data_9GQ2
# 
_entry.id   9GQ2 
# 
_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   9GQ2         pdb_00009gq2 10.2210/pdb9gq2/pdb 
WWPDB D_1292141215 ?            ?                   
# 
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                        9GQ2 
_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},13~{E})-2-cyclohexyl-18,21-dimethoxy-11,16-dioxa-4-azatricyclo[15.2.2.0^{4,9}]henicosa-1(19),13,17,20-tetraene-3,10-dione
;
457.559   2  ?       ?                    ? ? 
3 water       nat water 18.015    27 ?       ?                    ? ? 
# 
_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                 A,B 
_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},13~{E})-2-cyclohexyl-18,21-dimethoxy-11,16-dioxa-4-azatricyclo[15.2.2.0^{4,9}]henicosa-1(19),13,17,20-tetraene-3,10-dione
;
A1IN0 
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 
A1IN0 non-polymer         . 
;(2~{S},9~{S},13~{E})-2-cyclohexyl-18,21-dimethoxy-11,16-dioxa-4-azatricyclo[15.2.2.0^{4,9}]henicosa-1(19),13,17,20-tetraene-3,10-dione
;
? 'C26 H35 N O6'   457.559 
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  ?   ?   ?   A . n 
A 1 2   ALA 2   14  ?   ?   ?   A . n 
A 1 3   PRO 3   15  ?   ?   ?   A . n 
A 1 4   ALA 4   16  ?   ?   ?   A . n 
A 1 5   THR 5   17  ?   ?   ?   A . n 
A 1 6   VAL 6   18  ?   ?   ?   A . n 
A 1 7   THR 7   19  ?   ?   ?   A . n 
A 1 8   GLU 8   20  20  GLU GLU A . n 
A 1 9   GLN 9   21  21  GLN GLN A . n 
A 1 10  GLY 10  22  22  GLY GLY A . n 
A 1 11  GLU 11  23  23  GLU GLU A . n 
A 1 12  ASP 12  24  24  ASP ASP A . n 
A 1 13  ILE 13  25  25  ILE ILE A . n 
A 1 14  THR 14  26  26  THR THR A . n 
A 1 15  SER 15  27  27  SER SER A . n 
A 1 16  LYS 16  28  28  LYS LYS A . n 
A 1 17  LYS 17  29  29  LYS LYS A . n 
A 1 18  ASP 18  30  30  ASP ASP A . n 
A 1 19  ARG 19  31  31  ARG ARG A . n 
A 1 20  GLY 20  32  32  GLY GLY A . n 
A 1 21  VAL 21  33  33  VAL VAL A . n 
A 1 22  LEU 22  34  34  LEU LEU A . n 
A 1 23  LYS 23  35  35  LYS LYS A . n 
A 1 24  ILE 24  36  36  ILE ILE A . n 
A 1 25  VAL 25  37  37  VAL VAL A . n 
A 1 26  LYS 26  38  38  LYS LYS A . n 
A 1 27  ARG 27  39  39  ARG ARG A . n 
A 1 28  VAL 28  40  40  VAL VAL A . n 
A 1 29  GLY 29  41  41  GLY GLY A . n 
A 1 30  ASN 30  42  42  ASN ASN A . n 
A 1 31  GLY 31  43  43  GLY GLY A . n 
A 1 32  GLU 32  44  44  GLU GLU A . n 
A 1 33  GLU 33  45  45  GLU GLU A . n 
A 1 34  THR 34  46  46  THR THR A . n 
A 1 35  PRO 35  47  47  PRO PRO A . n 
A 1 36  MET 36  48  48  MET MET A . n 
A 1 37  ILE 37  49  49  ILE ILE A . n 
A 1 38  GLY 38  50  50  GLY GLY A . n 
A 1 39  ASP 39  51  51  ASP ASP A . n 
A 1 40  LYS 40  52  52  LYS LYS A . n 
A 1 41  VAL 41  53  53  VAL VAL A . n 
A 1 42  TYR 42  54  54  TYR TYR A . n 
A 1 43  VAL 43  55  55  VAL VAL A . n 
A 1 44  HIS 44  56  56  HIS HIS A . n 
A 1 45  TYR 45  57  57  TYR TYR A . n 
A 1 46  LYS 46  58  58  LYS LYS A . n 
A 1 47  GLY 47  59  59  GLY GLY A . n 
A 1 48  LYS 48  60  60  LYS LYS A . n 
A 1 49  LEU 49  61  61  LEU LEU A . n 
A 1 50  SER 50  62  62  SER SER A . n 
A 1 51  ASN 51  63  63  ASN ASN A . n 
A 1 52  GLY 52  64  64  GLY GLY A . n 
A 1 53  LYS 53  65  65  LYS LYS A . n 
A 1 54  LYS 54  66  66  LYS LYS A . n 
A 1 55  PHE 55  67  67  PHE PHE A . n 
A 1 56  ASP 56  68  68  ASP ASP A . n 
A 1 57  SER 57  69  69  SER SER A . n 
A 1 58  SER 58  70  70  SER SER A . n 
A 1 59  HIS 59  71  71  HIS HIS A . n 
A 1 60  ASP 60  72  72  ASP ASP A . n 
A 1 61  ARG 61  73  73  ARG ARG A . n 
A 1 62  ASN 62  74  74  ASN ASN A . n 
A 1 63  GLU 63  75  75  GLU GLU A . n 
A 1 64  PRO 64  76  76  PRO PRO A . n 
A 1 65  PHE 65  77  77  PHE PHE A . n 
A 1 66  VAL 66  78  78  VAL VAL A . n 
A 1 67  PHE 67  79  79  PHE PHE A . n 
A 1 68  SER 68  80  80  SER SER A . n 
A 1 69  LEU 69  81  81  LEU LEU A . n 
A 1 70  GLY 70  82  82  GLY GLY A . n 
A 1 71  LYS 71  83  83  LYS LYS A . n 
A 1 72  GLY 72  84  84  GLY GLY A . n 
A 1 73  GLN 73  85  85  GLN GLN A . n 
A 1 74  VAL 74  86  86  VAL VAL A . n 
A 1 75  ILE 75  87  87  ILE ILE A . n 
A 1 76  LYS 76  88  88  LYS LYS A . n 
A 1 77  ALA 77  89  89  ALA ALA A . n 
A 1 78  TRP 78  90  90  TRP TRP A . n 
A 1 79  ASP 79  91  91  ASP ASP A . n 
A 1 80  ILE 80  92  92  ILE ILE A . n 
A 1 81  GLY 81  93  93  GLY GLY A . n 
A 1 82  VAL 82  94  94  VAL VAL A . n 
A 1 83  ALA 83  95  95  ALA ALA A . n 
A 1 84  THR 84  96  96  THR THR A . n 
A 1 85  MET 85  97  97  MET MET A . n 
A 1 86  LYS 86  98  98  LYS LYS A . n 
A 1 87  LYS 87  99  99  LYS LYS A . n 
A 1 88  GLY 88  100 100 GLY GLY A . n 
A 1 89  GLU 89  101 101 GLU GLU A . n 
A 1 90  ILE 90  102 102 ILE ILE A . n 
A 1 91  ALA 91  103 103 ALA ALA A . n 
A 1 92  HIS 92  104 104 HIS HIS A . n 
A 1 93  LEU 93  105 105 LEU LEU A . n 
A 1 94  LEU 94  106 106 LEU LEU A . n 
A 1 95  ILE 95  107 107 ILE ILE A . n 
A 1 96  LYS 96  108 108 LYS LYS A . n 
A 1 97  PRO 97  109 109 PRO PRO A . n 
A 1 98  GLU 98  110 110 GLU GLU A . n 
A 1 99  TYR 99  111 111 TYR TYR A . n 
A 1 100 ALA 100 112 112 ALA ALA A . n 
A 1 101 TYR 101 113 113 TYR TYR A . n 
A 1 102 GLY 102 114 114 GLY GLY A . n 
A 1 103 SER 103 115 115 SER SER A . n 
A 1 104 ALA 104 116 116 ALA ALA A . n 
A 1 105 GLY 105 117 117 GLY GLY A . n 
A 1 106 SER 106 118 118 SER SER A . n 
A 1 107 LEU 107 119 119 LEU LEU A . n 
A 1 108 PRO 108 120 120 PRO PRO A . n 
A 1 109 LYS 109 121 121 LYS LYS A . n 
A 1 110 ILE 110 122 122 ILE ILE A . n 
A 1 111 PRO 111 123 123 PRO PRO A . n 
A 1 112 SER 112 124 124 SER SER A . n 
A 1 113 ASN 113 125 125 ASN ASN A . n 
A 1 114 ALA 114 126 126 ALA ALA A . n 
A 1 115 THR 115 127 127 THR THR A . n 
A 1 116 LEU 116 128 128 LEU LEU A . n 
A 1 117 PHE 117 129 129 PHE PHE A . n 
A 1 118 PHE 118 130 130 PHE PHE A . n 
A 1 119 GLU 119 131 131 GLU GLU A . n 
A 1 120 ILE 120 132 132 ILE ILE A . n 
A 1 121 GLU 121 133 133 GLU GLU A . n 
A 1 122 LEU 122 134 134 LEU LEU A . n 
A 1 123 LEU 123 135 135 LEU LEU A . n 
A 1 124 ASP 124 136 136 ASP ASP A . n 
A 1 125 PHE 125 137 137 PHE PHE A . n 
A 1 126 LYS 126 138 138 LYS LYS A . n 
A 1 127 GLY 127 139 139 GLY GLY A . n 
A 1 128 GLU 128 140 140 GLU GLU A . n 
B 1 1   GLY 1   13  13  GLY GLY B . n 
B 1 2   ALA 2   14  14  ALA ALA B . n 
B 1 3   PRO 3   15  15  PRO PRO B . n 
B 1 4   ALA 4   16  16  ALA ALA B . n 
B 1 5   THR 5   17  17  THR THR B . n 
B 1 6   VAL 6   18  18  VAL VAL B . n 
B 1 7   THR 7   19  19  THR THR B . n 
B 1 8   GLU 8   20  20  GLU GLU B . n 
B 1 9   GLN 9   21  21  GLN GLN B . n 
B 1 10  GLY 10  22  22  GLY GLY B . n 
B 1 11  GLU 11  23  23  GLU GLU B . n 
B 1 12  ASP 12  24  24  ASP ASP B . n 
B 1 13  ILE 13  25  25  ILE ILE B . n 
B 1 14  THR 14  26  26  THR THR B . n 
B 1 15  SER 15  27  27  SER SER B . n 
B 1 16  LYS 16  28  28  LYS LYS B . n 
B 1 17  LYS 17  29  29  LYS LYS B . n 
B 1 18  ASP 18  30  30  ASP ASP B . n 
B 1 19  ARG 19  31  31  ARG ARG B . n 
B 1 20  GLY 20  32  32  GLY GLY B . n 
B 1 21  VAL 21  33  33  VAL VAL B . n 
B 1 22  LEU 22  34  34  LEU LEU B . n 
B 1 23  LYS 23  35  35  LYS LYS B . n 
B 1 24  ILE 24  36  36  ILE ILE B . n 
B 1 25  VAL 25  37  37  VAL VAL B . n 
B 1 26  LYS 26  38  38  LYS LYS B . n 
B 1 27  ARG 27  39  39  ARG ARG B . n 
B 1 28  VAL 28  40  40  VAL VAL B . n 
B 1 29  GLY 29  41  41  GLY GLY B . n 
B 1 30  ASN 30  42  42  ASN ASN B . n 
B 1 31  GLY 31  43  43  GLY GLY B . n 
B 1 32  GLU 32  44  44  GLU GLU B . n 
B 1 33  GLU 33  45  45  GLU GLU B . n 
B 1 34  THR 34  46  46  THR THR B . n 
B 1 35  PRO 35  47  47  PRO PRO B . n 
B 1 36  MET 36  48  48  MET MET B . n 
B 1 37  ILE 37  49  49  ILE ILE B . n 
B 1 38  GLY 38  50  50  GLY GLY B . n 
B 1 39  ASP 39  51  51  ASP ASP B . n 
B 1 40  LYS 40  52  52  LYS LYS B . n 
B 1 41  VAL 41  53  53  VAL VAL B . n 
B 1 42  TYR 42  54  54  TYR TYR B . n 
B 1 43  VAL 43  55  55  VAL VAL B . n 
B 1 44  HIS 44  56  56  HIS HIS B . n 
B 1 45  TYR 45  57  57  TYR TYR B . n 
B 1 46  LYS 46  58  58  LYS LYS B . n 
B 1 47  GLY 47  59  59  GLY GLY B . n 
B 1 48  LYS 48  60  60  LYS LYS B . n 
B 1 49  LEU 49  61  61  LEU LEU B . n 
B 1 50  SER 50  62  62  SER SER B . n 
B 1 51  ASN 51  63  63  ASN ASN B . n 
B 1 52  GLY 52  64  64  GLY GLY B . n 
B 1 53  LYS 53  65  65  LYS LYS B . n 
B 1 54  LYS 54  66  66  LYS LYS B . n 
B 1 55  PHE 55  67  67  PHE PHE B . n 
B 1 56  ASP 56  68  68  ASP ASP B . n 
B 1 57  SER 57  69  69  SER SER B . n 
B 1 58  SER 58  70  70  SER SER B . n 
B 1 59  HIS 59  71  71  HIS HIS B . n 
B 1 60  ASP 60  72  72  ASP ASP B . n 
B 1 61  ARG 61  73  73  ARG ARG B . n 
B 1 62  ASN 62  74  74  ASN ASN B . n 
B 1 63  GLU 63  75  75  GLU GLU B . n 
B 1 64  PRO 64  76  76  PRO PRO B . n 
B 1 65  PHE 65  77  77  PHE PHE B . n 
B 1 66  VAL 66  78  78  VAL VAL B . n 
B 1 67  PHE 67  79  79  PHE PHE B . n 
B 1 68  SER 68  80  80  SER SER B . n 
B 1 69  LEU 69  81  81  LEU LEU B . n 
B 1 70  GLY 70  82  82  GLY GLY B . n 
B 1 71  LYS 71  83  83  LYS LYS B . n 
B 1 72  GLY 72  84  84  GLY GLY B . n 
B 1 73  GLN 73  85  85  GLN GLN B . n 
B 1 74  VAL 74  86  86  VAL VAL B . n 
B 1 75  ILE 75  87  87  ILE ILE B . n 
B 1 76  LYS 76  88  88  LYS LYS B . n 
B 1 77  ALA 77  89  89  ALA ALA B . n 
B 1 78  TRP 78  90  90  TRP TRP B . n 
B 1 79  ASP 79  91  91  ASP ASP B . n 
B 1 80  ILE 80  92  92  ILE ILE B . n 
B 1 81  GLY 81  93  93  GLY GLY B . n 
B 1 82  VAL 82  94  94  VAL VAL B . n 
B 1 83  ALA 83  95  95  ALA ALA B . n 
B 1 84  THR 84  96  96  THR THR B . n 
B 1 85  MET 85  97  97  MET MET B . n 
B 1 86  LYS 86  98  98  LYS LYS B . n 
B 1 87  LYS 87  99  99  LYS LYS B . n 
B 1 88  GLY 88  100 100 GLY GLY B . n 
B 1 89  GLU 89  101 101 GLU GLU B . n 
B 1 90  ILE 90  102 102 ILE ILE B . n 
B 1 91  ALA 91  103 103 ALA ALA B . n 
B 1 92  HIS 92  104 104 HIS HIS B . n 
B 1 93  LEU 93  105 105 LEU LEU B . n 
B 1 94  LEU 94  106 106 LEU LEU B . n 
B 1 95  ILE 95  107 107 ILE ILE B . n 
B 1 96  LYS 96  108 108 LYS LYS B . n 
B 1 97  PRO 97  109 109 PRO PRO B . n 
B 1 98  GLU 98  110 110 GLU GLU B . n 
B 1 99  TYR 99  111 111 TYR TYR B . n 
B 1 100 ALA 100 112 112 ALA ALA B . n 
B 1 101 TYR 101 113 113 TYR TYR B . n 
B 1 102 GLY 102 114 114 GLY GLY B . n 
B 1 103 SER 103 115 115 SER SER B . n 
B 1 104 ALA 104 116 116 ALA ALA B . n 
B 1 105 GLY 105 117 117 GLY GLY B . n 
B 1 106 SER 106 118 118 SER SER B . n 
B 1 107 LEU 107 119 119 LEU LEU B . n 
B 1 108 PRO 108 120 120 PRO PRO B . n 
B 1 109 LYS 109 121 121 LYS LYS B . n 
B 1 110 ILE 110 122 122 ILE ILE B . n 
B 1 111 PRO 111 123 123 PRO PRO B . n 
B 1 112 SER 112 124 124 SER SER B . n 
B 1 113 ASN 113 125 125 ASN ASN B . n 
B 1 114 ALA 114 126 126 ALA ALA B . n 
B 1 115 THR 115 127 127 THR THR B . n 
B 1 116 LEU 116 128 128 LEU LEU B . n 
B 1 117 PHE 117 129 129 PHE PHE B . n 
B 1 118 PHE 118 130 130 PHE PHE B . n 
B 1 119 GLU 119 131 131 GLU GLU B . n 
B 1 120 ILE 120 132 132 ILE ILE B . n 
B 1 121 GLU 121 133 133 GLU GLU B . n 
B 1 122 LEU 122 134 134 LEU LEU B . n 
B 1 123 LEU 123 135 135 LEU LEU B . n 
B 1 124 ASP 124 136 136 ASP ASP B . n 
B 1 125 PHE 125 137 137 PHE PHE B . n 
B 1 126 LYS 126 138 138 LYS LYS B . n 
B 1 127 GLY 127 139 139 GLY GLY B . n 
B 1 128 GLU 128 140 140 GLU GLU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IN0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IN0 
_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 A1IN0 1  201 201 A1IN0 PDB A . 
D 2 A1IN0 1  201 201 A1IN0 PDB B . 
E 3 HOH   1  301 17  HOH   HOH A . 
E 3 HOH   2  302 15  HOH   HOH A . 
E 3 HOH   3  303 14  HOH   HOH A . 
E 3 HOH   4  304 12  HOH   HOH A . 
E 3 HOH   5  305 23  HOH   HOH A . 
E 3 HOH   6  306 3   HOH   HOH A . 
E 3 HOH   7  307 25  HOH   HOH A . 
E 3 HOH   8  308 18  HOH   HOH A . 
E 3 HOH   9  309 20  HOH   HOH A . 
E 3 HOH   10 310 24  HOH   HOH A . 
F 3 HOH   1  301 1   HOH   HOH B . 
F 3 HOH   2  302 9   HOH   HOH B . 
F 3 HOH   3  303 5   HOH   HOH B . 
F 3 HOH   4  304 11  HOH   HOH B . 
F 3 HOH   5  305 16  HOH   HOH B . 
F 3 HOH   6  306 8   HOH   HOH B . 
F 3 HOH   7  307 4   HOH   HOH B . 
F 3 HOH   8  308 2   HOH   HOH B . 
F 3 HOH   9  309 13  HOH   HOH B . 
F 3 HOH   10 310 26  HOH   HOH B . 
F 3 HOH   11 311 7   HOH   HOH B . 
F 3 HOH   12 312 10  HOH   HOH B . 
F 3 HOH   13 313 27  HOH   HOH B . 
F 3 HOH   14 314 6   HOH   HOH B . 
F 3 HOH   15 315 22  HOH   HOH B . 
F 3 HOH   16 316 19  HOH   HOH B . 
F 3 HOH   17 317 21  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 20  ? CG  ? A GLU 8   CG  
2   1 Y 1 A GLU 20  ? CD  ? A GLU 8   CD  
3   1 Y 1 A GLU 20  ? OE1 ? A GLU 8   OE1 
4   1 Y 1 A GLU 20  ? OE2 ? A GLU 8   OE2 
5   1 Y 1 A LYS 28  ? CG  ? A LYS 16  CG  
6   1 Y 1 A LYS 28  ? CD  ? A LYS 16  CD  
7   1 Y 1 A LYS 28  ? CE  ? A LYS 16  CE  
8   1 Y 1 A LYS 28  ? NZ  ? A LYS 16  NZ  
9   1 Y 1 A GLU 44  ? CG  ? A GLU 32  CG  
10  1 Y 1 A GLU 44  ? CD  ? A GLU 32  CD  
11  1 Y 1 A GLU 44  ? OE1 ? A GLU 32  OE1 
12  1 Y 1 A GLU 44  ? OE2 ? A GLU 32  OE2 
13  1 Y 1 A LYS 52  ? CG  ? A LYS 40  CG  
14  1 Y 1 A LYS 52  ? CD  ? A LYS 40  CD  
15  1 Y 1 A LYS 52  ? CE  ? A LYS 40  CE  
16  1 Y 1 A LYS 52  ? NZ  ? A LYS 40  NZ  
17  1 Y 1 A LYS 58  ? CG  ? A LYS 46  CG  
18  1 Y 1 A LYS 58  ? CD  ? A LYS 46  CD  
19  1 Y 1 A LYS 58  ? CE  ? A LYS 46  CE  
20  1 Y 1 A LYS 58  ? NZ  ? A LYS 46  NZ  
21  1 Y 1 A LYS 65  ? CG  ? A LYS 53  CG  
22  1 Y 1 A LYS 65  ? CD  ? A LYS 53  CD  
23  1 Y 1 A LYS 65  ? CE  ? A LYS 53  CE  
24  1 Y 1 A LYS 65  ? NZ  ? A LYS 53  NZ  
25  1 Y 1 A LYS 66  ? CG  ? A LYS 54  CG  
26  1 Y 1 A LYS 66  ? CD  ? A LYS 54  CD  
27  1 Y 1 A LYS 66  ? CE  ? A LYS 54  CE  
28  1 Y 1 A LYS 66  ? NZ  ? A LYS 54  NZ  
29  1 Y 1 A ARG 73  ? CG  ? A ARG 61  CG  
30  1 Y 1 A ARG 73  ? CD  ? A ARG 61  CD  
31  1 Y 1 A ARG 73  ? NE  ? A ARG 61  NE  
32  1 Y 1 A ARG 73  ? CZ  ? A ARG 61  CZ  
33  1 Y 1 A ARG 73  ? NH1 ? A ARG 61  NH1 
34  1 Y 1 A ARG 73  ? NH2 ? A ARG 61  NH2 
35  1 Y 1 A ASN 74  ? CG  ? A ASN 62  CG  
36  1 Y 1 A ASN 74  ? OD1 ? A ASN 62  OD1 
37  1 Y 1 A ASN 74  ? ND2 ? A ASN 62  ND2 
38  1 Y 1 A GLU 75  ? CG  ? A GLU 63  CG  
39  1 Y 1 A GLU 75  ? CD  ? A GLU 63  CD  
40  1 Y 1 A GLU 75  ? OE1 ? A GLU 63  OE1 
41  1 Y 1 A GLU 75  ? OE2 ? A GLU 63  OE2 
42  1 Y 1 A LYS 83  ? CG  ? A LYS 71  CG  
43  1 Y 1 A LYS 83  ? CD  ? A LYS 71  CD  
44  1 Y 1 A LYS 83  ? CE  ? A LYS 71  CE  
45  1 Y 1 A LYS 83  ? NZ  ? A LYS 71  NZ  
46  1 Y 1 A LYS 88  ? CG  ? A LYS 76  CG  
47  1 Y 1 A LYS 88  ? CD  ? A LYS 76  CD  
48  1 Y 1 A LYS 88  ? CE  ? A LYS 76  CE  
49  1 Y 1 A LYS 88  ? NZ  ? A LYS 76  NZ  
50  1 Y 1 A LYS 121 ? CG  ? A LYS 109 CG  
51  1 Y 1 A LYS 121 ? CD  ? A LYS 109 CD  
52  1 Y 1 A LYS 121 ? CE  ? A LYS 109 CE  
53  1 Y 1 A LYS 121 ? NZ  ? A LYS 109 NZ  
54  1 Y 1 A LYS 138 ? CG  ? A LYS 126 CG  
55  1 Y 1 A LYS 138 ? CD  ? A LYS 126 CD  
56  1 Y 1 A LYS 138 ? CE  ? A LYS 126 CE  
57  1 Y 1 A LYS 138 ? NZ  ? A LYS 126 NZ  
58  1 Y 1 A GLU 140 ? CG  ? A GLU 128 CG  
59  1 Y 1 A GLU 140 ? CD  ? A GLU 128 CD  
60  1 Y 1 A GLU 140 ? OE1 ? A GLU 128 OE1 
61  1 Y 1 A GLU 140 ? OE2 ? A GLU 128 OE2 
62  1 Y 1 B GLU 44  ? CG  ? B GLU 32  CG  
63  1 Y 1 B GLU 44  ? CD  ? B GLU 32  CD  
64  1 Y 1 B GLU 44  ? OE1 ? B GLU 32  OE1 
65  1 Y 1 B GLU 44  ? OE2 ? B GLU 32  OE2 
66  1 Y 1 B GLU 45  ? CG  ? B GLU 33  CG  
67  1 Y 1 B GLU 45  ? CD  ? B GLU 33  CD  
68  1 Y 1 B GLU 45  ? OE1 ? B GLU 33  OE1 
69  1 Y 1 B GLU 45  ? OE2 ? B GLU 33  OE2 
70  1 Y 1 B LYS 65  ? CG  ? B LYS 53  CG  
71  1 Y 1 B LYS 65  ? CD  ? B LYS 53  CD  
72  1 Y 1 B LYS 65  ? CE  ? B LYS 53  CE  
73  1 Y 1 B LYS 65  ? NZ  ? B LYS 53  NZ  
74  1 Y 1 B LYS 66  ? CG  ? B LYS 54  CG  
75  1 Y 1 B LYS 66  ? CD  ? B LYS 54  CD  
76  1 Y 1 B LYS 66  ? CE  ? B LYS 54  CE  
77  1 Y 1 B LYS 66  ? NZ  ? B LYS 54  NZ  
78  1 Y 1 B ARG 73  ? CG  ? B ARG 61  CG  
79  1 Y 1 B ARG 73  ? CD  ? B ARG 61  CD  
80  1 Y 1 B ARG 73  ? NE  ? B ARG 61  NE  
81  1 Y 1 B ARG 73  ? CZ  ? B ARG 61  CZ  
82  1 Y 1 B ARG 73  ? NH1 ? B ARG 61  NH1 
83  1 Y 1 B ARG 73  ? NH2 ? B ARG 61  NH2 
84  1 Y 1 B ASN 74  ? CG  ? B ASN 62  CG  
85  1 Y 1 B ASN 74  ? OD1 ? B ASN 62  OD1 
86  1 Y 1 B ASN 74  ? ND2 ? B ASN 62  ND2 
87  1 Y 1 B LYS 83  ? CG  ? B LYS 71  CG  
88  1 Y 1 B LYS 83  ? CD  ? B LYS 71  CD  
89  1 Y 1 B LYS 83  ? CE  ? B LYS 71  CE  
90  1 Y 1 B LYS 83  ? NZ  ? B LYS 71  NZ  
91  1 Y 1 B LYS 88  ? CG  ? B LYS 76  CG  
92  1 Y 1 B LYS 88  ? CD  ? B LYS 76  CD  
93  1 Y 1 B LYS 88  ? CE  ? B LYS 76  CE  
94  1 Y 1 B LYS 88  ? NZ  ? B LYS 76  NZ  
95  1 Y 1 B LYS 98  ? CG  ? B LYS 86  CG  
96  1 Y 1 B LYS 98  ? CD  ? B LYS 86  CD  
97  1 Y 1 B LYS 98  ? CE  ? B LYS 86  CE  
98  1 Y 1 B LYS 98  ? NZ  ? B LYS 86  NZ  
99  1 Y 1 B LYS 99  ? CG  ? B LYS 87  CG  
100 1 Y 1 B LYS 99  ? CD  ? B LYS 87  CD  
101 1 Y 1 B LYS 99  ? CE  ? B LYS 87  CE  
102 1 Y 1 B LYS 99  ? NZ  ? B LYS 87  NZ  
103 1 Y 1 B LYS 121 ? CG  ? B LYS 109 CG  
104 1 Y 1 B LYS 121 ? CD  ? B LYS 109 CD  
105 1 Y 1 B LYS 121 ? CE  ? B LYS 109 CE  
106 1 Y 1 B LYS 121 ? NZ  ? B LYS 109 NZ  
107 1 Y 1 B LYS 138 ? CG  ? B LYS 126 CG  
108 1 Y 1 B LYS 138 ? CD  ? B LYS 126 CD  
109 1 Y 1 B LYS 138 ? CE  ? B LYS 126 CE  
110 1 Y 1 B LYS 138 ? NZ  ? B LYS 126 NZ  
111 1 Y 1 B GLU 140 ? CG  ? B GLU 128 CG  
112 1 Y 1 B GLU 140 ? CD  ? B GLU 128 CD  
113 1 Y 1 B GLU 140 ? OE1 ? B GLU 128 OE1 
114 1 Y 1 B 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                     9GQ2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.87 
_cell.length_a_esd                 ? 
_cell.length_b                     48.87 
_cell.length_b_esd                 ? 
_cell.length_c                     193.969 
_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                         9GQ2 
_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                   9GQ2 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.39 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.48 
_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                                       9GQ2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.30 
_reflns.d_resolution_low                               48.49 
_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                                     12744 
_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                                10.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          32.1 
_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                                0.040 
_reflns.pdbx_Rpim_I_all                                0.017 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.036 
_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 
8.61 48.49 ? 60.1 ? ? ? ? 308  ? ? ? ? ? ? ? ? ? ? ? 8.0  0.78 ? ? 0.025 0.011 ? 1 ? 1.000 ? ? 99.2  ? 0.023 ? ? ? ? ? ? ? ? ? 
2.30 2.39  ? 7.4  ? ? ? ? 1292 ? ? ? ? ? ? ? ? ? ? ? 10.3 1.05 ? ? 0.322 0.136 ? 2 ? 0.974 ? ? 100.0 ? 0.291 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.527 
_refine.aniso_B[1][2]                            -0.263 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -0.527 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            1.709 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               65.231 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.944 
_refine.correlation_coeff_Fo_to_Fc_free          0.914 
_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                                 9GQ2 
_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                            2.301 
_refine.ls_d_res_low                             42.359 
_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                     12691 
_refine.ls_number_reflns_R_free                  660 
_refine.ls_number_reflns_R_work                  12031 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.913 
_refine.ls_percent_reflns_R_free                 5.201 
_refine.ls_R_factor_all                          0.234 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2879 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2309 
_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                       0.357 
_refine.pdbx_overall_ESU_R_Free                  0.269 
_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                             21.656 
_refine.overall_SU_ML                            0.235 
_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                       2.301 
_refine_hist.d_res_low                        42.359 
_refine_hist.number_atoms_solvent             27 
_refine_hist.number_atoms_total               1911 
_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        1818 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         66 
_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' ? 0.013  0.012  1929 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.016  1750 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 2.369  1.844  2618 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.122  1.807  4069 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 9.355  5.000  247  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 3.369  5.000  4    ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 15.041 10.000 281  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.929 10.000 69   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.108  0.200  289  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 1.738  0.200  26   ? r_chiral_restr_other           ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  2224 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  400  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.216  0.200  389  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.202  0.200  1718 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.186  0.200  998  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.096  0.200  1064 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.201  0.200  49   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.189  0.200  8    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.174  0.200  21   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.131  0.200  3    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 3.749  2.999  1000 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.749  2.999  1000 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 5.264  5.387  1243 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.263  5.385  1244 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 3.570  3.124  929  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.568  3.122  930  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 5.147  5.636  1375 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.145  5.634  1376 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 7.414  28.335 2122 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 7.414  28.314 2120 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.125  0.050  3256 ? 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 ? ? 0.12537 ? 0.05008 1 'Local ncs' ? A ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.12537 ? 0.05008 2 'Local ncs' ? B ? ? ? 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' 2.301  2.361  921 . 38 883 100.0000 . 0.297 . . 0.290 . . . . . 0.260 . 20 . 0.956 0.909 0.465 
'X-RAY DIFFRACTION' 2.361  2.425  893 . 40 853 100.0000 . 0.311 . . 0.310 . . . . . 0.275 . 20 . 0.943 0.922 0.345 
'X-RAY DIFFRACTION' 2.425  2.495  864 . 41 823 100.0000 . 0.321 . . 0.320 . . . . . 0.287 . 20 . 0.936 0.927 0.332 
'X-RAY DIFFRACTION' 2.495  2.572  854 . 65 789 100.0000 . 0.282 . . 0.282 . . . . . 0.254 . 20 . 0.948 0.948 0.282 
'X-RAY DIFFRACTION' 2.572  2.656  792 . 53 739 100.0000 . 0.298 . . 0.291 . . . . . 0.262 . 20 . 0.942 0.901 0.414 
'X-RAY DIFFRACTION' 2.656  2.748  802 . 37 765 100.0000 . 0.279 . . 0.277 . . . . . 0.253 . 20 . 0.950 0.928 0.332 
'X-RAY DIFFRACTION' 2.748  2.852  768 . 46 722 100.0000 . 0.285 . . 0.282 . . . . . 0.263 . 20 . 0.943 0.927 0.325 
'X-RAY DIFFRACTION' 2.852  2.968  718 . 35 682 99.8607  . 0.276 . . 0.273 . . . . . 0.259 . 20 . 0.947 0.915 0.355 
'X-RAY DIFFRACTION' 2.968  3.099  728 . 41 686 99.8626  . 0.284 . . 0.280 . . . . . 0.272 . 20 . 0.947 0.915 0.343 
'X-RAY DIFFRACTION' 3.099  3.249  704 . 35 669 100.0000 . 0.261 . . 0.259 . . . . . 0.257 . 20 . 0.957 0.938 0.291 
'X-RAY DIFFRACTION' 3.249  3.424  620 . 37 583 100.0000 . 0.279 . . 0.280 . . . . . 0.281 . 20 . 0.954 0.949 0.263 
'X-RAY DIFFRACTION' 3.424  3.630  632 . 41 590 99.8418  . 0.281 . . 0.275 . . . . . 0.281 . 20 . 0.963 0.917 0.369 
'X-RAY DIFFRACTION' 3.630  3.879  578 . 27 551 100.0000 . 0.255 . . 0.250 . . . . . 0.259 . 20 . 0.967 0.899 0.379 
'X-RAY DIFFRACTION' 3.879  4.186  560 . 25 535 100.0000 . 0.194 . . 0.195 . . . . . 0.208 . 20 . 0.978 0.976 0.189 
'X-RAY DIFFRACTION' 4.186  4.582  506 . 26 479 99.8024  . 0.141 . . 0.139 . . . . . 0.154 . 20 . 0.989 0.985 0.175 
'X-RAY DIFFRACTION' 4.582  5.115  469 . 23 446 100.0000 . 0.127 . . 0.124 . . . . . 0.140 . 20 . 0.990 0.981 0.185 
'X-RAY DIFFRACTION' 5.115  5.892  431 . 27 403 99.7680  . 0.173 . . 0.171 . . . . . 0.190 . 20 . 0.983 0.979 0.205 
'X-RAY DIFFRACTION' 5.892  7.181  371 . 6  364 99.7305  . 0.236 . . 0.234 . . . . . 0.272 . 20 . 0.974 0.935 0.307 
'X-RAY DIFFRACTION' 7.181  10.013 291 . 8  282 99.6564  . 0.220 . . 0.220 . . . . . 0.278 . 20 . 0.972 0.983 0.225 
'X-RAY DIFFRACTION' 10.013 42.359 199 . 9  187 98.4925  . 0.299 . . 0.292 . . . . . 0.373 . 20 . 0.932 0.915 0.504 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 A 
2 1 B 
# 
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 GLU 8 . A GLY 127 . A GLU 20 A GLY 139 ? ? 
1 2 1 B GLU 8 . B GLY 127 . B GLU 20 B GLY 139 ? ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   'Local NCS retraints between domains:       1       2' 
# 
_struct.entry_id                     9GQ2 
_struct.title                        'The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog p5(1,1)-(E)' 
_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        9GQ2 
_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 9GQ2 A 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
2 1 9GQ2 B 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 9GQ2 GLY A 1  ? UNP Q13451 ?   ?   'expression tag'      13  1  
1 9GQ2 ALA A 2  ? UNP Q13451 ?   ?   'expression tag'      14  2  
1 9GQ2 PRO A 3  ? UNP Q13451 ?   ?   'expression tag'      15  3  
1 9GQ2 THR A 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  4  
1 9GQ2 ALA A 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 5  
1 9GQ2 ILE A 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 6  
2 9GQ2 GLY B 1  ? UNP Q13451 ?   ?   'expression tag'      13  7  
2 9GQ2 ALA B 2  ? UNP Q13451 ?   ?   'expression tag'      14  8  
2 9GQ2 PRO B 3  ? UNP Q13451 ?   ?   'expression tag'      15  9  
2 9GQ2 THR B 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  10 
2 9GQ2 ALA B 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 11 
2 9GQ2 ILE B 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 HIS A 59 ? ASN A 62  ? HIS A 71  ASN A 74  5 ? 4 
HELX_P HELX_P2 AA2 ILE A 75 ? ALA A 83  ? ILE A 87  ALA A 95  1 ? 9 
HELX_P HELX_P3 AA3 PRO A 97 ? ALA A 100 ? PRO A 109 ALA A 112 5 ? 4 
HELX_P HELX_P4 AA4 PRO B 3  ? GLY B 10  ? PRO B 15  GLY B 22  1 ? 8 
HELX_P HELX_P5 AA5 HIS B 59 ? ASN B 62  ? HIS B 71  ASN B 74  5 ? 4 
HELX_P HELX_P6 AA6 ILE B 75 ? ALA B 83  ? ILE B 87  ALA B 95  1 ? 9 
HELX_P HELX_P7 AA7 PRO B 97 ? ALA B 100 ? PRO B 109 ALA B 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 A PRO 108 A ? PRO 120 A 1 -1.67 
2 LEU 107 B . ? LEU 119 B PRO 108 B ? PRO 120 B 1 -6.02 
# 
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 A 23  ASP A 24  
AA1 2 VAL A 21  ? ARG A 27  ? VAL A 33  ARG A 39  
AA1 3 ILE A 90  ? ILE A 95  ? ILE A 102 ILE A 107 
AA1 4 LEU A 116 ? LYS A 126 ? LEU A 128 LYS A 138 
AA1 5 LYS A 40  ? LEU A 49  ? LYS A 52  LEU A 61  
AA1 6 PHE A 55  ? SER A 57  ? PHE A 67  SER A 69  
AA2 1 GLU A 11  ? ASP A 12  ? GLU A 23  ASP A 24  
AA2 2 VAL A 21  ? ARG A 27  ? VAL A 33  ARG A 39  
AA2 3 ILE A 90  ? ILE A 95  ? ILE A 102 ILE A 107 
AA2 4 LEU A 116 ? LYS A 126 ? LEU A 128 LYS A 138 
AA2 5 LYS A 40  ? LEU A 49  ? LYS A 52  LEU A 61  
AA2 6 PHE A 65  ? SER A 68  ? PHE A 77  SER A 80  
AA3 1 GLU B 11  ? ASP B 12  ? GLU B 23  ASP B 24  
AA3 2 VAL B 21  ? ARG B 27  ? VAL B 33  ARG B 39  
AA3 3 ILE B 90  ? ILE B 95  ? ILE B 102 ILE B 107 
AA3 4 LEU B 116 ? LYS B 126 ? LEU B 128 LYS B 138 
AA3 5 LYS B 40  ? LEU B 49  ? LYS B 52  LEU B 61  
AA3 6 PHE B 55  ? SER B 57  ? PHE B 67  SER B 69  
AA4 1 GLU B 11  ? ASP B 12  ? GLU B 23  ASP B 24  
AA4 2 VAL B 21  ? ARG B 27  ? VAL B 33  ARG B 39  
AA4 3 ILE B 90  ? ILE B 95  ? ILE B 102 ILE B 107 
AA4 4 LEU B 116 ? LYS B 126 ? LEU B 128 LYS B 138 
AA4 5 LYS B 40  ? LEU B 49  ? LYS B 52  LEU B 61  
AA4 6 PHE B 65  ? SER B 68  ? PHE B 77  SER B 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 A 23  O LYS A 23  ? O LYS A 35  
AA1 2 3 N LYS A 26  ? N LYS A 38  O ILE A 90  ? O ILE A 102 
AA1 3 4 N ILE A 95  ? N ILE A 107 O LEU A 116 ? O LEU A 128 
AA1 4 5 O ASP A 124 ? O ASP A 136 N TYR A 42  ? N TYR A 54  
AA1 5 6 N GLY A 47  ? N GLY A 59  O ASP A 56  ? O ASP A 68  
AA2 1 2 N GLU A 11  ? N GLU A 23  O LYS A 23  ? O LYS A 35  
AA2 2 3 N LYS A 26  ? N LYS A 38  O ILE A 90  ? O ILE A 102 
AA2 3 4 N ILE A 95  ? N ILE A 107 O LEU A 116 ? O LEU A 128 
AA2 4 5 O ASP A 124 ? O ASP A 136 N TYR A 42  ? N TYR A 54  
AA2 5 6 N VAL A 41  ? N VAL A 53  O PHE A 67  ? O PHE A 79  
AA3 1 2 N GLU B 11  ? N GLU B 23  O LYS B 23  ? O LYS B 35  
AA3 2 3 N LYS B 26  ? N LYS B 38  O ILE B 90  ? O ILE B 102 
AA3 3 4 N ALA B 91  ? N ALA B 103 O ILE B 120 ? O ILE B 132 
AA3 4 5 O GLU B 121 ? O GLU B 133 N HIS B 44  ? N HIS B 56  
AA3 5 6 N GLY B 47  ? N GLY B 59  O ASP B 56  ? O ASP B 68  
AA4 1 2 N GLU B 11  ? N GLU B 23  O LYS B 23  ? O LYS B 35  
AA4 2 3 N LYS B 26  ? N LYS B 38  O ILE B 90  ? O ILE B 102 
AA4 3 4 N ALA B 91  ? N ALA B 103 O ILE B 120 ? O ILE B 132 
AA4 4 5 O GLU B 121 ? O GLU B 133 N HIS B 44  ? N HIS B 56  
AA4 5 6 N VAL B 41  ? N VAL B 53  O PHE B 67  ? O PHE B 79  
# 
_pdbx_entry_details.entry_id                   9GQ2 
_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 HD1 B HIS 56  ? ? OG B SER 70  ? ? 1.32 
2 1 HG  A SER 124 ? ? OG B SER 118 ? ? 1.50 
# 
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 CG A MET 48 ? ? SD A MET 48 ? ? CE A MET 48 ? ? 112.51 100.20 12.31  1.60 N 
2 1 CB B GLN 21 ? ? CA B GLN 21 ? ? C  B GLN 21 ? ? 98.24  110.40 -12.16 2.00 N 
3 1 CG B MET 48 ? ? SD B MET 48 ? ? CE B MET 48 ? ? 112.16 100.20 11.96  1.60 N 
4 1 CB B LYS 65 ? ? CA B LYS 65 ? ? C  B LYS 65 ? ? 124.02 110.40 13.62  2.00 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 ASN A 74  ? ? 23.31   60.37   
2 1 ALA A 112 ? ? -141.26 -104.30 
3 1 SER A 118 ? ? -153.27 67.74   
4 1 ASN B 74  ? ? 27.29   58.29   
5 1 GLU B 75  ? ? -174.65 145.46  
6 1 PRO B 76  ? ? -49.66  160.10  
7 1 ALA B 112 ? ? -136.66 -101.19 
# 
_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     317 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_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 -9.1520  16.2964 28.1769 0.1697 ? -0.0274 ? -0.0134 ? 0.2233 ? -0.1178 ? 0.1793 ? 5.0787 ? 0.0174  
? -0.4037 ? 4.3839 ? 1.3216 ? 6.3662 ? -0.3552 ? 0.4264  ? 0.3329 ? -0.0327 ? -0.0683 ? -0.1081 ? -0.2082 ? -0.1118 ? 0.4235  ? 
2 'X-RAY DIFFRACTION' ? refined -18.4689 -0.4046 3.3171  0.2832 ? -0.1327 ? 0.0361  ? 0.1011 ? -0.1232 ? 0.4321 ? 7.4825 ? -2.3916 
? 0.2191  ? 8.1547 ? 0.2917 ? 6.4001 ? 0.0340  ? -0.3699 ? 0.3234 ? -0.5422 ? 0.0596  ? 1.3723  ? 0.4974  ? -0.0993 ? -0.0937 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 20 ? ? ? A 201 ? ALL ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 13 ? ? ? B 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 ? A GLY 1 
2 1 Y 1 A ALA 14 ? A ALA 2 
3 1 Y 1 A PRO 15 ? A PRO 3 
4 1 Y 1 A ALA 16 ? A ALA 4 
5 1 Y 1 A THR 17 ? A THR 5 
6 1 Y 1 A VAL 18 ? A VAL 6 
7 1 Y 1 A THR 19 ? A THR 7 
# 
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 
A1IN0 CAK  C N N 1   
A1IN0 CAL  C N N 2   
A1IN0 CAM  C N N 3   
A1IN0 CAN  C N N 4   
A1IN0 CAO  C N N 5   
A1IN0 CAJ  C N N 6   
A1IN0 CAI  C N S 7   
A1IN0 CAB  C N N 8   
A1IN0 OAA  O N N 9   
A1IN0 N    N N N 10  
A1IN0 CAH  C N N 11  
A1IN0 CAG  C N N 12  
A1IN0 CAF  C N N 13  
A1IN0 CB   C N N 14  
A1IN0 CA   C N S 15  
A1IN0 C    C N N 16  
A1IN0 O    O N N 17  
A1IN0 OBA  O N N 18  
A1IN0 CAZ  C N N 19  
A1IN0 CAY  C N N 20  
A1IN0 CAX  C N N 21  
A1IN0 CAW  C N N 22  
A1IN0 OAV  O N N 23  
A1IN0 CAU  C Y N 24  
A1IN0 CAR  C Y N 25  
A1IN0 OAS  O N N 26  
A1IN0 CAT  C N N 27  
A1IN0 CAQ  C Y N 28  
A1IN0 CAP  C Y N 29  
A1IN0 CBG  C Y N 30  
A1IN0 CBD  C Y N 31  
A1IN0 OBE  O N N 32  
A1IN0 CBF  C N N 33  
A1IN0 HAK  H N N 34  
A1IN0 HB6  H N N 35  
A1IN0 HAL  H N N 36  
A1IN0 HB7  H N N 37  
A1IN0 HAM  H N N 38  
A1IN0 HB8  H N N 39  
A1IN0 HAN  H N N 40  
A1IN0 HB9  H N N 41  
A1IN0 HCA  H N N 42  
A1IN0 HAO  H N N 43  
A1IN0 HAJ  H N N 44  
A1IN0 HAI  H N N 45  
A1IN0 HAH  H N N 46  
A1IN0 HB5  H N N 47  
A1IN0 HAG  H N N 48  
A1IN0 HB4  H N N 49  
A1IN0 HAF  H N N 50  
A1IN0 HB3  H N N 51  
A1IN0 HB2  H N N 52  
A1IN0 HB1  H N N 53  
A1IN0 HA   H N N 54  
A1IN0 HCE  H N N 55  
A1IN0 HAZ  H N N 56  
A1IN0 HAY  H N N 57  
A1IN0 HAX  H N N 58  
A1IN0 HCD  H N N 59  
A1IN0 HAW  H N N 60  
A1IN0 HCC  H N N 61  
A1IN0 HAT  H N N 62  
A1IN0 HCB  H N N 63  
A1IN0 HAQ  H N N 64  
A1IN0 HBG  H N N 65  
A1IN0 HCG  H N N 66  
A1IN0 HBF  H N N 67  
A1IN0 HCF  H N N 68  
ALA   N    N N N 69  
ALA   CA   C N S 70  
ALA   C    C N N 71  
ALA   O    O N N 72  
ALA   CB   C N N 73  
ALA   OXT  O N N 74  
ALA   H    H N N 75  
ALA   H2   H N N 76  
ALA   HA   H N N 77  
ALA   HB1  H N N 78  
ALA   HB2  H N N 79  
ALA   HB3  H N N 80  
ALA   HXT  H N N 81  
ARG   N    N N N 82  
ARG   CA   C N S 83  
ARG   C    C N N 84  
ARG   O    O N N 85  
ARG   CB   C N N 86  
ARG   CG   C N N 87  
ARG   CD   C N N 88  
ARG   NE   N N N 89  
ARG   CZ   C N N 90  
ARG   NH1  N N N 91  
ARG   NH2  N N N 92  
ARG   OXT  O N N 93  
ARG   H    H N N 94  
ARG   H2   H N N 95  
ARG   HA   H N N 96  
ARG   HB2  H N N 97  
ARG   HB3  H N N 98  
ARG   HG2  H N N 99  
ARG   HG3  H N N 100 
ARG   HD2  H N N 101 
ARG   HD3  H N N 102 
ARG   HE   H N N 103 
ARG   HH11 H N N 104 
ARG   HH12 H N N 105 
ARG   HH21 H N N 106 
ARG   HH22 H N N 107 
ARG   HXT  H N N 108 
ASN   N    N N N 109 
ASN   CA   C N S 110 
ASN   C    C N N 111 
ASN   O    O N N 112 
ASN   CB   C N N 113 
ASN   CG   C N N 114 
ASN   OD1  O N N 115 
ASN   ND2  N N N 116 
ASN   OXT  O N N 117 
ASN   H    H N N 118 
ASN   H2   H N N 119 
ASN   HA   H N N 120 
ASN   HB2  H N N 121 
ASN   HB3  H N N 122 
ASN   HD21 H N N 123 
ASN   HD22 H N N 124 
ASN   HXT  H N N 125 
ASP   N    N N N 126 
ASP   CA   C N S 127 
ASP   C    C N N 128 
ASP   O    O N N 129 
ASP   CB   C N N 130 
ASP   CG   C N N 131 
ASP   OD1  O N N 132 
ASP   OD2  O N N 133 
ASP   OXT  O N N 134 
ASP   H    H N N 135 
ASP   H2   H N N 136 
ASP   HA   H N N 137 
ASP   HB2  H N N 138 
ASP   HB3  H N N 139 
ASP   HD2  H N N 140 
ASP   HXT  H N N 141 
CYS   N    N N N 142 
CYS   CA   C N R 143 
CYS   C    C N N 144 
CYS   O    O N N 145 
CYS   CB   C N N 146 
CYS   SG   S N N 147 
CYS   OXT  O N N 148 
CYS   H    H N N 149 
CYS   H2   H N N 150 
CYS   HA   H N N 151 
CYS   HB2  H N N 152 
CYS   HB3  H N N 153 
CYS   HG   H N N 154 
CYS   HXT  H N N 155 
GLN   N    N N N 156 
GLN   CA   C N S 157 
GLN   C    C N N 158 
GLN   O    O N N 159 
GLN   CB   C N N 160 
GLN   CG   C N N 161 
GLN   CD   C N N 162 
GLN   OE1  O N N 163 
GLN   NE2  N N N 164 
GLN   OXT  O N N 165 
GLN   H    H N N 166 
GLN   H2   H N N 167 
GLN   HA   H N N 168 
GLN   HB2  H N N 169 
GLN   HB3  H N N 170 
GLN   HG2  H N N 171 
GLN   HG3  H N N 172 
GLN   HE21 H N N 173 
GLN   HE22 H N N 174 
GLN   HXT  H N N 175 
GLU   N    N N N 176 
GLU   CA   C N S 177 
GLU   C    C N N 178 
GLU   O    O N N 179 
GLU   CB   C N N 180 
GLU   CG   C N N 181 
GLU   CD   C N N 182 
GLU   OE1  O N N 183 
GLU   OE2  O N N 184 
GLU   OXT  O N N 185 
GLU   H    H N N 186 
GLU   H2   H N N 187 
GLU   HA   H N N 188 
GLU   HB2  H N N 189 
GLU   HB3  H N N 190 
GLU   HG2  H N N 191 
GLU   HG3  H N N 192 
GLU   HE2  H N N 193 
GLU   HXT  H N N 194 
GLY   N    N N N 195 
GLY   CA   C N N 196 
GLY   C    C N N 197 
GLY   O    O N N 198 
GLY   OXT  O N N 199 
GLY   H    H N N 200 
GLY   H2   H N N 201 
GLY   HA2  H N N 202 
GLY   HA3  H N N 203 
GLY   HXT  H N N 204 
HIS   N    N N N 205 
HIS   CA   C N S 206 
HIS   C    C N N 207 
HIS   O    O N N 208 
HIS   CB   C N N 209 
HIS   CG   C Y N 210 
HIS   ND1  N Y N 211 
HIS   CD2  C Y N 212 
HIS   CE1  C Y N 213 
HIS   NE2  N Y N 214 
HIS   OXT  O N N 215 
HIS   H    H N N 216 
HIS   H2   H N N 217 
HIS   HA   H N N 218 
HIS   HB2  H N N 219 
HIS   HB3  H N N 220 
HIS   HD1  H N N 221 
HIS   HD2  H N N 222 
HIS   HE1  H N N 223 
HIS   HE2  H N N 224 
HIS   HXT  H N N 225 
HOH   O    O N N 226 
HOH   H1   H N N 227 
HOH   H2   H N N 228 
ILE   N    N N N 229 
ILE   CA   C N S 230 
ILE   C    C N N 231 
ILE   O    O N N 232 
ILE   CB   C N S 233 
ILE   CG1  C N N 234 
ILE   CG2  C N N 235 
ILE   CD1  C N N 236 
ILE   OXT  O N N 237 
ILE   H    H N N 238 
ILE   H2   H N N 239 
ILE   HA   H N N 240 
ILE   HB   H N N 241 
ILE   HG12 H N N 242 
ILE   HG13 H N N 243 
ILE   HG21 H N N 244 
ILE   HG22 H N N 245 
ILE   HG23 H N N 246 
ILE   HD11 H N N 247 
ILE   HD12 H N N 248 
ILE   HD13 H N N 249 
ILE   HXT  H N N 250 
LEU   N    N N N 251 
LEU   CA   C N S 252 
LEU   C    C N N 253 
LEU   O    O N N 254 
LEU   CB   C N N 255 
LEU   CG   C N N 256 
LEU   CD1  C N N 257 
LEU   CD2  C N N 258 
LEU   OXT  O N N 259 
LEU   H    H N N 260 
LEU   H2   H N N 261 
LEU   HA   H N N 262 
LEU   HB2  H N N 263 
LEU   HB3  H N N 264 
LEU   HG   H N N 265 
LEU   HD11 H N N 266 
LEU   HD12 H N N 267 
LEU   HD13 H N N 268 
LEU   HD21 H N N 269 
LEU   HD22 H N N 270 
LEU   HD23 H N N 271 
LEU   HXT  H N N 272 
LYS   N    N N N 273 
LYS   CA   C N S 274 
LYS   C    C N N 275 
LYS   O    O N N 276 
LYS   CB   C N N 277 
LYS   CG   C N N 278 
LYS   CD   C N N 279 
LYS   CE   C N N 280 
LYS   NZ   N N N 281 
LYS   OXT  O N N 282 
LYS   H    H N N 283 
LYS   H2   H N N 284 
LYS   HA   H N N 285 
LYS   HB2  H N N 286 
LYS   HB3  H N N 287 
LYS   HG2  H N N 288 
LYS   HG3  H N N 289 
LYS   HD2  H N N 290 
LYS   HD3  H N N 291 
LYS   HE2  H N N 292 
LYS   HE3  H N N 293 
LYS   HZ1  H N N 294 
LYS   HZ2  H N N 295 
LYS   HZ3  H N N 296 
LYS   HXT  H N N 297 
MET   N    N N N 298 
MET   CA   C N S 299 
MET   C    C N N 300 
MET   O    O N N 301 
MET   CB   C N N 302 
MET   CG   C N N 303 
MET   SD   S N N 304 
MET   CE   C N N 305 
MET   OXT  O N N 306 
MET   H    H N N 307 
MET   H2   H N N 308 
MET   HA   H N N 309 
MET   HB2  H N N 310 
MET   HB3  H N N 311 
MET   HG2  H N N 312 
MET   HG3  H N N 313 
MET   HE1  H N N 314 
MET   HE2  H N N 315 
MET   HE3  H N N 316 
MET   HXT  H N N 317 
PHE   N    N N N 318 
PHE   CA   C N S 319 
PHE   C    C N N 320 
PHE   O    O N N 321 
PHE   CB   C N N 322 
PHE   CG   C Y N 323 
PHE   CD1  C Y N 324 
PHE   CD2  C Y N 325 
PHE   CE1  C Y N 326 
PHE   CE2  C Y N 327 
PHE   CZ   C Y N 328 
PHE   OXT  O N N 329 
PHE   H    H N N 330 
PHE   H2   H N N 331 
PHE   HA   H N N 332 
PHE   HB2  H N N 333 
PHE   HB3  H N N 334 
PHE   HD1  H N N 335 
PHE   HD2  H N N 336 
PHE   HE1  H N N 337 
PHE   HE2  H N N 338 
PHE   HZ   H N N 339 
PHE   HXT  H N N 340 
PRO   N    N N N 341 
PRO   CA   C N S 342 
PRO   C    C N N 343 
PRO   O    O N N 344 
PRO   CB   C N N 345 
PRO   CG   C N N 346 
PRO   CD   C N N 347 
PRO   OXT  O N N 348 
PRO   H    H N N 349 
PRO   HA   H N N 350 
PRO   HB2  H N N 351 
PRO   HB3  H N N 352 
PRO   HG2  H N N 353 
PRO   HG3  H N N 354 
PRO   HD2  H N N 355 
PRO   HD3  H N N 356 
PRO   HXT  H N N 357 
SER   N    N N N 358 
SER   CA   C N S 359 
SER   C    C N N 360 
SER   O    O N N 361 
SER   CB   C N N 362 
SER   OG   O N N 363 
SER   OXT  O N N 364 
SER   H    H N N 365 
SER   H2   H N N 366 
SER   HA   H N N 367 
SER   HB2  H N N 368 
SER   HB3  H N N 369 
SER   HG   H N N 370 
SER   HXT  H N N 371 
THR   N    N N N 372 
THR   CA   C N S 373 
THR   C    C N N 374 
THR   O    O N N 375 
THR   CB   C N R 376 
THR   OG1  O N N 377 
THR   CG2  C N N 378 
THR   OXT  O N N 379 
THR   H    H N N 380 
THR   H2   H N N 381 
THR   HA   H N N 382 
THR   HB   H N N 383 
THR   HG1  H N N 384 
THR   HG21 H N N 385 
THR   HG22 H N N 386 
THR   HG23 H N N 387 
THR   HXT  H N N 388 
TRP   N    N N N 389 
TRP   CA   C N S 390 
TRP   C    C N N 391 
TRP   O    O N N 392 
TRP   CB   C N N 393 
TRP   CG   C Y N 394 
TRP   CD1  C Y N 395 
TRP   CD2  C Y N 396 
TRP   NE1  N Y N 397 
TRP   CE2  C Y N 398 
TRP   CE3  C Y N 399 
TRP   CZ2  C Y N 400 
TRP   CZ3  C Y N 401 
TRP   CH2  C Y N 402 
TRP   OXT  O N N 403 
TRP   H    H N N 404 
TRP   H2   H N N 405 
TRP   HA   H N N 406 
TRP   HB2  H N N 407 
TRP   HB3  H N N 408 
TRP   HD1  H N N 409 
TRP   HE1  H N N 410 
TRP   HE3  H N N 411 
TRP   HZ2  H N N 412 
TRP   HZ3  H N N 413 
TRP   HH2  H N N 414 
TRP   HXT  H N N 415 
TYR   N    N N N 416 
TYR   CA   C N S 417 
TYR   C    C N N 418 
TYR   O    O N N 419 
TYR   CB   C N N 420 
TYR   CG   C Y N 421 
TYR   CD1  C Y N 422 
TYR   CD2  C Y N 423 
TYR   CE1  C Y N 424 
TYR   CE2  C Y N 425 
TYR   CZ   C Y N 426 
TYR   OH   O N N 427 
TYR   OXT  O N N 428 
TYR   H    H N N 429 
TYR   H2   H N N 430 
TYR   HA   H N N 431 
TYR   HB2  H N N 432 
TYR   HB3  H N N 433 
TYR   HD1  H N N 434 
TYR   HD2  H N N 435 
TYR   HE1  H N N 436 
TYR   HE2  H N N 437 
TYR   HH   H N N 438 
TYR   HXT  H N N 439 
VAL   N    N N N 440 
VAL   CA   C N S 441 
VAL   C    C N N 442 
VAL   O    O N N 443 
VAL   CB   C N N 444 
VAL   CG1  C N N 445 
VAL   CG2  C N N 446 
VAL   OXT  O N N 447 
VAL   H    H N N 448 
VAL   H2   H N N 449 
VAL   HA   H N N 450 
VAL   HB   H N N 451 
VAL   HG11 H N N 452 
VAL   HG12 H N N 453 
VAL   HG13 H N N 454 
VAL   HG21 H N N 455 
VAL   HG22 H N N 456 
VAL   HG23 H N N 457 
VAL   HXT  H N N 458 
# 
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 
A1IN0 CAW OAV  sing N N 1   
A1IN0 CAW CAX  sing N N 2   
A1IN0 OAV CAU  sing N N 3   
A1IN0 OBE CBF  sing N N 4   
A1IN0 OBE CBD  sing N N 5   
A1IN0 CAX CAY  doub N E 6   
A1IN0 CAU CBD  doub Y N 7   
A1IN0 CAU CAR  sing Y N 8   
A1IN0 OAS CAT  sing N N 9   
A1IN0 OAS CAR  sing N N 10  
A1IN0 CBD CBG  sing Y N 11  
A1IN0 CAY CAZ  sing N N 12  
A1IN0 CAR CAQ  doub Y N 13  
A1IN0 CAZ OBA  sing N N 14  
A1IN0 CBG CAP  doub Y N 15  
A1IN0 CAQ CAP  sing Y N 16  
A1IN0 CAP CAI  sing N N 17  
A1IN0 OBA C    sing N N 18  
A1IN0 CAK CAL  sing N N 19  
A1IN0 CAK CAJ  sing N N 20  
A1IN0 CAL CAM  sing N N 21  
A1IN0 CAI CAJ  sing N N 22  
A1IN0 CAI CAB  sing N N 23  
A1IN0 C   O    doub N N 24  
A1IN0 C   CA   sing N N 25  
A1IN0 CAJ CAO  sing N N 26  
A1IN0 CAH N    sing N N 27  
A1IN0 CAH CAG  sing N N 28  
A1IN0 CAB OAA  doub N N 29  
A1IN0 CAB N    sing N N 30  
A1IN0 N   CA   sing N N 31  
A1IN0 CA  CB   sing N N 32  
A1IN0 CAM CAN  sing N N 33  
A1IN0 CAG CAF  sing N N 34  
A1IN0 CAF CB   sing N N 35  
A1IN0 CAO CAN  sing N N 36  
A1IN0 CAK HAK  sing N N 37  
A1IN0 CAK HB6  sing N N 38  
A1IN0 CAL HAL  sing N N 39  
A1IN0 CAL HB7  sing N N 40  
A1IN0 CAM HAM  sing N N 41  
A1IN0 CAM HB8  sing N N 42  
A1IN0 CAN HAN  sing N N 43  
A1IN0 CAN HB9  sing N N 44  
A1IN0 CAO HCA  sing N N 45  
A1IN0 CAO HAO  sing N N 46  
A1IN0 CAJ HAJ  sing N N 47  
A1IN0 CAI HAI  sing N N 48  
A1IN0 CAH HAH  sing N N 49  
A1IN0 CAH HB5  sing N N 50  
A1IN0 CAG HAG  sing N N 51  
A1IN0 CAG HB4  sing N N 52  
A1IN0 CAF HAF  sing N N 53  
A1IN0 CAF HB3  sing N N 54  
A1IN0 CB  HB2  sing N N 55  
A1IN0 CB  HB1  sing N N 56  
A1IN0 CA  HA   sing N N 57  
A1IN0 CAZ HCE  sing N N 58  
A1IN0 CAZ HAZ  sing N N 59  
A1IN0 CAY HAY  sing N N 60  
A1IN0 CAX HAX  sing N N 61  
A1IN0 CAW HCD  sing N N 62  
A1IN0 CAW HAW  sing N N 63  
A1IN0 CAT HCC  sing N N 64  
A1IN0 CAT HAT  sing N N 65  
A1IN0 CAT HCB  sing N N 66  
A1IN0 CAQ HAQ  sing N N 67  
A1IN0 CBG HBG  sing N N 68  
A1IN0 CBF HCG  sing N N 69  
A1IN0 CBF HBF  sing N N 70  
A1IN0 CBF HCF  sing N N 71  
ALA   N   CA   sing N N 72  
ALA   N   H    sing N N 73  
ALA   N   H2   sing N N 74  
ALA   CA  C    sing N N 75  
ALA   CA  CB   sing N N 76  
ALA   CA  HA   sing N N 77  
ALA   C   O    doub N N 78  
ALA   C   OXT  sing N N 79  
ALA   CB  HB1  sing N N 80  
ALA   CB  HB2  sing N N 81  
ALA   CB  HB3  sing N N 82  
ALA   OXT HXT  sing N N 83  
ARG   N   CA   sing N N 84  
ARG   N   H    sing N N 85  
ARG   N   H2   sing N N 86  
ARG   CA  C    sing N N 87  
ARG   CA  CB   sing N N 88  
ARG   CA  HA   sing N N 89  
ARG   C   O    doub N N 90  
ARG   C   OXT  sing N N 91  
ARG   CB  CG   sing N N 92  
ARG   CB  HB2  sing N N 93  
ARG   CB  HB3  sing N N 94  
ARG   CG  CD   sing N N 95  
ARG   CG  HG2  sing N N 96  
ARG   CG  HG3  sing N N 97  
ARG   CD  NE   sing N N 98  
ARG   CD  HD2  sing N N 99  
ARG   CD  HD3  sing N N 100 
ARG   NE  CZ   sing N N 101 
ARG   NE  HE   sing N N 102 
ARG   CZ  NH1  sing N N 103 
ARG   CZ  NH2  doub N N 104 
ARG   NH1 HH11 sing N N 105 
ARG   NH1 HH12 sing N N 106 
ARG   NH2 HH21 sing N N 107 
ARG   NH2 HH22 sing N N 108 
ARG   OXT HXT  sing N N 109 
ASN   N   CA   sing N N 110 
ASN   N   H    sing N N 111 
ASN   N   H2   sing N N 112 
ASN   CA  C    sing N N 113 
ASN   CA  CB   sing N N 114 
ASN   CA  HA   sing N N 115 
ASN   C   O    doub N N 116 
ASN   C   OXT  sing N N 117 
ASN   CB  CG   sing N N 118 
ASN   CB  HB2  sing N N 119 
ASN   CB  HB3  sing N N 120 
ASN   CG  OD1  doub N N 121 
ASN   CG  ND2  sing N N 122 
ASN   ND2 HD21 sing N N 123 
ASN   ND2 HD22 sing N N 124 
ASN   OXT HXT  sing N N 125 
ASP   N   CA   sing N N 126 
ASP   N   H    sing N N 127 
ASP   N   H2   sing N N 128 
ASP   CA  C    sing N N 129 
ASP   CA  CB   sing N N 130 
ASP   CA  HA   sing N N 131 
ASP   C   O    doub N N 132 
ASP   C   OXT  sing N N 133 
ASP   CB  CG   sing N N 134 
ASP   CB  HB2  sing N N 135 
ASP   CB  HB3  sing N N 136 
ASP   CG  OD1  doub N N 137 
ASP   CG  OD2  sing N N 138 
ASP   OD2 HD2  sing N N 139 
ASP   OXT HXT  sing N N 140 
CYS   N   CA   sing N N 141 
CYS   N   H    sing N N 142 
CYS   N   H2   sing N N 143 
CYS   CA  C    sing N N 144 
CYS   CA  CB   sing N N 145 
CYS   CA  HA   sing N N 146 
CYS   C   O    doub N N 147 
CYS   C   OXT  sing N N 148 
CYS   CB  SG   sing N N 149 
CYS   CB  HB2  sing N N 150 
CYS   CB  HB3  sing N N 151 
CYS   SG  HG   sing N N 152 
CYS   OXT HXT  sing N N 153 
GLN   N   CA   sing N N 154 
GLN   N   H    sing N N 155 
GLN   N   H2   sing N N 156 
GLN   CA  C    sing N N 157 
GLN   CA  CB   sing N N 158 
GLN   CA  HA   sing N N 159 
GLN   C   O    doub N N 160 
GLN   C   OXT  sing N N 161 
GLN   CB  CG   sing N N 162 
GLN   CB  HB2  sing N N 163 
GLN   CB  HB3  sing N N 164 
GLN   CG  CD   sing N N 165 
GLN   CG  HG2  sing N N 166 
GLN   CG  HG3  sing N N 167 
GLN   CD  OE1  doub N N 168 
GLN   CD  NE2  sing N N 169 
GLN   NE2 HE21 sing N N 170 
GLN   NE2 HE22 sing N N 171 
GLN   OXT HXT  sing N N 172 
GLU   N   CA   sing N N 173 
GLU   N   H    sing N N 174 
GLU   N   H2   sing N N 175 
GLU   CA  C    sing N N 176 
GLU   CA  CB   sing N N 177 
GLU   CA  HA   sing N N 178 
GLU   C   O    doub N N 179 
GLU   C   OXT  sing N N 180 
GLU   CB  CG   sing N N 181 
GLU   CB  HB2  sing N N 182 
GLU   CB  HB3  sing N N 183 
GLU   CG  CD   sing N N 184 
GLU   CG  HG2  sing N N 185 
GLU   CG  HG3  sing N N 186 
GLU   CD  OE1  doub N N 187 
GLU   CD  OE2  sing N N 188 
GLU   OE2 HE2  sing N N 189 
GLU   OXT HXT  sing N N 190 
GLY   N   CA   sing N N 191 
GLY   N   H    sing N N 192 
GLY   N   H2   sing N N 193 
GLY   CA  C    sing N N 194 
GLY   CA  HA2  sing N N 195 
GLY   CA  HA3  sing N N 196 
GLY   C   O    doub N N 197 
GLY   C   OXT  sing N N 198 
GLY   OXT HXT  sing N N 199 
HIS   N   CA   sing N N 200 
HIS   N   H    sing N N 201 
HIS   N   H2   sing N N 202 
HIS   CA  C    sing N N 203 
HIS   CA  CB   sing N N 204 
HIS   CA  HA   sing N N 205 
HIS   C   O    doub N N 206 
HIS   C   OXT  sing N N 207 
HIS   CB  CG   sing N N 208 
HIS   CB  HB2  sing N N 209 
HIS   CB  HB3  sing N N 210 
HIS   CG  ND1  sing Y N 211 
HIS   CG  CD2  doub Y N 212 
HIS   ND1 CE1  doub Y N 213 
HIS   ND1 HD1  sing N N 214 
HIS   CD2 NE2  sing Y N 215 
HIS   CD2 HD2  sing N N 216 
HIS   CE1 NE2  sing Y N 217 
HIS   CE1 HE1  sing N N 218 
HIS   NE2 HE2  sing N N 219 
HIS   OXT HXT  sing N N 220 
HOH   O   H1   sing N N 221 
HOH   O   H2   sing N N 222 
ILE   N   CA   sing N N 223 
ILE   N   H    sing N N 224 
ILE   N   H2   sing N N 225 
ILE   CA  C    sing N N 226 
ILE   CA  CB   sing N N 227 
ILE   CA  HA   sing N N 228 
ILE   C   O    doub N N 229 
ILE   C   OXT  sing N N 230 
ILE   CB  CG1  sing N N 231 
ILE   CB  CG2  sing N N 232 
ILE   CB  HB   sing N N 233 
ILE   CG1 CD1  sing N N 234 
ILE   CG1 HG12 sing N N 235 
ILE   CG1 HG13 sing N N 236 
ILE   CG2 HG21 sing N N 237 
ILE   CG2 HG22 sing N N 238 
ILE   CG2 HG23 sing N N 239 
ILE   CD1 HD11 sing N N 240 
ILE   CD1 HD12 sing N N 241 
ILE   CD1 HD13 sing N N 242 
ILE   OXT HXT  sing N N 243 
LEU   N   CA   sing N N 244 
LEU   N   H    sing N N 245 
LEU   N   H2   sing N N 246 
LEU   CA  C    sing N N 247 
LEU   CA  CB   sing N N 248 
LEU   CA  HA   sing N N 249 
LEU   C   O    doub N N 250 
LEU   C   OXT  sing N N 251 
LEU   CB  CG   sing N N 252 
LEU   CB  HB2  sing N N 253 
LEU   CB  HB3  sing N N 254 
LEU   CG  CD1  sing N N 255 
LEU   CG  CD2  sing N N 256 
LEU   CG  HG   sing N N 257 
LEU   CD1 HD11 sing N N 258 
LEU   CD1 HD12 sing N N 259 
LEU   CD1 HD13 sing N N 260 
LEU   CD2 HD21 sing N N 261 
LEU   CD2 HD22 sing N N 262 
LEU   CD2 HD23 sing N N 263 
LEU   OXT HXT  sing N N 264 
LYS   N   CA   sing N N 265 
LYS   N   H    sing N N 266 
LYS   N   H2   sing N N 267 
LYS   CA  C    sing N N 268 
LYS   CA  CB   sing N N 269 
LYS   CA  HA   sing N N 270 
LYS   C   O    doub N N 271 
LYS   C   OXT  sing N N 272 
LYS   CB  CG   sing N N 273 
LYS   CB  HB2  sing N N 274 
LYS   CB  HB3  sing N N 275 
LYS   CG  CD   sing N N 276 
LYS   CG  HG2  sing N N 277 
LYS   CG  HG3  sing N N 278 
LYS   CD  CE   sing N N 279 
LYS   CD  HD2  sing N N 280 
LYS   CD  HD3  sing N N 281 
LYS   CE  NZ   sing N N 282 
LYS   CE  HE2  sing N N 283 
LYS   CE  HE3  sing N N 284 
LYS   NZ  HZ1  sing N N 285 
LYS   NZ  HZ2  sing N N 286 
LYS   NZ  HZ3  sing N N 287 
LYS   OXT HXT  sing N N 288 
MET   N   CA   sing N N 289 
MET   N   H    sing N N 290 
MET   N   H2   sing N N 291 
MET   CA  C    sing N N 292 
MET   CA  CB   sing N N 293 
MET   CA  HA   sing N N 294 
MET   C   O    doub N N 295 
MET   C   OXT  sing N N 296 
MET   CB  CG   sing N N 297 
MET   CB  HB2  sing N N 298 
MET   CB  HB3  sing N N 299 
MET   CG  SD   sing N N 300 
MET   CG  HG2  sing N N 301 
MET   CG  HG3  sing N N 302 
MET   SD  CE   sing N N 303 
MET   CE  HE1  sing N N 304 
MET   CE  HE2  sing N N 305 
MET   CE  HE3  sing N N 306 
MET   OXT HXT  sing N N 307 
PHE   N   CA   sing N N 308 
PHE   N   H    sing N N 309 
PHE   N   H2   sing N N 310 
PHE   CA  C    sing N N 311 
PHE   CA  CB   sing N N 312 
PHE   CA  HA   sing N N 313 
PHE   C   O    doub N N 314 
PHE   C   OXT  sing N N 315 
PHE   CB  CG   sing N N 316 
PHE   CB  HB2  sing N N 317 
PHE   CB  HB3  sing N N 318 
PHE   CG  CD1  doub Y N 319 
PHE   CG  CD2  sing Y N 320 
PHE   CD1 CE1  sing Y N 321 
PHE   CD1 HD1  sing N N 322 
PHE   CD2 CE2  doub Y N 323 
PHE   CD2 HD2  sing N N 324 
PHE   CE1 CZ   doub Y N 325 
PHE   CE1 HE1  sing N N 326 
PHE   CE2 CZ   sing Y N 327 
PHE   CE2 HE2  sing N N 328 
PHE   CZ  HZ   sing N N 329 
PHE   OXT HXT  sing N N 330 
PRO   N   CA   sing N N 331 
PRO   N   CD   sing N N 332 
PRO   N   H    sing N N 333 
PRO   CA  C    sing N N 334 
PRO   CA  CB   sing N N 335 
PRO   CA  HA   sing N N 336 
PRO   C   O    doub N N 337 
PRO   C   OXT  sing N N 338 
PRO   CB  CG   sing N N 339 
PRO   CB  HB2  sing N N 340 
PRO   CB  HB3  sing N N 341 
PRO   CG  CD   sing N N 342 
PRO   CG  HG2  sing N N 343 
PRO   CG  HG3  sing N N 344 
PRO   CD  HD2  sing N N 345 
PRO   CD  HD3  sing N N 346 
PRO   OXT HXT  sing N N 347 
SER   N   CA   sing N N 348 
SER   N   H    sing N N 349 
SER   N   H2   sing N N 350 
SER   CA  C    sing N N 351 
SER   CA  CB   sing N N 352 
SER   CA  HA   sing N N 353 
SER   C   O    doub N N 354 
SER   C   OXT  sing N N 355 
SER   CB  OG   sing N N 356 
SER   CB  HB2  sing N N 357 
SER   CB  HB3  sing N N 358 
SER   OG  HG   sing N N 359 
SER   OXT HXT  sing N N 360 
THR   N   CA   sing N N 361 
THR   N   H    sing N N 362 
THR   N   H2   sing N N 363 
THR   CA  C    sing N N 364 
THR   CA  CB   sing N N 365 
THR   CA  HA   sing N N 366 
THR   C   O    doub N N 367 
THR   C   OXT  sing N N 368 
THR   CB  OG1  sing N N 369 
THR   CB  CG2  sing N N 370 
THR   CB  HB   sing N N 371 
THR   OG1 HG1  sing N N 372 
THR   CG2 HG21 sing N N 373 
THR   CG2 HG22 sing N N 374 
THR   CG2 HG23 sing N N 375 
THR   OXT HXT  sing N N 376 
TRP   N   CA   sing N N 377 
TRP   N   H    sing N N 378 
TRP   N   H2   sing N N 379 
TRP   CA  C    sing N N 380 
TRP   CA  CB   sing N N 381 
TRP   CA  HA   sing N N 382 
TRP   C   O    doub N N 383 
TRP   C   OXT  sing N N 384 
TRP   CB  CG   sing N N 385 
TRP   CB  HB2  sing N N 386 
TRP   CB  HB3  sing N N 387 
TRP   CG  CD1  doub Y N 388 
TRP   CG  CD2  sing Y N 389 
TRP   CD1 NE1  sing Y N 390 
TRP   CD1 HD1  sing N N 391 
TRP   CD2 CE2  doub Y N 392 
TRP   CD2 CE3  sing Y N 393 
TRP   NE1 CE2  sing Y N 394 
TRP   NE1 HE1  sing N N 395 
TRP   CE2 CZ2  sing Y N 396 
TRP   CE3 CZ3  doub Y N 397 
TRP   CE3 HE3  sing N N 398 
TRP   CZ2 CH2  doub Y N 399 
TRP   CZ2 HZ2  sing N N 400 
TRP   CZ3 CH2  sing Y N 401 
TRP   CZ3 HZ3  sing N N 402 
TRP   CH2 HH2  sing N N 403 
TRP   OXT HXT  sing N N 404 
TYR   N   CA   sing N N 405 
TYR   N   H    sing N N 406 
TYR   N   H2   sing N N 407 
TYR   CA  C    sing N N 408 
TYR   CA  CB   sing N N 409 
TYR   CA  HA   sing N N 410 
TYR   C   O    doub N N 411 
TYR   C   OXT  sing N N 412 
TYR   CB  CG   sing N N 413 
TYR   CB  HB2  sing N N 414 
TYR   CB  HB3  sing N N 415 
TYR   CG  CD1  doub Y N 416 
TYR   CG  CD2  sing Y N 417 
TYR   CD1 CE1  sing Y N 418 
TYR   CD1 HD1  sing N N 419 
TYR   CD2 CE2  doub Y N 420 
TYR   CD2 HD2  sing N N 421 
TYR   CE1 CZ   doub Y N 422 
TYR   CE1 HE1  sing N N 423 
TYR   CE2 CZ   sing Y N 424 
TYR   CE2 HE2  sing N N 425 
TYR   CZ  OH   sing N N 426 
TYR   OH  HH   sing N N 427 
TYR   OXT HXT  sing N N 428 
VAL   N   CA   sing N N 429 
VAL   N   H    sing N N 430 
VAL   N   H2   sing N N 431 
VAL   CA  C    sing N N 432 
VAL   CA  CB   sing N N 433 
VAL   CA  HA   sing N N 434 
VAL   C   O    doub N N 435 
VAL   C   OXT  sing N N 436 
VAL   CB  CG1  sing N N 437 
VAL   CB  CG2  sing N N 438 
VAL   CB  HB   sing N N 439 
VAL   CG1 HG11 sing N N 440 
VAL   CG1 HG12 sing N N 441 
VAL   CG1 HG13 sing N N 442 
VAL   CG2 HG21 sing N N 443 
VAL   CG2 HG22 sing N N 444 
VAL   CG2 HG23 sing N N 445 
VAL   OXT HXT  sing N N 446 
# 
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                    9GQ2 
_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]   0.020462 
_atom_sites.fract_transf_matrix[1][2]   0.011814 
_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]   0.023628 
_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]   0.005155 
_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    . GLU   A 1 8   ? -6.397  3.322   37.054  1   69.492  ? 20  GLU   A N    1 ? 1 
ATOM   2    C CA   . GLU   A 1 8   ? -7.855  3.481   37.32   1   75.752  ? 20  GLU   A CA   1 ? 1 
ATOM   3    C C    . GLU   A 1 8   ? -8.154  4.194   38.657  1   73.598  ? 20  GLU   A C    1 ? 1 
ATOM   4    O O    . GLU   A 1 8   ? -9.226  4.009   39.22   1   82.031  ? 20  GLU   A O    1 ? 1 
ATOM   5    C CB   . GLU   A 1 8   ? -8.518  2.125   37.065  1   68.64   ? 20  GLU   A CB   1 ? 1 
ATOM   6    H H    . GLU   A 1 8   ? -6.263  2.788   36.338  1   71.876  ? 20  GLU   A H    1 c 1 
ATOM   7    H HA   . GLU   A 1 8   ? -8.209  4.073   36.608  1   69.894  ? 20  GLU   A HA   1 c 1 
ATOM   8    H HB2  . GLU   A 1 8   ? -8.803  1.305   37.553  0   30      ? 20  GLU   A HB2  1 c 1 
ATOM   9    H HB3  . GLU   A 1 8   ? -10.236 2.486   37.579  0   30      ? 20  GLU   A HB3  1 c 1 
ATOM   10   N N    . GLN   A 1 9   ? -7.199  4.973   39.194  1   83.814  ? 21  GLN   A N    1 ? 1 
ATOM   11   C CA   . GLN   A 1 9   ? -7.39   6.081   40.152  1   89.285  ? 21  GLN   A CA   1 ? 1 
ATOM   12   C C    . GLN   A 1 9   ? -8.196  7.28    39.584  1   89.888  ? 21  GLN   A C    1 ? 1 
ATOM   13   O O    . GLN   A 1 9   ? -8.161  7.532   38.344  1   81.985  ? 21  GLN   A O    1 ? 1 
ATOM   14   C CB   . GLN   A 1 9   ? -5.97   6.65    40.307  1   92.669  ? 21  GLN   A CB   1 ? 1 
ATOM   15   C CG   . GLN   A 1 9   ? -5.368  7.04    38.944  1   86.56   ? 21  GLN   A CG   1 ? 1 
ATOM   16   C CD   . GLN   A 1 9   ? -3.876  7.262   38.908  1   89.14   ? 21  GLN   A CD   1 ? 1 
ATOM   17   O OE1  . GLN   A 1 9   ? -3.388  8.193   39.562  1   88.857  ? 21  GLN   A OE1  1 ? 1 
ATOM   18   N NE2  . GLN   A 1 9   ? -3.164  6.436   38.132  1   83.179  ? 21  GLN   A NE2  1 ? 1 
ATOM   19   H H    . GLN   A 1 9   ? -6.339  4.761   38.974  1   82.654  ? 21  GLN   A H    1 c 1 
ATOM   20   H HA   . GLN   A 1 9   ? -7.777  5.748   41.001  1   90.994  ? 21  GLN   A HA   1 c 1 
ATOM   21   H HB2  . GLN   A 1 9   ? -5.998  7.439   40.888  1   90.829  ? 21  GLN   A HB2  1 c 1 
ATOM   22   H HB3  . GLN   A 1 9   ? -5.398  5.979   40.734  1   93.143  ? 21  GLN   A HB3  1 c 1 
ATOM   23   H HG2  . GLN   A 1 9   ? -5.585  6.351   38.284  1   87.497  ? 21  GLN   A HG2  1 c 1 
ATOM   24   H HG3  . GLN   A 1 9   ? -5.789  7.87    38.642  1   85.656  ? 21  GLN   A HG3  1 c 1 
ATOM   25   H HE21 . GLN   A 1 9   ? -2.396  6.105   38.428  1   87.019  ? 21  GLN   A HE21 1 c 1 
ATOM   26   H HE22 . GLN   A 1 9   ? -3.459  6.222   37.323  1   84.213  ? 21  GLN   A HE22 1 c 1 
ATOM   27   N N    . GLY   A 1 10  ? -8.848  8.079   40.474  1   68.593  ? 22  GLY   A N    1 ? 1 
ATOM   28   C CA   . GLY   A 1 10  ? -9.415  9.369   40.082  1   54.486  ? 22  GLY   A CA   1 ? 1 
ATOM   29   C C    . GLY   A 1 10  ? -10.957 9.406   40.012  1   56.005  ? 22  GLY   A C    1 ? 1 
ATOM   30   O O    . GLY   A 1 10  ? -11.686 8.431   40.166  1   51.644  ? 22  GLY   A O    1 ? 1 
ATOM   31   H H    . GLY   A 1 10  ? -8.936  7.804   41.341  1   71.571  ? 22  GLY   A H    1 c 1 
ATOM   32   H HA2  . GLY   A 1 10  ? -9.112  10.049  40.729  1   57.792  ? 22  GLY   A HA2  1 c 1 
ATOM   33   H HA3  . GLY   A 1 10  ? -9.05   9.62    39.202  1   56.101  ? 22  GLY   A HA3  1 c 1 
ATOM   34   N N    . GLU   A 1 11  ? -11.513 10.589  39.789  1   52.795  ? 23  GLU   A N    1 ? 1 
ATOM   35   C CA   . GLU   A 1 11  ? -12.947 10.782  39.968  1   55.803  ? 23  GLU   A CA   1 ? 1 
ATOM   36   C C    . GLU   A 1 11  ? -13.686 10.544  38.647  1   48.563  ? 23  GLU   A C    1 ? 1 
ATOM   37   O O    . GLU   A 1 11  ? -13.223 10.93   37.57   1   44.369  ? 23  GLU   A O    1 ? 1 
ATOM   38   C CB   . GLU   A 1 11  ? -13.229 12.118  40.678  1   64.303  ? 23  GLU   A CB   1 ? 1 
ATOM   39   C CG   . GLU   A 1 11  ? -14.128 13.049  39.875  1   69.019  ? 23  GLU   A CG   1 ? 1 
ATOM   40   C CD   . GLU   A 1 11  ? -14.314 14.386  40.559  1   76.67   ? 23  GLU   A CD   1 ? 1 
ATOM   41   O OE1  . GLU   A 1 11  ? -13.406 15.294  40.629  1   73.832  ? 23  GLU   A OE1  1 ? 1 
ATOM   42   O OE2  . GLU   A 1 11  ? -15.456 14.403  41.059  1   69.885  ? 23  GLU   A OE2  1 ? 1 
ATOM   43   H H    . GLU   A 1 11  ? -10.998 11.293  39.515  1   52.757  ? 23  GLU   A H    1 c 1 
ATOM   44   H HA   . GLU   A 1 11  ? -13.258 10.087  40.603  1   57.049  ? 23  GLU   A HA   1 c 1 
ATOM   45   H HB2  . GLU   A 1 11  ? -13.675 11.934  41.529  1   65.22   ? 23  GLU   A HB2  1 c 1 
ATOM   46   H HB3  . GLU   A 1 11  ? -12.38  12.566  40.873  1   62.95   ? 23  GLU   A HB3  1 c 1 
ATOM   47   H HG2  . GLU   A 1 11  ? -13.734 13.201  38.991  1   67.265  ? 23  GLU   A HG2  1 c 1 
ATOM   48   H HG3  . GLU   A 1 11  ? -15.007 12.63   39.753  1   69.656  ? 23  GLU   A HG3  1 c 1 
ATOM   49   N N    . ASP   A 1 12  ? -14.767 9.788   38.746  1   47.298  ? 24  ASP   A N    1 ? 1 
ATOM   50   C CA   . ASP   A 1 12  ? -15.545 9.39    37.597  1   51.679  ? 24  ASP   A CA   1 ? 1 
ATOM   51   C C    . ASP   A 1 12  ? -16.439 10.581  37.296  1   53.938  ? 24  ASP   A C    1 ? 1 
ATOM   52   O O    . ASP   A 1 12  ? -17.357 10.872  38.075  1   49.233  ? 24  ASP   A O    1 ? 1 
ATOM   53   C CB   . ASP   A 1 12  ? -16.378 8.143   37.887  1   56.362  ? 24  ASP   A CB   1 ? 1 
ATOM   54   C CG   . ASP   A 1 12  ? -17.225 7.63    36.733  1   56.636  ? 24  ASP   A CG   1 ? 1 
ATOM   55   O OD1  . ASP   A 1 12  ? -17.22  8.309   35.686  1   52.954  ? 24  ASP   A OD1  1 ? 1 
ATOM   56   O OD2  . ASP   A 1 12  ? -17.862 6.535   36.885  1   55.56   ? 24  ASP   A OD2  1 ? 1 
ATOM   57   H H    . ASP   A 1 12  ? -15.039 9.508   39.573  1   50.734  ? 24  ASP   A H    1 c 1 
ATOM   58   H HA   . ASP   A 1 12  ? -14.943 9.226   36.84   1   50.262  ? 24  ASP   A HA   1 c 1 
ATOM   59   H HB2  . ASP   A 1 12  ? -15.772 7.423   38.159  1   56.392  ? 24  ASP   A HB2  1 c 1 
ATOM   60   H HB3  . ASP   A 1 12  ? -16.974 8.331   38.642  1   57.248  ? 24  ASP   A HB3  1 c 1 
ATOM   61   N N    . ILE   A 1 13  ? -16.129 11.308  36.221  1   48.077  ? 25  ILE   A N    1 ? 1 
ATOM   62   C CA   . ILE   A 1 13  ? -16.861 12.528  35.921  1   51.149  ? 25  ILE   A CA   1 ? 1 
ATOM   63   C C    . ILE   A 1 13  ? -17.88  12.252  34.822  1   48.769  ? 25  ILE   A C    1 ? 1 
ATOM   64   O O    . ILE   A 1 13  ? -18.451 13.207  34.317  1   55.376  ? 25  ILE   A O    1 ? 1 
ATOM   65   C CB   . ILE   A 1 13  ? -15.974 13.712  35.519  1   51.012  ? 25  ILE   A CB   1 ? 1 
ATOM   66   C CG1  . ILE   A 1 13  ? -15.064 13.375  34.334  1   51.354  ? 25  ILE   A CG1  1 ? 1 
ATOM   67   C CG2  . ILE   A 1 13  ? -15.172 14.254  36.705  1   53.832  ? 25  ILE   A CG2  1 ? 1 
ATOM   68   C CD1  . ILE   A 1 13  ? -14.275 14.581  33.858  1   55.38   ? 25  ILE   A CD1  1 ? 1 
ATOM   69   H H    . ILE   A 1 13  ? -15.461 11.036  35.66   1   48.687  ? 25  ILE   A H    1 c 1 
ATOM   70   H HA   . ILE   A 1 13  ? -17.352 12.789  36.724  1   51.454  ? 25  ILE   A HA   1 c 1 
ATOM   71   H HB   . ILE   A 1 13  ? -16.569 14.43   35.226  1   52.052  ? 25  ILE   A HB   1 c 1 
ATOM   72   H HG12 . ILE   A 1 13  ? -14.439 12.67   34.6    1   51.617  ? 25  ILE   A HG12 1 c 1 
ATOM   73   H HG13 . ILE   A 1 13  ? -15.609 13.036  33.595  1   52.186  ? 25  ILE   A HG13 1 c 1 
ATOM   74   H HG21 . ILE   A 1 13  ? -14.95  15.188  36.549  1   52.701  ? 25  ILE   A HG21 1 c 1 
ATOM   75   H HG22 . ILE   A 1 13  ? -14.352 13.741  36.806  1   52.457  ? 25  ILE   A HG22 1 c 1 
ATOM   76   H HG23 . ILE   A 1 13  ? -15.699 14.181  37.518  1   54.27   ? 25  ILE   A HG23 1 c 1 
ATOM   77   H HD11 . ILE   A 1 13  ? -14.846 15.372  33.88   1   54.263  ? 25  ILE   A HD11 1 c 1 
ATOM   78   H HD12 . ILE   A 1 13  ? -13.968 14.429  32.944  1   53.081  ? 25  ILE   A HD12 1 c 1 
ATOM   79   H HD13 . ILE   A 1 13  ? -13.504 14.722  34.439  1   53.352  ? 25  ILE   A HD13 1 c 1 
ATOM   80   N N    . THR   A 1 14  ? -18.188 10.998  34.546  1   50.46   ? 26  THR   A N    1 ? 1 
ATOM   81   C CA   . THR   A 1 14  ? -19.206 10.681  33.526  1   59.52   ? 26  THR   A CA   1 ? 1 
ATOM   82   C C    . THR   A 1 14  ? -20.604 10.817  34.123  1   64.339  ? 26  THR   A C    1 ? 1 
ATOM   83   O O    . THR   A 1 14  ? -20.78  10.662  35.331  1   60.87   ? 26  THR   A O    1 ? 1 
ATOM   84   C CB   . THR   A 1 14  ? -19.066 9.28    32.932  1   49.641  ? 26  THR   A CB   1 ? 1 
ATOM   85   O OG1  . THR   A 1 14  ? -19.14  8.278   33.94   1   53.246  ? 26  THR   A OG1  1 ? 1 
ATOM   86   C CG2  . THR   A 1 14  ? -17.741 9.051   32.236  1   55.971  ? 26  THR   A CG2  1 ? 1 
ATOM   87   H H    . THR   A 1 14  ? -17.773 10.312  34.984  1   51.958  ? 26  THR   A H    1 c 1 
ATOM   88   H HA   . THR   A 1 14  ? -19.116 11.331  32.795  1   55.291  ? 26  THR   A HA   1 c 1 
ATOM   89   H HB   . THR   A 1 14  ? -19.791 9.134   32.279  1   54.407  ? 26  THR   A HB   1 c 1 
ATOM   90   H HG1  . THR   A 1 14  ? -18.527 8.444   34.54   0   30      ? 26  THR   A HG1  1 c 1 
ATOM   91   H HG21 . THR   A 1 14  ? -17.628 8.103   32.054  1   53.921  ? 26  THR   A HG21 1 c 1 
ATOM   92   H HG22 . THR   A 1 14  ? -17.017 9.36    32.806  1   52.154  ? 26  THR   A HG22 1 c 1 
ATOM   93   H HG23 . THR   A 1 14  ? -17.725 9.545   31.398  1   52.571  ? 26  THR   A HG23 1 c 1 
ATOM   94   N N    . SER   A 1 15  ? -21.586 11.028  33.234  1   68.903  ? 27  SER   A N    1 ? 1 
ATOM   95   C CA   . SER   A 1 15  ? -22.983 11.098  33.617  1   69.799  ? 27  SER   A CA   1 ? 1 
ATOM   96   C C    . SER   A 1 15  ? -23.485 9.728   34.039  1   65.134  ? 27  SER   A C    1 ? 1 
ATOM   97   O O    . SER   A 1 15  ? -24.239 9.598   35.007  1   77.452  ? 27  SER   A O    1 ? 1 
ATOM   98   C CB   . SER   A 1 15  ? -23.804 11.672  32.512  1   74.034  ? 27  SER   A CB   1 ? 1 
ATOM   99   O OG   . SER   A 1 15  ? -23.737 13.089  32.623  1   73.738  ? 27  SER   A OG   1 ? 1 
ATOM   100  H H    . SER   A 1 15  ? -21.369 11.129  32.352  1   66.757  ? 27  SER   A H    1 c 1 
ATOM   101  H HA   . SER   A 1 15  ? -23.053 11.702  34.4    1   69.551  ? 27  SER   A HA   1 c 1 
ATOM   102  H HB2  . SER   A 1 15  ? -23.452 11.386  31.648  1   72.506  ? 27  SER   A HB2  1 c 1 
ATOM   103  H HB3  . SER   A 1 15  ? -24.73  11.375  32.595  1   75.906  ? 27  SER   A HB3  1 c 1 
ATOM   104  H HG   . SER   A 1 15  ? -24.224 13.513  31.932  0   30      ? 27  SER   A HG   1 c 1 
ATOM   105  N N    . LYS   A 1 16  ? -23.015 8.72    33.326  1   61.331  ? 28  LYS   A N    1 ? 1 
ATOM   106  C CA   . LYS   A 1 16  ? -23.531 7.369   33.459  1   64.235  ? 28  LYS   A CA   1 ? 1 
ATOM   107  C C    . LYS   A 1 16  ? -22.85  6.67    34.64   1   61.771  ? 28  LYS   A C    1 ? 1 
ATOM   108  O O    . LYS   A 1 16  ? -23.252 5.57    34.975  1   69.561  ? 28  LYS   A O    1 ? 1 
ATOM   109  C CB   . LYS   A 1 16  ? -23.409 6.653   32.094  1   61.707  ? 28  LYS   A CB   1 ? 1 
ATOM   110  H H    . LYS   A 1 16  ? -22.342 8.873   32.727  1   60.282  ? 28  LYS   A H    1 c 1 
ATOM   111  H HA   . LYS   A 1 16  ? -24.498 7.433   33.666  1   65.807  ? 28  LYS   A HA   1 c 1 
ATOM   112  H HB2  . LYS   A 1 16  ? -22.458 6.846   31.827  0   30      ? 28  LYS   A HB2  1 c 1 
ATOM   113  H HB3  . LYS   A 1 16  ? -24.311 6.797   31.692  0   30      ? 28  LYS   A HB3  1 c 1 
ATOM   114  N N    . LYS   A 1 17  ? -21.773 7.256   35.188  1   63.367  ? 29  LYS   A N    1 ? 1 
ATOM   115  C CA   . LYS   A 1 17  ? -20.943 6.65    36.227  1   63.699  ? 29  LYS   A CA   1 ? 1 
ATOM   116  C C    . LYS   A 1 17  ? -20.411 5.254   35.832  1   62.848  ? 29  LYS   A C    1 ? 1 
ATOM   117  O O    . LYS   A 1 17  ? -20.515 4.281   36.569  1   58.733  ? 29  LYS   A O    1 ? 1 
ATOM   118  C CB   . LYS   A 1 17  ? -21.719 6.677   37.544  1   69.183  ? 29  LYS   A CB   1 ? 1 
ATOM   119  C CG   . LYS   A 1 17  ? -21.934 8.059   38.15   1   72.877  ? 29  LYS   A CG   1 ? 1 
ATOM   120  C CD   . LYS   A 1 17  ? -20.651 8.616   38.745  1   76.307  ? 29  LYS   A CD   1 ? 1 
ATOM   121  C CE   . LYS   A 1 17  ? -20.806 9.847   39.588  1   84.888  ? 29  LYS   A CE   1 ? 1 
ATOM   122  N NZ   . LYS   A 1 17  ? -20.58  11.029  38.755  1   81.102  ? 29  LYS   A NZ   1 ? 1 
ATOM   123  H H    . LYS   A 1 17  ? -21.534 8.085   34.889  1   60.589  ? 29  LYS   A H    1 c 1 
ATOM   124  H HA   . LYS   A 1 17  ? -20.157 7.238   36.349  1   61.682  ? 29  LYS   A HA   1 c 1 
ATOM   125  H HB2  . LYS   A 1 17  ? -22.597 6.265   37.401  1   71.835  ? 29  LYS   A HB2  1 c 1 
ATOM   126  H HB3  . LYS   A 1 17  ? -21.239 6.127   38.199  1   70.111  ? 29  LYS   A HB3  1 c 1 
ATOM   127  H HG2  . LYS   A 1 17  ? -22.26  8.667   37.452  1   72.263  ? 29  LYS   A HG2  1 c 1 
ATOM   128  H HG3  . LYS   A 1 17  ? -22.618 7.997   38.851  1   75.577  ? 29  LYS   A HG3  1 c 1 
ATOM   129  H HD2  . LYS   A 1 17  ? -20.234 7.915   39.29   1   77.329  ? 29  LYS   A HD2  1 c 1 
ATOM   130  H HD3  . LYS   A 1 17  ? -20.032 8.816   38.01   1   74.336  ? 29  LYS   A HD3  1 c 1 
ATOM   131  H HE2  . LYS   A 1 17  ? -21.703 9.885   39.966  1   84.67   ? 29  LYS   A HE2  1 c 1 
ATOM   132  H HE3  . LYS   A 1 17  ? -20.16  9.836   40.317  1   82.34   ? 29  LYS   A HE3  1 c 1 
ATOM   133  H HZ1  . LYS   A 1 17  ? -21.079 10.976  38.001  1   81.555  ? 29  LYS   A HZ1  1 c 1 
ATOM   134  H HZ2  . LYS   A 1 17  ? -19.704 11.082  38.529  1   79.523  ? 29  LYS   A HZ2  1 c 1 
ATOM   135  H HZ3  . LYS   A 1 17  ? -20.813 11.774  39.214  1   82.028  ? 29  LYS   A HZ3  1 c 1 
ATOM   136  N N    . ASP   A 1 18  ? -19.756 5.155   34.692  1   62.76   ? 30  ASP   A N    1 ? 1 
ATOM   137  C CA   . ASP   A 1 18  ? -19.257 3.88    34.203  1   71.165  ? 30  ASP   A CA   1 ? 1 
ATOM   138  C C    . ASP   A 1 18  ? -17.728 3.932   34.201  1   78.886  ? 30  ASP   A C    1 ? 1 
ATOM   139  O O    . ASP   A 1 18  ? -17.059 3.167   33.51   1   76.685  ? 30  ASP   A O    1 ? 1 
ATOM   140  C CB   . ASP   A 1 18  ? -19.721 3.676   32.77   1   67.416  ? 30  ASP   A CB   1 ? 1 
ATOM   141  C CG   . ASP   A 1 18  ? -19.131 4.766   31.895  1   60.723  ? 30  ASP   A CG   1 ? 1 
ATOM   142  O OD1  . ASP   A 1 18  ? -18.104 5.366   32.385  1   55.944  ? 30  ASP   A OD1  1 ? 1 
ATOM   143  O OD2  . ASP   A 1 18  ? -19.784 5.117   30.87   1   56.879  ? 30  ASP   A OD2  1 ? 1 
ATOM   144  H H    . ASP   A 1 18  ? -19.61  5.908   34.194  1   62.118  ? 30  ASP   A H    1 c 1 
ATOM   145  H HA   . ASP   A 1 18  ? -19.569 3.151   34.785  1   72.677  ? 30  ASP   A HA   1 c 1 
ATOM   146  H HB2  . ASP   A 1 18  ? -19.432 2.8     32.44   1   68.623  ? 30  ASP   A HB2  1 c 1 
ATOM   147  H HB3  . ASP   A 1 18  ? -20.699 3.723   32.727  1   69.225  ? 30  ASP   A HB3  1 c 1 
ATOM   148  N N    . ARG   A 1 19  ? -17.175 4.884   34.955  1   74.312  ? 31  ARG   A N    1 ? 1 
ATOM   149  C CA   . ARG   A 1 19  ? -15.737 4.978   35.14   1   69.901  ? 31  ARG   A CA   1 ? 1 
ATOM   150  C C    . ARG   A 1 19  ? -15.034 5.116   33.8    1   58.095  ? 31  ARG   A C    1 ? 1 
ATOM   151  O O    . ARG   A 1 19  ? -13.859 4.77    33.712  1   54.046  ? 31  ARG   A O    1 ? 1 
ATOM   152  C CB   . ARG   A 1 19  ? -15.148 3.834   35.98   1   75.793  ? 31  ARG   A CB   1 ? 1 
ATOM   153  C CG   . ARG   A 1 19  ? -15.665 3.931   37.411  1   90.26   ? 31  ARG   A CG   1 ? 1 
ATOM   154  C CD   . ARG   A 1 19  ? -15.197 2.855   38.371  1   101.854 ? 31  ARG   A CD   1 ? 1 
ATOM   155  N NE   . ARG   A 1 19  ? -13.735 2.753   38.328  1   108.455 ? 31  ARG   A NE   1 ? 1 
ATOM   156  C CZ   . ARG   A 1 19  ? -12.894 3.573   38.921  1   102.346 ? 31  ARG   A CZ   1 ? 1 
ATOM   157  N NH1  . ARG   A 1 19  ? -13.34  4.624   39.588  1   96.542  ? 31  ARG   A NH1  1 ? 1 
ATOM   158  N NH2  . ARG   A 1 19  ? -11.608 3.305   38.852  1   106.904 ? 31  ARG   A NH2  1 ? 1 
ATOM   159  H H    . ARG   A 1 19  ? -17.709 5.493   35.376  1   73.771  ? 31  ARG   A H    1 c 1 
ATOM   160  H HA   . ARG   A 1 19  ? -15.561 5.81    35.646  1   67.827  ? 31  ARG   A HA   1 c 1 
ATOM   161  H HB2  . ARG   A 1 19  ? -15.405 2.969   35.596  1   79.128  ? 31  ARG   A HB2  1 c 1 
ATOM   162  H HB3  . ARG   A 1 19  ? -14.169 3.893   35.983  1   76.425  ? 31  ARG   A HB3  1 c 1 
ATOM   163  H HG2  . ARG   A 1 19  ? -15.406 4.804   37.777  1   87.283  ? 31  ARG   A HG2  1 c 1 
ATOM   164  H HG3  . ARG   A 1 19  ? -16.647 3.916   37.388  1   89.928  ? 31  ARG   A HG3  1 c 1 
ATOM   165  H HD2  . ARG   A 1 19  ? -15.483 3.073   39.282  1   102.609 ? 31  ARG   A HD2  1 c 1 
ATOM   166  H HD3  . ARG   A 1 19  ? -15.591 1.994   38.122  1   103.5   ? 31  ARG   A HD3  1 c 1 
ATOM   167  H HE   . ARG   A 1 19  ? -13.392 2.095   37.871  1   106.157 ? 31  ARG   A HE   1 c 1 
ATOM   168  H HH11 . ARG   A 1 19  ? -13.854 4.509   40.299  1   99.744  ? 31  ARG   A HH11 1 c 1 
ATOM   169  H HH12 . ARG   A 1 19  ? -13.123 5.438   39.32   1   96.031  ? 31  ARG   A HH12 1 c 1 
ATOM   170  H HH21 . ARG   A 1 19  ? -11.314 2.501   39.073  1   107.367 ? 31  ARG   A HH21 1 c 1 
ATOM   171  H HH22 . ARG   A 1 19  ? -11.044 3.931   38.586  1   103.373 ? 31  ARG   A HH22 1 c 1 
ATOM   172  N N    . GLY   A 1 20  ? -15.699 5.746   32.824  1   57.383  ? 32  GLY   A N    1 ? 1 
ATOM   173  C CA   . GLY   A 1 20  ? -15.137 5.918   31.484  1   52.764  ? 32  GLY   A CA   1 ? 1 
ATOM   174  C C    . GLY   A 1 20  ? -14.043 6.982   31.474  1   63.765  ? 32  GLY   A C    1 ? 1 
ATOM   175  O O    . GLY   A 1 20  ? -12.938 6.813   30.902  1   54.296  ? 32  GLY   A O    1 ? 1 
ATOM   176  H H    . GLY   A 1 20  ? -16.523 6.099   32.998  1   57.319  ? 32  GLY   A H    1 c 1 
ATOM   177  H HA2  . GLY   A 1 20  ? -14.766 5.058   31.176  1   57.068  ? 32  GLY   A HA2  1 c 1 
ATOM   178  H HA3  . GLY   A 1 20  ? -15.856 6.178   30.865  1   56.542  ? 32  GLY   A HA3  1 c 1 
ATOM   179  N N    . VAL   A 1 21  ? -14.409 8.096   32.156  1   64.186  ? 33  VAL   A N    1 ? 1 
ATOM   180  C CA   . VAL   A 1 21  ? -13.595 9.296   32.229  1   50.376  ? 33  VAL   A CA   1 ? 1 
ATOM   181  C C    . VAL   A 1 21  ? -13.284 9.499   33.706  1   55.686  ? 33  VAL   A C    1 ? 1 
ATOM   182  O O    . VAL   A 1 21  ? -14.188 9.791   34.496  1   44.934  ? 33  VAL   A O    1 ? 1 
ATOM   183  C CB   . VAL   A 1 21  ? -14.159 10.599  31.637  1   45.285  ? 33  VAL   A CB   1 ? 1 
ATOM   184  C CG1  . VAL   A 1 21  ? -13.147 11.731  31.649  1   41.203  ? 33  VAL   A CG1  1 ? 1 
ATOM   185  C CG2  . VAL   A 1 21  ? -14.69  10.407  30.224  1   49.607  ? 33  VAL   A CG2  1 ? 1 
ATOM   186  H H    . VAL   A 1 21  ? -15.207 8.092   32.599  1   61.409  ? 33  VAL   A H    1 c 1 
ATOM   187  H HA   . VAL   A 1 21  ? -12.755 9.109   31.769  1   51.917  ? 33  VAL   A HA   1 c 1 
ATOM   188  H HB   . VAL   A 1 21  ? -14.917 10.871  32.205  1   46.871  ? 33  VAL   A HB   1 c 1 
ATOM   189  H HG11 . VAL   A 1 21  ? -12.305 11.417  31.278  1   41.587  ? 33  VAL   A HG11 1 c 1 
ATOM   190  H HG12 . VAL   A 1 21  ? -13.006 12.032  32.562  1   42.055  ? 33  VAL   A HG12 1 c 1 
ATOM   191  H HG13 . VAL   A 1 21  ? -13.48  12.47   31.113  1   41.969  ? 33  VAL   A HG13 1 c 1 
ATOM   192  H HG21 . VAL   A 1 21  ? -15.056 11.246  29.897  1   48.317  ? 33  VAL   A HG21 1 c 1 
ATOM   193  H HG22 . VAL   A 1 21  ? -15.388 9.731   30.229  1   49.637  ? 33  VAL   A HG22 1 c 1 
ATOM   194  H HG23 . VAL   A 1 21  ? -13.967 10.121  29.641  1   48.007  ? 33  VAL   A HG23 1 c 1 
ATOM   195  N N    . LEU   A 1 22  ? -11.998 9.318   34.025  1   51.192  ? 34  LEU   A N    1 ? 1 
ATOM   196  C CA   . LEU   A 1 22  ? -11.463 9.527   35.342  1   46.803  ? 34  LEU   A CA   1 ? 1 
ATOM   197  C C    . LEU   A 1 22  ? -10.565 10.742  35.339  1   42.921  ? 34  LEU   A C    1 ? 1 
ATOM   198  O O    . LEU   A 1 22  ? -9.635  10.835  34.559  1   45.538  ? 34  LEU   A O    1 ? 1 
ATOM   199  C CB   . LEU   A 1 22  ? -10.727 8.242   35.677  1   48.011  ? 34  LEU   A CB   1 ? 1 
ATOM   200  C CG   . LEU   A 1 22  ? -11.663 7.039   35.681  1   55.236  ? 34  LEU   A CG   1 ? 1 
ATOM   201  C CD1  . LEU   A 1 22  ? -10.944 5.715   35.709  1   59.31   ? 34  LEU   A CD1  1 ? 1 
ATOM   202  C CD2  . LEU   A 1 22  ? -12.622 7.204   36.849  1   58.094  ? 34  LEU   A CD2  1 ? 1 
ATOM   203  H H    . LEU   A 1 22  ? -11.423 9.047   33.368  1   50.496  ? 34  LEU   A H    1 c 1 
ATOM   204  H HA   . LEU   A 1 22  ? -12.206 9.662   35.975  1   47.904  ? 34  LEU   A HA   1 c 1 
ATOM   205  H HB2  . LEU   A 1 22  ? -10.024 8.096   35.003  1   48.73   ? 34  LEU   A HB2  1 c 1 
ATOM   206  H HB3  . LEU   A 1 22  ? -10.317 8.334   36.567  1   49.931  ? 34  LEU   A HB3  1 c 1 
ATOM   207  H HG   . LEU   A 1 22  ? -12.2   7.065   34.849  1   54.36   ? 34  LEU   A HG   1 c 1 
ATOM   208  H HD11 . LEU   A 1 22  ? -10.357 5.648   34.937  1   57.908  ? 34  LEU   A HD11 1 c 1 
ATOM   209  H HD12 . LEU   A 1 22  ? -11.594 4.992   35.683  1   59.988  ? 34  LEU   A HD12 1 c 1 
ATOM   210  H HD13 . LEU   A 1 22  ? -10.418 5.647   36.523  1   59.412  ? 34  LEU   A HD13 1 c 1 
ATOM   211  H HD21 . LEU   A 1 22  ? -13.351 7.789   36.59   1   56.868  ? 34  LEU   A HD21 1 c 1 
ATOM   212  H HD22 . LEU   A 1 22  ? -12.152 7.588   37.608  1   57.625  ? 34  LEU   A HD22 1 c 1 
ATOM   213  H HD23 . LEU   A 1 22  ? -12.981 6.335   37.099  1   59.321  ? 34  LEU   A HD23 1 c 1 
ATOM   214  N N    . LYS   A 1 23  ? -10.78  11.62   36.323  1   45.936  ? 35  LYS   A N    1 ? 1 
ATOM   215  C CA   . LYS   A 1 23  ? -10.043 12.86   36.446  1   42.832  ? 35  LYS   A CA   1 ? 1 
ATOM   216  C C    . LYS   A 1 23  ? -9.263  12.976  37.762  1   45.934  ? 35  LYS   A C    1 ? 1 
ATOM   217  O O    . LYS   A 1 23  ? -9.774  12.628  38.814  1   45.054  ? 35  LYS   A O    1 ? 1 
ATOM   218  C CB   . LYS   A 1 23  ? -11.094 13.974  36.41   1   42.656  ? 35  LYS   A CB   1 ? 1 
ATOM   219  C CG   . LYS   A 1 23  ? -10.488 15.391  36.517  1   40.952  ? 35  LYS   A CG   1 ? 1 
ATOM   220  C CD   . LYS   A 1 23  ? -11.539 16.452  36.928  1   44.389  ? 35  LYS   A CD   1 ? 1 
ATOM   221  C CE   . LYS   A 1 23  ? -10.96  17.821  36.849  1   46.529  ? 35  LYS   A CE   1 ? 1 
ATOM   222  N NZ   . LYS   A 1 23  ? -11.835 18.856  37.376  1   51.297  ? 35  LYS   A NZ   1 ? 1 
ATOM   223  H H    . LYS   A 1 23  ? -11.418 11.432  36.95   1   45.589  ? 35  LYS   A H    1 c 1 
ATOM   224  H HA   . LYS   A 1 23  ? -9.426  12.95   35.681  1   42.997  ? 35  LYS   A HA   1 c 1 
ATOM   225  H HB2  . LYS   A 1 23  ? -11.598 13.91   35.571  1   41.856  ? 35  LYS   A HB2  1 c 1 
ATOM   226  H HB3  . LYS   A 1 23  ? -11.724 13.844  37.151  1   43.212  ? 35  LYS   A HB3  1 c 1 
ATOM   227  H HG2  . LYS   A 1 23  ? -9.765  15.383  37.18   1   42.442  ? 35  LYS   A HG2  1 c 1 
ATOM   228  H HG3  . LYS   A 1 23  ? -10.103 15.637  35.648  1   41.231  ? 35  LYS   A HG3  1 c 1 
ATOM   229  H HD2  . LYS   A 1 23  ? -12.315 16.393  36.33   1   44.01   ? 35  LYS   A HD2  1 c 1 
ATOM   230  H HD3  . LYS   A 1 23  ? -11.837 16.278  37.847  1   45.161  ? 35  LYS   A HD3  1 c 1 
ATOM   231  H HE2  . LYS   A 1 23  ? -10.122 17.839  37.344  1   47.163  ? 35  LYS   A HE2  1 c 1 
ATOM   232  H HE3  . LYS   A 1 23  ? -10.759 18.027  35.919  1   46.214  ? 35  LYS   A HE3  1 c 1 
ATOM   233  H HZ1  . LYS   A 1 23  ? -12.247 18.564  38.129  1   50.877  ? 35  LYS   A HZ1  1 c 1 
ATOM   234  H HZ2  . LYS   A 1 23  ? -12.459 19.069  36.758  1   50.175  ? 35  LYS   A HZ2  1 c 1 
ATOM   235  H HZ3  . LYS   A 1 23  ? -11.349 19.595  37.571  1   50.851  ? 35  LYS   A HZ3  1 c 1 
ATOM   236  N N    . ILE   A 1 24  ? -8.047  13.544  37.686  1   47.629  ? 36  ILE   A N    1 ? 1 
ATOM   237  C CA   . ILE   A 1 24  ? -7.39   14.066  38.863  1   50.055  ? 36  ILE   A CA   1 ? 1 
ATOM   238  C C    . ILE   A 1 24  ? -6.923  15.492  38.599  1   47.45   ? 36  ILE   A C    1 ? 1 
ATOM   239  O O    . ILE   A 1 24  ? -6.35   15.752  37.55   1   45.99   ? 36  ILE   A O    1 ? 1 
ATOM   240  C CB   . ILE   A 1 24  ? -6.179  13.206  39.257  1   54.07   ? 36  ILE   A CB   1 ? 1 
ATOM   241  C CG1  . ILE   A 1 24  ? -6.539  11.757  39.359  1   54.139  ? 36  ILE   A CG1  1 ? 1 
ATOM   242  C CG2  . ILE   A 1 24  ? -5.532  13.755  40.537  1   51.584  ? 36  ILE   A CG2  1 ? 1 
ATOM   243  C CD1  . ILE   A 1 24  ? -5.306  10.879  39.498  1   63.333  ? 36  ILE   A CD1  1 ? 1 
ATOM   244  H H    . ILE   A 1 24  ? -7.623  13.601  36.879  1   46.636  ? 36  ILE   A H    1 c 1 
ATOM   245  H HA   . ILE   A 1 24  ? -8.025  14.072  39.606  1   50.543  ? 36  ILE   A HA   1 c 1 
ATOM   246  H HB   . ILE   A 1 24  ? -5.521  13.29   38.539  1   52.047  ? 36  ILE   A HB   1 c 1 
ATOM   247  H HG12 . ILE   A 1 24  ? -7.119  11.623  40.136  1   56.78   ? 36  ILE   A HG12 1 c 1 
ATOM   248  H HG13 . ILE   A 1 24  ? -7.033  11.488  38.558  1   54.66   ? 36  ILE   A HG13 1 c 1 
ATOM   249  H HG21 . ILE   A 1 24  ? -4.905  13.105  40.894  1   54.173  ? 36  ILE   A HG21 1 c 1 
ATOM   250  H HG22 . ILE   A 1 24  ? -6.221  13.934  41.2    1   53.431  ? 36  ILE   A HG22 1 c 1 
ATOM   251  H HG23 . ILE   A 1 24  ? -5.058  14.578  40.336  1   52.749  ? 36  ILE   A HG23 1 c 1 
ATOM   252  H HD11 . ILE   A 1 24  ? -4.596  11.21   38.916  1   60.373  ? 36  ILE   A HD11 1 c 1 
ATOM   253  H HD12 . ILE   A 1 24  ? -5.531  9.965   39.243  1   61.244  ? 36  ILE   A HD12 1 c 1 
ATOM   254  H HD13 . ILE   A 1 24  ? -4.997  10.889  40.423  1   62.478  ? 36  ILE   A HD13 1 c 1 
ATOM   255  N N    . VAL   A 1 25  ? -7.141  16.365  39.586  1   47.082  ? 37  VAL   A N    1 ? 1 
ATOM   256  C CA   . VAL   A 1 25  ? -6.635  17.712  39.59   1   44.397  ? 37  VAL   A CA   1 ? 1 
ATOM   257  C C    . VAL   A 1 25  ? -5.203  17.632  40.09   1   46.708  ? 37  VAL   A C    1 ? 1 
ATOM   258  O O    . VAL   A 1 25  ? -4.965  17.027  41.132  1   45.906  ? 37  VAL   A O    1 ? 1 
ATOM   259  C CB   . VAL   A 1 25  ? -7.517  18.442  40.593  1   49.425  ? 37  VAL   A CB   1 ? 1 
ATOM   260  C CG1  . VAL   A 1 25  ? -6.994  19.829  40.859  1   49.117  ? 37  VAL   A CG1  1 ? 1 
ATOM   261  C CG2  . VAL   A 1 25  ? -8.955  18.458  40.131  1   54.213  ? 37  VAL   A CG2  1 ? 1 
ATOM   262  H H    . VAL   A 1 25  ? -7.626  16.084  40.308  1   47.51   ? 37  VAL   A H    1 c 1 
ATOM   263  H HA   . VAL   A 1 25  ? -6.689  18.115  38.702  1   44.964  ? 37  VAL   A HA   1 c 1 
ATOM   264  H HB   . VAL   A 1 25  ? -7.476  17.94   41.441  1   50.264  ? 37  VAL   A HB   1 c 1 
ATOM   265  H HG11 . VAL   A 1 25  ? -6.704  20.233  40.024  1   49.044  ? 37  VAL   A HG11 1 c 1 
ATOM   266  H HG12 . VAL   A 1 25  ? -6.243  19.782  41.474  1   50.951  ? 37  VAL   A HG12 1 c 1 
ATOM   267  H HG13 . VAL   A 1 25  ? -7.698  20.373  41.253  1   50.551  ? 37  VAL   A HG13 1 c 1 
ATOM   268  H HG21 . VAL   A 1 25  ? -9.46   19.099  40.66   1   53.415  ? 37  VAL   A HG21 1 c 1 
ATOM   269  H HG22 . VAL   A 1 25  ? -9.344  17.574  40.24   1   51.917  ? 37  VAL   A HG22 1 c 1 
ATOM   270  H HG23 . VAL   A 1 25  ? -8.992  18.714  39.194  1   51.267  ? 37  VAL   A HG23 1 c 1 
ATOM   271  N N    . LYS   A 1 26  ? -4.262  18.189  39.318  1   48.124  ? 38  LYS   A N    1 ? 1 
ATOM   272  C CA   . LYS   A 1 26  ? -2.853  18.102  39.658  1   53.003  ? 38  LYS   A CA   1 ? 1 
ATOM   273  C C    . LYS   A 1 26  ? -2.375  19.428  40.231  1   54.461  ? 38  LYS   A C    1 ? 1 
ATOM   274  O O    . LYS   A 1 26  ? -1.69   19.428  41.244  1   65.211  ? 38  LYS   A O    1 ? 1 
ATOM   275  C CB   . LYS   A 1 26  ? -2.071  17.651  38.422  1   55.705  ? 38  LYS   A CB   1 ? 1 
ATOM   276  C CG   . LYS   A 1 26  ? -2.361  16.238  37.995  1   54.198  ? 38  LYS   A CG   1 ? 1 
ATOM   277  C CD   . LYS   A 1 26  ? -2.277  15.159  39.071  1   56.078  ? 38  LYS   A CD   1 ? 1 
ATOM   278  C CE   . LYS   A 1 26  ? -0.932  15.196  39.709  1   58.809  ? 38  LYS   A CE   1 ? 1 
ATOM   279  N NZ   . LYS   A 1 26  ? -0.902  14      40.538  1   61.393  ? 38  LYS   A NZ   1 ? 1 
ATOM   280  H H    . LYS   A 1 26  ? -4.507  18.626  38.554  1   47.63   ? 38  LYS   A H    1 c 1 
ATOM   281  H HA   . LYS   A 1 26  ? -2.744  17.414  40.36   1   53.619  ? 38  LYS   A HA   1 c 1 
ATOM   282  H HB2  . LYS   A 1 26  ? -2.286  18.251  37.678  1   54.131  ? 38  LYS   A HB2  1 c 1 
ATOM   283  H HB3  . LYS   A 1 26  ? -1.111  17.733  38.605  1   56.427  ? 38  LYS   A HB3  1 c 1 
ATOM   284  H HG2  . LYS   A 1 26  ? -3.262  16.218  37.606  1   52.889  ? 38  LYS   A HG2  1 c 1 
ATOM   285  H HG3  . LYS   A 1 26  ? -1.734  16.008  37.279  1   54.278  ? 38  LYS   A HG3  1 c 1 
ATOM   286  H HD2  . LYS   A 1 26  ? -2.967  15.311  39.751  1   55.978  ? 38  LYS   A HD2  1 c 1 
ATOM   287  H HD3  . LYS   A 1 26  ? -2.422  14.278  38.663  1   55.255  ? 38  LYS   A HD3  1 c 1 
ATOM   288  H HE2  . LYS   A 1 26  ? -0.225  15.159  39.041  1   59.268  ? 38  LYS   A HE2  1 c 1 
ATOM   289  H HE3  . LYS   A 1 26  ? -0.823  15.989  40.264  1   60.108  ? 38  LYS   A HE3  1 c 1 
ATOM   290  H HZ1  . LYS   A 1 26  ? -0.91   13.258  40.017  1   60.375  ? 38  LYS   A HZ1  1 c 1 
ATOM   291  H HZ2  . LYS   A 1 26  ? -1.618  13.983  41.094  1   60.854  ? 38  LYS   A HZ2  1 c 1 
ATOM   292  H HZ3  . LYS   A 1 26  ? -0.145  13.999  41.037  1   62.985  ? 38  LYS   A HZ3  1 c 1 
ATOM   293  N N    . ARG   A 1 27  ? -2.847  20.533  39.637  1   55.5    ? 39  ARG   A N    1 ? 1 
ATOM   294  C CA   . ARG   A 1 27  ? -2.677  21.864  40.185  1   58.157  ? 39  ARG   A CA   1 ? 1 
ATOM   295  C C    . ARG   A 1 27  ? -4.04   22.551  40.168  1   62.763  ? 39  ARG   A C    1 ? 1 
ATOM   296  O O    . ARG   A 1 27  ? -4.74   22.539  39.146  1   60.072  ? 39  ARG   A O    1 ? 1 
ATOM   297  C CB   . ARG   A 1 27  ? -1.579  22.671  39.475  1   59.502  ? 39  ARG   A CB   1 ? 1 
ATOM   298  C CG   . ARG   A 1 27  ? -1.154  23.969  40.158  1   61.789  ? 39  ARG   A CG   1 ? 1 
ATOM   299  C CD   . ARG   A 1 27  ? -0.344  24.879  39.267  1   61.367  ? 39  ARG   A CD   1 ? 1 
ATOM   300  N NE   . ARG   A 1 27  ? -1.226  25.253  38.151  1   64.688  ? 39  ARG   A NE   1 ? 1 
ATOM   301  C CZ   . ARG   A 1 27  ? -0.77   25.668  36.972  1   62.481  ? 39  ARG   A CZ   1 ? 1 
ATOM   302  N NH1  . ARG   A 1 27  ? 0.528   25.669  36.77   1   64.769  ? 39  ARG   A NH1  1 ? 1 
ATOM   303  N NH2  . ARG   A 1 27  ? -1.572  26.08   36.013  1   61.711  ? 39  ARG   A NH2  1 ? 1 
ATOM   304  H H    . ARG   A 1 27  ? -3.283  20.449  38.839  1   53.682  ? 39  ARG   A H    1 c 1 
ATOM   305  H HA   . ARG   A 1 27  ? -2.398  21.768  41.131  1   60.566  ? 39  ARG   A HA   1 c 1 
ATOM   306  H HB2  . ARG   A 1 27  ? -0.789  22.097  39.383  1   59.535  ? 39  ARG   A HB2  1 c 1 
ATOM   307  H HB3  . ARG   A 1 27  ? -1.894  22.882  38.57   1   58.178  ? 39  ARG   A HB3  1 c 1 
ATOM   308  H HG2  . ARG   A 1 27  ? -1.955  24.451  40.459  1   61.666  ? 39  ARG   A HG2  1 c 1 
ATOM   309  H HG3  . ARG   A 1 27  ? -0.623  23.751  40.954  1   63.055  ? 39  ARG   A HG3  1 c 1 
ATOM   310  H HD2  . ARG   A 1 27  ? -0.061  25.681  39.751  1   65.523  ? 39  ARG   A HD2  1 c 1 
ATOM   311  H HD3  . ARG   A 1 27  ? 0.447   24.413  38.927  1   63.074  ? 39  ARG   A HD3  1 c 1 
ATOM   312  H HE   . ARG   A 1 27  ? -2.089  25.209  38.264  1   61.64   ? 39  ARG   A HE   1 c 1 
ATOM   313  H HH11 . ARG   A 1 27  ? 1.059   26.117  37.317  1   66.957  ? 39  ARG   A HH11 1 c 1 
ATOM   314  H HH12 . ARG   A 1 27  ? 0.868   25.233  36.082  1   63.993  ? 39  ARG   A HH12 1 c 1 
ATOM   315  H HH21 . ARG   A 1 27  ? -2.348  25.677  35.886  1   59.77   ? 39  ARG   A HH21 1 c 1 
ATOM   316  H HH22 . ARG   A 1 27  ? -1.33   26.758  35.499  1   63.192  ? 39  ARG   A HH22 1 c 1 
ATOM   317  N N    . VAL   A 1 28  ? -4.381  23.149  41.327  1   63.997  ? 40  VAL   A N    1 ? 1 
ATOM   318  C CA   . VAL   A 1 28  ? -5.694  23.709  41.594  1   67.197  ? 40  VAL   A CA   1 ? 1 
ATOM   319  C C    . VAL   A 1 28  ? -5.773  25.022  40.846  1   65.768  ? 40  VAL   A C    1 ? 1 
ATOM   320  O O    . VAL   A 1 28  ? -4.817  25.771  40.926  1   66.943  ? 40  VAL   A O    1 ? 1 
ATOM   321  C CB   . VAL   A 1 28  ? -5.908  23.915  43.101  1   72.431  ? 40  VAL   A CB   1 ? 1 
ATOM   322  C CG1  . VAL   A 1 28  ? -7.277  24.481  43.426  1   75.804  ? 40  VAL   A CG1  1 ? 1 
ATOM   323  C CG2  . VAL   A 1 28  ? -5.7    22.618  43.864  1   74.957  ? 40  VAL   A CG2  1 ? 1 
ATOM   324  H H    . VAL   A 1 28  ? -3.744  23.221  41.978  1   66.61   ? 40  VAL   A H    1 c 1 
ATOM   325  H HA   . VAL   A 1 28  ? -6.376  23.099  41.252  1   64.773  ? 40  VAL   A HA   1 c 1 
ATOM   326  H HB   . VAL   A 1 28  ? -5.229  24.562  43.408  1   74.988  ? 40  VAL   A HB   1 c 1 
ATOM   327  H HG11 . VAL   A 1 28  ? -7.958  23.981  42.946  1   73.137  ? 40  VAL   A HG11 1 c 1 
ATOM   328  H HG12 . VAL   A 1 28  ? -7.315  25.415  43.16   1   76.195  ? 40  VAL   A HG12 1 c 1 
ATOM   329  H HG13 . VAL   A 1 28  ? -7.44   24.413  44.382  1   76.564  ? 40  VAL   A HG13 1 c 1 
ATOM   330  H HG21 . VAL   A 1 28  ? -5.987  22.732  44.786  1   75.775  ? 40  VAL   A HG21 1 c 1 
ATOM   331  H HG22 . VAL   A 1 28  ? -4.758  22.378  43.849  1   74.359  ? 40  VAL   A HG22 1 c 1 
ATOM   332  H HG23 . VAL   A 1 28  ? -6.221  21.91   43.449  1   72.063  ? 40  VAL   A HG23 1 c 1 
ATOM   333  N N    . GLY   A 1 29  ? -6.872  25.251  40.097  1   72.836  ? 41  GLY   A N    1 ? 1 
ATOM   334  C CA   . GLY   A 1 29  ? -7.099  26.547  39.466  1   74.947  ? 41  GLY   A CA   1 ? 1 
ATOM   335  C C    . GLY   A 1 29  ? -7.515  27.619  40.486  1   84.181  ? 41  GLY   A C    1 ? 1 
ATOM   336  O O    . GLY   A 1 29  ? -7.121  27.573  41.656  1   87.052  ? 41  GLY   A O    1 ? 1 
ATOM   337  H H    . GLY   A 1 29  ? -7.488  24.587  39.979  1   69.1    ? 41  GLY   A H    1 c 1 
ATOM   338  H HA2  . GLY   A 1 29  ? -6.274  26.832  39.009  1   76.444  ? 41  GLY   A HA2  1 c 1 
ATOM   339  H HA3  . GLY   A 1 29  ? -7.805  26.451  38.785  1   74.794  ? 41  GLY   A HA3  1 c 1 
ATOM   340  N N    . ASN   A 1 30  ? -8.283  28.618  40.014  1   87.271  ? 42  ASN   A N    1 ? 1 
ATOM   341  C CA   . ASN   A 1 30  ? -9.037  29.516  40.881  1   89.895  ? 42  ASN   A CA   1 ? 1 
ATOM   342  C C    . ASN   A 1 30  ? -10.217 30.109  40.112  1   85.001  ? 42  ASN   A C    1 ? 1 
ATOM   343  O O    . ASN   A 1 30  ? -10.449 29.813  38.951  1   86.57   ? 42  ASN   A O    1 ? 1 
ATOM   344  C CB   . ASN   A 1 30  ? -8.17   30.629  41.449  1   95.132  ? 42  ASN   A CB   1 ? 1 
ATOM   345  C CG   . ASN   A 1 30  ? -7.206  31.1    40.398  1   99.112  ? 42  ASN   A CG   1 ? 1 
ATOM   346  O OD1  . ASN   A 1 30  ? -6.023  31.233  40.71   1   105.54  ? 42  ASN   A OD1  1 ? 1 
ATOM   347  N ND2  . ASN   A 1 30  ? -7.666  31.26   39.16   1   97.48   ? 42  ASN   A ND2  1 ? 1 
ATOM   348  H H    . ASN   A 1 30  ? -8.343  28.733  39.109  1   86.061  ? 42  ASN   A H    1 c 1 
ATOM   349  H HA   . ASN   A 1 30  ? -9.387  28.994  41.638  1   88.763  ? 42  ASN   A HA   1 c 1 
ATOM   350  H HB2  . ASN   A 1 30  ? -8.727  31.376  41.741  1   97.927  ? 42  ASN   A HB2  1 c 1 
ATOM   351  H HB3  . ASN   A 1 30  ? -7.672  30.294  42.222  1   95.902  ? 42  ASN   A HB3  1 c 1 
ATOM   352  H HD21 . ASN   A 1 30  ? -7.367  30.741  38.505  1   95.608  ? 42  ASN   A HD21 1 c 1 
ATOM   353  H HD22 . ASN   A 1 30  ? -8.266  31.891  38.989  1   99.232  ? 42  ASN   A HD22 1 c 1 
ATOM   354  N N    . GLY   A 1 31  ? -11.007 30.926  40.802  1   88.673  ? 43  GLY   A N    1 ? 1 
ATOM   355  C CA   . GLY   A 1 31  ? -12.318 31.332  40.336  1   89.002  ? 43  GLY   A CA   1 ? 1 
ATOM   356  C C    . GLY   A 1 31  ? -13.342 30.317  40.827  1   94.672  ? 43  GLY   A C    1 ? 1 
ATOM   357  O O    . GLY   A 1 31  ? -13.04  29.134  40.988  1   91.228  ? 43  GLY   A O    1 ? 1 
ATOM   358  H H    . GLY   A 1 31  ? -10.725 31.235  41.614  1   90.373  ? 43  GLY   A H    1 c 1 
ATOM   359  H HA2  . GLY   A 1 31  ? -12.53  32.227  40.69   1   94.096  ? 43  GLY   A HA2  1 c 1 
ATOM   360  H HA3  . GLY   A 1 31  ? -12.326 31.374  39.352  1   89.924  ? 43  GLY   A HA3  1 c 1 
ATOM   361  N N    . GLU   A 1 32  ? -14.562 30.796  41.078  1   108.908 ? 44  GLU   A N    1 ? 1 
ATOM   362  C CA   . GLU   A 1 32  ? -15.697 29.912  41.29   1   102.141 ? 44  GLU   A CA   1 ? 1 
ATOM   363  C C    . GLU   A 1 32  ? -16.087 29.241  39.964  1   91.784  ? 44  GLU   A C    1 ? 1 
ATOM   364  O O    . GLU   A 1 32  ? -16.58  28.117  39.995  1   86.665  ? 44  GLU   A O    1 ? 1 
ATOM   365  C CB   . GLU   A 1 32  ? -16.845 30.709  41.911  1   103.753 ? 44  GLU   A CB   1 ? 1 
ATOM   366  H H    . GLU   A 1 32  ? -14.691 31.701  41.116  1   107.221 ? 44  GLU   A H    1 c 1 
ATOM   367  H HA   . GLU   A 1 32  ? -15.426 29.207  41.931  1   99.855  ? 44  GLU   A HA   1 c 1 
ATOM   368  H HB2  . GLU   A 1 32  ? -16.399 31.037  42.784  0   30      ? 44  GLU   A HB2  1 c 1 
ATOM   369  H HB3  . GLU   A 1 32  ? -17.657 30.139  41.756  0   30      ? 44  GLU   A HB3  1 c 1 
ATOM   370  N N    . GLU   A 1 33  ? -15.817 29.905  38.818  1   81.955  ? 45  GLU   A N    1 ? 1 
ATOM   371  C CA   . GLU   A 1 33  ? -16.476 29.602  37.562  1   79.058  ? 45  GLU   A CA   1 ? 1 
ATOM   372  C C    . GLU   A 1 33  ? -15.72  28.514  36.802  1   72.665  ? 45  GLU   A C    1 ? 1 
ATOM   373  O O    . GLU   A 1 33  ? -14.509 28.596  36.599  1   69.984  ? 45  GLU   A O    1 ? 1 
ATOM   374  C CB   . GLU   A 1 33  ? -16.617 30.836  36.68   1   82.98   ? 45  GLU   A CB   1 ? 1 
ATOM   375  C CG   . GLU   A 1 33  ? -17.298 31.992  37.405  1   92.339  ? 45  GLU   A CG   1 ? 1 
ATOM   376  C CD   . GLU   A 1 33  ? -16.991 33.289  36.694  1   99.137  ? 45  GLU   A CD   1 ? 1 
ATOM   377  O OE1  . GLU   A 1 33  ? -16.612 33.104  35.51   1   94.994  ? 45  GLU   A OE1  1 ? 1 
ATOM   378  O OE2  . GLU   A 1 33  ? -17.057 34.412  37.277  1   105.449 ? 45  GLU   A OE2  1 ? 1 
ATOM   379  H H    . GLU   A 1 33  ? -15.194 30.574  38.828  1   85.244  ? 45  GLU   A H    1 c 1 
ATOM   380  H HA   . GLU   A 1 33  ? -17.387 29.269  37.767  1   79.576  ? 45  GLU   A HA   1 c 1 
ATOM   381  H HB2  . GLU   A 1 33  ? -15.724 31.11   36.383  1   83.469  ? 45  GLU   A HB2  1 c 1 
ATOM   382  H HB3  . GLU   A 1 33  ? -17.138 30.598  35.884  1   83.416  ? 45  GLU   A HB3  1 c 1 
ATOM   383  H HG2  . GLU   A 1 33  ? -18.269 31.851  37.416  1   92.938  ? 45  GLU   A HG2  1 c 1 
ATOM   384  H HG3  . GLU   A 1 33  ? -16.975 32.046  38.328  1   92.324  ? 45  GLU   A HG3  1 c 1 
ATOM   385  N N    . THR   A 1 34  ? -16.48  27.506  36.373  1   67.524  ? 46  THR   A N    1 ? 1 
ATOM   386  C CA   . THR   A 1 34  ? -16.051 26.619  35.298  1   65.973  ? 46  THR   A CA   1 ? 1 
ATOM   387  C C    . THR   A 1 34  ? -16.664 27.084  33.978  1   67.829  ? 46  THR   A C    1 ? 1 
ATOM   388  O O    . THR   A 1 34  ? -17.672 27.784  33.954  1   79.627  ? 46  THR   A O    1 ? 1 
ATOM   389  C CB   . THR   A 1 34  ? -16.439 25.188  35.632  1   60.566  ? 46  THR   A CB   1 ? 1 
ATOM   390  O OG1  . THR   A 1 34  ? -17.827 25.163  35.896  1   62.822  ? 46  THR   A OG1  1 ? 1 
ATOM   391  C CG2  . THR   A 1 34  ? -15.813 24.703  36.913  1   61.594  ? 46  THR   A CG2  1 ? 1 
ATOM   392  H H    . THR   A 1 34  ? -17.293 27.358  36.764  1   69.585  ? 46  THR   A H    1 c 1 
ATOM   393  H HA   . THR   A 1 34  ? -15.074 26.667  35.228  1   64.31   ? 46  THR   A HA   1 c 1 
ATOM   394  H HB   . THR   A 1 34  ? -16.224 24.581  34.885  1   59.786  ? 46  THR   A HB   1 c 1 
ATOM   395  H HG1  . THR   A 1 34  ? -18.077 25.662  36.508  0   30      ? 46  THR   A HG1  1 c 1 
ATOM   396  H HG21 . THR   A 1 34  ? -16.006 23.758  37.032  1   59.629  ? 46  THR   A HG21 1 c 1 
ATOM   397  H HG22 . THR   A 1 34  ? -16.175 25.204  37.663  1   62.904  ? 46  THR   A HG22 1 c 1 
ATOM   398  H HG23 . THR   A 1 34  ? -14.85  24.833  36.873  1   60.241  ? 46  THR   A HG23 1 c 1 
ATOM   399  N N    . PRO   A 1 35  ? -16.066 26.751  32.82   1   70.037  ? 47  PRO   A N    1 ? 1 
ATOM   400  C CA   . PRO   A 1 35  ? -16.65  27.131  31.541  1   72.935  ? 47  PRO   A CA   1 ? 1 
ATOM   401  C C    . PRO   A 1 35  ? -18.073 26.601  31.359  1   78.287  ? 47  PRO   A C    1 ? 1 
ATOM   402  O O    . PRO   A 1 35  ? -18.369 25.463  31.759  1   66.868  ? 47  PRO   A O    1 ? 1 
ATOM   403  C CB   . PRO   A 1 35  ? -15.72  26.494  30.517  1   74.014  ? 47  PRO   A CB   1 ? 1 
ATOM   404  C CG   . PRO   A 1 35  ? -14.478 26.033  31.248  1   67.525  ? 47  PRO   A CG   1 ? 1 
ATOM   405  C CD   . PRO   A 1 35  ? -14.819 25.973  32.703  1   69.026  ? 47  PRO   A CD   1 ? 1 
ATOM   406  H HA   . PRO   A 1 35  ? -16.64  28.106  31.448  1   76.636  ? 47  PRO   A HA   1 c 1 
ATOM   407  H HB2  . PRO   A 1 35  ? -16.157 25.736  30.086  1   71.305  ? 47  PRO   A HB2  1 c 1 
ATOM   408  H HB3  . PRO   A 1 35  ? -15.486 27.139  29.822  1   73.847  ? 47  PRO   A HB3  1 c 1 
ATOM   409  H HG2  . PRO   A 1 35  ? -14.202 25.15   30.93   1   66.66   ? 47  PRO   A HG2  1 c 1 
ATOM   410  H HG3  . PRO   A 1 35  ? -13.742 26.659  31.1    1   69.567  ? 47  PRO   A HG3  1 c 1 
ATOM   411  H HD2  . PRO   A 1 35  ? -14.959 25.052  32.995  1   66.341  ? 47  PRO   A HD2  1 c 1 
ATOM   412  H HD3  . PRO   A 1 35  ? -14.112 26.376  33.242  1   68.308  ? 47  PRO   A HD3  1 c 1 
ATOM   413  N N    . MET   A 1 36  ? -18.928 27.446  30.757  1   85.256  ? 48  MET   A N    1 ? 1 
ATOM   414  C CA   . MET   A 1 36  ? -20.268 27.07   30.308  1   88.13   ? 48  MET   A CA   1 ? 1 
ATOM   415  C C    . MET   A 1 36  ? -20.183 26.43   28.921  1   84.694  ? 48  MET   A C    1 ? 1 
ATOM   416  O O    . MET   A 1 36  ? -19.219 26.683  28.19   1   82.436  ? 48  MET   A O    1 ? 1 
ATOM   417  C CB   . MET   A 1 36  ? -21.169 28.308  30.169  1   93.939  ? 48  MET   A CB   1 ? 1 
ATOM   418  C CG   . MET   A 1 36  ? -21.299 29.19   31.406  1   95.581  ? 48  MET   A CG   1 ? 1 
ATOM   419  S SD   . MET   A 1 36  ? -22.415 28.429  32.593  1   94.915  ? 48  MET   A SD   1 ? 1 
ATOM   420  C CE   . MET   A 1 36  ? -21.547 27.428  33.811  1   87.205  ? 48  MET   A CE   1 ? 1 
ATOM   421  H H    . MET   A 1 36  ? -18.657 28.307  30.618  1   86.376  ? 48  MET   A H    1 c 1 
ATOM   422  H HA   . MET   A 1 36  ? -20.662 26.428  30.952  1   86.464  ? 48  MET   A HA   1 c 1 
ATOM   423  H HB2  . MET   A 1 36  ? -20.822 28.857  29.433  1   94.765  ? 48  MET   A HB2  1 c 1 
ATOM   424  H HB3  . MET   A 1 36  ? -22.065 28.005  29.908  1   94.842  ? 48  MET   A HB3  1 c 1 
ATOM   425  H HG2  . MET   A 1 36  ? -20.423 29.315  31.821  1   94.032  ? 48  MET   A HG2  1 c 1 
ATOM   426  H HG3  . MET   A 1 36  ? -21.648 30.068  31.152  1   98.905  ? 48  MET   A HG3  1 c 1 
ATOM   427  H HE1  . MET   A 1 36  ? -22.192 27.04   34.431  1   88.574  ? 48  MET   A HE1  1 c 1 
ATOM   428  H HE2  . MET   A 1 36  ? -21.061 26.715  33.359  1   85.271  ? 48  MET   A HE2  1 c 1 
ATOM   429  H HE3  . MET   A 1 36  ? -20.919 27.989  34.303  1   88.175  ? 48  MET   A HE3  1 c 1 
ATOM   430  N N    . ILE   A 1 37  ? -21.213 25.648  28.542  1   82.918  ? 49  ILE   A N    1 ? 1 
ATOM   431  C CA   . ILE   A 1 37  ? -21.276 25.069  27.197  1   76.794  ? 49  ILE   A CA   1 ? 1 
ATOM   432  C C    . ILE   A 1 37  ? -21.28  26.213  26.184  1   78.186  ? 49  ILE   A C    1 ? 1 
ATOM   433  O O    . ILE   A 1 37  ? -22.077 27.147  26.327  1   81.509  ? 49  ILE   A O    1 ? 1 
ATOM   434  C CB   . ILE   A 1 37  ? -22.523 24.174  27.03   1   78.165  ? 49  ILE   A CB   1 ? 1 
ATOM   435  C CG1  . ILE   A 1 37  ? -22.59  22.95   28.013  1   79.615  ? 49  ILE   A CG1  1 ? 1 
ATOM   436  C CG2  . ILE   A 1 37  ? -22.73  23.756  25.571  1   76.626  ? 49  ILE   A CG2  1 ? 1 
ATOM   437  C CD1  . ILE   A 1 37  ? -21.413 22.697  28.965  1   75.194  ? 49  ILE   A CD1  1 ? 1 
ATOM   438  H H    . ILE   A 1 37  ? -21.896 25.486  29.127  1   82.79   ? 49  ILE   A H    1 c 1 
ATOM   439  H HA   . ILE   A 1 37  ? -20.478 24.524  27.055  1   74.842  ? 49  ILE   A HA   1 c 1 
ATOM   440  H HB   . ILE   A 1 37  ? -23.288 24.74   27.259  1   81.117  ? 49  ILE   A HB   1 c 1 
ATOM   441  H HG12 . ILE   A 1 37  ? -23.395 23.056  28.56   1   80.17   ? 49  ILE   A HG12 1 c 1 
ATOM   442  H HG13 . ILE   A 1 37  ? -22.716 22.141  27.476  1   77.688  ? 49  ILE   A HG13 1 c 1 
ATOM   443  H HG21 . ILE   A 1 37  ? -23.357 23.015  25.528  1   77.59   ? 49  ILE   A HG21 1 c 1 
ATOM   444  H HG22 . ILE   A 1 37  ? -21.88  23.48   25.187  1   75.323  ? 49  ILE   A HG22 1 c 1 
ATOM   445  H HG23 . ILE   A 1 37  ? -23.084 24.505  25.063  1   80.286  ? 49  ILE   A HG23 1 c 1 
ATOM   446  H HD11 . ILE   A 1 37  ? -20.573 22.72   28.469  1   73.985  ? 49  ILE   A HD11 1 c 1 
ATOM   447  H HD12 . ILE   A 1 37  ? -21.52  21.817  29.374  1   74.071  ? 49  ILE   A HD12 1 c 1 
ATOM   448  H HD13 . ILE   A 1 37  ? -21.396 23.376  29.665  1   76.234  ? 49  ILE   A HD13 1 c 1 
ATOM   449  N N    . GLY   A 1 38  ? -20.378 26.161  25.193  1   72.733  ? 50  GLY   A N    1 ? 1 
ATOM   450  C CA   . GLY   A 1 38  ? -20.334 27.189  24.16   1   77.514  ? 50  GLY   A CA   1 ? 1 
ATOM   451  C C    . GLY   A 1 38  ? -19.276 28.282  24.371  1   80.139  ? 50  GLY   A C    1 ? 1 
ATOM   452  O O    . GLY   A 1 38  ? -19.098 29.138  23.497  1   79.38   ? 50  GLY   A O    1 ? 1 
ATOM   453  H H    . GLY   A 1 38  ? -19.777 25.474  25.16   1   71.41   ? 50  GLY   A H    1 c 1 
ATOM   454  H HA2  . GLY   A 1 38  ? -20.163 26.748  23.295  1   77.44   ? 50  GLY   A HA2  1 c 1 
ATOM   455  H HA3  . GLY   A 1 38  ? -21.221 27.614  24.1    1   80.723  ? 50  GLY   A HA3  1 c 1 
ATOM   456  N N    . ASP   A 1 39  ? -18.592 28.278  25.531  1   76.703  ? 51  ASP   A N    1 ? 1 
ATOM   457  C CA   . ASP   A 1 39  ? -17.456 29.164  25.754  1   77.042  ? 51  ASP   A CA   1 ? 1 
ATOM   458  C C    . ASP   A 1 39  ? -16.327 28.807  24.777  1   77.143  ? 51  ASP   A C    1 ? 1 
ATOM   459  O O    . ASP   A 1 39  ? -16.147 27.631  24.423  1   74.638  ? 51  ASP   A O    1 ? 1 
ATOM   460  C CB   . ASP   A 1 39  ? -17.019 29.116  27.214  1   77.89   ? 51  ASP   A CB   1 ? 1 
ATOM   461  C CG   . ASP   A 1 39  ? -17.957 29.79   28.208  1   80.158  ? 51  ASP   A CG   1 ? 1 
ATOM   462  O OD1  . ASP   A 1 39  ? -18.879 30.461  27.751  1   85.303  ? 51  ASP   A OD1  1 ? 1 
ATOM   463  O OD2  . ASP   A 1 39  ? -17.763 29.646  29.436  1   80.71   ? 51  ASP   A OD2  1 ? 1 
ATOM   464  H H    . ASP   A 1 39  ? -18.843 27.709  26.2    1   75.042  ? 51  ASP   A H    1 c 1 
ATOM   465  H HA   . ASP   A 1 39  ? -17.747 30.084  25.563  1   81.305  ? 51  ASP   A HA   1 c 1 
ATOM   466  H HB2  . ASP   A 1 39  ? -16.917 28.179  27.479  1   74.121  ? 51  ASP   A HB2  1 c 1 
ATOM   467  H HB3  . ASP   A 1 39  ? -16.141 29.545  27.29   1   77.15   ? 51  ASP   A HB3  1 c 1 
ATOM   468  N N    . LYS   A 1 40  ? -15.579 29.82   24.308  1   79.155  ? 52  LYS   A N    1 ? 1 
ATOM   469  C CA   . LYS   A 1 40  ? -14.302 29.573  23.629  1   79.71   ? 52  LYS   A CA   1 ? 1 
ATOM   470  C C    . LYS   A 1 40  ? -13.245 29.3    24.703  1   79.668  ? 52  LYS   A C    1 ? 1 
ATOM   471  O O    . LYS   A 1 40  ? -13.044 30.115  25.612  1   82.428  ? 52  LYS   A O    1 ? 1 
ATOM   472  C CB   . LYS   A 1 40  ? -13.789 30.668  22.676  1   78.708  ? 52  LYS   A CB   1 ? 1 
ATOM   473  H H    . LYS   A 1 40  ? -15.867 30.681  24.413  1   82.551  ? 52  LYS   A H    1 c 1 
ATOM   474  H HA   . LYS   A 1 40  ? -14.406 28.751  23.086  1   77.365  ? 52  LYS   A HA   1 c 1 
ATOM   475  H HB2  . LYS   A 1 40  ? -12.783 30.859  22.758  0   30      ? 52  LYS   A HB2  1 c 1 
ATOM   476  H HB3  . LYS   A 1 40  ? -14.548 31.334  22.421  0   30      ? 52  LYS   A HB3  1 c 1 
ATOM   477  N N    . VAL   A 1 41  ? -12.577 28.137  24.606  1   79.027  ? 53  VAL   A N    1 ? 1 
ATOM   478  C CA   . VAL   A 1 41  ? -11.703 27.635  25.666  1   72.455  ? 53  VAL   A CA   1 ? 1 
ATOM   479  C C    . VAL   A 1 41  ? -10.274 27.482  25.158  1   71.017  ? 53  VAL   A C    1 ? 1 
ATOM   480  O O    . VAL   A 1 41  ? -10.02  26.945  24.075  1   82.017  ? 53  VAL   A O    1 ? 1 
ATOM   481  C CB   . VAL   A 1 41  ? -12.218 26.299  26.215  1   67.094  ? 53  VAL   A CB   1 ? 1 
ATOM   482  C CG1  . VAL   A 1 41  ? -11.363 25.803  27.352  1   72.18   ? 53  VAL   A CG1  1 ? 1 
ATOM   483  C CG2  . VAL   A 1 41  ? -13.657 26.417  26.67   1   65.616  ? 53  VAL   A CG2  1 ? 1 
ATOM   484  H H    . VAL   A 1 41  ? -12.668 27.637  23.846  1   77.081  ? 53  VAL   A H    1 c 1 
ATOM   485  H HA   . VAL   A 1 41  ? -11.703 28.284  26.396  1   73.615  ? 53  VAL   A HA   1 c 1 
ATOM   486  H HB   . VAL   A 1 41  ? -12.176 25.641  25.481  1   67.459  ? 53  VAL   A HB   1 c 1 
ATOM   487  H HG11 . VAL   A 1 41  ? -11.072 26.558  27.891  1   70.716  ? 53  VAL   A HG11 1 c 1 
ATOM   488  H HG12 . VAL   A 1 41  ? -10.585 25.342  26.996  1   68.552  ? 53  VAL   A HG12 1 c 1 
ATOM   489  H HG13 . VAL   A 1 41  ? -11.875 25.19   27.905  1   67.905  ? 53  VAL   A HG13 1 c 1 
ATOM   490  H HG21 . VAL   A 1 41  ? -13.927 25.596  27.115  1   64.364  ? 53  VAL   A HG21 1 c 1 
ATOM   491  H HG22 . VAL   A 1 41  ? -14.231 26.569  25.901  1   67.936  ? 53  VAL   A HG22 1 c 1 
ATOM   492  H HG23 . VAL   A 1 41  ? -13.742 27.162  27.289  1   67.684  ? 53  VAL   A HG23 1 c 1 
ATOM   493  N N    . TYR   A 1 42  ? -9.342  27.906  26.008  1   72.024  ? 54  TYR   A N    1 ? 1 
ATOM   494  C CA   . TYR   A 1 42  ? -7.935  27.967  25.667  1   75.212  ? 54  TYR   A CA   1 ? 1 
ATOM   495  C C    . TYR   A 1 42  ? -7.182  27.054  26.625  1   66.703  ? 54  TYR   A C    1 ? 1 
ATOM   496  O O    . TYR   A 1 42  ? -7.173  27.331  27.814  1   61.749  ? 54  TYR   A O    1 ? 1 
ATOM   497  C CB   . TYR   A 1 42  ? -7.456  29.419  25.814  1   82.98   ? 54  TYR   A CB   1 ? 1 
ATOM   498  C CG   . TYR   A 1 42  ? -8.027  30.435  24.839  1   89.246  ? 54  TYR   A CG   1 ? 1 
ATOM   499  C CD1  . TYR   A 1 42  ? -9.36   30.812  24.888  1   92.845  ? 54  TYR   A CD1  1 ? 1 
ATOM   500  C CD2  . TYR   A 1 42  ? -7.207  31.066  23.904  1   101.005 ? 54  TYR   A CD2  1 ? 1 
ATOM   501  C CE1  . TYR   A 1 42  ? -9.879  31.732  23.99   1   103.323 ? 54  TYR   A CE1  1 ? 1 
ATOM   502  C CE2  . TYR   A 1 42  ? -7.706  32.005  23.017  1   101.517 ? 54  TYR   A CE2  1 ? 1 
ATOM   503  C CZ   . TYR   A 1 42  ? -9.05   32.338  23.058  1   108.087 ? 54  TYR   A CZ   1 ? 1 
ATOM   504  O OH   . TYR   A 1 42  ? -9.569  33.249  22.176  1   120.277 ? 54  TYR   A OH   1 ? 1 
ATOM   505  H H    . TYR   A 1 42  ? -9.596  28.167  26.847  1   72.305  ? 54  TYR   A H    1 c 1 
ATOM   506  H HA   . TYR   A 1 42  ? -7.799  27.662  24.732  1   74.485  ? 54  TYR   A HA   1 c 1 
ATOM   507  H HB2  . TYR   A 1 42  ? -7.664  29.717  26.727  1   82.448  ? 54  TYR   A HB2  1 c 1 
ATOM   508  H HB3  . TYR   A 1 42  ? -6.476  29.425  25.729  1   83.075  ? 54  TYR   A HB3  1 c 1 
ATOM   509  H HD1  . TYR   A 1 42  ? -9.937  30.399  25.51   1   91.619  ? 54  TYR   A HD1  1 c 1 
ATOM   510  H HD2  . TYR   A 1 42  ? -6.292  30.837  23.863  1   97.657  ? 54  TYR   A HD2  1 c 1 
ATOM   511  H HE1  . TYR   A 1 42  ? -10.792 31.962  24.025  1   103.039 ? 54  TYR   A HE1  1 c 1 
ATOM   512  H HE2  . TYR   A 1 42  ? -7.14   32.401  22.377  1   106.194 ? 54  TYR   A HE2  1 c 1 
ATOM   513  H HH   . TYR   A 1 42  ? -10.275 33.645  22.581  0   30      ? 54  TYR   A HH   1 c 1 
ATOM   514  N N    . VAL   A 1 43  ? -6.57   25.978  26.107  1   63.555  ? 55  VAL   A N    1 ? 1 
ATOM   515  C CA   . VAL   A 1 43  ? -5.79   25.093  26.949  1   59.741  ? 55  VAL   A CA   1 ? 1 
ATOM   516  C C    . VAL   A 1 43  ? -4.401  24.875  26.376  1   61.016  ? 55  VAL   A C    1 ? 1 
ATOM   517  O O    . VAL   A 1 43  ? -4.148  25.26   25.246  1   65.298  ? 55  VAL   A O    1 ? 1 
ATOM   518  C CB   . VAL   A 1 43  ? -6.476  23.737  27.091  1   58.63   ? 55  VAL   A CB   1 ? 1 
ATOM   519  C CG1  . VAL   A 1 43  ? -7.912  23.877  27.592  1   55.54   ? 55  VAL   A CG1  1 ? 1 
ATOM   520  C CG2  . VAL   A 1 43  ? -6.403  22.992  25.769  1   62.797  ? 55  VAL   A CG2  1 ? 1 
ATOM   521  H H    . VAL   A 1 43  ? -6.637  25.8    25.214  1   64.081  ? 55  VAL   A H    1 c 1 
ATOM   522  H HA   . VAL   A 1 43  ? -5.704  25.496  27.832  1   60.797  ? 55  VAL   A HA   1 c 1 
ATOM   523  H HB   . VAL   A 1 43  ? -5.968  23.22   27.759  1   57.372  ? 55  VAL   A HB   1 c 1 
ATOM   524  H HG11 . VAL   A 1 43  ? -8.474  24.22   26.877  1   57.417  ? 55  VAL   A HG11 1 c 1 
ATOM   525  H HG12 . VAL   A 1 43  ? -7.935  24.492  28.344  1   57.001  ? 55  VAL   A HG12 1 c 1 
ATOM   526  H HG13 . VAL   A 1 43  ? -8.243  23.008  27.875  1   54.459  ? 55  VAL   A HG13 1 c 1 
ATOM   527  H HG21 . VAL   A 1 43  ? -6.995  22.225  25.802  1   59.828  ? 55  VAL   A HG21 1 c 1 
ATOM   528  H HG22 . VAL   A 1 43  ? -5.494  22.688  25.612  1   61.48   ? 55  VAL   A HG22 1 c 1 
ATOM   529  H HG23 . VAL   A 1 43  ? -6.678  23.579  25.045  1   63.013  ? 55  VAL   A HG23 1 c 1 
ATOM   530  N N    . HIS   A 1 44  ? -3.505  24.306  27.204  1   58.874  ? 56  HIS   A N    1 ? 1 
ATOM   531  C CA   . HIS   A 1 44  ? -2.385  23.511  26.724  1   56.168  ? 56  HIS   A CA   1 ? 1 
ATOM   532  C C    . HIS   A 1 44  ? -2.577  22.074  27.187  1   49.668  ? 56  HIS   A C    1 ? 1 
ATOM   533  O O    . HIS   A 1 44  ? -3.314  21.777  28.128  1   48.711  ? 56  HIS   A O    1 ? 1 
ATOM   534  C CB   . HIS   A 1 44  ? -1.061  24.016  27.305  1   67.821  ? 56  HIS   A CB   1 ? 1 
ATOM   535  C CG   . HIS   A 1 44  ? -0.33   25.007  26.474  1   65.531  ? 56  HIS   A CG   1 ? 1 
ATOM   536  N ND1  . HIS   A 1 44  ? 0.242   24.632  25.281  1   69.825  ? 56  HIS   A ND1  1 ? 1 
ATOM   537  C CD2  . HIS   A 1 44  ? -0.043  26.308  26.643  1   69.785  ? 56  HIS   A CD2  1 ? 1 
ATOM   538  C CE1  . HIS   A 1 44  ? 0.864   25.676  24.74   1   74.952  ? 56  HIS   A CE1  1 ? 1 
ATOM   539  N NE2  . HIS   A 1 44  ? 0.715   26.706  25.56   1   73.479  ? 56  HIS   A NE2  1 ? 1 
ATOM   540  H H    . HIS   A 1 44  ? -3.603  24.422  28.106  1   58.108  ? 56  HIS   A H    1 c 1 
ATOM   541  H HA   . HIS   A 1 44  ? -2.358  23.527  25.736  1   58.374  ? 56  HIS   A HA   1 c 1 
ATOM   542  H HB2  . HIS   A 1 44  ? -1.241  24.416  28.184  1   63.989  ? 56  HIS   A HB2  1 c 1 
ATOM   543  H HB3  . HIS   A 1 44  ? -0.474  23.244  27.459  1   63.236  ? 56  HIS   A HB3  1 c 1 
ATOM   544  H HD1  . HIS   A 1 44  ? 0.154   23.858  24.92   0   30      ? 56  HIS   A HD1  1 c 1 
ATOM   545  H HD2  . HIS   A 1 44  ? -0.283  26.847  27.371  1   70.155  ? 56  HIS   A HD2  1 c 1 
ATOM   546  H HE1  . HIS   A 1 44  ? 1.327   25.682  23.92   1   75.707  ? 56  HIS   A HE1  1 c 1 
ATOM   547  H HE2  . HIS   A 1 44  ? 1.131   27.501  25.398  0   30      ? 56  HIS   A HE2  1 c 1 
ATOM   548  N N    . TYR   A 1 45  ? -1.931  21.135  26.503  1   50.264  ? 57  TYR   A N    1 ? 1 
ATOM   549  C CA   . TYR   A 1 45  ? -2.173  19.732  26.772  1   46.021  ? 57  TYR   A CA   1 ? 1 
ATOM   550  C C    . TYR   A 1 45  ? -0.986  18.913  26.296  1   46.976  ? 57  TYR   A C    1 ? 1 
ATOM   551  O O    . TYR   A 1 45  ? -0.258  19.329  25.407  1   51.473  ? 57  TYR   A O    1 ? 1 
ATOM   552  C CB   . TYR   A 1 45  ? -3.463  19.213  26.133  1   44.452  ? 57  TYR   A CB   1 ? 1 
ATOM   553  C CG   . TYR   A 1 45  ? -3.354  18.997  24.632  1   48.597  ? 57  TYR   A CG   1 ? 1 
ATOM   554  C CD1  . TYR   A 1 45  ? -2.798  17.84   24.118  1   46.456  ? 57  TYR   A CD1  1 ? 1 
ATOM   555  C CD2  . TYR   A 1 45  ? -3.791  19.953  23.729  1   54.071  ? 57  TYR   A CD2  1 ? 1 
ATOM   556  C CE1  . TYR   A 1 45  ? -2.666  17.658  22.76   1   49.645  ? 57  TYR   A CE1  1 ? 1 
ATOM   557  C CE2  . TYR   A 1 45  ? -3.695  19.763  22.366  1   51.708  ? 57  TYR   A CE2  1 ? 1 
ATOM   558  C CZ   . TYR   A 1 45  ? -3.124  18.613  21.882  1   50.347  ? 57  TYR   A CZ   1 ? 1 
ATOM   559  O OH   . TYR   A 1 45  ? -3.023  18.342  20.559  1   54.328  ? 57  TYR   A OH   1 ? 1 
ATOM   560  H H    . TYR   A 1 45  ? -1.328  21.37   25.858  1   51.326  ? 57  TYR   A H    1 c 1 
ATOM   561  H HA   . TYR   A 1 45  ? -2.25   19.621  27.753  1   45.675  ? 57  TYR   A HA   1 c 1 
ATOM   562  H HB2  . TYR   A 1 45  ? -3.704  18.361  26.561  1   43.734  ? 57  TYR   A HB2  1 c 1 
ATOM   563  H HB3  . TYR   A 1 45  ? -4.184  19.857  26.311  1   45.059  ? 57  TYR   A HB3  1 c 1 
ATOM   564  H HD1  . TYR   A 1 45  ? -2.474  17.178  24.707  1   46.589  ? 57  TYR   A HD1  1 c 1 
ATOM   565  H HD2  . TYR   A 1 45  ? -4.182  20.749  24.055  1   52.464  ? 57  TYR   A HD2  1 c 1 
ATOM   566  H HE1  . TYR   A 1 45  ? -2.301  16.856  22.429  1   49.327  ? 57  TYR   A HE1  1 c 1 
ATOM   567  H HE2  . TYR   A 1 45  ? -4.008  20.422  21.77   1   53.676  ? 57  TYR   A HE2  1 c 1 
ATOM   568  H HH   . TYR   A 1 45  ? -2.668  17.577  20.414  0   30      ? 57  TYR   A HH   1 c 1 
ATOM   569  N N    . LYS   A 1 46  ? -0.763  17.804  26.992  1   49.006  ? 58  LYS   A N    1 ? 1 
ATOM   570  C CA   . LYS   A 1 46  ? 0.173   16.76   26.614  1   53.708  ? 58  LYS   A CA   1 ? 1 
ATOM   571  C C    . LYS   A 1 46  ? -0.694  15.496  26.612  1   55.046  ? 58  LYS   A C    1 ? 1 
ATOM   572  O O    . LYS   A 1 46  ? -1.471  15.265  27.534  1   52.288  ? 58  LYS   A O    1 ? 1 
ATOM   573  C CB   . LYS   A 1 46  ? 1.415   16.764  27.534  1   50.574  ? 58  LYS   A CB   1 ? 1 
ATOM   574  H H    . LYS   A 1 46  ? -1.23   17.69   27.77   1   47.854  ? 58  LYS   A H    1 c 1 
ATOM   575  H HA   . LYS   A 1 46  ? 0.475   16.934  25.686  1   53.774  ? 58  LYS   A HA   1 c 1 
ATOM   576  H HB2  . LYS   A 1 46  ? 2.111   16.601  27.068  0   30      ? 58  LYS   A HB2  1 c 1 
ATOM   577  H HB3  . LYS   A 1 46  ? 0.889   16.221  28.416  0   30      ? 58  LYS   A HB3  1 c 1 
ATOM   578  N N    . GLY   A 1 47  ? -0.686  14.762  25.504  1   53.915  ? 59  GLY   A N    1 ? 1 
ATOM   579  C CA   . GLY   A 1 47  ? -1.574  13.626  25.347  1   51.6    ? 59  GLY   A CA   1 ? 1 
ATOM   580  C C    . GLY   A 1 47  ? -0.841  12.428  24.768  1   51.064  ? 59  GLY   A C    1 ? 1 
ATOM   581  O O    . GLY   A 1 47  ? 0.195   12.545  24.129  1   60.831  ? 59  GLY   A O    1 ? 1 
ATOM   582  H H    . GLY   A 1 47  ? -0.111  14.97   24.826  1   55.454  ? 59  GLY   A H    1 c 1 
ATOM   583  H HA2  . GLY   A 1 47  ? -1.956  13.387  26.222  1   50.334  ? 59  GLY   A HA2  1 c 1 
ATOM   584  H HA3  . GLY   A 1 47  ? -2.317  13.878  24.75   1   50.978  ? 59  GLY   A HA3  1 c 1 
ATOM   585  N N    . LYS   A 1 48  ? -1.371  11.249  25.047  1   55.699  ? 60  LYS   A N    1 ? 1 
ATOM   586  C CA   . LYS   A 1 48  ? -0.733  10.002  24.67   1   55.925  ? 60  LYS   A CA   1 ? 1 
ATOM   587  C C    . LYS   A 1 48  ? -1.761  8.888   24.711  1   54.119  ? 60  LYS   A C    1 ? 1 
ATOM   588  O O    . LYS   A 1 48  ? -2.791  8.964   25.416  1   47.695  ? 60  LYS   A O    1 ? 1 
ATOM   589  C CB   . LYS   A 1 48  ? 0.425   9.623   25.603  1   61.603  ? 60  LYS   A CB   1 ? 1 
ATOM   590  C CG   . LYS   A 1 48  ? 0.329   10.063  27.067  1   78.386  ? 60  LYS   A CG   1 ? 1 
ATOM   591  C CD   . LYS   A 1 48  ? 1.402   9.578   28.039  1   80.632  ? 60  LYS   A CD   1 ? 1 
ATOM   592  C CE   . LYS   A 1 48  ? 1.289   8.091   28.205  1   88.672  ? 60  LYS   A CE   1 ? 1 
ATOM   593  N NZ   . LYS   A 1 48  ? 2.551   7.516   28.685  1   97.291  ? 60  LYS   A NZ   1 ? 1 
ATOM   594  H H    . LYS   A 1 48  ? -2.169  11.215  25.492  1   52.688  ? 60  LYS   A H    1 c 1 
ATOM   595  H HA   . LYS   A 1 48  ? -0.394  10.093  23.746  1   57.97   ? 60  LYS   A HA   1 c 1 
ATOM   596  H HB2  . LYS   A 1 48  ? 0.524   8.648   25.583  1   65.03   ? 60  LYS   A HB2  1 c 1 
ATOM   597  H HB3  . LYS   A 1 48  ? 1.247   10.004  25.229  1   65.431  ? 60  LYS   A HB3  1 c 1 
ATOM   598  H HG2  . LYS   A 1 48  ? 0.326   11.045  27.084  1   72.9    ? 60  LYS   A HG2  1 c 1 
ATOM   599  H HG3  . LYS   A 1 48  ? -0.545  9.773   27.408  1   72.323  ? 60  LYS   A HG3  1 c 1 
ATOM   600  H HD2  . LYS   A 1 48  ? 2.292   9.801   27.689  1   83.754  ? 60  LYS   A HD2  1 c 1 
ATOM   601  H HD3  . LYS   A 1 48  ? 1.283   10.014  28.911  1   81.421  ? 60  LYS   A HD3  1 c 1 
ATOM   602  H HE2  . LYS   A 1 48  ? 0.585   7.889   28.847  1   87.046  ? 60  LYS   A HE2  1 c 1 
ATOM   603  H HE3  . LYS   A 1 48  ? 1.057   7.669   27.36   1   87.87   ? 60  LYS   A HE3  1 c 1 
ATOM   604  H HZ1  . LYS   A 1 48  ? 2.805   7.93    29.45   1   95.458  ? 60  LYS   A HZ1  1 c 1 
ATOM   605  H HZ2  . LYS   A 1 48  ? 3.196   7.627   28.059  1   96.709  ? 60  LYS   A HZ2  1 c 1 
ATOM   606  H HZ3  . LYS   A 1 48  ? 2.443   6.632   28.847  1   96.309  ? 60  LYS   A HZ3  1 c 1 
ATOM   607  N N    . LEU   A 1 49  ? -1.465  7.86    23.928  1   54.825  ? 61  LEU   A N    1 ? 1 
ATOM   608  C CA   . LEU   A 1 49  ? -2.072  6.554   24.125  1   59.316  ? 61  LEU   A CA   1 ? 1 
ATOM   609  C C    . LEU   A 1 49  ? -1.498  5.952   25.408  1   59.519  ? 61  LEU   A C    1 ? 1 
ATOM   610  O O    . LEU   A 1 49  ? -0.342  6.2     25.731  1   60.802  ? 61  LEU   A O    1 ? 1 
ATOM   611  C CB   . LEU   A 1 49  ? -1.72   5.653   22.933  1   61.496  ? 61  LEU   A CB   1 ? 1 
ATOM   612  C CG   . LEU   A 1 49  ? -2.165  6.106   21.545  1   59.364  ? 61  LEU   A CG   1 ? 1 
ATOM   613  C CD1  . LEU   A 1 49  ? -1.813  4.961   20.583  1   67.772  ? 61  LEU   A CD1  1 ? 1 
ATOM   614  C CD2  . LEU   A 1 49  ? -3.636  6.435   21.365  1   53.763  ? 61  LEU   A CD2  1 ? 1 
ATOM   615  H H    . LEU   A 1 49  ? -0.863  7.97    23.249  1   57.324  ? 61  LEU   A H    1 c 1 
ATOM   616  H HA   . LEU   A 1 49  ? -3.055  6.653   24.202  1   57.078  ? 61  LEU   A HA   1 c 1 
ATOM   617  H HB2  . LEU   A 1 49  ? -0.741  5.544   22.917  1   62.659  ? 61  LEU   A HB2  1 c 1 
ATOM   618  H HB3  . LEU   A 1 49  ? -2.107  4.764   23.103  1   61.854  ? 61  LEU   A HB3  1 c 1 
ATOM   619  H HG   . LEU   A 1 49  ? -1.632  6.903   21.29   1   59.95   ? 61  LEU   A HG   1 c 1 
ATOM   620  H HD11 . LEU   A 1 49  ? -0.865  4.758   20.653  1   67.552  ? 61  LEU   A HD11 1 c 1 
ATOM   621  H HD12 . LEU   A 1 49  ? -2.019  5.228   19.671  1   66.709  ? 61  LEU   A HD12 1 c 1 
ATOM   622  H HD13 . LEU   A 1 49  ? -2.33   4.172   20.813  1   66.401  ? 61  LEU   A HD13 1 c 1 
ATOM   623  H HD21 . LEU   A 1 49  ? -3.844  7.259   21.835  1   53.266  ? 61  LEU   A HD21 1 c 1 
ATOM   624  H HD22 . LEU   A 1 49  ? -4.177  5.712   21.724  1   54.897  ? 61  LEU   A HD22 1 c 1 
ATOM   625  H HD23 . LEU   A 1 49  ? -3.831  6.545   20.419  1   55.867  ? 61  LEU   A HD23 1 c 1 
ATOM   626  N N    . SER   A 1 50  ? -2.259  5.092   26.092  1   67.456  ? 62  SER   A N    1 ? 1 
ATOM   627  C CA   . SER   A 1 50  ? -1.765  4.465   27.315  1   75.714  ? 62  SER   A CA   1 ? 1 
ATOM   628  C C    . SER   A 1 50  ? -0.738  3.363   27.028  1   84.362  ? 62  SER   A C    1 ? 1 
ATOM   629  O O    . SER   A 1 50  ? 0.201   3.18    27.795  1   95.867  ? 62  SER   A O    1 ? 1 
ATOM   630  C CB   . SER   A 1 50  ? -2.906  3.966   28.13   1   83.837  ? 62  SER   A CB   1 ? 1 
ATOM   631  O OG   . SER   A 1 50  ? -3.817  5.039   28.338  1   82.749  ? 62  SER   A OG   1 ? 1 
ATOM   632  H H    . SER   A 1 50  ? -3.1    4.89    25.794  1   66.305  ? 62  SER   A H    1 c 1 
ATOM   633  H HA   . SER   A 1 50  ? -1.306  5.166   27.844  1   75.825  ? 62  SER   A HA   1 c 1 
ATOM   634  H HB2  . SER   A 1 50  ? -3.353  3.237   27.66   1   83.012  ? 62  SER   A HB2  1 c 1 
ATOM   635  H HB3  . SER   A 1 50  ? -2.579  3.636   28.988  1   82.978  ? 62  SER   A HB3  1 c 1 
ATOM   636  H HG   . SER   A 1 50  ? -4.352  4.535   28.928  0   30      ? 62  SER   A HG   1 c 1 
ATOM   637  N N    . ASN   A 1 51  ? -0.865  2.659   25.896  1   86.674  ? 63  ASN   A N    1 ? 1 
ATOM   638  C CA   . ASN   A 1 51  ? 0.157   1.726   25.429  1   91.596  ? 63  ASN   A CA   1 ? 1 
ATOM   639  C C    . ASN   A 1 51  ? 1.525   2.391   25.172  1   96.627  ? 63  ASN   A C    1 ? 1 
ATOM   640  O O    . ASN   A 1 51  ? 2.483   1.66    24.925  1   82.296  ? 63  ASN   A O    1 ? 1 
ATOM   641  C CB   . ASN   A 1 51  ? -0.285  1.004   24.157  1   93.175  ? 63  ASN   A CB   1 ? 1 
ATOM   642  C CG   . ASN   A 1 51  ? -0.252  1.883   22.923  1   95.964  ? 63  ASN   A CG   1 ? 1 
ATOM   643  O OD1  . ASN   A 1 51  ? -0.194  3.112   23.007  1   101.128 ? 63  ASN   A OD1  1 ? 1 
ATOM   644  N ND2  . ASN   A 1 51  ? -0.32   1.278   21.751  1   96.474  ? 63  ASN   A ND2  1 ? 1 
ATOM   645  H H    . ASN   A 1 51  ? -1.624  2.759   25.397  1   85.655  ? 63  ASN   A H    1 c 1 
ATOM   646  H HA   . ASN   A 1 51  ? 0.279   1.041   26.125  1   93.48   ? 63  ASN   A HA   1 c 1 
ATOM   647  H HB2  . ASN   A 1 51  ? 0.299   0.233   24.011  1   96.776  ? 63  ASN   A HB2  1 c 1 
ATOM   648  H HB3  . ASN   A 1 51  ? -1.196  0.67    24.283  1   93.38   ? 63  ASN   A HB3  1 c 1 
ATOM   649  H HD21 . ASN   A 1 51  ? -0.061  1.704   21.017  1   97.361  ? 63  ASN   A HD21 1 c 1 
ATOM   650  H HD22 . ASN   A 1 51  ? -0.626  0.447   21.698  1   98.442  ? 63  ASN   A HD22 1 c 1 
ATOM   651  N N    . GLY   A 1 52  ? 1.601   3.744   25.147  1   99.706  ? 64  GLY   A N    1 ? 1 
ATOM   652  C CA   . GLY   A 1 52  ? 2.836   4.522   25.081  1   97.393  ? 64  GLY   A CA   1 ? 1 
ATOM   653  C C    . GLY   A 1 52  ? 3.477   4.588   23.682  1   110.65  ? 64  GLY   A C    1 ? 1 
ATOM   654  O O    . GLY   A 1 52  ? 4.697   4.78    23.602  1   122.092 ? 64  GLY   A O    1 ? 1 
ATOM   655  H H    . GLY   A 1 52  ? 0.816   4.211   25.149  1   95.006  ? 64  GLY   A H    1 c 1 
ATOM   656  H HA2  . GLY   A 1 52  ? 2.644   5.439   25.388  1   98.58   ? 64  GLY   A HA2  1 c 1 
ATOM   657  H HA3  . GLY   A 1 52  ? 3.485   4.13    25.712  1   102.222 ? 64  GLY   A HA3  1 c 1 
ATOM   658  N N    . LYS   A 1 53  ? 2.692   4.461   22.581  1   99.482  ? 65  LYS   A N    1 ? 1 
ATOM   659  C CA   . LYS   A 1 53  ? 3.265   4.376   21.226  1   96.262  ? 65  LYS   A CA   1 ? 1 
ATOM   660  C C    . LYS   A 1 53  ? 3.049   5.688   20.423  1   98.741  ? 65  LYS   A C    1 ? 1 
ATOM   661  O O    . LYS   A 1 53  ? 3.686   5.866   19.385  1   98.911  ? 65  LYS   A O    1 ? 1 
ATOM   662  C CB   . LYS   A 1 53  ? 2.884   3.065   20.495  1   79.01   ? 65  LYS   A CB   1 ? 1 
ATOM   663  H H    . LYS   A 1 53  ? 1.784   4.424   22.679  1   98.492  ? 65  LYS   A H    1 c 1 
ATOM   664  H HA   . LYS   A 1 53  ? 4.245   4.295   21.341  1   95.859  ? 65  LYS   A HA   1 c 1 
ATOM   665  H HB2  . LYS   A 1 53  ? 3.594   2.623   20.071  0   30      ? 65  LYS   A HB2  1 c 1 
ATOM   666  H HB3  . LYS   A 1 53  ? 1.848   3.17    20.4    0   30      ? 65  LYS   A HB3  1 c 1 
ATOM   667  N N    . LYS   A 1 54  ? 2.209   6.647   20.895  1   101.49  ? 66  LYS   A N    1 ? 1 
ATOM   668  C CA   . LYS   A 1 54  ? 2.104   7.991   20.305  1   90.748  ? 66  LYS   A CA   1 ? 1 
ATOM   669  C C    . LYS   A 1 54  ? 1.882   9.043   21.412  1   87.396  ? 66  LYS   A C    1 ? 1 
ATOM   670  O O    . LYS   A 1 54  ? 1.173   8.784   22.396  1   78.83   ? 66  LYS   A O    1 ? 1 
ATOM   671  C CB   . LYS   A 1 54  ? 1.054   8.125   19.182  1   75.601  ? 66  LYS   A CB   1 ? 1 
ATOM   672  H H    . LYS   A 1 54  ? 1.675   6.448   21.61   1   95.973  ? 66  LYS   A H    1 c 1 
ATOM   673  H HA   . LYS   A 1 54  ? 2.978   8.192   19.885  1   91.298  ? 66  LYS   A HA   1 c 1 
ATOM   674  H HB2  . LYS   A 1 54  ? 1.595   8.096   18.302  0   30      ? 66  LYS   A HB2  1 c 1 
ATOM   675  H HB3  . LYS   A 1 54  ? 0.258   8.02    19.591  0   30      ? 66  LYS   A HB3  1 c 1 
ATOM   676  N N    . PHE   A 1 55  ? 2.497   10.233  21.209  1   78.545  ? 67  PHE   A N    1 ? 1 
ATOM   677  C CA   . PHE   A 1 55  ? 2.399   11.424  22.059  1   74.879  ? 67  PHE   A CA   1 ? 1 
ATOM   678  C C    . PHE   A 1 55  ? 2.113   12.668  21.223  1   71.48   ? 67  PHE   A C    1 ? 1 
ATOM   679  O O    . PHE   A 1 55  ? 2.425   12.732  20.029  1   88.613  ? 67  PHE   A O    1 ? 1 
ATOM   680  C CB   . PHE   A 1 55  ? 3.678   11.811  22.795  1   68.958  ? 67  PHE   A CB   1 ? 1 
ATOM   681  C CG   . PHE   A 1 55  ? 4.225   10.551  23.425  1   73.288  ? 67  PHE   A CG   1 ? 1 
ATOM   682  C CD1  . PHE   A 1 55  ? 4.904   9.621   22.651  1   77.267  ? 67  PHE   A CD1  1 ? 1 
ATOM   683  C CD2  . PHE   A 1 55  ? 4.022   10.277  24.769  1   70.952  ? 67  PHE   A CD2  1 ? 1 
ATOM   684  C CE1  . PHE   A 1 55  ? 5.363   8.444   23.214  1   80.736  ? 67  PHE   A CE1  1 ? 1 
ATOM   685  C CE2  . PHE   A 1 55  ? 4.499   9.099   25.329  1   73.71   ? 67  PHE   A CE2  1 ? 1 
ATOM   686  C CZ   . PHE   A 1 55  ? 5.15    8.181   24.55   1   75.619  ? 67  PHE   A CZ   1 ? 1 
ATOM   687  H H    . PHE   A 1 55  ? 3.026   10.301  20.466  1   82.271  ? 67  PHE   A H    1 c 1 
ATOM   688  H HA   . PHE   A 1 55  ? 1.669   11.295  22.717  1   70.993  ? 67  PHE   A HA   1 c 1 
ATOM   689  H HB2  . PHE   A 1 55  ? 4.331   12.177  22.157  1   73.454  ? 67  PHE   A HB2  1 c 1 
ATOM   690  H HB3  . PHE   A 1 55  ? 3.472   12.473  23.49   1   70.187  ? 67  PHE   A HB3  1 c 1 
ATOM   691  H HD1  . PHE   A 1 55  ? 5.034   9.784   21.731  1   78.665  ? 67  PHE   A HD1  1 c 1 
ATOM   692  H HD2  . PHE   A 1 55  ? 3.555   10.896  25.306  1   69.882  ? 67  PHE   A HD2  1 c 1 
ATOM   693  H HE1  . PHE   A 1 55  ? 5.828   7.82    22.681  1   81.533  ? 67  PHE   A HE1  1 c 1 
ATOM   694  H HE2  . PHE   A 1 55  ? 4.356   8.923   26.246  1   72.528  ? 67  PHE   A HE2  1 c 1 
ATOM   695  H HZ   . PHE   A 1 55  ? 5.49    7.39    24.935  1   78.044  ? 67  PHE   A HZ   1 c 1 
ATOM   696  N N    . ASP   A 1 56  ? 1.521   13.668  21.861  1   64.8    ? 68  ASP   A N    1 ? 1 
ATOM   697  C CA   . ASP   A 1 56  ? 0.972   14.797  21.126  1   68.105  ? 68  ASP   A CA   1 ? 1 
ATOM   698  C C    . ASP   A 1 56  ? 0.805   15.965  22.08   1   59.624  ? 68  ASP   A C    1 ? 1 
ATOM   699  O O    . ASP   A 1 56  ? 0.138   15.811  23.066  1   56.042  ? 68  ASP   A O    1 ? 1 
ATOM   700  C CB   . ASP   A 1 56  ? -0.38   14.494  20.477  1   62.786  ? 68  ASP   A CB   1 ? 1 
ATOM   701  C CG   . ASP   A 1 56  ? -0.93   15.661  19.654  1   68.753  ? 68  ASP   A CG   1 ? 1 
ATOM   702  O OD1  . ASP   A 1 56  ? -0.186  16.157  18.742  1   69.648  ? 68  ASP   A OD1  1 ? 1 
ATOM   703  O OD2  . ASP   A 1 56  ? -2.045  16.137  19.985  1   64.923  ? 68  ASP   A OD2  1 ? 1 
ATOM   704  H H    . ASP   A 1 56  ? 1.455   13.652  22.773  1   65.392  ? 68  ASP   A H    1 c 1 
ATOM   705  H HA   . ASP   A 1 56  ? 1.608   15.052  20.421  1   67.648  ? 68  ASP   A HA   1 c 1 
ATOM   706  H HB2  . ASP   A 1 56  ? -0.285  13.716  19.888  1   65.504  ? 68  ASP   A HB2  1 c 1 
ATOM   707  H HB3  . ASP   A 1 56  ? -1.029  14.271  21.177  1   62.607  ? 68  ASP   A HB3  1 c 1 
ATOM   708  N N    . SER   A 1 57  ? 1.429   17.102  21.795  1   66.231  ? 69  SER   A N    1 ? 1 
ATOM   709  C CA   . SER   A 1 57  ? 1.341   18.238  22.705  1   68.36   ? 69  SER   A CA   1 ? 1 
ATOM   710  C C    . SER   A 1 57  ? 0.954   19.511  21.95   1   69.916  ? 69  SER   A C    1 ? 1 
ATOM   711  O O    . SER   A 1 57  ? 1.35    19.718  20.809  1   78.289  ? 69  SER   A O    1 ? 1 
ATOM   712  C CB   . SER   A 1 57  ? 2.625   18.458  23.462  1   67.648  ? 69  SER   A CB   1 ? 1 
ATOM   713  O OG   . SER   A 1 57  ? 2.618   19.74   24.084  1   69.822  ? 69  SER   A OG   1 ? 1 
ATOM   714  H H    . SER   A 1 57  ? 1.916   17.181  21.025  1   67.7    ? 69  SER   A H    1 c 1 
ATOM   715  H HA   . SER   A 1 57  ? 0.627   18.048  23.363  1   65.035  ? 69  SER   A HA   1 c 1 
ATOM   716  H HB2  . SER   A 1 57  ? 2.724   17.765  24.142  1   67.384  ? 69  SER   A HB2  1 c 1 
ATOM   717  H HB3  . SER   A 1 57  ? 3.38    18.397  22.847  1   70.737  ? 69  SER   A HB3  1 c 1 
ATOM   718  H HG   . SER   A 1 57  ? 3.255   19.734  24.666  0   30      ? 69  SER   A HG   1 c 1 
ATOM   719  N N    . SER   A 1 58  ? 0.204   20.372  22.638  1   67.102  ? 70  SER   A N    1 ? 1 
ATOM   720  C CA   . SER   A 1 58  ? -0.055  21.735  22.214  1   70.096  ? 70  SER   A CA   1 ? 1 
ATOM   721  C C    . SER   A 1 58  ? 1.269   22.461  21.958  1   79.124  ? 70  SER   A C    1 ? 1 
ATOM   722  O O    . SER   A 1 58  ? 1.323   23.294  21.069  1   84.617  ? 70  SER   A O    1 ? 1 
ATOM   723  C CB   . SER   A 1 58  ? -0.885  22.449  23.268  1   64.847  ? 70  SER   A CB   1 ? 1 
ATOM   724  O OG   . SER   A 1 58  ? -0.328  22.243  24.568  1   60.41   ? 70  SER   A OG   1 ? 1 
ATOM   725  H H    . SER   A 1 58  ? -0.171  20.089  23.422  1   65.769  ? 70  SER   A H    1 c 1 
ATOM   726  H HA   . SER   A 1 58  ? -0.569  21.708  21.367  1   70.513  ? 70  SER   A HA   1 c 1 
ATOM   727  H HB2  . SER   A 1 58  ? -0.908  23.404  23.07   1   66.812  ? 70  SER   A HB2  1 c 1 
ATOM   728  H HB3  . SER   A 1 58  ? -1.799  22.108  23.247  1   63.068  ? 70  SER   A HB3  1 c 1 
ATOM   729  H HG   . SER   A 1 58  ? -0.863  22.639  25.136  0   30      ? 70  SER   A HG   1 c 1 
ATOM   730  N N    . HIS   A 1 59  ? 2.333   22.108  22.697  1   75.509  ? 71  HIS   A N    1 ? 1 
ATOM   731  C CA   . HIS   A 1 59  ? 3.596   22.828  22.665  1   83.775  ? 71  HIS   A CA   1 ? 1 
ATOM   732  C C    . HIS   A 1 59  ? 4.391   22.597  21.379  1   90.324  ? 71  HIS   A C    1 ? 1 
ATOM   733  O O    . HIS   A 1 59  ? 5.188   23.457  20.985  1   82.219  ? 71  HIS   A O    1 ? 1 
ATOM   734  C CB   . HIS   A 1 59  ? 4.417   22.47   23.905  1   82.997  ? 71  HIS   A CB   1 ? 1 
ATOM   735  C CG   . HIS   A 1 59  ? 3.807   22.959  25.182  1   83.075  ? 71  HIS   A CG   1 ? 1 
ATOM   736  N ND1  . HIS   A 1 59  ? 3.121   22.122  26.048  1   77.345  ? 71  HIS   A ND1  1 ? 1 
ATOM   737  C CD2  . HIS   A 1 59  ? 3.844   24.174  25.766  1   85.709  ? 71  HIS   A CD2  1 ? 1 
ATOM   738  C CE1  . HIS   A 1 59  ? 2.715   22.801  27.107  1   79.744  ? 71  HIS   A CE1  1 ? 1 
ATOM   739  N NE2  . HIS   A 1 59  ? 3.153   24.053  26.956  1   91.969  ? 71  HIS   A NE2  1 ? 1 
ATOM   740  H H    . HIS   A 1 59  ? 2.26    21.393  23.261  1   75.381  ? 71  HIS   A H    1 c 1 
ATOM   741  H HA   . HIS   A 1 59  ? 3.38    23.792  22.718  1   84.706  ? 71  HIS   A HA   1 c 1 
ATOM   742  H HB2  . HIS   A 1 59  ? 4.515   21.494  23.949  1   82.082  ? 71  HIS   A HB2  1 c 1 
ATOM   743  H HB3  . HIS   A 1 59  ? 5.315   22.858  23.811  1   86.471  ? 71  HIS   A HB3  1 c 1 
ATOM   744  H HD1  . HIS   A 1 59  ? 3.109   21.204  25.952  0   30      ? 71  HIS   A HD1  1 c 1 
ATOM   745  H HD2  . HIS   A 1 59  ? 4.244   24.952  25.432  1   90.145  ? 71  HIS   A HD2  1 c 1 
ATOM   746  H HE1  . HIS   A 1 59  ? 2.218   22.467  27.834  1   78.95   ? 71  HIS   A HE1  1 c 1 
ATOM   747  H HE2  . HIS   A 1 59  ? 2.891   24.719  27.39   0   30      ? 71  HIS   A HE2  1 c 1 
ATOM   748  N N    . ASP   A 1 60  ? 4.162   21.446  20.731  1   94.684  ? 72  ASP   A N    1 ? 1 
ATOM   749  C CA   . ASP   A 1 60  ? 4.747   21.13   19.427  1   104.31  ? 72  ASP   A CA   1 ? 1 
ATOM   750  C C    . ASP   A 1 60  ? 4.186   22.032  18.314  1   109.948 ? 72  ASP   A C    1 ? 1 
ATOM   751  O O    . ASP   A 1 60  ? 4.732   22.091  17.213  1   108.585 ? 72  ASP   A O    1 ? 1 
ATOM   752  C CB   . ASP   A 1 60  ? 4.484   19.676  19.045  1   103.999 ? 72  ASP   A CB   1 ? 1 
ATOM   753  C CG   . ASP   A 1 60  ? 4.828   18.632  20.095  1   97.041  ? 72  ASP   A CG   1 ? 1 
ATOM   754  O OD1  . ASP   A 1 60  ? 5.903   18.797  20.716  1   106.385 ? 72  ASP   A OD1  1 ? 1 
ATOM   755  O OD2  . ASP   A 1 60  ? 4.034   17.669  20.246  1   80.255  ? 72  ASP   A OD2  1 ? 1 
ATOM   756  H H    . ASP   A 1 60  ? 3.615   20.826  21.12   1   91.744  ? 72  ASP   A H    1 c 1 
ATOM   757  H HA   . ASP   A 1 60  ? 5.72    21.264  19.483  1   106.155 ? 72  ASP   A HA   1 c 1 
ATOM   758  H HB2  . ASP   A 1 60  ? 3.533   19.58   18.826  1   100.558 ? 72  ASP   A HB2  1 c 1 
ATOM   759  H HB3  . ASP   A 1 60  ? 4.998   19.471  18.237  1   104.896 ? 72  ASP   A HB3  1 c 1 
ATOM   760  N N    . ARG   A 1 61  ? 3.055   22.7    18.571  1   113.811 ? 73  ARG   A N    1 ? 1 
ATOM   761  C CA   . ARG   A 1 61  ? 2.544   23.744  17.693  1   119.124 ? 73  ARG   A CA   1 ? 1 
ATOM   762  C C    . ARG   A 1 61  ? 2.96    25.138  18.214  1   125.65  ? 73  ARG   A C    1 ? 1 
ATOM   763  O O    . ARG   A 1 61  ? 2.504   26.152  17.688  1   134.843 ? 73  ARG   A O    1 ? 1 
ATOM   764  C CB   . ARG   A 1 61  ? 1.034   23.471  17.548  1   107.537 ? 73  ARG   A CB   1 ? 1 
ATOM   765  H H    . ARG   A 1 61  ? 2.575   22.488  19.319  1   109.72  ? 73  ARG   A H    1 c 1 
ATOM   766  H HA   . ARG   A 1 61  ? 2.951   23.621  16.798  1   119.979 ? 73  ARG   A HA   1 c 1 
ATOM   767  H HB2  . ARG   A 1 61  ? 0.778   23.755  18.678  0   30      ? 73  ARG   A HB2  1 c 1 
ATOM   768  H HB3  . ARG   A 1 61  ? 0.734   23.55   16.831  0   30      ? 73  ARG   A HB3  1 c 1 
ATOM   769  N N    . ASN   A 1 62  ? 3.844   25.202  19.232  1   118.418 ? 74  ASN   A N    1 ? 1 
ATOM   770  C CA   . ASN   A 1 62  ? 4.121   26.405  20.012  1   111.304 ? 74  ASN   A CA   1 ? 1 
ATOM   771  C C    . ASN   A 1 62  ? 2.934   27.383  19.945  1   107.995 ? 74  ASN   A C    1 ? 1 
ATOM   772  O O    . ASN   A 1 62  ? 3.079   28.509  19.485  1   104.858 ? 74  ASN   A O    1 ? 1 
ATOM   773  C CB   . ASN   A 1 62  ? 5.488   26.968  19.621  1   113.551 ? 74  ASN   A CB   1 ? 1 
ATOM   774  H H    . ASN   A 1 62  ? 4.314   24.447  19.441  1   116.566 ? 74  ASN   A H    1 c 1 
ATOM   775  H HA   . ASN   A 1 62  ? 4.198   26.123  20.951  1   109.565 ? 74  ASN   A HA   1 c 1 
ATOM   776  H HB2  . ASN   A 1 62  ? 6.111   26.48   19.854  0   30      ? 74  ASN   A HB2  1 c 1 
ATOM   777  H HB3  . ASN   A 1 62  ? 5.16    27.398  18.563  0   30      ? 74  ASN   A HB3  1 c 1 
ATOM   778  N N    . GLU   A 1 63  ? 1.741   26.963  20.407  1   102.091 ? 75  GLU   A N    1 ? 1 
ATOM   779  C CA   . GLU   A 1 63  ? 0.598   27.863  20.578  1   103.556 ? 75  GLU   A CA   1 ? 1 
ATOM   780  C C    . GLU   A 1 63  ? -0.504  27.151  21.372  1   96.278  ? 75  GLU   A C    1 ? 1 
ATOM   781  O O    . GLU   A 1 63  ? -0.676  25.943  21.21   1   95.168  ? 75  GLU   A O    1 ? 1 
ATOM   782  C CB   . GLU   A 1 63  ? 0.065   28.393  19.24   1   102.824 ? 75  GLU   A CB   1 ? 1 
ATOM   783  H H    . GLU   A 1 63  ? 1.639   26.081  20.624  1   100.144 ? 75  GLU   A H    1 c 1 
ATOM   784  H HA   . GLU   A 1 63  ? 0.907   28.642  21.105  1   103.858 ? 75  GLU   A HA   1 c 1 
ATOM   785  H HB2  . GLU   A 1 63  ? 0.747   28.496  18.5    0   30      ? 75  GLU   A HB2  1 c 1 
ATOM   786  H HB3  . GLU   A 1 63  ? -0.98   28.29   19.15   0   30      ? 75  GLU   A HB3  1 c 1 
ATOM   787  N N    . PRO   A 1 64  ? -1.285  27.845  22.249  1   93.403  ? 76  PRO   A N    1 ? 1 
ATOM   788  C CA   . PRO   A 1 64  ? -2.418  27.215  22.914  1   82.903  ? 76  PRO   A CA   1 ? 1 
ATOM   789  C C    . PRO   A 1 64  ? -3.329  26.516  21.918  1   82.238  ? 76  PRO   A C    1 ? 1 
ATOM   790  O O    . PRO   A 1 64  ? -3.313  26.826  20.733  1   83.365  ? 76  PRO   A O    1 ? 1 
ATOM   791  C CB   . PRO   A 1 64  ? -3.154  28.36   23.61   1   82.478  ? 76  PRO   A CB   1 ? 1 
ATOM   792  C CG   . PRO   A 1 64  ? -2.048  29.364  23.869  1   87.547  ? 76  PRO   A CG   1 ? 1 
ATOM   793  C CD   . PRO   A 1 64  ? -1.13   29.249  22.657  1   94.513  ? 76  PRO   A CD   1 ? 1 
ATOM   794  H HA   . PRO   A 1 64  ? -2.094  26.571  23.578  1   81.723  ? 76  PRO   A HA   1 c 1 
ATOM   795  H HB2  . PRO   A 1 64  ? -3.844  28.739  23.032  1   84.406  ? 76  PRO   A HB2  1 c 1 
ATOM   796  H HB3  . PRO   A 1 64  ? -3.56   28.06   24.447  1   80.886  ? 76  PRO   A HB3  1 c 1 
ATOM   797  H HG2  . PRO   A 1 64  ? -2.409  30.27   23.944  1   90.47   ? 76  PRO   A HG2  1 c 1 
ATOM   798  H HG3  . PRO   A 1 64  ? -1.564  29.146  24.69   1   87.144  ? 76  PRO   A HG3  1 c 1 
ATOM   799  H HD2  . PRO   A 1 64  ? -1.409  29.852  21.94   1   96.632  ? 76  PRO   A HD2  1 c 1 
ATOM   800  H HD3  . PRO   A 1 64  ? -0.202  29.44   22.897  1   95.627  ? 76  PRO   A HD3  1 c 1 
ATOM   801  N N    . PHE   A 1 65  ? -4.079  25.541  22.428  1   85.516  ? 77  PHE   A N    1 ? 1 
ATOM   802  C CA   . PHE   A 1 65  ? -5.127  24.87   21.684  1   79.357  ? 77  PHE   A CA   1 ? 1 
ATOM   803  C C    . PHE   A 1 65  ? -6.461  25.488  22.092  1   80.247  ? 77  PHE   A C    1 ? 1 
ATOM   804  O O    . PHE   A 1 65  ? -6.755  25.614  23.285  1   70.085  ? 77  PHE   A O    1 ? 1 
ATOM   805  C CB   . PHE   A 1 65  ? -5.042  23.366  21.944  1   73.284  ? 77  PHE   A CB   1 ? 1 
ATOM   806  C CG   . PHE   A 1 65  ? -6.1    22.545  21.227  1   68.326  ? 77  PHE   A CG   1 ? 1 
ATOM   807  C CD1  . PHE   A 1 65  ? -5.935  22.176  19.899  1   73.258  ? 77  PHE   A CD1  1 ? 1 
ATOM   808  C CD2  . PHE   A 1 65  ? -7.243  22.129  21.896  1   62.885  ? 77  PHE   A CD2  1 ? 1 
ATOM   809  C CE1  . PHE   A 1 65  ? -6.904  21.429  19.247  1   73.575  ? 77  PHE   A CE1  1 ? 1 
ATOM   810  C CE2  . PHE   A 1 65  ? -8.206  21.382  21.246  1   64.949  ? 77  PHE   A CE2  1 ? 1 
ATOM   811  C CZ   . PHE   A 1 65  ? -8.033  21.029  19.923  1   69.751  ? 77  PHE   A CZ   1 ? 1 
ATOM   812  H H    . PHE   A 1 65  ? -3.929  25.28   23.291  1   80.833  ? 77  PHE   A H    1 c 1 
ATOM   813  H HA   . PHE   A 1 65  ? -4.981  25.03   20.714  1   81.95   ? 77  PHE   A HA   1 c 1 
ATOM   814  H HB2  . PHE   A 1 65  ? -4.154  23.052  21.664  1   73.387  ? 77  PHE   A HB2  1 c 1 
ATOM   815  H HB3  . PHE   A 1 65  ? -5.123  23.213  22.911  1   71.129  ? 77  PHE   A HB3  1 c 1 
ATOM   816  H HD1  . PHE   A 1 65  ? -5.163  22.451  19.432  1   74.38   ? 77  PHE   A HD1  1 c 1 
ATOM   817  H HD2  . PHE   A 1 65  ? -7.367  22.369  22.801  1   63.444  ? 77  PHE   A HD2  1 c 1 
ATOM   818  H HE1  . PHE   A 1 65  ? -6.783  21.187  18.343  1   74.297  ? 77  PHE   A HE1  1 c 1 
ATOM   819  H HE2  . PHE   A 1 65  ? -8.981  21.109  21.71   1   63.942  ? 77  PHE   A HE2  1 c 1 
ATOM   820  H HZ   . PHE   A 1 65  ? -8.691  20.516  19.481  1   69.325  ? 77  PHE   A HZ   1 c 1 
ATOM   821  N N    . VAL   A 1 66  ? -7.227  25.857  21.058  1   82.321  ? 78  VAL   A N    1 ? 1 
ATOM   822  C CA   . VAL   A 1 66  ? -8.477  26.575  21.178  1   87.527  ? 78  VAL   A CA   1 ? 1 
ATOM   823  C C    . VAL   A 1 66  ? -9.604  25.684  20.691  1   82.722  ? 78  VAL   A C    1 ? 1 
ATOM   824  O O    . VAL   A 1 66  ? -9.428  25.012  19.688  1   91.514  ? 78  VAL   A O    1 ? 1 
ATOM   825  C CB   . VAL   A 1 66  ? -8.378  27.793  20.245  1   95.526  ? 78  VAL   A CB   1 ? 1 
ATOM   826  C CG1  . VAL   A 1 66  ? -9.495  28.799  20.531  1   100.122 ? 78  VAL   A CG1  1 ? 1 
ATOM   827  C CG2  . VAL   A 1 66  ? -6.983  28.43   20.261  1   97.028  ? 78  VAL   A CG2  1 ? 1 
ATOM   828  H H    . VAL   A 1 66  ? -6.949  25.631  20.217  1   84.32   ? 78  VAL   A H    1 c 1 
ATOM   829  H HA   . VAL   A 1 66  ? -8.626  26.857  22.099  1   85.707  ? 78  VAL   A HA   1 c 1 
ATOM   830  H HB   . VAL   A 1 66  ? -8.524  27.46   19.328  1   96.055  ? 78  VAL   A HB   1 c 1 
ATOM   831  H HG11 . VAL   A 1 66  ? -9.505  29.012  21.479  1   98.392  ? 78  VAL   A HG11 1 c 1 
ATOM   832  H HG12 . VAL   A 1 66  ? -10.351 28.416  20.277  1   98.933  ? 78  VAL   A HG12 1 c 1 
ATOM   833  H HG13 . VAL   A 1 66  ? -9.341  29.611  20.019  1   102.853 ? 78  VAL   A HG13 1 c 1 
ATOM   834  H HG21 . VAL   A 1 66  ? -7.035  29.335  19.91   1   100.534 ? 78  VAL   A HG21 1 c 1 
ATOM   835  H HG22 . VAL   A 1 66  ? -6.378  27.906  19.711  1   96.879  ? 78  VAL   A HG22 1 c 1 
ATOM   836  H HG23 . VAL   A 1 66  ? -6.649  28.458  21.174  1   95.694  ? 78  VAL   A HG23 1 c 1 
ATOM   837  N N    . PHE   A 1 67  ? -10.765 25.754  21.34   1   80.261  ? 79  PHE   A N    1 ? 1 
ATOM   838  C CA   . PHE   A 1 67  ? -11.948 25.028  20.89   1   72.926  ? 79  PHE   A CA   1 ? 1 
ATOM   839  C C    . PHE   A 1 67  ? -13.17  25.522  21.67   1   77.442  ? 79  PHE   A C    1 ? 1 
ATOM   840  O O    . PHE   A 1 67  ? -13.036 26.105  22.759  1   74.657  ? 79  PHE   A O    1 ? 1 
ATOM   841  C CB   . PHE   A 1 67  ? -11.812 23.508  21.059  1   67.344  ? 79  PHE   A CB   1 ? 1 
ATOM   842  C CG   . PHE   A 1 67  ? -11.943 22.994  22.486  1   63.944  ? 79  PHE   A CG   1 ? 1 
ATOM   843  C CD1  . PHE   A 1 67  ? -10.978 23.272  23.441  1   59.618  ? 79  PHE   A CD1  1 ? 1 
ATOM   844  C CD2  . PHE   A 1 67  ? -13.058 22.265  22.878  1   64.622  ? 79  PHE   A CD2  1 ? 1 
ATOM   845  C CE1  . PHE   A 1 67  ? -11.108 22.821  24.743  1   63.5    ? 79  PHE   A CE1  1 ? 1 
ATOM   846  C CE2  . PHE   A 1 67  ? -13.191 21.833  24.19   1   64.028  ? 79  PHE   A CE2  1 ? 1 
ATOM   847  C CZ   . PHE   A 1 67  ? -12.22  22.12   25.123  1   64.043  ? 79  PHE   A CZ   1 ? 1 
ATOM   848  H H    . PHE   A 1 67  ? -10.826 26.271  22.091  1   79.123  ? 79  PHE   A H    1 c 1 
ATOM   849  H HA   . PHE   A 1 67  ? -12.088 25.227  19.926  1   76.863  ? 79  PHE   A HA   1 c 1 
ATOM   850  H HB2  . PHE   A 1 67  ? -12.499 23.075  20.505  1   68.315  ? 79  PHE   A HB2  1 c 1 
ATOM   851  H HB3  . PHE   A 1 67  ? -10.938 23.233  20.706  1   67.552  ? 79  PHE   A HB3  1 c 1 
ATOM   852  H HD1  . PHE   A 1 67  ? -10.214 23.769  23.195  1   62.86   ? 79  PHE   A HD1  1 c 1 
ATOM   853  H HD2  . PHE   A 1 67  ? -13.738 22.079  22.251  1   65.661  ? 79  PHE   A HD2  1 c 1 
ATOM   854  H HE1  . PHE   A 1 67  ? -10.438 23.02   25.378  1   61.796  ? 79  PHE   A HE1  1 c 1 
ATOM   855  H HE2  . PHE   A 1 67  ? -13.952 21.334  24.443  1   63.375  ? 79  PHE   A HE2  1 c 1 
ATOM   856  H HZ   . PHE   A 1 67  ? -12.303 21.803  26.009  1   61.968  ? 79  PHE   A HZ   1 c 1 
ATOM   857  N N    . SER   A 1 68  ? -14.358 25.251  21.118  1   74.413  ? 80  SER   A N    1 ? 1 
ATOM   858  C CA   . SER   A 1 68  ? -15.592 25.723  21.72   1   75.373  ? 80  SER   A CA   1 ? 1 
ATOM   859  C C    . SER   A 1 68  ? -16.221 24.553  22.459  1   71.623  ? 80  SER   A C    1 ? 1 
ATOM   860  O O    . SER   A 1 68  ? -16.355 23.456  21.919  1   76.146  ? 80  SER   A O    1 ? 1 
ATOM   861  C CB   . SER   A 1 68  ? -16.539 26.317  20.7    1   85.278  ? 80  SER   A CB   1 ? 1 
ATOM   862  O OG   . SER   A 1 68  ? -16.196 27.649  20.339  1   92.817  ? 80  SER   A OG   1 ? 1 
ATOM   863  H H    . SER   A 1 68  ? -14.398 24.761  20.348  1   75.635  ? 80  SER   A H    1 c 1 
ATOM   864  H HA   . SER   A 1 68  ? -15.367 26.425  22.379  1   76.715  ? 80  SER   A HA   1 c 1 
ATOM   865  H HB2  . SER   A 1 68  ? -16.535 25.758  19.9    1   84.921  ? 80  SER   A HB2  1 c 1 
ATOM   866  H HB3  . SER   A 1 68  ? -17.445 26.308  21.064  1   85.373  ? 80  SER   A HB3  1 c 1 
ATOM   867  H HG   . SER   A 1 68  ? -16.791 27.759  19.526  0   30      ? 80  SER   A HG   1 c 1 
ATOM   868  N N    . LEU   A 1 69  ? -16.542 24.791  23.726  1   75.31   ? 81  LEU   A N    1 ? 1 
ATOM   869  C CA   . LEU   A 1 69  ? -16.865 23.706  24.632  1   69.958  ? 81  LEU   A CA   1 ? 1 
ATOM   870  C C    . LEU   A 1 69  ? -18.27  23.186  24.384  1   69.632  ? 81  LEU   A C    1 ? 1 
ATOM   871  O O    . LEU   A 1 69  ? -19.204 23.959  24.302  1   68.284  ? 81  LEU   A O    1 ? 1 
ATOM   872  C CB   . LEU   A 1 69  ? -16.749 24.207  26.051  1   69.395  ? 81  LEU   A CB   1 ? 1 
ATOM   873  C CG   . LEU   A 1 69  ? -16.991 23.141  27.118  1   73.203  ? 81  LEU   A CG   1 ? 1 
ATOM   874  C CD1  . LEU   A 1 69  ? -15.745 22.266  27.357  1   68.196  ? 81  LEU   A CD1  1 ? 1 
ATOM   875  C CD2  . LEU   A 1 69  ? -17.436 23.874  28.374  1   74.511  ? 81  LEU   A CD2  1 ? 1 
ATOM   876  H H    . LEU   A 1 69  ? -16.57  25.65   24.035  1   75.141  ? 81  LEU   A H    1 c 1 
ATOM   877  H HA   . LEU   A 1 69  ? -16.214 22.972  24.49   1   68.13   ? 81  LEU   A HA   1 c 1 
ATOM   878  H HB2  . LEU   A 1 69  ? -15.845 24.577  26.176  1   70.225  ? 81  LEU   A HB2  1 c 1 
ATOM   879  H HB3  . LEU   A 1 69  ? -17.402 24.933  26.176  1   73.063  ? 81  LEU   A HB3  1 c 1 
ATOM   880  H HG   . LEU   A 1 69  ? -17.733 22.555  26.821  1   71.902  ? 81  LEU   A HG   1 c 1 
ATOM   881  H HD11 . LEU   A 1 69  ? -15.555 21.747  26.557  1   68.197  ? 81  LEU   A HD11 1 c 1 
ATOM   882  H HD12 . LEU   A 1 69  ? -15.908 21.664  28.102  1   67.454  ? 81  LEU   A HD12 1 c 1 
ATOM   883  H HD13 . LEU   A 1 69  ? -14.983 22.834  27.562  1   68.638  ? 81  LEU   A HD13 1 c 1 
ATOM   884  H HD21 . LEU   A 1 69  ? -18.383 24.083  28.31   1   76.246  ? 81  LEU   A HD21 1 c 1 
ATOM   885  H HD22 . LEU   A 1 69  ? -16.929 24.697  28.466  1   75.135  ? 81  LEU   A HD22 1 c 1 
ATOM   886  H HD23 . LEU   A 1 69  ? -17.282 23.311  29.152  1   72.567  ? 81  LEU   A HD23 1 c 1 
ATOM   887  N N    . GLY   A 1 70  ? -18.379 21.864  24.266  1   74.86   ? 82  GLY   A N    1 ? 1 
ATOM   888  C CA   . GLY   A 1 70  ? -19.644 21.187  24.033  1   79.057  ? 82  GLY   A CA   1 ? 1 
ATOM   889  C C    . GLY   A 1 70  ? -20.185 21.399  22.616  1   86.815  ? 82  GLY   A C    1 ? 1 
ATOM   890  O O    . GLY   A 1 70  ? -21.315 21.004  22.347  1   91.511  ? 82  GLY   A O    1 ? 1 
ATOM   891  H H    . GLY   A 1 70  ? -17.623 21.356  24.336  1   71.456  ? 82  GLY   A H    1 c 1 
ATOM   892  H HA2  . GLY   A 1 70  ? -19.525 20.223  24.193  1   77.425  ? 82  GLY   A HA2  1 c 1 
ATOM   893  H HA3  . GLY   A 1 70  ? -20.305 21.519  24.684  1   80.146  ? 82  GLY   A HA3  1 c 1 
ATOM   894  N N    . LYS   A 1 71  ? -19.391 22.009  21.716  1   87.277  ? 83  LYS   A N    1 ? 1 
ATOM   895  C CA   . LYS   A 1 71  ? -19.812 22.208  20.338  1   87.083  ? 83  LYS   A CA   1 ? 1 
ATOM   896  C C    . LYS   A 1 71  ? -19.135 21.137  19.469  1   90.663  ? 83  LYS   A C    1 ? 1 
ATOM   897  O O    . LYS   A 1 71  ? -18.906 21.383  18.287  1   92.584  ? 83  LYS   A O    1 ? 1 
ATOM   898  C CB   . LYS   A 1 71  ? -19.676 23.677  19.894  1   89.258  ? 83  LYS   A CB   1 ? 1 
ATOM   899  H H    . LYS   A 1 71  ? -18.558 22.291  21.963  1   84.97   ? 83  LYS   A H    1 c 1 
ATOM   900  H HA   . LYS   A 1 71  ? -20.784 22.024  20.3    1   90.153  ? 83  LYS   A HA   1 c 1 
ATOM   901  H HB2  . LYS   A 1 71  ? -18.518 23.628  19.746  0   30      ? 83  LYS   A HB2  1 c 1 
ATOM   902  H HB3  . LYS   A 1 71  ? -20.351 23.924  19.648  0   30      ? 83  LYS   A HB3  1 c 1 
ATOM   903  N N    . GLY   A 1 72  ? -18.801 19.967  20.075  1   85.993  ? 84  GLY   A N    1 ? 1 
ATOM   904  C CA   . GLY   A 1 72  ? -18.482 18.714  19.388  1   82.954  ? 84  GLY   A CA   1 ? 1 
ATOM   905  C C    . GLY   A 1 72  ? -17.11  18.625  18.686  1   78.389  ? 84  GLY   A C    1 ? 1 
ATOM   906  O O    . GLY   A 1 72  ? -16.9   17.706  17.898  1   68.025  ? 84  GLY   A O    1 ? 1 
ATOM   907  H H    . GLY   A 1 72  ? -18.761 19.96   20.987  1   84.109  ? 84  GLY   A H    1 c 1 
ATOM   908  H HA2  . GLY   A 1 72  ? -18.54  17.984  20.048  1   80.753  ? 84  GLY   A HA2  1 c 1 
ATOM   909  H HA3  . GLY   A 1 72  ? -19.185 18.55   18.717  1   84.943  ? 84  GLY   A HA3  1 c 1 
ATOM   910  N N    . GLN   A 1 73  ? -16.148 19.514  18.975  1   72.89   ? 85  GLN   A N    1 ? 1 
ATOM   911  C CA   . GLN   A 1 73  ? -14.967 19.662  18.125  1   76.066  ? 85  GLN   A CA   1 ? 1 
ATOM   912  C C    . GLN   A 1 73  ? -13.768 18.877  18.665  1   69.786  ? 85  GLN   A C    1 ? 1 
ATOM   913  O O    . GLN   A 1 73  ? -12.728 18.727  18.001  1   69.504  ? 85  GLN   A O    1 ? 1 
ATOM   914  C CB   . GLN   A 1 73  ? -14.527 21.119  18.047  1   79.826  ? 85  GLN   A CB   1 ? 1 
ATOM   915  C CG   . GLN   A 1 73  ? -15.613 22.084  17.597  1   85.358  ? 85  GLN   A CG   1 ? 1 
ATOM   916  C CD   . GLN   A 1 73  ? -15.219 23.521  17.852  1   85.154  ? 85  GLN   A CD   1 ? 1 
ATOM   917  O OE1  . GLN   A 1 73  ? -14.393 23.802  18.726  1   84.424  ? 85  GLN   A OE1  1 ? 1 
ATOM   918  N NE2  . GLN   A 1 73  ? -15.814 24.45   17.115  1   86.662  ? 85  GLN   A NE2  1 ? 1 
ATOM   919  H H    . GLN   A 1 73  ? -16.233 20.048  19.712  1   73.944  ? 85  GLN   A H    1 c 1 
ATOM   920  H HA   . GLN   A 1 73  ? -15.184 19.337  17.214  1   77.014  ? 85  GLN   A HA   1 c 1 
ATOM   921  H HB2  . GLN   A 1 73  ? -14.208 21.392  18.933  1   78.074  ? 85  GLN   A HB2  1 c 1 
ATOM   922  H HB3  . GLN   A 1 73  ? -13.771 21.184  17.428  1   80.462  ? 85  GLN   A HB3  1 c 1 
ATOM   923  H HG2  . GLN   A 1 73  ? -15.784 21.961  16.639  1   86.641  ? 85  GLN   A HG2  1 c 1 
ATOM   924  H HG3  . GLN   A 1 73  ? -16.443 21.891  18.08   1   84.165  ? 85  GLN   A HG3  1 c 1 
ATOM   925  H HE21 . GLN   A 1 73  ? -15.538 25.292  17.158  1   89.06   ? 85  GLN   A HE21 1 c 1 
ATOM   926  H HE22 . GLN   A 1 73  ? -16.487 24.23   16.58   1   89.207  ? 85  GLN   A HE22 1 c 1 
ATOM   927  N N    . VAL   A 1 74  ? -13.926 18.391  19.896  1   57.414  ? 86  VAL   A N    1 ? 1 
ATOM   928  C CA   . VAL   A 1 74  ? -13.013 17.464  20.522  1   53.156  ? 86  VAL   A CA   1 ? 1 
ATOM   929  C C    . VAL   A 1 74  ? -13.837 16.263  20.952  1   53.671  ? 86  VAL   A C    1 ? 1 
ATOM   930  O O    . VAL   A 1 74  ? -15.062 16.326  20.925  1   57.056  ? 86  VAL   A O    1 ? 1 
ATOM   931  C CB   . VAL   A 1 74  ? -12.366 18.175  21.734  1   52.896  ? 86  VAL   A CB   1 ? 1 
ATOM   932  C CG1  . VAL   A 1 74  ? -11.415 19.268  21.244  1   57.409  ? 86  VAL   A CG1  1 ? 1 
ATOM   933  C CG2  . VAL   A 1 74  ? -13.403 18.777  22.69   1   51.161  ? 86  VAL   A CG2  1 ? 1 
ATOM   934  H H    . VAL   A 1 74  ? -14.66  18.652  20.372  1   59.387  ? 86  VAL   A H    1 c 1 
ATOM   935  H HA   . VAL   A 1 74  ? -12.325 17.189  19.886  1   54.433  ? 86  VAL   A HA   1 c 1 
ATOM   936  H HB   . VAL   A 1 74  ? -11.84  17.501  22.227  1   51.227  ? 86  VAL   A HB   1 c 1 
ATOM   937  H HG11 . VAL   A 1 74  ? -11.925 19.972  20.809  1   58.287  ? 86  VAL   A HG11 1 c 1 
ATOM   938  H HG12 . VAL   A 1 74  ? -10.782 18.889  20.61   1   56.793  ? 86  VAL   A HG12 1 c 1 
ATOM   939  H HG13 . VAL   A 1 74  ? -10.93  19.641  22      1   55.599  ? 86  VAL   A HG13 1 c 1 
ATOM   940  H HG21 . VAL   A 1 74  ? -12.958 19.09   23.494  1   50.807  ? 86  VAL   A HG21 1 c 1 
ATOM   941  H HG22 . VAL   A 1 74  ? -14.061 18.103  22.928  1   51.293  ? 86  VAL   A HG22 1 c 1 
ATOM   942  H HG23 . VAL   A 1 74  ? -13.848 19.526  22.26   1   53.701  ? 86  VAL   A HG23 1 c 1 
ATOM   943  N N    . ILE   A 1 75  ? -13.142 15.221  21.426  1   49.385  ? 87  ILE   A N    1 ? 1 
ATOM   944  C CA   . ILE   A 1 75  ? -13.765 14.008  21.912  1   49.525  ? 87  ILE   A CA   1 ? 1 
ATOM   945  C C    . ILE   A 1 75  ? -14.674 14.337  23.122  1   49.749  ? 87  ILE   A C    1 ? 1 
ATOM   946  O O    . ILE   A 1 75  ? -14.35  15.247  23.895  1   54.349  ? 87  ILE   A O    1 ? 1 
ATOM   947  C CB   . ILE   A 1 75  ? -12.646 12.994  22.263  1   52.249  ? 87  ILE   A CB   1 ? 1 
ATOM   948  C CG1  . ILE   A 1 75  ? -11.538 13.59   23.138  1   50.121  ? 87  ILE   A CG1  1 ? 1 
ATOM   949  C CG2  . ILE   A 1 75  ? -12.021 12.312  21.039  1   56.339  ? 87  ILE   A CG2  1 ? 1 
ATOM   950  C CD1  . ILE   A 1 75  ? -10.625 12.485  23.661  1   50.549  ? 87  ILE   A CD1  1 ? 1 
ATOM   951  H H    . ILE   A 1 75  ? -12.23  15.274  21.423  1   49.649  ? 87  ILE   A H    1 c 1 
ATOM   952  H HA   . ILE   A 1 75  ? -14.314 13.633  21.197  1   51.683  ? 87  ILE   A HA   1 c 1 
ATOM   953  H HB   . ILE   A 1 75  ? -13.069 12.289  22.792  1   51.485  ? 87  ILE   A HB   1 c 1 
ATOM   954  H HG12 . ILE   A 1 75  ? -11.008 14.224  22.613  1   51      ? 87  ILE   A HG12 1 c 1 
ATOM   955  H HG13 . ILE   A 1 75  ? -11.937 14.069  23.893  1   49.955  ? 87  ILE   A HG13 1 c 1 
ATOM   956  H HG21 . ILE   A 1 75  ? -11.618 11.468  21.304  1   54.999  ? 87  ILE   A HG21 1 c 1 
ATOM   957  H HG22 . ILE   A 1 75  ? -11.338 12.889  20.657  1   55.669  ? 87  ILE   A HG22 1 c 1 
ATOM   958  H HG23 . ILE   A 1 75  ? -12.708 12.143  20.373  1   56.866  ? 87  ILE   A HG23 1 c 1 
ATOM   959  H HD11 . ILE   A 1 75  ? -11.161 11.721  23.948  1   50.172  ? 87  ILE   A HD11 1 c 1 
ATOM   960  H HD12 . ILE   A 1 75  ? -10.111 12.822  24.419  1   49.259  ? 87  ILE   A HD12 1 c 1 
ATOM   961  H HD13 . ILE   A 1 75  ? -10.012 12.203  22.956  1   50.82   ? 87  ILE   A HD13 1 c 1 
ATOM   962  N N    . LYS   A 1 76  ? -15.803 13.619  23.243  1   46.959  ? 88  LYS   A N    1 ? 1 
ATOM   963  C CA   . LYS   A 1 76  ? -16.732 13.638  24.371  1   50.843  ? 88  LYS   A CA   1 ? 1 
ATOM   964  C C    . LYS   A 1 76  ? -16.011 13.955  25.696  1   47.55   ? 88  LYS   A C    1 ? 1 
ATOM   965  O O    . LYS   A 1 76  ? -16.301 14.948  26.328  1   46.575  ? 88  LYS   A O    1 ? 1 
ATOM   966  C CB   . LYS   A 1 76  ? -17.513 12.309  24.408  1   50.119  ? 88  LYS   A CB   1 ? 1 
ATOM   967  H H    . LYS   A 1 76  ? -16.01  13.066  22.544  1   49.752  ? 88  LYS   A H    1 c 1 
ATOM   968  H HA   . LYS   A 1 76  ? -17.389 14.361  24.205  1   50.67   ? 88  LYS   A HA   1 c 1 
ATOM   969  H HB2  . LYS   A 1 76  ? -16.829 11.572  24.393  0   30      ? 88  LYS   A HB2  1 c 1 
ATOM   970  H HB3  . LYS   A 1 76  ? -18.43  12.515  24.371  0   30      ? 88  LYS   A HB3  1 c 1 
ATOM   971  N N    . ALA   A 1 77  ? -15.027 13.143  26.078  1   45.64   ? 89  ALA   A N    1 ? 1 
ATOM   972  C CA   . ALA   A 1 77  ? -14.266 13.31   27.308  1   43.051  ? 89  ALA   A CA   1 ? 1 
ATOM   973  C C    . ALA   A 1 77  ? -13.678 14.699  27.501  1   45.177  ? 89  ALA   A C    1 ? 1 
ATOM   974  O O    . ALA   A 1 77  ? -13.522 15.11   28.642  1   46.897  ? 89  ALA   A O    1 ? 1 
ATOM   975  C CB   . ALA   A 1 77  ? -13.124 12.339  27.387  1   43.74   ? 89  ALA   A CB   1 ? 1 
ATOM   976  H H    . ALA   A 1 77  ? -14.811 12.442  25.533  1   45.772  ? 89  ALA   A H    1 c 1 
ATOM   977  H HA   . ALA   A 1 77  ? -14.884 13.134  28.07   1   44.259  ? 89  ALA   A HA   1 c 1 
ATOM   978  H HB1  . ALA   A 1 77  ? -13.465 11.429  27.34   1   43.869  ? 89  ALA   A HB1  1 c 1 
ATOM   979  H HB2  . ALA   A 1 77  ? -12.514 12.491  26.646  1   43.313  ? 89  ALA   A HB2  1 c 1 
ATOM   980  H HB3  . ALA   A 1 77  ? -12.648 12.46   28.225  1   42.622  ? 89  ALA   A HB3  1 c 1 
ATOM   981  N N    . TRP   A 1 78  ? -13.26  15.373  26.43   1   50.384  ? 90  TRP   A N    1 ? 1 
ATOM   982  C CA   . TRP   A 1 78  ? -12.736 16.714  26.606  1   50.993  ? 90  TRP   A CA   1 ? 1 
ATOM   983  C C    . TRP   A 1 78  ? -13.86  17.69   26.93   1   52.617  ? 90  TRP   A C    1 ? 1 
ATOM   984  O O    . TRP   A 1 78  ? -13.718 18.555  27.793  1   60.228  ? 90  TRP   A O    1 ? 1 
ATOM   985  C CB   . TRP   A 1 78  ? -11.978 17.195  25.375  1   51.207  ? 90  TRP   A CB   1 ? 1 
ATOM   986  C CG   . TRP   A 1 78  ? -10.507 16.957  25.473  1   55.747  ? 90  TRP   A CG   1 ? 1 
ATOM   987  C CD1  . TRP   A 1 78  ? -9.872  15.811  25.838  1   52.723  ? 90  TRP   A CD1  1 ? 1 
ATOM   988  C CD2  . TRP   A 1 78  ? -9.485  17.957  25.314  1   54.061  ? 90  TRP   A CD2  1 ? 1 
ATOM   989  N NE1  . TRP   A 1 78  ? -8.52   16.007  25.84   1   55.001  ? 90  TRP   A NE1  1 ? 1 
ATOM   990  C CE2  . TRP   A 1 78  ? -8.257  17.321  25.553  1   52.956  ? 90  TRP   A CE2  1 ? 1 
ATOM   991  C CE3  . TRP   A 1 78  ? -9.504  19.312  25.007  1   56.139  ? 90  TRP   A CE3  1 ? 1 
ATOM   992  C CZ2  . TRP   A 1 78  ? -7.045  17.991  25.475  1   52.411  ? 90  TRP   A CZ2  1 ? 1 
ATOM   993  C CZ3  . TRP   A 1 78  ? -8.31   19.985  24.979  1   56.935  ? 90  TRP   A CZ3  1 ? 1 
ATOM   994  C CH2  . TRP   A 1 78  ? -7.096  19.322  25.166  1   56.717  ? 90  TRP   A CH2  1 ? 1 
ATOM   995  H H    . TRP   A 1 78  ? -13.295 15.001  25.596  1   49.721  ? 90  TRP   A H    1 c 1 
ATOM   996  H HA   . TRP   A 1 78  ? -12.101 16.702  27.373  1   49.989  ? 90  TRP   A HA   1 c 1 
ATOM   997  H HB2  . TRP   A 1 78  ? -12.326 16.73   24.585  1   53.107  ? 90  TRP   A HB2  1 c 1 
ATOM   998  H HB3  . TRP   A 1 78  ? -12.137 18.157  25.266  1   53.444  ? 90  TRP   A HB3  1 c 1 
ATOM   999  H HD1  . TRP   A 1 78  ? -10.291 14.978  25.99   1   53.257  ? 90  TRP   A HD1  1 c 1 
ATOM   1000 H HE1  . TRP   A 1 78  ? -7.926  15.402  26.031  1   53.347  ? 90  TRP   A HE1  1 c 1 
ATOM   1001 H HE3  . TRP   A 1 78  ? -10.318 19.762  24.86   1   56.826  ? 90  TRP   A HE3  1 c 1 
ATOM   1002 H HZ2  . TRP   A 1 78  ? -6.228  17.552  25.638  1   53.25   ? 90  TRP   A HZ2  1 c 1 
ATOM   1003 H HZ3  . TRP   A 1 78  ? -8.303  20.897  24.743  1   58.486  ? 90  TRP   A HZ3  1 c 1 
ATOM   1004 H HH2  . TRP   A 1 78  ? -6.294  19.813  25.126  1   56.844  ? 90  TRP   A HH2  1 c 1 
ATOM   1005 N N    . ASP   A 1 79  ? -14.974 17.601  26.214  1   54.189  ? 91  ASP   A N    1 ? 1 
ATOM   1006 C CA   . ASP   A 1 79  ? -16.097 18.477  26.509  1   53.078  ? 91  ASP   A CA   1 ? 1 
ATOM   1007 C C    . ASP   A 1 79  ? -16.533 18.277  27.955  1   50.771  ? 91  ASP   A C    1 ? 1 
ATOM   1008 O O    . ASP   A 1 79  ? -16.81  19.245  28.649  1   64.384  ? 91  ASP   A O    1 ? 1 
ATOM   1009 C CB   . ASP   A 1 79  ? -17.272 18.234  25.59   1   58.46   ? 91  ASP   A CB   1 ? 1 
ATOM   1010 C CG   . ASP   A 1 79  ? -17.181 18.858  24.208  1   62.831  ? 91  ASP   A CG   1 ? 1 
ATOM   1011 O OD1  . ASP   A 1 79  ? -16.481 19.889  24.109  1   67.413  ? 91  ASP   A OD1  1 ? 1 
ATOM   1012 O OD2  . ASP   A 1 79  ? -17.867 18.331  23.277  1   61.381  ? 91  ASP   A OD2  1 ? 1 
ATOM   1013 H H    . ASP   A 1 79  ? -15.04  16.997  25.531  1   53.705  ? 91  ASP   A H    1 c 1 
ATOM   1014 H HA   . ASP   A 1 79  ? -15.8   19.407  26.4    1   54.744  ? 91  ASP   A HA   1 c 1 
ATOM   1015 H HB2  . ASP   A 1 79  ? -17.385 17.268  25.478  1   57.63   ? 91  ASP   A HB2  1 c 1 
ATOM   1016 H HB3  . ASP   A 1 79  ? -18.082 18.58   26.019  1   59.332  ? 91  ASP   A HB3  1 c 1 
ATOM   1017 N N    . ILE   A 1 80  ? -16.58  17.027  28.42   1   51.277  ? 92  ILE   A N    1 ? 1 
ATOM   1018 C CA   . ILE   A 1 80  ? -16.991 16.715  29.786  1   52.144  ? 92  ILE   A CA   1 ? 1 
ATOM   1019 C C    . ILE   A 1 80  ? -15.945 17.174  30.797  1   50.578  ? 92  ILE   A C    1 ? 1 
ATOM   1020 O O    . ILE   A 1 80  ? -16.284 17.734  31.829  1   51.278  ? 92  ILE   A O    1 ? 1 
ATOM   1021 C CB   . ILE   A 1 80  ? -17.222 15.206  29.904  1   55.236  ? 92  ILE   A CB   1 ? 1 
ATOM   1022 C CG1  . ILE   A 1 80  ? -18.448 14.778  29.154  1   59.687  ? 92  ILE   A CG1  1 ? 1 
ATOM   1023 C CG2  . ILE   A 1 80  ? -17.311 14.769  31.36   1   58.537  ? 92  ILE   A CG2  1 ? 1 
ATOM   1024 C CD1  . ILE   A 1 80  ? -18.47  13.286  28.995  1   63.214  ? 92  ILE   A CD1  1 ? 1 
ATOM   1025 H H    . ILE   A 1 80  ? -16.353 16.339  27.863  1   50.778  ? 92  ILE   A H    1 c 1 
ATOM   1026 H HA   . ILE   A 1 80  ? -17.833 17.174  29.972  1   53.927  ? 92  ILE   A HA   1 c 1 
ATOM   1027 H HB   . ILE   A 1 80  ? -16.453 14.755  29.503  1   54.633  ? 92  ILE   A HB   1 c 1 
ATOM   1028 H HG12 . ILE   A 1 80  ? -19.246 15.065  29.643  1   61.109  ? 92  ILE   A HG12 1 c 1 
ATOM   1029 H HG13 . ILE   A 1 80  ? -18.456 15.2    28.271  1   60.231  ? 92  ILE   A HG13 1 c 1 
ATOM   1030 H HG21 . ILE   A 1 80  ? -17.677 13.872  31.414  1   57.997  ? 92  ILE   A HG21 1 c 1 
ATOM   1031 H HG22 . ILE   A 1 80  ? -17.888 15.38   31.849  1   58.466  ? 92  ILE   A HG22 1 c 1 
ATOM   1032 H HG23 . ILE   A 1 80  ? -16.424 14.776  31.758  1   56.343  ? 92  ILE   A HG23 1 c 1 
ATOM   1033 H HD11 . ILE   A 1 80  ? -17.579 12.962  28.763  1   60.793  ? 92  ILE   A HD11 1 c 1 
ATOM   1034 H HD12 . ILE   A 1 80  ? -19.093 13.052  28.281  1   63.401  ? 92  ILE   A HD12 1 c 1 
ATOM   1035 H HD13 . ILE   A 1 80  ? -18.761 12.866  29.826  1   62.414  ? 92  ILE   A HD13 1 c 1 
ATOM   1036 N N    . GLY   A 1 81  ? -14.68  16.857  30.523  1   44.922  ? 93  GLY   A N    1 ? 1 
ATOM   1037 C CA   . GLY   A 1 81  ? -13.595 17.095  31.461  1   45.057  ? 93  GLY   A CA   1 ? 1 
ATOM   1038 C C    . GLY   A 1 81  ? -13.31  18.595  31.665  1   44.995  ? 93  GLY   A C    1 ? 1 
ATOM   1039 O O    . GLY   A 1 81  ? -13.225 19.081  32.785  1   42.843  ? 93  GLY   A O    1 ? 1 
ATOM   1040 H H    . GLY   A 1 81  ? -14.482 16.473  29.718  1   45.873  ? 93  GLY   A H    1 c 1 
ATOM   1041 H HA2  . GLY   A 1 81  ? -13.826 16.69   32.325  1   44.835  ? 93  GLY   A HA2  1 c 1 
ATOM   1042 H HA3  . GLY   A 1 81  ? -12.78  16.65   31.127  1   43.855  ? 93  GLY   A HA3  1 c 1 
ATOM   1043 N N    . VAL   A 1 82  ? -13.18  19.315  30.548  1   40.889  ? 94  VAL   A N    1 ? 1 
ATOM   1044 C CA   . VAL   A 1 82  ? -12.835 20.704  30.616  1   43.917  ? 94  VAL   A CA   1 ? 1 
ATOM   1045 C C    . VAL   A 1 82  ? -13.953 21.535  31.25   1   48.983  ? 94  VAL   A C    1 ? 1 
ATOM   1046 O O    . VAL   A 1 82  ? -13.653 22.557  31.866  1   43.765  ? 94  VAL   A O    1 ? 1 
ATOM   1047 C CB   . VAL   A 1 82  ? -12.402 21.193  29.239  1   44.064  ? 94  VAL   A CB   1 ? 1 
ATOM   1048 C CG1  . VAL   A 1 82  ? -12.117 22.666  29.261  1   52.608  ? 94  VAL   A CG1  1 ? 1 
ATOM   1049 C CG2  . VAL   A 1 82  ? -11.144 20.493  28.821  1   43.684  ? 94  VAL   A CG2  1 ? 1 
ATOM   1050 H H    . VAL   A 1 82  ? -13.317 18.927  29.733  1   42.276  ? 94  VAL   A H    1 c 1 
ATOM   1051 H HA   . VAL   A 1 82  ? -12.057 20.777  31.202  1   43.65   ? 94  VAL   A HA   1 c 1 
ATOM   1052 H HB   . VAL   A 1 82  ? -13.127 21      28.599  1   45.983  ? 94  VAL   A HB   1 c 1 
ATOM   1053 H HG11 . VAL   A 1 82  ? -11.636 22.893  30.075  1   50.327  ? 94  VAL   A HG11 1 c 1 
ATOM   1054 H HG12 . VAL   A 1 82  ? -12.953 23.161  29.231  1   51.828  ? 94  VAL   A HG12 1 c 1 
ATOM   1055 H HG13 . VAL   A 1 82  ? -11.575 22.906  28.49   1   51.022  ? 94  VAL   A HG13 1 c 1 
ATOM   1056 H HG21 . VAL   A 1 82  ? -10.867 20.816  27.947  1   44.214  ? 94  VAL   A HG21 1 c 1 
ATOM   1057 H HG22 . VAL   A 1 82  ? -11.302 19.535  28.774  1   42.361  ? 94  VAL   A HG22 1 c 1 
ATOM   1058 H HG23 . VAL   A 1 82  ? -10.442 20.673  29.468  1   43.197  ? 94  VAL   A HG23 1 c 1 
ATOM   1059 N N    . ALA   A 1 83  ? -15.211 21.078  31.171  1   45.799  ? 95  ALA   A N    1 ? 1 
ATOM   1060 C CA   . ALA   A 1 83  ? -16.291 21.785  31.844  1   49.467  ? 95  ALA   A CA   1 ? 1 
ATOM   1061 C C    . ALA   A 1 83  ? -16.235 21.66   33.369  1   50.859  ? 95  ALA   A C    1 ? 1 
ATOM   1062 O O    . ALA   A 1 83  ? -17.004 22.331  34.035  1   53.831  ? 95  ALA   A O    1 ? 1 
ATOM   1063 C CB   . ALA   A 1 83  ? -17.656 21.305  31.317  1   51.806  ? 95  ALA   A CB   1 ? 1 
ATOM   1064 H H    . ALA   A 1 83  ? -15.402 20.327  30.687  1   46.316  ? 95  ALA   A H    1 c 1 
ATOM   1065 H HA   . ALA   A 1 83  ? -16.198 22.753  31.621  1   50.984  ? 95  ALA   A HA   1 c 1 
ATOM   1066 H HB1  . ALA   A 1 83  ? -17.65  21.305  30.345  1   51.731  ? 95  ALA   A HB1  1 c 1 
ATOM   1067 H HB2  . ALA   A 1 83  ? -17.832 20.405  31.637  1   50.582  ? 95  ALA   A HB2  1 c 1 
ATOM   1068 H HB3  . ALA   A 1 83  ? -18.356 21.901  31.634  1   53.352  ? 95  ALA   A HB3  1 c 1 
ATOM   1069 N N    . THR   A 1 84  ? -15.379 20.793  33.933  1   53.787  ? 96  THR   A N    1 ? 1 
ATOM   1070 C CA   . THR   A 1 84  ? -15.169 20.725  35.382  1   54.071  ? 96  THR   A CA   1 ? 1 
ATOM   1071 C C    . THR   A 1 84  ? -13.984 21.569  35.851  1   57.453  ? 96  THR   A C    1 ? 1 
ATOM   1072 O O    . THR   A 1 84  ? -13.729 21.591  37.043  1   54.745  ? 96  THR   A O    1 ? 1 
ATOM   1073 C CB   . THR   A 1 84  ? -14.905 19.274  35.808  1   54.47   ? 96  THR   A CB   1 ? 1 
ATOM   1074 O OG1  . THR   A 1 84  ? -13.61  18.848  35.356  1   43.711  ? 96  THR   A OG1  1 ? 1 
ATOM   1075 C CG2  . THR   A 1 84  ? -15.939 18.331  35.216  1   53.365  ? 96  THR   A CG2  1 ? 1 
ATOM   1076 H H    . THR   A 1 84  ? -14.916 20.213  33.4    1   51.216  ? 96  THR   A H    1 c 1 
ATOM   1077 H HA   . THR   A 1 84  ? -15.981 21.041  35.833  1   56.402  ? 96  THR   A HA   1 c 1 
ATOM   1078 H HB   . THR   A 1 84  ? -14.942 19.21   36.793  1   52.631  ? 96  THR   A HB   1 c 1 
ATOM   1079 H HG1  . THR   A 1 84  ? -13.622 18.977  34.486  0   30      ? 96  THR   A HG1  1 c 1 
ATOM   1080 H HG21 . THR   A 1 84  ? -15.956 17.505  35.728  1   53.455  ? 96  THR   A HG21 1 c 1 
ATOM   1081 H HG22 . THR   A 1 84  ? -15.707 18.133  34.294  1   52.736  ? 96  THR   A HG22 1 c 1 
ATOM   1082 H HG23 . THR   A 1 84  ? -16.816 18.749  35.246  1   55.04   ? 96  THR   A HG23 1 c 1 
ATOM   1083 N N    . MET   A 1 85  ? -13.18  22.161  34.955  1   56.541  ? 97  MET   A N    1 ? 1 
ATOM   1084 C CA   . MET   A 1 85  ? -11.907 22.751  35.365  1   50.469  ? 97  MET   A CA   1 ? 1 
ATOM   1085 C C    . MET   A 1 85  ? -12.039 24.264  35.58   1   49.706  ? 97  MET   A C    1 ? 1 
ATOM   1086 O O    . MET   A 1 85  ? -12.818 24.9    34.911  1   50.066  ? 97  MET   A O    1 ? 1 
ATOM   1087 C CB   . MET   A 1 85  ? -10.817 22.506  34.305  1   45.966  ? 97  MET   A CB   1 ? 1 
ATOM   1088 C CG   . MET   A 1 85  ? -10.569 21.009  34.027  1   49.239  ? 97  MET   A CG   1 ? 1 
ATOM   1089 S SD   . MET   A 1 85  ? -9.414  20.776  32.668  1   48.666  ? 97  MET   A SD   1 ? 1 
ATOM   1090 C CE   . MET   A 1 85  ? -7.943  21.514  33.379  1   47.734  ? 97  MET   A CE   1 ? 1 
ATOM   1091 H H    . MET   A 1 85  ? -13.427 22.204  34.077  1   54.974  ? 97  MET   A H    1 c 1 
ATOM   1092 H HA   . MET   A 1 85  ? -11.63  22.335  36.217  1   50.118  ? 97  MET   A HA   1 c 1 
ATOM   1093 H HB2  . MET   A 1 85  ? -11.083 22.948  33.47   1   48.392  ? 97  MET   A HB2  1 c 1 
ATOM   1094 H HB3  . MET   A 1 85  ? -9.983  22.92   34.612  1   48.474  ? 97  MET   A HB3  1 c 1 
ATOM   1095 H HG2  . MET   A 1 85  ? -10.209 20.582  34.827  1   47.645  ? 97  MET   A HG2  1 c 1 
ATOM   1096 H HG3  . MET   A 1 85  ? -11.414 20.573  33.804  1   47.526  ? 97  MET   A HG3  1 c 1 
ATOM   1097 H HE1  . MET   A 1 85  ? -7.204  21.432  32.748  1   48.213  ? 97  MET   A HE1  1 c 1 
ATOM   1098 H HE2  . MET   A 1 85  ? -8.105  22.458  33.56   1   49.597  ? 97  MET   A HE2  1 c 1 
ATOM   1099 H HE3  . MET   A 1 85  ? -7.717  21.055  34.209  1   47.997  ? 97  MET   A HE3  1 c 1 
ATOM   1100 N N    . LYS   A 1 86  ? -11.186 24.855  36.408  1   56.172  ? 98  LYS   A N    1 ? 1 
ATOM   1101 C CA   . LYS   A 1 86  ? -11.202 26.31   36.627  1   62.063  ? 98  LYS   A CA   1 ? 1 
ATOM   1102 C C    . LYS   A 1 86  ? -9.973  26.913  35.943  1   60.714  ? 98  LYS   A C    1 ? 1 
ATOM   1103 O O    . LYS   A 1 86  ? -9.069  26.156  35.549  1   55.581  ? 98  LYS   A O    1 ? 1 
ATOM   1104 C CB   . LYS   A 1 86  ? -11.208 26.635  38.119  1   64.627  ? 98  LYS   A CB   1 ? 1 
ATOM   1105 C CG   . LYS   A 1 86  ? -11.914 25.72   39.114  1   69.971  ? 98  LYS   A CG   1 ? 1 
ATOM   1106 C CD   . LYS   A 1 86  ? -13.306 26.198  39.527  1   82.297  ? 98  LYS   A CD   1 ? 1 
ATOM   1107 C CE   . LYS   A 1 86  ? -13.615 25.877  40.975  1   94.848  ? 98  LYS   A CE   1 ? 1 
ATOM   1108 N NZ   . LYS   A 1 86  ? -13.701 24.417  41.149  1   96.026  ? 98  LYS   A NZ   1 ? 1 
ATOM   1109 H H    . LYS   A 1 86  ? -10.571 24.349  36.856  1   54.672  ? 98  LYS   A H    1 c 1 
ATOM   1110 H HA   . LYS   A 1 86  ? -12.018 26.688  36.211  1   62.04   ? 98  LYS   A HA   1 c 1 
ATOM   1111 H HB2  . LYS   A 1 86  ? -10.272 26.704  38.404  1   65.978  ? 98  LYS   A HB2  1 c 1 
ATOM   1112 H HB3  . LYS   A 1 86  ? -11.597 27.53   38.216  1   68.215  ? 98  LYS   A HB3  1 c 1 
ATOM   1113 H HG2  . LYS   A 1 86  ? -11.991 24.825  38.719  1   68.336  ? 98  LYS   A HG2  1 c 1 
ATOM   1114 H HG3  . LYS   A 1 86  ? -11.352 25.642  39.916  1   71.215  ? 98  LYS   A HG3  1 c 1 
ATOM   1115 H HD2  . LYS   A 1 86  ? -13.37  27.168  39.394  1   83.828  ? 98  LYS   A HD2  1 c 1 
ATOM   1116 H HD3  . LYS   A 1 86  ? -13.976 25.769  38.952  1   81.091  ? 98  LYS   A HD3  1 c 1 
ATOM   1117 H HE2  . LYS   A 1 86  ? -12.916 26.23   41.553  1   93.766  ? 98  LYS   A HE2  1 c 1 
ATOM   1118 H HE3  . LYS   A 1 86  ? -14.463 26.282  41.23   1   94.645  ? 98  LYS   A HE3  1 c 1 
ATOM   1119 H HZ1  . LYS   A 1 86  ? -12.87  24.056  41.151  1   93.569  ? 98  LYS   A HZ1  1 c 1 
ATOM   1120 H HZ2  . LYS   A 1 86  ? -14.185 24.049  40.477  1   93.527  ? 98  LYS   A HZ2  1 c 1 
ATOM   1121 H HZ3  . LYS   A 1 86  ? -14.105 24.23   41.938  1   95.907  ? 98  LYS   A HZ3  1 c 1 
ATOM   1122 N N    . LYS   A 1 87  ? -9.915  28.249  35.803  1   64.059  ? 99  LYS   A N    1 ? 1 
ATOM   1123 C CA   . LYS   A 1 87  ? -8.753  28.859  35.156  1   69.75   ? 99  LYS   A CA   1 ? 1 
ATOM   1124 C C    . LYS   A 1 87  ? -7.507  28.491  35.959  1   70.357  ? 99  LYS   A C    1 ? 1 
ATOM   1125 O O    . LYS   A 1 87  ? -7.51   28.479  37.186  1   73.602  ? 99  LYS   A O    1 ? 1 
ATOM   1126 C CB   . LYS   A 1 87  ? -8.822  30.365  34.873  1   77.773  ? 99  LYS   A CB   1 ? 1 
ATOM   1127 C CG   . LYS   A 1 87  ? -7.686  30.926  33.997  1   83.81   ? 99  LYS   A CG   1 ? 1 
ATOM   1128 C CD   . LYS   A 1 87  ? -7.67   32.451  33.791  1   96.226  ? 99  LYS   A CD   1 ? 1 
ATOM   1129 C CE   . LYS   A 1 87  ? -6.541  32.986  32.899  1   102.757 ? 99  LYS   A CE   1 ? 1 
ATOM   1130 N NZ   . LYS   A 1 87  ? -6.419  34.444  32.75   1   103.362 ? 99  LYS   A NZ   1 ? 1 
ATOM   1131 H H    . LYS   A 1 87  ? -10.594 28.779  36.107  1   66.553  ? 99  LYS   A H    1 c 1 
ATOM   1132 H HA   . LYS   A 1 87  ? -8.664  28.431  34.267  1   68.287  ? 99  LYS   A HA   1 c 1 
ATOM   1133 H HB2  . LYS   A 1 87  ? -9.676  30.56   34.432  1   78.216  ? 99  LYS   A HB2  1 c 1 
ATOM   1134 H HB3  . LYS   A 1 87  ? -8.816  30.844  35.73   1   79.498  ? 99  LYS   A HB3  1 c 1 
ATOM   1135 H HG2  . LYS   A 1 87  ? -6.83   30.657  34.395  1   83.855  ? 99  LYS   A HG2  1 c 1 
ATOM   1136 H HG3  . LYS   A 1 87  ? -7.747  30.494  33.12   1   82.935  ? 99  LYS   A HG3  1 c 1 
ATOM   1137 H HD2  . LYS   A 1 87  ? -8.531  32.718  33.401  1   96.009  ? 99  LYS   A HD2  1 c 1 
ATOM   1138 H HD3  . LYS   A 1 87  ? -7.605  32.881  34.671  1   96.922  ? 99  LYS   A HD3  1 c 1 
ATOM   1139 H HE2  . LYS   A 1 87  ? -5.694  32.643  33.235  1   99.86   ? 99  LYS   A HE2  1 c 1 
ATOM   1140 H HE3  . LYS   A 1 87  ? -6.668  32.621  32.007  1   99.336  ? 99  LYS   A HE3  1 c 1 
ATOM   1141 H HZ1  . LYS   A 1 87  ? -6.158  34.811  33.536  1   106.249 ? 99  LYS   A HZ1  1 c 1 
ATOM   1142 H HZ2  . LYS   A 1 87  ? -7.218  34.794  32.508  1   105.777 ? 99  LYS   A HZ2  1 c 1 
ATOM   1143 H HZ3  . LYS   A 1 87  ? -5.804  34.636  32.113  1   105.914 ? 99  LYS   A HZ3  1 c 1 
ATOM   1144 N N    . GLY   A 1 88  ? -6.459  28.072  35.251  1   71.652  ? 100 GLY   A N    1 ? 1 
ATOM   1145 C CA   . GLY   A 1 88  ? -5.195  27.737  35.893  1   71.209  ? 100 GLY   A CA   1 ? 1 
ATOM   1146 C C    . GLY   A 1 88  ? -5.144  26.313  36.464  1   64.567  ? 100 GLY   A C    1 ? 1 
ATOM   1147 O O    . GLY   A 1 88  ? -4.19   25.959  37.141  1   64.417  ? 100 GLY   A O    1 ? 1 
ATOM   1148 H H    . GLY   A 1 88  ? -6.528  27.993  34.343  1   70.353  ? 100 GLY   A H    1 c 1 
ATOM   1149 H HA2  . GLY   A 1 88  ? -4.471  27.842  35.232  1   71.011  ? 100 GLY   A HA2  1 c 1 
ATOM   1150 H HA3  . GLY   A 1 88  ? -5.028  28.382  36.62   1   72.655  ? 100 GLY   A HA3  1 c 1 
ATOM   1151 N N    . GLU   A 1 89  ? -6.166  25.487  36.212  1   59.081  ? 101 GLU   A N    1 ? 1 
ATOM   1152 C CA   . GLU   A 1 89  ? -6.184  24.117  36.702  1   54.551  ? 101 GLU   A CA   1 ? 1 
ATOM   1153 C C    . GLU   A 1 89  ? -5.368  23.293  35.703  1   55.625  ? 101 GLU   A C    1 ? 1 
ATOM   1154 O O    . GLU   A 1 89  ? -5.384  23.484  34.471  1   53.591  ? 101 GLU   A O    1 ? 1 
ATOM   1155 C CB   . GLU   A 1 89  ? -7.628  23.701  37.025  1   54.351  ? 101 GLU   A CB   1 ? 1 
ATOM   1156 C CG   . GLU   A 1 89  ? -7.819  22.334  37.683  1   50.175  ? 101 GLU   A CG   1 ? 1 
ATOM   1157 C CD   . GLU   A 1 89  ? -9.244  21.839  37.754  1   48.089  ? 101 GLU   A CD   1 ? 1 
ATOM   1158 O OE1  . GLU   A 1 89  ? -10.233 22.453  38.3    1   50.158  ? 101 GLU   A OE1  1 ? 1 
ATOM   1159 O OE2  . GLU   A 1 89  ? -9.361  20.731  37.15   1   48.61   ? 101 GLU   A OE2  1 ? 1 
ATOM   1160 H H    . GLU   A 1 89  ? -6.873  25.782  35.713  1   59.285  ? 101 GLU   A H    1 c 1 
ATOM   1161 H HA   . GLU   A 1 89  ? -5.701  24.107  37.564  1   56.689  ? 101 GLU   A HA   1 c 1 
ATOM   1162 H HB2  . GLU   A 1 89  ? -8.019  24.377  37.617  1   55.146  ? 101 GLU   A HB2  1 c 1 
ATOM   1163 H HB3  . GLU   A 1 89  ? -8.143  23.706  36.192  1   52.825  ? 101 GLU   A HB3  1 c 1 
ATOM   1164 H HG2  . GLU   A 1 89  ? -7.286  21.672  37.193  1   49.316  ? 101 GLU   A HG2  1 c 1 
ATOM   1165 H HG3  . GLU   A 1 89  ? -7.463  22.373  38.596  1   51.496  ? 101 GLU   A HG3  1 c 1 
ATOM   1166 N N    . ILE   A 1 90  ? -4.527  22.451  36.29   1   58.898  ? 102 ILE   A N    1 ? 1 
ATOM   1167 C CA   . ILE   A 1 90  ? -3.974  21.316  35.597  1   54.392  ? 102 ILE   A CA   1 ? 1 
ATOM   1168 C C    . ILE   A 1 90  ? -4.674  20.082  36.138  1   53.522  ? 102 ILE   A C    1 ? 1 
ATOM   1169 O O    . ILE   A 1 90  ? -4.663  19.837  37.344  1   51.658  ? 102 ILE   A O    1 ? 1 
ATOM   1170 C CB   . ILE   A 1 90  ? -2.467  21.237  35.819  1   55.913  ? 102 ILE   A CB   1 ? 1 
ATOM   1171 C CG1  . ILE   A 1 90  ? -1.734  22.488  35.27   1   60.341  ? 102 ILE   A CG1  1 ? 1 
ATOM   1172 C CG2  . ILE   A 1 90  ? -1.914  19.93   35.247  1   54.864  ? 102 ILE   A CG2  1 ? 1 
ATOM   1173 C CD1  . ILE   A 1 90  ? -0.311  22.629  35.796  1   64.67   ? 102 ILE   A CD1  1 ? 1 
ATOM   1174 H H    . ILE   A 1 90  ? -4.284  22.593  37.16   1   58.356  ? 102 ILE   A H    1 c 1 
ATOM   1175 H HA   . ILE   A 1 90  ? -4.151  21.403  34.645  1   54.363  ? 102 ILE   A HA   1 c 1 
ATOM   1176 H HB   . ILE   A 1 90  ? -2.318  21.218  36.786  1   57.206  ? 102 ILE   A HB   1 c 1 
ATOM   1177 H HG12 . ILE   A 1 90  ? -1.707  22.434  34.292  1   59.704  ? 102 ILE   A HG12 1 c 1 
ATOM   1178 H HG13 . ILE   A 1 90  ? -2.243  23.288  35.514  1   60.974  ? 102 ILE   A HG13 1 c 1 
ATOM   1179 H HG21 . ILE   A 1 90  ? -0.944  19.943  35.279  1   56.239  ? 102 ILE   A HG21 1 c 1 
ATOM   1180 H HG22 . ILE   A 1 90  ? -2.204  19.831  34.325  1   53.869  ? 102 ILE   A HG22 1 c 1 
ATOM   1181 H HG23 . ILE   A 1 90  ? -2.241  19.179  35.768  1   54.071  ? 102 ILE   A HG23 1 c 1 
ATOM   1182 H HD11 . ILE   A 1 90  ? -0.332  22.821  36.753  1   65.005  ? 102 ILE   A HD11 1 c 1 
ATOM   1183 H HD12 . ILE   A 1 90  ? 0.131   23.362  35.328  1   65.591  ? 102 ILE   A HD12 1 c 1 
ATOM   1184 H HD13 . ILE   A 1 90  ? 0.186   21.804  35.642  1   63.595  ? 102 ILE   A HD13 1 c 1 
ATOM   1185 N N    . ALA   A 1 91  ? -5.18   19.293  35.2    1   47.063  ? 103 ALA   A N    1 ? 1 
ATOM   1186 C CA   . ALA   A 1 91  ? -5.81   18.011  35.477  1   45.884  ? 103 ALA   A CA   1 ? 1 
ATOM   1187 C C    . ALA   A 1 91  ? -5.263  16.939  34.535  1   46.037  ? 103 ALA   A C    1 ? 1 
ATOM   1188 O O    . ALA   A 1 91  ? -4.765  17.249  33.457  1   46.387  ? 103 ALA   A O    1 ? 1 
ATOM   1189 C CB   . ALA   A 1 91  ? -7.333  18.118  35.299  1   40.979  ? 103 ALA   A CB   1 ? 1 
ATOM   1190 H H    . ALA   A 1 91  ? -5.134  19.567  34.329  1   48      ? 103 ALA   A H    1 c 1 
ATOM   1191 H HA   . ALA   A 1 91  ? -5.6    17.749  36.413  1   45.983  ? 103 ALA   A HA   1 c 1 
ATOM   1192 H HB1  . ALA   A 1 91  ? -7.685  18.793  35.904  1   42.901  ? 103 ALA   A HB1  1 c 1 
ATOM   1193 H HB2  . ALA   A 1 91  ? -7.539  18.368  34.383  1   41.713  ? 103 ALA   A HB2  1 c 1 
ATOM   1194 H HB3  . ALA   A 1 91  ? -7.746  17.261  35.499  1   41.6    ? 103 ALA   A HB3  1 c 1 
ATOM   1195 N N    . HIS   A 1 92  ? -5.384  15.695  34.989  1   47.01   ? 104 HIS   A N    1 ? 1 
ATOM   1196 C CA   . HIS   A 1 92  ? -5.13   14.487  34.243  1   47.162  ? 104 HIS   A CA   1 ? 1 
ATOM   1197 C C    . HIS   A 1 92  ? -6.477  13.79   34.038  1   42.978  ? 104 HIS   A C    1 ? 1 
ATOM   1198 O O    . HIS   A 1 92  ? -7.307  13.68   34.955  1   46.517  ? 104 HIS   A O    1 ? 1 
ATOM   1199 C CB   . HIS   A 1 92  ? -4.194  13.559  35.024  1   44.838  ? 104 HIS   A CB   1 ? 1 
ATOM   1200 C CG   . HIS   A 1 92  ? -2.811  14.059  35.183  1   45.735  ? 104 HIS   A CG   1 ? 1 
ATOM   1201 N ND1  . HIS   A 1 92  ? -1.806  13.422  35.893  1   45.808  ? 104 HIS   A ND1  1 ? 1 
ATOM   1202 C CD2  . HIS   A 1 92  ? -2.279  15.09   34.6    1   44.649  ? 104 HIS   A CD2  1 ? 1 
ATOM   1203 C CE1  . HIS   A 1 92  ? -0.704  14.123  35.783  1   50.127  ? 104 HIS   A CE1  1 ? 1 
ATOM   1204 N NE2  . HIS   A 1 92  ? -0.961  15.134  34.965  1   50.634  ? 104 HIS   A NE2  1 ? 1 
ATOM   1205 H H    . HIS   A 1 92  ? -5.654  15.596  35.856  1   47.226  ? 104 HIS   A H    1 c 1 
ATOM   1206 H HA   . HIS   A 1 92  ? -4.744  14.713  33.365  1   45.558  ? 104 HIS   A HA   1 c 1 
ATOM   1207 H HB2  . HIS   A 1 92  ? -4.579  13.406  35.914  1   45.872  ? 104 HIS   A HB2  1 c 1 
ATOM   1208 H HB3  . HIS   A 1 92  ? -4.165  12.691  34.566  1   45.44   ? 104 HIS   A HB3  1 c 1 
ATOM   1209 H HD1  . HIS   A 1 92  ? -1.981  12.736  36.347  0   30      ? 104 HIS   A HD1  1 c 1 
ATOM   1210 H HD2  . HIS   A 1 92  ? -2.705  15.7    34.033  1   45.272  ? 104 HIS   A HD2  1 c 1 
ATOM   1211 H HE1  . HIS   A 1 92  ? 0.128   13.924  36.178  1   51.386  ? 104 HIS   A HE1  1 c 1 
ATOM   1212 H HE2  . HIS   A 1 92  ? -0.368  15.75   34.701  0   30      ? 104 HIS   A HE2  1 c 1 
ATOM   1213 N N    . LEU   A 1 93  ? -6.696  13.353  32.809  1   41.48   ? 105 LEU   A N    1 ? 1 
ATOM   1214 C CA   . LEU   A 1 93  ? -7.886  12.612  32.443  1   44.713  ? 105 LEU   A CA   1 ? 1 
ATOM   1215 C C    . LEU   A 1 93  ? -7.46   11.258  31.874  1   44.161  ? 105 LEU   A C    1 ? 1 
ATOM   1216 O O    . LEU   A 1 93  ? -6.531  11.185  31.088  1   52.893  ? 105 LEU   A O    1 ? 1 
ATOM   1217 C CB   . LEU   A 1 93  ? -8.639  13.419  31.399  1   41.148  ? 105 LEU   A CB   1 ? 1 
ATOM   1218 C CG   . LEU   A 1 93  ? -9.276  14.727  31.805  1   43.93   ? 105 LEU   A CG   1 ? 1 
ATOM   1219 C CD1  . LEU   A 1 93  ? -10.001 15.243  30.566  1   44.145  ? 105 LEU   A CD1  1 ? 1 
ATOM   1220 C CD2  . LEU   A 1 93  ? -10.202 14.478  32.965  1   46.935  ? 105 LEU   A CD2  1 ? 1 
ATOM   1221 H H    . LEU   A 1 93  ? -6.073  13.522  32.161  1   42.605  ? 105 LEU   A H    1 c 1 
ATOM   1222 H HA   . LEU   A 1 93  ? -8.451  12.479  33.241  1   43.513  ? 105 LEU   A HA   1 c 1 
ATOM   1223 H HB2  . LEU   A 1 93  ? -8.016  13.602  30.658  1   42.496  ? 105 LEU   A HB2  1 c 1 
ATOM   1224 H HB3  . LEU   A 1 93  ? -9.343  12.841  31.026  1   42.496  ? 105 LEU   A HB3  1 c 1 
ATOM   1225 H HG   . LEU   A 1 93  ? -8.567  15.368  32.071  1   44.107  ? 105 LEU   A HG   1 c 1 
ATOM   1226 H HD11 . LEU   A 1 93  ? -9.367  15.345  29.836  1   44.12   ? 105 LEU   A HD11 1 c 1 
ATOM   1227 H HD12 . LEU   A 1 93  ? -10.406 16.105  30.763  1   44.44   ? 105 LEU   A HD12 1 c 1 
ATOM   1228 H HD13 . LEU   A 1 93  ? -10.693 14.613  30.308  1   44.111  ? 105 LEU   A HD13 1 c 1 
ATOM   1229 H HD21 . LEU   A 1 93  ? -9.682  14.367  33.778  1   46.256  ? 105 LEU   A HD21 1 c 1 
ATOM   1230 H HD22 . LEU   A 1 93  ? -10.722 13.673  32.801  1   46.099  ? 105 LEU   A HD22 1 c 1 
ATOM   1231 H HD23 . LEU   A 1 93  ? -10.804 15.235  33.067  1   46.334  ? 105 LEU   A HD23 1 c 1 
ATOM   1232 N N    . LEU   A 1 94  ? -8.118  10.189  32.295  1   49.558  ? 106 LEU   A N    1 ? 1 
ATOM   1233 C CA   . LEU   A 1 94  ? -7.895  8.873   31.724  1   46.883  ? 106 LEU   A CA   1 ? 1 
ATOM   1234 C C    . LEU   A 1 94  ? -9.211  8.39    31.138  1   51.985  ? 106 LEU   A C    1 ? 1 
ATOM   1235 O O    . LEU   A 1 94  ? -10.253 8.301   31.828  1   50.445  ? 106 LEU   A O    1 ? 1 
ATOM   1236 C CB   . LEU   A 1 94  ? -7.371  7.867   32.71   1   50.931  ? 106 LEU   A CB   1 ? 1 
ATOM   1237 C CG   . LEU   A 1 94  ? -7.162  6.475   32.093  1   59.698  ? 106 LEU   A CG   1 ? 1 
ATOM   1238 C CD1  . LEU   A 1 94  ? -5.88   6.444   31.291  1   54.009  ? 106 LEU   A CD1  1 ? 1 
ATOM   1239 C CD2  . LEU   A 1 94  ? -7.177  5.356   33.132  1   62.082  ? 106 LEU   A CD2  1 ? 1 
ATOM   1240 H H    . LEU   A 1 94  ? -8.732  10.277  32.967  1   47.586  ? 106 LEU   A H    1 c 1 
ATOM   1241 H HA   . LEU   A 1 94  ? -7.241  8.964   30.987  1   48.795  ? 106 LEU   A HA   1 c 1 
ATOM   1242 H HB2  . LEU   A 1 94  ? -6.509  8.191   33.061  1   51.987  ? 106 LEU   A HB2  1 c 1 
ATOM   1243 H HB3  . LEU   A 1 94  ? -8.014  7.791   33.452  1   52.129  ? 106 LEU   A HB3  1 c 1 
ATOM   1244 H HG   . LEU   A 1 94  ? -7.909  6.302   31.465  1   56.805  ? 106 LEU   A HG   1 c 1 
ATOM   1245 H HD11 . LEU   A 1 94  ? -5.945  7.068   30.549  1   54.663  ? 106 LEU   A HD11 1 c 1 
ATOM   1246 H HD12 . LEU   A 1 94  ? -5.734  5.547   30.946  1   57.002  ? 106 LEU   A HD12 1 c 1 
ATOM   1247 H HD13 . LEU   A 1 94  ? -5.134  6.696   31.86   1   56.015  ? 106 LEU   A HD13 1 c 1 
ATOM   1248 H HD21 . LEU   A 1 94  ? -8.038  5.343   33.582  1   62.059  ? 106 LEU   A HD21 1 c 1 
ATOM   1249 H HD22 . LEU   A 1 94  ? -6.473  5.51    33.785  1   62.488  ? 106 LEU   A HD22 1 c 1 
ATOM   1250 H HD23 . LEU   A 1 94  ? -7.029  4.502   32.692  1   63.279  ? 106 LEU   A HD23 1 c 1 
ATOM   1251 N N    . ILE   A 1 95  ? -9.125  8.123   29.834  1   42.733  ? 107 ILE   A N    1 ? 1 
ATOM   1252 C CA   . ILE   A 1 95  ? -10.284 8.13    28.974  1   44.76   ? 107 ILE   A CA   1 ? 1 
ATOM   1253 C C    . ILE   A 1 95  ? -10.409 6.785   28.258  1   52.917  ? 107 ILE   A C    1 ? 1 
ATOM   1254 O O    . ILE   A 1 95  ? -9.524  6.409   27.48   1   52.545  ? 107 ILE   A O    1 ? 1 
ATOM   1255 C CB   . ILE   A 1 95  ? -10.135 9.242   27.958  1   41.866  ? 107 ILE   A CB   1 ? 1 
ATOM   1256 C CG1  . ILE   A 1 95  ? -9.881  10.578  28.631  1   46.757  ? 107 ILE   A CG1  1 ? 1 
ATOM   1257 C CG2  . ILE   A 1 95  ? -11.344 9.234   27.032  1   39.102  ? 107 ILE   A CG2  1 ? 1 
ATOM   1258 C CD1  . ILE   A 1 95  ? -9.514  11.683  27.664  1   47.872  ? 107 ILE   A CD1  1 ? 1 
ATOM   1259 H H    . ILE   A 1 95  ? -8.312  7.919   29.471  1   45.505  ? 107 ILE   A H    1 c 1 
ATOM   1260 H HA   . ILE   A 1 95  ? -11.085 8.291   29.508  1   45.178  ? 107 ILE   A HA   1 c 1 
ATOM   1261 H HB   . ILE   A 1 95  ? -9.347  9.038   27.415  1   42.947  ? 107 ILE   A HB   1 c 1 
ATOM   1262 H HG12 . ILE   A 1 95  ? -10.687 10.842  29.122  1   45.459  ? 107 ILE   A HG12 1 c 1 
ATOM   1263 H HG13 . ILE   A 1 95  ? -9.155  10.476  29.279  1   45.439  ? 107 ILE   A HG13 1 c 1 
ATOM   1264 H HG21 . ILE   A 1 95  ? -11.409 10.087  26.571  1   39.881  ? 107 ILE   A HG21 1 c 1 
ATOM   1265 H HG22 . ILE   A 1 95  ? -12.152 9.088   27.551  1   40.442  ? 107 ILE   A HG22 1 c 1 
ATOM   1266 H HG23 . ILE   A 1 95  ? -11.249 8.523   26.377  1   41.101  ? 107 ILE   A HG23 1 c 1 
ATOM   1267 H HD11 . ILE   A 1 95  ? -8.877  11.343  27.008  1   47.81   ? 107 ILE   A HD11 1 c 1 
ATOM   1268 H HD12 . ILE   A 1 95  ? -9.108  12.423  28.155  1   47.027  ? 107 ILE   A HD12 1 c 1 
ATOM   1269 H HD13 . ILE   A 1 95  ? -10.313 12.001  27.205  1   47.532  ? 107 ILE   A HD13 1 c 1 
ATOM   1270 N N    . LYS   A 1 96  ? -11.478 6.048   28.571  1   58.045  ? 108 LYS   A N    1 ? 1 
ATOM   1271 C CA   . LYS   A 1 96  ? -11.823 4.837   27.841  1   61.939  ? 108 LYS   A CA   1 ? 1 
ATOM   1272 C C    . LYS   A 1 96  ? -12.308 5.23    26.446  1   55.865  ? 108 LYS   A C    1 ? 1 
ATOM   1273 O O    . LYS   A 1 96  ? -12.84  6.329   26.25   1   54.305  ? 108 LYS   A O    1 ? 1 
ATOM   1274 C CB   . LYS   A 1 96  ? -12.943 4.09    28.592  1   63.932  ? 108 LYS   A CB   1 ? 1 
ATOM   1275 C CG   . LYS   A 1 96  ? -12.584 3.373   29.873  1   74.529  ? 108 LYS   A CG   1 ? 1 
ATOM   1276 C CD   . LYS   A 1 96  ? -11.367 2.438   29.856  1   84.428  ? 108 LYS   A CD   1 ? 1 
ATOM   1277 C CE   . LYS   A 1 96  ? -10.995 2.007   31.272  1   83.452  ? 108 LYS   A CE   1 ? 1 
ATOM   1278 N NZ   . LYS   A 1 96  ? -10.308 3.068   32.038  1   79.717  ? 108 LYS   A NZ   1 ? 1 
ATOM   1279 H H    . LYS   A 1 96  ? -12.011 6.308   29.267  1   57.146  ? 108 LYS   A H    1 c 1 
ATOM   1280 H HA   . LYS   A 1 96  ? -11.015 4.27    27.764  1   61.158  ? 108 LYS   A HA   1 c 1 
ATOM   1281 H HB2  . LYS   A 1 96  ? -13.649 4.738   28.8    1   65.24   ? 108 LYS   A HB2  1 c 1 
ATOM   1282 H HB3  . LYS   A 1 96  ? -13.33  3.43    27.979  1   67.373  ? 108 LYS   A HB3  1 c 1 
ATOM   1283 H HG2  . LYS   A 1 96  ? -12.437 4.054   30.565  1   72.654  ? 108 LYS   A HG2  1 c 1 
ATOM   1284 H HG3  . LYS   A 1 96  ? -13.367 2.851   30.153  1   75.439  ? 108 LYS   A HG3  1 c 1 
ATOM   1285 H HD2  . LYS   A 1 96  ? -11.575 1.642   29.319  1   83.596  ? 108 LYS   A HD2  1 c 1 
ATOM   1286 H HD3  . LYS   A 1 96  ? -10.603 2.898   29.448  1   80.446  ? 108 LYS   A HD3  1 c 1 
ATOM   1287 H HE2  . LYS   A 1 96  ? -11.804 1.75    31.751  1   84.567  ? 108 LYS   A HE2  1 c 1 
ATOM   1288 H HE3  . LYS   A 1 96  ? -10.414 1.227   31.227  1   85.126  ? 108 LYS   A HE3  1 c 1 
ATOM   1289 H HZ1  . LYS   A 1 96  ? -10.907 3.693   32.303  1   79.207  ? 108 LYS   A HZ1  1 c 1 
ATOM   1290 H HZ2  . LYS   A 1 96  ? -9.675  3.461   31.522  1   79.172  ? 108 LYS   A HZ2  1 c 1 
ATOM   1291 H HZ3  . LYS   A 1 96  ? -9.912  2.708   32.769  1   81.26   ? 108 LYS   A HZ3  1 c 1 
ATOM   1292 N N    . PRO   A 1 97  ? -12.21  4.312   25.463  1   59.819  ? 109 PRO   A N    1 ? 1 
ATOM   1293 C CA   . PRO   A 1 97  ? -12.556 4.591   24.066  1   56.702  ? 109 PRO   A CA   1 ? 1 
ATOM   1294 C C    . PRO   A 1 97  ? -13.991 5.018   23.756  1   56.991  ? 109 PRO   A C    1 ? 1 
ATOM   1295 O O    . PRO   A 1 97  ? -14.234 5.708   22.768  1   53.129  ? 109 PRO   A O    1 ? 1 
ATOM   1296 C CB   . PRO   A 1 97  ? -12.297 3.281   23.33   1   58.859  ? 109 PRO   A CB   1 ? 1 
ATOM   1297 C CG   . PRO   A 1 97  ? -12.082 2.256   24.411  1   62.814  ? 109 PRO   A CG   1 ? 1 
ATOM   1298 C CD   . PRO   A 1 97  ? -11.651 2.963   25.659  1   61.912  ? 109 PRO   A CD   1 ? 1 
ATOM   1299 H HA   . PRO   A 1 97  ? -11.943 5.271   23.72   1   56.125  ? 109 PRO   A HA   1 c 1 
ATOM   1300 H HB2  . PRO   A 1 97  ? -13.06  3.038   22.77   1   61.086  ? 109 PRO   A HB2  1 c 1 
ATOM   1301 H HB3  . PRO   A 1 97  ? -11.506 3.355   22.761  1   59.616  ? 109 PRO   A HB3  1 c 1 
ATOM   1302 H HG2  . PRO   A 1 97  ? -12.91  1.763   24.577  1   63.812  ? 109 PRO   A HG2  1 c 1 
ATOM   1303 H HG3  . PRO   A 1 97  ? -11.396 1.616   24.138  1   63.584  ? 109 PRO   A HG3  1 c 1 
ATOM   1304 H HD2  . PRO   A 1 97  ? -12.026 2.538   26.453  1   62.283  ? 109 PRO   A HD2  1 c 1 
ATOM   1305 H HD3  . PRO   A 1 97  ? -10.678 2.996   25.735  1   61.119  ? 109 PRO   A HD3  1 c 1 
ATOM   1306 N N    . GLU   A 1 98  ? -14.942 4.605   24.595  1   58.213  ? 110 GLU   A N    1 ? 1 
ATOM   1307 C CA   . GLU   A 1 98  ? -16.319 5.041   24.465  1   64.654  ? 110 GLU   A CA   1 ? 1 
ATOM   1308 C C    . GLU   A 1 98  ? -16.42  6.572   24.517  1   62.713  ? 110 GLU   A C    1 ? 1 
ATOM   1309 O O    . GLU   A 1 98  ? -17.324 7.139   23.893  1   63.944  ? 110 GLU   A O    1 ? 1 
ATOM   1310 C CB   . GLU   A 1 98  ? -17.162 4.267   25.487  1   66.978  ? 110 GLU   A CB   1 ? 1 
ATOM   1311 C CG   . GLU   A 1 98  ? -17.158 2.75    25.223  1   73.078  ? 110 GLU   A CG   1 ? 1 
ATOM   1312 C CD   . GLU   A 1 98  ? -16.02  1.879   25.79   1   77.242  ? 110 GLU   A CD   1 ? 1 
ATOM   1313 O OE1  . GLU   A 1 98  ? -15.217 2.417   26.568  1   74.218  ? 110 GLU   A OE1  1 ? 1 
ATOM   1314 O OE2  . GLU   A 1 98  ? -15.906 0.662   25.501  1   81.115  ? 110 GLU   A OE2  1 ? 1 
ATOM   1315 H H    . GLU   A 1 98  ? -14.719 4.044   25.28   1   59.645  ? 110 GLU   A H    1 c 1 
ATOM   1316 H HA   . GLU   A 1 98  ? -16.634 4.758   23.569  1   65.242  ? 110 GLU   A HA   1 c 1 
ATOM   1317 H HB2  . GLU   A 1 98  ? -16.816 4.445   26.386  1   66.277  ? 110 GLU   A HB2  1 c 1 
ATOM   1318 H HB3  . GLU   A 1 98  ? -18.085 4.596   25.451  1   68.375  ? 110 GLU   A HB3  1 c 1 
ATOM   1319 H HG2  . GLU   A 1 98  ? -18.003 2.384   25.562  1   74.973  ? 110 GLU   A HG2  1 c 1 
ATOM   1320 H HG3  . GLU   A 1 98  ? -17.175 2.613   24.252  1   74.145  ? 110 GLU   A HG3  1 c 1 
ATOM   1321 N N    . TYR   A 1 99  ? -15.493 7.237   25.24   1   54.331  ? 111 TYR   A N    1 ? 1 
ATOM   1322 C CA   . TYR   A 1 99  ? -15.497 8.687   25.367  1   57.335  ? 111 TYR   A CA   1 ? 1 
ATOM   1323 C C    . TYR   A 1 99  ? -14.418 9.3     24.462  1   50.503  ? 111 TYR   A C    1 ? 1 
ATOM   1324 O O    . TYR   A 1 99  ? -13.961 10.443  24.65   1   53.431  ? 111 TYR   A O    1 ? 1 
ATOM   1325 C CB   . TYR   A 1 99  ? -15.417 9.022   26.883  1   52.997  ? 111 TYR   A CB   1 ? 1 
ATOM   1326 C CG   . TYR   A 1 99  ? -16.66  8.565   27.654  1   57.573  ? 111 TYR   A CG   1 ? 1 
ATOM   1327 C CD1  . TYR   A 1 99  ? -17.862 9.277   27.659  1   64.056  ? 111 TYR   A CD1  1 ? 1 
ATOM   1328 C CD2  . TYR   A 1 99  ? -16.636 7.366   28.341  1   61.981  ? 111 TYR   A CD2  1 ? 1 
ATOM   1329 C CE1  . TYR   A 1 99  ? -18.985 8.819   28.345  1   64.561  ? 111 TYR   A CE1  1 ? 1 
ATOM   1330 C CE2  . TYR   A 1 99  ? -17.753 6.863   28.985  1   67.064  ? 111 TYR   A CE2  1 ? 1 
ATOM   1331 C CZ   . TYR   A 1 99  ? -18.92  7.602   29.01   1   70.316  ? 111 TYR   A CZ   1 ? 1 
ATOM   1332 O OH   . TYR   A 1 99  ? -19.92  7.03    29.728  1   61.498  ? 111 TYR   A OH   1 ? 1 
ATOM   1333 H H    . TYR   A 1 99  ? -14.846 6.765   25.681  1   56.219  ? 111 TYR   A H    1 c 1 
ATOM   1334 H HA   . TYR   A 1 99  ? -16.377 9.015   25.041  1   55.795  ? 111 TYR   A HA   1 c 1 
ATOM   1335 H HB2  . TYR   A 1 99  ? -14.623 8.585   27.262  1   53.766  ? 111 TYR   A HB2  1 c 1 
ATOM   1336 H HB3  . TYR   A 1 99  ? -15.314 9.994   26.986  1   53.429  ? 111 TYR   A HB3  1 c 1 
ATOM   1337 H HD1  . TYR   A 1 99  ? -17.909 10.103  27.204  1   62.098  ? 111 TYR   A HD1  1 c 1 
ATOM   1338 H HD2  . TYR   A 1 99  ? -15.85  6.844   28.321  1   61.46   ? 111 TYR   A HD2  1 c 1 
ATOM   1339 H HE1  . TYR   A 1 99  ? -19.782 9.321   28.348  1   66.837  ? 111 TYR   A HE1  1 c 1 
ATOM   1340 H HE2  . TYR   A 1 99  ? -17.698 6.053   29.461  1   67.433  ? 111 TYR   A HE2  1 c 1 
ATOM   1341 H HH   . TYR   A 1 99  ? -20.662 7.686   29.673  0   30      ? 111 TYR   A HH   1 c 1 
ATOM   1342 N N    . ALA   A 1 100 ? -13.957 8.549   23.476  1   53.047  ? 112 ALA   A N    1 ? 1 
ATOM   1343 C CA   . ALA   A 1 100 ? -12.831 9.009   22.676  1   48.882  ? 112 ALA   A CA   1 ? 1 
ATOM   1344 C C    . ALA   A 1 100 ? -13.064 8.627   21.224  1   57.982  ? 112 ALA   A C    1 ? 1 
ATOM   1345 O O    . ALA   A 1 100 ? -13.926 9.291   20.642  1   60.677  ? 112 ALA   A O    1 ? 1 
ATOM   1346 C CB   . ALA   A 1 100 ? -11.518 8.509   23.267  1   44.766  ? 112 ALA   A CB   1 ? 1 
ATOM   1347 H H    . ALA   A 1 100 ? -14.348 7.748   23.277  1   53.189  ? 112 ALA   A H    1 c 1 
ATOM   1348 H HA   . ALA   A 1 100 ? -12.822 10.003  22.715  1   49.572  ? 112 ALA   A HA   1 c 1 
ATOM   1349 H HB1  . ALA   A 1 100 ? -11.318 9.001   24.08   1   44.412  ? 112 ALA   A HB1  1 c 1 
ATOM   1350 H HB2  . ALA   A 1 100 ? -11.592 7.563   23.475  1   46.43   ? 112 ALA   A HB2  1 c 1 
ATOM   1351 H HB3  . ALA   A 1 100 ? -10.799 8.642   22.627  1   46.012  ? 112 ALA   A HB3  1 c 1 
ATOM   1352 N N    . TYR   A 1 101 ? -12.371 7.579   20.698  1   52.606  ? 113 TYR   A N    1 ? 1 
ATOM   1353 C CA   . TYR   A 1 101 ? -12.503 7.223   19.277  1   60.776  ? 113 TYR   A CA   1 ? 1 
ATOM   1354 C C    . TYR   A 1 101 ? -13.119 5.846   19.036  1   56.056  ? 113 TYR   A C    1 ? 1 
ATOM   1355 O O    . TYR   A 1 101 ? -13.173 5.365   17.936  1   55.587  ? 113 TYR   A O    1 ? 1 
ATOM   1356 C CB   . TYR   A 1 101 ? -11.168 7.31    18.525  1   56.098  ? 113 TYR   A CB   1 ? 1 
ATOM   1357 C CG   . TYR   A 1 101 ? -10.608 8.722   18.619  1   58.08   ? 113 TYR   A CG   1 ? 1 
ATOM   1358 C CD1  . TYR   A 1 101 ? -11.021 9.711   17.74   1   57.753  ? 113 TYR   A CD1  1 ? 1 
ATOM   1359 C CD2  . TYR   A 1 101 ? -9.677  9.078   19.593  1   57.998  ? 113 TYR   A CD2  1 ? 1 
ATOM   1360 C CE1  . TYR   A 1 101 ? -10.502 10.995  17.79   1   54.619  ? 113 TYR   A CE1  1 ? 1 
ATOM   1361 C CE2  . TYR   A 1 101 ? -9.177  10.367  19.673  1   57.272  ? 113 TYR   A CE2  1 ? 1 
ATOM   1362 C CZ   . TYR   A 1 101 ? -9.572  11.334  18.757  1   56.618  ? 113 TYR   A CZ   1 ? 1 
ATOM   1363 O OH   . TYR   A 1 101 ? -9.054  12.628  18.813  1   47.997  ? 113 TYR   A OH   1 ? 1 
ATOM   1364 H H    . TYR   A 1 101 ? -11.811 7.087   21.228  1   54.588  ? 113 TYR   A H    1 c 1 
ATOM   1365 H HA   . TYR   A 1 101 ? -13.112 7.89    18.864  1   57.838  ? 113 TYR   A HA   1 c 1 
ATOM   1366 H HB2  . TYR   A 1 101 ? -10.531 6.675   18.922  1   57.706  ? 113 TYR   A HB2  1 c 1 
ATOM   1367 H HB3  . TYR   A 1 101 ? -11.312 7.077   17.581  1   59.846  ? 113 TYR   A HB3  1 c 1 
ATOM   1368 H HD1  . TYR   A 1 101 ? -11.639 9.493   17.06   1   59.222  ? 113 TYR   A HD1  1 c 1 
ATOM   1369 H HD2  . TYR   A 1 101 ? -9.386  8.431   20.215  1   56.853  ? 113 TYR   A HD2  1 c 1 
ATOM   1370 H HE1  . TYR   A 1 101 ? -10.789 11.643  17.17   1   57.261  ? 113 TYR   A HE1  1 c 1 
ATOM   1371 H HE2  . TYR   A 1 101 ? -8.534  10.581  20.328  1   55.542  ? 113 TYR   A HE2  1 c 1 
ATOM   1372 H HH   . TYR   A 1 101 ? -9.397  13.108  18.202  0   30      ? 113 TYR   A HH   1 c 1 
ATOM   1373 N N    . GLY   A 1 102 ? -13.583 5.233   20.104  1   60.437  ? 114 GLY   A N    1 ? 1 
ATOM   1374 C CA   . GLY   A 1 102 ? -14.491 4.117   19.986  1   59.706  ? 114 GLY   A CA   1 ? 1 
ATOM   1375 C C    . GLY   A 1 102 ? -13.803 2.902   19.37   1   65.293  ? 114 GLY   A C    1 ? 1 
ATOM   1376 O O    . GLY   A 1 102 ? -12.578 2.89    19.118  1   62.288  ? 114 GLY   A O    1 ? 1 
ATOM   1377 H H    . GLY   A 1 102 ? -13.326 5.505   20.937  1   56.758  ? 114 GLY   A H    1 c 1 
ATOM   1378 H HA2  . GLY   A 1 102 ? -14.835 3.884   20.88   1   60.665  ? 114 GLY   A HA2  1 c 1 
ATOM   1379 H HA3  . GLY   A 1 102 ? -15.257 4.382   19.424  1   62.399  ? 114 GLY   A HA3  1 c 1 
ATOM   1380 N N    . SER   A 1 103 ? -14.635 1.898   19.106  1   65.098  ? 115 SER   A N    1 ? 1 
ATOM   1381 C CA   . SER   A 1 103 ? -14.155 0.693   18.472  1   73.245  ? 115 SER   A CA   1 ? 1 
ATOM   1382 C C    . SER   A 1 103 ? -13.604 0.968   17.06   1   67.811  ? 115 SER   A C    1 ? 1 
ATOM   1383 O O    . SER   A 1 103 ? -12.684 0.273   16.634  1   70.638  ? 115 SER   A O    1 ? 1 
ATOM   1384 C CB   . SER   A 1 103 ? -15.21  -0.393  18.524  1   80.654  ? 115 SER   A CB   1 ? 1 
ATOM   1385 O OG   . SER   A 1 103 ? -16.498 0.11    18.851  1   91.049  ? 115 SER   A OG   1 ? 1 
ATOM   1386 H H    . SER   A 1 103 ? -15.52  1.966   19.326  1   67.474  ? 115 SER   A H    1 c 1 
ATOM   1387 H HA   . SER   A 1 103 ? -13.39  0.373   19.016  1   70.71   ? 115 SER   A HA   1 c 1 
ATOM   1388 H HB2  . SER   A 1 103 ? -15.251 -0.841  17.658  1   84.388  ? 115 SER   A HB2  1 c 1 
ATOM   1389 H HB3  . SER   A 1 103 ? -14.948 -1.057  19.19   1   82.243  ? 115 SER   A HB3  1 c 1 
ATOM   1390 H HG   . SER   A 1 103 ? -17.046 -0.453  18.313  0   30      ? 115 SER   A HG   1 c 1 
ATOM   1391 N N    . ALA   A 1 104 ? -14.092 2.009   16.37   1   64.557  ? 116 ALA   A N    1 ? 1 
ATOM   1392 C CA   . ALA   A 1 104 ? -13.64  2.31    15.014  1   68.464  ? 116 ALA   A CA   1 ? 1 
ATOM   1393 C C    . ALA   A 1 104 ? -12.24  2.916   14.974  1   69.32   ? 116 ALA   A C    1 ? 1 
ATOM   1394 O O    . ALA   A 1 104 ? -11.622 2.986   13.918  1   69.399  ? 116 ALA   A O    1 ? 1 
ATOM   1395 C CB   . ALA   A 1 104 ? -14.597 3.272   14.367  1   71.028  ? 116 ALA   A CB   1 ? 1 
ATOM   1396 H H    . ALA   A 1 104 ? -14.732 2.541   16.748  1   64.739  ? 116 ALA   A H    1 c 1 
ATOM   1397 H HA   . ALA   A 1 104 ? -13.628 1.46    14.492  1   71.593  ? 116 ALA   A HA   1 c 1 
ATOM   1398 H HB1  . ALA   A 1 104 ? -15.49  2.888   14.355  1   72.103  ? 116 ALA   A HB1  1 c 1 
ATOM   1399 H HB2  . ALA   A 1 104 ? -14.613 4.105   14.868  1   68.079  ? 116 ALA   A HB2  1 c 1 
ATOM   1400 H HB3  . ALA   A 1 104 ? -14.314 3.453   13.455  1   72.041  ? 116 ALA   A HB3  1 c 1 
ATOM   1401 N N    . GLY   A 1 105 ? -11.83  3.516   16.103  1   71.493  ? 117 GLY   A N    1 ? 1 
ATOM   1402 C CA   . GLY   A 1 105 ? -10.559 4.21    16.186  1   63.126  ? 117 GLY   A CA   1 ? 1 
ATOM   1403 C C    . GLY   A 1 105 ? -10.566 5.424   15.273  1   60.743  ? 117 GLY   A C    1 ? 1 
ATOM   1404 O O    . GLY   A 1 105 ? -11.576 5.896   14.822  1   59.523  ? 117 GLY   A O    1 ? 1 
ATOM   1405 H H    . GLY   A 1 105 ? -12.366 3.498   16.843  1   67.241  ? 117 GLY   A H    1 c 1 
ATOM   1406 H HA2  . GLY   A 1 105 ? -10.401 4.493   17.117  1   61.677  ? 117 GLY   A HA2  1 c 1 
ATOM   1407 H HA3  . GLY   A 1 105 ? -9.834  3.597   15.921  1   65.206  ? 117 GLY   A HA3  1 c 1 
ATOM   1408 N N    . SER   A 1 106 ? -9.394  5.928   14.991  1   64.857  ? 118 SER   A N    1 ? 1 
ATOM   1409 C CA   . SER   A 1 106 ? -9.224  7.015   14.056  1   69.552  ? 118 SER   A CA   1 ? 1 
ATOM   1410 C C    . SER   A 1 106 ? -7.817  6.855   13.509  1   67.965  ? 118 SER   A C    1 ? 1 
ATOM   1411 O O    . SER   A 1 106 ? -6.925  7.632   13.821  1   62.281  ? 118 SER   A O    1 ? 1 
ATOM   1412 C CB   . SER   A 1 106 ? -9.448  8.386   14.715  1   75.195  ? 118 SER   A CB   1 ? 1 
ATOM   1413 O OG   . SER   A 1 106 ? -9.005  9.425   13.84   1   76.163  ? 118 SER   A OG   1 ? 1 
ATOM   1414 H H    . SER   A 1 106 ? -8.653  5.584   15.402  1   63.978  ? 118 SER   A H    1 c 1 
ATOM   1415 H HA   . SER   A 1 106 ? -9.869  6.903   13.312  1   71.435  ? 118 SER   A HA   1 c 1 
ATOM   1416 H HB2  . SER   A 1 106 ? -10.397 8.503   14.909  1   72.779  ? 118 SER   A HB2  1 c 1 
ATOM   1417 H HB3  . SER   A 1 106 ? -8.952  8.429   15.554  1   71.142  ? 118 SER   A HB3  1 c 1 
ATOM   1418 H HG   . SER   A 1 106 ? -9.062  10.157  14.159  0   30      ? 118 SER   A HG   1 c 1 
ATOM   1419 N N    . LEU   A 1 107 ? -7.659  5.767   12.747  1   78.525  ? 119 LEU   A N    1 ? 1 
ATOM   1420 C CA   . LEU   A 1 107 ? -6.429  5.432   12.049  1   81.403  ? 119 LEU   A CA   1 ? 1 
ATOM   1421 C C    . LEU   A 1 107 ? -6.051  6.563   11.101  1   77.934  ? 119 LEU   A C    1 ? 1 
ATOM   1422 O O    . LEU   A 1 107 ? -6.911  7.226   10.529  1   76.675  ? 119 LEU   A O    1 ? 1 
ATOM   1423 C CB   . LEU   A 1 107 ? -6.512  4.107   11.272  1   85.189  ? 119 LEU   A CB   1 ? 1 
ATOM   1424 C CG   . LEU   A 1 107 ? -6.839  2.861   12.1    1   85.597  ? 119 LEU   A CG   1 ? 1 
ATOM   1425 C CD1  . LEU   A 1 107 ? -6.925  1.72    11.157  1   85.742  ? 119 LEU   A CD1  1 ? 1 
ATOM   1426 C CD2  . LEU   A 1 107 ? -5.841  2.541   13.19   1   88.112  ? 119 LEU   A CD2  1 ? 1 
ATOM   1427 H H    . LEU   A 1 107 ? -8.371  5.201   12.653  1   77.447  ? 119 LEU   A H    1 c 1 
ATOM   1428 H HA   . LEU   A 1 107 ? -5.722  5.352   12.734  1   78.947  ? 119 LEU   A HA   1 c 1 
ATOM   1429 H HB2  . LEU   A 1 107 ? -7.2    4.206   10.575  1   86.899  ? 119 LEU   A HB2  1 c 1 
ATOM   1430 H HB3  . LEU   A 1 107 ? -5.652  3.96    10.816  1   87.061  ? 119 LEU   A HB3  1 c 1 
ATOM   1431 H HG   . LEU   A 1 107 ? -7.73   2.987   12.517  1   83.86   ? 119 LEU   A HG   1 c 1 
ATOM   1432 H HD11 . LEU   A 1 107 ? -7.507  1.953   10.414  1   88.321  ? 119 LEU   A HD11 1 c 1 
ATOM   1433 H HD12 . LEU   A 1 107 ? -7.286  0.945   11.619  1   86.959  ? 119 LEU   A HD12 1 c 1 
ATOM   1434 H HD13 . LEU   A 1 107 ? -6.038  1.511   10.819  1   88.559  ? 119 LEU   A HD13 1 c 1 
ATOM   1435 H HD21 . LEU   A 1 107 ? -5.823  3.265   13.837  1   83.932  ? 119 LEU   A HD21 1 c 1 
ATOM   1436 H HD22 . LEU   A 1 107 ? -4.958  2.434   12.8    1   88.372  ? 119 LEU   A HD22 1 c 1 
ATOM   1437 H HD23 . LEU   A 1 107 ? -6.099  1.718   13.635  1   87.13   ? 119 LEU   A HD23 1 c 1 
ATOM   1438 N N    . PRO   A 1 108 ? -4.745  6.748   10.847  1   78.992  ? 120 PRO   A N    1 ? 1 
ATOM   1439 C CA   . PRO   A 1 108 ? -3.711  5.935   11.471  1   78.667  ? 120 PRO   A CA   1 ? 1 
ATOM   1440 C C    . PRO   A 1 108 ? -3.219  6.392   12.839  1   73.665  ? 120 PRO   A C    1 ? 1 
ATOM   1441 O O    . PRO   A 1 108 ? -2.347  5.722   13.367  1   73.672  ? 120 PRO   A O    1 ? 1 
ATOM   1442 C CB   . PRO   A 1 108 ? -2.56   6.052   10.489  1   86.577  ? 120 PRO   A CB   1 ? 1 
ATOM   1443 C CG   . PRO   A 1 108 ? -2.723  7.51    10.066  1   86.604  ? 120 PRO   A CG   1 ? 1 
ATOM   1444 C CD   . PRO   A 1 108 ? -4.202  7.689   9.861   1   83.043  ? 120 PRO   A CD   1 ? 1 
ATOM   1445 H HA   . PRO   A 1 108 ? -3.997  5.003   11.518  1   79.99   ? 120 PRO   A HA   1 c 1 
ATOM   1446 H HB2  . PRO   A 1 108 ? -1.698  5.897   10.922  1   85.454  ? 120 PRO   A HB2  1 c 1 
ATOM   1447 H HB3  . PRO   A 1 108 ? -2.673  5.444   9.732   1   88.333  ? 120 PRO   A HB3  1 c 1 
ATOM   1448 H HG2  . PRO   A 1 108 ? -2.396  8.116   10.76   1   83.782  ? 120 PRO   A HG2  1 c 1 
ATOM   1449 H HG3  . PRO   A 1 108 ? -2.237  7.689   9.236   1   88.761  ? 120 PRO   A HG3  1 c 1 
ATOM   1450 H HD2  . PRO   A 1 108 ? -4.487  8.603   10.054  1   81.929  ? 120 PRO   A HD2  1 c 1 
ATOM   1451 H HD3  . PRO   A 1 108 ? -4.474  7.444   8.955   1   86.016  ? 120 PRO   A HD3  1 c 1 
ATOM   1452 N N    . LYS   A 1 109 ? -3.806  7.448   13.431  1   69.785  ? 121 LYS   A N    1 ? 1 
ATOM   1453 C CA   . LYS   A 1 109 ? -3.301  8.018   14.672  1   68.809  ? 121 LYS   A CA   1 ? 1 
ATOM   1454 C C    . LYS   A 1 109 ? -3.666  7.115   15.867  1   69.419  ? 121 LYS   A C    1 ? 1 
ATOM   1455 O O    . LYS   A 1 109 ? -2.796  6.751   16.664  1   68.95   ? 121 LYS   A O    1 ? 1 
ATOM   1456 C CB   . LYS   A 1 109 ? -3.79   9.477   14.803  1   70.836  ? 121 LYS   A CB   1 ? 1 
ATOM   1457 H H    . LYS   A 1 109 ? -4.547  7.82    13.049  1   70.596  ? 121 LYS   A H    1 c 1 
ATOM   1458 H HA   . LYS   A 1 109 ? -2.312  8.048   14.608  1   70.636  ? 121 LYS   A HA   1 c 1 
ATOM   1459 H HB2  . LYS   A 1 109 ? -3.029  10.052  14.871  0   30      ? 121 LYS   A HB2  1 c 1 
ATOM   1460 H HB3  . LYS   A 1 109 ? -4.78   9.433   14.805  0   30      ? 121 LYS   A HB3  1 c 1 
ATOM   1461 N N    . ILE   A 1 110 ? -4.952  6.755   15.993  1   59.721  ? 122 ILE   A N    1 ? 1 
ATOM   1462 C CA   . ILE   A 1 110 ? -5.49   6.046   17.138  1   56.564  ? 122 ILE   A CA   1 ? 1 
ATOM   1463 C C    . ILE   A 1 110 ? -6.004  4.67    16.71   1   59.805  ? 122 ILE   A C    1 ? 1 
ATOM   1464 O O    . ILE   A 1 110 ? -6.84   4.564   15.81   1   61.77   ? 122 ILE   A O    1 ? 1 
ATOM   1465 C CB   . ILE   A 1 110 ? -6.667  6.86    17.731  1   55.282  ? 122 ILE   A CB   1 ? 1 
ATOM   1466 C CG1  . ILE   A 1 110 ? -6.377  8.338   17.744  1   54.441  ? 122 ILE   A CG1  1 ? 1 
ATOM   1467 C CG2  . ILE   A 1 110 ? -7.049  6.349   19.11   1   51.443  ? 122 ILE   A CG2  1 ? 1 
ATOM   1468 C CD1  . ILE   A 1 110 ? -5.261  8.718   18.711  1   56.584  ? 122 ILE   A CD1  1 ? 1 
ATOM   1469 H H    . ILE   A 1 110 ? -5.527  6.968   15.314  1   62.217  ? 122 ILE   A H    1 c 1 
ATOM   1470 H HA   . ILE   A 1 110 ? -4.795  5.945   17.814  1   56.707  ? 122 ILE   A HA   1 c 1 
ATOM   1471 H HB   . ILE   A 1 110 ? -7.439  6.724   17.145  1   55.742  ? 122 ILE   A HB   1 c 1 
ATOM   1472 H HG12 . ILE   A 1 110 ? -6.13   8.627   16.842  1   56.721  ? 122 ILE   A HG12 1 c 1 
ATOM   1473 H HG13 . ILE   A 1 110 ? -7.192  8.817   17.999  1   54.043  ? 122 ILE   A HG13 1 c 1 
ATOM   1474 H HG21 . ILE   A 1 110 ? -7.608  7.005   19.558  1   50.524  ? 122 ILE   A HG21 1 c 1 
ATOM   1475 H HG22 . ILE   A 1 110 ? -6.246  6.198   19.636  1   51.716  ? 122 ILE   A HG22 1 c 1 
ATOM   1476 H HG23 . ILE   A 1 110 ? -7.539  5.514   19.024  1   53.046  ? 122 ILE   A HG23 1 c 1 
ATOM   1477 H HD11 . ILE   A 1 110 ? -5.6    8.7     19.626  1   53.81   ? 122 ILE   A HD11 1 c 1 
ATOM   1478 H HD12 . ILE   A 1 110 ? -4.948  9.618   18.501  1   55.492  ? 122 ILE   A HD12 1 c 1 
ATOM   1479 H HD13 . ILE   A 1 110 ? -4.518  8.091   18.63   1   56.554  ? 122 ILE   A HD13 1 c 1 
ATOM   1480 N N    . PRO   A 1 111 ? -5.568  3.56    17.342  1   60.646  ? 123 PRO   A N    1 ? 1 
ATOM   1481 C CA   . PRO   A 1 111 ? -6.138  2.245   17.043  1   61.292  ? 123 PRO   A CA   1 ? 1 
ATOM   1482 C C    . PRO   A 1 111 ? -7.518  2.024   17.638  1   55.838  ? 123 PRO   A C    1 ? 1 
ATOM   1483 O O    . PRO   A 1 111 ? -8.026  2.864   18.328  1   52.809  ? 123 PRO   A O    1 ? 1 
ATOM   1484 C CB   . PRO   A 1 111 ? -5.118  1.236   17.56   1   64.551  ? 123 PRO   A CB   1 ? 1 
ATOM   1485 C CG   . PRO   A 1 111 ? -4.338  2.032   18.6    1   67.08   ? 123 PRO   A CG   1 ? 1 
ATOM   1486 C CD   . PRO   A 1 111 ? -4.47   3.516   18.314  1   62.37   ? 123 PRO   A CD   1 ? 1 
ATOM   1487 H HA   . PRO   A 1 111 ? -6.199  2.144   16.07   1   63.025  ? 123 PRO   A HA   1 c 1 
ATOM   1488 H HB2  . PRO   A 1 111 ? -5.559  0.464   17.966  1   65.91   ? 123 PRO   A HB2  1 c 1 
ATOM   1489 H HB3  . PRO   A 1 111 ? -4.532  0.93    16.84   1   67.521  ? 123 PRO   A HB3  1 c 1 
ATOM   1490 H HG2  . PRO   A 1 111 ? -4.683  1.838   19.495  1   64.064  ? 123 PRO   A HG2  1 c 1 
ATOM   1491 H HG3  . PRO   A 1 111 ? -3.395  1.775   18.579  1   66.594  ? 123 PRO   A HG3  1 c 1 
ATOM   1492 H HD2  . PRO   A 1 111 ? -4.699  4.017   19.121  1   59.999  ? 123 PRO   A HD2  1 c 1 
ATOM   1493 H HD3  . PRO   A 1 111 ? -3.649  3.88    17.928  1   62.949  ? 123 PRO   A HD3  1 c 1 
ATOM   1494 N N    . SER   A 1 112 ? -8.175  0.956   17.22   1   60.493  ? 124 SER   A N    1 ? 1 
ATOM   1495 C CA   . SER   A 1 112 ? -9.485  0.578   17.738  1   61.573  ? 124 SER   A CA   1 ? 1 
ATOM   1496 C C    . SER   A 1 112 ? -9.413  0.466   19.244  1   58.305  ? 124 SER   A C    1 ? 1 
ATOM   1497 O O    . SER   A 1 112 ? -8.446  -0.047  19.797  1   62.087  ? 124 SER   A O    1 ? 1 
ATOM   1498 C CB   . SER   A 1 112 ? -9.936  -0.762  17.182  1   65.237  ? 124 SER   A CB   1 ? 1 
ATOM   1499 O OG   . SER   A 1 112 ? -10.773 -1.402  18.143  1   64.417  ? 124 SER   A OG   1 ? 1 
ATOM   1500 H H    . SER   A 1 112 ? -7.793  0.432   16.577  1   62.637  ? 124 SER   A H    1 c 1 
ATOM   1501 H HA   . SER   A 1 112 ? -10.144 1.276   17.492  1   60.168  ? 124 SER   A HA   1 c 1 
ATOM   1502 H HB2  . SER   A 1 112 ? -10.427 -0.627  16.35   1   66.402  ? 124 SER   A HB2  1 c 1 
ATOM   1503 H HB3  . SER   A 1 112 ? -9.159  -1.321  17      1   66.636  ? 124 SER   A HB3  1 c 1 
ATOM   1504 H HG   . SER   A 1 112 ? -10.968 -2.237  17.778  0   30      ? 124 SER   A HG   1 c 1 
ATOM   1505 N N    . ASN   A 1 113 ? -10.443 0.949   19.904  1   60.358  ? 125 ASN   A N    1 ? 1 
ATOM   1506 C CA   . ASN   A 1 113 ? -10.592 0.744   21.326  1   62.724  ? 125 ASN   A CA   1 ? 1 
ATOM   1507 C C    . ASN   A 1 113 ? -9.403  1.3     22.11   1   58.263  ? 125 ASN   A C    1 ? 1 
ATOM   1508 O O    . ASN   A 1 113 ? -9.027  0.711   23.11   1   66.198  ? 125 ASN   A O    1 ? 1 
ATOM   1509 C CB   . ASN   A 1 113 ? -10.77  -0.73   21.652  1   63.624  ? 125 ASN   A CB   1 ? 1 
ATOM   1510 C CG   . ASN   A 1 113 ? -12.182 -1.182  21.381  1   70.199  ? 125 ASN   A CG   1 ? 1 
ATOM   1511 O OD1  . ASN   A 1 113 ? -13.146 -0.488  21.701  1   76.426  ? 125 ASN   A OD1  1 ? 1 
ATOM   1512 N ND2  . ASN   A 1 113 ? -12.324 -2.324  20.738  1   76.716  ? 125 ASN   A ND2  1 ? 1 
ATOM   1513 H H    . ASN   A 1 113 ? -11.082 1.427   19.459  1   59.93   ? 125 ASN   A H    1 c 1 
ATOM   1514 H HA   . ASN   A 1 113 ? -11.402 1.216   21.619  1   60.188  ? 125 ASN   A HA   1 c 1 
ATOM   1515 H HB2  . ASN   A 1 113 ? -10.151 -1.263  21.116  1   66.892  ? 125 ASN   A HB2  1 c 1 
ATOM   1516 H HB3  . ASN   A 1 113 ? -10.564 -0.884  22.596  1   64.541  ? 125 ASN   A HB3  1 c 1 
ATOM   1517 H HD21 . ASN   A 1 113 ? -12.978 -2.421  20.148  1   77.269  ? 125 ASN   A HD21 1 c 1 
ATOM   1518 H HD22 . ASN   A 1 113 ? -11.765 -2.995  20.898  1   77.189  ? 125 ASN   A HD22 1 c 1 
ATOM   1519 N N    . ALA   A 1 114 ? -8.794  2.411   21.692  1   54.963  ? 126 ALA   A N    1 ? 1 
ATOM   1520 C CA   . ALA   A 1 114 ? -7.678  2.951   22.491  1   54.241  ? 126 ALA   A CA   1 ? 1 
ATOM   1521 C C    . ALA   A 1 114 ? -8.203  3.697   23.71   1   51.459  ? 126 ALA   A C    1 ? 1 
ATOM   1522 O O    . ALA   A 1 114 ? -9.157  4.45    23.559  1   51.71   ? 126 ALA   A O    1 ? 1 
ATOM   1523 C CB   . ALA   A 1 114 ? -6.798  3.877   21.685  1   50.95   ? 126 ALA   A CB   1 ? 1 
ATOM   1524 H H    . ALA   A 1 114 ? -9.06   2.839   20.93   1   55.598  ? 126 ALA   A H    1 c 1 
ATOM   1525 H HA   . ALA   A 1 114 ? -7.125  2.185   22.808  1   54.88   ? 126 ALA   A HA   1 c 1 
ATOM   1526 H HB1  . ALA   A 1 114 ? -6.481  3.417   20.89   1   53.584  ? 126 ALA   A HB1  1 c 1 
ATOM   1527 H HB2  . ALA   A 1 114 ? -7.306  4.662   21.42   1   50.666  ? 126 ALA   A HB2  1 c 1 
ATOM   1528 H HB3  . ALA   A 1 114 ? -6.036  4.154   22.222  1   51.043  ? 126 ALA   A HB3  1 c 1 
ATOM   1529 N N    . THR   A 1 115 ? -7.564  3.435   24.863  1   56.408  ? 127 THR   A N    1 ? 1 
ATOM   1530 C CA   . THR   A 1 115 ? -7.508  4.289   26.036  1   52.962  ? 127 THR   A CA   1 ? 1 
ATOM   1531 C C    . THR   A 1 115 ? -6.416  5.352   25.897  1   53.695  ? 127 THR   A C    1 ? 1 
ATOM   1532 O O    . THR   A 1 115 ? -5.266  5.057   25.582  1   56.208  ? 127 THR   A O    1 ? 1 
ATOM   1533 C CB   . THR   A 1 115 ? -7.243  3.457   27.3    1   53.966  ? 127 THR   A CB   1 ? 1 
ATOM   1534 O OG1  . THR   A 1 115 ? -8.302  2.518   27.395  1   52.39   ? 127 THR   A OG1  1 ? 1 
ATOM   1535 C CG2  . THR   A 1 115 ? -7.374  4.272   28.59   1   53.771  ? 127 THR   A CG2  1 ? 1 
ATOM   1536 H H    . THR   A 1 115 ? -7.123  2.636   24.914  1   56.313  ? 127 THR   A H    1 c 1 
ATOM   1537 H HA   . THR   A 1 115 ? -8.375  4.734   26.131  1   52.674  ? 127 THR   A HA   1 c 1 
ATOM   1538 H HB   . THR   A 1 115 ? -6.374  2.991   27.253  1   54.829  ? 127 THR   A HB   1 c 1 
ATOM   1539 H HG1  . THR   A 1 115 ? -9.126  2.9     27.405  0   30      ? 127 THR   A HG1  1 c 1 
ATOM   1540 H HG21 . THR   A 1 115 ? -7.115  3.721   29.348  1   54.362  ? 127 THR   A HG21 1 c 1 
ATOM   1541 H HG22 . THR   A 1 115 ? -8.295  4.56    28.701  1   52.598  ? 127 THR   A HG22 1 c 1 
ATOM   1542 H HG23 . THR   A 1 115 ? -6.795  5.051   28.546  1   52.277  ? 127 THR   A HG23 1 c 1 
ATOM   1543 N N    . LEU   A 1 116 ? -6.781  6.584   26.274  1   58.844  ? 128 LEU   A N    1 ? 1 
ATOM   1544 C CA   . LEU   A 1 116 ? -5.975  7.784   26.109  1   52.945  ? 128 LEU   A CA   1 ? 1 
ATOM   1545 C C    . LEU   A 1 116 ? -5.838  8.445   27.479  1   52.843  ? 128 LEU   A C    1 ? 1 
ATOM   1546 O O    . LEU   A 1 116 ? -6.763  8.429   28.32   1   50.505  ? 128 LEU   A O    1 ? 1 
ATOM   1547 C CB   . LEU   A 1 116 ? -6.589  8.846   25.188  1   50.562  ? 128 LEU   A CB   1 ? 1 
ATOM   1548 C CG   . LEU   A 1 116 ? -7.149  8.422   23.827  1   52.217  ? 128 LEU   A CG   1 ? 1 
ATOM   1549 C CD1  . LEU   A 1 116 ? -7.139  9.636   22.925  1   52.484  ? 128 LEU   A CD1  1 ? 1 
ATOM   1550 C CD2  . LEU   A 1 116 ? -6.358  7.332   23.264  1   52.427  ? 128 LEU   A CD2  1 ? 1 
ATOM   1551 H H    . LEU   A 1 116 ? -7.599  6.68    26.669  1   55.187  ? 128 LEU   A H    1 c 1 
ATOM   1552 H HA   . LEU   A 1 116 ? -5.078  7.529   25.775  1   54.574  ? 128 LEU   A HA   1 c 1 
ATOM   1553 H HB2  . LEU   A 1 116 ? -7.313  9.292   25.685  1   50.111  ? 128 LEU   A HB2  1 c 1 
ATOM   1554 H HB3  . LEU   A 1 116 ? -5.904  9.537   25.033  1   50.967  ? 128 LEU   A HB3  1 c 1 
ATOM   1555 H HG   . LEU   A 1 116 ? -8.085  8.116   23.948  1   51.808  ? 128 LEU   A HG   1 c 1 
ATOM   1556 H HD11 . LEU   A 1 116 ? -7.6    10.371  23.363  1   51.412  ? 128 LEU   A HD11 1 c 1 
ATOM   1557 H HD12 . LEU   A 1 116 ? -7.589  9.423   22.091  1   53.349  ? 128 LEU   A HD12 1 c 1 
ATOM   1558 H HD13 . LEU   A 1 116 ? -6.22   9.895   22.74   1   52.806  ? 128 LEU   A HD13 1 c 1 
ATOM   1559 H HD21 . LEU   A 1 116 ? -6.697  6.482   23.588  1   53.483  ? 128 LEU   A HD21 1 c 1 
ATOM   1560 H HD22 . LEU   A 1 116 ? -5.427  7.431   23.527  1   53.097  ? 128 LEU   A HD22 1 c 1 
ATOM   1561 H HD23 . LEU   A 1 116 ? -6.42   7.353   22.294  1   53.907  ? 128 LEU   A HD23 1 c 1 
ATOM   1562 N N    . PHE   A 1 117 ? -4.696  9.116   27.609  1   45.134  ? 129 PHE   A N    1 ? 1 
ATOM   1563 C CA   . PHE   A 1 117 ? -4.359  9.931   28.742  1   42.999  ? 129 PHE   A CA   1 ? 1 
ATOM   1564 C C    . PHE   A 1 117 ? -4.03   11.328  28.242  1   47.199  ? 129 PHE   A C    1 ? 1 
ATOM   1565 O O    . PHE   A 1 117 ? -3.396  11.502  27.19   1   48.475  ? 129 PHE   A O    1 ? 1 
ATOM   1566 C CB   . PHE   A 1 117 ? -3.187  9.274   29.46   1   45.997  ? 129 PHE   A CB   1 ? 1 
ATOM   1567 C CG   . PHE   A 1 117 ? -2.598  10.183  30.521  1   54.878  ? 129 PHE   A CG   1 ? 1 
ATOM   1568 C CD1  . PHE   A 1 117 ? -1.657  11.147  30.186  1   57.356  ? 129 PHE   A CD1  1 ? 1 
ATOM   1569 C CD2  . PHE   A 1 117 ? -3.045  10.123  31.852  1   59.353  ? 129 PHE   A CD2  1 ? 1 
ATOM   1570 C CE1  . PHE   A 1 117 ? -1.146  11.999  31.165  1   65.762  ? 129 PHE   A CE1  1 ? 1 
ATOM   1571 C CE2  . PHE   A 1 117 ? -2.51   10.961  32.84   1   53.57   ? 129 PHE   A CE2  1 ? 1 
ATOM   1572 C CZ   . PHE   A 1 117 ? -1.59   11.913  32.492  1   59.013  ? 129 PHE   A CZ   1 ? 1 
ATOM   1573 H H    . PHE   A 1 117 ? -4.085  9.057   26.932  1   47.341  ? 129 PHE   A H    1 c 1 
ATOM   1574 H HA   . PHE   A 1 117 ? -5.136  9.974   29.357  1   43.805  ? 129 PHE   A HA   1 c 1 
ATOM   1575 H HB2  . PHE   A 1 117 ? -3.497  8.442   29.882  1   47.886  ? 129 PHE   A HB2  1 c 1 
ATOM   1576 H HB3  . PHE   A 1 117 ? -2.492  9.053   28.801  1   48.449  ? 129 PHE   A HB3  1 c 1 
ATOM   1577 H HD1  . PHE   A 1 117 ? -1.358  11.221  29.294  1   58.846  ? 129 PHE   A HD1  1 c 1 
ATOM   1578 H HD2  . PHE   A 1 117 ? -3.685  9.473   32.094  1   56.633  ? 129 PHE   A HD2  1 c 1 
ATOM   1579 H HE1  . PHE   A 1 117 ? -0.498  12.643  30.929  1   62.784  ? 129 PHE   A HE1  1 c 1 
ATOM   1580 H HE2  . PHE   A 1 117 ? -2.818  10.901  33.73   1   56.144  ? 129 PHE   A HE2  1 c 1 
ATOM   1581 H HZ   . PHE   A 1 117 ? -1.227  12.484  33.15   1   59.691  ? 129 PHE   A HZ   1 c 1 
ATOM   1582 N N    . PHE   A 1 118 ? -4.465  12.322  29.018  1   45.717  ? 130 PHE   A N    1 ? 1 
ATOM   1583 C CA   . PHE   A 1 118 ? -4.088  13.712  28.814  1   45.096  ? 130 PHE   A CA   1 ? 1 
ATOM   1584 C C    . PHE   A 1 118 ? -3.762  14.427  30.119  1   46.241  ? 130 PHE   A C    1 ? 1 
ATOM   1585 O O    . PHE   A 1 118 ? -4.438  14.201  31.139  1   45.441  ? 130 PHE   A O    1 ? 1 
ATOM   1586 C CB   . PHE   A 1 118 ? -5.265  14.51   28.25   1   45.713  ? 130 PHE   A CB   1 ? 1 
ATOM   1587 C CG   . PHE   A 1 118 ? -5.622  14.168  26.815  1   53.864  ? 130 PHE   A CG   1 ? 1 
ATOM   1588 C CD1  . PHE   A 1 118 ? -6.509  13.141  26.539  1   49.055  ? 130 PHE   A CD1  1 ? 1 
ATOM   1589 C CD2  . PHE   A 1 118 ? -5.035  14.86   25.763  1   50.871  ? 130 PHE   A CD2  1 ? 1 
ATOM   1590 C CE1  . PHE   A 1 118 ? -6.798  12.828  25.239  1   50.479  ? 130 PHE   A CE1  1 ? 1 
ATOM   1591 C CE2  . PHE   A 1 118 ? -5.363  14.537  24.461  1   53.1    ? 130 PHE   A CE2  1 ? 1 
ATOM   1592 C CZ   . PHE   A 1 118 ? -6.226  13.517  24.212  1   48.537  ? 130 PHE   A CZ   1 ? 1 
ATOM   1593 H H    . PHE   A 1 118 ? -5.027  12.125  29.711  1   45.159  ? 130 PHE   A H    1 c 1 
ATOM   1594 H HA   . PHE   A 1 118 ? -3.317  13.766  28.193  1   46.587  ? 130 PHE   A HA   1 c 1 
ATOM   1595 H HB2  . PHE   A 1 118 ? -6.051  14.35   28.819  1   46.348  ? 130 PHE   A HB2  1 c 1 
ATOM   1596 H HB3  . PHE   A 1 118 ? -5.047  15.467  28.302  1   47.393  ? 130 PHE   A HB3  1 c 1 
ATOM   1597 H HD1  . PHE   A 1 118 ? -6.9    12.651  27.245  1   49.62   ? 130 PHE   A HD1  1 c 1 
ATOM   1598 H HD2  . PHE   A 1 118 ? -4.431  15.564  25.939  1   52.626  ? 130 PHE   A HD2  1 c 1 
ATOM   1599 H HE1  . PHE   A 1 118 ? -7.407  12.131  25.052  1   49.659  ? 130 PHE   A HE1  1 c 1 
ATOM   1600 H HE2  . PHE   A 1 118 ? -4.968  15.008  23.745  1   52.853  ? 130 PHE   A HE2  1 c 1 
ATOM   1601 H HZ   . PHE   A 1 118 ? -6.449  13.3    23.321  1   50.959  ? 130 PHE   A HZ   1 c 1 
ATOM   1602 N N    . GLU   A 1 119 ? -2.817  15.366  30.025  1   46.191  ? 131 GLU   A N    1 ? 1 
ATOM   1603 C CA   . GLU   A 1 119 ? -2.622  16.426  31.011  1   48.811  ? 131 GLU   A CA   1 ? 1 
ATOM   1604 C C    . GLU   A 1 119 ? -3.095  17.724  30.373  1   51.781  ? 131 GLU   A C    1 ? 1 
ATOM   1605 O O    . GLU   A 1 119 ? -2.672  18.05   29.256  1   49.69   ? 131 GLU   A O    1 ? 1 
ATOM   1606 C CB   . GLU   A 1 119 ? -1.157  16.578  31.393  1   50.733  ? 131 GLU   A CB   1 ? 1 
ATOM   1607 C CG   . GLU   A 1 119 ? -0.927  17.636  32.457  1   56.262  ? 131 GLU   A CG   1 ? 1 
ATOM   1608 C CD   . GLU   A 1 119 ? 0.511   17.628  32.948  1   56.847  ? 131 GLU   A CD   1 ? 1 
ATOM   1609 O OE1  . GLU   A 1 119 ? 0.762   17.192  34.064  1   56.591  ? 131 GLU   A OE1  1 ? 1 
ATOM   1610 O OE2  . GLU   A 1 119 ? 1.377   18.146  32.225  1   64.469  ? 131 GLU   A OE2  1 ? 1 
ATOM   1611 H H    . GLU   A 1 119 ? -2.256  15.346  29.303  1   47.654  ? 131 GLU   A H    1 c 1 
ATOM   1612 H HA   . GLU   A 1 119 ? -3.166  16.228  31.812  1   48.299  ? 131 GLU   A HA   1 c 1 
ATOM   1613 H HB2  . GLU   A 1 119 ? -0.825  15.716  31.721  1   51.888  ? 131 GLU   A HB2  1 c 1 
ATOM   1614 H HB3  . GLU   A 1 119 ? -0.643  16.811  30.592  1   52.525  ? 131 GLU   A HB3  1 c 1 
ATOM   1615 H HG2  . GLU   A 1 119 ? -1.13   18.522  32.088  1   55.059  ? 131 GLU   A HG2  1 c 1 
ATOM   1616 H HG3  . GLU   A 1 119 ? -1.525  17.475  33.217  1   53.993  ? 131 GLU   A HG3  1 c 1 
ATOM   1617 N N    . ILE   A 1 120 ? -4.049  18.394  31.036  1   54.631  ? 132 ILE   A N    1 ? 1 
ATOM   1618 C CA   . ILE   A 1 120 ? -4.679  19.563  30.456  1   56.828  ? 132 ILE   A CA   1 ? 1 
ATOM   1619 C C    . ILE   A 1 120 ? -4.516  20.724  31.422  1   54.243  ? 132 ILE   A C    1 ? 1 
ATOM   1620 O O    . ILE   A 1 120 ? -4.885  20.592  32.599  1   45.777  ? 132 ILE   A O    1 ? 1 
ATOM   1621 C CB   . ILE   A 1 120 ? -6.167  19.376  30.165  1   56.41   ? 132 ILE   A CB   1 ? 1 
ATOM   1622 C CG1  . ILE   A 1 120 ? -6.418  18.163  29.314  1   57.458  ? 132 ILE   A CG1  1 ? 1 
ATOM   1623 C CG2  . ILE   A 1 120 ? -6.712  20.658  29.524  1   63.221  ? 132 ILE   A CG2  1 ? 1 
ATOM   1624 C CD1  . ILE   A 1 120 ? -7.874  17.957  28.979  1   53.215  ? 132 ILE   A CD1  1 ? 1 
ATOM   1625 H H    . ILE   A 1 120 ? -4.309  18.116  31.867  1   53.681  ? 132 ILE   A H    1 c 1 
ATOM   1626 H HA   . ILE   A 1 120 ? -4.226  19.782  29.62   1   56.389  ? 132 ILE   A HA   1 c 1 
ATOM   1627 H HB   . ILE   A 1 120 ? -6.627  19.244  31.018  1   57.066  ? 132 ILE   A HB   1 c 1 
ATOM   1628 H HG12 . ILE   A 1 120 ? -5.911  18.251  28.481  1   56.711  ? 132 ILE   A HG12 1 c 1 
ATOM   1629 H HG13 . ILE   A 1 120 ? -6.088  17.371  29.785  1   55.561  ? 132 ILE   A HG13 1 c 1 
ATOM   1630 H HG21 . ILE   A 1 120 ? -7.658  20.551  29.329  1   61.075  ? 132 ILE   A HG21 1 c 1 
ATOM   1631 H HG22 . ILE   A 1 120 ? -6.232  20.839  28.698  1   62.271  ? 132 ILE   A HG22 1 c 1 
ATOM   1632 H HG23 . ILE   A 1 120 ? -6.595  21.406  30.133  1   62.368  ? 132 ILE   A HG23 1 c 1 
ATOM   1633 H HD11 . ILE   A 1 120 ? -8.423  18.183  29.753  1   54.157  ? 132 ILE   A HD11 1 c 1 
ATOM   1634 H HD12 . ILE   A 1 120 ? -8.024  17.023  28.738  1   53.678  ? 132 ILE   A HD12 1 c 1 
ATOM   1635 H HD13 . ILE   A 1 120 ? -8.123  18.528  28.228  1   55.05   ? 132 ILE   A HD13 1 c 1 
ATOM   1636 N N    . GLU   A 1 121 ? -3.968  21.822  30.877  1   51.521  ? 133 GLU   A N    1 ? 1 
ATOM   1637 C CA   . GLU   A 1 121 ? -3.973  23.095  31.58   1   58.204  ? 133 GLU   A CA   1 ? 1 
ATOM   1638 C C    . GLU   A 1 121 ? -5.023  24.019  30.947  1   57.72   ? 133 GLU   A C    1 ? 1 
ATOM   1639 O O    . GLU   A 1 121 ? -4.872  24.433  29.788  1   61.202  ? 133 GLU   A O    1 ? 1 
ATOM   1640 C CB   . GLU   A 1 121 ? -2.566  23.688  31.629  1   57.942  ? 133 GLU   A CB   1 ? 1 
ATOM   1641 C CG   . GLU   A 1 121 ? -2.438  24.877  32.585  1   62.66   ? 133 GLU   A CG   1 ? 1 
ATOM   1642 C CD   . GLU   A 1 121 ? -1.086  25.568  32.604  1   66.307  ? 133 GLU   A CD   1 ? 1 
ATOM   1643 O OE1  . GLU   A 1 121 ? -0.14   25.029  31.965  1   65.529  ? 133 GLU   A OE1  1 ? 1 
ATOM   1644 O OE2  . GLU   A 1 121 ? -0.996  26.648  33.263  1   68.002  ? 133 GLU   A OE2  1 ? 1 
ATOM   1645 H H    . GLU   A 1 121 ? -3.579  21.776  30.051  1   54.135  ? 133 GLU   A H    1 c 1 
ATOM   1646 H HA   . GLU   A 1 121 ? -4.241  22.923  32.514  1   55.902  ? 133 GLU   A HA   1 c 1 
ATOM   1647 H HB2  . GLU   A 1 121 ? -1.938  22.988  31.906  1   58.629  ? 133 GLU   A HB2  1 c 1 
ATOM   1648 H HB3  . GLU   A 1 121 ? -2.313  23.976  30.727  1   59.956  ? 133 GLU   A HB3  1 c 1 
ATOM   1649 H HG2  . GLU   A 1 121 ? -3.118  25.544  32.35   1   62.815  ? 133 GLU   A HG2  1 c 1 
ATOM   1650 H HG3  . GLU   A 1 121 ? -2.638  24.571  33.495  1   61.575  ? 133 GLU   A HG3  1 c 1 
ATOM   1651 N N    . LEU   A 1 122 ? -6.07   24.334  31.721  1   51.873  ? 134 LEU   A N    1 ? 1 
ATOM   1652 C CA   . LEU   A 1 122 ? -7.019  25.361  31.353  1   56.405  ? 134 LEU   A CA   1 ? 1 
ATOM   1653 C C    . LEU   A 1 122 ? -6.431  26.772  31.547  1   63.003  ? 134 LEU   A C    1 ? 1 
ATOM   1654 O O    . LEU   A 1 122 ? -6.317  27.28   32.658  1   69.859  ? 134 LEU   A O    1 ? 1 
ATOM   1655 C CB   . LEU   A 1 122 ? -8.275  25.161  32.191  1   56.405  ? 134 LEU   A CB   1 ? 1 
ATOM   1656 C CG   . LEU   A 1 122 ? -9.438  26.103  31.82   1   58.823  ? 134 LEU   A CG   1 ? 1 
ATOM   1657 C CD1  . LEU   A 1 122 ? -9.692  26.13   30.321  1   56.266  ? 134 LEU   A CD1  1 ? 1 
ATOM   1658 C CD2  . LEU   A 1 122 ? -10.696 25.692  32.521  1   57.415  ? 134 LEU   A CD2  1 ? 1 
ATOM   1659 H H    . LEU   A 1 122 ? -6.194  23.886  32.508  1   52.996  ? 134 LEU   A H    1 c 1 
ATOM   1660 H HA   . LEU   A 1 122 ? -7.246  25.241  30.398  1   56.437  ? 134 LEU   A HA   1 c 1 
ATOM   1661 H HB2  . LEU   A 1 122 ? -8.578  24.231  32.08   1   54.454  ? 134 LEU   A HB2  1 c 1 
ATOM   1662 H HB3  . LEU   A 1 122 ? -8.044  25.304  33.138  1   56.768  ? 134 LEU   A HB3  1 c 1 
ATOM   1663 H HG   . LEU   A 1 122 ? -9.204  27.021  32.114  1   60.149  ? 134 LEU   A HG   1 c 1 
ATOM   1664 H HD11 . LEU   A 1 122 ? -9.037  26.704  29.89   1   58.586  ? 134 LEU   A HD11 1 c 1 
ATOM   1665 H HD12 . LEU   A 1 122 ? -10.584 26.474  30.149  1   58.169  ? 134 LEU   A HD12 1 c 1 
ATOM   1666 H HD13 . LEU   A 1 122 ? -9.618  25.229  29.962  1   55.271  ? 134 LEU   A HD13 1 c 1 
ATOM   1667 H HD21 . LEU   A 1 122 ? -10.499 25.493  33.452  1   57.18   ? 134 LEU   A HD21 1 c 1 
ATOM   1668 H HD22 . LEU   A 1 122 ? -11.063 24.9    32.093  1   56.023  ? 134 LEU   A HD22 1 c 1 
ATOM   1669 H HD23 . LEU   A 1 122 ? -11.345 26.414  32.476  1   59.37   ? 134 LEU   A HD23 1 c 1 
ATOM   1670 N N    . LEU   A 1 123 ? -6.039  27.414  30.447  1   65.363  ? 135 LEU   A N    1 ? 1 
ATOM   1671 C CA   . LEU   A 1 123 ? -5.369  28.703  30.482  1   71.85   ? 135 LEU   A CA   1 ? 1 
ATOM   1672 C C    . LEU   A 1 123 ? -6.421  29.796  30.67   1   78.895  ? 135 LEU   A C    1 ? 1 
ATOM   1673 O O    . LEU   A 1 123 ? -6.236  30.655  31.522  1   87.261  ? 135 LEU   A O    1 ? 1 
ATOM   1674 C CB   . LEU   A 1 123 ? -4.557  28.972  29.211  1   72.602  ? 135 LEU   A CB   1 ? 1 
ATOM   1675 C CG   . LEU   A 1 123 ? -3.565  27.888  28.771  1   74.244  ? 135 LEU   A CG   1 ? 1 
ATOM   1676 C CD1  . LEU   A 1 123 ? -2.928  28.272  27.436  1   79.88   ? 135 LEU   A CD1  1 ? 1 
ATOM   1677 C CD2  . LEU   A 1 123 ? -2.481  27.581  29.79   1   77.236  ? 135 LEU   A CD2  1 ? 1 
ATOM   1678 H H    . LEU   A 1 123 ? -6.199  27.031  29.633  1   65.108  ? 135 LEU   A H    1 c 1 
ATOM   1679 H HA   . LEU   A 1 123 ? -4.758  28.716  31.262  1   72.215  ? 135 LEU   A HA   1 c 1 
ATOM   1680 H HB2  . LEU   A 1 123 ? -5.191  29.126  28.473  1   74.054  ? 135 LEU   A HB2  1 c 1 
ATOM   1681 H HB3  . LEU   A 1 123 ? -4.059  29.811  29.341  1   76.39   ? 135 LEU   A HB3  1 c 1 
ATOM   1682 H HG   . LEU   A 1 123 ? -4.077  27.052  28.623  1   72.071  ? 135 LEU   A HG   1 c 1 
ATOM   1683 H HD11 . LEU   A 1 123 ? -3.607  28.635  26.843  1   79.636  ? 135 LEU   A HD11 1 c 1 
ATOM   1684 H HD12 . LEU   A 1 123 ? -2.532  27.484  27.027  1   77.475  ? 135 LEU   A HD12 1 c 1 
ATOM   1685 H HD13 . LEU   A 1 123 ? -2.238  28.94   27.585  1   81.409  ? 135 LEU   A HD13 1 c 1 
ATOM   1686 H HD21 . LEU   A 1 123 ? -2.889  27.262  30.612  1   74.765  ? 135 LEU   A HD21 1 c 1 
ATOM   1687 H HD22 . LEU   A 1 123 ? -1.97   28.387  29.974  1   78.933  ? 135 LEU   A HD22 1 c 1 
ATOM   1688 H HD23 . LEU   A 1 123 ? -1.888  26.897  29.437  1   75.449  ? 135 LEU   A HD23 1 c 1 
ATOM   1689 N N    . ASP   A 1 124 ? -7.493  29.773  29.856  1   77.282  ? 136 ASP   A N    1 ? 1 
ATOM   1690 C CA   . ASP   A 1 124 ? -8.473  30.844  29.843  1   82.01   ? 136 ASP   A CA   1 ? 1 
ATOM   1691 C C    . ASP   A 1 124 ? -9.757  30.353  29.181  1   81.973  ? 136 ASP   A C    1 ? 1 
ATOM   1692 O O    . ASP   A 1 124 ? -9.751  29.403  28.392  1   80.122  ? 136 ASP   A O    1 ? 1 
ATOM   1693 C CB   . ASP   A 1 124 ? -7.932  32.089  29.147  1   87.405  ? 136 ASP   A CB   1 ? 1 
ATOM   1694 C CG   . ASP   A 1 124 ? -8.64   33.366  29.554  1   95.107  ? 136 ASP   A CG   1 ? 1 
ATOM   1695 O OD1  . ASP   A 1 124 ? -9.356  33.325  30.588  1   95.842  ? 136 ASP   A OD1  1 ? 1 
ATOM   1696 O OD2  . ASP   A 1 124 ? -8.538  34.351  28.797  1   103.154 ? 136 ASP   A OD2  1 ? 1 
ATOM   1697 H H    . ASP   A 1 124 ? -7.608  29.065  29.289  1   76.139  ? 136 ASP   A H    1 c 1 
ATOM   1698 H HA   . ASP   A 1 124 ? -8.678  31.078  30.776  1   82.443  ? 136 ASP   A HA   1 c 1 
ATOM   1699 H HB2  . ASP   A 1 124 ? -6.979  32.188  29.352  1   88.488  ? 136 ASP   A HB2  1 c 1 
ATOM   1700 H HB3  . ASP   A 1 124 ? -8.023  31.98   28.177  1   88.268  ? 136 ASP   A HB3  1 c 1 
ATOM   1701 N N    . PHE   A 1 125 ? -10.867 31.026  29.496  1   80.017  ? 137 PHE   A N    1 ? 1 
ATOM   1702 C CA   . PHE   A 1 125 ? -12.088 30.831  28.726  1   76.1    ? 137 PHE   A CA   1 ? 1 
ATOM   1703 C C    . PHE   A 1 125 ? -12.883 32.129  28.683  1   79.356  ? 137 PHE   A C    1 ? 1 
ATOM   1704 O O    . PHE   A 1 125 ? -12.834 32.891  29.647  1   82.647  ? 137 PHE   A O    1 ? 1 
ATOM   1705 C CB   . PHE   A 1 125 ? -12.892 29.673  29.295  1   69.973  ? 137 PHE   A CB   1 ? 1 
ATOM   1706 C CG   . PHE   A 1 125 ? -13.322 29.82   30.742  1   72.976  ? 137 PHE   A CG   1 ? 1 
ATOM   1707 C CD1  . PHE   A 1 125 ? -14.558 30.366  31.075  1   75.737  ? 137 PHE   A CD1  1 ? 1 
ATOM   1708 C CD2  . PHE   A 1 125 ? -12.509 29.365  31.776  1   69.87   ? 137 PHE   A CD2  1 ? 1 
ATOM   1709 C CE1  . PHE   A 1 125 ? -14.965 30.478  32.407  1   76.76   ? 137 PHE   A CE1  1 ? 1 
ATOM   1710 C CE2  . PHE   A 1 125 ? -12.945 29.441  33.099  1   75.733  ? 137 PHE   A CE2  1 ? 1 
ATOM   1711 C CZ   . PHE   A 1 125 ? -14.175 29.997  33.415  1   74.515  ? 137 PHE   A CZ   1 ? 1 
ATOM   1712 H H    . PHE   A 1 125 ? -10.869 31.61   30.199  1   81.505  ? 137 PHE   A H    1 c 1 
ATOM   1713 H HA   . PHE   A 1 125 ? -11.83  30.598  27.796  1   75.986  ? 137 PHE   A HA   1 c 1 
ATOM   1714 H HB2  . PHE   A 1 125 ? -13.696 29.555  28.741  1   71.8    ? 137 PHE   A HB2  1 c 1 
ATOM   1715 H HB3  . PHE   A 1 125 ? -12.355 28.854  29.21   1   68.625  ? 137 PHE   A HB3  1 c 1 
ATOM   1716 H HD1  . PHE   A 1 125 ? -15.123 30.683  30.388  1   77.587  ? 137 PHE   A HD1  1 c 1 
ATOM   1717 H HD2  . PHE   A 1 125 ? -11.681 28.959  31.576  1   69.798  ? 137 PHE   A HD2  1 c 1 
ATOM   1718 H HE1  . PHE   A 1 125 ? -15.808 30.853  32.609  1   78.621  ? 137 PHE   A HE1  1 c 1 
ATOM   1719 H HE2  . PHE   A 1 125 ? -12.382 29.136  33.792  1   72.342  ? 137 PHE   A HE2  1 c 1 
ATOM   1720 H HZ   . PHE   A 1 125 ? -14.444 30.082  34.316  1   75.901  ? 137 PHE   A HZ   1 c 1 
ATOM   1721 N N    . LYS   A 1 126 ? -13.561 32.373  27.546  1   80.372  ? 138 LYS   A N    1 ? 1 
ATOM   1722 C CA   . LYS   A 1 126 ? -14.313 33.597  27.268  1   86.278  ? 138 LYS   A CA   1 ? 1 
ATOM   1723 C C    . LYS   A 1 126 ? -15.688 33.189  26.731  1   86.823  ? 138 LYS   A C    1 ? 1 
ATOM   1724 O O    . LYS   A 1 126 ? -15.828 32.133  26.132  1   80.145  ? 138 LYS   A O    1 ? 1 
ATOM   1725 C CB   . LYS   A 1 126 ? -13.531 34.53   26.322  1   85.369  ? 138 LYS   A CB   1 ? 1 
ATOM   1726 H H    . LYS   A 1 126 ? -13.552 31.726  26.899  1   79.225  ? 138 LYS   A H    1 c 1 
ATOM   1727 H HA   . LYS   A 1 126 ? -14.447 34.077  28.124  1   86.448  ? 138 LYS   A HA   1 c 1 
ATOM   1728 H HB2  . LYS   A 1 126 ? -12.641 34.365  26.478  0   30      ? 138 LYS   A HB2  1 c 1 
ATOM   1729 H HB3  . LYS   A 1 126 ? -14.268 34.96   25.806  0   30      ? 138 LYS   A HB3  1 c 1 
ATOM   1730 N N    . GLY   A 1 127 ? -16.715 34.005  27.003  1   97.417  ? 139 GLY   A N    1 ? 1 
ATOM   1731 C CA   . GLY   A 1 127 ? -18.073 33.723  26.553  1   103.124 ? 139 GLY   A CA   1 ? 1 
ATOM   1732 C C    . GLY   A 1 127 ? -18.209 33.938  25.044  1   109.638 ? 139 GLY   A C    1 ? 1 
ATOM   1733 O O    . GLY   A 1 127 ? -17.541 34.814  24.505  1   113.471 ? 139 GLY   A O    1 ? 1 
ATOM   1734 H H    . GLY   A 1 127 ? -16.564 34.766  27.486  1   98.763  ? 139 GLY   A H    1 c 1 
ATOM   1735 H HA2  . GLY   A 1 127 ? -18.302 32.793  26.778  1   99.375  ? 139 GLY   A HA2  1 c 1 
ATOM   1736 H HA3  . GLY   A 1 127 ? -18.701 34.316  27.029  1   105.528 ? 139 GLY   A HA3  1 c 1 
ATOM   1737 N N    . GLU   A 1 128 ? -19.045 33.13   24.356  1   110.232 ? 140 GLU   A N    1 ? 1 
ATOM   1738 C CA   . GLU   A 1 128 ? -19.241 33.285  22.916  1   107.565 ? 140 GLU   A CA   1 ? 1 
ATOM   1739 C C    . GLU   A 1 128 ? -19.502 34.792  22.68   1   110.442 ? 140 GLU   A C    1 ? 1 
ATOM   1740 O O    . GLU   A 1 128 ? -20.183 35.435  23.535  1   107.185 ? 140 GLU   A O    1 ? 1 
ATOM   1741 C CB   . GLU   A 1 128 ? -20.252 32.3    22.296  1   102.808 ? 140 GLU   A CB   1 ? 1 
ATOM   1742 O OXT  . GLU   A 1 128 ? -18.926 35.302  21.708  1   112.424 ? 140 GLU   A OXT  1 ? 1 
ATOM   1743 H H    . GLU   A 1 128 ? -19.5   32.471  24.798  1   106.282 ? 140 GLU   A H    1 c 1 
ATOM   1744 H HA   . GLU   A 1 128 ? -18.374 33.074  22.484  1   105.521 ? 140 GLU   A HA   1 c 1 
ATOM   1745 H HB2  . GLU   A 1 128 ? -19.544 31.699  21.758  0   30      ? 140 GLU   A HB2  1 c 1 
ATOM   1746 H HB3  . GLU   A 1 128 ? -20.966 32.707  22.397  0   30      ? 140 GLU   A HB3  1 c 1 
ATOM   1747 N N    . GLY   B 1 1   ? -16.259 -15.453 -6.62   1   87.496  ? 13  GLY   B N    1 ? 2 
ATOM   1748 C CA   . GLY   B 1 1   ? -16.986 -14.864 -5.48   1   83.277  ? 13  GLY   B CA   1 ? 2 
ATOM   1749 C C    . GLY   B 1 1   ? -17.063 -13.352 -5.624  1   78.131  ? 13  GLY   B C    1 ? 2 
ATOM   1750 O O    . GLY   B 1 1   ? -16.272 -12.738 -6.343  1   76.384  ? 13  GLY   B O    1 ? 2 
ATOM   1751 H H1   . GLY   B 1 1   ? -16.224 -16.354 -6.533  1   90.187  ? 13  GLY   B H1   1 c 2 
ATOM   1752 H H2   . GLY   B 1 1   ? -15.414 -15.129 -6.65   1   85.247  ? 13  GLY   B H2   1 c 2 
ATOM   1753 H H3   . GLY   B 1 1   ? -16.68  -15.25  -7.395  1   89.318  ? 13  GLY   B H3   1 c 2 
ATOM   1754 H HA2  . GLY   B 1 1   ? -17.896 -15.242 -5.444  1   85.877  ? 13  GLY   B HA2  1 c 2 
ATOM   1755 H HA3  . GLY   B 1 1   ? -16.524 -15.097 -4.641  1   81.544  ? 13  GLY   B HA3  1 c 2 
ATOM   1756 N N    . ALA   B 1 2   ? -17.986 -12.746 -4.89   1   75.551  ? 14  ALA   B N    1 ? 2 
ATOM   1757 C CA   . ALA   B 1 2   ? -18.253 -11.32  -5.015  1   69.501  ? 14  ALA   B CA   1 ? 2 
ATOM   1758 C C    . ALA   B 1 2   ? -17.058 -10.406 -4.684  1   65.342  ? 14  ALA   B C    1 ? 2 
ATOM   1759 O O    . ALA   B 1 2   ? -16.975 -9.281  -5.231  1   61.4    ? 14  ALA   B O    1 ? 2 
ATOM   1760 C CB   . ALA   B 1 2   ? -19.442 -11.019 -4.138  1   70.257  ? 14  ALA   B CB   1 ? 2 
ATOM   1761 H H    . ALA   B 1 2   ? -18.47  -13.235 -4.288  1   76.015  ? 14  ALA   B H    1 c 2 
ATOM   1762 H HA   . ALA   B 1 2   ? -18.509 -11.145 -5.963  1   72.569  ? 14  ALA   B HA   1 c 2 
ATOM   1763 H HB1  . ALA   B 1 2   ? -20.219 -11.502 -4.465  1   73.409  ? 14  ALA   B HB1  1 c 2 
ATOM   1764 H HB2  . ALA   B 1 2   ? -19.256 -11.292 -3.225  1   68.522  ? 14  ALA   B HB2  1 c 2 
ATOM   1765 H HB3  . ALA   B 1 2   ? -19.627 -10.065 -4.156  1   67.984  ? 14  ALA   B HB3  1 c 2 
ATOM   1766 N N    . PRO   B 1 3   ? -16.194 -10.776 -3.7    1   60.145  ? 15  PRO   B N    1 ? 2 
ATOM   1767 C CA   . PRO   B 1 3   ? -14.94  -10.061 -3.412  1   58.444  ? 15  PRO   B CA   1 ? 2 
ATOM   1768 C C    . PRO   B 1 3   ? -13.835 -10.138 -4.479  1   61.671  ? 15  PRO   B C    1 ? 2 
ATOM   1769 O O    . PRO   B 1 3   ? -13.129 -9.162  -4.733  1   64.489  ? 15  PRO   B O    1 ? 2 
ATOM   1770 C CB   . PRO   B 1 3   ? -14.339 -10.729 -2.184  1   56.106  ? 15  PRO   B CB   1 ? 2 
ATOM   1771 C CG   . PRO   B 1 3   ? -15.411 -11.668 -1.681  1   59.365  ? 15  PRO   B CG   1 ? 2 
ATOM   1772 C CD   . PRO   B 1 3   ? -16.456 -11.859 -2.752  1   62.69   ? 15  PRO   B CD   1 ? 2 
ATOM   1773 H HA   . PRO   B 1 3   ? -15.139 -9.122  -3.213  1   56.074  ? 15  PRO   B HA   1 c 2 
ATOM   1774 H HB2  . PRO   B 1 3   ? -13.529 -11.224 -2.415  1   57.528  ? 15  PRO   B HB2  1 c 2 
ATOM   1775 H HB3  . PRO   B 1 3   ? -14.114 -10.065 -1.503  1   53.975  ? 15  PRO   B HB3  1 c 2 
ATOM   1776 H HG2  . PRO   B 1 3   ? -15.017 -12.531 -1.447  1   60.733  ? 15  PRO   B HG2  1 c 2 
ATOM   1777 H HG3  . PRO   B 1 3   ? -15.828 -11.298 -0.877  1   57.705  ? 15  PRO   B HG3  1 c 2 
ATOM   1778 H HD2  . PRO   B 1 3   ? -16.354 -12.727 -3.181  1   65.395  ? 15  PRO   B HD2  1 c 2 
ATOM   1779 H HD3  . PRO   B 1 3   ? -17.355 -11.786 -2.381  1   62.939  ? 15  PRO   B HD3  1 c 2 
ATOM   1780 N N    . ALA   B 1 4   ? -13.667 -11.308 -5.091  1   63.638  ? 16  ALA   B N    1 ? 2 
ATOM   1781 C CA   . ALA   B 1 4   ? -12.721 -11.487 -6.175  1   66.239  ? 16  ALA   B CA   1 ? 2 
ATOM   1782 C C    . ALA   B 1 4   ? -13.032 -10.526 -7.322  1   65.158  ? 16  ALA   B C    1 ? 2 
ATOM   1783 O O    . ALA   B 1 4   ? -12.157 -9.792  -7.754  1   64.514  ? 16  ALA   B O    1 ? 2 
ATOM   1784 C CB   . ALA   B 1 4   ? -12.794 -12.921 -6.673  1   73.487  ? 16  ALA   B CB   1 ? 2 
ATOM   1785 H H    . ALA   B 1 4   ? -14.16  -12.027 -4.817  1   65.593  ? 16  ALA   B H    1 c 2 
ATOM   1786 H HA   . ALA   B 1 4   ? -11.804 -11.295 -5.835  1   64.661  ? 16  ALA   B HA   1 c 2 
ATOM   1787 H HB1  . ALA   B 1 4   ? -12.504 -13.526 -5.97   1   72.507  ? 16  ALA   B HB1  1 c 2 
ATOM   1788 H HB2  . ALA   B 1 4   ? -13.708 -13.136 -6.924  1   74.505  ? 16  ALA   B HB2  1 c 2 
ATOM   1789 H HB3  . ALA   B 1 4   ? -12.216 -13.028 -7.447  1   74.903  ? 16  ALA   B HB3  1 c 2 
ATOM   1790 N N    . THR   B 1 5   ? -14.278 -10.583 -7.795  1   63.622  ? 17  THR   B N    1 ? 2 
ATOM   1791 C CA   . THR   B 1 5   ? -14.869 -9.634  -8.724  1   63.62   ? 17  THR   B CA   1 ? 2 
ATOM   1792 C C    . THR   B 1 5   ? -14.625 -8.177  -8.304  1   59.175  ? 17  THR   B C    1 ? 2 
ATOM   1793 O O    . THR   B 1 5   ? -14.498 -7.293  -9.145  1   58.396  ? 17  THR   B O    1 ? 2 
ATOM   1794 C CB   . THR   B 1 5   ? -16.358 -9.988  -8.896  1   65.978  ? 17  THR   B CB   1 ? 2 
ATOM   1795 O OG1  . THR   B 1 5   ? -16.459 -11.309 -9.477  1   71.289  ? 17  THR   B OG1  1 ? 2 
ATOM   1796 C CG2  . THR   B 1 5   ? -17.115 -9.016  -9.8    1   67.608  ? 17  THR   B CG2  1 ? 2 
ATOM   1797 H H    . THR   B 1 5   ? -14.805 -11.273 -7.509  1   65.452  ? 17  THR   B H    1 c 2 
ATOM   1798 H HA   . THR   B 1 5   ? -14.433 -9.768  -9.593  1   66.498  ? 17  THR   B HA   1 c 2 
ATOM   1799 H HB   . THR   B 1 5   ? -16.792 -9.993  -8.01   1   63.874  ? 17  THR   B HB   1 c 2 
ATOM   1800 H HG1  . THR   B 1 5   ? -16.007 -11.3   -10.27  0   30      ? 17  THR   B HG1  1 c 2 
ATOM   1801 H HG21 . THR   B 1 5   ? -17.945 -9.426  -10.095 1   70.724  ? 17  THR   B HG21 1 c 2 
ATOM   1802 H HG22 . THR   B 1 5   ? -16.568 -8.8    -10.575 1   69.315  ? 17  THR   B HG22 1 c 2 
ATOM   1803 H HG23 . THR   B 1 5   ? -17.314 -8.201  -9.308  1   64.783  ? 17  THR   B HG23 1 c 2 
ATOM   1804 N N    . VAL   B 1 6   ? -14.477 -7.878  -7.025  1   56.04   ? 18  VAL   B N    1 ? 2 
ATOM   1805 C CA   . VAL   B 1 6   ? -14.165 -6.499  -6.664  1   54.762  ? 18  VAL   B CA   1 ? 2 
ATOM   1806 C C    . VAL   B 1 6   ? -12.699 -6.196  -6.924  1   55.968  ? 18  VAL   B C    1 ? 2 
ATOM   1807 O O    . VAL   B 1 6   ? -12.388 -5.127  -7.448  1   53.105  ? 18  VAL   B O    1 ? 2 
ATOM   1808 C CB   . VAL   B 1 6   ? -14.52  -6.141  -5.22   1   51.164  ? 18  VAL   B CB   1 ? 2 
ATOM   1809 C CG1  . VAL   B 1 6   ? -14.105 -4.708  -4.841  1   46.664  ? 18  VAL   B CG1  1 ? 2 
ATOM   1810 C CG2  . VAL   B 1 6   ? -16.012 -6.356  -5.073  1   53.879  ? 18  VAL   B CG2  1 ? 2 
ATOM   1811 H H    . VAL   B 1 6   ? -14.59  -8.506  -6.373  1   55.675  ? 18  VAL   B H    1 c 2 
ATOM   1812 H HA   . VAL   B 1 6   ? -14.691 -5.918  -7.242  1   55.862  ? 18  VAL   B HA   1 c 2 
ATOM   1813 H HB   . VAL   B 1 6   ? -14.049 -6.773  -4.63   1   50.342  ? 18  VAL   B HB   1 c 2 
ATOM   1814 H HG11 . VAL   B 1 6   ? -14.323 -4.103  -5.57   1   48.459  ? 18  VAL   B HG11 1 c 2 
ATOM   1815 H HG12 . VAL   B 1 6   ? -13.149 -4.679  -4.673  1   46.469  ? 18  VAL   B HG12 1 c 2 
ATOM   1816 H HG13 . VAL   B 1 6   ? -14.582 -4.433  -4.04   1   45.518  ? 18  VAL   B HG13 1 c 2 
ATOM   1817 H HG21 . VAL   B 1 6   ? -16.283 -6.138  -4.166  1   51.44   ? 18  VAL   B HG21 1 c 2 
ATOM   1818 H HG22 . VAL   B 1 6   ? -16.227 -7.282  -5.259  1   55.355  ? 18  VAL   B HG22 1 c 2 
ATOM   1819 H HG23 . VAL   B 1 6   ? -16.486 -5.783  -5.699  1   54.575  ? 18  VAL   B HG23 1 c 2 
ATOM   1820 N N    . THR   B 1 7   ? -11.823 -7.077  -6.428  1   60.671  ? 19  THR   B N    1 ? 2 
ATOM   1821 C CA   . THR   B 1 7   ? -10.403 -6.977  -6.702  1   63.12   ? 19  THR   B CA   1 ? 2 
ATOM   1822 C C    . THR   B 1 7   ? -10.26  -6.751  -8.203  1   72.457  ? 19  THR   B C    1 ? 2 
ATOM   1823 O O    . THR   B 1 7   ? -9.51   -5.886  -8.643  1   79.888  ? 19  THR   B O    1 ? 2 
ATOM   1824 C CB   . THR   B 1 7   ? -9.678  -8.22   -6.181  1   65.537  ? 19  THR   B CB   1 ? 2 
ATOM   1825 O OG1  . THR   B 1 7   ? -9.44   -7.977  -4.787  1   59.02   ? 19  THR   B OG1  1 ? 2 
ATOM   1826 C CG2  . THR   B 1 7   ? -8.385  -8.435  -6.95   1   69.17   ? 19  THR   B CG2  1 ? 2 
ATOM   1827 H H    . THR   B 1 7   ? -12.124 -7.757  -5.895  1   59.322  ? 19  THR   B H    1 c 2 
ATOM   1828 H HA   . THR   B 1 7   ? -10.053 -6.19   -6.23   1   61.962  ? 19  THR   B HA   1 c 2 
ATOM   1829 H HB   . THR   B 1 7   ? -10.252 -9.017  -6.281  1   65.972  ? 19  THR   B HB   1 c 2 
ATOM   1830 H HG1  . THR   B 1 7   ? -9.068  -7.262  -4.75   0   30      ? 19  THR   B HG1  1 c 2 
ATOM   1831 H HG21 . THR   B 1 7   ? -7.813  -9.047  -6.457  1   69.11   ? 19  THR   B HG21 1 c 2 
ATOM   1832 H HG22 . THR   B 1 7   ? -7.925  -7.585  -7.061  1   68.493  ? 19  THR   B HG22 1 c 2 
ATOM   1833 H HG23 . THR   B 1 7   ? -8.583  -8.813  -7.824  1   71.959  ? 19  THR   B HG23 1 c 2 
ATOM   1834 N N    . GLU   B 1 8   ? -11.101 -7.432  -8.983  1   75.983  ? 20  GLU   B N    1 ? 2 
ATOM   1835 C CA   . GLU   B 1 8   ? -10.868 -7.568  -10.41  1   80.508  ? 20  GLU   B CA   1 ? 2 
ATOM   1836 C C    . GLU   B 1 8   ? -11.475 -6.423  -11.21  1   79.079  ? 20  GLU   B C    1 ? 2 
ATOM   1837 O O    . GLU   B 1 8   ? -11.014 -6.202  -12.291 1   74.488  ? 20  GLU   B O    1 ? 2 
ATOM   1838 C CB   . GLU   B 1 8   ? -11.418 -8.875  -10.98  1   88.299  ? 20  GLU   B CB   1 ? 2 
ATOM   1839 C CG   . GLU   B 1 8   ? -10.521 -10.077 -10.691 1   93.576  ? 20  GLU   B CG   1 ? 2 
ATOM   1840 C CD   . GLU   B 1 8   ? -11.116 -11.425 -11.079 1   103.838 ? 20  GLU   B CD   1 ? 2 
ATOM   1841 O OE1  . GLU   B 1 8   ? -12.112 -11.413 -11.856 1   100.066 ? 20  GLU   B OE1  1 ? 2 
ATOM   1842 O OE2  . GLU   B 1 8   ? -10.598 -12.476 -10.583 1   104.601 ? 20  GLU   B OE2  1 ? 2 
ATOM   1843 H H    . GLU   B 1 8   ? -11.828 -7.846  -8.617  1   74.839  ? 20  GLU   B H    1 c 2 
ATOM   1844 H HA   . GLU   B 1 8   ? -9.888  -7.564  -10.562 1   81.634  ? 20  GLU   B HA   1 c 2 
ATOM   1845 H HB2  . GLU   B 1 8   ? -12.306 -9.037  -10.6   1   87.204  ? 20  GLU   B HB2  1 c 2 
ATOM   1846 H HB3  . GLU   B 1 8   ? -11.519 -8.783  -11.95  1   91.721  ? 20  GLU   B HB3  1 c 2 
ATOM   1847 H HG2  . GLU   B 1 8   ? -9.674  -9.963  -11.171 1   95.673  ? 20  GLU   B HG2  1 c 2 
ATOM   1848 H HG3  . GLU   B 1 8   ? -10.315 -10.095 -9.732  1   90.444  ? 20  GLU   B HG3  1 c 2 
ATOM   1849 N N    . GLN   B 1 9   ? -12.52  -5.745  -10.722 1   78.79   ? 21  GLN   B N    1 ? 2 
ATOM   1850 C CA   . GLN   B 1 9   ? -13.257 -4.769  -11.527 1   85.058  ? 21  GLN   B CA   1 ? 2 
ATOM   1851 C C    . GLN   B 1 9   ? -13.444 -3.458  -10.764 1   80.425  ? 21  GLN   B C    1 ? 2 
ATOM   1852 O O    . GLN   B 1 9   ? -13.902 -2.455  -11.33  1   83.124  ? 21  GLN   B O    1 ? 2 
ATOM   1853 C CB   . GLN   B 1 9   ? -14.737 -5.102  -11.758 1   93.562  ? 21  GLN   B CB   1 ? 2 
ATOM   1854 C CG   . GLN   B 1 9   ? -15.069 -6.55   -12.103 1   94.163  ? 21  GLN   B CG   1 ? 2 
ATOM   1855 C CD   . GLN   B 1 9   ? -14.66  -6.868  -13.501 1   95.186  ? 21  GLN   B CD   1 ? 2 
ATOM   1856 O OE1  . GLN   B 1 9   ? -15.104 -6.189  -14.428 1   104.021 ? 21  GLN   B OE1  1 ? 2 
ATOM   1857 N NE2  . GLN   B 1 9   ? -13.772 -7.842  -13.632 1   98.706  ? 21  GLN   B NE2  1 ? 2 
ATOM   1858 H H    . GLN   B 1 9   ? -12.816 -5.932  -9.878  1   76.247  ? 21  GLN   B H    1 c 2 
ATOM   1859 H HA   . GLN   B 1 9   ? -12.782 -4.602  -12.38  1   88.172  ? 21  GLN   B HA   1 c 2 
ATOM   1860 H HB2  . GLN   B 1 9   ? -15.232 -4.861  -10.949 1   87.967  ? 21  GLN   B HB2  1 c 2 
ATOM   1861 H HB3  . GLN   B 1 9   ? -15.068 -4.528  -12.48  1   93.765  ? 21  GLN   B HB3  1 c 2 
ATOM   1862 H HG2  . GLN   B 1 9   ? -14.605 -7.152  -11.486 1   91.217  ? 21  GLN   B HG2  1 c 2 
ATOM   1863 H HG3  . GLN   B 1 9   ? -16.034 -6.698  -12.006 1   94.079  ? 21  GLN   B HG3  1 c 2 
ATOM   1864 H HE21 . GLN   B 1 9   ? -13.046 -7.716  -14.125 1   99.793  ? 21  GLN   B HE21 1 c 2 
ATOM   1865 H HE22 . GLN   B 1 9   ? -13.906 -8.62   -13.227 1   97.684  ? 21  GLN   B HE22 1 c 2 
ATOM   1866 N N    . GLY   B 1 10  ? -13.159 -3.529  -9.462  1   67.597  ? 22  GLY   B N    1 ? 2 
ATOM   1867 C CA   . GLY   B 1 10  ? -13.558 -2.496  -8.549  1   65.499  ? 22  GLY   B CA   1 ? 2 
ATOM   1868 C C    . GLY   B 1 10  ? -12.914 -1.188  -8.947  1   63.629  ? 22  GLY   B C    1 ? 2 
ATOM   1869 O O    . GLY   B 1 10  ? -11.739 -1.192  -9.287  1   63.263  ? 22  GLY   B O    1 ? 2 
ATOM   1870 H H    . GLY   B 1 10  ? -12.676 -4.232  -9.138  1   69.083  ? 22  GLY   B H    1 c 2 
ATOM   1871 H HA2  . GLY   B 1 10  ? -14.54  -2.408  -8.564  1   64.864  ? 22  GLY   B HA2  1 c 2 
ATOM   1872 H HA3  . GLY   B 1 10  ? -13.283 -2.739  -7.634  1   61.745  ? 22  GLY   B HA3  1 c 2 
ATOM   1873 N N    . GLU   B 1 11  ? -13.712 -0.117  -8.82   1   63.029  ? 23  GLU   B N    1 ? 2 
ATOM   1874 C CA   . GLU   B 1 11  ? -13.272 1.275   -8.826  1   63.744  ? 23  GLU   B CA   1 ? 2 
ATOM   1875 C C    . GLU   B 1 11  ? -12.468 1.512   -7.54   1   54.507  ? 23  GLU   B C    1 ? 2 
ATOM   1876 O O    . GLU   B 1 11  ? -12.903 1.144   -6.457  1   52.797  ? 23  GLU   B O    1 ? 2 
ATOM   1877 C CB   . GLU   B 1 11  ? -14.584 2.032   -9.125  1   68.143  ? 23  GLU   B CB   1 ? 2 
ATOM   1878 C CG   . GLU   B 1 11  ? -14.515 3.509   -9.543  1   73.497  ? 23  GLU   B CG   1 ? 2 
ATOM   1879 C CD   . GLU   B 1 11  ? -15.742 4.442   -9.338  1   75.417  ? 23  GLU   B CD   1 ? 2 
ATOM   1880 O OE1  . GLU   B 1 11  ? -16.773 4.183   -8.666  1   79.169  ? 23  GLU   B OE1  1 ? 2 
ATOM   1881 O OE2  . GLU   B 1 11  ? -15.693 5.555   -9.87   1   84.356  ? 23  GLU   B OE2  1 ? 2 
ATOM   1882 H H    . GLU   B 1 11  ? -14.606 -0.275  -8.712  1   63.183  ? 23  GLU   B H    1 c 2 
ATOM   1883 H HA   . GLU   B 1 11  ? -12.666 1.4     -9.6    1   65.598  ? 23  GLU   B HA   1 c 2 
ATOM   1884 H HB2  . GLU   B 1 11  ? -15.053 1.56    -9.845  1   70.426  ? 23  GLU   B HB2  1 c 2 
ATOM   1885 H HB3  . GLU   B 1 11  ? -15.152 1.984   -8.328  1   65.707  ? 23  GLU   B HB3  1 c 2 
ATOM   1886 H HG2  . GLU   B 1 11  ? -13.757 3.918   -9.072  1   71.802  ? 23  GLU   B HG2  1 c 2 
ATOM   1887 H HG3  . GLU   B 1 11  ? -14.283 3.539   -10.496 1   76.439  ? 23  GLU   B HG3  1 c 2 
ATOM   1888 N N    . ASP   B 1 12  ? -11.244 2.034   -7.673  1   52.843  ? 24  ASP   B N    1 ? 2 
ATOM   1889 C CA   . ASP   B 1 12  ? -10.438 2.461   -6.547  1   51.91   ? 24  ASP   B CA   1 ? 2 
ATOM   1890 C C    . ASP   B 1 12  ? -11.005 3.799   -6.148  1   51.535  ? 24  ASP   B C    1 ? 2 
ATOM   1891 O O    . ASP   B 1 12  ? -10.806 4.735   -6.895  1   54.268  ? 24  ASP   B O    1 ? 2 
ATOM   1892 C CB   . ASP   B 1 12  ? -8.956  2.615   -6.883  1   53.651  ? 24  ASP   B CB   1 ? 2 
ATOM   1893 C CG   . ASP   B 1 12  ? -8.058  3.01    -5.694  1   55.152  ? 24  ASP   B CG   1 ? 2 
ATOM   1894 O OD1  . ASP   B 1 12  ? -8.597  3.358   -4.618  1   54.672  ? 24  ASP   B OD1  1 ? 2 
ATOM   1895 O OD2  . ASP   B 1 12  ? -6.812  2.964   -5.811  1   56.896  ? 24  ASP   B OD2  1 ? 2 
ATOM   1896 H H    . ASP   B 1 12  ? -10.896 2.127   -8.513  1   56.696  ? 24  ASP   B H    1 c 2 
ATOM   1897 H HA   . ASP   B 1 12  ? -10.55  1.823   -5.808  1   49.083  ? 24  ASP   B HA   1 c 2 
ATOM   1898 H HB2  . ASP   B 1 12  ? -8.628  1.763   -7.238  1   55.087  ? 24  ASP   B HB2  1 c 2 
ATOM   1899 H HB3  . ASP   B 1 12  ? -8.851  3.29    -7.585  1   57.246  ? 24  ASP   B HB3  1 c 2 
ATOM   1900 N N    . ILE   B 1 13  ? -11.756 3.876   -5.044  1   52.273  ? 25  ILE   B N    1 ? 2 
ATOM   1901 C CA   . ILE   B 1 13  ? -12.334 5.166   -4.63   1   53.727  ? 25  ILE   B CA   1 ? 2 
ATOM   1902 C C    . ILE   B 1 13  ? -11.515 5.899   -3.572  1   51.081  ? 25  ILE   B C    1 ? 2 
ATOM   1903 O O    . ILE   B 1 13  ? -12.016 6.881   -3.087  1   60.083  ? 25  ILE   B O    1 ? 2 
ATOM   1904 C CB   . ILE   B 1 13  ? -13.785 5.034   -4.131  1   51.022  ? 25  ILE   B CB   1 ? 2 
ATOM   1905 C CG1  . ILE   B 1 13  ? -13.89  4.104   -2.957  1   48.218  ? 25  ILE   B CG1  1 ? 2 
ATOM   1906 C CG2  . ILE   B 1 13  ? -14.714 4.592   -5.254  1   52.971  ? 25  ILE   B CG2  1 ? 2 
ATOM   1907 C CD1  . ILE   B 1 13  ? -15.301 3.928   -2.448  1   50.899  ? 25  ILE   B CD1  1 ? 2 
ATOM   1908 H H    . ILE   B 1 13  ? -11.905 3.13    -4.538  1   49.568  ? 25  ILE   B H    1 c 2 
ATOM   1909 H HA   . ILE   B 1 13  ? -12.358 5.738   -5.421  1   55.499  ? 25  ILE   B HA   1 c 2 
ATOM   1910 H HB   . ILE   B 1 13  ? -14.08  5.917   -3.834  1   51.966  ? 25  ILE   B HB   1 c 2 
ATOM   1911 H HG12 . ILE   B 1 13  ? -13.539 3.227   -3.214  1   48.403  ? 25  ILE   B HG12 1 c 2 
ATOM   1912 H HG13 . ILE   B 1 13  ? -13.334 4.447   -2.229  1   47.954  ? 25  ILE   B HG13 1 c 2 
ATOM   1913 H HG21 . ILE   B 1 13  ? -15.629 4.834   -5.035  1   53.126  ? 25  ILE   B HG21 1 c 2 
ATOM   1914 H HG22 . ILE   B 1 13  ? -14.653 3.629   -5.368  1   52.277  ? 25  ILE   B HG22 1 c 2 
ATOM   1915 H HG23 . ILE   B 1 13  ? -14.456 5.031   -6.083  1   55.521  ? 25  ILE   B HG23 1 c 2 
ATOM   1916 H HD11 . ILE   B 1 13  ? -15.763 4.787   -2.463  1   50.957  ? 25  ILE   B HD11 1 c 2 
ATOM   1917 H HD12 . ILE   B 1 13  ? -15.274 3.59    -1.532  1   48.115  ? 25  ILE   B HD12 1 c 2 
ATOM   1918 H HD13 . ILE   B 1 13  ? -15.781 3.293   -3.012  1   50.42   ? 25  ILE   B HD13 1 c 2 
ATOM   1919 N N    . THR   B 1 14  ? -10.274 5.529   -3.266  1   48.888  ? 26  THR   B N    1 ? 2 
ATOM   1920 C CA   . THR   B 1 14  ? -9.4    6.342   -2.414  1   50.831  ? 26  THR   B CA   1 ? 2 
ATOM   1921 C C    . THR   B 1 14  ? -8.873  7.586   -3.132  1   57.524  ? 26  THR   B C    1 ? 2 
ATOM   1922 O O    . THR   B 1 14  ? -8.742  7.638   -4.364  1   57.349  ? 26  THR   B O    1 ? 2 
ATOM   1923 C CB   . THR   B 1 14  ? -8.208  5.549   -1.886  1   49.907  ? 26  THR   B CB   1 ? 2 
ATOM   1924 O OG1  . THR   B 1 14  ? -7.409  5.104   -2.991  1   51.981  ? 26  THR   B OG1  1 ? 2 
ATOM   1925 C CG2  . THR   B 1 14  ? -8.689  4.377   -1.049  1   43.409  ? 26  THR   B CG2  1 ? 2 
ATOM   1926 H H    . THR   B 1 14  ? -9.95   4.742   -3.599  1   49.379  ? 26  THR   B H    1 c 2 
ATOM   1927 H HA   . THR   B 1 14  ? -9.929  6.635   -1.642  1   49.934  ? 26  THR   B HA   1 c 2 
ATOM   1928 H HB   . THR   B 1 14  ? -7.66   6.133   -1.311  1   50.325  ? 26  THR   B HB   1 c 2 
ATOM   1929 H HG1  . THR   B 1 14  ? -7.895  4.673   -3.599  0   30      ? 26  THR   B HG1  1 c 2 
ATOM   1930 H HG21 . THR   B 1 14  ? -7.924  3.884   -0.71   1   44.11   ? 26  THR   B HG21 1 c 2 
ATOM   1931 H HG22 . THR   B 1 14  ? -9.235  3.789   -1.596  1   43.734  ? 26  THR   B HG22 1 c 2 
ATOM   1932 H HG23 . THR   B 1 14  ? -9.217  4.706   -0.303  1   43.219  ? 26  THR   B HG23 1 c 2 
ATOM   1933 N N    . SER   B 1 15  ? -8.541  8.589   -2.3    1   58.565  ? 27  SER   B N    1 ? 2 
ATOM   1934 C CA   . SER   B 1 15  ? -7.919  9.815   -2.749  1   61.656  ? 27  SER   B CA   1 ? 2 
ATOM   1935 C C    . SER   B 1 15  ? -6.501  9.562   -3.239  1   64.64   ? 27  SER   B C    1 ? 2 
ATOM   1936 O O    . SER   B 1 15  ? -6.06   10.145  -4.249  1   70.616  ? 27  SER   B O    1 ? 2 
ATOM   1937 C CB   . SER   B 1 15  ? -7.917  10.811  -1.641  1   64.401  ? 27  SER   B CB   1 ? 2 
ATOM   1938 O OG   . SER   B 1 15  ? -9.223  11.371  -1.568  1   63.5    ? 27  SER   B OG   1 ? 2 
ATOM   1939 H H    . SER   B 1 15  ? -8.715  8.493   -1.408  1   56.397  ? 27  SER   B H    1 c 2 
ATOM   1940 H HA   . SER   B 1 15  ? -8.451  10.177  -3.503  1   63.899  ? 27  SER   B HA   1 c 2 
ATOM   1941 H HB2  . SER   B 1 15  ? -7.692  10.375  -0.798  1   61.925  ? 27  SER   B HB2  1 c 2 
ATOM   1942 H HB3  . SER   B 1 15  ? -7.263  11.512  -1.824  1   67.202  ? 27  SER   B HB3  1 c 2 
ATOM   1943 H HG   . SER   B 1 15  ? -9.241  11.922  -0.901  0   30      ? 27  SER   B HG   1 c 2 
ATOM   1944 N N    . LYS   B 1 16  ? -5.809  8.672   -2.528  1   62.955  ? 28  LYS   B N    1 ? 2 
ATOM   1945 C CA   . LYS   B 1 16  ? -4.411  8.403   -2.785  1   69.748  ? 28  LYS   B CA   1 ? 2 
ATOM   1946 C C    . LYS   B 1 16  ? -4.228  7.433   -3.956  1   67.877  ? 28  LYS   B C    1 ? 2 
ATOM   1947 O O    . LYS   B 1 16  ? -3.12   7.237   -4.397  1   65.779  ? 28  LYS   B O    1 ? 2 
ATOM   1948 C CB   . LYS   B 1 16  ? -3.796  7.872   -1.488  1   74.198  ? 28  LYS   B CB   1 ? 2 
ATOM   1949 C CG   . LYS   B 1 16  ? -3.388  8.949   -0.485  1   80.351  ? 28  LYS   B CG   1 ? 2 
ATOM   1950 C CD   . LYS   B 1 16  ? -2.192  8.514   0.361   1   88.148  ? 28  LYS   B CD   1 ? 2 
ATOM   1951 C CE   . LYS   B 1 16  ? -2.591  7.785   1.616   1   89.132  ? 28  LYS   B CE   1 ? 2 
ATOM   1952 N NZ   . LYS   B 1 16  ? -3.008  8.744   2.644   1   89.515  ? 28  LYS   B NZ   1 ? 2 
ATOM   1953 H H    . LYS   B 1 16  ? -6.226  8.216   -1.854  1   60.858  ? 28  LYS   B H    1 c 2 
ATOM   1954 H HA   . LYS   B 1 16  ? -3.967  9.258   -3.017  1   73.094  ? 28  LYS   B HA   1 c 2 
ATOM   1955 H HB2  . LYS   B 1 16  ? -4.437  7.27    -1.054  1   69.956  ? 28  LYS   B HB2  1 c 2 
ATOM   1956 H HB3  . LYS   B 1 16  ? -3.002  7.343   -1.715  1   74.548  ? 28  LYS   B HB3  1 c 2 
ATOM   1957 H HG2  . LYS   B 1 16  ? -3.158  9.77    -0.973  1   84.012  ? 28  LYS   B HG2  1 c 2 
ATOM   1958 H HG3  . LYS   B 1 16  ? -4.15   9.143   0.101   1   78.832  ? 28  LYS   B HG3  1 c 2 
ATOM   1959 H HD2  . LYS   B 1 16  ? -1.611  7.931   -0.175  1   88.257  ? 28  LYS   B HD2  1 c 2 
ATOM   1960 H HD3  . LYS   B 1 16  ? -1.671  9.309   0.606   1   90.882  ? 28  LYS   B HD3  1 c 2 
ATOM   1961 H HE2  . LYS   B 1 16  ? -3.329  7.178   1.426   1   84.83   ? 28  LYS   B HE2  1 c 2 
ATOM   1962 H HE3  . LYS   B 1 16  ? -1.84   7.263   1.95    1   88.619  ? 28  LYS   B HE3  1 c 2 
ATOM   1963 H HZ1  . LYS   B 1 16  ? -3.712  9.23    2.349   1   88.999  ? 28  LYS   B HZ1  1 c 2 
ATOM   1964 H HZ2  . LYS   B 1 16  ? -2.322  9.302   2.841   1   92.705  ? 28  LYS   B HZ2  1 c 2 
ATOM   1965 H HZ3  . LYS   B 1 16  ? -3.251  8.298   3.395   1   87.592  ? 28  LYS   B HZ3  1 c 2 
ATOM   1966 N N    . LYS   B 1 17  ? -5.305  6.782   -4.412  1   64.054  ? 29  LYS   B N    1 ? 2 
ATOM   1967 C CA   . LYS   B 1 17  ? -5.277  5.724   -5.419  1   62.037  ? 29  LYS   B CA   1 ? 2 
ATOM   1968 C C    . LYS   B 1 17  ? -4.349  4.575   -5.004  1   58.743  ? 29  LYS   B C    1 ? 2 
ATOM   1969 O O    . LYS   B 1 17  ? -3.496  4.134   -5.768  1   57.224  ? 29  LYS   B O    1 ? 2 
ATOM   1970 C CB   . LYS   B 1 17  ? -4.961  6.332   -6.782  1   69.136  ? 29  LYS   B CB   1 ? 2 
ATOM   1971 C CG   . LYS   B 1 17  ? -6.034  7.235   -7.384  1   72.594  ? 29  LYS   B CG   1 ? 2 
ATOM   1972 C CD   . LYS   B 1 17  ? -7.237  6.425   -7.852  1   72.237  ? 29  LYS   B CD   1 ? 2 
ATOM   1973 C CE   . LYS   B 1 17  ? -8.295  7.324   -8.374  1   76.428  ? 29  LYS   B CE   1 ? 2 
ATOM   1974 N NZ   . LYS   B 1 17  ? -9.194  7.629   -7.258  1   74.092  ? 29  LYS   B NZ   1 ? 2 
ATOM   1975 H H    . LYS   B 1 17  ? -6.119  7.009   -4.066  1   61.892  ? 29  LYS   B H    1 c 2 
ATOM   1976 H HA   . LYS   B 1 17  ? -6.192  5.354   -5.477  1   60.196  ? 29  LYS   B HA   1 c 2 
ATOM   1977 H HB2  . LYS   B 1 17  ? -4.132  6.851   -6.709  1   71.785  ? 29  LYS   B HB2  1 c 2 
ATOM   1978 H HB3  . LYS   B 1 17  ? -4.793  5.601   -7.414  1   69.908  ? 29  LYS   B HB3  1 c 2 
ATOM   1979 H HG2  . LYS   B 1 17  ? -6.321  7.886   -6.707  1   71.45   ? 29  LYS   B HG2  1 c 2 
ATOM   1980 H HG3  . LYS   B 1 17  ? -5.651  7.724   -8.144  1   76.616  ? 29  LYS   B HG3  1 c 2 
ATOM   1981 H HD2  . LYS   B 1 17  ? -6.958  5.806   -8.562  1   73.881  ? 29  LYS   B HD2  1 c 2 
ATOM   1982 H HD3  . LYS   B 1 17  ? -7.594  5.899   -7.104  1   68.644  ? 29  LYS   B HD3  1 c 2 
ATOM   1983 H HE2  . LYS   B 1 17  ? -7.91   8.15    -8.721  1   79.553  ? 29  LYS   B HE2  1 c 2 
ATOM   1984 H HE3  . LYS   B 1 17  ? -8.795  6.884   -9.085  1   77.006  ? 29  LYS   B HE3  1 c 2 
ATOM   1985 H HZ1  . LYS   B 1 17  ? -8.717  7.918   -6.544  1   72.706  ? 29  LYS   B HZ1  1 c 2 
ATOM   1986 H HZ2  . LYS   B 1 17  ? -9.661  6.888   -7.026  1   70.942  ? 29  LYS   B HZ2  1 c 2 
ATOM   1987 H HZ3  . LYS   B 1 17  ? -9.775  8.278   -7.506  1   75.019  ? 29  LYS   B HZ3  1 c 2 
ATOM   1988 N N    . ASP   B 1 18  ? -4.556  4.036   -3.797  1   51.327  ? 30  ASP   B N    1 ? 2 
ATOM   1989 C CA   . ASP   B 1 18  ? -3.695  2.97    -3.291  1   51.363  ? 30  ASP   B CA   1 ? 2 
ATOM   1990 C C    . ASP   B 1 18  ? -4.494  1.666   -3.201  1   49.047  ? 30  ASP   B C    1 ? 2 
ATOM   1991 O O    . ASP   B 1 18  ? -4.175  0.764   -2.423  1   46.503  ? 30  ASP   B O    1 ? 2 
ATOM   1992 C CB   . ASP   B 1 18  ? -3.107  3.376   -1.95   1   51.287  ? 30  ASP   B CB   1 ? 2 
ATOM   1993 C CG   . ASP   B 1 18  ? -4.187  3.667   -0.897  1   49.307  ? 30  ASP   B CG   1 ? 2 
ATOM   1994 O OD1  . ASP   B 1 18  ? -5.383  3.458   -1.192  1   43.894  ? 30  ASP   B OD1  1 ? 2 
ATOM   1995 O OD2  . ASP   B 1 18  ? -3.815  4.137   0.187   1   51.828  ? 30  ASP   B OD2  1 ? 2 
ATOM   1996 H H    . ASP   B 1 18  ? -5.252  4.33    -3.283  1   50.33   ? 30  ASP   B H    1 c 2 
ATOM   1997 H HA   . ASP   B 1 18  ? -2.95   2.839   -3.919  1   54.302  ? 30  ASP   B HA   1 c 2 
ATOM   1998 H HB2  . ASP   B 1 18  ? -2.527  2.66    -1.617  1   51.586  ? 30  ASP   B HB2  1 c 2 
ATOM   1999 H HB3  . ASP   B 1 18  ? -2.562  4.182   -2.069  1   54.209  ? 30  ASP   B HB3  1 c 2 
ATOM   2000 N N    . ARG   B 1 19  ? -5.592  1.617   -3.958  1   48.536  ? 31  ARG   B N    1 ? 2 
ATOM   2001 C CA   . ARG   B 1 19  ? -6.481  0.475   -3.992  1   48.007  ? 31  ARG   B CA   1 ? 2 
ATOM   2002 C C    . ARG   B 1 19  ? -6.982  0.069   -2.615  1   45.628  ? 31  ARG   B C    1 ? 2 
ATOM   2003 O O    . ARG   B 1 19  ? -7.417  -1.058  -2.498  1   45.256  ? 31  ARG   B O    1 ? 2 
ATOM   2004 C CB   . ARG   B 1 19  ? -5.808  -0.697  -4.739  1   49.576  ? 31  ARG   B CB   1 ? 2 
ATOM   2005 C CG   . ARG   B 1 19  ? -5.664  -0.429  -6.224  1   51.737  ? 31  ARG   B CG   1 ? 2 
ATOM   2006 C CD   . ARG   B 1 19  ? -4.944  -1.626  -6.856  1   55.178  ? 31  ARG   B CD   1 ? 2 
ATOM   2007 N NE   . ARG   B 1 19  ? -5.745  -2.845  -6.691  1   54.752  ? 31  ARG   B NE   1 ? 2 
ATOM   2008 C CZ   . ARG   B 1 19  ? -6.802  -3.106  -7.478  1   55.773  ? 31  ARG   B CZ   1 ? 2 
ATOM   2009 N NH1  . ARG   B 1 19  ? -7.243  -2.253  -8.394  1   56.678  ? 31  ARG   B NH1  1 ? 2 
ATOM   2010 N NH2  . ARG   B 1 19  ? -7.459  -4.24   -7.34   1   59.147  ? 31  ARG   B NH2  1 ? 2 
ATOM   2011 H H    . ARG   B 1 19  ? -5.79   2.33    -4.492  1   50.278  ? 31  ARG   B H    1 c 2 
ATOM   2012 H HA   . ARG   B 1 19  ? -7.272  0.73    -4.526  1   47.94   ? 31  ARG   B HA   1 c 2 
ATOM   2013 H HB2  . ARG   B 1 19  ? -4.919  -0.857  -4.357  1   50.001  ? 31  ARG   B HB2  1 c 2 
ATOM   2014 H HB3  . ARG   B 1 19  ? -6.342  -1.509  -4.612  1   48.062  ? 31  ARG   B HB3  1 c 2 
ATOM   2015 H HG2  . ARG   B 1 19  ? -6.55   -0.322  -6.634  1   52.044  ? 31  ARG   B HG2  1 c 2 
ATOM   2016 H HG3  . ARG   B 1 19  ? -5.136  0.387   -6.369  1   53.987  ? 31  ARG   B HG3  1 c 2 
ATOM   2017 H HD2  . ARG   B 1 19  ? -4.794  -1.459  -7.808  1   58.347  ? 31  ARG   B HD2  1 c 2 
ATOM   2018 H HD3  . ARG   B 1 19  ? -4.073  -1.75   -6.426  1   55.772  ? 31  ARG   B HD3  1 c 2 
ATOM   2019 H HE   . ARG   B 1 19  ? -5.527  -3.412  -6.067  1   53.389  ? 31  ARG   B HE   1 c 2 
ATOM   2020 H HH11 . ARG   B 1 19  ? -6.722  -2.026  -9.071  1   59.855  ? 31  ARG   B HH11 1 c 2 
ATOM   2021 H HH12 . ARG   B 1 19  ? -8.059  -1.917  -8.323  1   55.841  ? 31  ARG   B HH12 1 c 2 
ATOM   2022 H HH21 . ARG   B 1 19  ? -7.284  -4.772  -6.657  1   56.352  ? 31  ARG   B HH21 1 c 2 
ATOM   2023 H HH22 . ARG   B 1 19  ? -8.076  -4.465  -7.933  1   58.968  ? 31  ARG   B HH22 1 c 2 
ATOM   2024 N N    . GLY   B 1 20  ? -6.96   0.988   -1.627  1   45.599  ? 32  GLY   B N    1 ? 2 
ATOM   2025 C CA   . GLY   B 1 20  ? -7.291  0.654   -0.242  1   43.827  ? 32  GLY   B CA   1 ? 2 
ATOM   2026 C C    . GLY   B 1 20  ? -8.796  0.392   -0.042  1   40.994  ? 32  GLY   B C    1 ? 2 
ATOM   2027 O O    . GLY   B 1 20  ? -9.223  -0.379  0.812   1   36.846  ? 32  GLY   B O    1 ? 2 
ATOM   2028 H H    . GLY   B 1 20  ? -6.754  1.855   -1.828  1   46.634  ? 32  GLY   B H    1 c 2 
ATOM   2029 H HA2  . GLY   B 1 20  ? -6.782  -0.146  0.024   1   43.62   ? 32  GLY   B HA2  1 c 2 
ATOM   2030 H HA3  . GLY   B 1 20  ? -7.009  1.396   0.338   1   43.727  ? 32  GLY   B HA3  1 c 2 
ATOM   2031 N N    . VAL   B 1 21  ? -9.596  1.026   -0.892  1   41.723  ? 33  VAL   B N    1 ? 2 
ATOM   2032 C CA   . VAL   B 1 21  ? -11.028 0.871   -0.873  1   40.086  ? 33  VAL   B CA   1 ? 2 
ATOM   2033 C C    . VAL   B 1 21  ? -11.388 0.653   -2.337  1   36.789  ? 33  VAL   B C    1 ? 2 
ATOM   2034 O O    . VAL   B 1 21  ? -11.272 1.569   -3.098  1   37.447  ? 33  VAL   B O    1 ? 2 
ATOM   2035 C CB   . VAL   B 1 21  ? -11.845 2.052   -0.285  1   40.224  ? 33  VAL   B CB   1 ? 2 
ATOM   2036 C CG1  . VAL   B 1 21  ? -13.327 1.701   -0.26   1   40.023  ? 33  VAL   B CG1  1 ? 2 
ATOM   2037 C CG2  . VAL   B 1 21  ? -11.338 2.523   1.088   1   40.629  ? 33  VAL   B CG2  1 ? 2 
ATOM   2038 H H    . VAL   B 1 21  ? -9.228  1.586   -1.513  1   42.934  ? 33  VAL   B H    1 c 2 
ATOM   2039 H HA   . VAL   B 1 21  ? -11.249 0.062   -0.373  1   38.213  ? 33  VAL   B HA   1 c 2 
ATOM   2040 H HB   . VAL   B 1 21  ? -11.738 2.811   -0.906  1   41.629  ? 33  VAL   B HB   1 c 2 
ATOM   2041 H HG11 . VAL   B 1 21  ? -13.442 0.798   0.08    1   39.22   ? 33  VAL   B HG11 1 c 2 
ATOM   2042 H HG12 . VAL   B 1 21  ? -13.691 1.756   -1.16   1   41.065  ? 33  VAL   B HG12 1 c 2 
ATOM   2043 H HG13 . VAL   B 1 21  ? -13.799 2.325   0.316   1   39.787  ? 33  VAL   B HG13 1 c 2 
ATOM   2044 H HG21 . VAL   B 1 21  ? -11.891 3.258   1.404   1   40.465  ? 33  VAL   B HG21 1 c 2 
ATOM   2045 H HG22 . VAL   B 1 21  ? -10.417 2.822   1.01    1   41.091  ? 33  VAL   B HG22 1 c 2 
ATOM   2046 H HG23 . VAL   B 1 21  ? -11.386 1.788   1.722   1   39.327  ? 33  VAL   B HG23 1 c 2 
ATOM   2047 N N    . LEU   B 1 22  ? -11.931 -0.501  -2.665  1   36.173  ? 34  LEU   B N    1 ? 2 
ATOM   2048 C CA   . LEU   B 1 22  ? -12.48  -0.792  -3.994  1   41.669  ? 34  LEU   B CA   1 ? 2 
ATOM   2049 C C    . LEU   B 1 22  ? -13.996 -0.959  -3.991  1   40.762  ? 34  LEU   B C    1 ? 2 
ATOM   2050 O O    . LEU   B 1 22  ? -14.512 -1.664  -3.137  1   40.972  ? 34  LEU   B O    1 ? 2 
ATOM   2051 C CB   . LEU   B 1 22  ? -11.788 -2.071  -4.465  1   42.555  ? 34  LEU   B CB   1 ? 2 
ATOM   2052 C CG   . LEU   B 1 22  ? -10.275 -1.908  -4.641  1   45.936  ? 34  LEU   B CG   1 ? 2 
ATOM   2053 C CD1  . LEU   B 1 22  ? -9.538  -3.206  -4.708  1   49.054  ? 34  LEU   B CD1  1 ? 2 
ATOM   2054 C CD2  . LEU   B 1 22  ? -10.032 -1.162  -5.946  1   50.617  ? 34  LEU   B CD2  1 ? 2 
ATOM   2055 H H    . LEU   B 1 22  ? -11.968 -1.16   -2.032  1   36.048  ? 34  LEU   B H    1 c 2 
ATOM   2056 H HA   . LEU   B 1 22  ? -12.242 -0.051  -4.6    1   42.187  ? 34  LEU   B HA   1 c 2 
ATOM   2057 H HB2  . LEU   B 1 22  ? -11.954 -2.779  -3.8    1   41.999  ? 34  LEU   B HB2  1 c 2 
ATOM   2058 H HB3  . LEU   B 1 22  ? -12.181 -2.341  -5.326  1   45.135  ? 34  LEU   B HB3  1 c 2 
ATOM   2059 H HG   . LEU   B 1 22  ? -9.917  -1.371  -3.889  1   44.642  ? 34  LEU   B HG   1 c 2 
ATOM   2060 H HD11 . LEU   B 1 22  ? -9.722  -3.725  -3.907  1   46.915  ? 34  LEU   B HD11 1 c 2 
ATOM   2061 H HD12 . LEU   B 1 22  ? -8.583  -3.034  -4.77   1   49.199  ? 34  LEU   B HD12 1 c 2 
ATOM   2062 H HD13 . LEU   B 1 22  ? -9.828  -3.705  -5.49   1   50.23   ? 34  LEU   B HD13 1 c 2 
ATOM   2063 H HD21 . LEU   B 1 22  ? -10.532 -0.331  -5.945  1   49.889  ? 34  LEU   B HD21 1 c 2 
ATOM   2064 H HD22 . LEU   B 1 22  ? -10.32  -1.711  -6.693  1   51.91   ? 34  LEU   B HD22 1 c 2 
ATOM   2065 H HD23 . LEU   B 1 22  ? -9.084  -0.967  -6.036  1   51.073  ? 34  LEU   B HD23 1 c 2 
ATOM   2066 N N    . LYS   B 1 23  ? -14.677 -0.486  -5.047  1   45.788  ? 35  LYS   B N    1 ? 2 
ATOM   2067 C CA   . LYS   B 1 23  ? -16.128 -0.481  -5.069  1   46.507  ? 35  LYS   B CA   1 ? 2 
ATOM   2068 C C    . LYS   B 1 23  ? -16.705 -0.998  -6.358  1   54.658  ? 35  LYS   B C    1 ? 2 
ATOM   2069 O O    . LYS   B 1 23  ? -16.28  -0.577  -7.43   1   61.6    ? 35  LYS   B O    1 ? 2 
ATOM   2070 C CB   . LYS   B 1 23  ? -16.612 0.969   -5.064  1   47.107  ? 35  LYS   B CB   1 ? 2 
ATOM   2071 C CG   . LYS   B 1 23  ? -18.115 1.078   -4.808  1   49.062  ? 35  LYS   B CG   1 ? 2 
ATOM   2072 C CD   . LYS   B 1 23  ? -18.627 2.5     -4.922  1   51.129  ? 35  LYS   B CD   1 ? 2 
ATOM   2073 C CE   . LYS   B 1 23  ? -20.074 2.742   -4.64   1   53.522  ? 35  LYS   B CE   1 ? 2 
ATOM   2074 N NZ   . LYS   B 1 23  ? -20.419 4.066   -5.202  1   59.222  ? 35  LYS   B NZ   1 ? 2 
ATOM   2075 H H    . LYS   B 1 23  ? -14.222 -0.162  -5.771  1   46.633  ? 35  LYS   B H    1 c 2 
ATOM   2076 H HA   . LYS   B 1 23  ? -16.483 -0.987  -4.299  1   46.064  ? 35  LYS   B HA   1 c 2 
ATOM   2077 H HB2  . LYS   B 1 23  ? -16.136 1.462   -4.362  1   45.619  ? 35  LYS   B HB2  1 c 2 
ATOM   2078 H HB3  . LYS   B 1 23  ? -16.404 1.392   -5.925  1   49.398  ? 35  LYS   B HB3  1 c 2 
ATOM   2079 H HG2  . LYS   B 1 23  ? -18.59  0.515   -5.455  1   51.033  ? 35  LYS   B HG2  1 c 2 
ATOM   2080 H HG3  . LYS   B 1 23  ? -18.309 0.737   -3.909  1   47.36   ? 35  LYS   B HG3  1 c 2 
ATOM   2081 H HD2  . LYS   B 1 23  ? -18.097 3.059   -4.314  1   49.562  ? 35  LYS   B HD2  1 c 2 
ATOM   2082 H HD3  . LYS   B 1 23  ? -18.434 2.815   -5.832  1   53.273  ? 35  LYS   B HD3  1 c 2 
ATOM   2083 H HE2  . LYS   B 1 23  ? -20.623 2.055   -5.058  1   55.526  ? 35  LYS   B HE2  1 c 2 
ATOM   2084 H HE3  . LYS   B 1 23  ? -20.239 2.74    -3.679  1   52.29   ? 35  LYS   B HE3  1 c 2 
ATOM   2085 H HZ1  . LYS   B 1 23  ? -20.533 3.997   -6.098  1   60.537  ? 35  LYS   B HZ1  1 c 2 
ATOM   2086 H HZ2  . LYS   B 1 23  ? -19.756 4.657   -5.032  1   57.364  ? 35  LYS   B HZ2  1 c 2 
ATOM   2087 H HZ3  . LYS   B 1 23  ? -21.188 4.366   -4.827  1   58.942  ? 35  LYS   B HZ3  1 c 2 
ATOM   2088 N N    . ILE   B 1 24  ? -17.767 -1.818  -6.26   1   59.162  ? 36  ILE   B N    1 ? 2 
ATOM   2089 C CA   . ILE   B 1 24  ? -18.643 -2.038  -7.405  1   62.092  ? 36  ILE   B CA   1 ? 2 
ATOM   2090 C C    . ILE   B 1 24  ? -20.078 -1.74   -7.005  1   62.395  ? 36  ILE   B C    1 ? 2 
ATOM   2091 O O    . ILE   B 1 24  ? -20.494 -2.039  -5.896  1   62.205  ? 36  ILE   B O    1 ? 2 
ATOM   2092 C CB   . ILE   B 1 24  ? -18.512 -3.449  -7.967  1   64.98   ? 36  ILE   B CB   1 ? 2 
ATOM   2093 C CG1  . ILE   B 1 24  ? -17.093 -3.739  -8.322  1   65.326  ? 36  ILE   B CG1  1 ? 2 
ATOM   2094 C CG2  . ILE   B 1 24  ? -19.442 -3.651  -9.164  1   69.757  ? 36  ILE   B CG2  1 ? 2 
ATOM   2095 C CD1  . ILE   B 1 24  ? -16.913 -5.134  -8.846  1   69.491  ? 36  ILE   B CD1  1 ? 2 
ATOM   2096 H H    . ILE   B 1 24  ? -17.945 -2.247  -5.472  1   56.372  ? 36  ILE   B H    1 c 2 
ATOM   2097 H HA   . ILE   B 1 24  ? -18.387 -1.411  -8.109  1   63.738  ? 36  ILE   B HA   1 c 2 
ATOM   2098 H HB   . ILE   B 1 24  ? -18.78  -4.077  -7.266  1   63.861  ? 36  ILE   B HB   1 c 2 
ATOM   2099 H HG12 . ILE   B 1 24  ? -16.797 -3.1    -9.003  1   66.806  ? 36  ILE   B HG12 1 c 2 
ATOM   2100 H HG13 . ILE   B 1 24  ? -16.532 -3.622  -7.529  1   62.388  ? 36  ILE   B HG13 1 c 2 
ATOM   2101 H HG21 . ILE   B 1 24  ? -19.307 -4.535  -9.541  1   71.818  ? 36  ILE   B HG21 1 c 2 
ATOM   2102 H HG22 . ILE   B 1 24  ? -19.252 -2.979  -9.841  1   71.361  ? 36  ILE   B HG22 1 c 2 
ATOM   2103 H HG23 . ILE   B 1 24  ? -20.366 -3.566  -8.877  1   70.531  ? 36  ILE   B HG23 1 c 2 
ATOM   2104 H HD11 . ILE   B 1 24  ? -17.423 -5.761  -8.299  1   68.669  ? 36  ILE   B HD11 1 c 2 
ATOM   2105 H HD12 . ILE   B 1 24  ? -15.968 -5.367  -8.807  1   68.127  ? 36  ILE   B HD12 1 c 2 
ATOM   2106 H HD13 . ILE   B 1 24  ? -17.219 -5.187  -9.771  1   72.553  ? 36  ILE   B HD13 1 c 2 
ATOM   2107 N N    . VAL   B 1 25  ? -20.781 -1.06   -7.898  1   63.484  ? 37  VAL   B N    1 ? 2 
ATOM   2108 C CA   . VAL   B 1 25  ? -22.197 -0.835  -7.784  1   66.332  ? 37  VAL   B CA   1 ? 2 
ATOM   2109 C C    . VAL   B 1 25  ? -22.898 -2.09   -8.266  1   73.756  ? 37  VAL   B C    1 ? 2 
ATOM   2110 O O    . VAL   B 1 25  ? -22.599 -2.555  -9.365  1   75.083  ? 37  VAL   B O    1 ? 2 
ATOM   2111 C CB   . VAL   B 1 25  ? -22.352 0.348   -8.74   1   71.891  ? 37  VAL   B CB   1 ? 2 
ATOM   2112 C CG1  . VAL   B 1 25  ? -23.808 0.594   -9.17   1   77.428  ? 37  VAL   B CG1  1 ? 2 
ATOM   2113 C CG2  . VAL   B 1 25  ? -21.632 1.579   -8.166  1   70.52   ? 37  VAL   B CG2  1 ? 2 
ATOM   2114 H H    . VAL   B 1 25  ? -20.346 -0.736  -8.633  1   65.613  ? 37  VAL   B H    1 c 2 
ATOM   2115 H HA   . VAL   B 1 25  ? -22.449 -0.598  -6.87   1   65.309  ? 37  VAL   B HA   1 c 2 
ATOM   2116 H HB   . VAL   B 1 25  ? -21.871 0.107   -9.566  1   73.514  ? 37  VAL   B HB   1 c 2 
ATOM   2117 H HG11 . VAL   B 1 25  ? -24.394 0.503   -8.4    1   76.289  ? 37  VAL   B HG11 1 c 2 
ATOM   2118 H HG12 . VAL   B 1 25  ? -24.062 -0.056  -9.847  1   80.238  ? 37  VAL   B HG12 1 c 2 
ATOM   2119 H HG13 . VAL   B 1 25  ? -23.893 1.49    -9.537  1   78.656  ? 37  VAL   B HG13 1 c 2 
ATOM   2120 H HG21 . VAL   B 1 25  ? -21.999 2.386   -8.566  1   72.151  ? 37  VAL   B HG21 1 c 2 
ATOM   2121 H HG22 . VAL   B 1 25  ? -20.682 1.525   -8.366  1   68.736  ? 37  VAL   B HG22 1 c 2 
ATOM   2122 H HG23 . VAL   B 1 25  ? -21.758 1.611   -7.203  1   67.363  ? 37  VAL   B HG23 1 c 2 
ATOM   2123 N N    . LYS   B 1 26  ? -23.747 -2.695  -7.427  1   75.328  ? 38  LYS   B N    1 ? 2 
ATOM   2124 C CA   . LYS   B 1 26  ? -24.427 -3.906  -7.836  1   77.53   ? 38  LYS   B CA   1 ? 2 
ATOM   2125 C C    . LYS   B 1 26  ? -25.858 -3.573  -8.242  1   85.957  ? 38  LYS   B C    1 ? 2 
ATOM   2126 O O    . LYS   B 1 26  ? -26.344 -4.117  -9.235  1   89.446  ? 38  LYS   B O    1 ? 2 
ATOM   2127 C CB   . LYS   B 1 26  ? -24.283 -4.998  -6.786  1   76.889  ? 38  LYS   B CB   1 ? 2 
ATOM   2128 C CG   . LYS   B 1 26  ? -22.825 -5.433  -6.576  1   75.611  ? 38  LYS   B CG   1 ? 2 
ATOM   2129 C CD   . LYS   B 1 26  ? -22.088 -6.039  -7.776  1   76.858  ? 38  LYS   B CD   1 ? 2 
ATOM   2130 C CE   . LYS   B 1 26  ? -21.99  -7.505  -7.949  1   77.233  ? 38  LYS   B CE   1 ? 2 
ATOM   2131 N NZ   . LYS   B 1 26  ? -21.543 -7.9    -9.289  1   81.919  ? 38  LYS   B NZ   1 ? 2 
ATOM   2132 H H    . LYS   B 1 26  ? -23.894 -2.355  -6.592  1   72.319  ? 38  LYS   B H    1 c 2 
ATOM   2133 H HA   . LYS   B 1 26  ? -23.974 -4.242  -8.647  1   80.317  ? 38  LYS   B HA   1 c 2 
ATOM   2134 H HB2  . LYS   B 1 26  ? -24.643 -4.675  -5.933  1   75.574  ? 38  LYS   B HB2  1 c 2 
ATOM   2135 H HB3  . LYS   B 1 26  ? -24.809 -5.779  -7.061  1   80.546  ? 38  LYS   B HB3  1 c 2 
ATOM   2136 H HG2  . LYS   B 1 26  ? -22.319 -4.651  -6.267  1   71.655  ? 38  LYS   B HG2  1 c 2 
ATOM   2137 H HG3  . LYS   B 1 26  ? -22.812 -6.087  -5.846  1   73.7    ? 38  LYS   B HG3  1 c 2 
ATOM   2138 H HD2  . LYS   B 1 26  ? -22.497 -5.67   -8.588  1   79.38   ? 38  LYS   B HD2  1 c 2 
ATOM   2139 H HD3  . LYS   B 1 26  ? -21.174 -5.68   -7.757  1   73.889  ? 38  LYS   B HD3  1 c 2 
ATOM   2140 H HE2  . LYS   B 1 26  ? -21.367 -7.864  -7.292  1   75.286  ? 38  LYS   B HE2  1 c 2 
ATOM   2141 H HE3  . LYS   B 1 26  ? -22.863 -7.903  -7.781  1   80.415  ? 38  LYS   B HE3  1 c 2 
ATOM   2142 H HZ1  . LYS   B 1 26  ? -20.696 -7.61   -9.427  1   79.707  ? 38  LYS   B HZ1  1 c 2 
ATOM   2143 H HZ2  . LYS   B 1 26  ? -22.088 -7.537  -9.916  1   84.384  ? 38  LYS   B HZ2  1 c 2 
ATOM   2144 H HZ3  . LYS   B 1 26  ? -21.564 -8.802  -9.364  1   83.747  ? 38  LYS   B HZ3  1 c 2 
ATOM   2145 N N    . ARG   B 1 27  ? -26.508 -2.665  -7.499  1   86.703  ? 39  ARG   B N    1 ? 2 
ATOM   2146 C CA   . ARG   B 1 27  ? -27.825 -2.162  -7.874  1   91.056  ? 39  ARG   B CA   1 ? 2 
ATOM   2147 C C    . ARG   B 1 27  ? -27.803 -0.637  -7.77   1   86.395  ? 39  ARG   B C    1 ? 2 
ATOM   2148 O O    . ARG   B 1 27  ? -27.461 -0.101  -6.74   1   84.775  ? 39  ARG   B O    1 ? 2 
ATOM   2149 C CB   . ARG   B 1 27  ? -28.955 -2.765  -7.021  1   92.831  ? 39  ARG   B CB   1 ? 2 
ATOM   2150 C CG   . ARG   B 1 27  ? -30.348 -2.693  -7.641  1   99.877  ? 39  ARG   B CG   1 ? 2 
ATOM   2151 C CD   . ARG   B 1 27  ? -31.453 -3.113  -6.659  1   101.052 ? 39  ARG   B CD   1 ? 2 
ATOM   2152 N NE   . ARG   B 1 27  ? -31.438 -2.146  -5.55   1   96.129  ? 39  ARG   B NE   1 ? 2 
ATOM   2153 C CZ   . ARG   B 1 27  ? -31.918 -2.379  -4.347  1   93.503  ? 39  ARG   B CZ   1 ? 2 
ATOM   2154 N NH1  . ARG   B 1 27  ? -32.477 -3.551  -4.092  1   95.544  ? 39  ARG   B NH1  1 ? 2 
ATOM   2155 N NH2  . ARG   B 1 27  ? -31.84  -1.449  -3.415  1   88.892  ? 39  ARG   B NH2  1 ? 2 
ATOM   2156 H H    . ARG   B 1 27  ? -26.126 -2.359  -6.727  1   82.387  ? 39  ARG   B H    1 c 2 
ATOM   2157 H HA   . ARG   B 1 27  ? -27.993 -2.406  -8.819  1   94.104  ? 39  ARG   B HA   1 c 2 
ATOM   2158 H HB2  . ARG   B 1 27  ? -28.74  -3.706  -6.845  1   92.686  ? 39  ARG   B HB2  1 c 2 
ATOM   2159 H HB3  . ARG   B 1 27  ? -28.971 -2.3    -6.157  1   90.227  ? 39  ARG   B HB3  1 c 2 
ATOM   2160 H HG2  . ARG   B 1 27  ? -30.521 -1.775  -7.942  1   100.28  ? 39  ARG   B HG2  1 c 2 
ATOM   2161 H HG3  . ARG   B 1 27  ? -30.381 -3.279  -8.428  1   102.724 ? 39  ARG   B HG3  1 c 2 
ATOM   2162 H HD2  . ARG   B 1 27  ? -32.328 -3.101  -7.098  1   106.223 ? 39  ARG   B HD2  1 c 2 
ATOM   2163 H HD3  . ARG   B 1 27  ? -31.281 -4.015  -6.317  1   100.594 ? 39  ARG   B HD3  1 c 2 
ATOM   2164 H HE   . ARG   B 1 27  ? -31.093 -1.36   -5.698  1   93.915  ? 39  ARG   B HE   1 c 2 
ATOM   2165 H HH11 . ARG   B 1 27  ? -33.109 -3.863  -4.626  1   100.557 ? 39  ARG   B HH11 1 c 2 
ATOM   2166 H HH12 . ARG   B 1 27  ? -32.226 -4.013  -3.384  1   94.142  ? 39  ARG   B HH12 1 c 2 
ATOM   2167 H HH21 . ARG   B 1 27  ? -31.197 -0.843  -3.448  1   86.159  ? 39  ARG   B HH21 1 c 2 
ATOM   2168 H HH22 . ARG   B 1 27  ? -32.432 -1.437  -2.758  1   90.936  ? 39  ARG   B HH22 1 c 2 
ATOM   2169 N N    . VAL   B 1 28  ? -28.154 0.04    -8.861  1   90.079  ? 40  VAL   B N    1 ? 2 
ATOM   2170 C CA   . VAL   B 1 28  ? -27.889 1.449   -9.031  1   88.12   ? 40  VAL   B CA   1 ? 2 
ATOM   2171 C C    . VAL   B 1 28  ? -28.969 2.194   -8.268  1   90.708  ? 40  VAL   B C    1 ? 2 
ATOM   2172 O O    . VAL   B 1 28  ? -30.127 1.798   -8.351  1   93.411  ? 40  VAL   B O    1 ? 2 
ATOM   2173 C CB   . VAL   B 1 28  ? -27.842 1.856   -10.51  1   90.86   ? 40  VAL   B CB   1 ? 2 
ATOM   2174 C CG1  . VAL   B 1 28  ? -29.14  1.488   -11.242 1   99.909  ? 40  VAL   B CG1  1 ? 2 
ATOM   2175 C CG2  . VAL   B 1 28  ? -27.485 3.329   -10.673 1   89.364  ? 40  VAL   B CG2  1 ? 2 
ATOM   2176 H H    . VAL   B 1 28  ? -28.583 -0.408  -9.532  1   93.842  ? 40  VAL   B H    1 c 2 
ATOM   2177 H HA   . VAL   B 1 28  ? -27.022 1.651   -8.627  1   84.036  ? 40  VAL   B HA   1 c 2 
ATOM   2178 H HB   . VAL   B 1 28  ? -27.117 1.334   -10.927 1   90.423  ? 40  VAL   B HB   1 c 2 
ATOM   2179 H HG11 . VAL   B 1 28  ? -29.883 1.983   -10.86  1   100.786 ? 40  VAL   B HG11 1 c 2 
ATOM   2180 H HG12 . VAL   B 1 28  ? -29.307 0.536   -11.158 1   99.917  ? 40  VAL   B HG12 1 c 2 
ATOM   2181 H HG13 . VAL   B 1 28  ? -29.054 1.716   -12.183 1   102.742 ? 40  VAL   B HG13 1 c 2 
ATOM   2182 H HG21 . VAL   B 1 28  ? -27.241 3.503   -11.598 1   92.501  ? 40  VAL   B HG21 1 c 2 
ATOM   2183 H HG22 . VAL   B 1 28  ? -26.735 3.547   -10.095 1   85.372  ? 40  VAL   B HG22 1 c 2 
ATOM   2184 H HG23 . VAL   B 1 28  ? -28.249 3.878   -10.432 1   91.697  ? 40  VAL   B HG23 1 c 2 
ATOM   2185 N N    . GLY   B 1 29  ? -28.56  3.221   -7.499  1   88.258  ? 41  GLY   B N    1 ? 2 
ATOM   2186 C CA   . GLY   B 1 29  ? -29.497 4.075   -6.79   1   91.426  ? 41  GLY   B CA   1 ? 2 
ATOM   2187 C C    . GLY   B 1 29  ? -30.311 4.954   -7.752  1   99.572  ? 41  GLY   B C    1 ? 2 
ATOM   2188 O O    . GLY   B 1 29  ? -30.355 4.729   -8.962  1   104.022 ? 41  GLY   B O    1 ? 2 
ATOM   2189 H H    . GLY   B 1 29  ? -27.665 3.391   -7.418  1   85.03   ? 41  GLY   B H    1 c 2 
ATOM   2190 H HA2  . GLY   B 1 29  ? -30.11  3.512   -6.264  1   92.245  ? 41  GLY   B HA2  1 c 2 
ATOM   2191 H HA3  . GLY   B 1 29  ? -28.998 4.649   -6.163  1   88.362  ? 41  GLY   B HA3  1 c 2 
ATOM   2192 N N    . ASN   B 1 30  ? -30.965 5.97    -7.202  1   102.055 ? 42  ASN   B N    1 ? 2 
ATOM   2193 C CA   . ASN   B 1 30  ? -31.729 6.931   -7.98   1   109.408 ? 42  ASN   B CA   1 ? 2 
ATOM   2194 C C    . ASN   B 1 30  ? -31.426 8.317   -7.417  1   107.917 ? 42  ASN   B C    1 ? 2 
ATOM   2195 O O    . ASN   B 1 30  ? -31.27  8.469   -6.206  1   106.109 ? 42  ASN   B O    1 ? 2 
ATOM   2196 C CB   . ASN   B 1 30  ? -33.197 6.534   -7.924  1   119.611 ? 42  ASN   B CB   1 ? 2 
ATOM   2197 C CG   . ASN   B 1 30  ? -33.627 6.299   -6.493  1   119.66  ? 42  ASN   B CG   1 ? 2 
ATOM   2198 O OD1  . ASN   B 1 30  ? -33.783 7.252   -5.722  1   125.196 ? 42  ASN   B OD1  1 ? 2 
ATOM   2199 N ND2  . ASN   B 1 30  ? -33.807 5.052   -6.099  1   119.875 ? 42  ASN   B ND2  1 ? 2 
ATOM   2200 H H    . ASN   B 1 30  ? -30.925 6.076   -6.295  1   99.648  ? 42  ASN   B H    1 c 2 
ATOM   2201 H HA   . ASN   B 1 30  ? -31.436 6.891   -8.919  1   111.556 ? 42  ASN   B HA   1 c 2 
ATOM   2202 H HB2  . ASN   B 1 30  ? -33.742 7.245   -8.316  1   123.372 ? 42  ASN   B HB2  1 c 2 
ATOM   2203 H HB3  . ASN   B 1 30  ? -33.334 5.718   -8.445  1   120.644 ? 42  ASN   B HB3  1 c 2 
ATOM   2204 H HD21 . ASN   B 1 30  ? -33.486 4.784   -5.316  1   115.996 ? 42  ASN   B HD21 1 c 2 
ATOM   2205 H HD22 . ASN   B 1 30  ? -34.248 4.483   -6.617  1   122.642 ? 42  ASN   B HD22 1 c 2 
ATOM   2206 N N    . GLY   B 1 31  ? -31.274 9.304   -8.288  1   112.049 ? 43  GLY   B N    1 ? 2 
ATOM   2207 C CA   . GLY   B 1 31  ? -31.114 10.665  -7.818  1   113.458 ? 43  GLY   B CA   1 ? 2 
ATOM   2208 C C    . GLY   B 1 31  ? -29.648 11.082  -7.774  1   110.216 ? 43  GLY   B C    1 ? 2 
ATOM   2209 O O    . GLY   B 1 31  ? -28.752 10.246  -7.576  1   108.356 ? 43  GLY   B O    1 ? 2 
ATOM   2210 H H    . GLY   B 1 31  ? -31.271 9.136   -9.186  1   114.699 ? 43  GLY   B H    1 c 2 
ATOM   2211 H HA2  . GLY   B 1 31  ? -31.609 11.269  -8.42   1   118.435 ? 43  GLY   B HA2  1 c 2 
ATOM   2212 H HA3  . GLY   B 1 31  ? -31.506 10.748  -6.917  1   112.615 ? 43  GLY   B HA3  1 c 2 
ATOM   2213 N N    . GLU   B 1 32  ? -29.499 12.408  -7.917  1   112.888 ? 44  GLU   B N    1 ? 2 
ATOM   2214 C CA   . GLU   B 1 32  ? -28.258 13.116  -8.182  1   113.183 ? 44  GLU   B CA   1 ? 2 
ATOM   2215 C C    . GLU   B 1 32  ? -27.386 13.137  -6.909  1   108.567 ? 44  GLU   B C    1 ? 2 
ATOM   2216 O O    . GLU   B 1 32  ? -26.164 12.96   -6.984  1   104.724 ? 44  GLU   B O    1 ? 2 
ATOM   2217 C CB   . GLU   B 1 32  ? -28.681 14.465  -8.796  1   111.547 ? 44  GLU   B CB   1 ? 2 
ATOM   2218 H H    . GLU   B 1 32  ? -30.254 12.916  -7.825  1   116.778 ? 44  GLU   B H    1 c 2 
ATOM   2219 H HA   . GLU   B 1 32  ? -27.765 12.612  -8.879  1   110.835 ? 44  GLU   B HA   1 c 2 
ATOM   2220 H HB2  . GLU   B 1 32  ? -27.577 14.815  -9.011  0   30      ? 44  GLU   B HB2  1 c 2 
ATOM   2221 H HB3  . GLU   B 1 32  ? -29.411 14.554  -8.881  0   30      ? 44  GLU   B HB3  1 c 2 
ATOM   2222 N N    . GLU   B 1 33  ? -28.021 13.305  -5.73   1   105.095 ? 45  GLU   B N    1 ? 2 
ATOM   2223 C CA   . GLU   B 1 33  ? -27.337 13.691  -4.502  1   96.303  ? 45  GLU   B CA   1 ? 2 
ATOM   2224 C C    . GLU   B 1 33  ? -26.767 12.464  -3.786  1   89.868  ? 45  GLU   B C    1 ? 2 
ATOM   2225 O O    . GLU   B 1 33  ? -27.441 11.458  -3.579  1   84.029  ? 45  GLU   B O    1 ? 2 
ATOM   2226 C CB   . GLU   B 1 33  ? -28.266 14.507  -3.596  1   96.841  ? 45  GLU   B CB   1 ? 2 
ATOM   2227 H H    . GLU   B 1 33  ? -28.923 13.166  -5.697  1   106.86  ? 45  GLU   B H    1 c 2 
ATOM   2228 H HA   . GLU   B 1 33  ? -26.582 14.282  -4.751  1   96.839  ? 45  GLU   B HA   1 c 2 
ATOM   2229 H HB2  . GLU   B 1 33  ? -27.676 15.101  -2.903  0   30      ? 45  GLU   B HB2  1 c 2 
ATOM   2230 H HB3  . GLU   B 1 33  ? -29.172 14.41   -3.76   0   30      ? 45  GLU   B HB3  1 c 2 
ATOM   2231 N N    . THR   B 1 34  ? -25.488 12.578  -3.426  1   88.575  ? 46  THR   B N    1 ? 2 
ATOM   2232 C CA   . THR   B 1 34  ? -24.837 11.655  -2.516  1   83.265  ? 46  THR   B CA   1 ? 2 
ATOM   2233 C C    . THR   B 1 34  ? -24.76  12.281  -1.129  1   83.417  ? 46  THR   B C    1 ? 2 
ATOM   2234 O O    . THR   B 1 34  ? -24.853 13.489  -0.96   1   91.091  ? 46  THR   B O    1 ? 2 
ATOM   2235 C CB   . THR   B 1 34  ? -23.447 11.348  -3.059  1   81.907  ? 46  THR   B CB   1 ? 2 
ATOM   2236 O OG1  . THR   B 1 34  ? -22.741 12.578  -3.25   1   75.795  ? 46  THR   B OG1  1 ? 2 
ATOM   2237 C CG2  . THR   B 1 34  ? -23.518 10.578  -4.368  1   81.831  ? 46  THR   B CG2  1 ? 2 
ATOM   2238 H H    . THR   B 1 34  ? -24.994 13.268  -3.766  1   89.233  ? 46  THR   B H    1 c 2 
ATOM   2239 H HA   . THR   B 1 34  ? -25.357 10.825  -2.476  1   82.933  ? 46  THR   B HA   1 c 2 
ATOM   2240 H HB   . THR   B 1 34  ? -22.963 10.798  -2.399  1   76.329  ? 46  THR   B HB   1 c 2 
ATOM   2241 H HG1  . THR   B 1 34  ? -23.173 13.125  -3.76   0   30      ? 46  THR   B HG1  1 c 2 
ATOM   2242 H HG21 . THR   B 1 34  ? -22.626 10.287  -4.623  1   80.287  ? 46  THR   B HG21 1 c 2 
ATOM   2243 H HG22 . THR   B 1 34  ? -23.881 11.151  -5.064  1   85.675  ? 46  THR   B HG22 1 c 2 
ATOM   2244 H HG23 . THR   B 1 34  ? -24.091 9.801   -4.258  1   81.48   ? 46  THR   B HG23 1 c 2 
ATOM   2245 N N    . PRO   B 1 35  ? -24.635 11.486  -0.055  1   78.437  ? 47  PRO   B N    1 ? 2 
ATOM   2246 C CA   . PRO   B 1 35  ? -24.547 12.055  1.289   1   77.756  ? 47  PRO   B CA   1 ? 2 
ATOM   2247 C C    . PRO   B 1 35  ? -23.374 13.013  1.464   1   76.969  ? 47  PRO   B C    1 ? 2 
ATOM   2248 O O    . PRO   B 1 35  ? -22.297 12.718  0.982   1   77.579  ? 47  PRO   B O    1 ? 2 
ATOM   2249 C CB   . PRO   B 1 35  ? -24.332 10.831  2.188   1   70.295  ? 47  PRO   B CB   1 ? 2 
ATOM   2250 C CG   . PRO   B 1 35  ? -24.713 9.655   1.336   1   73.663  ? 47  PRO   B CG   1 ? 2 
ATOM   2251 C CD   . PRO   B 1 35  ? -24.605 10.027  -0.104  1   72.738  ? 47  PRO   B CD   1 ? 2 
ATOM   2252 H HA   . PRO   B 1 35  ? -25.387 12.504  1.518   1   80.031  ? 47  PRO   B HA   1 c 2 
ATOM   2253 H HB2  . PRO   B 1 35  ? -23.4   10.765  2.471   1   69.81   ? 47  PRO   B HB2  1 c 2 
ATOM   2254 H HB3  . PRO   B 1 35  ? -24.898 10.881  2.983   1   73.189  ? 47  PRO   B HB3  1 c 2 
ATOM   2255 H HG2  . PRO   B 1 35  ? -24.122 8.899   1.527   1   69.147  ? 47  PRO   B HG2  1 c 2 
ATOM   2256 H HG3  . PRO   B 1 35  ? -25.63  9.38    1.538   1   73.706  ? 47  PRO   B HG3  1 c 2 
ATOM   2257 H HD2  . PRO   B 1 35  ? -23.769 9.707   -0.496  1   71.817  ? 47  PRO   B HD2  1 c 2 
ATOM   2258 H HD3  . PRO   B 1 35  ? -25.359 9.679   -0.616  1   75.632  ? 47  PRO   B HD3  1 c 2 
ATOM   2259 N N    . MET   B 1 36  ? -23.596 14.138  2.152   1   84.369  ? 48  MET   B N    1 ? 2 
ATOM   2260 C CA   . MET   B 1 36  ? -22.55  15.077  2.537   1   84.904  ? 48  MET   B CA   1 ? 2 
ATOM   2261 C C    . MET   B 1 36  ? -21.997 14.655  3.901   1   80.916  ? 48  MET   B C    1 ? 2 
ATOM   2262 O O    . MET   B 1 36  ? -22.674 13.935  4.647   1   76.556  ? 48  MET   B O    1 ? 2 
ATOM   2263 C CB   . MET   B 1 36  ? -23.112 16.498  2.665   1   96.569  ? 48  MET   B CB   1 ? 2 
ATOM   2264 C CG   . MET   B 1 36  ? -23.71  17.087  1.387   1   101.769 ? 48  MET   B CG   1 ? 2 
ATOM   2265 S SD   . MET   B 1 36  ? -22.538 17.804  0.208   1   103.158 ? 48  MET   B SD   1 ? 2 
ATOM   2266 C CE   . MET   B 1 36  ? -21.796 16.56   -0.85   1   92.363  ? 48  MET   B CE   1 ? 2 
ATOM   2267 H H    . MET   B 1 36  ? -24.456 14.333  2.393   1   85.452  ? 48  MET   B H    1 c 2 
ATOM   2268 H HA   . MET   B 1 36  ? -21.825 15.056  1.862   1   84.712  ? 48  MET   B HA   1 c 2 
ATOM   2269 H HB2  . MET   B 1 36  ? -23.804 16.493  3.361   1   96.413  ? 48  MET   B HB2  1 c 2 
ATOM   2270 H HB3  . MET   B 1 36  ? -22.39  17.088  2.973   1   96.083  ? 48  MET   B HB3  1 c 2 
ATOM   2271 H HG2  . MET   B 1 36  ? -24.211 16.385  0.926   1   100.276 ? 48  MET   B HG2  1 c 2 
ATOM   2272 H HG3  . MET   B 1 36  ? -24.35  17.782  1.636   1   104.992 ? 48  MET   B HG3  1 c 2 
ATOM   2273 H HE1  . MET   B 1 36  ? -21.115 16.976  -1.41   1   95.151  ? 48  MET   B HE1  1 c 2 
ATOM   2274 H HE2  . MET   B 1 36  ? -21.386 15.868  -0.3    1   90.214  ? 48  MET   B HE2  1 c 2 
ATOM   2275 H HE3  . MET   B 1 36  ? -22.484 16.162  -1.415  1   94.3    ? 48  MET   B HE3  1 c 2 
ATOM   2276 N N    . ILE   B 1 37  ? -20.78  15.107  4.235   1   74.459  ? 49  ILE   B N    1 ? 2 
ATOM   2277 C CA   . ILE   B 1 37  ? -20.233 14.915  5.574   1   74.676  ? 49  ILE   B CA   1 ? 2 
ATOM   2278 C C    . ILE   B 1 37  ? -21.208 15.464  6.622   1   75.31   ? 49  ILE   B C    1 ? 2 
ATOM   2279 O O    . ILE   B 1 37  ? -21.654 16.592  6.517   1   73.771  ? 49  ILE   B O    1 ? 2 
ATOM   2280 C CB   . ILE   B 1 37  ? -18.878 15.624  5.721   1   83.049  ? 49  ILE   B CB   1 ? 2 
ATOM   2281 C CG1  . ILE   B 1 37  ? -17.824 15.146  4.653   1   88.484  ? 49  ILE   B CG1  1 ? 2 
ATOM   2282 C CG2  . ILE   B 1 37  ? -18.361 15.545  7.169   1   81.267  ? 49  ILE   B CG2  1 ? 2 
ATOM   2283 C CD1  . ILE   B 1 37  ? -17.177 13.805  4.902   1   94.921  ? 49  ILE   B CD1  1 ? 2 
ATOM   2284 H H    . ILE   B 1 37  ? -20.288 15.563  3.614   1   77.338  ? 49  ILE   B H    1 c 2 
ATOM   2285 H HA   . ILE   B 1 37  ? -20.105 13.96   5.727   1   72.034  ? 49  ILE   B HA   1 c 2 
ATOM   2286 H HB   . ILE   B 1 37  ? -19.043 16.571  5.538   1   85.822  ? 49  ILE   B HB   1 c 2 
ATOM   2287 H HG12 . ILE   B 1 37  ? -18.26  15.115  3.779   1   88.725  ? 49  ILE   B HG12 1 c 2 
ATOM   2288 H HG13 . ILE   B 1 37  ? -17.117 15.821  4.601   1   90.689  ? 49  ILE   B HG13 1 c 2 
ATOM   2289 H HG21 . ILE   B 1 37  ? -17.391 15.598  7.171   1   81.525  ? 49  ILE   B HG21 1 c 2 
ATOM   2290 H HG22 . ILE   B 1 37  ? -18.638 14.703  7.569   1   79.52   ? 49  ILE   B HG22 1 c 2 
ATOM   2291 H HG23 . ILE   B 1 37  ? -18.724 16.283  7.687   1   85.012  ? 49  ILE   B HG23 1 c 2 
ATOM   2292 H HD11 . ILE   B 1 37  ? -16.625 13.85   5.705   1   91.321  ? 49  ILE   B HD11 1 c 2 
ATOM   2293 H HD12 . ILE   B 1 37  ? -16.618 13.566  4.138   1   90.306  ? 49  ILE   B HD12 1 c 2 
ATOM   2294 H HD13 . ILE   B 1 37  ? -17.868 13.125  5.022   1   89.77   ? 49  ILE   B HD13 1 c 2 
ATOM   2295 N N    . GLY   B 1 38  ? -21.542 14.661  7.636   1   72.885  ? 50  GLY   B N    1 ? 2 
ATOM   2296 C CA   . GLY   B 1 38  ? -22.406 15.122  8.713   1   77.319  ? 50  GLY   B CA   1 ? 2 
ATOM   2297 C C    . GLY   B 1 38  ? -23.855 14.647  8.585   1   77.837  ? 50  GLY   B C    1 ? 2 
ATOM   2298 O O    . GLY   B 1 38  ? -24.636 14.797  9.535   1   80.28   ? 50  GLY   B O    1 ? 2 
ATOM   2299 H H    . GLY   B 1 38  ? -21.225 13.804  7.659   1   70.321  ? 50  GLY   B H    1 c 2 
ATOM   2300 H HA2  . GLY   B 1 38  ? -22.038 14.799  9.569   1   76.502  ? 50  GLY   B HA2  1 c 2 
ATOM   2301 H HA3  . GLY   B 1 38  ? -22.39  16.107  8.737   1   80.203  ? 50  GLY   B HA3  1 c 2 
ATOM   2302 N N    . ASP   B 1 39  ? -24.234 14.154  7.399   1   73.256  ? 51  ASP   B N    1 ? 2 
ATOM   2303 C CA   . ASP   B 1 39  ? -25.568 13.624  7.184   1   76.163  ? 51  ASP   B CA   1 ? 2 
ATOM   2304 C C    . ASP   B 1 39  ? -25.76  12.38   8.058   1   72.761  ? 51  ASP   B C    1 ? 2 
ATOM   2305 O O    . ASP   B 1 39  ? -24.824 11.618  8.298   1   64.417  ? 51  ASP   B O    1 ? 2 
ATOM   2306 C CB   . ASP   B 1 39  ? -25.825 13.346  5.704   1   77.172  ? 51  ASP   B CB   1 ? 2 
ATOM   2307 C CG   . ASP   B 1 39  ? -25.963 14.574  4.807   1   81.433  ? 51  ASP   B CG   1 ? 2 
ATOM   2308 O OD1  . ASP   B 1 39  ? -26.051 15.699  5.358   1   89.005  ? 51  ASP   B OD1  1 ? 2 
ATOM   2309 O OD2  . ASP   B 1 39  ? -26.004 14.396  3.557   1   80.27   ? 51  ASP   B OD2  1 ? 2 
ATOM   2310 H H    . ASP   B 1 39  ? -23.644 14.151  6.702   1   72.551  ? 51  ASP   B H    1 c 2 
ATOM   2311 H HA   . ASP   B 1 39  ? -26.216 14.306  7.472   1   79.746  ? 51  ASP   B HA   1 c 2 
ATOM   2312 H HB2  . ASP   B 1 39  ? -25.089 12.8    5.358   1   73.526  ? 51  ASP   B HB2  1 c 2 
ATOM   2313 H HB3  . ASP   B 1 39  ? -26.649 12.822  5.625   1   77.696  ? 51  ASP   B HB3  1 c 2 
ATOM   2314 N N    . LYS   B 1 40  ? -26.97  12.223  8.598   1   78.973  ? 52  LYS   B N    1 ? 2 
ATOM   2315 C CA   . LYS   B 1 40  ? -27.383 11      9.262   1   82.237  ? 52  LYS   B CA   1 ? 2 
ATOM   2316 C C    . LYS   B 1 40  ? -27.744 9.962   8.191   1   78.712  ? 52  LYS   B C    1 ? 2 
ATOM   2317 O O    . LYS   B 1 40  ? -28.637 10.197  7.375   1   81.471  ? 52  LYS   B O    1 ? 2 
ATOM   2318 C CB   . LYS   B 1 40  ? -28.579 11.354  10.164  1   89.94   ? 52  LYS   B CB   1 ? 2 
ATOM   2319 C CG   . LYS   B 1 40  ? -28.722 10.515  11.415  1   94.872  ? 52  LYS   B CG   1 ? 2 
ATOM   2320 C CD   . LYS   B 1 40  ? -30.045 10.746  12.152  1   104.338 ? 52  LYS   B CD   1 ? 2 
ATOM   2321 C CE   . LYS   B 1 40  ? -30.355 9.623   13.112  1   107.869 ? 52  LYS   B CE   1 ? 2 
ATOM   2322 N NZ   . LYS   B 1 40  ? -31.766 9.219   13.136  1   114.896 ? 52  LYS   B NZ   1 ? 2 
ATOM   2323 H H    . LYS   B 1 40  ? -27.569 12.911  8.54    1   82.476  ? 52  LYS   B H    1 c 2 
ATOM   2324 H HA   . LYS   B 1 40  ? -26.632 10.663  9.814   1   79.287  ? 52  LYS   B HA   1 c 2 
ATOM   2325 H HB2  . LYS   B 1 40  ? -28.499 12.293  10.436  1   92.436  ? 52  LYS   B HB2  1 c 2 
ATOM   2326 H HB3  . LYS   B 1 40  ? -29.403 11.269  9.64    1   92.171  ? 52  LYS   B HB3  1 c 2 
ATOM   2327 H HG2  . LYS   B 1 40  ? -28.654 9.568   11.165  1   92.275  ? 52  LYS   B HG2  1 c 2 
ATOM   2328 H HG3  . LYS   B 1 40  ? -27.977 10.722  12.02   1   93.681  ? 52  LYS   B HG3  1 c 2 
ATOM   2329 H HD2  . LYS   B 1 40  ? -29.992 11.59   12.651  1   106.624 ? 52  LYS   B HD2  1 c 2 
ATOM   2330 H HD3  . LYS   B 1 40  ? -30.771 10.822  11.496  1   105.703 ? 52  LYS   B HD3  1 c 2 
ATOM   2331 H HE2  . LYS   B 1 40  ? -29.817 8.845   12.887  1   104.002 ? 52  LYS   B HE2  1 c 2 
ATOM   2332 H HE3  . LYS   B 1 40  ? -30.102 9.903   14.01   1   109.447 ? 52  LYS   B HE3  1 c 2 
ATOM   2333 H HZ1  . LYS   B 1 40  ? -32.113 9.242   12.301  1   113.79  ? 52  LYS   B HZ1  1 c 2 
ATOM   2334 H HZ2  . LYS   B 1 40  ? -32.236 9.784   13.666  1   118.289 ? 52  LYS   B HZ2  1 c 2 
ATOM   2335 H HZ3  . LYS   B 1 40  ? -31.836 8.377   13.463  1   114.18  ? 52  LYS   B HZ3  1 c 2 
ATOM   2336 N N    . VAL   B 1 41  ? -27.079 8.796   8.239   1   75.945  ? 53  VAL   B N    1 ? 2 
ATOM   2337 C CA   . VAL   B 1 41  ? -27.175 7.783   7.194   1   74.689  ? 53  VAL   B CA   1 ? 2 
ATOM   2338 C C    . VAL   B 1 41  ? -27.736 6.459   7.722   1   73.566  ? 53  VAL   B C    1 ? 2 
ATOM   2339 O O    . VAL   B 1 41  ? -27.35  5.973   8.783   1   72.857  ? 53  VAL   B O    1 ? 2 
ATOM   2340 C CB   . VAL   B 1 41  ? -25.799 7.555   6.552   1   70.943  ? 53  VAL   B CB   1 ? 2 
ATOM   2341 C CG1  . VAL   B 1 41  ? -25.89  6.629   5.356   1   68.1    ? 53  VAL   B CG1  1 ? 2 
ATOM   2342 C CG2  . VAL   B 1 41  ? -25.189 8.864   6.101   1   73.252  ? 53  VAL   B CG2  1 ? 2 
ATOM   2343 H H    . VAL   B 1 41  ? -26.544 8.624   8.96    1   74.835  ? 53  VAL   B H    1 c 2 
ATOM   2344 H HA   . VAL   B 1 41  ? -27.778 8.117   6.503   1   76.114  ? 53  VAL   B HA   1 c 2 
ATOM   2345 H HB   . VAL   B 1 41  ? -25.214 7.145   7.232   1   69.274  ? 53  VAL   B HB   1 c 2 
ATOM   2346 H HG11 . VAL   B 1 41  ? -26.632 6.902   4.791   1   70.677  ? 53  VAL   B HG11 1 c 2 
ATOM   2347 H HG12 . VAL   B 1 41  ? -26.035 5.717   5.66    1   68.082  ? 53  VAL   B HG12 1 c 2 
ATOM   2348 H HG13 . VAL   B 1 41  ? -25.064 6.67    4.847   1   66.207  ? 53  VAL   B HG13 1 c 2 
ATOM   2349 H HG21 . VAL   B 1 41  ? -24.405 8.687   5.555   1   70.007  ? 53  VAL   B HG21 1 c 2 
ATOM   2350 H HG22 . VAL   B 1 41  ? -24.928 9.386   6.878   1   73.119  ? 53  VAL   B HG22 1 c 2 
ATOM   2351 H HG23 . VAL   B 1 41  ? -25.84  9.363   5.58    1   74.838  ? 53  VAL   B HG23 1 c 2 
ATOM   2352 N N    . TYR   B 1 42  ? -28.614 5.862   6.908   1   70.998  ? 54  TYR   B N    1 ? 2 
ATOM   2353 C CA   . TYR   B 1 42  ? -29.321 4.653   7.247   1   74.737  ? 54  TYR   B CA   1 ? 2 
ATOM   2354 C C    . TYR   B 1 42  ? -28.992 3.604   6.183   1   70.947  ? 54  TYR   B C    1 ? 2 
ATOM   2355 O O    . TYR   B 1 42  ? -29.303 3.811   5.002   1   72.358  ? 54  TYR   B O    1 ? 2 
ATOM   2356 C CB   . TYR   B 1 42  ? -30.831 4.939   7.267   1   81.823  ? 54  TYR   B CB   1 ? 2 
ATOM   2357 C CG   . TYR   B 1 42  ? -31.357 5.965   8.267   1   87.845  ? 54  TYR   B CG   1 ? 2 
ATOM   2358 C CD1  . TYR   B 1 42  ? -31.06  7.322   8.146   1   88.854  ? 54  TYR   B CD1  1 ? 2 
ATOM   2359 C CD2  . TYR   B 1 42  ? -32.229 5.595   9.281   1   95.037  ? 54  TYR   B CD2  1 ? 2 
ATOM   2360 C CE1  . TYR   B 1 42  ? -31.577 8.268   9.017   1   93.688  ? 54  TYR   B CE1  1 ? 2 
ATOM   2361 C CE2  . TYR   B 1 42  ? -32.751 6.533   10.16   1   99.972  ? 54  TYR   B CE2  1 ? 2 
ATOM   2362 C CZ   . TYR   B 1 42  ? -32.421 7.872   10.034  1   98.947  ? 54  TYR   B CZ   1 ? 2 
ATOM   2363 O OH   . TYR   B 1 42  ? -32.933 8.786   10.905  1   106.202 ? 54  TYR   B OH   1 ? 2 
ATOM   2364 H H    . TYR   B 1 42  ? -28.775 6.238   6.09    1   72.779  ? 54  TYR   B H    1 c 2 
ATOM   2365 H HA   . TYR   B 1 42  ? -29.03  4.331   8.14    1   73.982  ? 54  TYR   B HA   1 c 2 
ATOM   2366 H HB2  . TYR   B 1 42  ? -31.093 5.23    6.366   1   82.634  ? 54  TYR   B HB2  1 c 2 
ATOM   2367 H HB3  . TYR   B 1 42  ? -31.294 4.087   7.43    1   83.795  ? 54  TYR   B HB3  1 c 2 
ATOM   2368 H HD1  . TYR   B 1 42  ? -30.487 7.606   7.451   1   86.093  ? 54  TYR   B HD1  1 c 2 
ATOM   2369 H HD2  . TYR   B 1 42  ? -32.465 4.687   9.381   1   95.248  ? 54  TYR   B HD2  1 c 2 
ATOM   2370 H HE1  . TYR   B 1 42  ? -31.344 9.176   8.924   1   93.879  ? 54  TYR   B HE1  1 c 2 
ATOM   2371 H HE2  . TYR   B 1 42  ? -33.324 6.257   10.855  1   103.158 ? 54  TYR   B HE2  1 c 2 
ATOM   2372 H HH   . TYR   B 1 42  ? -32.619 9.655   10.503  0   30      ? 54  TYR   B HH   1 c 2 
ATOM   2373 N N    . VAL   B 1 43  ? -28.36  2.497   6.595   1   67.522  ? 55  VAL   B N    1 ? 2 
ATOM   2374 C CA   . VAL   B 1 43  ? -28.029 1.431   5.651   1   68.454  ? 55  VAL   B CA   1 ? 2 
ATOM   2375 C C    . VAL   B 1 43  ? -28.462 0.056   6.152   1   72.834  ? 55  VAL   B C    1 ? 2 
ATOM   2376 O O    . VAL   B 1 43  ? -28.596 -0.143  7.359   1   77.673  ? 55  VAL   B O    1 ? 2 
ATOM   2377 C CB   . VAL   B 1 43  ? -26.527 1.339   5.411   1   62.216  ? 55  VAL   B CB   1 ? 2 
ATOM   2378 C CG1  . VAL   B 1 43  ? -25.964 2.671   4.929   1   60.822  ? 55  VAL   B CG1  1 ? 2 
ATOM   2379 C CG2  . VAL   B 1 43  ? -25.831 0.794   6.66    1   59.977  ? 55  VAL   B CG2  1 ? 2 
ATOM   2380 H H    . VAL   B 1 43  ? -28.134 2.399   7.475   1   68.281  ? 55  VAL   B H    1 c 2 
ATOM   2381 H HA   . VAL   B 1 43  ? -28.475 1.611   4.803   1   69.421  ? 55  VAL   B HA   1 c 2 
ATOM   2382 H HB   . VAL   B 1 43  ? -26.389 0.683   4.689   1   61.867  ? 55  VAL   B HB   1 c 2 
ATOM   2383 H HG11 . VAL   B 1 43  ? -25.978 3.313   5.658   1   61.189  ? 55  VAL   B HG11 1 c 2 
ATOM   2384 H HG12 . VAL   B 1 43  ? -26.505 3.005   4.194   1   62.316  ? 55  VAL   B HG12 1 c 2 
ATOM   2385 H HG13 . VAL   B 1 43  ? -25.049 2.547   4.626   1   57.968  ? 55  VAL   B HG13 1 c 2 
ATOM   2386 H HG21 . VAL   B 1 43  ? -24.878 0.955   6.591   1   57.361  ? 55  VAL   B HG21 1 c 2 
ATOM   2387 H HG22 . VAL   B 1 43  ? -25.989 -0.162  6.733   1   61.117  ? 55  VAL   B HG22 1 c 2 
ATOM   2388 H HG23 . VAL   B 1 43  ? -26.177 1.242   7.448   1   61.963  ? 55  VAL   B HG23 1 c 2 
ATOM   2389 N N    . HIS   B 1 44  ? -28.533 -0.901  5.21    1   73.236  ? 56  HIS   B N    1 ? 2 
ATOM   2390 C CA   . HIS   B 1 44  ? -28.382 -2.314  5.536   1   77.292  ? 56  HIS   B CA   1 ? 2 
ATOM   2391 C C    . HIS   B 1 44  ? -27.076 -2.861  4.973   1   71.414  ? 56  HIS   B C    1 ? 2 
ATOM   2392 O O    . HIS   B 1 44  ? -26.659 -2.477  3.881   1   65.073  ? 56  HIS   B O    1 ? 2 
ATOM   2393 C CB   . HIS   B 1 44  ? -29.56  -3.151  5.036   1   84.374  ? 56  HIS   B CB   1 ? 2 
ATOM   2394 C CG   . HIS   B 1 44  ? -30.649 -3.317  6.048   1   93.509  ? 56  HIS   B CG   1 ? 2 
ATOM   2395 N ND1  . HIS   B 1 44  ? -30.425 -3.988  7.237   1   94.845  ? 56  HIS   B ND1  1 ? 2 
ATOM   2396 C CD2  . HIS   B 1 44  ? -31.927 -2.913  6.076   1   96.907  ? 56  HIS   B CD2  1 ? 2 
ATOM   2397 C CE1  . HIS   B 1 44  ? -31.54  -4.002  7.933   1   96.608  ? 56  HIS   B CE1  1 ? 2 
ATOM   2398 N NE2  . HIS   B 1 44  ? -32.455 -3.343  7.254   1   98.272  ? 56  HIS   B NE2  1 ? 2 
ATOM   2399 H H    . HIS   B 1 44  ? -28.68  -0.663  4.34    1   74.079  ? 56  HIS   B H    1 c 2 
ATOM   2400 H HA   . HIS   B 1 44  ? -28.343 -2.391  6.519   1   77.091  ? 56  HIS   B HA   1 c 2 
ATOM   2401 H HB2  . HIS   B 1 44  ? -29.933 -2.721  4.235   1   85.628  ? 56  HIS   B HB2  1 c 2 
ATOM   2402 H HB3  . HIS   B 1 44  ? -29.231 -4.038  4.774   1   84.539  ? 56  HIS   B HB3  1 c 2 
ATOM   2403 H HD1  . HIS   B 1 44  ? -29.634 -4.236  7.58    0   30      ? 56  HIS   B HD1  1 c 2 
ATOM   2404 H HD2  . HIS   B 1 44  ? -32.38  -2.428  5.414   1   97.867  ? 56  HIS   B HD2  1 c 2 
ATOM   2405 H HE1  . HIS   B 1 44  ? -31.654 -4.392  8.783   1   99.36   ? 56  HIS   B HE1  1 c 2 
ATOM   2406 H HE2  . HIS   B 1 44  ? -33.289 -3.208  7.556   0   30      ? 56  HIS   B HE2  1 c 2 
ATOM   2407 N N    . TYR   B 1 45  ? -26.474 -3.814  5.693   1   68.345  ? 57  TYR   B N    1 ? 2 
ATOM   2408 C CA   . TYR   B 1 45  ? -25.174 -4.276  5.258   1   62.566  ? 57  TYR   B CA   1 ? 2 
ATOM   2409 C C    . TYR   B 1 45  ? -24.987 -5.732  5.625   1   63.555  ? 57  TYR   B C    1 ? 2 
ATOM   2410 O O    . TYR   B 1 45  ? -25.591 -6.213  6.569   1   69.436  ? 57  TYR   B O    1 ? 2 
ATOM   2411 C CB   . TYR   B 1 45  ? -24.035 -3.423  5.808   1   55.487  ? 57  TYR   B CB   1 ? 2 
ATOM   2412 C CG   . TYR   B 1 45  ? -23.722 -3.685  7.26    1   54.8    ? 57  TYR   B CG   1 ? 2 
ATOM   2413 C CD1  . TYR   B 1 45  ? -24.376 -2.992  8.263   1   58.849  ? 57  TYR   B CD1  1 ? 2 
ATOM   2414 C CD2  . TYR   B 1 45  ? -22.733 -4.567  7.624   1   54.532  ? 57  TYR   B CD2  1 ? 2 
ATOM   2415 C CE1  . TYR   B 1 45  ? -24.095 -3.215  9.601   1   59.148  ? 57  TYR   B CE1  1 ? 2 
ATOM   2416 C CE2  . TYR   B 1 45  ? -22.458 -4.833  8.953   1   58.866  ? 57  TYR   B CE2  1 ? 2 
ATOM   2417 C CZ   . TYR   B 1 45  ? -23.164 -4.167  9.947   1   60.426  ? 57  TYR   B CZ   1 ? 2 
ATOM   2418 O OH   . TYR   B 1 45  ? -22.908 -4.456  11.246  1   57.675  ? 57  TYR   B OH   1 ? 2 
ATOM   2419 H H    . TYR   B 1 45  ? -26.866 -4.172  6.437   1   70.674  ? 57  TYR   B H    1 c 2 
ATOM   2420 H HA   . TYR   B 1 45  ? -25.149 -4.21   4.269   1   61.849  ? 57  TYR   B HA   1 c 2 
ATOM   2421 H HB2  . TYR   B 1 45  ? -23.229 -3.595  5.272   1   53.655  ? 57  TYR   B HB2  1 c 2 
ATOM   2422 H HB3  . TYR   B 1 45  ? -24.274 -2.475  5.699   1   55.595  ? 57  TYR   B HB3  1 c 2 
ATOM   2423 H HD1  . TYR   B 1 45  ? -25.045 -2.367  8.032   1   59.31   ? 57  TYR   B HD1  1 c 2 
ATOM   2424 H HD2  . TYR   B 1 45  ? -22.283 -5.057  6.954   1   53.975  ? 57  TYR   B HD2  1 c 2 
ATOM   2425 H HE1  . TYR   B 1 45  ? -24.592 -2.775  10.269  1   61.818  ? 57  TYR   B HE1  1 c 2 
ATOM   2426 H HE2  . TYR   B 1 45  ? -21.814 -5.48   9.183   1   57.473  ? 57  TYR   B HE2  1 c 2 
ATOM   2427 H HH   . TYR   B 1 45  ? -23.357 -3.994  11.787  0   30      ? 57  TYR   B HH   1 c 2 
ATOM   2428 N N    . LYS   B 1 46  ? -24.143 -6.39   4.834   1   59.848  ? 58  LYS   B N    1 ? 2 
ATOM   2429 C CA   . LYS   B 1 46  ? -23.577 -7.676  5.181   1   60.69   ? 58  LYS   B CA   1 ? 2 
ATOM   2430 C C    . LYS   B 1 46  ? -22.071 -7.529  5.088   1   54.309  ? 58  LYS   B C    1 ? 2 
ATOM   2431 O O    . LYS   B 1 46  ? -21.549 -6.837  4.218   1   57.646  ? 58  LYS   B O    1 ? 2 
ATOM   2432 C CB   . LYS   B 1 46  ? -24.13  -8.81   4.323   1   62.077  ? 58  LYS   B CB   1 ? 2 
ATOM   2433 C CG   . LYS   B 1 46  ? -25.643 -8.839  4.25    1   67.708  ? 58  LYS   B CG   1 ? 2 
ATOM   2434 C CD   . LYS   B 1 46  ? -26.167 -9.979  3.386   1   71.478  ? 58  LYS   B CD   1 ? 2 
ATOM   2435 C CE   . LYS   B 1 46  ? -27.437 -9.734  2.635   1   75.668  ? 58  LYS   B CE   1 ? 2 
ATOM   2436 N NZ   . LYS   B 1 46  ? -27.893 -11.015 2.049   1   80.412  ? 58  LYS   B NZ   1 ? 2 
ATOM   2437 H H    . LYS   B 1 46  ? -23.909 -6.017  4.033   1   58.881  ? 58  LYS   B H    1 c 2 
ATOM   2438 H HA   . LYS   B 1 46  ? -23.812 -7.87   6.123   1   61.332  ? 58  LYS   B HA   1 c 2 
ATOM   2439 H HB2  . LYS   B 1 46  ? -23.775 -8.721  3.413   1   61.49   ? 58  LYS   B HB2  1 c 2 
ATOM   2440 H HB3  . LYS   B 1 46  ? -23.817 -9.666  4.685   1   63.921  ? 58  LYS   B HB3  1 c 2 
ATOM   2441 H HG2  . LYS   B 1 46  ? -26.001 -8.932  5.16    1   69.015  ? 58  LYS   B HG2  1 c 2 
ATOM   2442 H HG3  . LYS   B 1 46  ? -25.959 -7.985  3.883   1   66.489  ? 58  LYS   B HG3  1 c 2 
ATOM   2443 H HD2  . LYS   B 1 46  ? -25.468 -10.22  2.742   1   69.995  ? 58  LYS   B HD2  1 c 2 
ATOM   2444 H HD3  . LYS   B 1 46  ? -26.296 -10.761 3.966   1   74.222  ? 58  LYS   B HD3  1 c 2 
ATOM   2445 H HE2  . LYS   B 1 46  ? -28.122 -9.389  3.235   1   77.152  ? 58  LYS   B HE2  1 c 2 
ATOM   2446 H HE3  . LYS   B 1 46  ? -27.287 -9.086  1.923   1   73.548  ? 58  LYS   B HE3  1 c 2 
ATOM   2447 H HZ1  . LYS   B 1 46  ? -28.082 -11.606 2.709   1   82.923  ? 58  LYS   B HZ1  1 c 2 
ATOM   2448 H HZ2  . LYS   B 1 46  ? -27.245 -11.359 1.517   1   79.355  ? 58  LYS   B HZ2  1 c 2 
ATOM   2449 H HZ3  . LYS   B 1 46  ? -28.64  -10.875 1.554   1   83.465  ? 58  LYS   B HZ3  1 c 2 
ATOM   2450 N N    . GLY   B 1 47  ? -21.384 -8.126  6.042   1   50.975  ? 59  GLY   B N    1 ? 2 
ATOM   2451 C CA   . GLY   B 1 47  ? -19.966 -7.891  6.201   1   45.719  ? 59  GLY   B CA   1 ? 2 
ATOM   2452 C C    . GLY   B 1 47  ? -19.277 -9.195  6.57    1   46.785  ? 59  GLY   B C    1 ? 2 
ATOM   2453 O O    . GLY   B 1 47  ? -19.864 -10.036 7.238   1   50.838  ? 59  GLY   B O    1 ? 2 
ATOM   2454 H H    . GLY   B 1 47  ? -21.804 -8.703  6.613   1   53.867  ? 59  GLY   B H    1 c 2 
ATOM   2455 H HA2  . GLY   B 1 47  ? -19.591 -7.539  5.362   1   44.337  ? 59  GLY   B HA2  1 c 2 
ATOM   2456 H HA3  . GLY   B 1 47  ? -19.821 -7.222  6.911   1   45.028  ? 59  GLY   B HA3  1 c 2 
ATOM   2457 N N    . LYS   B 1 48  ? -18.031 -9.33   6.139   1   44.84   ? 60  LYS   B N    1 ? 2 
ATOM   2458 C CA   . LYS   B 1 48  ? -17.184 -10.446 6.483   1   49.128  ? 60  LYS   B CA   1 ? 2 
ATOM   2459 C C    . LYS   B 1 48  ? -15.721 -10.053 6.362   1   47.344  ? 60  LYS   B C    1 ? 2 
ATOM   2460 O O    . LYS   B 1 48  ? -15.358 -9.08   5.707   1   46.641  ? 60  LYS   B O    1 ? 2 
ATOM   2461 C CB   . LYS   B 1 48  ? -17.366 -11.637 5.536   1   56.338  ? 60  LYS   B CB   1 ? 2 
ATOM   2462 C CG   . LYS   B 1 48  ? -17.632 -11.378 4.057   1   59.588  ? 60  LYS   B CG   1 ? 2 
ATOM   2463 C CD   . LYS   B 1 48  ? -17.695 -12.643 3.187   1   66.046  ? 60  LYS   B CD   1 ? 2 
ATOM   2464 C CE   . LYS   B 1 48  ? -16.39  -13.394 3.218   1   71.124  ? 60  LYS   B CE   1 ? 2 
ATOM   2465 N NZ   . LYS   B 1 48  ? -16.398 -14.597 2.375   1   79.507  ? 60  LYS   B NZ   1 ? 2 
ATOM   2466 H H    . LYS   B 1 48  ? -17.687 -8.681  5.594   1   43.257  ? 60  LYS   B H    1 c 2 
ATOM   2467 H HA   . LYS   B 1 48  ? -17.375 -10.715 7.414   1   51.129  ? 60  LYS   B HA   1 c 2 
ATOM   2468 H HB2  . LYS   B 1 48  ? -16.562 -12.194 5.603   1   56.465  ? 60  LYS   B HB2  1 c 2 
ATOM   2469 H HB3  . LYS   B 1 48  ? -18.112 -12.172 5.88    1   58.908  ? 60  LYS   B HB3  1 c 2 
ATOM   2470 H HG2  . LYS   B 1 48  ? -18.483 -10.895 3.975   1   59.334  ? 60  LYS   B HG2  1 c 2 
ATOM   2471 H HG3  . LYS   B 1 48  ? -16.924 -10.793 3.714   1   56.628  ? 60  LYS   B HG3  1 c 2 
ATOM   2472 H HD2  . LYS   B 1 48  ? -18.412 -13.228 3.515   1   69.323  ? 60  LYS   B HD2  1 c 2 
ATOM   2473 H HD3  . LYS   B 1 48  ? -17.9   -12.39  2.261   1   66.253  ? 60  LYS   B HD3  1 c 2 
ATOM   2474 H HE2  . LYS   B 1 48  ? -15.674 -12.805 2.919   1   68.314  ? 60  LYS   B HE2  1 c 2 
ATOM   2475 H HE3  . LYS   B 1 48  ? -16.191 -13.666 4.131   1   71.262  ? 60  LYS   B HE3  1 c 2 
ATOM   2476 H HZ1  . LYS   B 1 48  ? -16.423 -14.358 1.501   1   77.725  ? 60  LYS   B HZ1  1 c 2 
ATOM   2477 H HZ2  . LYS   B 1 48  ? -17.125 -15.101 2.567   1   80.728  ? 60  LYS   B HZ2  1 c 2 
ATOM   2478 H HZ3  . LYS   B 1 48  ? -15.649 -15.084 2.529   1   78.614  ? 60  LYS   B HZ3  1 c 2 
ATOM   2479 N N    . LEU   B 1 49  ? -14.902 -10.791 7.065   1   50.309  ? 61  LEU   B N    1 ? 2 
ATOM   2480 C CA   . LEU   B 1 49  ? -13.464 -10.713 6.958   1   51.73   ? 61  LEU   B CA   1 ? 2 
ATOM   2481 C C    . LEU   B 1 49  ? -13.122 -11.515 5.714   1   55.625  ? 61  LEU   B C    1 ? 2 
ATOM   2482 O O    . LEU   B 1 49  ? -13.866 -12.445 5.414   1   56.229  ? 61  LEU   B O    1 ? 2 
ATOM   2483 C CB   . LEU   B 1 49  ? -12.793 -11.371 8.159   1   52.048  ? 61  LEU   B CB   1 ? 2 
ATOM   2484 C CG   . LEU   B 1 49  ? -13.19  -10.822 9.52    1   56.226  ? 61  LEU   B CG   1 ? 2 
ATOM   2485 C CD1  . LEU   B 1 49  ? -12.387 -11.547 10.576  1   60.305  ? 61  LEU   B CD1  1 ? 2 
ATOM   2486 C CD2  . LEU   B 1 49  ? -12.95  -9.335  9.483   1   53.056  ? 61  LEU   B CD2  1 ? 2 
ATOM   2487 H H    . LEU   B 1 49  ? -15.257 -11.394 7.652   1   52.851  ? 61  LEU   B H    1 c 2 
ATOM   2488 H HA   . LEU   B 1 49  ? -13.175 -9.77   6.862   1   49.017  ? 61  LEU   B HA   1 c 2 
ATOM   2489 H HB2  . LEU   B 1 49  ? -13.013 -12.33  8.14    1   55.916  ? 61  LEU   B HB2  1 c 2 
ATOM   2490 H HB3  . LEU   B 1 49  ? -11.818 -11.28  8.057   1   52.674  ? 61  LEU   B HB3  1 c 2 
ATOM   2491 H HG   . LEU   B 1 49  ? -14.156 -10.994 9.668   1   56.95   ? 61  LEU   B HG   1 c 2 
ATOM   2492 H HD11 . LEU   B 1 49  ? -12.6   -12.495 10.553  1   62.443  ? 61  LEU   B HD11 1 c 2 
ATOM   2493 H HD12 . LEU   B 1 49  ? -12.604 -11.188 11.453  1   60.776  ? 61  LEU   B HD12 1 c 2 
ATOM   2494 H HD13 . LEU   B 1 49  ? -11.438 -11.425 10.404  1   59.116  ? 61  LEU   B HD13 1 c 2 
ATOM   2495 H HD21 . LEU   B 1 49  ? -13.694 -8.895  9.038   1   51.864  ? 61  LEU   B HD21 1 c 2 
ATOM   2496 H HD22 . LEU   B 1 49  ? -12.127 -9.149  9       1   51.629  ? 61  LEU   B HD22 1 c 2 
ATOM   2497 H HD23 . LEU   B 1 49  ? -12.874 -8.996  10.391  1   53.672  ? 61  LEU   B HD23 1 c 2 
ATOM   2498 N N    . SER   B 1 50  ? -12.011 -11.173 5.04    1   54.423  ? 62  SER   B N    1 ? 2 
ATOM   2499 C CA   . SER   B 1 50  ? -11.546 -11.959 3.881   1   65.294  ? 62  SER   B CA   1 ? 2 
ATOM   2500 C C    . SER   B 1 50  ? -11.046 -13.361 4.253   1   62.198  ? 62  SER   B C    1 ? 2 
ATOM   2501 O O    . SER   B 1 50  ? -11.269 -14.276 3.474   1   68.989  ? 62  SER   B O    1 ? 2 
ATOM   2502 C CB   . SER   B 1 50  ? -10.473 -11.219 3.134   1   62.001  ? 62  SER   B CB   1 ? 2 
ATOM   2503 O OG   . SER   B 1 50  ? -9.505  -10.803 4.091   1   67.128  ? 62  SER   B OG   1 ? 2 
ATOM   2504 H H    . SER   B 1 50  ? -11.531 -10.441 5.301   1   54.477  ? 62  SER   B H    1 c 2 
ATOM   2505 H HA   . SER   B 1 50  ? -12.317 -12.072 3.27    1   62.273  ? 62  SER   B HA   1 c 2 
ATOM   2506 H HB2  . SER   B 1 50  ? -10.061 -11.804 2.471   1   65.244  ? 62  SER   B HB2  1 c 2 
ATOM   2507 H HB3  . SER   B 1 50  ? -10.851 -10.441 2.688   1   62.162  ? 62  SER   B HB3  1 c 2 
ATOM   2508 H HG   . SER   B 1 50  ? -8.993  -10.381 3.45    0   30      ? 62  SER   B HG   1 c 2 
ATOM   2509 N N    . ASN   B 1 51  ? -10.438 -13.54  5.445   1   65.288  ? 63  ASN   B N    1 ? 2 
ATOM   2510 C CA   . ASN   B 1 51  ? -10.122 -14.869 5.967   1   69.505  ? 63  ASN   B CA   1 ? 2 
ATOM   2511 C C    . ASN   B 1 51  ? -11.338 -15.814 6.097   1   73.554  ? 63  ASN   B C    1 ? 2 
ATOM   2512 O O    . ASN   B 1 51  ? -11.148 -17     6.355   1   75.458  ? 63  ASN   B O    1 ? 2 
ATOM   2513 C CB   . ASN   B 1 51  ? -9.405  -14.802 7.308   1   70.872  ? 63  ASN   B CB   1 ? 2 
ATOM   2514 C CG   . ASN   B 1 51  ? -10.328 -14.476 8.469   1   79.116  ? 63  ASN   B CG   1 ? 2 
ATOM   2515 O OD1  . ASN   B 1 51  ? -11.45  -13.985 8.284   1   81.912  ? 63  ASN   B OD1  1 ? 2 
ATOM   2516 N ND2  . ASN   B 1 51  ? -9.883  -14.718 9.692   1   80.94   ? 63  ASN   B ND2  1 ? 2 
ATOM   2517 H H    . ASN   B 1 51  ? -10.211 -12.808 5.943   1   63.027  ? 63  ASN   B H    1 c 2 
ATOM   2518 H HA   . ASN   B 1 51  ? -9.496  -15.287 5.333   1   70.8    ? 63  ASN   B HA   1 c 2 
ATOM   2519 H HB2  . ASN   B 1 51  ? -8.973  -15.663 7.479   1   75.379  ? 63  ASN   B HB2  1 c 2 
ATOM   2520 H HB3  . ASN   B 1 51  ? -8.705  -14.121 7.259   1   70.578  ? 63  ASN   B HB3  1 c 2 
ATOM   2521 H HD21 . ASN   B 1 51  ? -10.455 -14.778 10.368  1   82.358  ? 63  ASN   B HD21 1 c 2 
ATOM   2522 H HD22 . ASN   B 1 51  ? -9.013  -14.821 9.834   1   81.734  ? 63  ASN   B HD22 1 c 2 
ATOM   2523 N N    . GLY   B 1 52  ? -12.578 -15.287 6.018   1   74.404  ? 64  GLY   B N    1 ? 2 
ATOM   2524 C CA   . GLY   B 1 52  ? -13.802 -16.076 5.893   1   79.486  ? 64  GLY   B CA   1 ? 2 
ATOM   2525 C C    . GLY   B 1 52  ? -14.313 -16.642 7.231   1   81.831  ? 64  GLY   B C    1 ? 2 
ATOM   2526 O O    . GLY   B 1 52  ? -15.096 -17.59  7.247   1   81.534  ? 64  GLY   B O    1 ? 2 
ATOM   2527 H H    . GLY   B 1 52  ? -12.663 -14.379 6.069   1   71.33   ? 64  GLY   B H    1 c 2 
ATOM   2528 H HA2  . GLY   B 1 52  ? -14.503 -15.509 5.495   1   77.358  ? 64  GLY   B HA2  1 c 2 
ATOM   2529 H HA3  . GLY   B 1 52  ? -13.634 -16.822 5.271   1   81.027  ? 64  GLY   B HA3  1 c 2 
ATOM   2530 N N    . LYS   B 1 53  ? -13.878 -16.065 8.357   1   79.133  ? 65  LYS   B N    1 ? 2 
ATOM   2531 C CA   . LYS   B 1 53  ? -14.11  -16.691 9.644   1   83.128  ? 65  LYS   B CA   1 ? 2 
ATOM   2532 C C    . LYS   B 1 53  ? -15.006 -15.793 10.531  1   82.189  ? 65  LYS   B C    1 ? 2 
ATOM   2533 O O    . LYS   B 1 53  ? -15.406 -16.248 11.6    1   89.976  ? 65  LYS   B O    1 ? 2 
ATOM   2534 C CB   . LYS   B 1 53  ? -12.758 -17.286 10.102  1   81.64   ? 65  LYS   B CB   1 ? 2 
ATOM   2535 H H    . LYS   B 1 53  ? -13.426 -15.271 8.321   1   76.277  ? 65  LYS   B H    1 c 2 
ATOM   2536 H HA   . LYS   B 1 53  ? -14.654 -17.499 9.471   1   85.836  ? 65  LYS   B HA   1 c 2 
ATOM   2537 H HB2  . LYS   B 1 53  ? -12.076 -16.662 9.687   0   30      ? 65  LYS   B HB2  1 c 2 
ATOM   2538 H HB3  . LYS   B 1 53  ? -12.928 -17.618 11.034  0   30      ? 65  LYS   B HB3  1 c 2 
ATOM   2539 N N    . LYS   B 1 54  ? -15.421 -14.578 10.099  1   75.746  ? 66  LYS   B N    1 ? 2 
ATOM   2540 C CA   . LYS   B 1 54  ? -16.476 -13.834 10.801  1   73.909  ? 66  LYS   B CA   1 ? 2 
ATOM   2541 C C    . LYS   B 1 54  ? -17.39  -13.122 9.796   1   73.229  ? 66  LYS   B C    1 ? 2 
ATOM   2542 O O    . LYS   B 1 54  ? -16.901 -12.586 8.79    1   67.981  ? 66  LYS   B O    1 ? 2 
ATOM   2543 C CB   . LYS   B 1 54  ? -15.954 -12.847 11.861  1   68.576  ? 66  LYS   B CB   1 ? 2 
ATOM   2544 H H    . LYS   B 1 54  ? -15.037 -14.203 9.359   1   73.056  ? 66  LYS   B H    1 c 2 
ATOM   2545 H HA   . LYS   B 1 54  ? -17.032 -14.495 11.286  1   77.755  ? 66  LYS   B HA   1 c 2 
ATOM   2546 H HB2  . LYS   B 1 54  ? -14.911 -12.886 11.812  0   30      ? 66  LYS   B HB2  1 c 2 
ATOM   2547 H HB3  . LYS   B 1 54  ? -16.62  -12.368 12.327  0   30      ? 66  LYS   B HB3  1 c 2 
ATOM   2548 N N    . PHE   B 1 55  ? -18.709 -13.107 10.106  1   71.995  ? 67  PHE   B N    1 ? 2 
ATOM   2549 C CA   . PHE   B 1 55  ? -19.746 -12.436 9.319   1   73.439  ? 67  PHE   B CA   1 ? 2 
ATOM   2550 C C    . PHE   B 1 55  ? -20.66  -11.6   10.21   1   73.922  ? 67  PHE   B C    1 ? 2 
ATOM   2551 O O    . PHE   B 1 55  ? -20.791 -11.842 11.403  1   80.438  ? 67  PHE   B O    1 ? 2 
ATOM   2552 C CB   . PHE   B 1 55  ? -20.731 -13.336 8.567   1   76.944  ? 67  PHE   B CB   1 ? 2 
ATOM   2553 C CG   . PHE   B 1 55  ? -19.932 -14.44  7.921   1   85.072  ? 67  PHE   B CG   1 ? 2 
ATOM   2554 C CD1  . PHE   B 1 55  ? -19.43  -15.493 8.698   1   95.624  ? 67  PHE   B CD1  1 ? 2 
ATOM   2555 C CD2  . PHE   B 1 55  ? -19.66  -14.408 6.561   1   86.143  ? 67  PHE   B CD2  1 ? 2 
ATOM   2556 C CE1  . PHE   B 1 55  ? -18.674 -16.5   8.115   1   101.603 ? 67  PHE   B CE1  1 ? 2 
ATOM   2557 C CE2  . PHE   B 1 55  ? -18.916 -15.43  5.979   1   93.41   ? 67  PHE   B CE2  1 ? 2 
ATOM   2558 C CZ   . PHE   B 1 55  ? -18.411 -16.462 6.752   1   97.998  ? 67  PHE   B CZ   1 ? 2 
ATOM   2559 H H    . PHE   B 1 55  ? -18.972 -13.546 10.863  1   76.632  ? 67  PHE   B H    1 c 2 
ATOM   2560 H HA   . PHE   B 1 55  ? -19.305 -11.836 8.665   1   69.156  ? 67  PHE   B HA   1 c 2 
ATOM   2561 H HB2  . PHE   B 1 55  ? -21.379 -13.719 9.2     1   82.21   ? 67  PHE   B HB2  1 c 2 
ATOM   2562 H HB3  . PHE   B 1 55  ? -21.197 -12.812 7.879   1   77.346  ? 67  PHE   B HB3  1 c 2 
ATOM   2563 H HD1  . PHE   B 1 55  ? -19.602 -15.513 9.626   1   96.39   ? 67  PHE   B HD1  1 c 2 
ATOM   2564 H HD2  . PHE   B 1 55  ? -19.994 -13.703 6.029   1   84.703  ? 67  PHE   B HD2  1 c 2 
ATOM   2565 H HE1  . PHE   B 1 55  ? -18.342 -17.209 8.642   1   102.637 ? 67  PHE   B HE1  1 c 2 
ATOM   2566 H HE2  . PHE   B 1 55  ? -18.734 -15.405 5.053   1   91.353  ? 67  PHE   B HE2  1 c 2 
ATOM   2567 H HZ   . PHE   B 1 55  ? -17.909 -17.152 6.348   1   99.273  ? 67  PHE   B HZ   1 c 2 
ATOM   2568 N N    . ASP   B 1 56  ? -21.346 -10.646 9.596   1   70.608  ? 68  ASP   B N    1 ? 2 
ATOM   2569 C CA   . ASP   B 1 56  ? -22.123 -9.691  10.365  1   72.881  ? 68  ASP   B CA   1 ? 2 
ATOM   2570 C C    . ASP   B 1 56  ? -23.13  -9.051  9.427   1   70.387  ? 68  ASP   B C    1 ? 2 
ATOM   2571 O O    . ASP   B 1 56  ? -22.742 -8.513  8.389   1   61.718  ? 68  ASP   B O    1 ? 2 
ATOM   2572 C CB   . ASP   B 1 56  ? -21.26  -8.651  11.079  1   67.331  ? 68  ASP   B CB   1 ? 2 
ATOM   2573 C CG   . ASP   B 1 56  ? -21.995 -7.498  11.76   1   68.316  ? 68  ASP   B CG   1 ? 2 
ATOM   2574 O OD1  . ASP   B 1 56  ? -23.061 -7.729  12.359  1   68.73   ? 68  ASP   B OD1  1 ? 2 
ATOM   2575 O OD2  . ASP   B 1 56  ? -21.504 -6.367  11.675  1   63.417  ? 68  ASP   B OD2  1 ? 2 
ATOM   2576 H H    . ASP   B 1 56  ? -21.33  -10.581 8.684   1   69.856  ? 68  ASP   B H    1 c 2 
ATOM   2577 H HA   . ASP   B 1 56  ? -22.615 -10.185 11.059  1   75.478  ? 68  ASP   B HA   1 c 2 
ATOM   2578 H HB2  . ASP   B 1 56  ? -20.724 -9.11   11.758  1   68.876  ? 68  ASP   B HB2  1 c 2 
ATOM   2579 H HB3  . ASP   B 1 56  ? -20.646 -8.267  10.418  1   64.432  ? 68  ASP   B HB3  1 c 2 
ATOM   2580 N N    . SER   B 1 57  ? -24.397 -9.091  9.839   1   73.473  ? 69  SER   B N    1 ? 2 
ATOM   2581 C CA   . SER   B 1 57  ? -25.427 -8.384  9.113   1   79.457  ? 69  SER   B CA   1 ? 2 
ATOM   2582 C C    . SER   B 1 57  ? -26.172 -7.399  10.017  1   83.725  ? 69  SER   B C    1 ? 2 
ATOM   2583 O O    . SER   B 1 57  ? -26.398 -7.655  11.2    1   94.062  ? 69  SER   B O    1 ? 2 
ATOM   2584 C CB   . SER   B 1 57  ? -26.368 -9.349  8.48    1   86.263  ? 69  SER   B CB   1 ? 2 
ATOM   2585 O OG   . SER   B 1 57  ? -27.481 -8.629  7.984   1   95.397  ? 69  SER   B OG   1 ? 2 
ATOM   2586 H H    . SER   B 1 57  ? -24.624 -9.567  10.585  1   78.023  ? 69  SER   B H    1 c 2 
ATOM   2587 H HA   . SER   B 1 57  ? -24.991 -7.865  8.393   1   75.624  ? 69  SER   B HA   1 c 2 
ATOM   2588 H HB2  . SER   B 1 57  ? -25.92  -9.814  7.748   1   86.137  ? 69  SER   B HB2  1 c 2 
ATOM   2589 H HB3  . SER   B 1 57  ? -26.663 -10.005 9.14    1   90.943  ? 69  SER   B HB3  1 c 2 
ATOM   2590 H HG   . SER   B 1 57  ? -27.946 -9.453  7.555   0   30      ? 69  SER   B HG   1 c 2 
ATOM   2591 N N    . SER   B 1 58  ? -26.598 -6.287  9.4     1   83.871  ? 70  SER   B N    1 ? 2 
ATOM   2592 C CA   . SER   B 1 58  ? -27.533 -5.354  9.997   1   81.478  ? 70  SER   B CA   1 ? 2 
ATOM   2593 C C    . SER   B 1 58  ? -28.813 -6.094  10.376  1   90.098  ? 70  SER   B C    1 ? 2 
ATOM   2594 O O    . SER   B 1 58  ? -29.419 -5.774  11.391  1   97.905  ? 70  SER   B O    1 ? 2 
ATOM   2595 C CB   . SER   B 1 58  ? -27.815 -4.16   9.108   1   76.189  ? 70  SER   B CB   1 ? 2 
ATOM   2596 O OG   . SER   B 1 58  ? -28.359 -4.479  7.84    1   74.708  ? 70  SER   B OG   1 ? 2 
ATOM   2597 H H    . SER   B 1 58  ? -26.283 -6.104  8.562   1   79.632  ? 70  SER   B H    1 c 2 
ATOM   2598 H HA   . SER   B 1 58  ? -27.124 -5.017  10.834  1   81.447  ? 70  SER   B HA   1 c 2 
ATOM   2599 H HB2  . SER   B 1 58  ? -28.432 -3.564  9.573   1   78.437  ? 70  SER   B HB2  1 c 2 
ATOM   2600 H HB3  . SER   B 1 58  ? -26.984 -3.667  8.977   1   72.435  ? 70  SER   B HB3  1 c 2 
ATOM   2601 H HG   . SER   B 1 58  ? -28.394 -3.796  7.598   0   30      ? 70  SER   B HG   1 c 2 
ATOM   2602 N N    . HIS   B 1 59  ? -29.153 -7.131  9.61    1   91.565  ? 71  HIS   B N    1 ? 2 
ATOM   2603 C CA   . HIS   B 1 59  ? -30.423 -7.817  9.733   1   101.033 ? 71  HIS   B CA   1 ? 2 
ATOM   2604 C C    . HIS   B 1 59  ? -30.516 -8.677  10.999  1   108.223 ? 71  HIS   B C    1 ? 2 
ATOM   2605 O O    . HIS   B 1 59  ? -31.623 -8.952  11.459  1   106.306 ? 71  HIS   B O    1 ? 2 
ATOM   2606 C CB   . HIS   B 1 59  ? -30.652 -8.653  8.477   1   102.91  ? 71  HIS   B CB   1 ? 2 
ATOM   2607 C CG   . HIS   B 1 59  ? -30.792 -7.877  7.217   1   98.701  ? 71  HIS   B CG   1 ? 2 
ATOM   2608 N ND1  . HIS   B 1 59  ? -29.756 -7.668  6.33    1   95.684  ? 71  HIS   B ND1  1 ? 2 
ATOM   2609 C CD2  . HIS   B 1 59  ? -31.873 -7.305  6.688   1   101.699 ? 71  HIS   B CD2  1 ? 2 
ATOM   2610 C CE1  . HIS   B 1 59  ? -30.2   -6.978  5.298   1   96.615  ? 71  HIS   B CE1  1 ? 2 
ATOM   2611 N NE2  . HIS   B 1 59  ? -31.49  -6.752  5.494   1   101.062 ? 71  HIS   B NE2  1 ? 2 
ATOM   2612 H H    . HIS   B 1 59  ? -28.57  -7.416  8.967   1   89.643  ? 71  HIS   B H    1 c 2 
ATOM   2613 H HA   . HIS   B 1 59  ? -31.13  -7.127  9.778   1   102.841 ? 71  HIS   B HA   1 c 2 
ATOM   2614 H HB2  . HIS   B 1 59  ? -29.905 -9.282  8.38    1   100.569 ? 71  HIS   B HB2  1 c 2 
ATOM   2615 H HB3  . HIS   B 1 59  ? -31.463 -9.191  8.606   1   107.705 ? 71  HIS   B HB3  1 c 2 
ATOM   2616 H HD1  . HIS   B 1 59  ? -28.968 -7.71   6.374   0   30      ? 71  HIS   B HD1  1 c 2 
ATOM   2617 H HD2  . HIS   B 1 59  ? -32.737 -7.286  7.052   1   106.923 ? 71  HIS   B HD2  1 c 2 
ATOM   2618 H HE1  . HIS   B 1 59  ? -29.692 -6.694  4.558   1   93.106  ? 71  HIS   B HE1  1 c 2 
ATOM   2619 H HE2  . HIS   B 1 59  ? -32.225 -6.43   4.875   0   30      ? 71  HIS   B HE2  1 c 2 
ATOM   2620 N N    . ASP   B 1 60  ? -29.357 -9.08   11.552  1   110.764 ? 72  ASP   B N    1 ? 2 
ATOM   2621 C CA   . ASP   B 1 60  ? -29.27  -9.803  12.818  1   116.076 ? 72  ASP   B CA   1 ? 2 
ATOM   2622 C C    . ASP   B 1 60  ? -29.695 -8.932  14.008  1   115.613 ? 72  ASP   B C    1 ? 2 
ATOM   2623 O O    . ASP   B 1 60  ? -29.94  -9.44   15.102  1   115.465 ? 72  ASP   B O    1 ? 2 
ATOM   2624 C CB   . ASP   B 1 60  ? -27.863 -10.333 13.065  1   116.464 ? 72  ASP   B CB   1 ? 2 
ATOM   2625 C CG   . ASP   B 1 60  ? -27.272 -11.167 11.933  1   116.893 ? 72  ASP   B CG   1 ? 2 
ATOM   2626 O OD1  . ASP   B 1 60  ? -28.056 -11.976 11.358  1   120.839 ? 72  ASP   B OD1  1 ? 2 
ATOM   2627 O OD2  . ASP   B 1 60  ? -26.043 -10.994 11.641  1   104.107 ? 72  ASP   B OD2  1 ? 2 
ATOM   2628 H H    . ASP   B 1 60  ? -28.579 -8.895  11.11   1   104.947 ? 72  ASP   B H    1 c 2 
ATOM   2629 H HA   . ASP   B 1 60  ? -29.875 -10.577 12.77   1   120.764 ? 72  ASP   B HA   1 c 2 
ATOM   2630 H HB2  . ASP   B 1 60  ? -27.266 -9.573  13.227  1   112.082 ? 72  ASP   B HB2  1 c 2 
ATOM   2631 H HB3  . ASP   B 1 60  ? -27.874 -10.885 13.875  1   119.708 ? 72  ASP   B HB3  1 c 2 
ATOM   2632 N N    . ARG   B 1 61  ? -29.747 -7.609  13.806  1   111.115 ? 73  ARG   B N    1 ? 2 
ATOM   2633 C CA   . ARG   B 1 61  ? -30.356 -6.701  14.771  1   110.841 ? 73  ARG   B CA   1 ? 2 
ATOM   2634 C C    . ARG   B 1 61  ? -31.815 -6.38   14.373  1   111.1   ? 73  ARG   B C    1 ? 2 
ATOM   2635 O O    . ARG   B 1 61  ? -32.433 -5.519  14.986  1   113.409 ? 73  ARG   B O    1 ? 2 
ATOM   2636 C CB   . ARG   B 1 61  ? -29.37  -5.526  14.925  1   101.936 ? 73  ARG   B CB   1 ? 2 
ATOM   2637 H H    . ARG   B 1 61  ? -29.378 -7.258  13.048  1   106.33  ? 73  ARG   B H    1 c 2 
ATOM   2638 H HA   . ARG   B 1 61  ? -30.383 -7.163  15.647  1   113.702 ? 73  ARG   B HA   1 c 2 
ATOM   2639 H HB2  . ARG   B 1 61  ? -28.543 -5.822  14.803  0   30      ? 73  ARG   B HB2  1 c 2 
ATOM   2640 H HB3  . ARG   B 1 61  ? -30.034 -4.717  14.91   0   30      ? 73  ARG   B HB3  1 c 2 
ATOM   2641 N N    . ASN   B 1 62  ? -32.397 -7.091  13.386  1   108.559 ? 74  ASN   B N    1 ? 2 
ATOM   2642 C CA   . ASN   B 1 62  ? -33.661 -6.723  12.749  1   111.454 ? 74  ASN   B CA   1 ? 2 
ATOM   2643 C C    . ASN   B 1 62  ? -33.874 -5.197  12.821  1   111.569 ? 74  ASN   B C    1 ? 2 
ATOM   2644 O O    . ASN   B 1 62  ? -34.864 -4.735  13.366  1   117.227 ? 74  ASN   B O    1 ? 2 
ATOM   2645 C CB   . ASN   B 1 62  ? -34.8   -7.608  13.28   1   116.867 ? 74  ASN   B CB   1 ? 2 
ATOM   2646 H H    . ASN   B 1 62  ? -31.988 -7.857  13.105  1   108.539 ? 74  ASN   B H    1 c 2 
ATOM   2647 H HA   . ASN   B 1 62  ? -33.569 -6.944  11.794  1   109.145 ? 74  ASN   B HA   1 c 2 
ATOM   2648 H HB2  . ASN   B 1 62  ? -34.401 -8.113  13.988  0   30      ? 74  ASN   B HB2  1 c 2 
ATOM   2649 H HB3  . ASN   B 1 62  ? -35.675 -7.094  13.121  0   30      ? 74  ASN   B HB3  1 c 2 
ATOM   2650 N N    . GLU   B 1 63  ? -32.939 -4.391  12.266  1   112.958 ? 75  GLU   B N    1 ? 2 
ATOM   2651 C CA   . GLU   B 1 63  ? -33.059 -2.93   12.212  1   112.902 ? 75  GLU   B CA   1 ? 2 
ATOM   2652 C C    . GLU   B 1 63  ? -31.911 -2.284  11.407  1   105.019 ? 75  GLU   B C    1 ? 2 
ATOM   2653 O O    . GLU   B 1 63  ? -30.742 -2.705  11.485  1   96.51   ? 75  GLU   B O    1 ? 2 
ATOM   2654 C CB   . GLU   B 1 63  ? -33.15  -2.27   13.599  1   120.154 ? 75  GLU   B CB   1 ? 2 
ATOM   2655 C CG   . GLU   B 1 63  ? -31.932 -2.472  14.508  1   119.298 ? 75  GLU   B CG   1 ? 2 
ATOM   2656 C CD   . GLU   B 1 63  ? -31.95  -1.749  15.862  1   125.284 ? 75  GLU   B CD   1 ? 2 
ATOM   2657 O OE1  . GLU   B 1 63  ? -30.845 -1.266  16.222  1   120.673 ? 75  GLU   B OE1  1 ? 2 
ATOM   2658 O OE2  . GLU   B 1 63  ? -33.002 -1.647  16.556  1   128.393 ? 75  GLU   B OE2  1 ? 2 
ATOM   2659 H H    . GLU   B 1 63  ? -32.192 -4.777  11.907  1   107.149 ? 75  GLU   B H    1 c 2 
ATOM   2660 H HA   . GLU   B 1 63  ? -33.907 -2.722  11.748  1   116.429 ? 75  GLU   B HA   1 c 2 
ATOM   2661 H HB2  . GLU   B 1 63  ? -33.274 -1.306  13.476  1   118.788 ? 75  GLU   B HB2  1 c 2 
ATOM   2662 H HB3  . GLU   B 1 63  ? -33.942 -2.612  14.062  1   124.955 ? 75  GLU   B HB3  1 c 2 
ATOM   2663 H HG2  . GLU   B 1 63  ? -31.826 -3.428  14.678  1   120.43  ? 75  GLU   B HG2  1 c 2 
ATOM   2664 H HG3  . GLU   B 1 63  ? -31.131 -2.181  14.024  1   114.035 ? 75  GLU   B HG3  1 c 2 
ATOM   2665 N N    . PRO   B 1 64  ? -32.167 -1.167  10.663  1   101.425 ? 76  PRO   B N    1 ? 2 
ATOM   2666 C CA   . PRO   B 1 64  ? -31.109 -0.495  9.932   1   90.924  ? 76  PRO   B CA   1 ? 2 
ATOM   2667 C C    . PRO   B 1 64  ? -29.906 -0.242  10.823  1   87.424  ? 76  PRO   B C    1 ? 2 
ATOM   2668 O O    . PRO   B 1 64  ? -30.01  -0.284  12.044  1   91.854  ? 76  PRO   B O    1 ? 2 
ATOM   2669 C CB   . PRO   B 1 64  ? -31.726 0.825   9.476   1   92.465  ? 76  PRO   B CB   1 ? 2 
ATOM   2670 C CG   . PRO   B 1 64  ? -32.972 1.021   10.328  1   102.643 ? 76  PRO   B CG   1 ? 2 
ATOM   2671 C CD   . PRO   B 1 64  ? -33.437 -0.404  10.598  1   106.555 ? 76  PRO   B CD   1 ? 2 
ATOM   2672 H HA   . PRO   B 1 64  ? -30.846 -1.034  9.158   1   89.901  ? 76  PRO   B HA   1 c 2 
ATOM   2673 H HB2  . PRO   B 1 64  ? -31.1   1.564   9.607   1   90.344  ? 76  PRO   B HB2  1 c 2 
ATOM   2674 H HB3  . PRO   B 1 64  ? -31.96  0.786   8.528   1   92.93   ? 76  PRO   B HB3  1 c 2 
ATOM   2675 H HG2  . PRO   B 1 64  ? -32.762 1.484   11.163  1   102.261 ? 76  PRO   B HG2  1 c 2 
ATOM   2676 H HG3  . PRO   B 1 64  ? -33.657 1.525   9.843   1   104.265 ? 76  PRO   B HG3  1 c 2 
ATOM   2677 H HD2  . PRO   B 1 64  ? -33.923 -0.462  11.442  1   110.558 ? 76  PRO   B HD2  1 c 2 
ATOM   2678 H HD3  . PRO   B 1 64  ? -34.004 -0.736  9.875   1   108.412 ? 76  PRO   B HD3  1 c 2 
ATOM   2679 N N    . PHE   B 1 65  ? -28.764 -0.022  10.181  1   80.256  ? 77  PHE   B N    1 ? 2 
ATOM   2680 C CA   . PHE   B 1 65  ? -27.584 0.541   10.81   1   78.394  ? 77  PHE   B CA   1 ? 2 
ATOM   2681 C C    . PHE   B 1 65  ? -27.562 2.035   10.497  1   78.388  ? 77  PHE   B C    1 ? 2 
ATOM   2682 O O    . PHE   B 1 65  ? -27.692 2.417   9.326   1   78.019  ? 77  PHE   B O    1 ? 2 
ATOM   2683 C CB   . PHE   B 1 65  ? -26.369 -0.193  10.254  1   74.758  ? 77  PHE   B CB   1 ? 2 
ATOM   2684 C CG   . PHE   B 1 65  ? -25.077 0.209   10.933  1   74.562  ? 77  PHE   B CG   1 ? 2 
ATOM   2685 C CD1  . PHE   B 1 65  ? -24.701 -0.392  12.132  1   78.272  ? 77  PHE   B CD1  1 ? 2 
ATOM   2686 C CD2  . PHE   B 1 65  ? -24.236 1.149   10.364  1   65.714  ? 77  PHE   B CD2  1 ? 2 
ATOM   2687 C CE1  . PHE   B 1 65  ? -23.535 -0.023  12.777  1   74.548  ? 77  PHE   B CE1  1 ? 2 
ATOM   2688 C CE2  . PHE   B 1 65  ? -23.09  1.529   11.03   1   67.863  ? 77  PHE   B CE2  1 ? 2 
ATOM   2689 C CZ   . PHE   B 1 65  ? -22.736 0.944   12.233  1   70.818  ? 77  PHE   B CZ   1 ? 2 
ATOM   2690 H H    . PHE   B 1 65  ? -28.717 -0.235  9.293   1   79.609  ? 77  PHE   B H    1 c 2 
ATOM   2691 H HA   . PHE   B 1 65  ? -27.633 0.403   11.793  1   80.479  ? 77  PHE   B HA   1 c 2 
ATOM   2692 H HB2  . PHE   B 1 65  ? -26.505 -1.16   10.369  1   76.256  ? 77  PHE   B HB2  1 c 2 
ATOM   2693 H HB3  . PHE   B 1 65  ? -26.299 -0.005  9.293   1   73.241  ? 77  PHE   B HB3  1 c 2 
ATOM   2694 H HD1  . PHE   B 1 65  ? -25.266 -1.04   12.522  1   80.024  ? 77  PHE   B HD1  1 c 2 
ATOM   2695 H HD2  . PHE   B 1 65  ? -24.484 1.579   9.56    1   67.288  ? 77  PHE   B HD2  1 c 2 
ATOM   2696 H HE1  . PHE   B 1 65  ? -23.3   -0.427  13.598  1   76.263  ? 77  PHE   B HE1  1 c 2 
ATOM   2697 H HE2  . PHE   B 1 65  ? -22.524 2.18    10.646  1   65.396  ? 77  PHE   B HE2  1 c 2 
ATOM   2698 H HZ   . PHE   B 1 65  ? -21.928 1.185   12.657  1   69.644  ? 77  PHE   B HZ   1 c 2 
ATOM   2699 N N    . VAL   B 1 66  ? -27.467 2.864   11.547  1   79.021  ? 78  VAL   B N    1 ? 2 
ATOM   2700 C CA   . VAL   B 1 66  ? -27.498 4.307   11.39   1   75.619  ? 78  VAL   B CA   1 ? 2 
ATOM   2701 C C    . VAL   B 1 66  ? -26.19  4.851   11.939  1   70.337  ? 78  VAL   B C    1 ? 2 
ATOM   2702 O O    . VAL   B 1 66  ? -25.573 4.291   12.855  1   67.897  ? 78  VAL   B O    1 ? 2 
ATOM   2703 C CB   . VAL   B 1 66  ? -28.707 4.986   12.051  1   85.707  ? 78  VAL   B CB   1 ? 2 
ATOM   2704 C CG1  . VAL   B 1 66  ? -29.069 6.285   11.352  1   87.677  ? 78  VAL   B CG1  1 ? 2 
ATOM   2705 C CG2  . VAL   B 1 66  ? -29.94  4.092   12.071  1   92.222  ? 78  VAL   B CG2  1 ? 2 
ATOM   2706 H H    . VAL   B 1 66  ? -27.378 2.516   12.388  1   79.737  ? 78  VAL   B H    1 c 2 
ATOM   2707 H HA   . VAL   B 1 66  ? -27.53  4.502   10.438  1   75.064  ? 78  VAL   B HA   1 c 2 
ATOM   2708 H HB   . VAL   B 1 66  ? -28.46  5.193   12.983  1   86.688  ? 78  VAL   B HB   1 c 2 
ATOM   2709 H HG11 . VAL   B 1 66  ? -29.381 6.094   10.452  1   86.717  ? 78  VAL   B HG11 1 c 2 
ATOM   2710 H HG12 . VAL   B 1 66  ? -28.286 6.859   11.308  1   85.023  ? 78  VAL   B HG12 1 c 2 
ATOM   2711 H HG13 . VAL   B 1 66  ? -29.773 6.735   11.848  1   91.34   ? 78  VAL   B HG13 1 c 2 
ATOM   2712 H HG21 . VAL   B 1 66  ? -30.707 4.603   12.379  1   95.404  ? 78  VAL   B HG21 1 c 2 
ATOM   2713 H HG22 . VAL   B 1 66  ? -29.79  3.343   12.672  1   91.997  ? 78  VAL   B HG22 1 c 2 
ATOM   2714 H HG23 . VAL   B 1 66  ? -30.113 3.758   11.175  1   90.343  ? 78  VAL   B HG23 1 c 2 
ATOM   2715 N N    . PHE   B 1 67  ? -25.7   5.897   11.278  1   67.263  ? 79  PHE   B N    1 ? 2 
ATOM   2716 C CA   . PHE   B 1 67  ? -24.468 6.542   11.689  1   63.327  ? 79  PHE   B CA   1 ? 2 
ATOM   2717 C C    . PHE   B 1 67  ? -24.392 7.897   10.989  1   64.774  ? 79  PHE   B C    1 ? 2 
ATOM   2718 O O    . PHE   B 1 67  ? -25.074 8.147   9.989   1   63.411  ? 79  PHE   B O    1 ? 2 
ATOM   2719 C CB   . PHE   B 1 67  ? -23.208 5.749   11.373  1   62.887  ? 79  PHE   B CB   1 ? 2 
ATOM   2720 C CG   . PHE   B 1 67  ? -22.824 5.691   9.899   1   58.133  ? 79  PHE   B CG   1 ? 2 
ATOM   2721 C CD1  . PHE   B 1 67  ? -23.566 4.928   8.998   1   58      ? 79  PHE   B CD1  1 ? 2 
ATOM   2722 C CD2  . PHE   B 1 67  ? -21.714 6.375   9.425   1   56.018  ? 79  PHE   B CD2  1 ? 2 
ATOM   2723 C CE1  . PHE   B 1 67  ? -23.232 4.866   7.657   1   54.82   ? 79  PHE   B CE1  1 ? 2 
ATOM   2724 C CE2  . PHE   B 1 67  ? -21.399 6.343   8.063   1   52.773  ? 79  PHE   B CE2  1 ? 2 
ATOM   2725 C CZ   . PHE   B 1 67  ? -22.156 5.592   7.181   1   51.761  ? 79  PHE   B CZ   1 ? 2 
ATOM   2726 H H    . PHE   B 1 67  ? -26.144 6.218   10.547  1   67.478  ? 79  PHE   B H    1 c 2 
ATOM   2727 H HA   . PHE   B 1 67  ? -24.506 6.695   12.671  1   66.918  ? 79  PHE   B HA   1 c 2 
ATOM   2728 H HB2  . PHE   B 1 67  ? -22.462 6.145   11.876  1   61.355  ? 79  PHE   B HB2  1 c 2 
ATOM   2729 H HB3  . PHE   B 1 67  ? -23.327 4.831   11.702  1   61.669  ? 79  PHE   B HB3  1 c 2 
ATOM   2730 H HD1  . PHE   B 1 67  ? -24.316 4.447   9.311   1   59.644  ? 79  PHE   B HD1  1 c 2 
ATOM   2731 H HD2  . PHE   B 1 67  ? -21.209 6.913   10.013  1   56.371  ? 79  PHE   B HD2  1 c 2 
ATOM   2732 H HE1  . PHE   B 1 67  ? -23.758 4.355   7.063   1   55.144  ? 79  PHE   B HE1  1 c 2 
ATOM   2733 H HE2  . PHE   B 1 67  ? -20.648 6.819   7.747   1   51.854  ? 79  PHE   B HE2  1 c 2 
ATOM   2734 H HZ   . PHE   B 1 67  ? -21.916 5.545   6.269   1   51.072  ? 79  PHE   B HZ   1 c 2 
ATOM   2735 N N    . SER   B 1 68  ? -23.572 8.783   11.542  1   63.097  ? 80  SER   B N    1 ? 2 
ATOM   2736 C CA   . SER   B 1 68  ? -23.434 10.111  10.967  1   66.391  ? 80  SER   B CA   1 ? 2 
ATOM   2737 C C    . SER   B 1 68  ? -22.117 10.107  10.186  1   61.356  ? 80  SER   B C    1 ? 2 
ATOM   2738 O O    . SER   B 1 68  ? -21.081 9.729   10.728  1   57.343  ? 80  SER   B O    1 ? 2 
ATOM   2739 C CB   . SER   B 1 68  ? -23.52  11.224  12.022  1   69.957  ? 80  SER   B CB   1 ? 2 
ATOM   2740 O OG   . SER   B 1 68  ? -24.876 11.523  12.397  1   73.519  ? 80  SER   B OG   1 ? 2 
ATOM   2741 H H    . SER   B 1 68  ? -23.089 8.564   12.286  1   64.194  ? 80  SER   B H    1 c 2 
ATOM   2742 H HA   . SER   B 1 68  ? -24.172 10.245  10.323  1   66.378  ? 80  SER   B HA   1 c 2 
ATOM   2743 H HB2  . SER   B 1 68  ? -23.022 10.95   12.815  1   70.02   ? 80  SER   B HB2  1 c 2 
ATOM   2744 H HB3  . SER   B 1 68  ? -23.1   12.031  11.669  1   70.238  ? 80  SER   B HB3  1 c 2 
ATOM   2745 H HG   . SER   B 1 68  ? -24.858 12.061  13.081  0   30      ? 80  SER   B HG   1 c 2 
ATOM   2746 N N    . LEU   B 1 69  ? -22.212 10.442  8.892   1   60.583  ? 81  LEU   B N    1 ? 2 
ATOM   2747 C CA   . LEU   B 1 69  ? -21.142 10.257  7.945   1   59.663  ? 81  LEU   B CA   1 ? 2 
ATOM   2748 C C    . LEU   B 1 69  ? -20.041 11.247  8.231   1   60.266  ? 81  LEU   B C    1 ? 2 
ATOM   2749 O O    . LEU   B 1 69  ? -20.32  12.439  8.361   1   62.182  ? 81  LEU   B O    1 ? 2 
ATOM   2750 C CB   . LEU   B 1 69  ? -21.664 10.44   6.53    1   64.839  ? 81  LEU   B CB   1 ? 2 
ATOM   2751 C CG   . LEU   B 1 69  ? -20.586 10.234  5.467   1   64.857  ? 81  LEU   B CG   1 ? 2 
ATOM   2752 C CD1  . LEU   B 1 69  ? -20.564 8.802   4.996   1   60.84   ? 81  LEU   B CD1  1 ? 2 
ATOM   2753 C CD2  . LEU   B 1 69  ? -20.683 11.205  4.311   1   75.747  ? 81  LEU   B CD2  1 ? 2 
ATOM   2754 H H    . LEU   B 1 69  ? -22.993 10.813  8.594   1   63.03   ? 81  LEU   B H    1 c 2 
ATOM   2755 H HA   . LEU   B 1 69  ? -20.79  9.337   8.048   1   57.669  ? 81  LEU   B HA   1 c 2 
ATOM   2756 H HB2  . LEU   B 1 69  ? -22.39  9.792   6.378   1   64.082  ? 81  LEU   B HB2  1 c 2 
ATOM   2757 H HB3  . LEU   B 1 69  ? -22.025 11.352  6.445   1   66.842  ? 81  LEU   B HB3  1 c 2 
ATOM   2758 H HG   . LEU   B 1 69  ? -19.708 10.399  5.896   1   64.81   ? 81  LEU   B HG   1 c 2 
ATOM   2759 H HD11 . LEU   B 1 69  ? -20.373 8.215   5.747   1   60.083  ? 81  LEU   B HD11 1 c 2 
ATOM   2760 H HD12 . LEU   B 1 69  ? -19.876 8.693   4.319   1   59.881  ? 81  LEU   B HD12 1 c 2 
ATOM   2761 H HD13 . LEU   B 1 69  ? -21.429 8.571   4.617   1   62.036  ? 81  LEU   B HD13 1 c 2 
ATOM   2762 H HD21 . LEU   B 1 69  ? -20.734 12.112  4.653   1   74.973  ? 81  LEU   B HD21 1 c 2 
ATOM   2763 H HD22 . LEU   B 1 69  ? -21.48  11.011  3.79    1   73.543  ? 81  LEU   B HD22 1 c 2 
ATOM   2764 H HD23 . LEU   B 1 69  ? -19.898 11.116  3.746   1   71.517  ? 81  LEU   B HD23 1 c 2 
ATOM   2765 N N    . GLY   B 1 70  ? -18.823 10.706  8.374   1   58.575  ? 82  GLY   B N    1 ? 2 
ATOM   2766 C CA   . GLY   B 1 70  ? -17.623 11.503  8.532   1   63.801  ? 82  GLY   B CA   1 ? 2 
ATOM   2767 C C    . GLY   B 1 70  ? -17.516 12.098  9.933   1   74.076  ? 82  GLY   B C    1 ? 2 
ATOM   2768 O O    . GLY   B 1 70  ? -16.678 12.974  10.15   1   77.501  ? 82  GLY   B O    1 ? 2 
ATOM   2769 H H    . GLY   B 1 70  ? -18.744 9.796   8.381   1   57.211  ? 82  GLY   B H    1 c 2 
ATOM   2770 H HA2  . GLY   B 1 70  ? -16.836 10.942  8.354   1   62.064  ? 82  GLY   B HA2  1 c 2 
ATOM   2771 H HA3  . GLY   B 1 70  ? -17.632 12.231  7.867   1   65.3    ? 82  GLY   B HA3  1 c 2 
ATOM   2772 N N    . LYS   B 1 71  ? -18.4   11.682  10.864  1   72.8    ? 83  LYS   B N    1 ? 2 
ATOM   2773 C CA   . LYS   B 1 71  ? -18.333 12.151  12.245  1   78.309  ? 83  LYS   B CA   1 ? 2 
ATOM   2774 C C    . LYS   B 1 71  ? -17.68  11.036  13.078  1   80.14   ? 83  LYS   B C    1 ? 2 
ATOM   2775 O O    . LYS   B 1 71  ? -18.043 10.88   14.244  1   93.204  ? 83  LYS   B O    1 ? 2 
ATOM   2776 C CB   . LYS   B 1 71  ? -19.684 12.75   12.704  1   76.676  ? 83  LYS   B CB   1 ? 2 
ATOM   2777 H H    . LYS   B 1 71  ? -19.047 11.078  10.638  1   72.312  ? 83  LYS   B H    1 c 2 
ATOM   2778 H HA   . LYS   B 1 71  ? -17.703 12.916  12.263  1   79.047  ? 83  LYS   B HA   1 c 2 
ATOM   2779 H HB2  . LYS   B 1 71  ? -19.442 13.257  13.465  0   30      ? 83  LYS   B HB2  1 c 2 
ATOM   2780 H HB3  . LYS   B 1 71  ? -20.277 12.069  12.304  0   30      ? 83  LYS   B HB3  1 c 2 
ATOM   2781 N N    . GLY   B 1 72  ? -16.796 10.218  12.452  1   75.564  ? 84  GLY   B N    1 ? 2 
ATOM   2782 C CA   . GLY   B 1 72  ? -15.864 9.314   13.13   1   79.422  ? 84  GLY   B CA   1 ? 2 
ATOM   2783 C C    . GLY   B 1 72  ? -16.427 7.989   13.693  1   73.408  ? 84  GLY   B C    1 ? 2 
ATOM   2784 O O    . GLY   B 1 72  ? -15.715 7.289   14.408  1   77.051  ? 84  GLY   B O    1 ? 2 
ATOM   2785 H H    . GLY   B 1 72  ? -16.783 10.223  11.539  1   74.893  ? 84  GLY   B H    1 c 2 
ATOM   2786 H HA2  . GLY   B 1 72  ? -15.141 9.097   12.495  1   75.011  ? 84  GLY   B HA2  1 c 2 
ATOM   2787 H HA3  . GLY   B 1 72  ? -15.45  9.812   13.873  1   79.716  ? 84  GLY   B HA3  1 c 2 
ATOM   2788 N N    . GLN   B 1 73  ? -17.663 7.594   13.393  1   64.736  ? 85  GLN   B N    1 ? 2 
ATOM   2789 C CA   . GLN   B 1 73  ? -18.284 6.443   14.06   1   67.952  ? 85  GLN   B CA   1 ? 2 
ATOM   2790 C C    . GLN   B 1 73  ? -18.059 5.068   13.39   1   62.292  ? 85  GLN   B C    1 ? 2 
ATOM   2791 O O    . GLN   B 1 73  ? -18.29  4.051   14.021  1   64.071  ? 85  GLN   B O    1 ? 2 
ATOM   2792 C CB   . GLN   B 1 73  ? -19.783 6.721   14.154  1   69.532  ? 85  GLN   B CB   1 ? 2 
ATOM   2793 C CG   . GLN   B 1 73  ? -20.088 7.93    15.027  1   75.658  ? 85  GLN   B CG   1 ? 2 
ATOM   2794 C CD   . GLN   B 1 73  ? -21.405 8.575   14.673  1   77.692  ? 85  GLN   B CD   1 ? 2 
ATOM   2795 O OE1  . GLN   B 1 73  ? -22.218 8.045   13.9    1   73.986  ? 85  GLN   B OE1  1 ? 2 
ATOM   2796 N NE2  . GLN   B 1 73  ? -21.57  9.778   15.19   1   84.804  ? 85  GLN   B NE2  1 ? 2 
ATOM   2797 H H    . GLN   B 1 73  ? -18.138 8.043   12.754  1   66.909  ? 85  GLN   B H    1 c 2 
ATOM   2798 H HA   . GLN   B 1 73  ? -17.93  6.396   14.985  1   68.924  ? 85  GLN   B HA   1 c 2 
ATOM   2799 H HB2  . GLN   B 1 73  ? -20.135 6.874   13.252  1   68.633  ? 85  GLN   B HB2  1 c 2 
ATOM   2800 H HB3  . GLN   B 1 73  ? -20.234 5.934   14.525  1   70.752  ? 85  GLN   B HB3  1 c 2 
ATOM   2801 H HG2  . GLN   B 1 73  ? -20.111 7.653   15.968  1   77.55   ? 85  GLN   B HG2  1 c 2 
ATOM   2802 H HG3  . GLN   B 1 73  ? -19.373 8.594   14.928  1   75.135  ? 85  GLN   B HG3  1 c 2 
ATOM   2803 H HE21 . GLN   B 1 73  ? -22.283 10.257  14.971  1   85.213  ? 85  GLN   B HE21 1 c 2 
ATOM   2804 H HE22 . GLN   B 1 73  ? -20.971 10.107  15.757  1   84.971  ? 85  GLN   B HE22 1 c 2 
ATOM   2805 N N    . VAL   B 1 74  ? -17.633 5.036   12.129  1   54.56   ? 86  VAL   B N    1 ? 2 
ATOM   2806 C CA   . VAL   B 1 74  ? -17.362 3.831   11.361  1   50.052  ? 86  VAL   B CA   1 ? 2 
ATOM   2807 C C    . VAL   B 1 74  ? -15.949 3.924   10.819  1   46.783  ? 86  VAL   B C    1 ? 2 
ATOM   2808 O O    . VAL   B 1 74  ? -15.319 4.938   10.942  1   49.146  ? 86  VAL   B O    1 ? 2 
ATOM   2809 C CB   . VAL   B 1 74  ? -18.365 3.734   10.202  1   47.776  ? 86  VAL   B CB   1 ? 2 
ATOM   2810 C CG1  . VAL   B 1 74  ? -19.752 3.371   10.745  1   51.095  ? 86  VAL   B CG1  1 ? 2 
ATOM   2811 C CG2  . VAL   B 1 74  ? -18.422 5.042   9.392   1   43.096  ? 86  VAL   B CG2  1 ? 2 
ATOM   2812 H H    . VAL   B 1 74  ? -17.488 5.839   11.716  1   55.023  ? 86  VAL   B H    1 c 2 
ATOM   2813 H HA   . VAL   B 1 74  ? -17.444 3.047   11.936  1   50.6    ? 86  VAL   B HA   1 c 2 
ATOM   2814 H HB   . VAL   B 1 74  ? -18.064 3.009   9.606   1   45.489  ? 86  VAL   B HB   1 c 2 
ATOM   2815 H HG11 . VAL   B 1 74  ? -20.065 4.077   11.337  1   52.873  ? 86  VAL   B HG11 1 c 2 
ATOM   2816 H HG12 . VAL   B 1 74  ? -19.699 2.536   11.239  1   51.228  ? 86  VAL   B HG12 1 c 2 
ATOM   2817 H HG13 . VAL   B 1 74  ? -20.375 3.27    10.006  1   50.622  ? 86  VAL   B HG13 1 c 2 
ATOM   2818 H HG21 . VAL   B 1 74  ? -18.904 4.887   8.562   1   43.807  ? 86  VAL   B HG21 1 c 2 
ATOM   2819 H HG22 . VAL   B 1 74  ? -17.521 5.342   9.189   1   43.513  ? 86  VAL   B HG22 1 c 2 
ATOM   2820 H HG23 . VAL   B 1 74  ? -18.883 5.725   9.907   1   46.458  ? 86  VAL   B HG23 1 c 2 
ATOM   2821 N N    . ILE   B 1 75  ? -15.466 2.863   10.192  1   46.929  ? 87  ILE   B N    1 ? 2 
ATOM   2822 C CA   . ILE   B 1 75  ? -14.139 2.837   9.601   1   41.841  ? 87  ILE   B CA   1 ? 2 
ATOM   2823 C C    . ILE   B 1 75  ? -14.046 3.839   8.446   1   38.148  ? 87  ILE   B C    1 ? 2 
ATOM   2824 O O    . ILE   B 1 75  ? -15.058 4.13    7.792   1   37.497  ? 87  ILE   B O    1 ? 2 
ATOM   2825 C CB   . ILE   B 1 75  ? -13.79  1.405   9.188   1   42.911  ? 87  ILE   B CB   1 ? 2 
ATOM   2826 C CG1  . ILE   B 1 75  ? -14.865 0.755   8.374   1   45.875  ? 87  ILE   B CG1  1 ? 2 
ATOM   2827 C CG2  . ILE   B 1 75  ? -13.458 0.539   10.39   1   46.899  ? 87  ILE   B CG2  1 ? 2 
ATOM   2828 C CD1  . ILE   B 1 75  ? -14.414 -0.566  7.778   1   45.391  ? 87  ILE   B CD1  1 ? 2 
ATOM   2829 H H    . ILE   B 1 75  ? -15.984 2.112   10.147  1   45.384  ? 87  ILE   B H    1 c 2 
ATOM   2830 H HA   . ILE   B 1 75  ? -13.503 3.112   10.289  1   43.448  ? 87  ILE   B HA   1 c 2 
ATOM   2831 H HB   . ILE   B 1 75  ? -12.989 1.452   8.629   1   42.745  ? 87  ILE   B HB   1 c 2 
ATOM   2832 H HG12 . ILE   B 1 75  ? -15.647 0.594   8.939   1   46.07   ? 87  ILE   B HG12 1 c 2 
ATOM   2833 H HG13 . ILE   B 1 75  ? -15.13  1.358   7.65    1   44.553  ? 87  ILE   B HG13 1 c 2 
ATOM   2834 H HG21 . ILE   B 1 75  ? -12.988 -0.26   10.097  1   45.507  ? 87  ILE   B HG21 1 c 2 
ATOM   2835 H HG22 . ILE   B 1 75  ? -14.278 0.282   10.843  1   47.053  ? 87  ILE   B HG22 1 c 2 
ATOM   2836 H HG23 . ILE   B 1 75  ? -12.893 1.035   11.004  1   47.192  ? 87  ILE   B HG23 1 c 2 
ATOM   2837 H HD11 . ILE   B 1 75  ? -13.506 -0.478  7.431   1   44.603  ? 87  ILE   B HD11 1 c 2 
ATOM   2838 H HD12 . ILE   B 1 75  ? -15.015 -0.816  7.052   1   44.95   ? 87  ILE   B HD12 1 c 2 
ATOM   2839 H HD13 . ILE   B 1 75  ? -14.432 -1.259  8.465   1   46.044  ? 87  ILE   B HD13 1 c 2 
ATOM   2840 N N    . LYS   B 1 76  ? -12.83  4.372   8.237   1   38.453  ? 88  LYS   B N    1 ? 2 
ATOM   2841 C CA   . LYS   B 1 76  ? -12.535 5.355   7.184   1   41.59   ? 88  LYS   B CA   1 ? 2 
ATOM   2842 C C    . LYS   B 1 76  ? -13.201 4.904   5.879   1   38.895  ? 88  LYS   B C    1 ? 2 
ATOM   2843 O O    . LYS   B 1 76  ? -13.926 5.658   5.247   1   40.017  ? 88  LYS   B O    1 ? 2 
ATOM   2844 C CB   . LYS   B 1 76  ? -11.017 5.561   7.021   1   40.532  ? 88  LYS   B CB   1 ? 2 
ATOM   2845 H H    . LYS   B 1 76  ? -12.145 4.108   8.782   1   39.541  ? 88  LYS   B H    1 c 2 
ATOM   2846 H HA   . LYS   B 1 76  ? -12.936 6.221   7.453   1   41.799  ? 88  LYS   B HA   1 c 2 
ATOM   2847 H HB2  . LYS   B 1 76  ? -10.615 4.996   7.496   0   30      ? 88  LYS   B HB2  1 c 2 
ATOM   2848 H HB3  . LYS   B 1 76  ? -11.028 6.331   6.272   0   30      ? 88  LYS   B HB3  1 c 2 
ATOM   2849 N N    . ALA   B 1 77  ? -13.073 3.622   5.544   1   35.257  ? 89  ALA   B N    1 ? 2 
ATOM   2850 C CA   . ALA   B 1 77  ? -13.609 3.102   4.283   1   36.907  ? 89  ALA   B CA   1 ? 2 
ATOM   2851 C C    . ALA   B 1 77  ? -15.102 3.303   4.136   1   42.285  ? 89  ALA   B C    1 ? 2 
ATOM   2852 O O    . ALA   B 1 77  ? -15.581 3.46    2.999   1   43.18   ? 89  ALA   B O    1 ? 2 
ATOM   2853 C CB   . ALA   B 1 77  ? -13.285 1.653   4.115   1   32.565  ? 89  ALA   B CB   1 ? 2 
ATOM   2854 H H    . ALA   B 1 77  ? -12.632 3.05    6.104   1   36.033  ? 89  ALA   B H    1 c 2 
ATOM   2855 H HA   . ALA   B 1 77  ? -13.168 3.606   3.544   1   36.985  ? 89  ALA   B HA   1 c 2 
ATOM   2856 H HB1  . ALA   B 1 77  ? -12.322 1.527   4.138   1   33.526  ? 89  ALA   B HB1  1 c 2 
ATOM   2857 H HB2  . ALA   B 1 77  ? -13.692 1.142   4.835   1   33.457  ? 89  ALA   B HB2  1 c 2 
ATOM   2858 H HB3  . ALA   B 1 77  ? -13.63  1.336   3.263   1   33.524  ? 89  ALA   B HB3  1 c 2 
ATOM   2859 N N    . TRP   B 1 78  ? -15.839 3.232   5.262   1   44.247  ? 90  TRP   B N    1 ? 2 
ATOM   2860 C CA   . TRP   B 1 78  ? -17.277 3.471   5.198   1   43.358  ? 90  TRP   B CA   1 ? 2 
ATOM   2861 C C    . TRP   B 1 78  ? -17.546 4.941   4.952   1   42.44   ? 90  TRP   B C    1 ? 2 
ATOM   2862 O O    . TRP   B 1 78  ? -18.377 5.279   4.142   1   46.892  ? 90  TRP   B O    1 ? 2 
ATOM   2863 C CB   . TRP   B 1 78  ? -17.996 2.996   6.471   1   44.018  ? 90  TRP   B CB   1 ? 2 
ATOM   2864 C CG   . TRP   B 1 78  ? -18.539 1.619   6.345   1   41.823  ? 90  TRP   B CG   1 ? 2 
ATOM   2865 C CD1  . TRP   B 1 78  ? -17.854 0.51    5.938   1   45.949  ? 90  TRP   B CD1  1 ? 2 
ATOM   2866 C CD2  . TRP   B 1 78  ? -19.898 1.201   6.526   1   45.397  ? 90  TRP   B CD2  1 ? 2 
ATOM   2867 N NE1  . TRP   B 1 78  ? -18.703 -0.56   5.821   1   44.083  ? 90  TRP   B NE1  1 ? 2 
ATOM   2868 C CE2  . TRP   B 1 78  ? -19.958 -0.168  6.196   1   45.521  ? 90  TRP   B CE2  1 ? 2 
ATOM   2869 C CE3  . TRP   B 1 78  ? -21.06  1.837   6.937   1   47.4    ? 90  TRP   B CE3  1 ? 2 
ATOM   2870 C CZ2  . TRP   B 1 78  ? -21.135 -0.899  6.287   1   47.696  ? 90  TRP   B CZ2  1 ? 2 
ATOM   2871 C CZ3  . TRP   B 1 78  ? -22.218 1.124   7.021   1   47.954  ? 90  TRP   B CZ3  1 ? 2 
ATOM   2872 C CH2  . TRP   B 1 78  ? -22.264 -0.224  6.674   1   50.027  ? 90  TRP   B CH2  1 ? 2 
ATOM   2873 H H    . TRP   B 1 78  ? -15.449 3.029   6.063   1   43.153  ? 90  TRP   B H    1 c 2 
ATOM   2874 H HA   . TRP   B 1 78  ? -17.642 2.956   4.429   1   43.093  ? 90  TRP   B HA   1 c 2 
ATOM   2875 H HB2  . TRP   B 1 78  ? -17.365 3.024   7.221   1   43.433  ? 90  TRP   B HB2  1 c 2 
ATOM   2876 H HB3  . TRP   B 1 78  ? -18.735 3.611   6.664   1   44.928  ? 90  TRP   B HB3  1 c 2 
ATOM   2877 H HD1  . TRP   B 1 78  ? -16.941 0.493   5.698   1   42.792  ? 90  TRP   B HD1  1 c 2 
ATOM   2878 H HE1  . TRP   B 1 78  ? -18.471 -1.365  5.601   1   44.397  ? 90  TRP   B HE1  1 c 2 
ATOM   2879 H HE3  . TRP   B 1 78  ? -21.045 2.75    7.168   1   47.517  ? 90  TRP   B HE3  1 c 2 
ATOM   2880 H HZ2  . TRP   B 1 78  ? -21.164 -1.81   6.049   1   48.084  ? 90  TRP   B HZ2  1 c 2 
ATOM   2881 H HZ3  . TRP   B 1 78  ? -23.008 1.558   7.297   1   50.91   ? 90  TRP   B HZ3  1 c 2 
ATOM   2882 H HH2  . TRP   B 1 78  ? -23.077 -0.692  6.746   1   51.686  ? 90  TRP   B HH2  1 c 2 
ATOM   2883 N N    . ASP   B 1 79  ? -16.846 5.823   5.636   1   43.532  ? 91  ASP   B N    1 ? 2 
ATOM   2884 C CA   . ASP   B 1 79  ? -17.034 7.243   5.405   1   47.875  ? 91  ASP   B CA   1 ? 2 
ATOM   2885 C C    . ASP   B 1 79  ? -16.778 7.573   3.933   1   52.839  ? 91  ASP   B C    1 ? 2 
ATOM   2886 O O    . ASP   B 1 79  ? -17.51  8.358   3.341   1   57.139  ? 91  ASP   B O    1 ? 2 
ATOM   2887 C CB   . ASP   B 1 79  ? -16.171 8.102   6.333   1   51.241  ? 91  ASP   B CB   1 ? 2 
ATOM   2888 C CG   . ASP   B 1 79  ? -16.671 8.316   7.77    1   55.809  ? 91  ASP   B CG   1 ? 2 
ATOM   2889 O OD1  . ASP   B 1 79  ? -17.864 8.173   8.008   1   53.621  ? 91  ASP   B OD1  1 ? 2 
ATOM   2890 O OD2  . ASP   B 1 79  ? -15.853 8.565   8.691   1   61.907  ? 91  ASP   B OD2  1 ? 2 
ATOM   2891 H H    . ASP   B 1 79  ? -16.243 5.547   6.265   1   43.532  ? 91  ASP   B H    1 c 2 
ATOM   2892 H HA   . ASP   B 1 79  ? -17.973 7.458   5.603   1   49.771  ? 91  ASP   B HA   1 c 2 
ATOM   2893 H HB2  . ASP   B 1 79  ? -15.281 7.698   6.385   1   50.26   ? 91  ASP   B HB2  1 c 2 
ATOM   2894 H HB3  . ASP   B 1 79  ? -16.068 8.987   5.924   1   52.815  ? 91  ASP   B HB3  1 c 2 
ATOM   2895 N N    . ILE   B 1 80  ? -15.692 7.019   3.35    1   52.864  ? 92  ILE   B N    1 ? 2 
ATOM   2896 C CA   . ILE   B 1 80  ? -15.347 7.239   1.95    1   51.171  ? 92  ILE   B CA   1 ? 2 
ATOM   2897 C C    . ILE   B 1 80  ? -16.376 6.588   1.03    1   48.056  ? 92  ILE   B C    1 ? 2 
ATOM   2898 O O    . ILE   B 1 80  ? -16.803 7.179   0.054   1   54.686  ? 92  ILE   B O    1 ? 2 
ATOM   2899 C CB   . ILE   B 1 80  ? -13.936 6.671   1.661   1   53.392  ? 92  ILE   B CB   1 ? 2 
ATOM   2900 C CG1  . ILE   B 1 80  ? -12.863 7.541   2.262   1   56.257  ? 92  ILE   B CG1  1 ? 2 
ATOM   2901 C CG2  . ILE   B 1 80  ? -13.676 6.454   0.167   1   53.403  ? 92  ILE   B CG2  1 ? 2 
ATOM   2902 C CD1  . ILE   B 1 80  ? -11.59  6.757   2.478   1   60.337  ? 92  ILE   B CD1  1 ? 2 
ATOM   2903 H H    . ILE   B 1 80  ? -15.146 6.488   3.855   1   50.784  ? 92  ILE   B H    1 c 2 
ATOM   2904 H HA   . ILE   B 1 80  ? -15.336 8.201   1.779   1   53.373  ? 92  ILE   B HA   1 c 2 
ATOM   2905 H HB   . ILE   B 1 80  ? -13.881 5.797   2.097   1   51.399  ? 92  ILE   B HB   1 c 2 
ATOM   2906 H HG12 . ILE   B 1 80  ? -12.682 8.294   1.663   1   58.771  ? 92  ILE   B HG12 1 c 2 
ATOM   2907 H HG13 . ILE   B 1 80  ? -13.174 7.896   3.12    1   57.182  ? 92  ILE   B HG13 1 c 2 
ATOM   2908 H HG21 . ILE   B 1 80  ? -12.722 6.36    0.01    1   53.878  ? 92  ILE   B HG21 1 c 2 
ATOM   2909 H HG22 . ILE   B 1 80  ? -14.01  7.215   -0.337  1   55.413  ? 92  ILE   B HG22 1 c 2 
ATOM   2910 H HG23 . ILE   B 1 80  ? -14.129 5.647   -0.131  1   52.765  ? 92  ILE   B HG23 1 c 2 
ATOM   2911 H HD11 . ILE   B 1 80  ? -11.781 5.959   3.007   1   57.128  ? 92  ILE   B HD11 1 c 2 
ATOM   2912 H HD12 . ILE   B 1 80  ? -10.946 7.313   2.956   1   59.933  ? 92  ILE   B HD12 1 c 2 
ATOM   2913 H HD13 . ILE   B 1 80  ? -11.211 6.492   1.619   1   58.901  ? 92  ILE   B HD13 1 c 2 
ATOM   2914 N N    . GLY   B 1 81  ? -16.701 5.329   1.291   1   46.471  ? 93  GLY   B N    1 ? 2 
ATOM   2915 C CA   . GLY   B 1 81  ? -17.491 4.534   0.37    1   47.185  ? 93  GLY   B CA   1 ? 2 
ATOM   2916 C C    . GLY   B 1 81  ? -18.934 5.013   0.309   1   51.12   ? 93  GLY   B C    1 ? 2 
ATOM   2917 O O    . GLY   B 1 81  ? -19.489 5.199   -0.761  1   49.081  ? 93  GLY   B O    1 ? 2 
ATOM   2918 H H    . GLY   B 1 81  ? -16.419 4.945   2.071   1   45.437  ? 93  GLY   B H    1 c 2 
ATOM   2919 H HA2  . GLY   B 1 81  ? -17.091 4.588   -0.527  1   48.199  ? 93  GLY   B HA2  1 c 2 
ATOM   2920 H HA3  . GLY   B 1 81  ? -17.469 3.591   0.656   1   46.408  ? 93  GLY   B HA3  1 c 2 
ATOM   2921 N N    . VAL   B 1 82  ? -19.53  5.223   1.488   1   58.124  ? 94  VAL   B N    1 ? 2 
ATOM   2922 C CA   . VAL   B 1 82  ? -20.938 5.528   1.558   1   55.439  ? 94  VAL   B CA   1 ? 2 
ATOM   2923 C C    . VAL   B 1 82  ? -21.172 6.923   1.014   1   55.463  ? 94  VAL   B C    1 ? 2 
ATOM   2924 O O    . VAL   B 1 82  ? -22.271 7.162   0.536   1   58.199  ? 94  VAL   B O    1 ? 2 
ATOM   2925 C CB   . VAL   B 1 82  ? -21.422 5.355   2.996   1   58.848  ? 94  VAL   B CB   1 ? 2 
ATOM   2926 C CG1  . VAL   B 1 82  ? -22.835 5.882   3.189   1   65.823  ? 94  VAL   B CG1  1 ? 2 
ATOM   2927 C CG2  . VAL   B 1 82  ? -21.33  3.89    3.398   1   56.305  ? 94  VAL   B CG2  1 ? 2 
ATOM   2928 H H    . VAL   B 1 82  ? -19.045 5.174   2.261   1   53.964  ? 94  VAL   B H    1 c 2 
ATOM   2929 H HA   . VAL   B 1 82  ? -21.419 4.892   0.993   1   57.009  ? 94  VAL   B HA   1 c 2 
ATOM   2930 H HB   . VAL   B 1 82  ? -20.819 5.876   3.575   1   57.986  ? 94  VAL   B HB   1 c 2 
ATOM   2931 H HG11 . VAL   B 1 82  ? -23.382 5.637   2.424   1   65.709  ? 94  VAL   B HG11 1 c 2 
ATOM   2932 H HG12 . VAL   B 1 82  ? -22.813 6.85    3.274   1   65.674  ? 94  VAL   B HG12 1 c 2 
ATOM   2933 H HG13 . VAL   B 1 82  ? -23.218 5.497   3.995   1   64.929  ? 94  VAL   B HG13 1 c 2 
ATOM   2934 H HG21 . VAL   B 1 82  ? -21.7   3.774   4.289   1   57.227  ? 94  VAL   B HG21 1 c 2 
ATOM   2935 H HG22 . VAL   B 1 82  ? -20.4   3.609   3.396   1   54.804  ? 94  VAL   B HG22 1 c 2 
ATOM   2936 H HG23 . VAL   B 1 82  ? -21.833 3.348   2.767   1   57.38   ? 94  VAL   B HG23 1 c 2 
ATOM   2937 N N    . ALA   B 1 83  ? -20.164 7.819   1.049   1   53.913  ? 95  ALA   B N    1 ? 2 
ATOM   2938 C CA   . ALA   B 1 83  ? -20.326 9.133   0.435   1   59.611  ? 95  ALA   B CA   1 ? 2 
ATOM   2939 C C    . ALA   B 1 83  ? -20.392 9.088   -1.087  1   58.623  ? 95  ALA   B C    1 ? 2 
ATOM   2940 O O    . ALA   B 1 83  ? -20.795 10.058  -1.708  1   66.439  ? 95  ALA   B O    1 ? 2 
ATOM   2941 C CB   . ALA   B 1 83  ? -19.205 10.069  0.837   1   61.822  ? 95  ALA   B CB   1 ? 2 
ATOM   2942 H H    . ALA   B 1 83  ? -19.377 7.614   1.466   1   53.194  ? 95  ALA   B H    1 c 2 
ATOM   2943 H HA   . ALA   B 1 83  ? -21.187 9.515   0.763   1   60.662  ? 95  ALA   B HA   1 c 2 
ATOM   2944 H HB1  . ALA   B 1 83  ? -19.094 10.05   1.802   1   60.392  ? 95  ALA   B HB1  1 c 2 
ATOM   2945 H HB2  . ALA   B 1 83  ? -18.377 9.789   0.413   1   60.104  ? 95  ALA   B HB2  1 c 2 
ATOM   2946 H HB3  . ALA   B 1 83  ? -19.419 10.975  0.557   1   63.718  ? 95  ALA   B HB3  1 c 2 
ATOM   2947 N N    . THR   B 1 84  ? -19.996 7.984   -1.708  1   60.692  ? 96  THR   B N    1 ? 2 
ATOM   2948 C CA   . THR   B 1 84  ? -20.167 7.814   -3.153  1   61.748  ? 96  THR   B CA   1 ? 2 
ATOM   2949 C C    . THR   B 1 84  ? -21.533 7.246   -3.554  1   63.45   ? 96  THR   B C    1 ? 2 
ATOM   2950 O O    . THR   B 1 84  ? -21.796 7.209   -4.735  1   68.442  ? 96  THR   B O    1 ? 2 
ATOM   2951 C CB   . THR   B 1 84  ? -19.074 6.9     -3.708  1   59.27   ? 96  THR   B CB   1 ? 2 
ATOM   2952 O OG1  . THR   B 1 84  ? -19.311 5.542   -3.322  1   52.607  ? 96  THR   B OG1  1 ? 2 
ATOM   2953 C CG2  . THR   B 1 84  ? -17.702 7.348   -3.244  1   57.915  ? 96  THR   B CG2  1 ? 2 
ATOM   2954 H H    . THR   B 1 84  ? -19.6   7.315   -1.23   1   57.162  ? 96  THR   B H    1 c 2 
ATOM   2955 H HA   . THR   B 1 84  ? -20.065 8.694   -3.576  1   63.975  ? 96  THR   B HA   1 c 2 
ATOM   2956 H HB   . THR   B 1 84  ? -19.092 6.954   -4.693  1   60.656  ? 96  THR   B HB   1 c 2 
ATOM   2957 H HG1  . THR   B 1 84  ? -19.258 5.52    -2.402  0   30      ? 96  THR   B HG1  1 c 2 
ATOM   2958 H HG21 . THR   B 1 84  ? -17.026 7.007   -3.853  1   57.948  ? 96  THR   B HG21 1 c 2 
ATOM   2959 H HG22 . THR   B 1 84  ? -17.534 7.007   -2.351  1   55.645  ? 96  THR   B HG22 1 c 2 
ATOM   2960 H HG23 . THR   B 1 84  ? -17.664 8.32    -3.231  1   59.487  ? 96  THR   B HG23 1 c 2 
ATOM   2961 N N    . MET   B 1 85  ? -22.396 6.816   -2.631  1   61.529  ? 97  MET   B N    1 ? 2 
ATOM   2962 C CA   . MET   B 1 85  ? -23.591 6.059   -3.007  1   63.199  ? 97  MET   B CA   1 ? 2 
ATOM   2963 C C    . MET   B 1 85  ? -24.844 6.941   -3.1    1   66.831  ? 97  MET   B C    1 ? 2 
ATOM   2964 O O    . MET   B 1 85  ? -24.939 7.979   -2.465  1   63.68   ? 97  MET   B O    1 ? 2 
ATOM   2965 C CB   . MET   B 1 85  ? -23.842 4.933   -1.997  1   61.032  ? 97  MET   B CB   1 ? 2 
ATOM   2966 C CG   . MET   B 1 85  ? -22.661 3.997   -1.807  1   55.372  ? 97  MET   B CG   1 ? 2 
ATOM   2967 S SD   . MET   B 1 85  ? -22.946 2.628   -0.672  1   56.727  ? 97  MET   B SD   1 ? 2 
ATOM   2968 C CE   . MET   B 1 85  ? -24.466 1.877   -1.234  1   63.159  ? 97  MET   B CE   1 ? 2 
ATOM   2969 H H    . MET   B 1 85  ? -22.245 6.993   -1.748  1   60.272  ? 97  MET   B H    1 c 2 
ATOM   2970 H HA   . MET   B 1 85  ? -23.432 5.658   -3.897  1   64.18   ? 97  MET   B HA   1 c 2 
ATOM   2971 H HB2  . MET   B 1 85  ? -24.072 5.335   -1.132  1   60.26   ? 97  MET   B HB2  1 c 2 
ATOM   2972 H HB3  . MET   B 1 85  ? -24.615 4.413   -2.3    1   62.577  ? 97  MET   B HB3  1 c 2 
ATOM   2973 H HG2  . MET   B 1 85  ? -22.407 3.628   -2.674  1   56.968  ? 97  MET   B HG2  1 c 2 
ATOM   2974 H HG3  . MET   B 1 85  ? -21.901 4.514   -1.475  1   54.747  ? 97  MET   B HG3  1 c 2 
ATOM   2975 H HE1  . MET   B 1 85  ? -24.706 1.146   -0.635  1   62.401  ? 97  MET   B HE1  1 c 2 
ATOM   2976 H HE2  . MET   B 1 85  ? -25.179 2.541   -1.232  1   64.58   ? 97  MET   B HE2  1 c 2 
ATOM   2977 H HE3  . MET   B 1 85  ? -24.344 1.531   -2.138  1   63.467  ? 97  MET   B HE3  1 c 2 
ATOM   2978 N N    . LYS   B 1 86  ? -25.837 6.49    -3.897  1   70.109  ? 98  LYS   B N    1 ? 2 
ATOM   2979 C CA   . LYS   B 1 86  ? -27.09  7.218   -4.107  1   74.564  ? 98  LYS   B CA   1 ? 2 
ATOM   2980 C C    . LYS   B 1 86  ? -28.181 6.5     -3.308  1   78.342  ? 98  LYS   B C    1 ? 2 
ATOM   2981 O O    . LYS   B 1 86  ? -27.956 5.371   -2.891  1   79.146  ? 98  LYS   B O    1 ? 2 
ATOM   2982 C CB   . LYS   B 1 86  ? -27.359 7.353   -5.612  1   73.751  ? 98  LYS   B CB   1 ? 2 
ATOM   2983 H H    . LYS   B 1 86  ? -25.726 5.688   -4.322  1   69.771  ? 98  LYS   B H    1 c 2 
ATOM   2984 H HA   . LYS   B 1 86  ? -26.985 8.13    -3.736  1   74.205  ? 98  LYS   B HA   1 c 2 
ATOM   2985 H HB2  . LYS   B 1 86  ? -26.371 7.411   -6.186  0   30      ? 98  LYS   B HB2  1 c 2 
ATOM   2986 H HB3  . LYS   B 1 86  ? -28.202 7.38    -5.864  0   30      ? 98  LYS   B HB3  1 c 2 
ATOM   2987 N N    . LYS   B 1 87  ? -29.355 7.122   -3.076  1   85.468  ? 99  LYS   B N    1 ? 2 
ATOM   2988 C CA   . LYS   B 1 87  ? -30.457 6.461   -2.369  1   86.843  ? 99  LYS   B CA   1 ? 2 
ATOM   2989 C C    . LYS   B 1 87  ? -30.799 5.201   -3.164  1   90.968  ? 99  LYS   B C    1 ? 2 
ATOM   2990 O O    . LYS   B 1 87  ? -30.879 5.23    -4.391  1   93.473  ? 99  LYS   B O    1 ? 2 
ATOM   2991 C CB   . LYS   B 1 87  ? -31.731 7.293   -2.089  1   88.793  ? 99  LYS   B CB   1 ? 2 
ATOM   2992 H H    . LYS   B 1 87  ? -29.471 7.981   -3.368  1   86.541  ? 99  LYS   B H    1 c 2 
ATOM   2993 H HA   . LYS   B 1 87  ? -30.109 6.176   -1.486  1   83.921  ? 99  LYS   B HA   1 c 2 
ATOM   2994 H HB2  . LYS   B 1 87  ? -31.309 8.323   -2.265  0   30      ? 99  LYS   B HB2  1 c 2 
ATOM   2995 H HB3  . LYS   B 1 87  ? -32.413 6.85    -2.522  0   30      ? 99  LYS   B HB3  1 c 2 
ATOM   2996 N N    . GLY   B 1 88  ? -30.907 4.067   -2.471  1   92.126  ? 100 GLY   B N    1 ? 2 
ATOM   2997 C CA   . GLY   B 1 88  ? -31.299 2.827   -3.123  1   98.31   ? 100 GLY   B CA   1 ? 2 
ATOM   2998 C C    . GLY   B 1 88  ? -30.152 2.103   -3.831  1   94.604  ? 100 GLY   B C    1 ? 2 
ATOM   2999 O O    . GLY   B 1 88  ? -30.399 1.136   -4.551  1   98.036  ? 100 GLY   B O    1 ? 2 
ATOM   3000 H H    . GLY   B 1 88  ? -30.734 4.061   -1.574  1   90.204  ? 100 GLY   B H    1 c 2 
ATOM   3001 H HA2  . GLY   B 1 88  ? -31.686 2.225   -2.444  1   97.798  ? 100 GLY   B HA2  1 c 2 
ATOM   3002 H HA3  . GLY   B 1 88  ? -32.009 3.025   -3.779  1   101.493 ? 100 GLY   B HA3  1 c 2 
ATOM   3003 N N    . GLU   B 1 89  ? -28.91  2.561   -3.615  1   92.21   ? 101 GLU   B N    1 ? 2 
ATOM   3004 C CA   . GLU   B 1 89  ? -27.747 1.907   -4.197  1   84.827  ? 101 GLU   B CA   1 ? 2 
ATOM   3005 C C    . GLU   B 1 89  ? -27.375 0.724   -3.303  1   76.822  ? 101 GLU   B C    1 ? 2 
ATOM   3006 O O    . GLU   B 1 89  ? -27.449 0.794   -2.074  1   68.237  ? 101 GLU   B O    1 ? 2 
ATOM   3007 C CB   . GLU   B 1 89  ? -26.644 2.926   -4.503  1   80.589  ? 101 GLU   B CB   1 ? 2 
ATOM   3008 C CG   . GLU   B 1 89  ? -25.493 2.44    -5.387  1   79.588  ? 101 GLU   B CG   1 ? 2 
ATOM   3009 C CD   . GLU   B 1 89  ? -24.293 3.371   -5.48   1   75.25   ? 101 GLU   B CD   1 ? 2 
ATOM   3010 O OE1  . GLU   B 1 89  ? -24.378 4.533   -5.98   1   82.495  ? 101 GLU   B OE1  1 ? 2 
ATOM   3011 O OE2  . GLU   B 1 89  ? -23.243 2.923   -4.975  1   66.515  ? 101 GLU   B OE2  1 ? 2 
ATOM   3012 H H    . GLU   B 1 89  ? -28.781 3.294   -3.086  1   89.154  ? 101 GLU   B H    1 c 2 
ATOM   3013 H HA   . GLU   B 1 89  ? -28.024 1.543   -5.073  1   87.053  ? 101 GLU   B HA   1 c 2 
ATOM   3014 H HB2  . GLU   B 1 89  ? -27.053 3.702   -4.939  1   83.575  ? 101 GLU   B HB2  1 c 2 
ATOM   3015 H HB3  . GLU   B 1 89  ? -26.263 3.232   -3.654  1   78.293  ? 101 GLU   B HB3  1 c 2 
ATOM   3016 H HG2  . GLU   B 1 89  ? -25.184 1.572   -5.051  1   77.223  ? 101 GLU   B HG2  1 c 2 
ATOM   3017 H HG3  . GLU   B 1 89  ? -25.836 2.292   -6.295  1   82.224  ? 101 GLU   B HG3  1 c 2 
ATOM   3018 N N    . ILE   B 1 90  ? -27.125 -0.41   -3.965  1   76.35   ? 102 ILE   B N    1 ? 2 
ATOM   3019 C CA   . ILE   B 1 90  ? -26.334 -1.476  -3.381  1   72.558  ? 102 ILE   B CA   1 ? 2 
ATOM   3020 C C    . ILE   B 1 90  ? -24.97  -1.483  -4.06   1   66.446  ? 102 ILE   B C    1 ? 2 
ATOM   3021 O O    . ILE   B 1 90  ? -24.859 -1.505  -5.293  1   68.031  ? 102 ILE   B O    1 ? 2 
ATOM   3022 C CB   . ILE   B 1 90  ? -26.998 -2.857  -3.489  1   71.86   ? 102 ILE   B CB   1 ? 2 
ATOM   3023 C CG1  . ILE   B 1 90  ? -28.441 -2.879  -2.925  1   77.154  ? 102 ILE   B CG1  1 ? 2 
ATOM   3024 C CG2  . ILE   B 1 90  ? -26.109 -3.861  -2.785  1   68.069  ? 102 ILE   B CG2  1 ? 2 
ATOM   3025 C CD1  . ILE   B 1 90  ? -29.249 -4.097  -3.34   1   80.411  ? 102 ILE   B CD1  1 ? 2 
ATOM   3026 H H    . ILE   B 1 90  ? -27.462 -0.524  -4.807  1   79.496  ? 102 ILE   B H    1 c 2 
ATOM   3027 H HA   . ILE   B 1 90  ? -26.21  -1.276  -2.438  1   68.987  ? 102 ILE   B HA   1 c 2 
ATOM   3028 H HB   . ILE   B 1 90  ? -27.041 -3.098  -4.436  1   74.884  ? 102 ILE   B HB   1 c 2 
ATOM   3029 H HG12 . ILE   B 1 90  ? -28.396 -2.85   -1.948  1   74.704  ? 102 ILE   B HG12 1 c 2 
ATOM   3030 H HG13 . ILE   B 1 90  ? -28.91  -2.075  -3.227  1   77.948  ? 102 ILE   B HG13 1 c 2 
ATOM   3031 H HG21 . ILE   B 1 90  ? -26.602 -4.683  -2.63   1   70.74   ? 102 ILE   B HG21 1 c 2 
ATOM   3032 H HG22 . ILE   B 1 90  ? -25.816 -3.497  -1.932  1   65.643  ? 102 ILE   B HG22 1 c 2 
ATOM   3033 H HG23 . ILE   B 1 90  ? -25.332 -4.053  -3.336  1   67.015  ? 102 ILE   B HG23 1 c 2 
ATOM   3034 H HD11 . ILE   B 1 90  ? -29.461 -4.04   -4.291  1   83.571  ? 102 ILE   B HD11 1 c 2 
ATOM   3035 H HD12 . ILE   B 1 90  ? -30.077 -4.123  -2.825  1   83.545  ? 102 ILE   B HD12 1 c 2 
ATOM   3036 H HD13 . ILE   B 1 90  ? -28.739 -4.911  -3.17   1   79.864  ? 102 ILE   B HD13 1 c 2 
ATOM   3037 N N    . ALA   B 1 91  ? -23.962 -1.546  -3.209  1   59.279  ? 103 ALA   B N    1 ? 2 
ATOM   3038 C CA   . ALA   B 1 91  ? -22.564 -1.596  -3.61   1   62.039  ? 103 ALA   B CA   1 ? 2 
ATOM   3039 C C    . ALA   B 1 91  ? -21.818 -2.66   -2.803  1   58.127  ? 103 ALA   B C    1 ? 2 
ATOM   3040 O O    . ALA   B 1 91  ? -22.191 -2.947  -1.677  1   60.649  ? 103 ALA   B O    1 ? 2 
ATOM   3041 C CB   . ALA   B 1 91  ? -21.9   -0.232  -3.441  1   60.063  ? 103 ALA   B CB   1 ? 2 
ATOM   3042 H H    . ALA   B 1 91  ? -24.15  -1.561  -2.315  1   60.181  ? 103 ALA   B H    1 c 2 
ATOM   3043 H HA   . ALA   B 1 91  ? -22.528 -1.855  -4.57   1   62.575  ? 103 ALA   B HA   1 c 2 
ATOM   3044 H HB1  . ALA   B 1 91  ? -22.383 0.434   -3.958  1   61.891  ? 103 ALA   B HB1  1 c 2 
ATOM   3045 H HB2  . ALA   B 1 91  ? -21.908 0.021   -2.502  1   58.313  ? 103 ALA   B HB2  1 c 2 
ATOM   3046 H HB3  . ALA   B 1 91  ? -20.98  -0.276  -3.753  1   58.705  ? 103 ALA   B HB3  1 c 2 
ATOM   3047 N N    . HIS   B 1 92  ? -20.797 -3.246  -3.443  1   54.796  ? 104 HIS   B N    1 ? 2 
ATOM   3048 C CA   . HIS   B 1 92  ? -19.766 -4.053  -2.827  1   49.773  ? 104 HIS   B CA   1 ? 2 
ATOM   3049 C C    . HIS   B 1 92  ? -18.495 -3.226  -2.629  1   46.61   ? 104 HIS   B C    1 ? 2 
ATOM   3050 O O    . HIS   B 1 92  ? -18.074 -2.53   -3.532  1   52.26   ? 104 HIS   B O    1 ? 2 
ATOM   3051 C CB   . HIS   B 1 92  ? -19.506 -5.224  -3.764  1   51.416  ? 104 HIS   B CB   1 ? 2 
ATOM   3052 C CG   . HIS   B 1 92  ? -20.606 -6.208  -3.78   1   54.093  ? 104 HIS   B CG   1 ? 2 
ATOM   3053 N ND1  . HIS   B 1 92  ? -20.645 -7.299  -4.608  1   56.618  ? 104 HIS   B ND1  1 ? 2 
ATOM   3054 C CD2  . HIS   B 1 92  ? -21.672 -6.252  -3.001  1   54.18   ? 104 HIS   B CD2  1 ? 2 
ATOM   3055 C CE1  . HIS   B 1 92  ? -21.763 -7.932  -4.354  1   61.819  ? 104 HIS   B CE1  1 ? 2 
ATOM   3056 N NE2  . HIS   B 1 92  ? -22.383 -7.308  -3.354  1   58.721  ? 104 HIS   B NE2  1 ? 2 
ATOM   3057 H H    . HIS   B 1 92  ? -20.746 -3.121  -4.348  1   56.29   ? 104 HIS   B H    1 c 2 
ATOM   3058 H HA   . HIS   B 1 92  ? -20.078 -4.375  -1.949  1   49.71   ? 104 HIS   B HA   1 c 2 
ATOM   3059 H HB2  . HIS   B 1 92  ? -19.37  -4.88   -4.674  1   52.657  ? 104 HIS   B HB2  1 c 2 
ATOM   3060 H HB3  . HIS   B 1 92  ? -18.679 -5.675  -3.485  1   50.106  ? 104 HIS   B HB3  1 c 2 
ATOM   3061 H HD1  . HIS   B 1 92  ? -20.066 -7.566  -5.2    0   30      ? 104 HIS   B HD1  1 c 2 
ATOM   3062 H HD2  . HIS   B 1 92  ? -21.908 -5.64   -2.333  1   53.175  ? 104 HIS   B HD2  1 c 2 
ATOM   3063 H HE1  . HIS   B 1 92  ? -22.051 -8.725  -4.774  1   64.124  ? 104 HIS   B HE1  1 c 2 
ATOM   3064 H HE2  . HIS   B 1 92  ? -23.198 -7.555  -3.037  0   30      ? 104 HIS   B HE2  1 c 2 
ATOM   3065 N N    . LEU   B 1 93  ? -17.9   -3.305  -1.441  1   46.498  ? 105 LEU   B N    1 ? 2 
ATOM   3066 C CA   . LEU   B 1 93  ? -16.67  -2.637  -1.073  1   42.728  ? 105 LEU   B CA   1 ? 2 
ATOM   3067 C C    . LEU   B 1 93  ? -15.675 -3.686  -0.588  1   42.762  ? 105 LEU   B C    1 ? 2 
ATOM   3068 O O    . LEU   B 1 93  ? -16.018 -4.558  0.218   1   44.152  ? 105 LEU   B O    1 ? 2 
ATOM   3069 C CB   . LEU   B 1 93  ? -16.847 -1.617  0.058   1   44.349  ? 105 LEU   B CB   1 ? 2 
ATOM   3070 C CG   . LEU   B 1 93  ? -17.688 -0.375  -0.201  1   43.715  ? 105 LEU   B CG   1 ? 2 
ATOM   3071 C CD1  . LEU   B 1 93  ? -17.627 0.547   1.006   1   41.089  ? 105 LEU   B CD1  1 ? 2 
ATOM   3072 C CD2  . LEU   B 1 93  ? -17.114 0.348   -1.373  1   49.794  ? 105 LEU   B CD2  1 ? 2 
ATOM   3073 H H    . LEU   B 1 93  ? -18.3   -3.825  -0.804  1   45.733  ? 105 LEU   B H    1 c 2 
ATOM   3074 H HA   . LEU   B 1 93  ? -16.303 -2.186  -1.87   1   44.198  ? 105 LEU   B HA   1 c 2 
ATOM   3075 H HB2  . LEU   B 1 93  ? -17.235 -2.091  0.83    1   43.16   ? 105 LEU   B HB2  1 c 2 
ATOM   3076 H HB3  . LEU   B 1 93  ? -15.951 -1.322  0.34    1   42.061  ? 105 LEU   B HB3  1 c 2 
ATOM   3077 H HG   . LEU   B 1 93  ? -18.626 -0.639  -0.386  1   46.044  ? 105 LEU   B HG   1 c 2 
ATOM   3078 H HD11 . LEU   B 1 93  ? -17.936 0.07    1.795   1   41.359  ? 105 LEU   B HD11 1 c 2 
ATOM   3079 H HD12 . LEU   B 1 93  ? -18.195 1.321   0.853   1   42.454  ? 105 LEU   B HD12 1 c 2 
ATOM   3080 H HD13 . LEU   B 1 93  ? -16.711 0.841   1.145   1   40.578  ? 105 LEU   B HD13 1 c 2 
ATOM   3081 H HD21 . LEU   B 1 93  ? -17.272 -0.165  -2.182  1   49.252  ? 105 LEU   B HD21 1 c 2 
ATOM   3082 H HD22 . LEU   B 1 93  ? -16.157 0.465   -1.247  1   47.022  ? 105 LEU   B HD22 1 c 2 
ATOM   3083 H HD23 . LEU   B 1 93  ? -17.536 1.219   -1.457  1   48.695  ? 105 LEU   B HD23 1 c 2 
ATOM   3084 N N    . LEU   B 1 94  ? -14.419 -3.56   -1.039  1   39.942  ? 106 LEU   B N    1 ? 2 
ATOM   3085 C CA   . LEU   B 1 94  ? -13.347 -4.43   -0.585  1   39.296  ? 106 LEU   B CA   1 ? 2 
ATOM   3086 C C    . LEU   B 1 94  ? -12.267 -3.545  0.031   1   39.444  ? 106 LEU   B C    1 ? 2 
ATOM   3087 O O    . LEU   B 1 94  ? -11.875 -2.497  -0.501  1   43.217  ? 106 LEU   B O    1 ? 2 
ATOM   3088 C CB   . LEU   B 1 94  ? -12.846 -5.299  -1.743  1   40.662  ? 106 LEU   B CB   1 ? 2 
ATOM   3089 C CG   . LEU   B 1 94  ? -11.667 -6.198  -1.371  1   44.349  ? 106 LEU   B CG   1 ? 2 
ATOM   3090 C CD1  . LEU   B 1 94  ? -11.991 -7.32   -0.359  1   45.105  ? 106 LEU   B CD1  1 ? 2 
ATOM   3091 C CD2  . LEU   B 1 94  ? -11.149 -6.909  -2.572  1   52.879  ? 106 LEU   B CD2  1 ? 2 
ATOM   3092 H H    . LEU   B 1 94  ? -14.225 -2.908  -1.65   1   40.763  ? 106 LEU   B H    1 c 2 
ATOM   3093 H HA   . LEU   B 1 94  ? -13.704 -5.021  0.125   1   39.499  ? 106 LEU   B HA   1 c 2 
ATOM   3094 H HB2  . LEU   B 1 94  ? -13.59  -5.865  -2.053  1   42.848  ? 106 LEU   B HB2  1 c 2 
ATOM   3095 H HB3  . LEU   B 1 94  ? -12.568 -4.705  -2.478  1   42.065  ? 106 LEU   B HB3  1 c 2 
ATOM   3096 H HG   . LEU   B 1 94  ? -10.939 -5.634  -1.001  1   43.747  ? 106 LEU   B HG   1 c 2 
ATOM   3097 H HD11 . LEU   B 1 94  ? -12.331 -6.929  0.463   1   43.62   ? 106 LEU   B HD11 1 c 2 
ATOM   3098 H HD12 . LEU   B 1 94  ? -11.184 -7.827  -0.165  1   45.544  ? 106 LEU   B HD12 1 c 2 
ATOM   3099 H HD13 . LEU   B 1 94  ? -12.662 -7.914  -0.736  1   46.446  ? 106 LEU   B HD13 1 c 2 
ATOM   3100 H HD21 . LEU   B 1 94  ? -10.91  -6.26   -3.256  1   51.361  ? 106 LEU   B HD21 1 c 2 
ATOM   3101 H HD22 . LEU   B 1 94  ? -11.834 -7.505  -2.918  1   52.278  ? 106 LEU   B HD22 1 c 2 
ATOM   3102 H HD23 . LEU   B 1 94  ? -10.362 -7.427  -2.33   1   51.381  ? 106 LEU   B HD23 1 c 2 
ATOM   3103 N N    . ILE   B 1 95  ? -11.821 -3.883  1.221   1   39.853  ? 107 ILE   B N    1 ? 2 
ATOM   3104 C CA   . ILE   B 1 95  ? -11.162 -2.88   2.04    1   37.252  ? 107 ILE   B CA   1 ? 2 
ATOM   3105 C C    . ILE   B 1 95  ? -9.855  -3.38   2.665   1   41.987  ? 107 ILE   B C    1 ? 2 
ATOM   3106 O O    . ILE   B 1 95  ? -9.842  -4.315  3.487   1   37.3    ? 107 ILE   B O    1 ? 2 
ATOM   3107 C CB   . ILE   B 1 95  ? -12.118 -2.436  3.157   1   37.122  ? 107 ILE   B CB   1 ? 2 
ATOM   3108 C CG1  . ILE   B 1 95  ? -13.43  -1.921  2.599   1   36.918  ? 107 ILE   B CG1  1 ? 2 
ATOM   3109 C CG2  . ILE   B 1 95  ? -11.454 -1.386  4.066   1   34.391  ? 107 ILE   B CG2  1 ? 2 
ATOM   3110 C CD1  . ILE   B 1 95  ? -14.512 -1.797  3.655   1   38.94   ? 107 ILE   B CD1  1 ? 2 
ATOM   3111 H H    . ILE   B 1 95  ? -11.917 -4.736  1.535   1   39.597  ? 107 ILE   B H    1 c 2 
ATOM   3112 H HA   . ILE   B 1 95  ? -10.963 -2.104  1.485   1   38.521  ? 107 ILE   B HA   1 c 2 
ATOM   3113 H HB   . ILE   B 1 95  ? -12.317 -3.221  3.705   1   36.76   ? 107 ILE   B HB   1 c 2 
ATOM   3114 H HG12 . ILE   B 1 95  ? -13.281 -1.043  2.192   1   37.368  ? 107 ILE   B HG12 1 c 2 
ATOM   3115 H HG13 . ILE   B 1 95  ? -13.744 -2.528  1.9     1   38.031  ? 107 ILE   B HG13 1 c 2 
ATOM   3116 H HG21 . ILE   B 1 95  ? -12.133 -0.913  4.573   1   35      ? 107 ILE   B HG21 1 c 2 
ATOM   3117 H HG22 . ILE   B 1 95  ? -10.959 -0.75   3.521   1   35.264  ? 107 ILE   B HG22 1 c 2 
ATOM   3118 H HG23 . ILE   B 1 95  ? -10.843 -1.825  4.682   1   35.421  ? 107 ILE   B HG23 1 c 2 
ATOM   3119 H HD11 . ILE   B 1 95  ? -14.523 -2.602  4.207   1   38.656  ? 107 ILE   B HD11 1 c 2 
ATOM   3120 H HD12 . ILE   B 1 95  ? -15.379 -1.692  3.22    1   38.862  ? 107 ILE   B HD12 1 c 2 
ATOM   3121 H HD13 . ILE   B 1 95  ? -14.338 -1.021  4.22    1   37.998  ? 107 ILE   B HD13 1 c 2 
ATOM   3122 N N    . LYS   B 1 96  ? -8.747  -2.673  2.362   1   39.144  ? 108 LYS   B N    1 ? 2 
ATOM   3123 C CA   . LYS   B 1 96  ? -7.487  -3.046  2.98    1   40.309  ? 108 LYS   B CA   1 ? 2 
ATOM   3124 C C    . LYS   B 1 96  ? -7.432  -2.487  4.393   1   40.501  ? 108 LYS   B C    1 ? 2 
ATOM   3125 O O    . LYS   B 1 96  ? -8.116  -1.504  4.696   1   38.872  ? 108 LYS   B O    1 ? 2 
ATOM   3126 C CB   . LYS   B 1 96  ? -6.363  -2.458  2.12    1   45.804  ? 108 LYS   B CB   1 ? 2 
ATOM   3127 C CG   . LYS   B 1 96  ? -6.123  -3.11   0.782   1   51.943  ? 108 LYS   B CG   1 ? 2 
ATOM   3128 C CD   . LYS   B 1 96  ? -4.837  -2.528  0.182   1   55.538  ? 108 LYS   B CD   1 ? 2 
ATOM   3129 C CE   . LYS   B 1 96  ? -4.409  -3.282  -1.028  1   57.797  ? 108 LYS   B CE   1 ? 2 
ATOM   3130 N NZ   . LYS   B 1 96  ? -5.174  -2.788  -2.18   1   61.011  ? 108 LYS   B NZ   1 ? 2 
ATOM   3131 H H    . LYS   B 1 96  ? -8.78   -1.97   1.779   1   40.072  ? 108 LYS   B H    1 c 2 
ATOM   3132 H HA   . LYS   B 1 96  ? -7.419  -4.034  3.004   1   41.518  ? 108 LYS   B HA   1 c 2 
ATOM   3133 H HB2  . LYS   B 1 96  ? -6.561  -1.51   1.963   1   45.571  ? 108 LYS   B HB2  1 c 2 
ATOM   3134 H HB3  . LYS   B 1 96  ? -5.528  -2.497  2.632   1   46.923  ? 108 LYS   B HB3  1 c 2 
ATOM   3135 H HG2  . LYS   B 1 96  ? -6.029  -4.08   0.903   1   51.424  ? 108 LYS   B HG2  1 c 2 
ATOM   3136 H HG3  . LYS   B 1 96  ? -6.884  -2.929  0.188   1   50.479  ? 108 LYS   B HG3  1 c 2 
ATOM   3137 H HD2  . LYS   B 1 96  ? -4.987  -1.588  -0.058  1   55.211  ? 108 LYS   B HD2  1 c 2 
ATOM   3138 H HD3  . LYS   B 1 96  ? -4.121  -2.563  0.852   1   55.916  ? 108 LYS   B HD3  1 c 2 
ATOM   3139 H HE2  . LYS   B 1 96  ? -3.459  -3.151  -1.195  1   60.598  ? 108 LYS   B HE2  1 c 2 
ATOM   3140 H HE3  . LYS   B 1 96  ? -4.576  -4.234  -0.912  1   58.354  ? 108 LYS   B HE3  1 c 2 
ATOM   3141 H HZ1  . LYS   B 1 96  ? -4.956  -1.925  -2.338  1   60.27   ? 108 LYS   B HZ1  1 c 2 
ATOM   3142 H HZ2  . LYS   B 1 96  ? -6.063  -2.848  -2.016  1   58.272  ? 108 LYS   B HZ2  1 c 2 
ATOM   3143 H HZ3  . LYS   B 1 96  ? -4.975  -3.283  -2.912  1   61.614  ? 108 LYS   B HZ3  1 c 2 
ATOM   3144 N N    . PRO   B 1 97  ? -6.546  -3.052  5.258   1   41.489  ? 109 PRO   B N    1 ? 2 
ATOM   3145 C CA   . PRO   B 1 97  ? -6.511  -2.739  6.672   1   39.862  ? 109 PRO   B CA   1 ? 2 
ATOM   3146 C C    . PRO   B 1 97  ? -6.266  -1.285  7.1     1   41.534  ? 109 PRO   B C    1 ? 2 
ATOM   3147 O O    . PRO   B 1 97  ? -6.771  -0.836  8.121   1   48.17   ? 109 PRO   B O    1 ? 2 
ATOM   3148 C CB   . PRO   B 1 97  ? -5.45   -3.642  7.243   1   40.464  ? 109 PRO   B CB   1 ? 2 
ATOM   3149 C CG   . PRO   B 1 97  ? -4.748  -4.362  6.145   1   42.495  ? 109 PRO   B CG   1 ? 2 
ATOM   3150 C CD   . PRO   B 1 97  ? -5.603  -4.136  4.894   1   43.871  ? 109 PRO   B CD   1 ? 2 
ATOM   3151 H HA   . PRO   B 1 97  ? -7.366  -3.02   7.059   1   39.451  ? 109 PRO   B HA   1 c 2 
ATOM   3152 H HB2  . PRO   B 1 97  ? -4.807  -3.12   7.762   1   42.45   ? 109 PRO   B HB2  1 c 2 
ATOM   3153 H HB3  . PRO   B 1 97  ? -5.854  -4.286  7.857   1   41.362  ? 109 PRO   B HB3  1 c 2 
ATOM   3154 H HG2  . PRO   B 1 97  ? -3.848  -4.003  6.014   1   44.256  ? 109 PRO   B HG2  1 c 2 
ATOM   3155 H HG3  . PRO   B 1 97  ? -4.679  -5.317  6.344   1   43.711  ? 109 PRO   B HG3  1 c 2 
ATOM   3156 H HD2  . PRO   B 1 97  ? -5.046  -3.869  4.14    1   43.64   ? 109 PRO   B HD2  1 c 2 
ATOM   3157 H HD3  . PRO   B 1 97  ? -6.092  -4.947  4.655   1   42.686  ? 109 PRO   B HD3  1 c 2 
ATOM   3158 N N    . GLU   B 1 98  ? -5.471  -0.579  6.359   1   43.436  ? 110 GLU   B N    1 ? 2 
ATOM   3159 C CA   . GLU   B 1 98  ? -5.231  0.836   6.546   1   47.113  ? 110 GLU   B CA   1 ? 2 
ATOM   3160 C C    . GLU   B 1 98  ? -6.524  1.658   6.5     1   42.247  ? 110 GLU   B C    1 ? 2 
ATOM   3161 O O    . GLU   B 1 98  ? -6.519  2.706   7.085   1   44.883  ? 110 GLU   B O    1 ? 2 
ATOM   3162 C CB   . GLU   B 1 98  ? -4.221  1.318   5.488   1   53.777  ? 110 GLU   B CB   1 ? 2 
ATOM   3163 C CG   . GLU   B 1 98  ? -2.861  0.591   5.429   1   65.003  ? 110 GLU   B CG   1 ? 2 
ATOM   3164 C CD   . GLU   B 1 98  ? -2.79   -0.754  4.715   1   69.622  ? 110 GLU   B CD   1 ? 2 
ATOM   3165 O OE1  . GLU   B 1 98  ? -3.748  -0.935  3.935   1   65.05   ? 110 GLU   B OE1  1 ? 2 
ATOM   3166 O OE2  . GLU   B 1 98  ? -1.866  -1.61   4.946   1   78.236  ? 110 GLU   B OE2  1 ? 2 
ATOM   3167 H H    . GLU   B 1 98  ? -5.048  -0.998  5.668   1   44.226  ? 110 GLU   B H    1 c 2 
ATOM   3168 H HA   . GLU   B 1 98  ? -4.82   0.96    7.439   1   48.204  ? 110 GLU   B HA   1 c 2 
ATOM   3169 H HB2  . GLU   B 1 98  ? -4.644  1.252   4.606   1   53.263  ? 110 GLU   B HB2  1 c 2 
ATOM   3170 H HB3  . GLU   B 1 98  ? -4.037  2.266   5.652   1   55.57   ? 110 GLU   B HB3  1 c 2 
ATOM   3171 H HG2  . GLU   B 1 98  ? -2.213  1.19    5       1   65.753  ? 110 GLU   B HG2  1 c 2 
ATOM   3172 H HG3  . GLU   B 1 98  ? -2.547  0.457   6.349   1   64.912  ? 110 GLU   B HG3  1 c 2 
ATOM   3173 N N    . TYR   B 1 99  ? -7.574  1.227   5.819   1   38.206  ? 111 TYR   B N    1 ? 2 
ATOM   3174 C CA   . TYR   B 1 99  ? -8.851  1.934   5.774   1   41.157  ? 111 TYR   B CA   1 ? 2 
ATOM   3175 C C    . TYR   B 1 99  ? -9.863  1.217   6.719   1   41.381  ? 111 TYR   B C    1 ? 2 
ATOM   3176 O O    . TYR   B 1 99  ? -11.102 1.347   6.636   1   37.51   ? 111 TYR   B O    1 ? 2 
ATOM   3177 C CB   . TYR   B 1 99  ? -9.307  2.032   4.303   1   38.702  ? 111 TYR   B CB   1 ? 2 
ATOM   3178 C CG   . TYR   B 1 99  ? -8.424  2.939   3.466   1   41.76   ? 111 TYR   B CG   1 ? 2 
ATOM   3179 C CD1  . TYR   B 1 99  ? -7.253  2.486   2.863   1   39.617  ? 111 TYR   B CD1  1 ? 2 
ATOM   3180 C CD2  . TYR   B 1 99  ? -8.672  4.296   3.406   1   46.873  ? 111 TYR   B CD2  1 ? 2 
ATOM   3181 C CE1  . TYR   B 1 99  ? -6.424  3.337   2.159   1   43.645  ? 111 TYR   B CE1  1 ? 2 
ATOM   3182 C CE2  . TYR   B 1 99  ? -7.845  5.165   2.711   1   46.89   ? 111 TYR   B CE2  1 ? 2 
ATOM   3183 C CZ   . TYR   B 1 99  ? -6.712  4.684   2.099   1   46.852  ? 111 TYR   B CZ   1 ? 2 
ATOM   3184 O OH   . TYR   B 1 99  ? -5.975  5.6     1.426   1   51.731  ? 111 TYR   B OH   1 ? 2 
ATOM   3185 H H    . TYR   B 1 99  ? -7.496  0.453   5.339   1   39.044  ? 111 TYR   B H    1 c 2 
ATOM   3186 H HA   . TYR   B 1 99  ? -8.709  2.857   6.115   1   41.225  ? 111 TYR   B HA   1 c 2 
ATOM   3187 H HB2  . TYR   B 1 99  ? -9.305  1.13    3.911   1   38.816  ? 111 TYR   B HB2  1 c 2 
ATOM   3188 H HB3  . TYR   B 1 99  ? -10.228 2.374   4.282   1   38.897  ? 111 TYR   B HB3  1 c 2 
ATOM   3189 H HD1  . TYR   B 1 99  ? -7.038  1.568   2.906   1   40.327  ? 111 TYR   B HD1  1 c 2 
ATOM   3190 H HD2  . TYR   B 1 99  ? -9.44   4.641   3.834   1   44.842  ? 111 TYR   B HD2  1 c 2 
ATOM   3191 H HE1  . TYR   B 1 99  ? -5.653  3.002   1.735   1   44.908  ? 111 TYR   B HE1  1 c 2 
ATOM   3192 H HE2  . TYR   B 1 99  ? -8.055  6.082   2.661   1   48.245  ? 111 TYR   B HE2  1 c 2 
ATOM   3193 H HH   . TYR   B 1 99  ? -5.335  5.155   0.972   0   30      ? 111 TYR   B HH   1 c 2 
ATOM   3194 N N    . ALA   B 1 100 ? -9.368  0.39    7.639   1   42.26   ? 112 ALA   B N    1 ? 2 
ATOM   3195 C CA   . ALA   B 1 100 ? -10.299 -0.366  8.499   1   38.196  ? 112 ALA   B CA   1 ? 2 
ATOM   3196 C C    . ALA   B 1 100 ? -9.786  -0.325  9.932   1   37.69   ? 112 ALA   B C    1 ? 2 
ATOM   3197 O O    . ALA   B 1 100 ? -9.86   0.746   10.535  1   41.263  ? 112 ALA   B O    1 ? 2 
ATOM   3198 C CB   . ALA   B 1 100 ? -10.47  -1.778  7.957   1   38.711  ? 112 ALA   B CB   1 ? 2 
ATOM   3199 H H    . ALA   B 1 100 ? -8.468  0.294   7.756   1   42.003  ? 112 ALA   B H    1 c 2 
ATOM   3200 H HA   . ALA   B 1 100 ? -11.183 0.091   8.482   1   38.29   ? 112 ALA   B HA   1 c 2 
ATOM   3201 H HB1  . ALA   B 1 100 ? -11.024 -1.755  7.159   1   37.426  ? 112 ALA   B HB1  1 c 2 
ATOM   3202 H HB2  . ALA   B 1 100 ? -9.601  -2.15   7.731   1   38.659  ? 112 ALA   B HB2  1 c 2 
ATOM   3203 H HB3  . ALA   B 1 100 ? -10.897 -2.338  8.626   1   38.996  ? 112 ALA   B HB3  1 c 2 
ATOM   3204 N N    . TYR   B 1 101 ? -9.146  -1.408  10.387  1   39.531  ? 113 TYR   B N    1 ? 2 
ATOM   3205 C CA   . TYR   B 1 101 ? -8.668  -1.627  11.743  1   42.241  ? 113 TYR   B CA   1 ? 2 
ATOM   3206 C C    . TYR   B 1 101 ? -7.164  -1.878  11.832  1   43.563  ? 113 TYR   B C    1 ? 2 
ATOM   3207 O O    . TYR   B 1 101 ? -6.591  -2.183  12.888  1   43.987  ? 113 TYR   B O    1 ? 2 
ATOM   3208 C CB   . TYR   B 1 101 ? -9.454  -2.793  12.351  1   44.173  ? 113 TYR   B CB   1 ? 2 
ATOM   3209 C CG   . TYR   B 1 101 ? -10.957 -2.559  12.379  1   43.261  ? 113 TYR   B CG   1 ? 2 
ATOM   3210 C CD1  . TYR   B 1 101 ? -11.546 -1.803  13.372  1   42.098  ? 113 TYR   B CD1  1 ? 2 
ATOM   3211 C CD2  . TYR   B 1 101 ? -11.807 -3.104  11.429  1   41.074  ? 113 TYR   B CD2  1 ? 2 
ATOM   3212 C CE1  . TYR   B 1 101 ? -12.907 -1.585  13.412  1   42.388  ? 113 TYR   B CE1  1 ? 2 
ATOM   3213 C CE2  . TYR   B 1 101 ? -13.19  -2.902  11.479  1   42.398  ? 113 TYR   B CE2  1 ? 2 
ATOM   3214 C CZ   . TYR   B 1 101 ? -13.767 -2.143  12.491  1   42.785  ? 113 TYR   B CZ   1 ? 2 
ATOM   3215 O OH   . TYR   B 1 101 ? -15.153 -1.908  12.591  1   42.523  ? 113 TYR   B OH   1 ? 2 
ATOM   3216 H H    . TYR   B 1 101 ? -8.994  -2.08   9.788   1   38.782  ? 113 TYR   B H    1 c 2 
ATOM   3217 H HA   . TYR   B 1 101 ? -8.873  -0.813  12.275  1   43.238  ? 113 TYR   B HA   1 c 2 
ATOM   3218 H HB2  . TYR   B 1 101 ? -9.267  -3.605  11.83   1   43.461  ? 113 TYR   B HB2  1 c 2 
ATOM   3219 H HB3  . TYR   B 1 101 ? -9.138  -2.941  13.269  1   46.223  ? 113 TYR   B HB3  1 c 2 
ATOM   3220 H HD1  . TYR   B 1 101 ? -11     -1.412  14.035  1   44.524  ? 113 TYR   B HD1  1 c 2 
ATOM   3221 H HD2  . TYR   B 1 101 ? -11.446 -3.638  10.74   1   40.556  ? 113 TYR   B HD2  1 c 2 
ATOM   3222 H HE1  . TYR   B 1 101 ? -13.266 -1.071  14.115  1   44.499  ? 113 TYR   B HE1  1 c 2 
ATOM   3223 H HE2  . TYR   B 1 101 ? -13.741 -3.293  10.824  1   40.968  ? 113 TYR   B HE2  1 c 2 
ATOM   3224 H HH   . TYR   B 1 101 ? -15.314 -1.369  13.191  0   30      ? 113 TYR   B HH   1 c 2 
ATOM   3225 N N    . GLY   B 1 102 ? -6.475  -1.732  10.718  1   49.806  ? 114 GLY   B N    1 ? 2 
ATOM   3226 C CA   . GLY   B 1 102 ? -5.043  -1.456  10.71   1   50.223  ? 114 GLY   B CA   1 ? 2 
ATOM   3227 C C    . GLY   B 1 102 ? -4.261  -2.589  11.326  1   55.15   ? 114 GLY   B C    1 ? 2 
ATOM   3228 O O    . GLY   B 1 102 ? -4.775  -3.719  11.42   1   53.176  ? 114 GLY   B O    1 ? 2 
ATOM   3229 H H    . GLY   B 1 102 ? -6.902  -1.818  9.915   1   45.437  ? 114 GLY   B H    1 c 2 
ATOM   3230 H HA2  . GLY   B 1 102 ? -4.745  -1.316  9.781   1   50.297  ? 114 GLY   B HA2  1 c 2 
ATOM   3231 H HA3  . GLY   B 1 102 ? -4.872  -0.625  11.213  1   52.498  ? 114 GLY   B HA3  1 c 2 
ATOM   3232 N N    . SER   B 1 103 ? -3.038  -2.26   11.77   1   59.196  ? 115 SER   B N    1 ? 2 
ATOM   3233 C CA   . SER   B 1 103 ? -2.15   -3.35   12.125  1   63.665  ? 115 SER   B CA   1 ? 2 
ATOM   3234 C C    . SER   B 1 103 ? -2.533  -3.831  13.52   1   63.105  ? 115 SER   B C    1 ? 2 
ATOM   3235 O O    . SER   B 1 103 ? -2.345  -4.992  13.869  1   64.466  ? 115 SER   B O    1 ? 2 
ATOM   3236 C CB   . SER   B 1 103 ? -0.702  -2.991  11.954  1   69.503  ? 115 SER   B CB   1 ? 2 
ATOM   3237 O OG   . SER   B 1 103 ? -0.422  -1.838  12.727  1   73.054  ? 115 SER   B OG   1 ? 2 
ATOM   3238 H H    . SER   B 1 103 ? -2.764  -1.391  11.848  1   60.148  ? 115 SER   B H    1 c 2 
ATOM   3239 H HA   . SER   B 1 103 ? -2.339  -4.095  11.502  1   61.761  ? 115 SER   B HA   1 c 2 
ATOM   3240 H HB2  . SER   B 1 103 ? -0.141  -3.733  12.251  1   71.377  ? 115 SER   B HB2  1 c 2 
ATOM   3241 H HB3  . SER   B 1 103 ? -0.516  -2.811  11.013  1   67.845  ? 115 SER   B HB3  1 c 2 
ATOM   3242 H HG   . SER   B 1 103 ? 0.393   -1.545  12.7    0   30      ? 115 SER   B HG   1 c 2 
ATOM   3243 N N    . ALA   B 1 104 ? -3.144  -2.971  14.328  1   68.184  ? 116 ALA   B N    1 ? 2 
ATOM   3244 C CA   . ALA   B 1 104 ? -3.51   -3.357  15.698  1   68.994  ? 116 ALA   B CA   1 ? 2 
ATOM   3245 C C    . ALA   B 1 104 ? -4.796  -4.179  15.693  1   63.917  ? 116 ALA   B C    1 ? 2 
ATOM   3246 O O    . ALA   B 1 104 ? -5.117  -4.865  16.665  1   73.732  ? 116 ALA   B O    1 ? 2 
ATOM   3247 C CB   . ALA   B 1 104 ? -3.663  -2.132  16.573  1   71.138  ? 116 ALA   B CB   1 ? 2 
ATOM   3248 H H    . ALA   B 1 104 ? -3.332  -2.124  14.041  1   65.223  ? 116 ALA   B H    1 c 2 
ATOM   3249 H HA   . ALA   B 1 104 ? -2.78   -3.926  16.068  1   71.583  ? 116 ALA   B HA   1 c 2 
ATOM   3250 H HB1  . ALA   B 1 104 ? -2.818  -1.654  16.618  1   73.06   ? 116 ALA   B HB1  1 c 2 
ATOM   3251 H HB2  . ALA   B 1 104 ? -4.344  -1.547  16.2    1   68.686  ? 116 ALA   B HB2  1 c 2 
ATOM   3252 H HB3  . ALA   B 1 104 ? -3.928  -2.401  17.469  1   73.535  ? 116 ALA   B HB3  1 c 2 
ATOM   3253 N N    . GLY   B 1 105 ? -5.555  -4.032  14.605  1   60.934  ? 117 GLY   B N    1 ? 2 
ATOM   3254 C CA   . GLY   B 1 105 ? -6.875  -4.636  14.474  1   59.558  ? 117 GLY   B CA   1 ? 2 
ATOM   3255 C C    . GLY   B 1 105 ? -7.781  -4.167  15.615  1   60.322  ? 117 GLY   B C    1 ? 2 
ATOM   3256 O O    . GLY   B 1 105 ? -7.509  -3.1    16.142  1   58.116  ? 117 GLY   B O    1 ? 2 
ATOM   3257 H H    . GLY   B 1 105 ? -5.246  -3.523  13.912  1   59.223  ? 117 GLY   B H    1 c 2 
ATOM   3258 H HA2  . GLY   B 1 105 ? -7.269  -4.384  13.608  1   56.379  ? 117 GLY   B HA2  1 c 2 
ATOM   3259 H HA3  . GLY   B 1 105 ? -6.787  -5.618  14.499  1   60.159  ? 117 GLY   B HA3  1 c 2 
ATOM   3260 N N    . SER   B 1 106 ? -8.85   -4.946  15.901  1   57.6    ? 118 SER   B N    1 ? 2 
ATOM   3261 C CA   . SER   B 1 106 ? -9.844  -4.641  16.895  1   59.995  ? 118 SER   B CA   1 ? 2 
ATOM   3262 C C    . SER   B 1 106 ? -10.287 -5.984  17.431  1   64.158  ? 118 SER   B C    1 ? 2 
ATOM   3263 O O    . SER   B 1 106 ? -11.423 -6.451  17.239  1   61.985  ? 118 SER   B O    1 ? 2 
ATOM   3264 C CB   . SER   B 1 106 ? -10.995 -3.809  16.402  1   56.863  ? 118 SER   B CB   1 ? 2 
ATOM   3265 O OG   . SER   B 1 106 ? -11.766 -3.491  17.547  1   57.34   ? 118 SER   B OG   1 ? 2 
ATOM   3266 H H    . SER   B 1 106 ? -8.949  -5.72   15.425  1   57.68   ? 118 SER   B H    1 c 2 
ATOM   3267 H HA   . SER   B 1 106 ? -9.4    -4.147  17.631  1   62.396  ? 118 SER   B HA   1 c 2 
ATOM   3268 H HB2  . SER   B 1 106 ? -10.666 -2.997  15.976  1   54.57   ? 118 SER   B HB2  1 c 2 
ATOM   3269 H HB3  . SER   B 1 106 ? -11.53  -4.318  15.764  1   54.613  ? 118 SER   B HB3  1 c 2 
ATOM   3270 H HG   . SER   B 1 106 ? -12.416 -3.058  17.196  0   30      ? 118 SER   B HG   1 c 2 
ATOM   3271 N N    . LEU   B 1 107 ? -9.294  -6.586  18.077  1   68.081  ? 119 LEU   B N    1 ? 2 
ATOM   3272 C CA   . LEU   B 1 107 ? -9.418  -7.873  18.714  1   76.003  ? 119 LEU   B CA   1 ? 2 
ATOM   3273 C C    . LEU   B 1 107 ? -10.564 -7.952  19.723  1   79.228  ? 119 LEU   B C    1 ? 2 
ATOM   3274 O O    . LEU   B 1 107 ? -10.995 -6.975  20.346  1   80.822  ? 119 LEU   B O    1 ? 2 
ATOM   3275 C CB   . LEU   B 1 107 ? -8.041  -8.129  19.32   1   82.382  ? 119 LEU   B CB   1 ? 2 
ATOM   3276 C CG   . LEU   B 1 107 ? -6.912  -8.272  18.275  1   87.161  ? 119 LEU   B CG   1 ? 2 
ATOM   3277 C CD1  . LEU   B 1 107 ? -5.548  -8.663  18.904  1   97.446  ? 119 LEU   B CD1  1 ? 2 
ATOM   3278 C CD2  . LEU   B 1 107 ? -7.355  -9.281  17.234  1   78.551  ? 119 LEU   B CD2  1 ? 2 
ATOM   3279 H H    . LEU   B 1 107 ? -8.494  -6.149  18.137  1   69.126  ? 119 LEU   B H    1 c 2 
ATOM   3280 H HA   . LEU   B 1 107 ? -9.587  -8.533  18.003  1   74.119  ? 119 LEU   B HA   1 c 2 
ATOM   3281 H HB2  . LEU   B 1 107 ? -7.82   -7.383  19.923  1   84.516  ? 119 LEU   B HB2  1 c 2 
ATOM   3282 H HB3  . LEU   B 1 107 ? -8.084  -8.958  19.851  1   86.554  ? 119 LEU   B HB3  1 c 2 
ATOM   3283 H HG   . LEU   B 1 107 ? -6.795  -7.398  17.822  1   82.427  ? 119 LEU   B HG   1 c 2 
ATOM   3284 H HD11 . LEU   B 1 107 ? -5.65   -9.481  19.419  1   98.851  ? 119 LEU   B HD11 1 c 2 
ATOM   3285 H HD12 . LEU   B 1 107 ? -5.243  -7.95   19.488  1   97.227  ? 119 LEU   B HD12 1 c 2 
ATOM   3286 H HD13 . LEU   B 1 107 ? -4.894  -8.805  18.199  1   94.143  ? 119 LEU   B HD13 1 c 2 
ATOM   3287 H HD21 . LEU   B 1 107 ? -7.824  -10.014 17.668  1   82.532  ? 119 LEU   B HD21 1 c 2 
ATOM   3288 H HD22 . LEU   B 1 107 ? -6.577  -9.63   16.768  1   80      ? 119 LEU   B HD22 1 c 2 
ATOM   3289 H HD23 . LEU   B 1 107 ? -7.946  -8.853  16.595  1   76.647  ? 119 LEU   B HD23 1 c 2 
ATOM   3290 N N    . PRO   B 1 108 ? -11.112 -9.168  19.895  1   82.367  ? 120 PRO   B N    1 ? 2 
ATOM   3291 C CA   . PRO   B 1 108 ? -10.741 -10.316 19.083  1   80.369  ? 120 PRO   B CA   1 ? 2 
ATOM   3292 C C    . PRO   B 1 108 ? -11.578 -10.46  17.821  1   75.312  ? 120 PRO   B C    1 ? 2 
ATOM   3293 O O    . PRO   B 1 108 ? -11.404 -11.456 17.129  1   79.143  ? 120 PRO   B O    1 ? 2 
ATOM   3294 C CB   . PRO   B 1 108 ? -10.966 -11.493 20.014  1   89.63   ? 120 PRO   B CB   1 ? 2 
ATOM   3295 C CG   . PRO   B 1 108 ? -12.236 -11.017 20.705  1   93.353  ? 120 PRO   B CG   1 ? 2 
ATOM   3296 C CD   . PRO   B 1 108 ? -12.097 -9.519  20.926  1   91.493  ? 120 PRO   B CD   1 ? 2 
ATOM   3297 H HA   . PRO   B 1 108 ? -9.794  -10.271 18.849  1   80.17   ? 120 PRO   B HA   1 c 2 
ATOM   3298 H HB2  . PRO   B 1 108 ? -11.112 -12.323 19.521  1   89.425  ? 120 PRO   B HB2  1 c 2 
ATOM   3299 H HB3  . PRO   B 1 108 ? -10.229 -11.595 20.648  1   92.169  ? 120 PRO   B HB3  1 c 2 
ATOM   3300 H HG2  . PRO   B 1 108 ? -13.02  -11.207 20.152  1   91.562  ? 120 PRO   B HG2  1 c 2 
ATOM   3301 H HG3  . PRO   B 1 108 ? -12.343 -11.473 21.555  1   97.899  ? 120 PRO   B HG3  1 c 2 
ATOM   3302 H HD2  . PRO   B 1 108 ? -12.942 -9.051  20.779  1   89.135  ? 120 PRO   B HD2  1 c 2 
ATOM   3303 H HD3  . PRO   B 1 108 ? -11.758 -9.314  21.819  1   93.816  ? 120 PRO   B HD3  1 c 2 
ATOM   3304 N N    . LYS   B 1 109 ? -12.437 -9.46   17.512  1   73.671  ? 121 LYS   B N    1 ? 2 
ATOM   3305 C CA   . LYS   B 1 109 ? -13.384 -9.508  16.391  1   67.94   ? 121 LYS   B CA   1 ? 2 
ATOM   3306 C C    . LYS   B 1 109 ? -12.646 -9.446  15.033  1   62.145  ? 121 LYS   B C    1 ? 2 
ATOM   3307 O O    . LYS   B 1 109 ? -12.866 -10.271 14.153  1   59.89   ? 121 LYS   B O    1 ? 2 
ATOM   3308 C CB   . LYS   B 1 109 ? -14.464 -8.421  16.597  1   65.308  ? 121 LYS   B CB   1 ? 2 
ATOM   3309 H H    . LYS   B 1 109 ? -12.427 -8.706  18.027  1   73.091  ? 121 LYS   B H    1 c 2 
ATOM   3310 H HA   . LYS   B 1 109 ? -13.849 -10.382 16.434  1   70.128  ? 121 LYS   B HA   1 c 2 
ATOM   3311 H HB2  . LYS   B 1 109 ? -13.935 -7.493  16.682  0   30      ? 121 LYS   B HB2  1 c 2 
ATOM   3312 H HB3  . LYS   B 1 109 ? -15.308 -8.73   16.484  0   30      ? 121 LYS   B HB3  1 c 2 
ATOM   3313 N N    . ILE   B 1 110 ? -11.775 -8.436  14.887  1   59.365  ? 122 ILE   B N    1 ? 2 
ATOM   3314 C CA   . ILE   B 1 110 ? -10.981 -8.173  13.714  1   55.263  ? 122 ILE   B CA   1 ? 2 
ATOM   3315 C C    . ILE   B 1 110 ? -9.51   -8.407  14.033  1   56.096  ? 122 ILE   B C    1 ? 2 
ATOM   3316 O O    . ILE   B 1 110 ? -8.973  -7.754  14.921  1   57.665  ? 122 ILE   B O    1 ? 2 
ATOM   3317 C CB   . ILE   B 1 110 ? -11.196 -6.733  13.256  1   51.718  ? 122 ILE   B CB   1 ? 2 
ATOM   3318 C CG1  . ILE   B 1 110 ? -12.642 -6.297  13.407  1   50.751  ? 122 ILE   B CG1  1 ? 2 
ATOM   3319 C CG2  . ILE   B 1 110 ? -10.743 -6.645  11.802  1   48.309  ? 122 ILE   B CG2  1 ? 2 
ATOM   3320 C CD1  . ILE   B 1 110 ? -13.588 -7.049  12.462  1   48.434  ? 122 ILE   B CD1  1 ? 2 
ATOM   3321 H H    . ILE   B 1 110 ? -11.67  -7.87   15.597  1   60.355  ? 122 ILE   B H    1 c 2 
ATOM   3322 H HA   . ILE   B 1 110 ? -11.259 -8.777  13.001  1   54.475  ? 122 ILE   B HA   1 c 2 
ATOM   3323 H HB   . ILE   B 1 110 ? -10.635 -6.143  13.797  1   52.199  ? 122 ILE   B HB   1 c 2 
ATOM   3324 H HG12 . ILE   B 1 110 ? -12.929 -6.441  14.331  1   53.18   ? 122 ILE   B HG12 1 c 2 
ATOM   3325 H HG13 . ILE   B 1 110 ? -12.704 -5.338  13.22   1   49.014  ? 122 ILE   B HG13 1 c 2 
ATOM   3326 H HG21 . ILE   B 1 110 ? -11.083 -5.827  11.404  1   46.522  ? 122 ILE   B HG21 1 c 2 
ATOM   3327 H HG22 . ILE   B 1 110 ? -11.081 -7.408  11.304  1   48.415  ? 122 ILE   B HG22 1 c 2 
ATOM   3328 H HG23 . ILE   B 1 110 ? -9.772  -6.641  11.763  1   48.565  ? 122 ILE   B HG23 1 c 2 
ATOM   3329 H HD11 . ILE   B 1 110 ? -13.444 -6.753  11.543  1   46.528  ? 122 ILE   B HD11 1 c 2 
ATOM   3330 H HD12 . ILE   B 1 110 ? -14.51  -6.86   12.721  1   49.727  ? 122 ILE   B HD12 1 c 2 
ATOM   3331 H HD13 . ILE   B 1 110 ? -13.427 -8.01   12.521  1   50.49   ? 122 ILE   B HD13 1 c 2 
ATOM   3332 N N    . PRO   B 1 111 ? -8.819  -9.355  13.366  1   54.448  ? 123 PRO   B N    1 ? 2 
ATOM   3333 C CA   . PRO   B 1 111 ? -7.386  -9.533  13.566  1   58.58   ? 123 PRO   B CA   1 ? 2 
ATOM   3334 C C    . PRO   B 1 111 ? -6.565  -8.351  13.035  1   56.306  ? 123 PRO   B C    1 ? 2 
ATOM   3335 O O    . PRO   B 1 111 ? -7.078  -7.472  12.303  1   54.073  ? 123 PRO   B O    1 ? 2 
ATOM   3336 C CB   . PRO   B 1 111 ? -7.001  -10.856 12.797  1   58.274  ? 123 PRO   B CB   1 ? 2 
ATOM   3337 C CG   . PRO   B 1 111 ? -8.333  -11.408 12.279  1   56.83   ? 123 PRO   B CG   1 ? 2 
ATOM   3338 C CD   . PRO   B 1 111 ? -9.381  -10.316 12.406  1   54.694  ? 123 PRO   B CD   1 ? 2 
ATOM   3339 H HA   . PRO   B 1 111 ? -7.205  -9.651  14.519  1   60.837  ? 123 PRO   B HA   1 c 2 
ATOM   3340 H HB2  . PRO   B 1 111 ? -6.393  -10.665 12.056  1   57.069  ? 123 PRO   B HB2  1 c 2 
ATOM   3341 H HB3  . PRO   B 1 111 ? -6.571  -11.495 13.398  1   61.61   ? 123 PRO   B HB3  1 c 2 
ATOM   3342 H HG2  . PRO   B 1 111 ? -8.246  -11.681 11.344  1   55.867  ? 123 PRO   B HG2  1 c 2 
ATOM   3343 H HG3  . PRO   B 1 111 ? -8.601  -12.19  12.802  1   59.893  ? 123 PRO   B HG3  1 c 2 
ATOM   3344 H HD2  . PRO   B 1 111 ? -9.542  -9.884  11.544  1   51.744  ? 123 PRO   B HD2  1 c 2 
ATOM   3345 H HD3  . PRO   B 1 111 ? -10.222 -10.682 12.74   1   55.727  ? 123 PRO   B HD3  1 c 2 
ATOM   3346 N N    . SER   B 1 112 ? -5.284  -8.345  13.449  1   60.419  ? 124 SER   B N    1 ? 2 
ATOM   3347 C CA   . SER   B 1 112 ? -4.276  -7.528  12.793  1   61.598  ? 124 SER   B CA   1 ? 2 
ATOM   3348 C C    . SER   B 1 112 ? -4.354  -7.679  11.274  1   57.443  ? 124 SER   B C    1 ? 2 
ATOM   3349 O O    . SER   B 1 112 ? -4.487  -8.785  10.762  1   55.854  ? 124 SER   B O    1 ? 2 
ATOM   3350 C CB   . SER   B 1 112 ? -2.901  -7.852  13.289  1   67.518  ? 124 SER   B CB   1 ? 2 
ATOM   3351 O OG   . SER   B 1 112 ? -2.852  -9.146  13.852  1   74.506  ? 124 SER   B OG   1 ? 2 
ATOM   3352 H H    . SER   B 1 112 ? -5.038  -8.865  14.159  1   63.391  ? 124 SER   B H    1 c 2 
ATOM   3353 H HA   . SER   B 1 112 ? -4.466  -6.582  13.017  1   60.335  ? 124 SER   B HA   1 c 2 
ATOM   3354 H HB2  . SER   B 1 112 ? -2.265  -7.794  12.551  1   67.445  ? 124 SER   B HB2  1 c 2 
ATOM   3355 H HB3  . SER   B 1 112 ? -2.642  -7.202  13.966  1   69.232  ? 124 SER   B HB3  1 c 2 
ATOM   3356 H HG   . SER   B 1 112 ? -1.832  -9.093  13.957  0   30      ? 124 SER   B HG   1 c 2 
ATOM   3357 N N    . ASN   B 1 113 ? -4.267  -6.532  10.608  1   53.336  ? 125 ASN   B N    1 ? 2 
ATOM   3358 C CA   . ASN   B 1 113 ? -4.031  -6.472  9.2     1   51.909  ? 125 ASN   B CA   1 ? 2 
ATOM   3359 C C    . ASN   B 1 113 ? -5.161  -7.156  8.411   1   51.839  ? 125 ASN   B C    1 ? 2 
ATOM   3360 O O    . ASN   B 1 113 ? -4.905  -7.799  7.408   1   45.269  ? 125 ASN   B O    1 ? 2 
ATOM   3361 C CB   . ASN   B 1 113 ? -2.683  -7.113  8.907   1   54.291  ? 125 ASN   B CB   1 ? 2 
ATOM   3362 C CG   . ASN   B 1 113 ? -1.53   -6.476  9.651   1   57.322  ? 125 ASN   B CG   1 ? 2 
ATOM   3363 O OD1  . ASN   B 1 113 ? -0.765  -7.191  10.292  1   61.069  ? 125 ASN   B OD1  1 ? 2 
ATOM   3364 N ND2  . ASN   B 1 113 ? -1.306  -5.181  9.537   1   55.85   ? 125 ASN   B ND2  1 ? 2 
ATOM   3365 H H    . ASN   B 1 113 ? -4.365  -5.746  11.064  1   53.731  ? 125 ASN   B H    1 c 2 
ATOM   3366 H HA   . ASN   B 1 113 ? -3.982  -5.527  8.931   1   51.013  ? 125 ASN   B HA   1 c 2 
ATOM   3367 H HB2  . ASN   B 1 113 ? -2.722  -8.062  9.137   1   55.765  ? 125 ASN   B HB2  1 c 2 
ATOM   3368 H HB3  . ASN   B 1 113 ? -2.506  -7.048  7.947   1   53.652  ? 125 ASN   B HB3  1 c 2 
ATOM   3369 H HD21 . ASN   B 1 113 ? -0.525  -4.846  9.79    1   58.388  ? 125 ASN   B HD21 1 c 2 
ATOM   3370 H HD22 . ASN   B 1 113 ? -1.929  -4.645  9.205   1   53.957  ? 125 ASN   B HD22 1 c 2 
ATOM   3371 N N    . ALA   B 1 114 ? -6.413  -7.023  8.844   1   48.285  ? 126 ALA   B N    1 ? 2 
ATOM   3372 C CA   . ALA   B 1 114 ? -7.501  -7.734  8.192   1   47.305  ? 126 ALA   B CA   1 ? 2 
ATOM   3373 C C    . ALA   B 1 114 ? -7.97   -6.96   6.954   1   45.742  ? 126 ALA   B C    1 ? 2 
ATOM   3374 O O    . ALA   B 1 114 ? -8.037  -5.735  6.961   1   46.73   ? 126 ALA   B O    1 ? 2 
ATOM   3375 C CB   . ALA   B 1 114 ? -8.635  -7.936  9.178   1   50.839  ? 126 ALA   B CB   1 ? 2 
ATOM   3376 H H    . ALA   B 1 114 ? -6.598  -6.476  9.552   1   48.884  ? 126 ALA   B H    1 c 2 
ATOM   3377 H HA   . ALA   B 1 114 ? -7.165  -8.625  7.898   1   49.297  ? 126 ALA   B HA   1 c 2 
ATOM   3378 H HB1  . ALA   B 1 114 ? -8.311  -8.424  9.953   1   52.005  ? 126 ALA   B HB1  1 c 2 
ATOM   3379 H HB2  . ALA   B 1 114 ? -8.979  -7.073  9.462   1   48.993  ? 126 ALA   B HB2  1 c 2 
ATOM   3380 H HB3  . ALA   B 1 114 ? -9.349  -8.442  8.755   1   49.817  ? 126 ALA   B HB3  1 c 2 
ATOM   3381 N N    . THR   B 1 115 ? -8.279  -7.69   5.864   1   43.86   ? 127 THR   B N    1 ? 2 
ATOM   3382 C CA   . THR   B 1 115 ? -9.049  -7.12   4.772   1   42.318  ? 127 THR   B CA   1 ? 2 
ATOM   3383 C C    . THR   B 1 115 ? -10.513 -7.45   5.022   1   41.462  ? 127 THR   B C    1 ? 2 
ATOM   3384 O O    . THR   B 1 115 ? -10.8   -8.492  5.564   1   41.246  ? 127 THR   B O    1 ? 2 
ATOM   3385 C CB   . THR   B 1 115 ? -8.52   -7.711  3.468   1   43.98   ? 127 THR   B CB   1 ? 2 
ATOM   3386 O OG1  . THR   B 1 115 ? -7.157  -7.306  3.419   1   44.562  ? 127 THR   B OG1  1 ? 2 
ATOM   3387 C CG2  . THR   B 1 115 ? -9.276  -7.265  2.228   1   43.205  ? 127 THR   B CG2  1 ? 2 
ATOM   3388 H H    . THR   B 1 115 ? -8.003  -8.56   5.806   1   45.825  ? 127 THR   B H    1 c 2 
ATOM   3389 H HA   . THR   B 1 115 ? -8.927  -6.148  4.762   1   41.195  ? 127 THR   B HA   1 c 2 
ATOM   3390 H HB   . THR   B 1 115 ? -8.558  -8.695  3.519   1   45.403  ? 127 THR   B HB   1 c 2 
ATOM   3391 H HG1  . THR   B 1 115 ? -7.118  -6.446  3.404   0   30      ? 127 THR   B HG1  1 c 2 
ATOM   3392 H HG21 . THR   B 1 115 ? -8.924  -7.73   1.45    1   44.462  ? 127 THR   B HG21 1 c 2 
ATOM   3393 H HG22 . THR   B 1 115 ? -9.166  -6.308  2.107   1   42.15   ? 127 THR   B HG22 1 c 2 
ATOM   3394 H HG23 . THR   B 1 115 ? -10.22  -7.473  2.327   1   43.055  ? 127 THR   B HG23 1 c 2 
ATOM   3395 N N    . LEU   B 1 116 ? -11.435 -6.567  4.635   1   40.906  ? 128 LEU   B N    1 ? 2 
ATOM   3396 C CA   . LEU   B 1 116 ? -12.861 -6.743  4.918   1   40.59   ? 128 LEU   B CA   1 ? 2 
ATOM   3397 C C    . LEU   B 1 116 ? -13.608 -6.553  3.615   1   40.02   ? 128 LEU   B C    1 ? 2 
ATOM   3398 O O    . LEU   B 1 116 ? -13.204 -5.757  2.751   1   35.616  ? 128 LEU   B O    1 ? 2 
ATOM   3399 C CB   . LEU   B 1 116 ? -13.534 -5.789  5.936   1   40.259  ? 128 LEU   B CB   1 ? 2 
ATOM   3400 C CG   . LEU   B 1 116 ? -12.778 -5.364  7.2     1   39.796  ? 128 LEU   B CG   1 ? 2 
ATOM   3401 C CD1  . LEU   B 1 116 ? -13.652 -4.62   8.215   1   42.052  ? 128 LEU   B CD1  1 ? 2 
ATOM   3402 C CD2  . LEU   B 1 116 ? -12.109 -6.46   7.896   1   41.571  ? 128 LEU   B CD2  1 ? 2 
ATOM   3403 H H    . LEU   B 1 116 ? -11.169 -5.822  4.176   1   39.615  ? 128 LEU   B H    1 c 2 
ATOM   3404 H HA   . LEU   B 1 116 ? -13     -7.676  5.218   1   42.179  ? 128 LEU   B HA   1 c 2 
ATOM   3405 H HB2  . LEU   B 1 116 ? -13.793 -4.971  5.453   1   39.064  ? 128 LEU   B HB2  1 c 2 
ATOM   3406 H HB3  . LEU   B 1 116 ? -14.38  -6.207  6.219   1   41.183  ? 128 LEU   B HB3  1 c 2 
ATOM   3407 H HG   . LEU   B 1 116 ? -12.068 -4.731  6.917   1   39.277  ? 128 LEU   B HG   1 c 2 
ATOM   3408 H HD11 . LEU   B 1 116 ? -14.159 -3.926  7.761   1   40.673  ? 128 LEU   B HD11 1 c 2 
ATOM   3409 H HD12 . LEU   B 1 116 ? -13.087 -4.214  8.894   1   41.709  ? 128 LEU   B HD12 1 c 2 
ATOM   3410 H HD13 . LEU   B 1 116 ? -14.265 -5.245  8.637   1   42.916  ? 128 LEU   B HD13 1 c 2 
ATOM   3411 H HD21 . LEU   B 1 116 ? -11.191 -6.531  7.583   1   41.388  ? 128 LEU   B HD21 1 c 2 
ATOM   3412 H HD22 . LEU   B 1 116 ? -12.576 -7.292  7.713   1   42.729  ? 128 LEU   B HD22 1 c 2 
ATOM   3413 H HD23 . LEU   B 1 116 ? -12.11  -6.292  8.853   1   42.474  ? 128 LEU   B HD23 1 c 2 
ATOM   3414 N N    . PHE   B 1 117 ? -14.746 -7.257  3.527   1   42.077  ? 129 PHE   B N    1 ? 2 
ATOM   3415 C CA   . PHE   B 1 117 ? -15.711 -7.067  2.473   1   40.531  ? 129 PHE   B CA   1 ? 2 
ATOM   3416 C C    . PHE   B 1 117 ? -17.06  -6.696  3.064   1   43.793  ? 129 PHE   B C    1 ? 2 
ATOM   3417 O O    . PHE   B 1 117 ? -17.491 -7.309  4.049   1   49.027  ? 129 PHE   B O    1 ? 2 
ATOM   3418 C CB   . PHE   B 1 117 ? -15.84  -8.396  1.77    1   41.74   ? 129 PHE   B CB   1 ? 2 
ATOM   3419 C CG   . PHE   B 1 117 ? -16.879 -8.346  0.66    1   47.49   ? 129 PHE   B CG   1 ? 2 
ATOM   3420 C CD1  . PHE   B 1 117 ? -16.597 -7.811  -0.586  1   48.699  ? 129 PHE   B CD1  1 ? 2 
ATOM   3421 C CD2  . PHE   B 1 117 ? -18.15  -8.844  0.854   1   54.243  ? 129 PHE   B CD2  1 ? 2 
ATOM   3422 C CE1  . PHE   B 1 117 ? -17.525 -7.786  -1.6    1   49.898  ? 129 PHE   B CE1  1 ? 2 
ATOM   3423 C CE2  . PHE   B 1 117 ? -19.093 -8.795  -0.164  1   57.328  ? 129 PHE   B CE2  1 ? 2 
ATOM   3424 C CZ   . PHE   B 1 117 ? -18.771 -8.257  -1.382  1   56.747  ? 129 PHE   B CZ   1 ? 2 
ATOM   3425 H H    . PHE   B 1 117 ? -14.922 -7.888  4.165   1   42.608  ? 129 PHE   B H    1 c 2 
ATOM   3426 H HA   . PHE   B 1 117 ? -15.402 -6.37   1.839   1   40.134  ? 129 PHE   B HA   1 c 2 
ATOM   3427 H HB2  . PHE   B 1 117 ? -14.968 -8.639  1.388   1   42.751  ? 129 PHE   B HB2  1 c 2 
ATOM   3428 H HB3  . PHE   B 1 117 ? -16.098 -9.079  2.427   1   44.283  ? 129 PHE   B HB3  1 c 2 
ATOM   3429 H HD1  . PHE   B 1 117 ? -15.73  -7.475  -0.75   1   46.821  ? 129 PHE   B HD1  1 c 2 
ATOM   3430 H HD2  . PHE   B 1 117 ? -18.385 -9.21   1.692   1   53.899  ? 129 PHE   B HD2  1 c 2 
ATOM   3431 H HE1  . PHE   B 1 117 ? -17.302 -7.407  -2.435  1   51.437  ? 129 PHE   B HE1  1 c 2 
ATOM   3432 H HE2  . PHE   B 1 117 ? -19.958 -9.133  -0.015  1   59.189  ? 129 PHE   B HE2  1 c 2 
ATOM   3433 H HZ   . PHE   B 1 117 ? -19.413 -8.234  -2.073  1   57.689  ? 129 PHE   B HZ   1 c 2 
ATOM   3434 N N    . PHE   B 1 118 ? -17.774 -5.818  2.366   1   45.062  ? 130 PHE   B N    1 ? 2 
ATOM   3435 C CA   . PHE   B 1 118 ? -19.154 -5.495  2.698   1   49.008  ? 130 PHE   B CA   1 ? 2 
ATOM   3436 C C    . PHE   B 1 118 ? -20.016 -5.422  1.444   1   50.964  ? 130 PHE   B C    1 ? 2 
ATOM   3437 O O    . PHE   B 1 118 ? -19.569 -4.921  0.409   1   53.943  ? 130 PHE   B O    1 ? 2 
ATOM   3438 C CB   . PHE   B 1 118 ? -19.308 -4.115  3.328   1   46.001  ? 130 PHE   B CB   1 ? 2 
ATOM   3439 C CG   . PHE   B 1 118 ? -18.688 -3.973  4.704   1   46.847  ? 130 PHE   B CG   1 ? 2 
ATOM   3440 C CD1  . PHE   B 1 118 ? -17.372 -3.575  4.855   1   44.752  ? 130 PHE   B CD1  1 ? 2 
ATOM   3441 C CD2  . PHE   B 1 118 ? -19.455 -4.193  5.833   1   48.121  ? 130 PHE   B CD2  1 ? 2 
ATOM   3442 C CE1  . PHE   B 1 118 ? -16.819 -3.486  6.118   1   44.921  ? 130 PHE   B CE1  1 ? 2 
ATOM   3443 C CE2  . PHE   B 1 118 ? -18.893 -4.096  7.073   1   48.986  ? 130 PHE   B CE2  1 ? 2 
ATOM   3444 C CZ   . PHE   B 1 118 ? -17.597 -3.726  7.223   1   47.544  ? 130 PHE   B CZ   1 ? 2 
ATOM   3445 H H    . PHE   B 1 118 ? -17.389 -5.399  1.651   1   44.456  ? 130 PHE   B H    1 c 2 
ATOM   3446 H HA   . PHE   B 1 118 ? -19.517 -6.182  3.313   1   49.704  ? 130 PHE   B HA   1 c 2 
ATOM   3447 H HB2  . PHE   B 1 118 ? -18.898 -3.453  2.727   1   45.621  ? 130 PHE   B HB2  1 c 2 
ATOM   3448 H HB3  . PHE   B 1 118 ? -20.266 -3.906  3.391   1   48.287  ? 130 PHE   B HB3  1 c 2 
ATOM   3449 H HD1  . PHE   B 1 118 ? -16.836 -3.425  4.093   1   43.961  ? 130 PHE   B HD1  1 c 2 
ATOM   3450 H HD2  . PHE   B 1 118 ? -20.354 -4.465  5.743   1   50.419  ? 130 PHE   B HD2  1 c 2 
ATOM   3451 H HE1  . PHE   B 1 118 ? -15.919 -3.221  6.221   1   43.958  ? 130 PHE   B HE1  1 c 2 
ATOM   3452 H HE2  . PHE   B 1 118 ? -19.423 -4.257  7.838   1   50.608  ? 130 PHE   B HE2  1 c 2 
ATOM   3453 H HZ   . PHE   B 1 118 ? -17.227 -3.639  8.086   1   47.344  ? 130 PHE   B HZ   1 c 2 
ATOM   3454 N N    . GLU   B 1 119 ? -21.289 -5.809  1.602   1   51.49   ? 131 GLU   B N    1 ? 2 
ATOM   3455 C CA   . GLU   B 1 119 ? -22.372 -5.396  0.706   1   55.219  ? 131 GLU   B CA   1 ? 2 
ATOM   3456 C C    . GLU   B 1 119 ? -23.186 -4.327  1.437   1   58.278  ? 131 GLU   B C    1 ? 2 
ATOM   3457 O O    . GLU   B 1 119 ? -23.534 -4.526  2.602   1   63.375  ? 131 GLU   B O    1 ? 2 
ATOM   3458 C CB   . GLU   B 1 119 ? -23.206 -6.637  0.391   1   59.645  ? 131 GLU   B CB   1 ? 2 
ATOM   3459 C CG   . GLU   B 1 119 ? -24.32  -6.307  -0.588  1   67.113  ? 131 GLU   B CG   1 ? 2 
ATOM   3460 C CD   . GLU   B 1 119 ? -25.021 -7.574  -1.028  1   74.877  ? 131 GLU   B CD   1 ? 2 
ATOM   3461 O OE1  . GLU   B 1 119 ? -24.796 -8.195  -2.102  1   70.076  ? 131 GLU   B OE1  1 ? 2 
ATOM   3462 O OE2  . GLU   B 1 119 ? -25.85  -7.912  -0.173  1   86.258  ? 131 GLU   B OE2  1 ? 2 
ATOM   3463 H H    . GLU   B 1 119 ? -21.495 -6.361  2.302   1   53.346  ? 131 GLU   B H    1 c 2 
ATOM   3464 H HA   . GLU   B 1 119 ? -21.985 -5.017  -0.121  1   54.825  ? 131 GLU   B HA   1 c 2 
ATOM   3465 H HB2  . GLU   B 1 119 ? -22.622 -7.328  0.013   1   60.524  ? 131 GLU   B HB2  1 c 2 
ATOM   3466 H HB3  . GLU   B 1 119 ? -23.587 -6.987  1.224   1   61.514  ? 131 GLU   B HB3  1 c 2 
ATOM   3467 H HG2  . GLU   B 1 119 ? -24.971 -5.711  -0.161  1   67.328  ? 131 GLU   B HG2  1 c 2 
ATOM   3468 H HG3  . GLU   B 1 119 ? -23.948 -5.855  -1.374  1   65.768  ? 131 GLU   B HG3  1 c 2 
ATOM   3469 N N    . ILE   B 1 120 ? -23.381 -3.148  0.832   1   61.41   ? 132 ILE   B N    1 ? 2 
ATOM   3470 C CA   . ILE   B 1 120 ? -24.087 -2.069  1.501   1   55.994  ? 132 ILE   B CA   1 ? 2 
ATOM   3471 C C    . ILE   B 1 120 ? -25.239 -1.6    0.653   1   59.284  ? 132 ILE   B C    1 ? 2 
ATOM   3472 O O    . ILE   B 1 120 ? -25.062 -1.313  -0.524  1   57.099  ? 132 ILE   B O    1 ? 2 
ATOM   3473 C CB   . ILE   B 1 120 ? -23.205 -0.86   1.79    1   53.466  ? 132 ILE   B CB   1 ? 2 
ATOM   3474 C CG1  . ILE   B 1 120 ? -21.962 -1.223  2.519   1   53.473  ? 132 ILE   B CG1  1 ? 2 
ATOM   3475 C CG2  . ILE   B 1 120 ? -24.01  0.193   2.557   1   54.8    ? 132 ILE   B CG2  1 ? 2 
ATOM   3476 C CD1  . ILE   B 1 120 ? -20.917 -0.114  2.488   1   51.114  ? 132 ILE   B CD1  1 ? 2 
ATOM   3477 H H    . ILE   B 1 120 ? -23.068 -3.015  -0.016  1   58.858  ? 132 ILE   B H    1 c 2 
ATOM   3478 H HA   . ILE   B 1 120 ? -24.437 -2.403  2.349   1   58.028  ? 132 ILE   B HA   1 c 2 
ATOM   3479 H HB   . ILE   B 1 120 ? -22.944 -0.471  0.931   1   53.656  ? 132 ILE   B HB   1 c 2 
ATOM   3480 H HG12 . ILE   B 1 120 ? -22.186 -1.424  3.451   1   53.13   ? 132 ILE   B HG12 1 c 2 
ATOM   3481 H HG13 . ILE   B 1 120 ? -21.578 -2.03   2.12    1   52.521  ? 132 ILE   B HG13 1 c 2 
ATOM   3482 H HG21 . ILE   B 1 120 ? -23.406 0.833   2.969   1   53.117  ? 132 ILE   B HG21 1 c 2 
ATOM   3483 H HG22 . ILE   B 1 120 ? -24.538 -0.24   3.249   1   56.202  ? 132 ILE   B HG22 1 c 2 
ATOM   3484 H HG23 . ILE   B 1 120 ? -24.603 0.662   1.946   1   56.566  ? 132 ILE   B HG23 1 c 2 
ATOM   3485 H HD11 . ILE   B 1 120 ? -20.83  0.231   1.579   1   51.261  ? 132 ILE   B HD11 1 c 2 
ATOM   3486 H HD12 . ILE   B 1 120 ? -20.058 -0.471  2.781   1   49.478  ? 132 ILE   B HD12 1 c 2 
ATOM   3487 H HD13 . ILE   B 1 120 ? -21.185 0.611   3.084   1   51.298  ? 132 ILE   B HD13 1 c 2 
ATOM   3488 N N    . GLU   B 1 121 ? -26.408 -1.49   1.301   1   68.974  ? 133 GLU   B N    1 ? 2 
ATOM   3489 C CA   . GLU   B 1 121 ? -27.561 -0.79   0.746   1   72.218  ? 133 GLU   B CA   1 ? 2 
ATOM   3490 C C    . GLU   B 1 121 ? -27.757 0.552   1.459   1   71.954  ? 133 GLU   B C    1 ? 2 
ATOM   3491 O O    . GLU   B 1 121 ? -27.95  0.615   2.67    1   77.196  ? 133 GLU   B O    1 ? 2 
ATOM   3492 C CB   . GLU   B 1 121 ? -28.79  -1.692  0.849   1   77.098  ? 133 GLU   B CB   1 ? 2 
ATOM   3493 C CG   . GLU   B 1 121 ? -29.961 -1.163  0.018   1   81.534  ? 133 GLU   B CG   1 ? 2 
ATOM   3494 C CD   . GLU   B 1 121 ? -31.205 -2.009  0.047   1   84.773  ? 133 GLU   B CD   1 ? 2 
ATOM   3495 O OE1  . GLU   B 1 121 ? -31.22  -3.066  0.691   1   87.294  ? 133 GLU   B OE1  1 ? 2 
ATOM   3496 O OE2  . GLU   B 1 121 ? -32.146 -1.586  -0.602  1   86.388  ? 133 GLU   B OE2  1 ? 2 
ATOM   3497 H H    . GLU   B 1 121 ? -26.492 -1.872  2.127   1   67.163  ? 133 GLU   B H    1 c 2 
ATOM   3498 H HA   . GLU   B 1 121 ? -27.388 -0.619  -0.211  1   72.327  ? 133 GLU   B HA   1 c 2 
ATOM   3499 H HB2  . GLU   B 1 121 ? -28.552 -2.591  0.542   1   77.192  ? 133 GLU   B HB2  1 c 2 
ATOM   3500 H HB3  . GLU   B 1 121 ? -29.059 -1.756  1.789   1   77.54   ? 133 GLU   B HB3  1 c 2 
ATOM   3501 H HG2  . GLU   B 1 121 ? -30.195 -0.265  0.336   1   81.049  ? 133 GLU   B HG2  1 c 2 
ATOM   3502 H HG3  . GLU   B 1 121 ? -29.671 -1.074  -0.915  1   80.734  ? 133 GLU   B HG3  1 c 2 
ATOM   3503 N N    . LEU   B 1 122 ? -27.692 1.637   0.691   1   71.527  ? 134 LEU   B N    1 ? 2 
ATOM   3504 C CA   . LEU   B 1 122 ? -28.053 2.96    1.193   1   70.485  ? 134 LEU   B CA   1 ? 2 
ATOM   3505 C C    . LEU   B 1 122 ? -29.573 3.139   1.175   1   79.4    ? 134 LEU   B C    1 ? 2 
ATOM   3506 O O    . LEU   B 1 122 ? -30.169 3.342   0.102   1   83.124  ? 134 LEU   B O    1 ? 2 
ATOM   3507 C CB   . LEU   B 1 122 ? -27.349 4.011   0.341   1   67.074  ? 134 LEU   B CB   1 ? 2 
ATOM   3508 C CG   . LEU   B 1 122 ? -27.515 5.461   0.822   1   65.179  ? 134 LEU   B CG   1 ? 2 
ATOM   3509 C CD1  . LEU   B 1 122 ? -27.263 5.578   2.314   1   61.551  ? 134 LEU   B CD1  1 ? 2 
ATOM   3510 C CD2  . LEU   B 1 122 ? -26.577 6.34    0.024   1   64.463  ? 134 LEU   B CD2  1 ? 2 
ATOM   3511 H H    . LEU   B 1 122 ? -27.413 1.558   -0.175  1   71.01   ? 134 LEU   B H    1 c 2 
ATOM   3512 H HA   . LEU   B 1 122 ? -27.734 3.033   2.128   1   69.374  ? 134 LEU   B HA   1 c 2 
ATOM   3513 H HB2  . LEU   B 1 122 ? -26.387 3.798   0.322   1   63.725  ? 134 LEU   B HB2  1 c 2 
ATOM   3514 H HB3  . LEU   B 1 122 ? -27.693 3.945   -0.579  1   68.871  ? 134 LEU   B HB3  1 c 2 
ATOM   3515 H HG   . LEU   B 1 122 ? -28.447 5.748   0.637   1   68.933  ? 134 LEU   B HG   1 c 2 
ATOM   3516 H HD11 . LEU   B 1 122 ? -28.054 5.292   2.802   1   64.42   ? 134 LEU   B HD11 1 c 2 
ATOM   3517 H HD12 . LEU   B 1 122 ? -27.064 6.502   2.537   1   62.393  ? 134 LEU   B HD12 1 c 2 
ATOM   3518 H HD13 . LEU   B 1 122 ? -26.509 5.016   2.562   1   59.355  ? 134 LEU   B HD13 1 c 2 
ATOM   3519 H HD21 . LEU   B 1 122 ? -26.572 6.055   -0.904  1   65.062  ? 134 LEU   B HD21 1 c 2 
ATOM   3520 H HD22 . LEU   B 1 122 ? -25.678 6.269   0.387   1   61.284  ? 134 LEU   B HD22 1 c 2 
ATOM   3521 H HD23 . LEU   B 1 122 ? -26.874 7.264   0.076   1   66.174  ? 134 LEU   B HD23 1 c 2 
ATOM   3522 N N    . LEU   B 1 123 ? -30.197 3.052   2.366   1   80.74   ? 135 LEU   B N    1 ? 2 
ATOM   3523 C CA   . LEU   B 1 123 ? -31.654 3.13    2.479   1   84.56   ? 135 LEU   B CA   1 ? 2 
ATOM   3524 C C    . LEU   B 1 123 ? -32.088 4.591   2.422   1   87.247  ? 135 LEU   B C    1 ? 2 
ATOM   3525 O O    . LEU   B 1 123 ? -32.945 4.944   1.627   1   91.783  ? 135 LEU   B O    1 ? 2 
ATOM   3526 C CB   . LEU   B 1 123 ? -32.174 2.482   3.762   1   87.518  ? 135 LEU   B CB   1 ? 2 
ATOM   3527 C CG   . LEU   B 1 123 ? -31.729 1.042   4.052   1   88.831  ? 135 LEU   B CG   1 ? 2 
ATOM   3528 C CD1  . LEU   B 1 123 ? -32.254 0.552   5.406   1   92.991  ? 135 LEU   B CD1  1 ? 2 
ATOM   3529 C CD2  . LEU   B 1 123 ? -32.201 0.104   2.94    1   90.963  ? 135 LEU   B CD2  1 ? 2 
ATOM   3530 H H    . LEU   B 1 123 ? -29.702 2.941   3.126   1   78.158  ? 135 LEU   B H    1 c 2 
ATOM   3531 H HA   . LEU   B 1 123 ? -32.048 2.659   1.701   1   87.263  ? 135 LEU   B HA   1 c 2 
ATOM   3532 H HB2  . LEU   B 1 123 ? -31.9   3.047   4.52    1   86.827  ? 135 LEU   B HB2  1 c 2 
ATOM   3533 H HB3  . LEU   B 1 123 ? -33.159 2.499   3.732   1   92.433  ? 135 LEU   B HB3  1 c 2 
ATOM   3534 H HG   . LEU   B 1 123 ? -30.738 1.021   4.077   1   84.144  ? 135 LEU   B HG   1 c 2 
ATOM   3535 H HD11 . LEU   B 1 123 ? -32.215 1.278   6.052   1   92.412  ? 135 LEU   B HD11 1 c 2 
ATOM   3536 H HD12 . LEU   B 1 123 ? -31.705 -0.186  5.719   1   90.71   ? 135 LEU   B HD12 1 c 2 
ATOM   3537 H HD13 . LEU   B 1 123 ? -33.174 0.254   5.31    1   96.997  ? 135 LEU   B HD13 1 c 2 
ATOM   3538 H HD21 . LEU   B 1 123 ? -31.711 0.295   2.123   1   89.043  ? 135 LEU   B HD21 1 c 2 
ATOM   3539 H HD22 . LEU   B 1 123 ? -33.152 0.237   2.784   1   95.473  ? 135 LEU   B HD22 1 c 2 
ATOM   3540 H HD23 . LEU   B 1 123 ? -32.044 -0.818  3.204   1   90.959  ? 135 LEU   B HD23 1 c 2 
ATOM   3541 N N    . ASP   B 1 124 ? -31.491 5.438   3.277   1   85.202  ? 136 ASP   B N    1 ? 2 
ATOM   3542 C CA   . ASP   B 1 124 ? -31.847 6.852   3.34    1   89.857  ? 136 ASP   B CA   1 ? 2 
ATOM   3543 C C    . ASP   B 1 124 ? -30.712 7.651   3.987   1   85.713  ? 136 ASP   B C    1 ? 2 
ATOM   3544 O O    . ASP   B 1 124 ? -29.852 7.086   4.655   1   78.749  ? 136 ASP   B O    1 ? 2 
ATOM   3545 C CB   . ASP   B 1 124 ? -33.168 7.051   4.074   1   99.3    ? 136 ASP   B CB   1 ? 2 
ATOM   3546 C CG   . ASP   B 1 124 ? -33.934 8.325   3.743   1   103.944 ? 136 ASP   B CG   1 ? 2 
ATOM   3547 O OD1  . ASP   B 1 124 ? -33.522 9.396   4.214   1   109.046 ? 136 ASP   B OD1  1 ? 2 
ATOM   3548 O OD2  . ASP   B 1 124 ? -34.924 8.244   2.991   1   108.065 ? 136 ASP   B OD2  1 ? 2 
ATOM   3549 H H    . ASP   B 1 124 ? -30.846 5.122   3.842   1   82.712  ? 136 ASP   B H    1 c 2 
ATOM   3550 H HA   . ASP   B 1 124 ? -31.968 7.179   2.419   1   91.056  ? 136 ASP   B HA   1 c 2 
ATOM   3551 H HB2  . ASP   B 1 124 ? -33.754 6.291   3.879   1   100.398 ? 136 ASP   B HB2  1 c 2 
ATOM   3552 H HB3  . ASP   B 1 124 ? -32.991 7.049   5.038   1   97.748  ? 136 ASP   B HB3  1 c 2 
ATOM   3553 N N    . PHE   B 1 125 ? -30.698 8.959   3.742   1   88.693  ? 137 PHE   B N    1 ? 2 
ATOM   3554 C CA   . PHE   B 1 125 ? -29.808 9.867   4.447   1   87.878  ? 137 PHE   B CA   1 ? 2 
ATOM   3555 C C    . PHE   B 1 125 ? -30.457 11.246  4.463   1   95.181  ? 137 PHE   B C    1 ? 2 
ATOM   3556 O O    . PHE   B 1 125 ? -30.997 11.663  3.437   1   102.795 ? 137 PHE   B O    1 ? 2 
ATOM   3557 C CB   . PHE   B 1 125 ? -28.445 9.918   3.758   1   83.08   ? 137 PHE   B CB   1 ? 2 
ATOM   3558 C CG   . PHE   B 1 125 ? -28.447 10.463  2.334   1   82.727  ? 137 PHE   B CG   1 ? 2 
ATOM   3559 C CD1  . PHE   B 1 125 ? -28.632 9.63    1.235   1   81.645  ? 137 PHE   B CD1  1 ? 2 
ATOM   3560 C CD2  . PHE   B 1 125 ? -28.237 11.813  2.095   1   82.181  ? 137 PHE   B CD2  1 ? 2 
ATOM   3561 C CE1  . PHE   B 1 125 ? -28.598 10.139  -0.058  1   82.911  ? 137 PHE   B CE1  1 ? 2 
ATOM   3562 C CE2  . PHE   B 1 125 ? -28.226 12.321  0.807   1   83.52   ? 137 PHE   B CE2  1 ? 2 
ATOM   3563 C CZ   . PHE   B 1 125 ? -28.409 11.49   -0.262  1   86.02   ? 137 PHE   B CZ   1 ? 2 
ATOM   3564 H H    . PHE   B 1 125 ? -31.261 9.3     3.108   1   91.415  ? 137 PHE   B H    1 c 2 
ATOM   3565 H HA   . PHE   B 1 125 ? -29.693 9.547   5.378   1   87.269  ? 137 PHE   B HA   1 c 2 
ATOM   3566 H HB2  . PHE   B 1 125 ? -27.845 10.472  4.305   1   81.814  ? 137 PHE   B HB2  1 c 2 
ATOM   3567 H HB3  . PHE   B 1 125 ? -28.073 9.008   3.745   1   80.002  ? 137 PHE   B HB3  1 c 2 
ATOM   3568 H HD1  . PHE   B 1 125 ? -28.761 8.704   1.37    1   80.545  ? 137 PHE   B HD1  1 c 2 
ATOM   3569 H HD2  . PHE   B 1 125 ? -28.112 12.398  2.826   1   83.325  ? 137 PHE   B HD2  1 c 2 
ATOM   3570 H HE1  . PHE   B 1 125 ? -28.735 9.564   -0.794  1   83.504  ? 137 PHE   B HE1  1 c 2 
ATOM   3571 H HE2  . PHE   B 1 125 ? -28.088 13.244  0.667   1   86.249  ? 137 PHE   B HE2  1 c 2 
ATOM   3572 H HZ   . PHE   B 1 125 ? -28.397 11.838  -1.139  1   86.893  ? 137 PHE   B HZ   1 c 2 
ATOM   3573 N N    . LYS   B 1 126 ? -30.374 11.932  5.618   1   95.804  ? 138 LYS   B N    1 ? 2 
ATOM   3574 C CA   . LYS   B 1 126 ? -30.967 13.254  5.808   1   97.385  ? 138 LYS   B CA   1 ? 2 
ATOM   3575 C C    . LYS   B 1 126 ? -29.931 14.162  6.477   1   93.141  ? 138 LYS   B C    1 ? 2 
ATOM   3576 O O    . LYS   B 1 126 ? -28.95  13.701  7.037   1   84.324  ? 138 LYS   B O    1 ? 2 
ATOM   3577 C CB   . LYS   B 1 126 ? -32.32  13.226  6.554   1   100.62  ? 138 LYS   B CB   1 ? 2 
ATOM   3578 H H    . LYS   B 1 126 ? -29.924 11.556  6.32    1   92.987  ? 138 LYS   B H    1 c 2 
ATOM   3579 H HA   . LYS   B 1 126 ? -31.15  13.632  4.911   1   98.368  ? 138 LYS   B HA   1 c 2 
ATOM   3580 H HB2  . LYS   B 1 126 ? -32.014 13.128  7.646   0   30      ? 138 LYS   B HB2  1 c 2 
ATOM   3581 H HB3  . LYS   B 1 126 ? -33.048 13.173  6.102   0   30      ? 138 LYS   B HB3  1 c 2 
ATOM   3582 N N    . GLY   B 1 127 ? -30.146 15.477  6.39    1   99.847  ? 139 GLY   B N    1 ? 2 
ATOM   3583 C CA   . GLY   B 1 127 ? -29.251 16.436  7.021   1   101.02  ? 139 GLY   B CA   1 ? 2 
ATOM   3584 C C    . GLY   B 1 127 ? -29.493 16.449  8.523   1   103.517 ? 139 GLY   B C    1 ? 2 
ATOM   3585 O O    . GLY   B 1 127 ? -30.633 16.25   8.95    1   105.415 ? 139 GLY   B O    1 ? 2 
ATOM   3586 H H    . GLY   B 1 127 ? -30.868 15.788  5.923   1   102.693 ? 139 GLY   B H    1 c 2 
ATOM   3587 H HA2  . GLY   B 1 127 ? -28.316 16.188  6.83    1   96.967  ? 139 GLY   B HA2  1 c 2 
ATOM   3588 H HA3  . GLY   B 1 127 ? -29.416 17.332  6.647   1   104.063 ? 139 GLY   B HA3  1 c 2 
ATOM   3589 N N    . GLU   B 1 128 ? -28.414 16.612  9.304   1   100.397 ? 140 GLU   B N    1 ? 2 
ATOM   3590 C CA   . GLU   B 1 128 ? -28.555 17.068  10.683  1   105.911 ? 140 GLU   B CA   1 ? 2 
ATOM   3591 C C    . GLU   B 1 128 ? -29.292 18.444  10.68   1   111.335 ? 140 GLU   B C    1 ? 2 
ATOM   3592 O O    . GLU   B 1 128 ? -29.388 19.059  9.596   1   111.701 ? 140 GLU   B O    1 ? 2 
ATOM   3593 C CB   . GLU   B 1 128 ? -27.176 16.954  11.346  1   102.437 ? 140 GLU   B CB   1 ? 2 
ATOM   3594 O OXT  . GLU   B 1 128 ? -29.819 18.85   11.74   1   115.372 ? 140 GLU   B OXT  1 ? 2 
ATOM   3595 H H    . GLU   B 1 128 ? -27.58  16.437  8.972   1   97.586  ? 140 GLU   B H    1 c 2 
ATOM   3596 H HA   . GLU   B 1 128 ? -29.144 16.421  11.149  1   105.814 ? 140 GLU   B HA   1 c 2 
ATOM   3597 H HB2  . GLU   B 1 128 ? -26.477 17.028  10.592  0   30      ? 140 GLU   B HB2  1 c 2 
ATOM   3598 H HB3  . GLU   B 1 128 ? -27.325 17.014  12.244  0   30      ? 140 GLU   B HB3  1 c 2 
HETATM 3599 C CAK  . A1IN0 C 2 .   ? -2.966  12.257  19.471  1   51.358  ? 201 A1IN0 A CAK  1 ? 1 
HETATM 3600 C CAL  . A1IN0 C 2 .   ? -2.222  11.06   19.912  1   54.013  ? 201 A1IN0 A CAL  1 ? 1 
HETATM 3601 C CAM  . A1IN0 C 2 .   ? -1.903  11.027  21.36   1   55.658  ? 201 A1IN0 A CAM  1 ? 1 
HETATM 3602 C CAN  . A1IN0 C 2 .   ? -3.224  10.856  22.002  1   56.179  ? 201 A1IN0 A CAN  1 ? 1 
HETATM 3603 C CAO  . A1IN0 C 2 .   ? -4.106  12.088  21.733  1   52.011  ? 201 A1IN0 A CAO  1 ? 1 
HETATM 3604 C CAJ  . A1IN0 C 2 .   ? -4.299  12.327  20.213  1   53.873  ? 201 A1IN0 A CAJ  1 ? 1 
HETATM 3605 C CAI  . A1IN0 C 2 .   ? -4.961  13.763  19.947  1   55.605  ? 201 A1IN0 A CAI  1 ? 1 
HETATM 3606 C CAB  . A1IN0 C 2 .   ? -6.292  13.86   20.462  1   52.122  ? 201 A1IN0 A CAB  1 ? 1 
HETATM 3607 O OAA  . A1IN0 C 2 .   ? -6.892  12.802  20.707  1   49.923  ? 201 A1IN0 A OAA  1 ? 1 
HETATM 3608 N N    . A1IN0 C 2 .   ? -6.899  15.083  20.75   1   48.431  ? 201 A1IN0 A N    1 ? 1 
HETATM 3609 C CAH  . A1IN0 C 2 .   ? -6.228  16.403  20.447  1   51.915  ? 201 A1IN0 A CAH  1 ? 1 
HETATM 3610 C CAG  . A1IN0 C 2 .   ? -6.449  17.409  21.515  1   54.726  ? 201 A1IN0 A CAG  1 ? 1 
HETATM 3611 C CAF  . A1IN0 C 2 .   ? -7.928  17.581  21.685  1   54.532  ? 201 A1IN0 A CAF  1 ? 1 
HETATM 3612 C CB   . A1IN0 C 2 .   ? -8.436  16.32   22.313  1   52.074  ? 201 A1IN0 A CB   1 ? 1 
HETATM 3613 C CA   . A1IN0 C 2 .   ? -8.322  15.148  21.284  1   50.026  ? 201 A1IN0 A CA   1 ? 1 
HETATM 3614 C C    . A1IN0 C 2 .   ? -9.112  15.426  20.122  1   55.153  ? 201 A1IN0 A C    1 ? 1 
HETATM 3615 O O    . A1IN0 C 2 .   ? -10.329 15.502  20.252  1   49.521  ? 201 A1IN0 A O    1 ? 1 
HETATM 3616 O OBA  . A1IN0 C 2 .   ? -8.385  15.613  18.908  1   52.198  ? 201 A1IN0 A OBA  1 ? 1 
HETATM 3617 C CAZ  . A1IN0 C 2 .   ? -8.931  16.3    17.761  1   63.426  ? 201 A1IN0 A CAZ  1 ? 1 
HETATM 3618 C CAY  . A1IN0 C 2 .   ? -8.374  15.794  16.485  1   67.64   ? 201 A1IN0 A CAY  1 ? 1 
HETATM 3619 C CAX  . A1IN0 C 2 .   ? -7.459  16.558  15.677  1   76.555  ? 201 A1IN0 A CAX  1 ? 1 
HETATM 3620 C CAW  . A1IN0 C 2 .   ? -6.836  16.148  14.456  1   75.168  ? 201 A1IN0 A CAW  1 ? 1 
HETATM 3621 O OAV  . A1IN0 C 2 .   ? -5.751  15.11   14.596  1   77.522  ? 201 A1IN0 A OAV  1 ? 1 
HETATM 3622 C CAU  . A1IN0 C 2 .   ? -5.5    14.752  15.908  1   72.508  ? 201 A1IN0 A CAU  1 ? 1 
HETATM 3623 C CAR  . A1IN0 C 2 .   ? -4.686  15.579  16.677  1   70.192  ? 201 A1IN0 A CAR  1 ? 1 
HETATM 3624 O OAS  . A1IN0 C 2 .   ? -4.161  16.658  15.98   1   77.235  ? 201 A1IN0 A OAS  1 ? 1 
HETATM 3625 C CAT  . A1IN0 C 2 .   ? -4.15   18.015  16.506  1   77.534  ? 201 A1IN0 A CAT  1 ? 1 
HETATM 3626 C CAQ  . A1IN0 C 2 .   ? -4.452  15.275  18.039  1   66.825  ? 201 A1IN0 A CAQ  1 ? 1 
HETATM 3627 C CAP  . A1IN0 C 2 .   ? -5.079  14.141  18.598  1   67.4    ? 201 A1IN0 A CAP  1 ? 1 
HETATM 3628 C CBG  . A1IN0 C 2 .   ? -5.954  13.353  17.795  1   71.027  ? 201 A1IN0 A CBG  1 ? 1 
HETATM 3629 C CBD  . A1IN0 C 2 .   ? -6.143  13.624  16.445  1   74.92   ? 201 A1IN0 A CBD  1 ? 1 
HETATM 3630 O OBE  . A1IN0 C 2 .   ? -6.972  12.879  15.609  1   80.92   ? 201 A1IN0 A OBE  1 ? 1 
HETATM 3631 C CBF  . A1IN0 C 2 .   ? -7.322  11.554  16.051  1   76.14   ? 201 A1IN0 A CBF  1 ? 1 
HETATM 3632 H HAK  . A1IN0 C 2 .   ? -3.323  12.14   18.494  1   54.395  ? 201 A1IN0 A HAK  1 c 1 
HETATM 3633 H HB6  . A1IN0 C 2 .   ? -2.601  13.302  19.69   1   53.321  ? 201 A1IN0 A HB6  1 c 1 
HETATM 3634 H HAL  . A1IN0 C 2 .   ? -1.28   11.033  19.365  1   56.181  ? 201 A1IN0 A HAL  1 c 1 
HETATM 3635 H HB7  . A1IN0 C 2 .   ? -2.795  10.173  19.643  1   54.335  ? 201 A1IN0 A HB7  1 c 1 
HETATM 3636 H HAM  . A1IN0 C 2 .   ? -1.434  11.962  21.672  1   55.453  ? 201 A1IN0 A HAM  1 c 1 
HETATM 3637 H HB8  . A1IN0 C 2 .   ? -1.253  10.178  21.582  1   56.368  ? 201 A1IN0 A HB8  1 c 1 
HETATM 3638 H HAN  . A1IN0 C 2 .   ? -3.087  10.757  23.076  1   53.767  ? 201 A1IN0 A HAN  1 c 1 
HETATM 3639 H HB9  . A1IN0 C 2 .   ? -3.718  9.959   21.625  1   55.152  ? 201 A1IN0 A HB9  1 c 1 
HETATM 3640 H HCA  . A1IN0 C 2 .   ? -5.083  11.946  22.044  1   51.573  ? 201 A1IN0 A HCA  1 c 1 
HETATM 3641 H HAO  . A1IN0 C 2 .   ? -3.683  13.006  22.019  1   52.625  ? 201 A1IN0 A HAO  1 c 1 
HETATM 3642 H HAJ  . A1IN0 C 2 .   ? -4.948  11.548  19.817  1   53.559  ? 201 A1IN0 A HAJ  1 c 1 
HETATM 3643 H HAI  . A1IN0 C 2 .   ? -4.335  14.491  20.457  1   56.363  ? 201 A1IN0 A HAI  1 c 1 
HETATM 3644 H HAH  . A1IN0 C 2 .   ? -6.573  16.807  19.498  1   54.013  ? 201 A1IN0 A HAH  1 c 1 
HETATM 3645 H HB5  . A1IN0 C 2 .   ? -5.155  16.282  20.401  1   53.072  ? 201 A1IN0 A HB5  1 c 1 
HETATM 3646 H HAG  . A1IN0 C 2 .   ? -6.198  18.428  21.269  1   55.421  ? 201 A1IN0 A HAG  1 c 1 
HETATM 3647 H HB4  . A1IN0 C 2 .   ? -6.155  17.111  22.476  1   52.566  ? 201 A1IN0 A HB4  1 c 1 
HETATM 3648 H HAF  . A1IN0 C 2 .   ? -8.479  17.617  20.799  1   55.567  ? 201 A1IN0 A HAF  1 c 1 
HETATM 3649 H HB3  . A1IN0 C 2 .   ? -8.211  18.285  22.408  1   53.923  ? 201 A1IN0 A HB3  1 c 1 
HETATM 3650 H HB2  . A1IN0 C 2 .   ? -7.878  15.944  23.105  1   50.392  ? 201 A1IN0 A HB2  1 c 1 
HETATM 3651 H HB1  . A1IN0 C 2 .   ? -9.455  16.422  22.508  1   51.335  ? 201 A1IN0 A HB1  1 c 1 
HETATM 3652 H HA   . A1IN0 C 2 .   ? -8.623  14.206  21.743  1   49.6    ? 201 A1IN0 A HA   1 c 1 
HETATM 3653 H HCE  . A1IN0 C 2 .   ? -9.941  16.096  17.634  1   61.918  ? 201 A1IN0 A HCE  1 c 1 
HETATM 3654 H HAZ  . A1IN0 C 2 .   ? -8.712  17.363  17.738  1   62.756  ? 201 A1IN0 A HAZ  1 c 1 
HETATM 3655 H HAY  . A1IN0 C 2 .   ? -8.677  14.805  16.144  1   68.827  ? 201 A1IN0 A HAY  1 c 1 
HETATM 3656 H HAX  . A1IN0 C 2 .   ? -7.17   17.538  16.058  1   74.119  ? 201 A1IN0 A HAX  1 c 1 
HETATM 3657 H HCD  . A1IN0 C 2 .   ? -7.507  15.679  13.816  1   77.88   ? 201 A1IN0 A HCD  1 c 1 
HETATM 3658 H HAW  . A1IN0 C 2 .   ? -6.335  16.954  14.008  1   78.747  ? 201 A1IN0 A HAW  1 c 1 
HETATM 3659 H HCC  . A1IN0 C 2 .   ? -4.322  18.723  15.696  1   79.98   ? 201 A1IN0 A HCC  1 c 1 
HETATM 3660 H HAT  . A1IN0 C 2 .   ? -3.179  18.216  16.961  1   77.548  ? 201 A1IN0 A HAT  1 c 1 
HETATM 3661 H HCB  . A1IN0 C 2 .   ? -4.931  18.123  17.257  1   75.399  ? 201 A1IN0 A HCB  1 c 1 
HETATM 3662 H HAQ  . A1IN0 C 2 .   ? -3.818  15.917  18.634  1   67.107  ? 201 A1IN0 A HAQ  1 c 1 
HETATM 3663 H HBG  . A1IN0 C 2 .   ? -6.414  12.469  18.229  1   68.99   ? 201 A1IN0 A HBG  1 c 1 
HETATM 3664 H HCG  . A1IN0 C 2 .   ? -7.773  11.018  15.223  1   78.842  ? 201 A1IN0 A HCG  1 c 1 
HETATM 3665 H HBF  . A1IN0 C 2 .   ? -8.027  11.615  16.856  1   74.843  ? 201 A1IN0 A HBF  1 c 1 
HETATM 3666 H HCF  . A1IN0 C 2 .   ? -6.43   11.019  16.377  1   76.681  ? 201 A1IN0 A HCF  1 c 1 
HETATM 3667 C CAK  . A1IN0 D 2 .   ? -17.938 -7.372  11.89   1   50.63   ? 201 A1IN0 B CAK  1 ? 2 
HETATM 3668 C CAL  . A1IN0 D 2 .   ? -17.031 -8.549  11.545  1   53.341  ? 201 A1IN0 B CAL  1 ? 2 
HETATM 3669 C CAM  . A1IN0 D 2 .   ? -17.097 -8.727  9.943   1   49.083  ? 201 A1IN0 B CAM  1 ? 2 
HETATM 3670 C CAN  . A1IN0 D 2 .   ? -16.656 -7.373  9.413   1   44.065  ? 201 A1IN0 B CAN  1 ? 2 
HETATM 3671 C CAO  . A1IN0 D 2 .   ? -17.461 -6.211  9.675   1   42.085  ? 201 A1IN0 B CAO  1 ? 2 
HETATM 3672 C CAJ  . A1IN0 D 2 .   ? -17.507 -6.093  11.12   1   45.814  ? 201 A1IN0 B CAJ  1 ? 2 
HETATM 3673 C CAI  . A1IN0 D 2 .   ? -18.366 -4.913  11.526  1   46.751  ? 201 A1IN0 B CAI  1 ? 2 
HETATM 3674 C CAB  . A1IN0 D 2 .   ? -17.824 -3.704  11.077  1   46.436  ? 201 A1IN0 B CAB  1 ? 2 
HETATM 3675 O OAA  . A1IN0 D 2 .   ? -16.593 -3.608  11.017  1   47.675  ? 201 A1IN0 B OAA  1 ? 2 
HETATM 3676 N N    . A1IN0 D 2 .   ? -18.535 -2.586  10.711  1   48.742  ? 201 A1IN0 B N    1 ? 2 
HETATM 3677 C CAH  . A1IN0 D 2 .   ? -20.011 -2.498  10.949  1   54.699  ? 201 A1IN0 B CAH  1 ? 2 
HETATM 3678 C CAG  . A1IN0 D 2 .   ? -20.703 -1.901  9.911   1   54.345  ? 201 A1IN0 B CAG  1 ? 2 
HETATM 3679 C CAF  . A1IN0 D 2 .   ? -20.203 -0.559  9.807   1   53.859  ? 201 A1IN0 B CAF  1 ? 2 
HETATM 3680 C CB   . A1IN0 D 2 .   ? -18.729 -0.519  9.32    1   47.754  ? 201 A1IN0 B CB   1 ? 2 
HETATM 3681 C CA   . A1IN0 D 2 .   ? -17.883 -1.303  10.382  1   49.436  ? 201 A1IN0 B CA   1 ? 2 
HETATM 3682 C C    . A1IN0 D 2 .   ? -17.627 -0.497  11.57   1   54.18   ? 201 A1IN0 B C    1 ? 2 
HETATM 3683 O O    . A1IN0 D 2 .   ? -17.153 0.576   11.425  1   53.069  ? 201 A1IN0 B O    1 ? 2 
HETATM 3684 O OBA  . A1IN0 D 2 .   ? -18.098 -0.972  12.778  1   67.953  ? 201 A1IN0 B OBA  1 ? 2 
HETATM 3685 C CAZ  . A1IN0 D 2 .   ? -17.925 -0.458  14.105  1   67.119  ? 201 A1IN0 B CAZ  1 ? 2 
HETATM 3686 C CAY  . A1IN0 D 2 .   ? -18.906 -1.019  14.977  1   64.533  ? 201 A1IN0 B CAY  1 ? 2 
HETATM 3687 C CAX  . A1IN0 D 2 .   ? -18.418 -1.724  16.085  1   66.292  ? 201 A1IN0 B CAX  1 ? 2 
HETATM 3688 C CAW  . A1IN0 D 2 .   ? -19.1   -2.455  17.06   1   66.706  ? 201 A1IN0 B CAW  1 ? 2 
HETATM 3689 O OAV  . A1IN0 D 2 .   ? -18.645 -3.908  16.999  1   63.879  ? 201 A1IN0 B OAV  1 ? 2 
HETATM 3690 C CAU  . A1IN0 D 2 .   ? -18.621 -4.227  15.703  1   60.2    ? 201 A1IN0 B CAU  1 ? 2 
HETATM 3691 C CAR  . A1IN0 D 2 .   ? -19.804 -4.408  14.976  1   60.799  ? 201 A1IN0 B CAR  1 ? 2 
HETATM 3692 O OAS  . A1IN0 D 2 .   ? -21.016 -4.4    15.683  1   67.829  ? 201 A1IN0 B OAS  1 ? 2 
HETATM 3693 C CAT  . A1IN0 D 2 .   ? -22.21  -4.176  14.927  1   66.149  ? 201 A1IN0 B CAT  1 ? 2 
HETATM 3694 C CAQ  . A1IN0 D 2 .   ? -19.69  -4.675  13.582  1   56.065  ? 201 A1IN0 B CAQ  1 ? 2 
HETATM 3695 C CAP  . A1IN0 D 2 .   ? -18.414 -4.689  12.918  1   51.766  ? 201 A1IN0 B CAP  1 ? 2 
HETATM 3696 C CBG  . A1IN0 D 2 .   ? -17.235 -4.469  13.706  1   52.423  ? 201 A1IN0 B CBG  1 ? 2 
HETATM 3697 C CBD  . A1IN0 D 2 .   ? -17.351 -4.266  15.099  1   56.753  ? 201 A1IN0 B CBD  1 ? 2 
HETATM 3698 O OBE  . A1IN0 D 2 .   ? -16.342 -4.036  15.959  1   54.39   ? 201 A1IN0 B OBE  1 ? 2 
HETATM 3699 C CBF  . A1IN0 D 2 .   ? -15.092 -4.51   15.541  1   55.381  ? 201 A1IN0 B CBF  1 ? 2 
HETATM 3700 H HAK  . A1IN0 D 2 .   ? -17.936 -7.107  12.87   1   52.683  ? 201 A1IN0 B HAK  1 c 2 
HETATM 3701 H HB6  . A1IN0 D 2 .   ? -18.824 -7.855  11.559  1   52.88   ? 201 A1IN0 B HB6  1 c 2 
HETATM 3702 H HAL  . A1IN0 D 2 .   ? -17.393 -9.454  12.036  1   55.714  ? 201 A1IN0 B HAL  1 c 2 
HETATM 3703 H HB7  . A1IN0 D 2 .   ? -16.01  -8.345  11.857  1   51.304  ? 201 A1IN0 B HB7  1 c 2 
HETATM 3704 H HAM  . A1IN0 D 2 .   ? -18.113 -8.953  9.62    1   50.673  ? 201 A1IN0 B HAM  1 c 2 
HETATM 3705 H HB8  . A1IN0 D 2 .   ? -16.41  -9.508  9.617   1   49.403  ? 201 A1IN0 B HB8  1 c 2 
HETATM 3706 H HAN  . A1IN0 D 2 .   ? -16.586 -7.465  8.331   1   42.63   ? 201 A1IN0 B HAN  1 c 2 
HETATM 3707 H HB9  . A1IN0 D 2 .   ? -15.655 -7.18   9.791   1   43.07   ? 201 A1IN0 B HB9  1 c 2 
HETATM 3708 H HCA  . A1IN0 D 2 .   ? -17.016 -5.328  9.37    1   40.742  ? 201 A1IN0 B HCA  1 c 2 
HETATM 3709 H HAO  . A1IN0 D 2 .   ? -18.472 -6.323  9.423   1   44.117  ? 201 A1IN0 B HAO  1 c 2 
HETATM 3710 H HAJ  . A1IN0 D 2 .   ? -16.488 -5.894  11.447  1   44.869  ? 201 A1IN0 B HAJ  1 c 2 
HETATM 3711 H HAI  . A1IN0 D 2 .   ? -19.359 -5.07   11.122  1   48.732  ? 201 A1IN0 B HAI  1 c 2 
HETATM 3712 H HAH  . A1IN0 D 2 .   ? -20.198 -1.946  11.868  1   55.827  ? 201 A1IN0 B HAH  1 c 2 
HETATM 3713 H HB5  . A1IN0 D 2 .   ? -20.434 -3.486  11.065  1   55.682  ? 201 A1IN0 B HB5  1 c 2 
HETATM 3714 H HAG  . A1IN0 D 2 .   ? -21.723 -1.844  10.093  1   56.845  ? 201 A1IN0 B HAG  1 c 2 
HETATM 3715 H HB4  . A1IN0 D 2 .   ? -20.479 -2.295  8.97    1   53.01   ? 201 A1IN0 B HB4  1 c 2 
HETATM 3716 H HAF  . A1IN0 D 2 .   ? -20.155 -0.026  10.705  1   54.053  ? 201 A1IN0 B HAF  1 c 2 
HETATM 3717 H HB3  . A1IN0 D 2 .   ? -20.669 -0.026  9.047   1   52.44   ? 201 A1IN0 B HB3  1 c 2 
HETATM 3718 H HB2  . A1IN0 D 2 .   ? -18.529 -1.104  8.474   1   47.415  ? 201 A1IN0 B HB2  1 c 2 
HETATM 3719 H HB1  . A1IN0 D 2 .   ? -18.261 0.399   9.323   1   47.882  ? 201 A1IN0 B HB1  1 c 2 
HETATM 3720 H HA   . A1IN0 D 2 .   ? -16.92  -1.511  9.917   1   47.453  ? 201 A1IN0 B HA   1 c 2 
HETATM 3721 H HCE  . A1IN0 D 2 .   ? -17.025 -0.753  14.519  1   66.159  ? 201 A1IN0 B HCE  1 c 2 
HETATM 3722 H HAZ  . A1IN0 D 2 .   ? -18.091 0.646   14.177  1   66.443  ? 201 A1IN0 B HAZ  1 c 2 
HETATM 3723 H HAY  . A1IN0 D 2 .   ? -19.971 -0.981  14.744  1   66.576  ? 201 A1IN0 B HAY  1 c 2 
HETATM 3724 H HAX  . A1IN0 D 2 .   ? -17.335 -1.731  16.203  1   64.412  ? 201 A1IN0 B HAX  1 c 2 
HETATM 3725 H HCD  . A1IN0 D 2 .   ? -18.835 -2.174  18.032  1   69.501  ? 201 A1IN0 B HCD  1 c 2 
HETATM 3726 H HAW  . A1IN0 D 2 .   ? -20.132 -2.493  16.914  1   68.121  ? 201 A1IN0 B HAW  1 c 2 
HETATM 3727 H HCC  . A1IN0 D 2 .   ? -23.03  -3.954  15.61   1   70.442  ? 201 A1IN0 B HCC  1 c 2 
HETATM 3728 H HAT  . A1IN0 D 2 .   ? -22.453 -5.07   14.353  1   66.871  ? 201 A1IN0 B HAT  1 c 2 
HETATM 3729 H HCB  . A1IN0 D 2 .   ? -22.068 -3.333  14.251  1   63.589  ? 201 A1IN0 B HCB  1 c 2 
HETATM 3730 H HAQ  . A1IN0 D 2 .   ? -20.588 -4.819  12.998  1   56.807  ? 201 A1IN0 B HAQ  1 c 2 
HETATM 3731 H HBG  . A1IN0 D 2 .   ? -16.253 -4.496  13.241  1   50.171  ? 201 A1IN0 B HBG  1 c 2 
HETATM 3732 H HCG  . A1IN0 D 2 .   ? -14.414 -4.514  16.395  1   56.58   ? 201 A1IN0 B HCG  1 c 2 
HETATM 3733 H HBF  . A1IN0 D 2 .   ? -14.686 -3.854  14.77   1   51.418  ? 201 A1IN0 B HBF  1 c 2 
HETATM 3734 H HCF  . A1IN0 D 2 .   ? -15.179 -5.528  15.156  1   54.579  ? 201 A1IN0 B HCF  1 c 2 
HETATM 3735 O O    . HOH   E 3 .   ? -16.385 20.227  21.807  1   75.924  ? 301 HOH   A O    1 ? ? 
HETATM 3736 O O    . HOH   E 3 .   ? -10.089 5.99    21.679  1   49.796  ? 302 HOH   A O    1 ? ? 
HETATM 3737 O O    . HOH   E 3 .   ? -10.095 3.809   19.845  1   46.735  ? 303 HOH   A O    1 ? ? 
HETATM 3738 O O    . HOH   E 3 .   ? -0.686  7.316   39.499  1   53.16   ? 304 HOH   A O    1 ? ? 
HETATM 3739 O O    . HOH   E 3 .   ? -6.523  9.109   36.528  1   55.335  ? 305 HOH   A O    1 ? ? 
HETATM 3740 O O    . HOH   E 3 .   ? 2.718   13.35   25.81   1   65.628  ? 306 HOH   A O    1 ? ? 
HETATM 3741 O O    . HOH   E 3 .   ? -8.868  15.059  42.097  1   51.418  ? 307 HOH   A O    1 ? ? 
HETATM 3742 O O    . HOH   E 3 .   ? -16.464 6.944   18.589  1   54.334  ? 308 HOH   A O    1 ? ? 
HETATM 3743 O O    . HOH   E 3 .   ? -13.517 14.806  17.221  1   59.679  ? 309 HOH   A O    1 ? ? 
HETATM 3744 O O    . HOH   E 3 .   ? 0.733   8.622   35.727  1   58.56   ? 310 HOH   A O    1 ? ? 
HETATM 3745 O O    . HOH   F 3 .   ? -6.932  -5.024  11.126  1   44.833  ? 301 HOH   B O    1 ? ? 
HETATM 3746 O O    . HOH   F 3 .   ? -0.911  -9.702  10.872  1   52.095  ? 302 HOH   B O    1 ? ? 
HETATM 3747 O O    . HOH   F 3 .   ? -6.78   7.925   -0.187  1   47.418  ? 303 HOH   B O    1 ? ? 
HETATM 3748 O O    . HOH   F 3 .   ? -7.325  -0.217  14.611  1   53.36   ? 304 HOH   B O    1 ? ? 
HETATM 3749 O O    . HOH   F 3 .   ? -18.605 8.358   10.962  1   62.838  ? 305 HOH   B O    1 ? ? 
HETATM 3750 O O    . HOH   F 3 .   ? -10.12  8.545   0.012   1   50.444  ? 306 HOH   B O    1 ? ? 
HETATM 3751 O O    . HOH   F 3 .   ? -9.267  -3.125  -1.336  1   41.287  ? 307 HOH   B O    1 ? ? 
HETATM 3752 O O    . HOH   F 3 .   ? -34.493 -4.071  9.946   1   61.241  ? 308 HOH   B O    1 ? ? 
HETATM 3753 O O    . HOH   F 3 .   ? -8.62   -4.483  9.496   1   46.696  ? 309 HOH   B O    1 ? ? 
HETATM 3754 O O    . HOH   F 3 .   ? -2.755  -5.183  18.838  1   62.788  ? 310 HOH   B O    1 ? ? 
HETATM 3755 O O    . HOH   F 3 .   ? -6.668  -6.673  0.272   1   51.812  ? 311 HOH   B O    1 ? ? 
HETATM 3756 O O    . HOH   F 3 .   ? -14.139 -14.606 -3.958  1   52.038  ? 312 HOH   B O    1 ? ? 
HETATM 3757 O O    . HOH   F 3 .   ? -8.975  -11.337 8.241   1   47.614  ? 313 HOH   B O    1 ? ? 
HETATM 3758 O O    . HOH   F 3 .   ? -8.093  -5.112  -1.452  1   41.405  ? 314 HOH   B O    1 ? ? 
HETATM 3759 O O    . HOH   F 3 .   ? -12.572 -10.431 1.325   1   51.121  ? 315 HOH   B O    1 ? ? 
HETATM 3760 O O    . HOH   F 3 .   ? -2.56   1.649   10.077  1   49.848  ? 316 HOH   B O    1 ? ? 
HETATM 3761 O O    . HOH   F 3 .   ? -1.298  -2.249  0       0.5 48.895  ? 317 HOH   B O    1 ? ? 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N    . GLU   A 8   ? 1.09562  0.728997 0.815772 0.0746684   0.120746    -0.0626738  20  GLU   A N    
2    C CA   . GLU   A 8   ? 1.18334  0.810398 0.884486 0.0396477   0.141272    -0.0725088  20  GLU   A CA   
3    C C    . GLU   A 8   ? 1.16446  0.799662 0.832269 0.040508    0.130344    -0.0628659  20  GLU   A C    
4    O O    . GLU   A 8   ? 1.28824  0.903259 0.925317 0.0181558   0.151969    -0.064282   20  GLU   A O    
5    C CB   . GLU   A 8   ? 1.12421  0.684215 0.799594 0.0219464   0.175616    -0.0736724  20  GLU   A CB   
6    H H    . GLU   A 8   ? 1.12529  0.747109 0.858566 0.0750209   0.131035    -0.0688699  20  GLU   A H    
7    H HA   . GLU   A 8   ? 1.08414  0.753018 0.818476 0.0254071   0.139887    -0.0891641  20  GLU   A HA   
10   N N    . GLN   A 9   ? 1.2819   0.948029 0.954603 0.0648401   0.0982529   -0.0550571  21  GLN   A N    
11   C CA   . GLN   A 9   ? 1.3455   1.04261  1.00434  0.0639319   0.0805549   -0.0579943  21  GLN   A CA   
12   C C    . GLN   A 9   ? 1.3218   1.07196  1.02159  0.0417418   0.0795355   -0.0831436  21  GLN   A C    
13   O O    . GLN   A 9   ? 1.19584  0.975119 0.944102 0.0341384   0.0790691   -0.0950566  21  GLN   A O    
14   C CB   . GLN   A 9   ? 1.37023  1.10044  1.05033  0.091643    0.0435105   -0.0518741  21  GLN   A CB   
15   C CG   . GLN   A 9   ? 1.25604  1.03012  1.00273  0.0906971   0.0356898   -0.0638639  21  GLN   A CG   
16   C CD   . GLN   A 9   ? 1.26784  1.07499  1.04408  0.116087    0.00682996  -0.057204   21  GLN   A CD   
17   O OE1  . GLN   A 9   ? 1.25181  1.09174  1.03259  0.120525    -0.0203611  -0.0593803  21  GLN   A OE1  
18   N NE2  . GLN   A 9   ? 1.18604  0.988722 0.985661 0.131526    0.0132601   -0.0526604  21  GLN   A NE2  
19   H H    . GLN   A 9   ? 1.26273  0.929955 0.947773 0.0838071   0.0866478   -0.0486226  21  GLN   A H    
20   H HA   . GLN   A 9   ? 1.39221  1.05897  1.00618  0.0622555   0.0900765   -0.0486495  21  GLN   A HA   
21   H HB2  . GLN   A 9   ? 1.3419   1.09345  1.01574  0.0908238   0.029021    -0.056724   21  GLN   A HB2  
22   H HB3  . GLN   A 9   ? 1.39345  1.09636  1.0492   0.110913    0.0390845   -0.0355868  21  GLN   A HB3  
23   H HG2  . GLN   A 9   ? 1.27216  1.02766  1.02467  0.0860031   0.0538779   -0.0650207  21  GLN   A HG2  
24   H HG3  . GLN   A 9   ? 1.22791  1.03088  0.99574  0.0757486   0.0331162   -0.0769458  21  GLN   A HG3  
25   H HE21 . GLN   A 9   ? 1.23492  1.03759  1.03383  0.153226    0.0015967   -0.0431671  21  GLN   A HE21 
26   H HE22 . GLN   A 9   ? 1.1942   0.995471 1.01004  0.121157    0.0288324   -0.0602574  21  GLN   A HE22 
27   N N    . GLY   A 10  ? 1.05431  0.81825  0.733658 0.0350248   0.0769842   -0.0912203  22  GLY   A N    
28   C CA   . GLY   A 10  ? 0.847122 0.658389 0.564706 0.0242693   0.0684724   -0.113506   22  GLY   A CA   
29   C C    . GLY   A 10  ? 0.862563 0.683634 0.581742 0.00155439  0.0957911   -0.13018    22  GLY   A C    
30   O O    . GLY   A 10  ? 0.823712 0.619122 0.519395 -0.0135287  0.125077    -0.1271     22  GLY   A O    
31   H H    . GLY   A 10  ? 1.11313  0.854305 0.751931 0.038706    0.0809995   -0.082508   22  GLY   A H    
32   H HA2  . GLY   A 10  ? 0.888934 0.709936 0.596952 0.0326333   0.0514161   -0.115572   22  GLY   A HA2  
33   H HA3  . GLY   A 10  ? 0.848863 0.679412 0.603305 0.0246076   0.0598631   -0.116758   22  GLY   A HA3  
34   N N    . GLU   A 11  ? 0.798317 0.65913  0.548512 -0.00152802 0.0865573   -0.149575   23  GLU   A N    
35   C CA   . GLU   A 11  ? 0.828329 0.709817 0.582101 -0.0166519  0.108673    -0.16799    23  GLU   A CA   
36   C C    . GLU   A 11  ? 0.712833 0.620803 0.511539 -0.032572   0.120042    -0.178973   23  GLU   A C    
37   O O    . GLU   A 11  ? 0.642565 0.566942 0.476325 -0.0280488  0.102579    -0.178875   23  GLU   A O    
38   C CB   . GLU   A 11  ? 0.927843 0.832817 0.682555 -0.00608163 0.0942179   -0.184829   23  GLU   A CB   
39   C CG   . GLU   A 11  ? 0.956486 0.903995 0.761932 -0.00788037 0.091115    -0.206198   23  GLU   A CG   
40   C CD   . GLU   A 11  ? 1.04905  1.00883  0.85525  0.00688367  0.0758707   -0.224      23  GLU   A CD   
41   O OE1  . GLU   A 11  ? 1.01533  0.964594 0.825339 0.0195877   0.0467711   -0.222942   23  GLU   A OE1  
42   O OE2  . GLU   A 11  ? 0.957391 0.937974 0.759949 0.00261561  0.0979499   -0.241066   23  GLU   A OE2  
43   H H    . GLU   A 11  ? 0.785893 0.661691 0.55694  0.0063029   0.0665537   -0.151651   23  GLU   A H    
44   H HA   . GLU   A 11  ? 0.862536 0.722476 0.582588 -0.0236666  0.127879    -0.162327   23  GLU   A HA   
45   H HB2  . GLU   A 11  ? 0.952117 0.850366 0.675575 -0.00896084 0.108692    -0.187597   23  GLU   A HB2  
46   H HB3  . GLU   A 11  ? 0.914414 0.81239  0.66501  0.00576777  0.0724852   -0.17971    23  GLU   A HB3  
47   H HG2  . GLU   A 11  ? 0.923486 0.876619 0.755672 -0.00657415 0.0784813   -0.201718   23  GLU   A HG2  
48   H HG3  . GLU   A 11  ? 0.95758  0.919542 0.769482 -0.0197077  0.111792    -0.213789   23  GLU   A HG3  
49   N N    . ASP   A 12  ? 0.698062 0.608309 0.490732 -0.0536525  0.150676    -0.186977   24  ASP   A N    
50   C CA   . ASP   A 12  ? 0.731744 0.669396 0.562417 -0.0727884  0.162702    -0.200405   24  ASP   A CA   
51   C C    . ASP   A 12  ? 0.726646 0.723843 0.598903 -0.0679446  0.152119    -0.222137   24  ASP   A C    
52   O O    . ASP   A 12  ? 0.660139 0.680199 0.530274 -0.0715038  0.166614    -0.236097   24  ASP   A O    
53   C CB   . ASP   A 12  ? 0.803759 0.722697 0.615041 -0.101668   0.200082    -0.203128   24  ASP   A CB   
54   C CG   . ASP   A 12  ? 0.783778 0.733841 0.634295 -0.126872   0.212842    -0.221847   24  ASP   A CG   
55   O OD1  . ASP   A 12  ? 0.71008  0.701294 0.600642 -0.118324   0.190705    -0.231834   24  ASP   A OD1  
56   O OD2  . ASP   A 12  ? 0.781148 0.711283 0.618612 -0.156531   0.244595    -0.225735   24  ASP   A OD2  
57   H H    . ASP   A 12  ? 0.75629  0.652165 0.519198 -0.0578623  0.164892    -0.184662   24  ASP   A H    
58   H HA   . ASP   A 12  ? 0.712262 0.643141 0.554318 -0.0692186  0.152294    -0.194555   24  ASP   A HA   
59   H HB2  . ASP   A 12  ? 0.830026 0.702597 0.610029 -0.100802   0.205631    -0.186888   24  ASP   A HB2  
60   H HB3  . ASP   A 12  ? 0.815095 0.744858 0.615226 -0.106207   0.212351    -0.208843   24  ASP   A HB3  
61   N N    . ILE   A 13  ? 0.633181 0.653465 0.540068 -0.056971   0.12699     -0.223692   25  ILE   A N    
62   C CA   . ILE   A 13  ? 0.644579 0.711444 0.58739  -0.0450336  0.111767    -0.239717   25  ILE   A CA   
63   C C    . ILE   A 13  ? 0.58562  0.700809 0.566571 -0.0590006  0.117525    -0.255206   25  ILE   A C    
64   O O    . ILE   A 13  ? 0.644771 0.800612 0.658643 -0.0454261  0.100534    -0.265641   25  ILE   A O    
65   C CB   . ILE   A 13  ? 0.641979 0.701209 0.595018 -0.0231769  0.0786527   -0.230112   25  ILE   A CB   
66   C CG1  . ILE   A 13  ? 0.647502 0.696618 0.607114 -0.0269007  0.0677975   -0.214669   25  ILE   A CG1  
67   C CG2  . ILE   A 13  ? 0.698834 0.724514 0.622023 -0.00953042 0.0687108   -0.223697   25  ILE   A CG2  
68   C CD1  . ILE   A 13  ? 0.695683 0.740706 0.667812 -0.011389   0.0389438   -0.204316   25  ILE   A CD1  
69   H H    . ILE   A 13  ? 0.645764 0.651464 0.552656 -0.0560695  0.119932    -0.214084   25  ILE   A H    
70   H HA   . ILE   A 13  ? 0.64822  0.722489 0.584317 -0.0423169  0.119942    -0.248593   25  ILE   A HA   
71   H HB   . ILE   A 13  ? 0.638331 0.724572 0.614849 -0.0153091  0.0701419   -0.240127   25  ILE   A HB   
72   H HG12 . ILE   A 13  ? 0.666424 0.689083 0.605722 -0.0312771  0.0752602   -0.205285   25  ILE   A HG12 
73   H HG13 . ILE   A 13  ? 0.645365 0.717039 0.620438 -0.0360261  0.0733552   -0.221239   25  ILE   A HG13 
74   H HG21 . ILE   A 13  ? 0.679734 0.707209 0.615436 0.0022159   0.0500322   -0.22473    25  ILE   A HG21 
75   H HG22 . ILE   A 13  ? 0.695855 0.696511 0.600776 -0.011772   0.0679934   -0.210287   25  ILE   A HG22 
76   H HG23 . ILE   A 13  ? 0.708215 0.736352 0.61745  -0.0104476  0.0816382   -0.232782   25  ILE   A HG23 
77   H HD11 . ILE   A 13  ? 0.671956 0.732014 0.657767 -0.00273539 0.030685    -0.212459   25  ILE   A HD11 
78   H HD12 . ILE   A 13  ? 0.661812 0.712485 0.642528 -0.0153504  0.0348527   -0.197565   25  ILE   A HD12 
79   H HD13 . ILE   A 13  ? 0.682726 0.704292 0.640122 -0.00652878 0.0330687   -0.196664   25  ILE   A HD13 
80   N N    . THR   A 14  ? 0.610118 0.72114  0.585981 -0.0850772  0.140803    -0.258707   26  THR   A N    
81   C CA   . THR   A 14  ? 0.694962 0.858628 0.707881 -0.102611   0.145315    -0.27847    26  THR   A CA   
82   C C    . THR   A 14  ? 0.729674 0.946703 0.768225 -0.111966   0.162982    -0.301946   26  THR   A C    
83   O O    . THR   A 14  ? 0.698883 0.89907  0.714837 -0.116139   0.184133    -0.301723   26  THR   A O    
84   C CB   . THR   A 14  ? 0.581856 0.721249 0.583045 -0.131112   0.164107    -0.279537   26  THR   A CB   
85   O OG1  . THR   A 14  ? 0.652601 0.748735 0.621766 -0.150848   0.195723    -0.275571   26  THR   A OG1  
86   C CG2  . THR   A 14  ? 0.682773 0.779267 0.664613 -0.121153   0.15036     -0.261107   26  THR   A CG2  
87   H H    . THR   A 14  ? 0.650313 0.724778 0.59906  -0.0925523  0.153451    -0.249492   26  THR   A H    
88   H HA   . THR   A 14  ? 0.628388 0.812956 0.65946  -0.0895022  0.123928    -0.277983   26  THR   A HA   
89   H HB   . THR   A 14  ? 0.620063 0.800054 0.647085 -0.143977   0.165202    -0.296022   26  THR   A HB   
91   H HG21 . THR   A 14  ? 0.669207 0.740795 0.638763 -0.137218   0.165681    -0.262586   26  THR   A HG21 
92   H HG22 . THR   A 14  ? 0.650153 0.717646 0.613832 -0.105769   0.14393     -0.246007   26  THR   A HG22 
93   H HG23 . THR   A 14  ? 0.624601 0.748466 0.624385 -0.114006   0.133013    -0.263593   26  THR   A HG23 
94   N N    . SER   A 15  ? 0.749256 1.0347   0.834043 -0.116371   0.155135    -0.322589   27  SER   A N    
95   C CA   . SER   A 15  ? 0.725029 1.07921  0.847808 -0.126429   0.171649    -0.349371   27  SER   A CA   
96   C C    . SER   A 15  ? 0.671535 1.0186   0.784656 -0.170603   0.211788    -0.358982   27  SER   A C    
97   O O    . SER   A 15  ? 0.818651 1.18808  0.936108 -0.183512   0.239653    -0.370721   27  SER   A O    
98   C CB   . SER   A 15  ? 0.735195 1.16711  0.910657 -0.116039   0.147476    -0.367302   27  SER   A CB   
99   O OG   . SER   A 15  ? 0.724099 1.16618  0.911425 -0.0735406  0.120047    -0.362419   27  SER   A OG   
100  H H    . SER   A 15  ? 0.716748 1.00967  0.810034 -0.112545   0.138617    -0.320173   27  SER   A H    
101  H HA   . SER   A 15  ? 0.723521 1.07698  0.842117 -0.110044   0.173004    -0.349401   27  SER   A HA   
102  H HB2  . SER   A 15  ? 0.719942 1.14375  0.891202 -0.121718   0.135998    -0.36215    27  SER   A HB2  
103  H HB3  . SER   A 15  ? 0.732216 1.21503  0.936828 -0.132062   0.161845    -0.387717   27  SER   A HB3  
105  N N    . LYS   A 16  ? 0.641286 0.951342 0.737657 -0.193755   0.216337    -0.353457   28  LYS   A N    
106  C CA   . LYS   A 16  ? 0.68409  0.981737 0.774807 -0.239953   0.252363    -0.364862   28  LYS   A CA   
107  C C    . LYS   A 16  ? 0.702452 0.911802 0.73275  -0.247934   0.279733    -0.340583   28  LYS   A C    
108  O O    . LYS   A 16  ? 0.81474  0.997794 0.830485 -0.286193   0.314104    -0.344526   28  LYS   A O    
109  C CB   . LYS   A 16  ? 0.64843  0.946865 0.749293 -0.259308   0.243238    -0.375343   28  LYS   A CB   
110  H H    . LYS   A 16  ? 0.637835 0.927272 0.72534  -0.181128   0.197474    -0.342881   28  LYS   A H    
111  H HA   . LYS   A 16  ? 0.674951 1.0283   0.797138 -0.253273   0.264527    -0.384145   28  LYS   A HA   
114  N N    . LYS   A 17  ? 0.751358 0.911586 0.744721 -0.213414   0.262807    -0.314766   29  LYS   A N    
115  C CA   . LYS   A 17  ? 0.804335 0.880434 0.735499 -0.212611   0.279292    -0.287937   29  LYS   A CA   
116  C C    . LYS   A 17  ? 0.827084 0.832206 0.728661 -0.235406   0.295459    -0.277156   29  LYS   A C    
117  O O    . LYS   A 17  ? 0.805943 0.756602 0.669035 -0.258644   0.327049    -0.266847   29  LYS   A O    
118  C CB   . LYS   A 17  ? 0.875451 0.963179 0.790018 -0.224794   0.309212    -0.291403   29  LYS   A CB   
119  C CG   . LYS   A 17  ? 0.901867 1.03694  0.83019  -0.192996   0.292917    -0.299106   29  LYS   A CG   
120  C CD   . LYS   A 17  ? 0.978982 1.05852  0.861833 -0.158474   0.269089    -0.274293   29  LYS   A CD   
121  C CE   . LYS   A 17  ? 1.07873  1.18621  0.960405 -0.131419   0.258599    -0.282956   29  LYS   A CE   
122  N NZ   . LYS   A 17  ? 1.00589  1.14554  0.930068 -0.102317   0.220446    -0.291016   29  LYS   A NZ   
123  H H    . LYS   A 17  ? 0.704668 0.885329 0.71211  -0.188889   0.238342    -0.313641   29  LYS   A H    
124  H HA   . LYS   A 17  ? 0.789248 0.847483 0.706897 -0.184922   0.257885    -0.274175   29  LYS   A HA   
125  H HB2  . LYS   A 17  ? 0.890226 1.01087  0.828313 -0.252478   0.329605    -0.308378   29  LYS   A HB2  
126  H HB3  . LYS   A 17  ? 0.922199 0.951333 0.790364 -0.228273   0.322399    -0.272413   29  LYS   A HB3  
127  H HG2  . LYS   A 17  ? 0.863339 1.04777  0.834545 -0.182844   0.274665    -0.31368    29  LYS   A HG2  
128  H HG3  . LYS   A 17  ? 0.930338 1.08563  0.855606 -0.205517   0.316478    -0.307671   29  LYS   A HG3  
129  H HD2  . LYS   A 17  ? 1.02362  1.05144  0.863104 -0.166733   0.283177    -0.257332   29  LYS   A HD2  
130  H HD3  . LYS   A 17  ? 0.953021 1.02428  0.847126 -0.145579   0.245575    -0.268472   29  LYS   A HD3  
131  H HE2  . LYS   A 17  ? 1.05907  1.20421  0.953781 -0.142326   0.278929    -0.298964   29  LYS   A HE2  
132  H HE3  . LYS   A 17  ? 1.07469  1.14065  0.913217 -0.122047   0.256973    -0.267868   29  LYS   A HE3  
133  H HZ1  . LYS   A 17  ? 0.988162 1.16251  0.948038 -0.109541   0.218734    -0.301742   29  LYS   A HZ1  
134  H HZ2  . LYS   A 17  ? 1.00193  1.1079   0.91167  -0.0919751  0.202944    -0.276036   29  LYS   A HZ2  
135  H HZ3  . LYS   A 17  ? 1.00991  1.16823  0.938566 -0.0871616  0.215892    -0.300427   29  LYS   A HZ3  
136  N N    . ASP   A 18  ? 0.824557 0.821886 0.738147 -0.226168   0.274309    -0.277501   30  ASP   A N    
137  C CA   . ASP   A 18  ? 0.960635 0.892593 0.850711 -0.24353    0.28855     -0.2731     30  ASP   A CA   
138  C C    . ASP   A 18  ? 1.08769  0.96299  0.946633 -0.207636   0.268416    -0.246161   30  ASP   A C    
139  O O    . ASP   A 18  ? 1.07726  0.910086 0.926349 -0.207388   0.269332    -0.244247   30  ASP   A O    
140  C CB   . ASP   A 18  ? 0.884664 0.861736 0.815101 -0.261797   0.281175    -0.301133   30  ASP   A CB   
141  C CG   . ASP   A 18  ? 0.778263 0.798068 0.730851 -0.227856   0.242529    -0.299018   30  ASP   A CG   
142  O OD1  . ASP   A 18  ? 0.734262 0.725614 0.665729 -0.194457   0.226189    -0.273825   30  ASP   A OD1  
143  O OD2  . ASP   A 18  ? 0.694712 0.781117 0.6853   -0.23543    0.22864     -0.321643   30  ASP   A OD2  
144  H H    . ASP   A 18  ? 0.797553 0.829458 0.733196 -0.20803    0.251122    -0.280902   30  ASP   A H    
145  H HA   . ASP   A 18  ? 0.998892 0.895607 0.866909 -0.264905   0.314631    -0.269995   30  ASP   A HA   
146  H HB2  . ASP   A 18  ? 0.920401 0.852054 0.834895 -0.274718   0.292526    -0.302115   30  ASP   A HB2  
147  H HB3  . ASP   A 18  ? 0.882673 0.907602 0.83994  -0.282949   0.289997    -0.320283   30  ASP   A HB3  
148  N N    . ARG   A 19  ? 1.03162  0.912657 0.879234 -0.176738   0.249375    -0.228816   31  ARG   A N    
149  C CA   . ARG   A 19  ? 0.998918 0.83601  0.821003 -0.144225   0.230042    -0.204005   31  ARG   A CA   
150  C C    . ARG   A 19  ? 0.835143 0.688312 0.683903 -0.132933   0.210205    -0.209137   31  ARG   A C    
151  O O    . ARG   A 19  ? 0.802392 0.616123 0.634977 -0.113063   0.202699    -0.193221   31  ARG   A O    
152  C CB   . ARG   A 19  ? 1.11987  0.871798 0.888141 -0.142936   0.248922    -0.180852   31  ARG   A CB   
153  C CG   . ARG   A 19  ? 1.31959  1.05861  1.05128  -0.148409   0.264407    -0.17007    31  ARG   A CG   
154  C CD   . ARG   A 19  ? 1.51678  1.16857  1.18462  -0.146671   0.283034    -0.142034   31  ARG   A CD   
155  N NE   . ARG   A 19  ? 1.61788  1.23298  1.26993  -0.109052   0.25778     -0.120594   31  ARG   A NE   
156  C CZ   . ARG   A 19  ? 1.53839  1.16911  1.18119  -0.0771201  0.229095    -0.107295   31  ARG   A CZ   
157  N NH1  . ARG   A 19  ? 1.44916  1.1255   1.09348  -0.0761548  0.220815    -0.114232   31  ARG   A NH1  
158  N NH2  . ARG   A 19  ? 1.609    1.21028  1.24258  -0.0463332  0.209454    -0.0895611  31  ARG   A NH2  
159  H H    . ARG   A 19  ? 1.00996  0.925394 0.86761  -0.176101   0.248336    -0.234371   31  ARG   A H    
160  H HA   . ARG   A 19  ? 0.966611 0.82218  0.788332 -0.127411   0.215398    -0.198179   31  ARG   A HA   
161  H HB2  . ARG   A 19  ? 1.17219  0.897126 0.937179 -0.161941   0.26693     -0.187088   31  ARG   A HB2  
162  H HB3  . ARG   A 19  ? 1.13773  0.869537 0.896554 -0.119113   0.233283    -0.166768   31  ARG   A HB3  
163  H HG2  . ARG   A 19  ? 1.27215  1.03739  1.00681  -0.129468   0.245813    -0.167047   31  ARG   A HG2  
164  H HG3  . ARG   A 19  ? 1.30102  1.06812  1.04771  -0.172332   0.280935    -0.185795   31  ARG   A HG3  
165  H HD2  . ARG   A 19  ? 1.53525  1.18625  1.17717  -0.147824   0.290015    -0.134742   31  ARG   A HD2  
166  H HD3  . ARG   A 19  ? 1.55008  1.17047  1.21199  -0.169495   0.305476    -0.145639   31  ARG   A HD3  
167  H HE   . ARG   A 19  ? 1.59999  1.18279  1.25071  -0.10802    0.262045    -0.118119   31  ARG   A HE   
168  H HH11 . ARG   A 19  ? 1.50193  1.16842  1.11945  -0.0862363  0.235953    -0.111322   31  ARG   A HH11 
169  H HH12 . ARG   A 19  ? 1.42092  1.13573  1.09207  -0.0655524  0.201138    -0.122183   31  ARG   A HH12 
170  H HH21 . ARG   A 19  ? 1.64104  1.19188  1.24653  -0.0413654  0.218334    -0.0755055  31  ARG   A HH21 
171  H HH22 . ARG   A 19  ? 1.54612  1.17878  1.20282  -0.0305546  0.187728    -0.0918776  31  ARG   A HH22 
172  N N    . GLY   A 20  ? 0.791565 0.708404 0.68034  -0.141182   0.199296    -0.229619   32  GLY   A N    
173  C CA   . GLY   A 20  ? 0.719727 0.657063 0.627994 -0.133582   0.182454    -0.234736   32  GLY   A CA   
174  C C    . GLY   A 20  ? 0.854474 0.801311 0.766997 -0.102372   0.154502    -0.216103   32  GLY   A C    
175  O O    . GLY   A 20  ? 0.740557 0.672027 0.650432 -0.08911    0.147289    -0.207009   32  GLY   A O    
176  H H    . GLY   A 20  ? 0.774701 0.72523  0.677915 -0.150503   0.202089    -0.240266   32  GLY   A H    
177  H HA2  . GLY   A 20  ? 0.789977 0.692752 0.685584 -0.138902   0.193657    -0.235475   32  GLY   A HA2  
178  H HA3  . GLY   A 20  ? 0.74576  0.725942 0.67665  -0.144782   0.178982    -0.250759   32  GLY   A HA3  
179  N N    . VAL   A 21  ? 0.847791 0.82194  0.769026 -0.0924362  0.14088     -0.21317    33  VAL   A N    
180  C CA   . VAL   A 21  ? 0.666489 0.65208  0.595495 -0.0687552  0.113951    -0.199602   33  VAL   A CA   
181  C C    . VAL   A 21  ? 0.751525 0.708768 0.655516 -0.0571374  0.113446    -0.188326   33  VAL   A C    
182  O O    . VAL   A 21  ? 0.612995 0.581325 0.512952 -0.0616164  0.120837    -0.197004   33  VAL   A O    
183  C CB   . VAL   A 21  ? 0.575716 0.610785 0.534129 -0.0628961  0.0931049   -0.206516   33  VAL   A CB   
184  C CG1  . VAL   A 21  ? 0.523755 0.555327 0.486429 -0.0434467  0.0681247   -0.190504   33  VAL   A CG1  
185  C CG2  . VAL   A 21  ? 0.612417 0.682913 0.589498 -0.0748319  0.0920403   -0.218866   33  VAL   A CG2  
186  H H    . VAL   A 21  ? 0.808503 0.793502 0.731264 -0.101989   0.150096    -0.221449   33  VAL   A H    
187  H HA   . VAL   A 21  ? 0.690249 0.664549 0.617823 -0.0626352  0.109324    -0.191667   33  VAL   A HA   
188  H HB   . VAL   A 21  ? 0.590383 0.638076 0.552436 -0.0642418  0.0965074   -0.214654   33  VAL   A HB   
189  H HG11 . VAL   A 21  ? 0.534025 0.553332 0.492749 -0.041862   0.0673206   -0.181772   33  VAL   A HG11 
190  H HG12 . VAL   A 21  ? 0.542282 0.560063 0.49556  -0.0362014  0.0653542   -0.187296   33  VAL   A HG12 
191  H HG13 . VAL   A 21  ? 0.520198 0.575738 0.498678 -0.0402929  0.0559211   -0.192786   33  VAL   A HG13 
192  H HG21 . VAL   A 21  ? 0.581432 0.680407 0.573989 -0.0680038  0.0772289   -0.220407   33  VAL   A HG21 
193  H HG22 . VAL   A 21  ? 0.61062  0.686816 0.588553 -0.0901573  0.107148    -0.232073   33  VAL   A HG22 
194  H HG23 . VAL   A 21  ? 0.597577 0.657175 0.569313 -0.0739845  0.0909987   -0.212674   33  VAL   A HG23 
195  N N    . LEU   A 22  ? 0.710097 0.636734 0.598219 -0.0417456  0.104732    -0.170846   34  LEU   A N    
196  C CA   . LEU   A 22  ? 0.671582 0.574175 0.532531 -0.0276177  0.0975067   -0.158814   34  LEU   A CA   
197  C C    . LEU   A 22  ? 0.610388 0.531836 0.488582 -0.0118908  0.0679888   -0.153204   34  LEU   A C    
198  O O    . LEU   A 22  ? 0.634316 0.564212 0.53172  -0.00659864 0.05712     -0.146224   34  LEU   A O    
199  C CB   . LEU   A 22  ? 0.712831 0.567422 0.543947 -0.0220424  0.109514    -0.14405    34  LEU   A CB   
200  C CG   . LEU   A 22  ? 0.820654 0.645606 0.632444 -0.0431598  0.141467    -0.149918   34  LEU   A CG   
201  C CD1  . LEU   A 22  ? 0.900101 0.667708 0.685693 -0.0365119  0.154141    -0.13614    34  LEU   A CD1  
202  C CD2  . LEU   A 22  ? 0.86634  0.688438 0.652535 -0.0530892  0.154424    -0.152582   34  LEU   A CD2  
203  H H    . LEU   A 22  ? 0.699677 0.624074 0.594856 -0.0394589  0.102629    -0.167391   34  LEU   A H    
204  H HA   . LEU   A 22  ? 0.688423 0.593095 0.538607 -0.0330134  0.105363    -0.165078   34  LEU   A HA   
205  H HB2  . LEU   A 22  ? 0.716227 0.57342  0.561878 -0.0156441  0.103422    -0.14063    34  LEU   A HB2  
206  H HB3  . LEU   A 22  ? 0.74963  0.588738 0.558772 -0.0107456  0.102502    -0.134234   34  LEU   A HB3  
207  H HG   . LEU   A 22  ? 0.793921 0.642427 0.629081 -0.0563207  0.146323    -0.163502   34  LEU   A HG   
208  H HD11 . LEU   A 22  ? 0.873367 0.648786 0.678087 -0.0294639  0.14743     -0.137542   34  LEU   A HD11 
209  H HD12 . LEU   A 22  ? 0.920207 0.665179 0.693903 -0.0537451  0.175485    -0.141161   34  LEU   A HD12 
210  H HD13 . LEU   A 22  ? 0.917156 0.662178 0.678063 -0.0215991  0.14782     -0.121314   34  LEU   A HD13 
211  H HD21 . LEU   A 22  ? 0.831014 0.689737 0.639958 -0.0616654  0.153981    -0.167038   34  LEU   A HD21 
212  H HD22 . LEU   A 22  ? 0.868719 0.683857 0.636924 -0.0386736  0.142593    -0.143133   34  LEU   A HD22 
213  H HD23 . LEU   A 22  ? 0.899456 0.690689 0.663802 -0.0654304  0.175611    -0.149961   34  LEU   A HD23 
214  N N    . LYS   A 23  ? 0.650858 0.575694 0.518815 -0.00556306 0.0570834   -0.157091   35  LYS   A N    
215  C CA   . LYS   A 23  ? 0.602553 0.539399 0.485454 0.00479839  0.029516    -0.155886   35  LYS   A CA   
216  C C    . LYS   A 23  ? 0.657871 0.576528 0.510896 0.0168341   0.0162835   -0.150017   35  LYS   A C    
217  O O    . LYS   A 23  ? 0.66456  0.566635 0.480663 0.0181036   0.0271854   -0.152389   35  LYS   A O    
218  C CB   . LYS   A 23  ? 0.588473 0.545277 0.48698  0.00318515  0.0252132   -0.172211   35  LYS   A CB   
219  C CG   . LYS   A 23  ? 0.5614   0.519969 0.474611 0.0112055   -0.00220805 -0.173748   35  LYS   A CG   
220  C CD   . LYS   A 23  ? 0.6014   0.566106 0.519081 0.0171642   -0.00567911 -0.192489   35  LYS   A CD   
221  C CE   . LYS   A 23  ? 0.626638 0.581593 0.559643 0.022606    -0.03137    -0.19392    35  LYS   A CE   
222  N NZ   . LYS   A 23  ? 0.687916 0.639044 0.622104 0.0334712   -0.0359866  -0.213888   35  LYS   A NZ   
223  H H    . LYS   A 23  ? 0.654539 0.572899 0.504722 -0.00924313 0.0684927   -0.161982   35  LYS   A H    
224  H HA   . LYS   A 23  ? 0.59512  0.540622 0.497953 0.00485714  0.0220747   -0.150002   35  LYS   A HA   
225  H HB2  . LYS   A 23  ? 0.567026 0.539397 0.483916 -0.00283635 0.0307525   -0.175487   35  LYS   A HB2  
226  H HB3  . LYS   A 23  ? 0.602763 0.55573  0.483362 0.00288095  0.0354647   -0.179828   35  LYS   A HB3  
227  H HG2  . LYS   A 23  ? 0.58883  0.536045 0.48772  0.0154247   -0.0107009  -0.169739   35  LYS   A HG2  
228  H HG3  . LYS   A 23  ? 0.555322 0.521776 0.489507 0.00844529  -0.0093592  -0.16718    35  LYS   A HG3  
229  H HD2  . LYS   A 23  ? 0.586206 0.56717  0.518816 0.0148979   0.00238058  -0.196998   35  LYS   A HD2  
230  H HD3  . LYS   A 23  ? 0.620772 0.579353 0.515788 0.0197451   0.00173007  -0.199989   35  LYS   A HD3  
231  H HE2  . LYS   A 23  ? 0.641648 0.586052 0.564265 0.0222039   -0.0406233  -0.190075   35  LYS   A HE2  
232  H HE3  . LYS   A 23  ? 0.614138 0.574674 0.567095 0.0190315   -0.0365496  -0.185233   35  LYS   A HE3  
233  H HZ1  . LYS   A 23  ? 0.688194 0.640802 0.604104 0.03604     -0.0257521  -0.223429   35  LYS   A HZ1  
234  H HZ2  . LYS   A 23  ? 0.664133 0.626652 0.615633 0.0360586   -0.033921   -0.215681   35  LYS   A HZ2  
235  H HZ3  . LYS   A 23  ? 0.686812 0.622741 0.622554 0.0355556   -0.0511044  -0.215845   35  LYS   A HZ3  
236  N N    . ILE   A 24  ? 0.671088 0.598029 0.540563 0.0237244   -0.00779887 -0.143664   36  ILE   A N    
237  C CA   . ILE   A 24  ? 0.710171 0.632244 0.559439 0.0329075   -0.0285208  -0.1452     36  ILE   A CA   
238  C C    . ILE   A 24  ? 0.661336 0.599213 0.542343 0.0284281   -0.0526161  -0.153936   36  ILE   A C    
239  O O    . ILE   A 24  ? 0.625513 0.578931 0.542949 0.0220141   -0.0578031  -0.147246   36  ILE   A O    
240  C CB   . ILE   A 24  ? 0.76681  0.684154 0.603459 0.0459074   -0.0373458  -0.128986   36  ILE   A CB   
241  C CG1  . ILE   A 24  ? 0.787502 0.676295 0.593257 0.050605    -0.0128792  -0.116777   36  ILE   A CG1  
242  C CG2  . ILE   A 24  ? 0.742965 0.661996 0.555008 0.0553096   -0.0629872  -0.132813   36  ILE   A CG2  
243  C CD1  . ILE   A 24  ? 0.907452 0.790078 0.708832 0.0695629   -0.0222311  -0.099203   36  ILE   A CD1  
244  H H    . ILE   A 24  ? 0.646529 0.585038 0.540392 0.0212218   -0.0110241  -0.139415   36  ILE   A H    
245  H HA   . ILE   A 24  ? 0.728927 0.640463 0.551022 0.0338976   -0.0218664  -0.151928   36  ILE   A HA   
246  H HB   . ILE   A 24  ? 0.72532  0.659157 0.593076 0.0450282   -0.0437547  -0.124825   36  ILE   A HB   
247  H HG12 . ILE   A 24  ? 0.837852 0.71006  0.609469 0.0503251   -0.00523761 -0.118567   36  ILE   A HG12 
248  H HG13 . ILE   A 24  ? 0.788636 0.678153 0.610052 0.0417083   0.00263141  -0.118969   36  ILE   A HG13 
249  H HG21 . ILE   A 24  ? 0.781658 0.697188 0.579488 0.066804    -0.0681801  -0.121546   36  ILE   A HG21 
250  H HG22 . ILE   A 24  ? 0.780016 0.686746 0.563362 0.0542499   -0.0574666  -0.140739   36  ILE   A HG22 
251  H HG23 . ILE   A 24  ? 0.743077 0.679589 0.581545 0.0507477   -0.079748   -0.139438   36  ILE   A HG23 
252  H HD11 . ILE   A 24  ? 0.849788 0.757563 0.686531 0.070659    -0.0337566  -0.099729   36  ILE   A HD11 
253  H HD12 . ILE   A 24  ? 0.892041 0.75251  0.682445 0.0710789   -0.00438888 -0.0920321  36  ILE   A HD12 
254  H HD13 . ILE   A 24  ? 0.907936 0.78405  0.681876 0.0797052   -0.0344388  -0.0950371  36  ILE   A HD13 
255  N N    . VAL   A 25  ? 0.665345 0.595487 0.528067 0.0307596   -0.0653299  -0.169099   37  VAL   A N    
256  C CA   . VAL   A 25  ? 0.623057 0.55577  0.508043 0.0253689   -0.0893689  -0.179841   37  VAL   A CA   
257  C C    . VAL   A 25  ? 0.647138 0.593127 0.534414 0.0265343   -0.112217   -0.174521   37  VAL   A C    
258  O O    . VAL   A 25  ? 0.650274 0.593648 0.500286 0.0375584   -0.116513   -0.173535   37  VAL   A O    
259  C CB   . VAL   A 25  ? 0.701664 0.618012 0.558264 0.0303159   -0.0900813  -0.202596   37  VAL   A CB   
260  C CG1  . VAL   A 25  ? 0.696398 0.603311 0.566516 0.0250559   -0.115845   -0.218703   37  VAL   A CG1  
261  C CG2  . VAL   A 25  ? 0.760919 0.676425 0.622506 0.0321714   -0.0675252  -0.20956    37  VAL   A CG2  
262  H H    . VAL   A 25  ? 0.683939 0.604493 0.516725 0.0350243   -0.0574345  -0.173625   37  VAL   A H    
263  H HA   . VAL   A 25  ? 0.619542 0.556281 0.532604 0.0187372   -0.0889045  -0.176781   37  VAL   A HA   
264  H HB   . VAL   A 25  ? 0.724323 0.637647 0.547825 0.0361487   -0.087973   -0.203369   37  VAL   A HB   
265  H HG11 . VAL   A 25  ? 0.684466 0.593076 0.585903 0.0172423   -0.120596   -0.211968   37  VAL   A HG11 
266  H HG12 . VAL   A 25  ? 0.722013 0.63332  0.580565 0.0247117   -0.130068   -0.220348   37  VAL   A HG12 
267  H HG13 . VAL   A 25  ? 0.722609 0.616898 0.581204 0.029466    -0.113361   -0.234941   37  VAL   A HG13 
268  H HG21 . VAL   A 25  ? 0.75649  0.664556 0.608498 0.0367147   -0.069316   -0.226234   37  VAL   A HG21 
269  H HG22 . VAL   A 25  ? 0.736024 0.654874 0.581723 0.0330953   -0.0504052  -0.203921   37  VAL   A HG22 
270  H HG23 . VAL   A 25  ? 0.712411 0.632716 0.602803 0.0279691   -0.0683345  -0.203749   37  VAL   A HG23 
271  N N    . LYS   A 26  ? 0.644695 0.608439 0.575348 0.0150763   -0.12585    -0.169608   38  LYS   A N    
272  C CA   . LYS   A 26  ? 0.692046 0.683177 0.638636 0.0145581   -0.147529   -0.166104   38  LYS   A CA   
273  C C    . LYS   A 26  ? 0.707674 0.697733 0.663879 0.00078565  -0.174015   -0.185462   38  LYS   A C    
274  O O    . LYS   A 26  ? 0.843991 0.848197 0.785518 0.00504425  -0.195778   -0.194488   38  LYS   A O    
275  C CB   . LYS   A 26  ? 0.701748 0.721992 0.692788 0.0091886   -0.13985    -0.148956   38  LYS   A CB   
276  C CG   . LYS   A 26  ? 0.687443 0.705817 0.666005 0.024177    -0.116496   -0.134307   38  LYS   A CG   
277  C CD   . LYS   A 26  ? 0.728466 0.736529 0.665723 0.0461857   -0.117699   -0.129094   38  LYS   A CD   
278  C CE   . LYS   A 26  ? 0.747494 0.788469 0.698506 0.0549225   -0.145698   -0.128427   38  LYS   A CE   
279  N NZ   . LYS   A 26  ? 0.800383 0.824945 0.707333 0.0805429   -0.144161   -0.11655    38  LYS   A NZ   
280  H H    . LYS   A 26  ? 0.632331 0.593714 0.583682 0.00713267  -0.121242   -0.168087   38  LYS   A H    
281  H HA   . LYS   A 26  ? 0.708609 0.70046  0.628191 0.0276054   -0.149096   -0.163365   38  LYS   A HA   
282  H HB2  . LYS   A 26  ? 0.676669 0.692826 0.68724  -0.0034512  -0.135151   -0.148576   38  LYS   A HB2  
283  H HB3  . LYS   A 26  ? 0.696022 0.741592 0.706372 0.00736803  -0.155043   -0.148902   38  LYS   A HB3  
284  H HG2  . LYS   A 26  ? 0.679849 0.680605 0.649084 0.0211663   -0.101151   -0.135123   38  LYS   A HG2  
285  H HG3  . LYS   A 26  ? 0.671548 0.711793 0.678989 0.0219005   -0.113491   -0.126672   38  LYS   A HG3  
286  H HD2  . LYS   A 26  ? 0.745242 0.731889 0.649766 0.0475227   -0.116339   -0.135958   38  LYS   A HD2  
287  H HD3  . LYS   A 26  ? 0.721561 0.722989 0.654876 0.0535109   -0.101272   -0.119469   38  LYS   A HD3  
288  H HE2  . LYS   A 26  ? 0.731355 0.800019 0.720549 0.0519995   -0.146887   -0.124      38  LYS   A HE2  
289  H HE3  . LYS   A 26  ? 0.763844 0.80812  0.711864 0.047468    -0.162789   -0.14019    38  LYS   A HE3  
290  H HZ1  . LYS   A 26  ? 0.787483 0.806848 0.69965  0.0875686   -0.129249   -0.106597   38  LYS   A HZ1  
291  H HZ2  . LYS   A 26  ? 0.814682 0.813082 0.684393 0.0811815   -0.138548   -0.119402   38  LYS   A HZ2  
292  H HZ3  . LYS   A 26  ? 0.812606 0.857817 0.722712 0.0893231   -0.163847   -0.116135   38  LYS   A HZ3  
293  N N    . ARG   A 27  ? 0.722221 0.689907 0.696619 -0.0140122  -0.172317   -0.192797   39  ARG   A N    
294  C CA   . ARG   A 27  ? 0.761828 0.709363 0.738526 -0.0274988  -0.193216   -0.21493    39  ARG   A CA   
295  C C    . ARG   A 27  ? 0.841047 0.745196 0.798466 -0.0210173  -0.181923   -0.227235   39  ARG   A C    
296  O O    . ARG   A 27  ? 0.805552 0.700512 0.776386 -0.0192854  -0.164839   -0.214153   39  ARG   A O    
297  C CB   . ARG   A 27  ? 0.7578   0.718728 0.784294 -0.0545786  -0.2065     -0.21103    39  ARG   A CB   
298  C CG   . ARG   A 27  ? 0.792318 0.73217  0.823203 -0.0739597  -0.231275   -0.236698   39  ARG   A CG   
299  C CD   . ARG   A 27  ? 0.771233 0.710012 0.850434 -0.106736   -0.23642    -0.230052   39  ARG   A CD   
300  N NE   . ARG   A 27  ? 0.825986 0.725207 0.906645 -0.106102   -0.216103   -0.212903   39  ARG   A NE   
301  C CZ   . ARG   A 27  ? 0.787183 0.685915 0.900894 -0.128714   -0.208195   -0.19231    39  ARG   A CZ   
302  N NH1  . ARG   A 27  ? 0.788753 0.730693 0.94147  -0.153973   -0.21482    -0.187953   39  ARG   A NH1  
303  N NH2  . ARG   A 27  ? 0.792164 0.652534 0.900056 -0.126245   -0.194143   -0.176029   39  ARG   A NH2  
304  H H    . ARG   A 27  ? 0.697458 0.659918 0.682281 -0.0153289  -0.158035   -0.18354    39  ARG   A H    
305  H HA   . ARG   A 27  ? 0.797263 0.751248 0.752711 -0.0224129  -0.206276   -0.226509   39  ARG   A HA   
306  H HB2  . ARG   A 27  ? 0.740441 0.73761  0.783989 -0.0553394  -0.209777   -0.202183   39  ARG   A HB2  
307  H HB3  . ARG   A 27  ? 0.740026 0.689215 0.781255 -0.0601694  -0.194206   -0.199494   39  ARG   A HB3  
308  H HG2  . ARG   A 27  ? 0.810594 0.71389  0.818561 -0.0674619  -0.229038   -0.249287   39  ARG   A HG2  
309  H HG3  . ARG   A 27  ? 0.803904 0.765824 0.826092 -0.0718474  -0.246584   -0.247277   39  ARG   A HG3  
310  H HD2  . ARG   A 27  ? 0.828676 0.750728 0.91016  -0.121302   -0.252389   -0.248461   39  ARG   A HD2  
311  H HD3  . ARG   A 27  ? 0.770095 0.750582 0.87585  -0.113468   -0.236424   -0.218617   39  ARG   A HD3  
312  H HE   . ARG   A 27  ? 0.80245  0.679256 0.86034  -0.0901231  -0.209115   -0.216023   39  ARG   A HE   
313  H HH11 . ARG   A 27  ? 0.812278 0.757123 0.974667 -0.167914   -0.230238   -0.202881   39  ARG   A HH11 
314  H HH12 . ARG   A 27  ? 0.763501 0.733848 0.934106 -0.15755    -0.203613   -0.171548   39  ARG   A HH12 
315  H HH21 . ARG   A 27  ? 0.77493  0.630721 0.86535  -0.107045   -0.18473    -0.172505   39  ARG   A HH21 
316  H HH22 . ARG   A 27  ? 0.813338 0.653297 0.934365 -0.144043   -0.194634   -0.168275   39  ARG   A HH22 
317  N N    . VAL   A 28  ? 0.874565 0.756728 0.80029  -0.015637   -0.193023   -0.254555   40  VAL   A N    
318  C CA   . VAL   A 28  ? 0.933659 0.781769 0.837736 -0.00250994 -0.181873   -0.272532   40  VAL   A CA   
319  C C    . VAL   A 28  ? 0.917808 0.728732 0.852343 -0.0135664  -0.189342   -0.27654    40  VAL   A C    
320  O O    . VAL   A 28  ? 0.930619 0.730877 0.882038 -0.033909   -0.209367   -0.2834     40  VAL   A O    
321  C CB   . VAL   A 28  ? 1.01863  0.857583 0.875817 0.00682953  -0.190251   -0.302945   40  VAL   A CB   
322  C CG1  . VAL   A 28  ? 1.07713  0.888034 0.915065 0.0233087   -0.175476   -0.325695   40  VAL   A CG1  
323  C CG2  . VAL   A 28  ? 1.05308  0.922577 0.872369 0.0169442   -0.185071   -0.292928   40  VAL   A CG2  
324  H H    . VAL   A 28  ? 0.906878 0.798753 0.825235 -0.0197481  -0.208698   -0.263921   40  VAL   A H    
325  H HA   . VAL   A 28  ? 0.901858 0.757469 0.801749 0.00742623  -0.163677   -0.262186   40  VAL   A HA   
326  H HB   . VAL   A 28  ? 1.05165  0.883112 0.914426 -0.00477121 -0.209926   -0.315776   40  VAL   A HB   
327  H HG11 . VAL   A 28  ? 1.03848  0.858775 0.881631 0.0314271   -0.157045   -0.313414   40  VAL   A HG11 
328  H HG12 . VAL   A 28  ? 1.0853   0.869179 0.940587 0.019374    -0.183639   -0.33591    40  VAL   A HG12 
329  H HG13 . VAL   A 28  ? 1.09818  0.909667 0.901233 0.0300385   -0.175998   -0.343143   40  VAL   A HG13 
330  H HG21 . VAL   A 28  ? 1.07774  0.940488 0.860867 0.0239003   -0.186763   -0.310903   40  VAL   A HG21 
331  H HG22 . VAL   A 28  ? 1.03558  0.923863 0.865874 0.00987938  -0.199286   -0.284065   40  VAL   A HG22 
332  H HG23 . VAL   A 28  ? 1.01419  0.890657 0.833235 0.0237259   -0.1657     -0.277518   40  VAL   A HG23 
333  N N    . GLY   A 29  ? 1.01068  0.803795 0.952965 -0.00103294 -0.173975   -0.270485   41  GLY   A N    
334  C CA   . GLY   A 29  ? 1.04645  0.792683 1.00851  -0.00469683 -0.18182    -0.272709   41  GLY   A CA   
335  C C    . GLY   A 29  ? 1.18492  0.886548 1.12704  0.00463333  -0.192547   -0.30992    41  GLY   A C    
336  O O    . GLY   A 29  ? 1.22773  0.935224 1.14464  0.00168883  -0.201864   -0.334301   41  GLY   A O    
337  H H    . GLY   A 29  ? 0.960266 0.770133 0.895094 0.0102381   -0.159123   -0.264512   41  GLY   A H    
338  H HA2  . GLY   A 29  ? 1.06041  0.802578 1.04153  -0.0239473  -0.190587   -0.261117   41  GLY   A HA2  
339  H HA3  . GLY   A 29  ? 1.04203  0.788446 1.01135  0.00604127  -0.171012   -0.261323   41  GLY   A HA3  
340  N N    . ASN   A 30  ? 1.23649  0.891193 1.18823  0.0174772   -0.192711   -0.314662   42  ASN   A N    
341  C CA   . ASN   A 30  ? 1.28963  0.903049 1.2229   0.0377488   -0.195952   -0.352286   42  ASN   A CA   
342  C C    . ASN   A 30  ? 1.23185  0.817226 1.18056  0.0655945   -0.188891   -0.347308   42  ASN   A C    
343  O O    . ASN   A 30  ? 1.24021  0.839963 1.2091   0.0675245   -0.183355   -0.314884   42  ASN   A O    
344  C CB   . ASN   A 30  ? 1.37492  0.935349 1.30431  0.0171033   -0.218169   -0.376198   42  ASN   A CB   
345  C CG   . ASN   A 30  ? 1.42314  0.959143 1.38353  -0.0136849  -0.228817   -0.3468     42  ASN   A CG   
346  O OD1  . ASN   A 30  ? 1.50088  1.04146  1.4677   -0.045544   -0.243416   -0.35173    42  ASN   A OD1  
347  N ND2  . ASN   A 30  ? 1.40155  0.92165  1.3806   -0.00596977 -0.221105   -0.315334   42  ASN   A ND2  
348  H H    . ASN   A 30  ? 1.21751  0.865642 1.18678  0.0154001   -0.190633   -0.293654   42  ASN   A H    
349  H HA   . ASN   A 30  ? 1.27359  0.913535 1.18548  0.0481859   -0.187777   -0.367684   42  ASN   A HA   
350  H HB2  . ASN   A 30  ? 1.42601  0.946427 1.34835  0.0321907   -0.21979    -0.398052   42  ASN   A HB2  
351  H HB3  . ASN   A 30  ? 1.38278  0.96535  1.29569  0.00786767  -0.223598   -0.390035   42  ASN   A HB3  
352  H HD21 . ASN   A 30  ? 1.36443  0.91296  1.35528  -0.0154354  -0.216004   -0.290206   42  ASN   A HD21 
353  H HD22 . ASN   A 30  ? 1.43697  0.918031 1.41534  0.00969653  -0.221691   -0.319823   42  ASN   A HD22 
354  N N    . GLY   A 31  ? 1.29409  0.843481 1.23161  0.0907708   -0.189484   -0.382168   43  GLY   A N    
355  C CA   . GLY   A 31  ? 1.29665  0.836353 1.24865  0.12789     -0.18151    -0.385003   43  GLY   A CA   
356  C C    . GLY   A 31  ? 1.34701  0.957711 1.29238  0.148476    -0.158003   -0.397497   43  GLY   A C    
357  O O    . GLY   A 31  ? 1.28912  0.953207 1.22392  0.131601    -0.146732   -0.384769   43  GLY   A O    
358  H H    . GLY   A 31  ? 1.32665  0.859882 1.24724  0.0861853   -0.195435   -0.407016   43  GLY   A H    
359  H HA2  . GLY   A 31  ? 1.37824  0.870547 1.32644  0.140649    -0.188426   -0.407594   43  GLY   A HA2  
360  H HA3  . GLY   A 31  ? 1.30401  0.838918 1.27376  0.126688    -0.184298   -0.356837   43  GLY   A HA3  
361  N N    . GLU   A 32  ? 1.52512  1.1349   1.47798  0.185304    -0.149457   -0.423248   44  GLU   A N    
362  C CA   . GLU   A 32  ? 1.41319  1.09579  1.37193  0.204032    -0.124484   -0.431857   44  GLU   A CA   
363  C C    . GLU   A 32  ? 1.25741  0.982513 1.24746  0.203801    -0.121125   -0.394345   44  GLU   A C    
364  O O    . GLU   A 32  ? 1.16994  0.960716 1.16224  0.198868    -0.100817   -0.390321   44  GLU   A O    
365  C CB   . GLU   A 32  ? 1.43382  1.10926  1.39908  0.244618    -0.116561   -0.473405   44  GLU   A CB   
366  H H    . GLU   A 32  ? 1.51817  1.08128  1.47445  0.198803    -0.158767   -0.436526   44  GLU   A H    
367  H HA   . GLU   A 32  ? 1.38254  1.09272  1.3188   0.188977    -0.114361   -0.436593   44  GLU   A HA   
370  N N    . GLU   A 33  ? 1.14013  0.82476  1.14903  0.205603    -0.14053    -0.366746   45  GLU   A N    
371  C CA   . GLU   A 33  ? 1.0825   0.802053 1.11928  0.217681    -0.141153   -0.339395   45  GLU   A CA   
372  C C    . GLU   A 33  ? 0.991616 0.744419 1.0249   0.182982    -0.137235   -0.304253   45  GLU   A C    
373  O O    . GLU   A 33  ? 0.973034 0.692078 0.993975 0.154769    -0.146658   -0.285181   45  GLU   A O    
374  C CB   . GLU   A 33  ? 1.14838  0.805967 1.1985   0.240064    -0.163624   -0.323813   45  GLU   A CB   
375  C CG   . GLU   A 33  ? 1.28093  0.892586 1.33494  0.278491    -0.168833   -0.360047   45  GLU   A CG   
376  C CD   . GLU   A 33  ? 1.39825  0.916629 1.45189  0.290193    -0.193104   -0.340797   45  GLU   A CD   
377  O OE1  . GLU   A 33  ? 1.34564  0.862736 1.40095  0.274959    -0.201981   -0.297383   45  GLU   A OE1  
378  O OE2  . GLU   A 33  ? 1.50466  0.94981  1.55213  0.310309    -0.201669   -0.366725   45  GLU   A OE2  
379  H H    . GLU   A 33  ? 1.20129  0.834497 1.2031   0.197863    -0.153929   -0.365052   45  GLU   A H    
380  H HA   . GLU   A 33  ? 1.06982  0.83489  1.11883  0.235467    -0.128723   -0.354767   45  GLU   A HA   
381  H HB2  . GLU   A 33  ? 1.17207  0.788006 1.21136  0.218287    -0.173537   -0.305458   45  GLU   A HB2  
382  H HB3  . GLU   A 33  ? 1.13837  0.826555 1.20451  0.250994    -0.164948   -0.307233   45  GLU   A HB3  
383  H HG2  . GLU   A 33  ? 1.26804  0.922323 1.34086  0.305338    -0.161555   -0.372826   45  GLU   A HG2  
384  H HG3  . GLU   A 33  ? 1.29063  0.889511 1.32775  0.269368    -0.163293   -0.384032   45  GLU   A HG3  
385  N N    . THR   A 34  ? 0.898628 0.720655 0.946312 0.185626    -0.122344   -0.298925   46  THR   A N    
386  C CA   . THR   A 34  ? 0.868286 0.719469 0.918929 0.162512    -0.120669   -0.265998   46  THR   A CA   
387  C C    . THR   A 34  ? 0.883633 0.739036 0.954516 0.181758    -0.135062   -0.245548   46  THR   A C    
388  O O    . THR   A 34  ? 1.02634  0.883617 1.11551  0.216592    -0.142412   -0.259183   46  THR   A O    
389  C CB   . THR   A 34  ? 0.778582 0.695001 0.827662 0.149123    -0.0959751  -0.273782   46  THR   A CB   
390  O OG1  . THR   A 34  ? 0.784987 0.746674 0.855278 0.173568    -0.0849623  -0.298258   46  THR   A OG1  
391  C CG2  . THR   A 34  ? 0.803827 0.712242 0.824208 0.132707    -0.0837344  -0.288123   46  THR   A CG2  
392  H H    . THR   A 34  ? 0.911487 0.764616 0.967817 0.20121     -0.111966   -0.318235   46  THR   A H    
393  H HA   . THR   A 34  ? 0.860729 0.683793 0.898978 0.142725    -0.126403   -0.252395   46  THR   A HA   
394  H HB   . THR   A 34  ? 0.761483 0.696821 0.813279 0.135526    -0.0942215  -0.255023   46  THR   A HB   
396  H HG21 . THR   A 34  ? 0.768969 0.711429 0.785243 0.122642    -0.0678107  -0.287766   46  THR   A HG21 
397  H HG22 . THR   A 34  ? 0.825218 0.723648 0.841209 0.146656    -0.0824061  -0.310211   46  THR   A HG22 
398  H HG23 . THR   A 34  ? 0.800026 0.679571 0.809298 0.118389    -0.0931704  -0.275964   46  THR   A HG23 
399  N N    . PRO   A 35  ? 0.91246  0.769791 0.978826 0.162564    -0.140752   -0.211993   47  PRO   A N    
400  C CA   . PRO   A 35  ? 0.943283 0.808152 1.01975  0.180716    -0.155702   -0.190286   47  PRO   A CA   
401  C C    . PRO   A 35  ? 0.977269 0.917068 1.0802   0.20385     -0.150448   -0.207834   47  PRO   A C    
402  O O    . PRO   A 35  ? 0.811542 0.808098 0.92105  0.188395    -0.12946    -0.224331   47  PRO   A O    
403  C CB   . PRO   A 35  ? 0.959757 0.831343 1.02109  0.148854    -0.15371    -0.158068   47  PRO   A CB   
404  C CG   . PRO   A 35  ? 0.887611 0.742291 0.935751 0.116618    -0.141807   -0.160345   47  PRO   A CG   
405  C CD   . PRO   A 35  ? 0.905103 0.7623   0.955274 0.125297    -0.132799   -0.194854   47  PRO   A CD   
406  H HA   . PRO   A 35  ? 1.00657  0.824249 1.08101  0.196079    -0.169914   -0.184832   47  PRO   A HA   
407  H HB2  . PRO   A 35  ? 0.907135 0.827616 0.974509 0.146677    -0.147032   -0.158389   47  PRO   A HB2  
408  H HB3  . PRO   A 35  ? 0.970996 0.810131 1.02473  0.151819    -0.16669    -0.136436   47  PRO   A HB3  
409  H HG2  . PRO   A 35  ? 0.86694  0.753354 0.912472 0.100122    -0.131502   -0.153854   47  PRO   A HG2  
410  H HG3  . PRO   A 35  ? 0.930465 0.742039 0.970707 0.107235    -0.150269   -0.146665   47  PRO   A HG3  
411  H HD2  . PRO   A 35  ? 0.858559 0.753755 0.908348 0.116968    -0.118287   -0.203255   47  PRO   A HD2  
412  H HD3  . PRO   A 35  ? 0.911091 0.732272 0.952033 0.11611     -0.136618   -0.197717   47  PRO   A HD3  
413  N N    . MET   A 36  ? 1.06096  0.998905 1.17947  0.240471    -0.170166   -0.203484   48  MET   A N    
414  C CA   . MET   A 36  ? 1.06026  1.07784  1.21044  0.264573    -0.172397   -0.216139   48  MET   A CA   
415  C C    . MET   A 36  ? 1.00749  1.06131  1.14919  0.248764    -0.180228   -0.1884     48  MET   A C    
416  O O    . MET   A 36  ? 1.00549  1.01014  1.11659  0.23226     -0.189025   -0.155183   48  MET   A O    
417  C CB   . MET   A 36  ? 1.13277  1.1331   1.30338  0.317048    -0.195576   -0.220718   48  MET   A CB   
418  C CG   . MET   A 36  ? 1.16739  1.12017  1.34409  0.340868    -0.191703   -0.249688   48  MET   A CG   
419  S SD   . MET   A 36  ? 1.11594  1.16103  1.32936  0.3484      -0.162412   -0.301288   48  MET   A SD   
420  C CE   . MET   A 36  ? 1.02939  1.07074  1.21327  0.299187    -0.129145   -0.316429   48  MET   A CE   
421  H H    . MET   A 36  ? 1.09588  0.980372 1.20563  0.251253    -0.183782   -0.192051   48  MET   A H    
422  H HA   . MET   A 36  ? 1.02016  1.08121  1.18386  0.257904    -0.154451   -0.240034   48  MET   A HA   
423  H HB2  . MET   A 36  ? 1.16285  1.12107  1.3167   0.322263    -0.213121   -0.193145   48  MET   A HB2  
424  H HB3  . MET   A 36  ? 1.11426  1.17837  1.31094  0.33278     -0.197249   -0.231637   48  MET   A HB3  
425  H HG2  . MET   A 36  ? 1.17271  1.07423  1.32583  0.319344    -0.186801   -0.245594   48  MET   A HG2  
426  H HG3  . MET   A 36  ? 1.2176   1.13978  1.40056  0.373485    -0.209433   -0.245205   48  MET   A HG3  
427  H HE1  . MET   A 36  ? 1.02575  1.11446  1.22522  0.302667    -0.111632   -0.341777   48  MET   A HE1  
428  H HE2  . MET   A 36  ? 1.00552  1.05719  1.17721  0.271159    -0.125517   -0.29832    48  MET   A HE2  
429  H HE3  . MET   A 36  ? 1.06838  1.05006  1.23179  0.297665    -0.132546   -0.317465   48  MET   A HE3  
430  N N    . ILE   A 37  ? 0.94655  1.08846  1.11549  0.253049    -0.17685    -0.203892   49  ILE   A N    
431  C CA   . ILE   A 37  ? 0.858393 1.04107  1.01836  0.240992    -0.186992   -0.183677   49  ILE   A CA   
432  C C    . ILE   A 37  ? 0.895482 1.03713  1.03812  0.27145     -0.220087   -0.150269   49  ILE   A C    
433  O O    . ILE   A 37  ? 0.932204 1.06893  1.09584  0.315565    -0.238813   -0.156114   49  ILE   A O    
434  C CB   . ILE   A 37  ? 0.827955 1.11539  1.02659  0.242399    -0.181268   -0.212291   49  ILE   A CB   
435  C CG1  . ILE   A 37  ? 0.829849 1.15383  1.04134  0.208051    -0.144737   -0.242723   49  ILE   A CG1  
436  C CG2  . ILE   A 37  ? 0.796864 1.12914  0.985437 0.236503    -0.198948   -0.195221   49  ILE   A CG2  
437  C CD1  . ILE   A 37  ? 0.80604  1.06409  0.986904 0.181301    -0.122533   -0.238772   49  ILE   A CD1  
438  H H    . ILE   A 37  ? 0.924439 1.10334  1.11787  0.262791    -0.167943   -0.228919   49  ILE   A H    
439  H HA   . ILE   A 37  ? 0.84623  1.01315  0.984273 0.211192    -0.175817   -0.173152   49  ILE   A HA   
440  H HB   . ILE   A 37  ? 0.850301 1.15672  1.07505  0.273499    -0.191174   -0.224717   49  ILE   A HB   
441  H HG12 . ILE   A 37  ? 0.814706 1.17508  1.05631  0.223683    -0.140005   -0.265875   49  ILE   A HG12 
442  H HG13 . ILE   A 37  ? 0.792049 1.15545  1.0043   0.187901    -0.139734   -0.244636   49  ILE   A HG13 
443  H HG21 . ILE   A 37  ? 0.779983 1.17679  0.99129  0.226492    -0.191072   -0.216156   49  ILE   A HG21 
444  H HG22 . ILE   A 37  ? 0.801483 1.10168  0.958753 0.21317     -0.194092   -0.176804   49  ILE   A HG22 
445  H HG23 . ILE   A 37  ? 0.843934 1.17296  1.03361  0.266033    -0.222911   -0.182547   49  ILE   A HG23 
446  H HD11 . ILE   A 37  ? 0.811652 1.0328   0.966648 0.168848    -0.127815   -0.216185   49  ILE   A HD11 
447  H HD12 . ILE   A 37  ? 0.781582 1.06642  0.966365 0.159975    -0.101719   -0.253369   49  ILE   A HD12 
448  H HD13 . ILE   A 37  ? 0.828718 1.05621  1.01162  0.197836    -0.123788   -0.244993   49  ILE   A HD13 
449  N N    . GLY   A 38  ? 0.850742 0.959559 0.953224 0.249548    -0.225788   -0.114839   50  GLY   A N    
450  C CA   . GLY   A 38  ? 0.935022 0.999939 1.01022  0.273987    -0.254933   -0.0768481  50  GLY   A CA   
451  C C    . GLY   A 38  ? 1.01521  0.969514 1.06019  0.270116    -0.25781    -0.0489862  50  GLY   A C    
452  O O    . GLY   A 38  ? 1.03303  0.936212 1.04682  0.284114    -0.278431   -0.0113461  50  GLY   A O    
453  H H    . GLY   A 38  ? 0.836654 0.949608 0.926979 0.219399    -0.210384   -0.113665   50  GLY   A H    
454  H HA2  . GLY   A 38  ? 0.932947 1.02113  0.9883   0.259572    -0.257516   -0.0616328  50  GLY   A HA2  
455  H HA3  . GLY   A 38  ? 0.96164  1.04874  1.05672  0.308447    -0.271638   -0.0837327  50  GLY   A HA3  
456  N N    . ASP   A 39  ? 0.981981 0.89826  1.03413  0.250312    -0.238068   -0.0671077  51  ASP   A N    
457  C CA   . ASP   A 39  ? 1.02694  0.846471 1.05382  0.234929    -0.238179   -0.0455687  51  ASP   A CA   
458  C C    . ASP   A 39  ? 1.04379  0.851741 1.03556  0.195179    -0.230835   -0.01034    51  ASP   A C    
459  O O    . ASP   A 39  ? 0.991276 0.862339 0.982276 0.170853    -0.215792   -0.015711   51  ASP   A O    
460  C CB   . ASP   A 39  ? 1.03964  0.837462 1.08236  0.221571    -0.220917   -0.0777369  51  ASP   A CB   
461  C CG   . ASP   A 39  ? 1.06323  0.850266 1.13213  0.261356    -0.226972   -0.110444   51  ASP   A CG   
462  O OD1  . ASP   A 39  ? 1.12598  0.911042 1.20409  0.303084    -0.247053   -0.105227   51  ASP   A OD1  
463  O OD2  . ASP   A 39  ? 1.06861  0.850952 1.14706  0.252769    -0.211947   -0.141511   51  ASP   A OD2  
464  H H    . ASP   A 39  ? 0.942025 0.89462  1.01462  0.245174    -0.224554   -0.093813   51  ASP   A H    
465  H HA   . ASP   A 39  ? 1.09745  0.872885 1.11889  0.260957    -0.255322   -0.0331222  51  ASP   A HA   
466  H HB2  . ASP   A 39  ? 0.973713 0.818782 1.02377  0.202681    -0.205099   -0.0920964  51  ASP   A HB2  
467  H HB3  . ASP   A 39  ? 1.05374  0.797115 1.0805   0.202954    -0.219845   -0.064141   51  ASP   A HB3  
468  N N    . LYS   A 40  ? 1.10643  0.832609 1.0685   0.18794     -0.239582   0.0252394   52  LYS   A N    
469  C CA   . LYS   A 40  ? 1.12806  0.838931 1.06163  0.143847    -0.225686   0.0544565   52  LYS   A CA   
470  C C    . LYS   A 40  ? 1.12633  0.823407 1.07728  0.109923    -0.205803   0.0337491   52  LYS   A C    
471  O O    . LYS   A 40  ? 1.17772  0.815717 1.13846  0.11355     -0.210312   0.0219085   52  LYS   A O    
472  C CB   . LYS   A 40  ? 1.15491  0.787964 1.04767  0.139066    -0.236937   0.103263    52  LYS   A CB   
473  H H    . LYS   A 40  ? 1.16587  0.844641 1.12605  0.210336    -0.253141   0.0310631   52  LYS   A H    
474  H HA   . LYS   A 40  ? 1.08098  0.848291 1.01023  0.135874    -0.219419   0.0545077   52  LYS   A HA   
477  N N    . VAL   A 41  ? 1.09863  0.851204 1.05284  0.0790237   -0.185215   0.0273622   53  VAL   A N    
478  C CA   . VAL   A 41  ? 1.00676  0.765722 0.980474 0.0536072   -0.168793   0.00425315  53  VAL   A CA   
479  C C    . VAL   A 41  ? 0.993568 0.747161 0.95759  0.0132477   -0.154766   0.0265961   53  VAL   A C    
480  O O    . VAL   A 41  ? 1.12748  0.914306 1.07448  0.00068673  -0.145675   0.0462145   53  VAL   A O    
481  C CB   . VAL   A 41  ? 0.90888  0.739449 0.900919 0.057775    -0.155607   -0.0279337  53  VAL   A CB   
482  C CG1  . VAL   A 41  ? 0.967912 0.800885 0.973704 0.0375473   -0.142169   -0.0485125  53  VAL   A CG1  
483  C CG2  . VAL   A 41  ? 0.879032 0.727996 0.886088 0.0942357   -0.165615   -0.0513771  53  VAL   A CG2  
484  H H    . VAL   A 41  ? 1.0663   0.853474 1.00896  0.0752668   -0.182232   0.0375378   53  VAL   A H    
485  H HA   . VAL   A 41  ? 1.03207  0.751547 1.01343  0.0601381   -0.175273   -0.00597504 53  VAL   A HA   
486  H HB   . VAL   A 41  ? 0.904281 0.770485 0.888358 0.0495032   -0.14873    -0.0197783  53  VAL   A HB   
487  H HG11 . VAL   A 41  ? 0.962531 0.753755 0.970606 0.0369933   -0.149178   -0.0508121  53  VAL   A HG11 
488  H HG12 . VAL   A 41  ? 0.918323 0.765449 0.920886 0.0167057   -0.132427   -0.0386663  53  VAL   A HG12 
489  H HG13 . VAL   A 41  ? 0.900888 0.763476 0.915719 0.0460966   -0.136376   -0.0697075  53  VAL   A HG13 
490  H HG21 . VAL   A 41  ? 0.845942 0.735258 0.864346 0.0921842   -0.15461    -0.0718588  53  VAL   A HG21 
491  H HG22 . VAL   A 41  ? 0.906764 0.767305 0.9072   0.108426    -0.175242   -0.0394942  53  VAL   A HG22 
492  H HG23 . VAL   A 41  ? 0.916497 0.726587 0.928617 0.105615    -0.173102   -0.0586191  53  VAL   A HG23 
493  N N    . TYR   A 42  ? 1.01322  0.732522 0.990832 -0.00734203 -0.152234   0.0187414   54  TYR   A N    
494  C CA   . TYR   A 42  ? 1.05496  0.769235 1.03352  -0.0467755  -0.140225   0.0370005   54  TYR   A CA   
495  C C    . TYR   A 42  ? 0.923627 0.682138 0.928656 -0.0615875  -0.128823   0.00978497  54  TYR   A C    
496  O O    . TYR   A 42  ? 0.862952 0.601734 0.881492 -0.056967   -0.136885   -0.0146863  54  TYR   A O    
497  C CB   . TYR   A 42  ? 1.1826   0.81356  1.15669  -0.0607372  -0.151027   0.0521806   54  TYR   A CB   
498  C CG   . TYR   A 42  ? 1.29284  0.863415 1.23469  -0.0471883  -0.162894   0.0869601   54  TYR   A CG   
499  C CD1  . TYR   A 42  ? 1.3484   0.898065 1.28124  -0.0028013  -0.181089   0.0817346   54  TYR   A CD1  
500  C CD2  . TYR   A 42  ? 1.46154  0.994268 1.38191  -0.078377   -0.155836   0.126152    54  TYR   A CD2  
501  C CE1  . TYR   A 42  ? 1.51045  1.00366  1.41168  0.0152836   -0.195355   0.116298    54  TYR   A CE1  
502  C CE2  . TYR   A 42  ? 1.50195  0.970738 1.38448  -0.0650038  -0.167344   0.163187    54  TYR   A CE2  
503  C CZ   . TYR   A 42  ? 1.59586  1.04315  1.46782  -0.015462   -0.18917    0.158998    54  TYR   A CZ   
504  O OH   . TYR   A 42  ? 1.78452  1.16835  1.61711  0.004243    -0.204138   0.197826    54  TYR   A OH   
505  H H    . TYR   A 42  ? 1.01897  0.721248 1.00705  0.00314328  -0.158173   -0.00057363 54  TYR   A H    
506  H HA   . TYR   A 42  ? 1.04321  0.779161 1.00771  -0.0542839  -0.132538   0.0563137   54  TYR   A HA   
507  H HB2  . TYR   A 42  ? 1.17919  0.788648 1.16481  -0.0510373  -0.159278   0.0299885   54  TYR   A HB2  
508  H HB3  . TYR   A 42  ? 1.17996  0.814768 1.16174  -0.0905487  -0.141803   0.0595377   54  TYR   A HB3  
509  H HD1  . TYR   A 42  ? 1.31827  0.89639  1.26644  0.0165526   -0.183501   0.0551798   54  TYR   A HD1  
510  H HD2  . TYR   A 42  ? 1.40908  0.961378 1.34006  -0.108958   -0.142397   0.12857     54  TYR   A HD2  
511  H HE1  . TYR   A 42  ? 1.51013  0.995616 1.40926  0.0488489   -0.20904    0.111521    54  TYR   A HE1  
512  H HE2  . TYR   A 42  ? 1.57622  1.01856  1.44012  -0.0884885  -0.160193   0.191833    54  TYR   A HE2  
514  N N    . VAL   A 43  ? 0.863133 0.679389 0.872295 -0.0763842  -0.111013   0.0136075   55  VAL   A N    
515  C CA   . VAL   A 43  ? 0.793699 0.649595 0.8266   -0.086242   -0.101876   -0.00787016 55  VAL   A CA   
516  C C    . VAL   A 43  ? 0.795576 0.680268 0.842481 -0.117496   -0.0871076  0.00701008  55  VAL   A C    
517  O O    . VAL   A 43  ? 0.85633  0.735363 0.889329 -0.132422   -0.0794843  0.0338228   55  VAL   A O    
518  C CB   . VAL   A 43  ? 0.764562 0.668135 0.794977 -0.0667996  -0.0923187  -0.0260241  55  VAL   A CB   
519  C CG1  . VAL   A 43  ? 0.732883 0.622474 0.754892 -0.0379762  -0.102852   -0.0423033  55  VAL   A CG1  
520  C CG2  . VAL   A 43  ? 0.808794 0.750451 0.826751 -0.072738   -0.0766413  -0.0108127  55  VAL   A CG2  
521  H H    . VAL   A 43  ? 0.869805 0.699739 0.865259 -0.0787088  -0.105036   0.0297373   55  VAL   A H    
522  H HA   . VAL   A 43  ? 0.811318 0.645478 0.853222 -0.085252   -0.111094   -0.0215577  55  VAL   A HA   
523  H HB   . VAL   A 43  ? 0.738658 0.659345 0.781884 -0.0704463  -0.0883955  -0.0388668  55  VAL   A HB   
524  H HG11 . VAL   A 43  ? 0.762916 0.645172 0.773478 -0.0303783  -0.107272   -0.0304221  55  VAL   A HG11 
525  H HG12 . VAL   A 43  ? 0.759439 0.620234 0.786099 -0.0343692  -0.112427   -0.0513159  55  VAL   A HG12 
526  H HG13 . VAL   A 43  ? 0.709221 0.627232 0.732747 -0.0307644  -0.0952109  -0.0562859  55  VAL   A HG13 
527  H HG21 . VAL   A 43  ? 0.7649   0.729125 0.779157 -0.0606716  -0.0720536  -0.0230924  55  VAL   A HG21 
528  H HG22 . VAL   A 43  ? 0.782426 0.743177 0.810351 -0.0881569  -0.0664926  -0.00691819 55  VAL   A HG22 
529  H HG23 . VAL   A 43  ? 0.822166 0.747077 0.824958 -0.0731259  -0.0810811  0.00636043  55  VAL   A HG23 
530  N N    . HIS   A 44  ? 0.748708 0.665438 0.822785 -0.126082   -0.0838426  -0.0104779  56  HIS   A N    
531  C CA   . HIS   A 44  ? 0.689367 0.661564 0.783216 -0.142487   -0.0657526  -0.00589337 56  HIS   A CA   
532  C C    . HIS   A 44  ? 0.592572 0.605252 0.689332 -0.120514   -0.0582748  -0.0259125  56  HIS   A C    
533  O O    . HIS   A 44  ? 0.587653 0.58689  0.676269 -0.100252   -0.0675407  -0.0438945  56  HIS   A O    
534  C CB   . HIS   A 44  ? 0.821637 0.803944 0.951323 -0.169189   -0.0702219  -0.00951842 56  HIS   A CB   
535  C CG   . HIS   A 44  ? 0.795149 0.763185 0.931561 -0.204189   -0.0633218  0.014697    56  HIS   A CG   
536  N ND1  . HIS   A 44  ? 0.83589  0.844103 0.973045 -0.219588   -0.039621   0.0337107   56  HIS   A ND1  
537  C CD2  . HIS   A 44  ? 0.86435  0.781968 1.00519  -0.22921    -0.0737806  0.0228532   56  HIS   A CD2  
538  C CE1  . HIS   A 44  ? 0.907067 0.892653 1.04811  -0.254789   -0.0342718  0.0556701   56  HIS   A CE1  
539  N NE2  . HIS   A 44  ? 0.906702 0.833932 1.05123  -0.262262   -0.0553323  0.0497163   56  HIS   A NE2  
540  H H    . HIS   A 44  ? 0.740916 0.645905 0.821035 -0.119557   -0.0937701  -0.0263606  56  HIS   A H    
541  H HA   . HIS   A 44  ? 0.718799 0.697981 0.801176 -0.149957   -0.0549621  0.0110774   56  HIS   A HA   
542  H HB2  . HIS   A 44  ? 0.780722 0.737959 0.912622 -0.16477    -0.0853785  -0.022718   56  HIS   A HB2  
543  H HB3  . HIS   A 44  ? 0.742824 0.768945 0.890895 -0.16775    -0.0630413  -0.0175064  56  HIS   A HB3  
545  H HD2  . HIS   A 44  ? 0.881059 0.762675 1.02182  -0.226314   -0.0893746  0.0114459   56  HIS   A HD2  
546  H HE1  . HIS   A 44  ? 0.910294 0.916112 1.05012  -0.272293   -0.0171883  0.0719811   56  HIS   A HE1  
548  N N    . TYR   A 45  ? 0.581294 0.641392 0.687113 -0.124167   -0.0388668  -0.0229411  57  TYR   A N    
549  C CA   . TYR   A 45  ? 0.519759 0.606162 0.622677 -0.102903   -0.0293166  -0.0393365  57  TYR   A CA   
550  C C    . TYR   A 45  ? 0.506714 0.644333 0.633815 -0.108369   -0.0108571  -0.0392754  57  TYR   A C    
551  O O    . TYR   A 45  ? 0.55285  0.712136 0.690769 -0.128841   0.0004957   -0.0251258  57  TYR   A O    
552  C CB   . TYR   A 45  ? 0.513477 0.59128  0.584232 -0.0887113  -0.0227425  -0.0413318  57  TYR   A CB   
553  C CG   . TYR   A 45  ? 0.562957 0.66398  0.619524 -0.0984313  -0.00554108 -0.028125   57  TYR   A CG   
554  C CD1  . TYR   A 45  ? 0.521502 0.660643 0.582973 -0.0964644  0.0155209   -0.0361253  57  TYR   A CD1  
555  C CD2  . TYR   A 45  ? 0.646033 0.728295 0.68012  -0.10769    -0.0103907  -0.00770003 57  TYR   A CD2  
556  C CE1  . TYR   A 45  ? 0.559929 0.722394 0.603979 -0.105903   0.0326481   -0.027347   57  TYR   A CE1  
557  C CE2  . TYR   A 45  ? 0.61598  0.72054  0.62815  -0.116655   0.00486886  0.00524922  57  TYR   A CE2  
558  C CZ   . TYR   A 45  ? 0.582999 0.730119 0.599848 -0.117023   0.0272732   -0.00625646 57  TYR   A CZ   
559  O OH   . TYR   A 45  ? 0.63348  0.805965 0.624759 -0.125267   0.044459    0.00146129  57  TYR   A OH   
560  H H    . TYR   A 45  ? 0.587654 0.661715 0.700789 -0.140361   -0.030234   -0.0108553  57  TYR   A H    
561  H HA   . TYR   A 45  ? 0.516886 0.594359 0.624185 -0.0935814  -0.0393824  -0.0512128  57  TYR   A HA   
562  H HB2  . TYR   A 45  ? 0.502721 0.587273 0.571693 -0.0761752  -0.0185438  -0.0545311  57  TYR   A HB2  
563  H HB3  . TYR   A 45  ? 0.534037 0.58442  0.59356  -0.0850353  -0.0344441  -0.0397387  57  TYR   A HB3  
564  H HD1  . TYR   A 45  ? 0.515554 0.663747 0.590862 -0.087698   0.0183414   -0.0478605  57  TYR   A HD1  
565  H HD2  . TYR   A 45  ? 0.637029 0.688781 0.667564 -0.106355   -0.02472    -0.00246595 57  TYR   A HD2  
566  H HE1  . TYR   A 45  ? 0.546716 0.733646 0.593844 -0.102997   0.0478687   -0.0360632  57  TYR   A HE1  
567  H HE2  . TYR   A 45  ? 0.652753 0.741951 0.644746 -0.12146    2.503e-05   0.0217105   57  TYR   A HE2  
569  N N    . LYS   A 46  ? 0.523738 0.678415 0.659846 -0.0891429  -0.00827251 -0.0548961  58  LYS   A N    
570  C CA   . LYS   A 46  ? 0.561203 0.761086 0.718353 -0.0823308  0.00976447  -0.0597505  58  LYS   A CA   
571  C C    . LYS   A 46  ? 0.592822 0.776514 0.722156 -0.0598596  0.0202577   -0.0720639  58  LYS   A C    
572  O O    . LYS   A 46  ? 0.574404 0.726123 0.686188 -0.0472003  0.00971728  -0.0796723  58  LYS   A O    
573  C CB   . LYS   A 46  ? 0.496847 0.728934 0.695788 -0.0803396  -0.00145762 -0.0650409  58  LYS   A CB   
574  H H    . LYS   A 46  ? 0.51867  0.653546 0.646007 -0.0781001  -0.0181015  -0.0628565  58  LYS   A H    
575  H HA   . LYS   A 46  ? 0.554884 0.773577 0.714705 -0.0949559  0.0226197   -0.0517111  58  LYS   A HA   
578  N N    . GLY   A 47  ? 0.575316 0.777425 0.695793 -0.0589405  0.042593    -0.0747791  59  GLY   A N    
579  C CA   . GLY   A 47  ? 0.561796 0.744166 0.654618 -0.0446315  0.0539254   -0.0886466  59  GLY   A CA   
580  C C    . GLY   A 47  ? 0.54367  0.750839 0.645704 -0.0328973  0.077113    -0.0998817  59  GLY   A C    
581  O O    . GLY   A 47  ? 0.645664 0.894204 0.771433 -0.0380867  0.0887407   -0.0965499  59  GLY   A O    
582  H H    . GLY   A 47  ? 0.582692 0.810327 0.713977 -0.0691119  0.0519533   -0.0690982  59  GLY   A H    
583  H HA2  . GLY   A 47  ? 0.555211 0.71468  0.642588 -0.0347401  0.045331    -0.0935061  59  GLY   A HA2  
584  H HA3  . GLY   A 47  ? 0.563492 0.737751 0.635685 -0.0525228  0.0551884   -0.0869669  59  GLY   A HA3  
585  N N    . LYS   A 48  ? 0.617425 0.797151 0.701723 -0.0167775  0.0854362   -0.114537   60  LYS   A N    
586  C CA   . LYS   A 48  ? 0.615163 0.803586 0.706133 0.00031495  0.106606    -0.128351   60  LYS   A CA   
587  C C    . LYS   A 48  ? 0.618579 0.761224 0.676477 0.00663608  0.117049    -0.144498   60  LYS   A C    
588  O O    . LYS   A 48  ? 0.555445 0.663246 0.593511 0.00225025  0.106439    -0.143719   60  LYS   A O    
589  C CB   . LYS   A 48  ? 0.67183  0.872591 0.796221 0.0238102   0.100345    -0.126108   60  LYS   A CB   
590  C CG   . LYS   A 48  ? 0.89088  1.07024  1.01718  0.0299811   0.073854    -0.116066   60  LYS   A CG   
591  C CD   . LYS   A 48  ? 0.906367 1.09838  1.05889  0.0573113   0.0631075   -0.114001   60  LYS   A CD   
592  C CE   . LYS   A 48  ? 1.02772  1.18052  1.16088  0.0851246   0.0773856   -0.122434   60  LYS   A CE   
593  N NZ   . LYS   A 48  ? 1.1173   1.29609  1.28322  0.117739    0.0717519   -0.121236   60  LYS   A NZ   
594  H H    . LYS   A 48  ? 0.593963 0.746521 0.661429 -0.0165316  0.0786725   -0.116583   60  LYS   A H    
595  H HA   . LYS   A 48  ? 0.630655 0.846909 0.725031 -0.0072087  0.119067    -0.13001    60  LYS   A HA   
596  H HB2  . LYS   A 48  ? 0.721567 0.908001 0.841265 0.040513    0.11195     -0.136039   60  LYS   A HB2  
597  H HB3  . LYS   A 48  ? 0.697889 0.939321 0.848864 0.0200511   0.103139    -0.122614   60  LYS   A HB3  
598  H HG2  . LYS   A 48  ? 0.814367 1.00721  0.94829  0.0141198   0.0626257   -0.108185   60  LYS   A HG2  
599  H HG3  . LYS   A 48  ? 0.835817 0.977468 0.934673 0.0303866   0.0730649   -0.118742   60  LYS   A HG3  
600  H HD2  . LYS   A 48  ? 0.920245 1.15649  1.10555  0.0574576   0.0650204   -0.113616   60  LYS   A HD2  
601  H HD3  . LYS   A 48  ? 0.921212 1.10258  1.06985  0.0569145   0.0447258   -0.10788    60  LYS   A HD3  
602  H HE2  . LYS   A 48  ? 1.03027  1.1417   1.13536  0.0862887   0.0721106   -0.120067   60  LYS   A HE2  
603  H HE3  . LYS   A 48  ? 1.02137  1.1706   1.14669  0.0812056   0.09605     -0.131734   60  LYS   A HE3  
604  H HZ1  . LYS   A 48  ? 1.08872  1.27599  1.26225  0.120683    0.0526341   -0.113551   60  LYS   A HZ1  
605  H HZ2  . LYS   A 48  ? 1.08656  1.30701  1.28094  0.117151    0.0797575   -0.125483   60  LYS   A HZ2  
606  H HZ3  . LYS   A 48  ? 1.1211   1.26683  1.27138  0.136248    0.0792292   -0.124407   60  LYS   A HZ3  
607  N N    . LEU   A 49  ? 0.628375 0.772902 0.681815 0.0150877   0.140066    -0.16138    61  LEU   A N    
608  C CA   . LEU   A 49  ? 0.710124 0.803933 0.739678 0.0248931   0.153068    -0.178935   61  LEU   A CA   
609  C C    . LEU   A 49  ? 0.719593 0.782105 0.759766 0.0522298   0.146482    -0.171306   61  LEU   A C    
610  O O    . LEU   A 49  ? 0.71425  0.809143 0.786822 0.0694347   0.13906     -0.161768   61  LEU   A O    
611  C CB   . LEU   A 49  ? 0.736749 0.839388 0.760433 0.0293186   0.179774    -0.201837   61  LEU   A CB   
612  C CG   . LEU   A 49  ? 0.704501 0.841645 0.709401 0.00505193  0.187894    -0.210852   61  LEU   A CG   
613  C CD1  . LEU   A 49  ? 0.815426 0.950211 0.809385 0.0138458   0.216321    -0.239984   61  LEU   A CD1  
614  C CD2  . LEU   A 49  ? 0.648492 0.770921 0.623346 -0.0188866  0.177186    -0.213986   61  LEU   A CD2  
615  H H    . LEU   A 49  ? 0.64559  0.821994 0.710452 0.0138268   0.149261    -0.162886   61  LEU   A H    
616  H HA   . LEU   A 49  ? 0.694867 0.769381 0.704474 0.0112343   0.148933    -0.181336   61  LEU   A HA   
617  H HB2  . LEU   A 49  ? 0.736297 0.860985 0.783468 0.0452438   0.184598    -0.200176   61  LEU   A HB2  
618  H HB3  . LEU   A 49  ? 0.760196 0.82194  0.768051 0.0349655   0.188573    -0.214406   61  LEU   A HB3  
619  H HG   . LEU   A 49  ? 0.694385 0.869481 0.713968 0.00043608  0.183424    -0.197609   61  LEU   A HG   
620  H HD11 . LEU   A 49  ? 0.799943 0.949972 0.816769 0.0317176   0.223903    -0.239378   61  LEU   A HD11 
621  H HD12 . LEU   A 49  ? 0.798585 0.958948 0.777092 -0.00072086 0.221917    -0.246305   61  LEU   A HD12 
622  H HD13 . LEU   A 49  ? 0.817188 0.909621 0.796136 0.0162441   0.221461    -0.253677   61  LEU   A HD13 
623  H HD21 . LEU   A 49  ? 0.63799  0.766327 0.619533 -0.0238141  0.160368    -0.196972   61  LEU   A HD21 
624  H HD22 . LEU   A 49  ? 0.678496 0.764909 0.642443 -0.0178127  0.181236    -0.225732   61  LEU   A HD22 
625  H HD23 . LEU   A 49  ? 0.672822 0.817119 0.632747 -0.0301762  0.183094    -0.221933   61  LEU   A HD23 
626  N N    . SER   A 50  ? 0.849641 0.851295 0.862088 0.0563775   0.150361    -0.175784   62  SER   A N    
627  C CA   . SER   A 50  ? 0.967331 0.931071 0.97839  0.0840732   0.143786    -0.1645     62  SER   A CA   
628  C C    . SER   A 50  ? 1.07603  1.02931  1.10001  0.116397    0.159052    -0.173344   62  SER   A C    
629  O O    . SER   A 50  ? 1.2146   1.17148  1.25642  0.147001    0.14744     -0.160843   62  SER   A O    
630  C CB   . SER   A 50  ? 1.10386  1.00454  1.07702  0.0748253   0.14588     -0.162847   62  SER   A CB   
631  O OG   . SER   A 50  ? 1.08506  1.00564  1.05339  0.0491393   0.132536    -0.158013   62  SER   A OG   
632  H H    . SER   A 50  ? 0.847486 0.831368 0.840434 0.0411627   0.157134    -0.185303   62  SER   A H    
633  H HA   . SER   A 50  ? 0.954452 0.944388 0.982167 0.0885871   0.126516    -0.151173   62  SER   A HA   
634  H HB2  . SER   A 50  ? 1.108    0.980198 1.06589  0.0683187   0.162859    -0.176938   62  SER   A HB2  
635  H HB3  . SER   A 50  ? 1.10371  0.978631 1.07045  0.0929044   0.139878    -0.151591   62  SER   A HB3  
637  N N    . ASN   A 51  ? 1.11021  1.0559   1.12712  0.112202    0.18371     -0.196907   63  ASN   A N    
638  C CA   . ASN   A 51  ? 1.16708  1.11189  1.20125  0.144413    0.200956    -0.210683   63  ASN   A CA   
639  C C    . ASN   A 51  ? 1.18596  1.214    1.27141  0.161487    0.194382    -0.204661   63  ASN   A C    
640  O O    . ASN   A 51  ? 0.993495 1.03108  1.10229  0.194627    0.206823    -0.215387   63  ASN   A O    
641  C CB   . ASN   A 51  ? 1.19908  1.12756  1.21357  0.131423    0.229129    -0.242439   63  ASN   A CB   
642  C CG   . ASN   A 51  ? 1.20671  1.20858  1.23089  0.106371    0.234177    -0.251678   63  ASN   A CG   
643  O OD1  . ASN   A 51  ? 1.24991  1.30308  1.2894   0.0903544   0.216651    -0.232502   63  ASN   A OD1  
644  N ND2  . ASN   A 51  ? 1.2176   1.22053  1.22744  0.101359    0.258462    -0.281138   63  ASN   A ND2  
645  H H    . ASN   A 51  ? 1.1039   1.04599  1.10462  0.0894945   0.189746    -0.206433   63  ASN   A H    
646  H HA   . ASN   A 51  ? 1.2095   1.10784  1.23449  0.165682    0.199854    -0.205139   63  ASN   A HA   
647  H HB2  . ASN   A 51  ? 1.24826  1.15962  1.26917  0.156335    0.241665    -0.253069   63  ASN   A HB2  
648  H HB3  . ASN   A 51  ? 1.22622  1.10965  1.21216  0.114819    0.23249     -0.247704   63  ASN   A HB3  
649  H HD21 . ASN   A 51  ? 1.21145  1.2603   1.22754  0.0932333   0.263822    -0.28572    63  ASN   A HD21 
650  H HD22 . ASN   A 51  ? 1.26402  1.22035  1.25597  0.105278    0.269849    -0.296752   63  ASN   A HD22 
651  N N    . GLY   A 52  ? 1.19874  1.28647  1.30318  0.137815    0.177753    -0.190301   64  GLY   A N    
652  C CA   . GLY   A 52  ? 1.12596  1.29296  1.28156  0.144873    0.16924     -0.181653   64  GLY   A CA   
653  C C    . GLY   A 52  ? 1.26654  1.49383  1.44383  0.138717    0.194776    -0.198177   64  GLY   A C    
654  O O    . GLY   A 52  ? 1.37336  1.66549  1.60011  0.154155    0.196598    -0.197518   64  GLY   A O    
655  H H    . GLY   A 52  ? 1.14908  1.22662  1.23408  0.114599    0.172183    -0.186585   64  GLY   A H    
656  H HA2  . GLY   A 52  ? 1.13436  1.3183   1.29292  0.125999    0.153138    -0.168458   64  GLY   A HA2  
657  H HA3  . GLY   A 52  ? 1.18088  1.34787  1.35523  0.172539    0.161843    -0.177527   64  GLY   A HA3  
658  N N    . LYS   A 53  ? 1.14127  1.35558  1.28301  0.115365    0.21438     -0.213779   65  LYS   A N    
659  C CA   . LYS   A 53  ? 1.08018  1.34663  1.23071  0.111324    0.242355    -0.232082   65  LYS   A CA   
660  C C    . LYS   A 53  ? 1.09781  1.41356  1.24033  0.0712722   0.240841    -0.218768   65  LYS   A C    
661  O O    . LYS   A 53  ? 1.07831  1.44952  1.23033  0.0641732   0.262926    -0.226519   65  LYS   A O    
662  C CB   . LYS   A 53  ? 0.887508 1.10886  1.00563  0.123444    0.269172    -0.264821   65  LYS   A CB   
663  H H    . LYS   A 53  ? 1.15196  1.32746  1.26282  0.101615    0.210241    -0.213859   65  LYS   A H    
664  H HA   . LYS   A 53  ? 1.04963  1.35429  1.23827  0.130925    0.245922    -0.232308   65  LYS   A HA   
667  N N    . LYS   A 54  ? 1.14489  1.44151  1.26977  0.0464536   0.21609     -0.197436   66  LYS   A N    
668  C CA   . LYS   A 54  ? 0.997993 1.33209  1.11792  0.0133949   0.210236    -0.178409   66  LYS   A CA   
669  C C    . LYS   A 54  ? 0.955477 1.2766   1.08858  0.00341146  0.178388    -0.153264   66  LYS   A C    
670  O O    . LYS   A 54  ? 0.867531 1.13953  0.988136 0.0123896   0.161112    -0.152399   66  LYS   A O    
671  C CB   . LYS   A 54  ? 0.827437 1.15043  0.894609 -0.0101057  0.218031    -0.184644   66  LYS   A CB   
672  H H    . LYS   A 54  ? 1.09209  1.3482   1.20624  0.0511773   0.203273    -0.194542   66  LYS   A H    
673  H HA   . LYS   A 54  ? 0.981082 1.3621   1.12574  0.0127587   0.222453    -0.177478   66  LYS   A HA   
676  N N    . PHE   A 55  ? 0.821427 1.1856   0.977338 -0.01756    0.173474    -0.134204   67  PHE   A N    
677  C CA   . PHE   A 55  ? 0.773796 1.12905  0.942233 -0.0326402  0.14571     -0.112669   67  PHE   A CA   
678  C C    . PHE   A 55  ? 0.734565 1.09797  0.883382 -0.0658163  0.145331    -0.0932333  67  PHE   A C    
679  O O    . PHE   A 55  ? 0.944496 1.3403   1.08211  -0.0790253  0.168059    -0.0919575  67  PHE   A O    
680  C CB   . PHE   A 55  ? 0.6652   1.06407  0.890814 -0.0289878  0.136648    -0.106711   67  PHE   A CB   
681  C CG   . PHE   A 55  ? 0.711246 1.11384  0.959538 0.00903219  0.139403    -0.123319   67  PHE   A CG   
682  C CD1  . PHE   A 55  ? 0.745111 1.18207  1.00863  0.0268847   0.167353    -0.140224   67  PHE   A CD1  
683  C CD2  . PHE   A 55  ? 0.693422 1.06043  0.94202  0.0291028   0.114928    -0.12184    67  PHE   A CD2  
684  C CE1  . PHE   A 55  ? 0.785395 1.21547  1.06675  0.066846    0.169023    -0.154304   67  PHE   A CE1  
685  C CE2  . PHE   A 55  ? 0.725853 1.08719  0.987597 0.0670616   0.116386    -0.132523   67  PHE   A CE2  
686  C CZ   . PHE   A 55  ? 0.73503  1.12434  1.0138   0.0871885   0.14267     -0.14827    67  PHE   A CZ   
687  H H    . PHE   A 55  ? 0.854195 1.25439  1.01734  -0.0241117  0.190223    -0.135863   67  PHE   A H    
688  H HA   . PHE   A 55  ? 0.743549 1.05862  0.895248 -0.0261228  0.131343    -0.11348    67  PHE   A HA   
689  H HB2  . PHE   A 55  ? 0.702018 1.14296  0.94593  -0.0427308  0.149848    -0.102917   67  PHE   A HB2  
690  H HB3  . PHE   A 55  ? 0.685705 1.06746  0.91362  -0.0366916  0.116043    -0.0969414  67  PHE   A HB3  
691  H HD1  . PHE   A 55  ? 0.755937 1.21822  1.01475  0.0130964   0.185696    -0.142159   67  PHE   A HD1  
692  H HD2  . PHE   A 55  ? 0.691184 1.03571  0.928302 0.0180017   0.0973956   -0.11301    67  PHE   A HD2  
693  H HE1  . PHE   A 55  ? 0.784406 1.23615  1.07733  0.0813747   0.1886      -0.167629   67  PHE   A HE1  
694  H HE2  . PHE   A 55  ? 0.721427 1.05671  0.977574 0.0803818   0.099627    -0.128908   67  PHE   A HE2  
695  H HZ   . PHE   A 55  ? 0.765245 1.14668  1.05338  0.116031    0.142874    -0.154785   67  PHE   A HZ   
696  N N    . ASP   A 56  ? 0.663489 0.994085 0.804514 -0.0778635  0.119959    -0.077529   68  ASP   A N    
697  C CA   . ASP   A 56  ? 0.719484 1.03723  0.830955 -0.103229   0.115561    -0.0572401  68  ASP   A CA   
698  C C    . ASP   A 56  ? 0.61825  0.905818 0.74139  -0.113182   0.0880263   -0.0423612  68  ASP   A C    
699  O O    . ASP   A 56  ? 0.585484 0.839353 0.704498 -0.0984599  0.0697384   -0.0502778  68  ASP   A O    
700  C CB   . ASP   A 56  ? 0.679195 0.967501 0.738878 -0.0998398  0.1149      -0.0620701  68  ASP   A CB   
701  C CG   . ASP   A 56  ? 0.770207 1.04628  0.795829 -0.120264   0.107532    -0.0377841  68  ASP   A CG   
702  O OD1  . ASP   A 56  ? 0.773503 1.07773  0.795066 -0.139699   0.123848    -0.0217732  68  ASP   A OD1  
703  O OD2  . ASP   A 56  ? 0.741029 0.979455 0.746276 -0.11625    0.0855369   -0.0329393  68  ASP   A OD2  
704  H H    . ASP   A 56  ? 0.67283  0.986717 0.825051 -0.0687003  0.104941    -0.0793178  68  ASP   A H    
705  H HA   . ASP   A 56  ? 0.701362 1.05011  0.81886  -0.116848   0.130556    -0.049995   68  ASP   A HA   
706  H HB2  . ASP   A 56  ? 0.711161 1.01607  0.761619 -0.0943146  0.132202    -0.0750713  68  ASP   A HB2  
707  H HB3  . ASP   A 56  ? 0.687361 0.947982 0.743435 -0.0888525  0.101825    -0.0692814  68  ASP   A HB3  
708  N N    . SER   A 57  ? 0.694079 0.991965 0.830437 -0.139466   0.0873627   -0.022456   69  SER   A N    
709  C CA   . SER   A 57  ? 0.728532 0.992128 0.876714 -0.15056    0.0617708   -0.012211   69  SER   A CA   
710  C C    . SER   A 57  ? 0.76892  0.999922 0.887629 -0.17504    0.0586669   0.0145377   69  SER   A C    
711  O O    . SER   A 57  ? 0.872353 1.12471  0.977564 -0.193741   0.0790712   0.030367    69  SER   A O    
712  C CB   . SER   A 57  ? 0.689185 0.98866  0.892466 -0.160111   0.0577243   -0.0167523  69  SER   A CB   
713  O OG   . SER   A 57  ? 0.725833 0.990717 0.936352 -0.180233   0.0362333   -0.00659535 69  SER   A OG   
714  H H    . SER   A 57  ? 0.703639 1.0282   0.840458 -0.151979   0.104061    -0.0158453  69  SER   A H    
715  H HA   . SER   A 57  ? 0.699641 0.934553 0.836848 -0.134814   0.0475209   -0.0206978  69  SER   A HA   
716  H HB2  . SER   A 57  ? 0.678344 0.986596 0.895343 -0.140305   0.0522407   -0.0315284  69  SER   A HB2  
717  H HB3  . SER   A 57  ? 0.709239 1.04849  0.929937 -0.172187   0.0755102   -0.0131466  69  SER   A HB3  
719  N N    . SER   A 58  ? 0.755242 0.931945 0.862396 -0.17332    0.033442    0.0197151   70  SER   A N    
720  C CA   . SER   A 58  ? 0.815339 0.947074 0.900919 -0.193624   0.0249236   0.0458617   70  SER   A CA   
721  C C    . SER   A 58  ? 0.912967 1.06484  1.02855  -0.230484   0.0373382   0.0609835   70  SER   A C    
722  O O    . SER   A 58  ? 0.998265 1.12801  1.08879  -0.253618   0.0455573   0.0888237   70  SER   A O    
723  C CB   . SER   A 58  ? 0.769489 0.843541 0.850851 -0.181356   -0.0038909  0.0401876   70  SER   A CB   
724  O OG   . SER   A 58  ? 0.696701 0.782322 0.816264 -0.177895   -0.0145232  0.0183685   70  SER   A OG   
725  H H    . SER   A 58  ? 0.740907 0.905532 0.852484 -0.157539   0.0215278   0.00612461  70  SER   A H    
726  H HA   . SER   A 58  ? 0.833467 0.959685 0.886029 -0.191381   0.0309298   0.0570154   70  SER   A HA   
727  H HB2  . SER   A 58  ? 0.808919 0.848645 0.880992 -0.195255   -0.00985649 0.0568769   70  SER   A HB2  
728  H HB3  . SER   A 58  ? 0.757774 0.820741 0.817769 -0.161481   -0.00929334 0.0342922   70  SER   A HB3  
730  N N    . HIS   A 59  ? 0.834405 1.03178  1.00283  -0.236188   0.0393737   0.0434725   71  HIS   A N    
731  C CA   . HIS   A 59  ? 0.916235 1.14094  1.12591  -0.274003   0.0478809   0.051895    71  HIS   A CA   
732  C C    . HIS   A 59  ? 0.979844 1.25959  1.19248  -0.295809   0.0834448   0.0662527   71  HIS   A C    
733  O O    . HIS   A 59  ? 0.868818 1.15675  1.09838  -0.336067   0.0961027   0.0840472   71  HIS   A O    
734  C CB   . HIS   A 59  ? 0.873407 1.13944  1.14066  -0.268641   0.0341615   0.0254841   71  HIS   A CB   
735  C CG   . HIS   A 59  ? 0.894281 1.10592  1.15628  -0.257098   0.00100175  0.0128331   71  HIS   A CG   
736  N ND1  . HIS   A 59  ? 0.828454 1.03196  1.07836  -0.218909   -0.0137914  -0.00713949 71  HIS   A ND1  
737  C CD2  . HIS   A 59  ? 0.941683 1.10591  1.20895  -0.28011    -0.0179365  0.0149852   71  HIS   A CD2  
738  C CE1  . HIS   A 59  ? 0.875885 1.03317  1.12087  -0.21709    -0.0398376  -0.0168198  71  HIS   A CE1  
739  N NE2  . HIS   A 59  ? 1.03535  1.16731  1.29175  -0.253029   -0.0436911  -0.00551383 71  HIS   A NE2  
740  H H    . HIS   A 59  ? 0.823782 1.03669  1.00367  -0.215896   0.0344863   0.0255043   71  HIS   A H    
741  H HA   . HIS   A 59  ? 0.947934 1.12533  1.14517  -0.290417   0.0380253   0.065415    71  HIS   A HA   
742  H HB2  . HIS   A 59  ? 0.846974 1.14929  1.12248  -0.246453   0.040671    0.0124922   71  HIS   A HB2  
743  H HB3  . HIS   A 59  ? 0.8958   1.19307  1.19664  -0.295057   0.0415942   0.0286117   71  HIS   A HB3  
745  H HD2  . HIS   A 59  ? 0.99941  1.15171  1.27398  -0.309671   -0.0133732  0.0275796   71  HIS   A HD2  
746  H HE1  . HIS   A 59  ? 0.874105 1.01746  1.10819  -0.195709   -0.0520283  -0.0297367  71  HIS   A HE1  
748  N N    . ASP   A 60  ? 1.02925  1.34464  1.22369  -0.271392   0.101286    0.0570417   72  ASP   A N    
749  C CA   . ASP   A 60  ? 1.13745  1.50349  1.32235  -0.286658   0.137417    0.0670389   72  ASP   A CA   
750  C C    . ASP   A 60  ? 1.24541  1.5647   1.36743  -0.308876   0.145063    0.102459    72  ASP   A C    
751  O O    . ASP   A 60  ? 1.22192  1.57546  1.32835  -0.331501   0.175884    0.118163    72  ASP   A O    
752  C CB   . ASP   A 60  ? 1.1257   1.52761  1.29816  -0.252157   0.15172     0.0439945   72  ASP   A CB   
753  C CG   . ASP   A 60  ? 1.01177  1.44418  1.23116  -0.220885   0.142646    0.0124257   72  ASP   A CG   
754  O OD1  . ASP   A 60  ? 1.09573  1.57147  1.37495  -0.230748   0.141073    0.0057577   72  ASP   A OD1  
755  O OD2  . ASP   A 60  ? 0.813697 1.2272   1.00844  -0.18847    0.137516    -0.00428374 72  ASP   A OD2  
756  H H    . ASP   A 60  ? 0.997626 1.30441  1.18383  -0.244971   0.0915523   0.0427144   72  ASP   A H    
757  H HA   . ASP   A 60  ? 1.13246  1.54187  1.35906  -0.305632   0.149155    0.0653253   72  ASP   A HA   
758  H HB2  . ASP   A 60  ? 1.10881  1.47332  1.23862  -0.239057   0.143164    0.0467936   72  ASP   A HB2  
759  H HB3  . ASP   A 60  ? 1.12431  1.56588  1.29538  -0.262706   0.17724     0.0469557   72  ASP   A HB3  
760  N N    . ARG   A 61  ? 1.33345  1.5755   1.41536  -0.299034   0.11741     0.115377    73  ARG   A N    
761  C CA   . ARG   A 61  ? 1.43857  1.62447  1.46311  -0.317064   0.117041    0.153272    73  ARG   A CA   
762  C C    . ARG   A 61  ? 1.53291  1.66524  1.57598  -0.349937   0.105534    0.173239    73  ARG   A C    
763  O O    . ARG   A 61  ? 1.68706  1.75283  1.68355  -0.36285    0.0999932   0.206974    73  ARG   A O    
764  C CB   . ARG   A 61  ? 1.3228   1.46786  1.29525  -0.280088   0.0948514   0.151402    73  ARG   A CB   
765  H H    . ARG   A 61  ? 1.28514  1.50897  1.37475  -0.278529   0.0982009   0.100391    73  ARG   A H    
766  H HA   . ARG   A 61  ? 1.44495  1.66095  1.45276  -0.331797   0.141167    0.165022    73  ARG   A HA   
769  N N    . ASN   A 62  ? 1.41028  1.56933  1.51973  -0.363833   0.10099     0.15236     74  ASN   A N    
770  C CA   . ASN   A 62  ? 1.33044  1.4355   1.46309  -0.390737   0.0830366   0.158467    74  ASN   A CA   
771  C C    . ASN   A 62  ? 1.34249  1.3428   1.41803  -0.379882   0.0597674   0.181644    74  ASN   A C    
772  O O    . ASN   A 62  ? 1.32998  1.27181  1.38233  -0.411283   0.0638511   0.213614    74  ASN   A O    
773  C CB   . ASN   A 62  ? 1.33392  1.47638  1.5041   -0.445133   0.109727    0.172077    74  ASN   A CB   
774  H H    . ASN   A 62  ? 1.3576   1.57217  1.49921  -0.355958   0.109034    0.132217    74  ASN   A H    
775  H HA   . ASN   A 62  ? 1.29288  1.41083  1.45926  -0.377636   0.0674055   0.133328    74  ASN   A HA   
778  N N    . GLU   A 63  ? 1.28346  1.25852  1.33701  -0.334553   0.0358343   0.165912    75  GLU   A N    
779  C CA   . GLU   A 63  ? 1.34571  1.22977  1.35919  -0.316275   0.00959888  0.179546    75  GLU   A CA   
780  C C    . GLU   A 63  ? 1.25272  1.1396   1.26582  -0.268565   -0.0127044  0.14903     75  GLU   A C    
781  O O    . GLU   A 63  ? 1.21801  1.16465  1.23328  -0.248526   -0.00370052 0.13188     75  GLU   A O    
782  C CB   . GLU   A 63  ? 1.37189  1.21503  1.31991  -0.318461   0.0165912   0.222125    75  GLU   A CB   
783  H H    . GLU   A 63  ? 1.2409   1.25777  1.30635  -0.314062   0.0367279   0.14554     75  GLU   A H    
784  H HA   . GLU   A 63  ? 1.35687  1.20218  1.38707  -0.334204   0.00114605  0.180161    75  GLU   A HA   
787  N N    . PRO   A 64  ? 1.23869  1.06138  1.24882  -0.249792   -0.0398224  0.139659    76  PRO   A N    
788  C CA   . PRO   A 64  ? 1.10522  0.933185 1.11154  -0.206782   -0.0567681  0.113209    76  PRO   A CA   
789  C C    . PRO   A 64  ? 1.10073  0.954414 1.06954  -0.182311   -0.0520648  0.122355    76  PRO   A C    
790  O O    . PRO   A 64  ? 1.12952  0.975187 1.0628   -0.192676   -0.0431358  0.153638    76  PRO   A O    
791  C CB   . PRO   A 64  ? 1.13003  0.876179 1.12758  -0.193155   -0.0820352  0.111673    76  PRO   A CB   
792  C CG   . PRO   A 64  ? 1.20024  0.908179 1.21795  -0.234745   -0.0799011  0.120628    76  PRO   A CG   
793  C CD   . PRO   A 64  ? 1.27962  1.02107  1.29037  -0.269563   -0.053258   0.151193    76  PRO   A CD   
794  H HA   . PRO   A 64  ? 1.06878  0.933749 1.10258  -0.203978   -0.0550834  0.0898943   76  PRO   A HA   
795  H HB2  . PRO   A 64  ? 1.17497  0.889886 1.14221  -0.179445   -0.0880474  0.129655    76  PRO   A HB2  
796  H HB3  . PRO   A 64  ? 1.10348  0.855792 1.11403  -0.17404    -0.0919582  0.0864885   76  PRO   A HB3  
797  H HG2  . PRO   A 64  ? 1.26406  0.906672 1.26671  -0.232808   -0.0917537  0.130103    76  PRO   A HG2  
798  H HG3  . PRO   A 64  ? 1.17737  0.907341 1.22636  -0.241592   -0.0825097  0.0971953   76  PRO   A HG3  
799  H HD2  . PRO   A 64  ? 1.33172  1.03054  1.30931  -0.273039   -0.0525828  0.179239    76  PRO   A HD2  
800  H HD3  . PRO   A 64  ? 1.27985  1.03427  1.31928  -0.29941    -0.0456582  0.147896    76  PRO   A HD3  
801  N N    . PHE   A 65  ? 1.12885  1.01567  1.1047   -0.152843   -0.0572868  0.0938503   77  PHE   A N    
802  C CA   . PHE   A 65  ? 1.05261  0.963989 0.998621 -0.128568   -0.057869   0.0934707   77  PHE   A CA   
803  C C    . PHE   A 65  ? 1.08183  0.95075  1.01645  -0.0975376  -0.083418   0.0895189   77  PHE   A C    
804  O O    . PHE   A 65  ? 0.950842 0.802858 0.909201 -0.0849222  -0.0943898  0.0659031   77  PHE   A O    
805  C CB   . PHE   A 65  ? 0.948759 0.922894 0.912817 -0.121144   -0.0435867  0.0639378   77  PHE   A CB   
806  C CG   . PHE   A 65  ? 0.884689 0.888876 0.822526 -0.101484   -0.0429258  0.0562294   77  PHE   A CG   
807  C CD1  . PHE   A 65  ? 0.947439 0.981333 0.854703 -0.110786   -0.0287147  0.0702842   77  PHE   A CD1  
808  C CD2  . PHE   A 65  ? 0.812674 0.819757 0.756929 -0.0764729  -0.0552836  0.0322255   77  PHE   A CD2  
809  C CE1  . PHE   A 65  ? 0.949455 1.01347  0.832584 -0.0954535  -0.0306076  0.0588901   77  PHE   A CE1  
810  C CE2  . PHE   A 65  ? 0.833973 0.873941 0.759842 -0.0634555  -0.0552459  0.0219421   77  PHE   A CE2  
811  C CZ   . PHE   A 65  ? 0.895619 0.963601 0.791009 -0.0730509  -0.0445274  0.0341763   77  PHE   A CZ   
812  H H    . PHE   A 65  ? 1.05882  0.953735 1.05873  -0.149244   -0.060673   0.073257    77  PHE   A H    
813  H HA   . PHE   A 65  ? 1.09298  1.00686  1.01389  -0.138282   -0.0504024  0.11552     77  PHE   A HA   
814  H HB2  . PHE   A 65  ? 0.938289 0.938303 0.911767 -0.13834    -0.0276569  0.0668713   77  PHE   A HB2  
815  H HB3  . PHE   A 65  ? 0.915785 0.885819 0.900959 -0.1131     -0.0499597  0.0450804   77  PHE   A HB3  
816  H HD1  . PHE   A 65  ? 0.962927 0.998094 0.865069 -0.129066   -0.0174555  0.0866816   77  PHE   A HD1  
817  H HD2  . PHE   A 65  ? 0.820212 0.80873  0.781632 -0.0699225  -0.0632704  0.0217642   77  PHE   A HD2  
818  H HE1  . PHE   A 65  ? 0.959912 1.0444   0.81862  -0.10209    -0.021535   0.0666342   77  PHE   A HE1  
819  H HE2  . PHE   A 65  ? 0.816713 0.862234 0.750561 -0.0493899  -0.0620509  0.00504223  77  PHE   A HE2  
820  H HZ   . PHE   A 65  ? 0.886499 0.978505 0.769018 -0.0655999  -0.045987   0.0244771   77  PHE   A HZ   
821  N N    . VAL   A 66  ? 1.1247   0.981647 1.02149  -0.0844264  -0.0922528  0.112661    78  VAL   A N    
822  C CA   . VAL   A 66  ? 1.20707  1.02681  1.09174  -0.0515507  -0.11783    0.11535     78  VAL   A CA   
823  C C    . VAL   A 66  ? 1.13095  1.00657  1.00552  -0.0269345  -0.122917   0.10082     78  VAL   A C    
824  O O    . VAL   A 66  ? 1.23623  1.15332  1.08756  -0.0375274  -0.111172   0.108737    78  VAL   A O    
825  C CB   . VAL   A 66  ? 1.34176  1.10106  1.18671  -0.0562958  -0.126714   0.160163    78  VAL   A CB   
826  C CG1  . VAL   A 66  ? 1.42133  1.12363  1.25921  -0.0191727  -0.155637   0.165082    78  VAL   A CG1  
827  C CG2  . VAL   A 66  ? 1.37225  1.0933   1.22108  -0.097647   -0.111055   0.180448    78  VAL   A CG2  
828  H H    . VAL   A 66  ? 1.15012  1.0264   1.02726  -0.095132   -0.0820022  0.127162    78  VAL   A H    
829  H HA   . VAL   A 66  ? 1.18412  0.982058 1.0903   -0.0434421  -0.125318   0.0990876   78  VAL   A HA   
830  H HB   . VAL   A 66  ? 1.34844  1.13482  1.16638  -0.0562662  -0.123048   0.173839    78  VAL   A HB   
831  H HG11 . VAL   A 66  ? 1.39712  1.07992  1.26143  -0.0148921  -0.159351   0.144959    78  VAL   A HG11 
832  H HG12 . VAL   A 66  ? 1.39699  1.13216  1.22985  0.004548    -0.164877   0.157353    78  VAL   A HG12 
833  H HG13 . VAL   A 66  ? 1.48106  1.13405  1.29284  -0.0230355  -0.160944   0.195376    78  VAL   A HG13 
834  H HG21 . VAL   A 66  ? 1.44245  1.10903  1.26834  -0.0986553  -0.119021   0.206873    78  VAL   A HG21 
835  H HG22 . VAL   A 66  ? 1.35973  1.11831  1.2029   -0.11736    -0.0932759  0.186444    78  VAL   A HG22 
836  H HG23 . VAL   A 66  ? 1.34715  1.06168  1.22712  -0.103657   -0.110673   0.160256    78  VAL   A HG23 
837  N N    . PHE   A 67  ? 1.09377  0.971046 0.984719 0.00444841  -0.140196   0.0793593   79  PHE   A N    
838  C CA   . PHE   A 67  ? 0.983306 0.916826 0.870715 0.0264526   -0.147952   0.0638851   79  PHE   A CA   
839  C C    . PHE   A 67  ? 1.03553  0.960504 0.946409 0.0622356   -0.168521   0.0452044   79  PHE   A C    
840  O O    . PHE   A 67  ? 1.00704  0.890253 0.939335 0.0674934   -0.170622   0.0342463   79  PHE   A O    
841  C CB   . PHE   A 67  ? 0.886455 0.88277  0.789539 0.0116126   -0.126421   0.0333964   79  PHE   A CB   
842  C CG   . PHE   A 67  ? 0.828849 0.831093 0.769654 0.0145307   -0.118739   -0.00068206 79  PHE   A CG   
843  C CD1  . PHE   A 67  ? 0.78035  0.747868 0.736975 0.00130817  -0.111211   -0.00270573 79  PHE   A CD1  
844  C CD2  . PHE   A 67  ? 0.817503 0.861862 0.775983 0.0292414   -0.119602   -0.0303882  79  PHE   A CD2  
845  C CE1  . PHE   A 67  ? 0.819749 0.791746 0.801219 0.00544637  -0.105742   -0.0314     79  PHE   A CE1  
846  C CE2  . PHE   A 67  ? 0.800729 0.846405 0.785642 0.0306394   -0.110315   -0.0577289  79  PHE   A CE2  
847  C CZ   . PHE   A 67  ? 0.811024 0.818717 0.803601 0.0204217   -0.104194   -0.0571292  79  PHE   A CZ   
848  H H    . PHE   A 67  ? 1.08492  0.93017  0.991237 0.0114616   -0.146877   0.0722888   79  PHE   A H    
849  H HA   . PHE   A 67  ? 1.04184  0.97851  0.900106 0.0287415   -0.154406   0.0852255   79  PHE   A HA   
850  H HB2  . PHE   A 67  ? 0.889637 0.921984 0.78405  0.0200465   -0.131054   0.0273452   79  PHE   A HB2  
851  H HB3  . PHE   A 67  ? 0.891269 0.890367 0.785048 -0.00926894 -0.111787   0.0423532   79  PHE   A HB3  
852  H HD1  . PHE   A 67  ? 0.832323 0.774739 0.781333 -0.0118914  -0.109785   0.015744    79  PHE   A HD1  
853  H HD2  . PHE   A 67  ? 0.823313 0.896717 0.774779 0.0373249   -0.126505   -0.0317869  79  PHE   A HD2  
854  H HE1  . PHE   A 67  ? 0.802346 0.753511 0.79212  -0.00307866 -0.103102   -0.0330395  79  PHE   A HE1  
855  H HE2  . PHE   A 67  ? 0.778931 0.853648 0.775388 0.0375635   -0.108243   -0.0769571  79  PHE   A HE2  
856  H HZ   . PHE   A 67  ? 0.780148 0.789352 0.785014 0.0218301   -0.0984292  -0.0746656  79  PHE   A HZ   
857  N N    . SER   A 68  ? 0.982364 0.953948 0.891053 0.0863938   -0.1831     0.0379426   80  SER   A N    
858  C CA   . SER   A 68  ? 0.983746 0.960876 0.919208 0.12384     -0.202406   0.0197089   80  SER   A CA   
859  C C    . SER   A 68  ? 0.902242 0.94559  0.873516 0.120888    -0.188229   -0.0235313  80  SER   A C    
860  O O    . SER   A 68  ? 0.941734 1.04193  0.909532 0.104904    -0.177928   -0.0350141  80  SER   A O    
861  C CB   . SER   A 68  ? 1.11182  1.10039  1.02795  0.156292    -0.231327   0.0401      80  SER   A CB   
862  O OG   . SER   A 68  ? 1.24425  1.15177  1.13062  0.169074    -0.247508   0.0795548   80  SER   A OG   
863  H H    . SER   A 68  ? 0.992604 0.99692  0.884249 0.0795045   -0.180962   0.0427252   80  SER   A H    
864  H HA   . SER   A 68  ? 1.01424  0.94286  0.95772  0.129596    -0.204859   0.021103    80  SER   A HA   
865  H HB2  . SER   A 68  ? 1.10108  1.12708  0.99846  0.145822    -0.22975    0.04541     80  SER   A HB2  
866  H HB3  . SER   A 68  ? 1.09456  1.11238  1.03685  0.179939    -0.241059   0.0198248   80  SER   A HB3  
868  N N    . LEU   A 69  ? 0.94322  0.972957 0.945242 0.133307    -0.185224   -0.0478046  81  LEU   A N    
869  C CA   . LEU   A 69  ? 0.851031 0.926731 0.880325 0.122371    -0.164754   -0.0844481  81  LEU   A CA   
870  C C    . LEU   A 69  ? 0.813685 0.964659 0.86737  0.139109    -0.170894   -0.107938   81  LEU   A C    
871  O O    . LEU   A 69  ? 0.787922 0.949248 0.857296 0.173342    -0.191962   -0.10965    81  LEU   A O    
872  C CB   . LEU   A 69  ? 0.851071 0.888027 0.89761  0.130125    -0.159426   -0.101571   81  LEU   A CB   
873  C CG   . LEU   A 69  ? 0.88069  0.954475 0.94623  0.117457    -0.135894   -0.134933   81  LEU   A CG   
874  C CD1  . LEU   A 69  ? 0.82725  0.887206 0.876668 0.0832342   -0.115491   -0.130297   81  LEU   A CD1  
875  C CD2  . LEU   A 69  ? 0.899275 0.950005 0.981779 0.139405    -0.137539   -0.15594    81  LEU   A CD2  
876  H H    . LEU   A 69  ? 0.954364 0.94289  0.957768 0.148707    -0.195387   -0.0413526  81  LEU   A H    
877  H HA   . LEU   A 69  ? 0.82871  0.911772 0.848165 0.0977276   -0.149636   -0.0834172  81  LEU   A HA   
878  H HB2  . LEU   A 69  ? 0.881178 0.872928 0.914127 0.117992    -0.157873   -0.0875613  81  LEU   A HB2  
879  H HB3  . LEU   A 69  ? 0.896749 0.925633 0.953679 0.156395    -0.173403   -0.104578   81  LEU   A HB3  
880  H HG   . LEU   A 69  ? 0.84376  0.967273 0.920924 0.11911     -0.133228   -0.146885   81  LEU   A HG   
881  H HD11 . LEU   A 69  ? 0.823961 0.903097 0.864129 0.0713517   -0.112401   -0.121326   81  LEU   A HD11 
882  H HD12 . LEU   A 69  ? 0.810461 0.884915 0.86755  0.0778584   -0.101835   -0.148738   81  LEU   A HD12 
883  H HD13 . LEU   A 69  ? 0.849719 0.867826 0.890379 0.0793673   -0.119356   -0.118425   81  LEU   A HD13 
884  H HD21 . LEU   A 69  ? 0.905724 0.985146 1.00613  0.16082     -0.144626   -0.166976   81  LEU   A HD21 
885  H HD22 . LEU   A 69  ? 0.927049 0.927881 0.999843 0.144229    -0.147197   -0.143848   81  LEU   A HD22 
886  H HD23 . LEU   A 69  ? 0.871774 0.929266 0.95616  0.127309    -0.121542   -0.171304   81  LEU   A HD23 
887  N N    . GLY   A 70  ? 0.861058 1.06354  0.919726 0.114193    -0.152166   -0.12696    82  GLY   A N    
888  C CA   . GLY   A 70  ? 0.879085 1.16016  0.964561 0.118978    -0.153969   -0.153842   82  GLY   A CA   
889  C C    . GLY   A 70  ? 0.968526 1.28889  1.04115  0.132055    -0.180144   -0.140114   82  GLY   A C    
890  O O    . GLY   A 70  ? 0.994687 1.38811  1.09421  0.139611    -0.188523   -0.163013   82  GLY   A O    
891  H H    . GLY   A 70  ? 0.827049 1.01474  0.873218 0.0925874   -0.137446   -0.12397    82  GLY   A H    
892  H HA2  . GLY   A 70  ? 0.851506 1.1515   0.938801 0.0955259   -0.134984   -0.168403   82  GLY   A HA2  
893  H HA3  . GLY   A 70  ? 0.880287 1.17328  0.991608 0.136694    -0.156407   -0.168907   82  GLY   A HA3  
894  N N    . LYS   A 71  ? 1.00302  1.27928  1.03382  0.133012    -0.192799   -0.103232   83  LYS   A N    
895  C CA   . LYS   A 71  ? 0.998144 1.30697  1.00363  0.144881    -0.217986   -0.0856559  83  LYS   A CA   
896  C C    . LYS   A 71  ? 1.04806  1.3764   1.02031  0.108256    -0.201377   -0.0854011  83  LYS   A C    
897  O O    . LYS   A 71  ? 1.08632  1.41518  1.01625  0.10921     -0.215357   -0.0600932  83  LYS   A O    
898  C CB   . LYS   A 71  ? 1.05385  1.3046   1.03293  0.176695    -0.24543    -0.0451133  83  LYS   A CB   
899  H H    . LYS   A 71  ? 0.99522  1.22181  1.01143  0.124662    -0.185083   -0.0886123  83  LYS   A H    
900  H HA   . LYS   A 71  ? 1.01022  1.37398  1.04121  0.157954    -0.228444   -0.105292   83  LYS   A HA   
903  N N    . GLY   A 72  ? 0.980039 1.31955  0.967764 0.0777624   -0.170695   -0.112968   84  GLY   A N    
904  C CA   . GLY   A 72  ? 0.937662 1.30776  0.90646  0.0462251   -0.153024   -0.127816   84  GLY   A CA   
905  C C    . GLY   A 72  ? 0.90824  1.23856  0.831636 0.0271644   -0.139493   -0.102289   84  GLY   A C    
906  O O    . GLY   A 72  ? 0.775151 1.13287  0.676632 0.00654251  -0.128208   -0.114121   84  GLY   A O    
907  H H    . GLY   A 72  ? 0.954504 1.27752  0.963744 0.0777618   -0.16007    -0.122993   84  GLY   A H    
908  H HA2  . GLY   A 72  ? 0.900597 1.27738  0.89028  0.032136    -0.13441    -0.15053    84  GLY   A HA2  
909  H HA3  . GLY   A 72  ? 0.947959 1.36482  0.914679 0.0503452   -0.167293   -0.136464   84  GLY   A HA3  
910  N N    . GLN   A 73  ? 0.863144 1.13188  0.774461 0.0310353   -0.137713   -0.0712669  85  GLN   A N    
911  C CA   . GLN   A 73  ? 0.926162 1.16828  0.795735 0.0151272   -0.128257   -0.0428581  85  GLN   A CA   
912  C C    . GLN   A 73  ? 0.850491 1.07264  0.728421 -0.00985558 -0.0959325  -0.0518848  85  GLN   A C    
913  O O    . GLN   A 73  ? 0.858366 1.0724   0.710063 -0.0265694  -0.0808089  -0.0369287  85  GLN   A O    
914  C CB   . GLN   A 73  ? 0.998487 1.18393  0.850599 0.028536    -0.143493   -0.00179869 85  GLN   A CB   
915  C CG   . GLN   A 73  ? 1.07043  1.25979  0.912997 0.0614184   -0.178362   0.0141283   85  GLN   A CG   
916  C CD   . GLN   A 73  ? 1.09587  1.21062  0.928971 0.0759153   -0.190873   0.0501414   85  GLN   A CD   
917  O OE1  . GLN   A 73  ? 1.09667  1.16408  0.946986 0.0634926   -0.176033   0.051727    85  GLN   A OE1  
918  N NE2  . GLN   A 73  ? 1.12892  1.22985  0.93399  0.102828    -0.219762   0.0786719   85  GLN   A NE2  
919  H H    . GLN   A 73  ? 0.878312 1.12289  0.808317 0.042472    -0.141656   -0.0689925  85  GLN   A H    
920  H HA   . GLN   A 73  ? 0.935875 1.20907  0.781242 0.0112604   -0.13225    -0.0437539  85  GLN   A HA   
921  H HB2  . GLN   A 73  ? 0.979291 1.13354  0.853629 0.0287996   -0.137979   -0.00361748 85  GLN   A HB2  
922  H HB3  . GLN   A 73  ? 1.02002  1.19325  0.843937 0.0147707   -0.134956   0.0170924   85  GLN   A HB3  
923  H HG2  . GLN   A 73  ? 1.08847  1.3028   0.900687 0.0610188   -0.186144   0.022861    85  GLN   A HG2  
924  H HG3  . GLN   A 73  ? 1.03624  1.25299  0.908661 0.0746569   -0.185773   -0.00871479 85  GLN   A HG3  
925  H HE21 . GLN   A 73  ? 1.18015  1.2301   0.973634 0.109518    -0.226219   0.102679    85  GLN   A HE21 
926  H HE22 . GLN   A 73  ? 1.15021  1.29174  0.947519 0.114399    -0.233324   0.0739188   85  GLN   A HE22 
927  N N    . VAL   A 74  ? 0.683391 0.900164 0.597903 -0.0103063  -0.0853749  -0.076008   86  VAL   A N    
928  C CA   . VAL   A 74  ? 0.630072 0.834198 0.555406 -0.0279392  -0.058235   -0.0892722  86  VAL   A CA   
929  C C    . VAL   A 74  ? 0.620793 0.85434  0.564103 -0.0335529  -0.0471626  -0.125373   86  VAL   A C    
930  O O    . VAL   A 74  ? 0.649037 0.914408 0.604406 -0.0247912  -0.0608426  -0.139698   86  VAL   A O    
931  C CB   . VAL   A 74  ? 0.635283 0.793643 0.580863 -0.0229564  -0.0583568  -0.078593   86  VAL   A CB   
932  C CG1  . VAL   A 74  ? 0.708724 0.835079 0.637464 -0.0264089  -0.0647179  -0.0441294  86  VAL   A CG1  
933  C CG2  . VAL   A 74  ? 0.607773 0.759593 0.57653  -0.00318117 -0.0739372  -0.0887797  86  VAL   A CG2  
934  H H    . VAL   A 74  ? 0.700657 0.922632 0.633133 0.00258284  -0.095913   -0.0841868  86  VAL   A H    
935  H HA   . VAL   A 74  ? 0.65143  0.857904 0.558879 -0.03896    -0.047951   -0.0823751  86  VAL   A HA   
936  H HB   . VAL   A 74  ? 0.612829 0.766793 0.566786 -0.0316095  -0.0426484  -0.0887027  86  VAL   A HB   
937  H HG11 . VAL   A 74  ? 0.724928 0.847304 0.642423 -0.015962   -0.0809423  -0.0313008  86  VAL   A HG11 
938  H HG12 . VAL   A 74  ? 0.702167 0.838752 0.61696  -0.0389787  -0.052782   -0.0387057  86  VAL   A HG12 
939  H HG13 . VAL   A 74  ? 0.690025 0.789747 0.632729 -0.0270001  -0.0640437  -0.0408478  86  VAL   A HG13 
940  H HG21 . VAL   A 74  ? 0.609288 0.733237 0.587909 -0.00223488 -0.0719335  -0.0866913  86  VAL   A HG21 
941  H HG22 . VAL   A 74  ? 0.597564 0.774264 0.577072 -0.00367747 -0.0685214  -0.109834   86  VAL   A HG22 
942  H HG23 . VAL   A 74  ? 0.642228 0.793399 0.604771 0.00914078  -0.0908742  -0.0770242  86  VAL   A HG23 
943  N N    . ILE   A 75  ? 0.569338 0.789855 0.517209 -0.047367   -0.0224293  -0.138883   87  ILE   A N    
944  C CA   . ILE   A 75  ? 0.562973 0.795361 0.523408 -0.05723    -0.00677723 -0.169943   87  ILE   A CA   
945  C C    . ILE   A 75  ? 0.55735  0.788134 0.544745 -0.0475161  -0.0128247  -0.179221   87  ILE   A C    
946  O O    . ILE   A 75  ? 0.622066 0.825656 0.6173   -0.0342221  -0.0214343  -0.163764   87  ILE   A O    
947  C CB   . ILE   A 75  ? 0.608598 0.811839 0.564785 -0.0673564  0.0191008   -0.17448    87  ILE   A CB   
948  C CG1  . ILE   A 75  ? 0.590534 0.758515 0.555309 -0.0586854  0.0189956   -0.153295   87  ILE   A CG1  
949  C CG2  . ILE   A 75  ? 0.664048 0.879785 0.596803 -0.0781331  0.0319006   -0.179249   87  ILE   A CG2  
950  C CD1  . ILE   A 75  ? 0.603216 0.748178 0.569246 -0.0624863  0.0412947   -0.160765   87  ILE   A CD1  
951  H H    . ILE   A 75  ? 0.580418 0.782957 0.523068 -0.0508008  -0.0148967  -0.127387   87  ILE   A H    
952  H HA   . ILE   A 75  ? 0.58318  0.84426  0.536269 -0.0634437  -0.00862931 -0.182392   87  ILE   A HA   
953  H HB   . ILE   A 75  ? 0.597663 0.79698  0.56154  -0.0726551  0.0291841   -0.191366   87  ILE   A HB   
954  H HG12 . ILE   A 75  ? 0.603545 0.772651 0.561562 -0.0573969  0.0125136   -0.136514   87  ILE   A HG12 
955  H HG13 . ILE   A 75  ? 0.587536 0.747002 0.563538 -0.0515314  0.0105527   -0.152022   87  ILE   A HG13 
956  H HG21 . ILE   A 75  ? 0.65186  0.852079 0.585756 -0.0828177  0.0489394   -0.190151   87  ILE   A HG21 
957  H HG22 . ILE   A 75  ? 0.658918 0.872543 0.583695 -0.0749839  0.0284168   -0.160656   87  ILE   A HG22 
958  H HG23 . ILE   A 75  ? 0.664986 0.906782 0.588885 -0.0833835  0.0268695   -0.190825   87  ILE   A HG23 
959  H HD11 . ILE   A 75  ? 0.59959  0.741089 0.565617 -0.067034   0.0505974   -0.177199   87  ILE   A HD11 
960  H HD12 . ILE   A 75  ? 0.589987 0.716988 0.564641 -0.0561575  0.0384066   -0.151056   87  ILE   A HD12 
961  H HD13 . ILE   A 75  ? 0.607246 0.758723 0.564976 -0.0661505  0.0491514   -0.159119   87  ILE   A HD13 
962  N N    . LYS   A 76  ? 0.506754 0.769331 0.50814  -0.0561968  -0.0072442  -0.20645    88  LYS   A N    
963  C CA   . LYS   A 76  ? 0.544456 0.815294 0.572059 -0.0528482  -0.00394336 -0.221689   88  LYS   A CA   
964  C C    . LYS   A 76  ? 0.518928 0.741188 0.546558 -0.0444752  0.00359675  -0.209542   88  LYS   A C    
965  O O    . LYS   A 76  ? 0.503945 0.722235 0.543453 -0.026974   -0.00923146 -0.204057   88  LYS   A O    
966  C CB   . LYS   A 76  ? 0.524473 0.819083 0.56073  -0.0775229  0.0164601   -0.252713   88  LYS   A CB   
967  H H    . LYS   A 76  ? 0.537756 0.820851 0.531728 -0.0667563  -0.00411688 -0.217624   88  LYS   A H    
968  H HA   . LYS   A 76  ? 0.529768 0.826058 0.569403 -0.0398679  -0.0211104  -0.220871   88  LYS   A HA   
971  N N    . ALA   A 77  ? 0.512045 0.697286 0.524771 -0.0544697  0.0222649   -0.205884   89  ALA   A N    
972  C CA   . ALA   A 77  ? 0.494373 0.63835  0.503003 -0.0471137  0.027196    -0.195313   89  ALA   A CA   
973  C C    . ALA   A 77  ? 0.525515 0.654179 0.536827 -0.0303422  0.00610955  -0.175441   89  ALA   A C    
974  O O    . ALA   A 77  ? 0.554326 0.660617 0.566945 -0.0222711  0.00427893  -0.174359   89  ALA   A O    
975  C CB   . ALA   A 77  ? 0.518874 0.631252 0.511776 -0.0542169  0.0436499   -0.189907   89  ALA   A CB   
976  H H    . ALA   A 77  ? 0.516139 0.702833 0.520142 -0.0651255  0.0313882   -0.211005   89  ALA   A H    
977  H HA   . ALA   A 77  ? 0.50746  0.652629 0.521536 -0.0481832  0.0341748   -0.205926   89  ALA   A HA   
978  H HB1  . ALA   A 77  ? 0.522086 0.633838 0.510911 -0.0651307  0.0583836   -0.202564   89  ALA   A HB1  
979  H HB2  . ALA   A 77  ? 0.513519 0.629241 0.502937 -0.0537012  0.0393315   -0.181234   89  ALA   A HB2  
980  H HB3  . ALA   A 77  ? 0.513334 0.602767 0.503327 -0.0479547  0.0440449   -0.182962   89  ALA   A HB3  
981  N N    . TRP   A 78  ? 0.590596 0.725731 0.59805  -0.0276604  -0.00788014 -0.159543   90  TRP   A N    
982  C CA   . TRP   A 78  ? 0.605341 0.717442 0.6147   -0.0161556  -0.0262931  -0.140308   90  TRP   A CA   
983  C C    . TRP   A 78  ? 0.619581 0.73816  0.641475 0.00151542  -0.0429665  -0.146026   90  TRP   A C    
984  O O    . TRP   A 78  ? 0.72366  0.814253 0.750469 0.0125232   -0.0518816  -0.143769   90  TRP   A O    
985  C CB   . TRP   A 78  ? 0.612008 0.724127 0.60951  -0.0209811  -0.0334872  -0.118099   90  TRP   A CB   
986  C CG   . TRP   A 78  ? 0.675932 0.770898 0.671286 -0.0312893  -0.0233002  -0.10668    90  TRP   A CG   
987  C CD1  . TRP   A 78  ? 0.637268 0.732389 0.633558 -0.0375646  -0.00490985 -0.116045   90  TRP   A CD1  
988  C CD2  . TRP   A 78  ? 0.660754 0.735961 0.65734  -0.0352414  -0.031974   -0.0843212  90  TRP   A CD2  
989  N NE1  . TRP   A 78  ? 0.666899 0.754209 0.668693 -0.0422686  -0.00282395 -0.102179   90  TRP   A NE1  
990  C CE2  . TRP   A 78  ? 0.643805 0.72077  0.647527 -0.0441781  -0.0182752  -0.0835699  90  TRP   A CE2  
991  C CE3  . TRP   A 78  ? 0.695278 0.749214 0.688544 -0.0324318  -0.0494941  -0.0651181  90  TRP   A CE3  
992  C CZ2  . TRP   A 78  ? 0.636173 0.705864 0.649337 -0.0539184  -0.0208041  -0.0666156  90  TRP   A CZ2  
993  C CZ3  . TRP   A 78  ? 0.710402 0.744873 0.708005 -0.0449401  -0.0505892  -0.0470133  90  TRP   A CZ3  
994  C CH2  . TRP   A 78  ? 0.698961 0.747443 0.708588 -0.057483   -0.0358541  -0.0485725  90  TRP   A CH2  
995  H H    . TRP   A 78  ? 0.578794 0.730203 0.580161 -0.0342989  -0.00522746 -0.160725   90  TRP   A H    
996  H HA   . TRP   A 78  ? 0.599792 0.690022 0.609536 -0.0165655  -0.0227462  -0.138303   90  TRP   A HA   
997  H HB2  . TRP   A 78  ? 0.630622 0.766286 0.620928 -0.02558    -0.0301285  -0.122405   90  TRP   A HB2  
998  H HB3  . TRP   A 78  ? 0.643571 0.745452 0.641595 -0.0125707  -0.0483707  -0.107181   90  TRP   A HB3  
999  H HD1  . TRP   A 78  ? 0.642911 0.74368  0.636932 -0.0390272  0.00545952  -0.129867   90  TRP   A HD1  
1000 H HE1  . TRP   A 78  ? 0.64464  0.732693 0.64961  -0.0434958  0.00664304  -0.104944   90  TRP   A HE1  
1001 H HE3  . TRP   A 78  ? 0.705842 0.757762 0.695537 -0.0222081  -0.0603276  -0.0650259  90  TRP   A HE3  
1002 H HZ2  . TRP   A 78  ? 0.640674 0.719136 0.663448 -0.0579885  -0.0124694  -0.0676457  90  TRP   A HZ2  
1003 H HZ3  . TRP   A 78  ? 0.73856  0.752041 0.731617 -0.0455178  -0.0610097  -0.0327097  90  TRP   A HZ3  
1004 H HH2  . TRP   A 78  ? 0.700284 0.742149 0.717363 -0.0678798  -0.0366924  -0.0373721  90  TRP   A HH2  
1005 N N    . ASP   A 79  ? 0.624204 0.782017 0.652727 0.00613498  -0.0489091  -0.155386   91  ASP   A N    
1006 C CA   . ASP   A 79  ? 0.599023 0.771631 0.646057 0.0282368   -0.0648815  -0.163408   91  ASP   A CA   
1007 C C    . ASP   A 79  ? 0.566277 0.735458 0.627328 0.0312661   -0.0517387  -0.184614   91  ASP   A C    
1008 O O    . ASP   A 79  ? 0.741187 0.893907 0.811218 0.0507357   -0.0619559  -0.187377   91  ASP   A O    
1009 C CB   . ASP   A 79  ? 0.644379 0.874255 0.70258  0.0325289   -0.0734789  -0.174827   91  ASP   A CB   
1010 C CG   . ASP   A 79  ? 0.703568 0.939719 0.743992 0.0408309   -0.0954371  -0.152157   91  ASP   A CG   
1011 O OD1  . ASP   A 79  ? 0.781728 0.971937 0.807734 0.0506943   -0.107686   -0.125984   91  ASP   A OD1  
1012 O OD2  . ASP   A 79  ? 0.668449 0.955436 0.708319 0.0364308   -0.100535   -0.161778   91  ASP   A OD2  
1013 H H    . ASP   A 79  ? 0.613301 0.791258 0.636004 -0.00337704 -0.0437504  -0.158288   91  ASP   A H    
1014 H HA   . ASP   A 79  ? 0.629936 0.777373 0.672729 0.039496    -0.0791044  -0.148058   91  ASP   A HA   
1015 H HB2  . ASP   A 79  ? 0.627105 0.877396 0.685166 0.0156753   -0.0590389  -0.187732   91  ASP   A HB2  
1016 H HB3  . ASP   A 79  ? 0.642892 0.890708 0.72075  0.0466384   -0.0788361  -0.186834   91  ASP   A HB3  
1017 N N    . ILE   A 80  ? 0.570027 0.749644 0.628635 0.012053    -0.0277844  -0.199397   92  ILE   A N    
1018 C CA   . ILE   A 80  ? 0.580862 0.756747 0.643644 0.0111766   -0.0110852  -0.216815   92  ILE   A CA   
1019 C C    . ILE   A 80  ? 0.584086 0.70874  0.628919 0.0162296   -0.0127138  -0.206341   92  ILE   A C    
1020 O O    . ILE   A 80  ? 0.59517  0.711242 0.641908 0.0283228   -0.0130024  -0.217059   92  ILE   A O    
1021 C CB   . ILE   A 80  ? 0.617494 0.806469 0.67476  -0.0139851  0.0158106   -0.229728   92  ILE   A CB   
1022 C CG1  . ILE   A 80  ? 0.646526 0.893913 0.727411 -0.0225159  0.0181359   -0.248894   92  ILE   A CG1  
1023 C CG2  . ILE   A 80  ? 0.66958  0.838801 0.715766 -0.018834   0.0366045   -0.238683   92  ILE   A CG2  
1024 C CD1  . ILE   A 80  ? 0.694235 0.94192  0.765694 -0.052447   0.0431765   -0.259609   92  ILE   A CD1  
1025 H H    . ILE   A 80  ? 0.56372  0.750556 0.615066 -0.00118095 -0.020673   -0.19832    92  ILE   A H    
1026 H HA   . ILE   A 80  ? 0.589891 0.789115 0.66998  0.0231776   -0.0158744  -0.228177   92  ILE   A HA   
1027 H HB   . ILE   A 80  ? 0.620879 0.791065 0.663849 -0.022682   0.018575    -0.219414   92  ILE   A HB   
1028 H HG12 . ILE   A 80  ? 0.650406 0.922233 0.74923  -0.0155955  0.0196989   -0.262      92  ILE   A HG12 
1029 H HG13 . ILE   A 80  ? 0.647318 0.909146 0.73204  -0.0153511  0.00139333  -0.242352   92  ILE   A HG13 
1030 H HG21 . ILE   A 80  ? 0.660062 0.838721 0.704826 -0.0351976  0.0543869   -0.24767    92  ILE   A HG21 
1031 H HG22 . ILE   A 80  ? 0.660434 0.842956 0.71804  -0.00711725 0.0332352   -0.247652   92  ILE   A HG22 
1032 H HG23 . ILE   A 80  ? 0.659745 0.793574 0.687444 -0.017307   0.0358005   -0.226751   92  ILE   A HG23 
1033 H HD11 . ILE   A 80  ? 0.680564 0.89666  0.73263  -0.0565565  0.0452261   -0.24744    92  ILE   A HD11 
1034 H HD12 . ILE   A 80  ? 0.679477 0.964726 0.764744 -0.0599802  0.0404463   -0.271157   92  ILE   A HD12 
1035 H HD13 . ILE   A 80  ? 0.686435 0.928175 0.756855 -0.0605047  0.0604265   -0.267991   92  ILE   A HD13 
1036 N N    . GLY   A 81  ? 0.527336 0.623882 0.555607 0.00616387  -0.0125302  -0.188769   93  GLY   A N    
1037 C CA   . GLY   A 81  ? 0.54673  0.604595 0.560637 0.00740826  -0.0148803  -0.180757   93  GLY   A CA   
1038 C C    . GLY   A 81  ? 0.552139 0.586098 0.571358 0.0213413   -0.0374169  -0.174964   93  GLY   A C    
1039 O O    . GLY   A 81  ? 0.533916 0.547202 0.546731 0.0286895   -0.0407858  -0.184089   93  GLY   A O    
1040 H H    . GLY   A 81  ? 0.536766 0.642462 0.563751 -0.00146741 -0.0111891  -0.183021   93  GLY   A H    
1041 H HA2  . GLY   A 81  ? 0.547798 0.602046 0.553667 0.00662427  -0.00410072 -0.190335   93  GLY   A HA2  
1042 H HA3  . GLY   A 81  ? 0.536243 0.586237 0.54381  -0.00071012 -0.0120876  -0.170309   93  GLY   A HA3  
1043 N N    . VAL   A 82  ? 0.497893 0.5311   0.524617 0.0238693   -0.0522233  -0.159895   94  VAL   A N    
1044 C CA   . VAL   A 82  ? 0.546935 0.545712 0.575987 0.0333465   -0.0721371  -0.150972   94  VAL   A CA   
1045 C C    . VAL   A 82  ? 0.609272 0.604134 0.647706 0.0565003   -0.080135   -0.1691     94  VAL   A C    
1046 O O    . VAL   A 82  ? 0.556904 0.512575 0.593394 0.0647323   -0.0922798  -0.171832   94  VAL   A O    
1047 C CB   . VAL   A 82  ? 0.551036 0.544733 0.578453 0.0281512   -0.0826588  -0.125839   94  VAL   A CB   
1048 C CG1  . VAL   A 82  ? 0.674705 0.622074 0.702102 0.0357435   -0.102031   -0.114096   94  VAL   A CG1  
1049 C CG2  . VAL   A 82  ? 0.547029 0.544565 0.568215 0.00665333  -0.0722941  -0.112208   94  VAL   A CG2  
1050 H H    . VAL   A 82  ? 0.508905 0.56073  0.536642 0.0188171   -0.0493804  -0.155065   94  VAL   A H    
1051 H HA   . VAL   A 82  ? 0.55191  0.530854 0.575731 0.0270724   -0.0726587  -0.149827   94  VAL   A HA   
1052 H HB   . VAL   A 82  ? 0.566502 0.58461  0.596038 0.0337044   -0.0829759  -0.126551   94  VAL   A HB   
1053 H HG11 . VAL   A 82  ? 0.652632 0.579191 0.680364 0.0323608   -0.102967   -0.120967   94  VAL   A HG11 
1054 H HG12 . VAL   A 82  ? 0.663892 0.609682 0.695673 0.0532145   -0.110206   -0.119337   94  VAL   A HG12 
1055 H HG13 . VAL   A 82  ? 0.659229 0.598143 0.681231 0.0264067   -0.105286   -0.0948705  94  VAL   A HG13 
1056 H HG21 . VAL   A 82  ? 0.555437 0.551435 0.573066 0.00186355  -0.0765454  -0.0962137  94  VAL   A HG21 
1057 H HG22 . VAL   A 82  ? 0.52328  0.543483 0.542757 0.00251565  -0.0596004  -0.119667   94  VAL   A HG22 
1058 H HG23 . VAL   A 82  ? 0.546422 0.526103 0.568772 0.00190226  -0.0737471  -0.112572   94  VAL   A HG23 
1059 N N    . ALA   A 83  ? 0.550686 0.587874 0.601584 0.0660584   -0.0720867  -0.18513    95  ALA   A N    
1060 C CA   . ALA   A 83  ? 0.589876 0.634106 0.655526 0.0905448   -0.076031   -0.206553   95  ALA   A CA   
1061 C C    . ALA   A 83  ? 0.615398 0.646913 0.670091 0.0901439   -0.0626721  -0.227708   95  ALA   A C    
1062 O O    . ALA   A 83  ? 0.649313 0.68258  0.713448 0.111125    -0.0639798  -0.248301   95  ALA   A O    
1063 C CB   . ALA   A 83  ? 0.590591 0.697623 0.680179 0.0989039   -0.0706108  -0.220164   95  ALA   A CB   
1064 H H    . ALA   A 83  ? 0.547835 0.611915 0.600049 0.0570377   -0.0636679  -0.184431   95  ALA   A H    
1065 H HA   . ALA   A 83  ? 0.617629 0.634372 0.685172 0.103728    -0.0923627  -0.199213   95  ALA   A HA   
1066 H HB1  . ALA   A 83  ? 0.585665 0.702872 0.677    0.0979116   -0.0798353  -0.206857   95  ALA   A HB1  
1067 H HB2  . ALA   A 83  ? 0.567772 0.697832 0.656279 0.0847648   -0.0528505  -0.229981   95  ALA   A HB2  
1068 H HB3  . ALA   A 83  ? 0.602642 0.71764  0.706861 0.119103    -0.0756921  -0.233134   95  ALA   A HB3  
1069 N N    . THR   A 84  ? 0.66318  0.684335 0.696158 0.0693579   -0.0497414  -0.223677   96  THR   A N    
1070 C CA   . THR   A 84  ? 0.679556 0.683644 0.691257 0.0692324   -0.0409109  -0.239287   96  THR   A CA   
1071 C C    . THR   A 84  ? 0.743132 0.699122 0.740683 0.0680848   -0.0594323  -0.233733   96  THR   A C    
1072 O O    . THR   A 84  ? 0.720871 0.662761 0.696439 0.0684525   -0.0566013  -0.247534   96  THR   A O    
1073 C CB   . THR   A 84  ? 0.687421 0.703792 0.678411 0.0499997   -0.0186476  -0.236015   96  THR   A CB   
1074 O OG1  . THR   A 84  ? 0.560387 0.557919 0.542498 0.0364024   -0.0251407  -0.213948   96  THR   A OG1  
1075 C CG2  . THR   A 84  ? 0.653729 0.71388  0.660001 0.042023    0.00057861  -0.241111   96  THR   A CG2  
1076 H H    . THR   A 84  ? 0.630363 0.65575  0.659848 0.0563707   -0.0467007  -0.21093    96  THR   A H    
1077 H HA   . THR   A 84  ? 0.702955 0.719133 0.720947 0.0820433   -0.0365156  -0.256911   96  THR   A HA   
1078 H HB   . THR   A 84  ? 0.67264  0.68149  0.64561  0.051642    -0.0115919  -0.246444   96  THR   A HB   
1080 H HG21 . THR   A 84  ? 0.659786 0.721129 0.65012  0.0313604   0.0175359   -0.243153   96  THR   A HG21 
1081 H HG22 . THR   A 84  ? 0.64099  0.70666  0.656084 0.0362821   -0.00451161 -0.229388   96  THR   A HG22 
1082 H HG23 . THR   A 84  ? 0.662113 0.744124 0.68503  0.0528953   0.00113796  -0.254897   96  THR   A HG23 
1083 N N    . MET   A 85  ? 0.736067 0.669423 0.742823 0.0623468   -0.0768382  -0.213437   97  MET   A N    
1084 C CA   . MET   A 85  ? 0.674567 0.570599 0.672424 0.0517581   -0.0916381  -0.207969   97  MET   A CA   
1085 C C    . MET   A 85  ? 0.677939 0.53009  0.680578 0.0642001   -0.109934   -0.218233   97  MET   A C    
1086 O O    . MET   A 85  ? 0.68015  0.525709 0.696405 0.0803203   -0.115479   -0.215714   97  MET   A O    
1087 C CB   . MET   A 85  ? 0.61417  0.511626 0.6207   0.0325466   -0.0959349  -0.180294   97  MET   A CB   
1088 C CG   . MET   A 85  ? 0.645387 0.578119 0.647369 0.0223136   -0.0780722  -0.171612   97  MET   A CG   
1089 S SD   . MET   A 85  ? 0.630867 0.572627 0.645602 0.00403838  -0.079269   -0.143863   97  MET   A SD   
1090 C CE   . MET   A 85  ? 0.625083 0.543743 0.644831 -0.00871652 -0.0958426  -0.142172   97  MET   A CE   
1091 H H    . MET   A 85  ? 0.708994 0.652276 0.72749  0.0635945   -0.0793101  -0.203163   97  MET   A H    
1092 H HA   . MET   A 85  ? 0.674577 0.572567 0.65711  0.0483565   -0.0867613  -0.216743   97  MET   A HA   
1093 H HB2  . MET   A 85  ? 0.643134 0.536411 0.659145 0.0354459   -0.100816   -0.170117   97  MET   A HB2  
1094 H HB3  . MET   A 85  ? 0.652676 0.531006 0.658114 0.0238615   -0.10552    -0.178651   97  MET   A HB3  
1095 H HG2  . MET   A 85  ? 0.629295 0.561631 0.619376 0.0203492   -0.0748591  -0.177684   97  MET   A HG2  
1096 H HG3  . MET   A 85  ? 0.617134 0.568564 0.62009  0.0278796   -0.0679911  -0.176294   97  MET   A HG3  
1097 H HE1  . MET   A 85  ? 0.624712 0.552319 0.654852 -0.0203407  -0.0952367  -0.128491   97  MET   A HE1  
1098 H HE2  . MET   A 85  ? 0.656636 0.550143 0.677674 -0.00666244 -0.106818   -0.146795   97  MET   A HE2  
1099 H HE3  . MET   A 85  ? 0.629727 0.553285 0.640672 -0.00657493 -0.0945481  -0.151182   97  MET   A HE3  
1100 N N    . LYS   A 86  ? 0.774437 0.593606 0.766253 0.0559409   -0.12171    -0.228041   98  LYS   A N    
1101 C CA   . LYS   A 86  ? 0.866091 0.631521 0.860491 0.0639879   -0.138984   -0.240181   98  LYS   A CA   
1102 C C    . LYS   A 86  ? 0.856445 0.589725 0.860677 0.0390945   -0.153534   -0.21779    98  LYS   A C    
1103 O O    . LYS   A 86  ? 0.780249 0.542259 0.789331 0.0179155   -0.149444   -0.199148   98  LYS   A O    
1104 C CB   . LYS   A 86  ? 0.911059 0.660505 0.883984 0.0698962   -0.141447   -0.27455    98  LYS   A CB   
1105 C CG   . LYS   A 86  ? 0.972642 0.761733 0.924213 0.0808211   -0.122384   -0.294459   98  LYS   A CG   
1106 C CD   . LYS   A 86  ? 1.12736  0.918736 1.08083  0.110148    -0.112741   -0.321772   98  LYS   A CD   
1107 C CE   . LYS   A 86  ? 1.29271  1.09824  1.21286  0.115592    -0.0993332  -0.35196    98  LYS   A CE   
1108 N NZ   . LYS   A 86  ? 1.29713  1.14941  1.202    0.103993    -0.0782653  -0.338914   98  LYS   A NZ   
1109 H H    . LYS   A 86  ? 0.755428 0.584155 0.737703 0.0451687   -0.119862   -0.228121   98  LYS   A H    
1110 H HA   . LYS   A 86  ? 0.864484 0.625105 0.867652 0.0814271   -0.138977   -0.240718   98  LYS   A HA   
1111 H HB2  . LYS   A 86  ? 0.933309 0.67252  0.901023 0.0525698   -0.150328   -0.273235   98  LYS   A HB2  
1112 H HB3  . LYS   A 86  ? 0.966527 0.683057 0.942275 0.0826948   -0.148605   -0.28721    98  LYS   A HB3  
1113 H HG2  . LYS   A 86  ? 0.940313 0.761296 0.894849 0.0756258   -0.111215   -0.279512   98  LYS   A HG2  
1114 H HG3  . LYS   A 86  ? 0.996527 0.780648 0.928657 0.0728968   -0.126321   -0.304683   98  LYS   A HG3  
1115 H HD2  . LYS   A 86  ? 1.15593  0.911343 1.11782  0.119549    -0.124856   -0.328747   98  LYS   A HD2  
1116 H HD3  . LYS   A 86  ? 1.09734  0.917973 1.06579  0.117111    -0.102663   -0.3133     98  LYS   A HD3  
1117 H HE2  . LYS   A 86  ? 1.29306  1.07394  1.19566  0.107618    -0.110808   -0.3609     98  LYS   A HE2  
1118 H HE3  . LYS   A 86  ? 1.28795  1.09568  1.21244  0.13477     -0.0926168  -0.371814   98  LYS   A HE3  
1119 H HZ1  . LYS   A 86  ? 1.27044  1.11874  1.16603  0.0895021   -0.0847557  -0.325437   98  LYS   A HZ1  
1120 H HZ2  . LYS   A 86  ? 1.25191  1.12595  1.17572  0.105835    -0.070021   -0.328066   98  LYS   A HZ2  
1121 H HZ3  . LYS   A 86  ? 1.29881  1.16174  1.18348  0.109342    -0.0665239  -0.355595   98  LYS   A HZ3  
1122 N N    . LYS   A 87  ? 0.917536 0.590824 0.925589 0.0407283   -0.168552   -0.219903   99  LYS   A N    
1123 C CA   . LYS   A 87  ? 0.997304 0.637992 1.0149   0.0110063   -0.17894    -0.197787   99  LYS   A CA   
1124 C C    . LYS   A 87  ? 0.997986 0.658862 1.01639  -0.0163079  -0.183137   -0.208494   99  LYS   A C    
1125 O O    . LYS   A 87  ? 1.04358  0.70506  1.04788  -0.0112095  -0.187931   -0.2387     99  LYS   A O    
1126 C CB   . LYS   A 87  ? 1.1255   0.685837 1.1437   0.01248     -0.193324   -0.195567   99  LYS   A CB   
1127 C CG   . LYS   A 87  ? 1.20945  0.737997 1.23696  -0.0238093  -0.198394   -0.165396   99  LYS   A CG   
1128 C CD   . LYS   A 87  ? 1.3999   0.833116 1.42312  -0.0275057  -0.211626   -0.161599   99  LYS   A CD   
1129 C CE   . LYS   A 87  ? 1.49073  0.892227 1.52134  -0.0700037  -0.211926   -0.128616   99  LYS   A CE   
1130 N NZ   . LYS   A 87  ? 1.53518  0.833587 1.55853  -0.0804529  -0.222918   -0.12333    99  LYS   A NZ   
1131 H H    . LYS   A 87  ? 0.957315 0.608937 0.962464 0.0597323   -0.171157   -0.23524    99  LYS   A H    
1132 H HA   . LYS   A 87  ? 0.969355 0.632186 0.993072 0.00546821  -0.172648   -0.173867   99  LYS   A HA   
1133 H HB2  . LYS   A 87  ? 1.13446  0.685802 1.15158  0.035687    -0.192527   -0.189765   99  LYS   A HB2  
1134 H HB3  . LYS   A 87  ? 1.15817  0.691969 1.17041  0.0153352   -0.200013   -0.221188   99  LYS   A HB3  
1135 H HG2  . LYS   A 87  ? 1.20099  0.749902 1.23523  -0.0466924  -0.199035   -0.171512   99  LYS   A HG2  
1136 H HG3  . LYS   A 87  ? 1.18941  0.742732 1.21903  -0.0246699  -0.191      -0.140629   99  LYS   A HG3  
1137 H HD2  . LYS   A 87  ? 1.40591  0.819401 1.4226   -0.0005854  -0.212726   -0.154754   99  LYS   A HD2  
1138 H HD3  . LYS   A 87  ? 1.41829  0.825474 1.43882  -0.0272768  -0.21889    -0.189558   99  LYS   A HD3  
1139 H HE2  . LYS   A 87  ? 1.4395   0.872627 1.4821   -0.0955952  -0.210466   -0.135489   99  LYS   A HE2  
1140 H HE3  . LYS   A 87  ? 1.44074  0.864362 1.46922  -0.0679091  -0.204381   -0.10144    99  LYS   A HE3  
1141 H HZ1  . LYS   A 87  ? 1.57819  0.854481 1.60432  -0.0886606  -0.229891   -0.149343   99  LYS   A HZ1  
1142 H HZ2  . LYS   A 87  ? 1.58013  0.84649  1.59241  -0.0525428  -0.226181   -0.118559   99  LYS   A HZ2  
1143 H HZ3  . LYS   A 87  ? 1.57017  0.857463 1.5966   -0.106748   -0.219333   -0.0991566  99  LYS   A HZ3  
1144 N N    . GLY   A 88  ? 1.0001   0.687919 1.03442  -0.0430769  -0.18046    -0.183786   100 GLY   A N    
1145 C CA   . GLY   A 88  ? 0.981677 0.69842  1.0255   -0.0674481  -0.187201   -0.191849   100 GLY   A CA   
1146 C C    . GLY   A 88  ? 0.880415 0.657829 0.915021 -0.0559477  -0.178336   -0.196702   100 GLY   A C    
1147 O O    . GLY   A 88  ? 0.867837 0.673065 0.906661 -0.0678069  -0.186991   -0.204996   100 GLY   A O    
1148 H H    . GLY   A 88  ? 0.980442 0.672233 1.02043  -0.0452818  -0.174578   -0.162133   100 GLY   A H    
1149 H HA2  . GLY   A 88  ? 0.971424 0.69413  1.03254  -0.0883114  -0.186512   -0.17405    100 GLY   A HA2  
1150 H HA3  . GLY   A 88  ? 1.01068  0.699906 1.04997  -0.0720601  -0.199192   -0.212215   100 GLY   A HA3  
1151 N N    . GLU   A 89  ? 0.808595 0.60585  0.83038  -0.0330253  -0.162012   -0.191594   101 GLU   A N    
1152 C CA   . GLU   A 89  ? 0.740709 0.582516 0.749457 -0.0236164  -0.150683   -0.193108   101 GLU   A CA   
1153 C C    . GLU   A 89  ? 0.73512  0.613917 0.764457 -0.0364318  -0.141638   -0.167353   101 GLU   A C    
1154 O O    . GLU   A 89  ? 0.704597 0.582781 0.748822 -0.0442497  -0.135012   -0.147488   101 GLU   A O    
1155 C CB   . GLU   A 89  ? 0.744867 0.587956 0.73225  0.00091289  -0.13627    -0.20467    101 GLU   A CB   
1156 C CG   . GLU   A 89  ? 0.688668 0.56378  0.653972 0.00912647  -0.121557   -0.207132   101 GLU   A CG   
1157 C CD   . GLU   A 89  ? 0.663384 0.54786  0.615925 0.0253512   -0.101851   -0.215092   101 GLU   A CD   
1158 O OE1  . GLU   A 89  ? 0.69662  0.568545 0.640593 0.0395526   -0.0998986  -0.23626    101 GLU   A OE1  
1159 O OE2  . GLU   A 89  ? 0.660759 0.570229 0.615983 0.0226962   -0.0859893  -0.200248   101 GLU   A OE2  
1160 H H    . GLU   A 89  ? 0.816568 0.59817  0.837812 -0.0235105  -0.158066   -0.186732   101 GLU   A H    
1161 H HA   . GLU   A 89  ? 0.769568 0.614402 0.769957 -0.0263662  -0.159841   -0.206009   101 GLU   A HA   
1162 H HB2  . GLU   A 89  ? 0.765831 0.585356 0.744101 0.00824101  -0.142585   -0.222422   101 GLU   A HB2  
1163 H HB3  . GLU   A 89  ? 0.721969 0.566559 0.718572 0.00467537  -0.129406   -0.193772   101 GLU   A HB3  
1164 H HG2  . GLU   A 89  ? 0.66844  0.562891 0.642461 0.00241661  -0.117054   -0.191731   101 GLU   A HG2  
1165 H HG3  . GLU   A 89  ? 0.71172  0.583624 0.661276 0.00933929  -0.129202   -0.218921   101 GLU   A HG3  
1166 N N    . ILE   A 90  ? 0.766095 0.676838 0.794912 -0.0381158  -0.143469   -0.168641   102 ILE   A N    
1167 C CA   . ILE   A 90  ? 0.691966 0.641148 0.733531 -0.0390334  -0.130247   -0.150563   102 ILE   A CA   
1168 C C    . ILE   A 90  ? 0.688053 0.644827 0.700724 -0.0189492  -0.116201   -0.154075   102 ILE   A C    
1169 O O    . ILE   A 90  ? 0.673799 0.627007 0.661951 -0.00956044 -0.123135   -0.166284   102 ILE   A O    
1170 C CB   . ILE   A 90  ? 0.691987 0.673243 0.759209 -0.0521832  -0.142915   -0.148291   102 ILE   A CB   
1171 C CG1  . ILE   A 90  ? 0.740131 0.713648 0.838911 -0.080266   -0.153548   -0.144756   102 ILE   A CG1  
1172 C CG2  . ILE   A 90  ? 0.661242 0.682877 0.740473 -0.0449951  -0.128017   -0.133547   102 ILE   A CG2  
1173 C CD1  . ILE   A 90  ? 0.772881 0.782769 0.901502 -0.0966822  -0.171056   -0.151729   102 ILE   A CD1  
1174 H H    . ILE   A 90  ? 0.763393 0.671271 0.782601 -0.0370154  -0.154059   -0.181962   102 ILE   A H    
1175 H HA   . ILE   A 90  ? 0.688122 0.637567 0.739841 -0.0439705  -0.121713   -0.13862    102 ILE   A HA   
1176 H HB   . ILE   A 90  ? 0.71284  0.693579 0.767137 -0.0466297  -0.154487   -0.160746   102 ILE   A HB   
1177 H HG12 . ILE   A 90  ? 0.726124 0.705802 0.83656  -0.0869151  -0.141712   -0.129549   102 ILE   A HG12 
1178 H HG13 . ILE   A 90  ? 0.763592 0.701566 0.851569 -0.0819513  -0.160314   -0.153374   102 ILE   A HG13 
1179 H HG21 . ILE   A 90  ? 0.662047 0.710241 0.764535 -0.0525473  -0.135729   -0.132067   102 ILE   A HG21 
1180 H HG22 . ILE   A 90  ? 0.646831 0.668544 0.73139  -0.0482362  -0.114613   -0.123459   102 ILE   A HG22 
1181 H HG23 . ILE   A 90  ? 0.658654 0.679267 0.716537 -0.0293554  -0.12389    -0.136419   102 ILE   A HG23 
1182 H HD11 . ILE   A 90  ? 0.784642 0.786106 0.899143 -0.0921524  -0.185558   -0.167954   102 ILE   A HD11 
1183 H HD12 . ILE   A 90  ? 0.778504 0.784392 0.929254 -0.118456   -0.173499   -0.147704   102 ILE   A HD12 
1184 H HD13 . ILE   A 90  ? 0.743139 0.790005 0.88316  -0.0901898  -0.165478   -0.144737   102 ILE   A HD13 
1185 N N    . ALA   A 91  ? 0.602267 0.569515 0.616405 -0.0154811  -0.0963826  -0.142477   103 ALA   A N    
1186 C CA   . ALA   A 91  ? 0.593886 0.565003 0.584511 -0.00272535 -0.0784452  -0.143238   103 ALA   A CA   
1187 C C    . ALA   A 91  ? 0.584235 0.577079 0.587873 -0.0040166  -0.0638848  -0.129204   103 ALA   A C    
1188 O O    . ALA   A 91  ? 0.575273 0.583495 0.603712 -0.0145486  -0.0629494  -0.119691   103 ALA   A O    
1189 C CB   . ALA   A 91  ? 0.539652 0.499406 0.517957 0.00216647  -0.0660868  -0.151795   103 ALA   A CB   
1190 H H    . ALA   A 91  ? 0.60813  0.578607 0.637025 -0.0229793  -0.0934932  -0.133871   103 ALA   A H    
1191 H HA   . ALA   A 91  ? 0.601945 0.569517 0.575678 0.00374226  -0.08336    -0.148464   103 ALA   A HA   
1192 H HB1  . ALA   A 91  ? 0.570808 0.517417 0.541821 0.00563679  -0.0738954  -0.162665   103 ALA   A HB1  
1193 H HB2  . ALA   A 91  ? 0.542587 0.507254 0.535049 -0.00234635 -0.0638139  -0.145931   103 ALA   A HB2  
1194 H HB3  . ALA   A 91  ? 0.551569 0.513661 0.515382 0.00642958  -0.0526089  -0.152972   103 ALA   A HB3  
1195 N N    . HIS   A 92  ? 0.604763 0.594099 0.587308 0.00686395  -0.051128   -0.128512   104 HIS   A N    
1196 C CA   . HIS   A 92  ? 0.602678 0.600355 0.588913 0.00995243  -0.0331733  -0.120535   104 HIS   A CA   
1197 C C    . HIS   A 92  ? 0.562078 0.543908 0.526993 0.00830867  -0.0118536  -0.126836   104 HIS   A C    
1198 O O    . HIS   A 92  ? 0.621376 0.585503 0.560556 0.0110974   -0.00751745 -0.134129   104 HIS   A O    
1199 C CB   . HIS   A 92  ? 0.576908 0.573289 0.553442 0.0255984   -0.0362957  -0.114488   104 HIS   A CB   
1200 C CG   . HIS   A 92  ? 0.568823 0.594617 0.574297 0.0273742   -0.0571343  -0.110725   104 HIS   A CG   
1201 N ND1  . HIS   A 92  ? 0.566043 0.603136 0.571314 0.0451434   -0.0680408  -0.105525   104 HIS   A ND1  
1202 C CD2  . HIS   A 92  ? 0.536052 0.585481 0.57493  0.0120573   -0.0673986  -0.110915   104 HIS   A CD2  
1203 C CE1  . HIS   A 92  ? 0.594967 0.670869 0.638756 0.0389724   -0.086138   -0.10625    104 HIS   A CE1  
1204 N NE2  . HIS   A 92  ? 0.592677 0.674051 0.657148 0.0161693   -0.0837324  -0.108956   104 HIS   A NE2  
1205 H H    . HIS   A 92  ? 0.61857  0.595621 0.580163 0.0129221   -0.0532316  -0.133808   104 HIS   A H    
1206 H HA   . HIS   A 92  ? 0.569713 0.583849 0.577436 0.00311629  -0.0322762  -0.116067   104 HIS   A HA   
1207 H HB2  . HIS   A 92  ? 0.604946 0.583108 0.554882 0.0314246   -0.037804   -0.117061   104 HIS   A HB2  
1208 H HB3  . HIS   A 92  ? 0.585924 0.579421 0.561168 0.0297883   -0.0219598  -0.110978   104 HIS   A HB3  
1210 H HD2  . HIS   A 92  ? 0.543125 0.589069 0.587927 0.00026636  -0.0646423  -0.111621   104 HIS   A HD2  
1211 H HE1  . HIS   A 92  ? 0.599824 0.697118 0.655495 0.04892     -0.098419   -0.104529   104 HIS   A HE1  
1213 N N    . LEU   A 93  ? 0.535531 0.528555 0.511968 0.00132403  0.00211053  -0.12596    105 LEU   A N    
1214 C CA   . LEU   A 93  ? 0.583215 0.569349 0.546317 -0.00474048 0.0218005   -0.134908   105 LEU   A CA   
1215 C C    . LEU   A 93  ? 0.580134 0.558705 0.539091 -0.00356641 0.0402671   -0.133549   105 LEU   A C    
1216 O O    . LEU   A 93  ? 0.679507 0.674372 0.655822 -0.00144174 0.0395719   -0.128347   105 LEU   A O    
1217 C CB   . LEU   A 93  ? 0.525715 0.533545 0.504177 -0.0140917  0.0180421   -0.139139   105 LEU   A CB   
1218 C CG   . LEU   A 93  ? 0.558944 0.567934 0.542263 -0.0117383  0.00192783  -0.142887   105 LEU   A CG   
1219 C CD1  . LEU   A 93  ? 0.55075  0.58042  0.546145 -0.0166384  -0.00093152 -0.143362   105 LEU   A CD1  
1220 C CD2  . LEU   A 93  ? 0.606719 0.604182 0.572428 -0.00790153 0.00947947  -0.155444   105 LEU   A CD2  
1221 H H    . LEU   A 93  ? 0.539182 0.547117 0.532484 -0.00123678 -0.00042043 -0.120809   105 LEU   A H    
1222 H HA   . LEU   A 93  ? 0.578099 0.550551 0.524644 -0.00314455 0.0251549   -0.139601   105 LEU   A HA   
1223 H HB2  . LEU   A 93  ? 0.534895 0.554595 0.525172 -0.0164647  0.0150069   -0.132343   105 LEU   A HB2  
1224 H HB3  . LEU   A 93  ? 0.543362 0.554251 0.517024 -0.0194787  0.0304475   -0.14662    105 LEU   A HB3  
1225 H HG   . LEU   A 93  ? 0.560769 0.565183 0.549929 -0.00946776 -0.0110055  -0.136821   105 LEU   A HG   
1226 H HD11 . LEU   A 93  ? 0.546316 0.582432 0.547596 -0.020488   -0.00309644 -0.13401    105 LEU   A HD11 
1227 H HD12 . LEU   A 93  ? 0.553745 0.581302 0.55347  -0.0119762  -0.0119994  -0.144971   105 LEU   A HD12 
1228 H HD13 . LEU   A 93  ? 0.548366 0.587323 0.540318 -0.0203162  0.0103037   -0.151724   105 LEU   A HD13 
1229 H HD21 . LEU   A 93  ? 0.606786 0.590055 0.56068  -0.0031755  0.00668449  -0.152833   105 LEU   A HD21 
1230 H HD22 . LEU   A 93  ? 0.597386 0.597049 0.557134 -0.013157   0.024723    -0.160473   105 LEU   A HD22 
1231 H HD23 . LEU   A 93  ? 0.595505 0.598075 0.566884 -0.00508861 0.00242427  -0.161663   105 LEU   A HD23 
1232 N N    . LEU   A 94  ? 0.665314 0.616805 0.600876 -0.00545321 0.0586019   -0.139062   106 LEU   A N    
1233 C CA   . LEU   A 94  ? 0.640021 0.572672 0.568658 -0.00559177 0.0783976   -0.141631   106 LEU   A CA   
1234 C C    . LEU   A 94  ? 0.706535 0.638881 0.629769 -0.0258979  0.096377    -0.158235   106 LEU   A C    
1235 O O    . LEU   A 94  ? 0.69474  0.617267 0.604658 -0.0358503  0.104322    -0.164433   106 LEU   A O    
1236 C CB   . LEU   A 94  ? 0.714172 0.603707 0.617261 0.00937236  0.0852932   -0.131892   106 LEU   A CB   
1237 C CG   . LEU   A 94  ? 0.838348 0.696551 0.733354 0.0115278   0.107172    -0.136255   106 LEU   A CG   
1238 C CD1  . LEU   A 94  ? 0.749527 0.631535 0.671021 0.0274508   0.101645    -0.133998   106 LEU   A CD1  
1239 C CD2  . LEU   A 94  ? 0.901656 0.698393 0.758779 0.0212988   0.119675    -0.126091   106 LEU   A CD2  
1240 H H    . LEU   A 94  ? 0.647775 0.589885 0.570408 -0.0075154  0.0601609   -0.142005   106 LEU   A H    
1241 H HA   . LEU   A 94  ? 0.653021 0.603063 0.597902 -0.00271355 0.0756864   -0.14017    106 LEU   A HA   
1242 H HB2  . LEU   A 94  ? 0.722612 0.620168 0.632496 0.0231488   0.0710177   -0.122717   106 LEU   A HB2  
1243 H HB3  . LEU   A 94  ? 0.741901 0.613843 0.624933 0.00488116  0.0895841   -0.1319     106 LEU   A HB3  
1244 H HG   . LEU   A 94  ? 0.799796 0.662112 0.69642  -0.00520142 0.118546    -0.148889   106 LEU   A HG   
1245 H HD11 . LEU   A 94  ? 0.740478 0.65626  0.680192 0.0179685   0.0976223   -0.139371   106 LEU   A HD11 
1246 H HD12 . LEU   A 94  ? 0.79722  0.65609  0.712506 0.0317854   0.116       -0.138672   106 LEU   A HD12 
1247 H HD13 . LEU   A 94  ? 0.771421 0.6591   0.697795 0.0427895   0.0882316   -0.123167   106 LEU   A HD13 
1248 H HD21 . LEU   A 94  ? 0.911129 0.695416 0.751418 0.00749257  0.127348    -0.128567   106 LEU   A HD21 
1249 H HD22 . LEU   A 94  ? 0.909052 0.703466 0.761739 0.0392826   0.106391    -0.11338    106 LEU   A HD22 
1250 H HD23 . LEU   A 94  ? 0.926513 0.698277 0.779531 0.0233786   0.133474    -0.129918   106 LEU   A HD23 
1251 N N    . ILE   A 95  ? 0.579393 0.529652 0.514603 -0.0330158  0.102522    -0.167082   107 ILE   A N    
1252 C CA   . ILE   A 95  ? 0.595463 0.569717 0.535492 -0.052689   0.108486    -0.184553   107 ILE   A CA   
1253 C C    . ILE   A 95  ? 0.709244 0.662742 0.638625 -0.0640802  0.131017    -0.200795   107 ILE   A C    
1254 O O    . ILE   A 95  ? 0.704193 0.657073 0.635219 -0.0566657  0.135227    -0.201728   107 ILE   A O    
1255 C CB   . ILE   A 95  ? 0.53818  0.55657  0.495965 -0.0521919  0.0909063   -0.181123   107 ILE   A CB   
1256 C CG1  . ILE   A 95  ? 0.593795 0.62105  0.561715 -0.0414966  0.0691307   -0.166005   107 ILE   A CG1  
1257 C CG2  . ILE   A 95  ? 0.491921 0.54114  0.45262  -0.0689163  0.0925008   -0.19889    107 ILE   A CG2  
1258 C CD1  . ILE   A 95  ? 0.593812 0.65039  0.574717 -0.041068   0.0530716   -0.156215   107 ILE   A CD1  
1259 H H    . ILE   A 95  ? 0.61271  0.563301 0.552988 -0.0248725  0.102738    -0.163135   107 ILE   A H    
1260 H HA   . ILE   A 95  ? 0.601235 0.5764   0.538926 -0.059039   0.109228    -0.188678   107 ILE   A HA   
1261 H HB   . ILE   A 95  ? 0.550759 0.570853 0.510174 -0.0479956  0.0934083   -0.177845   107 ILE   A HB   
1262 H HG12 . ILE   A 95  ? 0.577094 0.605897 0.544257 -0.0438847  0.0669684   -0.171106   107 ILE   A HG12 
1263 H HG13 . ILE   A 95  ? 0.583627 0.593802 0.549041 -0.0324433  0.0677218   -0.157662   107 ILE   A HG13 
1264 H HG21 . ILE   A 95  ? 0.49094  0.565126 0.459244 -0.0662804  0.0782913   -0.193283   107 ILE   A HG21 
1265 H HG22 . ILE   A 95  ? 0.509592 0.556741 0.470261 -0.0754001  0.0966125   -0.206855   107 ILE   A HG22 
1266 H HG23 . ILE   A 95  ? 0.51991  0.567147 0.474607 -0.0757489  0.103431    -0.208632   107 ILE   A HG23 
1267 H HD11 . ILE   A 95  ? 0.591159 0.653198 0.572204 -0.0420842  0.0591699   -0.15437    107 ILE   A HD11 
1268 H HD12 . ILE   A 95  ? 0.5823   0.635159 0.569341 -0.0348674  0.0410504   -0.146275   107 ILE   A HD12 
1269 H HD13 . ILE   A 95  ? 0.583538 0.65693  0.565535 -0.0461261  0.0489      -0.161735   107 ILE   A HD13 
1270 N N    . LYS   A 96  ? 0.783794 0.718909 0.702739 -0.0830318  0.147476    -0.215226   108 LYS   A N    
1271 C CA   . LYS   A 96  ? 0.843046 0.75747  0.752902 -0.101162   0.168698    -0.236679   108 LYS   A CA   
1272 C C    . LYS   A 96  ? 0.743157 0.712486 0.666973 -0.114062   0.160354    -0.255142   108 LYS   A C    
1273 O O    . LYS   A 96  ? 0.701782 0.720404 0.64115  -0.113862   0.141176    -0.25215    108 LYS   A O    
1274 C CB   . LYS   A 96  ? 0.881562 0.767464 0.78011  -0.125071   0.188518    -0.247275   108 LYS   A CB   
1275 C CG   . LYS   A 96  ? 1.04772  0.865789 0.918262 -0.117284   0.203081    -0.229638   108 LYS   A CG   
1276 C CD   . LYS   A 96  ? 1.1996   0.957498 1.05079  -0.0961348  0.211283    -0.219515   108 LYS   A CD   
1277 C CE   . LYS   A 96  ? 1.21779  0.915533 1.03749  -0.0810431  0.216955    -0.194201   108 LYS   A CE   
1278 N NZ   . LYS   A 96  ? 1.15985  0.885203 0.98383  -0.0548906  0.191755    -0.172068   108 LYS   A NZ   
1279 H H    . LYS   A 96  ? 0.772721 0.708185 0.690391 -0.0863106  0.146485    -0.213026   108 LYS   A H    
1280 H HA   . LYS   A 96  ? 0.846054 0.73046  0.747196 -0.0898857  0.175527    -0.232769   108 LYS   A HA   
1281 H HB2  . LYS   A 96  ? 0.882585 0.802933 0.793323 -0.131507   0.180949    -0.249494   108 LYS   A HB2  
1282 H HB3  . LYS   A 96  ? 0.927104 0.808304 0.824468 -0.142489   0.200304    -0.265862   108 LYS   A HB3  
1283 H HG2  . LYS   A 96  ? 1.02044  0.849004 0.891072 -0.104937   0.191498    -0.215117   108 LYS   A HG2  
1284 H HG3  . LYS   A 96  ? 1.06718  0.869019 0.93016  -0.138398   0.219181    -0.238624   108 LYS   A HG3  
1285 H HD2  . LYS   A 96  ? 1.19847  0.933389 1.04442  -0.109347   0.226476    -0.235175   108 LYS   A HD2  
1286 H HD3  . LYS   A 96  ? 1.13725  0.918552 1.00079  -0.0782208  0.197686    -0.214286   108 LYS   A HD3  
1287 H HE2  . LYS   A 96  ? 1.24114  0.923495 1.04853  -0.100518   0.229921    -0.196822   108 LYS   A HE2  
1288 H HE3  . LYS   A 96  ? 1.25847  0.911337 1.06459  -0.0697435  0.225354    -0.190442   108 LYS   A HE3  
1289 H HZ1  . LYS   A 96  ? 1.14218  0.895402 0.971936 -0.0644173  0.18688     -0.17421    108 LYS   A HZ1  
1290 H HZ2  . LYS   A 96  ? 1.13837  0.889739 0.98007  -0.0422722  0.179456    -0.171814   108 LYS   A HZ2  
1291 H HZ3  . LYS   A 96  ? 1.19875  0.887368 1.00138  -0.0419904  0.193321    -0.157156   108 LYS   A HZ3  
1292 N N    . PRO   A 97  ? 0.79955  0.758862 0.714419 -0.12498    0.174307    -0.276044   109 PRO   A N    
1293 C CA   . PRO   A 97  ? 0.741635 0.752594 0.660188 -0.136063   0.165912    -0.294222   109 PRO   A CA   
1294 C C    . PRO   A 97  ? 0.723307 0.786788 0.655307 -0.157378   0.154721    -0.310787   109 PRO   A C    
1295 O O    . PRO   A 97  ? 0.655711 0.772132 0.59081  -0.157118   0.136815    -0.314305   109 PRO   A O    
1296 C CB   . PRO   A 97  ? 0.785955 0.763223 0.687207 -0.146724   0.188073    -0.320066   109 PRO   A CB   
1297 C CG   . PRO   A 97  ? 0.864917 0.766383 0.755341 -0.144876   0.209149    -0.315851   109 PRO   A CG   
1298 C CD   . PRO   A 97  ? 0.854741 0.746863 0.750774 -0.123158   0.198139    -0.282409   109 PRO   A CD   
1299 H HA   . PRO   A 97  ? 0.72635  0.75841  0.647734 -0.12185    0.154193    -0.280813   109 PRO   A HA   
1300 H HB2  . PRO   A 97  ? 0.807708 0.805071 0.708209 -0.167046   0.189342    -0.341951   109 PRO   A HB2  
1301 H HB3  . PRO   A 97  ? 0.795108 0.778109 0.691916 -0.133891   0.187511    -0.317223   109 PRO   A HB3  
1302 H HG2  . PRO   A 97  ? 0.882336 0.771642 0.770584 -0.16706    0.218895    -0.330611   109 PRO   A HG2  
1303 H HG3  . PRO   A 97  ? 0.888577 0.758363 0.768945 -0.135688   0.220386    -0.32065    109 PRO   A HG3  
1304 H HD2  . PRO   A 97  ? 0.873246 0.731612 0.761595 -0.13       0.207847    -0.279724   109 PRO   A HD2  
1305 H HD3  . PRO   A 97  ? 0.849287 0.728842 0.744097 -0.10188    0.196173    -0.269395   109 PRO   A HD3  
1306 N N    . GLU   A 98  ? 0.740075 0.791934 0.679821 -0.175208   0.165483    -0.320232   110 GLU   A N    
1307 C CA   . GLU   A 98  ? 0.794198 0.90559  0.756766 -0.192804   0.15519     -0.336645   110 GLU   A CA   
1308 C C    . GLU   A 98  ? 0.747907 0.90791  0.727003 -0.169057   0.126229    -0.31621    110 GLU   A C    
1309 O O    . GLU   A 98  ? 0.737048 0.958936 0.733598 -0.172946   0.108328    -0.32785    110 GLU   A O    
1310 C CB   . GLU   A 98  ? 0.830252 0.916171 0.798442 -0.217408   0.178535    -0.348117   110 GLU   A CB   
1311 C CG   . GLU   A 98  ? 0.931456 0.963667 0.881498 -0.245244   0.206505    -0.37112    110 GLU   A CG   
1312 C CD   . GLU   A 98  ? 1.02561  0.964936 0.944282 -0.232172   0.22678     -0.354536   110 GLU   A CD   
1313 O OE1  . GLU   A 98  ? 0.996453 0.915407 0.908069 -0.202528   0.219407    -0.323496   110 GLU   A OE1  
1314 O OE2  . GLU   A 98  ? 1.09885  0.983296 0.999852 -0.249412   0.248876    -0.372602   110 GLU   A OE2  
1315 H H    . GLU   A 98  ? 0.775901 0.783372 0.706963 -0.175728   0.179927    -0.315657   110 GLU   A H    
1316 H HA   . GLU   A 98  ? 0.79362  0.929754 0.755534 -0.205935   0.153152    -0.356369   110 GLU   A HA   
1317 H HB2  . GLU   A 98  ? 0.833036 0.889956 0.795232 -0.204836   0.182238    -0.328984   110 GLU   A HB2  
1318 H HB3  . GLU   A 98  ? 0.825059 0.958502 0.814374 -0.228216   0.172172    -0.359931   110 GLU   A HB3  
1319 H HG2  . GLU   A 98  ? 0.9501   0.988281 0.910258 -0.269413   0.218159    -0.384987   110 GLU   A HG2  
1320 H HG3  . GLU   A 98  ? 0.937876 0.99216  0.887141 -0.251456   0.200785    -0.388062   110 GLU   A HG3  
1321 N N    . TYR   A 99  ? 0.653174 0.784349 0.626815 -0.143914   0.120087    -0.286928   111 TYR   A N    
1322 C CA   . TYR   A 99  ? 0.676879 0.838213 0.663387 -0.122344   0.094514    -0.267734   111 TYR   A CA   
1323 C C    . TYR   A 99  ? 0.593464 0.757031 0.568404 -0.107323   0.0805123   -0.249331   111 TYR   A C    
1324 O O    . TYR   A 99  ? 0.628632 0.793818 0.607702 -0.089328   0.063031    -0.226803   111 TYR   A O    
1325 C CB   . TYR   A 99  ? 0.630725 0.76287  0.620034 -0.111548   0.098352    -0.254158   111 TYR   A CB   
1326 C CG   . TYR   A 99  ? 0.680811 0.824781 0.68191  -0.129275   0.113827    -0.272857   111 TYR   A CG   
1327 C CD1  . TYR   A 99  ? 0.734321 0.935731 0.763789 -0.129195   0.102616    -0.285495   111 TYR   A CD1  
1328 C CD2  . TYR   A 99  ? 0.757604 0.855543 0.741834 -0.146702   0.141692    -0.278005   111 TYR   A CD2  
1329 C CE1  . TYR   A 99  ? 0.728641 0.950296 0.774097 -0.148482   0.12093     -0.304897   111 TYR   A CE1  
1330 C CE2  . TYR   A 99  ? 0.815784 0.923588 0.808767 -0.169667   0.161159    -0.294563   111 TYR   A CE2  
1331 C CZ   . TYR   A 99  ? 0.823851 0.998055 0.849766 -0.17176    0.151894    -0.308929   111 TYR   A CZ   
1332 O OH   . TYR   A 99  ? 0.705385 0.89019  0.741059 -0.197016   0.17637     -0.325038   111 TYR   A OH   
1333 H H    . TYR   A 99  ? 0.694778 0.784841 0.656441 -0.140256   0.13172     -0.279607   111 TYR   A H    
1334 H HA   . TYR   A 99  ? 0.639033 0.841274 0.639662 -0.126776   0.0848772   -0.278511   111 TYR   A HA   
1335 H HB2  . TYR   A 99  ? 0.658143 0.751521 0.633212 -0.107785   0.107616    -0.245003   111 TYR   A HB2  
1336 H HB3  . TYR   A 99  ? 0.629694 0.774279 0.626085 -0.0965134  0.0816891   -0.242346   111 TYR   A HB3  
1337 H HD1  . TYR   A 99  ? 0.697648 0.925297 0.736482 -0.114989   0.0827636   -0.280267   111 TYR   A HD1  
1338 H HD2  . TYR   A 99  ? 0.769997 0.828847 0.736372 -0.143741   0.148678    -0.270253   111 TYR   A HD2  
1339 H HE1  . TYR   A 99  ? 0.734468 1.00127  0.803779 -0.145873   0.11322     -0.314763   111 TYR   A HE1  
1340 H HE2  . TYR   A 99  ? 0.838777 0.907747 0.815628 -0.182454   0.1812      -0.294777   111 TYR   A HE2  
1342 N N    . ALA   A 100 ? 0.631769 0.792965 0.590818 -0.116253   0.0903743   -0.259532   112 ALA   A N    
1343 C CA   . ALA   A 100 ? 0.582452 0.745881 0.528958 -0.104684   0.0843891   -0.242343   112 ALA   A CA   
1344 C C    . ALA   A 100 ? 0.692841 0.888451 0.621747 -0.116969   0.084952    -0.260306   112 ALA   A C    
1345 O O    . ALA   A 100 ? 0.712129 0.951213 0.642098 -0.118566   0.0649915   -0.261922   112 ALA   A O    
1346 C CB   . ALA   A 100 ? 0.546256 0.665166 0.489472 -0.0944276  0.09987     -0.231191   112 ALA   A CB   
1347 H H    . ALA   A 100 ? 0.635388 0.79443  0.591125 -0.130862   0.10211     -0.278589   112 ALA   A H    
1348 H HA   . ALA   A 100 ? 0.584806 0.76178  0.536938 -0.0947527  0.0678705   -0.225772   112 ALA   A HA   
1349 H HB1  . ALA   A 100 ? 0.54285  0.649918 0.494686 -0.0850695  0.0934068   -0.216939   112 ALA   A HB1  
1350 H HB2  . ALA   A 100 ? 0.576809 0.672205 0.515128 -0.100949   0.115586    -0.244945   112 ALA   A HB2  
1351 H HB3  . ALA   A 100 ? 0.561473 0.688013 0.498747 -0.0902458  0.100411    -0.224999   112 ALA   A HB3  
1352 N N    . TYR   A 101 ? 0.637032 0.81228  0.549494 -0.123147   0.106148    -0.275238   113 TYR   A N    
1353 C CA   . TYR   A 101 ? 0.738055 0.9442   0.626942 -0.134751   0.10772     -0.295448   113 TYR   A CA   
1354 C C    . TYR   A 101 ? 0.68509  0.877962 0.566828 -0.157089   0.125772    -0.33558    113 TYR   A C    
1355 O O    . TYR   A 101 ? 0.680356 0.891914 0.539798 -0.168329   0.130132    -0.359079   113 TYR   A O    
1356 C CB   . TYR   A 101 ? 0.685211 0.890238 0.556011 -0.124353   0.11745     -0.283898   113 TYR   A CB   
1357 C CG   . TYR   A 101 ? 0.703503 0.92307  0.580203 -0.109862   0.0999912   -0.245294   113 TYR   A CG   
1358 C CD1  . TYR   A 101 ? 0.692325 0.950369 0.551645 -0.110714   0.079292    -0.231402   113 TYR   A CD1  
1359 C CD2  . TYR   A 101 ? 0.704583 0.896736 0.602329 -0.0960501  0.102793    -0.222589   113 TYR   A CD2  
1360 C CE1  . TYR   A 101 ? 0.651453 0.911225 0.512596 -0.100367   0.0653411   -0.19524    113 TYR   A CE1  
1361 C CE2  . TYR   A 101 ? 0.690147 0.891576 0.59434  -0.0881897  0.0875359   -0.190776   113 TYR   A CE2  
1362 C CZ   . TYR   A 101 ? 0.678388 0.909111 0.563721 -0.091336   0.0703648   -0.17626    113 TYR   A CZ   
1363 O OH   . TYR   A 101 ? 0.568876 0.797349 0.457458 -0.0861109  0.05707     -0.142997   113 TYR   A OH   
1364 H H    . TYR   A 101 ? 0.672563 0.814506 0.587023 -0.118629   0.119256    -0.273582   113 TYR   A H    
1365 H HA   . TYR   A 101 ? 0.689383 0.931341 0.576853 -0.1358     0.0893774   -0.291619   113 TYR   A HA   
1366 H HB2  . TYR   A 101 ? 0.714683 0.887898 0.589998 -0.119447   0.134139    -0.287581   113 TYR   A HB2  
1367 H HB3  . TYR   A 101 ? 0.732134 0.959042 0.582711 -0.132558   0.119033    -0.298758   113 TYR   A HB3  
1368 H HD1  . TYR   A 101 ? 0.708299 0.989894 0.551961 -0.118888   0.0745631   -0.246659   113 TYR   A HD1  
1369 H HD2  . TYR   A 101 ? 0.695917 0.861429 0.602826 -0.0925703  0.114536    -0.229242   113 TYR   A HD2  
1370 H HE1  . TYR   A 101 ? 0.68368  0.963259 0.52871  -0.100047   0.0515674   -0.183712   113 TYR   A HE1  
1371 H HE2  . TYR   A 101 ? 0.668255 0.854211 0.58789  -0.0809972  0.0887044   -0.178607   113 TYR   A HE2  
1373 N N    . GLY   A 102 ? 0.746948 0.9044   0.644977 -0.165248   0.137101    -0.343206   114 GLY   A N    
1374 C CA   . GLY   A 102 ? 0.74106  0.889484 0.638018 -0.193847   0.151022    -0.380284   114 GLY   A CA   
1375 C C    . GLY   A 102 ? 0.834104 0.939708 0.70701  -0.199908   0.175615    -0.404895   114 GLY   A C    
1376 O O    . GLY   A 102 ? 0.80667  0.892515 0.667481 -0.17836    0.183694    -0.392472   114 GLY   A O    
1377 H H    . GLY   A 102 ? 0.703593 0.840785 0.612181 -0.154555   0.136999    -0.325157   114 GLY   A H    
1378 H HA2  . GLY   A 102 ? 0.756983 0.881511 0.666502 -0.198974   0.158203    -0.378165   114 GLY   A HA2  
1379 H HA3  . GLY   A 102 ? 0.758872 0.9535   0.658516 -0.205015   0.137429    -0.393045   114 GLY   A HA3  
1380 N N    . SER   A 103 ? 0.836315 0.931672 0.705429 -0.230517   0.187765    -0.442945   115 SER   A N    
1381 C CA   . SER   A 103 ? 0.962662 1.01274  0.807582 -0.239173   0.211392    -0.474202   115 SER   A CA   
1382 C C    . SER   A 103 ? 0.887999 0.981444 0.707078 -0.230764   0.204486    -0.485262   115 SER   A C    
1383 O O    . SER   A 103 ? 0.942801 0.998664 0.742443 -0.220369   0.224977    -0.498233   115 SER   A O    
1384 C CB   . SER   A 103 ? 1.06384  1.08981  0.910819 -0.279059   0.225851    -0.514076   115 SER   A CB   
1385 O OG   . SER   A 103 ? 1.16797  1.24936  1.04213  -0.300966   0.209341    -0.516672   115 SER   A OG   
1386 H H    . SER   A 103 ? 0.854446 0.971626 0.737635 -0.246778   0.181767    -0.451178   115 SER   A H    
1387 H HA   . SER   A 103 ? 0.948003 0.947663 0.790984 -0.222518   0.225089    -0.460487   115 SER   A HA   
1388 H HB2  . SER   A 103 ? 1.1141   1.14749  0.944774 -0.290921   0.229309    -0.542984   115 SER   A HB2  
1389 H HB3  . SER   A 103 ? 1.10572  1.06814  0.950989 -0.27884    0.244838    -0.511396   115 SER   A HB3  
1391 N N    . ALA   A 104 ? 0.822035 0.992125 0.638707 -0.231264   0.176702    -0.477122   116 ALA   A N    
1392 C CA   . ALA   A 104 ? 0.868505 1.08125  0.651556 -0.225741   0.170335    -0.484304   116 ALA   A CA   
1393 C C    . ALA   A 104 ? 0.884318 1.0891   0.660411 -0.194704   0.176693    -0.449216   116 ALA   A C    
1394 O O    . ALA   A 104 ? 0.887516 1.1162   0.633123 -0.189731   0.181938    -0.455174   116 ALA   A O    
1395 C CB   . ALA   A 104 ? 0.876076 1.16759  0.655054 -0.232509   0.136441    -0.479778   116 ALA   A CB   
1396 H H    . ALA   A 104 ? 0.80993  1.00567  0.644195 -0.23433    0.161715    -0.466532   116 ALA   A H    
1397 H HA   . ALA   A 104 ? 0.919187 1.11629  0.684726 -0.238634   0.184533    -0.517167   116 ALA   A HA   
1398 H HB1  . ALA   A 104 ? 0.881872 1.18802  0.669681 -0.253028   0.131563    -0.504589   116 ALA   A HB1  
1399 H HB2  . ALA   A 104 ? 0.8297   1.13169  0.625313 -0.218677   0.12312     -0.448937   116 ALA   A HB2  
1400 H HB3  . ALA   A 104 ? 0.889634 1.20761  0.639962 -0.229744   0.132428    -0.483194   116 ALA   A HB3  
1401 N N    . GLY   A 105 ? 0.909549 1.09256  0.7143   -0.176112   0.173013    -0.411432   117 GLY   A N    
1402 C CA   . GLY   A 105 ? 0.802391 0.985936 0.610172 -0.150627   0.175676    -0.377188   117 GLY   A CA   
1403 C C    . GLY   A 105 ? 0.758766 1.00153  0.547674 -0.148631   0.154968    -0.35555    117 GLY   A C    
1404 O O    . GLY   A 105 ? 0.733853 1.01518  0.512555 -0.159582   0.132677    -0.358618   117 GLY   A O    
1405 H H    . GLY   A 105 ? 0.853836 1.02403  0.676973 -0.181007   0.168877    -0.408241   117 GLY   A H    
1406 H HA2  . GLY   A 105 ? 0.783362 0.946842 0.613233 -0.14094    0.17244     -0.356454   117 GLY   A HA2  
1407 H HA3  . GLY   A 105 ? 0.837854 1.00213  0.637568 -0.144372   0.194865    -0.388969   117 GLY   A HA3  
1408 N N    . SER   A 106 ? 0.809881 1.06027  0.594101 -0.134033   0.162917    -0.332291   118 SER   A N    
1409 C CA   . SER   A 106 ? 0.862709 1.15901  0.620925 -0.133955   0.149507    -0.308318   118 SER   A CA   
1410 C C    . SER   A 106 ? 0.84417  1.14553  0.592676 -0.125663   0.176091    -0.304929   118 SER   A C    
1411 O O    . SER   A 106 ? 0.76504  1.07013  0.53121  -0.116061   0.177481    -0.271999   118 SER   A O    
1412 C CB   . SER   A 106 ? 0.926003 1.22714  0.703915 -0.126104   0.12318     -0.266083   118 SER   A CB   
1413 O OG   . SER   A 106 ? 0.937629 1.26839  0.687815 -0.125164   0.115804    -0.236701   118 SER   A OG   
1414 H H    . SER   A 106 ? 0.802286 1.02843  0.600142 -0.123918   0.177729    -0.330232   118 SER   A H    
1415 H HA   . SER   A 106 ? 0.887078 1.20772  0.619404 -0.144607   0.141928    -0.324515   118 SER   A HA   
1416 H HB2  . SER   A 106 ? 0.891986 1.1992   0.674099 -0.130279   0.106662    -0.271139   118 SER   A HB2  
1417 H HB3  . SER   A 106 ? 0.873952 1.15052  0.678578 -0.117645   0.128285    -0.254781   118 SER   A HB3  
1419 N N    . LEU   A 107 ? 0.986043 1.28723  0.710304 -0.130602   0.198553    -0.344163   119 LEU   A N    
1420 C CA   . LEU   A 107 ? 1.02228  1.33663  0.734055 -0.122419   0.228375    -0.352258   119 LEU   A CA   
1421 C C    . LEU   A 107 ? 0.972335 1.33665  0.652174 -0.127867   0.223913    -0.321999   119 LEU   A C    
1422 O O    . LEU   A 107 ? 0.959586 1.34815  0.605585 -0.139381   0.200004    -0.310915   119 LEU   A O    
1423 C CB   . LEU   A 107 ? 1.083    1.38797  0.765823 -0.127767   0.251631    -0.405517   119 LEU   A CB   
1424 C CG   . LEU   A 107 ? 1.10083  1.34377  0.807678 -0.125103   0.261296    -0.437254   119 LEU   A CG   
1425 C CD1  . LEU   A 107 ? 1.11739  1.35142  0.789008 -0.13344    0.283027    -0.490298   119 LEU   A CD1  
1426 C CD2  . LEU   A 107 ? 1.13121  1.33344  0.883214 -0.0994549  0.275953    -0.422706   119 LEU   A CD2  
1427 H H    . LEU   A 107 ? 0.977669 1.27134  0.693621 -0.140094   0.195835    -0.369208   119 LEU   A H    
1428 H HA   . LEU   A 107 ? 0.986548 1.28256  0.730517 -0.109051   0.23765     -0.341984   119 LEU   A HA   
1429 H HB2  . LEU   A 107 ? 1.10796  1.43608  0.757738 -0.142032   0.240688    -0.41682    119 LEU   A HB2  
1430 H HB3  . LEU   A 107 ? 1.10452  1.42258  0.780834 -0.119714   0.272585    -0.409998   119 LEU   A HB3  
1431 H HG   . LEU   A 107 ? 1.07962  1.31421  0.792481 -0.136073   0.242804    -0.434719   119 LEU   A HG   
1432 H HD11 . LEU   A 107 ? 1.14976  1.41626  0.789773 -0.149248   0.272121    -0.499747   119 LEU   A HD11 
1433 H HD12 . LEU   A 107 ? 1.14396  1.33422  0.825878 -0.136576   0.287548    -0.511121   119 LEU   A HD12 
1434 H HD13 . LEU   A 107 ? 1.15212  1.3915   0.821222 -0.120044   0.303921    -0.495858   119 LEU   A HD13 
1435 H HD21 . LEU   A 107 ? 1.06957  1.27636  0.843094 -0.0958229  0.26078     -0.391392   119 LEU   A HD21 
1436 H HD22 . LEU   A 107 ? 1.12971  1.34624  0.881799 -0.0872936  0.293848    -0.425694   119 LEU   A HD22 
1437 H HD23 . LEU   A 107 ? 1.13126  1.28916  0.890118 -0.0984461  0.282498    -0.442123   119 LEU   A HD23 
1438 N N    . PRO   A 108 ? 0.976957 1.35977  0.664594 -0.119833   0.248688    -0.309406   120 PRO   A N    
1439 C CA   . PRO   A 108 ? 0.965288 1.32783  0.695879 -0.101005   0.274819    -0.32443    120 PRO   A CA   
1440 C C    . PRO   A 108 ? 0.889786 1.23073  0.678433 -0.08762    0.264232    -0.29393    120 PRO   A C    
1441 O O    . PRO   A 108 ? 0.882303 1.21038  0.706532 -0.0683027  0.282287    -0.304665   120 PRO   A O    
1442 C CB   . PRO   A 108 ? 1.05489  1.46445  0.770205 -0.0997622  0.305309    -0.324853   120 PRO   A CB   
1443 C CG   . PRO   A 108 ? 1.05316  1.49375  0.743648 -0.117166   0.28689     -0.27929    120 PRO   A CG   
1444 C CD   . PRO   A 108 ? 1.02478  1.45279  0.677692 -0.128865   0.254791    -0.28198    120 PRO   A CD   
1445 H HA   . PRO   A 108 ? 0.991232 1.32901  0.719008 -0.0978019  0.282333    -0.355873   120 PRO   A HA   
1446 H HB2  . PRO   A 108 ? 1.02786  1.43895  0.78005  -0.0862118  0.319503    -0.322087   120 PRO   A HB2  
1447 H HB3  . PRO   A 108 ? 1.08522  1.50264  0.768378 -0.102583   0.319361    -0.354357   120 PRO   A HB3  
1448 H HG2  . PRO   A 108 ? 1.00804  1.44277  0.73253  -0.114368   0.278333    -0.252149   120 PRO   A HG2  
1449 H HG3  . PRO   A 108 ? 1.07829  1.55177  0.742459 -0.123344   0.304142    -0.277324   120 PRO   A HG3  
1450 H HD2  . PRO   A 108 ? 1.01043  1.43919  0.663309 -0.133362   0.23445     -0.250218   120 PRO   A HD2  
1451 H HD3  . PRO   A 108 ? 1.07052  1.5179   0.679775 -0.136626   0.259756    -0.29931    120 PRO   A HD3  
1452 N N    . LYS   A 109 ? 0.839837 1.1748   0.636873 -0.0950593  0.234239    -0.26006    121 LYS   A N    
1453 C CA   . LYS   A 109 ? 0.816411 1.13562  0.6624   -0.0849722  0.222936    -0.231938   121 LYS   A CA   
1454 C C    . LYS   A 109 ? 0.831886 1.1013   0.704424 -0.0710398  0.218562    -0.248675   121 LYS   A C    
1455 O O    . LYS   A 109 ? 0.81801  1.07459  0.727189 -0.0527322  0.226722    -0.246614   121 LYS   A O    
1456 C CB   . LYS   A 109 ? 0.842087 1.16732  0.682036 -0.0972169  0.194785    -0.193415   121 LYS   A CB   
1457 H H    . LYS   A 109 ? 0.856642 1.1981   0.627577 -0.105693   0.219758    -0.255972   121 LYS   A H    
1458 H HA   . LYS   A 109 ? 0.82695  1.16531  0.691574 -0.0789199  0.238349    -0.227186   121 LYS   A HA   
1461 N N    . ILE   A 110 ? 0.723818 0.967903 0.5774   -0.0802066  0.205625    -0.264284   122 ILE   A N    
1462 C CA   . ILE   A 110 ? 0.694281 0.888996 0.565906 -0.0739654  0.201175    -0.274581   122 ILE   A CA   
1463 C C    . ILE   A 110 ? 0.751826 0.918589 0.60192  -0.0795248  0.218802    -0.31663    122 ILE   A C    
1464 O O    . ILE   A 110 ? 0.780837 0.966195 0.599949 -0.0981208  0.215617    -0.33688    122 ILE   A O    
1465 C CB   . ILE   A 110 ? 0.678646 0.870037 0.55179  -0.0847696  0.172636    -0.258283   122 ILE   A CB   
1466 C CG1  . ILE   A 110 ? 0.656336 0.875194 0.536991 -0.0848108  0.153982    -0.221597   122 ILE   A CG1  
1467 C CG2  . ILE   A 110 ? 0.638771 0.783056 0.532765 -0.0784298  0.169753    -0.259977   122 ILE   A CG2  
1468 C CD1  . ILE   A 110 ? 0.674716 0.883933 0.591272 -0.0706089  0.154391    -0.199474   122 ILE   A CD1  
1469 H H    . ILE   A 110 ? 0.758565 1.01945  0.585956 -0.0919453  0.199668    -0.268413   122 ILE   A H    
1470 H HA   . ILE   A 110 ? 0.692502 0.873739 0.588367 -0.0597407  0.205161    -0.265546   122 ILE   A HA   
1471 H HB   . ILE   A 110 ? 0.68778  0.889973 0.540205 -0.09692    0.168911    -0.272903   122 ILE   A HB   
1472 H HG12 . ILE   A 110 ? 0.682336 0.928042 0.54477  -0.0902582  0.15801     -0.218605   122 ILE   A HG12 
1473 H HG13 . ILE   A 110 ? 0.652287 0.869723 0.531378 -0.0895329  0.136552    -0.215151   122 ILE   A HG13 
1474 H HG21 . ILE   A 110 ? 0.62405  0.771737 0.523899 -0.0820245  0.153009    -0.246801   122 ILE   A HG21 
1475 H HG22 . ILE   A 110 ? 0.641383 0.771775 0.551824 -0.0644448  0.175911    -0.251776   122 ILE   A HG22 
1476 H HG23 . ILE   A 110 ? 0.669015 0.793588 0.55292  -0.0848726  0.178823    -0.282719   122 ILE   A HG23 
1477 H HD11 . ILE   A 110 ? 0.643311 0.828626 0.572608 -0.0661693  0.145093    -0.1966     122 ILE   A HD11 
1478 H HD12 . ILE   A 110 ? 0.653797 0.882114 0.572524 -0.0744691  0.146831    -0.179073   122 ILE   A HD12 
1479 H HD13 . ILE   A 110 ? 0.671807 0.880718 0.596266 -0.0621886  0.171199    -0.209036   122 ILE   A HD13 
1480 N N    . PRO   A 111 ? 0.774281 0.892093 0.637903 -0.0641693  0.236302    -0.332145   123 PRO   A N    
1481 C CA   . PRO   A 111 ? 0.803524 0.87917  0.646131 -0.0727408  0.253117    -0.37249    123 PRO   A CA   
1482 C C    . PRO   A 111 ? 0.745677 0.791972 0.58395  -0.0946823  0.240792    -0.379766   123 PRO   A C    
1483 O O    . PRO   A 111 ? 0.698434 0.757466 0.550589 -0.0988799  0.219942    -0.35428    123 PRO   A O    
1484 C CB   . PRO   A 111 ? 0.855657 0.882616 0.714379 -0.044225   0.275055    -0.380279   123 PRO   A CB   
1485 C CG   . PRO   A 111 ? 0.872049 0.91055  0.76612  -0.0233063  0.260899    -0.339489   123 PRO   A CG   
1486 C CD   . PRO   A 111 ? 0.790594 0.890837 0.688353 -0.0372438  0.239867    -0.312166   123 PRO   A CD   
1487 H HA   . PRO   A 111 ? 0.824554 0.92455  0.645565 -0.0815014  0.259878    -0.391088   123 PRO   A HA   
1488 H HB2  . PRO   A 111 ? 0.891399 0.868508 0.744384 -0.0473159  0.280811    -0.393983   123 PRO   A HB2  
1489 H HB3  . PRO   A 111 ? 0.890656 0.93174  0.74309  -0.0363829  0.290749    -0.396304   123 PRO   A HB3  
1490 H HG2  . PRO   A 111 ? 0.844474 0.845853 0.74382  -0.0214172  0.254158    -0.33112    123 PRO   A HG2  
1491 H HG3  . PRO   A 111 ? 0.859824 0.901856 0.76857  -0.0024068  0.272111    -0.339693   123 PRO   A HG3  
1492 H HD2  . PRO   A 111 ? 0.758755 0.851669 0.669258 -0.0371307  0.22405     -0.291891   123 PRO   A HD2  
1493 H HD3  . PRO   A 111 ? 0.783519 0.917287 0.690974 -0.0292857  0.245236    -0.304417   123 PRO   A HD3  
1494 N N    . SER   A 112 ? 0.821642 0.837076 0.639746 -0.112241   0.254352    -0.418563   124 SER   A N    
1495 C CA   . SER   A 112 ? 0.844022 0.833706 0.661757 -0.138581   0.248396    -0.431523   124 SER   A CA   
1496 C C    . SER   A 112 ? 0.812976 0.75086  0.65148  -0.126896   0.248524    -0.405279   124 SER   A C    
1497 O O    . SER   A 112 ? 0.874525 0.765968 0.718548 -0.100977   0.261708    -0.395398   124 SER   A O    
1498 C CB   . SER   A 112 ? 0.911833 0.859147 0.707726 -0.15902    0.269335    -0.47965    124 SER   A CB   
1499 O OG   . SER   A 112 ? 0.917111 0.809505 0.720923 -0.177698   0.274372    -0.484394   124 SER   A OG   
1500 H H    . SER   A 112 ? 0.854614 0.865875 0.659434 -0.109213   0.269123    -0.439726   124 SER   A H    
1501 H HA   . SER   A 112 ? 0.811548 0.845381 0.629193 -0.151521   0.230724    -0.426514   124 SER   A HA   
1502 H HB2  . SER   A 112 ? 0.918384 0.904678 0.699911 -0.176071   0.262973    -0.498878   124 SER   A HB2  
1503 H HB3  . SER   A 112 ? 0.941157 0.859492 0.731205 -0.142741   0.286229    -0.488708   124 SER   A HB3  
1505 N N    . ASN   A 113 ? 0.831598 0.781236 0.680488 -0.144118   0.233358    -0.394531   125 ASN   A N    
1506 C CA   . ASN   A 113 ? 0.874796 0.774276 0.734162 -0.139572   0.236176    -0.374501   125 ASN   A CA   
1507 C C    . ASN   A 113 ? 0.816351 0.708685 0.688688 -0.10415    0.229286    -0.337573   125 ASN   A C    
1508 O O    . ASN   A 113 ? 0.936978 0.770818 0.807444 -0.0899146  0.238343    -0.32524    125 ASN   A O    
1509 C CB   . ASN   A 113 ? 0.91874  0.73598  0.762712 -0.150422   0.262568    -0.396771   125 ASN   A CB   
1510 C CG   . ASN   A 113 ? 1.00182  0.823489 0.841929 -0.193752   0.267209    -0.428309   125 ASN   A CG   
1511 O OD1  . ASN   A 113 ? 1.06023  0.927769 0.915857 -0.21118    0.252256    -0.422078   125 ASN   A OD1  
1512 N ND2  . ASN   A 113 ? 1.10425  0.883899 0.926716 -0.211768   0.287484    -0.465894   125 ASN   A ND2  
1513 H H    . ASN   A 113 ? 0.812212 0.804245 0.660625 -0.158228   0.220947    -0.399895   125 ASN   A H    
1514 H HA   . ASN   A 113 ? 0.832095 0.755332 0.699425 -0.15369    0.225035    -0.370396   125 ASN   A HA   
1515 H HB2  . ASN   A 113 ? 0.969542 0.76776  0.804277 -0.140035   0.274169    -0.410405   125 ASN   A HB2  
1516 H HB3  . ASN   A 113 ? 0.943025 0.720908 0.788334 -0.139518   0.265805    -0.377466   125 ASN   A HB3  
1517 H HD21 . ASN   A 113 ? 1.10301  0.90908  0.923763 -0.23552    0.285584    -0.490371   125 ASN   A HD21 
1518 H HD22 . ASN   A 113 ? 1.13201  0.856507 0.944329 -0.199599   0.302374    -0.467627   125 ASN   A HD22 
1519 N N    . ALA   A 114 ? 0.751659 0.701041 0.635657 -0.090812   0.212993    -0.319178   126 ALA   A N    
1520 C CA   . ALA   A 114 ? 0.737172 0.684864 0.638887 -0.0619435  0.20507     -0.287351   126 ALA   A CA   
1521 C C    . ALA   A 114 ? 0.699682 0.644929 0.610611 -0.0632972  0.187426    -0.263487   126 ALA   A C    
1522 O O    . ALA   A 114 ? 0.690646 0.670232 0.603868 -0.080526   0.173806    -0.263854   126 ALA   A O    
1523 C CB   . ALA   A 114 ? 0.672486 0.678077 0.585303 -0.0522397  0.196964    -0.275778   126 ALA   A CB   
1524 H H    . ALA   A 114 ? 0.747709 0.736622 0.628139 -0.100363   0.206353    -0.325814   126 ALA   A H    
1525 H HA   . ALA   A 114 ? 0.759037 0.667267 0.65888  -0.0475112  0.21753     -0.289656   126 ALA   A HA   
1526 H HB1  . ALA   A 114 ? 0.706711 0.717801 0.611453 -0.051612   0.209905    -0.292348   126 ALA   A HB1  
1527 H HB2  . ALA   A 114 ? 0.658363 0.696167 0.570549 -0.0638699  0.183541    -0.269713   126 ALA   A HB2  
1528 H HB3  . ALA   A 114 ? 0.668596 0.674172 0.596652 -0.0353647  0.19266     -0.258079   126 ALA   A HB3  
1529 N N    . THR   A 115 ? 0.774425 0.680277 0.688563 -0.0426158  0.187884    -0.245133   127 THR   A N    
1530 C CA   . THR   A 115 ? 0.726364 0.636675 0.649266 -0.03379    0.169336    -0.219085   127 THR   A CA   
1531 C C    . THR   A 115 ? 0.71279  0.668458 0.65891  -0.0176094  0.152302    -0.200524   127 THR   A C    
1532 O O    . THR   A 115 ? 0.738403 0.700922 0.696312 0.0006088   0.157986    -0.198925   127 THR   A O    
1533 C CB   . THR   A 115 ? 0.764798 0.612494 0.673174 -0.0182734  0.176501    -0.207795   127 THR   A CB   
1534 O OG1  . THR   A 115 ? 0.767062 0.570077 0.653435 -0.0401306  0.195353    -0.224059   127 THR   A OG1  
1535 C CG2  . THR   A 115 ? 0.761602 0.611923 0.669513 -0.0128454  0.158375    -0.185414   127 THR   A CG2  
1536 H H    . THR   A 115 ? 0.786317 0.658705 0.694608 -0.0321687  0.200393    -0.250363   127 THR   A H    
1537 H HA   . THR   A 115 ? 0.718495 0.64264  0.640236 -0.0491398  0.163076    -0.221075   127 THR   A HA   
1538 H HB   . THR   A 115 ? 0.779639 0.61289  0.690727 0.00108371  0.181097    -0.20524    127 THR   A HB   
1540 H HG21 . THR   A 115 ? 0.78675  0.598082 0.680687 -0.00100562 0.162286    -0.176469   127 THR   A HG21 
1541 H HG22 . THR   A 115 ? 0.745526 0.603379 0.64957  -0.0303085  0.15782     -0.190409   127 THR   A HG22 
1542 H HG23 . THR   A 115 ? 0.726099 0.609577 0.650602 -0.00374813 0.143735    -0.175987   127 THR   A HG23 
1543 N N    . LEU   A 116 ? 0.765774 0.749374 0.72064  -0.0238968  0.131947    -0.18675    128 LEU   A N    
1544 C CA   . LEU   A 116 ? 0.670581 0.694576 0.646527 -0.0182515  0.114851    -0.169904   128 LEU   A CA   
1545 C C    . LEU   A 116 ? 0.671036 0.68407  0.65267  -0.00936273 0.0966944   -0.153474   128 LEU   A C    
1546 O O    . LEU   A 116 ? 0.654045 0.643765 0.62116  -0.0139559  0.0941518   -0.154954   128 LEU   A O    
1547 C CB   . LEU   A 116 ? 0.627565 0.689412 0.604158 -0.0350119  0.104412    -0.168711   128 LEU   A CB   
1548 C CG   . LEU   A 116 ? 0.647623 0.727381 0.609021 -0.0490109  0.116012    -0.186678   128 LEU   A CG   
1549 C CD1  . LEU   A 116 ? 0.637644 0.757187 0.599312 -0.0566557  0.1025      -0.173758   128 LEU   A CD1  
1550 C CD2  . LEU   A 116 ? 0.654088 0.725925 0.611968 -0.0420851  0.137622    -0.200287   128 LEU   A CD2  
1551 H H    . LEU   A 116 ? 0.724738 0.699803 0.672325 -0.0330925  0.129547    -0.188892   128 LEU   A H    
1552 H HA   . LEU   A 116 ? 0.684863 0.718161 0.670536 -0.00858149 0.120824    -0.169077   128 LEU   A HA   
1553 H HB2  . LEU   A 116 ? 0.624144 0.681369 0.598485 -0.0392276  0.0945689   -0.166508   128 LEU   A HB2  
1554 H HB3  . LEU   A 116 ? 0.621872 0.703664 0.610989 -0.0322897  0.0967452   -0.156477   128 LEU   A HB3  
1555 H HG   . LEU   A 116 ? 0.648671 0.718643 0.601158 -0.0576107  0.117249    -0.197918   128 LEU   A HG   
1556 H HD11 . LEU   A 116 ? 0.622783 0.742154 0.588484 -0.0574602  0.0878029   -0.164648   128 LEU   A HD11 
1557 H HD12 . LEU   A 116 ? 0.648657 0.782051 0.596323 -0.0652481  0.106753    -0.184625   128 LEU   A HD12 
1558 H HD13 . LEU   A 116 ? 0.634908 0.765873 0.605618 -0.0521801  0.104438    -0.163792   128 LEU   A HD13 
1559 H HD21 . LEU   A 116 ? 0.680443 0.721699 0.62997  -0.0418676  0.147428    -0.21234    128 LEU   A HD21 
1560 H HD22 . LEU   A 116 ? 0.656658 0.732037 0.628741 -0.0295877  0.137666    -0.190217   128 LEU   A HD22 
1561 H HD23 . LEU   A 116 ? 0.668378 0.762233 0.6176   -0.0499271  0.142505    -0.208244   128 LEU   A HD23 
1562 N N    . PHE   A 117 ? 0.557822 0.595276 0.561786 0.00011581  0.08462     -0.140106   129 PHE   A N    
1563 C CA   . PHE   A 117 ? 0.528053 0.565267 0.540443 0.00633324  0.0638093   -0.127267   129 PHE   A CA   
1564 C C    . PHE   A 117 ? 0.562993 0.634659 0.595709 -0.00581306 0.0492247   -0.118149   129 PHE   A C    
1565 O O    . PHE   A 117 ? 0.564215 0.666052 0.611546 -0.0119187  0.0562016   -0.11567    129 PHE   A O    
1566 C CB   . PHE   A 117 ? 0.564482 0.596551 0.586629 0.0291112   0.0619104   -0.121539   129 PHE   A CB   
1567 C CG   . PHE   A 117 ? 0.668675 0.713136 0.703294 0.0342499   0.0368418   -0.11081    129 PHE   A CG   
1568 C CD1  . PHE   A 117 ? 0.674103 0.762013 0.743149 0.0275841   0.0245913   -0.105279   129 PHE   A CD1  
1569 C CD2  . PHE   A 117 ? 0.744537 0.757193 0.75343  0.0416743   0.0264242   -0.107869   129 PHE   A CD2  
1570 C CE1  . PHE   A 117 ? 0.773087 0.871533 0.854035 0.0280061   0.00030787  -0.100038   129 PHE   A CE1  
1571 C CE2  . PHE   A 117 ? 0.664904 0.689823 0.680704 0.0455639   0.00180859  -0.102375   129 PHE   A CE2  
1572 C CZ   . PHE   A 117 ? 0.707373 0.774407 0.760432 0.0378569   -0.0123533  -0.100128   129 PHE   A CZ   
1573 H H    . PHE   A 117 ? 0.575309 0.633048 0.590381 0.00135947  0.0903322   -0.140779   129 PHE   A H    
1574 H HA   . PHE   A 117 ? 0.550228 0.567109 0.547049 0.00367796  0.0608806   -0.129076   129 PHE   A HA   
1575 H HB2  . PHE   A 117 ? 0.605564 0.605327 0.608543 0.0369506   0.0700759   -0.124298   129 PHE   A HB2  
1576 H HB3  . PHE   A 117 ? 0.582854 0.636254 0.621742 0.033218    0.0690888   -0.12311    129 PHE   A HB3  
1577 H HD1  . PHE   A 117 ? 0.68069  0.791106 0.764074 0.0209281   0.0334693   -0.105968   129 PHE   A HD1  
1578 H HD2  . PHE   A 117 ? 0.728032 0.710713 0.713034 0.0432385   0.036994    -0.110432   129 PHE   A HD2  
1579 H HE1  . PHE   A 117 ? 0.717283 0.844568 0.823668 0.0199545   -0.00698561 -0.0973106  129 PHE   A HE1  
1580 H HE2  . PHE   A 117 ? 0.711824 0.716006 0.705371 0.0508449   -0.00427705 -0.101299   129 PHE   A HE2  
1581 H HZ   . PHE   A 117 ? 0.711296 0.78661  0.770062 0.0379648   -0.0296009  -0.0991054  129 PHE   A HZ   
1582 N N    . PHE   A 118 ? 0.547793 0.610838 0.578426 -0.00981599 0.0308225   -0.113426   130 PHE   A N    
1583 C CA   . PHE   A 118 ? 0.528401 0.608597 0.576459 -0.0207339  0.0146095   -0.103454   130 PHE   A CA   
1584 C C    . PHE   A 118 ? 0.544624 0.614116 0.598211 -0.016691   -0.00624822 -0.101547   130 PHE   A C    
1585 O O    . PHE   A 118 ? 0.549655 0.594256 0.582627 -0.00825081 -0.00997711 -0.108234   130 PHE   A O    
1586 C CB   . PHE   A 118 ? 0.542645 0.616136 0.578089 -0.0310025  0.0101369   -0.103216   130 PHE   A CB   
1587 C CG   . PHE   A 118 ? 0.642925 0.733864 0.669811 -0.0388852  0.0240394   -0.104061   130 PHE   A CG   
1588 C CD1  . PHE   A 118 ? 0.589073 0.675698 0.599106 -0.0375333  0.0377233   -0.118926   130 PHE   A CD1  
1589 C CD2  . PHE   A 118 ? 0.596086 0.70769  0.629092 -0.050195   0.0241523   -0.0906702  130 PHE   A CD2  
1590 C CE1  . PHE   A 118 ? 0.60426  0.710009 0.603714 -0.0456356  0.0480719   -0.123399   130 PHE   A CE1  
1591 C CE2  . PHE   A 118 ? 0.623841 0.753063 0.640668 -0.0567745  0.0361741   -0.0919621  130 PHE   A CE2  
1592 C CZ   . PHE   A 118 ? 0.571998 0.699843 0.572353 -0.0536018  0.0467094   -0.109919   130 PHE   A CZ   
1593 H H    . PHE   A 118 ? 0.552132 0.59503  0.568659 -0.00611086 0.0294385   -0.117184   130 PHE   A H    
1594 H HA   . PHE   A 118 ? 0.534604 0.637207 0.598292 -0.0247378  0.0189652   -0.0984996  130 PHE   A HA   
1595 H HB2  . PHE   A 118 ? 0.55997  0.617674 0.583382 -0.0265506  0.00894448  -0.110617   130 PHE   A HB2  
1596 H HB3  . PHE   A 118 ? 0.561218 0.634505 0.604991 -0.0364468  -0.00203456 -0.0956969  130 PHE   A HB3  
1597 H HD1  . PHE   A 118 ? 0.603464 0.674044 0.607829 -0.032666   0.0402927   -0.126519   130 PHE   A HD1  
1598 H HD2  . PHE   A 118 ? 0.613484 0.7267   0.659357 -0.0549162  0.0162227   -0.0808986  130 PHE   A HD2  
1599 H HE1  . PHE   A 118 ? 0.598028 0.701506 0.587266 -0.0472225  0.0566167   -0.136193   130 PHE   A HE1  
1600 H HE2  . PHE   A 118 ? 0.616614 0.759083 0.632463 -0.0650767  0.0376495   -0.0810726  130 PHE   A HE2  
1601 H HZ   . PHE   A 118 ? 0.602223 0.744016 0.589957 -0.0588246  0.0534343   -0.113244   130 PHE   A HZ   
1602 N N    . GLU   A 119 ? 0.529168 0.617795 0.608102 -0.0266081  -0.0185744  -0.0938248  131 GLU   A N    
1603 C CA   . GLU   A 119 ? 0.564206 0.641657 0.648739 -0.0309168  -0.0411886  -0.0950281  131 GLU   A CA   
1604 C C    . GLU   A 119 ? 0.606212 0.669644 0.691572 -0.047408   -0.0475424  -0.0885942  131 GLU   A C    
1605 O O    . GLU   A 119 ? 0.570221 0.64992  0.667841 -0.0615326  -0.0399798  -0.0766265  131 GLU   A O    
1606 C CB   . GLU   A 119 ? 0.567179 0.676387 0.684057 -0.0339343  -0.0521909  -0.0930762  131 GLU   A CB   
1607 C CG   . GLU   A 119 ? 0.639609 0.737439 0.760645 -0.0412062  -0.0773527  -0.099406   131 GLU   A CG   
1608 C CD   . GLU   A 119 ? 0.62149  0.76106  0.777374 -0.0432803  -0.0911496  -0.101457   131 GLU   A CD   
1609 O OE1  . GLU   A 119 ? 0.620435 0.762916 0.766866 -0.0267239  -0.105294   -0.108784   131 GLU   A OE1  
1610 O OE2  . GLU   A 119 ? 0.69504  0.866823 0.887682 -0.0633499  -0.0888194  -0.0955948  131 GLU   A OE2  
1611 H H    . GLU   A 119 ? 0.535765 0.645677 0.629186 -0.0326675  -0.0116109  -0.0888994  131 GLU   A H    
1612 H HA   . GLU   A 119 ? 0.57029  0.628511 0.636326 -0.0215233  -0.045172   -0.10196    131 GLU   A HA   
1613 H HB2  . GLU   A 119 ? 0.578732 0.697434 0.695355 -0.0195653  -0.0488193  -0.0952526  131 GLU   A HB2  
1614 H HB3  . GLU   A 119 ? 0.576202 0.706855 0.712647 -0.0455809  -0.0457731  -0.086499   131 GLU   A HB3  
1615 H HG2  . GLU   A 119 ? 0.627353 0.712888 0.751763 -0.0557279  -0.080544   -0.0965426  131 GLU   A HG2  
1616 H HG3  . GLU   A 119 ? 0.626182 0.701949 0.723356 -0.0303585  -0.0821157  -0.106387   131 GLU   A HG3  
1617 N N    . ILE   A 120 ? 0.658787 0.690072 0.726882 -0.0431557  -0.0590216  -0.0960355  132 ILE   A N    
1618 C CA   . ILE   A 120 ? 0.695216 0.704033 0.759956 -0.0509989  -0.065956   -0.0896923  132 ILE   A CA   
1619 C C    . ILE   A 120 ? 0.670901 0.650813 0.739268 -0.0548836  -0.0864195  -0.0972713  132 ILE   A C    
1620 O O    . ILE   A 120 ? 0.571743 0.540323 0.627264 -0.0427354  -0.0931709  -0.113802   132 ILE   A O    
1621 C CB   . ILE   A 120 ? 0.700227 0.69861  0.744495 -0.038452   -0.0603581  -0.0950057  132 ILE   A CB   
1622 C CG1  . ILE   A 120 ? 0.707006 0.731245 0.744885 -0.0368716  -0.0410471  -0.0939858  132 ILE   A CG1  
1623 C CG2  . ILE   A 120 ? 0.795218 0.769671 0.837233 -0.0410173  -0.0715993  -0.0850337  132 ILE   A CG2  
1624 C CD1  . ILE   A 120 ? 0.657758 0.682571 0.681608 -0.0286165  -0.0369605  -0.102141   132 ILE   A CD1  
1625 H H    . ILE   A 120 ? 0.653311 0.675845 0.710466 -0.0337212  -0.0622321  -0.104983   132 ILE   A H    
1626 H HA   . ILE   A 120 ? 0.683279 0.702247 0.757011 -0.0622891  -0.0617756  -0.0776262  132 ILE   A HA   
1627 H HB   . ILE   A 120 ? 0.714343 0.703375 0.750534 -0.0291765  -0.0628838  -0.107135   132 ILE   A HB   
1628 H HG12 . ILE   A 120 ? 0.691663 0.727946 0.735162 -0.0457604  -0.0370183  -0.083157   132 ILE   A HG12 
1629 H HG13 . ILE   A 120 ? 0.680847 0.711712 0.718506 -0.0329724  -0.0344316  -0.0997126  132 ILE   A HG13 
1630 H HG21 . ILE   A 120 ? 0.770863 0.745771 0.803925 -0.0309621  -0.0700677  -0.089297   132 ILE   A HG21 
1631 H HG22 . ILE   A 120 ? 0.779811 0.760718 0.825491 -0.0518937  -0.0686272  -0.0707126  132 ILE   A HG22 
1632 H HG23 . ILE   A 120 ? 0.790979 0.742736 0.835991 -0.0414506  -0.0832654  -0.0889082  132 ILE   A HG23 
1633 H HD11 . ILE   A 120 ? 0.674755 0.687473 0.695487 -0.0210153  -0.042169   -0.111678   132 ILE   A HD11 
1634 H HD12 . ILE   A 120 ? 0.66075  0.698958 0.679795 -0.0286168  -0.0241788  -0.107245   132 ILE   A HD12 
1635 H HD13 . ILE   A 120 ? 0.681233 0.706412 0.704006 -0.0309343  -0.041809   -0.0935728  132 ILE   A HD13 
1636 N N    . GLU   A 121 ? 0.636455 0.602477 0.718648 -0.0736874  -0.0939975  -0.0852529  133 GLU   A N    
1637 C CA   . GLU   A 121 ? 0.734445 0.659471 0.817557 -0.0799646  -0.112852   -0.093388   133 GLU   A CA   
1638 C C    . GLU   A 121 ? 0.747567 0.62996  0.815557 -0.0733279  -0.116248   -0.0848413  133 GLU   A C    
1639 O O    . GLU   A 121 ? 0.793849 0.669443 0.862087 -0.0853458  -0.111589   -0.0618146  133 GLU   A O    
1640 C CB   . GLU   A 121 ? 0.718914 0.652495 0.830109 -0.108039   -0.120558   -0.0891604  133 GLU   A CB   
1641 C CG   . GLU   A 121 ? 0.792425 0.683387 0.904972 -0.117499   -0.141611   -0.105555   133 GLU   A CG   
1642 C CD   . GLU   A 121 ? 0.825091 0.724457 0.969799 -0.1522     -0.149979   -0.104027   133 GLU   A CD   
1643 O OE1  . GLU   A 121 ? 0.789354 0.739958 0.96049  -0.167103   -0.138474   -0.0908757  133 GLU   A OE1  
1644 O OE2  . GLU   A 121 ? 0.860935 0.716863 1.00596  -0.164973   -0.167014   -0.118741   133 GLU   A OE2  
1645 H H    . GLU   A 121 ? 0.662477 0.642363 0.752061 -0.0838257  -0.0861655  -0.0722035  133 GLU   A H    
1646 H HA   . GLU   A 121 ? 0.709585 0.630256 0.784184 -0.0687276  -0.118666   -0.109632   133 GLU   A HA   
1647 H HB2  . GLU   A 121 ? 0.711713 0.681034 0.834881 -0.107778   -0.118148   -0.0931249  133 GLU   A HB2  
1648 H HB3  . GLU   A 121 ? 0.74221  0.676035 0.85982  -0.121724   -0.113506   -0.0722926  133 GLU   A HB3  
1649 H HG2  . GLU   A 121 ? 0.811909 0.663145 0.911626 -0.113264   -0.14399    -0.102563   133 GLU   A HG2  
1650 H HG3  . GLU   A 121 ? 0.780646 0.675083 0.883835 -0.104396   -0.148117   -0.122854   133 GLU   A HG3  
1651 N N    . LEU   A 122 ? 0.687179 0.543072 0.740696 -0.0523334  -0.124116   -0.103044   134 LEU   A N    
1652 C CA   . LEU   A 122 ? 0.762274 0.574505 0.806372 -0.0398743  -0.13241    -0.0992396  134 LEU   A CA   
1653 C C    . LEU   A 122 ? 0.863169 0.618343 0.91231  -0.0559275  -0.147702   -0.0971551  134 LEU   A C    
1654 O O    . LEU   A 122 ? 0.958458 0.688256 1.00761  -0.0552293  -0.158877   -0.120942   134 LEU   A O    
1655 C CB   . LEU   A 122 ? 0.765716 0.578345 0.799065 -0.0112656  -0.132706   -0.123962   134 LEU   A CB   
1656 C CG   . LEU   A 122 ? 0.809258 0.587648 0.838104 0.0116164   -0.14147    -0.123442   134 LEU   A CG   
1657 C CD1  . LEU   A 122 ? 0.775389 0.560901 0.801578 0.0117371   -0.140019   -0.0938383  134 LEU   A CD1  
1658 C CD2  . LEU   A 122 ? 0.78506  0.585381 0.811083 0.0386412   -0.136011   -0.148778   134 LEU   A CD2  
1659 H H    . LEU   A 122 ? 0.699441 0.565697 0.748467 -0.0441338  -0.123877   -0.118202   134 LEU   A H    
1660 H HA   . LEU   A 122 ? 0.76091  0.581537 0.801887 -0.0395405  -0.126945   -0.0820801  134 LEU   A HA   
1661 H HB2  . LEU   A 122 ? 0.730195 0.577546 0.761259 -0.00624662 -0.121556   -0.125131   134 LEU   A HB2  
1662 H HB3  . LEU   A 122 ? 0.774073 0.577305 0.805565 -0.0117306  -0.137689   -0.140946   134 LEU   A HB3  
1663 H HG   . LEU   A 122 ? 0.840211 0.57618  0.869008 0.00920163  -0.152229   -0.1266     134 LEU   A HG   
1664 H HD11 . LEU   A 122 ? 0.813911 0.572897 0.839183 -0.00334892 -0.144413   -0.0770827  134 LEU   A HD11 
1665 H HD12 . LEU   A 122 ? 0.802874 0.580424 0.826875 0.0322227   -0.145543   -0.0959451  134 LEU   A HD12 
1666 H HD13 . LEU   A 122 ? 0.749556 0.574525 0.775956 0.00646446  -0.129141   -0.089989   134 LEU   A HD13 
1667 H HD21 . LEU   A 122 ? 0.782821 0.58508  0.804694 0.0369356   -0.133985   -0.165902   134 LEU   A HD21 
1668 H HD22 . LEU   A 122 ? 0.75494  0.591749 0.781931 0.0406298   -0.126185   -0.144595   134 LEU   A HD22 
1669 H HD23 . LEU   A 122 ? 0.817217 0.594226 0.844359 0.0556524   -0.143824   -0.152894   134 LEU   A HD23 
1670 N N    . LEU   A 123 ? 0.900634 0.632347 0.950525 -0.0730149  -0.147209   -0.0687322  135 LEU   A N    
1671 C CA   . LEU   A 123 ? 1.0009   0.673452 1.05561  -0.0963972  -0.15791    -0.062158   135 LEU   A CA   
1672 C C    . LEU   A 123 ? 1.11916  0.720887 1.15759  -0.0713676  -0.171713   -0.0679978  135 LEU   A C    
1673 O O    . LEU   A 123 ? 1.24092  0.792962 1.28165  -0.0764135  -0.183781   -0.0882042  135 LEU   A O    
1674 C CB   . LEU   A 123 ? 1.01028  0.680966 1.06729  -0.126777   -0.148102   -0.0259975  135 LEU   A CB   
1675 C CG   . LEU   A 123 ? 0.999975 0.745788 1.07519  -0.147176   -0.130699   -0.018222   135 LEU   A CG   
1676 C CD1  . LEU   A 123 ? 1.07417  0.815517 1.14538  -0.175623   -0.11748    0.0179556   135 LEU   A CD1  
1677 C CD2  . LEU   A 123 ? 1.01613  0.796747 1.12175  -0.165406   -0.134335   -0.0412316  135 LEU   A CD2  
1678 H H    . LEU   A 123 ? 0.892395 0.643997 0.937412 -0.0715224  -0.139114   -0.0526265  135 LEU   A H    
1679 H HA   . LEU   A 123 ? 0.999623 0.677951 1.06625  -0.108761   -0.162502   -0.0793208  135 LEU   A HA   
1680 H HB2  . LEU   A 123 ? 1.03957  0.695008 1.07912  -0.113761   -0.146946   -0.00852497 135 LEU   A HB2  
1681 H HB3  . LEU   A 123 ? 1.07009  0.700149 1.13223  -0.146703   -0.154058   -0.0235245  135 LEU   A HB3  
1682 H HG   . LEU   A 123 ? 0.963544 0.743148 1.03169  -0.128108   -0.12435    -0.0213223  135 LEU   A HG   
1683 H HD11 . LEU   A 123 ? 1.08925  0.799574 1.13699  -0.163744   -0.119392   0.0339617   135 LEU   A HD11 
1684 H HD12 . LEU   A 123 ? 1.02421  0.816785 1.10271  -0.180439   -0.104233   0.0220383   135 LEU   A HD12 
1685 H HD13 . LEU   A 123 ? 1.09691  0.815548 1.18071  -0.201026   -0.119923   0.0206102   135 LEU   A HD13 
1686 H HD21 . LEU   A 123 ? 0.984481 0.769914 1.08633  -0.146886   -0.141269   -0.0620862  135 LEU   A HD21 
1687 H HD22 . LEU   A 123 ? 1.04433  0.795234 1.15953  -0.186742   -0.14123    -0.0416371  135 LEU   A HD22 
1688 H HD23 . LEU   A 123 ? 0.973071 0.801761 1.0919   -0.174055   -0.123058   -0.035234   135 LEU   A HD23 
1689 N N    . ASP   A 124 ? 1.10482  0.703585 1.12795  -0.0437096  -0.171077   -0.0519167  136 ASP   A N    
1690 C CA   . ASP   A 124 ? 1.19067  0.723916 1.20141  -0.0147788  -0.185278   -0.0523134  136 ASP   A CA   
1691 C C    . ASP   A 124 ? 1.18094  0.749937 1.18372  0.0217886   -0.184948   -0.0451938  136 ASP   A C    
1692 O O    . ASP   A 124 ? 1.13889  0.766434 1.13894  0.0162916   -0.17416    -0.0302236  136 ASP   A O    
1693 C CB   . ASP   A 124 ? 1.28967  0.742506 1.28881  -0.0349037  -0.192266   -0.0221311  136 ASP   A CB   
1694 C CG   . ASP   A 124 ? 1.42007  0.783679 1.40989  -0.00857377 -0.209196   -0.0319632  136 ASP   A CG   
1695 O OD1  . ASP   A 124 ? 1.42489  0.794361 1.42229  0.0201495   -0.214391   -0.0699861  136 ASP   A OD1  
1696 O OD2  . ASP   A 124 ? 1.5526   0.841879 1.52489  -0.0139656  -0.215528   -0.00062977 136 ASP   A OD2  
1697 H H    . ASP   A 124 ? 1.07725  0.717322 1.09836  -0.0417732  -0.16242    -0.0413715  136 ASP   A H    
1698 H HA   . ASP   A 124 ? 1.19974  0.717785 1.21492  -0.00508606 -0.190704   -0.079244   136 ASP   A HA   
1699 H HB2  . ASP   A 124 ? 1.30161  0.750483 1.31005  -0.0666054  -0.188741   -0.0227832  136 ASP   A HB2  
1700 H HB3  . ASP   A 124 ? 1.30197  0.762647 1.28918  -0.0351995  -0.188564   0.00588425  136 ASP   A HB3  
1701 N N    . PHE   A 125 ? 1.16785  0.703395 1.16905  0.059912    -0.197456   -0.0587477  137 PHE   A N    
1702 C CA   . PHE   A 125 ? 1.1096   0.674653 1.10718  0.095537    -0.202684   -0.0486389  137 PHE   A CA   
1703 C C    . PHE   A 125 ? 1.17668  0.669747 1.16874  0.132447    -0.222091   -0.0457247  137 PHE   A C    
1704 O O    . PHE   A 125 ? 1.23493  0.673181 1.23209  0.139054    -0.22721    -0.0702104  137 PHE   A O    
1705 C CB   . PHE   A 125 ? 0.999051 0.646133 1.01348  0.11143     -0.191944   -0.0795468  137 PHE   A CB   
1706 C CG   . PHE   A 125 ? 1.03458  0.676669 1.0615   0.127769    -0.190196   -0.121684   137 PHE   A CG   
1707 C CD1  . PHE   A 125 ? 1.06795  0.704153 1.10554  0.170383    -0.198343   -0.141953   137 PHE   A CD1  
1708 C CD2  . PHE   A 125 ? 0.992356 0.642956 1.01942  0.102717    -0.180023   -0.142293   137 PHE   A CD2  
1709 C CE1  . PHE   A 125 ? 1.07802  0.714693 1.1238   0.185115    -0.192771   -0.18319    137 PHE   A CE1  
1710 C CE2  . PHE   A 125 ? 1.06564  0.716355 1.09551  0.117815    -0.177082   -0.181039   137 PHE   A CE2  
1711 C CZ   . PHE   A 125 ? 1.04975  0.693485 1.08799  0.157747    -0.181485   -0.202308   137 PHE   A CZ   
1712 H H    . PHE   A 125 ? 1.19862  0.695737 1.20245  0.0646485   -0.203301   -0.0762326  137 PHE   A H    
1713 H HA   . PHE   A 125 ? 1.10735  0.685885 1.09388  0.0837102   -0.200264   -0.0219216  137 PHE   A HA   
1714 H HB2  . PHE   A 125 ? 1.0135   0.685376 1.0292   0.132712    -0.196451   -0.0739386  137 PHE   A HB2  
1715 H HB3  . PHE   A 125 ? 0.969378 0.653999 0.984059 0.0890259   -0.180189   -0.0771593  137 PHE   A HB3  
1716 H HD1  . PHE   A 125 ? 1.09205  0.725176 1.13073  0.19081     -0.207872   -0.127948   137 PHE   A HD1  
1717 H HD2  . PHE   A 125 ? 0.988831 0.650053 1.01314  0.0768314   -0.174845   -0.130344   137 PHE   A HD2  
1718 H HE1  . PHE   A 125 ? 1.09825  0.735017 1.15398  0.215387    -0.196637   -0.198286   137 PHE   A HE1  
1719 H HE2  . PHE   A 125 ? 1.02224  0.678809 1.04764  0.101615    -0.172188   -0.193361   137 PHE   A HE2  
1720 H HZ   . PHE   A 125 ? 1.06737  0.711008 1.1055   0.167302    -0.177557   -0.229763   137 PHE   A HZ   
1721 N N    . LYS   A 126 ? 1.19438  0.686138 1.17327  0.156677    -0.233768   -0.015763   138 LYS   A N    
1722 C CA   . LYS   A 126 ? 1.29599  0.716377 1.26578  0.197567    -0.255279   -0.00349028 138 LYS   A CA   
1723 C C    . LYS   A 126 ? 1.27646  0.765278 1.25716  0.243036    -0.266126   -0.00561902 138 LYS   A C    
1724 O O    . LYS   A 126 ? 1.1642   0.735099 1.14586  0.232044    -0.25874    -0.00017648 138 LYS   A O    
1725 C CB   . LYS   A 126 ? 1.32579  0.657462 1.26039  0.177076    -0.262518   0.0455226   138 LYS   A CB   
1726 H H    . LYS   A 126 ? 1.16613  0.704036 1.14001  0.148666    -0.2289     -0.00226726 138 LYS   A H    
1727 H HA   . LYS   A 126 ? 1.30584  0.69225  1.28653  0.209115    -0.257404   -0.0289313  138 LYS   A HA   
1730 N N    . GLY   A 127 ? 1.41639  0.875522 1.40947  0.29466     -0.28353    -0.0185056  139 GLY   A N    
1731 C CA   . GLY   A 127 ? 1.45831  0.989125 1.47079  0.341702    -0.297041   -0.0243408  139 GLY   A CA   
1732 C C    . GLY   A 127 ? 1.55386  1.07779  1.5341   0.352289    -0.316685   0.0262008   139 GLY   A C    
1733 O O    . GLY   A 127 ? 1.64638  1.07582  1.58917  0.342829    -0.324833   0.0654236   139 GLY   A O    
1734 H H    . GLY   A 127 ? 1.45574  0.849672 1.44714  0.301244    -0.287439   -0.0255074  139 GLY   A H    
1735 H HA2  . GLY   A 127 ? 1.37889  0.9872   1.40969  0.33177     -0.284734   -0.0448551  139 GLY   A HA2  
1736 H HA3  . GLY   A 127 ? 1.49063  0.999783 1.51918  0.377372    -0.305706   -0.0425118  139 GLY   A HA3  
1737 N N    . GLU   A 128 ? 1.52458  1.14787  1.51585  0.368321    -0.32367    0.0254908   140 GLU   A N    
1738 C CA   . GLU   A 128 ? 1.50178  1.12827  1.45691  0.380716    -0.345024   0.0712135   140 GLU   A CA   
1739 C C    . GLU   A 128 ? 1.58158  1.09958  1.51511  0.425308    -0.371855   0.100903    140 GLU   A C    
1740 O O    . GLU   A 128 ? 1.53771  1.03032  1.5045   0.467657    -0.379878   0.0715711   140 GLU   A O    
1741 C CB   . GLU   A 128 ? 1.3934   1.14473  1.36812  0.396924    -0.353863   0.0583245   140 GLU   A CB   
1742 O OXT  . GLU   A 128 ? 1.64593  1.09865  1.52703  0.413435    -0.380556   0.152229    140 GLU   A OXT  
1743 H H    . GLU   A 128 ? 1.44266  1.13286  1.4627   0.370201    -0.314984   -0.00443989 140 GLU   A H    
1744 H HA   . GLU   A 128 ? 1.49184  1.09964  1.41784  0.34315     -0.334267   0.0937717   140 GLU   A HA   
1747 N N    . GLY   B 1   ? 1.75704  0.566932 1.00046  0.00073688  -0.286961   -0.303425   13  GLY   B N    
1748 C CA   . GLY   B 1   ? 1.63557  0.522377 1.00621  -0.0433534  -0.268877   -0.266257   13  GLY   B CA   
1749 C C    . GLY   B 1   ? 1.52837  0.51488  0.925378 -0.0466259  -0.259489   -0.249049   13  GLY   B C    
1750 O O    . GLY   B 1   ? 1.52548  0.531808 0.844955 -0.0124854  -0.248593   -0.253322   13  GLY   B O    
1751 H H1   . GLY   B 1   ? 1.81767  0.562214 1.0468   0.00370895  -0.293765   -0.315488   13  GLY   B H1   
1752 H H2   . GLY   B 1   ? 1.73295  0.572605 0.933448 0.030955    -0.256265   -0.296266   13  GLY   B H2   
1753 H H3   . GLY   B 1   ? 1.79222  0.589031 1.01245  -0.00342182 -0.321901   -0.322295   13  GLY   B H3   
1754 H HA2  . GLY   B 1   ? 1.66001  0.518921 1.08401  -0.0766754  -0.299023   -0.27276    13  GLY   B HA2  
1755 H HA3  . GLY   B 1   ? 1.60421  0.503295 0.990778 -0.0366126  -0.232519   -0.246163   13  GLY   B HA3  
1756 N N    . ALA   B 2   ? 1.43735  0.486257 0.94698  -0.0865014  -0.25801    -0.226936   14  ALA   B N    
1757 C CA   . ALA   B 2   ? 1.3202   0.452556 0.867979 -0.0924176  -0.255661   -0.212474   14  ALA   B CA   
1758 C C    . ALA   B 2   ? 1.25692  0.453023 0.772761 -0.0628985  -0.202624   -0.192584   14  ALA   B C    
1759 O O    . ALA   B 2   ? 1.19672  0.434143 0.702079 -0.0559462  -0.204239   -0.186412   14  ALA   B O    
1760 C CB   . ALA   B 2   ? 1.26837  0.451903 0.949185 -0.136624   -0.257569   -0.195087   14  ALA   B CB   
1761 H H    . ALA   B 2   ? 1.42844  0.465994 0.993804 -0.109762   -0.256727   -0.219905   14  ALA   B H    
1762 H HA   . ALA   B 2   ? 1.37871  0.48994  0.888648 -0.0872759  -0.291652   -0.228844   14  ALA   B HA   
1763 H HB1  . ALA   B 2   ? 1.30993  0.460442 1.01884  -0.157415   -0.294807   -0.208744   14  ALA   B HB1  
1764 H HB2  . ALA   B 2   ? 1.23219  0.428829 0.942484 -0.141679   -0.224105   -0.179509   14  ALA   B HB2  
1765 H HB3  . ALA   B 2   ? 1.21175  0.448929 0.922424 -0.13842    -0.254683   -0.185827   14  ALA   B HB3  
1766 N N    . PRO   B 3   ? 1.18628  0.39818  0.700775 -0.0487846  -0.156167   -0.179058   15  PRO   B N    
1767 C CA   . PRO   B 3   ? 1.15398  0.425688 0.640919 -0.0202106  -0.110773   -0.166549   15  PRO   B CA   
1768 C C    . PRO   B 3   ? 1.2379   0.485576 0.61974  0.0212076   -0.104299   -0.180356   15  PRO   B C    
1769 O O    . PRO   B 3   ? 1.25961  0.56171  0.628973 0.0340957   -0.0795291  -0.170581   15  PRO   B O    
1770 C CB   . PRO   B 3   ? 1.11626  0.397808 0.617714 -0.0102968  -0.0753911  -0.15385    15  PRO   B CB   
1771 C CG   . PRO   B 3   ? 1.15906  0.389516 0.707009 -0.0402177  -0.0943271  -0.150811   15  PRO   B CG   
1772 C CD   . PRO   B 3   ? 1.21817  0.395574 0.76819  -0.0624923  -0.146804   -0.171871   15  PRO   B CD   
1773 H HA   . PRO   B 3   ? 1.09173  0.416571 0.622246 -0.032336   -0.103296   -0.155848   15  PRO   B HA   
1774 H HB2  . PRO   B 3   ? 1.16114  0.419011 0.605659 0.0185957   -0.0659144  -0.160717   15  PRO   B HB2  
1775 H HB3  . PRO   B 3   ? 1.05615  0.399095 0.59555  -0.0136484  -0.0513923  -0.140662   15  PRO   B HB3  
1776 H HG2  . PRO   B 3   ? 1.20087  0.388918 0.717783 -0.0253892  -0.087111   -0.150857   15  PRO   B HG2  
1777 H HG3  . PRO   B 3   ? 1.10279  0.3771   0.712638 -0.0596007  -0.0798517  -0.134918   15  PRO   B HG3  
1778 H HD2  . PRO   B 3   ? 1.29025  0.400095 0.794383 -0.0529644  -0.163599   -0.187302   15  PRO   B HD2  
1779 H HD3  . PRO   B 3   ? 1.19366  0.384299 0.813437 -0.0931984  -0.156418   -0.16474    15  PRO   B HD3  
1780 N N    . ALA   B 4   ? 1.31501  0.4797   0.623254 0.0423963   -0.123173   -0.203317   16  ALA   B N    
1781 C CA   . ALA   B 4   ? 1.39329  0.529168 0.594332 0.0856933   -0.116493   -0.220702   16  ALA   B CA   
1782 C C    . ALA   B 4   ? 1.38911  0.535362 0.551246 0.0839466   -0.136262   -0.221978   16  ALA   B C    
1783 O O    . ALA   B 4   ? 1.37946  0.568576 0.503202 0.106364    -0.103523   -0.210513   16  ALA   B O    
1784 C CB   . ALA   B 4   ? 1.54357  0.573181 0.675433 0.104843    -0.144377   -0.252532   16  ALA   B CB   
1785 H H    . ALA   B 4   ? 1.34784  0.470842 0.673534 0.0299174   -0.139082   -0.208761   16  ALA   B H    
1786 H HA   . ALA   B 4   ? 1.36021  0.538653 0.557941 0.105914    -0.0797233  -0.210638   16  ALA   B HA   
1787 H HB1  . ALA   B 4   ? 1.52869  0.547564 0.678699 0.110766    -0.128715   -0.247843   16  ALA   B HB1  
1788 H HB2  . ALA   B 4   ? 1.56459  0.555327 0.710943 0.0808891   -0.182536   -0.263693   16  ALA   B HB2  
1789 H HB3  . ALA   B 4   ? 1.59388  0.603247 0.648856 0.136238    -0.140073   -0.267128   16  ALA   B HB3  
1790 N N    . THR   B 5   ? 1.37864  0.484819 0.553871 0.0575608   -0.190459   -0.2343     17  THR   B N    
1791 C CA   . THR   B 5   ? 1.3816   0.498483 0.537194 0.0510981   -0.220691   -0.230415   17  THR   B CA   
1792 C C    . THR   B 5   ? 1.27583  0.480898 0.491665 0.0406449   -0.184682   -0.194384   17  THR   B C    
1793 O O    . THR   B 5   ? 1.27759  0.49368  0.447498 0.0520185   -0.185337   -0.181889   17  THR   B O    
1794 C CB   . THR   B 5   ? 1.40798  0.486688 0.612211 0.0171343   -0.286936   -0.247824   17  THR   B CB   
1795 O OG1  . THR   B 5   ? 1.53002  0.515096 0.663543 0.0291057   -0.323225   -0.287079   17  THR   B OG1  
1796 C CG2  . THR   B 5   ? 1.42759  0.519904 0.621305 0.0122798   -0.328563   -0.242687   17  THR   B CG2  
1797 H H    . THR   B 5   ? 1.40526  0.475192 0.606416 0.0427331   -0.211327   -0.244912   17  THR   B H    
1798 H HA   . THR   B 5   ? 1.45882  0.544279 0.523504 0.0788504   -0.223595   -0.242264   17  THR   B HA   
1799 H HB   . THR   B 5   ? 1.34204  0.448849 0.63602  -0.00949972 -0.280175   -0.236927   17  THR   B HB   
1801 H HG21 . THR   B 5   ? 1.47348  0.533428 0.680277 -0.00210913 -0.376798   -0.261698   17  THR   B HG21 
1802 H HG22 . THR   B 5   ? 1.48376  0.561411 0.588465 0.0401432   -0.32281    -0.243695   17  THR   B HG22 
1803 H HG23 . THR   B 5   ? 1.35032  0.497798 0.613322 -0.00290609 -0.313039   -0.219191   17  THR   B HG23 
1804 N N    . VAL   B 6   ? 1.18477  0.449356 0.495156 0.0219146   -0.150575   -0.176793   18  VAL   B N    
1805 C CA   . VAL   B 6   ? 1.12631  0.465542 0.488869 0.0135611   -0.118201   -0.149824   18  VAL   B CA   
1806 C C    . VAL   B 6   ? 1.1503   0.518086 0.458157 0.042984    -0.0690904  -0.140807   18  VAL   B C    
1807 O O    . VAL   B 6   ? 1.10863  0.503386 0.405743 0.0450258   -0.053166   -0.121648   18  VAL   B O    
1808 C CB   . VAL   B 6   ? 1.02285  0.420211 0.500925 -0.0147012  -0.0999083  -0.138539   18  VAL   B CB   
1809 C CG1  . VAL   B 6   ? 0.92574  0.39244  0.454848 -0.0216909  -0.0676157  -0.118113   18  VAL   B CG1  
1810 C CG2  . VAL   B 6   ? 1.04235  0.421203 0.58361  -0.0441846  -0.143673   -0.144345   18  VAL   B CG2  
1811 H H    . VAL   B 6   ? 1.1725   0.428908 0.514001 0.0141368   -0.148283   -0.181608   18  VAL   B H    
1812 H HA   . VAL   B 6   ? 1.14321  0.477515 0.50179  0.00796663  -0.140501   -0.14444    18  VAL   B HA   
1813 H HB   . VAL   B 6   ? 1.01222  0.410994 0.48955  -0.00783314 -0.0814067  -0.142474   18  VAL   B HB   
1814 H HG11 . VAL   B 6   ? 0.957606 0.415389 0.468227 -0.020782   -0.0804439  -0.110918   18  VAL   B HG11 
1815 H HG12 . VAL   B 6   ? 0.92182  0.410917 0.432856 -0.00819468 -0.0369472  -0.115686   18  VAL   B HG12 
1816 H HG13 . VAL   B 6   ? 0.878163 0.374229 0.477079 -0.0398798  -0.0653125  -0.115209   18  VAL   B HG13 
1817 H HG21 . VAL   B 6   ? 0.975689 0.391799 0.586981 -0.0604222  -0.129129   -0.13697    18  VAL   B HG21 
1818 H HG22 . VAL   B 6   ? 1.08481  0.418081 0.600341 -0.0431579  -0.163114   -0.158332   18  VAL   B HG22 
1819 H HG23 . VAL   B 6   ? 1.05256  0.428812 0.592234 -0.0472302  -0.166826   -0.141492   18  VAL   B HG23 
1820 N N    . THR   B 7   ? 1.21534  0.584167 0.505731 0.063237    -0.0426728  -0.150847   19  THR   B N    
1821 C CA   . THR   B 7   ? 1.25043  0.651843 0.495995 0.0950954   0.00301426  -0.146374   19  THR   B CA   
1822 C C    . THR   B 7   ? 1.41513  0.778915 0.558978 0.117113    -0.00191631 -0.14642    19  THR   B C    
1823 O O    . THR   B 7   ? 1.49986  0.90533  0.630202 0.124998    0.0342791   -0.126085   19  THR   B O    
1824 C CB   . THR   B 7   ? 1.29271  0.679497 0.517907 0.122983    0.0175554   -0.162516   19  THR   B CB   
1825 O OG1  . THR   B 7   ? 1.15844  0.609967 0.474075 0.107611    0.0377511   -0.151134   19  THR   B OG1  
1826 C CG2  . THR   B 7   ? 1.36066  0.756732 0.510753 0.167265    0.0533698   -0.167361   19  THR   B CG2  
1827 H H    . THR   B 7   ? 1.19746  0.54801  0.508492 0.0575794   -0.0527431  -0.159233   19  THR   B H    
1828 H HA   . THR   B 7   ? 1.19884  0.657886 0.497551 0.0839038   0.0270123   -0.13142    19  THR   B HA   
1829 H HB   . THR   B 7   ? 1.32569  0.653417 0.52751  0.122946    -0.0107423  -0.177118   19  THR   B HB   
1831 H HG21 . THR   B 7   ? 1.355    0.759835 0.511041 0.185931    0.0676038   -0.173683   19  THR   B HG21 
1832 H HG22 . THR   B 7   ? 1.32797  0.776256 0.498182 0.163011    0.078682    -0.151579   19  THR   B HG22 
1833 H HG23 . THR   B 7   ? 1.43854  0.780154 0.5154   0.18248     0.0373552   -0.180032   19  THR   B HG23 
1834 N N    . GLU   B 8   ? 1.50839  0.793192 0.585429 0.12242     -0.0501565  -0.167423   20  GLU   B N    
1835 C CA   . GLU   B 8   ? 1.62439  0.859946 0.574615 0.155417    -0.0574142  -0.17674    20  GLU   B CA   
1836 C C    . GLU   B 8   ? 1.61246  0.849781 0.5424   0.143652    -0.0765193  -0.153504   20  GLU   B C    
1837 O O    . GLU   B 8   ? 1.59461  0.813633 0.421952 0.172388    -0.0630792  -0.146964   20  GLU   B O    
1838 C CB   . GLU   B 8   ? 1.78059  0.922017 0.652358 0.171876    -0.106345   -0.217701   20  GLU   B CB   
1839 C CG   . GLU   B 8   ? 1.86703  0.98302  0.705408 0.205185    -0.0809626  -0.241446   20  GLU   B CG   
1840 C CD   . GLU   B 8   ? 2.05199  1.06326  0.830102 0.215702    -0.131605   -0.285222   20  GLU   B CD   
1841 O OE1  . GLU   B 8   ? 2.03483  0.994438 0.772787 0.203328    -0.18806    -0.302255   20  GLU   B OE1  
1842 O OE2  . GLU   B 8   ? 2.07267  1.05271  0.848956 0.235921    -0.117871   -0.302511   20  GLU   B OE2  
1843 H H    . GLU   B 8   ? 1.49104  0.751989 0.600511 0.105675    -0.0793597  -0.177506   20  GLU   B H    
1844 H HA   . GLU   B 8   ? 1.64084  0.900553 0.560327 0.179286    -0.0164983  -0.172004   20  GLU   B HA   
1845 H HB2  . GLU   B 8   ? 1.75444  0.879926 0.679004 0.144791    -0.142314   -0.223717   20  GLU   B HB2  
1846 H HB3  . GLU   B 8   ? 1.8624   0.971186 0.651379 0.188689    -0.121919   -0.223994   20  GLU   B HB3  
1847 H HG2  . GLU   B 8   ? 1.90701  1.03857  0.689546 0.235302    -0.0468668  -0.238579   20  GLU   B HG2  
1848 H HG3  . GLU   B 8   ? 1.7893   0.943629 0.70351  0.192485    -0.0619563  -0.230722   20  GLU   B HG3  
1849 N N    . GLN   B 9   ? 1.57284  0.827966 0.592842 0.106465    -0.107623   -0.140738   21  GLN   B N    
1850 C CA   . GLN   B 9   ? 1.66325  0.907289 0.661272 0.10063     -0.138097   -0.120444   21  GLN   B CA   
1851 C C    . GLN   B 9   ? 1.54542  0.852149 0.658196 0.0702326   -0.117913   -0.0872019  21  GLN   B C    
1852 O O    . GLN   B 9   ? 1.58308  0.88605  0.689221 0.0674126   -0.132854   -0.0617339  21  GLN   B O    
1853 C CB   . GLN   B 9   ? 1.77972  0.98087  0.794349 0.0842382   -0.214978   -0.140645   21  GLN   B CB   
1854 C CG   . GLN   B 9   ? 1.83006  0.962628 0.785081 0.0948605   -0.257895   -0.185831   21  GLN   B CG   
1855 C CD   . GLN   B 9   ? 1.91642  0.990259 0.709964 0.137246    -0.270072   -0.200797   21  GLN   B CD   
1856 O OE1  . GLN   B 9   ? 2.0533   1.11275  0.786296 0.147407    -0.300334   -0.187507   21  GLN   B OE1  
1857 N NE2  . GLN   B 9   ? 1.99571  1.03796  0.716695 0.166292    -0.24285    -0.225754   21  GLN   B NE2  
1858 H H    . GLN   B 9   ? 1.51012  0.782389 0.60452  0.0868543   -0.111378   -0.145019   21  GLN   B H    
1859 H HA   . GLN   B 9   ? 1.73752  0.964964 0.647636 0.12485     -0.124923   -0.112359   21  GLN   B HA   
1860 H HB2  . GLN   B 9   ? 1.66543  0.898039 0.778868 0.0577917   -0.219088   -0.135763   21  GLN   B HB2  
1861 H HB3  . GLN   B 9   ? 1.79985  0.988485 0.774306 0.0912875   -0.235633   -0.127852   21  GLN   B HB3  
1862 H HG2  . GLN   B 9   ? 1.7837   0.92063  0.761507 0.0945565   -0.232937   -0.195523   21  GLN   B HG2  
1863 H HG3  . GLN   B 9   ? 1.81752  0.938252 0.818795 0.0746973   -0.303429   -0.196814   21  GLN   B HG3  
1864 H HE21 . GLN   B 9   ? 2.03311  1.07609  0.68248  0.192921    -0.211636   -0.219122   21  GLN   B HE21 
1865 H HE22 . GLN   B 9   ? 1.98205  1.00199  0.727505 0.160081    -0.254589   -0.248182   21  GLN   B HE22 
1866 N N    . GLY   B 10  ? 1.33254  0.689605 0.546213 0.0501777   -0.0893054  -0.0903163  22  GLY   B N    
1867 C CA   . GLY   B 10  ? 1.24992  0.658581 0.580156 0.0200247   -0.080793   -0.0728292  22  GLY   B CA   
1868 C C    . GLY   B 10  ? 1.21909  0.652635 0.545879 0.0212961   -0.0449794  -0.0391168  22  GLY   B C    
1869 O O    . GLY   B 10  ? 1.22631  0.673576 0.50381  0.0378769   -0.00085715 -0.0302093  22  GLY   B O    
1870 H H    . GLY   B 10  ? 1.35393  0.711972 0.558924 0.058365    -0.0743339  -0.104281   22  GLY   B H    
1871 H HA2  . GLY   B 10  ? 1.23641  0.631489 0.596642 0.00819831  -0.118065   -0.0758978  22  GLY   B HA2  
1872 H HA3  . GLY   B 10  ? 1.17401  0.614102 0.557903 0.0109694   -0.0612914  -0.0803239  22  GLY   B HA3  
1873 N N    . GLU   B 11  ? 1.18755  0.628443 0.578827 0.00290248  -0.0628249  -0.0212135  23  GLU   B N    
1874 C CA   . GLU   B 11  ? 1.17622  0.640428 0.605318 -0.00671698 -0.0295949  0.0112057   23  GLU   B CA   
1875 C C    . GLU   B 11  ? 1.00688  0.535493 0.528637 -0.025909   0.0149288   0.00209599  23  GLU   B C    
1876 O O    . GLU   B 11  ? 0.953043 0.508063 0.544946 -0.0391554  0.00491502  -0.0209973  23  GLU   B O    
1877 C CB   . GLU   B 11  ? 1.2303   0.668118 0.690724 -0.0123531  -0.0770929  0.0244719   23  GLU   B CB   
1878 C CG   . GLU   B 11  ? 1.2968   0.724099 0.77167  -0.0149472  -0.0624012  0.0649321   23  GLU   B CG   
1879 C CD   . GLU   B 11  ? 1.29729  0.71658  0.851636 -0.0225805  -0.10036    0.0747823   23  GLU   B CD   
1880 O OE1  . GLU   B 11  ? 1.31282  0.751105 0.944135 -0.0314683  -0.134796   0.0506192   23  GLU   B OE1  
1881 O OE2  . GLU   B 11  ? 1.42203  0.81502  0.968091 -0.018271   -0.0928719  0.111525    23  GLU   B OE2  
1882 H H    . GLU   B 11  ? 1.18452  0.613656 0.602474 -0.00414977 -0.098527   -0.0303875  23  GLU   B H    
1883 H HA   . GLU   B 11  ? 1.22801  0.676884 0.587549 0.00789969  -0.0104366  0.0279356   23  GLU   B HA   
1884 H HB2  . GLU   B 11  ? 1.29202  0.694287 0.689539 0.00184079  -0.111556   0.020358    23  GLU   B HB2  
1885 H HB3  . GLU   B 11  ? 1.16654  0.626449 0.703572 -0.0269661  -0.0895346  0.00928919  23  GLU   B HB3  
1886 H HG2  . GLU   B 11  ? 1.25317  0.709057 0.76594  -0.026544   -0.0218145  0.0701446   23  GLU   B HG2  
1887 H HG3  . GLU   B 11  ? 1.37349  0.768375 0.762481 0.00230208  -0.0625868  0.0839087   23  GLU   B HG3  
1888 N N    . ASP   B 12  ? 0.978017 0.534591 0.495186 -0.0259168  0.0646346   0.0191952   24  ASP   B N    
1889 C CA   . ASP   B 12  ? 0.913972 0.535081 0.523272 -0.0453765  0.101108    0.010394    24  ASP   B CA   
1890 C C    . ASP   B 12  ? 0.881101 0.502929 0.574083 -0.0697439  0.0955022   0.0223887   24  ASP   B C    
1891 O O    . ASP   B 12  ? 0.928144 0.526333 0.607477 -0.0731431  0.109874    0.0547785   24  ASP   B O    
1892 C CB   . ASP   B 12  ? 0.929543 0.586984 0.52196  -0.0403868  0.153995    0.0241695   24  ASP   B CB   
1893 C CG   . ASP   B 12  ? 0.889084 0.622267 0.58419  -0.0610098  0.184255    0.00895534  24  ASP   B CG   
1894 O OD1  . ASP   B 12  ? 0.851188 0.602198 0.62391  -0.0795664  0.166574    -0.0101992  24  ASP   B OD1  
1895 O OD2  . ASP   B 12  ? 0.893892 0.673715 0.594169 -0.0571595  0.224765    0.0135143   24  ASP   B OD2  
1896 H H    . ASP   B 12  ? 1.05454  0.590812 0.508836 -0.0132852  0.0757337   0.0366432   24  ASP   B H    
1897 H HA   . ASP   B 12  ? 0.86382  0.503974 0.49714  -0.0457306  0.0930042   -0.0127157  24  ASP   B HA   
1898 H HB2  . ASP   B 12  ? 0.969627 0.621619 0.501812 -0.0194591  0.157527    0.0166531   24  ASP   B HB2  
1899 H HB3  . ASP   B 12  ? 0.988654 0.626481 0.559968 -0.0424199  0.166315    0.0510848   24  ASP   B HB3  
1900 N N    . ILE   B 13  ? 0.857645 0.499336 0.629158 -0.0832548  0.0757652   -0.00125348 25  ILE   B N    
1901 C CA   . ILE   B 13  ? 0.849832 0.488753 0.702786 -0.101293   0.0705865   0.00460017  25  ILE   B CA   
1902 C C    . ILE   B 13  ? 0.771233 0.460899 0.708731 -0.122586   0.102867    -0.0111375  25  ILE   B C    
1903 O O    . ILE   B 13  ? 0.863903 0.548523 0.870449 -0.135528   0.0973143   -0.0154828  25  ILE   B O    
1904 C CB   . ILE   B 13  ? 0.804236 0.434388 0.699964 -0.101044   0.0306428   -0.0113417  25  ILE   B CB   
1905 C CG1  . ILE   B 13  ? 0.744509 0.417037 0.670501 -0.103998   0.0316894   -0.0442562  25  ILE   B CG1  
1906 C CG2  . ILE   B 13  ? 0.867683 0.44687  0.698104 -0.084097   -0.011337   0.00391248  25  ILE   B CG2  
1907 C CD1  . ILE   B 13  ? 0.761634 0.43438  0.737914 -0.106153   0.00121121  -0.0568855  25  ILE   B CD1  
1908 H H    . ILE   B 13  ? 0.818063 0.473432 0.591855 -0.0798674  0.0675094   -0.0207112  25  ILE   B H    
1909 H HA   . ILE   B 13  ? 0.891614 0.497984 0.719096 -0.098851   0.0709288   0.0305049   25  ILE   B HA   
1910 H HB   . ILE   B 13  ? 0.797869 0.427926 0.748668 -0.109529   0.0311558   -0.00936646 25  ILE   B HB   
1911 H HG12 . ILE   B 13  ? 0.765463 0.434381 0.639257 -0.0948505  0.0324072   -0.0464461  25  ILE   B HG12 
1912 H HG13 . ILE   B 13  ? 0.716903 0.422895 0.682231 -0.112738   0.0537006   -0.0555926  25  ILE   B HG13 
1913 H HG21 . ILE   B 13  ? 0.85587  0.432271 0.730411 -0.0859556  -0.0350979  -0.00022674 25  ILE   B HG21 
1914 H HG22 . ILE   B 13  ? 0.873683 0.45129  0.66132  -0.0768507  -0.0186596  -0.0067406  25  ILE   B HG22 
1915 H HG23 . ILE   B 13  ? 0.923789 0.474535 0.711219 -0.0776084  -0.0080318  0.0279515   25  ILE   B HG23 
1916 H HD11 . ILE   B 13  ? 0.750669 0.416934 0.768533 -0.10929    -0.00496851 -0.0512914  25  ILE   B HD11 
1917 H HD12 . ILE   B 13  ? 0.705979 0.410338 0.71184  -0.110677   0.0117801   -0.0748102  25  ILE   B HD12 
1918 H HD13 . ILE   B 13  ? 0.775869 0.424467 0.715397 -0.0991007  -0.0224996  -0.0528167  25  ILE   B HD13 
1919 N N    . THR   B 14  ? 0.72818  0.464772 0.664585 -0.124895   0.133663    -0.0207006  26  THR   B N    
1920 C CA   . THR   B 14  ? 0.708658 0.494737 0.727942 -0.147452   0.159395    -0.0359384  26  THR   B CA   
1921 C C    . THR   B 14  ? 0.792292 0.55595  0.837405 -0.166616   0.184114    -0.00459697 26  THR   B C    
1922 O O    . THR   B 14  ? 0.824546 0.549091 0.805373 -0.158117   0.195367    0.0342216   26  THR   B O    
1923 C CB   . THR   B 14  ? 0.675029 0.527276 0.693923 -0.141866   0.180118    -0.0555213  26  THR   B CB   
1924 O OG1  . THR   B 14  ? 0.723752 0.57241  0.67887  -0.128328   0.203998    -0.0295369  26  THR   B OG1  
1925 C CG2  . THR   B 14  ? 0.594811 0.462783 0.591747 -0.123984   0.158668    -0.0823036  26  THR   B CG2  
1926 H H    . THR   B 14  ? 0.750654 0.489781 0.635758 -0.111213   0.136988    -0.0196832  26  THR   B H    
1927 H HA   . THR   B 14  ? 0.679742 0.472345 0.74517  -0.154016   0.146521    -0.0555833  26  THR   B HA   
1928 H HB   . THR   B 14  ? 0.648249 0.536164 0.727722 -0.158281   0.191859    -0.0684834  26  THR   B HB   
1930 H HG21 . THR   B 14  ? 0.590989 0.498784 0.586188 -0.116852   0.169884    -0.0929613  26  THR   B HG21 
1931 H HG22 . THR   B 14  ? 0.628649 0.460304 0.572752 -0.110837   0.145152    -0.0722546  26  THR   B HG22 
1932 H HG23 . THR   B 14  ? 0.576833 0.450578 0.614732 -0.132049   0.147496    -0.0984303  26  THR   B HG23 
1933 N N    . SER   B 15  ? 0.766348 0.553603 0.905247 -0.192909   0.193453    -0.0231687  27  SER   B N    
1934 C CA   . SER   B 15  ? 0.795554 0.564527 0.982576 -0.219371   0.220191    0.00205375  27  SER   B CA   
1935 C C    . SER   B 15  ? 0.819565 0.635896 1.00057  -0.227086   0.261031    0.0187442   27  SER   B C    
1936 O O    . SER   B 15  ? 0.909674 0.696664 1.07675  -0.237328   0.291434    0.0635741   27  SER   B O    
1937 C CB   . SER   B 15  ? 0.791489 0.573544 1.0819   -0.245099   0.214808    -0.0330016  27  SER   B CB   
1938 O OG   . SER   B 15  ? 0.797546 0.519517 1.09566  -0.237005   0.187392    -0.0327109  27  SER   B OG   
1939 H H    . SER   B 15  ? 0.718807 0.532173 0.89186  -0.194597   0.182626    -0.0533571  27  SER   B H    
1940 H HA   . SER   B 15  ? 0.85287  0.566727 1.00827  -0.214171   0.21539     0.0325713   27  SER   B HA   
1941 H HB2  . SER   B 15  ? 0.73734  0.568474 1.04704  -0.243404   0.208623    -0.067574   27  SER   B HB2  
1942 H HB3  . SER   B 15  ? 0.812944 0.594527 1.1459   -0.267412   0.235715    -0.021747   27  SER   B HB3  
1944 N N    . LYS   B 16  ? 0.770307 0.661131 0.960582 -0.218987   0.263341    -0.0144484  28  LYS   B N    
1945 C CA   . LYS   B 16  ? 0.828953 0.785091 1.03608  -0.223646   0.300715    -0.00754429 28  LYS   B CA   
1946 C C    . LYS   B 16  ? 0.846263 0.787781 0.944956 -0.190864   0.318782    0.0239433   28  LYS   B C    
1947 O O    . LYS   B 16  ? 0.801772 0.792143 0.9054   -0.189482   0.357211    0.0374127   28  LYS   B O    
1948 C CB   . LYS   B 16  ? 0.838507 0.88006  1.10062  -0.222051   0.288676    -0.0578017  28  LYS   B CB   
1949 C CG   . LYS   B 16  ? 0.865077 0.943241 1.24467  -0.259286   0.283674    -0.090444   28  LYS   B CG   
1950 C CD   . LYS   B 16  ? 0.909144 1.09275  1.34734  -0.260007   0.285565    -0.12636    28  LYS   B CD   
1951 C CE   . LYS   B 16  ? 0.918522 1.1307   1.33741  -0.236227   0.248207    -0.171278   28  LYS   B CE   
1952 N NZ   . LYS   B 16  ? 0.904505 1.10929  1.38738  -0.259748   0.224014    -0.210055   28  LYS   B NZ   
1953 H H    . LYS   B 16  ? 0.740571 0.643419 0.928339 -0.208729   0.241503    -0.040977   28  LYS   B H    
1954 H HA   . LYS   B 16  ? 0.854799 0.809682 1.11278  -0.249157   0.322168    0.00842921  28  LYS   B HA   
1955 H HB2  . LYS   B 16  ? 0.800478 0.831171 1.02636  -0.203329   0.26377     -0.0748043  28  LYS   B HB2  
1956 H HB3  . LYS   B 16  ? 0.83091  0.917147 1.08441  -0.211999   0.307622    -0.0539126  28  LYS   B HB3  
1957 H HG2  . LYS   B 16  ? 0.906361 0.96367  1.32203  -0.283172   0.30284     -0.0687334  28  LYS   B HG2  
1958 H HG3  . LYS   B 16  ? 0.853349 0.905547 1.23636  -0.258472   0.258687    -0.110592   28  LYS   B HG3  
1959 H HD2  . LYS   B 16  ? 0.909793 1.12157  1.32199  -0.245786   0.305892    -0.109062   28  LYS   B HD2  
1960 H HD3  . LYS   B 16  ? 0.909001 1.11704  1.42704  -0.289888   0.292326    -0.136539   28  LYS   B HD3  
1961 H HE2  . LYS   B 16  ? 0.900573 1.07274  1.24985  -0.213755   0.238943    -0.161168   28  LYS   B HE2  
1962 H HE3  . LYS   B 16  ? 0.886774 1.16191  1.31842  -0.225658   0.249353    -0.185103   28  LYS   B HE3  
1963 H HZ1  . LYS   B 16  ? 0.920104 1.06692  1.39452  -0.266793   0.222777    -0.197643   28  LYS   B HZ1  
1964 H HZ2  . LYS   B 16  ? 0.910714 1.15077  1.46089  -0.282369   0.229245    -0.222996   28  LYS   B HZ2  
1965 H HZ3  . LYS   B 16  ? 0.880529 1.10304  1.34455  -0.243582   0.204674    -0.234714   28  LYS   B HZ3  
1966 N N    . LYS   B 17  ? 0.849737 0.72931  0.854701 -0.163148   0.289761    0.0304405   29  LYS   B N    
1967 C CA   . LYS   B 17  ? 0.86993  0.726664 0.760521 -0.127361   0.295346    0.0471547   29  LYS   B CA   
1968 C C    . LYS   B 17  ? 0.807592 0.732571 0.691786 -0.105112   0.308178    0.0208311   29  LYS   B C    
1969 O O    . LYS   B 17  ? 0.795925 0.742327 0.635994 -0.0861702  0.34296     0.0364077   29  LYS   B O    
1970 C CB   . LYS   B 17  ? 0.989604 0.8086   0.828641 -0.128101   0.330587    0.0984753   29  LYS   B CB   
1971 C CG   . LYS   B 17  ? 1.07055  0.804774 0.882898 -0.135406   0.309162    0.130445    29  LYS   B CG   
1972 C CD   . LYS   B 17  ? 1.1193   0.79391  0.831481 -0.103302   0.261027    0.124845    29  LYS   B CD   
1973 C CE   . LYS   B 17  ? 1.20157  0.803313 0.899033 -0.106583   0.233897    0.154321    29  LYS   B CE   
1974 N NZ   . LYS   B 17  ? 1.14146  0.746981 0.9267   -0.121221   0.196376    0.122223    29  LYS   B NZ   
1975 H H    . LYS   B 17  ? 0.828742 0.678937 0.843922 -0.166531   0.263512    0.0212897   29  LYS   B H    
1976 H HA   . LYS   B 17  ? 0.875489 0.689614 0.722088 -0.114604   0.263675    0.0418008   29  LYS   B HA   
1977 H HB2  . LYS   B 17  ? 0.990542 0.849299 0.88765  -0.147399   0.363625    0.107371    29  LYS   B HB2  
1978 H HB3  . LYS   B 17  ? 1.0276   0.839613 0.788986 -0.101988   0.338301    0.104642    29  LYS   B HB3  
1979 H HG2  . LYS   B 17  ? 1.03106  0.766264 0.917436 -0.156919   0.296859    0.11907     29  LYS   B HG2  
1980 H HG3  . LYS   B 17  ? 1.1347   0.852024 0.924341 -0.139202   0.338657    0.166426    29  LYS   B HG3  
1981 H HD2  . LYS   B 17  ? 1.16905  0.836056 0.802026 -0.0810253  0.271594    0.133722    29  LYS   B HD2  
1982 H HD3  . LYS   B 17  ? 1.05979  0.751958 0.796428 -0.10107    0.236298    0.0921677   29  LYS   B HD3  
1983 H HE2  . LYS   B 17  ? 1.23921  0.829469 0.953964 -0.120336   0.260685    0.184668    29  LYS   B HE2  
1984 H HE3  . LYS   B 17  ? 1.24946  0.812847 0.863589 -0.0837858  0.21349     0.16369     29  LYS   B HE3  
1985 H HZ1  . LYS   B 17  ? 1.08812  0.731469 0.942896 -0.139503   0.212041    0.106702    29  LYS   B HZ1  
1986 H HZ2  . LYS   B 17  ? 1.10718  0.716281 0.872017 -0.108698   0.171422    0.100201    29  LYS   B HZ2  
1987 H HZ3  . LYS   B 17  ? 1.16432  0.730482 0.955567 -0.123526   0.182384    0.139619    29  LYS   B HZ3  
1988 N N    . ASP   B 18  ? 0.69091  0.647354 0.61193  -0.101948   0.280358    -0.017918   30  ASP   B N    
1989 C CA   . ASP   B 18  ? 0.67142  0.689771 0.590371 -0.0771645  0.287607    -0.0413608  30  ASP   B CA   
1990 C C    . ASP   B 18  ? 0.68535  0.656699 0.521503 -0.0452064  0.255264    -0.0555004  30  ASP   B C    
1991 O O    . ASP   B 18  ? 0.641343 0.645925 0.479642 -0.0255177  0.246617    -0.0785899  30  ASP   B O    
1992 C CB   . ASP   B 18  ? 0.609209 0.705584 0.633896 -0.0967281  0.283476    -0.0717606  30  ASP   B CB   
1993 C CG   . ASP   B 18  ? 0.583502 0.655117 0.634839 -0.110523   0.245489    -0.0952296  30  ASP   B CG   
1994 O OD1  . ASP   B 18  ? 0.556206 0.557646 0.553935 -0.104627   0.223333    -0.0868911  30  ASP   B OD1  
1995 O OD2  . ASP   B 18  ? 0.571604 0.697923 0.699702 -0.126705   0.23879     -0.122904   30  ASP   B OD2  
1996 H H    . ASP   B 18  ? 0.676277 0.614489 0.621535 -0.112875   0.257203    -0.0284732  30  ASP   B H    
1997 H HA   . ASP   B 18  ? 0.707269 0.746417 0.609539 -0.0671849  0.31672     -0.0275717  30  ASP   B HA   
1998 H HB2  . ASP   B 18  ? 0.599748 0.738491 0.621781 -0.0767581  0.28576     -0.0853684  30  ASP   B HB2  
1999 H HB3  . ASP   B 18  ? 0.617909 0.742214 0.699573 -0.119482   0.303765    -0.0638923  30  ASP   B HB3  
2000 N N    . ARG   B 19  ? 0.7279   0.619011 0.497245 -0.0422111  0.233717    -0.040892   31  ARG   B N    
2001 C CA   . ARG   B 19  ? 0.762192 0.59941  0.46245  -0.0202769  0.199702    -0.0533119  31  ARG   B CA   
2002 C C    . ARG   B 19  ? 0.710085 0.565729 0.457847 -0.0260713  0.1756      -0.0788506  31  ARG   B C    
2003 O O    . ARG   B 19  ? 0.732134 0.554856 0.432518 -0.00728686 0.156185    -0.0889331  31  ARG   B O    
2004 C CB   . ARG   B 19  ? 0.81483  0.640402 0.428434 0.0186306   0.213658    -0.0552961  31  ARG   B CB   
2005 C CG   . ARG   B 19  ? 0.881365 0.668084 0.416331 0.0301974   0.232022    -0.0295972  31  ARG   B CG   
2006 C CD   . ARG   B 19  ? 0.956011 0.73506  0.405437 0.0742059   0.248892    -0.0395635  31  ARG   B CD   
2007 N NE   . ARG   B 19  ? 0.989409 0.707067 0.38385  0.0928317   0.206775    -0.0643827  31  ARG   B NE   
2008 C CZ   . ARG   B 19  ? 1.05475  0.690937 0.373416 0.0961079   0.170283    -0.064986   31  ARG   B CZ   
2009 N NH1  . ARG   B 19  ? 1.08782  0.694207 0.371468 0.0863895   0.166453    -0.0413847  31  ARG   B NH1  
2010 N NH2  . ARG   B 19  ? 1.1289   0.71006  0.40835  0.108784    0.13346     -0.0890453  31  ARG   B NH2  
2011 H H    . ARG   B 19  ? 0.75755  0.626116 0.526669 -0.0548384  0.239254    -0.02189    31  ARG   B H    
2012 H HA   . ARG   B 19  ? 0.786813 0.575336 0.459361 -0.0254445  0.182438    -0.042263   31  ARG   B HA   
2013 H HB2  . ARG   B 19  ? 0.792653 0.671381 0.435782 0.0265111   0.234734    -0.0621419  31  ARG   B HB2  
2014 H HB3  . ARG   B 19  ? 0.819398 0.609486 0.397253 0.0310032   0.189707    -0.0676594  31  ARG   B HB3  
2015 H HG2  . ARG   B 19  ? 0.914548 0.648148 0.414749 0.0260359   0.206083    -0.023767   31  ARG   B HG2  
2016 H HG3  . ARG   B 19  ? 0.886635 0.705685 0.45893  0.0158254   0.259327    -0.0128853  31  ARG   B HG3  
2017 H HD2  . ARG   B 19  ? 1.02264  0.780108 0.414185 0.0847157   0.264746    -0.0236946  31  ARG   B HD2  
2018 H HD3  . ARG   B 19  ? 0.930815 0.767403 0.420874 0.0808544   0.273018    -0.0454732  31  ARG   B HD3  
2019 H HE   . ARG   B 19  ? 0.960217 0.694367 0.373946 0.10133     0.20419     -0.0788101  31  ARG   B HE   
2020 H HH11 . ARG   B 19  ? 1.1402   0.750297 0.383711 0.0982187   0.191939    -0.0275676  31  ARG   B HH11 
2021 H HH12 . ARG   B 19  ? 1.07941  0.662753 0.379538 0.0696173   0.139096    -0.0381514  31  ARG   B HH12 
2022 H HH21 . ARG   B 19  ? 1.08023  0.674967 0.385908 0.113039    0.133123    -0.101064   31  ARG   B HH21 
2023 H HH22 . ARG   B 19  ? 1.16111  0.690564 0.388846 0.112556    0.108291    -0.0926832  31  ARG   B HH22 
2024 N N    . GLY   B 20  ? 0.66567  0.566263 0.500612 -0.0515819  0.177387    -0.088662   32  GLY   B N    
2025 C CA   . GLY   B 20  ? 0.621778 0.54944  0.494023 -0.0531094  0.161574    -0.112619   32  GLY   B CA   
2026 C C    . GLY   B 20  ? 0.607839 0.481793 0.467937 -0.0587687  0.132291    -0.113319   32  GLY   B C    
2027 O O    . GLY   B 20  ? 0.556205 0.431189 0.412593 -0.0515145  0.121287    -0.124558   32  GLY   B O    
2028 H H    . GLY   B 20  ? 0.664192 0.575081 0.5326   -0.0678917  0.188998    -0.0801472  32  GLY   B H    
2029 H HA2  . GLY   B 20  ? 0.620237 0.566162 0.47097  -0.0337951  0.164909    -0.119536   32  GLY   B HA2  
2030 H HA3  . GLY   B 20  ? 0.588617 0.554695 0.518111 -0.0686433  0.167562    -0.121899   32  GLY   B HA3  
2031 N N    . VAL   B 21  ? 0.634238 0.461996 0.489055 -0.0706832  0.120623    -0.0976735  33  VAL   B N    
2032 C CA   . VAL   B 21  ? 0.626947 0.412169 0.483967 -0.0766591  0.0911007   -0.0971214  33  VAL   B CA   
2033 C C    . VAL   B 21  ? 0.628159 0.353168 0.41649  -0.0672401  0.0744749   -0.078257   33  VAL   B C    
2034 O O    . VAL   B 21  ? 0.64185  0.353683 0.427288 -0.0723838  0.0798904   -0.0601795  33  VAL   B O    
2035 C CB   . VAL   B 21  ? 0.599356 0.394967 0.534017 -0.0975842  0.0847724   -0.10174    33  VAL   B CB   
2036 C CG1  . VAL   B 21  ? 0.603874 0.367986 0.548849 -0.0999852  0.0556393   -0.101453   33  VAL   B CG1  
2037 C CG2  . VAL   B 21  ? 0.564431 0.419815 0.559466 -0.105702   0.102265    -0.125302   33  VAL   B CG2  
2038 H H    . VAL   B 21  ? 0.651342 0.476211 0.503747 -0.074715   0.13157     -0.0854792  33  VAL   B H    
2039 H HA   . VAL   B 21  ? 0.606615 0.391775 0.453525 -0.0700495  0.0848395   -0.105812   33  VAL   B HA   
2040 H HB   . VAL   B 21  ? 0.620152 0.401994 0.559564 -0.103267   0.0875904   -0.0890913  33  VAL   B HB   
2041 H HG11 . VAL   B 21  ? 0.599838 0.363896 0.526434 -0.0943299  0.0525486   -0.107295   33  VAL   B HG11 
2042 H HG12 . VAL   B 21  ? 0.63754  0.36627  0.556479 -0.0975964  0.039718    -0.088407   33  VAL   B HG12 
2043 H HG13 . VAL   B 21  ? 0.577881 0.357989 0.575859 -0.108907   0.0559462   -0.108624   33  VAL   B HG13 
2044 H HG21 . VAL   B 21  ? 0.547555 0.403201 0.586717 -0.116045   0.0983352   -0.130775   33  VAL   B HG21 
2045 H HG22 . VAL   B 21  ? 0.560953 0.439644 0.56068  -0.107216   0.117444    -0.126101   33  VAL   B HG22 
2046 H HG23 . VAL   B 21  ? 0.54693  0.41632  0.531011 -0.0978351  0.101506    -0.13455    33  VAL   B HG23 
2047 N N    . LEU   B 22  ? 0.651267 0.335683 0.387464 -0.054972   0.0511826   -0.0830069  34  LEU   B N    
2048 C CA   . LEU   B 22  ? 0.76485  0.387529 0.430854 -0.0449323  0.0233269   -0.0733831  34  LEU   B CA   
2049 C C    . LEU   B 22  ? 0.753813 0.346475 0.448484 -0.0570373  -0.0197915  -0.0777346  34  LEU   B C    
2050 O O    . LEU   B 22  ? 0.74165  0.342235 0.472872 -0.065127   -0.02684    -0.0909086  34  LEU   B O    
2051 C CB   . LEU   B 22  ? 0.813027 0.409542 0.394312 -0.0190512  0.0277853   -0.082819   34  LEU   B CB   
2052 C CG   . LEU   B 22  ? 0.851314 0.485675 0.408357 -0.00261499 0.0717229   -0.0770901  34  LEU   B CG   
2053 C CD1  . LEU   B 22  ? 0.914396 0.53779  0.411636 0.0271526   0.0810951   -0.0915322  34  LEU   B CD1  
2054 C CD2  . LEU   B 22  ? 0.935764 0.548151 0.439319 0.00352396  0.0808491   -0.0544368  34  LEU   B CD2  
2055 H H    . LEU   B 22  ? 0.644905 0.337609 0.387127 -0.0524122  0.0508072   -0.0935173  34  LEU   B H    
2056 H HA   . LEU   B 22  ? 0.776552 0.39553  0.430821 -0.0448209  0.0308969   -0.0584878  34  LEU   B HA   
2057 H HB2  . LEU   B 22  ? 0.800573 0.398631 0.396577 -0.0194256  0.0231296   -0.094706   34  LEU   B HB2  
2058 H HB3  . LEU   B 22  ? 0.878409 0.430402 0.406118 -0.0109271  0.00577201  -0.0816568  34  LEU   B HB3  
2059 H HG   . LEU   B 22  ? 0.799071 0.480724 0.416412 -0.014476   0.0895276   -0.0772274  34  LEU   B HG   
2060 H HD11 . LEU   B 22  ? 0.876315 0.505923 0.400321 0.0248349   0.0746521   -0.101805   34  LEU   B HD11 
2061 H HD12 . LEU   B 22  ? 0.905099 0.563704 0.400522 0.0375359   0.110439    -0.0877142  34  LEU   B HD12 
2062 H HD13 . LEU   B 22  ? 0.966907 0.540939 0.400659 0.0398803   0.064199    -0.0946858  34  LEU   B HD13 
2063 H HD21 . LEU   B 22  ? 0.914753 0.52644  0.454347 -0.0130786  0.0727008   -0.043115   34  LEU   B HD21 
2064 H HD22 . LEU   B 22  ? 0.99008  0.557153 0.42511  0.0186406   0.0625979   -0.0570988  34  LEU   B HD22 
2065 H HD23 . LEU   B 22  ? 0.931941 0.575619 0.432976 0.0101329   0.113402    -0.0481309  34  LEU   B HD23 
2066 N N    . LYS   B 23  ? 0.838814 0.393902 0.507011 -0.0549085  -0.0502317  -0.0653914  35  LYS   B N    
2067 C CA   . LYS   B 23  ? 0.837331 0.377784 0.551949 -0.0664246  -0.0944793  -0.0693295  35  LYS   B CA   
2068 C C    . LYS   B 23  ? 0.984907 0.467864 0.623984 -0.0536787  -0.142126   -0.070508   35  LYS   B C    
2069 O O    . LYS   B 23  ? 1.1086   0.56285  0.669061 -0.0359291  -0.143906   -0.0548615  35  LYS   B O    
2070 C CB   . LYS   B 23  ? 0.818549 0.375718 0.595594 -0.0739436  -0.0968127  -0.0523212  35  LYS   B CB   
2071 C CG   . LYS   B 23  ? 0.814473 0.378878 0.670763 -0.0847227  -0.135986   -0.0583186  35  LYS   B CG   
2072 C CD   . LYS   B 23  ? 0.819272 0.391089 0.732303 -0.0838985  -0.142646   -0.0414983  35  LYS   B CD   
2073 C CE   . LYS   B 23  ? 0.8121   0.403463 0.818042 -0.0893506  -0.177207   -0.0471486  35  LYS   B CE   
2074 N NZ   . LYS   B 23  ? 0.883012 0.458668 0.908484 -0.076937   -0.192022   -0.0250174  35  LYS   B NZ   
2075 H H    . LYS   B 23  ? 0.869903 0.410859 0.49109  -0.0449405  -0.0432337  -0.0532603  35  LYS   B H    
2076 H HA   . LYS   B 23  ? 0.81199  0.368378 0.569841 -0.0764539  -0.0945541  -0.0813197  35  LYS   B HA   
2077 H HB2  . LYS   B 23  ? 0.775577 0.364882 0.592845 -0.0807707  -0.0664666  -0.0526465  35  LYS   B HB2  
2078 H HB3  . LYS   B 23  ? 0.872208 0.404029 0.600673 -0.0636502  -0.102053   -0.0365841  35  LYS   B HB3  
2079 H HG2  . LYS   B 23  ? 0.860121 0.39616  0.682723 -0.0802926  -0.16991    -0.0617334  35  LYS   B HG2  
2080 H HG3  . LYS   B 23  ? 0.766717 0.359309 0.673455 -0.0955746  -0.124067   -0.070591   35  LYS   B HG3  
2081 H HD2  . LYS   B 23  ? 0.782003 0.376415 0.724702 -0.0890285  -0.109779   -0.0411278  35  LYS   B HD2  
2082 H HD3  . LYS   B 23  ? 0.875854 0.415697 0.732563 -0.0721847  -0.153911   -0.0250932  35  LYS   B HD3  
2083 H HE2  . LYS   B 23  ? 0.846542 0.424763 0.838449 -0.0892646  -0.210043   -0.0530343  35  LYS   B HE2  
2084 H HE3  . LYS   B 23  ? 0.763641 0.390741 0.832405 -0.0996401  -0.157059   -0.058829   35  LYS   B HE3  
2085 H HZ1  . LYS   B 23  ? 0.928051 0.472188 0.899884 -0.0659966  -0.219258   -0.0136789  35  LYS   B HZ1  
2086 H HZ2  . LYS   B 23  ? 0.861717 0.436185 0.881665 -0.0772583  -0.162928   -0.017424   35  LYS   B HZ2  
2087 H HZ3  . LYS   B 23  ? 0.848374 0.445813 0.945339 -0.0787364  -0.203417   -0.0298894  35  LYS   B HZ3  
2088 N N    . ILE   B 24  ? 1.03725  0.504853 0.70578  -0.0643231  -0.183143   -0.0880022  36  ILE   B N    
2089 C CA   . ILE   B 24  ? 1.10328  0.526231 0.729694 -0.0573434  -0.243528   -0.0929674  36  ILE   B CA   
2090 C C    . ILE   B 24  ? 1.05961  0.511253 0.799874 -0.0778031  -0.280516   -0.0956469  36  ILE   B C    
2091 O O    . ILE   B 24  ? 1.01409  0.502897 0.846501 -0.0992217  -0.264525   -0.10332    36  ILE   B O    
2092 C CB   . ILE   B 24  ? 1.18594  0.55379  0.729203 -0.0486002  -0.268166   -0.118426   36  ILE   B CB   
2093 C CG1  . ILE   B 24  ? 1.23163  0.579612 0.670843 -0.0229711  -0.226699   -0.116958   36  ILE   B CG1  
2094 C CG2  . ILE   B 24  ? 1.27697  0.599513 0.773949 -0.0412848  -0.33936    -0.130296   36  ILE   B CG2  
2095 C CD1  . ILE   B 24  ? 1.3332   0.619921 0.687231 -0.00857932 -0.248043   -0.146247   36  ILE   B CD1  
2096 H H    . ILE   B 24  ? 0.979989 0.465839 0.696035 -0.0764858  -0.174216   -0.0967748  36  ILE   B H    
2097 H HA   . ILE   B 24  ? 1.14469  0.554529 0.722542 -0.0429279  -0.245127   -0.0780066  36  ILE   B HA   
2098 H HB   . ILE   B 24  ? 1.15248  0.528185 0.745777 -0.0642757  -0.265751   -0.129876   36  ILE   B HB   
2099 H HG12 . ILE   B 24  ? 1.26877  0.610714 0.65883  -0.00866008 -0.223022   -0.102001   36  ILE   B HG12 
2100 H HG13 . ILE   B 24  ? 1.17071  0.552766 0.646983 -0.0280371  -0.186968   -0.111414   36  ILE   B HG13 
2101 H HG21 . ILE   B 24  ? 1.3361   0.618072 0.774605 -0.0347219  -0.355272   -0.150492   36  ILE   B HG21 
2102 H HG22 . ILE   B 24  ? 1.3169   0.631368 0.763126 -0.0245098  -0.342716   -0.1149     36  ILE   B HG22 
2103 H HG23 . ILE   B 24  ? 1.25362  0.595808 0.83043  -0.0588632  -0.366604   -0.133565   36  ILE   B HG23 
2104 H HD11 . ILE   B 24  ? 1.307    0.589706 0.712388 -0.025846   -0.261709   -0.159325   36  ILE   B HD11 
2105 H HD12 . ILE   B 24  ? 1.33135  0.617255 0.639905 0.00755995  -0.212905   -0.145878   36  ILE   B HD12 
2106 H HD13 . ILE   B 24  ? 1.40451  0.655054 0.697115 0.00314774  -0.283186   -0.153111   36  ILE   B HD13 
2107 N N    . VAL   B 25  ? 1.07994  0.519095 0.81306  -0.0674905  -0.32547    -0.0855331  37  VAL   B N    
2108 C CA   . VAL   B 25  ? 1.07227  0.53903  0.909023 -0.0801693  -0.37215    -0.0899894  37  VAL   B CA   
2109 C C    . VAL   B 25  ? 1.18035  0.617405 1.00464  -0.0902407  -0.428177   -0.118255   37  VAL   B C    
2110 O O    . VAL   B 25  ? 1.25511  0.635364 0.962326 -0.0716498  -0.460991   -0.127968   37  VAL   B O    
2111 C CB   . VAL   B 25  ? 1.16045  0.611672 0.959389 -0.0553793  -0.397699   -0.0646151  37  VAL   B CB   
2112 C CG1  . VAL   B 25  ? 1.20147  0.668231 1.07222  -0.053857   -0.468342   -0.0679605  37  VAL   B CG1  
2113 C CG2  . VAL   B 25  ? 1.12684  0.600468 0.952134 -0.0518881  -0.338859   -0.0386101  37  VAL   B CG2  
2114 H H    . VAL   B 25  ? 1.14031  0.553602 0.799067 -0.0498619  -0.327146   -0.0742622  37  VAL   B H    
2115 H HA   . VAL   B 25  ? 1.01623  0.524723 0.940486 -0.0943502  -0.348043   -0.0892332  37  VAL   B HA   
2116 H HB   . VAL   B 25  ? 1.22941  0.638853 0.924922 -0.0393815  -0.407743   -0.0627796  37  VAL   B HB   
2117 H HG11 . VAL   B 25  ? 1.13873  0.647452 1.11245  -0.0718746  -0.463807   -0.0769189  37  VAL   B HG11 
2118 H HG12 . VAL   B 25  ? 1.26286  0.7017   1.08413  -0.0502825  -0.511064   -0.0823082  37  VAL   B HG12 
2119 H HG13 . VAL   B 25  ? 1.22036  0.683604 1.08463  -0.0373169  -0.475422   -0.046985   37  VAL   B HG13 
2120 H HG21 . VAL   B 25  ? 1.14565  0.614594 0.981163 -0.0402726  -0.357093   -0.0214812  37  VAL   B HG21 
2121 H HG22 . VAL   B 25  ? 1.13483  0.58882  0.888019 -0.0452785  -0.30877    -0.0320061  37  VAL   B HG22 
2122 H HG23 . VAL   B 25  ? 1.04768  0.559154 0.952645 -0.0672932  -0.313827   -0.0463476  37  VAL   B HG23 
2123 N N    . LYS   B 26  ? 1.15054  0.622142 1.08946  -0.120117   -0.434311   -0.132755   38  LYS   B N    
2124 C CA   . LYS   B 26  ? 1.18726  0.62783  1.13069  -0.13704    -0.487644   -0.160915   38  LYS   B CA   
2125 C C    . LYS   B 26  ? 1.24998  0.725074 1.29093  -0.145808   -0.555138   -0.166762   38  LYS   B C    
2126 O O    . LYS   B 26  ? 1.32011  0.758061 1.32038  -0.143458   -0.625129   -0.189144   38  LYS   B O    
2127 C CB   . LYS   B 26  ? 1.16382  0.604705 1.15291  -0.165074   -0.449877   -0.170805   38  LYS   B CB   
2128 C CG   . LYS   B 26  ? 1.19735  0.5988   1.07672  -0.14795    -0.39629    -0.168299   38  LYS   B CG   
2129 C CD   . LYS   B 26  ? 1.2892   0.612836 1.01823  -0.121246   -0.421954   -0.186087   38  LYS   B CD   
2130 C CE   . LYS   B 26  ? 1.33126  0.588241 1.01498  -0.12806    -0.440825   -0.215051   38  LYS   B CE   
2131 N NZ   . LYS   B 26  ? 1.46234  0.647411 1.0028   -0.0974515  -0.478416   -0.238371   38  LYS   B NZ   
2132 H H    . LYS   B 26  ? 1.07321  0.586691 1.08789  -0.130675   -0.403801   -0.125322   38  LYS   B H    
2133 H HA   . LYS   B 26  ? 1.27405  0.663906 1.11375  -0.12051    -0.507236   -0.170123   38  LYS   B HA   
2134 H HB2  . LYS   B 26  ? 1.09979  0.591076 1.1806   -0.179226   -0.422861   -0.16021    38  LYS   B HB2  
2135 H HB3  . LYS   B 26  ? 1.21317  0.63045  1.21674  -0.180116   -0.487368   -0.189359   38  LYS   B HB3  
2136 H HG2  . LYS   B 26  ? 1.13901  0.568631 1.01492  -0.136765   -0.360361   -0.151298   38  LYS   B HG2  
2137 H HG3  . LYS   B 26  ? 1.16075  0.563904 1.07562  -0.164317   -0.373813   -0.170906   38  LYS   B HG3  
2138 H HD2  . LYS   B 26  ? 1.33209  0.646807 1.0372   -0.111807   -0.463589   -0.189111   38  LYS   B HD2  
2139 H HD3  . LYS   B 26  ? 1.27047  0.594852 0.942105 -0.102236   -0.384038   -0.174125   38  LYS   B HD3  
2140 H HE2  . LYS   B 26  ? 1.30887  0.564367 0.987296 -0.127704   -0.397854   -0.209528   38  LYS   B HE2  
2141 H HE3  . LYS   B 26  ? 1.34562  0.606308 1.10348  -0.153462   -0.470588   -0.225166   38  LYS   B HE3  
2142 H HZ1  . LYS   B 26  ? 1.45744  0.639968 0.931097 -0.0745692  -0.445671   -0.22817    38  LYS   B HZ1  
2143 H HZ2  . LYS   B 26  ? 1.49464  0.680802 1.03076  -0.0946201  -0.5198     -0.242291   38  LYS   B HZ2  
2144 H HZ3  . LYS   B 26  ? 1.50666  0.647707 1.02762  -0.102757   -0.493093   -0.259613   38  LYS   B HZ3  
2145 N N    . ARG   B 27  ? 1.19345  0.740443 1.36044  -0.152117   -0.53654    -0.14968    39  ARG   B N    
2146 C CA   . ARG   B 27  ? 1.19929  0.791339 1.46907  -0.152211   -0.597498   -0.151478   39  ARG   B CA   
2147 C C    . ARG   B 27  ? 1.12129  0.74576  1.41558  -0.124436   -0.577009   -0.123043   39  ARG   B C    
2148 O O    . ARG   B 27  ? 1.07322  0.731499 1.41635  -0.127925   -0.511801   -0.110657   39  ARG   B O    
2149 C CB   . ARG   B 27  ? 1.14459  0.800185 1.58236  -0.191595   -0.601198   -0.164302   39  ARG   B CB   
2150 C CG   . ARG   B 27  ? 1.18465  0.882506 1.7277   -0.197007   -0.683401   -0.177551   39  ARG   B CG   
2151 C CD   . ARG   B 27  ? 1.10842  0.888181 1.84293  -0.237357   -0.670532   -0.183299   39  ARG   B CD   
2152 N NE   . ARG   B 27  ? 0.999098 0.842693 1.81069  -0.227799   -0.597942   -0.159657   39  ARG   B NE   
2153 C CZ   . ARG   B 27  ? 0.902306 0.810457 1.83992  -0.255152   -0.544081   -0.155139   39  ARG   B CZ   
2154 N NH1  . ARG   B 27  ? 0.899907 0.818155 1.91219  -0.298249   -0.552466   -0.166873   39  ARG   B NH1  
2155 N NH2  . ARG   B 27  ? 0.811273 0.769401 1.79682  -0.239377   -0.481523   -0.139284   39  ARG   B NH2  
2156 H H    . ARG   B 27  ? 1.12299  0.693148 1.3142   -0.154617   -0.485513   -0.138419   39  ARG   B H    
2157 H HA   . ARG   B 27  ? 1.26902  0.826539 1.47996  -0.142287   -0.652483   -0.162694   39  ARG   B HA   
2158 H HB2  . ARG   B 27  ? 1.15838  0.786342 1.5769   -0.211521   -0.593269   -0.176708   39  ARG   B HB2  
2159 H HB3  . ARG   B 27  ? 1.07541  0.774681 1.57812  -0.194805   -0.553121   -0.151326   39  ARG   B HB3  
2160 H HG2  . ARG   B 27  ? 1.18247  0.898059 1.72965  -0.17151    -0.697624   -0.164421   39  ARG   B HG2  
2161 H HG3  . ARG   B 27  ? 1.25491  0.909868 1.73826  -0.197964   -0.733968   -0.195731   39  ARG   B HG3  
2162 H HD2  . ARG   B 27  ? 1.13888  0.950236 1.94686  -0.241505   -0.726657   -0.193704   39  ARG   B HD2  
2163 H HD3  . ARG   B 27  ? 1.11065  0.868863 1.8426   -0.263781   -0.652649   -0.191979   39  ARG   B HD3  
2164 H HE   . ARG   B 27  ? 0.987588 0.824212 1.75655  -0.201608   -0.589346   -0.148302   39  ARG   B HE   
2165 H HH11 . ARG   B 27  ? 0.944986 0.871659 2.00406  -0.30995    -0.605553   -0.179912   39  ARG   B HH11 
2166 H HH12 . ARG   B 27  ? 0.881262 0.797218 1.89848  -0.315688   -0.505636   -0.161092   39  ARG   B HH12 
2167 H HH21 . ARG   B 27  ? 0.808035 0.742139 1.72347  -0.216708   -0.462887   -0.131685   39  ARG   B HH21 
2168 H HH22 . ARG   B 27  ? 0.783903 0.799075 1.87218  -0.251706   -0.457897   -0.137383   39  ARG   B HH22 
2169 N N    . VAL   B 28  ? 1.18774  0.794603 1.44025  -0.0949312  -0.635648   -0.11367    40  VAL   B N    
2170 C CA   . VAL   B 28  ? 1.1701   0.775157 1.40289  -0.0628886  -0.618672   -0.0819248  40  VAL   B CA   
2171 C C    . VAL   B 28  ? 1.11953  0.802789 1.52418  -0.064782   -0.618049   -0.0781455  40  VAL   B C    
2172 O O    . VAL   B 28  ? 1.1035   0.833483 1.61221  -0.0757195  -0.670497   -0.0947095  40  VAL   B O    
2173 C CB   . VAL   B 28  ? 1.26468  0.813394 1.37421  -0.026329   -0.68012    -0.067092   40  VAL   B CB   
2174 C CG1  . VAL   B 28  ? 1.35466  0.924851 1.51658  -0.0228252  -0.777216   -0.0865587  40  VAL   B CG1  
2175 C CG2  . VAL   B 28  ? 1.25893  0.792584 1.34389  0.00514826  -0.655163   -0.0265645  40  VAL   B CG2  
2176 H H    . VAL   B 28  ? 1.24646  0.838528 1.48057  -0.094526   -0.690162   -0.127493   40  VAL   B H    
2177 H HA   . VAL   B 28  ? 1.13754  0.727678 1.32777  -0.0631218  -0.564032   -0.0723485  40  VAL   B HA   
2178 H HB   . VAL   B 28  ? 1.31123  0.81332  1.3111   -0.0247471  -0.672453   -0.0718588  40  VAL   B HB   
2179 H HG11 . VAL   B 28  ? 1.31048  0.932151 1.58679  -0.0223494  -0.786227   -0.0822241  40  VAL   B HG11 
2180 H HG12 . VAL   B 28  ? 1.34965  0.92163  1.5251   -0.0461174  -0.791781   -0.11299    40  VAL   B HG12 
2181 H HG13 . VAL   B 28  ? 1.43508  0.965739 1.50291  0.00330469  -0.816483   -0.0771781  40  VAL   B HG13 
2182 H HG21 . VAL   B 28  ? 1.34812  0.836292 1.3302   0.0278494   -0.682039   -0.0124086  40  VAL   B HG21 
2183 H HG22 . VAL   B 28  ? 1.2129   0.742735 1.28811  -0.00259601 -0.595244   -0.0191431  40  VAL   B HG22 
2184 H HG23 . VAL   B 28  ? 1.2432   0.815212 1.42567  0.0110419   -0.672276   -0.0221519  40  VAL   B HG23 
2185 N N    . GLY   B 29  ? 1.07224  0.771091 1.51009  -0.0552544  -0.557012   -0.0602151  41  GLY   B N    
2186 C CA   . GLY   B 29  ? 1.03944  0.805693 1.62865  -0.0476048  -0.549935   -0.0577052  41  GLY   B CA   
2187 C C    . GLY   B 29  ? 1.13627  0.9001   1.7469   -0.0105328  -0.619081   -0.0406624  41  GLY   B C    
2188 O O    . GLY   B 29  ? 1.23819  0.957991 1.75619  0.00504064  -0.682813   -0.034556   41  GLY   B O    
2189 H H    . GLY   B 29  ? 1.06619  0.732877 1.4317   -0.0527505  -0.51915    -0.0514491  41  GLY   B H    
2190 H HA2  . GLY   B 29  ? 1.00393  0.819062 1.6819   -0.0681282  -0.549541   -0.0741066  41  GLY   B HA2  
2191 H HA3  . GLY   B 29  ? 0.999285 0.765661 1.5924   -0.0447306  -0.498765   -0.0510939  41  GLY   B HA3  
2192 N N    . ASN   B 30  ? 1.11272  0.922753 1.84215  0.00823855  -0.607304   -0.033694   42  ASN   B N    
2193 C CA   . ASN   B 30  ? 1.19566  1.00421  1.95714  0.0502233   -0.667554   -0.0136988  42  ASN   B CA   
2194 C C    . ASN   B 30  ? 1.17224  0.96495  1.96319  0.0754486   -0.616533   0.0053013   42  ASN   B C    
2195 O O    . ASN   B 30  ? 1.11302  0.942267 1.97638  0.0599667   -0.54991    -0.0108693  42  ASN   B O    
2196 C CB   . ASN   B 30  ? 1.24252  1.1412   2.16097  0.0472059   -0.723747   -0.0340979  42  ASN   B CB   
2197 C CG   . ASN   B 30  ? 1.16492  1.1485   2.23312  0.0199627   -0.660861   -0.0562175  42  ASN   B CG   
2198 O OD1  . ASN   B 30  ? 1.19958  1.21113  2.34618  0.0393408   -0.615979   -0.05244    42  ASN   B OD1  
2199 N ND2  . ASN   B 30  ? 1.14333  1.16337  2.24798  -0.0234951  -0.653091   -0.07888    42  ASN   B ND2  
2200 H H    . ASN   B 30  ? 1.05123  0.893373 1.84157  -0.00275954 -0.559504   -0.0418971  42  ASN   B H    
2201 H HA   . ASN   B 30  ? 1.27504  1.03134  1.93223  0.0635275   -0.704427   5.258e-05   42  ASN   B HA   
2202 H HB2  . ASN   B 30  ? 1.27493  1.18165  2.23099  0.0789523   -0.760792   -0.0212243  42  ASN   B HB2  
2203 H HB3  . ASN   B 30  ? 1.26782  1.16231  2.1538   0.0325241   -0.765071   -0.0455486  42  ASN   B HB3  
2204 H HD21 . ASN   B 30  ? 1.08656  1.11832  2.20244  -0.0432312  -0.599312   -0.0854084  42  ASN   B HD21 
2205 H HD22 . ASN   B 30  ? 1.17087  1.2011   2.28788  -0.0327395  -0.702696   -0.0872976  42  ASN   B HD22 
2206 N N    . GLY   B 31  ? 1.268    0.997821 1.99151  0.113923    -0.645763   0.0395393   43  GLY   B N    
2207 C CA   . GLY   B 31  ? 1.28001  0.986131 2.04474  0.139189    -0.606117   0.0568068   43  GLY   B CA   
2208 C C    . GLY   B 31  ? 1.30684  0.931814 1.94906  0.127647    -0.545116   0.075507    43  GLY   B C    
2209 O O    . GLY   B 31  ? 1.31156  0.928331 1.87713  0.093752    -0.509389   0.0631305   43  GLY   B O    
2210 H H    . GLY   B 31  ? 1.33741  1.03474  1.9859   0.125338    -0.690875   0.0525592   43  GLY   B H    
2211 H HA2  . GLY   B 31  ? 1.34507  1.03533  2.11957  0.172137    -0.64931    0.0771549   43  GLY   B HA2  
2212 H HA3  . GLY   B 31  ? 1.21617  0.976358 2.08633  0.132864    -0.57702    0.0355702   43  GLY   B HA3  
2213 N N    . GLU   B 32  ? 1.3587   0.928756 2.00176  0.157553    -0.535193   0.104538    44  GLU   B N    
2214 C CA   . GLU   B 32  ? 1.42749  0.908589 1.96435  0.154565    -0.492093   0.135618    44  GLU   B CA   
2215 C C    . GLU   B 32  ? 1.35308  0.850718 1.92124  0.119212    -0.411597   0.105006    44  GLU   B C    
2216 O O    . GLU   B 32  ? 1.34881  0.807893 1.82235  0.0946758   -0.37131    0.113139    44  GLU   B O    
2217 C CB   . GLU   B 32  ? 1.42325  0.842718 1.97232  0.20088     -0.521802   0.177497    44  GLU   B CB   
2218 H H    . GLU   B 32  ? 1.37404  0.964799 2.09819  0.181305    -0.556403   0.105012    44  GLU   B H    
2219 H HA   . GLU   B 32  ? 1.44209  0.894232 1.87491  0.147418    -0.502973   0.149948    44  GLU   B HA   
2222 N N    . GLU   B 33  ? 1.24354  0.80562  1.94396  0.118377    -0.388876   0.0677906   45  GLU   B N    
2223 C CA   . GLU   B 33  ? 1.11773  0.686751 1.8546   0.0982523   -0.319958   0.0389847   45  GLU   B CA   
2224 C C    . GLU   B 33  ? 1.02821  0.649061 1.73729  0.058415    -0.2842     0.0081493   45  GLU   B C    
2225 O O    . GLU   B 33  ? 0.920224 0.605646 1.66684  0.0490192   -0.300433   -0.00975849 45  GLU   B O    
2226 C CB   . GLU   B 33  ? 1.0653   0.672435 1.94177  0.123726    -0.309866   0.0130613   45  GLU   B CB   
2227 H H    . GLU   B 33  ? 1.22818  0.834004 1.99801  0.13199     -0.418312   0.0589902   45  GLU   B H    
2228 H HA   . GLU   B 33  ? 1.16227  0.671062 1.8461   0.0962972   -0.302414   0.0578031   45  GLU   B HA   
2231 N N    . THR   B 34  ? 1.04339  0.632551 1.68951  0.0349475   -0.235974   0.00439075  46  THR   B N    
2232 C CA   . THR   B 34  ? 0.966742 0.601438 1.59551  0.0033738   -0.194521   -0.0265665  46  THR   B CA   
2233 C C    . THR   B 34  ? 0.933304 0.597302 1.63885  0.00135446  -0.147826   -0.0638777  46  THR   B C    
2234 O O    . THR   B 34  ? 1.02647  0.65669  1.7779   0.0187061   -0.141059   -0.0656871  46  THR   B O    
2235 C CB   . THR   B 34  ? 1.00395  0.593279 1.51487  -0.0169471  -0.176173   -0.00822416 46  THR   B CB   
2236 O OG1  . THR   B 34  ? 0.950847 0.479132 1.44989  -0.0139159  -0.156408   0.0100064   46  THR   B OG1  
2237 C CG2  . THR   B 34  ? 1.04169  0.605328 1.4622   -0.0120336  -0.219107   0.0209021   46  THR   B CG2  
2238 H H    . THR   B 34  ? 1.07949  0.616736 1.69421  0.0392757   -0.229454   0.0232773   46  THR   B H    
2239 H HA   . THR   B 34  ? 0.944385 0.619557 1.58714  -0.00121346 -0.209796   -0.0347718  46  THR   B HA   
2240 H HB   . THR   B 34  ? 0.926123 0.545305 1.42871  -0.034938   -0.148343   -0.029186   46  THR   B HB   
2242 H HG21 . THR   B 34  ? 1.05292  0.596465 1.40116  -0.0240117  -0.201249   0.0286273   46  THR   B HG21 
2243 H HG22 . THR   B 34  ? 1.10371  0.633261 1.5183   0.00722068  -0.246641   0.044875    46  THR   B HG22 
2244 H HG23 . THR   B 34  ? 1.01829  0.619073 1.45851  -0.0149639  -0.237268   0.00722011  46  THR   B HG23 
2245 N N    . PRO   B 35  ? 0.845229 0.569803 1.56523  -0.0167697  -0.114868   -0.0964969  47  PRO   B N    
2246 C CA   . PRO   B 35  ? 0.80827  0.561329 1.58478  -0.0147831  -0.0714708  -0.135687   47  PRO   B CA   
2247 C C    . PRO   B 35  ? 0.827544 0.525921 1.57102  -0.0229374  -0.0470968  -0.142738   47  PRO   B C    
2248 O O    . PRO   B 35  ? 0.870981 0.540696 1.53598  -0.043635   -0.0425972  -0.125853   47  PRO   B O    
2249 C CB   . PRO   B 35  ? 0.700065 0.51487  1.45595  -0.0355759  -0.0428399  -0.157056   47  PRO   B CB   
2250 C CG   . PRO   B 35  ? 0.750302 0.574122 1.47443  -0.0453146  -0.0765151  -0.131538   47  PRO   B CG   
2251 C CD   . PRO   B 35  ? 0.775012 0.536042 1.45267  -0.0366639  -0.119715   -0.0964152  47  PRO   B CD   
2252 H HA   . PRO   B 35  ? 0.807523 0.57818  1.65511  0.00478088  -0.0767152  -0.144236   47  PRO   B HA   
2253 H HB2  . PRO   B 35  ? 0.713942 0.517671 1.42083  -0.0489414  -0.022589   -0.164708   47  PRO   B HB2  
2254 H HB3  . PRO   B 35  ? 0.704099 0.560814 1.51595  -0.0276756  -0.0250898  -0.178483   47  PRO   B HB3  
2255 H HG2  . PRO   B 35  ? 0.707985 0.538565 1.38074  -0.0618321  -0.0629598  -0.133827   47  PRO   B HG2  
2256 H HG3  . PRO   B 35  ? 0.717425 0.581212 1.50187  -0.0398769  -0.0840164  -0.136029   47  PRO   B HG3  
2257 H HD2  . PRO   B 35  ? 0.797544 0.530847 1.40031  -0.0486349  -0.116501   -0.0857292  47  PRO   B HD2  
2258 H HD3  . PRO   B 35  ? 0.80113  0.573228 1.49933  -0.0303488  -0.152171   -0.0859042  47  PRO   B HD3  
2259 N N    . MET   B 36  ? 0.90356  0.589429 1.71264  -0.00682307 -0.0311108  -0.169861   48  MET   B N    
2260 C CA   . MET   B 36  ? 0.929901 0.568325 1.72774  -0.0186019  -0.00737668 -0.188344   48  MET   B CA   
2261 C C    . MET   B 36  ? 0.863671 0.557703 1.65305  -0.0327823  0.0291528   -0.237496   48  MET   B C    
2262 O O    . MET   B 36  ? 0.779496 0.540623 1.58868  -0.0241818  0.0410834   -0.257059   48  MET   B O    
2263 C CB   . MET   B 36  ? 1.06878  0.658009 1.94238  0.00878551  -0.0112695  -0.200492   48  MET   B CB   
2264 C CG   . MET   B 36  ? 1.15156  0.678799 2.03638  0.0312807   -0.0497925  -0.150222   48  MET   B CG   
2265 S SD   . MET   B 36  ? 1.22773  0.648997 2.04282  0.0109371   -0.0551438  -0.0989563  48  MET   B SD   
2266 C CE   . MET   B 36  ? 1.12524  0.559015 1.82512  -0.0148864  -0.064511   -0.0540425  48  MET   B CE   
2267 H H    . MET   B 36  ? 0.890226 0.598379 1.75818  0.0126251   -0.0359506  -0.179209   48  MET   B H    
2268 H HA   . MET   B 36  ? 0.956406 0.558865 1.70338  -0.0341083  -0.0123243  -0.162586   48  MET   B HA   
2269 H HB2  . MET   B 36  ? 1.03673  0.666786 1.95973  0.0260207   -0.00266431 -0.228347   48  MET   B HB2  
2270 H HB3  . MET   B 36  ? 1.07508  0.631431 1.94421  -0.00309842 0.00428624  -0.216919   48  MET   B HB3  
2271 H HG2  . MET   B 36  ? 1.12656  0.68422  1.99927  0.0360841   -0.0702923  -0.130603   48  MET   B HG2  
2272 H HG3  . MET   B 36  ? 1.17563  0.691391 2.12219  0.0563956   -0.0531037  -0.163164   48  MET   B HG3  
2273 H HE1  . MET   B 36  ? 1.1897   0.571858 1.85375  -0.0261323  -0.0588554  -0.0272192  48  MET   B HE1  
2274 H HE2  . MET   B 36  ? 1.08797  0.569109 1.77065  -0.0324114  -0.0470489  -0.0775191  48  MET   B HE2  
2275 H HE3  . MET   B 36  ? 1.14951  0.593574 1.83988  0.0014428   -0.0925863  -0.033762   48  MET   B HE3  
2276 N N    . ILE   B 37  ? 0.799531 0.467864 1.5617   -0.0542568  0.0464739   -0.256137   49  ILE   B N    
2277 C CA   . ILE   B 37  ? 0.789054 0.504985 1.54331  -0.0621473  0.0742798   -0.308144   49  ILE   B CA   
2278 C C    . ILE   B 37  ? 0.767874 0.507919 1.58565  -0.0321659  0.0883498   -0.353498   49  ILE   B C    
2279 O O    . ILE   B 37  ? 0.745621 0.43698  1.62037  -0.013797   0.082123    -0.363539   49  ILE   B O    
2280 C CB   . ILE   B 37  ? 0.911626 0.590946 1.6529   -0.0879633  0.0822081   -0.326751   49  ILE   B CB   
2281 C CG1  . ILE   B 37  ? 1.00594  0.666642 1.6894   -0.116388   0.0763726   -0.280253   49  ILE   B CG1  
2282 C CG2  . ILE   B 37  ? 0.874941 0.603866 1.60897  -0.0908568  0.102347    -0.388433   49  ILE   B CG2  
2283 C CD1  . ILE   B 37  ? 1.08796  0.811325 1.70726  -0.128472   0.0846465   -0.279091   49  ILE   B CD1  
2284 H H    . ILE   B 37  ? 0.855892 0.477013 1.60557  -0.0637877  0.0399227   -0.23578    49  ILE   B H    
2285 H HA   . ILE   B 37  ? 0.754105 0.51216  1.4707   -0.0689678  0.0791072   -0.303038   49  ILE   B HA   
2286 H HB   . ILE   B 37  ? 0.950022 0.579985 1.73085  -0.0823306  0.0773318   -0.329491   49  ILE   B HB   
2287 H HG12 . ILE   B 37  ? 1.02029  0.653307 1.69755  -0.109505   0.0625134   -0.242791   49  ILE   B HG12 
2288 H HG13 . ILE   B 37  ? 1.04013  0.669301 1.73633  -0.132346   0.0807329   -0.286292   49  ILE   B HG13 
2289 H HG21 . ILE   B 37  ? 0.885806 0.610825 1.60096  -0.112271   0.103499    -0.393706   49  ILE   B HG21 
2290 H HG22 . ILE   B 37  ? 0.844674 0.623669 1.55304  -0.0837717  0.109578    -0.390379   49  ILE   B HG22 
2291 H HG23 . ILE   B 37  ? 0.914296 0.628291 1.68749  -0.0771107  0.106258    -0.420622   49  ILE   B HG23 
2292 H HD11 . ILE   B 37  ? 1.03343  0.783181 1.65318  -0.135401   0.0955868   -0.313006   49  ILE   B HD11 
2293 H HD12 . ILE   B 37  ? 1.04544  0.753445 1.63234  -0.141125   0.0815911   -0.248837   49  ILE   B HD12 
2294 H HD13 . ILE   B 37  ? 1.01625  0.768371 1.62622  -0.11543    0.0819633   -0.274611   49  ILE   B HD13 
2295 N N    . GLY   B 38  ? 0.716937 0.529932 1.52243  -0.0243863  0.11038     -0.379197   50  GLY   B N    
2296 C CA   . GLY   B 38  ? 0.745679 0.590511 1.60157  0.00647376  0.132939    -0.42432    50  GLY   B CA   
2297 C C    . GLY   B 38  ? 0.717759 0.610352 1.62935  0.0299637   0.135274    -0.403761   50  GLY   B C    
2298 O O    . GLY   B 38  ? 0.719741 0.658471 1.67207  0.0566847   0.163241    -0.437127   50  GLY   B O    
2299 H H    . GLY   B 38  ? 0.68899  0.531237 1.45164  -0.0369782  0.113543    -0.367258   50  GLY   B H    
2300 H HA2  . GLY   B 38  ? 0.735039 0.614296 1.55738  0.00403119  0.15192     -0.452268   50  GLY   B HA2  
2301 H HA3  . GLY   B 38  ? 0.785497 0.587344 1.67452  0.0159608   0.129305    -0.444129   50  GLY   B HA3  
2302 N N    . ASP   B 39  ? 0.660751 0.543155 1.57947  0.0219083   0.105367    -0.351715   51  ASP   B N    
2303 C CA   . ASP   B 39  ? 0.659469 0.59342  1.64097  0.037895    0.0995402   -0.331403   51  ASP   B CA   
2304 C C    . ASP   B 39  ? 0.597869 0.609657 1.55705  0.0273049   0.131723    -0.336945   51  ASP   B C    
2305 O O    . ASP   B 39  ? 0.518674 0.532554 1.39633  0.00335092  0.140652    -0.334069   51  ASP   B O    
2306 C CB   . ASP   B 39  ? 0.682915 0.584882 1.6644   0.0302887   0.0524539   -0.279386   51  ASP   B CB   
2307 C CG   . ASP   B 39  ? 0.75072  0.579113 1.76427  0.0497643   0.0208214   -0.263495   51  ASP   B CG   
2308 O OD1  . ASP   B 39  ? 0.840523 0.642756 1.89852  0.0721581   0.0354992   -0.295321   51  ASP   B OD1  
2309 O OD2  . ASP   B 39  ? 0.755708 0.54877  1.7454   0.04515     -0.0190452  -0.219256   51  ASP   B OD2  
2310 H H    . ASP   B 39  ? 0.675884 0.520026 1.56068  0.00600328  0.0874582   -0.329398   51  ASP   B H    
2311 H HA   . ASP   B 39  ? 0.682821 0.621925 1.72525  0.0633221   0.105983    -0.349714   51  ASP   B HA   
2312 H HB2  . ASP   B 39  ? 0.663662 0.549957 1.58004  0.00763938  0.0463357   -0.263599   51  ASP   B HB2  
2313 H HB3  . ASP   B 39  ? 0.661561 0.60715  1.68338  0.0353714   0.0468633   -0.268752   51  ASP   B HB3  
2314 N N    . LYS   B 40  ? 0.629234 0.706051 1.66532  0.0477582   0.153069    -0.344681   52  LYS   B N    
2315 C CA   . LYS   B 40  ? 0.647937 0.797181 1.6795   0.0360614   0.184129    -0.336343   52  LYS   B CA   
2316 C C    . LYS   B 40  ? 0.598594 0.752075 1.64003  0.011       0.147969    -0.289141   52  LYS   B C    
2317 O O    . LYS   B 40  ? 0.605618 0.764205 1.7257   0.0205451   0.11483     -0.271763   52  LYS   B O    
2318 C CB   . LYS   B 40  ? 0.69163  0.910305 1.81539  0.0680742   0.224189    -0.360846   52  LYS   B CB   
2319 C CG   . LYS   B 40  ? 0.740585 1.02726  1.83688  0.0653659   0.28136     -0.369877   52  LYS   B CG   
2320 C CD   . LYS   B 40  ? 0.799367 1.16621  1.9988   0.0960433   0.325587    -0.384687   52  LYS   B CD   
2321 C CE   . LYS   B 40  ? 0.826745 1.26448  2.00729  0.0843202   0.380966    -0.37103    52  LYS   B CE   
2322 N NZ   . LYS   B 40  ? 0.845103 1.36733  2.1531   0.0873084   0.404857    -0.349712   52  LYS   B NZ   
2323 H H    . LYS   B 40  ? 0.653541 0.729276 1.75089  0.0701907   0.149588    -0.353651   52  LYS   B H    
2324 H HA   . LYS   B 40  ? 0.634302 0.781737 1.59649  0.0254549   0.202312    -0.346721   52  LYS   B HA   
2325 H HB2  . LYS   B 40  ? 0.726635 0.923335 1.86216  0.0902812   0.229474    -0.390018   52  LYS   B HB2  
2326 H HB3  . LYS   B 40  ? 0.688085 0.929388 1.88461  0.0721402   0.207659    -0.342029   52  LYS   B HB3  
2327 H HG2  . LYS   B 40  ? 0.711732 1.00819  1.78611  0.0406343   0.275844    -0.340811   52  LYS   B HG2  
2328 H HG3  . LYS   B 40  ? 0.754206 1.02289  1.78235  0.06844     0.296764    -0.394287   52  LYS   B HG3  
2329 H HD2  . LYS   B 40  ? 0.830897 1.18888  2.03145  0.123043    0.341125    -0.420383   52  LYS   B HD2  
2330 H HD3  . LYS   B 40  ? 0.784684 1.16586  2.06571  0.098763    0.303028    -0.367625   52  LYS   B HD3  
2331 H HE2  . LYS   B 40  ? 0.803833 1.22199  1.92578  0.0566477   0.368816    -0.347677   52  LYS   B HE2  
2332 H HE3  . LYS   B 40  ? 0.858556 1.30554  1.99439  0.102283    0.416077    -0.39964    52  LYS   B HE3  
2333 H HZ1  . LYS   B 40  ? 0.814321 1.32972  2.17944  0.0798508   0.367178    -0.333285   52  LYS   B HZ1  
2334 H HZ2  . LYS   B 40  ? 0.863382 1.41824  2.2128   0.115884    0.434164    -0.373328   52  LYS   B HZ2  
2335 H HZ3  . LYS   B 40  ? 0.832193 1.38273  2.12339  0.0687234   0.428661    -0.329426   52  LYS   B HZ3  
2336 N N    . VAL   B 41  ? 0.590199 0.742577 1.5528   -0.0180006  0.152645    -0.271586   53  VAL   B N    
2337 C CA   . VAL   B 41  ? 0.583794 0.721544 1.53249  -0.043359   0.114777    -0.233939   53  VAL   B CA   
2338 C C    . VAL   B 41  ? 0.545755 0.73754  1.5119   -0.0628064  0.139811    -0.218653   53  VAL   B C    
2339 O O    . VAL   B 41  ? 0.544856 0.759251 1.46411  -0.0661481  0.184661    -0.226371   53  VAL   B O    
2340 C CB   . VAL   B 41  ? 0.595654 0.666956 1.43288  -0.0601565  0.0927392   -0.223349   53  VAL   B CB   
2341 C CG1  . VAL   B 41  ? 0.576147 0.62141  1.38992  -0.0796666  0.0496367   -0.190338   53  VAL   B CG1  
2342 C CG2  . VAL   B 41  ? 0.647466 0.66423  1.47156  -0.0466455  0.0762971   -0.234154   53  VAL   B CG2  
2343 H H    . VAL   B 41  ? 0.590196 0.749237 1.50394  -0.0199906  0.179144    -0.28535    53  VAL   B H    
2344 H HA   . VAL   B 41  ? 0.58529  0.718885 1.58781  -0.0361409  0.0853415   -0.224584   53  VAL   B HA   
2345 H HB   . VAL   B 41  ? 0.588251 0.668418 1.37543  -0.0663962  0.118639    -0.231593   53  VAL   B HB   
2346 H HG11 . VAL   B 41  ? 0.588906 0.637725 1.45876  -0.0727788  0.0236566   -0.182563   53  VAL   B HG11 
2347 H HG12 . VAL   B 41  ? 0.570834 0.638122 1.37784  -0.0930942  0.0612808   -0.183692   53  VAL   B HG12 
2348 H HG13 . VAL   B 41  ? 0.588065 0.59032  1.33717  -0.0845548  0.0358484   -0.184206   53  VAL   B HG13 
2349 H HG21 . VAL   B 41  ? 0.639059 0.61848  1.40242  -0.0584812  0.0616987   -0.222111   53  VAL   B HG21 
2350 H HG22 . VAL   B 41  ? 0.643155 0.667895 1.46715  -0.037452   0.101849    -0.259886   53  VAL   B HG22 
2351 H HG23 . VAL   B 41  ? 0.652032 0.662078 1.52939  -0.0347095  0.0549202   -0.2272     53  VAL   B HG23 
2352 N N    . TYR   B 42  ? 0.486931 0.693391 1.51727  -0.0767339  0.105941    -0.194961   54  TYR   B N    
2353 C CA   . TYR   B 42  ? 0.503769 0.757938 1.57795  -0.10064    0.123703    -0.17739    54  TYR   B CA   
2354 C C    . TYR   B 42  ? 0.489654 0.693766 1.51226  -0.129552   0.0758617   -0.154009   54  TYR   B C    
2355 O O    . TYR   B 42  ? 0.508049 0.687586 1.55365  -0.128777   0.0183033   -0.147343   54  TYR   B O    
2356 C CB   . TYR   B 42  ? 0.517873 0.846462 1.74456  -0.0918181  0.123844    -0.177473   54  TYR   B CB   
2357 C CG   . TYR   B 42  ? 0.553234 0.937743 1.84674  -0.0570458  0.172429    -0.203438   54  TYR   B CG   
2358 C CD1  . TYR   B 42  ? 0.579606 0.931621 1.86482  -0.0227606  0.161085    -0.228007   54  TYR   B CD1  
2359 C CD2  . TYR   B 42  ? 0.589913 1.05847  1.9626   -0.0571681  0.230205    -0.202925   54  TYR   B CD2  
2360 C CE1  . TYR   B 42  ? 0.605569 1.00135  1.95281  0.013011    0.202406    -0.25742    54  TYR   B CE1  
2361 C CE2  . TYR   B 42  ? 0.615161 1.13656  2.04676  -0.0198744  0.276549    -0.230181   54  TYR   B CE2  
2362 C CZ   . TYR   B 42  ? 0.619835 1.10268  2.037    0.0168824   0.260905    -0.260707   54  TYR   B CZ   
2363 O OH   . TYR   B 42  ? 0.678602 1.20614  2.15044  0.0570291   0.30588     -0.293163   54  TYR   B OH   
2364 H H    . TYR   B 42  ? 0.511115 0.694867 1.55929  -0.0717032  0.0683882   -0.189368   54  TYR   B H    
2365 H HA   . TYR   B 42  ? 0.500437 0.770482 1.54008  -0.102608   0.1662      -0.180974   54  TYR   B HA   
2366 H HB2  . TYR   B 42  ? 0.524221 0.835828 1.77966  -0.0880365  0.076918    -0.173064   54  TYR   B HB2  
2367 H HB3  . TYR   B 42  ? 0.520656 0.880125 1.78303  -0.113273   0.134434    -0.163276   54  TYR   B HB3  
2368 H HD1  . TYR   B 42  ? 0.579983 0.875703 1.81544  -0.0233959  0.125753    -0.224681   54  TYR   B HD1  
2369 H HD2  . TYR   B 42  ? 0.581676 1.07017  1.96715  -0.0824715  0.240572    -0.183587   54  TYR   B HD2  
2370 H HE1  . TYR   B 42  ? 0.620903 0.985176 1.96091  0.0351532   0.193034    -0.275086   54  TYR   B HE1  
2371 H HE2  . TYR   B 42  ? 0.619388 1.20033  2.09982  -0.0190739  0.320779    -0.228118   54  TYR   B HE2  
2373 N N    . VAL   B 43  ? 0.477903 0.6629   1.42473  -0.150582   0.0980082   -0.142672   55  VAL   B N    
2374 C CA   . VAL   B 43  ? 0.525361 0.65679  1.4188   -0.17502    0.0561955   -0.125489   55  VAL   B CA   
2375 C C    . VAL   B 43  ? 0.567943 0.715342 1.48407  -0.205019   0.0795077   -0.107001   55  VAL   B C    
2376 O O    . VAL   B 43  ? 0.611484 0.799764 1.53996  -0.204887   0.138367    -0.102531   55  VAL   B O    
2377 C CB   . VAL   B 43  ? 0.514176 0.579557 1.27021  -0.169406   0.051728    -0.127491   55  VAL   B CB   
2378 C CG1  . VAL   B 43  ? 0.513104 0.554706 1.24316  -0.145663   0.0344033   -0.141169   55  VAL   B CG1  
2379 C CG2  . VAL   B 43  ? 0.503105 0.578284 1.19747  -0.169668   0.106532    -0.126748   55  VAL   B CG2  
2380 H H    . VAL   B 43  ? 0.488692 0.691797 1.41388  -0.147296   0.138918    -0.146351   55  VAL   B H    
2381 H HA   . VAL   B 43  ? 0.52792  0.652097 1.45768  -0.175629   0.0142352   -0.124109   55  VAL   B HA   
2382 H HB   . VAL   B 43  ? 0.532273 0.561464 1.25693  -0.181707   0.021533    -0.118443   55  VAL   B HB   
2383 H HG11 . VAL   B 43  ? 0.501622 0.570354 1.25292  -0.132997   0.0633792   -0.154273   55  VAL   B HG11 
2384 H HG12 . VAL   B 43  ? 0.519763 0.557131 1.29082  -0.142644   0.00080787  -0.137948   55  VAL   B HG12 
2385 H HG13 . VAL   B 43  ? 0.516022 0.518523 1.16799  -0.145565   0.0280882   -0.139749   55  VAL   B HG13 
2386 H HG21 . VAL   B 43  ? 0.504243 0.550029 1.12519  -0.161335   0.104906    -0.132437   55  VAL   B HG21 
2387 H HG22 . VAL   B 43  ? 0.521411 0.589634 1.21114  -0.186256   0.110391    -0.11228    55  VAL   B HG22 
2388 H HG23 . VAL   B 43  ? 0.501608 0.618805 1.23388  -0.160155   0.138658    -0.134996   55  VAL   B HG23 
2389 N N    . HIS   B 44  ? 0.592395 0.695406 1.49483  -0.228993   0.0335871   -0.0964437  56  HIS   B N    
2390 C CA   . HIS   B 44  ? 0.663511 0.738846 1.53441  -0.25667    0.0503905   -0.0786985  56  HIS   B CA   
2391 C C    . HIS   B 44  ? 0.663666 0.654689 1.39506  -0.251737   0.0287153   -0.0792171  56  HIS   B C    
2392 O O    . HIS   B 44  ? 0.612412 0.563363 1.29669  -0.24053    -0.0189468  -0.0899313  56  HIS   B O    
2393 C CB   . HIS   B 44  ? 0.712631 0.802226 1.69097  -0.292251   0.0192268   -0.0697926  56  HIS   B CB   
2394 C CG   . HIS   B 44  ? 0.759556 0.930193 1.86318  -0.309516   0.0708331   -0.0557109  56  HIS   B CG   
2395 N ND1  . HIS   B 44  ? 0.784434 0.960588 1.85865  -0.318412   0.13849     -0.033938   56  HIS   B ND1  
2396 C CD2  . HIS   B 44  ? 0.725083 0.976895 1.98005  -0.316713   0.0691399   -0.0576284  56  HIS   B CD2  
2397 C CE1  . HIS   B 44  ? 0.737945 0.994182 1.93856  -0.333008   0.180264    -0.0213372  56  HIS   B CE1  
2398 N NE2  . HIS   B 44  ? 0.703124 1.01041  2.02034  -0.331986   0.139844    -0.037219   56  HIS   B NE2  
2399 H H    . HIS   B 44  ? 0.606263 0.691891 1.5165   -0.226708   -0.0101917  -0.1009     56  HIS   B H    
2400 H HA   . HIS   B 44  ? 0.651704 0.754646 1.52277  -0.254464   0.0996305   -0.0719002  56  HIS   B HA   
2401 H HB2  . HIS   B 44  ? 0.71555  0.808798 1.72911  -0.288107   -0.0258163  -0.0801842  56  HIS   B HB2  
2402 H HB3  . HIS   B 44  ? 0.747368 0.786626 1.67809  -0.308249   0.00650536  -0.0634049  56  HIS   B HB3  
2404 H HD2  . HIS   B 44  ? 0.713634 0.982875 2.022    -0.310626   0.0280161   -0.0691823  56  HIS   B HD2  
2405 H HE1  . HIS   B 44  ? 0.764686 1.0406   1.96996  -0.340239   0.231911    -0.00284407 56  HIS   B HE1  
2407 N N    . TYR   B 45  ? 0.655185 0.619456 1.32217  -0.258418   0.0644732   -0.0647775  57  TYR   B N    
2408 C CA   . TYR   B 45  ? 0.647931 0.541689 1.18761  -0.246315   0.0496428   -0.0669235  57  TYR   B CA   
2409 C C    . TYR   B 45  ? 0.688289 0.535984 1.19055  -0.263497   0.0653821   -0.0469165  57  TYR   B C    
2410 O O    . TYR   B 45  ? 0.736447 0.612396 1.2894   -0.279437   0.106424    -0.026866   57  TYR   B O    
2411 C CB   . TYR   B 45  ? 0.579473 0.485413 1.04337  -0.215149   0.0771866   -0.0773218  57  TYR   B CB   
2412 C CG   . TYR   B 45  ? 0.569988 0.504731 1.00742  -0.207241   0.135236    -0.0669985  57  TYR   B CG   
2413 C CD1  . TYR   B 45  ? 0.57803  0.580506 1.07745  -0.201715   0.175757    -0.0702804  57  TYR   B CD1  
2414 C CD2  . TYR   B 45  ? 0.611487 0.506116 0.954353 -0.198963   0.148757    -0.0554699  57  TYR   B CD2  
2415 C CE1  . TYR   B 45  ? 0.58636  0.61479  1.04621  -0.190029   0.228701    -0.0612634  57  TYR   B CE1  
2416 C CE2  . TYR   B 45  ? 0.66979  0.588874 0.977971 -0.187504   0.1978      -0.0427538  57  TYR   B CE2  
2417 C CZ   . TYR   B 45  ? 0.648952 0.634953 1.01199  -0.183913   0.238251    -0.0450552  57  TYR   B CZ   
2418 O OH   . TYR   B 45  ? 0.623112 0.630988 0.937278 -0.169281   0.286361    -0.0316553  57  TYR   B OH   
2419 H H    . TYR   B 45  ? 0.664426 0.654541 1.36632  -0.268456   0.0985212   -0.0523474  57  TYR   B H    
2420 H HA   . TYR   B 45  ? 0.652751 0.516811 1.18042  -0.246613   0.00697856  -0.075552   57  TYR   B HA   
2421 H HB2  . TYR   B 45  ? 0.59335  0.458247 0.987035 -0.206791   0.0591259   -0.0809498  57  TYR   B HB2  
2422 H HB3  . TYR   B 45  ? 0.558995 0.494007 1.05935  -0.206514   0.072377    -0.0886634  57  TYR   B HB3  
2423 H HD1  . TYR   B 45  ? 0.551535 0.582961 1.11903  -0.203454   0.167122    -0.0788957  57  TYR   B HD1  
2424 H HD2  . TYR   B 45  ? 0.634008 0.482407 0.934405 -0.199619   0.123718    -0.0549558  57  TYR   B HD2  
2425 H HE1  . TYR   B 45  ? 0.591851 0.666109 1.09082  -0.184858   0.258095    -0.0645925  57  TYR   B HE1  
2426 H HE2  . TYR   B 45  ? 0.682918 0.572893 0.927908 -0.179724   0.203913    -0.0323305  57  TYR   B HE2  
2428 N N    . LYS   B 46  ? 0.696085 0.469971 1.1079   -0.257592   0.0340681   -0.0516106  58  LYS   B N    
2429 C CA   . LYS   B 46  ? 0.748482 0.463105 1.09436  -0.260491   0.0495332   -0.0351679  58  LYS   B CA   
2430 C C    . LYS   B 46  ? 0.716326 0.403675 0.943505 -0.224733   0.0525142   -0.0436428  58  LYS   B C    
2431 O O    . LYS   B 46  ? 0.771839 0.454405 0.964051 -0.208889   0.0243452   -0.0628565  58  LYS   B O    
2432 C CB   . LYS   B 46  ? 0.781589 0.428967 1.14809  -0.289101   0.00773761  -0.0357698  58  LYS   B CB   
2433 C CG   . LYS   B 46  ? 0.793724 0.480701 1.29816  -0.327661   -0.00518803 -0.0325819  58  LYS   B CG   
2434 C CD   . LYS   B 46  ? 0.856418 0.473706 1.38573  -0.359901   -0.054146   -0.0396771  58  LYS   B CD   
2435 C CE   . LYS   B 46  ? 0.857947 0.510521 1.50655  -0.388861   -0.104076   -0.0557045  58  LYS   B CE   
2436 N NZ   . LYS   B 46  ? 0.933663 0.513741 1.60787  -0.425332   -0.1452     -0.0629749  58  LYS   B NZ   
2437 H H    . LYS   B 46  ? 0.696853 0.454897 1.08545  -0.249137   0.00251261  -0.0650908  58  LYS   B H    
2438 H HA   . LYS   B 46  ? 0.740809 0.480573 1.10897  -0.265564   0.0884655   -0.0178018  58  LYS   B HA   
2439 H HB2  . LYS   B 46  ? 0.799312 0.41424  1.12277  -0.279279   -0.0291424  -0.0532676  58  LYS   B HB2  
2440 H HB3  . LYS   B 46  ? 0.830807 0.436869 1.16103  -0.291302   0.0237497   -0.0218908  58  LYS   B HB3  
2441 H HG2  . LYS   B 46  ? 0.784311 0.506131 1.33182  -0.3371     0.0367892   -0.0132685  58  LYS   B HG2  
2442 H HG3  . LYS   B 46  ? 0.75276  0.480083 1.29345  -0.321773   -0.0232093  -0.0457874  58  LYS   B HG3  
2443 H HD2  . LYS   B 46  ? 0.884042 0.445548 1.32988  -0.343738   -0.0801729  -0.0534677  58  LYS   B HD2  
2444 H HD3  . LYS   B 46  ? 0.893885 0.489488 1.43671  -0.376975   -0.027904   -0.0201214  58  LYS   B HD3  
2445 H HE2  . LYS   B 46  ? 0.82584  0.542886 1.5627   -0.401086   -0.0773829  -0.0437072  58  LYS   B HE2  
2446 H HE3  . LYS   B 46  ? 0.837793 0.495869 1.46082  -0.370884   -0.137632   -0.0740819  58  LYS   B HE3  
2447 H HZ1  . LYS   B 46  ? 0.957479 0.530701 1.66251  -0.444561   -0.112652   -0.0425901  58  LYS   B HZ1  
2448 H HZ2  . LYS   B 46  ? 0.969857 0.487613 1.55766  -0.411057   -0.167523   -0.0757733  58  LYS   B HZ2  
2449 H HZ3  . LYS   B 46  ? 0.940439 0.543833 1.68703  -0.442498   -0.181491   -0.0756988  58  LYS   B HZ3  
2450 N N    . GLY   B 47  ? 0.696612 0.373383 0.866836 -0.210795   0.0896841   -0.0264842  59  GLY   B N    
2451 C CA   . GLY   B 47  ? 0.661842 0.336877 0.738379 -0.175031   0.0980742   -0.0342814  59  GLY   B CA   
2452 C C    . GLY   B 47  ? 0.719611 0.334984 0.723032 -0.16183    0.109659    -0.0151838  59  GLY   B C    
2453 O O    . GLY   B 47  ? 0.771142 0.365247 0.795212 -0.177802   0.131473    0.0113182   59  GLY   B O    
2454 H H    . GLY   B 47  ? 0.727476 0.39961  0.919602 -0.223456   0.110133    -0.00814201 59  GLY   B H    
2455 H HA2  . GLY   B 47  ? 0.655338 0.318407 0.710873 -0.167681   0.0722412   -0.0503728  59  GLY   B HA2  
2456 H HA3  . GLY   B 47  ? 0.634152 0.359365 0.71735  -0.165317   0.121854    -0.0360701  59  GLY   B HA3  
2457 N N    . LYS   B 48  ? 0.730431 0.320491 0.65281  -0.131291   0.0976051   -0.0264954  60  LYS   B N    
2458 C CA   . LYS   B 48  ? 0.826935 0.365217 0.674487 -0.106879   0.106916    -0.0112499  60  LYS   B CA   
2459 C C    . LYS   B 48  ? 0.818353 0.381127 0.59938  -0.0670343  0.105616    -0.0270678  60  LYS   B C    
2460 O O    . LYS   B 48  ? 0.795043 0.393872 0.583229 -0.0636543  0.0926965   -0.0498647  60  LYS   B O    
2461 C CB   . LYS   B 48  ? 0.958037 0.398363 0.784187 -0.115354   0.0772537   -0.0121088  60  LYS   B CB   
2462 C CG   . LYS   B 48  ? 1.00581  0.418778 0.839486 -0.126358   0.0328529   -0.0414277  60  LYS   B CG   
2463 C CD   . LYS   B 48  ? 1.13514  0.443165 0.931138 -0.128704   0.00133348  -0.0498089  60  LYS   B CD   
2464 C CE   . LYS   B 48  ? 1.24604  0.507802 0.948539 -0.0845265  0.0104126   -0.0493554  60  LYS   B CE   
2465 N NZ   . LYS   B 48  ? 1.40295  0.555395 1.06258  -0.0811019  -0.0194018  -0.063243   60  LYS   B NZ   
2466 H H    . LYS   B 48  ? 0.706925 0.313869 0.622778 -0.123998   0.0837833   -0.0435828  60  LYS   B H    
2467 H HA   . LYS   B 48  ? 0.847528 0.396602 0.698557 -0.107498   0.133197    0.00942849  60  LYS   B HA   
2468 H HB2  . LYS   B 48  ? 0.989658 0.398707 0.757048 -0.0893899  0.0802013   -0.00870259 60  LYS   B HB2  
2469 H HB3  . LYS   B 48  ? 0.986503 0.40389  0.847851 -0.137863   0.0847634   0.00509099  60  LYS   B HB3  
2470 H HG2  . LYS   B 48  ? 0.972638 0.413507 0.868294 -0.15119    0.0261003   -0.0434479  60  LYS   B HG2  
2471 H HG3  . LYS   B 48  ? 0.970543 0.408763 0.772295 -0.105971   0.0299581   -0.0548922  60  LYS   B HG3  
2472 H HD2  . LYS   B 48  ? 1.17285  0.453151 1.00797  -0.153102   0.00362049  -0.0360006  60  LYS   B HD2  
2473 H HD3  . LYS   B 48  ? 1.1415   0.438344 0.937452 -0.134148   -0.0284131  -0.0703298  60  LYS   B HD3  
2474 H HE2  . LYS   B 48  ? 1.20891  0.505541 0.881174 -0.062236   0.0112267   -0.0618766  60  LYS   B HE2  
2475 H HE3  . LYS   B 48  ? 1.24616  0.516789 0.944676 -0.0767596  0.0364801   -0.0275416  60  LYS   B HE3  
2476 H HZ1  . LYS   B 48  ? 1.38783  0.53146  1.0339   -0.0805668  -0.043851   -0.0857059  60  LYS   B HZ1  
2477 H HZ2  . LYS   B 48  ? 1.4173   0.535928 1.11408  -0.107337   -0.0235535  -0.0535907  60  LYS   B HZ2  
2478 H HZ3  . LYS   B 48  ? 1.41728  0.543088 1.02662  -0.0523344  -0.00974099 -0.059799   60  LYS   B HZ3  
2479 N N    . LEU   B 49  ? 0.880436 0.427874 0.603194 -0.0370561  0.121175    -0.011507   61  LEU   B N    
2480 C CA   . LEU   B 49  ? 0.910991 0.478345 0.576166 0.00382932  0.118141    -0.0240314  61  LEU   B CA   
2481 C C    . LEU   B 49  ? 0.999127 0.489329 0.625052 0.0148623   0.0934262   -0.0344983  61  LEU   B C    
2482 O O    . LEU   B 49  ? 1.03246  0.444129 0.659841 -0.00228863 0.0829083   -0.0247318  61  LEU   B O    
2483 C CB   . LEU   B 49  ? 0.929808 0.502209 0.54557  0.0369968   0.138238    -0.00097409 61  LEU   B CB   
2484 C CG   . LEU   B 49  ? 0.956119 0.591318 0.588879 0.031627    0.16505     0.0121594   61  LEU   B CG   
2485 C CD1  . LEU   B 49  ? 1.0311   0.664595 0.595607 0.0730133   0.177673    0.0358181   61  LEU   B CD1  
2486 C CD2  . LEU   B 49  ? 0.874275 0.596079 0.545545 0.0255661   0.162032    -0.0204392  61  LEU   B CD2  
2487 H H    . LEU   B 49  ? 0.920862 0.445304 0.641938 -0.0414092  0.134802    0.00982016  61  LEU   B H    
2488 H HA   . LEU   B 49  ? 0.852233 0.474705 0.535487 0.00381858  0.117587    -0.04075    61  LEU   B HA   
2489 H HB2  . LEU   B 49  ? 1.0072   0.514948 0.602388 0.0383799   0.137971    0.0168613   61  LEU   B HB2  
2490 H HB3  . LEU   B 49  ? 0.939959 0.534549 0.526878 0.0650022   0.133285    -0.0118175  61  LEU   B HB3  
2491 H HG   . LEU   B 49  ? 0.961755 0.576789 0.625297 0.00556341  0.174881    0.0263757   61  LEU   B HG   
2492 H HD11 . LEU   B 49  ? 1.08708  0.655338 0.630132 0.0748975   0.180234    0.0589342   61  LEU   B HD11 
2493 H HD12 . LEU   B 49  ? 1.02347  0.69768  0.588075 0.0730025   0.194481    0.0426816   61  LEU   B HD12 
2494 H HD13 . LEU   B 49  ? 1.01592  0.672519 0.557702 0.0992102   0.165984    0.0212303   61  LEU   B HD13 
2495 H HD21 . LEU   B 49  ? 0.844366 0.565318 0.560921 -0.00138733 0.158534    -0.0274146  61  LEU   B HD21 
2496 H HD22 . LEU   B 49  ? 0.856719 0.590825 0.51411  0.0412047   0.149429    -0.0361012  61  LEU   B HD22 
2497 H HD23 . LEU   B 49  ? 0.869487 0.6348   0.535015 0.0337298   0.176135    -0.0189638  61  LEU   B HD23 
2498 N N    . SER   B 50  ? 0.987059 0.500265 0.580508 0.0429008   0.0864664   -0.0548931  62  SER   B N    
2499 C CA   . SER   B 50  ? 1.1656   0.608234 0.707043 0.0636779   0.0684336   -0.0679449  62  SER   B CA   
2500 C C    . SER   B 50  ? 1.16727  0.541142 0.654826 0.0976012   0.0717437   -0.0534819  62  SER   B C    
2501 O O    . SER   B 50  ? 1.29431  0.576834 0.750108 0.100461    0.0541839   -0.0609691  62  SER   B O    
2502 C CB   . SER   B 50  ? 1.11259  0.606364 0.636794 0.0864538   0.0700235   -0.0886809  62  SER   B CB   
2503 O OG   . SER   B 50  ? 1.14784  0.72213  0.680578 0.109617    0.0894507   -0.084538   62  SER   B OG   
2504 H H    . SER   B 50  ? 0.963755 0.537794 0.568316 0.0494725   0.0943409   -0.0617849  62  SER   B H    
2505 H HA   . SER   B 50  ? 1.1372   0.538244 0.690639 0.0403538   0.0520765   -0.0733129  62  SER   B HA   
2506 H HB2  . SER   B 50  ? 1.18196  0.632833 0.66417  0.107518    0.0634839   -0.096854   62  SER   B HB2  
2507 H HB3  . SER   B 50  ? 1.09853  0.614167 0.649158 0.0650368   0.0645753   -0.0964333  62  SER   B HB3  
2509 N N    . ASN   B 51  ? 1.19815  0.609068 0.673441 0.123766    0.0908502   -0.0334506  63  ASN   B N    
2510 C CA   . ASN   B 51  ? 1.29176  0.630695 0.718412 0.155742    0.0946441   -0.0101572  63  ASN   B CA   
2511 C C    . ASN   B 51  ? 1.37335  0.611887 0.809478 0.122439    0.092214    0.0128066   63  ASN   B C    
2512 O O    . ASN   B 51  ? 1.43896  0.593839 0.834242 0.145578    0.0935037   0.0329979   63  ASN   B O    
2513 C CB   . ASN   B 51  ? 1.29377  0.695045 0.703997 0.188164    0.11198     0.0115266   63  ASN   B CB   
2514 C CG   . ASN   B 51  ? 1.37998  0.808615 0.81744  0.157377    0.130445    0.0378802   63  ASN   B CG   
2515 O OD1  . ASN   B 51  ? 1.39766  0.828367 0.886249 0.109283    0.133023    0.0352283   63  ASN   B OD1  
2516 N ND2  . ASN   B 51  ? 1.40591  0.860917 0.808506 0.187798    0.144092    0.0635584   63  ASN   B ND2  
2517 H H    . ASN   B 51  ? 1.13958  0.620002 0.63517  0.123083    0.100031    -0.0345286  63  ASN   B H    
2518 H HA   . ASN   B 51  ? 1.32903  0.638187 0.722866 0.183171    0.0864393   -0.0234127  63  ASN   B HA   
2519 H HB2  . ASN   B 51  ? 1.37959  0.733955 0.750533 0.219462    0.111359    0.0246408   63  ASN   B HB2  
2520 H HB3  . ASN   B 51  ? 1.26361  0.736146 0.681885 0.202238    0.111707    -0.00526974 63  ASN   B HB3  
2521 H HD21 . ASN   B 51  ? 1.42418  0.875924 0.829125 0.174102    0.15826     0.0847299   63  ASN   B HD21 
2522 H HD22 . ASN   B 51  ? 1.41722  0.895045 0.793263 0.223162    0.138974    0.0599539   63  ASN   B HD22 
2523 N N    . GLY   B 52  ? 1.35973  0.609902 0.857371 0.0687815   0.0906032   0.0129283   64  GLY   B N    
2524 C CA   . GLY   B 52  ? 1.44167  0.606833 0.971609 0.0275565   0.0837352   0.0273421   64  GLY   B CA   
2525 C C    . GLY   B 52  ? 1.47304  0.62226  1.0139   0.0168465   0.115313    0.075322    64  GLY   B C    
2526 O O    . GLY   B 52  ? 1.4918   0.554176 1.05195  -0.0105766  0.115311    0.0959165   64  GLY   B O    
2527 H H    . GLY   B 52  ? 1.28874  0.605972 0.81549  0.0572007   0.0939303   0.00350696  64  GLY   B H    
2528 H HA2  . GLY   B 52  ? 1.3911   0.580268 0.967866 -0.00470842 0.0741197   0.0146362   64  GLY   B HA2  
2529 H HA3  . GLY   B 52  ? 1.49601  0.586666 0.99599  0.037887    0.0669596   0.0176309   64  GLY   B HA3  
2530 N N    . LYS   B 53  ? 1.41617  0.647345 0.94317  0.0376919   0.142653    0.0934818   65  LYS   B N    
2531 C CA   . LYS   B 53  ? 1.48021  0.691421 0.986863 0.0428557   0.175185    0.142865    65  LYS   B CA   
2532 C C    . LYS   B 53  ? 1.4222   0.718575 0.98205  0.0104977   0.205668    0.156307    65  LYS   B C    
2533 O O    . LYS   B 53  ? 1.52934  0.813388 1.07595  0.00818391  0.239704    0.200627    65  LYS   B O    
2534 C CB   . LYS   B 53  ? 1.496    0.690051 0.915893 0.107877    0.174671    0.155658    65  LYS   B CB   
2535 H H    . LYS   B 53  ? 1.35738  0.655952 0.884859 0.0491774   0.140676    0.0749045   65  LYS   B H    
2536 H HA   . LYS   B 53  ? 1.53698  0.669848 1.05454  0.0232895   0.174567    0.159205    65  LYS   B HA   
2539 N N    . LYS   B 54  ? 1.29448  0.66883  0.914678 -0.0146757  0.197258    0.122138    66  LYS   B N    
2540 C CA   . LYS   B 54  ? 1.22787  0.668796 0.911523 -0.0477786  0.226093    0.13196     66  LYS   B CA   
2541 C C    . LYS   B 54  ? 1.18239  0.644809 0.955168 -0.0900686  0.203823    0.10107     66  LYS   B C    
2542 O O    . LYS   B 54  ? 1.11403  0.585606 0.883317 -0.0824164  0.170555    0.0645066   66  LYS   B O    
2543 C CB   . LYS   B 54  ? 1.13735  0.676311 0.791907 -0.0196535  0.247819    0.126136    66  LYS   B CB   
2544 H H    . LYS   B 54  ? 1.25642  0.641896 0.877474 -0.00898152 0.174897    0.0932693   66  LYS   B H    
2545 H HA   . LYS   B 54  ? 1.28644  0.690857 0.977036 -0.0618908  0.247508    0.16495     66  LYS   B HA   
2548 N N    . PHE   B 55  ? 1.13574  0.611076 0.988651 -0.13207    0.224536    0.11901     67  PHE   B N    
2549 C CA   . PHE   B 55  ? 1.11107  0.617355 1.0619   -0.171228   0.204346    0.0950197   67  PHE   B CA   
2550 C C    . PHE   B 55  ? 1.06459  0.658718 1.08538  -0.187783   0.243107    0.104091    67  PHE   B C    
2551 O O    . PHE   B 55  ? 1.14716  0.76011  1.14901  -0.181101   0.290005    0.136937    67  PHE   B O    
2552 C CB   . PHE   B 55  ? 1.15709  0.593298 1.17312  -0.214963   0.182068    0.101546    67  PHE   B CB   
2553 C CG   . PHE   B 55  ? 1.32039  0.65147  1.26047  -0.197226   0.153777    0.0986603   67  PHE   B CG   
2554 C CD1  . PHE   B 55  ? 1.49596  0.76479  1.37253  -0.177871   0.180405    0.136086    67  PHE   B CD1  
2555 C CD2  . PHE   B 55  ? 1.3519   0.644808 1.27634  -0.194147   0.10244     0.0593761   67  PHE   B CD2  
2556 C CE1  . PHE   B 55  ? 1.62803  0.796597 1.43583  -0.155188   0.154943    0.131078    67  PHE   B CE1  
2557 C CE2  . PHE   B 55  ? 1.50125  0.696419 1.35148  -0.172192   0.0798091   0.0523912   67  PHE   B CE2  
2558 C CZ   . PHE   B 55  ? 1.59818  0.731533 1.39378  -0.151772   0.105555    0.0863605   67  PHE   B CZ   
2559 H H    . PHE   B 55  ? 1.19916  0.665931 1.04657  -0.134864   0.25357     0.149547    67  PHE   B H    
2560 H HA   . PHE   B 55  ? 1.05501  0.578082 0.994519 -0.159708   0.17862     0.0657772   67  PHE   B HA   
2561 H HB2  . PHE   B 55  ? 1.21103  0.64732  1.26525  -0.235522   0.211028    0.130113    67  PHE   B HB2  
2562 H HB3  . PHE   B 55  ? 1.13754  0.596452 1.20481  -0.231609   0.156829    0.0780783   67  PHE   B HB3  
2563 H HD1  . PHE   B 55  ? 1.49716  0.790836 1.3744   -0.177299   0.216352    0.16522     67  PHE   B HD1  
2564 H HD2  . PHE   B 55  ? 1.30868  0.639714 1.26994  -0.204786   0.0835879   0.037753    67  PHE   B HD2  
2565 H HE1  . PHE   B 55  ? 1.67033  0.793228 1.43618  -0.13949    0.171919    0.158182    67  PHE   B HE1  
2566 H HE2  . PHE   B 55  ? 1.48947  0.659356 1.32218  -0.167598   0.0472349   0.0244608   67  PHE   B HE2  
2567 H HZ   . PHE   B 55  ? 1.6534   0.717724 1.40078  -0.133834   0.0899064   0.0800623   67  PHE   B HZ   
2568 N N    . ASP   B 56  ? 0.979148 0.623635 1.08001  -0.207296   0.223805    0.0760851   68  ASP   B N    
2569 C CA   . ASP   B 56  ? 0.956221 0.689458 1.12345  -0.214015   0.258601    0.0757231   68  ASP   B CA   
2570 C C    . ASP   B 56  ? 0.879105 0.640909 1.15436  -0.242876   0.226936    0.0524787   68  ASP   B C    
2571 O O    . ASP   B 56  ? 0.776779 0.52788  1.04034  -0.235103   0.181589    0.0221181   68  ASP   B O    
2572 C CB   . ASP   B 56  ? 0.885834 0.679124 0.99333  -0.174969   0.275207    0.056157    68  ASP   B CB   
2573 C CG   . ASP   B 56  ? 0.848181 0.728774 1.01873  -0.175353   0.305642    0.0431015   68  ASP   B CG   
2574 O OD1  . ASP   B 56  ? 0.823009 0.731054 1.05737  -0.195382   0.343728    0.0668586   68  ASP   B OD1  
2575 O OD2  . ASP   B 56  ? 0.776515 0.696322 0.93672  -0.155663   0.292851    0.00864742  68  ASP   B OD2  
2576 H H    . ASP   B 56  ? 0.973378 0.595847 1.08498  -0.213612   0.188534    0.0567027   68  ASP   B H    
2577 H HA   . ASP   B 56  ? 0.982853 0.717328 1.16764  -0.225528   0.292658    0.104447    68  ASP   B HA   
2578 H HB2  . ASP   B 56  ? 0.931076 0.711428 0.974472 -0.156585   0.295091    0.0735606   68  ASP   B HB2  
2579 H HB3  . ASP   B 56  ? 0.85945  0.644993 0.943686 -0.163835   0.244585    0.0325026   68  ASP   B HB3  
2580 N N    . SER   B 57  ? 0.869905 0.672957 1.24877  -0.272944   0.253751    0.0694789   69  SER   B N    
2581 C CA   . SER   B 57  ? 0.892228 0.740766 1.38602  -0.294822   0.225892    0.0483621   69  SER   B CA   
2582 C C    . SER   B 57  ? 0.889498 0.835629 1.45604  -0.288796   0.271977    0.0474229   69  SER   B C    
2583 O O    . SER   B 57  ? 1.01166  0.987653 1.57463  -0.286804   0.332268    0.0743472   69  SER   B O    
2584 C CB   . SER   B 57  ? 0.962406 0.774184 1.54102  -0.339531   0.200984    0.060615    69  SER   B CB   
2585 O OG   . SER   B 57  ? 1.01484  0.890525 1.71928  -0.358091   0.178818    0.0434843   69  SER   B OG   
2586 H H    . SER   B 57  ? 0.926594 0.731625 1.30628  -0.27869    0.290609    0.0961268   69  SER   B H    
2587 H HA   . SER   B 57  ? 0.855375 0.694773 1.32324  -0.28159    0.189795    0.0236125   69  SER   B HA   
2588 H HB2  . SER   B 57  ? 0.99653  0.746525 1.52974  -0.339867   0.163477    0.0512511   69  SER   B HB2  
2589 H HB3  . SER   B 57  ? 1.01852  0.8242   1.6127   -0.354533   0.236735    0.0892307   69  SER   B HB3  
2591 N N    . SER   B 58  ? 0.854421 0.846043 1.48624  -0.283821   0.24265     0.0170411   70  SER   B N    
2592 C CA   . SER   B 58  ? 0.761907 0.843436 1.49046  -0.279558   0.276171    0.0104096   70  SER   B CA   
2593 C C    . SER   B 58  ? 0.819835 0.937387 1.66608  -0.316837   0.308341    0.0404652   70  SER   B C    
2594 O O    . SER   B 58  ? 0.878736 1.06668  1.77452  -0.311389   0.368458    0.0516538   70  SER   B O    
2595 C CB   . SER   B 58  ? 0.66733  0.77603  1.45148  -0.26804    0.230494    -0.0231058  70  SER   B CB   
2596 O OG   . SER   B 58  ? 0.637235 0.719486 1.48183  -0.292491   0.168819    -0.0274229  70  SER   B OG   
2597 H H    . SER   B 58  ? 0.816537 0.77975  1.42936  -0.280533   0.200478    0.00038761  70  SER   B H    
2598 H HA   . SER   B 58  ? 0.771216 0.873839 1.44955  -0.25726    0.313004    0.00968804  70  SER   B HA   
2599 H HB2  . SER   B 58  ? 0.654542 0.822113 1.50361  -0.261639   0.256025    -0.0277485  70  SER   B HB2  
2600 H HB3  . SER   B 58  ? 0.650806 0.738932 1.36244  -0.246108   0.218783    -0.0387454  70  SER   B HB3  
2602 N N    . HIS   B 59  ? 0.842832 0.908997 1.72721  -0.354387   0.272004    0.0533613   71  HIS   B N    
2603 C CA   . HIS   B 59  ? 0.905675 1.00537  1.92774  -0.399234   0.289518    0.077852    71  HIS   B CA   
2604 C C    . HIS   B 59  ? 1.0027   1.10179  2.0075   -0.41199    0.368164    0.125046    71  HIS   B C    
2605 O O    . HIS   B 59  ? 0.91757  1.07512  2.04647  -0.443154   0.409485    0.149939    71  HIS   B O    
2606 C CB   . HIS   B 59  ? 0.939747 0.972993 1.99738  -0.435425   0.217623    0.0698071   71  HIS   B CB   
2607 C CG   . HIS   B 59  ? 0.874703 0.91502  1.96047  -0.425584   0.141346    0.0300412   71  HIS   B CG   
2608 N ND1  . HIS   B 59  ? 0.899722 0.870798 1.86503  -0.399663   0.0894934   0.00565105  71  HIS   B ND1  
2609 C CD2  . HIS   B 59  ? 0.844552 0.95344  2.0661   -0.437169   0.108879    0.0142807   71  HIS   B CD2  
2610 C CE1  . HIS   B 59  ? 0.887672 0.879179 1.90408  -0.395503   0.0291084   -0.0210706  71  HIS   B CE1  
2611 N NE2  . HIS   B 59  ? 0.864235 0.938729 2.03692  -0.416933   0.0360717   -0.017111   71  HIS   B NE2  
2612 H H    . HIS   B 59  ? 0.857511 0.86567  1.68285  -0.352585   0.233908    0.0446882   71  HIS   B H    
2613 H HA   . HIS   B 59  ? 0.875603 1.04543  1.98643  -0.397114   0.295497    0.0675947   71  HIS   B HA   
2614 H HB2  . HIS   B 59  ? 0.965177 0.925555 1.93043  -0.432515   0.209742    0.0758639   71  HIS   B HB2  
2615 H HB3  . HIS   B 59  ? 0.962154 1.01478  2.11536  -0.469813   0.229871    0.0870054   71  HIS   B HB3  
2617 H HD2  . HIS   B 59  ? 0.853533 1.02451  2.18454  -0.454558   0.13191     0.0241449   71  HIS   B HD2  
2618 H HE1  . HIS   B 59  ? 0.876195 0.831876 1.82955  -0.378754   -0.0104645  -0.0381725  71  HIS   B HE1  
2620 N N    . ASP   B 60  ? 1.10604  1.14295  1.95955  -0.386098   0.38915     0.139342    72  ASP   B N    
2621 C CA   . ASP   B 60  ? 1.19253  1.22174  1.99609  -0.385759   0.463668    0.187405    72  ASP   B CA   
2622 C C    . ASP   B 60  ? 1.14742  1.27684  1.96851  -0.360318   0.53515     0.191915    72  ASP   B C    
2623 O O    . ASP   B 60  ? 1.14656  1.29058  1.95002  -0.36272    0.606892    0.235682    72  ASP   B O    
2624 C CB   . ASP   B 60  ? 1.28265  1.22648  1.91595  -0.354344   0.458286    0.196655    72  ASP   B CB   
2625 C CG   . ASP   B 60  ? 1.33621  1.17578  1.92939  -0.367516   0.391886    0.187206    72  ASP   B CG   
2626 O OD1  . ASP   B 60  ? 1.3669   1.17177  2.05265  -0.414647   0.372402    0.199172    72  ASP   B OD1  
2627 O OD2  . ASP   B 60  ? 1.22805  1.02509  1.70246  -0.330503   0.36069     0.165491    72  ASP   B OD2  
2628 H H    . ASP   B 60  ? 1.07044  1.0691   1.84795  -0.366242   0.354936    0.119479    72  ASP   B H    
2629 H HA   . ASP   B 60  ? 1.23525  1.2479   2.10532  -0.422278   0.473236    0.213497    72  ASP   B HA   
2630 H HB2  . ASP   B 60  ? 1.2397   1.20673  1.81219  -0.320068   0.454126    0.172662    72  ASP   B HB2  
2631 H HB3  . ASP   B 60  ? 1.33754  1.27128  1.93952  -0.35499    0.505365    0.233238    72  ASP   B HB3  
2632 N N    . ARG   B 61  ? 1.06115  1.25358  1.90715  -0.332265   0.517265    0.146793    73  ARG   B N    
2633 C CA   . ARG   B 61  ? 1.01043  1.30148  1.89953  -0.308986   0.578711    0.140577    73  ARG   B CA   
2634 C C    . ARG   B 61  ? 0.922339 1.29528  2.00367  -0.337973   0.580738    0.136233    73  ARG   B C    
2635 O O    . ARG   B 61  ? 0.902426 1.36383  2.04279  -0.316119   0.624959    0.123466    73  ARG   B O    
2636 C CB   . ARG   B 61  ? 0.93122  1.22678  1.71511  -0.256929   0.560441    0.0943019   73  ARG   B CB   
2637 H H    . ARG   B 61  ? 1.01262  1.18251  1.84491  -0.325623   0.466484    0.119003    73  ARG   B H    
2638 H HA   . ARG   B 61  ? 1.05752  1.35325  1.90938  -0.307201   0.633379    0.172375    73  ARG   B HA   
2641 N N    . ASN   B 62  ? 0.864479 1.21213  2.04813  -0.385411   0.533293    0.144954    74  ASN   B N    
2642 C CA   . ASN   B 62  ? 0.814129 1.23763  2.18297  -0.410403   0.509411    0.131084    74  ASN   B CA   
2643 C C    . ASN   B 62  ? 0.77866  1.28016  2.1803   -0.364701   0.50921     0.0895752   74  ASN   B C    
2644 O O    . ASN   B 62  ? 0.77816  1.37865  2.29728  -0.360453   0.558045    0.0919139   74  ASN   B O    
2645 C CB   . ASN   B 62  ? 0.820466 1.29444  2.3255   -0.45883    0.567607    0.176994    74  ASN   B CB   
2646 H H    . ASN   B 62  ? 0.902514 1.18257  2.03892  -0.401901   0.5131      0.158932    74  ASN   B H    
2647 H HA   . ASN   B 62  ? 0.795187 1.17539  2.17646  -0.426591   0.44599     0.117462    74  ASN   B HA   
2650 N N    . GLU   B 63  ? 0.84505  1.30051  2.14632  -0.329265   0.456417    0.0516067   75  GLU   B N    
2651 C CA   . GLU   B 63  ? 0.818174 1.32562  2.14598  -0.287021   0.447068    0.0111786   75  GLU   B CA   
2652 C C    . GLU   B 63  ? 0.781152 1.21431  1.99476  -0.261337   0.381735    -0.0212845  75  GLU   B C    
2653 O O    . GLU   B 63  ? 0.744411 1.10463  1.8179   -0.256227   0.37535     -0.0172999  75  GLU   B O    
2654 C CB   . GLU   B 63  ? 0.896494 1.46867  2.20015  -0.249887   0.530486    0.00641797  75  GLU   B CB   
2655 C CG   . GLU   B 63  ? 0.963017 1.48335  2.08641  -0.226137   0.565493    0.0111975   75  GLU   B CG   
2656 C CD   . GLU   B 63  ? 1.03448  1.61323  2.11253  -0.183316   0.639909    -0.00260647 75  GLU   B CD   
2657 O OE1  . GLU   B 63  ? 1.03468  1.57375  1.9766   -0.150305   0.631949    -0.0285994  75  GLU   B OE1  
2658 O OE2  . GLU   B 63  ? 1.01377  1.67757  2.18701  -0.180842   0.704384    0.00903499  75  GLU   B OE2  
2659 H H    . GLU   B 63  ? 0.823076 1.20988  2.03823  -0.331831   0.426521    0.0519863   75  GLU   B H    
2660 H HA   . GLU   B 63  ? 0.80777  1.36081  2.25518  -0.297844   0.427204    0.00601303  75  GLU   B HA   
2661 H HB2  . GLU   B 63  ? 0.860906 1.46091  2.1916   -0.223093   0.5188      -0.023279   75  GLU   B HB2  
2662 H HB3  . GLU   B 63  ? 0.91185  1.53869  2.29717  -0.264913   0.575116    0.0279341   75  GLU   B HB3  
2663 H HG2  . GLU   B 63  ? 0.996451 1.48751  2.09182  -0.249326   0.580093    0.0435836   75  GLU   B HG2  
2664 H HG3  . GLU   B 63  ? 0.937444 1.40686  1.98852  -0.214607   0.521223    -0.00894924 75  GLU   B HG3  
2665 N N    . PRO   B 64  ? 0.710976 1.16301  1.97972  -0.24006    0.335669    -0.0530359  76  PRO   B N    
2666 C CA   . PRO   B 64  ? 0.63458  1.01884  1.80128  -0.217483   0.283027    -0.0780166  76  PRO   B CA   
2667 C C    . PRO   B 64  ? 0.647133 1.00151  1.67307  -0.19127    0.320257    -0.0880372  76  PRO   B C    
2668 O O    . PRO   B 64  ? 0.694811 1.09025  1.70497  -0.179506   0.385497    -0.0833498  76  PRO   B O    
2669 C CB   . PRO   B 64  ? 0.610555 1.03595  1.86674  -0.190273   0.256678    -0.104959   76  PRO   B CB   
2670 C CG   . PRO   B 64  ? 0.660856 1.18834  2.05076  -0.185299   0.313326    -0.101977   76  PRO   B CG   
2671 C CD   . PRO   B 64  ? 0.692673 1.23469  2.12123  -0.23047    0.33959     -0.0648156  76  PRO   B CD   
2672 H HA   . PRO   B 64  ? 0.646421 0.982078 1.78732  -0.23568    0.240422    -0.0710695  76  PRO   B HA   
2673 H HB2  . PRO   B 64  ? 0.611227 1.01549  1.80593  -0.165098   0.257505    -0.123839   76  PRO   B HB2  
2674 H HB3  . PRO   B 64  ? 0.610675 1.01885  1.90138  -0.200198   0.204509    -0.104415   76  PRO   B HB3  
2675 H HG2  . PRO   B 64  ? 0.661312 1.2076   2.01652  -0.161529   0.358137    -0.113517   76  PRO   B HG2  
2676 H HG3  . PRO   B 64  ? 0.639169 1.20011  2.12232  -0.178135   0.287212    -0.110837   76  PRO   B HG3  
2677 H HD2  . PRO   B 64  ? 0.710355 1.30821  2.18213  -0.228186   0.396708    -0.0560056  76  PRO   B HD2  
2678 H HD3  . PRO   B 64  ? 0.687398 1.23683  2.19492  -0.253163   0.300568    -0.0584679  76  PRO   B HD3  
2679 N N    . PHE   B 65  ? 0.613372 0.898663 1.53731  -0.182495   0.27722     -0.101086   77  PHE   B N    
2680 C CA   . PHE   B 65  ? 0.634916 0.898444 1.44525  -0.154782   0.295137    -0.121588   77  PHE   B CA   
2681 C C    . PHE   B 65  ? 0.622293 0.893476 1.46263  -0.128074   0.274553    -0.156371   77  PHE   B C    
2682 O O    . PHE   B 65  ? 0.615459 0.858909 1.49001  -0.131972   0.221564    -0.158272   77  PHE   B O    
2683 C CB   . PHE   B 65  ? 0.651133 0.840195 1.34913  -0.164318   0.262908    -0.111697   77  PHE   B CB   
2684 C CG   . PHE   B 65  ? 0.690842 0.864796 1.2774   -0.139638   0.278631    -0.130644   77  PHE   B CG   
2685 C CD1  . PHE   B 65  ? 0.756161 0.943642 1.27416  -0.131002   0.324698    -0.120088   77  PHE   B CD1  
2686 C CD2  . PHE   B 65  ? 0.599442 0.745942 1.15143  -0.126208   0.245819    -0.156511   77  PHE   B CD2  
2687 C CE1  . PHE   B 65  ? 0.743336 0.924997 1.16414  -0.10689    0.331865    -0.141258   77  PHE   B CE1  
2688 C CE2  . PHE   B 65  ? 0.656052 0.79863  1.1238   -0.107468   0.258093    -0.177427   77  PHE   B CE2  
2689 C CZ   . PHE   B 65  ? 0.708382 0.871196 1.1112   -0.0969149  0.29743     -0.172551   77  PHE   B CZ   
2690 H H    . PHE   B 65  ? 0.614959 0.867269 1.54255  -0.194722   0.233908    -0.0977774  77  PHE   B H    
2691 H HA   . PHE   B 65  ? 0.657612 0.950416 1.44981  -0.146784   0.341487    -0.118752   77  PHE   B HA   
2692 H HB2  . PHE   B 65  ? 0.676143 0.854463 1.36676  -0.181658   0.272461    -0.088575   77  PHE   B HB2  
2693 H HB3  . PHE   B 65  ? 0.638012 0.798784 1.34604  -0.16924    0.220284    -0.115604   77  PHE   B HB3  
2694 H HD1  . PHE   B 65  ? 0.765901 0.968594 1.30604  -0.141372   0.350929    -0.0978151  77  PHE   B HD1  
2695 H HD2  . PHE   B 65  ? 0.610492 0.744501 1.20165  -0.129583   0.216123    -0.160074   77  PHE   B HD2  
2696 H HE1  . PHE   B 65  ? 0.77864  0.97059  1.1484   -0.0977686  0.360152    -0.133561   77  PHE   B HE1  
2697 H HE2  . PHE   B 65  ? 0.635216 0.760691 1.08884  -0.102013   0.237703    -0.19412    77  PHE   B HE2  
2698 H HZ   . PHE   B 65  ? 0.71283  0.875109 1.05821  -0.083459   0.299431    -0.188693   77  PHE   B HZ   
2699 N N    . VAL   B 66  ? 0.623069 0.928693 1.45069  -0.0996145  0.316442    -0.183237   78  VAL   B N    
2700 C CA   . VAL   B 66  ? 0.56818  0.874941 1.43006  -0.0728679  0.302651    -0.218748   78  VAL   B CA   
2701 C C    . VAL   B 66  ? 0.548043 0.822487 1.30194  -0.0564325  0.30822     -0.247964   78  VAL   B C    
2702 O O    . VAL   B 66  ? 0.542709 0.824141 1.21293  -0.0537397  0.339083    -0.247806   78  VAL   B O    
2703 C CB   . VAL   B 66  ? 0.637192 1.01458  1.60469  -0.0500071  0.34146     -0.235107   78  VAL   B CB   
2704 C CG1  . VAL   B 66  ? 0.641729 1.00776  1.68182  -0.0282853  0.306306    -0.258592   78  VAL   B CG1  
2705 C CG2  . VAL   B 66  ? 0.666655 1.10284  1.73453  -0.0705229  0.362117    -0.202687   78  VAL   B CG2  
2706 H H    . VAL   B 66  ? 0.637079 0.962067 1.43049  -0.0957172  0.354167    -0.179746   78  VAL   B H    
2707 H HA   . VAL   B 66  ? 0.562592 0.841305 1.44821  -0.0795017  0.261156    -0.213757   78  VAL   B HA   
2708 H HB   . VAL   B 66  ? 0.658131 1.05241  1.5832   -0.0333319  0.379011    -0.252767   78  VAL   B HB   
2709 H HG11 . VAL   B 66  ? 0.62009  0.973731 1.70105  -0.0415163  0.268742    -0.240535   78  VAL   B HG11 
2710 H HG12 . VAL   B 66  ? 0.640754 0.965881 1.62384  -0.0193529  0.293553    -0.277448   78  VAL   B HG12 
2711 H HG13 . VAL   B 66  ? 0.652129 1.06322  1.75514  -0.00881903 0.334014    -0.272563   78  VAL   B HG13 
2712 H HG21 . VAL   B 66  ? 0.664951 1.14981  1.81016  -0.0537714  0.383833    -0.214012   78  VAL   B HG21 
2713 H HG22 . VAL   B 66  ? 0.674989 1.1199   1.70059  -0.08094    0.394268    -0.186922   78  VAL   B HG22 
2714 H HG23 . VAL   B 66  ? 0.639038 1.05561  1.73799  -0.0895772  0.321432    -0.186478   78  VAL   B HG23 
2715 N N    . PHE   B 67  ? 0.522414 0.756322 1.27693  -0.0477993  0.272188    -0.269601   79  PHE   B N    
2716 C CA   . PHE   B 67  ? 0.509016 0.713582 1.18354  -0.0373226  0.270851    -0.301222   79  PHE   B CA   
2717 C C    . PHE   B 67  ? 0.525321 0.691452 1.24433  -0.0273992  0.239852    -0.322728   79  PHE   B C    
2718 O O    . PHE   B 67  ? 0.490681 0.641694 1.27697  -0.0298462  0.210502    -0.304011   79  PHE   B O    
2719 C CB   . PHE   B 67  ? 0.547744 0.715886 1.12577  -0.0555739  0.251545    -0.284881   79  PHE   B CB   
2720 C CG   . PHE   B 67  ? 0.505657 0.620605 1.08252  -0.0736039  0.203305    -0.262109   79  PHE   B CG   
2721 C CD1  . PHE   B 67  ? 0.494683 0.601504 1.10754  -0.0892614  0.181409    -0.22817    79  PHE   B CD1  
2722 C CD2  . PHE   B 67  ? 0.505245 0.579791 1.04338  -0.0753678  0.180874    -0.275138   79  PHE   B CD2  
2723 C CE1  . PHE   B 67  ? 0.476479 0.533564 1.07287  -0.100663   0.137369    -0.209791   79  PHE   B CE1  
2724 C CE2  . PHE   B 67  ? 0.48277  0.509955 1.01242  -0.0885127  0.143552    -0.250685   79  PHE   B CE2  
2725 C CZ   . PHE   B 67  ? 0.466247 0.483353 1.0171   -0.0983771  0.121295    -0.219005   79  PHE   B CZ   
2726 H H    . PHE   B 67  ? 0.510394 0.734557 1.31892  -0.0492186  0.246952    -0.263602   79  PHE   B H    
2727 H HA   . PHE   B 67  ? 0.550287 0.784326 1.20798  -0.0219537  0.303591    -0.322037   79  PHE   B HA   
2728 H HB2  . PHE   B 67  ? 0.544317 0.709172 1.07772  -0.0471783  0.256811    -0.309184   79  PHE   B HB2  
2729 H HB3  . PHE   B 67  ? 0.535034 0.718985 1.08911  -0.0619784  0.26778     -0.265553   79  PHE   B HB3  
2730 H HD1  . PHE   B 67  ? 0.493706 0.630125 1.14236  -0.0921124  0.196965    -0.218429   79  PHE   B HD1  
2731 H HD2  . PHE   B 67  ? 0.513714 0.593488 1.03463  -0.0674725  0.19141     -0.301257   79  PHE   B HD2  
2732 H HE1  . PHE   B 67  ? 0.475231 0.526639 1.09335  -0.110003   0.1189      -0.191331   79  PHE   B HE1  
2733 H HE2  . PHE   B 67  ? 0.486923 0.489277 0.994009 -0.0908982  0.133515    -0.256431   79  PHE   B HE2  
2734 H HZ   . PHE   B 67  ? 0.474496 0.45842  1.00759  -0.104445   0.0957747   -0.204121   79  PHE   B HZ   
2735 N N    . SER   B 68  ? 0.522456 0.670714 1.20424  -0.0154523  0.244722    -0.362424   80  SER   B N    
2736 C CA   . SER   B 68  ? 0.566084 0.667103 1.28937  -0.00780479 0.219531    -0.382356   80  SER   B CA   
2737 C C    . SER   B 68  ? 0.539516 0.588218 1.20353  -0.0314114  0.188421    -0.370164   80  SER   B C    
2738 O O    . SER   B 68  ? 0.509489 0.566044 1.10325  -0.0396406  0.195675    -0.382938   80  SER   B O    
2739 C CB   . SER   B 68  ? 0.602771 0.711614 1.34365  0.0200151   0.243996    -0.438807   80  SER   B CB   
2740 O OG   . SER   B 68  ? 0.60768  0.756681 1.42901  0.0474663   0.268893    -0.447554   80  SER   B OG   
2741 H H    . SER   B 68  ? 0.548445 0.711706 1.17894  -0.0122379  0.262508    -0.377211   80  SER   B H    
2742 H HA   . SER   B 68  ? 0.548275 0.644694 1.32908  -0.0050754  0.205648    -0.364155   80  SER   B HA   
2743 H HB2  . SER   B 68  ? 0.615329 0.743988 1.3011   0.0215143   0.261505    -0.45758    80  SER   B HB2  
2744 H HB3  . SER   B 68  ? 0.61759  0.68295  1.36819  0.0189297   0.225058    -0.452583   80  SER   B HB3  
2746 N N    . LEU   B 69  ? 0.5359   0.537645 1.22835  -0.0399673  0.154751    -0.341303   81  LEU   B N    
2747 C CA   . LEU   B 69  ? 0.556586 0.514506 1.19584  -0.062046   0.130116    -0.317017   81  LEU   B CA   
2748 C C    . LEU   B 69  ? 0.578657 0.507089 1.20407  -0.0675707  0.131717    -0.348309   81  LEU   B C    
2749 O O    . LEU   B 69  ? 0.594878 0.49534  1.27242  -0.0559349  0.130924    -0.372388   81  LEU   B O    
2750 C CB   . LEU   B 69  ? 0.626793 0.54237  1.29442  -0.0637726  0.0962161   -0.277981   81  LEU   B CB   
2751 C CG   . LEU   B 69  ? 0.663384 0.533544 1.26734  -0.0833384  0.076401    -0.2491     81  LEU   B CG   
2752 C CD1  . LEU   B 69  ? 0.625336 0.509704 1.17661  -0.0938539  0.0671551   -0.220891   81  LEU   B CD1  
2753 C CD2  . LEU   B 69  ? 0.815074 0.622765 1.44021  -0.0799949  0.0506523   -0.224724   81  LEU   B CD2  
2754 H H    . LEU   B 69  ? 0.549809 0.548654 1.29638  -0.029169   0.147985    -0.336074   81  LEU   B H    
2755 H HA   . LEU   B 69  ? 0.540655 0.516856 1.13366  -0.0714201  0.134551    -0.305636   81  LEU   B HA   
2756 H HB2  . LEU   B 69  ? 0.604381 0.542806 1.28765  -0.0619599  0.0916447   -0.262259   81  LEU   B HB2  
2757 H HB3  . LEU   B 69  ? 0.643689 0.53876  1.35724  -0.0517463  0.0915086   -0.286902   81  LEU   B HB3  
2758 H HG   . LEU   B 69  ? 0.671131 0.542425 1.24893  -0.0911065  0.0889266   -0.266438   81  LEU   B HG   
2759 H HD11 . LEU   B 69  ? 0.611455 0.528285 1.14315  -0.0959637  0.0853557   -0.233299   81  LEU   B HD11 
2760 H HD12 . LEU   B 69  ? 0.636641 0.493327 1.14523  -0.102576   0.0572933   -0.204635   81  LEU   B HD12 
2761 H HD13 . LEU   B 69  ? 0.629861 0.51747  1.20977  -0.0888455  0.0525984   -0.206946   81  LEU   B HD13 
2762 H HD21 . LEU   B 69  ? 0.797536 0.590646 1.46044  -0.0727017  0.0569449   -0.243757   81  LEU   B HD21 
2763 H HD22 . LEU   B 69  ? 0.781042 0.587316 1.42595  -0.0714888  0.0322686   -0.205907   81  LEU   B HD22 
2764 H HD23 . LEU   B 69  ? 0.784632 0.567246 1.36543  -0.0924919  0.0461665   -0.208304   81  LEU   B HD23 
2765 N N    . GLY   B 70  ? 0.575472 0.513006 1.1371   -0.0844129  0.133598    -0.349592   82  GLY   B N    
2766 C CA   . GLY   B 70  ? 0.650574 0.568093 1.20548  -0.0977236  0.130824    -0.37596    82  GLY   B CA   
2767 C C    . GLY   B 70  ? 0.768875 0.713032 1.33263  -0.0851187  0.146184    -0.436254   82  GLY   B C    
2768 O O    . GLY   B 70  ? 0.814347 0.738169 1.39219  -0.0964807  0.139748    -0.468932   82  GLY   B O    
2769 H H    . GLY   B 70  ? 0.563071 0.5216   1.0891   -0.0877199  0.136195    -0.333861   82  GLY   B H    
2770 H HA2  . GLY   B 70  ? 0.638759 0.566356 1.15302  -0.109759   0.128501    -0.364526   82  GLY   B HA2  
2771 H HA3  . GLY   B 70  ? 0.673617 0.548361 1.25912  -0.10291    0.120139    -0.36591    82  GLY   B HA3  
2772 N N    . LYS   B 71  ? 0.739956 0.727376 1.29872  -0.061835   0.167069    -0.452277   83  LYS   B N    
2773 C CA   . LYS   B 71  ? 0.804065 0.819781 1.35155  -0.0434975  0.18419     -0.511328   83  LYS   B CA   
2774 C C    . LYS   B 71  ? 0.836825 0.906668 1.30144  -0.0417564  0.194479    -0.513909   83  LYS   B C    
2775 O O    . LYS   B 71  ? 0.999635 1.10873  1.43295  -0.018372   0.217563    -0.543011   83  LYS   B O    
2776 C CB   . LYS   B 71  ? 0.763665 0.783899 1.36577  -0.0137305  0.204192    -0.532198   83  LYS   B CB   
2777 H H    . LYS   B 71  ? 0.728859 0.729275 1.2894   -0.0573679  0.171495    -0.426152   83  LYS   B H    
2778 H HA   . LYS   B 71  ? 0.817574 0.807932 1.37791  -0.052038   0.172578    -0.537745   83  LYS   B HA   
2781 N N    . GLY   B 72  ? 0.791409 0.862296 1.21737  -0.0617579  0.179834    -0.479208   84  GLY   B N    
2782 C CA   . GLY   B 72  ? 0.851309 0.964169 1.2022   -0.0594851  0.180449    -0.48324    84  GLY   B CA   
2783 C C    . GLY   B 72  ? 0.782155 0.930366 1.07665  -0.0431381  0.203423    -0.454601   84  GLY   B C    
2784 O O    . GLY   B 72  ? 0.840404 1.02065  1.06652  -0.0338486  0.20488     -0.458869   84  GLY   B O    
2785 H H    . GLY   B 72  ? 0.785314 0.828775 1.23151  -0.074649   0.168666    -0.451073   84  GLY   B H    
2786 H HA2  . GLY   B 72  ? 0.800624 0.903857 1.14559  -0.0750367  0.166021    -0.465158   84  GLY   B HA2  
2787 H HA3  . GLY   B 72  ? 0.853515 0.980703 1.19463  -0.053055   0.178342    -0.524646   84  GLY   B HA3  
2788 N N    . GLN   B 73  ? 0.663869 0.807561 0.988232 -0.0398973  0.220346    -0.423126   85  GLN   B N    
2789 C CA   . GLN   B 73  ? 0.707539 0.883494 0.990816 -0.0277735  0.248924    -0.397626   85  GLN   B CA   
2790 C C    . GLN   B 73  ? 0.652099 0.814627 0.900073 -0.0416228  0.241245    -0.345039   85  GLN   B C    
2791 O O    . GLN   B 73  ? 0.683578 0.86507  0.885739 -0.0334191  0.263385    -0.322949   85  GLN   B O    
2792 C CB   . GLN   B 73  ? 0.70145  0.888539 1.05192  -0.0192599  0.274053    -0.393307   85  GLN   B CB   
2793 C CG   . GLN   B 73  ? 0.766305 0.968743 1.1396   0.00389899  0.290014    -0.448575   85  GLN   B CG   
2794 C CD   . GLN   B 73  ? 0.760552 0.961789 1.22962  0.0115976   0.301179    -0.448119   85  GLN   B CD   
2795 O OE1  . GLN   B 73  ? 0.696456 0.897397 1.21726  -0.00012767 0.298813    -0.405754   85  GLN   B OE1  
2796 N NE2  . GLN   B 73  ? 0.842484 1.04001  1.33967  0.0323364   0.307526    -0.499385   85  GLN   B NE2  
2797 H H    . GLN   B 73  ? 0.68245  0.802857 1.05693  -0.0459931  0.213777    -0.415736   85  GLN   B H    
2798 H HA   . GLN   B 73  ? 0.727186 0.928495 0.963122 -0.0131825  0.259676    -0.419653   85  GLN   B HA   
2799 H HB2  . GLN   B 73  ? 0.681623 0.844893 1.08121  -0.0312522  0.258379    -0.375667   85  GLN   B HB2  
2800 H HB3  . GLN   B 73  ? 0.715908 0.924039 1.04832  -0.0157654  0.295726    -0.371237   85  GLN   B HB3  
2801 H HG2  . GLN   B 73  ? 0.795447 1.02843  1.12267  0.0199596   0.3134      -0.460595   85  GLN   B HG2  
2802 H HG3  . GLN   B 73  ? 0.767192 0.950142 1.13747  0.0002929   0.269563    -0.475549   85  GLN   B HG3  
2803 H HE21 . GLN   B 73  ? 0.828969 1.02309  1.38563  0.0403856   0.311619    -0.502476   85  GLN   B HE21 
2804 H HE22 . GLN   B 73  ? 0.857708 1.05528  1.31552  0.0392883   0.306203    -0.532292   85  GLN   B HE22 
2805 N N    . VAL   B 74  ? 0.560843 0.686083 0.8261   -0.0605736  0.212434    -0.324738   86  VAL   B N    
2806 C CA   . VAL   B 74  ? 0.522837 0.62551  0.753391 -0.0711462  0.200997    -0.282877   86  VAL   B CA   
2807 C C    . VAL   B 74  ? 0.496287 0.586972 0.694263 -0.0764438  0.178408    -0.287902   86  VAL   B C    
2808 O O    . VAL   B 74  ? 0.517437 0.615725 0.734165 -0.0783367  0.170735    -0.319307   86  VAL   B O    
2809 C CB   . VAL   B 74  ? 0.486145 0.556587 0.772538 -0.0859353  0.187612    -0.254548   86  VAL   B CB   
2810 C CG1  . VAL   B 74  ? 0.505957 0.600687 0.834722 -0.0833539  0.212197    -0.243565   86  VAL   B CG1  
2811 C CG2  . VAL   B 74  ? 0.416447 0.462557 0.75846  -0.0915708  0.167452    -0.268405   86  VAL   B CG2  
2812 H H    . VAL   B 74  ? 0.560917 0.67083  0.858858 -0.0659743  0.199782    -0.338785   86  VAL   B H    
2813 H HA   . VAL   B 74  ? 0.537313 0.653669 0.731569 -0.0640258  0.215878    -0.271019   86  VAL   B HA   
2814 H HB   . VAL   B 74  ? 0.473772 0.522701 0.73192  -0.092729   0.175597    -0.232566   86  VAL   B HB   
2815 H HG11 . VAL   B 74  ? 0.512347 0.629592 0.866996 -0.0731954  0.226741    -0.266456   86  VAL   B HG11 
2816 H HG12 . VAL   B 74  ? 0.516922 0.621    0.808494 -0.0813285  0.227146    -0.230014   86  VAL   B HG12 
2817 H HG13 . VAL   B 74  ? 0.491988 0.57086  0.860541 -0.0931795  0.198734    -0.227148   86  VAL   B HG13 
2818 H HG21 . VAL   B 74  ? 0.425774 0.449386 0.789307 -0.0988302  0.152822    -0.247612   86  VAL   B HG21 
2819 H HG22 . VAL   B 74  ? 0.431932 0.468781 0.752575 -0.0946931  0.158428    -0.276702   86  VAL   B HG22 
2820 H HG23 . VAL   B 74  ? 0.44217  0.503425 0.81961  -0.0837363  0.178342    -0.289165   86  VAL   B HG23 
2821 N N    . ILE   B 75  ? 0.518721 0.590105 0.674272 -0.0793088  0.169019    -0.257557   87  ILE   B N    
2822 C CA   . ILE   B 75  ? 0.464452 0.531601 0.593724 -0.0815613  0.152959    -0.258189   87  ILE   B CA   
2823 C C    . ILE   B 75  ? 0.411802 0.449771 0.587863 -0.0986745  0.13855     -0.258032   87  ILE   B C    
2824 O O    . ILE   B 75  ? 0.401752 0.409038 0.613931 -0.106142   0.133002    -0.244263   87  ILE   B O    
2825 C CB   . ILE   B 75  ? 0.503737 0.551195 0.575496 -0.0746177  0.149625    -0.226198   87  ILE   B CB   
2826 C CG1  . ILE   B 75  ? 0.553003 0.55557  0.634468 -0.0847028  0.14468     -0.196423   87  ILE   B CG1  
2827 C CG2  . ILE   B 75  ? 0.563429 0.638895 0.579624 -0.053638   0.162521    -0.225592   87  ILE   B CG2  
2828 C CD1  . ILE   B 75  ? 0.577151 0.545587 0.601925 -0.0785015  0.136532    -0.171273   87  ILE   B CD1  
2829 H H    . ILE   B 75  ? 0.506061 0.567366 0.650962 -0.0793188  0.174299    -0.236348   87  ILE   B H    
2830 H HA   . ILE   B 75  ? 0.478437 0.575856 0.59652  -0.0743581  0.154812    -0.280714   87  ILE   B HA   
2831 H HB   . ILE   B 75  ? 0.505883 0.550023 0.568198 -0.0756242  0.140546    -0.225546   87  ILE   B HB   
2832 H HG12 . ILE   B 75  ? 0.548213 0.558612 0.643612 -0.0846922  0.156406    -0.193846   87  ILE   B HG12 
2833 H HG13 . ILE   B 75  ? 0.531086 0.517196 0.644534 -0.0947746  0.13426     -0.196557   87  ILE   B HG13 
2834 H HG21 . ILE   B 75  ? 0.562322 0.623858 0.542871 -0.0465859  0.157764    -0.209013   87  ILE   B HG21 
2835 H HG22 . ILE   B 75  ? 0.565361 0.638652 0.583785 -0.0530179  0.175703    -0.217484   87  ILE   B HG22 
2836 H HG23 . ILE   B 75  ? 0.556925 0.665928 0.570215 -0.046469   0.162266    -0.249533   87  ILE   B HG23 
2837 H HD11 . ILE   B 75  ? 0.572377 0.544496 0.577836 -0.0731284  0.130939    -0.175658   87  ILE   B HD11 
2838 H HD12 . ILE   B 75  ? 0.579037 0.514764 0.614076 -0.087843   0.126291    -0.157954   87  ILE   B HD12 
2839 H HD13 . ILE   B 75  ? 0.592561 0.566847 0.590064 -0.0692988  0.146957    -0.164365   87  ILE   B HD13 
2840 N N    . LYS   B 76  ? 0.410531 0.461462 0.589031 -0.104164   0.132819    -0.271742   88  LYS   B N    
2841 C CA   . LYS   B 76  ? 0.446727 0.468919 0.664578 -0.121751   0.125338    -0.266443   88  LYS   B CA   
2842 C C    . LYS   B 76  ? 0.434626 0.406388 0.63683  -0.124315   0.116349    -0.227492   88  LYS   B C    
2843 O O    . LYS   B 76  ? 0.448366 0.385917 0.686194 -0.131371   0.108556    -0.218482   88  LYS   B O    
2844 C CB   . LYS   B 76  ? 0.424321 0.474168 0.641529 -0.128816   0.125576    -0.275032   88  LYS   B CB   
2845 H H    . LYS   B 76  ? 0.421903 0.502115 0.57836  -0.096749   0.134292    -0.283169   88  LYS   B H    
2846 H HA   . LYS   B 76  ? 0.437388 0.455184 0.695618 -0.126538   0.12584     -0.283551   88  LYS   B HA   
2849 N N    . ALA   B 77  ? 0.409668 0.373763 0.556168 -0.115016   0.113975    -0.206562   89  ALA   B N    
2850 C CA   . ALA   B 77  ? 0.455707 0.370223 0.576375 -0.115959   0.0996412   -0.176432   89  ALA   B CA   
2851 C C    . ALA   B 77  ? 0.518517 0.410505 0.677602 -0.120134   0.0870113   -0.169914   89  ALA   B C    
2852 O O    . ALA   B 77  ? 0.544031 0.395891 0.700729 -0.122975   0.0676308   -0.150645   89  ALA   B O    
2853 C CB   . ALA   B 77  ? 0.425182 0.329958 0.482177 -0.103679   0.0980826   -0.163324   89  ALA   B CB   
2854 H H    . ALA   B 77  ? 0.420097 0.407542 0.541447 -0.106415   0.119394    -0.212362   89  ALA   B H    
2855 H HA   . ALA   B 77  ? 0.46174  0.361516 0.582014 -0.120928   0.0978388   -0.168626   89  ALA   B HA   
2856 H HB1  . ALA   B 77  ? 0.438478 0.360573 0.474781 -0.0977828  0.105385    -0.166641   89  ALA   B HB1  
2857 H HB2  . ALA   B 77  ? 0.433298 0.348598 0.489318 -0.0998483  0.101921    -0.166741   89  ALA   B HB2  
2858 H HB3  . ALA   B 77  ? 0.455688 0.325056 0.493031 -0.104202   0.0857793   -0.148231   89  ALA   B HB3  
2859 N N    . TRP   B 78  ? 0.522891 0.444202 0.714102 -0.117711   0.097823    -0.18455    90  TRP   B N    
2860 C CA   . TRP   B 78  ? 0.495527 0.410201 0.741684 -0.120588   0.0896399   -0.180139   90  TRP   B CA   
2861 C C    . TRP   B 78  ? 0.467954 0.374224 0.770344 -0.121698   0.0843562   -0.190205   90  TRP   B C    
2862 O O    . TRP   B 78  ? 0.522662 0.402871 0.856138 -0.121937   0.0637221   -0.175536   90  TRP   B O    
2863 C CB   . TRP   B 78  ? 0.484007 0.43724  0.751251 -0.116383   0.111585    -0.189696   90  TRP   B CB   
2864 C CG   . TRP   B 78  ? 0.467069 0.40797  0.71404  -0.121151   0.108285    -0.167022   90  TRP   B CG   
2865 C CD1  . TRP   B 78  ? 0.550754 0.463706 0.731374 -0.120446   0.101007    -0.152209   90  TRP   B CD1  
2866 C CD2  . TRP   B 78  ? 0.490563 0.441783 0.792542 -0.129026   0.110307    -0.156628   90  TRP   B CD2  
2867 N NE1  . TRP   B 78  ? 0.530959 0.425452 0.718554 -0.129512   0.0952956   -0.134434   90  TRP   B NE1  
2868 C CE2  . TRP   B 78  ? 0.513864 0.435853 0.77988  -0.13759    0.101639    -0.135679   90  TRP   B CE2  
2869 C CE3  . TRP   B 78  ? 0.477383 0.46171  0.861898 -0.12916    0.119865    -0.163856   90  TRP   B CE3  
2870 C CZ2  . TRP   B 78  ? 0.523553 0.448994 0.83968  -0.152369   0.101778    -0.121103   90  TRP   B CZ2  
2871 C CZ3  . TRP   B 78  ? 0.462381 0.46061  0.899038 -0.140678   0.122496    -0.148401   90  TRP   B CZ3  
2872 C CH2  . TRP   B 78  ? 0.508679 0.477204 0.914931 -0.155426   0.112173    -0.126619   90  TRP   B CH2  
2873 H H    . TRP   B 78  ? 0.504087 0.452335 0.683213 -0.112712   0.110802    -0.196624   90  TRP   B H    
2874 H HA   . TRP   B 78  ? 0.505113 0.393464 0.738753 -0.123436   0.072574    -0.16248    90  TRP   B HA   
2875 H HB2  . TRP   B 78  ? 0.476399 0.452398 0.721441 -0.110479   0.126832    -0.20386    90  TRP   B HB2  
2876 H HB3  . TRP   B 78  ? 0.474855 0.438816 0.793379 -0.115543   0.113976    -0.197403   90  TRP   B HB3  
2877 H HD1  . TRP   B 78  ? 0.526475 0.432135 0.667302 -0.114947   0.0990924   -0.154191   90  TRP   B HD1  
2878 H HE1  . TRP   B 78  ? 0.554871 0.425518 0.706511 -0.129763   0.0902268   -0.124916   90  TRP   B HE1  
2879 H HE3  . TRP   B 78  ? 0.466169 0.464302 0.874945 -0.121345   0.125429    -0.180043   90  TRP   B HE3  
2880 H HZ2  . TRP   B 78  ? 0.544559 0.44343  0.838992 -0.16022    0.094232    -0.108649   90  TRP   B HZ2  
2881 H HZ3  . TRP   B 78  ? 0.469134 0.496724 0.96848  -0.139148   0.131035    -0.153292   90  TRP   B HZ3  
2882 H HH2  . TRP   B 78  ? 0.511156 0.489927 0.962736 -0.167201   0.114113    -0.116445   90  TRP   B HH2  
2883 N N    . ASP   B 79  ? 0.470881 0.39556  0.78759  -0.121323   0.0993619   -0.216099   91  ASP   B N    
2884 C CA   . ASP   B 79  ? 0.514744 0.418407 0.885875 -0.122996   0.0947596   -0.226242   91  ASP   B CA   
2885 C C    . ASP   B 79  ? 0.599869 0.452136 0.955626 -0.129575   0.0754539   -0.194045   91  ASP   B C    
2886 O O    . ASP   B 79  ? 0.652374 0.471936 1.0467   -0.125599   0.0607321   -0.182525   91  ASP   B O    
2887 C CB   . ASP   B 79  ? 0.54511  0.469689 0.932137 -0.125867   0.110074    -0.264005   91  ASP   B CB   
2888 C CG   . ASP   B 79  ? 0.581816 0.546427 0.99225  -0.112863   0.12738     -0.303051   91  ASP   B CG   
2889 O OD1  . ASP   B 79  ? 0.541373 0.51494  0.981036 -0.101681   0.132526    -0.300181   91  ASP   B OD1  
2890 O OD2  . ASP   B 79  ? 0.65418  0.647062 1.05095  -0.112333   0.136278    -0.337616   91  ASP   B OD2  
2891 H H    . ASP   B 79  ? 0.470745 0.41915  0.764125 -0.119539   0.11081     -0.228593   91  ASP   B H    
2892 H HA   . ASP   B 79  ? 0.524385 0.431751 0.934924 -0.116291   0.0934234   -0.229788   91  ASP   B HA   
2893 H HB2  . ASP   B 79  ? 0.539859 0.478033 0.891762 -0.13064    0.113354    -0.264349   91  ASP   B HB2  
2894 H HB3  . ASP   B 79  ? 0.564584 0.461574 0.980582 -0.131286   0.104959    -0.264371   91  ASP   B HB3  
2895 N N    . ILE   B 80  ? 0.622062 0.46786  0.918654 -0.135929   0.0774945   -0.178713   92  ILE   B N    
2896 C CA   . ILE   B 80  ? 0.626813 0.426469 0.890993 -0.139252   0.0664053   -0.145559   92  ILE   B CA   
2897 C C    . ILE   B 80  ? 0.606197 0.375325 0.844374 -0.129697   0.0383149   -0.120533   92  ILE   B C    
2898 O O    . ILE   B 80  ? 0.704158 0.431476 0.942183 -0.125614   0.0194697   -0.0972778  92  ILE   B O    
2899 C CB   . ILE   B 80  ? 0.669025 0.482119 0.877512 -0.143854   0.0818189   -0.139202   92  ILE   B CB   
2900 C CG1  . ILE   B 80  ? 0.683293 0.523363 0.930838 -0.157907   0.10217     -0.159983   92  ILE   B CG1  
2901 C CG2  . ILE   B 80  ? 0.703896 0.473161 0.852016 -0.140304   0.0743475   -0.102151   92  ILE   B CG2  
2902 C CD1  . ILE   B 80  ? 0.732333 0.615814 0.944381 -0.157443   0.116765    -0.166146   92  ILE   B CD1  
2903 H H    . ILE   B 80  ? 0.594468 0.46687  0.868228 -0.135757   0.0875483   -0.188861   92  ILE   B H    
2904 H HA   . ILE   B 80  ? 0.65061  0.430634 0.946702 -0.14348    0.0671923   -0.143889   92  ILE   B HA   
2905 H HB   . ILE   B 80  ? 0.643981 0.479914 0.829031 -0.138106   0.083518    -0.147295   92  ILE   B HB   
2906 H HG12 . ILE   B 80  ? 0.719731 0.531834 0.981452 -0.166137   0.104342    -0.14539    92  ILE   B HG12 
2907 H HG13 . ILE   B 80  ? 0.676598 0.534122 0.96193  -0.158355   0.103113    -0.184943   92  ILE   B HG13 
2908 H HG21 . ILE   B 80  ? 0.712704 0.494298 0.840119 -0.143621   0.0902867   -0.0991062  92  ILE   B HG21 
2909 H HG22 . ILE   B 80  ? 0.734216 0.47266  0.898583 -0.142289   0.0676908   -0.0879031  92  ILE   B HG22 
2910 H HG23 . ILE   B 80  ? 0.710835 0.470149 0.823835 -0.131392   0.0603651   -0.0959192  92  ILE   B HG23 
2911 H HD11 . ILE   B 80  ? 0.692121 0.595568 0.882929 -0.147022   0.113844    -0.175571   92  ILE   B HD11 
2912 H HD12 . ILE   B 80  ? 0.707358 0.6157   0.954139 -0.167758   0.125834    -0.18397    92  ILE   B HD12 
2913 H HD13 . ILE   B 80  ? 0.731257 0.598597 0.908119 -0.155917   0.119938    -0.143253   92  ILE   B HD13 
2914 N N    . GLY   B 81  ? 0.589376 0.375721 0.80058  -0.126235   0.0331728   -0.124047   93  GLY   B N    
2915 C CA   . GLY   B 81  ? 0.618358 0.375076 0.799384 -0.121332   0.00236358  -0.105581   93  GLY   B CA   
2916 C C    . GLY   B 81  ? 0.645225 0.401265 0.895843 -0.1182     -0.0220276  -0.104049   93  GLY   B C    
2917 O O    . GLY   B 81  ? 0.634271 0.35594  0.874661 -0.111611   -0.0549906  -0.085089   93  GLY   B O    
2918 H H    . GLY   B 81  ? 0.566688 0.38188  0.777842 -0.127159   0.0478662   -0.138797   93  GLY   B H    
2919 H HA2  . GLY   B 81  ? 0.656193 0.382964 0.792196 -0.118251   -0.00568286 -0.0895615  93  GLY   B HA2  
2920 H HA3  . GLY   B 81  ? 0.612401 0.379308 0.771567 -0.12191    0.00442566  -0.110339   93  GLY   B HA3  
2921 N N    . VAL   B 82  ? 0.696347 0.495044 1.01707  -0.11946    -0.00514673 -0.12485    94  VAL   B N    
2922 C CA   . VAL   B 82  ? 0.631037 0.444659 1.03075  -0.114184   -0.0229766  -0.125897   94  VAL   B CA   
2923 C C    . VAL   B 82  ? 0.628679 0.414449 1.06421  -0.102635   -0.0367833  -0.118348   94  VAL   B C    
2924 O O    . VAL   B 82  ? 0.647522 0.431203 1.13259  -0.0926229  -0.0668975  -0.109153   94  VAL   B O    
2925 C CB   . VAL   B 82  ? 0.636581 0.506295 1.09309  -0.115349   0.00859471  -0.149083   94  VAL   B CB   
2926 C CG1  . VAL   B 82  ? 0.682359 0.580324 1.2383   -0.106289   -0.00010785 -0.153518   94  VAL   B CG1  
2927 C CG2  . VAL   B 82  ? 0.611744 0.496755 1.03083  -0.126142   0.0185673   -0.145933   94  VAL   B CG2  
2928 H H    . VAL   B 82  ? 0.636606 0.458306 0.955485 -0.121815   0.0182384   -0.139      94  VAL   B H    
2929 H HA   . VAL   B 82  ? 0.657169 0.461296 1.04762  -0.116033   -0.0469582  -0.115173   94  VAL   B HA   
2930 H HB   . VAL   B 82  ? 0.624698 0.502195 1.07631  -0.113273   0.0304657   -0.16368    94  VAL   B HB   
2931 H HG11 . VAL   B 82  ? 0.681632 0.567163 1.24784  -0.106847   -0.0303232  -0.139074   94  VAL   B HG11 
2932 H HG12 . VAL   B 82  ? 0.673804 0.565424 1.25609  -0.0964637  0.00362689  -0.161415   94  VAL   B HG12 
2933 H HG13 . VAL   B 82  ? 0.648997 0.584486 1.23353  -0.108485   0.0208627   -0.163106   94  VAL   B HG13 
2934 H HG21 . VAL   B 82  ? 0.600791 0.52061  1.05295  -0.126119   0.0406387   -0.155852   94  VAL   B HG21 
2935 H HG22 . VAL   B 82  ? 0.616134 0.488833 0.97733  -0.127396   0.027089    -0.145889   94  VAL   B HG22 
2936 H HG23 . VAL   B 82  ? 0.629584 0.500666 1.04992  -0.130835   -0.0056641  -0.133845   94  VAL   B HG23 
2937 N N    . ALA   B 83  ? 0.623168 0.386341 1.03893  -0.104207   -0.0176199  -0.12045    95  ALA   B N    
2938 C CA   . ALA   B 83  ? 0.700311 0.420526 1.14411  -0.0944066  -0.0301142  -0.106311   95  ALA   B CA   
2939 C C    . ALA   B 83  ? 0.724334 0.392461 1.11062  -0.0872753  -0.0646225  -0.06693    95  ALA   B C    
2940 O O    . ALA   B 83  ? 0.829587 0.458252 1.23655  -0.0736888  -0.0830997  -0.0469841  95  ALA   B O    
2941 C CB   . ALA   B 83  ? 0.73364  0.438017 1.17731  -0.104156   -0.00050346 -0.117572   95  ALA   B CB   
2942 H H    . ALA   B 83  ? 0.619513 0.393511 1.0081   -0.111711   0.00278193  -0.130081   95  ALA   B H    
2943 H HA   . ALA   B 83  ? 0.688386 0.422371 1.19413  -0.084053   -0.0363866  -0.115355   95  ALA   B HA   
2944 H HB1  . ALA   B 83  ? 0.696127 0.433707 1.16477  -0.107299   0.0185568   -0.145571   95  ALA   B HB1  
2945 H HB2  . ALA   B 83  ? 0.733378 0.425946 1.12436  -0.113273   0.00555807  -0.105172   95  ALA   B HB2  
2946 H HB3  . ALA   B 83  ? 0.7585   0.431153 1.23134  -0.0977479  -0.00683828 -0.109687   95  ALA   B HB3  
2947 N N    . THR   B 84  ? 0.778711 0.441204 1.08612  -0.0924694  -0.0741696  -0.0555124  96  THR   B N    
2948 C CA   . THR   B 84  ? 0.830802 0.445696 1.06966  -0.0810047  -0.110884   -0.0232089  96  THR   B CA   
2949 C C    . THR   B 84  ? 0.839733 0.464667 1.10642  -0.0706911  -0.160381   -0.0235566  96  THR   B C    
2950 O O    . THR   B 84  ? 0.934225 0.520291 1.14597  -0.0571296  -0.199227   -0.00049622 96  THR   B O    
2951 C CB   . THR   B 84  ? 0.839125 0.439178 0.973676 -0.0869618  -0.0986964  -0.0155928  96  THR   B CB   
2952 O OG1  . THR   B 84  ? 0.748968 0.377309 0.872553 -0.0929875  -0.105518   -0.0363909  96  THR   B OG1  
2953 C CG2  . THR   B 84  ? 0.822909 0.430627 0.946973 -0.0996626  -0.0503947  -0.0183512  96  THR   B CG2  
2954 H H    . THR   B 84  ? 0.731679 0.417886 1.02232  -0.101025   -0.0582237  -0.0688129  96  THR   B H    
2955 H HA   . THR   B 84  ? 0.869593 0.452724 1.10843  -0.0741928  -0.11225    -0.00504257 96  THR   B HA   
2956 H HB   . THR   B 84  ? 0.886908 0.450592 0.967156 -0.0767941  -0.118677   0.006518    96  THR   B HB   
2958 H HG21 . THR   B 84  ? 0.850664 0.442332 0.908768 -0.0984482  -0.0437181  -0.00528469 96  THR   B HG21 
2959 H HG22 . THR   B 84  ? 0.772621 0.416763 0.924872 -0.107704   -0.0335281  -0.0415969  96  THR   B HG22 
2960 H HG23 . THR   B 84  ? 0.836968 0.429687 0.993572 -0.100303   -0.0433841  -0.0102788  96  THR   B HG23 
2961 N N    . MET   B 85  ? 0.77     0.447895 1.11994  -0.0767161  -0.160143   -0.0481514  97  MET   B N    
2962 C CA   . MET   B 85  ? 0.773648 0.470093 1.15753  -0.0750036  -0.205818   -0.0505379  97  MET   B CA   
2963 C C    . MET   B 85  ? 0.780395 0.495362 1.26352  -0.0564356  -0.236588   -0.0464738  97  MET   B C    
2964 O O    . MET   B 85  ? 0.715852 0.441773 1.26193  -0.0467748  -0.212018   -0.0515233  97  MET   B O    
2965 C CB   . MET   B 85  ? 0.716714 0.462779 1.13944  -0.0953772  -0.184811   -0.0739449  97  MET   B CB   
2966 C CG   . MET   B 85  ? 0.68039  0.410328 1.01317  -0.108292   -0.156298   -0.0785503  97  MET   B CG   
2967 S SD   . MET   B 85  ? 0.672296 0.444682 1.03838  -0.129291   -0.132382   -0.0964423  97  MET   B SD   
2968 C CE   . MET   B 85  ? 0.727633 0.511257 1.16088  -0.139393   -0.186339   -0.0965603  97  MET   B CE   
2969 H H    . MET   B 85  ? 0.73235  0.437129 1.12057  -0.082622   -0.130762   -0.0639614  97  MET   B H    
2970 H HA   . MET   B 85  ? 0.819518 0.483327 1.13572  -0.0717076  -0.232294   -0.038966   97  MET   B HA   
2971 H HB2  . MET   B 85  ? 0.674491 0.454841 1.16029  -0.0957991  -0.159054   -0.0850733  97  MET   B HB2  
2972 H HB3  . MET   B 85  ? 0.723655 0.480155 1.17385  -0.098281   -0.216071   -0.0749872  97  MET   B HB3  
2973 H HG2  . MET   B 85  ? 0.73434  0.428867 1.00131  -0.105022   -0.179151   -0.0694708  97  MET   B HG2  
2974 H HG3  . MET   B 85  ? 0.679306 0.406612 0.994214 -0.10663    -0.12696    -0.0791883  97  MET   B HG3  
2975 H HE1  . MET   B 85  ? 0.701998 0.506176 1.16277  -0.153947   -0.171874   -0.102345   97  MET   B HE1  
2976 H HE2  . MET   B 85  ? 0.715124 0.522748 1.21589  -0.132492   -0.198151   -0.0956394  97  MET   B HE2  
2977 H HE3  . MET   B 85  ? 0.762789 0.508718 1.13996  -0.136834   -0.218964   -0.0923312  97  MET   B HE3  
2978 N N    . LYS   B 86  ? 0.814165 0.534201 1.31544  -0.0496277  -0.294493   -0.0408891  98  LYS   B N    
2979 C CA   . LYS   B 86  ? 0.828956 0.574409 1.42971  -0.027518   -0.33374    -0.0361041  98  LYS   B CA   
2980 C C    . LYS   B 86  ? 0.809762 0.635457 1.53143  -0.0426627  -0.334699   -0.0598894  98  LYS   B C    
2981 O O    . LYS   B 86  ? 0.820518 0.66221  1.52447  -0.0701215  -0.316712   -0.0729351  98  LYS   B O    
2982 C CB   . LYS   B 86  ? 0.857407 0.554034 1.39075  -0.00549092 -0.401454   -0.0107021  98  LYS   B CB   
2983 H H    . LYS   B 86  ? 0.830275 0.53854  1.28216  -0.0580585  -0.312117   -0.0419597  98  LYS   B H    
2984 H HA   . LYS   B 86  ? 0.815351 0.556862 1.44725  -0.0157713  -0.311029   -0.0335895  98  LYS   B HA   
2987 N N    . LYS   B 87  ? 0.840544 0.717674 1.68917  -0.0245621  -0.352131   -0.0636348  99  LYS   B N    
2988 C CA   . LYS   B 87  ? 0.786263 0.749492 1.76389  -0.0399801  -0.349527   -0.0823329  99  LYS   B CA   
2989 C C    . LYS   B 87  ? 0.847147 0.808126 1.80109  -0.0629342  -0.403537   -0.0833831  99  LYS   B C    
2990 O O    . LYS   B 87  ? 0.912594 0.831608 1.80736  -0.0489379  -0.467689   -0.0719453  99  LYS   B O    
2991 C CB   . LYS   B 87  ? 0.737921 0.767735 1.86807  -0.0130325  -0.362473   -0.0867599  99  LYS   B CB   
2992 H H    . LYS   B 87  ? 0.857132 0.715836 1.7152   -0.001497   -0.36416    -0.0529183  99  LYS   B H    
2993 H HA   . LYS   B 87  ? 0.742259 0.723708 1.72265  -0.055538   -0.299944   -0.0933005  99  LYS   B HA   
2996 N N    . GLY   B 88  ? 0.839736 0.835619 1.82501  -0.0980462  -0.376472   -0.0970685  100 GLY   B N    
2997 C CA   . GLY   B 88  ? 0.921715 0.912486 1.90115  -0.124398   -0.4268     -0.103577   100 GLY   B CA   
2998 C C    . GLY   B 88  ? 0.959256 0.862615 1.77265  -0.132439   -0.437453   -0.101886   100 GLY   B C    
2999 O O    . GLY   B 88  ? 1.01894  0.899883 1.80611  -0.148696   -0.487887   -0.111485   100 GLY   B O    
3000 H H    . GLY   B 88  ? 0.799523 0.819334 1.80846  -0.105575   -0.326392   -0.102586   100 GLY   B H    
3001 H HA2  . GLY   B 88  ? 0.87793  0.911276 1.92667  -0.147787   -0.402699   -0.111114   100 GLY   B HA2  
3002 H HA3  . GLY   B 88  ? 0.942403 0.947834 1.96603  -0.113384   -0.480166   -0.103014   100 GLY   B HA3  
3003 N N    . GLU   B 89  ? 0.979382 0.836456 1.68773  -0.120903   -0.390237   -0.0929433  101 GLU   B N    
3004 C CA   . GLU   B 89  ? 0.960115 0.744486 1.51843  -0.124644   -0.389271   -0.0911983  101 GLU   B CA   
3005 C C    . GLU   B 89  ? 0.857402 0.648939 1.41254  -0.154797   -0.346191   -0.102974   101 GLU   B C    
3006 O O    . GLU   B 89  ? 0.710173 0.549206 1.33333  -0.165008   -0.291916   -0.104948   101 GLU   B O    
3007 C CB   . GLU   B 89  ? 0.954198 0.69225  1.41558  -0.0998593  -0.364094   -0.0736927  101 GLU   B CB   
3008 C CG   . GLU   B 89  ? 1.01717  0.684005 1.32282  -0.094746   -0.368636   -0.0674998  101 GLU   B CG   
3009 C CD   . GLU   B 89  ? 0.999165 0.632469 1.22752  -0.0791087  -0.327229   -0.0484784  101 GLU   B CD   
3010 O OE1  . GLU   B 89  ? 1.09736  0.712828 1.32425  -0.0579726  -0.338695   -0.0272726  101 GLU   B OE1  
3011 O OE2  . GLU   B 89  ? 0.907701 0.534483 1.0851   -0.0893855  -0.280616   -0.0541732  101 GLU   B OE2  
3012 H H    . GLU   B 89  ? 0.926493 0.799719 1.66123  -0.110194   -0.357625   -0.089501   101 GLU   B H    
3013 H HA   . GLU   B 89  ? 1.00687  0.767133 1.53363  -0.122453   -0.440049   -0.0933963  101 GLU   B HA   
3014 H HB2  . GLU   B 89  ? 0.984902 0.722303 1.46827  -0.0814072  -0.389294   -0.0634269  101 GLU   B HB2  
3015 H HB3  . GLU   B 89  ? 0.911499 0.66853  1.39475  -0.103411   -0.316365   -0.0755986  101 GLU   B HB3  
3016 H HG2  . GLU   B 89  ? 0.994577 0.659128 1.28042  -0.110567   -0.352401   -0.0789264  101 GLU   B HG2  
3017 H HG3  . GLU   B 89  ? 1.06999  0.712864 1.34129  -0.0857191  -0.417038   -0.0653384  101 GLU   B HG3  
3018 N N    . ILE   B 90  ? 0.892734 0.635472 1.37273  -0.166994   -0.37681    -0.111605   102 ILE   B N    
3019 C CA   . ILE   B 90  ? 0.871923 0.588652 1.2963   -0.184458   -0.33652    -0.117144   102 ILE   B CA   
3020 C C    . ILE   B 90  ? 0.867422 0.518241 1.139    -0.16356    -0.328847   -0.113597   102 ILE   B C    
3021 O O    . ILE   B 90  ? 0.930505 0.533726 1.12065  -0.14815    -0.376049   -0.115277   102 ILE   B O    
3022 C CB   . ILE   B 90  ? 0.855604 0.559639 1.3151   -0.214834   -0.367962   -0.131574   102 ILE   B CB   
3023 C CG1  . ILE   B 90  ? 0.841299 0.620417 1.46977  -0.239544   -0.377359   -0.133099   102 ILE   B CG1  
3024 C CG2  . ILE   B 90  ? 0.838934 0.509423 1.23794  -0.226583   -0.319617   -0.1315     102 ILE   B CG2  
3025 C CD1  . ILE   B 90  ? 0.870434 0.635354 1.54945  -0.272999   -0.427087   -0.148961   102 ILE   B CD1  
3026 H H    . ILE   B 90  ? 0.945488 0.668353 1.40666  -0.1621     -0.425912   -0.115104   102 ILE   B H    
3027 H HA   . ILE   B 90  ? 0.802641 0.552518 1.26604  -0.188762   -0.290657   -0.113181   102 ILE   B HA   
3028 H HB   . ILE   B 90  ? 0.923693 0.58932  1.33224  -0.209209   -0.415391   -0.140157   102 ILE   B HB   
3029 H HG12 . ILE   B 90  ? 0.785261 0.59758  1.45556  -0.247132   -0.326806   -0.125734   102 ILE   B HG12 
3030 H HG13 . ILE   B 90  ? 0.827923 0.635786 1.49795  -0.225198   -0.399468   -0.130801   102 ILE   B HG13 
3031 H HG21 . ILE   B 90  ? 0.860072 0.526603 1.30112  -0.249494   -0.32961    -0.137081   102 ILE   B HG21 
3032 H HG22 . ILE   B 90  ? 0.791738 0.492967 1.20944  -0.223948   -0.272249   -0.122367   102 ILE   B HG22 
3033 H HG23 . ILE   B 90  ? 0.875106 0.496634 1.17452  -0.212506   -0.326053   -0.134878   102 ILE   B HG23 
3034 H HD11 . ILE   B 90  ? 0.927263 0.669604 1.57845  -0.264339   -0.483423   -0.159459   102 ILE   B HD11 
3035 H HD12 . ILE   B 90  ? 0.852986 0.673588 1.64774  -0.291512   -0.419936   -0.146599   102 ILE   B HD12 
3036 H HD13 . ILE   B 90  ? 0.895415 0.617856 1.52119  -0.284297   -0.410491   -0.151504   102 ILE   B HD13 
3037 N N    . ALA   B 91  ? 0.787675 0.441106 1.02354  -0.162836   -0.268731   -0.109696   103 ALA   B N    
3038 C CA   . ALA   B 91  ? 0.879086 0.487716 0.990411 -0.144932   -0.247337   -0.106131   103 ALA   B CA   
3039 C C    . ALA   B 91  ? 0.843411 0.442905 0.922262 -0.153157   -0.207813   -0.112059   103 ALA   B C    
3040 O O    . ALA   B 91  ? 0.839081 0.475796 0.989525 -0.169473   -0.179363   -0.111761   103 ALA   B O    
3041 C CB   . ALA   B 91  ? 0.849763 0.477613 0.954763 -0.128844   -0.214593   -0.0923498  103 ALA   B CB   
3042 H H    . ALA   B 91  ? 0.76796  0.456849 1.06181  -0.173      -0.238825   -0.109368   103 ALA   B H    
3043 H HA   . ALA   B 91  ? 0.919545 0.488253 0.96977  -0.136569   -0.281914   -0.108966   103 ALA   B HA   
3044 H HB1  . ALA   B 91  ? 0.866915 0.494078 0.990577 -0.121442   -0.239899   -0.0855377  103 ALA   B HB1  
3045 H HB2  . ALA   B 91  ? 0.79753  0.462115 0.955994 -0.135324   -0.182904   -0.0940194  103 ALA   B HB2  
3046 H HB3  . ALA   B 91  ? 0.865775 0.469015 0.895723 -0.11892    -0.200129   -0.0888852  103 ALA   B HB3  
3047 N N    . HIS   B 92  ? 0.85571  0.403876 0.822401 -0.137816   -0.20719    -0.115797   104 HIS   B N    
3048 C CA   . HIS   B 92  ? 0.813109 0.349063 0.728992 -0.13259    -0.16802    -0.118267   104 HIS   B CA   
3049 C C    . HIS   B 92  ? 0.778795 0.33869  0.653481 -0.113778   -0.125951   -0.109739   104 HIS   B C    
3050 O O    . HIS   B 92  ? 0.871029 0.417426 0.697183 -0.0995177  -0.133169   -0.103195   104 HIS   B O    
3051 C CB   . HIS   B 92  ? 0.888003 0.35199  0.713586 -0.123547   -0.198236   -0.132283   104 HIS   B CB   
3052 C CG   . HIS   B 92  ? 0.915053 0.35184  0.788404 -0.147903   -0.235844   -0.144509   104 HIS   B CG   
3053 N ND1  . HIS   B 92  ? 0.992688 0.357219 0.801303 -0.14544    -0.274141   -0.164703   104 HIS   B ND1  
3054 C CD2  . HIS   B 92  ? 0.865514 0.340863 0.8522   -0.176679   -0.236329   -0.139872   104 HIS   B CD2  
3055 C CE1  . HIS   B 92  ? 1.03241  0.392316 0.924092 -0.177183   -0.301948   -0.171869   104 HIS   B CE1  
3056 N NE2  . HIS   B 92  ? 0.932093 0.36384  0.93518  -0.196518   -0.275245   -0.154096   104 HIS   B NE2  
3057 H H    . HIS   B 92  ? 0.900647 0.420299 0.817814 -0.126965   -0.23351    -0.116569   104 HIS   B H    
3058 H HA   . HIS   B 92  ? 0.787447 0.345535 0.755763 -0.146051   -0.150837   -0.117213   104 HIS   B HA   
3059 H HB2  . HIS   B 92  ? 0.927374 0.371141 0.70222  -0.110212   -0.218671   -0.133393   104 HIS   B HB2  
3060 H HB3  . HIS   B 92  ? 0.889671 0.342889 0.671246 -0.11268    -0.171932   -0.132938   104 HIS   B HB3  
3062 H HD2  . HIS   B 92  ? 0.816101 0.34089  0.863408 -0.182333   -0.213441   -0.129774   104 HIS   B HD2  
3063 H HE1  . HIS   B 92  ? 1.08231  0.395325 0.958781 -0.185221   -0.333106   -0.18798    104 HIS   B HE1  
3065 N N    . LEU   B 93  ? 0.758135 0.354611 0.653984 -0.114563   -0.0829393  -0.108802   105 LEU   B N    
3066 C CA   . LEU   B 93  ? 0.707192 0.33575  0.580534 -0.101133   -0.0451792  -0.105998   105 LEU   B CA   
3067 C C    . LEU   B 93  ? 0.727324 0.349046 0.548394 -0.0870486  -0.02204    -0.110053   105 LEU   B C    
3068 O O    . LEU   B 93  ? 0.740507 0.358537 0.57854  -0.0930252  -0.0167168  -0.110509   105 LEU   B O    
3069 C CB   . LEU   B 93  ? 0.680957 0.369894 0.634202 -0.110862   -0.0193037  -0.106875   105 LEU   B CB   
3070 C CG   . LEU   B 93  ? 0.647264 0.349942 0.663783 -0.118768   -0.0337693  -0.103474   105 LEU   B CG   
3071 C CD1  . LEU   B 93  ? 0.57442  0.330714 0.656074 -0.122815   -0.00268383 -0.112168   105 LEU   B CD1  
3072 C CD2  . LEU   B 93  ? 0.749699 0.42482  0.717416 -0.108536   -0.0432813  -0.0926659  105 LEU   B CD2  
3073 H H    . LEU   B 93  ? 0.735459 0.338531 0.663642 -0.124663   -0.0779699  -0.110011   105 LEU   B H    
3074 H HA   . LEU   B 93  ? 0.742203 0.3571   0.58001  -0.0926085  -0.0509546  -0.101806   105 LEU   B HA   
3075 H HB2  . LEU   B 93  ? 0.651987 0.354443 0.633462 -0.117503   -0.0113282  -0.109212   105 LEU   B HB2  
3076 H HB3  . LEU   B 93  ? 0.650843 0.359681 0.587599 -0.103331   0.00299184  -0.108732   105 LEU   B HB3  
3077 H HG   . LEU   B 93  ? 0.669976 0.363646 0.715823 -0.126145   -0.056647   -0.102804   105 LEU   B HG   
3078 H HD11 . LEU   B 93  ? 0.564201 0.339635 0.667628 -0.126905   0.00832965  -0.116908   105 LEU   B HD11 
3079 H HD12 . LEU   B 93  ? 0.57587  0.336737 0.70046  -0.125325   -0.0118303  -0.110994   105 LEU   B HD12 
3080 H HD13 . LEU   B 93  ? 0.572342 0.338651 0.630777 -0.117653   0.0150613   -0.114898   105 LEU   B HD13 
3081 H HD21 . LEU   B 93  ? 0.769481 0.409426 0.692456 -0.103601   -0.0663876  -0.0892597  105 LEU   B HD21 
3082 H HD22 . LEU   B 93  ? 0.720311 0.405352 0.66097  -0.103155   -0.0201295  -0.0928836  105 LEU   B HD22 
3083 H HD23 . LEU   B 93  ? 0.720195 0.402157 0.727836 -0.111234   -0.0490942  -0.0883328  105 LEU   B HD23 
3084 N N    . LEU   B 94  ? 0.710321 0.334197 0.473095 -0.066924   -0.00489259 -0.109902   106 LEU   B N    
3085 C CA   . LEU   B 94  ? 0.71514  0.343045 0.434897 -0.0464338  0.017467    -0.11388    106 LEU   B CA   
3086 C C    . LEU   B 94  ? 0.68609  0.38145  0.431171 -0.041115   0.0498349   -0.114401   106 LEU   B C    
3087 O O    . LEU   B 94  ? 0.723831 0.439005 0.479198 -0.0450286  0.0576199   -0.110473   106 LEU   B O    
3088 C CB   . LEU   B 94  ? 0.781361 0.351585 0.412033 -0.0232463  0.00583326  -0.118491   106 LEU   B CB   
3089 C CG   . LEU   B 94  ? 0.841353 0.415196 0.428502 0.00598295  0.0289947   -0.122989   106 LEU   B CG   
3090 C CD1  . LEU   B 94  ? 0.855146 0.406965 0.451677 0.00662803  0.0274336   -0.122493   106 LEU   B CD1  
3091 C CD2  . LEU   B 94  ? 0.99695  0.516507 0.495705 0.0337135   0.0219853   -0.131433   106 LEU   B CD2  
3092 H H    . LEU   B 94  ? 0.72408  0.348528 0.476218 -0.0648306  -0.00631506 -0.10569    106 LEU   B H    
3093 H HA   . LEU   B 94  ? 0.713097 0.337957 0.449728 -0.0508731  0.0181451   -0.11416    106 LEU   B HA   
3094 H HB2  . LEU   B 94  ? 0.826988 0.353264 0.447767 -0.0296686  -0.0191219  -0.122375   106 LEU   B HB2  
3095 H HB3  . LEU   B 94  ? 0.805371 0.377586 0.415325 -0.0190007  0.00688762  -0.115235   106 LEU   B HB3  
3096 H HG   . LEU   B 94  ? 0.810039 0.435308 0.416858 0.0105917   0.0512967   -0.1207     106 LEU   B HG   
3097 H HD11 . LEU   B 94  ? 0.808068 0.394966 0.454328 -0.00835968 0.0348608   -0.117134   106 LEU   B HD11 
3098 H HD12 . LEU   B 94  ? 0.869651 0.424112 0.4367   0.029785    0.040825    -0.123911   106 LEU   B HD12 
3099 H HD13 . LEU   B 94  ? 0.894364 0.393697 0.476658 -0.00024692 0.0059242   -0.125552   106 LEU   B HD13 
3100 H HD21 . LEU   B 94  ? 0.979553 0.509499 0.462442 0.0357137   0.0263477   -0.128123   106 LEU   B HD21 
3101 H HD22 . LEU   B 94  ? 1.01401  0.480081 0.492236 0.0292139   -0.0032838  -0.137787   106 LEU   B HD22 
3102 H HD23 . LEU   B 94  ? 0.982878 0.509602 0.459779 0.0557187   0.0384226   -0.13439    106 LEU   B HD23 
3103 N N    . ILE   B 95  ? 0.67337  0.405909 0.434939 -0.03448    0.0675231   -0.118674   107 ILE   B N    
3104 C CA   . ILE   B 95  ? 0.601419 0.403974 0.410005 -0.0383522  0.08804     -0.125959   107 ILE   B CA   
3105 C C    . ILE   B 95  ? 0.654493 0.498488 0.442331 -0.0135223  0.105064    -0.132026   107 ILE   B C    
3106 O O    . ILE   B 95  ? 0.603132 0.443589 0.370515 0.0013055   0.105949    -0.130451   107 ILE   B O    
3107 C CB   . ILE   B 95  ? 0.572665 0.398954 0.438832 -0.0561064  0.0887431   -0.130659   107 ILE   B CB   
3108 C CG1  . ILE   B 95  ? 0.56795  0.364745 0.47003  -0.0769396  0.0705928   -0.125485   107 ILE   B CG1  
3109 C CG2  . ILE   B 95  ? 0.501101 0.394593 0.411011 -0.0589767  0.10508     -0.146885   107 ILE   B CG2  
3110 C CD1  . ILE   B 95  ? 0.568459 0.385663 0.525407 -0.0897433  0.074979    -0.128403   107 ILE   B CD1  
3111 H H    . ILE   B 95  ? 0.683241 0.395878 0.425401 -0.0270583  0.0654081   -0.117542   107 ILE   B H    
3112 H HA   . ILE   B 95  ? 0.611077 0.420998 0.431552 -0.0450558  0.0900543   -0.124939   107 ILE   B HA   
3113 H HB   . ILE   B 95  ? 0.575769 0.39353  0.427402 -0.0500259  0.0901582   -0.127469   107 ILE   B HB   
3114 H HG12 . ILE   B 95  ? 0.564853 0.37018  0.484774 -0.082412   0.0705188   -0.126645   107 ILE   B HG12 
3115 H HG13 . ILE   B 95  ? 0.605671 0.360918 0.478397 -0.0754116  0.0554151   -0.118803   107 ILE   B HG13 
3116 H HG21 . ILE   B 95  ? 0.493605 0.396949 0.439269 -0.0699793  0.105438    -0.152124   107 ILE   B HG21 
3117 H HG22 . ILE   B 95  ? 0.50623  0.408076 0.425568 -0.0628472  0.107325    -0.148393   107 ILE   B HG22 
3118 H HG23 . ILE   B 95  ? 0.511738 0.429277 0.404809 -0.045138   0.112279    -0.151222   107 ILE   B HG23 
3119 H HD11 . ILE   B 95  ? 0.571783 0.386115 0.510852 -0.0842472  0.0815015   -0.124692   107 ILE   B HD11 
3120 H HD12 . ILE   B 95  ? 0.566278 0.363431 0.546863 -0.100453   0.060368    -0.123825   107 ILE   B HD12 
3121 H HD13 . ILE   B 95  ? 0.534434 0.387781 0.521534 -0.0917049  0.0863616   -0.138538   107 ILE   B HD13 
3122 N N    . LYS   B 96  ? 0.598234 0.488293 0.400779 -0.00972701 0.119385    -0.137254   108 LYS   B N    
3123 C CA   . LYS   B 96  ? 0.59532  0.540685 0.395545 0.0142253   0.1316      -0.145644   108 LYS   B CA   
3124 C C    . LYS   B 96  ? 0.562052 0.566609 0.410206 0.00647891  0.13151     -0.161302   108 LYS   B C    
3125 O O    . LYS   B 96  ? 0.524486 0.535352 0.417105 -0.0194293  0.129233    -0.168854   108 LYS   B O    
3126 C CB   . LYS   B 96  ? 0.648337 0.63009  0.461921 0.0166225   0.14917     -0.145336   108 LYS   B CB   
3127 C CG   . LYS   B 96  ? 0.763202 0.697579 0.512806 0.0360746   0.155498    -0.133098   108 LYS   B CG   
3128 C CD   . LYS   B 96  ? 0.781488 0.77381  0.554878 0.0407293   0.183743    -0.130781   108 LYS   B CD   
3129 C CE   . LYS   B 96  ? 0.846177 0.802824 0.547023 0.0704105   0.197207    -0.122003   108 LYS   B CE   
3130 N NZ   . LYS   B 96  ? 0.920538 0.815364 0.582255 0.0542472   0.193758    -0.106834   108 LYS   B NZ   
3131 H H    . LYS   B 96  ? 0.605653 0.493995 0.422909 -0.0219177  0.121246    -0.13436    108 LYS   B H    
3132 H HA   . LYS   B 96  ? 0.633021 0.552642 0.391829 0.0347762   0.128438    -0.141199   108 LYS   B HA   
3133 H HB2  . LYS   B 96  ? 0.630252 0.620648 0.480574 -0.00624607 0.151629    -0.145455   108 LYS   B HB2  
3134 H HB3  . LYS   B 96  ? 0.638529 0.672691 0.471626 0.0281013   0.1558      -0.153973   108 LYS   B HB3  
3135 H HG2  . LYS   B 96  ? 0.776235 0.6901   0.487557 0.0591013   0.15101     -0.134314   108 LYS   B HG2  
3136 H HG3  . LYS   B 96  ? 0.765969 0.653724 0.498294 0.0235067   0.146457    -0.125747   108 LYS   B HG3  
3137 H HD2  . LYS   B 96  ? 0.764033 0.763283 0.570456 0.01634     0.188847    -0.125783   108 LYS   B HD2  
3138 H HD3  . LYS   B 96  ? 0.7563   0.805219 0.563035 0.0489695   0.188976    -0.140496   108 LYS   B HD3  
3139 H HE2  . LYS   B 96  ? 0.858941 0.865068 0.578431 0.080763    0.21901     -0.121868   108 LYS   B HE2  
3140 H HE3  . LYS   B 96  ? 0.878324 0.801697 0.537147 0.0919452   0.186216    -0.126625   108 LYS   B HE3  
3141 H HZ1  . LYS   B 96  ? 0.89038  0.811701 0.587892 0.0365264   0.206754    -0.0991792  108 LYS   B HZ1  
3142 H HZ2  . LYS   B 96  ? 0.900733 0.757147 0.556177 0.0431233   0.172113    -0.107744   108 LYS   B HZ2  
3143 H HZ3  . LYS   B 96  ? 0.955171 0.823321 0.562547 0.0743328   0.199956    -0.103992   108 LYS   B HZ3  
3144 N N    . PRO   B 97  ? 0.562491 0.613594 0.400293 0.033015    0.132536    -0.168889   109 PRO   B N    
3145 C CA   . PRO   B 97  ? 0.517706 0.619525 0.377347 0.0341674   0.127651    -0.185044   109 PRO   B CA   
3146 C C    . PRO   B 97  ? 0.496413 0.656254 0.425443 0.00860287  0.127005    -0.211532   109 PRO   B C    
3147 O O    . PRO   B 97  ? 0.570554 0.747158 0.512542 0.00170132  0.122385    -0.227578   109 PRO   B O    
3148 C CB   . PRO   B 97  ? 0.522947 0.66225  0.352243 0.0735024   0.124001    -0.185465   109 PRO   B CB   
3149 C CG   . PRO   B 97  ? 0.563915 0.683224 0.367477 0.0951508   0.130785    -0.173464   109 PRO   B CG   
3150 C CD   . PRO   B 97  ? 0.607594 0.657603 0.401688 0.0699923   0.136032    -0.16175    109 PRO   B CD   
3151 H HA   . PRO   B 97  ? 0.528835 0.598754 0.371354 0.0306198   0.125888    -0.178018   109 PRO   B HA   
3152 H HB2  . PRO   B 97  ? 0.517092 0.717187 0.378624 0.074442    0.119988    -0.203129   109 PRO   B HB2  
3153 H HB3  . PRO   B 97  ? 0.553491 0.670672 0.347403 0.0864264   0.120817    -0.176526   109 PRO   B HB3  
3154 H HG2  . PRO   B 97  ? 0.557543 0.731167 0.392809 0.0998571   0.134646    -0.183458   109 PRO   B HG2  
3155 H HG3  . PRO   B 97  ? 0.601666 0.69642  0.362744 0.121233    0.127698    -0.163441   109 PRO   B HG3  
3156 H HD2  . PRO   B 97  ? 0.597046 0.660227 0.400838 0.07007     0.144851    -0.162095   109 PRO   B HD2  
3157 H HD3  . PRO   B 97  ? 0.625787 0.619259 0.376814 0.0794061   0.132098    -0.15015    109 PRO   B HD3  
3158 N N    . GLU   B 98  ? 0.496524 0.685224 0.468633 -0.00422827 0.133566    -0.216819   110 GLU   B N    
3159 C CA   . GLU   B 98  ? 0.505429 0.733278 0.551385 -0.0346094  0.133763    -0.239637   110 GLU   B CA   
3160 C C    . GLU   B 98  ? 0.454662 0.63216  0.518374 -0.0608941  0.132682    -0.240158   110 GLU   B C    
3161 O O    . GLU   B 98  ? 0.462181 0.665275 0.577906 -0.0792819  0.128667    -0.266266   110 GLU   B O    
3162 C CB   . GLU   B 98  ? 0.567839 0.820877 0.654561 -0.0465268  0.149219    -0.232174   110 GLU   B CB   
3163 C CG   . GLU   B 98  ? 0.688791 1.00514  0.775871 -0.0185737  0.154532    -0.232752   110 GLU   B CG   
3164 C CD   . GLU   B 98  ? 0.785227 1.06285  0.797257 0.017397    0.162616    -0.207889   110 GLU   B CD   
3165 O OE1  . GLU   B 98  ? 0.769164 0.96708  0.73537  0.0106854   0.165985    -0.188339   110 GLU   B OE1  
3166 O OE2  . GLU   B 98  ? 0.884102 1.20544  0.883063 0.0532239   0.161945    -0.210125   110 GLU   B OE2  
3167 H H    . GLU   B 98  ? 0.514736 0.695515 0.470139 0.00604852  0.140034    -0.204914   110 GLU   B H    
3168 H HA   . GLU   B 98  ? 0.498345 0.77341  0.559781 -0.0286114  0.124736    -0.260945   110 GLU   B HA   
3169 H HB2  . GLU   B 98  ? 0.585095 0.789786 0.64886  -0.0510059  0.157546    -0.211501   110 GLU   B HB2  
3170 H HB3  . GLU   B 98  ? 0.564498 0.840714 0.706191 -0.0695582  0.149275    -0.246966   110 GLU   B HB3  
3171 H HG2  . GLU   B 98  ? 0.67098  1.02022  0.807127 -0.0339903  0.16604     -0.234312   110 GLU   B HG2  
3172 H HG3  . GLU   B 98  ? 0.670482 1.02958  0.766291 -0.00727326 0.140699    -0.25123    110 GLU   B HG3  
3173 N N    . TYR   B 99  ? 0.437908 0.548    0.465757 -0.0616271  0.13351     -0.215549   111 TYR   B N    
3174 C CA   . TYR   B 99  ? 0.480675 0.550374 0.532719 -0.0810807  0.129957    -0.214974   111 TYR   B CA   
3175 C C    . TYR   B 99  ? 0.496324 0.554777 0.521189 -0.0695235  0.126988    -0.215475   111 TYR   B C    
3176 O O    . TYR   B 99  ? 0.45474  0.478485 0.491992 -0.078851   0.125216    -0.208005   111 TYR   B O    
3177 C CB   . TYR   B 99  ? 0.47339  0.484275 0.512838 -0.090404   0.129272    -0.18706    111 TYR   B CB   
3178 C CG   . TYR   B 99  ? 0.498801 0.51948  0.568399 -0.104984   0.140368    -0.181492   111 TYR   B CG   
3179 C CD1  . TYR   B 99  ? 0.4712   0.5153   0.518769 -0.0941881  0.153768    -0.171652   111 TYR   B CD1  
3180 C CD2  . TYR   B 99  ? 0.546603 0.558969 0.675386 -0.129191   0.141596    -0.187338   111 TYR   B CD2  
3181 C CE1  . TYR   B 99  ? 0.504657 0.565239 0.588398 -0.11065    0.171594    -0.162915   111 TYR   B CE1  
3182 C CE2  . TYR   B 99  ? 0.533336 0.551546 0.696706 -0.147045   0.156211    -0.177881   111 TYR   B CE2  
3183 C CZ   . TYR   B 99  ? 0.530408 0.576618 0.673125 -0.139667   0.173228    -0.164401   111 TYR   B CZ   
3184 O OH   . TYR   B 99  ? 0.575934 0.629001 0.760616 -0.16125    0.193674    -0.150521   111 TYR   B OH   
3185 H H    . TYR   B 99  ? 0.468445 0.557341 0.457711 -0.0483951  0.134722    -0.19972    111 TYR   B H    
3186 H HA   . TYR   B 99  ? 0.459624 0.550684 0.556048 -0.0944547  0.130412    -0.233219   111 TYR   B HA   
3187 H HB2  . TYR   B 99  ? 0.4968   0.486972 0.491062 -0.0768908  0.127407    -0.173584   111 TYR   B HB2  
3188 H HB3  . TYR   B 99  ? 0.479431 0.464272 0.534189 -0.0990511  0.123236    -0.185076   111 TYR   B HB3  
3189 H HD1  . TYR   B 99  ? 0.492344 0.539354 0.500527 -0.0746011  0.152863    -0.169058   111 TYR   B HD1  
3190 H HD2  . TYR   B 99  ? 0.518767 0.518495 0.666521 -0.133427   0.134058    -0.196423   111 TYR   B HD2  
3191 H HE1  . TYR   B 99  ? 0.518135 0.599186 0.588988 -0.101753   0.184506    -0.155201   111 TYR   B HE1  
3192 H HE2  . TYR   B 99  ? 0.542249 0.54525  0.745585 -0.163686   0.156691    -0.179729   111 TYR   B HE2  
3194 N N    . ALA   B 100 ? 0.509341 0.598847 0.497511 -0.0472058  0.127937    -0.220474   112 ALA   B N    
3195 C CA   . ALA   B 100 ? 0.473598 0.547796 0.429873 -0.036726   0.132368    -0.211796   112 ALA   B CA   
3196 C C    . ALA   B 100 ? 0.453913 0.58412  0.394012 -0.0186153  0.133918    -0.234026   112 ALA   B C    
3197 O O    . ALA   B 100 ? 0.47618  0.638393 0.453243 -0.0280791  0.133435    -0.264553   112 ALA   B O    
3198 C CB   . ALA   B 100 ? 0.514372 0.538975 0.417484 -0.0236474  0.131248    -0.1809     112 ALA   B CB   
3199 H H    . ALA   B 100 ? 0.496791 0.618096 0.481028 -0.0378636  0.126702    -0.227395   112 ALA   B H    
3200 H HA   . ALA   B 100 ? 0.471007 0.529631 0.454197 -0.0504279  0.134856    -0.2128     112 ALA   B HA   
3201 H HB1  . ALA   B 100 ? 0.507339 0.495013 0.41965  -0.0362002  0.127311    -0.170731   112 ALA   B HB1  
3202 H HB2  . ALA   B 100 ? 0.5177   0.551848 0.399325 -0.00948603 0.128685    -0.179583   112 ALA   B HB2  
3203 H HB3  . ALA   B 100 ? 0.527113 0.54572  0.408833 -0.0160381  0.136713    -0.172941   112 ALA   B HB3  
3204 N N    . TYR   B 101 ? 0.492358 0.632782 0.376862 0.00963845  0.131999    -0.221809   113 TYR   B N    
3205 C CA   . TYR   B 101 ? 0.52326  0.711163 0.370528 0.0357079   0.129175    -0.23515    113 TYR   B CA   
3206 C C    . TYR   B 101 ? 0.52606  0.765257 0.363895 0.0596453   0.112175    -0.246034   113 TYR   B C    
3207 O O    . TYR   B 101 ? 0.529544 0.811995 0.329748 0.0884333   0.101734    -0.255522   113 TYR   B O    
3208 C CB   . TYR   B 101 ? 0.581446 0.730081 0.36684  0.0526234   0.143628    -0.201723   113 TYR   B CB   
3209 C CG   . TYR   B 101 ? 0.573235 0.68775  0.382728 0.0288851   0.162847    -0.191768   113 TYR   B CG   
3210 C CD1  . TYR   B 101 ? 0.544417 0.691262 0.363854 0.027186    0.175698    -0.213063   113 TYR   B CD1  
3211 C CD2  . TYR   B 101 ? 0.560559 0.61448  0.385583 0.0103672   0.167088    -0.164031   113 TYR   B CD2  
3212 C CE1  . TYR   B 101 ? 0.543935 0.670528 0.396101 0.00922406  0.196457    -0.204414   113 TYR   B CE1  
3213 C CE2  . TYR   B 101 ? 0.571273 0.606487 0.43317  -0.0109091  0.182247    -0.1556     113 TYR   B CE2  
3214 C CZ   . TYR   B 101 ? 0.557084 0.631918 0.436648 -0.0108326  0.200035    -0.173957   113 TYR   B CZ   
3215 O OH   . TYR   B 101 ? 0.540059 0.608431 0.467175 -0.0282364  0.219469    -0.166691   113 TYR   B OH   
3216 H H    . TYR   B 101 ? 0.498797 0.611626 0.363125 0.0156603   0.131049    -0.203294   113 TYR   B H    
3217 H HA   . TYR   B 101 ? 0.51978  0.733139 0.389921 0.027332    0.129363    -0.259575   113 TYR   B HA   
3218 H HB2  . TYR   B 101 ? 0.590488 0.706908 0.353937 0.0607336   0.141936    -0.179714   113 TYR   B HB2  
3219 H HB3  . TYR   B 101 ? 0.608965 0.787357 0.359934 0.0731668   0.142327    -0.207446   113 TYR   B HB3  
3220 H HD1  . TYR   B 101 ? 0.566527 0.752905 0.37227  0.0398761   0.169565    -0.236396   113 TYR   B HD1  
3221 H HD2  . TYR   B 101 ? 0.56731  0.594299 0.379347 0.0133727   0.158454    -0.152226   113 TYR   B HD2  
3222 H HE1  . TYR   B 101 ? 0.561053 0.712335 0.417377 0.0122987   0.207867    -0.220963   113 TYR   B HE1  
3223 H HE2  . TYR   B 101 ? 0.560953 0.558452 0.437207 -0.0239777  0.180104    -0.138941   113 TYR   B HE2  
3225 N N    . GLY   B 102 ? 0.592676 0.833758 0.465962 0.0505386   0.109065    -0.244652   114 GLY   B N    
3226 C CA   . GLY   B 102 ? 0.563457 0.875379 0.469396 0.060917    0.0956822   -0.26566    114 GLY   B CA   
3227 C C    . GLY   B 102 ? 0.634772 0.973291 0.487403 0.106552    0.0845475   -0.25539    114 GLY   B C    
3228 O O    . GLY   B 102 ? 0.650569 0.932563 0.437314 0.128373    0.0915779   -0.223536   114 GLY   B O    
3229 H H    . GLY   B 102 ? 0.549467 0.748948 0.427995 0.0379125   0.116103    -0.229615   114 GLY   B H    
3230 H HA2  . GLY   B 102 ? 0.557978 0.862364 0.490703 0.0500107   0.101559    -0.259312   114 GLY   B HA2  
3231 H HA3  . GLY   B 102 ? 0.567689 0.918914 0.508071 0.0491016   0.087742    -0.293632   114 GLY   B HA3  
3232 N N    . SER   B 103 ? 0.64602  1.07001  0.533147 0.120184    0.0651177   -0.282603   115 SER   B N    
3233 C CA   . SER   B 103 ? 0.70644  1.15962  0.552908 0.169006    0.0519618   -0.270048   115 SER   B CA   
3234 C C    . SER   B 103 ? 0.725342 1.17628  0.496072 0.19862     0.0396214   -0.266307   115 SER   B C    
3235 O O    . SER   B 103 ? 0.771627 1.20161  0.476167 0.241182    0.035886    -0.237971   115 SER   B O    
3236 C CB   . SER   B 103 ? 0.724831 1.27386  0.642091 0.176928    0.0359252   -0.29482    115 SER   B CB   
3237 O OG   . SER   B 103 ? 0.728993 1.34673  0.700014 0.154755    0.014657    -0.339003   115 SER   B OG   
3238 H H    . SER   B 103 ? 0.628302 1.09087  0.566159 0.100256    0.0587599   -0.308404   115 SER   B H    
3239 H HA   . SER   B 103 ? 0.708839 1.1113   0.526489 0.17909     0.0644459   -0.243196   115 SER   B HA   
3240 H HB2  . SER   B 103 ? 0.750287 1.3211   0.640597 0.214188    0.0249033   -0.28665    115 SER   B HB2  
3241 H HB3  . SER   B 103 ? 0.693651 1.23576  0.648401 0.16078     0.0510477   -0.289133   115 SER   B HB3  
3243 N N    . ALA   B 104 ? 0.785198 1.24861  0.556881 0.178863    0.0366508   -0.291835   116 ALA   B N    
3244 C CA   . ALA   B 104 ? 0.822242 1.28783  0.511398 0.209292    0.0297209   -0.28853    116 ALA   B CA   
3245 C C    . ALA   B 104 ? 0.810003 1.18344  0.435106 0.209043    0.0616804   -0.242184   116 ALA   B C    
3246 O O    . ALA   B 104 ? 0.966965 1.324    0.510518 0.239147    0.0662995   -0.219466   116 ALA   B O    
3247 C CB   . ALA   B 104 ? 0.826778 1.34066  0.535476 0.192482    0.016577    -0.338489   116 ALA   B CB   
3248 H H    . ALA   B 104 ? 0.729347 1.19877  0.550078 0.148175    0.0400902   -0.311488   116 ALA   B H    
3249 H HA   . ALA   B 104 ? 0.854281 1.35031  0.515226 0.243962    0.0121996   -0.283404   116 ALA   B HA   
3250 H HB1  . ALA   B 104 ? 0.816628 1.38954  0.569789 0.191273    -0.00680356 -0.368958   116 ALA   B HB1  
3251 H HB2  . ALA   B 104 ? 0.794656 1.27944  0.53565  0.161183    0.0329866   -0.344217   116 ALA   B HB2  
3252 H HB3  . ALA   B 104 ? 0.878323 1.39264  0.523013 0.215236    0.0148047   -0.335374   116 ALA   B HB3  
3253 N N    . GLY   B 105 ? 0.777521 1.09366  0.444036 0.172477    0.0833095   -0.228888   117 GLY   B N    
3254 C CA   . GLY   B 105 ? 0.797789 1.03322  0.431919 0.160225    0.111159    -0.191761   117 GLY   B CA   
3255 C C    . GLY   B 105 ? 0.812923 1.05833  0.420688 0.156165    0.126139    -0.200099   117 GLY   B C    
3256 O O    . GLY   B 105 ? 0.757641 1.06048  0.390011 0.151052    0.113929    -0.243814   117 GLY   B O    
3257 H H    . GLY   B 105 ? 0.733754 1.06334  0.453105 0.153777    0.0798265   -0.243337   117 GLY   B H    
3258 H HA2  . GLY   B 105 ? 0.753535 0.960459 0.428142 0.133743    0.118246    -0.190338   117 GLY   B HA2  
3259 H HA3  . GLY   B 105 ? 0.831162 1.03366  0.420956 0.182147    0.113659    -0.162423   117 GLY   B HA3  
3260 N N    . SER   B 106 ? 0.811728 0.999466 0.377351 0.155957    0.15415     -0.159747   118 SER   B N    
3261 C CA   . SER   B 106 ? 0.848602 1.04173  0.389212 0.152946    0.180086    -0.158865   118 SER   B CA   
3262 C C    . SER   B 106 ? 0.943564 1.08517  0.408983 0.17403     0.203572    -0.102415   118 SER   B C    
3263 O O    . SER   B 106 ? 0.929055 1.01854  0.40756  0.151505    0.234219    -0.0685054  118 SER   B O    
3264 C CB   . SER   B 106 ? 0.7892   0.968904 0.40242  0.112134    0.199174    -0.171478   118 SER   B CB   
3265 O OG   . SER   B 106 ? 0.798377 0.999469 0.380819 0.119847    0.226113    -0.176309   118 SER   B OG   
3266 H H    . SER   B 106 ? 0.831314 0.974142 0.38614  0.157484    0.158554    -0.131454   118 SER   B H    
3267 H HA   . SER   B 106 ? 0.870096 1.11148  0.389183 0.169282    0.169085    -0.186162   118 SER   B HA   
3268 H HB2  . SER   B 106 ? 0.736765 0.939387 0.397246 0.0989166   0.183694    -0.202771   118 SER   B HB2  
3269 H HB3  . SER   B 106 ? 0.769768 0.904004 0.401285 0.096489    0.208712    -0.144781   118 SER   B HB3  
3271 N N    . LEU   B 107 ? 1.01135  1.17074  0.404665 0.21799     0.185196    -0.0931697  119 LEU   B N    
3272 C CA   . LEU   B 107 ? 1.15686  1.26728  0.463649 0.248967    0.201787    -0.037369   119 LEU   B CA   
3273 C C    . LEU   B 107 ? 1.21711  1.31518  0.478013 0.245787    0.246039    -0.0100386  119 LEU   B C    
3274 O O    . LEU   B 107 ? 1.21873  1.36725  0.484876 0.239173    0.258209    -0.0428853  119 LEU   B O    
3275 C CB   . LEU   B 107 ? 1.24295  1.39904  0.48816  0.301724    0.16528     -0.0464569  119 LEU   B CB   
3276 C CG   . LEU   B 107 ? 1.28279  1.45016  0.578759 0.308386    0.130337    -0.0634571  119 LEU   B CG   
3277 C CD1  . LEU   B 107 ? 1.41331  1.63224  0.656957 0.366399    0.0927997   -0.0677405  119 LEU   B CD1  
3278 C CD2  . LEU   B 107 ? 1.19992  1.27315  0.511495 0.29347     0.146628    -0.022897   119 LEU   B CD2  
3279 H H    . LEU   B 107 ? 1.00683  1.21204  0.407607 0.229688    0.160193    -0.122813   119 LEU   B H    
3280 H HA   . LEU   B 107 ? 1.14549  1.20119  0.469506 0.238341    0.205948    -0.0121758  119 LEU   B HA   
3281 H HB2  . LEU   B 107 ? 1.25343  1.4674   0.490402 0.308758    0.15441     -0.0801561  119 LEU   B HB2  
3282 H HB3  . LEU   B 107 ? 1.3292   1.45258  0.506867 0.328104    0.175095    -0.00740829 119 LEU   B HB3  
3283 H HG   . LEU   B 107 ? 1.18953  1.39393  0.548399 0.28366     0.121195    -0.100903   119 LEU   B HG   
3284 H HD11 . LEU   B 107 ? 1.46633  1.64793  0.641637 0.39429     0.100797    -0.0294372  119 LEU   B HD11 
3285 H HD12 . LEU   B 107 ? 1.39007  1.67223  0.631868 0.372139    0.0767313   -0.101118   119 LEU   B HD12 
3286 H HD13 . LEU   B 107 ? 1.35634  1.58226  0.6384   0.370468    0.0767157   -0.0755397  119 LEU   B HD13 
3287 H HD21 . LEU   B 107 ? 1.28297  1.30783  0.545035 0.303229    0.16492     0.0154296   119 LEU   B HD21 
3288 H HD22 . LEU   B 107 ? 1.21602  1.2901   0.533519 0.312122    0.127907    -0.0250225  119 LEU   B HD22 
3289 H HD23 . LEU   B 107 ? 1.16252  1.22201  0.527715 0.256595    0.156888    -0.0336776  119 LEU   B HD23 
3290 N N    . PRO   B 108 ? 1.2959   1.32132  0.512346 0.250392    0.275313    0.0532559   120 PRO   B N    
3291 C CA   . PRO   B 108 ? 1.29523  1.24617  0.512261 0.255013    0.26261     0.0880463   120 PRO   B CA   
3292 C C    . PRO   B 108 ? 1.22005  1.11433  0.527113 0.203602    0.271411    0.0921334   120 PRO   B C    
3293 O O    . PRO   B 108 ? 1.29373  1.11495  0.59841  0.205298    0.262895    0.118427    120 PRO   B O    
3294 C CB   . PRO   B 108 ? 1.46324  1.35755  0.584733 0.284712    0.290433    0.15418     120 PRO   B CB   
3295 C CG   . PRO   B 108 ? 1.50189  1.41447  0.630635 0.257278    0.339766    0.164238    120 PRO   B CG   
3296 C CD   . PRO   B 108 ? 1.43578  1.44416  0.596376 0.253036    0.325376    0.0957379   120 PRO   B CD   
3297 H HA   . PRO   B 108 ? 1.28678  1.26009  0.499213 0.276763    0.231086    0.0683013   120 PRO   B HA   
3298 H HB2  . PRO   B 108 ? 1.48105  1.30698  0.609719 0.277616    0.294607    0.185222    120 PRO   B HB2  
3299 H HB3  . PRO   B 108 ? 1.50848  1.42847  0.565074 0.325454    0.274267    0.154937    120 PRO   B HB3  
3300 H HG2  . PRO   B 108 ? 1.47221  1.3474   0.659321 0.220592    0.358453    0.177998    120 PRO   B HG2  
3301 H HG3  . PRO   B 108 ? 1.58766  1.48824  0.643818 0.280376    0.361595    0.199712    120 PRO   B HG3  
3302 H HD2  . PRO   B 108 ? 1.38568  1.40186  0.599181 0.221859    0.348419    0.0871407   120 PRO   B HD2  
3303 H HD3  . PRO   B 108 ? 1.475    1.52104  0.568555 0.284326    0.324013    0.0891896   120 PRO   B HD3  
3304 N N    . LYS   B 109 ? 1.16278  1.08995  0.54641  0.162553    0.283664    0.0626934   121 LYS   B N    
3305 C CA   . LYS   B 109 ? 1.07628  0.958531 0.546578 0.114185    0.289024    0.0655704   121 LYS   B CA   
3306 C C    . LYS   B 109 ? 0.996517 0.860915 0.503799 0.10901     0.249276    0.0386397   121 LYS   B C    
3307 O O    . LYS   B 109 ? 0.987145 0.779538 0.508881 0.095207    0.242375    0.0572808   121 LYS   B O    
3308 C CB   . LYS   B 109 ? 1.00467  0.936142 0.540584 0.0827648   0.312554    0.0431725   121 LYS   B CB   
3309 H H    . LYS   B 109 ? 1.13866  1.1187   0.519758 0.167059    0.28629     0.0381751   121 LYS   B H    
3310 H HA   . LYS   B 109 ? 1.12645  0.953649 0.584444 0.10779     0.305858    0.10394     121 LYS   B HA   
3313 N N    . ILE   B 110 ? 0.934141 0.865051 0.456393 0.119643    0.224928    -0.00679025 122 ILE   B N    
3314 C CA   . ILE   B 110 ? 0.87034  0.803163 0.426246 0.117133    0.19496     -0.0332891  122 ILE   B CA   
3315 C C    . ILE   B 110 ? 0.884499 0.853582 0.393293 0.162174    0.173094    -0.0424274  122 ILE   B C    
3316 O O    . ILE   B 110 ? 0.885886 0.925734 0.37938  0.180391    0.166163    -0.0652521  122 ILE   B O    
3317 C CB   . ILE   B 110 ? 0.784528 0.767725 0.412784 0.0877698   0.188419    -0.0750099  122 ILE   B CB   
3318 C CG1  . ILE   B 110 ? 0.759417 0.735293 0.433601 0.0544974   0.21172     -0.0703812  122 ILE   B CG1  
3319 C CG2  . ILE   B 110 ? 0.737305 0.697734 0.400487 0.0760333   0.167418    -0.0871082  122 ILE   B CG2  
3320 C CD1  . ILE   B 110 ? 0.743779 0.647008 0.449486 0.0262595   0.214115    -0.0433236  122 ILE   B CD1  
3321 H H    . ILE   B 110 ? 0.934783 0.913579 0.444861 0.128931    0.229123    -0.0219185  122 ILE   B H    
3322 H HA   . ILE   B 110 ? 0.876123 0.753752 0.439942 0.106467    0.193236    -0.0178696  122 ILE   B HA   
3323 H HB   . ILE   B 110 ? 0.775146 0.8112   0.396989 0.100922    0.182175    -0.0975038  122 ILE   B HB   
3324 H HG12 . ILE   B 110 ? 0.795587 0.784082 0.440943 0.0643579   0.230393    -0.0591136  122 ILE   B HG12 
3325 H HG13 . ILE   B 110 ? 0.71272  0.7212   0.428373 0.0418732   0.206506    -0.0978096  122 ILE   B HG13 
3326 H HG21 . ILE   B 110 ? 0.694275 0.669736 0.403631 0.0536893   0.165697    -0.104723   122 ILE   B HG21 
3327 H HG22 . ILE   B 110 ? 0.760429 0.665279 0.413855 0.0716767   0.168048    -0.0666626  122 ILE   B HG22 
3328 H HG23 . ILE   B 110 ? 0.736828 0.723056 0.385374 0.0964434   0.155323    -0.0977212  122 ILE   B HG23 
3329 H HD11 . ILE   B 110 ? 0.71319  0.607339 0.447327 0.0152189   0.196415    -0.057596   122 ILE   B HD11 
3330 H HD12 . ILE   B 110 ? 0.748419 0.655327 0.485644 0.00814442  0.231135    -0.0371019  122 ILE   B HD12 
3331 H HD13 . ILE   B 110 ? 0.796349 0.65854  0.463497 0.0378627   0.215807    -0.0186624  122 ILE   B HD13 
3332 N N    . PRO   B 111 ? 0.886199 0.810922 0.371654 0.184545    0.159816    -0.0276907  123 PRO   B N    
3333 C CA   . PRO   B 111 ? 0.932244 0.903252 0.390292 0.229822    0.137596    -0.0389966  123 PRO   B CA   
3334 C C    . PRO   B 111 ? 0.855031 0.90776  0.376598 0.219506    0.120107    -0.0858181  123 PRO   B C    
3335 O O    . PRO   B 111 ? 0.806072 0.861957 0.386507 0.178515    0.124922    -0.105541   123 PRO   B O    
3336 C CB   . PRO   B 111 ? 0.96535  0.856735 0.392078 0.255108    0.13261     -0.0130175  123 PRO   B CB   
3337 C CG   . PRO   B 111 ? 0.976954 0.772106 0.410222 0.217605    0.150397    0.0121214   123 PRO   B CG   
3338 C CD   . PRO   B 111 ? 0.920753 0.749955 0.407424 0.170151    0.163622    -0.00307105 123 PRO   B CD   
3339 H HA   . PRO   B 111 ? 0.96634  0.960992 0.384201 0.25277     0.137502    -0.0309661  123 PRO   B HA   
3340 H HB2  . PRO   B 111 ? 0.935421 0.844915 0.388044 0.258774    0.122002    -0.0323756  123 PRO   B HB2  
3341 H HB3  . PRO   B 111 ? 1.02557  0.910148 0.405177 0.290301    0.129035    0.00567226  123 PRO   B HB3  
3342 H HG2  . PRO   B 111 ? 0.973128 0.730963 0.418585 0.21295     0.143381    0.00644126  123 PRO   B HG2  
3343 H HG3  . PRO   B 111 ? 1.0445   0.793751 0.437418 0.229839    0.159771    0.0431006   123 PRO   B HG3  
3344 H HD2  . PRO   B 111 ? 0.870487 0.697415 0.398124 0.147609    0.157404    -0.0208339  123 PRO   B HD2  
3345 H HD3  . PRO   B 111 ? 0.948476 0.740225 0.428672 0.155611    0.17991     0.020287    123 PRO   B HD3  
3346 N N    . SER   B 112 ? 0.887862 1.0076   0.400183 0.257856    0.099145    -0.10083    124 SER   B N    
3347 C CA   . SER   B 112 ? 0.856432 1.04858  0.435442 0.252303    0.084255    -0.137485   124 SER   B CA   
3348 C C    . SER   B 112 ? 0.809846 0.952806 0.419908 0.233144    0.094603    -0.133389   124 SER   B C    
3349 O O    . SER   B 112 ? 0.828079 0.896879 0.397257 0.251315    0.0998705   -0.107386   124 SER   B O    
3350 C CB   . SER   B 112 ? 0.911191 1.17337  0.480817 0.30127     0.0601674   -0.146186   124 SER   B CB   
3351 O OG   . SER   B 112 ? 1.04276  1.25561  0.532524 0.347853    0.0579359   -0.108794   124 SER   B OG   
3352 H H    . SER   B 112 ? 0.940156 1.06213  0.406287 0.288012    0.0942821   -0.086388   124 SER   B H    
3353 H HA   . SER   B 112 ? 0.815918 1.04666  0.429872 0.227676    0.0832265   -0.161152   124 SER   B HA   
3354 H HB2  . SER   B 112 ? 0.89058  1.17388  0.49813  0.303523    0.0579163   -0.155816   124 SER   B HB2  
3355 H HB3  . SER   B 112 ? 0.907701 1.23142  0.491378 0.300093    0.0472514   -0.169046   124 SER   B HB3  
3357 N N    . ASN   B 113 ? 0.722389 0.90414  0.39999  0.197767    0.0965997   -0.160164   125 ASN   B N    
3358 C CA   . ASN   B 113 ? 0.702615 0.86229  0.407388 0.185853    0.104918    -0.160801   125 ASN   B CA   
3359 C C    . ASN   B 113 ? 0.749708 0.802383 0.417549 0.171146    0.114662    -0.136746   125 ASN   B C    
3360 O O    . ASN   B 113 ? 0.68826  0.696865 0.334899 0.184657    0.117632    -0.129398   125 ASN   B O    
3361 C CB   . ASN   B 113 ? 0.721107 0.919052 0.422661 0.229719    0.100157    -0.161747   125 ASN   B CB   
3362 C CG   . ASN   B 113 ? 0.704182 1.01772  0.456073 0.243299    0.0845034   -0.187972   125 ASN   B CG   
3363 O OD1  . ASN   B 113 ? 0.748476 1.09563  0.476258 0.289786    0.0695922   -0.184093   125 ASN   B OD1  
3364 N ND2  . ASN   B 113 ? 0.640059 1.0159   0.466072 0.206228    0.0845393   -0.215133   125 ASN   B ND2  
3365 H H    . ASN   B 113 ? 0.70551  0.926366 0.409652 0.181441    0.0933786   -0.178197   125 ASN   B H    
3366 H HA   . ASN   B 113 ? 0.664121 0.857173 0.416973 0.159579    0.10685     -0.177921   125 ASN   B HA   
3367 H HB2  . ASN   B 113 ? 0.769449 0.927093 0.422286 0.258198    0.0976673   -0.144048   125 ASN   B HB2  
3368 H HB3  . ASN   B 113 ? 0.712376 0.89801  0.428144 0.223262    0.109724    -0.162643   125 ASN   B HB3  
3369 H HD21 . ASN   B 113 ? 0.636044 1.0808   0.501646 0.212504    0.0751031   -0.23213    125 ASN   B HD21 
3370 H HD22 . ASN   B 113 ? 0.62091  0.969038 0.460156 0.175082    0.0930744   -0.216373   125 ASN   B HD22 
3371 N N    . ALA   B 114 ? 0.719332 0.73276  0.382501 0.144203    0.118967    -0.127363   126 ALA   B N    
3372 C CA   . ALA   B 114 ? 0.746105 0.665386 0.385884 0.128335    0.122838    -0.106355   126 ALA   B CA   
3373 C C    . ALA   B 114 ? 0.719305 0.621833 0.396867 0.0942666   0.121522    -0.117396   126 ALA   B C    
3374 O O    . ALA   B 114 ? 0.699077 0.64976  0.426696 0.0703628   0.123137    -0.134098   126 ALA   B O    
3375 C CB   . ALA   B 114 ? 0.801937 0.696962 0.432735 0.113773    0.131404    -0.0889376  126 ALA   B CB   
3376 H H    . ALA   B 114 ? 0.710361 0.758478 0.388523 0.13545     0.119132    -0.135965   126 ALA   B H    
3377 H HA   . ALA   B 114 ? 0.795904 0.677223 0.399948 0.151719    0.12054     -0.095726   126 ALA   B HA   
3378 H HB1  . ALA   B 114 ? 0.824928 0.727992 0.42303  0.137831    0.133123    -0.0785315  126 ALA   B HB1  
3379 H HB2  . ALA   B 114 ? 0.755319 0.686255 0.419928 0.094149    0.134664    -0.101577   126 ALA   B HB2  
3380 H HB3  . ALA   B 114 ? 0.810894 0.646515 0.435398 0.100875    0.132595    -0.0752358  126 ALA   B HB3  
3381 N N    . THR   B 115 ? 0.730127 0.558149 0.378192 0.0947481   0.116239    -0.108637   127 THR   B N    
3382 C CA   . THR   B 115 ? 0.714304 0.510356 0.383221 0.0634574   0.109601    -0.113123   127 THR   B CA   
3383 C C    . THR   B 115 ? 0.716764 0.461115 0.397493 0.0366823   0.103322    -0.100532   127 THR   B C    
3384 O O    . THR   B 115 ? 0.736767 0.439768 0.390629 0.045714    0.105061    -0.0847253  127 THR   B O    
3385 C CB   . THR   B 115 ? 0.766025 0.51587  0.389145 0.08282     0.104665    -0.115765   127 THR   B CB   
3386 O OG1  . THR   B 115 ? 0.74796  0.566372 0.378818 0.10579     0.11777     -0.125341   127 THR   B OG1  
3387 C CG2  . THR   B 115 ? 0.770223 0.477879 0.393486 0.0581159   0.0924355   -0.118852   127 THR   B CG2  
3388 H H    . THR   B 115 ? 0.778219 0.573048 0.389874 0.11696     0.114673    -0.100788   127 THR   B H    
3389 H HA   . THR   B 115 ? 0.673183 0.513739 0.378301 0.0498111   0.112965    -0.122725   127 THR   B HA   
3390 H HB   . THR   B 115 ? 0.811751 0.514667 0.398682 0.0992978   0.100637    -0.109228   127 THR   B HB   
3392 H HG21 . THR   B 115 ? 0.810575 0.485865 0.392911 0.0747699   0.0899273   -0.121899   127 THR   B HG21 
3393 H HG22 . THR   B 115 ? 0.732776 0.480646 0.388071 0.0448403   0.0975781   -0.122622   127 THR   B HG22 
3394 H HG23 . THR   B 115 ? 0.777217 0.44965  0.409034 0.0403081   0.0814042   -0.114026   127 THR   B HG23 
3395 N N    . LEU   B 116 ? 0.693175 0.441055 0.420008 0.0042758   0.0970356   -0.105253   128 LEU   B N    
3396 C CA   . LEU   B 116 ? 0.687696 0.406504 0.448029 -0.0230458  0.092668    -0.0949419  128 LEU   B CA   
3397 C C    . LEU   B 116 ? 0.690801 0.366395 0.463366 -0.0427311  0.068123    -0.0992122  128 LEU   B C    
3398 O O    . LEU   B 116 ? 0.63196  0.319725 0.401572 -0.0414657  0.0612562   -0.108657   128 LEU   B O    
3399 C CB   . LEU   B 116 ? 0.644703 0.42068  0.464269 -0.0410612  0.107439    -0.0976707  128 LEU   B CB   
3400 C CG   . LEU   B 116 ? 0.618823 0.460216 0.433041 -0.0235181  0.126924    -0.105336   128 LEU   B CG   
3401 C CD1  . LEU   B 116 ? 0.618089 0.500899 0.478792 -0.0382643  0.14309     -0.110109   128 LEU   B CD1  
3402 C CD2  . LEU   B 116 ? 0.663984 0.494717 0.420805 0.00511003  0.134482    -0.0911945  128 LEU   B CD2  
3403 H H    . LEU   B 116 ? 0.664157 0.434877 0.406164 -0.00050734 0.096053    -0.113981   128 LEU   B H    
3404 H HA   . LEU   B 116 ? 0.727296 0.411129 0.464189 -0.0168594  0.0944025   -0.0830318  128 LEU   B HA   
3405 H HB2  . LEU   B 116 ? 0.614797 0.403173 0.466297 -0.0539299  0.100378    -0.106742   128 LEU   B HB2  
3406 H HB3  . LEU   B 116 ? 0.657635 0.413645 0.493478 -0.0536936  0.109844    -0.0864336  128 LEU   B HB3  
3407 H HG   . LEU   B 116 ? 0.601071 0.471131 0.420141 -0.0186397  0.123684    -0.119528   128 LEU   B HG   
3408 H HD11 . LEU   B 116 ? 0.585848 0.47177  0.487759 -0.0548215  0.137162    -0.118062   128 LEU   B HD11 
3409 H HD12 . LEU   B 116 ? 0.602257 0.526914 0.455563 -0.0262649  0.150275    -0.121915   128 LEU   B HD12 
3410 H HD13 . LEU   B 116 ? 0.636652 0.500709 0.493253 -0.0417099  0.152391    -0.0937933  128 LEU   B HD13 
3411 H HD21 . LEU   B 116 ? 0.666085 0.505771 0.400691 0.0229068   0.128982    -0.0979742  128 LEU   B HD21 
3412 H HD22 . LEU   B 116 ? 0.700459 0.480737 0.442318 0.00191578  0.13278     -0.0750202  128 LEU   B HD22 
3413 H HD23 . LEU   B 116 ? 0.664564 0.528928 0.42033  0.0109884   0.146446    -0.0909445  128 LEU   B HD23 
3414 N N    . PHE   B 117 ? 0.726781 0.354604 0.517339 -0.0624599  0.0548402   -0.0903753  129 PHE   B N    
3415 C CA   . PHE   B 117 ? 0.709615 0.304833 0.525526 -0.0842269  0.0242556   -0.095866   129 PHE   B CA   
3416 C C    . PHE   B 117 ? 0.713234 0.335949 0.614765 -0.114129   0.0256872   -0.0891     129 PHE   B C    
3417 O O    . PHE   B 117 ? 0.770972 0.396726 0.695107 -0.122626   0.0456625   -0.0749511  129 PHE   B O    
3418 C CB   . PHE   B 117 ? 0.768432 0.280458 0.537029 -0.0813002  0.00112909  -0.0971828  129 PHE   B CB   
3419 C CG   . PHE   B 117 ? 0.846612 0.321362 0.636429 -0.103108   -0.0403644  -0.107312   129 PHE   B CG   
3420 C CD1  . PHE   B 117 ? 0.8806   0.342056 0.627666 -0.0916742  -0.0639369  -0.120204   129 PHE   B CD1  
3421 C CD2  . PHE   B 117 ? 0.917217 0.372919 0.77086  -0.134728   -0.0568536  -0.102711   129 PHE   B CD2  
3422 C CE1  . PHE   B 117 ? 0.90428  0.331809 0.659802 -0.106328   -0.108332   -0.130255   129 PHE   B CE1  
3423 C CE2  . PHE   B 117 ? 0.956439 0.385932 0.83584  -0.153489   -0.102739   -0.115595   129 PHE   B CE2  
3424 C CZ   . PHE   B 117 ? 0.97204  0.38687  0.797215 -0.137021   -0.131073   -0.130201   129 PHE   B CZ   
3425 H H    . PHE   B 117 ? 0.73795  0.354288 0.52668  -0.0624219  0.064388    -0.0798301  129 PHE   B H    
3426 H HA   . PHE   B 117 ? 0.7033   0.310631 0.510983 -0.0796793  0.0173074   -0.103442   129 PHE   B HA   
3427 H HB2  . PHE   B 117 ? 0.805078 0.301096 0.518186 -0.0581074  0.00282652  -0.10286    129 PHE   B HB2  
3428 H HB3  . PHE   B 117 ? 0.802656 0.299111 0.580799 -0.0865967  0.0106805   -0.0864968  129 PHE   B HB3  
3429 H HD1  . PHE   B 117 ? 0.864469 0.34099  0.573539 -0.0723135  -0.0494653  -0.121357   129 PHE   B HD1  
3430 H HD2  . PHE   B 117 ? 0.900578 0.364435 0.782893 -0.143692   -0.0369434  -0.0900181  129 PHE   B HD2  
3431 H HE1  . PHE   B 117 ? 0.940268 0.35774  0.656345 -0.095181   -0.122865   -0.136275   129 PHE   B HE1  
3432 H HE2  . PHE   B 117 ? 0.963756 0.387184 0.897977 -0.177152   -0.114655   -0.113337   129 PHE   B HE2  
3433 H HZ   . PHE   B 117 ? 0.986312 0.383015 0.8226   -0.146888   -0.166173   -0.139234   129 PHE   B HZ   
3434 N N    . PHE   B 118 ? 0.709917 0.345753 0.656474 -0.128245   0.00346744  -0.0963327  130 PHE   B N    
3435 C CA   . PHE   B 118 ? 0.720178 0.383172 0.758747 -0.15407    -0.00128544 -0.0923503  130 PHE   B CA   
3436 C C    . PHE   B 118 ? 0.747147 0.379794 0.809446 -0.1674     -0.0495693  -0.0993615  130 PHE   B C    
3437 O O    . PHE   B 118 ? 0.806879 0.420352 0.82235  -0.153791   -0.0724317  -0.106769   130 PHE   B O    
3438 C CB   . PHE   B 118 ? 0.640957 0.372169 0.73471  -0.152522   0.0195916   -0.0968604  130 PHE   B CB   
3439 C CG   . PHE   B 118 ? 0.640647 0.415494 0.723824 -0.140696   0.062903    -0.0958923  130 PHE   B CG   
3440 C CD1  . PHE   B 118 ? 0.627356 0.416535 0.656463 -0.119703   0.0746781   -0.104845   130 PHE   B CD1  
3441 C CD2  . PHE   B 118 ? 0.630386 0.437252 0.760734 -0.150271   0.0911062   -0.086652   130 PHE   B CD2  
3442 C CE1  . PHE   B 118 ? 0.619971 0.450813 0.636015 -0.107061   0.105681    -0.107841   130 PHE   B CE1  
3443 C CE2  . PHE   B 118 ? 0.637853 0.481328 0.742078 -0.134987   0.127154    -0.0866217  130 PHE   B CE2  
3444 C CZ   . PHE   B 118 ? 0.634612 0.490243 0.681603 -0.112994   0.130533    -0.0993556  130 PHE   B CZ   
3445 H H    . PHE   B 118 ? 0.713194 0.342381 0.633554 -0.119831   -0.00840863 -0.102604   130 PHE   B H    
3446 H HA   . PHE   B 118 ? 0.724784 0.382924 0.780821 -0.163658   0.0115273   -0.0828687  130 PHE   B HA   
3447 H HB2  . PHE   B 118 ? 0.642498 0.37261  0.718299 -0.144168   0.00871987  -0.103294   130 PHE   B HB2  
3448 H HB3  . PHE   B 118 ? 0.643147 0.391166 0.800381 -0.166681   0.0133558   -0.0954215  130 PHE   B HB3  
3449 H HD1  . PHE   B 118 ? 0.63327  0.404449 0.632596 -0.113446   0.0609581   -0.108636   130 PHE   B HD1  
3450 H HD2  . PHE   B 118 ? 0.644771 0.448343 0.822572 -0.166762   0.0854651   -0.0796994  130 PHE   B HD2  
3451 H HE1  . PHE   B 118 ? 0.612561 0.45817  0.599457 -0.0939441  0.109935    -0.116074   130 PHE   B HE1  
3452 H HE2  . PHE   B 118 ? 0.643367 0.507719 0.771799 -0.139512   0.149535    -0.0783347  130 PHE   B HE2  
3453 H HZ   . PHE   B 118 ? 0.628679 0.512333 0.65786  -0.101551   0.150377    -0.102157   130 PHE   B HZ   
3454 N N    . GLU   B 119 ? 0.725202 0.363374 0.867805 -0.193881   -0.0630244  -0.0954627  131 GLU   B N    
3455 C CA   . GLU   B 119 ? 0.750843 0.393151 0.954086 -0.207678   -0.109188   -0.103019   131 GLU   B CA   
3456 C C    . GLU   B 119 ? 0.729508 0.448573 1.03623  -0.213546   -0.0890443  -0.0986961  131 GLU   B C    
3457 O O    . GLU   B 119 ? 0.763686 0.521656 1.12261  -0.22398    -0.0485106  -0.0892878  131 GLU   B O    
3458 C CB   . GLU   B 119 ? 0.810084 0.410681 1.04547  -0.234839   -0.140322   -0.105499   131 GLU   B CB   
3459 C CG   . GLU   B 119 ? 0.880908 0.488981 1.18008  -0.248157   -0.198716   -0.117361   131 GLU   B CG   
3460 C CD   . GLU   B 119 ? 0.986667 0.545839 1.31246  -0.277196   -0.238555   -0.127318   131 GLU   B CD   
3461 O OE1  . GLU   B 119 ? 0.973955 0.462619 1.22599  -0.272425   -0.286487   -0.146905   131 GLU   B OE1  
3462 O OE2  . GLU   B 119 ? 1.08331  0.680388 1.5137   -0.306502   -0.215963   -0.114965   131 GLU   B OE2  
3463 H H    . GLU   B 119 ? 0.740643 0.382412 0.903834 -0.203498   -0.0428979  -0.086598   131 GLU   B H    
3464 H HA   . GLU   B 119 ? 0.768756 0.390684 0.923659 -0.193669   -0.131333   -0.109621   131 GLU   B HA   
3465 H HB2  . GLU   B 119 ? 0.862706 0.409775 1.02716  -0.227627   -0.149142   -0.11054    131 GLU   B HB2  
3466 H HB3  . GLU   B 119 ? 0.809993 0.431408 1.09586  -0.25013    -0.113657   -0.0945321  131 GLU   B HB3  
3467 H HG2  . GLU   B 119 ? 0.838334 0.501196 1.21861  -0.255136   -0.188966   -0.111956   131 GLU   B HG2  
3468 H HG3  . GLU   B 119 ? 0.888207 0.478317 1.13238  -0.230046   -0.222006   -0.124592   131 GLU   B HG3  
3469 N N    . ILE   B 120 ? 0.755984 0.494835 1.08248  -0.201486   -0.110558   -0.104035   132 ILE   B N    
3470 C CA   . ILE   B 120 ? 0.633659 0.438939 1.05492  -0.199931   -0.0911203  -0.103715   132 ILE   B CA   
3471 C C    . ILE   B 120 ? 0.6453   0.464345 1.14289  -0.203574   -0.140896   -0.106302   132 ILE   B C    
3472 O O    . ILE   B 120 ? 0.647491 0.427536 1.09448  -0.191713   -0.185252   -0.107919   132 ILE   B O    
3473 C CB   . ILE   B 120 ? 0.60821  0.427966 0.995287 -0.177151   -0.0645865  -0.10771    132 ILE   B CB   
3474 C CG1  . ILE   B 120 ? 0.636143 0.448594 0.947001 -0.16966    -0.025032   -0.108518   132 ILE   B CG1  
3475 C CG2  . ILE   B 120 ? 0.571118 0.452789 1.05824  -0.172929   -0.0436074  -0.112965   132 ILE   B CG2  
3476 C CD1  . ILE   B 120 ? 0.61836  0.434435 0.889288 -0.151813   -0.0111745  -0.115395   132 ILE   B CD1  
3477 H H    . ILE   B 120 ? 0.750397 0.457961 1.02796  -0.19205    -0.136834   -0.107346   132 ILE   B H    
3478 H HA   . ILE   B 120 ? 0.635428 0.46952  1.09984  -0.210373   -0.0629475  -0.0998959  132 ILE   B HA   
3479 H HB   . ILE   B 120 ? 0.631243 0.423965 0.983467 -0.168245   -0.0901156  -0.107268   132 ILE   B HB   
3480 H HG12 . ILE   B 120 ? 0.612009 0.454283 0.952409 -0.174146   0.00350148  -0.107772   132 ILE   B HG12 
3481 H HG13 . ILE   B 120 ? 0.654129 0.429685 0.911759 -0.171438   -0.0359818  -0.105338   132 ILE   B HG13 
3482 H HG21 . ILE   B 120 ? 0.554188 0.443772 1.02023  -0.16149    -0.0207751  -0.118896   132 ILE   B HG21 
3483 H HG22 . ILE   B 120 ? 0.563679 0.474979 1.09677  -0.183188   -0.0236606  -0.111295   132 ILE   B HG22 
3484 H HG23 . ILE   B 120 ? 0.579717 0.463087 1.10644  -0.169991   -0.0728549  -0.112546   132 ILE   B HG23 
3485 H HD11 . ILE   B 120 ? 0.63527  0.42574  0.886661 -0.147502   -0.0359686  -0.11228    132 ILE   B HD11 
3486 H HD12 . ILE   B 120 ? 0.617132 0.427038 0.835783 -0.146813   0.00599077  -0.116451   132 ILE   B HD12 
3487 H HD13 . ILE   B 120 ? 0.59374  0.443472 0.911886 -0.149215   0.00540892  -0.121972   132 ILE   B HD13 
3488 N N    . GLU   B 121 ? 0.70686  0.587224 1.32661  -0.216714   -0.130356   -0.105285   133 GLU   B N    
3489 C CA   . GLU   B 121 ? 0.702525 0.619926 1.42149  -0.213365   -0.170831   -0.108313   133 GLU   B CA   
3490 C C    . GLU   B 121 ? 0.661487 0.632102 1.44035  -0.191295   -0.136542   -0.110856   133 GLU   B C    
3491 O O    . GLU   B 121 ? 0.694879 0.714901 1.5233   -0.193927   -0.0825103  -0.112397   133 GLU   B O    
3492 C CB   . GLU   B 121 ? 0.715543 0.668627 1.54519  -0.244654   -0.188016   -0.107761   133 GLU   B CB   
3493 C CG   . GLU   B 121 ? 0.726432 0.715462 1.65604  -0.240816   -0.248567   -0.113451   133 GLU   B CG   
3494 C CD   . GLU   B 121 ? 0.709145 0.743601 1.76823  -0.275553   -0.271916   -0.115699   133 GLU   B CD   
3495 O OE1  . GLU   B 121 ? 0.737496 0.768272 1.811    -0.306908   -0.23908    -0.109628   133 GLU   B OE1  
3496 O OE2  . GLU   B 121 ? 0.687511 0.75997  1.83487  -0.270513   -0.32499    -0.122048   133 GLU   B OE2  
3497 H H    . GLU   B 121 ? 0.66878  0.571131 1.31197  -0.226421   -0.0956345  -0.101453   133 GLU   B H    
3498 H HA   . GLU   B 121 ? 0.731363 0.612495 1.40423  -0.203937   -0.211788   -0.109668   133 GLU   B HA   
3499 H HB2  . GLU   B 121 ? 0.745636 0.656786 1.53053  -0.259782   -0.202882   -0.108259   133 GLU   B HB2  
3500 H HB3  . GLU   B 121 ? 0.689229 0.684519 1.57241  -0.252331   -0.144228   -0.103061   133 GLU   B HB3  
3501 H HG2  . GLU   B 121 ? 0.692271 0.719762 1.66746  -0.222874   -0.232573   -0.112785   133 GLU   B HG2  
3502 H HG3  . GLU   B 121 ? 0.75261  0.697248 1.61767  -0.230214   -0.2919     -0.116703   133 GLU   B HG3  
3503 N N    . LEU   B 122 ? 0.665742 0.61955  1.43241  -0.166906   -0.167675   -0.111161   134 LEU   B N    
3504 C CA   . LEU   B 122 ? 0.615857 0.609819 1.45245  -0.143581   -0.146892   -0.116183   134 LEU   B CA   
3505 C C    . LEU   B 122 ? 0.6582   0.718312 1.64033  -0.142289   -0.170241   -0.117922   134 LEU   B C    
3506 O O    . LEU   B 122 ? 0.699397 0.750725 1.70821  -0.133724   -0.232745   -0.113009   134 LEU   B O    
3507 C CB   . LEU   B 122 ? 0.614877 0.553479 1.38015  -0.119143   -0.170172   -0.110112   134 LEU   B CB   
3508 C CG   . LEU   B 122 ? 0.565666 0.52287  1.38797  -0.0932172  -0.148571   -0.116714   134 LEU   B CG   
3509 C CD1  . LEU   B 122 ? 0.497863 0.49668  1.3441   -0.095483   -0.0823725  -0.135798   134 LEU   B CD1  
3510 C CD2  . LEU   B 122 ? 0.608481 0.496433 1.34438  -0.0775085  -0.162476   -0.104809   134 LEU   B CD2  
3511 H H    . LEU   B 122 ? 0.69179  0.604108 1.40215  -0.163119   -0.202195   -0.107678   134 LEU   B H    
3512 H HA   . LEU   B 122 ? 0.595713 0.609328 1.43087  -0.143907   -0.100372   -0.122391   134 LEU   B HA   
3513 H HB2  . LEU   B 122 ? 0.612421 0.515915 1.29291  -0.122861   -0.155033   -0.108658   134 LEU   B HB2  
3514 H HB3  . LEU   B 122 ? 0.645806 0.56517  1.4058   -0.115679   -0.216529   -0.102436   134 LEU   B HB3  
3515 H HG   . LEU   B 122 ? 0.576972 0.563237 1.47893  -0.0837085  -0.171146   -0.115974   134 LEU   B HG   
3516 H HD11 . LEU   B 122 ? 0.493286 0.541459 1.41291  -0.0994289  -0.0713593  -0.140169   134 LEU   B HD11 
3517 H HD12 . LEU   B 122 ? 0.508292 0.500065 1.36228  -0.0793197  -0.0696538  -0.143562   134 LEU   B HD12 
3518 H HD13 . LEU   B 122 ? 0.497549 0.48044  1.27723  -0.10783    -0.0638846  -0.136203   134 LEU   B HD13 
3519 H HD21 . LEU   B 122 ? 0.640347 0.49766  1.33406  -0.0775328  -0.199802   -0.0915239  134 LEU   B HD21 
3520 H HD22 . LEU   B 122 ? 0.592614 0.464471 1.27144  -0.084446   -0.132863   -0.109136   134 LEU   B HD22 
3521 H HD23 . LEU   B 122 ? 0.614725 0.504545 1.39505  -0.0597924  -0.163145   -0.105734   134 LEU   B HD23 
3522 N N    . LEU   B 123 ? 0.620501 0.751333 1.69592  -0.148528   -0.119652   -0.124362   135 LEU   B N    
3523 C CA   . LEU   B 123 ? 0.5902   0.800847 1.82185  -0.149294   -0.1311     -0.125903   135 LEU   B CA   
3524 C C    . LEU   B 123 ? 0.595629 0.829265 1.89009  -0.108714   -0.137785   -0.133702   135 LEU   B C    
3525 O O    . LEU   B 123 ? 0.620291 0.874687 1.99235  -0.0952786  -0.192404   -0.130501   135 LEU   B O    
3526 C CB   . LEU   B 123 ? 0.578897 0.859493 1.88688  -0.169707   -0.0663479  -0.125527   135 LEU   B CB   
3527 C CG   . LEU   B 123 ? 0.624979 0.877407 1.87277  -0.208019   -0.0469119  -0.113475   135 LEU   B CG   
3528 C CD1  . LEU   B 123 ? 0.631223 0.951976 1.95003  -0.223339   0.026718    -0.105669   135 LEU   B CD1  
3529 C CD2  . LEU   B 123 ? 0.651797 0.88048  1.92391  -0.237063   -0.115066   -0.108212   135 LEU   B CD2  
3530 H H    . LEU   B 123 ? 0.598557 0.731135 1.63996  -0.151095   -0.07623    -0.127531   135 LEU   B H    
3531 H HA   . LEU   B 123 ? 0.620774 0.824305 1.87052  -0.161395   -0.179477   -0.121427   135 LEU   B HA   
3532 H HB2  . LEU   B 123 ? 0.569893 0.863625 1.86551  -0.152544   -0.0222426  -0.133191   135 LEU   B HB2  
3533 H HB3  . LEU   B 123 ? 0.58476  0.922432 2.00485  -0.172233   -0.0765235  -0.125346   135 LEU   B HB3  
3534 H HG   . LEU   B 123 ? 0.619102 0.819234 1.75876  -0.202677   -0.0378965  -0.114123   135 LEU   B HG   
3535 H HD11 . LEU   B 123 ? 0.612016 0.960984 1.93823  -0.200419   0.0630947   -0.114196   135 LEU   B HD11 
3536 H HD12 . LEU   B 123 ? 0.635496 0.924137 1.88695  -0.239131   0.0472299   -0.0965934  135 LEU   B HD12 
3537 H HD13 . LEU   B 123 ? 0.631405 0.999195 2.05485  -0.239102   0.017169    -0.100896   135 LEU   B HD13 
3538 H HD21 . LEU   B 123 ? 0.66927  0.845497 1.86845  -0.226565   -0.155732   -0.1114     135 LEU   B HD21 
3539 H HD22 . LEU   B 123 ? 0.654851 0.936122 2.03655  -0.240068   -0.134167   -0.109796   135 LEU   B HD22 
3540 H HD23 . LEU   B 123 ? 0.664029 0.876868 1.91514  -0.262136   -0.0993311  -0.10084    135 LEU   B HD23 
3541 N N    . ASP   B 124 ? 0.583097 0.810181 1.84399  -0.0873063  -0.0851852  -0.145882   136 ASP   B N    
3542 C CA   . ASP   B 124 ? 0.619412 0.856693 1.93805  -0.0470325  -0.0852581  -0.156952   136 ASP   B CA   
3543 C C    . ASP   B 124 ? 0.612954 0.802088 1.84165  -0.0325316  -0.0423811  -0.172485   136 ASP   B C    
3544 O O    . ASP   B 124 ? 0.555974 0.732607 1.70354  -0.0511288  -0.00362308 -0.17764    136 ASP   B O    
3545 C CB   . ASP   B 124 ? 0.65319  0.990739 2.12902  -0.0336291  -0.058121   -0.167581   136 ASP   B CB   
3546 C CG   . ASP   B 124 ? 0.674349 1.03012  2.24492  0.0113205   -0.0839716  -0.174554   136 ASP   B CG   
3547 O OD1  . ASP   B 124 ? 0.756655 1.08308  2.30352  0.0415543   -0.0553792  -0.191464   136 ASP   B OD1  
3548 O OD2  . ASP   B 124 ? 0.680887 1.07634  2.34875  0.0170801   -0.137027   -0.164238   136 ASP   B OD2  
3549 H H    . ASP   B 124 ? 0.576014 0.789853 1.77681  -0.0971875  -0.0501746  -0.148824   136 ASP   B H    
3550 H HA   . ASP   B 124 ? 0.645605 0.853461 1.96064  -0.0363969  -0.134292   -0.147339   136 ASP   B HA   
3551 H HB2  . ASP   B 124 ? 0.636774 1.01162  2.16627  -0.0543389  -0.073582   -0.158647   136 ASP   B HB2  
3552 H HB3  . ASP   B 124 ? 0.627923 0.988137 2.09793  -0.0333094  -0.00403277 -0.179204   136 ASP   B HB3  
3553 N N    . PHE   B 125 ? 0.655599 0.813929 1.90039  0.00068327  -0.054529   -0.179581   137 PHE   B N    
3554 C CA   . PHE   B 125 ? 0.67596  0.795925 1.86707  0.0147624   -0.0152249  -0.2019     137 PHE   B CA   
3555 C C    . PHE   B 125 ? 0.740936 0.858608 2.01691  0.056805    -0.0209366  -0.215361   137 PHE   B C    
3556 O O    . PHE   B 125 ? 0.831267 0.928378 2.14608  0.0741808   -0.0731274  -0.194529   137 PHE   B O    
3557 C CB   . PHE   B 125 ? 0.686602 0.719943 1.75011  -0.0004364  -0.0333521  -0.188555   137 PHE   B CB   
3558 C CG   . PHE   B 125 ? 0.70983  0.680068 1.75336  0.0112973   -0.0917052  -0.160022   137 PHE   B CG   
3559 C CD1  . PHE   B 125 ? 0.710976 0.669642 1.72151  -0.0020433  -0.140674   -0.132846   137 PHE   B CD1  
3560 C CD2  . PHE   B 125 ? 0.719145 0.634515 1.76885  0.036916    -0.0976853  -0.160179   137 PHE   B CD2  
3561 C CE1  . PHE   B 125 ? 0.759354 0.657985 1.7329   0.0132531   -0.192938   -0.105192   137 PHE   B CE1  
3562 C CE2  . PHE   B 125 ? 0.766702 0.619033 1.78765  0.0501779   -0.14737    -0.12688    137 PHE   B CE2  
3563 C CZ   . PHE   B 125 ? 0.814371 0.661122 1.79289  0.040133    -0.194449   -0.0987787  137 PHE   B CZ   
3564 H H    . PHE   B 125 ? 0.674255 0.832949 1.96614  0.0150789   -0.0907691  -0.170623   137 PHE   B H    
3565 H HA   . PHE   B 125 ? 0.658581 0.812101 1.84514  0.00815356  0.0274609   -0.217627   137 PHE   B HA   
3566 H HB2  . PHE   B 125 ? 0.685865 0.700202 1.72248  0.00457723  -0.00646429 -0.206297   137 PHE   B HB2  
3567 H HB3  . PHE   B 125 ? 0.6632   0.699704 1.67681  -0.0233286  -0.0301931  -0.181134   137 PHE   B HB3  
3568 H HD1  . PHE   B 125 ? 0.688399 0.67622  1.69573  -0.0210414  -0.138327   -0.133348   137 PHE   B HD1  
3569 H HD2  . PHE   B 125 ? 0.725475 0.643318 1.79719  0.0463692   -0.0674485  -0.182917   137 PHE   B HD2  
3570 H HE1  . PHE   B 125 ? 0.779063 0.670027 1.72369  0.0064276   -0.227965   -0.0904437  137 PHE   B HE1  
3571 H HE2  . PHE   B 125 ? 0.813579 0.62329  1.84018  0.0671358   -0.149008   -0.123756   137 PHE   B HE2  
3572 H HZ   . PHE   B 125 ? 0.849735 0.653    1.79881  0.052023    -0.228211   -0.0753122  137 PHE   B HZ   
3573 N N    . LYS   B 126 ? 0.736693 0.870451 2.03297  0.0759662   0.0302656   -0.25116    138 LYS   B N    
3574 C CA   . LYS   B 126 ? 0.731777 0.859139 2.10927  0.120392    0.0329255   -0.272189   138 LYS   B CA   
3575 C C    . LYS   B 126 ? 0.720996 0.785472 2.03246  0.127038    0.0632631   -0.305782   138 LYS   B C    
3576 O O    . LYS   B 126 ? 0.641663 0.697117 1.86513  0.100714    0.0897101   -0.318073   138 LYS   B O    
3577 C CB   . LYS   B 126 ? 0.695101 0.924168 2.20384  0.146761    0.0630502   -0.289999   138 LYS   B CB   
3578 H H    . LYS   B 126 ? 0.710558 0.857392 1.96514  0.0629074   0.0638697   -0.264352   138 LYS   B H    
3579 H HA   . LYS   B 126 ? 0.751432 0.843253 2.14285  0.13078     -0.009458   -0.251349   138 LYS   B HA   
3582 N N    . GLY   B 127 ? 0.805952 0.823484 2.16429  0.163303    0.0549212   -0.321465   139 GLY   B N    
3583 C CA   . GLY   B 127 ? 0.857582 0.810444 2.17026  0.169095    0.0790402   -0.359512   139 GLY   B CA   
3584 C C    . GLY   B 127 ? 0.862134 0.877424 2.1936   0.185822    0.137257    -0.413297   139 GLY   B C    
3585 O O    . GLY   B 127 ? 0.830941 0.926425 2.24794  0.211281    0.158401    -0.420566   139 GLY   B O    
3586 H H    . GLY   B 127 ? 0.818474 0.842384 2.24099  0.185157    0.0315023   -0.308998   139 GLY   B H    
3587 H HA2  . GLY   B 127 ? 0.843993 0.760606 2.07971  0.140449    0.0746668   -0.351032   139 GLY   B HA2  
3588 H HA3  . GLY   B 127 ? 0.901616 0.804753 2.24756  0.191787    0.061106    -0.358911   139 GLY   B HA3  
3589 N N    . GLU   B 128 ? 0.859857 0.845179 2.10958  0.170622    0.162653    -0.449167   140 GLU   B N    
3590 C CA   . GLU   B 128 ? 0.91731  0.932807 2.17403  0.198363    0.210818    -0.510636   140 GLU   B CA   
3591 C C    . GLU   B 128 ? 0.968569 0.945541 2.31612  0.24864     0.207113    -0.539813   140 GLU   B C    
3592 O O    . GLU   B 128 ? 0.983466 0.89364  2.36703  0.254102    0.163681    -0.508473   140 GLU   B O    
3593 C CB   . GLU   B 128 ? 0.919507 0.905782 2.06686  0.170071    0.223336    -0.540896   140 GLU   B CB   
3594 O OXT  . GLU   B 128 ? 0.996154 1.01123  2.37622  0.285947    0.248568    -0.590751   140 GLU   B OXT  
3595 H H    . GLU   B 128 ? 0.857129 0.805063 2.04563  0.1441      0.148922    -0.436642   140 GLU   B H    
3596 H HA   . GLU   B 128 ? 0.885202 0.973763 2.16148  0.203472    0.237042    -0.509067   140 GLU   B HA   
3599 C CAK  . A1IN0 C .   ? 0.573922 0.826069 0.551381 -0.0792454  0.125482    -0.111236   201 A1IN0 A CAK  
3600 C CAL  . A1IN0 C .   ? 0.599326 0.852687 0.600216 -0.0624935  0.142756    -0.13142    201 A1IN0 A CAL  
3601 C CAM  . A1IN0 C .   ? 0.616694 0.848625 0.649449 -0.0485812  0.129388    -0.127506   201 A1IN0 A CAM  
3602 C CAN  . A1IN0 C .   ? 0.643278 0.83501  0.656269 -0.046956   0.11525     -0.133901   201 A1IN0 A CAN  
3603 C CAO  . A1IN0 C .   ? 0.596285 0.786994 0.592885 -0.0616229  0.0959968   -0.118168   201 A1IN0 A CAO  
3604 C CAJ  . A1IN0 C .   ? 0.620589 0.838022 0.588332 -0.0750281  0.10426     -0.115662   201 A1IN0 A CAJ  
3605 C CAI  . A1IN0 C .   ? 0.649126 0.862149 0.601479 -0.084947   0.0816086   -0.0910966  201 A1IN0 A CAI  
3606 C CAB  . A1IN0 C .   ? 0.614106 0.806932 0.559375 -0.0791199  0.0633536   -0.0982242  201 A1IN0 A CAB  
3607 O OAA  . A1IN0 C .   ? 0.588712 0.776449 0.531679 -0.0747709  0.0704382   -0.122595   201 A1IN0 A OAA  
3608 N N    . A1IN0 C .   ? 0.57284  0.750339 0.516983 -0.0779274  0.0398256   -0.080101   201 A1IN0 A N    
3609 C CAH  . A1IN0 C .   ? 0.619571 0.79019  0.56279  -0.0863876  0.0316693   -0.0493443  201 A1IN0 A CAH  
3610 C CAG  . A1IN0 C .   ? 0.660345 0.797625 0.621375 -0.0807546  0.0109182   -0.0395875  201 A1IN0 A CAG  
3611 C CAF  . A1IN0 C .   ? 0.664193 0.792854 0.614921 -0.0672448  -0.00654526 -0.0479755  201 A1IN0 A CAF  
3612 C CB   . A1IN0 C .   ? 0.626628 0.764971 0.586984 -0.0611552  0.00332704  -0.0774548  201 A1IN0 A CB   
3613 C CA   . A1IN0 C .   ? 0.596776 0.764012 0.539962 -0.068798   0.0231136   -0.0916524  201 A1IN0 A CA   
3614 C C    . A1IN0 C .   ? 0.663937 0.852241 0.579379 -0.0707922  0.0141519   -0.0880018  201 A1IN0 A C    
3615 O O    . A1IN0 C .   ? 0.590381 0.785374 0.5058   -0.0634694  -0.00033208 -0.0981525  201 A1IN0 A O    
3616 O OBA  . A1IN0 C .   ? 0.629552 0.834275 0.519444 -0.0809566  0.0231458   -0.0724841  201 A1IN0 A OBA  
3617 C CAZ  . A1IN0 C .   ? 0.779292 0.997601 0.632995 -0.0817917  0.00936496  -0.0553633  201 A1IN0 A CAZ  
3618 C CAY  . A1IN0 C .   ? 0.834372 1.08137  0.654254 -0.0940409  0.0279436   -0.056295   201 A1IN0 A CAY  
3619 C CAX  . A1IN0 C .   ? 0.955287 1.20281  0.750636 -0.105378   0.0359898   -0.0249775  201 A1IN0 A CAX  
3620 C CAW  . A1IN0 C .   ? 0.939484 1.21771  0.698864 -0.118127   0.0581022   -0.0247509  201 A1IN0 A CAW  
3621 O OAV  . A1IN0 C .   ? 0.955398 1.25133  0.738743 -0.123745   0.0905642   -0.047874   201 A1IN0 A OAV  
3622 C CAU  . A1IN0 C .   ? 0.881555 1.15808  0.715349 -0.115286   0.0907519   -0.060926   201 A1IN0 A CAU  
3623 C CAR  . A1IN0 C .   ? 0.847061 1.10615  0.713753 -0.118725   0.0879506   -0.0386816  201 A1IN0 A CAR  
3624 O OAS  . A1IN0 C .   ? 0.942471 1.2026   0.789515 -0.134095   0.0895222   -0.00517528 201 A1IN0 A OAS  
3625 C CAT  . A1IN0 C .   ? 0.955376 1.17848  0.812092 -0.139029   0.0697657   0.0252965   201 A1IN0 A CAT  
3626 C CAQ  . A1IN0 C .   ? 0.795437 1.03664  0.706967 -0.108866   0.0841486   -0.0507662  201 A1IN0 A CAQ  
3627 C CAP  . A1IN0 C .   ? 0.802377 1.037    0.721506 -0.0960206  0.0855053   -0.081006   201 A1IN0 A CAP  
3628 C CBG  . A1IN0 C .   ? 0.854409 1.10188  0.742413 -0.096134   0.0897584   -0.102367   201 A1IN0 A CBG  
3629 C CBD  . A1IN0 C .   ? 0.909332 1.18123  0.756052 -0.105433   0.0916743   -0.0950691  201 A1IN0 A CBD  
3630 O OBE  . A1IN0 C .   ? 0.990007 1.28048  0.804086 -0.107559   0.0932192   -0.119125   201 A1IN0 A OBE  
3631 C CBF  . A1IN0 C .   ? 0.927628 1.21004  0.755285 -0.10392    0.104145    -0.156323   201 A1IN0 A CBF  
3632 H HAK  . A1IN0 C .   ? 0.617808 0.882683 0.566283 -0.0863002  0.132604    -0.11573    201 A1IN0 A HAK  
3633 H HB6  . A1IN0 C .   ? 0.593939 0.848234 0.583792 -0.0873364  0.114594    -0.0890395  201 A1IN0 A HB6  
3634 H HAL  . A1IN0 C .   ? 0.612321 0.897701 0.624606 -0.0640227  0.158822    -0.130209   201 A1IN0 A HAL  
3635 H HB7  . A1IN0 C .   ? 0.614153 0.854508 0.595812 -0.058278   0.151178    -0.15187    201 A1IN0 A HB7  
3636 H HAM  . A1IN0 C .   ? 0.604356 0.847109 0.655482 -0.0554525  0.118175    -0.109788   201 A1IN0 A HAM  
3637 H HB8  . A1IN0 C .   ? 0.61926  0.854424 0.668046 -0.0334507  0.141594    -0.139113   201 A1IN0 A HB8  
3638 H HAN  . A1IN0 C .   ? 0.61406  0.786818 0.64202  -0.0366551  0.106641    -0.131914   201 A1IN0 A HAN  
3639 H HB9  . A1IN0 C .   ? 0.639576 0.821211 0.634737 -0.0451469  0.127002    -0.152363   201 A1IN0 A HB9  
3640 H HCA  . A1IN0 C .   ? 0.600694 0.773019 0.585817 -0.0605264  0.088248    -0.125544   201 A1IN0 A HCA  
3641 H HAO  . A1IN0 C .   ? 0.598415 0.792276 0.608821 -0.065829   0.0851937   -0.100954   201 A1IN0 A HAO  
3642 H HAJ  . A1IN0 C .   ? 0.623644 0.838893 0.572453 -0.0744402  0.111143    -0.134765   201 A1IN0 A HAJ  
3643 H HAI  . A1IN0 C .   ? 0.653887 0.861271 0.626397 -0.0871604  0.0750531   -0.0751028  201 A1IN0 A HAI  
3644 H HAH  . A1IN0 C .   ? 0.652551 0.830904 0.568798 -0.0905892  0.027893    -0.0375763  201 A1IN0 A HAH  
3645 H HB5  . A1IN0 C .   ? 0.626298 0.807501 0.582686 -0.0935659  0.0451974   -0.0452179  201 A1IN0 A HB5  
3646 H HAG  . A1IN0 C .   ? 0.675518 0.798383 0.631858 -0.0873765  0.00258144  -0.0180933  201 A1IN0 A HAG  
3647 H HB4  . A1IN0 C .   ? 0.628458 0.757858 0.610951 -0.0764095  0.0118098   -0.0497364  201 A1IN0 A HB4  
3648 H HAF  . A1IN0 C .   ? 0.67992  0.822636 0.608753 -0.066969   -0.00993261 -0.0446051  201 A1IN0 A HAF  
3649 H HB3  . A1IN0 C .   ? 0.660805 0.766088 0.621945 -0.0603548  -0.0206134  -0.0443042  201 A1IN0 A HB3  
3650 H HB2  . A1IN0 C .   ? 0.603103 0.732202 0.579378 -0.0601486  0.0101237   -0.0834565  201 A1IN0 A HB2  
3651 H HB1  . A1IN0 C .   ? 0.617588 0.756171 0.576729 -0.0537078  -0.00693137 -0.0854864  201 A1IN0 A HB1  
3652 H HA   . A1IN0 C .   ? 0.589757 0.755727 0.539105 -0.0666648  0.0321144   -0.112262   201 A1IN0 A HA   
3653 H HCE  . A1IN0 C .   ? 0.757807 0.989242 0.605566 -0.0754646  -0.00230913 -0.0683294  201 A1IN0 A HCE  
3654 H HAZ  . A1IN0 C .   ? 0.778812 0.977545 0.628094 -0.0811048  -0.00157592 -0.0283906  201 A1IN0 A HAZ  
3655 H HAY  . A1IN0 C .   ? 0.845231 1.11298  0.656907 -0.0961261  0.0375092   -0.0827271  201 A1IN0 A HAY  
3656 H HAX  . A1IN0 C .   ? 0.930036 1.15112  0.735035 -0.106175   0.0268697   0.0001026   201 A1IN0 A HAX  
3657 H HCD  . A1IN0 C .   ? 0.976227 1.27473  0.708143 -0.116156   0.0542293   -0.0396646  201 A1IN0 A HCD  
3658 H HAW  . A1IN0 C .   ? 0.992684 1.26495  0.734399 -0.126812   0.0600125   0.00434701  201 A1IN0 A HAW  
3659 H HCC  . A1IN0 C .   ? 1.00075  1.21695  0.821179 -0.146744   0.0656627   0.0499197   201 A1IN0 A HCC  
3660 H HAT  . A1IN0 C .   ? 0.944232 1.16956  0.832669 -0.148673   0.0794605   0.0300649   201 A1IN0 A HAT  
3661 H HCB  . A1IN0 C .   ? 0.932289 1.13214  0.800398 -0.125478   0.0497149   0.0179315   201 A1IN0 A HCB  
3662 H HAQ  . A1IN0 C .   ? 0.794025 1.02527  0.730453 -0.11274    0.0799653   -0.0365003  201 A1IN0 A HAQ  
3663 H HBG  . A1IN0 C .   ? 0.829351 1.06782  0.724116 -0.0904224  0.0930718   -0.125786   201 A1IN0 A HBG  
3664 H HCG  . A1IN0 C .   ? 0.965186 1.26561  0.764841 -0.109888   0.108229    -0.175754   201 A1IN0 A HCG  
3665 H HBF  . A1IN0 C .   ? 0.911027 1.17646  0.756202 -0.0993632  0.0900497   -0.159141   201 A1IN0 A HBF  
3666 H HCF  . A1IN0 C .   ? 0.930419 1.20597  0.777138 -0.100083   0.122963    -0.162905   201 A1IN0 A HCF  
3667 C CAK  . A1IN0 D .   ? 0.723961 0.571591 0.628175 -0.0792137  0.25963     0.00450154  201 A1IN0 B CAK  
3668 C CAL  . A1IN0 D .   ? 0.804577 0.585349 0.636797 -0.0619663  0.242624    0.0222079   201 A1IN0 B CAL  
3669 C CAM  . A1IN0 D .   ? 0.758191 0.48641  0.620331 -0.0809272  0.201245    0.00755937  201 A1IN0 B CAM  
3670 C CAN  . A1IN0 D .   ? 0.670281 0.450028 0.553948 -0.0765214  0.182892    -0.0298717  201 A1IN0 B CAN  
3671 C CAO  . A1IN0 D .   ? 0.603266 0.439806 0.555952 -0.0922475  0.193229    -0.045343   201 A1IN0 B CAO  
3672 C CAJ  . A1IN0 D .   ? 0.641927 0.523479 0.575316 -0.0780504  0.230504    -0.0378791  201 A1IN0 B CAJ  
3673 C CAI  . A1IN0 D .   ? 0.611195 0.551674 0.613453 -0.0884103  0.247144    -0.0570363  201 A1IN0 B CAI  
3674 C CAB  . A1IN0 D .   ? 0.593059 0.560507 0.61078  -0.0826479  0.226058    -0.0929408  201 A1IN0 B CAB  
3675 O OAA  . A1IN0 D .   ? 0.625822 0.595108 0.590489 -0.0640291  0.212044    -0.106056   201 A1IN0 B OAA  
3676 N N    . A1IN0 D .   ? 0.589012 0.581346 0.681604 -0.095374   0.220395    -0.113583   201 A1IN0 B N    
3677 C CAH  . A1IN0 D .   ? 0.631287 0.644003 0.803007 -0.112323   0.240531    -0.103685   201 A1IN0 B CAH  
3678 C CAG  . A1IN0 D .   ? 0.604201 0.610417 0.850245 -0.128597   0.213525    -0.111813   201 A1IN0 B CAG  
3679 C CAF  . A1IN0 D .   ? 0.588895 0.61521  0.84229  -0.116074   0.203535    -0.143996   201 A1IN0 B CAF  
3680 C CB   . A1IN0 D .   ? 0.543816 0.544518 0.726086 -0.106517   0.181576    -0.15299    201 A1IN0 B CB   
3681 C CA   . A1IN0 D .   ? 0.587313 0.599687 0.691352 -0.0887291  0.203147    -0.147508   201 A1IN0 B CA   
3682 C C    . A1IN0 D .   ? 0.633914 0.696367 0.728326 -0.0715709  0.224865    -0.174877   201 A1IN0 B C    
3683 O O    . A1IN0 D .   ? 0.609308 0.685787 0.721292 -0.0691492  0.212727    -0.204814   201 A1IN0 B O    
3684 O OBA  . A1IN0 D .   ? 0.807786 0.895597 0.878533 -0.0607145  0.26014     -0.164312   201 A1IN0 B OBA  
3685 C CAZ  . A1IN0 D .   ? 0.792975 0.927338 0.829898 -0.0379648  0.285397    -0.18824    201 A1IN0 B CAZ  
3686 C CAY  . A1IN0 D .   ? 0.755309 0.906439 0.790225 -0.0348127  0.327788    -0.163879   201 A1IN0 B CAY  
3687 C CAX  . A1IN0 D .   ? 0.804858 0.966256 0.747662 -0.011063   0.350021    -0.148998   201 A1IN0 B CAX  
3688 C CAW  . A1IN0 D .   ? 0.81732  0.989361 0.727858 -0.00321276 0.396674    -0.115296   201 A1IN0 B CAW  
3689 O OAV  . A1IN0 D .   ? 0.818964 0.941806 0.666338 -0.00247392 0.394529    -0.0663214  201 A1IN0 B OAV  
3690 C CAU  . A1IN0 D .   ? 0.770576 0.848896 0.667853 -0.0278567  0.361084    -0.0587418  201 A1IN0 B CAU  
3691 C CAR  . A1IN0 D .   ? 0.752475 0.81481  0.742804 -0.0619534  0.365884    -0.0417241  201 A1IN0 B CAR  
3692 O OAS  . A1IN0 D .   ? 0.81418  0.910816 0.8522   -0.0707919  0.413388    -0.024761   201 A1IN0 B OAS  
3693 C CAT  . A1IN0 D .   ? 0.750421 0.855362 0.907563 -0.102652   0.410498    -0.0232841  201 A1IN0 B CAT  
3694 C CAQ  . A1IN0 D .   ? 0.696237 0.710665 0.723312 -0.083601   0.323261    -0.0410804  201 A1IN0 B CAQ  
3695 C CAP  . A1IN0 D .   ? 0.668435 0.655367 0.643075 -0.0704892  0.284478    -0.0565773  201 A1IN0 B CAP  
3696 C CBG  . A1IN0 D .   ? 0.694131 0.70734  0.59038  -0.037713   0.284964    -0.0724992  201 A1IN0 B CBG  
3697 C CBD  . A1IN0 D .   ? 0.747559 0.804713 0.604066 -0.0167918  0.319347    -0.0741202  201 A1IN0 B CBD  
3698 O OBE  . A1IN0 D .   ? 0.732206 0.820783 0.513575 0.0158923   0.316054    -0.0927271  201 A1IN0 B OBE  
3699 C CBF  . A1IN0 D .   ? 0.767128 0.835538 0.501567 0.0311125   0.283398    -0.0924025  201 A1IN0 B CBF  
3700 H HAK  . A1IN0 D .   ? 0.743791 0.629808 0.628127 -0.0658327  0.285747    0.00665412  201 A1IN0 B HAK  
3701 H HB6  . A1IN0 D .   ? 0.746073 0.565823 0.697312 -0.105085   0.262119    0.0215394   201 A1IN0 B HB6  
3702 H HAL  . A1IN0 D .   ? 0.851508 0.597898 0.667465 -0.065276   0.262824    0.0553211   201 A1IN0 B HAL  
3703 H HB7  . A1IN0 D .   ? 0.789157 0.59161  0.568534 -0.0328145  0.237539    0.0106453   201 A1IN0 B HB7  
3704 H HAM  . A1IN0 D .   ? 0.766263 0.474923 0.684173 -0.110172   0.199944    0.0163651   201 A1IN0 B HAM  
3705 H HB8  . A1IN0 D .   ? 0.795576 0.475495 0.606037 -0.0650659  0.188583    0.0140868   201 A1IN0 B HB8  
3706 H HAN  . A1IN0 D .   ? 0.661959 0.407396 0.550409 -0.0836968  0.15615     -0.0383921  201 A1IN0 B HAN  
3707 H HB9  . A1IN0 D .   ? 0.665054 0.468769 0.502635 -0.0507649  0.184672    -0.0388374  201 A1IN0 B HB9  
3708 H HCA  . A1IN0 D .   ? 0.575245 0.438199 0.534553 -0.086539   0.181495    -0.0686661  201 A1IN0 B HCA  
3709 H HAO  . A1IN0 D .   ? 0.613825 0.441026 0.621401 -0.115589   0.193217    -0.0371088  201 A1IN0 B HAO  
3710 H HAJ  . A1IN0 D .   ? 0.640917 0.540725 0.523189 -0.0536206  0.226914    -0.0500661  201 A1IN0 B HAJ  
3711 H HAI  . A1IN0 D .   ? 0.619694 0.549226 0.682666 -0.111834   0.246955    -0.0465392  201 A1IN0 B HAI  
3712 H HAH  . A1IN0 D .   ? 0.629495 0.684683 0.807006 -0.100733   0.267573    -0.116191   201 A1IN0 B HAH  
3713 H HB5  . A1IN0 D .   ? 0.651243 0.643601 0.820805 -0.122705   0.251366    -0.0762541  201 A1IN0 B HB5  
3714 H HAG  . A1IN0 D .   ? 0.607244 0.635546 0.917069 -0.138757   0.226589    -0.105827   201 A1IN0 B HAG  
3715 H HB4  . A1IN0 D .   ? 0.604916 0.570865 0.838343 -0.136793   0.184408    -0.105032   201 A1IN0 B HB4  
3716 H HAF  . A1IN0 D .   ? 0.580195 0.641929 0.831635 -0.103342   0.226813    -0.160475   201 A1IN0 B HAF  
3717 H HB3  . A1IN0 D .   ? 0.55675  0.575749 0.859973 -0.124052   0.183067    -0.148396   201 A1IN0 B HB3  
3718 H HB2  . A1IN0 D .   ? 0.558526 0.521657 0.721389 -0.113155   0.160908    -0.13922    201 A1IN0 B HB2  
3719 H HB1  . A1IN0 D .   ? 0.539151 0.553588 0.726575 -0.100481   0.177109    -0.174783   201 A1IN0 B HB1  
3720 H HA   . A1IN0 D .   ? 0.582199 0.576332 0.644467 -0.0827758  0.186111    -0.148629   201 A1IN0 B HA   
3721 H HCE  . A1IN0 D .   ? 0.800418 0.939136 0.7742   -0.0222323  0.279938    -0.191188   201 A1IN0 B HCE  
3722 H HAZ  . A1IN0 D .   ? 0.763927 0.919917 0.840671 -0.036519   0.283619    -0.221319   201 A1IN0 B HAZ  
3723 H HAY  . A1IN0 D .   ? 0.75753  0.912507 0.859549 -0.0502054  0.341804    -0.152636   201 A1IN0 B HAY  
3724 H HAX  . A1IN0 D .   ? 0.799884 0.96113  0.686358 0.00462294  0.328465    -0.162349   201 A1IN0 B HAX  
3725 H HCD  . A1IN0 D .   ? 0.8613   1.06409  0.715316 0.021849    0.413369    -0.130597   201 A1IN0 B HCD  
3726 H HAW  . A1IN0 D .   ? 0.811982 0.989231 0.787079 -0.0207148  0.41831     -0.100855   201 A1IN0 B HAW  
3727 H HCC  . A1IN0 D .   ? 0.777886 0.926058 0.972512 -0.102373   0.451152    -0.017974   201 A1IN0 B HCC  
3728 H HAT  . A1IN0 D .   ? 0.767193 0.829499 0.944108 -0.125333   0.399287    0.00445218  201 A1IN0 B HAT  
3729 H HCB  . A1IN0 D .   ? 0.704285 0.815494 0.896301 -0.10326    0.378864    -0.0552413  201 A1IN0 B HCB  
3730 H HAQ  . A1IN0 D .   ? 0.685667 0.689144 0.783584 -0.109099   0.319747    -0.0311312  201 A1IN0 B HAQ  
3731 H HBG  . A1IN0 D .   ? 0.679528 0.68125  0.545507 -0.027501   0.258703    -0.083301   201 A1IN0 B HBG  
3732 H HCG  . A1IN0 D .   ? 0.793785 0.890085 0.465924 0.0593815   0.2834      -0.100092   201 A1IN0 B HCG  
3733 H HBF  . A1IN0 D .   ? 0.701973 0.776507 0.475154 0.0214451   0.257783    -0.119392   201 A1IN0 B HBF  
3734 H HCF  . A1IN0 D .   ? 0.777826 0.797505 0.498438 0.0265969   0.283598    -0.058013   201 A1IN0 B HCF  
# 
