.76   -6.645  9.805   1   61.214  ? 120 PRO   A CG   1 ? 2 
ATOM   3372 C CD   . PRO   B 1 108 ? 4.228  -6.878  9.624   1   61.946  ? 120 PRO   A CD   1 ? 2 
ATOM   3373 H HA   . PRO   B 1 108 ? 4.148  -4.31   11.453  1   49.012  ? 120 PRO   A HA   1 c 2 
ATOM   3374 H HB2  . PRO   B 1 108 ? 1.797  -5.219  10.946  1   57.491  ? 120 PRO   A HB2  1 c 2 
ATOM   3375 H HB3  . PRO   B 1 108 ? 2.674  -4.584  9.78    1   58.313  ? 120 PRO   A HB3  1 c 2 
ATOM   3376 H HG2  . PRO   B 1 108 ? 2.372  -7.338  10.376  1   61.086  ? 120 PRO   A HG2  1 c 2 
ATOM   3377 H HG3  . PRO   B 1 108 ? 2.303  -6.66   8.941   1   63.403  ? 120 PRO   A HG3  1 c 2 
ATOM   3378 H HD2  . PRO   B 1 108 ? 4.457  -7.82   9.75    1   58.693  ? 120 PRO   A HD2  1 c 2 
ATOM   3379 H HD3  . PRO   B 1 108 ? 4.53   -6.587  8.741   1   60.026  ? 120 PRO   A HD3  1 c 2 
ATOM   3380 N N    . LYS   B 1 109 ? 3.817  -6.92   13.204  1   43.075  ? 121 LYS   A N    1 ? 2 
ATOM   3381 C CA   . LYS   B 1 109 ? 3.386  -7.458  14.497  1   44.369  ? 121 LYS   A CA   1 ? 2 
ATOM   3382 C C    . LYS   B 1 109 ? 3.864  -6.564  15.678  1   45.718  ? 121 LYS   A C    1 ? 2 
ATOM   3383 O O    . LYS   B 1 109 ? 3.135  -6.309  16.636  1   40.707  ? 121 LYS   A O    1 ? 2 
ATOM   3384 C CB   . LYS   B 1 109 ? 3.679  -8.988  14.499  1   41.839  ? 121 LYS   A CB   1 ? 2 
ATOM   3385 H H    . LYS   B 1 109 ? 4.41   -7.401  12.702  1   43.991  ? 121 LYS   A H    1 c 2 
ATOM   3386 H HA   . LYS   B 1 109 ? 2.397  -7.406  14.506  1   44.944  ? 121 LYS   A HA   1 c 2 
ATOM   3387 H HB2  . LYS   B 1 109 ? 4.788  -8.995  14.636  0   30      ? 121 LYS   A HB2  1 c 2 
ATOM   3388 H HB3  . LYS   B 1 109 ? 2.993  -9.475  14.676  0   30      ? 121 LYS   A HB3  1 c 2 
ATOM   3389 N N    . ILE   B 1 110 ? 5.131  -6.143  15.717  1   40.922  ? 122 ILE   A N    1 ? 2 
ATOM   3390 C CA   . ILE   B 1 110 ? 5.708  -5.555  16.92   1   36.412  ? 122 ILE   A CA   1 ? 2 
ATOM   3391 C C    . ILE   B 1 110 ? 6.248  -4.165  16.553  1   36.87   ? 122 ILE   A C    1 ? 2 
ATOM   3392 O O    . ILE   B 1 110 ? 7.089  -4.034  15.64   1   38.737  ? 122 ILE   A O    1 ? 2 
ATOM   3393 C CB   . ILE   B 1 110 ? 6.893  -6.409  17.413  1   36.381  ? 122 ILE   A CB   1 ? 2 
ATOM   3394 C CG1  . ILE   B 1 110 ? 6.634  -7.944  17.511  1   39.481  ? 122 ILE   A CG1  1 ? 2 
ATOM   3395 C CG2  . ILE   B 1 110 ? 7.448  -5.823  18.676  1   35.261  ? 122 ILE   A CG2  1 ? 2 
ATOM   3396 C CD1  . ILE   B 1 110 ? 5.469  -8.409  18.391  1   35.009  ? 122 ILE   A CD1  1 ? 2 
ATOM   3397 H H    . ILE   B 1 110 ? 5.653  -6.225  14.973  1   41.237  ? 122 ILE   A H    1 c 2 
ATOM   3398 H HA   . ILE   B 1 110 ? 5.035  -5.486  17.621  1   37.279  ? 122 ILE   A HA   1 c 2 
ATOM   3399 H HB   . ILE   B 1 110 ? 7.594  -6.305  16.739  1   36.764  ? 122 ILE   A HB   1 c 2 
ATOM   3400 H HG12 . ILE   B 1 110 ? 6.482  -8.283  16.605  1   38.429  ? 122 ILE   A HG12 1 c 2 
ATOM   3401 H HG13 . ILE   B 1 110 ? 7.451  -8.368  17.843  1   37.095  ? 122 ILE   A HG13 1 c 2 
ATOM   3402 H HG21 . ILE   B 1 110 ? 8.085  -6.442  19.069  1   34.821  ? 122 ILE   A HG21 1 c 2 
ATOM   3403 H HG22 . ILE   B 1 110 ? 6.725  -5.663  19.306  1   35.403  ? 122 ILE   A HG22 1 c 2 
ATOM   3404 H HG23 . ILE   B 1 110 ? 7.896  -4.984  18.48   1   35.331  ? 122 ILE   A HG23 1 c 2 
ATOM   3405 H HD11 . ILE   B 1 110 ? 5.675  -8.229  19.328  1   35.646  ? 122 ILE   A HD11 1 c 2 
ATOM   3406 H HD12 . ILE   B 1 110 ? 5.332  -9.367  18.268  1   36.649  ? 122 ILE   A HD12 1 c 2 
ATOM   3407 H HD13 . ILE   B 1 110 ? 4.656  -7.931  18.142  1   36.986  ? 122 ILE   A HD13 1 c 2 
ATOM   3408 N N    . PRO   B 1 111 ? 5.831  -3.105  17.236  1   35.008  ? 123 PRO   A N    1 ? 2 
ATOM   3409 C CA   . PRO   B 1 111 ? 6.327  -1.774  16.918  1   38.034  ? 123 PRO   A CA   1 ? 2 
ATOM   3410 C C    . PRO   B 1 111 ? 7.698  -1.567  17.541  1   34.928  ? 123 PRO   A C    1 ? 2 
ATOM   3411 O O    . PRO   B 1 111 ? 8.124  -2.335  18.355  1   36.238  ? 123 PRO   A O    1 ? 2 
ATOM   3412 C CB   . PRO   B 1 111 ? 5.235  -0.801  17.427  1   35.604  ? 123 PRO   A CB   1 ? 2 
ATOM   3413 C CG   . PRO   B 1 111 ? 4.507  -1.623  18.49   1   32.545  ? 123 PRO   A CG   1 ? 2 
ATOM   3414 C CD   . PRO   B 1 111 ? 4.747  -3.09   18.253  1   36.184  ? 123 PRO   A CD   1 ? 2 
ATOM   3415 H HA   . PRO   B 1 111 ? 6.4    -1.681  15.945  1   37.123  ? 123 PRO   A HA   1 c 2 
ATOM   3416 H HB2  . PRO   B 1 111 ? 5.633  0.002   17.816  1   35.7    ? 123 PRO   A HB2  1 c 2 
ATOM   3417 H HB3  . PRO   B 1 111 ? 4.629  -0.545  16.705  1   36.732  ? 123 PRO   A HB3  1 c 2 
ATOM   3418 H HG2  . PRO   B 1 111 ? 4.829  -1.376  19.38   1   33.613  ? 123 PRO   A HG2  1 c 2 
ATOM   3419 H HG3  . PRO   B 1 111 ? 3.548  -1.436  18.455  1   35.057  ? 123 PRO   A HG3  1 c 2 
ATOM   3420 H HD2  . PRO   B 1 111 ? 5.033  -3.54   19.071  1   34.136  ? 123 PRO   A HD2  1 c 2 
ATOM   3421 H HD3  . PRO   B 1 111 ? 3.943  -3.527  17.908  1   35.619  ? 123 PRO   A HD3  1 c 2 
ATOM   3422 N N    . SER   B 1 112 ? 8.322  -0.456  17.199  1   31.18   ? 124 SER   A N    1 ? 2 
ATOM   3423 C CA   . SER   B 1 112 ? 9.588  -0.041  17.771  1   29.747  ? 124 SER   A CA   1 ? 2 
ATOM   3424 C C    . SER   B 1 112 ? 9.432  0.031   19.293  1   32.446  ? 124 SER   A C    1 ? 2 
ATOM   3425 O O    . SER   B 1 112 ? 8.501  0.623   19.769  1   31.297  ? 124 SER   A O    1 ? 2 
ATOM   3426 C CB   . SER   B 1 112 ? 9.941  1.321   17.193  1   32.988  ? 124 SER   A CB   1 ? 2 
ATOM   3427 O OG   . SER   B 1 112 ? 11.141 1.826   17.76   1   32.634  ? 124 SER   A OG   1 ? 2 
ATOM   3428 H H    . SER   B 1 112 ? 7.937  0.081   16.567  1   32.74   ? 124 SER   A H    1 c 2 
ATOM   3429 H HA   . SER   B 1 112 ? 10.29  -0.7    17.535  1   30.419  ? 124 SER   A HA   1 c 2 
ATOM   3430 H HB2  . SER   B 1 112 ? 10.047 1.243   16.225  1   32.819  ? 124 SER   A HB2  1 c 2 
ATOM   3431 H HB3  . SER   B 1 112 ? 9.211  1.945   17.37   1   33.066  ? 124 SER   A HB3  1 c 2 
ATOM   3432 H HG   . SER   B 1 112 ? 11.337 2.548   17.382  0   30      ? 124 SER   A HG   1 c 2 
ATOM   3433 N N    . ASN   B 1 113 ? 10.415 -0.45   20.02   1   29.548  ? 125 ASN   A N    1 ? 2 
ATOM   3434 C CA   . ASN   B 1 113 ? 10.546 -0.186  21.467  1   33.723  ? 125 ASN   A CA   1 ? 2 
ATOM   3435 C C    . ASN   B 1 113 ? 9.374  -0.763  22.262  1   33.535  ? 125 ASN   A C    1 ? 2 
ATOM   3436 O O    . ASN   B 1 113 ? 8.991  -0.19   23.259  1   38.345  ? 125 ASN   A O    1 ? 2 
ATOM   3437 C CB   . ASN   B 1 113 ? 10.708 1.276   21.806  1   34.709  ? 125 ASN   A CB   1 ? 2 
ATOM   3438 C CG   . ASN   B 1 113 ? 12.086 1.717   21.434  1   35.762  ? 125 ASN   A CG   1 ? 2 
ATOM   3439 O OD1  . ASN   B 1 113 ? 12.988 0.891   21.432  1   41.017  ? 125 ASN   A OD1  1 ? 2 
ATOM   3440 N ND2  . ASN   B 1 113 ? 12.244 2.946   20.985  1   41.216  ? 125 ASN   A ND2  1 ? 2 
ATOM   3441 H H    . ASN   B 1 113 ? 11.046 -0.974  19.616  1   30.607  ? 125 ASN   A H    1 c 2 
ATOM   3442 H HA   . ASN   B 1 113 ? 11.357 -0.644  21.773  1   32.612  ? 125 ASN   A HA   1 c 2 
ATOM   3443 H HB2  . ASN   B 1 113 ? 10.049 1.808   21.32   1   35.415  ? 125 ASN   A HB2  1 c 2 
ATOM   3444 H HB3  . ASN   B 1 113 ? 10.573 1.413   22.765  1   35.227  ? 125 ASN   A HB3  1 c 2 
ATOM   3445 H HD21 . ASN   B 1 113 ? 13.012 3.183   20.608  1   40.153  ? 125 ASN   A HD21 1 c 2 
ATOM   3446 H HD22 . ASN   B 1 113 ? 11.586 3.536   21.059  1   40.321  ? 125 ASN   A HD22 1 c 2 
ATOM   3447 N N    . ALA   B 1 114 ? 8.834  -1.907  21.835  1   33.232  ? 126 ALA   A N    1 ? 2 
ATOM   3448 C CA   . ALA   B 1 114 ? 7.672  -2.495  22.526  1   34.231  ? 126 ALA   A CA   1 ? 2 
ATOM   3449 C C    . ALA   B 1 114 ? 8.124  -3.241  23.761  1   34.023  ? 126 ALA   A C    1 ? 2 
ATOM   3450 O O    . ALA   B 1 114 ? 9.068  -4.032  23.675  1   32.752  ? 126 ALA   A O    1 ? 2 
ATOM   3451 C CB   . ALA   B 1 114 ? 6.954  -3.425  21.575  1   35.376  ? 126 ALA   A CB   1 ? 2 
ATOM   3452 H H    . ALA   B 1 114 ? 9.188  -2.339  21.112  1   33.035  ? 126 ALA   A H    1 c 2 
ATOM   3453 H HA   . ALA   B 1 114 ? 7.057  -1.76   22.798  1   35.022  ? 126 ALA   A HA   1 c 2 
ATOM   3454 H HB1  . ALA   B 1 114 ? 6.65   -2.927  20.798  1   35.446  ? 126 ALA   A HB1  1 c 2 
ATOM   3455 H HB2  . ALA   B 1 114 ? 7.559  -4.13   21.288  1   34.487  ? 126 ALA   A HB2  1 c 2 
ATOM   3456 H HB3  . ALA   B 1 114 ? 6.188  -3.822  22.023  1   35.205  ? 126 ALA   A HB3  1 c 2 
ATOM   3457 N N    . THR   B 1 115 ? 7.345  -3.052  24.824  1   35.227  ? 127 THR   A N    1 ? 2 
ATOM   3458 C CA   . THR   B 1 115 ? 7.308  -3.892  25.993  1   33.612  ? 127 THR   A CA   1 ? 2 
ATOM   3459 C C    . THR   B 1 115 ? 6.319  -5.038  25.811  1   35.999  ? 127 THR   A C    1 ? 2 
ATOM   3460 O O    . THR   B 1 115 ? 5.143  -4.853  25.434  1   37.928  ? 127 THR   A O    1 ? 2 
ATOM   3461 C CB   . THR   B 1 115 ? 6.984  -3.041  27.215  1   34.858  ? 127 THR   A CB   1 ? 2 
ATOM   3462 O OG1  . THR   B 1 115 ? 8.113  -2.181  27.369  1   34.604  ? 127 THR   A OG1  1 ? 2 
ATOM   3463 C CG2  . THR   B 1 115 ? 7.05   -3.834  28.501  1   38.446  ? 127 THR   A CG2  1 ? 2 
ATOM   3464 H H    . THR   B 1 115 ? 6.787  -2.328  24.812  1   35.326  ? 127 THR   A H    1 c 2 
ATOM   3465 H HA   . THR   B 1 115 ? 8.204  -4.271  26.118  1   34.041  ? 127 THR   A HA   1 c 2 
ATOM   3466 H HB   . THR   B 1 115 ? 6.151  -2.521  27.118  1   35.924  ? 127 THR   A HB   1 c 2 
ATOM   3467 H HG1  . THR   B 1 115 ? 8.868  -2.575  27.491  0   30      ? 127 THR   A HG1  1 c 2 
ATOM   3468 H HG21 . THR   B 1 115 ? 6.956  -3.232  29.258  1   38.424  ? 127 THR   A HG21 1 c 2 
ATOM   3469 H HG22 . THR   B 1 115 ? 7.905  -4.292  28.557  1   36.998  ? 127 THR   A HG22 1 c 2 
ATOM   3470 H HG23 . THR   B 1 115 ? 6.331  -4.488  28.518  1   37.433  ? 127 THR   A HG23 1 c 2 
ATOM   3471 N N    . LEU   B 1 116 ? 6.814  -6.247  26.12   1   36.76   ? 128 LEU   A N    1 ? 2 
ATOM   3472 C CA   . LEU   B 1 116 ? 6.032  -7.471  25.977  1   37.312  ? 128 LEU   A CA   1 ? 2 
ATOM   3473 C C    . LEU   B 1 116 ? 5.817  -8.162  27.34   1   36.782  ? 128 LEU   A C    1 ? 2 
ATOM   3474 O O    . LEU   B 1 116 ? 6.651  -8.011  28.21   1   33.799  ? 128 LEU   A O    1 ? 2 
ATOM   3475 C CB   . LEU   B 1 116 ? 6.676  -8.509  25.076  1   39.674  ? 128 LEU   A CB   1 ? 2 
ATOM   3476 C CG   . LEU   B 1 116 ? 7.164  -8.066  23.686  1   45.083  ? 128 LEU   A CG   1 ? 2 
ATOM   3477 C CD1  . LEU   B 1 116 ? 7.077  -9.377  22.851  1   44.601  ? 128 LEU   A CD1  1 ? 2 
ATOM   3478 C CD2  . LEU   B 1 116 ? 6.399  -7.039  23.066  1   39.984  ? 128 LEU   A CD2  1 ? 2 
ATOM   3479 H H    . LEU   B 1 116 ? 7.671  -6.312  26.432  1   36.337  ? 128 LEU   A H    1 c 2 
ATOM   3480 H HA   . LEU   B 1 116 ? 5.145  -7.231  25.606  1   37.925  ? 128 LEU   A HA   1 c 2 
ATOM   3481 H HB2  . LEU   B 1 116 ? 7.445  -8.892  25.559  1   39.998  ? 128 LEU   A HB2  1 c 2 
ATOM   3482 H HB3  . LEU   B 1 116 ? 6.031  -9.243  24.958  1   40.497  ? 128 LEU   A HB3  1 c 2 
ATOM   3483 H HG   . LEU   B 1 116 ? 8.111  -7.78   23.75   1   42.425  ? 128 LEU   A HG   1 c 2 
ATOM   3484 H HD11 . LEU   B 1 116 ? 7.601  -10.073 23.283  1   44.643  ? 128 LEU   A HD11 1 c 2 
ATOM   3485 H HD12 . LEU   B 1 116 ? 7.427  -9.216  21.959  1   44.532  ? 128 LEU   A HD12 1 c 2 
ATOM   3486 H HD13 . LEU   B 1 116 ? 6.15   -9.663  22.787  1   45.162  ? 128 LEU   A HD13 1 c 2 
ATOM   3487 H HD21 . LEU   B 1 116 ? 6.652  -6.178  23.434  1   41.479  ? 128 LEU   A HD21 1 c 2 
ATOM   3488 H HD22 . LEU   B 1 116 ? 5.453  -7.196  23.227  1   42.006  ? 128 LEU   A HD22 1 c 2 
ATOM   3489 H HD23 . LEU   B 1 116 ? 6.567  -7.041  22.108  1   41.515  ? 128 LEU   A HD23 1 c 2 
ATOM   3490 N N    . PHE   B 1 117 ? 4.711  -8.921  27.397  1   39.133  ? 129 PHE   A N    1 ? 2 
ATOM   3491 C CA   . PHE   B 1 117 ? 4.271  -9.667  28.562  1   43.158  ? 129 PHE   A CA   1 ? 2 
ATOM   3492 C C    . PHE   B 1 117 ? 3.91   -11.073 28.079  1   36.445  ? 129 PHE   A C    1 ? 2 
ATOM   3493 O O    . PHE   B 1 117 ? 3.19   -11.249 27.081  1   37.139  ? 129 PHE   A O    1 ? 2 
ATOM   3494 C CB   . PHE   B 1 117 ? 3.01   -9.095  29.217  1   46.219  ? 129 PHE   A CB   1 ? 2 
ATOM   3495 C CG   . PHE   B 1 117 ? 2.493  -9.952  30.382  1   44.899  ? 129 PHE   A CG   1 ? 2 
ATOM   3496 C CD1  . PHE   B 1 117 ? 2.98   -9.743  31.671  1   47.881  ? 129 PHE   A CD1  1 ? 2 
ATOM   3497 C CD2  . PHE   B 1 117 ? 1.485  -10.897 30.186  1   49.19   ? 129 PHE   A CD2  1 ? 2 
ATOM   3498 C CE1  . PHE   B 1 117 ? 2.554  -10.546 32.751  1   55.398  ? 129 PHE   A CE1  1 ? 2 
ATOM   3499 C CE2  . PHE   B 1 117 ? 1.037  -11.68  31.229  1   58.294  ? 129 PHE   A CE2  1 ? 2 
ATOM   3500 C CZ   . PHE   B 1 117 ? 1.599  -11.538 32.514  1   61.65   ? 129 PHE   A CZ   1 ? 2 
ATOM   3501 H H    . PHE   B 1 117 ? 4.194  -8.971  26.645  1   39.363  ? 129 PHE   A H    1 c 2 
ATOM   3502 H HA   . PHE   B 1 117 ? 5.005  -9.714  29.227  1   41.338  ? 129 PHE   A HA   1 c 2 
ATOM   3503 H HB2  . PHE   B 1 117 ? 3.21   -8.192  29.548  1   45.364  ? 129 PHE   A HB2  1 c 2 
ATOM   3504 H HB3  . PHE   B 1 117 ? 2.306  -9.023  28.535  1   45.374  ? 129 PHE   A HB3  1 c 2 
ATOM   3505 H HD1  . PHE   B 1 117 ? 3.668  -9.112  31.806  1   48.403  ? 129 PHE   A HD1  1 c 2 
ATOM   3506 H HD2  . PHE   B 1 117 ? 1.146  -11.039 29.316  1   49.844  ? 129 PHE   A HD2  1 c 2 
ATOM   3507 H HE1  . PHE   B 1 117 ? 2.914  -10.42  33.614  1   55.672  ? 129 PHE   A HE1  1 c 2 
ATOM   3508 H HE2  . PHE   B 1 117 ? 0.385  -12.339 31.07   1   57.432  ? 129 PHE   A HE2  1 c 2 
ATOM   3509 H HZ   . PHE   B 1 117 ? 1.257  -12.044 33.235  1   60.512  ? 129 PHE   A HZ   1 c 2 
ATOM   3510 N N    . PHE   B 1 118 ? 4.443  -12.072 28.754  1   39.026  ? 130 PHE   A N    1 ? 2 
ATOM   3511 C CA   . PHE   B 1 118 ? 3.988  -13.446 28.593  1   40.502  ? 130 PHE   A CA   1 ? 2 
ATOM   3512 C C    . PHE   B 1 118 ? 3.668  -14.158 29.922  1   36.792  ? 130 PHE   A C    1 ? 2 
ATOM   3513 O O    . PHE   B 1 118 ? 4.401  -13.996 30.863  1   38.961  ? 130 PHE   A O    1 ? 2 
ATOM   3514 C CB   . PHE   B 1 118 ? 5.091  -14.289 27.94   1   36.884  ? 130 PHE   A CB   1 ? 2 
ATOM   3515 C CG   . PHE   B 1 118 ? 5.5    -13.903 26.522  1   35.751  ? 130 PHE   A CG   1 ? 2 
ATOM   3516 C CD1  . PHE   B 1 118 ? 6.436  -12.893 26.302  1   39.446  ? 130 PHE   A CD1  1 ? 2 
ATOM   3517 C CD2  . PHE   B 1 118 ? 4.919  -14.541 25.437  1   39.097  ? 130 PHE   A CD2  1 ? 2 
ATOM   3518 C CE1  . PHE   B 1 118 ? 6.813  -12.509 25.042  1   36.558  ? 130 PHE   A CE1  1 ? 2 
ATOM   3519 C CE2  . PHE   B 1 118 ? 5.316  -14.172 24.147  1   40.45   ? 130 PHE   A CE2  1 ? 2 
ATOM   3520 C CZ   . PHE   B 1 118 ? 6.279  -13.162 23.966  1   34.414  ? 130 PHE   A CZ   1 ? 2 
ATOM   3521 H H    . PHE   B 1 118 ? 5.121  -11.902 29.343  1   38.598  ? 130 PHE   A H    1 c 2 
ATOM   3522 H HA   . PHE   B 1 118 ? 3.184  -13.457 28.013  1   39.069  ? 130 PHE   A HA   1 c 2 
ATOM   3523 H HB2  . PHE   B 1 118 ? 5.887  -14.246 28.515  1   37.349  ? 130 PHE   A HB2  1 c 2 
ATOM   3524 H HB3  . PHE   B 1 118 ? 4.794  -15.226 27.932  1   38.197  ? 130 PHE   A HB3  1 c 2 
ATOM   3525 H HD1  . PHE   B 1 118 ? 6.816  -12.456 27.047  1   37.657  ? 130 PHE   A HD1  1 c 2 
ATOM   3526 H HD2  . PHE   B 1 118 ? 4.289  -15.232 25.568  1   39.637  ? 130 PHE   A HD2  1 c 2 
ATOM   3527 H HE1  . PHE   B 1 118 ? 7.461  -11.834 24.921  1   35.92   ? 130 PHE   A HE1  1 c 2 
ATOM   3528 H HE2  . PHE   B 1 118 ? 4.94   -14.605 23.397  1   39.308  ? 130 PHE   A HE2  1 c 2 
ATOM   3529 H HZ   . PHE   B 1 118 ? 6.527  -12.904 23.093  1   35.92   ? 130 PHE   A HZ   1 c 2 
ATOM   3530 N N    . GLU   B 1 119 ? 2.624  -15.002 29.873  1   39.541  ? 131 GLU   A N    1 ? 2 
ATOM   3531 C CA   . GLU   B 1 119 ? 2.476  -16.186 30.694  1   40.572  ? 131 GLU   A CA   1 ? 2 
ATOM   3532 C C    . GLU   B 1 119 ? 2.931  -17.426 29.914  1   50.197  ? 131 GLU   A C    1 ? 2 
ATOM   3533 O O    . GLU   B 1 119 ? 2.421  -17.763 28.829  1   49.125  ? 131 GLU   A O    1 ? 2 
ATOM   3534 C CB   . GLU   B 1 119 ? 1.027  -16.264 31.143  1   43.272  ? 131 GLU   A CB   1 ? 2 
ATOM   3535 C CG   . GLU   B 1 119 ? 0.682  -17.458 32.049  1   51.92   ? 131 GLU   A CG   1 ? 2 
ATOM   3536 C CD   . GLU   B 1 119 ? -0.649 -17.362 32.757  1   59.753  ? 131 GLU   A CD   1 ? 2 
ATOM   3537 O OE1  . GLU   B 1 119 ? -0.722 -16.866 33.907  1   60.125  ? 131 GLU   A OE1  1 ? 2 
ATOM   3538 O OE2  . GLU   B 1 119 ? -1.627 -17.872 32.163  1   70.08   ? 131 GLU   A OE2  1 ? 2 
ATOM   3539 H H    . GLU   B 1 119 ? 1.956  -14.815 29.277  1   39.274  ? 131 GLU   A H    1 c 2 
ATOM   3540 H HA   . GLU   B 1 119 ? 3.048  -16.083 31.495  1   42.464  ? 131 GLU   A HA   1 c 2 
ATOM   3541 H HB2  . GLU   B 1 119 ? 0.807  -15.44  31.624  1   44.489  ? 131 GLU   A HB2  1 c 2 
ATOM   3542 H HB3  . GLU   B 1 119 ? 0.456  -16.305 30.348  1   44.472  ? 131 GLU   A HB3  1 c 2 
ATOM   3543 H HG2  . GLU   B 1 119 ? 0.688  -18.276 31.512  1   51.863  ? 131 GLU   A HG2  1 c 2 
ATOM   3544 H HG3  . GLU   B 1 119 ? 1.385  -17.551 32.728  1   51.42   ? 131 GLU   A HG3  1 c 2 
ATOM   3545 N N    . ILE   B 1 120 ? 3.888  -18.139 30.52   1   48.158  ? 132 ILE   A N    1 ? 2 
ATOM   3546 C CA   . ILE   B 1 120 ? 4.441  -19.339 29.941  1   48.043  ? 132 ILE   A CA   1 ? 2 
ATOM   3547 C C    . ILE   B 1 120 ? 4.263  -20.502 30.904  1   47.385  ? 132 ILE   A C    1 ? 2 
ATOM   3548 O O    . ILE   B 1 120 ? 4.623  -20.362 32.064  1   44.525  ? 132 ILE   A O    1 ? 2 
ATOM   3549 C CB   . ILE   B 1 120 ? 5.937  -19.123 29.692  1   48.668  ? 132 ILE   A CB   1 ? 2 
ATOM   3550 C CG1  . ILE   B 1 120 ? 6.195  -17.9   28.828  1   48.426  ? 132 ILE   A CG1  1 ? 2 
ATOM   3551 C CG2  . ILE   B 1 120 ? 6.532  -20.397 29.113  1   50.483  ? 132 ILE   A CG2  1 ? 2 
ATOM   3552 C CD1  . ILE   B 1 120 ? 7.661  -17.598 28.6    1   47.228  ? 132 ILE   A CD1  1 ? 2 
ATOM   3553 H H    . ILE   B 1 120 ? 4.206  -17.862 31.331  1   48.576  ? 132 ILE   A H    1 c 2 
ATOM   3554 H HA   . ILE   B 1 120 ? 3.995  -19.535 29.095  1   47.961  ? 132 ILE   A HA   1 c 2 
ATOM   3555 H HB   . ILE   B 1 120 ? 6.36   -18.964 30.559  1   48.944  ? 132 ILE   A HB   1 c 2 
ATOM   3556 H HG12 . ILE   B 1 120 ? 5.763  -18.033 27.96   1   47.912  ? 132 ILE   A HG12 1 c 2 
ATOM   3557 H HG13 . ILE   B 1 120 ? 5.779  -17.122 29.252  1   47.672  ? 132 ILE   A HG13 1 c 2 
ATOM   3558 H HG21 . ILE   B 1 120 ? 7.474  -20.261 28.92   1   49.765  ? 132 ILE   A HG21 1 c 2 
ATOM   3559 H HG22 . ILE   B 1 120 ? 6.066  -20.631 28.293  1   50.301  ? 132 ILE   A HG22 1 c 2 
ATOM   3560 H HG23 . ILE   B 1 120 ? 6.44   -21.122 29.753  1   51.374  ? 132 ILE   A HG23 1 c 2 
ATOM   3561 H HD11 . ILE   B 1 120 ? 8.125  -17.563 29.458  1   47.716  ? 132 ILE   A HD11 1 c 2 
ATOM   3562 H HD12 . ILE   B 1 120 ? 7.747  -16.736 28.15   1   46.408  ? 132 ILE   A HD12 1 c 2 
ATOM   3563 H HD13 . ILE   B 1 120 ? 8.061  -18.293 28.044  1   47.711  ? 132 ILE   A HD13 1 c 2 
ATOM   3564 N N    . GLU   B 1 121 ? 3.789  -21.636 30.356  1   49.765  ? 133 GLU   A N    1 ? 2 
ATOM   3565 C CA   . GLU   B 1 121 ? 3.823  -22.911 31.055  1   50.46   ? 133 GLU   A CA   1 ? 2 
ATOM   3566 C C    . GLU   B 1 121 ? 4.871  -23.798 30.408  1   52.775  ? 133 GLU   A C    1 ? 2 
ATOM   3567 O O    . GLU   B 1 121 ? 4.733  -24.141 29.21   1   50.393  ? 133 GLU   A O    1 ? 2 
ATOM   3568 C CB   . GLU   B 1 121 ? 2.419  -23.518 31.053  1   54.226  ? 133 GLU   A CB   1 ? 2 
ATOM   3569 C CG   . GLU   B 1 121 ? 2.28   -24.83  31.836  1   59.237  ? 133 GLU   A CG   1 ? 2 
ATOM   3570 C CD   . GLU   B 1 121 ? 0.89   -25.422 31.781  1   61.833  ? 133 GLU   A CD   1 ? 2 
ATOM   3571 O OE1  . GLU   B 1 121 ? -0.094 -24.881 31.289  1   75.411  ? 133 GLU   A OE1  1 ? 2 
ATOM   3572 O OE2  . GLU   B 1 121 ? 0.768  -26.51  32.215  1   58.265  ? 133 GLU   A OE2  1 ? 2 
ATOM   3573 H H    . GLU   B 1 121 ? 3.43   -21.609 29.516  1   49.01   ? 133 GLU   A H    1 c 2 
ATOM   3574 H HA   . GLU   B 1 121 ? 4.083  -22.744 31.993  1   51.59   ? 133 GLU   A HA   1 c 2 
ATOM   3575 H HB2  . GLU   B 1 121 ? 1.794  -22.863 31.425  1   54.128  ? 133 GLU   A HB2  1 c 2 
ATOM   3576 H HB3  . GLU   B 1 121 ? 2.154  -23.686 30.124  1   54.281  ? 133 GLU   A HB3  1 c 2 
ATOM   3577 H HG2  . GLU   B 1 121 ? 2.914  -25.487 31.48   1   59.145  ? 133 GLU   A HG2  1 c 2 
ATOM   3578 H HG3  . GLU   B 1 121 ? 2.513  -24.668 32.775  1   59.005  ? 133 GLU   A HG3  1 c 2 
ATOM   3579 N N    . LEU   B 1 122 ? 5.88   -24.182 31.201  1   52.646  ? 134 LEU   A N    1 ? 2 
ATOM   3580 C CA   . LEU   B 1 122 ? 6.848  -25.167 30.74   1   54.562  ? 134 LEU   A CA   1 ? 2 
ATOM   3581 C C    . LEU   B 1 122 ? 6.326  -26.585 30.867  1   59.656  ? 134 LEU   A C    1 ? 2 
ATOM   3582 O O    . LEU   B 1 122 ? 6.152  -27.104 31.952  1   65.31   ? 134 LEU   A O    1 ? 2 
ATOM   3583 C CB   . LEU   B 1 122 ? 8.148  -24.952 31.496  1   51.479  ? 134 LEU   A CB   1 ? 2 
ATOM   3584 C CG   . LEU   B 1 122 ? 9.263  -25.92  31.127  1   55.603  ? 134 LEU   A CG   1 ? 2 
ATOM   3585 C CD1  . LEU   B 1 122 ? 9.567  -25.867 29.64   1   51.487  ? 134 LEU   A CD1  1 ? 2 
ATOM   3586 C CD2  . LEU   B 1 122 ? 10.51  -25.617 31.982  1   54.185  ? 134 LEU   A CD2  1 ? 2 
ATOM   3587 H H    . LEU   B 1 122 ? 5.967  -23.827 32.039  1   52.986  ? 134 LEU   A H    1 c 2 
ATOM   3588 H HA   . LEU   B 1 122 ? 7.015  -24.992 29.78   1   53.482  ? 134 LEU   A HA   1 c 2 
ATOM   3589 H HB2  . LEU   B 1 122 ? 8.459  -24.034 31.322  1   51.23   ? 134 LEU   A HB2  1 c 2 
ATOM   3590 H HB3  . LEU   B 1 122 ? 7.964  -25.039 32.46   1   53.584  ? 134 LEU   A HB3  1 c 2 
ATOM   3591 H HG   . LEU   B 1 122 ? 8.962  -26.839 31.346  1   55.847  ? 134 LEU   A HG   1 c 2 
ATOM   3592 H HD11 . LEU   B 1 122 ? 8.844  -26.286 29.144  1   52.913  ? 134 LEU   A HD11 1 c 2 
ATOM   3593 H HD12 . LEU   B 1 122 ? 10.396 -26.341 29.462  1   53.408  ? 134 LEU   A HD12 1 c 2 
ATOM   3594 H HD13 . LEU   B 1 122 ? 9.658  -24.941 29.359  1   50.762  ? 134 LEU   A HD13 1 c 2 
ATOM   3595 H HD21 . LEU   B 1 122 ? 10.268 -25.622 32.923  1   55.346  ? 134 LEU   A HD21 1 c 2 
ATOM   3596 H HD22 . LEU   B 1 122 ? 10.862 -24.743 31.744  1   53.167  ? 134 LEU   A HD22 1 c 2 
ATOM   3597 H HD23 . LEU   B 1 122 ? 11.188 -26.294 31.819  1   55.955  ? 134 LEU   A HD23 1 c 2 
ATOM   3598 N N    . LEU   B 1 123 ? 6.081  -27.249 29.74   1   64.777  ? 135 LEU   A N    1 ? 2 
ATOM   3599 C CA   . LEU   B 1 123 ? 5.41   -28.537 29.784  1   60.461  ? 135 LEU   A CA   1 ? 2 
ATOM   3600 C C    . LEU   B 1 123 ? 6.411  -29.669 29.953  1   63.21   ? 135 LEU   A C    1 ? 2 
ATOM   3601 O O    . LEU   B 1 123 ? 6.131  -30.661 30.614  1   60.84   ? 135 LEU   A O    1 ? 2 
ATOM   3602 C CB   . LEU   B 1 123 ? 4.649  -28.725 28.477  1   63.154  ? 135 LEU   A CB   1 ? 2 
ATOM   3603 C CG   . LEU   B 1 123 ? 3.593  -27.677 28.14   1   65.709  ? 135 LEU   A CG   1 ? 2 
ATOM   3604 C CD1  . LEU   B 1 123 ? 2.98   -27.883 26.749  1   73.797  ? 135 LEU   A CD1  1 ? 2 
ATOM   3605 C CD2  . LEU   B 1 123 ? 2.481  -27.658 29.156  1   62.716  ? 135 LEU   A CD2  1 ? 2 
ATOM   3606 H H    . LEU   B 1 123 ? 6.331  -26.9   28.933  1   60.979  ? 135 LEU   A H    1 c 2 
ATOM   3607 H HA   . LEU   B 1 123 ? 4.774  -28.547 30.544  1   62.849  ? 135 LEU   A HA   1 c 2 
ATOM   3608 H HB2  . LEU   B 1 123 ? 5.304  -28.752 27.743  1   63.093  ? 135 LEU   A HB2  1 c 2 
ATOM   3609 H HB3  . LEU   B 1 123 ? 4.21   -29.606 28.505  1   65.469  ? 135 LEU   A HB3  1 c 2 
ATOM   3610 H HG   . LEU   B 1 123 ? 4.029  -26.787 28.15   1   63.406  ? 135 LEU   A HG   1 c 2 
ATOM   3611 H HD11 . LEU   B 1 123 ? 3.685  -27.874 26.08   1   70.977  ? 135 LEU   A HD11 1 c 2 
ATOM   3612 H HD12 . LEU   B 1 123 ? 2.349  -27.167 26.562  1   70.51   ? 135 LEU   A HD12 1 c 2 
ATOM   3613 H HD13 . LEU   B 1 123 ? 2.518  -28.737 26.72   1   73.481  ? 135 LEU   A HD13 1 c 2 
ATOM   3614 H HD21 . LEU   B 1 123 ? 2.833  -27.383 30.019  1   63.31   ? 135 LEU   A HD21 1 c 2 
ATOM   3615 H HD22 . LEU   B 1 123 ? 2.096  -28.547 29.233  1   65.832  ? 135 LEU   A HD22 1 c 2 
ATOM   3616 H HD23 . LEU   B 1 123 ? 1.793  -27.032 28.873  1   63.22   ? 135 LEU   A HD23 1 c 2 
ATOM   3617 N N    . ASP   B 1 124 ? 7.547  -29.566 29.263  1   66.88   ? 136 ASP   A N    1 ? 2 
ATOM   3618 C CA   . ASP   B 1 124 ? 8.505  -30.661 29.144  1   68.539  ? 136 ASP   A CA   1 ? 2 
ATOM   3619 C C    . ASP   B 1 124 ? 9.732  -30.116 28.43   1   69.895  ? 136 ASP   A C    1 ? 2 
ATOM   3620 O O    . ASP   B 1 124 ? 9.615  -29.114 27.733  1   71.088  ? 136 ASP   A O    1 ? 2 
ATOM   3621 C CB   . ASP   B 1 124 ? 8.02   -31.836 28.295  1   69.767  ? 136 ASP   A CB   1 ? 2 
ATOM   3622 C CG   . ASP   B 1 124 ? 8.79   -33.129 28.543  1   73.737  ? 136 ASP   A CG   1 ? 2 
ATOM   3623 O OD1  . ASP   B 1 124 ? 9.584  -33.161 29.527  1   69.621  ? 136 ASP   A OD1  1 ? 2 
ATOM   3624 O OD2  . ASP   B 1 124 ? 8.54   -34.134 27.812  1   84.735  ? 136 ASP   A OD2  1 ? 2 
ATOM   3625 H H    . ASP   B 1 124 ? 7.736  -28.778 28.842  1   63.931  ? 136 ASP   A H    1 c 2 
ATOM   3626 H HA   . ASP   B 1 124 ? 8.757  -30.959 30.045  1   69.766  ? 136 ASP   A HA   1 c 2 
ATOM   3627 H HB2  . ASP   B 1 124 ? 7.074  -32.003 28.489  1   70.645  ? 136 ASP   A HB2  1 c 2 
ATOM   3628 H HB3  . ASP   B 1 124 ? 8.096  -31.607 27.345  1   69.635  ? 136 ASP   A HB3  1 c 2 
ATOM   3629 N N    . PHE   B 1 125 ? 10.893 -30.751 28.647  1   65.889  ? 137 PHE   A N    1 ? 2 
ATOM   3630 C CA   . PHE   B 1 125 ? 12.119 -30.424 27.943  1   64.188  ? 137 PHE   A CA   1 ? 2 
ATOM   3631 C C    . PHE   B 1 125 ? 12.914 -31.7   27.799  1   68.579  ? 137 PHE   A C    1 ? 2 
ATOM   3632 O O    . PHE   B 1 125 ? 12.878 -32.527 28.705  1   66.414  ? 137 PHE   A O    1 ? 2 
ATOM   3633 C CB   . PHE   B 1 125 ? 12.864 -29.279 28.656  1   63.826  ? 137 PHE   A CB   1 ? 2 
ATOM   3634 C CG   . PHE   B 1 125 ? 13.245 -29.514 30.105  1   63.596  ? 137 PHE   A CG   1 ? 2 
ATOM   3635 C CD1  . PHE   B 1 125 ? 12.384 -29.134 31.128  1   71.685  ? 137 PHE   A CD1  1 ? 2 
ATOM   3636 C CD2  . PHE   B 1 125 ? 14.491 -29.997 30.448  1   71.828  ? 137 PHE   A CD2  1 ? 2 
ATOM   3637 C CE1  . PHE   B 1 125 ? 12.766 -29.263 32.454  1   74.434  ? 137 PHE   A CE1  1 ? 2 
ATOM   3638 C CE2  . PHE   B 1 125 ? 14.849 -30.202 31.78   1   76.715  ? 137 PHE   A CE2  1 ? 2 
ATOM   3639 C CZ   . PHE   B 1 125 ? 13.986 -29.841 32.782  1   79.013  ? 137 PHE   A CZ   1 ? 2 
ATOM   3640 H H    . PHE   B 1 125 ? 10.918 -31.415 29.274  1   68.577  ? 137 PHE   A H    1 c 2 
ATOM   3641 H HA   . PHE   B 1 125 ? 11.872 -30.11  27.035  1   64.095  ? 137 PHE   A HA   1 c 2 
ATOM   3642 H HB2  . PHE   B 1 125 ? 13.682 -29.085 28.147  1   63.087  ? 137 PHE   A HB2  1 c 2 
ATOM   3643 H HB3  . PHE   B 1 125 ? 12.301 -28.475 28.611  1   61.098  ? 137 PHE   A HB3  1 c 2 
ATOM   3644 H HD1  . PHE   B 1 125 ? 11.548 -28.751 30.915  1   68.367  ? 137 PHE   A HD1  1 c 2 
ATOM   3645 H HD2  . PHE   B 1 125 ? 15.082 -30.269 29.764  1   71.868  ? 137 PHE   A HD2  1 c 2 
ATOM   3646 H HE1  . PHE   B 1 125 ? 12.156 -29.04  33.139  1   74.199  ? 137 PHE   A HE1  1 c 2 
ATOM   3647 H HE2  . PHE   B 1 125 ? 15.696 -30.562 31.99   1   78.26   ? 137 PHE   A HE2  1 c 2 
ATOM   3648 H HZ   . PHE   B 1 125 ? 14.235 -29.948 33.686  1   78.714  ? 137 PHE   A HZ   1 c 2 
ATOM   3649 N N    . LYS   B 1 126 ? 13.537 -31.893 26.63   1   68.843  ? 138 LYS   A N    1 ? 2 
ATOM   3650 C CA   . LYS   B 1 126 ? 14.235 -33.146 26.319  1   70.338  ? 138 LYS   A CA   1 ? 2 
ATOM   3651 C C    . LYS   B 1 126 ? 15.619 -32.709 25.842  1   73.125  ? 138 LYS   A C    1 ? 2 
ATOM   3652 O O    . LYS   B 1 126 ? 15.738 -31.771 25.053  1   68.467  ? 138 LYS   A O    1 ? 2 
ATOM   3653 C CB   . LYS   B 1 126 ? 13.434 -34.06  25.376  1   65.751  ? 138 LYS   A CB   1 ? 2 
ATOM   3654 H H    . LYS   B 1 126 ? 13.531 -31.228 26.003  1   66.875  ? 138 LYS   A H    1 c 2 
ATOM   3655 H HA   . LYS   B 1 126 ? 14.352 -33.645 27.166  1   71.298  ? 138 LYS   A HA   1 c 2 
ATOM   3656 H HB2  . LYS   B 1 126 ? 14.136 -34.455 24.739  0   30      ? 138 LYS   A HB2  1 c 2 
ATOM   3657 H HB3  . LYS   B 1 126 ? 12.515 -33.865 25.43   0   30      ? 138 LYS   A HB3  1 c 2 
ATOM   3658 N N    . GLY   B 1 127 ? 16.662 -33.312 26.427  1   80.973  ? 139 GLY   A N    1 ? 2 
ATOM   3659 C CA   . GLY   B 1 127 ? 18.024 -33.058 26.005  1   86.081  ? 139 GLY   A CA   1 ? 2 
ATOM   3660 C C    . GLY   B 1 127 ? 18.206 -33.522 24.564  1   89.767  ? 139 GLY   A C    1 ? 2 
ATOM   3661 O O    . GLY   B 1 127 ? 18.338 -34.715 24.366  1   100.082 ? 139 GLY   A O    1 ? 2 
ATOM   3662 H H    . GLY   B 1 127 ? 16.518 -33.895 27.116  1   81.765  ? 139 GLY   A H    1 c 2 
ATOM   3663 H HA2  . GLY   B 1 127 ? 18.216 -32.099 26.073  1   83.107  ? 139 GLY   A HA2  1 c 2 
ATOM   3664 H HA3  . GLY   B 1 127 ? 18.648 -33.543 26.595  1   87.524  ? 139 GLY   A HA3  1 c 2 
ATOM   3665 N N    . GLU   B 1 128 ? 18.202 -32.573 23.597  1   95.798  ? 140 GLU   A N    1 ? 2 
ATOM   3666 C CA   . GLU   B 1 128 ? 18.099 -32.866 22.169  1   95.521  ? 140 GLU   A CA   1 ? 2 
ATOM   3667 C C    . GLU   B 1 128 ? 19.088 -33.994 21.847  1   100.078 ? 140 GLU   A C    1 ? 2 
ATOM   3668 O O    . GLU   B 1 128 ? 20.252 -33.642 21.621  1   112.936 ? 140 GLU   A O    1 ? 2 
ATOM   3669 C CB   . GLU   B 1 128 ? 18.394 -31.695 21.218  1   85.77   ? 140 GLU   A CB   1 ? 2 
ATOM   3670 O OXT  . GLU   B 1 128 ? 18.675 -35.168 21.88   1   93.994  ? 140 GLU   A OXT  1 ? 2 
ATOM   3671 H H    . GLU   B 1 128 ? 18.271 -31.699 23.852  1   90.691  ? 140 GLU   A H    1 c 2 
ATOM   3672 H HA   . GLU   B 1 128 ? 17.181 -33.193 21.988  1   94.277  ? 140 GLU   A HA   1 c 2 
ATOM   3673 H HB2  . GLU   B 1 128 ? 18.699 -31.262 20.996  0   30      ? 140 GLU   A HB2  1 c 2 
ATOM   3674 H HB3  . GLU   B 1 128 ? 16.855 -31.438 21.116  0   30      ? 140 GLU   A HB3  1 c 2 
HETATM 3675 C C4   . A1IN8 C 2 .   ? 18.474 5.513   13.083  1   40.542  ? 201 A1IN8 B C4   1 ? 1 
HETATM 3676 C C14  . A1IN8 C 2 .   ? 17.769 1.045   11.606  1   36.258  ? 201 A1IN8 B C14  1 ? 1 
HETATM 3677 C C5   . A1IN8 C 2 .   ? 17.332 5.294   13.872  1   42.85   ? 201 A1IN8 B C5   1 ? 1 
HETATM 3678 C C6   . A1IN8 C 2 .   ? 17.469 4.965   15.227  1   42.213  ? 201 A1IN8 B C6   1 ? 1 
HETATM 3679 C C11  . A1IN8 C 2 .   ? 18.885 2.042   15.637  1   60.227  ? 201 A1IN8 B C11  1 ? 1 
HETATM 3680 C C7   . A1IN8 C 2 .   ? 15.114 4.687   15.837  1   48.583  ? 201 A1IN8 B C7   1 ? 1 
HETATM 3681 C C8   . A1IN8 C 2 .   ? 18.723 5.035   15.818  1   47.234  ? 201 A1IN8 B C8   1 ? 1 
HETATM 3682 C C9   . A1IN8 C 2 .   ? 19.439 3.625   17.647  1   60.282  ? 201 A1IN8 B C9   1 ? 1 
HETATM 3683 C C10  . A1IN8 C 2 .   ? 18.908 2.337   17.094  1   55.525  ? 201 A1IN8 B C10  1 ? 1 
HETATM 3684 C C12  . A1IN8 C 2 .   ? 17.583 1.367   15.268  1   58.018  ? 201 A1IN8 B C12  1 ? 1 
HETATM 3685 C C13  . A1IN8 C 2 .   ? 17.754 0.669   13.942  1   45.011  ? 201 A1IN8 B C13  1 ? 1 
HETATM 3686 N N1   . A1IN8 C 2 .   ? 18.676 3.288   10.815  1   34.76   ? 201 A1IN8 B N1   1 ? 1 
HETATM 3687 C C3   . A1IN8 C 2 .   ? 19.71  5.575   13.695  1   43.873  ? 201 A1IN8 B C3   1 ? 1 
HETATM 3688 C C1   . A1IN8 C 2 .   ? 22.183 5.316   14.954  1   54.814  ? 201 A1IN8 B C1   1 ? 1 
HETATM 3689 O O1   . A1IN8 C 2 .   ? 20.996 5.343   15.728  1   54.169  ? 201 A1IN8 B O1   1 ? 1 
HETATM 3690 C C2   . A1IN8 C 2 .   ? 19.827 5.365   15.057  1   47.059  ? 201 A1IN8 B C2   1 ? 1 
HETATM 3691 O O2   . A1IN8 C 2 .   ? 16.477 4.701   16.149  1   45.699  ? 201 A1IN8 B O2   1 ? 1 
HETATM 3692 O O3   . A1IN8 C 2 .   ? 18.781 4.792   17.182  1   52.244  ? 201 A1IN8 B O3   1 ? 1 
HETATM 3693 O O4   . A1IN8 C 2 .   ? 19.96  1.503   17.502  1   58.706  ? 201 A1IN8 B O4   1 ? 1 
HETATM 3694 O O5   . A1IN8 C 2 .   ? 19.843 1.113   15.104  1   53.62   ? 201 A1IN8 B O5   1 ? 1 
HETATM 3695 O O6   . A1IN8 C 2 .   ? 18.134 1.517   12.811  1   41.155  ? 201 A1IN8 B O6   1 ? 1 
HETATM 3696 O O7   . A1IN8 C 2 .   ? 17.237 -0.009  11.426  1   32.446  ? 201 A1IN8 B O7   1 ? 1 
HETATM 3697 C C15  . A1IN8 C 2 .   ? 18.029 2.022   10.475  1   31.003  ? 201 A1IN8 B C15  1 ? 1 
HETATM 3698 C C16  . A1IN8 C 2 .   ? 18.938 1.296   9.502   1   36.881  ? 201 A1IN8 B C16  1 ? 1 
HETATM 3699 C C17  . A1IN8 C 2 .   ? 20.34  1.095   10.031  1   41.197  ? 201 A1IN8 B C17  1 ? 1 
HETATM 3700 C C18  . A1IN8 C 2 .   ? 20.979 2.461   10.17   1   42.253  ? 201 A1IN8 B C18  1 ? 1 
HETATM 3701 C C19  . A1IN8 C 2 .   ? 20.175 3.301   11.111  1   40.057  ? 201 A1IN8 B C19  1 ? 1 
HETATM 3702 C C20  . A1IN8 C 2 .   ? 17.864 4.351   11.065  1   32.59   ? 201 A1IN8 B C20  1 ? 1 
HETATM 3703 O O8   . A1IN8 C 2 .   ? 16.64  4.157   10.947  1   33.558  ? 201 A1IN8 B O8   1 ? 1 
HETATM 3704 C C21  . A1IN8 C 2 .   ? 18.409 5.668   11.569  1   34.2    ? 201 A1IN8 B C21  1 ? 1 
HETATM 3705 C C22  . A1IN8 C 2 .   ? 17.539 6.885   11.172  1   35.992  ? 201 A1IN8 B C22  1 ? 1 
HETATM 3706 C C23  . A1IN8 C 2 .   ? 17.558 7.113   9.656   1   35.279  ? 201 A1IN8 B C23  1 ? 1 
HETATM 3707 C C24  . A1IN8 C 2 .   ? 16.648 8.273   9.361   1   41.279  ? 201 A1IN8 B C24  1 ? 1 
HETATM 3708 C C25  . A1IN8 C 2 .   ? 17.062 9.555   9.998   1   39.952  ? 201 A1IN8 B C25  1 ? 1 
HETATM 3709 C C26  . A1IN8 C 2 .   ? 17.065 9.353   11.458  1   42.767  ? 201 A1IN8 B C26  1 ? 1 
HETATM 3710 C C27  . A1IN8 C 2 .   ? 17.957 8.175   11.869  1   38.025  ? 201 A1IN8 B C27  1 ? 1 
HETATM 3711 H H5   . A1IN8 C 2 .   ? 16.495 5.18    13.448  1   40.248  ? 201 A1IN8 B H5   1 c 1 
HETATM 3712 H H13  . A1IN8 C 2 .   ? 18.966 2.88    15.119  1   56.468  ? 201 A1IN8 B H13  1 c 1 
HETATM 3713 H H7   . A1IN8 C 2 .   ? 14.597 4.576   16.652  1   49.193  ? 201 A1IN8 B H7   1 c 1 
HETATM 3714 H H8   . A1IN8 C 2 .   ? 14.93  3.949   15.233  1   45.052  ? 201 A1IN8 B H8   1 c 1 
HETATM 3715 H H6   . A1IN8 C 2 .   ? 14.871 5.524   15.41   1   46.983  ? 201 A1IN8 B H6   1 c 1 
HETATM 3716 H H10  . A1IN8 C 2 .   ? 20.393 3.694   17.427  1   58.259  ? 201 A1IN8 B H10  1 c 1 
HETATM 3717 H H9   . A1IN8 C 2 .   ? 19.37  3.598   18.626  1   60.794  ? 201 A1IN8 B H9   1 c 1 
HETATM 3718 H H11  . A1IN8 C 2 .   ? 18.071 2.084   17.573  1   58.347  ? 201 A1IN8 B H11  1 c 1 
HETATM 3719 H H15  . A1IN8 C 2 .   ? 16.867 2.037   15.203  1   55.501  ? 201 A1IN8 B H15  1 c 1 
HETATM 3720 H H16  . A1IN8 C 2 .   ? 17.344 0.71    15.953  1   56.701  ? 201 A1IN8 B H16  1 c 1 
HETATM 3721 H H17  . A1IN8 C 2 .   ? 16.911 0.22    13.727  1   45.4    ? 201 A1IN8 B H17  1 c 1 
HETATM 3722 H H18  . A1IN8 C 2 .   ? 18.42  -0.041  14.041  1   46.627  ? 201 A1IN8 B H18  1 c 1 
HETATM 3723 H H4   . A1IN8 C 2 .   ? 20.478 5.733   13.172  1   43.703  ? 201 A1IN8 B H4   1 c 1 
HETATM 3724 H H2   . A1IN8 C 2 .   ? 22.949 5.234   15.545  1   56.813  ? 201 A1IN8 B H2   1 c 1 
HETATM 3725 H H3   . A1IN8 C 2 .   ? 22.258 6.138   14.443  1   54.37   ? 201 A1IN8 B H3   1 c 1 
HETATM 3726 H H1   . A1IN8 C 2 .   ? 22.16  4.556   14.349  1   52.026  ? 201 A1IN8 B H1   1 c 1 
HETATM 3727 H H12  . A1IN8 C 2 .   ? 19.669 0.596   17.292  0   30      ? 201 A1IN8 B H12  1 c 1 
HETATM 3728 H H14  . A1IN8 C 2 .   ? 19.87  1.123   14.26   0   30      ? 201 A1IN8 B H14  1 c 1 
HETATM 3729 H H19  . A1IN8 C 2 .   ? 17.167 2.219   10.023  1   32.406  ? 201 A1IN8 B H19  1 c 1 
HETATM 3730 H H20  . A1IN8 C 2 .   ? 18.986 1.814   8.662   1   35.067  ? 201 A1IN8 B H20  1 c 1 
HETATM 3731 H H21  . A1IN8 C 2 .   ? 18.547 0.415   9.286   1   34.701  ? 201 A1IN8 B H21  1 c 1 
HETATM 3732 H H23  . A1IN8 C 2 .   ? 20.316 0.642   10.905  1   41.306  ? 201 A1IN8 B H23  1 c 1 
HETATM 3733 H H22  . A1IN8 C 2 .   ? 20.862 0.541   9.406   1   39.796  ? 201 A1IN8 B H22  1 c 1 
HETATM 3734 H H25  . A1IN8 C 2 .   ? 21.893 2.365   10.513  1   42.896  ? 201 A1IN8 B H25  1 c 1 
HETATM 3735 H H24  . A1IN8 C 2 .   ? 21.022 2.897   9.292   1   40.843  ? 201 A1IN8 B H24  1 c 1 
HETATM 3736 H H27  . A1IN8 C 2 .   ? 20.319 2.977   12.029  1   41.218  ? 201 A1IN8 B H27  1 c 1 
HETATM 3737 H H26  . A1IN8 C 2 .   ? 20.505 4.225   11.066  1   40.893  ? 201 A1IN8 B H26  1 c 1 
HETATM 3738 H H28  . A1IN8 C 2 .   ? 19.329 5.797   11.223  1   35.775  ? 201 A1IN8 B H28  1 c 1 
HETATM 3739 H H29  . A1IN8 C 2 .   ? 16.602 6.689   11.436  1   35.389  ? 201 A1IN8 B H29  1 c 1 
HETATM 3740 H H30  . A1IN8 C 2 .   ? 17.242 6.312   9.189   1   34.377  ? 201 A1IN8 B H30  1 c 1 
HETATM 3741 H H31  . A1IN8 C 2 .   ? 18.468 7.314   9.357   1   36.651  ? 201 A1IN8 B H31  1 c 1 
HETATM 3742 H H33  . A1IN8 C 2 .   ? 16.609 8.403   8.387   1   38.014  ? 201 A1IN8 B H33  1 c 1 
HETATM 3743 H H32  . A1IN8 C 2 .   ? 15.741 8.048   9.665   1   38.568  ? 201 A1IN8 B H32  1 c 1 
HETATM 3744 H H35  . A1IN8 C 2 .   ? 17.96  9.808   9.692   1   41.749  ? 201 A1IN8 B H35  1 c 1 
HETATM 3745 H H34  . A1IN8 C 2 .   ? 16.433 10.269  9.758   1   41.593  ? 201 A1IN8 B H34  1 c 1 
HETATM 3746 H H37  . A1IN8 C 2 .   ? 17.386 10.172  11.898  1   43.845  ? 201 A1IN8 B H37  1 c 1 
HETATM 3747 H H36  . A1IN8 C 2 .   ? 16.146 9.186   11.763  1   41.257  ? 201 A1IN8 B H36  1 c 1 
HETATM 3748 H H38  . A1IN8 C 2 .   ? 17.902 8.055   12.839  1   40.763  ? 201 A1IN8 B H38  1 c 1 
HETATM 3749 H H39  . A1IN8 C 2 .   ? 18.886 8.378   11.643  1   40.014  ? 201 A1IN8 B H39  1 c 1 
HETATM 3750 C C4   . A1IN8 D 2 .   ? 5.036  -13.626 18.08   1   35.839  ? 201 A1IN8 A C4   1 ? 2 
HETATM 3751 C C14  . A1IN8 D 2 .   ? 9.152  -14.931 19.737  1   37.925  ? 201 A1IN8 A C14  1 ? 2 
HETATM 3752 C C5   . A1IN8 D 2 .   ? 5.762  -12.778 17.253  1   38.262  ? 201 A1IN8 A C5   1 ? 2 
HETATM 3753 C C6   . A1IN8 D 2 .   ? 5.958  -13.074 15.908  1   38.828  ? 201 A1IN8 A C6   1 ? 2 
HETATM 3754 C C11  . A1IN8 D 2 .   ? 8.721  -15.751 14.812  1   55.47   ? 201 A1IN8 A C11  1 ? 2 
HETATM 3755 C C7   . A1IN8 D 2 .   ? 7.323  -11.143 15.557  1   37.466  ? 201 A1IN8 A C7   1 ? 2 
HETATM 3756 C C8   . A1IN8 D 2 .   ? 5.335  -14.168 15.338  1   39.335  ? 201 A1IN8 A C8   1 ? 2 
HETATM 3757 C C9   . A1IN8 D 2 .   ? 6.305  -15.776 13.888  1   55.768  ? 201 A1IN8 A C9   1 ? 2 
HETATM 3758 C C10  . A1IN8 D 2 .   ? 7.672  -15.127 13.882  1   59.185  ? 201 A1IN8 A C10  1 ? 2 
HETATM 3759 C C12  . A1IN8 D 2 .   ? 8.346  -15.726 16.283  1   44.961  ? 201 A1IN8 A C12  1 ? 2 
HETATM 3760 C C13  . A1IN8 D 2 .   ? 9.288  -15.109 17.303  1   46.838  ? 201 A1IN8 A C13  1 ? 2 
HETATM 3761 N N1   . A1IN8 D 2 .   ? 6.733  -14.64  20.517  1   33.161  ? 201 A1IN8 A N1   1 ? 2 
HETATM 3762 C C3   . A1IN8 D 2 .   ? 4.345  -14.658 17.502  1   38.794  ? 201 A1IN8 A C3   1 ? 2 
HETATM 3763 C C1   . A1IN8 D 2 .   ? 2.976  -16.676 16.194  1   46.736  ? 201 A1IN8 A C1   1 ? 2 
HETATM 3764 O O1   . A1IN8 D 2 .   ? 3.994  -15.992 15.491  1   43.19   ? 201 A1IN8 A O1   1 ? 2 
HETATM 3765 C C2   . A1IN8 D 2 .   ? 4.545  -14.957 16.147  1   42.631  ? 201 A1IN8 A C2   1 ? 2 
HETATM 3766 O O2   . A1IN8 D 2 .   ? 6.754  -12.333 15.082  1   36.337  ? 201 A1IN8 A O2   1 ? 2 
HETATM 3767 O O3   . A1IN8 D 2 .   ? 5.414  -14.652 14.053  1   52.267  ? 201 A1IN8 A O3   1 ? 2 
HETATM 3768 O O4   . A1IN8 D 2 .   ? 8.18   -15.04  12.559  1   55.108  ? 201 A1IN8 A O4   1 ? 2 
HETATM 3769 O O5   . A1IN8 D 2 .   ? 9.959  -15.069 14.713  1   46.339  ? 201 A1IN8 A O5   1 ? 2 
HETATM 3770 O O6   . A1IN8 D 2 .   ? 8.519  -15.053 18.56   1   38.744  ? 201 A1IN8 A O6   1 ? 2 
HETATM 3771 O O7   . A1IN8 D 2 .   ? 10.337 -14.986 19.9    1   40.942  ? 201 A1IN8 A O7   1 ? 2 
HETATM 3772 C C15  . A1IN8 D 2 .   ? 8.167  -14.713 20.871  1   32.694  ? 201 A1IN8 A C15  1 ? 2 
HETATM 3773 C C16  . A1IN8 D 2 .   ? 8.443  -15.847 21.855  1   36.957  ? 201 A1IN8 A C16  1 ? 2 
HETATM 3774 C C17  . A1IN8 D 2 .   ? 7.866  -17.148 21.335  1   37.735  ? 201 A1IN8 A C17  1 ? 2 
HETATM 3775 C C18  . A1IN8 D 2 .   ? 6.398  -17.019 21.295  1   37.982  ? 201 A1IN8 A C18  1 ? 2 
HETATM 3776 C C19  . A1IN8 D 2 .   ? 5.995  -15.922 20.263  1   38.477  ? 201 A1IN8 A C19  1 ? 2 
HETATM 3777 C C20  . A1IN8 D 2 .   ? 6.226  -13.423 20.154  1   34.299  ? 201 A1IN8 A C20  1 ? 2 
HETATM 3778 O O8   . A1IN8 D 2 .   ? 6.912  -12.416 20.211  1   32.074  ? 201 A1IN8 A O8   1 ? 2 
HETATM 3779 C C21  . A1IN8 D 2 .   ? 4.838  -13.265 19.556  1   36.224  ? 201 A1IN8 A C21  1 ? 2 
HETATM 3780 C C22  . A1IN8 D 2 .   ? 4.244  -11.873 19.9    1   35.679  ? 201 A1IN8 A C22  1 ? 2 
HETATM 3781 C C23  . A1IN8 D 2 .   ? 3.927  -11.756 21.407  1   38.634  ? 201 A1IN8 A C23  1 ? 2 
HETATM 3782 C C24  . A1IN8 D 2 .   ? 3.184  -10.391 21.635  1   40.973  ? 201 A1IN8 A C24  1 ? 2 
HETATM 3783 C C25  . A1IN8 D 2 .   ? 1.918  -10.28  20.805  1   37.753  ? 201 A1IN8 A C25  1 ? 2 
HETATM 3784 C C26  . A1IN8 D 2 .   ? 2.306  -10.343 19.359  1   42.535  ? 201 A1IN8 A C26  1 ? 2 
HETATM 3785 C C27  . A1IN8 D 2 .   ? 2.942  -11.674 19.136  1   36.974  ? 201 A1IN8 A C27  1 ? 2 
HETATM 3786 H H5   . A1IN8 D 2 .   ? 6.224  -12.051 17.642  1   36.38   ? 201 A1IN8 A H5   1 c 2 
HETATM 3787 H H13  . A1IN8 D 2 .   ? 8.87   -16.691 14.536  1   53.63   ? 201 A1IN8 A H13  1 c 2 
HETATM 3788 H H7   . A1IN8 D 2 .   ? 7.803  -10.706 14.836  1   36.938  ? 201 A1IN8 A H7   1 c 2 
HETATM 3789 H H8   . A1IN8 D 2 .   ? 7.939  -11.345 16.28   1   35.842  ? 201 A1IN8 A H8   1 c 2 
HETATM 3790 H H6   . A1IN8 D 2 .   ? 6.622  -10.555 15.882  1   36.431  ? 201 A1IN8 A H6   1 c 2 
HETATM 3791 H H10  . A1IN8 D 2 .   ? 6.221  -16.414 14.629  1   55.557  ? 201 A1IN8 A H10  1 c 2 
HETATM 3792 H H9   . A1IN8 D 2 .   ? 6.132  -16.237 13.038  1   57.715  ? 201 A1IN8 A H9   1 c 2 
HETATM 3793 H H11  . A1IN8 D 2 .   ? 7.57   -14.198 14.218  1   54.943  ? 201 A1IN8 A H11  1 c 2 
HETATM 3794 H H15  . A1IN8 D 2 .   ? 8.187  -16.655 16.557  1   48.383  ? 201 A1IN8 A H15  1 c 2 
HETATM 3795 H H16  . A1IN8 D 2 .   ? 7.489  -15.261 16.361  1   47.366  ? 201 A1IN8 A H16  1 c 2 
HETATM 3796 H H17  . A1IN8 D 2 .   ? 9.553  -14.209 17.025  1   43.547  ? 201 A1IN8 A H17  1 c 2 
HETATM 3797 H H18  . A1IN8 D 2 .   ? 10.085 -15.667 17.411  1   44.501  ? 201 A1IN8 A H18  1 c 2 
HETATM 3798 H H4   . A1IN8 D 2 .   ? 3.829  -15.231 18.043  1   39.611  ? 201 A1IN8 A H4   1 c 2 
HETATM 3799 H H2   . A1IN8 D 2 .   ? 2.565  -17.33  15.605  1   47.59   ? 201 A1IN8 A H2   1 c 2 
HETATM 3800 H H3   . A1IN8 D 2 .   ? 2.302  -16.044 16.492  1   45.534  ? 201 A1IN8 A H3   1 c 2 
HETATM 3801 H H1   . A1IN8 D 2 .   ? 3.36   -17.131 16.961  1   45.163  ? 201 A1IN8 A H1   1 c 2 
HETATM 3802 H H12  . A1IN8 D 2 .   ? 9.101  -14.664 12.617  0   30      ? 201 A1IN8 A H12  1 c 2 
HETATM 3803 H H14  . A1IN8 D 2 .   ? 10.532 -15.531 15.286  0   30      ? 201 A1IN8 A H14  1 c 2 
HETATM 3804 H H19  . A1IN8 D 2 .   ? 8.406  -13.856 21.314  1   33.296  ? 201 A1IN8 A H19  1 c 2 
HETATM 3805 H H20  . A1IN8 D 2 .   ? 8.035  -15.631 22.727  1   35.602  ? 201 A1IN8 A H20  1 c 2 
HETATM 3806 H H21  . A1IN8 D 2 .   ? 9.417  -15.947 21.989  1   35.876  ? 201 A1IN8 A H21  1 c 2 
HETATM 3807 H H23  . A1IN8 D 2 .   ? 8.212  -17.338 20.433  1   38.394  ? 201 A1IN8 A H23  1 c 2 
HETATM 3808 H H22  . A1IN8 D 2 .   ? 8.121  -17.891 21.929  1   38.372  ? 201 A1IN8 A H22  1 c 2 
HETATM 3809 H H25  . A1IN8 D 2 .   ? 5.997  -17.876 21.038  1   39.376  ? 201 A1IN8 A H25  1 c 2 
HETATM 3810 H H24  . A1IN8 D 2 .   ? 6.062  -16.775 22.184  1   37.795  ? 201 A1IN8 A H24  1 c 2 
HETATM 3811 H H27  . A1IN8 D 2 .   ? 6.197  -16.238 19.353  1   38.062  ? 201 A1IN8 A H27  1 c 2 
HETATM 3812 H H26  . A1IN8 D 2 .   ? 5.026  -15.764 20.322  1   37.717  ? 201 A1IN8 A H26  1 c 2 
HETATM 3813 H H28  . A1IN8 D 2 .   ? 4.256  -13.96  19.955  1   36.487  ? 201 A1IN8 A H28  1 c 2 
HETATM 3814 H H29  . A1IN8 D 2 .   ? 4.887  -11.162 19.643  1   35.577  ? 201 A1IN8 A H29  1 c 2 
HETATM 3815 H H30  . A1IN8 D 2 .   ? 4.755  -11.778 21.928  1   37.518  ? 201 A1IN8 A H30  1 c 2 
HETATM 3816 H H31  . A1IN8 D 2 .   ? 3.357  -12.5   21.689  1   38.996  ? 201 A1IN8 A H31  1 c 2 
HETATM 3817 H H33  . A1IN8 D 2 .   ? 2.955  -10.305 22.587  1   39.304  ? 201 A1IN8 A H33  1 c 2 
HETATM 3818 H H32  . A1IN8 D 2 .   ? 3.789  -9.652  21.403  1   38.694  ? 201 A1IN8 A H32  1 c 2 
HETATM 3819 H H35  . A1IN8 D 2 .   ? 1.307  -11.018 21.023  1   40.506  ? 201 A1IN8 A H35  1 c 2 
HETATM 3820 H H34  . A1IN8 D 2 .   ? 1.465  -9.43   20.995  1   39.972  ? 201 A1IN8 A H34  1 c 2 
HETATM 3821 H H37  . A1IN8 D 2 .   ? 1.511  -10.246 18.789  1   41.266  ? 201 A1IN8 A H37  1 c 2 
HETATM 3822 H H36  . A1IN8 D 2 .   ? 2.941  -9.623  19.146  1   39.387  ? 201 A1IN8 A H36  1 c 2 
HETATM 3823 H H38  . A1IN8 D 2 .   ? 3.117  -11.78  18.178  1   38.714  ? 201 A1IN8 A H38  1 c 2 
HETATM 3824 H H39  . A1IN8 D 2 .   ? 2.314  -12.374 19.397  1   39.078  ? 201 A1IN8 A H39  1 c 2 
HETATM 3825 O O    . HOH   E 3 .   ? -0.983 4.712   10.601  1   59.915  ? 301 HOH   B O    1 ? ? 
HETATM 3826 O O    . HOH   E 3 .   ? 26.891 -3.89   -7.745  1   46.868  ? 302 HOH   B O    1 ? ? 
HETATM 3827 O O    . HOH   E 3 .   ? 0.858  -4.938  -3.852  1   52.587  ? 303 HOH   B O    1 ? ? 
HETATM 3828 O O    . HOH   E 3 .   ? 29.597 -9.27   -4.33   1   41.447  ? 304 HOH   B O    1 ? ? 
HETATM 3829 O O    . HOH   E 3 .   ? 27.147 -17.272 4.126   1   50.037  ? 305 HOH   B O    1 ? ? 
HETATM 3830 O O    . HOH   E 3 .   ? 15.744 -8.741  -0.996  1   41.001  ? 306 HOH   B O    1 ? ? 
HETATM 3831 O O    . HOH   E 3 .   ? 7.447  0.626   14.697  1   39.521  ? 307 HOH   B O    1 ? ? 
HETATM 3832 O O    . HOH   E 3 .   ? 13.69  -7.22   15.97   1   35.432  ? 308 HOH   B O    1 ? ? 
HETATM 3833 O O    . HOH   E 3 .   ? 18.912 -7.789  10.811  1   37.167  ? 309 HOH   B O    1 ? ? 
HETATM 3834 O O    . HOH   E 3 .   ? 7.499  5.757   11.416  1   41.808  ? 310 HOH   B O    1 ? ? 
HETATM 3835 O O    . HOH   E 3 .   ? 10.651 -2.283  9.711   1   29.814  ? 311 HOH   B O    1 ? ? 
HETATM 3836 O O    . HOH   E 3 .   ? 33.298 4.9     -0.838  1   48.18   ? 312 HOH   B O    1 ? ? 
HETATM 3837 O O    . HOH   E 3 .   ? 13.061 -5.159  11.819  1   45.18   ? 313 HOH   B O    1 ? ? 
HETATM 3838 O O    . HOH   E 3 .   ? 5.375  8.49    4.805   1   41.306  ? 314 HOH   B O    1 ? ? 
HETATM 3839 O O    . HOH   E 3 .   ? 18.642 8.574   -6.49   1   47.031  ? 315 HOH   B O    1 ? ? 
HETATM 3840 O O    . HOH   E 3 .   ? 33.146 -4.192  -10.204 1   56.207  ? 316 HOH   B O    1 ? ? 
HETATM 3841 O O    . HOH   E 3 .   ? 9      4.981   9.303   1   32.182  ? 317 HOH   B O    1 ? ? 
HETATM 3842 O O    . HOH   E 3 .   ? 9.164  3.491   -1.128  1   31.194  ? 318 HOH   B O    1 ? ? 
HETATM 3843 O O    . HOH   E 3 .   ? 6.557  7.375   0.643   1   48.642  ? 319 HOH   B O    1 ? ? 
HETATM 3844 O O    . HOH   E 3 .   ? 6.578  -7.094  0.509   1   38.393  ? 320 HOH   B O    1 ? ? 
HETATM 3845 O O    . HOH   E 3 .   ? 3.218  6.116   18.57   1   42.732  ? 321 HOH   B O    1 ? ? 
HETATM 3846 O O    . HOH   E 3 .   ? 7.253  -0.042  -9.412  1   45.075  ? 322 HOH   B O    1 ? ? 
HETATM 3847 O O    . HOH   E 3 .   ? 26.699 6.122   2.439   1   55.521  ? 323 HOH   B O    1 ? ? 
HETATM 3848 O O    . HOH   E 3 .   ? 1.609  2.787   0       0.5 54.662  ? 324 HOH   B O    1 ? ? 
HETATM 3849 O O    . HOH   E 3 .   ? 17.851 -2.142  -8.176  1   42.855  ? 325 HOH   B O    1 ? ? 
HETATM 3850 O O    . HOH   E 3 .   ? 13.737 14.914  -4.23   1   52.735  ? 326 HOH   B O    1 ? ? 
HETATM 3851 O O    . HOH   E 3 .   ? 7.204  5.392   20.329  1   42.975  ? 327 HOH   B O    1 ? ? 
HETATM 3852 O O    . HOH   E 3 .   ? 9.098  12.127  8.275   1   51.227  ? 328 HOH   B O    1 ? ? 
HETATM 3853 O O    . HOH   E 3 .   ? 12.718 11.161  1.63    1   54.479  ? 329 HOH   B O    1 ? ? 
HETATM 3854 O O    . HOH   E 3 .   ? 34.27  -2.595  10.807  1   63.141  ? 330 HOH   B O    1 ? ? 
HETATM 3855 O O    . HOH   F 3 .   ? 8.378  -23.967 39.673  1   48.072  ? 301 HOH   A O    1 ? ? 
HETATM 3856 O O    . HOH   F 3 .   ? 11.815 -5.507  40.544  1   43.984  ? 302 HOH   A O    1 ? ? 
HETATM 3857 O O    . HOH   F 3 .   ? 12.767 -2.597  34.425  1   48.359  ? 303 HOH   A O    1 ? ? 
HETATM 3858 O O    . HOH   F 3 .   ? 18.746 -15.385 34.503  1   50.033  ? 304 HOH   A O    1 ? ? 
HETATM 3859 O O    . HOH   F 3 .   ? 16.36  -3.311  28.823  1   37.171  ? 305 HOH   A O    1 ? ? 
HETATM 3860 O O    . HOH   F 3 .   ? 10.355 -3.546  19.6    1   29.762  ? 306 HOH   A O    1 ? ? 
HETATM 3861 O O    . HOH   F 3 .   ? 22.082 -29.413 25.786  1   56.416  ? 307 HOH   A O    1 ? ? 
HETATM 3862 O O    . HOH   F 3 .   ? 16.008 -2.355  31.246  1   48.007  ? 308 HOH   A O    1 ? ? 
HETATM 3863 O O    . HOH   F 3 .   ? 7.631  -2.26   31.822  1   37.582  ? 309 HOH   A O    1 ? ? 
HETATM 3864 O O    . HOH   F 3 .   ? 15.602 -10.624 21.524  1   37.111  ? 310 HOH   A O    1 ? ? 
HETATM 3865 O O    . HOH   F 3 .   ? 10.101 -5.323  21.592  1   31.339  ? 311 HOH   A O    1 ? ? 
HETATM 3866 O O    . HOH   F 3 .   ? 10.51  -3.765  12.128  1   33.888  ? 312 HOH   A O    1 ? ? 
HETATM 3867 O O    . HOH   F 3 .   ? 11.789 -29.708 36.155  1   60.04   ? 313 HOH   A O    1 ? ? 
HETATM 3868 O O    . HOH   F 3 .   ? 16.278 -20.396 20.789  1   55.633  ? 314 HOH   A O    1 ? ? 
HETATM 3869 O O    . HOH   F 3 .   ? 9.507  -0.576  13.432  1   41.493  ? 315 HOH   A O    1 ? ? 
HETATM 3870 O O    . HOH   F 3 .   ? 5.834  -9.052  12.206  1   48.674  ? 316 HOH   A O    1 ? ? 
HETATM 3871 O O    . HOH   F 3 .   ? 6.646  -12.212 12.279  1   45.92   ? 317 HOH   A O    1 ? ? 
HETATM 3872 O O    . HOH   F 3 .   ? 1.006  -9.299  39.997  1   55.525  ? 318 HOH   A O    1 ? ? 
HETATM 3873 O O    . HOH   F 3 .   ? -2.141 -25.806 33.021  1   42.982  ? 319 HOH   A O    1 ? ? 
HETATM 3874 O O    . HOH   F 3 .   ? 0.493  -19.719 29.637  1   54.39   ? 320 HOH   A O    1 ? ? 
HETATM 3875 O O    . HOH   F 3 .   ? 17     -1.71   20.788  1   44.074  ? 321 HOH   A O    1 ? ? 
HETATM 3876 O O    . HOH   F 3 .   ? 16.539 -3.238  16.829  1   53.513  ? 322 HOH   A O    1 ? ? 
HETATM 3877 O O    . HOH   F 3 .   ? 11.336 -5.683  32.522  1   51.175  ? 323 HOH   A O    1 ? ? 
HETATM 3878 O O    . HOH   F 3 .   ? 6.747  -0.186  25.394  1   35.439  ? 324 HOH   A O    1 ? ? 
HETATM 3879 O O    . HOH   F 3 .   ? -4.984 -21.627 29.409  1   42.675  ? 325 HOH   A O    1 ? ? 
HETATM 3880 O O    . HOH   F 3 .   ? 12.739 -0.645  36.698  1   49.559  ? 326 HOH   A O    1 ? ? 
HETATM 3881 O O    . HOH   F 3 .   ? 0.725  -18.864 17.906  1   48.658  ? 327 HOH   A O    1 ? ? 
HETATM 3882 O O    . HOH   F 3 .   ? 17.325 -5.823  39.848  1   44.76   ? 328 HOH   A O    1 ? ? 
HETATM 3883 O O    . HOH   F 3 .   ? 3.361  -2.277  23.294  1   37.966  ? 329 HOH   A O    1 ? ? 
HETATM 3884 O O    . HOH   F 3 .   ? -3.029 -13.971 24.477  1   53.166  ? 330 HOH   A O    1 ? ? 
HETATM 3885 O O    . HOH   F 3 .   ? 16.38  -6.57   18.763  1   47.374  ? 331 HOH   A O    1 ? ? 
HETATM 3886 O O    . HOH   F 3 .   ? 0.794  -2.221  17.833  1   38.39   ? 332 HOH   A O    1 ? ? 
HETATM 3887 O O    . HOH   F 3 .   ? -2.022 -4.854  46.032  1   61.698  ? 333 HOH   A O    1 ? ? 
HETATM 3888 O O    . HOH   F 3 .   ? 15.087 -11.541 17.665  1   55.643  ? 334 HOH   A O    1 ? ? 
HETATM 3889 O O    . HOH   F 3 .   ? 0.375  -8.95   35.671  1   49.41   ? 335 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   ? 1.23677  0.586396 0.72992  -0.0899027  0.05472     0.232522    13  GLY   B N    
2    C CA   . GLY   A 1   ? 1.15862  0.54026  0.716146 -0.113358   0.0638146   0.204117    13  GLY   B CA   
3    C C    . GLY   A 1   ? 1.10894  0.545176 0.650533 -0.11376    0.0614288   0.183592    13  GLY   B C    
4    O O    . GLY   A 1   ? 1.22153  0.666154 0.703467 -0.0993674  0.054885    0.19049     13  GLY   B O    
5    H H1   . GLY   A 1   ? 1.2666   0.580752 0.769687 -0.0889801  0.057818    0.246706    13  GLY   B H1   
6    H H2   . GLY   A 1   ? 1.20855  0.575784 0.691802 -0.0757918  0.0315598   0.221119    13  GLY   B H2   
7    H H3   . GLY   A 1   ? 1.26213  0.608716 0.715112 -0.0889403  0.0685735   0.248107    13  GLY   B H3   
8    H HA2  . GLY   A 1   ? 1.18787  0.552568 0.765629 -0.129218   0.0881376   0.216649    13  GLY   B HA2  
9    H HA3  . GLY   A 1   ? 1.13658  0.520075 0.729381 -0.112038   0.046941    0.185957    13  GLY   B HA3  
10   N N    . ALA   A 2   ? 1.00718  0.476149 0.604365 -0.130636   0.066177    0.158896    14  ALA   B N    
11   C CA   . ALA   A 2   ? 1.07147  0.587896 0.66801  -0.133898   0.0688801   0.140035    14  ALA   B CA   
12   C C    . ALA   A 2   ? 1.07285  0.617634 0.647112 -0.114732   0.0377093   0.123336    14  ALA   B C    
13   O O    . ALA   A 2   ? 1.04677  0.611054 0.586726 -0.110411   0.0381936   0.120268    14  ALA   B O    
14   C CB   . ALA   A 2   ? 1.01191  0.555313 0.679296 -0.152506   0.0750545   0.119126    14  ALA   B CB   
15   H H    . ALA   A 2   ? 1.0377   0.497349 0.676801 -0.140066   0.0664206   0.153225    14  ALA   B H    
16   H HA   . ALA   A 2   ? 1.0818   0.593047 0.645712 -0.13543    0.0881909   0.153508    14  ALA   B HA   
17   H HB1  . ALA   A 2   ? 1.04037  0.568674 0.730151 -0.165986   0.0952341   0.130594    14  ALA   B HB1  
18   H HB2  . ALA   A 2   ? 0.993441 0.539231 0.685483 -0.149384   0.0557666   0.105004    14  ALA   B HB2  
19   H HB3  . ALA   A 2   ? 0.986032 0.559299 0.653619 -0.15323    0.0778395   0.108368    14  ALA   B HB3  
20   N N    . PRO   A 3   ? 0.966864 0.514212 0.5627   -0.102567   0.0121944   0.111727    15  PRO   B N    
21   C CA   . PRO   A 3   ? 0.949506 0.52774  0.53825  -0.0847984  -0.012283   0.0995973   15  PRO   B CA   
22   C C    . PRO   A 3   ? 1.06026  0.626967 0.597285 -0.0692007  -0.0250508  0.117175    15  PRO   B C    
23   O O    . PRO   A 3   ? 0.940805 0.535954 0.465173 -0.0634865  -0.0378802  0.109361    15  PRO   B O    
24   C CB   . PRO   A 3   ? 0.911951 0.484963 0.531329 -0.0725781  -0.0280598  0.0889786   15  PRO   B CB   
25   C CG   . PRO   A 3   ? 0.91823  0.472934 0.570784 -0.09063    -0.0152423  0.0819514   15  PRO   B CG   
26   C CD   . PRO   A 3   ? 1.01703  0.537795 0.649406 -0.104559   0.00723344  0.107743    15  PRO   B CD   
27   H HA   . PRO   A 3   ? 0.918602 0.526321 0.519022 -0.0895621  -0.0105381  0.0869268   15  PRO   B HA   
28   H HB2  . PRO   A 3   ? 0.947549 0.49864  0.552131 -0.0607615  -0.0358496  0.100311    15  PRO   B HB2  
29   H HB3  . PRO   A 3   ? 0.880715 0.482765 0.514327 -0.0658856  -0.0365102  0.0758505   15  PRO   B HB3  
30   H HG2  . PRO   A 3   ? 0.937346 0.474415 0.60298  -0.0842693  -0.0238669  0.0760687   15  PRO   B HG2  
31   H HG3  . PRO   A 3   ? 0.893716 0.474314 0.566777 -0.0987853  -0.0120297  0.0684874   15  PRO   B HG3  
32   H HD2  . PRO   A 3   ? 1.03667  0.526184 0.651786 -0.0967157  0.00455011  0.122776    15  PRO   B HD2  
33   H HD3  . PRO   A 3   ? 0.99697  0.513393 0.657831 -0.120416   0.0198779   0.105239    15  PRO   B HD3  
34   N N    . ALA   A 4   ? 1.02659  0.549163 0.53313  -0.0627957  -0.0223894  0.141916    16  ALA   B N    
35   C CA   . ALA   A 4   ? 1.0762   0.586479 0.527876 -0.0448271  -0.0389255  0.160277    16  ALA   B CA   
36   C C    . ALA   A 4   ? 1.13922  0.653703 0.537042 -0.0503818  -0.0283791  0.163203    16  ALA   B C    
37   O O    . ALA   A 4   ? 1.1839   0.711832 0.544149 -0.0379762  -0.0514348  0.159925    16  ALA   B O    
38   C CB   . ALA   A 4   ? 1.19266  0.649642 0.622955 -0.0347509  -0.0359737  0.189912    16  ALA   B CB   
39   H H    . ALA   A 4   ? 1.06273  0.561467 0.583907 -0.0691927  -0.0115752  0.147805    16  ALA   B H    
40   H HA   . ALA   A 4   ? 1.06587  0.599815 0.530481 -0.0333872  -0.0605427  0.150874    16  ALA   B HA   
41   H HB1  . ALA   A 4   ? 1.16338  0.61604  0.626255 -0.029039   -0.0440252  0.18486     16  ALA   B HB1  
42   H HB2  . ALA   A 4   ? 1.20351  0.637193 0.628376 -0.0470926  -0.0125957  0.200961    16  ALA   B HB2  
43   H HB3  . ALA   A 4   ? 1.21644  0.665473 0.606959 -0.0206186  -0.0492201  0.203532    16  ALA   B HB3  
44   N N    . THR   A 5   ? 1.11059  0.613209 0.505662 -0.0682905  0.00654004  0.167766    17  THR   B N    
45   C CA   . THR   A 5   ? 1.10259  0.609759 0.446598 -0.0711437  0.0219996   0.166284    17  THR   B CA   
46   C C    . THR   A 5   ? 1.03742  0.59119  0.40123  -0.0719397  0.00214436  0.133664    17  THR   B C    
47   O O    . THR   A 5   ? 0.994507 0.551333 0.307485 -0.0626232  -0.0122625  0.127255    17  THR   B O    
48   C CB   . THR   A 5   ? 1.12277  0.617187 0.480178 -0.0902286  0.0681145   0.176046    17  THR   B CB   
49   O OG1  . THR   A 5   ? 1.229    0.675264 0.564499 -0.0874948  0.08447     0.211146    17  THR   B OG1  
50   C CG2  . THR   A 5   ? 1.1237   0.626767 0.435955 -0.0917459  0.0907264   0.169496    17  THR   B CG2  
51   H H    . THR   A 5   ? 1.10363  0.595069 0.530168 -0.0781151  0.0210026   0.171038    17  THR   B H    
52   H HA   . THR   A 5   ? 1.16703  0.653377 0.455344 -0.0582945  0.014991    0.181283    17  THR   B HA   
53   H HB   . THR   A 5   ? 1.07263  0.58503  0.488775 -0.102237   0.0712953   0.162976    17  THR   B HB   
55   H HG21 . THR   A 5   ? 1.14868  0.641966 0.470695 -0.101743   0.123262    0.180853    17  THR   B HG21 
56   H HG22 . THR   A 5   ? 1.18428  0.67119  0.432752 -0.0778803  0.0824544   0.177546    17  THR   B HG22 
57   H HG23 . THR   A 5   ? 1.08296  0.616402 0.420867 -0.0954116  0.0812816   0.145916    17  THR   B HG23 
58   N N    . VAL   A 6   ? 0.937181 0.523896 0.372462 -0.0803236  -0.00303726 0.113696    18  VAL   B N    
59   C CA   . VAL   A 6   ? 0.918774 0.546803 0.380773 -0.0824241  -0.0155867  0.0875006   18  VAL   B CA   
60   C C    . VAL   A 6   ? 0.916861 0.559593 0.371486 -0.0668346  -0.0533452  0.0825856   18  VAL   B C    
61   O O    . VAL   A 6   ? 0.90156  0.561406 0.345769 -0.0664618  -0.0665958  0.0669177   18  VAL   B O    
62   C CB   . VAL   A 6   ? 0.801063 0.458414 0.333731 -0.0919539  -0.00949985 0.0722038   18  VAL   B CB   
63   C CG1  . VAL   A 6   ? 0.792142 0.4863   0.349144 -0.0943231  -0.015744   0.0508457   18  VAL   B CG1  
64   C CG2  . VAL   A 6   ? 0.932855 0.578571 0.483253 -0.107843   0.0219493   0.0767422   18  VAL   B CG2  
65   H H    . VAL   A 6   ? 0.936891 0.517961 0.403385 -0.0839842  0.0013595   0.116941    18  VAL   B H    
66   H HA   . VAL   A 6   ? 0.920513 0.547547 0.358381 -0.0868236  -0.00330857 0.0829143   18  VAL   B HA   
67   H HB   . VAL   A 6   ? 0.822448 0.480789 0.374693 -0.0851367  -0.0218359  0.0742034   18  VAL   B HB   
68   H HG11 . VAL   A 6   ? 0.803228 0.492829 0.335211 -0.0982101  -0.00622969 0.0472469   18  VAL   B HG11 
69   H HG12 . VAL   A 6   ? 0.774082 0.479293 0.335049 -0.0860039  -0.0360269  0.0480248   18  VAL   B HG12 
70   H HG13 . VAL   A 6   ? 0.743629 0.453624 0.338668 -0.0994056  -0.00874212 0.0440607   18  VAL   B HG13 
71   H HG21 . VAL   A 6   ? 0.846436 0.513635 0.436665 -0.113278   0.0237264   0.0646649   18  VAL   B HG21 
72   H HG22 . VAL   A 6   ? 0.909098 0.532904 0.460019 -0.107967   0.0243967   0.0886683   18  VAL   B HG22 
73   H HG23 . VAL   A 6   ? 0.916324 0.554927 0.440139 -0.111723   0.0378655   0.0799703   18  VAL   B HG23 
74   N N    . THR   A 7   ? 0.980076 0.613326 0.442305 -0.0535706  -0.070775   0.096189    19  THR   B N    
75   C CA   . THR   A 7   ? 1.01335  0.663476 0.479674 -0.0370563  -0.107142   0.0954062   19  THR   B CA   
76   C C    . THR   A 7   ? 1.1041   0.741231 0.503384 -0.030463   -0.125726   0.0966096   19  THR   B C    
77   O O    . THR   A 7   ? 1.18485  0.849273 0.598189 -0.0277727  -0.153535   0.0800918   19  THR   B O    
78   C CB   . THR   A 7   ? 1.07227  0.706554 0.550326 -0.0204231  -0.118225   0.113666    19  THR   B CB   
79   O OG1  . THR   A 7   ? 0.93275  0.584948 0.470146 -0.0241676  -0.105803   0.103373    19  THR   B OG1  
80   C CG2  . THR   A 7   ? 1.09588  0.748246 0.582032 -0.00051824 -0.156437   0.117468    19  THR   B CG2  
81   H H    . THR   A 7   ? 0.975785 0.592012 0.445817 -0.0545789  -0.0601009  0.105723    19  THR   B H    
82   H HA   . THR   A 7   ? 0.975129 0.655901 0.482749 -0.0396282  -0.113252   0.0814021   19  THR   B HA   
83   H HB   . THR   A 7   ? 1.08994  0.690568 0.535305 -0.0197419  -0.107258   0.129188    19  THR   B HB   
85   H HG21 . THR   A 7   ? 1.09187  0.739053 0.598374 0.0106374   -0.159454   0.126608    19  THR   B HG21 
86   H HG22 . THR   A 7   ? 1.05757  0.742813 0.577928 -0.00347587 -0.165847   0.103115    19  THR   B HG22 
87   H HG23 . THR   A 7   ? 1.14411  0.780153 0.582996 0.00496309  -0.168657   0.125374    19  THR   B HG23 
88   N N    . GLU   A 8   ? 1.13846  0.73339  0.467843 -0.0280312  -0.10903    0.115607    20  GLU   B N    
89   C CA   . GLU   A 8   ? 1.3494   0.921204 0.59571  -0.0132253  -0.129049   0.123736    20  GLU   B CA   
90   C C    . GLU   A 8   ? 1.32729  0.8982   0.527496 -0.0210755  -0.11733    0.103589    20  GLU   B C    
91   O O    . GLU   A 8   ? 1.30613  0.87699  0.459607 -0.0100163  -0.149668   0.0912611   20  GLU   B O    
92   C CB   . GLU   A 8   ? 1.45214  0.973446 0.634646 -0.00089617 -0.115303   0.160251    20  GLU   B CB   
93   C CG   . GLU   A 8   ? 1.42905  0.942059 0.654457 0.00945964  -0.125795   0.180128    20  GLU   B CG   
94   C CD   . GLU   A 8   ? 1.59356  1.05068  0.759804 0.0219175   -0.11137    0.219558    20  GLU   B CD   
95   O OE1  . GLU   A 8   ? 1.61744  1.04532  0.693544 0.0312011   -0.106045   0.235246    20  GLU   B OE1  
96   O OE2  . GLU   A 8   ? 1.46803  0.907241 0.675497 0.0240512   -0.104272   0.235077    20  GLU   B OE2  
97   H H    . GLU   A 8   ? 1.16957  0.74883  0.502919 -0.0352082  -0.083863   0.124656    20  GLU   B H    
98   H HA   . GLU   A 8   ? 1.31468  0.903624 0.574092 -0.00331072 -0.162525   0.118278    20  GLU   B HA   
99   H HB2  . GLU   A 8   ? 1.45305  0.957701 0.624773 -0.0113378  -0.0811347  0.167082    20  GLU   B HB2  
100  H HB3  . GLU   A 8   ? 1.50798  1.01568  0.629417 0.0120675   -0.132374   0.165005    20  GLU   B HB3  
101  H HG2  . GLU   A 8   ? 1.4392   0.972042 0.680987 0.0208535   -0.157986   0.174428    20  GLU   B HG2  
102  H HG3  . GLU   A 8   ? 1.39081  0.914705 0.670471 -0.00195295 -0.110233   0.173109    20  GLU   B HG3  
103  N N    . GLN   A 9   ? 1.27479  0.845579 0.490655 -0.0382385  -0.0750075  0.0978486   21  GLN   B N    
104  C CA   . GLN   A 9   ? 1.37141  0.935103 0.536664 -0.0413642  -0.0581461  0.0806427   21  GLN   B CA   
105  C C    . GLN   A 9   ? 1.17407  0.773215 0.409001 -0.0583036  -0.0476542  0.0516104   21  GLN   B C    
106  O O    . GLN   A 9   ? 1.37527  0.969789 0.579066 -0.0604151  -0.03289    0.0334545   21  GLN   B O    
107  C CB   . GLN   A 9   ? 1.50543  1.03408  0.614929 -0.042989   -0.00771002 0.1014      21  GLN   B CB   
108  C CG   . GLN   A 9   ? 1.60683  1.10806  0.719672 -0.04262    0.0128358   0.139735    21  GLN   B CG   
109  C CD   . GLN   A 9   ? 1.67054  1.12435  0.68068  -0.0238119  0.0219646   0.170689    21  GLN   B CD   
110  O OE1  . GLN   A 9   ? 1.78372  1.22073  0.712593 -0.0142328  0.0355753   0.166185    21  GLN   B OE1  
111  N NE2  . GLN   A 9   ? 1.76704  1.1952   0.778415 -0.0171573  0.0194299   0.203413    21  GLN   B NE2  
112  H H    . GLN   A 9   ? 1.2523   0.827419 0.511423 -0.0468975  -0.0574015  0.10356     21  GLN   B H    
113  H HA   . GLN   A 9   ? 1.39298  0.951276 0.512989 -0.0301809  -0.0850839  0.0721194   21  GLN   B HA   
114  H HB2  . GLN   A 9   ? 1.46706  1.00912  0.611086 -0.0552856  0.0166625   0.090828    21  GLN   B HB2  
115  H HB3  . GLN   A 9   ? 1.57478  1.08408  0.611994 -0.0314839  -0.010599   0.0999879   21  GLN   B HB3  
116  H HG2  . GLN   A 9   ? 1.533    1.04382  0.684073 -0.0410475  -0.0100376  0.141777    21  GLN   B HG2  
117  H HG3  . GLN   A 9   ? 1.5463   1.0503   0.696508 -0.056148   0.0443573   0.143606    21  GLN   B HG3  
118  H HE21 . GLN   A 9   ? 1.80499  1.21138  0.760434 -0.00104109 0.00554497  0.218617    21  GLN   B HE21 
119  H HE22 . GLN   A 9   ? 1.70207  1.13335  0.769507 -0.027943   0.0304456   0.209504    21  GLN   B HE22 
120  N N    . GLY   A 10  ? 1.05856  0.689834 0.381866 -0.0676348  -0.0527179  0.0474954   22  GLY   B N    
121  C CA   . GLY   A 10  ? 0.939053 0.599495 0.323284 -0.081379   -0.0380154  0.0266851   22  GLY   B CA   
122  C C    . GLY   A 10  ? 0.930342 0.612155 0.332635 -0.0805271  -0.0685672  -5.471e-05  22  GLY   B C    
123  O O    . GLY   A 10  ? 0.891926 0.579096 0.290613 -0.0717106  -0.10655    -0.00204811 22  GLY   B O    
124  H H    . GLY   A 10  ? 1.03911  0.672984 0.382302 -0.06348    -0.0649879  0.0581807   22  GLY   B H    
125  H HA2  . GLY   A 10  ? 0.969961 0.620512 0.336691 -0.0861938  -0.0110536  0.0258358   22  GLY   B HA2  
126  H HA3  . GLY   A 10  ? 0.902348 0.577736 0.336947 -0.0858984  -0.0342348  0.0314419   22  GLY   B HA3  
127  N N    . GLU   A 11  ? 0.983819 0.675417 0.407807 -0.0895006  -0.0514971  -0.0200177  23  GLU   B N    
128  C CA   . GLU   A 11  ? 0.899539 0.607075 0.353199 -0.0923739  -0.0741263  -0.0468812  23  GLU   B CA   
129  C C    . GLU   A 11  ? 0.818488 0.563804 0.364405 -0.0974051  -0.0868066  -0.0446045  23  GLU   B C    
130  O O    . GLU   A 11  ? 0.757738 0.518834 0.348589 -0.101531   -0.0637309  -0.0326021  23  GLU   B O    
131  C CB   . GLU   A 11  ? 0.985355 0.684694 0.431885 -0.098069   -0.0425315  -0.0638373  23  GLU   B CB   
132  C CG   . GLU   A 11  ? 1.18797  0.893046 0.661007 -0.10144    -0.0621686  -0.0945464  23  GLU   B CG   
133  C CD   . GLU   A 11  ? 1.32915  1.02357  0.800729 -0.104094   -0.0329508  -0.114817   23  GLU   B CD   
134  O OE1  . GLU   A 11  ? 1.30297  0.982011 0.734232 -0.100764   0.00488116  -0.107948   23  GLU   B OE1  
135  O OE2  . GLU   A 11  ? 1.31826  1.02005  0.8372   -0.109237   -0.0473031  -0.136694   23  GLU   B OE2  
136  H H    . GLU   A 11  ? 0.942532 0.629984 0.367446 -0.0942241  -0.0237013  -0.016201   23  GLU   B H    
137  H HA   . GLU   A 11  ? 0.970736 0.667347 0.387245 -0.0858616  -0.0995283  -0.0545515  23  GLU   B HA   
138  H HB2  . GLU   A 11  ? 1.05734  0.732883 0.443431 -0.0929003  -0.0293423  -0.0623967  23  GLU   B HB2  
139  H HB3  . GLU   A 11  ? 0.958386 0.670869 0.444637 -0.103744   -0.0207215  -0.0556283  23  GLU   B HB3  
140  H HG2  . GLU   A 11  ? 1.10611  0.834816 0.641065 -0.106307   -0.0725937  -0.092055   23  GLU   B HG2  
141  H HG3  . GLU   A 11  ? 1.20607  0.898406 0.641165 -0.0960913  -0.08831    -0.105083   23  GLU   B HG3  
142  N N    . ASP   A 12  ? 0.80307  0.563099 0.378026 -0.0961317  -0.123701   -0.0564679  24  ASP   B N    
143  C CA   . ASP   A 12  ? 0.715616 0.512374 0.381657 -0.0998244  -0.132502   -0.0531618  24  ASP   B CA   
144  C C    . ASP   A 12  ? 0.714849 0.517549 0.420901 -0.110204   -0.115367   -0.069055   24  ASP   B C    
145  O O    . ASP   A 12  ? 0.755757 0.545473 0.450489 -0.114405   -0.131311   -0.0934667  24  ASP   B O    
146  C CB   . ASP   A 12  ? 0.712714 0.525621 0.408835 -0.0963813  -0.176056   -0.0584733  24  ASP   B CB   
147  C CG   . ASP   A 12  ? 0.641185 0.49435  0.437833 -0.0989275  -0.177833   -0.0492951  24  ASP   B CG   
148  O OD1  . ASP   A 12  ? 0.612423 0.477065 0.447062 -0.102978   -0.147088   -0.042249   24  ASP   B OD1  
149  O OD2  . ASP   A 12  ? 0.653872 0.528802 0.492956 -0.0948177  -0.208913   -0.0464689  24  ASP   B OD2  
150  H H    . ASP   A 12  ? 0.849596 0.596254 0.386699 -0.0923278  -0.143612   -0.0663204  24  ASP   B H    
151  H HA   . ASP   A 12  ? 0.688112 0.494179 0.371662 -0.0969774  -0.119191   -0.0368638  24  ASP   B HA   
152  H HB2  . ASP   A 12  ? 0.737187 0.543636 0.402424 -0.0875876  -0.18803    -0.0480952  24  ASP   B HB2  
153  H HB3  . ASP   A 12  ? 0.750189 0.552871 0.430754 -0.0998489  -0.192717   -0.0780223  24  ASP   B HB3  
154  N N    . ILE   A 13  ? 0.625257 0.441778 0.368528 -0.112369   -0.0852492  -0.0573926  25  ILE   B N    
155  C CA   . ILE   A 13  ? 0.660511 0.481702 0.443601 -0.119198   -0.0676324  -0.0680272  25  ILE   B CA   
156  C C    . ILE   A 13  ? 0.574502 0.425308 0.441331 -0.120625   -0.0702947  -0.0587666  25  ILE   B C    
157  O O    . ILE   A 13  ? 0.582334 0.438194 0.488339 -0.123675   -0.0527048  -0.0595225  25  ILE   B O    
158  C CB   . ILE   A 13  ? 0.608311 0.423823 0.376879 -0.119256   -0.0327983  -0.0630191  25  ILE   B CB   
159  C CG1  . ILE   A 13  ? 0.6155   0.448197 0.401512 -0.114313   -0.0226781  -0.0405394  25  ILE   B CG1  
160  C CG2  . ILE   A 13  ? 0.707484 0.493064 0.401768 -0.118694   -0.0217798  -0.0717578  25  ILE   B CG2  
161  C CD1  . ILE   A 13  ? 0.592297 0.427664 0.383874 -0.115031   0.00422844  -0.0356525  25  ILE   B CD1  
162  H H    . ILE   A 13  ? 0.626747 0.448846 0.370629 -0.108363   -0.0769938  -0.0426899  25  ILE   B H    
163  H HA   . ILE   A 13  ? 0.669045 0.475471 0.435153 -0.122296   -0.0770656  -0.0862413  25  ILE   B HA   
164  H HB   . ILE   A 13  ? 0.618963 0.438683 0.418245 -0.121807   -0.0234798  -0.0690136  25  ILE   B HB   
165  H HG12 . ILE   A 13  ? 0.617473 0.442527 0.374011 -0.11156    -0.0305029  -0.0346856  25  ILE   B HG12 
166  H HG13 . ILE   A 13  ? 0.57607  0.426376 0.401728 -0.11184    -0.0280342  -0.0339636  25  ILE   B HG13 
167  H HG21 . ILE   A 13  ? 0.683732 0.469627 0.381694 -0.119737   0.00114774  -0.0691121  25  ILE   B HG21 
168  H HG22 . ILE   A 13  ? 0.708635 0.487909 0.372118 -0.115581   -0.0284122  -0.0623557  25  ILE   B HG22 
169  H HG23 . ILE   A 13  ? 0.729305 0.501003 0.403921 -0.119276   -0.0303956  -0.0887878  25  ILE   B HG23 
170  H HD11 . ILE   A 13  ? 0.58285  0.42386  0.400503 -0.11626    0.0122855   -0.0410439  25  ILE   B HD11 
171  H HD12 . ILE   A 13  ? 0.570042 0.416386 0.375358 -0.111045   0.00475956  -0.0244063  25  ILE   B HD12 
172  H HD13 . ILE   A 13  ? 0.618167 0.438437 0.37552  -0.117345   0.0127551   -0.0381555  25  ILE   B HD13 
173  N N    . THR   A 14  ? 0.630803 0.50127  0.530088 -0.117159   -0.0904721  -0.0483085  26  THR   B N    
174  C CA   . THR   A 14  ? 0.53651  0.435811 0.520813 -0.118121   -0.0875899  -0.0364507  26  THR   B CA   
175  C C    . THR   A 14  ? 0.615472 0.510648 0.64281  -0.130857   -0.108777   -0.0574711  26  THR   B C    
176  O O    . THR   A 14  ? 0.615466 0.492273 0.605126 -0.134908   -0.138383   -0.0805762  26  THR   B O    
177  C CB   . THR   A 14  ? 0.490664 0.415684 0.50291  -0.107842   -0.0963035  -0.0162919  26  THR   B CB   
178  O OG1  . THR   A 14  ? 0.495817 0.416804 0.491498 -0.108772   -0.13257    -0.0274623  26  THR   B OG1  
179  C CG2  . THR   A 14  ? 0.497771 0.420362 0.466645 -0.0943992  -0.0799318  -0.00033605 26  THR   B CG2  
180  H H    . THR   A 14  ? 0.616544 0.483116 0.48807  -0.113214   -0.10441    -0.0465855  26  THR   B H    
181  H HA   . THR   A 14  ? 0.52731  0.430664 0.524715 -0.116145   -0.0653691  -0.0278965  26  THR   B HA   
182  H HB   . THR   A 14  ? 0.474023 0.41926  0.544623 -0.107637   -0.0899978  -0.0060691  26  THR   B HB   
184  H HG21 . THR   A 14  ? 0.485315 0.422501 0.473222 -0.0861019  -0.0849305  0.010793    26  THR   B HG21 
185  H HG22 . THR   A 14  ? 0.513612 0.416324 0.431435 -0.0955213  -0.0850564  -0.00766539 26  THR   B HG22 
186  H HG23 . THR   A 14  ? 0.471789 0.396996 0.446202 -0.0921752  -0.0595343  0.00591502  26  THR   B HG23 
187  N N    . SER   A 15  ? 0.543135 0.454726 0.65002  -0.135646   -0.0963369  -0.0480736  27  SER   B N    
188  C CA   . SER   A 15  ? 0.584099 0.490907 0.749749 -0.150173   -0.117557   -0.0677096  27  SER   B CA   
189  C C    . SER   A 15  ? 0.554891 0.482099 0.760933 -0.153834   -0.155588   -0.0711268  27  SER   B C    
190  O O    . SER   A 15  ? 0.612965 0.526486 0.820713 -0.163689   -0.192154   -0.100217   27  SER   B O    
191  C CB   . SER   A 15  ? 0.556626 0.474366 0.804357 -0.154304   -0.092165   -0.0508807  27  SER   B CB   
192  O OG   . SER   A 15  ? 0.551244 0.453625 0.765498 -0.14797    -0.0605215  -0.0457906  27  SER   B OG   
193  H H    . SER   A 15  ? 0.529078 0.453152 0.654038 -0.129553   -0.0749239  -0.0292474  27  SER   B H    
194  H HA   . SER   A 15  ? 0.604167 0.485021 0.729699 -0.154301   -0.125326   -0.0910977  27  SER   B HA   
195  H HB2  . SER   A 15  ? 0.533495 0.476484 0.819737 -0.148985   -0.0828458  -0.0273425  27  SER   B HB2  
196  H HB3  . SER   A 15  ? 0.578545 0.488714 0.86794  -0.165644   -0.106696   -0.0658891  27  SER   B HB3  
198  N N    . LYS   A 16  ? 0.591476 0.551781 0.829613 -0.143579   -0.147788   -0.0422574  28  LYS   B N    
199  C CA   . LYS   A 16  ? 0.588123 0.57753  0.885979 -0.144486   -0.178815   -0.0389492  28  LYS   B CA   
200  C C    . LYS   A 16  ? 0.58686  0.564099 0.808517 -0.137104   -0.215363   -0.0538308  28  LYS   B C    
201  O O    . LYS   A 16  ? 0.545132 0.543924 0.809156 -0.136968   -0.251628   -0.0565613  28  LYS   B O    
202  C CB   . LYS   A 16  ? 0.58433  0.611074 0.933282 -0.130174   -0.148528   -0.00045676 28  LYS   B CB   
203  C CG   . LYS   A 16  ? 0.574335 0.617128 0.998895 -0.131978   -0.109502   0.0236897   28  LYS   B CG   
204  C CD   . LYS   A 16  ? 0.645002 0.721545 1.09912  -0.11155    -0.0782017  0.0607295   28  LYS   B CD   
205  C CE   . LYS   A 16  ? 0.782854 0.856209 1.22319  -0.0993816  -0.0306641  0.0854263   28  LYS   B CE   
206  N NZ   . LYS   A 16  ? 0.815758 0.894186 1.33925  -0.111036   -0.0118013  0.0980895   28  LYS   B NZ   
207  H H    . LYS   A 16  ? 0.547049 0.512502 0.770691 -0.134454   -0.1223     -0.0244194  28  LYS   B H    
208  H HA   . LYS   A 16  ? 0.601573 0.594146 0.957577 -0.157233   -0.194494   -0.0505533  28  LYS   B HA   
209  H HB2  . LYS   A 16  ? 0.571059 0.58993  0.860312 -0.118205   -0.135016   0.00700769  28  LYS   B HB2  
210  H HB3  . LYS   A 16  ? 0.582197 0.630785 0.971291 -0.128529   -0.167864   0.00306349  28  LYS   B HB3  
211  H HG2  . LYS   A 16  ? 0.599341 0.649531 1.09209  -0.145147   -0.121454   0.018091    28  LYS   B HG2  
212  H HG3  . LYS   A 16  ? 0.589051 0.611395 0.975918 -0.132068   -0.0919596  0.0211253   28  LYS   B HG3  
213  H HD2  . LYS   A 16  ? 0.651474 0.72674  1.05729  -0.100698   -0.0861344  0.0595311   28  LYS   B HD2  
214  H HD3  . LYS   A 16  ? 0.649763 0.752292 1.1819   -0.115015   -0.0822062  0.0702956   28  LYS   B HD3  
215  H HE2  . LYS   A 16  ? 0.750005 0.799702 1.12399  -0.0981117  -0.0290594  0.0745302   28  LYS   B HE2  
216  H HE3  . LYS   A 16  ? 0.741229 0.831325 1.18144  -0.0830472  -0.0131263  0.104909    28  LYS   B HE3  
217  H HZ1  . LYS   A 16  ? 0.814359 0.874011 1.33649  -0.12516    -0.0273155  0.0782442   28  LYS   B HZ1  
218  H HZ2  . LYS   A 16  ? 0.804114 0.90571  1.39654  -0.113661   -0.0119646  0.10929     28  LYS   B HZ2  
219  H HZ3  . LYS   A 16  ? 0.797805 0.874127 1.30745  -0.100808   0.0160712   0.115271    28  LYS   B HZ3  
220  N N    . LYS   A 17  ? 0.630121 0.573489 0.745633 -0.130751   -0.205469   -0.0616239  29  LYS   B N    
221  C CA   . LYS   A 17  ? 0.710664 0.635137 0.741325 -0.121403   -0.232501   -0.0698649  29  LYS   B CA   
222  C C    . LYS   A 17  ? 0.626235 0.579383 0.683004 -0.106899   -0.240466   -0.0448045  29  LYS   B C    
223  O O    . LYS   A 17  ? 0.652817 0.612478 0.709913 -0.102366   -0.280817   -0.0507632  29  LYS   B O    
224  C CB   . LYS   A 17  ? 0.74784  0.654823 0.754388 -0.127668   -0.282564   -0.103099   29  LYS   B CB   
225  C CG   . LYS   A 17  ? 0.803033 0.671902 0.761177 -0.136927   -0.278978   -0.134211   29  LYS   B CG   
226  C CD   . LYS   A 17  ? 0.796932 0.636807 0.66543  -0.12982    -0.238049   -0.127656   29  LYS   B CD   
227  C CE   . LYS   A 17  ? 0.903871 0.705204 0.717218 -0.134269   -0.233141   -0.159176   29  LYS   B CE   
228  N NZ   . LYS   A 17  ? 0.893512 0.684726 0.677037 -0.131662   -0.182917   -0.145838   29  LYS   B NZ   
229  H H    . LYS   A 17  ? 0.617146 0.549267 0.714759 -0.131561   -0.179708   -0.0594749  29  LYS   B H    
230  H HA   . LYS   A 17  ? 0.68768  0.590549 0.655321 -0.117642   -0.21299    -0.0687104  29  LYS   B HA   
231  H HB2  . LYS   A 17  ? 0.752848 0.682723 0.831789 -0.133645   -0.30379    -0.105923   29  LYS   B HB2  
232  H HB3  . LYS   A 17  ? 0.78793  0.685646 0.739127 -0.117778   -0.299343   -0.101808   29  LYS   B HB3  
233  H HG2  . LYS   A 17  ? 0.776401 0.653029 0.796924 -0.147226   -0.270166   -0.138117   29  LYS   B HG2  
234  H HG3  . LYS   A 17  ? 0.851688 0.706097 0.778121 -0.136791   -0.312922   -0.155975   29  LYS   B HG3  
235  H HD2  . LYS   A 17  ? 0.828831 0.661776 0.64357  -0.120108   -0.242679   -0.118773   29  LYS   B HD2  
236  H HD3  . LYS   A 17  ? 0.76171  0.615098 0.663329 -0.13047    -0.208333   -0.109943   29  LYS   B HD3  
237  H HE2  . LYS   A 17  ? 0.895073 0.698167 0.759246 -0.14367    -0.242236   -0.174431   29  LYS   B HE2  
238  H HE3  . LYS   A 17  ? 0.950973 0.731669 0.698655 -0.128241   -0.25329    -0.172848   29  LYS   B HE3  
239  H HZ1  . LYS   A 17  ? 0.842593 0.649989 0.682054 -0.136117   -0.166677   -0.135948   29  LYS   B HZ1  
240  H HZ2  . LYS   A 17  ? 0.881232 0.673029 0.6306   -0.12484    -0.173937   -0.129939   29  LYS   B HZ2  
241  H HZ3  . LYS   A 17  ? 0.921452 0.689194 0.666005 -0.131657   -0.176858   -0.163273   29  LYS   B HZ3  
242  N N    . ASP   A 18  ? 0.578813 0.546313 0.651872 -0.0971696  -0.203519   -0.018689   30  ASP   B N    
243  C CA   . ASP   A 18  ? 0.559752 0.550162 0.65479  -0.0798773  -0.204856   0.00380635  30  ASP   B CA   
244  C C    . ASP   A 18  ? 0.587075 0.548129 0.593547 -0.0670232  -0.189143   0.0125255   30  ASP   B C    
245  O O    . ASP   A 18  ? 0.569354 0.542115 0.587977 -0.0505197  -0.180199   0.0311447   30  ASP   B O    
246  C CB   . ASP   A 18  ? 0.522331 0.548388 0.702111 -0.0749691  -0.173004   0.0259339   30  ASP   B CB   
247  C CG   . ASP   A 18  ? 0.482871 0.496125 0.636867 -0.0745773  -0.129952   0.0331234   30  ASP   B CG   
248  O OD1  . ASP   A 18  ? 0.481764 0.46174  0.552181 -0.0743717  -0.121454   0.0252327   30  ASP   B OD1  
249  O OD2  . ASP   A 18  ? 0.443476 0.481041 0.663085 -0.0731286  -0.104473   0.0489383   30  ASP   B OD2  
250  H H    . ASP   A 18  ? 0.557806 0.519209 0.62571  -0.0998446  -0.177374   -0.0159183  30  ASP   B H    
251  H HA   . ASP   A 18  ? 0.588802 0.588957 0.701407 -0.0784416  -0.236005   -0.00062852 30  ASP   B HA   
252  H HB2  . ASP   A 18  ? 0.512645 0.553089 0.705303 -0.0610013  -0.17111    0.0400604   30  ASP   B HB2  
253  H HB3  . ASP   A 18  ? 0.514612 0.559322 0.758861 -0.0843846  -0.182192   0.0227968   30  ASP   B HB3  
254  N N    . ARG   A 19  ? 0.601323 0.524707 0.527052 -0.0740985  -0.185498   -0.00097517 31  ARG   B N    
255  C CA   . ARG   A 19  ? 0.643934 0.536118 0.492616 -0.066335   -0.169839   0.00732801  31  ARG   B CA   
256  C C    . ARG   A 19  ? 0.633182 0.530979 0.496231 -0.059727   -0.134519   0.021903    31  ARG   B C    
257  O O    . ARG   A 19  ? 0.598994 0.474669 0.418258 -0.0526447  -0.123699   0.0297329   31  ARG   B O    
258  C CB   . ARG   A 19  ? 0.714066 0.594757 0.526415 -0.0525733  -0.198079   0.0157034   31  ARG   B CB   
259  C CG   . ARG   A 19  ? 0.735976 0.603235 0.509025 -0.055639   -0.236514   -0.00070305 31  ARG   B CG   
260  C CD   . ARG   A 19  ? 0.862668 0.714537 0.588083 -0.0388112  -0.265652   0.0107239   31  ARG   B CD   
261  N NE   . ARG   A 19  ? 0.880796 0.69877  0.545381 -0.0309663  -0.238285   0.0293882   31  ARG   B NE   
262  C CZ   . ARG   A 19  ? 0.898444 0.675192 0.478491 -0.0335668  -0.223299   0.0305604   31  ARG   B CZ   
263  N NH1  . ARG   A 19  ? 0.955668 0.716745 0.488523 -0.0419747  -0.226418   0.0124241   31  ARG   B NH1  
264  N NH2  . ARG   A 19  ? 1.02221  0.770091 0.565084 -0.0274171  -0.201088   0.050495    31  ARG   B NH2  
265  H H    . ARG   A 19  ? 0.622213 0.538397 0.543963 -0.0843095  -0.191845   -0.015946   31  ARG   B H    
266  H HA   . ARG   A 19  ? 0.666328 0.537146 0.472453 -0.0741092  -0.164656   -0.00325221 31  ARG   B HA   
267  H HB2  . ARG   A 19  ? 0.686136 0.589559 0.544613 -0.0437727  -0.204815   0.0252252   31  ARG   B HB2  
268  H HB3  . ARG   A 19  ? 0.710313 0.568459 0.478314 -0.0481333  -0.18492    0.0235138   31  ARG   B HB3  
269  H HG2  . ARG   A 19  ? 0.777971 0.622953 0.505437 -0.0630944  -0.226404   -0.0111013  31  ARG   B HG2  
270  H HG3  . ARG   A 19  ? 0.751308 0.641069 0.575696 -0.0609392  -0.253433   -0.0100933  31  ARG   B HG3  
271  H HD2  . ARG   A 19  ? 0.892662 0.731123 0.578335 -0.0397912  -0.288613   -0.00127149 31  ARG   B HD2  
272  H HD3  . ARG   A 19  ? 0.833283 0.710221 0.609701 -0.0308934  -0.280941   0.0182615   31  ARG   B HD3  
273  H HE   . ARG   A 19  ? 0.85199  0.67704  0.541566 -0.023844   -0.229685   0.0413384   31  ARG   B HE   
274  H HH11 . ARG   A 19  ? 0.931062 0.706852 0.493134 -0.0505559  -0.229502   -0.00317458 31  ARG   B HH11 
275  H HH12 . ARG   A 19  ? 0.997693 0.731783 0.468354 -0.0382162  -0.224098   0.0158689   31  ARG   B HH12 
276  H HH21 . ARG   A 19  ? 0.970727 0.723026 0.537016 -0.0191705  -0.201387   0.0618092   31  ARG   B HH21 
277  H HH22 . ARG   A 19  ? 1.00805  0.731646 0.50564  -0.031521   -0.185218   0.0523919   31  ARG   B HH22 
278  N N    . GLY   A 20  ? 0.537245 0.458826 0.454641 -0.062471   -0.115055   0.0242627   32  GLY   B N    
279  C CA   . GLY   A 20  ? 0.49341  0.419998 0.415805 -0.051633   -0.0867579  0.0364961   32  GLY   B CA   
280  C C    . GLY   A 20  ? 0.500904 0.401876 0.373598 -0.0583491  -0.0688954  0.0297586   32  GLY   B C    
281  O O    . GLY   A 20  ? 0.498835 0.396086 0.361016 -0.0492191  -0.0541146  0.0352718   32  GLY   B O    
282  H H    . GLY   A 20  ? 0.540836 0.47354  0.490304 -0.0703725  -0.119869   0.0180323   32  GLY   B H    
283  H HA2  . GLY   A 20  ? 0.506773 0.43319  0.424663 -0.0394775  -0.0894836  0.044537    32  GLY   B HA2  
284  H HA3  . GLY   A 20  ? 0.478398 0.425977 0.444677 -0.0503993  -0.0764846  0.0416942   32  GLY   B HA3  
285  N N    . VAL   A 21  ? 0.524395 0.410013 0.372877 -0.0734067  -0.0702869  0.0163081   33  VAL   B N    
286  C CA   . VAL   A 21  ? 0.52181  0.388129 0.3353   -0.0804981  -0.0525018  0.0108708   33  VAL   B CA   
287  C C    . VAL   A 21  ? 0.543647 0.382907 0.305381 -0.0894095  -0.0595673  0.00116471  33  VAL   B C    
288  O O    . VAL   A 21  ? 0.575151 0.413547 0.337328 -0.0960828  -0.0682339  -0.0118706  33  VAL   B O    
289  C CB   . VAL   A 21  ? 0.543964 0.423163 0.388163 -0.0857795  -0.0348967  0.00662201  33  VAL   B CB   
290  C CG1  . VAL   A 21  ? 0.463274 0.327559 0.2806   -0.0917406  -0.0187074  0.00190446  33  VAL   B CG1  
291  C CG2  . VAL   A 21  ? 0.565252 0.470422 0.454018 -0.0733564  -0.0263362  0.0199476   33  VAL   B CG2  
292  H H    . VAL   A 21  ? 0.532284 0.420041 0.388746 -0.0788697  -0.0829829  0.00947831  33  VAL   B H    
293  H HA   . VAL   A 21  ? 0.524896 0.385089 0.326189 -0.0746814  -0.0473172  0.0168459   33  VAL   B HA   
294  H HB   . VAL   A 21  ? 0.531401 0.41117  0.38599  -0.0925005  -0.0398218  -0.00139059 33  VAL   B HB   
295  H HG11 . VAL   A 21  ? 0.486924 0.345711 0.291518 -0.0874206  -0.0178595  0.00696758  33  VAL   B HG11 
296  H HG12 . VAL   A 21  ? 0.507884 0.357566 0.300636 -0.098781   -0.0188032  -0.00516091 33  VAL   B HG12 
297  H HG13 . VAL   A 21  ? 0.467911 0.342568 0.307619 -0.0920174  -0.00893898 0.00120139  33  VAL   B HG13 
298  H HG21 . VAL   A 21  ? 0.536663 0.44729  0.439608 -0.0748069  -0.0150653  0.0197915   33  VAL   B HG21 
299  H HG22 . VAL   A 21  ? 0.546662 0.464175 0.463313 -0.0717471  -0.0334852  0.0235999   33  VAL   B HG22 
300  H HG23 . VAL   A 21  ? 0.549251 0.452187 0.424298 -0.0644109  -0.0244949  0.0253832   33  VAL   B HG23 
301  N N    . LEU   A 22  ? 0.55964  0.374029 0.276209 -0.0880372  -0.0546529  0.00809109  34  LEU   B N    
302  C CA   . LEU   A 22  ? 0.614116 0.398989 0.271377 -0.0922984  -0.0545814  0.00599159  34  LEU   B CA   
303  C C    . LEU   A 22  ? 0.632264 0.403403 0.275699 -0.101291   -0.0249553  0.00669062  34  LEU   B C    
304  O O    . LEU   A 22  ? 0.615126 0.389477 0.281962 -0.102557   -0.013443   0.0130603   34  LEU   B O    
305  C CB   . LEU   A 22  ? 0.644669 0.411864 0.268431 -0.0816753  -0.0728705  0.0196076   34  LEU   B CB   
306  C CG   . LEU   A 22  ? 0.691393 0.478085 0.340475 -0.0716851  -0.104103   0.0197899   34  LEU   B CG   
307  C CD1  . LEU   A 22  ? 0.72165  0.492391 0.348836 -0.0578826  -0.116809   0.03713     34  LEU   B CD1  
308  C CD2  . LEU   A 22  ? 0.698207 0.485832 0.330893 -0.0752147  -0.127297   0.00337725  34  LEU   B CD2  
309  H H    . LEU   A 22  ? 0.551536 0.365853 0.274391 -0.0834597  -0.0499871  0.0151163   34  LEU   B H    
310  H HA   . LEU   A 22  ? 0.629416 0.415749 0.281182 -0.0949782  -0.0621809  -0.00483265 34  LEU   B HA   
311  H HB2  . LEU   A 22  ? 0.647694 0.4096   0.277811 -0.0790803  -0.0649497  0.0286932   34  LEU   B HB2  
312  H HB3  . LEU   A 22  ? 0.699019 0.444436 0.276771 -0.0827055  -0.0712669  0.0207952   34  LEU   B HB3  
313  H HG   . LEU   A 22  ? 0.637274 0.447167 0.33368  -0.0707367  -0.101215   0.0191775   34  LEU   B HG   
314  H HD11 . LEU   A 22  ? 0.70071  0.470549 0.34359  -0.0552031  -0.104615   0.0435727   34  LEU   B HD11 
315  H HD12 . LEU   A 22  ? 0.722418 0.50808  0.369563 -0.0504632  -0.137783   0.037878    34  LEU   B HD12 
316  H HD13 . LEU   A 22  ? 0.763051 0.508365 0.341431 -0.0578601  -0.116256   0.0416093   34  LEU   B HD13 
317  H HD21 . LEU   A 22  ? 0.686627 0.483018 0.339904 -0.0833795  -0.118386   -0.00806362 34  LEU   B HD21 
318  H HD22 . LEU   A 22  ? 0.7514   0.514801 0.329235 -0.0739219  -0.12861    0.00355872  34  LEU   B HD22 
319  H HD23 . LEU   A 22  ? 0.705329 0.507936 0.362712 -0.0695993  -0.149829   0.00405733  34  LEU   B HD23 
320  N N    . LYS   A 23  ? 0.686741 0.44201  0.292626 -0.106502   -0.0131244  -0.00114521 35  LYS   B N    
321  C CA   . LYS   A 23  ? 0.64311  0.39303  0.250316 -0.114927   0.0189751   -0.0012123  35  LYS   B CA   
322  C C    . LYS   A 23  ? 0.734092 0.451771 0.276842 -0.114794   0.0363351   0.00641036  35  LYS   B C    
323  O O    . LYS   A 23  ? 0.807641 0.509443 0.296786 -0.108263   0.0260896   -0.00165499 35  LYS   B O    
324  C CB   . LYS   A 23  ? 0.652068 0.414809 0.279785 -0.1186     0.0302374   -0.0192885  35  LYS   B CB   
325  C CG   . LYS   A 23  ? 0.626258 0.396589 0.282871 -0.125437   0.0620694   -0.0179433  35  LYS   B CG   
326  C CD   . LYS   A 23  ? 0.634859 0.414937 0.312804 -0.125646   0.0748346   -0.0351104  35  LYS   B CD   
327  C CE   . LYS   A 23  ? 0.650461 0.443755 0.367109 -0.129842   0.104572    -0.0331772  35  LYS   B CE   
328  N NZ   . LYS   A 23  ? 0.658169 0.451777 0.382961 -0.126797   0.123631    -0.0490792  35  LYS   B NZ   
329  H H    . LYS   A 23  ? 0.700445 0.448445 0.280015 -0.103707   -0.0253175  -0.00710617 35  LYS   B H    
330  H HA   . LYS   A 23  ? 0.633903 0.390844 0.269449 -0.117382   0.0249434   0.00533483  35  LYS   B HA   
331  H HB2  . LYS   A 23  ? 0.611799 0.392174 0.274205 -0.117383   0.0181056   -0.0240199  35  LYS   B HB2  
332  H HB3  . LYS   A 23  ? 0.68363  0.432116 0.274364 -0.116563   0.0283979   -0.0276265  35  LYS   B HB3  
333  H HG2  . LYS   A 23  ? 0.66537  0.41953  0.294011 -0.127359   0.0774716   -0.0107412  35  LYS   B HG2  
334  H HG3  . LYS   A 23  ? 0.597903 0.382266 0.289852 -0.126817   0.0593979   -0.0123397  35  LYS   B HG3  
335  H HD2  . LYS   A 23  ? 0.608718 0.402707 0.316008 -0.124001   0.0607026   -0.0396045  35  LYS   B HD2  
336  H HD3  . LYS   A 23  ? 0.679854 0.442914 0.318409 -0.123184   0.0763382   -0.0438493  35  LYS   B HD3  
337  H HE2  . LYS   A 23  ? 0.664347 0.447803 0.364542 -0.133001   0.118844    -0.0242536  35  LYS   B HE2  
338  H HE3  . LYS   A 23  ? 0.602602 0.414542 0.36     -0.130647   0.0978312   -0.0290258  35  LYS   B HE3  
339  H HZ1  . LYS   A 23  ? 0.702028 0.476314 0.383493 -0.124277   0.128926    -0.055573   35  LYS   B HZ1  
340  H HZ2  . LYS   A 23  ? 0.638298 0.440488 0.385938 -0.12474    0.111976    -0.0557676  35  LYS   B HZ2  
341  H HZ3  . LYS   A 23  ? 0.652439 0.456026 0.403657 -0.128487   0.141939    -0.0457015  35  LYS   B HZ3  
342  N N    . ILE   A 24  ? 0.748247 0.455981 0.297432 -0.121664   0.0635745   0.0211144   36  ILE   B N    
343  C CA   . ILE   A 24  ? 0.861946 0.544284 0.361879 -0.122498   0.0956317   0.0300592   36  ILE   B CA   
344  C C    . ILE   A 24  ? 0.800775 0.5013   0.354637 -0.133268   0.129319    0.0277672   36  ILE   B C    
345  O O    . ILE   A 24  ? 0.699899 0.417495 0.31522  -0.141875   0.128504    0.0316543   36  ILE   B O    
346  C CB   . ILE   A 24  ? 0.906333 0.556875 0.369172 -0.120401   0.0997977   0.0568206   36  ILE   B CB   
347  C CG1  . ILE   A 24  ? 0.946604 0.585036 0.363996 -0.106932   0.0632259   0.05795     36  ILE   B CG1  
348  C CG2  . ILE   A 24  ? 1.01276  0.634991 0.427209 -0.12057    0.141508    0.075022    36  ILE   B CG2  
349  C CD1  . ILE   A 24  ? 1.03641  0.638413 0.40586  -0.0996606  0.064011    0.0860317   36  ILE   B CD1  
350  H H    . ILE   A 24  ? 0.726358 0.442699 0.311539 -0.125424   0.0628404   0.0256166   36  ILE   B H    
351  H HA   . ILE   A 24  ? 0.87648  0.55073  0.335604 -0.11604    0.0921576   0.0205202   36  ILE   B HA   
352  H HB   . ILE   A 24  ? 0.884593 0.541303 0.390719 -0.1269     0.0989805   0.062671    36  ILE   B HB   
353  H HG12 . ILE   A 24  ? 0.974328 0.610649 0.356008 -0.101016   0.056639    0.0464507   36  ILE   B HG12 
354  H HG13 . ILE   A 24  ? 0.901825 0.558872 0.358052 -0.107012   0.0425884   0.0509865   36  ILE   B HG13 
355  H HG21 . ILE   A 24  ? 1.02733  0.630281 0.433141 -0.12141    0.146494    0.0950268   36  ILE   B HG21 
356  H HG22 . ILE   A 24  ? 1.0477   0.657082 0.404256 -0.110656   0.13995     0.0702354   36  ILE   B HG22 
357  H HG23 . ILE   A 24  ? 0.98483  0.620481 0.435851 -0.128642   0.165367    0.0720043   36  ILE   B HG23 
358  H HD11 . ILE   A 24  ? 1.00881  0.608208 0.414322 -0.106879   0.073645    0.0964682   36  ILE   B HD11 
359  H HD12 . ILE   A 24  ? 1.03345  0.633647 0.38642  -0.0900753  0.0358486   0.0857928   36  ILE   B HD12 
360  H HD13 . ILE   A 24  ? 1.08345  0.664991 0.403063 -0.0961832  0.0830473   0.0947843   36  ILE   B HD13 
361  N N    . VAL   A 25  ? 0.814265 0.510572 0.345157 -0.130957   0.157918    0.0205949   37  VAL   B N    
362  C CA   . VAL   A 25  ? 0.79384  0.507292 0.377073 -0.138933   0.195405    0.0226079   37  VAL   B CA   
363  C C    . VAL   A 25  ? 0.900351 0.594885 0.478432 -0.145969   0.226223    0.0505947   37  VAL   B C    
364  O O    . VAL   A 25  ? 0.890137 0.551887 0.392442 -0.137727   0.243743    0.0641254   37  VAL   B O    
365  C CB   . VAL   A 25  ? 0.856289 0.567238 0.411479 -0.129935   0.219052    0.00516137  37  VAL   B CB   
366  C CG1  . VAL   A 25  ? 0.883471 0.609581 0.485399 -0.133969   0.266679    0.0109414   37  VAL   B CG1  
367  C CG2  . VAL   A 25  ? 0.815215 0.540077 0.385302 -0.125182   0.188853    -0.0212587  37  VAL   B CG2  
368  H H    . VAL   A 25  ? 0.855372 0.537624 0.336559 -0.122949   0.153562    0.0132968   37  VAL   B H    
369  H HA   . VAL   A 25  ? 0.758401 0.495677 0.399679 -0.144447   0.185126    0.0177206   37  VAL   B HA   
370  H HB   . VAL   A 25  ? 0.912462 0.597208 0.399564 -0.122073   0.223891    0.00783     37  VAL   B HB   
371  H HG11 . VAL   A 25  ? 0.825396 0.577121 0.495299 -0.141999   0.261136    0.0114179   37  VAL   B HG11 
372  H HG12 . VAL   A 25  ? 0.917356 0.629025 0.499033 -0.135534   0.290491    0.0286527   37  VAL   B HG12 
373  H HG13 . VAL   A 25  ? 0.896299 0.620761 0.482433 -0.125966   0.279017    -0.00324735 37  VAL   B HG13 
374  H HG21 . VAL   A 25  ? 0.840562 0.561037 0.397286 -0.119546   0.20438     -0.0339901  37  VAL   B HG21 
375  H HG22 . VAL   A 25  ? 0.825846 0.539414 0.361744 -0.121599   0.162933    -0.0246159  37  VAL   B HG22 
376  H HG23 . VAL   A 25  ? 0.761809 0.51046  0.390791 -0.13056    0.18012     -0.021714   37  VAL   B HG23 
377  N N    . LYS   A 26  ? 0.835976 0.549176 0.494047 -0.160485   0.232703    0.0596122   38  LYS   B N    
378  C CA   . LYS   A 26  ? 0.862717 0.556315 0.530138 -0.170377   0.263807    0.087602    38  LYS   B CA   
379  C C    . LYS   A 26  ? 0.862097 0.575017 0.582588 -0.177684   0.311914    0.0941124   38  LYS   B C    
380  O O    . LYS   A 26  ? 0.894894 0.588341 0.604335 -0.181266   0.351294    0.119441    38  LYS   B O    
381  C CB   . LYS   A 26  ? 0.818289 0.51482  0.546479 -0.183391   0.236903    0.0919835   38  LYS   B CB   
382  C CG   . LYS   A 26  ? 0.816841 0.495383 0.503034 -0.174418   0.194492    0.0883127   38  LYS   B CG   
383  C CD   . LYS   A 26  ? 0.865828 0.504338 0.459538 -0.161619   0.195222    0.105429    38  LYS   B CD   
384  C CE   . LYS   A 26  ? 0.903131 0.509974 0.495059 -0.169198   0.223468    0.135681    38  LYS   B CE   
385  N NZ   . LYS   A 26  ? 1.02234  0.587342 0.525164 -0.154226   0.219042    0.156536    38  LYS   B NZ   
386  H H    . LYS   A 26  ? 0.78813  0.524746 0.495161 -0.16409    0.217484    0.0488895   38  LYS   B H    
387  H HA   . LYS   A 26  ? 0.915239 0.579766 0.517082 -0.162846   0.270671    0.0998621   38  LYS   B HA   
388  H HB2  . LYS   A 26  ? 0.775311 0.500083 0.561624 -0.1888     0.227762    0.0789569   38  LYS   B HB2  
389  H HB3  . LYS   A 26  ? 0.851007 0.53342  0.595237 -0.192121   0.257737    0.110404    38  LYS   B HB3  
390  H HG2  . LYS   A 26  ? 0.774119 0.471342 0.462072 -0.168322   0.173994    0.0707922   38  LYS   B HG2  
391  H HG3  . LYS   A 26  ? 0.795295 0.471506 0.518875 -0.181821   0.18297     0.0908894   38  LYS   B HG3  
392  H HD2  . LYS   A 26  ? 0.890222 0.527658 0.441421 -0.153671   0.205816    0.101209    38  LYS   B HD2  
393  H HD3  . LYS   A 26  ? 0.851156 0.485656 0.429927 -0.154968   0.165391    0.10053     38  LYS   B HD3  
394  H HE2  . LYS   A 26  ? 0.895523 0.503298 0.538112 -0.179029   0.213933    0.136747    38  LYS   B HE2  
395  H HE3  . LYS   A 26  ? 0.939345 0.550155 0.542264 -0.174174   0.256836    0.143052    38  LYS   B HE3  
396  H HZ1  . LYS   A 26  ? 0.9873   0.550063 0.484919 -0.14895    0.188962    0.15069     38  LYS   B HZ1  
397  H HZ2  . LYS   A 26  ? 1.03432  0.596512 0.485717 -0.144333   0.225589    0.153931    38  LYS   B HZ2  
398  H HZ3  . LYS   A 26  ? 1.04416  0.587153 0.547979 -0.158905   0.239589    0.178567    38  LYS   B HZ3  
399  N N    . ARG   A 27  ? 0.793768 0.546406 0.58086  -0.179474   0.312039    0.0751371   39  ARG   B N    
400  C CA   . ARG   A 27  ? 0.835646 0.608287 0.671076 -0.181852   0.361888    0.0816826   39  ARG   B CA   
401  C C    . ARG   A 27  ? 0.79412  0.585606 0.622495 -0.167163   0.362373    0.0559377   39  ARG   B C    
402  O O    . ARG   A 27  ? 0.76426  0.575152 0.618847 -0.165555   0.323565    0.0366387   39  ARG   B O    
403  C CB   . ARG   A 27  ? 0.8121   0.618443 0.769812 -0.201735   0.369402    0.0905268   39  ARG   B CB   
404  C CG   . ARG   A 27  ? 0.885026 0.716408 0.905917 -0.204233   0.425351    0.101845    39  ARG   B CG   
405  C CD   . ARG   A 27  ? 0.912073 0.784354 1.07162  -0.225687   0.419444    0.105951    39  ARG   B CD   
406  N NE   . ARG   A 27  ? 0.922062 0.831082 1.12765  -0.22096    0.373747    0.0779023   39  ARG   B NE   
407  C CZ   . ARG   A 27  ? 0.83978  0.783504 1.1429   -0.233105   0.34        0.0689795   39  ARG   B CZ   
408  N NH1  . ARG   A 27  ? 0.814765 0.763897 1.19743  -0.255276   0.344257    0.0825439   39  ARG   B NH1  
409  N NH2  . ARG   A 27  ? 0.719887 0.691408 1.04114  -0.221982   0.302709    0.046894    39  ARG   B NH2  
410  H H    . ARG   A 27  ? 0.758627 0.526419 0.562993 -0.17792    0.282752    0.0597355   39  ARG   B H    
411  H HA   . ARG   A 27  ? 0.887461 0.636589 0.676583 -0.17792    0.3934      0.097669    39  ARG   B HA   
412  H HB2  . ARG   A 27  ? 0.833895 0.62331  0.795956 -0.211682   0.365718    0.104769    39  ARG   B HB2  
413  H HB3  . ARG   A 27  ? 0.768846 0.598099 0.766592 -0.20313    0.337869    0.074462    39  ARG   B HB3  
414  H HG2  . ARG   A 27  ? 0.879708 0.724118 0.892485 -0.19232    0.431485    0.0875837   39  ARG   B HG2  
415  H HG3  . ARG   A 27  ? 0.943708 0.751787 0.926379 -0.2027     0.460529    0.121099    39  ARG   B HG3  
416  H HD2  . ARG   A 27  ? 0.933936 0.821981 1.13996  -0.228627   0.459117    0.117846    39  ARG   B HD2  
417  H HD3  . ARG   A 27  ? 0.916023 0.773647 1.08688  -0.238063   0.40496     0.114795    39  ARG   B HD3  
418  H HE   . ARG   A 27  ? 0.882807 0.789496 1.04585  -0.207941   0.367179    0.0660774   39  ARG   B HE   
419  H HH11 . ARG   A 27  ? 0.860949 0.800592 1.25226  -0.26201    0.380001    0.100735    39  ARG   B HH11 
420  H HH12 . ARG   A 27  ? 0.800725 0.76187  1.22781  -0.262972   0.311061    0.0730659   39  ARG   B HH12 
421  H HH21 . ARG   A 27  ? 0.733881 0.695308 1.00005  -0.209552   0.29403     0.038422    39  ARG   B HH21 
422  H HH22 . ARG   A 27  ? 0.715654 0.715273 1.10518  -0.226807   0.286284    0.0415681   39  ARG   B HH22 
423  N N    . VAL   A 28  ? 0.844056 0.623294 0.626354 -0.153803   0.40574     0.0555376   40  VAL   B N    
424  C CA   . VAL   A 28  ? 0.87258  0.657512 0.635605 -0.13792    0.403286    0.0276925   40  VAL   B CA   
425  C C    . VAL   A 28  ? 0.818265 0.650338 0.693998 -0.141319   0.415517    0.0220996   40  VAL   B C    
426  O O    . VAL   A 28  ? 0.803545 0.658573 0.7515   -0.150415   0.449572    0.0403778   40  VAL   B O    
427  C CB   . VAL   A 28  ? 1.04012  0.789136 0.705534 -0.119561   0.446833    0.0274978   40  VAL   B CB   
428  C CG1  . VAL   A 28  ? 1.01175  0.768785 0.683063 -0.102955   0.469222    0.00186644  40  VAL   B CG1  
429  C CG2  . VAL   A 28  ? 1.11041  0.816113 0.660765 -0.11159    0.414319    0.023049    40  VAL   B CG2  
430  H H    . VAL   A 28  ? 0.903542 0.668565 0.665642 -0.153706   0.438465    0.0728535   40  VAL   B H    
431  H HA   . VAL   A 28  ? 0.853342 0.632751 0.59301  -0.135841   0.366316    0.0142336   40  VAL   B HA   
432  H HB   . VAL   A 28  ? 1.05407  0.801605 0.72925  -0.122922   0.482796    0.0491262   40  VAL   B HB   
433  H HG11 . VAL   A 28  ? 0.980984 0.745749 0.668215 -0.102673   0.435963    -0.0165509  40  VAL   B HG11 
434  H HG12 . VAL   A 28  ? 1.01183  0.794289 0.75009  -0.105406   0.498459    0.00979935  40  VAL   B HG12 
435  H HG13 . VAL   A 28  ? 1.0915   0.819192 0.684355 -0.0890824  0.487653    -0.00388864 40  VAL   B HG13 
436  H HG21 . VAL   A 28  ? 1.1713   0.852206 0.651291 -0.0977309  0.436964    0.020031    40  VAL   B HG21 
437  H HG22 . VAL   A 28  ? 1.10214  0.800536 0.649566 -0.119937   0.407438    0.042307    40  VAL   B HG22 
438  H HG23 . VAL   A 28  ? 1.06547  0.775284 0.617229 -0.110999   0.377596    0.00426306  40  VAL   B HG23 
439  N N    . GLY   A 29  ? 0.879275 0.726033 0.775077 -0.134041   0.385868    -0.00098298 41  GLY   B N    
440  C CA   . GLY   A 29  ? 0.858128 0.748119 0.854604 -0.132382   0.389243    -0.00706696 41  GLY   B CA   
441  C C    . GLY   A 29  ? 0.887425 0.777026 0.883907 -0.115764   0.439672    -0.0149583  41  GLY   B C    
442  O O    . GLY   A 29  ? 0.993974 0.854759 0.922887 -0.10841    0.479641    -0.010154   41  GLY   B O    
443  H H    . GLY   A 29  ? 0.856909 0.685999 0.703926 -0.129356   0.362021    -0.0121778  41  GLY   B H    
444  H HA2  . GLY   A 29  ? 0.823918 0.737077 0.882566 -0.143502   0.390141    0.00554067  41  GLY   B HA2  
445  H HA3  . GLY   A 29  ? 0.810389 0.706355 0.814698 -0.129645   0.357132    -0.018472   41  GLY   B HA3  
446  N N    . ASN   A 30  ? 0.918389 0.836352 0.983279 -0.10638    0.437446    -0.0272474  42  ASN   B N    
447  C CA   . ASN   A 30  ? 1.02063  0.938747 1.09461  -0.0874284  0.485514    -0.037065   42  ASN   B CA   
448  C C    . ASN   A 30  ? 0.969584 0.88605  1.05595  -0.0732887  0.460627    -0.0606864  42  ASN   B C    
449  O O    . ASN   A 30  ? 0.882951 0.817883 1.01023  -0.0793769  0.415175    -0.0600509  42  ASN   B O    
450  C CB   . ASN   A 30  ? 1.07086  1.03567  1.25398  -0.090858   0.524617    -0.0179741  42  ASN   B CB   
451  C CG   . ASN   A 30  ? 1.04425  1.05742  1.33589  -0.101261   0.481402    -0.0133028  42  ASN   B CG   
452  O OD1  . ASN   A 30  ? 1.12218  1.15052  1.45121  -0.0884484  0.461657    -0.0260733  42  ASN   B OD1  
453  N ND2  . ASN   A 30  ? 1.01324  1.04572  1.349    -0.122777   0.461982    0.00362278  42  ASN   B ND2  
454  H H    . ASN   A 30  ? 0.866078 0.802314 0.971071 -0.109994   0.40602     -0.0291304  42  ASN   B H    
455  H HA   . ASN   A 30  ? 1.07134  0.957698 1.07084  -0.0806602  0.508741    -0.0404808  42  ASN   B HA   
456  H HB2  . ASN   A 30  ? 1.09788  1.06502  1.29221  -0.0758033  0.557676    -0.0248154  42  ASN   B HB2  
457  H HB3  . ASN   A 30  ? 1.09456  1.05537  1.2678   -0.100179   0.54473     -0.00172709 42  ASN   B HB3  
458  H HD21 . ASN   A 30  ? 0.975823 1.03787  1.37718  -0.127599   0.438266    0.00518437  42  ASN   B HD21 
459  H HD22 . ASN   A 30  ? 1.0368   1.05087  1.33572  -0.131652   0.471607    0.0127989   42  ASN   B HD22 
460  N N    . GLY   A 31  ? 1.09391  0.984613 1.14221  -0.0528674  0.493372    -0.080649   43  GLY   B N    
461  C CA   . GLY   A 31  ? 1.06732  0.942839 1.11795  -0.0387277  0.474268    -0.105283   43  GLY   B CA   
462  C C    . GLY   A 31  ? 1.04944  0.879018 1.00728  -0.0422791  0.434975    -0.124315   43  GLY   B C    
463  O O    . GLY   A 31  ? 1.1263   0.941018 1.02234  -0.0546741  0.417004    -0.117126   43  GLY   B O    
464  H H    . GLY   A 31  ? 1.12267  1.0026   1.14219  -0.0468158  0.530448    -0.0787408  43  GLY   B H    
465  H HA2  . GLY   A 31  ? 1.10652  0.973134 1.15592  -0.0232121  0.507809    -0.116306   43  GLY   B HA2  
466  H HA3  . GLY   A 31  ? 1.01063  0.915121 1.13064  -0.0410618  0.454074    -0.0983273  43  GLY   B HA3  
467  N N    . GLU   A 32  ? 1.07189  0.878498 1.02706  -0.030847   0.421977    -0.148565   44  GLU   B N    
468  C CA   . GLU   A 32  ? 1.04171  0.809675 0.930943 -0.0358295  0.382067    -0.167784   44  GLU   B CA   
469  C C    . GLU   A 32  ? 0.907428 0.699233 0.860164 -0.0465611  0.337408    -0.154847   44  GLU   B C    
470  O O    . GLU   A 32  ? 0.852598 0.628513 0.771488 -0.0563494  0.301126    -0.158781   44  GLU   B O    
471  C CB   . GLU   A 32  ? 1.10368  0.823801 0.941551 -0.0168631  0.401152    -0.204748   44  GLU   B CB   
472  H H    . GLU   A 32  ? 1.05827  0.873676 1.05928  -0.01986    0.438092    -0.152932   44  GLU   B H    
473  H HA   . GLU   A 32  ? 1.05269  0.810347 0.886473 -0.0433923  0.37532     -0.16341    44  GLU   B HA   
476  N N    . GLU   A 33  ? 0.878127 0.709381 0.922571 -0.0430574  0.338662    -0.13759    45  GLU   B N    
477  C CA   . GLU   A 33  ? 0.785066 0.630402 0.875416 -0.0466841  0.300269    -0.126222   45  GLU   B CA   
478  C C    . GLU   A 33  ? 0.754277 0.616697 0.826984 -0.0634255  0.267998    -0.107281   45  GLU   B C    
479  O O    . GLU   A 33  ? 0.658538 0.543703 0.734843 -0.0713575  0.273358    -0.0930253  45  GLU   B O    
480  C CB   . GLU   A 33  ? 0.757583 0.636512 0.940597 -0.0330789  0.308061    -0.113008   45  GLU   B CB   
481  H H    . GLU   A 33  ? 0.867501 0.717636 0.946039 -0.0372297  0.363511    -0.131654   45  GLU   B H    
482  H HA   . GLU   A 33  ? 0.813614 0.630951 0.883654 -0.0449272  0.290044    -0.140817   45  GLU   B HA   
485  N N    . THR   A 34  ? 0.702251 0.553644 0.76364  -0.0684256  0.234923    -0.10623    46  THR   B N    
486  C CA   . THR   A 34  ? 0.634566 0.504665 0.692812 -0.0784198  0.204909    -0.0872271  46  THR   B CA   
487  C C    . THR   A 34  ? 0.663993 0.550804 0.774733 -0.0707376  0.186314    -0.0720042  46  THR   B C    
488  O O    . THR   A 34  ? 0.641472 0.519997 0.786767 -0.0603066  0.193599    -0.0754154  46  THR   B O    
489  C CB   . THR   A 34  ? 0.669885 0.513075 0.663565 -0.088577   0.185986    -0.0962087  46  THR   B CB   
490  O OG1  . THR   A 34  ? 0.622485 0.44215  0.626204 -0.0843516  0.179871    -0.111232   46  THR   B OG1  
491  C CG2  . THR   A 34  ? 0.674617 0.496279 0.603394 -0.0920157  0.203861    -0.10831    46  THR   B CG2  
492  H H    . THR   A 34  ? 0.7223   0.552724 0.779967 -0.0648581  0.232321    -0.118323   46  THR   B H    
493  H HA   . THR   A 34  ? 0.641376 0.530245 0.706797 -0.0818009  0.209433    -0.0778146  46  THR   B HA   
494  H HB   . THR   A 34  ? 0.616174 0.470948 0.609765 -0.0933586  0.167192    -0.083775   46  THR   B HB   
496  H HG21 . THR   A 34  ? 0.698415 0.50612  0.58699  -0.0974464  0.187111    -0.111395   46  THR   B HG21 
497  H HG22 . THR   A 34  ? 0.723596 0.528422 0.642928 -0.085369   0.220869    -0.123698   46  THR   B HG22 
498  H HG23 . THR   A 34  ? 0.678487 0.516118 0.615212 -0.0942515  0.21543     -0.0970389  46  THR   B HG23 
499  N N    . PRO   A 35  ? 0.587893 0.499102 0.708652 -0.0721317  0.164662    -0.0524101  47  PRO   B N    
500  C CA   . PRO   A 35  ? 0.524833 0.452731 0.690346 -0.0588994  0.152933    -0.0344585  47  PRO   B CA   
501  C C    . PRO   A 35  ? 0.482226 0.387724 0.646281 -0.0577149  0.145173    -0.0318931  47  PRO   B C    
502  O O    . PRO   A 35  ? 0.545405 0.436261 0.673803 -0.0689293  0.134558    -0.0376355  47  PRO   B O    
503  C CB   . PRO   A 35  ? 0.451135 0.404767 0.609539 -0.0593562  0.130775    -0.0184694  47  PRO   B CB   
504  C CG   . PRO   A 35  ? 0.513448 0.457868 0.625888 -0.075729   0.13023     -0.0283359  47  PRO   B CG   
505  C CD   . PRO   A 35  ? 0.538108 0.461421 0.63164  -0.0824561  0.154535    -0.0462114  47  PRO   B CD   
506  H HA   . PRO   A 35  ? 0.517476 0.45455  0.718322 -0.0499206  0.163794    -0.0335792  47  PRO   B HA   
507  H HB2  . PRO   A 35  ? 0.466415 0.419154 0.619835 -0.0547965  0.118851    -0.00801245 47  PRO   B HB2  
508  H HB3  . PRO   A 35  ? 0.466255 0.440981 0.6542   -0.0527812  0.129561    -0.0129162  47  PRO   B HB3  
509  H HG2  . PRO   A 35  ? 0.494698 0.429624 0.580441 -0.079018   0.118597    -0.0262096  47  PRO   B HG2  
510  H HG3  . PRO   A 35  ? 0.488597 0.449611 0.609039 -0.0774077  0.124831    -0.0241047  47  PRO   B HG3  
511  H HD2  . PRO   A 35  ? 0.56026  0.465942 0.613189 -0.0899958  0.15091     -0.0522587  47  PRO   B HD2  
512  H HD3  . PRO   A 35  ? 0.552299 0.486573 0.659161 -0.0840136  0.167122    -0.0469008  47  PRO   B HD3  
513  N N    . MET   A 36  ? 0.49084  0.397239 0.700626 -0.0434078  0.149528    -0.0197357  48  MET   B N    
514  C CA   . MET   A 36  ? 0.478815 0.367699 0.705365 -0.0410156  0.144836    -0.0084454  48  MET   B CA   
515  C C    . MET   A 36  ? 0.460514 0.372516 0.686617 -0.0312224  0.130324    0.0229586   48  MET   B C    
516  O O    . MET   A 36  ? 0.458292 0.398071 0.680372 -0.0205428  0.121603    0.0349521   48  MET   B O    
517  C CB   . MET   A 36  ? 0.530651 0.405022 0.807962 -0.027333   0.160743    -0.00689909 48  MET   B CB   
518  C CG   . MET   A 36  ? 0.619234 0.468324 0.898783 -0.0294653  0.179826    -0.0386453  48  MET   B CG   
519  S SD   . MET   A 36  ? 0.72352  0.523429 0.97943  -0.046486   0.176024    -0.069924   48  MET   B SD   
520  C CE   . MET   A 36  ? 0.784903 0.58242  0.962056 -0.0633169  0.16794     -0.0948312  48  MET   B CE   
521  H H    . MET   A 36  ? 0.486205 0.404957 0.722095 -0.0343728  0.156537    -0.0166195  48  MET   B H    
522  H HA   . MET   A 36  ? 0.498464 0.369208 0.705762 -0.052715   0.141647    -0.0214417  48  MET   B HA   
523  H HB2  . MET   A 36  ? 0.52498  0.419956 0.821905 -0.0142844  0.160494    0.00858528  48  MET   B HB2  
524  H HB3  . MET   A 36  ? 0.5415   0.401758 0.8352   -0.0269772  0.159149    0.00234454  48  MET   B HB3  
525  H HG2  . MET   A 36  ? 0.612948 0.473826 0.871285 -0.0326071  0.184138    -0.0479255  48  MET   B HG2  
526  H HG3  . MET   A 36  ? 0.626047 0.473078 0.942289 -0.0166655  0.190169    -0.0338792  48  MET   B HG3  
527  H HE1  . MET   A 36  ? 0.801027 0.571666 0.961882 -0.0701382  0.162813    -0.115178   48  MET   B HE1  
528  H HE2  . MET   A 36  ? 0.744346 0.559982 0.908799 -0.0685026  0.155055    -0.08048    48  MET   B HE2  
529  H HE3  . MET   A 36  ? 0.778487 0.582319 0.942602 -0.0590952  0.181856    -0.101601   48  MET   B HE3  
530  N N    . ILE   A 37  ? 0.44186  0.342284 0.673567 -0.033427   0.127612    0.0361106   49  ILE   B N    
531  C CA   . ILE   A 37  ? 0.428913 0.346531 0.658433 -0.0190954  0.122047    0.0688653   49  ILE   B CA   
532  C C    . ILE   A 37  ? 0.401124 0.32921  0.657336 0.00484697  0.126543    0.0911622   49  ILE   B C    
533  O O    . ILE   A 37  ? 0.42457  0.336366 0.723282 0.0108788   0.139502    0.093191    49  ILE   B O    
534  C CB   . ILE   A 37  ? 0.507162 0.411357 0.754541 -0.0249965  0.126343    0.0832223   49  ILE   B CB   
535  C CG1  . ILE   A 37  ? 0.512102 0.415148 0.730136 -0.0446932  0.114382    0.0641377   49  ILE   B CG1  
536  C CG2  . ILE   A 37  ? 0.497275 0.416325 0.744968 -0.00354483 0.131214    0.123847    49  ILE   B CG2  
537  C CD1  . ILE   A 37  ? 0.605349 0.501005 0.85602  -0.053029   0.116253    0.0754151   49  ILE   B CD1  
538  H H    . ILE   A 37  ? 0.45817  0.339481 0.695735 -0.0433976  0.129853    0.0243986   49  ILE   B H    
539  H HA   . ILE   A 37  ? 0.421443 0.353544 0.619822 -0.0198299  0.112038    0.0673936   49  ILE   B HA   
540  H HB   . ILE   A 37  ? 0.50684  0.392147 0.787208 -0.0289639  0.134304    0.0789007   49  ILE   B HB   
541  H HG12 . ILE   A 37  ? 0.514766 0.433465 0.701393 -0.0403801  0.107249    0.0680398   49  ILE   B HG12 
542  H HG13 . ILE   A 37  ? 0.53047  0.422186 0.739909 -0.0555487  0.111811    0.0398969   49  ILE   B HG13 
543  H HG21 . ILE   A 37  ? 0.50646  0.419592 0.771234 -0.00826043 0.137278    0.134292    49  ILE   B HG21 
544  H HG22 . ILE   A 37  ? 0.492098 0.427414 0.704182 0.00253417  0.122085    0.12548     49  ILE   B HG22 
545  H HG23 . ILE   A 37  ? 0.513439 0.430697 0.779655 0.0100842   0.137775    0.138034    49  ILE   B HG23 
546  H HD11 . ILE   A 37  ? 0.591838 0.471129 0.880423 -0.0558962  0.123447    0.0752286   49  ILE   B HD11 
547  H HD12 . ILE   A 37  ? 0.573941 0.467326 0.810348 -0.0658387  0.105757    0.0586267   49  ILE   B HD12 
548  H HD13 . ILE   A 37  ? 0.57232  0.481478 0.822593 -0.0421373  0.120776    0.0997435   49  ILE   B HD13 
549  N N    . GLY   A 38  ? 0.412874 0.366263 0.642323 0.0206665   0.113214    0.107193    50  GLY   B N    
550  C CA   . GLY   A 38  ? 0.437709 0.405127 0.682612 0.0479661   0.109451    0.130988    50  GLY   B CA   
551  C C    . GLY   A 38  ? 0.427662 0.419616 0.678953 0.0503482   0.0949352   0.113531    50  GLY   B C    
552  O O    . GLY   A 38  ? 0.431748 0.442399 0.6959   0.0728835   0.0830843   0.128573    50  GLY   B O    
553  H H    . GLY   A 38  ? 0.401403 0.362564 0.60036  0.0157885   0.104184    0.102581    50  GLY   B H    
554  H HA2  . GLY   A 38  ? 0.444787 0.419383 0.665022 0.061049    0.103706    0.150222    50  GLY   B HA2  
555  H HA3  . GLY   A 38  ? 0.448772 0.402199 0.726826 0.0532218   0.121997    0.140405    50  GLY   B HA3  
556  N N    . ASP   A 39  ? 0.418453 0.408071 0.673631 0.028199    0.0998893   0.0832444   51  ASP   B N    
557  C CA   . ASP   A 39  ? 0.458017 0.472137 0.733265 0.0272211   0.0927159   0.0685221   51  ASP   B CA   
558  C C    . ASP   A 39  ? 0.464093 0.502925 0.709364 0.030104    0.0644858   0.0694265   51  ASP   B C    
559  O O    . ASP   A 39  ? 0.46278  0.494178 0.660449 0.0242616   0.0558235   0.0695904   51  ASP   B O    
560  C CB   . ASP   A 39  ? 0.450439 0.455271 0.726888 0.00394808  0.109074    0.0397293   51  ASP   B CB   
561  C CG   . ASP   A 39  ? 0.516951 0.498233 0.823315 0.00303748  0.135682    0.0282086   51  ASP   B CG   
562  O OD1  . ASP   A 39  ? 0.51131  0.48376  0.851183 0.0203676   0.14118     0.0438602   51  ASP   B OD1  
563  O OD2  . ASP   A 39  ? 0.538172 0.503892 0.826488 -0.0136168  0.150629    0.00449209  51  ASP   B OD2  
564  H H    . ASP   A 39  ? 0.423118 0.395965 0.669679 0.0139167   0.108366    0.0724827   51  ASP   B H    
565  H HA   . ASP   A 39  ? 0.459462 0.481119 0.769142 0.0413157   0.0948779   0.076689    51  ASP   B HA   
566  H HB2  . ASP   A 39  ? 0.456155 0.449533 0.698101 -0.00861552 0.107269    0.0334753   51  ASP   B HB2  
567  H HB3  . ASP   A 39  ? 0.455665 0.480358 0.745271 0.00216915  0.104126    0.0335247   51  ASP   B HB3  
568  N N    . LYS   A 40  ? 0.459463 0.527796 0.739697 0.0393311   0.0492778   0.0673415   52  LYS   B N    
569  C CA   . LYS   A 40  ? 0.49398  0.585703 0.759174 0.0392124   0.017717    0.0600769   52  LYS   B CA   
570  C C    . LYS   A 40  ? 0.410625 0.502037 0.681765 0.0101674   0.0259851   0.0361264   52  LYS   B C    
571  O O    . LYS   A 40  ? 0.426095 0.52125  0.73903  0.00030205  0.0482174   0.0273188   52  LYS   B O    
572  C CB   . LYS   A 40  ? 0.469931 0.595825 0.781521 0.0608909   -0.00681797 0.0672811   52  LYS   B CB   
573  C CG   . LYS   A 40  ? 0.542091 0.684457 0.822138 0.0699012   -0.0489253  0.0630928   52  LYS   B CG   
574  C CD   . LYS   A 40  ? 0.655518 0.831469 0.971066 0.095738    -0.0839061  0.0703439   52  LYS   B CD   
575  C CE   . LYS   A 40  ? 0.738886 0.933149 1.04568  0.0913421   -0.127166   0.0497513   52  LYS   B CE   
576  N NZ   . LYS   A 40  ? 0.791025 1.02543  1.15502  0.107134    -0.166541   0.0468265   52  LYS   B NZ   
577  H H    . LYS   A 40  ? 0.471746 0.545848 0.79052  0.0460364   0.0574372   0.069381    52  LYS   B H    
578  H HA   . LYS   A 40  ? 0.476029 0.559432 0.697318 0.0450617   0.00738369  0.0666917   52  LYS   B HA   
579  H HB2  . LYS   A 40  ? 0.503491 0.625702 0.82031  0.0790996   -0.00288874 0.0845794   52  LYS   B HB2  
580  H HB3  . LYS   A 40  ? 0.480066 0.620318 0.838838 0.0522387   0.00032434  0.0572555   52  LYS   B HB3  
581  H HG2  . LYS   A 40  ? 0.536067 0.681506 0.820798 0.0509587   -0.0527527  0.0458066   52  LYS   B HG2  
582  H HG3  . LYS   A 40  ? 0.55819  0.684098 0.785843 0.0780319   -0.0511546  0.0716736   52  LYS   B HG3  
583  H HD2  . LYS   A 40  ? 0.671414 0.840635 0.958241 0.118597    -0.088493   0.089391    52  LYS   B HD2  
584  H HD3  . LYS   A 40  ? 0.637814 0.829454 1.01234  0.0935382   -0.0744522  0.0693372   52  LYS   B HD3  
585  H HE2  . LYS   A 40  ? 0.701797 0.894097 1.02496  0.066902    -0.117775   0.0338923   52  LYS   B HE2  
586  H HE3  . LYS   A 40  ? 0.748473 0.927974 0.99403  0.101513    -0.139618   0.052357    52  LYS   B HE3  
587  H HZ1  . LYS   A 40  ? 0.762538 1.01308  1.18839  0.0985318   -0.153253   0.0449827   52  LYS   B HZ1  
588  H HZ2  . LYS   A 40  ? 0.806217 1.0419   1.15041  0.132053    -0.177863   0.0625958   52  LYS   B HZ2  
589  H HZ3  . LYS   A 40  ? 0.791899 1.03398  1.15127  0.101667    -0.193852   0.031177    52  LYS   B HZ3  
590  N N    . VAL   A 41  ? 0.527417 0.609872 0.752933 -0.00155552 0.0125152   0.0275927   53  VAL   B N    
591  C CA   . VAL   A 41  ? 0.464468 0.538445 0.687564 -0.0283239  0.023877    0.0104146   53  VAL   B CA   
592  C C    . VAL   A 41  ? 0.486427 0.575962 0.716557 -0.0341157  -0.00585424 0.00015542  53  VAL   B C    
593  O O    . VAL   A 41  ? 0.491037 0.58016  0.685746 -0.0202713  -0.0347227  0.00171932  53  VAL   B O    
594  C CB   . VAL   A 41  ? 0.458248 0.499682 0.622292 -0.0373146  0.03559     0.0102973   53  VAL   B CB   
595  C CG1  . VAL   A 41  ? 0.557734 0.585294 0.702703 -0.0600708  0.042259    -0.00264625 53  VAL   B CG1  
596  C CG2  . VAL   A 41  ? 0.456909 0.480636 0.623765 -0.0362386  0.0615674   0.014558    53  VAL   B CG2  
597  H H    . VAL   A 41  ? 0.492386 0.572279 0.685996 0.00896212  -0.00285129 0.0337717   53  VAL   B H    
598  H HA   . VAL   A 41  ? 0.471874 0.54988  0.727763 -0.0350279  0.0426078   0.00639856  53  VAL   B HA   
599  H HB   . VAL   A 41  ? 0.480895 0.520167 0.616753 -0.0270368  0.0208225   0.016806    53  VAL   B HB   
600  H HG11 . VAL   A 41  ? 0.523162 0.553991 0.693852 -0.068628   0.058345    -0.00760165 53  VAL   B HG11 
601  H HG12 . VAL   A 41  ? 0.526089 0.559104 0.66721  -0.0616531  0.0246163   -0.00607562 53  VAL   B HG12 
602  H HG13 . VAL   A 41  ? 0.522916 0.531698 0.634283 -0.0636882  0.0483978   -0.00208318 53  VAL   B HG13 
603  H HG21 . VAL   A 41  ? 0.45775  0.463863 0.593249 -0.0430341  0.0652862   0.013017    53  VAL   B HG21 
604  H HG22 . VAL   A 41  ? 0.461033 0.489208 0.638554 -0.0213496  0.0587392   0.0261408   53  VAL   B HG22 
605  H HG23 . VAL   A 41  ? 0.458662 0.483156 0.649322 -0.0428284  0.0770319   0.00706658  53  VAL   B HG23 
606  N N    . TYR   A 42  ? 0.451766 0.551992 0.726789 -0.054126   0.00293206  -0.010622   54  TYR   B N    
607  C CA   . TYR   A 42  ? 0.418678 0.531198 0.715982 -0.0644773  -0.0249005  -0.0221604  54  TYR   B CA   
608  C C    . TYR   A 42  ? 0.410259 0.49754  0.688717 -0.0902398  -0.00614573 -0.0285081  54  TYR   B C    
609  O O    . TYR   A 42  ? 0.353825 0.436055 0.648293 -0.103089   0.0297902   -0.0257886  54  TYR   B O    
610  C CB   . TYR   A 42  ? 0.488974 0.642036 0.880294 -0.0672121  -0.0302168  -0.0251473  54  TYR   B CB   
611  C CG   . TYR   A 42  ? 0.506579 0.688462 0.930662 -0.0404557  -0.0469716  -0.0163635  54  TYR   B CG   
612  C CD1  . TYR   A 42  ? 0.484146 0.662559 0.909941 -0.0261575  -0.0188289  -0.00314545 54  TYR   B CD1  
613  C CD2  . TYR   A 42  ? 0.57879  0.788501 1.03175  -0.0283093  -0.0942086  -0.0221859  54  TYR   B CD2  
614  C CE1  . TYR   A 42  ? 0.561175 0.761265 1.01478  0.00091503  -0.0344993  0.00879215  54  TYR   B CE1  
615  C CE2  . TYR   A 42  ? 0.671087 0.906188 1.14794  -5.65e-05   -0.113546   -0.0112813  54  TYR   B CE2  
616  C CZ   . TYR   A 42  ? 0.60186  0.832124 1.08052  0.0149598   -0.0819161  0.00649979  54  TYR   B CZ   
617  O OH   . TYR   A 42  ? 0.533074 0.788472 1.03978  0.0441833   -0.105815   0.0189757   54  TYR   B OH   
618  H H    . TYR   A 42  ? 0.444245 0.542663 0.737656 -0.0612986  0.028001    -0.0106976  54  TYR   B H    
619  H HA   . TYR   A 42  ? 0.447689 0.557991 0.715357 -0.0530058  -0.0519664  -0.023835   54  TYR   B HA   
620  H HB2  . TYR   A 42  ? 0.466923 0.620297 0.884324 -0.0787628  0.00031473  -0.0236971  54  TYR   B HB2  
621  H HB3  . TYR   A 42  ? 0.483935 0.644381 0.894811 -0.0757954  -0.0523075  -0.0343526  54  TYR   B HB3  
622  H HD1  . TYR   A 42  ? 0.497024 0.65456  0.900477 -0.0338002  0.00959488  -0.00230782 54  TYR   B HD1  
623  H HD2  . TYR   A 42  ? 0.590528 0.800047 1.04477  -0.0381659  -0.115833   -0.0341085  54  TYR   B HD2  
624  H HE1  . TYR   A 42  ? 0.546698 0.7406   1.00464  0.010105    -0.01439    0.0176867   54  TYR   B HE1  
625  H HE2  . TYR   A 42  ? 0.651814 0.905961 1.14437  0.00971676  -0.149726   -0.0162756  54  TYR   B HE2  
627  N N    . VAL   A 43  ? 0.415233 0.483457 0.655489 -0.0952084  -0.0297104  -0.0365291  55  VAL   B N    
628  C CA   . VAL   A 43  ? 0.429943 0.46952  0.648303 -0.116448   -0.0114559  -0.0381513  55  VAL   B CA   
629  C C    . VAL   A 43  ? 0.423884 0.459621 0.665356 -0.128667   -0.0402849  -0.051064   55  VAL   B C    
630  O O    . VAL   A 43  ? 0.474196 0.522379 0.72315  -0.116772   -0.0798311  -0.0625714  55  VAL   B O    
631  C CB   . VAL   A 43  ? 0.404958 0.410879 0.543554 -0.111337   -0.00297932 -0.0332054  55  VAL   B CB   
632  C CG1  . VAL   A 43  ? 0.442425 0.448608 0.558542 -0.0981882  0.0154629   -0.0237552  55  VAL   B CG1  
633  C CG2  . VAL   A 43  ? 0.490553 0.484709 0.582848 -0.0964004  -0.035131   -0.0387134  55  VAL   B CG2  
634  H H    . VAL   A 43  ? 0.428413 0.499686 0.65423  -0.083688   -0.0563291  -0.0405847  55  VAL   B H    
635  H HA   . VAL   A 43  ? 0.416596 0.46023  0.662068 -0.126742   0.0142619   -0.0341306  55  VAL   B HA   
636  H HB   . VAL   A 43  ? 0.438321 0.427022 0.567146 -0.12486    0.0117986   -0.0321575  55  VAL   B HB   
637  H HG11 . VAL   A 43  ? 0.423838 0.44379  0.546194 -0.0836371  0.00240414  -0.0214079  55  VAL   B HG11 
638  H HG12 . VAL   A 43  ? 0.423962 0.434537 0.562707 -0.104376   0.0366066   -0.0223691  55  VAL   B HG12 
639  H HG13 . VAL   A 43  ? 0.427846 0.41501  0.502631 -0.0975248  0.0190292   -0.0214252  55  VAL   B HG13 
640  H HG21 . VAL   A 43  ? 0.46412  0.440989 0.515406 -0.093159   -0.0270569  -0.0339803  55  VAL   B HG21 
641  H HG22 . VAL   A 43  ? 0.480343 0.467873 0.581052 -0.104112   -0.0493962  -0.0474881  55  VAL   B HG22 
642  H HG23 . VAL   A 43  ? 0.466374 0.476023 0.561996 -0.0811256  -0.0489586  -0.0380331  55  VAL   B HG23 
643  N N    . HIS   A 44  ? 0.398925 0.410805 0.64065  -0.150063   -0.0213533  -0.0490925  56  HIS   B N    
644  C CA   . HIS   A 44  ? 0.472937 0.462594 0.715764 -0.161555   -0.0449792  -0.0601776  56  HIS   B CA   
645  C C    . HIS   A 44  ? 0.466197 0.414078 0.63012  -0.159809   -0.0317699  -0.0533979  56  HIS   B C    
646  O O    . HIS   A 44  ? 0.493692 0.433649 0.626216 -0.159682   -0.00048571 -0.0399648  56  HIS   B O    
647  C CB   . HIS   A 44  ? 0.570517 0.567041 0.895933 -0.189031   -0.0318955  -0.0586769  56  HIS   B CB   
648  C CG   . HIS   A 44  ? 0.573216 0.605188 0.98206  -0.191951   -0.0686815  -0.0745692  56  HIS   B CG   
649  N ND1  . HIS   A 44  ? 0.579396 0.607314 0.971168 -0.179844   -0.121589   -0.0968698  56  HIS   B ND1  
650  C CD2  . HIS   A 44  ? 0.577449 0.651544 1.0822   -0.201057   -0.062295   -0.0721629  56  HIS   B CD2  
651  C CE1  . HIS   A 44  ? 0.639402 0.704916 1.11294  -0.182801   -0.151705   -0.109096   56  HIS   B CE1  
652  N NE2  . HIS   A 44  ? 0.626741 0.723267 1.17715  -0.196769   -0.115511   -0.0930675  56  HIS   B NE2  
653  H H    . HIS   A 44  ? 0.414982 0.421763 0.654527 -0.15679    0.00781343  -0.0402614  56  HIS   B H    
654  H HA   . HIS   A 44  ? 0.480897 0.47625  0.719392 -0.150555   -0.0771521  -0.072087   56  HIS   B HA   
655  H HB2  . HIS   A 44  ? 0.539521 0.544604 0.880548 -0.194178   0.00085839  -0.0464069  56  HIS   B HB2  
656  H HB3  . HIS   A 44  ? 0.566513 0.534828 0.877126 -0.19924    -0.0312616  -0.058806   56  HIS   B HB3  
658  H HD2  . HIS   A 44  ? 0.573389 0.659459 1.10881  -0.207981   -0.0282478  -0.0593435  56  HIS   B HD2  
659  H HE1  . HIS   A 44  ? 0.647623 0.716973 1.12524  -0.17575    -0.191938   -0.126802   56  HIS   B HE1  
661  N N    . TYR   A 45  ? 0.495785 0.416353 0.627278 -0.156442   -0.0571458  -0.0641448  57  TYR   B N    
662  C CA   . TYR   A 45  ? 0.509209 0.392778 0.574134 -0.152895   -0.0451936  -0.0560853  57  TYR   B CA   
663  C C    . TYR   A 45  ? 0.499367 0.347677 0.559088 -0.158633   -0.0664204  -0.0678741  57  TYR   B C    
664  O O    . TYR   A 45  ? 0.556164 0.407326 0.642154 -0.157274   -0.0990925  -0.0880276  57  TYR   B O    
665  C CB   . TYR   A 45  ? 0.510043 0.398173 0.515987 -0.126845   -0.0508113  -0.0539981  57  TYR   B CB   
666  C CG   . TYR   A 45  ? 0.507768 0.396733 0.48929  -0.104704   -0.0854743  -0.0694795  57  TYR   B CG   
667  C CD1  . TYR   A 45  ? 0.506351 0.42476  0.510244 -0.0928066  -0.106761   -0.0777027  57  TYR   B CD1  
668  C CD2  . TYR   A 45  ? 0.489723 0.347427 0.424705 -0.0938777  -0.0976498  -0.0767245  57  TYR   B CD2  
669  C CE1  . TYR   A 45  ? 0.576529 0.491525 0.54644  -0.0696283  -0.139731   -0.0929281  57  TYR   B CE1  
670  C CE2  . TYR   A 45  ? 0.552125 0.40488  0.458377 -0.0720478  -0.127346   -0.0941044  57  TYR   B CE2  
671  C CZ   . TYR   A 45  ? 0.565114 0.446453 0.480274 -0.0578357  -0.147355   -0.101142   57  TYR   B CZ   
672  O OH   . TYR   A 45  ? 0.683602 0.554544 0.552764 -0.0319688  -0.174817   -0.117571   57  TYR   B OH   
673  H H    . TYR   A 45  ? 0.50797  0.432098 0.658393 -0.15506    -0.0831901  -0.0774686  57  TYR   B H    
674  H HA   . TYR   A 45  ? 0.501647 0.379395 0.565954 -0.162779   -0.018883   -0.0435875  57  TYR   B HA   
675  H HB2  . TYR   A 45  ? 0.504466 0.373569 0.475935 -0.125863   -0.0401472  -0.0467397  57  TYR   B HB2  
676  H HB3  . TYR   A 45  ? 0.482156 0.390988 0.498719 -0.123849   -0.0396192  -0.0479543  57  TYR   B HB3  
677  H HD1  . TYR   A 45  ? 0.498306 0.438759 0.53814  -0.0984423  -0.098675   -0.0726088  57  TYR   B HD1  
678  H HD2  . TYR   A 45  ? 0.51178  0.349099 0.434279 -0.100832   -0.0859041  -0.070599   57  TYR   B HD2  
679  H HE1  . TYR   A 45  ? 0.561554 0.496257 0.540324 -0.0589164  -0.155124   -0.0965189  57  TYR   B HE1  
680  H HE2  . TYR   A 45  ? 0.568045 0.398563 0.440443 -0.0622721  -0.131846   -0.0989274  57  TYR   B HE2  
682  N N    . LYS   A 46  ? 0.504605 0.317873 0.522965 -0.160548   -0.0515977  -0.0569052  58  LYS   B N    
683  C CA   . LYS   A 46  ? 0.560026 0.332971 0.554773 -0.157429   -0.0691563  -0.0658885  58  LYS   B CA   
684  C C    . LYS   A 46  ? 0.554886 0.315484 0.480406 -0.135868   -0.0637421  -0.0573473  58  LYS   B C    
685  O O    . LYS   A 46  ? 0.600999 0.366089 0.504893 -0.136642   -0.0399739  -0.0388449  58  LYS   B O    
686  C CB   . LYS   A 46  ? 0.607755 0.345852 0.632866 -0.181712   -0.0541499  -0.0554041  58  LYS   B CB   
687  C CG   . LYS   A 46  ? 0.65452  0.407409 0.76262  -0.206273   -0.052771   -0.0588222  58  LYS   B CG   
688  C CD   . LYS   A 46  ? 0.723778 0.446134 0.863896 -0.230817   -0.0229052  -0.0370731  58  LYS   B CD   
689  C CE   . LYS   A 46  ? 0.739987 0.48427  0.973787 -0.256936   -0.00835434 -0.0320767  58  LYS   B CE   
690  N NZ   . LYS   A 46  ? 0.797786 0.500481 1.06316  -0.278954   0.0143432   -0.0124986  58  LYS   B NZ   
691  H H    . LYS   A 46  ? 0.502414 0.315923 0.505619 -0.16275    -0.0295121  -0.0430854  58  LYS   B H    
692  H HA   . LYS   A 46  ? 0.57149  0.346725 0.575019 -0.151058   -0.094983   -0.0842198  58  LYS   B HA   
693  H HB2  . LYS   A 46  ? 0.610801 0.34303  0.614421 -0.18399    -0.0299524  -0.0368935  58  LYS   B HB2  
694  H HB3  . LYS   A 46  ? 0.639485 0.348178 0.649081 -0.177353   -0.0682735  -0.06315    58  LYS   B HB3  
695  H HG2  . LYS   A 46  ? 0.665034 0.416496 0.795137 -0.205626   -0.0814859  -0.0790508  58  LYS   B HG2  
696  H HG3  . LYS   A 46  ? 0.62548  0.411128 0.751304 -0.206598   -0.042986   -0.0550949  58  LYS   B HG3  
697  H HD2  . LYS   A 46  ? 0.71332  0.430584 0.814752 -0.226858   0.00181865  -0.0184772  58  LYS   B HD2  
698  H HD3  . LYS   A 46  ? 0.746905 0.435468 0.879841 -0.231584   -0.0355906  -0.0423094  58  LYS   B HD3  
699  H HE2  . LYS   A 46  ? 0.736757 0.49702  1.01218  -0.259289   -0.0361989  -0.0523581  58  LYS   B HE2  
700  H HE3  . LYS   A 46  ? 0.718958 0.488925 0.955596 -0.256684   0.0149437   -0.0205165  58  LYS   B HE3  
701  H HZ1  . LYS   A 46  ? 0.815437 0.494996 1.09241  -0.281646   -0.00890198 -0.0259042  58  LYS   B HZ1  
702  H HZ2  . LYS   A 46  ? 0.803792 0.486964 1.02042  -0.273352   0.0351608   0.00547022  58  LYS   B HZ2  
703  H HZ3  . LYS   A 46  ? 0.79652  0.515291 1.11995  -0.294773   0.0313173   -0.00423172 58  LYS   B HZ3  
704  N N    . GLY   A 47  ? 0.631817 0.372045 0.524564 -0.117101   -0.0856073  -0.0714756  59  GLY   B N    
705  C CA   . GLY   A 47  ? 0.658909 0.390646 0.498651 -0.0960132  -0.0789423  -0.0619739  59  GLY   B CA   
706  C C    . GLY   A 47  ? 0.629021 0.320045 0.442778 -0.0825183  -0.0936611  -0.073228   59  GLY   B C    
707  O O    . GLY   A 47  ? 0.646572 0.31737  0.47447  -0.0845549  -0.115053   -0.0949532  59  GLY   B O    
708  H H    . GLY   A 47  ? 0.643847 0.375824 0.549005 -0.116614   -0.104932   -0.0879059  59  GLY   B H    
709  H HA2  . GLY   A 47  ? 0.622468 0.353006 0.457474 -0.103183   -0.061667   -0.0459518  59  GLY   B HA2  
710  H HA3  . GLY   A 47  ? 0.616101 0.370548 0.442572 -0.0817417  -0.0810572  -0.063256   59  GLY   B HA3  
711  N N    . LYS   A 48  ? 0.629675 0.308948 0.410102 -0.069021   -0.0828364  -0.0588128  60  LYS   B N    
712  C CA   . LYS   A 48  ? 0.733241 0.373679 0.489711 -0.0525304  -0.0917372  -0.0656645  60  LYS   B CA   
713  C C    . LYS   A 48  ? 0.79142  0.443382 0.515957 -0.0272891  -0.0822143  -0.0521528  60  LYS   B C    
714  O O    . LYS   A 48  ? 0.715352 0.399418 0.441222 -0.0293762  -0.0691771  -0.0349621  60  LYS   B O    
715  C CB   . LYS   A 48  ? 0.813457 0.409245 0.586402 -0.0712204  -0.0883539  -0.0575001  60  LYS   B CB   
716  C CG   . LYS   A 48  ? 0.890361 0.483244 0.651588 -0.0771596  -0.068532   -0.0275373  60  LYS   B CG   
717  C CD   . LYS   A 48  ? 0.912022 0.462441 0.691722 -0.0987763  -0.059637   -0.0135753  60  LYS   B CD   
718  C CE   . LYS   A 48  ? 1.13568  0.634645 0.903516 -0.0854889  -0.06869    -0.0145129  60  LYS   B CE   
719  N NZ   . LYS   A 48  ? 1.19124  0.676437 0.925979 -0.0717447  -0.0599444  0.0124828   60  LYS   B NZ   
720  H H    . LYS   A 48  ? 0.620306 0.316747 0.395306 -0.0694903  -0.0703386  -0.0448419  60  LYS   B H    
721  H HA   . LYS   A 48  ? 0.758942 0.392582 0.510987 -0.0432045  -0.107185   -0.0855916  60  LYS   B HA   
722  H HB2  . LYS   A 48  ? 0.854611 0.421012 0.616992 -0.0598103  -0.0981887  -0.0677015  60  LYS   B HB2  
723  H HB3  . LYS   A 48  ? 0.824182 0.418678 0.627692 -0.0900762  -0.0906062  -0.062695   60  LYS   B HB3  
724  H HG2  . LYS   A 48  ? 0.832945 0.455379 0.596787 -0.0835002  -0.0594046  -0.0201963  60  LYS   B HG2  
725  H HG3  . LYS   A 48  ? 0.870127 0.458648 0.608605 -0.0592147  -0.06979    -0.0229141  60  LYS   B HG3  
726  H HD2  . LYS   A 48  ? 0.952974 0.503495 0.764618 -0.115043   -0.0613421  -0.0224071  60  LYS   B HD2  
727  H HD3  . LYS   A 48  ? 0.946033 0.501967 0.715621 -0.104862   -0.0450413  0.00609422  60  LYS   B HD3  
728  H HE2  . LYS   A 48  ? 1.09869  0.597766 0.858518 -0.0693317  -0.0821261  -0.0334658  60  LYS   B HE2  
729  H HE3  . LYS   A 48  ? 1.12703  0.597997 0.919721 -0.100796   -0.0683558  -0.015297   60  LYS   B HE3  
730  H HZ1  . LYS   A 48  ? 1.15318  0.664369 0.871905 -0.0580021  -0.0618728  0.012341    60  LYS   B HZ1  
731  H HZ2  . LYS   A 48  ? 1.18059  0.663616 0.914411 -0.084367   -0.0477801  0.0300838   60  LYS   B HZ2  
732  H HZ3  . LYS   A 48  ? 1.21119  0.66352  0.94327  -0.0633709  -0.0652132  0.0119804   60  LYS   B HZ3  
733  N N    . LEU   A 49  ? 0.771394 0.398041 0.472436 -0.00227168 -0.0900503  -0.0634445  61  LEU   B N    
734  C CA   . LEU   A 49  ? 0.7929   0.426086 0.474635 0.024178    -0.0807125  -0.0512201  61  LEU   B CA   
735  C C    . LEU   A 49  ? 0.796434 0.404193 0.484102 0.0155742   -0.0770741  -0.0323     61  LEU   B C    
736  O O    . LEU   A 49  ? 0.799141 0.366758 0.493717 0.00149912  -0.0831319  -0.0367724  61  LEU   B O    
737  C CB   . LEU   A 49  ? 0.812144 0.423648 0.465385 0.057401    -0.0868596  -0.0711938  61  LEU   B CB   
738  C CG   . LEU   A 49  ? 0.84935  0.480628 0.479037 0.0750375   -0.0913709  -0.0895889  61  LEU   B CG   
739  C CD1  . LEU   A 49  ? 0.976039 0.57873  0.564229 0.112868    -0.0947291  -0.11086    61  LEU   B CD1  
740  C CD2  . LEU   A 49  ? 0.811753 0.496062 0.44842  0.080106    -0.072488   -0.0667879  61  LEU   B CD2  
741  H H    . LEU   A 49  ? 0.818376 0.422261 0.518437 -0.00122681 -0.102163   -0.0809175  61  LEU   B H    
742  H HA   . LEU   A 49  ? 0.750166 0.417589 0.434973 0.0266365   -0.0720878  -0.0409774  61  LEU   B HA   
743  H HB2  . LEU   A 49  ? 0.860525 0.434686 0.513387 0.0536479   -0.096997   -0.0832996  61  LEU   B HB2  
744  H HB3  . LEU   A 49  ? 0.824815 0.441857 0.473538 0.0742194   -0.077632   -0.0598746  61  LEU   B HB3  
745  H HG   . LEU   A 49  ? 0.8586   0.486171 0.496569 0.0590892   -0.104131   -0.101884   61  LEU   B HG   
746  H HD11 . LEU   A 49  ? 0.991158 0.556195 0.577862 0.108473    -0.10874    -0.127875   61  LEU   B HD11 
747  H HD12 . LEU   A 49  ? 0.965739 0.581321 0.53113  0.126355    -0.0968593  -0.120517   61  LEU   B HD12 
748  H HD13 . LEU   A 49  ? 0.953622 0.561877 0.540013 0.129101    -0.0804112  -0.0977295  61  LEU   B HD13 
749  H HD21 . LEU   A 49  ? 0.776272 0.476168 0.433034 0.0583767   -0.0730319  -0.060419   61  LEU   B HD21 
750  H HD22 . LEU   A 49  ? 0.797788 0.489242 0.441625 0.0873001   -0.0614582  -0.0517729  61  LEU   B HD22 
751  H HD23 . LEU   A 49  ? 0.820948 0.5158   0.436494 0.0986957   -0.0707201  -0.0732608  61  LEU   B HD23 
752  N N    . SER   A 50  ? 0.837654 0.466887 0.524939 0.0253531   -0.069183   -0.0112372  62  SER   B N    
753  C CA   . SER   A 50  ? 0.890085 0.491558 0.57469  0.024835    -0.0707906  0.00737137  62  SER   B CA   
754  C C    . SER   A 50  ? 0.849494 0.405631 0.526033 0.0463167   -0.0766976  -0.00074391 62  SER   B C    
755  O O    . SER   A 50  ? 0.981219 0.500762 0.655929 0.0430261   -0.0792933  0.012551    62  SER   B O    
756  C CB   . SER   A 50  ? 0.899237 0.533476 0.58872  0.0331733   -0.0693453  0.0288097   62  SER   B CB   
757  O OG   . SER   A 50  ? 1.0463   0.717489 0.748587 0.0559386   -0.0645547  0.0263237   62  SER   B OG   
758  H H    . SER   A 50  ? 0.801558 0.462177 0.492066 0.0326912   -0.0640896  -0.00776149 62  SER   B H    
759  H HA   . SER   A 50  ? 0.8772   0.463623 0.563167 0.00457842  -0.0699601  0.0120271   62  SER   B HA   
760  H HB2  . SER   A 50  ? 0.952211 0.565325 0.636739 0.0395051   -0.0738369  0.0394921   62  SER   B HB2  
761  H HB3  . SER   A 50  ? 0.907703 0.557605 0.598349 0.0165771   -0.0674295  0.0345448   62  SER   B HB3  
763  N N    . ASN   A 51  ? 0.865864 0.418943 0.533104 0.0713768   -0.0777226  -0.0219018  63  ASN   B N    
764  C CA   . ASN   A 51  ? 0.928991 0.429251 0.586664 0.0921907   -0.0833999  -0.033638   63  ASN   B CA   
765  C C    . ASN   A 51  ? 0.971632 0.417409 0.632815 0.0713866   -0.0955813  -0.052187   63  ASN   B C    
766  O O    . ASN   A 51  ? 1.03782  0.43105  0.694358 0.0861132   -0.102123   -0.0650503  63  ASN   B O    
767  C CB   . ASN   A 51  ? 0.979226 0.488626 0.619008 0.130749    -0.0774185  -0.0506377  63  ASN   B CB   
768  C CG   . ASN   A 51  ? 1.0321   0.54675  0.649554 0.132023    -0.0825739  -0.0797582  63  ASN   B CG   
769  O OD1  . ASN   A 51  ? 1.05811  0.56559  0.682067 0.103457    -0.095124   -0.0911019  63  ASN   B OD1  
770  N ND2  . ASN   A 51  ? 1.09094  0.616126 0.681115 0.167881    -0.0731858  -0.0921387  63  ASN   B ND2  
771  H H    . ASN   A 51  ? 0.847494 0.427999 0.511765 0.077288    -0.0741196  -0.0286762  63  ASN   B H    
772  H HA   . ASN   A 51  ? 0.942809 0.434781 0.606124 0.0969873   -0.0821441  -0.0156763  63  ASN   B HA   
773  H HB2  . ASN   A 51  ? 1.02386  0.498289 0.658239 0.14714     -0.0794969  -0.0567284  63  ASN   B HB2  
774  H HB3  . ASN   A 51  ? 0.95387  0.500024 0.601911 0.141195    -0.0675704  -0.0356556  63  ASN   B HB3  
775  H HD21 . ASN   A 51  ? 1.09507  0.618325 0.663833 0.173055    -0.0781506  -0.110239   63  ASN   B HD21 
776  H HD22 . ASN   A 51  ? 1.08157  0.616179 0.674544 0.187791    -0.0614092  -0.0816383  63  ASN   B HD22 
777  N N    . GLY   A 52  ? 0.966592 0.423117 0.643008 0.0384289   -0.0986314  -0.05551    64  GLY   B N    
778  C CA   . GLY   A 52  ? 1.08432  0.497026 0.781622 0.014831    -0.110107   -0.0721451  64  GLY   B CA   
779  C C    . GLY   A 52  ? 1.19332  0.584093 0.88113  0.0278091   -0.130388   -0.114934   64  GLY   B C    
780  O O    . GLY   A 52  ? 1.16987  0.520188 0.88327  0.00876519  -0.145394   -0.133417   64  GLY   B O    
781  H H    . GLY   A 52  ? 0.938182 0.431725 0.61721  0.0304432   -0.093052   -0.0472118  64  GLY   B H    
782  H HA2  . GLY   A 52  ? 1.05038  0.482033 0.764859 -0.00854763 -0.106766   -0.0654607  64  GLY   B HA2  
783  H HA3  . GLY   A 52  ? 1.10791  0.483932 0.811454 0.0126084   -0.10832    -0.0612581  64  GLY   B HA3  
784  N N    . LYS   A 53  ? 1.21197  0.626785 0.863539 0.0603352   -0.131373   -0.131106   65  LYS   B N    
785  C CA   . LYS   A 53  ? 1.25603  0.643433 0.881583 0.0793052   -0.152168   -0.173641   65  LYS   B CA   
786  C C    . LYS   A 53  ? 1.20979  0.631028 0.838918 0.0642871   -0.168523   -0.191587   65  LYS   B C    
787  O O    . LYS   A 53  ? 1.31692  0.713012 0.930989 0.0715599   -0.194843   -0.22949    65  LYS   B O    
788  C CB   . LYS   A 53  ? 1.21731  0.596604 0.795212 0.127691    -0.142855   -0.183456   65  LYS   B CB   
789  H H    . LYS   A 53  ? 1.16909  0.617039 0.811192 0.0711935   -0.118872   -0.115499   65  LYS   B H    
790  H HA   . LYS   A 53  ? 1.27874  0.621197 0.919711 0.0697965   -0.163806   -0.186202   65  LYS   B HA   
793  N N    . LYS   A 54  ? 1.09441  0.567914 0.746374 0.0426488   -0.15792    -0.168296   66  LYS   B N    
794  C CA   . LYS   A 54  ? 1.02696  0.53232  0.684719 0.0334453   -0.174761   -0.18474    66  LYS   B CA   
795  C C    . LYS   A 54  ? 0.984057 0.525516 0.692764 -0.0035984  -0.164605   -0.160877   66  LYS   B C    
796  O O    . LYS   A 54  ? 0.932073 0.498112 0.645175 -0.00918519 -0.139201   -0.128832   66  LYS   B O    
797  C CB   . LYS   A 54  ? 0.987507 0.526859 0.59253  0.0695648   -0.169556   -0.187804   66  LYS   B CB   
798  H H    . LYS   A 54  ? 1.05945  0.548148 0.722998 0.0348345   -0.141491   -0.142903   66  LYS   B H    
799  H HA   . LYS   A 54  ? 1.07562  0.55293  0.738852 0.0297531   -0.197495   -0.211339   66  LYS   B HA   
802  N N    . PHE   A 55  ? 0.926897 0.470515 0.675411 -0.0270352  -0.185976   -0.178989   67  PHE   B N    
803  C CA   . PHE   A 55  ? 0.91333  0.490537 0.717392 -0.0603979  -0.177185   -0.162143   67  PHE   B CA   
804  C C    . PHE   A 55  ? 0.947512 0.563075 0.765098 -0.0596922  -0.199448   -0.180205   67  PHE   B C    
805  O O    . PHE   A 55  ? 0.985406 0.586227 0.788537 -0.0464061  -0.233069   -0.213675   67  PHE   B O    
806  C CB   . PHE   A 55  ? 0.986112 0.529184 0.851439 -0.0944416  -0.180478   -0.163193   67  PHE   B CB   
807  C CG   . PHE   A 55  ? 1.15921  0.653406 1.01184  -0.0935758  -0.164044   -0.1466     67  PHE   B CG   
808  C CD1  . PHE   A 55  ? 1.29428  0.738377 1.11678  -0.0718568  -0.180171   -0.168446   67  PHE   B CD1  
809  C CD2  . PHE   A 55  ? 1.2394   0.73442  1.1069   -0.111778   -0.132798   -0.109131   67  PHE   B CD2  
810  C CE1  . PHE   A 55  ? 1.33345  0.732316 1.14802  -0.0684686  -0.165284   -0.150284   67  PHE   B CE1  
811  C CE2  . PHE   A 55  ? 1.26561  0.714867 1.11762  -0.107723   -0.120204   -0.0904417  67  PHE   B CE2  
812  C CZ   . PHE   A 55  ? 1.29275  0.695376 1.12214  -0.086266   -0.136521   -0.109704   67  PHE   B CZ   
813  H H    . PHE   A 55  ? 0.990255 0.512927 0.7326   -0.020583   -0.208297   -0.205103   67  PHE   B H    
814  H HA   . PHE   A 55  ? 0.884194 0.481607 0.682593 -0.0618144  -0.15425    -0.137438   67  PHE   B HA   
815  H HB2  . PHE   A 55  ? 1.03771  0.565953 0.919132 -0.0966374  -0.206408   -0.189686   67  PHE   B HB2  
816  H HB3  . PHE   A 55  ? 0.974524 0.541806 0.874804 -0.114358   -0.167486   -0.147668   67  PHE   B HB3  
817  H HD1  . PHE   A 55  ? 1.2989   0.739032 1.10292  -0.0568472  -0.201087   -0.19546    67  PHE   B HD1  
818  H HD2  . PHE   A 55  ? 1.17583  0.701516 1.06019  -0.124606   -0.120239   -0.0960683  67  PHE   B HD2  
819  H HE1  . PHE   A 55  ? 1.36717  0.731388 1.16308  -0.0519542  -0.175228   -0.165712   67  PHE   B HE1  
820  H HE2  . PHE   A 55  ? 1.25057  0.699924 1.10488  -0.117503   -0.100481   -0.0645024  67  PHE   B HE2  
821  H HZ   . PHE   A 55  ? 1.32549  0.696603 1.14754  -0.0823232  -0.128383   -0.0958095  67  PHE   B HZ   
822  N N    . ASP   A 56  ? 0.836777 0.498968 0.683773 -0.0735858  -0.183744   -0.159999   68  ASP   B N    
823  C CA   . ASP   A 56  ? 0.86549  0.568463 0.72265  -0.0673935  -0.202025   -0.170592   68  ASP   B CA   
824  C C    . ASP   A 56  ? 0.842859 0.579357 0.76793  -0.0976958  -0.184757   -0.151953   68  ASP   B C    
825  O O    . ASP   A 56  ? 0.814469 0.558664 0.738279 -0.105976   -0.150695   -0.12463    68  ASP   B O    
826  C CB   . ASP   A 56  ? 0.870354 0.600674 0.668977 -0.0348799  -0.191311   -0.159125   68  ASP   B CB   
827  C CG   . ASP   A 56  ? 0.896491 0.671169 0.705727 -0.0273798  -0.202803   -0.159025   68  ASP   B CG   
828  O OD1  . ASP   A 56  ? 0.94388  0.721285 0.774701 -0.0293415  -0.238308   -0.183867   68  ASP   B OD1  
829  O OD2  . ASP   A 56  ? 0.756626 0.562242 0.555002 -0.0182733  -0.179248   -0.134774   68  ASP   B OD2  
830  H H    . ASP   A 56  ? 0.83262  0.499795 0.69205  -0.0858002  -0.161114   -0.138846   68  ASP   B H    
831  H HA   . ASP   A 56  ? 0.903097 0.593893 0.765924 -0.0650328  -0.231113   -0.195723   68  ASP   B HA   
832  H HB2  . ASP   A 56  ? 0.907408 0.618205 0.662669 -0.0130362  -0.201001   -0.171771   68  ASP   B HB2  
833  H HB3  . ASP   A 56  ? 0.842057 0.57893  0.636493 -0.0375534  -0.165493   -0.137371   68  ASP   B HB3  
834  N N    . SER   A 57  ? 0.882448 0.639174 0.865643 -0.111766   -0.208656   -0.167663   69  SER   B N    
835  C CA   . SER   A 57  ? 0.865585 0.659387 0.918374 -0.136136   -0.189542   -0.150378   69  SER   B CA   
836  C C    . SER   A 57  ? 0.876102 0.712686 0.95729  -0.126997   -0.218232   -0.163871   69  SER   B C    
837  O O    . SER   A 57  ? 0.917814 0.746598 1.00473  -0.120424   -0.262671   -0.194238   69  SER   B O    
838  C CB   . SER   A 57  ? 0.962595 0.736451 1.08863  -0.170349   -0.184944   -0.150687   69  SER   B CB   
839  O OG   . SER   A 57  ? 1.03955  0.852916 1.2422   -0.191859   -0.166855   -0.136744   69  SER   B OG   
840  H H    . SER   A 57  ? 0.91259  0.660145 0.893459 -0.104958   -0.23838    -0.190762   69  SER   B H    
841  H HA   . SER   A 57  ? 0.843416 0.646626 0.878384 -0.134743   -0.160707   -0.129132   69  SER   B HA   
842  H HB2  . SER   A 57  ? 0.970096 0.717601 1.07632  -0.175057   -0.163577   -0.137077   69  SER   B HB2  
843  H HB3  . SER   A 57  ? 1.00134  0.759515 1.14361  -0.172145   -0.215165   -0.17368    69  SER   B HB3  
845  N N    . SER   A 58  ? 0.782052 0.659599 0.885412 -0.127722   -0.194792   -0.142933   70  SER   B N    
846  C CA   . SER   A 58  ? 0.778353 0.700438 0.926342 -0.121756   -0.217211   -0.149364   70  SER   B CA   
847  C C    . SER   A 58  ? 0.8247   0.75799  1.06541  -0.145258   -0.247575   -0.169526   70  SER   B C    
848  O O    . SER   A 58  ? 0.831801 0.794894 1.10171  -0.134933   -0.287024   -0.18605    70  SER   B O    
849  C CB   . SER   A 58  ? 0.591771 0.551001 0.766731 -0.123442   -0.182272   -0.123667   70  SER   B CB   
850  O OG   . SER   A 58  ? 0.528169 0.483387 0.743611 -0.150336   -0.140865   -0.106248   70  SER   B OG   
851  H H    . SER   A 58  ? 0.769225 0.645766 0.859406 -0.130954   -0.164741   -0.124464   70  SER   B H    
852  H HA   . SER   A 58  ? 0.770046 0.692266 0.87208  -0.0980467  -0.239423   -0.15885    70  SER   B HA   
853  H HB2  . SER   A 58  ? 0.607712 0.595668 0.822942 -0.120712   -0.199207   -0.128571   70  SER   B HB2  
854  H HB3  . SER   A 58  ? 0.596288 0.553751 0.719203 -0.10598    -0.171433   -0.113915   70  SER   B HB3  
856  N N    . HIS   A 59  ? 0.88465  0.798028 1.17896  -0.176766   -0.227732   -0.164608   71  HIS   B N    
857  C CA   . HIS   A 59  ? 1.03027  0.955748 1.43106  -0.203616   -0.25239    -0.180773   71  HIS   B CA   
858  C C    . HIS   A 59  ? 1.19903  1.09929  1.59108  -0.196764   -0.314602   -0.221673   71  HIS   B C    
859  O O    . HIS   A 59  ? 1.18092  1.10205  1.65982  -0.211359   -0.3535     -0.243425   71  HIS   B O    
860  C CB   . HIS   A 59  ? 1.0421   0.949184 1.50245  -0.23818    -0.209233   -0.159762   71  HIS   B CB   
861  C CG   . HIS   A 59  ? 1.02426  0.954868 1.4899   -0.242543   -0.151451   -0.124776   71  HIS   B CG   
862  N ND1  . HIS   A 59  ? 1.13211  1.11322  1.6825   -0.252139   -0.134327   -0.113837   71  HIS   B ND1  
863  C CD2  . HIS   A 59  ? 0.996064 0.904354 1.39019  -0.236583   -0.108526   -0.100764   71  HIS   B CD2  
864  C CE1  . HIS   A 59  ? 1.04011  1.02412  1.56302  -0.251075   -0.0799109  -0.0856384  71  HIS   B CE1  
865  N NE2  . HIS   A 59  ? 1.04191  0.981668 1.46997  -0.242782   -0.0661173  -0.0781299  71  HIS   B NE2  
866  H H    . HIS   A 59  ? 0.886204 0.778967 1.15434  -0.181684   -0.198673   -0.14985    71  HIS   B H    
867  H HA   . HIS   A 59  ? 1.00402  0.969576 1.45006  -0.202766   -0.256163   -0.177775   71  HIS   B HA   
868  H HB2  . HIS   A 59  ? 1.06381  0.930299 1.4802   -0.238177   -0.204833   -0.160301   71  HIS   B HB2  
869  H HB3  . HIS   A 59  ? 1.06055  0.977341 1.60123  -0.257286   -0.224666   -0.169389   71  HIS   B HB3  
871  H HD2  . HIS   A 59  ? 1.02606  0.902429 1.36019  -0.229222   -0.107636   -0.100102   71  HIS   B HD2  
872  H HE1  . HIS   A 59  ? 1.0363   1.04869  1.60093  -0.254551   -0.0562444  -0.0741894  71  HIS   B HE1  
874  N N    . ASP   A 60  ? 1.26427  1.11999  1.55504  -0.173573   -0.325447   -0.234275   72  ASP   B N    
875  C CA   . ASP   A 60  ? 1.36046  1.19178  1.61651  -0.155706   -0.384945   -0.276531   72  ASP   B CA   
876  C C    . ASP   A 60  ? 1.35985  1.23927  1.62674  -0.136201   -0.426919   -0.290611   72  ASP   B C    
877  O O    . ASP   A 60  ? 1.55919  1.45146  1.89801  -0.14842    -0.475749   -0.319317   72  ASP   B O    
878  C CB   . ASP   A 60  ? 1.31873  1.10329  1.45449  -0.124651   -0.380851   -0.282922   72  ASP   B CB   
879  C CG   . ASP   A 60  ? 1.34836  1.08425  1.47566  -0.140751   -0.344955   -0.269099   72  ASP   B CG   
880  O OD1  . ASP   A 60  ? 1.19259  0.916169 1.40769  -0.177108   -0.339682   -0.26736    72  ASP   B OD1  
881  O OD2  . ASP   A 60  ? 1.1546   0.867995 1.19412  -0.116802   -0.319735   -0.255925   72  ASP   B OD2  
882  H H    . ASP   A 60  ? 1.23995  1.08001  1.48238  -0.167678   -0.295312   -0.217072   72  ASP   B H    
883  H HA   . ASP   A 60  ? 1.36658  1.17992  1.67857  -0.177281   -0.401596   -0.292392   72  ASP   B HA   
884  H HB2  . ASP   A 60  ? 1.31394  1.11621  1.39922  -0.104163   -0.363425   -0.26614    72  ASP   B HB2  
885  H HB3  . ASP   A 60  ? 1.39232  1.15952  1.50215  -0.110842   -0.420335   -0.313326   72  ASP   B HB3  
886  N N    . ARG   A 61  ? 1.3192   1.22689  1.52556  -0.10778    -0.40729    -0.267664   73  ARG   B N    
887  C CA   . ARG   A 61  ? 1.24446  1.19603  1.45206  -0.0839635  -0.443085   -0.273607   73  ARG   B CA   
888  C C    . ARG   A 61  ? 1.18521  1.18904  1.52642  -0.111214   -0.450874   -0.268949   73  ARG   B C    
889  O O    . ARG   A 61  ? 1.25762  1.30263  1.61818  -0.0933472  -0.483388   -0.272577   73  ARG   B O    
890  C CB   . ARG   A 61  ? 0.984505 0.947576 1.10305  -0.0496865  -0.410916   -0.243581   73  ARG   B CB   
891  H H    . ARG   A 61  ? 1.27194  1.17043  1.43711  -0.102832   -0.371337   -0.246947   73  ARG   B H    
892  H HA   . ARG   A 61  ? 1.25822  1.19464  1.43463  -0.069417   -0.486691   -0.302273   73  ARG   B HA   
895  N N    . ASN   A 62  ? 1.10999  1.1133   1.54635  -0.152184   -0.421032   -0.259342   74  ASN   B N    
896  C CA   . ASN   A 62  ? 1.03672  1.09169  1.60321  -0.178036   -0.407805   -0.245129   74  ASN   B CA   
897  C C    . ASN   A 62  ? 0.953863 1.05617  1.50958  -0.153744   -0.390386   -0.220561   74  ASN   B C    
898  O O    . ASN   A 62  ? 0.899639 1.04715  1.51357  -0.144513   -0.428257   -0.229145   74  ASN   B O    
899  C CB   . ASN   A 62  ? 0.930988 1.00303  1.60757  -0.198605   -0.467095   -0.278817   74  ASN   B CB   
900  H H    . ASN   A 62  ? 1.12271  1.0911   1.54169  -0.163176   -0.405875   -0.260064   74  ASN   B H    
901  H HA   . ASN   A 62  ? 0.980801 1.02532  1.57382  -0.199292   -0.365733   -0.227169   74  ASN   B HA   
904  N N    . GLU   A 63  ? 0.880131 0.970979 1.35937  -0.139968   -0.339011   -0.191665   75  GLU   B N    
905  C CA   . GLU   A 63  ? 0.765458 0.897849 1.25553  -0.122658   -0.317317   -0.167575   75  GLU   B CA   
906  C C    . GLU   A 63  ? 0.69397  0.802914 1.09719  -0.11075    -0.265757   -0.141679   75  GLU   B C    
907  O O    . GLU   A 63  ? 0.706161 0.773266 1.02084  -0.102482   -0.261948   -0.144646   75  GLU   B O    
908  C CB   . GLU   A 63  ? 0.799322 0.961291 1.26734  -0.08693    -0.364149   -0.174354   75  GLU   B CB   
909  C CG   . GLU   A 63  ? 0.848702 0.975727 1.18311  -0.0515299  -0.384252   -0.180728   75  GLU   B CG   
910  C CD   . GLU   A 63  ? 0.991128 1.12565  1.31179  -0.0296625  -0.458264   -0.211964   75  GLU   B CD   
911  O OE1  . GLU   A 63  ? 0.973199 1.15427  1.36338  -0.0231708  -0.487934   -0.212199   75  GLU   B OE1  
912  O OE2  . GLU   A 63  ? 1.01706  1.11157  1.261    -0.0179767  -0.488258   -0.237681   75  GLU   B OE2  
913  H H    . GLU   A 63  ? 0.868926 0.926378 1.29406  -0.141107   -0.319456   -0.18774    75  GLU   B H    
914  H HA   . GLU   A 63  ? 0.751334 0.909369 1.32438  -0.141124   -0.299903   -0.15967    75  GLU   B HA   
915  H HB2  . GLU   A 63  ? 0.770423 0.957038 1.25726  -0.0793493  -0.342458   -0.155192   75  GLU   B HB2  
916  H HB3  . GLU   A 63  ? 0.824015 1.00523  1.35024  -0.092555   -0.403013   -0.192445   75  GLU   B HB3  
917  H HG2  . GLU   A 63  ? 0.865358 0.95767  1.15884  -0.05933    -0.370837   -0.185117   75  GLU   B HG2  
918  H HG3  . GLU   A 63  ? 0.844773 0.978047 1.14207  -0.0333545  -0.362896   -0.160228   75  GLU   B HG3  
919  N N    . PRO   A 64  ? 0.608771 0.745003 1.04301  -0.109393   -0.226248   -0.117438   76  PRO   B N    
920  C CA   . PRO   A 64  ? 0.531953 0.647416 0.899666 -0.102372   -0.178596   -0.0954584  76  PRO   B CA   
921  C C    . PRO   A 64  ? 0.523512 0.620429 0.792006 -0.0704578  -0.194036   -0.0933761  76  PRO   B C    
922  O O    . PRO   A 64  ? 0.659613 0.77021  0.913087 -0.0466765  -0.23496    -0.101984   76  PRO   B O    
923  C CB   . PRO   A 64  ? 0.50378  0.65539  0.928014 -0.0985408  -0.150191   -0.0779229  76  PRO   B CB   
924  C CG   . PRO   A 64  ? 0.545293 0.734455 1.08558  -0.117122   -0.164971   -0.0870568  76  PRO   B CG   
925  C CD   . PRO   A 64  ? 0.617134 0.805182 1.15544  -0.112684   -0.227454   -0.112109   76  PRO   B CD   
926  H HA   . PRO   A 64  ? 0.53143  0.624169 0.889309 -0.119037   -0.155631   -0.0929666  76  PRO   B HA   
927  H HB2  . PRO   A 64  ? 0.513662 0.67563  0.916471 -0.0764243  -0.162236   -0.0730891  76  PRO   B HB2  
928  H HB3  . PRO   A 64  ? 0.494867 0.634497 0.906955 -0.106346   -0.112291   -0.0667385  76  PRO   B HB3  
929  H HG2  . PRO   A 64  ? 0.534262 0.753788 1.11842  -0.108294   -0.161398   -0.0799434  76  PRO   B HG2  
930  H HG3  . PRO   A 64  ? 0.538113 0.719929 1.10827  -0.139066   -0.138817   -0.084218   76  PRO   B HG3  
931  H HD2  . PRO   A 64  ? 0.616003 0.822501 1.14787  -0.0912458  -0.255682   -0.114423   76  PRO   B HD2  
932  H HD3  . PRO   A 64  ? 0.612522 0.812289 1.22046  -0.132301   -0.237878   -0.121708   76  PRO   B HD3  
933  N N    . PHE   A 65  ? 0.544707 0.610322 0.74744  -0.0698723  -0.162088   -0.0818549  77  PHE   B N    
934  C CA   . PHE   A 65  ? 0.550224 0.602165 0.671815 -0.041701   -0.160317   -0.0713396  77  PHE   B CA   
935  C C    . PHE   A 65  ? 0.447985 0.517375 0.581913 -0.0323328  -0.130388   -0.0484376  77  PHE   B C    
936  O O    . PHE   A 65  ? 0.4364   0.505121 0.597493 -0.0491796  -0.0958097  -0.0403874  77  PHE   B O    
937  C CB   . PHE   A 65  ? 0.5397   0.552873 0.603253 -0.0484342  -0.143744   -0.0719145  77  PHE   B CB   
938  C CG   . PHE   A 65  ? 0.568556 0.568464 0.556337 -0.0208392  -0.137725   -0.0599571  77  PHE   B CG   
939  C CD1  . PHE   A 65  ? 0.677759 0.666677 0.609245 0.00501397  -0.167244   -0.0707682  77  PHE   B CD1  
940  C CD2  . PHE   A 65  ? 0.526074 0.522769 0.499384 -0.0200778  -0.102002   -0.0389293  77  PHE   B CD2  
941  C CE1  . PHE   A 65  ? 0.638941 0.616728 0.503618 0.0319666   -0.154756   -0.0563043  77  PHE   B CE1  
942  C CE2  . PHE   A 65  ? 0.585762 0.574881 0.504889 0.00448389  -0.0948762  -0.0250553  77  PHE   B CE2  
943  C CZ   . PHE   A 65  ? 0.63848  0.619489 0.504693 0.0305457   -0.117237   -0.0310567  77  PHE   B CZ   
944  H H    . PHE   A 65  ? 0.524306 0.577299 0.736021 -0.0877567  -0.139728   -0.0792274  77  PHE   B H    
945  H HA   . PHE   A 65  ? 0.562159 0.617974 0.662789 -0.0237776  -0.190822   -0.0794364  77  PHE   B HA   
946  H HB2  . PHE   A 65  ? 0.568433 0.5687   0.631162 -0.0546516  -0.16315    -0.0874996  77  PHE   B HB2  
947  H HB3  . PHE   A 65  ? 0.52438  0.533053 0.604214 -0.0647874  -0.116722   -0.0642634  77  PHE   B HB3  
948  H HD1  . PHE   A 65  ? 0.673951 0.661653 0.613166 0.00425915  -0.195146   -0.0888373  77  PHE   B HD1  
949  H HD2  . PHE   A 65  ? 0.517629 0.519278 0.52157  -0.0346313  -0.0831509  -0.0338817  77  PHE   B HD2  
950  H HE1  . PHE   A 65  ? 0.695582 0.665316 0.517411 0.0522694   -0.171999   -0.0633431  77  PHE   B HE1  
951  H HE2  . PHE   A 65  ? 0.557353 0.54528  0.475838 0.00306932  -0.0728458  -0.0117232  77  PHE   B HE2  
952  H HZ   . PHE   A 65  ? 0.637    0.612919 0.467807 0.0474326   -0.106765   -0.0191799  77  PHE   B HZ   
953  N N    . VAL   A 66  ? 0.509884 0.590359 0.617329 -0.00258195 -0.144212   -0.0379529  78  VAL   B N    
954  C CA   . VAL   A 66  ? 0.490187 0.588852 0.621663 0.011002    -0.126253   -0.0172018  78  VAL   B CA   
955  C C    . VAL   A 66  ? 0.522686 0.601883 0.583558 0.0342998   -0.113923   0.00176807  78  VAL   B C    
956  O O    . VAL   A 66  ? 0.563883 0.631401 0.563742 0.053517    -0.13443    -0.00103809 78  VAL   B O    
957  C CB   . VAL   A 66  ? 0.531579 0.664749 0.707801 0.0291168   -0.158032   -0.016852   78  VAL   B CB   
958  C CG1  . VAL   A 66  ? 0.525739 0.67561  0.747909 0.0368405   -0.131936   0.00353023  78  VAL   B CG1  
959  C CG2  . VAL   A 66  ? 0.560202 0.715833 0.804514 0.0100544   -0.187298   -0.0403147  78  VAL   B CG2  
960  H H    . VAL   A 66  ? 0.525552 0.599193 0.594097 0.0120792   -0.166387   -0.0436601  78  VAL   B H    
961  H HA   . VAL   A 66  ? 0.474072 0.572794 0.635997 -0.00470616 -0.100058   -0.0141919  78  VAL   B HA   
962  H HB   . VAL   A 66  ? 0.564864 0.694337 0.695307 0.0515189   -0.179108   -0.0140532  78  VAL   B HB   
963  H HG11 . VAL   A 66  ? 0.49674  0.64645  0.753928 0.0174515   -0.107251   0.00069677  78  VAL   B HG11 
964  H HG12 . VAL   A 66  ? 0.525562 0.661528 0.709774 0.0504082   -0.118285   0.018926    78  VAL   B HG12 
965  H HG13 . VAL   A 66  ? 0.53648  0.710036 0.792153 0.0486973   -0.153519   0.00406658  78  VAL   B HG13 
966  H HG21 . VAL   A 66  ? 0.564747 0.745623 0.843106 0.0224144   -0.208634   -0.0393253  78  VAL   B HG21 
967  H HG22 . VAL   A 66  ? 0.573328 0.715574 0.787963 0.00793457  -0.208653   -0.0547768  78  VAL   B HG22 
968  H HG23 . VAL   A 66  ? 0.527546 0.68509  0.813134 -0.0116647  -0.163083   -0.0414387  78  VAL   B HG23 
969  N N    . PHE   A 67  ? 0.527457 0.600696 0.598739 0.0314296   -0.0779513  0.0196212   79  PHE   B N    
970  C CA   . PHE   A 67  ? 0.499458 0.555324 0.523129 0.0474706   -0.0596223  0.0402557   79  PHE   B CA   
971  C C    . PHE   A 67  ? 0.509804 0.563227 0.570491 0.0428379   -0.0273654  0.0561325   79  PHE   B C    
972  O O    . PHE   A 67  ? 0.439933 0.50007  0.549445 0.0264161   -0.0166254  0.0471024   79  PHE   B O    
973  C CB   . PHE   A 67  ? 0.49566  0.527972 0.470889 0.0397383   -0.0507763  0.0357578   79  PHE   B CB   
974  C CG   . PHE   A 67  ? 0.462224 0.480954 0.45612  0.0102982   -0.0264648  0.0286295   79  PHE   B CG   
975  C CD1  . PHE   A 67  ? 0.437925 0.454978 0.452985 -0.0135581  -0.0301964  0.00940171  79  PHE   B CD1  
976  C CD2  . PHE   A 67  ? 0.41601  0.422814 0.405793 0.00786717  -0.00132906 0.0421031   79  PHE   B CD2  
977  C CE1  . PHE   A 67  ? 0.445852 0.448061 0.465735 -0.0358065  -0.00824327 0.0051275   79  PHE   B CE1  
978  C CE2  . PHE   A 67  ? 0.394202 0.38771  0.393126 -0.0159101  0.0141203   0.0328881   79  PHE   B CE2  
979  C CZ   . PHE   A 67  ? 0.427825 0.418744 0.437569 -0.0357109  0.0119734   0.0155244   79  PHE   B CZ   
980  H H    . PHE   A 67  ? 0.492575 0.572426 0.604795 0.019055    -0.0641118  0.0183265   79  PHE   B H    
981  H HA   . PHE   A 67  ? 0.539313 0.600454 0.539533 0.070758    -0.0740022  0.04955     79  PHE   B HA   
982  H HB2  . PHE   A 67  ? 0.508804 0.535663 0.456678 0.0557605   -0.0422893  0.0515526   79  PHE   B HB2  
983  H HB3  . PHE   A 67  ? 0.512271 0.542333 0.467287 0.0409817   -0.0708692  0.0222216   79  PHE   B HB3  
984  H HD1  . PHE   A 67  ? 0.455602 0.481752 0.48354  -0.014135   -0.0478923  -6.075e-05  79  PHE   B HD1  
985  H HD2  . PHE   A 67  ? 0.432814 0.440362 0.414674 0.0229323   0.00442531  0.0579096   79  PHE   B HD2  
986  H HE1  . PHE   A 67  ? 0.435094 0.435157 0.467844 -0.050543   -0.00724893 -0.00440033 79  PHE   B HE1  
987  H HE2  . PHE   A 67  ? 0.398929 0.385185 0.399455 -0.017928   0.0269175   0.0396453   79  PHE   B HE2  
988  H HZ   . PHE   A 67  ? 0.414052 0.393541 0.420229 -0.0490488  0.0224434   0.0107604   79  PHE   B HZ   
989  N N    . SER   A 68  ? 0.462245 0.506235 0.501651 0.0611746   -0.0128508  0.0807276   80  SER   B N    
990  C CA   . SER   A 68  ? 0.531541 0.568684 0.609391 0.0605208   0.0140445   0.0969661   80  SER   B CA   
991  C C    . SER   A 68  ? 0.466451 0.482229 0.534901 0.0415888   0.036362    0.0951103   80  SER   B C    
992  O O    . SER   A 68  ? 0.492872 0.501851 0.523662 0.0474101   0.0378985   0.103577    80  SER   B O    
993  C CB   . SER   A 68  ? 0.525614 0.564439 0.596971 0.0923017   0.016283    0.12917     80  SER   B CB   
994  O OG   . SER   A 68  ? 0.721416 0.78094  0.816681 0.108351    -0.00474142 0.13014     80  SER   B OG   
995  H H    . SER   A 68  ? 0.512882 0.553    0.513815 0.0750332   -0.018749   0.0879249   80  SER   B H    
996  H HA   . SER   A 68  ? 0.485967 0.529611 0.601317 0.0512304   0.0162821   0.0872064   80  SER   B HA   
997  H HB2  . SER   A 68  ? 0.590435 0.626535 0.61953  0.105594    0.0117179   0.138339    80  SER   B HB2  
998  H HB3  . SER   A 68  ? 0.56616  0.593677 0.660058 0.0896181   0.037091    0.140961    80  SER   B HB3  
1000 N N    . LEU   A 69  ? 0.412891 0.419629 0.514321 0.019198    0.0508968   0.0799648   81  LEU   B N    
1001 C CA   . LEU   A 69  ? 0.389773 0.377932 0.480997 -0.00065028 0.0627538   0.0709258   81  LEU   B CA   
1002 C C    . LEU   A 69  ? 0.381131 0.357619 0.485471 0.00556009  0.0782475   0.092082    81  LEU   B C    
1003 O O    . LEU   A 69  ? 0.339306 0.311148 0.478351 0.014955    0.0900062   0.106975    81  LEU   B O    
1004 C CB   . LEU   A 69  ? 0.418802 0.397134 0.533035 -0.0209029  0.0736693   0.0489405   81  LEU   B CB   
1005 C CG   . LEU   A 69  ? 0.485599 0.444237 0.579552 -0.0413953  0.0785746   0.0335655   81  LEU   B CG   
1006 C CD1  . LEU   A 69  ? 0.465393 0.425217 0.521142 -0.0500301  0.0664947   0.0247616   81  LEU   B CD1  
1007 C CD2  . LEU   A 69  ? 0.576976 0.522679 0.688912 -0.0528727  0.0932975   0.013924    81  LEU   B CD2  
1008 H H    . LEU   A 69  ? 0.416724 0.428989 0.546206 0.0178939   0.052775    0.0748011   81  LEU   B H    
1009 H HA   . LEU   A 69  ? 0.394222 0.382983 0.456374 -0.00410173 0.0536797   0.0653005   81  LEU   B HA   
1010 H HB2  . LEU   A 69  ? 0.42104  0.409607 0.537658 -0.0234497  0.0678532   0.0398581   81  LEU   B HB2  
1011 H HB3  . LEU   A 69  ? 0.430317 0.404662 0.572994 -0.0163743  0.0837109   0.0533281   81  LEU   B HB3  
1012 H HG   . LEU   A 69  ? 0.483226 0.43465  0.581098 -0.0401069  0.0815853   0.0420409   81  LEU   B HG   
1013 H HD11 . LEU   A 69  ? 0.468701 0.434792 0.510458 -0.0406926  0.0581692   0.0348477   81  LEU   B HD11 
1014 H HD12 . LEU   A 69  ? 0.472197 0.419213 0.515055 -0.0609447  0.0686642   0.0166832   81  LEU   B HD12 
1015 H HD13 . LEU   A 69  ? 0.469417 0.435483 0.527708 -0.0532699  0.0647082   0.0171689   81  LEU   B HD13 
1016 H HD21 . LEU   A 69  ? 0.553658 0.495825 0.693183 -0.046246   0.101287    0.0184527   81  LEU   B HD21 
1017 H HD22 . LEU   A 69  ? 0.546784 0.501723 0.65995  -0.0544597  0.0936823   0.00781587  81  LEU   B HD22 
1018 H HD23 . LEU   A 69  ? 0.555477 0.486381 0.650053 -0.0639098  0.0945991   0.00316781  81  LEU   B HD23 
1019 N N    . GLY   A 70  ? 0.396146 0.368754 0.47764  0.0012056   0.0782589   0.0950216   82  GLY   B N    
1020 C CA   . GLY   A 70  ? 0.478932 0.444112 0.582502 0.0021169   0.0933641   0.114103    82  GLY   B CA   
1021 C C    . GLY   A 70  ? 0.544758 0.518815 0.637335 0.0301487   0.102456    0.148968    82  GLY   B C    
1022 O O    . GLY   A 70  ? 0.595021 0.563584 0.720538 0.0323191   0.121349    0.171721    82  GLY   B O    
1023 H H    . GLY   A 70  ? 0.402911 0.37824  0.458386 -0.00260105 0.0686558   0.0851437   82  GLY   B H    
1024 H HA2  . GLY   A 70  ? 0.459134 0.42221  0.553998 -0.00811413 0.0906668   0.106567    82  GLY   B HA2  
1025 H HA3  . GLY   A 70  ? 0.466557 0.421613 0.603557 -0.00516074 0.101356    0.112128    82  GLY   B HA3  
1026 N N    . LYS   A 71  ? 0.542787 0.528356 0.594987 0.0520936   0.0897053   0.153845    83  LYS   B N    
1027 C CA   . LYS   A 71  ? 0.533668 0.524165 0.56392  0.0851327   0.0977836   0.188135    83  LYS   B CA   
1028 C C    . LYS   A 71  ? 0.689078 0.68424  0.663175 0.101181    0.0968137   0.193686    83  LYS   B C    
1029 O O    . LYS   A 71  ? 0.826978 0.826075 0.753824 0.13284     0.0938971   0.211185    83  LYS   B O    
1030 C CB   . LYS   A 71  ? 0.530104 0.529299 0.547501 0.106122    0.0805059   0.191608    83  LYS   B CB   
1031 H H    . LYS   A 71  ? 0.526141 0.515766 0.562545 0.0470705   0.0747786   0.135327    83  LYS   B H    
1032 H HA   . LYS   A 71  ? 0.565842 0.549794 0.627206 0.0860145   0.116843    0.208121    83  LYS   B HA   
1035 N N    . GLY   A 72  ? 0.734719 0.727903 0.710113 0.0821248   0.0972709   0.177136    84  GLY   B N    
1036 C CA   . GLY   A 72  ? 0.796381 0.791898 0.728661 0.094544    0.099083    0.178339    84  GLY   B CA   
1037 C C    . GLY   A 72  ? 0.830631 0.825919 0.694973 0.114141    0.0743708   0.162004    84  GLY   B C    
1038 O O    . GLY   A 72  ? 0.804767 0.798259 0.622232 0.135585    0.0790466   0.16714     84  GLY   B O    
1039 H H    . GLY   A 72  ? 0.698533 0.687701 0.703808 0.060822    0.0962313   0.16363     84  GLY   B H    
1040 H HA2  . GLY   A 72  ? 0.763224 0.75693  0.710137 0.0762917   0.0971333   0.164594    84  GLY   B HA2  
1041 H HA3  . GLY   A 72  ? 0.805614 0.803493 0.740715 0.109271    0.119462    0.20396     84  GLY   B HA3  
1042 N N    . GLN   A 73  ? 0.65202  0.648629 0.515576 0.106154    0.0480186   0.139752    85  GLN   B N    
1043 C CA   . GLN   A 73  ? 0.640351 0.636233 0.452135 0.120427    0.0178892   0.119272    85  GLN   B CA   
1044 C C    . GLN   A 73  ? 0.567029 0.553368 0.370428 0.0995805   0.00273024  0.0881102   85  GLN   B C    
1045 O O    . GLN   A 73  ? 0.582593 0.561506 0.342252 0.110992    -0.0191856  0.0700002   85  GLN   B O    
1046 C CB   . GLN   A 73  ? 0.60096  0.607125 0.429446 0.120612    -0.00692435 0.109412    85  GLN   B CB   
1047 C CG   . GLN   A 73  ? 0.677194 0.690704 0.520385 0.141157    0.00536215  0.140983    85  GLN   B CG   
1048 C CD   . GLN   A 73  ? 0.722409 0.74946  0.606965 0.135028    -0.014918   0.131015    85  GLN   B CD   
1049 O OE1  . GLN   A 73  ? 0.682616 0.716113 0.595302 0.11183     -0.0329386  0.102104    85  GLN   B OE1  
1050 N NE2  . GLN   A 73  ? 0.710032 0.741506 0.604251 0.157099    -0.0077209  0.159212    85  GLN   B NE2  
1051 H H    . GLN   A 73  ? 0.655794 0.65375  0.555706 0.0909291   0.0483871   0.135858    85  GLN   B H    
1052 H HA   . GLN   A 73  ? 0.667942 0.66193  0.438028 0.145903    0.0214709   0.131424    85  GLN   B HA   
1053 H HB2  . GLN   A 73  ? 0.590691 0.598453 0.456172 0.0966989   -0.00927709 0.0952769   85  GLN   B HB2  
1054 H HB3  . GLN   A 73  ? 0.649028 0.654986 0.44412  0.131778    -0.0296635  0.0959758   85  GLN   B HB3  
1055 H HG2  . GLN   A 73  ? 0.717252 0.729632 0.516227 0.168173    0.00330958  0.154304    85  GLN   B HG2  
1056 H HG3  . GLN   A 73  ? 0.65927  0.669098 0.530831 0.133317    0.0296141   0.156232    85  GLN   B HG3  
1057 H HE21 . GLN   A 73  ? 0.720055 0.761101 0.638695 0.158602    -0.0197988  0.156612    85  GLN   B HE21 
1058 H HE22 . GLN   A 73  ? 0.739048 0.763968 0.617971 0.171133    0.010116    0.182354    85  GLN   B HE22 
1059 N N    . VAL   A 74  ? 0.469123 0.45142  0.308316 0.0722926   0.0150633   0.0832447   86  VAL   B N    
1060 C CA   . VAL   A 74  ? 0.47999  0.449624 0.308364 0.0553185   0.00476736  0.0605928   86  VAL   B CA   
1061 C C    . VAL   A 74  ? 0.443772 0.410614 0.283847 0.0496478   0.0248457   0.0717154   86  VAL   B C    
1062 O O    . VAL   A 74  ? 0.466983 0.442803 0.33516  0.0524385   0.0446176   0.0930708   86  VAL   B O    
1063 C CB   . VAL   A 74  ? 0.460157 0.427669 0.322967 0.0247102   -0.0041888  0.0415501   86  VAL   B CB   
1064 C CG1  . VAL   A 74  ? 0.497137 0.471228 0.36152  0.0273238   -0.0276396  0.0273459   86  VAL   B CG1  
1065 C CG2  . VAL   A 74  ? 0.413041 0.3868   0.320779 0.0108528   0.0145125   0.0520041   86  VAL   B CG2  
1066 H H    . VAL   A 74  ? 0.472256 0.457827 0.342455 0.0646664   0.0294289   0.0943522   86  VAL   B H    
1067 H HA   . VAL   A 74  ? 0.499146 0.462723 0.293383 0.0677854   -0.00822477 0.0514458   86  VAL   B HA   
1068 H HB   . VAL   A 74  ? 0.453435 0.410196 0.309468 0.0135976   -0.00641542 0.0319289   86  VAL   B HB   
1069 H HG11 . VAL   A 74  ? 0.498193 0.483059 0.366751 0.0408346   -0.0275862  0.0378682   86  VAL   B HG11 
1070 H HG12 . VAL   A 74  ? 0.512093 0.478729 0.348271 0.0352043   -0.0422653  0.0171391   86  VAL   B HG12 
1071 H HG13 . VAL   A 74  ? 0.473351 0.448075 0.364763 0.00843591  -0.0285302  0.0179761   86  VAL   B HG13 
1072 H HG21 . VAL   A 74  ? 0.406091 0.376673 0.329355 -0.00654713 0.0127264   0.0400409   86  VAL   B HG21 
1073 H HG22 . VAL   A 74  ? 0.413224 0.384302 0.324973 0.00958069  0.0260184   0.0604975   86  VAL   B HG22 
1074 H HG23 . VAL   A 74  ? 0.424561 0.406933 0.342357 0.021549    0.0165807   0.0618232   86  VAL   B HG23 
1075 N N    . ILE   A 75  ? 0.428146 0.38271  0.254908 0.0406939   0.0179095   0.0576421   87  ILE   B N    
1076 C CA   . ILE   A 75  ? 0.438619 0.39395  0.282889 0.035343    0.0309003   0.0665011   87  ILE   B CA   
1077 C C    . ILE   A 75  ? 0.40635  0.366581 0.298184 0.0109301   0.0373542   0.0691272   87  ILE   B C    
1078 O O    . ILE   A 75  ? 0.375519 0.330947 0.275293 -0.00540849 0.0302533   0.056346    87  ILE   B O    
1079 C CB   . ILE   A 75  ? 0.456747 0.394988 0.277198 0.0317467   0.0186691   0.050829    87  ILE   B CB   
1080 C CG1  . ILE   A 75  ? 0.46804  0.389909 0.286405 0.007507    0.00149623  0.0297645   87  ILE   B CG1  
1081 C CG2  . ILE   A 75  ? 0.519526 0.449695 0.295429 0.0600279   0.0163138   0.0480631   87  ILE   B CG2  
1082 C CD1  . ILE   A 75  ? 0.524647 0.424205 0.324862 0.00170209  -0.00811867 0.0193562   87  ILE   B CD1  
1083 H H    . ILE   A 75  ? 0.446994 0.392444 0.256185 0.0384407   0.00349112  0.0425554   87  ILE   B H    
1084 H HA   . ILE   A 75  ? 0.448027 0.41126  0.289865 0.0526586   0.0438847   0.0821229   87  ILE   B HA   
1085 H HB   . ILE   A 75  ? 0.452873 0.394465 0.291148 0.027062    0.0247488   0.0571256   87  ILE   B HB   
1086 H HG12 . ILE   A 75  ? 0.482414 0.403035 0.290699 0.0110848   -0.00684205 0.0223273   87  ILE   B HG12 
1087 H HG13 . ILE   A 75  ? 0.4544   0.380551 0.295618 -0.00763118 0.00556833  0.0310833   87  ILE   B HG13 
1088 H HG21 . ILE   A 75  ? 0.518482 0.436572 0.285103 0.058831    0.0111468   0.0402571   87  ILE   B HG21 
1089 H HG22 . ILE   A 75  ? 0.526742 0.451682 0.282891 0.0642003   0.00469832  0.0380531   87  ILE   B HG22 
1090 H HG23 . ILE   A 75  ? 0.520917 0.462001 0.296702 0.0769212   0.0316362   0.0639461   87  ILE   B HG23 
1091 H HD11 . ILE   A 75  ? 0.504071 0.406704 0.313961 0.00080465  -0.00275277 0.0269961   87  ILE   B HD11 
1092 H HD12 . ILE   A 75  ? 0.508065 0.397825 0.31124  -0.0145541  -0.0141624  0.0107267   87  ILE   B HD12 
1093 H HD13 . ILE   A 75  ? 0.532644 0.423741 0.309842 0.0161813   -0.0134257  0.0142469   87  ILE   B HD13 
1094 N N    . LYS   A 76  ? 0.44723  0.415813 0.370696 0.00891331  0.048848    0.0822729   88  LYS   B N    
1095 C CA   . LYS   A 76  ? 0.399035 0.36949  0.368947 -0.0124397  0.0511202   0.0815928   88  LYS   B CA   
1096 C C    . LYS   A 76  ? 0.441081 0.395032 0.395659 -0.0343201  0.0353733   0.0575512   88  LYS   B C    
1097 O O    . LYS   A 76  ? 0.411766 0.360519 0.383629 -0.048171   0.0367215   0.0495229   88  LYS   B O    
1098 C CB   . LYS   A 76  ? 0.415252 0.398544 0.428124 -0.0133774  0.0576696   0.094744    88  LYS   B CB   
1099 H H    . LYS   A 76  ? 0.437264 0.410422 0.355017 0.0218955   0.0545424   0.0906778   88  LYS   B H    
1100 H HA   . LYS   A 76  ? 0.415479 0.389055 0.401893 -0.0110492  0.0592858   0.0886935   88  LYS   B HA   
1103 N N    . ALA   A 77  ? 0.410134 0.353126 0.331597 -0.035547   0.0233194   0.0476725   89  ALA   B N    
1104 C CA   . ALA   A 77  ? 0.426114 0.3509   0.32828  -0.0540043  0.012769    0.0309945   89  ALA   B CA   
1105 C C    . ALA   A 77  ? 0.436445 0.355496 0.333133 -0.0624864  0.0165578   0.0212594   89  ALA   B C    
1106 O O    . ALA   A 77  ? 0.414409 0.322232 0.306798 -0.077376   0.0178118   0.0109255   89  ALA   B O    
1107 C CB   . ALA   A 77  ? 0.45787  0.368582 0.32757  -0.0507375  0.00207943  0.0276303   89  ALA   B CB   
1108 H H    . ALA   A 77  ? 0.428184 0.373183 0.337204 -0.0231047  0.0233189   0.0526586   89  ALA   B H    
1109 H HA   . ALA   A 77  ? 0.428742 0.353107 0.345404 -0.0627084  0.0107547   0.0287895   89  ALA   B HA   
1110 H HB1  . ALA   A 77  ? 0.453913 0.370185 0.331209 -0.0441163  -0.00022223 0.0340676   89  ALA   B HB1  
1111 H HB2  . ALA   A 77  ? 0.457147 0.365364 0.313339 -0.0428347  0.00192551  0.0266654   89  ALA   B HB2  
1112 H HB3  . ALA   A 77  ? 0.460906 0.358229 0.316496 -0.0621349  -0.00232035 0.0202678   89  ALA   B HB3  
1113 N N    . TRP   A 78  ? 0.420545 0.349242 0.319255 -0.0506095  0.018796    0.025081    90  TRP   B N    
1114 C CA   . TRP   A 78  ? 0.424477 0.354533 0.332197 -0.0575971  0.0205074   0.0168919   90  TRP   B CA   
1115 C C    . TRP   A 78  ? 0.424879 0.362501 0.365712 -0.0601645  0.0328797   0.0203409   90  TRP   B C    
1116 O O    . TRP   A 78  ? 0.461149 0.394831 0.413027 -0.0712702  0.0394675   0.0105656   90  TRP   B O    
1117 C CB   . TRP   A 78  ? 0.370651 0.308037 0.270196 -0.0443118  0.0102041   0.015858    90  TRP   B CB   
1118 C CG   . TRP   A 78  ? 0.427197 0.35038  0.308203 -0.0515075  -0.0021607  0.00331808  90  TRP   B CG   
1119 C CD1  . TRP   A 78  ? 0.422131 0.325937 0.277946 -0.0544286  -0.00742534 0.00015608  90  TRP   B CD1  
1120 C CD2  . TRP   A 78  ? 0.408073 0.33495  0.304759 -0.057507   -0.011712   -0.00734321 90  TRP   B CD2  
1121 N NE1  . TRP   A 78  ? 0.441211 0.331864 0.294478 -0.0626193  -0.0177913  -0.011196   90  TRP   B NE1  
1122 C CE2  . TRP   A 78  ? 0.500284 0.406434 0.382101 -0.0662731  -0.0211235  -0.0167221  90  TRP   B CE2  
1123 C CE3  . TRP   A 78  ? 0.365096 0.31137  0.293402 -0.0558413  -0.0144867  -0.00905245 90  TRP   B CE3  
1124 C CZ2  . TRP   A 78  ? 0.461623 0.366411 0.365425 -0.0762101  -0.032898   -0.0285197  90  TRP   B CZ2  
1125 C CZ3  . TRP   A 78  ? 0.401784 0.351969 0.353572 -0.0647452  -0.0274539  -0.0210143  90  TRP   B CZ3  
1126 C CH2  . TRP   A 78  ? 0.474824 0.404322 0.41546  -0.075279   -0.0376424  -0.0313218  90  TRP   B CH2  
1127 H H    . TRP   A 78  ? 0.427156 0.362134 0.321356 -0.0369109  0.0187064   0.0327632   90  TRP   B H    
1128 H HA   . TRP   A 78  ? 0.41753  0.336656 0.316576 -0.069824   0.0198282   0.00843039  90  TRP   B HA   
1129 H HB2  . TRP   A 78  ? 0.398661 0.340944 0.288684 -0.0290129  0.0094334   0.0243341   90  TRP   B HB2  
1130 H HB3  . TRP   A 78  ? 0.389063 0.335544 0.307354 -0.0443858  0.0121453   0.0155178   90  TRP   B HB3  
1131 H HD1  . TRP   A 78  ? 0.426381 0.32651  0.272977 -0.0513381  -0.00484312 0.00553846  90  TRP   B HD1  
1132 H HE1  . TRP   A 78  ? 0.466089 0.341059 0.306432 -0.0653736  -0.0218053  -0.0138957  90  TRP   B HE1  
1133 H HE3  . TRP   A 78  ? 0.372832 0.329975 0.312297 -0.0491982  -0.00747702 -0.00146954 90  TRP   B HE3  
1134 H HZ2  . TRP   A 78  ? 0.491214 0.379114 0.389284 -0.0827554  -0.0387043  -0.0340672  90  TRP   B HZ2  
1135 H HZ3  . TRP   A 78  ? 0.404655 0.371441 0.383328 -0.0624604  -0.0315471  -0.0219838  90  TRP   B HZ3  
1136 H HH2  . TRP   A 78  ? 0.463522 0.395742 0.428762 -0.083436   -0.0466911  -0.0394699  90  TRP   B HH2  
1137 N N    . ASP   A 79  ? 0.415635 0.362479 0.374809 -0.0484311  0.0389199   0.0353987   91  ASP   B N    
1138 C CA   . ASP   A 79  ? 0.439159 0.387475 0.435467 -0.0504583  0.0508308   0.0398808   91  ASP   B CA   
1139 C C    . ASP   A 79  ? 0.474071 0.40629  0.475856 -0.0697417  0.0515411   0.0233695   91  ASP   B C    
1140 O O    . ASP   A 79  ? 0.419647 0.343503 0.437501 -0.0764734  0.0593436   0.0131207   91  ASP   B O    
1141 C CB   . ASP   A 79  ? 0.412387 0.370686 0.428714 -0.034416   0.0597177   0.0641233   91  ASP   B CB   
1142 C CG   . ASP   A 79  ? 0.417636 0.387491 0.429607 -0.0112481  0.0635761   0.0822273   91  ASP   B CG   
1143 O OD1  . ASP   A 79  ? 0.419939 0.393313 0.427981 -0.00858781 0.0566191   0.0747604   91  ASP   B OD1  
1144 O OD2  . ASP   A 79  ? 0.506853 0.483324 0.519415 0.00602202  0.0736611   0.105348    91  ASP   B OD2  
1145 H H    . ASP   A 79  ? 0.425382 0.37636  0.375599 -0.0381842  0.0374101   0.0440086   91  ASP   B H    
1146 H HA   . ASP   A 79  ? 0.433111 0.385115 0.43609  -0.0479786  0.0524934   0.037891    91  ASP   B HA   
1147 H HB2  . ASP   A 79  ? 0.418528 0.378989 0.424064 -0.0315106  0.0573916   0.0683255   91  ASP   B HB2  
1148 H HB3  . ASP   A 79  ? 0.417443 0.37151  0.463071 -0.0408441  0.0665434   0.0658006   91  ASP   B HB3  
1149 N N    . ILE   A 80  ? 0.444246 0.370425 0.427977 -0.0761769  0.0416527   0.0191697   92  ILE   B N    
1150 C CA   . ILE   A 80  ? 0.472146 0.381721 0.44877  -0.0910086  0.0354723   0.00219737  92  ILE   B CA   
1151 C C    . ILE   A 80  ? 0.53215  0.42645  0.469878 -0.0991791  0.0377206   -0.0131546  92  ILE   B C    
1152 O O    . ILE   A 80  ? 0.431494 0.311659 0.366174 -0.106083   0.0448111   -0.0281572  92  ILE   B O    
1153 C CB   . ILE   A 80  ? 0.437926 0.349938 0.41268  -0.0920873  0.0203392   0.00551626  92  ILE   B CB   
1154 C CG1  . ILE   A 80  ? 0.541082 0.468927 0.570053 -0.0871801  0.0242872   0.0212058   92  ILE   B CG1  
1155 C CG2  . ILE   A 80  ? 0.554915 0.44732  0.502747 -0.104537   0.00622374  -0.0144254  92  ILE   B CG2  
1156 C CD1  . ILE   A 80  ? 0.496276 0.436592 0.53453  -0.0834108  0.0130598   0.0301369   92  ILE   B CD1  
1157 H H    . ILE   A 80  ? 0.451139 0.3832   0.424938 -0.0693171  0.0374831   0.0267603   92  ILE   B H    
1158 H HA   . ILE   A 80  ? 0.473368 0.379656 0.475202 -0.0937704  0.040151    -0.00093946 92  ILE   B HA   
1159 H HB   . ILE   A 80  ? 0.475942 0.391708 0.431208 -0.0859852  0.0177188   0.0115774   92  ILE   B HB   
1160 H HG12 . ILE   A 80  ? 0.50977  0.430756 0.562174 -0.0952766  0.0234806   0.0133397   92  ILE   B HG12 
1161 H HG13 . ILE   A 80  ? 0.49184  0.428489 0.529848 -0.0772462  0.0358637   0.0343593   92  ILE   B HG13 
1162 H HG21 . ILE   A 80  ? 0.529837 0.426441 0.485057 -0.104768   -0.00645103 -0.0124344  92  ILE   B HG21 
1163 H HG22 . ILE   A 80  ? 0.536816 0.420906 0.495885 -0.109981   0.00894175  -0.0249372  92  ILE   B HG22 
1164 H HG23 . ILE   A 80  ? 0.536093 0.419032 0.447751 -0.10563    0.00692474  -0.0185807  92  ILE   B HG23 
1165 H HD11 . ILE   A 80  ? 0.505339 0.447886 0.51639  -0.0749043  0.0133338   0.0350137   92  ILE   B HD11 
1166 H HD12 . ILE   A 80  ? 0.502135 0.455416 0.580257 -0.0793325  0.0203715   0.0436941   92  ILE   B HD12 
1167 H HD13 . ILE   A 80  ? 0.520951 0.453828 0.554399 -0.0923917  -0.00155283 0.0178709   92  ILE   B HD13 
1168 N N    . GLY   A 81  ? 0.440752 0.33599  0.352001 -0.097288   0.0350242   -0.00909093 93  GLY   B N    
1169 C CA   . GLY   A 81  ? 0.499302 0.378205 0.377157 -0.106409   0.0403456   -0.0182285  93  GLY   B CA   
1170 C C    . GLY   A 81  ? 0.508004 0.392412 0.404904 -0.108615   0.0582736   -0.0223587  93  GLY   B C    
1171 O O    . GLY   A 81  ? 0.552292 0.423446 0.434911 -0.114862   0.0723956   -0.0322746  93  GLY   B O    
1172 H H    . GLY   A 81  ? 0.457388 0.361667 0.371608 -0.0898518  0.0310727   -0.00025179 93  GLY   B H    
1173 H HA2  . GLY   A 81  ? 0.513119 0.378835 0.372195 -0.111094   0.0383548   -0.0257943  93  GLY   B HA2  
1174 H HA3  . GLY   A 81  ? 0.493677 0.370091 0.355607 -0.105601   0.0345417   -0.0135082  93  GLY   B HA3  
1175 N N    . VAL   A 82  ? 0.460533 0.365681 0.392005 -0.100341   0.058166    -0.0150406  94  VAL   B N    
1176 C CA   . VAL   A 82  ? 0.444139 0.360905 0.406405 -0.10041    0.0713726   -0.017851   94  VAL   B CA   
1177 C C    . VAL   A 82  ? 0.447996 0.360635 0.430335 -0.0989854  0.0869055   -0.0249857  94  VAL   B C    
1178 O O    . VAL   A 82  ? 0.449261 0.361913 0.444769 -0.101673   0.105665    -0.0324575  94  VAL   B O    
1179 C CB   . VAL   A 82  ? 0.466109 0.405953 0.455895 -0.089662   0.060115    -0.00957484 94  VAL   B CB   
1180 C CG1  . VAL   A 82  ? 0.52939  0.486765 0.562947 -0.0886221  0.0701311   -0.0120431  94  VAL   B CG1  
1181 C CG2  . VAL   A 82  ? 0.443934 0.379634 0.411706 -0.0931179  0.0455918   -0.00984934 94  VAL   B CG2  
1182 H H    . VAL   A 82  ? 0.451693 0.364516 0.387274 -0.0929711  0.0494167   -0.00769135 94  VAL   B H    
1183 H HA   . VAL   A 82  ? 0.465745 0.376331 0.41765  -0.108139   0.078029    -0.02154    94  VAL   B HA   
1184 H HB   . VAL   A 82  ? 0.456852 0.401298 0.450058 -0.0799282  0.0549948   -0.00241982 94  VAL   B HB   
1185 H HG11 . VAL   A 82  ? 0.518361 0.470294 0.551997 -0.0983253  0.0822449   -0.0178744  94  VAL   B HG11 
1186 H HG12 . VAL   A 82  ? 0.505903 0.465817 0.556068 -0.0822947  0.0769087   -0.0102872  94  VAL   B HG12 
1187 H HG13 . VAL   A 82  ? 0.502644 0.473915 0.549389 -0.0835254  0.0576735   -0.00923084 94  VAL   B HG13 
1188 H HG21 . VAL   A 82  ? 0.447587 0.395788 0.428467 -0.0859758  0.0350188   -0.00829256 94  VAL   B HG21 
1189 H HG22 . VAL   A 82  ? 0.453094 0.379661 0.39684  -0.0909095  0.0394928   -0.00723322 94  VAL   B HG22 
1190 H HG23 . VAL   A 82  ? 0.461451 0.389953 0.427159 -0.103746   0.0528747   -0.0141493  94  VAL   B HG23 
1191 N N    . ALA   A 83  ? 0.487655 0.392734 0.472437 -0.0959534  0.0814288   -0.0244755  95  ALA   B N    
1192 C CA   . ALA   A 83  ? 0.475395 0.369099 0.480709 -0.0951708  0.0934924   -0.0344962  95  ALA   B CA   
1193 C C    . ALA   A 83  ? 0.550656 0.419379 0.518457 -0.103735   0.103415    -0.0553074  95  ALA   B C    
1194 O O    . ALA   A 83  ? 0.513168 0.368565 0.491495 -0.101344   0.118023    -0.0693109  95  ALA   B O    
1195 C CB   . ALA   A 83  ? 0.53312  0.42269  0.561243 -0.0924762  0.0848287   -0.0285404  95  ALA   B CB   
1196 H H    . ALA   A 83  ? 0.464402 0.370985 0.44211  -0.0942657  0.0706382   -0.0180571  95  ALA   B H    
1197 H HA   . ALA   A 83  ? 0.491572 0.395678 0.523864 -0.0891709  0.102458    -0.0314     95  ALA   B HA   
1198 H HB1  . ALA   A 83  ? 0.496618 0.400788 0.54335  -0.0842813  0.0826729   -0.0128097  95  ALA   B HB1  
1199 H HB2  . ALA   A 83  ? 0.518878 0.401913 0.528048 -0.0980939  0.0744249   -0.0315466  95  ALA   B HB2  
1200 H HB3  . ALA   A 83  ? 0.527412 0.405689 0.572557 -0.0926174  0.0922061   -0.0369588  95  ALA   B HB3  
1201 N N    . THR   A 84  ? 0.480181 0.338838 0.40017  -0.110719   0.0960665   -0.057269   96  THR   B N    
1202 C CA   . THR   A 84  ? 0.573105 0.404691 0.441889 -0.114745   0.106264    -0.0743767  96  THR   B CA   
1203 C C    . THR   A 84  ? 0.618546 0.45273  0.479701 -0.115318   0.134173    -0.0714895  96  THR   B C    
1204 O O    . THR   A 84  ? 0.56944  0.380897 0.381751 -0.115417   0.150767    -0.0811508  96  THR   B O    
1205 C CB   . THR   A 84  ? 0.591421 0.407768 0.407318 -0.119161   0.0853024   -0.0746522  96  THR   B CB   
1206 O OG1  . THR   A 84  ? 0.573654 0.398977 0.378754 -0.121404   0.0833052   -0.0569578  96  THR   B OG1  
1207 C CG2  . THR   A 84  ? 0.598672 0.417869 0.432685 -0.119805   0.0580388   -0.0758918  96  THR   B CG2  
1208 H H    . THR   A 84  ? 0.493374 0.359608 0.408267 -0.11122    0.0850332   -0.047681   96  THR   B H    
1209 H HA   . THR   A 84  ? 0.587198 0.407012 0.460116 -0.112811   0.109217    -0.0875995  96  THR   B HA   
1210 H HB   . THR   A 84  ? 0.636889 0.433198 0.413002 -0.119142   0.0909417   -0.0863235  96  THR   B HB   
1212 H HG21 . THR   A 84  ? 0.608092 0.41969  0.411474 -0.12133    0.0439576   -0.0761402  96  THR   B HG21 
1213 H HG22 . THR   A 84  ? 0.556288 0.393852 0.424151 -0.117678   0.0553592   -0.0629068  96  THR   B HG22 
1214 H HG23 . THR   A 84  ? 0.606986 0.416914 0.451573 -0.120015   0.0574908   -0.0890099  96  THR   B HG23 
1215 N N    . MET   A 85  ? 0.586168 0.44743  0.492963 -0.11521    0.139331    -0.05746    97  MET   B N    
1216 C CA   . MET   A 85  ? 0.59854  0.465591 0.5103   -0.11963    0.163314    -0.0518436  97  MET   B CA   
1217 C C    . MET   A 85  ? 0.562531 0.441737 0.517825 -0.113115   0.191804    -0.0577529  97  MET   B C    
1218 O O    . MET   A 85  ? 0.531017 0.423363 0.529573 -0.104743   0.187046    -0.0602458  97  MET   B O    
1219 C CB   . MET   A 85  ? 0.583287 0.472783 0.527622 -0.124798   0.148233    -0.0369442  97  MET   B CB   
1220 C CG   . MET   A 85  ? 0.598186 0.47311  0.500879 -0.12908    0.125675    -0.0307652  97  MET   B CG   
1221 S SD   . MET   A 85  ? 0.518375 0.408358 0.44815  -0.132554   0.104149    -0.0203103  97  MET   B SD   
1222 C CE   . MET   A 85  ? 0.591174 0.482931 0.549701 -0.146201   0.131236    -0.014796   97  MET   B CE   
1223 H H    . MET   A 85  ? 0.554899 0.431108 0.491137 -0.112147   0.127808    -0.0511309  97  MET   B H    
1224 H HA   . MET   A 85  ? 0.626397 0.473853 0.493433 -0.12261    0.170919    -0.0536357  97  MET   B HA   
1225 H HB2  . MET   A 85  ? 0.554524 0.461643 0.533404 -0.119379   0.137646    -0.0352884  97  MET   B HB2  
1226 H HB3  . MET   A 85  ? 0.590033 0.48596  0.551965 -0.129378   0.164145    -0.0332171  97  MET   B HB3  
1227 H HG2  . MET   A 85  ? 0.613811 0.470393 0.480798 -0.13304    0.135458    -0.030355   97  MET   B HG2  
1228 H HG3  . MET   A 85  ? 0.57653  0.447667 0.467392 -0.124621   0.111984    -0.0337845  97  MET   B HG3  
1229 H HE1  . MET   A 85  ? 0.567524 0.466742 0.550148 -0.150228   0.118995    -0.0122517  97  MET   B HE1  
1230 H HE2  . MET   A 85  ? 0.576196 0.48189  0.564626 -0.144656   0.14647     -0.017443   97  MET   B HE2  
1231 H HE3  . MET   A 85  ? 0.607055 0.47805  0.52964  -0.150279   0.143403    -0.0110526  97  MET   B HE3  
1232 N N    . LYS   A 86  ? 0.619582 0.496112 0.569174 -0.115623   0.224545    -0.056038   98  LYS   B N    
1233 C CA   . LYS   A 86  ? 0.589387 0.484535 0.591971 -0.109157   0.257875    -0.0574794  98  LYS   B CA   
1234 C C    . LYS   A 86  ? 0.587327 0.521225 0.664833 -0.11667    0.257804    -0.0414088  98  LYS   B C    
1235 O O    . LYS   A 86  ? 0.577925 0.511225 0.645943 -0.128842   0.244108    -0.0310514  98  LYS   B O    
1236 C CB   . LYS   A 86  ? 0.640475 0.508641 0.590151 -0.104664   0.299777    -0.0648101  98  LYS   B CB   
1237 H H    . LYS   A 86  ? 0.626834 0.489408 0.538839 -0.120818   0.227963    -0.0519205  98  LYS   B H    
1238 H HA   . LYS   A 86  ? 0.587198 0.48625  0.612435 -0.100832   0.253363    -0.0648457  98  LYS   B HA   
1241 N N    . LYS   A 87  ? 0.526133 0.49188  0.68086  -0.108717   0.272442    -0.0409018  99  LYS   B N    
1242 C CA   . LYS   A 87  ? 0.496875 0.504928 0.7385   -0.114357   0.270815    -0.0294684  99  LYS   B CA   
1243 C C    . LYS   A 87  ? 0.511757 0.514216 0.748185 -0.129843   0.298918    -0.0188778  99  LYS   B C    
1244 O O    . LYS   A 87  ? 0.535317 0.517468 0.734815 -0.126144   0.340662    -0.0195368  99  LYS   B O    
1245 C CB   . LYS   A 87  ? 0.425253 0.470901 0.757421 -0.102877   0.291321    -0.0287414  99  LYS   B CB   
1246 H H    . LYS   A 87  ? 0.54559  0.505477 0.700389 -0.09847    0.282468    -0.0493562  99  LYS   B H    
1247 H HA   . LYS   A 87  ? 0.453297 0.470715 0.704117 -0.117125   0.238259    -0.0266907  99  LYS   B HA   
1250 N N    . GLY   A 88  ? 0.527182 0.539795 0.78835  -0.145519   0.275163    -0.00965473 100 GLY   B N    
1251 C CA   . GLY   A 88  ? 0.516153 0.521262 0.784432 -0.162196   0.301559    0.00456767  100 GLY   B CA   
1252 C C    . GLY   A 88  ? 0.569575 0.528087 0.741297 -0.168481   0.296535    0.0094239   100 GLY   B C    
1253 O O    . GLY   A 88  ? 0.60127  0.546013 0.771672 -0.182279   0.314585    0.0252488   100 GLY   B O    
1254 H H    . GLY   A 88  ? 0.480881 0.503022 0.754268 -0.14516    0.242565    -0.0120339  100 GLY   B H    
1255 H HA2  . GLY   A 88  ? 0.51245  0.539885 0.841043 -0.171825   0.286139    0.00841921  100 GLY   B HA2  
1256 H HA3  . GLY   A 88  ? 0.557231 0.566215 0.839533 -0.159134   0.339675    0.00860956  100 GLY   B HA3  
1257 N N    . GLU   A 89  ? 0.56449  0.498704 0.661715 -0.158329   0.272629    -0.00178496 101 GLU   B N    
1258 C CA   . GLU   A 89  ? 0.638602 0.531841 0.646653 -0.160697   0.264669    0.00211667  101 GLU   B CA   
1259 C C    . GLU   A 89  ? 0.649026 0.540372 0.669051 -0.171925   0.229323    0.00863315  101 GLU   B C    
1260 O O    . GLU   A 89  ? 0.562084 0.477497 0.627263 -0.170899   0.196371    0.00128147  101 GLU   B O    
1261 C CB   . GLU   A 89  ? 0.637948 0.512167 0.581333 -0.146934   0.247942    -0.0139622  101 GLU   B CB   
1262 C CG   . GLU   A 89  ? 0.665578 0.501293 0.519761 -0.146747   0.235408    -0.0114848  101 GLU   B CG   
1263 C CD   . GLU   A 89  ? 0.664932 0.486125 0.471669 -0.136111   0.21307     -0.0291274  101 GLU   B CD   
1264 O OE1  . GLU   A 89  ? 0.685759 0.504154 0.488625 -0.127075   0.228603    -0.0446106  101 GLU   B OE1  
1265 O OE2  . GLU   A 89  ? 0.617724 0.432063 0.401968 -0.136603   0.178645    -0.0286006  101 GLU   B OE2  
1266 H H    . GLU   A 89  ? 0.552807 0.496741 0.658766 -0.149501   0.26044     -0.0110084  101 GLU   B H    
1267 H HA   . GLU   A 89  ? 0.675484 0.553698 0.660126 -0.162731   0.294525    0.0109101   101 GLU   B HA   
1268 H HB2  . GLU   A 89  ? 0.656672 0.529507 0.595605 -0.139555   0.269718    -0.0209209  101 GLU   B HB2  
1269 H HB3  . GLU   A 89  ? 0.59912  0.487832 0.567097 -0.144398   0.222668    -0.0192394  101 GLU   B HB3  
1270 H HG2  . GLU   A 89  ? 0.649356 0.48516  0.50977  -0.152802   0.215987    -0.0043481  101 GLU   B HG2  
1271 H HG3  . GLU   A 89  ? 0.711228 0.530049 0.533102 -0.146905   0.260827    -0.00471837 101 GLU   B HG3  
1272 N N    . ILE   A 90  ? 0.635809 0.494874 0.609039 -0.179335   0.236522    0.0221696   102 ILE   B N    
1273 C CA   . ILE   A 90  ? 0.692115 0.535676 0.653862 -0.18534    0.203044    0.0258388   102 ILE   B CA   
1274 C C    . ILE   A 90  ? 0.710219 0.52032  0.580286 -0.175312   0.191368    0.0263395   102 ILE   B C    
1275 O O    . ILE   A 90  ? 0.716826 0.500999 0.529717 -0.172378   0.216151    0.0357461   102 ILE   B O    
1276 C CB   . ILE   A 90  ? 0.70637  0.5376   0.70409  -0.202678   0.215389    0.0429872   102 ILE   B CB   
1277 C CG1  . ILE   A 90  ? 0.669228 0.538686 0.774937 -0.215317   0.222396    0.0412473   102 ILE   B CG1  
1278 C CG2  . ILE   A 90  ? 0.695116 0.501333 0.667544 -0.204036   0.179068    0.0428177   102 ILE   B CG2  
1279 C CD1  . ILE   A 90  ? 0.750726 0.61149  0.915911 -0.236632   0.234169    0.0567774   102 ILE   B CD1  
1280 H H    . ILE   A 90  ? 0.699601 0.544053 0.645254 -0.178859   0.264524    0.0299394   102 ILE   B H    
1281 H HA   . ILE   A 90  ? 0.637338 0.498638 0.627475 -0.183075   0.177505    0.0161981   102 ILE   B HA   
1282 H HB   . ILE   A 90  ? 0.744517 0.557    0.710824 -0.203414   0.244135    0.0561086   102 ILE   B HB   
1283 H HG12 . ILE   A 90  ? 0.649286 0.537123 0.779399 -0.211875   0.192359    0.0277789   102 ILE   B HG12 
1284 H HG13 . ILE   A 90  ? 0.689042 0.573383 0.808201 -0.21181    0.248328    0.0423732   102 ILE   B HG13 
1285 H HG21 . ILE   A 90  ? 0.713306 0.511234 0.71828  -0.215832   0.18331     0.0510229   102 ILE   B HG21 
1286 H HG22 . ILE   A 90  ? 0.663904 0.485121 0.64969  -0.19888    0.151586    0.0293711   102 ILE   B HG22 
1287 H HG23 . ILE   A 90  ? 0.718761 0.5015   0.630212 -0.197055   0.179514    0.0480636   102 ILE   B HG23 
1288 H HD11 . ILE   A 90  ? 0.772617 0.61449  0.913324 -0.239095   0.267628    0.0738868   102 ILE   B HD11 
1289 H HD12 . ILE   A 90  ? 0.718362 0.608542 0.958208 -0.244086   0.235269    0.0532344   102 ILE   B HD12 
1290 H HD13 . ILE   A 90  ? 0.731444 0.575373 0.886873 -0.239714   0.207559    0.0534979   102 ILE   B HD13 
1291 N N    . ALA   A 91  ? 0.577332 0.389304 0.436112 -0.168796   0.15355     0.0174264   103 ALA   B N    
1292 C CA   . ALA   A 91  ? 0.646114 0.433746 0.435246 -0.159332   0.135837    0.0176452   103 ALA   B CA   
1293 C C    . ALA   A 91  ? 0.592293 0.368521 0.379348 -0.158788   0.107801    0.0222028   103 ALA   B C    
1294 O O    . ALA   A 91  ? 0.604073 0.39554  0.437763 -0.16132    0.0925533   0.0166775   103 ALA   B O    
1295 C CB   . ALA   A 91  ? 0.617195 0.418913 0.397505 -0.14869    0.12081     0.00264219  103 ALA   B CB   
1296 H H    . ALA   A 91  ? 0.579939 0.410061 0.476707 -0.169101   0.138013    0.0114223   103 ALA   B H    
1297 H HA   . ALA   A 91  ? 0.667823 0.434868 0.416818 -0.159197   0.152375    0.0254559   103 ALA   B HA   
1298 H HB1  . ALA   A 91  ? 0.628615 0.433517 0.408125 -0.147714   0.138025    -0.0024786  103 ALA   B HB1  
1299 H HB2  . ALA   A 91  ? 0.582374 0.402822 0.397454 -0.146965   0.107048    -0.00183781 103 ALA   B HB2  
1300 H HB3  . ALA   A 91  ? 0.629801 0.418043 0.372109 -0.14362    0.107616    0.0026837   103 ALA   B HB3  
1301 N N    . HIS   A 92  ? 0.622763 0.372766 0.352246 -0.151857   0.09791     0.0294921   104 HIS   B N    
1302 C CA   . HIS   A 92  ? 0.609704 0.348976 0.331482 -0.145235   0.0704751   0.0319998   104 HIS   B CA   
1303 C C    . HIS   A 92  ? 0.605856 0.357313 0.30866  -0.131417   0.0468641   0.0237331   104 HIS   B C    
1304 O O    . HIS   A 92  ? 0.650228 0.397347 0.317852 -0.127384   0.0463009   0.0220505   104 HIS   B O    
1305 C CB   . HIS   A 92  ? 0.663406 0.36315  0.34335  -0.145762   0.0760362   0.0513732   104 HIS   B CB   
1306 C CG   . HIS   A 92  ? 0.687612 0.370321 0.398717 -0.160179   0.0955529   0.0636031   104 HIS   B CG   
1307 N ND1  . HIS   A 92  ? 0.804419 0.448199 0.489163 -0.162946   0.107914    0.0860654   104 HIS   B ND1  
1308 C CD2  . HIS   A 92  ? 0.661819 0.3624   0.436388 -0.172936   0.102787    0.0567903   104 HIS   B CD2  
1309 C CE1  . HIS   A 92  ? 0.78933  0.428268 0.527864 -0.179933   0.126298    0.0927175   104 HIS   B CE1  
1310 N NE2  . HIS   A 92  ? 0.673496 0.349724 0.470067 -0.186314   0.120089    0.0726286   104 HIS   B NE2  
1311 H H    . HIS   A 92  ? 0.651315 0.389399 0.343886 -0.149502   0.108267    0.0326513   104 HIS   B H    
1312 H HA   . HIS   A 92  ? 0.592735 0.341126 0.350745 -0.147997   0.0635534   0.027488    104 HIS   B HA   
1313 H HB2  . HIS   A 92  ? 0.693282 0.38358  0.3337   -0.142725   0.0851082   0.0561474   104 HIS   B HB2  
1314 H HB3  . HIS   A 92  ? 0.661858 0.354441 0.331016 -0.137696   0.0567549   0.0521948   104 HIS   B HB3  
1316 H HD2  . HIS   A 92  ? 0.623161 0.350025 0.427081 -0.17283    0.096741    0.0437411   104 HIS   B HD2  
1317 H HE1  . HIS   A 92  ? 0.814009 0.427105 0.553333 -0.186057   0.139202    0.10931     104 HIS   B HE1  
1319 N N    . LEU   A 93  ? 0.56632  0.334553 0.29648  -0.12358    0.0277986   0.0175293   105 LEU   B N    
1320 C CA   . LEU   A 93  ? 0.551875 0.335209 0.279868 -0.110826   0.00999281  0.0141264   105 LEU   B CA   
1321 C C    . LEU   A 93  ? 0.560466 0.332265 0.280794 -0.0991145  -0.00655288 0.020202    105 LEU   B C    
1322 O O    . LEU   A 93  ? 0.527477 0.291614 0.26089  -0.097248   -0.00924618 0.0183245   105 LEU   B O    
1323 C CB   . LEU   A 93  ? 0.507798 0.321972 0.274726 -0.106784   0.00940332  0.00583785  105 LEU   B CB   
1324 C CG   . LEU   A 93  ? 0.551318 0.380429 0.337794 -0.113898   0.0244206   -0.00107324 105 LEU   B CG   
1325 C CD1  . LEU   A 93  ? 0.581088 0.437889 0.404196 -0.104503   0.0200517   -0.00336787 105 LEU   B CD1  
1326 C CD2  . LEU   A 93  ? 0.549131 0.370019 0.311269 -0.117058   0.028993    -0.00522654 105 LEU   B CD2  
1327 H H    . LEU   A 93  ? 0.559524 0.329857 0.312475 -0.125934   0.0267984   0.0156242   105 LEU   B H    
1328 H HA   . LEU   A 93  ? 0.565003 0.345033 0.272519 -0.110775   0.00925867  0.0141078   105 LEU   B HA   
1329 H HB2  . LEU   A 93  ? 0.513284 0.329397 0.293874 -0.104783   0.00665059  0.00460376  105 LEU   B HB2  
1330 H HB3  . LEU   A 93  ? 0.510587 0.333881 0.279913 -0.0983033  0.00027316  0.00683952  105 LEU   B HB3  
1331 H HG   . LEU   A 93  ? 0.553001 0.378552 0.347044 -0.121195   0.0347853   -0.00131587 105 LEU   B HG   
1332 H HD11 . LEU   A 93  ? 0.555458 0.415637 0.387503 -0.101298   0.0157725   -0.00326373 105 LEU   B HD11 
1333 H HD12 . LEU   A 93  ? 0.553971 0.419058 0.3925   -0.107653   0.0292218   -0.00695032 105 LEU   B HD12 
1334 H HD13 . LEU   A 93  ? 0.553726 0.415234 0.375723 -0.0974804  0.012719    -0.00064894 105 LEU   B HD13 
1335 H HD21 . LEU   A 93  ? 0.585    0.387239 0.317164 -0.120385   0.0327454   -0.00184194 105 LEU   B HD21 
1336 H HD22 . LEU   A 93  ? 0.549847 0.375657 0.312136 -0.111713   0.0167985   -0.00578359 105 LEU   B HD22 
1337 H HD23 . LEU   A 93  ? 0.550394 0.378594 0.326754 -0.1201     0.0401219   -0.0110036  105 LEU   B HD23 
1338 N N    . LEU   A 94  ? 0.564087 0.333606 0.264748 -0.0901588  -0.0196322  0.0255655   106 LEU   B N    
1339 C CA   . LEU   A 94  ? 0.566091 0.331683 0.267892 -0.0744936  -0.0344708  0.0315588   106 LEU   B CA   
1340 C C    . LEU   A 94  ? 0.599012 0.397624 0.329444 -0.0636797  -0.0429326  0.0296435   106 LEU   B C    
1341 O O    . LEU   A 94  ? 0.57066  0.381407 0.304511 -0.0684463  -0.0479488  0.0273263   106 LEU   B O    
1342 C CB   . LEU   A 94  ? 0.627434 0.364159 0.291829 -0.0711753  -0.0430788  0.0439923   106 LEU   B CB   
1343 C CG   . LEU   A 94  ? 0.636479 0.371246 0.306093 -0.051856   -0.0598065  0.0515066   106 LEU   B CG   
1344 C CD1  . LEU   A 94  ? 0.765388 0.478713 0.441878 -0.0471045  -0.0542246  0.0499771   106 LEU   B CD1  
1345 C CD2  . LEU   A 94  ? 0.772258 0.484989 0.40582  -0.0460496  -0.0733584  0.0652095   106 LEU   B CD2  
1346 H H    . LEU   A 94  ? 0.574953 0.345655 0.262735 -0.0929433  -0.0201559  0.0245492   106 LEU   B H    
1347 H HA   . LEU   A 94  ? 0.577941 0.337659 0.288481 -0.0721025  -0.0323413  0.0293368   106 LEU   B HA   
1348 H HB2  . LEU   A 94  ? 0.646707 0.36081  0.297844 -0.077823   -0.0340119  0.0482869   106 LEU   B HB2  
1349 H HB3  . LEU   A 94  ? 0.635335 0.375219 0.284245 -0.0741857  -0.0462899  0.0437819   106 LEU   B HB3  
1350 H HG   . LEU   A 94  ? 0.646209 0.407028 0.340201 -0.0452034  -0.0649373  0.0479602   106 LEU   B HG   
1351 H HD11 . LEU   A 94  ? 0.696398 0.424816 0.39167  -0.0479788  -0.0491968  0.0404068   106 LEU   B HD11 
1352 H HD12 . LEU   A 94  ? 0.73394  0.441833 0.411801 -0.0329578  -0.0624845  0.0544245   106 LEU   B HD12 
1353 H HD13 . LEU   A 94  ? 0.745804 0.434547 0.407446 -0.0563585  -0.0477751  0.0538871   106 LEU   B HD13 
1354 H HD21 . LEU   A 94  ? 0.744445 0.469444 0.370935 -0.0485088  -0.0807281  0.0626113   106 LEU   B HD21 
1355 H HD22 . LEU   A 94  ? 0.771294 0.457071 0.379966 -0.0521657  -0.0647647  0.0717707   106 LEU   B HD22 
1356 H HD23 . LEU   A 94  ? 0.748152 0.460305 0.390342 -0.032453   -0.0836928  0.0706419   106 LEU   B HD23 
1357 N N    . ILE   A 95  ? 0.602585 0.413961 0.354376 -0.0489413  -0.0427062  0.0300466   107 ILE   B N    
1358 C CA   . ILE   A 95  ? 0.508618 0.353381 0.29514  -0.0393442  -0.0393416  0.0315886   107 ILE   B CA   
1359 C C    . ILE   A 95  ? 0.518775 0.372819 0.319468 -0.0170158  -0.042926   0.0401585   107 ILE   B C    
1360 O O    . ILE   A 95  ? 0.516687 0.354952 0.301871 -0.00339048 -0.0409878  0.0383774   107 ILE   B O    
1361 C CB   . ILE   A 95  ? 0.494638 0.347335 0.287692 -0.0380724  -0.0274365  0.0256568   107 ILE   B CB   
1362 C CG1  . ILE   A 95  ? 0.503819 0.354214 0.296314 -0.0576279  -0.0211504  0.0183854   107 ILE   B CG1  
1363 C CG2  . ILE   A 95  ? 0.548522 0.431775 0.371623 -0.0235528  -0.0184873  0.0332609   107 ILE   B CG2  
1364 C CD1  . ILE   A 95  ? 0.512011 0.362552 0.30724  -0.0580639  -0.0165812  0.0110319   107 ILE   B CD1  
1365 H H    . ILE   A 95  ? 0.593404 0.389465 0.336056 -0.0436754  -0.0432233  0.0299658   107 ILE   B H    
1366 H HA   . ILE   A 95  ? 0.514346 0.370388 0.312828 -0.0465403  -0.0413727  0.0313839   107 ILE   B HA   
1367 H HB   . ILE   A 95  ? 0.522899 0.36133  0.301743 -0.0321682  -0.0290554  0.0222979   107 ILE   B HB   
1368 H HG12 . ILE   A 95  ? 0.48957  0.354848 0.299021 -0.060536   -0.0180443  0.0193377   107 ILE   B HG12 
1369 H HG13 . ILE   A 95  ? 0.51957  0.353327 0.294983 -0.0666893  -0.0232778  0.0175794   107 ILE   B HG13 
1370 H HG21 . ILE   A 95  ? 0.51694  0.405305 0.341196 -0.023386   -0.0122992  0.0307709   107 ILE   B HG21 
1371 H HG22 . ILE   A 95  ? 0.514875 0.410707 0.359048 -0.0288564  -0.0190016  0.0372558   107 ILE   B HG22 
1372 H HG23 . ILE   A 95  ? 0.532443 0.41665  0.353526 -0.00820784 -0.0178484  0.0373146   107 ILE   B HG23 
1373 H HD11 . ILE   A 95  ? 0.523604 0.359053 0.306331 -0.054333   -0.0218379  0.0080875   107 ILE   B HD11 
1374 H HD12 . ILE   A 95  ? 0.506182 0.354978 0.305099 -0.0705895  -0.0117142  0.0074268   107 ILE   B HD12 
1375 H HD13 . ILE   A 95  ? 0.495866 0.362891 0.303011 -0.0485551  -0.0137765  0.0128952   107 ILE   B HD13 
1376 N N    . LYS   A 96  ? 0.518189 0.397718 0.353245 -0.0131674  -0.0483897  0.0479805   108 LYS   B N    
1377 C CA   . LYS   A 96  ? 0.479122 0.376946 0.343309 0.0087448   -0.0467385  0.0587615   108 LYS   B CA   
1378 C C    . LYS   A 96  ? 0.512214 0.429917 0.39352  0.022946    -0.0237637  0.0632965   108 LYS   B C    
1379 O O    . LYS   A 96  ? 0.451066 0.378502 0.339652 0.013101    -0.0142031  0.0618275   108 LYS   B O    
1380 C CB   . LYS   A 96  ? 0.478864 0.400944 0.385627 0.00488877  -0.0628772  0.0652313   108 LYS   B CB   
1381 C CG   . LYS   A 96  ? 0.577589 0.477042 0.453798 -0.00081528 -0.0899681  0.0631039   108 LYS   B CG   
1382 C CD   . LYS   A 96  ? 0.664525 0.589498 0.581747 -0.0063355  -0.114512   0.0638204   108 LYS   B CD   
1383 C CE   . LYS   A 96  ? 0.691904 0.593685 0.566594 -0.00883517 -0.145362   0.0616165   108 LYS   B CE   
1384 N NZ   . LYS   A 96  ? 0.798328 0.728823 0.719121 -0.0157008  -0.17227    0.0559823   108 LYS   B NZ   
1385 H H    . LYS   A 96  ? 0.500468 0.386591 0.344456 -0.0246026  -0.053191   0.045839    108 LYS   B H    
1386 H HA   . LYS   A 96  ? 0.515975 0.394841 0.359117 0.018031    -0.0505933  0.058718    108 LYS   B HA   
1387 H HB2  . LYS   A 96  ? 0.476938 0.411462 0.402654 -0.00710915 -0.0614188  0.0624825   108 LYS   B HB2  
1388 H HB3  . LYS   A 96  ? 0.489452 0.430754 0.428482 0.0193122   -0.0581187  0.0742156   108 LYS   B HB3  
1389 H HG2  . LYS   A 96  ? 0.59536  0.483359 0.460733 0.0125548   -0.0918545  0.0683414   108 LYS   B HG2  
1390 H HG3  . LYS   A 96  ? 0.58664  0.46469  0.426643 -0.0129119  -0.0897985  0.0561726   108 LYS   B HG3  
1391 H HD2  . LYS   A 96  ? 0.62504  0.55981  0.55785  -0.0189448  -0.111669   0.0574095   108 LYS   B HD2  
1392 H HD3  . LYS   A 96  ? 0.632324 0.581014 0.593298 0.00562943  -0.113741   0.0724466   108 LYS   B HD3  
1393 H HE2  . LYS   A 96  ? 0.734421 0.628493 0.602031 0.00496854  -0.150559   0.0703351   108 LYS   B HE2  
1394 H HE3  . LYS   A 96  ? 0.730817 0.607886 0.559672 -0.0187938  -0.142272   0.0553947   108 LYS   B HE3  
1395 H HZ1  . LYS   A 96  ? 0.749733 0.705362 0.719849 -0.00671769 -0.174228   0.0635641   108 LYS   B HZ1  
1396 H HZ2  . LYS   A 96  ? 0.74571  0.681612 0.677299 -0.0279549  -0.166492   0.0475114   108 LYS   B HZ2  
1397 H HZ3  . LYS   A 96  ? 0.792818 0.710302 0.684354 -0.0158142  -0.193537   0.0534121   108 LYS   B HZ3  
1398 N N    . PRO   A 97  ? 0.538228 0.463265 0.427259 0.0494103   -0.0129656  0.071253    109 PRO   B N    
1399 C CA   . PRO   A 97  ? 0.536119 0.474994 0.425164 0.0696021   0.0118259   0.0774226   109 PRO   B CA   
1400 C C    . PRO   A 97  ? 0.476812 0.448964 0.411457 0.0636532   0.0279753   0.0917152   109 PRO   B C    
1401 O O    . PRO   A 97  ? 0.524932 0.498686 0.442138 0.0716169   0.0440882   0.0947315   109 PRO   B O    
1402 C CB   . PRO   A 97  ? 0.540469 0.486142 0.44009  0.100445    0.0232697   0.0863693   109 PRO   B CB   
1403 C CG   . PRO   A 97  ? 0.561289 0.503748 0.4823   0.0940425   0.00100239  0.0875231   109 PRO   B CG   
1404 C CD   . PRO   A 97  ? 0.552208 0.469312 0.444231 0.0649233   -0.0225813  0.0752312   109 PRO   B CD   
1405 H HA   . PRO   A 97  ? 0.537121 0.456855 0.388747 0.0705586   0.0115062   0.0670959   109 PRO   B HA   
1406 H HB2  . PRO   A 97  ? 0.543361 0.515459 0.475511 0.110613    0.0409241   0.100178    109 PRO   B HB2  
1407 H HB3  . PRO   A 97  ? 0.573189 0.49774  0.433811 0.114676    0.0266364   0.0776377   109 PRO   B HB3  
1408 H HG2  . PRO   A 97  ? 0.542984 0.513979 0.512523 0.0933013   0.0019886   0.0988244   109 PRO   B HG2  
1409 H HG3  . PRO   A 97  ? 0.579572 0.507244 0.485215 0.111032    0.00123028  0.0855992   109 PRO   B HG3  
1410 H HD2  . PRO   A 97  ? 0.549913 0.475423 0.463126 0.056253    -0.0365802  0.0789542   109 PRO   B HD2  
1411 H HD3  . PRO   A 97  ? 0.574358 0.462009 0.430184 0.0667733   -0.0282177  0.067066    109 PRO   B HD3  
1412 N N    . GLU   A 98  ? 0.535115 0.530442 0.527438 0.0491252   0.0206569   0.0995434   110 GLU   B N    
1413 C CA   . GLU   A 98  ? 0.511838 0.535995 0.56118  0.0421351   0.0368009   0.114326    110 GLU   B CA   
1414 C C    . GLU   A 98  ? 0.518682 0.528794 0.543281 0.026465    0.0381795   0.106125    110 GLU   B C    
1415 O O    . GLU   A 98  ? 0.430093 0.455103 0.486345 0.0267942   0.0570022   0.120149    110 GLU   B O    
1416 C CB   . GLU   A 98  ? 0.538847 0.586252 0.659194 0.0258444   0.0202163   0.117592    110 GLU   B CB   
1417 C CG   . GLU   A 98  ? 0.556809 0.626682 0.717817 0.0441863   0.0193334   0.129265    110 GLU   B CG   
1418 C CD   . GLU   A 98  ? 0.653291 0.701487 0.770517 0.05477     -0.00226283 0.118883    110 GLU   B CD   
1419 O OE1  . GLU   A 98  ? 0.521726 0.537443 0.584447 0.0400455   -0.025987   0.101567    110 GLU   B OE1  
1420 O OE2  . GLU   A 98  ? 0.660583 0.722388 0.798176 0.080828    0.00885635  0.130488    110 GLU   B OE2  
1421 H H    . GLU   A 98  ? 0.517098 0.508878 0.514901 0.0432122   0.00395814  0.0954797   110 GLU   B H    
1422 H HA   . GLU   A 98  ? 0.531019 0.568565 0.591153 0.0610348   0.0589677   0.128663    110 GLU   B HA   
1423 H HB2  . GLU   A 98  ? 0.530924 0.563075 0.632344 0.0100013   -0.00184851 0.102947    110 GLU   B HB2  
1424 H HB3  . GLU   A 98  ? 0.521139 0.584059 0.683214 0.0193111   0.0309746   0.126442    110 GLU   B HB3  
1425 H HG2  . GLU   A 98  ? 0.562695 0.6537   0.781774 0.033639    0.0096834   0.133149    110 GLU   B HG2  
1426 H HG3  . GLU   A 98  ? 0.576236 0.658531 0.747662 0.0626486   0.0453581   0.143535    110 GLU   B HG3  
1427 N N    . TYR   A 99  ? 0.464989 0.446956 0.440338 0.012527    0.0196065   0.085741    111 TYR   B N    
1428 C CA   . TYR   A 99  ? 0.438163 0.408807 0.39561  -0.00147906 0.0203517   0.0767421   111 TYR   B CA   
1429 C C    . TYR   A 99  ? 0.476988 0.431046 0.382036 0.0104378   0.0235139   0.0697005   111 TYR   B C    
1430 O O    . TYR   A 99  ? 0.456161 0.401549 0.346856 -7.181e-05  0.0209448   0.0605619   111 TYR   B O    
1431 C CB   . TYR   A 99  ? 0.431148 0.386533 0.382573 -0.0269806  0.00086776  0.0599002   111 TYR   B CB   
1432 C CG   . TYR   A 99  ? 0.417016 0.386173 0.418632 -0.0401467  -0.00842189 0.060397    111 TYR   B CG   
1433 C CD1  . TYR   A 99  ? 0.428387 0.407511 0.451891 -0.0375386  -0.0241454  0.0631599   111 TYR   B CD1  
1434 C CD2  . TYR   A 99  ? 0.47146  0.446381 0.509502 -0.052035   -0.00157593 0.0598114   111 TYR   B CD2  
1435 C CE1  . TYR   A 99  ? 0.455669 0.450566 0.53438  -0.0495427  -0.0384425  0.0613589   111 TYR   B CE1  
1436 C CE2  . TYR   A 99  ? 0.43849  0.425668 0.533565 -0.0636195  -0.0115758  0.0588913   111 TYR   B CE2  
1437 C CZ   . TYR   A 99  ? 0.404279 0.400613 0.516658 -0.0643365  -0.0333804  0.0566519   111 TYR   B CZ   
1438 O OH   . TYR   A 99  ? 0.462395 0.473895 0.63842  -0.0758145  -0.0495118  0.0536097   111 TYR   B OH   
1439 H H    . TYR   A 99  ? 0.481783 0.451734 0.43783  0.0121933   0.00724368  0.0786706   111 TYR   B H    
1440 H HA   . TYR   A 99  ? 0.437899 0.422649 0.426048 -0.0010658  0.0324945   0.0870927   111 TYR   B HA   
1441 H HB2  . TYR   A 99  ? 0.441283 0.382655 0.365236 -0.0270618  -0.00964097 0.0536499   111 TYR   B HB2  
1442 H HB3  . TYR   A 99  ? 0.426503 0.374245 0.365444 -0.0339247  0.00417203  0.0537525   111 TYR   B HB3  
1443 H HD1  . TYR   A 99  ? 0.443156 0.41646  0.444137 -0.0280826  -0.0283512  0.0644027   111 TYR   B HD1  
1444 H HD2  . TYR   A 99  ? 0.442005 0.412623 0.470343 -0.0511014  0.00961982  0.0605383   111 TYR   B HD2  
1445 H HE1  . TYR   A 99  ? 0.446308 0.450054 0.542543 -0.0474624  -0.0530676  0.0624754   111 TYR   B HE1  
1446 H HE2  . TYR   A 99  ? 0.432598 0.418508 0.552116 -0.0724061  -0.00775543 0.0563251   111 TYR   B HE2  
1448 N N    . ALA   A 100 ? 0.473821 0.424885 0.355039 0.0343585   0.0287413   0.0730112   112 ALA   B N    
1449 C CA   . ALA   A 100 ? 0.511335 0.443743 0.341725 0.0480857   0.0255755   0.0614964   112 ALA   B CA   
1450 C C    . ALA   A 100 ? 0.522958 0.464457 0.334782 0.0819899   0.044707    0.07362     112 ALA   B C    
1451 O O    . ALA   A 100 ? 0.502228 0.460771 0.324617 0.0901811   0.0612218   0.089709    112 ALA   B O    
1452 C CB   . ALA   A 100 ? 0.511562 0.415417 0.314335 0.0424816   0.00755543  0.0446277   112 ALA   B CB   
1453 H H    . ALA   A 100 ? 0.485928 0.446706 0.384725 0.0431853   0.0335995   0.0814075   112 ALA   B H    
1454 H HA   . ALA   A 100 ? 0.495188 0.426437 0.322224 0.0388113   0.0226138   0.0568918   112 ALA   B HA   
1455 H HB1  . ALA   A 100 ? 0.504904 0.401569 0.311693 0.0227382   -0.00111742 0.0385616   112 ALA   B HB1  
1456 H HB2  . ALA   A 100 ? 0.521134 0.426154 0.332363 0.0493018   0.00849014  0.049674    112 ALA   B HB2  
1457 H HB3  . ALA   A 100 ? 0.536288 0.426422 0.309863 0.0525444   0.00375265  0.03515     112 ALA   B HB3  
1458 N N    . TYR   A 101 ? 0.494295 0.422212 0.27681  0.104094    0.0453387   0.0677687   113 TYR   B N    
1459 C CA   . TYR   A 101 ? 0.586855 0.516783 0.334721 0.141442    0.065098    0.0751809   113 TYR   B CA   
1460 C C    . TYR   A 101 ? 0.59324  0.542767 0.371692 0.162488    0.0906817   0.0953995   113 TYR   B C    
1461 O O    . TYR   A 101 ? 0.601705 0.55341  0.349612 0.197048    0.114163    0.104312    113 TYR   B O    
1462 C CB   . TYR   A 101 ? 0.605027 0.500272 0.285682 0.158663    0.0483605   0.0482977   113 TYR   B CB   
1463 C CG   . TYR   A 101 ? 0.574689 0.46019  0.235545 0.142696    0.0258883   0.0322224   113 TYR   B CG   
1464 C CD1  . TYR   A 101 ? 0.613242 0.51008  0.250736 0.158085    0.0313606   0.0399736   113 TYR   B CD1  
1465 C CD2  . TYR   A 101 ? 0.601013 0.469852 0.275017 0.111709    0.00145054  0.0139331   113 TYR   B CD2  
1466 C CE1  . TYR   A 101 ? 0.566746 0.458793 0.194721 0.145203    0.00748664  0.0251682   113 TYR   B CE1  
1467 C CE2  . TYR   A 101 ? 0.586387 0.45238  0.257648 0.0961283   -0.0169989  0.00084587  113 TYR   B CE2  
1468 C CZ   . TYR   A 101 ? 0.580423 0.459866 0.231971 0.112602    -0.0163662  0.00518678  113 TYR   B CZ   
1469 O OH   . TYR   A 101 ? 0.561513 0.440958 0.218842 0.0979183   -0.0390863  -0.00928272 113 TYR   B OH   
1470 H H    . TYR   A 101 ? 0.520079 0.435113 0.301471 0.0974508   0.0341907   0.0591196   113 TYR   B H    
1471 H HA   . TYR   A 101 ? 0.57077  0.512465 0.31853  0.145039    0.0747389   0.0858262   113 TYR   B HA   
1472 H HB2  . TYR   A 101 ? 0.608027 0.486974 0.289898 0.15269     0.0374741   0.0372674   113 TYR   B HB2  
1473 H HB3  . TYR   A 101 ? 0.641092 0.53625  0.29282  0.186812    0.0627255   0.0524762   113 TYR   B HB3  
1474 H HD1  . TYR   A 101 ? 0.618462 0.525099 0.243225 0.180801    0.0512122   0.0554356   113 TYR   B HD1  
1475 H HD2  . TYR   A 101 ? 0.578411 0.437955 0.265308 0.101894    -0.00188468 0.0115794   113 TYR   B HD2  
1476 H HE1  . TYR   A 101 ? 0.603554 0.502996 0.213158 0.158861    0.00912898  0.031341    113 TYR   B HE1  
1477 H HE2  . TYR   A 101 ? 0.571455 0.426466 0.254994 0.0758947   -0.0297051  -0.00987482 113 TYR   B HE2  
1479 N N    . GLY   A 102 ? 0.55542  0.520996 0.394067 0.143562    0.0864748   0.103267    114 GLY   B N    
1480 C CA   . GLY   A 102 ? 0.555904 0.553531 0.453041 0.156609    0.109915    0.127384    114 GLY   B CA   
1481 C C    . GLY   A 102 ? 0.648282 0.637226 0.52483  0.18939     0.120403    0.12476     114 GLY   B C    
1482 O O    . GLY   A 102 ? 0.613819 0.565785 0.434374 0.196169    0.102316    0.100475    114 GLY   B O    
1483 H H    . GLY   A 102 ? 0.537401 0.494093 0.382023 0.12197     0.0671989   0.0929997   114 GLY   B H    
1484 H HA2  . GLY   A 102 ? 0.538214 0.547017 0.479818 0.136358    0.0979132   0.129264    114 GLY   B HA2  
1485 H HA3  . GLY   A 102 ? 0.569192 0.584043 0.480288 0.164752    0.131788    0.144748    114 GLY   B HA3  
1486 N N    . SER   A 103 ? 0.630217 0.654165 0.562992 0.207613    0.150578    0.150763    115 SER   B N    
1487 C CA   . SER   A 103 ? 0.723389 0.749116 0.653882 0.243521    0.17075     0.154881    115 SER   B CA   
1488 C C    . SER   A 103 ? 0.786571 0.782601 0.625479 0.280661    0.189023    0.143781    115 SER   B C    
1489 O O    . SER   A 103 ? 0.812918 0.78394  0.613646 0.307051    0.189435    0.127938    115 SER   B O    
1490 C CB   . SER   A 103 ? 0.755634 0.832188 0.777546 0.254392    0.204833    0.189067    115 SER   B CB   
1491 O OG   . SER   A 103 ? 0.780563 0.878312 0.881541 0.225593    0.176282    0.189905    115 SER   B OG   
1492 H H    . SER   A 103 ? 0.626059 0.674385 0.605743 0.196867    0.160074    0.167087    115 SER   B H    
1493 H HA   . SER   A 103 ? 0.71534  0.726788 0.645814 0.237992    0.149129    0.141592    115 SER   B HA   
1494 H HB2  . SER   A 103 ? 0.755451 0.84725  0.791401 0.251545    0.223336    0.205322    115 SER   B HB2  
1495 H HB3  . SER   A 103 ? 0.793961 0.87247  0.807914 0.284247    0.226625    0.193937    115 SER   B HB3  
1497 N N    . ALA   A 104 ? 0.835043 0.832382 0.63782  0.2857      0.203667    0.152185    116 ALA   B N    
1498 C CA   . ALA   A 104 ? 0.896678 0.868005 0.605438 0.325897    0.220085    0.142974    116 ALA   B CA   
1499 C C    . ALA   A 104 ? 0.850443 0.77279  0.483717 0.318403    0.177132    0.100534    116 ALA   B C    
1500 O O    . ALA   A 104 ? 0.881767 0.771124 0.434802 0.350805    0.176567    0.0788149   116 ALA   B O    
1501 C CB   . ALA   A 104 ? 0.897829 0.886481 0.591331 0.335585    0.247281    0.169907    116 ALA   B CB   
1502 H H    . ALA   A 104 ? 0.791393 0.804556 0.626081 0.265505    0.202442    0.163497    116 ALA   B H    
1503 H HA   . ALA   A 104 ? 0.917129 0.890485 0.622544 0.35402     0.242308    0.147555    116 ALA   B HA   
1504 H HB1  . ALA   A 104 ? 0.892324 0.910871 0.639919 0.339832    0.277078    0.198437    116 ALA   B HB1  
1505 H HB2  . ALA   A 104 ? 0.869373 0.856589 0.570365 0.309399    0.226348    0.165689    116 ALA   B HB2  
1506 H HB3  . ALA   A 104 ? 0.957681 0.927933 0.580742 0.364817    0.25593     0.163401    116 ALA   B HB3  
1507 N N    . GLY   A 105 ? 0.828986 0.746025 0.487628 0.275721    0.141693    0.0883714   117 GLY   B N    
1508 C CA   . GLY   A 105 ? 0.844461 0.720569 0.448961 0.262928    0.10306     0.0524793   117 GLY   B CA   
1509 C C    . GLY   A 105 ? 0.922061 0.788855 0.460642 0.279133    0.0998758   0.0448631   117 GLY   B C    
1510 O O    . GLY   A 105 ? 0.887279 0.781141 0.431232 0.288735    0.124335    0.0721513   117 GLY   B O    
1511 H H    . GLY   A 105 ? 0.778078 0.717143 0.490558 0.253967    0.141793    0.102276    117 GLY   B H    
1512 H HA2  . GLY   A 105 ? 0.810431 0.688556 0.446332 0.231618    0.0845232   0.0497472   117 GLY   B HA2  
1513 H HA3  . GLY   A 105 ? 0.881859 0.733494 0.46361  0.275506    0.0965755   0.0358527   117 GLY   B HA3  
1514 N N    . SER   A 106 ? 0.87283  0.702005 0.359575 0.277002    0.0654062   0.00896089  118 SER   B N    
1515 C CA   . SER   A 106 ? 0.965634 0.784543 0.387928 0.293792    0.0520871   -0.00364071 118 SER   B CA   
1516 C C    . SER   A 106 ? 1.06357  0.835333 0.416946 0.317766    0.0296911   -0.0439906  118 SER   B C    
1517 O O    . SER   A 106 ? 1.0336   0.778717 0.380196 0.297029    -0.010696   -0.07611    118 SER   B O    
1518 C CB   . SER   A 106 ? 0.914318 0.743976 0.362517 0.258884    0.0250889   -0.00646871 118 SER   B CB   
1519 O OG   . SER   A 106 ? 0.890505 0.72452  0.286475 0.281632    0.0207027   -0.00420359 118 SER   B OG   
1520 H H    . SER   A 106 ? 0.897208 0.706693 0.391366 0.265075    0.0486817   -0.00752205 118 SER   B H    
1521 H HA   . SER   A 106 ? 0.982175 0.816876 0.386432 0.318074    0.0783192   0.0169903   118 SER   B HA   
1522 H HB2  . SER   A 106 ? 0.84614  0.699033 0.346307 0.238791    0.0369295   0.0139885   118 SER   B HB2  
1523 H HB3  . SER   A 106 ? 0.894033 0.704181 0.346285 0.240737    -0.00146329 -0.0298001  118 SER   B HB3  
1525 N N    . LEU   A 107 ? 1.14195  0.907243 0.454675 0.361376    0.0613616   -0.038294   119 LEU   B N    
1526 C CA   . LEU   A 107 ? 1.33103  1.05197  0.59452  0.389376    0.0553395   -0.0706613  119 LEU   B CA   
1527 C C    . LEU   A 107 ? 1.45499  1.13669  0.629187 0.408666    0.0190863   -0.111908   119 LEU   B C    
1528 O O    . LEU   A 107 ? 1.41436  1.10572  0.526163 0.438788    0.028523    -0.103605   119 LEU   B O    
1529 C CB   . LEU   A 107 ? 1.3711   1.10357  0.615047 0.436564    0.107492    -0.0481666  119 LEU   B CB   
1530 C CG   . LEU   A 107 ? 1.25454  1.01357  0.581487 0.431457    0.139279    -0.020245   119 LEU   B CG   
1531 C CD1  . LEU   A 107 ? 1.24293  1.00669  0.539313 0.488083    0.191061    -0.00599226 119 LEU   B CD1  
1532 C CD2  . LEU   A 107 ? 1.13684  0.866828 0.503712 0.403981    0.107971    -0.0432318  119 LEU   B CD2  
1533 H H    . LEU   A 107 ? 1.15865  0.948898 0.477146 0.375423    0.0910949   -0.0112613  119 LEU   B H    
1534 H HA   . LEU   A 107 ? 1.28026  0.98875  0.582479 0.366501    0.0408735   -0.0802925  119 LEU   B HA   
1535 H HB2  . LEU   A 107 ? 1.36714  1.12165  0.592515 0.451507    0.128404    -0.0265911  119 LEU   B HB2  
1536 H HB3  . LEU   A 107 ? 1.42801  1.1266   0.610758 0.465422    0.102858    -0.073971   119 LEU   B HB3  
1537 H HG   . LEU   A 107 ? 1.17253  0.967882 0.553729 0.410108    0.149398    0.00753945  119 LEU   B HG   
1538 H HD11 . LEU   A 107 ? 1.26994  1.06016  0.560588 0.500934    0.218252    0.0196741   119 LEU   B HD11 
1539 H HD12 . LEU   A 107 ? 1.2362   1.01342  0.588804 0.484649    0.204045    0.00593603  119 LEU   B HD12 
1540 H HD13 . LEU   A 107 ? 1.33445  1.06085  0.56314  0.514547    0.183444    -0.0343074  119 LEU   B HD13 
1541 H HD21 . LEU   A 107 ? 1.1196   0.849999 0.509558 0.369505    0.0820696   -0.0476291  119 LEU   B HD21 
1542 H HD22 . LEU   A 107 ? 1.2194   0.910405 0.538797 0.422653    0.0966071   -0.0716078  119 LEU   B HD22 
1543 H HD23 . LEU   A 107 ? 1.13355  0.882614 0.551011 0.403378    0.12564     -0.0243924  119 LEU   B HD23 
1544 N N    . PRO   A 108 ? 1.51181  1.14456  0.670316 0.399738    -0.0206304  -0.157142   120 PRO   B N    
1545 C CA   . PRO   A 108 ? 1.43972  1.05334  0.661556 0.371012    -0.028256   -0.163879   120 PRO   B CA   
1546 C C    . PRO   A 108 ? 1.3528   0.967564 0.639111 0.315187    -0.0632625  -0.169465   120 PRO   B C    
1547 O O    . PRO   A 108 ? 1.32759  0.925434 0.663021 0.290984    -0.0681117  -0.170033   120 PRO   B O    
1548 C CB   . PRO   A 108 ? 1.59443  1.14568  0.754466 0.401652    -0.0450424  -0.209368   120 PRO   B CB   
1549 C CG   . PRO   A 108 ? 1.74099  1.27429  0.819828 0.420473    -0.0774136  -0.242081   120 PRO   B CG   
1550 C CD   . PRO   A 108 ? 1.64841  1.23588  0.719102 0.425204    -0.0576737  -0.204708   120 PRO   B CD   
1551 H HA   . PRO   A 108 ? 1.41749  1.05277  0.67397  0.373514    0.00103219  -0.137447   120 PRO   B HA   
1552 H HB2  . PRO   A 108 ? 1.58412  1.11008  0.776889 0.378597    -0.0652622  -0.224425   120 PRO   B HB2  
1553 H HB3  . PRO   A 108 ? 1.62704  1.1761   0.766392 0.433092    -0.0159177  -0.201987   120 PRO   B HB3  
1554 H HG2  . PRO   A 108 ? 1.70599  1.22176  0.803263 0.393827    -0.11442    -0.265229   120 PRO   B HG2  
1555 H HG3  . PRO   A 108 ? 1.79079  1.29422  0.805347 0.457316    -0.074353   -0.263702   120 PRO   B HG3  
1556 H HD2  . PRO   A 108 ? 1.63905  1.232    0.715519 0.405622    -0.0871868  -0.213545   120 PRO   B HD2  
1557 H HD3  . PRO   A 108 ? 1.71109  1.29685  0.718323 0.464378    -0.0390986  -0.202293   120 PRO   B HD3  
1558 N N    . LYS   A 109 ? 1.29584  0.931054 0.583181 0.297125    -0.0847026  -0.17049    121 LYS   B N    
1559 C CA   . LYS   A 109 ? 1.16722  0.816982 0.524427 0.245407    -0.106891   -0.166518   121 LYS   B CA   
1560 C C    . LYS   A 109 ? 1.06563  0.733277 0.496629 0.213222    -0.086097   -0.136559   121 LYS   B C    
1561 O O    . LYS   A 109 ? 0.954811 0.605845 0.431657 0.178922    -0.0998498  -0.140916   121 LYS   B O    
1562 C CB   . LYS   A 109 ? 1.01646  0.711576 0.373464 0.244577    -0.101789   -0.144237   121 LYS   B CB   
1563 H H    . LYS   A 109 ? 1.32869  0.969022 0.569847 0.320087    -0.0845874  -0.173159   121 LYS   B H    
1564 H HA   . LYS   A 109 ? 1.17549  0.797515 0.531306 0.23427     -0.136892   -0.194694   121 LYS   B HA   
1567 N N    . ILE   A 110 ? 0.994939 0.700752 0.439543 0.224474    -0.0508667  -0.101561   122 ILE   B N    
1568 C CA   . ILE   A 110 ? 0.883358 0.610071 0.390849 0.199606    -0.0346877  -0.0744129  122 ILE   B CA   
1569 C C    . ILE   A 110 ? 0.875946 0.60601  0.379716 0.231195    -0.00587467 -0.0602036  122 ILE   B C    
1570 O O    . ILE   A 110 ? 0.902649 0.659152 0.390981 0.259714    0.0223075   -0.0420653  122 ILE   B O    
1571 C CB   . ILE   A 110 ? 0.790403 0.564168 0.337242 0.179753    -0.0217578  -0.0458278  122 ILE   B CB   
1572 C CG1  . ILE   A 110 ? 0.758301 0.536313 0.307677 0.15777     -0.0446916  -0.0570758  122 ILE   B CG1  
1573 C CG2  . ILE   A 110 ? 0.787308 0.578596 0.393397 0.155073    -0.0112338  -0.0235386  122 ILE   B CG2  
1574 C CD1  . ILE   A 110 ? 0.692818 0.453776 0.277679 0.118889    -0.0676177  -0.0706585  122 ILE   B CD1  
1575 H H    . ILE   A 110 ? 1.01375  0.73209  0.42818  0.248756    -0.037218   -0.0944218  122 ILE   B H    
1576 H HA   . ILE   A 110 ? 0.871673 0.579059 0.398857 0.178       -0.0499698  -0.0835798  122 ILE   B HA   
1577 H HB   . ILE   A 110 ? 0.812984 0.604156 0.344823 0.201993    -0.00295884 -0.0328219  122 ILE   B HB   
1578 H HG12 . ILE   A 110 ? 0.796405 0.562445 0.305776 0.175987    -0.0557115  -0.0729603  122 ILE   B HG12 
1579 H HG13 . ILE   A 110 ? 0.721728 0.527734 0.289437 0.153192    -0.0326918  -0.0384566  122 ILE   B HG13 
1580 H HG21 . ILE   A 110 ? 0.732332 0.546837 0.363044 0.139184    -0.0076566  -0.0112162  122 ILE   B HG21 
1581 H HG22 . ILE   A 110 ? 0.76931  0.53895  0.383006 0.139256    -0.0254202  -0.0336082  122 ILE   B HG22 
1582 H HG23 . ILE   A 110 ? 0.774573 0.574678 0.386598 0.172093    0.00559501  -0.0115987  122 ILE   B HG23 
1583 H HD11 . ILE   A 110 ? 0.665407 0.438737 0.283049 0.10151     -0.057631   -0.054838   122 ILE   B HD11 
1584 H HD12 . ILE   A 110 ? 0.701815 0.468667 0.28978  0.109623    -0.0810479  -0.078434   122 ILE   B HD12 
1585 H HD13 . ILE   A 110 ? 0.734838 0.465765 0.307809 0.121389    -0.0784445  -0.0869512  122 ILE   B HD13 
1586 N N    . PRO   A 111 ? 0.881048 0.588204 0.406602 0.227768    -0.00841488 -0.0626853  123 PRO   B N    
1587 C CA   . PRO   A 111 ? 0.872838 0.588678 0.405102 0.260314    0.0194056   -0.0478969  123 PRO   B CA   
1588 C C    . PRO   A 111 ? 0.795587 0.567539 0.386828 0.252217    0.0436633   -0.00977999 123 PRO   B C    
1589 O O    . PRO   A 111 ? 0.756582 0.553589 0.383157 0.218855    0.0363032   0.003086    123 PRO   B O    
1590 C CB   . PRO   A 111 ? 0.924496 0.597065 0.466684 0.257165    0.00411228  -0.0612932  123 PRO   B CB   
1591 C CG   . PRO   A 111 ? 0.87868  0.533652 0.439758 0.213149    -0.0247644  -0.0687337  123 PRO   B CG   
1592 C CD   . PRO   A 111 ? 0.857038 0.532051 0.405899 0.195363    -0.0339231  -0.074487   123 PRO   B CD   
1593 H HA   . PRO   A 111 ? 0.92611  0.634753 0.416872 0.290237    0.0301772   -0.0564401  123 PRO   B HA   
1594 H HB2  . PRO   A 111 ? 0.896896 0.585359 0.472089 0.262017    0.0163219   -0.043038   123 PRO   B HB2  
1595 H HB3  . PRO   A 111 ? 0.969326 0.609749 0.473833 0.279686    0.00159432  -0.0822967  123 PRO   B HB3  
1596 H HG2  . PRO   A 111 ? 0.844545 0.514877 0.441983 0.196419    -0.0231066  -0.0501329  123 PRO   B HG2  
1597 H HG3  . PRO   A 111 ? 0.918525 0.53314  0.465258 0.213137    -0.0393176  -0.0879345  123 PRO   B HG3  
1598 H HD2  . PRO   A 111 ? 0.813891 0.508233 0.394256 0.169201    -0.0360289  -0.061053   123 PRO   B HD2  
1599 H HD3  . PRO   A 111 ? 0.891319 0.538559 0.417178 0.192379    -0.0524759  -0.0979557  123 PRO   B HD3  
1600 N N    . SER   A 112 ? 0.78547  0.575588 0.39039  0.284667    0.0732874   0.00639044  124 SER   B N    
1601 C CA   . SER   A 112 ? 0.758241 0.60044  0.433367 0.280945    0.0960767   0.0411346   124 SER   B CA   
1602 C C    . SER   A 112 ? 0.714217 0.563329 0.445213 0.243364    0.0711783   0.0479726   124 SER   B C    
1603 O O    . SER   A 112 ? 0.705825 0.522879 0.432721 0.241783    0.0527942   0.0365492   124 SER   B O    
1604 C CB   . SER   A 112 ? 0.831806 0.680444 0.513489 0.323435    0.126345    0.0498076   124 SER   B CB   
1605 O OG   . SER   A 112 ? 0.894135 0.798463 0.65352  0.323643    0.152109    0.0846752   124 SER   B OG   
1606 H H    . SER   A 112 ? 0.846347 0.614767 0.417715 0.311212    0.0795564   -0.0059945  124 SER   B H    
1607 H HA   . SER   A 112 ? 0.746364 0.612175 0.425318 0.277621    0.107845    0.0533032   124 SER   B HA   
1608 H HB2  . SER   A 112 ? 0.889509 0.725921 0.52154  0.349587    0.140916    0.0417042   124 SER   B HB2  
1609 H HB3  . SER   A 112 ? 0.858068 0.683539 0.541187 0.326657    0.114227    0.0393219   124 SER   B HB3  
1611 N N    . ASN   A 113 ? 0.681416 0.567976 0.460004 0.21611     0.0708885   0.0664263   125 ASN   B N    
1612 C CA   . ASN   A 113 ? 0.655702 0.554834 0.484332 0.185491    0.0497821   0.0746295   125 ASN   B CA   
1613 C C    . ASN   A 113 ? 0.663647 0.520375 0.458405 0.160981    0.0190602   0.0555891   125 ASN   B C    
1614 O O    . ASN   A 113 ? 0.622283 0.472437 0.436961 0.150509    0.00193818  0.0602194   125 ASN   B O    
1615 C CB   . ASN   A 113 ? 0.689291 0.608953 0.571364 0.202035    0.0538654   0.0900791   125 ASN   B CB   
1616 C CG   . ASN   A 113 ? 0.617423 0.589011 0.558799 0.218397    0.0859802   0.114994    125 ASN   B CG   
1617 O OD1  . ASN   A 113 ? 0.683397 0.667424 0.645371 0.251209    0.10833     0.124609    125 ASN   B OD1  
1618 N ND2  . ASN   A 113 ? 0.615625 0.619629 0.600497 0.194194    0.0875145   0.127926    125 ASN   B ND2  
1619 H H    . ASN   A 113 ? 0.673637 0.576799 0.450168 0.218165    0.0842627   0.0736936   125 ASN   B H    
1620 H HA   . ASN   A 113 ? 0.628025 0.551635 0.482727 0.16989     0.0526789   0.0842182   125 ASN   B HA   
1621 H HB2  . ASN   A 113 ? 0.700613 0.596532 0.558942 0.221975    0.0552599   0.0819626   125 ASN   B HB2  
1622 H HB3  . ASN   A 113 ? 0.64785  0.570332 0.552808 0.18301     0.0339913   0.0926359   125 ASN   B HB3  
1623 H HD21 . ASN   A 113 ? 0.597731 0.631881 0.625202 0.20143     0.10686     0.144415    125 ASN   B HD21 
1624 H HD22 . ASN   A 113 ? 0.585005 0.580049 0.559497 0.17091     0.0702214   0.120448    125 ASN   B HD22 
1625 N N    . ALA   A 114 ? 0.652492 0.486615 0.403767 0.149667    0.0124455   0.0381971   126 ALA   B N    
1626 C CA   . ALA   A 114 ? 0.670231 0.466656 0.398124 0.125134    -0.0109558  0.0222982   126 ALA   B CA   
1627 C C    . ALA   A 114 ? 0.598711 0.408715 0.350017 0.0896813   -0.0214871  0.0303232   126 ALA   B C    
1628 O O    . ALA   A 114 ? 0.581127 0.420555 0.350346 0.079005    -0.0144667  0.0366227   126 ALA   B O    
1629 C CB   . ALA   A 114 ? 0.688653 0.462789 0.374732 0.127896    -0.0152663  0.00062967  126 ALA   B CB   
1630 H H    . ALA   A 114 ? 0.662306 0.506398 0.401443 0.158103    0.0235604   0.0378563   126 ALA   B H    
1631 H HA   . ALA   A 114 ? 0.682871 0.456746 0.406953 0.13185     -0.0173564  0.0201601   126 ALA   B HA   
1632 H HB1  . ALA   A 114 ? 0.725045 0.486525 0.388959 0.152184    -0.0100144  -0.00732862 126 ALA   B HB1  
1633 H HB2  . ALA   A 114 ? 0.671329 0.467072 0.360299 0.123404    -0.00962905 0.0042925   126 ALA   B HB2  
1634 H HB3  . ALA   A 114 ? 0.695834 0.44558  0.374423 0.110907    -0.0295587  -0.00955214 126 ALA   B HB3  
1635 N N    . THR   A 115 ? 0.548398 0.333949 0.29697  0.0739835   -0.0368419  0.0314547   127 THR   B N    
1636 C CA   . THR   A 115 ? 0.544736 0.328974 0.293477 0.0428136   -0.0448719  0.0326843   127 THR   B CA   
1637 C C    . THR   A 115 ? 0.544644 0.303461 0.271465 0.0266851   -0.0471329  0.0171083   127 THR   B C    
1638 O O    . THR   A 115 ? 0.558187 0.280736 0.267389 0.0310029   -0.0530952  0.00632348  127 THR   B O    
1639 C CB   . THR   A 115 ? 0.559591 0.327389 0.306217 0.0368403   -0.0578399  0.043738    127 THR   B CB   
1640 O OG1  . THR   A 115 ? 0.575273 0.378379 0.354918 0.0450446   -0.0609574  0.056144    127 THR   B OG1  
1641 C CG2  . THR   A 115 ? 0.587088 0.346608 0.320239 0.00922224  -0.0628322  0.0455539   127 THR   B CG2  
1642 H H    . THR   A 115 ? 0.588328 0.356425 0.332656 0.0849118   -0.0406473  0.0324766   127 THR   B H    
1643 H HA   . THR   A 115 ? 0.514331 0.326358 0.281376 0.0373505   -0.0401668  0.0373855   127 THR   B HA   
1644 H HB   . THR   A 115 ? 0.602011 0.343281 0.336572 0.0465606   -0.0614123  0.0431886   127 THR   B HB   
1646 H HG21 . THR   A 115 ? 0.5947   0.345095 0.320831 0.00958552  -0.0717408  0.0543279   127 THR   B HG21 
1647 H HG22 . THR   A 115 ? 0.552191 0.336058 0.298517 0.00148164  -0.0596196  0.0445693   127 THR   B HG22 
1648 H HG23 . THR   A 115 ? 0.587363 0.325416 0.306005 -3.039e-05  -0.0598925  0.0391957   127 THR   B HG23 
1649 N N    . LEU   A 116 ? 0.531088 0.307288 0.266227 0.00651894  -0.0438191  0.0158819   128 LEU   B N    
1650 C CA   . LEU   A 116 ? 0.554629 0.317573 0.284661 -0.0101643  -0.0456316  0.00300501  128 LEU   B CA   
1651 C C    . LEU   A 116 ? 0.559181 0.31387  0.291968 -0.0368196  -0.043028   0.00869465  128 LEU   B C    
1652 O O    . LEU   A 116 ? 0.536443 0.305175 0.271075 -0.0428492  -0.0399856  0.0184335   128 LEU   B O    
1653 C CB   . LEU   A 116 ? 0.519919 0.311216 0.259077 -0.00757422 -0.0410608  -0.00319727 128 LEU   B CB   
1654 C CG   . LEU   A 116 ? 0.552283 0.357166 0.280408 0.0219979   -0.0371278  -0.00480255 128 LEU   B CG   
1655 C CD1  . LEU   A 116 ? 0.560614 0.380251 0.284766 0.0252157   -0.0387451  -0.0131662  128 LEU   B CD1  
1656 C CD2  . LEU   A 116 ? 0.619369 0.398613 0.324113 0.0431254   -0.041954   -0.0132605  128 LEU   B CD2  
1657 H H    . LEU   A 116 ? 0.511393 0.309441 0.260565 0.00301474  -0.0406282  0.0230194   128 LEU   B H    
1658 H HA   . LEU   A 116 ? 0.575687 0.314159 0.295314 -0.00532493 -0.0515711  -0.00547667 128 LEU   B HA   
1659 H HB2  . LEU   A 116 ? 0.504357 0.314661 0.257231 -0.016112   -0.0350291  0.00414851  128 LEU   B HB2  
1660 H HB3  . LEU   A 116 ? 0.533977 0.31628  0.273833 -0.0173305  -0.0458495  -0.0128641  128 LEU   B HB3  
1661 H HG   . LEU   A 116 ? 0.538438 0.363779 0.27983  0.0273963   -0.0280918  0.00772258  128 LEU   B HG   
1662 H HD11 . LEU   A 116 ? 0.531411 0.368876 0.274288 0.0135273   -0.0332948  -0.00618023 128 LEU   B HD11 
1663 H HD12 . LEU   A 116 ? 0.569495 0.396683 0.279667 0.0462803   -0.0337973  -0.0113335  128 LEU   B HD12 
1664 H HD13 . LEU   A 116 ? 0.573464 0.376453 0.291241 0.019015    -0.0504436  -0.0268852  128 LEU   B HD13 
1665 H HD21 . LEU   A 116 ? 0.60996  0.38853  0.320674 0.0482553   -0.0384277  -0.00386147 128 LEU   B HD21 
1666 H HD22 . LEU   A 116 ? 0.629589 0.383602 0.32707  0.0347143   -0.052413   -0.0250066  128 LEU   B HD22 
1667 H HD23 . LEU   A 116 ? 0.622528 0.408818 0.313168 0.0621765   -0.0382352  -0.0167861  128 LEU   B HD23 
1668 N N    . PHE   A 117 ? 0.583215 0.31453  0.317936 -0.0518483  -0.0439569  0.00089152  129 PHE   B N    
1669 C CA   . PHE   A 117 ? 0.568216 0.29045  0.307617 -0.0754677  -0.0343428  0.00702733  129 PHE   B CA   
1670 C C    . PHE   A 117 ? 0.531908 0.269337 0.299963 -0.0882796  -0.031698   -0.00499809 129 PHE   B C    
1671 O O    . PHE   A 117 ? 0.574029 0.304052 0.352909 -0.0847434  -0.0435614  -0.0188645  129 PHE   B O    
1672 C CB   . PHE   A 117 ? 0.668162 0.347558 0.394152 -0.0814107  -0.0337479  0.0167606   129 PHE   B CB   
1673 C CG   . PHE   A 117 ? 0.731827 0.401298 0.457327 -0.103262   -0.0161614  0.0286494   129 PHE   B CG   
1674 C CD1  . PHE   A 117 ? 0.718944 0.380326 0.477076 -0.122123   -0.00739099 0.024245    129 PHE   B CD1  
1675 C CD2  . PHE   A 117 ? 0.672938 0.341638 0.365706 -0.103319   -0.00836709 0.043877    129 PHE   B CD2  
1676 C CE1  . PHE   A 117 ? 0.80181  0.455544 0.562377 -0.139899   0.0163074   0.0388228   129 PHE   B CE1  
1677 C CE2  . PHE   A 117 ? 0.759127 0.418887 0.442047 -0.119039   0.0129553   0.0541884   129 PHE   B CE2  
1678 C CZ   . PHE   A 117 ? 0.787827 0.440312 0.505649 -0.136817   0.0288765   0.0538458   129 PHE   B CZ   
1679 H H    . PHE   A 117 ? 0.589954 0.310378 0.324803 -0.0460541  -0.0503521  -0.0090996  129 PHE   B H    
1680 H HA   . PHE   A 117 ? 0.565235 0.300945 0.298875 -0.0775765  -0.029065   0.0141309   129 PHE   B HA   
1681 H HB2  . PHE   A 117 ? 0.674088 0.34705  0.382778 -0.07026    -0.0379206  0.0249627   129 PHE   B HB2  
1682 H HB3  . PHE   A 117 ? 0.679957 0.34264  0.415198 -0.0804283  -0.040094   0.00796579  129 PHE   B HB3  
1683 H HD1  . PHE   A 117 ? 0.735422 0.395493 0.514654 -0.121985   -0.0174051  0.0116337   129 PHE   B HD1  
1684 H HD2  . PHE   A 117 ? 0.696307 0.374359 0.375496 -0.0920422  -0.0173889  0.0452488   129 PHE   B HD2  
1685 H HE1  . PHE   A 117 ? 0.783423 0.435619 0.575643 -0.15316    0.0238842   0.0371137   129 PHE   B HE1  
1686 H HE2  . PHE   A 117 ? 0.765681 0.421989 0.418194 -0.116702   0.0166931   0.0622961   129 PHE   B HE2  
1687 H HZ   . PHE   A 117 ? 0.806955 0.452665 0.519694 -0.146129   0.0476933   0.0637606   129 PHE   B HZ   
1688 N N    . PHE   A 118 ? 0.540932 0.29805  0.321086 -0.101827   -0.017611   -0.00075598 130 PHE   B N    
1689 C CA   . PHE   A 118 ? 0.518935 0.289088 0.335733 -0.115984   -0.0127702  -0.00865489 130 PHE   B CA   
1690 C C    . PHE   A 118 ? 0.556835 0.32113  0.383323 -0.135889   0.0108151   0.00176162  130 PHE   B C    
1691 O O    . PHE   A 118 ? 0.577749 0.339344 0.374879 -0.135797   0.0239421   0.01159     130 PHE   B O    
1692 C CB   . PHE   A 118 ? 0.551282 0.359088 0.385089 -0.108634   -0.0134729  -0.0146629  130 PHE   B CB   
1693 C CG   . PHE   A 118 ? 0.501408 0.32055  0.325038 -0.086144   -0.0303723  -0.0219258  130 PHE   B CG   
1694 C CD1  . PHE   A 118 ? 0.512702 0.336393 0.313224 -0.0696669  -0.0292375  -0.0141416  130 PHE   B CD1  
1695 C CD2  . PHE   A 118 ? 0.551973 0.376054 0.389221 -0.0806375  -0.0472835  -0.0362125  130 PHE   B CD2  
1696 C CE1  . PHE   A 118 ? 0.522728 0.358014 0.31268  -0.0465118  -0.0364178  -0.0164956  130 PHE   B CE1  
1697 C CE2  . PHE   A 118 ? 0.562339 0.395811 0.377733 -0.0558133  -0.0586972  -0.0408664  130 PHE   B CE2  
1698 C CZ   . PHE   A 118 ? 0.517666 0.353454 0.306393 -0.0380207  -0.0503909  -0.0298806  130 PHE   B CZ   
1699 H H    . PHE   A 118 ? 0.525915 0.288393 0.293421 -0.101358   -0.0118709  0.00604576  130 PHE   B H    
1700 H HA   . PHE   A 118 ? 0.550462 0.309883 0.379526 -0.116827   -0.0234076  -0.0168026  130 PHE   B HA   
1701 H HB2  . PHE   A 118 ? 0.514173 0.329429 0.339187 -0.1088     -0.00374645 -0.00843774 130 PHE   B HB2  
1702 H HB3  . PHE   A 118 ? 0.520448 0.338031 0.382278 -0.117662   -0.0107782  -0.018898   130 PHE   B HB3  
1703 H HD1  . PHE   A 118 ? 0.508311 0.329394 0.302017 -0.0734511  -0.0226332  -0.00650904 130 PHE   B HD1  
1704 H HD2  . PHE   A 118 ? 0.547142 0.372098 0.410031 -0.0928267  -0.0499655  -0.0418268  130 PHE   B HD2  
1705 H HE1  . PHE   A 118 ? 0.511506 0.352059 0.293188 -0.035669   -0.0323425  -0.00904964 130 PHE   B HE1  
1706 H HE2  . PHE   A 118 ? 0.564939 0.399735 0.382008 -0.049881   -0.0732418  -0.0522257  130 PHE   B HE2  
1707 H HZ   . PHE   A 118 ? 0.539976 0.381346 0.312788 -0.0195972  -0.0539512  -0.0309165  130 PHE   B HZ   
1708 N N    . GLU   A 119 ? 0.523587 0.292654 0.395464 -0.150397   0.0147652   -0.0032151  131 GLU   B N    
1709 C CA   . GLU   A 119 ? 0.57266  0.35008  0.474261 -0.167541   0.0418875   0.00475962  131 GLU   B CA   
1710 C C    . GLU   A 119 ? 0.533268 0.351254 0.481225 -0.166107   0.0365118   -0.00785051 131 GLU   B C    
1711 O O    . GLU   A 119 ? 0.600861 0.430482 0.588556 -0.167184   0.0153141   -0.0205755  131 GLU   B O    
1712 C CB   . GLU   A 119 ? 0.625174 0.37707  0.55637  -0.186119   0.0540062   0.0142572   131 GLU   B CB   
1713 C CG   . GLU   A 119 ? 0.716427 0.478176 0.681594 -0.202193   0.0905981   0.0272823   131 GLU   B CG   
1714 C CD   . GLU   A 119 ? 0.724133 0.455738 0.718034 -0.220784   0.109729    0.0445649   131 GLU   B CD   
1715 O OE1  . GLU   A 119 ? 0.731466 0.424924 0.686154 -0.222919   0.129719    0.06701     131 GLU   B OE1  
1716 O OE2  . GLU   A 119 ? 0.747068 0.494288 0.815154 -0.233642   0.0977858   0.033371    131 GLU   B OE2  
1717 H H    . GLU   A 119 ? 0.543342 0.311    0.431637 -0.148848   -0.00072078 -0.0129004  131 GLU   B H    
1718 H HA   . GLU   A 119 ? 0.570998 0.345167 0.442434 -0.165367   0.0563079   0.0128657   131 GLU   B HA   
1719 H HB2  . GLU   A 119 ? 0.662004 0.385959 0.559506 -0.183738   0.0553707   0.0237581   131 GLU   B HB2  
1720 H HB3  . GLU   A 119 ? 0.635572 0.389305 0.599907 -0.189398   0.036522    0.00319482  131 GLU   B HB3  
1721 H HG2  . GLU   A 119 ? 0.665526 0.455509 0.674265 -0.205055   0.0880832   0.0180728   131 GLU   B HG2  
1722 H HG3  . GLU   A 119 ? 0.692999 0.453458 0.620207 -0.196542   0.106678    0.0345345   131 GLU   B HG3  
1723 N N    . ILE   A 120 ? 0.501049 0.337754 0.443006 -0.162566   0.0541135   -0.00502971 132 ILE   B N    
1724 C CA   . ILE   A 120 ? 0.486506 0.359446 0.471923 -0.158512   0.0521095   -0.0131442  132 ILE   B CA   
1725 C C    . ILE   A 120 ? 0.48079  0.368366 0.505235 -0.16933    0.0835806   -0.00818425 132 ILE   B C    
1726 O O    . ILE   A 120 ? 0.529159 0.402053 0.51764  -0.170213   0.110053    -0.00078405 132 ILE   B O    
1727 C CB   . ILE   A 120 ? 0.473231 0.355228 0.426437 -0.141891   0.0477519   -0.0145978  132 ILE   B CB   
1728 C CG1  . ILE   A 120 ? 0.44353  0.314654 0.360486 -0.128494   0.0243438   -0.0158868  132 ILE   B CG1  
1729 C CG2  . ILE   A 120 ? 0.441841 0.357937 0.441605 -0.135506   0.046612    -0.0194781  132 ILE   B CG2  
1730 C CD1  . ILE   A 120 ? 0.488817 0.370582 0.386829 -0.113811   0.0225466   -0.0135305  132 ILE   B CD1  
1731 H H    . ILE   A 120 ? 0.519125 0.344281 0.42864  -0.161585   0.0665347   0.00155268  132 ILE   B H    
1732 H HA   . ILE   A 120 ? 0.478267 0.360349 0.489052 -0.157222   0.0330855   -0.0205789  132 ILE   B HA   
1733 H HB   . ILE   A 120 ? 0.474156 0.346697 0.404615 -0.143849   0.0634611   -0.0105571  132 ILE   B HB   
1734 H HG12 . ILE   A 120 ? 0.461926 0.338764 0.393451 -0.124664   0.00859679  -0.0217401  132 ILE   B HG12 
1735 H HG13 . ILE   A 120 ? 0.480279 0.330037 0.373033 -0.132167   0.0255709   -0.0119665  132 ILE   B HG13 
1736 H HG21 . ILE   A 120 ? 0.432132 0.353272 0.417602 -0.124408   0.0418206   -0.0191044  132 ILE   B HG21 
1737 H HG22 . ILE   A 120 ? 0.442269 0.368517 0.467866 -0.135149   0.0310394   -0.0240827  132 ILE   B HG22 
1738 H HG23 . ILE   A 120 ? 0.447574 0.369495 0.466507 -0.14167    0.0661689   -0.0179055  132 ILE   B HG23 
1739 H HD11 . ILE   A 120 ? 0.472364 0.348102 0.358087 -0.117949   0.0345811   -0.0112075  132 ILE   B HD11 
1740 H HD12 . ILE   A 120 ? 0.469698 0.344957 0.347737 -0.105355   0.0114555   -0.0122885  132 ILE   B HD12 
1741 H HD13 . ILE   A 120 ? 0.454053 0.35433  0.373996 -0.107992   0.0206451   -0.0151539  132 ILE   B HD13 
1742 N N    . GLU   A 121 ? 0.474865 0.393581 0.56971  -0.173358   0.0788677   -0.0138065  133 GLU   B N    
1743 C CA   . GLU   A 121 ? 0.475493 0.416997 0.618765 -0.178573   0.11019     -0.00953822 133 GLU   B CA   
1744 C C    . GLU   A 121 ? 0.451979 0.425592 0.621336 -0.162936   0.100273    -0.0169124  133 GLU   B C    
1745 O O    . GLU   A 121 ? 0.491612 0.487292 0.694609 -0.156264   0.0683063   -0.0242265  133 GLU   B O    
1746 C CB   . GLU   A 121 ? 0.489703 0.444333 0.710662 -0.197304   0.118401    -0.00566765 133 GLU   B CB   
1747 C CG   . GLU   A 121 ? 0.479427 0.461156 0.760162 -0.201684   0.158399    0.00184185  133 GLU   B CG   
1748 C CD   . GLU   A 121 ? 0.500145 0.500943 0.877673 -0.222516   0.165459    0.00757646  133 GLU   B CD   
1749 O OE1  . GLU   A 121 ? 0.499005 0.480122 0.886728 -0.237148   0.149133    0.00842163  133 GLU   B OE1  
1750 O OE2  . GLU   A 121 ? 0.463926 0.499122 0.914864 -0.224681   0.190938    0.0120917   133 GLU   B OE2  
1751 H H    . GLU   A 121 ? 0.466389 0.392505 0.579406 -0.171384   0.054924    -0.0210127  133 GLU   B H    
1752 H HA   . GLU   A 121 ? 0.494355 0.420151 0.603033 -0.178905   0.134637    -0.00326946 133 GLU   B HA   
1753 H HB2  . GLU   A 121 ? 0.508772 0.438632 0.711866 -0.206822   0.125324    0.00131392  133 GLU   B HB2  
1754 H HB3  . GLU   A 121 ? 0.474084 0.443756 0.729166 -0.196901   0.0898444   -0.014828   133 GLU   B HB3  
1755 H HG2  . GLU   A 121 ? 0.464275 0.469121 0.764005 -0.190905   0.15163     -0.00454485 133 GLU   B HG2  
1756 H HG3  . GLU   A 121 ? 0.505097 0.468933 0.745721 -0.200666   0.187839    0.00977436  133 GLU   B HG3  
1757 N N    . LEU   A 122 ? 0.524872 0.498098 0.677433 -0.155634   0.127179    -0.0152579  134 LEU   B N    
1758 C CA   . LEU   A 122 ? 0.491812 0.490591 0.674209 -0.140201   0.123228    -0.0194736  134 LEU   B CA   
1759 C C    . LEU   A 122 ? 0.527316 0.560994 0.794607 -0.142619   0.139506    -0.0182643  134 LEU   B C    
1760 O O    . LEU   A 122 ? 0.540883 0.573248 0.823305 -0.148827   0.178705    -0.0142933  134 LEU   B O    
1761 C CB   . LEU   A 122 ? 0.488092 0.466947 0.622598 -0.131432   0.143611    -0.0218414  134 LEU   B CB   
1762 C CG   . LEU   A 122 ? 0.460198 0.457374 0.626135 -0.114969   0.142176    -0.0244699  134 LEU   B CG   
1763 C CD1  . LEU   A 122 ? 0.436483 0.451096 0.61626  -0.10281    0.105887    -0.0207555  134 LEU   B CD1  
1764 C CD2  . LEU   A 122 ? 0.478305 0.447103 0.595472 -0.108885   0.157059    -0.0310433  134 LEU   B CD2  
1765 H H    . LEU   A 122 ? 0.522339 0.476894 0.642787 -0.159093   0.147848    -0.011762   134 LEU   B H    
1766 H HA   . LEU   A 122 ? 0.48305  0.488575 0.663539 -0.132548   0.0960379   -0.0214786  134 LEU   B HA   
1767 H HB2  . LEU   A 122 ? 0.4889   0.448992 0.577257 -0.130577   0.131617    -0.022199   134 LEU   B HB2  
1768 H HB3  . LEU   A 122 ? 0.510742 0.480568 0.638548 -0.136625   0.170275    -0.0212534  134 LEU   B HB3  
1769 H HG   . LEU   A 122 ? 0.46615  0.481052 0.6776   -0.114519   0.15762     -0.0242963  134 LEU   B HG   
1770 H HD11 . LEU   A 122 ? 0.43217  0.466502 0.648547 -0.104476   0.094387    -0.0202531  134 LEU   B HD11 
1771 H HD12 . LEU   A 122 ? 0.432089 0.451712 0.623386 -0.0915557  0.107993    -0.0193198  134 LEU   B HD12 
1772 H HD13 . LEU   A 122 ? 0.434769 0.434893 0.575143 -0.103284   0.092328    -0.0199399  134 LEU   B HD13 
1773 H HD21 . LEU   A 122 ? 0.502202 0.456915 0.598948 -0.114171   0.178363    -0.0346064  134 LEU   B HD21 
1774 H HD22 . LEU   A 122 ? 0.472779 0.428882 0.555687 -0.108686   0.140809    -0.0303749  134 LEU   B HD22 
1775 H HD23 . LEU   A 122 ? 0.472755 0.449729 0.615526 -0.0992112  0.160832    -0.032462   134 LEU   B HD23 
1776 N N    . LEU   A 123 ? 0.537389 0.604035 0.862611 -0.136493   0.109406    -0.0210189  135 LEU   B N    
1777 C CA   . LEU   A 123 ? 0.518109 0.623553 0.93934  -0.141092   0.119884    -0.0194982  135 LEU   B CA   
1778 C C    . LEU   A 123 ? 0.59474  0.718995 1.04437  -0.122588   0.139501    -0.0179553  135 LEU   B C    
1779 O O    . LEU   A 123 ? 0.524161 0.665525 1.02712  -0.123903   0.176444    -0.0147528  135 LEU   B O    
1780 C CB   . LEU   A 123 ? 0.506876 0.63897  0.978674 -0.142038   0.071558    -0.0261398  135 LEU   B CB   
1781 C CG   . LEU   A 123 ? 0.597296 0.705489 1.04273  -0.157969   0.0470541   -0.0321966  135 LEU   B CG   
1782 C CD1  . LEU   A 123 ? 0.707422 0.836978 1.18745  -0.152562   -0.00920624 -0.0457939  135 LEU   B CD1  
1783 C CD2  . LEU   A 123 ? 0.633557 0.734875 1.11973  -0.18358    0.0790464   -0.0252747  135 LEU   B CD2  
1784 H H    . LEU   A 123 ? 0.517076 0.583216 0.823423 -0.128439   0.0824735   -0.0234668  135 LEU   B H    
1785 H HA   . LEU   A 123 ? 0.550504 0.650533 0.984753 -0.154499   0.145574    -0.0153132  135 LEU   B HA   
1786 H HB2  . LEU   A 123 ? 0.514219 0.651726 0.968814 -0.125772   0.0491604   -0.0280196  135 LEU   B HB2  
1787 H HB3  . LEU   A 123 ? 0.523814 0.685236 1.06881  -0.146195   0.0761574   -0.0253107  135 LEU   B HB3  
1788 H HG   . LEU   A 123 ? 0.600738 0.680743 0.976425 -0.153478   0.0463918   -0.031709   135 LEU   B HG   
1789 H HD11 . LEU   A 123 ? 0.665479 0.798622 1.11524  -0.133847   -0.0262195  -0.0467575  135 LEU   B HD11 
1790 H HD12 . LEU   A 123 ? 0.684481 0.793433 1.14183  -0.160933   -0.024457   -0.0520714  135 LEU   B HD12 
1791 H HD13 . LEU   A 123 ? 0.673272 0.832363 1.22804  -0.15829    -0.0128141  -0.0472629  135 LEU   B HD13 
1792 H HD21 . LEU   A 123 ? 0.634745 0.717705 1.08368  -0.184303   0.112184    -0.0173353  135 LEU   B HD21 
1793 H HD22 . LEU   A 123 ? 0.627118 0.758586 1.18874  -0.18854    0.0842374   -0.0241325  135 LEU   B HD22 
1794 H HD23 . LEU   A 123 ? 0.638637 0.722917 1.1139   -0.193385   0.0617563   -0.0292146  135 LEU   B HD23 
1795 N N    . ASP   A 124 ? 0.54575  0.665052 0.961697 -0.103399   0.117824    -0.0186671  136 ASP   B N    
1796 C CA   . ASP   A 124 ? 0.495804 0.632837 0.949778 -0.0832286  0.12804     -0.0158249  136 ASP   B CA   
1797 C C    . ASP   A 124 ? 0.512205 0.627456 0.90758  -0.0665318  0.109428    -0.0125227  136 ASP   B C    
1798 O O    . ASP   A 124 ? 0.418963 0.522318 0.767058 -0.0680253  0.0814468   -0.0117633  136 ASP   B O    
1799 C CB   . ASP   A 124 ? 0.464906 0.650902 1.00987  -0.0751862  0.10296     -0.0132149  136 ASP   B CB   
1800 C CG   . ASP   A 124 ? 0.447126 0.65958  1.06036  -0.056826   0.12302     -0.00857664 136 ASP   B CG   
1801 O OD1  . ASP   A 124 ? 0.436446 0.623901 1.01952  -0.047389   0.153975    -0.00889485 136 ASP   B OD1  
1802 O OD2  . ASP   A 124 ? 0.574498 0.832324 1.27726  -0.0528221  0.108374    -0.006407   136 ASP   B OD2  
1803 H H    . ASP   A 124 ? 0.538698 0.642554 0.909658 -0.101975   0.0980757   -0.0194893  136 ASP   B H    
1804 H HA   . ASP   A 124 ? 0.515227 0.644595 0.972259 -0.0845264  0.161589    -0.017217   136 ASP   B HA   
1805 H HB2  . ASP   A 124 ? 0.468483 0.668083 1.0498   -0.0896511  0.103487    -0.0153542  136 ASP   B HB2  
1806 H HB3  . ASP   A 124 ? 0.461422 0.65031  0.989754 -0.0666266  0.0691546   -0.0123639  136 ASP   B HB3  
1807 N N    . PHE   A 125 ? 0.471643 0.57968  0.873317 -0.0509315  0.127503    -0.010053   137 PHE   B N    
1808 C CA   . PHE   A 125 ? 0.453857 0.547793 0.824902 -0.033474   0.110584    -0.00107564 137 PHE   B CA   
1809 C C    . PHE   A 125 ? 0.468105 0.574459 0.894019 -0.0121796  0.121252    0.00587003  137 PHE   B C    
1810 O O    . PHE   A 125 ? 0.4967   0.60586  0.960424 -0.0125023  0.152655    -0.0018001  137 PHE   B O    
1811 C CB   . PHE   A 125 ? 0.512441 0.564049 0.815232 -0.0412183  0.123328    -0.00576291 137 PHE   B CB   
1812 C CG   . PHE   A 125 ? 0.493851 0.520403 0.784869 -0.0491948  0.160175    -0.0201362  137 PHE   B CG   
1813 C CD1  . PHE   A 125 ? 0.486875 0.501912 0.745644 -0.0669127  0.175478    -0.0295943  137 PHE   B CD1  
1814 C CD2  . PHE   A 125 ? 0.520991 0.527375 0.819998 -0.0378736  0.177566    -0.0245188  137 PHE   B CD2  
1815 C CE1  . PHE   A 125 ? 0.556528 0.546256 0.790905 -0.0696061  0.208763    -0.0430492  137 PHE   B CE1  
1816 C CE2  . PHE   A 125 ? 0.581438 0.560072 0.859112 -0.0422793  0.208773    -0.0430821  137 PHE   B CE2  
1817 C CZ   . PHE   A 125 ? 0.61521  0.586142 0.85488  -0.0570264  0.223849    -0.052297   137 PHE   B CZ   
1818 H H    . PHE   A 125 ? 0.48735  0.59767  0.914504 -0.0506367  0.15284     -0.0133416  137 PHE   B H    
1819 H HA   . PHE   A 125 ? 0.461378 0.565593 0.82404  -0.0291402  0.0830211   0.0043815   137 PHE   B HA   
1820 H HB2  . PHE   A 125 ? 0.49036  0.534717 0.786067 -0.0299731  0.116198    0.00228423  137 PHE   B HB2  
1821 H HB3  . PHE   A 125 ? 0.486036 0.531659 0.7551   -0.0509037  0.111767    -0.00710419 137 PHE   B HB3  
1822 H HD1  . PHE   A 125 ? 0.49239  0.517343 0.749015 -0.0753594  0.16447     -0.026476   137 PHE   B HD1  
1823 H HD2  . PHE   A 125 ? 0.520752 0.531683 0.841782 -0.0254023  0.16904     -0.0152142  137 PHE   B HD2  
1824 H HE1  . PHE   A 125 ? 0.570753 0.552404 0.779812 -0.0792969  0.220586    -0.0463869  137 PHE   B HE1  
1825 H HE2  . PHE   A 125 ? 0.594193 0.556627 0.879638 -0.0340298  0.219318    -0.0491009  137 PHE   B HE2  
1826 H HZ   . PHE   A 125 ? 0.629974 0.579858 0.844896 -0.0575053  0.244448    -0.0648019  137 PHE   B HZ   
1827 N N    . LYS   A 126 ? 0.461556 0.575693 0.892289 0.00895706  0.0966218   0.0219844   138 LYS   B N    
1828 C CA   . LYS   A 126 ? 0.477081 0.602302 0.962701 0.0329999   0.102726    0.0333243   138 LYS   B CA   
1829 C C    . LYS   A 126 ? 0.412726 0.503742 0.8622   0.0462584   0.1049      0.0483021   138 LYS   B C    
1830 O O    . LYS   A 126 ? 0.411041 0.491222 0.809785 0.0466709   0.0873542   0.058412    138 LYS   B O    
1831 C CB   . LYS   A 126 ? 0.399297 0.571647 0.936289 0.0473902   0.0681329   0.0420525   138 LYS   B CB   
1832 H H    . LYS   A 126 ? 0.461465 0.572493 0.858531 0.0102571   0.076582    0.02737     138 LYS   B H    
1833 H HA   . LYS   A 126 ? 0.451356 0.574164 0.964922 0.0300063   0.128807    0.0243207   138 LYS   B HA   
1836 N N    . GLY   A 127 ? 0.50896  0.582173 0.990557 0.0580407   0.128678    0.0506654   139 GLY   B N    
1837 C CA   . GLY   A 127 ? 0.509356 0.557981 0.987031 0.0763358   0.128541    0.0723858   139 GLY   B CA   
1838 C C    . GLY   A 127 ? 0.587823 0.65775  1.05209  0.0977064   0.0953728   0.100828    139 GLY   B C    
1839 O O    . GLY   A 127 ? 0.672999 0.780689 1.16916  0.111553    0.073004    0.105376    139 GLY   B O    
1840 H H    . GLY   A 127 ? 0.487816 0.562244 0.996538 0.0550959   0.147882    0.0386494   139 GLY   B H    
1841 H HA2  . GLY   A 127 ? 0.53043  0.551324 0.9749   0.0649092   0.136811    0.0680943   139 GLY   B HA2  
1842 H HA3  . GLY   A 127 ? 0.542576 0.585871 1.06013  0.0874843   0.143236    0.0731552   139 GLY   B HA3  
1843 N N    . GLU   A 128 ? 0.631748 0.679315 1.04613  0.100045    0.0910292   0.118273    140 GLU   B N    
1844 C CA   . GLU   A 128 ? 0.756021 0.807214 1.15905  0.130181    0.075085    0.153707    140 GLU   B CA   
1845 C C    . GLU   A 128 ? 0.816809 0.876006 1.28484  0.156485    0.0785493   0.168826    140 GLU   B C    
1846 O O    . GLU   A 128 ? 0.828204 0.874472 1.34634  0.150222    0.103975    0.153789    140 GLU   B O    
1847 C CB   . GLU   A 128 ? 0.779292 0.796463 1.14391  0.1306      0.0892792   0.175736    140 GLU   B CB   
1848 O OXT  . GLU   A 128 ? 0.948902 1.02595  1.41271  0.185747    0.0549093   0.195152    140 GLU   B OXT  
1849 H H    . GLU   A 128 ? 0.632808 0.663031 1.01949  0.0836601   0.0992009   0.109165    140 GLU   B H    
1850 H HA   . GLU   A 128 ? 0.743844 0.817218 1.12359  0.135632    0.0508639   0.154475    140 GLU   B HA   
1853 N N    . THR   B 5   ? 1.58024  0.617337 0.515354 0.17132     0.363951    -0.00601617 17  THR   A N    
1854 C CA   . THR   B 5   ? 1.55175  0.621825 0.514553 0.153682    0.311298    -0.00639824 17  THR   A CA   
1855 C C    . THR   B 5   ? 1.5747   0.646979 0.561971 0.150201    0.290503    -0.0205139  17  THR   A C    
1856 O O    . THR   B 5   ? 1.55     0.616253 0.561786 0.163386    0.315474    -0.0240305  17  THR   A O    
1857 C CB   . THR   B 5   ? 1.57307  0.708702 0.620643 0.153194    0.306541    0.0146526   17  THR   A CB   
1858 O OG1  . THR   B 5   ? 1.56582  0.691491 0.579042 0.151018    0.315896    0.0268501   17  THR   A OG1  
1859 C CG2  . THR   B 5   ? 1.51476  0.693408 0.613342 0.140024    0.261749    0.0152349   17  THR   A CG2  
1860 H H    . THR   B 5   ? 1.60614  0.644476 0.530202 0.172685    0.376888    0.00379895  17  THR   A H    
1861 H HA   . THR   B 5   ? 1.60609  0.65317  0.515741 0.144112    0.293965    -0.0101212  17  THR   A HA   
1862 H HB   . THR   B 5   ? 1.52555  0.681481 0.618375 0.163294    0.329399    0.0209057   17  THR   A HB   
1864 H HG21 . THR   B 5   ? 1.47377  0.683117 0.609938 0.138325    0.260203    0.0271164   17  THR   A HG21 
1865 H HG22 . THR   B 5   ? 1.52871  0.689122 0.588029 0.131077    0.238442    0.00855379  17  THR   A HG22 
1866 H HG23 . THR   B 5   ? 1.47947  0.672486 0.612097 0.142183    0.258787    0.0109482   17  THR   A HG23 
1867 N N    . VAL   B 6   ? 1.6002   0.68483  0.586811 0.132723    0.244388    -0.0257078  18  VAL   A N    
1868 C CA   . VAL   B 6   ? 1.53797  0.631364 0.551023 0.124583    0.217936    -0.0362016  18  VAL   A CA   
1869 C C    . VAL   B 6   ? 1.42272  0.584617 0.5213   0.12073     0.195234    -0.0226803  18  VAL   A C    
1870 O O    . VAL   B 6   ? 1.40729  0.598264 0.52506  0.118053    0.187187    -0.0102035  18  VAL   A O    
1871 C CB   . VAL   B 6   ? 1.52513  0.579247 0.471924 0.10568     0.184018    -0.0532852  18  VAL   A CB   
1872 C CG1  . VAL   B 6   ? 1.6283   0.606705 0.48349  0.106216    0.204741    -0.0716513  18  VAL   A CG1  
1873 C CG2  . VAL   B 6   ? 1.58423  0.653389 0.510978 0.0919417   0.149256    -0.0460445  18  VAL   A CG2  
1874 H H    . VAL   B 6   ? 1.5822   0.670136 0.551115 0.125641    0.229361    -0.0211191  18  VAL   A H    
1875 H HA   . VAL   B 6   ? 1.53524  0.617588 0.558905 0.133973    0.238362    -0.0398879  18  VAL   A HA   
1876 H HB   . VAL   B 6   ? 1.51606  0.583735 0.493288 0.100491    0.168644    -0.0573003  18  VAL   A HB   
1877 H HG11 . VAL   B 6   ? 1.66553  0.627956 0.484435 0.110708    0.220289    -0.0679186  18  VAL   A HG11 
1878 H HG12 . VAL   B 6   ? 1.63551  0.601297 0.503768 0.116451    0.227911    -0.0759928  18  VAL   A HG12 
1879 H HG13 . VAL   B 6   ? 1.65749  0.615065 0.4767   0.0915605   0.179785    -0.0824558  18  VAL   A HG13 
1880 H HG21 . VAL   B 6   ? 1.60579  0.648182 0.486672 0.0802455   0.130006    -0.0560807  18  VAL   A HG21 
1881 H HG22 . VAL   B 6   ? 1.50433  0.61531  0.484441 0.0893401   0.132194    -0.0383298  18  VAL   A HG22 
1882 H HG23 . VAL   B 6   ? 1.58542  0.648575 0.492296 0.0975572   0.163894    -0.0383491  18  VAL   A HG23 
1883 N N    . THR   B 7   ? 1.28686  0.469238 0.432612 0.120583    0.187139    -0.025513   19  THR   A N    
1884 C CA   . THR   B 7   ? 1.24927  0.4903   0.467411 0.115337    0.165036    -0.0163148  19  THR   A CA   
1885 C C    . THR   B 7   ? 1.18536  0.436336 0.390921 0.0995698   0.128046    -0.0181959  19  THR   A C    
1886 O O    . THR   B 7   ? 1.31375  0.597442 0.548994 0.0982073   0.120331    -0.00781541 19  THR   A O    
1887 C CB   . THR   B 7   ? 1.20753  0.458156 0.461362 0.115932    0.160541    -0.0199544  19  THR   A CB   
1888 O OG1  . THR   B 7   ? 1.28702  0.523478 0.55053  0.132849    0.194483    -0.0171293  19  THR   A OG1  
1889 C CG2  . THR   B 7   ? 1.08065  0.389339 0.401336 0.110188    0.140042    -0.0107791  19  THR   A CG2  
1890 H H    . THR   B 7   ? 1.34678  0.503002 0.476328 0.123868    0.196704    -0.0335553  19  THR   A H    
1891 H HA   . THR   B 7   ? 1.20153  0.468923 0.452995 0.121258    0.17689     -0.0056634  19  THR   A HA   
1892 H HB   . THR   B 7   ? 1.23615  0.461513 0.458988 0.107531    0.146875    -0.0304097  19  THR   A HB   
1894 H HG21 . THR   B 7   ? 1.08158  0.396703 0.424814 0.112443    0.141292    -0.0103053  19  THR   A HG21 
1895 H HG22 . THR   B 7   ? 1.07115  0.404602 0.418403 0.114468    0.148303    -0.00159994 19  THR   A HG22 
1896 H HG23 . THR   B 7   ? 1.0855   0.399338 0.399245 0.0997186   0.117918    -0.0141525  19  THR   A HG23 
1897 N N    . GLU   B 8   ? 1.23401  0.451992 0.392044 0.088011    0.107606    -0.0311628  20  GLU   A N    
1898 C CA   . GLU   B 8   ? 1.22438  0.4542   0.376499 0.0725819   0.0697487   -0.032443   20  GLU   A CA   
1899 C C    . GLU   B 8   ? 1.2406   0.454636 0.345054 0.0705776   0.0625187   -0.0270577  20  GLU   A C    
1900 O O    . GLU   B 8   ? 1.31471  0.50078  0.364557 0.0587569   0.0404532   -0.0335376  20  GLU   A O    
1901 C CB   . GLU   B 8   ? 1.31853  0.524379 0.447293 0.0585601   0.0500028   -0.0465324  20  GLU   A CB   
1902 C CG   . GLU   B 8   ? 1.33943  0.561366 0.517518 0.0609535   0.0571277   -0.0481809  20  GLU   A CG   
1903 C CD   . GLU   B 8   ? 1.22846  0.509283 0.480119 0.0604977   0.045471    -0.037676   20  GLU   A CD   
1904 O OE1  . GLU   B 8   ? 1.09752  0.4152   0.37685  0.0545356   0.0238023   -0.030974   20  GLU   A OE1  
1905 O OE2  . GLU   B 8   ? 1.25375  0.537622 0.532646 0.0665892   0.0601614   -0.0371954  20  GLU   A OE2  
1906 H H    . GLU   B 8   ? 1.27261  0.458187 0.401116 0.0898253   0.118804    -0.039522   20  GLU   A H    
1907 H HA   . GLU   B 8   ? 1.17871  0.446791 0.379462 0.0723551   0.0611787   -0.0255702  20  GLU   A HA   
1908 H HB2  . GLU   B 8   ? 1.37264  0.536692 0.448753 0.0570175   0.0571123   -0.0553328  20  GLU   A HB2  
1909 H HB3  . GLU   B 8   ? 1.30511  0.526011 0.438341 0.0484112   0.0245145   -0.0450623  20  GLU   A HB3  
1910 H HG2  . GLU   B 8   ? 1.32569  0.53543  0.50366  0.0724681   0.082157    -0.0476632  20  GLU   A HG2  
1911 H HG3  . GLU   B 8   ? 1.34525  0.544541 0.502669 0.0513493   0.0472344   -0.0575146  20  GLU   A HG3  
1912 N N    . GLN   B 9   ? 1.25716  0.482997 0.375523 0.0819013   0.0845181   -0.014822   21  GLN   A N    
1913 C CA   . GLN   B 9   ? 1.31595  0.523805 0.388333 0.08228     0.0838325   -0.00604219 21  GLN   A CA   
1914 C C    . GLN   B 9   ? 1.25682  0.507049 0.378726 0.0813988   0.0658265   0.00835424  21  GLN   A C    
1915 O O    . GLN   B 9   ? 1.25671  0.546586 0.443752 0.0817568   0.0613654   0.00990673  21  GLN   A O    
1916 C CB   . GLN   B 9   ? 1.47214  0.661104 0.52785  0.0952452   0.125446    -0.00078785 21  GLN   A CB   
1917 C CG   . GLN   B 9   ? 1.4674   0.700004 0.599221 0.103967    0.145529    0.0106142   21  GLN   A CG   
1918 C CD   . GLN   B 9   ? 1.46213  0.68527  0.580498 0.112169    0.176955    0.0235113   21  GLN   A CD   
1919 O OE1  . GLN   B 9   ? 1.4914   0.67399  0.540363 0.112652    0.184827    0.02404     21  GLN   A OE1  
1920 N NE2  . GLN   B 9   ? 1.37234  0.633672 0.554875 0.115844    0.191441    0.0352373   21  GLN   A NE2  
1921 H H    . GLN   B 9   ? 1.21945  0.465825 0.377442 0.0885375   0.0990198   -0.0106873  21  GLN   A H    
1922 H HA   . GLN   B 9   ? 1.377    0.558775 0.400848 0.0747625   0.0689744   -0.0119279  21  GLN   A HA   
1923 H HB2  . GLN   B 9   ? 1.48691  0.659696 0.505713 0.0948599   0.125895    0.00529366  21  GLN   A HB2  
1924 H HB3  . GLN   B 9   ? 1.48504  0.646573 0.513082 0.0979044   0.140017    -0.0103819  21  GLN   A HB3  
1925 H HG2  . GLN   B 9   ? 1.42855  0.667108 0.583449 0.107915    0.156062    0.00581818  21  GLN   A HG2  
1926 H HG3  . GLN   B 9   ? 1.40032  0.661886 0.568339 0.0996285   0.127569    0.0151879   21  GLN   A HG3  
1927 H HE21 . GLN   B 9   ? 1.39959  0.657481 0.579828 0.119985    0.211954    0.0432632   21  GLN   A HE21 
1928 H HE22 . GLN   B 9   ? 1.33828  0.62813  0.564761 0.113154    0.180405    0.0350005   21  GLN   A HE22 
1929 N N    . GLY   B 10  ? 1.32662  0.565693 0.415588 0.080925    0.0572002   0.0194424   22  GLY   A N    
1930 C CA   . GLY   B 10  ? 1.18148  0.453693 0.314137 0.0811028   0.0392865   0.0325493   22  GLY   A CA   
1931 C C    . GLY   B 10  ? 1.19564  0.475571 0.321067 0.0720002   -2.822e-05  0.0320066   22  GLY   A C    
1932 O O    . GLY   B 10  ? 1.24618  0.509684 0.339495 0.0626574   -0.0144266  0.0199744   22  GLY   A O    
1933 H H    . GLY   B 10  ? 1.34319  0.552053 0.380864 0.0810048   0.0633018   0.0192247   22  GLY   A H    
1934 H HA2  . GLY   B 10  ? 1.22574  0.488529 0.342825 0.085054    0.047682    0.0432052   22  GLY   A HA2  
1935 H HA3  . GLY   B 10  ? 1.15678  0.455701 0.34019  0.0831242   0.0449209   0.0320958   22  GLY   A HA3  
1936 N N    . GLU   B 11  ? 1.17165  0.474682 0.326735 0.0747866   -0.0163784  0.0466242   23  GLU   A N    
1937 C CA   . GLU   B 11  ? 1.17694  0.493807 0.333339 0.0691997   -0.05345    0.053183    23  GLU   A CA   
1938 C C    . GLU   B 11  ? 1.14798  0.504829 0.369973 0.0655619   -0.0655646  0.0456823   23  GLU   A C    
1939 O O    . GLU   B 11  ? 1.05239  0.432103 0.327045 0.0715702   -0.0484387  0.0442836   23  GLU   A O    
1940 C CB   . GLU   B 11  ? 1.20799  0.529255 0.371516 0.0782945   -0.0581105  0.074919    23  GLU   A CB   
1941 C CG   . GLU   B 11  ? 1.25268  0.598156 0.435618 0.077       -0.0956644  0.0874107   23  GLU   A CG   
1942 C CD   . GLU   B 11  ? 1.30274  0.654618 0.504187 0.0892422   -0.100425   0.111193    23  GLU   A CD   
1943 O OE1  . GLU   B 11  ? 1.27615  0.604242 0.457431 0.096332    -0.0775688  0.120277    23  GLU   A OE1  
1944 O OE2  . GLU   B 11  ? 1.36009  0.740365 0.596708 0.0915819   -0.127332   0.122075    23  GLU   A OE2  
1945 H H    . GLU   B 11  ? 1.15269  0.463653 0.331057 0.0807969   -0.00293162 0.0535514   23  GLU   A H    
1946 H HA   . GLU   B 11  ? 1.23234  0.528246 0.342094 0.0619536   -0.0652852  0.0489989   23  GLU   A HA   
1947 H HB2  . GLU   B 11  ? 1.25629  0.550598 0.373504 0.0795378   -0.0506128  0.0804322   23  GLU   A HB2  
1948 H HB3  . GLU   B 11  ? 1.17523  0.509645 0.377785 0.0843255   -0.0426413  0.0769333   23  GLU   A HB3  
1949 H HG2  . GLU   B 11  ? 1.21155  0.583191 0.438033 0.0750446   -0.10179    0.0811097   23  GLU   A HG2  
1950 H HG3  . GLU   B 11  ? 1.29343  0.625687 0.43484  0.0692016   -0.113268   0.0865296   23  GLU   A HG3  
1951 N N    . ASP   B 12  ? 1.1407   0.504827 0.356181 0.054101    -0.0951566  0.041566    24  ASP   A N    
1952 C CA   . ASP   B 12  ? 1.14194  0.543944 0.415768 0.0490784   -0.108448   0.0371926   24  ASP   A CA   
1953 C C    . ASP   B 12  ? 1.09709  0.533073 0.41943  0.0580069   -0.121481   0.0543377   24  ASP   A C    
1954 O O    . ASP   B 12  ? 1.06013  0.499032 0.367828 0.0561663   -0.147756   0.0671376   24  ASP   A O    
1955 C CB   . ASP   B 12  ? 1.11892  0.516445 0.372086 0.0315113   -0.13396    0.027838    24  ASP   A CB   
1956 C CG   . ASP   B 12  ? 1.09735  0.53535  0.414817 0.0255698   -0.143242   0.0245377   24  ASP   A CG   
1957 O OD1  . ASP   B 12  ? 1.02472  0.494054 0.398544 0.0365562   -0.13101    0.0299703   24  ASP   A OD1  
1958 O OD2  . ASP   B 12  ? 1.06522  0.501222 0.375148 0.00935074  -0.160498   0.016216    24  ASP   A OD2  
1959 H H    . ASP   B 12  ? 1.20191  0.545912 0.373114 0.0482297   -0.107246   0.0418515   24  ASP   A H    
1960 H HA   . ASP   B 12  ? 1.08429  0.492609 0.382104 0.0518112   -0.0902107  0.0301099   24  ASP   A HA   
1961 H HB2  . ASP   B 12  ? 1.1615   0.530454 0.37893  0.0272813   -0.122981   0.0166171   24  ASP   A HB2  
1962 H HB3  . ASP   B 12  ? 1.17154  0.566289 0.402583 0.0271223   -0.155402   0.0354027   24  ASP   A HB3  
1963 N N    . ILE   B 13  ? 0.991423 0.451151 0.369033 0.0673889   -0.103608   0.0546047   25  ILE   A N    
1964 C CA   . ILE   B 13  ? 1.05228  0.537582 0.475283 0.0783594   -0.110463   0.0694787   25  ILE   A CA   
1965 C C    . ILE   B 13  ? 1.03429  0.560446 0.517198 0.0763676   -0.118541   0.0662656   25  ILE   A C    
1966 O O    . ILE   B 13  ? 0.950995 0.499905 0.480969 0.0873173   -0.115577   0.0744926   25  ILE   A O    
1967 C CB   . ILE   B 13  ? 1.00676  0.481822 0.442444 0.0903161   -0.0836137  0.0731337   25  ILE   A CB   
1968 C CG1  . ILE   B 13  ? 0.965489 0.447945 0.426625 0.0880581   -0.0592148  0.0575549   25  ILE   A CG1  
1969 C CG2  . ILE   B 13  ? 1.11776  0.555413 0.499392 0.0931488   -0.0747588  0.081472    25  ILE   A CG2  
1970 C CD1  . ILE   B 13  ? 1.05415  0.52727  0.529215 0.0956726   -0.036385   0.0607146   25  ILE   A CD1  
1971 H H    . ILE   B 13  ? 0.998545 0.457406 0.384752 0.0670033   -0.0870844  0.0454952   25  ILE   A H    
1972 H HA   . ILE   B 13  ? 1.06444  0.546116 0.470323 0.0791295   -0.127729   0.0807205   25  ILE   A HA   
1973 H HB   . ILE   B 13  ? 1.018    0.506782 0.48335  0.0979072   -0.0878934  0.0820891   25  ILE   A HB   
1974 H HG12 . ILE   B 13  ? 0.991004 0.461327 0.427554 0.0822522   -0.0538047  0.0498627   25  ILE   A HG12 
1975 H HG13 . ILE   B 13  ? 0.959187 0.464377 0.45228  0.0866014   -0.0636684  0.0534027   25  ILE   A HG13 
1976 H HG21 . ILE   B 13  ? 1.09187  0.525243 0.487073 0.100075    -0.0611956  0.0868698   25  ILE   A HG21 
1977 H HG22 . ILE   B 13  ? 1.10423  0.527134 0.459829 0.0878494   -0.0644129  0.0722334   25  ILE   A HG22 
1978 H HG23 . ILE   B 13  ? 1.13037  0.56244  0.48934  0.093091    -0.0924708  0.0913459   25  ILE   A HG23 
1979 H HD11 . ILE   B 13  ? 1.02628  0.503306 0.518255 0.102678    -0.0408805  0.0696169   25  ILE   A HD11 
1980 H HD12 . ILE   B 13  ? 0.994053 0.477761 0.490821 0.0932122   -0.0253756  0.0514938   25  ILE   A HD12 
1981 H HD13 . ILE   B 13  ? 1.04419  0.49618  0.48981  0.0955166   -0.0278595  0.0634885   25  ILE   A HD13 
1982 N N    . THR   B 14  ? 0.929451 0.463241 0.410791 0.0627043   -0.127803   0.0553696   26  THR   A N    
1983 C CA   . THR   B 14  ? 0.889998 0.462976 0.426711 0.0588829   -0.134283   0.0538196   26  THR   A CA   
1984 C C    . THR   B 14  ? 0.996106 0.592369 0.54795  0.0554714   -0.166808   0.0688052   26  THR   A C    
1985 O O    . THR   B 14  ? 1.01672  0.594325 0.523193 0.0480336   -0.188793   0.0740847   26  THR   A O    
1986 C CB   . THR   B 14  ? 0.862658 0.433009 0.393784 0.0443216   -0.130066   0.0380803   26  THR   A CB   
1987 O OG1  . THR   B 14  ? 0.919159 0.465411 0.402778 0.0299258   -0.149058   0.0340912   26  THR   A OG1  
1988 C CG2  . THR   B 14  ? 0.80801  0.362253 0.330817 0.047355    -0.100821   0.0258904   26  THR   A CG2  
1989 H H    . THR   B 14  ? 0.97195  0.48467  0.416592 0.0553336   -0.12886    0.048817    26  THR   A H    
1990 H HA   . THR   B 14  ? 0.87683  0.462725 0.445114 0.0679921   -0.120567   0.0549624   26  THR   A HA   
1991 H HB   . THR   B 14  ? 0.840191 0.437907 0.409105 0.0417037   -0.134361   0.0393684   26  THR   A HB   
1993 H HG21 . THR   B 14  ? 0.814274 0.36662  0.334259 0.0389783   -0.100422   0.0186007   26  THR   A HG21 
1994 H HG22 . THR   B 14  ? 0.836074 0.366044 0.326801 0.050586    -0.0937495  0.0252771   26  THR   A HG22 
1995 H HG23 . THR   B 14  ? 0.789921 0.360062 0.342641 0.0542095   -0.0896517  0.0268737   26  THR   A HG23 
1996 N N    . SER   B 15  ? 0.961647 0.599748 0.576667 0.0601379   -0.169878   0.0760067   27  SER   A N    
1997 C CA   . SER   B 15  ? 1.01957  0.693265 0.668649 0.0572547   -0.200088   0.0926783   27  SER   A CA   
1998 C C    . SER   B 15  ? 1.01734  0.693366 0.648085 0.0321968   -0.224866   0.0858956   27  SER   A C    
1999 O O    . SER   B 15  ? 1.03667  0.719223 0.654156 0.0221732   -0.257713   0.0965421   27  SER   A O    
2000 C CB   . SER   B 15  ? 1.01218  0.72907  0.736827 0.0690028   -0.187589   0.0988725   27  SER   A CB   
2001 O OG   . SER   B 15  ? 1.07863  0.785169 0.812899 0.0911407   -0.168043   0.105414    27  SER   A OG   
2002 H H    . SER   B 15  ? 0.943252 0.589427 0.582689 0.0654151   -0.15162    0.0707283   27  SER   A H    
2003 H HA   . SER   B 15  ? 1.03765  0.704701 0.672496 0.0638656   -0.211443   0.104812    27  SER   A HA   
2004 H HB2  . SER   B 15  ? 0.996103 0.716    0.729821 0.06381     -0.173057   0.0871007   27  SER   A HB2  
2005 H HB3  . SER   B 15  ? 1.02562  0.772011 0.781147 0.0665567   -0.206645   0.110615    27  SER   A HB3  
2007 N N    . LYS   B 16  ? 0.922911 0.59214  0.552093 0.0209789   -0.210119   0.06878     28  LYS   A N    
2008 C CA   . LYS   B 16  ? 1.03252  0.70144  0.650767 -0.00395284 -0.230253   0.0614214   28  LYS   A CA   
2009 C C    . LYS   B 16  ? 1.04253  0.658348 0.578912 -0.0167731  -0.240014   0.0499203   28  LYS   A C    
2010 O O    . LYS   B 16  ? 1.07334  0.67774  0.587064 -0.0396185  -0.260208   0.0424895   28  LYS   A O    
2011 C CB   . LYS   B 16  ? 1.08236  0.758556 0.726986 -0.00965451 -0.20811    0.0493104   28  LYS   A CB   
2012 C CG   . LYS   B 16  ? 1.12319  0.853015 0.845942 -0.00196331 -0.200162   0.0598432   28  LYS   A CG   
2013 C CD   . LYS   B 16  ? 1.03911  0.773892 0.782043 -0.00347914 -0.172719   0.0496343   28  LYS   A CD   
2014 C CE   . LYS   B 16  ? 1.14589  0.884785 0.894861 -0.0274824  -0.183656   0.0454857   28  LYS   A CE   
2015 N NZ   . LYS   B 16  ? 1.14917  0.888765 0.910958 -0.0273902  -0.156296   0.038168    28  LYS   A NZ   
2016 H H    . LYS   B 16  ? 0.935628 0.599341 0.570602 0.0282999   -0.187331   0.0618967   28  LYS   A H    
2017 H HA   . LYS   B 16  ? 1.02576  0.724234 0.673446 -0.00946034 -0.251943   0.0726654   28  LYS   A HA   
2018 H HB2  . LYS   B 16  ? 1.06544  0.719547 0.689915 -0.00182785 -0.186762   0.0410153   28  LYS   A HB2  
2019 H HB3  . LYS   B 16  ? 1.09455  0.760992 0.724251 -0.0266146  -0.218866   0.0430252   28  LYS   A HB3  
2020 H HG2  . LYS   B 16  ? 1.10186  0.856528 0.849459 -0.0119748  -0.220628   0.0680614   28  LYS   A HG2  
2021 H HG3  . LYS   B 16  ? 1.08077  0.818775 0.817775 0.0143522   -0.193007   0.0669754   28  LYS   A HG3  
2022 H HD2  . LYS   B 16  ? 1.04786  0.809878 0.831081 0.00672443  -0.161638   0.0554969   28  LYS   A HD2  
2023 H HD3  . LYS   B 16  ? 1.06862  0.775656 0.78024  0.00160775  -0.157166   0.0405384   28  LYS   A HD3  
2024 H HE2  . LYS   B 16  ? 1.15785  0.866384 0.865161 -0.0377819  -0.194248   0.0386145   28  LYS   A HE2  
2025 H HE3  . LYS   B 16  ? 1.13066  0.901059 0.916019 -0.0337648  -0.198484   0.0551977   28  LYS   A HE3  
2026 H HZ1  . LYS   B 16  ? 1.13545  0.849944 0.868017 -0.0209015  -0.143389   0.0307555   28  LYS   A HZ1  
2027 H HZ2  . LYS   B 16  ? 1.11698  0.883675 0.914674 -0.0193977  -0.146211   0.0436845   28  LYS   A HZ2  
2028 H HZ3  . LYS   B 16  ? 1.14793  0.885388 0.910428 -0.0420579  -0.162059   0.0361345   28  LYS   A HZ3  
2029 N N    . LYS   B 17  ? 1.01277  0.594516 0.504894 -0.00263445 -0.223791   0.048266    29  LYS   A N    
2030 C CA   . LYS   B 17  ? 1.07118  0.598749 0.482886 -0.00986941 -0.223076   0.037028    29  LYS   A CA   
2031 C C    . LYS   B 17  ? 1.0916   0.593352 0.484007 -0.0241555  -0.211429   0.0171462   29  LYS   A C    
2032 O O    . LYS   B 17  ? 1.08886  0.564006 0.437921 -0.0440034  -0.230492   0.008325    29  LYS   A O    
2033 C CB   . LYS   B 17  ? 1.15112  0.66783  0.518311 -0.0241312  -0.260434   0.0440065   29  LYS   A CB   
2034 C CG   . LYS   B 17  ? 1.18156  0.715592 0.555329 -0.00934594 -0.274549   0.066996    29  LYS   A CG   
2035 C CD   . LYS   B 17  ? 1.21069  0.723011 0.570273 0.0134517   -0.241858   0.069768    29  LYS   A CD   
2036 C CE   . LYS   B 17  ? 1.42762  0.959094 0.805782 0.0293366   -0.254521   0.0951794   29  LYS   A CE   
2037 N NZ   . LYS   B 17  ? 1.40527  0.942916 0.82234  0.0516352   -0.222712   0.0999057   29  LYS   A NZ   
2038 H H    . LYS   B 17  ? 1.00133  0.59289  0.514347 0.0122123   -0.210625   0.0542592   29  LYS   A H    
2039 H HA   . LYS   B 17  ? 1.07233  0.583856 0.46818  0.0032418   -0.204336   0.0374448   29  LYS   A HA   
2040 H HB2  . LYS   B 17  ? 1.15477  0.691394 0.543363 -0.0384441  -0.280512   0.0445591   29  LYS   A HB2  
2041 H HB3  . LYS   B 17  ? 1.1911   0.667401 0.500332 -0.0302518  -0.256708   0.0333924   29  LYS   A HB3  
2042 H HG2  . LYS   B 17  ? 1.15914  0.733527 0.589202 -0.0055548  -0.283699   0.0782974   29  LYS   A HG2  
2043 H HG3  . LYS   B 17  ? 1.23624  0.755879 0.568344 -0.0192539  -0.297153   0.0702295   29  LYS   A HG3  
2044 H HD2  . LYS   B 17  ? 1.27311  0.747558 0.577043 0.0104584   -0.233624   0.0614057   29  LYS   A HD2  
2045 H HD3  . LYS   B 17  ? 1.19599  0.71838  0.589635 0.0207635   -0.219966   0.0642192   29  LYS   A HD3  
2046 H HE2  . LYS   B 17  ? 1.36925  0.93371  0.783956 0.0262298   -0.276409   0.10547     29  LYS   A HE2  
2047 H HE3  . LYS   B 17  ? 1.4221   0.927829 0.748831 0.0275334   -0.262838   0.0994715   29  LYS   A HE3  
2048 H HZ1  . LYS   B 17  ? 1.35823  0.919228 0.820087 0.0534092   -0.21538    0.0961936   29  LYS   A HZ1  
2049 H HZ2  . LYS   B 17  ? 1.40083  0.911495 0.788511 0.0536093   -0.203081   0.0913895   29  LYS   A HZ2  
2050 H HZ3  . LYS   B 17  ? 1.40837  0.952449 0.833582 0.0612798   -0.229608   0.115308    29  LYS   A HZ3  
2051 N N    . ASP   B 18  ? 1.04173  0.551098 0.46646  -0.0149024  -0.182179   0.0112252   30  ASP   A N    
2052 C CA   . ASP   B 18  ? 0.9901   0.474601 0.400671 -0.0239125  -0.167515   -0.00395437 30  ASP   A CA   
2053 C C    . ASP   B 18  ? 1.01099  0.46148  0.388272 -0.00937229 -0.136161   -0.011033   30  ASP   A C    
2054 O O    . ASP   B 18  ? 0.98788  0.425437 0.36744  -0.00874088 -0.116678   -0.0193478  30  ASP   A O    
2055 C CB   . ASP   B 18  ? 0.978724 0.501454 0.452888 -0.0244921  -0.158908   -0.00181833 30  ASP   A CB   
2056 C CG   . ASP   B 18  ? 0.873256 0.425873 0.389899 -0.00486153 -0.137707   0.00521963  30  ASP   A CG   
2057 O OD1  . ASP   B 18  ? 0.895694 0.433677 0.392301 0.00972686  -0.123785   0.00645072  30  ASP   A OD1  
2058 O OD2  . ASP   B 18  ? 0.830153 0.420153 0.399019 -0.00572886 -0.135816   0.00976547  30  ASP   A OD2  
2059 H H    . ASP   B 18  ? 0.994926 0.524437 0.45032  -0.00257277 -0.171456   0.0174395   30  ASP   A H    
2060 H HA   . ASP   B 18  ? 1.05047  0.514702 0.431631 -0.0385927  -0.182222   -0.00998674 30  ASP   A HA   
2061 H HB2  . ASP   B 18  ? 0.960012 0.464859 0.424316 -0.0296293  -0.148975   -0.0100335  30  ASP   A HB2  
2062 H HB3  . ASP   B 18  ? 0.956488 0.502751 0.455396 -0.0342619  -0.17745    0.003442    30  ASP   A HB3  
2063 N N    . ARG   B 19  ? 0.982749 0.422966 0.336355 0.00364014  -0.129518   -0.00492953 31  ARG   A N    
2064 C CA   . ARG   B 19  ? 0.982672 0.394058 0.308414 0.0164512   -0.0991907  -0.0094318  31  ARG   A CA   
2065 C C    . ARG   B 19  ? 0.953769 0.387476 0.326873 0.0256252   -0.0751897  -0.0102024  31  ARG   A C    
2066 O O    . ARG   B 19  ? 0.963318 0.377489 0.322243 0.0330859   -0.0513016  -0.0144658  31  ARG   A O    
2067 C CB   . ARG   B 19  ? 1.1067   0.465364 0.366849 0.00772751  -0.0955966  -0.0229658  31  ARG   A CB   
2068 C CG   . ARG   B 19  ? 1.18521  0.519333 0.387529 7.51e-06    -0.117637   -0.0209714  31  ARG   A CG   
2069 C CD   . ARG   B 19  ? 1.2541   0.534383 0.387738 -0.0128487  -0.118736   -0.0369675  31  ARG   A CD   
2070 N NE   . ARG   B 19  ? 1.27312  0.518092 0.378669 0.00146109  -0.0801761  -0.0441598  31  ARG   A NE   
2071 C CZ   . ARG   B 19  ? 1.28045  0.511577 0.359008 0.0155489   -0.0602143  -0.0379866  31  ARG   A CZ   
2072 N NH1  . ARG   B 19  ? 1.31827  0.550133 0.370333 0.0161899   -0.0741803  -0.0270628  31  ARG   A NH1  
2073 N NH2  . ARG   B 19  ? 1.35852  0.572423 0.434571 0.0293102   -0.0241645  -0.0414465  31  ARG   A NH2  
2074 H H    . ARG   B 19  ? 0.998762 0.451095 0.355582 0.004557    -0.143953   0.00360033  31  ARG   A H    
2075 H HA   . ARG   B 19  ? 1.00613  0.416204 0.321859 0.0241022   -0.097717   -0.00226578 31  ARG   A HA   
2076 H HB2  . ARG   B 19  ? 1.09741  0.453672 0.363838 -0.00223343 -0.101456   -0.0295815  31  ARG   A HB2  
2077 H HB3  . ARG   B 19  ? 1.09834  0.439742 0.345744 0.0169191   -0.0726032  -0.0258642  31  ARG   A HB3  
2078 H HG2  . ARG   B 19  ? 1.18545  0.515127 0.375012 0.0104203   -0.108076   -0.0143803  31  ARG   A HG2  
2079 H HG3  . ARG   B 19  ? 1.17332  0.532158 0.396521 -0.00707501 -0.141346   -0.0144582  31  ARG   A HG3  
2080 H HD2  . ARG   B 19  ? 1.30043  0.566104 0.394181 -0.0197078  -0.13566    -0.0356117  31  ARG   A HD2  
2081 H HD3  . ARG   B 19  ? 1.25431  0.535722 0.400538 -0.0240451  -0.127085   -0.0437459  31  ARG   A HD3  
2082 H HE   . ARG   B 19  ? 1.26943  0.502398 0.378513 0.0009275   -0.0686428  -0.0519673  31  ARG   A HE   
2083 H HH11 . ARG   B 19  ? 1.30674  0.559807 0.373677 0.010369    -0.0976216  -0.0203928  31  ARG   A HH11 
2084 H HH12 . ARG   B 19  ? 1.34372  0.554941 0.363469 0.0229158   -0.0595835  -0.0252225  31  ARG   A HH12 
2085 H HH21 . ARG   B 19  ? 1.36644  0.548534 0.4121   0.0281601   -0.0128192  -0.0514716  31  ARG   A HH21 
2086 H HH22 . ARG   B 19  ? 1.29722  0.53107  0.402365 0.0395953   -0.0112155  -0.0334292  31  ARG   A HH22 
2087 N N    . GLY   B 20  ? 0.889476 0.36565  0.31838  0.0269878   -0.0801373  -0.0040701  32  GLY   A N    
2088 C CA   . GLY   B 20  ? 0.896975 0.393991 0.363862 0.0339538   -0.0599424  -0.00459236 32  GLY   A CA   
2089 C C    . GLY   B 20  ? 0.898865 0.399958 0.37308  0.0468955   -0.042755   0.00016048  32  GLY   A C    
2090 O O    . GLY   B 20  ? 0.851775 0.364537 0.347735 0.0510008   -0.0259083  -0.00108846 32  GLY   A O    
2091 H H    . GLY   B 20  ? 0.90394  0.396454 0.34662  0.0236013   -0.0961549  0.00087251  32  GLY   A H    
2092 H HA2  . GLY   B 20  ? 0.891577 0.374855 0.348575 0.0321001   -0.0509549  -0.00983816 32  GLY   A HA2  
2093 H HA3  . GLY   B 20  ? 0.863998 0.386556 0.363108 0.0309471   -0.0663394  -0.00251099 32  GLY   A HA3  
2094 N N    . VAL   B 21  ? 0.858927 0.351979 0.317032 0.0518082   -0.0488932  0.00704637  33  VAL   A N    
2095 C CA   . VAL   B 21  ? 0.877615 0.368195 0.339001 0.0616999   -0.0332382  0.0124267   33  VAL   A CA   
2096 C C    . VAL   B 21  ? 0.907564 0.365854 0.320078 0.0645734   -0.0338189  0.0177526   33  VAL   A C    
2097 O O    . VAL   B 21  ? 0.941936 0.397682 0.340334 0.0634441   -0.0538642  0.0248493   33  VAL   A O    
2098 C CB   . VAL   B 21  ? 0.807625 0.323626 0.309366 0.0673703   -0.0356884  0.018764    33  VAL   A CB   
2099 C CG1  . VAL   B 21  ? 0.794132 0.300533 0.296175 0.0743411   -0.0179906  0.0226007   33  VAL   A CG1  
2100 C CG2  . VAL   B 21  ? 0.792027 0.338718 0.336784 0.0644805   -0.0333594  0.0132194   33  VAL   A CG2  
2101 H H    . VAL   B 21  ? 0.898703 0.387411 0.343348 0.0479811   -0.0642568  0.0093108   33  VAL   A H    
2102 H HA   . VAL   B 21  ? 0.84832  0.338593 0.315054 0.0629203   -0.0184467  0.00896846  33  VAL   A HA   
2103 H HB   . VAL   B 21  ? 0.831975 0.349485 0.331059 0.0681493   -0.0500594  0.0247534   33  VAL   A HB   
2104 H HG11 . VAL   B 21  ? 0.787307 0.293073 0.290781 0.0727124   -0.0054666  0.0180352   33  VAL   A HG11 
2105 H HG12 . VAL   B 21  ? 0.825395 0.31344  0.301608 0.0768784   -0.019038   0.0282907   33  VAL   A HG12 
2106 H HG13 . VAL   B 21  ? 0.784594 0.303127 0.311367 0.0775363   -0.0175383  0.0245574   33  VAL   A HG13 
2107 H HG21 . VAL   B 21  ? 0.774582 0.3327   0.340794 0.069009    -0.032347   0.0160975   33  VAL   A HG21 
2108 H HG22 . VAL   B 21  ? 0.785364 0.339519 0.333502 0.0591169   -0.0442177  0.0119996   33  VAL   A HG22 
2109 H HG23 . VAL   B 21  ? 0.772234 0.318775 0.318741 0.0632371   -0.021542   0.00863694  33  VAL   A HG23 
2110 N N    . LEU   B 22  ? 0.944836 0.38267  0.336025 0.0687153   -0.0114235  0.016427    34  LEU   A N    
2111 C CA   . LEU   B 22  ? 0.984589 0.387208 0.322124 0.0713514   -0.00524788 0.020433    34  LEU   A CA   
2112 C C    . LEU   B 22  ? 0.932939 0.334984 0.280862 0.0789849   0.0152708   0.0296823   34  LEU   A C    
2113 O O    . LEU   B 22  ? 0.897257 0.315923 0.279909 0.0803482   0.0313273   0.0279954   34  LEU   A O    
2114 C CB   . LEU   B 22  ? 1.0584   0.430259 0.353995 0.0688442   0.00571611  0.0101616   34  LEU   A CB   
2115 C CG   . LEU   B 22  ? 1.09778  0.463232 0.380167 0.0579916   -0.0143176  -0.0001907  34  LEU   A CG   
2116 C CD1  . LEU   B 22  ? 1.13935  0.466762 0.379866 0.0562948   -1.866e-05  -0.0120649  34  LEU   A CD1  
2117 C CD2  . LEU   B 22  ? 1.1104   0.466277 0.359641 0.049939    -0.0431511  0.00317606  34  LEU   A CD2  
2118 H H    . LEU   B 22  ? 0.912258 0.359487 0.32347  0.0699315   0.00102737  0.0137254   34  LEU   A H    
2119 H HA   . LEU   B 22  ? 1.00539  0.403836 0.327014 0.0694244   -0.0223686  0.0249248   34  LEU   A HA   
2120 H HB2  . LEU   B 22  ? 1.03491  0.412761 0.349413 0.0724767   0.023058    0.00812679  34  LEU   A HB2  
2121 H HB3  . LEU   B 22  ? 1.09468  0.441623 0.35081  0.0708513   0.0113132   0.0127718   34  LEU   A HB3  
2122 H HG   . LEU   B 22  ? 1.05091  0.442037 0.37264  0.0558099   -0.0197004  -0.00129623 34  LEU   A HG   
2123 H HD11 . LEU   B 22  ? 1.11734  0.451032 0.379489 0.0623283   0.018208    -0.0127394  34  LEU   A HD11 
2124 H HD12 . LEU   B 22  ? 1.14784  0.470884 0.382843 0.0474776   -0.0142019  -0.0186005  34  LEU   A HD12 
2125 H HD13 . LEU   B 22  ? 1.18136  0.481323 0.378657 0.0579779   0.00587749  -0.0120253  34  LEU   A HD13 
2126 H HD21 . LEU   B 22  ? 1.09489  0.474753 0.372788 0.0518681   -0.0537216  0.0114891   34  LEU   A HD21 
2127 H HD22 . LEU   B 22  ? 1.15934  0.488999 0.365696 0.0516854   -0.0383702  0.00482792  34  LEU   A HD22 
2128 H HD23 . LEU   B 22  ? 1.12954  0.481285 0.37148  0.0407198   -0.0561578  -0.00382487 34  LEU   A HD23 
2129 N N    . LYS   B 23  ? 1.01299  0.398249 0.334553 0.0826518   0.0120897   0.0416311   35  LYS   A N    
2130 C CA   . LYS   B 23  ? 0.936798 0.322024 0.275188 0.0878687   0.0290604   0.0521538   35  LYS   A CA   
2131 C C    . LYS   B 23  ? 0.999411 0.350053 0.284871 0.0908886   0.0443579   0.0609245   35  LYS   A C    
2132 O O    . LYS   B 23  ? 1.10005  0.428777 0.336278 0.0902058   0.0302643   0.064208    35  LYS   A O    
2133 C CB   . LYS   B 23  ? 0.995612 0.390121 0.354042 0.0914601   0.0118731   0.062771    35  LYS   A CB   
2134 C CG   . LYS   B 23  ? 0.967939 0.352924 0.337947 0.0963328   0.0268654   0.0754452   35  LYS   A CG   
2135 C CD   . LYS   B 23  ? 1.00569  0.386474 0.38069  0.103705    0.0115404   0.0908304   35  LYS   A CD   
2136 C CE   . LYS   B 23  ? 1.00163  0.371881 0.398591 0.106372    0.0310996   0.0989912   35  LYS   A CE   
2137 N NZ   . LYS   B 23  ? 1.00688  0.362993 0.405102 0.116068    0.0229814   0.117738    35  LYS   A NZ   
2138 H H    . LYS   B 23  ? 1.01481  0.387655 0.306822 0.0809857   -0.00154393 0.0438391   35  LYS   A H    
2139 H HA   . LYS   B 23  ? 0.932162 0.33125  0.300118 0.0870409   0.0415981   0.0480167   35  LYS   A HA   
2140 H HB2  . LYS   B 23  ? 0.939538 0.355791 0.331675 0.09025     0.00463896  0.0572384   35  LYS   A HB2  
2141 H HB3  . LYS   B 23  ? 1.00043  0.385548 0.331915 0.091748    -0.00355198 0.0676598   35  LYS   A HB3  
2142 H HG2  . LYS   B 23  ? 1.00617  0.372546 0.348372 0.0964395   0.0400463   0.0798161   35  LYS   A HG2  
2143 H HG3  . LYS   B 23  ? 0.949257 0.347855 0.352433 0.0942852   0.0365677   0.069903    35  LYS   A HG3  
2144 H HD2  . LYS   B 23  ? 0.978725 0.378383 0.379643 0.104792    -0.00175742 0.0874602   35  LYS   A HD2  
2145 H HD3  . LYS   B 23  ? 1.03718  0.402311 0.375752 0.105394    0.00304114  0.0995425   35  LYS   A HD3  
2146 H HE2  . LYS   B 23  ? 1.01218  0.368726 0.390223 0.103657    0.0464675   0.101175    35  LYS   A HE2  
2147 H HE3  . LYS   B 23  ? 0.964081 0.349522 0.395001 0.103586    0.0363097   0.089619    35  LYS   A HE3  
2148 H HZ1  . LYS   B 23  ? 1.04713  0.389657 0.411879 0.118315    0.0165236   0.127825    35  LYS   A HZ1  
2149 H HZ2  . LYS   B 23  ? 0.999497 0.369993 0.420588 0.119875    0.0108971   0.11656     35  LYS   A HZ2  
2150 H HZ3  . LYS   B 23  ? 1.01671  0.362743 0.426478 0.116034    0.036842    0.121123    35  LYS   A HZ3  
2151 N N    . ILE   B 24  ? 1.0365   0.383664 0.332398 0.092971    0.071284    0.0662882   36  ILE   A N    
2152 C CA   . ILE   B 24  ? 1.07251  0.388897 0.32443  0.0962877   0.0894336   0.0789      36  ILE   A CA   
2153 C C    . ILE   B 24  ? 1.06412  0.38681  0.350986 0.0964373   0.101193    0.0915557   36  ILE   A C    
2154 O O    . ILE   B 24  ? 0.977816 0.325086 0.316898 0.0924403   0.110993    0.0866611   36  ILE   A O    
2155 C CB   . ILE   B 24  ? 1.10224  0.406267 0.334145 0.0980616   0.118712    0.0734202   36  ILE   A CB   
2156 C CG1  . ILE   B 24  ? 1.19977  0.496854 0.407936 0.0969828   0.108603    0.057488    36  ILE   A CG1  
2157 C CG2  . ILE   B 24  ? 1.14732  0.417269 0.327589 0.101835    0.142296    0.086413    36  ILE   A CG2  
2158 C CD1  . ILE   B 24  ? 1.24879  0.557566 0.484253 0.0997911   0.130929    0.0487557   36  ILE   A CD1  
2159 H H    . ILE   B 24  ? 0.989202 0.354714 0.321404 0.0914603   0.078924    0.0626511   36  ILE   A H    
2160 H HA   . ILE   B 24  ? 1.11302  0.412229 0.327135 0.097101    0.0763507   0.0833246   36  ILE   A HA   
2161 H HB   . ILE   B 24  ? 1.07873  0.403205 0.352205 0.0972391   0.130392    0.0723427   36  ILE   A HB   
2162 H HG12 . ILE   B 24  ? 1.23834  0.507254 0.394559 0.0975195   0.108645    0.057589    36  ILE   A HG12 
2163 H HG13 . ILE   B 24  ? 1.16566  0.476645 0.389835 0.0936156   0.086446    0.0531906   36  ILE   A HG13 
2164 H HG21 . ILE   B 24  ? 1.16443  0.428026 0.335835 0.104366    0.162936    0.0825817   36  ILE   A HG21 
2165 H HG22 . ILE   B 24  ? 1.19092  0.439695 0.325934 0.101918    0.129523    0.088555    36  ILE   A HG22 
2166 H HG23 . ILE   B 24  ? 1.14648  0.421596 0.347505 0.101396    0.150033    0.096999    36  ILE   A HG23 
2167 H HD11 . ILE   B 24  ? 1.1801   0.517441 0.463355 0.0977766   0.126637    0.047811    36  ILE   A HD11 
2168 H HD12 . ILE   B 24  ? 1.2418   0.537942 0.454658 0.0995413   0.126323    0.0391707   36  ILE   A HD12 
2169 H HD13 . ILE   B 24  ? 1.2452   0.545345 0.473521 0.103842    0.154551    0.0544354   36  ILE   A HD13 
2170 N N    . VAL   B 25  ? 1.07017  0.368263 0.32522  0.0997714   0.0995997   0.108314    37  VAL   A N    
2171 C CA   . VAL   B 25  ? 1.08049  0.371876 0.356339 0.0995568   0.114081    0.12316     37  VAL   A CA   
2172 C C    . VAL   B 25  ? 1.12077  0.402656 0.387609 0.0969714   0.148527    0.128155    37  VAL   A C    
2173 O O    . VAL   B 25  ? 1.18524  0.44221  0.396644 0.100434    0.159455    0.133202    37  VAL   A O    
2174 C CB   . VAL   B 25  ? 1.14485  0.4097   0.382951 0.105786    0.100036    0.142833    37  VAL   A CB   
2175 C CG1  . VAL   B 25  ? 1.13724  0.386062 0.390586 0.105595    0.118527    0.160642    37  VAL   A CG1  
2176 C CG2  . VAL   B 25  ? 1.13567  0.417025 0.392821 0.109904    0.0661166   0.140273    37  VAL   A CG2  
2177 H H    . VAL   B 25  ? 1.11259  0.395755 0.328924 0.101633    0.0882291   0.111113    37  VAL   A H    
2178 H HA   . VAL   B 25  ? 1.04951  0.358765 0.368646 0.0969807   0.111087    0.118364    37  VAL   A HA   
2179 H HB   . VAL   B 25  ? 1.17924  0.425997 0.368904 0.10703     0.101306    0.146326    37  VAL   A HB   
2180 H HG11 . VAL   B 25  ? 1.10919  0.37296  0.407416 0.101963    0.121832    0.154401    37  VAL   A HG11 
2181 H HG12 . VAL   B 25  ? 1.16823  0.40481  0.402117 0.103391    0.139086    0.165855    37  VAL   A HG12 
2182 H HG13 . VAL   B 25  ? 1.17153  0.406445 0.409122 0.110928    0.10689     0.173665    37  VAL   A HG13 
2183 H HG21 . VAL   B 25  ? 1.16176  0.429829 0.403429 0.114942    0.0570636   0.155058    37  VAL   A HG21 
2184 H HG22 . VAL   B 25  ? 1.13052  0.417856 0.371094 0.108535    0.0537622   0.131394    37  VAL   A HG22 
2185 H HG23 . VAL   B 25  ? 1.09336  0.392371 0.395192 0.108714    0.0665172   0.133485    37  VAL   A HG23 
2186 N N    . LYS   B 26  ? 1.10302  0.403093 0.421577 0.0902368   0.166002    0.128222    38  LYS   A N    
2187 C CA   . LYS   B 26  ? 1.15866  0.458484 0.481541 0.0871019   0.199263    0.135073    38  LYS   A CA   
2188 C C    . LYS   B 26  ? 1.14032  0.423649 0.4709   0.0818521   0.21579     0.154151    38  LYS   A C    
2189 O O    . LYS   B 26  ? 1.13323  0.404755 0.448129 0.0811013   0.244773    0.166895    38  LYS   A O    
2190 C CB   . LYS   B 26  ? 1.09749  0.436342 0.47885  0.0806834   0.207189    0.123438    38  LYS   A CB   
2191 C CG   . LYS   B 26  ? 1.14613  0.498833 0.522194 0.0859797   0.19397     0.106685    38  LYS   A CG   
2192 C CD   . LYS   B 26  ? 1.16474  0.490992 0.481334 0.0954617   0.205888    0.105753    38  LYS   A CD   
2193 C CE   . LYS   B 26  ? 1.18859  0.502641 0.491435 0.0985024   0.243464    0.118154    38  LYS   A CE   
2194 N NZ   . LYS   B 26  ? 1.23841  0.542793 0.512636 0.10768     0.25806     0.108787    38  LYS   A NZ   
2195 H H    . LYS   B 26  ? 1.07832  0.392366 0.431558 0.0868884   0.156983    0.123884    38  LYS   A H    
2196 H HA   . LYS   B 26  ? 1.17302  0.457093 0.454758 0.0923998   0.207609    0.136407    38  LYS   A HA   
2197 H HB2  . LYS   B 26  ? 1.08809  0.440403 0.505265 0.0738706   0.198915    0.121077    38  LYS   A HB2  
2198 H HB3  . LYS   B 26  ? 1.12635  0.468027 0.514963 0.0792276   0.229749    0.130294    38  LYS   A HB3  
2199 H HG2  . LYS   B 26  ? 1.10686  0.46081  0.482025 0.0861128   0.172098    0.100494    38  LYS   A HG2  
2200 H HG3  . LYS   B 26  ? 1.09006  0.467959 0.504077 0.0824419   0.198889    0.102101    38  LYS   A HG3  
2201 H HD2  . LYS   B 26  ? 1.19274  0.497455 0.470167 0.0976952   0.192756    0.107245    38  LYS   A HD2  
2202 H HD3  . LYS   B 26  ? 1.14878  0.485501 0.471634 0.0975166   0.20122     0.0949449   38  LYS   A HD3  
2203 H HE2  . LYS   B 26  ? 1.17533  0.511625 0.523313 0.0935811   0.254827    0.122948    38  LYS   A HE2  
2204 H HE3  . LYS   B 26  ? 1.23756  0.526962 0.504868 0.0994001   0.247769    0.127891    38  LYS   A HE3  
2205 H HZ1  . LYS   B 26  ? 1.19471  0.522421 0.504883 0.107619    0.256546    0.102403    38  LYS   A HZ1  
2206 H HZ2  . LYS   B 26  ? 1.25016  0.534308 0.483467 0.109959    0.244903    0.102334    38  LYS   A HZ2  
2207 H HZ3  . LYS   B 26  ? 1.25945  0.553449 0.5202   0.111175    0.282695    0.116177    38  LYS   A HZ3  
2208 N N    . ARG   B 27  ? 1.14788  0.429678 0.507133 0.0775601   0.201717    0.156506    39  ARG   A N    
2209 C CA   . ARG   B 27  ? 1.2198   0.47456  0.576089 0.0737938   0.215906    0.176704    39  ARG   A CA   
2210 C C    . ARG   B 27  ? 1.22774  0.462723 0.573158 0.0815433   0.191285    0.182108    39  ARG   A C    
2211 O O    . ARG   B 27  ? 1.15057  0.402207 0.526958 0.0822985   0.171003    0.167944    39  ARG   A O    
2212 C CB   . ARG   B 27  ? 1.23035  0.4978   0.644029 0.0574754   0.233054    0.177848    39  ARG   A CB   
2213 C CG   . ARG   B 27  ? 1.28833  0.523758 0.700369 0.0510269   0.250516    0.199412    39  ARG   A CG   
2214 C CD   . ARG   B 27  ? 1.26855  0.514812 0.740044 0.0304457   0.261954    0.197289    39  ARG   A CD   
2215 N NE   . ARG   B 27  ? 1.2529   0.506466 0.755379 0.0266837   0.238355    0.178214    39  ARG   A NE   
2216 C CZ   . ARG   B 27  ? 1.21531  0.487301 0.766728 0.00846227  0.236305    0.164152    39  ARG   A CZ   
2217 N NH1  . ARG   B 27  ? 1.22654  0.524818 0.811535 -0.00839111 0.251905    0.16579     39  ARG   A NH1  
2218 N NH2  . ARG   B 27  ? 1.18265  0.447988 0.749442 0.0066744   0.218742    0.148513    39  ARG   A NH2  
2219 H H    . ARG   B 27  ? 1.11836  0.413817 0.498672 0.0771151   0.185133    0.145868    39  ARG   A H    
2220 H HA   . ARG   B 27  ? 1.25533  0.492816 0.575197 0.0772622   0.230041    0.188209    39  ARG   A HA   
2221 H HB2  . ARG   B 27  ? 1.21465  0.501142 0.641954 0.0533099   0.246833    0.175274    39  ARG   A HB2  
2222 H HB3  . ARG   B 27  ? 1.19394  0.474616 0.637364 0.0535698   0.218947    0.165746    39  ARG   A HB3  
2223 H HG2  . ARG   B 27  ? 1.30207  0.516056 0.69701  0.057903    0.237953    0.204728    39  ARG   A HG2  
2224 H HG3  . ARG   B 27  ? 1.3174   0.541885 0.701879 0.0535135   0.267719    0.211933    39  ARG   A HG3  
2225 H HD2  . ARG   B 27  ? 1.30942  0.531314 0.776131 0.0262052   0.274617    0.212461    39  ARG   A HD2  
2226 H HD3  . ARG   B 27  ? 1.2563   0.528252 0.749663 0.023403    0.272757    0.193787    39  ARG   A HD3  
2227 H HE   . ARG   B 27  ? 1.24556  0.490042 0.730973 0.0372777   0.224153    0.17573     39  ARG   A HE   
2228 H HH11 . ARG   B 27  ? 1.22012  0.531321 0.799196 -0.00500274 0.262716    0.172324    39  ARG   A HH11 
2229 H HH12 . ARG   B 27  ? 1.21376  0.517348 0.828486 -0.0235038  0.251634    0.160443    39  ARG   A HH12 
2230 H HH21 . ARG   B 27  ? 1.18727  0.444023 0.737438 0.0193069   0.207078    0.146219    39  ARG   A HH21 
2231 H HH22 . ARG   B 27  ? 1.18214  0.451574 0.775405 -0.0073682  0.219236    0.140429    39  ARG   A HH22 
2232 N N    . VAL   B 28  ? 1.27892  0.479396 0.577137 0.089126    0.193181    0.204022    40  VAL   A N    
2233 C CA   . VAL   B 28  ? 1.31152  0.495287 0.595868 0.100245    0.168324    0.214115    40  VAL   A CA   
2234 C C    . VAL   B 28  ? 1.32224  0.495093 0.654219 0.0962425   0.173171    0.218485    40  VAL   A C    
2235 O O    . VAL   B 28  ? 1.35042  0.509739 0.698391 0.085208    0.197587    0.22628     40  VAL   A O    
2236 C CB   . VAL   B 28  ? 1.4329   0.583453 0.648396 0.109142    0.166947    0.238804    40  VAL   A CB   
2237 C CG1  . VAL   B 28  ? 1.46487  0.602375 0.67579  0.121628    0.139905    0.254238    40  VAL   A CG1  
2238 C CG2  . VAL   B 28  ? 1.39671  0.550643 0.556803 0.111057    0.162926    0.230681    40  VAL   A CG2  
2239 H H    . VAL   B 28  ? 1.31519  0.503118 0.590027 0.0877463   0.210933    0.214302    40  VAL   A H    
2240 H HA   . VAL   B 28  ? 1.29502  0.496355 0.585153 0.104073    0.14923     0.201837    40  VAL   A HA   
2241 H HB   . VAL   B 28  ? 1.44277  0.575769 0.652302 0.104931    0.188465    0.251626    40  VAL   A HB   
2242 H HG11 . VAL   B 28  ? 1.42713  0.585586 0.660744 0.124508    0.121505    0.241347    40  VAL   A HG11 
2243 H HG12 . VAL   B 28  ? 1.47099  0.594002 0.704054 0.121522    0.148532    0.26431     40  VAL   A HG12 
2244 H HG13 . VAL   B 28  ? 1.50426  0.626604 0.66762  0.126929    0.132588    0.267889    40  VAL   A HG13 
2245 H HG21 . VAL   B 28  ? 1.46262  0.593552 0.574298 0.115405    0.1611      0.246023    40  VAL   A HG21 
2246 H HG22 . VAL   B 28  ? 1.40209  0.562642 0.567032 0.105346    0.183375    0.223312    40  VAL   A HG22 
2247 H HG23 . VAL   B 28  ? 1.38419  0.55547  0.551768 0.113354    0.142199    0.217822    40  VAL   A HG23 
2248 N N    . GLY   B 29  ? 1.35009  0.528474 0.707048 0.104369    0.151273    0.212272    41  GLY   A N    
2249 C CA   . GLY   B 29  ? 1.35613  0.516299 0.752741 0.103085    0.156453    0.214396    41  GLY   A CA   
2250 C C    . GLY   B 29  ? 1.44414  0.565385 0.814859 0.116429    0.154652    0.244723    41  GLY   A C    
2251 O O    . GLY   B 29  ? 1.48417  0.589503 0.805986 0.119492    0.158706    0.265067    41  GLY   A O    
2252 H H    . GLY   B 29  ? 1.32577  0.51852  0.675125 0.110867    0.13374     0.206299    41  GLY   A H    
2253 H HA2  . GLY   B 29  ? 1.35677  0.514219 0.771837 0.0901355   0.173647    0.210112    41  GLY   A HA2  
2254 H HA3  . GLY   B 29  ? 1.33154  0.506543 0.752762 0.106366    0.144202    0.200965    41  GLY   A HA3  
2255 N N    . ASN   B 30  ? 1.39637  0.500404 0.797966 0.124908    0.1502      0.24816     42  ASN   A N    
2256 C CA   . ASN   B 30  ? 1.5435   0.608562 0.927501 0.139575    0.149309    0.279989    42  ASN   A CA   
2257 C C    . ASN   B 30  ? 1.50097  0.566345 0.920513 0.157538    0.133252    0.279038    42  ASN   A C    
2258 O O    . ASN   B 30  ? 1.34118  0.429794 0.798653 0.154633    0.130154    0.252028    42  ASN   A O    
2259 C CB   . ASN   B 30  ? 1.60998  0.631922 0.998958 0.128506    0.178131    0.294067    42  ASN   A CB   
2260 C CG   . ASN   B 30  ? 1.61932  0.644759 1.05799  0.111097    0.191638    0.266132    42  ASN   A CG   
2261 O OD1  . ASN   B 30  ? 1.70243  0.73555  1.14797  0.0894085   0.209265    0.256607    42  ASN   A OD1  
2262 N ND2  . ASN   B 30  ? 1.61564  0.643949 1.08783  0.119974    0.181345    0.250667    42  ASN   A ND2  
2263 H H    . ASN   B 30  ? 1.39789  0.513125 0.830961 0.122299    0.148493    0.231159    42  ASN   A H    
2264 H HA   . ASN   B 30  ? 1.54607  0.611582 0.89219  0.145803    0.140218    0.294642    42  ASN   A HA   
2265 H HB2  . ASN   B 30  ? 1.65097  0.645282 1.03689  0.140016    0.176861    0.31362     42  ASN   A HB2  
2266 H HB3  . ASN   B 30  ? 1.63053  0.649876 0.993353 0.120435    0.189196    0.301835    42  ASN   A HB3  
2267 H HD21 . ASN   B 30  ? 1.57025  0.62499  1.05728  0.116179    0.174816    0.23042     42  ASN   A HD21 
2268 H HD22 . ASN   B 30  ? 1.63711  0.640033 1.11673  0.130243    0.182299    0.261099    42  ASN   A HD22 
2269 N N    . GLY   B 31  ? 1.48979  0.528454 0.896271 0.176672    0.125096    0.310836    43  GLY   A N    
2270 C CA   . GLY   B 31  ? 1.54642  0.586588 0.988092 0.199006    0.110246    0.317324    43  GLY   A CA   
2271 C C    . GLY   B 31  ? 1.54654  0.632017 0.980757 0.211296    0.0763183   0.319439    43  GLY   A C    
2272 O O    . GLY   B 31  ? 1.58306  0.697979 0.988933 0.199607    0.0658078   0.306343    43  GLY   A O    
2273 H H    . GLY   B 31  ? 1.55611  0.57594  0.931365 0.176524    0.129442    0.330387    43  GLY   A H    
2274 H HA2  . GLY   B 31  ? 1.58363  0.593054 1.02127  0.209552    0.114001    0.341242    43  GLY   A HA2  
2275 H HA3  . GLY   B 31  ? 1.51209  0.553178 0.988107 0.195542    0.119354    0.297348    43  GLY   A HA3  
2276 N N    . GLU   B 32  ? 1.62624  0.715992 1.09084  0.234945    0.0605786   0.336195    44  GLU   A N    
2277 C CA   . GLU   B 32  ? 1.54136  0.675415 1.00819  0.246901    0.0259004   0.343608    44  GLU   A CA   
2278 C C    . GLU   B 32  ? 1.41585  0.591172 0.930224 0.24454     0.0229961   0.310577    44  GLU   A C    
2279 O O    . GLU   B 32  ? 1.35765  0.574539 0.865573 0.241119    -0.00110958 0.303818    44  GLU   A O    
2280 C CB   . GLU   B 32  ? 1.57033  0.68956  1.04267  0.272813    0.0103144   0.385825    44  GLU   A CB   
2281 H H    . GLU   B 32  ? 1.61169  0.676079 1.09872  0.243552    0.0723633   0.343427    44  GLU   A H    
2282 H HA   . GLU   B 32  ? 1.53943  0.683513 0.965912 0.237093    0.0155245   0.344099    44  GLU   A HA   
2285 N N    . GLU   B 33  ? 1.35525  0.516238 0.909627 0.242698    0.0483516   0.288464    45  GLU   A N    
2286 C CA   . GLU   B 33  ? 1.35308  0.546829 0.954861 0.247117    0.04734     0.26457     45  GLU   A CA   
2287 C C    . GLU   B 33  ? 1.29603  0.512472 0.88931  0.222137    0.0538288   0.228219    45  GLU   A C    
2288 O O    . GLU   B 33  ? 1.26649  0.463019 0.836355 0.203007    0.0703385   0.216702    45  GLU   A O    
2289 C CB   . GLU   B 33  ? 1.43689  0.607597 1.08846  0.265845    0.0662936   0.263754    45  GLU   A CB   
2290 C CG   . GLU   B 33  ? 1.47453  0.583838 1.12597  0.261011    0.0987696   0.258929    45  GLU   A CG   
2291 C CD   . GLU   B 33  ? 1.58104  0.646991 1.1965   0.259278    0.103601    0.287834    45  GLU   A CD   
2292 O OE1  . GLU   B 33  ? 1.67814  0.716191 1.30096  0.281621    0.102724    0.320401    45  GLU   A OE1  
2293 O OE2  . GLU   B 33  ? 1.63497  0.697363 1.21418  0.235151    0.108728    0.27915     45  GLU   A OE2  
2294 H H    . GLU   B 33  ? 1.39592  0.524612 0.945021 0.237086    0.0672918   0.287905    45  GLU   A H    
2295 H HA   . GLU   B 33  ? 1.34762  0.571764 0.955732 0.256076    0.0255535   0.274611    45  GLU   A HA   
2296 H HB2  . GLU   B 33  ? 1.3863   0.579501 1.06134  0.2642      0.0685673   0.243325    45  GLU   A HB2  
2297 H HB3  . GLU   B 33  ? 1.44336  0.617865 1.10925  0.285191    0.054938    0.287384    45  GLU   A HB3  
2298 H HG2  . GLU   B 33  ? 1.46264  0.571528 1.10906  0.242453    0.109901    0.233734    45  GLU   A HG2  
2299 H HG3  . GLU   B 33  ? 1.50172  0.597284 1.18395  0.276598    0.108256    0.260292    45  GLU   A HG3  
2300 N N    . THR   B 34  ? 1.22573  0.487221 0.841936 0.223169    0.0397449   0.213167    46  THR   A N    
2301 C CA   . THR   B 34  ? 1.21547  0.500395 0.833426 0.203792    0.0457552   0.18021     46  THR   A CA   
2302 C C    . THR   B 34  ? 1.21407  0.509748 0.878326 0.210803    0.0574082   0.161245    46  THR   A C    
2303 O O    . THR   B 34  ? 1.12975  0.425288 0.827889 0.232176    0.0577369   0.173155    46  THR   A O    
2304 C CB   . THR   B 34  ? 1.21363  0.539466 0.813158 0.197723    0.0198368   0.179566    46  THR   A CB   
2305 O OG1  . THR   B 34  ? 1.14682  0.496518 0.778751 0.217116    0.00160126  0.195792    46  THR   A OG1  
2306 C CG2  . THR   B 34  ? 1.32516  0.637353 0.870014 0.189413    0.0112896   0.193568    46  THR   A CG2  
2307 H H    . THR   B 34  ? 1.24418  0.523563 0.877024 0.236534    0.025382    0.225541    46  THR   A H    
2308 H HA   . THR   B 34  ? 1.21697  0.483647 0.817502 0.190303    0.0589786   0.17179     46  THR   A HA   
2309 H HB   . THR   B 34  ? 1.17326  0.517004 0.778361 0.187124    0.0227619   0.159294    46  THR   A HB   
2311 H HG21 . THR   B 34  ? 1.28344  0.618164 0.814862 0.184347    -0.00410789 0.189834    46  THR   A HG21 
2312 H HG22 . THR   B 34  ? 1.3327   0.629613 0.869445 0.199979    0.00571818  0.215298    46  THR   A HG22 
2313 H HG23 . THR   B 34  ? 1.29447  0.589855 0.825013 0.17841     0.0273469   0.185075    46  THR   A HG23 
2314 N N    . PRO   B 35  ? 1.22027  0.527084 0.888231 0.194146    0.0683654   0.131449    47  PRO   A N    
2315 C CA   . PRO   B 35  ? 1.26112  0.575164 0.965039 0.201054    0.0808999   0.11393     47  PRO   A CA   
2316 C C    . PRO   B 35  ? 1.32157  0.680655 1.05793  0.216813    0.0648378   0.120896    47  PRO   A C    
2317 O O    . PRO   B 35  ? 1.23928  0.635082 0.965808 0.209273    0.0432007   0.122823    47  PRO   A O    
2318 C CB   . PRO   B 35  ? 1.22819  0.547717 0.91874  0.176466    0.0906904   0.0839838   47  PRO   A CB   
2319 C CG   . PRO   B 35  ? 1.14136  0.470784 0.79807  0.159297    0.0796218   0.0867428   47  PRO   A CG   
2320 C CD   . PRO   B 35  ? 1.21487  0.527929 0.853318 0.169804    0.0700136   0.115542    47  PRO   A CD   
2321 H HA   . PRO   B 35  ? 1.29067  0.574102 1.00467  0.209552    0.0951258   0.116934    47  PRO   A HA   
2322 H HB2  . PRO   B 35  ? 1.18586  0.530548 0.89007  0.176605    0.0886326   0.0728141   47  PRO   A HB2  
2323 H HB3  . PRO   B 35  ? 1.23031  0.521124 0.9206   0.171434    0.107017    0.0744218   47  PRO   A HB3  
2324 H HG2  . PRO   B 35  ? 1.13637  0.495876 0.792076 0.155543    0.0685307   0.0814146   47  PRO   A HG2  
2325 H HG3  . PRO   B 35  ? 1.16654  0.482056 0.81381  0.145205    0.0904226   0.0759187   47  PRO   A HG3  
2326 H HD2  . PRO   B 35  ? 1.18831  0.521259 0.811404 0.167781    0.0552187   0.121002    47  PRO   A HD2  
2327 H HD3  . PRO   B 35  ? 1.22137  0.507748 0.845376 0.163158    0.0803788   0.118778    47  PRO   A HD3  
2328 N N    . MET   B 36  ? 1.2538   0.606517 1.02968  0.23841     0.0775805   0.125196    48  MET   A N    
2329 C CA   . MET   B 36  ? 1.19562  0.589985 1.01571  0.253822    0.0732182   0.127199    48  MET   A CA   
2330 C C    . MET   B 36  ? 1.17416  0.583033 0.997455 0.239955    0.0889043   0.0945544   48  MET   A C    
2331 O O    . MET   B 36  ? 1.0768   0.454103 0.876444 0.224562    0.108273    0.0706374   48  MET   A O    
2332 C CB   . MET   B 36  ? 1.32249  0.697697 1.18534  0.283916    0.0903282   0.141723    48  MET   A CB   
2333 C CG   . MET   B 36  ? 1.33511  0.692036 1.20553  0.305015    0.0791766   0.178573    48  MET   A CG   
2334 S SD   . MET   B 36  ? 1.35726  0.773771 1.24876  0.316535    0.036032    0.214992    48  MET   A SD   
2335 C CE   . MET   B 36  ? 1.29915  0.703457 1.11896  0.291403    0.0112193   0.220915    48  MET   A CE   
2336 H H    . MET   B 36  ? 1.2939   0.612217 1.07035  0.244236    0.0918607   0.127602    48  MET   A H    
2337 H HA   . MET   B 36  ? 1.2049   0.630401 1.02686  0.25397     0.0508844   0.140108    48  MET   A HA   
2338 H HB2  . MET   B 36  ? 1.31084  0.652583 1.16798  0.281553    0.113262    0.125339    48  MET   A HB2  
2339 H HB3  . MET   B 36  ? 1.2795   0.686767 1.1746   0.293292    0.0891785   0.142414    48  MET   A HB3  
2340 H HG2  . MET   B 36  ? 1.36238  0.690261 1.19899  0.294515    0.079265    0.179701    48  MET   A HG2  
2341 H HG3  . MET   B 36  ? 1.37594  0.712033 1.27181  0.322895    0.0967469   0.182725    48  MET   A HG3  
2342 H HE1  . MET   B 36  ? 1.31943  0.746798 1.13978  0.295729    -0.0132545  0.241037    48  MET   A HE1  
2343 H HE2  . MET   B 36  ? 1.28385  0.697081 1.08402  0.272807    0.0118823   0.200111    48  MET   A HE2  
2344 H HE3  . MET   B 36  ? 1.34153  0.706375 1.14135  0.292112    0.0225881   0.225276    48  MET   A HE3  
2345 N N    . ILE   B 37  ? 1.11745  0.576243 0.969054 0.243144    0.0789397   0.094393    49  ILE   A N    
2346 C CA   . ILE   B 37  ? 1.10328  0.575407 0.961303 0.234444    0.096604    0.0677335   49  ILE   A CA   
2347 C C    . ILE   B 37  ? 1.08371  0.515648 0.953518 0.247513    0.131068    0.0545774   49  ILE   A C    
2348 O O    . ILE   B 37  ? 1.02898  0.450991 0.933923 0.273792    0.141443    0.0705177   49  ILE   A O    
2349 C CB   . ILE   B 37  ? 1.12768  0.657986 1.02302  0.239308    0.0843112   0.0745131   49  ILE   A CB   
2350 C CG1  . ILE   B 37  ? 1.14014  0.701226 1.01302  0.219555    0.0536083   0.0783616   49  ILE   A CG1  
2351 C CG2  . ILE   B 37  ? 1.08757  0.627596 0.995612 0.237179    0.109705    0.0513503   49  ILE   A CG2  
2352 C CD1  . ILE   B 37  ? 1.11486  0.73054  1.02753  0.223746    0.0352541   0.0919574   49  ILE   A CD1  
2353 H H    . ILE   B 37  ? 1.12047  0.604712 0.986329 0.249697    0.0609254   0.111409    49  ILE   A H    
2354 H HA   . ILE   B 37  ? 1.08168  0.54893  0.909876 0.215604    0.0949041   0.0537169   49  ILE   A HA   
2355 H HB   . ILE   B 37  ? 1.1318   0.673104 1.05874  0.257177    0.0800651   0.0931604   49  ILE   A HB   
2356 H HG12 . ILE   B 37  ? 1.11261  0.669545 0.961765 0.20375     0.058585    0.0609745   49  ILE   A HG12 
2357 H HG13 . ILE   B 37  ? 1.13797  0.685313 0.991945 0.218631    0.0410246   0.0893994   49  ILE   A HG13 
2358 H HG21 . ILE   B 37  ? 1.07702  0.654822 1.00872  0.238265    0.101914    0.0567992   49  ILE   A HG21 
2359 H HG22 . ILE   B 37  ? 1.08799  0.615489 0.964345 0.219999    0.113768    0.0337199   49  ILE   A HG22 
2360 H HG23 . ILE   B 37  ? 1.12297  0.643242 1.04639  0.251656    0.130117    0.049318    49  ILE   A HG23 
2361 H HD11 . ILE   B 37  ? 1.13145  0.755447 1.07209  0.239808    0.0293167   0.110576    49  ILE   A HD11 
2362 H HD12 . ILE   B 37  ? 1.10107  0.728569 0.994298 0.210287    0.0159005   0.0934467   49  ILE   A HD12 
2363 H HD13 . ILE   B 37  ? 1.10349  0.734191 1.0332   0.223115    0.0485426   0.0812979   49  ILE   A HD13 
2364 N N    . GLY   B 38  ? 1.04946  0.457793 0.889163 0.228919    0.14885     0.0251313   50  GLY   A N    
2365 C CA   . GLY   B 38  ? 1.06516  0.430714 0.906389 0.237074    0.182417    0.00690348  50  GLY   A CA   
2366 C C    . GLY   B 38  ? 1.13281  0.43801  0.939544 0.224675    0.192052    -0.00260436 50  GLY   A C    
2367 O O    . GLY   B 38  ? 1.19522  0.458461 0.985404 0.21893     0.217084    -0.0264232  50  GLY   A O    
2368 H H    . GLY   B 38  ? 1.03002  0.447798 0.8468   0.21073     0.139936    0.0161517   50  GLY   A H    
2369 H HA2  . GLY   B 38  ? 1.07021  0.444926 0.903395 0.22808     0.191487    -0.011358   50  GLY   A HA2  
2370 H HA3  . GLY   B 38  ? 1.09616  0.462278 0.969405 0.259502    0.191007    0.0189937   50  GLY   A HA3  
2371 N N    . ASP   B 39  ? 1.14085  0.441797 0.933763 0.217907    0.17219     0.015153    51  ASP   A N    
2372 C CA   . ASP   B 39  ? 1.14299  0.392274 0.90589  0.20242     0.180053    0.00868987  51  ASP   A CA   
2373 C C    . ASP   B 39  ? 1.11261  0.360356 0.841873 0.169785    0.181858    -0.0204851  51  ASP   A C    
2374 O O    . ASP   B 39  ? 1.06737  0.359834 0.790231 0.157463    0.166675    -0.0257497  51  ASP   A O    
2375 C CB   . ASP   B 39  ? 1.16064  0.411164 0.913862 0.201296    0.159762    0.035338    51  ASP   A CB   
2376 C CG   . ASP   B 39  ? 1.15965  0.400888 0.937512 0.230428    0.155648    0.0680038   51  ASP   A CG   
2377 O OD1  . ASP   B 39  ? 1.18175  0.404613 0.98911  0.253819    0.17325     0.0711224   51  ASP   A OD1  
2378 O OD2  . ASP   B 39  ? 1.15824  0.408625 0.923035 0.229525    0.135453    0.0910965   51  ASP   A OD2  
2379 H H    . ASP   B 39  ? 1.10703  0.436933 0.908588 0.222228    0.154045    0.0316569   51  ASP   A H    
2380 H HA   . ASP   B 39  ? 1.19104  0.403708 0.961138 0.213209    0.198223    0.00653321  51  ASP   A HA   
2381 H HB2  . ASP   B 39  ? 1.11209  0.398311 0.859673 0.193886    0.142735    0.038149    51  ASP   A HB2  
2382 H HB3  . ASP   B 39  ? 1.16466  0.386361 0.897655 0.186723    0.165223    0.0294037   51  ASP   A HB3  
2383 N N    . LYS   B 40  ? 1.1684   0.363235 0.877269 0.15537     0.199293    -0.0376343  52  LYS   A N    
2384 C CA   . LYS   B 40  ? 1.16294  0.355663 0.841182 0.12129     0.195686    -0.0595512  52  LYS   A CA   
2385 C C    . LYS   B 40  ? 1.17216  0.37156  0.842491 0.108284    0.179257    -0.041547   52  LYS   A C    
2386 O O    . LYS   B 40  ? 1.27841  0.448628 0.953232 0.117653    0.182399    -0.0224297  52  LYS   A O    
2387 C CB   . LYS   B 40  ? 1.17024  0.308956 0.826513 0.104294    0.217008    -0.0881265  52  LYS   A CB   
2388 H H    . LYS   B 40  ? 1.20379  0.363454 0.919312 0.166629    0.212992    -0.0348526  52  LYS   A H    
2389 H HA   . LYS   B 40  ? 1.12562  0.353588 0.801721 0.11614     0.187992    -0.0667435  52  LYS   A HA   
2392 N N    . VAL   B 41  ? 1.1124   0.351113 0.771469 0.0886162   0.163188    -0.0457112  53  VAL   A N    
2393 C CA   . VAL   B 41  ? 1.05813  0.314269 0.711918 0.0804979   0.148893    -0.0274681  53  VAL   A CA   
2394 C C    . VAL   B 41  ? 1.06006  0.318793 0.700449 0.0487427   0.147453    -0.0420354  53  VAL   A C    
2395 O O    . VAL   B 41  ? 1.02944  0.30725  0.663488 0.0346652   0.144552    -0.0618876  53  VAL   A O    
2396 C CB   . VAL   B 41  ? 1.06478  0.372146 0.723485 0.0911255   0.13024     -0.0152805  53  VAL   A CB   
2397 C CG1  . VAL   B 41  ? 1.087    0.409132 0.733745 0.0813864   0.119329    -0.00126019 53  VAL   A CG1  
2398 C CG2  . VAL   B 41  ? 1.10272  0.412254 0.77858  0.119783    0.12701     0.00337624  53  VAL   A CG2  
2399 H H    . VAL   B 41  ? 1.09644  0.351195 0.750275 0.0804613   0.162347    -0.0603711  53  VAL   A H    
2400 H HA   . VAL   B 41  ? 1.09768  0.329686 0.753236 0.0880368   0.152873    -0.0134566  53  VAL   A HA   
2401 H HB   . VAL   B 41  ? 1.04667  0.375588 0.70517  0.0853063   0.127833    -0.0283077  53  VAL   A HB   
2402 H HG11 . VAL   B 41  ? 1.09674  0.394444 0.740376 0.083895    0.124066    0.0102219   53  VAL   A HG11 
2403 H HG12 . VAL   B 41  ? 1.06267  0.393587 0.704359 0.0643489   0.119167    -0.0113113  53  VAL   A HG12 
2404 H HG13 . VAL   B 41  ? 1.04983  0.39644  0.696741 0.0895597   0.108396    0.00693857  53  VAL   A HG13 
2405 H HG21 . VAL   B 41  ? 1.06511  0.405277 0.742241 0.123453    0.113662    0.0105874   53  VAL   A HG21 
2406 H HG22 . VAL   B 41  ? 1.10379  0.407344 0.791152 0.12813     0.135961    -0.00479962 53  VAL   A HG22 
2407 H HG23 . VAL   B 41  ? 1.11661  0.402859 0.791066 0.125955    0.129393    0.0171335   53  VAL   A HG23 
2408 N N    . TYR   B 42  ? 1.04533  0.287614 0.68279  0.0371394   0.14904     -0.0299913  54  TYR   A N    
2409 C CA   . TYR   B 42  ? 1.04128  0.290782 0.675036 0.0065249   0.147076    -0.0395825  54  TYR   A CA   
2410 C C    . TYR   B 42  ? 1.00127  0.284868 0.6377   0.00493854  0.137957    -0.0198307  54  TYR   A C    
2411 O O    . TYR   B 42  ? 0.987096 0.256292 0.621032 0.0175532   0.141633    0.00161395  54  TYR   A O    
2412 C CB   . TYR   B 42  ? 1.10971  0.306661 0.741907 -0.00978889 0.161454    -0.0437179  54  TYR   A CB   
2413 C CG   . TYR   B 42  ? 1.18126  0.327659 0.806839 -0.0057176  0.176419    -0.0623558  54  TYR   A CG   
2414 C CD1  . TYR   B 42  ? 1.20765  0.327618 0.838696 0.0249986   0.18655     -0.0526631  54  TYR   A CD1  
2415 C CD2  . TYR   B 42  ? 1.29488  0.419104 0.908127 -0.0329322  0.180659    -0.0894795  54  TYR   A CD2  
2416 C CE1  . TYR   B 42  ? 1.32995  0.399698 0.957007 0.0313612   0.20492     -0.0693306  54  TYR   A CE1  
2417 C CE2  . TYR   B 42  ? 1.33135  0.400571 0.932434 -0.0299977  0.19814     -0.109183   54  TYR   A CE2  
2418 C CZ   . TYR   B 42  ? 1.37155  0.412836 0.980813 0.00398698  0.212362    -0.0992045  54  TYR   A CZ   
2419 O OH   . TYR   B 42  ? 1.5417   0.527264 1.14033  0.00931437  0.233389    -0.119284   54  TYR   A OH   
2420 H H    . TYR   B 42  ? 1.06401  0.291845 0.703144 0.0484336   0.151326    -0.0141238  54  TYR   A H    
2421 H HA   . TYR   B 42  ? 1.03263  0.299113 0.663255 -0.00295722 0.142612    -0.0553482  54  TYR   A HA   
2422 H HB2  . TYR   B 42  ? 1.12089  0.30464  0.755714 -0.00245147 0.165343    -0.0257417  54  TYR   A HB2  
2423 H HB3  . TYR   B 42  ? 1.11052  0.317516 0.743381 -0.032377   0.158       -0.0506263  54  TYR   A HB3  
2424 H HD1  . TYR   B 42  ? 1.20285  0.337931 0.840624 0.0421853   0.181333    -0.0338264  54  TYR   A HD1  
2425 H HD2  . TYR   B 42  ? 1.25734  0.402092 0.869628 -0.0545821  0.171841    -0.0945025  54  TYR   A HD2  
2426 H HE1  . TYR   B 42  ? 1.32676  0.381543 0.962464 0.054361    0.212287    -0.0603699  54  TYR   A HE1  
2427 H HE2  . TYR   B 42  ? 1.36896  0.420792 0.956205 -0.0506031  0.200232    -0.12925    54  TYR   A HE2  
2429 N N    . VAL   B 43  ? 1.00911  0.334649 0.648683 -0.00982885 0.127677    -0.0261118  55  VAL   A N    
2430 C CA   . VAL   B 43  ? 0.986515 0.342982 0.629114 -0.00894168 0.122825    -0.00890333 55  VAL   A CA   
2431 C C    . VAL   B 43  ? 0.95605  0.338868 0.612381 -0.035081   0.120059    -0.0133896  55  VAL   A C    
2432 O O    . VAL   B 43  ? 1.05033  0.435021 0.709865 -0.0544949  0.115844    -0.0313176  55  VAL   A O    
2433 C CB   . VAL   B 43  ? 0.997657 0.387128 0.634551 0.00918204  0.111344    -0.00514396 55  VAL   A CB   
2434 C CG1  . VAL   B 43  ? 0.987278 0.361931 0.617488 0.0332742   0.109391    -0.00038806 55  VAL   A CG1  
2435 C CG2  . VAL   B 43  ? 1.04288  0.466288 0.684377 -0.00060638 0.101464    -0.021464   55  VAL   A CG2  
2436 H H    . VAL   B 43  ? 0.996415 0.330189 0.635334 -0.019892   0.124464    -0.0408325  55  VAL   A H    
2437 H HA   . VAL   B 43  ? 1.00634  0.344165 0.646089 -0.00360685 0.129526    0.00460452  55  VAL   A HA   
2438 H HB   . VAL   B 43  ? 0.98724  0.387832 0.622093 0.0110671   0.111211    0.00649198  55  VAL   A HB   
2439 H HG11 . VAL   B 43  ? 1.00101  0.365932 0.634777 0.033618    0.111799    -0.0117151  55  VAL   A HG11 
2440 H HG12 . VAL   B 43  ? 1.01318  0.366321 0.639047 0.03998     0.114258    0.0118339   55  VAL   A HG12 
2441 H HG13 . VAL   B 43  ? 0.969249 0.365722 0.596504 0.0413992   0.101042    0.00255741  55  VAL   A HG13 
2442 H HG21 . VAL   B 43  ? 0.996758 0.435468 0.634922 0.0111155   0.0953579   -0.0198575  55  VAL   A HG21 
2443 H HG22 . VAL   B 43  ? 1.00832  0.449895 0.65653  -0.0125343  0.0995376   -0.0198251  55  VAL   A HG22 
2444 H HG23 . VAL   B 43  ? 1.03341  0.444386 0.673988 -0.00681002 0.10348     -0.0343536  55  VAL   A HG23 
2445 N N    . HIS   B 44  ? 0.898938 0.303306 0.562991 -0.0354696  0.122506    0.0037564   56  HIS   A N    
2446 C CA   . HIS   B 44  ? 0.860837 0.30667  0.544822 -0.0518486  0.117527    0.00473579  56  HIS   A CA   
2447 C C    . HIS   B 44  ? 0.855568 0.331673 0.533434 -0.0327733  0.112009    0.0120229   56  HIS   A C    
2448 O O    . HIS   B 44  ? 0.834052 0.294502 0.492364 -0.0123536  0.11465     0.0199699   56  HIS   A O    
2449 C CB   . HIS   B 44  ? 0.918668 0.363969 0.622088 -0.0668933  0.129892    0.0197622   56  HIS   A CB   
2450 C CG   . HIS   B 44  ? 1.04928  0.486529 0.769439 -0.0974508  0.127752    0.00836918  56  HIS   A CG   
2451 N ND1  . HIS   B 44  ? 1.05574  0.519601 0.7842   -0.11614    0.111608    -0.00808038 56  HIS   A ND1  
2452 C CD2  . HIS   B 44  ? 1.04766  0.450646 0.773895 -0.113946   0.138461    0.0106725   56  HIS   A CD2  
2453 C CE1  . HIS   B 44  ? 1.09161  0.538659 0.829553 -0.144899   0.111095    -0.0167357  56  HIS   A CE1  
2454 N NE2  . HIS   B 44  ? 1.07756  0.486996 0.816489 -0.144407   0.128065    -0.00575719 56  HIS   A NE2  
2455 H H    . HIS   B 44  ? 0.912711 0.304972 0.569201 -0.0241119  0.12823     0.0161507   56  HIS   A H    
2456 H HA   . HIS   B 44  ? 0.877317 0.332139 0.565505 -0.0643498  0.10969     -0.00848594 56  HIS   A HA   
2457 H HB2  . HIS   B 44  ? 0.947829 0.367361 0.640696 -0.0576782  0.139796    0.0295792   56  HIS   A HB2  
2458 H HB3  . HIS   B 44  ? 0.909664 0.385131 0.625059 -0.0662287  0.129806    0.0278053   56  HIS   A HB3  
2460 H HD2  . HIS   B 44  ? 1.07884  0.457851 0.800713 -0.107638   0.15034     0.0220821   56  HIS   A HD2  
2461 H HE1  . HIS   B 44  ? 1.08674  0.544873 0.827958 -0.163386   0.100128    -0.0283997  56  HIS   A HE1  
2463 N N    . TYR   B 45  ? 0.827115 0.344438 0.520794 -0.0399849  0.103578    0.0103146   57  TYR   A N    
2464 C CA   . TYR   B 45  ? 0.80722  0.346723 0.494369 -0.0222329  0.100303    0.0166244   57  TYR   A CA   
2465 C C    . TYR   B 45  ? 0.794053 0.376411 0.508724 -0.0307465  0.0982103   0.0236159   57  TYR   A C    
2466 O O    . TYR   B 45  ? 0.780746 0.384806 0.519092 -0.0516409  0.0912801   0.020279    57  TYR   A O    
2467 C CB   . TYR   B 45  ? 0.775948 0.312516 0.444863 -0.0106815  0.0887577   0.00437682  57  TYR   A CB   
2468 C CG   . TYR   B 45  ? 0.783978 0.345755 0.461241 -0.0233567  0.076426    -0.00862038 57  TYR   A CG   
2469 C CD1  . TYR   B 45  ? 0.713251 0.310978 0.4001   -0.022724   0.0684608   -0.00479604 57  TYR   A CD1  
2470 C CD2  . TYR   B 45  ? 0.797141 0.342887 0.469221 -0.0360615  0.0738902   -0.0243271  57  TYR   A CD2  
2471 C CE1  . TYR   B 45  ? 0.738449 0.358185 0.428993 -0.0356527  0.0562067   -0.0141487  57  TYR   A CE1  
2472 C CE2  . TYR   B 45  ? 0.775341 0.339892 0.446004 -0.0493328  0.0630726   -0.0368546  57  TYR   A CE2  
2473 C CZ   . TYR   B 45  ? 0.793745 0.396931 0.473109 -0.0494722  0.0530577   -0.0307099  57  TYR   A CZ   
2474 O OH   . TYR   B 45  ? 0.796768 0.417544 0.470148 -0.062806   0.0413832   -0.0408206  57  TYR   A OH   
2475 H H    . TYR   B 45  ? 0.830732 0.361063 0.53865  -0.0560441  0.0994112   0.0056916   57  TYR   A H    
2476 H HA   . TYR   B 45  ? 0.812404 0.338121 0.489123 -0.0116214  0.108806    0.0262981   57  TYR   A HA   
2477 H HB2  . TYR   B 45  ? 0.773462 0.315027 0.433996 0.00179225  0.0880298   0.00964881  57  TYR   A HB2  
2478 H HB3  . TYR   B 45  ? 0.800215 0.312198 0.459215 -0.00703098 0.0907404   0.00070889  57  TYR   A HB3  
2479 H HD1  . TYR   B 45  ? 0.721377 0.326949 0.411129 -0.0138738  0.0720802   0.00485151  57  TYR   A HD1  
2480 H HD2  . TYR   B 45  ? 0.814222 0.332896 0.480854 -0.0353144  0.0804557   -0.0265405  57  TYR   A HD2  
2481 H HE1  . TYR   B 45  ? 0.723595 0.366812 0.420877 -0.0341968  0.0506089   -0.00944258 57  TYR   A HE1  
2482 H HE2  . TYR   B 45  ? 0.809517 0.358677 0.471477 -0.0580792  0.0630881   -0.0490776  57  TYR   A HE2  
2484 N N    . LYS   B 46  ? 0.781906 0.375223 0.492751 -0.0141602  0.10385     0.0339563   58  LYS   A N    
2485 C CA   . LYS   B 46  ? 0.747547 0.379862 0.482071 -0.0134235  0.101775    0.0411933   58  LYS   A CA   
2486 C C    . LYS   B 46  ? 0.755893 0.385767 0.467876 0.00427209  0.0955763   0.0370985   58  LYS   A C    
2487 O O    . LYS   B 46  ? 0.753518 0.35731  0.43756  0.0189087   0.101485    0.0378929   58  LYS   A O    
2488 C CB   . LYS   B 46  ? 0.795067 0.438858 0.55058  -0.0100885  0.121019    0.059036    58  LYS   A CB   
2489 C CG   . LYS   B 46  ? 0.816222 0.454904 0.590904 -0.0274846  0.130258    0.0648502   58  LYS   A CG   
2490 C CD   . LYS   B 46  ? 0.84469  0.490407 0.637285 -0.0225305  0.154576    0.0839992   58  LYS   A CD   
2491 C CE   . LYS   B 46  ? 0.900228 0.530214 0.704112 -0.0405868  0.163813    0.088866    58  LYS   A CE   
2492 N NZ   . LYS   B 46  ? 0.906037 0.554116 0.739776 -0.0408973  0.187846    0.109172    58  LYS   A NZ   
2493 H H    . LYS   B 46  ? 0.786368 0.359987 0.477844 -0.00239475 0.109478    0.0369014   58  LYS   A H    
2494 H HA   . LYS   B 46  ? 0.755529 0.407603 0.506683 -0.0268233  0.0916489   0.037126    58  LYS   A HA   
2495 H HB2  . LYS   B 46  ? 0.793722 0.418829 0.527776 0.00412865  0.130684    0.0623688   58  LYS   A HB2  
2496 H HB3  . LYS   B 46  ? 0.772551 0.445762 0.550894 -0.0102772  0.119085    0.0646688   58  LYS   A HB3  
2497 H HG2  . LYS   B 46  ? 0.81435  0.473792 0.611563 -0.0434584  0.120087    0.0618751   58  LYS   A HG2  
2498 H HG3  . LYS   B 46  ? 0.833752 0.442282 0.586815 -0.0277929  0.130565    0.0590202   58  LYS   A HG3  
2499 H HD2  . LYS   B 46  ? 0.855789 0.481687 0.622032 -0.00645227 0.164468    0.0864633   58  LYS   A HD2  
2500 H HD3  . LYS   B 46  ? 0.835526 0.514634 0.65855  -0.0241684  0.155135    0.0913198   58  LYS   A HD3  
2501 H HE2  . LYS   B 46  ? 0.888695 0.530018 0.710183 -0.0580487  0.151432    0.0824811   58  LYS   A HE2  
2502 H HE3  . LYS   B 46  ? 0.907777 0.503073 0.681695 -0.0352592  0.16682     0.085481    58  LYS   A HE3  
2503 H HZ1  . LYS   B 46  ? 0.892998 0.575912 0.75875  -0.0447379  0.185009    0.113992    58  LYS   A HZ1  
2504 H HZ2  . LYS   B 46  ? 0.916    0.549795 0.72852  -0.0249649  0.200832    0.114081    58  LYS   A HZ2  
2505 H HZ3  . LYS   B 46  ? 0.925093 0.563661 0.767013 -0.0532832  0.193555    0.112863    58  LYS   A HZ3  
2506 N N    . GLY   B 47  ? 0.784997 0.441324 0.507287 0.00084567  0.0818375   0.0329086   59  GLY   A N    
2507 C CA   . GLY   B 47  ? 0.678703 0.332965 0.38284  0.0144128   0.0755205   0.0293645   59  GLY   A CA   
2508 C C    . GLY   B 47  ? 0.703786 0.389799 0.430182 0.0182052   0.0739846   0.0395803   59  GLY   A C    
2509 O O    . GLY   B 47  ? 0.677242 0.395226 0.435323 0.00735638  0.0703539   0.0472396   59  GLY   A O    
2510 H H    . GLY   B 47  ? 0.746306 0.422223 0.486829 -0.0113241  0.0757265   0.0328871   59  GLY   A H    
2511 H HA2  . GLY   B 47  ? 0.715303 0.348892 0.401121 0.0251284   0.082045    0.0303903   59  GLY   A HA2  
2512 H HA3  . GLY   B 47  ? 0.703468 0.355102 0.398912 0.0102655   0.0660046   0.0198988   59  GLY   A HA3  
2513 N N    . LYS   B 48  ? 0.708329 0.384611 0.41849  0.03326     0.0753701   0.040324    60  LYS   A N    
2514 C CA   . LYS   B 48  ? 0.743883 0.444718 0.474314 0.0395185   0.0749876   0.0509963   60  LYS   A CA   
2515 C C    . LYS   B 48  ? 0.726098 0.408442 0.43199  0.050957    0.0720671   0.0465848   60  LYS   A C    
2516 O O    . LYS   B 48  ? 0.691131 0.344138 0.367025 0.0542517   0.0716056   0.0368749   60  LYS   A O    
2517 C CB   . LYS   B 48  ? 0.756044 0.465835 0.510003 0.0483074   0.0939072   0.0660338   60  LYS   A CB   
2518 C CG   . LYS   B 48  ? 0.84163  0.510746 0.562193 0.0631946   0.112185    0.0636163   60  LYS   A CG   
2519 C CD   . LYS   B 48  ? 0.896197 0.567415 0.633103 0.074746    0.137667    0.0774782   60  LYS   A CD   
2520 C CE   . LYS   B 48  ? 0.970472 0.650871 0.722594 0.089859    0.145741    0.0865561   60  LYS   A CE   
2521 N NZ   . LYS   B 48  ? 1.21314  0.874915 0.960326 0.106502    0.176203    0.0942477   60  LYS   A NZ   
2522 H H    . LYS   B 48  ? 0.721033 0.37518  0.408647 0.0390912   0.0761114   0.0348917   60  LYS   A H    
2523 H HA   . LYS   B 48  ? 0.722398 0.446755 0.468391 0.0296686   0.0641055   0.0519633   60  LYS   A HA   
2524 H HB2  . LYS   B 48  ? 0.763331 0.491433 0.535508 0.0537417   0.0938079   0.0747596   60  LYS   A HB2  
2525 H HB3  . LYS   B 48  ? 0.768199 0.491154 0.540431 0.0389533   0.095387    0.0694441   60  LYS   A HB3  
2526 H HG2  . LYS   B 48  ? 0.839612 0.492011 0.542897 0.0582514   0.110782    0.0570618   60  LYS   A HG2  
2527 H HG3  . LYS   B 48  ? 0.837094 0.492056 0.538902 0.0700969   0.109028    0.0591388   60  LYS   A HG3  
2528 H HD2  . LYS   B 48  ? 0.898819 0.592802 0.664202 0.066681    0.139545    0.0845563   60  LYS   A HD2  
2529 H HD3  . LYS   B 48  ? 0.925719 0.568236 0.634712 0.080075    0.14837     0.0741214   60  LYS   A HD3  
2530 H HE2  . LYS   B 48  ? 0.992181 0.65655  0.722494 0.0931801   0.137996    0.0792768   60  LYS   A HE2  
2531 H HE3  . LYS   B 48  ? 0.979346 0.693533 0.766796 0.0858049   0.139339    0.0955096   60  LYS   A HE3  
2532 H HZ1  . LYS   B 48  ? 1.15555  0.784312 0.865233 0.10992     0.180879    0.0857555   60  LYS   A HZ1  
2533 H HZ2  . LYS   B 48  ? 1.1383   0.815085 0.906394 0.103114    0.18482     0.101716    60  LYS   A HZ2  
2534 H HZ3  . LYS   B 48  ? 1.14201  0.809348 0.902202 0.116833    0.182712    0.1005      60  LYS   A HZ3  
2535 N N    . LEU   B 49  ? 0.720767 0.424936 0.443375 0.0538312   0.066521    0.0549939   61  LEU   A N    
2536 C CA   . LEU   B 49  ? 0.745678 0.43285  0.452211 0.0646823   0.0669976   0.0549351   61  LEU   A CA   
2537 C C    . LEU   B 49  ? 0.718462 0.383635 0.420812 0.080792    0.0880496   0.0609961   61  LEU   A C    
2538 O O    . LEU   B 49  ? 0.772918 0.454929 0.501823 0.0848898   0.100592    0.0723362   61  LEU   A O    
2539 C CB   . LEU   B 49  ? 0.684717 0.400248 0.412325 0.0641298   0.0573764   0.0661837   61  LEU   A CB   
2540 C CG   . LEU   B 49  ? 0.727897 0.46639  0.455504 0.0478928   0.0385496   0.0617368   61  LEU   A CG   
2541 C CD1  . LEU   B 49  ? 0.684026 0.449065 0.428038 0.0486654   0.0292975   0.0767798   61  LEU   A CD1  
2542 C CD2  . LEU   B 49  ? 0.715999 0.43307  0.413284 0.0418678   0.0326309   0.044831    61  LEU   A CD2  
2543 H H    . LEU   B 49  ? 0.717891 0.447875 0.462802 0.0480136   0.0617139   0.061714    61  LEU   A H    
2544 H HA   . LEU   B 49  ? 0.723697 0.39378  0.408413 0.0622276   0.0617103   0.0448978   61  LEU   A HA   
2545 H HB2  . LEU   B 49  ? 0.708902 0.442819 0.461206 0.0679859   0.0623752   0.0779049   61  LEU   A HB2  
2546 H HB3  . LEU   B 49  ? 0.715943 0.415794 0.432902 0.0717287   0.0598007   0.0668092   61  LEU   A HB3  
2547 H HG   . LEU   B 49  ? 0.704058 0.456719 0.44242  0.0392822   0.0360229   0.0610307   61  LEU   A HG   
2548 H HD11 . LEU   B 49  ? 0.69664  0.480872 0.46527  0.0519149   0.0314198   0.08888     61  LEU   A HD11 
2549 H HD12 . LEU   B 49  ? 0.693364 0.471014 0.431671 0.0374345   0.0179255   0.0732129   61  LEU   A HD12 
2550 H HD13 . LEU   B 49  ? 0.701115 0.450937 0.436574 0.0569962   0.0328137   0.0787823   61  LEU   A HD13 
2551 H HD21 . LEU   B 49  ? 0.720946 0.424997 0.410553 0.0407064   0.0363562   0.0372004   61  LEU   A HD21 
2552 H HD22 . LEU   B 49  ? 0.72271  0.42507  0.409872 0.0483133   0.0345802   0.0448208   61  LEU   A HD22 
2553 H HD23 . LEU   B 49  ? 0.715272 0.446509 0.411853 0.0327146   0.0236892   0.0425865   61  LEU   A HD23 
2554 N N    . SER   B 50  ? 0.833945 0.461958 0.503327 0.088714    0.092737    0.053456    62  SER   A N    
2555 C CA   . SER   B 50  ? 0.906935 0.507389 0.564505 0.104404    0.115184    0.057194    62  SER   A CA   
2556 C C    . SER   B 50  ? 0.87012  0.488769 0.561796 0.116864    0.125755    0.0732913   62  SER   A C    
2557 O O    . SER   B 50  ? 0.925348 0.535899 0.625115 0.131032    0.149281    0.0811078   62  SER   A O    
2558 C CB   . SER   B 50  ? 0.857287 0.411391 0.467497 0.106533    0.114841    0.0439145   62  SER   A CB   
2559 O OG   . SER   B 50  ? 1.02313  0.572371 0.613885 0.0958469   0.103214    0.0343904   62  SER   A OG   
2560 H H    . SER   B 50  ? 0.813011 0.431648 0.46642  0.0840492   0.0828253   0.0457358   62  SER   A H    
2561 H HA   . SER   B 50  ? 0.881296 0.481669 0.539946 0.104957    0.124633    0.0586641   62  SER   A HA   
2562 H HB2  . SER   B 50  ? 0.906643 0.4589   0.515822 0.104787    0.106185    0.04239     62  SER   A HB2  
2563 H HB3  . SER   B 50  ? 0.937281 0.468179 0.532506 0.115832    0.13074     0.044093    62  SER   A HB3  
2565 N N    . ASN   B 51  ? 0.889362 0.534198 0.603474 0.113306    0.110471    0.0809227   63  ASN   A N    
2566 C CA   . ASN   B 51  ? 0.802803 0.465671 0.552326 0.127641    0.119918    0.100286    63  ASN   A CA   
2567 C C    . ASN   B 51  ? 0.942359 0.653978 0.742382 0.127892    0.123479    0.1176      63  ASN   A C    
2568 O O    . ASN   B 51  ? 0.788423 0.523787 0.627138 0.140758    0.129839    0.137659    63  ASN   A O    
2569 C CB   . ASN   B 51  ? 0.824306 0.49655  0.578933 0.125175    0.103776    0.106544    63  ASN   A CB   
2570 C CG   . ASN   B 51  ? 0.818931 0.536722 0.592114 0.107717    0.0798367   0.110663    63  ASN   A CG   
2571 O OD1  . ASN   B 51  ? 0.736748 0.481675 0.5262   0.0977619   0.0753893   0.11046     63  ASN   A OD1  
2572 N ND2  . ASN   B 51  ? 0.830511 0.552852 0.596695 0.102057    0.0650027   0.113199    63  ASN   A ND2  
2573 H H    . ASN   B 51  ? 0.843318 0.494127 0.550636 0.103141    0.0954942   0.0753158   63  ASN   A H    
2574 H HA   . ASN   B 51  ? 0.875297 0.509482 0.612486 0.140161    0.136973    0.099406    63  ASN   A HA   
2575 H HB2  . ASN   B 51  ? 0.833903 0.50884  0.607386 0.137769    0.112394    0.119644    63  ASN   A HB2  
2576 H HB3  . ASN   B 51  ? 0.831016 0.47492  0.556469 0.122288    0.100894    0.0954223   63  ASN   A HB3  
2577 H HD21 . ASN   B 51  ? 0.812826 0.55715  0.5823   0.0911223   0.051646    0.113566    63  ASN   A HD21 
2578 H HD22 . ASN   B 51  ? 0.837763 0.539676 0.594518 0.108696    0.0691785   0.11447     63  ASN   A HD22 
2579 N N    . GLY   B 52  ? 0.875674 0.603602 0.67972  0.113448    0.118867    0.112002    64  GLY   A N    
2580 C CA   . GLY   B 52  ? 0.882598 0.655751 0.735382 0.109144    0.121437    0.127438    64  GLY   A CA   
2581 C C    . GLY   B 52  ? 0.902425 0.728555 0.79389  0.0973428   0.0968602   0.141473    64  GLY   A C    
2582 O O    . GLY   B 52  ? 0.915478 0.785843 0.855454 0.0936763   0.0960901   0.158355    64  GLY   A O    
2583 H H    . GLY   B 52  ? 0.889447 0.599382 0.666131 0.105387    0.113509    0.0986227   64  GLY   A H    
2584 H HA2  . GLY   B 52  ? 0.884546 0.653854 0.728465 0.0991632   0.121487    0.119542    64  GLY   A HA2  
2585 H HA3  . GLY   B 52  ? 0.900518 0.673123 0.770337 0.123518    0.140538    0.137485    64  GLY   A HA3  
2586 N N    . LYS   B 53  ? 0.822685 0.647091 0.693297 0.0898288   0.0759151   0.135989    65  LYS   A N    
2587 C CA   . LYS   B 53  ? 0.752788 0.623762 0.650435 0.0787609   0.0520451   0.150186    65  LYS   A CA   
2588 C C    . LYS   B 53  ? 0.76467  0.647082 0.648326 0.0515225   0.0333464   0.134835    65  LYS   A C    
2589 O O    . LYS   B 53  ? 0.761556 0.682082 0.661668 0.0355484   0.0118269   0.142426    65  LYS   A O    
2590 C CB   . LYS   B 53  ? 0.670522 0.538885 0.560115 0.0873986   0.0429012   0.159862    65  LYS   A CB   
2591 H H    . LYS   B 53  ? 0.826368 0.620928 0.664836 0.0908834   0.0763251   0.123908    65  LYS   A H    
2592 H HA   . LYS   B 53  ? 0.750723 0.650809 0.687057 0.0835039   0.0556943   0.166645    65  LYS   A HA   
2595 N N    . LYS   B 54  ? 0.712459 0.561433 0.565768 0.0455029   0.0412253   0.11406     66  LYS   A N    
2596 C CA   . LYS   B 54  ? 0.721005 0.573852 0.560293 0.0216515   0.0264192   0.0989876   66  LYS   A CA   
2597 C C    . LYS   B 54  ? 0.721815 0.547113 0.549702 0.018878    0.0408127   0.0865267   66  LYS   A C    
2598 O O    . LYS   B 54  ? 0.684763 0.472962 0.487022 0.0319473   0.055358    0.0788341   66  LYS   A O    
2599 C CB   . LYS   B 54  ? 0.684022 0.52773  0.48798  0.0116187   0.00989685  0.0857033   66  LYS   A CB   
2600 H H    . LYS   B 54  ? 0.733401 0.555603 0.573268 0.0561577   0.055605    0.109402    66  LYS   A H    
2601 H HA   . LYS   B 54  ? 0.711889 0.59698  0.577321 0.0116218   0.0168847   0.108305    66  LYS   A HA   
2604 N N    . PHE   B 55  ? 0.720417 0.564335 0.566468 -0.00051474 0.0344772   0.0855778   67  PHE   A N    
2605 C CA   . PHE   B 55  ? 0.809544 0.629174 0.646677 -0.00835329 0.0450888   0.0752426   67  PHE   A CA   
2606 C C    . PHE   B 55  ? 0.798591 0.61555  0.621618 -0.033483   0.0286554   0.0593188   67  PHE   A C    
2607 O O    . PHE   B 55  ? 0.770344 0.616413 0.601881 -0.0496298  0.00896477  0.0604123   67  PHE   A O    
2608 C CB   . PHE   B 55  ? 0.778635 0.623366 0.659772 -0.011575   0.0567546   0.0915445   67  PHE   A CB   
2609 C CG   . PHE   B 55  ? 0.8953   0.748997 0.798225 0.0131103   0.0756717   0.109572    67  PHE   A CG   
2610 C CD1  . PHE   B 55  ? 0.819969 0.711475 0.755044 0.0206729   0.0676362   0.126733    67  PHE   A CD1  
2611 C CD2  . PHE   B 55  ? 0.935775 0.756836 0.823957 0.0294842   0.102678    0.109851    67  PHE   A CD2  
2612 C CE1  . PHE   B 55  ? 0.850592 0.746486 0.808442 0.0453712   0.0889644   0.143502    67  PHE   A CE1  
2613 C CE2  . PHE   B 55  ? 0.967906 0.790606 0.870464 0.0526438   0.123604    0.12382     67  PHE   A CE2  
2614 C CZ   . PHE   B 55  ? 0.888263 0.746579 0.826533 0.0616626   0.117833    0.139945    67  PHE   A CZ   
2615 H H    . PHE   B 55  ? 0.737774 0.610846 0.602783 -0.0104308  0.0220071   0.0925035   67  PHE   A H    
2616 H HA   . PHE   B 55  ? 0.78274  0.571716 0.595776 0.00270601  0.0554685   0.0686338   67  PHE   A HA   
2617 H HB2  . PHE   B 55  ? 0.81123  0.686446 0.716006 -0.0264391  0.0434558   0.0966368   67  PHE   A HB2  
2618 H HB3  . PHE   B 55  ? 0.820846 0.644916 0.692974 -0.0152389  0.0660897   0.0858312   67  PHE   A HB3  
2619 H HD1  . PHE   B 55  ? 0.836287 0.750417 0.778662 0.00896335  0.0485766   0.128004    67  PHE   A HD1  
2620 H HD2  . PHE   B 55  ? 0.940245 0.735858 0.805856 0.0252739   0.107058    0.100453    67  PHE   A HD2  
2621 H HE1  . PHE   B 55  ? 0.847113 0.767017 0.828063 0.0520851   0.0839403   0.156399    67  PHE   A HE1  
2622 H HE2  . PHE   B 55  ? 0.957199 0.754996 0.843742 0.0628532   0.142297    0.122721    67  PHE   A HE2  
2623 H HZ   . PHE   B 55  ? 0.905972 0.763061 0.855674 0.0787181   0.134307    0.149606    67  PHE   A HZ   
2624 N N    . ASP   B 56  ? 0.69774  0.477523 0.496979 -0.0363004  0.0372      0.0452638   68  ASP   A N    
2625 C CA   . ASP   B 56  ? 0.716149 0.479889 0.495491 -0.0561914  0.0272522   0.0271032   68  ASP   A CA   
2626 C C    . ASP   B 56  ? 0.703397 0.433509 0.477386 -0.0577866  0.0422301   0.0224441   68  ASP   A C    
2627 O O    . ASP   B 56  ? 0.698921 0.402783 0.457333 -0.0392161  0.0558734   0.0239466   68  ASP   A O    
2628 C CB   . ASP   B 56  ? 0.757076 0.498115 0.498585 -0.0493877  0.0225932   0.011601    68  ASP   A CB   
2629 C CG   . ASP   B 56  ? 0.845968 0.560028 0.562793 -0.0641777  0.0198578   -0.00895451 68  ASP   A CG   
2630 O OD1  . ASP   B 56  ? 0.782509 0.50716  0.505044 -0.0869518  0.0101647   -0.0137685  68  ASP   A OD1  
2631 O OD2  . ASP   B 56  ? 0.831027 0.514392 0.52358  -0.053146   0.0268931   -0.0199264  68  ASP   A OD2  
2632 H H    . ASP   B 56  ? 0.723272 0.484985 0.517009 -0.0249517  0.0503193   0.047228    68  ASP   A H    
2633 H HA   . ASP   B 56  ? 0.724218 0.510728 0.517767 -0.0724435  0.0158627   0.0286398   68  ASP   A HA   
2634 H HB2  . ASP   B 56  ? 0.753577 0.514471 0.496118 -0.0498166  0.0132005   0.0149929   68  ASP   A HB2  
2635 H HB3  . ASP   B 56  ? 0.753115 0.47708  0.485034 -0.0339395  0.0315274   0.0124666   68  ASP   A HB3  
2636 N N    . SER   B 57  ? 0.72846  0.457254 0.51317  -0.0808096  0.0390021   0.0176681   69  SER   A N    
2637 C CA   . SER   B 57  ? 0.790234 0.484949 0.571505 -0.0828094  0.0543822   0.0161698   69  SER   A CA   
2638 C C    . SER   B 57  ? 0.863814 0.535133 0.631573 -0.106699   0.047091    -0.00213591 69  SER   A C    
2639 O O    . SER   B 57  ? 0.800354 0.496855 0.581825 -0.130448   0.0318187   -0.00508193 69  SER   A O    
2640 C CB   . SER   B 57  ? 0.765374 0.480458 0.584102 -0.086403   0.066183    0.0353612   69  SER   A CB   
2641 O OG   . SER   B 57  ? 0.767768 0.448537 0.582328 -0.0935832  0.0800457   0.0344026   69  SER   A OG   
2642 H H    . SER   B 57  ? 0.742554 0.490581 0.535646 -0.0962816  0.0266472   0.0157607   69  SER   A H    
2643 H HA   . SER   B 57  ? 0.780364 0.4511   0.541691 -0.066496   0.0626009   0.0143515   69  SER   A HA   
2644 H HB2  . SER   B 57  ? 0.752062 0.473677 0.57387  -0.0690769  0.0748432   0.0453382   69  SER   A HB2  
2645 H HB3  . SER   B 57  ? 0.764616 0.510378 0.608359 -0.101195   0.056364    0.0397381   69  SER   A HB3  
2647 N N    . SER   B 58  ? 0.819415 0.442967 0.562191 -0.100156   0.0583799   -0.0121543  70  SER   A N    
2648 C CA   . SER   B 58  ? 0.952529 0.541183 0.682895 -0.120384   0.0586552   -0.0286734  70  SER   A CA   
2649 C C    . SER   B 58  ? 0.936143 0.535954 0.695614 -0.149393   0.0566926   -0.0233958  70  SER   A C    
2650 O O    . SER   B 58  ? 0.997247 0.579352 0.74778  -0.17557    0.049046    -0.0399297  70  SER   A O    
2651 C CB   . SER   B 58  ? 0.98998  0.526865 0.699065 -0.104923   0.0744882   -0.0327254  70  SER   A CB   
2652 O OG   . SER   B 58  ? 0.974117 0.505252 0.694568 -0.0927625  0.0885037   -0.0133964  70  SER   A OG   
2653 H H    . SER   B 58  ? 0.844727 0.455646 0.577581 -0.0821902  0.0661746   -0.00819249 70  SER   A H    
2654 H HA   . SER   B 58  ? 0.933923 0.524004 0.649494 -0.127025   0.0489793   -0.0416836  70  SER   A HA   
2655 H HB2  . SER   B 58  ? 1.0125   0.524085 0.71517  -0.1185     0.0761878   -0.0433119  70  SER   A HB2  
2656 H HB3  . SER   B 58  ? 0.972727 0.504002 0.665454 -0.0898226  0.0736186   -0.0377888  70  SER   A HB3  
2658 N N    . HIS   B 59  ? 0.900843 0.52724  0.694171 -0.146323   0.064899    -0.00133327 71  HIS   A N    
2659 C CA   . HIS   B 59  ? 0.943489 0.585093 0.772228 -0.175339   0.0640554   0.00619726  71  HIS   A CA   
2660 C C    . HIS   B 59  ? 0.968621 0.659057 0.819985 -0.201082   0.0389893   0.00432704  71  HIS   A C    
2661 O O    . HIS   B 59  ? 1.01253  0.709604 0.884335 -0.233525   0.0305027   0.00227398  71  HIS   A O    
2662 C CB   . HIS   B 59  ? 0.941564 0.598586 0.80259  -0.165105   0.0838375   0.0315851   71  HIS   A CB   
2663 C CG   . HIS   B 59  ? 0.95575  0.564807 0.78959  -0.143046   0.105774    0.0354045   71  HIS   A CG   
2664 N ND1  . HIS   B 59  ? 1.06708  0.632052 0.894558 -0.154209   0.118288    0.034618    71  HIS   A ND1  
2665 C CD2  . HIS   B 59  ? 0.94451  0.54318  0.755435 -0.11207    0.1157      0.0415521   71  HIS   A CD2  
2666 C CE1  . HIS   B 59  ? 1.08656  0.618112 0.887362 -0.128422   0.134295    0.0420142   71  HIS   A CE1  
2667 N NE2  . HIS   B 59  ? 1.00576  0.557866 0.79483  -0.103778   0.131526    0.0450339   71  HIS   A NE2  
2668 H H    . HIS   B 59  ? 0.890252 0.524343 0.684896 -0.12724    0.0718914   0.00881347  71  HIS   A H    
2669 H HA   . HIS   B 59  ? 0.975563 0.581423 0.79105  -0.186808   0.0677063   -0.00420582 71  HIS   A HA   
2670 H HB2  . HIS   B 59  ? 0.91449  0.604301 0.789311 -0.15299    0.0824059   0.0416887   71  HIS   A HB2  
2671 H HB3  . HIS   B 59  ? 0.955853 0.623981 0.843597 -0.186017   0.0837561   0.0369757   71  HIS   A HB3  
2673 H HD2  . HIS   B 59  ? 0.927309 0.545298 0.735636 -0.0988322  0.11151     0.0430855   71  HIS   A HD2  
2674 H HE1  . HIS   B 59  ? 1.09564  0.593328 0.886319 -0.128281   0.144873    0.0449022   71  HIS   A HE1  
2676 N N    . ASP   B 60  ? 0.912848 0.638109 0.761559 -0.188183   0.025899    0.0069452   72  ASP   A N    
2677 C CA   . ASP   B 60  ? 1.01138  0.775132 0.866881 -0.211265   -0.0015411  0.00280593  72  ASP   A CA   
2678 C C    . ASP   B 60  ? 1.1317   0.855406 0.950672 -0.239839   -0.0115762  -0.0247424  72  ASP   A C    
2679 O O    . ASP   B 60  ? 1.31364  1.04896  1.1501   -0.273922   -0.0250089  -0.0270608  72  ASP   A O    
2680 C CB   . ASP   B 60  ? 0.964324 0.75278  0.805142 -0.190936   -0.012018   0.0053279   72  ASP   A CB   
2681 C CG   . ASP   B 60  ? 0.967223 0.785716 0.837172 -0.16089    -0.00021585 0.0294843   72  ASP   A CG   
2682 O OD1  . ASP   B 60  ? 0.988452 0.829441 0.901604 -0.161649   0.0102518   0.0481325   72  ASP   A OD1  
2683 O OD2  . ASP   B 60  ? 0.881777 0.698986 0.73114  -0.137176   0.00051012  0.029549    72  ASP   A OD2  
2684 H H    . ASP   B 60  ? 0.916898 0.641019 0.758072 -0.165118   0.0336691   0.0120913   72  ASP   A H    
2685 H HA   . ASP   B 60  ? 0.999145 0.798073 0.893068 -0.223368   -0.00656008 0.0170744   72  ASP   A HA   
2686 H HB2  . ASP   B 60  ? 0.981936 0.738835 0.787081 -0.181466   -0.00804204 -0.00888794 72  ASP   A HB2  
2687 H HB3  . ASP   B 60  ? 0.986297 0.801317 0.831587 -0.207612   -0.0310843  0.00490298  72  ASP   A HB3  
2688 N N    . ARG   B 61  ? 1.18805  0.862234 0.957971 -0.226467   -0.00316063 -0.0455473  73  ARG   A N    
2689 C CA   . ARG   B 61  ? 1.24763  0.87509  0.978104 -0.249258   -0.00671309 -0.0737354  73  ARG   A CA   
2690 C C    . ARG   B 61  ? 1.21578  0.804162 0.956839 -0.269742   0.00477513  -0.0780231  73  ARG   A C    
2691 O O    . ARG   B 61  ? 1.30747  0.84958  1.01679  -0.29041    0.00438268  -0.102112   73  ARG   A O    
2692 C CB   . ARG   B 61  ? 1.29768  0.888848 0.983576 -0.222918   0.00445308  -0.0894388  73  ARG   A CB   
2693 H H    . ARG   B 61  ? 1.15352  0.822412 0.91514  -0.202249   0.00594231  -0.0419567  73  ARG   A H    
2694 H HA   . ARG   B 61  ? 1.25667  0.905327 0.982733 -0.269537   -0.0253481  -0.0788973  73  ARG   A HA   
2697 N N    . ASN   B 62  ? 1.18813  0.79183  0.972025 -0.265741   0.0165816   -0.0549917  74  ASN   A N    
2698 C CA   . ASN   B 62  ? 1.2019   0.767641 0.998396 -0.282655   0.0311053   -0.0541919  74  ASN   A CA   
2699 C C    . ASN   B 62  ? 1.22915  0.716944 0.98039  -0.276553   0.0467605   -0.0766555  74  ASN   A C    
2700 O O    . ASN   B 62  ? 1.21169  0.658368 0.957916 -0.303219   0.0501613   -0.0885227  74  ASN   A O    
2701 C CB   . ASN   B 62  ? 1.14014  0.730786 0.969018 -0.328133   0.0139691   -0.053109   74  ASN   A CB   
2702 H H    . ASN   B 62  ? 1.15089  0.78877  0.956422 -0.251367   0.0171908   -0.0384213  74  ASN   A H    
2703 H HA   . ASN   B 62  ? 1.16183  0.736314 0.9793   -0.266509   0.0445547   -0.0360956  74  ASN   A HA   
2706 N N    . GLU   B 63  ? 1.19359  0.659369 0.916289 -0.241083   0.0579971   -0.0805123  75  GLU   A N    
2707 C CA   . GLU   B 63  ? 1.23506  0.632299 0.926461 -0.227328   0.0765977   -0.0941916  75  GLU   A CA   
2708 C C    . GLU   B 63  ? 1.17164  0.571027 0.853905 -0.184574   0.086651    -0.0838012  75  GLU   A C    
2709 O O    . GLU   B 63  ? 1.00682  0.45113  0.692184 -0.172222   0.0760284   -0.0781949  75  GLU   A O    
2710 C CB   . GLU   B 63  ? 1.22979  0.586413 0.881137 -0.244576   0.0723796   -0.126731   75  GLU   A CB   
2711 H H    . GLU   B 63  ? 1.16347  0.659129 0.888904 -0.224652   0.0538402   -0.0731741  75  GLU   A H    
2712 H HA   . GLU   B 63  ? 1.23931  0.61381  0.942559 -0.234019   0.0868268   -0.0872292  75  GLU   A HA   
2715 N N    . PRO   B 64  ? 1.17191  0.523795 0.844192 -0.163018   0.105501    -0.0796268  76  PRO   A N    
2716 C CA   . PRO   B 64  ? 1.10744  0.459605 0.770292 -0.125681   0.111711    -0.0705841  76  PRO   A CA   
2717 C C    . PRO   B 64  ? 1.08183  0.445304 0.724284 -0.114834   0.104173    -0.0873463  76  PRO   A C    
2718 O O    . PRO   B 64  ? 1.07124  0.419641 0.696015 -0.13292    0.100791    -0.109719   76  PRO   A O    
2719 C CB   . PRO   B 64  ? 1.13081  0.422894 0.783369 -0.111985   0.129719    -0.0692167  76  PRO   A CB   
2720 C CG   . PRO   B 64  ? 1.24044  0.503076 0.903512 -0.140252   0.136682    -0.068398   76  PRO   A CG   
2721 C CD   . PRO   B 64  ? 1.26734  0.560345 0.936424 -0.175327   0.120222    -0.083514   76  PRO   A CD   
2722 H HA   . PRO   B 64  ? 1.07827  0.457566 0.753977 -0.116563   0.110542    -0.0541391  76  PRO   A HA   
2723 H HB2  . PRO   B 64  ? 1.16599  0.436019 0.803222 -0.106285   0.132604    -0.0837543  76  PRO   A HB2  
2724 H HB3  . PRO   B 64  ? 1.13259  0.4273   0.787897 -0.0917733  0.133977    -0.0534729  76  PRO   A HB3  
2725 H HG2  . PRO   B 64  ? 1.26901  0.486061 0.920929 -0.139622   0.146663    -0.0764282  76  PRO   A HG2  
2726 H HG3  . PRO   B 64  ? 1.22061  0.491339 0.897706 -0.137414   0.141287    -0.0497276  76  PRO   A HG3  
2727 H HD2  . PRO   B 64  ? 1.28632  0.551884 0.937682 -0.187007   0.119877    -0.103345   76  PRO   A HD2  
2728 H HD3  . PRO   B 64  ? 1.25898  0.560652 0.947325 -0.193185   0.119791    -0.0746152  76  PRO   A HD3  
2729 N N    . PHE   B 65  ? 1.02911  0.418095 0.672405 -0.0881111  0.101915    -0.0763469  77  PHE   A N    
2730 C CA   . PHE   B 65  ? 1.04154  0.439745 0.669792 -0.0723222  0.0987791   -0.0868911  77  PHE   A CA   
2731 C C    . PHE   B 65  ? 1.11486  0.474238 0.735705 -0.0479192  0.112867    -0.0881039  77  PHE   A C    
2732 O O    . PHE   B 65  ? 1.12046  0.468887 0.749553 -0.0305389  0.118194    -0.0704028  77  PHE   A O    
2733 C CB   . PHE   B 65  ? 0.950856 0.397345 0.58877  -0.0594706  0.0881708   -0.0722293  77  PHE   A CB   
2734 C CG   . PHE   B 65  ? 0.988433 0.451314 0.615338 -0.0448356  0.0839856   -0.0793479  77  PHE   A CG   
2735 C CD1  . PHE   B 65  ? 1.06761  0.549298 0.682511 -0.0588193  0.0756619   -0.0933743  77  PHE   A CD1  
2736 C CD2  . PHE   B 65  ? 0.948313 0.408778 0.576674 -0.0187622  0.0876748   -0.0706899  77  PHE   A CD2  
2737 C CE1  . PHE   B 65  ? 1.14884  0.645185 0.75431  -0.0458912  0.0745509   -0.0977161  77  PHE   A CE1  
2738 C CE2  . PHE   B 65  ? 1.0263   0.50354  0.649976 -0.00743412 0.0849998   -0.0758701  77  PHE   A CE2  
2739 C CZ   . PHE   B 65  ? 0.99331  0.487801 0.605837 -0.0205176  0.0801297   -0.0890867  77  PHE   A CZ   
2740 H H    . PHE   B 65  ? 1.01929  0.420408 0.673177 -0.0798373  0.102974    -0.060745   77  PHE   A H    
2741 H HA   . PHE   B 65  ? 1.05374  0.452401 0.67096  -0.0870764  0.0945733   -0.102198   77  PHE   A HA   
2742 H HB2  . PHE   B 65  ? 0.962341 0.433207 0.608536 -0.0737642  0.080316    -0.0699226  77  PHE   A HB2  
2743 H HB3  . PHE   B 65  ? 0.962324 0.406029 0.606666 -0.0468618  0.0921485   -0.0583934  77  PHE   A HB3  
2744 H HD1  . PHE   B 65  ? 1.07982  0.565774 0.692997 -0.0779506  0.0701692   -0.0986995  77  PHE   A HD1  
2745 H HD2  . PHE   B 65  ? 0.978448 0.425757 0.611284 -0.00948964 0.091793    -0.0604512  77  PHE   A HD2  
2746 H HE1  . PHE   B 65  ? 1.09274  0.60053  0.686935 -0.0556172  0.0696372   -0.106098   77  PHE   A HE1  
2747 H HE2  . PHE   B 65  ? 0.98516  0.463223 0.613303 0.00849301  0.0859607   -0.0690084  77  PHE   A HE2  
2748 H HZ   . PHE   B 65  ? 1.019    0.524913 0.628471 -0.0132503  0.0798194   -0.091342   77  PHE   A HZ   
2749 N N    . VAL   B 66  ? 1.21433  0.555662 0.819081 -0.0458524  0.118905    -0.108061   78  VAL   A N    
2750 C CA   . VAL   B 66  ? 1.19831  0.503032 0.801429 -0.0225185  0.134938    -0.110493   78  VAL   A CA   
2751 C C    . VAL   B 66  ? 1.08311  0.416569 0.685686 -0.00463178 0.133215    -0.113379   78  VAL   A C    
2752 O O    . VAL   B 66  ? 1.21848  0.575789 0.8082   -0.017378   0.126379    -0.125573   78  VAL   A O    
2753 C CB   . VAL   B 66  ? 1.24135  0.489629 0.826939 -0.0346758  0.151082    -0.133013   78  VAL   A CB   
2754 C CG1  . VAL   B 66  ? 1.2136   0.418163 0.807258 -0.00729074 0.170424    -0.127414   78  VAL   A CG1  
2755 C CG2  . VAL   B 66  ? 1.37396  0.602079 0.956184 -0.0662988  0.147979    -0.137234   78  VAL   A CG2  
2756 H H    . VAL   B 66  ? 1.18568  0.538684 0.780361 -0.0589808  0.113467    -0.119852   78  VAL   A H    
2757 H HA   . VAL   B 66  ? 1.17668  0.474708 0.790837 -0.00996527 0.136997    -0.0947591  78  VAL   A HA   
2758 H HB   . VAL   B 66  ? 1.25863  0.511088 0.829076 -0.0403785  0.15156     -0.149057   78  VAL   A HB   
2759 H HG11 . VAL   B 66  ? 1.22272  0.424665 0.828971 -0.00020076 0.168906    -0.109614   78  VAL   A HG11 
2760 H HG12 . VAL   B 66  ? 1.21483  0.434075 0.813408 0.0108322   0.172601    -0.126014   78  VAL   A HG12 
2761 H HG13 . VAL   B 66  ? 1.27703  0.441316 0.858611 -0.0150595  0.182388    -0.142217   78  VAL   A HG13 
2762 H HG21 . VAL   B 66  ? 1.38745  0.574038 0.956965 -0.0735604  0.158911    -0.151788   78  VAL   A HG21 
2763 H HG22 . VAL   B 66  ? 1.32664  0.58289  0.905143 -0.084062   0.135565    -0.141875   78  VAL   A HG22 
2764 H HG23 . VAL   B 66  ? 1.33109  0.559439 0.927947 -0.0619096  0.147782    -0.120078   78  VAL   A HG23 
2765 N N    . PHE   B 67  ? 1.04051  0.372181 0.658106 0.0236522   0.138959    -0.1007     79  PHE   A N    
2766 C CA   . PHE   B 67  ? 1.00229  0.357326 0.625935 0.0409512   0.141032    -0.102833   79  PHE   A CA   
2767 C C    . PHE   B 67  ? 1.05627  0.395176 0.701588 0.07022     0.151216    -0.0896909  79  PHE   A C    
2768 O O    . PHE   B 67  ? 1.1246   0.441166 0.777641 0.0777225   0.151535    -0.0745364  79  PHE   A O    
2769 C CB   . PHE   B 67  ? 0.911424 0.318995 0.541576 0.0415053   0.122578    -0.0910322  79  PHE   A CB   
2770 C CG   . PHE   B 67  ? 0.925789 0.348352 0.570902 0.0552437   0.111062    -0.0667235  79  PHE   A CG   
2771 C CD1  . PHE   B 67  ? 0.865099 0.278005 0.506892 0.0478077   0.106424    -0.0554799  79  PHE   A CD1  
2772 C CD2  . PHE   B 67  ? 0.926994 0.372628 0.587789 0.07441     0.105376    -0.0550658  79  PHE   A CD2  
2773 C CE1  . PHE   B 67  ? 0.894453 0.315879 0.540588 0.0603188   0.0977786   -0.0347386  79  PHE   A CE1  
2774 C CE2  . PHE   B 67  ? 0.919518 0.376919 0.585558 0.0836221   0.0921487   -0.0348766  79  PHE   A CE2  
2775 C CZ   . PHE   B 67  ? 0.863549 0.307181 0.518462 0.0770661   0.0888565   -0.0253981  79  PHE   A CZ   
2776 H H    . PHE   B 67  ? 1.05192  0.368582 0.677723 0.0320365   0.141249    -0.0888494  79  PHE   A H    
2777 H HA   . PHE   B 67  ? 1.028    0.374247 0.637915 0.033467    0.148739    -0.120001   79  PHE   A HA   
2778 H HB2  . PHE   B 67  ? 0.923479 0.345262 0.556081 0.0484656   0.125124    -0.0950644  79  PHE   A HB2  
2779 H HB3  . PHE   B 67  ? 0.922921 0.341446 0.542799 0.0243693   0.115587    -0.0960833  79  PHE   A HB3  
2780 H HD1  . PHE   B 67  ? 0.905101 0.303935 0.540526 0.0336803   0.109988    -0.0620038  79  PHE   A HD1  
2781 H HD2  . PHE   B 67  ? 0.920118 0.375734 0.586353 0.0791499   0.109566    -0.0611475  79  PHE   A HD2  
2782 H HE1  . PHE   B 67  ? 0.885542 0.299877 0.52704  0.0552148   0.0971118   -0.0272882  79  PHE   A HE1  
2783 H HE2  . PHE   B 67  ? 0.888557 0.362435 0.564956 0.0940874   0.0860618   -0.0275344  79  PHE   A HE2  
2784 H HZ   . PHE   B 67  ? 0.874278 0.321692 0.527526 0.0836873   0.0814543   -0.0123704  79  PHE   A HZ   
2785 N N    . SER   B 68  ? 1.05812  0.413084 0.715433 0.0866273   0.15856     -0.0925387  80  SER   A N    
2786 C CA   . SER   B 68  ? 1.10884  0.457381 0.795182 0.115963    0.167575    -0.0781971  80  SER   A CA   
2787 C C    . SER   B 68  ? 1.11051  0.509064 0.818582 0.12692     0.147313    -0.0568649  80  SER   A C    
2788 O O    . SER   B 68  ? 1.00222  0.436842 0.709504 0.120414    0.140085    -0.0611659  80  SER   A O    
2789 C CB   . SER   B 68  ? 1.2181   0.549098 0.907311 0.126614    0.192856    -0.0953252  80  SER   A CB   
2790 O OG   . SER   B 68  ? 1.28838  0.629692 1.01633  0.157301    0.200842    -0.0787827  80  SER   A OG   
2791 H H    . SER   B 68  ? 1.05521  0.427431 0.704225 0.0793851   0.157993    -0.102299   80  SER   A H    
2792 H HA   . SER   B 68  ? 1.14197  0.463486 0.830566 0.120405    0.170158    -0.0704725  80  SER   A HA   
2793 H HB2  . SER   B 68  ? 1.2538   0.54514  0.927772 0.12079     0.205722    -0.107826   80  SER   A HB2  
2794 H HB3  . SER   B 68  ? 1.2019   0.552714 0.880254 0.11727     0.192238    -0.106026   80  SER   A HB3  
2796 N N    . LEU   B 69  ? 1.0892   0.486224 0.812107 0.141008    0.137023    -0.0336416  81  LEU   A N    
2797 C CA   . LEU   B 69  ? 0.967052 0.403373 0.69932  0.145145    0.113583    -0.0144106  81  LEU   A CA   
2798 C C    . LEU   B 69  ? 0.953941 0.425331 0.71898  0.161126    0.112402    -0.00821164 81  LEU   A C    
2799 O O    . LEU   B 69  ? 1.00924  0.47242  0.801957 0.181549    0.125396    -0.00233195 81  LEU   A O    
2800 C CB   . LEU   B 69  ? 0.934099 0.355325 0.666486 0.155133    0.10282     0.00902775  81  LEU   A CB   
2801 C CG   . LEU   B 69  ? 0.848945 0.303914 0.584162 0.159386    0.077301    0.0289143   81  LEU   A CG   
2802 C CD1  . LEU   B 69  ? 0.841916 0.305144 0.546186 0.138822    0.0667571   0.0234885   81  LEU   A CD1  
2803 C CD2  . LEU   B 69  ? 0.891094 0.332448 0.63157  0.176076    0.0678417   0.0549986   81  LEU   A CD2  
2804 H H    . LEU   B 69  ? 1.09827  0.466213 0.823082 0.147735    0.144803    -0.0296321  81  LEU   A H    
2805 H HA   . LEU   B 69  ? 0.951724 0.40219  0.668191 0.130155    0.10534     -0.0200345  81  LEU   A HA   
2806 H HB2  . LEU   B 69  ? 0.936941 0.337644 0.649736 0.143831    0.104867    0.0059396   81  LEU   A HB2  
2807 H HB3  . LEU   B 69  ? 0.954342 0.358491 0.702489 0.170078    0.111871    0.0152012   81  LEU   A HB3  
2808 H HG   . LEU   B 69  ? 0.850264 0.332315 0.603848 0.164027    0.0734508   0.0285752   81  LEU   A HG   
2809 H HD11 . LEU   B 69  ? 0.820532 0.295391 0.523116 0.129161    0.0706318   0.00950056  81  LEU   A HD11 
2810 H HD12 . LEU   B 69  ? 0.827093 0.306904 0.52844  0.14053     0.0517505   0.033809    81  LEU   A HD12 
2811 H HD13 . LEU   B 69  ? 0.851988 0.291759 0.541102 0.133531    0.0716884   0.0243035   81  LEU   A HD13 
2812 H HD21 . LEU   B 69  ? 0.900448 0.344868 0.667014 0.1915      0.0718403   0.0615683   81  LEU   A HD21 
2813 H HD22 . LEU   B 69  ? 0.908938 0.320381 0.634502 0.173244    0.0752465   0.0561617   81  LEU   A HD22 
2814 H HD23 . LEU   B 69  ? 0.875819 0.334817 0.60807  0.173989    0.0504915   0.0648164   81  LEU   A HD23 
2815 N N    . GLY   B 70  ? 0.930597 0.44081  0.694164 0.151171    0.0972109   -0.0081861  82  GLY   A N    
2816 C CA   . GLY   B 70  ? 0.971725 0.522167 0.768385 0.161405    0.0914849   0.00060271  82  GLY   A CA   
2817 C C    . GLY   B 70  ? 0.971437 0.530837 0.777614 0.16139     0.113481    -0.0163279  82  GLY   A C    
2818 O O    . GLY   B 70  ? 0.997094 0.591152 0.8361   0.170116    0.112841    -0.00827971 82  GLY   A O    
2819 H H    . GLY   B 70  ? 0.925771 0.437443 0.668764 0.137193    0.0906415   -0.0132068  82  GLY   A H    
2820 H HA2  . GLY   B 70  ? 0.932437 0.503728 0.723404 0.152949    0.0752725   0.00504488  82  GLY   A HA2  
2821 H HA3  . GLY   B 70  ? 0.966986 0.518772 0.786231 0.176767    0.0891691   0.0147222   82  GLY   A HA3  
2822 N N    . LYS   B 71  ? 0.997229 0.526051 0.774145 0.150521    0.13217     -0.0386064  83  LYS   A N    
2823 C CA   . LYS   B 71  ? 0.976421 0.5041   0.750631 0.15005     0.156165    -0.056813   83  LYS   A CA   
2824 C C    . LYS   B 71  ? 1.10246  0.65385  0.851692 0.128283    0.148477    -0.0669468  83  LYS   A C    
2825 O O    . LYS   B 71  ? 1.24659  0.78683  0.972267 0.119428    0.165359    -0.0857973  83  LYS   A O    
2826 C CB   . LYS   B 71  ? 1.05302  0.528522 0.803947 0.149606    0.181044    -0.0767938  83  LYS   A CB   
2827 H H    . LYS   B 71  ? 0.992814 0.500461 0.748642 0.141817    0.129329    -0.0424825  83  LYS   A H    
2828 H HA   . LYS   B 71  ? 1.01312  0.559094 0.817685 0.164576    0.162454    -0.0488629  83  LYS   A HA   
2831 N N    . GLY   B 72  ? 1.08481  0.663954 0.835526 0.119974    0.12344     -0.0541569  84  GLY   A N    
2832 C CA   . GLY   B 72  ? 1.04882  0.651392 0.78155  0.102117    0.112738    -0.0575392  84  GLY   A CA   
2833 C C    . GLY   B 72  ? 1.01014  0.594378 0.703257 0.083198    0.117674    -0.0753999  84  GLY   A C    
2834 O O    . GLY   B 72  ? 0.924879 0.527131 0.603364 0.0710652   0.115902    -0.0798552  84  GLY   A O    
2835 H H    . GLY   B 72  ? 1.06681  0.64825  0.829828 0.12661     0.11248     -0.0417514  84  GLY   A H    
2836 H HA2  . GLY   B 72  ? 1.01901  0.631085 0.752991 0.0993073   0.0959578   -0.047655   84  GLY   A HA2  
2837 H HA3  . GLY   B 72  ? 1.03384  0.657028 0.780448 0.10493     0.118013    -0.0561825  84  GLY   A HA3  
2838 N N    . GLN   B 73  ? 0.92968  0.480369 0.606026 0.0785692   0.120253    -0.0828081  85  GLN   A N    
2839 C CA   . GLN   B 73  ? 0.90373  0.440341 0.546538 0.0573249   0.119042    -0.0971795  85  GLN   A CA   
2840 C C    . GLN   B 73  ? 0.925328 0.477469 0.562622 0.0451548   0.0981753   -0.0872801  85  GLN   A C    
2841 O O    . GLN   B 73  ? 0.840018 0.396292 0.457145 0.0270916   0.0924458   -0.0941435  85  GLN   A O    
2842 C CB   . GLN   B 73  ? 1.00147  0.494113 0.633346 0.0556366   0.131093    -0.108563   85  GLN   A CB   
2843 C CG   . GLN   B 73  ? 1.17957  0.647465 0.814994 0.0697307   0.156457    -0.120081   85  GLN   A CG   
2844 C CD   . GLN   B 73  ? 1.18912  0.606543 0.817769 0.0711826   0.169003    -0.128463   85  GLN   A CD   
2845 O OE1  . GLN   B 73  ? 1.14419  0.546586 0.767944 0.0610634   0.158369    -0.123974   85  GLN   A OE1  
2846 N NE2  . GLN   B 73  ? 1.21944  0.609406 0.851007 0.0857266   0.194433    -0.139065   85  GLN   A NE2  
2847 H H    . GLN   B 73  ? 0.953744 0.490737 0.641382 0.0882771   0.121703    -0.0773491  85  GLN   A H    
2848 H HA   . GLN   B 73  ? 0.939056 0.48284  0.569288 0.0512231   0.124899    -0.105885   85  GLN   A HA   
2849 H HB2  . GLN   B 73  ? 1.00888  0.494572 0.651977 0.0613012   0.125484    -0.0982766  85  GLN   A HB2  
2850 H HB3  . GLN   B 73  ? 1.0262   0.511273 0.636892 0.0390014   0.128339    -0.118173   85  GLN   A HB3  
2851 H HG2  . GLN   B 73  ? 1.15132  0.620226 0.768448 0.0620708   0.164191    -0.132605   85  GLN   A HG2  
2852 H HG3  . GLN   B 73  ? 1.12295  0.605747 0.783693 0.0860375   0.15852     -0.109182   85  GLN   A HG3  
2853 H HE21 . GLN   B 73  ? 1.25377  0.609944 0.88123  0.0877793   0.204211    -0.144641   85  GLN   A HE21 
2854 H HE22 . GLN   B 73  ? 1.22184  0.626175 0.860078 0.0937426   0.203022    -0.140345   85  GLN   A HE22 
2855 N N    . VAL   B 74  ? 0.850103 0.413596 0.505189 0.0552956   0.0865408   -0.0701968  86  VAL   A N    
2856 C CA   . VAL   B 74  ? 0.828601 0.404363 0.478372 0.047385    0.0712315   -0.0606694  86  VAL   A CA   
2857 C C    . VAL   B 74  ? 0.744358 0.344171 0.406763 0.0554293   0.0605943   -0.0482106  86  VAL   A C    
2858 O O    . VAL   B 74  ? 0.761786 0.369722 0.441362 0.0662417   0.063293    -0.045175   86  VAL   A O    
2859 C CB   . VAL   B 74  ? 0.846016 0.398799 0.495411 0.0498489   0.0698053   -0.0535025  86  VAL   A CB   
2860 C CG1  . VAL   B 74  ? 0.867665 0.396233 0.505887 0.0371058   0.0784194   -0.0651409  86  VAL   A CG1  
2861 C CG2  . VAL   B 74  ? 0.870477 0.41219  0.534707 0.0684984   0.071216    -0.0435067  86  VAL   A CG2  
2862 H H    . VAL   B 74  ? 0.862858 0.425962 0.533073 0.067669    0.0886868   -0.0643309  86  VAL   A H    
2863 H HA   . VAL   B 74  ? 0.816812 0.399171 0.455498 0.0355952   0.0693182   -0.0658089  86  VAL   A HA   
2864 H HB   . VAL   B 74  ? 0.830727 0.39256  0.477359 0.0468935   0.0616822   -0.0462521  86  VAL   A HB   
2865 H HG11 . VAL   B 74  ? 0.889216 0.40424  0.526599 0.0398532   0.0880627   -0.0740168  86  VAL   A HG11 
2866 H HG12 . VAL   B 74  ? 0.864201 0.404032 0.494728 0.0245252   0.0744429   -0.0694576  86  VAL   A HG12 
2867 H HG13 . VAL   B 74  ? 0.87592  0.39035  0.515254 0.0381258   0.0785288   -0.0590411  86  VAL   A HG13 
2868 H HG21 . VAL   B 74  ? 0.871929 0.39921  0.532637 0.0698667   0.0697253   -0.0369847  86  VAL   A HG21 
2869 H HG22 . VAL   B 74  ? 0.849605 0.408663 0.521308 0.0739357   0.0636211   -0.0365921  86  VAL   A HG22 
2870 H HG23 . VAL   B 74  ? 0.881861 0.413231 0.551741 0.0734922   0.0812855   -0.0496641  86  VAL   A HG23 
2871 N N    . ILE   B 75  ? 0.757162 0.366841 0.412962 0.0499891   0.0493563   -0.0407888  87  ILE   A N    
2872 C CA   . ILE   B 75  ? 0.769721 0.395082 0.431824 0.0542383   0.0385394   -0.0309577  87  ILE   A CA   
2873 C C    . ILE   B 75  ? 0.767058 0.385083 0.439189 0.0665423   0.0325067   -0.0217762  87  ILE   A C    
2874 O O    . ILE   B 75  ? 0.728566 0.3261   0.398387 0.0725787   0.035848    -0.0194648  87  ILE   A O    
2875 C CB   . ILE   B 75  ? 0.740831 0.368457 0.390274 0.0478445   0.0311699   -0.0256599  87  ILE   A CB   
2876 C CG1  . ILE   B 75  ? 0.776195 0.385662 0.416139 0.0477756   0.0330683   -0.0225129  87  ILE   A CG1  
2877 C CG2  . ILE   B 75  ? 0.682249 0.326222 0.32794  0.0376632   0.0322407   -0.0290527  87  ILE   A CG2  
2878 C CD1  . ILE   B 75  ? 0.765364 0.377959 0.396961 0.0446529   0.0303957   -0.0162117  87  ILE   A CD1  
2879 H H    . ILE   B 75  ? 0.757681 0.363641 0.405254 0.0429395   0.048809    -0.0419927  87  ILE   A H    
2880 H HA   . ILE   B 75  ? 0.753265 0.392262 0.421386 0.0529417   0.0401887   -0.0330483  87  ILE   A HA   
2881 H HB   . ILE   B 75  ? 0.734077 0.364534 0.384351 0.0508002   0.0245051   -0.0203116  87  ILE   A HB   
2882 H HG12 . ILE   B 75  ? 0.775191 0.380669 0.415574 0.0431523   0.0387695   -0.0278215  87  ILE   A HG12 
2883 H HG13 . ILE   B 75  ? 0.777131 0.375442 0.416236 0.0545451   0.0315722   -0.0184946  87  ILE   A HG13 
2884 H HG21 . ILE   B 75  ? 0.690806 0.337463 0.333003 0.0363697   0.0280283   -0.0236784  87  ILE   A HG21 
2885 H HG22 . ILE   B 75  ? 0.703509 0.344849 0.345407 0.0323742   0.0364029   -0.0343554  87  ILE   A HG22 
2886 H HG23 . ILE   B 75  ? 0.694535 0.348564 0.344802 0.0374776   0.0331387   -0.0305206  87  ILE   A HG23 
2887 H HD11 . ILE   B 75  ? 0.763232 0.377333 0.391702 0.047576    0.0253003   -0.0130301  87  ILE   A HD11 
2888 H HD12 . ILE   B 75  ? 0.774286 0.375187 0.400899 0.0462136   0.0333561   -0.0128982  87  ILE   A HD12 
2889 H HD13 . ILE   B 75  ? 0.759593 0.383584 0.394127 0.0382939   0.0315161   -0.0180761  87  ILE   A HD13 
2890 N N    . LYS   B 76  ? 0.731322 0.366466 0.414952 0.068758    0.0225974   -0.0152972  88  LYS   A N    
2891 C CA   . LYS   B 76  ? 0.723713 0.36005  0.41847  0.0775817   0.0108411   -0.00444972 88  LYS   A CA   
2892 C C    . LYS   B 76  ? 0.700777 0.312454 0.372452 0.0803109   0.00472137  0.00182275  88  LYS   A C    
2893 O O    . LYS   B 76  ? 0.747892 0.349957 0.424989 0.0903119   0.0023029   0.00983354  88  LYS   A O    
2894 C CB   . LYS   B 76  ? 0.725953 0.385142 0.434409 0.0734233   -0.0020636  0.0010093   88  LYS   A CB   
2895 H H    . LYS   B 76  ? 0.725045 0.372392 0.409797 0.0633077   0.0221333   -0.0170402  88  LYS   A H    
2896 H HA   . LYS   B 76  ? 0.727416 0.365502 0.438616 0.0852042   0.0169046   -0.00398398 88  LYS   A HA   
2899 N N    . ALA   B 77  ? 0.743929 0.345485 0.391079 0.0728433   0.00389889  1.34e-06    89  ALA   A N    
2900 C CA   . ALA   B 77  ? 0.757331 0.335641 0.378458 0.0749471   0.00079636  0.0064693   89  ALA   A CA   
2901 C C    . ALA   B 77  ? 0.729599 0.28962  0.350243 0.0799455   0.0118853   0.00841852  89  ALA   A C    
2902 O O    . ALA   B 77  ? 0.716786 0.257393 0.320544 0.0852142   0.00910115  0.0179945   89  ALA   A O    
2903 C CB   . ALA   B 77  ? 0.730104 0.302075 0.331107 0.0682602   0.00430504  0.00369663  89  ALA   A CB   
2904 H H    . ALA   B 77  ? 0.720412 0.329588 0.366863 0.0669223   0.00651931  -0.00457355 89  ALA   A H    
2905 H HA   . ALA   B 77  ? 0.756672 0.333924 0.373654 0.0778156   -0.0104877  0.0126688   89  ALA   A HA   
2906 H HB1  . ALA   B 77  ? 0.732842 0.311898 0.332831 0.0650227   -0.00199027 0.00255139  89  ALA   A HB1  
2907 H HB2  . ALA   B 77  ? 0.727107 0.303459 0.334467 0.0650098   0.0131301   -0.00056711 89  ALA   A HB2  
2908 H HB3  . ALA   B 77  ? 0.753391 0.309118 0.335817 0.0703056   0.0046887   0.00792571  89  ALA   A HB3  
2909 N N    . TRP   B 78  ? 0.74316  0.305832 0.378346 0.0769224   0.0244484   -0.00049705 90  TRP   A N    
2910 C CA   . TRP   B 78  ? 0.746567 0.287081 0.381512 0.0785896   0.0357804   -0.00045349 90  TRP   A CA   
2911 C C    . TRP   B 78  ? 0.784076 0.315661 0.433432 0.0922421   0.035348    0.00628547  90  TRP   A C    
2912 O O    . TRP   B 78  ? 0.823442 0.331337 0.466137 0.098703    0.037829    0.0159837   90  TRP   A O    
2913 C CB   . TRP   B 78  ? 0.719256 0.260626 0.35878  0.0673393   0.0472894   -0.0134516  90  TRP   A CB   
2914 C CG   . TRP   B 78  ? 0.719228 0.259159 0.34905  0.0558645   0.0508556   -0.0134225  90  TRP   A CG   
2915 C CD1  . TRP   B 78  ? 0.751322 0.304073 0.373915 0.0523765   0.0469364   -0.00923427 90  TRP   A CD1  
2916 C CD2  . TRP   B 78  ? 0.834303 0.36039  0.465756 0.0455139   0.0606124   -0.0176936  90  TRP   A CD2  
2917 N NE1  . TRP   B 78  ? 0.737121 0.288623 0.360862 0.0433224   0.054146    -0.00786888 90  TRP   A NE1  
2918 C CE2  . TRP   B 78  ? 0.775978 0.313156 0.405803 0.0368677   0.0610743   -0.0131517  90  TRP   A CE2  
2919 C CE3  . TRP   B 78  ? 0.823629 0.327195 0.458857 0.0423948   0.0696559   -0.0246415  90  TRP   A CE3  
2920 C CZ2  . TRP   B 78  ? 0.744118 0.276672 0.380376 0.0236319   0.0681437   -0.0137423  90  TRP   A CZ2  
2921 C CZ3  . TRP   B 78  ? 0.808661 0.30143  0.444442 0.0273867   0.0761988   -0.0275312  90  TRP   A CZ3  
2922 C CH2  . TRP   B 78  ? 0.814628 0.326061 0.453284 0.0167743   0.0740556   -0.0219861  90  TRP   A CH2  
2923 H H    . TRP   B 78  ? 0.721935 0.298228 0.364872 0.072662    0.0259803   -0.00685177 90  TRP   A H    
2924 H HA   . TRP   B 78  ? 0.757262 0.285775 0.377836 0.0779227   0.0359297   0.00556031  90  TRP   A HA   
2925 H HB2  . TRP   B 78  ? 0.713085 0.270493 0.358576 0.0647409   0.0460087   -0.0195517  90  TRP   A HB2  
2926 H HB3  . TRP   B 78  ? 0.741297 0.268605 0.385935 0.0697203   0.0543213   -0.0160666  90  TRP   A HB3  
2927 H HD1  . TRP   B 78  ? 0.72921  0.288734 0.347347 0.05613     0.0407426   -0.00659429 90  TRP   A HD1  
2928 H HE1  . TRP   B 78  ? 0.74053  0.299539 0.363205 0.0415327   0.054735    -0.0043218  90  TRP   A HE1  
2929 H HE3  . TRP   B 78  ? 0.831605 0.326765 0.47028  0.0501955   0.0717454   -0.0270085  90  TRP   A HE3  
2930 H HZ2  . TRP   B 78  ? 0.757985 0.30251  0.398591 0.0186974   0.0689185   -0.00913728 90  TRP   A HZ2  
2931 H HZ3  . TRP   B 78  ? 0.84114  0.314823 0.477535 0.0235476   0.0824942   -0.0336341  90  TRP   A HZ3  
2932 H HH2  . TRP   B 78  ? 0.809089 0.316197 0.452524 0.00553201  0.0779414   -0.0226783  90  TRP   A HH2  
2933 N N    . ASP   B 79  ? 0.738806 0.290764 0.409909 0.0977496   0.032443    0.00412079  91  ASP   A N    
2934 C CA   . ASP   B 79  ? 0.821107 0.370614 0.514774 0.113501    0.0329096   0.0129654   91  ASP   A CA   
2935 C C    . ASP   B 79  ? 0.88954  0.435444 0.574579 0.121066    0.0151748   0.0319835   91  ASP   A C    
2936 O O    . ASP   B 79  ? 0.872323 0.403525 0.564075 0.133874    0.0145626   0.0450737   91  ASP   A O    
2937 C CB   . ASP   B 79  ? 0.777346 0.354108 0.499994 0.117526    0.0361257   0.00795317  91  ASP   A CB   
2938 C CG   . ASP   B 79  ? 0.80506  0.373664 0.533052 0.115797    0.0583206   -0.00901416 91  ASP   A CG   
2939 O OD1  . ASP   B 79  ? 0.826754 0.364723 0.543582 0.114919    0.0707461   -0.015523   91  ASP   A OD1  
2940 O OD2  . ASP   B 79  ? 0.755405 0.345532 0.496832 0.114787    0.063654    -0.015399   91  ASP   A OD2  
2941 H H    . ASP   B 79  ? 0.745175 0.313388 0.419222 0.0922856   0.0311096   -0.00162755 91  ASP   A H    
2942 H HA   . ASP   B 79  ? 0.825759 0.355376 0.519837 0.116149    0.0444537   0.0101475   91  ASP   A HA   
2943 H HB2  . ASP   B 79  ? 0.771216 0.365788 0.491107 0.110165    0.0282463   0.00647549  91  ASP   A HB2  
2944 H HB3  . ASP   B 79  ? 0.796984 0.380321 0.538705 0.128771    0.0315845   0.0182413   91  ASP   A HB3  
2945 N N    . ILE   B 80  ? 0.823097 0.380214 0.489821 0.11286     -9.337e-05  0.0341369   92  ILE   A N    
2946 C CA   . ILE   B 80  ? 0.873502 0.429045 0.526195 0.117021    -0.02026    0.0500364   92  ILE   A CA   
2947 C C    . ILE   B 80  ? 0.816568 0.339051 0.431986 0.116467    -0.0161346  0.0563567   92  ILE   A C    
2948 O O    . ILE   B 80  ? 0.914987 0.42322  0.521964 0.125672    -0.023015   0.0723401   92  ILE   A O    
2949 C CB   . ILE   B 80  ? 0.958853 0.532708 0.601197 0.105857    -0.0365731  0.0466163   92  ILE   A CB   
2950 C CG1  . ILE   B 80  ? 0.939455 0.547642 0.62054  0.105551    -0.0421545  0.0449726   92  ILE   A CG1  
2951 C CG2  . ILE   B 80  ? 1.0779   0.639794 0.687885 0.10518     -0.0573354  0.0593507   92  ILE   A CG2  
2952 C CD1  . ILE   B 80  ? 1.03121  0.650974 0.700159 0.0908279   -0.0541542  0.0389348   92  ILE   A CD1  
2953 H H    . ILE   B 80  ? 0.826667 0.391158 0.487782 0.104189    0.00167979  0.0255483   92  ILE   A H    
2954 H HA   . ILE   B 80  ? 0.874252 0.437147 0.547653 0.126756    -0.0252768  0.0592855   92  ILE   A HA   
2955 H HB   . ILE   B 80  ? 0.943648 0.51165  0.571387 0.0981576   -0.0288978  0.0373055   92  ILE   A HB   
2956 H HG12 . ILE   B 80  ? 0.970122 0.588482 0.668875 0.11303     -0.0519779  0.0560116   92  ILE   A HG12 
2957 H HG13 . ILE   B 80  ? 0.944922 0.557483 0.64244  0.107237    -0.0274873  0.0374793   92  ILE   A HG13 
2958 H HG21 . ILE   B 80  ? 1.04808  0.619753 0.652536 0.0974067   -0.0690136  0.0567589   92  ILE   A HG21 
2959 H HG22 . ILE   B 80  ? 1.06253  0.628288 0.685091 0.113713    -0.0652623  0.0711505   92  ILE   A HG22 
2960 H HG23 . ILE   B 80  ? 1.06141  0.601101 0.642561 0.103612    -0.0508206  0.0587816   92  ILE   A HG23 
2961 H HD11 . ILE   B 80  ? 0.9912   0.600012 0.64268  0.0851618   -0.0447659  0.0301825   92  ILE   A HD11 
2962 H HD12 . ILE   B 80  ? 0.985142 0.627509 0.68112  0.0895212   -0.0551395  0.0380424   92  ILE   A HD12 
2963 H HD13 . ILE   B 80  ? 1.01707  0.631754 0.668824 0.0880836   -0.0696826  0.0451416   92  ILE   A HD13 
2964 N N    . GLY   B 81  ? 0.80289  0.314856 0.400562 0.106362    -0.0026312  0.0453656   93  GLY   A N    
2965 C CA   . GLY   B 81  ? 0.837091 0.3223   0.401726 0.103947    0.00475072  0.0509213   93  GLY   A CA   
2966 C C    . GLY   B 81  ? 0.839005 0.300384 0.409129 0.108934    0.0192989   0.057338    93  GLY   A C    
2967 O O    . GLY   B 81  ? 0.862905 0.301499 0.409321 0.113728    0.0186227   0.0721367   93  GLY   A O    
2968 H H    . GLY   B 81  ? 0.787122 0.310691 0.39509  0.100867    0.00254155  0.0351108   93  GLY   A H    
2969 H HA2  . GLY   B 81  ? 0.850262 0.329538 0.393493 0.105856    -0.00621478 0.0592034   93  GLY   A HA2  
2970 H HA3  . GLY   B 81  ? 0.81817  0.305334 0.375869 0.0963147   0.0116984   0.0429032   93  GLY   A HA3  
2971 N N    . VAL   B 82  ? 0.796552 0.260012 0.395097 0.108199    0.0313081   0.0473351   94  VAL   A N    
2972 C CA   . VAL   B 82  ? 0.821522 0.256219 0.423981 0.110143    0.0463126   0.0511006   94  VAL   A CA   
2973 C C    . VAL   B 82  ? 0.828767 0.250663 0.439103 0.127685    0.0399245   0.0685242   94  VAL   A C    
2974 O O    . VAL   B 82  ? 0.91474  0.305862 0.517098 0.132533    0.0479805   0.0810549   94  VAL   A O    
2975 C CB   . VAL   B 82  ? 0.880026 0.313003 0.502624 0.10117     0.0614766   0.0327623   94  VAL   A CB   
2976 C CG1  . VAL   B 82  ? 0.932863 0.329621 0.560373 0.102666    0.0765986   0.0352349   94  VAL   A CG1  
2977 C CG2  . VAL   B 82  ? 0.856697 0.30195  0.472293 0.0834213   0.065991    0.0211684   94  VAL   A CG2  
2978 H H    . VAL   B 82  ? 0.783712 0.264064 0.396856 0.105688    0.0307326   0.0378394   94  VAL   A H    
2979 H HA   . VAL   B 82  ? 0.839904 0.262079 0.424262 0.105265    0.0509055   0.0558261   94  VAL   A HA   
2980 H HB   . VAL   B 82  ? 0.857032 0.304332 0.494616 0.105327    0.0587223   0.0266446   94  VAL   A HB   
2981 H HG11 . VAL   B 82  ? 0.942063 0.324375 0.555922 0.100053    0.0792156   0.0445727   94  VAL   A HG11 
2982 H HG12 . VAL   B 82  ? 0.940076 0.329667 0.577931 0.115446    0.0757618   0.0414312   94  VAL   A HG12 
2983 H HG13 . VAL   B 82  ? 0.924655 0.318669 0.558427 0.0931197   0.0849948   0.0217809   94  VAL   A HG13 
2984 H HG21 . VAL   B 82  ? 0.854605 0.29993  0.48015  0.0765363   0.0724456   0.00978796  94  VAL   A HG21 
2985 H HG22 . VAL   B 82  ? 0.838156 0.30317  0.450604 0.0827545   0.057898    0.0194856   94  VAL   A HG22 
2986 H HG23 . VAL   B 82  ? 0.869235 0.302444 0.473897 0.0794554   0.0707637   0.0275922   94  VAL   A HG23 
2987 N N    . ALA   B 83  ? 0.824371 0.270791 0.454501 0.137426    0.0259834   0.0715072   95  ALA   A N    
2988 C CA   . ALA   B 83  ? 0.841835 0.286345 0.486626 0.155779    0.0153371   0.0920377   95  ALA   A CA   
2989 C C    . ALA   B 83  ? 0.9287   0.356341 0.537591 0.158273    0.00227455  0.113195    95  ALA   A C    
2990 O O    . ALA   B 83  ? 0.995211 0.409363 0.609765 0.173174    -0.00263858 0.134192    95  ALA   A O    
2991 C CB   . ALA   B 83  ? 0.814178 0.29832  0.488741 0.16227     -0.00132961 0.093761    95  ALA   A CB   
2992 H H    . ALA   B 83  ? 0.797504 0.264642 0.43517  0.132549    0.0227105   0.0617306   95  ALA   A H    
2993 H HA   . ALA   B 83  ? 0.865098 0.29238  0.525006 0.162822    0.028184    0.0926902   95  ALA   A HA   
2994 H HB1  . ALA   B 83  ? 0.799035 0.293112 0.494022 0.161153    0.00879351  0.0810267   95  ALA   A HB1  
2995 H HB2  . ALA   B 83  ? 0.807595 0.305253 0.466309 0.154315    -0.0145048  0.0929622   95  ALA   A HB2  
2996 H HB3  . ALA   B 83  ? 0.834458 0.320207 0.523871 0.175121    -0.00852147 0.109103    95  ALA   A HB3  
2997 N N    . THR   B 84  ? 0.975918 0.403369 0.546423 0.145189    -0.00308106 0.109141    96  THR   A N    
2998 C CA   . THR   B 84  ? 1.01125  0.420029 0.537711 0.146558    -0.0142657  0.127705    96  THR   A CA   
2999 C C    . THR   B 84  ? 1.02876  0.400827 0.531573 0.143728    0.00721886  0.133633    96  THR   A C    
3000 O O    . THR   B 84  ? 1.09055  0.442421 0.553287 0.144984    0.00334041  0.149745    96  THR   A O    
3001 C CB   . THR   B 84  ? 0.99385  0.412814 0.484103 0.134778    -0.0271531  0.120125    96  THR   A CB   
3002 O OG1  . THR   B 84  ? 0.918135 0.334979 0.400275 0.122505    -0.00871702 0.101718    96  THR   A OG1  
3003 C CG2  . THR   B 84  ? 1.05491  0.507789 0.56402  0.134       -0.0512969  0.11692     96  THR   A CG2  
3004 H H    . THR   B 84  ? 0.936072 0.373944 0.506081 0.135935    0.00079719  0.0951533   96  THR   A H    
3005 H HA   . THR   B 84  ? 1.02593  0.437462 0.559496 0.156766    -0.0271921  0.142622    96  THR   A HA   
3006 H HB   . THR   B 84  ? 1.03266  0.435314 0.488744 0.135761    -0.0332148  0.132067    96  THR   A HB   
3008 H HG21 . THR   B 84  ? 1.03324  0.486254 0.515371 0.125481    -0.0586695  0.111586    96  THR   A HG21 
3009 H HG22 . THR   B 84  ? 0.997984 0.467389 0.539201 0.133408    -0.0448818  0.10617     96  THR   A HG22 
3010 H HG23 . THR   B 84  ? 1.04731  0.505016 0.56369  0.142174    -0.065526   0.131567    96  THR   A HG23 
3011 N N    . MET   B 85  ? 0.985048 0.347993 0.509211 0.13751     0.0298516   0.120788    97  MET   A N    
3012 C CA   . MET   B 85  ? 0.995944 0.328932 0.502103 0.12998     0.0505845   0.125332    97  MET   A CA   
3013 C C    . MET   B 85  ? 1.06618  0.365865 0.582783 0.139143    0.0607655   0.141255    97  MET   A C    
3014 O O    . MET   B 85  ? 1.00715  0.305159 0.555505 0.15036     0.0595163   0.141626    97  MET   A O    
3015 C CB   . MET   B 85  ? 0.966869 0.310676 0.491313 0.113848    0.0668103   0.103039    97  MET   A CB   
3016 C CG   . MET   B 85  ? 0.934508 0.305199 0.447383 0.105519    0.0611769   0.0906469   97  MET   A CG   
3017 S SD   . MET   B 85  ? 0.941255 0.331063 0.481816 0.0884308   0.0754615   0.0689336   97  MET   A SD   
3018 C CE   . MET   B 85  ? 0.94665  0.312957 0.479747 0.0778028   0.0981664   0.0786183   97  MET   A CE   
3019 H H    . MET   B 85  ? 0.964468 0.340401 0.514837 0.136799    0.0323564   0.10908     97  MET   A H    
3020 H HA   . MET   B 85  ? 1.024    0.351034 0.498235 0.128274    0.0480416   0.133123    97  MET   A HA   
3021 H HB2  . MET   B 85  ? 0.951544 0.300902 0.501815 0.114603    0.0681615   0.0936533   97  MET   A HB2  
3022 H HB3  . MET   B 85  ? 0.981544 0.307654 0.500798 0.10785     0.0805838   0.106912    97  MET   A HB3  
3023 H HG2  . MET   B 85  ? 0.961095 0.323007 0.446659 0.104627    0.0631924   0.0981778   97  MET   A HG2  
3024 H HG3  . MET   B 85  ? 0.930457 0.317001 0.447039 0.110141    0.0472237   0.0878408   97  MET   A HG3  
3025 H HE1  . MET   B 85  ? 0.934466 0.312851 0.484645 0.0671109   0.104405    0.0692616   97  MET   A HE1  
3026 H HE2  . MET   B 85  ? 0.974692 0.319786 0.510169 0.0803143   0.102528    0.0858214   97  MET   A HE2  
3027 H HE3  . MET   B 85  ? 0.964613 0.327171 0.474747 0.0798193   0.100369    0.0867663   97  MET   A HE3  
3028 N N    . LYS   B 86  ? 1.17708  0.447185 0.665826 0.134897    0.0737545   0.155779    98  LYS   A N    
3029 C CA   . LYS   B 86  ? 1.20312  0.433973 0.695875 0.140496    0.0871806   0.17321     98  LYS   A CA   
3030 C C    . LYS   B 86  ? 1.18463  0.400009 0.696497 0.122957    0.111695    0.159011    98  LYS   A C    
3031 O O    . LYS   B 86  ? 1.12836  0.363064 0.640195 0.106767    0.11822     0.143706    98  LYS   A O    
3032 C CB   . LYS   B 86  ? 1.32932  0.534782 0.776683 0.145044    0.0870359   0.20131     98  LYS   A CB   
3033 C CG   . LYS   B 86  ? 1.38354  0.597856 0.800393 0.158931    0.0604086   0.219855    98  LYS   A CG   
3034 C CD   . LYS   B 86  ? 1.44766  0.665499 0.895811 0.178714    0.0437213   0.233157    98  LYS   A CD   
3035 C CE   . LYS   B 86  ? 1.50846  0.746686 0.931936 0.188141    0.0115962   0.249381    98  LYS   A CE   
3036 N NZ   . LYS   B 86  ? 1.55191  0.768663 0.910867 0.184544    0.00744962  0.268731    98  LYS   A NZ   
3037 H H    . LYS   B 86  ? 1.15217  0.425578 0.617924 0.128178    0.0757387   0.155218    98  LYS   A H    
3038 H HA   . LYS   B 86  ? 1.21997  0.448965 0.733097 0.152294    0.081145    0.176761    98  LYS   A HA   
3039 H HB2  . LYS   B 86  ? 1.31498  0.521296 0.744125 0.134001    0.0967159   0.197211    98  LYS   A HB2  
3040 H HB3  . LYS   B 86  ? 1.3466   0.524485 0.799657 0.14811     0.0975572   0.213087    98  LYS   A HB3  
3041 H HG2  . LYS   B 86  ? 1.36369  0.601856 0.772313 0.154327    0.0503114   0.207781    98  LYS   A HG2  
3042 H HG3  . LYS   B 86  ? 1.42722  0.621436 0.809766 0.159075    0.0638131   0.236387    98  LYS   A HG3  
3043 H HD2  . LYS   B 86  ? 1.47596  0.666027 0.927466 0.185158    0.0531325   0.248254    98  LYS   A HD2  
3044 H HD3  . LYS   B 86  ? 1.40832  0.64231  0.891099 0.178853    0.0450568   0.216833    98  LYS   A HD3  
3045 H HE2  . LYS   B 86  ? 1.50665  0.746655 0.952573 0.202136    0.00191231  0.263057    98  LYS   A HE2  
3046 H HE3  . LYS   B 86  ? 1.46291  0.728402 0.891603 0.182592    0.00183872  0.233508    98  LYS   A HE3  
3047 H HZ1  . LYS   B 86  ? 1.58072  0.770561 0.932554 0.186109    0.02179     0.280731    98  LYS   A HZ1  
3048 H HZ2  . LYS   B 86  ? 1.54132  0.763141 0.878483 0.173491    0.0117387   0.255799    98  LYS   A HZ2  
3049 H HZ3  . LYS   B 86  ? 1.57374  0.798079 0.920153 0.191727    -0.0135468  0.282503    98  LYS   A HZ3  
3050 N N    . LYS   B 87  ? 1.17933  0.359419 0.709866 0.12595     0.124416    0.1645      99  LYS   A N    
3051 C CA   . LYS   B 87  ? 1.20769  0.366753 0.754788 0.106149    0.145836    0.152014    99  LYS   A CA   
3052 C C    . LYS   B 87  ? 1.26965  0.424567 0.795462 0.0904387   0.158774    0.162424    99  LYS   A C    
3053 O O    . LYS   B 87  ? 1.29518  0.432495 0.790109 0.0989422   0.160261    0.187978    99  LYS   A O    
3054 C CB   . LYS   B 87  ? 1.25644  0.365717 0.816846 0.112703    0.158969    0.161803    99  LYS   A CB   
3055 C CG   . LYS   B 87  ? 1.30325  0.38505  0.880798 0.0887067   0.179423    0.145893    99  LYS   A CG   
3056 C CD   . LYS   B 87  ? 1.40515  0.4284   0.99232  0.0976112   0.193479    0.156153    99  LYS   A CD   
3057 C CE   . LYS   B 87  ? 1.50311  0.488949 1.10281  0.0718152   0.21321     0.141581    99  LYS   A CE   
3058 N NZ   . LYS   B 87  ? 1.42783  0.445242 1.04073  0.0529384   0.208419    0.107259    99  LYS   A NZ   
3059 H H    . LYS   B 87  ? 1.21399  0.382073 0.747597 0.140378    0.119146    0.176701    99  LYS   A H    
3060 H HA   . LYS   B 87  ? 1.18014  0.358714 0.743462 0.0977076   0.144569    0.131216    99  LYS   A HA   
3061 H HB2  . LYS   B 87  ? 1.26011  0.370907 0.834649 0.126168    0.152753    0.157992    99  LYS   A HB2  
3062 H HB3  . LYS   B 87  ? 1.2964   0.386493 0.839738 0.120309    0.160389    0.184269    99  LYS   A HB3  
3063 H HG2  . LYS   B 87  ? 1.30905  0.391974 0.87776  0.0751008   0.186322    0.151482    99  LYS   A HG2  
3064 H HG3  . LYS   B 87  ? 1.27806  0.378143 0.86908  0.0805666   0.17683     0.123836    99  LYS   A HG3  
3065 H HD2  . LYS   B 87  ? 1.40596  0.429859 1.00477  0.112472    0.188525    0.150366    99  LYS   A HD2  
3066 H HD3  . LYS   B 87  ? 1.43793  0.444958 1.01082  0.107665    0.194205    0.180453    99  LYS   A HD3  
3067 H HE2  . LYS   B 87  ? 1.51568  0.463085 1.12208  0.0797586   0.221686    0.143927    99  LYS   A HE2  
3068 H HE3  . LYS   B 87  ? 1.492    0.471505 1.08412  0.0589995   0.220454    0.152511    99  LYS   A HE3  
3069 H HZ1  . LYS   B 87  ? 1.41669  0.448606 1.03364  0.0656021   0.200677    0.0989623   99  LYS   A HZ1  
3070 H HZ2  . LYS   B 87  ? 1.40887  0.455912 1.01854  0.0418818   0.204002    0.10591     99  LYS   A HZ2  
3071 H HZ3  . LYS   B 87  ? 1.45966  0.451498 1.07986  0.0388298   0.218051    0.0956323   99  LYS   A HZ3  
3072 N N    . GLY   B 88  ? 1.19539  0.371776 0.73731  0.0685049   0.166817    0.143391    100 GLY   A N    
3073 C CA   . GLY   B 88  ? 1.18282  0.366827 0.715287 0.0534348   0.181025    0.15137     100 GLY   A CA   
3074 C C    . GLY   B 88  ? 1.17518  0.393447 0.683767 0.0590575   0.173886    0.15198     100 GLY   A C    
3075 O O    . GLY   B 88  ? 1.21054  0.437463 0.712918 0.0495012   0.188582    0.158059    100 GLY   A O    
3076 H H    . GLY   B 88  ? 1.17891  0.366809 0.739488 0.0631733   0.163571    0.125763    100 GLY   A H    
3077 H HA2  . GLY   B 88  ? 1.17888  0.370547 0.733837 0.0368361   0.18757     0.139378    100 GLY   A HA2  
3078 H HA3  . GLY   B 88  ? 1.22961  0.386039 0.749584 0.0548457   0.191139    0.169263    100 GLY   A HA3  
3079 N N    . GLU   B 89  ? 1.11923  0.355871 0.61584  0.0739653   0.153235    0.14575     101 GLU   A N    
3080 C CA   . GLU   B 89  ? 1.13472  0.396192 0.60521  0.0783949   0.145846    0.143898    101 GLU   A CA   
3081 C C    . GLU   B 89  ? 1.08911  0.38779  0.585791 0.0654764   0.148291    0.123158    101 GLU   A C    
3082 O O    . GLU   B 89  ? 0.967289 0.280008 0.499257 0.0559325   0.145324    0.106581    101 GLU   A O    
3083 C CB   . GLU   B 89  ? 1.08991  0.356869 0.542366 0.095441    0.120926    0.145314    101 GLU   A CB   
3084 C CG   . GLU   B 89  ? 1.11454  0.400353 0.534907 0.0982407   0.110871    0.141122    101 GLU   A CG   
3085 C CD   . GLU   B 89  ? 1.07603  0.371903 0.484725 0.11011     0.0832726   0.141231    101 GLU   A CD   
3086 O OE1  . GLU   B 89  ? 1.12144  0.401019 0.522276 0.121689    0.0715202   0.158544    101 GLU   A OE1  
3087 O OE2  . GLU   B 89  ? 1.09049  0.412379 0.501889 0.107656    0.0724751   0.125442    101 GLU   A OE2  
3088 H H    . GLU   B 89  ? 1.13199  0.364442 0.637995 0.0812797   0.144134    0.142345    101 GLU   A H    
3089 H HA   . GLU   B 89  ? 1.1486   0.397336 0.594863 0.0784678   0.156228    0.157236    101 GLU   A HA   
3090 H HB2  . GLU   B 89  ? 1.14123  0.386407 0.578833 0.103733    0.118683    0.161135    101 GLU   A HB2  
3091 H HB3  . GLU   B 89  ? 1.08226  0.361222 0.55998  0.0962949   0.113029    0.133601    101 GLU   A HB3  
3092 H HG2  . GLU   B 89  ? 1.06789  0.37381  0.503945 0.0910172   0.114584    0.127389    101 GLU   A HG2  
3093 H HG3  . GLU   B 89  ? 1.12832  0.399333 0.518603 0.098455    0.119768    0.152309    101 GLU   A HG3  
3094 N N    . ILE   B 90  ? 1.09625  0.407767 0.572804 0.0650856   0.156122    0.125769    102 ILE   A N    
3095 C CA   . ILE   B 90  ? 1.04854  0.39595  0.544731 0.0586958   0.156269    0.110528    102 ILE   A CA   
3096 C C    . ILE   B 90  ? 1.0638   0.416239 0.524997 0.0707879   0.144586    0.107326    102 ILE   A C    
3097 O O    . ILE   B 90  ? 1.0727   0.405502 0.491031 0.0773739   0.15274     0.118866    102 ILE   A O    
3098 C CB   . ILE   B 90  ? 1.05491  0.415043 0.569495 0.0470468   0.180003    0.115995    102 ILE   A CB   
3099 C CG1  . ILE   B 90  ? 1.12592  0.483368 0.678829 0.0294674   0.189225    0.117654    102 ILE   A CG1  
3100 C CG2  . ILE   B 90  ? 0.982389 0.380698 0.516203 0.0455797   0.177764    0.103523    102 ILE   A CG2  
3101 C CD1  . ILE   B 90  ? 1.16168  0.53489  0.741207 0.0153697   0.212278    0.127236    102 ILE   A CD1  
3102 H H    . ILE   B 90  ? 1.12264  0.418034 0.57105  0.0698047   0.162524    0.138268    102 ILE   A H    
3103 H HA   . ILE   B 90  ? 1.02628  0.387067 0.547428 0.0541407   0.147611    0.0988816   102 ILE   A HA   
3104 H HB   . ILE   B 90  ? 1.08895  0.433588 0.577124 0.0519686   0.191648    0.127916    102 ILE   A HB   
3105 H HG12 . ILE   B 90  ? 1.09022  0.461413 0.664833 0.0237416   0.178046    0.104531    102 ILE   A HG12 
3106 H HG13 . ILE   B 90  ? 1.1425   0.47245  0.682881 0.0319156   0.190445    0.125611    102 ILE   A HG13 
3107 H HG21 . ILE   B 90  ? 0.991905 0.402991 0.545455 0.0385173   0.191936    0.108088    102 ILE   A HG21 
3108 H HG22 . ILE   B 90  ? 0.965055 0.377707 0.518253 0.0418265   0.16457     0.0920865   102 ILE   A HG22 
3109 H HG23 . ILE   B 90  ? 0.997649 0.392321 0.504512 0.05543     0.175717    0.103277    102 ILE   A HG23 
3110 H HD11 . ILE   B 90  ? 1.1825   0.538537 0.74011  0.0202597   0.226409    0.141081    102 ILE   A HD11 
3111 H HD12 . ILE   B 90  ? 1.15381  0.525941 0.758961 0.00157359  0.213547    0.125711    102 ILE   A HD12 
3112 H HD13 . ILE   B 90  ? 1.12666  0.527843 0.720131 0.0149297   0.212194    0.121977    102 ILE   A HD13 
3113 N N    . ALA   B 91  ? 0.963861 0.33979  0.44101  0.0717823   0.12689     0.0914369   103 ALA   A N    
3114 C CA   . ALA   B 91  ? 0.95633  0.338382 0.40665  0.0793128   0.114625    0.0855147   103 ALA   A CA   
3115 C C    . ALA   B 91  ? 0.916408 0.327654 0.388499 0.0750349   0.115537    0.0720366   103 ALA   A C    
3116 O O    . ALA   B 91  ? 0.88925  0.324307 0.402001 0.0665392   0.115162    0.063922    103 ALA   A O    
3117 C CB   . ALA   B 91  ? 0.972114 0.352785 0.4167   0.0863368   0.0902774   0.0834947   103 ALA   A CB   
3118 H H    . ALA   B 91  ? 0.956208 0.342901 0.460308 0.0667112   0.122857    0.0839059   103 ALA   A H    
3119 H HA   . ALA   B 91  ? 0.990972 0.356598 0.409167 0.0829886   0.122242    0.0933891   103 ALA   A HA   
3120 H HB1  . ALA   B 91  ? 0.993377 0.355817 0.424329 0.0906968   0.0887783   0.0944553   103 ALA   A HB1  
3121 H HB2  . ALA   B 91  ? 0.940099 0.33533  0.414003 0.0836816   0.0851737   0.0755315   103 ALA   A HB2  
3122 H HB3  . ALA   B 91  ? 0.967984 0.351402 0.393712 0.0890749   0.0812547   0.0799217   103 ALA   A HB3  
3123 N N    . HIS   B 92  ? 0.990652 0.397755 0.432075 0.0808859   0.112827    0.0687662   104 HIS   A N    
3124 C CA   . HIS   B 92  ? 0.934881 0.364588 0.392707 0.0797      0.112144    0.0575793   104 HIS   A CA   
3125 C C    . HIS   B 92  ? 0.944142 0.377721 0.392298 0.0816928   0.0885736   0.047745    104 HIS   A C    
3126 O O    . HIS   B 92  ? 0.967393 0.380011 0.375943 0.0856667   0.0776452   0.0493951   104 HIS   A O    
3127 C CB   . HIS   B 92  ? 0.94687  0.368557 0.38563  0.084357    0.133447    0.0601485   104 HIS   A CB   
3128 C CG   . HIS   B 92  ? 0.9675   0.397026 0.429243 0.0818411   0.159142    0.0703811   104 HIS   A CG   
3129 N ND1  . HIS   B 92  ? 0.956747 0.376097 0.401603 0.0885544   0.184787    0.0764306   104 HIS   A ND1  
3130 C CD2  . HIS   B 92  ? 0.997058 0.439959 0.494394 0.0727862   0.164548    0.0765795   104 HIS   A CD2  
3131 C CE1  . HIS   B 92  ? 0.960998 0.394635 0.438341 0.0837424   0.20486     0.0876572   104 HIS   A CE1  
3132 N NE2  . HIS   B 92  ? 1.0062   0.452819 0.513895 0.0727344   0.191694    0.0876927   104 HIS   A NE2  
3133 H H    . HIS   B 92  ? 0.997537 0.385139 0.405225 0.085426    0.111234    0.0738342   104 HIS   A H    
3134 H HA   . HIS   B 92  ? 0.914147 0.363809 0.406322 0.0740067   0.113693    0.0549652   104 HIS   A HA   
3135 H HB2  . HIS   B 92  ? 0.98621  0.383872 0.384967 0.0888521   0.13358     0.0620566   104 HIS   A HB2  
3136 H HB3  . HIS   B 92  ? 0.935515 0.36926  0.383881 0.0851185   0.130328    0.0531496   104 HIS   A HB3  
3138 H HD2  . HIS   B 92  ? 0.968435 0.416662 0.481849 0.0670885   0.153344    0.0737944   104 HIS   A HD2  
3139 H HE1  . HIS   B 92  ? 0.992053 0.425311 0.470217 0.0874088   0.226023    0.0944793   104 HIS   A HE1  
3141 N N    . LEU   B 93  ? 0.841029 0.302504 0.323824 0.0774031   0.0808892   0.0381745   105 LEU   A N    
3142 C CA   . LEU   B 93  ? 0.856887 0.324678 0.336114 0.0776411   0.0612781   0.03029     105 LEU   A CA   
3143 C C    . LEU   B 93  ? 0.886591 0.364713 0.371286 0.0768783   0.0652701   0.0238676   105 LEU   A C    
3144 O O    . LEU   B 93  ? 0.885314 0.383081 0.399012 0.0746553   0.0758499   0.0243215   105 LEU   A O    
3145 C CB   . LEU   B 93  ? 0.844752 0.332463 0.35489  0.0746948   0.0477725   0.0258059   105 LEU   A CB   
3146 C CG   . LEU   B 93  ? 0.833781 0.31224  0.348807 0.0773918   0.0454296   0.0320296   105 LEU   A CG   
3147 C CD1  . LEU   B 93  ? 0.834468 0.329883 0.383127 0.0756795   0.0402408   0.0257306   105 LEU   A CD1  
3148 C CD2  . LEU   B 93  ? 0.892372 0.353525 0.376785 0.0837225   0.0314895   0.0396764   105 LEU   A CD2  
3149 H H    . LEU   B 93  ? 0.843412 0.320095 0.351313 0.0735219   0.0877326   0.0375151   105 LEU   A H    
3150 H HA   . LEU   B 93  ? 0.887488 0.337972 0.337848 0.0804453   0.0546883   0.0325517   105 LEU   A HA   
3151 H HB2  . LEU   B 93  ? 0.81408  0.318091 0.347125 0.0705314   0.0524502   0.0219062   105 LEU   A HB2  
3152 H HB3  . LEU   B 93  ? 0.832295 0.324181 0.338958 0.0748997   0.0359419   0.0222925   105 LEU   A HB3  
3153 H HG   . LEU   B 93  ? 0.857751 0.327109 0.371241 0.076398    0.0574234   0.0367294   105 LEU   A HG   
3154 H HD11 . LEU   B 93  ? 0.811946 0.317385 0.375928 0.0698638   0.0473175   0.020574    105 LEU   A HD11 
3155 H HD12 . LEU   B 93  ? 0.840136 0.32475  0.390369 0.0792278   0.0407798   0.0306065   105 LEU   A HD12 
3156 H HD13 . LEU   B 93  ? 0.817007 0.32319  0.369855 0.0767048   0.0299724   0.0223554   105 LEU   A HD13 
3157 H HD21 . LEU   B 93  ? 0.907226 0.352225 0.363948 0.084606    0.036897    0.0434886   105 LEU   A HD21 
3158 H HD22 . LEU   B 93  ? 0.875622 0.346521 0.361912 0.0830094   0.0193331   0.0355044   105 LEU   A HD22 
3159 H HD23 . LEU   B 93  ? 0.892195 0.348201 0.382302 0.0872846   0.0291546   0.0456804   105 LEU   A HD23 
3160 N N    . LEU   B 94  ? 0.866176 0.329494 0.322602 0.078064    0.0558826   0.0192899   106 LEU   A N    
3161 C CA   . LEU   B 94  ? 0.885523 0.354686 0.348339 0.0773731   0.0572855   0.0130517   106 LEU   A CA   
3162 C C    . LEU   B 94  ? 0.810266 0.290869 0.281826 0.0714739   0.0356667   0.00714909  106 LEU   A C    
3163 O O    . LEU   B 94  ? 0.841523 0.310565 0.292042 0.0693426   0.0203617   0.006545    106 LEU   A O    
3164 C CB   . LEU   B 94  ? 0.962773 0.399129 0.385073 0.0824671   0.0699508   0.011239    106 LEU   A CB   
3165 C CG   . LEU   B 94  ? 0.896639 0.32909  0.320495 0.0826792   0.0709669   0.00481075  106 LEU   A CG   
3166 C CD1  . LEU   B 94  ? 0.897319 0.356582 0.363707 0.0874107   0.0865014   0.010924    106 LEU   A CD1  
3167 C CD2  . LEU   B 94  ? 1.04683  0.435738 0.418956 0.0856454   0.0789081   -0.00121409 106 LEU   A CD2  
3168 H H    . LEU   B 94  ? 0.903379 0.35174  0.335825 0.0786738   0.0479207   0.0204613   106 LEU   A H    
3169 H HA   . LEU   B 94  ? 0.851733 0.339385 0.341839 0.0771632   0.0649191   0.0146741   106 LEU   A HA   
3170 H HB2  . LEU   B 94  ? 0.945544 0.379467 0.369243 0.0869821   0.0868828   0.0161707   106 LEU   A HB2  
3171 H HB3  . LEU   B 94  ? 0.966914 0.383399 0.357339 0.0813162   0.0620979   0.0100049   106 LEU   A HB3  
3172 H HG   . LEU   B 94  ? 0.915245 0.35785  0.348631 0.0768292   0.0550956   0.0014011   106 LEU   A HG   
3173 H HD11 . LEU   B 94  ? 0.857144 0.341915 0.351287 0.0829425   0.078348    0.0125466   106 LEU   A HD11 
3174 H HD12 . LEU   B 94  ? 0.891561 0.346149 0.358983 0.0895339   0.089178    0.00904126  106 LEU   A HD12 
3175 H HD13 . LEU   B 94  ? 0.89899  0.354508 0.363989 0.0924963   0.101966    0.0158676   106 LEU   A HD13 
3176 H HD21 . LEU   B 94  ? 1.03445  0.409856 0.380398 0.0803184   0.0646999   -0.00459539 106 LEU   A HD21 
3177 H HD22 . LEU   B 94  ? 1.03355  0.411299 0.393962 0.0920713   0.0964612   0.00234052  106 LEU   A HD22 
3178 H HD23 . LEU   B 94  ? 1.01757  0.401141 0.392461 0.0862213   0.0813348   -0.00505689 106 LEU   A HD23 
3179 N N    . ILE   B 95  ? 0.839876 0.34662  0.345171 0.0682854   0.034417    0.00496639  107 ILE   A N    
3180 C CA   . ILE   B 95  ? 0.804613 0.331578 0.330391 0.0625539   0.0185731   0.00173972  107 ILE   A CA   
3181 C C    . ILE   B 95  ? 0.818601 0.351025 0.351367 0.0589006   0.0171547   -0.00099185 107 ILE   A C    
3182 O O    . ILE   B 95  ? 0.782261 0.326949 0.331577 0.0603555   0.0271053   0.00149076  107 ILE   A O    
3183 C CB   . ILE   B 95  ? 0.769033 0.321019 0.32647  0.0612069   0.0216494   0.00225738  107 ILE   A CB   
3184 C CG1  . ILE   B 95  ? 0.809869 0.351179 0.362094 0.0647552   0.0258187   0.006066    107 ILE   A CG1  
3185 C CG2  . ILE   B 95  ? 0.700401 0.273497 0.278839 0.0567346   0.01097     -0.00129311 107 ILE   A CG2  
3186 C CD1  . ILE   B 95  ? 0.779953 0.336506 0.357798 0.0612947   0.0335019   0.00470389  107 ILE   A CD1  
3187 H H    . ILE   B 95  ? 0.812994 0.326067 0.329136 0.0699201   0.0443954   0.0065577   107 ILE   A H    
3188 H HA   . ILE   B 95  ? 0.821275 0.341388 0.336072 0.0616566   0.00812542  0.00162275  107 ILE   A HA   
3189 H HB   . ILE   B 95  ? 0.756105 0.316137 0.323176 0.0605646   0.029589    0.00307487  107 ILE   A HB   
3190 H HG12 . ILE   B 95  ? 0.807647 0.345431 0.355901 0.066172    0.0167544   0.00690206  107 ILE   A HG12 
3191 H HG13 . ILE   B 95  ? 0.81752  0.343479 0.352263 0.0674566   0.0327898   0.00920188  107 ILE   A HG13 
3192 H HG21 . ILE   B 95  ? 0.704857 0.287729 0.297119 0.0565266   0.0133415   -0.00239983 107 ILE   A HG21 
3193 H HG22 . ILE   B 95  ? 0.723828 0.292164 0.296016 0.0567898   0.00170466  -0.00091971 107 ILE   A HG22 
3194 H HG23 . ILE   B 95  ? 0.705772 0.286952 0.290102 0.053865    0.0117144   -0.00219942 107 ILE   A HG23 
3195 H HD11 . ILE   B 95  ? 0.775159 0.340122 0.360218 0.0586575   0.0395749   0.00491449  107 ILE   A HD11 
3196 H HD12 . ILE   B 95  ? 0.794944 0.340567 0.368506 0.0630591   0.0376936   0.00779615  107 ILE   A HD12 
3197 H HD13 . ILE   B 95  ? 0.77152  0.339412 0.36223  0.0594282   0.0283893   0.0008601   107 ILE   A HD13 
3198 N N    . LYS   B 96  ? 0.798324 0.323474 0.321242 0.053142    0.00334586  -0.00430059 108 LYS   A N    
3199 C CA   . LYS   B 96  ? 0.776839 0.3035   0.306433 0.0478695   0.00141854  -0.00589346 108 LYS   A CA   
3200 C C    . LYS   B 96  ? 0.692683 0.254643 0.258147 0.0439186   -0.00157061 -0.00384806 108 LYS   A C    
3201 O O    . LYS   B 96  ? 0.71499  0.294861 0.295914 0.0442851   -0.00496517 -0.00384158 108 LYS   A O    
3202 C CB   . LYS   B 96  ? 0.765176 0.270178 0.271145 0.03944     -0.0134198  -0.0104839  108 LYS   A CB   
3203 C CG   . LYS   B 96  ? 0.883467 0.345958 0.340806 0.0415021   -0.0105619  -0.0150904  108 LYS   A CG   
3204 C CD   . LYS   B 96  ? 0.864957 0.299866 0.305966 0.0469102   0.00804189  -0.0176798  108 LYS   A CD   
3205 C CE   . LYS   B 96  ? 0.993234 0.381689 0.382722 0.0504696   0.0174606   -0.0239754  108 LYS   A CE   
3206 N NZ   . LYS   B 96  ? 1.04493  0.441486 0.43102  0.0589776   0.0252736   -0.0184217  108 LYS   A NZ   
3207 H H    . LYS   B 96  ? 0.812596 0.33182  0.325129 0.0518167   -0.00572212 -0.00457156 108 LYS   A H    
3208 H HA   . LYS   B 96  ? 0.768398 0.286306 0.293772 0.0519696   0.0123381   -0.0047163  108 LYS   A HA   
3209 H HB2  . LYS   B 96  ? 0.783102 0.301555 0.298544 0.0360602   -0.0249168  -0.00950634 108 LYS   A HB2  
3210 H HB3  . LYS   B 96  ? 0.789    0.293589 0.301057 0.034617    -0.0143634  -0.0112543  108 LYS   A HB3  
3211 H HG2  . LYS   B 96  ? 0.861509 0.323686 0.312384 0.0471695   -0.00652293 -0.0126683  108 LYS   A HG2  
3212 H HG3  . LYS   B 96  ? 0.878848 0.331361 0.321202 0.0335784   -0.0245709  -0.0182026  108 LYS   A HG3  
3213 H HD2  . LYS   B 96  ? 0.890697 0.323975 0.338393 0.0411302   0.00396957  -0.0192252  108 LYS   A HD2  
3214 H HD3  . LYS   B 96  ? 0.868293 0.318648 0.329435 0.0541625   0.0197719   -0.0127077  108 LYS   A HD3  
3215 H HE2  . LYS   B 96  ? 1.01485  0.385646 0.379463 0.0416994   0.00434304  -0.0296195  108 LYS   A HE2  
3216 H HE3  . LYS   B 96  ? 0.999957 0.372459 0.384846 0.0561047   0.032208    -0.0248833  108 LYS   A HE3  
3217 H HZ1  . LYS   B 96  ? 1.03152  0.428454 0.406898 0.0545586   0.0124498   -0.0185857  108 LYS   A HZ1  
3218 H HZ2  . LYS   B 96  ? 0.99043  0.412338 0.406889 0.0626369   0.0298137   -0.0130532  108 LYS   A HZ2  
3219 H HZ3  . LYS   B 96  ? 1.0512   0.425663 0.414657 0.0648543   0.0391089   -0.0196132  108 LYS   A HZ3  
3220 N N    . PRO   B 97  ? 0.745138 0.314374 0.321723 0.0400362   0.00036436  -0.00182473 109 PRO   A N    
3221 C CA   . PRO   B 97  ? 0.690421 0.291002 0.293815 0.0360605   0.00043251  0.00063194  109 PRO   A CA   
3222 C C    . PRO   B 97  ? 0.700987 0.319165 0.32007  0.0314767   -0.00810946 -0.00136262 109 PRO   A C    
3223 O O    . PRO   B 97  ? 0.657745 0.297276 0.293142 0.0321986   -0.00358883 -0.00208447 109 PRO   A O    
3224 C CB   . PRO   B 97  ? 0.715322 0.312552 0.320834 0.0319508   0.00221032  0.0054466   109 PRO   A CB   
3225 C CG   . PRO   B 97  ? 0.733149 0.294624 0.314832 0.0322611   0.00135596  0.003002    109 PRO   A CG   
3226 C CD   . PRO   B 97  ? 0.730465 0.27486  0.291867 0.040127    0.00504811  -0.00103107 109 PRO   A CD   
3227 H HA   . PRO   B 97  ? 0.69165  0.302166 0.300813 0.0391707   0.00635683  0.00159233  109 PRO   A HA   
3228 H HB2  . PRO   B 97  ? 0.702464 0.311692 0.318831 0.0258131   -0.00185964 0.00625053  109 PRO   A HB2  
3229 H HB3  . PRO   B 97  ? 0.700236 0.305204 0.310904 0.0350784   0.00851828  0.00978694  109 PRO   A HB3  
3230 H HG2  . PRO   B 97  ? 0.74362  0.299933 0.322945 0.0248493   -0.00725658 0.00049763  109 PRO   A HG2  
3231 H HG3  . PRO   B 97  ? 0.740156 0.293007 0.320516 0.034628    0.00776708  0.00691936  109 PRO   A HG3  
3232 H HD2  . PRO   B 97  ? 0.765672 0.287921 0.306886 0.0378213   0.00053043  -0.00520599 109 PRO   A HD2  
3233 H HD3  . PRO   B 97  ? 0.742819 0.283531 0.303127 0.0469705   0.0153042   0.00188619  109 PRO   A HD3  
3234 N N    . GLU   B 98  ? 0.692502 0.301575 0.30667  0.0269928   -0.0200681  -0.00223546 110 GLU   A N    
3235 C CA   . GLU   B 98  ? 0.710087 0.342072 0.348627 0.0231454   -0.0288897  -0.00064735 110 GLU   A CA   
3236 C C    . GLU   B 98  ? 0.730115 0.37177  0.377957 0.0325307   -0.0266201  -0.0009631  110 GLU   A C    
3237 O O    . GLU   B 98  ? 0.698851 0.364234 0.374326 0.0338732   -0.0259628  0.00087028  110 GLU   A O    
3238 C CB   . GLU   B 98  ? 0.850468 0.473243 0.483457 0.0139942   -0.0468999  0.00017597  110 GLU   A CB   
3239 C CG   . GLU   B 98  ? 0.913704 0.51829  0.534961 0.00280025  -0.0484309  -0.00092757 110 GLU   A CG   
3240 C CD   . GLU   B 98  ? 0.939003 0.50552  0.525473 0.00554586  -0.0401805  -0.00492109 110 GLU   A CD   
3241 O OE1  . GLU   B 98  ? 0.844391 0.391395 0.405396 0.0135233   -0.0380748  -0.0082377  110 GLU   A OE1  
3242 O OE2  . GLU   B 98  ? 0.891894 0.447962 0.477955 0.00154732  -0.0332957  -0.00316472 110 GLU   A OE2  
3243 H H    . GLU   B 98  ? 0.724019 0.312574 0.319671 0.0261589   -0.0229728  -0.00354643 110 GLU   A H    
3244 H HA   . GLU   B 98  ? 0.71714  0.365107 0.371514 0.0198614   -0.0242746  0.0009876   110 GLU   A HA   
3245 H HB2  . GLU   B 98  ? 0.844686 0.451335 0.458198 0.0169946   -0.051989   -0.00121811 110 GLU   A HB2  
3246 H HB3  . GLU   B 98  ? 0.822701 0.466551 0.478976 0.0118947   -0.0525769  0.0033642   110 GLU   A HB3  
3247 H HG2  . GLU   B 98  ? 0.918367 0.52149  0.540705 -0.0059633  -0.0613412  -0.00080658 110 GLU   A HG2  
3248 H HG3  . GLU   B 98  ? 0.889326 0.509926 0.528921 0.00046219  -0.0422664  0.00207069  110 GLU   A HG3  
3249 N N    . TYR   B 99  ? 0.714504 0.337397 0.341829 0.0395645   -0.0218525  -0.0025656  111 TYR   A N    
3250 C CA   . TYR   B 99  ? 0.758531 0.384776 0.393796 0.0479195   -0.0178793  -0.00217481 111 TYR   A CA   
3251 C C    . TYR   B 99  ? 0.658095 0.287131 0.29559  0.0495268   -0.00284756 -0.0063608  111 TYR   A C    
3252 O O    . TYR   B 99  ? 0.676377 0.300057 0.315439 0.0545822   0.00310514  -0.00758774 111 TYR   A O    
3253 C CB   . TYR   B 99  ? 0.748404 0.351411 0.35918  0.0521093   -0.0264376  0.00150402  111 TYR   A CB   
3254 C CG   . TYR   B 99  ? 0.771655 0.380838 0.386713 0.0476565   -0.0461355  0.00606488  111 TYR   A CG   
3255 C CD1  . TYR   B 99  ? 0.751753 0.379461 0.392999 0.0532735   -0.0540735  0.0130184   111 TYR   A CD1  
3256 C CD2  . TYR   B 99  ? 0.861741 0.4575   0.456157 0.0373423   -0.0568481  0.00390363  111 TYR   A CD2  
3257 C CE1  . TYR   B 99  ? 0.82447  0.462285 0.472842 0.0483088   -0.0755539  0.0200104   111 TYR   A CE1  
3258 C CE2  . TYR   B 99  ? 0.833756 0.435407 0.431067 0.0291838   -0.0781021  0.00768983  111 TYR   A CE2  
3259 C CZ   . TYR   B 99  ? 0.85997  0.486023 0.485999 0.0344233   -0.0888469  0.0167785   111 TYR   A CZ   
3260 O OH   . TYR   B 99  ? 0.786902 0.424705 0.420538 0.0257324   -0.113319   0.0233864   111 TYR   A OH   
3261 H H    . TYR   B 99  ? 0.737886 0.344716 0.347148 0.0393709   -0.0199766  -0.00333651 111 TYR   A H    
3262 H HA   . TYR   B 99  ? 0.719999 0.361803 0.375302 0.0487913   -0.0205686  -0.00066238 111 TYR   A HA   
3263 H HB2  . TYR   B 99  ? 0.767011 0.353692 0.356763 0.0509608   -0.0232956  6.595e-05   111 TYR   A HB2  
3264 H HB3  . TYR   B 99  ? 0.758481 0.359586 0.37247  0.0580614   -0.0224174  0.0030758   111 TYR   A HB3  
3265 H HD1  . TYR   B 99  ? 0.762768 0.393744 0.415197 0.0607997   -0.0455265  0.0137845   111 TYR   A HD1  
3266 H HD2  . TYR   B 99  ? 0.835324 0.417132 0.414154 0.035504    -0.0495829  -5.735e-05  111 TYR   A HD2  
3267 H HE1  . TYR   B 99  ? 0.813297 0.466474 0.483553 0.0535784   -0.0812687  0.0269862   111 TYR   A HE1  
3268 H HE2  . TYR   B 99  ? 0.867564 0.455808 0.447387 0.0204187   -0.0856137  0.0047474   111 TYR   A HE2  
3270 N N    . ALA   B 100 ? 0.69183  0.328327 0.32906  0.0439642   0.00211589  -0.00759256 112 ALA   A N    
3271 C CA   . ALA   B 100 ? 0.696077 0.339925 0.335123 0.0420525   0.011983    -0.010597   112 ALA   A CA   
3272 C C    . ALA   B 100 ? 0.641657 0.30582  0.289978 0.0358701   0.0149994   -0.011858   112 ALA   A C    
3273 O O    . ALA   B 100 ? 0.693508 0.367192 0.35247  0.0363276   0.0188294   -0.0159095  112 ALA   A O    
3274 C CB   . ALA   B 100 ? 0.722404 0.356318 0.349729 0.0425651   0.0152018   -0.00705624 112 ALA   A CB   
3275 H H    . ALA   B 100 ? 0.685449 0.322277 0.321104 0.0405759   -0.00167895 -0.00586111 112 ALA   A H    
3276 H HA   . ALA   B 100 ? 0.690685 0.332248 0.332628 0.0443945   0.0152895   -0.0135964  112 ALA   A HA   
3277 H HB1  . ALA   B 100 ? 0.723008 0.34407  0.343087 0.0462763   0.0161625   -0.00652082 112 ALA   A HB1  
3278 H HB2  . ALA   B 100 ? 0.71701  0.347791 0.340121 0.0422257   0.0131139   -0.00401121 112 ALA   A HB2  
3279 H HB3  . ALA   B 100 ? 0.709438 0.352605 0.341044 0.0395175   0.0190153   -0.0076371  112 ALA   A HB3  
3280 N N    . TYR   B 101 ? 0.656712 0.326633 0.300406 0.0314363   0.0153796   -0.00737503 113 TYR   A N    
3281 C CA   . TYR   B 101 ? 0.628947 0.31675  0.274924 0.0249155   0.0182346   -0.00615775 113 TYR   A CA   
3282 C C    . TYR   B 101 ? 0.649743 0.340159 0.299188 0.0219471   0.015352    0.00156674  113 TYR   A C    
3283 O O    . TYR   B 101 ? 0.613716 0.316883 0.262752 0.0167734   0.0183918   0.00528897  113 TYR   A O    
3284 C CB   . TYR   B 101 ? 0.614075 0.309177 0.253356 0.0210815   0.0185812   -0.00312555 113 TYR   A CB   
3285 C CG   . TYR   B 101 ? 0.610659 0.303231 0.247476 0.0192481   0.0213605   -0.0118388  113 TYR   A CG   
3286 C CD1  . TYR   B 101 ? 0.671174 0.367539 0.302258 0.0137534   0.0263107   -0.0218472  113 TYR   A CD1  
3287 C CD2  . TYR   B 101 ? 0.621846 0.302724 0.260623 0.0232734   0.021377    -0.0106615  113 TYR   A CD2  
3288 C CE1  . TYR   B 101 ? 0.710049 0.397175 0.337094 0.0103098   0.0293829   -0.0310763  113 TYR   A CE1  
3289 C CE2  . TYR   B 101 ? 0.64391  0.320339 0.282175 0.0193827   0.0243359   -0.0172107  113 TYR   A CE2  
3290 C CZ   . TYR   B 101 ? 0.614817 0.292585 0.2472   0.012268    0.0275532   -0.0280972  113 TYR   A CZ   
3291 O OH   . TYR   B 101 ? 0.666075 0.331509 0.296423 0.00703538  0.0313107   -0.0362332  113 TYR   A OH   
3292 H H    . TYR   B 101 ? 0.649786 0.311675 0.288096 0.0332076   0.0144283   -0.00388938 113 TYR   A H    
3293 H HA   . TYR   B 101 ? 0.635925 0.329474 0.285273 0.024166    0.0223061   -0.0116026  113 TYR   A HA   
3294 H HB2  . TYR   B 101 ? 0.615686 0.305532 0.255257 0.024045    0.016598    0.00299079  113 TYR   A HB2  
3295 H HB3  . TYR   B 101 ? 0.619261 0.325475 0.255809 0.0163368   0.0190959   -0.00091953 113 TYR   A HB3  
3296 H HD1  . TYR   B 101 ? 0.667276 0.370864 0.29546  0.0114908   0.0287974   -0.0226575  113 TYR   A HD1  
3297 H HD2  . TYR   B 101 ? 0.621208 0.296785 0.260738 0.027672    0.0203761   -0.00474679 113 TYR   A HD2  
3298 H HE1  . TYR   B 101 ? 0.69078  0.376297 0.310436 0.00606066  0.033953    -0.0394426  113 TYR   A HE1  
3299 H HE2  . TYR   B 101 ? 0.632591 0.301967 0.273137 0.0214737   0.0255544   -0.0148476  113 TYR   A HE2  
3301 N N    . GLY   B 102 ? 0.698207 0.373873 0.348059 0.0236853   0.00946053  0.00360167  114 GLY   A N    
3302 C CA   . GLY   B 102 ? 0.666272 0.339725 0.32115  0.0178012   0.00556483  0.00885125  114 GLY   A CA   
3303 C C    . GLY   B 102 ? 0.70244  0.372039 0.351768 0.0152059   0.00821596  0.0180389   114 GLY   A C    
3304 O O    . GLY   B 102 ? 0.703302 0.371514 0.345778 0.019831    0.0111457   0.0225799   114 GLY   A O    
3305 H H    . GLY   B 102 ? 0.679676 0.344025 0.324489 0.0276188   0.00749715  0.00137503  114 GLY   A H    
3306 H HA2  . GLY   B 102 ? 0.688744 0.348283 0.33986  0.0182665   -0.00024046 0.00742008  114 GLY   A HA2  
3307 H HA3  . GLY   B 102 ? 0.678404 0.365954 0.344925 0.0146235   0.00697912  0.00840366  114 GLY   A HA3  
3308 N N    . SER   B 103 ? 0.691515 0.363442 0.348696 0.0072558   0.00738771  0.0231234   115 SER   A N    
3309 C CA   . SER   B 103 ? 0.739739 0.403376 0.392361 0.00483792  0.0101465   0.0342516   115 SER   A CA   
3310 C C    . SER   B 103 ? 0.649086 0.335933 0.300082 0.00425384  0.0160741   0.0411977   115 SER   A C    
3311 O O    . SER   B 103 ? 0.654305 0.337931 0.299611 0.00642814  0.01705     0.0527695   115 SER   A O    
3312 C CB   . SER   B 103 ? 0.742608 0.395155 0.402528 -0.00567357 0.00703686  0.037696    115 SER   A CB   
3313 O OG   . SER   B 103 ? 0.875367 0.55493  0.552534 -0.0134489  0.0105279   0.0397832   115 SER   A OG   
3314 H H    . SER   B 103 ? 0.702016 0.380984 0.369265 0.00344932  0.00538095  0.0209613   115 SER   A H    
3315 H HA   . SER   B 103 ? 0.71871  0.366466 0.363009 0.0105706   0.00995689  0.0351893   115 SER   A HA   
3316 H HB2  . SER   B 103 ? 0.78765  0.427428 0.442767 -0.00634501 0.00933206  0.0451863   115 SER   A HB2  
3317 H HB3  . SER   B 103 ? 0.780308 0.419466 0.437968 -0.00675467 0.00092356  0.0315311   115 SER   A HB3  
3319 N N    . ALA   B 104 ? 0.649756 0.358248 0.303334 0.00172177  0.020288    0.0348426   116 ALA   A N    
3320 C CA   . ALA   B 104 ? 0.683884 0.409678 0.325434 -0.00101826 0.0250528   0.0390942   116 ALA   A CA   
3321 C C    . ALA   B 104 ? 0.647905 0.375869 0.279239 0.00320363  0.0202323   0.0382342   116 ALA   A C    
3322 O O    . ALA   B 104 ? 0.646541 0.386965 0.266144 -0.00016533 0.018384    0.0460668   116 ALA   A O    
3323 C CB   . ALA   B 104 ? 0.775882 0.517736 0.418181 -0.00458104 0.0345106   0.0297408   116 ALA   A CB   
3324 H H    . ALA   B 104 ? 0.649187 0.360445 0.310472 0.00172842  0.0203291   0.0279969   116 ALA   A H    
3325 H HA   . ALA   B 104 ? 0.695544 0.421323 0.334715 -0.00415894 0.0260092   0.0499359   116 ALA   A HA   
3326 H HB1  . ALA   B 104 ? 0.748579 0.493621 0.40239  -0.00742312 0.0381721   0.0322247   116 ALA   A HB1  
3327 H HB2  . ALA   B 104 ? 0.740713 0.480631 0.385987 -0.00074222 0.0341575   0.0200481   116 ALA   A HB2  
3328 H HB3  . ALA   B 104 ? 0.757321 0.507324 0.385528 -0.00781916 0.0379673   0.0315007   116 ALA   A HB3  
3329 N N    . GLY   B 105 ? 0.659765 0.378531 0.295706 0.00888365  0.017751    0.0289737   117 GLY   A N    
3330 C CA   . GLY   B 105 ? 0.653235 0.375498 0.286016 0.0113261   0.0144287   0.0270797   117 GLY   A CA   
3331 C C    . GLY   B 105 ? 0.656077 0.391991 0.277501 0.003812    0.0159526   0.0176452   117 GLY   A C    
3332 O O    . GLY   B 105 ? 0.661956 0.398819 0.279637 0.00119152  0.0228815   0.00899501  117 GLY   A O    
3333 H H    . GLY   B 105 ? 0.649464 0.359876 0.291447 0.01065     0.0178385   0.024274    117 GLY   A H    
3334 H HA2  . GLY   B 105 ? 0.647769 0.359366 0.284774 0.0159852   0.0143412   0.0221446   117 GLY   A HA2  
3335 H HA3  . GLY   B 105 ? 0.656801 0.381964 0.290451 0.0128471   0.011598    0.0374069   117 GLY   A HA3  
3336 N N    . SER   B 106 ? 0.667705 0.41306  0.285134 0.00015971  0.00996007  0.0193868   118 SER   A N    
3337 C CA   . SER   B 106 ? 0.703576 0.456835 0.304659 -0.0105366  0.00904402  0.00877329  118 SER   A CA   
3338 C C    . SER   B 106 ? 0.713408 0.485928 0.312586 -0.017629   -0.00357294 0.0203392   118 SER   A C    
3339 O O    . SER   B 106 ? 0.698451 0.475731 0.306577 -0.0208558  -0.0091678  0.0187539   118 SER   A O    
3340 C CB   . SER   B 106 ? 0.682424 0.421625 0.285814 -0.0101962  0.0137725   -0.00779624 118 SER   A CB   
3341 O OG   . SER   B 106 ? 0.700002 0.437969 0.281709 -0.0210358  0.0171992   -0.0216469  118 SER   A OG   
3342 H H    . SER   B 106 ? 0.66628  0.412664 0.291994 0.00394923  0.00629535  0.0275564   118 SER   A H    
3343 H HA   . SER   B 106 ? 0.707067 0.46229  0.295614 -0.0143617  0.0135559   0.00591196  118 SER   A HA   
3344 H HB2  . SER   B 106 ? 0.677088 0.406234 0.287541 -0.00331022 0.0192772   -0.0110644  118 SER   A HB2  
3345 H HB3  . SER   B 106 ? 0.679331 0.41903  0.291481 -0.00953496 0.00952931  -0.00495606 118 SER   A HB3  
3347 N N    . LEU   B 107 ? 0.70533  0.490368 0.298388 -0.0188281  -0.00842077 0.0358741   119 LEU   A N    
3348 C CA   . LEU   B 107 ? 0.789757 0.597888 0.384376 -0.0237824  -0.022783   0.0526953   119 LEU   A CA   
3349 C C    . LEU   B 107 ? 0.822592 0.641874 0.392725 -0.0418527  -0.0318687  0.0418231   119 LEU   A C    
3350 O O    . LEU   B 107 ? 0.859849 0.668761 0.399021 -0.0504347  -0.0247746  0.0263025   119 LEU   A O    
3351 C CB   . LEU   B 107 ? 0.729011 0.544394 0.317076 -0.0210798  -0.0251012  0.0731555   119 LEU   A CB   
3352 C CG   . LEU   B 107 ? 0.732832 0.532687 0.343661 -0.00537185 -0.0174361  0.0848902   119 LEU   A CG   
3353 C CD1  . LEU   B 107 ? 0.80017  0.604807 0.399787 -0.00620431 -0.0191552  0.104645    119 LEU   A CD1  
3354 C CD2  . LEU   B 107 ? 0.748111 0.55028  0.389248 0.00669511  -0.020097   0.0957822   119 LEU   A CD2  
3355 H H    . LEU   B 107 ? 0.725922 0.505776 0.314939 -0.0164902  -0.00281681 0.0376269   119 LEU   A H    
3356 H HA   . LEU   B 107 ? 0.748798 0.559829 0.364815 -0.0175334  -0.0251048  0.0587795   119 LEU   A HA   
3357 H HB2  . LEU   B 107 ? 0.762025 0.573379 0.32926  -0.02677    -0.0200354  0.0671283   119 LEU   A HB2  
3358 H HB3  . LEU   B 107 ? 0.760617 0.593906 0.348612 -0.0248125  -0.0364827  0.0855204   119 LEU   A HB3  
3359 H HG   . LEU   B 107 ? 0.734367 0.518375 0.344936 -0.0033663  -0.0086448  0.0731996   119 LEU   A HG   
3360 H HD11 . LEU   B 107 ? 0.794726 0.598129 0.37492  -0.0136601  -0.0149715  0.0979486   119 LEU   A HD11 
3361 H HD12 . LEU   B 107 ? 0.781006 0.572179 0.392505 0.00211548  -0.01381    0.111671    119 LEU   A HD12 
3362 H HD13 . LEU   B 107 ? 0.795521 0.61718  0.395265 -0.00781395 -0.02937    0.117776    119 LEU   A HD13 
3363 H HD21 . LEU   B 107 ? 0.728637 0.525457 0.375423 0.00713566  -0.0172195  0.0839233   119 LEU   A HD21 
3364 H HD22 . LEU   B 107 ? 0.747408 0.569504 0.393884 0.00467299  -0.0295705  0.107903    119 LEU   A HD22 
3365 H HD23 . LEU   B 107 ? 0.739376 0.527948 0.388702 0.0158469   -0.0144601  0.103014    119 LEU   A HD23 
3366 N N    . PRO   B 108 ? 0.820098 0.66199  0.402738 -0.0487522  -0.0478849  0.0517959   120 PRO   A N    
3367 C CA   . PRO   B 108 ? 0.781153 0.638895 0.402826 -0.0362813  -0.0530447  0.0736357   120 PRO   A CA   
3368 C C    . PRO   B 108 ? 0.738556 0.58787  0.390402 -0.028098   -0.0450779  0.0678208   120 PRO   A C    
3369 O O    . PRO   B 108 ? 0.716832 0.575391 0.399931 -0.0151867  -0.0439317  0.0849268   120 PRO   A O    
3370 C CB   . PRO   B 108 ? 0.911922 0.805287 0.53631  -0.0496497  -0.0753296  0.0887887   120 PRO   A CB   
3371 C CG   . PRO   B 108 ? 0.948677 0.836835 0.540343 -0.0720805  -0.0808485  0.0652862   120 PRO   A CG   
3372 C CD   . PRO   B 108 ? 0.980018 0.836308 0.537358 -0.0704352  -0.0630517  0.0453197   120 PRO   A CD   
3373 H HA   . PRO   B 108 ? 0.794285 0.647873 0.420087 -0.0260657  -0.0487532  0.0846346   120 PRO   A HA   
3374 H HB2  . PRO   B 108 ? 0.873866 0.781623 0.528896 -0.0450194  -0.0790752  0.0989801   120 PRO   A HB2  
3375 H HB3  . PRO   B 108 ? 0.899224 0.802092 0.514303 -0.0489493  -0.0813832  0.102625    120 PRO   A HB3  
3376 H HG2  . PRO   B 108 ? 0.942778 0.828675 0.549543 -0.0749922  -0.0796946  0.0571381   120 PRO   A HG2  
3377 H HG3  . PRO   B 108 ? 0.974975 0.881467 0.552597 -0.0846151  -0.0961485  0.071706    120 PRO   A HG3  
3378 H HD2  . PRO   B 108 ? 0.947122 0.788789 0.494138 -0.0771582  -0.0577984  0.0266912   120 PRO   A HD2  
3379 H HD3  . PRO   B 108 ? 0.963279 0.822917 0.494504 -0.0762111  -0.0662228  0.0482857   120 PRO   A HD3  
3380 N N    . LYS   B 109 ? 0.72166  0.551158 0.363836 -0.0337702  -0.0372364  0.0454021   121 LYS   A N    
3381 C CA   . LYS   B 109 ? 0.733487 0.552874 0.399472 -0.0269493  -0.0288924  0.0414208   121 LYS   A CA   
3382 C C    . LYS   B 109 ? 0.753486 0.552871 0.430724 -0.00622763 -0.0152655  0.0467339   121 LYS   A C    
3383 O O    . LYS   B 109 ? 0.68233  0.481662 0.38268  0.00406554  -0.00938371 0.0555134   121 LYS   A O    
3384 C CB   . LYS   B 109 ? 0.712429 0.514892 0.362377 -0.0402076  -0.0258963  0.018634    121 LYS   A CB   
3385 H H    . LYS   B 109 ? 0.743725 0.564499 0.363228 -0.0414135  -0.0358497  0.0330655   121 LYS   A H    
3386 H HA   . LYS   B 109 ? 0.727374 0.56686  0.413445 -0.0292131  -0.0357086  0.052492    121 LYS   A HA   
3389 N N    . ILE   B 110 ? 0.705175 0.484652 0.365011 -0.00084612 -0.00863997 0.0399135   122 ILE   A N    
3390 C CA   . ILE   B 110 ? 0.654789 0.410012 0.318692 0.0134444   0.00183682  0.0393739   122 ILE   A CA   
3391 C C    . ILE   B 110 ? 0.662895 0.41488  0.3231   0.0190138   0.00195177  0.0502058   122 ILE   A C    
3392 O O    . ILE   B 110 ? 0.690345 0.445692 0.335794 0.0120784   9.27e-06    0.0477809   122 ILE   A O    
3393 C CB   . ILE   B 110 ? 0.66593  0.399873 0.316524 0.0125538   0.00790019  0.0213451   122 ILE   A CB   
3394 C CG1  . ILE   B 110 ? 0.706799 0.437924 0.355387 0.00483586  0.00892074  0.0085912   122 ILE   A CG1  
3395 C CG2  . ILE   B 110 ? 0.659244 0.369956 0.31055  0.0241421   0.0140775   0.0213597   122 ILE   A CG2  
3396 C CD1  . ILE   B 110 ? 0.644808 0.376066 0.309304 0.00659499  0.0111578   0.0130153   122 ILE   A CD1  
3397 H H    . ILE   B 110 ? 0.713692 0.494968 0.358144 -0.00723369 -0.0108673  0.0355074   122 ILE   A H    
3398 H HA   . ILE   B 110 ? 0.661974 0.415678 0.338777 0.0195691   0.00506181  0.0443335   122 ILE   A HA   
3399 H HB   . ILE   B 110 ? 0.673262 0.409411 0.3142   0.00861127  0.00713698  0.0182889   122 ILE   A HB   
3400 H HG12 . ILE   B 110 ? 0.692077 0.434144 0.333912 -0.00478417 0.00442084  0.00574476  122 ILE   A HG12 
3401 H HG13 . ILE   B 110 ? 0.683337 0.400345 0.325755 0.00719074  0.0133673   -0.00015852 122 ILE   A HG13 
3402 H HG21 . ILE   B 110 ? 0.658792 0.359159 0.305081 0.0240975   0.0160905   0.0122837   122 ILE   A HG21 
3403 H HG22 . ILE   B 110 ? 0.659853 0.367135 0.318181 0.0295505   0.0167877   0.026468    122 ILE   A HG22 
3404 H HG23 . ILE   B 110 ? 0.661618 0.370138 0.31066  0.0258762   0.0135272   0.0257275   122 ILE   A HG23 
3405 H HD11 . ILE   B 110 ? 0.657619 0.373949 0.322823 0.0155626   0.0170684   0.013612    122 ILE   A HD11 
3406 H HD12 . ILE   B 110 ? 0.666929 0.396243 0.329334 -0.00099757 0.011046    0.00526896  122 ILE   A HD12 
3407 H HD13 . ILE   B 110 ? 0.660465 0.40825  0.336594 0.00608627  0.0074111   0.0236469   122 ILE   A HD13 
3408 N N    . PRO   B 111 ? 0.638816 0.380707 0.310603 0.0313118   0.00668618  0.0619935   123 PRO   A N    
3409 C CA   . PRO   B 111 ? 0.681463 0.413924 0.349722 0.0356058   0.00785464  0.0724638   123 PRO   A CA   
3410 C C    . PRO   B 111 ? 0.655321 0.36124  0.310534 0.0347402   0.0127303   0.0600828   123 PRO   A C    
3411 O O    . PRO   B 111 ? 0.6771   0.371961 0.327832 0.0344473   0.0148456   0.0464205   123 PRO   A O    
3412 C CB   . PRO   B 111 ? 0.645905 0.374049 0.332824 0.0501178   0.0131864   0.0892559   123 PRO   A CB   
3413 C CG   . PRO   B 111 ? 0.60478  0.330564 0.301235 0.0549883   0.0195818   0.0822131   123 PRO   A CG   
3414 C CD   . PRO   B 111 ? 0.648977 0.387464 0.338393 0.0417782   0.0134092   0.0676439   123 PRO   A CD   
3415 H HA   . PRO   B 111 ? 0.666388 0.41388  0.330225 0.0293652   0.00217786  0.0779892   123 PRO   A HA   
3416 H HB2  . PRO   B 111 ? 0.655977 0.362114 0.338334 0.0556284   0.0187689   0.0905329   123 PRO   A HB2  
3417 H HB3  . PRO   B 111 ? 0.650222 0.398458 0.346979 0.0501832   0.007657    0.102767    123 PRO   A HB3  
3418 H HG2  . PRO   B 111 ? 0.629283 0.329949 0.317912 0.06087     0.0274775   0.0759804   123 PRO   A HG2  
3419 H HG3  . PRO   B 111 ? 0.625812 0.365506 0.340705 0.0608666   0.0207622   0.0941439   123 PRO   A HG3  
3420 H HD2  . PRO   B 111 ? 0.630483 0.352731 0.31381  0.0435057   0.0187682   0.0576622   123 PRO   A HD2  
3421 H HD3  . PRO   B 111 ? 0.630686 0.390157 0.332509 0.0381995   0.00909457  0.072779    123 PRO   A HD3  
3422 N N    . SER   B 112 ? 0.612363 0.30835  0.263993 0.0342508   0.0136786   0.0676292   124 SER   A N    
3423 C CA   . SER   B 112 ? 0.604117 0.277491 0.248648 0.0309807   0.0160253   0.0591479   124 SER   A CA   
3424 C C    . SER   B 112 ? 0.649263 0.293979 0.28956  0.0385231   0.0197965   0.0509445   124 SER   A C    
3425 O O    . SER   B 112 ? 0.638514 0.2697   0.280946 0.0485932   0.0256404   0.0579202   124 SER   A O    
3426 C CB   . SER   B 112 ? 0.648268 0.312435 0.292683 0.0291314   0.0175053   0.0726729   124 SER   A CB   
3427 O OG   . SER   B 112 ? 0.652154 0.294777 0.293017 0.0227638   0.0182155   0.065471    124 SER   A OG   
3428 H H    . SER   B 112 ? 0.62825  0.332622 0.283086 0.0351522   0.0120326   0.0797847   124 SER   A H    
3429 H HA   . SER   B 112 ? 0.610492 0.292728 0.252576 0.0246546   0.0144981   0.0508995   124 SER   A HA   
3430 H HB2  . SER   B 112 ? 0.640488 0.322622 0.28386  0.0240984   0.0156461   0.0785195   124 SER   A HB2  
3431 H HB3  . SER   B 112 ? 0.65114  0.306006 0.299198 0.0369299   0.0200179   0.0817336   124 SER   A HB3  
3433 N N    . ASN   B 113 ? 0.618346 0.252745 0.251588 0.033903    0.0170628   0.0378376   125 ASN   A N    
3434 C CA   . ASN   B 113 ? 0.686639 0.288551 0.306121 0.0376246   0.0181812   0.0300344   125 ASN   A CA   
3435 C C    . ASN   B 113 ? 0.687692 0.283416 0.303068 0.0481799   0.0251123   0.028738    125 ASN   A C    
3436 O O    . ASN   B 113 ? 0.763309 0.329195 0.364437 0.054941    0.0319057   0.0271269   125 ASN   A O    
3437 C CB   . ASN   B 113 ? 0.712718 0.282997 0.323079 0.0373937   0.0208951   0.0336212   125 ASN   A CB   
3438 C CG   . ASN   B 113 ? 0.724432 0.296187 0.338157 0.0235894   0.0131862   0.0321827   125 ASN   A CG   
3439 O OD1  . ASN   B 113 ? 0.782886 0.372741 0.40284  0.0168656   0.00611992  0.0255717   125 ASN   A OD1  
3440 N ND2  . ASN   B 113 ? 0.797926 0.355202 0.412893 0.0197361   0.0157938   0.0407442   125 ASN   A ND2  
3441 H H    . ASN   B 113 ? 0.626423 0.27415  0.262341 0.0282712   0.0142661   0.0338348   125 ASN   A H    
3442 H HA   . ASN   B 113 ? 0.673089 0.275765 0.290245 0.0325456   0.012912    0.0227082   125 ASN   A HA   
3443 H HB2  . ASN   B 113 ? 0.719131 0.29084  0.335645 0.0426403   0.0260401   0.0433682   125 ASN   A HB2  
3444 H HB3  . ASN   B 113 ? 0.73203  0.27824  0.328177 0.0406589   0.0231546   0.0276981   125 ASN   A HB3  
3445 H HD21 . ASN   B 113 ? 0.780622 0.343531 0.401463 0.0107443   0.0123977   0.0421019   125 ASN   A HD21 
3446 H HD22 . ASN   B 113 ? 0.793102 0.33463  0.40428  0.0264123   0.0217894   0.0459127   125 ASN   A HD22 
3447 N N    . ALA   B 114 ? 0.671709 0.293108 0.297846 0.0483477   0.024813    0.0287458   126 ALA   A N    
3448 C CA   . ALA   B 114 ? 0.684313 0.304013 0.312284 0.056357    0.0326237   0.0298481   126 ALA   A CA   
3449 C C    . ALA   B 114 ? 0.694353 0.29385  0.304534 0.0569778   0.0330126   0.0192689   126 ALA   A C    
3450 O O    . ALA   B 114 ? 0.676632 0.282412 0.285396 0.0506535   0.0250234   0.0122203   126 ALA   A O    
3451 C CB   . ALA   B 114 ? 0.681653 0.334794 0.327673 0.0521571   0.030038    0.0337656   126 ALA   A CB   
3452 H H    . ALA   B 114 ? 0.661386 0.300424 0.293381 0.0427106   0.0206395   0.0278366   126 ALA   A H    
3453 H HA   . ALA   B 114 ? 0.697692 0.306703 0.326294 0.0636254   0.0396158   0.0359716   126 ALA   A HA   
3454 H HB1  . ALA   B 114 ? 0.675047 0.341785 0.329937 0.0514821   0.0280122   0.0419824   126 ALA   A HB1  
3455 H HB2  . ALA   B 114 ? 0.669147 0.328647 0.312548 0.045766    0.0253229   0.0267537   126 ALA   A HB2  
3456 H HB3  . ALA   B 114 ? 0.677519 0.331617 0.328499 0.0559544   0.035237    0.0354811   126 ALA   A HB3  
3457 N N    . THR   B 115 ? 0.720619 0.298545 0.319296 0.0659016   0.0440248   0.020349    127 THR   A N    
3458 C CA   . THR   B 115 ? 0.711747 0.272949 0.292415 0.0682656   0.0478389   0.0147608   127 THR   A CA   
3459 C C    . THR   B 115 ? 0.728571 0.311217 0.328026 0.0690518   0.0541896   0.0193533   127 THR   A C    
3460 O O    . THR   B 115 ? 0.740311 0.339625 0.361159 0.0731896   0.0628536   0.0287469   127 THR   A O    
3461 C CB   . THR   B 115 ? 0.749811 0.272653 0.301969 0.076501    0.0594705   0.0130319   127 THR   A CB   
3462 O OG1  . THR   B 115 ? 0.759959 0.261929 0.292904 0.0700611   0.0487125   0.00611098  127 THR   A OG1  
3463 C CG2  . THR   B 115 ? 0.811924 0.313137 0.335708 0.0780979   0.0628305   0.00814409  127 THR   A CG2  
3464 H H    . THR   B 115 ? 0.722753 0.295103 0.324361 0.0715737   0.0509023   0.0258597   127 THR   A H    
3465 H HA   . THR   B 115 ? 0.720438 0.279432 0.293529 0.0630772   0.0386124   0.00918049  127 THR   A HA   
3466 H HB   . THR   B 115 ? 0.760452 0.283036 0.321467 0.0837322   0.0706857   0.0191129   127 THR   A HB   
3468 H HG21 . THR   B 115 ? 0.829217 0.302531 0.328189 0.0819907   0.0697192   0.00526937  127 THR   A HG21 
3469 H HG22 . THR   B 115 ? 0.794843 0.29788  0.313018 0.0719597   0.0505109   0.00404385  127 THR   A HG22 
3470 H HG23 . THR   B 115 ? 0.791444 0.304048 0.326809 0.0811754   0.070766    0.0127199   127 THR   A HG23 
3471 N N    . LEU   B 116 ? 0.740397 0.322293 0.334022 0.0646444   0.0493913   0.0139249   128 LEU   A N    
3472 C CA   . LEU   B 116 ? 0.737358 0.333775 0.346543 0.061894    0.0544508   0.0165054   128 LEU   A CA   
3473 C C    . LEU   B 116 ? 0.745457 0.317486 0.334601 0.0665823   0.0637543   0.017214    128 LEU   A C    
3474 O O    . LEU   B 116 ? 0.725207 0.272805 0.286205 0.0693287   0.0595298   0.0133087   128 LEU   A O    
3475 C CB   . LEU   B 116 ? 0.758554 0.370494 0.37837  0.0526974   0.0446083   0.0103652   128 LEU   A CB   
3476 C CG   . LEU   B 116 ? 0.816073 0.449548 0.447342 0.0463059   0.0355438   0.00804694  128 LEU   A CG   
3477 C CD1  . LEU   B 116 ? 0.802331 0.448881 0.443406 0.0369232   0.0337052   0.00223275  128 LEU   A CD1  
3478 C CD2  . LEU   B 116 ? 0.742585 0.391276 0.385356 0.0471067   0.0364289   0.0163796   128 LEU   A CD2  
3479 H H    . LEU   B 116 ? 0.742767 0.314289 0.323576 0.0629946   0.0425766   0.00916378  128 LEU   A H    
3480 H HA   . LEU   B 116 ? 0.734866 0.345601 0.360523 0.0626779   0.0597395   0.0226964   128 LEU   A HA   
3481 H HB2  . LEU   B 116 ? 0.770958 0.36987  0.378913 0.0538352   0.0412737   0.00647087  128 LEU   A HB2  
3482 H HB3  . LEU   B 116 ? 0.763325 0.382295 0.39307  0.0493565   0.0485106   0.0118078   128 LEU   A HB3  
3483 H HG   . LEU   B 116 ? 0.787169 0.414108 0.410696 0.0469559   0.0306098   0.00454013  128 LEU   A HG   
3484 H HD11 . LEU   B 116 ? 0.808973 0.443225 0.444049 0.0382159   0.0343524   -0.00211221 128 LEU   A HD11 
3485 H HD12 . LEU   B 116 ? 0.796724 0.454987 0.440319 0.0323728   0.0291828   -0.00034681 128 LEU   A HD12 
3486 H HD13 . LEU   B 116 ? 0.803924 0.458037 0.454002 0.0339391   0.036867    0.00579177  128 LEU   A HD13 
3487 H HD21 . LEU   B 116 ? 0.768046 0.405004 0.402951 0.052183    0.0374694   0.01811     128 LEU   A HD21 
3488 H HD22 . LEU   B 116 ? 0.762929 0.41771  0.415396 0.0483804   0.0418726   0.0217992   128 LEU   A HD22 
3489 H HD23 . LEU   B 116 ? 0.754714 0.41903  0.403654 0.0412337   0.0308439   0.0157305   128 LEU   A HD23 
3490 N N    . PHE   B 117 ? 0.766324 0.348525 0.372011 0.0652611   0.0745609   0.0233721   129 PHE   A N    
3491 C CA   . PHE   B 117 ? 0.828661 0.391306 0.419828 0.0685435   0.0872129   0.02746     129 PHE   A CA   
3492 C C    . PHE   B 117 ? 0.731803 0.308159 0.344801 0.0584381   0.0866281   0.028493    129 PHE   A C    
3493 O O    . PHE   B 117 ? 0.720926 0.325431 0.364768 0.0499448   0.0848198   0.0302776   129 PHE   A O    
3494 C CB   . PHE   B 117 ? 0.867085 0.427234 0.461775 0.0768434   0.108215    0.0368148   129 PHE   A CB   
3495 C CG   . PHE   B 117 ? 0.861793 0.402915 0.441252 0.0790258   0.124714    0.0428717   129 PHE   A CG   
3496 C CD1  . PHE   B 117 ? 0.928156 0.431186 0.459909 0.0864484   0.130606    0.0409478   129 PHE   A CD1  
3497 C CD2  . PHE   B 117 ? 0.899076 0.459868 0.510037 0.0721231   0.134289    0.0513931   129 PHE   A CD2  
3498 C CE1  . PHE   B 117 ? 1.03672  0.519868 0.548303 0.0883216   0.146281    0.0483302   129 PHE   A CE1  
3499 C CE2  . PHE   B 117 ? 1.02496  0.567412 0.622526 0.0731319   0.150978    0.0587886   129 PHE   A CE2  
3500 C CZ   . PHE   B 117 ? 1.09783  0.600657 0.643941 0.0820197   0.157466    0.057846    129 PHE   A CZ   
3501 H H    . PHE   B 117 ? 0.75485  0.358261 0.382505 0.0610589   0.0736646   0.0259906   129 PHE   A H    
3502 H HA   . PHE   B 117 ? 0.821136 0.362782 0.386722 0.0712293   0.0834926   0.024256    129 PHE   A HA   
3503 H HB2  . PHE   B 117 ? 0.866629 0.41258  0.444428 0.0835362   0.110567    0.0349494   129 PHE   A HB2  
3504 H HB3  . PHE   B 117 ? 0.838175 0.423246 0.462571 0.0742931   0.10985     0.0417692   129 PHE   A HB3  
3505 H HD1  . PHE   B 117 ? 0.94623  0.43597  0.456897 0.0886549   0.122324    0.0347448   129 PHE   A HD1  
3506 H HD2  . PHE   B 117 ? 0.889051 0.475296 0.52951  0.0651358   0.128253    0.0522451   129 PHE   A HD2  
3507 H HE1  . PHE   B 117 ? 1.06148  0.517972 0.535826 0.0925065   0.148677    0.0472711   129 PHE   A HE1  
3508 H HE2  . PHE   B 117 ? 1.00176  0.557537 0.62284  0.0664932   0.156949    0.0647339   129 PHE   A HE2  
3509 H HZ   . PHE   B 117 ? 1.09181  0.581377 0.625998 0.0830055   0.170152    0.0643305   129 PHE   A HZ   
3510 N N    . PHE   B 118 ? 0.777442 0.332272 0.373081 0.0582595   0.0865199   0.0275991   130 PHE   A N    
3511 C CA   . PHE   B 118 ? 0.790646 0.346498 0.401764 0.0493954   0.091019    0.0297239   130 PHE   A CA   
3512 C C    . PHE   B 118 ? 0.759046 0.288113 0.350771 0.0534862   0.105134    0.0390996   130 PHE   A C    
3513 O O    . PHE   B 118 ? 0.805829 0.310399 0.364104 0.0623013   0.103171    0.0404401   130 PHE   A O    
3514 C CB   . PHE   B 118 ? 0.746369 0.297322 0.35773  0.045173    0.0782831   0.0204944   130 PHE   A CB   
3515 C CG   . PHE   B 118 ? 0.719164 0.293362 0.345848 0.0389884   0.0665705   0.0106008   130 PHE   A CG   
3516 C CD1  . PHE   B 118 ? 0.767308 0.346158 0.385305 0.0450412   0.0570302   0.00681658  130 PHE   A CD1  
3517 C CD2  . PHE   B 118 ? 0.749692 0.33942  0.396402 0.0252428   0.0653609   0.00559613  130 PHE   A CD2  
3518 C CE1  . PHE   B 118 ? 0.720436 0.319233 0.349353 0.0396223   0.0489337   -6.534e-05  130 PHE   A CE1  
3519 C CE2  . PHE   B 118 ? 0.75883  0.36709  0.411011 0.01936     0.0554025   -0.00312558 130 PHE   A CE2  
3520 C CZ   . PHE   B 118 ? 0.683846 0.296568 0.327151 0.0276506   0.0485422   -0.00506197 130 PHE   A CZ   
3521 H H    . PHE   B 118 ? 0.785182 0.322953 0.358421 0.0633673   0.0829963   0.0262232   130 PHE   A H    
3522 H HA   . PHE   B 118 ? 0.758062 0.333836 0.392553 0.0426801   0.0937648   0.0315986   130 PHE   A HA   
3523 H HB2  . PHE   B 118 ? 0.763533 0.299129 0.356431 0.0522962   0.074274    0.0206922   130 PHE   A HB2  
3524 H HB3  . PHE   B 118 ? 0.762797 0.307556 0.380943 0.0396132   0.0828197   0.0215482   130 PHE   A HB3  
3525 H HD1  . PHE   B 118 ? 0.753647 0.320756 0.356382 0.0520092   0.0562853   0.00935781  130 PHE   A HD1  
3526 H HD2  . PHE   B 118 ? 0.755145 0.341506 0.409363 0.018841    0.0710155   0.00792533  130 PHE   A HD2  
3527 H HE1  . PHE   B 118 ? 0.713013 0.31442  0.337375 0.0429885   0.0435568   -0.00148508 130 PHE   A HE1  
3528 H HE2  . PHE   B 118 ? 0.738764 0.355644 0.399122 0.00869507  0.0533823   -0.00753354 130 PHE   A HE2  
3529 H HZ   . PHE   B 118 ? 0.697882 0.322944 0.343953 0.0235433   0.0434508   -0.00962259 130 PHE   A HZ   
3530 N N    . GLU   B 119 ? 0.784281 0.319862 0.398242 0.044431    0.116972    0.0457265   131 GLU   A N    
3531 C CA   . GLU   B 119 ? 0.809015 0.319664 0.41289  0.0423871   0.127555    0.0537032   131 GLU   A CA   
3532 C C    . GLU   B 119 ? 0.928333 0.433085 0.545833 0.0316963   0.118722    0.0466782   131 GLU   A C    
3533 O O    . GLU   B 119 ? 0.898551 0.423095 0.544896 0.0171966   0.11493     0.0401931   131 GLU   A O    
3534 C CB   . GLU   B 119 ? 0.833513 0.354409 0.456226 0.0379971   0.148766    0.0662518   131 GLU   A CB   
3535 C CG   . GLU   B 119 ? 0.954619 0.449626 0.568485 0.0342253   0.164264    0.0779936   131 GLU   A CG   
3536 C CD   . GLU   B 119 ? 1.04664  0.54989  0.673805 0.0333084   0.190034    0.0930689   131 GLU   A CD   
3537 O OE1  . GLU   B 119 ? 1.06914  0.552902 0.662429 0.0464962   0.205983    0.100839    131 GLU   A OE1  
3538 O OE2  . GLU   B 119 ? 1.15425  0.682699 0.825753 0.0177095   0.194909    0.097422    131 GLU   A OE2  
3539 H H    . GLU   B 119 ? 0.765547 0.323121 0.40358  0.0384201   0.117997    0.0462766   131 GLU   A H    
3540 H HA   . GLU   B 119 ? 0.849732 0.339277 0.424414 0.0514113   0.127554    0.0562554   131 GLU   A HA   
3541 H HB2  . GLU   B 119 ? 0.852303 0.373824 0.464251 0.0469673   0.156304    0.0695238   131 GLU   A HB2  
3542 H HB3  . GLU   B 119 ? 0.830211 0.375674 0.483857 0.0283103   0.146243    0.0647389   131 GLU   A HB3  
3543 H HG2  . GLU   B 119 ? 0.948408 0.443476 0.578677 0.0235559   0.159494    0.0751197   131 GLU   A HG2  
3544 H HG3  . GLU   B 119 ? 0.967279 0.437373 0.549055 0.0427993   0.162564    0.0794463   131 GLU   A HG3  
3545 N N    . ILE   B 120 ? 0.920363 0.394829 0.514607 0.0390668   0.115843    0.0487265   132 ILE   A N    
3546 C CA   . ILE   B 120 ? 0.920828 0.380413 0.524192 0.0336496   0.111448    0.0428698   132 ILE   A CA   
3547 C C    . ILE   B 120 ? 0.927345 0.353281 0.519806 0.0343759   0.123802    0.0563322   132 ILE   A C    
3548 O O    . ILE   B 120 ? 0.906743 0.314805 0.47018  0.0467474   0.125884    0.0683738   132 ILE   A O    
3549 C CB   . ILE   B 120 ? 0.933527 0.389592 0.526054 0.0454336   0.0962339   0.035707    132 ILE   A CB   
3550 C CG1  . ILE   B 120 ? 0.917876 0.404301 0.517806 0.0450217   0.0852879   0.0248289   132 ILE   A CG1  
3551 C CG2  . ILE   B 120 ? 0.959503 0.396254 0.562382 0.0434748   0.0963605   0.0299337   132 ILE   A CG2  
3552 C CD1  . ILE   B 120 ? 0.904034 0.39195  0.498462 0.05518     0.0717471   0.0195529   132 ILE   A CD1  
3553 H H    . ILE   B 120 ? 0.937561 0.399228 0.508867 0.0482195   0.116848    0.0543852   132 ILE   A H    
3554 H HA   . ILE   B 120 ? 0.908815 0.381288 0.532195 0.0221007   0.110836    0.0356857   132 ILE   A HA   
3555 H HB   . ILE   B 120 ? 0.947564 0.391734 0.520369 0.0551687   0.0946235   0.0437354   132 ILE   A HB   
3556 H HG12 . ILE   B 120 ? 0.901631 0.400664 0.518155 0.0350251   0.0856315   0.0177347   132 ILE   A HG12 
3557 H HG13 . ILE   B 120 ? 0.908187 0.401964 0.50115  0.0472523   0.0873193   0.0290236   132 ILE   A HG13 
3558 H HG21 . ILE   B 120 ? 0.950549 0.388632 0.551649 0.0518316   0.0883681   0.026413    132 ILE   A HG21 
3559 H HG22 . ILE   B 120 ? 0.949897 0.393979 0.567341 0.0318092   0.098327    0.0210843   132 ILE   A HG22 
3560 H HG23 . ILE   B 120 ? 0.980304 0.394835 0.576827 0.0454706   0.103124    0.039015    132 ILE   A HG23 
3561 H HD11 . ILE   B 120 ? 0.919537 0.395309 0.498146 0.0636892   0.0689054   0.0271969   132 ILE   A HD11 
3562 H HD12 . ILE   B 120 ? 0.886651 0.392571 0.484069 0.0542214   0.0662463   0.0145495   132 ILE   A HD12 
3563 H HD13 . ILE   B 120 ? 0.908534 0.391577 0.512695 0.0539479   0.0716841   0.0142174   132 ILE   A HD13 
3564 N N    . GLU   B 121 ? 0.954387 0.36944  0.566999 0.0199937   0.130283    0.0534547   133 GLU   A N    
3565 C CA   . GLU   B 121 ? 0.978609 0.35518  0.58347  0.0201278   0.14114     0.0651228   133 GLU   A CA   
3566 C C    . GLU   B 121 ? 1.01464  0.368093 0.622477 0.0239428   0.134641    0.055444    133 GLU   A C    
3567 O O    . GLU   B 121 ? 0.976867 0.334815 0.603021 0.0102554   0.132534    0.038315    133 GLU   A O    
3568 C CB   . GLU   B 121 ? 1.01896  0.395973 0.645392 -0.00023055 0.15671     0.0709891   133 GLU   A CB   
3569 C CG   . GLU   B 121 ? 1.09901  0.433456 0.718286 -0.00278376 0.171452    0.0860178   133 GLU   A CG   
3570 C CD   . GLU   B 121 ? 1.12181  0.459507 0.768069 -0.0265264  0.186791    0.0920755   133 GLU   A CD   
3571 O OE1  . GLU   B 121 ? 1.2722   0.647464 0.945603 -0.0409512  0.187267    0.088465    133 GLU   A OE1  
3572 O OE2  . GLU   B 121 ? 1.08914  0.391353 0.733331 -0.0320635  0.198391    0.1022      133 GLU   A OE2  
3573 H H    . GLU   B 121 ? 0.933735 0.364264 0.564168 0.00899516  0.127508    0.0441257   133 GLU   A H    
3574 H HA   . GLU   B 121 ? 1.0038   0.369334 0.587052 0.0315611   0.143207    0.0768541   133 GLU   A HA   
3575 H HB2  . GLU   B 121 ? 1.01103  0.406693 0.638913 -0.00015774 0.162083    0.0773373   133 GLU   A HB2  
3576 H HB3  . GLU   B 121 ? 1.00951  0.397578 0.655335 -0.0134317  0.152333    0.0591444   133 GLU   A HB3  
3577 H HG2  . GLU   B 121 ? 1.10516  0.418364 0.723713 -0.00110571 0.167448    0.0801611   133 GLU   A HG2  
3578 H HG3  . GLU   B 121 ? 1.10722  0.430723 0.703964 0.00978534  0.175386    0.0990608   133 GLU   A HG3  
3579 N N    . LEU   B 122 ? 1.02764  0.355926 0.616731 0.0423669   0.132146    0.0671312   134 LEU   A N    
3580 C CA   . LEU   B 122 ? 1.0583   0.360221 0.65459  0.04995     0.130962    0.0625712   134 LEU   A CA   
3581 C C    . LEU   B 122 ? 1.13482  0.395077 0.736754 0.0404494   0.146968    0.0685634   134 LEU   A C    
3582 O O    . LEU   B 122 ? 1.21936  0.454562 0.807561 0.0456593   0.155077    0.0895546   134 LEU   A O    
3583 C CB   . LEU   B 122 ? 1.02529  0.32394  0.606718 0.0739779   0.119249    0.0754475   134 LEU   A CB   
3584 C CG   . LEU   B 122 ? 1.08097  0.35593  0.675743 0.0877996   0.119328    0.075275    134 LEU   A CG   
3585 C CD1  . LEU   B 122 ? 1.01774  0.305176 0.633363 0.0818262   0.11986     0.0499034   134 LEU   A CD1  
3586 C CD2  . LEU   B 122 ? 1.06397  0.345315 0.649482 0.110971    0.103748    0.0928772   134 LEU   A CD2  
3587 H H    . LEU   B 122 ? 1.03813  0.36544  0.609667 0.0507233   0.131336    0.078557    134 LEU   A H    
3588 H HA   . LEU   B 122 ? 1.03629  0.351195 0.644588 0.0449999   0.126997    0.0465342   134 LEU   A HA   
3589 H HB2  . LEU   B 122 ? 1.01399  0.338786 0.593707 0.0769098   0.108945    0.0695957   134 LEU   A HB2  
3590 H HB3  . LEU   B 122 ? 1.06165  0.348532 0.625788 0.0781027   0.121596    0.0913681   134 LEU   A HB3  
3591 H HG   . LEU   B 122 ? 1.09407  0.338724 0.689139 0.0854706   0.130185    0.0819748   134 LEU   A HG   
3592 H HD11 . LEU   B 122 ? 1.03805  0.314638 0.657775 0.0668189   0.128714    0.0403902   134 LEU   A HD11 
3593 H HD12 . LEU   B 122 ? 1.04314  0.318732 0.66737  0.0942208   0.120703    0.0504916   134 LEU   A HD12 
3594 H HD13 . LEU   B 122 ? 0.998637 0.315957 0.614148 0.0803807   0.110975    0.0430884   134 LEU   A HD13 
3595 H HD21 . LEU   B 122 ? 1.08829  0.360399 0.654205 0.113137    0.102969    0.108353    134 LEU   A HD21 
3596 H HD22 . LEU   B 122 ? 1.04135  0.350651 0.628107 0.112175    0.0930258   0.0858686   134 LEU   A HD22 
3597 H HD23 . LEU   B 122 ? 1.08714  0.353688 0.685225 0.121796    0.105353    0.096166    134 LEU   A HD23 
3598 N N    . LEU   B 123 ? 1.19794  0.44646  0.816834 0.024983    0.152045    0.0498797   135 LEU   A N    
3599 C CA   . LEU   B 123 ? 1.15504  0.362224 0.779972 0.00972182  0.167553    0.05284     135 LEU   A CA   
3600 C C    . LEU   B 123 ? 1.20728  0.365455 0.828961 0.0268644   0.174672    0.0586831   135 LEU   A C    
3601 O O    . LEU   B 123 ? 1.19188  0.309158 0.810614 0.0253436   0.187583    0.0744309   135 LEU   A O    
3602 C CB   . LEU   B 123 ? 1.18177  0.395697 0.822113 -0.0183399  0.167816    0.0282456   135 LEU   A CB   
3603 C CG   . LEU   B 123 ? 1.19319  0.458608 0.844852 -0.0360725  0.159758    0.023711    135 LEU   A CG   
3604 C CD1  . LEU   B 123 ? 1.28866  0.562577 0.952734 -0.0641667  0.154496    -0.00026249 135 LEU   A CD1  
3605 C CD2  . LEU   B 123 ? 1.15078  0.423056 0.809078 -0.0446681  0.169924    0.0448995   135 LEU   A CD2  
3606 H H    . LEU   B 123 ? 1.14261  0.406991 0.767321 0.0227818   0.145978    0.0348696   135 LEU   A H    
3607 H HA   . LEU   B 123 ? 1.18683  0.393102 0.80805  0.00558559  0.17351     0.0676478   135 LEU   A HA   
3608 H HB2  . LEU   B 123 ? 1.18233  0.393243 0.821687 -0.01367    0.163984    0.0135426   135 LEU   A HB2  
3609 H HB3  . LEU   B 123 ? 1.2198   0.403604 0.864108 -0.0307284  0.177674    0.0293487   135 LEU   A HB3  
3610 H HG   . LEU   B 123 ? 1.15693  0.448716 0.803495 -0.0234506  0.150937    0.0232974   135 LEU   A HG   
3611 H HD11 . LEU   B 123 ? 1.25723  0.52582  0.913737 -0.0584983  0.150204    -0.0143379  135 LEU   A HD11 
3612 H HD12 . LEU   B 123 ? 1.23162  0.541954 0.90548  -0.0729418  0.147819    -7.411e-05  135 LEU   A HD12 
3613 H HD13 . LEU   B 123 ? 1.29176  0.539395 0.960806 -0.0793329  0.162179    -0.00108837 135 LEU   A HD13 
3614 H HD21 . LEU   B 123 ? 1.16357  0.433606 0.808292 -0.0276932  0.17189     0.0591335   135 LEU   A HD21 
3615 H HD22 . LEU   B 123 ? 1.19754  0.442453 0.861337 -0.0567476  0.179274    0.0476444   135 LEU   A HD22 
3616 H HD23 . LEU   B 123 ? 1.14186  0.447724 0.812494 -0.0552984  0.165889    0.042244    135 LEU   A HD23 
3617 N N    . ASP   B 124 ? 1.25147  0.41252  0.877158 0.0425577   0.168567    0.0459838   136 ASP   A N    
3618 C CA   . ASP   B 124 ? 1.28588  0.401801 0.916491 0.0597339   0.178228    0.0476705   136 ASP   A CA   
3619 C C    . ASP   B 124 ? 1.29217  0.432209 0.931297 0.0784122   0.170073    0.0354634   136 ASP   A C    
3620 O O    . ASP   B 124 ? 1.29353  0.474702 0.932788 0.0694201   0.160177    0.0192877   136 ASP   A O    
3621 C CB   . ASP   B 124 ? 1.31612  0.383775 0.95092  0.0403711   0.195038    0.0290347   136 ASP   A CB   
3622 C CG   . ASP   B 124 ? 1.38521  0.392765 1.02371  0.0595372   0.210669    0.0387587   136 ASP   A CG   
3623 O OD1  . ASP   B 124 ? 1.33289  0.33968  0.972721 0.0874361   0.206754    0.0658859   136 ASP   A OD1  
3624 O OD2  . ASP   B 124 ? 1.54078  0.499296 1.17949  0.0455703   0.226506    0.0208883   136 ASP   A OD2  
3625 H H    . ASP   B 124 ? 1.20322  0.395634 0.830231 0.0433285   0.159356    0.0366282   136 ASP   A H    
3626 H HA   . ASP   B 124 ? 1.30783  0.409139 0.933806 0.0730049   0.179307    0.0688677   136 ASP   A HA   
3627 H HB2  . ASP   B 124 ? 1.32931  0.392234 0.962646 0.0210383   0.198372    0.0313686   136 ASP   A HB2  
3628 H HB3  . ASP   B 124 ? 1.31047  0.388649 0.946696 0.0327626   0.193236    0.00762577  136 ASP   A HB3  
3629 N N    . PHE   B 125 ? 1.24591  0.362604 0.894976 0.105103    0.174739    0.0463084   137 PHE   A N    
3630 C CA   . PHE   B 125 ? 1.2125   0.349022 0.877309 0.124166    0.172062    0.0366272   137 PHE   A CA   
3631 C C    . PHE   B 125 ? 1.27982  0.366519 0.959356 0.144546    0.190399    0.0404865   137 PHE   A C    
3632 O O    . PHE   B 125 ? 1.26446  0.315458 0.943515 0.154212    0.195675    0.0635833   137 PHE   A O    
3633 C CB   . PHE   B 125 ? 1.18959  0.377372 0.858127 0.140549    0.150053    0.0541171   137 PHE   A CB   
3634 C CG   . PHE   B 125 ? 1.19058  0.37097  0.854812 0.158799    0.140738    0.0882737   137 PHE   A CG   
3635 C CD1  . PHE   B 125 ? 1.30029  0.484675 0.938746 0.147685    0.13316     0.102755    137 PHE   A CD1  
3636 C CD2  . PHE   B 125 ? 1.28966  0.464669 0.974822 0.187518    0.138269    0.107093    137 PHE   A CD2  
3637 C CE1  . PHE   B 125 ? 1.34143  0.519785 0.966922 0.163306    0.122882    0.133868    137 PHE   A CE1  
3638 C CE2  . PHE   B 125 ? 1.35559  0.525801 1.03345  0.203377    0.125876    0.140815    137 PHE   A CE2  
3639 C CZ   . PHE   B 125 ? 1.39612  0.566029 1.03997  0.190355    0.117827    0.153577    137 PHE   A CZ   
3640 H H    . PHE   B 125 ? 1.28976  0.378124 0.937716 0.112216    0.180453    0.0620817   137 PHE   A H    
3641 H HA   . PHE   B 125 ? 1.2083   0.356018 0.870993 0.110735    0.173718    0.0149446   137 PHE   A HA   
3642 H HB2  . PHE   B 125 ? 1.17035  0.372963 0.853697 0.15204     0.149314    0.0481649   137 PHE   A HB2  
3643 H HB3  . PHE   B 125 ? 1.14965  0.363909 0.807895 0.126546    0.141641    0.0479262   137 PHE   A HB3  
3644 H HD1  . PHE   B 125 ? 1.25862  0.45143  0.887591 0.129758    0.134929    0.0918335   137 PHE   A HD1  
3645 H HD2  . PHE   B 125 ? 1.28469  0.456665 0.989316 0.196744    0.146389    0.0979133   137 PHE   A HD2  
3646 H HE1  . PHE   B 125 ? 1.34597  0.523271 0.949973 0.155555    0.120734    0.142875    137 PHE   A HE1  
3647 H HE2  . PHE   B 125 ? 1.36977  0.538296 1.06544  0.223374    0.12303     0.155476    137 PHE   A HE2  
3648 H HZ   . PHE   B 125 ? 1.39713  0.563258 1.03039  0.20025     0.108836    0.176237    137 PHE   A HZ   
3649 N N    . LYS   B 126 ? 1.28207  0.361681 0.971967 0.149917    0.203006    0.0174646   138 LYS   A N    
3650 C CA   . LYS   B 126 ? 1.31459  0.339748 1.0182   0.169438    0.226699    0.0161409   138 LYS   A CA   
3651 C C    . LYS   B 126 ? 1.32968  0.388362 1.06038  0.196811    0.227528    0.0156839   138 LYS   A C    
3652 O O    . LYS   B 126 ? 1.25776  0.357834 0.985853 0.1878      0.221417    -0.00283454 138 LYS   A O    
3653 C CB   . LYS   B 126 ? 1.2824   0.249426 0.966424 0.14494     0.248425    -0.0137461  138 LYS   A CB   
3654 H H    . LYS   B 126 ? 1.24865  0.356273 0.936006 0.141899    0.198269    0.00238178  138 LYS   A H    
3655 H HA   . LYS   B 126 ? 1.33119  0.337457 1.04034  0.181785    0.226642    0.0390562   138 LYS   A HA   
3658 N N    . GLY   B 127 ? 1.42321  0.470198 1.18321  0.230653    0.232801    0.0409918   139 GLY   A N    
3659 C CA   . GLY   B 127 ? 1.46555  0.543663 1.26148  0.258974    0.237024    0.0442823   139 GLY   A CA   
3660 C C    . GLY   B 127 ? 1.52407  0.570096 1.31657  0.257213    0.267829    0.00952742  139 GLY   A C    
3661 O O    . GLY   B 127 ? 1.6744   0.658237 1.47003  0.269235    0.294065    0.00585812  139 GLY   A O    
3662 H H    . GLY   B 127 ? 1.44215  0.462763 1.20176  0.236405    0.233775    0.058352    139 GLY   A H    
3663 H HA2  . GLY   B 127 ? 1.41008  0.537902 1.20969  0.255661    0.21938     0.046675    139 GLY   A HA2  
3664 H HA3  . GLY   B 127 ? 1.47893  0.548933 1.29765  0.282586    0.23799     0.0675788   139 GLY   A HA3  
3665 N N    . GLU   B 128 ? 1.59089  0.675824 1.37316  0.242086    0.265063    -0.0149992  140 GLU   A N    
3666 C CA   . GLU   B 128 ? 1.60473  0.658979 1.36564  0.230689    0.291253    -0.0525912  140 GLU   A CA   
3667 C C    . GLU   B 128 ? 1.66992  0.676741 1.45583  0.263468    0.3256      -0.0524192  140 GLU   A C    
3668 O O    . GLU   B 128 ? 1.80803  0.852287 1.63073  0.289959    0.332329    -0.0437545  140 GLU   A O    
3669 C CB   . GLU   B 128 ? 1.46474  0.573034 1.2211   0.221593    0.286391    -0.0703096  140 GLU   A CB   
3670 O OXT  . GLU   B 128 ? 1.6216   0.556708 1.39305  0.262113    0.344851    -0.058829   140 GLU   A OXT  
3671 H H    . GLU   B 128 ? 1.50947  0.640541 1.29583  0.238456    0.245881    -0.00744026 140 GLU   A H    
3672 H HA   . GLU   B 128 ? 1.60956  0.631665 1.34089  0.207591    0.292949    -0.0672432  140 GLU   A HA   
3675 C C4   . A1IN8 C .   ? 0.691384 0.50908  0.339934 0.0690338   -0.133142   -0.0969243  201 A1IN8 B C4   
3676 C C14  . A1IN8 C .   ? 0.574015 0.48728  0.316334 0.0506774   -0.0525165  -0.00779555 201 A1IN8 B C14  
3677 C C5   . A1IN8 C .   ? 0.73809  0.555465 0.334535 0.104026    -0.115529   -0.0854797  201 A1IN8 B C5   
3678 C C6   . A1IN8 C .   ? 0.746696 0.568024 0.289185 0.138668    -0.125927   -0.0903132  201 A1IN8 B C6   
3679 C C11  . A1IN8 C .   ? 0.935543 0.829323 0.52348  0.139786    -0.120924   -0.0470391  201 A1IN8 B C11  
3680 C C7   . A1IN8 C .   ? 0.844625 0.668507 0.332803 0.186326    -0.0683717  -0.0548518  201 A1IN8 B C7   
3681 C C8   . A1IN8 C .   ? 0.811407 0.633349 0.349902 0.138595    -0.163485   -0.113043   201 A1IN8 B C8   
3682 C C9   . A1IN8 C .   ? 0.988615 0.84041  0.46141  0.18769     -0.182548   -0.101846   201 A1IN8 B C9   
3683 C C10  . A1IN8 C .   ? 0.906441 0.787661 0.415598 0.181043    -0.140604   -0.0591273  201 A1IN8 B C10  
3684 C C12  . A1IN8 C .   ? 0.902239 0.805035 0.497162 0.143925    -0.0771739  -0.0144373  201 A1IN8 B C12  
3685 C C13  . A1IN8 C .   ? 0.708152 0.627326 0.374743 0.107914    -0.0625133  -0.00168822 201 A1IN8 B C13  
3686 N N1   . A1IN8 C .   ? 0.566229 0.43886  0.315642 0.0203539   -0.0850532  -0.04788    201 A1IN8 B N1   
3687 C C3   . A1IN8 C .   ? 0.729913 0.5516   0.385471 0.067575    -0.166115   -0.117891   201 A1IN8 B C3   
3688 C C1   . A1IN8 C .   ? 0.849822 0.69744  0.535417 0.0682025   -0.23751    -0.154188   201 A1IN8 B C1   
3689 O O1   . A1IN8 C .   ? 0.873989 0.705077 0.479119 0.104751    -0.223487   -0.148629   201 A1IN8 B O1   
3690 C C2   . A1IN8 C .   ? 0.787862 0.611425 0.388756 0.10202     -0.185156   -0.127953   201 A1IN8 B C2   
3691 O O2   . A1IN8 C .   ? 0.809762 0.631441 0.295159 0.177832    -0.10464    -0.0765904  201 A1IN8 B O2   
3692 O O3   . A1IN8 C .   ? 0.897942 0.719038 0.368057 0.178247    -0.177113   -0.118731   201 A1IN8 B O3   
3693 O O4   . A1IN8 C .   ? 0.93508  0.838798 0.456688 0.18523     -0.160662   -0.0542449  201 A1IN8 B O4   
3694 O O5   . A1IN8 C .   ? 0.823637 0.743538 0.470141 0.118665    -0.123831   -0.0374258  201 A1IN8 B O5   
3695 O O6   . A1IN8 C .   ? 0.652218 0.558527 0.35296  0.0746732   -0.0730358  -0.0208501  201 A1IN8 B O6   
3696 O O7   . A1IN8 C .   ? 0.514669 0.443596 0.274517 0.0523395   -0.0310493  0.0137741   201 A1IN8 B O7   
3697 C C15  . A1IN8 C .   ? 0.506845 0.401726 0.269407 0.0222712   -0.0592214  -0.0228532  201 A1IN8 B C15  
3698 C C16  . A1IN8 C .   ? 0.56049  0.469772 0.371058 -0.00384143 -0.0532905  -0.0197846  201 A1IN8 B C16  
3699 C C17  . A1IN8 C .   ? 0.603333 0.526565 0.435415 -0.00478058 -0.0721292  -0.0303601  201 A1IN8 B C17  
3700 C C18  . A1IN8 C .   ? 0.623154 0.527195 0.455083 -0.0135208  -0.0970525  -0.0540976  201 A1IN8 B C18  
3701 C C19  . A1IN8 C .   ? 0.621134 0.502928 0.397903 0.0105758   -0.109594   -0.0640204  201 A1IN8 B C19  
3702 C C20  . A1IN8 C .   ? 0.559172 0.405061 0.274028 0.0326474   -0.0882074  -0.0564402  201 A1IN8 B C20  
3703 O O8   . A1IN8 C .   ? 0.575247 0.423099 0.276709 0.0444861   -0.0677669  -0.0402797  201 A1IN8 B O8   
3704 C C21  . A1IN8 C .   ? 0.595269 0.410634 0.293526 0.0344669   -0.116677   -0.0855912  201 A1IN8 B C21  
3705 C C22  . A1IN8 C .   ? 0.635312 0.415011 0.317212 0.0354859   -0.112796   -0.0909501  201 A1IN8 B C22  
3706 C C23  . A1IN8 C .   ? 0.615393 0.388539 0.336509 0.00385938  -0.099665   -0.078339   201 A1IN8 B C23  
3707 C C24  . A1IN8 C .   ? 0.70945  0.447178 0.411787 0.0104966   -0.0975622  -0.0800748  201 A1IN8 B C24  
3708 C C25  . A1IN8 C .   ? 0.710318 0.408349 0.399325 0.0156536   -0.121421   -0.108104   201 A1IN8 B C25  
3709 C C26  . A1IN8 C .   ? 0.758073 0.461092 0.405777 0.0462746   -0.135559   -0.126129   201 A1IN8 B C26  
3710 C C27  . A1IN8 C .   ? 0.680644 0.422728 0.34142  0.0427312   -0.14179    -0.123184   201 A1IN8 B C27  
3711 H H5   . A1IN8 C .   ? 0.702373 0.52247  0.304412 0.104204    -0.0938402  -0.0699302  201 A1IN8 B H5   
3712 H H13  . A1IN8 C .   ? 0.888273 0.766458 0.490804 0.12225     -0.129945   -0.0644169  201 A1IN8 B H13  
3713 H H7   . A1IN8 C .   ? 0.866971 0.690111 0.312014 0.216846    -0.0556047  -0.0482374  201 A1IN8 B H7   
3714 H H8   . A1IN8 C .   ? 0.779259 0.624614 0.307901 0.170848    -0.0518191  -0.0335473  201 A1IN8 B H8   
3715 H H6   . A1IN8 C .   ? 0.828718 0.633121 0.323305 0.178055    -0.0726688  -0.0674561  201 A1IN8 B H6   
3716 H H10  . A1IN8 C .   ? 0.948262 0.807101 0.458204 0.169105    -0.20804    -0.115645   201 A1IN8 B H10  
3717 H H9   . A1IN8 C .   ? 1.01722  0.862578 0.4301   0.219412    -0.19187    -0.106059   201 A1IN8 B H9   
3718 H H11  . A1IN8 C .   ? 0.95531  0.835106 0.426494 0.205303    -0.117508   -0.0421956  201 A1IN8 B H11  
3719 H H15  . A1IN8 C .   ? 0.880965 0.768926 0.458905 0.148408    -0.0699441  -0.0192654  201 A1IN8 B H15  
3720 H H16  . A1IN8 C .   ? 0.890351 0.802426 0.461603 0.166498    -0.0657939  0.00307374  201 A1IN8 B H16  
3721 H H17  . A1IN8 C .   ? 0.708461 0.633456 0.383083 0.110085    -0.0385723  0.0170198   201 A1IN8 B H17  
3722 H H18  . A1IN8 C .   ? 0.717938 0.651538 0.402152 0.10627     -0.0667301  0.00417716  201 A1IN8 B H18  
3723 H H4   . A1IN8 C .   ? 0.712499 0.537068 0.410952 0.0439478   -0.175545   -0.12422    201 A1IN8 B H4   
3724 H H2   . A1IN8 C .   ? 0.870889 0.727917 0.559836 0.0743072   -0.266506   -0.167908   201 A1IN8 B H2   
3725 H H3   . A1IN8 C .   ? 0.843095 0.671037 0.551667 0.0491058   -0.240975   -0.166246   201 A1IN8 B H3   
3726 H H1   . A1IN8 C .   ? 0.797423 0.666232 0.513113 0.0572609   -0.214327   -0.131887   201 A1IN8 B H1   
3729 H H19  . A1IN8 C .   ? 0.528224 0.416234 0.286812 0.0208962   -0.0477343  -0.0161309  201 A1IN8 B H19  
3730 H H20  . A1IN8 C .   ? 0.538085 0.435546 0.358764 -0.0212033  -0.0510288  -0.0240739  201 A1IN8 B H20  
3731 H H21  . A1IN8 C .   ? 0.525571 0.446601 0.346308 -0.00275609 -0.0381224  -0.00588149 201 A1IN8 B H21  
3732 H H23  . A1IN8 C .   ? 0.607089 0.539857 0.422505 0.0150354   -0.077171   -0.0258092  201 A1IN8 B H23  
3733 H H22  . A1IN8 C .   ? 0.570767 0.50519  0.436125 -0.0188404  -0.0635439  -0.0263163  201 A1IN8 B H22  
3734 H H25  . A1IN8 C .   ? 0.620404 0.53602  0.473433 -0.0151027  -0.112667   -0.0623362  201 A1IN8 B H25  
3735 H H24  . A1IN8 C .   ? 0.603161 0.496548 0.452126 -0.032703   -0.0892221  -0.0549172  201 A1IN8 B H24  
3736 H H27  . A1IN8 C .   ? 0.640025 0.530282 0.395793 0.0303983   -0.120358   -0.0658131  201 A1IN8 B H27  
3737 H H26  . A1IN8 C .   ? 0.636715 0.500456 0.41656  0.00233871  -0.124602   -0.0803921  201 A1IN8 B H26  
3738 H H28  . A1IN8 C .   ? 0.603914 0.420733 0.334656 0.0146324   -0.127943   -0.0936995  201 A1IN8 B H28  
3739 H H29  . A1IN8 C .   ? 0.634342 0.417682 0.292601 0.0545491   -0.0987453  -0.0805055  201 A1IN8 B H29  
3740 H H30  . A1IN8 C .   ? 0.593764 0.387427 0.324979 9.056e-05   -0.0837272  -0.0613987  201 A1IN8 B H30  
3741 H H31  . A1IN8 C .   ? 0.624859 0.39501  0.372696 -0.0150129  -0.10853    -0.0857766  201 A1IN8 B H31  
3742 H H33  . A1IN8 C .   ? 0.663706 0.396316 0.384318 -0.00684814 -0.0892709  -0.0693739  201 A1IN8 B H33  
3743 H H32  . A1IN8 C .   ? 0.679564 0.424308 0.361543 0.0299592   -0.0874535  -0.0719131  201 A1IN8 B H32  
3744 H H35  . A1IN8 C .   ? 0.725494 0.417381 0.443416 -0.00541324 -0.131413   -0.115446   201 A1IN8 B H35  
3745 H H34  . A1IN8 C .   ? 0.742583 0.416265 0.421503 0.0210638   -0.117773   -0.107121   201 A1IN8 B H34  
3746 H H37  . A1IN8 C .   ? 0.784488 0.459613 0.421814 0.0498115   -0.155055   -0.148967   201 A1IN8 B H37  
3747 H H36  . A1IN8 C .   ? 0.746713 0.453793 0.36706  0.0682008   -0.121686   -0.117299   201 A1IN8 B H36  
3748 H H38  . A1IN8 C .   ? 0.726637 0.470026 0.352154 0.0662396   -0.151069   -0.132778   201 A1IN8 B H38  
3749 H H39  . A1IN8 C .   ? 0.696065 0.436245 0.388053 0.0229004   -0.156485   -0.133354   201 A1IN8 B H39  
3750 C C4   . A1IN8 D .   ? 0.675502 0.363665 0.32256  -0.0329574  0.0188463   -0.0325232  201 A1IN8 A C4   
3751 C C14  . A1IN8 D .   ? 0.731497 0.347543 0.361954 0.00913182  0.0459551   -0.0503708  201 A1IN8 A C14  
3752 C C5   . A1IN8 D .   ? 0.706827 0.405488 0.341467 -0.0299417  0.0150884   -0.0331487  201 A1IN8 A C5   
3753 C C6   . A1IN8 D .   ? 0.71981  0.422109 0.333381 -0.0435806  0.0108007   -0.0440759  201 A1IN8 A C6   
3754 C C11  . A1IN8 D .   ? 0.972907 0.599486 0.535219 -0.0417207  0.0462975   -0.0943098  201 A1IN8 A C11  
3755 C C7   . A1IN8 D .   ? 0.699368 0.416124 0.308062 -0.0257934  0.0121584   -0.0322236  201 A1IN8 A C7   
3756 C C8   . A1IN8 D .   ? 0.731853 0.427319 0.335382 -0.0626016  0.0073483   -0.0557828  201 A1IN8 A C8   
3757 C C9   . A1IN8 D .   ? 0.9705   0.624831 0.523598 -0.0796102  0.0185114   -0.0912357  201 A1IN8 A C9   
3758 C C10  . A1IN8 D .   ? 1.01533  0.668116 0.565315 -0.0601595  0.0299482   -0.0898784  201 A1IN8 A C10  
3759 C C12  . A1IN8 D .   ? 0.831069 0.456344 0.420916 -0.0313194  0.043984    -0.0810772  201 A1IN8 A C12  
3760 C C13  . A1IN8 D .   ? 0.848668 0.475619 0.455355 -0.0103268  0.0475283   -0.0701398  201 A1IN8 A C13  
3761 N N1   . A1IN8 D .   ? 0.661902 0.292378 0.305687 -0.00304978 0.0399055   -0.0350009  201 A1IN8 A N1   
3762 C C3   . A1IN8 D .   ? 0.714636 0.400506 0.358868 -0.0522593  0.0152206   -0.0413089  201 A1IN8 A C3   
3763 C C1   . A1IN8 D .   ? 0.822277 0.499072 0.454387 -0.0988607  0.00387579  -0.0624752  201 A1IN8 A C1   
3764 O O1   . A1IN8 D .   ? 0.784524 0.462588 0.393908 -0.0893673  0.00449251  -0.0673083  201 A1IN8 A O1   
3765 C C2   . A1IN8 D .   ? 0.770624 0.457642 0.391505 -0.0674294  0.00894774  -0.0545316  201 A1IN8 A C2   
3766 O O2   . A1IN8 D .   ? 0.690811 0.400707 0.289135 -0.0408945  0.0105619   -0.0443843  201 A1IN8 A O2   
3767 O O3   . A1IN8 D .   ? 0.906762 0.598252 0.48089  -0.0796536  0.00345562  -0.0702368  201 A1IN8 A O3   
3768 O O4   . A1IN8 D .   ? 0.974768 0.627094 0.491998 -0.0680928  0.0331108   -0.100587   201 A1IN8 A O4   
3769 O O5   . A1IN8 D .   ? 0.853975 0.487542 0.419141 -0.0267626  0.0540745   -0.0909622  201 A1IN8 A O5   
3770 O O6   . A1IN8 D .   ? 0.741683 0.367065 0.363346 -0.00643856 0.0434914   -0.0581999  201 A1IN8 A O6   
3771 O O7   . A1IN8 D .   ? 0.770832 0.381077 0.403693 0.02025     0.0497049   -0.05162    201 A1IN8 A O7   
3772 C C15  . A1IN8 D .   ? 0.663037 0.278496 0.300697 0.010704    0.0435322   -0.0382846  201 A1IN8 A C15  
3773 C C16  . A1IN8 D .   ? 0.7265   0.313521 0.364177 0.0176141   0.0508836   -0.0377804  201 A1IN8 A C16  
3774 C C17  . A1IN8 D .   ? 0.742422 0.31275  0.37858  0.00448876  0.0569439   -0.0476861  201 A1IN8 A C17  
3775 C C18  . A1IN8 D .   ? 0.738307 0.322876 0.381972 -0.00998245 0.0533914   -0.0426461  201 A1IN8 A C18  
3776 C C19  . A1IN8 D .   ? 0.732951 0.35117  0.377845 -0.0178916  0.0429585   -0.042301   201 A1IN8 A C19  
3777 C C20  . A1IN8 D .   ? 0.665777 0.322335 0.315079 -0.0039921  0.0327878   -0.0264661  201 A1IN8 A C20  
3778 O O8   . A1IN8 D .   ? 0.636863 0.298677 0.283142 0.00549041  0.0307454   -0.022554   201 A1IN8 A O8   
3779 C C21  . A1IN8 D .   ? 0.677689 0.359109 0.339537 -0.0177575  0.0259814   -0.0203978  201 A1IN8 A C21  
3780 C C22  . A1IN8 D .   ? 0.659139 0.361463 0.335021 -0.00844673 0.0237446   -0.00379886 201 A1IN8 A C22  
3781 C C23  . A1IN8 D .   ? 0.699167 0.387066 0.381694 0.00429018  0.0347385   0.00475387  201 A1IN8 A C23  
3782 C C24  . A1IN8 D .   ? 0.718064 0.423724 0.414982 0.0137653   0.0361779   0.0200896   201 A1IN8 A C24  
3783 C C25  . A1IN8 D .   ? 0.656499 0.397864 0.380088 0.00340493  0.029083    0.0304763   201 A1IN8 A C25  
3784 C C26  . A1IN8 D .   ? 0.71572  0.471339 0.429084 -0.00960839 0.0142198   0.0236106   201 A1IN8 A C26  
3785 C C27  . A1IN8 D .   ? 0.658349 0.393289 0.353212 -0.0209599  0.0144915   0.00549861  201 A1IN8 A C27  
3786 H H5   . A1IN8 D .   ? 0.68179  0.381178 0.319296 -0.018759   0.0169253   -0.0271945  201 A1IN8 A H5   
3787 H H13  . A1IN8 D .   ? 0.961383 0.564991 0.511337 -0.0464316  0.054328    -0.107882   201 A1IN8 A H13  
3788 H H7   . A1IN8 D .   ? 0.694404 0.4172   0.291875 -0.0271325  0.0120544   -0.0323327  201 A1IN8 A H7   
3789 H H8   . A1IN8 D .   ? 0.681793 0.384425 0.295596 -0.0165087  0.0190644   -0.034941   201 A1IN8 A H8   
3790 H H6   . A1IN8 D .   ? 0.677953 0.406684 0.299582 -0.0237253  0.00676042  -0.0205747  201 A1IN8 A H6   
3791 H H10  . A1IN8 D .   ? 0.969361 0.6073   0.534244 -0.0764832  0.0242328   -0.0929152  201 A1IN8 A H10  
3792 H H9   . A1IN8 D .   ? 1.00509  0.652712 0.535112 -0.0947379  0.0158515   -0.103029   201 A1IN8 A H9   
3793 H H11  . A1IN8 D .   ? 0.950251 0.622575 0.514774 -0.052814   0.0242498   -0.0756432  201 A1IN8 A H11  
3794 H H15  . A1IN8 D .   ? 0.881339 0.486184 0.470815 -0.0341375  0.0490201   -0.0875594  201 A1IN8 A H15  
3795 H H16  . A1IN8 D .   ? 0.853636 0.495783 0.450287 -0.0374672  0.0345514   -0.0725212  201 A1IN8 A H16  
3796 H H17  . A1IN8 D .   ? 0.801347 0.444929 0.408329 -0.00790466 0.043874    -0.0647043  201 A1IN8 A H17  
3797 H H18  . A1IN8 D .   ? 0.824082 0.435855 0.430905 -0.00278556 0.0562489   -0.0758724  201 A1IN8 A H18  
3798 H H4   . A1IN8 D .   ? 0.723846 0.402867 0.378334 -0.0557938  0.0182214   -0.039876   201 A1IN8 A H4   
3799 H H2   . A1IN8 D .   ? 0.837662 0.509875 0.460676 -0.117616   -0.00179409 -0.0718664  201 A1IN8 A H2   
3800 H H3   . A1IN8 D .   ? 0.79137  0.493759 0.444971 -0.0966373  -0.00174283 -0.0475101  201 A1IN8 A H3   
3801 H H1   . A1IN8 D .   ? 0.808793 0.463142 0.444055 -0.0892896  0.0152116   -0.0641821  201 A1IN8 A H1   
3804 H H19  . A1IN8 D .   ? 0.667994 0.290266 0.306848 0.0181543   0.0404064   -0.0312178  201 A1IN8 A H19  
3805 H H20  . A1IN8 D .   ? 0.709812 0.294332 0.348567 0.0214732   0.0508635   -0.0288994  201 A1IN8 A H20  
3806 H H21  . A1IN8 D .   ? 0.715117 0.295702 0.352307 0.0266921   0.0520089   -0.0389721  201 A1IN8 A H21  
3807 H H23  . A1IN8 D .   ? 0.752661 0.323122 0.383019 -0.00028417 0.0578464   -0.0580195  201 A1IN8 A H23  
3808 H H22  . A1IN8 D .   ? 0.757478 0.306728 0.393766 0.00997401  0.0627026   -0.0465179  201 A1IN8 A H22  
3809 H H25  . A1IN8 D .   ? 0.760028 0.332695 0.403379 -0.0207325  0.0562222   -0.0487246  201 A1IN8 A H25  
3810 H H24  . A1IN8 D .   ? 0.73423  0.318777 0.383039 -0.00407899 0.0550994   -0.0322793  201 A1IN8 A H24  
3811 H H27  . A1IN8 D .   ? 0.731034 0.348264 0.366879 -0.0262707  0.0414934   -0.0527337  201 A1IN8 A H27  
3812 H H26  . A1IN8 D .   ? 0.715327 0.347158 0.370582 -0.0252379  0.0399191   -0.0358295  201 A1IN8 A H26  
3813 H H28  . A1IN8 D .   ? 0.680598 0.35601  0.349736 -0.0229097  0.0292081   -0.0199546  201 A1IN8 A H28  
3814 H H29  . A1IN8 D .   ? 0.659965 0.363583 0.328234 -0.00268351 0.021669    -0.00361878 201 A1IN8 A H29  
3815 H H30  . A1IN8 D .   ? 0.695514 0.36483  0.365175 0.0121392   0.0378088   0.00077892  201 A1IN8 A H30  
3816 H H31  . A1IN8 D .   ? 0.702134 0.387401 0.392126 -0.00142128 0.0384333   0.0052167   201 A1IN8 A H31  
3817 H H33  . A1IN8 D .   ? 0.700653 0.394771 0.39794  0.0218729   0.0453585   0.0244741   201 A1IN8 A H33  
3818 H H32  . A1IN8 D .   ? 0.692631 0.39669  0.380888 0.0189845   0.0331032   0.0196152   201 A1IN8 A H32  
3819 H H35  . A1IN8 D .   ? 0.686533 0.431075 0.42142  -0.0037836  0.0316386   0.0311915   201 A1IN8 A H35  
3820 H H34  . A1IN8 D .   ? 0.677198 0.428689 0.412861 0.0121072   0.0318758   0.0416367   201 A1IN8 A H34  
3821 H H37  . A1IN8 D .   ? 0.686364 0.466639 0.414923 -0.0174475  0.00648394  0.031257    201 A1IN8 A H37  
3822 H H36  . A1IN8 D .   ? 0.680462 0.432726 0.383357 -0.00287511 0.0129634   0.0237917   201 A1IN8 A H36  
3823 H H38  . A1IN8 D .   ? 0.681124 0.423561 0.366277 -0.0305003  0.00661096  -0.00015824 201 A1IN8 A H38  
3824 H H39  . A1IN8 D .   ? 0.681505 0.416618 0.386647 -0.0281924  0.016372    0.00567424  201 A1IN8 A H39  
# 
