data_9GPN
# 
_entry.id   9GPN 
# 
_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   9GPN         pdb_00009gpn 10.2210/pdb9gpn/pdb 
WWPDB D_1292141130 ?            ?                   
# 
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 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 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 2 'Structure model' '_citation_author.name'             
5 3 'Structure model' '_citation.page_first'              
6 3 'Structure model' '_citation.page_last'               
7 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                        9GPN 
_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 ? 
'Buffa, V.'   2 ? 
'Walz, C.'    3 ? 
'Hausch, F.'  4 ? 
# 
_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                e202418512 
_citation.page_last                 e202418512 
_citation.title                     
'Conformational Plasticity and Binding Affinity Enhancement Controlled by Linker Derivatization in Macrocycles.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202418512 
_citation.pdbx_database_id_PubMed   39749563 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Buffa, V.'        1  ?                   
primary 'Walz, C.'         2  ?                   
primary 'Meyners, C.'      3  ?                   
primary 'Zheng, M.'        4  ?                   
primary 'Oki Sugiarto, W.' 5  ?                   
primary 'Repity, M.'       6  ?                   
primary 'Achaq, H.'        7  ?                   
primary 'Brudy, C.'        8  ?                   
primary 'Spiske, M.'       9  ?                   
primary 'Cica, M.'         10 ?                   
primary 'Hausch, F.'       11 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 
;3-cyclohexyl-1,19-dimethoxy-11,16-dioxa-19lambda4-polona-1,13-diaza-2lambda5-polonapentacyclo[16.4.0.04,9.013,19.020,25]docosane-2,12-dione
;
540.651   2   ?       ?                    ? ? 
3 water       nat water 18.015    100 ?       ?                    ? ? 
# 
_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 
;3-cyclohexyl-1,19-dimethoxy-11,16-dioxa-19lambda4-polona-1,13-diaza-2lambda5-polonapentacyclo[16.4.0.04,9.013,19.020,25]docosane-2,12-dione
;
A1INN 
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 
A1INN non-polymer         . 
;3-cyclohexyl-1,19-dimethoxy-11,16-dioxa-19lambda4-polona-1,13-diaza-2lambda5-polonapentacyclo[16.4.0.04,9.013,19.020,25]docosane-2,12-dione
;
? 'C29 H40 N4 O6'  540.651 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   13  13  GLY GLY A . n 
A 1 2   ALA 2   14  14  ALA ALA A . n 
A 1 3   PRO 3   15  15  PRO PRO A . n 
A 1 4   ALA 4   16  16  ALA ALA A . n 
A 1 5   THR 5   17  17  THR THR A . n 
A 1 6   VAL 6   18  18  VAL VAL A . n 
A 1 7   THR 7   19  19  THR THR 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        A1INN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1INN 
_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 A1INN 1  201 201 A1INN DRG A . 
D 2 A1INN 1  201 201 A1INN DRG B . 
E 3 HOH   1  301 30  HOH   HOH A . 
E 3 HOH   2  302 96  HOH   HOH A . 
E 3 HOH   3  303 92  HOH   HOH A . 
E 3 HOH   4  304 57  HOH   HOH A . 
E 3 HOH   5  305 52  HOH   HOH A . 
E 3 HOH   6  306 69  HOH   HOH A . 
E 3 HOH   7  307 17  HOH   HOH A . 
E 3 HOH   8  308 64  HOH   HOH A . 
E 3 HOH   9  309 41  HOH   HOH A . 
E 3 HOH   10 310 55  HOH   HOH A . 
E 3 HOH   11 311 25  HOH   HOH A . 
E 3 HOH   12 312 18  HOH   HOH A . 
E 3 HOH   13 313 28  HOH   HOH A . 
E 3 HOH   14 314 85  HOH   HOH A . 
E 3 HOH   15 315 21  HOH   HOH A . 
E 3 HOH   16 316 14  HOH   HOH A . 
E 3 HOH   17 317 20  HOH   HOH A . 
E 3 HOH   18 318 79  HOH   HOH A . 
E 3 HOH   19 319 36  HOH   HOH A . 
E 3 HOH   20 320 38  HOH   HOH A . 
E 3 HOH   21 321 26  HOH   HOH A . 
E 3 HOH   22 322 72  HOH   HOH A . 
E 3 HOH   23 323 46  HOH   HOH A . 
E 3 HOH   24 324 67  HOH   HOH A . 
E 3 HOH   25 325 34  HOH   HOH A . 
E 3 HOH   26 326 86  HOH   HOH A . 
E 3 HOH   27 327 44  HOH   HOH A . 
E 3 HOH   28 328 95  HOH   HOH A . 
E 3 HOH   29 329 15  HOH   HOH A . 
E 3 HOH   30 330 29  HOH   HOH A . 
E 3 HOH   31 331 42  HOH   HOH A . 
E 3 HOH   32 332 62  HOH   HOH A . 
E 3 HOH   33 333 31  HOH   HOH A . 
E 3 HOH   34 334 4   HOH   HOH A . 
E 3 HOH   35 335 66  HOH   HOH A . 
E 3 HOH   36 336 80  HOH   HOH A . 
E 3 HOH   37 337 37  HOH   HOH A . 
E 3 HOH   38 338 33  HOH   HOH A . 
E 3 HOH   39 339 65  HOH   HOH A . 
E 3 HOH   40 340 56  HOH   HOH A . 
E 3 HOH   41 341 23  HOH   HOH A . 
E 3 HOH   42 342 24  HOH   HOH A . 
E 3 HOH   43 343 10  HOH   HOH A . 
E 3 HOH   44 344 43  HOH   HOH A . 
E 3 HOH   45 345 83  HOH   HOH A . 
E 3 HOH   46 346 73  HOH   HOH A . 
E 3 HOH   47 347 89  HOH   HOH A . 
E 3 HOH   48 348 93  HOH   HOH A . 
E 3 HOH   49 349 54  HOH   HOH A . 
E 3 HOH   50 350 74  HOH   HOH A . 
E 3 HOH   51 351 98  HOH   HOH A . 
F 3 HOH   1  301 22  HOH   HOH B . 
F 3 HOH   2  302 71  HOH   HOH B . 
F 3 HOH   3  303 53  HOH   HOH B . 
F 3 HOH   4  304 16  HOH   HOH B . 
F 3 HOH   5  305 27  HOH   HOH B . 
F 3 HOH   6  306 91  HOH   HOH B . 
F 3 HOH   7  307 59  HOH   HOH B . 
F 3 HOH   8  308 39  HOH   HOH B . 
F 3 HOH   9  309 102 HOH   HOH B . 
F 3 HOH   10 310 32  HOH   HOH B . 
F 3 HOH   11 311 77  HOH   HOH B . 
F 3 HOH   12 312 40  HOH   HOH B . 
F 3 HOH   13 313 61  HOH   HOH B . 
F 3 HOH   14 314 8   HOH   HOH B . 
F 3 HOH   15 315 45  HOH   HOH B . 
F 3 HOH   16 316 50  HOH   HOH B . 
F 3 HOH   17 317 70  HOH   HOH B . 
F 3 HOH   18 318 9   HOH   HOH B . 
F 3 HOH   19 319 19  HOH   HOH B . 
F 3 HOH   20 320 49  HOH   HOH B . 
F 3 HOH   21 321 78  HOH   HOH B . 
F 3 HOH   22 322 60  HOH   HOH B . 
F 3 HOH   23 323 7   HOH   HOH B . 
F 3 HOH   24 324 11  HOH   HOH B . 
F 3 HOH   25 325 35  HOH   HOH B . 
F 3 HOH   26 326 51  HOH   HOH B . 
F 3 HOH   27 327 6   HOH   HOH B . 
F 3 HOH   28 328 13  HOH   HOH B . 
F 3 HOH   29 329 5   HOH   HOH B . 
F 3 HOH   30 330 97  HOH   HOH B . 
F 3 HOH   31 331 76  HOH   HOH B . 
F 3 HOH   32 332 94  HOH   HOH B . 
F 3 HOH   33 333 3   HOH   HOH B . 
F 3 HOH   34 334 99  HOH   HOH B . 
F 3 HOH   35 335 58  HOH   HOH B . 
F 3 HOH   36 336 48  HOH   HOH B . 
F 3 HOH   37 337 81  HOH   HOH B . 
F 3 HOH   38 338 12  HOH   HOH B . 
F 3 HOH   39 339 84  HOH   HOH B . 
F 3 HOH   40 340 68  HOH   HOH B . 
F 3 HOH   41 341 75  HOH   HOH B . 
F 3 HOH   42 342 82  HOH   HOH B . 
F 3 HOH   43 343 88  HOH   HOH B . 
F 3 HOH   44 344 87  HOH   HOH B . 
F 3 HOH   45 345 90  HOH   HOH B . 
F 3 HOH   46 346 100 HOH   HOH B . 
F 3 HOH   47 347 47  HOH   HOH B . 
F 3 HOH   48 348 101 HOH   HOH B . 
F 3 HOH   49 349 63  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 44  ? CG  ? A GLU 32  CG  
2   1 Y 1 A GLU 44  ? CD  ? A GLU 32  CD  
3   1 Y 1 A GLU 44  ? OE1 ? A GLU 32  OE1 
4   1 Y 1 A GLU 44  ? OE2 ? A GLU 32  OE2 
5   1 Y 1 A GLU 45  ? CG  ? A GLU 33  CG  
6   1 Y 1 A GLU 45  ? CD  ? A GLU 33  CD  
7   1 Y 1 A GLU 45  ? OE1 ? A GLU 33  OE1 
8   1 Y 1 A GLU 45  ? OE2 ? A GLU 33  OE2 
9   1 Y 1 A LYS 58  ? CG  ? A LYS 46  CG  
10  1 Y 1 A LYS 58  ? CD  ? A LYS 46  CD  
11  1 Y 1 A LYS 58  ? CE  ? A LYS 46  CE  
12  1 Y 1 A LYS 58  ? NZ  ? A LYS 46  NZ  
13  1 Y 1 A ASN 63  ? CG  ? A ASN 51  CG  
14  1 Y 1 A ASN 63  ? OD1 ? A ASN 51  OD1 
15  1 Y 1 A ASN 63  ? ND2 ? A ASN 51  ND2 
16  1 Y 1 A LYS 65  ? CG  ? A LYS 53  CG  
17  1 Y 1 A LYS 65  ? CD  ? A LYS 53  CD  
18  1 Y 1 A LYS 65  ? CE  ? A LYS 53  CE  
19  1 Y 1 A LYS 65  ? NZ  ? A LYS 53  NZ  
20  1 Y 1 A LYS 66  ? CG  ? A LYS 54  CG  
21  1 Y 1 A LYS 66  ? CD  ? A LYS 54  CD  
22  1 Y 1 A LYS 66  ? CE  ? A LYS 54  CE  
23  1 Y 1 A LYS 66  ? NZ  ? A LYS 54  NZ  
24  1 Y 1 A ARG 73  ? CG  ? A ARG 61  CG  
25  1 Y 1 A ARG 73  ? CD  ? A ARG 61  CD  
26  1 Y 1 A ARG 73  ? NE  ? A ARG 61  NE  
27  1 Y 1 A ARG 73  ? CZ  ? A ARG 61  CZ  
28  1 Y 1 A ARG 73  ? NH1 ? A ARG 61  NH1 
29  1 Y 1 A ARG 73  ? NH2 ? A ARG 61  NH2 
30  1 Y 1 A ASN 74  ? CG  ? A ASN 62  CG  
31  1 Y 1 A ASN 74  ? OD1 ? A ASN 62  OD1 
32  1 Y 1 A ASN 74  ? ND2 ? A ASN 62  ND2 
33  1 Y 1 A LYS 83  ? CG  ? A LYS 71  CG  
34  1 Y 1 A LYS 83  ? CD  ? A LYS 71  CD  
35  1 Y 1 A LYS 83  ? CE  ? A LYS 71  CE  
36  1 Y 1 A LYS 83  ? NZ  ? A LYS 71  NZ  
37  1 Y 1 A LYS 88  ? CG  ? A LYS 76  CG  
38  1 Y 1 A LYS 88  ? CD  ? A LYS 76  CD  
39  1 Y 1 A LYS 88  ? CE  ? A LYS 76  CE  
40  1 Y 1 A LYS 88  ? NZ  ? A LYS 76  NZ  
41  1 Y 1 A LYS 138 ? CG  ? A LYS 126 CG  
42  1 Y 1 A LYS 138 ? CD  ? A LYS 126 CD  
43  1 Y 1 A LYS 138 ? CE  ? A LYS 126 CE  
44  1 Y 1 A LYS 138 ? NZ  ? A LYS 126 NZ  
45  1 Y 1 A GLU 140 ? CG  ? A GLU 128 CG  
46  1 Y 1 A GLU 140 ? CD  ? A GLU 128 CD  
47  1 Y 1 A GLU 140 ? OE1 ? A GLU 128 OE1 
48  1 Y 1 A GLU 140 ? OE2 ? A GLU 128 OE2 
49  1 Y 1 B GLU 20  ? CG  ? B GLU 8   CG  
50  1 Y 1 B GLU 20  ? CD  ? B GLU 8   CD  
51  1 Y 1 B GLU 20  ? OE1 ? B GLU 8   OE1 
52  1 Y 1 B GLU 20  ? OE2 ? B GLU 8   OE2 
53  1 Y 1 B GLU 44  ? CG  ? B GLU 32  CG  
54  1 Y 1 B GLU 44  ? CD  ? B GLU 32  CD  
55  1 Y 1 B GLU 44  ? OE1 ? B GLU 32  OE1 
56  1 Y 1 B GLU 44  ? OE2 ? B GLU 32  OE2 
57  1 Y 1 B GLU 45  ? CG  ? B GLU 33  CG  
58  1 Y 1 B GLU 45  ? CD  ? B GLU 33  CD  
59  1 Y 1 B GLU 45  ? OE1 ? B GLU 33  OE1 
60  1 Y 1 B GLU 45  ? OE2 ? B GLU 33  OE2 
61  1 Y 1 B ASN 63  ? CG  ? B ASN 51  CG  
62  1 Y 1 B ASN 63  ? OD1 ? B ASN 51  OD1 
63  1 Y 1 B ASN 63  ? ND2 ? B ASN 51  ND2 
64  1 Y 1 B LYS 65  ? CG  ? B LYS 53  CG  
65  1 Y 1 B LYS 65  ? CD  ? B LYS 53  CD  
66  1 Y 1 B LYS 65  ? CE  ? B LYS 53  CE  
67  1 Y 1 B LYS 65  ? NZ  ? B LYS 53  NZ  
68  1 Y 1 B LYS 66  ? CG  ? B LYS 54  CG  
69  1 Y 1 B LYS 66  ? CD  ? B LYS 54  CD  
70  1 Y 1 B LYS 66  ? CE  ? B LYS 54  CE  
71  1 Y 1 B LYS 66  ? NZ  ? B LYS 54  NZ  
72  1 Y 1 B ASP 72  ? CG  ? B ASP 60  CG  
73  1 Y 1 B ASP 72  ? OD1 ? B ASP 60  OD1 
74  1 Y 1 B ASP 72  ? OD2 ? B ASP 60  OD2 
75  1 Y 1 B ARG 73  ? CG  ? B ARG 61  CG  
76  1 Y 1 B ARG 73  ? CD  ? B ARG 61  CD  
77  1 Y 1 B ARG 73  ? NE  ? B ARG 61  NE  
78  1 Y 1 B ARG 73  ? CZ  ? B ARG 61  CZ  
79  1 Y 1 B ARG 73  ? NH1 ? B ARG 61  NH1 
80  1 Y 1 B ARG 73  ? NH2 ? B ARG 61  NH2 
81  1 Y 1 B ASN 74  ? CG  ? B ASN 62  CG  
82  1 Y 1 B ASN 74  ? OD1 ? B ASN 62  OD1 
83  1 Y 1 B ASN 74  ? ND2 ? B ASN 62  ND2 
84  1 Y 1 B LYS 83  ? CG  ? B LYS 71  CG  
85  1 Y 1 B LYS 83  ? CD  ? B LYS 71  CD  
86  1 Y 1 B LYS 83  ? CE  ? B LYS 71  CE  
87  1 Y 1 B LYS 83  ? NZ  ? B LYS 71  NZ  
88  1 Y 1 B LYS 88  ? CG  ? B LYS 76  CG  
89  1 Y 1 B LYS 88  ? CD  ? B LYS 76  CD  
90  1 Y 1 B LYS 88  ? CE  ? B LYS 76  CE  
91  1 Y 1 B LYS 88  ? NZ  ? B LYS 76  NZ  
92  1 Y 1 B LYS 99  ? CG  ? B LYS 87  CG  
93  1 Y 1 B LYS 99  ? CD  ? B LYS 87  CD  
94  1 Y 1 B LYS 99  ? CE  ? B LYS 87  CE  
95  1 Y 1 B LYS 99  ? NZ  ? B LYS 87  NZ  
96  1 Y 1 B LYS 138 ? CG  ? B LYS 126 CG  
97  1 Y 1 B LYS 138 ? CD  ? B LYS 126 CD  
98  1 Y 1 B LYS 138 ? CE  ? B LYS 126 CE  
99  1 Y 1 B LYS 138 ? NZ  ? B LYS 126 NZ  
100 1 Y 1 B GLU 140 ? CG  ? B GLU 128 CG  
101 1 Y 1 B GLU 140 ? CD  ? B GLU 128 CD  
102 1 Y 1 B GLU 140 ? OE1 ? B GLU 128 OE1 
103 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                     9GPN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.933 
_cell.length_a_esd                 ? 
_cell.length_b                     48.933 
_cell.length_b_esd                 ? 
_cell.length_c                     194.667 
_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                         9GPN 
_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                   9GPN 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.40 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.79 
_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    '14% PEG3350, 0.2M ammonium acetate, 0.1M HEPES-NaOH pH 7.5, 10% glycol' 
_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         2023-05-20 
_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                                       9GPN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               48.67 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     26029 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_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                                0.102 
_reflns.pdbx_Rpim_I_all                                0.046 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.090 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
9.00 48.67 ? 29.0 ? ? ? ? 275  ? ? ? ? ? ? ? ? ? ? ? 7.6 0.65 ? ? 0.044 0.019 ? 1 ? 0.999 ? ? 98.7 ? 0.039 ? ? ? ? ? ? ? ? ? 
1.80 1.84  ? 1.1  ? ? ? ? 1472 ? ? ? ? ? ? ? ? ? ? ? 5.9 0.91 ? ? 1.819 0.948 ? 2 ? 0.417 ? ? 98.5 ? 1.532 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.710 
_refine.aniso_B[1][2]                            -0.355 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -0.710 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            2.304 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               37.423 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.949 
_refine.correlation_coeff_Fo_to_Fc_free          0.940 
_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                                 9GPN 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.800 
_refine.ls_d_res_low                             42.413 
_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                     25957 
_refine.ls_number_reflns_R_free                  1304 
_refine.ls_number_reflns_R_work                  24653 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.387 
_refine.ls_percent_reflns_R_free                 5.024 
_refine.ls_R_factor_all                          0.227 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2628 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2255 
_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                       0.146 
_refine.pdbx_overall_ESU_R_Free                  0.139 
_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                             8.516 
_refine.overall_SU_ML                            0.128 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.800 
_refine_hist.d_res_low                        42.413 
_refine_hist.number_atoms_solvent             100 
_refine_hist.number_atoms_total               2049 
_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        1871 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         78 
_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' ? 0.007  0.012  1997 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1846 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.448  1.815  2707 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 0.486  1.740  4299 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 8.739  5.000  254  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 28.246 13.571 14   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 12.598 10.000 301  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.783 10.000 66   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.068  0.200  298  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  2268 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  400  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.185  0.200  368  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.192  0.200  1688 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.174  0.200  1032 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  1015 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.157  0.200  88   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.028  0.200  1    ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.113  0.200  8    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.138  0.200  32   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.291  0.200  12   ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 1.729  2.064  1022 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 1.728  2.064  1022 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 2.714  3.701  1274 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 2.713  3.702  1275 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 1.667  2.071  975  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 1.667  2.071  976  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 2.607  3.764  1433 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 2.606  3.763  1434 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 4.703  19.617 2221 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 4.684  19.199 2205 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.106  0.050  3529 ? 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 ? ? 0.10629 ? 0.05008 1 'Local ncs' ? A ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.10629 ? 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' 1.800 1.847  1871 . 110 1726 98.1293  . 0.329 . . 0.325 . . . . . 0.327 . 20 . 0.908 0.852 0.396 
'X-RAY DIFFRACTION' 1.847 1.897  1849 . 73  1752 98.7020  . 0.314 . . 0.311 . . . . . 0.311 . 20 . 0.924 0.902 0.362 
'X-RAY DIFFRACTION' 1.897 1.952  1787 . 121 1652 99.2166  . 0.296 . . 0.293 . . . . . 0.290 . 20 . 0.935 0.919 0.330 
'X-RAY DIFFRACTION' 1.952 2.012  1737 . 80  1646 99.3667  . 0.274 . . 0.271 . . . . . 0.265 . 20 . 0.944 0.909 0.327 
'X-RAY DIFFRACTION' 2.012 2.078  1675 . 86  1556 98.0299  . 0.261 . . 0.261 . . . . . 0.250 . 20 . 0.954 0.954 0.265 
'X-RAY DIFFRACTION' 2.078 2.151  1652 . 78  1568 99.6368  . 0.237 . . 0.235 . . . . . 0.224 . 20 . 0.962 0.949 0.279 
'X-RAY DIFFRACTION' 2.151 2.232  1623 . 86  1532 99.6919  . 0.233 . . 0.232 . . . . . 0.216 . 20 . 0.963 0.953 0.261 
'X-RAY DIFFRACTION' 2.232 2.323  1512 . 72  1439 99.9339  . 0.240 . . 0.237 . . . . . 0.219 . 20 . 0.960 0.935 0.290 
'X-RAY DIFFRACTION' 2.323 2.426  1447 . 63  1383 99.9309  . 0.229 . . 0.227 . . . . . 0.210 . 20 . 0.966 0.961 0.269 
'X-RAY DIFFRACTION' 2.426 2.543  1418 . 86  1327 99.6474  . 0.228 . . 0.227 . . . . . 0.208 . 20 . 0.969 0.961 0.246 
'X-RAY DIFFRACTION' 2.543 2.681  1349 . 79  1269 99.9259  . 0.237 . . 0.230 . . . . . 0.214 . 20 . 0.967 0.936 0.356 
'X-RAY DIFFRACTION' 2.681 2.842  1283 . 54  1229 100.0000 . 0.241 . . 0.239 . . . . . 0.225 . 20 . 0.961 0.942 0.291 
'X-RAY DIFFRACTION' 2.842 3.038  1221 . 62  1157 99.8362  . 0.229 . . 0.228 . . . . . 0.220 . 20 . 0.965 0.955 0.265 
'X-RAY DIFFRACTION' 3.038 3.280  1121 . 43  1076 99.8216  . 0.231 . . 0.230 . . . . . 0.230 . 20 . 0.964 0.966 0.243 
'X-RAY DIFFRACTION' 3.280 3.591  1041 . 56  984  99.9039  . 0.217 . . 0.215 . . . . . 0.217 . 20 . 0.971 0.960 0.255 
'X-RAY DIFFRACTION' 3.591 4.011  964  . 50  911  99.6888  . 0.200 . . 0.200 . . . . . 0.212 . 20 . 0.976 0.977 0.197 
'X-RAY DIFFRACTION' 4.011 4.624  850  . 31  816  99.6471  . 0.176 . . 0.174 . . . . . 0.193 . 20 . 0.983 0.974 0.220 
'X-RAY DIFFRACTION' 4.624 5.647  736  . 38  694  99.4565  . 0.184 . . 0.185 . . . . . 0.207 . 20 . 0.980 0.984 0.174 
'X-RAY DIFFRACTION' 5.647 7.916  598  . 15  582  99.8328  . 0.237 . . 0.237 . . . . . 0.264 . 20 . 0.965 0.967 0.240 
'X-RAY DIFFRACTION' 7.916 42.413 382  . 21  354  98.1675  . 0.252 . . 0.247 . . . . . 0.350 . 20 . 0.947 0.953 0.340 
# 
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 GLY 1 . A GLU 128 . A GLY 13 A GLU 140 ? ? 
1 2 1 B GLY 1 . B GLU 128 . B GLY 13 B GLU 140 ? ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   'Local NCS retraints between domains:       1       2' 
# 
_struct.entry_id                     9GPN 
_struct.title                        'The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog 11b/j' 
_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        9GPN 
_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 9GPN A 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
2 1 9GPN 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 9GPN GLY A 1  ? UNP Q13451 ?   ?   'expression tag'      13  1  
1 9GPN ALA A 2  ? UNP Q13451 ?   ?   'expression tag'      14  2  
1 9GPN PRO A 3  ? UNP Q13451 ?   ?   'expression tag'      15  3  
1 9GPN THR A 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  4  
1 9GPN ALA A 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 5  
1 9GPN ILE A 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 6  
2 9GPN GLY B 1  ? UNP Q13451 ?   ?   'expression tag'      13  7  
2 9GPN ALA B 2  ? UNP Q13451 ?   ?   'expression tag'      14  8  
2 9GPN PRO B 3  ? UNP Q13451 ?   ?   'expression tag'      15  9  
2 9GPN THR B 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  10 
2 9GPN ALA B 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 11 
2 9GPN 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 GLY A 1  ? GLY A 10  ? GLY A 13  GLY A 22  1 ? 10 
HELX_P HELX_P2 AA2 HIS A 59 ? ASN A 62  ? HIS A 71  ASN A 74  5 ? 4  
HELX_P HELX_P3 AA3 ILE A 75 ? ALA A 83  ? ILE A 87  ALA A 95  1 ? 9  
HELX_P HELX_P4 AA4 PRO A 97 ? ALA A 100 ? PRO A 109 ALA A 112 5 ? 4  
HELX_P HELX_P5 AA5 ALA B 2  ? GLY B 10  ? ALA B 14  GLY B 22  1 ? 9  
HELX_P HELX_P6 AA6 HIS B 59 ? ASN B 62  ? HIS B 71  ASN B 74  5 ? 4  
HELX_P HELX_P7 AA7 ILE B 75 ? THR B 84  ? ILE B 87  THR B 96  1 ? 10 
HELX_P HELX_P8 AA8 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 1.99  
2 LEU 107 B . ? LEU 119 B PRO 108 B ? PRO 120 B 1 -1.47 
# 
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 ASP A 56  ? SER A 57  ? ASP A 68  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 GLU A 121 ? O GLU A 133 N HIS A 44  ? N HIS A 56  
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 GLU A 121 ? O GLU A 133 N HIS A 44  ? N HIS A 56  
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 ILE B 95  ? N ILE B 107 O LEU B 116 ? O LEU B 128 
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 ILE B 95  ? N ILE B 107 O LEU B 116 ? O LEU B 128 
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                   9GPN 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   H 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   GLY 
_pdbx_validate_close_contact.auth_seq_id_1    41 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.59 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HG A SER 27  ? ? 1_555 OE2 A GLU 133 ? ? 4_565 1.57 
2 1 O  B HOH 333 ? ? 1_555 O   B HOH 344 ? ? 5_555 2.13 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 112 ? ? -133.96 -106.44 
2 1 SER A 118 ? ? -152.09 75.12   
3 1 ASP B 72  ? ? -86.93  32.93   
4 1 ASN B 74  ? ? 88.89   -15.10  
5 1 ALA B 112 ? ? -128.13 -99.18  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    64 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   LYS 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    65 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -148.88 
# 
_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     341 
_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 -9.7586 15.8089 4.1947  0.0807 ? -0.0036 ? -0.0157 ? 0.1059 ? -0.0300 ? 0.0849 ? 3.7576 ? -0.2788 
? 0.4095  ? 1.3027 ? 0.2168 ? 4.6130 ? -0.0691 ? -0.0858 ? -0.0386 ? -0.0551 ? -0.0844 ? 0.3280  ? 0.0110 ? -0.4766 ? 0.1535  ? 
2 'X-RAY DIFFRACTION' ? refined 8.3676  16.1736 29.4340 0.0033 ? 0.0080  ? -0.0062 ? 0.2405 ? -0.0604 ? 0.0844 ? 4.0197 ? -1.1647 
? -0.8144 ? 4.1513 ? 1.0411 ? 2.6473 ? -0.0215 ? -0.6216 ? 0.5429  ? 0.0461  ? 0.1991  ? -0.2806 ? 0.0912 ? 0.3462  ? -0.1775 ? 
# 
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 13 ? ? ? A 201 ? ALL ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 13 ? ? ? B 201 ? ALL ? 
# 
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 
A1INN C4   C Y N 1   
A1INN C14  C N N 2   
A1INN C5   C Y N 3   
A1INN C6   C Y N 4   
A1INN C11  C N N 5   
A1INN C7   C N N 6   
A1INN C8   C Y N 7   
A1INN C9   C N N 8   
A1INN C10  C N N 9   
A1INN C12  C Y N 10  
A1INN C13  C Y N 11  
A1INN N1   N Y N 12  
A1INN N2   N Y N 13  
A1INN C3   C Y N 14  
A1INN N3   N Y N 15  
A1INN C1   C N N 16  
A1INN O1   O N N 17  
A1INN C2   C Y N 18  
A1INN O2   O N N 19  
A1INN O3   O N N 20  
A1INN C15  C N N 21  
A1INN O4   O N N 22  
A1INN C16  C N N 23  
A1INN O5   O N N 24  
A1INN C17  C N S 25  
A1INN C18  C N N 26  
A1INN C19  C N N 27  
A1INN C20  C N N 28  
A1INN C21  C N N 29  
A1INN N4   N N N 30  
A1INN C22  C N N 31  
A1INN O6   O N N 32  
A1INN C23  C N S 33  
A1INN C24  C N N 34  
A1INN C25  C N N 35  
A1INN C26  C N N 36  
A1INN C27  C N N 37  
A1INN C28  C N N 38  
A1INN C29  C N N 39  
A1INN H17  H N N 40  
A1INN H16  H N N 41  
A1INN H5   H N N 42  
A1INN H14  H N N 43  
A1INN H13  H N N 44  
A1INN H7   H N N 45  
A1INN H8   H N N 46  
A1INN H6   H N N 47  
A1INN H9   H N N 48  
A1INN H10  H N N 49  
A1INN H12  H N N 50  
A1INN H11  H N N 51  
A1INN H15  H N N 52  
A1INN H4   H N N 53  
A1INN H2   H N N 54  
A1INN H3   H N N 55  
A1INN H1   H N N 56  
A1INN H19  H N N 57  
A1INN H18  H N N 58  
A1INN H20  H N N 59  
A1INN H22  H N N 60  
A1INN H21  H N N 61  
A1INN H23  H N N 62  
A1INN H24  H N N 63  
A1INN H25  H N N 64  
A1INN H26  H N N 65  
A1INN H27  H N N 66  
A1INN H28  H N N 67  
A1INN H29  H N N 68  
A1INN H30  H N N 69  
A1INN H32  H N N 70  
A1INN H31  H N N 71  
A1INN H33  H N N 72  
A1INN H34  H N N 73  
A1INN H35  H N N 74  
A1INN H36  H N N 75  
A1INN H37  H N N 76  
A1INN H38  H N N 77  
A1INN H40  H N N 78  
A1INN H39  H N N 79  
ALA   N    N N N 80  
ALA   CA   C N S 81  
ALA   C    C N N 82  
ALA   O    O N N 83  
ALA   CB   C N N 84  
ALA   OXT  O N N 85  
ALA   H    H N N 86  
ALA   H2   H N N 87  
ALA   HA   H N N 88  
ALA   HB1  H N N 89  
ALA   HB2  H N N 90  
ALA   HB3  H N N 91  
ALA   HXT  H N N 92  
ARG   N    N N N 93  
ARG   CA   C N S 94  
ARG   C    C N N 95  
ARG   O    O N N 96  
ARG   CB   C N N 97  
ARG   CG   C N N 98  
ARG   CD   C N N 99  
ARG   NE   N N N 100 
ARG   CZ   C N N 101 
ARG   NH1  N N N 102 
ARG   NH2  N N N 103 
ARG   OXT  O N N 104 
ARG   H    H N N 105 
ARG   H2   H N N 106 
ARG   HA   H N N 107 
ARG   HB2  H N N 108 
ARG   HB3  H N N 109 
ARG   HG2  H N N 110 
ARG   HG3  H N N 111 
ARG   HD2  H N N 112 
ARG   HD3  H N N 113 
ARG   HE   H N N 114 
ARG   HH11 H N N 115 
ARG   HH12 H N N 116 
ARG   HH21 H N N 117 
ARG   HH22 H N N 118 
ARG   HXT  H N N 119 
ASN   N    N N N 120 
ASN   CA   C N S 121 
ASN   C    C N N 122 
ASN   O    O N N 123 
ASN   CB   C N N 124 
ASN   CG   C N N 125 
ASN   OD1  O N N 126 
ASN   ND2  N N N 127 
ASN   OXT  O N N 128 
ASN   H    H N N 129 
ASN   H2   H N N 130 
ASN   HA   H N N 131 
ASN   HB2  H N N 132 
ASN   HB3  H N N 133 
ASN   HD21 H N N 134 
ASN   HD22 H N N 135 
ASN   HXT  H N N 136 
ASP   N    N N N 137 
ASP   CA   C N S 138 
ASP   C    C N N 139 
ASP   O    O N N 140 
ASP   CB   C N N 141 
ASP   CG   C N N 142 
ASP   OD1  O N N 143 
ASP   OD2  O N N 144 
ASP   OXT  O N N 145 
ASP   H    H N N 146 
ASP   H2   H N N 147 
ASP   HA   H N N 148 
ASP   HB2  H N N 149 
ASP   HB3  H N N 150 
ASP   HD2  H N N 151 
ASP   HXT  H N N 152 
CYS   N    N N N 153 
CYS   CA   C N R 154 
CYS   C    C N N 155 
CYS   O    O N N 156 
CYS   CB   C N N 157 
CYS   SG   S N N 158 
CYS   OXT  O N N 159 
CYS   H    H N N 160 
CYS   H2   H N N 161 
CYS   HA   H N N 162 
CYS   HB2  H N N 163 
CYS   HB3  H N N 164 
CYS   HG   H N N 165 
CYS   HXT  H N N 166 
GLN   N    N N N 167 
GLN   CA   C N S 168 
GLN   C    C N N 169 
GLN   O    O N N 170 
GLN   CB   C N N 171 
GLN   CG   C N N 172 
GLN   CD   C N N 173 
GLN   OE1  O N N 174 
GLN   NE2  N N N 175 
GLN   OXT  O N N 176 
GLN   H    H N N 177 
GLN   H2   H N N 178 
GLN   HA   H N N 179 
GLN   HB2  H N N 180 
GLN   HB3  H N N 181 
GLN   HG2  H N N 182 
GLN   HG3  H N N 183 
GLN   HE21 H N N 184 
GLN   HE22 H N N 185 
GLN   HXT  H N N 186 
GLU   N    N N N 187 
GLU   CA   C N S 188 
GLU   C    C N N 189 
GLU   O    O N N 190 
GLU   CB   C N N 191 
GLU   CG   C N N 192 
GLU   CD   C N N 193 
GLU   OE1  O N N 194 
GLU   OE2  O N N 195 
GLU   OXT  O N N 196 
GLU   H    H N N 197 
GLU   H2   H N N 198 
GLU   HA   H N N 199 
GLU   HB2  H N N 200 
GLU   HB3  H N N 201 
GLU   HG2  H N N 202 
GLU   HG3  H N N 203 
GLU   HE2  H N N 204 
GLU   HXT  H N N 205 
GLY   N    N N N 206 
GLY   CA   C N N 207 
GLY   C    C N N 208 
GLY   O    O N N 209 
GLY   OXT  O N N 210 
GLY   H    H N N 211 
GLY   H2   H N N 212 
GLY   HA2  H N N 213 
GLY   HA3  H N N 214 
GLY   HXT  H N N 215 
HIS   N    N N N 216 
HIS   CA   C N S 217 
HIS   C    C N N 218 
HIS   O    O N N 219 
HIS   CB   C N N 220 
HIS   CG   C Y N 221 
HIS   ND1  N Y N 222 
HIS   CD2  C Y N 223 
HIS   CE1  C Y N 224 
HIS   NE2  N Y N 225 
HIS   OXT  O N N 226 
HIS   H    H N N 227 
HIS   H2   H N N 228 
HIS   HA   H N N 229 
HIS   HB2  H N N 230 
HIS   HB3  H N N 231 
HIS   HD1  H N N 232 
HIS   HD2  H N N 233 
HIS   HE1  H N N 234 
HIS   HE2  H N N 235 
HIS   HXT  H N N 236 
HOH   O    O N N 237 
HOH   H1   H N N 238 
HOH   H2   H N N 239 
ILE   N    N N N 240 
ILE   CA   C N S 241 
ILE   C    C N N 242 
ILE   O    O N N 243 
ILE   CB   C N S 244 
ILE   CG1  C N N 245 
ILE   CG2  C N N 246 
ILE   CD1  C N N 247 
ILE   OXT  O N N 248 
ILE   H    H N N 249 
ILE   H2   H N N 250 
ILE   HA   H N N 251 
ILE   HB   H N N 252 
ILE   HG12 H N N 253 
ILE   HG13 H N N 254 
ILE   HG21 H N N 255 
ILE   HG22 H N N 256 
ILE   HG23 H N N 257 
ILE   HD11 H N N 258 
ILE   HD12 H N N 259 
ILE   HD13 H N N 260 
ILE   HXT  H N N 261 
LEU   N    N N N 262 
LEU   CA   C N S 263 
LEU   C    C N N 264 
LEU   O    O N N 265 
LEU   CB   C N N 266 
LEU   CG   C N N 267 
LEU   CD1  C N N 268 
LEU   CD2  C N N 269 
LEU   OXT  O N N 270 
LEU   H    H N N 271 
LEU   H2   H N N 272 
LEU   HA   H N N 273 
LEU   HB2  H N N 274 
LEU   HB3  H N N 275 
LEU   HG   H N N 276 
LEU   HD11 H N N 277 
LEU   HD12 H N N 278 
LEU   HD13 H N N 279 
LEU   HD21 H N N 280 
LEU   HD22 H N N 281 
LEU   HD23 H N N 282 
LEU   HXT  H N N 283 
LYS   N    N N N 284 
LYS   CA   C N S 285 
LYS   C    C N N 286 
LYS   O    O N N 287 
LYS   CB   C N N 288 
LYS   CG   C N N 289 
LYS   CD   C N N 290 
LYS   CE   C N N 291 
LYS   NZ   N N N 292 
LYS   OXT  O N N 293 
LYS   H    H N N 294 
LYS   H2   H N N 295 
LYS   HA   H N N 296 
LYS   HB2  H N N 297 
LYS   HB3  H N N 298 
LYS   HG2  H N N 299 
LYS   HG3  H N N 300 
LYS   HD2  H N N 301 
LYS   HD3  H N N 302 
LYS   HE2  H N N 303 
LYS   HE3  H N N 304 
LYS   HZ1  H N N 305 
LYS   HZ2  H N N 306 
LYS   HZ3  H N N 307 
LYS   HXT  H N N 308 
MET   N    N N N 309 
MET   CA   C N S 310 
MET   C    C N N 311 
MET   O    O N N 312 
MET   CB   C N N 313 
MET   CG   C N N 314 
MET   SD   S N N 315 
MET   CE   C N N 316 
MET   OXT  O N N 317 
MET   H    H N N 318 
MET   H2   H N N 319 
MET   HA   H N N 320 
MET   HB2  H N N 321 
MET   HB3  H N N 322 
MET   HG2  H N N 323 
MET   HG3  H N N 324 
MET   HE1  H N N 325 
MET   HE2  H N N 326 
MET   HE3  H N N 327 
MET   HXT  H N N 328 
PHE   N    N N N 329 
PHE   CA   C N S 330 
PHE   C    C N N 331 
PHE   O    O N N 332 
PHE   CB   C N N 333 
PHE   CG   C Y N 334 
PHE   CD1  C Y N 335 
PHE   CD2  C Y N 336 
PHE   CE1  C Y N 337 
PHE   CE2  C Y N 338 
PHE   CZ   C Y N 339 
PHE   OXT  O N N 340 
PHE   H    H N N 341 
PHE   H2   H N N 342 
PHE   HA   H N N 343 
PHE   HB2  H N N 344 
PHE   HB3  H N N 345 
PHE   HD1  H N N 346 
PHE   HD2  H N N 347 
PHE   HE1  H N N 348 
PHE   HE2  H N N 349 
PHE   HZ   H N N 350 
PHE   HXT  H N N 351 
PRO   N    N N N 352 
PRO   CA   C N S 353 
PRO   C    C N N 354 
PRO   O    O N N 355 
PRO   CB   C N N 356 
PRO   CG   C N N 357 
PRO   CD   C N N 358 
PRO   OXT  O N N 359 
PRO   H    H N N 360 
PRO   HA   H N N 361 
PRO   HB2  H N N 362 
PRO   HB3  H N N 363 
PRO   HG2  H N N 364 
PRO   HG3  H N N 365 
PRO   HD2  H N N 366 
PRO   HD3  H N N 367 
PRO   HXT  H N N 368 
SER   N    N N N 369 
SER   CA   C N S 370 
SER   C    C N N 371 
SER   O    O N N 372 
SER   CB   C N N 373 
SER   OG   O N N 374 
SER   OXT  O N N 375 
SER   H    H N N 376 
SER   H2   H N N 377 
SER   HA   H N N 378 
SER   HB2  H N N 379 
SER   HB3  H N N 380 
SER   HG   H N N 381 
SER   HXT  H N N 382 
THR   N    N N N 383 
THR   CA   C N S 384 
THR   C    C N N 385 
THR   O    O N N 386 
THR   CB   C N R 387 
THR   OG1  O N N 388 
THR   CG2  C N N 389 
THR   OXT  O N N 390 
THR   H    H N N 391 
THR   H2   H N N 392 
THR   HA   H N N 393 
THR   HB   H N N 394 
THR   HG1  H N N 395 
THR   HG21 H N N 396 
THR   HG22 H N N 397 
THR   HG23 H N N 398 
THR   HXT  H N N 399 
TRP   N    N N N 400 
TRP   CA   C N S 401 
TRP   C    C N N 402 
TRP   O    O N N 403 
TRP   CB   C N N 404 
TRP   CG   C Y N 405 
TRP   CD1  C Y N 406 
TRP   CD2  C Y N 407 
TRP   NE1  N Y N 408 
TRP   CE2  C Y N 409 
TRP   CE3  C Y N 410 
TRP   CZ2  C Y N 411 
TRP   CZ3  C Y N 412 
TRP   CH2  C Y N 413 
TRP   OXT  O N N 414 
TRP   H    H N N 415 
TRP   H2   H N N 416 
TRP   HA   H N N 417 
TRP   HB2  H N N 418 
TRP   HB3  H N N 419 
TRP   HD1  H N N 420 
TRP   HE1  H N N 421 
TRP   HE3  H N N 422 
TRP   HZ2  H N N 423 
TRP   HZ3  H N N 424 
TRP   HH2  H N N 425 
TRP   HXT  H N N 426 
TYR   N    N N N 427 
TYR   CA   C N S 428 
TYR   C    C N N 429 
TYR   O    O N N 430 
TYR   CB   C N N 431 
TYR   CG   C Y N 432 
TYR   CD1  C Y N 433 
TYR   CD2  C Y N 434 
TYR   CE1  C Y N 435 
TYR   CE2  C Y N 436 
TYR   CZ   C Y N 437 
TYR   OH   O N N 438 
TYR   OXT  O N N 439 
TYR   H    H N N 440 
TYR   H2   H N N 441 
TYR   HA   H N N 442 
TYR   HB2  H N N 443 
TYR   HB3  H N N 444 
TYR   HD1  H N N 445 
TYR   HD2  H N N 446 
TYR   HE1  H N N 447 
TYR   HE2  H N N 448 
TYR   HH   H N N 449 
TYR   HXT  H N N 450 
VAL   N    N N N 451 
VAL   CA   C N S 452 
VAL   C    C N N 453 
VAL   O    O N N 454 
VAL   CB   C N N 455 
VAL   CG1  C N N 456 
VAL   CG2  C N N 457 
VAL   OXT  O N N 458 
VAL   H    H N N 459 
VAL   H2   H N N 460 
VAL   HA   H N N 461 
VAL   HB   H N N 462 
VAL   HG11 H N N 463 
VAL   HG12 H N N 464 
VAL   HG13 H N N 465 
VAL   HG21 H N N 466 
VAL   HG22 H N N 467 
VAL   HG23 H N N 468 
VAL   HXT  H N N 469 
# 
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 
A1INN C18 C19  sing N N 1   
A1INN C18 C17  sing N N 2   
A1INN C26 C25  sing N N 3   
A1INN C26 C27  sing N N 4   
A1INN C19 C20  sing N N 5   
A1INN C25 C24  sing N N 6   
A1INN C20 C21  sing N N 7   
A1INN C17 N4   sing N N 8   
A1INN C17 C16  sing N N 9   
A1INN C27 C28  sing N N 10  
A1INN N4  C22  sing N N 11  
A1INN N4  C21  sing N N 12  
A1INN O6  C22  doub N N 13  
A1INN C22 C23  sing N N 14  
A1INN O5  C16  doub N N 15  
A1INN C16 O4   sing N N 16  
A1INN C24 C23  sing N N 17  
A1INN C24 C29  sing N N 18  
A1INN C23 C4   sing N N 19  
A1INN C28 C29  sing N N 20  
A1INN O4  C15  sing N N 21  
A1INN C4  C5   doub Y N 22  
A1INN C4  C3   sing Y N 23  
A1INN C5  C6   sing Y N 24  
A1INN C15 C14  sing N N 25  
A1INN C14 C13  sing N N 26  
A1INN C3  C2   doub Y N 27  
A1INN C13 C12  doub Y N 28  
A1INN C13 N2   sing Y N 29  
A1INN C7  O2   sing N N 30  
A1INN C12 N1   sing Y N 31  
A1INN C6  O2   sing N N 32  
A1INN C6  C8   doub Y N 33  
A1INN N2  N3   doub Y N 34  
A1INN C2  C8   sing Y N 35  
A1INN C2  O1   sing N N 36  
A1INN N1  N3   sing Y N 37  
A1INN N1  C11  sing N N 38  
A1INN C8  O3   sing N N 39  
A1INN C1  O1   sing N N 40  
A1INN C11 C10  sing N N 41  
A1INN O3  C9   sing N N 42  
A1INN C9  C10  sing N N 43  
A1INN C14 H17  sing N N 44  
A1INN C14 H16  sing N N 45  
A1INN C5  H5   sing N N 46  
A1INN C11 H14  sing N N 47  
A1INN C11 H13  sing N N 48  
A1INN C7  H7   sing N N 49  
A1INN C7  H8   sing N N 50  
A1INN C7  H6   sing N N 51  
A1INN C9  H9   sing N N 52  
A1INN C9  H10  sing N N 53  
A1INN C10 H12  sing N N 54  
A1INN C10 H11  sing N N 55  
A1INN C12 H15  sing N N 56  
A1INN C3  H4   sing N N 57  
A1INN C1  H2   sing N N 58  
A1INN C1  H3   sing N N 59  
A1INN C1  H1   sing N N 60  
A1INN C15 H19  sing N N 61  
A1INN C15 H18  sing N N 62  
A1INN C17 H20  sing N N 63  
A1INN C18 H22  sing N N 64  
A1INN C18 H21  sing N N 65  
A1INN C19 H23  sing N N 66  
A1INN C19 H24  sing N N 67  
A1INN C20 H25  sing N N 68  
A1INN C20 H26  sing N N 69  
A1INN C21 H27  sing N N 70  
A1INN C21 H28  sing N N 71  
A1INN C23 H29  sing N N 72  
A1INN C24 H30  sing N N 73  
A1INN C25 H32  sing N N 74  
A1INN C25 H31  sing N N 75  
A1INN C26 H33  sing N N 76  
A1INN C26 H34  sing N N 77  
A1INN C27 H35  sing N N 78  
A1INN C27 H36  sing N N 79  
A1INN C28 H37  sing N N 80  
A1INN C28 H38  sing N N 81  
A1INN C29 H40  sing N N 82  
A1INN C29 H39  sing N N 83  
ALA   N   CA   sing N N 84  
ALA   N   H    sing N N 85  
ALA   N   H2   sing N N 86  
ALA   CA  C    sing N N 87  
ALA   CA  CB   sing N N 88  
ALA   CA  HA   sing N N 89  
ALA   C   O    doub N N 90  
ALA   C   OXT  sing N N 91  
ALA   CB  HB1  sing N N 92  
ALA   CB  HB2  sing N N 93  
ALA   CB  HB3  sing N N 94  
ALA   OXT HXT  sing N N 95  
ARG   N   CA   sing N N 96  
ARG   N   H    sing N N 97  
ARG   N   H2   sing N N 98  
ARG   CA  C    sing N N 99  
ARG   CA  CB   sing N N 100 
ARG   CA  HA   sing N N 101 
ARG   C   O    doub N N 102 
ARG   C   OXT  sing N N 103 
ARG   CB  CG   sing N N 104 
ARG   CB  HB2  sing N N 105 
ARG   CB  HB3  sing N N 106 
ARG   CG  CD   sing N N 107 
ARG   CG  HG2  sing N N 108 
ARG   CG  HG3  sing N N 109 
ARG   CD  NE   sing N N 110 
ARG   CD  HD2  sing N N 111 
ARG   CD  HD3  sing N N 112 
ARG   NE  CZ   sing N N 113 
ARG   NE  HE   sing N N 114 
ARG   CZ  NH1  sing N N 115 
ARG   CZ  NH2  doub N N 116 
ARG   NH1 HH11 sing N N 117 
ARG   NH1 HH12 sing N N 118 
ARG   NH2 HH21 sing N N 119 
ARG   NH2 HH22 sing N N 120 
ARG   OXT HXT  sing N N 121 
ASN   N   CA   sing N N 122 
ASN   N   H    sing N N 123 
ASN   N   H2   sing N N 124 
ASN   CA  C    sing N N 125 
ASN   CA  CB   sing N N 126 
ASN   CA  HA   sing N N 127 
ASN   C   O    doub N N 128 
ASN   C   OXT  sing N N 129 
ASN   CB  CG   sing N N 130 
ASN   CB  HB2  sing N N 131 
ASN   CB  HB3  sing N N 132 
ASN   CG  OD1  doub N N 133 
ASN   CG  ND2  sing N N 134 
ASN   ND2 HD21 sing N N 135 
ASN   ND2 HD22 sing N N 136 
ASN   OXT HXT  sing N N 137 
ASP   N   CA   sing N N 138 
ASP   N   H    sing N N 139 
ASP   N   H2   sing N N 140 
ASP   CA  C    sing N N 141 
ASP   CA  CB   sing N N 142 
ASP   CA  HA   sing N N 143 
ASP   C   O    doub N N 144 
ASP   C   OXT  sing N N 145 
ASP   CB  CG   sing N N 146 
ASP   CB  HB2  sing N N 147 
ASP   CB  HB3  sing N N 148 
ASP   CG  OD1  doub N N 149 
ASP   CG  OD2  sing N N 150 
ASP   OD2 HD2  sing N N 151 
ASP   OXT HXT  sing N N 152 
CYS   N   CA   sing N N 153 
CYS   N   H    sing N N 154 
CYS   N   H2   sing N N 155 
CYS   CA  C    sing N N 156 
CYS   CA  CB   sing N N 157 
CYS   CA  HA   sing N N 158 
CYS   C   O    doub N N 159 
CYS   C   OXT  sing N N 160 
CYS   CB  SG   sing N N 161 
CYS   CB  HB2  sing N N 162 
CYS   CB  HB3  sing N N 163 
CYS   SG  HG   sing N N 164 
CYS   OXT HXT  sing N N 165 
GLN   N   CA   sing N N 166 
GLN   N   H    sing N N 167 
GLN   N   H2   sing N N 168 
GLN   CA  C    sing N N 169 
GLN   CA  CB   sing N N 170 
GLN   CA  HA   sing N N 171 
GLN   C   O    doub N N 172 
GLN   C   OXT  sing N N 173 
GLN   CB  CG   sing N N 174 
GLN   CB  HB2  sing N N 175 
GLN   CB  HB3  sing N N 176 
GLN   CG  CD   sing N N 177 
GLN   CG  HG2  sing N N 178 
GLN   CG  HG3  sing N N 179 
GLN   CD  OE1  doub N N 180 
GLN   CD  NE2  sing N N 181 
GLN   NE2 HE21 sing N N 182 
GLN   NE2 HE22 sing N N 183 
GLN   OXT HXT  sing N N 184 
GLU   N   CA   sing N N 185 
GLU   N   H    sing N N 186 
GLU   N   H2   sing N N 187 
GLU   CA  C    sing N N 188 
GLU   CA  CB   sing N N 189 
GLU   CA  HA   sing N N 190 
GLU   C   O    doub N N 191 
GLU   C   OXT  sing N N 192 
GLU   CB  CG   sing N N 193 
GLU   CB  HB2  sing N N 194 
GLU   CB  HB3  sing N N 195 
GLU   CG  CD   sing N N 196 
GLU   CG  HG2  sing N N 197 
GLU   CG  HG3  sing N N 198 
GLU   CD  OE1  doub N N 199 
GLU   CD  OE2  sing N N 200 
GLU   OE2 HE2  sing N N 201 
GLU   OXT HXT  sing N N 202 
GLY   N   CA   sing N N 203 
GLY   N   H    sing N N 204 
GLY   N   H2   sing N N 205 
GLY   CA  C    sing N N 206 
GLY   CA  HA2  sing N N 207 
GLY   CA  HA3  sing N N 208 
GLY   C   O    doub N N 209 
GLY   C   OXT  sing N N 210 
GLY   OXT HXT  sing N N 211 
HIS   N   CA   sing N N 212 
HIS   N   H    sing N N 213 
HIS   N   H2   sing N N 214 
HIS   CA  C    sing N N 215 
HIS   CA  CB   sing N N 216 
HIS   CA  HA   sing N N 217 
HIS   C   O    doub N N 218 
HIS   C   OXT  sing N N 219 
HIS   CB  CG   sing N N 220 
HIS   CB  HB2  sing N N 221 
HIS   CB  HB3  sing N N 222 
HIS   CG  ND1  sing Y N 223 
HIS   CG  CD2  doub Y N 224 
HIS   ND1 CE1  doub Y N 225 
HIS   ND1 HD1  sing N N 226 
HIS   CD2 NE2  sing Y N 227 
HIS   CD2 HD2  sing N N 228 
HIS   CE1 NE2  sing Y N 229 
HIS   CE1 HE1  sing N N 230 
HIS   NE2 HE2  sing N N 231 
HIS   OXT HXT  sing N N 232 
HOH   O   H1   sing N N 233 
HOH   O   H2   sing N N 234 
ILE   N   CA   sing N N 235 
ILE   N   H    sing N N 236 
ILE   N   H2   sing N N 237 
ILE   CA  C    sing N N 238 
ILE   CA  CB   sing N N 239 
ILE   CA  HA   sing N N 240 
ILE   C   O    doub N N 241 
ILE   C   OXT  sing N N 242 
ILE   CB  CG1  sing N N 243 
ILE   CB  CG2  sing N N 244 
ILE   CB  HB   sing N N 245 
ILE   CG1 CD1  sing N N 246 
ILE   CG1 HG12 sing N N 247 
ILE   CG1 HG13 sing N N 248 
ILE   CG2 HG21 sing N N 249 
ILE   CG2 HG22 sing N N 250 
ILE   CG2 HG23 sing N N 251 
ILE   CD1 HD11 sing N N 252 
ILE   CD1 HD12 sing N N 253 
ILE   CD1 HD13 sing N N 254 
ILE   OXT HXT  sing N N 255 
LEU   N   CA   sing N N 256 
LEU   N   H    sing N N 257 
LEU   N   H2   sing N N 258 
LEU   CA  C    sing N N 259 
LEU   CA  CB   sing N N 260 
LEU   CA  HA   sing N N 261 
LEU   C   O    doub N N 262 
LEU   C   OXT  sing N N 263 
LEU   CB  CG   sing N N 264 
LEU   CB  HB2  sing N N 265 
LEU   CB  HB3  sing N N 266 
LEU   CG  CD1  sing N N 267 
LEU   CG  CD2  sing N N 268 
LEU   CG  HG   sing N N 269 
LEU   CD1 HD11 sing N N 270 
LEU   CD1 HD12 sing N N 271 
LEU   CD1 HD13 sing N N 272 
LEU   CD2 HD21 sing N N 273 
LEU   CD2 HD22 sing N N 274 
LEU   CD2 HD23 sing N N 275 
LEU   OXT HXT  sing N N 276 
LYS   N   CA   sing N N 277 
LYS   N   H    sing N N 278 
LYS   N   H2   sing N N 279 
LYS   CA  C    sing N N 280 
LYS   CA  CB   sing N N 281 
LYS   CA  HA   sing N N 282 
LYS   C   O    doub N N 283 
LYS   C   OXT  sing N N 284 
LYS   CB  CG   sing N N 285 
LYS   CB  HB2  sing N N 286 
LYS   CB  HB3  sing N N 287 
LYS   CG  CD   sing N N 288 
LYS   CG  HG2  sing N N 289 
LYS   CG  HG3  sing N N 290 
LYS   CD  CE   sing N N 291 
LYS   CD  HD2  sing N N 292 
LYS   CD  HD3  sing N N 293 
LYS   CE  NZ   sing N N 294 
LYS   CE  HE2  sing N N 295 
LYS   CE  HE3  sing N N 296 
LYS   NZ  HZ1  sing N N 297 
LYS   NZ  HZ2  sing N N 298 
LYS   NZ  HZ3  sing N N 299 
LYS   OXT HXT  sing N N 300 
MET   N   CA   sing N N 301 
MET   N   H    sing N N 302 
MET   N   H2   sing N N 303 
MET   CA  C    sing N N 304 
MET   CA  CB   sing N N 305 
MET   CA  HA   sing N N 306 
MET   C   O    doub N N 307 
MET   C   OXT  sing N N 308 
MET   CB  CG   sing N N 309 
MET   CB  HB2  sing N N 310 
MET   CB  HB3  sing N N 311 
MET   CG  SD   sing N N 312 
MET   CG  HG2  sing N N 313 
MET   CG  HG3  sing N N 314 
MET   SD  CE   sing N N 315 
MET   CE  HE1  sing N N 316 
MET   CE  HE2  sing N N 317 
MET   CE  HE3  sing N N 318 
MET   OXT HXT  sing N N 319 
PHE   N   CA   sing N N 320 
PHE   N   H    sing N N 321 
PHE   N   H2   sing N N 322 
PHE   CA  C    sing N N 323 
PHE   CA  CB   sing N N 324 
PHE   CA  HA   sing N N 325 
PHE   C   O    doub N N 326 
PHE   C   OXT  sing N N 327 
PHE   CB  CG   sing N N 328 
PHE   CB  HB2  sing N N 329 
PHE   CB  HB3  sing N N 330 
PHE   CG  CD1  doub Y N 331 
PHE   CG  CD2  sing Y N 332 
PHE   CD1 CE1  sing Y N 333 
PHE   CD1 HD1  sing N N 334 
PHE   CD2 CE2  doub Y N 335 
PHE   CD2 HD2  sing N N 336 
PHE   CE1 CZ   doub Y N 337 
PHE   CE1 HE1  sing N N 338 
PHE   CE2 CZ   sing Y N 339 
PHE   CE2 HE2  sing N N 340 
PHE   CZ  HZ   sing N N 341 
PHE   OXT HXT  sing N N 342 
PRO   N   CA   sing N N 343 
PRO   N   CD   sing N N 344 
PRO   N   H    sing N N 345 
PRO   CA  C    sing N N 346 
PRO   CA  CB   sing N N 347 
PRO   CA  HA   sing N N 348 
PRO   C   O    doub N N 349 
PRO   C   OXT  sing N N 350 
PRO   CB  CG   sing N N 351 
PRO   CB  HB2  sing N N 352 
PRO   CB  HB3  sing N N 353 
PRO   CG  CD   sing N N 354 
PRO   CG  HG2  sing N N 355 
PRO   CG  HG3  sing N N 356 
PRO   CD  HD2  sing N N 357 
PRO   CD  HD3  sing N N 358 
PRO   OXT HXT  sing N N 359 
SER   N   CA   sing N N 360 
SER   N   H    sing N N 361 
SER   N   H2   sing N N 362 
SER   CA  C    sing N N 363 
SER   CA  CB   sing N N 364 
SER   CA  HA   sing N N 365 
SER   C   O    doub N N 366 
SER   C   OXT  sing N N 367 
SER   CB  OG   sing N N 368 
SER   CB  HB2  sing N N 369 
SER   CB  HB3  sing N N 370 
SER   OG  HG   sing N N 371 
SER   OXT HXT  sing N N 372 
THR   N   CA   sing N N 373 
THR   N   H    sing N N 374 
THR   N   H2   sing N N 375 
THR   CA  C    sing N N 376 
THR   CA  CB   sing N N 377 
THR   CA  HA   sing N N 378 
THR   C   O    doub N N 379 
THR   C   OXT  sing N N 380 
THR   CB  OG1  sing N N 381 
THR   CB  CG2  sing N N 382 
THR   CB  HB   sing N N 383 
THR   OG1 HG1  sing N N 384 
THR   CG2 HG21 sing N N 385 
THR   CG2 HG22 sing N N 386 
THR   CG2 HG23 sing N N 387 
THR   OXT HXT  sing N N 388 
TRP   N   CA   sing N N 389 
TRP   N   H    sing N N 390 
TRP   N   H2   sing N N 391 
TRP   CA  C    sing N N 392 
TRP   CA  CB   sing N N 393 
TRP   CA  HA   sing N N 394 
TRP   C   O    doub N N 395 
TRP   C   OXT  sing N N 396 
TRP   CB  CG   sing N N 397 
TRP   CB  HB2  sing N N 398 
TRP   CB  HB3  sing N N 399 
TRP   CG  CD1  doub Y N 400 
TRP   CG  CD2  sing Y N 401 
TRP   CD1 NE1  sing Y N 402 
TRP   CD1 HD1  sing N N 403 
TRP   CD2 CE2  doub Y N 404 
TRP   CD2 CE3  sing Y N 405 
TRP   NE1 CE2  sing Y N 406 
TRP   NE1 HE1  sing N N 407 
TRP   CE2 CZ2  sing Y N 408 
TRP   CE3 CZ3  doub Y N 409 
TRP   CE3 HE3  sing N N 410 
TRP   CZ2 CH2  doub Y N 411 
TRP   CZ2 HZ2  sing N N 412 
TRP   CZ3 CH2  sing Y N 413 
TRP   CZ3 HZ3  sing N N 414 
TRP   CH2 HH2  sing N N 415 
TRP   OXT HXT  sing N N 416 
TYR   N   CA   sing N N 417 
TYR   N   H    sing N N 418 
TYR   N   H2   sing N N 419 
TYR   CA  C    sing N N 420 
TYR   CA  CB   sing N N 421 
TYR   CA  HA   sing N N 422 
TYR   C   O    doub N N 423 
TYR   C   OXT  sing N N 424 
TYR   CB  CG   sing N N 425 
TYR   CB  HB2  sing N N 426 
TYR   CB  HB3  sing N N 427 
TYR   CG  CD1  doub Y N 428 
TYR   CG  CD2  sing Y N 429 
TYR   CD1 CE1  sing Y N 430 
TYR   CD1 HD1  sing N N 431 
TYR   CD2 CE2  doub Y N 432 
TYR   CD2 HD2  sing N N 433 
TYR   CE1 CZ   doub Y N 434 
TYR   CE1 HE1  sing N N 435 
TYR   CE2 CZ   sing Y N 436 
TYR   CE2 HE2  sing N N 437 
TYR   CZ  OH   sing N N 438 
TYR   OH  HH   sing N N 439 
TYR   OXT HXT  sing N N 440 
VAL   N   CA   sing N N 441 
VAL   N   H    sing N N 442 
VAL   N   H2   sing N N 443 
VAL   CA  C    sing N N 444 
VAL   CA  CB   sing N N 445 
VAL   CA  HA   sing N N 446 
VAL   C   O    doub N N 447 
VAL   C   OXT  sing N N 448 
VAL   CB  CG1  sing N N 449 
VAL   CB  CG2  sing N N 450 
VAL   CB  HB   sing N N 451 
VAL   CG1 HG11 sing N N 452 
VAL   CG1 HG12 sing N N 453 
VAL   CG1 HG13 sing N N 454 
VAL   CG2 HG21 sing N N 455 
VAL   CG2 HG22 sing N N 456 
VAL   CG2 HG23 sing N N 457 
VAL   OXT HXT  sing N N 458 
# 
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                    9GPN 
_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]   0.020436 
_atom_sites.fract_transf_matrix[1][2]   0.011799 
_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]   0.023598 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005137 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C 6  6  2.3103  20.8439 1.0201 10.2075 1.5888 0.5687  0.8651 51.6512 0.2156   
H 1  1  0.4930  10.5109 0.3229 26.1257 0.1402 3.1424  0.0408 57.7997 0.0030   
N 7  7  12.2220 0.0057  3.1346 9.8933  2.0141 28.9975 1.1672 0.5826  -11.5379 
O 8  8  3.0487  13.2771 2.2870 5.7011  1.5464 0.3239  0.8671 32.9089 0.2508   
S 16 16 6.9054  1.4679  5.2035 22.2151 1.4379 0.2536  1.5863 56.1720 1.0316   
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
_atom_site.calc_flag 
_atom_site.pdbx_tls_group_id 
ATOM   1    N N    . GLY   A 1 1   ? -5.468  0.031  -3.719  1   48.239 ? 13  GLY   A N    1 ? 1 
ATOM   2    C CA   . GLY   A 1 1   ? -6.745  0.677  -3.361  1   47.083 ? 13  GLY   A CA   1 ? 1 
ATOM   3    C C    . GLY   A 1 1   ? -6.623  2.197  -3.358  1   43.111 ? 13  GLY   A C    1 ? 1 
ATOM   4    O O    . GLY   A 1 1   ? -5.717  2.755  -3.977  1   42.287 ? 13  GLY   A O    1 ? 1 
ATOM   5    H H1   . GLY   A 1 1   ? -5.594  -0.858 -3.837  1   50.244 ? 13  GLY   A H1   1 c 1 
ATOM   6    H H2   . GLY   A 1 1   ? -4.863  0.156  -3.058  1   47.364 ? 13  GLY   A H2   1 c 1 
ATOM   7    H H3   . GLY   A 1 1   ? -5.144  0.386  -4.486  1   47.817 ? 13  GLY   A H3   1 c 1 
ATOM   8    H HA2  . GLY   A 1 1   ? -7.437  0.404  -4.009  1   48.173 ? 13  GLY   A HA2  1 c 1 
ATOM   9    H HA3  . GLY   A 1 1   ? -7.024  0.365  -2.468  1   47.202 ? 13  GLY   A HA3  1 c 1 
ATOM   10   N N    . ALA   A 1 2   ? -7.567  2.841  -2.669  1   41.112 ? 14  ALA   A N    1 ? 1 
ATOM   11   C CA   . ALA   A 1 2   ? -7.779  4.273  -2.807  1   39.75  ? 14  ALA   A CA   1 ? 1 
ATOM   12   C C    . ALA   A 1 2   ? -6.505  5.045  -2.477  1   37.434 ? 14  ALA   A C    1 ? 1 
ATOM   13   O O    . ALA   A 1 2   ? -6.116  5.921  -3.249  1   35.25  ? 14  ALA   A O    1 ? 1 
ATOM   14   C CB   . ALA   A 1 2   ? -8.959  4.72   -1.96   1   38.524 ? 14  ALA   A CB   1 ? 1 
ATOM   15   H H    . ALA   A 1 2   ? -8.098  2.372  -2.091  1   42.407 ? 14  ALA   A H    1 c 1 
ATOM   16   H HA   . ALA   A 1 2   ? -7.996  4.451  -3.764  1   39.73  ? 14  ALA   A HA   1 c 1 
ATOM   17   H HB1  . ALA   A 1 2   ? -9.783  4.368  -2.336  1   40.062 ? 14  ALA   A HB1  1 c 1 
ATOM   18   H HB2  . ALA   A 1 2   ? -8.859  4.393  -1.052  1   38.841 ? 14  ALA   A HB2  1 c 1 
ATOM   19   H HB3  . ALA   A 1 2   ? -9.003  5.691  -1.949  1   37.352 ? 14  ALA   A HB3  1 c 1 
ATOM   20   N N    . PRO   A 1 3   ? -5.827  4.806  -1.324  1   36.354 ? 15  PRO   A N    1 ? 1 
ATOM   21   C CA   . PRO   A 1 3   ? -4.61   5.557  -0.995  1   36.28  ? 15  PRO   A CA   1 ? 1 
ATOM   22   C C    . PRO   A 1 3   ? -3.53   5.53   -2.092  1   34.525 ? 15  PRO   A C    1 ? 1 
ATOM   23   O O    . PRO   A 1 3   ? -2.964  6.562  -2.441  1   31.248 ? 15  PRO   A O    1 ? 1 
ATOM   24   C CB   . PRO   A 1 3   ? -4.132  4.889  0.31    1   37     ? 15  PRO   A CB   1 ? 1 
ATOM   25   C CG   . PRO   A 1 3   ? -5.442  4.452  0.932   1   37.464 ? 15  PRO   A CG   1 ? 1 
ATOM   26   C CD   . PRO   A 1 3   ? -6.223  3.897  -0.238  1   38.494 ? 15  PRO   A CD   1 ? 1 
ATOM   27   H HA   . PRO   A 1 3   ? -4.852  6.488  -0.807  1   34.417 ? 15  PRO   A HA   1 c 1 
ATOM   28   H HB2  . PRO   A 1 3   ? -3.554  4.124  0.125   1   37.921 ? 15  PRO   A HB2  1 c 1 
ATOM   29   H HB3  . PRO   A 1 3   ? -3.663  5.527  0.882   1   35.668 ? 15  PRO   A HB3  1 c 1 
ATOM   30   H HG2  . PRO   A 1 3   ? -5.297  3.764  1.612   1   38.357 ? 15  PRO   A HG2  1 c 1 
ATOM   31   H HG3  . PRO   A 1 3   ? -5.91   5.209  1.337   1   36.417 ? 15  PRO   A HG3  1 c 1 
ATOM   32   H HD2  . PRO   A 1 3   ? -5.964  2.977  -0.44   1   39.864 ? 15  PRO   A HD2  1 c 1 
ATOM   33   H HD3  . PRO   A 1 3   ? -7.181  3.936  -0.075  1   38.702 ? 15  PRO   A HD3  1 c 1 
ATOM   34   N N    . ALA   A 1 4   ? -3.251  4.341  -2.63   1   33.964 ? 16  ALA   A N    1 ? 1 
ATOM   35   C CA   . ALA   A 1 4   ? -2.248  4.209  -3.673  1   35.742 ? 16  ALA   A CA   1 ? 1 
ATOM   36   C C    . ALA   A 1 4   ? -2.674  4.994  -4.919  1   35.717 ? 16  ALA   A C    1 ? 1 
ATOM   37   O O    . ALA   A 1 4   ? -1.818  5.549  -5.612  1   33.355 ? 16  ALA   A O    1 ? 1 
ATOM   38   C CB   . ALA   A 1 4   ? -1.997  2.74   -3.992  1   37.479 ? 16  ALA   A CB   1 ? 1 
ATOM   39   H H    . ALA   A 1 4   ? -3.691  3.594  -2.339  1   35.908 ? 16  ALA   A H    1 c 1 
ATOM   40   H HA   . ALA   A 1 4   ? -1.401  4.611  -3.334  1   34.628 ? 16  ALA   A HA   1 c 1 
ATOM   41   H HB1  . ALA   A 1 4   ? -1.692  2.279  -3.193  1   38.06  ? 16  ALA   A HB1  1 c 1 
ATOM   42   H HB2  . ALA   A 1 4   ? -2.819  2.328  -4.307  1   38.701 ? 16  ALA   A HB2  1 c 1 
ATOM   43   H HB3  . ALA   A 1 4   ? -1.316  2.668  -4.683  1   38.339 ? 16  ALA   A HB3  1 c 1 
ATOM   44   N N    . THR   A 1 5   ? -3.989  5.034  -5.206  1   35.967 ? 17  THR   A N    1 ? 1 
ATOM   45   C CA   . THR   A 1 5   ? -4.48   5.737  -6.382  1   34.948 ? 17  THR   A CA   1 ? 1 
ATOM   46   C C    . THR   A 1 5   ? -4.262  7.242  -6.22   1   32.468 ? 17  THR   A C    1 ? 1 
ATOM   47   O O    . THR   A 1 5   ? -4.01   7.943  -7.197  1   31.602 ? 17  THR   A O    1 ? 1 
ATOM   48   C CB   . THR   A 1 5   ? -5.947  5.402  -6.664  1   36.946 ? 17  THR   A CB   1 ? 1 
ATOM   49   O OG1  . THR   A 1 5   ? -5.943  4.012  -6.98   1   38.214 ? 17  THR   A OG1  1 ? 1 
ATOM   50   C CG2  . THR   A 1 5   ? -6.525  6.125  -7.874  1   36.607 ? 17  THR   A CG2  1 ? 1 
ATOM   51   H H    . THR   A 1 5   ? -4.587  4.608  -4.663  1   36.111 ? 17  THR   A H    1 c 1 
ATOM   52   H HA   . THR   A 1 5   ? -3.95   5.436  -7.153  1   36.197 ? 17  THR   A HA   1 c 1 
ATOM   53   H HB   . THR   A 1 5   ? -6.503  5.564  -5.865  1   35.805 ? 17  THR   A HB   1 c 1 
ATOM   54   H HG1  . THR   A 1 5   ? -5.439  3.907  -7.658  0   30     ? 17  THR   A HG1  1 c 1 
ATOM   55   H HG21 . THR   A 1 5   ? -7.377  5.724  -8.116  1   37.927 ? 17  THR   A HG21 1 c 1 
ATOM   56   H HG22 . THR   A 1 5   ? -5.909  6.049  -8.622  1   37.394 ? 17  THR   A HG22 1 c 1 
ATOM   57   H HG23 . THR   A 1 5   ? -6.659  7.064  -7.66   1   35.497 ? 17  THR   A HG23 1 c 1 
ATOM   58   N N    . VAL   A 1 6   ? -4.377  7.75   -4.984  1   27.966 ? 18  VAL   A N    1 ? 1 
ATOM   59   C CA   . VAL   A 1 6   ? -4.147  9.16   -4.752  1   26.915 ? 18  VAL   A CA   1 ? 1 
ATOM   60   C C    . VAL   A 1 6   ? -2.652  9.462  -4.885  1   26.99  ? 18  VAL   A C    1 ? 1 
ATOM   61   O O    . VAL   A 1 6   ? -2.282  10.481 -5.462  1   25.931 ? 18  VAL   A O    1 ? 1 
ATOM   62   C CB   . VAL   A 1 6   ? -4.623  9.617  -3.357  1   26.227 ? 18  VAL   A CB   1 ? 1 
ATOM   63   C CG1  . VAL   A 1 6   ? -4.286  11.088 -3.174  1   24.579 ? 18  VAL   A CG1  1 ? 1 
ATOM   64   C CG2  . VAL   A 1 6   ? -6.108  9.331  -3.141  1   27.292 ? 18  VAL   A CG2  1 ? 1 
ATOM   65   H H    . VAL   A 1 6   ? -4.602  7.21   -4.281  1   28.972 ? 18  VAL   A H    1 c 1 
ATOM   66   H HA   . VAL   A 1 6   ? -4.63   9.67   -5.427  1   27.186 ? 18  VAL   A HA   1 c 1 
ATOM   67   H HB   . VAL   A 1 6   ? -4.112  9.101  -2.69   1   26.104 ? 18  VAL   A HB   1 c 1 
ATOM   68   H HG11 . VAL   A 1 6   ? -4.43   11.563 -4.011  1   24.96  ? 18  VAL   A HG11 1 c 1 
ATOM   69   H HG12 . VAL   A 1 6   ? -3.357  11.179 -2.907  1   24.337 ? 18  VAL   A HG12 1 c 1 
ATOM   70   H HG13 . VAL   A 1 6   ? -4.857  11.469 -2.486  1   24.212 ? 18  VAL   A HG13 1 c 1 
ATOM   71   H HG21 . VAL   A 1 6   ? -6.384  9.686  -2.28   1   26.489 ? 18  VAL   A HG21 1 c 1 
ATOM   72   H HG22 . VAL   A 1 6   ? -6.262  8.374  -3.16   1   28.123 ? 18  VAL   A HG22 1 c 1 
ATOM   73   H HG23 . VAL   A 1 6   ? -6.625  9.756  -3.846  1   27.412 ? 18  VAL   A HG23 1 c 1 
ATOM   74   N N    . THR   A 1 7   ? -1.796  8.575  -4.36   1   27.497 ? 19  THR   A N    1 ? 1 
ATOM   75   C CA   . THR   A 1 7   ? -0.353  8.725  -4.53   1   29.314 ? 19  THR   A CA   1 ? 1 
ATOM   76   C C    . THR   A 1 7   ? -0.017  8.86   -6.023  1   29.597 ? 19  THR   A C    1 ? 1 
ATOM   77   O O    . THR   A 1 7   ? 0.722   9.756  -6.42   1   28.208 ? 19  THR   A O    1 ? 1 
ATOM   78   C CB   . THR   A 1 7   ? 0.376   7.54   -3.904  1   31.993 ? 19  THR   A CB   1 ? 1 
ATOM   79   O OG1  . THR   A 1 7   ? 0.21    7.738  -2.498  1   32.637 ? 19  THR   A OG1  1 ? 1 
ATOM   80   C CG2  . THR   A 1 7   ? 1.834   7.478  -4.322  1   34.274 ? 19  THR   A CG2  1 ? 1 
ATOM   81   H H    . THR   A 1 7   ? -2.115  7.865  -3.88   1   28.246 ? 19  THR   A H    1 c 1 
ATOM   82   H HA   . THR   A 1 7   ? -0.071  9.545  -4.069  1   28.167 ? 19  THR   A HA   1 c 1 
ATOM   83   H HB   . THR   A 1 7   ? -0.068  6.699  -4.168  1   33.251 ? 19  THR   A HB   1 c 1 
ATOM   84   H HG1  . THR   A 1 7   ? 0.524   8.541  -2.308  0   30     ? 19  THR   A HG1  1 c 1 
ATOM   85   H HG21 . THR   A 1 7   ? 2.33    6.936  -3.685  1   34.181 ? 19  THR   A HG21 1 c 1 
ATOM   86   H HG22 . THR   A 1 7   ? 2.206   8.376  -4.341  1   33.03  ? 19  THR   A HG22 1 c 1 
ATOM   87   H HG23 . THR   A 1 7   ? 1.903   7.079  -5.206  1   34.924 ? 19  THR   A HG23 1 c 1 
ATOM   88   N N    . GLU   A 1 8   ? -0.59   7.986  -6.835  1   30.93  ? 20  GLU   A N    1 ? 1 
ATOM   89   C CA   . GLU   A 1 8   ? -0.242  7.887  -8.252  1   33.954 ? 20  GLU   A CA   1 ? 1 
ATOM   90   C C    . GLU   A 1 8   ? -0.851  9.02   -9.084  1   33.043 ? 20  GLU   A C    1 ? 1 
ATOM   91   O O    . GLU   A 1 8   ? -0.207  9.457  -10.044 1   33.038 ? 20  GLU   A O    1 ? 1 
ATOM   92   C CB   . GLU   A 1 8   ? -0.706  6.547  -8.834  1   38.983 ? 20  GLU   A CB   1 ? 1 
ATOM   93   C CG   . GLU   A 1 8   ? 0.021   5.336  -8.244  1   46.123 ? 20  GLU   A CG   1 ? 1 
ATOM   94   C CD   . GLU   A 1 8   ? -0.593  3.95   -8.486  1   54.553 ? 20  GLU   A CD   1 ? 1 
ATOM   95   O OE1  . GLU   A 1 8   ? -1.665  3.8    -9.14   1   55.494 ? 20  GLU   A OE1  1 ? 1 
ATOM   96   O OE2  . GLU   A 1 8   ? 0.016   2.985  -7.961  1   59.537 ? 20  GLU   A OE2  1 ? 1 
ATOM   97   H H    . GLU   A 1 8   ? -1.224  7.418  -6.502  1   31.52  ? 20  GLU   A H    1 c 1 
ATOM   98   H HA   . GLU   A 1 8   ? 0.745   7.935  -8.332  1   34.316 ? 20  GLU   A HA   1 c 1 
ATOM   99   H HB2  . GLU   A 1 8   ? -1.668  6.451  -8.673  1   39.349 ? 20  GLU   A HB2  1 c 1 
ATOM   100  H HB3  . GLU   A 1 8   ? -0.566  6.559  -9.804  1   40.528 ? 20  GLU   A HB3  1 c 1 
ATOM   101  H HG2  . GLU   A 1 8   ? 0.935   5.324  -8.6    1   46.46  ? 20  GLU   A HG2  1 c 1 
ATOM   102  H HG3  . GLU   A 1 8   ? 0.102   5.464  -7.276  1   44.629 ? 20  GLU   A HG3  1 c 1 
ATOM   103  N N    . GLN   A 1 9   ? -2.088  9.457  -8.76   1   29.681 ? 21  GLN   A N    1 ? 1 
ATOM   104  C CA   . GLN   A 1 9   ? -2.898  10.25  -9.672  1   29.423 ? 21  GLN   A CA   1 ? 1 
ATOM   105  C C    . GLN   A 1 9   ? -3.375  11.568 -9.069  1   27.559 ? 21  GLN   A C    1 ? 1 
ATOM   106  O O    . GLN   A 1 9   ? -3.948  12.38  -9.798  1   28.635 ? 21  GLN   A O    1 ? 1 
ATOM   107  C CB   . GLN   A 1 9   ? -4.166  9.517  -10.111 1   31.696 ? 21  GLN   A CB   1 ? 1 
ATOM   108  C CG   . GLN   A 1 9   ? -3.848  8.161  -10.729 1   35.315 ? 21  GLN   A CG   1 ? 1 
ATOM   109  C CD   . GLN   A 1 9   ? -5.06   7.335  -11.075 1   37.367 ? 21  GLN   A CD   1 ? 1 
ATOM   110  O OE1  . GLN   A 1 9   ? -6.202  7.807  -11.115 1   36.522 ? 21  GLN   A OE1  1 ? 1 
ATOM   111  N NE2  . GLN   A 1 9   ? -4.793  6.07   -11.342 1   41.609 ? 21  GLN   A NE2  1 ? 1 
ATOM   112  H H    . GLN   A 1 9   ? -2.441  9.228  -7.949  1   29.426 ? 21  GLN   A H    1 c 1 
ATOM   113  H HA   . GLN   A 1 9   ? -2.359  10.452 -10.478 1   30.49  ? 21  GLN   A HA   1 c 1 
ATOM   114  H HB2  . GLN   A 1 9   ? -4.751  9.39   -9.336  1   31.143 ? 21  GLN   A HB2  1 c 1 
ATOM   115  H HB3  . GLN   A 1 9   ? -4.646  10.065 -10.767 1   32.211 ? 21  GLN   A HB3  1 c 1 
ATOM   116  H HG2  . GLN   A 1 9   ? -3.324  8.298  -11.547 1   35.86  ? 21  GLN   A HG2  1 c 1 
ATOM   117  H HG3  . GLN   A 1 9   ? -3.293  7.647  -10.106 1   34.775 ? 21  GLN   A HG3  1 c 1 
ATOM   118  H HE21 . GLN   A 1 9   ? -5.392  5.443  -11.152 1   41.553 ? 21  GLN   A HE21 1 c 1 
ATOM   119  H HE22 . GLN   A 1 9   ? -4.017  5.848  -11.711 1   41.413 ? 21  GLN   A HE22 1 c 1 
ATOM   120  N N    . GLY   A 1 10  ? -3.183  11.773 -7.76   1   24.252 ? 22  GLY   A N    1 ? 1 
ATOM   121  C CA   . GLY   A 1 10  ? -3.746  12.94  -7.12   1   22.702 ? 22  GLY   A CA   1 ? 1 
ATOM   122  C C    . GLY   A 1 10  ? -2.989  14.224 -7.465  1   23.218 ? 22  GLY   A C    1 ? 1 
ATOM   123  O O    . GLY   A 1 10  ? -1.774  14.219 -7.694  1   24.17  ? 22  GLY   A O    1 ? 1 
ATOM   124  H H    . GLY   A 1 10  ? -2.69   11.187 -7.263  1   24.463 ? 22  GLY   A H    1 c 1 
ATOM   125  H HA2  . GLY   A 1 10  ? -4.688  13.031 -7.395  1   23.377 ? 22  GLY   A HA2  1 c 1 
ATOM   126  H HA3  . GLY   A 1 10  ? -3.729  12.806 -6.144  1   22.148 ? 22  GLY   A HA3  1 c 1 
ATOM   127  N N    . GLU   A 1 11  ? -3.729  15.329 -7.403  1   22.787 ? 23  GLU   A N    1 ? 1 
ATOM   128  C CA   . GLU   A 1 11  ? -3.195  16.66  -7.6    1   24.807 ? 23  GLU   A CA   1 ? 1 
ATOM   129  C C    . GLU   A 1 11  ? -2.569  17.163 -6.31   1   25.03  ? 23  GLU   A C    1 ? 1 
ATOM   130  O O    . GLU   A 1 11  ? -3.175  17.027 -5.253  1   25.047 ? 23  GLU   A O    1 ? 1 
ATOM   131  C CB   . GLU   A 1 11  ? -4.361  17.566 -7.988  1   27.809 ? 23  GLU   A CB   1 ? 1 
ATOM   132  C CG   . GLU   A 1 11  ? -3.962  19.027 -8.147  1   32.442 ? 23  GLU   A CG   1 ? 1 
ATOM   133  C CD   . GLU   A 1 11  ? -5.116  19.918 -8.589  1   39.203 ? 23  GLU   A CD   1 ? 1 
ATOM   134  O OE1  . GLU   A 1 11  ? -6.259  19.444 -8.747  1   43.747 ? 23  GLU   A OE1  1 ? 1 
ATOM   135  O OE2  . GLU   A 1 11  ? -4.852  21.114 -8.743  1   43.763 ? 23  GLU   A OE2  1 ? 1 
ATOM   136  H H    . GLU   A 1 11  ? -4.621  15.245 -7.223  1   23.244 ? 23  GLU   A H    1 c 1 
ATOM   137  H HA   . GLU   A 1 11  ? -2.516  16.636 -8.321  1   25.759 ? 23  GLU   A HA   1 c 1 
ATOM   138  H HB2  . GLU   A 1 11  ? -4.745  17.244 -8.83   1   28.971 ? 23  GLU   A HB2  1 c 1 
ATOM   139  H HB3  . GLU   A 1 11  ? -5.055  17.501 -7.299  1   27.528 ? 23  GLU   A HB3  1 c 1 
ATOM   140  H HG2  . GLU   A 1 11  ? -3.617  19.364 -7.293  1   31.843 ? 23  GLU   A HG2  1 c 1 
ATOM   141  H HG3  . GLU   A 1 11  ? -3.241  19.094 -8.81   1   33.263 ? 23  GLU   A HG3  1 c 1 
ATOM   142  N N    . ASP   A 1 12  ? -1.411  17.807 -6.413  1   23.869 ? 24  ASP   A N    1 ? 1 
ATOM   143  C CA   . ASP   A 1 12  ? -0.795  18.426 -5.245  1   23.855 ? 24  ASP   A CA   1 ? 1 
ATOM   144  C C    . ASP   A 1 12  ? -1.427  19.8   -5.005  1   24.547 ? 24  ASP   A C    1 ? 1 
ATOM   145  O O    . ASP   A 1 12  ? -1.26   20.707 -5.825  1   25.664 ? 24  ASP   A O    1 ? 1 
ATOM   146  C CB   . ASP   A 1 12  ? 0.706   18.531 -5.436  1   23.949 ? 24  ASP   A CB   1 ? 1 
ATOM   147  C CG   . ASP   A 1 12  ? 1.48    19.074 -4.248  1   24.307 ? 24  ASP   A CG   1 ? 1 
ATOM   148  O OD1  . ASP   A 1 12  ? 0.849   19.425 -3.226  1   23.211 ? 24  ASP   A OD1  1 ? 1 
ATOM   149  O OD2  . ASP   A 1 12  ? 2.715   19.095 -4.329  1   24.129 ? 24  ASP   A OD2  1 ? 1 
ATOM   150  H H    . ASP   A 1 12  ? -0.991  17.867 -7.223  1   25.195 ? 24  ASP   A H    1 c 1 
ATOM   151  H HA   . ASP   A 1 12  ? -0.963  17.856 -4.463  1   22.89  ? 24  ASP   A HA   1 c 1 
ATOM   152  H HB2  . ASP   A 1 12  ? 1.056   17.64  -5.645  1   24.228 ? 24  ASP   A HB2  1 c 1 
ATOM   153  H HB3  . ASP   A 1 12  ? 0.884   19.111 -6.205  1   25.218 ? 24  ASP   A HB3  1 c 1 
ATOM   154  N N    . ILE   A 1 13  ? -2.186  19.936 -3.909  1   23.281 ? 25  ILE   A N    1 ? 1 
ATOM   155  C CA   . ILE   A 1 13  ? -2.89   21.186 -3.637  1   24.731 ? 25  ILE   A CA   1 ? 1 
ATOM   156  C C    . ILE   A 1 13  ? -2.178  21.971 -2.522  1   24.602 ? 25  ILE   A C    1 ? 1 
ATOM   157  O O    . ILE   A 1 13  ? -2.752  22.905 -1.964  1   26.833 ? 25  ILE   A O    1 ? 1 
ATOM   158  C CB   . ILE   A 1 13  ? -4.378  20.933 -3.31   1   25.518 ? 25  ILE   A CB   1 ? 1 
ATOM   159  C CG1  . ILE   A 1 13  ? -4.541  20.017 -2.095  1   24.864 ? 25  ILE   A CG1  1 ? 1 
ATOM   160  C CG2  . ILE   A 1 13  ? -5.148  20.387 -4.525  1   26.356 ? 25  ILE   A CG2  1 ? 1 
ATOM   161  C CD1  . ILE   A 1 13  ? -5.937  20.036 -1.495  1   27.132 ? 25  ILE   A CD1  1 ? 1 
ATOM   162  H H    . ILE   A 1 13  ? -2.26   19.244 -3.317  1   22.841 ? 25  ILE   A H    1 c 1 
ATOM   163  H HA   . ILE   A 1 13  ? -2.859  21.73  -4.448  1   25.727 ? 25  ILE   A HA   1 c 1 
ATOM   164  H HB   . ILE   A 1 13  ? -4.775  21.795 -3.077  1   26.042 ? 25  ILE   A HB   1 c 1 
ATOM   165  H HG12 . ILE   A 1 13  ? -4.328  19.1   -2.361  1   24.829 ? 25  ILE   A HG12 1 c 1 
ATOM   166  H HG13 . ILE   A 1 13  ? -3.9    20.285 -1.406  1   24.899 ? 25  ILE   A HG13 1 c 1 
ATOM   167  H HG21 . ILE   A 1 13  ? -6.1    20.377 -4.33   1   26.427 ? 25  ILE   A HG21 1 c 1 
ATOM   168  H HG22 . ILE   A 1 13  ? -4.849  19.483 -4.72   1   25.87  ? 25  ILE   A HG22 1 c 1 
ATOM   169  H HG23 . ILE   A 1 13  ? -4.983  20.955 -5.297  1   27.221 ? 25  ILE   A HG23 1 c 1 
ATOM   170  H HD11 . ILE   A 1 13  ? -6.197  20.957 -1.303  1   27.015 ? 25  ILE   A HD11 1 c 1 
ATOM   171  H HD12 . ILE   A 1 13  ? -5.943  19.519 -0.668  1   25.817 ? 25  ILE   A HD12 1 c 1 
ATOM   172  H HD13 . ILE   A 1 13  ? -6.57   19.646 -2.126  1   26.757 ? 25  ILE   A HD13 1 c 1 
ATOM   173  N N    . THR   A 1 14  ? -0.918  21.665 -2.223  1   24.265 ? 26  THR   A N    1 ? 1 
ATOM   174  C CA   . THR   A 1 14  ? -0.146  22.452 -1.259  1   24.638 ? 26  THR   A CA   1 ? 1 
ATOM   175  C C    . THR   A 1 14  ? 0.436   23.683 -1.951  1   27.244 ? 26  THR   A C    1 ? 1 
ATOM   176  O O    . THR   A 1 14  ? 0.712   23.668 -3.151  1   28.105 ? 26  THR   A O    1 ? 1 
ATOM   177  C CB   . THR   A 1 14  ? 0.952   21.629 -0.56   1   25.196 ? 26  THR   A CB   1 ? 1 
ATOM   178  O OG1  . THR   A 1 14  ? 1.94    21.241 -1.512  1   25.295 ? 26  THR   A OG1  1 ? 1 
ATOM   179  C CG2  . THR   A 1 14  ? 0.385   20.45  0.215   1   23.281 ? 26  THR   A CG2  1 ? 1 
ATOM   180  H H    . THR   A 1 14  ? -0.518  20.948 -2.623  1   24.052 ? 26  THR   A H    1 c 1 
ATOM   181  H HA   . THR   A 1 14  ? -0.767  22.761 -0.564  1   24.848 ? 26  THR   A HA   1 c 1 
ATOM   182  H HB   . THR   A 1 14  ? 1.384   22.217 0.104   1   25.166 ? 26  THR   A HB   1 c 1 
ATOM   183  H HG1  . THR   A 1 14  ? 1.594   20.792 -2.15   0   30     ? 26  THR   A HG1  1 c 1 
ATOM   184  H HG21 . THR   A 1 14  ? 1.112   19.897 0.544   1   23.231 ? 26  THR   A HG21 1 c 1 
ATOM   185  H HG22 . THR   A 1 14  ? -0.185  19.923 -0.368  1   23.234 ? 26  THR   A HG22 1 c 1 
ATOM   186  H HG23 . THR   A 1 14  ? -0.138  20.778 0.967   1   23.281 ? 26  THR   A HG23 1 c 1 
ATOM   187  N N    . SER   A 1 15  ? 0.627   24.75  -1.167  1   27.302 ? 27  SER   A N    1 ? 1 
ATOM   188  C CA   . SER   A 1 15  ? 1.278   25.961 -1.644  1   30.513 ? 27  SER   A CA   1 ? 1 
ATOM   189  C C    . SER   A 1 15  ? 2.752   25.691 -1.951  1   30.109 ? 27  SER   A C    1 ? 1 
ATOM   190  O O    . SER   A 1 15  ? 3.286   26.131 -2.963  1   28.498 ? 27  SER   A O    1 ? 1 
ATOM   191  C CB   . SER   A 1 15  ? 1.111   27.082 -0.653  1   33.241 ? 27  SER   A CB   1 ? 1 
ATOM   192  O OG   . SER   A 1 15  ? -0.25   27.491 -0.687  1   35.47  ? 27  SER   A OG   1 ? 1 
ATOM   193  H H    . SER   A 1 15  ? 0.339   24.721 -0.3    1   27.244 ? 27  SER   A H    1 c 1 
ATOM   194  H HA   . SER   A 1 15  ? 0.836   26.23  -2.489  1   31.138 ? 27  SER   A HA   1 c 1 
ATOM   195  H HB2  . SER   A 1 15  ? 1.345   26.773 0.243   1   32.509 ? 27  SER   A HB2  1 c 1 
ATOM   196  H HB3  . SER   A 1 15  ? 1.69    27.829 -0.895  1   34.819 ? 27  SER   A HB3  1 c 1 
ATOM   197  H HG   . SER   A 1 15  ? -0.335  28.142 -0.189  0   30     ? 27  SER   A HG   1 c 1 
ATOM   198  N N    . LYS   A 1 16  ? 3.378   24.914 -1.074  1   29.252 ? 28  LYS   A N    1 ? 1 
ATOM   199  C CA   . LYS   A 1 16  ? 4.793   24.612 -1.201  1   32.42  ? 28  LYS   A CA   1 ? 1 
ATOM   200  C C    . LYS   A 1 16  ? 5.057   23.575 -2.286  1   29.625 ? 28  LYS   A C    1 ? 1 
ATOM   201  O O    . LYS   A 1 16  ? 6.205   23.408 -2.65   1   29.779 ? 28  LYS   A O    1 ? 1 
ATOM   202  C CB   . LYS   A 1 16  ? 5.365   24.109 0.128   1   33.206 ? 28  LYS   A CB   1 ? 1 
ATOM   203  C CG   . LYS   A 1 16  ? 5.683   25.199 1.13    1   37.073 ? 28  LYS   A CG   1 ? 1 
ATOM   204  C CD   . LYS   A 1 16  ? 5.873   24.641 2.531   1   39.711 ? 28  LYS   A CD   1 ? 1 
ATOM   205  C CE   . LYS   A 1 16  ? 5.792   25.723 3.541   1   44.837 ? 28  LYS   A CE   1 ? 1 
ATOM   206  N NZ   . LYS   A 1 16  ? 5.728   25.157 4.896   1   48.262 ? 28  LYS   A NZ   1 ? 1 
ATOM   207  H H    . LYS   A 1 16  ? 2.914   24.564 -0.369  1   28.738 ? 28  LYS   A H    1 c 1 
ATOM   208  H HA   . LYS   A 1 16  ? 5.267   25.447 -1.445  1   33.21  ? 28  LYS   A HA   1 c 1 
ATOM   209  H HB2  . LYS   A 1 16  ? 4.722   23.49  0.534   1   32.119 ? 28  LYS   A HB2  1 c 1 
ATOM   210  H HB3  . LYS   A 1 16  ? 6.188   23.606 -0.05   1   33.533 ? 28  LYS   A HB3  1 c 1 
ATOM   211  H HG2  . LYS   A 1 16  ? 6.503   25.66  0.849   1   38.591 ? 28  LYS   A HG2  1 c 1 
ATOM   212  H HG3  . LYS   A 1 16  ? 4.948   25.85  1.133   1   37.576 ? 28  LYS   A HG3  1 c 1 
ATOM   213  H HD2  . LYS   A 1 16  ? 5.177   23.973 2.716   1   38.312 ? 28  LYS   A HD2  1 c 1 
ATOM   214  H HD3  . LYS   A 1 16  ? 6.75    24.204 2.593   1   39.898 ? 28  LYS   A HD3  1 c 1 
ATOM   215  H HE2  . LYS   A 1 16  ? 6.575   26.298 3.471   1   46.245 ? 28  LYS   A HE2  1 c 1 
ATOM   216  H HE3  . LYS   A 1 16  ? 4.998   26.265 3.385   1   44.888 ? 28  LYS   A HE3  1 c 1 
ATOM   217  H HZ1  . LYS   A 1 16  ? 6.457   24.641 5.048   1   46.734 ? 28  LYS   A HZ1  1 c 1 
ATOM   218  H HZ2  . LYS   A 1 16  ? 4.981   24.65  4.982   1   45.615 ? 28  LYS   A HZ2  1 c 1 
ATOM   219  H HZ3  . LYS   A 1 16  ? 5.705   25.826 5.506   1   47.683 ? 28  LYS   A HZ3  1 c 1 
ATOM   220  N N    . LYS   A 1 17  ? 4.029   22.875 -2.775  1   28.571 ? 29  LYS   A N    1 ? 1 
ATOM   221  C CA   . LYS   A 1 17  ? 4.2     21.802 -3.749  1   29.729 ? 29  LYS   A CA   1 ? 1 
ATOM   222  C C    . LYS   A 1 17  ? 5.157   20.728 -3.211  1   30.354 ? 29  LYS   A C    1 ? 1 
ATOM   223  O O    . LYS   A 1 17  ? 6.106   20.325 -3.89   1   29.412 ? 29  LYS   A O    1 ? 1 
ATOM   224  C CB   . LYS   A 1 17  ? 4.612   22.344 -5.124  1   33.692 ? 29  LYS   A CB   1 ? 1 
ATOM   225  C CG   . LYS   A 1 17  ? 3.492   23.126 -5.792  1   37.437 ? 29  LYS   A CG   1 ? 1 
ATOM   226  C CD   . LYS   A 1 17  ? 2.259   22.286 -6.128  1   39.784 ? 29  LYS   A CD   1 ? 1 
ATOM   227  C CE   . LYS   A 1 17  ? 1.286   22.945 -7.067  1   45.914 ? 29  LYS   A CE   1 ? 1 
ATOM   228  N NZ   . LYS   A 1 17  ? 0.248   23.63  -6.291  1   50.058 ? 29  LYS   A NZ   1 ? 1 
ATOM   229  H H    . LYS   A 1 17  ? 3.183   23.063 -2.485  1   28.345 ? 29  LYS   A H    1 c 1 
ATOM   230  H HA   . LYS   A 1 17  ? 3.318   21.373 -3.863  1   29.282 ? 29  LYS   A HA   1 c 1 
ATOM   231  H HB2  . LYS   A 1 17  ? 5.393   22.929 -5.027  1   34.882 ? 29  LYS   A HB2  1 c 1 
ATOM   232  H HB3  . LYS   A 1 17  ? 4.863   21.596 -5.706  1   33.862 ? 29  LYS   A HB3  1 c 1 
ATOM   233  H HG2  . LYS   A 1 17  ? 3.225   23.859 -5.195  1   37.489 ? 29  LYS   A HG2  1 c 1 
ATOM   234  H HG3  . LYS   A 1 17  ? 3.841   23.525 -6.618  1   38.863 ? 29  LYS   A HG3  1 c 1 
ATOM   235  H HD2  . LYS   A 1 17  ? 2.558   21.439 -6.527  1   39.783 ? 29  LYS   A HD2  1 c 1 
ATOM   236  H HD3  . LYS   A 1 17  ? 1.791   22.067 -5.293  1   38.814 ? 29  LYS   A HD3  1 c 1 
ATOM   237  H HE2  . LYS   A 1 17  ? 1.747   23.592 -7.63   1   47     ? 29  LYS   A HE2  1 c 1 
ATOM   238  H HE3  . LYS   A 1 17  ? 0.871   22.275 -7.64   1   45.417 ? 29  LYS   A HE3  1 c 1 
ATOM   239  H HZ1  . LYS   A 1 17  ? 0.63    24.168 -5.671  1   48.699 ? 29  LYS   A HZ1  1 c 1 
ATOM   240  H HZ2  . LYS   A 1 17  ? -0.278  23.021 -5.875  1   47.359 ? 29  LYS   A HZ2  1 c 1 
ATOM   241  H HZ3  . LYS   A 1 17  ? -0.264  24.133 -6.845  1   49.498 ? 29  LYS   A HZ3  1 c 1 
ATOM   242  N N    . ASP   A 1 18  ? 4.877   20.265 -1.979  1   27.036 ? 30  ASP   A N    1 ? 1 
ATOM   243  C CA   . ASP   A 1 18  ? 5.667   19.237 -1.314  1   26.405 ? 30  ASP   A CA   1 ? 1 
ATOM   244  C C    . ASP   A 1 18  ? 4.917   17.903 -1.298  1   24.617 ? 30  ASP   A C    1 ? 1 
ATOM   245  O O    . ASP   A 1 18  ? 5.257   17.008 -0.518  1   24.748 ? 30  ASP   A O    1 ? 1 
ATOM   246  C CB   . ASP   A 1 18  ? 6.036   19.699 0.092   1   26.487 ? 30  ASP   A CB   1 ? 1 
ATOM   247  C CG   . ASP   A 1 18  ? 4.851   20.068 0.967   1   27.14  ? 30  ASP   A CG   1 ? 1 
ATOM   248  O OD1  . ASP   A 1 18  ? 3.731   19.62  0.632   1   24.776 ? 30  ASP   A OD1  1 ? 1 
ATOM   249  O OD2  . ASP   A 1 18  ? 5.06    20.838 1.944   1   25.391 ? 30  ASP   A OD2  1 ? 1 
ATOM   250  H H    . ASP   A 1 18  ? 4.149   20.603 -1.542  1   26.926 ? 30  ASP   A H    1 c 1 
ATOM   251  H HA   . ASP   A 1 18  ? 6.505   19.116 -1.813  1   27.284 ? 30  ASP   A HA   1 c 1 
ATOM   252  H HB2  . ASP   A 1 18  ? 6.544   18.992 0.541   1   26.674 ? 30  ASP   A HB2  1 c 1 
ATOM   253  H HB3  . ASP   A 1 18  ? 6.617   20.485 0.02    1   27.803 ? 30  ASP   A HB3  1 c 1 
ATOM   254  N N    . ARG   A 1 19  ? 3.841   17.777 -2.087  1   23.567 ? 31  ARG   A N    1 ? 1 
ATOM   255  C CA   . ARG   A 1 19  ? 2.983   16.589 -2.127  1   23.733 ? 31  ARG   A CA   1 ? 1 
ATOM   256  C C    . ARG   A 1 19  ? 2.415   16.215 -0.743  1   23.807 ? 31  ARG   A C    1 ? 1 
ATOM   257  O O    . ARG   A 1 19  ? 2.02    15.076 -0.498  1   25.551 ? 31  ARG   A O    1 ? 1 
ATOM   258  C CB   . ARG   A 1 19  ? 3.737   15.405 -2.756  1   23.486 ? 31  ARG   A CB   1 ? 1 
ATOM   259  C CG   . ARG   A 1 19  ? 4.078   15.624 -4.221  1   25.845 ? 31  ARG   A CG   1 ? 1 
ATOM   260  C CD   . ARG   A 1 19  ? 4.79    14.455 -4.9    1   28.505 ? 31  ARG   A CD   1 ? 1 
ATOM   261  N NE   . ARG   A 1 19  ? 4.178   13.136 -4.677  1   29.601 ? 31  ARG   A NE   1 ? 1 
ATOM   262  C CZ   . ARG   A 1 19  ? 3.139   12.586 -5.315  1   30.772 ? 31  ARG   A CZ   1 ? 1 
ATOM   263  N NH1  . ARG   A 1 19  ? 2.552   13.204 -6.331  1   29.157 ? 31  ARG   A NH1  1 ? 1 
ATOM   264  N NH2  . ARG   A 1 19  ? 2.75    11.357 -4.95   1   30.28  ? 31  ARG   A NH2  1 ? 1 
ATOM   265  H H    . ARG   A 1 19  ? 3.629   18.471 -2.64   1   24.418 ? 31  ARG   A H    1 c 1 
ATOM   266  H HA   . ARG   A 1 19  ? 2.217   16.794 -2.719  1   23.579 ? 31  ARG   A HA   1 c 1 
ATOM   267  H HB2  . ARG   A 1 19  ? 4.567   15.249 -2.257  1   24.19  ? 31  ARG   A HB2  1 c 1 
ATOM   268  H HB3  . ARG   A 1 19  ? 3.185   14.599 -2.678  1   23.705 ? 31  ARG   A HB3  1 c 1 
ATOM   269  H HG2  . ARG   A 1 19  ? 3.249   15.812 -4.712  1   25.866 ? 31  ARG   A HG2  1 c 1 
ATOM   270  H HG3  . ARG   A 1 19  ? 4.645   16.422 -4.296  1   26.414 ? 31  ARG   A HG3  1 c 1 
ATOM   271  H HD2  . ARG   A 1 19  ? 4.825   14.631 -5.863  1   29.264 ? 31  ARG   A HD2  1 c 1 
ATOM   272  H HD3  . ARG   A 1 19  ? 5.713   14.433 -4.576  1   28.87  ? 31  ARG   A HD3  1 c 1 
ATOM   273  H HE   . ARG   A 1 19  ? 4.536   12.65  -4.049  1   29.451 ? 31  ARG   A HE   1 c 1 
ATOM   274  H HH11 . ARG   A 1 19  ? 2.808   14.014 -6.573  1   29.879 ? 31  ARG   A HH11 1 c 1 
ATOM   275  H HH12 . ARG   A 1 19  ? 1.897   12.8   -6.766  1   29.987 ? 31  ARG   A HH12 1 c 1 
ATOM   276  H HH21 . ARG   A 1 19  ? 3.308   10.826 -4.515  1   30.71  ? 31  ARG   A HH21 1 c 1 
ATOM   277  H HH22 . ARG   A 1 19  ? 1.934   11.08  -5.149  1   30.396 ? 31  ARG   A HH22 1 c 1 
ATOM   278  N N    . GLY   A 1 20  ? 2.273   17.215 0.122   1   25.293 ? 32  GLY   A N    1 ? 1 
ATOM   279  C CA   . GLY   A 1 20  ? 1.837   16.995 1.492   1   23.125 ? 32  GLY   A CA   1 ? 1 
ATOM   280  C C    . GLY   A 1 20  ? 0.338   16.714 1.575   1   24.369 ? 32  GLY   A C    1 ? 1 
ATOM   281  O O    . GLY   A 1 20  ? -0.119  16.102 2.543   1   23.994 ? 32  GLY   A O    1 ? 1 
ATOM   282  H H    . GLY   A 1 20  ? 2.434   18.072 -0.151  1   24.862 ? 32  GLY   A H    1 c 1 
ATOM   283  H HA2  . GLY   A 1 20  ? 2.335   16.234 1.871   1   23.914 ? 32  GLY   A HA2  1 c 1 
ATOM   284  H HA3  . GLY   A 1 20  ? 2.051   17.792 2.027   1   24.007 ? 32  GLY   A HA3  1 c 1 
ATOM   285  N N    . VAL   A 1 21  ? -0.412  17.223 0.582   1   23.576 ? 33  VAL   A N    1 ? 1 
ATOM   286  C CA   . VAL   A 1 21  ? -1.844  17.02  0.455   1   21.185 ? 33  VAL   A CA   1 ? 1 
ATOM   287  C C    . VAL   A 1 21  ? -2.126  16.746 -1.025  1   22.481 ? 33  VAL   A C    1 ? 1 
ATOM   288  O O    . VAL   A 1 21  ? -1.926  17.621 -1.842  1   20.84  ? 33  VAL   A O    1 ? 1 
ATOM   289  C CB   . VAL   A 1 21  ? -2.675  18.217 0.946   1   21.343 ? 33  VAL   A CB   1 ? 1 
ATOM   290  C CG1  . VAL   A 1 21  ? -4.159  17.897 0.95    1   21.768 ? 33  VAL   A CG1  1 ? 1 
ATOM   291  C CG2  . VAL   A 1 21  ? -2.311  18.657 2.362   1   20.639 ? 33  VAL   A CG2  1 ? 1 
ATOM   292  H H    . VAL   A 1 21  ? 0.004   17.725 -0.057  1   23.67  ? 33  VAL   A H    1 c 1 
ATOM   293  H HA   . VAL   A 1 21  ? -2.096  16.232 0.974   1   21.518 ? 33  VAL   A HA   1 c 1 
ATOM   294  H HB   . VAL   A 1 21  ? -2.513  18.969 0.329   1   21.777 ? 33  VAL   A HB   1 c 1 
ATOM   295  H HG11 . VAL   A 1 21  ? -4.316  17.093 1.474   1   21.38  ? 33  VAL   A HG11 1 c 1 
ATOM   296  H HG12 . VAL   A 1 21  ? -4.464  17.753 0.039   1   21.967 ? 33  VAL   A HG12 1 c 1 
ATOM   297  H HG13 . VAL   A 1 21  ? -4.651  18.638 1.341   1   21.884 ? 33  VAL   A HG13 1 c 1 
ATOM   298  H HG21 . VAL   A 1 21  ? -2.886  19.393 2.632   1   21.091 ? 33  VAL   A HG21 1 c 1 
ATOM   299  H HG22 . VAL   A 1 21  ? -1.384  18.948 2.384   1   20.965 ? 33  VAL   A HG22 1 c 1 
ATOM   300  H HG23 . VAL   A 1 21  ? -2.43   17.912 2.975   1   20.464 ? 33  VAL   A HG23 1 c 1 
ATOM   301  N N    . LEU   A 1 22  ? -2.616  15.542 -1.32   1   22.369 ? 34  LEU   A N    1 ? 1 
ATOM   302  C CA   . LEU   A 1 22  ? -2.927  15.103 -2.678  1   22.207 ? 34  LEU   A CA   1 ? 1 
ATOM   303  C C    . LEU   A 1 22  ? -4.426  14.839 -2.72   1   23.882 ? 34  LEU   A C    1 ? 1 
ATOM   304  O O    . LEU   A 1 22  ? -4.995  14.293 -1.759  1   23.075 ? 34  LEU   A O    1 ? 1 
ATOM   305  C CB   . LEU   A 1 22  ? -2.137  13.847 -3.006  1   21.071 ? 34  LEU   A CB   1 ? 1 
ATOM   306  C CG   . LEU   A 1 22  ? -0.612  13.98  -2.992  1   23.648 ? 34  LEU   A CG   1 ? 1 
ATOM   307  C CD1  . LEU   A 1 22  ? 0.059   12.599 -2.988  1   24.051 ? 34  LEU   A CD1  1 ? 1 
ATOM   308  C CD2  . LEU   A 1 22  ? -0.071  14.822 -4.151  1   23.238 ? 34  LEU   A CD2  1 ? 1 
ATOM   309  H H    . LEU   A 1 22  ? -2.767  14.955 -0.636  1   21.952 ? 34  LEU   A H    1 c 1 
ATOM   310  H HA   . LEU   A 1 22  ? -2.694  15.822 -3.314  1   22.682 ? 34  LEU   A HA   1 c 1 
ATOM   311  H HB2  . LEU   A 1 22  ? -2.392  13.15  -2.359  1   21.801 ? 34  LEU   A HB2  1 c 1 
ATOM   312  H HB3  . LEU   A 1 22  ? -2.413  13.537 -3.9    1   22.598 ? 34  LEU   A HB3  1 c 1 
ATOM   313  H HG   . LEU   A 1 22  ? -0.356  14.436 -2.149  1   22.392 ? 34  LEU   A HG   1 c 1 
ATOM   314  H HD11 . LEU   A 1 22  ? -0.207  12.11  -2.19   1   23.802 ? 34  LEU   A HD11 1 c 1 
ATOM   315  H HD12 . LEU   A 1 22  ? 1.025   12.706 -2.993  1   24.321 ? 34  LEU   A HD12 1 c 1 
ATOM   316  H HD13 . LEU   A 1 22  ? -0.216  12.102 -3.777  1   24.762 ? 34  LEU   A HD13 1 c 1 
ATOM   317  H HD21 . LEU   A 1 22  ? -0.42   15.726 -4.086  1   23.393 ? 34  LEU   A HD21 1 c 1 
ATOM   318  H HD22 . LEU   A 1 22  ? -0.349  14.429 -4.996  1   24.18  ? 34  LEU   A HD22 1 c 1 
ATOM   319  H HD23 . LEU   A 1 22  ? 0.9     14.847 -4.11   1   23.799 ? 34  LEU   A HD23 1 c 1 
ATOM   320  N N    . LYS   A 1 23  ? -5.05   15.199 -3.859  1   23     ? 35  LYS   A N    1 ? 1 
ATOM   321  C CA   . LYS   A 1 23  ? -6.493  15.172 -3.976  1   22.611 ? 35  LYS   A CA   1 ? 1 
ATOM   322  C C    . LYS   A 1 23  ? -6.911  14.542 -5.301  1   24.548 ? 35  LYS   A C    1 ? 1 
ATOM   323  O O    . LYS   A 1 23  ? -6.341  14.875 -6.336  1   24.242 ? 35  LYS   A O    1 ? 1 
ATOM   324  C CB   . LYS   A 1 23  ? -7.029  16.608 -3.914  1   22.242 ? 35  LYS   A CB   1 ? 1 
ATOM   325  C CG   . LYS   A 1 23  ? -8.545  16.753 -4.074  1   23.778 ? 35  LYS   A CG   1 ? 1 
ATOM   326  C CD   . LYS   A 1 23  ? -9.024  18.197 -4.218  1   25.098 ? 35  LYS   A CD   1 ? 1 
ATOM   327  C CE   . LYS   A 1 23  ? -10.53  18.209 -4.278  1   25.579 ? 35  LYS   A CE   1 ? 1 
ATOM   328  N NZ   . LYS   A 1 23  ? -11.142 19.507 -4.527  1   26.438 ? 35  LYS   A NZ   1 ? 1 
ATOM   329  H H    . LYS   A 1 23  ? -4.554  15.464 -4.58   1   23.538 ? 35  LYS   A H    1 c 1 
ATOM   330  H HA   . LYS   A 1 23  ? -6.866  14.645 -3.23   1   22.612 ? 35  LYS   A HA   1 c 1 
ATOM   331  H HB2  . LYS   A 1 23  ? -6.772  16.999 -3.052  1   21.928 ? 35  LYS   A HB2  1 c 1 
ATOM   332  H HB3  . LYS   A 1 23  ? -6.593  17.134 -4.618  1   22.895 ? 35  LYS   A HB3  1 c 1 
ATOM   333  H HG2  . LYS   A 1 23  ? -8.828  16.247 -4.866  1   24.439 ? 35  LYS   A HG2  1 c 1 
ATOM   334  H HG3  . LYS   A 1 23  ? -8.981  16.35  -3.291  1   23.504 ? 35  LYS   A HG3  1 c 1 
ATOM   335  H HD2  . LYS   A 1 23  ? -8.721  18.727 -3.448  1   24.33  ? 35  LYS   A HD2  1 c 1 
ATOM   336  H HD3  . LYS   A 1 23  ? -8.659  18.589 -5.041  1   25.316 ? 35  LYS   A HD3  1 c 1 
ATOM   337  H HE2  . LYS   A 1 23  ? -10.816 17.597 -4.979  1   26.206 ? 35  LYS   A HE2  1 c 1 
ATOM   338  H HE3  . LYS   A 1 23  ? -10.875 17.865 -3.434  1   25.286 ? 35  LYS   A HE3  1 c 1 
ATOM   339  H HZ1  . LYS   A 1 23  ? -10.826 19.85  -5.303  1   27.009 ? 35  LYS   A HZ1  1 c 1 
ATOM   340  H HZ2  . LYS   A 1 23  ? -10.945 20.074 -3.848  1   26.215 ? 35  LYS   A HZ2  1 c 1 
ATOM   341  H HZ3  . LYS   A 1 23  ? -12.041 19.415 -4.586  1   27.283 ? 35  LYS   A HZ3  1 c 1 
ATOM   342  N N    . ILE   A 1 24  ? -7.936  13.682 -5.248  1   25.869 ? 36  ILE   A N    1 ? 1 
ATOM   343  C CA   . ILE   A 1 24  ? -8.697  13.327 -6.443  1   27.467 ? 36  ILE   A CA   1 ? 1 
ATOM   344  C C    . ILE   A 1 24  ? -10.171 13.666 -6.229  1   29.734 ? 36  ILE   A C    1 ? 1 
ATOM   345  O O    . ILE   A 1 24  ? -10.751 13.308 -5.213  1   29.834 ? 36  ILE   A O    1 ? 1 
ATOM   346  C CB   . ILE   A 1 24  ? -8.562  11.837 -6.786  1   29.613 ? 36  ILE   A CB   1 ? 1 
ATOM   347  C CG1  . ILE   A 1 24  ? -7.109  11.403 -6.934  1   29.932 ? 36  ILE   A CG1  1 ? 1 
ATOM   348  C CG2  . ILE   A 1 24  ? -9.381  11.508 -8.053  1   32.578 ? 36  ILE   A CG2  1 ? 1 
ATOM   349  C CD1  . ILE   A 1 24  ? -6.918  9.91   -7.176  1   32.267 ? 36  ILE   A CD1  1 ? 1 
ATOM   350  H H    . ILE   A 1 24  ? -8.167  13.303 -4.449  1   25.388 ? 36  ILE   A H    1 c 1 
ATOM   351  H HA   . ILE   A 1 24  ? -8.362  13.85  -7.197  1   28.267 ? 36  ILE   A HA   1 c 1 
ATOM   352  H HB   . ILE   A 1 24  ? -8.946  11.328 -6.045  1   29.601 ? 36  ILE   A HB   1 c 1 
ATOM   353  H HG12 . ILE   A 1 24  ? -6.711  11.894 -7.681  1   30.232 ? 36  ILE   A HG12 1 c 1 
ATOM   354  H HG13 . ILE   A 1 24  ? -6.623  11.651 -6.121  1   28.984 ? 36  ILE   A HG13 1 c 1 
ATOM   355  H HG21 . ILE   A 1 24  ? -9.259  10.574 -8.29   1   32.997 ? 36  ILE   A HG21 1 c 1 
ATOM   356  H HG22 . ILE   A 1 24  ? -9.081  12.068 -8.789  1   32.476 ? 36  ILE   A HG22 1 c 1 
ATOM   357  H HG23 . ILE   A 1 24  ? -10.323 11.673 -7.887  1   32.629 ? 36  ILE   A HG23 1 c 1 
ATOM   358  H HD11 . ILE   A 1 24  ? -7.376  9.404  -6.478  1   31.922 ? 36  ILE   A HD11 1 c 1 
ATOM   359  H HD12 . ILE   A 1 24  ? -5.966  9.699  -7.157  1   31.672 ? 36  ILE   A HD12 1 c 1 
ATOM   360  H HD13 . ILE   A 1 24  ? -7.283  9.663  -8.046  1   33.062 ? 36  ILE   A HD13 1 c 1 
ATOM   361  N N    . VAL   A 1 25  ? -10.8   14.321 -7.207  1   32.104 ? 37  VAL   A N    1 ? 1 
ATOM   362  C CA   . VAL   A 1 25  ? -12.245 14.5   -7.203  1   34.046 ? 37  VAL   A CA   1 ? 1 
ATOM   363  C C    . VAL   A 1 25  ? -12.875 13.188 -7.661  1   36.135 ? 37  VAL   A C    1 ? 1 
ATOM   364  O O    . VAL   A 1 25  ? -12.593 12.746 -8.764  1   33.629 ? 37  VAL   A O    1 ? 1 
ATOM   365  C CB   . VAL   A 1 25  ? -12.661 15.686 -8.099  1   35.194 ? 37  VAL   A CB   1 ? 1 
ATOM   366  C CG1  . VAL   A 1 25  ? -14.177 15.76  -8.333  1   38.381 ? 37  VAL   A CG1  1 ? 1 
ATOM   367  C CG2  . VAL   A 1 25  ? -12.138 17.004 -7.539  1   34.052 ? 37  VAL   A CG2  1 ? 1 
ATOM   368  H H    . VAL   A 1 25  ? -10.315 14.669 -7.899  1   32.153 ? 37  VAL   A H    1 c 1 
ATOM   369  H HA   . VAL   A 1 25  ? -12.533 14.686 -6.289  1   33.479 ? 37  VAL   A HA   1 c 1 
ATOM   370  H HB   . VAL   A 1 25  ? -12.234 15.547 -8.976  1   35.871 ? 37  VAL   A HB   1 c 1 
ATOM   371  H HG11 . VAL   A 1 25  ? -14.643 15.612 -7.493  1   37.688 ? 37  VAL   A HG11 1 c 1 
ATOM   372  H HG12 . VAL   A 1 25  ? -14.441 15.078 -8.974  1   38.911 ? 37  VAL   A HG12 1 c 1 
ATOM   373  H HG13 . VAL   A 1 25  ? -14.41  16.636 -8.682  1   38.552 ? 37  VAL   A HG13 1 c 1 
ATOM   374  H HG21 . VAL   A 1 25  ? -12.433 17.737 -8.105  1   35.044 ? 37  VAL   A HG21 1 c 1 
ATOM   375  H HG22 . VAL   A 1 25  ? -11.167 16.984 -7.516  1   33.264 ? 37  VAL   A HG22 1 c 1 
ATOM   376  H HG23 . VAL   A 1 25  ? -12.48  17.133 -6.639  1   33.599 ? 37  VAL   A HG23 1 c 1 
ATOM   377  N N    . LYS   A 1 26  ? -13.721 12.58  -6.818  1   35.242 ? 38  LYS   A N    1 ? 1 
ATOM   378  C CA   . LYS   A 1 26  ? -14.352 11.309 -7.132  1   38.119 ? 38  LYS   A CA   1 ? 1 
ATOM   379  C C    . LYS   A 1 26  ? -15.784 11.498 -7.622  1   41.082 ? 38  LYS   A C    1 ? 1 
ATOM   380  O O    . LYS   A 1 26  ? -16.271 10.646 -8.353  1   43.169 ? 38  LYS   A O    1 ? 1 
ATOM   381  C CB   . LYS   A 1 26  ? -14.307 10.367 -5.927  1   38.742 ? 38  LYS   A CB   1 ? 1 
ATOM   382  C CG   . LYS   A 1 26  ? -12.899 10.016 -5.488  1   38.762 ? 38  LYS   A CG   1 ? 1 
ATOM   383  C CD   . LYS   A 1 26  ? -12.003 9.377  -6.541  1   41.47  ? 38  LYS   A CD   1 ? 1 
ATOM   384  C CE   . LYS   A 1 26  ? -12.388 8.01   -6.853  1   44.273 ? 38  LYS   A CE   1 ? 1 
ATOM   385  N NZ   . LYS   A 1 26  ? -11.425 7.441  -7.792  1   48.418 ? 38  LYS   A NZ   1 ? 1 
ATOM   386  H H    . LYS   A 1 26  ? -13.906 12.972 -6.013  1   35.21  ? 38  LYS   A H    1 c 1 
ATOM   387  H HA   . LYS   A 1 26  ? -13.841 10.886 -7.865  1   38.606 ? 38  LYS   A HA   1 c 1 
ATOM   388  H HB2  . LYS   A 1 26  ? -14.776 10.787 -5.175  1   38.559 ? 38  LYS   A HB2  1 c 1 
ATOM   389  H HB3  . LYS   A 1 26  ? -14.779 9.539  -6.154  1   40.255 ? 38  LYS   A HB3  1 c 1 
ATOM   390  H HG2  . LYS   A 1 26  ? -12.466 10.837 -5.167  1   37.579 ? 38  LYS   A HG2  1 c 1 
ATOM   391  H HG3  . LYS   A 1 26  ? -12.963 9.405  -4.722  1   38.885 ? 38  LYS   A HG3  1 c 1 
ATOM   392  H HD2  . LYS   A 1 26  ? -12.027 9.913  -7.362  1   41.374 ? 38  LYS   A HD2  1 c 1 
ATOM   393  H HD3  . LYS   A 1 26  ? -11.078 9.379  -6.211  1   40.097 ? 38  LYS   A HD3  1 c 1 
ATOM   394  H HE2  . LYS   A 1 26  ? -12.403 7.473  -6.041  1   44.827 ? 38  LYS   A HE2  1 c 1 
ATOM   395  H HE3  . LYS   A 1 26  ? -13.276 7.996  -7.253  1   46.092 ? 38  LYS   A HE3  1 c 1 
ATOM   396  H HZ1  . LYS   A 1 26  ? -10.602 7.414  -7.413  1   46.229 ? 38  LYS   A HZ1  1 c 1 
ATOM   397  H HZ2  . LYS   A 1 26  ? -11.39  7.945  -8.544  1   47.33  ? 38  LYS   A HZ2  1 c 1 
ATOM   398  H HZ3  . LYS   A 1 26  ? -11.676 6.599  -8.013  1   48.668 ? 38  LYS   A HZ3  1 c 1 
ATOM   399  N N    . ARG   A 1 27  ? -16.478 12.536 -7.139  1   40.765 ? 39  ARG   A N    1 ? 1 
ATOM   400  C CA   . ARG   A 1 27  ? -17.763 12.938 -7.684  1   41.96  ? 39  ARG   A CA   1 ? 1 
ATOM   401  C C    . ARG   A 1 27  ? -17.776 14.462 -7.808  1   41.523 ? 39  ARG   A C    1 ? 1 
ATOM   402  O O    . ARG   A 1 27  ? -17.49  15.17  -6.835  1   38.406 ? 39  ARG   A O    1 ? 1 
ATOM   403  C CB   . ARG   A 1 27  ? -18.931 12.508 -6.796  1   44.43  ? 39  ARG   A CB   1 ? 1 
ATOM   404  C CG   . ARG   A 1 27  ? -20.286 12.896 -7.383  1   48.722 ? 39  ARG   A CG   1 ? 1 
ATOM   405  C CD   . ARG   A 1 27  ? -21.178 13.53  -6.304  1   51.279 ? 39  ARG   A CD   1 ? 1 
ATOM   406  N NE   . ARG   A 1 27  ? -21.806 12.501 -5.476  1   52.548 ? 39  ARG   A NE   1 ? 1 
ATOM   407  C CZ   . ARG   A 1 27  ? -22.429 12.684 -4.317  1   50.674 ? 39  ARG   A CZ   1 ? 1 
ATOM   408  N NH1  . ARG   A 1 27  ? -22.311 13.81  -3.636  1   50.674 ? 39  ARG   A NH1  1 ? 1 
ATOM   409  N NH2  . ARG   A 1 27  ? -23.119 11.685 -3.804  1   52.392 ? 39  ARG   A NH2  1 ? 1 
ATOM   410  H H    . ARG   A 1 27  ? -16.141 13.005 -6.431  1   39.369 ? 39  ARG   A H    1 c 1 
ATOM   411  H HA   . ARG   A 1 27  ? -17.867 12.538 -8.585  1   43.461 ? 39  ARG   A HA   1 c 1 
ATOM   412  H HB2  . ARG   A 1 27  ? -18.902 11.534 -6.678  1   44.942 ? 39  ARG   A HB2  1 c 1 
ATOM   413  H HB3  . ARG   A 1 27  ? -18.83  12.922 -5.912  1   43.556 ? 39  ARG   A HB3  1 c 1 
ATOM   414  H HG2  . ARG   A 1 27  ? -20.164 13.535 -8.118  1   48.861 ? 39  ARG   A HG2  1 c 1 
ATOM   415  H HG3  . ARG   A 1 27  ? -20.729 12.097 -7.741  1   50.204 ? 39  ARG   A HG3  1 c 1 
ATOM   416  H HD2  . ARG   A 1 27  ? -20.64  14.119 -5.739  1   49.205 ? 39  ARG   A HD2  1 c 1 
ATOM   417  H HD3  . ARG   A 1 27  ? -21.873 14.07  -6.732  1   52.223 ? 39  ARG   A HD3  1 c 1 
ATOM   418  H HE   . ARG   A 1 27  ? -21.768 11.681 -5.768  1   52.481 ? 39  ARG   A HE   1 c 1 
ATOM   419  H HH11 . ARG   A 1 27  ? -21.512 14.171 -3.516  1   48.701 ? 39  ARG   A HH11 1 c 1 
ATOM   420  H HH12 . ARG   A 1 27  ? -23.032 14.198 -3.302  1   51.438 ? 39  ARG   A HH12 1 c 1 
ATOM   421  H HH21 . ARG   A 1 27  ? -23.478 11.076 -4.337  1   53.801 ? 39  ARG   A HH21 1 c 1 
ATOM   422  H HH22 . ARG   A 1 27  ? -23.222 11.629 -2.927  1   52.191 ? 39  ARG   A HH22 1 c 1 
ATOM   423  N N    . VAL   A 1 28  ? -18.119 14.98  -8.996  1   40.474 ? 40  VAL   A N    1 ? 1 
ATOM   424  C CA   . VAL   A 1 28  ? -18.126 16.419 -9.213  1   42.256 ? 40  VAL   A CA   1 ? 1 
ATOM   425  C C    . VAL   A 1 28  ? -19.358 17.008 -8.518  1   44.297 ? 40  VAL   A C    1 ? 1 
ATOM   426  O O    . VAL   A 1 28  ? -20.436 16.412 -8.557  1   43.814 ? 40  VAL   A O    1 ? 1 
ATOM   427  C CB   . VAL   A 1 28  ? -18.082 16.801 -10.707 1   45.562 ? 40  VAL   A CB   1 ? 1 
ATOM   428  C CG1  . VAL   A 1 28  ? -18.147 18.311 -10.903 1   46.855 ? 40  VAL   A CG1  1 ? 1 
ATOM   429  C CG2  . VAL   A 1 28  ? -16.84  16.251 -11.4   1   45.817 ? 40  VAL   A CG2  1 ? 1 
ATOM   430  H H    . VAL   A 1 28  ? -18.356 14.427 -9.684  1   42.625 ? 40  VAL   A H    1 c 1 
ATOM   431  H HA   . VAL   A 1 28  ? -17.329 16.789 -8.786  1   40.963 ? 40  VAL   A HA   1 c 1 
ATOM   432  H HB   . VAL   A 1 28  ? -18.875 16.402 -11.135 1   47.184 ? 40  VAL   A HB   1 c 1 
ATOM   433  H HG11 . VAL   A 1 28  ? -17.627 18.752 -10.209 1   45.362 ? 40  VAL   A HG11 1 c 1 
ATOM   434  H HG12 . VAL   A 1 28  ? -19.071 18.606 -10.851 1   48.102 ? 40  VAL   A HG12 1 c 1 
ATOM   435  H HG13 . VAL   A 1 28  ? -17.783 18.543 -11.774 1   47.284 ? 40  VAL   A HG13 1 c 1 
ATOM   436  H HG21 . VAL   A 1 28  ? -16.862 16.488 -12.343 1   46.649 ? 40  VAL   A HG21 1 c 1 
ATOM   437  H HG22 . VAL   A 1 28  ? -16.819 15.283 -11.311 1   45.308 ? 40  VAL   A HG22 1 c 1 
ATOM   438  H HG23 . VAL   A 1 28  ? -16.044 16.63  -10.99  1   43.98  ? 40  VAL   A HG23 1 c 1 
ATOM   439  N N    . GLY   A 1 29  ? -19.186 18.169 -7.868  1   45.315 ? 41  GLY   A N    1 ? 1 
ATOM   440  C CA   . GLY   A 1 29  ? -20.276 18.867 -7.196  1   49.404 ? 41  GLY   A CA   1 ? 1 
ATOM   441  C C    . GLY   A 1 29  ? -20.83  19.985 -8.079  1   57.629 ? 41  GLY   A C    1 ? 1 
ATOM   442  O O    . GLY   A 1 29  ? -20.601 19.994 -9.285  1   58.876 ? 41  GLY   A O    1 ? 1 
ATOM   443  H H    . GLY   A 1 29  ? -18.352 18.543 -7.845  1   44.414 ? 41  GLY   A H    1 c 1 
ATOM   444  H HA2  . GLY   A 1 29  ? -20.994 18.226 -6.98   1   50.672 ? 41  GLY   A HA2  1 c 1 
ATOM   445  H HA3  . GLY   A 1 29  ? -19.942 19.247 -6.35   1   48.771 ? 41  GLY   A HA3  1 c 1 
ATOM   446  N N    . ASN   A 1 30  ? -21.528 20.957 -7.492  1   65.225 ? 42  ASN   A N    1 ? 1 
ATOM   447  C CA   . ASN   A 1 30  ? -21.948 22.122 -8.264  1   69.526 ? 42  ASN   A CA   1 ? 1 
ATOM   448  C C    . ASN   A 1 30  ? -21.681 23.388 -7.462  1   73.982 ? 42  ASN   A C    1 ? 1 
ATOM   449  O O    . ASN   A 1 30  ? -21.797 23.377 -6.243  1   70.826 ? 42  ASN   A O    1 ? 1 
ATOM   450  C CB   . ASN   A 1 30  ? -23.411 22.072 -8.685  1   71.886 ? 42  ASN   A CB   1 ? 1 
ATOM   451  C CG   . ASN   A 1 30  ? -24.263 21.333 -7.688  1   73.732 ? 42  ASN   A CG   1 ? 1 
ATOM   452  O OD1  . ASN   A 1 30  ? -24.423 21.792 -6.55   1   75.21  ? 42  ASN   A OD1  1 ? 1 
ATOM   453  N ND2  . ASN   A 1 30  ? -24.818 20.203 -8.101  1   74.604 ? 42  ASN   A ND2  1 ? 1 
ATOM   454  H H    . ASN   A 1 30  ? -21.74  20.902 -6.604  1   63.603 ? 42  ASN   A H    1 c 1 
ATOM   455  H HA   . ASN   A 1 30  ? -21.408 22.161 -9.085  1   69.582 ? 42  ASN   A HA   1 c 1 
ATOM   456  H HB2  . ASN   A 1 30  ? -23.751 22.985 -8.78   1   73.956 ? 42  ASN   A HB2  1 c 1 
ATOM   457  H HB3  . ASN   A 1 30  ? -23.479 21.632 -9.556  1   73.088 ? 42  ASN   A HB3  1 c 1 
ATOM   458  H HD21 . ASN   A 1 30  ? -24.798 19.483 -7.582  1   73.757 ? 42  ASN   A HD21 1 c 1 
ATOM   459  H HD22 . ASN   A 1 30  ? -25.208 20.166 -8.898  1   76.103 ? 42  ASN   A HD22 1 c 1 
ATOM   460  N N    . GLY   A 1 31  ? -21.359 24.483 -8.158  1   78.855 ? 43  GLY   A N    1 ? 1 
ATOM   461  C CA   . GLY   A 1 31  ? -21.394 25.795 -7.537  1   82.849 ? 43  GLY   A CA   1 ? 1 
ATOM   462  C C    . GLY   A 1 31  ? -20.594 26.827 -8.321  1   87.509 ? 43  GLY   A C    1 ? 1 
ATOM   463  O O    . GLY   A 1 31  ? -21.094 27.913 -8.583  1   92.01  ? 43  GLY   A O    1 ? 1 
ATOM   464  H H    . GLY   A 1 31  ? -21.117 24.411 -9.036  1   78.923 ? 43  GLY   A H    1 c 1 
ATOM   465  H HA2  . GLY   A 1 31  ? -22.331 26.091 -7.466  1   84.956 ? 43  GLY   A HA2  1 c 1 
ATOM   466  H HA3  . GLY   A 1 31  ? -21.029 25.728 -6.623  1   81.393 ? 43  GLY   A HA3  1 c 1 
ATOM   467  N N    . GLU   A 1 32  ? -19.348 26.481 -8.674  1   90.148 ? 44  GLU   A N    1 ? 1 
ATOM   468  C CA   . GLU   A 1 32  ? -18.328 27.467 -9.02   1   91.459 ? 44  GLU   A CA   1 ? 1 
ATOM   469  C C    . GLU   A 1 32  ? -18.097 28.39  -7.814  1   87.703 ? 44  GLU   A C    1 ? 1 
ATOM   470  O O    . GLU   A 1 32  ? -17.612 29.515 -7.958  1   92.732 ? 44  GLU   A O    1 ? 1 
ATOM   471  C CB   . GLU   A 1 32  ? -18.649 28.22  -10.317 1   87.215 ? 44  GLU   A CB   1 ? 1 
ATOM   472  H H    . GLU   A 1 32  ? -19.124 25.596 -8.701  1   87.195 ? 44  GLU   A H    1 c 1 
ATOM   473  H HA   . GLU   A 1 32  ? -17.485 26.976 -9.181  1   86.653 ? 44  GLU   A HA   1 c 1 
ATOM   474  H HB2  . GLU   A 1 32  ? -17.795 28.438 -10.72  0   30     ? 44  GLU   A HB2  1 c 1 
ATOM   475  H HB3  . GLU   A 1 32  ? -19.608 28.241 -10.37  0   30     ? 44  GLU   A HB3  1 c 1 
ATOM   476  N N    . GLU   A 1 33  ? -18.463 27.904 -6.62   1   75.068 ? 45  GLU   A N    1 ? 1 
ATOM   477  C CA   . GLU   A 1 33  ? -18.172 28.593 -5.378  1   67.305 ? 45  GLU   A CA   1 ? 1 
ATOM   478  C C    . GLU   A 1 33  ? -17.74  27.536 -4.362  1   58.224 ? 45  GLU   A C    1 ? 1 
ATOM   479  O O    . GLU   A 1 33  ? -18.493 26.619 -4.038  1   54.411 ? 45  GLU   A O    1 ? 1 
ATOM   480  C CB   . GLU   A 1 33  ? -19.362 29.422 -4.895  1   66.969 ? 45  GLU   A CB   1 ? 1 
ATOM   481  H H    . GLU   A 1 33  ? -18.895 27.101 -6.576  1   75.111 ? 45  GLU   A H    1 c 1 
ATOM   482  H HA   . GLU   A 1 33  ? -17.411 29.208 -5.534  1   67.024 ? 45  GLU   A HA   1 c 1 
ATOM   483  H HB2  . GLU   A 1 33  ? -19.03  30.197 -4.287  0   30     ? 45  GLU   A HB2  1 c 1 
ATOM   484  H HB3  . GLU   A 1 33  ? -20.225 29.012 -5.072  0   30     ? 45  GLU   A HB3  1 c 1 
ATOM   485  N N    . THR   A 1 34  ? -16.516 27.682 -3.866  1   54.567 ? 46  THR   A N    1 ? 1 
ATOM   486  C CA   . THR   A 1 34  ? -16.037 26.864 -2.767  1   50.192 ? 46  THR   A CA   1 ? 1 
ATOM   487  C C    . THR   A 1 34  ? -16.353 27.592 -1.466  1   53.812 ? 46  THR   A C    1 ? 1 
ATOM   488  O O    . THR   A 1 34  ? -16.643 28.779 -1.499  1   57.673 ? 46  THR   A O    1 ? 1 
ATOM   489  C CB   . THR   A 1 34  ? -14.544 26.629 -2.961  1   45.71  ? 46  THR   A CB   1 ? 1 
ATOM   490  O OG1  . THR   A 1 34  ? -13.961 27.925 -2.856  1   42.966 ? 46  THR   A OG1  1 ? 1 
ATOM   491  C CG2  . THR   A 1 34  ? -14.238 25.988 -4.306  1   46.193 ? 46  THR   A CG2  1 ? 1 
ATOM   492  H H    . THR   A 1 34  ? -15.956 28.311 -4.223  1   55.156 ? 46  THR   A H    1 c 1 
ATOM   493  H HA   . THR   A 1 34  ? -16.502 26.001 -2.78   1   49.904 ? 46  THR   A HA   1 c 1 
ATOM   494  H HB   . THR   A 1 34  ? -14.199 26.054 -2.238  1   43.843 ? 46  THR   A HB   1 c 1 
ATOM   495  H HG1  . THR   A 1 34  ? -14.298 28.465 -3.388  0   30     ? 46  THR   A HG1  1 c 1 
ATOM   496  H HG21 . THR   A 1 34  ? -13.321 25.667 -4.311  1   44.586 ? 46  THR   A HG21 1 c 1 
ATOM   497  H HG22 . THR   A 1 34  ? -14.355 26.643 -5.014  1   47.473 ? 46  THR   A HG22 1 c 1 
ATOM   498  H HG23 . THR   A 1 34  ? -14.842 25.241 -4.454  1   45.742 ? 46  THR   A HG23 1 c 1 
ATOM   499  N N    . PRO   A 1 35  ? -16.279 26.944 -0.281  1   54.99  ? 47  PRO   A N    1 ? 1 
ATOM   500  C CA   . PRO   A 1 35  ? -16.354 27.69  0.967   1   55.019 ? 47  PRO   A CA   1 ? 1 
ATOM   501  C C    . PRO   A 1 35  ? -15.137 28.577 1.184   1   56.734 ? 47  PRO   A C    1 ? 1 
ATOM   502  O O    . PRO   A 1 35  ? -14.032 28.243 0.758   1   61.165 ? 47  PRO   A O    1 ? 1 
ATOM   503  C CB   . PRO   A 1 35  ? -16.456 26.617 2.04    1   51.405 ? 47  PRO   A CB   1 ? 1 
ATOM   504  C CG   . PRO   A 1 35  ? -15.865 25.378 1.405   1   48.539 ? 47  PRO   A CG   1 ? 1 
ATOM   505  C CD   . PRO   A 1 35  ? -16.083 25.497 -0.081  1   50.305 ? 47  PRO   A CD   1 ? 1 
ATOM   506  H HA   . PRO   A 1 35  ? -17.167 28.237 0.972   1   57.081 ? 47  PRO   A HA   1 c 1 
ATOM   507  H HB2  . PRO   A 1 35  ? -15.953 26.872 2.838   1   51.261 ? 47  PRO   A HB2  1 c 1 
ATOM   508  H HB3  . PRO   A 1 35  ? -17.386 26.466 2.294   1   52.702 ? 47  PRO   A HB3  1 c 1 
ATOM   509  H HG2  . PRO   A 1 35  ? -14.909 25.315 1.603   1   47.621 ? 47  PRO   A HG2  1 c 1 
ATOM   510  H HG3  . PRO   A 1 35  ? -16.305 24.574 1.748   1   48.461 ? 47  PRO   A HG3  1 c 1 
ATOM   511  H HD2  . PRO   A 1 35  ? -15.305 25.181 -0.576  1   49.221 ? 47  PRO   A HD2  1 c 1 
ATOM   512  H HD3  . PRO   A 1 35  ? -16.873 24.997 -0.366  1   51.104 ? 47  PRO   A HD3  1 c 1 
ATOM   513  N N    . MET   A 1 36  ? -15.365 29.712 1.855   1   58.768 ? 48  MET   A N    1 ? 1 
ATOM   514  C CA   . MET   A 1 36  ? -14.302 30.651 2.164   1   57.777 ? 48  MET   A CA   1 ? 1 
ATOM   515  C C    . MET   A 1 36  ? -13.94  30.562 3.64    1   53.935 ? 48  MET   A C    1 ? 1 
ATOM   516  O O    . MET   A 1 36  ? -14.745 30.123 4.457   1   51.615 ? 48  MET   A O    1 ? 1 
ATOM   517  C CB   . MET   A 1 36  ? -14.729 32.084 1.848   1   63.994 ? 48  MET   A CB   1 ? 1 
ATOM   518  C CG   . MET   A 1 36  ? -15.121 32.307 0.401   1   65.369 ? 48  MET   A CG   1 ? 1 
ATOM   519  S SD   . MET   A 1 36  ? -14.218 33.72  -0.249  1   66.19  ? 48  MET   A SD   1 ? 1 
ATOM   520  C CE   . MET   A 1 36  ? -12.738 33.052 -1.023  1   63.305 ? 48  MET   A CE   1 ? 1 
ATOM   521  H H    . MET   A 1 36  ? -16.216 29.911 2.122   1   59.712 ? 48  MET   A H    1 c 1 
ATOM   522  H HA   . MET   A 1 36  ? -13.504 30.418 1.625   1   56.776 ? 48  MET   A HA   1 c 1 
ATOM   523  H HB2  . MET   A 1 36  ? -15.489 32.317 2.421   1   64.613 ? 48  MET   A HB2  1 c 1 
ATOM   524  H HB3  . MET   A 1 36  ? -13.989 32.687 2.075   1   63.782 ? 48  MET   A HB3  1 c 1 
ATOM   525  H HG2  . MET   A 1 36  ? -14.908 31.514 -0.13   1   63.275 ? 48  MET   A HG2  1 c 1 
ATOM   526  H HG3  . MET   A 1 36  ? -16.082 32.477 0.337   1   66.569 ? 48  MET   A HG3  1 c 1 
ATOM   527  H HE1  . MET   A 1 36  ? -12.096 33.772 -1.169  1   64.523 ? 48  MET   A HE1  1 c 1 
ATOM   528  H HE2  . MET   A 1 36  ? -12.344 32.376 -0.441  1   61.253 ? 48  MET   A HE2  1 c 1 
ATOM   529  H HE3  . MET   A 1 36  ? -12.973 32.648 -1.878  1   63.062 ? 48  MET   A HE3  1 c 1 
ATOM   530  N N    . ILE   A 1 37  ? -12.738 31.032 3.977   1   53.573 ? 49  ILE   A N    1 ? 1 
ATOM   531  C CA   . ILE   A 1 37  ? -12.259 30.958 5.348   1   52.109 ? 49  ILE   A CA   1 ? 1 
ATOM   532  C C    . ILE   A 1 37  ? -13.277 31.615 6.28    1   52.472 ? 49  ILE   A C    1 ? 1 
ATOM   533  O O    . ILE   A 1 37  ? -13.764 32.706 6.012   1   55.404 ? 49  ILE   A O    1 ? 1 
ATOM   534  C CB   . ILE   A 1 37  ? -10.872 31.603 5.506   1   54.549 ? 49  ILE   A CB   1 ? 1 
ATOM   535  C CG1  . ILE   A 1 37  ? -9.809  30.907 4.652   1   53.856 ? 49  ILE   A CG1  1 ? 1 
ATOM   536  C CG2  . ILE   A 1 37  ? -10.483 31.653 6.991   1   53.873 ? 49  ILE   A CG2  1 ? 1 
ATOM   537  C CD1  . ILE   A 1 37  ? -8.415  31.487 4.81    1   54.068 ? 49  ILE   A CD1  1 ? 1 
ATOM   538  H H    . ILE   A 1 37  ? -12.209 31.419 3.34    1   53.797 ? 49  ILE   A H    1 c 1 
ATOM   539  H HA   . ILE   A 1 37  ? -12.183 30.014 5.589   1   50.402 ? 49  ILE   A HA   1 c 1 
ATOM   540  H HB   . ILE   A 1 37  ? -10.942 32.526 5.188   1   56.248 ? 49  ILE   A HB   1 c 1 
ATOM   541  H HG12 . ILE   A 1 37  ? -9.785  29.958 4.892   1   51.642 ? 49  ILE   A HG12 1 c 1 
ATOM   542  H HG13 . ILE   A 1 37  ? -10.069 30.971 3.71    1   53.771 ? 49  ILE   A HG13 1 c 1 
ATOM   543  H HG21 . ILE   A 1 37  ? -9.564  31.955 7.08    1   54.073 ? 49  ILE   A HG21 1 c 1 
ATOM   544  H HG22 . ILE   A 1 37  ? -10.57  30.767 7.381   1   52.383 ? 49  ILE   A HG22 1 c 1 
ATOM   545  H HG23 . ILE   A 1 37  ? -11.068 32.27  7.463   1   55.905 ? 49  ILE   A HG23 1 c 1 
ATOM   546  H HD11 . ILE   A 1 37  ? -8.475  32.452 4.943   1   56.182 ? 49  ILE   A HD11 1 c 1 
ATOM   547  H HD12 . ILE   A 1 37  ? -7.892  31.303 4.008   1   53.462 ? 49  ILE   A HD12 1 c 1 
ATOM   548  H HD13 . ILE   A 1 37  ? -7.978  31.08  5.582   1   53.062 ? 49  ILE   A HD13 1 c 1 
ATOM   549  N N    . GLY   A 1 38  ? -13.572 30.938 7.391   1   50.504 ? 50  GLY   A N    1 ? 1 
ATOM   550  C CA   . GLY   A 1 38  ? -14.532 31.404 8.375   1   51.731 ? 50  GLY   A CA   1 ? 1 
ATOM   551  C C    . GLY   A 1 38  ? -15.907 30.769 8.194   1   50.739 ? 50  GLY   A C    1 ? 1 
ATOM   552  O O    . GLY   A 1 38  ? -16.725 30.847 9.102   1   52.647 ? 50  GLY   A O    1 ? 1 
ATOM   553  H H    . GLY   A 1 38  ? -13.15  30.143 7.544   1   48.634 ? 50  GLY   A H    1 c 1 
ATOM   554  H HA2  . GLY   A 1 38  ? -14.192 31.19  9.276   1   51.2   ? 50  GLY   A HA2  1 c 1 
ATOM   555  H HA3  . GLY   A 1 38  ? -14.613 32.384 8.311   1   53.8   ? 50  GLY   A HA3  1 c 1 
ATOM   556  N N    . ASP   A 1 39  ? -16.163 30.153 7.03    1   49.172 ? 51  ASP   A N    1 ? 1 
ATOM   557  C CA   . ASP   A 1 39  ? -17.479 29.592 6.749   1   48.95  ? 51  ASP   A CA   1 ? 1 
ATOM   558  C C    . ASP   A 1 39  ? -17.78  28.442 7.703   1   48.19  ? 51  ASP   A C    1 ? 1 
ATOM   559  O O    . ASP   A 1 39  ? -16.875 27.739 8.12    1   45.612 ? 51  ASP   A O    1 ? 1 
ATOM   560  C CB   . ASP   A 1 39  ? -17.59  29.113 5.309   1   49.155 ? 51  ASP   A CB   1 ? 1 
ATOM   561  C CG   . ASP   A 1 39  ? -17.785 30.205 4.266   1   51.882 ? 51  ASP   A CG   1 ? 1 
ATOM   562  O OD1  . ASP   A 1 39  ? -17.904 31.389 4.652   1   53.06  ? 51  ASP   A OD1  1 ? 1 
ATOM   563  O OD2  . ASP   A 1 39  ? -17.827 29.864 3.07    1   52.632 ? 51  ASP   A OD2  1 ? 1 
ATOM   564  H H    . ASP   A 1 39  ? -15.508 30.078 6.398   1   47.999 ? 51  ASP   A H    1 c 1 
ATOM   565  H HA   . ASP   A 1 39  ? -18.15  30.297 6.89    1   51.719 ? 51  ASP   A HA   1 c 1 
ATOM   566  H HB2  . ASP   A 1 39  ? -16.781 28.61  5.079   1   47.053 ? 51  ASP   A HB2  1 c 1 
ATOM   567  H HB3  . ASP   A 1 39  ? -18.35  28.499 5.241   1   49.115 ? 51  ASP   A HB3  1 c 1 
ATOM   568  N N    . LYS   A 1 40  ? -19.054 28.227 8.037   1   49.328 ? 52  LYS   A N    1 ? 1 
ATOM   569  C CA   . LYS   A 1 40  ? -19.442 27.026 8.767   1   50.092 ? 52  LYS   A CA   1 ? 1 
ATOM   570  C C    . LYS   A 1 40  ? -19.666 25.899 7.76    1   48.62  ? 52  LYS   A C    1 ? 1 
ATOM   571  O O    . LYS   A 1 40  ? -20.504 26.052 6.875   1   50.158 ? 52  LYS   A O    1 ? 1 
ATOM   572  C CB   . LYS   A 1 40  ? -20.707 27.273 9.593   1   55.621 ? 52  LYS   A CB   1 ? 1 
ATOM   573  C CG   . LYS   A 1 40  ? -21.144 26.113 10.473  1   57.338 ? 52  LYS   A CG   1 ? 1 
ATOM   574  C CD   . LYS   A 1 40  ? -22.52  26.366 11.071  1   64.109 ? 52  LYS   A CD   1 ? 1 
ATOM   575  C CE   . LYS   A 1 40  ? -22.865 25.463 12.224  1   66.439 ? 52  LYS   A CE   1 ? 1 
ATOM   576  N NZ   . LYS   A 1 40  ? -24.284 25.551 12.6    1   70.662 ? 52  LYS   A NZ   1 ? 1 
ATOM   577  H H    . LYS   A 1 40  ? -19.695 28.837 7.809   1   51.783 ? 52  LYS   A H    1 c 1 
ATOM   578  H HA   . LYS   A 1 40  ? -18.705 26.773 9.378   1   48.934 ? 52  LYS   A HA   1 c 1 
ATOM   579  H HB2  . LYS   A 1 40  ? -20.557 28.056 10.166  1   56.622 ? 52  LYS   A HB2  1 c 1 
ATOM   580  H HB3  . LYS   A 1 40  ? -21.442 27.491 8.982   1   56.763 ? 52  LYS   A HB3  1 c 1 
ATOM   581  H HG2  . LYS   A 1 40  ? -21.168 25.291 9.937   1   56.331 ? 52  LYS   A HG2  1 c 1 
ATOM   582  H HG3  . LYS   A 1 40  ? -20.489 25.994 11.196  1   56.721 ? 52  LYS   A HG3  1 c 1 
ATOM   583  H HD2  . LYS   A 1 40  ? -22.563 27.298 11.377  1   65.208 ? 52  LYS   A HD2  1 c 1 
ATOM   584  H HD3  . LYS   A 1 40  ? -23.194 26.256 10.367  1   64.42  ? 52  LYS   A HD3  1 c 1 
ATOM   585  H HE2  . LYS   A 1 40  ? -22.663 24.543 11.98   1   64.344 ? 52  LYS   A HE2  1 c 1 
ATOM   586  H HE3  . LYS   A 1 40  ? -22.318 25.699 12.995  1   65.93  ? 52  LYS   A HE3  1 c 1 
ATOM   587  H HZ1  . LYS   A 1 40  ? -24.8   25.228 11.928  1   70.615 ? 52  LYS   A HZ1  1 c 1 
ATOM   588  H HZ2  . LYS   A 1 40  ? -24.507 26.415 12.757  1   72.035 ? 52  LYS   A HZ2  1 c 1 
ATOM   589  H HZ3  . LYS   A 1 40  ? -24.433 25.064 13.35   1   70.748 ? 52  LYS   A HZ3  1 c 1 
ATOM   590  N N    . VAL   A 1 41  ? -18.928 24.782 7.904   1   44.768 ? 53  VAL   A N    1 ? 1 
ATOM   591  C CA   . VAL   A 1 41  ? -18.882 23.733 6.893   1   43.208 ? 53  VAL   A CA   1 ? 1 
ATOM   592  C C    . VAL   A 1 41  ? -19.434 22.42  7.456   1   41.847 ? 53  VAL   A C    1 ? 1 
ATOM   593  O O    . VAL   A 1 41  ? -19.171 22.059 8.613   1   40.482 ? 53  VAL   A O    1 ? 1 
ATOM   594  C CB   . VAL   A 1 41  ? -17.442 23.582 6.359   1   42.324 ? 53  VAL   A CB   1 ? 1 
ATOM   595  C CG1  . VAL   A 1 41  ? -17.312 22.392 5.427   1   41.523 ? 53  VAL   A CG1  1 ? 1 
ATOM   596  C CG2  . VAL   A 1 41  ? -16.974 24.848 5.654   1   43.763 ? 53  VAL   A CG2  1 ? 1 
ATOM   597  H H    . VAL   A 1 41  ? -18.436 24.672 8.667   1   44.491 ? 53  VAL   A H    1 c 1 
ATOM   598  H HA   . VAL   A 1 41  ? -19.451 24.006 6.147   1   44.211 ? 53  VAL   A HA   1 c 1 
ATOM   599  H HB   . VAL   A 1 41  ? -16.856 23.428 7.136   1   41.522 ? 53  VAL   A HB   1 c 1 
ATOM   600  H HG11 . VAL   A 1 41  ? -18.129 22.294 4.91    1   42.204 ? 53  VAL   A HG11 1 c 1 
ATOM   601  H HG12 . VAL   A 1 41  ? -17.161 21.586 5.949   1   40.494 ? 53  VAL   A HG12 1 c 1 
ATOM   602  H HG13 . VAL   A 1 41  ? -16.563 22.531 4.824   1   40.191 ? 53  VAL   A HG13 1 c 1 
ATOM   603  H HG21 . VAL   A 1 41  ? -16.066 24.724 5.331   1   42.07  ? 53  VAL   A HG21 1 c 1 
ATOM   604  H HG22 . VAL   A 1 41  ? -16.994 25.594 6.277   1   44.499 ? 53  VAL   A HG22 1 c 1 
ATOM   605  H HG23 . VAL   A 1 41  ? -17.561 25.038 4.904   1   44.434 ? 53  VAL   A HG23 1 c 1 
ATOM   606  N N    . TYR   A 1 42  ? -20.213 21.714 6.617   1   38.82  ? 54  TYR   A N    1 ? 1 
ATOM   607  C CA   . TYR   A 1 42  ? -20.85  20.453 6.977   1   39.677 ? 54  TYR   A CA   1 ? 1 
ATOM   608  C C    . TYR   A 1 42  ? -20.353 19.35  6.042   1   38.329 ? 54  TYR   A C    1 ? 1 
ATOM   609  O O    . TYR   A 1 42  ? -20.498 19.467 4.814   1   36.155 ? 54  TYR   A O    1 ? 1 
ATOM   610  C CB   . TYR   A 1 42  ? -22.382 20.547 6.865   1   44.004 ? 54  TYR   A CB   1 ? 1 
ATOM   611  C CG   . TYR   A 1 42  ? -23.066 21.627 7.705   1   47.248 ? 54  TYR   A CG   1 ? 1 
ATOM   612  C CD1  . TYR   A 1 42  ? -23.003 22.972 7.35    1   48.873 ? 54  TYR   A CD1  1 ? 1 
ATOM   613  C CD2  . TYR   A 1 42  ? -23.755 21.302 8.865   1   49.384 ? 54  TYR   A CD2  1 ? 1 
ATOM   614  C CE1  . TYR   A 1 42  ? -23.606 23.955 8.117   1   52.245 ? 54  TYR   A CE1  1 ? 1 
ATOM   615  C CE2  . TYR   A 1 42  ? -24.369 22.275 9.634   1   54.259 ? 54  TYR   A CE2  1 ? 1 
ATOM   616  C CZ   . TYR   A 1 42  ? -24.287 23.605 9.263   1   55.02  ? 54  TYR   A CZ   1 ? 1 
ATOM   617  O OH   . TYR   A 1 42  ? -24.904 24.553 10.025  1   59.507 ? 54  TYR   A OH   1 ? 1 
ATOM   618  H H    . TYR   A 1 42  ? -20.351 22.038 5.774   1   40.025 ? 54  TYR   A H    1 c 1 
ATOM   619  H HA   . TYR   A 1 42  ? -20.609 20.222 7.912   1   39.694 ? 54  TYR   A HA   1 c 1 
ATOM   620  H HB2  . TYR   A 1 42  ? -22.61  20.699 5.92    1   44.118 ? 54  TYR   A HB2  1 c 1 
ATOM   621  H HB3  . TYR   A 1 42  ? -22.76  19.674 7.114   1   44.302 ? 54  TYR   A HB3  1 c 1 
ATOM   622  H HD1  . TYR   A 1 42  ? -22.533 23.221 6.571   1   47.962 ? 54  TYR   A HD1  1 c 1 
ATOM   623  H HD2  . TYR   A 1 42  ? -23.814 20.398 9.132   1   49.6   ? 54  TYR   A HD2  1 c 1 
ATOM   624  H HE1  . TYR   A 1 42  ? -23.555 24.858 7.855   1   53     ? 54  TYR   A HE1  1 c 1 
ATOM   625  H HE2  . TYR   A 1 42  ? -24.835 22.034 10.416  1   54.909 ? 54  TYR   A HE2  1 c 1 
ATOM   626  H HH   . TYR   A 1 42  ? -24.76  25.379 9.598   0   30     ? 54  TYR   A HH   1 c 1 
ATOM   627  N N    . VAL   A 1 43  ? -19.833 18.254 6.622   1   35.649 ? 55  VAL   A N    1 ? 1 
ATOM   628  C CA   . VAL   A 1 43  ? -19.326 17.164 5.796   1   35.797 ? 55  VAL   A CA   1 ? 1 
ATOM   629  C C    . VAL   A 1 43  ? -19.776 15.816 6.34    1   35.7   ? 55  VAL   A C    1 ? 1 
ATOM   630  O O    . VAL   A 1 43  ? -20.17  15.704 7.493   1   36.432 ? 55  VAL   A O    1 ? 1 
ATOM   631  C CB   . VAL   A 1 43  ? -17.785 17.179 5.669   1   33.371 ? 55  VAL   A CB   1 ? 1 
ATOM   632  C CG1  . VAL   A 1 43  ? -17.277 18.51  5.136   1   33.178 ? 55  VAL   A CG1  1 ? 1 
ATOM   633  C CG2  . VAL   A 1 43  ? -17.093 16.822 6.984   1   32.549 ? 55  VAL   A CG2  1 ? 1 
ATOM   634  H H    . VAL   A 1 43  ? -19.794 18.184 7.532   1   36.544 ? 55  VAL   A H    1 c 1 
ATOM   635  H HA   . VAL   A 1 43  ? -19.702 17.265 4.903   1   35.855 ? 55  VAL   A HA   1 c 1 
ATOM   636  H HB   . VAL   A 1 43  ? -17.544 16.486 5.011   1   32.926 ? 55  VAL   A HB   1 c 1 
ATOM   637  H HG11 . VAL   A 1 43  ? -17.42  19.203 5.803   1   33.631 ? 55  VAL   A HG11 1 c 1 
ATOM   638  H HG12 . VAL   A 1 43  ? -17.758 18.739 4.323   1   33.747 ? 55  VAL   A HG12 1 c 1 
ATOM   639  H HG13 . VAL   A 1 43  ? -16.328 18.44  4.941   1   31.69  ? 55  VAL   A HG13 1 c 1 
ATOM   640  H HG21 . VAL   A 1 43  ? -16.134 16.927 6.881   1   31.225 ? 55  VAL   A HG21 1 c 1 
ATOM   641  H HG22 . VAL   A 1 43  ? -17.291 15.9   7.219   1   32.952 ? 55  VAL   A HG22 1 c 1 
ATOM   642  H HG23 . VAL   A 1 43  ? -17.409 17.411 7.689   1   33.32  ? 55  VAL   A HG23 1 c 1 
ATOM   643  N N    . HIS   A 1 44  ? -19.719 14.801 5.474   1   36.31  ? 56  HIS   A N    1 ? 1 
ATOM   644  C CA   . HIS   A 1 44  ? -19.541 13.422 5.904   1   38.054 ? 56  HIS   A CA   1 ? 1 
ATOM   645  C C    . HIS   A 1 44  ? -18.157 12.996 5.43    1   35.358 ? 56  HIS   A C    1 ? 1 
ATOM   646  O O    . HIS   A 1 44  ? -17.669 13.482 4.421   1   34.97  ? 56  HIS   A O    1 ? 1 
ATOM   647  C CB   . HIS   A 1 44  ? -20.651 12.494 5.389   1   42.58  ? 56  HIS   A CB   1 ? 1 
ATOM   648  C CG   . HIS   A 1 44  ? -21.893 12.467 6.227   1   47.971 ? 56  HIS   A CG   1 ? 1 
ATOM   649  N ND1  . HIS   A 1 44  ? -21.89  12.048 7.543   1   51.404 ? 56  HIS   A ND1  1 ? 1 
ATOM   650  C CD2  . HIS   A 1 44  ? -23.154 12.813 5.951   1   51.585 ? 56  HIS   A CD2  1 ? 1 
ATOM   651  C CE1  . HIS   A 1 44  ? -23.124 12.124 8.034   1   54.152 ? 56  HIS   A CE1  1 ? 1 
ATOM   652  N NE2  . HIS   A 1 44  ? -23.91  12.588 7.078   1   55.14  ? 56  HIS   A NE2  1 ? 1 
ATOM   653  H H    . HIS   A 1 44  ? -19.795 14.974 4.579   1   36.397 ? 56  HIS   A H    1 c 1 
ATOM   654  H HA   . HIS   A 1 44  ? -19.548 13.402 6.892   1   38.362 ? 56  HIS   A HA   1 c 1 
ATOM   655  H HB2  . HIS   A 1 44  ? -20.891 12.773 4.478   1   42.789 ? 56  HIS   A HB2  1 c 1 
ATOM   656  H HB3  . HIS   A 1 44  ? -20.292 11.582 5.329   1   42.544 ? 56  HIS   A HB3  1 c 1 
ATOM   657  H HD1  . HIS   A 1 44  ? -21.088 11.669 8.013   0   30     ? 56  HIS   A HD1  1 c 1 
ATOM   658  H HD2  . HIS   A 1 44  ? -23.477 13.137 5.133   1   51.887 ? 56  HIS   A HD2  1 c 1 
ATOM   659  H HE1  . HIS   A 1 44  ? -23.389 11.895 8.909   1   55.193 ? 56  HIS   A HE1  1 c 1 
ATOM   660  H HE2  . HIS   A 1 44  ? -24.683 12.747 7.301   0   30     ? 56  HIS   A HE2  1 c 1 
ATOM   661  N N    . TYR   A 1 45  ? -17.521 12.109 6.191   1   35.214 ? 57  TYR   A N    1 ? 1 
ATOM   662  C CA   . TYR   A 1 45  ? -16.163 11.69  5.887   1   33.164 ? 57  TYR   A CA   1 ? 1 
ATOM   663  C C    . TYR   A 1 45  ? -15.97  10.26  6.373   1   34.358 ? 57  TYR   A C    1 ? 1 
ATOM   664  O O    . TYR   A 1 45  ? -16.662 9.805  7.289   1   37.896 ? 57  TYR   A O    1 ? 1 
ATOM   665  C CB   . TYR   A 1 45  ? -15.126 12.631 6.515   1   29.092 ? 57  TYR   A CB   1 ? 1 
ATOM   666  C CG   . TYR   A 1 45  ? -14.953 12.442 8.021   1   30.456 ? 57  TYR   A CG   1 ? 1 
ATOM   667  C CD1  . TYR   A 1 45  ? -15.736 13.133 8.946   1   31.274 ? 57  TYR   A CD1  1 ? 1 
ATOM   668  C CD2  . TYR   A 1 45  ? -14.054 11.507 8.516   1   29.686 ? 57  TYR   A CD2  1 ? 1 
ATOM   669  C CE1  . TYR   A 1 45  ? -15.597 12.922 10.314  1   33.204 ? 57  TYR   A CE1  1 ? 1 
ATOM   670  C CE2  . TYR   A 1 45  ? -13.892 11.311 9.878   1   32.277 ? 57  TYR   A CE2  1 ? 1 
ATOM   671  C CZ   . TYR   A 1 45  ? -14.666 12.011 10.777  1   32.542 ? 57  TYR   A CZ   1 ? 1 
ATOM   672  O OH   . TYR   A 1 45  ? -14.486 11.768 12.107  1   38.029 ? 57  TYR   A OH   1 ? 1 
ATOM   673  H H    . TYR   A 1 45  ? -17.942 11.754 6.92    1   36.181 ? 57  TYR   A H    1 c 1 
ATOM   674  H HA   . TYR   A 1 45  ? -16.047 11.706 4.903   1   32.495 ? 57  TYR   A HA   1 c 1 
ATOM   675  H HB2  . TYR   A 1 45  ? -14.26  12.482 6.074   1   28.717 ? 57  TYR   A HB2  1 c 1 
ATOM   676  H HB3  . TYR   A 1 45  ? -15.399 13.559 6.34    1   29.714 ? 57  TYR   A HB3  1 c 1 
ATOM   677  H HD1  . TYR   A 1 45  ? -16.373 13.758 8.638   1   32.13  ? 57  TYR   A HD1  1 c 1 
ATOM   678  H HD2  . TYR   A 1 45  ? -13.512 11.024 7.914   1   29.706 ? 57  TYR   A HD2  1 c 1 
ATOM   679  H HE1  . TYR   A 1 45  ? -16.121 13.411 10.925  1   33.732 ? 57  TYR   A HE1  1 c 1 
ATOM   680  H HE2  . TYR   A 1 45  ? -13.266 10.682 10.189  1   31.581 ? 57  TYR   A HE2  1 c 1 
ATOM   681  H HH   . TYR   A 1 45  ? -14.999 12.22  12.621  0   30     ? 57  TYR   A HH   1 c 1 
ATOM   682  N N    . LYS   A 1 46  ? -15.014 9.58   5.745   1   35.109 ? 58  LYS   A N    1 ? 1 
ATOM   683  C CA   . LYS   A 1 46  ? -14.451 8.33   6.225   1   37.102 ? 58  LYS   A CA   1 ? 1 
ATOM   684  C C    . LYS   A 1 46  ? -12.945 8.546  6.23    1   35.651 ? 58  LYS   A C    1 ? 1 
ATOM   685  O O    . LYS   A 1 46  ? -12.388 9.081  5.279   1   35.855 ? 58  LYS   A O    1 ? 1 
ATOM   686  C CB   . LYS   A 1 46  ? -14.866 7.119  5.366   1   37.593 ? 58  LYS   A CB   1 ? 1 
ATOM   687  H H    . LYS   A 1 46  ? -14.692 9.918  4.959   1   34.153 ? 58  LYS   A H    1 c 1 
ATOM   688  H HA   . LYS   A 1 46  ? -14.757 8.184  7.154   1   37.532 ? 58  LYS   A HA   1 c 1 
ATOM   689  H HB2  . LYS   A 1 46  ? -14.069 6.624  5.051   0   30     ? 58  LYS   A HB2  1 c 1 
ATOM   690  H HB3  . LYS   A 1 46  ? -15.86  7.038  5.327   0   30     ? 58  LYS   A HB3  1 c 1 
ATOM   691  N N    . GLY   A 1 47  ? -12.291 8.133  7.309   1   36.402 ? 59  GLY   A N    1 ? 1 
ATOM   692  C CA   . GLY   A 1 47  ? -10.883 8.417  7.497   1   34.561 ? 59  GLY   A CA   1 ? 1 
ATOM   693  C C    . GLY   A 1 47  ? -10.163 7.194  8.034   1   37.561 ? 59  GLY   A C    1 ? 1 
ATOM   694  O O    . GLY   A 1 47  ? -10.736 6.402  8.785   1   42.178 ? 59  GLY   A O    1 ? 1 
ATOM   695  H H    . GLY   A 1 47  ? -12.734 7.656  7.95    1   37.409 ? 59  GLY   A H    1 c 1 
ATOM   696  H HA2  . GLY   A 1 47  ? -10.486 8.687  6.639   1   34.168 ? 59  GLY   A HA2  1 c 1 
ATOM   697  H HA3  . GLY   A 1 47  ? -10.785 9.166  8.13    1   34.441 ? 59  GLY   A HA3  1 c 1 
ATOM   698  N N    . LYS   A 1 48  ? -8.904  7.037  7.635   1   36.827 ? 60  LYS   A N    1 ? 1 
ATOM   699  C CA   . LYS   A 1 48  ? -8.115  5.923  8.123   1   39.173 ? 60  LYS   A CA   1 ? 1 
ATOM   700  C C    . LYS   A 1 48  ? -6.65   6.287  7.997   1   35.245 ? 60  LYS   A C    1 ? 1 
ATOM   701  O O    . LYS   A 1 48  ? -6.326  7.222  7.268   1   33.659 ? 60  LYS   A O    1 ? 1 
ATOM   702  C CB   . LYS   A 1 48  ? -8.469  4.642  7.364   1   44.301 ? 60  LYS   A CB   1 ? 1 
ATOM   703  C CG   . LYS   A 1 48  ? -8.151  4.627  5.883   1   45.863 ? 60  LYS   A CG   1 ? 1 
ATOM   704  C CD   . LYS   A 1 48  ? -8.163  3.215  5.307   1   51.494 ? 60  LYS   A CD   1 ? 1 
ATOM   705  C CE   . LYS   A 1 48  ? -7.839  3.203  3.84    1   56.692 ? 60  LYS   A CE   1 ? 1 
ATOM   706  N NZ   . LYS   A 1 48  ? -7.584  1.858  3.31    1   60.669 ? 60  LYS   A NZ   1 ? 1 
ATOM   707  H H    . LYS   A 1 48  ? -8.528  7.631  7.05    1   35.864 ? 60  LYS   A H    1 c 1 
ATOM   708  H HA   . LYS   A 1 48  ? -8.322  5.79   9.083   1   39.675 ? 60  LYS   A HA   1 c 1 
ATOM   709  H HB2  . LYS   A 1 48  ? -7.993  3.895  7.785   1   45.066 ? 60  LYS   A HB2  1 c 1 
ATOM   710  H HB3  . LYS   A 1 48  ? -9.429  4.475  7.472   1   44.997 ? 60  LYS   A HB3  1 c 1 
ATOM   711  H HG2  . LYS   A 1 48  ? -8.809  5.178  5.41    1   45.661 ? 60  LYS   A HG2  1 c 1 
ATOM   712  H HG3  . LYS   A 1 48  ? -7.264  5.023  5.743   1   44.889 ? 60  LYS   A HG3  1 c 1 
ATOM   713  H HD2  . LYS   A 1 48  ? -7.506  2.668  5.786   1   52.479 ? 60  LYS   A HD2  1 c 1 
ATOM   714  H HD3  . LYS   A 1 48  ? -9.051  2.818  5.444   1   53.198 ? 60  LYS   A HD3  1 c 1 
ATOM   715  H HE2  . LYS   A 1 48  ? -8.58   3.598  3.347   1   55.536 ? 60  LYS   A HE2  1 c 1 
ATOM   716  H HE3  . LYS   A 1 48  ? -7.051  3.755  3.684   1   54.351 ? 60  LYS   A HE3  1 c 1 
ATOM   717  H HZ1  . LYS   A 1 48  ? -8.299  1.325  3.469   1   61.623 ? 60  LYS   A HZ1  1 c 1 
ATOM   718  H HZ2  . LYS   A 1 48  ? -6.853  1.504  3.713   1   60.419 ? 60  LYS   A HZ2  1 c 1 
ATOM   719  H HZ3  . LYS   A 1 48  ? -7.439  1.903  2.417   1   60.012 ? 60  LYS   A HZ3  1 c 1 
ATOM   720  N N    . LEU   A 1 49  ? -5.823  5.598  8.783   1   34.101 ? 61  LEU   A N    1 ? 1 
ATOM   721  C CA   . LEU   A 1 49  ? -4.387  5.545  8.584   1   32.405 ? 61  LEU   A CA   1 ? 1 
ATOM   722  C C    . LEU   A 1 49  ? -4.17   4.908  7.207   1   34.969 ? 61  LEU   A C    1 ? 1 
ATOM   723  O O    . LEU   A 1 49  ? -4.892  3.984  6.84    1   35.928 ? 61  LEU   A O    1 ? 1 
ATOM   724  C CB   . LEU   A 1 49  ? -3.77   4.721  9.712   1   32.254 ? 61  LEU   A CB   1 ? 1 
ATOM   725  C CG   . LEU   A 1 49  ? -4.102  5.123  11.156  1   32.179 ? 61  LEU   A CG   1 ? 1 
ATOM   726  C CD1  . LEU   A 1 49  ? -3.219  4.391  12.146  1   33.442 ? 61  LEU   A CD1  1 ? 1 
ATOM   727  C CD2  . LEU   A 1 49  ? -3.983  6.604  11.406  1   30.847 ? 61  LEU   A CD2  1 ? 1 
ATOM   728  H H    . LEU   A 1 49  ? -6.182  5.124  9.477   1   35.426 ? 61  LEU   A H    1 c 1 
ATOM   729  H HA   . LEU   A 1 49  ? -4.022  6.466  8.594   1   31.349 ? 61  LEU   A HA   1 c 1 
ATOM   730  H HB2  . LEU   A 1 49  ? -4.043  3.783  9.585   1   34.07  ? 61  LEU   A HB2  1 c 1 
ATOM   731  H HB3  . LEU   A 1 49  ? -2.791  4.747  9.604   1   32.254 ? 61  LEU   A HB3  1 c 1 
ATOM   732  H HG   . LEU   A 1 49  ? -5.041  4.86   11.34   1   33.217 ? 61  LEU   A HG   1 c 1 
ATOM   733  H HD11 . LEU   A 1 49  ? -3.326  3.432  12.031  1   35.039 ? 61  LEU   A HD11 1 c 1 
ATOM   734  H HD12 . LEU   A 1 49  ? -3.471  4.638  13.052  1   33.836 ? 61  LEU   A HD12 1 c 1 
ATOM   735  H HD13 . LEU   A 1 49  ? -2.29   4.633  11.993  1   32.875 ? 61  LEU   A HD13 1 c 1 
ATOM   736  H HD21 . LEU   A 1 49  ? -4.668  7.076  10.903  1   30     ? 61  LEU   A HD21 1 c 1 
ATOM   737  H HD22 . LEU   A 1 49  ? -3.105  6.912  11.122  1   29.905 ? 61  LEU   A HD22 1 c 1 
ATOM   738  H HD23 . LEU   A 1 49  ? -4.097  6.785  12.354  1   31.077 ? 61  LEU   A HD23 1 c 1 
ATOM   739  N N    . SER   A 1 50  ? -3.244  5.452  6.411   1   35.686 ? 62  SER   A N    1 ? 1 
ATOM   740  C CA   . SER   A 1 50  ? -3.127  5.051  5.015   1   39.404 ? 62  SER   A CA   1 ? 1 
ATOM   741  C C    . SER   A 1 50  ? -2.805  3.563  4.92    1   45.145 ? 62  SER   A C    1 ? 1 
ATOM   742  O O    . SER   A 1 50  ? -3.198  2.906  3.955   1   44.728 ? 62  SER   A O    1 ? 1 
ATOM   743  C CB   . SER   A 1 50  ? -2.095  5.87   4.289   1   40.217 ? 62  SER   A CB   1 ? 1 
ATOM   744  O OG   . SER   A 1 50  ? -0.839  5.754  4.935   1   43.615 ? 62  SER   A OG   1 ? 1 
ATOM   745  H H    . SER   A 1 50  ? -2.673  6.084  6.742   1   34.999 ? 62  SER   A H    1 c 1 
ATOM   746  H HA   . SER   A 1 50  ? -4.004  5.202  4.58    1   39.546 ? 62  SER   A HA   1 c 1 
ATOM   747  H HB2  . SER   A 1 50  ? -2.02   5.557  3.368   1   40.89  ? 62  SER   A HB2  1 c 1 
ATOM   748  H HB3  . SER   A 1 50  ? -2.372  6.806  4.277   1   39.264 ? 62  SER   A HB3  1 c 1 
ATOM   749  H HG   . SER   A 1 50  ? -0.26   6.241  4.61    0   30     ? 62  SER   A HG   1 c 1 
ATOM   750  N N    . ASN   A 1 51  ? -2.035  3.076  5.905   1   46.442 ? 63  ASN   A N    1 ? 1 
ATOM   751  C CA   . ASN   A 1 51  ? -1.769  1.665  6.093   1   53.698 ? 63  ASN   A CA   1 ? 1 
ATOM   752  C C    . ASN   A 1 51  ? -2.55   1.275  7.339   1   58.552 ? 63  ASN   A C    1 ? 1 
ATOM   753  O O    . ASN   A 1 51  ? -2.197  1.683  8.444   1   61.773 ? 63  ASN   A O    1 ? 1 
ATOM   754  C CB   . ASN   A 1 51  ? -0.274  1.361  6.162   1   53.558 ? 63  ASN   A CB   1 ? 1 
ATOM   755  H H    . ASN   A 1 51  ? -1.648  3.666  6.486   1   46.281 ? 63  ASN   A H    1 c 1 
ATOM   756  H HA   . ASN   A 1 51  ? -2.134  1.173  5.324   1   54.096 ? 63  ASN   A HA   1 c 1 
ATOM   757  H HB2  . ASN   A 1 51  ? 0.223   2.196  6.008   0   30     ? 63  ASN   A HB2  1 c 1 
ATOM   758  H HB3  . ASN   A 1 51  ? -0.113  0.392  6.224   0   30     ? 63  ASN   A HB3  1 c 1 
ATOM   759  N N    . GLY   A 1 52  ? -3.625  0.514  7.126   1   61.229 ? 64  GLY   A N    1 ? 1 
ATOM   760  C CA   . GLY   A 1 52  ? -4.708  0.384  8.087   1   61.679 ? 64  GLY   A CA   1 ? 1 
ATOM   761  C C    . GLY   A 1 52  ? -6.011  0.178  7.328   1   60.49  ? 64  GLY   A C    1 ? 1 
ATOM   762  O O    . GLY   A 1 52  ? -6.151  0.656  6.204   1   59.018 ? 64  GLY   A O    1 ? 1 
ATOM   763  H H    . GLY   A 1 52  ? -3.683  0.045  6.343   1   61.606 ? 64  GLY   A H    1 c 1 
ATOM   764  H HA2  . GLY   A 1 52  ? -4.535  -0.384 8.68    1   63.197 ? 64  GLY   A HA2  1 c 1 
ATOM   765  H HA3  . GLY   A 1 52  ? -4.764  1.2    8.638   1   59.929 ? 64  GLY   A HA3  1 c 1 
ATOM   766  N N    . LYS   A 1 53  ? -6.921  -0.594 7.931   1   67.929 ? 65  LYS   A N    1 ? 1 
ATOM   767  C CA   . LYS   A 1 53  ? -8.135  -1.05  7.264   1   68.478 ? 65  LYS   A CA   1 ? 1 
ATOM   768  C C    . LYS   A 1 53  ? -9.335  -0.332 7.885   1   66.851 ? 65  LYS   A C    1 ? 1 
ATOM   769  O O    . LYS   A 1 53  ? -10.149 0.233  7.153   1   69.513 ? 65  LYS   A O    1 ? 1 
ATOM   770  C CB   . LYS   A 1 53  ? -8.253  -2.584 7.278   1   67.946 ? 65  LYS   A CB   1 ? 1 
ATOM   771  H H    . LYS   A 1 53  ? -6.774  -0.854 8.795   1   67.146 ? 65  LYS   A H    1 c 1 
ATOM   772  H HA   . LYS   A 1 53  ? -8.082  -0.776 6.314   1   66.678 ? 65  LYS   A HA   1 c 1 
ATOM   773  H HB2  . LYS   A 1 53  ? -7.173  -2.854 7.167   0   30     ? 65  LYS   A HB2  1 c 1 
ATOM   774  H HB3  . LYS   A 1 53  ? -9.032  -2.876 7.166   0   30     ? 65  LYS   A HB3  1 c 1 
ATOM   775  N N    . LYS   A 1 54  ? -9.398  -0.323 9.23    1   61.894 ? 66  LYS   A N    1 ? 1 
ATOM   776  C CA   . LYS   A 1 54  ? -10.522 0.217  9.986   1   57.997 ? 66  LYS   A CA   1 ? 1 
ATOM   777  C C    . LYS   A 1 54  ? -10.642 1.742  9.816   1   52.052 ? 66  LYS   A C    1 ? 1 
ATOM   778  O O    . LYS   A 1 54  ? -9.731  2.523  10.114  1   48.091 ? 66  LYS   A O    1 ? 1 
ATOM   779  C CB   . LYS   A 1 54  ? -10.423 -0.213 11.457  1   60.105 ? 66  LYS   A CB   1 ? 1 
ATOM   780  H H    . LYS   A 1 54  ? -8.701  -0.682 9.699   1   62.764 ? 66  LYS   A H    1 c 1 
ATOM   781  H HA   . LYS   A 1 54  ? -11.347 -0.195 9.622   1   59.683 ? 66  LYS   A HA   1 c 1 
ATOM   782  H HB2  . LYS   A 1 54  ? -9.471  -0.367 11.705  0   30     ? 66  LYS   A HB2  1 c 1 
ATOM   783  H HB3  . LYS   A 1 54  ? -11.326 -0.405 11.807  0   30     ? 66  LYS   A HB3  1 c 1 
ATOM   784  N N    . PHE   A 1 55  ? -11.83  2.159  9.379   1   49.429 ? 67  PHE   A N    1 ? 1 
ATOM   785  C CA   . PHE   A 1 55  ? -12.14  3.55   9.146   1   47.07  ? 67  PHE   A CA   1 ? 1 
ATOM   786  C C    . PHE   A 1 55  ? -12.776 4.182  10.377  1   47.212 ? 67  PHE   A C    1 ? 1 
ATOM   787  O O    . PHE   A 1 55  ? -13.541 3.533  11.084  1   48.89  ? 67  PHE   A O    1 ? 1 
ATOM   788  C CB   . PHE   A 1 55  ? -13.132 3.689  7.987   1   50.892 ? 67  PHE   A CB   1 ? 1 
ATOM   789  C CG   . PHE   A 1 55  ? -12.516 3.679  6.596   1   51.741 ? 67  PHE   A CG   1 ? 1 
ATOM   790  C CD1  . PHE   A 1 55  ? -11.877 4.807  6.09    1   52.976 ? 67  PHE   A CD1  1 ? 1 
ATOM   791  C CD2  . PHE   A 1 55  ? -12.613 2.557  5.788   1   54.47  ? 67  PHE   A CD2  1 ? 1 
ATOM   792  C CE1  . PHE   A 1 55  ? -11.327 4.801  4.813   1   52.784 ? 67  PHE   A CE1  1 ? 1 
ATOM   793  C CE2  . PHE   A 1 55  ? -12.073 2.557  4.511   1   55.985 ? 67  PHE   A CE2  1 ? 1 
ATOM   794  C CZ   . PHE   A 1 55  ? -11.428 3.675  4.026   1   54.351 ? 67  PHE   A CZ   1 ? 1 
ATOM   795  H H    . PHE   A 1 55  ? -12.482 1.539  9.221   1   51.982 ? 67  PHE   A H    1 c 1 
ATOM   796  H HA   . PHE   A 1 55  ? -11.306 4.036  8.918   1   45.876 ? 67  PHE   A HA   1 c 1 
ATOM   797  H HB2  . PHE   A 1 55  ? -13.784 2.955  8.048   1   52.56  ? 67  PHE   A HB2  1 c 1 
ATOM   798  H HB3  . PHE   A 1 55  ? -13.627 4.53   8.103   1   49.706 ? 67  PHE   A HB3  1 c 1 
ATOM   799  H HD1  . PHE   A 1 55  ? -11.809 5.581  6.623   1   50.84  ? 67  PHE   A HD1  1 c 1 
ATOM   800  H HD2  . PHE   A 1 55  ? -13.052 1.787  6.111   1   56.821 ? 67  PHE   A HD2  1 c 1 
ATOM   801  H HE1  . PHE   A 1 55  ? -10.892 5.571  4.483   1   50.911 ? 67  PHE   A HE1  1 c 1 
ATOM   802  H HE2  . PHE   A 1 55  ? -12.136 1.782  3.975   1   57.13  ? 67  PHE   A HE2  1 c 1 
ATOM   803  H HZ   . PHE   A 1 55  ? -11.056 3.668  3.158   1   53.756 ? 67  PHE   A HZ   1 c 1 
ATOM   804  N N    . ASP   A 1 56  ? -12.47  5.469  10.591  1   43.675 ? 68  ASP   A N    1 ? 1 
ATOM   805  C CA   . ASP   A 1 56  ? -13.297 6.356  11.406  1   44.837 ? 68  ASP   A CA   1 ? 1 
ATOM   806  C C    . ASP   A 1 56  ? -14.311 7.045  10.497  1   44.297 ? 68  ASP   A C    1 ? 1 
ATOM   807  O O    . ASP   A 1 56  ? -13.93  7.621  9.489   1   43.2   ? 68  ASP   A O    1 ? 1 
ATOM   808  C CB   . ASP   A 1 56  ? -12.472 7.419  12.116  1   42.615 ? 68  ASP   A CB   1 ? 1 
ATOM   809  C CG   . ASP   A 1 56  ? -13.263 8.594  12.686  1   42.87  ? 68  ASP   A CG   1 ? 1 
ATOM   810  O OD1  . ASP   A 1 56  ? -14.235 8.33   13.415  1   47.037 ? 68  ASP   A OD1  1 ? 1 
ATOM   811  O OD2  . ASP   A 1 56  ? -12.91  9.764  12.388  1   42.523 ? 68  ASP   A OD2  1 ? 1 
ATOM   812  H H    . ASP   A 1 56  ? -11.711 5.81   10.213  1   42.716 ? 68  ASP   A H    1 c 1 
ATOM   813  H HA   . ASP   A 1 56  ? -13.774 5.819  12.078  1   46.31  ? 68  ASP   A HA   1 c 1 
ATOM   814  H HB2  . ASP   A 1 56  ? -11.986 6.995  12.853  1   43.333 ? 68  ASP   A HB2  1 c 1 
ATOM   815  H HB3  . ASP   A 1 56  ? -11.811 7.776  11.486  1   41.231 ? 68  ASP   A HB3  1 c 1 
ATOM   816  N N    . SER   A 1 57  ? -15.594 7.008  10.859  1   46.518 ? 69  SER   A N    1 ? 1 
ATOM   817  C CA   . SER   A 1 57  ? -16.638 7.535  9.988   1   46.906 ? 69  SER   A CA   1 ? 1 
ATOM   818  C C    . SER   A 1 57  ? -17.622 8.396  10.779  1   47.42  ? 69  SER   A C    1 ? 1 
ATOM   819  O O    . SER   A 1 57  ? -18.111 7.986  11.83   1   48.395 ? 69  SER   A O    1 ? 1 
ATOM   820  C CB   . SER   A 1 57  ? -17.373 6.445  9.255   1   49.763 ? 69  SER   A CB   1 ? 1 
ATOM   821  O OG   . SER   A 1 57  ? -18.354 7.02   8.396   1   50.28  ? 69  SER   A OG   1 ? 1 
ATOM   822  H H    . SER   A 1 57  ? -15.83  6.648  11.665  1   47.811 ? 69  SER   A H    1 c 1 
ATOM   823  H HA   . SER   A 1 57  ? -16.205 8.115  9.312   1   45.235 ? 69  SER   A HA   1 c 1 
ATOM   824  H HB2  . SER   A 1 57  ? -16.74  5.921  8.727   1   49.14  ? 69  SER   A HB2  1 c 1 
ATOM   825  H HB3  . SER   A 1 57  ? -17.807 5.853  9.898   1   51.514 ? 69  SER   A HB3  1 c 1 
ATOM   826  H HG   . SER   A 1 57  ? -18.762 6.528  7.887   0   30     ? 69  SER   A HG   1 c 1 
ATOM   827  N N    . SER   A 1 58  ? -17.903 9.584  10.226  1   46.111 ? 70  SER   A N    1 ? 1 
ATOM   828  C CA   . SER   A 1 58  ? -18.983 10.451 10.678  1   46.642 ? 70  SER   A CA   1 ? 1 
ATOM   829  C C    . SER   A 1 58  ? -20.312 9.697  10.72   1   51.593 ? 70  SER   A C    1 ? 1 
ATOM   830  O O    . SER   A 1 58  ? -21.129 9.915  11.617  1   52.939 ? 70  SER   A O    1 ? 1 
ATOM   831  C CB   . SER   A 1 58  ? -19.079 11.65  9.787   1   44.649 ? 70  SER   A CB   1 ? 1 
ATOM   832  O OG   . SER   A 1 58  ? -19.384 11.25  8.457   1   41.933 ? 70  SER   A OG   1 ? 1 
ATOM   833  H H    . SER   A 1 58  ? -17.39  9.869  9.526   1   44.539 ? 70  SER   A H    1 c 1 
ATOM   834  H HA   . SER   A 1 58  ? -18.771 10.758 11.596  1   46.998 ? 70  SER   A HA   1 c 1 
ATOM   835  H HB2  . SER   A 1 58  ? -19.778 12.246 10.118  1   45.099 ? 70  SER   A HB2  1 c 1 
ATOM   836  H HB3  . SER   A 1 58  ? -18.232 12.132 9.798   1   42.352 ? 70  SER   A HB3  1 c 1 
ATOM   837  H HG   . SER   A 1 58  ? -19.415 11.915 7.964   0   30     ? 70  SER   A HG   1 c 1 
ATOM   838  N N    . HIS   A 1 59  ? -20.509 8.789  9.753   1   52.805 ? 71  HIS   A N    1 ? 1 
ATOM   839  C CA   . HIS   A 1 59  ? -21.698 7.946  9.718   1   56.907 ? 71  HIS   A CA   1 ? 1 
ATOM   840  C C    . HIS   A 1 59  ? -21.872 7.184  11.031  1   59.49  ? 71  HIS   A C    1 ? 1 
ATOM   841  O O    . HIS   A 1 59  ? -22.995 7.041  11.488  1   60.998 ? 71  HIS   A O    1 ? 1 
ATOM   842  C CB   . HIS   A 1 59  ? -21.74  7.058  8.465   1   56.519 ? 71  HIS   A CB   1 ? 1 
ATOM   843  C CG   . HIS   A 1 59  ? -21.907 7.829  7.181   1   54.862 ? 71  HIS   A CG   1 ? 1 
ATOM   844  N ND1  . HIS   A 1 59  ? -23.009 8.612  6.893   1   55.315 ? 71  HIS   A ND1  1 ? 1 
ATOM   845  C CD2  . HIS   A 1 59  ? -21.074 7.984  6.139   1   52.842 ? 71  HIS   A CD2  1 ? 1 
ATOM   846  C CE1  . HIS   A 1 59  ? -22.847 9.185  5.708   1   54.076 ? 71  HIS   A CE1  1 ? 1 
ATOM   847  N NE2  . HIS   A 1 59  ? -21.695 8.802  5.223   1   52.679 ? 71  HIS   A NE2  1 ? 1 
ATOM   848  H H    . HIS   A 1 59  ? -19.891 8.701  9.086   1   51.459 ? 71  HIS   A H    1 c 1 
ATOM   849  H HA   . HIS   A 1 59  ? -22.462 8.569  9.639   1   57.389 ? 71  HIS   A HA   1 c 1 
ATOM   850  H HB2  . HIS   A 1 59  ? -20.909 6.538  8.419   1   55.687 ? 71  HIS   A HB2  1 c 1 
ATOM   851  H HB3  . HIS   A 1 59  ? -22.484 6.424  8.554   1   58.969 ? 71  HIS   A HB3  1 c 1 
ATOM   852  H HD1  . HIS   A 1 59  ? -23.655 8.75   7.425   0   30     ? 71  HIS   A HD1  1 c 1 
ATOM   853  H HD2  . HIS   A 1 59  ? -20.238 7.575  6.027   1   51.697 ? 71  HIS   A HD2  1 c 1 
ATOM   854  H HE1  . HIS   A 1 59  ? -23.468 9.75   5.28    1   54.833 ? 71  HIS   A HE1  1 c 1 
ATOM   855  H HE2  . HIS   A 1 59  ? -21.32  8.975  4.438   0   30     ? 71  HIS   A HE2  1 c 1 
ATOM   856  N N    . ASP   A 1 60  ? -20.778 6.75   11.664  1   62.345 ? 72  ASP   A N    1 ? 1 
ATOM   857  C CA   . ASP   A 1 60  ? -20.851 6.025  12.931  1   68.037 ? 72  ASP   A CA   1 ? 1 
ATOM   858  C C    . ASP   A 1 60  ? -21.525 6.864  14.023  1   69.307 ? 72  ASP   A C    1 ? 1 
ATOM   859  O O    . ASP   A 1 60  ? -22.116 6.287  14.934  1   71.894 ? 72  ASP   A O    1 ? 1 
ATOM   860  C CB   . ASP   A 1 60  ? -19.491 5.512  13.394  1   67.366 ? 72  ASP   A CB   1 ? 1 
ATOM   861  C CG   . ASP   A 1 60  ? -18.776 4.556  12.444  1   67.497 ? 72  ASP   A CG   1 ? 1 
ATOM   862  O OD1  . ASP   A 1 60  ? -19.471 3.669  11.888  1   70.671 ? 72  ASP   A OD1  1 ? 1 
ATOM   863  O OD2  . ASP   A 1 60  ? -17.534 4.697  12.275  1   61.878 ? 72  ASP   A OD2  1 ? 1 
ATOM   864  H H    . ASP   A 1 60  ? -19.957 6.9    11.293  1   60.039 ? 72  ASP   A H    1 c 1 
ATOM   865  H HA   . ASP   A 1 60  ? -21.408 5.228  12.784  1   69.621 ? 72  ASP   A HA   1 c 1 
ATOM   866  H HB2  . ASP   A 1 60  ? -18.903 6.279  13.556  1   65.27  ? 72  ASP   A HB2  1 c 1 
ATOM   867  H HB3  . ASP   A 1 60  ? -19.613 5.048  14.248  1   69.05  ? 72  ASP   A HB3  1 c 1 
ATOM   868  N N    . ARG   A 1 61  ? -21.45  8.203  13.926  1   68.51  ? 73  ARG   A N    1 ? 1 
ATOM   869  C CA   . ARG   A 1 61  ? -21.987 9.096  14.953  1   67.926 ? 73  ARG   A CA   1 ? 1 
ATOM   870  C C    . ARG   A 1 61  ? -23.4   9.565  14.579  1   68.383 ? 73  ARG   A C    1 ? 1 
ATOM   871  O O    . ARG   A 1 61  ? -24.063 10.226 15.375  1   69.708 ? 73  ARG   A O    1 ? 1 
ATOM   872  C CB   . ARG   A 1 61  ? -21.023 10.271 15.185  1   65.746 ? 73  ARG   A CB   1 ? 1 
ATOM   873  H H    . ARG   A 1 61  ? -21.031 8.574  13.204  1   65.806 ? 73  ARG   A H    1 c 1 
ATOM   874  H HA   . ARG   A 1 61  ? -22.047 8.589  15.802  1   69.597 ? 73  ARG   A HA   1 c 1 
ATOM   875  H HB2  . ARG   A 1 61  ? -20.086 9.912  15.265  0   30     ? 73  ARG   A HB2  1 c 1 
ATOM   876  H HB3  . ARG   A 1 61  ? -21.517 11.055 15.581  0   30     ? 73  ARG   A HB3  1 c 1 
ATOM   877  N N    . ASN   A 1 62  ? -23.841 9.237  13.352  1   66.249 ? 74  ASN   A N    1 ? 1 
ATOM   878  C CA   . ASN   A 1 62  ? -25.21  9.439  12.895  1   66.562 ? 74  ASN   A CA   1 ? 1 
ATOM   879  C C    . ASN   A 1 62  ? -25.502 10.929 12.671  1   65.192 ? 74  ASN   A C    1 ? 1 
ATOM   880  O O    . ASN   A 1 62  ? -26.658 11.347 12.741  1   70.968 ? 74  ASN   A O    1 ? 1 
ATOM   881  C CB   . ASN   A 1 62  ? -26.197 8.741  13.832  1   69.345 ? 74  ASN   A CB   1 ? 1 
ATOM   882  H H    . ASN   A 1 62  ? -23.247 8.875  12.76   1   64.97  ? 74  ASN   A H    1 c 1 
ATOM   883  H HA   . ASN   A 1 62  ? -25.292 8.995  12.021  1   66.581 ? 74  ASN   A HA   1 c 1 
ATOM   884  H HB2  . ASN   A 1 62  ? -25.739 7.855  14.186  0   30     ? 74  ASN   A HB2  1 c 1 
ATOM   885  H HB3  . ASN   A 1 62  ? -27.111 8.786  13.37   0   30     ? 74  ASN   A HB3  1 c 1 
ATOM   886  N N    . GLU   A 1 63  ? -24.469 11.729 12.371  1   61.841 ? 75  GLU   A N    1 ? 1 
ATOM   887  C CA   . GLU   A 1 63  ? -24.652 13.148 12.077  1   59.504 ? 75  GLU   A CA   1 ? 1 
ATOM   888  C C    . GLU   A 1 63  ? -23.434 13.689 11.319  1   53.534 ? 75  GLU   A C    1 ? 1 
ATOM   889  O O    . GLU   A 1 63  ? -22.319 13.19  11.478  1   47.399 ? 75  GLU   A O    1 ? 1 
ATOM   890  C CB   . GLU   A 1 63  ? -24.869 13.94  13.375  1   62.948 ? 75  GLU   A CB   1 ? 1 
ATOM   891  C CG   . GLU   A 1 63  ? -23.602 14.064 14.223  1   62.396 ? 75  GLU   A CG   1 ? 1 
ATOM   892  C CD   . GLU   A 1 63  ? -23.741 14.644 15.624  1   66.027 ? 75  GLU   A CD   1 ? 1 
ATOM   893  O OE1  . GLU   A 1 63  ? -22.687 15.013 16.198  1   64.647 ? 75  GLU   A OE1  1 ? 1 
ATOM   894  O OE2  . GLU   A 1 63  ? -24.879 14.714 16.136  1   71.141 ? 75  GLU   A OE2  1 ? 1 
ATOM   895  H H    . GLU   A 1 63  ? -23.624 11.381 12.34   1   59.917 ? 75  GLU   A H    1 c 1 
ATOM   896  H HA   . GLU   A 1 63  ? -25.454 13.244 11.505  1   61.024 ? 75  GLU   A HA   1 c 1 
ATOM   897  H HB2  . GLU   A 1 63  ? -25.189 14.838 13.147  1   62.933 ? 75  GLU   A HB2  1 c 1 
ATOM   898  H HB3  . GLU   A 1 63  ? -25.567 13.5   13.902  1   65.039 ? 75  GLU   A HB3  1 c 1 
ATOM   899  H HG2  . GLU   A 1 63  ? -23.199 13.173 14.306  1   62.122 ? 75  GLU   A HG2  1 c 1 
ATOM   900  H HG3  . GLU   A 1 63  ? -22.957 14.619 13.736  1   60.501 ? 75  GLU   A HG3  1 c 1 
ATOM   901  N N    . PRO   A 1 64  ? -23.578 14.773 10.52   1   50.712 ? 76  PRO   A N    1 ? 1 
ATOM   902  C CA   . PRO   A 1 64  ? -22.434 15.356 9.831   1   47.306 ? 76  PRO   A CA   1 ? 1 
ATOM   903  C C    . PRO   A 1 64  ? -21.405 15.926 10.793  1   45.643 ? 76  PRO   A C    1 ? 1 
ATOM   904  O O    . PRO   A 1 64  ? -21.755 16.286 11.923  1   46.468 ? 76  PRO   A O    1 ? 1 
ATOM   905  C CB   . PRO   A 1 64  ? -23     16.48  8.979   1   49.181 ? 76  PRO   A CB   1 ? 1 
ATOM   906  C CG   . PRO   A 1 64  ? -24.51  16.395 9.123   1   52.042 ? 76  PRO   A CG   1 ? 1 
ATOM   907  C CD   . PRO   A 1 64  ? -24.832 15.499 10.283  1   53.767 ? 76  PRO   A CD   1 ? 1 
ATOM   908  H HA   . PRO   A 1 64  ? -22.016 14.68  9.258   1   46.604 ? 76  PRO   A HA   1 c 1 
ATOM   909  H HB2  . PRO   A 1 64  ? -22.673 17.347 9.288   1   48.3   ? 76  PRO   A HB2  1 c 1 
ATOM   910  H HB3  . PRO   A 1 64  ? -22.736 16.368 8.046   1   47.784 ? 76  PRO   A HB3  1 c 1 
ATOM   911  H HG2  . PRO   A 1 64  ? -24.885 17.286 9.277   1   53.093 ? 76  PRO   A HG2  1 c 1 
ATOM   912  H HG3  . PRO   A 1 64  ? -24.908 16.036 8.304   1   52.678 ? 76  PRO   A HG3  1 c 1 
ATOM   913  H HD2  . PRO   A 1 64  ? -25.085 16.017 11.071  1   54.604 ? 76  PRO   A HD2  1 c 1 
ATOM   914  H HD3  . PRO   A 1 64  ? -25.553 14.881 10.058  1   55.225 ? 76  PRO   A HD3  1 c 1 
ATOM   915  N N    . PHE   A 1 65  ? -20.14  15.938 10.343  1   40.997 ? 77  PHE   A N    1 ? 1 
ATOM   916  C CA   . PHE   A 1 65  ? -19.075 16.644 11.037  1   38.472 ? 77  PHE   A CA   1 ? 1 
ATOM   917  C C    . PHE   A 1 65  ? -19.103 18.114 10.62   1   37.912 ? 77  PHE   A C    1 ? 1 
ATOM   918  O O    . PHE   A 1 65  ? -19.176 18.44  9.434   1   36.002 ? 77  PHE   A O    1 ? 1 
ATOM   919  C CB   . PHE   A 1 65  ? -17.73  15.978 10.738  1   36.011 ? 77  PHE   A CB   1 ? 1 
ATOM   920  C CG   . PHE   A 1 65  ? -16.564 16.597 11.496  1   36.119 ? 77  PHE   A CG   1 ? 1 
ATOM   921  C CD1  . PHE   A 1 65  ? -16.288 16.254 12.822  1   38.541 ? 77  PHE   A CD1  1 ? 1 
ATOM   922  C CD2  . PHE   A 1 65  ? -15.774 17.567 10.889  1   35.528 ? 77  PHE   A CD2  1 ? 1 
ATOM   923  C CE1  . PHE   A 1 65  ? -15.229 16.852 13.498  1   36.914 ? 77  PHE   A CE1  1 ? 1 
ATOM   924  C CE2  . PHE   A 1 65  ? -14.722 18.163 11.566  1   36.351 ? 77  PHE   A CE2  1 ? 1 
ATOM   925  C CZ   . PHE   A 1 65  ? -14.451 17.801 12.865  1   36.856 ? 77  PHE   A CZ   1 ? 1 
ATOM   926  H H    . PHE   A 1 65  ? -19.937 15.488 9.574   1   40.496 ? 77  PHE   A H    1 c 1 
ATOM   927  H HA   . PHE   A 1 65  ? -19.244 16.586 12.014  1   39.511 ? 77  PHE   A HA   1 c 1 
ATOM   928  H HB2  . PHE   A 1 65  ? -17.794 15.026 10.972  1   36.728 ? 77  PHE   A HB2  1 c 1 
ATOM   929  H HB3  . PHE   A 1 65  ? -17.555 16.043 9.773   1   35.535 ? 77  PHE   A HB3  1 c 1 
ATOM   930  H HD1  . PHE   A 1 65  ? -16.817 15.603 13.257  1   39.093 ? 77  PHE   A HD1  1 c 1 
ATOM   931  H HD2  . PHE   A 1 65  ? -15.955 17.818 9.998   1   35.488 ? 77  PHE   A HD2  1 c 1 
ATOM   932  H HE1  . PHE   A 1 65  ? -15.041 16.605 14.389  1   37.878 ? 77  PHE   A HE1  1 c 1 
ATOM   933  H HE2  . PHE   A 1 65  ? -14.189 18.81  11.133  1   35.174 ? 77  PHE   A HE2  1 c 1 
ATOM   934  H HZ   . PHE   A 1 65  ? -13.732 18.205 13.326  1   36.084 ? 77  PHE   A HZ   1 c 1 
ATOM   935  N N    . VAL   A 1 66  ? -19.089 18.994 11.619  1   37.12  ? 78  VAL   A N    1 ? 1 
ATOM   936  C CA   . VAL   A 1 66  ? -19.292 20.417 11.414  1   38.343 ? 78  VAL   A CA   1 ? 1 
ATOM   937  C C    . VAL   A 1 66  ? -18.119 21.188 12.011  1   38.933 ? 78  VAL   A C    1 ? 1 
ATOM   938  O O    . VAL   A 1 66  ? -17.7   20.889 13.131  1   39.143 ? 78  VAL   A O    1 ? 1 
ATOM   939  C CB   . VAL   A 1 66  ? -20.613 20.834 12.08   1   42.588 ? 78  VAL   A CB   1 ? 1 
ATOM   940  C CG1  . VAL   A 1 66  ? -20.892 22.315 11.863  1   44.167 ? 78  VAL   A CG1  1 ? 1 
ATOM   941  C CG2  . VAL   A 1 66  ? -21.777 19.96  11.62   1   43.347 ? 78  VAL   A CG2  1 ? 1 
ATOM   942  H H    . VAL   A 1 66  ? -18.943 18.695 12.471  1   37.901 ? 78  VAL   A H    1 c 1 
ATOM   943  H HA   . VAL   A 1 66  ? -19.344 20.598 10.459  1   38.39  ? 78  VAL   A HA   1 c 1 
ATOM   944  H HB   . VAL   A 1 66  ? -20.503 20.694 13.049  1   42.739 ? 78  VAL   A HB   1 c 1 
ATOM   945  H HG11 . VAL   A 1 66  ? -20.755 22.539 10.927  1   43.413 ? 78  VAL   A HG11 1 c 1 
ATOM   946  H HG12 . VAL   A 1 66  ? -20.292 22.845 12.414  1   43.851 ? 78  VAL   A HG12 1 c 1 
ATOM   947  H HG13 . VAL   A 1 66  ? -21.812 22.51  12.11   1   46.209 ? 78  VAL   A HG13 1 c 1 
ATOM   948  H HG21 . VAL   A 1 66  ? -22.616 20.36  11.905  1   45.557 ? 78  VAL   A HG21 1 c 1 
ATOM   949  H HG22 . VAL   A 1 66  ? -21.693 19.075 12.011  1   43.316 ? 78  VAL   A HG22 1 c 1 
ATOM   950  H HG23 . VAL   A 1 66  ? -21.766 19.888 10.651  1   42.845 ? 78  VAL   A HG23 1 c 1 
ATOM   951  N N    . PHE   A 1 67  ? -17.592 22.166 11.264  1   38.46  ? 79  PHE   A N    1 ? 1 
ATOM   952  C CA   . PHE   A 1 67  ? -16.415 22.914 11.707  1   37.348 ? 79  PHE   A CA   1 ? 1 
ATOM   953  C C    . PHE   A 1 67  ? -16.339 24.234 10.931  1   38.224 ? 79  PHE   A C    1 ? 1 
ATOM   954  O O    . PHE   A 1 67  ? -16.931 24.369 9.861   1   37.74  ? 79  PHE   A O    1 ? 1 
ATOM   955  C CB   . PHE   A 1 67  ? -15.129 22.096 11.565  1   33.892 ? 79  PHE   A CB   1 ? 1 
ATOM   956  C CG   . PHE   A 1 67  ? -14.614 21.986 10.13   1   32.909 ? 79  PHE   A CG   1 ? 1 
ATOM   957  C CD1  . PHE   A 1 67  ? -15.186 21.092 9.233   1   32.429 ? 79  PHE   A CD1  1 ? 1 
ATOM   958  C CD2  . PHE   A 1 67  ? -13.56  22.783 9.689   1   31.379 ? 79  PHE   A CD2  1 ? 1 
ATOM   959  C CE1  . PHE   A 1 67  ? -14.731 21.02  7.922   1   30.172 ? 79  PHE   A CE1  1 ? 1 
ATOM   960  C CE2  . PHE   A 1 67  ? -13.108 22.711 8.382   1   30.719 ? 79  PHE   A CE2  1 ? 1 
ATOM   961  C CZ   . PHE   A 1 67  ? -13.712 21.838 7.491   1   30.937 ? 79  PHE   A CZ   1 ? 1 
ATOM   962  H H    . PHE   A 1 67  ? -17.972 22.375 10.459  1   38.583 ? 79  PHE   A H    1 c 1 
ATOM   963  H HA   . PHE   A 1 67  ? -16.535 23.132 12.67   1   38.286 ? 79  PHE   A HA   1 c 1 
ATOM   964  H HB2  . PHE   A 1 67  ? -14.432 22.511 12.122  1   34.07  ? 79  PHE   A HB2  1 c 1 
ATOM   965  H HB3  . PHE   A 1 67  ? -15.292 21.192 11.914  1   34.068 ? 79  PHE   A HB3  1 c 1 
ATOM   966  H HD1  . PHE   A 1 67  ? -15.906 20.548 9.51    1   32.942 ? 79  PHE   A HD1  1 c 1 
ATOM   967  H HD2  . PHE   A 1 67  ? -13.166 23.401 10.285  1   32.07  ? 79  PHE   A HD2  1 c 1 
ATOM   968  H HE1  . PHE   A 1 67  ? -15.134 20.416 7.32    1   30.739 ? 79  PHE   A HE1  1 c 1 
ATOM   969  H HE2  . PHE   A 1 67  ? -12.399 23.265 8.096   1   30.408 ? 79  PHE   A HE2  1 c 1 
ATOM   970  H HZ   . PHE   A 1 67  ? -13.388 21.765 6.607   1   29.794 ? 79  PHE   A HZ   1 c 1 
ATOM   971  N N    . SER   A 1 68  ? -15.618 25.215 11.494  1   38.567 ? 80  SER   A N    1 ? 1 
ATOM   972  C CA   . SER   A 1 68  ? -15.424 26.506 10.849  1   38.754 ? 80  SER   A CA   1 ? 1 
ATOM   973  C C    . SER   A 1 68  ? -14.133 26.452 10.049  1   37.086 ? 80  SER   A C    1 ? 1 
ATOM   974  O O    . SER   A 1 68  ? -13.088 26.169 10.612  1   35.513 ? 80  SER   A O    1 ? 1 
ATOM   975  C CB   . SER   A 1 68  ? -15.382 27.646 11.838  1   40.379 ? 80  SER   A CB   1 ? 1 
ATOM   976  O OG   . SER   A 1 68  ? -16.657 27.854 12.416  1   42.785 ? 80  SER   A OG   1 ? 1 
ATOM   977  H H    . SER   A 1 68  ? -15.233 25.071 12.31   1   38.305 ? 80  SER   A H    1 c 1 
ATOM   978  H HA   . SER   A 1 68  ? -16.176 26.66  10.226  1   39.763 ? 80  SER   A HA   1 c 1 
ATOM   979  H HB2  . SER   A 1 68  ? -14.735 27.442 12.54   1   39.892 ? 80  SER   A HB2  1 c 1 
ATOM   980  H HB3  . SER   A 1 68  ? -15.094 28.46  11.383  1   41.125 ? 80  SER   A HB3  1 c 1 
ATOM   981  H HG   . SER   A 1 68  ? -16.625 28.452 12.963  0   30     ? 80  SER   A HG   1 c 1 
ATOM   982  N N    . LEU   A 1 69  ? -14.218 26.779 8.756   1   37.696 ? 81  LEU   A N    1 ? 1 
ATOM   983  C CA   . LEU   A 1 69  ? -13.098 26.604 7.847   1   36.568 ? 81  LEU   A CA   1 ? 1 
ATOM   984  C C    . LEU   A 1 69  ? -11.978 27.588 8.162   1   38.056 ? 81  LEU   A C    1 ? 1 
ATOM   985  O O    . LEU   A 1 69  ? -12.213 28.771 8.392   1   39.747 ? 81  LEU   A O    1 ? 1 
ATOM   986  C CB   . LEU   A 1 69  ? -13.606 26.785 6.413   1   37.63  ? 81  LEU   A CB   1 ? 1 
ATOM   987  C CG   . LEU   A 1 69  ? -12.589 26.493 5.298   1   36.347 ? 81  LEU   A CG   1 ? 1 
ATOM   988  C CD1  . LEU   A 1 69  ? -12.066 25.085 5.346   1   33.164 ? 81  LEU   A CD1  1 ? 1 
ATOM   989  C CD2  . LEU   A 1 69  ? -13.196 26.741 3.905   1   38.604 ? 81  LEU   A CD2  1 ? 1 
ATOM   990  H H    . LEU   A 1 69  ? -14.998 27.127 8.431   1   38.968 ? 81  LEU   A H    1 c 1 
ATOM   991  H HA   . LEU   A 1 69  ? -12.754 25.681 7.957   1   35.242 ? 81  LEU   A HA   1 c 1 
ATOM   992  H HB2  . LEU   A 1 69  ? -14.384 26.195 6.286   1   37.589 ? 81  LEU   A HB2  1 c 1 
ATOM   993  H HB3  . LEU   A 1 69  ? -13.917 27.715 6.314   1   39.234 ? 81  LEU   A HB3  1 c 1 
ATOM   994  H HG   . LEU   A 1 69  ? -11.82  27.109 5.41    1   36.526 ? 81  LEU   A HG   1 c 1 
ATOM   995  H HD11 . LEU   A 1 69  ? -11.494 24.977 6.123   1   32.89  ? 81  LEU   A HD11 1 c 1 
ATOM   996  H HD12 . LEU   A 1 69  ? -11.554 24.901 4.54    1   32.714 ? 81  LEU   A HD12 1 c 1 
ATOM   997  H HD13 . LEU   A 1 69  ? -12.811 24.464 5.404   1   33.444 ? 81  LEU   A HD13 1 c 1 
ATOM   998  H HD21 . LEU   A 1 69  ? -13.556 27.643 3.863   1   39.899 ? 81  LEU   A HD21 1 c 1 
ATOM   999  H HD22 . LEU   A 1 69  ? -13.908 26.101 3.741   1   38.125 ? 81  LEU   A HD22 1 c 1 
ATOM   1000 H HD23 . LEU   A 1 69  ? -12.507 26.638 3.227   1   37.403 ? 81  LEU   A HD23 1 c 1 
ATOM   1001 N N    . GLY   A 1 70  ? -10.745 27.091 8.123   1   38.553 ? 82  GLY   A N    1 ? 1 
ATOM   1002 C CA   . GLY   A 1 70  ? -9.56   27.933 8.196   1   39.069 ? 82  GLY   A CA   1 ? 1 
ATOM   1003 C C    . GLY   A 1 70  ? -9.303  28.493 9.59    1   42.084 ? 82  GLY   A C    1 ? 1 
ATOM   1004 O O    . GLY   A 1 70  ? -8.65   29.531 9.703   1   46.083 ? 82  GLY   A O    1 ? 1 
ATOM   1005 H H    . GLY   A 1 70  ? -10.634 26.188 8.046   1   36.571 ? 82  GLY   A H    1 c 1 
ATOM   1006 H HA2  . GLY   A 1 70  ? -8.779  27.406 7.911   1   38.007 ? 82  GLY   A HA2  1 c 1 
ATOM   1007 H HA3  . GLY   A 1 70  ? -9.663  28.679 7.562   1   40.539 ? 82  GLY   A HA3  1 c 1 
ATOM   1008 N N    . LYS   A 1 71  ? -9.864  27.859 10.63   1   41.287 ? 83  LYS   A N    1 ? 1 
ATOM   1009 C CA   . LYS   A 1 71  ? -9.721  28.331 12      1   42.476 ? 83  LYS   A CA   1 ? 1 
ATOM   1010 C C    . LYS   A 1 71  ? -8.875  27.35  12.82   1   44.431 ? 83  LYS   A C    1 ? 1 
ATOM   1011 O O    . LYS   A 1 71  ? -8.816  27.464 14.037  1   46.754 ? 83  LYS   A O    1 ? 1 
ATOM   1012 C CB   . LYS   A 1 71  ? -11.101 28.541 12.647  1   43.886 ? 83  LYS   A CB   1 ? 1 
ATOM   1013 H H    . LYS   A 1 71  ? -10.346 27.097 10.48   1   40.54  ? 83  LYS   A H    1 c 1 
ATOM   1014 H HA   . LYS   A 1 71  ? -9.254  29.205 11.984  1   44.179 ? 83  LYS   A HA   1 c 1 
ATOM   1015 H HB2  . LYS   A 1 71  ? -10.922 28.934 13.594  0   30     ? 83  LYS   A HB2  1 c 1 
ATOM   1016 H HB3  . LYS   A 1 71  ? -11.778 28.379 12.04   0   30     ? 83  LYS   A HB3  1 c 1 
ATOM   1017 N N    . GLY   A 1 72  ? -8.225  26.385 12.156  1   45.804 ? 84  GLY   A N    1 ? 1 
ATOM   1018 C CA   . GLY   A 1 72  ? -7.494  25.314 12.819  1   44.902 ? 84  GLY   A CA   1 ? 1 
ATOM   1019 C C    . GLY   A 1 72  ? -8.332  24.508 13.816  1   42.666 ? 84  GLY   A C    1 ? 1 
ATOM   1020 O O    . GLY   A 1 72  ? -7.785  24.032 14.799  1   39.86  ? 84  GLY   A O    1 ? 1 
ATOM   1021 H H    . GLY   A 1 72  ? -8.229  26.399 11.243  1   44.306 ? 84  GLY   A H    1 c 1 
ATOM   1022 H HA2  . GLY   A 1 72  ? -7.14   24.703 12.13   1   42.867 ? 84  GLY   A HA2  1 c 1 
ATOM   1023 H HA3  . GLY   A 1 72  ? -6.722  25.706 13.291  1   44.643 ? 84  GLY   A HA3  1 c 1 
ATOM   1024 N N    . GLN   A 1 73  ? -9.63   24.295 13.541  1   37.054 ? 85  GLN   A N    1 ? 1 
ATOM   1025 C CA   . GLN   A 1 73  ? -10.432 23.341 14.298  1   34.939 ? 85  GLN   A CA   1 ? 1 
ATOM   1026 C C    . GLN   A 1 73  ? -10.193 21.924 13.781  1   33.352 ? 85  GLN   A C    1 ? 1 
ATOM   1027 O O    . GLN   A 1 73  ? -10.667 20.942 14.355  1   34.152 ? 85  GLN   A O    1 ? 1 
ATOM   1028 C CB   . GLN   A 1 73  ? -11.917 23.701 14.247  1   37.036 ? 85  GLN   A CB   1 ? 1 
ATOM   1029 C CG   . GLN   A 1 73  ? -12.232 25.007 14.966  1   39.279 ? 85  GLN   A CG   1 ? 1 
ATOM   1030 C CD   . GLN   A 1 73  ? -13.57  25.592 14.585  1   42.36  ? 85  GLN   A CD   1 ? 1 
ATOM   1031 O OE1  . GLN   A 1 73  ? -14.414 24.937 13.96   1   42.379 ? 85  GLN   A OE1  1 ? 1 
ATOM   1032 N NE2  . GLN   A 1 73  ? -13.766 26.845 14.973  1   45.392 ? 85  GLN   A NE2  1 ? 1 
ATOM   1033 H H    . GLN   A 1 73  ? -10.026 24.754 12.857  1   38.134 ? 85  GLN   A H    1 c 1 
ATOM   1034 H HA   . GLN   A 1 73  ? -10.143 23.378 15.246  1   36.186 ? 85  GLN   A HA   1 c 1 
ATOM   1035 H HB2  . GLN   A 1 73  ? -12.193 23.775 13.309  1   36.533 ? 85  GLN   A HB2  1 c 1 
ATOM   1036 H HB3  . GLN   A 1 73  ? -12.436 22.977 14.656  1   37.124 ? 85  GLN   A HB3  1 c 1 
ATOM   1037 H HG2  . GLN   A 1 73  ? -12.221 24.853 15.934  1   40.301 ? 85  GLN   A HG2  1 c 1 
ATOM   1038 H HG3  . GLN   A 1 73  ? -11.533 25.664 14.762  1   39.529 ? 85  GLN   A HG3  1 c 1 
ATOM   1039 H HE21 . GLN   A 1 73  ? -14.589 27.173 15.006  1   46.582 ? 85  GLN   A HE21 1 c 1 
ATOM   1040 H HE22 . GLN   A 1 73  ? -13.076 27.356 15.199  1   45.262 ? 85  GLN   A HE22 1 c 1 
ATOM   1041 N N    . VAL   A 1 74  ? -9.492  21.835 12.646  1   30.219 ? 86  VAL   A N    1 ? 1 
ATOM   1042 C CA   . VAL   A 1 74  ? -9.19   20.582 11.989  1   28.516 ? 86  VAL   A CA   1 ? 1 
ATOM   1043 C C    . VAL   A 1 74  ? -7.718  20.638 11.582  1   25.988 ? 86  VAL   A C    1 ? 1 
ATOM   1044 O O    . VAL   A 1 74  ? -7.08   21.686 11.704  1   27.668 ? 86  VAL   A O    1 ? 1 
ATOM   1045 C CB   . VAL   A 1 74  ? -10.11  20.354 10.769  1   27.428 ? 86  VAL   A CB   1 ? 1 
ATOM   1046 C CG1  . VAL   A 1 74  ? -11.548 20.011 11.17   1   28.71  ? 86  VAL   A CG1  1 ? 1 
ATOM   1047 C CG2  . VAL   A 1 74  ? -10.051 21.552 9.837   1   27.64  ? 86  VAL   A CG2  1 ? 1 
ATOM   1048 H H    . VAL   A 1 74  ? -9.194  22.604 12.254  1   30.757 ? 86  VAL   A H    1 c 1 
ATOM   1049 H HA   . VAL   A 1 74  ? -9.315  19.85  12.624  1   28.299 ? 86  VAL   A HA   1 c 1 
ATOM   1050 H HB   . VAL   A 1 74  ? -9.749  19.58  10.277  1   26.664 ? 86  VAL   A HB   1 c 1 
ATOM   1051 H HG11 . VAL   A 1 74  ? -11.921 20.738 11.695  1   29.781 ? 86  VAL   A HG11 1 c 1 
ATOM   1052 H HG12 . VAL   A 1 74  ? -11.552 19.195 11.698  1   28.692 ? 86  VAL   A HG12 1 c 1 
ATOM   1053 H HG13 . VAL   A 1 74  ? -12.086 19.881 10.371  1   28.72  ? 86  VAL   A HG13 1 c 1 
ATOM   1054 H HG21 . VAL   A 1 74  ? -10.555 21.359 9.029   1   27.563 ? 86  VAL   A HG21 1 c 1 
ATOM   1055 H HG22 . VAL   A 1 74  ? -9.127  21.74  9.602   1   26.997 ? 86  VAL   A HG22 1 c 1 
ATOM   1056 H HG23 . VAL   A 1 74  ? -10.437 22.328 10.278  1   28.767 ? 86  VAL   A HG23 1 c 1 
ATOM   1057 N N    . ILE   A 1 75  ? -7.185  19.494 11.17   1   24.768 ? 87  ILE   A N    1 ? 1 
ATOM   1058 C CA   . ILE   A 1 75  ? -5.813  19.419 10.695  1   24.766 ? 87  ILE   A CA   1 ? 1 
ATOM   1059 C C    . ILE   A 1 75  ? -5.68   20.329 9.475   1   24.632 ? 87  ILE   A C    1 ? 1 
ATOM   1060 O O    . ILE   A 1 75  ? -6.68   20.616 8.803   1   24.371 ? 87  ILE   A O    1 ? 1 
ATOM   1061 C CB   . ILE   A 1 75  ? -5.383  17.979 10.367  1   25.051 ? 87  ILE   A CB   1 ? 1 
ATOM   1062 C CG1  . ILE   A 1 75  ? -6.34   17.278 9.422   1   23.7   ? 87  ILE   A CG1  1 ? 1 
ATOM   1063 C CG2  . ILE   A 1 75  ? -5.155  17.152 11.638  1   25.265 ? 87  ILE   A CG2  1 ? 1 
ATOM   1064 C CD1  . ILE   A 1 75  ? -5.828  15.936 8.932   1   25.284 ? 87  ILE   A CD1  1 ? 1 
ATOM   1065 H H    . ILE   A 1 75  ? -7.687  18.731 11.199  1   25.029 ? 87  ILE   A H    1 c 1 
ATOM   1066 H HA   . ILE   A 1 75  ? -5.228  19.76  11.399  1   25.105 ? 87  ILE   A HA   1 c 1 
ATOM   1067 H HB   . ILE   A 1 75  ? -4.524  18.039 9.905   1   24.096 ? 87  ILE   A HB   1 c 1 
ATOM   1068 H HG12 . ILE   A 1 75  ? -7.194  17.139 9.88    1   24.998 ? 87  ILE   A HG12 1 c 1 
ATOM   1069 H HG13 . ILE   A 1 75  ? -6.504  17.854 8.649   1   24.278 ? 87  ILE   A HG13 1 c 1 
ATOM   1070 H HG21 . ILE   A 1 75  ? -4.66   16.345 11.418  1   24.989 ? 87  ILE   A HG21 1 c 1 
ATOM   1071 H HG22 . ILE   A 1 75  ? -6.012  16.908 12.026  1   25.88  ? 87  ILE   A HG22 1 c 1 
ATOM   1072 H HG23 . ILE   A 1 75  ? -4.648  17.675 12.281  1   25.652 ? 87  ILE   A HG23 1 c 1 
ATOM   1073 H HD11 . ILE   A 1 75  ? -4.892  16.018 8.671   1   24.212 ? 87  ILE   A HD11 1 c 1 
ATOM   1074 H HD12 . ILE   A 1 75  ? -6.354  15.648 8.162   1   24.603 ? 87  ILE   A HD12 1 c 1 
ATOM   1075 H HD13 . ILE   A 1 75  ? -5.909  15.273 9.644   1   25.02  ? 87  ILE   A HD13 1 c 1 
ATOM   1076 N N    . LYS   A 1 76  ? -4.45   20.787 9.225   1   23.042 ? 88  LYS   A N    1 ? 1 
ATOM   1077 C CA   . LYS   A 1 76  ? -4.176  21.778 8.188   1   23.68  ? 88  LYS   A CA   1 ? 1 
ATOM   1078 C C    . LYS   A 1 76  ? -4.656  21.257 6.83    1   24.011 ? 88  LYS   A C    1 ? 1 
ATOM   1079 O O    . LYS   A 1 76  ? -5.167  22.031 6.018   1   24.151 ? 88  LYS   A O    1 ? 1 
ATOM   1080 C CB   . LYS   A 1 76  ? -2.681  22.153 8.191   1   25.115 ? 88  LYS   A CB   1 ? 1 
ATOM   1081 H H    . LYS   A 1 76  ? -3.752  20.467 9.72    1   23.32  ? 88  LYS   A H    1 c 1 
ATOM   1082 H HA   . LYS   A 1 76  ? -4.694  22.594 8.404   1   24.868 ? 88  LYS   A HA   1 c 1 
ATOM   1083 H HB2  . LYS   A 1 76  ? -2.109  21.36  8.177   0   30     ? 88  LYS   A HB2  1 c 1 
ATOM   1084 H HB3  . LYS   A 1 76  ? -2.595  23.148 8.327   0   30     ? 88  LYS   A HB3  1 c 1 
ATOM   1085 N N    . ALA   A 1 77  ? -4.511  19.95  6.586   1   23.02  ? 89  ALA   A N    1 ? 1 
ATOM   1086 C CA   . ALA   A 1 77  ? -4.885  19.353 5.309   1   22.873 ? 89  ALA   A CA   1 ? 1 
ATOM   1087 C C    . ALA   A 1 77  ? -6.382  19.506 5.027   1   22.297 ? 89  ALA   A C    1 ? 1 
ATOM   1088 O O    . ALA   A 1 77  ? -6.8    19.597 3.856   1   21.607 ? 89  ALA   A O    1 ? 1 
ATOM   1089 C CB   . ALA   A 1 77  ? -4.512  17.888 5.268   1   21.896 ? 89  ALA   A CB   1 ? 1 
ATOM   1090 H H    . ALA   A 1 77  ? -4.157  19.411 7.233   1   22.863 ? 89  ALA   A H    1 c 1 
ATOM   1091 H HA   . ALA   A 1 77  ? -4.387  19.831 4.59    1   22.633 ? 89  ALA   A HA   1 c 1 
ATOM   1092 H HB1  . ALA   A 1 77  ? -3.545  17.799 5.248   1   21.809 ? 89  ALA   A HB1  1 c 1 
ATOM   1093 H HB2  . ALA   A 1 77  ? -4.861  17.439 6.056   1   22.104 ? 89  ALA   A HB2  1 c 1 
ATOM   1094 H HB3  . ALA   A 1 77  ? -4.888  17.478 4.471   1   21.991 ? 89  ALA   A HB3  1 c 1 
ATOM   1095 N N    . TRP   A 1 78  ? -7.193  19.563 6.087   1   21.971 ? 90  TRP   A N    1 ? 1 
ATOM   1096 C CA   . TRP   A 1 78  ? -8.617  19.748 5.901   1   24.292 ? 90  TRP   A CA   1 ? 1 
ATOM   1097 C C    . TRP   A 1 78  ? -8.928  21.205 5.559   1   24.524 ? 90  TRP   A C    1 ? 1 
ATOM   1098 O O    . TRP   A 1 78  ? -9.824  21.449 4.737   1   25.222 ? 90  TRP   A O    1 ? 1 
ATOM   1099 C CB   . TRP   A 1 78  ? -9.431  19.245 7.105   1   24.871 ? 90  TRP   A CB   1 ? 1 
ATOM   1100 C CG   . TRP   A 1 78  ? -9.884  17.807 7.009   1   23.94  ? 90  TRP   A CG   1 ? 1 
ATOM   1101 C CD1  . TRP   A 1 78  ? -9.15   16.684 6.754   1   23.657 ? 90  TRP   A CD1  1 ? 1 
ATOM   1102 C CD2  . TRP   A 1 78  ? -11.233 17.347 7.23    1   24.905 ? 90  TRP   A CD2  1 ? 1 
ATOM   1103 N NE1  . TRP   A 1 78  ? -9.94   15.57  6.774   1   24.251 ? 90  TRP   A NE1  1 ? 1 
ATOM   1104 C CE2  . TRP   A 1 78  ? -11.229 15.941 7.059   1   26.242 ? 90  TRP   A CE2  1 ? 1 
ATOM   1105 C CE3  . TRP   A 1 78  ? -12.432 17.987 7.531   1   27.12  ? 90  TRP   A CE3  1 ? 1 
ATOM   1106 C CZ2  . TRP   A 1 78  ? -12.371 15.166 7.21    1   27.298 ? 90  TRP   A CZ2  1 ? 1 
ATOM   1107 C CZ3  . TRP   A 1 78  ? -13.564 17.22  7.7     1   29.28  ? 90  TRP   A CZ3  1 ? 1 
ATOM   1108 C CH2  . TRP   A 1 78  ? -13.532 15.825 7.543   1   29.743 ? 90  TRP   A CH2  1 ? 1 
ATOM   1109 H H    . TRP   A 1 78  ? -6.858  19.474 6.933   1   22.501 ? 90  TRP   A H    1 c 1 
ATOM   1110 H HA   . TRP   A 1 78  ? -8.886  19.196 5.118   1   23.682 ? 90  TRP   A HA   1 c 1 
ATOM   1111 H HB2  . TRP   A 1 78  ? -8.888  19.351 7.915   1   24.572 ? 90  TRP   A HB2  1 c 1 
ATOM   1112 H HB3  . TRP   A 1 78  ? -10.221 19.817 7.207   1   25.547 ? 90  TRP   A HB3  1 c 1 
ATOM   1113 H HD1  . TRP   A 1 78  ? -8.224  16.674 6.57    1   22.915 ? 90  TRP   A HD1  1 c 1 
ATOM   1114 H HE1  . TRP   A 1 78  ? -9.668  14.76  6.631   1   24.322 ? 90  TRP   A HE1  1 c 1 
ATOM   1115 H HE3  . TRP   A 1 78  ? -12.459 18.921 7.654   1   27.495 ? 90  TRP   A HE3  1 c 1 
ATOM   1116 H HZ2  . TRP   A 1 78  ? -12.346 14.23  7.111   1   27.734 ? 90  TRP   A HZ2  1 c 1 
ATOM   1117 H HZ3  . TRP   A 1 78  ? -14.38  17.643 7.909   1   30.205 ? 90  TRP   A HZ3  1 c 1 
ATOM   1118 H HH2  . TRP   A 1 78  ? -14.328 15.332 7.64    1   30.302 ? 90  TRP   A HH2  1 c 1 
ATOM   1119 N N    . ASP   A 1 79  ? -8.24   22.154 6.21    1   24.682 ? 91  ASP   A N    1 ? 1 
ATOM   1120 C CA   . ASP   A 1 79  ? -8.449  23.568 5.934   1   27.551 ? 91  ASP   A CA   1 ? 1 
ATOM   1121 C C    . ASP   A 1 79  ? -8.05   23.841 4.481   1   27.889 ? 91  ASP   A C    1 ? 1 
ATOM   1122 O O    . ASP   A 1 79  ? -8.733  24.589 3.778   1   28.605 ? 91  ASP   A O    1 ? 1 
ATOM   1123 C CB   . ASP   A 1 79  ? -7.743  24.486 6.923   1   29.272 ? 91  ASP   A CB   1 ? 1 
ATOM   1124 C CG   . ASP   A 1 79  ? -8.474  24.705 8.247   1   30.919 ? 91  ASP   A CG   1 ? 1 
ATOM   1125 O OD1  . ASP   A 1 79  ? -9.713  24.49  8.305   1   30.513 ? 91  ASP   A OD1  1 ? 1 
ATOM   1126 O OD2  . ASP   A 1 79  ? -7.819  25.107 9.203   1   32.408 ? 91  ASP   A OD2  1 ? 1 
ATOM   1127 H H    . ASP   A 1 79  ? -7.629  21.914 6.846   1   24.677 ? 91  ASP   A H    1 c 1 
ATOM   1128 H HA   . ASP   A 1 79  ? -9.413  23.749 6.016   1   28.3   ? 91  ASP   A HA   1 c 1 
ATOM   1129 H HB2  . ASP   A 1 79  ? -6.858  24.114 7.121   1   28.376 ? 91  ASP   A HB2  1 c 1 
ATOM   1130 H HB3  . ASP   A 1 79  ? -7.613  25.361 6.502   1   30.067 ? 91  ASP   A HB3  1 c 1 
ATOM   1131 N N    . ILE   A 1 80  ? -6.973  23.189 4.029   1   23.744 ? 92  ILE   A N    1 ? 1 
ATOM   1132 C CA   . ILE   A 1 80  ? -6.517  23.361 2.652   1   25.351 ? 92  ILE   A CA   1 ? 1 
ATOM   1133 C C    . ILE   A 1 80  ? -7.481  22.673 1.68    1   25.986 ? 92  ILE   A C    1 ? 1 
ATOM   1134 O O    . ILE   A 1 80  ? -7.909  23.278 0.695   1   27.548 ? 92  ILE   A O    1 ? 1 
ATOM   1135 C CB   . ILE   A 1 80  ? -5.068  22.859 2.493   1   25.527 ? 92  ILE   A CB   1 ? 1 
ATOM   1136 C CG1  . ILE   A 1 80  ? -4.066  23.745 3.266   1   27.756 ? 92  ILE   A CG1  1 ? 1 
ATOM   1137 C CG2  . ILE   A 1 80  ? -4.648  22.736 1.021   1   27.584 ? 92  ILE   A CG2  1 ? 1 
ATOM   1138 C CD1  . ILE   A 1 80  ? -2.734  23.044 3.568   1   27.48  ? 92  ILE   A CD1  1 ? 1 
ATOM   1139 H H    . ILE   A 1 80  ? -6.506  22.634 4.586   1   24.068 ? 92  ILE   A H    1 c 1 
ATOM   1140 H HA   . ILE   A 1 80  ? -6.522  24.317 2.453   1   26.42  ? 92  ILE   A HA   1 c 1 
ATOM   1141 H HB   . ILE   A 1 80  ? -5.026  21.964 2.885   1   25.101 ? 92  ILE   A HB   1 c 1 
ATOM   1142 H HG12 . ILE   A 1 80  ? -3.886  24.551 2.74    1   28.424 ? 92  ILE   A HG12 1 c 1 
ATOM   1143 H HG13 . ILE   A 1 80  ? -4.474  24.023 4.111   1   27.762 ? 92  ILE   A HG13 1 c 1 
ATOM   1144 H HG21 . ILE   A 1 80  ? -3.68   22.69  0.959   1   26.83  ? 92  ILE   A HG21 1 c 1 
ATOM   1145 H HG22 . ILE   A 1 80  ? -4.966  23.509 0.526   1   27.96  ? 92  ILE   A HG22 1 c 1 
ATOM   1146 H HG23 . ILE   A 1 80  ? -5.032  21.928 0.639   1   26.491 ? 92  ILE   A HG23 1 c 1 
ATOM   1147 H HD11 . ILE   A 1 80  ? -2.905  22.213 4.051   1   26.529 ? 92  ILE   A HD11 1 c 1 
ATOM   1148 H HD12 . ILE   A 1 80  ? -2.176  23.628 4.117   1   27.841 ? 92  ILE   A HD12 1 c 1 
ATOM   1149 H HD13 . ILE   A 1 80  ? -2.269  22.844 2.734   1   27.213 ? 92  ILE   A HD13 1 c 1 
ATOM   1150 N N    . GLY   A 1 81  ? -7.809  21.405 1.952   1   24.461 ? 93  GLY   A N    1 ? 1 
ATOM   1151 C CA   . GLY   A 1 81  ? -8.561  20.559 1.036   1   24.632 ? 93  GLY   A CA   1 ? 1 
ATOM   1152 C C    . GLY   A 1 81  ? -10.009 20.998 0.843   1   25.265 ? 93  GLY   A C    1 ? 1 
ATOM   1153 O O    . GLY   A 1 81  ? -10.504 21.094 -0.28   1   23.654 ? 93  GLY   A O    1 ? 1 
ATOM   1154 H H    . GLY   A 1 81  ? -7.546  21.047 2.751   1   24.112 ? 93  GLY   A H    1 c 1 
ATOM   1155 H HA2  . GLY   A 1 81  ? -8.107  20.558 0.162   1   24.471 ? 93  GLY   A HA2  1 c 1 
ATOM   1156 H HA3  . GLY   A 1 81  ? -8.548  19.634 1.378   1   23.868 ? 93  GLY   A HA3  1 c 1 
ATOM   1157 N N    . VAL   A 1 82  ? -10.696 21.243 1.962   1   25.791 ? 94  VAL   A N    1 ? 1 
ATOM   1158 C CA   . VAL   A 1 82  ? -12.103 21.537 1.904   1   26.548 ? 94  VAL   A CA   1 ? 1 
ATOM   1159 C C    . VAL   A 1 82  ? -12.297 22.91  1.245   1   27.828 ? 94  VAL   A C    1 ? 1 
ATOM   1160 O O    . VAL   A 1 82  ? -13.282 23.102 0.542   1   28.561 ? 94  VAL   A O    1 ? 1 
ATOM   1161 C CB   . VAL   A 1 82  ? -12.77  21.396 3.289   1   27.671 ? 94  VAL   A CB   1 ? 1 
ATOM   1162 C CG1  . VAL   A 1 82  ? -14.233 21.817 3.255   1   30.272 ? 94  VAL   A CG1  1 ? 1 
ATOM   1163 C CG2  . VAL   A 1 82  ? -12.62  19.959 3.81    1   26.137 ? 94  VAL   A CG2  1 ? 1 
ATOM   1164 H H    . VAL   A 1 82  ? -10.275 21.228 2.773   1   25.182 ? 94  VAL   A H    1 c 1 
ATOM   1165 H HA   . VAL   A 1 82  ? -12.514 20.872 1.318   1   26.821 ? 94  VAL   A HA   1 c 1 
ATOM   1166 H HB   . VAL   A 1 82  ? -12.293 21.998 3.907   1   27.538 ? 94  VAL   A HB   1 c 1 
ATOM   1167 H HG11 . VAL   A 1 82  ? -14.644 21.497 2.435   1   30.354 ? 94  VAL   A HG11 1 c 1 
ATOM   1168 H HG12 . VAL   A 1 82  ? -14.293 22.787 3.29    1   30.901 ? 94  VAL   A HG12 1 c 1 
ATOM   1169 H HG13 . VAL   A 1 82  ? -14.698 21.437 4.019   1   30.337 ? 94  VAL   A HG13 1 c 1 
ATOM   1170 H HG21 . VAL   A 1 82  ? -13.083 19.871 4.66    1   26.752 ? 94  VAL   A HG21 1 c 1 
ATOM   1171 H HG22 . VAL   A 1 82  ? -11.678 19.753 3.933   1   25.302 ? 94  VAL   A HG22 1 c 1 
ATOM   1172 H HG23 . VAL   A 1 82  ? -13.004 19.339 3.168   1   26.406 ? 94  VAL   A HG23 1 c 1 
ATOM   1173 N N    . ALA   A 1 83  ? -11.334 23.831 1.39    1   26.573 ? 95  ALA   A N    1 ? 1 
ATOM   1174 C CA   . ALA   A 1 83  ? -11.402 25.109 0.696   1   27.41  ? 95  ALA   A CA   1 ? 1 
ATOM   1175 C C    . ALA   A 1 83  ? -11.428 24.937 -0.825  1   27.382 ? 95  ALA   A C    1 ? 1 
ATOM   1176 O O    . ALA   A 1 83  ? -11.837 25.853 -1.512  1   29.562 ? 95  ALA   A O    1 ? 1 
ATOM   1177 C CB   . ALA   A 1 83  ? -10.236 25.981 1.1     1   27.91  ? 95  ALA   A CB   1 ? 1 
ATOM   1178 H H    . ALA   A 1 83  ? -10.625 23.663 1.94    1   25.848 ? 95  ALA   A H    1 c 1 
ATOM   1179 H HA   . ALA   A 1 83  ? -12.248 25.56  0.968   1   28.802 ? 95  ALA   A HA   1 c 1 
ATOM   1180 H HB1  . ALA   A 1 83  ? -10.263 26.141 2.059   1   27.82  ? 95  ALA   A HB1  1 c 1 
ATOM   1181 H HB2  . ALA   A 1 83  ? -9.401  25.537 0.873   1   26.724 ? 95  ALA   A HB2  1 c 1 
ATOM   1182 H HB3  . ALA   A 1 83  ? -10.285 26.83  0.631   1   29.133 ? 95  ALA   A HB3  1 c 1 
ATOM   1183 N N    . THR   A 1 84  ? -10.99  23.799 -1.359  1   26.945 ? 96  THR   A N    1 ? 1 
ATOM   1184 C CA   . THR   A 1 84  ? -10.999 23.578 -2.809  1   28.439 ? 96  THR   A CA   1 ? 1 
ATOM   1185 C C    . THR   A 1 84  ? -12.281 22.898 -3.281  1   30.35  ? 96  THR   A C    1 ? 1 
ATOM   1186 O O    . THR   A 1 84  ? -12.454 22.723 -4.492  1   28.299 ? 96  THR   A O    1 ? 1 
ATOM   1187 C CB   . THR   A 1 84  ? -9.816  22.72  -3.254  1   27.735 ? 96  THR   A CB   1 ? 1 
ATOM   1188 O OG1  . THR   A 1 84  ? -10.056 21.389 -2.807  1   24.512 ? 96  THR   A OG1  1 ? 1 
ATOM   1189 C CG2  . THR   A 1 84  ? -8.481  23.224 -2.733  1   28.837 ? 96  THR   A CG2  1 ? 1 
ATOM   1190 H H    . THR   A 1 84  ? -10.654 23.145 -0.818  1   25.817 ? 96  THR   A H    1 c 1 
ATOM   1191 H HA   . THR   A 1 84  ? -10.928 24.45  -3.254  1   29.704 ? 96  THR   A HA   1 c 1 
ATOM   1192 H HB   . THR   A 1 84  ? -9.778  22.721 -4.241  1   28.078 ? 96  THR   A HB   1 c 1 
ATOM   1193 H HG1  . THR   A 1 84  ? -10.073 21.379 -1.944  0   30     ? 96  THR   A HG1  1 c 1 
ATOM   1194 H HG21 . THR   A 1 84  ? -7.759  22.734 -3.161  1   27.724 ? 96  THR   A HG21 1 c 1 
ATOM   1195 H HG22 . THR   A 1 84  ? -8.436  23.09  -1.773  1   27.631 ? 96  THR   A HG22 1 c 1 
ATOM   1196 H HG23 . THR   A 1 84  ? -8.391  24.171 -2.932  1   29.358 ? 96  THR   A HG23 1 c 1 
ATOM   1197 N N    . MET   A 1 85  ? -13.183 22.506 -2.367  1   30.837 ? 97  MET   A N    1 ? 1 
ATOM   1198 C CA   . MET   A 1 85  ? -14.31  21.657 -2.741  1   31.916 ? 97  MET   A CA   1 ? 1 
ATOM   1199 C C    . MET   A 1 85  ? -15.587 22.457 -3.001  1   34.368 ? 97  MET   A C    1 ? 1 
ATOM   1200 O O    . MET   A 1 85  ? -15.823 23.484 -2.371  1   33.409 ? 97  MET   A O    1 ? 1 
ATOM   1201 C CB   . MET   A 1 85  ? -14.583 20.639 -1.631  1   31.559 ? 97  MET   A CB   1 ? 1 
ATOM   1202 C CG   . MET   A 1 85  ? -13.409 19.686 -1.389  1   29.481 ? 97  MET   A CG   1 ? 1 
ATOM   1203 S SD   . MET   A 1 85  ? -13.851 18.5   -0.119  1   29.272 ? 97  MET   A SD   1 ? 1 
ATOM   1204 C CE   . MET   A 1 85  ? -15.218 17.535 -0.8    1   30.936 ? 97  MET   A CE   1 ? 1 
ATOM   1205 H H    . MET   A 1 85  ? -13.101 22.774 -1.497  1   30.499 ? 97  MET   A H    1 c 1 
ATOM   1206 H HA   . MET   A 1 85  ? -14.071 21.172 -3.571  1   31.795 ? 97  MET   A HA   1 c 1 
ATOM   1207 H HB2  . MET   A 1 85  ? -14.781 21.123 -0.801  1   31.594 ? 97  MET   A HB2  1 c 1 
ATOM   1208 H HB3  . MET   A 1 85  ? -15.377 20.117 -1.872  1   32.135 ? 97  MET   A HB3  1 c 1 
ATOM   1209 H HG2  . MET   A 1 85  ? -13.188 19.212 -2.213  1   29.491 ? 97  MET   A HG2  1 c 1 
ATOM   1210 H HG3  . MET   A 1 85  ? -12.626 20.19  -1.101  1   28.903 ? 97  MET   A HG3  1 c 1 
ATOM   1211 H HE1  . MET   A 1 85  ? -15.49  16.859 -0.153  1   30.924 ? 97  MET   A HE1  1 c 1 
ATOM   1212 H HE2  . MET   A 1 85  ? -15.972 18.124 -0.988  1   32.026 ? 97  MET   A HE2  1 c 1 
ATOM   1213 H HE3  . MET   A 1 85  ? -14.93  17.1   -1.624  1   30.803 ? 97  MET   A HE3  1 c 1 
ATOM   1214 N N    . LYS   A 1 86  ? -16.43  21.958 -3.925  1   35.471 ? 98  LYS   A N    1 ? 1 
ATOM   1215 C CA   . LYS   A 1 86  ? -17.76  22.506 -4.149  1   39.056 ? 98  LYS   A CA   1 ? 1 
ATOM   1216 C C    . LYS   A 1 86  ? -18.816 21.697 -3.401  1   38.824 ? 98  LYS   A C    1 ? 1 
ATOM   1217 O O    . LYS   A 1 86  ? -18.593 20.541 -3.039  1   37.532 ? 98  LYS   A O    1 ? 1 
ATOM   1218 C CB   . LYS   A 1 86  ? -18.029 22.546 -5.662  1   44.059 ? 98  LYS   A CB   1 ? 1 
ATOM   1219 C CG   . LYS   A 1 86  ? -17.162 23.62  -6.311  1   48.552 ? 98  LYS   A CG   1 ? 1 
ATOM   1220 C CD   . LYS   A 1 86  ? -16.999 23.591 -7.823  1   56.56  ? 98  LYS   A CD   1 ? 1 
ATOM   1221 C CE   . LYS   A 1 86  ? -16.042 24.668 -8.235  1   58.974 ? 98  LYS   A CE   1 ? 1 
ATOM   1222 N NZ   . LYS   A 1 86  ? -16.024 24.862 -9.684  1   62.569 ? 98  LYS   A NZ   1 ? 1 
ATOM   1223 H H    . LYS   A 1 86  ? -16.161 21.247 -4.432  1   35.258 ? 98  LYS   A H    1 c 1 
ATOM   1224 H HA   . LYS   A 1 86  ? -17.777 23.436 -3.807  1   39.939 ? 98  LYS   A HA   1 c 1 
ATOM   1225 H HB2  . LYS   A 1 86  ? -17.821 21.675 -6.063  1   43.337 ? 98  LYS   A HB2  1 c 1 
ATOM   1226 H HB3  . LYS   A 1 86  ? -18.975 22.748 -5.828  1   45.723 ? 98  LYS   A HB3  1 c 1 
ATOM   1227 H HG2  . LYS   A 1 86  ? -17.535 24.494 -6.061  1   50.188 ? 98  LYS   A HG2  1 c 1 
ATOM   1228 H HG3  . LYS   A 1 86  ? -16.268 23.57  -5.907  1   47.322 ? 98  LYS   A HG3  1 c 1 
ATOM   1229 H HD2  . LYS   A 1 86  ? -16.649 22.717 -8.102  1   54.288 ? 98  LYS   A HD2  1 c 1 
ATOM   1230 H HD3  . LYS   A 1 86  ? -17.869 23.739 -8.254  1   57.18  ? 98  LYS   A HD3  1 c 1 
ATOM   1231 H HE2  . LYS   A 1 86  ? -16.293 25.507 -7.807  1   59.838 ? 98  LYS   A HE2  1 c 1 
ATOM   1232 H HE3  . LYS   A 1 86  ? -15.145 24.434 -7.937  1   57.319 ? 98  LYS   A HE3  1 c 1 
ATOM   1233 H HZ1  . LYS   A 1 86  ? -16.869 24.872 -10.009 1   63.479 ? 98  LYS   A HZ1  1 c 1 
ATOM   1234 H HZ2  . LYS   A 1 86  ? -15.563 24.188 -10.075 1   61.13  ? 98  LYS   A HZ2  1 c 1 
ATOM   1235 H HZ3  . LYS   A 1 86  ? -15.621 25.649 -9.88   1   62.819 ? 98  LYS   A HZ3  1 c 1 
ATOM   1236 N N    . LYS   A 1 87  ? -19.981 22.323 -3.19   1   41.216 ? 99  LYS   A N    1 ? 1 
ATOM   1237 C CA   . LYS   A 1 87  ? -21.131 21.644 -2.618  1   43.682 ? 99  LYS   A CA   1 ? 1 
ATOM   1238 C C    . LYS   A 1 87  ? -21.448 20.405 -3.454  1   43.095 ? 99  LYS   A C    1 ? 1 
ATOM   1239 O O    . LYS   A 1 87  ? -21.513 20.482 -4.682  1   41.667 ? 99  LYS   A O    1 ? 1 
ATOM   1240 C CB   . LYS   A 1 87  ? -22.371 22.542 -2.541  1   49.534 ? 99  LYS   A CB   1 ? 1 
ATOM   1241 C CG   . LYS   A 1 87  ? -23.45  21.992 -1.628  1   53.064 ? 99  LYS   A CG   1 ? 1 
ATOM   1242 C CD   . LYS   A 1 87  ? -24.71  22.842 -1.564  1   58.122 ? 99  LYS   A CD   1 ? 1 
ATOM   1243 C CE   . LYS   A 1 87  ? -25.591 22.336 -0.475  1   60.869 ? 99  LYS   A CE   1 ? 1 
ATOM   1244 N NZ   . LYS   A 1 87  ? -26.838 23.09  -0.375  1   65.157 ? 99  LYS   A NZ   1 ? 1 
ATOM   1245 H H    . LYS   A 1 87  ? -20.06  23.206 -3.413  1   42.532 ? 99  LYS   A H    1 c 1 
ATOM   1246 H HA   . LYS   A 1 87  ? -20.893 21.358 -1.7    1   42.746 ? 99  LYS   A HA   1 c 1 
ATOM   1247 H HB2  . LYS   A 1 87  ? -22.105 23.428 -2.215  1   49.431 ? 99  LYS   A HB2  1 c 1 
ATOM   1248 H HB3  . LYS   A 1 87  ? -22.746 22.651 -3.441  1   50.528 ? 99  LYS   A HB3  1 c 1 
ATOM   1249 H HG2  . LYS   A 1 87  ? -23.69  21.091 -1.936  1   52.877 ? 99  LYS   A HG2  1 c 1 
ATOM   1250 H HG3  . LYS   A 1 87  ? -23.077 21.907 -0.724  1   51.852 ? 99  LYS   A HG3  1 c 1 
ATOM   1251 H HD2  . LYS   A 1 87  ? -24.471 23.777 -1.384  1   58.352 ? 99  LYS   A HD2  1 c 1 
ATOM   1252 H HD3  . LYS   A 1 87  ? -25.188 22.793 -2.421  1   59.364 ? 99  LYS   A HD3  1 c 1 
ATOM   1253 H HE2  . LYS   A 1 87  ? -25.8   21.398 -0.636  1   60.515 ? 99  LYS   A HE2  1 c 1 
ATOM   1254 H HE3  . LYS   A 1 87  ? -25.119 22.399 0.373   1   59.447 ? 99  LYS   A HE3  1 c 1 
ATOM   1255 H HZ1  . LYS   A 1 87  ? -27.334 22.963 -1.122  1   66.126 ? 99  LYS   A HZ1  1 c 1 
ATOM   1256 H HZ2  . LYS   A 1 87  ? -26.656 23.973 -0.284  1   65.246 ? 99  LYS   A HZ2  1 c 1 
ATOM   1257 H HZ3  . LYS   A 1 87  ? -27.308 22.807 0.346   1   65.565 ? 99  LYS   A HZ3  1 c 1 
ATOM   1258 N N    . GLY   A 1 88  ? -21.553 19.263 -2.753  1   42.207 ? 100 GLY   A N    1 ? 1 
ATOM   1259 C CA   . GLY   A 1 88  ? -21.943 17.991 -3.338  1   43.032 ? 100 GLY   A CA   1 ? 1 
ATOM   1260 C C    . GLY   A 1 88  ? -20.758 17.161 -3.822  1   40.151 ? 100 GLY   A C    1 ? 1 
ATOM   1261 O O    . GLY   A 1 88  ? -20.937 16.007 -4.207  1   40.587 ? 100 GLY   A O    1 ? 1 
ATOM   1262 H H    . GLY   A 1 88  ? -21.369 19.284 -1.858  1   41.606 ? 100 GLY   A H    1 c 1 
ATOM   1263 H HA2  . GLY   A 1 88  ? -22.445 17.474 -2.665  1   43.293 ? 100 GLY   A HA2  1 c 1 
ATOM   1264 H HA3  . GLY   A 1 88  ? -22.55  18.161 -4.096  1   44.346 ? 100 GLY   A HA3  1 c 1 
ATOM   1265 N N    . GLU   A 1 89  ? -19.56  17.76  -3.837  1   37.28  ? 101 GLU   A N    1 ? 1 
ATOM   1266 C CA   . GLU   A 1 89  ? -18.345 17.081 -4.259  1   35.591 ? 101 GLU   A CA   1 ? 1 
ATOM   1267 C C    . GLU   A 1 89  ? -17.97  16.005 -3.244  1   34.438 ? 101 GLU   A C    1 ? 1 
ATOM   1268 O O    . GLU   A 1 89  ? -18.132 16.183 -2.016  1   31.587 ? 101 GLU   A O    1 ? 1 
ATOM   1269 C CB   . GLU   A 1 89  ? -17.195 18.088 -4.385  1   34.147 ? 101 GLU   A CB   1 ? 1 
ATOM   1270 C CG   . GLU   A 1 89  ? -15.838 17.506 -4.79   1   32.163 ? 101 GLU   A CG   1 ? 1 
ATOM   1271 C CD   . GLU   A 1 89  ? -14.785 18.58  -4.975  1   31.38  ? 101 GLU   A CD   1 ? 1 
ATOM   1272 O OE1  . GLU   A 1 89  ? -15.097 19.678 -5.532  1   31.595 ? 101 GLU   A OE1  1 ? 1 
ATOM   1273 O OE2  . GLU   A 1 89  ? -13.636 18.323 -4.548  1   30.039 ? 101 GLU   A OE2  1 ? 1 
ATOM   1274 H H    . GLU   A 1 89  ? -19.496 18.63  -3.568  1   37.522 ? 101 GLU   A H    1 c 1 
ATOM   1275 H HA   . GLU   A 1 89  ? -18.512 16.659 -5.138  1   36.357 ? 101 GLU   A HA   1 c 1 
ATOM   1276 H HB2  . GLU   A 1 89  ? -17.451 18.768 -5.042  1   35.148 ? 101 GLU   A HB2  1 c 1 
ATOM   1277 H HB3  . GLU   A 1 89  ? -17.082 18.537 -3.523  1   33.564 ? 101 GLU   A HB3  1 c 1 
ATOM   1278 H HG2  . GLU   A 1 89  ? -15.532 16.88  -4.1    1   31.35  ? 101 GLU   A HG2  1 c 1 
ATOM   1279 H HG3  . GLU   A 1 89  ? -15.935 17.01  -5.631  1   32.9   ? 101 GLU   A HG3  1 c 1 
ATOM   1280 N N    . ILE   A 1 90  ? -17.452 14.894 -3.795  1   33.495 ? 102 ILE   A N    1 ? 1 
ATOM   1281 C CA   . ILE   A 1 90  ? -16.731 13.915 -2.997  1   31.619 ? 102 ILE   A CA   1 ? 1 
ATOM   1282 C C    . ILE   A 1 90  ? -15.295 13.871 -3.494  1   29.537 ? 102 ILE   A C    1 ? 1 
ATOM   1283 O O    . ILE   A 1 90  ? -15.06  13.717 -4.701  1   30.358 ? 102 ILE   A O    1 ? 1 
ATOM   1284 C CB   . ILE   A 1 90  ? -17.394 12.538 -3.053  1   33.723 ? 102 ILE   A CB   1 ? 1 
ATOM   1285 C CG1  . ILE   A 1 90  ? -18.851 12.599 -2.555  1   36.519 ? 102 ILE   A CG1  1 ? 1 
ATOM   1286 C CG2  . ILE   A 1 90  ? -16.552 11.519 -2.269  1   34.129 ? 102 ILE   A CG2  1 ? 1 
ATOM   1287 C CD1  . ILE   A 1 90  ? -19.656 11.332 -2.814  1   39.09  ? 102 ILE   A CD1  1 ? 1 
ATOM   1288 H H    . ILE   A 1 90  ? -17.553 14.743 -4.69   1   34.2   ? 102 ILE   A H    1 c 1 
ATOM   1289 H HA   . ILE   A 1 90  ? -16.732 14.214 -2.071  1   31.222 ? 102 ILE   A HA   1 c 1 
ATOM   1290 H HB   . ILE   A 1 90  ? -17.412 12.254 -3.989  1   34.685 ? 102 ILE   A HB   1 c 1 
ATOM   1291 H HG12 . ILE   A 1 90  ? -18.844 12.774 -1.593  1   35.935 ? 102 ILE   A HG12 1 c 1 
ATOM   1292 H HG13 . ILE   A 1 90  ? -19.302 13.35  -2.991  1   36.998 ? 102 ILE   A HG13 1 c 1 
ATOM   1293 H HG21 . ILE   A 1 90  ? -17.047 10.689 -2.173  1   34.931 ? 102 ILE   A HG21 1 c 1 
ATOM   1294 H HG22 . ILE   A 1 90  ? -16.348 11.875 -1.387  1   32.867 ? 102 ILE   A HG22 1 c 1 
ATOM   1295 H HG23 . ILE   A 1 90  ? -15.723 11.343 -2.745  1   32.94  ? 102 ILE   A HG23 1 c 1 
ATOM   1296 H HD11 . ILE   A 1 90  ? -19.629 11.116 -3.765  1   39.548 ? 102 ILE   A HD11 1 c 1 
ATOM   1297 H HD12 . ILE   A 1 90  ? -20.582 11.474 -2.541  1   40.349 ? 102 ILE   A HD12 1 c 1 
ATOM   1298 H HD13 . ILE   A 1 90  ? -19.281 10.59  -2.303  1   38.664 ? 102 ILE   A HD13 1 c 1 
ATOM   1299 N N    . ALA   A 1 91  ? -14.368 14.029 -2.549  1   27.395 ? 103 ALA   A N    1 ? 1 
ATOM   1300 C CA   . ALA   A 1 91  ? -12.95  14.05  -2.868  1   26.365 ? 103 ALA   A CA   1 ? 1 
ATOM   1301 C C    . ALA   A 1 91  ? -12.219 13.035 -2.005  1   25.889 ? 103 ALA   A C    1 ? 1 
ATOM   1302 O O    . ALA   A 1 91  ? -12.667 12.729 -0.895  1   26.604 ? 103 ALA   A O    1 ? 1 
ATOM   1303 C CB   . ALA   A 1 91  ? -12.432 15.444 -2.662  1   25.53  ? 103 ALA   A CB   1 ? 1 
ATOM   1304 H H    . ALA   A 1 91  ? -14.623 14.125 -1.677  1   27.484 ? 103 ALA   A H    1 c 1 
ATOM   1305 H HA   . ALA   A 1 91  ? -12.835 13.793 -3.823  1   26.87  ? 103 ALA   A HA   1 c 1 
ATOM   1306 H HB1  . ALA   A 1 91  ? -12.909 16.06  -3.243  1   26.279 ? 103 ALA   A HB1  1 c 1 
ATOM   1307 H HB2  . ALA   A 1 91  ? -12.564 15.709 -1.736  1   25.198 ? 103 ALA   A HB2  1 c 1 
ATOM   1308 H HB3  . ALA   A 1 91  ? -11.483 15.475 -2.872  1   24.775 ? 103 ALA   A HB3  1 c 1 
ATOM   1309 N N    . HIS   A 1 92  ? -11.113 12.501 -2.534  1   24.409 ? 104 HIS   A N    1 ? 1 
ATOM   1310 C CA   . HIS   A 1 92  ? -10.179 11.715 -1.755  1   24.055 ? 104 HIS   A CA   1 ? 1 
ATOM   1311 C C    . HIS   A 1 92  ? -8.954  12.576 -1.451  1   23.881 ? 104 HIS   A C    1 ? 1 
ATOM   1312 O O    . HIS   A 1 92  ? -8.473  13.261 -2.344  1   23.892 ? 104 HIS   A O    1 ? 1 
ATOM   1313 C CB   . HIS   A 1 92  ? -9.799  10.443 -2.504  1   25.37  ? 104 HIS   A CB   1 ? 1 
ATOM   1314 C CG   . HIS   A 1 92  ? -10.854 9.402  -2.493  1   27.145 ? 104 HIS   A CG   1 ? 1 
ATOM   1315 N ND1  . HIS   A 1 92  ? -10.714 8.208  -3.165  1   29.196 ? 104 HIS   A ND1  1 ? 1 
ATOM   1316 C CD2  . HIS   A 1 92  ? -12.053 9.356  -1.886  1   28.658 ? 104 HIS   A CD2  1 ? 1 
ATOM   1317 C CE1  . HIS   A 1 92  ? -11.806 7.474  -2.975  1   31.462 ? 104 HIS   A CE1  1 ? 1 
ATOM   1318 N NE2  . HIS   A 1 92  ? -12.632 8.149  -2.187  1   31.82  ? 104 HIS   A NE2  1 ? 1 
ATOM   1319 H H    . HIS   A 1 92  ? -10.936 12.636 -3.42   1   24.988 ? 104 HIS   A H    1 c 1 
ATOM   1320 H HA   . HIS   A 1 92  ? -10.607 11.47  -0.902  1   24.478 ? 104 HIS   A HA   1 c 1 
ATOM   1321 H HB2  . HIS   A 1 92  ? -9.593  10.677 -3.435  1   25.484 ? 104 HIS   A HB2  1 c 1 
ATOM   1322 H HB3  . HIS   A 1 92  ? -8.983  10.073 -2.102  1   24.837 ? 104 HIS   A HB3  1 c 1 
ATOM   1323 H HD1  . HIS   A 1 92  ? -10.01  8.016  -3.695  0   30     ? 104 HIS   A HD1  1 c 1 
ATOM   1324 H HD2  . HIS   A 1 92  ? -12.43  10.023 -1.346  1   28.335 ? 104 HIS   A HD2  1 c 1 
ATOM   1325 H HE1  . HIS   A 1 92  ? -11.959 6.616  -3.328  1   32.822 ? 104 HIS   A HE1  1 c 1 
ATOM   1326 H HE2  . HIS   A 1 92  ? -13.385 7.841  -1.871  0   30     ? 104 HIS   A HE2  1 c 1 
ATOM   1327 N N    . LEU   A 1 93  ? -8.5    12.572 -0.178  1   23.204 ? 105 LEU   A N    1 ? 1 
ATOM   1328 C CA   . LEU   A 1 93  ? -7.261  13.235 0.225   1   23.95  ? 105 LEU   A CA   1 ? 1 
ATOM   1329 C C    . LEU   A 1 93  ? -6.295  12.204 0.804   1   24.887 ? 105 LEU   A C    1 ? 1 
ATOM   1330 O O    . LEU   A 1 93  ? -6.706  11.323 1.564   1   25.833 ? 105 LEU   A O    1 ? 1 
ATOM   1331 C CB   . LEU   A 1 93  ? -7.478  14.337 1.269   1   22.83  ? 105 LEU   A CB   1 ? 1 
ATOM   1332 C CG   . LEU   A 1 93  ? -8.454  15.466 0.955   1   22.74  ? 105 LEU   A CG   1 ? 1 
ATOM   1333 C CD1  . LEU   A 1 93  ? -8.561  16.441 2.114   1   22.996 ? 105 LEU   A CD1  1 ? 1 
ATOM   1334 C CD2  . LEU   A 1 93  ? -8.005  16.166 -0.309  1   23.091 ? 105 LEU   A CD2  1 ? 1 
ATOM   1335 H H    . LEU   A 1 93  ? -8.986  12.137 0.462   1   23.884 ? 105 LEU   A H    1 c 1 
ATOM   1336 H HA   . LEU   A 1 93  ? -6.85   13.633 -0.578  1   23.588 ? 105 LEU   A HA   1 c 1 
ATOM   1337 H HB2  . LEU   A 1 93  ? -7.773  13.905 2.104   1   22.97  ? 105 LEU   A HB2  1 c 1 
ATOM   1338 H HB3  . LEU   A 1 93  ? -6.601  14.74  1.465   1   22.327 ? 105 LEU   A HB3  1 c 1 
ATOM   1339 H HG   . LEU   A 1 93  ? -9.349  15.071 0.793   1   23.616 ? 105 LEU   A HG   1 c 1 
ATOM   1340 H HD11 . LEU   A 1 93  ? -8.844  15.966 2.913   1   22.944 ? 105 LEU   A HD11 1 c 1 
ATOM   1341 H HD12 . LEU   A 1 93  ? -9.212  17.13  1.9     1   23.384 ? 105 LEU   A HD12 1 c 1 
ATOM   1342 H HD13 . LEU   A 1 93  ? -7.695  16.853 2.273   1   22.386 ? 105 LEU   A HD13 1 c 1 
ATOM   1343 H HD21 . LEU   A 1 93  ? -8.168  15.591 -1.075  1   23.405 ? 105 LEU   A HD21 1 c 1 
ATOM   1344 H HD22 . LEU   A 1 93  ? -7.055  16.365 -0.25   1   22.536 ? 105 LEU   A HD22 1 c 1 
ATOM   1345 H HD23 . LEU   A 1 93  ? -8.502  16.994 -0.415  1   23.403 ? 105 LEU   A HD23 1 c 1 
ATOM   1346 N N    . LEU   A 1 94  ? -5.016  12.336 0.459   1   24.083 ? 106 LEU   A N    1 ? 1 
ATOM   1347 C CA   . LEU   A 1 94  ? -3.926  11.588 1.071   1   23.865 ? 106 LEU   A CA   1 ? 1 
ATOM   1348 C C    . LEU   A 1 94  ? -2.956  12.616 1.64    1   25.247 ? 106 LEU   A C    1 ? 1 
ATOM   1349 O O    . LEU   A 1 94  ? -2.552  13.532 0.929   1   21.653 ? 106 LEU   A O    1 ? 1 
ATOM   1350 C CB   . LEU   A 1 94  ? -3.196  10.673 0.103   1   25.74  ? 106 LEU   A CB   1 ? 1 
ATOM   1351 C CG   . LEU   A 1 94  ? -2.229  9.677  0.748   1   25.229 ? 106 LEU   A CG   1 ? 1 
ATOM   1352 C CD1  . LEU   A 1 94  ? -2.97   8.648  1.591   1   25.852 ? 106 LEU   A CD1  1 ? 1 
ATOM   1353 C CD2  . LEU   A 1 94  ? -1.375  8.971  -0.262  1   28.49  ? 106 LEU   A CD2  1 ? 1 
ATOM   1354 H H    . LEU   A 1 94  ? -4.806  12.93  -0.203  1   24.028 ? 106 LEU   A H    1 c 1 
ATOM   1355 H HA   . LEU   A 1 94  ? -4.294  11.051 1.815   1   24.72  ? 106 LEU   A HA   1 c 1 
ATOM   1356 H HB2  . LEU   A 1 94  ? -3.869  10.168 -0.409  1   25.891 ? 106 LEU   A HB2  1 c 1 
ATOM   1357 H HB3  . LEU   A 1 94  ? -2.691  11.234 -0.531  1   25.074 ? 106 LEU   A HB3  1 c 1 
ATOM   1358 H HG   . LEU   A 1 94  ? -1.625  10.182 1.351   1   25.254 ? 106 LEU   A HG   1 c 1 
ATOM   1359 H HD11 . LEU   A 1 94  ? -3.341  9.079  2.378   1   25.41  ? 106 LEU   A HD11 1 c 1 
ATOM   1360 H HD12 . LEU   A 1 94  ? -2.354  7.949  1.867   1   26.524 ? 106 LEU   A HD12 1 c 1 
ATOM   1361 H HD13 . LEU   A 1 94  ? -3.689  8.257  1.067   1   26.509 ? 106 LEU   A HD13 1 c 1 
ATOM   1362 H HD21 . LEU   A 1 94  ? -0.849  9.623  -0.754  1   27.435 ? 106 LEU   A HD21 1 c 1 
ATOM   1363 H HD22 . LEU   A 1 94  ? -1.942  8.481  -0.88   1   28.449 ? 106 LEU   A HD22 1 c 1 
ATOM   1364 H HD23 . LEU   A 1 94  ? -0.78   8.351  0.192   1   28.235 ? 106 LEU   A HD23 1 c 1 
ATOM   1365 N N    . ILE   A 1 95  ? -2.619  12.485 2.938   1   23.487 ? 107 ILE   A N    1 ? 1 
ATOM   1366 C CA   . ILE   A 1 95  ? -2.016  13.572 3.686   1   22.797 ? 107 ILE   A CA   1 ? 1 
ATOM   1367 C C    . ILE   A 1 95  ? -0.762  13.109 4.418   1   23.048 ? 107 ILE   A C    1 ? 1 
ATOM   1368 O O    . ILE   A 1 95  ? -0.839  12.226 5.263   1   24.356 ? 107 ILE   A O    1 ? 1 
ATOM   1369 C CB   . ILE   A 1 95  ? -3.047  14.107 4.692   1   22.578 ? 107 ILE   A CB   1 ? 1 
ATOM   1370 C CG1  . ILE   A 1 95  ? -4.32   14.583 3.985   1   24.384 ? 107 ILE   A CG1  1 ? 1 
ATOM   1371 C CG2  . ILE   A 1 95  ? -2.428  15.198 5.56    1   21.144 ? 107 ILE   A CG2  1 ? 1 
ATOM   1372 C CD1  . ILE   A 1 95  ? -5.55   14.537 4.885   1   25.553 ? 107 ILE   A CD1  1 ? 1 
ATOM   1373 H H    . ILE   A 1 95  ? -2.769  11.689 3.363   1   24.179 ? 107 ILE   A H    1 c 1 
ATOM   1374 H HA   . ILE   A 1 95  ? -1.78   14.289 3.069   1   22.69  ? 107 ILE   A HA   1 c 1 
ATOM   1375 H HB   . ILE   A 1 95  ? -3.296  13.366 5.279   1   22.976 ? 107 ILE   A HB   1 c 1 
ATOM   1376 H HG12 . ILE   A 1 95  ? -4.186  15.502 3.675   1   23.98  ? 107 ILE   A HG12 1 c 1 
ATOM   1377 H HG13 . ILE   A 1 95  ? -4.483  14.022 3.201   1   24.341 ? 107 ILE   A HG13 1 c 1 
ATOM   1378 H HG21 . ILE   A 1 95  ? -3.132  15.688 6.015   1   21.6   ? 107 ILE   A HG21 1 c 1 
ATOM   1379 H HG22 . ILE   A 1 95  ? -1.918  15.808 5.002   1   21.431 ? 107 ILE   A HG22 1 c 1 
ATOM   1380 H HG23 . ILE   A 1 95  ? -1.842  14.796 6.221   1   21.625 ? 107 ILE   A HG23 1 c 1 
ATOM   1381 H HD11 . ILE   A 1 95  ? -5.637  13.645 5.27    1   25.558 ? 107 ILE   A HD11 1 c 1 
ATOM   1382 H HD12 . ILE   A 1 95  ? -6.348  14.744 4.362   1   25.546 ? 107 ILE   A HD12 1 c 1 
ATOM   1383 H HD13 . ILE   A 1 95  ? -5.456  15.191 5.604   1   25.197 ? 107 ILE   A HD13 1 c 1 
ATOM   1384 N N    . LYS   A 1 96  ? 0.368   13.759 4.159   1   22.8   ? 108 LYS   A N    1 ? 1 
ATOM   1385 C CA   . LYS   A 1 96  ? 1.604   13.507 4.901   1   22.563 ? 108 LYS   A CA   1 ? 1 
ATOM   1386 C C    . LYS   A 1 96  ? 1.479   14.088 6.314   1   24.067 ? 108 LYS   A C    1 ? 1 
ATOM   1387 O O    . LYS   A 1 96  ? 0.66    14.976 6.57    1   22.114 ? 108 LYS   A O    1 ? 1 
ATOM   1388 C CB   . LYS   A 1 96  ? 2.815   14.173 4.243   1   25.997 ? 108 LYS   A CB   1 ? 1 
ATOM   1389 C CG   . LYS   A 1 96  ? 3.11    13.623 2.86    1   26.328 ? 108 LYS   A CG   1 ? 1 
ATOM   1390 C CD   . LYS   A 1 96  ? 4.393   14.142 2.212   1   31.803 ? 108 LYS   A CD   1 ? 1 
ATOM   1391 C CE   . LYS   A 1 96  ? 4.728   13.484 0.903   1   33.71  ? 108 LYS   A CE   1 ? 1 
ATOM   1392 N NZ   . LYS   A 1 96  ? 5.777   14.288 0.264   1   37.242 ? 108 LYS   A NZ   1 ? 1 
ATOM   1393 H H    . LYS   A 1 96  ? 0.378   14.387 3.495   1   22.649 ? 108 LYS   A H    1 c 1 
ATOM   1394 H HA   . LYS   A 1 96  ? 1.747   12.529 4.956   1   23.915 ? 108 LYS   A HA   1 c 1 
ATOM   1395 H HB2  . LYS   A 1 96  ? 2.647   15.137 4.168   1   25.009 ? 108 LYS   A HB2  1 c 1 
ATOM   1396 H HB3  . LYS   A 1 96  ? 3.606   14.05  4.805   1   25.593 ? 108 LYS   A HB3  1 c 1 
ATOM   1397 H HG2  . LYS   A 1 96  ? 3.163   12.646 2.923   1   27.725 ? 108 LYS   A HG2  1 c 1 
ATOM   1398 H HG3  . LYS   A 1 96  ? 2.352   13.839 2.274   1   27.02  ? 108 LYS   A HG3  1 c 1 
ATOM   1399 H HD2  . LYS   A 1 96  ? 4.305   15.109 2.069   1   30.736 ? 108 LYS   A HD2  1 c 1 
ATOM   1400 H HD3  . LYS   A 1 96  ? 5.138   14.002 2.836   1   31.268 ? 108 LYS   A HD3  1 c 1 
ATOM   1401 H HE2  . LYS   A 1 96  ? 5.054   12.578 1.051   1   34.523 ? 108 LYS   A HE2  1 c 1 
ATOM   1402 H HE3  . LYS   A 1 96  ? 3.943   13.45  0.327   1   33.74  ? 108 LYS   A HE3  1 c 1 
ATOM   1403 H HZ1  . LYS   A 1 96  ? 6.474   14.396 0.833   1   36.657 ? 108 LYS   A HZ1  1 c 1 
ATOM   1404 H HZ2  . LYS   A 1 96  ? 5.448   15.102 0.038   1   36.068 ? 108 LYS   A HZ2  1 c 1 
ATOM   1405 H HZ3  . LYS   A 1 96  ? 6.068   13.869 -0.485  1   36.968 ? 108 LYS   A HZ3  1 c 1 
ATOM   1406 N N    . PRO   A 1 97  ? 2.292   13.596 7.264   1   21.188 ? 109 PRO   A N    1 ? 1 
ATOM   1407 C CA   . PRO   A 1 97  ? 2.132   13.979 8.679   1   22.718 ? 109 PRO   A CA   1 ? 1 
ATOM   1408 C C    . PRO   A 1 97  ? 2.309   15.472 8.966   1   23.308 ? 109 PRO   A C    1 ? 1 
ATOM   1409 O O    . PRO   A 1 97  ? 1.73    16.009 9.916   1   23.801 ? 109 PRO   A O    1 ? 1 
ATOM   1410 C CB   . PRO   A 1 97  ? 3.18    13.131 9.38    1   24.749 ? 109 PRO   A CB   1 ? 1 
ATOM   1411 C CG   . PRO   A 1 97  ? 4.077   12.491 8.346   1   24.828 ? 109 PRO   A CG   1 ? 1 
ATOM   1412 C CD   . PRO   A 1 97  ? 3.339   12.592 7.031   1   24.548 ? 109 PRO   A CD   1 ? 1 
ATOM   1413 H HA   . PRO   A 1 97  ? 1.244   13.701 8.984   1   22.677 ? 109 PRO   A HA   1 c 1 
ATOM   1414 H HB2  . PRO   A 1 97  ? 3.71    13.682 9.989   1   24.736 ? 109 PRO   A HB2  1 c 1 
ATOM   1415 H HB3  . PRO   A 1 97  ? 2.747   12.441 9.92    1   24.748 ? 109 PRO   A HB3  1 c 1 
ATOM   1416 H HG2  . PRO   A 1 97  ? 4.933   12.961 8.293   1   25.272 ? 109 PRO   A HG2  1 c 1 
ATOM   1417 H HG3  . PRO   A 1 97  ? 4.249   11.554 8.569   1   25.619 ? 109 PRO   A HG3  1 c 1 
ATOM   1418 H HD2  . PRO   A 1 97  ? 3.939   12.877 6.321   1   23.988 ? 109 PRO   A HD2  1 c 1 
ATOM   1419 H HD3  . PRO   A 1 97  ? 2.941   11.734 6.786   1   24.028 ? 109 PRO   A HD3  1 c 1 
ATOM   1420 N N    . GLU   A 1 98  ? 3.088   16.162 8.129   1   24.307 ? 110 GLU   A N    1 ? 1 
ATOM   1421 C CA   . GLU   A 1 98  ? 3.278   17.606 8.254   1   25.385 ? 110 GLU   A CA   1 ? 1 
ATOM   1422 C C    . GLU   A 1 98  ? 1.958   18.381 8.141   1   23.954 ? 110 GLU   A C    1 ? 1 
ATOM   1423 O O    . GLU   A 1 98  ? 1.866   19.475 8.692   1   23.963 ? 110 GLU   A O    1 ? 1 
ATOM   1424 C CB   . GLU   A 1 98  ? 4.233   18.134 7.191   1   29.59  ? 110 GLU   A CB   1 ? 1 
ATOM   1425 C CG   . GLU   A 1 98  ? 5.679   17.683 7.389   1   33.835 ? 110 GLU   A CG   1 ? 1 
ATOM   1426 C CD   . GLU   A 1 98  ? 6.054   16.282 6.92    1   36.835 ? 110 GLU   A CD   1 ? 1 
ATOM   1427 O OE1  . GLU   A 1 98  ? 5.293   15.568 6.209   1   27.784 ? 110 GLU   A OE1  1 ? 1 
ATOM   1428 O OE2  . GLU   A 1 98  ? 7.194   15.912 7.339   1   42.609 ? 110 GLU   A OE2  1 ? 1 
ATOM   1429 H H    . GLU   A 1 98  ? 3.518   15.721 7.454   1   24.336 ? 110 GLU   A H    1 c 1 
ATOM   1430 H HA   . GLU   A 1 98  ? 3.67    17.787 9.146   1   26.219 ? 110 GLU   A HA   1 c 1 
ATOM   1431 H HB2  . GLU   A 1 98  ? 3.921   17.836 6.311   1   28.964 ? 110 GLU   A HB2  1 c 1 
ATOM   1432 H HB3  . GLU   A 1 98  ? 4.206   19.113 7.201   1   29.699 ? 110 GLU   A HB3  1 c 1 
ATOM   1433 H HG2  . GLU   A 1 98  ? 6.265   18.32  6.928   1   34.224 ? 110 GLU   A HG2  1 c 1 
ATOM   1434 H HG3  . GLU   A 1 98  ? 5.894   17.746 8.344   1   34.036 ? 110 GLU   A HG3  1 c 1 
ATOM   1435 N N    . TYR   A 1 99  ? 0.946   17.841 7.437   1   21.934 ? 111 TYR   A N    1 ? 1 
ATOM   1436 C CA   . TYR   A 1 99  ? -0.338  18.513 7.295   1   23.533 ? 111 TYR   A CA   1 ? 1 
ATOM   1437 C C    . TYR   A 1 99  ? -1.405  17.825 8.152   1   24.502 ? 111 TYR   A C    1 ? 1 
ATOM   1438 O O    . TYR   A 1 99  ? -2.606  18.086 7.994   1   22.874 ? 111 TYR   A O    1 ? 1 
ATOM   1439 C CB   . TYR   A 1 99  ? -0.702  18.585 5.793   1   23.056 ? 111 TYR   A CB   1 ? 1 
ATOM   1440 C CG   . TYR   A 1 99  ? 0.262   19.458 5.001   1   25.453 ? 111 TYR   A CG   1 ? 1 
ATOM   1441 C CD1  . TYR   A 1 99  ? 1.477   18.958 4.518   1   24.107 ? 111 TYR   A CD1  1 ? 1 
ATOM   1442 C CD2  . TYR   A 1 99  ? -0.015  20.803 4.765   1   24.643 ? 111 TYR   A CD2  1 ? 1 
ATOM   1443 C CE1  . TYR   A 1 99  ? 2.37    19.757 3.827   1   25.98  ? 111 TYR   A CE1  1 ? 1 
ATOM   1444 C CE2  . TYR   A 1 99  ? 0.853   21.608 4.052   1   26.759 ? 111 TYR   A CE2  1 ? 1 
ATOM   1445 C CZ   . TYR   A 1 99  ? 2.055   21.091 3.599   1   27.146 ? 111 TYR   A CZ   1 ? 1 
ATOM   1446 O OH   . TYR   A 1 99  ? 2.907   21.924 2.953   1   26.577 ? 111 TYR   A OH   1 ? 1 
ATOM   1447 H H    . TYR   A 1 99  ? 1.066   17.035 7.024   1   22.424 ? 111 TYR   A H    1 c 1 
ATOM   1448 H HA   . TYR   A 1 99  ? -0.237  19.445 7.625   1   23.801 ? 111 TYR   A HA   1 c 1 
ATOM   1449 H HB2  . TYR   A 1 99  ? -0.692  17.676 5.422   1   23.211 ? 111 TYR   A HB2  1 c 1 
ATOM   1450 H HB3  . TYR   A 1 99  ? -1.61   18.948 5.705   1   23.568 ? 111 TYR   A HB3  1 c 1 
ATOM   1451 H HD1  . TYR   A 1 99  ? 1.7     18.055 4.68    1   24.432 ? 111 TYR   A HD1  1 c 1 
ATOM   1452 H HD2  . TYR   A 1 99  ? -0.829  21.168 5.076   1   25.402 ? 111 TYR   A HD2  1 c 1 
ATOM   1453 H HE1  . TYR   A 1 99  ? 3.185   19.403 3.517   1   26.038 ? 111 TYR   A HE1  1 c 1 
ATOM   1454 H HE2  . TYR   A 1 99  ? 0.65    22.517 3.915   1   27.224 ? 111 TYR   A HE2  1 c 1 
ATOM   1455 H HH   . TYR   A 1 99  ? 3.648   21.532 2.74    0   30     ? 111 TYR   A HH   1 c 1 
ATOM   1456 N N    . ALA   A 1 100 ? -0.971  16.949 9.079   1   22.575 ? 112 ALA   A N    1 ? 1 
ATOM   1457 C CA   . ALA   A 1 100 ? -1.89   16.206 9.913   1   22.534 ? 112 ALA   A CA   1 ? 1 
ATOM   1458 C C    . ALA   A 1 100 ? -1.373  16.288 11.346  1   23.523 ? 112 ALA   A C    1 ? 1 
ATOM   1459 O O    . ALA   A 1 100 ? -1.487  17.349 11.939  1   26.511 ? 112 ALA   A O    1 ? 1 
ATOM   1460 C CB   . ALA   A 1 100 ? -2.07   14.799 9.397   1   21.989 ? 112 ALA   A CB   1 ? 1 
ATOM   1461 H H    . ALA   A 1 100 ? -0.075  16.822 9.196   1   23.097 ? 112 ALA   A H    1 c 1 
ATOM   1462 H HA   . ALA   A 1 100 ? -2.772  16.665 9.886   1   22.658 ? 112 ALA   A HA   1 c 1 
ATOM   1463 H HB1  . ALA   A 1 100 ? -2.605  14.815 8.585   1   21.854 ? 112 ALA   A HB1  1 c 1 
ATOM   1464 H HB2  . ALA   A 1 100 ? -1.201  14.409 9.2     1   22.113 ? 112 ALA   A HB2  1 c 1 
ATOM   1465 H HB3  . ALA   A 1 100 ? -2.521  14.259 10.067  1   22.562 ? 112 ALA   A HB3  1 c 1 
ATOM   1466 N N    . TYR   A 1 101 ? -0.802  15.214 11.907  1   24.738 ? 113 TYR   A N    1 ? 1 
ATOM   1467 C CA   . TYR   A 1 101 ? -0.501  15.214 13.349  1   23.048 ? 113 TYR   A CA   1 ? 1 
ATOM   1468 C C    . TYR   A 1 101 ? 0.997   15.118 13.635  1   23.274 ? 113 TYR   A C    1 ? 1 
ATOM   1469 O O    . TYR   A 1 101 ? 1.41    15.014 14.798  1   21.931 ? 113 TYR   A O    1 ? 1 
ATOM   1470 C CB   . TYR   A 1 101 ? -1.263  14.105 14.064  1   24.804 ? 113 TYR   A CB   1 ? 1 
ATOM   1471 C CG   . TYR   A 1 101 ? -2.773  14.263 13.979  1   24.539 ? 113 TYR   A CG   1 ? 1 
ATOM   1472 C CD1  . TYR   A 1 101 ? -3.449  15.131 14.82   1   24.279 ? 113 TYR   A CD1  1 ? 1 
ATOM   1473 C CD2  . TYR   A 1 101 ? -3.523  13.583 13.024  1   24.139 ? 113 TYR   A CD2  1 ? 1 
ATOM   1474 C CE1  . TYR   A 1 101 ? -4.832  15.247 14.784  1   24.211 ? 113 TYR   A CE1  1 ? 1 
ATOM   1475 C CE2  . TYR   A 1 101 ? -4.894  13.742 12.931  1   22.647 ? 113 TYR   A CE2  1 ? 1 
ATOM   1476 C CZ   . TYR   A 1 101 ? -5.559  14.571 13.821  1   24.36  ? 113 TYR   A CZ   1 ? 1 
ATOM   1477 O OH   . TYR   A 1 101 ? -6.929  14.746 13.747  1   23.132 ? 113 TYR   A OH   1 ? 1 
ATOM   1478 H H    . TYR   A 1 101 ? -0.6    14.477 11.406  1   23.714 ? 113 TYR   A H    1 c 1 
ATOM   1479 H HA   . TYR   A 1 101 ? -0.818  16.077 13.723  1   23.91  ? 113 TYR   A HA   1 c 1 
ATOM   1480 H HB2  . TYR   A 1 101 ? -1.009  13.242 13.667  1   24.476 ? 113 TYR   A HB2  1 c 1 
ATOM   1481 H HB3  . TYR   A 1 101 ? -0.996  14.097 15.01   1   25.25  ? 113 TYR   A HB3  1 c 1 
ATOM   1482 H HD1  . TYR   A 1 101 ? -2.969  15.584 15.496  1   24.834 ? 113 TYR   A HD1  1 c 1 
ATOM   1483 H HD2  . TYR   A 1 101 ? -3.085  13.009 12.416  1   23.453 ? 113 TYR   A HD2  1 c 1 
ATOM   1484 H HE1  . TYR   A 1 101 ? -5.269  15.841 15.371  1   25.049 ? 113 TYR   A HE1  1 c 1 
ATOM   1485 H HE2  . TYR   A 1 101 ? -5.381  13.261 12.285  1   23.213 ? 113 TYR   A HE2  1 c 1 
ATOM   1486 H HH   . TYR   A 1 101 ? -7.21   15.302 14.31   0   30     ? 113 TYR   A HH   1 c 1 
ATOM   1487 N N    . GLY   A 1 102 ? 1.812   15.18  12.584  1   20.896 ? 114 GLY   A N    1 ? 1 
ATOM   1488 C CA   . GLY   A 1 102 ? 3.239   15.451 12.698  1   22.87  ? 114 GLY   A CA   1 ? 1 
ATOM   1489 C C    . GLY   A 1 102 ? 3.998   14.356 13.448  1   23.546 ? 114 GLY   A C    1 ? 1 
ATOM   1490 O O    . GLY   A 1 102 ? 3.567   13.207 13.517  1   24.023 ? 114 GLY   A O    1 ? 1 
ATOM   1491 H H    . GLY   A 1 102 ? 1.468   15.04  11.75   1   21.125 ? 114 GLY   A H    1 c 1 
ATOM   1492 H HA2  . GLY   A 1 102 ? 3.617   15.546 11.793  1   22.096 ? 114 GLY   A HA2  1 c 1 
ATOM   1493 H HA3  . GLY   A 1 102 ? 3.362   16.311 13.165  1   22.812 ? 114 GLY   A HA3  1 c 1 
ATOM   1494 N N    . SER   A 1 103 ? 5.136   14.739 14.04   1   26.223 ? 115 SER   A N    1 ? 1 
ATOM   1495 C CA   . SER   A 1 103 ? 5.995   13.766 14.7    1   25.603 ? 115 SER   A CA   1 ? 1 
ATOM   1496 C C    . SER   A 1 103 ? 5.406   13.31  16.034  1   25.608 ? 115 SER   A C    1 ? 1 
ATOM   1497 O O    . SER   A 1 103 ? 5.716   12.211 16.495  1   25.467 ? 115 SER   A O    1 ? 1 
ATOM   1498 C CB   . SER   A 1 103 ? 7.408   14.279 14.806  1   26.878 ? 115 SER   A CB   1 ? 1 
ATOM   1499 O OG   . SER   A 1 103 ? 7.491   15.4   15.674  1   29.208 ? 115 SER   A OG   1 ? 1 
ATOM   1500 H H    . SER   A 1 103 ? 5.382   15.619 14.033  1   25.413 ? 115 SER   A H    1 c 1 
ATOM   1501 H HA   . SER   A 1 103 ? 6.024   12.968 14.118  1   25.695 ? 115 SER   A HA   1 c 1 
ATOM   1502 H HB2  . SER   A 1 103 ? 7.984   13.566 15.142  1   28.154 ? 115 SER   A HB2  1 c 1 
ATOM   1503 H HB3  . SER   A 1 103 ? 7.725   14.531 13.918  1   26.841 ? 115 SER   A HB3  1 c 1 
ATOM   1504 H HG   . SER   A 1 103 ? 8.291   15.664 15.746  0   30     ? 115 SER   A HG   1 c 1 
ATOM   1505 N N    . ALA   A 1 104 ? 4.575   14.158 16.663  1   24.622 ? 116 ALA   A N    1 ? 1 
ATOM   1506 C CA   . ALA   A 1 104 ? 4.031   13.877 17.982  1   26.125 ? 116 ALA   A CA   1 ? 1 
ATOM   1507 C C    . ALA   A 1 104 ? 2.927   12.83  17.893  1   25.558 ? 116 ALA   A C    1 ? 1 
ATOM   1508 O O    . ALA   A 1 104 ? 2.728   12.017 18.796  1   26.648 ? 116 ALA   A O    1 ? 1 
ATOM   1509 C CB   . ALA   A 1 104 ? 3.486   15.151 18.587  1   27.125 ? 116 ALA   A CB   1 ? 1 
ATOM   1510 H H    . ALA   A 1 104 ? 4.345   14.942 16.255  1   24.299 ? 116 ALA   A H    1 c 1 
ATOM   1511 H HA   . ALA   A 1 104 ? 4.762   13.521 18.559  1   27.232 ? 116 ALA   A HA   1 c 1 
ATOM   1512 H HB1  . ALA   A 1 104 ? 4.213   15.777 18.742  1   27.32  ? 116 ALA   A HB1  1 c 1 
ATOM   1513 H HB2  . ALA   A 1 104 ? 2.841   15.552 17.98   1   25.911 ? 116 ALA   A HB2  1 c 1 
ATOM   1514 H HB3  . ALA   A 1 104 ? 3.049   14.95  19.432  1   27.693 ? 116 ALA   A HB3  1 c 1 
ATOM   1515 N N    . GLY   A 1 105 ? 2.255   12.835 16.742  1   24.65  ? 117 GLY   A N    1 ? 1 
ATOM   1516 C CA   . GLY   A 1 105 ? 1.008   12.126 16.533  1   24.686 ? 117 GLY   A CA   1 ? 1 
ATOM   1517 C C    . GLY   A 1 105 ? -0.094  12.632 17.464  1   25.942 ? 117 GLY   A C    1 ? 1 
ATOM   1518 O O    . GLY   A 1 105 ? -0.039  13.751 17.987  1   25.973 ? 117 GLY   A O    1 ? 1 
ATOM   1519 H H    . GLY   A 1 105 ? 2.591   13.317 16.043  1   23.828 ? 117 GLY   A H    1 c 1 
ATOM   1520 H HA2  . GLY   A 1 105 ? 0.726   12.241 15.597  1   23.855 ? 117 GLY   A HA2  1 c 1 
ATOM   1521 H HA3  . GLY   A 1 105 ? 1.156   11.163 16.69   1   25.564 ? 117 GLY   A HA3  1 c 1 
ATOM   1522 N N    . SER   A 1 106 ? -1.109  11.782 17.627  1   26.477 ? 118 SER   A N    1 ? 1 
ATOM   1523 C CA   . SER   A 1 106 ? -2.228  12.052 18.501  1   28.193 ? 118 SER   A CA   1 ? 1 
ATOM   1524 C C    . SER   A 1 106 ? -2.798  10.724 18.997  1   28.918 ? 118 SER   A C    1 ? 1 
ATOM   1525 O O    . SER   A 1 106 ? -3.876  10.289 18.589  1   29.777 ? 118 SER   A O    1 ? 1 
ATOM   1526 C CB   . SER   A 1 106 ? -3.285  12.898 17.796  1   27.2   ? 118 SER   A CB   1 ? 1 
ATOM   1527 O OG   . SER   A 1 106 ? -4.166  13.455 18.766  1   26.5   ? 118 SER   A OG   1 ? 1 
ATOM   1528 H H    . SER   A 1 106 ? -1.101  10.994 17.163  1   26.682 ? 118 SER   A H    1 c 1 
ATOM   1529 H HA   . SER   A 1 106 ? -1.895  12.557 19.286  1   28.494 ? 118 SER   A HA   1 c 1 
ATOM   1530 H HB2  . SER   A 1 106 ? -2.851  13.615 17.297  1   25.818 ? 118 SER   A HB2  1 c 1 
ATOM   1531 H HB3  . SER   A 1 106 ? -3.789  12.344 17.171  1   26.46  ? 118 SER   A HB3  1 c 1 
ATOM   1532 H HG   . SER   A 1 106 ? -4.706  13.923 18.379  0   30     ? 118 SER   A HG   1 c 1 
ATOM   1533 N N    . LEU   A 1 107 ? -2.083  10.106 19.928  1   30.225 ? 119 LEU   A N    1 ? 1 
ATOM   1534 C CA   . LEU   A 1 107 ? -2.464  8.797  20.446  1   32.081 ? 119 LEU   A CA   1 ? 1 
ATOM   1535 C C    . LEU   A 1 107 ? -3.732  8.869  21.3    1   34.301 ? 119 LEU   A C    1 ? 1 
ATOM   1536 O O    . LEU   A 1 107 ? -3.995  9.886  21.95   1   33.83  ? 119 LEU   A O    1 ? 1 
ATOM   1537 C CB   . LEU   A 1 107 ? -1.313  8.207  21.257  1   33.463 ? 119 LEU   A CB   1 ? 1 
ATOM   1538 C CG   . LEU   A 1 107 ? -0.085  7.766  20.454  1   32.8   ? 119 LEU   A CG   1 ? 1 
ATOM   1539 C CD1  . LEU   A 1 107 ? 0.943   7.175  21.41   1   34.918 ? 119 LEU   A CD1  1 ? 1 
ATOM   1540 C CD2  . LEU   A 1 107 ? -0.46   6.752  19.397  1   32.624 ? 119 LEU   A CD2  1 ? 1 
ATOM   1541 H H    . LEU   A 1 107 ? -1.33   10.508 20.255  1   30.283 ? 119 LEU   A H    1 c 1 
ATOM   1542 H HA   . LEU   A 1 107 ? -2.645  8.211  19.671  1   31.864 ? 119 LEU   A HA   1 c 1 
ATOM   1543 H HB2  . LEU   A 1 107 ? -1.026  8.879  21.917  1   33.72  ? 119 LEU   A HB2  1 c 1 
ATOM   1544 H HB3  . LEU   A 1 107 ? -1.652  7.43   21.757  1   35.199 ? 119 LEU   A HB3  1 c 1 
ATOM   1545 H HG   . LEU   A 1 107 ? 0.309   8.562  20.012  1   31.398 ? 119 LEU   A HG   1 c 1 
ATOM   1546 H HD11 . LEU   A 1 107 ? 1.172   7.832  22.089  1   35.124 ? 119 LEU   A HD11 1 c 1 
ATOM   1547 H HD12 . LEU   A 1 107 ? 1.743   6.929  20.915  1   34.68  ? 119 LEU   A HD12 1 c 1 
ATOM   1548 H HD13 . LEU   A 1 107 ? 0.573   6.385  21.838  1   36.475 ? 119 LEU   A HD13 1 c 1 
ATOM   1549 H HD21 . LEU   A 1 107 ? -0.856  7.208  18.635  1   31.194 ? 119 LEU   A HD21 1 c 1 
ATOM   1550 H HD22 . LEU   A 1 107 ? -1.1    6.12   19.764  1   33.975 ? 119 LEU   A HD22 1 c 1 
ATOM   1551 H HD23 . LEU   A 1 107 ? 0.336   6.275  19.108  1   33.043 ? 119 LEU   A HD23 1 c 1 
ATOM   1552 N N    . PRO   A 1 108 ? -4.515  7.767  21.398  1   34.802 ? 120 PRO   A N    1 ? 1 
ATOM   1553 C CA   . PRO   A 1 108 ? -4.188  6.494  20.761  1   35.744 ? 120 PRO   A CA   1 ? 1 
ATOM   1554 C C    . PRO   A 1 108 ? -4.607  6.34   19.297  1   35.44  ? 120 PRO   A C    1 ? 1 
ATOM   1555 O O    . PRO   A 1 108 ? -4.29   5.321  18.698  1   35.445 ? 120 PRO   A O    1 ? 1 
ATOM   1556 C CB   . PRO   A 1 108 ? -4.995  5.466  21.535  1   38.702 ? 120 PRO   A CB   1 ? 1 
ATOM   1557 C CG   . PRO   A 1 108 ? -6.169  6.265  22.068  1   39.698 ? 120 PRO   A CG   1 ? 1 
ATOM   1558 C CD   . PRO   A 1 108 ? -5.759  7.711  22.172  1   37.753 ? 120 PRO   A CD   1 ? 1 
ATOM   1559 H HA   . PRO   A 1 108 ? -3.234  6.304  20.856  1   35.989 ? 120 PRO   A HA   1 c 1 
ATOM   1560 H HB2  . PRO   A 1 108 ? -5.299  4.742  20.953  1   39.272 ? 120 PRO   A HB2  1 c 1 
ATOM   1561 H HB3  . PRO   A 1 108 ? -4.469  5.088  22.266  1   40.264 ? 120 PRO   A HB3  1 c 1 
ATOM   1562 H HG2  . PRO   A 1 108 ? -6.936  6.178  21.468  1   39.208 ? 120 PRO   A HG2  1 c 1 
ATOM   1563 H HG3  . PRO   A 1 108 ? -6.433  5.929  22.949  1   41.477 ? 120 PRO   A HG3  1 c 1 
ATOM   1564 H HD2  . PRO   A 1 108 ? -6.435  8.3    21.784  1   36.595 ? 120 PRO   A HD2  1 c 1 
ATOM   1565 H HD3  . PRO   A 1 108 ? -5.601  7.969  23.101  1   38.507 ? 120 PRO   A HD3  1 c 1 
ATOM   1566 N N    . LYS   A 1 109 ? -5.339  7.306  18.729  1   35.953 ? 121 LYS   A N    1 ? 1 
ATOM   1567 C CA   . LYS   A 1 109 ? -5.883  7.113  17.386  1   36.546 ? 121 LYS   A CA   1 ? 1 
ATOM   1568 C C    . LYS   A 1 109 ? -4.798  7.244  16.321  1   34.978 ? 121 LYS   A C    1 ? 1 
ATOM   1569 O O    . LYS   A 1 109 ? -4.797  6.485  15.355  1   34.098 ? 121 LYS   A O    1 ? 1 
ATOM   1570 C CB   . LYS   A 1 109 ? -7.061  8.045  17.069  1   39.453 ? 121 LYS   A CB   1 ? 1 
ATOM   1571 C CG   . LYS   A 1 109 ? -8.388  7.679  17.777  1   43.452 ? 121 LYS   A CG   1 ? 1 
ATOM   1572 C CD   . LYS   A 1 109 ? -9.521  8.702  17.673  1   44.292 ? 121 LYS   A CD   1 ? 1 
ATOM   1573 C CE   . LYS   A 1 109 ? -10.823 8.227  18.283  1   49.891 ? 121 LYS   A CE   1 ? 1 
ATOM   1574 N NZ   . LYS   A 1 109 ? -11.316 7.036  17.582  1   52.004 ? 121 LYS   A NZ   1 ? 1 
ATOM   1575 H H    . LYS   A 1 109 ? -5.503  8.089  19.171  1   35.42  ? 121 LYS   A H    1 c 1 
ATOM   1576 H HA   . LYS   A 1 109 ? -6.237  6.188  17.338  1   38.152 ? 121 LYS   A HA   1 c 1 
ATOM   1577 H HB2  . LYS   A 1 109 ? -6.816  8.96   17.321  1   38.164 ? 121 LYS   A HB2  1 c 1 
ATOM   1578 H HB3  . LYS   A 1 109 ? -7.217  8.036  16.1    1   38.034 ? 121 LYS   A HB3  1 c 1 
ATOM   1579 H HG2  . LYS   A 1 109 ? -8.703  6.826  17.407  1   44.202 ? 121 LYS   A HG2  1 c 1 
ATOM   1580 H HG3  . LYS   A 1 109 ? -8.193  7.527  18.728  1   44.453 ? 121 LYS   A HG3  1 c 1 
ATOM   1581 H HD2  . LYS   A 1 109 ? -9.242  9.53   18.123  1   44.185 ? 121 LYS   A HD2  1 c 1 
ATOM   1582 H HD3  . LYS   A 1 109 ? -9.671  8.914  16.726  1   43.588 ? 121 LYS   A HD3  1 c 1 
ATOM   1583 H HE2  . LYS   A 1 109 ? -10.686 8.012  19.223  1   50.65  ? 121 LYS   A HE2  1 c 1 
ATOM   1584 H HE3  . LYS   A 1 109 ? -11.491 8.933  18.223  1   49.208 ? 121 LYS   A HE3  1 c 1 
ATOM   1585 H HZ1  . LYS   A 1 109 ? -10.925 6.294  17.925  1   52.602 ? 121 LYS   A HZ1  1 c 1 
ATOM   1586 H HZ2  . LYS   A 1 109 ? -11.126 7.09   16.697  1   50.369 ? 121 LYS   A HZ2  1 c 1 
ATOM   1587 H HZ3  . LYS   A 1 109 ? -12.213 6.972  17.687  1   52.81  ? 121 LYS   A HZ3  1 c 1 
ATOM   1588 N N    . ILE   A 1 110 ? -3.918  8.252  16.431  1   31.655 ? 122 ILE   A N    1 ? 1 
ATOM   1589 C CA   . ILE   A 1 110 ? -2.96   8.52   15.368  1   30.729 ? 122 ILE   A CA   1 ? 1 
ATOM   1590 C C    . ILE   A 1 110 ? -1.542  8.38   15.9    1   28.552 ? 122 ILE   A C    1 ? 1 
ATOM   1591 O O    . ILE   A 1 110 ? -1.181  9.122  16.801  1   27.91  ? 122 ILE   A O    1 ? 1 
ATOM   1592 C CB   . ILE   A 1 110 ? -3.098  9.931  14.76   1   31.413 ? 122 ILE   A CB   1 ? 1 
ATOM   1593 C CG1  . ILE   A 1 110 ? -4.551  10.394 14.631  1   35.439 ? 122 ILE   A CG1  1 ? 1 
ATOM   1594 C CG2  . ILE   A 1 110 ? -2.307  9.989  13.447  1   30.874 ? 122 ILE   A CG2  1 ? 1 
ATOM   1595 C CD1  . ILE   A 1 110 ? -5.387  9.492  13.753  1   39.673 ? 122 ILE   A CD1  1 ? 1 
ATOM   1596 H H    . ILE   A 1 110 ? -3.918  8.781  17.176  1   32.454 ? 122 ILE   A H    1 c 1 
ATOM   1597 H HA   . ILE   A 1 110 ? -3.094  7.867  14.657  1   30.591 ? 122 ILE   A HA   1 c 1 
ATOM   1598 H HB   . ILE   A 1 110 ? -2.664  10.551 15.379  1   31.644 ? 122 ILE   A HB   1 c 1 
ATOM   1599 H HG12 . ILE   A 1 110 ? -4.953  10.432 15.523  1   36.092 ? 122 ILE   A HG12 1 c 1 
ATOM   1600 H HG13 . ILE   A 1 110 ? -4.563  11.298 14.258  1   34.166 ? 122 ILE   A HG13 1 c 1 
ATOM   1601 H HG21 . ILE   A 1 110 ? -2.507  10.819 12.983  1   29.651 ? 122 ILE   A HG21 1 c 1 
ATOM   1602 H HG22 . ILE   A 1 110 ? -2.555  9.237  12.883  1   30.892 ? 122 ILE   A HG22 1 c 1 
ATOM   1603 H HG23 . ILE   A 1 110 ? -1.355  9.949  13.636  1   30.672 ? 122 ILE   A HG23 1 c 1 
ATOM   1604 H HD11 . ILE   A 1 110 ? -4.96   9.38   12.883  1   37.57  ? 122 ILE   A HD11 1 c 1 
ATOM   1605 H HD12 . ILE   A 1 110 ? -6.26   9.907  13.634  1   38.035 ? 122 ILE   A HD12 1 c 1 
ATOM   1606 H HD13 . ILE   A 1 110 ? -5.494  8.622  14.176  1   39.354 ? 122 ILE   A HD13 1 c 1 
ATOM   1607 N N    . PRO   A 1 111 ? -0.692  7.516  15.318  1   27.941 ? 123 PRO   A N    1 ? 1 
ATOM   1608 C CA   . PRO   A 1 111 ? 0.694   7.423  15.76   1   28.326 ? 123 PRO   A CA   1 ? 1 
ATOM   1609 C C    . PRO   A 1 111 ? 1.576   8.509  15.162  1   26.44  ? 123 PRO   A C    1 ? 1 
ATOM   1610 O O    . PRO   A 1 111 ? 1.106   9.306  14.356  1   24.754 ? 123 PRO   A O    1 ? 1 
ATOM   1611 C CB   . PRO   A 1 111 ? 1.056   5.994  15.399  1   29.824 ? 123 PRO   A CB   1 ? 1 
ATOM   1612 C CG   . PRO   A 1 111 ? 0.278   5.822  14.084  1   29.22  ? 123 PRO   A CG   1 ? 1 
ATOM   1613 C CD   . PRO   A 1 111 ? -1.035  6.514  14.295  1   28.297 ? 123 PRO   A CD   1 ? 1 
ATOM   1614 H HA   . PRO   A 1 111 ? 0.72    7.504  16.737  1   29.166 ? 123 PRO   A HA   1 c 1 
ATOM   1615 H HB2  . PRO   A 1 111 ? 2.018   5.894  15.261  1   30.196 ? 123 PRO   A HB2  1 c 1 
ATOM   1616 H HB3  . PRO   A 1 111 ? 0.747   5.365  16.081  1   31.393 ? 123 PRO   A HB3  1 c 1 
ATOM   1617 H HG2  . PRO   A 1 111 ? 0.763   6.23   13.339  1   28.049 ? 123 PRO   A HG2  1 c 1 
ATOM   1618 H HG3  . PRO   A 1 111 ? 0.137   4.875  13.886  1   30.298 ? 123 PRO   A HG3  1 c 1 
ATOM   1619 H HD2  . PRO   A 1 111 ? -1.349  6.944  13.476  1   27.163 ? 123 PRO   A HD2  1 c 1 
ATOM   1620 H HD3  . PRO   A 1 111 ? -1.718  5.897  14.624  1   29.46  ? 123 PRO   A HD3  1 c 1 
ATOM   1621 N N    . SER   A 1 112 ? 2.848   8.53   15.594  1   26.632 ? 124 SER   A N    1 ? 1 
ATOM   1622 C CA   . SER   A 1 112 ? 3.845   9.448  15.09   1   24.671 ? 124 SER   A CA   1 ? 1 
ATOM   1623 C C    . SER   A 1 112 ? 4.004   9.231  13.577  1   25.053 ? 124 SER   A C    1 ? 1 
ATOM   1624 O O    . SER   A 1 112 ? 3.949   8.099  13.104  1   25.257 ? 124 SER   A O    1 ? 1 
ATOM   1625 C CB   . SER   A 1 112 ? 5.141   9.238  15.813  1   26.532 ? 124 SER   A CB   1 ? 1 
ATOM   1626 O OG   . SER   A 1 112 ? 6.226   9.967  15.249  1   25.251 ? 124 SER   A OG   1 ? 1 
ATOM   1627 H H    . SER   A 1 112 ? 3.096   7.935  16.242  1   27.811 ? 124 SER   A H    1 c 1 
ATOM   1628 H HA   . SER   A 1 112 ? 3.533   10.375 15.251  1   24.428 ? 124 SER   A HA   1 c 1 
ATOM   1629 H HB2  . SER   A 1 112 ? 5.029   9.506  16.743  1   26.837 ? 124 SER   A HB2  1 c 1 
ATOM   1630 H HB3  . SER   A 1 112 ? 5.359   8.287  15.803  1   27.284 ? 124 SER   A HB3  1 c 1 
ATOM   1631 H HG   . SER   A 1 112 ? 6.923   9.784  15.705  0   30     ? 124 SER   A HG   1 c 1 
ATOM   1632 N N    . ASN   A 1 113 ? 4.119   10.334 12.847  1   23.561 ? 125 ASN   A N    1 ? 1 
ATOM   1633 C CA   . ASN   A 1 113 ? 4.566   10.314 11.461  1   25.624 ? 125 ASN   A CA   1 ? 1 
ATOM   1634 C C    . ASN   A 1 113 ? 3.591   9.532  10.571  1   26.655 ? 125 ASN   A C    1 ? 1 
ATOM   1635 O O    . ASN   A 1 113 ? 4.009   8.889  9.596   1   27.235 ? 125 ASN   A O    1 ? 1 
ATOM   1636 C CB   . ASN   A 1 113 ? 5.993   9.783  11.345  1   27.386 ? 125 ASN   A CB   1 ? 1 
ATOM   1637 C CG   . ASN   A 1 113 ? 6.958   10.737 11.995  1   28.569 ? 125 ASN   A CG   1 ? 1 
ATOM   1638 O OD1  . ASN   A 1 113 ? 6.709   11.948 12.061  1   28.898 ? 125 ASN   A OD1  1 ? 1 
ATOM   1639 N ND2  . ASN   A 1 113 ? 8.095   10.227 12.417  1   32.679 ? 125 ASN   A ND2  1 ? 1 
ATOM   1640 H H    . ASN   A 1 113 ? 3.908   11.139 13.224  1   23.717 ? 125 ASN   A H    1 c 1 
ATOM   1641 H HA   . ASN   A 1 113 ? 4.576   11.243 11.139  1   24.622 ? 125 ASN   A HA   1 c 1 
ATOM   1642 H HB2  . ASN   A 1 113 ? 6.056   8.908  11.776  1   28.466 ? 125 ASN   A HB2  1 c 1 
ATOM   1643 H HB3  . ASN   A 1 113 ? 6.228   9.679  10.401  1   27.245 ? 125 ASN   A HB3  1 c 1 
ATOM   1644 H HD21 . ASN   A 1 113 ? 8.604   10.688 12.98   1   32.313 ? 125 ASN   A HD21 1 c 1 
ATOM   1645 H HD22 . ASN   A 1 113 ? 8.354   9.425  12.139  1   32.513 ? 125 ASN   A HD22 1 c 1 
ATOM   1646 N N    . ALA   A 1 114 ? 2.293   9.682  10.851  1   24.786 ? 126 ALA   A N    1 ? 1 
ATOM   1647 C CA   . ALA   A 1 114 ? 1.255   8.964  10.143  1   26.054 ? 126 ALA   A CA   1 ? 1 
ATOM   1648 C C    . ALA   A 1 114 ? 0.821   9.727  8.889   1   23.942 ? 126 ALA   A C    1 ? 1 
ATOM   1649 O O    . ALA   A 1 114 ? 0.539   10.925 8.949   1   24.348 ? 126 ALA   A O    1 ? 1 
ATOM   1650 C CB   . ALA   A 1 114 ? 0.073   8.739  11.038  1   27.018 ? 126 ALA   A CB   1 ? 1 
ATOM   1651 H H    . ALA   A 1 114 ? 2.046   10.267 11.509  1   25.171 ? 126 ALA   A H    1 c 1 
ATOM   1652 H HA   . ALA   A 1 114 ? 1.621   8.08   9.863   1   26.576 ? 126 ALA   A HA   1 c 1 
ATOM   1653 H HB1  . ALA   A 1 114 ? 0.347   8.229  11.819  1   27.863 ? 126 ALA   A HB1  1 c 1 
ATOM   1654 H HB2  . ALA   A 1 114 ? -0.289  9.594  11.324  1   26.201 ? 126 ALA   A HB2  1 c 1 
ATOM   1655 H HB3  . ALA   A 1 114 ? -0.612  8.245  10.557  1   27.051 ? 126 ALA   A HB3  1 c 1 
ATOM   1656 N N    . THR   A 1 115 ? 0.681   8.969  7.797   1   23.793 ? 127 THR   A N    1 ? 1 
ATOM   1657 C CA   . THR   A 1 115 ? -0.062  9.38   6.607   1   23.038 ? 127 THR   A CA   1 ? 1 
ATOM   1658 C C    . THR   A 1 115 ? -1.536  9      6.749   1   22.94  ? 127 THR   A C    1 ? 1 
ATOM   1659 O O    . THR   A 1 115 ? -1.872  7.869  7.11    1   25.293 ? 127 THR   A O    1 ? 1 
ATOM   1660 C CB   . THR   A 1 115 ? 0.563   8.711  5.392   1   23.185 ? 127 THR   A CB   1 ? 1 
ATOM   1661 O OG1  . THR   A 1 115 ? 1.866   9.276  5.362   1   24.061 ? 127 THR   A OG1  1 ? 1 
ATOM   1662 C CG2  . THR   A 1 115 ? -0.069  9.136  4.079   1   24.669 ? 127 THR   A CG2  1 ? 1 
ATOM   1663 H H    . THR   A 1 115 ? 1.074   8.144  7.791   1   24.807 ? 127 THR   A H    1 c 1 
ATOM   1664 H HA   . THR   A 1 115 ? 0.015   10.352 6.509   1   22.138 ? 127 THR   A HA   1 c 1 
ATOM   1665 H HB   . THR   A 1 115 ? 0.612   7.731  5.49    1   24.902 ? 127 THR   A HB   1 c 1 
ATOM   1666 H HG1  . THR   A 1 115 ? 1.758   10.148 5.257   0   30     ? 127 THR   A HG1  1 c 1 
ATOM   1667 H HG21 . THR   A 1 115 ? 0.42    8.737  3.34    1   24.536 ? 127 THR   A HG21 1 c 1 
ATOM   1668 H HG22 . THR   A 1 115 ? -0.038  10.104 4.001   1   23.256 ? 127 THR   A HG22 1 c 1 
ATOM   1669 H HG23 . THR   A 1 115 ? -0.994  8.839  4.05    1   24.214 ? 127 THR   A HG23 1 c 1 
ATOM   1670 N N    . LEU   A 1 116 ? -2.412  9.955  6.434   1   22.274 ? 128 LEU   A N    1 ? 1 
ATOM   1671 C CA   . LEU   A 1 116 ? -3.851  9.763  6.535   1   24.127 ? 128 LEU   A CA   1 ? 1 
ATOM   1672 C C    . LEU   A 1 116 ? -4.509  9.801  5.162   1   24.054 ? 128 LEU   A C    1 ? 1 
ATOM   1673 O O    . LEU   A 1 116 ? -4.153  10.639 4.349   1   23.452 ? 128 LEU   A O    1 ? 1 
ATOM   1674 C CB   . LEU   A 1 116 ? -4.463  10.857 7.407   1   25.272 ? 128 LEU   A CB   1 ? 1 
ATOM   1675 C CG   . LEU   A 1 116 ? -3.896  10.996 8.825   1   25.255 ? 128 LEU   A CG   1 ? 1 
ATOM   1676 C CD1  . LEU   A 1 116 ? -4.753  11.978 9.603   1   25.892 ? 128 LEU   A CD1  1 ? 1 
ATOM   1677 C CD2  . LEU   A 1 116 ? -3.852  9.659  9.47    1   26.926 ? 128 LEU   A CD2  1 ? 1 
ATOM   1678 H H    . LEU   A 1 116 ? -2.101  10.764 6.142   1   21.868 ? 128 LEU   A H    1 c 1 
ATOM   1679 H HA   . LEU   A 1 116 ? -4.026  8.879  6.947   1   25.042 ? 128 LEU   A HA   1 c 1 
ATOM   1680 H HB2  . LEU   A 1 116 ? -4.348  11.718 6.942   1   24.129 ? 128 LEU   A HB2  1 c 1 
ATOM   1681 H HB3  . LEU   A 1 116 ? -5.431  10.687 7.476   1   25.286 ? 128 LEU   A HB3  1 c 1 
ATOM   1682 H HG   . LEU   A 1 116 ? -2.973  11.354 8.765   1   25.063 ? 128 LEU   A HG   1 c 1 
ATOM   1683 H HD11 . LEU   A 1 116 ? -4.766  12.833 9.142   1   25.061 ? 128 LEU   A HD11 1 c 1 
ATOM   1684 H HD12 . LEU   A 1 116 ? -4.384  12.096 10.494  1   25.912 ? 128 LEU   A HD12 1 c 1 
ATOM   1685 H HD13 . LEU   A 1 116 ? -5.66   11.634 9.672   1   26.239 ? 128 LEU   A HD13 1 c 1 
ATOM   1686 H HD21 . LEU   A 1 116 ? -3.072  9.171  9.157   1   26.914 ? 128 LEU   A HD21 1 c 1 
ATOM   1687 H HD22 . LEU   A 1 116 ? -4.656  9.161  9.244   1   27.367 ? 128 LEU   A HD22 1 c 1 
ATOM   1688 H HD23 . LEU   A 1 116 ? -3.8    9.765  10.435  1   27.158 ? 128 LEU   A HD23 1 c 1 
ATOM   1689 N N    . PHE   A 1 117 ? -5.573  9.004  5.029   1   25.99  ? 129 PHE   A N    1 ? 1 
ATOM   1690 C CA   . PHE   A 1 117 ? -6.492  9.043  3.904   1   25.645 ? 129 PHE   A CA   1 ? 1 
ATOM   1691 C C    . PHE   A 1 117 ? -7.898  9.42   4.361   1   25.929 ? 129 PHE   A C    1 ? 1 
ATOM   1692 O O    . PHE   A 1 117 ? -8.394  8.915  5.381   1   27.216 ? 129 PHE   A O    1 ? 1 
ATOM   1693 C CB   . PHE   A 1 117 ? -6.522  7.659  3.258   1   26.894 ? 129 PHE   A CB   1 ? 1 
ATOM   1694 C CG   . PHE   A 1 117 ? -7.573  7.528  2.167   1   27.853 ? 129 PHE   A CG   1 ? 1 
ATOM   1695 C CD1  . PHE   A 1 117 ? -8.865  7.114  2.462   1   29.792 ? 129 PHE   A CD1  1 ? 1 
ATOM   1696 C CD2  . PHE   A 1 117 ? -7.282  7.869  0.862   1   27.768 ? 129 PHE   A CD2  1 ? 1 
ATOM   1697 C CE1  . PHE   A 1 117 ? -9.833  7.032  1.467   1   31.884 ? 129 PHE   A CE1  1 ? 1 
ATOM   1698 C CE2  . PHE   A 1 117 ? -8.242  7.78   -0.125  1   29.575 ? 129 PHE   A CE2  1 ? 1 
ATOM   1699 C CZ   . PHE   A 1 117 ? -9.513  7.365  0.175   1   29.911 ? 129 PHE   A CZ   1 ? 1 
ATOM   1700 H H    . PHE   A 1 117 ? -5.736  8.392  5.688   1   26.366 ? 129 PHE   A H    1 c 1 
ATOM   1701 H HA   . PHE   A 1 117 ? -6.169  9.705  3.241   1   24.975 ? 129 PHE   A HA   1 c 1 
ATOM   1702 H HB2  . PHE   A 1 117 ? -5.636  7.473  2.874   1   26.844 ? 129 PHE   A HB2  1 c 1 
ATOM   1703 H HB3  . PHE   A 1 117 ? -6.7    6.99   3.956   1   27.84  ? 129 PHE   A HB3  1 c 1 
ATOM   1704 H HD1  . PHE   A 1 117 ? -9.09   6.891  3.352   1   30.267 ? 129 PHE   A HD1  1 c 1 
ATOM   1705 H HD2  . PHE   A 1 117 ? -6.412  8.162  0.642   1   27.258 ? 129 PHE   A HD2  1 c 1 
ATOM   1706 H HE1  . PHE   A 1 117 ? -10.705 6.738  1.678   1   32.241 ? 129 PHE   A HE1  1 c 1 
ATOM   1707 H HE2  . PHE   A 1 117 ? -8.021  8.008  -1.014  1   29.076 ? 129 PHE   A HE2  1 c 1 
ATOM   1708 H HZ   . PHE   A 1 117 ? -10.164 7.299  -0.506  1   31.248 ? 129 PHE   A HZ   1 c 1 
ATOM   1709 N N    . PHE   A 1 118 ? -8.537  10.292 3.575   1   23.754 ? 130 PHE   A N    1 ? 1 
ATOM   1710 C CA   . PHE   A 1 118 ? -9.93   10.648 3.78    1   25.401 ? 130 PHE   A CA   1 ? 1 
ATOM   1711 C C    . PHE   A 1 118 ? -10.707 10.592 2.472   1   26.594 ? 130 PHE   A C    1 ? 1 
ATOM   1712 O O    . PHE   A 1 118 ? -10.19  10.927 1.407   1   27.497 ? 130 PHE   A O    1 ? 1 
ATOM   1713 C CB   . PHE   A 1 118 ? -10.126 12.054 4.345   1   24.026 ? 130 PHE   A CB   1 ? 1 
ATOM   1714 C CG   . PHE   A 1 118 ? -9.603  12.254 5.762   1   24.252 ? 130 PHE   A CG   1 ? 1 
ATOM   1715 C CD1  . PHE   A 1 118 ? -8.273  12.616 5.969   1   23.644 ? 130 PHE   A CD1  1 ? 1 
ATOM   1716 C CD2  . PHE   A 1 118 ? -10.436 12.099 6.865   1   26.739 ? 130 PHE   A CD2  1 ? 1 
ATOM   1717 C CE1  . PHE   A 1 118 ? -7.786  12.837 7.241   1   24.833 ? 130 PHE   A CE1  1 ? 1 
ATOM   1718 C CE2  . PHE   A 1 118 ? -9.933  12.292 8.158   1   26.901 ? 130 PHE   A CE2  1 ? 1 
ATOM   1719 C CZ   . PHE   A 1 118 ? -8.606  12.656 8.336   1   24.954 ? 130 PHE   A CZ   1 ? 1 
ATOM   1720 H H    . PHE   A 1 118 ? -8.086  10.681 2.881   1   23.859 ? 130 PHE   A H    1 c 1 
ATOM   1721 H HA   . PHE   A 1 118 ? -10.328 9.998  4.413   1   26.084 ? 130 PHE   A HA   1 c 1 
ATOM   1722 H HB2  . PHE   A 1 118 ? -9.676  12.693 3.75    1   23.615 ? 130 PHE   A HB2  1 c 1 
ATOM   1723 H HB3  . PHE   A 1 118 ? -11.087 12.262 4.333   1   24.997 ? 130 PHE   A HB3  1 c 1 
ATOM   1724 H HD1  . PHE   A 1 118 ? -7.707  12.74  5.225   1   23.386 ? 130 PHE   A HD1  1 c 1 
ATOM   1725 H HD2  . PHE   A 1 118 ? -11.338 11.846 6.741   1   27.333 ? 130 PHE   A HD2  1 c 1 
ATOM   1726 H HE1  . PHE   A 1 118 ? -6.88   13.072 7.364   1   23.761 ? 130 PHE   A HE1  1 c 1 
ATOM   1727 H HE2  . PHE   A 1 118 ? -10.499 12.182 8.906   1   27.44  ? 130 PHE   A HE2  1 c 1 
ATOM   1728 H HZ   . PHE   A 1 118 ? -8.267  12.795 9.206   1   25.392 ? 130 PHE   A HZ   1 c 1 
ATOM   1729 N N    . GLU   A 1 119 ? -11.952 10.148 2.594   1   27.144 ? 131 GLU   A N    1 ? 1 
ATOM   1730 C CA   . GLU   A 1 119 ? -13.009 10.5   1.665   1   28.103 ? 131 GLU   A CA   1 ? 1 
ATOM   1731 C C    . GLU   A 1 119 ? -13.937 11.469 2.396   1   29.572 ? 131 GLU   A C    1 ? 1 
ATOM   1732 O O    . GLU   A 1 119 ? -14.387 11.202 3.529   1   30.062 ? 131 GLU   A O    1 ? 1 
ATOM   1733 C CB   . GLU   A 1 119 ? -13.737 9.263  1.166   1   30.752 ? 131 GLU   A CB   1 ? 1 
ATOM   1734 C CG   . GLU   A 1 119 ? -14.9   9.539  0.216   1   31.518 ? 131 GLU   A CG   1 ? 1 
ATOM   1735 C CD   . GLU   A 1 119 ? -15.607 8.29   -0.276  1   33.385 ? 131 GLU   A CD   1 ? 1 
ATOM   1736 O OE1  . GLU   A 1 119 ? -15.07  7.604  -1.132  1   34.485 ? 131 GLU   A OE1  1 ? 1 
ATOM   1737 O OE2  . GLU   A 1 119 ? -16.724 8.012  0.178   1   35.505 ? 131 GLU   A OE2  1 ? 1 
ATOM   1738 H H    . GLU   A 1 119 ? -12.155 9.591  3.29    1   28.019 ? 131 GLU   A H    1 c 1 
ATOM   1739 H HA   . GLU   A 1 119 ? -12.604 10.963 0.891   1   27.817 ? 131 GLU   A HA   1 c 1 
ATOM   1740 H HB2  . GLU   A 1 119 ? -13.092 8.685  0.707   1   30.394 ? 131 GLU   A HB2  1 c 1 
ATOM   1741 H HB3  . GLU   A 1 119 ? -14.079 8.769  1.94    1   31.223 ? 131 GLU   A HB3  1 c 1 
ATOM   1742 H HG2  . GLU   A 1 119 ? -15.557 10.107 0.67    1   31.795 ? 131 GLU   A HG2  1 c 1 
ATOM   1743 H HG3  . GLU   A 1 119 ? -14.568 10.035 -0.562  1   30.931 ? 131 GLU   A HG3  1 c 1 
ATOM   1744 N N    . ILE   A 1 120 ? -14.187 12.592 1.73    1   28.159 ? 132 ILE   A N    1 ? 1 
ATOM   1745 C CA   . ILE   A 1 120 ? -14.956 13.698 2.266   1   27.773 ? 132 ILE   A CA   1 ? 1 
ATOM   1746 C C    . ILE   A 1 120 ? -16.048 14.041 1.264   1   29.782 ? 132 ILE   A C    1 ? 1 
ATOM   1747 O O    . ILE   A 1 120 ? -15.747 14.251 0.088   1   27.987 ? 132 ILE   A O    1 ? 1 
ATOM   1748 C CB   . ILE   A 1 120 ? -14.064 14.928 2.501   1   27.141 ? 132 ILE   A CB   1 ? 1 
ATOM   1749 C CG1  . ILE   A 1 120 ? -12.863 14.616 3.409   1   26.456 ? 132 ILE   A CG1  1 ? 1 
ATOM   1750 C CG2  . ILE   A 1 120 ? -14.892 16.085 3.052   1   29.742 ? 132 ILE   A CG2  1 ? 1 
ATOM   1751 C CD1  . ILE   A 1 120 ? -11.844 15.74  3.518   1   25.249 ? 132 ILE   A CD1  1 ? 1 
ATOM   1752 H H    . ILE   A 1 120 ? -13.858 12.674 0.881   1   27.964 ? 132 ILE   A H    1 c 1 
ATOM   1753 H HA   . ILE   A 1 120 ? -15.361 13.431 3.112   1   28.775 ? 132 ILE   A HA   1 c 1 
ATOM   1754 H HB   . ILE   A 1 120 ? -13.71  15.205 1.632   1   27.08  ? 132 ILE   A HB   1 c 1 
ATOM   1755 H HG12 . ILE   A 1 120 ? -13.195 14.408 4.306   1   26.731 ? 132 ILE   A HG12 1 c 1 
ATOM   1756 H HG13 . ILE   A 1 120 ? -12.409 13.819 3.067   1   26.072 ? 132 ILE   A HG13 1 c 1 
ATOM   1757 H HG21 . ILE   A 1 120 ? -14.313 16.841 3.241   1   28.515 ? 132 ILE   A HG21 1 c 1 
ATOM   1758 H HG22 . ILE   A 1 120 ? -15.335 15.806 3.871   1   29.763 ? 132 ILE   A HG22 1 c 1 
ATOM   1759 H HG23 . ILE   A 1 120 ? -15.561 16.35  2.399   1   30.058 ? 132 ILE   A HG23 1 c 1 
ATOM   1760 H HD11 . ILE   A 1 120 ? -11.659 16.1   2.63    1   25.125 ? 132 ILE   A HD11 1 c 1 
ATOM   1761 H HD12 . ILE   A 1 120 ? -11.018 15.394 3.906   1   24.553 ? 132 ILE   A HD12 1 c 1 
ATOM   1762 H HD13 . ILE   A 1 120 ? -12.196 16.45  4.088   1   25.597 ? 132 ILE   A HD13 1 c 1 
ATOM   1763 N N    . GLU   A 1 121 ? -17.285 14.172 1.777   1   32.189 ? 133 GLU   A N    1 ? 1 
ATOM   1764 C CA   . GLU   A 1 121 ? -18.364 14.757 0.997   1   34.461 ? 133 GLU   A CA   1 ? 1 
ATOM   1765 C C    . GLU   A 1 121 ? -18.71  16.114 1.594   1   34.53  ? 133 GLU   A C    1 ? 1 
ATOM   1766 O O    . GLU   A 1 121 ? -19.004 16.216 2.793   1   37.98  ? 133 GLU   A O    1 ? 1 
ATOM   1767 C CB   . GLU   A 1 121 ? -19.598 13.859 0.925   1   37.244 ? 133 GLU   A CB   1 ? 1 
ATOM   1768 C CG   . GLU   A 1 121 ? -20.778 14.528 0.221   1   39.309 ? 133 GLU   A CG   1 ? 1 
ATOM   1769 C CD   . GLU   A 1 121 ? -21.982 13.645 0.001   1   42.101 ? 133 GLU   A CD   1 ? 1 
ATOM   1770 O OE1  . GLU   A 1 121 ? -21.86  12.452 0.317   1   42.352 ? 133 GLU   A OE1  1 ? 1 
ATOM   1771 O OE2  . GLU   A 1 121 ? -23.024 14.141 -0.485  1   45.519 ? 133 GLU   A OE2  1 ? 1 
ATOM   1772 H H    . GLU   A 1 121 ? -17.457 13.888 2.628   1   32.402 ? 133 GLU   A H    1 c 1 
ATOM   1773 H HA   . GLU   A 1 121 ? -18.039 14.895 0.074   1   33.994 ? 133 GLU   A HA   1 c 1 
ATOM   1774 H HB2  . GLU   A 1 121 ? -19.36  13.032 0.459   1   37.154 ? 133 GLU   A HB2  1 c 1 
ATOM   1775 H HB3  . GLU   A 1 121 ? -19.867 13.62  1.837   1   37.561 ? 133 GLU   A HB3  1 c 1 
ATOM   1776 H HG2  . GLU   A 1 121 ? -21.061 15.305 0.746   1   39.614 ? 133 GLU   A HG2  1 c 1 
ATOM   1777 H HG3  . GLU   A 1 121 ? -20.477 14.861 -0.652  1   38.971 ? 133 GLU   A HG3  1 c 1 
ATOM   1778 N N    . LEU   A 1 122 ? -18.643 17.153 0.767   1   33.826 ? 134 LEU   A N    1 ? 1 
ATOM   1779 C CA   . LEU   A 1 122 ? -19.086 18.469 1.198   1   34.794 ? 134 LEU   A CA   1 ? 1 
ATOM   1780 C C    . LEU   A 1 122 ? -20.606 18.581 1.067   1   38.217 ? 134 LEU   A C    1 ? 1 
ATOM   1781 O O    . LEU   A 1 122 ? -21.138 18.672 -0.041  1   38.81  ? 134 LEU   A O    1 ? 1 
ATOM   1782 C CB   . LEU   A 1 122 ? -18.361 19.55  0.395   1   33.855 ? 134 LEU   A CB   1 ? 1 
ATOM   1783 C CG   . LEU   A 1 122 ? -18.62  20.994 0.837   1   34.401 ? 134 LEU   A CG   1 ? 1 
ATOM   1784 C CD1  . LEU   A 1 122 ? -18.453 21.147 2.367   1   33.485 ? 134 LEU   A CD1  1 ? 1 
ATOM   1785 C CD2  . LEU   A 1 122 ? -17.675 21.915 0.081   1   33.811 ? 134 LEU   A CD2  1 ? 1 
ATOM   1786 H H    . LEU   A 1 122 ? -18.316 17.047 -0.08   1   33.719 ? 134 LEU   A H    1 c 1 
ATOM   1787 H HA   . LEU   A 1 122 ? -18.847 18.571 2.154   1   34.423 ? 134 LEU   A HA   1 c 1 
ATOM   1788 H HB2  . LEU   A 1 122 ? -17.393 19.376 0.451   1   32.32  ? 134 LEU   A HB2  1 c 1 
ATOM   1789 H HB3  . LEU   A 1 122 ? -18.627 19.461 -0.549  1   34.455 ? 134 LEU   A HB3  1 c 1 
ATOM   1790 H HG   . LEU   A 1 122 ? -19.552 21.235 0.597   1   36.075 ? 134 LEU   A HG   1 c 1 
ATOM   1791 H HD11 . LEU   A 1 122 ? -19.25  20.819 2.816   1   34.687 ? 134 LEU   A HD11 1 c 1 
ATOM   1792 H HD12 . LEU   A 1 122 ? -18.322 22.085 2.586   1   34.135 ? 134 LEU   A HD12 1 c 1 
ATOM   1793 H HD13 . LEU   A 1 122 ? -17.681 20.635 2.662   1   32.171 ? 134 LEU   A HD13 1 c 1 
ATOM   1794 H HD21 . LEU   A 1 122 ? -17.686 21.688 -0.863  1   33.977 ? 134 LEU   A HD21 1 c 1 
ATOM   1795 H HD22 . LEU   A 1 122 ? -16.773 21.81  0.427   1   32.389 ? 134 LEU   A HD22 1 c 1 
ATOM   1796 H HD23 . LEU   A 1 122 ? -17.96  22.837 0.194   1   34.949 ? 134 LEU   A HD23 1 c 1 
ATOM   1797 N N    . LEU   A 1 123 ? -21.288 18.63  2.221   1   40.418 ? 135 LEU   A N    1 ? 1 
ATOM   1798 C CA   . LEU   A 1 123 ? -22.743 18.614 2.266   1   45.579 ? 135 LEU   A CA   1 ? 1 
ATOM   1799 C C    . LEU   A 1 123 ? -23.284 20.031 2.104   1   49.538 ? 135 LEU   A C    1 ? 1 
ATOM   1800 O O    . LEU   A 1 123 ? -24.276 20.229 1.395   1   52.813 ? 135 LEU   A O    1 ? 1 
ATOM   1801 C CB   . LEU   A 1 123 ? -23.255 18.026 3.577   1   46.463 ? 135 LEU   A CB   1 ? 1 
ATOM   1802 C CG   . LEU   A 1 123 ? -22.754 16.624 3.916   1   46.058 ? 135 LEU   A CG   1 ? 1 
ATOM   1803 C CD1  . LEU   A 1 123 ? -23.183 16.24  5.331   1   47.234 ? 135 LEU   A CD1  1 ? 1 
ATOM   1804 C CD2  . LEU   A 1 123 ? -23.246 15.613 2.888   1   48.538 ? 135 LEU   A CD2  1 ? 1 
ATOM   1805 H H    . LEU   A 1 123 ? -20.828 18.677 3.01    1   39.833 ? 135 LEU   A H    1 c 1 
ATOM   1806 H HA   . LEU   A 1 123 ? -23.074 18.062 1.512   1   46.035 ? 135 LEU   A HA   1 c 1 
ATOM   1807 H HB2  . LEU   A 1 123 ? -22.996 18.635 4.307   1   46.29  ? 135 LEU   A HB2  1 c 1 
ATOM   1808 H HB3  . LEU   A 1 123 ? -24.239 18.004 3.54    1   48.628 ? 135 LEU   A HB3  1 c 1 
ATOM   1809 H HG   . LEU   A 1 123 ? -21.763 16.633 3.888   1   44.254 ? 135 LEU   A HG   1 c 1 
ATOM   1810 H HD11 . LEU   A 1 123 ? -23.104 17.012 5.916   1   47.171 ? 135 LEU   A HD11 1 c 1 
ATOM   1811 H HD12 . LEU   A 1 123 ? -22.611 15.526 5.661   1   46.194 ? 135 LEU   A HD12 1 c 1 
ATOM   1812 H HD13 . LEU   A 1 123 ? -24.106 15.935 5.32    1   49.124 ? 135 LEU   A HD13 1 c 1 
ATOM   1813 H HD21 . LEU   A 1 123 ? -22.872 15.825 2.017   1   47.283 ? 135 LEU   A HD21 1 c 1 
ATOM   1814 H HD22 . LEU   A 1 123 ? -24.216 15.645 2.839   1   50.065 ? 135 LEU   A HD22 1 c 1 
ATOM   1815 H HD23 . LEU   A 1 123 ? -22.966 14.72  3.151   1   47.687 ? 135 LEU   A HD23 1 c 1 
ATOM   1816 N N    . ASP   A 1 124 ? -22.662 20.996 2.8     1   47.87  ? 136 ASP   A N    1 ? 1 
ATOM   1817 C CA   . ASP   A 1 124 ? -23.159 22.36  2.82    1   52.074 ? 136 ASP   A CA   1 ? 1 
ATOM   1818 C C    . ASP   A 1 124 ? -22.132 23.28  3.481   1   52.662 ? 136 ASP   A C    1 ? 1 
ATOM   1819 O O    . ASP   A 1 124 ? -21.228 22.81  4.169   1   48.766 ? 136 ASP   A O    1 ? 1 
ATOM   1820 C CB   . ASP   A 1 124 ? -24.493 22.417 3.554   1   55.418 ? 136 ASP   A CB   1 ? 1 
ATOM   1821 C CG   . ASP   A 1 124 ? -25.409 23.563 3.178   1   57.704 ? 136 ASP   A CG   1 ? 1 
ATOM   1822 O OD1  . ASP   A 1 124 ? -25.07  24.278 2.211   1   58.578 ? 136 ASP   A OD1  1 ? 1 
ATOM   1823 O OD2  . ASP   A 1 124 ? -26.442 23.722 3.863   1   59.716 ? 136 ASP   A OD2  1 ? 1 
ATOM   1824 H H    . ASP   A 1 124 ? -21.911 20.794 3.28    1   46.984 ? 136 ASP   A H    1 c 1 
ATOM   1825 H HA   . ASP   A 1 124 ? -23.292 22.652 1.89    1   52.601 ? 136 ASP   A HA   1 c 1 
ATOM   1826 H HB2  . ASP   A 1 124 ? -24.987 21.584 3.408   1   55.556 ? 136 ASP   A HB2  1 c 1 
ATOM   1827 H HB3  . ASP   A 1 124 ? -24.314 22.484 4.516   1   54.902 ? 136 ASP   A HB3  1 c 1 
ATOM   1828 N N    . PHE   A 1 125 ? -22.295 24.597 3.282   1   55.589 ? 137 PHE   A N    1 ? 1 
ATOM   1829 C CA   . PHE   A 1 125 ? -21.533 25.602 4.01    1   55.492 ? 137 PHE   A CA   1 ? 1 
ATOM   1830 C C    . PHE   A 1 125 ? -22.27  26.94  3.996   1   59.279 ? 137 PHE   A C    1 ? 1 
ATOM   1831 O O    . PHE   A 1 125 ? -22.884 27.307 2.993   1   63.213 ? 137 PHE   A O    1 ? 1 
ATOM   1832 C CB   . PHE   A 1 125 ? -20.125 25.769 3.433   1   52.769 ? 137 PHE   A CB   1 ? 1 
ATOM   1833 C CG   . PHE   A 1 125 ? -20.068 26.136 1.956   1   53.76  ? 137 PHE   A CG   1 ? 1 
ATOM   1834 C CD1  . PHE   A 1 125 ? -20.052 25.146 0.976   1   51.679 ? 137 PHE   A CD1  1 ? 1 
ATOM   1835 C CD2  . PHE   A 1 125 ? -20.01  27.463 1.556   1   57.058 ? 137 PHE   A CD2  1 ? 1 
ATOM   1836 C CE1  . PHE   A 1 125 ? -19.983 25.48  -0.366  1   51.883 ? 137 PHE   A CE1  1 ? 1 
ATOM   1837 C CE2  . PHE   A 1 125 ? -19.955 27.791 0.208   1   58.829 ? 137 PHE   A CE2  1 ? 1 
ATOM   1838 C CZ   . PHE   A 1 125 ? -19.945 26.796 -0.751  1   56.278 ? 137 PHE   A CZ   1 ? 1 
ATOM   1839 H H    . PHE   A 1 125 ? -22.905 24.876 2.661   1   56.731 ? 137 PHE   A H    1 c 1 
ATOM   1840 H HA   . PHE   A 1 125 ? -21.45  25.299 4.949   1   55.029 ? 137 PHE   A HA   1 c 1 
ATOM   1841 H HB2  . PHE   A 1 125 ? -19.661 26.466 3.948   1   53.136 ? 137 PHE   A HB2  1 c 1 
ATOM   1842 H HB3  . PHE   A 1 125 ? -19.634 24.928 3.567   1   51.165 ? 137 PHE   A HB3  1 c 1 
ATOM   1843 H HD1  . PHE   A 1 125 ? -20.081 24.238 1.232   1   50.841 ? 137 PHE   A HD1  1 c 1 
ATOM   1844 H HD2  . PHE   A 1 125 ? -20.022 28.147 2.206   1   57.886 ? 137 PHE   A HD2  1 c 1 
ATOM   1845 H HE1  . PHE   A 1 125 ? -19.981 24.799 -1.02   1   52.027 ? 137 PHE   A HE1  1 c 1 
ATOM   1846 H HE2  . PHE   A 1 125 ? -19.922 28.698 -0.054  1   59.653 ? 137 PHE   A HE2  1 c 1 
ATOM   1847 H HZ   . PHE   A 1 125 ? -19.901 27.021 -1.667  1   56.531 ? 137 PHE   A HZ   1 c 1 
ATOM   1848 N N    . LYS   A 1 126 ? -22.196 27.654 5.126   1   60.531 ? 138 LYS   A N    1 ? 1 
ATOM   1849 C CA   . LYS   A 1 126 ? -22.88  28.926 5.329   1   60.822 ? 138 LYS   A CA   1 ? 1 
ATOM   1850 C C    . LYS   A 1 126 ? -21.855 29.952 5.82    1   60.762 ? 138 LYS   A C    1 ? 1 
ATOM   1851 O O    . LYS   A 1 126 ? -20.955 29.618 6.596   1   55.369 ? 138 LYS   A O    1 ? 1 
ATOM   1852 C CB   . LYS   A 1 126 ? -24.054 28.746 6.3     1   62.392 ? 138 LYS   A CB   1 ? 1 
ATOM   1853 H H    . LYS   A 1 126 ? -21.686 27.33  5.811   1   58.417 ? 138 LYS   A H    1 c 1 
ATOM   1854 H HA   . LYS   A 1 126 ? -23.238 29.231 4.457   1   62.404 ? 138 LYS   A HA   1 c 1 
ATOM   1855 H HB2  . LYS   A 1 126 ? -23.677 28.52  7.248   0   30     ? 138 LYS   A HB2  1 c 1 
ATOM   1856 H HB3  . LYS   A 1 126 ? -24.874 28.847 5.864   0   30     ? 138 LYS   A HB3  1 c 1 
ATOM   1857 N N    . GLY   A 1 127 ? -21.976 31.195 5.33    1   63.946 ? 139 GLY   A N    1 ? 1 
ATOM   1858 C CA   . GLY   A 1 127 ? -21.054 32.263 5.689   1   65.874 ? 139 GLY   A CA   1 ? 1 
ATOM   1859 C C    . GLY   A 1 127 ? -21.17  32.603 7.172   1   69.157 ? 139 GLY   A C    1 ? 1 
ATOM   1860 O O    . GLY   A 1 127 ? -22.243 32.435 7.748   1   71.644 ? 139 GLY   A O    1 ? 1 
ATOM   1861 H H    . GLY   A 1 127 ? -22.659 31.382 4.753   1   65.635 ? 139 GLY   A H    1 c 1 
ATOM   1862 H HA2  . GLY   A 1 127 ? -20.135 31.979 5.484   1   63.767 ? 139 GLY   A HA2  1 c 1 
ATOM   1863 H HA3  . GLY   A 1 127 ? -21.256 33.062 5.148   1   67.979 ? 139 GLY   A HA3  1 c 1 
ATOM   1864 N N    . GLU   A 1 128 ? -20.063 33.06  7.777   1   69.887 ? 140 GLU   A N    1 ? 1 
ATOM   1865 C CA   . GLU   A 1 128 ? -20.049 33.462 9.178   1   71.775 ? 140 GLU   A CA   1 ? 1 
ATOM   1866 C C    . GLU   A 1 128 ? -20.938 34.708 9.351   1   78.49  ? 140 GLU   A C    1 ? 1 
ATOM   1867 O O    . GLU   A 1 128 ? -21.208 35.37  8.316   1   80.906 ? 140 GLU   A O    1 ? 1 
ATOM   1868 C CB   . GLU   A 1 128 ? -18.632 33.713 9.696   1   68.158 ? 140 GLU   A CB   1 ? 1 
ATOM   1869 O OXT  . GLU   A 1 128 ? -21.358 34.961 10.504  1   84.045 ? 140 GLU   A OXT  1 ? 1 
ATOM   1870 H H    . GLU   A 1 128 ? -19.289 33.126 7.294   1   68.324 ? 140 GLU   A H    1 c 1 
ATOM   1871 H HA   . GLU   A 1 128 ? -20.443 32.725 9.711   1   70.929 ? 140 GLU   A HA   1 c 1 
ATOM   1872 H HB2  . GLU   A 1 128 ? -17.94  33.437 9.128   0   30     ? 140 GLU   A HB2  1 c 1 
ATOM   1873 H HB3  . GLU   A 1 128 ? -18.735 34.178 10.633  0   30     ? 140 GLU   A HB3  1 c 1 
ATOM   1874 N N    . GLY   B 1 1   ? 20.065  6.013  38.753  1   57.061 ? 13  GLY   B N    1 ? 2 
ATOM   1875 C CA   . GLY   B 1 1   ? 20.153  7.303  38.046  1   55.285 ? 13  GLY   B CA   1 ? 2 
ATOM   1876 C C    . GLY   B 1 1   ? 18.86   8.102  38.179  1   53.208 ? 13  GLY   B C    1 ? 2 
ATOM   1877 O O    . GLY   B 1 1   ? 17.949  7.719  38.907  1   54.418 ? 13  GLY   B O    1 ? 2 
ATOM   1878 H H1   . GLY   B 1 1   ? 20.825  5.538  38.627  1   58.542 ? 13  GLY   B H1   1 c 2 
ATOM   1879 H H2   . GLY   B 1 1   ? 19.364  5.534  38.44   1   55.554 ? 13  GLY   B H2   1 c 2 
ATOM   1880 H H3   . GLY   B 1 1   ? 19.951  6.154  39.64   1   58.808 ? 13  GLY   B H3   1 c 2 
ATOM   1881 H HA2  . GLY   B 1 1   ? 20.898  7.824  38.418  1   57.214 ? 13  GLY   B HA2  1 c 2 
ATOM   1882 H HA3  . GLY   B 1 1   ? 20.343  7.136  37.092  1   53.812 ? 13  GLY   B HA3  1 c 2 
ATOM   1883 N N    . ALA   B 1 2   ? 18.777  9.197  37.423  1   50.929 ? 14  ALA   B N    1 ? 2 
ATOM   1884 C CA   . ALA   B 1 2   ? 17.619  10.069 37.459  1   50.66  ? 14  ALA   B CA   1 ? 2 
ATOM   1885 C C    . ALA   B 1 2   ? 16.339  9.283  37.172  1   47.694 ? 14  ALA   B C    1 ? 2 
ATOM   1886 O O    . ALA   B 1 2   ? 15.373  9.423  37.92   1   48.904 ? 14  ALA   B O    1 ? 2 
ATOM   1887 C CB   . ALA   B 1 2   ? 17.81   11.224 36.5    1   50.043 ? 14  ALA   B CB   1 ? 2 
ATOM   1888 H H    . ALA   B 1 2   ? 19.469  9.407  36.864  1   51.481 ? 14  ALA   B H    1 c 2 
ATOM   1889 H HA   . ALA   B 1 2   ? 17.548  10.435 38.384  1   51.969 ? 14  ALA   B HA   1 c 2 
ATOM   1890 H HB1  . ALA   B 1 2   ? 18.547  11.78  36.802  1   51.473 ? 14  ALA   B HB1  1 c 2 
ATOM   1891 H HB2  . ALA   B 1 2   ? 18.007  10.889 35.611  1   48.579 ? 14  ALA   B HB2  1 c 2 
ATOM   1892 H HB3  . ALA   B 1 2   ? 16.999  11.758 36.469  1   48.321 ? 14  ALA   B HB3  1 c 2 
ATOM   1893 N N    . PRO   B 1 3   ? 16.253  8.463  36.097  1   46.691 ? 15  PRO   B N    1 ? 2 
ATOM   1894 C CA   . PRO   B 1 3   ? 15.038  7.698  35.826  1   45.292 ? 15  PRO   B CA   1 ? 2 
ATOM   1895 C C    . PRO   B 1 3   ? 14.544  6.856  37.003  1   46.473 ? 15  PRO   B C    1 ? 2 
ATOM   1896 O O    . PRO   B 1 3   ? 13.355  6.851  37.312  1   42.963 ? 15  PRO   B O    1 ? 2 
ATOM   1897 C CB   . PRO   B 1 3   ? 15.389  6.875  34.581  1   45.545 ? 15  PRO   B CB   1 ? 2 
ATOM   1898 C CG   . PRO   B 1 3   ? 16.488  7.683  33.912  1   45.809 ? 15  PRO   B CG   1 ? 2 
ATOM   1899 C CD   . PRO   B 1 3   ? 17.27   8.283  35.045  1   48.292 ? 15  PRO   B CD   1 ? 2 
ATOM   1900 H HA   . PRO   B 1 3   ? 14.328  8.327  35.58   1   43.807 ? 15  PRO   B HA   1 c 2 
ATOM   1901 H HB2  . PRO   B 1 3   ? 15.709  5.986  34.828  1   46.561 ? 15  PRO   B HB2  1 c 2 
ATOM   1902 H HB3  . PRO   B 1 3   ? 14.614  6.784  33.993  1   43.521 ? 15  PRO   B HB3  1 c 2 
ATOM   1903 H HG2  . PRO   B 1 3   ? 17.06   7.109  33.365  1   45.99  ? 15  PRO   B HG2  1 c 2 
ATOM   1904 H HG3  . PRO   B 1 3   ? 16.11   8.385  33.345  1   44.122 ? 15  PRO   B HG3  1 c 2 
ATOM   1905 H HD2  . PRO   B 1 3   ? 17.976  7.68   35.347  1   49.722 ? 15  PRO   B HD2  1 c 2 
ATOM   1906 H HD3  . PRO   B 1 3   ? 17.661  9.135  34.787  1   47.797 ? 15  PRO   B HD3  1 c 2 
ATOM   1907 N N    . ALA   B 1 4   ? 15.449  6.132  37.659  1   49.543 ? 16  ALA   B N    1 ? 2 
ATOM   1908 C CA   . ALA   B 1 4   ? 15.069  5.29   38.779  1   51.912 ? 16  ALA   B CA   1 ? 2 
ATOM   1909 C C    . ALA   B 1 4   ? 14.553  6.145  39.939  1   54.14  ? 16  ALA   B C    1 ? 2 
ATOM   1910 O O    . ALA   B 1 4   ? 13.653  5.725  40.659  1   55.385 ? 16  ALA   B O    1 ? 2 
ATOM   1911 C CB   . ALA   B 1 4   ? 16.24   4.424  39.183  1   54.641 ? 16  ALA   B CB   1 ? 2 
ATOM   1912 H H    . ALA   B 1 4   ? 16.326  6.159  37.401  1   50.107 ? 16  ALA   B H    1 c 2 
ATOM   1913 H HA   . ALA   B 1 4   ? 14.323  4.699  38.48   1   50.989 ? 16  ALA   B HA   1 c 2 
ATOM   1914 H HB1  . ALA   B 1 4   ? 16.53   3.891  38.423  1   53.971 ? 16  ALA   B HB1  1 c 2 
ATOM   1915 H HB2  . ALA   B 1 4   ? 16.975  4.986  39.48   1   55.959 ? 16  ALA   B HB2  1 c 2 
ATOM   1916 H HB3  . ALA   B 1 4   ? 15.975  3.832  39.907  1   56.546 ? 16  ALA   B HB3  1 c 2 
ATOM   1917 N N    . THR   B 1 5   ? 15.106  7.354  40.111  1   54.074 ? 17  THR   B N    1 ? 2 
ATOM   1918 C CA   . THR   B 1 5   ? 14.672  8.235  41.19   1   55.346 ? 17  THR   B CA   1 ? 2 
ATOM   1919 C C    . THR   B 1 5   ? 13.253  8.724  40.898  1   53.714 ? 17  THR   B C    1 ? 2 
ATOM   1920 O O    . THR   B 1 5   ? 12.473  8.96   41.812  1   57.106 ? 17  THR   B O    1 ? 2 
ATOM   1921 C CB   . THR   B 1 5   ? 15.651  9.399  41.379  1   55.957 ? 17  THR   B CB   1 ? 2 
ATOM   1922 O OG1  . THR   B 1 5   ? 16.883  8.799  41.784  1   58.043 ? 17  THR   B OG1  1 ? 2 
ATOM   1923 C CG2  . THR   B 1 5   ? 15.21   10.398 42.439  1   56.556 ? 17  THR   B CG2  1 ? 2 
ATOM   1924 H H    . THR   B 1 5   ? 15.772  7.634  39.552  1   53.584 ? 17  THR   B H    1 c 2 
ATOM   1925 H HA   . THR   B 1 5   ? 14.655  7.712  42.022  1   57.731 ? 17  THR   B HA   1 c 2 
ATOM   1926 H HB   . THR   B 1 5   ? 15.781  9.869  40.521  1   53.719 ? 17  THR   B HB   1 c 2 
ATOM   1927 H HG1  . THR   B 1 5   ? 16.749  8.349  42.583  0   30     ? 17  THR   B HG1  1 c 2 
ATOM   1928 H HG21 . THR   B 1 5   ? 15.964  10.955 42.693  1   58.441 ? 17  THR   B HG21 1 c 2 
ATOM   1929 H HG22 . THR   B 1 5   ? 14.883  9.92   43.22   1   58.568 ? 17  THR   B HG22 1 c 2 
ATOM   1930 H HG23 . THR   B 1 5   ? 14.5    10.959 42.083  1   54.885 ? 17  THR   B HG23 1 c 2 
ATOM   1931 N N    . VAL   B 1 6   ? 12.896  8.883  39.622  1   48.721 ? 18  VAL   B N    1 ? 2 
ATOM   1932 C CA   . VAL   B 1 6   ? 11.541  9.288  39.284  1   45.369 ? 18  VAL   B CA   1 ? 2 
ATOM   1933 C C    . VAL   B 1 6   ? 10.583  8.133  39.556  1   45.985 ? 18  VAL   B C    1 ? 2 
ATOM   1934 O O    . VAL   B 1 6   ? 9.502   8.34   40.099  1   44.56  ? 18  VAL   B O    1 ? 2 
ATOM   1935 C CB   . VAL   B 1 6   ? 11.394  9.774  37.837  1   40.756 ? 18  VAL   B CB   1 ? 2 
ATOM   1936 C CG1  . VAL   B 1 6   ? 9.931   10.097 37.544  1   37.719 ? 18  VAL   B CG1  1 ? 2 
ATOM   1937 C CG2  . VAL   B 1 6   ? 12.317  10.963 37.57   1   40.422 ? 18  VAL   B CG2  1 ? 2 
ATOM   1938 H H    . VAL   B 1 6   ? 13.501  8.744  38.952  1   48.126 ? 18  VAL   B H    1 c 2 
ATOM   1939 H HA   . VAL   B 1 6   ? 11.294  10.026 39.87   1   46.086 ? 18  VAL   B HA   1 c 2 
ATOM   1940 H HB   . VAL   B 1 6   ? 11.67   9.032  37.249  1   40.172 ? 18  VAL   B HB   1 c 2 
ATOM   1941 H HG11 . VAL   B 1 6   ? 9.53    10.524 38.32   1   39.083 ? 18  VAL   B HG11 1 c 2 
ATOM   1942 H HG12 . VAL   B 1 6   ? 9.45    9.277  37.341  1   37.677 ? 18  VAL   B HG12 1 c 2 
ATOM   1943 H HG13 . VAL   B 1 6   ? 9.877   10.698 36.782  1   36.522 ? 18  VAL   B HG13 1 c 2 
ATOM   1944 H HG21 . VAL   B 1 6   ? 12.181  11.281 36.662  1   38.735 ? 18  VAL   B HG21 1 c 2 
ATOM   1945 H HG22 . VAL   B 1 6   ? 13.242  10.69  37.681  1   41.829 ? 18  VAL   B HG22 1 c 2 
ATOM   1946 H HG23 . VAL   B 1 6   ? 12.114  11.678 38.197  1   41.374 ? 18  VAL   B HG23 1 c 2 
ATOM   1947 N N    . THR   B 1 7   ? 10.974  6.919  39.161  1   46.902 ? 19  THR   B N    1 ? 2 
ATOM   1948 C CA   . THR   B 1 7   ? 10.177  5.74   39.461  1   50.611 ? 19  THR   B CA   1 ? 2 
ATOM   1949 C C    . THR   B 1 7   ? 9.865   5.698  40.963  1   54.253 ? 19  THR   B C    1 ? 2 
ATOM   1950 O O    . THR   B 1 7   ? 8.721   5.477  41.354  1   55.837 ? 19  THR   B O    1 ? 2 
ATOM   1951 C CB   . THR   B 1 7   ? 10.933  4.492  39.016  1   52.666 ? 19  THR   B CB   1 ? 2 
ATOM   1952 O OG1  . THR   B 1 7   ? 10.905  4.525  37.594  1   51.718 ? 19  THR   B OG1  1 ? 2 
ATOM   1953 C CG2  . THR   B 1 7   ? 10.324  3.218  39.569  1   55.04  ? 19  THR   B CG2  1 ? 2 
ATOM   1954 H H    . THR   B 1 7   ? 11.75   6.822  38.686  1   47.129 ? 19  THR   B H    1 c 2 
ATOM   1955 H HA   . THR   B 1 7   ? 9.334   5.796  38.961  1   48.731 ? 19  THR   B HA   1 c 2 
ATOM   1956 H HB   . THR   B 1 7   ? 11.87   4.55   39.321  1   54.162 ? 19  THR   B HB   1 c 2 
ATOM   1957 H HG1  . THR   B 1 7   ? 10.169  4.53   37.286  0   30     ? 19  THR   B HG1  1 c 2 
ATOM   1958 H HG21 . THR   B 1 7   ? 10.605  2.462  39.026  1   54.82  ? 19  THR   B HG21 1 c 2 
ATOM   1959 H HG22 . THR   B 1 7   ? 9.354   3.285  39.55   1   54.204 ? 19  THR   B HG22 1 c 2 
ATOM   1960 H HG23 . THR   B 1 7   ? 10.621  3.084  40.485  1   57.349 ? 19  THR   B HG23 1 c 2 
ATOM   1961 N N    . GLU   B 1 8   ? 10.881  5.949  41.797  1   58.117 ? 20  GLU   B N    1 ? 2 
ATOM   1962 C CA   . GLU   B 1 8   ? 10.762  5.76   43.24   1   61.552 ? 20  GLU   B CA   1 ? 2 
ATOM   1963 C C    . GLU   B 1 8   ? 10.022  6.912  43.926  1   60.978 ? 20  GLU   B C    1 ? 2 
ATOM   1964 O O    . GLU   B 1 8   ? 9.257   6.682  44.858  1   63.959 ? 20  GLU   B O    1 ? 2 
ATOM   1965 C CB   . GLU   B 1 8   ? 12.143  5.588  43.882  1   64.556 ? 20  GLU   B CB   1 ? 2 
ATOM   1966 H H    . GLU   B 1 8   ? 11.677  6.244  41.457  1   57.288 ? 20  GLU   B H    1 c 2 
ATOM   1967 H HA   . GLU   B 1 8   ? 10.256  4.927  43.399  1   62.29  ? 20  GLU   B HA   1 c 2 
ATOM   1968 H HB2  . GLU   B 1 8   ? 12.84   5.826  43.286  0   30     ? 20  GLU   B HB2  1 c 2 
ATOM   1969 H HB3  . GLU   B 1 8   ? 11.956  5.483  44.882  0   30     ? 20  GLU   B HB3  1 c 2 
ATOM   1970 N N    . GLN   B 1 9   ? 10.317  8.159  43.542  1   59.072 ? 21  GLN   B N    1 ? 2 
ATOM   1971 C CA   . GLN   B 1 9   ? 9.828   9.325  44.274  1   61.73  ? 21  GLN   B CA   1 ? 2 
ATOM   1972 C C    . GLN   B 1 9   ? 8.815   10.13  43.455  1   56.147 ? 21  GLN   B C    1 ? 2 
ATOM   1973 O O    . GLN   B 1 9   ? 8.228   11.073 43.984  1   56.244 ? 21  GLN   B O    1 ? 2 
ATOM   1974 C CB   . GLN   B 1 9   ? 10.867  10.385 44.66   1   64.402 ? 21  GLN   B CB   1 ? 2 
ATOM   1975 C CG   . GLN   B 1 9   ? 12.194  9.862  45.181  1   69.503 ? 21  GLN   B CG   1 ? 2 
ATOM   1976 C CD   . GLN   B 1 9   ? 12.02   9.095  46.458  1   75.73  ? 21  GLN   B CD   1 ? 2 
ATOM   1977 O OE1  . GLN   B 1 9   ? 11.789  9.672  47.523  1   82.855 ? 21  GLN   B OE1  1 ? 2 
ATOM   1978 N NE2  . GLN   B 1 9   ? 12.124  7.781  46.348  1   80.406 ? 21  GLN   B NE2  1 ? 2 
ATOM   1979 H H    . GLN   B 1 9   ? 10.852  8.29   42.812  1   57.975 ? 21  GLN   B H    1 c 2 
ATOM   1980 H HA   . GLN   B 1 9   ? 9.382   9.013  45.102  1   63.254 ? 21  GLN   B HA   1 c 2 
ATOM   1981 H HB2  . GLN   B 1 9   ? 11.042  10.944 43.875  1   62.211 ? 21  GLN   B HB2  1 c 2 
ATOM   1982 H HB3  . GLN   B 1 9   ? 10.472  10.963 45.346  1   65.808 ? 21  GLN   B HB3  1 c 2 
ATOM   1983 H HG2  . GLN   B 1 9   ? 12.603  9.279  44.506  1   68.347 ? 21  GLN   B HG2  1 c 2 
ATOM   1984 H HG3  . GLN   B 1 9   ? 12.802  10.615 45.339  1   70.348 ? 21  GLN   B HG3  1 c 2 
ATOM   1985 H HE21 . GLN   B 1 9   ? 11.405  7.27   46.438  1   78.944 ? 21  GLN   B HE21 1 c 2 
ATOM   1986 H HE22 . GLN   B 1 9   ? 12.916  7.414  46.19   1   79.676 ? 21  GLN   B HE22 1 c 2 
ATOM   1987 N N    . GLY   B 1 10  ? 8.645   9.791  42.171  1   50.521 ? 22  GLY   B N    1 ? 2 
ATOM   1988 C CA   . GLY   B 1 10  ? 7.9     10.642 41.258  1   46.379 ? 22  GLY   B CA   1 ? 2 
ATOM   1989 C C    . GLY   B 1 10  ? 6.402   10.58  41.536  1   45.783 ? 22  GLY   B C    1 ? 2 
ATOM   1990 O O    . GLY   B 1 10  ? 5.871   9.528  41.849  1   46.782 ? 22  GLY   B O    1 ? 2 
ATOM   1991 H H    . GLY   B 1 10  ? 8.991   9.006  41.857  1   50.756 ? 22  GLY   B H    1 c 2 
ATOM   1992 H HA2  . GLY   B 1 10  ? 8.216   11.569 41.353  1   46.603 ? 22  GLY   B HA2  1 c 2 
ATOM   1993 H HA3  . GLY   B 1 10  ? 8.074   10.355 40.332  1   44.709 ? 22  GLY   B HA3  1 c 2 
ATOM   1994 N N    . GLU   B 1 11  ? 5.745   11.732 41.393  1   45.316 ? 23  GLU   B N    1 ? 2 
ATOM   1995 C CA   . GLU   B 1 11  ? 4.312   11.883 41.592  1   45.338 ? 23  GLU   B CA   1 ? 2 
ATOM   1996 C C    . GLU   B 1 11  ? 3.598   11.467 40.315  1   40.597 ? 23  GLU   B C    1 ? 2 
ATOM   1997 O O    . GLU   B 1 11  ? 4.024   11.836 39.207  1   33.314 ? 23  GLU   B O    1 ? 2 
ATOM   1998 C CB   . GLU   B 1 11  ? 4.158   13.328 42.087  1   51.521 ? 23  GLU   B CB   1 ? 2 
ATOM   1999 C CG   . GLU   B 1 11  ? 2.836   14.023 41.783  1   54.879 ? 23  GLU   B CG   1 ? 2 
ATOM   2000 C CD   . GLU   B 1 11  ? 2.662   15.342 42.527  1   60.575 ? 23  GLU   B CD   1 ? 2 
ATOM   2001 O OE1  . GLU   B 1 11  ? 3.372   15.578 43.529  1   67.376 ? 23  GLU   B OE1  1 ? 2 
ATOM   2002 O OE2  . GLU   B 1 11  ? 1.805   16.153 42.095  1   67.475 ? 23  GLU   B OE2  1 ? 2 
ATOM   2003 H H    . GLU   B 1 11  ? 6.224   12.468 41.14   1   44.723 ? 23  GLU   B H    1 c 2 
ATOM   2004 H HA   . GLU   B 1 11  ? 4.034   11.274 42.323  1   47.604 ? 23  GLU   B HA   1 c 2 
ATOM   2005 H HB2  . GLU   B 1 11  ? 4.287   13.332 43.059  1   53.44  ? 23  GLU   B HB2  1 c 2 
ATOM   2006 H HB3  . GLU   B 1 11  ? 4.87    13.874 41.695  1   50.243 ? 23  GLU   B HB3  1 c 2 
ATOM   2007 H HG2  . GLU   B 1 11  ? 2.78    14.198 40.82   1   52.425 ? 23  GLU   B HG2  1 c 2 
ATOM   2008 H HG3  . GLU   B 1 11  ? 2.096   13.427 42.023  1   55.254 ? 23  GLU   B HG3  1 c 2 
ATOM   2009 N N    . ASP   B 1 12  ? 2.525   10.676 40.459  1   40.104 ? 24  ASP   B N    1 ? 2 
ATOM   2010 C CA   . ASP   B 1 12  ? 1.711   10.296 39.304  1   37.026 ? 24  ASP   B CA   1 ? 2 
ATOM   2011 C C    . ASP   B 1 12  ? 0.752   11.436 38.963  1   35.122 ? 24  ASP   B C    1 ? 2 
ATOM   2012 O O    . ASP   B 1 12  ? -0.147  11.75  39.749  1   36.41  ? 24  ASP   B O    1 ? 2 
ATOM   2013 C CB   . ASP   B 1 12  ? 0.948   9.01   39.575  1   37.878 ? 24  ASP   B CB   1 ? 2 
ATOM   2014 C CG   . ASP   B 1 12  ? 0.102   8.477  38.428  1   35.271 ? 24  ASP   B CG   1 ? 2 
ATOM   2015 O OD1  . ASP   B 1 12  ? 0.091   9.111  37.34   1   32.291 ? 24  ASP   B OD1  1 ? 2 
ATOM   2016 O OD2  . ASP   B 1 12  ? -0.51   7.401  38.621  1   34.915 ? 24  ASP   B OD2  1 ? 2 
ATOM   2017 H H    . ASP   B 1 12  ? 2.293   10.367 41.288  1   42.077 ? 24  ASP   B H    1 c 2 
ATOM   2018 H HA   . ASP   B 1 12  ? 2.306   10.14  38.538  1   35.513 ? 24  ASP   B HA   1 c 2 
ATOM   2019 H HB2  . ASP   B 1 12  ? 1.593   8.315  39.823  1   38.596 ? 24  ASP   B HB2  1 c 2 
ATOM   2020 H HB3  . ASP   B 1 12  ? 0.358   9.156  40.344  1   39.353 ? 24  ASP   B HB3  1 c 2 
ATOM   2021 N N    . ILE   B 1 13  ? 0.992   12.087 37.817  1   33.642 ? 25  ILE   B N    1 ? 2 
ATOM   2022 C CA   . ILE   B 1 13  ? 0.24    13.27  37.432  1   33.364 ? 25  ILE   B CA   1 ? 2 
ATOM   2023 C C    . ILE   B 1 13  ? -0.751  12.922 36.321  1   32.374 ? 25  ILE   B C    1 ? 2 
ATOM   2024 O O    . ILE   B 1 13  ? -1.26   13.826 35.672  1   34.199 ? 25  ILE   B O    1 ? 2 
ATOM   2025 C CB   . ILE   B 1 13  ? 1.179   14.427 37.027  1   34.262 ? 25  ILE   B CB   1 ? 2 
ATOM   2026 C CG1  . ILE   B 1 13  ? 2.093   14.055 35.86   1   33.33  ? 25  ILE   B CG1  1 ? 2 
ATOM   2027 C CG2  . ILE   B 1 13  ? 1.974   14.942 38.231  1   38.339 ? 25  ILE   B CG2  1 ? 2 
ATOM   2028 C CD1  . ILE   B 1 13  ? 2.835   15.232 35.238  1   34.972 ? 25  ILE   B CD1  1 ? 2 
ATOM   2029 H H    . ILE   B 1 13  ? 1.639   11.774 37.253  1   32.649 ? 25  ILE   B H    1 c 2 
ATOM   2030 H HA   . ILE   B 1 13  ? -0.273  13.566 38.208  1   35.021 ? 25  ILE   B HA   1 c 2 
ATOM   2031 H HB   . ILE   B 1 13  ? 0.612   15.163 36.721  1   34.093 ? 25  ILE   B HB   1 c 2 
ATOM   2032 H HG12 . ILE   B 1 13  ? 2.753   13.404 36.176  1   34.087 ? 25  ILE   B HG12 1 c 2 
ATOM   2033 H HG13 . ILE   B 1 13  ? 1.557   13.622 35.165  1   32.769 ? 25  ILE   B HG13 1 c 2 
ATOM   2034 H HG21 . ILE   B 1 13  ? 2.418   15.774 37.997  1   37.352 ? 25  ILE   B HG21 1 c 2 
ATOM   2035 H HG22 . ILE   B 1 13  ? 2.64    14.282 38.487  1   38.181 ? 25  ILE   B HG22 1 c 2 
ATOM   2036 H HG23 . ILE   B 1 13  ? 1.371   15.097 38.978  1   39.004 ? 25  ILE   B HG23 1 c 2 
ATOM   2037 H HD11 . ILE   B 1 13  ? 2.204   15.954 35.054  1   34.033 ? 25  ILE   B HD11 1 c 2 
ATOM   2038 H HD12 . ILE   B 1 13  ? 3.257   14.953 34.404  1   33.089 ? 25  ILE   B HD12 1 c 2 
ATOM   2039 H HD13 . ILE   B 1 13  ? 3.519   15.551 35.856  1   35.13  ? 25  ILE   B HD13 1 c 2 
ATOM   2040 N N    . THR   B 1 14  ? -1.049  11.636 36.098  1   30.645 ? 26  THR   B N    1 ? 2 
ATOM   2041 C CA   . THR   B 1 14  ? -2.075  11.256 35.133  1   29.529 ? 26  THR   B CA   1 ? 2 
ATOM   2042 C C    . THR   B 1 14  ? -3.457  11.374 35.78   1   31.272 ? 26  THR   B C    1 ? 2 
ATOM   2043 O O    . THR   B 1 14  ? -3.599  11.214 36.991  1   33.648 ? 26  THR   B O    1 ? 2 
ATOM   2044 C CB   . THR   B 1 14  ? -1.836  9.858  34.545  1   29.319 ? 26  THR   B CB   1 ? 2 
ATOM   2045 O OG1  . THR   B 1 14  ? -1.97   8.895  35.593  1   30.495 ? 26  THR   B OG1  1 ? 2 
ATOM   2046 C CG2  . THR   B 1 14  ? -0.509  9.748  33.818  1   27.735 ? 26  THR   B CG2  1 ? 2 
ATOM   2047 H H    . THR   B 1 14  ? -0.607  10.979 36.553  1   31.726 ? 26  THR   B H    1 c 2 
ATOM   2048 H HA   . THR   B 1 14  ? -2.034  11.897 34.39   1   28.496 ? 26  THR   B HA   1 c 2 
ATOM   2049 H HB   . THR   B 1 14  ? -2.543  9.687  33.878  1   28.916 ? 26  THR   B HB   1 c 2 
ATOM   2050 H HG1  . THR   B 1 14  ? -1.404  9.056  36.249  0   30     ? 26  THR   B HG1  1 c 2 
ATOM   2051 H HG21 . THR   B 1 14  ? -0.365  8.829  33.539  1   27.87  ? 26  THR   B HG21 1 c 2 
ATOM   2052 H HG22 . THR   B 1 14  ? 0.21    10.022 34.412  1   28.049 ? 26  THR   B HG22 1 c 2 
ATOM   2053 H HG23 . THR   B 1 14  ? -0.519  10.325 33.036  1   26.606 ? 26  THR   B HG23 1 c 2 
ATOM   2054 N N    . SER   B 1 15  ? -4.459  11.684 34.953  1   31.935 ? 27  SER   B N    1 ? 2 
ATOM   2055 C CA   . SER   B 1 15  ? -5.862  11.688 35.375  1   37.025 ? 27  SER   B CA   1 ? 2 
ATOM   2056 C C    . SER   B 1 15  ? -6.316  10.276 35.739  1   37.701 ? 27  SER   B C    1 ? 2 
ATOM   2057 O O    . SER   B 1 15  ? -7.009  10.063 36.743  1   38.554 ? 27  SER   B O    1 ? 2 
ATOM   2058 C CB   . SER   B 1 15  ? -6.749  12.252 34.287  1   37.521 ? 27  SER   B CB   1 ? 2 
ATOM   2059 O OG   . SER   B 1 15  ? -6.366  13.579 33.96   1   37.662 ? 27  SER   B OG   1 ? 2 
ATOM   2060 H H    . SER   B 1 15  ? -4.265  11.902 34.087  1   31.076 ? 27  SER   B H    1 c 2 
ATOM   2061 H HA   . SER   B 1 15  ? -5.945  12.26  36.18   1   37.254 ? 27  SER   B HA   1 c 2 
ATOM   2062 H HB2  . SER   B 1 15  ? -6.684  11.69  33.492  1   36.858 ? 27  SER   B HB2  1 c 2 
ATOM   2063 H HB3  . SER   B 1 15  ? -7.674  12.245 34.59   1   38.951 ? 27  SER   B HB3  1 c 2 
ATOM   2064 H HG   . SER   B 1 15  ? -6.825  13.905 33.366  0   30     ? 27  SER   B HG   1 c 2 
ATOM   2065 N N    . LYS   B 1 16  ? -5.871  9.301  34.94   1   36.7   ? 28  LYS   B N    1 ? 2 
ATOM   2066 C CA   . LYS   B 1 16  ? -6.263  7.915  35.148  1   40.781 ? 28  LYS   B CA   1 ? 2 
ATOM   2067 C C    . LYS   B 1 16  ? -5.519  7.281  36.322  1   40.038 ? 28  LYS   B C    1 ? 2 
ATOM   2068 O O    . LYS   B 1 16  ? -5.901  6.21   36.747  1   44.233 ? 28  LYS   B O    1 ? 2 
ATOM   2069 C CB   . LYS   B 1 16  ? -6.019  7.044  33.914  1   41.983 ? 28  LYS   B CB   1 ? 2 
ATOM   2070 C CG   . LYS   B 1 16  ? -6.907  7.297  32.701  1   44.893 ? 28  LYS   B CG   1 ? 2 
ATOM   2071 C CD   . LYS   B 1 16  ? -6.658  6.218  31.653  1   49.98  ? 28  LYS   B CD   1 ? 2 
ATOM   2072 C CE   . LYS   B 1 16  ? -6.544  6.675  30.228  1   52.01  ? 28  LYS   B CE   1 ? 2 
ATOM   2073 N NZ   . LYS   B 1 16  ? -7.78   7.253  29.698  1   54.622 ? 28  LYS   B NZ   1 ? 2 
ATOM   2074 H H    . LYS   B 1 16  ? -5.315  9.502  34.244  1   35.699 ? 28  LYS   B H    1 c 2 
ATOM   2075 H HA   . LYS   B 1 16  ? -7.233  7.896  35.348  1   41.645 ? 28  LYS   B HA   1 c 2 
ATOM   2076 H HB2  . LYS   B 1 16  ? -5.086  7.163  33.636  1   40.822 ? 28  LYS   B HB2  1 c 2 
ATOM   2077 H HB3  . LYS   B 1 16  ? -6.127  6.104  34.175  1   43.563 ? 28  LYS   B HB3  1 c 2 
ATOM   2078 H HG2  . LYS   B 1 16  ? -7.849  7.279  32.979  1   46.666 ? 28  LYS   B HG2  1 c 2 
ATOM   2079 H HG3  . LYS   B 1 16  ? -6.702  8.18   32.325  1   43.902 ? 28  LYS   B HG3  1 c 2 
ATOM   2080 H HD2  . LYS   B 1 16  ? -5.834  5.74   31.891  1   48.992 ? 28  LYS   B HD2  1 c 2 
ATOM   2081 H HD3  . LYS   B 1 16  ? -7.39   5.566  31.711  1   51.053 ? 28  LYS   B HD3  1 c 2 
ATOM   2082 H HE2  . LYS   B 1 16  ? -5.834  7.339  30.163  1   50.109 ? 28  LYS   B HE2  1 c 2 
ATOM   2083 H HE3  . LYS   B 1 16  ? -6.292  5.915  29.672  1   51.584 ? 28  LYS   B HE3  1 c 2 
ATOM   2084 H HZ1  . LYS   B 1 16  ? -7.925  8.064  30.075  1   53.8   ? 28  LYS   B HZ1  1 c 2 
ATOM   2085 H HZ2  . LYS   B 1 16  ? -8.48   6.708  29.885  1   55.572 ? 28  LYS   B HZ2  1 c 2 
ATOM   2086 H HZ3  . LYS   B 1 16  ? -7.712  7.351  28.8    1   53.384 ? 28  LYS   B HZ3  1 c 2 
ATOM   2087 N N    . LYS   B 1 17  ? -4.459  7.916  36.838  1   39.168 ? 29  LYS   B N    1 ? 2 
ATOM   2088 C CA   . LYS   B 1 17  ? -3.621  7.342  37.888  1   40.225 ? 29  LYS   B CA   1 ? 2 
ATOM   2089 C C    . LYS   B 1 17  ? -3.093  5.958  37.491  1   39.47  ? 29  LYS   B C    1 ? 2 
ATOM   2090 O O    . LYS   B 1 17  ? -3.192  5.003  38.257  1   39.728 ? 29  LYS   B O    1 ? 2 
ATOM   2091 C CB   . LYS   B 1 17  ? -4.371  7.365  39.22   1   44.785 ? 29  LYS   B CB   1 ? 2 
ATOM   2092 C CG   . LYS   B 1 17  ? -4.529  8.767  39.776  1   47.802 ? 29  LYS   B CG   1 ? 2 
ATOM   2093 C CD   . LYS   B 1 17  ? -3.202  9.453  40.116  1   49.516 ? 29  LYS   B CD   1 ? 2 
ATOM   2094 C CE   . LYS   B 1 17  ? -3.377  10.702 40.963  1   55.831 ? 29  LYS   B CE   1 ? 2 
ATOM   2095 N NZ   . LYS   B 1 17  ? -3.453  11.895 40.107  1   54.391 ? 29  LYS   B NZ   1 ? 2 
ATOM   2096 H H    . LYS   B 1 17  ? -4.238  8.742  36.516  1   37.755 ? 29  LYS   B H    1 c 2 
ATOM   2097 H HA   . LYS   B 1 17  ? -2.836  7.933  37.988  1   39.557 ? 29  LYS   B HA   1 c 2 
ATOM   2098 H HB2  . LYS   B 1 17  ? -5.261  6.97   39.102  1   46.018 ? 29  LYS   B HB2  1 c 2 
ATOM   2099 H HB3  . LYS   B 1 17  ? -3.883  6.822  39.875  1   46.412 ? 29  LYS   B HB3  1 c 2 
ATOM   2100 H HG2  . LYS   B 1 17  ? -5.011  9.312  39.117  1   46.353 ? 29  LYS   B HG2  1 c 2 
ATOM   2101 H HG3  . LYS   B 1 17  ? -5.081  8.719  40.587  1   49.751 ? 29  LYS   B HG3  1 c 2 
ATOM   2102 H HD2  . LYS   B 1 17  ? -2.629  8.818  40.597  1   51.069 ? 29  LYS   B HD2  1 c 2 
ATOM   2103 H HD3  . LYS   B 1 17  ? -2.746  9.698  39.281  1   47.904 ? 29  LYS   B HD3  1 c 2 
ATOM   2104 H HE2  . LYS   B 1 17  ? -4.192  10.636 41.493  1   56.358 ? 29  LYS   B HE2  1 c 2 
ATOM   2105 H HE3  . LYS   B 1 17  ? -2.623  10.794 41.572  1   55.487 ? 29  LYS   B HE3  1 c 2 
ATOM   2106 H HZ1  . LYS   B 1 17  ? -4.091  11.779 39.474  1   53.386 ? 29  LYS   B HZ1  1 c 2 
ATOM   2107 H HZ2  . LYS   B 1 17  ? -2.654  12.035 39.704  1   52.768 ? 29  LYS   B HZ2  1 c 2 
ATOM   2108 H HZ3  . LYS   B 1 17  ? -3.663  12.619 40.61   1   54.94  ? 29  LYS   B HZ3  1 c 2 
ATOM   2109 N N    . ASP   B 1 18  ? -2.471  5.883  36.308  1   35.34  ? 30  ASP   B N    1 ? 2 
ATOM   2110 C CA   . ASP   B 1 18  ? -1.901  4.653  35.771  1   36.528 ? 30  ASP   B CA   1 ? 2 
ATOM   2111 C C    . ASP   B 1 18  ? -0.364  4.694  35.765  1   35.246 ? 30  ASP   B C    1 ? 2 
ATOM   2112 O O    . ASP   B 1 18  ? 0.298   3.937  35.047  1   36.276 ? 30  ASP   B O    1 ? 2 
ATOM   2113 C CB   . ASP   B 1 18  ? -2.474  4.429  34.38   1   36.209 ? 30  ASP   B CB   1 ? 2 
ATOM   2114 C CG   . ASP   B 1 18  ? -2.18   5.552  33.398  1   33.401 ? 30  ASP   B CG   1 ? 2 
ATOM   2115 O OD1  . ASP   B 1 18  ? -1.291  6.384  33.71   1   31.013 ? 30  ASP   B OD1  1 ? 2 
ATOM   2116 O OD2  . ASP   B 1 18  ? -2.852  5.598  32.371  1   32.178 ? 30  ASP   B OD2  1 ? 2 
ATOM   2117 H H    . ASP   B 1 18  ? -2.388  6.648  35.814  1   34.51  ? 30  ASP   B H    1 c 2 
ATOM   2118 H HA   . ASP   B 1 18  ? -2.19   3.901  36.337  1   38.368 ? 30  ASP   B HA   1 c 2 
ATOM   2119 H HB2  . ASP   B 1 18  ? -2.116  3.594  34.015  1   36.276 ? 30  ASP   B HB2  1 c 2 
ATOM   2120 H HB3  . ASP   B 1 18  ? -3.447  4.334  34.453  1   36.956 ? 30  ASP   B HB3  1 c 2 
ATOM   2121 N N    . ARG   B 1 19  ? 0.215   5.632  36.516  1   34.955 ? 31  ARG   B N    1 ? 2 
ATOM   2122 C CA   . ARG   B 1 19  ? 1.657   5.865  36.572  1   32.92  ? 31  ARG   B CA   1 ? 2 
ATOM   2123 C C    . ARG   B 1 19  ? 2.277   6.122  35.19   1   30.007 ? 31  ARG   B C    1 ? 2 
ATOM   2124 O O    . ARG   B 1 19  ? 3.473   5.962  35.02   1   29.122 ? 31  ARG   B O    1 ? 2 
ATOM   2125 C CB   . ARG   B 1 19  ? 2.378   4.732  37.316  1   34.341 ? 31  ARG   B CB   1 ? 2 
ATOM   2126 C CG   . ARG   B 1 19  ? 2.05    4.703  38.804  1   37.159 ? 31  ARG   B CG   1 ? 2 
ATOM   2127 C CD   . ARG   B 1 19  ? 2.83    3.614  39.54   1   39.817 ? 31  ARG   B CD   1 ? 2 
ATOM   2128 N NE   . ARG   B 1 19  ? 4.292   3.633  39.387  1   39.985 ? 31  ARG   B NE   1 ? 2 
ATOM   2129 C CZ   . ARG   B 1 19  ? 5.165   4.359  40.083  1   41.938 ? 31  ARG   B CZ   1 ? 2 
ATOM   2130 N NH1  . ARG   B 1 19  ? 4.791   5.259  40.978  1   43.409 ? 31  ARG   B NH1  1 ? 2 
ATOM   2131 N NH2  . ARG   B 1 19  ? 6.456   4.17   39.913  1   43.288 ? 31  ARG   B NH2  1 ? 2 
ATOM   2132 H H    . ARG   B 1 19  ? -0.32   6.159  37.037  1   35.266 ? 31  ARG   B H    1 c 2 
ATOM   2133 H HA   . ARG   B 1 19  ? 1.8     6.684  37.11   1   33.09  ? 31  ARG   B HA   1 c 2 
ATOM   2134 H HB2  . ARG   B 1 19  ? 2.126   3.872  36.917  1   34.887 ? 31  ARG   B HB2  1 c 2 
ATOM   2135 H HB3  . ARG   B 1 19  ? 3.347   4.842  37.208  1   34.091 ? 31  ARG   B HB3  1 c 2 
ATOM   2136 H HG2  . ARG   B 1 19  ? 2.265   5.575  39.201  1   37.017 ? 31  ARG   B HG2  1 c 2 
ATOM   2137 H HG3  . ARG   B 1 19  ? 1.088   4.543  38.921  1   37.835 ? 31  ARG   B HG3  1 c 2 
ATOM   2138 H HD2  . ARG   B 1 19  ? 2.614   3.684  40.492  1   41.927 ? 31  ARG   B HD2  1 c 2 
ATOM   2139 H HD3  . ARG   B 1 19  ? 2.495   2.747  39.232  1   40.44  ? 31  ARG   B HD3  1 c 2 
ATOM   2140 H HE   . ARG   B 1 19  ? 4.626   3.114  38.772  1   39.53  ? 31  ARG   B HE   1 c 2 
ATOM   2141 H HH11 . ARG   B 1 19  ? 4.124   5.811  40.796  1   42.227 ? 31  ARG   B HH11 1 c 2 
ATOM   2142 H HH12 . ARG   B 1 19  ? 5.211   5.305  41.755  1   45.081 ? 31  ARG   B HH12 1 c 2 
ATOM   2143 H HH21 . ARG   B 1 19  ? 6.746   3.479  39.445  1   42.711 ? 31  ARG   B HH21 1 c 2 
ATOM   2144 H HH22 . ARG   B 1 19  ? 7.033   4.739  40.269  1   43.252 ? 31  ARG   B HH22 1 c 2 
ATOM   2145 N N    . GLY   B 1 20  ? 1.493   6.614  34.239  1   29.005 ? 32  GLY   B N    1 ? 2 
ATOM   2146 C CA   . GLY   B 1 20  ? 1.933   6.76   32.862  1   26.351 ? 32  GLY   B CA   1 ? 2 
ATOM   2147 C C    . GLY   B 1 20  ? 2.88    7.938  32.679  1   25.594 ? 32  GLY   B C    1 ? 2 
ATOM   2148 O O    . GLY   B 1 20  ? 3.673   7.95   31.734  1   26.45  ? 32  GLY   B O    1 ? 2 
ATOM   2149 H H    . GLY   B 1 20  ? 0.65    6.889  34.457  1   29.079 ? 32  GLY   B H    1 c 2 
ATOM   2150 H HA2  . GLY   B 1 20  ? 2.385   5.932  32.579  1   26.904 ? 32  GLY   B HA2  1 c 2 
ATOM   2151 H HA3  . GLY   B 1 20  ? 1.144   6.884  32.287  1   26.16  ? 32  GLY   B HA3  1 c 2 
ATOM   2152 N N    . VAL   B 1 21  ? 2.752   8.937  33.57   1   26.737 ? 33  VAL   B N    1 ? 2 
ATOM   2153 C CA   . VAL   B 1 21  ? 3.583   10.128 33.6    1   26.281 ? 33  VAL   B CA   1 ? 2 
ATOM   2154 C C    . VAL   B 1 21  ? 3.91    10.406 35.069  1   28.337 ? 33  VAL   B C    1 ? 2 
ATOM   2155 O O    . VAL   B 1 21  ? 2.995   10.696 35.828  1   27.756 ? 33  VAL   B O    1 ? 2 
ATOM   2156 C CB   . VAL   B 1 21  ? 2.936   11.367 32.961  1   26.436 ? 33  VAL   B CB   1 ? 2 
ATOM   2157 C CG1  . VAL   B 1 21  ? 3.875   12.569 32.936  1   27.815 ? 33  VAL   B CG1  1 ? 2 
ATOM   2158 C CG2  . VAL   B 1 21  ? 2.392   11.096 31.56   1   25.607 ? 33  VAL   B CG2  1 ? 2 
ATOM   2159 H H    . VAL   B 1 21  ? 2.099   8.863  34.204  1   27.519 ? 33  VAL   B H    1 c 2 
ATOM   2160 H HA   . VAL   B 1 21  ? 4.415   9.935  33.126  1   26.068 ? 33  VAL   B HA   1 c 2 
ATOM   2161 H HB   . VAL   B 1 21  ? 2.166   11.611 33.527  1   27.182 ? 33  VAL   B HB   1 c 2 
ATOM   2162 H HG11 . VAL   B 1 21  ? 4.705   12.324 32.493  1   26.971 ? 33  VAL   B HG11 1 c 2 
ATOM   2163 H HG12 . VAL   B 1 21  ? 4.067   12.853 33.846  1   28.35  ? 33  VAL   B HG12 1 c 2 
ATOM   2164 H HG13 . VAL   B 1 21  ? 3.455   13.3   32.452  1   26.745 ? 33  VAL   B HG13 1 c 2 
ATOM   2165 H HG21 . VAL   B 1 21  ? 2.019   11.915 31.193  1   25.043 ? 33  VAL   B HG21 1 c 2 
ATOM   2166 H HG22 . VAL   B 1 21  ? 1.698   10.418 31.606  1   25.849 ? 33  VAL   B HG22 1 c 2 
ATOM   2167 H HG23 . VAL   B 1 21  ? 3.112   10.783 30.987  1   24.989 ? 33  VAL   B HG23 1 c 2 
ATOM   2168 N N    . LEU   B 1 22  ? 5.202   10.302 35.421  1   28.121 ? 34  LEU   B N    1 ? 2 
ATOM   2169 C CA   . LEU   B 1 22  ? 5.695   10.525 36.769  1   30.606 ? 34  LEU   B CA   1 ? 2 
ATOM   2170 C C    . LEU   B 1 22  ? 6.606   11.747 36.752  1   31.49  ? 34  LEU   B C    1 ? 2 
ATOM   2171 O O    . LEU   B 1 22  ? 7.432   11.869 35.84   1   28.982 ? 34  LEU   B O    1 ? 2 
ATOM   2172 C CB   . LEU   B 1 22  ? 6.449   9.274  37.217  1   33.254 ? 34  LEU   B CB   1 ? 2 
ATOM   2173 C CG   . LEU   B 1 22  ? 5.647   7.969  37.25   1   34.344 ? 34  LEU   B CG   1 ? 2 
ATOM   2174 C CD1  . LEU   B 1 22  ? 6.561   6.748  37.418  1   37.363 ? 34  LEU   B CD1  1 ? 2 
ATOM   2175 C CD2  . LEU   B 1 22  ? 4.614   7.995  38.386  1   36.476 ? 34  LEU   B CD2  1 ? 2 
ATOM   2176 H H    . LEU   B 1 22  ? 5.81    10.078 34.776  1   27.733 ? 34  LEU   B H    1 c 2 
ATOM   2177 H HA   . LEU   B 1 22  ? 4.929   10.688 37.371  1   31.664 ? 34  LEU   B HA   1 c 2 
ATOM   2178 H HB2  . LEU   B 1 22  ? 7.217   9.149  36.613  1   32.45  ? 34  LEU   B HB2  1 c 2 
ATOM   2179 H HB3  . LEU   B 1 22  ? 6.808   9.44   38.119  1   34.766 ? 34  LEU   B HB3  1 c 2 
ATOM   2180 H HG   . LEU   B 1 22  ? 5.162   7.878  36.39   1   33.092 ? 34  LEU   B HG   1 c 2 
ATOM   2181 H HD11 . LEU   B 1 22  ? 7.203   6.719  36.689  1   35.835 ? 34  LEU   B HD11 1 c 2 
ATOM   2182 H HD12 . LEU   B 1 22  ? 6.025   5.937  37.408  1   37.365 ? 34  LEU   B HD12 1 c 2 
ATOM   2183 H HD13 . LEU   B 1 22  ? 7.036   6.81   38.264  1   38.552 ? 34  LEU   B HD13 1 c 2 
ATOM   2184 H HD21 . LEU   B 1 22  ? 3.971   8.704  38.224  1   35.55  ? 34  LEU   B HD21 1 c 2 
ATOM   2185 H HD22 . LEU   B 1 22  ? 5.064   8.155  39.233  1   37.988 ? 34  LEU   B HD22 1 c 2 
ATOM   2186 H HD23 . LEU   B 1 22  ? 4.15    7.141  38.424  1   37.035 ? 34  LEU   B HD23 1 c 2 
ATOM   2187 N N    . LYS   B 1 23  ? 6.532   12.56  37.819  1   31.61  ? 35  LYS   B N    1 ? 2 
ATOM   2188 C CA   . LYS   B 1 23  ? 7.174   13.858 37.863  1   32.23  ? 35  LYS   B CA   1 ? 2 
ATOM   2189 C C    . LYS   B 1 23  ? 7.874   14.061 39.198  1   35.962 ? 35  LYS   B C    1 ? 2 
ATOM   2190 O O    . LYS   B 1 23  ? 7.287   13.822 40.265  1   37.698 ? 35  LYS   B O    1 ? 2 
ATOM   2191 C CB   . LYS   B 1 23  ? 6.137   14.973 37.708  1   32.529 ? 35  LYS   B CB   1 ? 2 
ATOM   2192 C CG   . LYS   B 1 23  ? 6.703   16.389 37.745  1   33.603 ? 35  LYS   B CG   1 ? 2 
ATOM   2193 C CD   . LYS   B 1 23  ? 5.739   17.541 37.944  1   33.544 ? 35  LYS   B CD   1 ? 2 
ATOM   2194 C CE   . LYS   B 1 23  ? 6.342   18.851 37.532  1   34.046 ? 35  LYS   B CE   1 ? 2 
ATOM   2195 N NZ   . LYS   B 1 23  ? 5.523   19.99  37.971  1   34.166 ? 35  LYS   B NZ   1 ? 2 
ATOM   2196 H H    . LYS   B 1 23  ? 6.06    12.284 38.552  1   33.216 ? 35  LYS   B H    1 c 2 
ATOM   2197 H HA   . LYS   B 1 23  ? 7.834   13.914 37.132  1   31.647 ? 35  LYS   B HA   1 c 2 
ATOM   2198 H HB2  . LYS   B 1 23  ? 5.669   14.849 36.855  1   30.823 ? 35  LYS   B HB2  1 c 2 
ATOM   2199 H HB3  . LYS   B 1 23  ? 5.474   14.886 38.426  1   33.387 ? 35  LYS   B HB3  1 c 2 
ATOM   2200 H HG2  . LYS   B 1 23  ? 7.371   16.429 38.462  1   35.035 ? 35  LYS   B HG2  1 c 2 
ATOM   2201 H HG3  . LYS   B 1 23  ? 7.186   16.538 36.903  1   32.351 ? 35  LYS   B HG3  1 c 2 
ATOM   2202 H HD2  . LYS   B 1 23  ? 4.928   17.379 37.414  1   32.455 ? 35  LYS   B HD2  1 c 2 
ATOM   2203 H HD3  . LYS   B 1 23  ? 5.483   17.588 38.891  1   35.233 ? 35  LYS   B HD3  1 c 2 
ATOM   2204 H HE2  . LYS   B 1 23  ? 7.232   18.934 37.918  1   34.947 ? 35  LYS   B HE2  1 c 2 
ATOM   2205 H HE3  . LYS   B 1 23  ? 6.428   18.878 36.562  1   32.336 ? 35  LYS   B HE3  1 c 2 
ATOM   2206 H HZ1  . LYS   B 1 23  ? 5.535   20.045 38.875  1   35.995 ? 35  LYS   B HZ1  1 c 2 
ATOM   2207 H HZ2  . LYS   B 1 23  ? 4.668   19.879 37.691  1   33.575 ? 35  LYS   B HZ2  1 c 2 
ATOM   2208 H HZ3  . LYS   B 1 23  ? 5.853   20.757 37.621  1   34.539 ? 35  LYS   B HZ3  1 c 2 
ATOM   2209 N N    . ILE   B 1 24  ? 9.123   14.546 39.13   1   37.384 ? 36  ILE   B N    1 ? 2 
ATOM   2210 C CA   . ILE   B 1 24  ? 9.775   15.151 40.283  1   40.691 ? 36  ILE   B CA   1 ? 2 
ATOM   2211 C C    . ILE   B 1 24  ? 10.131  16.589 39.937  1   41.441 ? 36  ILE   B C    1 ? 2 
ATOM   2212 O O    . ILE   B 1 24  ? 10.763  16.841 38.919  1   41.319 ? 36  ILE   B O    1 ? 2 
ATOM   2213 C CB   . ILE   B 1 24  ? 11.037  14.381 40.684  1   44.029 ? 36  ILE   B CB   1 ? 2 
ATOM   2214 C CG1  . ILE   B 1 24  ? 10.727  12.936 40.978  1   44.824 ? 36  ILE   B CG1  1 ? 2 
ATOM   2215 C CG2  . ILE   B 1 24  ? 11.769  15.056 41.858  1   47.31  ? 36  ILE   B CG2  1 ? 2 
ATOM   2216 C CD1  . ILE   B 1 24  ? 11.908  12.187 41.555  1   48.557 ? 36  ILE   B CD1  1 ? 2 
ATOM   2217 H H    . ILE   B 1 24  ? 9.583   14.495 38.342  1   36.165 ? 36  ILE   B H    1 c 2 
ATOM   2218 H HA   . ILE   B 1 24  ? 9.154   15.15  41.037  1   42.07  ? 36  ILE   B HA   1 c 2 
ATOM   2219 H HB   . ILE   B 1 24  ? 11.641  14.396 39.915  1   42.799 ? 36  ILE   B HB   1 c 2 
ATOM   2220 H HG12 . ILE   B 1 24  ? 9.985   12.895 41.614  1   45.771 ? 36  ILE   B HG12 1 c 2 
ATOM   2221 H HG13 . ILE   B 1 24  ? 10.444  12.495 40.151  1   42.976 ? 36  ILE   B HG13 1 c 2 
ATOM   2222 H HG21 . ILE   B 1 24  ? 12.662  14.683 41.944  1   48.537 ? 36  ILE   B HG21 1 c 2 
ATOM   2223 H HG22 . ILE   B 1 24  ? 11.275  14.902 42.681  1   48.755 ? 36  ILE   B HG22 1 c 2 
ATOM   2224 H HG23 . ILE   B 1 24  ? 11.837  16.01  41.697  1   47.255 ? 36  ILE   B HG23 1 c 2 
ATOM   2225 H HD11 . ILE   B 1 24  ? 12.689  12.315 40.983  1   47.76  ? 36  ILE   B HD11 1 c 2 
ATOM   2226 H HD12 . ILE   B 1 24  ? 11.692  11.239 41.601  1   48.382 ? 36  ILE   B HD12 1 c 2 
ATOM   2227 H HD13 . ILE   B 1 24  ? 12.107  12.514 42.453  1   50.552 ? 36  ILE   B HD13 1 c 2 
ATOM   2228 N N    . VAL   B 1 25  ? 9.79    17.519 40.827  1   42.17  ? 37  VAL   B N    1 ? 2 
ATOM   2229 C CA   . VAL   B 1 25  ? 10.279  18.879 40.714  1   43.824 ? 37  VAL   B CA   1 ? 2 
ATOM   2230 C C    . VAL   B 1 25  ? 11.727  18.877 41.222  1   46.625 ? 37  VAL   B C    1 ? 2 
ATOM   2231 O O    . VAL   B 1 25  ? 11.965  18.508 42.368  1   50.197 ? 37  VAL   B O    1 ? 2 
ATOM   2232 C CB   . VAL   B 1 25  ? 9.38    19.835 41.524  1   46.07  ? 37  VAL   B CB   1 ? 2 
ATOM   2233 C CG1  . VAL   B 1 25  ? 9.969   21.237 41.65   1   48.268 ? 37  VAL   B CG1  1 ? 2 
ATOM   2234 C CG2  . VAL   B 1 25  ? 7.965   19.901 40.969  1   43.407 ? 37  VAL   B CG2  1 ? 2 
ATOM   2235 H H    . VAL   B 1 25  ? 9.238   17.302 41.522  1   43.55  ? 37  VAL   B H    1 c 2 
ATOM   2236 H HA   . VAL   B 1 25  ? 10.265  19.147 39.774  1   42.105 ? 37  VAL   B HA   1 c 2 
ATOM   2237 H HB   . VAL   B 1 25  ? 9.318   19.464 42.435  1   47.647 ? 37  VAL   B HB   1 c 2 
ATOM   2238 H HG11 . VAL   B 1 25  ? 10.303  21.528 40.785  1   46.919 ? 37  VAL   B HG11 1 c 2 
ATOM   2239 H HG12 . VAL   B 1 25  ? 10.699  21.227 42.292  1   50.318 ? 37  VAL   B HG12 1 c 2 
ATOM   2240 H HG13 . VAL   B 1 25  ? 9.282   21.853 41.955  1   48.633 ? 37  VAL   B HG13 1 c 2 
ATOM   2241 H HG21 . VAL   B 1 25  ? 7.443   20.542 41.48   1   44.614 ? 37  VAL   B HG21 1 c 2 
ATOM   2242 H HG22 . VAL   B 1 25  ? 7.549   19.024 41.032  1   42.852 ? 37  VAL   B HG22 1 c 2 
ATOM   2243 H HG23 . VAL   B 1 25  ? 7.994   20.177 40.038  1   41.886 ? 37  VAL   B HG23 1 c 2 
ATOM   2244 N N    . LYS   B 1 26  ? 12.682  19.282 40.375  1   45.422 ? 38  LYS   B N    1 ? 2 
ATOM   2245 C CA   . LYS   B 1 26  ? 14.086  19.327 40.762  1   47.669 ? 38  LYS   B CA   1 ? 2 
ATOM   2246 C C    . LYS   B 1 26  ? 14.493  20.735 41.177  1   50.658 ? 38  LYS   B C    1 ? 2 
ATOM   2247 O O    . LYS   B 1 26  ? 15.3    20.875 42.079  1   55.913 ? 38  LYS   B O    1 ? 2 
ATOM   2248 C CB   . LYS   B 1 26  ? 14.991  18.828 39.631  1   46.525 ? 38  LYS   B CB   1 ? 2 
ATOM   2249 C CG   . LYS   B 1 26  ? 14.686  17.4   39.159  1   45.131 ? 38  LYS   B CG   1 ? 2 
ATOM   2250 C CD   . LYS   B 1 26  ? 14.813  16.355 40.264  1   47.909 ? 38  LYS   B CD   1 ? 2 
ATOM   2251 C CE   . LYS   B 1 26  ? 16.214  16.142 40.658  1   51.536 ? 38  LYS   B CE   1 ? 2 
ATOM   2252 N NZ   . LYS   B 1 26  ? 16.339  15.162 41.726  1   55.247 ? 38  LYS   B NZ   1 ? 2 
ATOM   2253 H H    . LYS   B 1 26  ? 12.451  19.535 39.528  1   43.723 ? 38  LYS   B H    1 c 2 
ATOM   2254 H HA   . LYS   B 1 26  ? 14.213  18.733 41.542  1   49.427 ? 38  LYS   B HA   1 c 2 
ATOM   2255 H HB2  . LYS   B 1 26  ? 14.9    19.434 38.865  1   45.463 ? 38  LYS   B HB2  1 c 2 
ATOM   2256 H HB3  . LYS   B 1 26  ? 15.923  18.867 39.932  1   48.745 ? 38  LYS   B HB3  1 c 2 
ATOM   2257 H HG2  . LYS   B 1 26  ? 13.773  17.376 38.798  1   43.174 ? 38  LYS   B HG2  1 c 2 
ATOM   2258 H HG3  . LYS   B 1 26  ? 15.304  17.172 38.43   1   44.509 ? 38  LYS   B HG3  1 c 2 
ATOM   2259 H HD2  . LYS   B 1 26  ? 14.297  16.639 41.048  1   48.953 ? 38  LYS   B HD2  1 c 2 
ATOM   2260 H HD3  . LYS   B 1 26  ? 14.437  15.506 39.946  1   46.424 ? 38  LYS   B HD3  1 c 2 
ATOM   2261 H HE2  . LYS   B 1 26  ? 16.724  15.836 39.886  1   50.72  ? 38  LYS   B HE2  1 c 2 
ATOM   2262 H HE3  . LYS   B 1 26  ? 16.599  16.982 40.962  1   53.284 ? 38  LYS   B HE3  1 c 2 
ATOM   2263 H HZ1  . LYS   B 1 26  ? 15.962  14.379 41.47   1   53.45  ? 38  LYS   B HZ1  1 c 2 
ATOM   2264 H HZ2  . LYS   B 1 26  ? 15.921  15.465 42.47   1   56.002 ? 38  LYS   B HZ2  1 c 2 
ATOM   2265 H HZ3  . LYS   B 1 26  ? 17.215  15.024 41.912  1   56.642 ? 38  LYS   B HZ3  1 c 2 
ATOM   2266 N N    . ARG   B 1 27  ? 13.939  21.768 40.536  1   51.076 ? 39  ARG   B N    1 ? 2 
ATOM   2267 C CA   . ARG   B 1 27  ? 14.098  23.139 40.999  1   55.636 ? 39  ARG   B CA   1 ? 2 
ATOM   2268 C C    . ARG   B 1 27  ? 12.739  23.837 41.026  1   54.285 ? 39  ARG   B C    1 ? 2 
ATOM   2269 O O    . ARG   B 1 27  ? 12.006  23.796 40.041  1   51.837 ? 39  ARG   B O    1 ? 2 
ATOM   2270 C CB   . ARG   B 1 27  ? 15.055  23.903 40.081  1   57.151 ? 39  ARG   B CB   1 ? 2 
ATOM   2271 C CG   . ARG   B 1 27  ? 15.274  25.338 40.536  1   61.661 ? 39  ARG   B CG   1 ? 2 
ATOM   2272 C CD   . ARG   B 1 27  ? 15.214  26.282 39.361  1   62.281 ? 39  ARG   B CD   1 ? 2 
ATOM   2273 N NE   . ARG   B 1 27  ? 16.473  26.341 38.61   1   65.823 ? 39  ARG   B NE   1 ? 2 
ATOM   2274 C CZ   . ARG   B 1 27  ? 16.639  26.874 37.403  1   64.041 ? 39  ARG   B CZ   1 ? 2 
ATOM   2275 N NH1  . ARG   B 1 27  ? 15.603  27.22  36.649  1   60.263 ? 39  ARG   B NH1  1 ? 2 
ATOM   2276 N NH2  . ARG   B 1 27  ? 17.87   26.998 36.947  1   65.918 ? 39  ARG   B NH2  1 ? 2 
ATOM   2277 H H    . ARG   B 1 27  ? 13.453  21.616 39.778  1   48.722 ? 39  ARG   B H    1 c 2 
ATOM   2278 H HA   . ARG   B 1 27  ? 14.47   23.125 41.917  1   57.868 ? 39  ARG   B HA   1 c 2 
ATOM   2279 H HB2  . ARG   B 1 27  ? 15.92   23.439 40.062  1   58.063 ? 39  ARG   B HB2  1 c 2 
ATOM   2280 H HB3  . ARG   B 1 27  ? 14.693  23.903 39.169  1   54.964 ? 39  ARG   B HB3  1 c 2 
ATOM   2281 H HG2  . ARG   B 1 27  ? 14.588  25.591 41.189  1   62.223 ? 39  ARG   B HG2  1 c 2 
ATOM   2282 H HG3  . ARG   B 1 27  ? 16.153  25.414 40.967  1   64.177 ? 39  ARG   B HG3  1 c 2 
ATOM   2283 H HD2  . ARG   B 1 27  ? 14.496  25.999 38.761  1   59.749 ? 39  ARG   B HD2  1 c 2 
ATOM   2284 H HD3  . ARG   B 1 27  ? 14.994  27.178 39.687  1   64.051 ? 39  ARG   B HD3  1 c 2 
ATOM   2285 H HE   . ARG   B 1 27  ? 17.179  25.996 38.985  1   66.357 ? 39  ARG   B HE   1 c 2 
ATOM   2286 H HH11 . ARG   B 1 27  ? 14.934  27.683 37.001  1   60.859 ? 39  ARG   B HH11 1 c 2 
ATOM   2287 H HH12 . ARG   B 1 27  ? 15.588  26.986 35.794  1   59.072 ? 39  ARG   B HH12 1 c 2 
ATOM   2288 H HH21 . ARG   B 1 27  ? 18.515  27.264 37.491  1   68.439 ? 39  ARG   B HH21 1 c 2 
ATOM   2289 H HH22 . ARG   B 1 27  ? 18.044  26.816 36.1    1   64.659 ? 39  ARG   B HH22 1 c 2 
ATOM   2290 N N    . VAL   B 1 28  ? 12.39   24.451 42.17   1   57.949 ? 40  VAL   B N    1 ? 2 
ATOM   2291 C CA   . VAL   B 1 28  ? 11.08   25.075 42.318  1   58.448 ? 40  VAL   B CA   1 ? 2 
ATOM   2292 C C    . VAL   B 1 28  ? 11.077  26.374 41.508  1   59.696 ? 40  VAL   B C    1 ? 2 
ATOM   2293 O O    . VAL   B 1 28  ? 12.098  27.045 41.425  1   63.712 ? 40  VAL   B O    1 ? 2 
ATOM   2294 C CB   . VAL   B 1 28  ? 10.693  25.314 43.793  1   62.822 ? 40  VAL   B CB   1 ? 2 
ATOM   2295 C CG1  . VAL   B 1 28  ? 9.341   26.008 43.89   1   62.092 ? 40  VAL   B CG1  1 ? 2 
ATOM   2296 C CG2  . VAL   B 1 28  ? 10.68   24.02  44.61   1   61.99  ? 40  VAL   B CG2  1 ? 2 
ATOM   2297 H H    . VAL   B 1 28  ? 12.979  24.484 42.868  1   60.355 ? 40  VAL   B H    1 c 2 
ATOM   2298 H HA   . VAL   B 1 28  ? 10.417  24.473 41.929  1   56.347 ? 40  VAL   B HA   1 c 2 
ATOM   2299 H HB   . VAL   B 1 28  ? 11.373  25.912 44.181  1   64.792 ? 40  VAL   B HB   1 c 2 
ATOM   2300 H HG11 . VAL   B 1 28  ? 8.724   25.607 43.255  1   59.591 ? 40  VAL   B HG11 1 c 2 
ATOM   2301 H HG12 . VAL   B 1 28  ? 9.445   26.953 43.688  1   63.04  ? 40  VAL   B HG12 1 c 2 
ATOM   2302 H HG13 . VAL   B 1 28  ? 8.988   25.908 44.79   1   63.848 ? 40  VAL   B HG13 1 c 2 
ATOM   2303 H HG21 . VAL   B 1 28  ? 10.442  24.219 45.531  1   64.667 ? 40  VAL   B HG21 1 c 2 
ATOM   2304 H HG22 . VAL   B 1 28  ? 11.562  23.611 44.586  1   62.957 ? 40  VAL   B HG22 1 c 2 
ATOM   2305 H HG23 . VAL   B 1 28  ? 10.029  23.405 44.233  1   60.089 ? 40  VAL   B HG23 1 c 2 
ATOM   2306 N N    . GLY   B 1 29  ? 9.945   26.701 40.873  1   57.896 ? 41  GLY   B N    1 ? 2 
ATOM   2307 C CA   . GLY   B 1 29  ? 9.815   27.87  40.007  1   59.043 ? 41  GLY   B CA   1 ? 2 
ATOM   2308 C C    . GLY   B 1 29  ? 9.332   29.113 40.761  1   62.832 ? 41  GLY   B C    1 ? 2 
ATOM   2309 O O    . GLY   B 1 29  ? 9.41    29.162 41.983  1   64.888 ? 41  GLY   B O    1 ? 2 
ATOM   2310 H H    . GLY   B 1 29  ? 9.212   26.167 40.988  1   56.793 ? 41  GLY   B H    1 c 2 
ATOM   2311 H HA2  . GLY   B 1 29  ? 10.688  28.06  39.59   1   59.482 ? 41  GLY   B HA2  1 c 2 
ATOM   2312 H HA3  . GLY   B 1 29  ? 9.177   27.66  39.285  1   56.697 ? 41  GLY   B HA3  1 c 2 
ATOM   2313 N N    . ASN   B 1 30  ? 8.862   30.117 39.994  1   63.64  ? 42  ASN   B N    1 ? 2 
ATOM   2314 C CA   . ASN   B 1 30  ? 8.468   31.431 40.486  1   66.677 ? 42  ASN   B CA   1 ? 2 
ATOM   2315 C C    . ASN   B 1 30  ? 6.981   31.673 40.225  1   64.467 ? 42  ASN   B C    1 ? 2 
ATOM   2316 O O    . ASN   B 1 30  ? 6.448   31.288 39.184  1   60     ? 42  ASN   B O    1 ? 2 
ATOM   2317 C CB   . ASN   B 1 30  ? 9.23    32.55  39.776  1   70.419 ? 42  ASN   B CB   1 ? 2 
ATOM   2318 C CG   . ASN   B 1 30  ? 10.684  32.226 39.489  1   72.577 ? 42  ASN   B CG   1 ? 2 
ATOM   2319 O OD1  . ASN   B 1 30  ? 11.037  31.842 38.366  1   73.97  ? 42  ASN   B OD1  1 ? 2 
ATOM   2320 N ND2  . ASN   B 1 30  ? 11.55   32.361 40.479  1   75.78  ? 42  ASN   B ND2  1 ? 2 
ATOM   2321 H H    . ASN   B 1 30  ? 8.785   29.962 39.096  1   61.525 ? 42  ASN   B H    1 c 2 
ATOM   2322 H HA   . ASN   B 1 30  ? 8.655   31.49  41.45   1   68.929 ? 42  ASN   B HA   1 c 2 
ATOM   2323 H HB2  . ASN   B 1 30  ? 8.782   32.75  38.93   1   68.809 ? 42  ASN   B HB2  1 c 2 
ATOM   2324 H HB3  . ASN   B 1 30  ? 9.192   33.356 40.329  1   72.872 ? 42  ASN   B HB3  1 c 2 
ATOM   2325 H HD21 . ASN   B 1 30  ? 12.399  32.134 40.358  1   76.304 ? 42  ASN   B HD21 1 c 2 
ATOM   2326 H HD22 . ASN   B 1 30  ? 11.282  32.679 41.263  1   77.499 ? 42  ASN   B HD22 1 c 2 
ATOM   2327 N N    . GLY   B 1 31  ? 6.309   32.327 41.18   1   66.092 ? 43  GLY   B N    1 ? 2 
ATOM   2328 C CA   . GLY   B 1 31  ? 4.905   32.68  41.025  1   66.728 ? 43  GLY   B CA   1 ? 2 
ATOM   2329 C C    . GLY   B 1 31  ? 3.979   31.47  41.171  1   62.919 ? 43  GLY   B C    1 ? 2 
ATOM   2330 O O    . GLY   B 1 31  ? 4.418   30.387 41.551  1   63.431 ? 43  GLY   B O    1 ? 2 
ATOM   2331 H H    . GLY   B 1 31  ? 6.739   32.561 41.952  1   68.856 ? 43  GLY   B H    1 c 2 
ATOM   2332 H HA2  . GLY   B 1 31  ? 4.668   33.355 41.703  1   68.545 ? 43  GLY   B HA2  1 c 2 
ATOM   2333 H HA3  . GLY   B 1 31  ? 4.773   33.087 40.136  1   65.278 ? 43  GLY   B HA3  1 c 2 
ATOM   2334 N N    . GLU   B 1 32  ? 2.694   31.674 40.869  1   61.592 ? 44  GLU   B N    1 ? 2 
ATOM   2335 C CA   . GLU   B 1 32  ? 1.673   30.648 41.057  1   59.286 ? 44  GLU   B CA   1 ? 2 
ATOM   2336 C C    . GLU   B 1 32  ? 1.199   30.086 39.712  1   54.732 ? 44  GLU   B C    1 ? 2 
ATOM   2337 O O    . GLU   B 1 32  ? 0.827   28.914 39.628  1   53.095 ? 44  GLU   B O    1 ? 2 
ATOM   2338 C CB   . GLU   B 1 32  ? 0.549   31.223 41.918  1   61.127 ? 44  GLU   B CB   1 ? 2 
ATOM   2339 H H    . GLU   B 1 32  ? 2.441   32.49  40.543  1   62.374 ? 44  GLU   B H    1 c 2 
ATOM   2340 H HA   . GLU   B 1 32  ? 2.078   29.903 41.568  1   58.968 ? 44  GLU   B HA   1 c 2 
ATOM   2341 H HB2  . GLU   B 1 32  ? 1.014   31.649 42.751  0   30     ? 44  GLU   B HB2  1 c 2 
ATOM   2342 H HB3  . GLU   B 1 32  ? -0.334  31.002 41.65   0   30     ? 44  GLU   B HB3  1 c 2 
ATOM   2343 N N    . GLU   B 1 33  ? 1.231   30.914 38.656  1   53.427 ? 45  GLU   B N    1 ? 2 
ATOM   2344 C CA   . GLU   B 1 33  ? 0.643   30.559 37.371  1   49.766 ? 45  GLU   B CA   1 ? 2 
ATOM   2345 C C    . GLU   B 1 33  ? 1.374   29.364 36.774  1   46.953 ? 45  GLU   B C    1 ? 2 
ATOM   2346 O O    . GLU   B 1 33  ? 2.603   29.342 36.721  1   44.599 ? 45  GLU   B O    1 ? 2 
ATOM   2347 C CB   . GLU   B 1 33  ? 0.639   31.747 36.406  1   50.778 ? 45  GLU   B CB   1 ? 2 
ATOM   2348 H H    . GLU   B 1 33  ? 1.634   31.729 38.741  1   55.09  ? 45  GLU   B H    1 c 2 
ATOM   2349 H HA   . GLU   B 1 33  ? -0.299  30.298 37.532  1   49.711 ? 45  GLU   B HA   1 c 2 
ATOM   2350 H HB2  . GLU   B 1 33  ? 1.403   32.084 36.084  0   30     ? 45  GLU   B HB2  1 c 2 
ATOM   2351 H HB3  . GLU   B 1 33  ? -0.444  31.935 36.206  0   30     ? 45  GLU   B HB3  1 c 2 
ATOM   2352 N N    . THR   B 1 34  ? 0.597   28.354 36.356  1   45.762 ? 46  THR   B N    1 ? 2 
ATOM   2353 C CA   . THR   B 1 34  ? 1.055   27.334 35.421  1   41.395 ? 46  THR   B CA   1 ? 2 
ATOM   2354 C C    . THR   B 1 34  ? 0.32    27.544 34.1    1   41.156 ? 46  THR   B C    1 ? 2 
ATOM   2355 O O    . THR   B 1 34  ? -0.75   28.145 34.079  1   43.511 ? 46  THR   B O    1 ? 2 
ATOM   2356 C CB   . THR   B 1 34  ? 0.803   25.942 35.991  1   40.098 ? 46  THR   B CB   1 ? 2 
ATOM   2357 O OG1  . THR   B 1 34  ? -0.613  25.87  36.165  1   40.15  ? 46  THR   B OG1  1 ? 2 
ATOM   2358 C CG2  . THR   B 1 34  ? 1.533   25.739 37.303  1   41.228 ? 46  THR   B CG2  1 ? 2 
ATOM   2359 H H    . THR   B 1 34  ? -0.256  28.294 36.676  1   45.412 ? 46  THR   B H    1 c 2 
ATOM   2360 H HA   . THR   B 1 34  ? 2.019   27.447 35.274  1   41.977 ? 46  THR   B HA   1 c 2 
ATOM   2361 H HB   . THR   B 1 34  ? 1.094   25.256 35.345  1   38.511 ? 46  THR   B HB   1 c 2 
ATOM   2362 H HG1  . THR   B 1 34  ? -0.85   26.615 36.693  0   30     ? 46  THR   B HG1  1 c 2 
ATOM   2363 H HG21 . THR   B 1 34  ? 1.511   24.797 37.544  1   40.623 ? 46  THR   B HG21 1 c 2 
ATOM   2364 H HG22 . THR   B 1 34  ? 1.101   26.261 38      1   42.934 ? 46  THR   B HG22 1 c 2 
ATOM   2365 H HG23 . THR   B 1 34  ? 2.457   26.027 37.209  1   41.709 ? 46  THR   B HG23 1 c 2 
ATOM   2366 N N    . PRO   B 1 35  ? 0.873   27.107 32.951  1   40.359 ? 47  PRO   B N    1 ? 2 
ATOM   2367 C CA   . PRO   B 1 35  ? 0.326   27.525 31.667  1   39.183 ? 47  PRO   B CA   1 ? 2 
ATOM   2368 C C    . PRO   B 1 35  ? -1.01   26.875 31.333  1   35.977 ? 47  PRO   B C    1 ? 2 
ATOM   2369 O O    . PRO   B 1 35  ? -1.24   25.72  31.678  1   35.477 ? 47  PRO   B O    1 ? 2 
ATOM   2370 C CB   . PRO   B 1 35  ? 1.429   27.167 30.689  1   38.389 ? 47  PRO   B CB   1 ? 2 
ATOM   2371 C CG   . PRO   B 1 35  ? 2.167   26.022 31.362  1   39.268 ? 47  PRO   B CG   1 ? 2 
ATOM   2372 C CD   . PRO   B 1 35  ? 2.074   26.268 32.83   1   40.051 ? 47  PRO   B CD   1 ? 2 
ATOM   2373 H HA   . PRO   B 1 35  ? 0.215   28.498 31.672  1   40.401 ? 47  PRO   B HA   1 c 2 
ATOM   2374 H HB2  . PRO   B 1 35  ? 1.057   26.887 29.831  1   37.989 ? 47  PRO   B HB2  1 c 2 
ATOM   2375 H HB3  . PRO   B 1 35  ? 2.024   27.925 30.542  1   39.846 ? 47  PRO   B HB3  1 c 2 
ATOM   2376 H HG2  . PRO   B 1 35  ? 1.755   25.166 31.134  1   37.406 ? 47  PRO   B HG2  1 c 2 
ATOM   2377 H HG3  . PRO   B 1 35  ? 3.103   26.002 31.08   1   38.615 ? 47  PRO   B HG3  1 c 2 
ATOM   2378 H HD2  . PRO   B 1 35  ? 1.966   25.433 33.324  1   39.298 ? 47  PRO   B HD2  1 c 2 
ATOM   2379 H HD3  . PRO   B 1 35  ? 2.861   26.741 33.161  1   40.989 ? 47  PRO   B HD3  1 c 2 
ATOM   2380 N N    . MET   B 1 36  ? -1.809  27.6   30.559  1   36.786 ? 48  MET   B N    1 ? 2 
ATOM   2381 C CA   . MET   B 1 36  ? -3.127  27.181 30.12   1   36.607 ? 48  MET   B CA   1 ? 2 
ATOM   2382 C C    . MET   B 1 36  ? -3.057  26.644 28.697  1   36.429 ? 48  MET   B C    1 ? 2 
ATOM   2383 O O    . MET   B 1 36  ? -2.192  27.036 27.908  1   34.102 ? 48  MET   B O    1 ? 2 
ATOM   2384 C CB   . MET   B 1 36  ? -4.091  28.372 30.084  1   40.349 ? 48  MET   B CB   1 ? 2 
ATOM   2385 C CG   . MET   B 1 36  ? -4.32   29.024 31.414  1   42.87  ? 48  MET   B CG   1 ? 2 
ATOM   2386 S SD   . MET   B 1 36  ? -5.392  27.996 32.431  1   44.39  ? 48  MET   B SD   1 ? 2 
ATOM   2387 C CE   . MET   B 1 36  ? -5.079  28.668 34.066  1   46.497 ? 48  MET   B CE   1 ? 2 
ATOM   2388 H H    . MET   B 1 36  ? -1.513  28.42  30.289  1   37.851 ? 48  MET   B H    1 c 2 
ATOM   2389 H HA   . MET   B 1 36  ? -3.47   26.478 30.729  1   36.542 ? 48  MET   B HA   1 c 2 
ATOM   2390 H HB2  . MET   B 1 36  ? -3.735  29.041 29.461  1   40.828 ? 48  MET   B HB2  1 c 2 
ATOM   2391 H HB3  . MET   B 1 36  ? -4.953  28.065 29.729  1   40.147 ? 48  MET   B HB3  1 c 2 
ATOM   2392 H HG2  . MET   B 1 36  ? -3.467  29.152 31.873  1   43.084 ? 48  MET   B HG2  1 c 2 
ATOM   2393 H HG3  . MET   B 1 36  ? -4.737  29.899 31.288  1   44.538 ? 48  MET   B HG3  1 c 2 
ATOM   2394 H HE1  . MET   B 1 36  ? -5.608  28.18  34.725  1   46.689 ? 48  MET   B HE1  1 c 2 
ATOM   2395 H HE2  . MET   B 1 36  ? -4.132  28.578 34.278  1   45.993 ? 48  MET   B HE2  1 c 2 
ATOM   2396 H HE3  . MET   B 1 36  ? -5.328  29.611 34.083  1   48.004 ? 48  MET   B HE3  1 c 2 
ATOM   2397 N N    . ILE   B 1 37  ? -4.02   25.778 28.36   1   34.115 ? 49  ILE   B N    1 ? 2 
ATOM   2398 C CA   . ILE   B 1 37  ? -4.106  25.298 26.992  1   34.183 ? 49  ILE   B CA   1 ? 2 
ATOM   2399 C C    . ILE   B 1 37  ? -4.138  26.479 26.019  1   34.559 ? 49  ILE   B C    1 ? 2 
ATOM   2400 O O    . ILE   B 1 37  ? -4.893  27.428 26.206  1   37.61  ? 49  ILE   B O    1 ? 2 
ATOM   2401 C CB   . ILE   B 1 37  ? -5.293  24.348 26.791  1   33.6   ? 49  ILE   B CB   1 ? 2 
ATOM   2402 C CG1  . ILE   B 1 37  ? -5.083  23.051 27.589  1   33.411 ? 49  ILE   B CG1  1 ? 2 
ATOM   2403 C CG2  . ILE   B 1 37  ? -5.53   24.093 25.301  1   33.201 ? 49  ILE   B CG2  1 ? 2 
ATOM   2404 C CD1  . ILE   B 1 37  ? -6.207  22.037 27.431  1   34.649 ? 49  ILE   B CD1  1 ? 2 
ATOM   2405 H H    . ILE   B 1 37  ? -4.628  25.493 28.98   1   34.837 ? 49  ILE   B H    1 c 2 
ATOM   2406 H HA   . ILE   B 1 37  ? -3.293  24.788 26.814  1   32.651 ? 49  ILE   B HA   1 c 2 
ATOM   2407 H HB   . ILE   B 1 37  ? -6.089  24.789 27.149  1   34.926 ? 49  ILE   B HB   1 c 2 
ATOM   2408 H HG12 . ILE   B 1 37  ? -4.243  22.638 27.302  1   32.33  ? 49  ILE   B HG12 1 c 2 
ATOM   2409 H HG13 . ILE   B 1 37  ? -4.996  23.276 28.538  1   33.633 ? 49  ILE   B HG13 1 c 2 
ATOM   2410 H HG21 . ILE   B 1 37  ? -6.224  23.423 25.19   1   33.342 ? 49  ILE   B HG21 1 c 2 
ATOM   2411 H HG22 . ILE   B 1 37  ? -4.708  23.776 24.891  1   32.47  ? 49  ILE   B HG22 1 c 2 
ATOM   2412 H HG23 . ILE   B 1 37  ? -5.809  24.917 24.868  1   34.639 ? 49  ILE   B HG23 1 c 2 
ATOM   2413 H HD11 . ILE   B 1 37  ? -7.068  22.497 27.441  1   35.506 ? 49  ILE   B HD11 1 c 2 
ATOM   2414 H HD12 . ILE   B 1 37  ? -6.175  21.395 28.166  1   33.858 ? 49  ILE   B HD12 1 c 2 
ATOM   2415 H HD13 . ILE   B 1 37  ? -6.104  21.562 26.584  1   33.789 ? 49  ILE   B HD13 1 c 2 
ATOM   2416 N N    . GLY   B 1 38  ? -3.323  26.372 24.957  1   34.028 ? 50  GLY   B N    1 ? 2 
ATOM   2417 C CA   . GLY   B 1 38  ? -3.214  27.396 23.936  1   35.551 ? 50  GLY   B CA   1 ? 2 
ATOM   2418 C C    . GLY   B 1 38  ? -2.02   28.322 24.182  1   36.584 ? 50  GLY   B C    1 ? 2 
ATOM   2419 O O    . GLY   B 1 38  ? -1.598  29.006 23.26   1   38.367 ? 50  GLY   B O    1 ? 2 
ATOM   2420 H H    . GLY   B 1 38  ? -2.813  25.619 24.869  1   32.768 ? 50  GLY   B H    1 c 2 
ATOM   2421 H HA2  . GLY   B 1 38  ? -3.115  26.962 23.056  1   35.416 ? 50  GLY   B HA2  1 c 2 
ATOM   2422 H HA3  . GLY   B 1 38  ? -4.044  27.928 23.918  1   36.982 ? 50  GLY   B HA3  1 c 2 
ATOM   2423 N N    . ASP   B 1 39  ? -1.514  28.385 25.421  1   34.626 ? 51  ASP   B N    1 ? 2 
ATOM   2424 C CA   . ASP   B 1 39  ? -0.409  29.276 25.751  1   36.829 ? 51  ASP   B CA   1 ? 2 
ATOM   2425 C C    . ASP   B 1 39  ? 0.838   28.872 24.963  1   36.303 ? 51  ASP   B C    1 ? 2 
ATOM   2426 O O    . ASP   B 1 39  ? 1.054   27.681 24.679  1   33.294 ? 51  ASP   B O    1 ? 2 
ATOM   2427 C CB   . ASP   B 1 39  ? -0.048  29.226 27.227  1   35.817 ? 51  ASP   B CB   1 ? 2 
ATOM   2428 C CG   . ASP   B 1 39  ? -0.964  29.975 28.176  1   37.215 ? 51  ASP   B CG   1 ? 2 
ATOM   2429 O OD1  . ASP   B 1 39  ? -1.869  30.694 27.686  1   38.005 ? 51  ASP   B OD1  1 ? 2 
ATOM   2430 O OD2  . ASP   B 1 39  ? -0.73   29.854 29.4    1   37.254 ? 51  ASP   B OD2  1 ? 2 
ATOM   2431 H H    . ASP   B 1 39  ? -1.864  27.86  26.081  1   34.387 ? 51  ASP   B H    1 c 2 
ATOM   2432 H HA   . ASP   B 1 39  ? -0.662  30.194 25.506  1   38.24  ? 51  ASP   B HA   1 c 2 
ATOM   2433 H HB2  . ASP   B 1 39  ? -0.013  28.289 27.509  1   34.434 ? 51  ASP   B HB2  1 c 2 
ATOM   2434 H HB3  . ASP   B 1 39  ? 0.852   29.599 27.337  1   36.54  ? 51  ASP   B HB3  1 c 2 
ATOM   2435 N N    . LYS   B 1 40  ? 1.646   29.883 24.604  1   39.103 ? 52  LYS   B N    1 ? 2 
ATOM   2436 C CA   . LYS   B 1 40  ? 2.907   29.631 23.928  1   39.225 ? 52  LYS   B CA   1 ? 2 
ATOM   2437 C C    . LYS   B 1 40  ? 3.974   29.372 24.984  1   37.371 ? 52  LYS   B C    1 ? 2 
ATOM   2438 O O    . LYS   B 1 40  ? 4.222   30.243 25.813  1   38.694 ? 52  LYS   B O    1 ? 2 
ATOM   2439 C CB   . LYS   B 1 40  ? 3.271   30.808 23.014  1   44.512 ? 52  LYS   B CB   1 ? 2 
ATOM   2440 C CG   . LYS   B 1 40  ? 4.552   30.632 22.203  1   47.362 ? 52  LYS   B CG   1 ? 2 
ATOM   2441 C CD   . LYS   B 1 40  ? 4.465   31.066 20.741  1   51.732 ? 52  LYS   B CD   1 ? 2 
ATOM   2442 C CE   . LYS   B 1 40  ? 4.982   32.429 20.475  1   57.594 ? 52  LYS   B CE   1 ? 2 
ATOM   2443 N NZ   . LYS   B 1 40  ? 6.436   32.4   20.289  1   59.775 ? 52  LYS   B NZ   1 ? 2 
ATOM   2444 H H    . LYS   B 1 40  ? 1.405   30.746 24.787  1   40.481 ? 52  LYS   B H    1 c 2 
ATOM   2445 H HA   . LYS   B 1 40  ? 2.806   28.82  23.368  1   38.11  ? 52  LYS   B HA   1 c 2 
ATOM   2446 H HB2  . LYS   B 1 40  ? 2.528   30.962 22.393  1   45.091 ? 52  LYS   B HB2  1 c 2 
ATOM   2447 H HB3  . LYS   B 1 40  ? 3.365   31.613 23.567  1   45.815 ? 52  LYS   B HB3  1 c 2 
ATOM   2448 H HG2  . LYS   B 1 40  ? 5.266   31.144 22.642  1   48.385 ? 52  LYS   B HG2  1 c 2 
ATOM   2449 H HG3  . LYS   B 1 40  ? 4.809   29.685 22.234  1   45.468 ? 52  LYS   B HG3  1 c 2 
ATOM   2450 H HD2  . LYS   B 1 40  ? 4.97    30.425 20.195  1   51.056 ? 52  LYS   B HD2  1 c 2 
ATOM   2451 H HD3  . LYS   B 1 40  ? 3.528   31.022 20.452  1   51.56  ? 52  LYS   B HD3  1 c 2 
ATOM   2452 H HE2  . LYS   B 1 40  ? 4.564   32.789 19.672  1   58.713 ? 52  LYS   B HE2  1 c 2 
ATOM   2453 H HE3  . LYS   B 1 40  ? 4.767   33.015 21.222  1   57.9   ? 52  LYS   B HE3  1 c 2 
ATOM   2454 H HZ1  . LYS   B 1 40  ? 6.636   32.003 19.5    1   59.241 ? 52  LYS   B HZ1  1 c 2 
ATOM   2455 H HZ2  . LYS   B 1 40  ? 6.824   31.935 20.963  1   57.873 ? 52  LYS   B HZ2  1 c 2 
ATOM   2456 H HZ3  . LYS   B 1 40  ? 6.761   33.246 20.286  1   61.46  ? 52  LYS   B HZ3  1 c 2 
ATOM   2457 N N    . VAL   B 1 41  ? 4.63    28.207 24.903  1   36.342 ? 53  VAL   B N    1 ? 2 
ATOM   2458 C CA   . VAL   B 1 41  ? 5.53    27.737 25.945  1   36.748 ? 53  VAL   B CA   1 ? 2 
ATOM   2459 C C    . VAL   B 1 41  ? 6.964   27.611 25.405  1   38.152 ? 53  VAL   B C    1 ? 2 
ATOM   2460 O O    . VAL   B 1 41  ? 7.186   27.129 24.296  1   36.239 ? 53  VAL   B O    1 ? 2 
ATOM   2461 C CB   . VAL   B 1 41  ? 4.99    26.403 26.493  1   37.973 ? 53  VAL   B CB   1 ? 2 
ATOM   2462 C CG1  . VAL   B 1 41  ? 5.95    25.749 27.467  1   39.275 ? 53  VAL   B CG1  1 ? 2 
ATOM   2463 C CG2  . VAL   B 1 41  ? 3.619   26.579 27.146  1   38.768 ? 53  VAL   B CG2  1 ? 2 
ATOM   2464 H H    . VAL   B 1 41  ? 4.514   27.684 24.163  1   35.661 ? 53  VAL   B H    1 c 2 
ATOM   2465 H HA   . VAL   B 1 41  ? 5.529   28.39  26.672  1   38.334 ? 53  VAL   B HA   1 c 2 
ATOM   2466 H HB   . VAL   B 1 41  ? 4.881   25.796 25.723  1   36.834 ? 53  VAL   B HB   1 c 2 
ATOM   2467 H HG11 . VAL   B 1 41  ? 6.36    26.431 28.023  1   39.986 ? 53  VAL   B HG11 1 c 2 
ATOM   2468 H HG12 . VAL   B 1 41  ? 6.642   25.276 26.974  1   38.252 ? 53  VAL   B HG12 1 c 2 
ATOM   2469 H HG13 . VAL   B 1 41  ? 5.467   25.119 28.028  1   37.697 ? 53  VAL   B HG13 1 c 2 
ATOM   2470 H HG21 . VAL   B 1 41  ? 3.326   25.732 27.522  1   37.27  ? 53  VAL   B HG21 1 c 2 
ATOM   2471 H HG22 . VAL   B 1 41  ? 2.976   26.875 26.48   1   38.77  ? 53  VAL   B HG22 1 c 2 
ATOM   2472 H HG23 . VAL   B 1 41  ? 3.68    27.243 27.853  1   39.592 ? 53  VAL   B HG23 1 c 2 
ATOM   2473 N N    . TYR   B 1 42  ? 7.927   28.067 26.222  1   38.276 ? 54  TYR   B N    1 ? 2 
ATOM   2474 C CA   . TYR   B 1 42  ? 9.349   28.025 25.898  1   39.783 ? 54  TYR   B CA   1 ? 2 
ATOM   2475 C C    . TYR   B 1 42  ? 10.073  27.152 26.918  1   37.018 ? 54  TYR   B C    1 ? 2 
ATOM   2476 O O    . TYR   B 1 42  ? 10.003  27.423 28.122  1   37.805 ? 54  TYR   B O    1 ? 2 
ATOM   2477 C CB   . TYR   B 1 42  ? 9.951   29.432 25.967  1   44.365 ? 54  TYR   B CB   1 ? 2 
ATOM   2478 C CG   . TYR   B 1 42  ? 9.349   30.475 25.038  1   47.802 ? 54  TYR   B CG   1 ? 2 
ATOM   2479 C CD1  . TYR   B 1 42  ? 8.115   31.06  25.321  1   49.611 ? 54  TYR   B CD1  1 ? 2 
ATOM   2480 C CD2  . TYR   B 1 42  ? 10.049  30.929 23.925  1   50.329 ? 54  TYR   B CD2  1 ? 2 
ATOM   2481 C CE1  . TYR   B 1 42  ? 7.577   32.035 24.496  1   51.925 ? 54  TYR   B CE1  1 ? 2 
ATOM   2482 C CE2  . TYR   B 1 42  ? 9.522   31.9   23.091  1   53.106 ? 54  TYR   B CE2  1 ? 2 
ATOM   2483 C CZ   . TYR   B 1 42  ? 8.292   32.465 23.391  1   53.272 ? 54  TYR   B CZ   1 ? 2 
ATOM   2484 O OH   . TYR   B 1 42  ? 7.771   33.417 22.57   1   56.615 ? 54  TYR   B OH   1 ? 2 
ATOM   2485 H H    . TYR   B 1 42  ? 7.682   28.422 27.028  1   39.145 ? 54  TYR   B H    1 c 2 
ATOM   2486 H HA   . TYR   B 1 42  ? 9.476   27.652 24.985  1   39.093 ? 54  TYR   B HA   1 c 2 
ATOM   2487 H HB2  . TYR   B 1 42  ? 9.866   29.755 26.891  1   44.94  ? 54  TYR   B HB2  1 c 2 
ATOM   2488 H HB3  . TYR   B 1 42  ? 10.912  29.361 25.774  1   45.257 ? 54  TYR   B HB3  1 c 2 
ATOM   2489 H HD1  . TYR   B 1 42  ? 7.631   30.777 26.081  1   48.223 ? 54  TYR   B HD1  1 c 2 
ATOM   2490 H HD2  . TYR   B 1 42  ? 10.892  30.556 23.723  1   50.486 ? 54  TYR   B HD2  1 c 2 
ATOM   2491 H HE1  . TYR   B 1 42  ? 6.738   32.415 24.693  1   51.864 ? 54  TYR   B HE1  1 c 2 
ATOM   2492 H HE2  . TYR   B 1 42  ? 10.005  32.19  22.336  1   54.42  ? 54  TYR   B HE2  1 c 2 
ATOM   2493 H HH   . TYR   B 1 42  ? 7.008   33.729 22.929  0   30     ? 54  TYR   B HH   1 c 2 
ATOM   2494 N N    . VAL   B 1 43  ? 10.812  26.141 26.441  1   36.303 ? 55  VAL   B N    1 ? 2 
ATOM   2495 C CA   . VAL   B 1 43  ? 11.535  25.262 27.351  1   36.011 ? 55  VAL   B CA   1 ? 2 
ATOM   2496 C C    . VAL   B 1 43  ? 12.953  24.994 26.852  1   38.328 ? 55  VAL   B C    1 ? 2 
ATOM   2497 O O    . VAL   B 1 43  ? 13.243  25.169 25.676  1   40.025 ? 55  VAL   B O    1 ? 2 
ATOM   2498 C CB   . VAL   B 1 43  ? 10.821  23.921 27.571  1   33.802 ? 55  VAL   B CB   1 ? 2 
ATOM   2499 C CG1  . VAL   B 1 43  ? 9.415   24.117 28.098  1   32.449 ? 55  VAL   B CG1  1 ? 2 
ATOM   2500 C CG2  . VAL   B 1 43  ? 10.816  23.047 26.324  1   32.517 ? 55  VAL   B CG2  1 ? 2 
ATOM   2501 H H    . VAL   B 1 43  ? 10.868  25.996 25.54   1   36.1   ? 55  VAL   B H    1 c 2 
ATOM   2502 H HA   . VAL   B 1 43  ? 11.601  25.713 28.213  1   37.255 ? 55  VAL   B HA   1 c 2 
ATOM   2503 H HB   . VAL   B 1 43  ? 11.328  23.437 28.264  1   33.763 ? 55  VAL   B HB   1 c 2 
ATOM   2504 H HG11 . VAL   B 1 43  ? 8.86    24.513 27.405  1   32.541 ? 55  VAL   B HG11 1 c 2 
ATOM   2505 H HG12 . VAL   B 1 43  ? 9.436   24.705 28.871  1   33.706 ? 55  VAL   B HG12 1 c 2 
ATOM   2506 H HG13 . VAL   B 1 43  ? 9.042   23.257 28.356  1   31.325 ? 55  VAL   B HG13 1 c 2 
ATOM   2507 H HG21 . VAL   B 1 43  ? 10.255  22.271 26.479  1   31.054 ? 55  VAL   B HG21 1 c 2 
ATOM   2508 H HG22 . VAL   B 1 43  ? 11.721  22.755 26.125  1   32.987 ? 55  VAL   B HG22 1 c 2 
ATOM   2509 H HG23 . VAL   B 1 43  ? 10.466  23.554 25.573  1   32.77  ? 55  VAL   B HG23 1 c 2 
ATOM   2510 N N    . HIS   B 1 44  ? 13.812  24.569 27.782  1   39.812 ? 56  HIS   B N    1 ? 2 
ATOM   2511 C CA   . HIS   B 1 44  ? 14.995  23.781 27.46   1   40.923 ? 56  HIS   B CA   1 ? 2 
ATOM   2512 C C    . HIS   B 1 44  ? 14.788  22.388 28.038  1   36.926 ? 56  HIS   B C    1 ? 2 
ATOM   2513 O O    . HIS   B 1 44  ? 14.133  22.257 29.051  1   36.26  ? 56  HIS   B O    1 ? 2 
ATOM   2514 C CB   . HIS   B 1 44  ? 16.285  24.423 27.989  1   45.479 ? 56  HIS   B CB   1 ? 2 
ATOM   2515 C CG   . HIS   B 1 44  ? 16.869  25.439 27.072  1   48.718 ? 56  HIS   B CG   1 ? 2 
ATOM   2516 N ND1  . HIS   B 1 44  ? 17.26   25.157 25.779  1   49.107 ? 56  HIS   B ND1  1 ? 2 
ATOM   2517 C CD2  . HIS   B 1 44  ? 17.162  26.732 27.287  1   51.443 ? 56  HIS   B CD2  1 ? 2 
ATOM   2518 C CE1  . HIS   B 1 44  ? 17.743  26.262 25.227  1   51.44  ? 56  HIS   B CE1  1 ? 2 
ATOM   2519 N NE2  . HIS   B 1 44  ? 17.7    27.228 26.128  1   52.782 ? 56  HIS   B NE2  1 ? 2 
ATOM   2520 H H    . HIS   B 1 44  ? 13.656  24.781 28.658  1   40.188 ? 56  HIS   B H    1 c 2 
ATOM   2521 H HA   . HIS   B 1 44  ? 15.058  23.7   26.477  1   40.411 ? 56  HIS   B HA   1 c 2 
ATOM   2522 H HB2  . HIS   B 1 44  ? 16.093  24.848 28.853  1   46.083 ? 56  HIS   B HB2  1 c 2 
ATOM   2523 H HB3  . HIS   B 1 44  ? 16.949  23.716 28.143  1   45.544 ? 56  HIS   B HB3  1 c 2 
ATOM   2524 H HD1  . HIS   B 1 44  ? 17.227  24.391 25.37   0   30     ? 56  HIS   B HD1  1 c 2 
ATOM   2525 H HD2  . HIS   B 1 44  ? 17.016  27.216 28.075  1   52.236 ? 56  HIS   B HD2  1 c 2 
ATOM   2526 H HE1  . HIS   B 1 44  ? 18.074  26.338 24.349  1   52.182 ? 56  HIS   B HE1  1 c 2 
ATOM   2527 H HE2  . HIS   B 1 44  ? 17.976  28.064 26.103  0   30     ? 56  HIS   B HE2  1 c 2 
ATOM   2528 N N    . TYR   B 1 45  ? 15.317  21.359 27.38   1   36.522 ? 57  TYR   B N    1 ? 2 
ATOM   2529 C CA   . TYR   B 1 45  ? 15.066  19.986 27.782  1   34.635 ? 57  TYR   B CA   1 ? 2 
ATOM   2530 C C    . TYR   B 1 45  ? 16.24   19.101 27.337  1   36.587 ? 57  TYR   B C    1 ? 2 
ATOM   2531 O O    . TYR   B 1 45  ? 16.956  19.417 26.389  1   35.272 ? 57  TYR   B O    1 ? 2 
ATOM   2532 C CB   . TYR   B 1 45  ? 13.735  19.458 27.22   1   31.792 ? 57  TYR   B CB   1 ? 2 
ATOM   2533 C CG   . TYR   B 1 45  ? 13.802  19.064 25.751  1   30.371 ? 57  TYR   B CG   1 ? 2 
ATOM   2534 C CD1  . TYR   B 1 45  ? 13.539  19.983 24.735  1   31.284 ? 57  TYR   B CD1  1 ? 2 
ATOM   2535 C CD2  . TYR   B 1 45  ? 14.208  17.785 25.373  1   29.18  ? 57  TYR   B CD2  1 ? 2 
ATOM   2536 C CE1  . TYR   B 1 45  ? 13.652  19.63  23.392  1   29.423 ? 57  TYR   B CE1  1 ? 2 
ATOM   2537 C CE2  . TYR   B 1 45  ? 14.347  17.43  24.038  1   28.23  ? 57  TYR   B CE2  1 ? 2 
ATOM   2538 C CZ   . TYR   B 1 45  ? 14.064  18.355 23.049  1   28.554 ? 57  TYR   B CZ   1 ? 2 
ATOM   2539 O OH   . TYR   B 1 45  ? 14.214  17.97  21.752  1   27.116 ? 57  TYR   B OH   1 ? 2 
ATOM   2540 H H    . TYR   B 1 45  ? 15.852  21.516 26.656  1   37.148 ? 57  TYR   B H    1 c 2 
ATOM   2541 H HA   . TYR   B 1 45  ? 15.016  19.961 28.771  1   35.243 ? 57  TYR   B HA   1 c 2 
ATOM   2542 H HB2  . TYR   B 1 45  ? 13.461  18.675 27.747  1   30.915 ? 57  TYR   B HB2  1 c 2 
ATOM   2543 H HB3  . TYR   B 1 45  ? 13.05   20.154 27.332  1   31.598 ? 57  TYR   B HB3  1 c 2 
ATOM   2544 H HD1  . TYR   B 1 45  ? 13.272  20.86  24.961  1   31.344 ? 57  TYR   B HD1  1 c 2 
ATOM   2545 H HD2  . TYR   B 1 45  ? 14.421  17.153 26.041  1   29.034 ? 57  TYR   B HD2  1 c 2 
ATOM   2546 H HE1  . TYR   B 1 45  ? 13.47   20.263 22.719  1   30.365 ? 57  TYR   B HE1  1 c 2 
ATOM   2547 H HE2  . TYR   B 1 45  ? 14.618  16.559 23.807  1   28.107 ? 57  TYR   B HE2  1 c 2 
ATOM   2548 H HH   . TYR   B 1 45  ? 14.037  18.596 21.256  0   30     ? 57  TYR   B HH   1 c 2 
ATOM   2549 N N    . LYS   B 1 46  ? 16.387  17.969 28.036  1   36.407 ? 58  LYS   B N    1 ? 2 
ATOM   2550 C CA   . LYS   B 1 46  ? 17.239  16.859 27.636  1   37.211 ? 58  LYS   B CA   1 ? 2 
ATOM   2551 C C    . LYS   B 1 46  ? 16.358  15.62  27.699  1   36.628 ? 58  LYS   B C    1 ? 2 
ATOM   2552 O O    . LYS   B 1 46  ? 15.505  15.518 28.584  1   39.95  ? 58  LYS   B O    1 ? 2 
ATOM   2553 C CB   . LYS   B 1 46  ? 18.467  16.678 28.545  1   40.845 ? 58  LYS   B CB   1 ? 2 
ATOM   2554 C CG   . LYS   B 1 46  ? 19.353  17.883 28.63   1   42.884 ? 58  LYS   B CG   1 ? 2 
ATOM   2555 C CD   . LYS   B 1 46  ? 20.799  17.638 29.041  1   45.541 ? 58  LYS   B CD   1 ? 2 
ATOM   2556 C CE   . LYS   B 1 46  ? 20.999  17.49  30.517  1   46.987 ? 58  LYS   B CE   1 ? 2 
ATOM   2557 N NZ   . LYS   B 1 46  ? 22.424  17.589 30.846  1   49.485 ? 58  LYS   B NZ   1 ? 2 
ATOM   2558 H H    . LYS   B 1 46  ? 15.924  17.887 28.82   1   36.159 ? 58  LYS   B H    1 c 2 
ATOM   2559 H HA   . LYS   B 1 46  ? 17.533  17.003 26.702  1   37.711 ? 58  LYS   B HA   1 c 2 
ATOM   2560 H HB2  . LYS   B 1 46  ? 18.162  16.451 29.449  1   40.407 ? 58  LYS   B HB2  1 c 2 
ATOM   2561 H HB3  . LYS   B 1 46  ? 18.999  15.923 28.211  1   40.66  ? 58  LYS   B HB3  1 c 2 
ATOM   2562 H HG2  . LYS   B 1 46  ? 19.35   18.325 27.753  1   42.83  ? 58  LYS   B HG2  1 c 2 
ATOM   2563 H HG3  . LYS   B 1 46  ? 18.95   18.511 29.269  1   43.185 ? 58  LYS   B HG3  1 c 2 
ATOM   2564 H HD2  . LYS   B 1 46  ? 21.121  16.826 28.593  1   45.292 ? 58  LYS   B HD2  1 c 2 
ATOM   2565 H HD3  . LYS   B 1 46  ? 21.347  18.388 28.72   1   47.083 ? 58  LYS   B HD3  1 c 2 
ATOM   2566 H HE2  . LYS   B 1 46  ? 20.512  18.188 30.99   1   46.825 ? 58  LYS   B HE2  1 c 2 
ATOM   2567 H HE3  . LYS   B 1 46  ? 20.662  16.625 30.811  1   45.772 ? 58  LYS   B HE3  1 c 2 
ATOM   2568 H HZ1  . LYS   B 1 46  ? 22.745  18.396 30.588  1   50.893 ? 58  LYS   B HZ1  1 c 2 
ATOM   2569 H HZ2  . LYS   B 1 46  ? 22.882  16.936 30.418  1   49.828 ? 58  LYS   B HZ2  1 c 2 
ATOM   2570 H HZ3  . LYS   B 1 46  ? 22.538  17.498 31.74   1   50.826 ? 58  LYS   B HZ3  1 c 2 
ATOM   2571 N N    . GLY   B 1 47  ? 16.5    14.749 26.7    1   33.72  ? 59  GLY   B N    1 ? 2 
ATOM   2572 C CA   . GLY   B 1 47  ? 15.612  13.611 26.535  1   31.756 ? 59  GLY   B CA   1 ? 2 
ATOM   2573 C C    . GLY   B 1 47  ? 16.419  12.367 26.181  1   32.227 ? 59  GLY   B C    1 ? 2 
ATOM   2574 O O    . GLY   B 1 47  ? 17.465  12.458 25.512  1   31.221 ? 59  GLY   B O    1 ? 2 
ATOM   2575 H H    . GLY   B 1 47  ? 17.179  14.865 26.099  1   34.99  ? 59  GLY   B H    1 c 2 
ATOM   2576 H HA2  . GLY   B 1 47  ? 15.112  13.46  27.368  1   31.506 ? 59  GLY   B HA2  1 c 2 
ATOM   2577 H HA3  . GLY   B 1 47  ? 14.964  13.804 25.817  1   30.83  ? 59  GLY   B HA3  1 c 2 
ATOM   2578 N N    . LYS   B 1 48  ? 15.925  11.21  26.621  1   29.744 ? 60  LYS   B N    1 ? 2 
ATOM   2579 C CA   . LYS   B 1 48  ? 16.558  9.955  26.262  1   30.079 ? 60  LYS   B CA   1 ? 2 
ATOM   2580 C C    . LYS   B 1 48  ? 15.545  8.829  26.409  1   30.581 ? 60  LYS   B C    1 ? 2 
ATOM   2581 O O    . LYS   B 1 48  ? 14.526  9.004  27.081  1   30.106 ? 60  LYS   B O    1 ? 2 
ATOM   2582 C CB   . LYS   B 1 48  ? 17.814  9.67   27.078  1   33.6   ? 60  LYS   B CB   1 ? 2 
ATOM   2583 C CG   . LYS   B 1 48  ? 17.598  9.559  28.585  1   35.669 ? 60  LYS   B CG   1 ? 2 
ATOM   2584 C CD   . LYS   B 1 48  ? 18.804  8.981  29.315  1   40.977 ? 60  LYS   B CD   1 ? 2 
ATOM   2585 C CE   . LYS   B 1 48  ? 18.629  8.985  30.793  1   42.436 ? 60  LYS   B CE   1 ? 2 
ATOM   2586 N NZ   . LYS   B 1 48  ? 19.731  8.246  31.425  1   47.151 ? 60  LYS   B NZ   1 ? 2 
ATOM   2587 H H    . LYS   B 1 48  ? 15.182  11.2   27.153  1   29.451 ? 60  LYS   B H    1 c 2 
ATOM   2588 H HA   . LYS   B 1 48  ? 16.818  10.008 25.311  1   30.807 ? 60  LYS   B HA   1 c 2 
ATOM   2589 H HB2  . LYS   B 1 48  ? 18.209  8.831  26.76   1   34.08  ? 60  LYS   B HB2  1 c 2 
ATOM   2590 H HB3  . LYS   B 1 48  ? 18.464  10.386 26.911  1   34.449 ? 60  LYS   B HB3  1 c 2 
ATOM   2591 H HG2  . LYS   B 1 48  ? 17.404  10.453 28.942  1   35.865 ? 60  LYS   B HG2  1 c 2 
ATOM   2592 H HG3  . LYS   B 1 48  ? 16.818  8.989  28.754  1   35.045 ? 60  LYS   B HG3  1 c 2 
ATOM   2593 H HD2  . LYS   B 1 48  ? 18.945  8.061  29.015  1   40.787 ? 60  LYS   B HD2  1 c 2 
ATOM   2594 H HD3  . LYS   B 1 48  ? 19.602  9.505  29.084  1   41.466 ? 60  LYS   B HD3  1 c 2 
ATOM   2595 H HE2  . LYS   B 1 48  ? 18.624  9.901  31.125  1   43.041 ? 60  LYS   B HE2  1 c 2 
ATOM   2596 H HE3  . LYS   B 1 48  ? 17.782  8.564  31.029  1   41.871 ? 60  LYS   B HE3  1 c 2 
ATOM   2597 H HZ1  . LYS   B 1 48  ? 20.525  8.608  31.18   1   47.502 ? 60  LYS   B HZ1  1 c 2 
ATOM   2598 H HZ2  . LYS   B 1 48  ? 19.707  7.378  31.166  1   46.403 ? 60  LYS   B HZ2  1 c 2 
ATOM   2599 H HZ3  . LYS   B 1 48  ? 19.651  8.289  32.327  1   47.44  ? 60  LYS   B HZ3  1 c 2 
ATOM   2600 N N    . LEU   B 1 49  ? 15.807  7.724  25.71   1   29.784 ? 61  LEU   B N    1 ? 2 
ATOM   2601 C CA   . LEU   B 1 49  ? 15.148  6.461  25.976  1   33.269 ? 61  LEU   B CA   1 ? 2 
ATOM   2602 C C    . LEU   B 1 49  ? 15.646  6.031  27.351  1   38.582 ? 61  LEU   B C    1 ? 2 
ATOM   2603 O O    . LEU   B 1 49  ? 16.797  6.303  27.693  1   37.439 ? 61  LEU   B O    1 ? 2 
ATOM   2604 C CB   . LEU   B 1 49  ? 15.466  5.445  24.882  1   34.611 ? 61  LEU   B CB   1 ? 2 
ATOM   2605 C CG   . LEU   B 1 49  ? 15.116  5.885  23.458  1   35.887 ? 61  LEU   B CG   1 ? 2 
ATOM   2606 C CD1  . LEU   B 1 49  ? 15.398  4.787  22.438  1   38.457 ? 61  LEU   B CD1  1 ? 2 
ATOM   2607 C CD2  . LEU   B 1 49  ? 13.671  6.335  23.365  1   37.094 ? 61  LEU   B CD2  1 ? 2 
ATOM   2608 H H    . LEU   B 1 49  ? 16.433  7.76   25.046  1   31.427 ? 61  LEU   B H    1 c 2 
ATOM   2609 H HA   . LEU   B 1 49  ? 14.17   6.613  26.016  1   32.256 ? 61  LEU   B HA   1 c 2 
ATOM   2610 H HB2  . LEU   B 1 49  ? 16.43   5.244  24.918  1   36.083 ? 61  LEU   B HB2  1 c 2 
ATOM   2611 H HB3  . LEU   B 1 49  ? 14.976  4.614  25.081  1   34.887 ? 61  LEU   B HB3  1 c 2 
ATOM   2612 H HG   . LEU   B 1 49  ? 15.688  6.661  23.228  1   36.482 ? 61  LEU   B HG   1 c 2 
ATOM   2613 H HD11 . LEU   B 1 49  ? 16.327  4.512  22.505  1   39.092 ? 61  LEU   B HD11 1 c 2 
ATOM   2614 H HD12 . LEU   B 1 49  ? 15.224  5.123  21.543  1   37.65  ? 61  LEU   B HD12 1 c 2 
ATOM   2615 H HD13 . LEU   B 1 49  ? 14.822  4.024  22.614  1   37.809 ? 61  LEU   B HD13 1 c 2 
ATOM   2616 H HD21 . LEU   B 1 49  ? 13.604  7.263  23.646  1   35.724 ? 61  LEU   B HD21 1 c 2 
ATOM   2617 H HD22 . LEU   B 1 49  ? 13.119  5.781  23.942  1   36.02  ? 61  LEU   B HD22 1 c 2 
ATOM   2618 H HD23 . LEU   B 1 49  ? 13.362  6.253  22.447  1   35.971 ? 61  LEU   B HD23 1 c 2 
ATOM   2619 N N    . SER   B 1 50  ? 14.764  5.453  28.173  1   42.672 ? 62  SER   B N    1 ? 2 
ATOM   2620 C CA   . SER   B 1 50  ? 15.103  5.139  29.558  1   49.177 ? 62  SER   B CA   1 ? 2 
ATOM   2621 C C    . SER   B 1 50  ? 16.351  4.254  29.638  1   52.43  ? 62  SER   B C    1 ? 2 
ATOM   2622 O O    . SER   B 1 50  ? 17.112  4.362  30.593  1   61.722 ? 62  SER   B O    1 ? 2 
ATOM   2623 C CB   . SER   B 1 50  ? 13.93   4.492  30.257  1   49.603 ? 62  SER   B CB   1 ? 2 
ATOM   2624 O OG   . SER   B 1 50  ? 13.587  3.277  29.601  1   53.037 ? 62  SER   B OG   1 ? 2 
ATOM   2625 H H    . SER   B 1 50  ? 13.929  5.246  27.864  1   41.556 ? 62  SER   B H    1 c 2 
ATOM   2626 H HA   . SER   B 1 50  ? 15.304  5.992  30.02   1   48.615 ? 62  SER   B HA   1 c 2 
ATOM   2627 H HB2  . SER   B 1 50  ? 14.165  4.309  31.186  1   51.611 ? 62  SER   B HB2  1 c 2 
ATOM   2628 H HB3  . SER   B 1 50  ? 13.166  5.1    30.243  1   49.094 ? 62  SER   B HB3  1 c 2 
ATOM   2629 H HG   . SER   B 1 50  ? 13.255  2.519  29.775  0   30     ? 62  SER   B HG   1 c 2 
ATOM   2630 N N    . ASN   B 1 51  ? 16.526  3.378  28.636  1   53.872 ? 63  ASN   B N    1 ? 2 
ATOM   2631 C CA   . ASN   B 1 51  ? 17.763  2.647  28.36   1   60.197 ? 63  ASN   B CA   1 ? 2 
ATOM   2632 C C    . ASN   B 1 51  ? 19.007  3.543  28.324  1   65.828 ? 63  ASN   B C    1 ? 2 
ATOM   2633 O O    . ASN   B 1 51  ? 20.093  3.115  28.702  1   66.75  ? 63  ASN   B O    1 ? 2 
ATOM   2634 C CB   . ASN   B 1 51  ? 17.708  1.969  26.991  1   55.588 ? 63  ASN   B CB   1 ? 2 
ATOM   2635 H H    . ASN   B 1 51  ? 15.81   3.215  28.092  1   53.157 ? 63  ASN   B H    1 c 2 
ATOM   2636 H HA   . ASN   B 1 51  ? 17.882  1.95   29.044  1   60.669 ? 63  ASN   B HA   1 c 2 
ATOM   2637 H HB2  . ASN   B 1 51  ? 18.929  1.866  26.826  0   30     ? 63  ASN   B HB2  1 c 2 
ATOM   2638 H HB3  . ASN   B 1 51  ? 17.082  1.856  26.81   0   30     ? 63  ASN   B HB3  1 c 2 
ATOM   2639 N N    . GLY   B 1 52  ? 18.864  4.746  27.747  1   71.206 ? 64  GLY   B N    1 ? 2 
ATOM   2640 C CA   . GLY   B 1 52  ? 19.937  5.726  27.645  1   66.159 ? 64  GLY   B CA   1 ? 2 
ATOM   2641 C C    . GLY   B 1 52  ? 20.42   5.942  26.208  1   63.748 ? 64  GLY   B C    1 ? 2 
ATOM   2642 O O    . GLY   B 1 52  ? 21.311  6.76   26.002  1   67.352 ? 64  GLY   B O    1 ? 2 
ATOM   2643 H H    . GLY   B 1 52  ? 18.051  4.965  27.394  1   65.952 ? 64  GLY   B H    1 c 2 
ATOM   2644 H HA2  . GLY   B 1 52  ? 19.617  6.58   28.006  1   65.895 ? 64  GLY   B HA2  1 c 2 
ATOM   2645 H HA3  . GLY   B 1 52  ? 20.695  5.432  28.202  1   68.716 ? 64  GLY   B HA3  1 c 2 
ATOM   2646 N N    . LYS   B 1 53  ? 19.789  5.282  25.219  1   60.042 ? 65  LYS   B N    1 ? 2 
ATOM   2647 C CA   . LYS   B 1 53  ? 20.491  4.866  24.004  1   59.243 ? 65  LYS   B CA   1 ? 2 
ATOM   2648 C C    . LYS   B 1 53  ? 20.297  5.806  22.799  1   58.573 ? 65  LYS   B C    1 ? 2 
ATOM   2649 O O    . LYS   B 1 53  ? 20.963  5.623  21.771  1   61.597 ? 65  LYS   B O    1 ? 2 
ATOM   2650 C CB   . LYS   B 1 53  ? 20.112  3.413  23.686  1   56.699 ? 65  LYS   B CB   1 ? 2 
ATOM   2651 H H    . LYS   B 1 53  ? 18.896  5.102  25.295  1   59.028 ? 65  LYS   B H    1 c 2 
ATOM   2652 H HA   . LYS   B 1 53  ? 21.461  4.858  24.212  1   60.831 ? 65  LYS   B HA   1 c 2 
ATOM   2653 H HB2  . LYS   B 1 53  ? 20.74   2.853  23.438  0   30     ? 65  LYS   B HB2  1 c 2 
ATOM   2654 H HB3  . LYS   B 1 53  ? 18.979  3.42   23.614  0   30     ? 65  LYS   B HB3  1 c 2 
ATOM   2655 N N    . LYS   B 1 54  ? 19.382  6.782  22.91   1   51.081 ? 66  LYS   B N    1 ? 2 
ATOM   2656 C CA   . LYS   B 1 54  ? 19.253  7.912  21.996  1   45.769 ? 66  LYS   B CA   1 ? 2 
ATOM   2657 C C    . LYS   B 1 54  ? 19.079  9.169  22.849  1   46.346 ? 66  LYS   B C    1 ? 2 
ATOM   2658 O O    . LYS   B 1 54  ? 17.998  9.386  23.384  1   57.581 ? 66  LYS   B O    1 ? 2 
ATOM   2659 C CB   . LYS   B 1 54  ? 18.007  7.777  21.103  1   39.476 ? 66  LYS   B CB   1 ? 2 
ATOM   2660 H H    . LYS   B 1 54  ? 18.787  6.73   23.602  1   50.392 ? 66  LYS   B H    1 c 2 
ATOM   2661 H HA   . LYS   B 1 54  ? 20.074  7.988  21.447  1   47.316 ? 66  LYS   B HA   1 c 2 
ATOM   2662 H HB2  . LYS   B 1 54  ? 18.307  7.518  20.29   0   30     ? 66  LYS   B HB2  1 c 2 
ATOM   2663 H HB3  . LYS   B 1 54  ? 17.173  7.819  21.731  0   30     ? 66  LYS   B HB3  1 c 2 
ATOM   2664 N N    . PHE   B 1 55  ? 20.156  9.935  23.064  1   41.966 ? 67  PHE   B N    1 ? 2 
ATOM   2665 C CA   . PHE   B 1 55  ? 20.116  11.142 23.88   1   39.902 ? 67  PHE   B CA   1 ? 2 
ATOM   2666 C C    . PHE   B 1 55  ? 19.852  12.358 22.995  1   37.912 ? 67  PHE   B C    1 ? 2 
ATOM   2667 O O    . PHE   B 1 55  ? 20.444  12.448 21.921  1   38.029 ? 67  PHE   B O    1 ? 2 
ATOM   2668 C CB   . PHE   B 1 55  ? 21.476  11.198 24.582  1   42.575 ? 67  PHE   B CB   1 ? 2 
ATOM   2669 C CG   . PHE   B 1 55  ? 21.56   12.19  25.727  1   44.805 ? 67  PHE   B CG   1 ? 2 
ATOM   2670 C CD1  . PHE   B 1 55  ? 21.843  13.53  25.482  1   46.643 ? 67  PHE   B CD1  1 ? 2 
ATOM   2671 C CD2  . PHE   B 1 55  ? 21.382  11.775 27.047  1   46.697 ? 67  PHE   B CD2  1 ? 2 
ATOM   2672 C CE1  . PHE   B 1 55  ? 21.915  14.442 26.53   1   48.038 ? 67  PHE   B CE1  1 ? 2 
ATOM   2673 C CE2  . PHE   B 1 55  ? 21.443  12.693 28.09   1   48.41  ? 67  PHE   B CE2  1 ? 2 
ATOM   2674 C CZ   . PHE   B 1 55  ? 21.706  14.022 27.829  1   48.041 ? 67  PHE   B CZ   1 ? 2 
ATOM   2675 H H    . PHE   B 1 55  ? 20.951  9.694  22.682  1   44.121 ? 67  PHE   B H    1 c 2 
ATOM   2676 H HA   . PHE   B 1 55  ? 19.397  11.059 24.56   1   38.969 ? 67  PHE   B HA   1 c 2 
ATOM   2677 H HB2  . PHE   B 1 55  ? 21.684  10.301 24.927  1   43.309 ? 67  PHE   B HB2  1 c 2 
ATOM   2678 H HB3  . PHE   B 1 55  ? 22.159  11.427 23.915  1   44.108 ? 67  PHE   B HB3  1 c 2 
ATOM   2679 H HD1  . PHE   B 1 55  ? 21.97   13.825 24.594  1   46.696 ? 67  PHE   B HD1  1 c 2 
ATOM   2680 H HD2  . PHE   B 1 55  ? 21.184  10.87  27.229  1   45.999 ? 67  PHE   B HD2  1 c 2 
ATOM   2681 H HE1  . PHE   B 1 55  ? 22.097  15.351 26.352  1   48.744 ? 67  PHE   B HE1  1 c 2 
ATOM   2682 H HE2  . PHE   B 1 55  ? 21.313  12.404 28.979  1   48.231 ? 67  PHE   B HE2  1 c 2 
ATOM   2683 H HZ   . PHE   B 1 55  ? 21.768  14.638 28.54   1   49.176 ? 67  PHE   B HZ   1 c 2 
ATOM   2684 N N    . ASP   B 1 56  ? 18.994  13.288 23.441  1   34.19  ? 68  ASP   B N    1 ? 2 
ATOM   2685 C CA   . ASP   B 1 56  ? 18.616  14.455 22.658  1   35.83  ? 68  ASP   B CA   1 ? 2 
ATOM   2686 C C    . ASP   B 1 56  ? 18.658  15.715 23.527  1   38.528 ? 68  ASP   B C    1 ? 2 
ATOM   2687 O O    . ASP   B 1 56  ? 18.108  15.719 24.617  1   37.792 ? 68  ASP   B O    1 ? 2 
ATOM   2688 C CB   . ASP   B 1 56  ? 17.213  14.3   22.083  1   32.371 ? 68  ASP   B CB   1 ? 2 
ATOM   2689 C CG   . ASP   B 1 56  ? 16.634  15.555 21.44   1   32.763 ? 68  ASP   B CG   1 ? 2 
ATOM   2690 O OD1  . ASP   B 1 56  ? 17.369  16.302 20.748  1   35.882 ? 68  ASP   B OD1  1 ? 2 
ATOM   2691 O OD2  . ASP   B 1 56  ? 15.441  15.783 21.617  1   33.322 ? 68  ASP   B OD2  1 ? 2 
ATOM   2692 H H    . ASP   B 1 56  ? 18.629  13.187 24.273  1   34.664 ? 68  ASP   B H    1 c 2 
ATOM   2693 H HA   . ASP   B 1 56  ? 19.252  14.558 21.916  1   36.843 ? 68  ASP   B HA   1 c 2 
ATOM   2694 H HB2  . ASP   B 1 56  ? 17.229  13.59  21.407  1   32.601 ? 68  ASP   B HB2  1 c 2 
ATOM   2695 H HB3  . ASP   B 1 56  ? 16.61   14.017 22.802  1   31.68  ? 68  ASP   B HB3  1 c 2 
ATOM   2696 N N    . SER   B 1 57  ? 19.24   16.804 23.011  1   45.107 ? 69  SER   B N    1 ? 2 
ATOM   2697 C CA   . SER   B 1 57  ? 19.328  18.046 23.772  1   51.486 ? 69  SER   B CA   1 ? 2 
ATOM   2698 C C    . SER   B 1 57  ? 18.912  19.276 22.959  1   52.475 ? 69  SER   B C    1 ? 2 
ATOM   2699 O O    . SER   B 1 57  ? 19.505  19.547 21.912  1   50.659 ? 69  SER   B O    1 ? 2 
ATOM   2700 C CB   . SER   B 1 57  ? 20.715  18.25  24.295  1   55.233 ? 69  SER   B CB   1 ? 2 
ATOM   2701 O OG   . SER   B 1 57  ? 20.673  19.271 25.283  1   61.345 ? 69  SER   B OG   1 ? 2 
ATOM   2702 H H    . SER   B 1 57  ? 19.59   16.776 22.167  1   45.482 ? 69  SER   B H    1 c 2 
ATOM   2703 H HA   . SER   B 1 57  ? 18.717  17.975 24.548  1   49.47  ? 69  SER   B HA   1 c 2 
ATOM   2704 H HB2  . SER   B 1 57  ? 21.045  17.42  24.689  1   56.042 ? 69  SER   B HB2  1 c 2 
ATOM   2705 H HB3  . SER   B 1 57  ? 21.309  18.513 23.568  1   57.534 ? 69  SER   B HB3  1 c 2 
ATOM   2706 H HG   . SER   B 1 57  ? 21.489  19.443 25.44   0   30     ? 69  SER   B HG   1 c 2 
ATOM   2707 N N    . SER   B 1 58  ? 17.912  20.027 23.469  1   49.768 ? 70  SER   B N    1 ? 2 
ATOM   2708 C CA   . SER   B 1 58  ? 17.644  21.383 23.004  1   49.881 ? 70  SER   B CA   1 ? 2 
ATOM   2709 C C    . SER   B 1 58  ? 18.877  22.256 23.218  1   54.134 ? 70  SER   B C    1 ? 2 
ATOM   2710 O O    . SER   B 1 58  ? 19.16   23.12  22.387  1   54.628 ? 70  SER   B O    1 ? 2 
ATOM   2711 C CB   . SER   B 1 58  ? 16.471  22.019 23.706  1   48.771 ? 70  SER   B CB   1 ? 2 
ATOM   2712 O OG   . SER   B 1 58  ? 16.855  22.476 25.003  1   48.94  ? 70  SER   B OG   1 ? 2 
ATOM   2713 H H    . SER   B 1 58  ? 17.38   19.676 24.124  1   48.652 ? 70  SER   B H    1 c 2 
ATOM   2714 H HA   . SER   B 1 58  ? 17.45   21.347 22.032  1   50.193 ? 70  SER   B HA   1 c 2 
ATOM   2715 H HB2  . SER   B 1 58  ? 16.145  22.772 23.177  1   49.119 ? 70  SER   B HB2  1 c 2 
ATOM   2716 H HB3  . SER   B 1 58  ? 15.751  21.368 23.789  1   46.531 ? 70  SER   B HB3  1 c 2 
ATOM   2717 H HG   . SER   B 1 58  ? 16.263  22.846 25.376  0   30     ? 70  SER   B HG   1 c 2 
ATOM   2718 N N    . HIS   B 1 59  ? 19.588  22.046 24.34   1   56.341 ? 71  HIS   B N    1 ? 2 
ATOM   2719 C CA   . HIS   B 1 59  ? 20.806  22.807 24.628  1   66.604 ? 71  HIS   B CA   1 ? 2 
ATOM   2720 C C    . HIS   B 1 59  ? 21.783  22.715 23.451  1   68.133 ? 71  HIS   B C    1 ? 2 
ATOM   2721 O O    . HIS   B 1 59  ? 22.404  23.713 23.089  1   73.006 ? 71  HIS   B O    1 ? 2 
ATOM   2722 C CB   . HIS   B 1 59  ? 21.488  22.341 25.925  1   70.661 ? 71  HIS   B CB   1 ? 2 
ATOM   2723 C CG   . HIS   B 1 59  ? 20.702  22.578 27.175  1   78.137 ? 71  HIS   B CG   1 ? 2 
ATOM   2724 N ND1  . HIS   B 1 59  ? 20.498  23.853 27.66   1   83.447 ? 71  HIS   B ND1  1 ? 2 
ATOM   2725 C CD2  . HIS   B 1 59  ? 20.069  21.748 28.024  1   78.648 ? 71  HIS   B CD2  1 ? 2 
ATOM   2726 C CE1  . HIS   B 1 59  ? 19.767  23.795 28.767  1   80.372 ? 71  HIS   B CE1  1 ? 2 
ATOM   2727 N NE2  . HIS   B 1 59  ? 19.49   22.527 29.006  1   80.926 ? 71  HIS   B NE2  1 ? 2 
ATOM   2728 H H    . HIS   B 1 59  ? 19.306  21.42  24.944  1   56.207 ? 71  HIS   B H    1 c 2 
ATOM   2729 H HA   . HIS   B 1 59  ? 20.545  23.754 24.738  1   66.505 ? 71  HIS   B HA   1 c 2 
ATOM   2730 H HB2  . HIS   B 1 59  ? 21.681  21.383 25.849  1   70.785 ? 71  HIS   B HB2  1 c 2 
ATOM   2731 H HB3  . HIS   B 1 59  ? 22.351  22.802 26.004  1   74.185 ? 71  HIS   B HB3  1 c 2 
ATOM   2732 H HD1  . HIS   B 1 59  ? 20.54   24.56  27.375  0   30     ? 71  HIS   B HD1  1 c 2 
ATOM   2733 H HD2  . HIS   B 1 59  ? 20.02   20.814 27.964  1   77.167 ? 71  HIS   B HD2  1 c 2 
ATOM   2734 H HE1  . HIS   B 1 59  ? 19.493  24.53  29.289  1   82.282 ? 71  HIS   B HE1  1 c 2 
ATOM   2735 H HE2  . HIS   B 1 59  ? 19.215  22.042 29.944  0   30     ? 71  HIS   B HE2  1 c 2 
ATOM   2736 N N    . ASP   B 1 60  ? 21.878  21.518 22.837  1   68.56  ? 72  ASP   B N    1 ? 2 
ATOM   2737 C CA   . ASP   B 1 60  ? 22.778  21.264 21.716  1   72.027 ? 72  ASP   B CA   1 ? 2 
ATOM   2738 C C    . ASP   B 1 60  ? 22.104  21.631 20.387  1   71.785 ? 72  ASP   B C    1 ? 2 
ATOM   2739 O O    . ASP   B 1 60  ? 22.308  20.976 19.364  1   76.874 ? 72  ASP   B O    1 ? 2 
ATOM   2740 C CB   . ASP   B 1 60  ? 23.305  19.832 21.74   1   70.246 ? 72  ASP   B CB   1 ? 2 
ATOM   2741 H H    . ASP   B 1 60  ? 21.361  20.829 23.141  1   66.229 ? 72  ASP   B H    1 c 2 
ATOM   2742 H HA   . ASP   B 1 60  ? 23.565  21.844 21.824  1   74.005 ? 72  ASP   B HA   1 c 2 
ATOM   2743 H HB2  . ASP   B 1 60  ? 24.59   20.324 21.961  0   30     ? 72  ASP   B HB2  1 c 2 
ATOM   2744 H HB3  . ASP   B 1 60  ? 22.989  19.393 22.064  0   30     ? 72  ASP   B HB3  1 c 2 
ATOM   2745 N N    . ARG   B 1 61  ? 21.249  22.655 20.421  1   70.515 ? 73  ARG   B N    1 ? 2 
ATOM   2746 C CA   . ARG   B 1 61  ? 20.83   23.401 19.245  1   71.409 ? 73  ARG   B CA   1 ? 2 
ATOM   2747 C C    . ARG   B 1 61  ? 20.867  24.906 19.547  1   72.1   ? 73  ARG   B C    1 ? 2 
ATOM   2748 O O    . ARG   B 1 61  ? 20.612  25.717 18.654  1   72.195 ? 73  ARG   B O    1 ? 2 
ATOM   2749 C CB   . ARG   B 1 61  ? 19.44   22.903 18.825  1   69.185 ? 73  ARG   B CB   1 ? 2 
ATOM   2750 H H    . ARG   B 1 61  ? 20.858  22.862 21.218  1   69.717 ? 73  ARG   B H    1 c 2 
ATOM   2751 H HA   . ARG   B 1 61  ? 21.469  23.214 18.511  1   72.796 ? 73  ARG   B HA   1 c 2 
ATOM   2752 H HB2  . ARG   B 1 61  ? 19.794  21.971 18.197  0   30     ? 73  ARG   B HB2  1 c 2 
ATOM   2753 H HB3  . ARG   B 1 61  ? 18.842  23.253 19.149  0   30     ? 73  ARG   B HB3  1 c 2 
ATOM   2754 N N    . ASN   B 1 62  ? 21.146  25.263 20.818  1   69.736 ? 74  ASN   B N    1 ? 2 
ATOM   2755 C CA   . ASN   B 1 62  ? 21.414  26.622 21.28   1   71.983 ? 74  ASN   B CA   1 ? 2 
ATOM   2756 C C    . ASN   B 1 62  ? 20.13   27.347 21.685  1   69.103 ? 74  ASN   B C    1 ? 2 
ATOM   2757 O O    . ASN   B 1 62  ? 20.216  28.354 22.375  1   72.018 ? 74  ASN   B O    1 ? 2 
ATOM   2758 C CB   . ASN   B 1 62  ? 22.245  27.46  20.301  1   75.245 ? 74  ASN   B CB   1 ? 2 
ATOM   2759 H H    . ASN   B 1 62  ? 21.16   24.604 21.449  1   68.959 ? 74  ASN   B H    1 c 2 
ATOM   2760 H HA   . ASN   B 1 62  ? 21.957  26.539 22.096  1   72.35  ? 74  ASN   B HA   1 c 2 
ATOM   2761 H HB2  . ASN   B 1 62  ? 23.154  27.441 20.364  0   30     ? 74  ASN   B HB2  1 c 2 
ATOM   2762 H HB3  . ASN   B 1 62  ? 21.548  28.047 19.68   0   30     ? 74  ASN   B HB3  1 c 2 
ATOM   2763 N N    . GLU   B 1 63  ? 18.942  26.838 21.305  1   63.9   ? 75  GLU   B N    1 ? 2 
ATOM   2764 C CA   . GLU   B 1 63  ? 17.737  27.655 21.303  1   62.166 ? 75  GLU   B CA   1 ? 2 
ATOM   2765 C C    . GLU   B 1 63  ? 16.564  26.882 21.911  1   54.565 ? 75  GLU   B C    1 ? 2 
ATOM   2766 O O    . GLU   B 1 63  ? 16.487  25.655 21.814  1   47.692 ? 75  GLU   B O    1 ? 2 
ATOM   2767 C CB   . GLU   B 1 63  ? 17.407  28.178 19.902  1   67.384 ? 75  GLU   B CB   1 ? 2 
ATOM   2768 C CG   . GLU   B 1 63  ? 16.557  27.247 19.032  1   67.781 ? 75  GLU   B CG   1 ? 2 
ATOM   2769 C CD   . GLU   B 1 63  ? 16.31   27.716 17.596  1   72.799 ? 75  GLU   B CD   1 ? 2 
ATOM   2770 O OE1  . GLU   B 1 63  ? 15.389  27.186 16.931  1   68.88  ? 75  GLU   B OE1  1 ? 2 
ATOM   2771 O OE2  . GLU   B 1 63  ? 17.049  28.61  17.12   1   80.86  ? 75  GLU   B OE2  1 ? 2 
ATOM   2772 H H    . GLU   B 1 63  ? 18.88   25.961 21.057  1   62.55  ? 75  GLU   B H    1 c 2 
ATOM   2773 H HA   . GLU   B 1 63  ? 17.91   28.443 21.873  1   63.798 ? 75  GLU   B HA   1 c 2 
ATOM   2774 H HB2  . GLU   B 1 63  ? 16.933  29.031 19.992  1   68.02  ? 75  GLU   B HB2  1 c 2 
ATOM   2775 H HB3  . GLU   B 1 63  ? 18.248  28.355 19.432  1   69.289 ? 75  GLU   B HB3  1 c 2 
ATOM   2776 H HG2  . GLU   B 1 63  ? 16.99   26.367 18.996  1   66.811 ? 75  GLU   B HG2  1 c 2 
ATOM   2777 H HG3  . GLU   B 1 63  ? 15.685  27.122 19.462  1   65.824 ? 75  GLU   B HG3  1 c 2 
ATOM   2778 N N    . PRO   B 1 64  ? 15.618  27.581 22.579  1   51.749 ? 76  PRO   B N    1 ? 2 
ATOM   2779 C CA   . PRO   B 1 64  ? 14.548  26.889 23.272  1   48.542 ? 76  PRO   B CA   1 ? 2 
ATOM   2780 C C    . PRO   B 1 64  ? 13.624  26.157 22.311  1   43.31  ? 76  PRO   B C    1 ? 2 
ATOM   2781 O O    . PRO   B 1 64  ? 13.519  26.548 21.147  1   45.426 ? 76  PRO   B O    1 ? 2 
ATOM   2782 C CB   . PRO   B 1 64  ? 13.783  27.981 24.013  1   49.691 ? 76  PRO   B CB   1 ? 2 
ATOM   2783 C CG   . PRO   B 1 64  ? 14.521  29.274 23.759  1   53.303 ? 76  PRO   B CG   1 ? 2 
ATOM   2784 C CD   . PRO   B 1 64  ? 15.537  29.045 22.681  1   55.233 ? 76  PRO   B CD   1 ? 2 
ATOM   2785 H HA   . PRO   B 1 64  ? 14.93   26.255 23.914  1   47.235 ? 76  PRO   B HA   1 c 2 
ATOM   2786 H HB2  . PRO   B 1 64  ? 12.864  28.042 23.685  1   48.628 ? 76  PRO   B HB2  1 c 2 
ATOM   2787 H HB3  . PRO   B 1 64  ? 13.751  27.786 24.968  1   49.081 ? 76  PRO   B HB3  1 c 2 
ATOM   2788 H HG2  . PRO   B 1 64  ? 13.894  29.971 23.481  1   54.071 ? 76  PRO   B HG2  1 c 2 
ATOM   2789 H HG3  . PRO   B 1 64  ? 14.966  29.574 24.577  1   54.505 ? 76  PRO   B HG3  1 c 2 
ATOM   2790 H HD2  . PRO   B 1 64  ? 15.248  29.435 21.833  1   55.695 ? 76  PRO   B HD2  1 c 2 
ATOM   2791 H HD3  . PRO   B 1 64  ? 16.401  29.424 22.931  1   57.033 ? 76  PRO   B HD3  1 c 2 
ATOM   2792 N N    . PHE   B 1 65  ? 13.016  25.083 22.824  1   39.401 ? 77  PHE   B N    1 ? 2 
ATOM   2793 C CA   . PHE   B 1 65  ? 11.938  24.372 22.154  1   37.523 ? 77  PHE   B CA   1 ? 2 
ATOM   2794 C C    . PHE   B 1 65  ? 10.638  25.101 22.479  1   36.895 ? 77  PHE   B C    1 ? 2 
ATOM   2795 O O    . PHE   B 1 65  ? 10.377  25.423 23.646  1   36.741 ? 77  PHE   B O    1 ? 2 
ATOM   2796 C CB   . PHE   B 1 65  ? 11.91   22.91  22.607  1   35.161 ? 77  PHE   B CB   1 ? 2 
ATOM   2797 C CG   . PHE   B 1 65  ? 10.854  22.062 21.921  1   33.369 ? 77  PHE   B CG   1 ? 2 
ATOM   2798 C CD1  . PHE   B 1 65  ? 11.142  21.422 20.725  1   33.897 ? 77  PHE   B CD1  1 ? 2 
ATOM   2799 C CD2  . PHE   B 1 65  ? 9.577   21.913 22.455  1   32.007 ? 77  PHE   B CD2  1 ? 2 
ATOM   2800 C CE1  . PHE   B 1 65  ? 10.184  20.632 20.093  1   32.47  ? 77  PHE   B CE1  1 ? 2 
ATOM   2801 C CE2  . PHE   B 1 65  ? 8.614   21.142 21.802  1   31.121 ? 77  PHE   B CE2  1 ? 2 
ATOM   2802 C CZ   . PHE   B 1 65  ? 8.92    20.511 20.62   1   31.342 ? 77  PHE   B CZ   1 ? 2 
ATOM   2803 H H    . PHE   B 1 65  ? 13.29   24.776 23.641  1   39.384 ? 77  PHE   B H    1 c 2 
ATOM   2804 H HA   . PHE   B 1 65  ? 12.095  24.402 21.173  1   38.215 ? 77  PHE   B HA   1 c 2 
ATOM   2805 H HB2  . PHE   B 1 65  ? 12.794  22.515 22.437  1   35.626 ? 77  PHE   B HB2  1 c 2 
ATOM   2806 H HB3  . PHE   B 1 65  ? 11.753  22.887 23.577  1   34.719 ? 77  PHE   B HB3  1 c 2 
ATOM   2807 H HD1  . PHE   B 1 65  ? 12.005  21.502 20.35   1   34.858 ? 77  PHE   B HD1  1 c 2 
ATOM   2808 H HD2  . PHE   B 1 65  ? 9.356   22.352 23.261  1   32.171 ? 77  PHE   B HD2  1 c 2 
ATOM   2809 H HE1  . PHE   B 1 65  ? 10.395  20.206 19.277  1   32.824 ? 77  PHE   B HE1  1 c 2 
ATOM   2810 H HE2  . PHE   B 1 65  ? 7.753   21.05  22.177  1   30.309 ? 77  PHE   B HE2  1 c 2 
ATOM   2811 H HZ   . PHE   B 1 65  ? 8.274   19.978 20.185  1   30.658 ? 77  PHE   B HZ   1 c 2 
ATOM   2812 N N    . VAL   B 1 66  ? 9.884   25.421 21.427  1   38.463 ? 78  VAL   B N    1 ? 2 
ATOM   2813 C CA   . VAL   B 1 66  ? 8.721   26.287 21.552  1   39.897 ? 78  VAL   B CA   1 ? 2 
ATOM   2814 C C    . VAL   B 1 66  ? 7.512   25.567 20.975  1   37.661 ? 78  VAL   B C    1 ? 2 
ATOM   2815 O O    . VAL   B 1 66  ? 7.583   25.037 19.871  1   37.678 ? 78  VAL   B O    1 ? 2 
ATOM   2816 C CB   . VAL   B 1 66  ? 8.967   27.625 20.842  1   43.836 ? 78  VAL   B CB   1 ? 2 
ATOM   2817 C CG1  . VAL   B 1 66  ? 7.761   28.543 20.941  1   44.742 ? 78  VAL   B CG1  1 ? 2 
ATOM   2818 C CG2  . VAL   B 1 66  ? 10.226  28.312 21.37   1   46.68  ? 78  VAL   B CG2  1 ? 2 
ATOM   2819 H H    . VAL   B 1 66  ? 10.096  25.088 20.603  1   38.54  ? 78  VAL   B H    1 c 2 
ATOM   2820 H HA   . VAL   B 1 66  ? 8.562   26.461 22.496  1   39.373 ? 78  VAL   B HA   1 c 2 
ATOM   2821 H HB   . VAL   B 1 66  ? 9.113   27.424 19.888  1   44.297 ? 78  VAL   B HB   1 c 2 
ATOM   2822 H HG11 . VAL   B 1 66  ? 7.438   28.558 21.858  1   43.933 ? 78  VAL   B HG11 1 c 2 
ATOM   2823 H HG12 . VAL   B 1 66  ? 7.055   28.219 20.355  1   44.128 ? 78  VAL   B HG12 1 c 2 
ATOM   2824 H HG13 . VAL   B 1 66  ? 8.013   29.443 20.672  1   46.801 ? 78  VAL   B HG13 1 c 2 
ATOM   2825 H HG21 . VAL   B 1 66  ? 10.282  29.212 21.009  1   48.433 ? 78  VAL   B HG21 1 c 2 
ATOM   2826 H HG22 . VAL   B 1 66  ? 11.011  27.806 21.098  1   46.36  ? 78  VAL   B HG22 1 c 2 
ATOM   2827 H HG23 . VAL   B 1 66  ? 10.19   28.355 22.341  1   45.915 ? 78  VAL   B HG23 1 c 2 
ATOM   2828 N N    . PHE   B 1 67  ? 6.395   25.572 21.721  1   36.517 ? 79  PHE   B N    1 ? 2 
ATOM   2829 C CA   . PHE   B 1 67  ? 5.184   24.894 21.273  1   34.245 ? 79  PHE   B CA   1 ? 2 
ATOM   2830 C C    . PHE   B 1 67  ? 3.974   25.487 21.99   1   33.8   ? 79  PHE   B C    1 ? 2 
ATOM   2831 O O    . PHE   B 1 67  ? 4.116   26.149 23.018  1   33.099 ? 79  PHE   B O    1 ? 2 
ATOM   2832 C CB   . PHE   B 1 67  ? 5.314   23.379 21.481  1   31.607 ? 79  PHE   B CB   1 ? 2 
ATOM   2833 C CG   . PHE   B 1 67  ? 5.155   22.924 22.927  1   30.888 ? 79  PHE   B CG   1 ? 2 
ATOM   2834 C CD1  . PHE   B 1 67  ? 6.191   23.065 23.845  1   29.996 ? 79  PHE   B CD1  1 ? 2 
ATOM   2835 C CD2  . PHE   B 1 67  ? 3.959   22.368 23.37   1   29.606 ? 79  PHE   B CD2  1 ? 2 
ATOM   2836 C CE1  . PHE   B 1 67  ? 6.037   22.67  25.159  1   29.364 ? 79  PHE   B CE1  1 ? 2 
ATOM   2837 C CE2  . PHE   B 1 67  ? 3.804   21.994 24.695  1   28.507 ? 79  PHE   B CE2  1 ? 2 
ATOM   2838 C CZ   . PHE   B 1 67  ? 4.85    22.123 25.583  1   28.539 ? 79  PHE   B CZ   1 ? 2 
ATOM   2839 H H    . PHE   B 1 67  ? 6.388   26.007 22.525  1   36.532 ? 79  PHE   B H    1 c 2 
ATOM   2840 H HA   . PHE   B 1 67  ? 5.078   25.063 20.299  1   35.168 ? 79  PHE   B HA   1 c 2 
ATOM   2841 H HB2  . PHE   B 1 67  ? 4.633   22.93  20.932  1   31.496 ? 79  PHE   B HB2  1 c 2 
ATOM   2842 H HB3  . PHE   B 1 67  ? 6.196   23.093 21.155  1   31.987 ? 79  PHE   B HB3  1 c 2 
ATOM   2843 H HD1  . PHE   B 1 67  ? 7.011   23.438 23.564  1   31.179 ? 79  PHE   B HD1  1 c 2 
ATOM   2844 H HD2  . PHE   B 1 67  ? 3.236   22.278 22.77   1   29.635 ? 79  PHE   B HD2  1 c 2 
ATOM   2845 H HE1  . PHE   B 1 67  ? 6.753   22.768 25.766  1   29.787 ? 79  PHE   B HE1  1 c 2 
ATOM   2846 H HE2  . PHE   B 1 67  ? 2.991   21.61  24.981  1   28.043 ? 79  PHE   B HE2  1 c 2 
ATOM   2847 H HZ   . PHE   B 1 67  ? 4.746   21.853 26.482  1   28.27  ? 79  PHE   B HZ   1 c 2 
ATOM   2848 N N    . SER   B 1 68  ? 2.791   25.262 21.409  1   33.696 ? 80  SER   B N    1 ? 2 
ATOM   2849 C CA   . SER   B 1 68  ? 1.529   25.679 22.013  1   34.968 ? 80  SER   B CA   1 ? 2 
ATOM   2850 C C    . SER   B 1 68  ? 0.987   24.536 22.86   1   32.025 ? 80  SER   B C    1 ? 2 
ATOM   2851 O O    . SER   B 1 68  ? 0.731   23.447 22.341  1   31.092 ? 80  SER   B O    1 ? 2 
ATOM   2852 C CB   . SER   B 1 68  ? 0.491   26.077 20.999  1   35.657 ? 80  SER   B CB   1 ? 2 
ATOM   2853 O OG   . SER   B 1 68  ? 0.822   27.304 20.392  1   39.381 ? 80  SER   B OG   1 ? 2 
ATOM   2854 H H    . SER   B 1 68  ? 2.768   24.832 20.603  1   33.905 ? 80  SER   B H    1 c 2 
ATOM   2855 H HA   . SER   B 1 68  ? 1.705   26.454 22.601  1   35.198 ? 80  SER   B HA   1 c 2 
ATOM   2856 H HB2  . SER   B 1 68  ? 0.425   25.384 20.316  1   35.714 ? 80  SER   B HB2  1 c 2 
ATOM   2857 H HB3  . SER   B 1 68  ? -0.377  26.156 21.439  1   36.154 ? 80  SER   B HB3  1 c 2 
ATOM   2858 H HG   . SER   B 1 68  ? 0.158   27.467 19.914  0   30     ? 80  SER   B HG   1 c 2 
ATOM   2859 N N    . LEU   B 1 69  ? 0.726   24.831 24.134  1   32.327 ? 81  LEU   B N    1 ? 2 
ATOM   2860 C CA   . LEU   B 1 69  ? 0.354   23.796 25.078  1   30.836 ? 81  LEU   B CA   1 ? 2 
ATOM   2861 C C    . LEU   B 1 69  ? -1.041  23.24  24.786  1   29.572 ? 81  LEU   B C    1 ? 2 
ATOM   2862 O O    . LEU   B 1 69  ? -1.982  23.97  24.469  1   30.224 ? 81  LEU   B O    1 ? 2 
ATOM   2863 C CB   . LEU   B 1 69  ? 0.423   24.385 26.48   1   35.244 ? 81  LEU   B CB   1 ? 2 
ATOM   2864 C CG   . LEU   B 1 69  ? 0.141   23.397 27.615  1   37.521 ? 81  LEU   B CG   1 ? 2 
ATOM   2865 C CD1  . LEU   B 1 69  ? 1.243   22.356 27.713  1   38.745 ? 81  LEU   B CD1  1 ? 2 
ATOM   2866 C CD2  . LEU   B 1 69  ? -0.034  24.204 28.875  1   40.912 ? 81  LEU   B CD2  1 ? 2 
ATOM   2867 H H    . LEU   B 1 69  ? 0.776   25.697 24.421  1   33.306 ? 81  LEU   B H    1 c 2 
ATOM   2868 H HA   . LEU   B 1 69  ? 1.013   23.06  25.002  1   30.405 ? 81  LEU   B HA   1 c 2 
ATOM   2869 H HB2  . LEU   B 1 69  ? 1.323   24.763 26.612  1   35.354 ? 81  LEU   B HB2  1 c 2 
ATOM   2870 H HB3  . LEU   B 1 69  ? -0.228  25.122 26.537  1   36.06  ? 81  LEU   B HB3  1 c 2 
ATOM   2871 H HG   . LEU   B 1 69  ? -0.714  22.932 27.424  1   37.325 ? 81  LEU   B HG   1 c 2 
ATOM   2872 H HD11 . LEU   B 1 69  ? 1.202   21.766 26.942  1   37.203 ? 81  LEU   B HD11 1 c 2 
ATOM   2873 H HD12 . LEU   B 1 69  ? 1.126   21.835 28.525  1   37.689 ? 81  LEU   B HD12 1 c 2 
ATOM   2874 H HD13 . LEU   B 1 69  ? 2.108   22.799 27.736  1   38.332 ? 81  LEU   B HD13 1 c 2 
ATOM   2875 H HD21 . LEU   B 1 69  ? -0.814  24.777 28.789  1   40.951 ? 81  LEU   B HD21 1 c 2 
ATOM   2876 H HD22 . LEU   B 1 69  ? 0.755   24.751 29.022  1   40.671 ? 81  LEU   B HD22 1 c 2 
ATOM   2877 H HD23 . LEU   B 1 69  ? -0.156  23.604 29.631  1   39.832 ? 81  LEU   B HD23 1 c 2 
ATOM   2878 N N    . GLY   B 1 70  ? -1.151  21.916 24.942  1   28.346 ? 82  GLY   B N    1 ? 2 
ATOM   2879 C CA   . GLY   B 1 70  ? -2.422  21.232 24.943  1   28.929 ? 82  GLY   B CA   1 ? 2 
ATOM   2880 C C    . GLY   B 1 70  ? -3.03   21.126 23.554  1   31.983 ? 82  GLY   B C    1 ? 2 
ATOM   2881 O O    . GLY   B 1 70  ? -4.232  20.949 23.478  1   32.929 ? 82  GLY   B O    1 ? 2 
ATOM   2882 H H    . GLY   B 1 70  ? -0.391  21.421 25.055  1   27.711 ? 82  GLY   B H    1 c 2 
ATOM   2883 H HA2  . GLY   B 1 70  ? -2.299  20.329 25.316  1   28.448 ? 82  GLY   B HA2  1 c 2 
ATOM   2884 H HA3  . GLY   B 1 70  ? -3.044  21.718 25.533  1   29.96  ? 82  GLY   B HA3  1 c 2 
ATOM   2885 N N    . LYS   B 1 71  ? -2.207  21.283 22.491  1   31.334 ? 83  LYS   B N    1 ? 2 
ATOM   2886 C CA   . LYS   B 1 71  ? -2.652  21.142 21.111  1   33.685 ? 83  LYS   B CA   1 ? 2 
ATOM   2887 C C    . LYS   B 1 71  ? -2.116  19.833 20.511  1   33.142 ? 83  LYS   B C    1 ? 2 
ATOM   2888 O O    . LYS   B 1 71  ? -2.308  19.546 19.354  1   37.21  ? 83  LYS   B O    1 ? 2 
ATOM   2889 C CB   . LYS   B 1 71  ? -2.241  22.412 20.355  1   32.927 ? 83  LYS   B CB   1 ? 2 
ATOM   2890 H H    . LYS   B 1 71  ? -1.326  21.475 22.642  1   31.423 ? 83  LYS   B H    1 c 2 
ATOM   2891 H HA   . LYS   B 1 71  ? -3.642  21.098 21.108  1   33.705 ? 83  LYS   B HA   1 c 2 
ATOM   2892 H HB2  . LYS   B 1 71  ? -1.35   22.608 20.329  0   30     ? 83  LYS   B HB2  1 c 2 
ATOM   2893 H HB3  . LYS   B 1 71  ? -3.167  22.958 20.153  0   30     ? 83  LYS   B HB3  1 c 2 
ATOM   2894 N N    . GLY   B 1 72  ? -1.47   18.987 21.308  1   35.876 ? 84  GLY   B N    1 ? 2 
ATOM   2895 C CA   . GLY   B 1 72  ? -0.843  17.778 20.791  1   36.318 ? 84  GLY   B CA   1 ? 2 
ATOM   2896 C C    . GLY   B 1 72  ? 0.236   18.063 19.735  1   35.297 ? 84  GLY   B C    1 ? 2 
ATOM   2897 O O    . GLY   B 1 72  ? 0.486   17.204 18.903  1   34.885 ? 84  GLY   B O    1 ? 2 
ATOM   2898 H H    . GLY   B 1 72  ? -1.418  19.158 22.204  1   34.473 ? 84  GLY   B H    1 c 2 
ATOM   2899 H HA2  . GLY   B 1 72  ? -0.439  17.285 21.543  1   34.783 ? 84  GLY   B HA2  1 c 2 
ATOM   2900 H HA3  . GLY   B 1 72  ? -1.54   17.203 20.396  1   36.053 ? 84  GLY   B HA3  1 c 2 
ATOM   2901 N N    . GLN   B 1 73  ? 0.945   19.208 19.853  1   31.179 ? 85  GLN   B N    1 ? 2 
ATOM   2902 C CA   . GLN   B 1 73  ? 2.183   19.456 19.123  1   28.624 ? 85  GLN   B CA   1 ? 2 
ATOM   2903 C C    . GLN   B 1 73  ? 3.335   18.65  19.719  1   26.92  ? 85  GLN   B C    1 ? 2 
ATOM   2904 O O    . GLN   B 1 73  ? 4.414   18.573 19.135  1   25.704 ? 85  GLN   B O    1 ? 2 
ATOM   2905 C CB   . GLN   B 1 73  ? 2.534   20.942 19.143  1   30.097 ? 85  GLN   B CB   1 ? 2 
ATOM   2906 C CG   . GLN   B 1 73  ? 1.602   21.808 18.316  1   31.874 ? 85  GLN   B CG   1 ? 2 
ATOM   2907 C CD   . GLN   B 1 73  ? 1.843   23.286 18.514  1   33.973 ? 85  GLN   B CD   1 ? 2 
ATOM   2908 O OE1  . GLN   B 1 73  ? 2.802   23.711 19.164  1   34.341 ? 85  GLN   B OE1  1 ? 2 
ATOM   2909 N NE2  . GLN   B 1 73  ? 0.915   24.091 18.022  1   36.237 ? 85  GLN   B NE2  1 ? 2 
ATOM   2910 H H    . GLN   B 1 73  ? 0.643   19.857 20.421  1   31.606 ? 85  GLN   B H    1 c 2 
ATOM   2911 H HA   . GLN   B 1 73  ? 2.052   19.173 18.182  1   29.868 ? 85  GLN   B HA   1 c 2 
ATOM   2912 H HB2  . GLN   B 1 73  ? 2.517   21.254 20.072  1   29.605 ? 85  GLN   B HB2  1 c 2 
ATOM   2913 H HB3  . GLN   B 1 73  ? 3.448   21.054 18.809  1   30.394 ? 85  GLN   B HB3  1 c 2 
ATOM   2914 H HG2  . GLN   B 1 73  ? 1.719   21.593 17.366  1   32.81  ? 85  GLN   B HG2  1 c 2 
ATOM   2915 H HG3  . GLN   B 1 73  ? 0.673   21.604 18.556  1   31.824 ? 85  GLN   B HG3  1 c 2 
ATOM   2916 H HE21 . GLN   B 1 73  ? 1.045   24.968 18.025  1   37.231 ? 85  GLN   B HE21 1 c 2 
ATOM   2917 H HE22 . GLN   B 1 73  ? 0.163   23.755 17.691  1   36.212 ? 85  GLN   B HE22 1 c 2 
ATOM   2918 N N    . VAL   B 1 74  ? 3.109   18.109 20.922  1   23.81  ? 86  VAL   B N    1 ? 2 
ATOM   2919 C CA   . VAL   B 1 74  ? 4.06    17.251 21.599  1   23.9   ? 86  VAL   B CA   1 ? 2 
ATOM   2920 C C    . VAL   B 1 74  ? 3.313   16.001 22.068  1   21.784 ? 86  VAL   B C    1 ? 2 
ATOM   2921 O O    . VAL   B 1 74  ? 2.094   15.923 21.971  1   23.281 ? 86  VAL   B O    1 ? 2 
ATOM   2922 C CB   . VAL   B 1 74  ? 4.682   18.03  22.767  1   25.058 ? 86  VAL   B CB   1 ? 2 
ATOM   2923 C CG1  . VAL   B 1 74  ? 5.597   19.152 22.306  1   26.068 ? 86  VAL   B CG1  1 ? 2 
ATOM   2924 C CG2  . VAL   B 1 74  ? 3.585   18.583 23.687  1   26.28  ? 86  VAL   B CG2  1 ? 2 
ATOM   2925 H H    . VAL   B 1 74  ? 2.319   18.29  21.343  1   24.559 ? 86  VAL   B H    1 c 2 
ATOM   2926 H HA   . VAL   B 1 74  ? 4.763   16.991 20.973  1   23.867 ? 86  VAL   B HA   1 c 2 
ATOM   2927 H HB   . VAL   B 1 74  ? 5.222   17.391 23.288  1   24.56  ? 86  VAL   B HB   1 c 2 
ATOM   2928 H HG11 . VAL   B 1 74  ? 5.084   19.8   21.794  1   26.761 ? 86  VAL   B HG11 1 c 2 
ATOM   2929 H HG12 . VAL   B 1 74  ? 6.304   18.786 21.748  1   26.25  ? 86  VAL   B HG12 1 c 2 
ATOM   2930 H HG13 . VAL   B 1 74  ? 5.99    19.589 23.08   1   26.295 ? 86  VAL   B HG13 1 c 2 
ATOM   2931 H HG21 . VAL   B 1 74  ? 3.993   18.978 24.475  1   26.044 ? 86  VAL   B HG21 1 c 2 
ATOM   2932 H HG22 . VAL   B 1 74  ? 2.992   17.863 23.96   1   25.382 ? 86  VAL   B HG22 1 c 2 
ATOM   2933 H HG23 . VAL   B 1 74  ? 3.075   19.262 23.216  1   26.495 ? 86  VAL   B HG23 1 c 2 
ATOM   2934 N N    . ILE   B 1 75  ? 4.059   15.002 22.497  1   19.802 ? 87  ILE   B N    1 ? 2 
ATOM   2935 C CA   . ILE   B 1 75  ? 3.505   13.782 23.059  1   21.412 ? 87  ILE   B CA   1 ? 2 
ATOM   2936 C C    . ILE   B 1 75  ? 2.639   14.152 24.271  1   21.039 ? 87  ILE   B C    1 ? 2 
ATOM   2937 O O    . ILE   B 1 75  ? 2.821   15.209 24.868  1   22.867 ? 87  ILE   B O    1 ? 2 
ATOM   2938 C CB   . ILE   B 1 75  ? 4.605   12.787 23.463  1   22.008 ? 87  ILE   B CB   1 ? 2 
ATOM   2939 C CG1  . ILE   B 1 75  ? 5.64    13.392 24.419  1   23.754 ? 87  ILE   B CG1  1 ? 2 
ATOM   2940 C CG2  . ILE   B 1 75  ? 5.285   12.186 22.244  1   24.06  ? 87  ILE   B CG2  1 ? 2 
ATOM   2941 C CD1  . ILE   B 1 75  ? 6.61    12.371 24.992  1   25.333 ? 87  ILE   B CD1  1 ? 2 
ATOM   2942 H H    . ILE   B 1 75  ? 4.967   15.076 22.424  1   20.74  ? 87  ILE   B H    1 c 2 
ATOM   2943 H HA   . ILE   B 1 75  ? 2.937   13.361 22.385  1   21.293 ? 87  ILE   B HA   1 c 2 
ATOM   2944 H HB   . ILE   B 1 75  ? 4.167   12.056 23.941  1   22.365 ? 87  ILE   B HB   1 c 2 
ATOM   2945 H HG12 . ILE   B 1 75  ? 6.152   14.075 23.94   1   23.883 ? 87  ILE   B HG12 1 c 2 
ATOM   2946 H HG13 . ILE   B 1 75  ? 5.172   13.831 25.158  1   23.66  ? 87  ILE   B HG13 1 c 2 
ATOM   2947 H HG21 . ILE   B 1 75  ? 5.811   11.414 22.511  1   23.498 ? 87  ILE   B HG21 1 c 2 
ATOM   2948 H HG22 . ILE   B 1 75  ? 5.869   12.848 21.837  1   23.777 ? 87  ILE   B HG22 1 c 2 
ATOM   2949 H HG23 . ILE   B 1 75  ? 4.613   11.909 21.599  1   23.698 ? 87  ILE   B HG23 1 c 2 
ATOM   2950 H HD11 . ILE   B 1 75  ? 6.114   11.593 25.312  1   24.776 ? 87  ILE   B HD11 1 c 2 
ATOM   2951 H HD12 . ILE   B 1 75  ? 7.101   12.77  25.735  1   25.138 ? 87  ILE   B HD12 1 c 2 
ATOM   2952 H HD13 . ILE   B 1 75  ? 7.24    12.091 24.301  1   25.01  ? 87  ILE   B HD13 1 c 2 
ATOM   2953 N N    . LYS   B 1 76  ? 1.656   13.297 24.565  1   22.049 ? 88  LYS   B N    1 ? 2 
ATOM   2954 C CA   . LYS   B 1 76  ? 0.639   13.561 25.581  1   22.203 ? 88  LYS   B CA   1 ? 2 
ATOM   2955 C C    . LYS   B 1 76  ? 1.302   13.889 26.914  1   22.263 ? 88  LYS   B C    1 ? 2 
ATOM   2956 O O    . LYS   B 1 76  ? 0.833   14.775 27.622  1   23.609 ? 88  LYS   B O    1 ? 2 
ATOM   2957 C CB   . LYS   B 1 76  ? -0.358  12.395 25.687  1   25.29  ? 88  LYS   B CB   1 ? 2 
ATOM   2958 H H    . LYS   B 1 76  ? 1.619   12.505 24.11   1   21.823 ? 88  LYS   B H    1 c 2 
ATOM   2959 H HA   . LYS   B 1 76  ? 0.129   14.36  25.293  1   22.975 ? 88  LYS   B HA   1 c 2 
ATOM   2960 H HB2  . LYS   B 1 76  ? -0.051  11.599 25.706  0   30     ? 88  LYS   B HB2  1 c 2 
ATOM   2961 H HB3  . LYS   B 1 76  ? -1.347  12.929 25.632  0   30     ? 88  LYS   B HB3  1 c 2 
ATOM   2962 N N    . ALA   B 1 77  ? 2.401   13.189 27.238  1   24.29  ? 89  ALA   B N    1 ? 2 
ATOM   2963 C CA   . ALA   B 1 77  ? 3.112   13.368 28.504  1   24.856 ? 89  ALA   B CA   1 ? 2 
ATOM   2964 C C    . ALA   B 1 77  ? 3.606   14.803 28.689  1   25.522 ? 89  ALA   B C    1 ? 2 
ATOM   2965 O O    . ALA   B 1 77  ? 3.68    15.313 29.816  1   23.812 ? 89  ALA   B O    1 ? 2 
ATOM   2966 C CB   . ALA   B 1 77  ? 4.269   12.392 28.577  1   24.883 ? 89  ALA   B CB   1 ? 2 
ATOM   2967 H H    . ALA   B 1 77  ? 2.715   12.564 26.65   1   23.539 ? 89  ALA   B H    1 c 2 
ATOM   2968 H HA   . ALA   B 1 77  ? 2.475   13.166 29.243  1   25.328 ? 89  ALA   B HA   1 c 2 
ATOM   2969 H HB1  . ALA   B 1 77  ? 3.926   11.488 28.676  1   24.993 ? 89  ALA   B HB1  1 c 2 
ATOM   2970 H HB2  . ALA   B 1 77  ? 4.798   12.448 27.763  1   24.523 ? 89  ALA   B HB2  1 c 2 
ATOM   2971 H HB3  . ALA   B 1 77  ? 4.831   12.607 29.34   1   25.332 ? 89  ALA   B HB3  1 c 2 
ATOM   2972 N N    . TRP   B 1 78  ? 3.946   15.458 27.575  1   22.753 ? 90  TRP   B N    1 ? 2 
ATOM   2973 C CA   . TRP   B 1 78  ? 4.418   16.831 27.66   1   24.463 ? 90  TRP   B CA   1 ? 2 
ATOM   2974 C C    . TRP   B 1 78  ? 3.255   17.795 27.858  1   25.044 ? 90  TRP   B C    1 ? 2 
ATOM   2975 O O    . TRP   B 1 78  ? 3.402   18.764 28.618  1   25.821 ? 90  TRP   B O    1 ? 2 
ATOM   2976 C CB   . TRP   B 1 78  ? 5.256   17.224 26.438  1   23.868 ? 90  TRP   B CB   1 ? 2 
ATOM   2977 C CG   . TRP   B 1 78  ? 6.734   16.975 26.576  1   23.147 ? 90  TRP   B CG   1 ? 2 
ATOM   2978 C CD1  . TRP   B 1 78  ? 7.388   15.834 26.937  1   22.054 ? 90  TRP   B CD1  1 ? 2 
ATOM   2979 C CD2  . TRP   B 1 78  ? 7.752   17.971 26.363  1   23.791 ? 90  TRP   B CD2  1 ? 2 
ATOM   2980 N NE1  . TRP   B 1 78  ? 8.739   16.059 26.98   1   23.51  ? 90  TRP   B NE1  1 ? 2 
ATOM   2981 C CE2  . TRP   B 1 78  ? 8.999   17.357 26.623  1   23.517 ? 90  TRP   B CE2  1 ? 2 
ATOM   2982 C CE3  . TRP   B 1 78  ? 7.718   19.311 25.971  1   23.634 ? 90  TRP   B CE3  1 ? 2 
ATOM   2983 C CZ2  . TRP   B 1 78  ? 10.201  18.034 26.494  1   25.963 ? 90  TRP   B CZ2  1 ? 2 
ATOM   2984 C CZ3  . TRP   B 1 78  ? 8.915   19.973 25.83   1   25.853 ? 90  TRP   B CZ3  1 ? 2 
ATOM   2985 C CH2  . TRP   B 1 78  ? 10.131  19.348 26.09   1   27.027 ? 90  TRP   B CH2  1 ? 2 
ATOM   2986 H H    . TRP   B 1 78  ? 3.896   15.049 26.76   1   23.237 ? 90  TRP   B H    1 c 2 
ATOM   2987 H HA   . TRP   B 1 78  ? 5.008   16.899 28.459  1   24.575 ? 90  TRP   B HA   1 c 2 
ATOM   2988 H HB2  . TRP   B 1 78  ? 4.924   16.727 25.659  1   23.363 ? 90  TRP   B HB2  1 c 2 
ATOM   2989 H HB3  . TRP   B 1 78  ? 5.114   18.178 26.259  1   24.25  ? 90  TRP   B HB3  1 c 2 
ATOM   2990 H HD1  . TRP   B 1 78  ? 6.976   15.015 27.162  1   22.03  ? 90  TRP   B HD1  1 c 2 
ATOM   2991 H HE1  . TRP   B 1 78  ? 9.337   15.466 27.177  1   23.41  ? 90  TRP   B HE1  1 c 2 
ATOM   2992 H HE3  . TRP   B 1 78  ? 6.9     19.738 25.781  1   24.057 ? 90  TRP   B HE3  1 c 2 
ATOM   2993 H HZ2  . TRP   B 1 78  ? 11.025  17.612 26.665  1   26.137 ? 90  TRP   B HZ2  1 c 2 
ATOM   2994 H HZ3  . TRP   B 1 78  ? 8.91    20.878 25.568  1   26.655 ? 90  TRP   B HZ3  1 c 2 
ATOM   2995 H HH2  . TRP   B 1 78  ? 10.928  19.841 26.001  1   27.853 ? 90  TRP   B HH2  1 c 2 
ATOM   2996 N N    . ASP   B 1 79  ? 2.123   17.547 27.187  1   24.926 ? 91  ASP   B N    1 ? 2 
ATOM   2997 C CA   . ASP   B 1 79  ? 0.951   18.39  27.373  1   23.862 ? 91  ASP   B CA   1 ? 2 
ATOM   2998 C C    . ASP   B 1 79  ? 0.493   18.288 28.827  1   26.467 ? 91  ASP   B C    1 ? 2 
ATOM   2999 O O    . ASP   B 1 79  ? 0.112   19.304 29.425  1   28.176 ? 91  ASP   B O    1 ? 2 
ATOM   3000 C CB   . ASP   B 1 79  ? -0.145  18.107 26.378  1   24.856 ? 91  ASP   B CB   1 ? 2 
ATOM   3001 C CG   . ASP   B 1 79  ? -0.002  18.795 25.017  1   24.688 ? 91  ASP   B CG   1 ? 2 
ATOM   3002 O OD1  . ASP   B 1 79  ? 0.739   19.801 24.937  1   23.353 ? 91  ASP   B OD1  1 ? 2 
ATOM   3003 O OD2  . ASP   B 1 79  ? -0.683  18.324 24.082  1   24.433 ? 91  ASP   B OD2  1 ? 2 
ATOM   3004 H H    . ASP   B 1 79  ? 2.082   16.848 26.6    1   24.061 ? 91  ASP   B H    1 c 2 
ATOM   3005 H HA   . ASP   B 1 79  ? 1.228   19.32  27.219  1   25.21  ? 91  ASP   B HA   1 c 2 
ATOM   3006 H HB2  . ASP   B 1 79  ? -0.19   17.14  26.226  1   24.07  ? 91  ASP   B HB2  1 c 2 
ATOM   3007 H HB3  . ASP   B 1 79  ? -1      18.387 26.766  1   25.033 ? 91  ASP   B HB3  1 c 2 
ATOM   3008 N N    . ILE   B 1 80  ? 0.579   17.085 29.4    1   24.864 ? 92  ILE   B N    1 ? 2 
ATOM   3009 C CA   . ILE   B 1 80  ? 0.22    16.875 30.8    1   27.723 ? 92  ILE   B CA   1 ? 2 
ATOM   3010 C C    . ILE   B 1 80  ? 1.229   17.546 31.72   1   27.053 ? 92  ILE   B C    1 ? 2 
ATOM   3011 O O    . ILE   B 1 80  ? 0.847   18.316 32.609  1   26.71  ? 92  ILE   B O    1 ? 2 
ATOM   3012 C CB   . ILE   B 1 80  ? 0.058   15.365 31.099  1   29.539 ? 92  ILE   B CB   1 ? 2 
ATOM   3013 C CG1  . ILE   B 1 80  ? -1.19   14.796 30.396  1   30.111 ? 92  ILE   B CG1  1 ? 2 
ATOM   3014 C CG2  . ILE   B 1 80  ? -0.013  15.096 32.606  1   33.159 ? 92  ILE   B CG2  1 ? 2 
ATOM   3015 C CD1  . ILE   B 1 80  ? -1.159  13.283 30.209  1   31.156 ? 92  ILE   B CD1  1 ? 2 
ATOM   3016 H H    . ILE   B 1 80  ? 0.861   16.37  28.906  1   25.1   ? 92  ILE   B H    1 c 2 
ATOM   3017 H HA   . ILE   B 1 80  ? -0.648  17.299 30.949  1   27.884 ? 92  ILE   B HA   1 c 2 
ATOM   3018 H HB   . ILE   B 1 80  ? 0.842   14.901 30.744  1   29.137 ? 92  ILE   B HB   1 c 2 
ATOM   3019 H HG12 . ILE   B 1 80  ? -1.981  15.032 30.922  1   31.007 ? 92  ILE   B HG12 1 c 2 
ATOM   3020 H HG13 . ILE   B 1 80  ? -1.277  15.219 29.518  1   29.769 ? 92  ILE   B HG13 1 c 2 
ATOM   3021 H HG21 . ILE   B 1 80  ? -0.39   14.214 32.763  1   32.665 ? 92  ILE   B HG21 1 c 2 
ATOM   3022 H HG22 . ILE   B 1 80  ? -0.574  15.766 33.031  1   33.079 ? 92  ILE   B HG22 1 c 2 
ATOM   3023 H HG23 . ILE   B 1 80  ? 0.881   15.134 32.987  1   32.539 ? 92  ILE   B HG23 1 c 2 
ATOM   3024 H HD11 . ILE   B 1 80  ? -0.403  13.04  29.641  1   30.125 ? 92  ILE   B HD11 1 c 2 
ATOM   3025 H HD12 . ILE   B 1 80  ? -1.988  12.991 29.786  1   31.042 ? 92  ILE   B HD12 1 c 2 
ATOM   3026 H HD13 . ILE   B 1 80  ? -1.066  12.844 31.076  1   31.418 ? 92  ILE   B HD13 1 c 2 
ATOM   3027 N N    . GLY   B 1 81  ? 2.515   17.249 31.505  1   25.693 ? 93  GLY   B N    1 ? 2 
ATOM   3028 C CA   . GLY   B 1 81  ? 3.571   17.559 32.461  1   25.954 ? 93  GLY   B CA   1 ? 2 
ATOM   3029 C C    . GLY   B 1 81  ? 3.883   19.052 32.512  1   27.89  ? 93  GLY   B C    1 ? 2 
ATOM   3030 O O    . GLY   B 1 81  ? 3.992   19.653 33.598  1   27.885 ? 93  GLY   B O    1 ? 2 
ATOM   3031 H H    . GLY   B 1 81  ? 2.746   16.831 30.726  1   25.025 ? 93  GLY   B H    1 c 2 
ATOM   3032 H HA2  . GLY   B 1 81  ? 3.294   17.253 33.355  1   27.149 ? 93  GLY   B HA2  1 c 2 
ATOM   3033 H HA3  . GLY   B 1 81  ? 4.386   17.063 32.211  1   26.073 ? 93  GLY   B HA3  1 c 2 
ATOM   3034 N N    . VAL   B 1 82  ? 4.052   19.643 31.324  1   26.674 ? 94  VAL   B N    1 ? 2 
ATOM   3035 C CA   . VAL   B 1 82  ? 4.445   21.034 31.252  1   30.455 ? 94  VAL   B CA   1 ? 2 
ATOM   3036 C C    . VAL   B 1 82  ? 3.315   21.918 31.787  1   31.868 ? 94  VAL   B C    1 ? 2 
ATOM   3037 O O    . VAL   B 1 82  ? 3.6     22.943 32.408  1   33.947 ? 94  VAL   B O    1 ? 2 
ATOM   3038 C CB   . VAL   B 1 82  ? 4.93    21.421 29.846  1   30.353 ? 94  VAL   B CB   1 ? 2 
ATOM   3039 C CG1  . VAL   B 1 82  ? 5.314   22.89  29.771  1   32.694 ? 94  VAL   B CG1  1 ? 2 
ATOM   3040 C CG2  . VAL   B 1 82  ? 6.125   20.575 29.416  1   27.789 ? 94  VAL   B CG2  1 ? 2 
ATOM   3041 H H    . VAL   B 1 82  ? 3.918   19.174 30.551  1   26.542 ? 94  VAL   B H    1 c 2 
ATOM   3042 H HA   . VAL   B 1 82  ? 5.205   21.146 31.855  1   30.803 ? 94  VAL   B HA   1 c 2 
ATOM   3043 H HB   . VAL   B 1 82  ? 4.187   21.258 29.219  1   29.395 ? 94  VAL   B HB   1 c 2 
ATOM   3044 H HG11 . VAL   B 1 82  ? 5.804   23.138 30.573  1   33.364 ? 94  VAL   B HG11 1 c 2 
ATOM   3045 H HG12 . VAL   B 1 82  ? 4.511   23.433 29.702  1   32.741 ? 94  VAL   B HG12 1 c 2 
ATOM   3046 H HG13 . VAL   B 1 82  ? 5.873   23.042 28.991  1   32.475 ? 94  VAL   B HG13 1 c 2 
ATOM   3047 H HG21 . VAL   B 1 82  ? 6.438   20.873 28.545  1   28.374 ? 94  VAL   B HG21 1 c 2 
ATOM   3048 H HG22 . VAL   B 1 82  ? 5.861   19.642 29.361  1   27.481 ? 94  VAL   B HG22 1 c 2 
ATOM   3049 H HG23 . VAL   B 1 82  ? 6.841   20.67  30.066  1   29.133 ? 94  VAL   B HG23 1 c 2 
ATOM   3050 N N    . ALA   B 1 83  ? 2.05    21.487 31.629  1   29.675 ? 95  ALA   B N    1 ? 2 
ATOM   3051 C CA   . ALA   B 1 83  ? 0.914   22.189 32.207  1   31.354 ? 95  ALA   B CA   1 ? 2 
ATOM   3052 C C    . ALA   B 1 83  ? 1.034   22.339 33.724  1   33.833 ? 95  ALA   B C    1 ? 2 
ATOM   3053 O O    . ALA   B 1 83  ? 0.471   23.287 34.265  1   38.362 ? 95  ALA   B O    1 ? 2 
ATOM   3054 C CB   . ALA   B 1 83  ? -0.403  21.505 31.861  1   31.568 ? 95  ALA   B CB   1 ? 2 
ATOM   3055 H H    . ALA   B 1 83  ? 1.894   20.734 31.135  1   29.224 ? 95  ALA   B H    1 c 2 
ATOM   3056 H HA   . ALA   B 1 83  ? 0.9     23.105 31.817  1   32.144 ? 95  ALA   B HA   1 c 2 
ATOM   3057 H HB1  . ALA   B 1 83  ? -0.511  21.473 30.895  1   30.681 ? 95  ALA   B HB1  1 c 2 
ATOM   3058 H HB2  . ALA   B 1 83  ? -0.405  20.6   32.214  1   30.915 ? 95  ALA   B HB2  1 c 2 
ATOM   3059 H HB3  . ALA   B 1 83  ? -1.142  22.003 32.249  1   32.216 ? 95  ALA   B HB3  1 c 2 
ATOM   3060 N N    . THR   B 1 84  ? 1.753   21.433 34.4    1   33.02  ? 96  THR   B N    1 ? 2 
ATOM   3061 C CA   . THR   B 1 84  ? 1.884   21.489 35.853  1   34.514 ? 96  THR   B CA   1 ? 2 
ATOM   3062 C C    . THR   B 1 84  ? 3.048   22.376 36.296  1   36.291 ? 96  THR   B C    1 ? 2 
ATOM   3063 O O    . THR   B 1 84  ? 3.236   22.53  37.499  1   39.605 ? 96  THR   B O    1 ? 2 
ATOM   3064 C CB   . THR   B 1 84  ? 2.095   20.09  36.429  1   33.317 ? 96  THR   B CB   1 ? 2 
ATOM   3065 O OG1  . THR   B 1 84  ? 3.443   19.705 36.109  1   34.398 ? 96  THR   B OG1  1 ? 2 
ATOM   3066 C CG2  . THR   B 1 84  ? 1.057   19.097 35.941  1   33.457 ? 96  THR   B CG2  1 ? 2 
ATOM   3067 H H    . THR   B 1 84  ? 2.164   20.754 33.948  1   32.13  ? 96  THR   B H    1 c 2 
ATOM   3068 H HA   . THR   B 1 84  ? 1.052   21.854 36.226  1   35.212 ? 96  THR   B HA   1 c 2 
ATOM   3069 H HB   . THR   B 1 84  ? 2.01    20.145 37.411  1   35.503 ? 96  THR   B HB   1 c 2 
ATOM   3070 H HG1  . THR   B 1 84  ? 3.603   19.793 35.256  0   30     ? 96  THR   B HG1  1 c 2 
ATOM   3071 H HG21 . THR   B 1 84  ? 1.075   18.306 36.505  1   33.477 ? 96  THR   B HG21 1 c 2 
ATOM   3072 H HG22 . THR   B 1 84  ? 1.256   18.844 35.025  1   31.749 ? 96  THR   B HG22 1 c 2 
ATOM   3073 H HG23 . THR   B 1 84  ? 0.174   19.503 35.981  1   33.417 ? 96  THR   B HG23 1 c 2 
ATOM   3074 N N    . MET   B 1 85  ? 3.843   22.926 35.369  1   36.047 ? 97  MET   B N    1 ? 2 
ATOM   3075 C CA   . MET   B 1 85  ? 5.078   23.601 35.746  1   38.381 ? 97  MET   B CA   1 ? 2 
ATOM   3076 C C    . MET   B 1 85  ? 4.894   25.118 35.85   1   39.958 ? 97  MET   B C    1 ? 2 
ATOM   3077 O O    . MET   B 1 85  ? 4.104   25.718 35.114  1   38.339 ? 97  MET   B O    1 ? 2 
ATOM   3078 C CB   . MET   B 1 85  ? 6.183   23.294 34.727  1   36.435 ? 97  MET   B CB   1 ? 2 
ATOM   3079 C CG   . MET   B 1 85  ? 6.517   21.804 34.631  1   34.578 ? 97  MET   B CG   1 ? 2 
ATOM   3080 S SD   . MET   B 1 85  ? 7.801   21.481 33.392  1   33.491 ? 97  MET   B SD   1 ? 2 
ATOM   3081 C CE   . MET   B 1 85  ? 9.235   22.301 34.092  1   36.359 ? 97  MET   B CE   1 ? 2 
ATOM   3082 H H    . MET   B 1 85  ? 3.615   22.884 34.486  1   35.027 ? 97  MET   B H    1 c 2 
ATOM   3083 H HA   . MET   B 1 85  ? 5.356   23.26  36.633  1   39.025 ? 97  MET   B HA   1 c 2 
ATOM   3084 H HB2  . MET   B 1 85  ? 5.898   23.617 33.846  1   35.771 ? 97  MET   B HB2  1 c 2 
ATOM   3085 H HB3  . MET   B 1 85  ? 6.991   23.789 34.982  1   37.84  ? 97  MET   B HB3  1 c 2 
ATOM   3086 H HG2  . MET   B 1 85  ? 6.826   21.481 35.499  1   35.649 ? 97  MET   B HG2  1 c 2 
ATOM   3087 H HG3  . MET   B 1 85  ? 5.714   21.305 34.391  1   33.533 ? 97  MET   B HG3  1 c 2 
ATOM   3088 H HE1  . MET   B 1 85  ? 9.998   22.182 33.498  1   36.191 ? 97  MET   B HE1  1 c 2 
ATOM   3089 H HE2  . MET   B 1 85  ? 9.05    23.253 34.193  1   37.264 ? 97  MET   B HE2  1 c 2 
ATOM   3090 H HE3  . MET   B 1 85  ? 9.437   21.914 34.964  1   37.133 ? 97  MET   B HE3  1 c 2 
ATOM   3091 N N    . LYS   B 1 86  ? 5.664   25.733 36.769  1   43.727 ? 98  LYS   B N    1 ? 2 
ATOM   3092 C CA   . LYS   B 1 86  ? 5.774   27.179 36.864  1   46.025 ? 98  LYS   B CA   1 ? 2 
ATOM   3093 C C    . LYS   B 1 86  ? 7.009   27.692 36.119  1   47.146 ? 98  LYS   B C    1 ? 2 
ATOM   3094 O O    . LYS   B 1 86  ? 7.944   26.94  35.851  1   45.093 ? 98  LYS   B O    1 ? 2 
ATOM   3095 C CB   . LYS   B 1 86  ? 5.855   27.548 38.348  1   52.322 ? 98  LYS   B CB   1 ? 2 
ATOM   3096 C CG   . LYS   B 1 86  ? 4.716   27.052 39.221  1   53.849 ? 98  LYS   B CG   1 ? 2 
ATOM   3097 C CD   . LYS   B 1 86  ? 5.007   27.174 40.709  1   59.388 ? 98  LYS   B CD   1 ? 2 
ATOM   3098 C CE   . LYS   B 1 86  ? 3.786   26.926 41.535  1   61.236 ? 98  LYS   B CE   1 ? 2 
ATOM   3099 N NZ   . LYS   B 1 86  ? 4.036   27.286 42.931  1   65.828 ? 98  LYS   B NZ   1 ? 2 
ATOM   3100 H H    . LYS   B 1 86  ? 6.139   25.222 37.359  1   43.911 ? 98  LYS   B H    1 c 2 
ATOM   3101 H HA   . LYS   B 1 86  ? 4.963   27.589 36.469  1   46.272 ? 98  LYS   B HA   1 c 2 
ATOM   3102 H HB2  . LYS   B 1 86  ? 6.695   27.192 38.71   1   52.421 ? 98  LYS   B HB2  1 c 2 
ATOM   3103 H HB3  . LYS   B 1 86  ? 5.894   28.525 38.422  1   53.377 ? 98  LYS   B HB3  1 c 2 
ATOM   3104 H HG2  . LYS   B 1 86  ? 3.909   27.569 39.008  1   54.063 ? 98  LYS   B HG2  1 c 2 
ATOM   3105 H HG3  . LYS   B 1 86  ? 4.539   26.111 39.006  1   52.375 ? 98  LYS   B HG3  1 c 2 
ATOM   3106 H HD2  . LYS   B 1 86  ? 5.701   26.524 40.956  1   59.076 ? 98  LYS   B HD2  1 c 2 
ATOM   3107 H HD3  . LYS   B 1 86  ? 5.349   28.074 40.899  1   60.859 ? 98  LYS   B HD3  1 c 2 
ATOM   3108 H HE2  . LYS   B 1 86  ? 3.043   27.456 41.197  1   60.941 ? 98  LYS   B HE2  1 c 2 
ATOM   3109 H HE3  . LYS   B 1 86  ? 3.54    25.984 41.487  1   59.869 ? 98  LYS   B HE3  1 c 2 
ATOM   3110 H HZ1  . LYS   B 1 86  ? 4.201   28.174 42.993  1   66.861 ? 98  LYS   B HZ1  1 c 2 
ATOM   3111 H HZ2  . LYS   B 1 86  ? 4.753   26.828 43.243  1   65.92  ? 98  LYS   B HZ2  1 c 2 
ATOM   3112 H HZ3  . LYS   B 1 86  ? 3.311   27.082 43.434  1   65.968 ? 98  LYS   B HZ3  1 c 2 
ATOM   3113 N N    . LYS   B 1 87  ? 6.998   28.994 35.79   1   48.887 ? 99  LYS   B N    1 ? 2 
ATOM   3114 C CA   . LYS   B 1 87  ? 8.138   29.689 35.217  1   48.944 ? 99  LYS   B CA   1 ? 2 
ATOM   3115 C C    . LYS   B 1 87  ? 9.347   29.487 36.126  1   50.204 ? 99  LYS   B C    1 ? 2 
ATOM   3116 O O    . LYS   B 1 87  ? 9.254   29.685 37.334  1   51.538 ? 99  LYS   B O    1 ? 2 
ATOM   3117 C CB   . LYS   B 1 87  ? 7.846   31.183 35.025  1   51.493 ? 99  LYS   B CB   1 ? 2 
ATOM   3118 H H    . LYS   B 1 87  ? 6.231   29.469 35.935  1   48.962 ? 99  LYS   B H    1 c 2 
ATOM   3119 H HA   . LYS   B 1 87  ? 8.331   29.287 34.332  1   47.629 ? 99  LYS   B HA   1 c 2 
ATOM   3120 H HB2  . LYS   B 1 87  ? 8.709   31.708 34.907  0   30     ? 99  LYS   B HB2  1 c 2 
ATOM   3121 H HB3  . LYS   B 1 87  ? 6.885   31.356 34.953  0   30     ? 99  LYS   B HB3  1 c 2 
ATOM   3122 N N    . GLY   B 1 88  ? 10.454  29.023 35.527  1   49.616 ? 100 GLY   B N    1 ? 2 
ATOM   3123 C CA   . GLY   B 1 88  ? 11.721  28.821 36.211  1   51.627 ? 100 GLY   B CA   1 ? 2 
ATOM   3124 C C    . GLY   B 1 88  ? 11.895  27.407 36.764  1   49.057 ? 100 GLY   B C    1 ? 2 
ATOM   3125 O O    . GLY   B 1 88  ? 12.986  27.046 37.194  1   48.241 ? 100 GLY   B O    1 ? 2 
ATOM   3126 H H    . GLY   B 1 88  ? 10.413  28.821 34.636  1   48.243 ? 100 GLY   B H    1 c 2 
ATOM   3127 H HA2  . GLY   B 1 88  ? 12.454  29.011 35.579  1   51.82  ? 100 GLY   B HA2  1 c 2 
ATOM   3128 H HA3  . GLY   B 1 88  ? 11.791  29.469 36.951  1   53.592 ? 100 GLY   B HA3  1 c 2 
ATOM   3129 N N    . GLU   B 1 89  ? 10.825  26.611 36.739  1   47.112 ? 101 GLU   B N    1 ? 2 
ATOM   3130 C CA   . GLU   B 1 89  ? 10.853  25.264 37.296  1   46.226 ? 101 GLU   B CA   1 ? 2 
ATOM   3131 C C    . GLU   B 1 89  ? 11.658  24.337 36.389  1   44.542 ? 101 GLU   B C    1 ? 2 
ATOM   3132 O O    . GLU   B 1 89  ? 11.653  24.481 35.167  1   42.46  ? 101 GLU   B O    1 ? 2 
ATOM   3133 C CB   . GLU   B 1 89  ? 9.431   24.722 37.461  1   45.398 ? 101 GLU   B CB   1 ? 2 
ATOM   3134 C CG   . GLU   B 1 89  ? 9.349   23.38  38.186  1   45.411 ? 101 GLU   B CG   1 ? 2 
ATOM   3135 C CD   . GLU   B 1 89  ? 7.91    22.878 38.245  1   45.016 ? 101 GLU   B CD   1 ? 2 
ATOM   3136 O OE1  . GLU   B 1 89  ? 7.034   23.674 38.64   1   45.535 ? 101 GLU   B OE1  1 ? 2 
ATOM   3137 O OE2  . GLU   B 1 89  ? 7.655   21.703 37.9    1   46.034 ? 101 GLU   B OE2  1 ? 2 
ATOM   3138 H H    . GLU   B 1 89  ? 10.051  26.909 36.357  1   46.082 ? 101 GLU   B H    1 c 2 
ATOM   3139 H HA   . GLU   B 1 89  ? 11.287  25.304 38.184  1   48.314 ? 101 GLU   B HA   1 c 2 
ATOM   3140 H HB2  . GLU   B 1 89  ? 8.9     25.382 37.954  1   46.347 ? 101 GLU   B HB2  1 c 2 
ATOM   3141 H HB3  . GLU   B 1 89  ? 9.03    24.621 36.573  1   43.442 ? 101 GLU   B HB3  1 c 2 
ATOM   3142 H HG2  . GLU   B 1 89  ? 9.899   22.716 37.719  1   44.66  ? 101 GLU   B HG2  1 c 2 
ATOM   3143 H HG3  . GLU   B 1 89  ? 9.689   23.479 39.1    1   47.576 ? 101 GLU   B HG3  1 c 2 
ATOM   3144 N N    . ILE   B 1 90  ? 12.341  23.375 37.014  1   45.043 ? 102 ILE   B N    1 ? 2 
ATOM   3145 C CA   . ILE   B 1 90  ? 12.937  22.25  36.317  1   42.566 ? 102 ILE   B CA   1 ? 2 
ATOM   3146 C C    . ILE   B 1 90  ? 12.346  20.98  36.912  1   40.855 ? 102 ILE   B C    1 ? 2 
ATOM   3147 O O    . ILE   B 1 90  ? 12.347  20.807 38.124  1   44.048 ? 102 ILE   B O    1 ? 2 
ATOM   3148 C CB   . ILE   B 1 90  ? 14.478  22.256 36.416  1   43.885 ? 102 ILE   B CB   1 ? 2 
ATOM   3149 C CG1  . ILE   B 1 90  ? 15.06   23.538 35.807  1   47.261 ? 102 ILE   B CG1  1 ? 2 
ATOM   3150 C CG2  . ILE   B 1 90  ? 15.078  21.002 35.789  1   41.204 ? 102 ILE   B CG2  1 ? 2 
ATOM   3151 C CD1  . ILE   B 1 90  ? 16.561  23.75  35.992  1   49.876 ? 102 ILE   B CD1  1 ? 2 
ATOM   3152 H H    . ILE   B 1 90  ? 12.441  23.424 37.921  1   46.477 ? 102 ILE   B H    1 c 2 
ATOM   3153 H HA   . ILE   B 1 90  ? 12.689  22.301 35.377  1   40.866 ? 102 ILE   B HA   1 c 2 
ATOM   3154 H HB   . ILE   B 1 90  ? 14.71   22.252 37.366  1   45.958 ? 102 ILE   B HB   1 c 2 
ATOM   3155 H HG12 . ILE   B 1 90  ? 14.866  23.536 34.848  1   45.148 ? 102 ILE   B HG12 1 c 2 
ATOM   3156 H HG13 . ILE   B 1 90  ? 14.593  24.305 36.197  1   47.548 ? 102 ILE   B HG13 1 c 2 
ATOM   3157 H HG21 . ILE   B 1 90  ? 16.037  21.113 35.685  1   43.055 ? 102 ILE   B HG21 1 c 2 
ATOM   3158 H HG22 . ILE   B 1 90  ? 14.675  20.849 34.917  1   39.66  ? 102 ILE   B HG22 1 c 2 
ATOM   3159 H HG23 . ILE   B 1 90  ? 14.906  20.236 36.362  1   41.521 ? 102 ILE   B HG23 1 c 2 
ATOM   3160 H HD11 . ILE   B 1 90  ? 16.783  23.707 36.941  1   51.737 ? 102 ILE   B HD11 1 c 2 
ATOM   3161 H HD12 . ILE   B 1 90  ? 16.809  24.626 35.641  1   51.077 ? 102 ILE   B HD12 1 c 2 
ATOM   3162 H HD13 . ILE   B 1 90  ? 17.056  23.06  35.512  1   49.247 ? 102 ILE   B HD13 1 c 2 
ATOM   3163 N N    . ALA   B 1 91  ? 11.908  20.076 36.045  1   38.328 ? 103 ALA   B N    1 ? 2 
ATOM   3164 C CA   . ALA   B 1 91  ? 11.246  18.85  36.45   1   38.046 ? 103 ALA   B CA   1 ? 2 
ATOM   3165 C C    . ALA   B 1 91  ? 11.871  17.672 35.713  1   36.47  ? 103 ALA   B C    1 ? 2 
ATOM   3166 O O    . ALA   B 1 91  ? 12.403  17.847 34.626  1   37.655 ? 103 ALA   B O    1 ? 2 
ATOM   3167 C CB   . ALA   B 1 91  ? 9.757   18.952 36.149  1   36.182 ? 103 ALA   B CB   1 ? 2 
ATOM   3168 H H    . ALA   B 1 91  ? 12.029  20.228 35.152  1   37.486 ? 103 ALA   B H    1 c 2 
ATOM   3169 H HA   . ALA   B 1 91  ? 11.38   18.721 37.428  1   39.432 ? 103 ALA   B HA   1 c 2 
ATOM   3170 H HB1  . ALA   B 1 91  ? 9.369   19.684 36.658  1   37.109 ? 103 ALA   B HB1  1 c 2 
ATOM   3171 H HB2  . ALA   B 1 91  ? 9.626   19.117 35.2    1   34.865 ? 103 ALA   B HB2  1 c 2 
ATOM   3172 H HB3  . ALA   B 1 91  ? 9.316   18.121 36.395  1   35.719 ? 103 ALA   B HB3  1 c 2 
ATOM   3173 N N    . HIS   B 1 92  ? 11.792  16.485 36.319  1   36.146 ? 104 HIS   B N    1 ? 2 
ATOM   3174 C CA   . HIS   B 1 92  ? 12.064  15.239 35.628  1   34.45  ? 104 HIS   B CA   1 ? 2 
ATOM   3175 C C    . HIS   B 1 92  ? 10.736  14.531 35.368  1   33.676 ? 104 HIS   B C    1 ? 2 
ATOM   3176 O O    . HIS   B 1 92  ? 9.901   14.484 36.275  1   33.892 ? 104 HIS   B O    1 ? 2 
ATOM   3177 C CB   . HIS   B 1 92  ? 12.959  14.345 36.481  1   36.447 ? 104 HIS   B CB   1 ? 2 
ATOM   3178 C CG   . HIS   B 1 92  ? 14.393  14.763 36.495  1   37.734 ? 104 HIS   B CG   1 ? 2 
ATOM   3179 N ND1  . HIS   B 1 92  ? 15.334  14.126 37.262  1   39.754 ? 104 HIS   B ND1  1 ? 2 
ATOM   3180 C CD2  . HIS   B 1 92  ? 15.045  15.696 35.793  1   37.179 ? 104 HIS   B CD2  1 ? 2 
ATOM   3181 C CE1  . HIS   B 1 92  ? 16.508  14.687 37.038  1   41.565 ? 104 HIS   B CE1  1 ? 2 
ATOM   3182 N NE2  . HIS   B 1 92  ? 16.349  15.649 36.153  1   38.899 ? 104 HIS   B NE2  1 ? 2 
ATOM   3183 H H    . HIS   B 1 92  ? 11.558  16.452 37.201  1   37.343 ? 104 HIS   B H    1 c 2 
ATOM   3184 H HA   . HIS   B 1 92  ? 12.5    15.427 34.765  1   33.992 ? 104 HIS   B HA   1 c 2 
ATOM   3185 H HB2  . HIS   B 1 92  ? 12.618  14.345 37.402  1   37.513 ? 104 HIS   B HB2  1 c 2 
ATOM   3186 H HB3  . HIS   B 1 92  ? 12.9    13.426 36.141  1   35.617 ? 104 HIS   B HB3  1 c 2 
ATOM   3187 H HD1  . HIS   B 1 92  ? 15.199  13.401 37.816  0   30     ? 104 HIS   B HD1  1 c 2 
ATOM   3188 H HD2  . HIS   B 1 92  ? 14.67   16.294 35.177  1   36.014 ? 104 HIS   B HD2  1 c 2 
ATOM   3189 H HE1  . HIS   B 1 92  ? 17.318  14.446 37.453  1   43.134 ? 104 HIS   B HE1  1 c 2 
ATOM   3190 H HE2  . HIS   B 1 92  ? 16.963  16.168 35.866  0   30     ? 104 HIS   B HE2  1 c 2 
ATOM   3191 N N    . LEU   B 1 93  ? 10.555  14.02  34.14   1   29.741 ? 105 LEU   B N    1 ? 2 
ATOM   3192 C CA   . LEU   B 1 93  ? 9.425   13.185 33.763  1   29.512 ? 105 LEU   B CA   1 ? 2 
ATOM   3193 C C    . LEU   B 1 93  ? 9.935   11.826 33.287  1   30.325 ? 105 LEU   B C    1 ? 2 
ATOM   3194 O O    . LEU   B 1 93  ? 10.856  11.751 32.465  1   30.565 ? 105 LEU   B O    1 ? 2 
ATOM   3195 C CB   . LEU   B 1 93  ? 8.567   13.76  32.632  1   27.503 ? 105 LEU   B CB   1 ? 2 
ATOM   3196 C CG   . LEU   B 1 93  ? 7.985   15.159 32.821  1   27.362 ? 105 LEU   B CG   1 ? 2 
ATOM   3197 C CD1  . LEU   B 1 93  ? 7.168   15.577 31.631  1   26.609 ? 105 LEU   B CD1  1 ? 2 
ATOM   3198 C CD2  . LEU   B 1 93  ? 7.155   15.205 34.075  1   28.802 ? 105 LEU   B CD2  1 ? 2 
ATOM   3199 H H    . LEU   B 1 93  ? 11.179  14.208 33.499  1   30.243 ? 105 LEU   B H    1 c 2 
ATOM   3200 H HA   . LEU   B 1 93  ? 8.86    13.052 34.56   1   30.059 ? 105 LEU   B HA   1 c 2 
ATOM   3201 H HB2  . LEU   B 1 93  ? 9.111   13.764 31.811  1   26.991 ? 105 LEU   B HB2  1 c 2 
ATOM   3202 H HB3  . LEU   B 1 93  ? 7.821   13.138 32.472  1   26.875 ? 105 LEU   B HB3  1 c 2 
ATOM   3203 H HG   . LEU   B 1 93  ? 8.737   15.798 32.922  1   28.368 ? 105 LEU   B HG   1 c 2 
ATOM   3204 H HD11 . LEU   B 1 93  ? 7.715   15.533 30.829  1   25.964 ? 105 LEU   B HD11 1 c 2 
ATOM   3205 H HD12 . LEU   B 1 93  ? 6.852   16.488 31.757  1   26.665 ? 105 LEU   B HD12 1 c 2 
ATOM   3206 H HD13 . LEU   B 1 93  ? 6.406   14.981 31.535  1   25.837 ? 105 LEU   B HD13 1 c 2 
ATOM   3207 H HD21 . LEU   B 1 93  ? 7.737   15.176 34.852  1   29.969 ? 105 LEU   B HD21 1 c 2 
ATOM   3208 H HD22 . LEU   B 1 93  ? 6.552   14.442 34.094  1   28.304 ? 105 LEU   B HD22 1 c 2 
ATOM   3209 H HD23 . LEU   B 1 93  ? 6.636   16.026 34.092  1   28.663 ? 105 LEU   B HD23 1 c 2 
ATOM   3210 N N    . LEU   B 1 94  ? 9.241   10.776 33.736  1   29.164 ? 106 LEU   B N    1 ? 2 
ATOM   3211 C CA   . LEU   B 1 94  ? 9.415   9.425  33.246  1   30.016 ? 106 LEU   B CA   1 ? 2 
ATOM   3212 C C    . LEU   B 1 94  ? 8.072   8.969  32.686  1   30.195 ? 106 LEU   B C    1 ? 2 
ATOM   3213 O O    . LEU   B 1 94  ? 7.05    9.113  33.356  1   30.249 ? 106 LEU   B O    1 ? 2 
ATOM   3214 C CB   . LEU   B 1 94  ? 9.877   8.518  34.382  1   32.517 ? 106 LEU   B CB   1 ? 2 
ATOM   3215 C CG   . LEU   B 1 94  ? 10.263  7.094  33.967  1   33.68  ? 106 LEU   B CG   1 ? 2 
ATOM   3216 C CD1  . LEU   B 1 94  ? 11.505  7.051  33.086  1   33.847 ? 106 LEU   B CD1  1 ? 2 
ATOM   3217 C CD2  . LEU   B 1 94  ? 10.48   6.262  35.204  1   36.824 ? 106 LEU   B CD2  1 ? 2 
ATOM   3218 H H    . LEU   B 1 94  ? 8.621   10.915 34.393  1   30.182 ? 106 LEU   B H    1 c 2 
ATOM   3219 H HA   . LEU   B 1 94  ? 10.091  9.428  32.524  1   29.722 ? 106 LEU   B HA   1 c 2 
ATOM   3220 H HB2  . LEU   B 1 94  ? 10.655  8.939  34.815  1   33.601 ? 106 LEU   B HB2  1 c 2 
ATOM   3221 H HB3  . LEU   B 1 94  ? 9.153   8.464  35.047  1   33.157 ? 106 LEU   B HB3  1 c 2 
ATOM   3222 H HG   . LEU   B 1 94  ? 9.508   6.701  33.459  1   32.822 ? 106 LEU   B HG   1 c 2 
ATOM   3223 H HD11 . LEU   B 1 94  ? 11.315  7.476  32.233  1   32.291 ? 106 LEU   B HD11 1 c 2 
ATOM   3224 H HD12 . LEU   B 1 94  ? 11.764  6.126  32.934  1   34.298 ? 106 LEU   B HD12 1 c 2 
ATOM   3225 H HD13 . LEU   B 1 94  ? 12.233  7.522  33.526  1   34.663 ? 106 LEU   B HD13 1 c 2 
ATOM   3226 H HD21 . LEU   B 1 94  ? 9.653   6.216  35.713  1   36.929 ? 106 LEU   B HD21 1 c 2 
ATOM   3227 H HD22 . LEU   B 1 94  ? 11.173  6.668  35.75   1   37.748 ? 106 LEU   B HD22 1 c 2 
ATOM   3228 H HD23 . LEU   B 1 94  ? 10.753  5.365  34.948  1   37.093 ? 106 LEU   B HD23 1 c 2 
ATOM   3229 N N    . ILE   B 1 95  ? 8.095   8.444  31.451  1   28.113 ? 107 ILE   B N    1 ? 2 
ATOM   3230 C CA   . ILE   B 1 95  ? 6.898   8.322  30.653  1   27.935 ? 107 ILE   B CA   1 ? 2 
ATOM   3231 C C    . ILE   B 1 95  ? 6.76    6.924  30.056  1   27.61  ? 107 ILE   B C    1 ? 2 
ATOM   3232 O O    . ILE   B 1 95  ? 7.599   6.497  29.269  1   26.561 ? 107 ILE   B O    1 ? 2 
ATOM   3233 C CB   . ILE   B 1 95  ? 6.915   9.369  29.528  1   26.143 ? 107 ILE   B CB   1 ? 2 
ATOM   3234 C CG1  . ILE   B 1 95  ? 7.074   10.777 30.074  1   26.201 ? 107 ILE   B CG1  1 ? 2 
ATOM   3235 C CG2  . ILE   B 1 95  ? 5.653   9.229  28.686  1   25.822 ? 107 ILE   B CG2  1 ? 2 
ATOM   3236 C CD1  . ILE   B 1 95  ? 7.569   11.799 29.073  1   24.045 ? 107 ILE   B CD1  1 ? 2 
ATOM   3237 H H    . ILE   B 1 95  ? 8.887   8.149  31.102  1   28.704 ? 107 ILE   B H    1 c 2 
ATOM   3238 H HA   . ILE   B 1 95  ? 6.126   8.497  31.222  1   27.799 ? 107 ILE   B HA   1 c 2 
ATOM   3239 H HB   . ILE   B 1 95  ? 7.684   9.18   28.955  1   26.224 ? 107 ILE   B HB   1 c 2 
ATOM   3240 H HG12 . ILE   B 1 95  ? 6.209   11.076 30.421  1   25.813 ? 107 ILE   B HG12 1 c 2 
ATOM   3241 H HG13 . ILE   B 1 95  ? 7.701   10.756 30.824  1   26.717 ? 107 ILE   B HG13 1 c 2 
ATOM   3242 H HG21 . ILE   B 1 95  ? 5.541   10.019 28.134  1   25.083 ? 107 ILE   B HG21 1 c 2 
ATOM   3243 H HG22 . ILE   B 1 95  ? 4.881   9.13   29.268  1   25.98  ? 107 ILE   B HG22 1 c 2 
ATOM   3244 H HG23 . ILE   B 1 95  ? 5.728   8.449  28.113  1   25.661 ? 107 ILE   B HG23 1 c 2 
ATOM   3245 H HD11 . ILE   B 1 95  ? 8.478   11.568 28.803  1   24.727 ? 107 ILE   B HD11 1 c 2 
ATOM   3246 H HD12 . ILE   B 1 95  ? 7.568   12.685 29.481  1   24.73  ? 107 ILE   B HD12 1 c 2 
ATOM   3247 H HD13 . ILE   B 1 95  ? 6.991   11.803 28.288  1   23.839 ? 107 ILE   B HD13 1 c 2 
ATOM   3248 N N    . LYS   B 1 96  ? 5.633   6.265  30.366  1   28.286 ? 108 LYS   B N    1 ? 2 
ATOM   3249 C CA   . LYS   B 1 96  ? 5.307   4.999  29.738  1   27.504 ? 108 LYS   B CA   1 ? 2 
ATOM   3250 C C    . LYS   B 1 96  ? 4.918   5.222  28.28   1   25.639 ? 108 LYS   B C    1 ? 2 
ATOM   3251 O O    . LYS   B 1 96  ? 4.456   6.304  27.925  1   24.934 ? 108 LYS   B O    1 ? 2 
ATOM   3252 C CB   . LYS   B 1 96  ? 4.187   4.302  30.511  1   29.502 ? 108 LYS   B CB   1 ? 2 
ATOM   3253 C CG   . LYS   B 1 96  ? 4.619   3.8    31.889  1   33.06  ? 108 LYS   B CG   1 ? 2 
ATOM   3254 C CD   . LYS   B 1 96  ? 3.49    3.127  32.685  1   36.978 ? 108 LYS   B CD   1 ? 2 
ATOM   3255 C CE   . LYS   B 1 96  ? 3.866   2.691  34.08   1   39.18  ? 108 LYS   B CE   1 ? 2 
ATOM   3256 N NZ   . LYS   B 1 96  ? 2.67    2.183  34.761  1   42.484 ? 108 LYS   B NZ   1 ? 2 
ATOM   3257 H H    . LYS   B 1 96  ? 5.057   6.615  30.984  1   28.233 ? 108 LYS   B H    1 c 2 
ATOM   3258 H HA   . LYS   B 1 96  ? 6.114   4.426  29.769  1   28.34  ? 108 LYS   B HA   1 c 2 
ATOM   3259 H HB2  . LYS   B 1 96  ? 3.442   4.929  30.627  1   29.34  ? 108 LYS   B HB2  1 c 2 
ATOM   3260 H HB3  . LYS   B 1 96  ? 3.859   3.54   29.99   1   30.097 ? 108 LYS   B HB3  1 c 2 
ATOM   3261 H HG2  . LYS   B 1 96  ? 5.354   3.16   31.772  1   33.658 ? 108 LYS   B HG2  1 c 2 
ATOM   3262 H HG3  . LYS   B 1 96  ? 4.964   4.562  32.405  1   32.942 ? 108 LYS   B HG3  1 c 2 
ATOM   3263 H HD2  . LYS   B 1 96  ? 2.734   3.749  32.742  1   35.928 ? 108 LYS   B HD2  1 c 2 
ATOM   3264 H HD3  . LYS   B 1 96  ? 3.183   2.342  32.182  1   36.829 ? 108 LYS   B HD3  1 c 2 
ATOM   3265 H HE2  . LYS   B 1 96  ? 4.538   1.988  34.041  1   40.278 ? 108 LYS   B HE2  1 c 2 
ATOM   3266 H HE3  . LYS   B 1 96  ? 4.229   3.443  34.581  1   39.3   ? 108 LYS   B HE3  1 c 2 
ATOM   3267 H HZ1  . LYS   B 1 96  ? 2.342   1.468  34.311  1   42.362 ? 108 LYS   B HZ1  1 c 2 
ATOM   3268 H HZ2  . LYS   B 1 96  ? 2.036   2.829  34.793  1   41.328 ? 108 LYS   B HZ2  1 c 2 
ATOM   3269 H HZ3  . LYS   B 1 96  ? 2.882   1.932  35.605  1   43.557 ? 108 LYS   B HZ3  1 c 2 
ATOM   3270 N N    . PRO   B 1 97  ? 5.023   4.177  27.426  1   27.351 ? 109 PRO   B N    1 ? 2 
ATOM   3271 C CA   . PRO   B 1 97  ? 4.82    4.347  25.991  1   26.902 ? 109 PRO   B CA   1 ? 2 
ATOM   3272 C C    . PRO   B 1 97  ? 3.446   4.88   25.589  1   28.555 ? 109 PRO   B C    1 ? 2 
ATOM   3273 O O    . PRO   B 1 97  ? 3.316   5.594  24.606  1   25.846 ? 109 PRO   B O    1 ? 2 
ATOM   3274 C CB   . PRO   B 1 97  ? 5.066   2.964  25.413  1   29.357 ? 109 PRO   B CB   1 ? 2 
ATOM   3275 C CG   . PRO   B 1 97  ? 5.304   2.005  26.57   1   30.863 ? 109 PRO   B CG   1 ? 2 
ATOM   3276 C CD   . PRO   B 1 97  ? 5.412   2.808  27.822  1   30.07  ? 109 PRO   B CD   1 ? 2 
ATOM   3277 H HA   . PRO   B 1 97  ? 5.507   4.955  25.647  1   26.825 ? 109 PRO   B HA   1 c 2 
ATOM   3278 H HB2  . PRO   B 1 97  ? 4.296   2.673  24.886  1   29.345 ? 109 PRO   B HB2  1 c 2 
ATOM   3279 H HB3  . PRO   B 1 97  ? 5.842   2.977  24.82   1   28.881 ? 109 PRO   B HB3  1 c 2 
ATOM   3280 H HG2  . PRO   B 1 97  ? 4.563   1.37   26.642  1   31.546 ? 109 PRO   B HG2  1 c 2 
ATOM   3281 H HG3  . PRO   B 1 97  ? 6.128   1.498  26.426  1   31.197 ? 109 PRO   B HG3  1 c 2 
ATOM   3282 H HD2  . PRO   B 1 97  ? 4.81    2.463  28.507  1   30.723 ? 109 PRO   B HD2  1 c 2 
ATOM   3283 H HD3  . PRO   B 1 97  ? 6.326   2.797  28.166  1   30.147 ? 109 PRO   B HD3  1 c 2 
ATOM   3284 N N    . GLU   B 1 98  ? 2.406   4.545  26.364  1   29.805 ? 110 GLU   B N    1 ? 2 
ATOM   3285 C CA   . GLU   B 1 98  ? 1.052   5.006  26.097  1   29.092 ? 110 GLU   B CA   1 ? 2 
ATOM   3286 C C    . GLU   B 1 98  ? 0.949   6.54   26.057  1   25.498 ? 110 GLU   B C    1 ? 2 
ATOM   3287 O O    . GLU   B 1 98  ? 0.095   7.048  25.348  1   24.333 ? 110 GLU   B O    1 ? 2 
ATOM   3288 C CB   . GLU   B 1 98  ? 0.105   4.463  27.172  1   32.109 ? 110 GLU   B CB   1 ? 2 
ATOM   3289 C CG   . GLU   B 1 98  ? -0.042  2.944  27.161  1   38.337 ? 110 GLU   B CG   1 ? 2 
ATOM   3290 C CD   . GLU   B 1 98  ? 1.136   2.071  27.634  1   43.24  ? 110 GLU   B CD   1 ? 2 
ATOM   3291 O OE1  . GLU   B 1 98  ? 1.923   2.505  28.526  1   39.06  ? 110 GLU   B OE1  1 ? 2 
ATOM   3292 O OE2  . GLU   B 1 98  ? 1.263   0.942  27.093  1   46.641 ? 110 GLU   B OE2  1 ? 2 
ATOM   3293 H H    . GLU   B 1 98  ? 2.553   4.021  27.097  1   30.272 ? 110 GLU   B H    1 c 2 
ATOM   3294 H HA   . GLU   B 1 98  ? 0.771   4.648  25.216  1   29.327 ? 110 GLU   B HA   1 c 2 
ATOM   3295 H HB2  . GLU   B 1 98  ? 0.434   4.742  28.051  1   32.627 ? 110 GLU   B HB2  1 c 2 
ATOM   3296 H HB3  . GLU   B 1 98  ? -0.78   4.864  27.044  1   32.762 ? 110 GLU   B HB3  1 c 2 
ATOM   3297 H HG2  . GLU   B 1 98  ? -0.819  2.711  27.713  1   39.134 ? 110 GLU   B HG2  1 c 2 
ATOM   3298 H HG3  . GLU   B 1 98  ? -0.264  2.668  26.247  1   38.25  ? 110 GLU   B HG3  1 c 2 
ATOM   3299 N N    . TYR   B 1 99  ? 1.806   7.269  26.787  1   23.502 ? 111 TYR   B N    1 ? 2 
ATOM   3300 C CA   . TYR   B 1 99  ? 1.797   8.728  26.798  1   22.596 ? 111 TYR   B CA   1 ? 2 
ATOM   3301 C C    . TYR   B 1 99  ? 2.957   9.313  25.989  1   23.604 ? 111 TYR   B C    1 ? 2 
ATOM   3302 O O    . TYR   B 1 99  ? 3.247   10.524 26.087  1   24.637 ? 111 TYR   B O    1 ? 2 
ATOM   3303 C CB   . TYR   B 1 99  ? 1.854   9.215  28.252  1   22.163 ? 111 TYR   B CB   1 ? 2 
ATOM   3304 C CG   . TYR   B 1 99  ? 0.607   8.837  29.048  1   23.445 ? 111 TYR   B CG   1 ? 2 
ATOM   3305 C CD1  . TYR   B 1 99  ? 0.446   7.576  29.619  1   24.742 ? 111 TYR   B CD1  1 ? 2 
ATOM   3306 C CD2  . TYR   B 1 99  ? -0.427  9.75   29.207  1   24.517 ? 111 TYR   B CD2  1 ? 2 
ATOM   3307 C CE1  . TYR   B 1 99  ? -0.704  7.236  30.323  1   26.447 ? 111 TYR   B CE1  1 ? 2 
ATOM   3308 C CE2  . TYR   B 1 99  ? -1.57   9.432  29.924  1   25.9   ? 111 TYR   B CE2  1 ? 2 
ATOM   3309 C CZ   . TYR   B 1 99  ? -1.722  8.171  30.465  1   25.93  ? 111 TYR   B CZ   1 ? 2 
ATOM   3310 O OH   . TYR   B 1 99  ? -2.878  7.901  31.13   1   28.798 ? 111 TYR   B OH   1 ? 2 
ATOM   3311 H H    . TYR   B 1 99  ? 2.416   6.837  27.312  1   24.141 ? 111 TYR   B H    1 c 2 
ATOM   3312 H HA   . TYR   B 1 99  ? 0.944   9.043  26.396  1   22.844 ? 111 TYR   B HA   1 c 2 
ATOM   3313 H HB2  . TYR   B 1 99  ? 2.644   8.823  28.686  1   22.639 ? 111 TYR   B HB2  1 c 2 
ATOM   3314 H HB3  . TYR   B 1 99  ? 1.952   10.193 28.256  1   22.057 ? 111 TYR   B HB3  1 c 2 
ATOM   3315 H HD1  . TYR   B 1 99  ? 1.129   6.933  29.515  1   24.89  ? 111 TYR   B HD1  1 c 2 
ATOM   3316 H HD2  . TYR   B 1 99  ? -0.343  10.613 28.834  1   23.739 ? 111 TYR   B HD2  1 c 2 
ATOM   3317 H HE1  . TYR   B 1 99  ? -0.796  6.376  30.695  1   27.241 ? 111 TYR   B HE1  1 c 2 
ATOM   3318 H HE2  . TYR   B 1 99  ? -2.263  10.065 30.008  1   25.791 ? 111 TYR   B HE2  1 c 2 
ATOM   3319 H HH   . TYR   B 1 99  ? -2.891  7.112  31.447  0   30     ? 111 TYR   B HH   1 c 2 
ATOM   3320 N N    . ALA   B 1 100 ? 3.63    8.458  25.198  1   21.31  ? 112 ALA   B N    1 ? 2 
ATOM   3321 C CA   . ALA   B 1 100 ? 4.738   8.902  24.376  1   21.533 ? 112 ALA   B CA   1 ? 2 
ATOM   3322 C C    . ALA   B 1 100 ? 4.504   8.442  22.931  1   20.723 ? 112 ALA   B C    1 ? 2 
ATOM   3323 O O    . ALA   B 1 100 ? 3.65    9.016  22.285  1   21.881 ? 112 ALA   B O    1 ? 2 
ATOM   3324 C CB   . ALA   B 1 100 ? 6.041   8.442  24.954  1   22.035 ? 112 ALA   B CB   1 ? 2 
ATOM   3325 H H    . ALA   B 1 100 ? 3.387   7.579  25.167  1   22.451 ? 112 ALA   B H    1 c 2 
ATOM   3326 H HA   . ALA   B 1 100 ? 4.735   9.897  24.373  1   21.036 ? 112 ALA   B HA   1 c 2 
ATOM   3327 H HB1  . ALA   B 1 100 ? 6.264   8.986  25.728  1   21.934 ? 112 ALA   B HB1  1 c 2 
ATOM   3328 H HB2  . ALA   B 1 100 ? 5.968   7.512  25.226  1   22.393 ? 112 ALA   B HB2  1 c 2 
ATOM   3329 H HB3  . ALA   B 1 100 ? 6.744   8.529  24.288  1   21.969 ? 112 ALA   B HB3  1 c 2 
ATOM   3330 N N    . TYR   B 1 101 ? 5.121   7.346  22.486  1   21.729 ? 113 TYR   B N    1 ? 2 
ATOM   3331 C CA   . TYR   B 1 101 ? 5.024   6.951  21.083  1   22.921 ? 113 TYR   B CA   1 ? 2 
ATOM   3332 C C    . TYR   B 1 101 ? 4.345   5.596  20.904  1   26.142 ? 113 TYR   B C    1 ? 2 
ATOM   3333 O O    . TYR   B 1 101 ? 4.201   5.119  19.772  1   25.513 ? 113 TYR   B O    1 ? 2 
ATOM   3334 C CB   . TYR   B 1 101 ? 6.399   6.988  20.412  1   24.973 ? 113 TYR   B CB   1 ? 2 
ATOM   3335 C CG   . TYR   B 1 101 ? 6.903   8.418  20.321  1   24.6   ? 113 TYR   B CG   1 ? 2 
ATOM   3336 C CD1  . TYR   B 1 101 ? 6.438   9.295  19.335  1   24.047 ? 113 TYR   B CD1  1 ? 2 
ATOM   3337 C CD2  . TYR   B 1 101 ? 7.778   8.925  21.272  1   23.209 ? 113 TYR   B CD2  1 ? 2 
ATOM   3338 C CE1  . TYR   B 1 101 ? 6.843   10.622 19.299  1   22.39  ? 113 TYR   B CE1  1 ? 2 
ATOM   3339 C CE2  . TYR   B 1 101 ? 8.205   10.242 21.237  1   21.721 ? 113 TYR   B CE2  1 ? 2 
ATOM   3340 C CZ   . TYR   B 1 101 ? 7.769   11.084 20.225  1   21.992 ? 113 TYR   B CZ   1 ? 2 
ATOM   3341 O OH   . TYR   B 1 101 ? 8.177   12.377 20.246  1   19.3   ? 113 TYR   B OH   1 ? 2 
ATOM   3342 H H    . TYR   B 1 101 ? 5.62    6.836  23.057  1   21.958 ? 113 TYR   B H    1 c 2 
ATOM   3343 H HA   . TYR   B 1 101 ? 4.457   7.623  20.623  1   23.499 ? 113 TYR   B HA   1 c 2 
ATOM   3344 H HB2  . TYR   B 1 101 ? 7.031   6.451  20.94   1   24.705 ? 113 TYR   B HB2  1 c 2 
ATOM   3345 H HB3  . TYR   B 1 101 ? 6.329   6.608  19.509  1   25.193 ? 113 TYR   B HB3  1 c 2 
ATOM   3346 H HD1  . TYR   B 1 101 ? 5.821   8.982  18.693  1   24.217 ? 113 TYR   B HD1  1 c 2 
ATOM   3347 H HD2  . TYR   B 1 101 ? 8.098   8.357  21.955  1   23.123 ? 113 TYR   B HD2  1 c 2 
ATOM   3348 H HE1  . TYR   B 1 101 ? 6.538   11.19  18.615  1   23.122 ? 113 TYR   B HE1  1 c 2 
ATOM   3349 H HE2  . TYR   B 1 101 ? 8.815   10.558 21.88   1   22.086 ? 113 TYR   B HE2  1 c 2 
ATOM   3350 H HH   . TYR   B 1 101 ? 7.714   12.809 19.674  0   30     ? 113 TYR   B HH   1 c 2 
ATOM   3351 N N    . GLY   B 1 102 ? 3.906   4.987  22.012  1   25.626 ? 114 GLY   B N    1 ? 2 
ATOM   3352 C CA   . GLY   B 1 102 ? 2.993   3.853  21.957  1   27.832 ? 114 GLY   B CA   1 ? 2 
ATOM   3353 C C    . GLY   B 1 102 ? 3.611   2.609  21.323  1   29.209 ? 114 GLY   B C    1 ? 2 
ATOM   3354 O O    . GLY   B 1 102 ? 4.825   2.46   21.244  1   28.625 ? 114 GLY   B O    1 ? 2 
ATOM   3355 H H    . GLY   B 1 102 ? 4.188   5.278  22.83   1   25.552 ? 114 GLY   B H    1 c 2 
ATOM   3356 H HA2  . GLY   B 1 102 ? 2.7     3.637  22.873  1   27.777 ? 114 GLY   B HA2  1 c 2 
ATOM   3357 H HA3  . GLY   B 1 102 ? 2.195   4.116  21.442  1   27.854 ? 114 GLY   B HA3  1 c 2 
ATOM   3358 N N    . SER   B 1 103 ? 2.75    1.702  20.862  1   29.813 ? 115 SER   B N    1 ? 2 
ATOM   3359 C CA   . SER   B 1 103 ? 3.217   0.453  20.279  1   31.352 ? 115 SER   B CA   1 ? 2 
ATOM   3360 C C    . SER   B 1 103 ? 3.834   0.667  18.897  1   30.052 ? 115 SER   B C    1 ? 2 
ATOM   3361 O O    . SER   B 1 103 ? 4.686   -0.122 18.507  1   29.455 ? 115 SER   B O    1 ? 2 
ATOM   3362 C CB   . SER   B 1 103 ? 2.134   -0.617 20.241  1   34.039 ? 115 SER   B CB   1 ? 2 
ATOM   3363 O OG   . SER   B 1 103 ? 1.035   -0.184 19.475  1   36.987 ? 115 SER   B OG   1 ? 2 
ATOM   3364 H H    . SER   B 1 103 ? 1.851   1.862  20.91   1   30.252 ? 115 SER   B H    1 c 2 
ATOM   3365 H HA   . SER   B 1 103 ? 3.938   0.113  20.865  1   31.164 ? 115 SER   B HA   1 c 2 
ATOM   3366 H HB2  . SER   B 1 103 ? 2.5     -1.435 19.853  1   35.517 ? 115 SER   B HB2  1 c 2 
ATOM   3367 H HB3  . SER   B 1 103 ? 1.841   -0.813 21.151  1   34.55  ? 115 SER   B HB3  1 c 2 
ATOM   3368 H HG   . SER   B 1 103 ? 0.431   -0.791 19.458  0   30     ? 115 SER   B HG   1 c 2 
ATOM   3369 N N    . ALA   B 1 104 ? 3.423   1.722  18.174  1   29.85  ? 116 ALA   B N    1 ? 2 
ATOM   3370 C CA   . ALA   B 1 104 ? 3.905   1.94   16.812  1   30.748 ? 116 ALA   B CA   1 ? 2 
ATOM   3371 C C    . ALA   B 1 104 ? 5.323   2.503  16.838  1   29.436 ? 116 ALA   B C    1 ? 2 
ATOM   3372 O O    . ALA   B 1 104 ? 6.125   2.24   15.939  1   29.397 ? 116 ALA   B O    1 ? 2 
ATOM   3373 C CB   . ALA   B 1 104 ? 2.956   2.85   16.072  1   31.61  ? 116 ALA   B CB   1 ? 2 
ATOM   3374 H H    . ALA   B 1 104 ? 2.828   2.316  18.532  1   29.249 ? 116 ALA   B H    1 c 2 
ATOM   3375 H HA   . ALA   B 1 104 ? 3.932   1.058  16.347  1   32.036 ? 116 ALA   B HA   1 c 2 
ATOM   3376 H HB1  . ALA   B 1 104 ? 2.075   2.442  16.033  1   32.256 ? 116 ALA   B HB1  1 c 2 
ATOM   3377 H HB2  . ALA   B 1 104 ? 2.895   3.703  16.534  1   30.271 ? 116 ALA   B HB2  1 c 2 
ATOM   3378 H HB3  . ALA   B 1 104 ? 3.282   2.998  15.168  1   32.089 ? 116 ALA   B HB3  1 c 2 
ATOM   3379 N N    . GLY   B 1 105 ? 5.637   3.21   17.927  1   27.843 ? 117 GLY   B N    1 ? 2 
ATOM   3380 C CA   . GLY   B 1 105 ? 6.894   3.928  18.052  1   27.112 ? 117 GLY   B CA   1 ? 2 
ATOM   3381 C C    . GLY   B 1 105 ? 6.988   5.071  17.039  1   27.485 ? 117 GLY   B C    1 ? 2 
ATOM   3382 O O    . GLY   B 1 105 ? 5.982   5.568  16.538  1   28.082 ? 117 GLY   B O    1 ? 2 
ATOM   3383 H H    . GLY   B 1 105 ? 5.042   3.255  18.618  1   27.442 ? 117 GLY   B H    1 c 2 
ATOM   3384 H HA2  . GLY   B 1 105 ? 6.97    4.29   18.966  1   26.385 ? 117 GLY   B HA2  1 c 2 
ATOM   3385 H HA3  . GLY   B 1 105 ? 7.641   3.299  17.911  1   27.822 ? 117 GLY   B HA3  1 c 2 
ATOM   3386 N N    . SER   B 1 106 ? 8.228   5.489  16.768  1   26.986 ? 118 SER   B N    1 ? 2 
ATOM   3387 C CA   . SER   B 1 106 ? 8.507   6.482  15.738  1   27.228 ? 118 SER   B CA   1 ? 2 
ATOM   3388 C C    . SER   B 1 106 ? 9.842   6.116  15.11   1   26.06  ? 118 SER   B C    1 ? 2 
ATOM   3389 O O    . SER   B 1 106 ? 10.831  6.791  15.32   1   25.791 ? 118 SER   B O    1 ? 2 
ATOM   3390 C CB   . SER   B 1 106 ? 8.483   7.874  16.329  1   25.039 ? 118 SER   B CB   1 ? 2 
ATOM   3391 O OG   . SER   B 1 106 ? 8.491   8.893  15.332  1   27.621 ? 118 SER   B OG   1 ? 2 
ATOM   3392 H H    . SER   B 1 106 ? 8.927   5.146  17.247  1   26.994 ? 118 SER   B H    1 c 2 
ATOM   3393 H HA   . SER   B 1 106 ? 7.806   6.421  15.04   1   27.258 ? 118 SER   B HA   1 c 2 
ATOM   3394 H HB2  . SER   B 1 106 ? 7.683   7.972  16.879  1   24.976 ? 118 SER   B HB2  1 c 2 
ATOM   3395 H HB3  . SER   B 1 106 ? 9.258   7.989  16.911  1   25.358 ? 118 SER   B HB3  1 c 2 
ATOM   3396 H HG   . SER   B 1 106 ? 8.504   9.703  15.752  0   30     ? 118 SER   B HG   1 c 2 
ATOM   3397 N N    . LEU   B 1 107 ? 9.845   5.002  14.385  1   26.922 ? 119 LEU   B N    1 ? 2 
ATOM   3398 C CA   . LEU   B 1 107 ? 11.07   4.384  13.894  1   29.306 ? 119 LEU   B CA   1 ? 2 
ATOM   3399 C C    . LEU   B 1 107 ? 11.639  5.233  12.764  1   30.254 ? 119 LEU   B C    1 ? 2 
ATOM   3400 O O    . LEU   B 1 107 ? 10.878  5.893  12.055  1   30.173 ? 119 LEU   B O    1 ? 2 
ATOM   3401 C CB   . LEU   B 1 107 ? 10.811  2.973  13.378  1   32.383 ? 119 LEU   B CB   1 ? 2 
ATOM   3402 C CG   . LEU   B 1 107 ? 10.706  1.854  14.411  1   34.625 ? 119 LEU   B CG   1 ? 2 
ATOM   3403 C CD1  . LEU   B 1 107 ? 11.974  1.722  15.247  1   34.503 ? 119 LEU   B CD1  1 ? 2 
ATOM   3404 C CD2  . LEU   B 1 107 ? 9.503   2.136  15.267  1   36.222 ? 119 LEU   B CD2  1 ? 2 
ATOM   3405 H H    . LEU   B 1 107 ? 9.045   4.612  14.175  1   27.617 ? 119 LEU   B H    1 c 2 
ATOM   3406 H HA   . LEU   B 1 107 ? 11.719  4.353  14.638  1   28.85  ? 119 LEU   B HA   1 c 2 
ATOM   3407 H HB2  . LEU   B 1 107 ? 9.977   2.989  12.855  1   32.909 ? 119 LEU   B HB2  1 c 2 
ATOM   3408 H HB3  . LEU   B 1 107 ? 11.531  2.741  12.748  1   33.764 ? 119 LEU   B HB3  1 c 2 
ATOM   3409 H HG   . LEU   B 1 107 ? 10.555  0.999  13.931  1   35.868 ? 119 LEU   B HG   1 c 2 
ATOM   3410 H HD11 . LEU   B 1 107 ? 12.747  1.668  14.66   1   35.481 ? 119 LEU   B HD11 1 c 2 
ATOM   3411 H HD12 . LEU   B 1 107 ? 11.923  0.916  15.788  1   34.643 ? 119 LEU   B HD12 1 c 2 
ATOM   3412 H HD13 . LEU   B 1 107 ? 12.063  2.495  15.829  1   33.312 ? 119 LEU   B HD13 1 c 2 
ATOM   3413 H HD21 . LEU   B 1 107 ? 8.737   2.33   14.701  1   35.358 ? 119 LEU   B HD21 1 c 2 
ATOM   3414 H HD22 . LEU   B 1 107 ? 9.682   2.899  15.839  1   33.987 ? 119 LEU   B HD22 1 c 2 
ATOM   3415 H HD23 . LEU   B 1 107 ? 9.308   1.36   15.817  1   35.296 ? 119 LEU   B HD23 1 c 2 
ATOM   3416 N N    . PRO   B 1 108 ? 12.97   5.179  12.517  1   30.556 ? 120 PRO   B N    1 ? 2 
ATOM   3417 C CA   . PRO   B 1 108 ? 13.887  4.362  13.312  1   31.314 ? 120 PRO   B CA   1 ? 2 
ATOM   3418 C C    . PRO   B 1 108 ? 14.405  5.008  14.6    1   31.006 ? 120 PRO   B C    1 ? 2 
ATOM   3419 O O    . PRO   B 1 108 ? 15.093  4.341  15.354  1   31.483 ? 120 PRO   B O    1 ? 2 
ATOM   3420 C CB   . PRO   B 1 108 ? 15.053  4.119  12.384  1   33.833 ? 120 PRO   B CB   1 ? 2 
ATOM   3421 C CG   . PRO   B 1 108 ? 15.045  5.35   11.5    1   33.836 ? 120 PRO   B CG   1 ? 2 
ATOM   3422 C CD   . PRO   B 1 108 ? 13.631  5.804  11.362  1   32.708 ? 120 PRO   B CD   1 ? 2 
ATOM   3423 H HA   . PRO   B 1 108 ? 13.467  3.507  13.524  1   31.357 ? 120 PRO   B HA   1 c 2 
ATOM   3424 H HB2  . PRO   B 1 108 ? 15.892  4.047  12.879  1   33.763 ? 120 PRO   B HB2  1 c 2 
ATOM   3425 H HB3  . PRO   B 1 108 ? 14.918  3.308  11.856  1   34.614 ? 120 PRO   B HB3  1 c 2 
ATOM   3426 H HG2  . PRO   B 1 108 ? 15.587  6.059  11.901  1   33.699 ? 120 PRO   B HG2  1 c 2 
ATOM   3427 H HG3  . PRO   B 1 108 ? 15.417  5.14   10.621  1   35.716 ? 120 PRO   B HG3  1 c 2 
ATOM   3428 H HD2  . PRO   B 1 108 ? 13.564  6.776  11.406  1   32.359 ? 120 PRO   B HD2  1 c 2 
ATOM   3429 H HD3  . PRO   B 1 108 ? 13.236  5.49   10.526  1   33.809 ? 120 PRO   B HD3  1 c 2 
ATOM   3430 N N    . LYS   B 1 109 ? 14.065  6.277  14.855  1   31.083 ? 121 LYS   B N    1 ? 2 
ATOM   3431 C CA   . LYS   B 1 109 ? 14.538  7.002  16.032  1   30.708 ? 121 LYS   B CA   1 ? 2 
ATOM   3432 C C    . LYS   B 1 109 ? 14.029  6.402  17.351  1   29.519 ? 121 LYS   B C    1 ? 2 
ATOM   3433 O O    . LYS   B 1 109 ? 14.81   6.258  18.283  1   29.817 ? 121 LYS   B O    1 ? 2 
ATOM   3434 C CB   . LYS   B 1 109 ? 14.101  8.469  15.946  1   31.339 ? 121 LYS   B CB   1 ? 2 
ATOM   3435 C CG   . LYS   B 1 109 ? 14.665  9.415  17.033  1   31.428 ? 121 LYS   B CG   1 ? 2 
ATOM   3436 C CD   . LYS   B 1 109 ? 14.179  10.859 16.993  1   32.541 ? 121 LYS   B CD   1 ? 2 
ATOM   3437 C CE   . LYS   B 1 109 ? 14.562  11.659 15.789  1   35.402 ? 121 LYS   B CE   1 ? 2 
ATOM   3438 N NZ   . LYS   B 1 109 ? 16.006  11.671 15.58   1   37.157 ? 121 LYS   B NZ   1 ? 2 
ATOM   3439 H H    . LYS   B 1 109 ? 13.516  6.715  14.269  1   30.998 ? 121 LYS   B H    1 c 2 
ATOM   3440 H HA   . LYS   B 1 109 ? 15.529  6.969  16.035  1   31.786 ? 121 LYS   B HA   1 c 2 
ATOM   3441 H HB2  . LYS   B 1 109 ? 14.365  8.819  15.069  1   32.369 ? 121 LYS   B HB2  1 c 2 
ATOM   3442 H HB3  . LYS   B 1 109 ? 13.121  8.501  15.992  1   30.345 ? 121 LYS   B HB3  1 c 2 
ATOM   3443 H HG2  . LYS   B 1 109 ? 14.444  9.039  17.911  1   30.773 ? 121 LYS   B HG2  1 c 2 
ATOM   3444 H HG3  . LYS   B 1 109 ? 15.644  9.414  16.958  1   32.713 ? 121 LYS   B HG3  1 c 2 
ATOM   3445 H HD2  . LYS   B 1 109 ? 13.2    10.853 17.064  1   31.531 ? 121 LYS   B HD2  1 c 2 
ATOM   3446 H HD3  . LYS   B 1 109 ? 14.52   11.317 17.792  1   32.224 ? 121 LYS   B HD3  1 c 2 
ATOM   3447 H HE2  . LYS   B 1 109 ? 14.13   11.284 15.001  1   35.451 ? 121 LYS   B HE2  1 c 2 
ATOM   3448 H HE3  . LYS   B 1 109 ? 14.252  12.576 15.897  1   34.97  ? 121 LYS   B HE3  1 c 2 
ATOM   3449 H HZ1  . LYS   B 1 109 ? 16.265  10.899 15.182  1   37.628 ? 121 LYS   B HZ1  1 c 2 
ATOM   3450 H HZ2  . LYS   B 1 109 ? 16.434  11.756 16.374  1   36.9   ? 121 LYS   B HZ2  1 c 2 
ATOM   3451 H HZ3  . LYS   B 1 109 ? 16.23   12.368 15.046  1   38.223 ? 121 LYS   B HZ3  1 c 2 
ATOM   3452 N N    . ILE   B 1 110 ? 12.716  6.154  17.474  1   28.268 ? 122 ILE   B N    1 ? 2 
ATOM   3453 C CA   . ILE   B 1 110 ? 12.137  5.673  18.723  1   27.523 ? 122 ILE   B CA   1 ? 2 
ATOM   3454 C C    . ILE   B 1 110 ? 11.514  4.312  18.465  1   27.611 ? 122 ILE   B C    1 ? 2 
ATOM   3455 O O    . ILE   B 1 110 ? 10.576  4.204  17.658  1   27.718 ? 122 ILE   B O    1 ? 2 
ATOM   3456 C CB   . ILE   B 1 110 ? 11.046  6.614  19.271  1   28.471 ? 122 ILE   B CB   1 ? 2 
ATOM   3457 C CG1  . ILE   B 1 110 ? 11.463  8.083  19.31   1   30.676 ? 122 ILE   B CG1  1 ? 2 
ATOM   3458 C CG2  . ILE   B 1 110 ? 10.53   6.145  20.63   1   28.214 ? 122 ILE   B CG2  1 ? 2 
ATOM   3459 C CD1  . ILE   B 1 110 ? 12.724  8.347  20.069  1   31.826 ? 122 ILE   B CD1  1 ? 2 
ATOM   3460 H H    . ILE   B 1 110 ? 12.165  6.292  16.758  1   28.495 ? 122 ILE   B H    1 c 2 
ATOM   3461 H HA   . ILE   B 1 110 ? 12.842  5.585  19.391  1   28.042 ? 122 ILE   B HA   1 c 2 
ATOM   3462 H HB   . ILE   B 1 110 ? 10.292  6.559  18.65   1   28.478 ? 122 ILE   B HB   1 c 2 
ATOM   3463 H HG12 . ILE   B 1 110 ? 11.578  8.4    18.391  1   30.785 ? 122 ILE   B HG12 1 c 2 
ATOM   3464 H HG13 . ILE   B 1 110 ? 10.739  8.603  19.714  1   29.484 ? 122 ILE   B HG13 1 c 2 
ATOM   3465 H HG21 . ILE   B 1 110 ? 9.995   6.848  21.036  1   27.406 ? 122 ILE   B HG21 1 c 2 
ATOM   3466 H HG22 . ILE   B 1 110 ? 11.282  5.938  21.21   1   28.433 ? 122 ILE   B HG22 1 c 2 
ATOM   3467 H HG23 . ILE   B 1 110 ? 9.983   5.35   20.516  1   28.264 ? 122 ILE   B HG23 1 c 2 
ATOM   3468 H HD11 . ILE   B 1 110 ? 12.608  8.092  21.004  1   31.172 ? 122 ILE   B HD11 1 c 2 
ATOM   3469 H HD12 . ILE   B 1 110 ? 12.912  9.301  20.014  1   31.536 ? 122 ILE   B HD12 1 c 2 
ATOM   3470 H HD13 . ILE   B 1 110 ? 13.469  7.848  19.687  1   32.316 ? 122 ILE   B HD13 1 c 2 
ATOM   3471 N N    . PRO   B 1 111 ? 11.929  3.26   19.192  1   28.452 ? 123 PRO   B N    1 ? 2 
ATOM   3472 C CA   . PRO   B 1 111 ? 11.352  1.937  18.996  1   29.881 ? 123 PRO   B CA   1 ? 2 
ATOM   3473 C C    . PRO   B 1 111 ? 9.949   1.822  19.579  1   28.315 ? 123 PRO   B C    1 ? 2 
ATOM   3474 O O    . PRO   B 1 111 ? 9.466   2.714  20.268  1   28.016 ? 123 PRO   B O    1 ? 2 
ATOM   3475 C CB   . PRO   B 1 111 ? 12.381  1.006  19.621  1   32.663 ? 123 PRO   B CB   1 ? 2 
ATOM   3476 C CG   . PRO   B 1 111 ? 12.941  1.845  20.738  1   31.701 ? 123 PRO   B CG   1 ? 2 
ATOM   3477 C CD   . PRO   B 1 111 ? 12.977  3.258  20.224  1   31.157 ? 123 PRO   B CD   1 ? 2 
ATOM   3478 H HA   . PRO   B 1 111 ? 11.31   1.75   18.035  1   30.546 ? 123 PRO   B HA   1 c 2 
ATOM   3479 H HB2  . PRO   B 1 111 ? 11.959  0.194  19.966  1   32.693 ? 123 PRO   B HB2  1 c 2 
ATOM   3480 H HB3  . PRO   B 1 111 ? 13.075  0.765  18.977  1   33.168 ? 123 PRO   B HB3  1 c 2 
ATOM   3481 H HG2  . PRO   B 1 111 ? 12.372  1.787  21.531  1   31.379 ? 123 PRO   B HG2  1 c 2 
ATOM   3482 H HG3  . PRO   B 1 111 ? 13.841  1.546  20.976  1   32.733 ? 123 PRO   B HG3  1 c 2 
ATOM   3483 H HD2  . PRO   B 1 111 ? 12.77   3.899  20.931  1   29.663 ? 123 PRO   B HD2  1 c 2 
ATOM   3484 H HD3  . PRO   B 1 111 ? 13.847  3.474  19.835  1   31.102 ? 123 PRO   B HD3  1 c 2 
ATOM   3485 N N    . SER   B 1 112 ? 9.287   0.739  19.196  1   27.872 ? 124 SER   B N    1 ? 2 
ATOM   3486 C CA   . SER   B 1 112 ? 8.016   0.325  19.737  1   29.249 ? 124 SER   B CA   1 ? 2 
ATOM   3487 C C    . SER   B 1 112 ? 8.122   0.205  21.263  1   29.128 ? 124 SER   B C    1 ? 2 
ATOM   3488 O O    . SER   B 1 112 ? 9.152   -0.191 21.773  1   28.835 ? 124 SER   B O    1 ? 2 
ATOM   3489 C CB   . SER   B 1 112 ? 7.631   -0.977 19.078  1   33.602 ? 124 SER   B CB   1 ? 2 
ATOM   3490 O OG   . SER   B 1 112 ? 6.454   -1.504 19.655  1   38.229 ? 124 SER   B OG   1 ? 2 
ATOM   3491 H H    . SER   B 1 112 ? 9.662   0.219  18.544  1   29.571 ? 124 SER   B H    1 c 2 
ATOM   3492 H HA   . SER   B 1 112 ? 7.339   1.013  19.514  1   28.709 ? 124 SER   B HA   1 c 2 
ATOM   3493 H HB2  . SER   B 1 112 ? 7.487   -0.827 18.124  1   34.192 ? 124 SER   B HB2  1 c 2 
ATOM   3494 H HB3  . SER   B 1 112 ? 8.359   -1.62  19.18   1   34.69  ? 124 SER   B HB3  1 c 2 
ATOM   3495 H HG   . SER   B 1 112 ? 6.312   -2.195 19.226  0   30     ? 124 SER   B HG   1 c 2 
ATOM   3496 N N    . ASN   B 1 113 ? 7.083   0.646  21.968  1   27.166 ? 125 ASN   B N    1 ? 2 
ATOM   3497 C CA   . ASN   B 1 113 ? 6.927   0.396  23.398  1   28.518 ? 125 ASN   B CA   1 ? 2 
ATOM   3498 C C    . ASN   B 1 113 ? 8.071   0.993  24.212  1   29.244 ? 125 ASN   B C    1 ? 2 
ATOM   3499 O O    . ASN   B 1 113 ? 8.462   0.413  25.236  1   32.868 ? 125 ASN   B O    1 ? 2 
ATOM   3500 C CB   . ASN   B 1 113 ? 6.745   -1.095 23.632  1   30.965 ? 125 ASN   B CB   1 ? 2 
ATOM   3501 C CG   . ASN   B 1 113 ? 5.513   -1.598 22.937  1   31.745 ? 125 ASN   B CG   1 ? 2 
ATOM   3502 O OD1  . ASN   B 1 113 ? 4.459   -0.953 23.027  1   32.946 ? 125 ASN   B OD1  1 ? 2 
ATOM   3503 N ND2  . ASN   B 1 113 ? 5.675   -2.649 22.15   1   34.084 ? 125 ASN   B ND2  1 ? 2 
ATOM   3504 H H    . ASN   B 1 113 ? 6.436   1.13   21.541  1   27.226 ? 125 ASN   B H    1 c 2 
ATOM   3505 H HA   . ASN   B 1 113 ? 6.097   0.838  23.688  1   28.111 ? 125 ASN   B HA   1 c 2 
ATOM   3506 H HB2  . ASN   B 1 113 ? 7.528   -1.577 23.3    1   31.518 ? 125 ASN   B HB2  1 c 2 
ATOM   3507 H HB3  . ASN   B 1 113 ? 6.664   -1.265 24.591  1   31.284 ? 125 ASN   B HB3  1 c 2 
ATOM   3508 H HD21 . ASN   B 1 113 ? 5.085   -2.812 21.507  1   34.27  ? 125 ASN   B HD21 1 c 2 
ATOM   3509 H HD22 . ASN   B 1 113 ? 6.368   -3.193 22.265  1   34.571 ? 125 ASN   B HD22 1 c 2 
ATOM   3510 N N    . ALA   B 1 114 ? 8.517   2.201  23.835  1   26.995 ? 126 ALA   B N    1 ? 2 
ATOM   3511 C CA   . ALA   B 1 114 ? 9.644   2.829  24.509  1   27.633 ? 126 ALA   B CA   1 ? 2 
ATOM   3512 C C    . ALA   B 1 114 ? 9.183   3.65   25.721  1   26.42  ? 126 ALA   B C    1 ? 2 
ATOM   3513 O O    . ALA   B 1 114 ? 8.189   4.4    25.642  1   24.932 ? 126 ALA   B O    1 ? 2 
ATOM   3514 C CB   . ALA   B 1 114 ? 10.404  3.684  23.531  1   27.897 ? 126 ALA   B CB   1 ? 2 
ATOM   3515 H H    . ALA   B 1 114 ? 8.106   2.646  23.151  1   26.827 ? 126 ALA   B H    1 c 2 
ATOM   3516 H HA   . ALA   B 1 114 ? 10.248  2.107  24.835  1   28.606 ? 126 ALA   B HA   1 c 2 
ATOM   3517 H HB1  . ALA   B 1 114 ? 10.718  3.136  22.792  1   28.23  ? 126 ALA   B HB1  1 c 2 
ATOM   3518 H HB2  . ALA   B 1 114 ? 9.823   4.383  23.188  1   26.853 ? 126 ALA   B HB2  1 c 2 
ATOM   3519 H HB3  . ALA   B 1 114 ? 11.167  4.09   23.976  1   27.807 ? 126 ALA   B HB3  1 c 2 
ATOM   3520 N N    . THR   B 1 115 ? 9.949   3.52   26.821  1   26.459 ? 127 THR   B N    1 ? 2 
ATOM   3521 C CA   . THR   B 1 115 ? 9.858   4.429  27.957  1   26.62  ? 127 THR   B CA   1 ? 2 
ATOM   3522 C C    . THR   B 1 115 ? 10.821  5.602  27.764  1   26.414 ? 127 THR   B C    1 ? 2 
ATOM   3523 O O    . THR   B 1 115 ? 11.991  5.386  27.46   1   26.346 ? 127 THR   B O    1 ? 2 
ATOM   3524 C CB   . THR   B 1 115 ? 10.172  3.673  29.251  1   28.128 ? 127 THR   B CB   1 ? 2 
ATOM   3525 O OG1  . THR   B 1 115 ? 9.099   2.756  29.32   1   29.286 ? 127 THR   B OG1  1 ? 2 
ATOM   3526 C CG2  . THR   B 1 115 ? 10.086  4.527  30.5    1   29.65  ? 127 THR   B CG2  1 ? 2 
ATOM   3527 H H    . THR   B 1 115 ? 10.551  2.834  26.862  1   27.689 ? 127 THR   B H    1 c 2 
ATOM   3528 H HA   . THR   B 1 115 ? 8.941   4.773  28.009  1   25.916 ? 127 THR   B HA   1 c 2 
ATOM   3529 H HB   . THR   B 1 115 ? 11.032  3.192  29.193  1   29.486 ? 127 THR   B HB   1 c 2 
ATOM   3530 H HG1  . THR   B 1 115 ? 8.362   3.31   29.38   0   30     ? 127 THR   B HG1  1 c 2 
ATOM   3531 H HG21 . THR   B 1 115 ? 10.211  3.967  31.285  1   30.646 ? 127 THR   B HG21 1 c 2 
ATOM   3532 H HG22 . THR   B 1 115 ? 9.213   4.952  30.544  1   28.548 ? 127 THR   B HG22 1 c 2 
ATOM   3533 H HG23 . THR   B 1 115 ? 10.777  5.21   30.478  1   29.16  ? 127 THR   B HG23 1 c 2 
ATOM   3534 N N    . LEU   B 1 116 ? 10.324  6.83   28.005  1   24.653 ? 128 LEU   B N    1 ? 2 
ATOM   3535 C CA   . LEU   B 1 116 ? 11.112  8.031  27.819  1   26.215 ? 128 LEU   B CA   1 ? 2 
ATOM   3536 C C    . LEU   B 1 116 ? 11.354  8.742  29.153  1   26.953 ? 128 LEU   B C    1 ? 2 
ATOM   3537 O O    . LEU   B 1 116 ? 10.513  8.732  30.05   1   27.909 ? 128 LEU   B O    1 ? 2 
ATOM   3538 C CB   . LEU   B 1 116 ? 10.473  9.012  26.847  1   25.577 ? 128 LEU   B CB   1 ? 2 
ATOM   3539 C CG   . LEU   B 1 116 ? 10.052  8.46   25.476  1   27.218 ? 128 LEU   B CG   1 ? 2 
ATOM   3540 C CD1  . LEU   B 1 116 ? 9.779   9.67   24.568  1   27.385 ? 128 LEU   B CD1  1 ? 2 
ATOM   3541 C CD2  . LEU   B 1 116 ? 11.043  7.594  24.825  1   29.38  ? 128 LEU   B CD2  1 ? 2 
ATOM   3542 H H    . LEU   B 1 116 ? 9.462   6.914  28.298  1   24.898 ? 128 LEU   B H    1 c 2 
ATOM   3543 H HA   . LEU   B 1 116 ? 11.994  7.762  27.457  1   26.522 ? 128 LEU   B HA   1 c 2 
ATOM   3544 H HB2  . LEU   B 1 116 ? 9.677   9.396  27.282  1   25.523 ? 128 LEU   B HB2  1 c 2 
ATOM   3545 H HB3  . LEU   B 1 116 ? 11.108  9.751  26.701  1   26.143 ? 128 LEU   B HB3  1 c 2 
ATOM   3546 H HG   . LEU   B 1 116 ? 9.209   7.95   25.586  1   26.966 ? 128 LEU   B HG   1 c 2 
ATOM   3547 H HD11 . LEU   B 1 116 ? 9.146   10.266 25.002  1   26.756 ? 128 LEU   B HD11 1 c 2 
ATOM   3548 H HD12 . LEU   B 1 116 ? 9.408   9.364  23.724  1   26.909 ? 128 LEU   B HD12 1 c 2 
ATOM   3549 H HD13 . LEU   B 1 116 ? 10.61   10.146 24.402  1   27.532 ? 128 LEU   B HD13 1 c 2 
ATOM   3550 H HD21 . LEU   B 1 116 ? 11.067  6.732  25.271  1   29.389 ? 128 LEU   B HD21 1 c 2 
ATOM   3551 H HD22 . LEU   B 1 116 ? 11.919  8.01   24.878  1   29.466 ? 128 LEU   B HD22 1 c 2 
ATOM   3552 H HD23 . LEU   B 1 116 ? 10.801  7.467  23.892  1   28.718 ? 128 LEU   B HD23 1 c 2 
ATOM   3553 N N    . PHE   B 1 117 ? 12.502  9.435  29.198  1   27.151 ? 129 PHE   B N    1 ? 2 
ATOM   3554 C CA   . PHE   B 1 117 ? 12.868  10.298 30.299  1   29.131 ? 129 PHE   B CA   1 ? 2 
ATOM   3555 C C    . PHE   B 1 117 ? 13.219  11.688 29.772  1   30.429 ? 129 PHE   B C    1 ? 2 
ATOM   3556 O O    . PHE   B 1 117 ? 13.968  11.819 28.799  1   30.751 ? 129 PHE   B O    1 ? 2 
ATOM   3557 C CB   . PHE   B 1 117 ? 14.057  9.679  31.03   1   30.457 ? 129 PHE   B CB   1 ? 2 
ATOM   3558 C CG   . PHE   B 1 117 ? 14.587  10.581 32.125  1   32.093 ? 129 PHE   B CG   1 ? 2 
ATOM   3559 C CD1  . PHE   B 1 117 ? 14.084  10.495 33.416  1   33.212 ? 129 PHE   B CD1  1 ? 2 
ATOM   3560 C CD2  . PHE   B 1 117 ? 15.578  11.516 31.856  1   33.129 ? 129 PHE   B CD2  1 ? 2 
ATOM   3561 C CE1  . PHE   B 1 117 ? 14.567  11.313 34.419  1   34.54  ? 129 PHE   B CE1  1 ? 2 
ATOM   3562 C CE2  . PHE   B 1 117 ? 16.024  12.361 32.854  1   35.761 ? 129 PHE   B CE2  1 ? 2 
ATOM   3563 C CZ   . PHE   B 1 117 ? 15.516  12.258 34.137  1   36.39  ? 129 PHE   B CZ   1 ? 2 
ATOM   3564 H H    . PHE   B 1 117 ? 13.085  9.361  28.499  1   27.556 ? 129 PHE   B H    1 c 2 
ATOM   3565 H HA   . PHE   B 1 117 ? 12.103  10.368 30.925  1   28.936 ? 129 PHE   B HA   1 c 2 
ATOM   3566 H HB2  . PHE   B 1 117 ? 13.776  8.823  31.423  1   30.934 ? 129 PHE   B HB2  1 c 2 
ATOM   3567 H HB3  . PHE   B 1 117 ? 14.773  9.504  30.38   1   30.826 ? 129 PHE   B HB3  1 c 2 
ATOM   3568 H HD1  . PHE   B 1 117 ? 13.42   9.854  33.615  1   32.725 ? 129 PHE   B HD1  1 c 2 
ATOM   3569 H HD2  . PHE   B 1 117 ? 15.913  11.605 30.977  1   32.806 ? 129 PHE   B HD2  1 c 2 
ATOM   3570 H HE1  . PHE   B 1 117 ? 14.211  11.249 35.291  1   35.779 ? 129 PHE   B HE1  1 c 2 
ATOM   3571 H HE2  . PHE   B 1 117 ? 16.694  12.994 32.664  1   36.278 ? 129 PHE   B HE2  1 c 2 
ATOM   3572 H HZ   . PHE   B 1 117 ? 15.844  12.818 34.822  1   37.729 ? 129 PHE   B HZ   1 c 2 
ATOM   3573 N N    . PHE   B 1 118 ? 12.741  12.721 30.479  1   28.277 ? 130 PHE   B N    1 ? 2 
ATOM   3574 C CA   . PHE   B 1 118 ? 13.083  14.099 30.167  1   29.501 ? 130 PHE   B CA   1 ? 2 
ATOM   3575 C C    . PHE   B 1 118 ? 13.415  14.878 31.438  1   30.742 ? 130 PHE   B C    1 ? 2 
ATOM   3576 O O    . PHE   B 1 118 ? 12.789  14.687 32.48   1   31.138 ? 130 PHE   B O    1 ? 2 
ATOM   3577 C CB   . PHE   B 1 118 ? 11.98   14.893 29.473  1   27.136 ? 130 PHE   B CB   1 ? 2 
ATOM   3578 C CG   . PHE   B 1 118 ? 11.543  14.374 28.107  1   26.4   ? 130 PHE   B CG   1 ? 2 
ATOM   3579 C CD1  . PHE   B 1 118 ? 10.602  13.358 28      1   24.203 ? 130 PHE   B CD1  1 ? 2 
ATOM   3580 C CD2  . PHE   B 1 118 ? 12.081  14.926 26.944  1   27.126 ? 130 PHE   B CD2  1 ? 2 
ATOM   3581 C CE1  . PHE   B 1 118 ? 10.194  12.915 26.749  1   25.929 ? 130 PHE   B CE1  1 ? 2 
ATOM   3582 C CE2  . PHE   B 1 118 ? 11.655  14.498 25.695  1   25.971 ? 130 PHE   B CE2  1 ? 2 
ATOM   3583 C CZ   . PHE   B 1 118 ? 10.735  13.483 25.601  1   26.381 ? 130 PHE   B CZ   1 ? 2 
ATOM   3584 H H    . PHE   B 1 118 ? 12.18   12.559 31.182  1   29.079 ? 130 PHE   B H    1 c 2 
ATOM   3585 H HA   . PHE   B 1 118 ? 13.881  14.096 29.581  1   29.55  ? 130 PHE   B HA   1 c 2 
ATOM   3586 H HB2  . PHE   B 1 118 ? 11.196  14.911 30.066  1   27.226 ? 130 PHE   B HB2  1 c 2 
ATOM   3587 H HB3  . PHE   B 1 118 ? 12.289  15.821 29.37   1   28.108 ? 130 PHE   B HB3  1 c 2 
ATOM   3588 H HD1  . PHE   B 1 118 ? 10.233  12.977 28.781  1   25.176 ? 130 PHE   B HD1  1 c 2 
ATOM   3589 H HD2  . PHE   B 1 118 ? 12.707  15.629 27.009  1   27.868 ? 130 PHE   B HD2  1 c 2 
ATOM   3590 H HE1  . PHE   B 1 118 ? 9.557   12.222 26.679  1   24.825 ? 130 PHE   B HE1  1 c 2 
ATOM   3591 H HE2  . PHE   B 1 118 ? 12.03   14.873 24.914  1   26.719 ? 130 PHE   B HE2  1 c 2 
ATOM   3592 H HZ   . PHE   B 1 118 ? 10.459  13.176 24.752  1   25.535 ? 130 PHE   B HZ   1 c 2 
ATOM   3593 N N    . GLU   B 1 119 ? 14.407  15.764 31.297  1   32.309 ? 131 GLU   B N    1 ? 2 
ATOM   3594 C CA   . GLU   B 1 119 ? 14.605  16.906 32.172  1   34.162 ? 131 GLU   B CA   1 ? 2 
ATOM   3595 C C    . GLU   B 1 119 ? 14.207  18.158 31.389  1   34.625 ? 131 GLU   B C    1 ? 2 
ATOM   3596 O O    . GLU   B 1 119 ? 14.71   18.399 30.295  1   36.343 ? 131 GLU   B O    1 ? 2 
ATOM   3597 C CB   . GLU   B 1 119 ? 16.046  16.878 32.685  1   36.126 ? 131 GLU   B CB   1 ? 2 
ATOM   3598 C CG   . GLU   B 1 119 ? 16.456  18.053 33.579  1   38.351 ? 131 GLU   B CG   1 ? 2 
ATOM   3599 C CD   . GLU   B 1 119 ? 17.916  17.955 34.015  1   41.122 ? 131 GLU   B CD   1 ? 2 
ATOM   3600 O OE1  . GLU   B 1 119 ? 18.282  17.097 34.843  1   41.846 ? 131 GLU   B OE1  1 ? 2 
ATOM   3601 O OE2  . GLU   B 1 119 ? 18.736  18.753 33.527  1   44.261 ? 131 GLU   B OE2  1 ? 2 
ATOM   3602 H H    . GLU   B 1 119 ? 15.001  15.644 30.612  1   32.388 ? 131 GLU   B H    1 c 2 
ATOM   3603 H HA   . GLU   B 1 119 ? 13.999  16.811 32.948  1   34.23  ? 131 GLU   B HA   1 c 2 
ATOM   3604 H HB2  . GLU   B 1 119 ? 16.181  16.048 33.188  1   36.549 ? 131 GLU   B HB2  1 c 2 
ATOM   3605 H HB3  . GLU   B 1 119 ? 16.65   16.857 31.913  1   36.265 ? 131 GLU   B HB3  1 c 2 
ATOM   3606 H HG2  . GLU   B 1 119 ? 16.327  18.895 33.092  1   38.238 ? 131 GLU   B HG2  1 c 2 
ATOM   3607 H HG3  . GLU   B 1 119 ? 15.887  18.071 34.377  1   38.534 ? 131 GLU   B HG3  1 c 2 
ATOM   3608 N N    . ILE   B 1 120 ? 13.278  18.93  31.959  1   35.338 ? 132 ILE   B N    1 ? 2 
ATOM   3609 C CA   . ILE   B 1 120 ? 12.645  20.06  31.297  1   34.01  ? 132 ILE   B CA   1 ? 2 
ATOM   3610 C C    . ILE   B 1 120 ? 12.766  21.291 32.188  1   36.797 ? 132 ILE   B C    1 ? 2 
ATOM   3611 O O    . ILE   B 1 120 ? 12.381  21.234 33.351  1   36.425 ? 132 ILE   B O    1 ? 2 
ATOM   3612 C CB   . ILE   B 1 120 ? 11.156  19.783 31.031  1   32.269 ? 132 ILE   B CB   1 ? 2 
ATOM   3613 C CG1  . ILE   B 1 120 ? 10.918  18.457 30.279  1   30.755 ? 132 ILE   B CG1  1 ? 2 
ATOM   3614 C CG2  . ILE   B 1 120 ? 10.514  20.987 30.336  1   32.491 ? 132 ILE   B CG2  1 ? 2 
ATOM   3615 C CD1  . ILE   B 1 120 ? 9.46    18.045 30.166  1   30.587 ? 132 ILE   B CD1  1 ? 2 
ATOM   3616 H H    . ILE   B 1 120 ? 13.025  18.742 32.817  1   35.359 ? 132 ILE   B H    1 c 2 
ATOM   3617 H HA   . ILE   B 1 120 ? 13.095  20.229 30.447  1   34.376 ? 132 ILE   B HA   1 c 2 
ATOM   3618 H HB   . ILE   B 1 120 ? 10.724  19.694 31.904  1   32.58  ? 132 ILE   B HB   1 c 2 
ATOM   3619 H HG12 . ILE   B 1 120 ? 11.29   18.539 29.377  1   30.802 ? 132 ILE   B HG12 1 c 2 
ATOM   3620 H HG13 . ILE   B 1 120 ? 11.406  17.744 30.738  1   31.332 ? 132 ILE   B HG13 1 c 2 
ATOM   3621 H HG21 . ILE   B 1 120 ? 9.612   20.761 30.057  1   31.257 ? 132 ILE   B HG21 1 c 2 
ATOM   3622 H HG22 . ILE   B 1 120 ? 11.041  21.231 29.556  1   32.657 ? 132 ILE   B HG22 1 c 2 
ATOM   3623 H HG23 . ILE   B 1 120 ? 10.48   21.74  30.95   1   33.567 ? 132 ILE   B HG23 1 c 2 
ATOM   3624 H HD11 . ILE   B 1 120 ? 9.027   18.135 31.036  1   30.558 ? 132 ILE   B HD11 1 c 2 
ATOM   3625 H HD12 . ILE   B 1 120 ? 9.406   17.116 29.872  1   29.393 ? 132 ILE   B HD12 1 c 2 
ATOM   3626 H HD13 . ILE   B 1 120 ? 9.005   18.616 29.518  1   29.794 ? 132 ILE   B HD13 1 c 2 
ATOM   3627 N N    . GLU   B 1 121 ? 13.222  22.409 31.612  1   38.45  ? 133 GLU   B N    1 ? 2 
ATOM   3628 C CA   . GLU   B 1 121 ? 13.162  23.699 32.278  1   41.151 ? 133 GLU   B CA   1 ? 2 
ATOM   3629 C C    . GLU   B 1 121 ? 12.119  24.571 31.589  1   39.713 ? 133 GLU   B C    1 ? 2 
ATOM   3630 O O    . GLU   B 1 121 ? 12.194  24.795 30.385  1   38.08  ? 133 GLU   B O    1 ? 2 
ATOM   3631 C CB   . GLU   B 1 121 ? 14.531  24.374 32.226  1   43.381 ? 133 GLU   B CB   1 ? 2 
ATOM   3632 C CG   . GLU   B 1 121 ? 14.544  25.773 32.851  1   46.307 ? 133 GLU   B CG   1 ? 2 
ATOM   3633 C CD   . GLU   B 1 121 ? 15.921  26.407 32.904  1   48.68  ? 133 GLU   B CD   1 ? 2 
ATOM   3634 O OE1  . GLU   B 1 121 ? 16.864  25.729 32.517  1   50.35  ? 133 GLU   B OE1  1 ? 2 
ATOM   3635 O OE2  . GLU   B 1 121 ? 16.091  27.549 33.334  1   52.568 ? 133 GLU   B OE2  1 ? 2 
ATOM   3636 H H    . GLU   B 1 121 ? 13.585  22.365 30.774  1   38.208 ? 133 GLU   B H    1 c 2 
ATOM   3637 H HA   . GLU   B 1 121 ? 12.903  23.56  33.222  1   41.213 ? 133 GLU   B HA   1 c 2 
ATOM   3638 H HB2  . GLU   B 1 121 ? 15.181  23.804 32.687  1   44.197 ? 133 GLU   B HB2  1 c 2 
ATOM   3639 H HB3  . GLU   B 1 121 ? 14.811  24.446 31.29   1   43.255 ? 133 GLU   B HB3  1 c 2 
ATOM   3640 H HG2  . GLU   B 1 121 ? 13.951  26.36  32.338  1   45.644 ? 133 GLU   B HG2  1 c 2 
ATOM   3641 H HG3  . GLU   B 1 121 ? 14.191  25.718 33.764  1   46.409 ? 133 GLU   B HG3  1 c 2 
ATOM   3642 N N    . LEU   B 1 122 ? 11.144  25.053 32.363  1   39.626 ? 134 LEU   B N    1 ? 2 
ATOM   3643 C CA   . LEU   B 1 122 ? 10.162  25.979 31.831  1   40.463 ? 134 LEU   B CA   1 ? 2 
ATOM   3644 C C    . LEU   B 1 122 ? 10.739  27.391 31.891  1   43.512 ? 134 LEU   B C    1 ? 2 
ATOM   3645 O O    . LEU   B 1 122 ? 10.888  27.966 32.97   1   47.766 ? 134 LEU   B O    1 ? 2 
ATOM   3646 C CB   . LEU   B 1 122 ? 8.822   25.881 32.566  1   39.869 ? 134 LEU   B CB   1 ? 2 
ATOM   3647 C CG   . LEU   B 1 122 ? 7.696   26.75  31.995  1   40.185 ? 134 LEU   B CG   1 ? 2 
ATOM   3648 C CD1  . LEU   B 1 122 ? 7.517   26.534 30.514  1   39.629 ? 134 LEU   B CD1  1 ? 2 
ATOM   3649 C CD2  . LEU   B 1 122 ? 6.396   26.489 32.709  1   40.879 ? 134 LEU   B CD2  1 ? 2 
ATOM   3650 H H    . LEU   B 1 122 ? 11.088  24.801 33.239  1   40.356 ? 134 LEU   B H    1 c 2 
ATOM   3651 H HA   . LEU   B 1 122 ? 10.015  25.746 30.88   1   39.171 ? 134 LEU   B HA   1 c 2 
ATOM   3652 H HB2  . LEU   B 1 122 ? 8.529   24.941 32.549  1   38.396 ? 134 LEU   B HB2  1 c 2 
ATOM   3653 H HB3  . LEU   B 1 122 ? 8.967   26.136 33.506  1   41.298 ? 134 LEU   B HB3  1 c 2 
ATOM   3654 H HG   . LEU   B 1 122 ? 7.937   27.701 32.139  1   42.278 ? 134 LEU   B HG   1 c 2 
ATOM   3655 H HD11 . LEU   B 1 122 ? 8.22    26.998 30.03   1   40.288 ? 134 LEU   B HD11 1 c 2 
ATOM   3656 H HD12 . LEU   B 1 122 ? 6.652   26.882 30.238  1   39.192 ? 134 LEU   B HD12 1 c 2 
ATOM   3657 H HD13 . LEU   B 1 122 ? 7.56    25.583 30.316  1   37.908 ? 134 LEU   B HD13 1 c 2 
ATOM   3658 H HD21 . LEU   B 1 122 ? 6.529   26.567 33.667  1   41.52  ? 134 LEU   B HD21 1 c 2 
ATOM   3659 H HD22 . LEU   B 1 122 ? 6.084   25.593 32.499  1   38.859 ? 134 LEU   B HD22 1 c 2 
ATOM   3660 H HD23 . LEU   B 1 122 ? 5.731   27.137 32.422  1   40.782 ? 134 LEU   B HD23 1 c 2 
ATOM   3661 N N    . LEU   B 1 123 ? 11.036  27.95  30.712  1   45.006 ? 135 LEU   B N    1 ? 2 
ATOM   3662 C CA   . LEU   B 1 123 ? 11.693  29.246 30.603  1   48.46  ? 135 LEU   B CA   1 ? 2 
ATOM   3663 C C    . LEU   B 1 123 ? 10.656  30.362 30.679  1   47.936 ? 135 LEU   B C    1 ? 2 
ATOM   3664 O O    . LEU   B 1 123 ? 10.874  31.361 31.342  1   49.425 ? 135 LEU   B O    1 ? 2 
ATOM   3665 C CB   . LEU   B 1 123 ? 12.464  29.337 29.291  1   50.591 ? 135 LEU   B CB   1 ? 2 
ATOM   3666 C CG   . LEU   B 1 123 ? 13.505  28.24  29.047  1   51.222 ? 135 LEU   B CG   1 ? 2 
ATOM   3667 C CD1  . LEU   B 1 123 ? 14.059  28.313 27.634  1   53.399 ? 135 LEU   B CD1  1 ? 2 
ATOM   3668 C CD2  . LEU   B 1 123 ? 14.609  28.366 30.071  1   53.927 ? 135 LEU   B CD2  1 ? 2 
ATOM   3669 H H    . LEU   B 1 123 ? 10.819  27.507 29.942  1   43.448 ? 135 LEU   B H    1 c 2 
ATOM   3670 H HA   . LEU   B 1 123 ? 12.324  29.346 31.361  1   49.866 ? 135 LEU   B HA   1 c 2 
ATOM   3671 H HB2  . LEU   B 1 123 ? 11.814  29.319 28.552  1   49.355 ? 135 LEU   B HB2  1 c 2 
ATOM   3672 H HB3  . LEU   B 1 123 ? 12.92   30.209 29.263  1   52.788 ? 135 LEU   B HB3  1 c 2 
ATOM   3673 H HG   . LEU   B 1 123 ? 13.067  27.359 29.165  1   49.223 ? 135 LEU   B HG   1 c 2 
ATOM   3674 H HD11 . LEU   B 1 123 ? 13.34   28.521 27.015  1   52.082 ? 135 LEU   B HD11 1 c 2 
ATOM   3675 H HD12 . LEU   B 1 123 ? 14.453  27.457 27.395  1   51.745 ? 135 LEU   B HD12 1 c 2 
ATOM   3676 H HD13 . LEU   B 1 123 ? 14.738  29.006 27.585  1   55.116 ? 135 LEU   B HD13 1 c 2 
ATOM   3677 H HD21 . LEU   B 1 123 ? 14.285  28.071 30.937  1   53.255 ? 135 LEU   B HD21 1 c 2 
ATOM   3678 H HD22 . LEU   B 1 123 ? 14.891  29.293 30.131  1   55.969 ? 135 LEU   B HD22 1 c 2 
ATOM   3679 H HD23 . LEU   B 1 123 ? 15.365  27.815 29.804  1   53.801 ? 135 LEU   B HD23 1 c 2 
ATOM   3680 N N    . ASP   B 1 124 ? 9.537   30.193 29.965  1   47.273 ? 136 ASP   B N    1 ? 2 
ATOM   3681 C CA   . ASP   B 1 124 ? 8.515   31.219 29.891  1   47.418 ? 136 ASP   B CA   1 ? 2 
ATOM   3682 C C    . ASP   B 1 124 ? 7.255   30.66  29.234  1   45.569 ? 136 ASP   B C    1 ? 2 
ATOM   3683 O O    . ASP   B 1 124 ? 7.309   29.641 28.536  1   42.478 ? 136 ASP   B O    1 ? 2 
ATOM   3684 C CB   . ASP   B 1 124 ? 9.016   32.431 29.123  1   52.045 ? 136 ASP   B CB   1 ? 2 
ATOM   3685 C CG   . ASP   B 1 124 ? 8.352   33.75  29.484  1   54.892 ? 136 ASP   B CG   1 ? 2 
ATOM   3686 O OD1  . ASP   B 1 124 ? 7.594   33.768 30.472  1   54.86  ? 136 ASP   B OD1  1 ? 2 
ATOM   3687 O OD2  . ASP   B 1 124 ? 8.58    34.728 28.763  1   58.496 ? 136 ASP   B OD2  1 ? 2 
ATOM   3688 H H    . ASP   B 1 124 ? 9.412   29.414 29.505  1   44.993 ? 136 ASP   B H    1 c 2 
ATOM   3689 H HA   . ASP   B 1 124 ? 8.293   31.496 30.808  1   48.83  ? 136 ASP   B HA   1 c 2 
ATOM   3690 H HB2  . ASP   B 1 124 ? 9.98    32.535 29.262  1   52.89  ? 136 ASP   B HB2  1 c 2 
ATOM   3691 H HB3  . ASP   B 1 124 ? 8.873   32.277 28.165  1   50.966 ? 136 ASP   B HB3  1 c 2 
ATOM   3692 N N    . PHE   B 1 125 ? 6.121   31.341 29.478  1   44.844 ? 137 PHE   B N    1 ? 2 
ATOM   3693 C CA   . PHE   B 1 125 ? 4.92    31.106 28.698  1   42.859 ? 137 PHE   B CA   1 ? 2 
ATOM   3694 C C    . PHE   B 1 125 ? 4.097   32.381 28.603  1   45.35  ? 137 PHE   B C    1 ? 2 
ATOM   3695 O O    . PHE   B 1 125 ? 3.96    33.116 29.575  1   46.536 ? 137 PHE   B O    1 ? 2 
ATOM   3696 C CB   . PHE   B 1 125 ? 4.118   29.919 29.241  1   40.562 ? 137 PHE   B CB   1 ? 2 
ATOM   3697 C CG   . PHE   B 1 125 ? 3.641   30.079 30.676  1   41.622 ? 137 PHE   B CG   1 ? 2 
ATOM   3698 C CD1  . PHE   B 1 125 ? 2.404   30.644 30.949  1   41.89  ? 137 PHE   B CD1  1 ? 2 
ATOM   3699 C CD2  . PHE   B 1 125 ? 4.419   29.641 31.743  1   42.143 ? 137 PHE   B CD2  1 ? 2 
ATOM   3700 C CE1  . PHE   B 1 125 ? 1.97    30.792 32.26   1   44.508 ? 137 PHE   B CE1  1 ? 2 
ATOM   3701 C CE2  . PHE   B 1 125 ? 3.988   29.8   33.049  1   43.854 ? 137 PHE   B CE2  1 ? 2 
ATOM   3702 C CZ   . PHE   B 1 125 ? 2.743   30.34  33.304  1   45.203 ? 137 PHE   B CZ   1 ? 2 
ATOM   3703 H H    . PHE   B 1 125 ? 6.101   31.963 30.148  1   46.535 ? 137 PHE   B H    1 c 2 
ATOM   3704 H HA   . PHE   B 1 125 ? 5.211   30.871 27.78   1   42.598 ? 137 PHE   B HA   1 c 2 
ATOM   3705 H HB2  . PHE   B 1 125 ? 3.336   29.781 28.662  1   39.968 ? 137 PHE   B HB2  1 c 2 
ATOM   3706 H HB3  . PHE   B 1 125 ? 4.678   29.113 29.183  1   39.39  ? 137 PHE   B HB3  1 c 2 
ATOM   3707 H HD1  . PHE   B 1 125 ? 1.859   30.941 30.238  1   42.551 ? 137 PHE   B HD1  1 c 2 
ATOM   3708 H HD2  . PHE   B 1 125 ? 5.265   29.258 31.574  1   41.843 ? 137 PHE   B HD2  1 c 2 
ATOM   3709 H HE1  . PHE   B 1 125 ? 1.123   31.173 32.433  1   44.906 ? 137 PHE   B HE1  1 c 2 
ATOM   3710 H HE2  . PHE   B 1 125 ? 4.525   29.492 33.762  1   44.135 ? 137 PHE   B HE2  1 c 2 
ATOM   3711 H HZ   . PHE   B 1 125 ? 2.449   30.452 34.195  1   45.783 ? 137 PHE   B HZ   1 c 2 
ATOM   3712 N N    . LYS   B 1 126 ? 3.524   32.591 27.411  1   46.227 ? 138 LYS   B N    1 ? 2 
ATOM   3713 C CA   . LYS   B 1 126 ? 2.788   33.792 27.06   1   50.226 ? 138 LYS   B CA   1 ? 2 
ATOM   3714 C C    . LYS   B 1 126 ? 1.435   33.371 26.484  1   49.456 ? 138 LYS   B C    1 ? 2 
ATOM   3715 O O    . LYS   B 1 126 ? 1.304   32.31  25.872  1   46.539 ? 138 LYS   B O    1 ? 2 
ATOM   3716 C CB   . LYS   B 1 126 ? 3.631   34.64  26.093  1   51.598 ? 138 LYS   B CB   1 ? 2 
ATOM   3717 H H    . LYS   B 1 126 ? 3.597   31.935 26.777  1   45.061 ? 138 LYS   B H    1 c 2 
ATOM   3718 H HA   . LYS   B 1 126 ? 2.63    34.316 27.886  1   50.899 ? 138 LYS   B HA   1 c 2 
ATOM   3719 H HB2  . LYS   B 1 126 ? 4.604   34.465 26.259  0   30     ? 138 LYS   B HB2  1 c 2 
ATOM   3720 H HB3  . LYS   B 1 126 ? 3.074   35.175 25.478  0   30     ? 138 LYS   B HB3  1 c 2 
ATOM   3721 N N    . GLY   B 1 127 ? 0.43    34.22  26.686  1   51.377 ? 139 GLY   B N    1 ? 2 
ATOM   3722 C CA   . GLY   B 1 127 ? -0.902  33.986 26.168  1   54.677 ? 139 GLY   B CA   1 ? 2 
ATOM   3723 C C    . GLY   B 1 127 ? -0.901  33.985 24.643  1   60.635 ? 139 GLY   B C    1 ? 2 
ATOM   3724 O O    . GLY   B 1 127 ? -0.067  34.639 24.009  1   62.013 ? 139 GLY   B O    1 ? 2 
ATOM   3725 H H    . GLY   B 1 127 ? 0.582   34.982 27.168  1   53.778 ? 139 GLY   B H    1 c 2 
ATOM   3726 H HA2  . GLY   B 1 127 ? -1.233  33.119 26.503  1   53.02  ? 139 GLY   B HA2  1 c 2 
ATOM   3727 H HA3  . GLY   B 1 127 ? -1.503  34.691 26.498  1   56.452 ? 139 GLY   B HA3  1 c 2 
ATOM   3728 N N    . GLU   B 1 128 ? -1.859  33.243 24.075  1   64.039 ? 140 GLU   B N    1 ? 2 
ATOM   3729 C CA   . GLU   B 1 128 ? -2.057  33.175 22.637  1   68.086 ? 140 GLU   B CA   1 ? 2 
ATOM   3730 C C    . GLU   B 1 128 ? -2.539  34.552 22.141  1   71.848 ? 140 GLU   B C    1 ? 2 
ATOM   3731 O O    . GLU   B 1 128 ? -3.021  35.349 22.991  1   71.264 ? 140 GLU   B O    1 ? 2 
ATOM   3732 C CB   . GLU   B 1 128 ? -3.035  32.046 22.284  1   69.052 ? 140 GLU   B CB   1 ? 2 
ATOM   3733 O OXT  . GLU   B 1 128 ? -2.403  34.784 20.923  1   75.301 ? 140 GLU   B OXT  1 ? 2 
ATOM   3734 H H    . GLU   B 1 128 ? -2.416  32.759 24.615  1   62.366 ? 140 GLU   B H    1 c 2 
ATOM   3735 H HA   . GLU   B 1 128 ? -1.183  32.977 22.213  1   67.457 ? 140 GLU   B HA   1 c 2 
ATOM   3736 H HB2  . GLU   B 1 128 ? -2.429  31.262 22.029  0   30     ? 140 GLU   B HB2  1 c 2 
ATOM   3737 H HB3  . GLU   B 1 128 ? -3.914  32.336 22.327  0   30     ? 140 GLU   B HB3  1 c 2 
HETATM 3738 C C4   . A1INN C 2 .   ? -10.195 11.759 14.301  1   32.244 ? 201 A1INN A C4   1 ? 1 
HETATM 3739 C C14  . A1INN C 2 .   ? -10.446 17.45  15.115  1   30.301 ? 201 A1INN A C14  1 ? 1 
HETATM 3740 C C5   . A1INN C 2 .   ? -11.423 11.316 14.786  1   34.333 ? 201 A1INN A C5   1 ? 1 
HETATM 3741 C C6   . A1INN C 2 .   ? -11.732 11.426 16.134  1   36.798 ? 201 A1INN A C6   1 ? 1 
HETATM 3742 C C11  . A1INN C 2 .   ? -13.483 14.155 17.441  1   38.57  ? 201 A1INN A C11  1 ? 1 
HETATM 3743 C C7   . A1INN C 2 .   ? -13.952 10.506 15.888  1   41.75  ? 201 A1INN A C7   1 ? 1 
HETATM 3744 C C8   . A1INN C 2 .   ? -10.813 11.994 17.012  1   35.427 ? 201 A1INN A C8   1 ? 1 
HETATM 3745 C C9   . A1INN C 2 .   ? -11.401 13.496 18.786  1   37.976 ? 201 A1INN A C9   1 ? 1 
HETATM 3746 C C10  . A1INN C 2 .   ? -12.887 13.81  18.812  1   40.104 ? 201 A1INN A C10  1 ? 1 
HETATM 3747 C C12  . A1INN C 2 .   ? -11.718 15.4   16.111  1   36.037 ? 201 A1INN A C12  1 ? 1 
HETATM 3748 C C13  . A1INN C 2 .   ? -11.53  16.732 15.862  1   33.732 ? 201 A1INN A C13  1 ? 1 
HETATM 3749 N N1   . A1INN C 2 .   ? -12.847 15.327 16.846  1   37.394 ? 201 A1INN A N1   1 ? 1 
HETATM 3750 N N2   . A1INN C 2 .   ? -12.527 17.404 16.491  1   37.447 ? 201 A1INN A N2   1 ? 1 
HETATM 3751 C C3   . A1INN C 2 .   ? -9.268  12.318 15.182  1   32.514 ? 201 A1INN A C3   1 ? 1 
HETATM 3752 N N3   . A1INN C 2 .   ? -13.34  16.555 17.084  1   39.522 ? 201 A1INN A N3   1 ? 1 
HETATM 3753 C C1   . A1INN C 2 .   ? -7.439  13.319 17.131  1   32.513 ? 201 A1INN A C1   1 ? 1 
HETATM 3754 O O1   . A1INN C 2 .   ? -8.763  12.971 17.499  1   34.29  ? 201 A1INN A O1   1 ? 1 
HETATM 3755 C C2   . A1INN C 2 .   ? -9.578  12.429 16.539  1   34.395 ? 201 A1INN A C2   1 ? 1 
HETATM 3756 O O2   . A1INN C 2 .   ? -12.909 11.032 16.723  1   40.454 ? 201 A1INN A O2   1 ? 1 
HETATM 3757 O O3   . A1INN C 2 .   ? -11.198 12.132 18.334  1   37.953 ? 201 A1INN A O3   1 ? 1 
HETATM 3758 C C15  . A1INN C 2 .   ? -9.232  16.579 14.876  1   28.492 ? 201 A1INN A C15  1 ? 1 
HETATM 3759 O O4   . A1INN C 2 .   ? -9.563  15.682 13.77   1   28.453 ? 201 A1INN A O4   1 ? 1 
HETATM 3760 C C16  . A1INN C 2 .   ? -9.347  16.149 12.526  1   27.556 ? 201 A1INN A C16  1 ? 1 
HETATM 3761 O O5   . A1INN C 2 .   ? -8.968  17.253 12.276  1   28.232 ? 201 A1INN A O5   1 ? 1 
HETATM 3762 C C17  . A1INN C 2 .   ? -9.607  15.114 11.45   1   26.951 ? 201 A1INN A C17  1 ? 1 
HETATM 3763 C C18  . A1INN C 2 .   ? -10.489 15.72  10.37   1   29.145 ? 201 A1INN A C18  1 ? 1 
HETATM 3764 C C19  . A1INN C 2 .   ? -11.913 15.92  10.87   1   30.223 ? 201 A1INN A C19  1 ? 1 
HETATM 3765 C C20  . A1INN C 2 .   ? -12.504 14.582 11.247  1   31.508 ? 201 A1INN A C20  1 ? 1 
HETATM 3766 C C21  . A1INN C 2 .   ? -11.647 13.842 12.298  1   31.554 ? 201 A1INN A C21  1 ? 1 
HETATM 3767 N N4   . A1INN C 2 .   ? -10.196 13.877 11.991  1   30.134 ? 201 A1INN A N4   1 ? 1 
HETATM 3768 C C22  . A1INN C 2 .   ? -9.322  12.889 12.276  1   28.271 ? 201 A1INN A C22  1 ? 1 
HETATM 3769 O O6   . A1INN C 2 .   ? -8.102  13.081 12.181  1   27.882 ? 201 A1INN A O6   1 ? 1 
HETATM 3770 C C23  . A1INN C 2 .   ? -9.86   11.582 12.82   1   30.621 ? 201 A1INN A C23  1 ? 1 
HETATM 3771 C C24  . A1INN C 2 .   ? -8.859  10.426 12.555  1   29.676 ? 201 A1INN A C24  1 ? 1 
HETATM 3772 C C25  . A1INN C 2 .   ? -8.8    10.034 11.073  1   28.698 ? 201 A1INN A C25  1 ? 1 
HETATM 3773 C C26  . A1INN C 2 .   ? -7.744  8.956  10.839  1   29.117 ? 201 A1INN A C26  1 ? 1 
HETATM 3774 C C27  . A1INN C 2 .   ? -8.036  7.716  11.646  1   30.495 ? 201 A1INN A C27  1 ? 1 
HETATM 3775 C C28  . A1INN C 2 .   ? -8.234  8.02   13.133  1   33.398 ? 201 A1INN A C28  1 ? 1 
HETATM 3776 C C29  . A1INN C 2 .   ? -9.204  9.18   13.373  1   31.95  ? 201 A1INN A C29  1 ? 1 
HETATM 3777 H H17  . A1INN C 2 .   ? -10.8   17.755 14.254  1   30.171 ? 201 A1INN A H17  1 c 1 
HETATM 3778 H H16  . A1INN C 2 .   ? -10.177 18.241 15.627  1   30.963 ? 201 A1INN A H16  1 c 1 
HETATM 3779 H H5   . A1INN C 2 .   ? -12.041 10.923 14.192  1   34.972 ? 201 A1INN A H5   1 c 1 
HETATM 3780 H H14  . A1INN C 2 .   ? -13.376 13.394 16.837  1   38.294 ? 201 A1INN A H14  1 c 1 
HETATM 3781 H H13  . A1INN C 2 .   ? -14.441 14.331 17.542  1   40.045 ? 201 A1INN A H13  1 c 1 
HETATM 3782 H H7   . A1INN C 2 .   ? -14.735 10.317 16.431  1   43.302 ? 201 A1INN A H7   1 c 1 
HETATM 3783 H H8   . A1INN C 2 .   ? -13.646 9.687  15.468  1   41.489 ? 201 A1INN A H8   1 c 1 
HETATM 3784 H H6   . A1INN C 2 .   ? -14.181 11.157 15.205  1   40.647 ? 201 A1INN A H6   1 c 1 
HETATM 3785 H H9   . A1INN C 2 .   ? -10.938 14.122 18.19   1   36.726 ? 201 A1INN A H9   1 c 1 
HETATM 3786 H H10  . A1INN C 2 .   ? -11.027 13.603 19.689  1   38.855 ? 201 A1INN A H10  1 c 1 
HETATM 3787 H H12  . A1INN C 2 .   ? -13.366 13.037 19.179  1   41.205 ? 201 A1INN A H12  1 c 1 
HETATM 3788 H H11  . A1INN C 2 .   ? -13.039 14.565 19.42   1   40.546 ? 201 A1INN A H11  1 c 1 
HETATM 3789 H H15  . A1INN C 2 .   ? -11.176 14.684 15.829  1   34.776 ? 201 A1INN A H15  1 c 1 
HETATM 3790 H H4   . A1INN C 2 .   ? -8.428  12.606 14.86   1   31.383 ? 201 A1INN A H4   1 c 1 
HETATM 3791 H H2   . A1INN C 2 .   ? -6.957  13.627 17.916  1   33.068 ? 201 A1INN A H2   1 c 1 
HETATM 3792 H H3   . A1INN C 2 .   ? -7.462  14.027 16.467  1   31.675 ? 201 A1INN A H3   1 c 1 
HETATM 3793 H H1   . A1INN C 2 .   ? -6.99   12.541 16.761  1   32.318 ? 201 A1INN A H1   1 c 1 
HETATM 3794 H H19  . A1INN C 2 .   ? -8.456  17.133 14.65   1   28.052 ? 201 A1INN A H19  1 c 1 
HETATM 3795 H H18  . A1INN C 2 .   ? -9.023  16.061 15.681  1   29.375 ? 201 A1INN A H18  1 c 1 
HETATM 3796 H H20  . A1INN C 2 .   ? -8.733  14.879 11.04   1   26.907 ? 201 A1INN A H20  1 c 1 
HETATM 3797 H H22  . A1INN C 2 .   ? -10.115 16.589 10.085  1   28.031 ? 201 A1INN A H22  1 c 1 
HETATM 3798 H H21  . A1INN C 2 .   ? -10.5   15.121 9.585   1   28.195 ? 201 A1INN A H21  1 c 1 
HETATM 3799 H H23  . A1INN C 2 .   ? -12.459 16.337 10.165  1   30.522 ? 201 A1INN A H23  1 c 1 
HETATM 3800 H H24  . A1INN C 2 .   ? -11.914 16.517 11.653  1   30.847 ? 201 A1INN A H24  1 c 1 
HETATM 3801 H H25  . A1INN C 2 .   ? -12.581 14.024 10.444  1   31.204 ? 201 A1INN A H25  1 c 1 
HETATM 3802 H H26  . A1INN C 2 .   ? -13.408 14.717 11.605  1   32.635 ? 201 A1INN A H26  1 c 1 
HETATM 3803 H H27  . A1INN C 2 .   ? -11.948 12.908 12.349  1   32.273 ? 201 A1INN A H27  1 c 1 
HETATM 3804 H H28  . A1INN C 2 .   ? -11.796 14.252 13.18   1   32.236 ? 201 A1INN A H28  1 c 1 
HETATM 3805 H H29  . A1INN C 2 .   ? -10.707 11.378 12.345  1   30.912 ? 201 A1INN A H29  1 c 1 
HETATM 3806 H H30  . A1INN C 2 .   ? -7.955  10.73  12.828  1   29.226 ? 201 A1INN A H30  1 c 1 
HETATM 3807 H H32  . A1INN C 2 .   ? -9.675  9.701  10.788  1   29.608 ? 201 A1INN A H32  1 c 1 
HETATM 3808 H H31  . A1INN C 2 .   ? -8.584  10.822 10.534  1   27.738 ? 201 A1INN A H31  1 c 1 
HETATM 3809 H H33  . A1INN C 2 .   ? -6.861  9.307  11.088  1   28.205 ? 201 A1INN A H33  1 c 1 
HETATM 3810 H H34  . A1INN C 2 .   ? -7.722  8.725  9.884   1   28.608 ? 201 A1INN A H34  1 c 1 
HETATM 3811 H H35  . A1INN C 2 .   ? -7.291  7.083  11.544  1   31.305 ? 201 A1INN A H35  1 c 1 
HETATM 3812 H H36  . A1INN C 2 .   ? -8.846  7.286  11.295  1   31.934 ? 201 A1INN A H36  1 c 1 
HETATM 3813 H H37  . A1INN C 2 .   ? -7.369  8.23   13.54   1   32.355 ? 201 A1INN A H37  1 c 1 
HETATM 3814 H H38  . A1INN C 2 .   ? -8.584  7.216  13.578  1   34.227 ? 201 A1INN A H38  1 c 1 
HETATM 3815 H H40  . A1INN C 2 .   ? -10.112 8.89   13.147  1   32.984 ? 201 A1INN A H40  1 c 1 
HETATM 3816 H H39  . A1INN C 2 .   ? -9.194  9.407  14.325  1   32.703 ? 201 A1INN A H39  1 c 1 
HETATM 3817 C C4   . A1INN D 2 .   ? 12.304  13.992 19.71   1   24.567 ? 201 A1INN B C4   1 ? 2 
HETATM 3818 C C14  . A1INN D 2 .   ? 7.327   16.642 18.583  1   22.778 ? 201 A1INN B C14  1 ? 2 
HETATM 3819 C C5   . A1INN D 2 .   ? 13.283  14.813 19.147  1   27.314 ? 201 A1INN B C5   1 ? 2 
HETATM 3820 C C6   . A1INN D 2 .   ? 13.334  15.014 17.771  1   27.675 ? 201 A1INN B C6   1 ? 2 
HETATM 3821 C C11  . A1INN D 2 .   ? 11.79   17.786 16.568  1   29.442 ? 201 A1INN B C11  1 ? 2 
HETATM 3822 C C7   . A1INN D 2 .   ? 15.199  16.496 17.92   1   33.726 ? 201 A1INN B C7   1 ? 2 
HETATM 3823 C C8   . A1INN D 2 .   ? 12.373  14.436 16.94   1   26.972 ? 201 A1INN B C8   1 ? 2 
HETATM 3824 C C9   . A1INN D 2 .   ? 11.463  15.686 15.12   1   29.703 ? 201 A1INN B C9   1 ? 2 
HETATM 3825 C C10  . A1INN D 2 .   ? 11.988  17.11  15.203  1   30.878 ? 201 A1INN B C10  1 ? 2 
HETATM 3826 C C12  . A1INN D 2 .   ? 9.763   16.805 17.73   1   24.988 ? 201 A1INN B C12  1 ? 2 
HETATM 3827 C C13  . A1INN D 2 .   ? 8.497   17.283 17.907  1   24.728 ? 201 A1INN B C13  1 ? 2 
HETATM 3828 N N1   . A1INN D 2 .   ? 10.41   17.768 17.059  1   28.569 ? 201 A1INN B N1   1 ? 2 
HETATM 3829 N N2   . A1INN D 2 .   ? 8.425   18.516 17.327  1   26.953 ? 201 A1INN B N2   1 ? 2 
HETATM 3830 C C3   . A1INN D 2 .   ? 11.346  13.404 18.887  1   23.191 ? 201 A1INN B C3   1 ? 2 
HETATM 3831 N N3   . A1INN D 2 .   ? 9.597   18.823 16.83   1   28.84  ? 201 A1INN B N3   1 ? 2 
HETATM 3832 C C1   . A1INN D 2 .   ? 9.658   12.042 17.061  1   23.108 ? 201 A1INN B C1   1 ? 2 
HETATM 3833 O O1   . A1INN D 2 .   ? 10.511  13.072 16.601  1   23.826 ? 201 A1INN B O1   1 ? 2 
HETATM 3834 C C2   . A1INN D 2 .   ? 11.391  13.607 17.502  1   24.968 ? 201 A1INN B C2   1 ? 2 
HETATM 3835 O O2   . A1INN D 2 .   ? 14.238  15.809 17.128  1   31.359 ? 201 A1INN B O2   1 ? 2 
HETATM 3836 O O3   . A1INN D 2 .   ? 12.456  14.728 15.583  1   28.486 ? 201 A1INN B O3   1 ? 2 
HETATM 3837 C C15  . A1INN D 2 .   ? 7.597   15.22  19.033  1   22.332 ? 201 A1INN B C15  1 ? 2 
HETATM 3838 O O4   . A1INN D 2 .   ? 8.537   15.18  20.159  1   22.001 ? 201 A1INN B O4   1 ? 2 
HETATM 3839 C C16  . A1INN D 2 .   ? 7.979   15.304 21.357  1   22.364 ? 201 A1INN B C16  1 ? 2 
HETATM 3840 O O5   . A1INN D 2 .   ? 6.81    15.469 21.506  1   23.621 ? 201 A1INN B O5   1 ? 2 
HETATM 3841 C C17  . A1INN D 2 .   ? 8.985   15.16  22.488  1   23.737 ? 201 A1INN B C17  1 ? 2 
HETATM 3842 C C18  . A1INN D 2 .   ? 8.801   16.321 23.465  1   25.422 ? 201 A1INN B C18  1 ? 2 
HETATM 3843 C C19  . A1INN D 2 .   ? 9.266   17.628 22.874  1   25.075 ? 201 A1INN B C19  1 ? 2 
HETATM 3844 C C20  . A1INN D 2 .   ? 10.73   17.504 22.561  1   26.694 ? 201 A1INN B C20  1 ? 2 
HETATM 3845 C C21  . A1INN D 2 .   ? 11.051  16.328 21.598  1   25.24  ? 201 A1INN B C21  1 ? 2 
HETATM 3846 N N4   . A1INN D 2 .   ? 10.364  15.076 21.979  1   23.662 ? 201 A1INN B N4   1 ? 2 
HETATM 3847 C C22  . A1INN D 2 .   ? 10.884  13.853 21.734  1   23.934 ? 201 A1INN B C22  1 ? 2 
HETATM 3848 O O6   . A1INN D 2 .   ? 10.22   12.825 21.876  1   24.598 ? 201 A1INN B O6   1 ? 2 
HETATM 3849 C C23  . A1INN D 2 .   ? 12.308  13.744 21.212  1   25.081 ? 201 A1INN B C23  1 ? 2 
HETATM 3850 C C24  . A1INN D 2 .   ? 12.91   12.376 21.599  1   25.388 ? 201 A1INN B C24  1 ? 2 
HETATM 3851 C C25  . A1INN D 2 .   ? 13.078  12.222 23.125  1   24.875 ? 201 A1INN B C25  1 ? 2 
HETATM 3852 C C26  . A1INN D 2 .   ? 13.698  10.874 23.484  1   26.061 ? 201 A1INN B C26  1 ? 2 
HETATM 3853 C C27  . A1INN D 2 .   ? 15.015  10.617 22.791  1   26.986 ? 201 A1INN B C27  1 ? 2 
HETATM 3854 C C28  . A1INN D 2 .   ? 14.87   10.81  21.293  1   27.841 ? 201 A1INN B C28  1 ? 2 
HETATM 3855 C C29  . A1INN D 2 .   ? 14.256  12.158 20.936  1   26.108 ? 201 A1INN B C29  1 ? 2 
HETATM 3856 H H17  . A1INN D 2 .   ? 7.076   17.181 19.362  1   22.681 ? 201 A1INN B H17  1 c 2 
HETATM 3857 H H16  . A1INN D 2 .   ? 6.566   16.64  17.964  1   23.345 ? 201 A1INN B H16  1 c 2 
HETATM 3858 H H5   . A1INN D 2 .   ? 13.934  15.205 19.706  1   27.449 ? 201 A1INN B H5   1 c 2 
HETATM 3859 H H14  . A1INN D 2 .   ? 12.359  17.344 17.229  1   29.114 ? 201 A1INN B H14  1 c 2 
HETATM 3860 H H13  . A1INN D 2 .   ? 12.083  18.718 16.501  1   30.838 ? 201 A1INN B H13  1 c 2 
HETATM 3861 H H7   . A1INN D 2 .   ? 15.766  17.033 17.343  1   34.846 ? 201 A1INN B H7   1 c 2 
HETATM 3862 H H8   . A1INN D 2 .   ? 15.744  15.852 18.4    1   33.015 ? 201 A1INN B H8   1 c 2 
HETATM 3863 H H6   . A1INN D 2 .   ? 14.744  17.075 18.553  1   32.64  ? 201 A1INN B H6   1 c 2 
HETATM 3864 H H9   . A1INN D 2 .   ? 10.648  15.603 15.658  1   28.194 ? 201 A1INN B H9   1 c 2 
HETATM 3865 H H10  . A1INN D 2 .   ? 11.227  15.482 14.188  1   30.344 ? 201 A1INN B H10  1 c 2 
HETATM 3866 H H12  . A1INN D 2 .   ? 12.946  17.105 14.991  1   32.018 ? 201 A1INN B H12  1 c 2 
HETATM 3867 H H11  . A1INN D 2 .   ? 11.54   17.651 14.517  1   31.852 ? 201 A1INN B H11  1 c 2 
HETATM 3868 H H15  . A1INN D 2 .   ? 10.104  15.973 18.002  1   24.855 ? 201 A1INN B H15  1 c 2 
HETATM 3869 H H4   . A1INN D 2 .   ? 10.694  12.832 19.262  1   22.713 ? 201 A1INN B H4   1 c 2 
HETATM 3870 H H2   . A1INN D 2 .   ? 9.172   11.667 16.308  1   23.416 ? 201 A1INN B H2   1 c 2 
HETATM 3871 H H3   . A1INN D 2 .   ? 9.026   12.407 17.701  1   22.195 ? 201 A1INN B H3   1 c 2 
HETATM 3872 H H1   . A1INN D 2 .   ? 10.186  11.346 17.484  1   22.752 ? 201 A1INN B H1   1 c 2 
HETATM 3873 H H19  . A1INN D 2 .   ? 6.753   14.793 19.289  1   21.616 ? 201 A1INN B H19  1 c 2 
HETATM 3874 H H18  . A1INN D 2 .   ? 7.97    14.71  18.283  1   22.7   ? 201 A1INN B H18  1 c 2 
HETATM 3875 H H20  . A1INN D 2 .   ? 8.786   14.313 22.968  1   22.986 ? 201 A1INN B H20  1 c 2 
HETATM 3876 H H22  . A1INN D 2 .   ? 7.847   16.396 23.713  1   24.237 ? 201 A1INN B H22  1 c 2 
HETATM 3877 H H21  . A1INN D 2 .   ? 9.315   16.137 24.286  1   24.826 ? 201 A1INN B H21  1 c 2 
HETATM 3878 H H23  . A1INN D 2 .   ? 9.12    18.36  23.516  1   25.848 ? 201 A1INN B H23  1 c 2 
HETATM 3879 H H24  . A1INN D 2 .   ? 8.761   17.829 22.052  1   25.653 ? 201 A1INN B H24  1 c 2 
HETATM 3880 H H25  . A1INN D 2 .   ? 11.227  17.376 23.397  1   26.393 ? 201 A1INN B H25  1 c 2 
HETATM 3881 H H26  . A1INN D 2 .   ? 11.043  18.341 22.157  1   27.285 ? 201 A1INN B H26  1 c 2 
HETATM 3882 H H27  . A1INN D 2 .   ? 12.023  16.181 21.593  1   26.133 ? 201 A1INN B H27  1 c 2 
HETATM 3883 H H28  . A1INN D 2 .   ? 10.781  16.576 20.685  1   25.784 ? 201 A1INN B H28  1 c 2 
HETATM 3884 H H29  . A1INN D 2 .   ? 12.851  14.458 21.634  1   25.53  ? 201 A1INN B H29  1 c 2 
HETATM 3885 H H30  . A1INN D 2 .   ? 12.296  11.663 21.282  1   24.575 ? 201 A1INN B H30  1 c 2 
HETATM 3886 H H32  . A1INN D 2 .   ? 13.648  12.942 23.463  1   25.827 ? 201 A1INN B H32  1 c 2 
HETATM 3887 H H31  . A1INN D 2 .   ? 12.205  12.299 23.558  1   24.368 ? 201 A1INN B H31  1 c 2 
HETATM 3888 H H33  . A1INN D 2 .   ? 13.067  10.159 23.245  1   25.186 ? 201 A1INN B H33  1 c 2 
HETATM 3889 H H34  . A1INN D 2 .   ? 13.837  10.836 24.456  1   25.968 ? 201 A1INN B H34  1 c 2 
HETATM 3890 H H35  . A1INN D 2 .   ? 15.311  9.699  22.977  1   27.569 ? 201 A1INN B H35  1 c 2 
HETATM 3891 H H36  . A1INN D 2 .   ? 15.695  11.235 23.137  1   28.079 ? 201 A1INN B H36  1 c 2 
HETATM 3892 H H37  . A1INN D 2 .   ? 14.309  10.093 20.93   1   26.899 ? 201 A1INN B H37  1 c 2 
HETATM 3893 H H38  . A1INN D 2 .   ? 15.756  10.739 20.872  1   28.467 ? 201 A1INN B H38  1 c 2 
HETATM 3894 H H40  . A1INN D 2 .   ? 14.868  12.872 21.21   1   27.363 ? 201 A1INN B H40  1 c 2 
HETATM 3895 H H39  . A1INN D 2 .   ? 14.151  12.212 19.965  1   26.92  ? 201 A1INN B H39  1 c 2 
HETATM 3896 O O    . HOH   E 3 .   ? -16.867 19.087 -7.657  1   38.196 ? 301 HOH   A O    1 ? ? 
HETATM 3897 O O    . HOH   E 3 .   ? -14.813 34.287 4.374   1   34.394 ? 302 HOH   A O    1 ? ? 
HETATM 3898 O O    . HOH   E 3 .   ? 6.308   13.385 5.273   1   35.122 ? 303 HOH   A O    1 ? ? 
HETATM 3899 O O    . HOH   E 3 .   ? 7.265   13.203 -1.557  1   42.644 ? 304 HOH   A O    1 ? ? 
HETATM 3900 O O    . HOH   E 3 .   ? -18.456 6.141  -0.286  1   38.082 ? 305 HOH   A O    1 ? ? 
HETATM 3901 O O    . HOH   E 3 .   ? 1.926   9.103  -1.11   1   34.4   ? 306 HOH   A O    1 ? ? 
HETATM 3902 O O    . HOH   E 3 .   ? 3.86    18.306 -6.529  1   28.633 ? 307 HOH   A O    1 ? ? 
HETATM 3903 O O    . HOH   E 3 .   ? 3.856   8.424  6.861   1   40.805 ? 308 HOH   A O    1 ? ? 
HETATM 3904 O O    . HOH   E 3 .   ? -20.632 24.728 -4.102  1   41.758 ? 309 HOH   A O    1 ? ? 
HETATM 3905 O O    . HOH   E 3 .   ? 4.426   5.704  14.206  1   29.589 ? 310 HOH   A O    1 ? ? 
HETATM 3906 O O    . HOH   E 3 .   ? 0.026   12.2   -7.802  1   24.792 ? 311 HOH   A O    1 ? ? 
HETATM 3907 O O    . HOH   E 3 .   ? 2.87    9.45   19.662  1   28.023 ? 312 HOH   A O    1 ? ? 
HETATM 3908 O O    . HOH   E 3 .   ? -2.804  22.37  -7.313  1   42.558 ? 313 HOH   A O    1 ? ? 
HETATM 3909 O O    . HOH   E 3 .   ? 8.351   17.095 13.734  1   37.355 ? 314 HOH   A O    1 ? ? 
HETATM 3910 O O    . HOH   E 3 .   ? -6.837  25.412 -0.619  1   27.965 ? 315 HOH   A O    1 ? ? 
HETATM 3911 O O    . HOH   E 3 .   ? 1.252   11.723 13.104  1   24.631 ? 316 HOH   A O    1 ? ? 
HETATM 3912 O O    . HOH   E 3 .   ? -9.321  15.415 -9.256  1   37.156 ? 317 HOH   A O    1 ? ? 
HETATM 3913 O O    . HOH   E 3 .   ? -7.146  3.42   10.432  1   36.152 ? 318 HOH   A O    1 ? ? 
HETATM 3914 O O    . HOH   E 3 .   ? 2.217   24.194 1.539   1   25.668 ? 319 HOH   A O    1 ? ? 
HETATM 3915 O O    . HOH   E 3 .   ? 0.197   13.172 0.602   1   27.894 ? 320 HOH   A O    1 ? ? 
HETATM 3916 O O    . HOH   E 3 .   ? -0.43   12.51  11.034  1   26.247 ? 321 HOH   A O    1 ? ? 
HETATM 3917 O O    . HOH   E 3 .   ? -4.203  16.247 18.541  1   32.562 ? 322 HOH   A O    1 ? ? 
HETATM 3918 O O    . HOH   E 3 .   ? -2.226  19.884 10.999  1   21.609 ? 323 HOH   A O    1 ? ? 
HETATM 3919 O O    . HOH   E 3 .   ? -10.557 25.007 10.966  1   38.723 ? 324 HOH   A O    1 ? ? 
HETATM 3920 O O    . HOH   E 3 .   ? 0.996   6.185  8.003   1   32.939 ? 325 HOH   A O    1 ? ? 
HETATM 3921 O O    . HOH   E 3 .   ? -0.382  18.242 -8.995  1   28.697 ? 326 HOH   A O    1 ? ? 
HETATM 3922 O O    . HOH   E 3 .   ? 0.486   15.612 -8.645  1   28.989 ? 327 HOH   A O    1 ? ? 
HETATM 3923 O O    . HOH   E 3 .   ? -4.094  12.846 21.53   1   31.63  ? 328 HOH   A O    1 ? ? 
HETATM 3924 O O    . HOH   E 3 .   ? -6.511  9.971  19.602  1   34.113 ? 329 HOH   A O    1 ? ? 
HETATM 3925 O O    . HOH   E 3 .   ? 3.06    10.129 2.929   1   28.389 ? 330 HOH   A O    1 ? ? 
HETATM 3926 O O    . HOH   E 3 .   ? 0.455   26.442 -5.746  1   48.763 ? 331 HOH   A O    1 ? ? 
HETATM 3927 O O    . HOH   E 3 .   ? -26.55  18.575 0.808   1   40.659 ? 332 HOH   A O    1 ? ? 
HETATM 3928 O O    . HOH   E 3 .   ? 2.91    15.871 -7.386  1   31.13  ? 333 HOH   A O    1 ? ? 
HETATM 3929 O O    . HOH   E 3 .   ? 4.141   16.948 16.043  1   26.01  ? 334 HOH   A O    1 ? ? 
HETATM 3930 O O    . HOH   E 3 .   ? -8.347  7.211  -4.584  1   35.63  ? 335 HOH   A O    1 ? ? 
HETATM 3931 O O    . HOH   E 3 .   ? 5.3     11.915 -2.281  1   34.415 ? 336 HOH   A O    1 ? ? 
HETATM 3932 O O    . HOH   E 3 .   ? -9.955  20.021 -7.173  1   31.164 ? 337 HOH   A O    1 ? ? 
HETATM 3933 O O    . HOH   E 3 .   ? 0.485   11.467 20.63   1   28.434 ? 338 HOH   A O    1 ? ? 
HETATM 3934 O O    . HOH   E 3 .   ? 8.19    16.51  -0.281  1   41.395 ? 339 HOH   A O    1 ? ? 
HETATM 3935 O O    . HOH   E 3 .   ? -18.897 13.058 -11.145 1   37.22  ? 340 HOH   A O    1 ? ? 
HETATM 3936 O O    . HOH   E 3 .   ? -17.109 10.002 13.881  1   48.71  ? 341 HOH   A O    1 ? ? 
HETATM 3937 O O    . HOH   E 3 .   ? 6.155   17.582 13.579  1   31.564 ? 342 HOH   A O    1 ? ? 
HETATM 3938 O O    . HOH   E 3 .   ? -9.575  2.351  0.934   1   46.12  ? 343 HOH   A O    1 ? ? 
HETATM 3939 O O    . HOH   E 3 .   ? 7.046   16.601 2.156   1   36.504 ? 344 HOH   A O    1 ? ? 
HETATM 3940 O O    . HOH   E 3 .   ? -18.056 10.108 2.3     1   39.977 ? 345 HOH   A O    1 ? ? 
HETATM 3941 O O    . HOH   E 3 .   ? -16.397 32.67  11.83   1   64.822 ? 346 HOH   A O    1 ? ? 
HETATM 3942 O O    . HOH   E 3 .   ? 1.598   18.442 15.049  1   38.188 ? 347 HOH   A O    1 ? ? 
HETATM 3943 O O    . HOH   E 3 .   ? -6.298  20.376 14.927  1   50.389 ? 348 HOH   A O    1 ? ? 
HETATM 3944 O O    . HOH   E 3 .   ? -22.124 27.506 -4.295  1   39.75  ? 349 HOH   A O    1 ? ? 
HETATM 3945 O O    . HOH   E 3 .   ? 1.759   10.812 0.822   1   33.579 ? 350 HOH   A O    1 ? ? 
HETATM 3946 O O    . HOH   E 3 .   ? 9.661   15.855 11.616  1   38.512 ? 351 HOH   A O    1 ? ? 
HETATM 3947 O O    . HOH   F 3 .   ? 9.835   6.694  10.111  1   28.162 ? 301 HOH   B O    1 ? ? 
HETATM 3948 O O    . HOH   F 3 .   ? 0.545   29.446 21.563  1   38.34  ? 302 HOH   B O    1 ? ? 
HETATM 3949 O O    . HOH   F 3 .   ? 0.129   2.734  32.91   1   46.76  ? 303 HOH   B O    1 ? ? 
HETATM 3950 O O    . HOH   F 3 .   ? 4.725   23.368 39.43   1   38.98  ? 304 HOH   B O    1 ? ? 
HETATM 3951 O O    . HOH   F 3 .   ? 4.661   30.727 37.038  1   36.751 ? 305 HOH   B O    1 ? ? 
HETATM 3952 O O    . HOH   F 3 .   ? 22.627  7.979  24.104  1   40.398 ? 306 HOH   B O    1 ? ? 
HETATM 3953 O O    . HOH   F 3 .   ? -1.522  31.912 30.804  1   47.497 ? 307 HOH   B O    1 ? ? 
HETATM 3954 O O    . HOH   F 3 .   ? -0.336  6.44   41.064  1   35.235 ? 308 HOH   B O    1 ? ? 
HETATM 3955 O O    . HOH   F 3 .   ? 7.028   23.23  18.029  1   48.101 ? 309 HOH   B O    1 ? ? 
HETATM 3956 O O    . HOH   F 3 .   ? -2.203  16.168 24.307  1   35.198 ? 310 HOH   B O    1 ? ? 
HETATM 3957 O O    . HOH   F 3 .   ? 17.826  21.338 30.728  1   50.374 ? 311 HOH   B O    1 ? ? 
HETATM 3958 O O    . HOH   F 3 .   ? -3.438  32.456 28.955  1   40.404 ? 312 HOH   B O    1 ? ? 
HETATM 3959 O O    . HOH   F 3 .   ? 8.13    4.201  43.637  1   37.611 ? 313 HOH   B O    1 ? ? 
HETATM 3960 O O    . HOH   F 3 .   ? 6.033   6.669  33.833  1   32.724 ? 314 HOH   B O    1 ? ? 
HETATM 3961 O O    . HOH   F 3 .   ? 7.316   5.759  23.491  1   23.32  ? 315 HOH   B O    1 ? ? 
HETATM 3962 O O    . HOH   F 3 .   ? 0.568   3.672  30.567  1   38.944 ? 316 HOH   B O    1 ? ? 
HETATM 3963 O O    . HOH   F 3 .   ? 15.426  23.635 20.342  1   43.307 ? 317 HOH   B O    1 ? ? 
HETATM 3964 O O    . HOH   F 3 .   ? 7.195   3.757  21.576  1   22.788 ? 318 HOH   B O    1 ? ? 
HETATM 3965 O O    . HOH   F 3 .   ? 0.821   20.722 22.315  1   25.163 ? 319 HOH   B O    1 ? ? 
HETATM 3966 O O    . HOH   F 3 .   ? 14.867  15.356 14.424  1   41.629 ? 320 HOH   B O    1 ? ? 
HETATM 3967 O O    . HOH   F 3 .   ? 11.414  12.603 14.047  1   32.357 ? 321 HOH   B O    1 ? ? 
HETATM 3968 O O    . HOH   F 3 .   ? -2.024  6.007  23.919  1   32.173 ? 322 HOH   B O    1 ? ? 
HETATM 3969 O O    . HOH   F 3 .   ? 3.313   7      17.942  1   27.268 ? 323 HOH   B O    1 ? ? 
HETATM 3970 O O    . HOH   F 3 .   ? 0.299   14.144 20.785  1   22.926 ? 324 HOH   B O    1 ? ? 
HETATM 3971 O O    . HOH   F 3 .   ? -0.637  13.806 41.588  1   43.466 ? 325 HOH   B O    1 ? ? 
HETATM 3972 O O    . HOH   F 3 .   ? 6.151   20.233 17.655  1   42.654 ? 326 HOH   B O    1 ? ? 
HETATM 3973 O O    . HOH   F 3 .   ? 11.028  9.866  14.53   1   29.118 ? 327 HOH   B O    1 ? ? 
HETATM 3974 O O    . HOH   F 3 .   ? -4.77   9.797  32.348  1   30.092 ? 328 HOH   B O    1 ? ? 
HETATM 3975 O O    . HOH   F 3 .   ? 1.517   10.762 23.087  1   20.355 ? 329 HOH   B O    1 ? ? 
HETATM 3976 O O    . HOH   F 3 .   ? 12.242  1.796  26.594  1   40.497 ? 330 HOH   B O    1 ? ? 
HETATM 3977 O O    . HOH   F 3 .   ? 17.381  19.01  19.758  1   41.089 ? 331 HOH   B O    1 ? ? 
HETATM 3978 O O    . HOH   F 3 .   ? 11.012  25.032 18.789  1   41.537 ? 332 HOH   B O    1 ? ? 
HETATM 3979 O O    . HOH   F 3 .   ? 4.707   1.803  37.176  1   40.376 ? 333 HOH   B O    1 ? ? 
HETATM 3980 O O    . HOH   F 3 .   ? 22.225  10.331 20.948  1   47.189 ? 334 HOH   B O    1 ? ? 
HETATM 3981 O O    . HOH   F 3 .   ? 1.239   3.756  18.72   1   42.65  ? 335 HOH   B O    1 ? ? 
HETATM 3982 O O    . HOH   F 3 .   ? -1.753  30.806 32.926  1   45.091 ? 336 HOH   B O    1 ? ? 
HETATM 3983 O O    . HOH   F 3 .   ? 11.224  8.525  10.494  1   29.629 ? 337 HOH   B O    1 ? ? 
HETATM 3984 O O    . HOH   F 3 .   ? 12.543  8.353  13.008  1   22.696 ? 338 HOH   B O    1 ? ? 
HETATM 3985 O O    . HOH   F 3 .   ? 18.291  5.017  36.344  1   38.552 ? 339 HOH   B O    1 ? ? 
HETATM 3986 O O    . HOH   F 3 .   ? 17.155  9.028  14.234  1   53.73  ? 340 HOH   B O    1 ? ? 
HETATM 3987 O O    . HOH   F 3 .   ? 1.423   -0     32.445  0.5 37.346 ? 341 HOH   B O    1 ? ? 
HETATM 3988 O O    . HOH   F 3 .   ? -0.498  2.63   21.93   1   39.683 ? 342 HOH   B O    1 ? ? 
HETATM 3989 O O    . HOH   F 3 .   ? 19.729  5.998  34.369  1   42.082 ? 343 HOH   B O    1 ? ? 
HETATM 3990 O O    . HOH   F 3 .   ? 6.781   -1.400 28.007  1   49.048 ? 344 HOH   B O    1 ? ? 
HETATM 3991 O O    . HOH   F 3 .   ? 15.128  21.219 20.187  1   41.405 ? 345 HOH   B O    1 ? ? 
HETATM 3992 O O    . HOH   F 3 .   ? 9.85    23.364 17.412  1   48.138 ? 346 HOH   B O    1 ? ? 
HETATM 3993 O O    . HOH   F 3 .   ? 15.123  9.453  12.549  1   38.069 ? 347 HOH   B O    1 ? ? 
HETATM 3994 O O    . HOH   F 3 .   ? 12.355  21.803 16.465  1   49.126 ? 348 HOH   B O    1 ? ? 
HETATM 3995 O O    . HOH   F 3 .   ? 7.604   4.349  34.067  1   35.561 ? 349 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    . GLY   A 1   ? 0.766175 0.422821 0.64385  -0.0181301  -0.0282252  -0.143595   13  GLY   A N    
2    C CA   . GLY   A 1   ? 0.734657 0.421186 0.633081 -0.0451874  -0.0295056  -0.135146   13  GLY   A CA   
3    C C    . GLY   A 1   ? 0.661856 0.408071 0.568098 -0.0381218  -0.0282909  -0.123326   13  GLY   A C    
4    O O    . GLY   A 1   ? 0.647572 0.416052 0.543106 -0.0182893  -0.0285629  -0.126139   13  GLY   A O    
5    H H1   . GLY   A 1   ? 0.80626  0.424551 0.678222 -0.0217886  -0.0302445  -0.153355   13  GLY   A H1   
6    H H2   . GLY   A 1   ? 0.756309 0.410908 0.632397 -0.00695751 -0.0228645  -0.129195   13  GLY   A H2   
7    H H3   . GLY   A 1   ? 0.755214 0.434668 0.626936 -0.00820886 -0.0308727  -0.153726   13  GLY   A H3   
8    H HA2  . GLY   A 1   ? 0.747763 0.433897 0.648698 -0.0586244  -0.0357088  -0.150675   13  GLY   A HA2  
9    H HA3  . GLY   A 1   ? 0.740396 0.408067 0.645016 -0.055018   -0.0252532  -0.122009   13  GLY   A HA3  
10   N N    . ALA   A 2   ? 0.622055 0.393191 0.546817 -0.0551724  -0.0269383  -0.110581   14  ALA   A N    
11   C CA   . ALA   A 2   ? 0.584741 0.407394 0.51817  -0.0518835  -0.0285191  -0.103619   14  ALA   A CA   
12   C C    . ALA   A 2   ? 0.554514 0.388869 0.478926 -0.0302075  -0.0231867  -0.0902958  14  ALA   A C    
13   O O    . ALA   A 2   ? 0.518955 0.382288 0.438112 -0.0204572  -0.0264506  -0.0924036  14  ALA   A O    
14   C CB   . ALA   A 2   ? 0.555031 0.399059 0.509659 -0.0701778  -0.0268393  -0.0930747  14  ALA   A CB   
15   H H    . ALA   A 2   ? 0.641505 0.396431 0.573323 -0.0688216  -0.0249029  -0.105991   14  ALA   A H    
16   H HA   . ALA   A 2   ? 0.580202 0.418438 0.510923 -0.0517521  -0.0349539  -0.116022   14  ALA   A HA   
17   H HB1  . ALA   A 2   ? 0.571153 0.417992 0.533014 -0.0844664  -0.0313714  -0.10289    14  ALA   A HB1  
18   H HB2  . ALA   A 2   ? 0.563874 0.391563 0.520325 -0.0730507  -0.0206535  -0.0821984  14  ALA   A HB2  
19   H HB3  . ALA   A 2   ? 0.529056 0.40209  0.488063 -0.0645805  -0.0275359  -0.0876084  14  ALA   A HB3  
20   N N    . PRO   A 3   ? 0.547566 0.363768 0.469956 -0.0233818  -0.0152606  -0.0750011  15  PRO   A N    
21   C CA   . PRO   A 3   ? 0.543115 0.376554 0.45881  -0.0051758  -0.0111332  -0.0637432  15  PRO   A CA   
22   C C    . PRO   A 3   ? 0.523544 0.364133 0.424129 0.0125674   -0.0131144  -0.0741741  15  PRO   A C    
23   O O    . PRO   A 3   ? 0.471909 0.34486  0.370497 0.0192722   -0.0133542  -0.0697076  15  PRO   A O    
24   C CB   . PRO   A 3   ? 0.561584 0.369123 0.475122 -0.0008477  -0.00395631 -0.0493638  15  PRO   A CB   
25   C CG   . PRO   A 3   ? 0.567876 0.362119 0.493481 -0.0228766  -0.00297787 -0.0458363  15  PRO   A CG   
26   C CD   . PRO   A 3   ? 0.584055 0.367767 0.510773 -0.0344218  -0.0101335  -0.0656632  15  PRO   A CD   
27   H HA   . PRO   A 3   ? 0.508934 0.367023 0.431729 -0.00826276 -0.0114708  -0.0576207  15  PRO   A HA   
28   H HB2  . PRO   A 3   ? 0.584161 0.368798 0.487881 0.00903337  -0.00346415 -0.0533639  15  PRO   A HB2  
29   H HB3  . PRO   A 3   ? 0.538534 0.363462 0.453214 0.00484702  -0.00105308 -0.0390728  15  PRO   A HB3  
30   H HG2  . PRO   A 3   ? 0.588497 0.358178 0.510712 -0.0230356  0.00089578  -0.03783    15  PRO   A HG2  
31   H HG3  . PRO   A 3   ? 0.543195 0.361982 0.478518 -0.0292041  -0.00208728 -0.0398912  15  PRO   A HG3  
32   H HD2  . PRO   A 3   ? 0.615028 0.366489 0.533131 -0.0318586  -0.0105468  -0.071764   15  PRO   A HD2  
33   H HD3  . PRO   A 3   ? 0.580438 0.371506 0.518567 -0.050579   -0.0110682  -0.0657425  15  PRO   A HD3  
34   N N    . ALA   A 4   ? 0.530413 0.340288 0.419782 0.0197382   -0.0143034  -0.0883246  16  ALA   A N    
35   C CA   . ALA   A 4   ? 0.554463 0.374805 0.428776 0.0386128   -0.0152837  -0.100783   16  ALA   A CA   
36   C C    . ALA   A 4   ? 0.542943 0.398697 0.415448 0.0329887   -0.0214345  -0.110737   16  ALA   A C    
37   O O    . ALA   A 4   ? 0.505967 0.392173 0.369196 0.0452699   -0.0204881  -0.111154   16  ALA   A O    
38   C CB   . ALA   A 4   ? 0.595529 0.371057 0.457451 0.0487605   -0.0161957  -0.117424   16  ALA   A CB   
39   H H    . ALA   A 4   ? 0.563936 0.345766 0.454653 0.0128167   -0.0143549  -0.0905768  16  ALA   A H    
40   H HA   . ALA   A 4   ? 0.5357   0.371665 0.408349 0.0495591   -0.0112625  -0.0910471  16  ALA   A HA   
41   H HB1  . ALA   A 4   ? 0.610579 0.363098 0.472417 0.0539102   -0.0125446  -0.108483   16  ALA   A HB1  
42   H HB2  . ALA   A 4   ? 0.615923 0.374867 0.479665 0.0358742   -0.0204822  -0.127755   16  ALA   A HB2  
43   H HB3  . ALA   A 4   ? 0.606139 0.392677 0.45788  0.0632765   -0.0163767  -0.12697    16  ALA   A HB3  
44   N N    . THR   A 5   ? 0.543309 0.398762 0.424494 0.0143202   -0.0277654  -0.117539   17  THR   A N    
45   C CA   . THR   A 5   ? 0.519893 0.409635 0.398325 0.010283    -0.0350915  -0.125798   17  THR   A CA   
46   C C    . THR   A 5   ? 0.474934 0.400636 0.358078 0.0117128   -0.0338682  -0.106508   17  THR   A C    
47   O O    . THR   A 5   ? 0.457258 0.412457 0.330999 0.0165414   -0.0371449  -0.10686    17  THR   A O    
48   C CB   . THR   A 5   ? 0.543026 0.429028 0.431708 -0.00941055 -0.043061   -0.137663   17  THR   A CB   
49   O OG1  . THR   A 5   ? 0.574433 0.422954 0.45458  -0.0105155  -0.0447716  -0.157887   17  THR   A OG1  
50   C CG2  . THR   A 5   ? 0.526736 0.452055 0.412102 -0.0119231  -0.0522553  -0.14527    17  THR   A CG2  
51   H H    . THR   A 5   ? 0.549153 0.384915 0.437993 0.00400234  -0.0276339  -0.116393   17  THR   A H    
52   H HA   . THR   A 5   ? 0.538874 0.432102 0.404348 0.0202003   -0.0360098  -0.136882   17  THR   A HA   
53   H HB   . THR   A 5   ? 0.525279 0.407741 0.427415 -0.0193518  -0.0414032  -0.127983   17  THR   A HB   
55   H HG21 . THR   A 5   ? 0.542288 0.465516 0.433232 -0.0235618  -0.0578755  -0.156295   17  THR   A HG21 
56   H HG22 . THR   A 5   ? 0.538952 0.471952 0.409885 -0.00151972 -0.052853   -0.152699   17  THR   A HG22 
57   H HG23 . THR   A 5   ? 0.503737 0.449665 0.39533  -0.0120501  -0.0521548  -0.131592   17  THR   A HG23 
58   N N    . VAL   A 6   ? 0.414799 0.336715 0.311081 0.0069152   -0.0293978  -0.089577   18  VAL   A N    
59   C CA   . VAL   A 6   ? 0.391699 0.339316 0.291625 0.00789869  -0.0287872  -0.0733382  18  VAL   A CA   
60   C C    . VAL   A 6   ? 0.392542 0.352104 0.280852 0.0207107   -0.0234716  -0.0665596  18  VAL   A C    
61   O O    . VAL   A 6   ? 0.372595 0.357041 0.255612 0.0216459   -0.0249762  -0.0589077  18  VAL   A O    
62   C CB   . VAL   A 6   ? 0.379704 0.321598 0.295203 0.00070603  -0.0253908  -0.060439   18  VAL   A CB   
63   C CG1  . VAL   A 6   ? 0.351696 0.313804 0.268394 0.00274547  -0.0257134  -0.0467748  18  VAL   A CG1  
64   C CG2  . VAL   A 6   ? 0.389439 0.328278 0.319271 -0.012854   -0.0292139  -0.0660394  18  VAL   A CG2  
65   H H    . VAL   A 6   ? 0.432206 0.334318 0.334265 0.0027447   -0.0268447  -0.0884266  18  VAL   A H    
66   H HA   . VAL   A 6   ? 0.390047 0.353574 0.289317 0.00510623  -0.0342104  -0.0750861  18  VAL   A HA   
67   H HB   . VAL   A 6   ? 0.383203 0.310816 0.297797 0.00397757  -0.020222   -0.057544   18  VAL   A HB   
68   H HG11 . VAL   A 6   ? 0.353753 0.328713 0.265909 0.00327027  -0.0303972  -0.047918   18  VAL   A HG11 
69   H HG12 . VAL   A 6   ? 0.350055 0.312879 0.261775 0.00805246  -0.0215842  -0.0414571  18  VAL   A HG12 
70   H HG13 . VAL   A 6   ? 0.343857 0.305627 0.270446 -0.00183527 -0.0255847  -0.0423059  18  VAL   A HG13 
71   H HG21 . VAL   A 6   ? 0.375789 0.315978 0.314688 -0.0160582  -0.0264603  -0.0580426  18  VAL   A HG21 
72   H HG22 . VAL   A 6   ? 0.405992 0.327548 0.335007 -0.016558   -0.0285965  -0.0737681  18  VAL   A HG22 
73   H HG23 . VAL   A 6   ? 0.385453 0.339995 0.316089 -0.0146485  -0.0351515  -0.0699411  18  VAL   A HG23 
74   N N    . THR   A 7   ? 0.405665 0.348962 0.290127 0.0304234   -0.0174632  -0.0683051  19  THR   A N    
75   C CA   . THR   A 7   ? 0.425364 0.387791 0.300625 0.0440048   -0.0124173  -0.064152   19  THR   A CA   
76   C C    . THR   A 7   ? 0.425103 0.413058 0.286377 0.0494793   -0.0148484  -0.0735699  19  THR   A C    
77   O O    . THR   A 7   ? 0.398481 0.418122 0.255185 0.0502847   -0.0129381  -0.0638402  19  THR   A O    
78   C CB   . THR   A 7   ? 0.467764 0.407939 0.33988  0.058003    -0.00736334 -0.0679179  19  THR   A CB   
79   O OG1  . THR   A 7   ? 0.476071 0.404757 0.359228 0.0521716   -0.00461528 -0.0538032  19  THR   A OG1  
80   C CG2  . THR   A 7   ? 0.490969 0.457741 0.353554 0.0758118   -0.00281779 -0.0688851  19  THR   A CG2  
81   H H    . THR   A 7   ? 0.421342 0.342642 0.30922  0.0287376   -0.0165413  -0.0714204  19  THR   A H    
82   H HA   . THR   A 7   ? 0.404915 0.380488 0.28483  0.0406103   -0.0108788  -0.0521858  19  THR   A HA   
83   H HB   . THR   A 7   ? 0.492405 0.40966  0.36134  0.0588669   -0.009349   -0.0792917  19  THR   A HB   
85   H HG21 . THR   A 7   ? 0.493191 0.449252 0.356266 0.0854549   0.00025239  -0.0667984  19  THR   A HG21 
86   H HG22 . THR   A 7   ? 0.465697 0.458837 0.330467 0.0714867   -0.00180033 -0.0594402  19  THR   A HG22 
87   H HG23 . THR   A 7   ? 0.501149 0.471023 0.354786 0.082101    -0.00407434 -0.0811437  19  THR   A HG23 
88   N N    . GLU   A 8   ? 0.44871  0.423832 0.302647 0.0512533   -0.0191924  -0.0923265  20  GLU   A N    
89   C CA   . GLU   A 8   ? 0.484243 0.484321 0.321549 0.0592391   -0.0211954  -0.105206   20  GLU   A CA   
90   C C    . GLU   A 8   ? 0.464005 0.493058 0.298408 0.0485818   -0.0272312  -0.097731   20  GLU   A C    
91   O O    . GLU   A 8   ? 0.457335 0.520117 0.277839 0.053981    -0.0260951  -0.0959868  20  GLU   A O    
92   C CB   . GLU   A 8   ? 0.559449 0.533297 0.388419 0.064076    -0.025275   -0.131297   20  GLU   A CB   
93   C CG   . GLU   A 8   ? 0.661818 0.602619 0.488039 0.0797734   -0.0200458  -0.139967   20  GLU   A CG   
94   C CD   . GLU   A 8   ? 0.785627 0.680912 0.60624  0.080393    -0.0247709  -0.164106   20  GLU   A CD   
95   O OE1  . GLU   A 8   ? 0.799248 0.690023 0.619244 0.0661604   -0.0327719  -0.177978   20  GLU   A OE1  
96   O OE2  . GLU   A 8   ? 0.861124 0.722859 0.678157 0.0951386   -0.0209424  -0.168685   20  GLU   A OE2  
97   H H    . GLU   A 8   ? 0.462592 0.413562 0.321476 0.0466247   -0.0210261  -0.0979268  20  GLU   A H    
98   H HA   . GLU   A 8   ? 0.485049 0.501948 0.316862 0.0694297   -0.016076   -0.102368   20  GLU   A HA   
99   H HB2  . GLU   A 8   ? 0.566797 0.525099 0.403174 0.0521537   -0.0300587  -0.133827   20  GLU   A HB2  
100  H HB3  . GLU   A 8   ? 0.576219 0.570307 0.393336 0.0687549   -0.0272757  -0.140893   20  GLU   A HB3  
101  H HG2  . GLU   A 8   ? 0.662243 0.623041 0.479987 0.0938206   -0.0161374  -0.141991   20  GLU   A HG2  
102  H HG3  . GLU   A 8   ? 0.643452 0.572714 0.479535 0.077157    -0.0169672  -0.126661   20  GLU   A HG3  
103  N N    . GLN   A 9   ? 0.420909 0.439466 0.267361 0.0349259   -0.0336103  -0.093089   21  GLN   A N    
104  C CA   . GLN   A 9   ? 0.411472 0.452593 0.253879 0.0284438   -0.0420525  -0.0905656  21  GLN   A CA   
105  C C    . GLN   A 9   ? 0.382887 0.427099 0.237122 0.0203104   -0.0442174  -0.0693512  21  GLN   A C    
106  O O    . GLN   A 9   ? 0.391987 0.454313 0.241689 0.0179822   -0.0514807  -0.0629096  21  GLN   A O    
107  C CB   . GLN   A 9   ? 0.44206  0.474635 0.287615 0.0217378   -0.0509272  -0.109692   21  GLN   A CB   
108  C CG   . GLN   A 9   ? 0.495958 0.517007 0.328834 0.0287595   -0.0507052  -0.135164   21  GLN   A CG   
109  C CD   . GLN   A 9   ? 0.524849 0.532971 0.361947 0.0180538   -0.0597751  -0.156541   21  GLN   A CD   
110  O OE1  . GLN   A 9   ? 0.506243 0.526715 0.354702 0.00620551  -0.06749    -0.15356    21  GLN   A OE1  
111  N NE2  . GLN   A 9   ? 0.589834 0.57335  0.41778  0.0227374   -0.0592849  -0.179579   21  GLN   A NE2  
112  H H    . GLN   A 9   ? 0.42074  0.419313 0.278003 0.030612    -0.0327146  -0.091423   21  GLN   A H    
113  H HA   . GLN   A 9   ? 0.422209 0.485131 0.251143 0.0338113   -0.0415499  -0.0904567  21  GLN   A HA   
114  H HB2  . GLN   A 9   ? 0.436058 0.451522 0.295714 0.0146626   -0.0511492  -0.108044   21  GLN   A HB2  
115  H HB3  . GLN   A 9   ? 0.443187 0.495711 0.284973 0.0195495   -0.0571128  -0.107514   21  GLN   A HB3  
116  H HG2  . GLN   A 9   ? 0.500421 0.543346 0.318758 0.0363951   -0.050513   -0.138136   21  GLN   A HG2  
117  H HG3  . GLN   A 9   ? 0.495165 0.495843 0.330272 0.0335538   -0.0446508  -0.135675   21  GLN   A HG3  
118  H HE21 . GLN   A 9   ? 0.593984 0.556709 0.428125 0.0141547   -0.0623861  -0.190004   21  GLN   A HE21 
119  H HE22 . GLN   A 9   ? 0.590189 0.577561 0.40575  0.0344904   -0.0558947  -0.184876   21  GLN   A HE22 
120  N N    . GLY   A 10  ? 0.34246  0.368622 0.210381 0.0175493   -0.0388148  -0.0594283  22  GLY   A N    
121  C CA   . GLY   A 10  ? 0.31959  0.344225 0.198745 0.0113913   -0.0414649  -0.0442857  22  GLY   A CA   
122  C C    . GLY   A 10  ? 0.32429  0.363554 0.19433  0.011356    -0.0410447  -0.0262033  22  GLY   A C    
123  O O    . GLY   A 10  ? 0.3356   0.386772 0.195983 0.0138259   -0.034987   -0.0218532  22  GLY   A O    
124  H H    . GLY   A 10  ? 0.348381 0.36339  0.217722 0.0206967   -0.0337107  -0.0625711  22  GLY   A H    
125  H HA2  . GLY   A 10  ? 0.32583  0.353222 0.209158 0.00870579  -0.0476777  -0.0479161  22  GLY   A HA2  
126  H HA3  . GLY   A 10  ? 0.313924 0.324783 0.202833 0.00962311  -0.0376353  -0.0423442  22  GLY   A HA3  
127  N N    . GLU   A 11  ? 0.318007 0.355179 0.192608 0.00823835  -0.0473667  -0.0152649  23  GLU   A N    
128  C CA   . GLU   A 11  ? 0.345263 0.385107 0.212178 0.00550185  -0.04836    0.00393179  23  GLU   A CA   
129  C C    . GLU   A 11  ? 0.350211 0.374181 0.226648 0.00078666  -0.0425842  0.0112385   23  GLU   A C    
130  O O    . GLU   A 11  ? 0.350562 0.359779 0.241323 0.00109594  -0.0421753  0.0057289   23  GLU   A O    
131  C CB   . GLU   A 11  ? 0.383777 0.421078 0.251751 0.0075804   -0.0589193  0.0109039   23  GLU   A CB   
132  C CG   . GLU   A 11  ? 0.448347 0.476798 0.307504 0.00463093  -0.061572   0.0325671   23  GLU   A CG   
133  C CD   . GLU   A 11  ? 0.536031 0.559321 0.394177 0.0114953   -0.0732125  0.0406273   23  GLU   A CD   
134  O OE1  . GLU   A 11  ? 0.587275 0.620956 0.453964 0.0182616   -0.0793762  0.0288233   23  GLU   A OE1  
135  O OE2  . GLU   A 11  ? 0.601797 0.609984 0.451026 0.00982232  -0.0764265  0.0593103   23  GLU   A OE2  
136  H H    . GLU   A 11  ? 0.322401 0.355346 0.205431 0.00782507  -0.0514244  -0.0200222  23  GLU   A H    
137  H HA   . GLU   A 11  ? 0.356517 0.411108 0.211094 0.00563249  -0.0464316  0.00722154  23  GLU   A HA   
138  H HB2  . GLU   A 11  ? 0.396034 0.447406 0.257319 0.0104412   -0.0632919  0.00605796  23  GLU   A HB2  
139  H HB3  . GLU   A 11  ? 0.379017 0.406835 0.260073 0.00849603  -0.0602699  0.0056233   23  GLU   A HB3  
140  H HG2  . GLU   A 11  ? 0.443282 0.457284 0.309313 0.00100367  -0.0580387  0.0354013   23  GLU   A HG2  
141  H HG3  . GLU   A 11  ? 0.458969 0.499516 0.305354 0.00181298  -0.0593076  0.0393257   23  GLU   A HG3  
142  N N    . ASP   A 12  ? 0.33597  0.366622 0.204303 -0.00490666 -0.0386141  0.0237727   24  ASP   A N    
143  C CA   . ASP   A 12  ? 0.337201 0.355599 0.213597 -0.0116465  -0.0349144  0.0300198   24  ASP   A CA   
144  C C    . ASP   A 12  ? 0.353055 0.348633 0.230985 -0.0155132  -0.0421109  0.0405044   24  ASP   A C    
145  O O    . ASP   A 12  ? 0.371661 0.365672 0.237774 -0.020253   -0.0461979  0.0550236   24  ASP   A O    
146  C CB   . ASP   A 12  ? 0.333762 0.373031 0.203145 -0.018443   -0.0281661  0.0377676   24  ASP   A CB   
147  C CG   . ASP   A 12  ? 0.337315 0.371099 0.215156 -0.0272329  -0.0248153  0.041925    24  ASP   A CG   
148  O OD1  . ASP   A 12  ? 0.327969 0.338569 0.215372 -0.0272636  -0.0276108  0.0383777   24  ASP   A OD1  
149  O OD2  . ASP   A 12  ? 0.327986 0.385603 0.203216 -0.0335261  -0.0193353  0.0470513   24  ASP   A OD2  
150  H H    . ASP   A 12  ? 0.351452 0.396831 0.209002 -0.00556352 -0.0382381  0.0281928   24  ASP   A H    
151  H HA   . ASP   A 12  ? 0.323873 0.336453 0.209375 -0.00873994 -0.0323636  0.0215077   24  ASP   A HA   
152  H HB2  . ASP   A 12  ? 0.332974 0.386757 0.200808 -0.0125357  -0.0240909  0.0299373   24  ASP   A HB2  
153  H HB3  . ASP   A 12  ? 0.350773 0.396814 0.2106   -0.0230943  -0.0300288  0.0478479   24  ASP   A HB3  
154  N N    . ILE   A 13  ? 0.338619 0.316192 0.22975  -0.0122055  -0.0437099  0.033398    25  ILE   A N    
155  C CA   . ILE   A 13  ? 0.364307 0.318155 0.257222 -0.0109518  -0.0510607  0.0394482   25  ILE   A CA   
156  C C    . ILE   A 13  ? 0.367316 0.304077 0.263387 -0.0194173  -0.0487323  0.0414461   25  ILE   A C    
157  O O    . ILE   A 13  ? 0.402527 0.315159 0.301851 -0.0165249  -0.0539467  0.0409556   25  ILE   A O    
158  C CB   . ILE   A 13  ? 0.37092  0.322542 0.276095 0.0006442   -0.0555543  0.0285713   25  ILE   A CB   
159  C CG1  . ILE   A 13  ? 0.356314 0.313018 0.2754   0.00113209  -0.0485213  0.0151331   25  ILE   A CG1  
160  C CG2  . ILE   A 13  ? 0.376878 0.346258 0.278271 0.00686358  -0.0608403  0.0267376   25  ILE   A CG2  
161  C CD1  . ILE   A 13  ? 0.380153 0.33726  0.31348  0.00943213  -0.051507   0.00612543  25  ILE   A CD1  
162  H H    . ILE   A 13  ? 0.32978  0.309853 0.228229 -0.00991692 -0.0400588  0.0247417   25  ILE   A H    
163  H HA   . ILE   A 13  ? 0.380836 0.332605 0.264054 -0.0120937  -0.0552056  0.0495395   25  ILE   A HA   
164  H HB   . ILE   A 13  ? 0.382334 0.318514 0.288622 0.00385011  -0.0602141  0.0318025   25  ILE   A HB   
165  H HG12 . ILE   A 13  ? 0.35228  0.320533 0.270579 6.926e-05   -0.044999   0.0111924   25  ILE   A HG12 
166  H HG13 . ILE   A 13  ? 0.358859 0.309151 0.27804  -0.00321847 -0.0451318  0.0163232   25  ILE   A HG13 
167  H HG21 . ILE   A 13  ? 0.374399 0.345011 0.284689 0.0131549   -0.0645432  0.0210192   25  ILE   A HG21 
168  H HG22 . ILE   A 13  ? 0.366782 0.348778 0.26738  0.0047212   -0.0566272  0.0207296   25  ILE   A HG22 
169  H HG23 . ILE   A 13  ? 0.391894 0.359985 0.282379 0.00669583  -0.0649736  0.0370267   25  ILE   A HG23 
170  H HD11 . ILE   A 13  ? 0.382609 0.327804 0.316048 0.013359    -0.0556676  0.00887532  25  ILE   A HD11 
171  H HD12 . ILE   A 13  ? 0.360067 0.320322 0.300531 0.00794019  -0.0461652  2.741e-05   25  ILE   A HD12 
172  H HD13 . ILE   A 13  ? 0.371237 0.339062 0.306343 0.0124695   -0.0546924  0.00354643  25  ILE   A HD13 
173  N N    . THR   A 14  ? 0.358984 0.309399 0.253589 -0.0291582  -0.0418379  0.0427403   26  THR   A N    
174  C CA   . THR   A 14  ? 0.366677 0.306043 0.263404 -0.0402222  -0.0408872  0.0440651   26  THR   A CA   
175  C C    . THR   A 14  ? 0.408294 0.333087 0.293758 -0.0542621  -0.0451249  0.0602466   26  THR   A C    
176  O O    . THR   A 14  ? 0.418593 0.35564  0.293612 -0.0575819  -0.0450608  0.0723864   26  THR   A O    
177  C CB   . THR   A 14  ? 0.363467 0.328873 0.264988 -0.044346   -0.032777   0.0387479   26  THR   A CB   
178  O OG1  . THR   A 14  ? 0.358089 0.350428 0.252577 -0.0494473  -0.0285799  0.0466339   26  THR   A OG1  
179  C CG2  . THR   A 14  ? 0.333891 0.306306 0.244362 -0.0317548  -0.0287484  0.026126    26  THR   A CG2  
180  H H    . THR   A 14  ? 0.350952 0.319571 0.243326 -0.0285654  -0.0379885  0.0418148   26  THR   A H    
181  H HA   . THR   A 14  ? 0.372709 0.296494 0.274903 -0.03564    -0.0434153  0.0376741   26  THR   A HA   
182  H HB   . THR   A 14  ? 0.364547 0.32389  0.267769 -0.0522526  -0.0333872  0.03849     26  THR   A HB   
184  H HG21 . THR   A 14  ? 0.327539 0.315946 0.239189 -0.0323176  -0.024158   0.0247377   26  THR   A HG21 
185  H HG22 . THR   A 14  ? 0.332987 0.307026 0.24279  -0.0251153  -0.0291767  0.024564    26  THR   A HG22 
186  H HG23 . THR   A 14  ? 0.33646  0.29641  0.251719 -0.0298942  -0.0304646  0.0211708   26  THR   A HG23 
187  N N    . SER   A 15  ? 0.417729 0.315473 0.304142 -0.0634893  -0.0488164  0.060177    27  SER   A N    
188  C CA   . SER   A 15  ? 0.468832 0.345676 0.344865 -0.0816643  -0.0528017  0.0759304   27  SER   A CA   
189  C C    . SER   A 15  ? 0.452321 0.36505  0.326646 -0.100512   -0.045593   0.0841242   27  SER   A C    
190  O O    . SER   A 15  ? 0.433633 0.351793 0.297362 -0.113557   -0.0453071  0.101934    27  SER   A O    
191  C CB   . SER   A 15  ? 0.516532 0.352308 0.394186 -0.0869247  -0.0590064  0.0694821   27  SER   A CB   
192  O OG   . SER   A 15  ? 0.555378 0.359996 0.432309 -0.0675366  -0.0663128  0.0657946   27  SER   A OG   
193  H H    . SER   A 15  ? 0.416889 0.30821  0.310035 -0.0590573  -0.0488945  0.0497422   27  SER   A H    
194  H HA   . SER   A 15  ? 0.482641 0.349699 0.350763 -0.0778042  -0.0564995  0.0859729   27  SER   A HA   
195  H HB2  . SER   A 15  ? 0.501134 0.347595 0.386448 -0.087247   -0.0561046  0.0573765   27  SER   A HB2  
196  H HB3  . SER   A 15  ? 0.5435   0.364773 0.414675 -0.102711   -0.061145   0.0795884   27  SER   A HB3  
198  N N    . LYS   A 16  ? 0.428257 0.370161 0.313035 -0.100194   -0.0395062  0.0716661   28  LYS   A N    
199  C CA   . LYS   A 16  ? 0.453864 0.437551 0.340413 -0.114769   -0.03281    0.0766272   28  LYS   A CA   
200  C C    . LYS   A 16  ? 0.407033 0.429272 0.289327 -0.105146   -0.0262694  0.0811313   28  LYS   A C    
201  O O    . LYS   A 16  ? 0.396011 0.457242 0.278222 -0.115665   -0.0204703  0.087403    28  LYS   A O    
202  C CB   . LYS   A 16  ? 0.45289  0.457515 0.351277 -0.113823   -0.029713   0.0620331   28  LYS   A CB   
203  C CG   . LYS   A 16  ? 0.508121 0.49113  0.409372 -0.131356   -0.035075   0.0572871   28  LYS   A CG   
204  C CD   . LYS   A 16  ? 0.532508 0.533192 0.443118 -0.123996   -0.0335523  0.0406665   28  LYS   A CD   
205  C CE   . LYS   A 16  ? 0.607321 0.578067 0.51822  -0.136051   -0.040502   0.0308248   28  LYS   A CE   
206  N NZ   . LYS   A 16  ? 0.643159 0.630475 0.560094 -0.124893   -0.0393163  0.0145689   28  LYS   A NZ   
207  H H    . LYS   A 16  ? 0.420987 0.358938 0.311988 -0.0900526  -0.0395439  0.060303    28  LYS   A H    
208  H HA   . LYS   A 16  ? 0.46798  0.443622 0.350244 -0.132208   -0.0347613  0.0867229   28  LYS   A HA   
209  H HB2  . LYS   A 16  ? 0.439397 0.439878 0.341105 -0.0981052  -0.0291656  0.0528627   28  LYS   A HB2  
210  H HB3  . LYS   A 16  ? 0.444514 0.484431 0.34517  -0.116328   -0.024655   0.0640266   28  LYS   A HB3  
211  H HG2  . LYS   A 16  ? 0.523766 0.518551 0.423963 -0.149485   -0.0346253  0.0653784   28  LYS   A HG2  
212  H HG3  . LYS   A 16  ? 0.528267 0.474003 0.425427 -0.129938   -0.0404421  0.0571063   28  LYS   A HG3  
213  H HD2  . LYS   A 16  ? 0.515278 0.513187 0.427209 -0.106546   -0.0319943  0.0349623   28  LYS   A HD2  
214  H HD3  . LYS   A 16  ? 0.521596 0.55814  0.436189 -0.128114   -0.0296146  0.0418167   28  LYS   A HD3  
215  H HE2  . LYS   A 16  ? 0.62325  0.599785 0.534075 -0.155443   -0.0419634  0.0350679   28  LYS   A HE2  
216  H HE3  . LYS   A 16  ? 0.621567 0.555988 0.527978 -0.132167   -0.0447564  0.0306354   28  LYS   A HE3  
217  H HZ1  . LYS   A 16  ? 0.611322 0.63228  0.532087 -0.12657    -0.0359372  0.0153783   28  LYS   A HZ1  
218  H HZ2  . LYS   A 16  ? 0.611627 0.592794 0.528759 -0.108868   -0.0377086  0.0114455   28  LYS   A HZ2  
219  H HZ3  . LYS   A 16  ? 0.641462 0.612644 0.557633 -0.132185   -0.0436902  0.00685898  28  LYS   A HZ3  
220  N N    . LYS   A 17  ? 0.397065 0.412057 0.27643  -0.0855617  -0.0272715  0.0760954   29  LYS   A N    
221  C CA   . LYS   A 17  ? 0.402428 0.450507 0.276646 -0.0743881  -0.0219447  0.0751026   29  LYS   A CA   
222  C C    . LYS   A 17  ? 0.395356 0.480247 0.277708 -0.0681072  -0.0141048  0.0651109   29  LYS   A C    
223  O O    . LYS   A 17  ? 0.371527 0.495809 0.2502   -0.0689704  -0.00808542 0.0686639   29  LYS   A O    
224  C CB   . LYS   A 17  ? 0.452381 0.515633 0.312141 -0.0850122  -0.0214316  0.0927605   29  LYS   A CB   
225  C CG   . LYS   A 17  ? 0.51511  0.542962 0.364359 -0.0831331  -0.0301142  0.1027      29  LYS   A CG   
226  C CD   . LYS   A 17  ? 0.546603 0.56937  0.395648 -0.0615044  -0.0335858  0.0904728   29  LYS   A CD   
227  C CE   . LYS   A 17  ? 0.634593 0.638487 0.471434 -0.0573199  -0.0422378  0.101907    29  LYS   A CE   
228  N NZ   . LYS   A 17  ? 0.698306 0.66076  0.542905 -0.0516024  -0.0503511  0.0986989   29  LYS   A NZ   
229  H H    . LYS   A 17  ? 0.402128 0.391879 0.282957 -0.0788709  -0.0316201  0.0718236   29  LYS   A H    
230  H HA   . LYS   A 17  ? 0.400862 0.436713 0.274991 -0.0619238  -0.0243023  0.0685821   29  LYS   A HA   
231  H HB2  . LYS   A 17  ? 0.464587 0.536202 0.324555 -0.100777   -0.0197619  0.101352    29  LYS   A HB2  
232  H HB3  . LYS   A 17  ? 0.446571 0.537237 0.302805 -0.0772791  -0.0170781  0.089685    29  LYS   A HB3  
233  H HG2  . LYS   A 17  ? 0.524522 0.52279  0.377092 -0.0884824  -0.0346269  0.104299    29  LYS   A HG2  
234  H HG3  . LYS   A 17  ? 0.533328 0.571359 0.37193  -0.0915522  -0.0295582  0.116486    29  LYS   A HG3  
235  H HD2  . LYS   A 17  ? 0.538335 0.587584 0.385648 -0.0554588  -0.0289546  0.0844241   29  LYS   A HD2  
236  H HD3  . LYS   A 17  ? 0.535864 0.543866 0.39504  -0.0553467  -0.0348038  0.079662    29  LYS   A HD3  
237  H HE2  . LYS   A 17  ? 0.651111 0.656961 0.477699 -0.0679076  -0.042403   0.117476    29  LYS   A HE2  
238  H HE3  . LYS   A 17  ? 0.624499 0.643139 0.457986 -0.0471442  -0.0426066  0.0958623   29  LYS   A HE3  
239  H HZ1  . LYS   A 17  ? 0.684745 0.632707 0.532879 -0.0602448  -0.049969   0.100765    29  LYS   A HZ1  
240  H HZ2  . LYS   A 17  ? 0.660719 0.624699 0.514002 -0.0419199  -0.0501653  0.0855977   29  LYS   A HZ2  
241  H HZ3  . LYS   A 17  ? 0.697723 0.648308 0.534653 -0.0486745  -0.0561308  0.107508    29  LYS   A HZ3  
242  N N    . ASP   A 18  ? 0.353683 0.427237 0.246334 -0.0598719  -0.0142553  0.0530896   30  ASP   A N    
243  C CA   . ASP   A 18  ? 0.333911 0.435924 0.233453 -0.050335   -0.00836827 0.0449132   30  ASP   A CA   
244  C C    . ASP   A 18  ? 0.314401 0.406848 0.214085 -0.0292649  -0.00671677 0.0337173   30  ASP   A C    
245  O O    . ASP   A 18  ? 0.311536 0.412525 0.216235 -0.0182635  -0.00332102 0.0272076   30  ASP   A O    
246  C CB   . ASP   A 18  ? 0.33275  0.432424 0.241217 -0.05829    -0.00986846 0.0419548   30  ASP   A CB   
247  C CG   . ASP   A 18  ? 0.353287 0.413363 0.264541 -0.0558751  -0.014944   0.03551     30  ASP   A CG   
248  O OD1  . ASP   A 18  ? 0.330695 0.370367 0.240295 -0.0443839  -0.0161208  0.0319179   30  ASP   A OD1  
249  O OD2  . ASP   A 18  ? 0.332161 0.385311 0.247267 -0.0662135  -0.0179072  0.0330612   30  ASP   A OD2  
250  H H    . ASP   A 18  ? 0.360165 0.407991 0.254922 -0.0591058  -0.0182559  0.0504991   30  ASP   A H    
251  H HA   . ASP   A 18  ? 0.335895 0.467295 0.233489 -0.052792   -0.00464844 0.0488072   30  ASP   A HA   
252  H HB2  . ASP   A 18  ? 0.327146 0.446904 0.239446 -0.0501728  -0.00651346 0.0377529   30  ASP   A HB2  
253  H HB3  . ASP   A 18  ? 0.346777 0.454385 0.255219 -0.0735137  -0.0109023  0.0481761   30  ASP   A HB3  
254  N N    . ARG   A 19  ? 0.309608 0.382025 0.203806 -0.0243749  -0.00999177 0.0318152   31  ARG   A N    
255  C CA   . ARG   A 19  ? 0.31594  0.374958 0.210836 -0.00947243 -0.00969836 0.0204757   31  ARG   A CA   
256  C C    . ARG   A 19  ? 0.320137 0.359629 0.224775 -0.00565808 -0.00950669 0.0148392   31  ARG   A C    
257  O O    . ARG   A 19  ? 0.344609 0.375383 0.250834 0.00460935  -0.00737821 0.00735556  31  ARG   A O    
258  C CB   . ARG   A 19  ? 0.307064 0.388993 0.196314 0.00341052  -0.00433407 0.0140043   31  ARG   A CB   
259  C CG   . ARG   A 19  ? 0.333272 0.437989 0.21072  0.00189343  -0.00394566 0.0171988   31  ARG   A CG   
260  C CD   . ARG   A 19  ? 0.361119 0.490355 0.231572 0.0178677   0.00142042  0.00701779  31  ARG   A CD   
261  N NE   . ARG   A 19  ? 0.383118 0.487504 0.25409  0.0330422   0.00100155  -0.00822444 31  ARG   A NE   
262  C CZ   . ARG   A 19  ? 0.40646  0.490488 0.272255 0.0364297   -0.00318271 -0.0188627  31  ARG   A CZ   
263  N NH1  . ARG   A 19  ? 0.386624 0.476454 0.244769 0.0292479   -0.00786418 -0.0164596  31  ARG   A NH1  
264  N NH2  . ARG   A 19  ? 0.408087 0.466946 0.275469 0.0471004   -0.00293653 -0.0317261  31  ARG   A NH2  
265  H H    . ARG   A 19  ? 0.323678 0.390781 0.213317 -0.0314782  -0.0129701  0.038202    31  ARG   A H    
266  H HA   . ARG   A 19  ? 0.318739 0.366722 0.210417 -0.0100828  -0.0134935  0.0204113   31  ARG   A HA   
267  H HB2  . ARG   A 19  ? 0.309772 0.407263 0.202079 0.00537482  -0.00087962 0.0151338   31  ARG   A HB2  
268  H HB3  . ARG   A 19  ? 0.314447 0.381994 0.204235 0.0118459   -0.00451522 0.00593976  31  ARG   A HB3  
269  H HG2  . ARG   A 19  ? 0.33933  0.430269 0.213182 0.00033417  -0.00821001 0.0167051   31  ARG   A HG2  
270  H HG3  . ARG   A 19  ? 0.336004 0.454781 0.212844 -0.00846366 -0.00332248 0.0269082   31  ARG   A HG3  
271  H HD2  . ARG   A 19  ? 0.368979 0.512316 0.230586 0.016616    0.0012168   0.00824999  31  ARG   A HD2  
272  H HD3  . ARG   A 19  ? 0.357538 0.508346 0.231043 0.0192764   0.00550193  0.00963522  31  ARG   A HD3  
273  H HE   . ARG   A 19  ? 0.380525 0.482885 0.255577 0.0397715   0.00345312  -0.0104025  31  ARG   A HE   
274  H HH11 . ARG   A 19  ? 0.392159 0.495021 0.248081 0.0217851   -0.00811625 -0.00626311 31  ARG   A HH11 
275  H HH12 . ARG   A 19  ? 0.401339 0.481796 0.256225 0.0317141   -0.011091   -0.0247374  31  ARG   A HH12 
276  H HH21 . ARG   A 19  ? 0.413127 0.472042 0.281666 0.0556289   0.00044773  -0.033563   31  ARG   A HH21 
277  H HH22 . ARG   A 19  ? 0.415258 0.457193 0.282439 0.0452239   -0.00640871 -0.0378958  31  ARG   A HH22 
278  N N    . GLY   A 20  ? 0.340409 0.370431 0.250174 -0.0148152  -0.0121038  0.0183699   32  GLY   A N    
279  C CA   . GLY   A 20  ? 0.314088 0.333343 0.231231 -0.0119573  -0.011183   0.0137131   32  GLY   A CA   
280  C C    . GLY   A 20  ? 0.335419 0.333598 0.256907 -0.00772767 -0.0133     0.00816328  32  GLY   A C    
281  O O    . GLY   A 20  ? 0.330618 0.32382  0.257215 -0.00371647 -0.0104839  0.00459125  32  GLY   A O    
282  H H    . GLY   A 20  ? 0.335802 0.365374 0.243457 -0.0231621  -0.0145975  0.0236871   32  GLY   A H    
283  H HA2  . GLY   A 20  ? 0.320748 0.349653 0.238236 -0.00586303 -0.00746712 0.0125104   32  GLY   A HA2  
284  H HA3  . GLY   A 20  ? 0.324919 0.343516 0.243731 -0.0189918  -0.0128736  0.0154084   32  GLY   A HA3  
285  N N    . VAL   A 21  ? 0.328801 0.318713 0.248259 -0.00940096 -0.018424   0.00884245  33  VAL   A N    
286  C CA   . VAL   A 21  ? 0.300314 0.279096 0.225536 -0.00580267 -0.0216189  0.00327754  33  VAL   A CA   
287  C C    . VAL   A 21  ? 0.317475 0.300653 0.236036 -0.00391859 -0.0252892  0.00279234  33  VAL   A C    
288  O O    . VAL   A 21  ? 0.298521 0.283595 0.209721 -0.00674145 -0.0295431  0.00999175  33  VAL   A O    
289  C CB   . VAL   A 21  ? 0.304349 0.271587 0.234996 -0.00690652 -0.0266376  0.0033333   33  VAL   A CB   
290  C CG1  . VAL   A 21  ? 0.306891 0.273202 0.24699  -0.00186582 -0.0289818  -0.00338726 33  VAL   A CG1  
291  C CG2  . VAL   A 21  ? 0.294966 0.260091 0.229147 -0.0090588  -0.0238426  0.0015322   33  VAL   A CG2  
292  H H    . VAL   A 21  ? 0.330317 0.324466 0.244554 -0.0131554  -0.0201511  0.0136857   33  VAL   A H    
293  H HA   . VAL   A 21  ? 0.303386 0.281397 0.232801 -0.00321928 -0.0183047  -0.00081097 33  VAL   A HA   
294  H HB   . VAL   A 21  ? 0.312969 0.27609  0.238353 -0.0091629  -0.0307174  0.00848925  33  VAL   A HB   
295  H HG11 . VAL   A 21  ? 0.299322 0.269143 0.243893 -0.00174827 -0.0245969  -0.00699505 33  VAL   A HG11 
296  H HG12 . VAL   A 21  ? 0.309369 0.278188 0.247096 -0.00075382 -0.0323235  -0.00318867 33  VAL   A HG12 
297  H HG13 . VAL   A 21  ? 0.308723 0.270052 0.252699 9.834e-05   -0.0316849  -0.00440544 33  VAL   A HG13 
298  H HG21 . VAL   A 21  ? 0.302588 0.259209 0.239558 -0.00785764 -0.0271934  -0.00061894 33  VAL   A HG21 
299  H HG22 . VAL   A 21  ? 0.299565 0.267906 0.229094 -0.0137656  -0.0231972  0.00528499  33  VAL   A HG22 
300  H HG23 . VAL   A 21  ? 0.289807 0.260128 0.227619 -0.00680984 -0.0195714  -0.00147932 33  VAL   A HG23 
301  N N    . LEU   A 22  ? 0.315429 0.298905 0.235572 -0.0001256  -0.0239875  -0.00561417 34  LEU   A N    
302  C CA   . LEU   A 22  ? 0.313607 0.303612 0.226565 0.00197346  -0.0278879  -0.0104641  34  LEU   A CA   
303  C C    . LEU   A 22  ? 0.332651 0.319209 0.255545 0.00093913  -0.0327774  -0.0181388  34  LEU   A C    
304  O O    . LEU   A 22  ? 0.321074 0.300568 0.255088 -0.00128894 -0.0295805  -0.022296   34  LEU   A O    
305  C CB   . LEU   A 22  ? 0.300673 0.293432 0.206494 0.00702605  -0.0228559  -0.0174876  34  LEU   A CB   
306  C CG   . LEU   A 22  ? 0.331256 0.337826 0.229446 0.0100607   -0.0174882  -0.0112066  34  LEU   A CG   
307  C CD1  . LEU   A 22  ? 0.338156 0.343608 0.232057 0.0203946   -0.0122424  -0.0199754  34  LEU   A CD1  
308  C CD2  . LEU   A 22  ? 0.323152 0.349587 0.210191 0.00732514  -0.0196913  -0.00387755 34  LEU   A CD2  
309  H H    . LEU   A 22  ? 0.310002 0.288862 0.235206 0.00059028  -0.0207401  -0.00878063 34  LEU   A H    
310  H HA   . LEU   A 22  ? 0.319744 0.315977 0.226087 0.00102103  -0.0308709  -0.00442349 34  LEU   A HA   
311  H HB2  . LEU   A 22  ? 0.311572 0.293725 0.22305  0.00761111  -0.020295   -0.0217291  34  LEU   A HB2  
312  H HB3  . LEU   A 22  ? 0.32036  0.317472 0.220784 0.00846434  -0.0258536  -0.0232056  34  LEU   A HB3  
313  H HG   . LEU   A 22  ? 0.31426  0.318987 0.217552 0.00719132  -0.0157922  -0.00553647 34  LEU   A HG   
314  H HD11 . LEU   A 22  ? 0.337787 0.32903  0.237532 0.0212024   -0.0105352  -0.0213916  34  LEU   A HD11 
315  H HD12 . LEU   A 22  ? 0.337906 0.357929 0.228244 0.0236536   -0.0089666  -0.0162248  34  LEU   A HD12 
316  H HD13 . LEU   A 22  ? 0.349186 0.354026 0.237642 0.0233044   -0.0141215  -0.027994   34  LEU   A HD13 
317  H HD21 . LEU   A 22  ? 0.32592  0.348171 0.214754 0.00161274  -0.023219   0.00324039  34  LEU   A HD21 
318  H HD22 . LEU   A 22  ? 0.335637 0.366697 0.21639  0.0104802   -0.0217517  -0.00969642 34  LEU   A HD22 
319  H HD23 . LEU   A 22  ? 0.326868 0.366551 0.21082  0.00808867  -0.0155957  -0.00031536 34  LEU   A HD23 
320  N N    . LYS   A 23  ? 0.319702 0.315944 0.238256 0.00204032  -0.040504   -0.0192003  35  LYS   A N    
321  C CA   . LYS   A 23  ? 0.309098 0.311203 0.238819 0.0013977   -0.0468972  -0.025657   35  LYS   A CA   
322  C C    . LYS   A 23  ? 0.331536 0.347051 0.254131 0.00139385  -0.0531221  -0.0351448  35  LYS   A C    
323  O O    . LYS   A 23  ? 0.329864 0.354423 0.236793 0.00486002  -0.0559375  -0.0308874  35  LYS   A O    
324  C CB   . LYS   A 23  ? 0.302882 0.30648  0.235723 0.00599136  -0.0531936  -0.0162615  35  LYS   A CB   
325  C CG   . LYS   A 23  ? 0.31314  0.331243 0.259067 0.0092599   -0.0609198  -0.0221283  35  LYS   A CG   
326  C CD   . LYS   A 23  ? 0.330308 0.347355 0.275948 0.0192894   -0.0688594  -0.0125007  35  LYS   A CD   
327  C CE   . LYS   A 23  ? 0.323593 0.362962 0.285316 0.0250751   -0.0759665  -0.0200734  35  LYS   A CE   
328  N NZ   . LYS   A 23  ? 0.33436  0.374174 0.295997 0.0396528   -0.0854121  -0.0120508  35  LYS   A NZ   
329  H H    . LYS   A 23  ? 0.327795 0.330361 0.23617  0.00330349  -0.0418488  -0.0153952  35  LYS   A H    
330  H HA   . LYS   A 23  ? 0.307287 0.304953 0.246914 -0.00166499 -0.0434958  -0.0302991  35  LYS   A HA   
331  H HB2  . LYS   A 23  ? 0.30067  0.295047 0.237432 0.00577298  -0.049548   -0.0127113  35  LYS   A HB2  
332  H HB3  . LYS   A 23  ? 0.314494 0.319289 0.236141 0.00779342  -0.0561301  -0.00919727 35  LYS   A HB3  
333  H HG2  . LYS   A 23  ? 0.31878  0.347994 0.261787 0.00799219  -0.0646787  -0.0276607  35  LYS   A HG2  
334  H HG3  . LYS   A 23  ? 0.305424 0.32431  0.263305 0.00633268  -0.0572543  -0.027493   35  LYS   A HG3  
335  H HD2  . LYS   A 23  ? 0.324419 0.328132 0.271876 0.0203214   -0.0656079  -0.00871939 35  LYS   A HD2  
336  H HD3  . LYS   A 23  ? 0.337546 0.353844 0.270507 0.0212852   -0.0728612  -0.00528072 35  LYS   A HD3  
337  H HE2  . LYS   A 23  ? 0.327079 0.380844 0.287793 0.0219218   -0.0791521  -0.0256256  35  LYS   A HE2  
338  H HE3  . LYS   A 23  ? 0.314793 0.356959 0.289008 0.0221044   -0.0711552  -0.0260114  35  LYS   A HE3  
339  H HZ1  . LYS   A 23  ? 0.347003 0.383295 0.29591  0.0419625   -0.0898814  -0.00443873 35  LYS   A HZ1  
340  H HZ2  . LYS   A 23  ? 0.336058 0.360939 0.299069 0.0427553   -0.0829225  -0.00902104 35  LYS   A HZ2  
341  H HZ3  . LYS   A 23  ? 0.335083 0.393956 0.307606 0.0437997   -0.0895955  -0.0176394  35  LYS   A HZ3  
342  N N    . ILE   A 24  ? 0.343121 0.362653 0.277135 -0.0040253  -0.0554305  -0.0478527  36  ILE   A N    
343  C CA   . ILE   A 24  ? 0.358167 0.396274 0.289166 -0.00533329 -0.0646345  -0.0587236  36  ILE   A CA   
344  C C    . ILE   A 24  ? 0.374348 0.431218 0.32419  -0.00765896 -0.0715555  -0.0613768  36  ILE   A C    
345  O O    . ILE   A 24  ? 0.370813 0.424833 0.337901 -0.0144911  -0.0671089  -0.0642055  36  ILE   A O    
346  C CB   . ILE   A 24  ? 0.389854 0.418643 0.316666 -0.0119783  -0.0627448  -0.0759921  36  ILE   A CB   
347  C CG1  . ILE   A 24  ? 0.404589 0.418281 0.314415 -0.00566997 -0.0553868  -0.075449   36  ILE   A CG1  
348  C CG2  . ILE   A 24  ? 0.421147 0.472638 0.344042 -0.0147366  -0.073785   -0.0903736  36  ILE   A CG2  
349  C CD1  . ILE   A 24  ? 0.441957 0.437723 0.346336 -0.00832115 -0.0534635  -0.0937041  36  ILE   A CD1  
350  H H    . ILE   A 24  ? 0.336267 0.348392 0.279981 -0.00808278 -0.0513371  -0.0497685  36  ILE   A H    
351  H HA   . ILE   A 24  ? 0.369525 0.41599  0.288518 2.01e-05    -0.0681911  -0.0536209  36  ILE   A HA   
352  H HB   . ILE   A 24  ? 0.389148 0.407982 0.327584 -0.018781   -0.0594598  -0.0791316  36  ILE   A HB   
353  H HG12 . ILE   A 24  ? 0.407949 0.434658 0.306071 -0.00024712 -0.057822   -0.0717414  36  ILE   A HG12 
354  H HG13 . ILE   A 24  ? 0.394868 0.398382 0.307992 -0.00424667 -0.0494014  -0.0663351  36  ILE   A HG13 
355  H HG21 . ILE   A 24  ? 0.430946 0.472977 0.349796 -0.0190537  -0.0730084  -0.103132   36  ILE   A HG21 
356  H HG22 . ILE   A 24  ? 0.419641 0.483898 0.330386 -0.00775664 -0.0773805  -0.0855439  36  ILE   A HG22 
357  H HG23 . ILE   A 24  ? 0.413172 0.477186 0.349377 -0.0190794  -0.0782562  -0.0918055  36  ILE   A HG23 
358  H HD11 . ILE   A 24  ? 0.438678 0.420135 0.354084 -0.0155954  -0.0514504  -0.0960779  36  ILE   A HD11 
359  H HD12 . ILE   A 24  ? 0.440171 0.428094 0.335122 -0.00134489 -0.0482875  -0.0923313  36  ILE   A HD12 
360  H HD13 . ILE   A 24  ? 0.450316 0.456825 0.349081 -0.00948595 -0.0595929  -0.104621   36  ILE   A HD13 
361  N N    . VAL   A 25  ? 0.397537 0.478291 0.343984 -0.00136308 -0.0825079  -0.0600983  37  VAL   A N    
362  C CA   . VAL   A 25  ? 0.406757 0.515059 0.371785 -0.00172436 -0.090756   -0.0655459  37  VAL   A CA   
363  C C    . VAL   A 25  ? 0.426614 0.548305 0.398045 -0.0160541  -0.0939913  -0.0853477  37  VAL   A C    
364  O O    . VAL   A 25  ? 0.398343 0.525522 0.3539   -0.0167209  -0.0992429  -0.0939328  37  VAL   A O    
365  C CB   . VAL   A 25  ? 0.416843 0.545933 0.37443  0.012988    -0.102648   -0.0554417  37  VAL   A CB   
366  C CG1  . VAL   A 25  ? 0.437942 0.606054 0.414309 0.01525     -0.11347    -0.0633997  37  VAL   A CG1  
367  C CG2  . VAL   A 25  ? 0.411172 0.518786 0.363849 0.0248036   -0.100051   -0.0366487  37  VAL   A CG2  
368  H H    . VAL   A 25  ? 0.402298 0.484935 0.334429 0.00374108  -0.0849916  -0.0550604  37  VAL   A H    
369  H HA   . VAL   A 25  ? 0.396355 0.501223 0.374484 -0.00232218 -0.0865034  -0.0629811  37  VAL   A HA   
370  H HB   . VAL   A 25  ? 0.429743 0.561784 0.371392 0.0136798   -0.105652   -0.0558136  37  VAL   A HB   
371  H HG11 . VAL   A 25  ? 0.422609 0.593175 0.416207 0.0112629   -0.109325   -0.066815   37  VAL   A HG11 
372  H HG12 . VAL   A 25  ? 0.439977 0.623629 0.414818 0.00813116  -0.117865   -0.0745174  37  VAL   A HG12 
373  H HG13 . VAL   A 25  ? 0.43856  0.615191 0.411042 0.0279535   -0.120298   -0.0540449  37  VAL   A HG13 
374  H HG21 . VAL   A 25  ? 0.422605 0.539135 0.369784 0.0345236   -0.108009   -0.0290591  37  VAL   A HG21 
375  H HG22 . VAL   A 25  ? 0.411439 0.500369 0.352062 0.0223832   -0.0943092  -0.0315004  37  VAL   A HG22 
376  H HG23 . VAL   A 25  ? 0.401922 0.506071 0.368621 0.0249753   -0.0964109  -0.037629   37  VAL   A HG23 
377  N N    . LYS   A 26  ? 0.405868 0.533483 0.399677 -0.0286345  -0.0907921  -0.0929011  38  LYS   A N    
378  C CA   . LYS   A 26  ? 0.437158 0.572203 0.438984 -0.0472409  -0.0936     -0.111555   38  LYS   A CA   
379  C C    . LYS   A 26  ? 0.452352 0.636264 0.472308 -0.0510455  -0.10556    -0.120055   38  LYS   A C    
380  O O    . LYS   A 26  ? 0.473676 0.671548 0.494996 -0.0648391  -0.112762   -0.137485   38  LYS   A O    
381  C CB   . LYS   A 26  ? 0.449925 0.558759 0.463332 -0.0631945  -0.0818749  -0.112808   38  LYS   A CB   
382  C CG   . LYS   A 26  ? 0.470986 0.535189 0.46661  -0.0583937  -0.0714458  -0.106066   38  LYS   A CG   
383  C CD   . LYS   A 26  ? 0.519215 0.564689 0.491758 -0.0549497  -0.073948   -0.116547   38  LYS   A CD   
384  C CE   . LYS   A 26  ? 0.558996 0.590237 0.532931 -0.071802   -0.0762438  -0.135685   38  LYS   A CE   
385  N NZ   . LYS   A 26  ? 0.625989 0.637925 0.575767 -0.0638768  -0.0776629  -0.147436   38  LYS   A NZ   
386  H H    . LYS   A 26  ? 0.402286 0.529206 0.406318 -0.0265342  -0.0865785  -0.0862722  38  LYS   A H    
387  H HA   . LYS   A 26  ? 0.451646 0.577199 0.438026 -0.0473458  -0.0957974  -0.118452   38  LYS   A HA   
388  H HB2  . LYS   A 26  ? 0.43893  0.559635 0.466517 -0.0628153  -0.0787749  -0.106018   38  LYS   A HB2  
389  H HB3  . LYS   A 26  ? 0.466401 0.577665 0.485447 -0.0775729  -0.0843553  -0.124873   38  LYS   A HB3  
390  H HG2  . LYS   A 26  ? 0.457502 0.520692 0.449655 -0.0469642  -0.0687744  -0.0943507  38  LYS   A HG2  
391  H HG3  . LYS   A 26  ? 0.475262 0.524118 0.47809  -0.0681724  -0.0648856  -0.105639   38  LYS   A HG3  
392  H HD2  . LYS   A 26  ? 0.51419  0.578723 0.479126 -0.0472067  -0.0807662  -0.117275   38  LYS   A HD2  
393  H HD3  . LYS   A 26  ? 0.512185 0.536394 0.47494  -0.0480199  -0.0672746  -0.109676   38  LYS   A HD3  
394  H HE2  . LYS   A 26  ? 0.570525 0.5812   0.551501 -0.0803526  -0.0696414  -0.133076   38  LYS   A HE2  
395  H HE3  . LYS   A 26  ? 0.570674 0.626446 0.554182 -0.0798678  -0.083628   -0.143813   38  LYS   A HE3  
396  H HZ1  . LYS   A 26  ? 0.607426 0.599475 0.549609 -0.0561893  -0.0708246  -0.140304   38  LYS   A HZ1  
397  H HZ2  . LYS   A 26  ? 0.607818 0.640715 0.549778 -0.0562945  -0.0832588  -0.148598   38  LYS   A HZ2  
398  H HZ3  . LYS   A 26  ? 0.633198 0.633106 0.582859 -0.0739043  -0.0798889  -0.161133   38  LYS   A HZ3  
399  N N    . ARG   A 27  ? 0.434413 0.644727 0.469733 -0.0394283  -0.107573   -0.109826   39  ARG   A N    
400  C CA   . ARG   A 27  ? 0.426409 0.689963 0.477907 -0.035624   -0.120371   -0.11544    39  ARG   A CA   
401  C C    . ARG   A 27  ? 0.419643 0.692294 0.465732 -0.00769903 -0.125954   -0.0989565  39  ARG   A C    
402  O O    . ARG   A 27  ? 0.385543 0.63891  0.434819 0.00245554  -0.11795    -0.0872369  39  ARG   A O    
403  C CB   . ARG   A 27  ? 0.436311 0.731662 0.520175 -0.0509881  -0.117049   -0.122438   39  ARG   A CB   
404  C CG   . ARG   A 27  ? 0.462428 0.822795 0.56599  -0.0461994  -0.131041   -0.129618   39  ARG   A CG   
405  C CD   . ARG   A 27  ? 0.474298 0.868556 0.605522 -0.03825    -0.126456   -0.124034   39  ARG   A CD   
406  N NE   . ARG   A 27  ? 0.476924 0.887347 0.632306 -0.0672114  -0.117469   -0.132731   39  ARG   A NE   
407  C CZ   . ARG   A 27  ? 0.437084 0.872625 0.615685 -0.0688077  -0.108113   -0.128956   39  ARG   A CZ   
408  N NH1  . ARG   A 27  ? 0.437714 0.87163  0.61602  -0.0421447  -0.103997   -0.117963   39  ARG   A NH1  
409  N NH2  . ARG   A 27  ? 0.443694 0.902712 0.644234 -0.0991479  -0.101998   -0.136461   39  ARG   A NH2  
410  H H    . ARG   A 27  ? 0.421447 0.617099 0.457313 -0.032674   -0.101004   -0.099803   39  ARG   A H    
411  H HA   . ARG   A 27  ? 0.444004 0.719137 0.488186 -0.0402816  -0.128195   -0.125078   39  ARG   A HA   
412  H HB2  . ARG   A 27  ? 0.445819 0.729543 0.532245 -0.0705235  -0.113213   -0.131196   39  ARG   A HB2  
413  H HB3  . ARG   A 27  ? 0.426216 0.712787 0.515918 -0.0450902  -0.109227   -0.113529   39  ARG   A HB3  
414  H HG2  . ARG   A 27  ? 0.466202 0.833025 0.557268 -0.0296421  -0.139643   -0.125243   39  ARG   A HG2  
415  H HG3  . ARG   A 27  ? 0.473198 0.85024  0.58408  -0.064352   -0.1349     -0.142765   39  ARG   A HG3  
416  H HD2  . ARG   A 27  ? 0.459221 0.827343 0.583005 -0.025327   -0.119917   -0.113292   39  ARG   A HD2  
417  H HD3  . ARG   A 27  ? 0.470468 0.903539 0.610242 -0.0258188  -0.136264   -0.125139   39  ARG   A HD3  
418  H HE   . ARG   A 27  ? 0.479096 0.882024 0.632926 -0.0857884  -0.118054   -0.140996   39  ARG   A HE   
419  H HH11 . ARG   A 27  ? 0.431115 0.827164 0.592147 -0.0318692  -0.100874   -0.110447   39  ARG   A HH11 
420  H HH12 . ARG   A 27  ? 0.429227 0.900456 0.624741 -0.0347409  -0.104529   -0.119015   39  ARG   A HH12 
421  H HH21 . ARG   A 27  ? 0.455041 0.928285 0.66086  -0.11562    -0.107718   -0.146141   39  ARG   A HH21 
422  H HH22 . ARG   A 27  ? 0.43764  0.898278 0.647112 -0.10379    -0.0922017  -0.131633   39  ARG   A HH22 
423  N N    . VAL   A 28  ? 0.400305 0.700696 0.436843 0.00511518  -0.140345   -0.0980168  40  VAL   A N    
424  C CA   . VAL   A 28  ? 0.425193 0.727074 0.453269 0.032278    -0.147065   -0.0801386  40  VAL   A CA   
425  C C    . VAL   A 28  ? 0.429254 0.767939 0.485902 0.0439788   -0.150425   -0.0806865  40  VAL   A C    
426  O O    . VAL   A 28  ? 0.3994   0.786028 0.479308 0.0336564   -0.155141   -0.0949504  40  VAL   A O    
427  C CB   . VAL   A 28  ? 0.468534 0.788399 0.474231 0.0438564   -0.161486   -0.0753203  40  VAL   A CB   
428  C CG1  . VAL   A 28  ? 0.48959  0.804961 0.485719 0.0721396   -0.169116   -0.0535539  40  VAL   A CG1  
429  C CG2  . VAL   A 28  ? 0.491326 0.781377 0.468132 0.0343774   -0.156962   -0.0757825  40  VAL   A CG2  
430  H H    . VAL   A 28  ? 0.422637 0.74003  0.456902 -0.00310619 -0.146469   -0.108492   40  VAL   A H    
431  H HA   . VAL   A 28  ? 0.42401  0.690671 0.441718 0.0362031   -0.139615   -0.0701702  40  VAL   A HA   
432  H HB   . VAL   A 28  ? 0.473009 0.830652 0.489098 0.0393362   -0.169607   -0.0867185  40  VAL   A HB   
433  H HG11 . VAL   A 28  ? 0.482265 0.764753 0.476522 0.0755746   -0.161134   -0.044895   40  VAL   A HG11 
434  H HG12 . VAL   A 28  ? 0.489685 0.836501 0.501484 0.0817306   -0.176366   -0.0557237  40  VAL   A HG12 
435  H HG13 . VAL   A 28  ? 0.502245 0.81639  0.477954 0.0773723   -0.174971   -0.0461019  40  VAL   A HG13 
436  H HG21 . VAL   A 28  ? 0.501332 0.807577 0.463522 0.0414674   -0.165865   -0.0727322  40  VAL   A HG21 
437  H HG22 . VAL   A 28  ? 0.483435 0.772844 0.465216 0.0182749   -0.153134   -0.0904534  40  VAL   A HG22 
438  H HG23 . VAL   A 28  ? 0.482137 0.73906  0.449838 0.0376685   -0.149096   -0.0646689  40  VAL   A HG23 
439  N N    . GLY   A 29  ? 0.449726 0.767059 0.504969 0.0650301   -0.147854   -0.0665435  41  GLY   A N    
440  C CA   . GLY   A 29  ? 0.482426 0.832563 0.562145 0.0826373   -0.150763   -0.0675716  41  GLY   A CA   
441  C C    . GLY   A 29  ? 0.582088 0.952397 0.655159 0.112645    -0.167621   -0.0572479  41  GLY   A C    
442  O O    . GLY   A 29  ? 0.603446 0.97688  0.656708 0.114553    -0.177935   -0.051659   41  GLY   A O    
443  H H    . GLY   A 29  ? 0.4559   0.737394 0.494243 0.0687674   -0.14425    -0.0568272  41  GLY   A H    
444  H HA2  . GLY   A 29  ? 0.479894 0.865622 0.579787 0.0710343   -0.149912   -0.0792903  41  GLY   A HA2  
445  H HA3  . GLY   A 29  ? 0.482624 0.807367 0.56308  0.0870746   -0.142529   -0.0633981  41  GLY   A HA3  
446  N N    . ASN   A 30  ? 0.669433 1.05221  0.75663  0.138404    -0.17069    -0.0540044  42  ASN   A N    
447  C CA   . ASN   A 30  ? 0.724893 1.11459  0.802186 0.171447    -0.186897   -0.0407689  42  ASN   A CA   
448  C C    . ASN   A 30  ? 0.798673 1.14209  0.870211 0.196949    -0.184113   -0.0300744  42  ASN   A C    
449  O O    . ASN   A 30  ? 0.754335 1.09423  0.842503 0.195553    -0.172735   -0.0395736  42  ASN   A O    
450  C CB   . ASN   A 30  ? 0.720388 1.18808  0.82288  0.185115    -0.20035    -0.0503484  42  ASN   A CB   
451  C CG   . ASN   A 30  ? 0.715092 1.23192  0.85445  0.170519    -0.191041   -0.0699225  42  ASN   A CG   
452  O OD1  . ASN   A 30  ? 0.732024 1.24106  0.884543 0.181708    -0.181877   -0.072062   42  ASN   A OD1  
453  N ND2  . ASN   A 30  ? 0.703675 1.27188  0.859052 0.144646    -0.193299   -0.0845406  42  ASN   A ND2  
454  H H    . ASN   A 30  ? 0.642758 1.02906  0.744812 0.136697    -0.162762   -0.0598037  42  ASN   A H    
455  H HA   . ASN   A 30  ? 0.738631 1.1109   0.79426  0.169211    -0.191738   -0.0316401  42  ASN   A HA   
456  H HB2  . ASN   A 30  ? 0.747109 1.21507  0.847804 0.21264     -0.208495   -0.0419136  42  ASN   A HB2  
457  H HB3  . ASN   A 30  ? 0.730773 1.21948  0.826758 0.176679    -0.207799   -0.0517588  42  ASN   A HB3  
458  H HD21 . ASN   A 30  ? 0.688179 1.25971  0.854526 0.122952    -0.183782   -0.0932526  42  ASN   A HD21 
459  H HD22 . ASN   A 30  ? 0.712871 1.31129  0.867415 0.14857     -0.204663   -0.0855697  42  ASN   A HD22 
460  N N    . GLY   A 31  ? 0.880268 1.18861  0.927233 0.220076    -0.195053   -0.01048    43  GLY   A N    
461  C CA   . GLY   A 31  ? 0.94543  1.21382  0.988628 0.249716    -0.19716    -0.00213538 43  GLY   A CA   
462  C C    . GLY   A 31  ? 1.03646  1.24409  1.04439  0.26213     -0.205699   0.0237256   43  GLY   A C    
463  O O    . GLY   A 31  ? 1.09937  1.29513  1.10145  0.295255    -0.218442   0.0353028   43  GLY   A O    
464  H H    . GLY   A 31  ? 0.886421 1.19448  0.917803 0.217196    -0.201425   -0.00218532 43  GLY   A H    
465  H HA2  . GLY   A 31  ? 0.954956 1.25874  1.01425  0.270563    -0.204206   -0.0072634  43  GLY   A HA2  
466  H HA3  . GLY   A 31  ? 0.932678 1.17911  0.980773 0.241334    -0.185915   -0.00883541 43  GLY   A HA3  
467  N N    . GLU   A 32  ? 1.09034  1.25996  1.07492  0.235671    -0.198323   0.0333894   44  GLU   A N    
468  C CA   . GLU   A 32  ? 1.14026  1.24168  1.09309  0.238732    -0.200277   0.0574404   44  GLU   A CA   
469  C C    . GLU   A 32  ? 1.10953  1.15739  1.06537  0.250095    -0.194918   0.0551776   44  GLU   A C    
470  O O    . GLU   A 32  ? 1.20017  1.18883  1.1344   0.261472    -0.200331   0.0736928   44  GLU   A O    
471  C CB   . GLU   A 32  ? 1.09328  1.1959   1.0246   0.260795    -0.217934   0.0808996   44  GLU   A CB   
472  H H    . GLU   A 32  ? 1.04554  1.23308  1.0344   0.214618    -0.191757   0.0247243   44  GLU   A H    
473  H HA   . GLU   A 32  ? 1.08708  1.17621  1.02912  0.216008    -0.192654   0.0596476   44  GLU   A HA   
476  N N    . GLU   A 33  ? 0.933786 1.00283  0.91562  0.246007    -0.184411   0.0320205   45  GLU   A N    
477  C CA   . GLU   A 33  ? 0.849223 0.874278 0.833781 0.252668    -0.177309   0.0245882   45  GLU   A CA   
478  C C    . GLU   A 33  ? 0.724014 0.765105 0.723115 0.224445    -0.159834   0.00669143  45  GLU   A C    
479  O O    . GLU   A 33  ? 0.648699 0.746836 0.671836 0.218929    -0.15501    -0.00908307 45  GLU   A O    
480  C CB   . GLU   A 33  ? 0.835197 0.873533 0.835779 0.291272    -0.185731   0.0154053   45  GLU   A CB   
481  H H    . GLU   A 33  ? 0.914514 1.02732  0.912055 0.237603    -0.181443   0.0203389   45  GLU   A H    
482  H HA   . GLU   A 33  ? 0.86911  0.843893 0.833622 0.24978     -0.178445   0.0378044   45  GLU   A HA   
485  N N    . THR   A 34  ? 0.699451 0.690383 0.683452 0.205944    -0.150838   0.0106086   46  THR   A N    
486  C CA   . THR   A 34  ? 0.637978 0.636429 0.632673 0.183944    -0.135169   -0.00421886 46  THR   A CA   
487  C C    . THR   A 34  ? 0.685767 0.669198 0.689631 0.200711    -0.131818   -0.0182512  46  THR   A C    
488  O O    . THR   A 34  ? 0.747639 0.699233 0.744444 0.226094    -0.141463   -0.0149396  46  THR   A O    
489  C CB   . THR   A 34  ? 0.600584 0.561504 0.574666 0.157109    -0.128333   0.00683128  46  THR   A CB   
490  O OG1  . THR   A 34  ? 0.591384 0.493504 0.547615 0.165336    -0.133348   0.017379    46  THR   A OG1  
491  C CG2  . THR   A 34  ? 0.605028 0.582561 0.567532 0.144415    -0.131907   0.0191959   46  THR   A CG2  
492  H H    . THR   A 34  ? 0.725761 0.677862 0.692072 0.20668     -0.154795   0.0236709   46  THR   A H    
493  H HA   . THR   A 34  ? 0.615695 0.655889 0.624532 0.1767      -0.13183    -0.0121891  46  THR   A HA   
494  H HB   . THR   A 34  ? 0.572895 0.539583 0.553364 0.143592    -0.118426   -0.00210547 46  THR   A HB   
496  H HG21 . THR   A 34  ? 0.592596 0.555731 0.545731 0.127023    -0.125457   0.0228837   46  THR   A HG21 
497  H HG22 . THR   A 34  ? 0.629189 0.594131 0.580432 0.155638    -0.141177   0.0314549   46  THR   A HG22 
498  H HG23 . THR   A 34  ? 0.582144 0.598496 0.557354 0.142649    -0.131517   0.0108628   46  THR   A HG23 
499  N N    . PRO   A 35  ? 0.689842 0.692402 0.707108 0.188411    -0.118458   -0.0340883  47  PRO   A N    
500  C CA   . PRO   A 35  ? 0.695532 0.679336 0.715614 0.202442    -0.114643   -0.0479421  47  PRO   A CA   
501  C C    . PRO   A 35  ? 0.748411 0.662399 0.744807 0.195931    -0.115739   -0.0413624  47  PRO   A C    
502  O O    . PRO   A 35  ? 0.816568 0.708659 0.798756 0.17123     -0.112778   -0.0288696  47  PRO   A O    
503  C CB   . PRO   A 35  ? 0.630259 0.656114 0.666779 0.185749    -0.0995578  -0.0620321  47  PRO   A CB   
504  C CG   . PRO   A 35  ? 0.590594 0.629109 0.624572 0.156131    -0.0944813  -0.0522337  47  PRO   A CG   
505  C CD   . PRO   A 35  ? 0.61503  0.653905 0.642414 0.161181    -0.106857   -0.0388386  47  PRO   A CD   
506  H HA   . PRO   A 35  ? 0.715826 0.709788 0.743204 0.226063    -0.120972   -0.0528632  47  PRO   A HA   
507  H HB2  . PRO   A 35  ? 0.637253 0.642288 0.668128 0.182738    -0.0942566  -0.0678351  47  PRO   A HB2  
508  H HB3  . PRO   A 35  ? 0.627933 0.693329 0.681162 0.197069    -0.0988884  -0.0709614  47  PRO   A HB3  
509  H HG2  . PRO   A 35  ? 0.592353 0.602867 0.614168 0.142356    -0.0901283  -0.0481782  47  PRO   A HG2  
510  H HG3  . PRO   A 35  ? 0.572628 0.647965 0.620707 0.148233    -0.0879558  -0.0587813  47  PRO   A HG3  
511  H HD2  . PRO   A 35  ? 0.611057 0.632964 0.626153 0.145721    -0.105845   -0.029883   47  PRO   A HD2  
512  H HD3  . PRO   A 35  ? 0.607132 0.686188 0.648399 0.163219    -0.108508   -0.0426781  47  PRO   A HD3  
513  N N    . MET   A 36  ? 0.786205 0.66758  0.779147 0.218408    -0.120198   -0.0513831  48  MET   A N    
514  C CA   . MET   A 36  ? 0.803591 0.616315 0.77536  0.211486    -0.122392   -0.0485328  48  MET   A CA   
515  C C    . MET   A 36  ? 0.752975 0.567947 0.728353 0.204311    -0.11166    -0.0695347  48  MET   A C    
516  O O    . MET   A 36  ? 0.701804 0.564639 0.694675 0.215122    -0.104675   -0.0867102  48  MET   A O    
517  C CB   . MET   A 36  ? 0.903159 0.6644   0.863923 0.241592    -0.136913   -0.0455997  48  MET   A CB   
518  C CG   . MET   A 36  ? 0.924121 0.681535 0.87805  0.252695    -0.149222   -0.0225734  48  MET   A CG   
519  S SD   . MET   A 36  ? 0.977386 0.638267 0.89928  0.251027    -0.161407   -0.00022359 48  MET   A SD   
520  C CE   . MET   A 36  ? 0.94799  0.602961 0.854336 0.204971    -0.154436   0.0229319   48  MET   A CE   
521  H H    . MET   A 36  ? 0.787162 0.690174 0.791464 0.238581    -0.12221    -0.0611396  48  MET   A H    
522  H HA   . MET   A 36  ? 0.799404 0.597246 0.760589 0.191289    -0.121637   -0.0347746  48  MET   A HA   
523  H HB2  . MET   A 36  ? 0.902091 0.679416 0.873478 0.263312    -0.137281   -0.0610615  48  MET   A HB2  
524  H HB3  . MET   A 36  ? 0.921321 0.634197 0.867901 0.233389    -0.138241   -0.0441943  48  MET   A HB3  
525  H HG2  . MET   A 36  ? 0.887505 0.673267 0.843386 0.235438    -0.145602   -0.0138205  48  MET   A HG2  
526  H HG3  . MET   A 36  ? 0.928273 0.708419 0.892609 0.277821    -0.154454   -0.0280997  48  MET   A HG3  
527  H HE1  . MET   A 36  ? 0.985618 0.590151 0.875828 0.197072    -0.158257   0.0333736   48  MET   A HE1  
528  H HE2  . MET   A 36  ? 0.9116   0.589983 0.82575  0.188181    -0.144392   0.0124226   48  MET   A HE2  
529  H HE3  . MET   A 36  ? 0.936502 0.617032 0.842527 0.205217    -0.156988   0.0352837   48  MET   A HE3  
530  N N    . ILE   A 37  ? 0.770515 0.536281 0.728753 0.18588     -0.110836   -0.0678328  49  ILE   A N    
531  C CA   . ILE   A 37  ? 0.75093  0.519536 0.709453 0.176956    -0.101825   -0.0871962  49  ILE   A CA   
532  C C    . ILE   A 37  ? 0.750525 0.526347 0.716829 0.208782    -0.103275   -0.111753   49  ILE   A C    
533  O O    . ILE   A 37  ? 0.802525 0.53949  0.763071 0.234441    -0.114595   -0.11477    49  ILE   A O    
534  C CB   . ILE   A 37  ? 0.807312 0.519128 0.746164 0.15456     -0.104085   -0.0832603  49  ILE   A CB   
535  C CG1  . ILE   A 37  ? 0.799656 0.514494 0.732114 0.123805    -0.10085    -0.0605198  49  ILE   A CG1  
536  C CG2  . ILE   A 37  ? 0.797147 0.514399 0.735389 0.1495      -0.0969768  -0.106884   49  ILE   A CG2  
537  C CD1  . ILE   A 37  ? 0.82256  0.492923 0.738869 0.0986063   -0.102216   -0.0561098  49  ILE   A CD1  
538  H H    . ILE   A 37  ? 0.788692 0.520704 0.73464  0.17829     -0.116218   -0.0542131  49  ILE   A H    
539  H HA   . ILE   A 37  ? 0.713615 0.521067 0.680359 0.164538    -0.0930249  -0.0874857  49  ILE   A HA   
540  H HB   . ILE   A 37  ? 0.84623  0.514924 0.776008 0.164834    -0.113205   -0.0807654  49  ILE   A HB   
541  H HG12 . ILE   A 37  ? 0.755397 0.510236 0.69653  0.115694    -0.0925312  -0.0621776  49  ILE   A HG12 
542  H HG13 . ILE   A 37  ? 0.800818 0.510881 0.731349 0.128311    -0.106098   -0.0465319  49  ILE   A HG13 
543  H HG21 . ILE   A 37  ? 0.812921 0.501207 0.740393 0.132114    -0.0982183  -0.104428   49  ILE   A HG21 
544  H HG22 . ILE   A 37  ? 0.760589 0.52172  0.707996 0.143505    -0.0880892  -0.109526   49  ILE   A HG22 
545  H HG23 . ILE   A 37  ? 0.826011 0.533167 0.764947 0.169825    -0.1003     -0.121919   49  ILE   A HG23 
546  H HD11 . ILE   A 37  ? 0.865786 0.494604 0.774265 0.106523    -0.109421   -0.0608766  49  ILE   A HD11 
547  H HD12 . ILE   A 37  ? 0.81797  0.484426 0.728899 0.0846617   -0.10282    -0.0388649  49  ILE   A HD12 
548  H HD13 . ILE   A 37  ? 0.802854 0.491458 0.721804 0.0881571   -0.095452   -0.0658349  49  ILE   A HD13 
549  N N    . GLY   A 38  ? 0.704926 0.530942 0.683063 0.207843    -0.0914846  -0.128828   50  GLY   A N    
550  C CA   . GLY   A 38  ? 0.71029  0.558371 0.696899 0.236988    -0.0898138  -0.154101   50  GLY   A CA   
551  C C    . GLY   A 38  ? 0.666614 0.584104 0.677137 0.255046    -0.0861583  -0.155623   50  GLY   A C    
552  O O    . GLY   A 38  ? 0.67365  0.631356 0.69533  0.275044    -0.0805561  -0.176003   50  GLY   A O    
553  H H    . GLY   A 38  ? 0.672967 0.521574 0.653332 0.18859     -0.0838842  -0.124118   50  GLY   A H    
554  H HA2  . GLY   A 38  ? 0.70017  0.560437 0.68477  0.228404    -0.0823427  -0.165386   50  GLY   A HA2  
555  H HA3  . GLY   A 38  ? 0.753241 0.55951  0.73139  0.253938    -0.0986513  -0.160213   50  GLY   A HA3  
556  N N    . ASP   A 39  ? 0.638087 0.573699 0.656531 0.247391    -0.0893404  -0.13536    51  ASP   A N    
557  C CA   . ASP   A 39  ? 0.604921 0.607652 0.647323 0.262045    -0.0879372  -0.136822   51  ASP   A CA   
558  C C    . ASP   A 39  ? 0.567884 0.636875 0.62625  0.246121    -0.0716014  -0.145117   51  ASP   A C    
559  O O    . ASP   A 39  ? 0.539777 0.603078 0.590209 0.217827    -0.0626721  -0.139954   51  ASP   A O    
560  C CB   . ASP   A 39  ? 0.604633 0.613202 0.649841 0.253044    -0.095294   -0.114981   51  ASP   A CB   
561  C CG   . ASP   A 39  ? 0.657531 0.621741 0.692016 0.277054    -0.112278   -0.104662   51  ASP   A CG   
562  O OD1  . ASP   A 39  ? 0.689071 0.612144 0.714815 0.3033      -0.119232   -0.114917   51  ASP   A OD1  
563  O OD2  . ASP   A 39  ? 0.665517 0.635297 0.698946 0.270164    -0.118892   -0.0864531  51  ASP   A OD2  
564  H H    . ASP   A 39  ? 0.635477 0.543896 0.644386 0.232187    -0.092514   -0.121104   51  ASP   A H    
565  H HA   . ASP   A 39  ? 0.638276 0.642113 0.684691 0.289411    -0.0931801  -0.147331   51  ASP   A HA   
566  H HB2  . ASP   A 39  ? 0.585677 0.579639 0.62248  0.228679    -0.0919901  -0.104657   51  ASP   A HB2  
567  H HB3  . ASP   A 39  ? 0.581062 0.641475 0.643595 0.254393    -0.092114   -0.116913   51  ASP   A HB3  
568  N N    . LYS   A 40  ? 0.552909 0.687373 0.63394  0.263947    -0.0676229  -0.156323   52  LYS   A N    
569  C CA   . LYS   A 40  ? 0.53474  0.736248 0.632292 0.244497    -0.0520637  -0.15863    52  LYS   A CA   
570  C C    . LYS   A 40  ? 0.502676 0.732033 0.612633 0.221169    -0.05235    -0.140992   52  LYS   A C    
571  O O    . LYS   A 40  ? 0.510194 0.762268 0.633311 0.235622    -0.061742   -0.138505   52  LYS   A O    
572  C CB   . LYS   A 40  ? 0.576361 0.843092 0.69389  0.270882    -0.0463445  -0.178409   52  LYS   A CB   
573  C CG   . LYS   A 40  ? 0.568944 0.907206 0.702434 0.249783    -0.0288466  -0.179671   52  LYS   A CG   
574  C CD   . LYS   A 40  ? 0.621487 1.03595  0.778418 0.276516    -0.0237537  -0.197394   52  LYS   A CD   
575  C CE   . LYS   A 40  ? 0.625117 1.10667  0.792599 0.258038    -0.00464673 -0.200408   52  LYS   A CE   
576  N NZ   . LYS   A 40  ? 0.640194 1.20938  0.835268 0.2794      0.00091912  -0.214209   52  LYS   A NZ   
577  H H    . LYS   A 40  ? 0.580873 0.719346 0.667285 0.288427    -0.0746477  -0.161875   52  LYS   A H    
578  H HA   . LYS   A 40  ? 0.528702 0.715161 0.6154   0.22863     -0.0451128  -0.158729   52  LYS   A HA   
579  H HB2  . LYS   A 40  ? 0.599717 0.844137 0.707512 0.288319    -0.0475382  -0.191605   52  LYS   A HB2  
580  H HB3  . LYS   A 40  ? 0.580319 0.866434 0.709995 0.287062    -0.0535042  -0.178101   52  LYS   A HB3  
581  H HG2  . LYS   A 40  ? 0.549323 0.90095  0.690051 0.228832    -0.0276228  -0.166574   52  LYS   A HG2  
582  H HG3  . LYS   A 40  ? 0.570463 0.893382 0.691281 0.238869    -0.0219041  -0.181596   52  LYS   A HG3  
583  H HD2  . LYS   A 40  ? 0.644227 1.03947  0.79391  0.302912    -0.0282253  -0.211377   52  LYS   A HD2  
584  H HD3  . LYS   A 40  ? 0.611328 1.05238  0.783945 0.282107    -0.0293189  -0.193493   52  LYS   A HD3  
585  H HE2  . LYS   A 40  ? 0.595527 1.0832   0.766049 0.229869    -0.00033699 -0.185797   52  LYS   A HE2  
586  H HE3  . LYS   A 40  ? 0.630128 1.09255  0.782341 0.258588    0.00024521  -0.207203   52  LYS   A HE3  
587  H HZ1  . LYS   A 40  ? 0.626212 1.2199   0.836943 0.275352    -0.00292654 -0.207485   52  LYS   A HZ1  
588  H HZ2  . LYS   A 40  ? 0.660552 1.2232   0.853237 0.308521    -0.00403208 -0.228473   52  LYS   A HZ2  
589  H HZ3  . LYS   A 40  ? 0.627208 1.23473  0.826147 0.267794    0.0131064   -0.215391   52  LYS   A HZ3  
590  N N    . VAL   A 41  ? 0.456099 0.683707 0.561159 0.186972    -0.0429429  -0.130057   53  VAL   A N    
591  C CA   . VAL   A 41  ? 0.431556 0.667998 0.542141 0.163086    -0.0444611  -0.114849   53  VAL   A CA   
592  C C    . VAL   A 41  ? 0.389334 0.682883 0.517783 0.140064    -0.0309997  -0.114063   53  VAL   A C    
593  O O    . VAL   A 41  ? 0.36954  0.673688 0.494914 0.130434    -0.0183323  -0.116759   53  VAL   A O    
594  C CB   . VAL   A 41  ? 0.448908 0.623497 0.535702 0.14432     -0.0472002  -0.101298   53  VAL   A CB   
595  C CG1  . VAL   A 41  ? 0.434767 0.618012 0.524889 0.11978     -0.0471594  -0.0888804  53  VAL   A CG1  
596  C CG2  . VAL   A 41  ? 0.490825 0.611003 0.560963 0.162595    -0.060836   -0.0983152  53  VAL   A CG2  
597  H H    . VAL   A 41  ? 0.457629 0.677893 0.554936 0.179414    -0.0357154  -0.13295    53  VAL   A H    
598  H HA   . VAL   A 41  ? 0.438472 0.684942 0.556421 0.174916    -0.0531584  -0.114057   53  VAL   A HA   
599  H HB   . VAL   A 41  ? 0.444708 0.609208 0.523727 0.135768    -0.03971    -0.102872   53  VAL   A HB   
600  H HG11 . VAL   A 41  ? 0.429342 0.64163  0.532578 0.125041    -0.0516856  -0.0902053  53  VAL   A HG11 
601  H HG12 . VAL   A 41  ? 0.416581 0.612731 0.509279 0.103314    -0.037907   -0.0876709  53  VAL   A HG12 
602  H HG13 . VAL   A 41  ? 0.434462 0.582024 0.510579 0.115388    -0.0520646  -0.0811576  53  VAL   A HG13 
603  H HG21 . VAL   A 41  ? 0.484876 0.572317 0.541281 0.148954    -0.0615369  -0.0894179  53  VAL   A HG21 
604  H HG22 . VAL   A 41  ? 0.505344 0.613634 0.57178  0.177253    -0.0611156  -0.107651   53  VAL   A HG22 
605  H HG23 . VAL   A 41  ? 0.493783 0.624281 0.570228 0.173175    -0.0687392  -0.0957874  53  VAL   A HG23 
606  N N    . TYR   A 42  ? 0.332728 0.663231 0.479006 0.130215    -0.0344074  -0.109784   54  TYR   A N    
607  C CA   . TYR   A 42  ? 0.319815 0.702732 0.484999 0.104772    -0.0234168  -0.107875   54  TYR   A CA   
608  C C    . TYR   A 42  ? 0.311987 0.672261 0.472074 0.0758523   -0.0258907  -0.0959853  54  TYR   A C    
609  O O    . TYR   A 42  ? 0.286447 0.640237 0.44706  0.0796836   -0.0385007  -0.0942191  54  TYR   A O    
610  C CB   . TYR   A 42  ? 0.33953  0.797471 0.534942 0.11668     -0.0254051  -0.117338   54  TYR   A CB   
611  C CG   . TYR   A 42  ? 0.366823 0.857729 0.570674 0.150612    -0.0235311  -0.13239    54  TYR   A CG   
612  C CD1  . TYR   A 42  ? 0.401226 0.860293 0.595438 0.186811    -0.0361929  -0.139361   54  TYR   A CD1  
613  C CD2  . TYR   A 42  ? 0.3682   0.920229 0.587936 0.146917    -0.00883096 -0.139559   54  TYR   A CD2  
614  C CE1  . TYR   A 42  ? 0.433802 0.917252 0.634032 0.220659    -0.0350872  -0.155771   54  TYR   A CE1  
615  C CE2  . TYR   A 42  ? 0.416631 1.00192  0.643046 0.180342    -0.00663073 -0.156103   54  TYR   A CE2  
616  C CZ   . TYR   A 42  ? 0.441724 0.990547 0.658253 0.218506    -0.0201316  -0.165652   54  TYR   A CZ   
617  O OH   . TYR   A 42  ? 0.486819 1.06507  0.7091   0.254171    -0.0184278  -0.184597   54  TYR   A OH   
618  H H    . TYR   A 42  ? 0.350885 0.672938 0.496958 0.138803    -0.0444324  -0.107747   54  TYR   A H    
619  H HA   . TYR   A 42  ? 0.320108 0.706411 0.481664 0.0978586   -0.0129621  -0.108274   54  TYR   A HA   
620  H HB2  . TYR   A 42  ? 0.340347 0.797037 0.538895 0.122298    -0.0362187  -0.116066   54  TYR   A HB2  
621  H HB3  . TYR   A 42  ? 0.328118 0.819295 0.535857 0.0955171   -0.0175793  -0.114952   54  TYR   A HB3  
622  H HD1  . TYR   A 42  ? 0.407166 0.82563  0.589535 0.188701    -0.0457324  -0.132736   54  TYR   A HD1  
623  H HD2  . TYR   A 42  ? 0.3625   0.934085 0.588    0.121498    -4.614e-05  -0.133059   54  TYR   A HD2  
624  H HE1  . TYR   A 42  ? 0.455197 0.910788 0.647767 0.24542     -0.0443946  -0.160169   54  TYR   A HE1  
625  H HE2  . TYR   A 42  ? 0.406036 1.03747  0.64278  0.177439    0.0041406   -0.160844   54  TYR   A HE2  
627  N N    . VAL   A 43  ? 0.28282  0.633993 0.437698 0.0483911   -0.0141552  -0.0883687  55  VAL   A N    
628  C CA   . VAL   A 43  ? 0.295605 0.620438 0.444079 0.0230991   -0.0161775  -0.0795422  55  VAL   A CA   
629  C C    . VAL   A 43  ? 0.281078 0.633268 0.442107 -0.00695893 -0.00454951 -0.075007   55  VAL   A C    
630  O O    . VAL   A 43  ? 0.27733  0.660876 0.44606  -0.0102867  0.00731349  -0.0745796  55  VAL   A O    
631  C CB   . VAL   A 43  ? 0.296137 0.555381 0.416411 0.0209718   -0.0167295  -0.0713411  55  VAL   A CB   
632  C CG1  . VAL   A 43  ? 0.308705 0.536594 0.415307 0.0456283   -0.027683   -0.0732241  55  VAL   A CG1  
633  C CG2  . VAL   A 43  ? 0.293419 0.540177 0.403127 0.012766    -0.00344832 -0.0660836  55  VAL   A CG2  
634  H H    . VAL   A 43  ? 0.291123 0.651929 0.445471 0.0465473   -0.00511906 -0.0888506  55  VAL   A H    
635  H HA   . VAL   A 43  ? 0.291744 0.624619 0.445951 0.0264724   -0.0253737  -0.0819308  55  VAL   A HA   
636  H HB   . VAL   A 43  ? 0.296074 0.541755 0.413225 0.00742536  -0.0190629  -0.0675634  55  VAL   A HB   
637  H HG11 . VAL   A 43  ? 0.312204 0.546067 0.419549 0.0593501   -0.025768   -0.0781474  55  VAL   A HG11 
638  H HG12 . VAL   A 43  ? 0.310518 0.548731 0.422997 0.0521268   -0.0362755  -0.0750333  55  VAL   A HG12 
639  H HG13 . VAL   A 43  ? 0.307111 0.499071 0.397889 0.0410781   -0.0281876  -0.0675681  55  VAL   A HG13 
640  H HG21 . VAL   A 43  ? 0.294209 0.504539 0.387667 0.0136307   -0.00487321 -0.061913   55  VAL   A HG21 
641  H HG22 . VAL   A 43  ? 0.293105 0.55079  0.40812  -0.00483479 0.00299951  -0.0616035  55  VAL   A HG22 
642  H HG23 . VAL   A 43  ? 0.295725 0.561178 0.409108 0.02451     -0.00025978 -0.0713603  55  VAL   A HG23 
643  N N    . HIS   A 44  ? 0.292975 0.631957 0.454668 -0.0292149  -0.00832849 -0.0717445  56  HIS   A N    
644  C CA   . HIS   A 44  ? 0.319199 0.646899 0.479787 -0.0599653  0.00177336  -0.0632292  56  HIS   A CA   
645  C C    . HIS   A 44  ? 0.315984 0.577129 0.450335 -0.0631251  -0.00078171 -0.0566965  56  HIS   A C    
646  O O    . HIS   A 44  ? 0.32234  0.560074 0.446284 -0.050588   -0.0116666  -0.0603079  56  HIS   A O    
647  C CB   . HIS   A 44  ? 0.356026 0.722085 0.539727 -0.0855465  6.268e-05   -0.0671738  56  HIS   A CB   
648  C CG   . HIS   A 44  ? 0.392379 0.827731 0.602557 -0.0933757  0.00891203  -0.0688282  56  HIS   A CG   
649  N ND1  . HIS   A 44  ? 0.432588 0.878398 0.642143 -0.105534   0.0248605   -0.058667   56  HIS   A ND1  
650  C CD2  . HIS   A 44  ? 0.40662  0.909143 0.64425  -0.0898983  0.00443815  -0.0787929  56  HIS   A CD2  
651  C CE1  . HIS   A 44  ? 0.434135 0.953042 0.670334 -0.110969   0.0308825   -0.0625083  56  HIS   A CE1  
652  N NE2  . HIS   A 44  ? 0.428211 0.983768 0.683109 -0.101083   0.0184151   -0.0754603  56  HIS   A NE2  
653  H H    . HIS   A 44  ? 0.29527  0.630585 0.457077 -0.0246429  -0.0178677  -0.0750929  56  HIS   A H    
654  H HA   . HIS   A 44  ? 0.31964  0.657706 0.48024  -0.061271   0.0115535   -0.0589577  56  HIS   A HA   
655  H HB2  . HIS   A 44  ? 0.355234 0.727786 0.542782 -0.0788824  -0.0105652  -0.0742203  56  HIS   A HB2  
656  H HB3  . HIS   A 44  ? 0.36703  0.705522 0.543919 -0.104928   0.00295212  -0.0619359  56  HIS   A HB3  
658  H HD2  . HIS   A 44  ? 0.404154 0.919109 0.648206 -0.0813148  -0.0062717  -0.0862391  56  HIS   A HD2  
659  H HE1  . HIS   A 44  ? 0.437671 0.981054 0.678348 -0.119672   0.0420768   -0.0566133  56  HIS   A HE1  
661  N N    . TYR   A 45  ? 0.326926 0.560932 0.450103 -0.0783617  0.00961285  -0.0459877  57  TYR   A N    
662  C CA   . TYR   A 45  ? 0.328284 0.504458 0.427345 -0.0779501  0.00835857  -0.0398189  57  TYR   A CA   
663  C C    . TYR   A 45  ? 0.352503 0.505891 0.447065 -0.101974   0.0172009   -0.0292909  57  TYR   A C    
664  O O    . TYR   A 45  ? 0.385082 0.564388 0.49041  -0.116853   0.0270048   -0.0225065  57  TYR   A O    
665  C CB   . TYR   A 45  ? 0.288821 0.445927 0.370619 -0.0569348  0.0102136   -0.0362549  57  TYR   A CB   
666  C CG   . TYR   A 45  ? 0.304775 0.470103 0.382308 -0.0598863  0.0230264   -0.0271276  57  TYR   A CG   
667  C CD1  . TYR   A 45  ? 0.296699 0.506088 0.385477 -0.0522912  0.0286705   -0.0310259  57  TYR   A CD1  
668  C CD2  . TYR   A 45  ? 0.311322 0.443638 0.372971 -0.0692866  0.0294893   -0.0145549  57  TYR   A CD2  
669  C CE1  . TYR   A 45  ? 0.318953 0.541026 0.401611 -0.0554426  0.0406982   -0.022701   57  TYR   A CE1  
670  C CE2  . TYR   A 45  ? 0.342896 0.485297 0.3982   -0.0714532  0.040545    -0.004165   57  TYR   A CE2  
671  C CZ   . TYR   A 45  ? 0.327597 0.516059 0.392805 -0.0656595  0.0464037   -0.00817145 57  TYR   A CZ   
672  O OH   . TYR   A 45  ? 0.395697 0.597278 0.45197  -0.0682181  0.0575384   0.00241305  57  TYR   A OH   
673  H H    . TYR   A 45  ? 0.330102 0.583913 0.460695 -0.0884816  0.01773     -0.0418218  57  TYR   A H    
674  H HA   . TYR   A 45  ? 0.324432 0.489142 0.421085 -0.075992   -0.00012074 -0.0451904  57  TYR   A HA   
675  H HB2  . TYR   A 45  ? 0.299392 0.424263 0.367461 -0.0547288  0.00716424  -0.0340491  57  TYR   A HB2  
676  H HB3  . TYR   A 45  ? 0.290259 0.462362 0.376361 -0.0428119  0.00532477  -0.0425858  57  TYR   A HB3  
677  H HD1  . TYR   A 45  ? 0.296006 0.528754 0.396027 -0.0435828  0.0241641   -0.039684   57  TYR   A HD1  
678  H HD2  . TYR   A 45  ? 0.323901 0.427066 0.377709 -0.0723266  0.0259639   -0.0130588  57  TYR   A HD2  
679  H HE1  . TYR   A 45  ? 0.312611 0.567059 0.402007 -0.0490113  0.0446917   -0.0269664  57  TYR   A HE1  
680  H HE2  . TYR   A 45  ? 0.34562  0.465062 0.389247 -0.0759539  0.044031    0.00553097  57  TYR   A HE2  
682  N N    . LYS   A 46  ? 0.38391  0.488593 0.461483 -0.104376   0.0137068   -0.0274586  58  LYS   A N    
683  C CA   . LYS   A 46  ? 0.426011 0.492149 0.491561 -0.11874    0.0208879   -0.0158151  58  LYS   A CA   
684  C C    . LYS   A 46  ? 0.428001 0.456306 0.470251 -0.0996176  0.019893    -0.011307   58  LYS   A C    
685  O O    . LYS   A 46  ? 0.436162 0.454558 0.471593 -0.0862168  0.0114002   -0.0197819  58  LYS   A O    
686  C CB   . LYS   A 46  ? 0.438128 0.482423 0.507798 -0.1411     0.0166184   -0.0214435  58  LYS   A CB   
687  H H    . LYS   A 46  ? 0.376687 0.471667 0.449287 -0.095353   0.00629669  -0.0336725  58  LYS   A H    
688  H HA   . LYS   A 46  ? 0.425379 0.505997 0.49466  -0.125381   0.0291235   -0.00716094 58  LYS   A HA   
691  N N    . GLY   A 47  ? 0.447012 0.458961 0.477119 -0.0987686  0.0286169   0.0030965   59  GLY   A N    
692  C CA   . GLY   A 47  ? 0.438105 0.426242 0.448819 -0.0802398  0.0281323   0.00782362  59  GLY   A CA   
693  C C    . GLY   A 47  ? 0.49368  0.444134 0.489326 -0.0842299  0.0337661   0.022212    59  GLY   A C    
694  O O    . GLY   A 47  ? 0.551955 0.500517 0.550092 -0.100078   0.0412107   0.0339992   59  GLY   A O    
695  H H    . GLY   A 47  ? 0.456322 0.474658 0.490379 -0.11045    0.0349686   0.0108101   59  GLY   A H    
696  H HA2  . GLY   A 47  ? 0.437425 0.41606  0.444753 -0.0726958  0.0214727   -2.892e-05  59  GLY   A HA2  
697  H HA3  . GLY   A 47  ? 0.430166 0.437822 0.440599 -0.0719016  0.0304315   0.00937824  59  GLY   A HA3  
698  N N    . LYS   A 48  ? 0.499299 0.420847 0.479101 -0.0693491  0.0302103   0.0223042   60  LYS   A N    
699  C CA   . LYS   A 48  ? 0.546571 0.431171 0.510656 -0.0668413  0.0342594   0.0359681   60  LYS   A CA   
700  C C    . LYS   A 48  ? 0.503859 0.38163  0.453659 -0.0441421  0.0311802   0.0358256   60  LYS   A C    
701  O O    . LYS   A 48  ? 0.477603 0.371364 0.42994  -0.0355625  0.0254763   0.0240322   60  LYS   A O    
702  C CB   . LYS   A 48  ? 0.625302 0.469257 0.588691 -0.0801437  0.0319557   0.0324579   60  LYS   A CB   
703  C CG   . LYS   A 48  ? 0.650545 0.479864 0.612159 -0.0734277  0.0227054   0.0135128   60  LYS   A CG   
704  C CD   . LYS   A 48  ? 0.741254 0.519855 0.695428 -0.0816463  0.0205147   0.00943288  60  LYS   A CD   
705  C CE   . LYS   A 48  ? 0.811481 0.580872 0.761687 -0.0734639  0.0115734   -0.0117147  60  LYS   A CE   
706  N NZ   . LYS   A 48  ? 0.883869 0.599003 0.822273 -0.0748777  0.00897321  -0.0187381  60  LYS   A NZ   
707  H H    . LYS   A 48  ? 0.486037 0.411932 0.464705 -0.0600049  0.0251943   0.014345    60  LYS   A H    
708  H HA   . LYS   A 48  ? 0.550466 0.443434 0.513581 -0.0713707  0.0405031   0.0477847   60  LYS   A HA   
709  H HB2  . LYS   A 48  ? 0.647923 0.464148 0.600242 -0.077587   0.0348728   0.0431794   60  LYS   A HB2  
710  H HB3  . LYS   A 48  ? 0.627093 0.48104  0.60155  -0.0970987  0.0338763   0.0324879   60  LYS   A HB3  
711  H HG2  . LYS   A 48  ? 0.636405 0.489246 0.609249 -0.0793893  0.0193559   0.00404089  60  LYS   A HG2  
712  H HG3  . LYS   A 48  ? 0.640351 0.471386 0.593823 -0.0570673  0.0210732   0.0125637   60  LYS   A HG3  
713  H HD2  . LYS   A 48  ? 0.766121 0.519314 0.708509 -0.0734606  0.0235004   0.0197057   60  LYS   A HD2  
714  H HD3  . LYS   A 48  ? 0.760474 0.537393 0.723431 -0.100779   0.0219803   0.0105402   60  LYS   A HD3  
715  H HE2  . LYS   A 48  ? 0.78587  0.577147 0.747088 -0.0832226  0.00800118  -0.0210466  60  LYS   A HE2  
716  H HE3  . LYS   A 48  ? 0.780175 0.560637 0.724259 -0.0566555  0.0105701   -0.0125358  60  LYS   A HE3  
717  H HZ1  . LYS   A 48  ? 0.898502 0.600527 0.84236  -0.092613   0.00979649  -0.0174596  60  LYS   A HZ1  
718  H HZ2  . LYS   A 48  ? 0.891105 0.585821 0.818721 -0.0627193  0.0116214   -0.0103597  60  LYS   A HZ2  
719  H HZ3  . LYS   A 48  ? 0.876417 0.591411 0.812354 -0.0699402  0.00367593  -0.0330713  60  LYS   A HZ3  
720  N N    . LEU   A 49  ? 0.500522 0.359179 0.435969 -0.0353995  0.0351872   0.0507783   61  LEU   A N    
721  C CA   . LEU   A 49  ? 0.486866 0.335403 0.408971 -0.0140799  0.0321703   0.0514132   61  LEU   A CA   
722  C C    . LEU   A 49  ? 0.530332 0.348315 0.450019 -0.0106104  0.0265415   0.0380464   61  LEU   A C    
723  O O    . LEU   A 49  ? 0.552146 0.339516 0.473421 -0.023318   0.0263784   0.0356565   61  LEU   A O    
724  C CB   . LEU   A 49  ? 0.495109 0.327586 0.402827 -0.00571348 0.0370942   0.0717476   61  LEU   A CB   
725  C CG   . LEU   A 49  ? 0.484528 0.346811 0.391307 -0.0108947  0.043573    0.0863193   61  LEU   A CG   
726  C CD1  . LEU   A 49  ? 0.510482 0.360807 0.399371 0.00296327  0.0463592   0.106965    61  LEU   A CD1  
727  C CD2  . LEU   A 49  ? 0.449965 0.358528 0.363535 -0.00738979 0.0419369   0.0762246   61  LEU   A CD2  
728  H H    . LEU   A 49  ? 0.519408 0.373182 0.453453 -0.0429277  0.0400323   0.0617924   61  LEU   A H    
729  H HA   . LEU   A 49  ? 0.464306 0.33841  0.388418 -0.00788758 0.0303578   0.0468178   61  LEU   A HA   
730  H HB2  . LEU   A 49  ? 0.530038 0.330157 0.434292 -0.0109702  0.0380869   0.0762231   61  LEU   A HB2  
731  H HB3  . LEU   A 49  ? 0.497592 0.330046 0.397885 0.0100894   0.0347276   0.0716122   61  LEU   A HB3  
732  H HG   . LEU   A 49  ? 0.496503 0.356369 0.409239 -0.0262888  0.0471901   0.0895633   61  LEU   A HG   
733  H HD11 . LEU   A 49  ? 0.544185 0.359551 0.427571 0.00090629  0.0473093   0.114585    61  LEU   A HD11 
734  H HD12 . LEU   A 49  ? 0.508929 0.38066  0.396013 -0.00098855 0.0505613   0.115951    61  LEU   A HD12 
735  H HD13 . LEU   A 49  ? 0.502527 0.359806 0.38678  0.0182221   0.0427507   0.103713    61  LEU   A HD13 
736  H HD21 . LEU   A 49  ? 0.432855 0.349626 0.357384 -0.0158187  0.0405135   0.0656314   61  LEU   A HD21 
737  H HD22 . LEU   A 49  ? 0.43808  0.35044  0.347732 0.00443174  0.0380944   0.0719429   61  LEU   A HD22 
738  H HD23 . LEU   A 49  ? 0.447839 0.374633 0.358318 -0.00844888 0.0459153   0.0843819   61  LEU   A HD23 
739  N N    . SER   A 50  ? 0.536635 0.366289 0.452973 0.00422567  0.0218826   0.0278728   62  SER   A N    
740  C CA   . SER   A 50  ? 0.590431 0.402321 0.504423 0.00753761  0.0166224   0.0120327   62  SER   A CA   
741  C C    . SER   A 50  ? 0.683235 0.446769 0.585312 0.0146115   0.0171487   0.01362     62  SER   A C    
742  O O    . SER   A 50  ? 0.687134 0.424394 0.587928 0.00963519  0.0133776   -0.00041729 62  SER   A O    
743  C CB   . SER   A 50  ? 0.593189 0.430933 0.503943 0.0221298   0.0132723   0.00439248  62  SER   A CB   
744  O OG   . SER   A 50  ? 0.637038 0.481092 0.539054 0.0398537   0.0156673   0.0141077   62  SER   A OG   
745  H H    . SER   A 50  ? 0.521296 0.372116 0.436404 0.0116661   0.0220819   0.0306059   62  SER   A H    
746  H HA   . SER   A 50  ? 0.588558 0.403277 0.51073  -0.00541248 0.014662    0.00472501  62  SER   A HA   
747  H HB2  . SER   A 50  ? 0.605948 0.434062 0.513621 0.0250032   0.0103152   -0.00609218 62  SER   A HB2  
748  H HB3  . SER   A 50  ? 0.570818 0.432577 0.488451 0.0163025   0.0121788   0.00309636  62  SER   A HB3  
750  N N    . ASN   A 51  ? 0.706773 0.458992 0.598821 0.0281019   0.0208871   0.0298871   63  ASN   A N    
751  C CA   . ASN   A 51  ? 0.820367 0.52047  0.699433 0.0365314   0.021655    0.0367625   63  ASN   A CA   
752  C C    . ASN   A 51  ? 0.886043 0.573055 0.765613 0.0199052   0.0273288   0.0577036   63  ASN   A C    
753  O O    . ASN   A 51  ? 0.919284 0.631633 0.796183 0.025469    0.0311935   0.0742961   63  ASN   A O    
754  C CB   . ASN   A 51  ? 0.823267 0.522333 0.689346 0.0680993   0.0207441   0.0402502   63  ASN   A CB   
755  H H    . ASN   A 51  ? 0.696032 0.473725 0.588702 0.0329421   0.0224942   0.0370425   63  ASN   A H    
756  H HA   . ASN   A 51  ? 0.83367  0.509244 0.712494 0.0312383   0.0188639   0.0247526   63  ASN   A HA   
759  N N    . GLY   A 52  ? 0.930505 0.582321 0.813594 -0.00229113 0.0277087   0.0559469   64  GLY   A N    
760  C CA   . GLY   A 52  ? 0.933142 0.587527 0.822857 -0.0274215  0.0338506   0.0723292   64  GLY   A CA   
761  C C    . GLY   A 52  ? 0.915914 0.562496 0.819923 -0.0559338  0.0317354   0.0579057   64  GLY   A C    
762  O O    . GLY   A 52  ? 0.889515 0.551553 0.801338 -0.0556624  0.0256123   0.0355789   64  GLY   A O    
763  H H    . GLY   A 52  ? 0.944145 0.571156 0.825463 -0.00252773 0.0240705   0.0435496   64  GLY   A H    
764  H HA2  . GLY   A 52  ? 0.96613  0.589726 0.845342 -0.0254314  0.0364968   0.0877406   64  GLY   A HA2  
765  H HA3  . GLY   A 52  ? 0.895914 0.590046 0.791072 -0.0277813  0.0365756   0.0772762   64  GLY   A HA3  
766  N N    . LYS   A 53  ? 1.01724  0.640224 0.923527 -0.0808621  0.0365202   0.0717735   65  LYS   A N    
767  C CA   . LYS   A 53  ? 1.02408  0.634132 0.943633 -0.111211   0.0341001   0.0592761   65  LYS   A CA   
768  C C    . LYS   A 53  ? 0.978039 0.644177 0.917816 -0.135329   0.0400441   0.0656004   65  LYS   A C    
769  O O    . LYS   A 53  ? 0.994399 0.694663 0.952116 -0.147664   0.0358982   0.0472868   65  LYS   A O    
770  C CB   . LYS   A 53  ? 1.04657  0.581056 0.954002 -0.124185   0.0338154   0.066785    65  LYS   A CB   
771  H H    . LYS   A 53  ? 1.01189  0.62827  0.911068 -0.0798389  0.0413971   0.0902221   65  LYS   A H    
772  H HA   . LYS   A 53  ? 0.997824 0.614413 0.921207 -0.106489   0.027917    0.0394949   65  LYS   A HA   
775  N N    . LYS   A 54  ? 0.911953 0.591985 0.847752 -0.138755   0.0494919   0.0911318   66  LYS   A N    
776  C CA   . LYS   A 54  ? 0.838999 0.572828 0.791813 -0.16044    0.0571902   0.0992463   66  LYS   A CA   
777  C C    . LYS   A 54  ? 0.737183 0.536782 0.703777 -0.14726    0.0551207   0.0836113   66  LYS   A C    
778  O O    . LYS   A 54  ? 0.684344 0.500787 0.6421   -0.122008   0.0544124   0.0839488   66  LYS   A O    
779  C CB   . LYS   A 54  ? 0.870914 0.601861 0.810951 -0.164254   0.0679712   0.131013    66  LYS   A CB   
780  H H    . LYS   A 54  ? 0.935538 0.592485 0.856742 -0.125899   0.0512307   0.103942    66  LYS   A H    
781  H HA   . LYS   A 54  ? 0.858508 0.586984 0.822202 -0.183103   0.0565582   0.0941783   66  LYS   A HA   
784  N N    . PHE   A 55  ? 0.683847 0.521371 0.672862 -0.165907   0.053923    0.0704729   67  PHE   A N    
785  C CA   . PHE   A 55  ? 0.630267 0.52477  0.633413 -0.154644   0.0510073   0.055534    67  PHE   A CA   
786  C C    . PHE   A 55  ? 0.611468 0.559351 0.623026 -0.15879    0.0609314   0.0666694   67  PHE   A C    
787  O O    . PHE   A 55  ? 0.62808  0.584521 0.644992 -0.181762   0.0695953   0.081167    67  PHE   A O    
788  C CB   . PHE   A 55  ? 0.665894 0.578633 0.689131 -0.168897   0.0432249   0.0347394   67  PHE   A CB   
789  C CG   . PHE   A 55  ? 0.688453 0.572684 0.704783 -0.156254   0.0314929   0.0159047   67  PHE   A CG   
790  C CD1  . PHE   A 55  ? 0.699142 0.601795 0.711894 -0.131336   0.0256684   0.00576024  67  PHE   A CD1  
791  C CD2  . PHE   A 55  ? 0.738812 0.579148 0.751663 -0.170672   0.0263616   0.00778868  67  PHE   A CD2  
792  C CE1  . PHE   A 55  ? 0.705801 0.58867  0.711068 -0.120774   0.0160962   -0.00975775 67  PHE   A CE1  
793  C CE2  . PHE   A 55  ? 0.767167 0.587747 0.772253 -0.158017   0.016144    -0.0112353  67  PHE   A CE2  
794  C CZ   . PHE   A 55  ? 0.739743 0.584442 0.740903 -0.133      0.0115657   -0.0189135  67  PHE   A CZ   
795  H H    . PHE   A 55  ? 0.717476 0.544297 0.713291 -0.186492   0.0545985   0.0710646   67  PHE   A H    
796  H HA   . PHE   A 55  ? 0.619861 0.509235 0.613966 -0.134211   0.0471384   0.0507649   67  PHE   A HA   
797  H HB2  . PHE   A 55  ? 0.687325 0.59253  0.71718  -0.19097    0.0456087   0.038516    67  PHE   A HB2  
798  H HB3  . PHE   A 55  ? 0.632429 0.588504 0.667663 -0.165723   0.0435414   0.0296434   67  PHE   A HB3  
799  H HD1  . PHE   A 55  ? 0.662842 0.591408 0.677429 -0.122123   0.0283988   0.00962011  67  PHE   A HD1  
800  H HD2  . PHE   A 55  ? 0.773395 0.597119 0.788442 -0.189735   0.0299024   0.0149423   67  PHE   A HD2  
801  H HE1  . PHE   A 55  ? 0.678742 0.574513 0.681115 -0.105743   0.0127196   -0.0144196  67  PHE   A HE1  
802  H HE2  . PHE   A 55  ? 0.79303  0.583053 0.794604 -0.16712    0.012457    -0.0188015  67  PHE   A HE2  
803  H HZ   . PHE   A 55  ? 0.737711 0.572084 0.73268  -0.124945   0.00534892  -0.0305791  67  PHE   A HZ   
804  N N    . ASP   A 56  ? 0.554323 0.538391 0.566723 -0.137163   0.0595086   0.0587124   68  ASP   A N    
805  C CA   . ASP   A 56  ? 0.544666 0.588815 0.570112 -0.137605   0.0658912   0.0578477   68  ASP   A CA   
806  C C    . ASP   A 56  ? 0.51831  0.597608 0.567157 -0.140529   0.0591926   0.0377255   68  ASP   A C    
807  O O    . ASP   A 56  ? 0.508154 0.576626 0.556619 -0.126404   0.0487529   0.0230926   68  ASP   A O    
808  C CB   . ASP   A 56  ? 0.514918 0.575933 0.52832  -0.1124     0.0665389   0.0568643   68  ASP   A CB   
809  C CG   . ASP   A 56  ? 0.494164 0.613999 0.520711 -0.105573   0.0697682   0.046954    68  ASP   A CG   
810  O OD1  . ASP   A 56  ? 0.531372 0.687799 0.568015 -0.120294   0.0793141   0.0541073   68  ASP   A OD1  
811  O OD2  . ASP   A 56  ? 0.487011 0.615292 0.513386 -0.0856309  0.0628193   0.0320785   68  ASP   A OD2  
812  H H    . ASP   A 56  ? 0.549463 0.519827 0.553727 -0.121403   0.0543237   0.0529667   68  ASP   A H    
813  H HA   . ASP   A 56  ? 0.559705 0.613003 0.586846 -0.152579   0.0738385   0.0703541   68  ASP   A HA   
814  H HB2  . ASP   A 56  ? 0.532107 0.582143 0.53222  -0.111664   0.0717166   0.0708796   68  ASP   A HB2  
815  H HB3  . ASP   A 56  ? 0.505044 0.548156 0.513373 -0.0997153  0.0592411   0.0484998   68  ASP   A HB3  
816  N N    . SER   A 57  ? 0.524199 0.650034 0.593236 -0.158007   0.0651874   0.0380231   69  SER   A N    
817  C CA   . SER   A 57  ? 0.50839  0.672351 0.601471 -0.161043   0.0581102   0.0199384   69  SER   A CA   
818  C C    . SER   A 57  ? 0.485699 0.719789 0.59624  -0.156273   0.0649288   0.0163267   69  SER   A C    
819  O O    . SER   A 57  ? 0.487524 0.749851 0.601426 -0.170843   0.0774384   0.0294872   69  SER   A O    
820  C CB   . SER   A 57  ? 0.543614 0.697515 0.649641 -0.190794   0.0554215   0.0183752   69  SER   A CB   
821  O OG   . SER   A 57  ? 0.52766  0.72573  0.657003 -0.191135   0.0470598   0.00016015  69  SER   A OG   
822  H H    . SER   A 57  ? 0.537115 0.674392 0.605078 -0.167924   0.0738478   0.0502259   69  SER   A H    
823  H HA   . SER   A 57  ? 0.492355 0.644814 0.581552 -0.144778   0.0496294   0.00950694  69  SER   A HA   
824  H HB2  . SER   A 57  ? 0.554952 0.663233 0.648896 -0.191344   0.0506842   0.0182301   69  SER   A HB2  
825  H HB3  . SER   A 57  ? 0.561327 0.724618 0.671349 -0.209441   0.0638642   0.02993     69  SER   A HB3  
827  N N    . SER   A 58  ? 0.456743 0.717975 0.577276 -0.134638   0.0563911   -0.00135691 70  SER   A N    
828  C CA   . SER   A 58  ? 0.433925 0.763415 0.574825 -0.125832   0.0597398   -0.0105419  70  SER   A CA   
829  C C    . SER   A 58  ? 0.471762 0.850004 0.638517 -0.154762   0.0655752   -0.0080964  70  SER   A C    
830  O O    . SER   A 58  ? 0.464388 0.90229  0.644752 -0.157327   0.0760666   -0.00633238 70  SER   A O    
831  C CB   . SER   A 58  ? 0.40414  0.741386 0.550925 -0.0996458  0.0465861   -0.0285711  70  SER   A CB   
832  O OG   . SER   A 58  ? 0.370148 0.696907 0.526206 -0.109772   0.0354078   -0.0351978  70  SER   A OG   
833  H H    . SER   A 58  ? 0.447655 0.683215 0.561395 -0.123813   0.0479971   -0.00770439 70  SER   A H    
834  H HA   . SER   A 58  ? 0.437344 0.777865 0.5705   -0.117709   0.0671107   -0.00611037 70  SER   A HA   
835  H HB2  . SER   A 58  ? 0.390929 0.772047 0.550594 -0.0904936  0.0485448   -0.0352706  70  SER   A HB2  
836  H HB3  . SER   A 58  ? 0.390571 0.697381 0.521231 -0.0841356  0.0434888   -0.0291585  70  SER   A HB3  
838  N N    . HIS   A 59  ? 0.492808 0.847516 0.666023 -0.177779   0.0589254   -0.00888664 71  HIS   A N    
839  C CA   . HIS   A 59  ? 0.523209 0.918112 0.720896 -0.211871   0.0633434   -0.00648554 71  HIS   A CA   
840  C C    . HIS   A 59  ? 0.553052 0.959576 0.747705 -0.235173   0.0808003   0.0150739   71  HIS   A C    
841  O O    . HIS   A 59  ? 0.542758 1.01422  0.76067  -0.253943   0.0892098   0.0173646   71  HIS   A O    
842  C CB   . HIS   A 59  ? 0.529685 0.88739  0.730388 -0.233664   0.0520831   -0.013064   71  HIS   A CB   
843  C CG   . HIS   A 59  ? 0.502201 0.87159  0.710718 -0.213961   0.0356133   -0.0337871  71  HIS   A CG   
844  N ND1  . HIS   A 59  ? 0.474969 0.916802 0.709951 -0.204899   0.0306473   -0.0468776  71  HIS   A ND1  
845  C CD2  . HIS   A 59  ? 0.498712 0.818882 0.690162 -0.198822   0.0231974   -0.0420972  71  HIS   A CD2  
846  C CE1  . HIS   A 59  ? 0.463325 0.89555  0.69575  -0.185802   0.0150851   -0.0607705  71  HIS   A CE1  
847  N NE2  . HIS   A 59  ? 0.47836  0.838614 0.68458  -0.183613   0.010824    -0.0580826  71  HIS   A NE2  
848  H H    . HIS   A 59  ? 0.492999 0.807002 0.65522  -0.172751   0.0512556   -0.0119425  71  HIS   A H    
849  H HA   . HIS   A 59  ? 0.505513 0.953332 0.721669 -0.203915   0.0617135   -0.0164519  71  HIS   A HA   
850  H HB2  . HIS   A 59  ? 0.544307 0.846041 0.725506 -0.235731   0.0519132   -0.00607183 71  HIS   A HB2  
851  H HB3  . HIS   A 59  ? 0.547801 0.92895  0.763812 -0.260265   0.0558875   -0.0101109  71  HIS   A HB3  
853  H HD2  . HIS   A 59  ? 0.507189 0.77693  0.680122 -0.198722   0.0228555   -0.0375554  71  HIS   A HD2  
854  H HE1  . HIS   A 59  ? 0.454673 0.927164 0.701583 -0.175345   0.00824923  -0.0703984  71  HIS   A HE1  
856  N N    . ASP   A 60  ? 0.617416 0.967824 0.783593 -0.23248    0.0864391   0.0317061   72  ASP   A N    
857  C CA   . ASP   A 60  ? 0.689851 1.04717  0.848065 -0.252533   0.102616    0.0559447   72  ASP   A CA   
858  C C    . ASP   A 60  ? 0.675811 1.11324  0.844315 -0.241211   0.114345    0.0555902   72  ASP   A C    
859  O O    . ASP   A 60  ? 0.695147 1.16811  0.868386 -0.265131   0.128712    0.0730841   72  ASP   A O    
860  C CB   . ASP   A 60  ? 0.71662  1.00221  0.840784 -0.244943   0.104583    0.0734656   72  ASP   A CB   
861  C CG   . ASP   A 60  ? 0.749392 0.954354 0.86083  -0.254466   0.0948946   0.0748174   72  ASP   A CG   
862  O OD1  . ASP   A 60  ? 0.788013 0.983979 0.913183 -0.285748   0.0931629   0.0747446   72  ASP   A OD1  
863  O OD2  . ASP   A 60  ? 0.702922 0.856997 0.791147 -0.230906   0.089125    0.0746875   72  ASP   A OD2  
864  H H    . ASP   A 60  ? 0.607313 0.915649 0.758233 -0.217636   0.0799464   0.0287578   72  ASP   A H    
865  H HA   . ASP   A 60  ? 0.705987 1.06463  0.874647 -0.281048   0.104989    0.0621911   72  ASP   A HA   
866  H HB2  . ASP   A 60  ? 0.693802 0.978488 0.80769  -0.218943   0.102108    0.0673312   72  ASP   A HB2  
867  H HB3  . ASP   A 60  ? 0.736888 1.03106  0.85563  -0.258167   0.115258    0.0910218   72  ASP   A HB3  
868  N N    . ARG   A 61  ? 0.655715 1.12059  0.82678  -0.205377   0.108424    0.0358338   73  ARG   A N    
869  C CA   . ARG   A 61  ? 0.622615 1.15818  0.800083 -0.187881   0.118356    0.0307122   73  ARG   A CA   
870  C C    . ARG   A 61  ? 0.590035 1.20496  0.803238 -0.18892    0.117386    0.014279    73  ARG   A C    
871  O O    . ARG   A 61  ? 0.579997 1.26488  0.803691 -0.175725   0.126401    0.0079533   73  ARG   A O    
872  C CB   . ARG   A 61  ? 0.609498 1.12237  0.766165 -0.147935   0.112495    0.0184878   73  ARG   A CB   
873  H H    . ARG   A 61  ? 0.632075 1.06876  0.799493 -0.19091    0.0978532   0.0251036   73  ARG   A H    
874  H HA   . ARG   A 61  ? 0.641732 1.18984  0.812811 -0.202232   0.130066    0.0467325   73  ARG   A HA   
877  N N    . ASN   A 62  ? 0.559623 1.16654  0.790988 -0.202378   0.105733    0.00580171  74  ASN   A N    
878  C CA   . ASN   A 62  ? 0.525869 1.20976  0.793415 -0.209556   0.103502    -0.0074088  74  ASN   A CA   
879  C C    . ASN   A 62  ? 0.492312 1.21565  0.76904  -0.165311   0.0952328   -0.0304766  74  ASN   A C    
880  O O    . ASN   A 62  ? 0.528504 1.33408  0.833889 -0.160301   0.097365    -0.0412885  74  ASN   A O    
881  C CB   . ASN   A 62  ? 0.532019 1.28487  0.817902 -0.242477   0.121235    0.0068833   74  ASN   A CB   
882  H H    . ASN   A 62  ? 0.565042 1.11806  0.785472 -0.2064     0.0983898   0.00757869  74  ASN   A H    
883  H HA   . ASN   A 62  ? 0.531139 1.19351  0.805116 -0.223579   0.0946214   -0.0103997  74  ASN   A HA   
886  N N    . GLU   A 63  ? 0.477254 1.14207  0.73036  -0.133313   0.0852662   -0.0378878  75  GLU   A N    
887  C CA   . GLU   A 63  ? 0.439156 1.1246   0.697122 -0.0914725  0.075551    -0.0582977  75  GLU   A CA   
888  C C    . GLU   A 63  ? 0.399331 1.00299  0.631719 -0.0705172  0.0614753   -0.0620001  75  GLU   A C    
889  O O    . GLU   A 63  ? 0.350844 0.891847 0.558269 -0.0798967  0.0633399   -0.0500562  75  GLU   A O    
890  C CB   . GLU   A 63  ? 0.46798  1.20029  0.723463 -0.0683267  0.087528    -0.0639164  75  GLU   A CB   
891  C CG   . GLU   A 63  ? 0.491079 1.16778  0.711921 -0.0602163  0.0929844   -0.0559488  75  GLU   A CG   
892  C CD   . GLU   A 63  ? 0.524235 1.24643  0.738073 -0.0430485  0.106274    -0.0606976  75  GLU   A CD   
893  O OE1  . GLU   A 63  ? 0.530853 1.20901  0.716431 -0.0295811  0.106677    -0.0600565  75  GLU   A OE1  
894  O OE2  . GLU   A 63  ? 0.554069 1.35862  0.790352 -0.0435303  0.116087    -0.0658405  75  GLU   A OE2  
895  H H    . GLU   A 63  ? 0.477763 1.08762  0.711206 -0.137883   0.0843034   -0.0296304  75  GLU   A H    
896  H HA   . GLU   A 63  ? 0.438232 1.16251  0.717894 -0.091857   0.069988    -0.0664639  75  GLU   A HA   
897  H HB2  . GLU   A 63  ? 0.458744 1.21079  0.721629 -0.0414877  0.0809236   -0.078778   75  GLU   A HB2  
898  H HB3  . GLU   A 63  ? 0.472292 1.25683  0.742056 -0.0846739  0.0982021   -0.0589193  75  GLU   A HB3  
899  H HG2  . GLU   A 63  ? 0.500003 1.14844  0.711905 -0.0842022  0.09718     -0.0405294  75  GLU   A HG2  
900  H HG3  . GLU   A 63  ? 0.486042 1.11805  0.694682 -0.0426638  0.0826633   -0.062459   75  GLU   A HG3  
901  N N    . PRO   A 64  ? 0.362163 0.965667 0.598976 -0.0398805  0.0473151   -0.0774857  76  PRO   A N    
902  C CA   . PRO   A 64  ? 0.351565 0.8819   0.563944 -0.0217233  0.0350684   -0.0790785  76  PRO   A CA   
903  C C    . PRO   A 64  ? 0.351255 0.845124 0.537839 -0.00598509 0.0407626   -0.0775991  76  PRO   A C    
904  O O    . PRO   A 64  ? 0.347852 0.880995 0.536711 0.00345373  0.051228    -0.0819061  76  PRO   A O    
905  C CB   . PRO   A 64  ? 0.365538 0.913893 0.589228 0.00879417  0.0205854   -0.0937615  76  PRO   A CB   
906  C CG   . PRO   A 64  ? 0.360905 0.997967 0.6185   0.00689803  0.0240454   -0.101416   76  PRO   A CG   
907  C CD   . PRO   A 64  ? 0.367607 1.04287  0.632403 -0.020414   0.0427428   -0.0925115  76  PRO   A CD   
908  H HA   . PRO   A 64  ? 0.35595  0.852739 0.562056 -0.0387925  0.0317704   -0.0721872  76  PRO   A HA   
909  H HB2  . PRO   A 64  ? 0.362749 0.896328 0.576105 0.0321072   0.0189006   -0.0993934  76  PRO   A HB2  
910  H HB3  . PRO   A 64  ? 0.358557 0.878865 0.578163 0.00594532  0.0108446   -0.0923936  76  PRO   A HB3  
911  H HG2  . PRO   A 64  ? 0.364678 1.02499  0.627622 0.0338588   0.0212403   -0.111574   76  PRO   A HG2  
912  H HG3  . PRO   A 64  ? 0.361357 1.00956  0.630619 -0.00345668 0.0167804   -0.101858   76  PRO   A HG3  
913  H HD2  . PRO   A 64  ? 0.3673   1.07325  0.634135 -0.00493428 0.0496142   -0.0979394  76  PRO   A HD2  
914  H HD3  . PRO   A 64  ? 0.366761 1.08064  0.650912 -0.0404028  0.0443686   -0.090815   76  PRO   A HD3  
915  N N    . PHE   A 65  ? 0.323783 0.74768  0.486219 -0.00518934 0.0341944   -0.0719461  77  PHE   A N    
916  C CA   . PHE   A 65  ? 0.312188 0.699001 0.450571 0.0111439   0.0354828   -0.0731756  77  PHE   A CA   
917  C C    . PHE   A 65  ? 0.309245 0.685432 0.445795 0.0437068   0.0236362   -0.0882453  77  PHE   A C    
918  O O    . PHE   A 65  ? 0.289993 0.648192 0.429709 0.0506967   0.0109306   -0.0900737  77  PHE   A O    
919  C CB   . PHE   A 65  ? 0.30923  0.63372  0.425299 -0.00325465 0.0339591   -0.0601619  77  PHE   A CB   
920  C CG   . PHE   A 65  ? 0.329388 0.621226 0.421738 0.00919409  0.0352969   -0.0606274  77  PHE   A CG   
921  C CD1  . PHE   A 65  ? 0.358531 0.664801 0.441037 0.00369762  0.0475035   -0.054766   77  PHE   A CD1  
922  C CD2  . PHE   A 65  ? 0.339863 0.590353 0.419686 0.0255465   0.0239191   -0.0668727  77  PHE   A CD2  
923  C CE1  . PHE   A 65  ? 0.353221 0.634795 0.414545 0.014748    0.047113    -0.0574915  77  PHE   A CE1  
924  C CE2  . PHE   A 65  ? 0.365763 0.589572 0.425823 0.033839    0.0241692   -0.0690238  77  PHE   A CE2  
925  C CZ   . PHE   A 65  ? 0.369475 0.610134 0.420757 0.0287438   0.0352538   -0.0655786  77  PHE   A CZ   
926  H H    . PHE   A 65  ? 0.325325 0.726663 0.486676 -0.0156308  0.0286404   -0.0679817  77  PHE   A H    
927  H HA   . PHE   A 65  ? 0.316973 0.72932  0.454928 0.010356    0.045291    -0.0728114  77  PHE   A HA   
928  H HB2  . PHE   A 65  ? 0.316282 0.645301 0.433918 -0.0226748  0.0408281   -0.0504204  77  PHE   A HB2  
929  H HB3  . PHE   A 65  ? 0.31083  0.612887 0.426462 -0.0021405  0.0248561   -0.0610282  77  PHE   A HB3  
930  H HD1  . PHE   A 65  ? 0.353784 0.687943 0.443629 -0.00861149 0.0558281   -0.0484526  77  PHE   A HD1  
931  H HD2  . PHE   A 65  ? 0.340724 0.582275 0.425378 0.0297962   0.0157189   -0.0692199  77  PHE   A HD2  
932  H HE1  . PHE   A 65  ? 0.363852 0.657914 0.417436 0.0114742   0.0548207   -0.0533567  77  PHE   A HE1  
933  H HE2  . PHE   A 65  ? 0.362896 0.558397 0.415143 0.0419976   0.0165325   -0.0724086  77  PHE   A HE2  
934  H HZ   . PHE   A 65  ? 0.369176 0.594717 0.407122 0.0339161   0.034648    -0.0681393  77  PHE   A HZ   
935  N N    . VAL   A 66  ? 0.297372 0.685254 0.427762 0.0639264   0.0277222   -0.0991675  78  VAL   A N    
936  C CA   . VAL   A 66  ? 0.31592  0.695399 0.445536 0.096734    0.0175024   -0.115358   78  VAL   A CA   
937  C C    . VAL   A 66  ? 0.348564 0.678469 0.452244 0.106768    0.0158999   -0.12033    78  VAL   A C    
938  O O    . VAL   A 66  ? 0.35169  0.690676 0.444899 0.0991936   0.0265153   -0.119715   78  VAL   A O    
939  C CB   . VAL   A 66  ? 0.339407 0.789034 0.489713 0.115235    0.0233286   -0.129978   78  VAL   A CB   
940  C CG1  . VAL   A 66  ? 0.363873 0.801083 0.513177 0.153712    0.0118022   -0.147914   78  VAL   A CG1  
941  C CG2  . VAL   A 66  ? 0.319597 0.829145 0.498255 0.0993827   0.0264821   -0.124605   78  VAL   A CG2  
942  H H    . VAL   A 66  ? 0.30493  0.704884 0.430235 0.0574479   0.036986    -0.0966577  78  VAL   A H    
943  H HA   . VAL   A 66  ? 0.32122  0.683707 0.453719 0.100349    0.00773351  -0.113813   78  VAL   A HA   
944  H HB   . VAL   A 66  ? 0.337635 0.803775 0.482494 0.112121    0.0333262   -0.131581   78  VAL   A HB   
945  H HG11 . VAL   A 66  ? 0.36428  0.772723 0.512491 0.157076    0.00112091  -0.144017   78  VAL   A HG11 
946  H HG12 . VAL   A 66  ? 0.374407 0.784072 0.507646 0.162098    0.0122694   -0.15418    78  VAL   A HG12 
947  H HG13 . VAL   A 66  ? 0.368148 0.854065 0.533527 0.166845    0.0144126   -0.157051   78  VAL   A HG13 
948  H HG21 . VAL   A 66  ? 0.327327 0.883096 0.520526 0.11482     0.0283125   -0.134986   78  VAL   A HG21 
949  H HG22 . VAL   A 66  ? 0.3153   0.836211 0.494306 0.0761575   0.0358404   -0.11476    78  VAL   A HG22 
950  H HG23 . VAL   A 66  ? 0.318257 0.80972  0.499949 0.096825    0.017092    -0.120827   78  VAL   A HG23 
951  N N    . PHE   A 67  ? 0.363045 0.642332 0.455914 0.122061    0.00237174  -0.124306   79  PHE   A N    
952  C CA   . PHE   A 67  ? 0.373765 0.602414 0.442863 0.126828    -0.00080328 -0.128916   79  PHE   A CA   
953  C C    . PHE   A 67  ? 0.401517 0.586125 0.464696 0.149337    -0.0159426  -0.136395   79  PHE   A C    
954  O O    . PHE   A 67  ? 0.391602 0.577159 0.46517  0.157078    -0.0245924  -0.131929   79  PHE   A O    
955  C CB   . PHE   A 67  ? 0.346369 0.541171 0.400185 0.100915    0.00152462  -0.112559   79  PHE   A CB   
956  C CG   . PHE   A 67  ? 0.34817  0.503585 0.398645 0.0930742   -0.00880069 -0.100249   79  PHE   A CG   
957  C CD1  . PHE   A 67  ? 0.331467 0.505251 0.395436 0.081914    -0.00937723 -0.0907353  79  PHE   A CD1  
958  C CD2  . PHE   A 67  ? 0.352027 0.454949 0.385272 0.0954328   -0.0177765  -0.0988921  79  PHE   A CD2  
959  C CE1  . PHE   A 67  ? 0.315096 0.457495 0.373799 0.0765927   -0.0187763  -0.0814843  79  PHE   A CE1  
960  C CE2  . PHE   A 67  ? 0.354938 0.428347 0.383902 0.0886967   -0.0261129  -0.0869515  79  PHE   A CE2  
961  C CZ   . PHE   A 67  ? 0.346695 0.441055 0.387723 0.0809477   -0.0266755  -0.0788867  79  PHE   A CZ   
962  H H    . PHE   A 67  ? 0.362916 0.639917 0.463157 0.128612    -0.00525417 -0.123629   79  PHE   A H    
963  H HA   . PHE   A 67  ? 0.380091 0.627927 0.446675 0.133528    0.00541087  -0.138797   79  PHE   A HA   
964  H HB2  . PHE   A 67  ? 0.359634 0.534971 0.399902 0.102663    0.00167221  -0.11713    79  PHE   A HB2  
965  H HB3  . PHE   A 67  ? 0.338493 0.558808 0.397137 0.0873277   0.0101074   -0.105526   79  PHE   A HB3  
966  H HD1  . PHE   A 67  ? 0.321819 0.531405 0.398415 0.0775512   -0.0034847  -0.0912541  79  PHE   A HD1  
967  H HD2  . PHE   A 67  ? 0.368399 0.45747  0.39263  0.101165    -0.0181951  -0.106582   79  PHE   A HD2  
968  H HE1  . PHE   A 67  ? 0.31497  0.470902 0.382086 0.0691721   -0.0197105  -0.077183   79  PHE   A HE1  
969  H HE2  . PHE   A 67  ? 0.365723 0.40637  0.383255 0.0887719   -0.0314804  -0.0848532  79  PHE   A HE2  
970  H HZ   . PHE   A 67  ? 0.339538 0.416353 0.376136 0.0766855   -0.0321104  -0.0716506  79  PHE   A HZ   
971  N N    . SER   A 68  ? 0.424753 0.570436 0.47019  0.159266    -0.0196205  -0.147605   80  SER   A N    
972  C CA   . SER   A 68  ? 0.447958 0.540482 0.48402  0.177825    -0.0339693  -0.15303    80  SER   A CA   
973  C C    . SER   A 68  ? 0.45005  0.488866 0.470182 0.156937    -0.040071   -0.136385   80  SER   A C    
974  O O    . SER   A 68  ? 0.438609 0.464392 0.446339 0.139066    -0.0352423  -0.13435    80  SER   A O    
975  C CB   . SER   A 68  ? 0.478001 0.552783 0.503416 0.198683    -0.0358375  -0.176247   80  SER   A CB   
976  O OG   . SER   A 68  ? 0.486385 0.612194 0.527042 0.224182    -0.0315488  -0.193204   80  SER   A OG   
977  H H    . SER   A 68  ? 0.42184  0.573403 0.460161 0.153503    -0.0132877  -0.151715   80  SER   A H    
978  H HA   . SER   A 68  ? 0.453395 0.557121 0.500307 0.190369    -0.0389801  -0.151883   80  SER   A HA   
979  H HB2  . SER   A 68  ? 0.475447 0.548835 0.491426 0.186617    -0.0303755  -0.178931   80  SER   A HB2  
980  H HB3  . SER   A 68  ? 0.505489 0.534973 0.522087 0.206742    -0.0457555  -0.177411   80  SER   A HB3  
982  N N    . LEU   A 69  ? 0.466698 0.478808 0.486776 0.160983    -0.0509093  -0.124856   81  LEU   A N    
983  C CA   . LEU   A 69  ? 0.469824 0.442822 0.476774 0.140472    -0.0553624  -0.106911   81  LEU   A CA   
984  C C    . LEU   A 69  ? 0.513493 0.431735 0.500718 0.136226    -0.0603939  -0.110529   81  LEU   A C    
985  O O    . LEU   A 69  ? 0.547308 0.434247 0.528636 0.154935    -0.0679815  -0.122554   81  LEU   A O    
986  C CB   . LEU   A 69  ? 0.484801 0.449636 0.49535  0.148605    -0.0658388  -0.0943306  81  LEU   A CB   
987  C CG   . LEU   A 69  ? 0.48241  0.418329 0.480264 0.128296    -0.0696063  -0.0745566  81  LEU   A CG   
988  C CD1  . LEU   A 69  ? 0.432257 0.394688 0.433138 0.104168    -0.0593663  -0.0677356  81  LEU   A CD1  
989  C CD2  . LEU   A 69  ? 0.511459 0.444647 0.510675 0.139239    -0.0806532  -0.0627796  81  LEU   A CD2  
990  H H    . LEU   A 69  ? 0.47702  0.49843  0.505148 0.177779    -0.0556111  -0.128081   81  LEU   A H    
991  H HA   . LEU   A 69  ? 0.446355 0.43762  0.455045 0.123585    -0.0481873  -0.100541   81  LEU   A HA   
992  H HB2  . LEU   A 69  ? 0.466735 0.470179 0.491306 0.151305    -0.0631573  -0.0948232  81  LEU   A HB2  
993  H HB3  . LEU   A 69  ? 0.513271 0.456632 0.520794 0.166585    -0.0734173  -0.0991318  81  LEU   A HB3  
994  H HG   . LEU   A 69  ? 0.500988 0.400871 0.485969 0.124088    -0.0722634  -0.0733748  81  LEU   A HG   
995  H HD11 . LEU   A 69  ? 0.431376 0.390502 0.427809 0.0964676   -0.0536514  -0.0717888  81  LEU   A HD11 
996  H HD12 . LEU   A 69  ? 0.433219 0.382508 0.427264 0.094898    -0.0621768  -0.0566504  81  LEU   A HD12 
997  H HD13 . LEU   A 69  ? 0.420184 0.416667 0.433862 0.105799    -0.0558438  -0.0704202  81  LEU   A HD13 
998  H HD21 . LEU   A 69  ? 0.535094 0.449089 0.531812 0.156957    -0.0878284  -0.0659072  81  LEU   A HD21 
999  H HD22 . LEU   A 69  ? 0.488652 0.45902  0.500901 0.140913    -0.0786504  -0.0642539  81  LEU   A HD22 
1000 H HD23 . LEU   A 69  ? 0.505765 0.420565 0.494813 0.126976    -0.0827093  -0.050737   81  LEU   A HD23 
1001 N N    . GLY   A 70  ? 0.527156 0.433251 0.504429 0.111231    -0.0568309  -0.100217   82  GLY   A N    
1002 C CA   . GLY   A 70  ? 0.555451 0.413368 0.515614 0.100304    -0.0623124  -0.099956   82  GLY   A CA   
1003 C C    . GLY   A 70  ? 0.597247 0.450679 0.55106  0.103606    -0.0601257  -0.121315   82  GLY   A C    
1004 O O    . GLY   A 70  ? 0.667561 0.474949 0.608432 0.100317    -0.0677372  -0.127471   82  GLY   A O    
1005 H H    . GLY   A 70  ? 0.492734 0.422316 0.474488 0.100329    -0.0509113  -0.0932478  82  GLY   A H    
1006 H HA2  . GLY   A 70  ? 0.54285  0.40193  0.499325 0.0828856   -0.0596702  -0.0890934  82  GLY   A HA2  
1007 H HA3  . GLY   A 70  ? 0.586106 0.412571 0.541603 0.107238    -0.0707226  -0.0961027  82  GLY   A HA3  
1008 N N    . LYS   A 71  ? 0.568729 0.469286 0.530702 0.109826    -0.0502917  -0.133022   83  LYS   A N    
1009 C CA   . LYS   A 71  ? 0.584453 0.490269 0.539167 0.115217    -0.0475758  -0.155199   83  LYS   A CA   
1010 C C    . LYS   A 71  ? 0.599826 0.537983 0.55038  0.0951799   -0.0377279  -0.15119    83  LYS   A C    
1011 O O    . LYS   A 71  ? 0.624578 0.582613 0.569259 0.0986224   -0.0333716  -0.167711   83  LYS   A O    
1012 C CB   . LYS   A 71  ? 0.587751 0.526938 0.552787 0.142549    -0.0440555  -0.173423   83  LYS   A CB   
1013 H H    . LYS   A 71  ? 0.545733 0.477191 0.517411 0.109786    -0.0450325  -0.126872   83  LYS   A H    
1014 H HA   . LYS   A 71  ? 0.622415 0.489039 0.567152 0.114779    -0.0550252  -0.161672   83  LYS   A HA   
1017 N N    . GLY   A 72  ? 0.614512 0.55901  0.566827 0.0764369   -0.0346109  -0.12966    84  GLY   A N    
1018 C CA   . GLY   A 72  ? 0.593828 0.569228 0.543032 0.0611789   -0.0256371  -0.12217    84  GLY   A CA   
1019 C C    . GLY   A 72  ? 0.546688 0.572189 0.502232 0.068229    -0.0142137  -0.126184   84  GLY   A C    
1020 O O    . GLY   A 72  ? 0.5061   0.554617 0.453793 0.0613578   -0.00811132 -0.126813   84  GLY   A O    
1021 H H    . GLY   A 72  ? 0.600086 0.528559 0.554767 0.0743802   -0.0385605  -0.119255   84  GLY   A H    
1022 H HA2  . GLY   A 72  ? 0.567886 0.541649 0.519234 0.0515639   -0.0248763  -0.107212   84  GLY   A HA2  
1023 H HA3  . GLY   A 72  ? 0.597032 0.562424 0.536763 0.0547381   -0.0279969  -0.128354   84  GLY   A HA3  
1024 N N    . GLN   A 73  ? 0.46382  0.510425 0.43363  0.0803804   -0.011161   -0.126643   85  GLN   A N    
1025 C CA   . GLN   A 73  ? 0.417109 0.515089 0.395309 0.0810677   0.00105966  -0.124478   85  GLN   A CA   
1026 C C    . GLN   A 73  ? 0.392392 0.499515 0.375306 0.0632021   0.00683925  -0.10161    85  GLN   A C    
1027 O O    . GLN   A 73  ? 0.389009 0.531779 0.376833 0.0574231   0.0172958   -0.0941756  85  GLN   A O    
1028 C CB   . GLN   A 73  ? 0.429779 0.55384  0.42357  0.0999357   0.00209358  -0.135424   85  GLN   A CB   
1029 C CG   . GLN   A 73  ? 0.461796 0.580837 0.449774 0.121988    -0.00204913 -0.16119    85  GLN   A CG   
1030 C CD   . GLN   A 73  ? 0.490844 0.624279 0.494365 0.145902    -0.00520543 -0.172088   85  GLN   A CD   
1031 O OE1  . GLN   A 73  ? 0.475713 0.637663 0.496837 0.144753    -0.00246558 -0.161338   85  GLN   A OE1  
1032 N NE2  . GLN   A 73  ? 0.537957 0.651822 0.534903 0.168549    -0.0118038  -0.194988   85  GLN   A NE2  
1033 H H    . GLN   A 73  ? 0.481371 0.511619 0.455941 0.0876908   -0.0169206  -0.127485   85  GLN   A H    
1034 H HA   . GLN   A 73  ? 0.431026 0.543012 0.400853 0.0809565   0.00503615  -0.131261   85  GLN   A HA   
1035 H HB2  . GLN   A 73  ? 0.425663 0.535639 0.426771 0.101654    -0.00336426 -0.129944   85  GLN   A HB2  
1036 H HB3  . GLN   A 73  ? 0.416411 0.576949 0.417185 0.0964771   0.0108416   -0.131137   85  GLN   A HB3  
1037 H HG2  . GLN   A 73  ? 0.467686 0.612954 0.450632 0.122358    0.00478939  -0.168126   85  GLN   A HG2  
1038 H HG3  . GLN   A 73  ? 0.481262 0.561607 0.459059 0.121026    -0.0098723  -0.165026   85  GLN   A HG3  
1039 H HE21 . GLN   A 73  ? 0.544433 0.675501 0.549955 0.186058    -0.0120485  -0.204391   85  GLN   A HE21 
1040 H HE22 . GLN   A 73  ? 0.550722 0.634203 0.534827 0.166419    -0.0162193  -0.201514   85  GLN   A HE22 
1041 N N    . VAL   A 74  ? 0.364677 0.437968 0.345536 0.0546311   -0.00010885 -0.0905271  86  VAL   A N    
1042 C CA   . VAL   A 74  ? 0.342107 0.415676 0.325683 0.0404045   0.00334984  -0.072186   86  VAL   A CA   
1043 C C    . VAL   A 74  ? 0.324134 0.3684   0.294873 0.0312258   -0.00147413 -0.0649571  86  VAL   A C    
1044 O O    . VAL   A 74  ? 0.354871 0.379205 0.31719  0.0332986   -0.00796393 -0.0733718  86  VAL   A O    
1045 C CB   . VAL   A 74  ? 0.323773 0.396874 0.321495 0.0418778   -0.00035886 -0.0680666  86  VAL   A CB   
1046 C CG1  . VAL   A 74  ? 0.320966 0.434885 0.335014 0.046674    0.00595431  -0.0726737  86  VAL   A CG1  
1047 C CG2  . VAL   A 74  ? 0.33741  0.379677 0.333115 0.05161     -0.0123125  -0.0731969  86  VAL   A CG2  
1048 H H    . VAL   A 74  ? 0.38114  0.429418 0.35807  0.05813     -0.00737489 -0.0950245  86  VAL   A H    
1049 H HA   . VAL   A 74  ? 0.332159 0.426991 0.316068 0.0358613   0.010989    -0.0676421  86  VAL   A HA   
1050 H HB   . VAL   A 74  ? 0.316398 0.383484 0.313247 0.0321025   0.00074096  -0.0577772  86  VAL   A HB   
1051 H HG11 . VAL   A 74  ? 0.331068 0.45444  0.346015 0.0582825   0.00557578  -0.0839042  86  VAL   A HG11 
1052 H HG12 . VAL   A 74  ? 0.31517  0.445611 0.329378 0.0378138   0.0137318   -0.0663864  86  VAL   A HG12 
1053 H HG13 . VAL   A 74  ? 0.31747  0.433047 0.340713 0.0469138   0.00247846  -0.0707162  86  VAL   A HG13 
1054 H HG21 . VAL   A 74  ? 0.333433 0.377358 0.336485 0.0524056   -0.0152324  -0.069348   86  VAL   A HG21 
1055 H HG22 . VAL   A 74  ? 0.339953 0.359883 0.325907 0.04586     -0.0153927  -0.0691921  86  VAL   A HG22 
1056 H HG23 . VAL   A 74  ? 0.35098  0.394729 0.347313 0.062901    -0.0141756  -0.0841168  86  VAL   A HG23 
1057 N N    . ILE   A 75  ? 0.309351 0.352961 0.278774 0.0208791   0.00202113  -0.050342   87  ILE   A N    
1058 C CA   . ILE   A 75  ? 0.31887  0.343623 0.278495 0.0136493   -0.00157139 -0.0429489  87  ILE   A CA   
1059 C C    . ILE   A 75  ? 0.325906 0.32423  0.285749 0.0142367   -0.0110115  -0.0442345  87  ILE   A C    
1060 O O    . ILE   A 75  ? 0.321139 0.315732 0.289118 0.0204557   -0.0144445  -0.0466609  87  ILE   A O    
1061 C CB   . ILE   A 75  ? 0.321959 0.349338 0.280516 0.00699049  0.00360132  -0.0286378  87  ILE   A CB   
1062 C CG1  . ILE   A 75  ? 0.302236 0.327201 0.271071 0.00528096  0.00413443  -0.0249439  87  ILE   A CG1  
1063 C CG2  . ILE   A 75  ? 0.319968 0.367131 0.272846 0.00599424  0.0118641   -0.0228692  87  ILE   A CG2  
1064 C CD1  . ILE   A 75  ? 0.326009 0.343051 0.291623 -0.0005447  0.00730487  -0.0139167  87  ILE   A CD1  
1065 H H    . ILE   A 75  ? 0.306666 0.362753 0.281583 0.0184065   0.00688008  -0.0452562  87  ILE   A H    
1066 H HA   . ILE   A 75  ? 0.324366 0.352457 0.277066 0.0131755   -0.00158217 -0.0467418  87  ILE   A HA   
1067 H HB   . ILE   A 75  ? 0.314981 0.332146 0.268423 0.00436003  0.00057413  -0.0252361  87  ILE   A HB   
1068 H HG12 . ILE   A 75  ? 0.311707 0.350983 0.287132 0.00629313  0.00773208  -0.0274213  87  ILE   A HG12 
1069 H HG13 . ILE   A 75  ? 0.312055 0.327211 0.283202 0.0072744   -0.0016199  -0.0280872  87  ILE   A HG13 
1070 H HG21 . ILE   A 75  ? 0.319051 0.36161  0.268799 0.00341481  0.0136819   -0.0137075  87  ILE   A HG21 
1071 H HG22 . ILE   A 75  ? 0.321914 0.381411 0.280015 0.0066038   0.0162197   -0.0235806  87  ILE   A HG22 
1072 H HG23 . ILE   A 75  ? 0.325014 0.378046 0.271614 0.0075073   0.0107772   -0.0274502  87  ILE   A HG23 
1073 H HD11 . ILE   A 75  ? 0.31736  0.326566 0.276015 -0.0002922  0.00513764  -0.0114588  87  ILE   A HD11 
1074 H HD12 . ILE   A 75  ? 0.317005 0.329559 0.288221 -0.00242371 0.0055698   -0.0142129  87  ILE   A HD12 
1075 H HD13 . ILE   A 75  ? 0.320488 0.345226 0.284937 -0.0023324  0.0130384   -0.009227   87  ILE   A HD13 
1076 N N    . LYS   A 76  ? 0.313601 0.297457 0.26442  0.00738785  -0.0152049  -0.0415281  88  LYS   A N    
1077 C CA   . LYS   A 76  ? 0.331481 0.288963 0.279299 0.00503357  -0.0237701  -0.0401534  88  LYS   A CA   
1078 C C    . LYS   A 76  ? 0.335423 0.289374 0.287523 0.00620471  -0.0252936  -0.0310352  88  LYS   A C    
1079 O O    . LYS   A 76  ? 0.34263  0.279892 0.295121 0.0106589   -0.0322468  -0.0305594  88  LYS   A O    
1080 C CB   . LYS   A 76  ? 0.354611 0.306212 0.293423 -0.0072385  -0.0260901  -0.0365577  88  LYS   A CB   
1081 H H    . LYS   A 76  ? 0.315794 0.308169 0.262098 0.0035021   -0.0125994  -0.0394893  88  LYS   A H    
1082 H HA   . LYS   A 76  ? 0.349678 0.296961 0.29825  0.0108777   -0.0274497  -0.0482171  88  LYS   A HA   
1085 N N    . ALA   A 77  ? 0.317478 0.285755 0.271437 0.00323391  -0.019575   -0.0243211  89  ALA   A N    
1086 C CA   . ALA   A 77  ? 0.315334 0.282103 0.271622 0.00320797  -0.0213119  -0.0187286  89  ALA   A CA   
1087 C C    . ALA   A 77  ? 0.302935 0.274484 0.269765 0.0106674   -0.0243056  -0.0239219  89  ALA   A C    
1088 O O    . ALA   A 77  ? 0.295143 0.263192 0.262631 0.0126058   -0.0300498  -0.021253   89  ALA   A O    
1089 C CB   . ALA   A 77  ? 0.299971 0.2763   0.255688 -0.00016351 -0.0148239  -0.014103   89  ALA   A CB   
1090 H H    . ALA   A 77  ? 0.312547 0.290821 0.265304 0.00154799  -0.01488    -0.0236253  89  ALA   A H    
1091 H HA   . ALA   A 77  ? 0.317456 0.274373 0.268136 0.0007792   -0.0254606  -0.0146761  89  ALA   A HA   
1092 H HB1  . ALA   A 77  ? 0.301094 0.277012 0.250525 -0.00272021 -0.0138696  -0.0104406  89  ALA   A HB1  
1093 H HB2  . ALA   A 77  ? 0.298766 0.282937 0.258147 0.00045958  -0.0103382  -0.0156936  89  ALA   A HB2  
1094 H HB3  . ALA   A 77  ? 0.300896 0.27625  0.258394 -0.00012326 -0.0162945  -0.0132939  89  ALA   A HB3  
1095 N N    . TRP   A 78  ? 0.291572 0.276666 0.266551 0.0155922   -0.0206303  -0.031483   90  TRP   A N    
1096 C CA   . TRP   A 78  ? 0.312218 0.310917 0.299845 0.0238277   -0.0231148  -0.0374069  90  TRP   A CA   
1097 C C    . TRP   A 78  ? 0.321226 0.303505 0.307063 0.0359349   -0.0324602  -0.0417361  90  TRP   A C    
1098 O O    . TRP   A 78  ? 0.326249 0.313285 0.318783 0.0440805   -0.0388006  -0.0419127  90  TRP   A O    
1099 C CB   . TRP   A 78  ? 0.306913 0.333259 0.304809 0.024713    -0.0146919  -0.0432297  90  TRP   A CB   
1100 C CG   . TRP   A 78  ? 0.286962 0.330008 0.292652 0.0139496   -0.0083177  -0.0380705  90  TRP   A CG   
1101 C CD1  . TRP   A 78  ? 0.289186 0.321414 0.288269 0.00330026  -0.00472025 -0.0297228  90  TRP   A CD1  
1102 C CD2  . TRP   A 78  ? 0.283461 0.357052 0.305761 0.0123582   -0.00477256 -0.0417867  90  TRP   A CD2  
1103 N NE1  . TRP   A 78  ? 0.28896  0.334729 0.297752 -0.00591754 6.363e-05   -0.0279205  90  TRP   A NE1  
1104 C CE2  . TRP   A 78  ? 0.29966  0.373687 0.323728 -0.00281201 0.0004051   -0.0346273  90  TRP   A CE2  
1105 C CE3  . TRP   A 78  ? 0.297443 0.399224 0.333761 0.02256     -0.00568169 -0.0508882  90  TRP   A CE3  
1106 C CZ2  . TRP   A 78  ? 0.298951 0.399705 0.338545 -0.0126005  0.00490653  -0.0352235  90  TRP   A CZ2  
1107 C CZ3  . TRP   A 78  ? 0.307411 0.444407 0.3607   0.014795    -0.00049901 -0.0517236  90  TRP   A CZ3  
1108 C CH2  . TRP   A 78  ? 0.313007 0.449002 0.368077 -0.0048834  0.00479581  -0.0433861  90  TRP   A CH2  
1109 H H    . TRP   A 78  ? 0.297482 0.28719  0.270248 0.014189    -0.0164436  -0.033003   90  TRP   A H    
1110 H HA   . TRP   A 78  ? 0.302276 0.304584 0.292933 0.0208634   -0.0245517  -0.0341721  90  TRP   A HA   
1111 H HB2  . TRP   A 78  ? 0.305573 0.330643 0.29739  0.0237333   -0.0110856  -0.0442151  90  TRP   A HB2  
1112 H HB3  . TRP   A 78  ? 0.309976 0.345662 0.315025 0.0336372   -0.0170663  -0.0498531  90  TRP   A HB3  
1113 H HD1  . TRP   A 78  ? 0.287923 0.305422 0.277324 0.00237019  -0.00560972 -0.0259879  90  TRP   A HD1  
1114 H HE1  . TRP   A 78  ? 0.293481 0.331249 0.29939  -0.0126226  0.00240295  -0.023532   90  TRP   A HE1  
1115 H HE3  . TRP   A 78  ? 0.304196 0.401852 0.338622 0.0343906   -0.00954276 -0.0566148  90  TRP   A HE3  
1116 H HZ2  . TRP   A 78  ? 0.306181 0.40169  0.345894 -0.0240998  0.0079965   -0.0304495  90  TRP   A HZ2  
1117 H HZ3  . TRP   A 78  ? 0.307244 0.469065 0.371359 0.0225685   -0.00074568 -0.0582543  90  TRP   A HZ3  
1118 H HH2  . TRP   A 78  ? 0.308149 0.467721 0.375461 -0.0126718  0.00799713  -0.0438395  90  TRP   A HH2  
1119 N N    . ASP   A 79  ? 0.332725 0.295616 0.309477 0.0375321   -0.0340357  -0.0456941  91  ASP   A N    
1120 C CA   . ASP   A 79  ? 0.37939  0.315616 0.351814 0.0485465   -0.0435134  -0.0495104  91  ASP   A CA   
1121 C C    . ASP   A 79  ? 0.393428 0.30837  0.357869 0.0445031   -0.0511495  -0.035904   91  ASP   A C    
1122 O O    . ASP   A 79  ? 0.406652 0.308999 0.371202 0.05663     -0.0597522  -0.0339072  91  ASP   A O    
1123 C CB   . ASP   A 79  ? 0.411118 0.326764 0.374312 0.0476116   -0.0442781  -0.0584507  91  ASP   A CB   
1124 C CG   . ASP   A 79  ? 0.423933 0.357944 0.392905 0.059741    -0.0400687  -0.0756659  91  ASP   A CG   
1125 O OD1  . ASP   A 79  ? 0.406081 0.36548  0.387788 0.072869    -0.0383249  -0.0808681  91  ASP   A OD1  
1126 O OD2  . ASP   A 79  ? 0.447679 0.375075 0.408614 0.0560248   -0.038691   -0.0846378  91  ASP   A OD2  
1127 H H    . ASP   A 79  ? 0.333258 0.298383 0.30598  0.0316053   -0.0295933  -0.0462112  91  ASP   A H    
1128 H HA   . ASP   A 79  ? 0.382398 0.329651 0.363214 0.0602944   -0.0449426  -0.055515   91  ASP   A HA   
1129 H HB2  . ASP   A 79  ? 0.401113 0.318018 0.359043 0.0357342   -0.0408671  -0.0545264  91  ASP   A HB2  
1130 H HB3  . ASP   A 79  ? 0.432248 0.320663 0.389489 0.0503835   -0.0514001  -0.0572524  91  ASP   A HB3  
1131 N N    . ILE   A 80  ? 0.343278 0.258486 0.300406 0.0292993   -0.0477842  -0.0261205  92  ILE   A N    
1132 C CA   . ILE   A 80  ? 0.370888 0.273576 0.31876  0.0242765   -0.0532738  -0.0127804  92  ILE   A CA   
1133 C C    . ILE   A 80  ? 0.370159 0.292676 0.324526 0.0306504   -0.0556753  -0.0106815  92  ILE   A C    
1134 O O    . ILE   A 80  ? 0.394306 0.308103 0.344301 0.0377634   -0.0642276  -0.0039115  92  ILE   A O    
1135 C CB   . ILE   A 80  ? 0.375212 0.280337 0.314348 0.00815761  -0.0481483  -0.0051583  92  ILE   A CB   
1136 C CG1  . ILE   A 80  ? 0.411734 0.298709 0.344172 -0.00092203 -0.0485207  -0.0065059  92  ILE   A CG1  
1137 C CG2  . ILE   A 80  ? 0.404329 0.309495 0.33426  0.00315219  -0.0512046  0.00792565  92  ILE   A CG2  
1138 C CD1  . ILE   A 80  ? 0.403356 0.307938 0.332814 -0.0141372  -0.0416814  -0.00345421 92  ILE   A CD1  
1139 H H    . ILE   A 80  ? 0.344006 0.269178 0.301308 0.0229329   -0.0419214  -0.0275603  92  ILE   A H    
1140 H HA   . ILE   A 80  ? 0.393549 0.274301 0.336001 0.0276085   -0.0593278  -0.0103053  92  ILE   A HA   
1141 H HB   . ILE   A 80  ? 0.362512 0.284876 0.306338 0.00665892  -0.0422136  -0.00855389 92  ILE   A HB   
1142 H HG12 . ILE   A 80  ? 0.429141 0.295924 0.354901 -0.00346934 -0.0540155  -0.00029471 92  ILE   A HG12 
1143 H HG13 . ILE   A 80  ? 0.411302 0.295769 0.34775  0.00466211  -0.0483225  -0.0160364  92  ILE   A HG13 
1144 H HG21 . ILE   A 80  ? 0.396443 0.302401 0.320571 -0.00629071 -0.0485562  0.0126769   92  ILE   A HG21 
1145 H HG22 . ILE   A 80  ? 0.415527 0.305562 0.341281 0.00695447  -0.05759    0.012805    92  ILE   A HG22 
1146 H HG23 . ILE   A 80  ? 0.384028 0.304981 0.317546 0.00576671  -0.0495245  0.00652441  92  ILE   A HG23 
1147 H HD11 . ILE   A 80  ? 0.383985 0.305404 0.318588 -0.0108259  -0.03656    -0.00772736 92  ILE   A HD11 
1148 H HD12 . ILE   A 80  ? 0.411539 0.308144 0.338157 -0.0205014  -0.042655   -0.00594085 92  ILE   A HD12 
1149 H HD13 . ILE   A 80  ? 0.400205 0.308549 0.325218 -0.0191133  -0.041668   0.00513024  92  ILE   A HD13 
1150 N N    . GLY   A 81  ? 0.339085 0.287482 0.302849 0.0271673   -0.048785   -0.0159622  93  GLY   A N    
1151 C CA   . GLY   A 81  ? 0.332669 0.300958 0.302269 0.0277221   -0.0507432  -0.016175   93  GLY   A CA   
1152 C C    . GLY   A 81  ? 0.331759 0.314751 0.313451 0.0410783   -0.0575842  -0.0214101  93  GLY   A C    
1153 O O    . GLY   A 81  ? 0.309433 0.299576 0.289716 0.0459262   -0.0656192  -0.0177817  93  GLY   A O    
1154 H H    . GLY   A 81  ? 0.332387 0.285347 0.298407 0.023522    -0.0429313  -0.0195914  93  GLY   A H    
1155 H HA2  . GLY   A 81  ? 0.335375 0.298494 0.295929 0.024832    -0.0536682  -0.00969782 93  GLY   A HA2  
1156 H HA3  . GLY   A 81  ? 0.317701 0.297221 0.291969 0.0218056   -0.0447663  -0.0195126  93  GLY   A HA3  
1157 N N    . VAL   A 82  ? 0.331016 0.324243 0.32467  0.0482253   -0.0543096  -0.0305324  94  VAL   A N    
1158 C CA   . VAL   A 82  ? 0.327469 0.345055 0.336164 0.0622437   -0.0593116  -0.0373477  94  VAL   A CA   
1159 C C    . VAL   A 82  ? 0.353559 0.349273 0.354494 0.0797257   -0.0712843  -0.0325158  94  VAL   A C    
1160 O O    . VAL   A 82  ? 0.354067 0.368634 0.362483 0.0921376   -0.0795029  -0.0326564  94  VAL   A O    
1161 C CB   . VAL   A 82  ? 0.329013 0.370132 0.352224 0.0658029   -0.0511391  -0.0486361  94  VAL   A CB   
1162 C CG1  . VAL   A 82  ? 0.3453   0.41887  0.386047 0.0831944   -0.0561857  -0.0567963  94  VAL   A CG1  
1163 C CG2  . VAL   A 82  ? 0.301652 0.361062 0.330389 0.0470485   -0.0400043  -0.048659   94  VAL   A CG2  
1164 H H    . VAL   A 82  ? 0.325389 0.313667 0.317744 0.0449464   -0.0488678  -0.0328397  94  VAL   A H    
1165 H HA   . VAL   A 82  ? 0.323059 0.358813 0.337195 0.0577706   -0.0605118  -0.0372205  94  VAL   A HA   
1166 H HB   . VAL   A 82  ? 0.335595 0.358749 0.351975 0.0693511   -0.0497776  -0.050407   94  VAL   A HB   
1167 H HG11 . VAL   A 82  ? 0.340435 0.427351 0.385519 0.0818785   -0.0609986  -0.0543222  94  VAL   A HG11 
1168 H HG12 . VAL   A 82  ? 0.359792 0.41788  0.396432 0.0978335   -0.0615995  -0.0583343  94  VAL   A HG12 
1169 H HG13 . VAL   A 82  ? 0.334332 0.432427 0.385927 0.0813198   -0.0493636  -0.0630957  94  VAL   A HG13 
1170 H HG21 . VAL   A 82  ? 0.300587 0.378053 0.337823 0.0485596   -0.0345052  -0.0540367  94  VAL   A HG21 
1171 H HG22 . VAL   A 82  ? 0.301008 0.341469 0.318888 0.0394597   -0.0369109  -0.0441201  94  VAL   A HG22 
1172 H HG23 . VAL   A 82  ? 0.298982 0.37124  0.333101 0.0413759   -0.0417338  -0.0477316  94  VAL   A HG23 
1173 N N    . ALA   A 83  ? 0.356313 0.311873 0.341455 0.0794949   -0.0731369  -0.0268275  95  ALA   A N    
1174 C CA   . ALA   A 83  ? 0.380906 0.305472 0.35506  0.0932113   -0.0847486  -0.018456   95  ALA   A CA   
1175 C C    . ALA   A 83  ? 0.381805 0.311114 0.347474 0.0917427   -0.0923319  -0.00435394 95  ALA   A C    
1176 O O    . ALA   A 83  ? 0.416915 0.330604 0.375694 0.106821    -0.103192   0.00417738  95  ALA   A O    
1177 C CB   . ALA   A 83  ? 0.407595 0.28697  0.365899 0.0855507   -0.0845266  -0.0140324  95  ALA   A CB   
1178 H H    . ALA   A 83  ? 0.351426 0.298296 0.332397 0.0700774   -0.0673598  -0.0276914  95  ALA   A H    
1179 H HA   . ALA   A 83  ? 0.39358  0.324775 0.375999 0.1095      -0.0884252  -0.0252366  95  ALA   A HA   
1180 H HB1  . ALA   A 83  ? 0.405584 0.283214 0.36822  0.0878546   -0.0807645  -0.0245215  95  ALA   A HB1  
1181 H HB2  . ALA   A 83  ? 0.395178 0.273297 0.346908 0.0702206   -0.0805206  -0.00782726 95  ALA   A HB2  
1182 H HB3  . ALA   A 83  ? 0.434232 0.288417 0.384278 0.0933879   -0.0923658  -0.00705602 95  ALA   A HB3  
1183 N N    . THR   A 84  ? 0.370106 0.319432 0.334262 0.0754749   -0.0872719  -0.00195251 96  THR   A N    
1184 C CA   . THR   A 84  ? 0.389144 0.348183 0.343239 0.074158    -0.0941559  0.00871334  96  THR   A CA   
1185 C C    . THR   A 84  ? 0.394163 0.39569  0.3633   0.0813972   -0.0988935  0.00026262  96  THR   A C    
1186 O O    . THR   A 84  ? 0.366158 0.381808 0.327285 0.082372    -0.106261   0.00653496  96  THR   A O    
1187 C CB   . THR   A 84  ? 0.383858 0.343492 0.326444 0.0547439   -0.0870237  0.0132175   96  THR   A CB   
1188 O OG1  . THR   A 84  ? 0.330107 0.315289 0.285944 0.0463952   -0.0792429  4.97e-06    96  THR   A OG1  
1189 C CG2  . THR   A 84  ? 0.411789 0.340833 0.343038 0.0439536   -0.0812938  0.020145    96  THR   A CG2  
1190 H H    . THR   A 84  ? 0.352072 0.30863  0.320209 0.0656599   -0.0795551  -0.00725853 96  THR   A H    
1191 H HA   . THR   A 84  ? 0.415209 0.354347 0.359048 0.0815089   -0.101005   0.0187489   96  THR   A HA   
1192 H HB   . THR   A 84  ? 0.389551 0.354551 0.322724 0.055117    -0.0919378  0.0205789   96  THR   A HB   
1194 H HG21 . THR   A 84  ? 0.398521 0.332554 0.322294 0.0341703   -0.0776929  0.0239831   96  THR   A HG21 
1195 H HG22 . THR   A 84  ? 0.394381 0.321823 0.333639 0.0423727   -0.0760292  0.0120413   96  THR   A HG22 
1196 H HG23 . THR   A 84  ? 0.428233 0.335732 0.351493 0.0482998   -0.0867091  0.0286876   96  THR   A HG23 
1197 N N    . MET   A 85  ? 0.384805 0.411503 0.375373 0.0851007   -0.094866   -0.0139331  97  MET   A N    
1198 C CA   . MET   A 85  ? 0.377366 0.450211 0.385095 0.0845374   -0.0976025  -0.0232938  97  MET   A CA   
1199 C C    . MET   A 85  ? 0.396574 0.493434 0.415818 0.108154    -0.10897    -0.0249051  97  MET   A C    
1200 O O    . MET   A 85  ? 0.388956 0.470234 0.41019  0.126239    -0.110869   -0.0250567  97  MET   A O    
1201 C CB   . MET   A 85  ? 0.360077 0.453304 0.385716 0.0711864   -0.0856637  -0.0358318  97  MET   A CB   
1202 C CG   . MET   A 85  ? 0.343975 0.416895 0.359285 0.0506247   -0.0752876  -0.0343448  97  MET   A CG   
1203 S SD   . MET   A 85  ? 0.327869 0.42229  0.36205  0.0359325   -0.0624323  -0.0446377  97  MET   A SD   
1204 C CE   . MET   A 85  ? 0.327004 0.467525 0.380904 0.0271269   -0.0673202  -0.0542313  97  MET   A CE   
1205 H H    . MET   A 85  ? 0.382325 0.399577 0.376929 0.086993    -0.0903243  -0.0180424  97  MET   A H    
1206 H HA   . MET   A 85  ? 0.376759 0.454504 0.376798 0.0768959   -0.0999995  -0.0204736  97  MET   A HA   
1207 H HB2  . MET   A 85  ? 0.359276 0.450149 0.391005 0.0789436   -0.0827546  -0.0389365  97  MET   A HB2  
1208 H HB3  . MET   A 85  ? 0.352797 0.477126 0.391078 0.0689132   -0.0877865  -0.041972   97  MET   A HB3  
1209 H HG2  . MET   A 85  ? 0.345833 0.420455 0.354238 0.0443743   -0.0779723  -0.0328133  97  MET   A HG2  
1210 H HG3  . MET   A 85  ? 0.348786 0.395999 0.353384 0.0518519   -0.0730666  -0.0288928  97  MET   A HG3  
1211 H HE1  . MET   A 85  ? 0.319782 0.471276 0.383907 0.0163276   -0.0602028  -0.058133   97  MET   A HE1  
1212 H HE2  . MET   A 85  ? 0.331103 0.492223 0.393519 0.0389736   -0.0737052  -0.0561202  97  MET   A HE2  
1213 H HE3  . MET   A 85  ? 0.329852 0.465013 0.375496 0.0210119   -0.0709415  -0.0539028  97  MET   A HE3  
1214 N N    . LYS   A 86  ? 0.39446  0.531661 0.421632 0.109033    -0.117162   -0.027909   98  LYS   A N    
1215 C CA   . LYS   A 86  ? 0.422056 0.596854 0.465023 0.13145     -0.128051   -0.031519   98  LYS   A CA   
1216 C C    . LYS   A 86  ? 0.391481 0.618866 0.464802 0.124476    -0.122106   -0.0482853  98  LYS   A C    
1217 O O    . LYS   A 86  ? 0.370358 0.605634 0.450038 0.0991379   -0.111985   -0.055284   98  LYS   A O    
1218 C CB   . LYS   A 86  ? 0.483093 0.675859 0.515107 0.137142    -0.142302   -0.0234712  98  LYS   A CB   
1219 C CG   . LYS   A 86  ? 0.566278 0.709536 0.568954 0.148296    -0.148625   -0.00305067 98  LYS   A CG   
1220 C CD   . LYS   A 86  ? 0.671554 0.823595 0.65389  0.148485    -0.159549   0.00932433  98  LYS   A CD   
1221 C CE   . LYS   A 86  ? 0.729457 0.828158 0.683121 0.15498     -0.16242    0.0321006   98  LYS   A CE   
1222 N NZ   . LYS   A 86  ? 0.778275 0.888643 0.710404 0.160347    -0.174143   0.047816    98  LYS   A NZ   
1223 H H    . LYS   A 86  ? 0.391315 0.534393 0.413954 0.0957441   -0.116279   -0.028608   98  LYS   A H    
1224 H HA   . LYS   A 86  ? 0.44103  0.59561  0.480844 0.148436    -0.130414   -0.0275993  98  LYS   A HA   
1225 H HB2  . LYS   A 86  ? 0.470709 0.674915 0.500981 0.119746    -0.140081   -0.0275363  98  LYS   A HB2  
1226 H HB3  . LYS   A 86  ? 0.488585 0.715036 0.533628 0.150861    -0.149874   -0.0272538  98  LYS   A HB3  
1227 H HG2  . LYS   A 86  ? 0.589645 0.723061 0.594198 0.167877    -0.153572   0.00053352  98  LYS   A HG2  
1228 H HG3  . LYS   A 86  ? 0.564405 0.675658 0.557971 0.136629    -0.140222   -0.00042968 98  LYS   A HG3  
1229 H HD2  . LYS   A 86  ? 0.640139 0.802485 0.620067 0.130556    -0.155054   0.00370285  98  LYS   A HD2  
1230 H HD3  . LYS   A 86  ? 0.666385 0.850022 0.656161 0.162024    -0.169335   0.00809515  98  LYS   A HD3  
1231 H HE2  . LYS   A 86  ? 0.7462   0.825408 0.701974 0.170957    -0.165511   0.0360765   98  LYS   A HE2  
1232 H HE3  . LYS   A 86  ? 0.718977 0.793591 0.665277 0.139404    -0.153223   0.0330259   98  LYS   A HE3  
1233 H HZ1  . LYS   A 86  ? 0.776749 0.918138 0.717012 0.172528    -0.182702   0.0447048   98  LYS   A HZ1  
1234 H HZ2  . LYS   A 86  ? 0.759313 0.878612 0.68472  0.144988    -0.170201   0.0452437   98  LYS   A HZ2  
1235 H HZ3  . LYS   A 86  ? 0.797194 0.875943 0.713713 0.166954    -0.177005   0.0634793   98  LYS   A HZ3  
1236 N N    . LYS   A 87  ? 0.403285 0.66753  0.495201 0.147793    -0.128669   -0.0537578  99  LYS   A N    
1237 C CA   . LYS   A 87  ? 0.403122 0.730257 0.526356 0.141909    -0.124296   -0.0684694  99  LYS   A CA   
1238 C C    . LYS   A 87  ? 0.381265 0.74421  0.511953 0.116421    -0.127251   -0.0736817  99  LYS   A C    
1239 O O    . LYS   A 87  ? 0.364366 0.734117 0.48468  0.120974    -0.140197   -0.0691696  99  LYS   A O    
1240 C CB   . LYS   A 87  ? 0.456308 0.827357 0.598413 0.174918    -0.133661   -0.0734207  99  LYS   A CB   
1241 C CG   . LYS   A 87  ? 0.467815 0.904901 0.643493 0.169355    -0.125146   -0.0885577  99  LYS   A CG   
1242 C CD   . LYS   A 87  ? 0.506805 0.997722 0.703841 0.204776    -0.134199   -0.0953591  99  LYS   A CD   
1243 C CE   . LYS   A 87  ? 0.510012 1.06435  0.738397 0.197044    -0.121899   -0.109524   99  LYS   A CE   
1244 N NZ   . LYS   A 87  ? 0.535585 1.15238  0.787708 0.232413    -0.129527   -0.118249   99  LYS   A NZ   
1245 H H    . LYS   A 87  ? 0.426859 0.677366 0.511802 0.16814     -0.136064   -0.0477579  99  LYS   A H    
1246 H HA   . LYS   A 87  ? 0.392252 0.712049 0.519866 0.132011    -0.112889   -0.0725671  99  LYS   A HA   
1247 H HB2  . LYS   A 87  ? 0.468803 0.807965 0.601377 0.193933    -0.13457    -0.0696449  99  LYS   A HB2  
1248 H HB3  . LYS   A 87  ? 0.463016 0.852532 0.604285 0.182713    -0.145098   -0.0701892  99  LYS   A HB3  
1249 H HG2  . LYS   A 87  ? 0.453096 0.917981 0.638024 0.147502    -0.124193   -0.0920968  99  LYS   A HG2  
1250 H HG3  . LYS   A 87  ? 0.458581 0.878259 0.633314 0.162635    -0.113791   -0.0908489  99  LYS   A HG3  
1251 H HD2  . LYS   A 87  ? 0.524712 0.982179 0.710224 0.228599    -0.13719    -0.0918193  99  LYS   A HD2  
1252 H HD3  . LYS   A 87  ? 0.511653 1.03081  0.713085 0.209409    -0.145311   -0.0939573  99  LYS   A HD3  
1253 H HE2  . LYS   A 87  ? 0.492482 1.07519  0.731635 0.170831    -0.118767   -0.112114   99  LYS   A HE2  
1254 H HE3  . LYS   A 87  ? 0.502788 1.03072  0.725195 0.193513    -0.111199   -0.110619   99  LYS   A HE3  
1255 H HZ1  . LYS   A 87  ? 0.534464 1.18356  0.794447 0.234453    -0.139361   -0.11778    99  LYS   A HZ1  
1256 H HZ2  . LYS   A 87  ? 0.550617 1.13687  0.791555 0.258235    -0.133647   -0.11607    99  LYS   A HZ2  
1257 H HZ3  . LYS   A 87  ? 0.521804 1.17736  0.791997 0.227222    -0.120524   -0.126541   99  LYS   A HZ3  
1258 N N    . GLY   A 88  ? 0.359494 0.739249 0.504941 0.0884903   -0.114881   -0.0826112  100 GLY   A N    
1259 C CA   . GLY   A 88  ? 0.356136 0.767104 0.511766 0.06041     -0.11638    -0.091062   100 GLY   A CA   
1260 C C    . GLY   A 88  ? 0.344231 0.705569 0.475766 0.038505    -0.112695   -0.0880487  100 GLY   A C    
1261 O O    . GLY   A 88  ? 0.343574 0.718138 0.480421 0.0132439   -0.112582   -0.0969946  100 GLY   A O    
1262 H H    . GLY   A 88  ? 0.354333 0.723804 0.502712 0.0865108   -0.105273   -0.0833483  100 GLY   A H    
1263 H HA2  . GLY   A 88  ? 0.344496 0.78187  0.518573 0.0476575   -0.10893    -0.0973956  100 GLY   A HA2  
1264 H HA3  . GLY   A 88  ? 0.360428 0.803071 0.521448 0.0684207   -0.127696   -0.0934906  100 GLY   A HA3  
1265 N N    . GLU   A 89  ? 0.335152 0.640819 0.440508 0.0484816   -0.110318   -0.0765344  101 GLU   A N    
1266 C CA   . GLU   A 89  ? 0.335954 0.598114 0.418218 0.0324649   -0.106096   -0.073358   101 GLU   A CA   
1267 C C    . GLU   A 89  ? 0.324822 0.570744 0.412914 0.00924841  -0.0911554  -0.0775959  101 GLU   A C    
1268 O O    . GLU   A 89  ? 0.284247 0.532231 0.383701 0.0103817   -0.081416   -0.0763145  101 GLU   A O    
1269 C CB   . GLU   A 89  ? 0.342088 0.55664  0.398704 0.0480623   -0.106242   -0.0589     101 GLU   A CB   
1270 C CG   . GLU   A 89  ? 0.337864 0.513265 0.370915 0.0348096   -0.100989   -0.0547729  101 GLU   A CG   
1271 C CD   . GLU   A 89  ? 0.348125 0.485618 0.358554 0.0475233   -0.101789   -0.0394537  101 GLU   A CD   
1272 O OE1  . GLU   A 89  ? 0.352218 0.491697 0.356542 0.0659536   -0.11218    -0.030328   101 GLU   A OE1  
1273 O OE2  . GLU   A 89  ? 0.345607 0.451307 0.344447 0.0385954   -0.0922538  -0.0357044  101 GLU   A OE2  
1274 H H    . GLU   A 89  ? 0.342687 0.638121 0.444842 0.066055    -0.1114     -0.0709466  101 GLU   A H    
1275 H HA   . GLU   A 89  ? 0.342259 0.617835 0.421299 0.0265472   -0.113158   -0.0777705  101 GLU   A HA   
1276 H HB2  . GLU   A 89  ? 0.3539   0.576086 0.405479 0.062531    -0.115935   -0.0541131  101 GLU   A HB2  
1277 H HB3  . GLU   A 89  ? 0.337493 0.540147 0.397642 0.0539911   -0.100399   -0.0564455  101 GLU   A HB3  
1278 H HG2  . GLU   A 89  ? 0.329993 0.494406 0.366763 0.0229996   -0.0916902  -0.0580603  101 GLU   A HG2  
1279 H HG3  . GLU   A 89  ? 0.344786 0.531926 0.373324 0.0289915   -0.106295   -0.0591744  101 GLU   A HG3  
1280 N N    . ILE   A 90  ? 0.321944 0.550815 0.399888 -0.0100584  -0.0899179  -0.0825958  102 ILE   A N    
1281 C CA   . ILE   A 90  ? 0.310364 0.506695 0.384315 -0.0279277  -0.0768382  -0.082395   102 ILE   A CA   
1282 C C    . ILE   A 90  ? 0.307989 0.460056 0.354214 -0.0241177  -0.075417   -0.0766421  102 ILE   A C    
1283 O O    . ILE   A 90  ? 0.322876 0.4749   0.355681 -0.0230748  -0.0836891  -0.0806714  102 ILE   A O    
1284 C CB   . ILE   A 90  ? 0.327595 0.538375 0.415344 -0.0543664  -0.0754694  -0.0942776  102 ILE   A CB   
1285 C CG1  . ILE   A 90  ? 0.334638 0.599952 0.452958 -0.060637   -0.0761474  -0.0993429  102 ILE   A CG1  
1286 C CG2  . ILE   A 90  ? 0.349923 0.517623 0.429205 -0.0699091  -0.0627056  -0.0910352  102 ILE   A CG2  
1287 C CD1  . ILE   A 90  ? 0.354771 0.641484 0.489001 -0.090472   -0.0777012  -0.111885   102 ILE   A CD1  
1288 H H    . ILE   A 90  ? 0.329782 0.56731  0.402358 -0.0108059  -0.0977869  -0.0864739  102 ILE   A H    
1289 H HA   . ILE   A 90  ? 0.304061 0.498345 0.383893 -0.0246966  -0.0698345  -0.0777784  102 ILE   A HA   
1290 H HB   . ILE   A 90  ? 0.340917 0.554652 0.422311 -0.0572245  -0.0831903  -0.101077   102 ILE   A HB   
1291 H HG12 . ILE   A 90  ? 0.325748 0.589733 0.449872 -0.0592857  -0.0674494  -0.0936798  102 ILE   A HG12 
1292 H HG13 . ILE   A 90  ? 0.330773 0.621743 0.453223 -0.045826   -0.0843652  -0.0999409  102 ILE   A HG13 
1293 H HG21 . ILE   A 90  ? 0.354671 0.528687 0.443859 -0.0877549  -0.0612517  -0.0970192  102 ILE   A HG21 
1294 H HG22 . ILE   A 90  ? 0.335258 0.497392 0.416141 -0.0647112  -0.055377   -0.0831417  102 ILE   A HG22 
1295 H HG23 . ILE   A 90  ? 0.349787 0.490089 0.411707 -0.0667786  -0.0635847  -0.0907835  102 ILE   A HG23 
1296 H HD11 . ILE   A 90  ? 0.362834 0.649919 0.489876 -0.0922736  -0.0865529  -0.119427   102 ILE   A HD11 
1297 H HD12 . ILE   A 90  ? 0.35     0.678265 0.5048   -0.0935494  -0.0784745  -0.114506   102 ILE   A HD12 
1298 H HD13 . ILE   A 90  ? 0.359599 0.618993 0.490451 -0.105031   -0.0693135  -0.109976   102 ILE   A HD13 
1299 N N    . ALA   A 91  ? 0.293775 0.415026 0.332076 -0.0216063  -0.0650214  -0.0677946  103 ALA   A N    
1300 C CA   . ALA   A 91  ? 0.300228 0.386375 0.315157 -0.0175693  -0.0623761  -0.0615011  103 ALA   A CA   
1301 C C    . ALA   A 91  ? 0.304155 0.363618 0.315895 -0.02866    -0.0507974  -0.0607844  103 ALA   A C    
1302 O O    . ALA   A 91  ? 0.307425 0.371078 0.332346 -0.0358729  -0.0434532  -0.059549   103 ALA   A O    
1303 C CB   . ALA   A 91  ? 0.295609 0.372167 0.302263 -0.00116611 -0.0635377  -0.0499588  103 ALA   A CB   
1304 H H    . ALA   A 91  ? 0.290166 0.415982 0.338108 -0.0224382  -0.0594251  -0.0659358  103 ALA   A H    
1305 H HA   . ALA   A 91  ? 0.308925 0.396716 0.315287 -0.0184237  -0.0679756  -0.0656201  103 ALA   A HA   
1306 H HB1  . ALA   A 91  ? 0.300292 0.390541 0.307652 0.00699773  -0.071478   -0.0490941  103 ALA   A HB1  
1307 H HB2  . ALA   A 91  ? 0.289045 0.364968 0.303388 0.0003816   -0.0585902  -0.048089   103 ALA   A HB2  
1308 H HB3  . ALA   A 91  ? 0.297088 0.354714 0.289551 -0.00028543 -0.0615228  -0.0452987  103 ALA   A HB3  
1309 N N    . HIS   A 92  ? 0.299591 0.33466  0.293198 -0.0286446  -0.0492371  -0.0610282  104 HIS   A N    
1310 C CA   . HIS   A 92  ? 0.30673  0.31382  0.293449 -0.0323515  -0.0392878  -0.0575273  104 HIS   A CA   
1311 C C    . HIS   A 92  ? 0.312277 0.308663 0.286421 -0.0204878  -0.0359004  -0.0465072  104 HIS   A C    
1312 O O    . HIS   A 92  ? 0.314883 0.314995 0.277926 -0.0130415  -0.0410903  -0.0441382  104 HIS   A O    
1313 C CB   . HIS   A 92  ? 0.332948 0.321574 0.309418 -0.0384415  -0.0399698  -0.0677968  104 HIS   A CB   
1314 C CG   . HIS   A 92  ? 0.351031 0.340359 0.340014 -0.0555579  -0.0413413  -0.078348   104 HIS   A CG   
1315 N ND1  . HIS   A 92  ? 0.38678  0.354962 0.367565 -0.0632012  -0.0434755  -0.0913335  104 HIS   A ND1  
1316 C CD2  . HIS   A 92  ? 0.356784 0.365998 0.36609  -0.0679393  -0.0407228  -0.0785714  104 HIS   A CD2  
1317 C CE1  . HIS   A 92  ? 0.409268 0.380978 0.405153 -0.0826082  -0.0447614  -0.0986653  104 HIS   A CE1  
1318 N NE2  . HIS   A 92  ? 0.398201 0.398352 0.412475 -0.0863232  -0.0425219  -0.0900837  104 HIS   A NE2  
1319 H H    . HIS   A 92  ? 0.308781 0.346985 0.293651 -0.0248971  -0.0547075  -0.0633228  104 HIS   A H    
1320 H HA   . HIS   A 92  ? 0.308235 0.316614 0.30519  -0.0384199  -0.0345256  -0.0557439  104 HIS   A HA   
1321 H HB2  . HIS   A 92  ? 0.335207 0.330174 0.302894 -0.0332737  -0.0454366  -0.0715994  104 HIS   A HB2  
1322 H HB3  . HIS   A 92  ? 0.335205 0.30456  0.303937 -0.0356806  -0.0342342  -0.0639645  104 HIS   A HB3  
1324 H HD2  . HIS   A 92  ? 0.343811 0.37044  0.36235  -0.0649035  -0.0392478  -0.0726703  104 HIS   A HD2  
1325 H HE1  . HIS   A 92  ? 0.432217 0.388828 0.426054 -0.0923826  -0.0468024  -0.108813   104 HIS   A HE1  
1327 N N    . LEU   A 93  ? 0.306367 0.292897 0.282398 -0.0203621  -0.0275293  -0.0392288  105 LEU   A N    
1328 C CA   . LEU   A 93  ? 0.322194 0.300369 0.28744  -0.0124751  -0.0241977  -0.0305253  105 LEU   A CA   
1329 C C    . LEU   A 93  ? 0.342177 0.303405 0.300013 -0.0127388  -0.0165905  -0.0278577  105 LEU   A C    
1330 O O    . LEU   A 93  ? 0.354924 0.308203 0.318416 -0.0188529  -0.011618   -0.0275411  105 LEU   A O    
1331 C CB   . LEU   A 93  ? 0.303418 0.288592 0.275436 -0.00908205 -0.0227383  -0.0254337  105 LEU   A CB   
1332 C CG   . LEU   A 93  ? 0.295128 0.293811 0.27508  -0.00395374 -0.0301155  -0.0273457  105 LEU   A CG   
1333 C CD1  . LEU   A 93  ? 0.296248 0.296648 0.280867 0.00141937  -0.0278055  -0.0256709  105 LEU   A CD1  
1334 C CD2  . LEU   A 93  ? 0.304704 0.299761 0.272897 0.00103407  -0.0378777  -0.0239132  105 LEU   A CD2  
1335 H H    . LEU   A 93  ? 0.311943 0.299334 0.296222 -0.0263108  -0.0239372  -0.0396573  105 LEU   A H    
1336 H HA   . LEU   A 93  ? 0.319801 0.299384 0.277037 -0.00865548 -0.0281475  -0.0299482  105 LEU   A HA   
1337 H HB2  . LEU   A 93  ? 0.302758 0.28916  0.280843 -0.0125885  -0.0177482  -0.0252599  105 LEU   A HB2  
1338 H HB3  . LEU   A 93  ? 0.301536 0.280856 0.265917 -0.00598275 -0.0213206  -0.0208244  105 LEU   A HB3  
1339 H HG   . LEU   A 93  ? 0.299266 0.309422 0.288603 -0.0071224  -0.0316527  -0.0323049  105 LEU   A HG   
1340 H HD11 . LEU   A 93  ? 0.291526 0.297883 0.282354 -0.00194186 -0.022269   -0.0270217  105 LEU   A HD11 
1341 H HD12 . LEU   A 93  ? 0.297255 0.304377 0.286849 0.00708107  -0.0328488  -0.0276207  105 LEU   A HD12 
1342 H HD13 . LEU   A 93  ? 0.294963 0.284698 0.270918 0.00276854  -0.0270121  -0.0216809  105 LEU   A HD13 
1343 H HD21 . LEU   A 93  ? 0.307968 0.307176 0.274136 -0.0012592  -0.0402834  -0.0274423  105 LEU   A HD21 
1344 H HD22 . LEU   A 93  ? 0.303767 0.289603 0.262882 0.0012013   -0.035662   -0.0190585  105 LEU   A HD22 
1345 H HD23 . LEU   A 93  ? 0.306364 0.305285 0.277575 0.00638452  -0.0427959  -0.0228508  105 LEU   A HD23 
1346 N N    . LEU   A 94  ? 0.337328 0.295124 0.282591 -0.00579831 -0.015689   -0.0245193  106 LEU   A N    
1347 C CA   . LEU   A 94  ? 0.340398 0.28791  0.278468 -0.00089087 -0.00930488 -0.0204334  106 LEU   A CA   
1348 C C    . LEU   A 94  ? 0.355008 0.314217 0.290034 0.00277585  -0.00787382 -0.0123261  106 LEU   A C    
1349 O O    . LEU   A 94  ? 0.307664 0.27653  0.23853  0.00305712  -0.0116343  -0.0108665  106 LEU   A O    
1350 C CB   . LEU   A 94  ? 0.370612 0.309962 0.29742  0.005665    -0.00949844 -0.0266456  106 LEU   A CB   
1351 C CG   . LEU   A 94  ? 0.370922 0.296506 0.291162 0.0145789   -0.00359495 -0.0233723  106 LEU   A CG   
1352 C CD1  . LEU   A 94  ? 0.385365 0.286691 0.31021  0.00888293  -0.00042455 -0.0217973  106 LEU   A CD1  
1353 C CD2  . LEU   A 94  ? 0.417223 0.339638 0.325611 0.0258963   -0.00395726 -0.0314556  106 LEU   A CD2  
1354 H H    . LEU   A 94  ? 0.335834 0.300274 0.27684  -0.00359986 -0.0193307  -0.0241378  106 LEU   A H    
1355 H HA   . LEU   A 94  ? 0.352308 0.292165 0.294774 -0.00392089 -0.00591769 -0.0188685  106 LEU   A HA   
1356 H HB2  . LEU   A 94  ? 0.374351 0.306804 0.302584 0.00177952  -0.0120773  -0.0340677  106 LEU   A HB2  
1357 H HB3  . LEU   A 94  ? 0.359982 0.311236 0.281494 0.00879056  -0.0115031  -0.0262386  106 LEU   A HB3  
1358 H HG   . LEU   A 94  ? 0.367739 0.303859 0.287936 0.0173893   -0.0014416  -0.0161515  106 LEU   A HG   
1359 H HD11 . LEU   A 94  ? 0.375372 0.283471 0.306634 0.00386474  0.00131481  -0.0156146  106 LEU   A HD11 
1360 H HD12 . LEU   A 94  ? 0.400235 0.288745 0.318829 0.0164543   0.00237651  -0.0194187  106 LEU   A HD12 
1361 H HD13 . LEU   A 94  ? 0.395771 0.288472 0.322989 0.00251735  -0.00303199 -0.0291756  106 LEU   A HD13 
1362 H HD21 . LEU   A 94  ? 0.398624 0.339993 0.303787 0.0284174   -0.00493798 -0.0304942  106 LEU   A HD21 
1363 H HD22 . LEU   A 94  ? 0.420624 0.332441 0.327885 0.0230001   -0.00665529 -0.040373   106 LEU   A HD22 
1364 H HD23 . LEU   A 94  ? 0.418298 0.331573 0.32293  0.0339702   -0.00063194 -0.0290457  106 LEU   A HD23 
1365 N N    . ILE   A 95  ? 0.332284 0.291298 0.268808 0.00387176  -0.00284519 -0.00657542 107 ILE   A N    
1366 C CA   . ILE   A 95  ? 0.319428 0.290964 0.255786 0.0036604   -0.00277096 -0.00193978 107 ILE   A CA   
1367 C C    . ILE   A 95  ? 0.322309 0.300823 0.252568 0.00980409  0.00146459  0.00368585  107 ILE   A C    
1368 O O    . ILE   A 95  ? 0.341186 0.313567 0.270647 0.0131825   0.00575306  0.00744576  107 ILE   A O    
1369 C CB   . ILE   A 95  ? 0.313034 0.286815 0.257994 -0.00041052 -0.00214793 -0.00296945 107 ILE   A CB   
1370 C CG1  . ILE   A 95  ? 0.333505 0.306505 0.286484 -0.00336464 -0.00709944 -0.00871488 107 ILE   A CG1  
1371 C CG2  . ILE   A 95  ? 0.292256 0.275731 0.235398 -0.0006282  -0.0026973  -0.00173862 107 ILE   A CG2  
1372 C CD1  . ILE   A 95  ? 0.342229 0.322433 0.306233 -0.00590996 -0.00438535 -0.0112457  107 ILE   A CD1  
1373 H H    . ILE   A 95  ? 0.343807 0.294251 0.280639 0.00426519  0.00027022  -0.00562197 107 ILE   A H    
1374 H HA   . ILE   A 95  ? 0.317227 0.293165 0.251739 0.00236255  -0.00622967 -0.00227372 107 ILE   A HA   
1375 H HB   . ILE   A 95  ? 0.318543 0.289684 0.264749 -0.0005501  0.00187915  -0.00107425 107 ILE   A HB   
1376 H HG12 . ILE   A 95  ? 0.328406 0.302651 0.28006  -0.00268615 -0.0111055  -0.00896096 107 ILE   A HG12 
1377 H HG13 . ILE   A 95  ? 0.334664 0.303406 0.286771 -0.00397763 -0.00845796 -0.0106995  107 ILE   A HG13 
1378 H HG21 . ILE   A 95  ? 0.295936 0.280899 0.243867 -0.00164106 -0.00325422 -0.00485983 107 ILE   A HG21 
1379 H HG22 . ILE   A 95  ? 0.296703 0.280706 0.236861 -0.00183093 -0.00603952 -0.00150328 107 ILE   A HG22 
1380 H HG23 . ILE   A 95  ? 0.297793 0.286269 0.237603 0.00137661  0.00060717  0.00159547  107 ILE   A HG23 
1381 H HD11 . ILE   A 95  ? 0.342949 0.320754 0.307392 -0.00846221 0.0001001   -0.00887841 107 ILE   A HD11 
1382 H HD12 . ILE   A 95  ? 0.338989 0.322448 0.309199 -0.00672625 -0.00790834 -0.0152071  107 ILE   A HD12 
1383 H HD13 . ILE   A 95  ? 0.335859 0.321487 0.300039 -0.00409324 -0.00364153 -0.011343   107 ILE   A HD13 
1384 N N    . LYS   A 96  ? 0.315327 0.309373 0.241611 0.0104599   4.625e-05   0.00567492  108 LYS   A N    
1385 C CA   . LYS   A 96  ? 0.307896 0.31877  0.230612 0.0163715   0.0027838   0.0104894   108 LYS   A CA   
1386 C C    . LYS   A 96  ? 0.3237   0.34192  0.248799 0.0123567   0.00314464  0.0120633   108 LYS   A C    
1387 O O    . LYS   A 96  ? 0.299479 0.312031 0.228719 0.00490358  0.00084741  0.00801623  108 LYS   A O    
1388 C CB   . LYS   A 96  ? 0.344485 0.378319 0.264968 0.014128    0.00110148  0.0117187   108 LYS   A CB   
1389 C CG   . LYS   A 96  ? 0.349627 0.385296 0.265436 0.0199613   0.0016472   0.00947694  108 LYS   A CG   
1390 C CD   . LYS   A 96  ? 0.409179 0.476408 0.322799 0.0178328   0.00198943  0.0123482   108 LYS   A CD   
1391 C CE   . LYS   A 96  ? 0.432759 0.508147 0.339905 0.0267785   0.00379787  0.00864223  108 LYS   A CE   
1392 N NZ   . LYS   A 96  ? 0.46622  0.57651  0.37231  0.0190148   0.00452717  0.0135931   108 LYS   A NZ   
1393 H H    . LYS   A 96  ? 0.312748 0.309117 0.238689 0.00665947  -0.00290145 0.00462343  108 LYS   A H    
1394 H HA   . LYS   A 96  ? 0.327905 0.332965 0.247792 0.0244725   0.00537421  0.0118578   108 LYS   A HA   
1395 H HB2  . LYS   A 96  ? 0.331266 0.365371 0.253603 0.00489809  -0.00178455 0.0112985   108 LYS   A HB2  
1396 H HB3  . LYS   A 96  ? 0.334213 0.384118 0.254091 0.0176505   0.00240267  0.0143444   108 LYS   A HB3  
1397 H HG2  . LYS   A 96  ? 0.370268 0.399402 0.28376  0.0299051   0.00397356  0.00819642  108 LYS   A HG2  
1398 H HG3  . LYS   A 96  ? 0.362499 0.385693 0.278456 0.0156345   -0.0005396  0.00691938  108 LYS   A HG3  
1399 H HD2  . LYS   A 96  ? 0.394729 0.463487 0.309623 0.00628357  -0.00059405 0.0145539   108 LYS   A HD2  
1400 H HD3  . LYS   A 96  ? 0.396351 0.480312 0.311387 0.0215527   0.00351134  0.014538    108 LYS   A HD3  
1401 H HE2  . LYS   A 96  ? 0.44344  0.519473 0.34879  0.0394907   0.00625749  0.00609319  108 LYS   A HE2  
1402 H HE3  . LYS   A 96  ? 0.439342 0.498246 0.344365 0.0247805   0.00193188  0.00544248  108 LYS   A HE3  
1403 H HZ1  . LYS   A 96  ? 0.451672 0.579884 0.361242 0.0188484   0.00564763  0.016187    108 LYS   A HZ1  
1404 H HZ2  . LYS   A 96  ? 0.453161 0.557953 0.359317 0.00732969  0.00194089  0.0167875   108 LYS   A HZ2  
1405 H HZ3  . LYS   A 96  ? 0.460713 0.581577 0.362328 0.0258087   0.00639476  0.0109937   108 LYS   A HZ3  
1406 N N    . PRO   A 97  ? 0.283509 0.316544 0.204994 0.0193565   0.00559122  0.0171314   109 PRO   A N    
1407 C CA   . PRO   A 97  ? 0.299629 0.342963 0.220587 0.017045    0.00620377  0.0179414   109 PRO   A CA   
1408 C C    . PRO   A 97  ? 0.302511 0.357178 0.225906 0.00589137  0.00153959  0.0106476   109 PRO   A C    
1409 O O    . PRO   A 97  ? 0.308327 0.364239 0.231755 0.00277989  0.00129646  0.0059327   109 PRO   A O    
1410 C CB   . PRO   A 97  ? 0.321482 0.382571 0.236303 0.0289007   0.00821286  0.026047    109 PRO   A CB   
1411 C CG   . PRO   A 97  ? 0.321771 0.386176 0.235415 0.0384016   0.00824037  0.0277333   109 PRO   A CG   
1412 C CD   . PRO   A 97  ? 0.324671 0.366713 0.241326 0.0326072   0.00759725  0.0218131   109 PRO   A CD   
1413 H HA   . PRO   A 97  ? 0.30273  0.334139 0.224741 0.016462    0.00835732  0.0182589   109 PRO   A HA   
1414 H HB2  . PRO   A 97  ? 0.314764 0.3961   0.228977 0.0264718   0.00631509  0.0249364   109 PRO   A HB2  
1415 H HB3  . PRO   A 97  ? 0.325567 0.377472 0.237273 0.0335497   0.011224    0.0312334   109 PRO   A HB3  
1416 H HG2  . PRO   A 97  ? 0.319207 0.406937 0.234084 0.0371809   0.00628331  0.0267999   109 PRO   A HG2  
1417 H HG3  . PRO   A 97  ? 0.335063 0.393925 0.244403 0.0496288   0.0104207   0.0331867   109 PRO   A HG3  
1418 H HD2  . PRO   A 97  ? 0.313614 0.367111 0.230711 0.0320406   0.00628874  0.0199585   109 PRO   A HD2  
1419 H HD3  . PRO   A 97  ? 0.324868 0.34866  0.239432 0.0384054   0.00953539  0.0227646   109 PRO   A HD3  
1420 N N    . GLU   A 98  ? 0.312361 0.374184 0.237009 -0.0007933  -0.00208099 0.0092449   110 GLU   A N    
1421 C CA   . GLU   A 98  ? 0.32505  0.388363 0.251107 -0.0143423  -0.00737606 0.00302577  110 GLU   A CA   
1422 C C    . GLU   A 98  ? 0.315404 0.351119 0.243638 -0.017714   -0.00987613 -0.00340043 110 GLU   A C    
1423 O O    . GLU   A 98  ? 0.317376 0.347942 0.24515  -0.0247292  -0.0140237  -0.0111201  110 GLU   A O    
1424 C CB   . GLU   A 98  ? 0.374956 0.447656 0.30168  -0.0236768  -0.00987355 0.00622385  110 GLU   A CB   
1425 C CG   . GLU   A 98  ? 0.41586  0.526712 0.342997 -0.0216763  -0.00844837 0.0102748   110 GLU   A CG   
1426 C CD   . GLU   A 98  ? 0.450737 0.57245  0.376373 -0.0042309  -0.00347083 0.0160686   110 GLU   A CD   
1427 O OE1  . GLU   A 98  ? 0.344596 0.442854 0.268204 0.0041341   -0.00099028 0.0167802   110 GLU   A OE1  
1428 O OE2  . GLU   A 98  ? 0.51193  0.668556 0.438477 0.00162287  -0.00285921 0.0186961   110 GLU   A OE2  
1429 H H    . GLU   A 98  ? 0.311832 0.37693  0.235908 0.00271147  -0.00115399 0.0123177   110 GLU   A H    
1430 H HA   . GLU   A 98  ? 0.331215 0.409042 0.255937 -0.0155222  -0.00807395 0.00067592  110 GLU   A HA   
1431 H HB2  . GLU   A 98  ? 0.370469 0.433138 0.296889 -0.0208076  -0.00883356 0.00891959  110 GLU   A HB2  
1432 H HB3  . GLU   A 98  ? 0.378731 0.443915 0.305786 -0.0342935  -0.0137133  0.00299822  110 GLU   A HB3  
1433 H HG2  . GLU   A 98  ? 0.417062 0.53758  0.345698 -0.0325197  -0.0104884  0.0111      110 GLU   A HG2  
1434 H HG3  . GLU   A 98  ? 0.414599 0.537254 0.341363 -0.0214398  -0.00933777 0.00777005  110 GLU   A HG3  
1435 N N    . TYR   A 99  ? 0.294512 0.313625 0.225257 -0.0120599  -0.00814283 -0.00175895 111 TYR   A N    
1436 C CA   . TYR   A 99  ? 0.319771 0.319946 0.254441 -0.0121298  -0.0109269  -0.0076105  111 TYR   A CA   
1437 C C    . TYR   A 99  ? 0.329685 0.332996 0.268279 -0.00543786 -0.00602916 -0.0101205  111 TYR   A C    
1438 O O    . TYR   A 99  ? 0.309674 0.305184 0.254264 -0.00308458 -0.00700184 -0.0147181  111 TYR   A O    
1439 C CB   . TYR   A 99  ? 0.317977 0.304731 0.253306 -0.0127952  -0.0140418  -0.00407144 111 TYR   A CB   
1440 C CG   . TYR   A 99  ? 0.350581 0.335672 0.280845 -0.0219587  -0.0183212  0.00055592  111 TYR   A CG   
1441 C CD1  . TYR   A 99  ? 0.328438 0.332262 0.255239 -0.0246724  -0.0157022  0.00675135  111 TYR   A CD1  
1442 C CD2  . TYR   A 99  ? 0.347421 0.312808 0.276078 -0.0279613  -0.0248106  -0.0005785  111 TYR   A CD2  
1443 C CE1  . TYR   A 99  ? 0.351708 0.360634 0.274775 -0.0360786  -0.0183675  0.0124916   111 TYR   A CE1  
1444 C CE2  . TYR   A 99  ? 0.377388 0.338815 0.300531 -0.0399498  -0.028298   0.00658809  111 TYR   A CE2  
1445 C CZ   . TYR   A 99  ? 0.374752 0.361011 0.295657 -0.0457381  -0.0245657  0.0134988   111 TYR   A CZ   
1446 O OH   . TYR   A 99  ? 0.368576 0.356234 0.284979 -0.0606594  -0.0270484  0.021688    111 TYR   A OH   
1447 H H    . TYR   A 99  ? 0.300325 0.321144 0.23053  -0.00758606 -0.00560895 0.00235772  111 TYR   A H    
1448 H HA   . TYR   A 99  ? 0.324822 0.320983 0.258529 -0.0163749  -0.0144096  -0.0123234  111 TYR   A HA   
1449 H HB2  . TYR   A 99  ? 0.318759 0.309123 0.254045 -0.00928995 -0.0111294  -0.00121298 111 TYR   A HB2  
1450 H HB3  . TYR   A 99  ? 0.326618 0.303582 0.265291 -0.0106688  -0.0162359  -0.00752266 111 TYR   A HB3  
1451 H HD1  . TYR   A 99  ? 0.329041 0.343189 0.256067 -0.018485   -0.0118531  0.00735782  111 TYR   A HD1  
1452 H HD2  . TYR   A 99  ? 0.360022 0.313971 0.29116  -0.023607   -0.0268301  -0.00572974 111 TYR   A HD2  
1453 H HE1  . TYR   A 99  ? 0.346714 0.37409  0.268507 -0.0372439  -0.0159423  0.0161745   111 TYR   A HE1  
1454 H HE2  . TYR   A 99  ? 0.390238 0.332992 0.311154 -0.0442552  -0.03304    0.00692846  111 TYR   A HE2  
1456 N N    . ALA   A 100 ? 0.30152  0.319516 0.236718 -0.00225502 -0.00071798 -0.00580807 112 ALA   A N    
1457 C CA   . ALA   A 100 ? 0.298731 0.321585 0.235875 0.00132977  0.00520506  -0.00419246 112 ALA   A CA   
1458 C C    . ALA   A 100 ? 0.306772 0.35002  0.236978 0.00317182  0.00759647  -0.00424431 112 ALA   A C    
1459 O O    . ALA   A 100 ? 0.342797 0.392307 0.272209 0.00164264  0.00472305  -0.0147739  112 ALA   A O    
1460 C CB   . ALA   A 100 ? 0.294727 0.308391 0.232351 0.0032841   0.00933898  0.00468091  112 ALA   A CB   
1461 H H    . ALA   A 100 ? 0.306507 0.333191 0.237869 -0.00247841 -0.00081638 -0.00282757 112 ALA   A H    
1462 H HA   . ALA   A 100 ? 0.299592 0.319363 0.241942 0.00092315  0.00438896  -0.00987686 112 ALA   A HA   
1463 H HB1  . ALA   A 100 ? 0.294696 0.298602 0.237046 0.00149383  0.00749788  0.00220557  112 ALA   A HB1  
1464 H HB2  . ALA   A 100 ? 0.297716 0.311871 0.230599 0.00597976  0.0091928   0.00904896  112 ALA   A HB2  
1465 H HB3  . ALA   A 100 ? 0.300814 0.318087 0.238339 0.00369427  0.0137741   0.00827501  112 ALA   A HB3  
1466 N N    . TYR   A 101 ? 0.321151 0.373893 0.244875 0.00764052  0.0119645   0.0066932   113 TYR   A N    
1467 C CA   . TYR   A 101 ? 0.294534 0.371224 0.209965 0.0105583   0.0143513   0.00818363  113 TYR   A CA   
1468 C C    . TYR   A 101 ? 0.293783 0.388527 0.201988 0.0141037   0.0110896   0.0123318   113 TYR   A C    
1469 O O    . TYR   A 101 ? 0.271542 0.39057  0.171161 0.0178925   0.0118932   0.0149459   113 TYR   A O    
1470 C CB   . TYR   A 101 ? 0.317177 0.395934 0.22932  0.0132749   0.0224361   0.0200315   113 TYR   A CB   
1471 C CG   . TYR   A 101 ? 0.312211 0.386456 0.233696 0.00820017  0.0261948   0.014843    113 TYR   A CG   
1472 C CD1  . TYR   A 101 ? 0.301985 0.396244 0.224268 0.0082621   0.0275054   0.00375294  113 TYR   A CD1  
1473 C CD2  . TYR   A 101 ? 0.311096 0.364748 0.241318 0.00403136  0.0277828   0.0186812   113 TYR   A CD2  
1474 C CE1  . TYR   A 101 ? 0.296194 0.395001 0.228723 0.00596137  0.0314295   -0.00114838 113 TYR   A CE1  
1475 C CE2  . TYR   A 101 ? 0.287165 0.344932 0.228394 -0.00102755 0.0305034   0.0134161   113 TYR   A CE2  
1476 C CZ   . TYR   A 101 ? 0.299965 0.38241  0.243199 0.00069446  0.0326991   0.00416222  113 TYR   A CZ   
1477 O OH   . TYR   A 101 ? 0.276125 0.370619 0.232181 -0.00195852 0.0356426   -0.00180516 113 TYR   A OH   
1478 H H    . TYR   A 101 ? 0.311124 0.355412 0.234498 0.00987627  0.0131507   0.0131992   113 TYR   A H    
1479 H HA   . TYR   A 101 ? 0.303173 0.385775 0.219533 0.00808852  0.0125369   -0.00200735 113 TYR   A HA   
1480 H HB2  . TYR   A 101 ? 0.317486 0.38422  0.228267 0.0158181   0.0237917   0.0294857   113 TYR   A HB2  
1481 H HB3  . TYR   A 101 ? 0.319219 0.416304 0.223877 0.0159159   0.0239084   0.0224332   113 TYR   A HB3  
1482 H HD1  . TYR   A 101 ? 0.306554 0.415002 0.222012 0.0105559   0.0260676   -0.00070143 113 TYR   A HD1  
1483 H HD2  . TYR   A 101 ? 0.307753 0.346653 0.236685 0.00494395  0.0266396   0.0238499   113 TYR   A HD2  
1484 H HE1  . TYR   A 101 ? 0.301402 0.416125 0.234209 0.00830645  0.0325478   -0.00987186 113 TYR   A HE1  
1485 H HE2  . TYR   A 101 ? 0.296062 0.34242  0.243519 -0.00511829 0.0308841   0.0153658   113 TYR   A HE2  
1487 N N    . GLY   A 102 ? 0.264429 0.35343  0.17609  0.0131043   0.00730009  0.0126761   114 GLY   A N    
1488 C CA   . GLY   A 102 ? 0.281922 0.395862 0.191161 0.0132445   0.00295052  0.0125884   114 GLY   A CA   
1489 C C    . GLY   A 102 ? 0.286188 0.420928 0.187511 0.0265712   0.00519559  0.0251118   114 GLY   A C    
1490 O O    . GLY   A 102 ? 0.298807 0.417943 0.196031 0.0361027   0.0102277   0.0366637   114 GLY   A O    
1491 H H    . GLY   A 102 ? 0.27147  0.343779 0.187416 0.011996    0.00753019  0.0128953   114 GLY   A H    
1492 H HA2  . GLY   A 102 ? 0.27253  0.381315 0.185696 0.0110609   0.00128545  0.0124503   114 GLY   A HA2  
1493 H HA3  . GLY   A 102 ? 0.277923 0.402089 0.186733 0.0066151   -0.00035762 0.00407075  114 GLY   A HA3  
1494 N N    . SER   A 103 ? 0.309161 0.479201 0.208001 0.0267291   0.00065581  0.0230445   115 SER   A N    
1495 C CA   . SER   A 103 ? 0.2954   0.490664 0.186734 0.0424805   0.00103578  0.0356576   115 SER   A CA   
1496 C C    . SER   A 103 ? 0.297622 0.498285 0.177069 0.0486835   0.00435964  0.0433845   115 SER   A C    
1497 O O    . SER   A 103 ? 0.297386 0.502349 0.167883 0.0642931   0.00651444  0.0596553   115 SER   A O    
1498 C CB   . SER   A 103 ? 0.296011 0.534616 0.190623 0.0406163   -0.00542693 0.0310984   115 SER   A CB   
1499 O OG   . SER   A 103 ? 0.318582 0.579483 0.211715 0.0268386   -0.0104668  0.0179953   115 SER   A OG   
1500 H H    . SER   A 103 ? 0.295041 0.4737   0.196844 0.0169644   -0.00322262 0.0137665   115 SER   A H    
1501 H HA   . SER   A 103 ? 0.301586 0.48142  0.193269 0.0513447   0.00360791  0.0433969   115 SER   A HA   
1502 H HB2  . SER   A 103 ? 0.307728 0.563928 0.198085 0.0540874   -0.00549615 0.040259    115 SER   A HB2  
1503 H HB3  . SER   A 103 ? 0.294131 0.529678 0.19604  0.0356348   -0.0063386  0.0278712   115 SER   A HB3  
1505 N N    . ALA   A 104 ? 0.285407 0.486637 0.163484 0.0377865   0.00481056  0.0322582   116 ALA   A N    
1506 C CA   . ALA   A 104 ? 0.303635 0.519617 0.169379 0.0421036   0.00859376  0.0378932   116 ALA   A CA   
1507 C C    . ALA   A 104 ? 0.307335 0.492917 0.17082  0.0458224   0.0174079   0.052975    116 ALA   A C    
1508 O O    . ALA   A 104 ? 0.32267  0.516001 0.173837 0.0531305   0.022069    0.0690497   116 ALA   A O    
1509 C CB   . ALA   A 104 ? 0.312604 0.539946 0.178078 0.0308739   0.0065266   0.017658    116 ALA   A CB   
1510 H H    . ALA   A 104 ? 0.28198  0.47493  0.166325 0.0281392   0.00276601  0.0208408   116 ALA   A H    
1511 H HA   . ALA   A 104 ? 0.312074 0.55229  0.170329 0.0501991   0.00656799  0.0452269   116 ALA   A HA   
1512 H HB1  . ALA   A 104 ? 0.308782 0.554843 0.174403 0.0269001   0.00050343  0.00818711  116 ALA   A HB1  
1513 H HB2  . ALA   A 104 ? 0.302222 0.506779 0.175506 0.0247217   0.00749611  0.0104081   116 ALA   A HB2  
1514 H HB3  . ALA   A 104 ? 0.318639 0.558014 0.175541 0.0340776   0.0100415   0.020935    116 ALA   A HB3  
1515 N N    . GLY   A 105 ? 0.303312 0.454774 0.178489 0.0394917   0.0191349   0.0487077   117 GLY   A N    
1516 C CA   . GLY   A 105 ? 0.312185 0.436046 0.18974  0.0362945   0.0264369   0.0566651   117 GLY   A CA   
1517 C C    . GLY   A 105 ? 0.323369 0.462978 0.199315 0.0295909   0.0313121   0.0511813   117 GLY   A C    
1518 O O    . GLY   A 105 ? 0.316422 0.478813 0.191632 0.0270378   0.0279711   0.0350907   117 GLY   A O    
1519 H H    . GLY   A 105 ? 0.292019 0.439218 0.174116 0.0360237   0.0153287   0.0404445   117 GLY   A H    
1520 H HA2  . GLY   A 105 ? 0.305262 0.409323 0.19181  0.032115    0.0254834   0.0510399   117 GLY   A HA2  
1521 H HA3  . GLY   A 105 ? 0.328238 0.443642 0.199428 0.0427922   0.0291526   0.0713578   117 GLY   A HA3  
1522 N N    . SER   A 106 ? 0.334448 0.46138  0.210165 0.0261689   0.0393374   0.0637605   118 SER   A N    
1523 C CA   . SER   A 106 ? 0.34953  0.497286 0.22438  0.0203185   0.0462337   0.0616267   118 SER   A CA   
1524 C C    . SER   A 106 ? 0.363701 0.503877 0.231192 0.0172456   0.055441    0.0862813   118 SER   A C    
1525 O O    . SER   A 106 ? 0.376273 0.501402 0.253711 0.0066773   0.0610169   0.0898099   118 SER   A O    
1526 C CB   . SER   A 106 ? 0.333474 0.474866 0.225135 0.0128609   0.0458301   0.0431187   118 SER   A CB   
1527 O OG   . SER   A 106 ? 0.314486 0.487465 0.204923 0.0116352   0.051263    0.035197    118 SER   A OG   
1528 H H    . SER   A 106 ? 0.344039 0.449377 0.220364 0.0270313   0.0406881   0.0736833   118 SER   A H    
1529 H HA   . SER   A 106 ? 0.34737  0.520965 0.214311 0.0238171   0.0449669   0.0564987   118 SER   A HA   
1530 H HB2  . SER   A 106 ? 0.316395 0.45254  0.212041 0.0142439   0.0394046   0.0309616   118 SER   A HB2  
1531 H HB3  . SER   A 106 ? 0.328078 0.450291 0.227009 0.00812693  0.0480128   0.0486607   118 SER   A HB3  
1533 N N    . LEU   A 107 ? 0.382009 0.534894 0.231509 0.0255489   0.0566632   0.104095    119 LEU   A N    
1534 C CA   . LEU   A 107 ? 0.413604 0.553227 0.252095 0.0230446   0.0647279   0.132199    119 LEU   A CA   
1535 C C    . LEU   A 107 ? 0.432781 0.599919 0.27057  0.0108789   0.0753947   0.136444    119 LEU   A C    
1536 O O    . LEU   A 107 ? 0.413334 0.621374 0.250686 0.01188     0.076196    0.119988    119 LEU   A O    
1537 C CB   . LEU   A 107 ? 0.434923 0.584233 0.252282 0.0385088   0.0620262   0.151455    119 LEU   A CB   
1538 C CG   . LEU   A 107 ? 0.43532  0.558235 0.252696 0.0528662   0.053425    0.153605    119 LEU   A CG   
1539 C CD1  . LEU   A 107 ? 0.46327  0.603971 0.25949  0.0706741   0.050811    0.174363    119 LEU   A CD1  
1540 C CD2  . LEU   A 107 ? 0.449239 0.516621 0.273714 0.0489188   0.0552681   0.161779    119 LEU   A CD2  
1541 H H    . LEU   A 107 ? 0.37903  0.549148 0.222436 0.0326444   0.0520059   0.0994371   119 LEU   A H    
1542 H HA   . LEU   A 107 ? 0.419795 0.525948 0.264946 0.0193204   0.0647976   0.136495    119 LEU   A HA   
1543 H HB2  . LEU   A 107 ? 0.428489 0.612617 0.240109 0.0423048   0.0601208   0.143425    119 LEU   A HB2  
1544 H HB3  . LEU   A 107 ? 0.46229  0.605137 0.269972 0.036256    0.0679553   0.17157     119 LEU   A HB3  
1545 H HG   . LEU   A 107 ? 0.411112 0.544653 0.237207 0.0538065   0.0478731   0.135193    119 LEU   A HG   
1546 H HD11 . LEU   A 107 ? 0.454912 0.633455 0.246202 0.0721964   0.0490594   0.16739     119 LEU   A HD11 
1547 H HD12 . LEU   A 107 ? 0.463715 0.592953 0.26102  0.0817178   0.0453028   0.174454    119 LEU   A HD12 
1548 H HD13 . LEU   A 107 ? 0.490919 0.617889 0.277061 0.0698319   0.0561405   0.194546    119 LEU   A HD13 
1549 H HD21 . LEU   A 107 ? 0.429069 0.488729 0.267444 0.041012    0.0542035   0.146037    119 LEU   A HD21 
1550 H HD22 . LEU   A 107 ? 0.472158 0.527295 0.291457 0.0418663   0.0614748   0.176749    119 LEU   A HD22 
1551 H HD23 . LEU   A 107 ? 0.461075 0.513425 0.280969 0.0613819   0.0510734   0.167463    119 LEU   A HD23 
1552 N N    . PRO   A 108 ? 0.446116 0.593879 0.282317 -0.00099083 0.0841823   0.159033    120 PRO   A N    
1553 C CA   . PRO   A 108 ? 0.477103 0.57101  0.309995 -0.00137249 0.0829289   0.178508    120 PRO   A CA   
1554 C C    . PRO   A 108 ? 0.479988 0.533671 0.332898 -0.0101966  0.0793741   0.164973    120 PRO   A C    
1555 O O    . PRO   A 108 ? 0.496958 0.503324 0.346478 -0.00894367 0.0772792   0.176425    120 PRO   A O    
1556 C CB   . PRO   A 108 ? 0.519457 0.608819 0.342224 -0.0155057  0.0941992   0.207569    120 PRO   A CB   
1557 C CG   . PRO   A 108 ? 0.511743 0.65191  0.344702 -0.0288533  0.102571    0.195928    120 PRO   A CG   
1558 C CD   . PRO   A 108 ? 0.47285  0.651635 0.309949 -0.0154544  0.0960494   0.166282    120 PRO   A CD   
1559 H HA   . PRO   A 108 ? 0.485869 0.573212 0.308346 0.0122771   0.077842    0.184036    120 PRO   A HA   
1560 H HB2  . PRO   A 108 ? 0.537515 0.589405 0.365232 -0.0242794  0.0950937   0.21485     120 PRO   A HB2  
1561 H HB3  . PRO   A 108 ? 0.543419 0.637921 0.348514 -0.00702613 0.0949417   0.224915    120 PRO   A HB3  
1562 H HG2  . PRO   A 108 ? 0.503989 0.633319 0.352415 -0.0417844  0.104745    0.190127    120 PRO   A HG2  
1563 H HG3  . PRO   A 108 ? 0.531732 0.691389 0.352806 -0.0331033  0.109892    0.213187    120 PRO   A HG3  
1564 H HD2  . PRO   A 108 ? 0.44961  0.638724 0.302092 -0.0213926  0.0967071   0.149259    120 PRO   A HD2  
1565 H HD3  . PRO   A 108 ? 0.475546 0.687569 0.299981 -0.0102079  0.0985768   0.169509    120 PRO   A HD3  
1566 N N    . LYS   A 109 ? 0.474181 0.54552  0.34634  -0.0177868  0.0783005   0.140886    121 LYS   A N    
1567 C CA   . LYS   A 109 ? 0.486438 0.525747 0.376379 -0.0275197  0.0751381   0.129762    121 LYS   A CA   
1568 C C    . LYS   A 109 ? 0.475634 0.487367 0.366019 -0.0139323  0.0647698   0.118429    121 LYS   A C    
1569 O O    . LYS   A 109 ? 0.476555 0.448494 0.370511 -0.0169244  0.0621604   0.119094    121 LYS   A O    
1570 C CB   . LYS   A 109 ? 0.506845 0.575095 0.417086 -0.0377752  0.0765762   0.109861    121 LYS   A CB   
1571 C CG   . LYS   A 109 ? 0.546698 0.641256 0.463032 -0.0558133  0.0879818   0.120309    121 LYS   A CG   
1572 C CD   . LYS   A 109 ? 0.536825 0.673114 0.472944 -0.060205   0.0897581   0.0998499   121 LYS   A CD   
1573 C CE   . LYS   A 109 ? 0.59423  0.76236  0.539021 -0.0794293  0.101775    0.110881    121 LYS   A CE   
1574 N NZ   . LYS   A 109 ? 0.630182 0.762696 0.583043 -0.100458   0.103083    0.123428    121 LYS   A NZ   
1575 H H    . LYS   A 109 ? 0.456305 0.559625 0.329856 -0.0159986  0.079053    0.130947    121 LYS   A H    
1576 H HA   . LYS   A 109 ? 0.515167 0.531007 0.403421 -0.0369046  0.0789087   0.143646    121 LYS   A HA   
1577 H HB2  . LYS   A 109 ? 0.482788 0.574541 0.392717 -0.0292233  0.0740191   0.0978462   121 LYS   A HB2  
1578 H HB3  . LYS   A 109 ? 0.491911 0.540781 0.412423 -0.0406917  0.0721179   0.100669    121 LYS   A HB3  
1579 H HG2  . LYS   A 109 ? 0.563895 0.632612 0.48296  -0.0673814  0.0897168   0.130142    121 LYS   A HG2  
1580 H HG3  . LYS   A 109 ? 0.558242 0.669112 0.461671 -0.0534312  0.0929722   0.132742    121 LYS   A HG3  
1581 H HD2  . LYS   A 109 ? 0.529179 0.688545 0.461086 -0.0488602  0.0883779   0.0899998   121 LYS   A HD2  
1582 H HD3  . LYS   A 109 ? 0.528907 0.650551 0.476669 -0.0608041  0.0838485   0.0878486   121 LYS   A HD3  
1583 H HE2  . LYS   A 109 ? 0.60279  0.786984 0.534693 -0.0791768  0.108121    0.124095    121 LYS   A HE2  
1584 H HE3  . LYS   A 109 ? 0.571098 0.769727 0.528838 -0.0785434  0.102392    0.0963038   121 LYS   A HE3  
1585 H HZ1  . LYS   A 109 ? 0.649276 0.760165 0.589207 -0.103581   0.105652    0.140841    121 LYS   A HZ1  
1586 H HZ2  . LYS   A 109 ? 0.615429 0.72406  0.574292 -0.0979285  0.0957884   0.113382    121 LYS   A HZ2  
1587 H HZ3  . LYS   A 109 ? 0.628545 0.784898 0.593091 -0.11327    0.108481    0.123716    121 LYS   A HZ3  
1588 N N    . ILE   A 110 ? 0.42672  0.461615 0.314426 -0.00068915 0.0587924   0.105827    122 ILE   A N    
1589 C CA   . ILE   A 110 ? 0.419568 0.437729 0.310251 0.00918719  0.0500031   0.0942106   122 ILE   A CA   
1590 C C    . ILE   A 110 ? 0.393781 0.421265 0.269793 0.0259706   0.0463873   0.102422    122 ILE   A C    
1591 O O    . ILE   A 110 ? 0.375643 0.438843 0.245966 0.0297711   0.0455904   0.099405    122 ILE   A O    
1592 C CB   . ILE   A 110 ? 0.418183 0.453761 0.321598 0.00735699  0.0444858   0.0708591   122 ILE   A CB   
1593 C CG1  . ILE   A 110 ? 0.461278 0.506408 0.378825 -0.0050163  0.0478131   0.0615162   122 ILE   A CG1  
1594 C CG2  . ILE   A 110 ? 0.417127 0.431739 0.324203 0.0129967   0.037178    0.0625909   122 ILE   A CG2  
1595 C CD1  . ILE   A 110 ? 0.520903 0.538656 0.447822 -0.0160682  0.0495204   0.0648983   122 ILE   A CD1  
1596 H H    . ILE   A 110 ? 0.428828 0.491562 0.312698 0.00121288  0.0603343   0.104134    122 ILE   A H    
1597 H HA   . ILE   A 110 ? 0.426284 0.416261 0.319771 0.00673357  0.0494941   0.0962663   122 ILE   A HA   
1598 H HB   . ILE   A 110 ? 0.415245 0.473241 0.313857 0.0119834   0.0431797   0.067453    122 ILE   A HB   
1599 H HG12 . ILE   A 110 ? 0.463946 0.528998 0.378403 -0.00722653 0.0529289   0.0659748   122 ILE   A HG12 
1600 H HG13 . ILE   A 110 ? 0.440644 0.493172 0.36434  -0.00348669 0.0434582   0.0479109   122 ILE   A HG13 
1601 H HG21 . ILE   A 110 ? 0.397022 0.417831 0.311734 0.0100796   0.0339208   0.0502974   122 ILE   A HG21 
1602 H HG22 . ILE   A 110 ? 0.424694 0.415759 0.333295 0.0107431   0.0380044   0.0663057   122 ILE   A HG22 
1603 H HG23 . ILE   A 110 ? 0.415142 0.435249 0.314994 0.0218566   0.034883    0.0658055   122 ILE   A HG23 
1604 H HD11 . ILE   A 110 ? 0.500309 0.498875 0.4283   -0.0129282  0.0446458   0.0604236   122 ILE   A HD11 
1605 H HD12 . ILE   A 110 ? 0.492393 0.522802 0.429972 -0.0227347  0.0505599   0.0572989   122 ILE   A HD12 
1606 H HD13 . ILE   A 110 ? 0.522083 0.530034 0.443157 -0.0198442  0.0542104   0.078661    122 ILE   A HD13 
1607 N N    . PRO   A 111 ? 0.397087 0.397003 0.267537 0.0375061   0.0431965   0.109777    123 PRO   A N    
1608 C CA   . PRO   A 111 ? 0.400145 0.416847 0.259277 0.0559785   0.0388556   0.116349    123 PRO   A CA   
1609 C C    . PRO   A 111 ? 0.365173 0.406928 0.232493 0.059633    0.0317126   0.0976586   123 PRO   A C    
1610 O O    . PRO   A 111 ? 0.340496 0.379794 0.220261 0.0487815   0.0300539   0.081349    123 PRO   A O    
1611 C CB   . PRO   A 111 ? 0.436043 0.410729 0.286393 0.0679413   0.0392156   0.131779    123 PRO   A CB   
1612 C CG   . PRO   A 111 ? 0.435801 0.375542 0.298869 0.0559997   0.0393158   0.118751    123 PRO   A CG   
1613 C CD   . PRO   A 111 ? 0.415935 0.369529 0.289698 0.0347717   0.0435103   0.111784    123 PRO   A CD   
1614 H HA   . PRO   A 111 ? 0.40645  0.444248 0.257474 0.0573041   0.040797    0.124348    123 PRO   A HA   
1615 H HB2  . PRO   A 111 ? 0.439797 0.420989 0.286526 0.0826203   0.0351386   0.132003    123 PRO   A HB2  
1616 H HB3  . PRO   A 111 ? 0.462282 0.42707  0.30343  0.0673086   0.043171    0.147778    123 PRO   A HB3  
1617 H HG2  . PRO   A 111 ? 0.417329 0.362346 0.286059 0.0604536   0.0351498   0.106402    123 PRO   A HG2  
1618 H HG3  . PRO   A 111 ? 0.462366 0.368302 0.320534 0.0578965   0.0406695   0.12717     123 PRO   A HG3  
1619 H HD2  . PRO   A 111 ? 0.399116 0.349644 0.283328 0.0287549   0.0412621   0.0980275   123 PRO   A HD2  
1620 H HD3  . PRO   A 111 ? 0.436466 0.374939 0.307947 0.0265813   0.0482404   0.122245    123 PRO   A HD3  
1621 N N    . SER   A 112 ? 0.36132  0.429274 0.221298 0.074345    0.0273225   0.101754    124 SER   A N    
1622 C CA   . SER   A 112 ? 0.324678 0.420513 0.192179 0.0760106   0.020782    0.0870694   124 SER   A CA   
1623 C C    . SER   A 112 ? 0.334934 0.405577 0.211398 0.0773428   0.0194372   0.0791982   124 SER   A C    
1624 O O    . SER   A 112 ? 0.349656 0.387947 0.222059 0.0872631   0.0214266   0.0871267   124 SER   A O    
1625 C CB   . SER   A 112 ? 0.339452 0.470322 0.198338 0.0924504   0.0166133   0.0953385   124 SER   A CB   
1626 O OG   . SER   A 112 ? 0.310162 0.471379 0.177884 0.0931279   0.0106026   0.0829576   124 SER   A OG   
1627 H H    . SER   A 112 ? 0.378937 0.448926 0.228846 0.0831008   0.0284163   0.115176    124 SER   A H    
1628 H HA   . SER   A 112 ? 0.315339 0.425239 0.187592 0.0648844   0.0198304   0.0763879   124 SER   A HA   
1629 H HB2  . SER   A 112 ? 0.338661 0.489573 0.191456 0.0901862   0.0168247   0.0979921   124 SER   A HB2  
1630 H HB3  . SER   A 112 ? 0.356447 0.471416 0.208789 0.105571    0.0177335   0.107624    124 SER   A HB3  
1632 N N    . ASN   A 113 ? 0.308396 0.391412 0.195399 0.0663558   0.0160751   0.0634775   125 ASN   A N    
1633 C CA   . ASN   A 113 ? 0.335166 0.409811 0.228623 0.0684927   0.0141506   0.0560967   125 ASN   A CA   
1634 C C    . ASN   A 113 ? 0.362433 0.393391 0.256933 0.0668773   0.017208    0.0554853   125 ASN   A C    
1635 O O    . ASN   A 113 ? 0.374564 0.391985 0.268262 0.0766501   0.0167539   0.0532348   125 ASN   A O    
1636 C CB   . ASN   A 113 ? 0.350725 0.448757 0.241063 0.087174    0.011968    0.0607725   125 ASN   A CB   
1637 C CG   . ASN   A 113 ? 0.348199 0.495962 0.241343 0.0833297   0.00754968  0.0574421   125 ASN   A CG   
1638 O OD1  . ASN   A 113 ? 0.346876 0.505345 0.245776 0.0647101   0.00529282  0.0473805   125 ASN   A OD1  
1639 N ND2  . ASN   A 113 ? 0.391211 0.569671 0.280777 0.100954    0.00540839  0.0646152   125 ASN   A ND2  
1640 H H    . ASN   A 113 ? 0.304995 0.401846 0.194295 0.057259    0.0149604   0.0573047   125 ASN   A H    
1641 H HA   . ASN   A 113 ? 0.316802 0.402393 0.216336 0.0580011   0.0118531   0.0471379   125 ASN   A HA   
1642 H HB2  . ASN   A 113 ? 0.370403 0.457815 0.253378 0.0996447   0.0134444   0.0706826   125 ASN   A HB2  
1643 H HB3  . ASN   A 113 ? 0.349583 0.442305 0.243287 0.0896122   0.0117271   0.0557649   125 ASN   A HB3  
1644 H HD21 . ASN   A 113 ? 0.376039 0.585435 0.266288 0.0987223   0.00247979  0.0636345   125 ASN   A HD21 
1645 H HD22 . ASN   A 113 ? 0.393362 0.562158 0.27983  0.115673    0.00649353  0.0698597   125 ASN   A HD22 
1646 N N    . ALA   A 114 ? 0.343438 0.35759  0.240736 0.0537049   0.0198776   0.0547638   126 ALA   A N    
1647 C CA   . ALA   A 114 ? 0.370715 0.348632 0.27059  0.0481746   0.0221829   0.053609    126 ALA   A CA   
1648 C C    . ALA   A 114 ? 0.341606 0.317152 0.250934 0.0385944   0.0188363   0.0392356   126 ALA   A C    
1649 O O    . ALA   A 114 ? 0.339056 0.331543 0.254526 0.0294119   0.0166475   0.032411    126 ALA   A O    
1650 C CB   . ALA   A 114 ? 0.385463 0.355443 0.285655 0.0377106   0.0269931   0.060632    126 ALA   A CB   
1651 H H    . ALA   A 114 ? 0.343302 0.371705 0.241386 0.0477351   0.0200909   0.0539416   126 ALA   A H    
1652 H HA   . ALA   A 114 ? 0.384728 0.345676 0.279367 0.0578984   0.0225919   0.0577835   126 ALA   A HA   
1653 H HB1  . ALA   A 114 ? 0.398433 0.369464 0.290774 0.043703    0.0292317   0.0717526   126 ALA   A HB1  
1654 H HB2  . ALA   A 114 ? 0.367717 0.355078 0.272735 0.0305637   0.0266402   0.0551398   126 ALA   A HB2  
1655 H HB3  . ALA   A 114 ? 0.392241 0.34019  0.295397 0.0320301   0.0282045   0.0595774   126 ALA   A HB3  
1656 N N    . THR   A 115 ? 0.348076 0.299132 0.25683  0.0413937   0.0181612   0.0349164   127 THR   A N    
1657 C CA   . THR   A 115 ? 0.338645 0.282417 0.254291 0.0318435   0.0151816   0.0232898   127 THR   A CA   
1658 C C    . THR   A 115 ? 0.341383 0.266917 0.263301 0.019107    0.016953    0.0227281   127 THR   A C    
1659 O O    . THR   A 115 ? 0.380337 0.281963 0.298719 0.0184402   0.0202718   0.0292184   127 THR   A O    
1660 C CB   . THR   A 115 ? 0.34611  0.278508 0.256325 0.0418452   0.01336     0.0167964   127 THR   A CB   
1661 O OG1  . THR   A 115 ? 0.348314 0.309862 0.256049 0.0507583   0.0124735   0.018011    127 THR   A OG1  
1662 C CG2  . THR   A 115 ? 0.364149 0.294742 0.278425 0.0336628   0.00944155  0.00508472  127 THR   A CG2  
1663 H H    . THR   A 115 ? 0.367108 0.30545  0.27     0.0506653   0.0191623   0.0390118   127 THR   A H    
1664 H HA   . THR   A 115 ? 0.320294 0.281237 0.23963  0.0275895   0.0130169   0.0198842   127 THR   A HA   
1665 H HB   . THR   A 115 ? 0.376374 0.288229 0.281543 0.0482989   0.0149656   0.019307    127 THR   A HB   
1667 H HG21 . THR   A 115 ? 0.365097 0.292844 0.274328 0.0411504   0.00862356  0.00027038  127 THR   A HG21 
1668 H HG22 . THR   A 115 ? 0.339273 0.287274 0.257065 0.0288099   0.00764113  0.0045052   127 THR   A HG22 
1669 H HG23 . THR   A 115 ? 0.362    0.27812  0.279902 0.0260276   0.00930878  0.00298347  127 THR   A HG23 
1670 N N    . LEU   A 116 ? 0.325817 0.263147 0.25735  0.00882996  0.0144068   0.0154545   128 LEU   A N    
1671 C CA   . LEU   A 116 ? 0.34768  0.280208 0.288823 -0.00358277 0.0156745   0.013415    128 LEU   A CA   
1672 C C    . LEU   A 116 ? 0.346727 0.273687 0.293543 -0.00881515 0.010131    0.00190852  128 LEU   A C    
1673 O O    . LEU   A 116 ? 0.336095 0.273073 0.281897 -0.00488538 0.00514653  -0.00373494 128 LEU   A O    
1674 C CB   . LEU   A 116 ? 0.351431 0.308716 0.300074 -0.00776686 0.0168397   0.0132018   128 LEU   A CB   
1675 C CG   . LEU   A 116 ? 0.348971 0.319605 0.290986 -0.00326207 0.0215207   0.0220774   128 LEU   A CG   
1676 C CD1  . LEU   A 116 ? 0.346749 0.340742 0.296286 -0.00731738 0.0228878   0.0175294   128 LEU   A CD1  
1677 C CD2  . LEU   A 116 ? 0.377597 0.332716 0.312769 -0.0036145  0.0273559   0.034936    128 LEU   A CD2  
1678 H H    . LEU   A 116 ? 0.316185 0.266053 0.248628 0.00975301  0.0116121   0.011945    128 LEU   A H    
1679 H HA   . LEU   A 116 ? 0.36469  0.283285 0.303518 -0.00574845 0.0192465   0.0193948   128 LEU   A HA   
1680 H HB2  . LEU   A 116 ? 0.333692 0.298863 0.284226 -0.00600223 0.0126415   0.00734489  128 LEU   A HB2  
1681 H HB3  . LEU   A 116 ? 0.348468 0.307556 0.304739 -0.0153461  0.0182103   0.0118724   128 LEU   A HB3  
1682 H HG   . LEU   A 116 ? 0.346875 0.321933 0.283488 0.00318871  0.0192558   0.0217802   128 LEU   A HG   
1683 H HD11 . LEU   A 116 ? 0.333749 0.331845 0.286613 -0.00596625 0.0183568   0.00976448  128 LEU   A HD11 
1684 H HD12 . LEU   A 116 ? 0.345274 0.349948 0.28931  -0.00440366 0.0254771   0.0216134   128 LEU   A HD12 
1685 H HD13 . LEU   A 116 ? 0.348513 0.343763 0.304669 -0.0137794  0.0255562   0.0179792   128 LEU   A HD13 
1686 H HD21 . LEU   A 116 ? 0.383966 0.326465 0.312184 0.00368728  0.0261392   0.037438    128 LEU   A HD21 
1687 H HD22 . LEU   A 116 ? 0.384707 0.329964 0.325144 -0.011923   0.0288228   0.0348178   128 LEU   A HD22 
1688 H HD23 . LEU   A 116 ? 0.377398 0.345236 0.309255 -0.0027306  0.0307555   0.0411641   128 LEU   A HD23 
1689 N N    . PHE   A 117 ? 0.372843 0.288318 0.326341 -0.0200185  0.0109876   -0.00038373 129 PHE   A N    
1690 C CA   . PHE   A 117 ? 0.364932 0.282962 0.326511 -0.0279311  0.00511207  -0.012143   129 PHE   A CA   
1691 C C    . PHE   A 117 ? 0.35577  0.295664 0.333746 -0.0398339  0.00596131  -0.013128   129 PHE   A C    
1692 O O    . PHE   A 117 ? 0.370118 0.31118  0.352778 -0.0485802  0.0127006   -0.00529302 129 PHE   A O    
1693 C CB   . PHE   A 117 ? 0.392728 0.280129 0.348988 -0.0326237  0.0042519   -0.0174546  129 PHE   A CB   
1694 C CG   . PHE   A 117 ? 0.400339 0.29276  0.365177 -0.0439384  -0.00244237 -0.0313177  129 PHE   A CG   
1695 C CD1  . PHE   A 117 ? 0.418282 0.316233 0.397434 -0.0623465  -0.00157666 -0.0325801  129 PHE   A CD1  
1696 C CD2  . PHE   A 117 ? 0.399251 0.297673 0.35813  -0.0369476  -0.0096748  -0.0425267  129 PHE   A CD2  
1697 C CE1  . PHE   A 117 ? 0.437613 0.347674 0.426164 -0.0731788  -0.00896062 -0.0463585  129 PHE   A CE1  
1698 C CE2  . PHE   A 117 ? 0.416582 0.325012 0.382112 -0.046355   -0.0169615  -0.0554182  129 PHE   A CE2  
1699 C CZ   . PHE   A 117 ? 0.41357  0.32835  0.394572 -0.0642665  -0.0171793  -0.0580813  129 PHE   A CZ   
1700 H H    . PHE   A 117 ? 0.380677 0.287559 0.333542 -0.0237884  0.015267    0.0061869   129 PHE   A H    
1701 H HA   . PHE   A 117 ? 0.354389 0.280864 0.313671 -0.0220666  0.00078546  -0.0165635  129 PHE   A HA   
1702 H HB2  . PHE   A 117 ? 0.398872 0.276112 0.344966 -0.022347   0.00338818  -0.0188444  129 PHE   A HB2  
1703 H HB3  . PHE   A 117 ? 0.409109 0.283208 0.365485 -0.0381787  0.00877692  -0.0105877  129 PHE   A HB3  
1704 H HD1  . PHE   A 117 ? 0.423432 0.320438 0.406134 -0.0680866  0.00404513  -0.0237777  129 PHE   A HD1  
1705 H HD2  . PHE   A 117 ? 0.39571  0.294354 0.345608 -0.0259785  -0.0096748  -0.0410742  129 PHE   A HD2  
1706 H HE1  . PHE   A 117 ? 0.43577  0.353614 0.435617 -0.0870813  -0.00834539 -0.0473718  129 PHE   A HE1  
1707 H HE2  . PHE   A 117 ? 0.410322 0.324611 0.369806 -0.0409455  -0.0218786  -0.0622609  129 PHE   A HE2  
1708 H HZ   . PHE   A 117 ? 0.425215 0.350525 0.411546 -0.0710623  -0.0228836  -0.0676454  129 PHE   A HZ   
1709 N N    . PHE   A 118 ? 0.318803 0.278744 0.304999 -0.0392151  -0.00086285 -0.0218857  130 PHE   A N    
1710 C CA   . PHE   A 118 ? 0.324771 0.311776 0.328579 -0.0474065  -0.00165111 -0.0256192  130 PHE   A CA   
1711 C C    . PHE   A 118 ? 0.334339 0.33083  0.345265 -0.05219    -0.0106749  -0.0371661  130 PHE   A C    
1712 O O    . PHE   A 118 ? 0.350818 0.341665 0.352277 -0.0440701  -0.0175644  -0.0418013  130 PHE   A O    
1713 C CB   . PHE   A 118 ? 0.297685 0.308607 0.306571 -0.0369588  -0.0021896  -0.0249973  130 PHE   A CB   
1714 C CG   . PHE   A 118 ? 0.301803 0.314054 0.305612 -0.0332505  0.00600729  -0.0166987  130 PHE   A CG   
1715 C CD1  . PHE   A 118 ? 0.303839 0.301533 0.292977 -0.0239455  0.00614881  -0.012344   130 PHE   A CD1  
1716 C CD2  . PHE   A 118 ? 0.322803 0.356745 0.336398 -0.0395909  0.0133685   -0.0136932  130 PHE   A CD2  
1717 C CE1  . PHE   A 118 ? 0.318763 0.322269 0.30251  -0.0204669  0.0120901   -0.00645023 130 PHE   A CE1  
1718 C CE2  . PHE   A 118 ? 0.325692 0.364657 0.331762 -0.0352625  0.0204493   -0.00671219 130 PHE   A CE2  
1719 C CZ   . PHE   A 118 ? 0.311442 0.33441  0.302274 -0.0254586  0.0191078   -0.00371546 130 PHE   A CZ   
1720 H H    . PHE   A 118 ? 0.322462 0.281089 0.302975 -0.0326916  -0.00522432 -0.0250484  130 PHE   A H    
1721 H HA   . PHE   A 118 ? 0.332064 0.318467 0.340551 -0.0569189  0.00375326  -0.0216719  130 PHE   A HA   
1722 H HB2  . PHE   A 118 ? 0.295731 0.302848 0.298702 -0.0288353  -0.00738456 -0.0269189  130 PHE   A HB2  
1723 H HB3  . PHE   A 118 ? 0.299031 0.330422 0.320312 -0.0400855  -0.00354328 -0.0290779  130 PHE   A HB3  
1724 H HD1  . PHE   A 118 ? 0.306034 0.2935   0.289032 -0.0203242  0.00193932  -0.013828   130 PHE   A HD1  
1725 H HD2  . PHE   A 118 ? 0.321677 0.370084 0.346765 -0.0473141  0.0136727   -0.0164101  130 PHE   A HD2  
1726 H HE1  . PHE   A 118 ? 0.310295 0.307328 0.285178 -0.0152179  0.0115154   -0.00420026 130 PHE   A HE1  
1727 H HE2  . PHE   A 118 ? 0.324795 0.381556 0.336244 -0.0394224  0.0260301   -0.00432495 130 PHE   A HE2  
1728 H HZ   . PHE   A 118 ? 0.31671  0.345851 0.302207 -0.022667   0.0230306   2.022e-05   130 PHE   A HZ   
1729 N N    . GLU   A 119 ? 0.3294   0.344973 0.356971 -0.0665499  -0.0103083  -0.0411587  131 GLU   A N    
1730 C CA   . GLU   A 119 ? 0.327521 0.372036 0.368236 -0.0691875  -0.0194493  -0.0518759  131 GLU   A CA   
1731 C C    . GLU   A 119 ? 0.32738  0.411193 0.385027 -0.0637577  -0.0179382  -0.0505383  131 GLU   A C    
1732 O O    . GLU   A 119 ? 0.325862 0.423265 0.393084 -0.0719693  -0.008774   -0.0453095  131 GLU   A O    
1733 C CB   . GLU   A 119 ? 0.359072 0.401513 0.407855 -0.0905485  -0.0215134  -0.0602845  131 GLU   A CB   
1734 C CG   . GLU   A 119 ? 0.350885 0.431539 0.41511  -0.0951701  -0.0320633  -0.0726721  131 GLU   A CG   
1735 C CD   . GLU   A 119 ? 0.372258 0.451316 0.444916 -0.120249   -0.0350735  -0.0835237  131 GLU   A CD   
1736 O OE1  . GLU   A 119 ? 0.400943 0.450097 0.45922  -0.122948   -0.0398697  -0.0922221  131 GLU   A OE1  
1737 O OE2  . GLU   A 119 ? 0.381522 0.491816 0.47568  -0.137915   -0.0328449  -0.0846175  131 GLU   A OE2  
1738 H H    . GLU   A 119 ? 0.340252 0.35301  0.371333 -0.0755657  -0.00419468 -0.036407   131 GLU   A H    
1739 H HA   . GLU   A 119 ? 0.327946 0.368662 0.360298 -0.0593995  -0.0256221  -0.0547356  131 GLU   A HA   
1740 H HB2  . GLU   A 119 ? 0.368028 0.382535 0.404259 -0.0910321  -0.0226654  -0.0627287  131 GLU   A HB2  
1741 H HB3  . GLU   A 119 ? 0.362369 0.405685 0.418263 -0.102077   -0.014791   -0.0553694  131 GLU   A HB3  
1742 H HG2  . GLU   A 119 ? 0.339997 0.450524 0.417556 -0.0927488  -0.0309773  -0.0707618  131 GLU   A HG2  
1743 H HG3  . GLU   A 119 ? 0.34654  0.426602 0.402113 -0.0834374  -0.0388461  -0.0759825  131 GLU   A HG3  
1744 N N    . ILE   A 120 ? 0.303026 0.404408 0.362473 -0.048339   -0.0269158  -0.054767   132 ILE   A N    
1745 C CA   . ILE   A 120 ? 0.282944 0.416797 0.355494 -0.0355677  -0.0276824  -0.0556597  132 ILE   A CA   
1746 C C    . ILE   A 120 ? 0.292265 0.460695 0.378638 -0.0317704  -0.0390531  -0.0641816  132 ILE   A C    
1747 O O    . ILE   A 120 ? 0.276443 0.434762 0.352188 -0.0258633  -0.0488995  -0.0659348  132 ILE   A O    
1748 C CB   . ILE   A 120 ? 0.286553 0.400163 0.344533 -0.0157174  -0.0289685  -0.0507908  132 ILE   A CB   
1749 C CG1  . ILE   A 120 ? 0.292609 0.376626 0.33599  -0.0187789  -0.0195215  -0.043102   132 ILE   A CG1  
1750 C CG2  . ILE   A 120 ? 0.306131 0.447596 0.376323 0.00045877  -0.030645   -0.0545697  132 ILE   A CG2  
1751 C CD1  . ILE   A 120 ? 0.289418 0.352043 0.317877 -0.00445521 -0.0218607  -0.0394707  132 ILE   A CD1  
1752 H H    . ILE   A 120 ? 0.306491 0.398372 0.357624 -0.0445089  -0.0330723  -0.0571254  132 ILE   A H    
1753 H HA   . ILE   A 120 ? 0.287859 0.435878 0.369581 -0.0420761  -0.0204837  -0.0543201  132 ILE   A HA   
1754 H HB   . ILE   A 120 ? 0.292527 0.394623 0.341769 -0.0106363  -0.0358479  -0.0506096  132 ILE   A HB   
1755 H HG12 . ILE   A 120 ? 0.289751 0.386029 0.339869 -0.0227579  -0.0126777  -0.0420796  132 ILE   A HG12 
1756 H HG13 . ILE   A 120 ? 0.295352 0.363133 0.332137 -0.0271852  -0.0184884  -0.0414303  132 ILE   A HG13 
1757 H HG21 . ILE   A 120 ? 0.299813 0.423584 0.360034 0.0112156   -0.031625   -0.0523142  132 ILE   A HG21 
1758 H HG22 . ILE   A 120 ? 0.297131 0.456826 0.376905 -0.00449945 -0.0236115  -0.0555931  132 ILE   A HG22 
1759 H HG23 . ILE   A 120 ? 0.301457 0.461115 0.379494 0.00551623  -0.037951   -0.0585169  132 ILE   A HG23 
1760 H HD11 . ILE   A 120 ? 0.29215  0.347342 0.315143 3.99e-06    -0.0287988  -0.039434   132 ILE   A HD11 
1761 H HD12 . ILE   A 120 ? 0.289076 0.335601 0.308236 -0.00790022 -0.017089   -0.0350251  132 ILE   A HD12 
1762 H HD13 . ILE   A 120 ? 0.288696 0.361863 0.321999 0.00349517  -0.0213892  -0.0417003  132 ILE   A HD13 
1763 N N    . GLU   A 121 ? 0.299853 0.513906 0.409266 -0.0331356  -0.0374887  -0.0687265  133 GLU   A N    
1764 C CA   . GLU   A 121 ? 0.309583 0.565532 0.434239 -0.0227553  -0.048931   -0.0762785  133 GLU   A CA   
1765 C C    . GLU   A 121 ? 0.302985 0.576038 0.432947 0.00375687  -0.0497344  -0.0761008  133 GLU   A C    
1766 O O    . GLU   A 121 ? 0.337803 0.628085 0.477188 0.00461916  -0.0395509  -0.076523   133 GLU   A O    
1767 C CB   . GLU   A 121 ? 0.320598 0.624133 0.470364 -0.0439701  -0.048806   -0.0841855  133 GLU   A CB   
1768 C CG   . GLU   A 121 ? 0.322222 0.680552 0.490776 -0.0302812  -0.0611384  -0.092337   133 GLU   A CG   
1769 C CD   . GLU   A 121 ? 0.330879 0.742884 0.525867 -0.0539763  -0.0629994  -0.10167    133 GLU   A CD   
1770 O OE1  . GLU   A 121 ? 0.338468 0.735826 0.534874 -0.0838948  -0.0549293  -0.101342   133 GLU   A OE1  
1771 O OE2  . GLU   A 121 ? 0.349364 0.816845 0.563292 -0.0429383  -0.0729345  -0.108824   133 GLU   A OE2  
1772 H H    . GLU   A 121 ? 0.297756 0.519899 0.413474 -0.0400333  -0.0291236  -0.0667014  133 GLU   A H    
1773 H HA   . GLU   A 121 ? 0.311806 0.553979 0.425846 -0.0181669  -0.0571523  -0.0766014  133 GLU   A HA   
1774 H HB2  . GLU   A 121 ? 0.326692 0.613707 0.47128  -0.0601646  -0.0498344  -0.0859257  133 GLU   A HB2  
1775 H HB3  . GLU   A 121 ? 0.317139 0.633782 0.476217 -0.0515189  -0.0394376  -0.0822212  133 GLU   A HB3  
1776 H HG2  . GLU   A 121 ? 0.318641 0.693258 0.493248 -0.0132385  -0.0596184  -0.0915474  133 GLU   A HG2  
1777 H HG3  . GLU   A 121 ? 0.326385 0.671051 0.483302 -0.0205373  -0.0704986  -0.0923607  133 GLU   A HG3  
1778 N N    . LEU   A 122 ? 0.299341 0.564926 0.420961 0.025998    -0.0617862  -0.0752456  134 LEU   A N    
1779 C CA   . LEU   A 122 ? 0.305941 0.583573 0.432497 0.0540111   -0.0650823  -0.0768423  134 LEU   A CA   
1780 C C    . LEU   A 122 ? 0.318061 0.661643 0.472372 0.0624517   -0.0704651  -0.0858009  134 LEU   A C    
1781 O O    . LEU   A 122 ? 0.316994 0.68198  0.47561  0.0681283   -0.0832744  -0.0872411  134 LEU   A O    
1782 C CB   . LEU   A 122 ? 0.315233 0.551381 0.41971  0.0737096   -0.0758834  -0.0693123  134 LEU   A CB   
1783 C CG   . LEU   A 122 ? 0.324627 0.553988 0.428456 0.104047    -0.0802949  -0.070362   134 LEU   A CG   
1784 C CD1  . LEU   A 122 ? 0.312925 0.539233 0.420125 0.104954    -0.0673539  -0.076309   134 LEU   A CD1  
1785 C CD2  . LEU   A 122 ? 0.343587 0.519488 0.421591 0.115151    -0.0892133  -0.058992   134 LEU   A CD2  
1786 H H    . LEU   A 122 ? 0.305952 0.557539 0.417667 0.0243909   -0.0681621  -0.0734938  134 LEU   A H    
1787 H HA   . LEU   A 122 ? 0.303858 0.574351 0.429697 0.0543308   -0.0563393  -0.076978   134 LEU   A HA   
1788 H HB2  . LEU   A 122 ? 0.312783 0.51355  0.401666 0.0652933   -0.0719187  -0.0639737  134 LEU   A HB2  
1789 H HB3  . LEU   A 122 ? 0.319461 0.566059 0.423607 0.0743824   -0.0845921  -0.0684841  134 LEU   A HB3  
1790 H HG   . LEU   A 122 ? 0.329524 0.593748 0.4474   0.11627     -0.0862902  -0.0748476  134 LEU   A HG   
1791 H HD11 . LEU   A 122 ? 0.308748 0.575537 0.433644 0.103594    -0.0630518  -0.0829476  134 LEU   A HD11 
1792 H HD12 . LEU   A 122 ? 0.329818 0.536833 0.430315 0.122777    -0.070587   -0.0772233  134 LEU   A HD12 
1793 H HD13 . LEU   A 122 ? 0.306686 0.511202 0.404471 0.0892439   -0.060455   -0.0726561  134 LEU   A HD13 
1794 H HD21 . LEU   A 122 ? 0.346008 0.525398 0.419562 0.111731    -0.0958837  -0.0544839  134 LEU   A HD21 
1795 H HD22 . LEU   A 122 ? 0.339839 0.485067 0.405741 0.105266    -0.0831607  -0.0555386  134 LEU   A HD22 
1796 H HD23 . LEU   A 122 ? 0.360143 0.529965 0.437787 0.135377    -0.0943867  -0.0595326  134 LEU   A HD23 
1797 N N    . LEU   A 123 ? 0.327537 0.708025 0.500144 0.0650331   -0.0607353  -0.091847   135 LEU   A N    
1798 C CA   . LEU   A 123 ? 0.358118 0.812589 0.56109  0.0702185   -0.06298    -0.101049   135 LEU   A CA   
1799 C C    . LEU   A 123 ? 0.402406 0.87103  0.608774 0.110858    -0.0735391  -0.10542    135 LEU   A C    
1800 O O    . LEU   A 123 ? 0.421854 0.93925  0.645557 0.123085    -0.0846029  -0.110016   135 LEU   A O    
1801 C CB   . LEU   A 123 ? 0.349919 0.844512 0.570941 0.0548841   -0.0466025  -0.104701   135 LEU   A CB   
1802 C CG   . LEU   A 123 ? 0.3525   0.82832  0.569189 0.0158599   -0.0351511  -0.0979118  135 LEU   A CG   
1803 C CD1  . LEU   A 123 ? 0.350961 0.863025 0.580699 0.00438303  -0.0181578  -0.0975263  135 LEU   A CD1  
1804 C CD2  . LEU   A 123 ? 0.37346  0.869001 0.60178  -0.00984258 -0.0422268  -0.100086   135 LEU   A CD2  
1805 H H    . LEU   A 123 ? 0.32829  0.690868 0.494314 0.0636318   -0.0523047  -0.0903567  135 LEU   A H    
1806 H HA   . LEU   A 123 ? 0.355809 0.827859 0.565454 0.0576827   -0.0688827  -0.102059   135 LEU   A HA   
1807 H HB2  . LEU   A 123 ? 0.353952 0.836449 0.568391 0.0698395   -0.0416584  -0.105621   135 LEU   A HB2  
1808 H HB3  . LEU   A 123 ? 0.351824 0.901165 0.59467  0.0572124   -0.0482298  -0.110851   135 LEU   A HB3  
1809 H HG   . LEU   A 123 ? 0.353861 0.778201 0.549407 0.0151607   -0.0343732  -0.0920802  135 LEU   A HG   
1810 H HD11 . LEU   A 123 ? 0.351279 0.863867 0.577138 0.0249307   -0.0156457  -0.10026    135 LEU   A HD11 
1811 H HD12 . LEU   A 123 ? 0.350347 0.834723 0.570074 -0.0150352  -0.0108138  -0.0903577  135 LEU   A HD12 
1812 H HD13 . LEU   A 123 ? 0.350455 0.914132 0.601892 -0.00399789 -0.0172611  -0.101638   135 LEU   A HD13 
1813 H HD21 . LEU   A 123 ? 0.369775 0.840477 0.586273 -0.00283569 -0.0521718  -0.099732   135 LEU   A HD21 
1814 H HD22 . LEU   A 123 ? 0.367697 0.91687  0.61766  -0.00922273 -0.0443605  -0.10615    135 LEU   A HD22 
1815 H HD23 . LEU   A 123 ? 0.368664 0.848981 0.594228 -0.0339762  -0.0349024  -0.0961312  135 LEU   A HD23 
1816 N N    . ASP   A 124 ? 0.40047  0.827623 0.590733 0.131952    -0.0705402  -0.104903   136 ASP   A N    
1817 C CA   . ASP   A 124 ? 0.451702 0.883232 0.643638 0.172301    -0.0795993  -0.110467   136 ASP   A CA   
1818 C C    . ASP   A 124 ? 0.489805 0.85436  0.656738 0.186209    -0.076818   -0.109356   136 ASP   A C    
1819 O O    . ASP   A 124 ? 0.454637 0.789074 0.609168 0.165273    -0.0655907  -0.10667    136 ASP   A O    
1820 C CB   . ASP   A 124 ? 0.457304 0.968154 0.680175 0.185648    -0.0744577  -0.123977   136 ASP   A CB   
1821 C CG   . ASP   A 124 ? 0.473334 1.01236  0.706813 0.228847    -0.0878482  -0.13095    136 ASP   A CG   
1822 O OD1  . ASP   A 124 ? 0.504794 1        0.720903 0.246884    -0.102811   -0.122628   136 ASP   A OD1  
1823 O OD2  . ASP   A 124 ? 0.468323 1.07398  0.726645 0.244653    -0.0828782  -0.143688   136 ASP   A OD2  
1824 H H    . ASP   A 124 ? 0.404263 0.798919 0.581996 0.121132    -0.0630992  -0.101602   136 ASP   A H    
1825 H HA   . ASP   A 124 ? 0.460855 0.888167 0.649582 0.182033    -0.091483   -0.106268   136 ASP   A HA   
1826 H HB2  . ASP   A 124 ? 0.439673 0.992456 0.678751 0.165588    -0.0716178  -0.12454    136 ASP   A HB2  
1827 H HB3  . ASP   A 124 ? 0.452215 0.960323 0.673495 0.18553     -0.0640848  -0.128409   136 ASP   A HB3  
1828 N N    . PHE   A 125 ? 0.536927 0.878597 0.69662  0.221962    -0.0878813  -0.111765   137 PHE   A N    
1829 C CA   . PHE   A 125 ? 0.561935 0.845143 0.701378 0.237594    -0.0864101  -0.115353   137 PHE   A CA   
1830 C C    . PHE   A 125 ? 0.609481 0.891105 0.751739 0.282236    -0.0975573  -0.124174   137 PHE   A C    
1831 O O    . PHE   A 125 ? 0.653707 0.947379 0.800716 0.301338    -0.111404   -0.118281   137 PHE   A O    
1832 C CB   . PHE   A 125 ? 0.562774 0.769551 0.672661 0.222169    -0.0904036  -0.100453   137 PHE   A CB   
1833 C CG   . PHE   A 125 ? 0.586426 0.770511 0.685713 0.229583    -0.106068   -0.0856052  137 PHE   A CG   
1834 C CD1  . PHE   A 125 ? 0.551885 0.757963 0.653718 0.207322    -0.108108   -0.0763175  137 PHE   A CD1  
1835 C CD2  . PHE   A 125 ? 0.648324 0.786774 0.73283  0.258483    -0.118882   -0.0807635  137 PHE   A CD2  
1836 C CE1  . PHE   A 125 ? 0.563922 0.754023 0.653364 0.214398    -0.122167   -0.0627391  137 PHE   A CE1  
1837 C CE2  . PHE   A 125 ? 0.681135 0.800712 0.753377 0.264929    -0.132929   -0.0638654  137 PHE   A CE2  
1838 C CZ   . PHE   A 125 ? 0.638141 0.787412 0.712745 0.243057    -0.134313   -0.0550042  137 PHE   A CZ   
1839 H H    . PHE   A 125 ? 0.542096 0.904128 0.709303 0.237008    -0.0972889  -0.1113     137 PHE   A H    
1840 H HA   . PHE   A 125 ? 0.55055  0.846687 0.693605 0.229171    -0.0751556  -0.122591   137 PHE   A HA   
1841 H HB2  . PHE   A 125 ? 0.583642 0.753731 0.681537 0.231337    -0.0899154  -0.104101   137 PHE   A HB2  
1842 H HB3  . PHE   A 125 ? 0.542592 0.750695 0.650741 0.196795    -0.082506   -0.0967553  137 PHE   A HB3  
1843 H HD1  . PHE   A 125 ? 0.529936 0.761045 0.640753 0.187229    -0.0999524  -0.0794028  137 PHE   A HD1  
1844 H HD2  . PHE   A 125 ? 0.665983 0.785595 0.747834 0.27415     -0.118247   -0.0888598  137 PHE   A HD2  
1845 H HE1  . PHE   A 125 ? 0.559739 0.766903 0.650147 0.199736    -0.123625   -0.0586786  137 PHE   A HE1  
1846 H HE2  . PHE   A 125 ? 0.706646 0.792169 0.767718 0.284412    -0.14172    -0.0585369  137 PHE   A HE2  
1847 H HZ   . PHE   A 125 ? 0.6479   0.787397 0.712637 0.24773     -0.143762   -0.0436876  137 PHE   A HZ   
1848 N N    . LYS   A 126 ? 0.631842 0.89829  0.769781 0.300013    -0.0919202  -0.139018   138 LYS   A N    
1849 C CA   . LYS   A 126 ? 0.636782 0.897673 0.776502 0.345513    -0.100968   -0.151987   138 LYS   A CA   
1850 C C    . LYS   A 126 ? 0.674418 0.848719 0.785524 0.353488    -0.103372   -0.155986   138 LYS   A C    
1851 O O    . LYS   A 126 ? 0.617344 0.769477 0.716965 0.328588    -0.0925123  -0.158815   138 LYS   A O    
1852 C CB   . LYS   A 126 ? 0.619489 0.964227 0.786894 0.362365    -0.0911097  -0.172526   138 LYS   A CB   
1853 H H    . LYS   A 126 ? 0.609416 0.868008 0.74217  0.283863    -0.082236   -0.141919   138 LYS   A H    
1854 H HA   . LYS   A 126 ? 0.656879 0.916297 0.797878 0.359839    -0.11262    -0.144218   138 LYS   A HA   
1857 N N    . GLY   A 127 ? 0.73566  0.859444 0.834561 0.387244    -0.11864    -0.155158   139 GLY   A N    
1858 C CA   . GLY   A 127 ? 0.798889 0.833665 0.870361 0.394013    -0.123366   -0.158883   139 GLY   A CA   
1859 C C    . GLY   A 127 ? 0.836657 0.881179 0.909821 0.407156    -0.113477   -0.187401   139 GLY   A C    
1860 O O    . GLY   A 127 ? 0.837048 0.95271  0.932402 0.428528    -0.107553   -0.20441    139 GLY   A O    
1861 H H    . GLY   A 127 ? 0.747097 0.891873 0.854856 0.406259    -0.126812   -0.151927   139 GLY   A H    
1862 H HA2  . GLY   A 127 ? 0.787711 0.789309 0.84585  0.366213    -0.121273   -0.147236   139 GLY   A HA2  
1863 H HA3  . GLY   A 127 ? 0.839302 0.840162 0.90341  0.417611    -0.135607   -0.154332   139 GLY   A HA3  
1864 N N    . GLU   A 128 ? 0.875538 0.854371 0.925487 0.393126    -0.111587   -0.193026   140 GLU   A N    
1865 C CA   . GLU   A 128 ? 0.899737 0.881303 0.946102 0.404901    -0.103641   -0.221828   140 GLU   A CA   
1866 C C    . GLU   A 128 ? 0.990243 0.954862 1.03714  0.457587    -0.114272   -0.242525   140 GLU   A C    
1867 O O    . GLU   A 128 ? 1.03546  0.960555 1.07805  0.478904    -0.129759   -0.228939   140 GLU   A O    
1868 C CB   . GLU   A 128 ? 0.884683 0.799449 0.905578 0.377016    -0.101766   -0.223582   140 GLU   A CB   
1869 O OXT  . GLU   A 128 ? 1.04938  1.04359  1.10036  0.477592    -0.106785   -0.271322   140 GLU   A OXT  
1870 H H    . GLU   A 128 ? 0.875561 0.809104 0.911349 0.375272    -0.11554    -0.178963   140 GLU   A H    
1871 H HA   . GLU   A 128 ? 0.863041 0.907711 0.924211 0.397899    -0.0922845  -0.227894   140 GLU   A HA   
1874 N N    . GLY   B 1   ? 0.566408 1.11751  0.484152 0.308646    -0.205242   -0.0520297  13  GLY   B N    
1875 C CA   . GLY   B 1   ? 0.516732 1.08864  0.495193 0.275304    -0.196869   -0.0838362  13  GLY   B CA   
1876 C C    . GLY   B 1   ? 0.5059   1.05384  0.461914 0.249216    -0.181116   -0.0847092  13  GLY   B C    
1877 O O    . GLY   B 1   ? 0.549136 1.07258  0.445916 0.256662    -0.177629   -0.0645933  13  GLY   B O    
1878 H H1   . GLY   B 1   ? 0.575609 1.13957  0.509161 0.324918    -0.214278   -0.0512998  13  GLY   B H1   
1879 H H2   . GLY   B 1   ? 0.569865 1.07837  0.462566 0.302798    -0.188364   -0.0297461  13  GLY   B H2   
1880 H H3   . GLY   B 1   ? 0.592719 1.15994  0.481782 0.319716    -0.217889   -0.0550626  13  GLY   B H3   
1881 H HA2  . GLY   B 1   ? 0.515832 1.13382  0.524204 0.280322    -0.214618   -0.10926    13  GLY   B HA2  
1882 H HA3  . GLY   B 1   ? 0.493945 1.05002  0.500627 0.265513    -0.183409   -0.0800907  13  GLY   B HA3  
1883 N N    . ALA   B 2   ? 0.458904 1.01169  0.464462 0.218918    -0.169021   -0.106459   14  ALA   B N    
1884 C CA   . ALA   B 2   ? 0.465648 0.998631 0.460551 0.194637    -0.154729   -0.110538   14  ALA   B CA   
1885 C C    . ALA   B 2   ? 0.46395  0.938377 0.409843 0.190467    -0.133981   -0.0745166  14  ALA   B C    
1886 O O    . ALA   B 2   ? 0.495782 0.959768 0.40258  0.1894      -0.13031    -0.0684217  14  ALA   B O    
1887 C CB   . ALA   B 2   ? 0.435208 0.9738   0.492385 0.165396    -0.142563   -0.133275   14  ALA   B CB   
1888 H H    . ALA   B 2   ? 0.44652  1.01491  0.494619 0.213978    -0.168853   -0.118538   14  ALA   B H    
1889 H HA   . ALA   B 2   ? 0.47993  1.03602  0.458628 0.201461    -0.167237   -0.123243   14  ALA   B HA   
1890 H HB1  . ALA   B 2   ? 0.429671 1.00647  0.519584 0.166285    -0.155181   -0.158238   14  ALA   B HB1  
1891 H HB2  . ALA   B 2   ? 0.417454 0.938177 0.490149 0.16068     -0.131523   -0.122973   14  ALA   B HB2  
1892 H HB3  . ALA   B 2   ? 0.421577 0.943205 0.471209 0.150786    -0.132625   -0.133607   14  ALA   B HB3  
1893 N N    . PRO   B 3   ? 0.463251 0.898976 0.411816 0.187007    -0.118893   -0.0521036  15  PRO   B N    
1894 C CA   . PRO   B 3   ? 0.476598 0.858977 0.385298 0.18152     -0.100737   -0.0217593  15  PRO   B CA   
1895 C C    . PRO   B 3   ? 0.51496  0.886149 0.364643 0.202367    -0.104403   0.00029429  15  PRO   B C    
1896 O O    . PRO   B 3   ? 0.488402 0.834895 0.309083 0.192812    -0.0909729  0.0129059   15  PRO   B O    
1897 C CB   . PRO   B 3   ? 0.48467  0.837091 0.408756 0.180576    -0.0903251  -0.00812623 15  PRO   B CB   
1898 C CG   . PRO   B 3   ? 0.457807 0.844284 0.438455 0.173167    -0.09424    -0.0342825  15  PRO   B CG   
1899 C CD   . PRO   B 3   ? 0.46674  0.908297 0.459848 0.186123    -0.1166     -0.0577147  15  PRO   B CD   
1900 H HA   . PRO   B 3   ? 0.458878 0.831693 0.373906 0.16329     -0.0912123  -0.0263143  15  PRO   B HA   
1901 H HB2  . PRO   B 3   ? 0.506058 0.851327 0.411725 0.198859    -0.0947894  0.00543432  15  PRO   B HB2  
1902 H HB3  . PRO   B 3   ? 0.471461 0.792388 0.389737 0.166567    -0.0766472  0.00166935  15  PRO   B HB3  
1903 H HG2  . PRO   B 3   ? 0.458489 0.839291 0.449616 0.180469    -0.0922805  -0.0293735  15  PRO   B HG2  
1904 H HG3  . PRO   B 3   ? 0.433127 0.812224 0.431092 0.153684    -0.0843334  -0.0413752  15  PRO   B HG3  
1905 H HD2  . PRO   B 3   ? 0.480745 0.937075 0.471386 0.206097    -0.128016   -0.0551732  15  PRO   B HD2  
1906 H HD3  . PRO   B 3   ? 0.440313 0.904348 0.471421 0.174005    -0.117048   -0.0785598  15  PRO   B HD3  
1907 N N    . ALA   B 4   ? 0.553757 0.942752 0.3859   0.231948    -0.121387   0.00623926  16  ALA   B N    
1908 C CA   . ALA   B 4   ? 0.608987 0.984037 0.379381 0.255337    -0.123826   0.0312299   16  ALA   B CA   
1909 C C    . ALA   B 4   ? 0.637458 1.03929  0.380319 0.25483     -0.129424   0.017371    16  ALA   B C    
1910 O O    . ALA   B 4   ? 0.678317 1.05615  0.369903 0.259942    -0.1177     0.0392228   16  ALA   B O    
1911 C CB   . ALA   B 4   ? 0.641658 1.03272  0.401715 0.290158    -0.143746   0.0392501   16  ALA   B CB   
1912 H H    . ALA   B 4   ? 0.544869 0.95495  0.404024 0.238568    -0.131134   -0.00469508 16  ALA   B H    
1913 H HA   . ALA   B 4   ? 0.616642 0.951085 0.369635 0.248651    -0.10683    0.052886    16  ALA   B HA   
1914 H HB1  . ALA   B 4   ? 0.633145 1.0057   0.411814 0.290023    -0.138192   0.0469087   16  ALA   B HB1  
1915 H HB2  . ALA   B 4   ? 0.637321 1.07115  0.417715 0.296778    -0.161729   0.0165143   16  ALA   B HB2  
1916 H HB3  . ALA   B 4   ? 0.685356 1.06264  0.400495 0.306995    -0.144085   0.059152    16  ALA   B HB3  
1917 N N    . THR   B 5   ? 0.608541 1.0589   0.387115 0.247706    -0.145027   -0.020076   17  THR   B N    
1918 C CA   . THR   B 5   ? 0.623337 1.10091  0.378667 0.247348    -0.15129    -0.0393353  17  THR   B CA   
1919 C C    . THR   B 5   ? 0.614131 1.05983  0.366931 0.219876    -0.124834   -0.0341879  17  THR   B C    
1920 O O    . THR   B 5   ? 0.669927 1.11653  0.383318 0.222313    -0.118807   -0.0331335  17  THR   B O    
1921 C CB   . THR   B 5   ? 0.595947 1.13147  0.398694 0.244625    -0.174554   -0.0843472  17  THR   B CB   
1922 O OG1  . THR   B 5   ? 0.612353 1.18003  0.413001 0.274379    -0.20069    -0.086634   17  THR   B OG1  
1923 C CG2  . THR   B 5   ? 0.600857 1.16421  0.383802 0.24261     -0.18123    -0.110605   17  THR   B CG2  
1924 H H    . THR   B 5   ? 0.583491 1.04995  0.402516 0.242869    -0.150986   -0.03481    17  THR   B H    
1925 H HA   . THR   B 5   ? 0.668496 1.14714  0.377873 0.268264    -0.157324   -0.0262305  17  THR   B HA   
1926 H HB   . THR   B 5   ? 0.552778 1.08604  0.402263 0.225318    -0.167712   -0.0952217  17  THR   B HB   
1928 H HG21 . THR   B 5   ? 0.603139 1.20555  0.41182  0.246162    -0.200087   -0.138863   17  THR   B HG21 
1929 H HG22 . THR   B 5   ? 0.645641 1.20359  0.376067 0.259414    -0.182176   -0.0956936  17  THR   B HG22 
1930 H HG23 . THR   B 5   ? 0.580141 1.12762  0.377628 0.221508    -0.165347   -0.114771   17  THR   B HG23 
1931 N N    . VAL   B 6   ? 0.54614  0.964832 0.340197 0.195009    -0.108835   -0.0313637  18  VAL   B N    
1932 C CA   . VAL   B 6   ? 0.512843 0.902871 0.308096 0.171398    -0.0863585  -0.0257286  18  VAL   B CA   
1933 C C    . VAL   B 6   ? 0.550102 0.899066 0.298042 0.177132    -0.0685208  0.0108994   18  VAL   B C    
1934 O O    . VAL   B 6   ? 0.542333 0.882592 0.268146 0.170314    -0.0539104  0.0158442   18  VAL   B O    
1935 C CB   . VAL   B 6   ? 0.44304  0.815319 0.290173 0.145949    -0.0762619  -0.0317841  18  VAL   B CB   
1936 C CG1  . VAL   B 6   ? 0.414219 0.758504 0.260425 0.125702    -0.0561011  -0.0241888  18  VAL   B CG1  
1937 C CG2  . VAL   B 6   ? 0.409908 0.818807 0.307123 0.137916    -0.0887768  -0.0662727  18  VAL   B CG2  
1938 H H    . VAL   B 6   ? 0.529228 0.948551 0.350796 0.193662    -0.112254   -0.0334061  18  VAL   B H    
1939 H HA   . VAL   B 6   ? 0.516512 0.925708 0.308848 0.168765    -0.0885734  -0.042381   18  VAL   B HA   
1940 H HB   . VAL   B 6   ? 0.44126  0.795275 0.289814 0.149237    -0.0742154  -0.0171268  18  VAL   B HB   
1941 H HG11 . VAL   B 6   ? 0.431969 0.789226 0.263795 0.127265    -0.0554261  -0.0319551  18  VAL   B HG11 
1942 H HG12 . VAL   B 6   ? 0.42862  0.745561 0.257359 0.126313    -0.0465979  -0.00242181 18  VAL   B HG12 
1943 H HG13 . VAL   B 6   ? 0.389311 0.730449 0.267927 0.11113     -0.0532296  -0.0339088  18  VAL   B HG13 
1944 H HG21 . VAL   B 6   ? 0.384018 0.778534 0.309191 0.122587    -0.0802576  -0.0673534  18  VAL   B HG21 
1945 H HG22 . VAL   B 6   ? 0.419452 0.847236 0.322607 0.150318    -0.101222   -0.0709006  18  VAL   B HG22 
1946 H HG23 . VAL   B 6   ? 0.416063 0.843537 0.312409 0.135903    -0.0922194  -0.0829903  18  VAL   B HG23 
1947 N N    . THR   B 7   ? 0.574208 0.896982 0.310888 0.188941    -0.0676414  0.0357337   19  THR   B N    
1948 C CA   . THR   B 7   ? 0.649233 0.930021 0.343726 0.195162    -0.0499566  0.0711691   19  THR   B CA   
1949 C C    . THR   B 7   ? 0.709868 1.00339  0.348108 0.213338    -0.0490968  0.0790762   19  THR   B C    
1950 O O    . THR   B 7   ? 0.745974 1.01624  0.359344 0.205542    -0.0268666  0.095869    19  THR   B O    
1951 C CB   . THR   B 7   ? 0.685172 0.941491 0.374419 0.211897    -0.0540004  0.0923349   19  THR   B CB   
1952 O OG1  . THR   B 7   ? 0.664276 0.902102 0.398674 0.191468    -0.048068   0.0862781   19  THR   B OG1  
1953 C CG2  . THR   B 7   ? 0.745627 0.959012 0.386643 0.224201    -0.0375452  0.130065    19  THR   B CG2  
1954 H H    . THR   B 7   ? 0.567589 0.897711 0.325395 0.192799    -0.0768841  0.0301826   19  THR   B H    
1955 H HA   . THR   B 7   ? 0.628344 0.887727 0.335486 0.176682    -0.0348963  0.0755166   19  THR   B HA   
1956 H HB   . THR   B 7   ? 0.695551 0.978008 0.384367 0.228902    -0.0714662  0.0836244   19  THR   B HB   
1958 H HG21 . THR   B 7   ? 0.74872  0.938003 0.396181 0.228199    -0.0358577  0.142187    19  THR   B HG21 
1959 H HG22 . THR   B 7   ? 0.741487 0.9378   0.38023  0.208503    -0.0207917  0.13602     19  THR   B HG22 
1960 H HG23 . THR   B 7   ? 0.781989 1.00844  0.388587 0.244161    -0.0447817  0.13604     19  THR   B HG23 
1961 N N    . GLU   B 8   ? 0.751791 1.08511  0.371286 0.237588    -0.0732562  0.0649662   20  GLU   B N    
1962 C CA   . GLU   B 8   ? 0.813037 1.15813  0.367529 0.261804    -0.0758698  0.0746768   20  GLU   B CA   
1963 C C    . GLU   B 8   ? 0.79998  1.17024  0.346685 0.250205    -0.0699925  0.0506275   20  GLU   B C    
1964 O O    . GLU   B 8   ? 0.858762 1.21875  0.352625 0.258063    -0.0540007  0.0667976   20  GLU   B O    
1965 C CB   . GLU   B 8   ? 0.844866 1.22706  0.380915 0.295159    -0.108382   0.0660222   20  GLU   B CB   
1966 H H    . GLU   B 8   ? 0.724799 1.07948  0.372409 0.239604    -0.0886781  0.048365    20  GLU   B H    
1967 H HA   . GLU   B 8   ? 0.843727 1.15501  0.368009 0.266396    -0.0596858  0.103951    20  GLU   B HA   
1970 N N    . GLN   B 9   ? 0.747766 1.15166  0.345041 0.233859    -0.0823464  0.0113895   21  GLN   B N    
1971 C CA   . GLN   B 9   ? 0.773568 1.20611  0.365777 0.227144    -0.0815565  -0.0177844  21  GLN   B CA   
1972 C C    . GLN   B 9   ? 0.691903 1.10914  0.332301 0.194184    -0.061327   -0.0285092  21  GLN   B C    
1973 O O    . GLN   B 9   ? 0.687626 1.1217   0.327679 0.186951    -0.0556477  -0.0506386  21  GLN   B O    
1974 C CB   . GLN   B 9   ? 0.781622 1.2682   0.397162 0.23346     -0.111659   -0.0623072  21  GLN   B CB   
1975 C CG   . GLN   B 9   ? 0.843184 1.35948  0.438147 0.264093    -0.142263   -0.064638   21  GLN   B CG   
1976 C CD   . GLN   B 9   ? 0.95136  1.46532  0.460696 0.29545     -0.143407   -0.0412653  21  GLN   B CD   
1977 O OE1  . GLN   B 9   ? 1.0462   1.58581  0.516095 0.305247    -0.148339   -0.0599372  21  GLN   B OE1  
1978 N NE2  . GLN   B 9   ? 1.03225  1.51253  0.510278 0.312127    -0.137393   0.00028193  21  GLN   B NE2  
1979 H H    . GLN   B 9   ? 0.719505 1.12769  0.35558  0.227128    -0.0905714  0.00225477  21  GLN   B H    
1980 H HA   . GLN   B 9   ? 0.810733 1.23854  0.354076 0.23906     -0.0731149  -0.00466864 21  GLN   B HA   
1981 H HB2  . GLN   B 9   ? 0.735625 1.22525  0.402866 0.215742    -0.113003   -0.078142   21  GLN   B HB2  
1982 H HB3  . GLN   B 9   ? 0.800646 1.30192  0.397827 0.233992    -0.109667   -0.077545   21  GLN   B HB3  
1983 H HG2  . GLN   B 9   ? 0.82681  1.32886  0.441211 0.264631    -0.143514   -0.0501541  21  GLN   B HG2  
1984 H HG3  . GLN   B 9   ? 0.833434 1.38578  0.453667 0.263836    -0.160752   -0.0968724  21  GLN   B HG3  
1985 H HE21 . GLN   B 9   ? 1.03349  1.48217  0.483867 0.310467    -0.116655   0.0259293   21  GLN   B HE21 
1986 H HE22 . GLN   B 9   ? 1.01716  1.50636  0.503807 0.325033    -0.15366    0.00192845  21  GLN   B HE22 
1987 N N    . GLY   B 10  ? 0.617115 1.00415  0.298308 0.176356    -0.0522474  -0.014997   22  GLY   B N    
1988 C CA   . GLY   B 10  ? 0.551118 0.928274 0.282803 0.148217    -0.0401643  -0.0280373  22  GLY   B CA   
1989 C C    . GLY   B 10  ? 0.555773 0.911821 0.271957 0.137634    -0.0137447  -0.0141164  22  GLY   B C    
1990 O O    . GLY   B 10  ? 0.588737 0.919563 0.269185 0.143957    0.00160999  0.0163701   22  GLY   B O    
1991 H H    . GLY   B 10  ? 0.627071 0.998649 0.302794 0.183066    -0.0539158  0.00278253  22  GLY   B H    
1992 H HA2  . GLY   B 10  ? 0.538519 0.940204 0.291982 0.144371    -0.0497273  -0.0547509  22  GLY   B HA2  
1993 H HA3  . GLY   B 10  ? 0.527151 0.887445 0.28414  0.14015     -0.039685   -0.0203189  22  GLY   B HA3  
1994 N N    . GLU   B 11  ? 0.535672 0.90195  0.284197 0.121315    -0.00764573 -0.0372139  23  GLU   B N    
1995 C CA   . GLU   B 11  ? 0.540413 0.894159 0.288078 0.110026    0.0168002   -0.0305982  23  GLU   B CA   
1996 C C    . GLU   B 11  ? 0.479108 0.799798 0.26358  0.0909114   0.027958    -0.0127873  23  GLU   B C    
1997 O O    . GLU   B 11  ? 0.375345 0.690868 0.199581 0.0806979   0.0170073   -0.0211143  23  GLU   B O    
1998 C CB   . GLU   B 11  ? 0.602827 0.98638  0.368346 0.10642     0.013425    -0.0673845  23  GLU   B CB   
1999 C CG   . GLU   B 11  ? 0.636879 1.01258  0.435713 0.0891966   0.0326517   -0.073653   23  GLU   B CG   
2000 C CD   . GLU   B 11  ? 0.697066 1.10057  0.503936 0.0903858   0.0320259   -0.10964    23  GLU   B CD   
2001 O OE1  . GLU   B 11  ? 0.785563 1.21529  0.559125 0.105782    0.0202323   -0.128078   23  GLU   B OE1  
2002 O OE2  . GLU   B 11  ? 0.772326 1.17144  0.619986 0.0769334   0.0422349   -0.120933   23  GLU   B OE2  
2003 H H    . GLU   B 11  ? 0.513926 0.895787 0.289565 0.117092    -0.0188356  -0.0584657  23  GLU   B H    
2004 H HA   . GLU   B 11  ? 0.583666 0.933205 0.291848 0.120133    0.0265596   -0.014999   23  GLU   B HA   
2005 H HB2  . GLU   B 11  ? 0.633646 1.03353  0.363313 0.11964     0.0123647   -0.0728913  23  GLU   B HB2  
2006 H HB3  . GLU   B 11  ? 0.574336 0.968697 0.365967 0.103802    -0.00159013 -0.0848128  23  GLU   B HB3  
2007 H HG2  . GLU   B 11  ? 0.597902 0.961048 0.432961 0.0774051   0.0300724   -0.0726872  23  GLU   B HG2  
2008 H HG3  . GLU   B 11  ? 0.65142  1.01518  0.432791 0.088989    0.0491823   -0.0550804  23  GLU   B HG3  
2009 N N    . ASP   B 12  ? 0.484812 0.783273 0.255688 0.0862245   0.0502107   0.0114408   24  ASP   B N    
2010 C CA   . ASP   B 12  ? 0.442579 0.713497 0.250752 0.067511    0.0594849   0.0241569   24  ASP   B CA   
2011 C C    . ASP   B 12  ? 0.400465 0.682377 0.251636 0.0525233   0.0651769   0.00442891  24  ASP   B C    
2012 O O    . ASP   B 12  ? 0.414594 0.707952 0.260877 0.0517601   0.0821538   0.00048435  24  ASP   B O    
2013 C CB   . ASP   B 12  ? 0.469683 0.713641 0.255877 0.0663365   0.081127    0.0549681   24  ASP   B CB   
2014 C CG   . ASP   B 12  ? 0.432652 0.649448 0.258047 0.047002    0.0889138   0.0658762   24  ASP   B CG   
2015 O OD1  . ASP   B 12  ? 0.381083 0.59925  0.246565 0.0361043   0.0760005   0.0510463   24  ASP   B OD1  
2016 O OD2  . ASP   B 12  ? 0.439699 0.632786 0.25413  0.043547    0.107602    0.089355    24  ASP   B OD2  
2017 H H    . ASP   B 12  ? 0.51976  0.82075  0.258208 0.0947253   0.0598783   0.0195622   24  ASP   B H    
2018 H HA   . ASP   B 12  ? 0.421817 0.684205 0.243311 0.065933    0.0475841   0.0247228   24  ASP   B HA   
2019 H HB2  . ASP   B 12  ? 0.491276 0.726481 0.248725 0.0780189   0.077169    0.0681006   24  ASP   B HB2  
2020 H HB3  . ASP   B 12  ? 0.490123 0.742699 0.262418 0.0678622   0.0954407   0.0554412   24  ASP   B HB3  
2021 N N    . ILE   B 13  ? 0.369367 0.648028 0.260849 0.0427679   0.0516185   -0.00788731 25  ILE   B N    
2022 C CA   . ILE   B 13  ? 0.349274 0.636627 0.281789 0.0322405   0.0533009   -0.0265845  25  ILE   B CA   
2023 C C    . ILE   B 13  ? 0.332877 0.599174 0.298022 0.0182343   0.0579576   -0.0144997  25  ILE   B C    
2024 O O    . ILE   B 13  ? 0.343057 0.611435 0.344906 0.0110684   0.0543076   -0.0265438  25  ILE   B O    
2025 C CB   . ILE   B 13  ? 0.349687 0.648408 0.303717 0.0326742   0.0361304   -0.0500608  25  ILE   B CB   
2026 C CG1  . ILE   B 13  ? 0.340725 0.622306 0.303363 0.0301018   0.0227772   -0.0418896  25  ILE   B CG1  
2027 C CG2  . ILE   B 13  ? 0.399955 0.726571 0.330187 0.0451162   0.0303703   -0.0700816  25  ILE   B CG2  
2028 C CD1  . ILE   B 13  ? 0.349374 0.636559 0.342826 0.0261708   0.0117005   -0.0617561  25  ILE   B CD1  
2029 H H    . ILE   B 13  ? 0.359518 0.629017 0.251983 0.043664    0.041888    -0.00346874 25  ILE   B H    
2030 H HA   . ILE   B 13  ? 0.368123 0.668392 0.294133 0.034583    0.0635269   -0.0328301  25  ILE   B HA   
2031 H HB   . ILE   B 13  ? 0.338197 0.637707 0.319456 0.0262651   0.0384401   -0.0594747  25  ILE   B HB   
2032 H HG12 . ILE   B 13  ? 0.357879 0.640659 0.296621 0.0379901   0.0191071   -0.0349136  25  ILE   B HG12 
2033 H HG13 . ILE   B 13  ? 0.336449 0.600575 0.308031 0.023556    0.0259578   -0.0295437  25  ILE   B HG13 
2034 H HG21 . ILE   B 13  ? 0.377759 0.711866 0.329574 0.0427291   0.022011    -0.0876721  25  ILE   B HG21 
2035 H HG22 . ILE   B 13  ? 0.406138 0.733683 0.310864 0.0533386   0.0249068   -0.0617622  25  ILE   B HG22 
2036 H HG23 . ILE   B 13  ? 0.408783 0.74499  0.328211 0.0477487   0.0405338   -0.0743133  25  ILE   B HG23 
2037 H HD11 . ILE   B 13  ? 0.33056  0.61687  0.345681 0.0206121   0.0153418   -0.0693652  25  ILE   B HD11 
2038 H HD12 . ILE   B 13  ? 0.328126 0.601969 0.327148 0.0235806   0.00688687  -0.0540696  25  ILE   B HD12 
2039 H HD13 . ILE   B 13  ? 0.347764 0.652439 0.334593 0.0321112   0.00641788  -0.074911   25  ILE   B HD13 
2040 N N    . THR   B 14  ? 0.321763 0.567427 0.275195 0.0150098   0.065147    0.00811763  26  THR   B N    
2041 C CA   . THR   B 14  ? 0.301959 0.531648 0.288353 0.00124963  0.0684091   0.0156724   26  THR   B CA   
2042 C C    . THR   B 14  ? 0.313458 0.555992 0.318745 -0.00508068 0.0885957   0.0147365   26  THR   B C    
2043 O O    . THR   B 14  ? 0.348562 0.601906 0.327998 0.00106398  0.105509    0.018265    26  THR   B O    
2044 C CB   . THR   B 14  ? 0.313135 0.514016 0.286825 -0.00160684 0.0675393   0.0357556   26  THR   B CB   
2045 O OG1  . THR   B 14  ? 0.340263 0.535032 0.283378 0.00297091  0.085584    0.053046    26  THR   B OG1  
2046 C CG2  . THR   B 14  ? 0.301279 0.491149 0.261358 0.00507098  0.0495311   0.0352492   26  THR   B CG2  
2047 H H    . THR   B 14  ? 0.346257 0.587499 0.271688 0.0218343   0.0674233   0.0183069   26  THR   B H    
2048 H HA   . THR   B 14  ? 0.281548 0.511517 0.289653 -0.00185889 0.0576339   0.00627577  26  THR   B HA   
2049 H HB   . THR   B 14  ? 0.30238  0.495315 0.300977 -0.0113281  0.0675942   0.0367368   26  THR   B HB   
2051 H HG21 . THR   B 14  ? 0.312431 0.483616 0.262899 0.00467093  0.050499    0.0472985   26  THR   B HG21 
2052 H HG22 . THR   B 14  ? 0.307411 0.509047 0.249262 0.0144148   0.0467781   0.0311207   26  THR   B HG22 
2053 H HG23 . THR   B 14  ? 0.280301 0.470219 0.260384 0.00085455  0.0403224   0.0265144   26  THR   B HG23 
2054 N N    . SER   B 15  ? 0.306648 0.549797 0.356954 -0.0159517  0.0864701   0.00929472  27  SER   B N    
2055 C CA   . SER   B 15  ? 0.356195 0.613313 0.43729  -0.0238014  0.105565    0.00805814  27  SER   B CA   
2056 C C    . SER   B 15  ? 0.372903 0.615275 0.444281 -0.0313016  0.125062    0.0288399   27  SER   B C    
2057 O O    . SER   B 15  ? 0.380965 0.634062 0.44985  -0.0327711  0.150786    0.0339437   27  SER   B O    
2058 C CB   . SER   B 15  ? 0.343184 0.605198 0.47723  -0.0316515  0.0936788   -0.00235455 27  SER   B CB   
2059 O OG   . SER   B 15  ? 0.339244 0.609336 0.482413 -0.0241235  0.0787281   -0.0186016  27  SER   B OG   
2060 H H    . SER   B 15  ? 0.293963 0.529736 0.357033 -0.0179057  0.0725949   0.00605909  27  SER   B H    
2061 H HA   . SER   B 15  ? 0.355825 0.629502 0.430153 -0.0182303  0.11466     -9.495e-05  27  SER   B HA   
2062 H HB2  . SER   B 15  ? 0.338529 0.585079 0.476838 -0.0366563  0.0839422   0.00406253  27  SER   B HB2  
2063 H HB3  . SER   B 15  ? 0.348855 0.623413 0.507696 -0.0365136  0.10638     -0.0043201  27  SER   B HB3  
2065 N N    . LYS   B 16  ? 0.371798 0.586966 0.435669 -0.0355459  0.114924    0.0411313   28  LYS   B N    
2066 C CA   . LYS   B 16  ? 0.432052 0.625856 0.491566 -0.044018   0.132818    0.0607736   28  LYS   B CA   
2067 C C    . LYS   B 16  ? 0.445138 0.628129 0.448008 -0.0317165  0.148516    0.0791983   28  LYS   B C    
2068 O O    . LYS   B 16  ? 0.507231 0.671187 0.502241 -0.0370102  0.169889    0.0985748   28  LYS   B O    
2069 C CB   . LYS   B 16  ? 0.453514 0.618768 0.522864 -0.0515526  0.116948    0.0654603   28  LYS   B CB   
2070 C CG   . LYS   B 16  ? 0.470887 0.641922 0.592926 -0.0642527  0.101893    0.0509037   28  LYS   B CG   
2071 C CD   . LYS   B 16  ? 0.545428 0.685334 0.668258 -0.0711671  0.0899635   0.0554846   28  LYS   B CD   
2072 C CE   . LYS   B 16  ? 0.566742 0.705338 0.704074 -0.071139   0.0610296   0.0408988   28  LYS   B CE   
2073 N NZ   . LYS   B 16  ? 0.575069 0.736556 0.763772 -0.0796647  0.052882    0.0259499   28  LYS   B NZ   
2074 H H    . LYS   B 16  ? 0.36193  0.570335 0.424123 -0.0332385  0.0977044   0.0369298   28  LYS   B H    
2075 H HA   . LYS   B 16  ? 0.430013 0.633945 0.518349 -0.0528643  0.146869    0.0593299   28  LYS   B HA   
2076 H HB2  . LYS   B 16  ? 0.449115 0.607206 0.494726 -0.0427875  0.103042    0.0648821   28  LYS   B HB2  
2077 H HB3  . LYS   B 16  ? 0.482012 0.629638 0.543544 -0.055618   0.130134    0.0791654   28  LYS   B HB3  
2078 H HG2  . LYS   B 16  ? 0.479321 0.662717 0.631071 -0.0726545  0.114546    0.0488893   28  LYS   B HG2  
2079 H HG3  . LYS   B 16  ? 0.453093 0.635834 0.579141 -0.0587913  0.087383    0.0398055   28  LYS   B HG3  
2080 H HD2  . LYS   B 16  ? 0.549932 0.672711 0.638826 -0.0641275  0.0920265   0.065881    28  LYS   B HD2  
2081 H HD3  . LYS   B 16  ? 0.552942 0.687864 0.698989 -0.0825316  0.101338    0.0587494   28  LYS   B HD3  
2082 H HE2  . LYS   B 16  ? 0.548039 0.690618 0.665271 -0.0610714  0.0521576   0.0383299   28  LYS   B HE2  
2083 H HE3  . LYS   B 16  ? 0.57056  0.687916 0.70147  -0.0741605  0.0556103   0.0437352   28  LYS   B HE3  
2084 H HZ1  . LYS   B 16  ? 0.556712 0.736647 0.750811 -0.0748663  0.0549919   0.0216792   28  LYS   B HZ1  
2085 H HZ2  . LYS   B 16  ? 0.578783 0.741493 0.791193 -0.0897331  0.0633218   0.0270721   28  LYS   B HZ2  
2086 H HZ3  . LYS   B 16  ? 0.559798 0.716208 0.752329 -0.0791083  0.0352637   0.0193273   28  LYS   B HZ3  
2087 N N    . LYS   B 17  ? 0.443202 0.637448 0.407572 -0.014897   0.137681    0.0734164   29  LYS   B N    
2088 C CA   . LYS   B 17  ? 0.478504 0.66505  0.384826 0.00121695  0.145605    0.0896197   29  LYS   B CA   
2089 C C    . LYS   B 17  ? 0.487407 0.636595 0.37568  0.00228406  0.144756    0.112231    29  LYS   B C    
2090 O O    . LYS   B 17  ? 0.507053 0.637147 0.36529  0.00669223  0.165336    0.135591    29  LYS   B O    
2091 C CB   . LYS   B 17  ? 0.538257 0.738009 0.425341 0.00399675  0.175227    0.0966149   29  LYS   B CB   
2092 C CG   . LYS   B 17  ? 0.562829 0.799201 0.454215 0.00969331  0.173133    0.0713787   29  LYS   B CG   
2093 C CD   . LYS   B 17  ? 0.591786 0.84247  0.447129 0.0277392   0.150129    0.0573207   29  LYS   B CD   
2094 C CE   . LYS   B 17  ? 0.662145 0.946188 0.512987 0.0348276   0.153333    0.032482    29  LYS   B CE   
2095 N NZ   . LYS   B 17  ? 0.622996 0.91994  0.523661 0.0271026   0.135737    0.0063714   29  LYS   B NZ   
2096 H H    . LYS   B 17  ? 0.417232 0.624629 0.392653 -0.0128708  0.124019    0.0584414   29  LYS   B H    
2097 H HA   . LYS   B 17  ? 0.471238 0.669932 0.361813 0.0115249   0.130842    0.0791735   29  LYS   B HA   
2098 H HB2  . LYS   B 17  ? 0.547387 0.740737 0.460352 -0.0085219  0.191367    0.103076    29  LYS   B HB2  
2099 H HB3  . LYS   B 17  ? 0.576132 0.76602  0.421282 0.0151867   0.181508    0.111538    29  LYS   B HB3  
2100 H HG2  . LYS   B 17  ? 0.527913 0.772311 0.46097  0.00010559  0.166666    0.0579847   29  LYS   B HG2  
2101 H HG3  . LYS   B 17  ? 0.58897  0.83288  0.468463 0.0109436   0.194477    0.0759469   29  LYS   B HG3  
2102 H HD2  . LYS   B 17  ? 0.627817 0.868878 0.443679 0.0383774   0.151416    0.0715614   29  LYS   B HD2  
2103 H HD3  . LYS   B 17  ? 0.566038 0.813299 0.4408   0.0248617   0.131151    0.0494635   29  LYS   B HD3  
2104 H HE2  . LYS   B 17  ? 0.66688  0.956079 0.518379 0.0319659   0.174674    0.0361625   29  LYS   B HE2  
2105 H HE3  . LYS   B 17  ? 0.667563 0.959229 0.481457 0.0482624   0.146366    0.0294766   29  LYS   B HE3  
2106 H HZ1  . LYS   B 17  ? 0.601733 0.891585 0.535118 0.0162928   0.138683    0.00960848  29  LYS   B HZ1  
2107 H HZ2  . LYS   B 17  ? 0.604392 0.898354 0.502209 0.0303144   0.118057    0.0019647   29  LYS   B HZ2  
2108 H HZ3  . LYS   B 17  ? 0.62357  0.938205 0.525676 0.0304259   0.13991     -0.00884451 29  LYS   B HZ3  
2109 N N    . ASP   B 18  ? 0.434035 0.571222 0.337485 0.00016437  0.121808    0.105438    30  ASP   B N    
2110 C CA   . ASP   B 18  ? 0.465119 0.566669 0.356106 0.00202295  0.118318    0.121706    30  ASP   B CA   
2111 C C    . ASP   B 18  ? 0.459867 0.562291 0.317016 0.0217531   0.0987581   0.121073    30  ASP   B C    
2112 O O    . ASP   B 18  ? 0.482188 0.560173 0.335976 0.024953    0.089624    0.127203    30  ASP   B O    
2113 C CB   . ASP   B 18  ? 0.450867 0.538173 0.386721 -0.0158131  0.109369    0.112673    30  ASP   B CB   
2114 C CG   . ASP   B 18  ? 0.401929 0.508157 0.359004 -0.0169035  0.0852998   0.0898881   30  ASP   B CG   
2115 O OD1  . ASP   B 18  ? 0.371514 0.496932 0.30989  -0.00420277 0.0748389   0.0816144   30  ASP   B OD1  
2116 O OD2  . ASP   B 18  ? 0.376269 0.478173 0.368187 -0.0299874  0.077732    0.0805852   30  ASP   B OD2  
2117 H H    . ASP   B 18  ? 0.412902 0.563878 0.334446 -0.0018376  0.108638    0.0898156   30  ASP   B H    
2118 H HA   . ASP   B 18  ? 0.498381 0.584252 0.375188 0.00228254  0.135757    0.138788    30  ASP   B HA   
2119 H HB2  . ASP   B 18  ? 0.462595 0.524897 0.390829 -0.0148519  0.107835    0.12158     30  ASP   B HB2  
2120 H HB3  . ASP   B 18  ? 0.451708 0.540691 0.411759 -0.0278359  0.121714    0.112949    30  ASP   B HB3  
2121 N N    . ARG   B 19  ? 0.452507 0.585909 0.289732 0.034718    0.0913175   0.109912    31  ARG   B N    
2122 C CA   . ARG   B 19  ? 0.430293 0.575151 0.245359 0.0524765   0.0711682   0.103526    31  ARG   B CA   
2123 C C    . ARG   B 19  ? 0.385391 0.525664 0.229084 0.0468516   0.0524989   0.0904433   31  ARG   B C    
2124 O O    . ARG   B 19  ? 0.377537 0.519565 0.209394 0.05969     0.0391348   0.0891477   31  ARG   B O    
2125 C CB   . ARG   B 19  ? 0.469451 0.596459 0.23891  0.0721544   0.0747909   0.12718     31  ARG   B CB   
2126 C CG   . ARG   B 19  ? 0.515437 0.653052 0.243394 0.0839565   0.0903992   0.138725    31  ARG   B CG   
2127 C CD   . ARG   B 19  ? 0.572449 0.690946 0.249475 0.107899    0.0915784   0.164756    31  ARG   B CD   
2128 N NE   . ARG   B 19  ? 0.573918 0.705234 0.240087 0.12767     0.065009    0.157371    31  ARG   B NE   
2129 C CZ   . ARG   B 19  ? 0.592712 0.761972 0.238779 0.145432    0.0464748   0.141415    31  ARG   B CZ   
2130 N NH1  . ARG   B 19  ? 0.606186 0.805847 0.237327 0.146696    0.0492985   0.127298    31  ARG   B NH1  
2131 N NH2  . ARG   B 19  ? 0.607791 0.786858 0.250106 0.163174    0.0243316   0.137338    31  ARG   B NH2  
2132 H H    . ARG   B 19  ? 0.45015  0.599832 0.28995  0.0322809   0.0993217   0.104437    31  ARG   B H    
2133 H HA   . ARG   B 19  ? 0.425585 0.596022 0.235647 0.0572038   0.067373    0.0909019   31  ARG   B HA   
2134 H HB2  . ARG   B 19  ? 0.484516 0.583067 0.257967 0.0672103   0.0823132   0.141028    31  ARG   B HB2  
2135 H HB3  . ARG   B 19  ? 0.465775 0.601526 0.228011 0.083469    0.0594491   0.121457    31  ARG   B HB3  
2136 H HG2  . ARG   B 19  ? 0.50515  0.671488 0.229845 0.0884166   0.0825198   0.122156    31  ARG   B HG2  
2137 H HG3  . ARG   B 19  ? 0.524005 0.652612 0.260944 0.0723719   0.108437    0.145498    31  ARG   B HG3  
2138 H HD2  . ARG   B 19  ? 0.606602 0.733503 0.252926 0.116438    0.101237    0.171474    31  ARG   B HD2  
2139 H HD3  . ARG   B 19  ? 0.589617 0.676568 0.270334 0.102395    0.103167    0.181985    31  ARG   B HD3  
2140 H HE   . ARG   B 19  ? 0.570644 0.684255 0.247058 0.127648    0.0607941   0.162518    31  ARG   B HE   
2141 H HH11 . ARG   B 19  ? 0.582088 0.787436 0.23491  0.131895    0.0567015   0.116883    31  ARG   B HH11 
2142 H HH12 . ARG   B 19  ? 0.633062 0.847512 0.232281 0.163189    0.043306    0.127577    31  ARG   B HH12 
2143 H HH21 . ARG   B 19  ? 0.606319 0.764128 0.25239  0.166039    0.02366     0.148532    31  ARG   B HH21 
2144 H HH22 . ARG   B 19  ? 0.599092 0.806974 0.237305 0.172202    0.0102189   0.122216    31  ARG   B HH22 
2145 N N    . GLY   B 20  ? 0.361046 0.499259 0.241741 0.0294663   0.0513764   0.0796183   32  GLY   B N    
2146 C CA   . GLY   B 20  ? 0.323852 0.452265 0.225108 0.0241957   0.037113    0.0706927   32  GLY   B CA   
2147 C C    . GLY   B 20  ? 0.303706 0.456975 0.211792 0.0298158   0.0230819   0.0525212   32  GLY   B C    
2148 O O    . GLY   B 20  ? 0.314846 0.461039 0.229093 0.0311098   0.0133275   0.0482802   32  GLY   B O    
2149 H H    . GLY   B 20  ? 0.356074 0.500081 0.248722 0.0216199   0.0598302   0.07762     32  GLY   B H    
2150 H HA2  . GLY   B 20  ? 0.340729 0.450355 0.231136 0.0286137   0.0360261   0.0797715   32  GLY   B HA2  
2151 H HA3  . GLY   B 20  ? 0.316147 0.438948 0.238848 0.01246     0.0385293   0.0673786   32  GLY   B HA3  
2152 N N    . VAL   B 21  ? 0.308401 0.48983  0.217653 0.0320959   0.024251    0.040611    33  VAL   B N    
2153 C CA   . VAL   B 21  ? 0.29058  0.496854 0.211133 0.0357351   0.013187    0.0206156   33  VAL   B CA   
2154 C C    . VAL   B 21  ? 0.315468 0.548518 0.212684 0.0481036   0.0138119   0.0140821   33  VAL   B C    
2155 O O    . VAL   B 21  ? 0.306708 0.548204 0.199677 0.0457536   0.0245542   0.0123421   33  VAL   B O    
2156 C CB   . VAL   B 21  ? 0.27936  0.490908 0.234199 0.0234913   0.0120828   0.00572777  33  VAL   B CB   
2157 C CG1  . VAL   B 21  ? 0.284968 0.51629  0.25558  0.0255715   0.00319968  -0.0143586  33  VAL   B CG1  
2158 C CG2  . VAL   B 21  ? 0.271685 0.457929 0.243341 0.0131656   0.0103067   0.0126685   33  VAL   B CG2  
2159 H H    . VAL   B 21  ? 0.318993 0.503739 0.222853 0.030873    0.0335819   0.044377    33  VAL   B H    
2160 H HA   . VAL   B 21  ? 0.289278 0.49188  0.209322 0.0396814   0.00603014  0.0205547   33  VAL   B HA   
2161 H HB   . VAL   B 21  ? 0.285513 0.504615 0.242678 0.0211907   0.0192014   0.00371011  33  VAL   B HB   
2162 H HG11 . VAL   B 21  ? 0.276065 0.503708 0.24502  0.0285526   -0.00220278 -0.0129318  33  VAL   B HG11 
2163 H HG12 . VAL   B 21  ? 0.288238 0.538089 0.250856 0.0312292   0.00308923  -0.0226751  33  VAL   B HG12 
2164 H HG13 . VAL   B 21  ? 0.265257 0.494187 0.256748 0.018484    0.00351839  -0.0208325  33  VAL   B HG13 
2165 H HG21 . VAL   B 21  ? 0.256955 0.446702 0.247847 0.00803513  0.00856969  0.0044885   33  VAL   B HG21 
2166 H HG22 . VAL   B 21  ? 0.27934  0.455137 0.247665 0.0097712   0.0160319   0.0220964   33  VAL   B HG22 
2167 H HG23 . VAL   B 21  ? 0.268564 0.445711 0.235188 0.0157084   0.00525318  0.0152479   33  VAL   B HG23 
2168 N N    . LEU   B 22  ? 0.31254  0.560241 0.195687 0.0619545   0.00194492  0.00933097  34  LEU   B N    
2169 C CA   . LEU   B 22  ? 0.343286 0.619452 0.200157 0.0771128   -0.00313731 0.00059446  34  LEU   B CA   
2170 C C    . LEU   B 22  ? 0.335514 0.641975 0.218986 0.0768014   -0.017524   -0.0288354  34  LEU   B C    
2171 O O    . LEU   B 22  ? 0.295983 0.600541 0.20465  0.0734615   -0.0252812  -0.0336518  34  LEU   B O    
2172 C CB   . LEU   B 22  ? 0.391341 0.660455 0.211703 0.0960289   -0.00759839 0.0198871   34  LEU   B CB   
2173 C CG   . LEU   B 22  ? 0.425321 0.658599 0.221002 0.0962108   0.00880424  0.0505778   34  LEU   B CG   
2174 C CD1  . LEU   B 22  ? 0.477797 0.697115 0.244721 0.115831    0.00288951  0.0700672   34  LEU   B CD1  
2175 C CD2  . LEU   B 22  ? 0.460161 0.696922 0.228834 0.0971218   0.0255358   0.057643    34  LEU   B CD2  
2176 H H    . LEU   B 22  ? 0.307378 0.548339 0.198027 0.062651    -0.00388312 0.0106851   34  LEU   B H    
2177 H HA   . LEU   B 22  ? 0.358996 0.638233 0.205856 0.0755457   0.00618463  0.0010545   34  LEU   B HA   
2178 H HB2  . LEU   B 22  ? 0.376998 0.645313 0.210658 0.097948    -0.0164019  0.0175779   34  LEU   B HB2  
2179 H HB3  . LEU   B 22  ? 0.410392 0.700369 0.210204 0.108173    -0.0133373  0.0136191   34  LEU   B HB3  
2180 H HG   . LEU   B 22  ? 0.408203 0.623213 0.225926 0.082804    0.013922    0.0534477   34  LEU   B HG   
2181 H HD11 . LEU   B 22  ? 0.452655 0.670657 0.238239 0.115366    -0.00582805 0.0648814   34  LEU   B HD11 
2182 H HD12 . LEU   B 22  ? 0.490849 0.683701 0.245164 0.114405    0.0149673   0.0893613   34  LEU   B HD12 
2183 H HD13 . LEU   B 22  ? 0.494488 0.732531 0.237791 0.130872    -0.00394105 0.067992    34  LEU   B HD13 
2184 H HD21 . LEU   B 22  ? 0.43896  0.682526 0.229242 0.0849627   0.0303992   0.0460537   34  LEU   B HD21 
2185 H HD22 . LEU   B 22  ? 0.481277 0.737102 0.224987 0.110879    0.0198186   0.0530947   34  LEU   B HD22 
2186 H HD23 . LEU   B 22  ? 0.479581 0.692678 0.234914 0.0965777   0.0376649   0.0778889   34  LEU   B HD23 
2187 N N    . LYS   B 23  ? 0.330197 0.664701 0.206126 0.0814591   -0.0200542  -0.0487561  35  LYS   B N    
2188 C CA   . LYS   B 23  ? 0.318286 0.679652 0.22665  0.0771989   -0.0309482  -0.0809922  35  LYS   B CA   
2189 C C    . LYS   B 23  ? 0.361787 0.759773 0.244842 0.0941728   -0.0445048  -0.100143   35  LYS   B C    
2190 O O    . LYS   B 23  ? 0.395382 0.799461 0.237522 0.104387    -0.0387407  -0.096106   35  LYS   B O    
2191 C CB   . LYS   B 23  ? 0.314453 0.67177  0.249737 0.0623241   -0.0201053  -0.0946713  35  LYS   B CB   
2192 C CG   . LYS   B 23  ? 0.308342 0.686802 0.281599 0.0560319   -0.0282011  -0.128652   35  LYS   B CG   
2193 C CD   . LYS   B 23  ? 0.300536 0.678745 0.295238 0.0469504   -0.0185392  -0.146224   35  LYS   B CD   
2194 C CE   . LYS   B 23  ? 0.288827 0.673292 0.331474 0.0368588   -0.023813   -0.173566   35  LYS   B CE   
2195 N NZ   . LYS   B 23  ? 0.283363 0.670335 0.344452 0.0321308   -0.0159886  -0.195165   35  LYS   B NZ   
2196 H H    . LYS   B 23  ? 0.358862 0.694802 0.208406 0.0873362   -0.0137743  -0.0424739  35  LYS   B H    
2197 H HA   . LYS   B 23  ? 0.304222 0.663122 0.235082 0.0735279   -0.0365894  -0.0829819  35  LYS   B HA   
2198 H HB2  . LYS   B 23  ? 0.295182 0.630743 0.245203 0.0530437   -0.0135778  -0.0826941  35  LYS   B HB2  
2199 H HB3  . LYS   B 23  ? 0.331228 0.691947 0.245362 0.0661167   -0.0127896  -0.0928162  35  LYS   B HB3  
2200 H HG2  . LYS   B 23  ? 0.322449 0.72429  0.284417 0.0653489   -0.0384056  -0.142073   35  LYS   B HG2  
2201 H HG3  . LYS   B 23  ? 0.286882 0.657167 0.285152 0.0493624   -0.0307268  -0.127919   35  LYS   B HG3  
2202 H HD2  . LYS   B 23  ? 0.291863 0.649967 0.291315 0.0408337   -0.00887638 -0.131264   35  LYS   B HD2  
2203 H HD3  . LYS   B 23  ? 0.324195 0.717492 0.296991 0.0543418   -0.0173678  -0.154733   35  LYS   B HD3  
2204 H HE2  . LYS   B 23  ? 0.293048 0.69786  0.336905 0.0413989   -0.0345363  -0.188182   35  LYS   B HE2  
2205 H HE3  . LYS   B 23  ? 0.266662 0.632724 0.329217 0.0291283   -0.0213719  -0.163142   35  LYS   B HE3  
2206 H HZ1  . LYS   B 23  ? 0.306324 0.712034 0.349279 0.0393886   -0.0185085  -0.20836    35  LYS   B HZ1  
2207 H HZ2  . LYS   B 23  ? 0.281312 0.652991 0.341413 0.0295015   -0.00672524 -0.182114   35  LYS   B HZ2  
2208 H HZ3  . LYS   B 23  ? 0.278322 0.663289 0.370721 0.025081    -0.0175004  -0.208999   35  LYS   B HZ3  
2209 N N    . ILE   B 24  ? 0.362446 0.786583 0.271382 0.0969761   -0.0621034  -0.122757   36  ILE   B N    
2210 C CA   . ILE   B 24  ? 0.393242 0.858748 0.29408  0.108726    -0.0787994  -0.153496   36  ILE   B CA   
2211 C C    . ILE   B 24  ? 0.378443 0.859208 0.336935 0.092091    -0.0826067  -0.189137   36  ILE   B C    
2212 O O    . ILE   B 24  ? 0.364079 0.838885 0.366974 0.0805894   -0.0831086  -0.191321   36  ILE   B O    
2213 C CB   . ILE   B 24  ? 0.433126 0.923085 0.316701 0.129712    -0.099845   -0.152142   36  ILE   B CB   
2214 C CG1  . ILE   B 24  ? 0.469175 0.937022 0.29691  0.14715     -0.0944425  -0.11396    36  ILE   B CG1  
2215 C CG2  . ILE   B 24  ? 0.460268 0.9989   0.338407 0.1427      -0.122208   -0.189077   36  ILE   B CG2  
2216 C CD1  . ILE   B 24  ? 0.515988 1.00886  0.320086 0.173519    -0.116909   -0.111844   36  ILE   B CD1  
2217 H H    . ILE   B 24  ? 0.341219 0.758376 0.274502 0.0913452   -0.0636962  -0.120103   36  ILE   B H    
2218 H HA   . ILE   B 24  ? 0.420108 0.887926 0.290449 0.114391    -0.0737491  -0.153127   36  ILE   B HA   
2219 H HB   . ILE   B 24  ? 0.406882 0.895462 0.323833 0.123507    -0.102828   -0.153278   36  ILE   B HB   
2220 H HG12 . ILE   B 24  ? 0.493426 0.956375 0.289292 0.150373    -0.0858142  -0.108495   36  ILE   B HG12 
2221 H HG13 . ILE   B 24  ? 0.451595 0.891495 0.289787 0.138574    -0.0835736  -0.0948028  36  ILE   B HG13 
2222 H HG21 . ILE   B 24  ? 0.468947 1.02628  0.34898  0.15438     -0.137764   -0.191512   36  ILE   B HG21 
2223 H HG22 . ILE   B 24  ? 0.491618 1.03295  0.327899 0.152968    -0.120358   -0.186067   36  ILE   B HG22 
2224 H HG23 . ILE   B 24  ? 0.443957 0.992435 0.35907  0.129555    -0.122741   -0.213964   36  ILE   B HG23 
2225 H HD11 . ILE   B 24  ? 0.490258 0.993643 0.330748 0.170351    -0.12563    -0.121321   36  ILE   B HD11 
2226 H HD12 . ILE   B 24  ? 0.531591 1.00303  0.303686 0.183452    -0.110887   -0.0842929  36  ILE   B HD12 
2227 H HD13 . ILE   B 24  ? 0.538675 1.05859  0.323486 0.184635    -0.128585   -0.128638   36  ILE   B HD13 
2228 N N    . VAL   B 25  ? 0.38174  0.882042 0.338504 0.0918608   -0.084337   -0.217964   37  VAL   B N    
2229 C CA   . VAL   B 25  ? 0.378742 0.896272 0.390107 0.0783844   -0.0902302  -0.256673   37  VAL   B CA   
2230 C C    . VAL   B 25  ? 0.395891 0.95662  0.419013 0.0890549   -0.115943   -0.282419   37  VAL   B C    
2231 O O    . VAL   B 25  ? 0.446104 1.03564  0.42552  0.109284    -0.1316     -0.291627   37  VAL   B O    
2232 C CB   . VAL   B 25  ? 0.407591 0.929879 0.412977 0.0758246   -0.0829171  -0.28114    37  VAL   B CB   
2233 C CG1  . VAL   B 25  ? 0.410688 0.953152 0.47011  0.0642838   -0.0912705  -0.327135   37  VAL   B CG1  
2234 C CG2  . VAL   B 25  ? 0.386573 0.871065 0.391637 0.0655443   -0.0586046  -0.258173   37  VAL   B CG2  
2235 H H    . VAL   B 25  ? 0.410568 0.912347 0.331797 0.100133    -0.0805334  -0.213858   37  VAL   B H    
2236 H HA   . VAL   B 25  ? 0.352094 0.850181 0.397512 0.0648689   -0.0819988  -0.250294   37  VAL   B HA   
2237 H HB   . VAL   B 25  ? 0.435981 0.974818 0.399569 0.0904635   -0.0887793  -0.283374   37  VAL   B HB   
2238 H HG11 . VAL   B 25  ? 0.384267 0.914156 0.484268 0.0517012   -0.0877042  -0.324767   37  VAL   B HG11 
2239 H HG12 . VAL   B 25  ? 0.428547 1.00159  0.481696 0.0732522   -0.108166   -0.347244   37  VAL   B HG12 
2240 H HG13 . VAL   B 25  ? 0.416694 0.953742 0.477388 0.0607929   -0.082833   -0.339372   37  VAL   B HG13 
2241 H HG21 . VAL   B 25  ? 0.400137 0.889427 0.405571 0.0646868   -0.0536774  -0.275637   37  VAL   B HG21 
2242 H HG22 . VAL   B 25  ? 0.394316 0.868575 0.365296 0.0725436   -0.0530179  -0.232616   37  VAL   B HG22 
2243 H HG23 . VAL   B 25  ? 0.361937 0.828042 0.401495 0.0533685   -0.0534564  -0.252121   37  VAL   B HG23 
2244 N N    . LYS   B 26  ? 0.35917  0.925639 0.441022 0.0764183   -0.119881   -0.293804   38  LYS   B N    
2245 C CA   . LYS   B 26  ? 0.363955 0.975905 0.471352 0.0843469   -0.14408    -0.321136   38  LYS   B CA   
2246 C C    . LYS   B 26  ? 0.375584 1.01487  0.534317 0.0713374   -0.152138   -0.37137    38  LYS   B C    
2247 O O    . LYS   B 26  ? 0.425782 1.11149  0.587164 0.0828285   -0.177007   -0.404028   38  LYS   B O    
2248 C CB   . LYS   B 26  ? 0.338676 0.945466 0.483588 0.0792024   -0.141916   -0.304774   38  LYS   B CB   
2249 C CG   . LYS   B 26  ? 0.345866 0.923955 0.444939 0.0919434   -0.134654   -0.258388   38  LYS   B CG   
2250 C CD   . LYS   B 26  ? 0.395083 0.993009 0.432228 0.1212      -0.152507   -0.248027   38  LYS   B CD   
2251 C CE   . LYS   B 26  ? 0.418438 1.06392  0.475773 0.136828    -0.178862   -0.268272   38  LYS   B CE   
2252 N NZ   . LYS   B 26  ? 0.481216 1.14359  0.47435  0.168421    -0.197353   -0.256012   38  LYS   B NZ   
2253 H H    . LYS   B 26  ? 0.337169 0.879447 0.444677 0.062804    -0.106756   -0.284239   38  LYS   B H    
2254 H HA   . LYS   B 26  ? 0.393754 1.02418  0.460076 0.103197    -0.157344   -0.318938   38  LYS   B HA   
2255 H HB2  . LYS   B 26  ? 0.318793 0.907169 0.501441 0.0613181   -0.12818    -0.306442   38  LYS   B HB2  
2256 H HB3  . LYS   B 26  ? 0.348312 0.989385 0.514373 0.0850304   -0.15843    -0.324695   38  LYS   B HB3  
2257 H HG2  . LYS   B 26  ? 0.336918 0.882557 0.420936 0.0845405   -0.118702   -0.240361   38  LYS   B HG2  
2258 H HG3  . LYS   B 26  ? 0.329531 0.905885 0.45573  0.08835     -0.132748   -0.252201   38  LYS   B HG3  
2259 H HD2  . LYS   B 26  ? 0.415263 1.01931  0.425412 0.125497    -0.154639   -0.257385   38  LYS   B HD2  
2260 H HD3  . LYS   B 26  ? 0.394525 0.966274 0.40311  0.126637    -0.143732   -0.217401   38  LYS   B HD3  
2261 H HE2  . LYS   B 26  ? 0.400812 1.04088  0.485436 0.133218    -0.175084   -0.258852   38  LYS   B HE2  
2262 H HE3  . LYS   B 26  ? 0.42077  1.09341  0.510381 0.130188    -0.188093   -0.300758   38  LYS   B HE3  
2263 H HZ1  . LYS   B 26  ? 0.477302 1.11215  0.441421 0.174034    -0.187577   -0.225814   38  LYS   B HZ1  
2264 H HZ2  . LYS   B 26  ? 0.497223 1.16714  0.463452 0.172646    -0.200843   -0.266299   38  LYS   B HZ2  
2265 H HZ3  . LYS   B 26  ? 0.48365  1.17631  0.492185 0.179126    -0.214965   -0.268241   38  LYS   B HZ3  
2266 N N    . ARG   B 27  ? 0.376888 0.987235 0.576518 0.0486361   -0.132417   -0.378514   39  ARG   B N    
2267 C CA   . ARG   B 27  ? 0.414016 1.04098  0.658919 0.0358809   -0.136164   -0.425706   39  ARG   B CA   
2268 C C    . ARG   B 27  ? 0.412435 1.00392  0.646234 0.0279994   -0.116015   -0.423275   39  ARG   B C    
2269 O O    . ARG   B 27  ? 0.39438  0.942664 0.632507 0.0183209   -0.0945792  -0.391305   39  ARG   B O    
2270 C CB   . ARG   B 27  ? 0.405465 1.03288  0.733112 0.0136479   -0.130685   -0.442166   39  ARG   B CB   
2271 C CG   . ARG   B 27  ? 0.439604 1.08087  0.82236  -0.00185401 -0.133306   -0.493041   39  ARG   B CG   
2272 C CD   . ARG   B 27  ? 0.439986 1.04037  0.88605  -0.0281278  -0.107032   -0.488157   39  ARG   B CD   
2273 N NE   . ARG   B 27  ? 0.459505 1.0737   0.967783 -0.0413371  -0.105321   -0.492854   39  ARG   B NE   
2274 C CZ   . ARG   B 27  ? 0.432566 1.01101  0.989714 -0.06189    -0.0798625  -0.477849   39  ARG   B CZ   
2275 N NH1  . ARG   B 27  ? 0.407734 0.930714 0.951254 -0.0686292  -0.0559408  -0.448724   39  ARG   B NH1  
2276 N NH2  . ARG   B 27  ? 0.428671 1.0292   1.0467   -0.0737851  -0.0786001  -0.49057    39  ARG   B NH2  
2277 H H    . ARG   B 27  ? 0.357689 0.935975 0.557556 0.0414111   -0.116477   -0.353564   39  ARG   B H    
2278 H HA   . ARG   B 27  ? 0.435708 1.09724  0.665756 0.0475029   -0.154982   -0.44984    39  ARG   B HA   
2279 H HB2  . ARG   B 27  ? 0.405083 1.05791  0.743148 0.0191821   -0.14292    -0.444315   39  ARG   B HB2  
2280 H HB3  . ARG   B 27  ? 0.386452 0.978875 0.723055 0.00393395  -0.11215    -0.4169     39  ARG   B HB3  
2281 H HG2  . ARG   B 27  ? 0.456783 1.09597  0.811422 0.00378658  -0.134288   -0.503188   39  ARG   B HG2  
2282 H HG3  . ARG   B 27  ? 0.451015 1.13027  0.857136 0.00019953  -0.151126   -0.520528   39  ARG   B HG3  
2283 H HD2  . ARG   B 27  ? 0.427496 0.992883 0.849791 -0.0279815  -0.0917945  -0.455021   39  ARG   B HD2  
2284 H HD3  . ARG   B 27  ? 0.455641 1.05276  0.925262 -0.0364058  -0.104537   -0.514789   39  ARG   B HD3  
2285 H HE   . ARG   B 27  ? 0.452816 1.10209  0.966357 -0.0345452  -0.12163    -0.506219   39  ARG   B HE   
2286 H HH11 . ARG   B 27  ? 0.422405 0.9332   0.956772 -0.0684178  -0.0540919  -0.45684    39  ARG   B HH11 
2287 H HH12 . ARG   B 27  ? 0.400545 0.899767 0.944142 -0.0724406  -0.0424018  -0.421835   39  ARG   B HH12 
2288 H HH21 . ARG   B 27  ? 0.438602 1.07411  1.08768  -0.0757795  -0.0924891  -0.522756   39  ARG   B HH21 
2289 H HH22 . ARG   B 27  ? 0.415676 0.99704  1.04402  -0.0796368  -0.0636212  -0.46763    39  ARG   B HH22 
2290 N N    . VAL   B 28  ? 0.457486 1.0691   0.675219 0.034228    -0.123882   -0.458001   40  VAL   B N    
2291 C CA   . VAL   B 28  ? 0.477243 1.05989  0.683613 0.0302132   -0.104805   -0.458073   40  VAL   B CA   
2292 C C    . VAL   B 28  ? 0.477494 1.03301  0.757676 0.00643306  -0.0902095  -0.474896   40  VAL   B C    
2293 O O    . VAL   B 28  ? 0.504103 1.07694  0.839728 -0.00540876 -0.0989428  -0.50647    40  VAL   B O    
2294 C CB   . VAL   B 28  ? 0.537692 1.14912  0.700139 0.0458219   -0.114817   -0.490464   40  VAL   B CB   
2295 C CG1  . VAL   B 28  ? 0.539188 1.12145  0.698588 0.0414199   -0.0921983  -0.492243   40  VAL   B CG1  
2296 C CG2  . VAL   B 28  ? 0.546417 1.1798   0.629104 0.0713853   -0.1266     -0.469003   40  VAL   B CG2  
2297 H H    . VAL   B 28  ? 0.478005 1.12306  0.692164 0.0419449   -0.141721   -0.483116   40  VAL   B H    
2298 H HA   . VAL   B 28  ? 0.46738  1.02685  0.646691 0.0333055   -0.0931109  -0.42394    40  VAL   B HA   
2299 H HB   . VAL   B 28  ? 0.545173 1.18114  0.735482 0.042718    -0.128502   -0.527255   40  VAL   B HB   
2300 H HG11 . VAL   B 28  ? 0.519028 1.07406  0.671092 0.0390748   -0.0778152  -0.458347   40  VAL   B HG11 
2301 H HG12 . VAL   B 28  ? 0.538007 1.11308  0.744144 0.0289523   -0.0889326  -0.516351   40  VAL   B HG12 
2302 H HG13 . VAL   B 28  ? 0.569599 1.16778  0.688555 0.0540402   -0.0950461  -0.503666   40  VAL   B HG13 
2303 H HG21 . VAL   B 28  ? 0.584583 1.23544  0.637026 0.0816125   -0.131596   -0.489802   40  VAL   B HG21 
2304 H HG22 . VAL   B 28  ? 0.550532 1.20433  0.637212 0.0761895   -0.142634   -0.469978   40  VAL   B HG22 
2305 H HG23 . VAL   B 28  ? 0.538582 1.14756  0.596984 0.0732198   -0.112583   -0.433639   40  VAL   B HG23 
2306 N N    . GLY   B 29  ? 0.468044 0.98037  0.751363 -0.00015198 -0.0675919  -0.452147   41  GLY   B N    
2307 C CA   . GLY   B 29  ? 0.47334  0.95062  0.819421 -0.0194573  -0.0512037  -0.45873    41  GLY   B CA   
2308 C C    . GLY   B 29  ? 0.513751 0.990355 0.883224 -0.0224582  -0.0475244  -0.501203   41  GLY   B C    
2309 O O    . GLY   B 29  ? 0.536477 1.04816  0.880825 -0.0118157  -0.061347   -0.53502    41  GLY   B O    
2310 H H    . GLY   B 29  ? 0.469571 0.97368  0.714607 0.00847261  -0.0620847  -0.431014   41  GLY   B H    
2311 H HA2  . GLY   B 29  ? 0.465402 0.947064 0.847564 -0.0291279  -0.0542543  -0.465574   41  GLY   B HA2  
2312 H HA3  . GLY   B 29  ? 0.455903 0.903354 0.794962 -0.0207794  -0.0383569  -0.42759    41  GLY   B HA3  
2313 N N    . ASN   B 30  ? 0.522303 0.956952 0.93876  -0.0356625  -0.0287535  -0.498927   42  ASN   B N    
2314 C CA   . ASN   B 30  ? 0.552173 0.976121 1.00511  -0.0408434  -0.0218487  -0.538597   42  ASN   B CA   
2315 C C    . ASN   B 30  ? 0.540453 0.928868 0.980115 -0.0338851  -0.00335083 -0.51647    42  ASN   B C    
2316 O O    . ASN   B 30  ? 0.496204 0.853336 0.930196 -0.0341958  0.00762337  -0.471923   42  ASN   B O    
2317 C CB   . ASN   B 30  ? 0.581836 0.981283 1.1125   -0.0623794  -0.0132964  -0.556041   42  ASN   B CB   
2318 C CG   . ASN   B 30  ? 0.591516 1.01624  1.14985  -0.073345   -0.024579   -0.561878   42  ASN   B CG   
2319 O OD1  . ASN   B 30  ? 0.612546 1.01654  1.18142  -0.0805954  -0.015056   -0.525043   42  ASN   B OD1  
2320 N ND2  . ASN   B 30  ? 0.612163 1.08408  1.18303  -0.073676   -0.0452993  -0.60901    42  ASN   B ND2  
2321 H H    . ASN   B 30  ? 0.500909 0.910756 0.926005 -0.0407277  -0.0196673  -0.470354   42  ASN   B H    
2322 H HA   . ASN   B 30  ? 0.575181 1.02959  1.01423  -0.0346918  -0.0336313  -0.570035   42  ASN   B HA   
2323 H HB2  . ASN   B 30  ? 0.569787 0.932294 1.11235  -0.0662732  0.00163429  -0.528845   42  ASN   B HB2  
2324 H HB3  . ASN   B 30  ? 0.604062 1.00572  1.15902  -0.0654554  -0.0134596  -0.591618   42  ASN   B HB3  
2325 H HD21 . ASN   B 30  ? 0.606327 1.09789  1.19499  -0.0787751  -0.0534246  -0.613814   42  ASN   B HD21 
2326 H HD22 . ASN   B 30  ? 0.632608 1.11774  1.19425  -0.0681892  -0.051548   -0.636665   42  ASN   B HD22 
2327 N N    . GLY   B 31  ? 0.559773 0.955346 0.996075 -0.0266137  -0.00063072 -0.550282   43  GLY   B N    
2328 C CA   . GLY   B 31  ? 0.578236 0.945013 1.0121   -0.0190417  0.0171233   -0.536202   43  GLY   B CA   
2329 C C    . GLY   B 31  ? 0.546775 0.9251   0.918778 -0.00407013 0.0197063   -0.499747   43  GLY   B C    
2330 O O    . GLY   B 31  ? 0.55906  0.966493 0.884523 0.00195398  0.00808065  -0.488406   43  GLY   B O    
2331 H H    . GLY   B 31  ? 0.586457 1.00695  1.02283  -0.0256331  -0.010403   -0.584293   43  GLY   B H    
2332 H HA2  . GLY   B 31  ? 0.596049 0.967881 1.04045  -0.0164813  0.0191652   -0.569353   43  GLY   B HA2  
2333 H HA3  . GLY   B 31  ? 0.560318 0.893811 1.02612  -0.0261381  0.0264628   -0.5187     43  GLY   B HA3  
2334 N N    . GLU   B 32  ? 0.536418 0.891328 0.912473 0.00211415  0.0354586   -0.48204    44  GLU   B N    
2335 C CA   . GLU   B 32  ? 0.519418 0.885187 0.848007 0.0143082   0.0416436   -0.452146   44  GLU   B CA   
2336 C C    . GLU   B 32  ? 0.469472 0.806083 0.804002 0.0111775   0.0459577   -0.402104   44  GLU   B C    
2337 O O    . GLU   B 32  ? 0.458503 0.804989 0.753886 0.0160247   0.0455734   -0.371625   44  GLU   B O    
2338 C CB   . GLU   B 32  ? 0.54062  0.913196 0.868731 0.02532     0.0555913   -0.47618    44  GLU   B CB   
2339 H H    . GLU   B 32  ? 0.541951 0.873663 0.954298 -0.00132026 0.04293     -0.489494   44  GLU   B H    
2340 H HA   . GLU   B 32  ? 0.519719 0.910204 0.8106   0.0181066   0.0336086   -0.451035   44  GLU   B HA   
2343 N N    . GLU   B 33  ? 0.44963  0.748825 0.831517 0.00350433  0.0500639   -0.393966   45  GLU   B N    
2344 C CA   . GLU   B 33  ? 0.411359 0.681202 0.798307 0.00354921  0.0534486   -0.350328   45  GLU   B CA   
2345 C C    . GLU   B 33  ? 0.384587 0.659652 0.739765 -0.00135523 0.0438833   -0.320069   45  GLU   B C    
2346 O O    . GLU   B 33  ? 0.351695 0.632423 0.710457 -0.00974367 0.0366449   -0.328745   45  GLU   B O    
2347 C CB   . GLU   B 33  ? 0.42176  0.647999 0.859573 -0.00126579 0.0599068   -0.347547   45  GLU   B CB   
2348 H H    . GLU   B 33  ? 0.463728 0.75475  0.874691 -0.00145487 0.0507077   -0.416535   45  GLU   B H    
2349 H HA   . GLU   B 33  ? 0.412304 0.687239 0.789267 0.0113969   0.0584261   -0.342041   45  GLU   B HA   
2352 N N    . THR   B 34  ? 0.378702 0.653777 0.706257 0.00404665  0.0442243   -0.286889   46  THR   B N    
2353 C CA   . THR   B 34  ? 0.333525 0.600086 0.639223 5.889e-05   0.0374397   -0.253146   46  THR   B CA   
2354 C C    . THR   B 34  ? 0.336036 0.568065 0.659622 0.00090834  0.0401161   -0.224577   46  THR   B C    
2355 O O    . THR   B 34  ? 0.361675 0.585009 0.706546 0.007499    0.0457664   -0.226729   46  THR   B O    
2356 C CB   . THR   B 34  ? 0.324215 0.61633  0.582978 0.00541675  0.0346244   -0.239454   46  THR   B CB   
2357 O OG1  . THR   B 34  ? 0.323802 0.617383 0.584348 0.0119802   0.0434724   -0.232802   46  THR   B OG1  
2358 C CG2  . THR   B 34  ? 0.335761 0.66138  0.569349 0.00859523  0.0300913   -0.265503   46  THR   B CG2  
2359 H H    . THR   B 34  ? 0.373462 0.654639 0.697354 0.0102461   0.0494153   -0.286826   46  THR   B H    
2360 H HA   . THR   B 34  ? 0.339403 0.605142 0.650393 -0.00599737 0.033376    -0.258822   46  THR   B HA   
2361 H HB   . THR   B 34  ? 0.311002 0.595451 0.556773 0.00303234  0.0302862   -0.218037   46  THR   B HB   
2363 H HG21 . THR   B 34  ? 0.335047 0.671859 0.536595 0.0122522   0.0282978   -0.251905   46  THR   B HG21 
2364 H HG22 . THR   B 34  ? 0.352478 0.687579 0.591222 0.0124433   0.0352298   -0.285531   46  THR   B HG22 
2365 H HG23 . THR   B 34  ? 0.337924 0.664527 0.582303 0.00384056  0.0238742   -0.276264   46  THR   B HG23 
2366 N N    . PRO   B 35  ? 0.335328 0.547147 0.650986 -0.00387229 0.0357519   -0.198308   47  PRO   B N    
2367 C CA   . PRO   B 35  ? 0.327298 0.503559 0.657935 -0.00137757 0.0369903   -0.174392   47  PRO   B CA   
2368 C C    . PRO   B 35  ? 0.2897   0.468296 0.608963 0.00725229  0.033095    -0.154426   47  PRO   B C    
2369 O O    . PRO   B 35  ? 0.285364 0.485587 0.577026 0.00727839  0.0297364   -0.147193   47  PRO   B O    
2370 C CB   . PRO   B 35  ? 0.326924 0.486261 0.645421 -0.0087369  0.0350956   -0.156125   47  PRO   B CB   
2371 C CG   . PRO   B 35  ? 0.337467 0.528616 0.625905 -0.0118783  0.0292568   -0.160836   47  PRO   B CG   
2372 C CD   . PRO   B 35  ? 0.335863 0.55785  0.628047 -0.00987829 0.0297302   -0.191931   47  PRO   B CD   
2373 H HA   . PRO   B 35  ? 0.338317 0.500562 0.696189 -0.00063956 0.0420806   -0.185194   47  PRO   B HA   
2374 H HB2  . PRO   B 35  ? 0.330723 0.473481 0.639202 -0.00559091 0.0327232   -0.134044   47  PRO   B HB2  
2375 H HB3  . PRO   B 35  ? 0.342719 0.488777 0.682463 -0.0137324  0.0403817   -0.16444    47  PRO   B HB3  
2376 H HG2  . PRO   B 35  ? 0.320509 0.514676 0.586089 -0.00867936 0.0252911   -0.144466   47  PRO   B HG2  
2377 H HG3  . PRO   B 35  ? 0.329639 0.517907 0.619638 -0.0174905  0.029529    -0.160726   47  PRO   B HG3  
2378 H HD2  . PRO   B 35  ? 0.328489 0.569772 0.594891 -0.00680929 0.0263111   -0.189207   47  PRO   B HD2  
2379 H HD3  . PRO   B 35  ? 0.341117 0.56895  0.647346 -0.0146775  0.029998    -0.210298   47  PRO   B HD3  
2380 N N    . MET   B 36  ? 0.300572 0.454457 0.642683 0.0145062   0.0330368   -0.143818   48  MET   B N    
2381 C CA   . MET   B 36  ? 0.296956 0.453801 0.640154 0.0236707   0.0269044   -0.127741   48  MET   B CA   
2382 C C    . MET   B 36  ? 0.309256 0.443061 0.631825 0.0249675   0.0164808   -0.0971844  48  MET   B C    
2383 O O    . MET   B 36  ? 0.291313 0.397022 0.607373 0.022245    0.0177658   -0.0867236  48  MET   B O    
2384 C CB   . MET   B 36  ? 0.335063 0.479791 0.718231 0.0351439   0.030019    -0.135378   48  MET   B CB   
2385 C CG   . MET   B 36  ? 0.352651 0.517413 0.758813 0.03638     0.0413231   -0.168048   48  MET   B CG   
2386 S SD   . MET   B 36  ? 0.359835 0.57024  0.756559 0.0387158   0.0450636   -0.17507    48  MET   B SD   
2387 C CE   . MET   B 36  ? 0.377158 0.60958  0.779938 0.0379362   0.059654    -0.215913   48  MET   B CE   
2388 H H    . MET   B 36  ? 0.314646 0.44883  0.674678 0.0141429   0.036726    -0.147191   48  MET   B H    
2389 H HA   . MET   B 36  ? 0.291577 0.472727 0.624111 0.0226815   0.0273672   -0.131749   48  MET   B HA   
2390 H HB2  . MET   B 36  ? 0.347544 0.46468  0.739043 0.0364962   0.0304406   -0.12885    48  MET   B HB2  
2391 H HB3  . MET   B 36  ? 0.329824 0.479194 0.716395 0.0417388   0.0240445   -0.124546   48  MET   B HB3  
2392 H HG2  . MET   B 36  ? 0.356735 0.523897 0.75636  0.0291091   0.0450816   -0.181375   48  MET   B HG2  
2393 H HG3  . MET   B 36  ? 0.36942  0.519726 0.803076 0.0436064   0.0440424   -0.173125   48  MET   B HG3  
2394 H HE1  . MET   B 36  ? 0.374283 0.630851 0.768827 0.0396274   0.0653556   -0.220809   48  MET   B HE1  
2395 H HE2  . MET   B 36  ? 0.37658  0.608596 0.762332 0.031065    0.0581756   -0.221906   48  MET   B HE2  
2396 H HE3  . MET   B 36  ? 0.390652 0.611355 0.821939 0.0433034   0.0634397   -0.227958   48  MET   B HE3  
2397 N N    . ILE   B 37  ? 0.278666 0.424575 0.592961 0.0292618   0.00719074  -0.0842629  49  ILE   B N    
2398 C CA   . ILE   B 37  ? 0.293098 0.418653 0.587049 0.0327119   -0.0053945  -0.0589087  49  ILE   B CA   
2399 C C    . ILE   B 37  ? 0.306011 0.395185 0.61187  0.043027    -0.00737024 -0.0473449  49  ILE   B C    
2400 O O    . ILE   B 37  ? 0.334968 0.420368 0.673682 0.0531032   -0.00620077 -0.0542093  49  ILE   B O    
2401 C CB   . ILE   B 37  ? 0.278794 0.42441  0.573427 0.0360369   -0.0168095  -0.0521052  49  ILE   B CB   
2402 C CG1  . ILE   B 37  ? 0.27431  0.445709 0.54943  0.0247682   -0.0120703  -0.0568394  49  ILE   B CG1  
2403 C CG2  . ILE   B 37  ? 0.28695  0.410658 0.563886 0.0432791   -0.0335541  -0.0300789  49  ILE   B CG2  
2404 C CD1  . ILE   B 37  ? 0.281782 0.471759 0.562958 0.0241845   -0.0200049  -0.0513873  49  ILE   B CD1  
2405 H H    . ILE   B 37  ? 0.278231 0.445356 0.600059 0.0299311   0.00905505  -0.0922324  49  ILE   B H    
2406 H HA   . ILE   B 37  ? 0.28289  0.404362 0.553354 0.0260407   -0.00458324 -0.0537997  49  ILE   B HA   
2407 H HB   . ILE   B 37  ? 0.282951 0.43938  0.604682 0.0417973   -0.0157652  -0.0602126  49  ILE   B HB   
2408 H HG12 . ILE   B 37  ? 0.272166 0.433713 0.522512 0.019973    -0.0125834  -0.0503336  49  ILE   B HG12 
2409 H HG13 . ILE   B 37  ? 0.269659 0.45521  0.553027 0.0225765   -0.00216741 -0.0706887  49  ILE   B HG13 
2410 H HG21 . ILE   B 37  ? 0.282993 0.421513 0.562325 0.0436133   -0.041821   -0.0285149  49  ILE   B HG21 
2411 H HG22 . ILE   B 37  ? 0.29104  0.401194 0.541484 0.0386712   -0.0327624  -0.0222416  49  ILE   B HG22 
2412 H HG23 . ILE   B 37  ? 0.306037 0.414461 0.595634 0.0528194   -0.0366367  -0.025901   49  ILE   B HG23 
2413 H HD11 . ILE   B 37  ? 0.280828 0.478613 0.589641 0.0305666   -0.0222425  -0.0555079  49  ILE   B HD11 
2414 H HD12 . ILE   B 37  ? 0.268461 0.474533 0.543451 0.0177325   -0.0123379  -0.0561293  49  ILE   B HD12 
2415 H HD13 . ILE   B 37  ? 0.280293 0.458403 0.545137 0.0241086   -0.0301419  -0.0396486  49  ILE   B HD13 
2416 N N    . GLY   B 38  ? 0.318304 0.379339 0.595253 0.0417242   -0.00906707 -0.0282269  50  GLY   B N    
2417 C CA   . GLY   B 38  ? 0.350923 0.37132  0.628528 0.0516358   -0.00797616 -0.0112787  50  GLY   B CA   
2418 C C    . GLY   B 38  ? 0.367232 0.365594 0.657192 0.0425343   0.0112173   -0.0183043  50  GLY   B C    
2419 O O    . GLY   B 38  ? 0.405129 0.364795 0.687831 0.0466541   0.0176233   -0.00021253 50  GLY   B O    
2420 H H    . GLY   B 38  ? 0.307941 0.374428 0.562683 0.0350058   -0.00971035 -0.0248958  50  GLY   B H    
2421 H HA2  . GLY   B 38  ? 0.362436 0.370675 0.61254  0.0546113   -0.0149355  0.00563183  50  GLY   B HA2  
2422 H HA3  . GLY   B 38  ? 0.362941 0.38123  0.660975 0.0622315   -0.0127301  -0.0116506  50  GLY   B HA3  
2423 N N    . ASP   B 39  ? 0.32776  0.350295 0.637576 0.0307951   0.0206423   -0.0450224  51  ASP   B N    
2424 C CA   . ASP   B 39  ? 0.353652 0.361125 0.684565 0.0204582   0.036962    -0.0582646  51  ASP   B CA   
2425 C C    . ASP   B 39  ? 0.360442 0.352869 0.666027 0.0110415   0.0436034   -0.042997   51  ASP   B C    
2426 O O    . ASP   B 39  ? 0.328412 0.336383 0.60024  0.00902549  0.0359208   -0.0335597  51  ASP   B O    
2427 C CB   . ASP   B 39  ? 0.32271  0.365929 0.672262 0.0105933   0.0411063   -0.0923171  51  ASP   B CB   
2428 C CG   . ASP   B 39  ? 0.325646 0.380148 0.7082   0.0173734   0.0427888   -0.115452   51  ASP   B CG   
2429 O OD1  . ASP   B 39  ? 0.33733  0.369092 0.737612 0.0301707   0.0417008   -0.105721   51  ASP   B OD1  
2430 O OD2  . ASP   B 39  ? 0.313488 0.399346 0.702639 0.0113201   0.0452849   -0.143629   51  ASP   B OD2  
2431 H H    . ASP   B 39  ? 0.315528 0.364986 0.626046 0.0292173   0.0167704   -0.0559077  51  ASP   B H    
2432 H HA   . ASP   B 39  ? 0.373167 0.356271 0.7235   0.026278    0.0418049   -0.0555393  51  ASP   B HA   
2433 H HB2  . ASP   B 39  ? 0.304061 0.371262 0.633013 0.00815311  0.0350662   -0.0927897  51  ASP   B HB2  
2434 H HB3  . ASP   B 39  ? 0.330511 0.367535 0.690308 0.00175905  0.049467    -0.100802   51  ASP   B HB3  
2435 N N    . LYS   B 40  ? 0.399908 0.36058  0.725238 0.00518931  0.0600546   -0.0411115  52  LYS   B N    
2436 C CA   . LYS   B 40  ? 0.410622 0.358835 0.720923 -0.00525985 0.0717056   -0.0295211  52  LYS   B CA   
2437 C C    . LYS   B 40  ? 0.368412 0.351932 0.699587 -0.0213029  0.0760212   -0.0593179  52  LYS   B C    
2438 O O    . LYS   B 40  ? 0.370068 0.358087 0.742025 -0.0284559  0.0829047   -0.0854087  52  LYS   B O    
2439 C CB   . LYS   B 40  ? 0.490508 0.387024 0.813704 -0.00479274 0.090641    -0.0111555  52  LYS   B CB   
2440 C CG   . LYS   B 40  ? 0.536511 0.416872 0.846153 -0.0155423  0.108236    0.00361173  52  LYS   B CG   
2441 C CD   . LYS   B 40  ? 0.619334 0.447331 0.898923 -0.00510222 0.1197      0.0421065   52  LYS   B CD   
2442 C CE   . LYS   B 40  ? 0.696782 0.48051  1.011    -0.0114933  0.146101    0.0479589   52  LYS   B CE   
2443 N NZ   . LYS   B 40  ? 0.719525 0.503352 1.0483   -0.0309676  0.170043    0.044916    52  LYS   B NZ   
2444 H H    . LYS   B 40  ? 0.413702 0.35993  0.764473 0.00752575  0.0654739   -0.0474776  52  LYS   B H    
2445 H HA   . LYS   B 40  ? 0.406589 0.357625 0.68379  -0.00110788 0.064357    -0.013987   52  LYS   B HA   
2446 H HB2  . LYS   B 40  ? 0.510106 0.385941 0.817221 0.00834868  0.0850795   0.0077627   52  LYS   B HB2  
2447 H HB3  . LYS   B 40  ? 0.496725 0.388489 0.855533 -0.00955644 0.0982835   -0.027711   52  LYS   B HB3  
2448 H HG2  . LYS   B 40  ? 0.537715 0.419858 0.880822 -0.0278207  0.120645    -0.0125937  52  LYS   B HG2  
2449 H HG3  . LYS   B 40  ? 0.511721 0.416283 0.799587 -0.0175869  0.100879    0.00255008  52  LYS   B HG3  
2450 H HD2  . LYS   B 40  ? 0.619298 0.449443 0.871137 -0.00712709 0.122643    0.0532827   52  LYS   B HD2  
2451 H HD3  . LYS   B 40  ? 0.625861 0.446299 0.886874 0.00945305  0.106382    0.0536988   52  LYS   B HD3  
2452 H HE2  . LYS   B 40  ? 0.729727 0.478574 1.02254  0.00075479  0.148974    0.0733522   52  LYS   B HE2  
2453 H HE3  . LYS   B 40  ? 0.686931 0.475294 1.03773  -0.0145911  0.145604    0.0281332   52  LYS   B HE3  
2454 H HZ1  . LYS   B 40  ? 0.72781  0.500176 1.02289  -0.0270625  0.174473    0.0656566   52  LYS   B HZ1  
2455 H HZ2  . LYS   B 40  ? 0.679039 0.498146 1.02173  -0.0399565  0.164226    0.0231345   52  LYS   B HZ2  
2456 H HZ3  . LYS   B 40  ? 0.73869  0.499031 1.09747  -0.0377179  0.186836    0.0436061   52  LYS   B HZ3  
2457 N N    . VAL   B 41  ? 0.356691 0.363551 0.660583 -0.0256467  0.071373    -0.0559861  53  VAL   B N    
2458 C CA   . VAL   B 41  ? 0.344121 0.391294 0.660834 -0.0358821  0.0692377   -0.0826871  53  VAL   B CA   
2459 C C    . VAL   B 41  ? 0.360597 0.405387 0.683625 -0.0469087  0.0823751   -0.079318   53  VAL   B C    
2460 O O    . VAL   B 41  ? 0.352577 0.377795 0.646534 -0.0441512  0.0877256   -0.0532728  53  VAL   B O    
2461 C CB   . VAL   B 41  ? 0.359925 0.440141 0.642731 -0.0289481  0.0519063   -0.0830468  53  VAL   B CB   
2462 C CG1  . VAL   B 41  ? 0.362413 0.48244  0.6474   -0.0350439  0.0475424   -0.104498   53  VAL   B CG1  
2463 C CG2  . VAL   B 41  ? 0.366482 0.454451 0.652088 -0.0201759  0.0430792   -0.0900133  53  VAL   B CG2  
2464 H H    . VAL   B 41  ? 0.360743 0.357783 0.636432 -0.0208409  0.0687133   -0.0366275  53  VAL   B H    
2465 H HA   . VAL   B 41  ? 0.352263 0.406934 0.69733  -0.0394228  0.0709725   -0.103529   53  VAL   B HA   
2466 H HB   . VAL   B 41  ? 0.357955 0.427502 0.614084 -0.0250626  0.0496359   -0.063126   53  VAL   B HB   
2467 H HG11 . VAL   B 41  ? 0.359303 0.487155 0.672829 -0.0407892  0.0513916   -0.124591   53  VAL   B HG11 
2468 H HG12 . VAL   B 41  ? 0.353053 0.472244 0.628087 -0.0374883  0.0501889   -0.0956416  53  VAL   B HG12 
2469 H HG13 . VAL   B 41  ? 0.341834 0.48048  0.610015 -0.0300323  0.0383262   -0.107364   53  VAL   B HG13 
2470 H HG21 . VAL   B 41  ? 0.347183 0.455389 0.613502 -0.017383   0.0349461   -0.0900213  53  VAL   B HG21 
2471 H HG22 . VAL   B 41  ? 0.375056 0.440457 0.657588 -0.0140899  0.0429535   -0.0749315  53  VAL   B HG22 
2472 H HG23 . VAL   B 41  ? 0.366049 0.461508 0.676747 -0.0229981  0.0462537   -0.11002    53  VAL   B HG23 
2473 N N    . TYR   B 42  ? 0.341103 0.408519 0.7047   -0.0591077  0.087478    -0.108603   54  TYR   B N    
2474 C CA   . TYR   B 42  ? 0.350854 0.425357 0.735381 -0.0712959  0.100406    -0.112573   54  TYR   B CA   
2475 C C    . TYR   B 42  ? 0.297423 0.42495  0.684133 -0.07266    0.085723    -0.137129   54  TYR   B C    
2476 O O    . TYR   B 42  ? 0.291443 0.447495 0.697489 -0.073652   0.0747423   -0.16735    54  TYR   B O    
2477 C CB   . TYR   B 42  ? 0.395325 0.452178 0.838176 -0.0859278  0.119139    -0.129574   54  TYR   B CB   
2478 C CG   . TYR   B 42  ? 0.456715 0.456098 0.903433 -0.0839988  0.136448    -0.105643   54  TYR   B CG   
2479 C CD1  . TYR   B 42  ? 0.486356 0.467683 0.930943 -0.0736247  0.128887    -0.105774   54  TYR   B CD1  
2480 C CD2  . TYR   B 42  ? 0.49792  0.461116 0.953242 -0.091695   0.162066    -0.0835712  54  TYR   B CD2  
2481 C CE1  . TYR   B 42  ? 0.532025 0.45992  0.980978 -0.0686712  0.143119    -0.0830693  54  TYR   B CE1  
2482 C CE2  . TYR   B 42  ? 0.552082 0.459051 1.00664  -0.0875469  0.178544    -0.0587074  54  TYR   B CE2  
2483 C CZ   . TYR   B 42  ? 0.560936 0.450028 1.01311  -0.0753011  0.167644    -0.0587104  54  TYR   B CZ   
2484 O OH   . TYR   B 42  ? 0.622571 0.455209 1.07335  -0.0678809  0.182175    -0.0326052  54  TYR   B OH   
2485 H H    . TYR   B 42  ? 0.341897 0.422805 0.722612 -0.0596913  0.0824291   -0.128553   54  TYR   B H    
2486 H HA   . TYR   B 42  ? 0.355662 0.412584 0.717112 -0.0688419  0.107041    -0.0893483  54  TYR   B HA   
2487 H HB2  . TYR   B 42  ? 0.388726 0.465255 0.853536 -0.0882162  0.111329    -0.155638   54  TYR   B HB2  
2488 H HB3  . TYR   B 42  ? 0.397637 0.463298 0.858624 -0.0950048  0.128296    -0.133507   54  TYR   B HB3  
2489 H HD1  . TYR   B 42  ? 0.462383 0.468015 0.901851 -0.0687137  0.114345    -0.120646   54  TYR   B HD1  
2490 H HD2  . TYR   B 42  ? 0.49377  0.47037  0.954109 -0.0987687  0.169123    -0.0842692  54  TYR   B HD2  
2491 H HE1  . TYR   B 42  ? 0.534389 0.451948 0.984252 -0.0601055  0.137161    -0.0837223  54  TYR   B HE1  
2492 H HE2  . TYR   B 42  ? 0.576795 0.457621 1.0333   -0.0922407  0.197863    -0.0416993  54  TYR   B HE2  
2494 N N    . VAL   B 43  ? 0.290852 0.431033 0.657477 -0.0712361  0.0858608   -0.125073   55  VAL   B N    
2495 C CA   . VAL   B 43  ? 0.270941 0.459574 0.637751 -0.0689507  0.070896    -0.144906   55  VAL   B CA   
2496 C C    . VAL   B 43  ? 0.287816 0.4903   0.678156 -0.0762787  0.0819735   -0.146387   55  VAL   B C    
2497 O O    . VAL   B 43  ? 0.319633 0.491755 0.709385 -0.0808364  0.10195     -0.124972   55  VAL   B O    
2498 C CB   . VAL   B 43  ? 0.257676 0.456705 0.569943 -0.0540283  0.0538748   -0.130278   55  VAL   B CB   
2499 C CG1  . VAL   B 43  ? 0.249357 0.440208 0.543363 -0.0473421  0.0449709   -0.129733   55  VAL   B CG1  
2500 C CG2  . VAL   B 43  ? 0.261506 0.436767 0.537235 -0.0488463  0.0600621   -0.0988206  55  VAL   B CG2  
2501 H H    . VAL   B 43  ? 0.300689 0.418748 0.652209 -0.0703756  0.0952259   -0.10431    55  VAL   B H    
2502 H HA   . VAL   B 43  ? 0.27265  0.480454 0.662431 -0.0718901  0.0646549   -0.168899   55  VAL   B HA   
2503 H HB   . VAL   B 43  ? 0.246263 0.476273 0.56031  -0.0515115  0.0442418   -0.144083   55  VAL   B HB   
2504 H HG11 . VAL   B 43  ? 0.26151  0.423215 0.551674 -0.0473787  0.0518927   -0.114933   55  VAL   B HG11 
2505 H HG12 . VAL   B 43  ? 0.253206 0.458073 0.569414 -0.0502389  0.042358    -0.151187   55  VAL   B HG12 
2506 H HG13 . VAL   B 43  ? 0.24146  0.442414 0.506326 -0.0396376  0.0354288   -0.123212   55  VAL   B HG13 
2507 H HG21 . VAL   B 43  ? 0.252131 0.430575 0.497191 -0.0406837  0.0496968   -0.0909139  55  VAL   B HG21 
2508 H HG22 . VAL   B 43  ? 0.260476 0.447114 0.545772 -0.051186   0.064749    -0.100951   55  VAL   B HG22 
2509 H HG23 . VAL   B 43  ? 0.27533  0.420796 0.54899  -0.050812   0.069924    -0.0851678  55  VAL   B HG23 
2510 N N    . HIS   B 44  ? 0.284105 0.53439  0.694167 -0.0757108  0.0686579   -0.172206   56  HIS   B N    
2511 C CA   . HIS   B 44  ? 0.287258 0.561727 0.7059   -0.074702   0.0710884   -0.171209   56  HIS   B CA   
2512 C C    . HIS   B 44  ? 0.243987 0.54264  0.616409 -0.0568654  0.0490512   -0.165992   56  HIS   B C    
2513 O O    . HIS   B 44  ? 0.237063 0.550017 0.590626 -0.0493932  0.0315456   -0.176278   56  HIS   B O    
2514 C CB   . HIS   B 44  ? 0.309334 0.621852 0.796797 -0.0873967  0.0732812   -0.2057     56  HIS   B CB   
2515 C CG   . HIS   B 44  ? 0.342851 0.629853 0.878342 -0.106011   0.103211    -0.202967   56  HIS   B CG   
2516 N ND1  . HIS   B 44  ? 0.359713 0.620796 0.885327 -0.108023   0.127126    -0.174847   56  HIS   B ND1  
2517 C CD2  . HIS   B 44  ? 0.359187 0.64173  0.953664 -0.123655   0.115028    -0.225522   56  HIS   B CD2  
2518 C CE1  . HIS   B 44  ? 0.380065 0.619834 0.954586 -0.126189   0.154513    -0.177014   56  HIS   B CE1  
2519 N NE2  . HIS   B 44  ? 0.377969 0.629551 0.997945 -0.136695   0.147614    -0.207894   56  HIS   B NE2  
2520 H H    . HIS   B 44  ? 0.279728 0.549197 0.698031 -0.0746999  0.0571758   -0.191723   56  HIS   B H    
2521 H HA   . HIS   B 44  ? 0.292605 0.54138  0.701436 -0.0764575  0.0863482   -0.150441   56  HIS   B HA   
2522 H HB2  . HIS   B 44  ? 0.307255 0.635843 0.807837 -0.0884305  0.0614398   -0.227602   56  HIS   B HB2  
2523 H HB3  . HIS   B 44  ? 0.300293 0.64111  0.789044 -0.081572   0.0658677   -0.209992   56  HIS   B HB3  
2525 H HD2  . HIS   B 44  ? 0.358199 0.654396 0.97212  -0.12654    0.1043      -0.24907    56  HIS   B HD2  
2526 H HE1  . HIS   B 44  ? 0.395775 0.614898 0.972019 -0.130758   0.17626     -0.159881   56  HIS   B HE1  
2528 N N    . TYR   B 45  ? 0.244967 0.544699 0.59802  -0.0496111  0.0523298   -0.149045   57  TYR   B N    
2529 C CA   . TYR   B 45  ? 0.232239 0.544255 0.539481 -0.0322863  0.0348266   -0.139081   57  TYR   B CA   
2530 C C    . TYR   B 45  ? 0.248169 0.578548 0.563412 -0.0259556  0.0382126   -0.136056   57  TYR   B C    
2531 O O    . TYR   B 45  ? 0.225727 0.547318 0.567128 -0.034659   0.0586744   -0.132148   57  TYR   B O    
2532 C CB   . TYR   B 45  ? 0.227827 0.499733 0.480408 -0.0262551  0.0351635   -0.110739   57  TYR   B CB   
2533 C CG   . TYR   B 45  ? 0.227881 0.465865 0.460198 -0.0265405  0.0514919   -0.0857251  57  TYR   B CG   
2534 C CD1  . TYR   B 45  ? 0.24911  0.452168 0.487362 -0.0361844  0.0699672   -0.0740544  57  TYR   B CD1  
2535 C CD2  . TYR   B 45  ? 0.220691 0.46091  0.427119 -0.0157011  0.0493406   -0.0745433  57  TYR   B CD2  
2536 C CE1  . TYR   B 45  ? 0.243956 0.417047 0.456939 -0.034448   0.0851091   -0.0519014  57  TYR   B CE1  
2537 C CE2  . TYR   B 45  ? 0.225051 0.436251 0.411305 -0.0151116  0.0648329   -0.0556796  57  TYR   B CE2  
2538 C CZ   . TYR   B 45  ? 0.239804 0.418401 0.426725 -0.0243171  0.0824938   -0.0444478  57  TYR   B CZ   
2539 O OH   . TYR   B 45  ? 0.240086 0.390963 0.399251 -0.0214653  0.0974532   -0.0261667  57  TYR   B OH   
2540 H H    . TYR   B 45  ? 0.250438 0.54145  0.619562 -0.0554724  0.0672704   -0.143391   57  TYR   B H    
2541 H HA   . TYR   B 45  ? 0.231226 0.567842 0.539992 -0.0277694  0.020041    -0.154564   57  TYR   B HA   
2542 H HB2  . TYR   B 45  ? 0.221891 0.503587 0.449165 -0.0164315  0.0227452   -0.108232   57  TYR   B HB2  
2543 H HB3  . TYR   B 45  ? 0.228884 0.487692 0.484017 -0.031183   0.0364373   -0.112301   57  TYR   B HB3  
2544 H HD1  . TYR   B 45  ? 0.245083 0.443378 0.502469 -0.0429082  0.072444    -0.0810005  57  TYR   B HD1  
2545 H HD2  . TYR   B 45  ? 0.213318 0.474701 0.415152 -0.00771875 0.0375029   -0.0804268  57  TYR   B HD2  
2546 H HE1  . TYR   B 45  ? 0.264228 0.412561 0.476946 -0.039315   0.0975694   -0.0423586  57  TYR   B HE1  
2547 H HE2  . TYR   B 45  ? 0.228662 0.440936 0.398355 -0.00735617 0.0634454   -0.0502267  57  TYR   B HE2  
2549 N N    . LYS   B 46  ? 0.246342 0.60017  0.536804 -0.00929432 0.0195247   -0.136283   58  LYS   B N    
2550 C CA   . LYS   B 46  ? 0.254622 0.619393 0.539841 0.00256681  0.0200076   -0.128423   58  LYS   B CA   
2551 C C    . LYS   B 46  ? 0.275061 0.617113 0.499526 0.0173963   0.0102467   -0.105913   58  LYS   B C    
2552 O O    . LYS   B 46  ? 0.32564  0.668025 0.524246 0.0220295   -0.00344553 -0.105697   58  LYS   B O    
2553 C CB   . LYS   B 46  ? 0.269182 0.68951  0.593233 0.0110636   0.00461113  -0.15373    58  LYS   B CB   
2554 C CG   . LYS   B 46  ? 0.262367 0.711353 0.655693 -0.00530157 0.011908    -0.181681   58  LYS   B CG   
2555 C CD   . LYS   B 46  ? 0.260467 0.764811 0.705088 0.00140205  0.00242419  -0.205391   58  LYS   B CD   
2556 C CE   . LYS   B 46  ? 0.262861 0.81363  0.708808 0.0153316   -0.0301728  -0.229327   58  LYS   B CE   
2557 N NZ   . LYS   B 46  ? 0.253342 0.862105 0.764759 0.0177423   -0.0395642  -0.258648   58  LYS   B NZ   
2558 H H    . LYS   B 46  ? 0.245333 0.607711 0.520845 -0.00419204 0.00648184  -0.141251   58  LYS   B H    
2559 H HA   . LYS   B 46  ? 0.263119 0.611926 0.557805 -0.00378863 0.0371283   -0.120654   58  LYS   B HA   
2560 H HB2  . LYS   B 46  ? 0.26491  0.699062 0.571325 0.0198431   -0.0126857  -0.1591     58  LYS   B HB2  
2561 H HB3  . LYS   B 46  ? 0.266246 0.691377 0.587274 0.0202195   0.00607534  -0.146943   58  LYS   B HB3  
2562 H HG2  . LYS   B 46  ? 0.265979 0.691001 0.670352 -0.016983   0.0323416   -0.17316    58  LYS   B HG2  
2563 H HG3  . LYS   B 46  ? 0.262937 0.71701  0.660884 -0.0102871  0.00401122  -0.194345   58  LYS   B HG3  
2564 H HD2  . LYS   B 46  ? 0.262282 0.763976 0.694635 0.0114118   0.005942    -0.192545   58  LYS   B HD2  
2565 H HD3  . LYS   B 46  ? 0.261213 0.774297 0.753435 -0.0129959  0.015502    -0.218332   58  LYS   B HD3  
2566 H HE2  . LYS   B 46  ? 0.261287 0.809922 0.70794  0.00751392  -0.0343435  -0.24025    58  LYS   B HE2  
2567 H HE3  . LYS   B 46  ? 0.263768 0.809123 0.66622  0.0315745   -0.0414075  -0.215255   58  LYS   B HE3  
2568 H HZ1  . LYS   B 46  ? 0.254858 0.868641 0.810204 0.00125058  -0.0278955  -0.272492   58  LYS   B HZ1  
2569 H HZ2  . LYS   B 46  ? 0.256366 0.86816  0.768696 0.0260637   -0.0352775  -0.248971   58  LYS   B HZ2  
2570 H HZ3  . LYS   B 46  ? 0.261656 0.899137 0.770345 0.0278134   -0.0612887  -0.273447   58  LYS   B HZ3  
2571 N N    . GLY   B 47  ? 0.25312  0.572046 0.456037 0.0230264   0.0203395   -0.0875041  59  GLY   B N    
2572 C CA   . GLY   B 47  ? 0.255724 0.545103 0.405755 0.0333159   0.0148716   -0.0664541  59  GLY   B CA   
2573 C C    . GLY   B 47  ? 0.263549 0.555674 0.405272 0.0483985   0.0155048   -0.0600583  59  GLY   B C    
2574 O O    . GLY   B 47  ? 0.237537 0.540652 0.408075 0.0476335   0.0282493   -0.065798   59  GLY   B O    
2575 H H    . GLY   B 47  ? 0.261554 0.583106 0.48479  0.0199531   0.0318719   -0.0892258  59  GLY   B H    
2576 H HA2  . GLY   B 47  ? 0.255021 0.550856 0.391216 0.0376635   0.0027667   -0.0675463  59  GLY   B HA2  
2577 H HA3  . GLY   B 47  ? 0.258907 0.519309 0.393173 0.0264592   0.0233338   -0.0557561  59  GLY   B HA3  
2578 N N    . LYS   B 48  ? 0.248389 0.52883  0.352929 0.0620628   0.00414473  -0.0479518  60  LYS   B N    
2579 C CA   . LYS   B 48  ? 0.258199 0.533041 0.351628 0.0779321   0.00512239  -0.0403115  60  LYS   B CA   
2580 C C    . LYS   B 48  ? 0.291526 0.532363 0.338041 0.0855389   -0.00090802 -0.0220177  60  LYS   B C    
2581 O O    . LYS   B 48  ? 0.293848 0.527848 0.322187 0.0808769   -0.0080452  -0.0174151  60  LYS   B O    
2582 C CB   . LYS   B 48  ? 0.277952 0.597636 0.401063 0.0939277   -0.00623457 -0.0535635  60  LYS   B CB   
2583 C CG   . LYS   B 48  ? 0.299881 0.643659 0.411731 0.105026    -0.0280601  -0.0572717  60  LYS   B CG   
2584 C CD   . LYS   B 48  ? 0.347287 0.731414 0.478228 0.127559    -0.0432877  -0.0663971  60  LYS   B CD   
2585 C CE   . LYS   B 48  ? 0.362882 0.772443 0.477063 0.140019    -0.0654181  -0.0708388  60  LYS   B CE   
2586 N NZ   . LYS   B 48  ? 0.40778  0.851619 0.532124 0.166825    -0.0826548  -0.0752807  60  LYS   B NZ   
2587 H H    . LYS   B 48  ? 0.252392 0.527127 0.339468 0.0615699   -0.00302268 -0.0443454  60  LYS   B H    
2588 H HA   . LYS   B 48  ? 0.27021  0.532203 0.368097 0.0735353   0.0183739   -0.0384954  60  LYS   B HA   
2589 H HB2  . LYS   B 48  ? 0.288542 0.601376 0.404975 0.105356    -0.00423303 -0.0476103  60  LYS   B HB2  
2590 H HB3  . LYS   B 48  ? 0.269524 0.611243 0.428136 0.087032    -0.00090216 -0.0667662  60  LYS   B HB3  
2591 H HG2  . LYS   B 48  ? 0.293264 0.650663 0.418796 0.0947388   -0.0302782  -0.0680452  60  LYS   B HG2  
2592 H HG3  . LYS   B 48  ? 0.311757 0.630774 0.389005 0.108354    -0.0301293  -0.0431052  60  LYS   B HG3  
2593 H HD2  . LYS   B 48  ? 0.355317 0.723243 0.471178 0.139279    -0.0412143  -0.05475    60  LYS   B HD2  
2594 H HD3  . LYS   B 48  ? 0.331627 0.741828 0.502082 0.123484    -0.0402558  -0.0815106  60  LYS   B HD3  
2595 H HE2  . LYS   B 48  ? 0.357288 0.787331 0.490754 0.129787    -0.0686051  -0.0863705  60  LYS   B HE2  
2596 H HE3  . LYS   B 48  ? 0.37692  0.760206 0.453797 0.141575    -0.0653303  -0.0556793  60  LYS   B HE3  
2597 H HZ1  . LYS   B 48  ? 0.390476 0.860681 0.553718 0.165064    -0.0822357  -0.0902112  60  LYS   B HZ1  
2598 H HZ2  . LYS   B 48  ? 0.411785 0.834129 0.517199 0.177388    -0.0796092  -0.0603009  60  LYS   B HZ2  
2599 H HZ3  . LYS   B 48  ? 0.410227 0.870772 0.521493 0.175477    -0.0968697  -0.0784259  60  LYS   B HZ3  
2600 N N    . LEU   B 49  ? 0.294305 0.512462 0.324891 0.0955982   0.00470566  -0.0130238  61  LEU   B N    
2601 C CA   . LEU   B 49  ? 0.35997  0.548977 0.355109 0.105765    -0.00089639 0.00209135  61  LEU   B CA   
2602 C C    . LEU   B 49  ? 0.417538 0.634081 0.414325 0.123894    -0.0156642  0.0025274   61  LEU   B C    
2603 O O    . LEU   B 49  ? 0.380309 0.635264 0.406925 0.133629    -0.0210665  -0.00998298 61  LEU   B O    
2604 C CB   . LEU   B 49  ? 0.390872 0.550239 0.37394  0.113026    0.00912641  0.00701957  61  LEU   B CB   
2605 C CG   . LEU   B 49  ? 0.417697 0.552624 0.393204 0.0985378   0.0230616   0.00526847  61  LEU   B CG   
2606 C CD1  . LEU   B 49  ? 0.466181 0.571081 0.423917 0.107627    0.0321296   0.00727824  61  LEU   B CD1  
2607 C CD2  . LEU   B 49  ? 0.446954 0.560115 0.402318 0.0826652   0.019471    0.011288    61  LEU   B CD2  
2608 H H    . LEU   B 49  ? 0.31005  0.530284 0.353753 0.095972    0.0136091   -0.0170242  61  LEU   B H    
2609 H HA   . LEU   B 49  ? 0.358077 0.53022  0.337286 0.0963449   -0.00157536 0.00764937  61  LEU   B HA   
2610 H HB2  . LEU   B 49  ? 0.397573 0.575268 0.39814  0.124005    0.00991031  0.00166654  61  LEU   B HB2  
2611 H HB3  . LEU   B 49  ? 0.408842 0.54606  0.370662 0.118351    0.00579387  0.0164851   61  LEU   B HB3  
2612 H HG   . LEU   B 49  ? 0.411531 0.56591  0.408707 0.0940228   0.02929     -0.00242671 61  LEU   B HG   
2613 H HD11 . LEU   B 49  ? 0.463667 0.584206 0.437432 0.118822    0.0349699   0.00298348  61  LEU   B HD11 
2614 H HD12 . LEU   B 49  ? 0.463009 0.554839 0.412692 0.0997198   0.0406109   0.00546963  61  LEU   B HD12 
2615 H HD13 . LEU   B 49  ? 0.471571 0.55456  0.410443 0.110664    0.0269629   0.0139802   61  LEU   B HD13 
2616 H HD21 . LEU   B 49  ? 0.419151 0.549449 0.388734 0.0750166   0.0186216   0.00715339  61  LEU   B HD21 
2617 H HD22 . LEU   B 49  ? 0.440328 0.544751 0.38351  0.0853149   0.0124775   0.0175906   61  LEU   B HD22 
2618 H HD23 . LEU   B 49  ? 0.444719 0.535841 0.386177 0.0780227   0.0252491   0.0124636   61  LEU   B HD23 
2619 N N    . SER   B 50  ? 0.485073 0.684987 0.451262 0.128077    -0.0221744  0.0161295   62  SER   B N    
2620 C CA   . SER   B 50  ? 0.562426 0.786369 0.519712 0.146431    -0.0361833  0.0192671   62  SER   B CA   
2621 C C    . SER   B 50  ? 0.596695 0.832674 0.562732 0.17141     -0.0421854  0.0202654   62  SER   B C    
2622 O O    . SER   B 50  ? 0.698752 0.972826 0.673562 0.188155    -0.0571638  0.0137885   62  SER   B O    
2623 C CB   . SER   B 50  ? 0.59033  0.785205 0.509151 0.147101    -0.0356247  0.0383951   62  SER   B CB   
2624 O OG   . SER   B 50  ? 0.654761 0.804301 0.556096 0.149994    -0.0267339  0.0539761   62  SER   B OG   
2625 H H    . SER   B 50  ? 0.485262 0.658498 0.435169 0.119716    -0.0174176  0.023806    62  SER   B H    
2626 H HA   . SER   B 50  ? 0.540224 0.794095 0.51282  0.142688    -0.0420637  0.0070077   62  SER   B HA   
2627 H HB2  . SER   B 50  ? 0.614344 0.824378 0.522262 0.160625    -0.0440896  0.0418474   62  SER   B HB2  
2628 H HB3  . SER   B 50  ? 0.585118 0.777249 0.502973 0.132228    -0.0323168  0.0359819   62  SER   B HB3  
2630 N N    . ASN   B 51  ? 0.62655  0.830496 0.589838 0.175071    -0.0315608  0.0269269   63  ASN   B N    
2631 C CA   . ASN   B 51  ? 0.697353 0.911338 0.678526 0.196666    -0.0326242  0.0240576   63  ASN   B CA   
2632 C C    . ASN   B 51  ? 0.734285 1.00322  0.763642 0.198567    -0.0367708  0.00164223  63  ASN   B C    
2633 O O    . ASN   B 51  ? 0.729458 1.02729  0.779447 0.221338    -0.046381   -0.00317558 63  ASN   B O    
2634 C CB   . ASN   B 51  ? 0.653672 0.827606 0.630797 0.192577    -0.0158832  0.0262765   63  ASN   B CB   
2635 H H    . ASN   B 51  ? 0.63186  0.806091 0.581764 0.163939    -0.0233459  0.0325655   63  ASN   B H    
2636 H HA   . ASN   B 51  ? 0.709345 0.920013 0.675805 0.214247    -0.0406656  0.0344214   63  ASN   B HA   
2639 N N    . GLY   B 52  ? 0.791224 1.07192  0.842356 0.174624    -0.0275686  -0.0119677  64  GLY   B N    
2640 C CA   . GLY   B 52  ? 0.693845 1.02308  0.796827 0.170085    -0.0268868  -0.0341785  64  GLY   B CA   
2641 C C    . GLY   B 52  ? 0.659005 0.97849  0.784622 0.15923     -0.00362448 -0.0401773  64  GLY   B C    
2642 O O    . GLY   B 52  ? 0.676534 1.03292  0.849627 0.152613    0.00262902  -0.057565   64  GLY   B O    
2643 H H    . GLY   B 52  ? 0.738331 0.994776 0.772785 0.160374    -0.0208918  -0.00694096 64  GLY   B H    
2644 H HA2  . GLY   B 52  ? 0.683995 1.02644  0.79328  0.157656    -0.030301   -0.0411952  64  GLY   B HA2  
2645 H HA3  . GLY   B 52  ? 0.711423 1.06903  0.83045  0.187019    -0.0381725  -0.0394204  64  GLY   B HA3  
2646 N N    . LYS   B 53  ? 0.639907 0.909888 0.731524 0.15574     0.0101856   -0.0270409  65  LYS   B N    
2647 C CA   . LYS   B 53  ? 0.629908 0.889123 0.731933 0.159639    0.0295765   -0.0304228  65  LYS   B CA   
2648 C C    . LYS   B 53  ? 0.62515  0.870959 0.7294   0.137298    0.0516065   -0.0340889  65  LYS   B C    
2649 O O    . LYS   B 53  ? 0.662011 0.903186 0.775201 0.139637    0.0713293   -0.0382502  65  LYS   B O    
2650 C CB   . LYS   B 53  ? 0.62523  0.839977 0.689098 0.174656    0.0299814   -0.017153   65  LYS   B CB   
2651 H H    . LYS   B 53  ? 0.645819 0.889221 0.70776  0.150639    0.00775291  -0.0171829  65  LYS   B H    
2652 H HA   . LYS   B 53  ? 0.627941 0.919952 0.763412 0.169935    0.0283162   -0.0399534  65  LYS   B HA   
2655 N N    . LYS   B 54  ? 0.536574 0.774174 0.630099 0.117708    0.0495391   -0.0314544  66  LYS   B N    
2656 C CA   . LYS   B 54  ? 0.469472 0.699656 0.56988  0.097858    0.0679824   -0.0336526  66  LYS   B CA   
2657 C C    . LYS   B 54  ? 0.458323 0.715921 0.586688 0.0841081   0.0595824   -0.0416711  66  LYS   B C    
2658 O O    . LYS   B 54  ? 0.613048 0.856848 0.717907 0.0780907   0.047029    -0.03557    66  LYS   B O    
2659 C CB   . LYS   B 54  ? 0.423733 0.603221 0.472966 0.0890877   0.0725479   -0.0203036  66  LYS   B CB   
2660 H H    . LYS   B 54  ? 0.533153 0.768161 0.613354 0.117692    0.0365046   -0.0270997  66  LYS   B H    
2661 H HA   . LYS   B 54  ? 0.478325 0.719572 0.599904 0.0994      0.0824916   -0.0394638  66  LYS   B HA   
2664 N N    . PHE   B 55  ? 0.371056 0.669951 0.553504 0.0799842   0.0657282   -0.0577154  67  PHE   B N    
2665 C CA   . PHE   B 55  ? 0.324601 0.651241 0.540242 0.0667228   0.0579957   -0.0706078  67  PHE   B CA   
2666 C C    . PHE   B 55  ? 0.303221 0.609612 0.527657 0.0450589   0.0802377   -0.0683069  67  PHE   B C    
2667 O O    . PHE   B 55  ? 0.304645 0.601952 0.538349 0.0414085   0.104717    -0.0653715  67  PHE   B O    
2668 C CB   . PHE   B 55  ? 0.319931 0.703705 0.594007 0.0750601   0.050799    -0.0919402  67  PHE   B CB   
2669 C CG   . PHE   B 55  ? 0.323743 0.74538  0.633279 0.0668911   0.0343781   -0.111689   67  PHE   B CG   
2670 C CD1  . PHE   B 55  ? 0.328155 0.760816 0.68324  0.0450076   0.0492068   -0.125518   67  PHE   B CD1  
2671 C CD2  . PHE   B 55  ? 0.344492 0.789092 0.640693 0.081846    0.00526065  -0.116993   67  PHE   B CD2  
2672 C CE1  . PHE   B 55  ? 0.323248 0.789313 0.712647 0.0370478   0.0336859   -0.147769   67  PHE   B CE1  
2673 C CE2  . PHE   B 55  ? 0.345305 0.824778 0.669268 0.0752929   -0.0104688  -0.138305   67  PHE   B CE2  
2674 C CZ   . PHE   B 55  ? 0.320861 0.811424 0.693068 0.0524843   0.00297781  -0.155487   67  PHE   B CZ   
2675 H H    . PHE   B 55  ? 0.387978 0.698622 0.5898   0.0853243   0.0755952   -0.062273   67  PHE   B H    
2676 H HA   . PHE   B 55  ? 0.321605 0.643142 0.515895 0.0683965   0.042627    -0.0672862  67  PHE   B HA   
2677 H HB2  . PHE   B 55  ? 0.330701 0.721039 0.593795 0.0920117   0.0394499   -0.0894946  67  PHE   B HB2  
2678 H HB3  . PHE   B 55  ? 0.327825 0.718622 0.629446 0.0703584   0.0686169   -0.0964437  67  PHE   B HB3  
2679 H HD1  . PHE   B 55  ? 0.332528 0.74784  0.693886 0.0356049   0.0706342   -0.119811   67  PHE   B HD1  
2680 H HD2  . PHE   B 55  ? 0.349491 0.783442 0.614825 0.0966442   -0.00312884 -0.10577    67  PHE   B HD2  
2681 H HE1  . PHE   B 55  ? 0.319729 0.790045 0.742292 0.0213973   0.0448245   -0.157606   67  PHE   B HE1  
2682 H HE2  . PHE   B 55  ? 0.342975 0.837356 0.652215 0.0867834   -0.0297491  -0.141354   67  PHE   B HE2  
2683 H HZ   . PHE   B 55  ? 0.320379 0.834542 0.713532 0.0479186   -0.00805407 -0.172663   67  PHE   B HZ   
2684 N N    . ASP   B 56  ? 0.259893 0.55826  0.480923 0.0322725   0.0734977   -0.0689626  68  ASP   B N    
2685 C CA   . ASP   B 56  ? 0.287728 0.560668 0.512976 0.0142084   0.0928989   -0.0635038  68  ASP   B CA   
2686 C C    . ASP   B 56  ? 0.299159 0.596058 0.568683 0.00066043  0.087672    -0.0812901  68  ASP   B C    
2687 O O    . ASP   B 56  ? 0.287488 0.597766 0.550684 0.00409517  0.0655452   -0.0889011  68  ASP   B O    
2688 C CB   . ASP   B 56  ? 0.279233 0.504323 0.446389 0.0136161   0.090553    -0.0430795  68  ASP   B CB   
2689 C CG   . ASP   B 56  ? 0.293724 0.490901 0.460233 -0.00125255 0.104911    -0.0353091  68  ASP   B CG   
2690 O OD1  . ASP   B 56  ? 0.325089 0.519874 0.518385 -0.0105579  0.129096    -0.0355659  68  ASP   B OD1  
2691 O OD2  . ASP   B 56  ? 0.316332 0.493071 0.456697 -0.00284706 0.0933444   -0.0279115  68  ASP   B OD2  
2692 H H    . ASP   B 56  ? 0.264597 0.572833 0.479662 0.0360649   0.0567016   -0.0724485  68  ASP   B H    
2693 H HA   . ASP   B 56  ? 0.296749 0.567648 0.535482 0.0114238   0.111729    -0.0622544  68  ASP   B HA   
2694 H HB2  . ASP   B 56  ? 0.296489 0.504566 0.437639 0.0204407   0.0959517   -0.0339572  68  ASP   B HB2  
2695 H HB3  . ASP   B 56  ? 0.274089 0.502069 0.427552 0.017688    0.0733638   -0.0436112  68  ASP   B HB3  
2696 N N    . SER   B 57  ? 0.36812  0.665907 0.679821 -0.0152524  0.110253    -0.0873351  69  SER   B N    
2697 C CA   . SER   B 57  ? 0.426444 0.74362  0.786156 -0.0298856  0.107441    -0.107324   69  SER   B CA   
2698 C C    . SER   B 57  ? 0.450048 0.728138 0.815615 -0.0470538  0.13172     -0.0965918  69  SER   B C    
2699 O O    . SER   B 57  ? 0.428266 0.690675 0.805881 -0.0541019  0.160564    -0.0868183  69  SER   B O    
2700 C CB   . SER   B 57  ? 0.433211 0.803244 0.862142 -0.033444   0.10792     -0.134563   69  SER   B CB   
2701 O OG   . SER   B 57  ? 0.489567 0.882205 0.959075 -0.0447337  0.0962989   -0.159204   69  SER   B OG   
2702 H H    . SER   B 57  ? 0.377549 0.662282 0.688266 -0.0172331  0.128923    -0.0791936  69  SER   B H    
2703 H HA   . SER   B 57  ? 0.404383 0.726407 0.74885  -0.0256262  0.0881078   -0.111566   69  SER   B HA   
2704 H HB2  . SER   B 57  ? 0.437661 0.830631 0.861049 -0.0199695  0.0937993   -0.138627   69  SER   B HB2  
2705 H HB3  . SER   B 57  ? 0.455798 0.821978 0.908263 -0.0409858  0.130323    -0.132187   69  SER   B HB3  
2707 N N    . SER   B 58  ? 0.42375  0.686032 0.781183 -0.0524336  0.121333    -0.0981211  70  SER   B N    
2708 C CA   . SER   B 58  ? 0.428314 0.660076 0.806843 -0.0683607  0.141401    -0.0940724  70  SER   B CA   
2709 C C    . SER   B 58  ? 0.446826 0.706867 0.903166 -0.085123   0.157837    -0.118003   70  SER   B C    
2710 O O    . SER   B 58  ? 0.454785 0.68727  0.933546 -0.0987321  0.187854    -0.108571   70  SER   B O    
2711 C CB   . SER   B 58  ? 0.422428 0.640953 0.789697 -0.0694292  0.125341    -0.0979221  70  SER   B CB   
2712 O OG   . SER   B 58  ? 0.395238 0.655023 0.809252 -0.0747908  0.110136    -0.131183   70  SER   B OG   
2713 H H    . SER   B 58  ? 0.41358  0.683171 0.75182  -0.045259   0.102268    -0.101186   70  SER   B H    
2714 H HA   . SER   B 58  ? 0.451816 0.651717 0.803583 -0.0675583  0.156978    -0.0731902  70  SER   B HA   
2715 H HB2  . SER   B 58  ? 0.436391 0.624715 0.805211 -0.0762503  0.139428    -0.0879334  70  SER   B HB2  
2716 H HB3  . SER   B 58  ? 0.41021  0.621492 0.736244 -0.0589184  0.111624    -0.0879363  70  SER   B HB3  
2718 N N    . HIS   B 59  ? 0.442782 0.757348 0.94057  -0.0838568  0.138058    -0.14899    71  HIS   B N    
2719 C CA   . HIS   B 59  ? 0.533113 0.883747 1.11378  -0.100159   0.149381    -0.177904   71  HIS   B CA   
2720 C C    . HIS   B 59  ? 0.546526 0.891081 1.15112  -0.107012   0.183956    -0.165334   71  HIS   B C    
2721 O O    . HIS   B 59  ? 0.590368 0.930701 1.25284  -0.127071   0.211377    -0.172937   71  HIS   B O    
2722 C CB   . HIS   B 59  ? 0.551764 0.967779 1.16524  -0.0919951  0.11824     -0.212146   71  HIS   B CB   
2723 C CG   . HIS   B 59  ? 0.647944 1.07569  1.24523  -0.0868813  0.0879792   -0.229825   71  HIS   B CG   
2724 N ND1  . HIS   B 59  ? 0.703113 1.12742  1.34007  -0.103355   0.0898683   -0.252116   71  HIS   B ND1  
2725 C CD2  . HIS   B 59  ? 0.667263 1.10746  1.21356  -0.0676436  0.0585304   -0.228577   71  HIS   B CD2  
2726 C CE1  . HIS   B 59  ? 0.669317 1.10613  1.2783   -0.0935051  0.0620293   -0.265561   71  HIS   B CE1  
2727 N NE2  . HIS   B 59  ? 0.691832 1.13825  1.24472  -0.0720729  0.0436663   -0.250158   71  HIS   B NE2  
2728 H H    . HIS   B 59  ? 0.443611 0.773712 0.918299 -0.0724215  0.116788    -0.152598   71  HIS   B H    
2729 H HA   . HIS   B 59  ? 0.529641 0.865264 1.13199  -0.112417   0.156141    -0.184265   71  HIS   B HA   
2730 H HB2  . HIS   B 59  ? 0.557526 0.985264 1.14673  -0.0779459  0.110543    -0.204109   71  HIS   B HB2  
2731 H HB3  . HIS   B 59  ? 0.568085 1.01009  1.24051  -0.10313    0.126418    -0.231906   71  HIS   B HB3  
2733 H HD2  . HIS   B 59  ? 0.659056 1.10158  1.17137  -0.0537067  0.0508384   -0.21547    71  HIS   B HD2  
2734 H HE1  . HIS   B 59  ? 0.687613 1.12495  1.31378  -0.100496   0.0575944   -0.283103   71  HIS   B HE1  
2736 N N    . ASP   B 60  ? 0.568376 0.909244 1.12736  -0.090486   0.185       -0.145721   72  ASP   B N    
2737 C CA   . ASP   B 60  ? 0.609157 0.945801 1.18174  -0.0930675  0.218145    -0.133728   72  ASP   B CA   
2738 C C    . ASP   B 60  ? 0.645431 0.916202 1.16586  -0.0965051  0.247761    -0.0980783  72  ASP   B C    
2739 O O    . ASP   B 60  ? 0.72809  0.980544 1.21222  -0.0881117  0.266601    -0.077955   72  ASP   B O    
2740 C CB   . ASP   B 60  ? 0.582556 0.949314 1.13718  -0.0724767  0.205405    -0.134481   72  ASP   B CB   
2741 H H    . ASP   B 60  ? 0.55248  0.893076 1.07083  -0.0770552  0.16521     -0.140364   72  ASP   B H    
2742 H HA   . ASP   B 60  ? 0.606227 0.965581 1.24003  -0.106285   0.231158    -0.150493   72  ASP   B HA   
2745 N N    . ARG   B 61  ? 0.644212 0.878727 1.15631  -0.106181   0.249688    -0.0906116  73  ARG   B N    
2746 C CA   . ARG   B 61  ? 0.684689 0.860136 1.16841  -0.112855   0.28159     -0.0605812  73  ARG   B CA   
2747 C C    . ARG   B 61  ? 0.678725 0.840725 1.22002  -0.134046   0.296409    -0.0707025  73  ARG   B C    
2748 O O    . ARG   B 61  ? 0.701314 0.812418 1.22934  -0.141016   0.325824    -0.046025   73  ARG   B O    
2749 C CB   . ARG   B 61  ? 0.700094 0.833719 1.09488  -0.0955645  0.263924    -0.0339415  73  ARG   B CB   
2750 H H    . ARG   B 61  ? 0.627831 0.873536 1.14758  -0.106478   0.229057    -0.103738   73  ARG   B H    
2751 H HA   . ARG   B 61  ? 0.702345 0.874801 1.18875  -0.114084   0.305735    -0.0517935  73  ARG   B HA   
2754 N N    . ASN   B 62  ? 0.614361 0.819695 1.21559  -0.142553   0.274811    -0.107035   74  ASN   B N    
2755 C CA   . ASN   B 62  ? 0.619373 0.823492 1.29217  -0.164691   0.286768    -0.128003   74  ASN   B CA   
2756 C C    . ASN   B 62  ? 0.604098 0.771745 1.24975  -0.162718   0.27135     -0.123652   74  ASN   B C    
2757 O O    . ASN   B 62  ? 0.620286 0.793221 1.32284  -0.177809   0.27088     -0.148921   74  ASN   B O    
2758 C CB   . ASN   B 62  ? 0.653984 0.832376 1.37259  -0.184591   0.336221    -0.116288   74  ASN   B CB   
2759 H H    . ASN   B 62  ? 0.595791 0.832819 1.19153  -0.133352   0.250467    -0.120304   74  ASN   B H    
2760 H HA   . ASN   B 62  ? 0.59398  0.843465 1.31151  -0.168483   0.271441    -0.157676   74  ASN   B HA   
2763 N N    . GLU   B 63  ? 0.576586 0.710472 1.14084  -0.144143   0.257582    -0.0953983  75  GLU   B N    
2764 C CA   . GLU   B 63  ? 0.577919 0.666448 1.11766  -0.142047   0.25363     -0.0827114  75  GLU   B CA   
2765 C C    . GLU   B 63  ? 0.497719 0.594751 0.980766 -0.122881   0.216053    -0.0817567  75  GLU   B C    
2766 O O    . GLU   B 63  ? 0.41956  0.533848 0.858654 -0.108872   0.20101     -0.0740321  75  GLU   B O    
2767 C CB   . GLU   B 63  ? 0.677528 0.701465 1.18131  -0.14104    0.285631    -0.0418923  75  GLU   B CB   
2768 C CG   . GLU   B 63  ? 0.72121  0.71925  1.1349   -0.11909    0.276096    -0.00830673 75  GLU   B CG   
2769 C CD   . GLU   B 63  ? 0.819733 0.756433 1.18985  -0.114805   0.306333    0.0322322   75  GLU   B CD   
2770 O OE1  . GLU   B 63  ? 0.803228 0.714025 1.09988  -0.0960675  0.293867    0.0573636   75  GLU   B OE1  
2771 O OE2  . GLU   B 63  ? 0.916393 0.830586 1.32533  -0.129907   0.343118    0.0390318   75  GLU   B OE2  
2772 H H    . GLU   B 63  ? 0.569934 0.710478 1.0962   -0.132309   0.249864    -0.0852695  75  GLU   B H    
2773 H HA   . GLU   B 63  ? 0.580271 0.675123 1.16862  -0.154044   0.255192    -0.103347   75  GLU   B HA   
2774 H HB2  . GLU   B 63  ? 0.690727 0.687901 1.20583  -0.145113   0.289467    -0.0399807  75  GLU   B HB2  
2775 H HB3  . GLU   B 63  ? 0.692883 0.716145 1.22362  -0.151062   0.311206    -0.0393164  75  GLU   B HB3  
2776 H HG2  . GLU   B 63  ? 0.704028 0.727905 1.10659  -0.114418   0.270964    -0.0119496  75  GLU   B HG2  
2777 H HG3  . GLU   B 63  ? 0.704292 0.70158  1.09513  -0.110268   0.252724    -0.010084   75  GLU   B HG3  
2778 N N    . PRO   B 64  ? 0.465077 0.549861 0.951288 -0.12216    0.20173     -0.0906819  76  PRO   B N    
2779 C CA   . PRO   B 64  ? 0.434679 0.532867 0.876816 -0.106249   0.169261    -0.09309    76  PRO   B CA   
2780 C C    . PRO   B 64  ? 0.403434 0.469085 0.773056 -0.0899192  0.165599    -0.0572078  76  PRO   B C    
2781 O O    . PRO   B 64  ? 0.451387 0.473585 0.801026 -0.0893225  0.186639    -0.0295614  76  PRO   B O    
2782 C CB   . PRO   B 64  ? 0.444854 0.531104 0.912057 -0.110151   0.162858    -0.109109   76  PRO   B CB   
2783 C CG   . PRO   B 64  ? 0.47671  0.542394 1.00617  -0.12942    0.191015    -0.117808   76  PRO   B CG   
2784 C CD   . PRO   B 64  ? 0.502821 0.558914 1.03688  -0.136379   0.218586    -0.0987933  76  PRO   B CD   
2785 H HA   . PRO   B 64  ? 0.403738 0.539778 0.851205 -0.103929   0.154763    -0.109693   76  PRO   B HA   
2786 H HB2  . PRO   B 64  ? 0.45137  0.51055  0.885736 -0.101259   0.159431    -0.0911995  76  PRO   B HB2  
2787 H HB3  . PRO   B 64  ? 0.422979 0.541537 0.900319 -0.108878   0.145061    -0.132137   76  PRO   B HB3  
2788 H HG2  . PRO   B 64  ? 0.499723 0.529363 1.02535  -0.128455   0.198248    -0.106377   76  PRO   B HG2  
2789 H HG3  . PRO   B 64  ? 0.468258 0.562495 1.0402   -0.138113   0.185005    -0.147819   76  PRO   B HG3  
2790 H HD2  . PRO   B 64  ? 0.528887 0.542987 1.04428  -0.135088   0.236059    -0.073167   76  PRO   B HD2  
2791 H HD3  . PRO   B 64  ? 0.502324 0.57639  1.0883   -0.150331   0.229226    -0.118189   76  PRO   B HD3  
2792 N N    . PHE   B 65  ? 0.359064 0.447143 0.690833 -0.0768988  0.139274    -0.0591148  77  PHE   B N    
2793 C CA   . PHE   B 65  ? 0.364271 0.427738 0.633674 -0.0621151  0.128929    -0.0328583  77  PHE   B CA   
2794 C C    . PHE   B 65  ? 0.363959 0.408097 0.62977  -0.0578806  0.118553    -0.0313287  77  PHE   B C    
2795 O O    . PHE   B 65  ? 0.345176 0.413075 0.637736 -0.0604668  0.106549    -0.0553305  77  PHE   B O    
2796 C CB   . PHE   B 65  ? 0.333843 0.428693 0.573405 -0.0523044  0.10847     -0.0371008  77  PHE   B CB   
2797 C CG   . PHE   B 65  ? 0.338059 0.410614 0.519216 -0.0392658  0.0972146   -0.0142481  77  PHE   B CG   
2798 C CD1  . PHE   B 65  ? 0.363419 0.415929 0.508573 -0.0339721  0.106757    0.00541692  77  PHE   B CD1  
2799 C CD2  . PHE   B 65  ? 0.326115 0.399131 0.49089  -0.032667   0.0779059   -0.0146519  77  PHE   B CD2  
2800 C CE1  . PHE   B 65  ? 0.368518 0.402567 0.462616 -0.0226232  0.0939794   0.021744    77  PHE   B CE1  
2801 C CE2  . PHE   B 65  ? 0.335851 0.391408 0.455204 -0.0225129  0.0668704   0.00314665  77  PHE   B CE2  
2802 C CZ   . PHE   B 65  ? 0.356911 0.392882 0.441077 -0.0176789  0.0735009   0.0202634   77  PHE   B CZ   
2803 H H    . PHE   B 65  ? 0.343098 0.463595 0.68973  -0.0773562  0.127183    -0.078253   77  PHE   B H    
2804 H HA   . PHE   B 65  ? 0.387564 0.425584 0.63884  -0.0610022  0.143253    -0.0137716  77  PHE   B HA   
2805 H HB2  . PHE   B 65  ? 0.33261  0.440879 0.580141 -0.0542754  0.115575    -0.0398637  77  PHE   B HB2  
2806 H HB3  . PHE   B 65  ? 0.315693 0.434314 0.569151 -0.0524093  0.0954785   -0.0541032  77  PHE   B HB3  
2807 H HD1  . PHE   B 65  ? 0.371595 0.424652 0.528194 -0.0381915  0.122036    0.00593076  77  PHE   B HD1  
2808 H HD2  . PHE   B 65  ? 0.31653  0.402665 0.50317  -0.0353923  0.0727304   -0.0284205  77  PHE   B HD2  
2809 H HE1  . PHE   B 65  ? 0.386266 0.406705 0.4542   -0.0185909  0.100099    0.0328696   77  PHE   B HE1  
2810 H HE2  . PHE   B 65  ? 0.326428 0.384775 0.440387 -0.0190741  0.0549938   0.00185467  77  PHE   B HE2  
2811 H HZ   . PHE   B 65  ? 0.361604 0.387054 0.416193 -0.0110889  0.0644127   0.0294294   77  PHE   B HZ   
2812 N N    . VAL   B 66  ? 0.408604 0.410096 0.642712 -0.050322   0.124282    -0.00406826 78  VAL   B N    
2813 C CA   . VAL   B 66  ? 0.433304 0.41186  0.670754 -0.0448294  0.117988    -0.00010069 78  VAL   B CA   
2814 C C    . VAL   B 66  ? 0.426276 0.39291  0.61177  -0.0288005  0.0998958   0.0199458   78  VAL   B C    
2815 O O    . VAL   B 66  ? 0.44666  0.394002 0.590945 -0.0221499  0.103274    0.0418424   78  VAL   B O    
2816 C CB   . VAL   B 66  ? 0.490638 0.425602 0.749314 -0.0498773  0.142728    0.01331     78  VAL   B CB   
2817 C CG1  . VAL   B 66  ? 0.509165 0.417781 0.773041 -0.0410523  0.135918    0.018417    78  VAL   B CG1  
2818 C CG2  . VAL   B 66  ? 0.50226  0.450479 0.820896 -0.0690175  0.162253    -0.00943809 78  VAL   B CG2  
2819 H H    . VAL   B 66  ? 0.422863 0.40967  0.631799 -0.047166   0.131784    0.0122367   78  VAL   B H    
2820 H HA   . VAL   B 66  ? 0.411576 0.411364 0.673038 -0.0478056  0.109567    -0.0201954  78  VAL   B HA   
2821 H HB   . VAL   B 66  ? 0.513568 0.42695  0.742583 -0.0455813  0.151769    0.034858    78  VAL   B HB   
2822 H HG11 . VAL   B 66  ? 0.484675 0.416607 0.767958 -0.042316   0.124185    -0.00190129 78  VAL   B HG11 
2823 H HG12 . VAL   B 66  ? 0.518048 0.413037 0.745581 -0.0289201  0.126854    0.0366046   78  VAL   B HG12 
2824 H HG13 . VAL   B 66  ? 0.537038 0.419084 0.822103 -0.0456127  0.152656    0.0233592   78  VAL   B HG13 
2825 H HG21 . VAL   B 66  ? 0.528744 0.446736 0.864771 -0.0729788  0.17851     -0.00175128 78  VAL   B HG21 
2826 H HG22 . VAL   B 66  ? 0.495217 0.455283 0.810979 -0.0732412  0.169779    -0.00830192 78  VAL   B HG22 
2827 H HG23 . VAL   B 66  ? 0.475211 0.450561 0.818773 -0.0727197  0.151117    -0.0335101  78  VAL   B HG23 
2828 N N    . PHE   B 67  ? 0.406096 0.385576 0.595825 -0.0227461  0.0812812   0.0103966   79  PHE   B N    
2829 C CA   . PHE   B 67  ? 0.391666 0.366188 0.543281 -0.00925145 0.0625457   0.0248372   79  PHE   B CA   
2830 C C    . PHE   B 67  ? 0.376838 0.356765 0.550631 -0.00368624 0.0509441   0.0152703   79  PHE   B C    
2831 O O    . PHE   B 67  ? 0.350316 0.344675 0.562611 -0.0103996  0.0552738   -0.00641474 79  PHE   B O    
2832 C CB   . PHE   B 67  ? 0.357835 0.360188 0.482883 -0.00890449 0.0503645   0.0208888   79  PHE   B CB   
2833 C CG   . PHE   B 67  ? 0.32905  0.370649 0.473891 -0.0129034  0.0402234   -0.00240715 79  PHE   B CG   
2834 C CD1  . PHE   B 67  ? 0.300211 0.366698 0.472811 -0.0220177  0.0470113   -0.0228554  79  PHE   B CD1  
2835 C CD2  . PHE   B 67  ? 0.311537 0.366114 0.447248 -0.0069157  0.0243107   -0.00406569 79  PHE   B CD2  
2836 C CE1  . PHE   B 67  ? 0.277624 0.378464 0.459618 -0.0226645  0.037237    -0.0425696  79  PHE   B CE1  
2837 C CE2  . PHE   B 67  ? 0.282419 0.369662 0.43105  -0.00957722 0.0189692   -0.0225825  79  PHE   B CE2  
2838 C CZ   . PHE   B 67  ? 0.269388 0.378739 0.436242 -0.0162427  0.0248514   -0.0408416  79  PHE   B CZ   
2839 H H    . PHE   B 67  ? 0.392211 0.385024 0.610825 -0.0273297  0.0806402   -0.00670359 79  PHE   B H    
2840 H HA   . PHE   B 67  ? 0.419864 0.367204 0.549154 -0.00324215 0.0665505   0.0439239   79  PHE   B HA   
2841 H HB2  . PHE   B 67  ? 0.36808  0.361777 0.466832 -0.00118079 0.0404172   0.0322944   79  PHE   B HB2  
2842 H HB3  . PHE   B 67  ? 0.364996 0.366744 0.483617 -0.0127766  0.0596514   0.0232395   79  PHE   B HB3  
2843 H HD1  . PHE   B 67  ? 0.313107 0.373613 0.497951 -0.0273648  0.0584666   -0.0234392  79  PHE   B HD1  
2844 H HD2  . PHE   B 67  ? 0.321082 0.36245  0.442451 -0.00074354 0.0177064   0.00733152  79  PHE   B HD2  
2845 H HE1  . PHE   B 67  ? 0.271301 0.39044  0.470039 -0.0272879  0.0395439   -0.0572659  79  PHE   B HE1  
2846 H HE2  . PHE   B 67  ? 0.275505 0.370835 0.41918  -0.00633057 0.0111286   -0.0226268  79  PHE   B HE2  
2847 H HZ   . PHE   B 67  ? 0.257689 0.388828 0.427604 -0.0162032  0.0205621   -0.0525746  79  PHE   B HZ   
2848 N N    . SER   B 68  ? 0.386706 0.356113 0.53746  0.00933306  0.036054    0.0298264   80  SER   B N    
2849 C CA   . SER   B 68  ? 0.392295 0.371159 0.565175 0.0166737   0.0242023   0.0213912   80  SER   B CA   
2850 C C    . SER   B 68  ? 0.343291 0.360902 0.512595 0.014557    0.0106507   0.00780361  80  SER   B C    
2851 O O    . SER   B 68  ? 0.340133 0.362254 0.478955 0.0172164   -0.00016978 0.0173197   80  SER   B O    
2852 C CB   . SER   B 68  ? 0.414892 0.367115 0.572785 0.0330953   0.0136482   0.0422253   80  SER   B CB   
2853 O OG   . SER   B 68  ? 0.472865 0.385464 0.637971 0.0372692   0.0280183   0.05591     80  SER   B OG   
2854 H H    . SER   B 68  ? 0.40306  0.360528 0.524655 0.014205    0.0329686   0.0443078   80  SER   B H    
2855 H HA   . SER   B 68  ? 0.385301 0.364229 0.587834 0.0126414   0.0324924   0.00935981  80  SER   B HA   
2856 H HB2  . SER   B 68  ? 0.426981 0.37621  0.553765 0.0368995   0.00600218  0.0535397   80  SER   B HB2  
2857 H HB3  . SER   B 68  ? 0.411304 0.376847 0.585544 0.0380396   0.00413739  0.0348515   80  SER   B HB3  
2859 N N    . LEU   B 69  ? 0.328593 0.371085 0.528614 0.0106761   0.0121774   -0.0141782  81  LEU   B N    
2860 C CA   . LEU   B 69  ? 0.299524 0.377124 0.49496  0.00772516  0.00503576  -0.0261056  81  LEU   B CA   
2861 C C    . LEU   B 69  ? 0.283163 0.366943 0.473502 0.0157438   -0.00895033 -0.0180739  81  LEU   B C    
2862 O O    . LEU   B 69  ? 0.288551 0.363109 0.496726 0.025032    -0.0140647  -0.0147067  81  LEU   B O    
2863 C CB   . LEU   B 69  ? 0.337844 0.438315 0.56294  0.00354063  0.0120069   -0.0517548  81  LEU   B CB   
2864 C CG   . LEU   B 69  ? 0.357936 0.493679 0.573997 0.00137119  0.00885374  -0.063423   81  LEU   B CG   
2865 C CD1  . LEU   B 69  ? 0.379068 0.524646 0.568426 -0.00420749 0.00859712  -0.0608472  81  LEU   B CD1  
2866 C CD2  . LEU   B 69  ? 0.385823 0.540265 0.628387 0.00108876  0.0154375   -0.0888402  81  LEU   B CD2  
2867 H H    . LEU   B 69  ? 0.335455 0.371492 0.558511 0.0102127   0.0188015   -0.0217221  81  LEU   B H    
2868 H HA   . LEU   B 69  ? 0.298623 0.38129  0.475347 0.00335087  0.00550868  -0.0235796  81  LEU   B HA   
2869 H HB2  . LEU   B 69  ? 0.337942 0.435401 0.569938 -0.00202669 0.0192718   -0.0586645  81  LEU   B HB2  
2870 H HB3  . LEU   B 69  ? 0.343658 0.437892 0.588571 0.00844253  0.0124673   -0.0549844  81  LEU   B HB3  
2871 H HG   . LEU   B 69  ? 0.356169 0.494754 0.56726  0.00506986  0.00297752  -0.0557745  81  LEU   B HG   
2872 H HD11 . LEU   B 69  ? 0.369203 0.503553 0.54079  -0.0031389  0.00443174  -0.0459913  81  LEU   B HD11 
2873 H HD12 . LEU   B 69  ? 0.360947 0.526849 0.544202 -0.00450023 0.00796298  -0.0681174  81  LEU   B HD12 
2874 H HD13 . LEU   B 69  ? 0.372265 0.515055 0.569136 -0.00788874 0.0134993   -0.067193   81  LEU   B HD13 
2875 H HD21 . LEU   B 69  ? 0.382484 0.530895 0.642586 0.00603534  0.0155851   -0.0897458  81  LEU   B HD21 
2876 H HD22 . LEU   B 69  ? 0.380668 0.53165  0.632985 -0.00292846 0.020149    -0.098498   81  LEU   B HD22 
2877 H HD23 . LEU   B 69  ? 0.368257 0.544251 0.600925 0.00050174  0.0151602   -0.0953947  81  LEU   B HD23 
2878 N N    . GLY   B 70  ? 0.268787 0.369558 0.438691 0.0120668   -0.0149546  -0.0163474  82  GLY   B N    
2879 C CA   . GLY   B 70  ? 0.270162 0.384966 0.444051 0.0151566   -0.0259026  -0.0145789  82  GLY   B CA   
2880 C C    . GLY   B 70  ? 0.319621 0.415137 0.480438 0.0235728   -0.0409592  0.00117584  82  GLY   B C    
2881 O O    . GLY   B 70  ? 0.321852 0.429774 0.499511 0.028137    -0.0520986  -0.00018468 82  GLY   B O    
2882 H H    . GLY   B 70  ? 0.264611 0.368082 0.420211 0.0072398   -0.0114926  -0.0166777  82  GLY   B H    
2883 H HA2  . GLY   B 70  ? 0.263802 0.390722 0.42637  0.0100098   -0.0253647  -0.0160806  82  GLY   B HA2  
2884 H HA3  . GLY   B 70  ? 0.27125  0.397861 0.469248 0.0172311   -0.0238504  -0.0235143  82  GLY   B HA3  
2885 N N    . LYS   B 71  ? 0.330291 0.397649 0.462617 0.0263365   -0.040665   0.0147748   83  LYS   B N    
2886 C CA   . LYS   B 71  ? 0.374975 0.422185 0.482716 0.0364868   -0.0555736  0.0301465   83  LYS   B CA   
2887 C C    . LYS   B 71  ? 0.382064 0.425361 0.451818 0.0318169   -0.0596313  0.0347956   83  LYS   B C    
2888 O O    . LYS   B 71  ? 0.44872  0.475688 0.489394 0.0394757   -0.0716501  0.0449138   83  LYS   B O    
2889 C CB   . LYS   B 71  ? 0.378428 0.392874 0.479785 0.0456896   -0.0492261  0.0435718   83  LYS   B CB   
2890 H H    . LYS   B 71  ? 0.334977 0.3966   0.462343 0.022024    -0.0304896  0.0138235   83  LYS   B H    
2891 H HA   . LYS   B 71  ? 0.366595 0.424704 0.489346 0.0412567   -0.0669724  0.0276524   83  LYS   B HA   
2894 N N    . GLY   B 72  ? 0.412249 0.470495 0.480392 0.0208418   -0.0505927  0.026528    84  GLY   B N    
2895 C CA   . GLY   B 72  ? 0.431176 0.482645 0.466104 0.0174908   -0.0518638  0.0301095   84  GLY   B CA   
2896 C C    . GLY   B 72  ? 0.438089 0.462428 0.440612 0.0216351   -0.0442014  0.0417332   84  GLY   B C    
2897 O O    . GLY   B 72  ? 0.447627 0.460458 0.417403 0.0236081   -0.0488829  0.0461444   84  GLY   B O    
2898 H H    . GLY   B 72  ? 0.383324 0.455922 0.470573 0.0164586   -0.0436298  0.0182322   84  GLY   B H    
2899 H HA2  . GLY   B 72  ? 0.406099 0.469905 0.445579 0.0111      -0.0449818  0.0240963   84  GLY   B HA2  
2900 H HA3  . GLY   B 72  ? 0.429175 0.481967 0.45871  0.0191394   -0.064041   0.0301965   84  GLY   B HA3  
2901 N N    . GLN   B 73  ? 0.385248 0.400154 0.399257 0.0214739   -0.0294892  0.0447194   85  GLN   B N    
2902 C CA   . GLN   B 73  ? 0.367114 0.361007 0.359445 0.0213513   -0.0141681  0.0540511   85  GLN   B CA   
2903 C C    . GLN   B 73  ? 0.339866 0.349717 0.33327  0.0126479   -0.00353332 0.0450222   85  GLN   B C    
2904 O O    . GLN   B 73  ? 0.333478 0.33195  0.3112   0.0118929   0.00967548  0.0503286   85  GLN   B O    
2905 C CB   . GLN   B 73  ? 0.38366  0.362387 0.397491 0.0215142   0.00020824  0.0586039   85  GLN   B CB   
2906 C CG   . GLN   B 73  ? 0.417178 0.371206 0.422677 0.0343871   -0.00805398 0.073236    85  GLN   B CG   
2907 C CD   . GLN   B 73  ? 0.440029 0.376554 0.474229 0.0342039   0.00720203  0.0766162   85  GLN   B CD   
2908 O OE1  . GLN   B 73  ? 0.434088 0.375966 0.494731 0.0226477   0.0250965   0.0667956   85  GLN   B OE1  
2909 N NE2  . GLN   B 73  ? 0.475153 0.39222  0.509467 0.0475468   -0.00139555 0.0882862   85  GLN   B NE2  
2910 H H    . GLN   B 73  ? 0.380083 0.402066 0.418725 0.0208411   -0.0277132  0.0398788   85  GLN   B H    
2911 H HA   . GLN   B 73  ? 0.397904 0.376034 0.360905 0.0276223   -0.0194894  0.0633364   85  GLN   B HA   
2912 H HB2  . GLN   B 73  ? 0.362214 0.357143 0.405517 0.0161986   0.00279545  0.0469606   85  GLN   B HB2  
2913 H HB3  . GLN   B 73  ? 0.393383 0.36212  0.399315 0.018636    0.013701    0.0628734   85  GLN   B HB3  
2914 H HG2  . GLN   B 73  ? 0.446043 0.382219 0.418362 0.0406197   -0.0093662  0.0853802   85  GLN   B HG2  
2915 H HG3  . GLN   B 73  ? 0.409656 0.375965 0.423535 0.0379526   -0.0227542  0.0685489   85  GLN   B HG3  
2916 H HE21 . GLN   B 73  ? 0.488324 0.389344 0.536929 0.0487931   0.00825376  0.0926075   85  GLN   B HE21 
2917 H HE22 . GLN   B 73  ? 0.478069 0.398147 0.499685 0.0556554   -0.0171354  0.0914473   85  GLN   B HE22 
2918 N N    . VAL   B 74  ? 0.284763 0.32176  0.298142 0.00737534  -0.00804621 0.0318541   86  VAL   B N    
2919 C CA   . VAL   B 74  ? 0.280291 0.334475 0.293341 0.00280312  -0.00227331 0.0240764   86  VAL   B CA   
2920 C C    . VAL   B 74  ? 0.252529 0.31786  0.257302 0.00269214  -0.0137567  0.0213861   86  VAL   B C    
2921 O O    . VAL   B 74  ? 0.270725 0.335314 0.278524 0.00368849  -0.0246183  0.0224764   86  VAL   B O    
2922 C CB   . VAL   B 74  ? 0.27672  0.352141 0.323245 -0.00258495 0.00649245  0.0106687   86  VAL   B CB   
2923 C CG1  . VAL   B 74  ? 0.288619 0.352012 0.349823 -0.00562404 0.0212087   0.011624    86  VAL   B CG1  
2924 C CG2  . VAL   B 74  ? 0.280033 0.369005 0.349499 -0.00312008 0.00031525  0.0021403   86  VAL   B CG2  
2925 H H    . VAL   B 74  ? 0.286985 0.332028 0.31413  0.00776492  -0.01468    0.0282203   86  VAL   B H    
2926 H HA   . VAL   B 74  ? 0.28849  0.332636 0.285713 0.00392511  0.00349858  0.0288331   86  VAL   B HA   
2927 H HB   . VAL   B 74  ? 0.26612  0.355888 0.311162 -0.00353383 0.00712968  0.0053967   86  VAL   B HB   
2928 H HG11 . VAL   B 74  ? 0.303237 0.349505 0.364046 -0.00340052 0.0213484   0.0187711   86  VAL   B HG11 
2929 H HG12 . VAL   B 74  ? 0.297456 0.354387 0.345519 -0.0053295  0.0272842   0.0165758   86  VAL   B HG12 
2930 H HG13 . VAL   B 74  ? 0.278334 0.357342 0.363422 -0.00982295 0.0250652   -0.00020089 86  VAL   B HG13 
2931 H HG21 . VAL   B 74  ? 0.266212 0.369944 0.353391 -0.00603839 0.00482803  -0.00879369 86  VAL   B HG21 
2932 H HG22 . VAL   B 74  ? 0.268662 0.364884 0.330853 -0.00224157 -0.00654954 0.00243131  86  VAL   B HG22 
2933 H HG23 . VAL   B 74  ? 0.285538 0.361245 0.359921 -0.00091107 -0.00067908 0.00678946  86  VAL   B HG23 
2934 N N    . ILE   B 75  ? 0.22743  0.301445 0.223505 0.00199417  -0.0106682  0.0186461   87  ILE   B N    
2935 C CA   . ILE   B 75  ? 0.247754 0.32844  0.237381 0.00127289  -0.0170585  0.0178414   87  ILE   B CA   
2936 C C    . ILE   B 75  ? 0.228411 0.329669 0.241306 -0.00185431 -0.0182053  0.0115324   87  ILE   B C    
2937 O O    . ILE   B 75  ? 0.240843 0.35484  0.273144 -0.00254098 -0.0136421  0.00430537  87  ILE   B O    
2938 C CB   . ILE   B 75  ? 0.257352 0.343122 0.235748 0.00398351  -0.011826   0.0172432   87  ILE   B CB   
2939 C CG1  . ILE   B 75  ? 0.265834 0.374902 0.261797 0.00485714  -0.00491824 0.0090292   87  ILE   B CG1  
2940 C CG2  . ILE   B 75  ? 0.298301 0.363126 0.252732 0.00786716  -0.00969801 0.0221944   87  ILE   B CG2  
2941 C CD1  . ILE   B 75  ? 0.285309 0.404603 0.272637 0.0109915   -0.003524   0.00838536  87  ILE   B CD1  
2942 H H    . ILE   B 75  ? 0.239269 0.314202 0.234569 0.00232221  -0.00349701 0.0177901   87  ILE   B H    
2943 H HA   . ILE   B 75  ? 0.254271 0.322312 0.232453 0.00176235  -0.0235791  0.0215806   87  ILE   B HA   
2944 H HB   . ILE   B 75  ? 0.262012 0.350194 0.237546 0.00352789  -0.0146163  0.0181379   87  ILE   B HB   
2945 H HG12 . ILE   B 75  ? 0.266393 0.372369 0.268686 0.00397727  -0.00012044 0.00782036  87  ILE   B HG12 
2946 H HG13 . ILE   B 75  ? 0.256299 0.377778 0.264883 0.00292275  -0.00614248 0.0043073   87  ILE   B HG13 
2947 H HG21 . ILE   B 75  ? 0.292463 0.359358 0.240984 0.0106845   -0.00776759 0.0218983   87  ILE   B HG21 
2948 H HG22 . ILE   B 75  ? 0.294531 0.357634 0.251245 0.00841099  -0.00360768 0.0223541   87  ILE   B HG22 
2949 H HG23 . ILE   B 75  ? 0.302181 0.353127 0.245099 0.00754909  -0.0158626  0.0249687   87  ILE   B HG23 
2950 H HD11 . ILE   B 75  ? 0.282783 0.398499 0.26008  0.012205    -0.00661569 0.0125516   87  ILE   B HD11 
2951 H HD12 . ILE   B 75  ? 0.272233 0.410744 0.272161 0.0120684   -0.00246297 0.00122284  87  ILE   B HD12 
2952 H HD13 . ILE   B 75  ? 0.286755 0.396963 0.266533 0.0134017   -0.00040961 0.0106587   87  ILE   B HD13 
2953 N N    . LYS   B 76  ? 0.240743 0.343715 0.253301 -0.00429816 -0.0228791  0.0132172   88  LYS   B N    
2954 C CA   . LYS   B 76  ? 0.229383 0.350731 0.263483 -0.00740057 -0.0213355  0.00838991  88  LYS   B CA   
2955 C C    . LYS   B 76  ? 0.221965 0.364209 0.259733 -0.00566997 -0.0125135  0.00148055  88  LYS   B C    
2956 O O    . LYS   B 76  ? 0.227491 0.385274 0.284287 -0.00613127 -0.00938603 -0.00711612 88  LYS   B O    
2957 C CB   . LYS   B 76  ? 0.269003 0.388014 0.3039   -0.0122153  -0.0234644  0.0121697   88  LYS   B CB   
2958 H H    . LYS   B 76  ? 0.245816 0.337831 0.245521 -0.00441406 -0.0258354  0.0169348   88  LYS   B H    
2959 H HA   . LYS   B 76  ? 0.234441 0.356244 0.282263 -0.00708953 -0.0244614  0.00611333  88  LYS   B HA   
2962 N N    . ALA   B 77  ? 0.253267 0.396784 0.272842 -0.00201842 -0.00978442 0.0036002   89  ALA   B N    
2963 C CA   . ALA   B 77  ? 0.253358 0.419443 0.271624 0.00234585  -0.00551184 -0.00397317 89  ALA   B CA   
2964 C C    . ALA   B 77  ? 0.250279 0.429809 0.289637 0.00166114  -0.00474315 -0.0185153  89  ALA   B C    
2965 O O    . ALA   B 77  ? 0.219039 0.420579 0.26514  0.00353994  -0.00277878 -0.0308271  89  ALA   B O    
2966 C CB   . ALA   B 77  ? 0.261068 0.425309 0.259045 0.00912174  -0.00610906 0.00127775  89  ALA   B CB   
2967 H H    . ALA   B 77  ? 0.252168 0.382814 0.259399 -0.00109252 -0.011586   0.00918749  89  ALA   B H    
2968 H HA   . ALA   B 77  ? 0.256798 0.431048 0.274502 0.00201624  -0.00245169 -0.00376341 89  ALA   B HA   
2969 H HB1  . ALA   B 77  ? 0.269522 0.425049 0.255049 0.00995425  -0.00512199 0.009823    89  ALA   B HB1  
2970 H HB2  . ALA   B 77  ? 0.259681 0.414239 0.257826 0.00902744  -0.00735741 0.0022108   89  ALA   B HB2  
2971 H HB3  . ALA   B 77  ? 0.261029 0.442502 0.258989 0.013435    -0.00596745 -0.0052202  89  ALA   B HB3  
2972 N N    . TRP   B 78  ? 0.217193 0.381521 0.265804 -0.00090171 -0.00520072 -0.0175144  90  TRP   B N    
2973 C CA   . TRP   B 78  ? 0.228505 0.399318 0.301676 -0.00334899 -0.00168665 -0.0301442  90  TRP   B CA   
2974 C C    . TRP   B 78  ? 0.229467 0.399666 0.322429 -0.00522946 -0.00119281 -0.0354352  90  TRP   B C    
2975 O O    . TRP   B 78  ? 0.227697 0.411891 0.341483 -0.00626161 0.0020748   -0.0516218  90  TRP   B O    
2976 C CB   . TRP   B 78  ? 0.226384 0.378367 0.302116 -0.00525918 0.00242014  -0.0246838  90  TRP   B CB   
2977 C CG   . TRP   B 78  ? 0.212097 0.376915 0.290484 -0.00442768 0.0059648   -0.0306749  90  TRP   B CG   
2978 C CD1  . TRP   B 78  ? 0.199816 0.376165 0.261982 0.00140584  0.0026513   -0.0289311  90  TRP   B CD1  
2979 C CD2  . TRP   B 78  ? 0.209976 0.378577 0.315413 -0.00944259 0.0142681   -0.0405385  90  TRP   B CD2  
2980 N NE1  . TRP   B 78  ? 0.207578 0.399238 0.286455 0.00166429  0.00627021  -0.0384228  90  TRP   B NE1  
2981 C CE2  . TRP   B 78  ? 0.199317 0.387375 0.306841 -0.0064874  0.014308    -0.0463808  90  TRP   B CE2  
2982 C CE3  . TRP   B 78  ? 0.203704 0.359671 0.334613 -0.0160004  0.0226461   -0.044498   90  TRP   B CE3  
2983 C CZ2  . TRP   B 78  ? 0.216033 0.415713 0.354732 -0.0116662  0.0225084   -0.058096   90  TRP   B CZ2  
2984 C CZ3  . TRP   B 78  ? 0.220387 0.382353 0.379538 -0.0222457  0.032972    -0.0542283  90  TRP   B CZ3  
2985 C CH2  . TRP   B 78  ? 0.22529  0.411055 0.390558 -0.0210154  0.0329158   -0.0620488  90  TRP   B CH2  
2986 H H    . TRP   B 78  ? 0.231794 0.380359 0.270761 -0.0010716  -0.00682599 -0.00900427 90  TRP   B H    
2987 H HA   . TRP   B 78  ? 0.222545 0.411725 0.299481 -0.00194929 -0.00126078 -0.040239   90  TRP   B HA   
2988 H HB2  . TRP   B 78  ? 0.230699 0.366135 0.290838 -0.00410949 0.00035987  -0.0133677  90  TRP   B HB2  
2989 H HB3  . TRP   B 78  ? 0.227497 0.374017 0.319866 -0.00780694 0.00556785  -0.0283124  90  TRP   B HB3  
2990 H HD1  . TRP   B 78  ? 0.205881 0.380484 0.250662 0.00493764  -0.00117555 -0.0225325  90  TRP   B HD1  
2991 H HE1  . TRP   B 78  ? 0.204657 0.406099 0.278701 0.00641911  0.0042702   -0.0390331  90  TRP   B HE1  
2992 H HE3  . TRP   B 78  ? 0.2135   0.35634  0.344208 -0.0160395  0.0219268   -0.0401798  90  TRP   B HE3  
2993 H HZ2  . TRP   B 78  ? 0.211165 0.427032 0.354895 -0.00881539 0.0215992   -0.0629645  90  TRP   B HZ2  
2994 H HZ3  . TRP   B 78  ? 0.22822  0.378551 0.406002 -0.0273427  0.0405342   -0.0561034  90  TRP   B HZ3  
2995 H HH2  . TRP   B 78  ? 0.225066 0.417583 0.415625 -0.0263377  0.0404495   -0.0703745  90  TRP   B HH2  
2996 N N    . ASP   B 79  ? 0.233899 0.389642 0.323528 -0.00494933 -0.00530923 -0.0244259  91  ASP   B N    
2997 C CA   . ASP   B 79  ? 0.211981 0.370166 0.324495 -0.00437188 -0.00578547 -0.0293856  91  ASP   B CA   
2998 C C    . ASP   B 79  ? 0.234038 0.418598 0.352986 -0.00423737 -0.0008722  -0.0415104  91  ASP   B C    
2999 O O    . ASP   B 79  ? 0.244921 0.439258 0.386397 -0.00320192 0.0031842   -0.0552341  91  ASP   B O    
3000 C CB   . ASP   B 79  ? 0.229896 0.373232 0.341293 -0.00267968 -0.0141914  -0.0173761  91  ASP   B CB   
3001 C CG   . ASP   B 79  ? 0.237675 0.354554 0.345798 0.00105804  -0.018567   -0.00770297 91  ASP   B CG   
3002 O OD1  . ASP   B 79  ? 0.22047  0.328925 0.337923 0.00105641  -0.0112462  -0.0108098  91  ASP   B OD1  
3003 O OD2  . ASP   B 79  ? 0.242129 0.347234 0.338975 0.00408602  -0.0290254  0.00221459  91  ASP   B OD2  
3004 H H    . ASP   B 79  ? 0.231366 0.37666  0.306168 -0.00458227 -0.00848424 -0.0150263  91  ASP   B H    
3005 H HA   . ASP   B 79  ? 0.226209 0.37904  0.352631 -0.00428797 -0.00321041 -0.0343118  91  ASP   B HA   
3006 H HB2  . ASP   B 79  ? 0.225526 0.367522 0.321507 -0.0039988  -0.016958   -0.0113725  91  ASP   B HB2  
3007 H HB3  . ASP   B 79  ? 0.223426 0.376087 0.351621 -0.00190188 -0.0144217  -0.0218968  91  ASP   B HB3  
3008 N N    . ILE   B 80  ? 0.217993 0.41168  0.315041 -0.00420067 0.00036573  -0.0363232  92  ILE   B N    
3009 C CA   . ILE   B 80  ? 0.247922 0.464511 0.340902 -0.00242584 0.00763939  -0.0442814  92  ILE   B CA   
3010 C C    . ILE   B 80  ? 0.233942 0.46845  0.325492 0.00096428  0.00898823  -0.0618295  92  ILE   B C    
3011 O O    . ILE   B 80  ? 0.220205 0.471117 0.323524 0.00263613  0.013962    -0.0781047  92  ILE   B O    
3012 C CB   . ILE   B 80  ? 0.280061 0.495075 0.347194 -0.00239841 0.0104186   -0.0298161  92  ILE   B CB   
3013 C CG1  . ILE   B 80  ? 0.287207 0.490573 0.366287 -0.00803997 0.00979337  -0.0191221  92  ILE   B CG1  
3014 C CG2  . ILE   B 80  ? 0.324287 0.560465 0.375151 0.00211083  0.0200733   -0.0345935  92  ILE   B CG2  
3015 C CD1  . ILE   B 80  ? 0.311936 0.501752 0.370112 -0.0104704  0.0107597   -0.0040399  92  ILE   B CD1  
3016 H H    . ILE   B 80  ? 0.229096 0.41293  0.311677 -0.00457977 -0.00245289 -0.0269854  92  ILE   B H    
3017 H HA   . ILE   B 80  ? 0.242957 0.463996 0.352522 -0.00305609 0.0104844   -0.048232   92  ILE   B HA   
3018 H HB   . ILE   B 80  ? 0.282395 0.489289 0.335374 -0.00105363 0.00649095  -0.0243572  92  ILE   B HB   
3019 H HG12 . ILE   B 80  ? 0.290215 0.505145 0.382764 -0.00902911 0.0158983   -0.0234627  92  ILE   B HG12 
3020 H HG13 . ILE   B 80  ? 0.28269  0.475842 0.372551 -0.00890031 0.00276933  -0.0188653  92  ILE   B HG13 
3021 H HG21 . ILE   B 80  ? 0.323392 0.555135 0.362597 0.00120664  0.024806    -0.0233958  92  ILE   B HG21 
3022 H HG22 . ILE   B 80  ? 0.314872 0.56194  0.380037 0.00191623  0.0246805   -0.0443591  92  ILE   B HG22 
3023 H HG23 . ILE   B 80  ? 0.31854  0.561645 0.35613  0.00674859  0.0172988   -0.0393467  92  ILE   B HG23 
3024 H HD11 . ILE   B 80  ? 0.306823 0.485051 0.352747 -0.00877145 0.00501181  -0.00051557 92  ILE   B HD11 
3025 H HD12 . ILE   B 80  ? 0.307867 0.492682 0.37889  -0.0152898  0.00974078  -0.00068133 92  ILE   B HD12 
3026 H HD13 . ILE   B 80  ? 0.317209 0.514381 0.362151 -0.00848313 0.0185412   -0.00167592 92  ILE   B HD13 
3027 N N    . GLY   B 81  ? 0.221072 0.454517 0.300646 0.0023786   0.00414297  -0.0609671  93  GLY   B N    
3028 C CA   . GLY   B 81  ? 0.217792 0.474377 0.293964 0.00663298  0.00186623  -0.0782402  93  GLY   B CA   
3029 C C    . GLY   B 81  ? 0.229467 0.491436 0.338774 0.00253576  0.00246283  -0.100464   93  GLY   B C    
3030 O O    . GLY   B 81  ? 0.220335 0.504538 0.334622 0.00511837  0.00249661  -0.122423   93  GLY   B O    
3031 H H    . GLY   B 81  ? 0.219017 0.43836  0.293478 0.0011305   0.00162414  -0.0504054  93  GLY   B H    
3032 H HA2  . GLY   B 81  ? 0.23334  0.503478 0.294719 0.0110312   0.00384717  -0.0808603  93  GLY   B HA2  
3033 H HA3  . GLY   B 81  ? 0.222666 0.478314 0.289662 0.00847231  -0.00197578 -0.0734554  93  GLY   B HA3  
3034 N N    . VAL   B 82  ? 0.214636 0.454018 0.344827 -0.00341006 0.00370714  -0.0949338  94  VAL   B N    
3035 C CA   . VAL   B 82  ? 0.251817 0.488947 0.416376 -0.00849919 0.00699994  -0.113033   94  VAL   B CA   
3036 C C    . VAL   B 82  ? 0.263547 0.501701 0.445574 -0.00742937 0.0112209   -0.125042   94  VAL   B C    
3037 O O    . VAL   B 82  ? 0.278704 0.526364 0.484758 -0.0093531  0.0134437   -0.149524   94  VAL   B O    
3038 C CB   . VAL   B 82  ? 0.255635 0.464293 0.433364 -0.0139552  0.0109892   -0.100066   94  VAL   B CB   
3039 C CG1  . VAL   B 82  ? 0.274995 0.475547 0.491695 -0.020437   0.018096    -0.116677   94  VAL   B CG1  
3040 C CG2  . VAL   B 82  ? 0.226557 0.438748 0.390558 -0.0142256  0.00934901  -0.092323   94  VAL   B CG2  
3041 H H    . VAL   B 82  ? 0.220888 0.444667 0.342901 -0.00409194 0.00319372  -0.0796202  94  VAL   B H    
3042 H HA   . VAL   B 82  ? 0.248935 0.504155 0.417281 -0.0083943  0.00460122  -0.127818   94  VAL   B HA   
3043 H HB   . VAL   B 82  ? 0.251728 0.443306 0.421843 -0.0124738  0.0110027   -0.0853072  94  VAL   B HB   
3044 H HG11 . VAL   B 82  ? 0.273005 0.49402  0.500646 -0.0218002  0.0165182   -0.136248   94  VAL   B HG11 
3045 H HG12 . VAL   B 82  ? 0.276322 0.465667 0.502016 -0.0191608  0.020185    -0.11615    94  VAL   B HG12 
3046 H HG13 . VAL   B 82  ? 0.275198 0.460839 0.497855 -0.0241684  0.022647    -0.108716   94  VAL   B HG13 
3047 H HG21 . VAL   B 82  ? 0.237395 0.431791 0.408901 -0.0176984  0.0144342   -0.0847195  94  VAL   B HG21 
3048 H HG22 . VAL   B 82  ? 0.230751 0.442575 0.370824 -0.0100756  0.00572077  -0.0804688  94  VAL   B HG22 
3049 H HG23 . VAL   B 82  ? 0.233908 0.4666   0.40641  -0.0144842  0.00724555  -0.107339   94  VAL   B HG23 
3050 N N    . ALA   B 83  ? 0.240942 0.472583 0.413999 -0.00420609 0.0123747   -0.111027   95  ALA   B N    
3051 C CA   . ALA   B 83  ? 0.254154 0.491807 0.445355 -0.00132493 0.0175914   -0.122545   95  ALA   B CA   
3052 C C    . ALA   B 83  ? 0.277931 0.545489 0.462092 0.00205896  0.020987    -0.146819   95  ALA   B C    
3053 O O    . ALA   B 83  ? 0.326266 0.59918  0.532131 0.00401975  0.0266674   -0.165855   95  ALA   B O    
3054 C CB   . ALA   B 83  ? 0.259974 0.493455 0.446015 0.00102359  0.0180554   -0.104688   95  ALA   B CB   
3055 H H    . ALA   B 83  ? 0.242804 0.466869 0.400702 -0.00387473 0.0100847   -0.0950214  95  ALA   B H    
3056 H HA   . ALA   B 83  ? 0.26068  0.485246 0.475409 -0.00256467 0.0191768   -0.127872   95  ALA   B HA   
3057 H HB1  . ALA   B 83  ? 0.253647 0.469121 0.442981 0.00015441  0.0139405   -0.0916023  95  ALA   B HB1  
3058 H HB2  . ALA   B 83  ? 0.255711 0.498525 0.420383 0.00128141  0.0183383   -0.098312   95  ALA   B HB2  
3059 H HB3  . ALA   B 83  ? 0.260748 0.500502 0.46282  0.00345036  0.0224385   -0.113352   95  ALA   B HB3  
3060 N N    . THR   B 84  ? 0.272076 0.558129 0.424405 0.00473653  0.0172417   -0.14663    96  THR   B N    
3061 C CA   . THR   B 84  ? 0.287069 0.602277 0.422034 0.0110435   0.0186735   -0.168088   96  THR   B CA   
3062 C C    . THR   B 84  ? 0.299481 0.628803 0.450626 0.00967134  0.0115218   -0.197703   96  THR   B C    
3063 O O    . THR   B 84  ? 0.337815 0.69331  0.473693 0.0160308   0.00957862  -0.220431   96  THR   B O    
3064 C CB   . THR   B 84  ? 0.283049 0.610462 0.372393 0.0177598   0.0170542   -0.152324   96  THR   B CB   
3065 O OG1  . THR   B 84  ? 0.29837  0.627778 0.380806 0.0181035   0.00549254  -0.150189   96  THR   B OG1  
3066 C CG2  . THR   B 84  ? 0.293691 0.605568 0.371943 0.0162232   0.0245415   -0.123808   96  THR   B CG2  
3067 H H    . THR   B 84  ? 0.267227 0.547274 0.40631  0.00398079  0.0134441   -0.132649   96  THR   B H    
3068 H HA   . THR   B 84  ? 0.292467 0.610917 0.434527 0.0127499   0.0258775   -0.17459    96  THR   B HA   
3069 H HB   . THR   B 84  ? 0.310031 0.655565 0.383349 0.0236088   0.0194802   -0.164647   96  THR   B HB   
3071 H HG21 . THR   B 84  ? 0.300967 0.620097 0.350907 0.0209394   0.0269226   -0.115796   96  THR   B HG21 
3072 H HG22 . THR   B 84  ? 0.275246 0.57087  0.360214 0.0121806   0.0201621   -0.11113    96  THR   B HG22 
3073 H HG23 . THR   B 84  ? 0.28829  0.599306 0.382091 0.0148529   0.0316086   -0.126903   96  THR   B HG23 
3074 N N    . MET   B 85  ? 0.291691 0.605395 0.472534 0.00154399  0.00814046  -0.198636   97  MET   B N    
3075 C CA   . MET   B 85  ? 0.308803 0.638801 0.510689 -0.002171   0.00133658  -0.226589   97  MET   B CA   
3076 C C    . MET   B 85  ? 0.316993 0.638514 0.562726 -0.00850004 0.00735954  -0.25389    97  MET   B C    
3077 O O    . MET   B 85  ? 0.299001 0.591483 0.56624  -0.0114395  0.0164974   -0.243222   97  MET   B O    
3078 C CB   . MET   B 85  ? 0.283685 0.60353  0.497157 -0.00863848 -0.00206564 -0.213172   97  MET   B CB   
3079 C CG   . MET   B 85  ? 0.270961 0.598059 0.444796 -0.00126308 -0.00847588 -0.189499   97  MET   B CG   
3080 S SD   . MET   B 85  ? 0.255457 0.571371 0.445688 -0.0076559  -0.00923867 -0.17606    97  MET   B SD   
3081 C CE   . MET   B 85  ? 0.267426 0.617808 0.496248 -0.0120773  -0.0172498  -0.214685   97  MET   B CE   
3082 H H    . MET   B 85  ? 0.28293  0.576042 0.471879 -0.00189508 0.0105654   -0.182096   97  MET   B H    
3083 H HA   . MET   B 85  ? 0.315796 0.670155 0.496823 0.0041865   -0.00471771 -0.238082   97  MET   B HA   
3084 H HB2  . MET   B 85  ? 0.278637 0.573233 0.507246 -0.0137748  0.00450572  -0.200454   97  MET   B HB2  
3085 H HB3  . MET   B 85  ? 0.290199 0.623022 0.52453  -0.0123566  -0.00577769 -0.233578   97  MET   B HB3  
3086 H HG2  . MET   B 85  ? 0.282341 0.63319  0.43895  0.00554333  -0.015401   -0.200167   97  MET   B HG2  
3087 H HG3  . MET   B 85  ? 0.267979 0.582129 0.423993 0.00109392  -0.0045289  -0.170946   97  MET   B HG3  
3088 H HE1  . MET   B 85  ? 0.260902 0.60975  0.504457 -0.016047   -0.0160137  -0.210356   97  MET   B HE1  
3089 H HE2  . MET   B 85  ? 0.271903 0.617559 0.526415 -0.0185336  -0.0128592  -0.23055    97  MET   B HE2  
3090 H HE3  . MET   B 85  ? 0.274785 0.650513 0.48557  -0.00377213 -0.0271202  -0.224983   97  MET   B HE3  
3091 N N    . LYS   B 86  ? 0.351482 0.698504 0.611446 -0.00956037 0.00077477  -0.290597   98  LYS   B N    
3092 C CA   . LYS   B 86  ? 0.367478 0.705516 0.675762 -0.0177963  0.00583019  -0.321518   98  LYS   B CA   
3093 C C    . LYS   B 86  ? 0.370492 0.699307 0.721528 -0.0315188  0.0056512   -0.327567   98  LYS   B C    
3094 O O    . LYS   B 86  ? 0.342797 0.685588 0.684933 -0.0327217  -0.0017207  -0.317786   98  LYS   B O    
3095 C CB   . LYS   B 86  ? 0.43851  0.811442 0.738039 -0.011406   -0.00146849 -0.362894   98  LYS   B CB   
3096 C CG   . LYS   B 86  ? 0.468482 0.85411  0.723408 0.00242532  0.00261789  -0.359239   98  LYS   B CG   
3097 C CD   . LYS   B 86  ? 0.533985 0.958411 0.764071 0.0117354   -0.00654181 -0.397332   98  LYS   B CD   
3098 C CE   . LYS   B 86  ? 0.56755  0.999585 0.759552 0.0241707   0.00452211  -0.395701   98  LYS   B CE   
3099 N NZ   . LYS   B 86  ? 0.622175 1.08793  0.791057 0.0336422   -0.00245598 -0.437298   98  LYS   B NZ   
3100 H H    . LYS   B 86  ? 0.35295  0.723448 0.592029 -0.00453943 -0.00775879 -0.297156   98  LYS   B H    
3101 H HA   . LYS   B 86  ? 0.374677 0.689771 0.693695 -0.0179124  0.0149793   -0.312418   98  LYS   B HA   
3102 H HB2  . LYS   B 86  ? 0.434789 0.831253 0.725725 -0.010399   -0.0126308  -0.372825   98  LYS   B HB2  
3103 H HB3  . LYS   B 86  ? 0.442968 0.80823  0.776878 -0.0172404  0.00230871  -0.385738   98  LYS   B HB3  
3104 H HG2  . LYS   B 86  ? 0.471873 0.839482 0.742799 0.00181228  0.0129155   -0.357599   98  LYS   B HG2  
3105 H HG3  . LYS   B 86  ? 0.459672 0.845209 0.685131 0.00669731  0.00210612  -0.332432   98  LYS   B HG3  
3106 H HD2  . LYS   B 86  ? 0.531098 0.97492  0.738595 0.015623    -0.0179137  -0.394876   98  LYS   B HD2  
3107 H HD3  . LYS   B 86  ? 0.541377 0.967572 0.803426 0.00622804  -0.00840724 -0.427073   98  LYS   B HD3  
3108 H HE2  . LYS   B 86  ? 0.562408 0.975256 0.777828 0.0214029   0.0158621   -0.393649   98  LYS   B HE2  
3109 H HE3  . LYS   B 86  ? 0.560685 0.994403 0.719673 0.0294032   0.00587366  -0.369111   98  LYS   B HE3  
3110 H HZ1  . LYS   B 86  ? 0.625262 1.08838  0.826775 0.028342    -0.00297309 -0.464002   98  LYS   B HZ1  
3111 H HZ2  . LYS   B 86  ? 0.623923 1.10868  0.77206  0.0374346   -0.0150248  -0.440107   98  LYS   B HZ2  
3112 H HZ3  . LYS   B 86  ? 0.631141 1.10177  0.773574 0.0416451   0.00638734  -0.434481   98  LYS   B HZ3  
3113 N N    . LYS   B 87  ? 0.384374 0.688287 0.784836 -0.0416428  0.015997    -0.34367    99  LYS   B N    
3114 C CA   . LYS   B 87  ? 0.371823 0.665793 0.822046 -0.0571943  0.0207616   -0.354805   99  LYS   B CA   
3115 C C    . LYS   B 87  ? 0.368926 0.710623 0.827989 -0.0597571  0.00471322  -0.389651   99  LYS   B C    
3116 O O    . LYS   B 87  ? 0.378578 0.750312 0.829327 -0.0535758  -0.00642788 -0.424082   99  LYS   B O    
3117 C CB   . LYS   B 87  ? 0.398165 0.658251 0.900069 -0.0663224  0.0350504   -0.372656   99  LYS   B CB   
3118 H H    . LYS   B 87  ? 0.387905 0.679619 0.792817 -0.0386391  0.0216405   -0.34754    99  LYS   B H    
3119 H HA   . LYS   B 87  ? 0.362216 0.640159 0.80731  -0.0595174  0.0255155   -0.32732    99  LYS   B HA   
3122 N N    . GLY   B 88  ? 0.354051 0.704654 0.826469 -0.066685   0.00289392  -0.379665   100 GLY   B N    
3123 C CA   . GLY   B 88  ? 0.3577   0.755753 0.848154 -0.0689336  -0.0136542  -0.41098    100 GLY   B CA   
3124 C C    . GLY   B 88  ? 0.332156 0.766215 0.765557 -0.0511413  -0.0323749  -0.398716   100 GLY   B C    
3125 O O    . GLY   B 88  ? 0.304911 0.779226 0.748809 -0.0491409  -0.048307   -0.417497   100 GLY   B O    
3126 H H    . GLY   B 88  ? 0.345073 0.672105 0.815829 -0.0693309  0.0122195   -0.352454   100 GLY   B H    
3127 H HA2  . GLY   B 88  ? 0.350499 0.742991 0.875425 -0.0799028  -0.00683695 -0.408608   100 GLY   B HA2  
3128 H HA3  . GLY   B 88  ? 0.37126  0.783996 0.881014 -0.0712104  -0.0192647  -0.444886   100 GLY   B HA3  
3129 N N    . GLU   B 89  ? 0.331422 0.750471 0.708152 -0.0379922  -0.030105   -0.367032   101 GLU   B N    
3130 C CA   . GLU   B 89  ? 0.330585 0.775631 0.650149 -0.0205042  -0.0443395  -0.351886   101 GLU   B CA   
3131 C C    . GLU   B 89  ? 0.310317 0.75345  0.628622 -0.0206219  -0.0447     -0.32427    101 GLU   B C    
3132 O O    . GLU   B 89  ? 0.288327 0.698177 0.626795 -0.0310691  -0.0292248  -0.301665   101 GLU   B O    
3133 C CB   . GLU   B 89  ? 0.343631 0.769338 0.611949 -0.00982898 -0.0372021  -0.325881   101 GLU   B CB   
3134 C CG   . GLU   B 89  ? 0.356738 0.804693 0.56397  0.00828641  -0.0483305  -0.310327   101 GLU   B CG   
3135 C CD   . GLU   B 89  ? 0.372343 0.798681 0.53936  0.0147908   -0.0363998  -0.283854   101 GLU   B CD   
3136 O OE1  . GLU   B 89  ? 0.378424 0.798733 0.55296  0.0131334   -0.0279656  -0.298535   101 GLU   B OE1  
3137 O OE2  . GLU   B 89  ? 0.400203 0.816072 0.532806 0.0211435   -0.0346605  -0.250313   101 GLU   B OE2  
3138 H H    . GLU   B 89  ? 0.328185 0.719352 0.703367 -0.0398245  -0.0189929  -0.354051   101 GLU   B H    
3139 H HA   . GLU   B 89  ? 0.347428 0.824722 0.663561 -0.0148676  -0.0580422  -0.377793   101 GLU   B HA   
3140 H HB2  . GLU   B 89  ? 0.354063 0.779148 0.627779 -0.0102034  -0.0342449  -0.343539   101 GLU   B HB2  
3141 H HB3  . GLU   B 89  ? 0.327486 0.724384 0.598736 -0.0143778  -0.0265734  -0.301106   101 GLU   B HB3  
3142 H HG2  . GLU   B 89  ? 0.348479 0.796777 0.551617 0.00967283  -0.0516542  -0.294075   101 GLU   B HG2  
3143 H HG3  . GLU   B 89  ? 0.377686 0.854078 0.575907 0.0150895   -0.0596006  -0.33391    101 GLU   B HG3  
3144 N N    . ILE   B 90  ? 0.313889 0.792505 0.605044 -0.00667097 -0.0624028  -0.326114   102 ILE   B N    
3145 C CA   . ILE   B 90  ? 0.287511 0.764864 0.564944 -0.00090665 -0.0636641  -0.297468   102 ILE   B CA   
3146 C C    . ILE   B 90  ? 0.287425 0.767698 0.497191 0.0190322   -0.0714903  -0.2739     102 ILE   B C    
3147 O O    . ILE   B 90  ? 0.327694 0.837466 0.508456 0.0327228   -0.0861704  -0.290353   102 ILE   B O    
3148 C CB   . ILE   B 90  ? 0.277209 0.794323 0.59591  -0.00181127 -0.0767782  -0.320927   102 ILE   B CB   
3149 C CG1  . ILE   B 90  ? 0.297443 0.808704 0.689572 -0.024752   -0.0642209  -0.34373    102 ILE   B CG1  
3150 C CG2  . ILE   B 90  ? 0.248719 0.766598 0.550256 0.00811102  -0.0783146  -0.29214    102 ILE   B CG2  
3151 C CD1  . ILE   B 90  ? 0.296685 0.853096 0.74527  -0.0295599  -0.0759098  -0.375206   102 ILE   B CD1  
3152 H H    . ILE   B 90  ? 0.327292 0.831611 0.607002 0.00080219  -0.0744246  -0.346475   102 ILE   B H    
3153 H HA   . ILE   B 90  ? 0.273044 0.720606 0.559081 -0.0089587  -0.0497667  -0.277817   102 ILE   B HA   
3154 H HB   . ILE   B 90  ? 0.296076 0.844313 0.605795 0.00714575  -0.0929095  -0.342428   102 ILE   B HB   
3155 H HG12 . ILE   B 90  ? 0.279426 0.75932  0.676662 -0.0321883  -0.0478995  -0.320862   102 ILE   B HG12 
3156 H HG13 . ILE   B 90  ? 0.299911 0.805986 0.70071  -0.030054   -0.0624626  -0.360755   102 ILE   B HG13 
3157 H HG21 . ILE   B 90  ? 0.252665 0.793447 0.58978  0.00531342  -0.0830334  -0.306509   102 ILE   B HG21 
3158 H HG22 . ILE   B 90  ? 0.241852 0.72704  0.538013 0.00242162  -0.0634467  -0.268158   102 ILE   B HG22 
3159 H HG23 . ILE   B 90  ? 0.262948 0.790862 0.523806 0.0235517   -0.0890586  -0.283782   102 ILE   B HG23 
3160 H HD11 . ILE   B 90  ? 0.311555 0.901589 0.752625 -0.0203234  -0.0949807  -0.39845    102 ILE   B HD11 
3161 H HD12 . ILE   B 90  ? 0.298724 0.847166 0.794799 -0.0459917  -0.0648825  -0.389567   102 ILE   B HD12 
3162 H HD13 . ILE   B 90  ? 0.288187 0.848351 0.734618 -0.0251386  -0.0750803  -0.358601   102 ILE   B HD13 
3163 N N    . ALA   B 91  ? 0.27411  0.723419 0.458772 0.0209115   -0.0613752  -0.235979   103 ALA   B N    
3164 C CA   . ALA   B 91  ? 0.292456 0.734808 0.418292 0.0364469   -0.0635558  -0.209556   103 ALA   B CA   
3165 C C    . ALA   B 91  ? 0.279014 0.712899 0.393786 0.0431216   -0.0646137  -0.183729   103 ALA   B C    
3166 O O    . ALA   B 91  ? 0.287367 0.708693 0.434662 0.032927    -0.0570391  -0.179209   103 ALA   B O    
3167 C CB   . ALA   B 91  ? 0.28613  0.693879 0.394755 0.0305125   -0.0478985  -0.191049   103 ALA   B CB   
3168 H H    . ALA   B 91  ? 0.26283  0.693418 0.468058 0.0118808   -0.0520047  -0.226395   103 ALA   B H    
3169 H HA   . ALA   B 91  ? 0.308537 0.775267 0.414425 0.0472682   -0.0744558  -0.221874   103 ALA   B HA   
3170 H HB1  . ALA   B 91  ? 0.293293 0.707389 0.409288 0.0279035   -0.0467889  -0.208351   103 ALA   B HB1  
3171 H HB2  . ALA   B 91  ? 0.271168 0.656131 0.39743  0.0213406   -0.0392917  -0.180029   103 ALA   B HB2  
3172 H HB3  . ALA   B 91  ? 0.293722 0.696039 0.367391 0.0389891   -0.0473589  -0.173427   103 ALA   B HB3  
3173 N N    . HIS   B 92  ? 0.289137 0.727591 0.356645 0.0610024   -0.0720221  -0.166518   104 HIS   B N    
3174 C CA   . HIS   B 92  ? 0.279821 0.699654 0.329467 0.0685046   -0.0698199  -0.13778    104 HIS   B CA   
3175 C C    . HIS   B 92  ? 0.294952 0.676498 0.308102 0.0670631   -0.0564937  -0.108257   104 HIS   B C    
3176 O O    . HIS   B 92  ? 0.306935 0.690339 0.290466 0.0718989   -0.0547967  -0.106666   104 HIS   B O    
3177 C CB   . HIS   B 92  ? 0.303591 0.752254 0.328976 0.0913621   -0.0875471  -0.137843   104 HIS   B CB   
3178 C CG   . HIS   B 92  ? 0.292321 0.780201 0.361198 0.0938357   -0.101926   -0.163934   104 HIS   B CG   
3179 N ND1  . HIS   B 92  ? 0.310459 0.832802 0.367212 0.116137    -0.122455   -0.169746   104 HIS   B ND1  
3180 C CD2  . HIS   B 92  ? 0.26276  0.760219 0.389635 0.0771546   -0.0975733  -0.184093   104 HIS   B CD2  
3181 C CE1  . HIS   B 92  ? 0.303732 0.860249 0.41529  0.111949    -0.131576   -0.195985   104 HIS   B CE1  
3182 N NE2  . HIS   B 92  ? 0.260676 0.801391 0.415916 0.0870396   -0.114765   -0.20474    104 HIS   B NE2  
3183 H H    . HIS   B 92  ? 0.307381 0.759488 0.352007 0.0693357   -0.0778352  -0.172903   104 HIS   B H    
3184 H HA   . HIS   B 92  ? 0.267125 0.67961  0.344801 0.0601745   -0.0649336  -0.1376     104 HIS   B HA   
3185 H HB2  . HIS   B 92  ? 0.322309 0.782056 0.320965 0.0996616   -0.0929012  -0.142014   104 HIS   B HB2  
3186 H HB3  . HIS   B 92  ? 0.305867 0.735949 0.311473 0.097887    -0.0841459  -0.115609   104 HIS   B HB3  
3188 H HD2  . HIS   B 92  ? 0.24811  0.726375 0.393897 0.0618309   -0.0848273  -0.184061   104 HIS   B HD2  
3189 H HE1  . HIS   B 92  ? 0.310771 0.898211 0.429896 0.125058    -0.14737    -0.20658    104 HIS   B HE1  
3191 N N    . LEU   B 93  ? 0.254416 0.603687 0.271925 0.0600672   -0.0466185  -0.0876293  105 LEU   B N    
3192 C CA   . LEU   B 93  ? 0.272494 0.586971 0.261858 0.058283    -0.036354   -0.0613285  105 LEU   B CA   
3193 C C    . LEU   B 93  ? 0.29439  0.592633 0.265188 0.0684537   -0.0373122  -0.0407799  105 LEU   B C    
3194 O O    . LEU   B 93  ? 0.290782 0.588985 0.281567 0.0682245   -0.0384859  -0.0430108  105 LEU   B O    
3195 C CB   . LEU   B 93  ? 0.249872 0.536435 0.258683 0.0413691   -0.0253526  -0.0565273  105 LEU   B CB   
3196 C CG   . LEU   B 93  ? 0.237515 0.530937 0.271172 0.0307796   -0.021986   -0.0744647  105 LEU   B CG   
3197 C CD1  . LEU   B 93  ? 0.233115 0.496631 0.28127  0.0187983   -0.013486   -0.0649755  105 LEU   B CD1  
3198 C CD2  . LEU   B 93  ? 0.258136 0.564781 0.271439 0.0358389   -0.0212528  -0.0791686  105 LEU   B CD2  
3199 H H    . LEU   B 93  ? 0.252988 0.602814 0.293301 0.0559547   -0.0461196  -0.0915059  105 LEU   B H    
3200 H HA   . LEU   B 93  ? 0.285004 0.603599 0.253498 0.0627347   -0.0357628  -0.0593524  105 LEU   B HA   
3201 H HB2  . LEU   B 93  ? 0.241376 0.520467 0.263691 0.0383447   -0.0243123  -0.0550418  105 LEU   B HB2  
3202 H HB3  . LEU   B 93  ? 0.253934 0.521701 0.24548  0.0408918   -0.0207007  -0.0413058  105 LEU   B HB3  
3203 H HG   . LEU   B 93  ? 0.237745 0.547631 0.292465 0.0294655   -0.0257547  -0.0906872  105 LEU   B HG   
3204 H HD11 . LEU   B 93  ? 0.225325 0.479584 0.281607 0.0165063   -0.0125291  -0.0612302  105 LEU   B HD11 
3205 H HD12 . LEU   B 93  ? 0.226855 0.49372  0.29257  0.0136563   -0.0114173  -0.0761343  105 LEU   B HD12 
3206 H HD13 . LEU   B 93  ? 0.233176 0.483255 0.265248 0.0191826   -0.0109415  -0.0517688  105 LEU   B HD13 
3207 H HD21 . LEU   B 93  ? 0.268419 0.596921 0.273345 0.0440773   -0.0282421  -0.0892409  105 LEU   B HD21 
3208 H HD22 . LEU   B 93  ? 0.263137 0.556592 0.255704 0.0380256   -0.0169548  -0.0628064  105 LEU   B HD22 
3209 H HD23 . LEU   B 93  ? 0.251018 0.557521 0.280519 0.0291908   -0.0174698  -0.0888921  105 LEU   B HD23 
3210 N N    . LEU   B 94  ? 0.297542 0.578097 0.232473 0.0759172   -0.0334338  -0.0203457  106 LEU   B N    
3211 C CA   . LEU   B 94  ? 0.323218 0.577452 0.239792 0.0836441   -0.0309303  0.00126996  106 LEU   B CA   
3212 C C    . LEU   B 94  ? 0.34005  0.558572 0.248645 0.0711505   -0.0184062  0.0173346   106 LEU   B C    
3213 O O    . LEU   B 94  ? 0.344346 0.562425 0.242564 0.066881    -0.0118744  0.0205592   106 LEU   B O    
3214 C CB   . LEU   B 94  ? 0.363007 0.626786 0.24569  0.1055      -0.0376008  0.0116956   106 LEU   B CB   
3215 C CG   . LEU   B 94  ? 0.392505 0.628557 0.258615 0.117458    -0.0358941  0.0331444   106 LEU   B CG   
3216 C CD1  . LEU   B 94  ? 0.382911 0.627228 0.275887 0.121909    -0.042527   0.0240255   106 LEU   B CD1  
3217 C CD2  . LEU   B 94  ? 0.444199 0.684134 0.270815 0.140233    -0.0405127  0.0480236   106 LEU   B CD2  
3218 H H    . LEU   B 94  ? 0.313487 0.597525 0.235766 0.075962    -0.0308925  -0.0202418  106 LEU   B H    
3219 H HA   . LEU   B 94  ? 0.314323 0.567729 0.247255 0.0830456   -0.0328038  -0.00227215 106 LEU   B HA   
3220 H HB2  . LEU   B 94  ? 0.36477  0.656981 0.254941 0.113278    -0.048091   -0.00221251 106 LEU   B HB2  
3221 H HB3  . LEU   B 94  ? 0.378554 0.639541 0.241712 0.105663    -0.0326881  0.0175951   106 LEU   B HB3  
3222 H HG   . LEU   B 94  ? 0.392106 0.599944 0.255055 0.107942    -0.0260381  0.0440377   106 LEU   B HG   
3223 H HD11 . LEU   B 94  ? 0.359714 0.595459 0.271739 0.10815     -0.0370991  0.0185232   106 LEU   B HD11 
3224 H HD12 . LEU   B 94  ? 0.398141 0.625746 0.279275 0.131969    -0.0417426  0.0367352   106 LEU   B HD12 
3225 H HD13 . LEU   B 94  ? 0.379444 0.654454 0.283141 0.128917    -0.0523623  0.0105588   106 LEU   B HD13 
3226 H HD21 . LEU   B 94  ? 0.454555 0.685899 0.262678 0.136803    -0.0325638  0.0560084   106 LEU   B HD21 
3227 H HD22 . LEU   B 94  ? 0.445203 0.71556  0.273488 0.150431    -0.0524048  0.0357641   106 LEU   B HD22 
3228 H HD23 . LEU   B 94  ? 0.45708  0.677386 0.274913 0.148898    -0.0392122  0.0618141   106 LEU   B HD23 
3229 N N    . ILE   B 95  ? 0.320383 0.511786 0.236013 0.0654994   -0.0151664  0.0248564   107 ILE   B N    
3230 C CA   . ILE   B 95  ? 0.325908 0.489885 0.245609 0.050847    -0.00772967 0.031675    107 ILE   B CA   
3231 C C    . ILE   B 95  ? 0.338058 0.467851 0.243133 0.0530015   -0.003868   0.0474865   107 ILE   B C    
3232 O O    . ILE   B 95  ? 0.327842 0.447723 0.233649 0.0582916   -0.00623779 0.0471379   107 ILE   B O    
3233 C CB   . ILE   B 95  ? 0.294927 0.458725 0.239653 0.0393364   -0.00897547 0.0197714   107 ILE   B CB   
3234 C CG1  . ILE   B 95  ? 0.279494 0.472027 0.243998 0.0361414   -0.0112561  0.00281658  107 ILE   B CG1  
3235 C CG2  . ILE   B 95  ? 0.298345 0.436984 0.2458   0.0271335   -0.0057072  0.0257506   107 ILE   B CG2  
3236 C CD1  . ILE   B 95  ? 0.243942 0.436581 0.233096 0.028725    -0.0107509  -0.00739737 107 ILE   B CD1  
3237 H H    . ILE   B 95  ? 0.326934 0.518549 0.245122 0.0717067   -0.0183125  0.0244384   107 ILE   B H    
3238 H HA   . ILE   B 95  ? 0.324028 0.491358 0.240837 0.0471127   -0.00401697 0.0330179   107 ILE   B HA   
3239 H HB   . ILE   B 95  ? 0.29648  0.45679  0.24314  0.0428415   -0.0102777  0.0189229   107 ILE   B HB   
3240 H HG12 . ILE   B 95  ? 0.273946 0.467204 0.239625 0.0312317   -0.00873976 0.00243062  107 ILE   B HG12 
3241 H HG13 . ILE   B 95  ? 0.281099 0.492329 0.241701 0.044394    -0.0149313  -0.00192347 107 ILE   B HG13 
3242 H HG21 . ILE   B 95  ? 0.284142 0.424253 0.244656 0.0214562   -0.00686707 0.0192882   107 ILE   B HG21 
3243 H HG22 . ILE   B 95  ? 0.300455 0.440633 0.246021 0.0244927   -0.00278855 0.0288942   107 ILE   B HG22 
3244 H HG23 . ILE   B 95  ? 0.305422 0.425271 0.244314 0.0281575   -0.00537714 0.0322458   107 ILE   B HG23 
3245 H HD11 . ILE   B 95  ? 0.250822 0.446757 0.241951 0.0333998   -0.0115596  -0.00861705 107 ILE   B HD11 
3246 H HD12 . ILE   B 95  ? 0.242622 0.450622 0.246376 0.0257859   -0.0112559  -0.0184485  107 ILE   B HD12 
3247 H HD13 . ILE   B 95  ? 0.247727 0.421425 0.236617 0.0226973   -0.00848458 -0.00188209 107 ILE   B HD13 
3248 N N    . LYS   B 96  ? 0.355795 0.466863 0.252071 0.0470673   0.00393069  0.0593344   108 LYS   B N    
3249 C CA   . LYS   B 96  ? 0.36021  0.435248 0.249556 0.0448445   0.00857637  0.0710727   108 LYS   B CA   
3250 C C    . LYS   B 96  ? 0.336245 0.396571 0.241337 0.0324036   0.00465019  0.0619647   108 LYS   B C    
3251 O O    . LYS   B 96  ? 0.317415 0.391734 0.238216 0.0234766   0.00114646  0.0518929   108 LYS   B O    
3252 C CB   . LYS   B 96  ? 0.392679 0.45329  0.274989 0.039387    0.0205222   0.0850412   108 LYS   B CB   
3253 C CG   . LYS   B 96  ? 0.445374 0.51104  0.299731 0.055632    0.02623     0.0996829   108 LYS   B CG   
3254 C CD   . LYS   B 96  ? 0.503579 0.552381 0.349025 0.0495445   0.043809    0.116597    108 LYS   B CD   
3255 C CE   . LYS   B 96  ? 0.54263  0.594646 0.351398 0.0678337   0.0510053   0.134051    108 LYS   B CE   
3256 N NZ   . LYS   B 96  ? 0.591712 0.627431 0.395063 0.0586495   0.0728858   0.150277    108 LYS   B NZ   
3257 H H    . LYS   B 96  ? 0.35166  0.472705 0.248345 0.0438586   0.0073191   0.0589888   108 LYS   B H    
3258 H HA   . LYS   B 96  ? 0.376262 0.445521 0.254993 0.0561353   0.00699689  0.0755735   108 LYS   B HA   
3259 H HB2  . LYS   B 96  ? 0.382726 0.454735 0.277313 0.0300262   0.0224463   0.0797063   108 LYS   B HB2  
3260 H HB3  . LYS   B 96  ? 0.407819 0.443504 0.292241 0.0344457   0.0236549   0.0899117   108 LYS   B HB3  
3261 H HG2  . LYS   B 96  ? 0.460359 0.514455 0.304029 0.0664978   0.0235222   0.105563    108 LYS   B HG2  
3262 H HG3  . LYS   B 96  ? 0.435833 0.528009 0.28782  0.0608198   0.021407    0.0921211   108 LYS   B HG3  
3263 H HD2  . LYS   B 96  ? 0.481221 0.542641 0.341237 0.0385966   0.0469687   0.109556    108 LYS   B HD2  
3264 H HD3  . LYS   B 96  ? 0.508914 0.530577 0.359847 0.0436965   0.0485903   0.122961    108 LYS   B HD3  
3265 H HE2  . LYS   B 96  ? 0.566148 0.602972 0.361269 0.0797253   0.0483658   0.143146    108 LYS   B HE2  
3266 H HE3  . LYS   B 96  ? 0.536992 0.617    0.339229 0.0745931   0.0443831   0.125409    108 LYS   B HE3  
3267 H HZ1  . LYS   B 96  ? 0.595922 0.605356 0.408269 0.0515376   0.0791055   0.15726     108 LYS   B HZ1  
3268 H HZ2  . LYS   B 96  ? 0.566827 0.618106 0.385335 0.0482485   0.0755951   0.141111    108 LYS   B HZ2  
3269 H HZ3  . LYS   B 96  ? 0.614057 0.650272 0.390653 0.0706877   0.0783165   0.162354    108 LYS   B HZ3  
3270 N N    . PRO   B 97  ? 0.370154 0.399877 0.269167 0.0326796   0.00507447  0.0653512   109 PRO   B N    
3271 C CA   . PRO   B 97  ? 0.366897 0.383224 0.272019 0.0247261   -0.00054708 0.0552306   109 PRO   B CA   
3272 C C    . PRO   B 97  ? 0.382005 0.399611 0.303359 0.00927954  -0.00419913 0.049526    109 PRO   B C    
3273 O O    . PRO   B 97  ? 0.34583  0.365242 0.270962 0.00555325  -0.0115191  0.040754    109 PRO   B O    
3274 C CB   . PRO   B 97  ? 0.41314  0.395366 0.306924 0.0287002   0.00169707  0.0586636   109 PRO   B CB   
3275 C CG   . PRO   B 97  ? 0.438527 0.41155  0.322587 0.0383525   0.00981604  0.0740166   109 PRO   B CG   
3276 C CD   . PRO   B 97  ? 0.417991 0.423502 0.301045 0.0431035   0.0108831   0.0786348   109 PRO   B CD   
3277 H HA   . PRO   B 97  ? 0.362026 0.389768 0.267445 0.0287765   -0.00324676 0.0495452   109 PRO   B HA   
3278 H HB2  . PRO   B 97  ? 0.416311 0.383698 0.314984 0.0192621   6.593e-05   0.0552492   109 PRO   B HB2  
3279 H HB3  . PRO   B 97  ? 0.409704 0.389999 0.29763  0.0352386   -4.378e-05  0.0540788   109 PRO   B HB3  
3280 H HG2  . PRO   B 97  ? 0.452505 0.406695 0.33942  0.0311303   0.0143853   0.0786973   109 PRO   B HG2  
3281 H HG3  . PRO   B 97  ? 0.448513 0.41289  0.323958 0.0494387   0.0100724   0.0758175   109 PRO   B HG3  
3282 H HD2  . PRO   B 97  ? 0.428868 0.429131 0.309326 0.0405005   0.0173189   0.0876355   109 PRO   B HD2  
3283 H HD3  . PRO   B 97  ? 0.418206 0.433784 0.293458 0.0558787   0.00901375  0.0803417   109 PRO   B HD3  
3284 N N    . GLU   B 98  ? 0.394436 0.411918 0.326092 0.00136806  0.00171563  0.0553272   110 GLU   B N    
3285 C CA   . GLU   B 98  ? 0.375416 0.399557 0.330395 -0.0124253  -0.00159602 0.0489006   110 GLU   B CA   
3286 C C    . GLU   B 98  ? 0.317198 0.368434 0.283169 -0.0122931  -0.00743523 0.0409378   110 GLU   B C    
3287 O O    . GLU   B 98  ? 0.296162 0.350093 0.27829  -0.0192208  -0.0157246  0.0335888   110 GLU   B O    
3288 C CB   . GLU   B 98  ? 0.409245 0.43424  0.376516 -0.01994    0.0113402   0.0576389   110 GLU   B CB   
3289 C CG   . GLU   B 98  ? 0.500301 0.492373 0.463941 -0.023452   0.0195724   0.0662883   110 GLU   B CG   
3290 C CD   . GLU   B 98  ? 0.578411 0.551432 0.513074 -0.00846065 0.0262737   0.0795683   110 GLU   B CD   
3291 O OE1  . GLU   B 98  ? 0.525347 0.516533 0.442217 0.00489017  0.028723    0.086523    110 GLU   B OE1  
3292 O OE2  . GLU   B 98  ? 0.633525 0.573663 0.564962 -0.00915212 0.027723    0.081277    110 GLU   B OE2  
3293 H H    . GLU   B 98  ? 0.403834 0.417874 0.328501 0.00542082  0.00864824  0.0639303   110 GLU   B H    
3294 H HA   . GLU   B 98  ? 0.382489 0.391952 0.339836 -0.0168536  -0.00782887 0.0435971   110 GLU   B HA   
3295 H HB2  . GLU   B 98  ? 0.414311 0.452275 0.373095 -0.0137553  0.0175575   0.0631344   110 GLU   B HB2  
3296 H HB3  . GLU   B 98  ? 0.407458 0.44224  0.395109 -0.0285772  0.00939778  0.0519808   110 GLU   B HB3  
3297 H HG2  . GLU   B 98  ? 0.505554 0.498674 0.48267  -0.031297   0.0289577   0.0708846   110 GLU   B HG2  
3298 H HG3  . GLU   B 98  ? 0.501158 0.480598 0.471559 -0.0287388  0.0117698   0.0580124   110 GLU   B HG3  
3299 N N    . TYR   B 99  ? 0.287774 0.358262 0.24692  -0.00378158 -0.00430308 0.0412182   111 TYR   B N    
3300 C CA   . TYR   B 99  ? 0.264714 0.356771 0.237049 -0.00395862 -0.00785219 0.0325101   111 TYR   B CA   
3301 C C    . TYR   B 99  ? 0.280598 0.370828 0.245415 0.00192603  -0.0121375  0.0281672   111 TYR   B C    
3302 O O    . TYR   B 99  ? 0.284775 0.390382 0.260927 0.0025101   -0.0123353  0.0215105   111 TYR   B O    
3303 C CB   . TYR   B 99  ? 0.250203 0.366982 0.224901 -0.00050651 -0.00036123 0.0315772   111 TYR   B CB   
3304 C CG   . TYR   B 99  ? 0.262006 0.38279  0.245989 -0.00709501 0.00860102  0.0360832   111 TYR   B CG   
3305 C CD1  . TYR   B 99  ? 0.287511 0.394626 0.257957 -0.00690129 0.0182308   0.0488294   111 TYR   B CD1  
3306 C CD2  . TYR   B 99  ? 0.261808 0.398757 0.27096  -0.013307   0.00963303  0.0281881   111 TYR   B CD2  
3307 C CE1  . TYR   B 99  ? 0.304343 0.41423  0.286282 -0.0146745  0.0309798   0.054118    111 TYR   B CE1  
3308 C CE2  . TYR   B 99  ? 0.272434 0.416425 0.295216 -0.0198383  0.0209139   0.0312216   111 TYR   B CE2  
3309 C CZ   . TYR   B 99  ? 0.281649 0.412195 0.291364 -0.0217024  0.0326768   0.0444197   111 TYR   B CZ   
3310 O OH   . TYR   B 99  ? 0.309905 0.447284 0.33702  -0.0299273  0.0476247   0.0479351   111 TYR   B OH   
3311 H H    . TYR   B 99  ? 0.300084 0.36997  0.247188 0.00267155  -0.00016491 0.0463367   111 TYR   B H    
3312 H HA   . TYR   B 99  ? 0.263381 0.355187 0.249405 -0.0100371  -0.01154    0.0293803   111 TYR   B HA   
3313 H HB2  . TYR   B 99  ? 0.260634 0.378714 0.220839 0.00670699  0.00145844  0.0349496   111 TYR   B HB2  
3314 H HB3  . TYR   B 99  ? 0.241266 0.370784 0.226    -0.00039156 -0.00254529 0.0239087   111 TYR   B HB3  
3315 H HD1  . TYR   B 99  ? 0.298884 0.393474 0.253363 -0.00129212 0.0174944   0.0545514   111 TYR   B HD1  
3316 H HD2  . TYR   B 99  ? 0.246753 0.389908 0.265328 -0.0126582  0.00386844  0.0208272   111 TYR   B HD2  
3317 H HE1  . TYR   B 99  ? 0.321695 0.418991 0.29433  -0.0149453  0.0396298   0.0644777   111 TYR   B HE1  
3318 H HE2  . TYR   B 99  ? 0.260172 0.416792 0.30296  -0.0230954  0.0217487   0.024796    111 TYR   B HE2  
3320 N N    . ALA   B 100 ? 0.263768 0.334169 0.211754 0.00593949  -0.0132381  0.0312335   112 ALA   B N    
3321 C CA   . ALA   B 100 ? 0.269627 0.337664 0.210849 0.0111979   -0.0130592  0.027973    112 ALA   B CA   
3322 C C    . ALA   B 100 ? 0.273163 0.314967 0.199239 0.0099589   -0.017578   0.0278469   112 ALA   B C    
3323 O O    . ALA   B 100 ? 0.288139 0.325759 0.217468 0.00513852  -0.0242415  0.02592     112 ALA   B O    
3324 C CB   . ALA   B 100 ? 0.274871 0.351896 0.210462 0.0211104   -0.00835216 0.0289066   112 ALA   B CB   
3325 H H    . ALA   B 100 ? 0.284582 0.342069 0.226398 0.0051779   -0.0126572  0.035056    112 ALA   B H    
3326 H HA   . ALA   B 100 ? 0.256205 0.335031 0.208051 0.00932805  -0.0130716  0.0242407   112 ALA   B HA   
3327 H HB1  . ALA   B 100 ? 0.263976 0.3606   0.2088   0.0223824   -0.00760236 0.0259599   112 ALA   B HB1  
3328 H HB2  . ALA   B 100 ? 0.285447 0.353161 0.212229 0.02402     -0.0077177  0.0339951   112 ALA   B HB2  
3329 H HB3  . ALA   B 100 ? 0.276487 0.349442 0.208805 0.0240907   -0.00657302 0.0268963   112 ALA   B HB3  
3330 N N    . TYR   B 101 ? 0.297423 0.321578 0.206619 0.0153954   -0.0154367  0.0289623   113 TYR   B N    
3331 C CA   . TYR   B 101 ? 0.326977 0.327035 0.21688  0.0158923   -0.0194561  0.0253275   113 TYR   B CA   
3332 C C    . TYR   B 101 ? 0.37718  0.354959 0.261144 0.0126866   -0.0241173  0.0232535   113 TYR   B C    
3333 O O    . TYR   B 101 ? 0.381911 0.338962 0.248495 0.0132307   -0.0294822  0.0164413   113 TYR   B O    
3334 C CB   . TYR   B 101 ? 0.358996 0.355195 0.234678 0.0250229   -0.0106089  0.0241657   113 TYR   B CB   
3335 C CG   . TYR   B 101 ? 0.345344 0.358492 0.230839 0.0244676   -0.00491043 0.0249164   113 TYR   B CG   
3336 C CD1  . TYR   B 101 ? 0.344946 0.348597 0.220147 0.0220561   -0.00723459 0.0261288   113 TYR   B CD1  
3337 C CD2  . TYR   B 101 ? 0.31227  0.350525 0.219029 0.0264927   0.00185015  0.024107    113 TYR   B CD2  
3338 C CE1  . TYR   B 101 ? 0.316561 0.330374 0.203786 0.0206734   0.00039222  0.0286465   113 TYR   B CE1  
3339 C CE2  . TYR   B 101 ? 0.283456 0.335655 0.206176 0.0234606   0.00804393  0.0224109   113 TYR   B CE2  
3340 C CZ   . TYR   B 101 ? 0.294986 0.332285 0.208344 0.0201119   0.00934034  0.0257699   113 TYR   B CZ   
3341 O OH   . TYR   B 101 ? 0.251683 0.297996 0.183638 0.0165472   0.0178449   0.0255532   113 TYR   B OH   
3342 H H    . TYR   B 101 ? 0.29972  0.326546 0.208045 0.0200389   -0.0116749  0.0314741   113 TYR   B H    
3343 H HA   . TYR   B 101 ? 0.333655 0.334577 0.224625 0.0123536   -0.0247172  0.0239116   113 TYR   B HA   
3344 H HB2  . TYR   B 101 ? 0.353395 0.353256 0.232035 0.0301627   -0.00606196 0.0253853   113 TYR   B HB2  
3345 H HB3  . TYR   B 101 ? 0.373387 0.352051 0.231772 0.0264505   -0.0123548  0.0212104   113 TYR   B HB3  
3346 H HD1  . TYR   B 101 ? 0.356873 0.34617  0.217085 0.021736    -0.0144601  0.0252241   113 TYR   B HD1  
3347 H HD2  . TYR   B 101 ? 0.307371 0.352863 0.218336 0.0303063   0.00191596  0.024173    113 TYR   B HD2  
3348 H HE1  . TYR   B 101 ? 0.332349 0.336291 0.209909 0.0206387   -0.00039777 0.0318201   113 TYR   B HE1  
3349 H HE2  . TYR   B 101 ? 0.276225 0.346941 0.215985 0.0242527   0.0114151   0.0189518   113 TYR   B HE2  
3351 N N    . GLY   B 102 ? 0.365126 0.345774 0.262786 0.00913373  -0.0211521  0.0284836   114 GLY   B N    
3352 C CA   . GLY   B 102 ? 0.398369 0.358257 0.300867 0.00145277  -0.023621   0.0267653   114 GLY   B CA   
3353 C C    . GLY   B 102 ? 0.431589 0.361406 0.31683  0.00743862  -0.0212658  0.023269    114 GLY   B C    
3354 O O    . GLY   B 102 ? 0.429502 0.357176 0.300938 0.0196691   -0.0150301  0.0253852   114 GLY   B O    
3355 H H    . GLY   B 102 ? 0.357116 0.352461 0.26128  0.0114285   -0.0166751  0.0330923   114 GLY   B H    
3356 H HA2  . GLY   B 102 ? 0.392377 0.357493 0.305526 -0.00114953 -0.0183008  0.0332771   114 GLY   B HA2  
3357 H HA3  . GLY   B 102 ? 0.396443 0.356687 0.305197 -0.00534058 -0.0318019  0.0206356   114 GLY   B HA3  
3358 N N    . SER   B 103 ? 0.44499  0.352289 0.335465 -0.00147194 -0.0262442  0.015563    115 SER   B N    
3359 C CA   . SER   B 103 ? 0.479899 0.354374 0.356957 0.00325051  -0.0236996  0.00926202  115 SER   B CA   
3360 C C    . SER   B 103 ? 0.474924 0.34192  0.324997 0.0112511   -0.0295678  -0.00353062 115 SER   B C    
3361 O O    . SER   B 103 ? 0.4794   0.325699 0.314038 0.0211184   -0.023205   -0.00738359 115 SER   B O    
3362 C CB   . SER   B 103 ? 0.515699 0.366435 0.411205 -0.0103764  -0.0259429  0.00218817  115 SER   B CB   
3363 O OG   . SER   B 103 ? 0.546509 0.406183 0.452637 -0.0219445  -0.041752   -0.0125897  115 SER   B OG   
3364 H H    . SER   B 103 ? 0.443801 0.35661  0.349026 -0.0107685  -0.0312803  0.0127552   115 SER   B H    
3365 H HA   . SER   B 103 ? 0.47967  0.351136 0.353265 0.0115972   -0.0146498  0.018263    115 SER   B HA   
3366 H HB2  . SER   B 103 ? 0.545333 0.372117 0.432049 -0.00658366 -0.0237274  -0.00311295 115 SER   B HB2  
3367 H HB3  . SER   B 103 ? 0.516556 0.369441 0.426742 -0.0144455  -0.0181431  0.0127616   115 SER   B HB3  
3369 N N    . ALA   B 104 ? 0.469687 0.352054 0.312428 0.00876683  -0.0400649  -0.00893699 116 ALA   B N    
3370 C CA   . ALA   B 104 ? 0.495169 0.36783  0.305275 0.0169181   -0.0440894  -0.0191243  116 ALA   B CA   
3371 C C    . ALA   B 104 ? 0.479628 0.362217 0.276589 0.0294468   -0.0292828  -0.0104648  116 ALA   B C    
3372 O O    . ALA   B 104 ? 0.492206 0.361398 0.263336 0.0390502   -0.0231198  -0.0169769  116 ALA   B O    
3373 C CB   . ALA   B 104 ? 0.504548 0.387691 0.30881  0.0124355   -0.060345   -0.0245145  116 ALA   B CB   
3374 H H    . ALA   B 104 ? 0.452156 0.350265 0.308922 0.00289372  -0.0440416  -0.00556698 116 ALA   B H    
3375 H HA   . ALA   B 104 ? 0.521501 0.373172 0.322534 0.0179332   -0.0453155  -0.0289724  116 ALA   B HA   
3376 H HB1  . ALA   B 104 ? 0.509693 0.389237 0.32664  0.0045068   -0.0706056  -0.0323448  116 ALA   B HB1  
3377 H HB2  . ALA   B 104 ? 0.477857 0.379289 0.293029 0.0114768   -0.0586691  -0.0153833  116 ALA   B HB2  
3378 H HB3  . ALA   B 104 ? 0.522227 0.397437 0.299556 0.0191586   -0.0621959  -0.0296001  116 ALA   B HB3  
3379 N N    . GLY   B 105 ? 0.444255 0.351479 0.262184 0.02909     -0.0226597  0.00224377  117 GLY   B N    
3380 C CA   . GLY   B 105 ? 0.429722 0.353912 0.246498 0.0379983   -0.010321   0.00817937  117 GLY   B CA   
3381 C C    . GLY   B 105 ? 0.438888 0.366885 0.238512 0.0386266   -0.00959817 0.00756344  117 GLY   B C    
3382 O O    . GLY   B 105 ? 0.449914 0.374766 0.242293 0.0330788   -0.0214735  0.00604468  117 GLY   B O    
3383 H H    . GLY   B 105 ? 0.430981 0.345776 0.26593  0.0227406   -0.0257357  0.00605436  117 GLY   B H    
3384 H HA2  . GLY   B 105 ? 0.408649 0.350366 0.24351  0.0365549   -0.00847916 0.0146196   117 GLY   B HA2  
3385 H HA3  . GLY   B 105 ? 0.443669 0.359383 0.254044 0.0457022   -0.00334923 0.0060987   117 GLY   B HA3  
3386 N N    . SER   B 106 ? 0.43151  0.366879 0.226937 0.0462885   0.005415    0.00971248  118 SER   B N    
3387 C CA   . SER   B 106 ? 0.442088 0.375056 0.217413 0.0481741   0.0125983   0.0120534   118 SER   B CA   
3388 C C    . SER   B 106 ? 0.433181 0.361356 0.195606 0.0583      0.0313891   0.00880177  118 SER   B C    
3389 O O    . SER   B 106 ? 0.417728 0.364034 0.198186 0.059721    0.0468998   0.0129031   118 SER   B O    
3390 C CB   . SER   B 106 ? 0.398997 0.353799 0.198581 0.0421344   0.0154267   0.0206248   118 SER   B CB   
3391 O OG   . SER   B 106 ? 0.441515 0.387373 0.220587 0.0431636   0.0216038   0.0264938   118 SER   B OG   
3392 H H    . SER   B 106 ? 0.425678 0.367878 0.232095 0.0507824   0.0121809   0.0103022   118 SER   B H    
3393 H HA   . SER   B 106 ? 0.454357 0.372942 0.208371 0.047459    0.00351825  0.00924355  118 SER   B HA   
3394 H HB2  . SER   B 106 ? 0.392394 0.352448 0.204143 0.0367229   0.00459212  0.0213402   118 SER   B HB2  
3395 H HB3  . SER   B 106 ? 0.391307 0.361523 0.210674 0.0432268   0.0241958   0.0211856   118 SER   B HB3  
3397 N N    . LEU   B 107 ? 0.460681 0.365568 0.19668  0.0648289   0.0301091   -0.00091259 119 LEU   B N    
3398 C CA   . LEU   B 107 ? 0.495523 0.395249 0.22274  0.0763208   0.0481362   -0.00688133 119 LEU   B CA   
3399 C C    . LEU   B 107 ? 0.517503 0.414207 0.217794 0.0800576   0.0656425   -0.00376072 119 LEU   B C    
3400 O O    . LEU   B 107 ? 0.529959 0.415154 0.20133  0.077022    0.0587284   0.00038978  119 LEU   B O    
3401 C CB   . LEU   B 107 ? 0.55152  0.422695 0.256187 0.0822993   0.0419636   -0.0206336  119 LEU   B CB   
3402 C CG   . LEU   B 107 ? 0.572411 0.439591 0.303579 0.0829836   0.0348728   -0.0224737  119 LEU   B CG   
3403 C CD1  . LEU   B 107 ? 0.553577 0.442104 0.315287 0.0928027   0.0482965   -0.0170067  119 LEU   B CD1  
3404 C CD2  . LEU   B 107 ? 0.584308 0.458273 0.333675 0.06972     0.017686    -0.0156167  119 LEU   B CD2  
3405 H H    . LEU   B 107 ? 0.477465 0.369604 0.202236 0.0620823   0.0176868   -0.00541491 119 LEU   B H    
3406 H HA   . LEU   B 107 ? 0.474857 0.391708 0.229587 0.0783075   0.0541501   -0.00431401 119 LEU   B HA   
3407 H HB2  . LEU   B 107 ? 0.569572 0.427567 0.253259 0.0783521   0.0304058   -0.024623   119 LEU   B HB2  
3408 H HB3  . LEU   B 107 ? 0.576107 0.441029 0.265758 0.0906779   0.0549398   -0.0257414  119 LEU   B HB3  
3409 H HG   . LEU   B 107 ? 0.600751 0.445648 0.316434 0.0864233   0.0326915   -0.0325891  119 LEU   B HG   
3410 H HD11 . LEU   B 107 ? 0.568739 0.456842 0.322524 0.100731    0.0609898   -0.0216291  119 LEU   B HD11 
3411 H HD12 . LEU   B 107 ? 0.554717 0.435259 0.32631  0.0961028   0.0442866   -0.017245   119 LEU   B HD12 
3412 H HD13 . LEU   B 107 ? 0.524922 0.43582  0.304975 0.0884899   0.0481778   -0.00922779 119 LEU   B HD13 
3413 H HD21 . LEU   B 107 ? 0.581553 0.446783 0.31512  0.0643393   0.00843001  -0.0196525  119 LEU   B HD21 
3414 H HD22 . LEU   B 107 ? 0.543271 0.438547 0.309546 0.0671802   0.0199499   -0.00709051 119 LEU   B HD22 
3415 H HD23 . LEU   B 107 ? 0.571478 0.437322 0.332289 0.0695105   0.0140679   -0.0161457  119 LEU   B HD23 
3416 N N    . PRO   B 108 ? 0.515953 0.421494 0.223531 0.0881466   0.0894464   -0.00538835 120 PRO   B N    
3417 C CA   . PRO   B 108 ? 0.508871 0.429664 0.251261 0.09542     0.0950733   -0.0108855  120 PRO   B CA   
3418 C C    . PRO   B 108 ? 0.475525 0.432886 0.269691 0.0909115   0.0952465   -0.00428517 120 PRO   B C    
3419 O O    . PRO   B 108 ? 0.467302 0.439642 0.289283 0.0991477   0.0952763   -0.00785251 120 PRO   B O    
3420 C CB   . PRO   B 108 ? 0.545746 0.463951 0.275804 0.106834    0.120842    -0.0174388  120 PRO   B CB   
3421 C CG   . PRO   B 108 ? 0.554576 0.470136 0.26089  0.101247    0.135518    -0.00836238 120 PRO   B CG   
3422 C CD   . PRO   B 108 ? 0.554774 0.453825 0.234151 0.0926946   0.113021    -0.00224479 120 PRO   B CD   
3423 H HA   . PRO   B 108 ? 0.515087 0.423071 0.253257 0.097586    0.0835693   -0.0159751  120 PRO   B HA   
3424 H HB2  . PRO   B 108 ? 0.52735  0.466007 0.289493 0.111034    0.129669    -0.0184038  120 PRO   B HB2  
3425 H HB3  . PRO   B 108 ? 0.570844 0.468277 0.276046 0.113466    0.119316    -0.02611    120 PRO   B HB3  
3426 H HG2  . PRO   B 108 ? 0.535544 0.472543 0.272325 0.0969266   0.145714    -0.0026645  120 PRO   B HG2  
3427 H HG3  . PRO   B 108 ? 0.591741 0.494727 0.270595 0.108211    0.149836    -0.0123843  120 PRO   B HG3  
3428 H HD2  . PRO   B 108 ? 0.545686 0.452201 0.231601 0.0866043   0.117117    0.00753476  120 PRO   B HD2  
3429 H HD3  . PRO   B 108 ? 0.589178 0.466643 0.228753 0.0969983   0.109983    -0.00666476 120 PRO   B HD3  
3430 N N    . LYS   B 109 ? 0.468081 0.438801 0.274126 0.0794892   0.09395     0.00413071  121 LYS   B N    
3431 C CA   . LYS   B 109 ? 0.435545 0.441558 0.289645 0.0742996   0.0934077   0.00630147  121 LYS   B CA   
3432 C C    . LYS   B 109 ? 0.411528 0.427329 0.282727 0.0749723   0.0725912   0.0061206   121 LYS   B C    
3433 O O    . LYS   B 109 ? 0.395261 0.438515 0.299121 0.080666    0.0720007   0.00324514  121 LYS   B O    
3434 C CB   . LYS   B 109 ? 0.440474 0.450436 0.299813 0.0616259   0.0959179   0.0140041   121 LYS   B CB   
3435 C CG   . LYS   B 109 ? 0.412369 0.458501 0.323268 0.0544543   0.0979467   0.0120724   121 LYS   B CG   
3436 C CD   . LYS   B 109 ? 0.424057 0.469044 0.343313 0.0419632   0.100788    0.018559    121 LYS   B CD   
3437 C CE   . LYS   B 109 ? 0.470872 0.498704 0.375537 0.039132    0.124578    0.0264592   121 LYS   B CE   
3438 N NZ   . LYS   B 109 ? 0.477182 0.524179 0.410444 0.0408333   0.149073    0.0206848   121 LYS   B NZ   
3439 H H    . LYS   B 109 ? 0.479219 0.436219 0.262358 0.0754912   0.0927824   0.00778019  121 LYS   B H    
3440 H HA   . LYS   B 109 ? 0.43738  0.459179 0.311162 0.0792632   0.106313    0.00244151  121 LYS   B HA   
3441 H HB2  . LYS   B 109 ? 0.462556 0.461698 0.305607 0.0619462   0.11022     0.0167929   121 LYS   B HB2  
3442 H HB3  . LYS   B 109 ? 0.437263 0.434741 0.280976 0.0578538   0.0821907   0.017206    121 LYS   B HB3  
3443 H HG2  . LYS   B 109 ? 0.396413 0.453724 0.319114 0.0559013   0.0841885   0.00944388  121 LYS   B HG2  
3444 H HG3  . LYS   B 109 ? 0.417052 0.478172 0.347717 0.0575852   0.111281    0.00765055  121 LYS   B HG3  
3445 H HD2  . LYS   B 109 ? 0.42129  0.45349  0.323266 0.0399623   0.0871335   0.0223368   121 LYS   B HD2  
3446 H HD3  . LYS   B 109 ? 0.400686 0.469373 0.354311 0.0377668   0.0995611   0.0137252   121 LYS   B HD3  
3447 H HE2  . LYS   B 109 ? 0.492338 0.496389 0.358238 0.0439031   0.123696    0.0310618   121 LYS   B HE2  
3448 H HE3  . LYS   B 109 ? 0.462666 0.489151 0.376897 0.0317405   0.125535    0.0311012   121 LYS   B HE3  
3449 H HZ1  . LYS   B 109 ? 0.490697 0.531872 0.407129 0.0488933   0.152237    0.0183708   121 LYS   B HZ1  
3450 H HZ2  . LYS   B 109 ? 0.45335  0.525897 0.422771 0.0387899   0.145554    0.0131686   121 LYS   B HZ2  
3451 H HZ3  . LYS   B 109 ? 0.493226 0.532847 0.426231 0.0362421   0.165329    0.0264203   121 LYS   B HZ3  
3452 N N    . ILE   B 110 ? 0.408773 0.405211 0.260061 0.0690921   0.0559512   0.00955084  122 ILE   B N    
3453 C CA   . ILE   B 110 ? 0.392387 0.395868 0.25749  0.0681449   0.0406092   0.0121274   122 ILE   B CA   
3454 C C    . ILE   B 110 ? 0.411503 0.383791 0.253783 0.0720269   0.0332658   0.0105622   122 ILE   B C    
3455 O O    . ILE   B 110 ? 0.428809 0.377436 0.24692  0.0658217   0.0271676   0.00813983  122 ILE   B O    
3456 C CB   . ILE   B 110 ? 0.399483 0.410588 0.271711 0.0554709   0.0299176   0.0167508   122 ILE   B CB   
3457 C CG1  . ILE   B 110 ? 0.413363 0.446132 0.306059 0.0491489   0.0377488   0.0169307   122 ILE   B CG1  
3458 C CG2  . ILE   B 110 ? 0.388745 0.409476 0.273794 0.0552069   0.0187164   0.0201222   122 ILE   B CG2  
3459 C CD1  . ILE   B 110 ? 0.405703 0.471209 0.332324 0.0536769   0.0448361   0.0117529   122 ILE   B CD1  
3460 H H    . ILE   B 110 ? 0.424969 0.40405  0.253663 0.0658951   0.0546968   0.0103654   122 ILE   B H    
3461 H HA   . ILE   B 110 ? 0.385841 0.408562 0.271047 0.0738064   0.0424639   0.0113349   122 ILE   B HA   
3462 H HB   . ILE   B 110 ? 0.412036 0.404563 0.26545  0.051535    0.025433    0.0172362   122 ILE   B HB   
3463 H HG12 . ILE   B 110 ? 0.423182 0.444215 0.302284 0.0484306   0.0456152   0.0178329   122 ILE   B HG12 
3464 H HG13 . ILE   B 110 ? 0.395324 0.431663 0.293289 0.0425407   0.0304675   0.0189659   122 ILE   B HG13 
3465 H HG21 . ILE   B 110 ? 0.372378 0.40298  0.265957 0.0481222   0.0145056   0.0215038   122 ILE   B HG21 
3466 H HG22 . ILE   B 110 ? 0.382305 0.41815  0.279885 0.0624115   0.0208584   0.0195258   122 ILE   B HG22 
3467 H HG23 . ILE   B 110 ? 0.399982 0.401682 0.272223 0.0554527   0.0142149   0.0213121   122 ILE   B HG23 
3468 H HD11 . ILE   B 110 ? 0.390028 0.467925 0.326441 0.055754    0.0360565   0.0113168   122 ILE   B HD11 
3469 H HD12 . ILE   B 110 ? 0.393704 0.469606 0.334924 0.0475381   0.0505577   0.0106382   122 ILE   B HD12 
3470 H HD13 . ILE   B 110 ? 0.412532 0.477226 0.338111 0.0609675   0.0525927   0.00928325  122 ILE   B HD13 
3471 N N    . PRO   B 111 ? 0.419757 0.390539 0.270764 0.082205    0.0319422   0.0116864   123 PRO   B N    
3472 C CA   . PRO   B 111 ? 0.454831 0.391329 0.289194 0.0847796   0.0272547   0.0101236   123 PRO   B CA   
3473 C C    . PRO   B 111 ? 0.438077 0.364805 0.272944 0.072037    0.0151656   0.0154421   123 PRO   B C    
3474 O O    . PRO   B 111 ? 0.422884 0.37121  0.270372 0.0637321   0.0103945   0.0210212   123 PRO   B O    
3475 C CB   . PRO   B 111 ? 0.48525  0.424067 0.33173  0.102113    0.0321158   0.012443    123 PRO   B CB   
3476 C CG   . PRO   B 111 ? 0.450914 0.430717 0.322854 0.104537    0.0299514   0.018521    123 PRO   B CG   
3477 C CD   . PRO   B 111 ? 0.43521  0.435642 0.312963 0.0930688   0.0340398   0.0140998   123 PRO   B CD   
3478 H HA   . PRO   B 111 ? 0.474734 0.394309 0.291548 0.0848689   0.0302432   0.00308621  123 PRO   B HA   
3479 H HB2  . PRO   B 111 ? 0.493275 0.41287  0.336056 0.103603    0.0282639   0.0159926   123 PRO   B HB2  
3480 H HB3  . PRO   B 111 ? 0.494209 0.429062 0.33695  0.110061    0.0402731   0.00601831  123 PRO   B HB3  
3481 H HG2  . PRO   B 111 ? 0.445841 0.42688  0.319528 0.101272    0.0228885   0.0254326   123 PRO   B HG2  
3482 H HG3  . PRO   B 111 ? 0.45647  0.447663 0.339574 0.117115    0.0333482   0.0177258   123 PRO   B HG3  
3483 H HD2  . PRO   B 111 ? 0.40583  0.425263 0.295983 0.0879199   0.029046    0.0171141   123 PRO   B HD2  
3484 H HD3  . PRO   B 111 ? 0.427954 0.439868 0.313918 0.0984086   0.0430492   0.00942233  123 PRO   B HD3  
3485 N N    . SER   B 112 ? 0.447428 0.340927 0.270666 0.0697761   0.0116421   0.0110867   124 SER   B N    
3486 C CA   . SER   B 112 ? 0.466811 0.347528 0.296977 0.0577158   0.00369228  0.0148913   124 SER   B CA   
3487 C C    . SER   B 112 ? 0.455237 0.350063 0.301444 0.0614508   0.00623448  0.0303837   124 SER   B C    
3488 O O    . SER   B 112 ? 0.449431 0.348895 0.297265 0.0768219   0.0116415   0.0361528   124 SER   B O    
3489 C CB   . SER   B 112 ? 0.538342 0.379442 0.358947 0.056826    0.00275702  0.00510827  124 SER   B CB   
3490 O OG   . SER   B 112 ? 0.596743 0.424203 0.431563 0.043842    -0.00161408 0.00872101  124 SER   B OG   
3491 H H    . SER   B 112 ? 0.477789 0.355683 0.290082 0.0757104   0.0154589   0.00418408  124 SER   B H    
3492 H HA   . SER   B 112 ? 0.456876 0.346175 0.287753 0.0480579   -0.00233964 0.0128265   124 SER   B HA   
3493 H HB2  . SER   B 112 ? 0.552487 0.387116 0.35952  0.0545647   -0.00072733 -0.00596587 124 SER   B HB2  
3494 H HB3  . SER   B 112 ? 0.556125 0.386898 0.375052 0.0679823   0.0093505   0.0063483   124 SER   B HB3  
3496 N N    . ASN   B 113 ? 0.423311 0.328606 0.280251 0.0490293   0.00202714  0.0363931   125 ASN   B N    
3497 C CA   . ASN   B 113 ? 0.435442 0.34801  0.30009  0.0515532   0.00576717  0.0514146   125 ASN   B CA   
3498 C C    . ASN   B 113 ? 0.433491 0.378118 0.299535 0.0660409   0.00681911  0.0569292   125 ASN   B C    
3499 O O    . ASN   B 113 ? 0.480587 0.425237 0.343008 0.0781627   0.00957485  0.0692116   125 ASN   B O    
3500 C CB   . ASN   B 113 ? 0.480229 0.354872 0.34142  0.054918    0.0119393   0.0587434   125 ASN   B CB   
3501 C CG   . ASN   B 113 ? 0.496468 0.344773 0.364913 0.0371473   0.00957537  0.0495655   125 ASN   B CG   
3502 O OD1  . ASN   B 113 ? 0.502552 0.365515 0.383744 0.0219167   0.00511335  0.0470733   125 ASN   B OD1  
3503 N ND2  . ASN   B 113 ? 0.539635 0.352816 0.402589 0.039586    0.0109391   0.0407789   125 ASN   B ND2  
3504 H H    . ASN   B 113 ? 0.422571 0.330923 0.280971 0.0395023   -0.00297333 0.0310706   125 ASN   B H    
3505 H HA   . ASN   B 113 ? 0.424866 0.345986 0.297231 0.0408617   0.00366377  0.0525176   125 ASN   B HA   
3506 H HB2  . ASN   B 113 ? 0.493002 0.356988 0.347539 0.0662822   0.0139618   0.0567176   125 ASN   B HB2  
3507 H HB3  . ASN   B 113 ? 0.482978 0.360665 0.344996 0.0580739   0.0159034   0.0712197   125 ASN   B HB3  
3508 H HD21 . ASN   B 113 ? 0.544769 0.346551 0.410794 0.0299452   0.00648102  0.0298348   125 ASN   B HD21 
3509 H HD22 . ASN   B 113 ? 0.551803 0.353125 0.40861  0.0513629   0.0157533   0.044776    125 ASN   B HD22 
3510 N N    . ALA   B 114 ? 0.39353  0.366175 0.265993 0.0642601   0.00415272  0.0482455   126 ALA   B N    
3511 C CA   . ALA   B 114 ? 0.387253 0.39381  0.268852 0.0757697   0.00399084  0.0480873   126 ALA   B CA   
3512 C C    . ALA   B 114 ? 0.360196 0.394344 0.249292 0.0713265   0.00025335  0.0517218   126 ALA   B C    
3513 O O    . ALA   B 114 ? 0.338347 0.376114 0.232829 0.0568282   -0.00116014 0.0489703   126 ALA   B O    
3514 C CB   . ALA   B 114 ? 0.383426 0.403902 0.272645 0.0747765   0.00676244  0.0366073   126 ALA   B CB   
3515 H H    . ALA   B 114 ? 0.392175 0.362611 0.264503 0.0557361   0.00225834  0.0420293   126 ALA   B H    
3516 H HA   . ALA   B 114 ? 0.402203 0.404198 0.28049  0.0883544   0.0052159   0.0526961   126 ALA   B HA   
3517 H HB1  . ALA   B 114 ? 0.395805 0.399324 0.277492 0.0788978   0.0104284   0.0338623   126 ALA   B HB1  
3518 H HB2  . ALA   B 114 ? 0.369259 0.39134  0.259703 0.0640586   0.0055506   0.033741    126 ALA   B HB2  
3519 H HB3  . ALA   B 114 ? 0.370327 0.414928 0.271289 0.0811192   0.00681523  0.0345572   126 ALA   B HB3  
3520 N N    . THR   B 115 ? 0.353744 0.408877 0.24271  0.0859776   -0.00223562 0.0563652   127 THR   B N    
3521 C CA   . THR   B 115 ? 0.342804 0.431392 0.237233 0.0855591   -0.00682499 0.0543622   127 THR   B CA   
3522 C C    . THR   B 115 ? 0.320897 0.444376 0.238329 0.0856003   -0.0103412  0.0383241   127 THR   B C    
3523 O O    . THR   B 115 ? 0.313454 0.447043 0.240547 0.0967264   -0.0108386  0.0334945   127 THR   B O    
3524 C CB   . THR   B 115 ? 0.36601  0.459501 0.243243 0.103258    -0.00955345 0.0669428   127 THR   B CB   
3525 O OG1  . THR   B 115 ? 0.398025 0.455288 0.259417 0.0973398   -0.00162737 0.0818372   127 THR   B OG1  
3526 C CG2  . THR   B 115 ? 0.374286 0.502624 0.249648 0.105438    -0.0151011  0.0631097   127 THR   B CG2  
3527 H H    . THR   B 115 ? 0.372998 0.421547 0.257518 0.0977383   -0.00182047 0.060008    127 THR   B H    
3528 H HA   . THR   B 115 ? 0.335206 0.419737 0.229732 0.0740419   -0.00526213 0.0549047   127 THR   B HA   
3529 H HB   . THR   B 115 ? 0.382834 0.477609 0.259883 0.116709    -0.0119489  0.0679068   127 THR   B HB   
3531 H HG21 . THR   B 115 ? 0.392931 0.520594 0.250899 0.117892    -0.0164364  0.0732979   127 THR   B HG21 
3532 H HG22 . THR   B 115 ? 0.360853 0.486429 0.237425 0.0929292   -0.0113857  0.0622899   127 THR   B HG22 
3533 H HG23 . THR   B 115 ? 0.354419 0.508546 0.244985 0.107451    -0.0207601  0.0506217   127 THR   B HG23 
3534 N N    . LEU   B 116 ? 0.288188 0.430315 0.2182   0.0733598   -0.0115371  0.0295861   128 LEU   B N    
3535 C CA   . LEU   B 116 ? 0.289516 0.460228 0.246317 0.0696502   -0.0123502  0.0137941   128 LEU   B CA   
3536 C C    . LEU   B 116 ? 0.283449 0.491029 0.249604 0.0737383   -0.0204565  0.00365605  128 LEU   B C    
3537 O O    . LEU   B 116 ? 0.300372 0.509017 0.251039 0.0733414   -0.0225558  0.00801616  128 LEU   B O    
3538 C CB   . LEU   B 116 ? 0.281951 0.440884 0.248971 0.0528976   -0.00644874 0.00952267  128 LEU   B CB   
3539 C CG   . LEU   B 116 ? 0.319608 0.442892 0.271654 0.0484202   -0.0009133  0.0169941   128 LEU   B CG   
3540 C CD1  . LEU   B 116 ? 0.3196   0.438678 0.282238 0.0366051   0.00384733  0.0122925   128 LEU   B CD1  
3541 C CD2  . LEU   B 116 ? 0.351838 0.466045 0.298427 0.0586944   0.00342659  0.0181186   128 LEU   B CD2  
3542 H H    . LEU   B 116 ? 0.295364 0.431357 0.219272 0.0669684   -0.0108099  0.0332983   128 LEU   B H    
3543 H HA   . LEU   B 116 ? 0.289639 0.464616 0.253444 0.0765938   -0.0112758  0.0113005   128 LEU   B HA   
3544 H HB2  . LEU   B 116 ? 0.281215 0.441487 0.247072 0.0470562   -0.00817619 0.00968424  128 LEU   B HB2  
3545 H HB3  . LEU   B 116 ? 0.277421 0.452353 0.263557 0.0507755   -0.00459317 0.00028352  128 LEU   B HB3  
3546 H HG   . LEU   B 116 ? 0.325864 0.433713 0.264993 0.0461863   -0.00295274 0.0236155   128 LEU   B HG   
3547 H HD11 . LEU   B 116 ? 0.307445 0.432731 0.27642  0.0309801   0.0010867   0.0106556   128 LEU   B HD11 
3548 H HD12 . LEU   B 116 ? 0.325383 0.422721 0.274317 0.034586    0.00538284  0.0166269   128 LEU   B HD12 
3549 H HD13 . LEU   B 116 ? 0.312561 0.444034 0.289505 0.0374148   0.00848268  0.0065276   128 LEU   B HD13 
3550 H HD21 . LEU   B 116 ? 0.357041 0.465894 0.293729 0.0667223   0.00062501  0.0235763   128 LEU   B HD21 
3551 H HD22 . LEU   B 116 ? 0.340876 0.474701 0.303998 0.0618397   0.00565249  0.011355    128 LEU   B HD22 
3552 H HD23 . LEU   B 116 ? 0.353387 0.447328 0.290451 0.0549002   0.00732289  0.0196277   128 LEU   B HD23 
3553 N N    . PHE   B 117 ? 0.266096 0.504814 0.260696 0.0761945   -0.0236041  -0.0123727  129 PHE   B N    
3554 C CA   . PHE   B 117 ? 0.272845 0.550311 0.2837   0.0780975   -0.0329746  -0.0294781  129 PHE   B CA   
3555 C C    . PHE   B 117 ? 0.271581 0.562562 0.32201  0.0626257   -0.0273961  -0.0476442  129 PHE   B C    
3556 O O    . PHE   B 117 ? 0.269327 0.557616 0.341461 0.058799    -0.0189495  -0.0499994  129 PHE   B O    
3557 C CB   . PHE   B 117 ? 0.278968 0.586254 0.292022 0.0986163   -0.045314   -0.034105   129 PHE   B CB   
3558 C CG   . PHE   B 117 ? 0.277925 0.631019 0.310437 0.101729    -0.0586874  -0.0572802  129 PHE   B CG   
3559 C CD1  . PHE   B 117 ? 0.298206 0.66311  0.300572 0.111398    -0.0688035  -0.056822   129 PHE   B CD1  
3560 C CD2  . PHE   B 117 ? 0.264562 0.64847  0.34572  0.0944631   -0.0598735  -0.0807777  129 PHE   B CD2  
3561 C CE1  . PHE   B 117 ? 0.296023 0.703779 0.312556 0.115384    -0.0830037  -0.081697   129 PHE   B CE1  
3562 C CE2  . PHE   B 117 ? 0.27666  0.702789 0.379306 0.0956344   -0.0736046  -0.106467   129 PHE   B CE2  
3563 C CZ   . PHE   B 117 ? 0.29189  0.730477 0.360284 0.106815    -0.0866781  -0.10813    129 PHE   B CZ   
3564 H H    . PHE   B 117 ? 0.268393 0.504517 0.274107 0.0763371   -0.019304   -0.0139874  129 PHE   B H    
3565 H HA   . PHE   B 117 ? 0.276492 0.551606 0.271322 0.0769846   -0.034787   -0.0265401  129 PHE   B HA   
3566 H HB2  . PHE   B 117 ? 0.298333 0.593424 0.283603 0.109216    -0.0479131  -0.0204037  129 PHE   B HB2  
3567 H HB3  . PHE   B 117 ? 0.27763  0.586234 0.307368 0.100411    -0.0420615  -0.0359724  129 PHE   B HB3  
3568 H HD1  . PHE   B 117 ? 0.309468 0.653035 0.280909 0.115553    -0.0654857  -0.0400044  129 PHE   B HD1  
3569 H HD2  . PHE   B 117 ? 0.257039 0.632217 0.357215 0.0876655   -0.0502316  -0.0800805  129 PHE   B HD2  
3570 H HE1  . PHE   B 117 ? 0.317722 0.732848 0.308852 0.12302     -0.0891333  -0.0814172  129 PHE   B HE1  
3571 H HE2  . PHE   B 117 ? 0.263684 0.710505 0.404195 0.0890492   -0.0736185  -0.123667   129 PHE   B HE2  
3572 H HZ   . PHE   B 117 ? 0.294738 0.763235 0.375549 0.108735    -0.0974095  -0.127872   129 PHE   B HZ   
3573 N N    . PHE   B 118 ? 0.235972 0.541816 0.296612 0.0547713   -0.0305474  -0.0611422  130 PHE   B N    
3574 C CA   . PHE   B 118 ? 0.233945 0.551491 0.335466 0.040439    -0.0250854  -0.0798472  130 PHE   B CA   
3575 C C    . PHE   B 118 ? 0.230356 0.587135 0.350556 0.0421511   -0.0371139  -0.105399   130 PHE   B C    
3576 O O    . PHE   B 118 ? 0.24186  0.606393 0.334835 0.0497523   -0.0456599  -0.106012   130 PHE   B O    
3577 C CB   . PHE   B 118 ? 0.214073 0.500938 0.316038 0.0254477   -0.0139917  -0.0736332  130 PHE   B CB   
3578 C CG   . PHE   B 118 ? 0.223706 0.471826 0.307564 0.0221453   -0.0036673  -0.0524106  130 PHE   B CG   
3579 C CD1  . PHE   B 118 ? 0.215495 0.440506 0.263606 0.0268531   -0.00603359 -0.0348111  130 PHE   B CD1  
3580 C CD2  . PHE   B 118 ? 0.230915 0.466042 0.333707 0.0141158   0.00913211  -0.0514446  130 PHE   B CD2  
3581 C CE1  . PHE   B 118 ? 0.253721 0.445691 0.285789 0.023908    0.00047075  -0.0201933  130 PHE   B CE1  
3582 C CE2  . PHE   B 118 ? 0.235673 0.435971 0.315143 0.0129254   0.0171927   -0.0337969  130 PHE   B CE2  
3583 C CZ   . PHE   B 118 ? 0.259154 0.439589 0.303623 0.0182015   0.010949    -0.020082   130 PHE   B CZ   
3584 H H    . PHE   B 118 ? 0.251919 0.559216 0.293749 0.0585408   -0.0349694  -0.0586559  130 PHE   B H    
3585 H HA   . PHE   B 118 ? 0.226831 0.548299 0.347632 0.0394919   -0.0204747  -0.0822373  130 PHE   B HA   
3586 H HB2  . PHE   B 118 ? 0.220582 0.506212 0.307673 0.026368    -0.0177034  -0.0726137  130 PHE   B HB2  
3587 H HB3  . PHE   B 118 ? 0.214406 0.508817 0.344742 0.0171746   -0.0100824  -0.0862367  130 PHE   B HB3  
3588 H HD1  . PHE   B 118 ? 0.229974 0.461735 0.26488  0.0318447   -0.0117424  -0.0335658  130 PHE   B HD1  
3589 H HD2  . PHE   B 118 ? 0.226054 0.47563  0.357177 0.00920729  0.0128779   -0.0633321  130 PHE   B HD2  
3590 H HE1  . PHE   B 118 ? 0.251329 0.428553 0.263351 0.0259221   -0.00173935 -0.0107189  130 PHE   B HE1  
3591 H HE2  . PHE   B 118 ? 0.24562  0.436328 0.333261 0.00868349  0.0272225   -0.0319484  130 PHE   B HE2  
3592 H HZ   . PHE   B 118 ? 0.260999 0.419389 0.289816 0.0176776   0.0145484   -0.010835   130 PHE   B HZ   
3593 N N    . GLU   B 119 ? 0.226406 0.607003 0.39418  0.0342663   -0.0359831  -0.127344   131 GLU   B N    
3594 C CA   . GLU   B 119 ? 0.229735 0.640074 0.428195 0.027961    -0.0433418  -0.157291   131 GLU   B CA   
3595 C C    . GLU   B 119 ? 0.233396 0.619091 0.463096 0.00751697  -0.0262137  -0.161351   131 GLU   B C    
3596 O O    . GLU   B 119 ? 0.251974 0.622592 0.506312 -0.00187887 -0.0113243  -0.154953   131 GLU   B O    
3597 C CB   . GLU   B 119 ? 0.227033 0.685182 0.46041  0.0352345   -0.0569056  -0.181049   131 GLU   B CB   
3598 C CG   . GLU   B 119 ? 0.229548 0.724594 0.503037 0.0280301   -0.0673385  -0.219219   131 GLU   B CG   
3599 C CD   . GLU   B 119 ? 0.233695 0.781025 0.547718 0.0356626   -0.0834776  -0.244572   131 GLU   B CD   
3600 O OE1  . GLU   B 119 ? 0.242272 0.818119 0.52956  0.0578126   -0.104611   -0.245456   131 GLU   B OE1  
3601 O OE2  . GLU   B 119 ? 0.24797  0.809368 0.62437  0.0199081   -0.0748319  -0.264071   131 GLU   B OE2  
3602 H H    . GLU   B 119 ? 0.222994 0.601054 0.406555 0.032275    -0.0294371  -0.124524   131 GLU   B H    
3603 H HA   . GLU   B 119 ? 0.237777 0.651685 0.411128 0.0338697   -0.0507669  -0.158358   131 GLU   B HA   
3604 H HB2  . GLU   B 119 ? 0.237293 0.706886 0.444517 0.0508756   -0.0684284  -0.174945   131 GLU   B HB2  
3605 H HB3  . GLU   B 119 ? 0.221667 0.676945 0.479297 0.0303262   -0.0477882  -0.178294   131 GLU   B HB3  
3606 H HG2  . GLU   B 119 ? 0.223514 0.70444  0.524913 0.0123737   -0.0547382  -0.224913   131 GLU   B HG2  
3607 H HG3  . GLU   B 119 ? 0.239194 0.738742 0.486182 0.0341731   -0.0761835  -0.223418   131 GLU   B HG3  
3608 N N    . ILE   B 120 ? 0.245728 0.625441 0.4715   0.00245381  -0.0269688  -0.170459   132 ILE   B N    
3609 C CA   . ILE   B 120 ? 0.231678 0.581396 0.479158 -0.0129247  -0.011794   -0.169968   132 ILE   B CA   
3610 C C    . ILE   B 120 ? 0.247733 0.618885 0.531508 -0.0204154  -0.0159622  -0.204232   132 ILE   B C    
3611 O O    . ILE   B 120 ? 0.242187 0.63483  0.506986 -0.0119591  -0.0289362  -0.218824   132 ILE   B O    
3612 C CB   . ILE   B 120 ? 0.233811 0.549855 0.442409 -0.0104346  -0.00767371 -0.146648   132 ILE   B CB   
3613 C CG1  . ILE   B 120 ? 0.234276 0.529888 0.404399 -0.00270377 -0.00642619 -0.116599   132 ILE   B CG1  
3614 C CG2  . ILE   B 120 ? 0.239117 0.524468 0.470911 -0.0226827  0.00581124  -0.145329   132 ILE   B CG2  
3615 C CD1  . ILE   B 120 ? 0.25167  0.522157 0.388345 -0.00028007 -0.00552889 -0.0976909  132 ILE   B CD1  
3616 H H    . ILE   B 120 ? 0.246974 0.64168  0.454812 0.0101958   -0.0370851  -0.177033   132 ILE   B H    
3617 H HA   . ILE   B 120 ? 0.234399 0.571729 0.499986 -0.0196572  -0.00125906 -0.163658   132 ILE   B HA   
3618 H HB   . ILE   B 120 ? 0.238226 0.567417 0.432236 -0.00482407 -0.0153337  -0.154035   132 ILE   B HB   
3619 H HG12 . ILE   B 120 ? 0.236351 0.517514 0.416483 -0.00743286 0.00201979  -0.108956   132 ILE   B HG12 
3620 H HG13 . ILE   B 120 ? 0.239295 0.553115 0.398066 0.00589237  -0.0143535  -0.117818   132 ILE   B HG13 
3621 H HG21 . ILE   B 120 ? 0.237276 0.503128 0.447238 -0.0202522  0.00729488  -0.129948   132 ILE   B HG21 
3622 H HG22 . ILE   B 120 ? 0.239433 0.513228 0.488165 -0.0287625  0.0148379   -0.140509   132 ILE   B HG22 
3623 H HG23 . ILE   B 120 ? 0.242356 0.538744 0.494303 -0.0261637  0.00422637  -0.164848   132 ILE   B HG23 
3624 H HD11 . ILE   B 120 ? 0.249186 0.532481 0.379398 0.00281015  -0.0103048  -0.10589    132 ILE   B HD11 
3625 H HD12 . ILE   B 120 ? 0.246894 0.509111 0.360784 0.00498026  -0.00678424 -0.0828731  132 ILE   B HD12 
3626 H HD13 . ILE   B 120 ? 0.245472 0.495558 0.390995 -0.00669126 0.00137835  -0.0926952  132 ILE   B HD13 
3627 N N    . GLU   B 121 ? 0.255584 0.616419 0.588919 -0.0362932  -0.00271915 -0.215982   133 GLU   B N    
3628 C CA   . GLU   B 121 ? 0.274208 0.643378 0.645961 -0.0460809  -0.00282926 -0.247814   133 GLU   B CA   
3629 C C    . GLU   B 121 ? 0.270337 0.592732 0.645844 -0.0541404  0.0139506   -0.23391    133 GLU   B C    
3630 O O    . GLU   B 121 ? 0.257685 0.546562 0.642633 -0.0614894  0.0309486   -0.212269   133 GLU   B O    
3631 C CB   . GLU   B 121 ? 0.273329 0.66642  0.708524 -0.0591901  0.00033545  -0.275094   133 GLU   B CB   
3632 C CG   . GLU   B 121 ? 0.292542 0.690895 0.776    -0.0721117  0.00158647  -0.311992   133 GLU   B CG   
3633 C CD   . GLU   B 121 ? 0.289369 0.716782 0.843467 -0.0869943  0.00336346  -0.344011   133 GLU   B CD   
3634 O OE1  . GLU   B 121 ? 0.300101 0.748274 0.864704 -0.0854222  0.00271478  -0.337551   133 GLU   B OE1  
3635 O OE2  . GLU   B 121 ? 0.320987 0.752343 0.924013 -0.100311   0.00561093  -0.37726    133 GLU   B OE2  
3636 H H    . GLU   B 121 ? 0.253871 0.600503 0.597356 -0.0411885  0.00788489  -0.203881   133 GLU   B H    
3637 H HA   . GLU   B 121 ? 0.273613 0.663547 0.628733 -0.038229   -0.0157608  -0.261443   133 GLU   B HA   
3638 H HB2  . GLU   B 121 ? 0.27314  0.699172 0.706968 -0.0520234  -0.0127239  -0.284704   133 GLU   B HB2  
3639 H HB3  . GLU   B 121 ? 0.274108 0.646649 0.722743 -0.0663424  0.0153828   -0.259521   133 GLU   B HB3  
3640 H HG2  . GLU   B 121 ? 0.294329 0.65774  0.782189 -0.0785382  0.0156224   -0.301114   133 GLU   B HG2  
3641 H HG3  . GLU   B 121 ? 0.293709 0.710557 0.759062 -0.0641385  -0.0124136  -0.327377   133 GLU   B HG3  
3642 N N    . LEU   B 122 ? 0.272968 0.593685 0.638953 -0.0506516  0.00928544  -0.246044   134 LEU   B N    
3643 C CA   . LEU   B 122 ? 0.293663 0.573828 0.669904 -0.0557609  0.0229861   -0.236981   134 LEU   B CA   
3644 C C    . LEU   B 122 ? 0.314001 0.588155 0.751098 -0.0708257  0.0329251   -0.265169   134 LEU   B C    
3645 O O    . LEU   B 122 ? 0.352069 0.651712 0.811101 -0.0726647  0.0244354   -0.30205    134 LEU   B O    
3646 C CB   . LEU   B 122 ? 0.296484 0.576805 0.641536 -0.0450254  0.0167349   -0.23729    134 LEU   B CB   
3647 C CG   . LEU   B 122 ? 0.310229 0.550705 0.665922 -0.0463098  0.0286719   -0.22596    134 LEU   B CG   
3648 C CD1  . LEU   B 122 ? 0.319316 0.521561 0.664827 -0.0473271  0.0384498   -0.188866   134 LEU   B CD1  
3649 C CD2  . LEU   B 122 ? 0.326122 0.573277 0.653807 -0.0350643  0.0235805   -0.225662   134 LEU   B CD2  
3650 H H    . LEU   B 122 ? 0.278594 0.623942 0.63081  -0.0437776  -0.0023504  -0.259992   134 LEU   B H    
3651 H HA   . LEU   B 122 ? 0.289205 0.544051 0.655076 -0.0562896  0.0312835   -0.211375   134 LEU   B HA   
3652 H HB2  . LEU   B 122 ? 0.288004 0.572906 0.597955 -0.0370201  0.0114927   -0.220095   134 LEU   B HB2  
3653 H HB3  . LEU   B 122 ? 0.304236 0.608763 0.656128 -0.043772   0.00955576  -0.263164   134 LEU   B HB3  
3654 H HG   . LEU   B 122 ? 0.326976 0.561947 0.717467 -0.0534158  0.0341053   -0.244883   134 LEU   B HG   
3655 H HD11 . LEU   B 122 ? 0.323163 0.514608 0.692972 -0.0555434  0.0468752   -0.189995   134 LEU   B HD11 
3656 H HD12 . LEU   B 122 ? 0.321469 0.502862 0.664774 -0.0438554  0.0417313   -0.179355   134 LEU   B HD12 
3657 H HD13 . LEU   B 122 ? 0.304791 0.513944 0.621584 -0.0426156  0.0332843   -0.173779   134 LEU   B HD13 
3658 H HD21 . LEU   B 122 ? 0.326011 0.598091 0.653468 -0.0330287  0.0178355   -0.248638   134 LEU   B HD21 
3659 H HD22 . LEU   B 122 ? 0.310334 0.558647 0.607483 -0.0294368  0.0200887   -0.205815   134 LEU   B HD22 
3660 H HD23 . LEU   B 122 ? 0.327625 0.553108 0.66879  -0.035071   0.0301502   -0.222688   134 LEU   B HD23 
3661 N N    . LEU   B 123 ? 0.336556 0.574291 0.799183 -0.0813932  0.0521979   -0.247521   135 LEU   B N    
3662 C CA   . LEU   B 123 ? 0.363537 0.588762 0.888944 -0.098314   0.0668506   -0.269572   135 LEU   B CA   
3663 C C    . LEU   B 123 ? 0.364413 0.553919 0.903029 -0.0983891  0.0748809   -0.273519   135 LEU   B C    
3664 O O    . LEU   B 123 ? 0.366709 0.56059  0.950622 -0.107496   0.0767733   -0.308352   135 LEU   B O    
3665 C CB   . LEU   B 123 ? 0.393523 0.591646 0.937055 -0.10875    0.0885515   -0.244992   135 LEU   B CB   
3666 C CG   . LEU   B 123 ? 0.394033 0.623912 0.928271 -0.107624   0.0843934   -0.238752   135 LEU   B CG   
3667 C CD1  . LEU   B 123 ? 0.430032 0.626768 0.972107 -0.115597   0.110276    -0.209492   135 LEU   B CD1  
3668 C CD2  . LEU   B 123 ? 0.395123 0.677826 0.976037 -0.11516    0.0721076   -0.281898   135 LEU   B CD2  
3669 H H    . LEU   B 123 ? 0.330882 0.54957  0.770378 -0.0779519  0.057268    -0.220599   135 LEU   B H    
3670 H HA   . LEU   B 123 ? 0.362494 0.620643 0.91153  -0.102448   0.0579841   -0.299267   135 LEU   B HA   
3671 H HB2  . LEU   B 123 ? 0.397532 0.561901 0.915844 -0.103669   0.0963463   -0.217054   135 LEU   B HB2  
3672 H HB3  . LEU   B 123 ? 0.409094 0.598524 0.998089 -0.121377   0.100187    -0.260193   135 LEU   B HB3  
3673 H HG   . LEU   B 123 ? 0.380311 0.618947 0.870988 -0.0951415  0.0721766   -0.226021   135 LEU   B HG   
3674 H HD11 . LEU   B 123 ? 0.43325  0.593138 0.952476 -0.111832   0.118388    -0.186356   135 LEU   B HD11 
3675 H HD12 . LEU   B 123 ? 0.410451 0.622487 0.933134 -0.110453   0.106838    -0.199724   135 LEU   B HD12 
3676 H HD13 . LEU   B 123 ? 0.435982 0.632835 1.02532  -0.129067   0.122774    -0.223926   135 LEU   B HD13 
3677 H HD21 . LEU   B 123 ? 0.385005 0.691574 0.946885 -0.106253   0.0539406   -0.296247   135 LEU   B HD21 
3678 H HD22 . LEU   B 123 ? 0.408408 0.683794 1.03435  -0.127858   0.0817267   -0.299758   135 LEU   B HD22 
3679 H HD23 . LEU   B 123 ? 0.386003 0.686518 0.971666 -0.115652   0.0727205   -0.278149   135 LEU   B HD23 
3680 N N    . ASP   B 124 ? 0.379973 0.534288 0.881905 -0.0875654  0.0789769   -0.239084   136 ASP   B N    
3681 C CA   . ASP   B 124 ? 0.389515 0.507472 0.904693 -0.084302   0.0867639   -0.237943   136 ASP   B CA   
3682 C C    . ASP   B 124 ? 0.389439 0.485359 0.856602 -0.0682618  0.0828392   -0.201288   136 ASP   B C    
3683 O O    . ASP   B 124 ? 0.362851 0.459538 0.791584 -0.0634242  0.0793052   -0.173407   136 ASP   B O    
3684 C CB   . ASP   B 124 ? 0.446661 0.521121 1.00967  -0.0976707  0.110058    -0.234589   136 ASP   B CB   
3685 C CG   . ASP   B 124 ? 0.48024  0.525704 1.07969  -0.0980279  0.117684    -0.252499   136 ASP   B CG   
3686 O OD1  . ASP   B 124 ? 0.475207 0.541942 1.06726  -0.0889605  0.104282    -0.274943   136 ASP   B OD1  
3687 O OD2  . ASP   B 124 ? 0.529837 0.529661 1.1631   -0.106316   0.138705    -0.242437   136 ASP   B OD2  
3688 H H    . ASP   B 124 ? 0.362201 0.515777 0.831563 -0.0814149  0.076134    -0.21654    136 ASP   B H    
3689 H HA   . ASP   B 124 ? 0.397678 0.534315 0.923322 -0.0830657  0.0794077   -0.264651   136 ASP   B HA   
3690 H HB2  . ASP   B 124 ? 0.442835 0.532479 1.03427  -0.109602   0.114046    -0.250707   136 ASP   B HB2  
3691 H HB3  . ASP   B 124 ? 0.44851  0.495398 0.992551 -0.0944926  0.118437    -0.203274   136 ASP   B HB3  
3692 N N    . PHE   B 125 ? 0.384043 0.462237 0.857595 -0.0597587  0.0828598   -0.204545   137 PHE   B N    
3693 C CA   . PHE   B 125 ? 0.377655 0.430018 0.820755 -0.0452961  0.0805358   -0.171209   137 PHE   B CA   
3694 C C    . PHE   B 125 ? 0.410925 0.427533 0.884654 -0.0393907  0.0889619   -0.1737     137 PHE   B C    
3695 O O    . PHE   B 125 ? 0.41207  0.438223 0.917864 -0.0414028  0.0902708   -0.206935   137 PHE   B O    
3696 C CB   . PHE   B 125 ? 0.350596 0.437299 0.753282 -0.0345156  0.0638581   -0.168062   137 PHE   B CB   
3697 C CG   . PHE   B 125 ? 0.349996 0.469397 0.762071 -0.0313528  0.0578258   -0.201832   137 PHE   B CG   
3698 C CD1  . PHE   B 125 ? 0.352661 0.463481 0.775501 -0.0209825  0.0588248   -0.206072   137 PHE   B CD1  
3699 C CD2  . PHE   B 125 ? 0.344519 0.504599 0.752133 -0.0365907  0.0509845   -0.229058   137 PHE   B CD2  
3700 C CE1  . PHE   B 125 ? 0.373997 0.514807 0.802315 -0.0173495  0.0564925   -0.237688   137 PHE   B CE1  
3701 C CE2  . PHE   B 125 ? 0.356366 0.545259 0.764634 -0.0318579  0.0464241   -0.259686   137 PHE   B CE2  
3702 C CZ   . PHE   B 125 ? 0.373939 0.55311  0.790476 -0.0225693  0.050551    -0.263482   137 PHE   B CZ   
3703 H H    . PHE   B 125 ? 0.395057 0.478947 0.894121 -0.0625168  0.0836776   -0.229551   137 PHE   B H    
3704 H HA   . PHE   B 125 ? 0.385228 0.418788 0.814503 -0.0461166  0.085374    -0.147177   137 PHE   B HA   
3705 H HB2  . PHE   B 125 ? 0.353451 0.424028 0.741137 -0.0259299  0.061738    -0.147208   137 PHE   B HB2  
3706 H HB3  . PHE   B 125 ? 0.336841 0.43999  0.719823 -0.0373944  0.0596298   -0.162984   137 PHE   B HB3  
3707 H HD1  . PHE   B 125 ? 0.368544 0.453489 0.79472  -0.0153507  0.0613512   -0.187721   137 PHE   B HD1  
3708 H HD2  . PHE   B 125 ? 0.339224 0.507605 0.743009 -0.0424326  0.0495157   -0.227161   137 PHE   B HD2  
3709 H HE1  . PHE   B 125 ? 0.377485 0.513435 0.815304 -0.00983999 0.0586713   -0.240999   137 PHE   B HE1  
3710 H HE2  . PHE   B 125 ? 0.353228 0.569778 0.753919 -0.0335703  0.0403345   -0.277316   137 PHE   B HE2  
3711 H HZ   . PHE   B 125 ? 0.37505  0.573907 0.790605 -0.0189673  0.0494353   -0.284915   137 PHE   B HZ   
3712 N N    . LYS   B 126 ? 0.440298 0.415828 0.900276 -0.0297664  0.0933658   -0.138027   138 LYS   B N    
3713 C CA   . LYS   B 126 ? 0.496522 0.429346 0.982499 -0.0206206  0.101826    -0.131356   138 LYS   B CA   
3714 C C    . LYS   B 126 ? 0.499019 0.425843 0.954246 6.05e-06    0.0883677   -0.104251   138 LYS   B C    
3715 O O    . LYS   B 126 ? 0.472469 0.409924 0.885867 0.00420455  0.0779149   -0.0813809  138 LYS   B O    
3716 C CB   . LYS   B 126 ? 0.524327 0.40738  1.02879  -0.0291496  0.123005    -0.113454   138 LYS   B CB   
3717 H H    . LYS   B 126 ? 0.435646 0.409499 0.866978 -0.0274974  0.0901985   -0.116662   138 LYS   B H    
3718 H HA   . LYS   B 126 ? 0.492754 0.434935 1.00624  -0.0221284  0.10279     -0.158229   138 LYS   B HA   
3721 N N    . GLY   B 127 ? 0.520281 0.431097 1.0007   0.0131696   0.0881765   -0.109453   139 GLY   B N    
3722 C CA   . GLY   B 127 ? 0.568809 0.476264 1.03239  0.0340191   0.0744729   -0.0875765  139 GLY   B CA   
3723 C C    . GLY   B 127 ? 0.668156 0.534271 1.10141  0.0437114   0.0737126   -0.0448825  139 GLY   B C    
3724 O O    . GLY   B 127 ? 0.697849 0.523357 1.13502  0.037521    0.0903279   -0.0313862  139 GLY   B O    
3725 H H    . GLY   B 127 ? 0.542912 0.445567 1.05483  0.00932326  0.0965191   -0.128795   139 GLY   B H    
3726 H HA2  . GLY   B 127 ? 0.542574 0.483728 0.988229 0.0345382   0.0637199   -0.091402   139 GLY   B HA2  
3727 H HA3  . GLY   B 127 ? 0.584958 0.484479 1.07547  0.0422313   0.0763097   -0.0978813  139 GLY   B HA3  
3728 N N    . GLU   B 128 ? 0.717405 0.595156 1.12065  0.058985    0.0548454   -0.0249013  140 GLU   B N    
3729 C CA   . GLU   B 128 ? 0.792179 0.635572 1.15921  0.0729773   0.0486812   0.0139418   140 GLU   B CA   
3730 C C    . GLU   B 128 ? 0.848874 0.642195 1.23882  0.0904968   0.0555553   0.0288858   140 GLU   B C    
3731 O O    . GLU   B 128 ? 0.825253 0.620926 1.26154  0.0939657   0.0597588   0.00575951  140 GLU   B O    
3732 C CB   . GLU   B 128 ? 0.804088 0.678533 1.14105  0.0845248   0.0235024   0.0237857   140 GLU   B CB   
3733 O OXT  . GLU   B 128 ? 0.916981 0.668699 1.2754   0.101347    0.0574776   0.0634941   140 GLU   B OXT  
3734 H H    . GLU   B 128 ? 0.685066 0.59409  1.09048  0.0608522   0.045417    -0.0368735  140 GLU   B H    
3735 H HA   . GLU   B 128 ? 0.794675 0.625971 1.14241  0.0633656   0.0576089   0.0234783   140 GLU   B HA   
3738 C C4   . A1INN C .   ? 0.370837 0.500706 0.353569 -0.0392817  0.0607768   0.0284888   201 A1INN A C4   
3739 C C14  . A1INN C .   ? 0.328053 0.509313 0.313919 0.0204515   0.0408346   -0.0480113  201 A1INN A C14  
3740 C C5   . A1INN C .   ? 0.38314  0.543904 0.37744  -0.0522107  0.0698132   0.0336635   201 A1INN A C5   
3741 C C6   . A1INN C .   ? 0.403497 0.602607 0.392053 -0.0517586  0.0797582   0.039114    201 A1INN A C6   
3742 C C11  . A1INN C .   ? 0.383416 0.69137  0.390684 -0.021357   0.0844902   -0.0049614  201 A1INN A C11  
3743 C C7   . A1INN C .   ? 0.441185 0.683108 0.462011 -0.0822566  0.0905112   0.0451535   201 A1INN A C7   
3744 C C8   . A1INN C .   ? 0.390185 0.595365 0.360506 -0.0376513  0.0794568   0.0374976   201 A1INN A C8   
3745 C C9   . A1INN C .   ? 0.399268 0.67966  0.363972 -0.0200999  0.0872057   0.0174218   201 A1INN A C9   
3746 C C10  . A1INN C .   ? 0.404872 0.728696 0.390211 -0.0220365  0.0932897   0.00730191  201 A1INN A C10  
3747 C C12  . A1INN C .   ? 0.380633 0.613373 0.375238 -0.00177539 0.0619356   -0.0221043  201 A1INN A C12  
3748 C C13  . A1INN C .   ? 0.354487 0.57848  0.348705 0.0144634   0.0528836   -0.0418806  201 A1INN A C13  
3749 N N1   . A1INN C .   ? 0.378818 0.659113 0.382868 -0.00342633 0.071726    -0.0237338  201 A1INN A N1   
3750 N N2   . A1INN C .   ? 0.38563  0.649308 0.387889 0.025101    0.0570743   -0.0562348  201 A1INN A N2   
3751 C C3   . A1INN C .   ? 0.377264 0.514067 0.344036 -0.02725    0.0607295   0.0278724   201 A1INN A C3   
3752 N N3   . A1INN C .   ? 0.396604 0.699305 0.405754 0.0144813   0.069008    -0.0455777  201 A1INN A N3   
3753 C C1   . A1INN C .   ? 0.38     0.541509 0.313828 -0.00703012 0.0599425   0.0253145   201 A1INN A C1   
3754 O O1   . A1INN C .   ? 0.390666 0.577791 0.33441  -0.0154009  0.0692161   0.0290098   201 A1INN A O1   
3755 C C2   . A1INN C .   ? 0.391082 0.564562 0.351204 -0.0262428  0.0694795   0.0316106   201 A1INN A C2   
3756 O O2   . A1INN C .   ? 0.433041 0.671621 0.432409 -0.0651804  0.0904526   0.045575    201 A1INN A O2   
3757 O O3   . A1INN C .   ? 0.409898 0.658788 0.373344 -0.0365344  0.0893138   0.0408151   201 A1INN A O3   
3758 C C15  . A1INN C .   ? 0.318312 0.472116 0.292157 0.0105722   0.0399897   -0.0316458  201 A1INN A C15  
3759 O O4   . A1INN C .   ? 0.32005  0.456974 0.304047 0.00061402  0.039159    -0.0213277  201 A1INN A O4   
3760 C C16  . A1INN C .   ? 0.315984 0.42693  0.304096 0.0033626   0.0294703   -0.0267305  201 A1INN A C16  
3761 O O5   . A1INN C .   ? 0.329595 0.428651 0.314452 0.012221    0.0220101   -0.0372408  201 A1INN A O5   
3762 C C17  . A1INN C .   ? 0.310905 0.406761 0.306345 -0.00722786 0.0286124   -0.0177922  201 A1INN A C17  
3763 C C18  . A1INN C .   ? 0.333274 0.431239 0.34285  -0.00335177 0.0211412   -0.0277639  201 A1INN A C18  
3764 C C19  . A1INN C .   ? 0.328363 0.465777 0.354214 -0.00161516 0.0256483   -0.0345887  201 A1INN A C19  
3765 C C20  . A1INN C .   ? 0.336674 0.491107 0.369386 -0.0190859  0.0352615   -0.0233542  201 A1INN A C20  
3766 C C21  . A1INN C .   ? 0.345535 0.491623 0.361746 -0.025132   0.0437146   -0.00967508 201 A1INN A C21  
3767 N N4   . A1INN C .   ? 0.345436 0.45484  0.344671 -0.0199622  0.0382482   -0.00606216 201 A1INN A N4   
3768 C C22  . A1INN C .   ? 0.332761 0.422431 0.318959 -0.0253361  0.0417928   0.00815799  201 A1INN A C22  
3769 O O6   . A1INN C .   ? 0.338384 0.409156 0.311841 -0.018188   0.0375948   0.00940375  201 A1INN A O6   
3770 C C23  . A1INN C .   ? 0.360904 0.454508 0.348053 -0.0399829  0.0512546   0.023569    201 A1INN A C23  
3771 C C24  . A1INN C .   ? 0.366653 0.420789 0.340127 -0.0428213  0.0508548   0.0376378   201 A1INN A C24  
3772 C C25  . A1INN C .   ? 0.362631 0.386375 0.341395 -0.0460115  0.0432731   0.0314085   201 A1INN A C25  
3773 C C26  . A1INN C .   ? 0.385723 0.370808 0.349778 -0.0436436  0.0426927   0.0420813   201 A1INN A C26  
3774 C C27  . A1INN C .   ? 0.409245 0.381783 0.367625 -0.0549473  0.0510041   0.0602898   201 A1INN A C27  
3775 C C28  . A1INN C .   ? 0.43645  0.442406 0.390125 -0.0548039  0.0593623   0.070907    201 A1INN A C28  
3776 C C29  . A1INN C .   ? 0.398164 0.449101 0.366675 -0.0560251  0.0605676   0.0571364   201 A1INN A C29  
3777 H H17  . A1INN C .   ? 0.327136 0.496932 0.322299 0.022889    0.0352196   -0.0523129  201 A1INN A H17  
3778 H H16  . A1INN C .   ? 0.33793  0.521754 0.316763 0.0291775   0.0386296   -0.0592474  201 A1INN A H16  
3779 H H5   . A1INN C .   ? 0.388206 0.546427 0.394141 -0.0621321  0.0692927   0.0334551   201 A1INN A H5   
3780 H H14  . A1INN C .   ? 0.387093 0.670811 0.397089 -0.0332954  0.0831805   0.00615948  201 A1INN A H14  
3781 H H13  . A1INN C .   ? 0.386148 0.728267 0.407099 -0.0215418  0.0886189   -0.0109504  201 A1INN A H13  
3782 H H7   . A1INN C .   ? 0.446719 0.723477 0.475082 -0.0915987  0.0988236   0.0496505   201 A1INN A H7   
3783 H H8   . A1INN C .   ? 0.450325 0.658689 0.467375 -0.0924339  0.0890387   0.0552958   201 A1INN A H8   
3784 H H6   . A1INN C .   ? 0.422959 0.667196 0.454234 -0.0743113  0.0834953   0.0300488   201 A1INN A H6   
3785 H H9   . A1INN C .   ? 0.390464 0.648899 0.356051 -0.0117981  0.0781844   0.00563156  201 A1INN A H9   
3786 H H10  . A1INN C .   ? 0.409535 0.706505 0.360277 -0.0154393  0.0906377   0.0195045   201 A1INN A H10  
3787 H H12  . A1INN C .   ? 0.412358 0.753568 0.399666 -0.0350965  0.102069    0.0217829   201 A1INN A H12  
3788 H H11  . A1INN C .   ? 0.402596 0.75302  0.384936 -0.0103596  0.0946562   -0.00578477 201 A1INN A H11  
3789 H H15  . A1INN C .   ? 0.373963 0.584168 0.363181 -0.00980816 0.0615244   -0.0099221  201 A1INN A H15  
3790 H H4   . A1INN C .   ? 0.370933 0.490281 0.331196 -0.0205141  0.0547949   0.0247396   201 A1INN A H4   
3791 H H2   . A1INN C .   ? 0.385604 0.562401 0.308425 -0.00149298 0.060317    0.0238557   201 A1INN A H2   
3792 H H3   . A1INN C .   ? 0.370008 0.522324 0.311183 -0.00358299 0.0537024   0.0122379   201 A1INN A H3   
3793 H H1   . A1INN C .   ? 0.386013 0.525434 0.316497 -0.0103061  0.0593562   0.0372598   201 A1INN A H1   
3794 H H19  . A1INN C .   ? 0.321066 0.456591 0.288181 0.0143572   0.0335805   -0.0364412  201 A1INN A H19  
3795 H H18  . A1INN C .   ? 0.327689 0.494827 0.293608 0.00743131  0.0461968   -0.0236378  201 A1INN A H18  
3796 H H20  . A1INN C .   ? 0.320355 0.394491 0.307509 -0.00798189 0.0256792   -0.0132437  201 A1INN A H20  
3797 H H22  . A1INN C .   ? 0.324226 0.411007 0.329808 0.00501773  0.0150031   -0.0338164  201 A1INN A H22  
3798 H H21  . A1INN C .   ? 0.324419 0.410526 0.336337 -0.00988416 0.0190052   -0.0238144  201 A1INN A H21  
3799 H H23  . A1INN C .   ? 0.328031 0.468643 0.363011 0.00303929  0.0198351   -0.0408948  201 A1INN A H23  
3800 H H24  . A1INN C .   ? 0.333082 0.483211 0.355742 0.00635329  0.0279462   -0.0401808  201 A1INN A H24  
3801 H H25  . A1INN C .   ? 0.336026 0.477047 0.372529 -0.0269724  0.0321819   -0.0204846  201 A1INN A H25  
3802 H H26  . A1INN C .   ? 0.336725 0.522416 0.380836 -0.0191008  0.038998    -0.0273576  201 A1INN A H26  
3803 H H27  . A1INN C .   ? 0.353542 0.500094 0.372599 -0.037744   0.0486212   -0.00018992 201 A1INN A H27  
3804 H H28  . A1INN C .   ? 0.347541 0.515736 0.361555 -0.0198931  0.0481947   -0.0124032  201 A1INN A H28  
3805 H H29  . A1INN C .   ? 0.358274 0.458119 0.358135 -0.0481005  0.0512358   0.0206412   201 A1INN A H29  
3806 H H30  . A1INN C .   ? 0.365886 0.415967 0.328619 -0.0330515  0.0489247   0.038412    201 A1INN A H30  
3807 H H32  . A1INN C .   ? 0.369008 0.397501 0.358477 -0.0567327  0.0443771   0.0299105   201 A1INN A H32  
3808 H H31  . A1INN C .   ? 0.349092 0.375003 0.329827 -0.0383583  0.0373455   0.0213381   201 A1INN A H31  
3809 H H33  . A1INN C .   ? 0.377122 0.362511 0.33204  -0.0327293  0.04118     0.0431063   201 A1INN A H33  
3810 H H34  . A1INN C .   ? 0.384159 0.352011 0.350797 -0.0448942  0.0379697   0.0359596   201 A1INN A H34  
3811 H H35  . A1INN C .   ? 0.432008 0.377895 0.379553 -0.0496369  0.0499878   0.0670304   201 A1INN A H35  
3812 H H36  . A1INN C .   ? 0.425594 0.394409 0.393326 -0.0681249  0.0519399   0.0590215   201 A1INN A H36  
3813 H H37  . A1INN C .   ? 0.426937 0.433106 0.369306 -0.0431818  0.0583451   0.0740958   201 A1INN A H37  
3814 H H38  . A1INN C .   ? 0.450081 0.4492   0.401197 -0.0650292  0.0651394   0.0840641   201 A1INN A H38  
3815 H H40  . A1INN C .   ? 0.405077 0.462936 0.385247 -0.0681758  0.0628024   0.0563775   201 A1INN A H40  
3816 H H39  . A1INN C .   ? 0.402276 0.475046 0.365244 -0.0533675  0.0656058   0.0620187   201 A1INN A H39  
3817 C C4   . A1INN D .   ? 0.285044 0.366928 0.281462 0.0130928   0.0716694   0.0143289   201 A1INN B C4   
3818 C C14  . A1INN D .   ? 0.303723 0.310267 0.251456 0.00876193  0.0364932   0.0461534   201 A1INN B C14  
3819 C C5   . A1INN D .   ? 0.312412 0.395634 0.329749 0.00788558  0.093856    0.0143013   201 A1INN B C5   
3820 C C6   . A1INN D .   ? 0.337315 0.389801 0.324405 0.00920217  0.110747    0.0276248   201 A1INN B C6   
3821 C C11  . A1INN D .   ? 0.386432 0.377439 0.354796 -0.00035772 0.12391     0.057443    201 A1INN B C11  
3822 C C7   . A1INN D .   ? 0.378914 0.459305 0.443229 -0.00616049 0.147104    0.0173882   201 A1INN B C7   
3823 C C8   . A1INN D .   ? 0.355838 0.378168 0.290804 0.0165245   0.101174    0.0383016   201 A1INN B C8   
3824 C C9   . A1INN D .   ? 0.427025 0.394369 0.307185 0.0189011   0.113232    0.0646624   201 A1INN B C9   
3825 C C10  . A1INN D .   ? 0.430791 0.396635 0.345794 0.00940907  0.134339    0.0700715   201 A1INN B C10  
3826 C C12  . A1INN D .   ? 0.330842 0.334818 0.283774 0.00590118  0.0753923   0.0484704   201 A1INN B C12  
3827 C C13  . A1INN D .   ? 0.331293 0.326941 0.2813   0.00685778  0.0599651   0.0520597   201 A1INN B C13  
3828 N N1   . A1INN D .   ? 0.379376 0.367919 0.338192 0.00256732  0.0977573   0.057114    201 A1INN B N1   
3829 N N2   . A1INN D .   ? 0.366152 0.339713 0.318208 0.00604815  0.0717972   0.0634528   201 A1INN B N2   
3830 C C3   . A1INN D .   ? 0.292251 0.344266 0.244634 0.0177944   0.0641756   0.0245947   201 A1INN B C3   
3831 N N3   . A1INN D .   ? 0.390306 0.357996 0.347484 0.00253911  0.0959765   0.0672787   201 A1INN B N3   
3832 C C1   . A1INN D .   ? 0.33814  0.335223 0.204638 0.0282632   0.0467246   0.0370273   201 A1INN B C1   
3833 O O1   . A1INN D .   ? 0.344207 0.340648 0.220422 0.0259509   0.0674471   0.0419509   201 A1INN B O1   
3834 C C2   . A1INN D .   ? 0.334499 0.358322 0.255832 0.0201242   0.0767639   0.0349337   201 A1INN B C2   
3835 O O2   . A1INN D .   ? 0.379753 0.428191 0.383555 0.00360862  0.13749     0.0312976   201 A1INN B O2   
3836 O O3   . A1INN D .   ? 0.396811 0.389341 0.296171 0.0198341   0.117575    0.0513722   201 A1INN B O3   
3837 C C15  . A1INN D .   ? 0.295518 0.317156 0.235855 0.0103748   0.0295906   0.0381891   201 A1INN B C15  
3838 O O4   . A1INN D .   ? 0.270726 0.321395 0.243829 0.00644923  0.0353056   0.0264335   201 A1INN B O4   
3839 C C16  . A1INN D .   ? 0.261835 0.332289 0.255599 0.0036805   0.0251518   0.0182515   201 A1INN B C16  
3840 O O5   . A1INN D .   ? 0.280244 0.345869 0.271373 0.00321538  0.0148553   0.0203231   201 A1INN B O5   
3841 C C17  . A1INN D .   ? 0.260078 0.36192  0.279909 0.00289447  0.027559    0.00526535  201 A1INN B C17  
3842 C C18  . A1INN D .   ? 0.264368 0.384278 0.317278 -0.0031817  0.0267163   -0.00639017 201 A1INN B C18  
3843 C C19  . A1INN D .   ? 0.256176 0.365371 0.331188 -0.0098862  0.0409591   -0.00674691 201 A1INN B C19  
3844 C C20  . A1INN D .   ? 0.268573 0.387863 0.357816 -0.0113793  0.0544126   -0.0108465  201 A1INN B C20  
3845 C C21  . A1INN D .   ? 0.266554 0.371452 0.320983 -0.00373462 0.0576112   0.00106586  201 A1INN B C21  
3846 N N4   . A1INN D .   ? 0.255272 0.361216 0.282545 0.00385578  0.0412624   0.00354453  201 A1INN B N4   
3847 C C22  . A1INN D .   ? 0.264811 0.37051  0.274073 0.0115625   0.0408397   0.00561101  201 A1INN B C22  
3848 O O6   . A1INN D .   ? 0.283726 0.381425 0.26948  0.0166467   0.0297703   0.00977155  201 A1INN B O6   
3849 C C23  . A1INN D .   ? 0.272556 0.386186 0.294228 0.0137833   0.0566112   0.00242425  201 A1INN B C23  
3850 C C24  . A1INN D .   ? 0.274312 0.40074  0.289594 0.0250494   0.050756    -0.0009104  201 A1INN B C24  
3851 C C25  . A1INN D .   ? 0.249568 0.409197 0.28636  0.0286227   0.0368751   -0.0111345  201 A1INN B C25  
3852 C C26  . A1INN D .   ? 0.264447 0.432833 0.292901 0.0430792   0.0311687   -0.0109487  201 A1INN B C26  
3853 C C27  . A1INN D .   ? 0.268105 0.445027 0.312216 0.0488757   0.0445678   -0.0152718  201 A1INN B C27  
3854 C C28  . A1INN D .   ? 0.296379 0.441268 0.320191 0.0434497   0.0613825   -0.00727643 201 A1INN B C28  
3855 C C29  . A1INN D .   ? 0.276809 0.410624 0.304542 0.0292847   0.0674381   -0.00420618 201 A1INN B C29  
3856 H H17  . A1INN D .   ? 0.28964  0.308645 0.263495 0.00477723  0.0339185   0.0401794   201 A1INN B H17  
3857 H H16  . A1INN D .   ? 0.323434 0.314026 0.249535 0.0133991   0.0282735   0.0534402   201 A1INN B H16  
3858 H H5   . A1INN D .   ? 0.29515  0.400718 0.347059 0.00368437  0.0980056   0.00486175  201 A1INN B H5   
3859 H H14  . A1INN D .   ? 0.365751 0.382333 0.358111 -0.00251998 0.12207     0.0448595   201 A1INN B H14  
3860 H H13  . A1INN D .   ? 0.399202 0.38416  0.388331 -0.00659794 0.138133    0.060716    201 A1INN B H13  
3861 H H7   . A1INN D .   ? 0.392035 0.465268 0.46669  -0.0110103  0.168436    0.0217155   201 A1INN B H7   
3862 H H8   . A1INN D .   ? 0.356814 0.461323 0.436289 -0.00237199 0.141994    0.00699712  201 A1INN B H8   
3863 H H6   . A1INN D .   ? 0.35795  0.443317 0.438901 -0.011379   0.137669    0.013285    201 A1INN B H6   
3864 H H9   . A1INN D .   ? 0.405147 0.377144 0.288936 0.0185177   0.0944965   0.0615051   201 A1INN B H9   
3865 H H10  . A1INN D .   ? 0.455793 0.40109  0.296039 0.0256623   0.115191    0.073208    201 A1INN B H10  
3866 H H12  . A1INN D .   ? 0.439064 0.411002 0.36649  0.00699532  0.153368    0.0684554   201 A1INN B H12  
3867 H H11  . A1INN D .   ? 0.459693 0.400337 0.350217 0.012324    0.138035    0.0834563   201 A1INN B H11  
3868 H H15  . A1INN D .   ? 0.325267 0.341985 0.277109 0.00776124  0.0720578   0.0420315   201 A1INN B H15  
3869 H H4   . A1INN D .   ? 0.289501 0.340939 0.232532 0.0197879   0.0508389   0.0239065   201 A1INN B H4   
3870 H H2   . A1INN D .   ? 0.35816  0.336639 0.194914 0.0320167   0.0414477   0.0395636   201 A1INN B H2   
3871 H H3   . A1INN D .   ? 0.318811 0.32394  0.200569 0.0240741   0.037317    0.036391    201 A1INN B H3   
3872 H H1   . A1INN D .   ? 0.327238 0.335004 0.202239 0.0306112   0.0477433   0.0314304   201 A1INN B H1   
3873 H H19  . A1INN D .   ? 0.28761  0.31061  0.223089 0.0111647   0.016544    0.0369583   201 A1INN B H19  
3874 H H18  . A1INN D .   ? 0.311774 0.321537 0.229176 0.014294    0.0340811   0.0419777   201 A1INN B H18  
3875 H H20  . A1INN D .   ? 0.251537 0.359996 0.261844 0.00665024  0.0198475   0.00464746  201 A1INN B H20  
3876 H H22  . A1INN D .   ? 0.252128 0.368414 0.300359 -0.00321698 0.0195248   -0.00476171 201 A1INN B H22  
3877 H H21  . A1INN D .   ? 0.245056 0.387585 0.310631 -0.00223551 0.0242575   -0.0162464  201 A1INN B H21  
3878 H H23  . A1INN D .   ? 0.255038 0.374242 0.352823 -0.0138858  0.0400768   -0.0161747  201 A1INN B H23  
3879 H H24  . A1INN D .   ? 0.276843 0.362373 0.335484 -0.00886587 0.0430544   0.00476024  201 A1INN B H24  
3880 H H25  . A1INN D .   ? 0.249842 0.394998 0.357974 -0.0114562  0.050207    -0.0234878  201 A1INN B H25  
3881 H H26  . A1INN D .   ? 0.273679 0.384175 0.378841 -0.0169905  0.0664302   -0.0100529  201 A1INN B H26  
3882 H H27  . A1INN D .   ? 0.268693 0.386696 0.337536 -0.00368614 0.0655693   -0.00424082 201 A1INN B H27  
3883 H H28  . A1INN D .   ? 0.287361 0.368105 0.324209 -0.00371265 0.0641153   0.0119607   201 A1INN B H28  
3884 H H29  . A1INN D .   ? 0.261946 0.393779 0.314313 0.00886306  0.0615061   -0.00582151 201 A1INN B H29  
3885 H H30  . A1INN D .   ? 0.279569 0.386995 0.267179 0.0287259   0.0451736   0.00577169  201 A1INN B H30  
3886 H H32  . A1INN D .   ? 0.245215 0.425285 0.310811 0.0245817   0.0402185   -0.0205487  201 A1INN B H32  
3887 H H31  . A1INN D .   ? 0.247826 0.40271  0.275341 0.0263525   0.0284055   -0.00879053 201 A1INN B H31  
3888 H H33  . A1INN D .   ? 0.269323 0.416179 0.271466 0.0459392   0.0275574   -0.00267226 201 A1INN B H33  
3889 H H34  . A1INN D .   ? 0.252574 0.442436 0.291661 0.0469214   0.0220716   -0.0164184  201 A1INN B H34  
3890 H H35  . A1INN D .   ? 0.277461 0.455986 0.314061 0.0597808   0.0402334   -0.0140635  201 A1INN B H35  
3891 H H36  . A1INN D .   ? 0.262901 0.465367 0.33861  0.0461747   0.047199    -0.0251042  201 A1INN B H36  
3892 H H37  . A1INN D .   ? 0.301811 0.424174 0.296039 0.0474105   0.0573942   -0.00055678 201 A1INN B H37  
3893 H H38  . A1INN D .   ? 0.297437 0.450083 0.334112 0.0464289   0.0730851   -0.0107849  201 A1INN B H38  
3894 H H40  . A1INN D .   ? 0.275638 0.429009 0.335035 0.0242617   0.0737357   -0.0117639  201 A1INN B H40  
3895 H H39  . A1INN D .   ? 0.300957 0.41262  0.309271 0.0283176   0.0773179   0.00283837  201 A1INN B H39  
# 
