data_9GPX
# 
_entry.id   9GPX 
# 
_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   9GPX         pdb_00009gpx 10.2210/pdb9gpx/pdb 
WWPDB D_1292141194 ?            ?                   
# 
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                        9GPX 
_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-17-hydroxy-16,17-dimethoxy-12-methyl-15,18-dioxa-5-aza-1lambda5,17lambda5-diphosphapentacyclo[17.3.1.01,10.05,10.011,19]tricosa-10,19(23)-diene-4,11-quinone
;
582.731   2   ?       ?                    ? ? 
3 water       nat water 18.015    109 ?       ?                    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;PPIase FKBP5,51 kDa FK506-binding protein,FKBP-51,54 kDa progesterone receptor-associated immunophilin,Androgen-regulated protein 6,FF1 antigen,FK506-binding protein 5,FKBP-5,FKBP54,p54,HSP90-binding immunophilin,Rotamase
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GAPATVTEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDI
GVATMKKGEIAHLLIKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAPATVTEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDI
GVATMKKGEIAHLLIKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGE
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;3-cyclohexyl-17-hydroxy-16,17-dimethoxy-12-methyl-15,18-dioxa-5-aza-1lambda5,17lambda5-diphosphapentacyclo[17.3.1.01,10.05,10.011,19]tricosa-10,19(23)-diene-4,11-quinone
;
A1INX 
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 
A1INX non-polymer         . 
;3-cyclohexyl-17-hydroxy-16,17-dimethoxy-12-methyl-15,18-dioxa-5-aza-1lambda5,17lambda5-diphosphapentacyclo[17.3.1.01,10.05,10.011,19]tricosa-10,19(23)-diene-4,11-quinone
;
? 'C32 H46 N4 O6'  582.731 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   13  13  GLY GLY B . n 
A 1 2   ALA 2   14  14  ALA ALA B . n 
A 1 3   PRO 3   15  15  PRO PRO B . n 
A 1 4   ALA 4   16  16  ALA ALA B . n 
A 1 5   THR 5   17  17  THR THR B . n 
A 1 6   VAL 6   18  18  VAL VAL B . n 
A 1 7   THR 7   19  19  THR THR B . n 
A 1 8   GLU 8   20  20  GLU GLU B . n 
A 1 9   GLN 9   21  21  GLN GLN B . n 
A 1 10  GLY 10  22  22  GLY GLY B . n 
A 1 11  GLU 11  23  23  GLU GLU B . n 
A 1 12  ASP 12  24  24  ASP ASP B . n 
A 1 13  ILE 13  25  25  ILE ILE B . n 
A 1 14  THR 14  26  26  THR THR B . n 
A 1 15  SER 15  27  27  SER SER B . n 
A 1 16  LYS 16  28  28  LYS LYS B . n 
A 1 17  LYS 17  29  29  LYS LYS B . n 
A 1 18  ASP 18  30  30  ASP ASP B . n 
A 1 19  ARG 19  31  31  ARG ARG B . n 
A 1 20  GLY 20  32  32  GLY GLY B . n 
A 1 21  VAL 21  33  33  VAL VAL B . n 
A 1 22  LEU 22  34  34  LEU LEU B . n 
A 1 23  LYS 23  35  35  LYS LYS B . n 
A 1 24  ILE 24  36  36  ILE ILE B . n 
A 1 25  VAL 25  37  37  VAL VAL B . n 
A 1 26  LYS 26  38  38  LYS LYS B . n 
A 1 27  ARG 27  39  39  ARG ARG B . n 
A 1 28  VAL 28  40  40  VAL VAL B . n 
A 1 29  GLY 29  41  41  GLY GLY B . n 
A 1 30  ASN 30  42  42  ASN ASN B . n 
A 1 31  GLY 31  43  43  GLY GLY B . n 
A 1 32  GLU 32  44  44  GLU GLU B . n 
A 1 33  GLU 33  45  45  GLU GLU B . n 
A 1 34  THR 34  46  46  THR THR B . n 
A 1 35  PRO 35  47  47  PRO PRO B . n 
A 1 36  MET 36  48  48  MET MET B . n 
A 1 37  ILE 37  49  49  ILE ILE B . n 
A 1 38  GLY 38  50  50  GLY GLY B . n 
A 1 39  ASP 39  51  51  ASP ASP B . n 
A 1 40  LYS 40  52  52  LYS LYS B . n 
A 1 41  VAL 41  53  53  VAL VAL B . n 
A 1 42  TYR 42  54  54  TYR TYR B . n 
A 1 43  VAL 43  55  55  VAL VAL B . n 
A 1 44  HIS 44  56  56  HIS HIS B . n 
A 1 45  TYR 45  57  57  TYR TYR B . n 
A 1 46  LYS 46  58  58  LYS LYS B . n 
A 1 47  GLY 47  59  59  GLY GLY B . n 
A 1 48  LYS 48  60  60  LYS LYS B . n 
A 1 49  LEU 49  61  61  LEU LEU B . n 
A 1 50  SER 50  62  62  SER SER B . n 
A 1 51  ASN 51  63  63  ASN ASN B . n 
A 1 52  GLY 52  64  64  GLY GLY B . n 
A 1 53  LYS 53  65  65  LYS LYS B . n 
A 1 54  LYS 54  66  66  LYS LYS B . n 
A 1 55  PHE 55  67  67  PHE PHE B . n 
A 1 56  ASP 56  68  68  ASP ASP B . n 
A 1 57  SER 57  69  69  SER SER B . n 
A 1 58  SER 58  70  70  SER SER B . n 
A 1 59  HIS 59  71  71  HIS HIS B . n 
A 1 60  ASP 60  72  72  ASP ASP B . n 
A 1 61  ARG 61  73  73  ARG ARG B . n 
A 1 62  ASN 62  74  74  ASN ASN B . n 
A 1 63  GLU 63  75  75  GLU GLU B . n 
A 1 64  PRO 64  76  76  PRO PRO B . n 
A 1 65  PHE 65  77  77  PHE PHE B . n 
A 1 66  VAL 66  78  78  VAL VAL B . n 
A 1 67  PHE 67  79  79  PHE PHE B . n 
A 1 68  SER 68  80  80  SER SER B . n 
A 1 69  LEU 69  81  81  LEU LEU B . n 
A 1 70  GLY 70  82  82  GLY GLY B . n 
A 1 71  LYS 71  83  83  LYS LYS B . n 
A 1 72  GLY 72  84  84  GLY GLY B . n 
A 1 73  GLN 73  85  85  GLN GLN B . n 
A 1 74  VAL 74  86  86  VAL VAL B . n 
A 1 75  ILE 75  87  87  ILE ILE B . n 
A 1 76  LYS 76  88  88  LYS LYS B . n 
A 1 77  ALA 77  89  89  ALA ALA B . n 
A 1 78  TRP 78  90  90  TRP TRP B . n 
A 1 79  ASP 79  91  91  ASP ASP B . n 
A 1 80  ILE 80  92  92  ILE ILE B . n 
A 1 81  GLY 81  93  93  GLY GLY B . n 
A 1 82  VAL 82  94  94  VAL VAL B . n 
A 1 83  ALA 83  95  95  ALA ALA B . n 
A 1 84  THR 84  96  96  THR THR B . n 
A 1 85  MET 85  97  97  MET MET B . n 
A 1 86  LYS 86  98  98  LYS LYS B . n 
A 1 87  LYS 87  99  99  LYS LYS B . n 
A 1 88  GLY 88  100 100 GLY GLY B . n 
A 1 89  GLU 89  101 101 GLU GLU B . n 
A 1 90  ILE 90  102 102 ILE ILE B . n 
A 1 91  ALA 91  103 103 ALA ALA B . n 
A 1 92  HIS 92  104 104 HIS HIS B . n 
A 1 93  LEU 93  105 105 LEU LEU B . n 
A 1 94  LEU 94  106 106 LEU LEU B . n 
A 1 95  ILE 95  107 107 ILE ILE B . n 
A 1 96  LYS 96  108 108 LYS LYS B . n 
A 1 97  PRO 97  109 109 PRO PRO B . n 
A 1 98  GLU 98  110 110 GLU GLU B . n 
A 1 99  TYR 99  111 111 TYR TYR B . n 
A 1 100 ALA 100 112 112 ALA ALA B . n 
A 1 101 TYR 101 113 113 TYR TYR B . n 
A 1 102 GLY 102 114 114 GLY GLY B . n 
A 1 103 SER 103 115 115 SER SER B . n 
A 1 104 ALA 104 116 116 ALA ALA B . n 
A 1 105 GLY 105 117 117 GLY GLY B . n 
A 1 106 SER 106 118 118 SER SER B . n 
A 1 107 LEU 107 119 119 LEU LEU B . n 
A 1 108 PRO 108 120 120 PRO PRO B . n 
A 1 109 LYS 109 121 121 LYS LYS B . n 
A 1 110 ILE 110 122 122 ILE ILE B . n 
A 1 111 PRO 111 123 123 PRO PRO B . n 
A 1 112 SER 112 124 124 SER SER B . n 
A 1 113 ASN 113 125 125 ASN ASN B . n 
A 1 114 ALA 114 126 126 ALA ALA B . n 
A 1 115 THR 115 127 127 THR THR B . n 
A 1 116 LEU 116 128 128 LEU LEU B . n 
A 1 117 PHE 117 129 129 PHE PHE B . n 
A 1 118 PHE 118 130 130 PHE PHE B . n 
A 1 119 GLU 119 131 131 GLU GLU B . n 
A 1 120 ILE 120 132 132 ILE ILE B . n 
A 1 121 GLU 121 133 133 GLU GLU B . n 
A 1 122 LEU 122 134 134 LEU LEU B . n 
A 1 123 LEU 123 135 135 LEU LEU B . n 
A 1 124 ASP 124 136 136 ASP ASP B . n 
A 1 125 PHE 125 137 137 PHE PHE B . n 
A 1 126 LYS 126 138 138 LYS LYS B . n 
A 1 127 GLY 127 139 139 GLY GLY B . n 
A 1 128 GLU 128 140 140 GLU GLU B . n 
B 1 1   GLY 1   13  13  GLY GLY A . n 
B 1 2   ALA 2   14  14  ALA ALA A . n 
B 1 3   PRO 3   15  15  PRO PRO A . n 
B 1 4   ALA 4   16  16  ALA ALA A . n 
B 1 5   THR 5   17  17  THR THR A . n 
B 1 6   VAL 6   18  18  VAL VAL A . n 
B 1 7   THR 7   19  19  THR THR A . n 
B 1 8   GLU 8   20  20  GLU GLU A . n 
B 1 9   GLN 9   21  21  GLN GLN A . n 
B 1 10  GLY 10  22  22  GLY GLY A . n 
B 1 11  GLU 11  23  23  GLU GLU A . n 
B 1 12  ASP 12  24  24  ASP ASP A . n 
B 1 13  ILE 13  25  25  ILE ILE A . n 
B 1 14  THR 14  26  26  THR THR A . n 
B 1 15  SER 15  27  27  SER SER A . n 
B 1 16  LYS 16  28  28  LYS LYS A . n 
B 1 17  LYS 17  29  29  LYS LYS A . n 
B 1 18  ASP 18  30  30  ASP ASP A . n 
B 1 19  ARG 19  31  31  ARG ARG A . n 
B 1 20  GLY 20  32  32  GLY GLY A . n 
B 1 21  VAL 21  33  33  VAL VAL A . n 
B 1 22  LEU 22  34  34  LEU LEU A . n 
B 1 23  LYS 23  35  35  LYS LYS A . n 
B 1 24  ILE 24  36  36  ILE ILE A . n 
B 1 25  VAL 25  37  37  VAL VAL A . n 
B 1 26  LYS 26  38  38  LYS LYS A . n 
B 1 27  ARG 27  39  39  ARG ARG A . n 
B 1 28  VAL 28  40  40  VAL VAL A . n 
B 1 29  GLY 29  41  41  GLY GLY A . n 
B 1 30  ASN 30  42  42  ASN ASN A . n 
B 1 31  GLY 31  43  43  GLY GLY A . n 
B 1 32  GLU 32  44  44  GLU GLU A . n 
B 1 33  GLU 33  45  45  GLU GLU A . n 
B 1 34  THR 34  46  46  THR THR A . n 
B 1 35  PRO 35  47  47  PRO PRO A . n 
B 1 36  MET 36  48  48  MET MET A . n 
B 1 37  ILE 37  49  49  ILE ILE A . n 
B 1 38  GLY 38  50  50  GLY GLY A . n 
B 1 39  ASP 39  51  51  ASP ASP A . n 
B 1 40  LYS 40  52  52  LYS LYS A . n 
B 1 41  VAL 41  53  53  VAL VAL A . n 
B 1 42  TYR 42  54  54  TYR TYR A . n 
B 1 43  VAL 43  55  55  VAL VAL A . n 
B 1 44  HIS 44  56  56  HIS HIS A . n 
B 1 45  TYR 45  57  57  TYR TYR A . n 
B 1 46  LYS 46  58  58  LYS LYS A . n 
B 1 47  GLY 47  59  59  GLY GLY A . n 
B 1 48  LYS 48  60  60  LYS LYS A . n 
B 1 49  LEU 49  61  61  LEU LEU A . n 
B 1 50  SER 50  62  62  SER SER A . n 
B 1 51  ASN 51  63  63  ASN ASN A . n 
B 1 52  GLY 52  64  64  GLY GLY A . n 
B 1 53  LYS 53  65  65  LYS LYS A . n 
B 1 54  LYS 54  66  66  LYS LYS A . n 
B 1 55  PHE 55  67  67  PHE PHE A . n 
B 1 56  ASP 56  68  68  ASP ASP A . n 
B 1 57  SER 57  69  69  SER SER A . n 
B 1 58  SER 58  70  70  SER SER A . n 
B 1 59  HIS 59  71  71  HIS HIS A . n 
B 1 60  ASP 60  72  72  ASP ASP A . n 
B 1 61  ARG 61  73  73  ARG ARG A . n 
B 1 62  ASN 62  74  74  ASN ASN A . n 
B 1 63  GLU 63  75  75  GLU GLU A . n 
B 1 64  PRO 64  76  76  PRO PRO A . n 
B 1 65  PHE 65  77  77  PHE PHE A . n 
B 1 66  VAL 66  78  78  VAL VAL A . n 
B 1 67  PHE 67  79  79  PHE PHE A . n 
B 1 68  SER 68  80  80  SER SER A . n 
B 1 69  LEU 69  81  81  LEU LEU A . n 
B 1 70  GLY 70  82  82  GLY GLY A . n 
B 1 71  LYS 71  83  83  LYS LYS A . n 
B 1 72  GLY 72  84  84  GLY GLY A . n 
B 1 73  GLN 73  85  85  GLN GLN A . n 
B 1 74  VAL 74  86  86  VAL VAL A . n 
B 1 75  ILE 75  87  87  ILE ILE A . n 
B 1 76  LYS 76  88  88  LYS LYS A . n 
B 1 77  ALA 77  89  89  ALA ALA A . n 
B 1 78  TRP 78  90  90  TRP TRP A . n 
B 1 79  ASP 79  91  91  ASP ASP A . n 
B 1 80  ILE 80  92  92  ILE ILE A . n 
B 1 81  GLY 81  93  93  GLY GLY A . n 
B 1 82  VAL 82  94  94  VAL VAL A . n 
B 1 83  ALA 83  95  95  ALA ALA A . n 
B 1 84  THR 84  96  96  THR THR A . n 
B 1 85  MET 85  97  97  MET MET A . n 
B 1 86  LYS 86  98  98  LYS LYS A . n 
B 1 87  LYS 87  99  99  LYS LYS A . n 
B 1 88  GLY 88  100 100 GLY GLY A . n 
B 1 89  GLU 89  101 101 GLU GLU A . n 
B 1 90  ILE 90  102 102 ILE ILE A . n 
B 1 91  ALA 91  103 103 ALA ALA A . n 
B 1 92  HIS 92  104 104 HIS HIS A . n 
B 1 93  LEU 93  105 105 LEU LEU A . n 
B 1 94  LEU 94  106 106 LEU LEU A . n 
B 1 95  ILE 95  107 107 ILE ILE A . n 
B 1 96  LYS 96  108 108 LYS LYS A . n 
B 1 97  PRO 97  109 109 PRO PRO A . n 
B 1 98  GLU 98  110 110 GLU GLU A . n 
B 1 99  TYR 99  111 111 TYR TYR A . n 
B 1 100 ALA 100 112 112 ALA ALA A . n 
B 1 101 TYR 101 113 113 TYR TYR A . n 
B 1 102 GLY 102 114 114 GLY GLY A . n 
B 1 103 SER 103 115 115 SER SER A . n 
B 1 104 ALA 104 116 116 ALA ALA A . n 
B 1 105 GLY 105 117 117 GLY GLY A . n 
B 1 106 SER 106 118 118 SER SER A . n 
B 1 107 LEU 107 119 119 LEU LEU A . n 
B 1 108 PRO 108 120 120 PRO PRO A . n 
B 1 109 LYS 109 121 121 LYS LYS A . n 
B 1 110 ILE 110 122 122 ILE ILE A . n 
B 1 111 PRO 111 123 123 PRO PRO A . n 
B 1 112 SER 112 124 124 SER SER A . n 
B 1 113 ASN 113 125 125 ASN ASN A . n 
B 1 114 ALA 114 126 126 ALA ALA A . n 
B 1 115 THR 115 127 127 THR THR A . n 
B 1 116 LEU 116 128 128 LEU LEU A . n 
B 1 117 PHE 117 129 129 PHE PHE A . n 
B 1 118 PHE 118 130 130 PHE PHE A . n 
B 1 119 GLU 119 131 131 GLU GLU A . n 
B 1 120 ILE 120 132 132 ILE ILE A . n 
B 1 121 GLU 121 133 133 GLU GLU A . n 
B 1 122 LEU 122 134 134 LEU LEU A . n 
B 1 123 LEU 123 135 135 LEU LEU A . n 
B 1 124 ASP 124 136 136 ASP ASP A . n 
B 1 125 PHE 125 137 137 PHE PHE A . n 
B 1 126 LYS 126 138 138 LYS LYS A . n 
B 1 127 GLY 127 139 139 GLY GLY A . n 
B 1 128 GLU 128 140 140 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1INX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1INX 
_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 A1INX 1  201 201 A1INX DRG B . 
D 2 A1INX 1  201 201 A1INX DRG A . 
E 3 HOH   1  301 78  HOH   HOH B . 
E 3 HOH   2  302 47  HOH   HOH B . 
E 3 HOH   3  303 50  HOH   HOH B . 
E 3 HOH   4  304 74  HOH   HOH B . 
E 3 HOH   5  305 69  HOH   HOH B . 
E 3 HOH   6  306 14  HOH   HOH B . 
E 3 HOH   7  307 66  HOH   HOH B . 
E 3 HOH   8  308 17  HOH   HOH B . 
E 3 HOH   9  309 2   HOH   HOH B . 
E 3 HOH   10 310 38  HOH   HOH B . 
E 3 HOH   11 311 13  HOH   HOH B . 
E 3 HOH   12 312 42  HOH   HOH B . 
E 3 HOH   13 313 9   HOH   HOH B . 
E 3 HOH   14 314 41  HOH   HOH B . 
E 3 HOH   15 315 68  HOH   HOH B . 
E 3 HOH   16 316 15  HOH   HOH B . 
E 3 HOH   17 317 44  HOH   HOH B . 
E 3 HOH   18 318 28  HOH   HOH B . 
E 3 HOH   19 319 58  HOH   HOH B . 
E 3 HOH   20 320 5   HOH   HOH B . 
E 3 HOH   21 321 37  HOH   HOH B . 
E 3 HOH   22 322 22  HOH   HOH B . 
E 3 HOH   23 323 75  HOH   HOH B . 
E 3 HOH   24 324 46  HOH   HOH B . 
E 3 HOH   25 325 45  HOH   HOH B . 
E 3 HOH   26 326 88  HOH   HOH B . 
E 3 HOH   27 327 21  HOH   HOH B . 
E 3 HOH   28 328 60  HOH   HOH B . 
E 3 HOH   29 329 53  HOH   HOH B . 
E 3 HOH   30 330 91  HOH   HOH B . 
E 3 HOH   31 331 43  HOH   HOH B . 
E 3 HOH   32 332 82  HOH   HOH B . 
E 3 HOH   33 333 10  HOH   HOH B . 
E 3 HOH   34 334 81  HOH   HOH B . 
E 3 HOH   35 335 94  HOH   HOH B . 
E 3 HOH   36 336 96  HOH   HOH B . 
E 3 HOH   37 337 36  HOH   HOH B . 
E 3 HOH   38 338 4   HOH   HOH B . 
E 3 HOH   39 339 39  HOH   HOH B . 
E 3 HOH   40 340 64  HOH   HOH B . 
E 3 HOH   41 341 93  HOH   HOH B . 
E 3 HOH   42 342 27  HOH   HOH B . 
E 3 HOH   43 343 87  HOH   HOH B . 
E 3 HOH   44 344 101 HOH   HOH B . 
E 3 HOH   45 345 18  HOH   HOH B . 
E 3 HOH   46 346 80  HOH   HOH B . 
E 3 HOH   47 347 89  HOH   HOH B . 
E 3 HOH   48 348 104 HOH   HOH B . 
E 3 HOH   49 349 98  HOH   HOH B . 
F 3 HOH   1  301 35  HOH   HOH A . 
F 3 HOH   2  302 97  HOH   HOH A . 
F 3 HOH   3  303 99  HOH   HOH A . 
F 3 HOH   4  304 107 HOH   HOH A . 
F 3 HOH   5  305 29  HOH   HOH A . 
F 3 HOH   6  306 70  HOH   HOH A . 
F 3 HOH   7  307 67  HOH   HOH A . 
F 3 HOH   8  308 26  HOH   HOH A . 
F 3 HOH   9  309 52  HOH   HOH A . 
F 3 HOH   10 310 30  HOH   HOH A . 
F 3 HOH   11 311 31  HOH   HOH A . 
F 3 HOH   12 312 20  HOH   HOH A . 
F 3 HOH   13 313 16  HOH   HOH A . 
F 3 HOH   14 314 49  HOH   HOH A . 
F 3 HOH   15 315 105 HOH   HOH A . 
F 3 HOH   16 316 110 HOH   HOH A . 
F 3 HOH   17 317 6   HOH   HOH A . 
F 3 HOH   18 318 77  HOH   HOH A . 
F 3 HOH   19 319 84  HOH   HOH A . 
F 3 HOH   20 320 63  HOH   HOH A . 
F 3 HOH   21 321 76  HOH   HOH A . 
F 3 HOH   22 322 19  HOH   HOH A . 
F 3 HOH   23 323 11  HOH   HOH A . 
F 3 HOH   24 324 95  HOH   HOH A . 
F 3 HOH   25 325 24  HOH   HOH A . 
F 3 HOH   26 326 92  HOH   HOH A . 
F 3 HOH   27 327 61  HOH   HOH A . 
F 3 HOH   28 328 33  HOH   HOH A . 
F 3 HOH   29 329 23  HOH   HOH A . 
F 3 HOH   30 330 85  HOH   HOH A . 
F 3 HOH   31 331 57  HOH   HOH A . 
F 3 HOH   32 332 32  HOH   HOH A . 
F 3 HOH   33 333 72  HOH   HOH A . 
F 3 HOH   34 334 40  HOH   HOH A . 
F 3 HOH   35 335 34  HOH   HOH A . 
F 3 HOH   36 336 48  HOH   HOH A . 
F 3 HOH   37 337 83  HOH   HOH A . 
F 3 HOH   38 338 8   HOH   HOH A . 
F 3 HOH   39 339 59  HOH   HOH A . 
F 3 HOH   40 340 25  HOH   HOH A . 
F 3 HOH   41 341 54  HOH   HOH A . 
F 3 HOH   42 342 1   HOH   HOH A . 
F 3 HOH   43 343 51  HOH   HOH A . 
F 3 HOH   44 344 7   HOH   HOH A . 
F 3 HOH   45 345 55  HOH   HOH A . 
F 3 HOH   46 346 100 HOH   HOH A . 
F 3 HOH   47 347 65  HOH   HOH A . 
F 3 HOH   48 348 3   HOH   HOH A . 
F 3 HOH   49 349 62  HOH   HOH A . 
F 3 HOH   50 350 108 HOH   HOH A . 
F 3 HOH   51 351 103 HOH   HOH A . 
F 3 HOH   52 352 86  HOH   HOH A . 
F 3 HOH   53 353 90  HOH   HOH A . 
F 3 HOH   54 354 106 HOH   HOH A . 
F 3 HOH   55 355 56  HOH   HOH A . 
F 3 HOH   56 356 73  HOH   HOH A . 
F 3 HOH   57 357 102 HOH   HOH A . 
F 3 HOH   58 358 71  HOH   HOH A . 
F 3 HOH   59 359 12  HOH   HOH A . 
F 3 HOH   60 360 109 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 B GLU 20  ? CG  ? A GLU 8   CG  
2   1 Y 1 B GLU 20  ? CD  ? A GLU 8   CD  
3   1 Y 1 B GLU 20  ? OE1 ? A GLU 8   OE1 
4   1 Y 1 B GLU 20  ? OE2 ? A GLU 8   OE2 
5   1 Y 1 B ASN 42  ? CG  ? A ASN 30  CG  
6   1 Y 1 B ASN 42  ? OD1 ? A ASN 30  OD1 
7   1 Y 1 B ASN 42  ? ND2 ? A ASN 30  ND2 
8   1 Y 1 B GLU 44  ? CG  ? A GLU 32  CG  
9   1 Y 1 B GLU 44  ? CD  ? A GLU 32  CD  
10  1 Y 1 B GLU 44  ? OE1 ? A GLU 32  OE1 
11  1 Y 1 B GLU 44  ? OE2 ? A GLU 32  OE2 
12  1 Y 1 B GLU 45  ? CG  ? A GLU 33  CG  
13  1 Y 1 B GLU 45  ? CD  ? A GLU 33  CD  
14  1 Y 1 B GLU 45  ? OE1 ? A GLU 33  OE1 
15  1 Y 1 B GLU 45  ? OE2 ? A GLU 33  OE2 
16  1 Y 1 B LYS 58  ? CG  ? A LYS 46  CG  
17  1 Y 1 B LYS 58  ? CD  ? A LYS 46  CD  
18  1 Y 1 B LYS 58  ? CE  ? A LYS 46  CE  
19  1 Y 1 B LYS 58  ? NZ  ? A LYS 46  NZ  
20  1 Y 1 B ASN 63  ? CG  ? A ASN 51  CG  
21  1 Y 1 B ASN 63  ? OD1 ? A ASN 51  OD1 
22  1 Y 1 B ASN 63  ? ND2 ? A ASN 51  ND2 
23  1 Y 1 B LYS 65  ? CG  ? A LYS 53  CG  
24  1 Y 1 B LYS 65  ? CD  ? A LYS 53  CD  
25  1 Y 1 B LYS 65  ? CE  ? A LYS 53  CE  
26  1 Y 1 B LYS 65  ? NZ  ? A LYS 53  NZ  
27  1 Y 1 B LYS 66  ? CG  ? A LYS 54  CG  
28  1 Y 1 B LYS 66  ? CD  ? A LYS 54  CD  
29  1 Y 1 B LYS 66  ? CE  ? A LYS 54  CE  
30  1 Y 1 B LYS 66  ? NZ  ? A LYS 54  NZ  
31  1 Y 1 B ASN 74  ? CG  ? A ASN 62  CG  
32  1 Y 1 B ASN 74  ? OD1 ? A ASN 62  OD1 
33  1 Y 1 B ASN 74  ? ND2 ? A ASN 62  ND2 
34  1 Y 1 B LYS 83  ? CG  ? A LYS 71  CG  
35  1 Y 1 B LYS 83  ? CD  ? A LYS 71  CD  
36  1 Y 1 B LYS 83  ? CE  ? A LYS 71  CE  
37  1 Y 1 B LYS 83  ? NZ  ? A LYS 71  NZ  
38  1 Y 1 B LYS 88  ? CG  ? A LYS 76  CG  
39  1 Y 1 B LYS 88  ? CD  ? A LYS 76  CD  
40  1 Y 1 B LYS 88  ? CE  ? A LYS 76  CE  
41  1 Y 1 B LYS 88  ? NZ  ? A LYS 76  NZ  
42  1 Y 1 B LYS 98  ? CG  ? A LYS 86  CG  
43  1 Y 1 B LYS 98  ? CD  ? A LYS 86  CD  
44  1 Y 1 B LYS 98  ? CE  ? A LYS 86  CE  
45  1 Y 1 B LYS 98  ? NZ  ? A LYS 86  NZ  
46  1 Y 1 B LYS 138 ? CG  ? A LYS 126 CG  
47  1 Y 1 B LYS 138 ? CD  ? A LYS 126 CD  
48  1 Y 1 B LYS 138 ? CE  ? A LYS 126 CE  
49  1 Y 1 B LYS 138 ? NZ  ? A LYS 126 NZ  
50  1 Y 1 B GLU 140 ? CG  ? A GLU 128 CG  
51  1 Y 1 B GLU 140 ? CD  ? A GLU 128 CD  
52  1 Y 1 B GLU 140 ? OE1 ? A GLU 128 OE1 
53  1 Y 1 B GLU 140 ? OE2 ? A GLU 128 OE2 
54  1 Y 1 A GLU 20  ? CG  ? B GLU 8   CG  
55  1 Y 1 A GLU 20  ? CD  ? B GLU 8   CD  
56  1 Y 1 A GLU 20  ? OE1 ? B GLU 8   OE1 
57  1 Y 1 A GLU 20  ? OE2 ? B GLU 8   OE2 
58  1 Y 1 A GLN 21  ? CG  ? B GLN 9   CG  
59  1 Y 1 A GLN 21  ? CD  ? B GLN 9   CD  
60  1 Y 1 A GLN 21  ? OE1 ? B GLN 9   OE1 
61  1 Y 1 A GLN 21  ? NE2 ? B GLN 9   NE2 
62  1 Y 1 A GLU 23  ? CG  ? B GLU 11  CG  
63  1 Y 1 A GLU 23  ? CD  ? B GLU 11  CD  
64  1 Y 1 A GLU 23  ? OE1 ? B GLU 11  OE1 
65  1 Y 1 A GLU 23  ? OE2 ? B GLU 11  OE2 
66  1 Y 1 A GLU 44  ? CG  ? B GLU 32  CG  
67  1 Y 1 A GLU 44  ? CD  ? B GLU 32  CD  
68  1 Y 1 A GLU 44  ? OE1 ? B GLU 32  OE1 
69  1 Y 1 A GLU 44  ? OE2 ? B GLU 32  OE2 
70  1 Y 1 A GLU 45  ? CG  ? B GLU 33  CG  
71  1 Y 1 A GLU 45  ? CD  ? B GLU 33  CD  
72  1 Y 1 A GLU 45  ? OE1 ? B GLU 33  OE1 
73  1 Y 1 A GLU 45  ? OE2 ? B GLU 33  OE2 
74  1 Y 1 A ASN 63  ? CG  ? B ASN 51  CG  
75  1 Y 1 A ASN 63  ? OD1 ? B ASN 51  OD1 
76  1 Y 1 A ASN 63  ? ND2 ? B ASN 51  ND2 
77  1 Y 1 A LYS 65  ? CG  ? B LYS 53  CG  
78  1 Y 1 A LYS 65  ? CD  ? B LYS 53  CD  
79  1 Y 1 A LYS 65  ? CE  ? B LYS 53  CE  
80  1 Y 1 A LYS 65  ? NZ  ? B LYS 53  NZ  
81  1 Y 1 A LYS 66  ? CG  ? B LYS 54  CG  
82  1 Y 1 A LYS 66  ? CD  ? B LYS 54  CD  
83  1 Y 1 A LYS 66  ? CE  ? B LYS 54  CE  
84  1 Y 1 A LYS 66  ? NZ  ? B LYS 54  NZ  
85  1 Y 1 A LYS 83  ? CG  ? B LYS 71  CG  
86  1 Y 1 A LYS 83  ? CD  ? B LYS 71  CD  
87  1 Y 1 A LYS 83  ? CE  ? B LYS 71  CE  
88  1 Y 1 A LYS 83  ? NZ  ? B LYS 71  NZ  
89  1 Y 1 A LYS 88  ? CG  ? B LYS 76  CG  
90  1 Y 1 A LYS 88  ? CD  ? B LYS 76  CD  
91  1 Y 1 A LYS 88  ? CE  ? B LYS 76  CE  
92  1 Y 1 A LYS 88  ? NZ  ? B LYS 76  NZ  
93  1 Y 1 A LYS 138 ? CG  ? B LYS 126 CG  
94  1 Y 1 A LYS 138 ? CD  ? B LYS 126 CD  
95  1 Y 1 A LYS 138 ? CE  ? B LYS 126 CE  
96  1 Y 1 A LYS 138 ? NZ  ? B LYS 126 NZ  
97  1 Y 1 A GLU 140 ? CG  ? B GLU 128 CG  
98  1 Y 1 A GLU 140 ? CD  ? B GLU 128 CD  
99  1 Y 1 A GLU 140 ? OE1 ? B GLU 128 OE1 
100 1 Y 1 A GLU 140 ? OE2 ? B GLU 128 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 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                     9GPX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.193 
_cell.length_a_esd                 ? 
_cell.length_b                     49.193 
_cell.length_b_esd                 ? 
_cell.length_c                     196.443 
_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                         9GPX 
_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                   9GPX 
_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             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.79 
_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    '18% 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         2024-06-26 
_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                                       9GPX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               49.11 
_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                                     26718 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.03 
_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                                0.066 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.061 
_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 49.11 ? 69.5 ? ? ? ? 279  ? ? ? ? ? ? ? ? ? ? ? 8.8  0.79 ? ? 0.024 0.010 ? 1 ? 1.000 ? ? 98.2  ? 0.022 ? ? ? ? ? ? ? ? ? 
1.80 1.84  ? 1.8  ? ? ? ? 1549 ? ? ? ? ? ? ? ? ? ? ? 12.2 1.04 ? ? 1.557 0.607 ? 2 ? 0.642 ? ? 100.0 ? 1.431 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.224 
_refine.aniso_B[1][2]                            -0.112 
_refine.aniso_B[1][3]                            -0.000 
_refine.aniso_B[2][2]                            -0.224 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.726 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               40.030 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.953 
_refine.correlation_coeff_Fo_to_Fc_free          0.933 
_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                                 9GPX 
_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                             35.735 
_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                     26645 
_refine.ls_number_reflns_R_free                  1399 
_refine.ls_number_reflns_R_work                  25246 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.962 
_refine.ls_percent_reflns_R_free                 5.251 
_refine.ls_R_factor_all                          0.225 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2611 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2226 
_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                       0.142 
_refine.pdbx_overall_ESU_R_Free                  0.137 
_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                             7.773 
_refine.overall_SU_ML                            0.118 
_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                        35.735 
_refine_hist.number_atoms_solvent             109 
_refine_hist.number_atoms_total               2067 
_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        1874 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.015  0.012  2006 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  1868 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 2.336  1.826  2720 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 0.788  1.744  4343 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 8.708  5.000  254  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 28.218 13.333 18   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 11.788 10.000 302  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 16.149 10.000 66   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.119  0.200  302  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  2280 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  408  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.213  0.200  331  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.196  0.200  1690 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.185  0.200  1010 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.093  0.200  1078 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.147  0.200  107  ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.176  0.200  1    ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.113  0.200  8    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.153  0.200  35   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.274  0.200  15   ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 3.197  2.320  1022 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.195  2.320  1022 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 4.157  4.156  1274 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 4.156  4.157  1275 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 3.369  2.428  984  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.368  2.427  985  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 4.595  4.375  1446 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 4.593  4.374  1447 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 6.363  22.455 2179 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 6.351  21.710 2153 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.128  0.050  3509 ? 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 ? ? 0.12786 ? 0.05007 1 'Local ncs' ? B ? ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.12786 ? 0.05007 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  1926 . 98  1827 99.9481  . 0.286 . . 0.285 . . . . . 0.278 . 20 . 0.940 0.947 0.295 
'X-RAY DIFFRACTION' 1.847 1.897  1894 . 77  1817 100.0000 . 0.284 . . 0.283 . . . . . 0.272 . 20 . 0.945 0.936 0.305 
'X-RAY DIFFRACTION' 1.897 1.952  1810 . 83  1727 100.0000 . 0.305 . . 0.303 . . . . . 0.288 . 20 . 0.934 0.913 0.356 
'X-RAY DIFFRACTION' 1.952 2.012  1756 . 78  1678 100.0000 . 0.246 . . 0.243 . . . . . 0.222 . 20 . 0.958 0.935 0.308 
'X-RAY DIFFRACTION' 2.012 2.078  1750 . 111 1639 100.0000 . 0.218 . . 0.213 . . . . . 0.193 . 20 . 0.970 0.942 0.287 
'X-RAY DIFFRACTION' 2.078 2.150  1670 . 73  1597 100.0000 . 0.231 . . 0.231 . . . . . 0.204 . 20 . 0.964 0.964 0.234 
'X-RAY DIFFRACTION' 2.150 2.231  1626 . 99  1526 99.9385  . 0.233 . . 0.227 . . . . . 0.199 . 20 . 0.967 0.934 0.322 
'X-RAY DIFFRACTION' 2.231 2.322  1547 . 83  1464 100.0000 . 0.239 . . 0.238 . . . . . 0.213 . 20 . 0.964 0.961 0.254 
'X-RAY DIFFRACTION' 2.322 2.425  1490 . 85  1405 100.0000 . 0.206 . . 0.203 . . . . . 0.179 . 20 . 0.975 0.961 0.261 
'X-RAY DIFFRACTION' 2.425 2.542  1433 . 83  1350 100.0000 . 0.197 . . 0.194 . . . . . 0.173 . 20 . 0.977 0.961 0.240 
'X-RAY DIFFRACTION' 2.542 2.679  1387 . 73  1314 100.0000 . 0.231 . . 0.227 . . . . . 0.206 . 20 . 0.968 0.933 0.311 
'X-RAY DIFFRACTION' 2.679 2.841  1309 . 77  1232 100.0000 . 0.240 . . 0.238 . . . . . 0.218 . 20 . 0.962 0.950 0.264 
'X-RAY DIFFRACTION' 2.841 3.036  1214 . 67  1147 100.0000 . 0.207 . . 0.205 . . . . . 0.195 . 20 . 0.973 0.970 0.235 
'X-RAY DIFFRACTION' 3.036 3.277  1188 . 81  1107 100.0000 . 0.223 . . 0.221 . . . . . 0.215 . 20 . 0.970 0.962 0.252 
'X-RAY DIFFRACTION' 3.277 3.587  1040 . 47  993  100.0000 . 0.240 . . 0.239 . . . . . 0.235 . 20 . 0.969 0.957 0.274 
'X-RAY DIFFRACTION' 3.587 4.005  977  . 39  938  100.0000 . 0.223 . . 0.220 . . . . . 0.220 . 20 . 0.974 0.938 0.288 
'X-RAY DIFFRACTION' 4.005 4.615  872  . 49  823  100.0000 . 0.187 . . 0.187 . . . . . 0.200 . 20 . 0.980 0.977 0.189 
'X-RAY DIFFRACTION' 4.615 5.628  763  . 43  720  100.0000 . 0.214 . . 0.210 . . . . . 0.225 . 20 . 0.974 0.944 0.282 
'X-RAY DIFFRACTION' 5.628 7.863  607  . 28  579  100.0000 . 0.234 . . 0.232 . . . . . 0.252 . 20 . 0.971 0.958 0.286 
'X-RAY DIFFRACTION' 7.863 35.735 390  . 25  363  99.4872  . 0.230 . . 0.230 . . . . . 0.272 . 20 . 0.963 0.967 0.237 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.details 
1 1 B 
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 . B GLY 13 B GLU 140 ? ? 
1 2 1 A GLY 1 . A 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                     9GPX 
_struct.title                        'The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog 12f/l' 
_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        9GPX 
_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 9GPX B 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
2 1 9GPX A 4 ? 128 ? Q13451 16 ? 140 ? 16 140 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GPX GLY B 1  ? UNP Q13451 ?   ?   'expression tag'      13  1  
1 9GPX ALA B 2  ? UNP Q13451 ?   ?   'expression tag'      14  2  
1 9GPX PRO B 3  ? UNP Q13451 ?   ?   'expression tag'      15  3  
1 9GPX THR B 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  4  
1 9GPX ALA B 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 5  
1 9GPX ILE B 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 6  
2 9GPX GLY A 1  ? UNP Q13451 ?   ?   'expression tag'      13  7  
2 9GPX ALA A 2  ? UNP Q13451 ?   ?   'expression tag'      14  8  
2 9GPX PRO A 3  ? UNP Q13451 ?   ?   'expression tag'      15  9  
2 9GPX THR A 7  ? UNP Q13451 ALA 19  'engineered mutation' 19  10 
2 9GPX ALA A 91 ? UNP Q13451 CYS 103 'engineered mutation' 103 11 
2 9GPX ILE A 95 ? UNP Q13451 CYS 107 'engineered mutation' 107 12 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 1  ? GLY A 10  ? GLY B 13  GLY B 22  1 ? 10 
HELX_P HELX_P2 AA2 HIS A 59 ? ASN A 62  ? HIS B 71  ASN B 74  5 ? 4  
HELX_P HELX_P3 AA3 ILE A 75 ? ALA A 83  ? ILE B 87  ALA B 95  1 ? 9  
HELX_P HELX_P4 AA4 PRO A 97 ? ALA A 100 ? PRO B 109 ALA B 112 5 ? 4  
HELX_P HELX_P5 AA5 ALA B 2  ? GLY B 10  ? ALA A 14  GLY A 22  1 ? 9  
HELX_P HELX_P6 AA6 HIS B 59 ? ASN B 62  ? HIS A 71  ASN A 74  5 ? 4  
HELX_P HELX_P7 AA7 ILE B 75 ? THR B 84  ? ILE A 87  THR A 96  1 ? 10 
HELX_P HELX_P8 AA8 PRO B 97 ? ALA B 100 ? PRO A 109 ALA A 112 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 LEU 107 A . ? LEU 119 B PRO 108 A ? PRO 120 B 1 3.27 
2 LEU 107 B . ? LEU 119 A PRO 108 B ? PRO 120 A 1 4.09 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 11  ? ASP A 12  ? GLU B 23  ASP B 24  
AA1 2 VAL A 21  ? ARG A 27  ? VAL B 33  ARG B 39  
AA1 3 ILE A 90  ? ILE A 95  ? ILE B 102 ILE B 107 
AA1 4 LEU A 116 ? LYS A 126 ? LEU B 128 LYS B 138 
AA1 5 LYS A 40  ? LEU A 49  ? LYS B 52  LEU B 61  
AA1 6 ASP A 56  ? SER A 57  ? ASP B 68  SER B 69  
AA2 1 GLU A 11  ? ASP A 12  ? GLU B 23  ASP B 24  
AA2 2 VAL A 21  ? ARG A 27  ? VAL B 33  ARG B 39  
AA2 3 ILE A 90  ? ILE A 95  ? ILE B 102 ILE B 107 
AA2 4 LEU A 116 ? LYS A 126 ? LEU B 128 LYS B 138 
AA2 5 LYS A 40  ? LEU A 49  ? LYS B 52  LEU B 61  
AA2 6 PHE A 65  ? SER A 68  ? PHE B 77  SER B 80  
AA3 1 GLU B 11  ? ASP B 12  ? GLU A 23  ASP A 24  
AA3 2 VAL B 21  ? ARG B 27  ? VAL A 33  ARG A 39  
AA3 3 ILE B 90  ? ILE B 95  ? ILE A 102 ILE A 107 
AA3 4 LEU B 116 ? LYS B 126 ? LEU A 128 LYS A 138 
AA3 5 LYS B 40  ? LEU B 49  ? LYS A 52  LEU A 61  
AA3 6 PHE B 55  ? SER B 57  ? PHE A 67  SER A 69  
AA4 1 GLU B 11  ? ASP B 12  ? GLU A 23  ASP A 24  
AA4 2 VAL B 21  ? ARG B 27  ? VAL A 33  ARG A 39  
AA4 3 ILE B 90  ? ILE B 95  ? ILE A 102 ILE A 107 
AA4 4 LEU B 116 ? LYS B 126 ? LEU A 128 LYS A 138 
AA4 5 LYS B 40  ? LEU B 49  ? LYS A 52  LEU A 61  
AA4 6 PHE B 65  ? SER B 68  ? PHE A 77  SER A 80  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 11  ? N GLU B 23  O LYS A 23  ? O LYS B 35  
AA1 2 3 N LYS A 26  ? N LYS B 38  O ILE A 90  ? O ILE B 102 
AA1 3 4 N ILE A 95  ? N ILE B 107 O LEU A 116 ? O LEU B 128 
AA1 4 5 O GLU A 121 ? O GLU B 133 N HIS A 44  ? N HIS B 56  
AA1 5 6 N GLY A 47  ? N GLY B 59  O ASP A 56  ? O ASP B 68  
AA2 1 2 N GLU A 11  ? N GLU B 23  O LYS A 23  ? O LYS B 35  
AA2 2 3 N LYS A 26  ? N LYS B 38  O ILE A 90  ? O ILE B 102 
AA2 3 4 N ILE A 95  ? N ILE B 107 O LEU A 116 ? O LEU B 128 
AA2 4 5 O GLU A 121 ? O GLU B 133 N HIS A 44  ? N HIS B 56  
AA2 5 6 N VAL A 41  ? N VAL B 53  O PHE A 67  ? O PHE B 79  
AA3 1 2 N GLU B 11  ? N GLU A 23  O LYS B 23  ? O LYS A 35  
AA3 2 3 N ILE B 24  ? N ILE A 36  O HIS B 92  ? O HIS A 104 
AA3 3 4 N ILE B 95  ? N ILE A 107 O LEU B 116 ? O LEU A 128 
AA3 4 5 O LYS B 126 ? O LYS A 138 N LYS B 40  ? N LYS A 52  
AA3 5 6 N GLY B 47  ? N GLY A 59  O ASP B 56  ? O ASP A 68  
AA4 1 2 N GLU B 11  ? N GLU A 23  O LYS B 23  ? O LYS A 35  
AA4 2 3 N ILE B 24  ? N ILE A 36  O HIS B 92  ? O HIS A 104 
AA4 3 4 N ILE B 95  ? N ILE A 107 O LEU B 116 ? O LEU A 128 
AA4 4 5 O LYS B 126 ? O LYS A 138 N LYS B 40  ? N LYS A 52  
AA4 5 6 N VAL B 41  ? N VAL A 53  O PHE B 67  ? O PHE A 79  
# 
_pdbx_entry_details.entry_id                   9GPX 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 H B LYS 65  ? ? O B HOH 301 ? ? 1.44 
2 1 O A HOH 315 ? ? O A HOH 343 ? ? 2.17 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB  B ASN 63  ? ? CA B ASN 63  ? ? C   B ASN 63  ? ? 97.96  110.40 -12.44 2.00 N 
2 1 CB  A GLU 44  ? ? CA A GLU 44  ? ? C   A GLU 44  ? ? 123.05 110.40 12.65  2.00 N 
3 1 CB  A ASN 63  ? ? CA A ASN 63  ? ? C   A ASN 63  ? ? 98.15  110.40 -12.25 2.00 N 
4 1 OG1 A THR 127 ? ? CB A THR 127 ? ? CG2 A THR 127 ? ? 96.04  110.00 -13.96 2.30 N 
5 1 CB  A LEU 128 ? ? CG A LEU 128 ? ? CD1 A LEU 128 ? ? 124.20 111.00 13.20  1.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU B 44  ? ? 105.44  -19.38  
2 1 ALA B 112 ? ? -134.38 -107.66 
3 1 SER B 118 ? ? -159.55 74.65   
4 1 ASN A 63  ? ? -60.44  2.37    
5 1 ALA A 112 ? ? -128.95 -106.26 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    67 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ASP 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    68 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            147.32 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     73 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.073 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     349 
_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 18.5384 -0.7156 -4.6799  0.0873 ? -0.0061 ? -0.0123 ? 0.0281 ? 0.0243 ? 0.0736 ? 2.9022 ? -0.9768 
? 0.2608  ? 3.2266 ? 0.2080 ? 4.5638 ? 0.0590 ? -0.0148 ? -0.3429 ? -0.1848 ? -0.0655 ? -0.1269 ? 0.3221  ? 0.2002  ? 0.0065  ? 
2 'X-RAY DIFFRACTION' ? refined 9.8627  15.9192 -29.4587 0.0888 ? 0.0582  ? -0.0006 ? 0.0463 ? 0.0154 ? 0.1123 ? 5.2546 ? 0.6996  
? -0.3634 ? 3.7667 ? 0.4310 ? 3.7634 ? 0.2993 ? 0.1609  ? 0.4720  ? -0.0576 ? -0.1906 ? -0.3570 ? -0.0670 ? -0.1425 ? -0.1087 ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    Bp 
_pdbx_refine_tls_group.beg_auth_seq_id     13 
_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    Bp 
_pdbx_refine_tls_group.end_auth_seq_id     201 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ALL 
_pdbx_refine_tls_group.selection_details   ? 
# 
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 
A1INX C4   C Y N 1   
A1INX C14  C Y N 2   
A1INX C5   C Y N 3   
A1INX C6   C Y N 4   
A1INX C11  C N R 5   
A1INX C7   C Y N 6   
A1INX C8   C N N 7   
A1INX C9   C N N 8   
A1INX C10  C N N 9   
A1INX C12  C N N 10  
A1INX C13  C Y N 11  
A1INX N1   N Y N 12  
A1INX N2   N Y N 13  
A1INX C3   C Y N 14  
A1INX N3   N Y N 15  
A1INX C1   C N N 16  
A1INX O1   O N N 17  
A1INX C2   C Y N 18  
A1INX O2   O N N 19  
A1INX O3   O N N 20  
A1INX C15  C N N 21  
A1INX C16  C N S 22  
A1INX C17  C N N 23  
A1INX C18  C N N 24  
A1INX O4   O N N 25  
A1INX C19  C N N 26  
A1INX O5   O N N 27  
A1INX C20  C N S 28  
A1INX C21  C N N 29  
A1INX C22  C N N 30  
A1INX C23  C N N 31  
A1INX C24  C N N 32  
A1INX N4   N N N 33  
A1INX C25  C N N 34  
A1INX O6   O N N 35  
A1INX C26  C N S 36  
A1INX C27  C N N 37  
A1INX C28  C N N 38  
A1INX C29  C N N 39  
A1INX C30  C N N 40  
A1INX C31  C N N 41  
A1INX C32  C N N 42  
A1INX H5   H N N 43  
A1INX H13  H N N 44  
A1INX H7   H N N 45  
A1INX H8   H N N 46  
A1INX H6   H N N 47  
A1INX H9   H N N 48  
A1INX H10  H N N 49  
A1INX H12  H N N 50  
A1INX H11  H N N 51  
A1INX H15  H N N 52  
A1INX H16  H N N 53  
A1INX H14  H N N 54  
A1INX H17  H N N 55  
A1INX H4   H N N 56  
A1INX H2   H N N 57  
A1INX H3   H N N 58  
A1INX H1   H N N 59  
A1INX H18  H N N 60  
A1INX H19  H N N 61  
A1INX H20  H N N 62  
A1INX H23  H N N 63  
A1INX H21  H N N 64  
A1INX H22  H N N 65  
A1INX H25  H N N 66  
A1INX H24  H N N 67  
A1INX H26  H N N 68  
A1INX H28  H N N 69  
A1INX H27  H N N 70  
A1INX H29  H N N 71  
A1INX H30  H N N 72  
A1INX H31  H N N 73  
A1INX H32  H N N 74  
A1INX H33  H N N 75  
A1INX H34  H N N 76  
A1INX H35  H N N 77  
A1INX H36  H N N 78  
A1INX H38  H N N 79  
A1INX H37  H N N 80  
A1INX H39  H N N 81  
A1INX H40  H N N 82  
A1INX H41  H N N 83  
A1INX H42  H N N 84  
A1INX H43  H N N 85  
A1INX H44  H N N 86  
A1INX H46  H N N 87  
A1INX H45  H N N 88  
ALA   N    N N N 89  
ALA   CA   C N S 90  
ALA   C    C N N 91  
ALA   O    O N N 92  
ALA   CB   C N N 93  
ALA   OXT  O N N 94  
ALA   H    H N N 95  
ALA   H2   H N N 96  
ALA   HA   H N N 97  
ALA   HB1  H N N 98  
ALA   HB2  H N N 99  
ALA   HB3  H N N 100 
ALA   HXT  H N N 101 
ARG   N    N N N 102 
ARG   CA   C N S 103 
ARG   C    C N N 104 
ARG   O    O N N 105 
ARG   CB   C N N 106 
ARG   CG   C N N 107 
ARG   CD   C N N 108 
ARG   NE   N N N 109 
ARG   CZ   C N N 110 
ARG   NH1  N N N 111 
ARG   NH2  N N N 112 
ARG   OXT  O N N 113 
ARG   H    H N N 114 
ARG   H2   H N N 115 
ARG   HA   H N N 116 
ARG   HB2  H N N 117 
ARG   HB3  H N N 118 
ARG   HG2  H N N 119 
ARG   HG3  H N N 120 
ARG   HD2  H N N 121 
ARG   HD3  H N N 122 
ARG   HE   H N N 123 
ARG   HH11 H N N 124 
ARG   HH12 H N N 125 
ARG   HH21 H N N 126 
ARG   HH22 H N N 127 
ARG   HXT  H N N 128 
ASN   N    N N N 129 
ASN   CA   C N S 130 
ASN   C    C N N 131 
ASN   O    O N N 132 
ASN   CB   C N N 133 
ASN   CG   C N N 134 
ASN   OD1  O N N 135 
ASN   ND2  N N N 136 
ASN   OXT  O N N 137 
ASN   H    H N N 138 
ASN   H2   H N N 139 
ASN   HA   H N N 140 
ASN   HB2  H N N 141 
ASN   HB3  H N N 142 
ASN   HD21 H N N 143 
ASN   HD22 H N N 144 
ASN   HXT  H N N 145 
ASP   N    N N N 146 
ASP   CA   C N S 147 
ASP   C    C N N 148 
ASP   O    O N N 149 
ASP   CB   C N N 150 
ASP   CG   C N N 151 
ASP   OD1  O N N 152 
ASP   OD2  O N N 153 
ASP   OXT  O N N 154 
ASP   H    H N N 155 
ASP   H2   H N N 156 
ASP   HA   H N N 157 
ASP   HB2  H N N 158 
ASP   HB3  H N N 159 
ASP   HD2  H N N 160 
ASP   HXT  H N N 161 
CYS   N    N N N 162 
CYS   CA   C N R 163 
CYS   C    C N N 164 
CYS   O    O N N 165 
CYS   CB   C N N 166 
CYS   SG   S N N 167 
CYS   OXT  O N N 168 
CYS   H    H N N 169 
CYS   H2   H N N 170 
CYS   HA   H N N 171 
CYS   HB2  H N N 172 
CYS   HB3  H N N 173 
CYS   HG   H N N 174 
CYS   HXT  H N N 175 
GLN   N    N N N 176 
GLN   CA   C N S 177 
GLN   C    C N N 178 
GLN   O    O N N 179 
GLN   CB   C N N 180 
GLN   CG   C N N 181 
GLN   CD   C N N 182 
GLN   OE1  O N N 183 
GLN   NE2  N N N 184 
GLN   OXT  O N N 185 
GLN   H    H N N 186 
GLN   H2   H N N 187 
GLN   HA   H N N 188 
GLN   HB2  H N N 189 
GLN   HB3  H N N 190 
GLN   HG2  H N N 191 
GLN   HG3  H N N 192 
GLN   HE21 H N N 193 
GLN   HE22 H N N 194 
GLN   HXT  H N N 195 
GLU   N    N N N 196 
GLU   CA   C N S 197 
GLU   C    C N N 198 
GLU   O    O N N 199 
GLU   CB   C N N 200 
GLU   CG   C N N 201 
GLU   CD   C N N 202 
GLU   OE1  O N N 203 
GLU   OE2  O N N 204 
GLU   OXT  O N N 205 
GLU   H    H N N 206 
GLU   H2   H N N 207 
GLU   HA   H N N 208 
GLU   HB2  H N N 209 
GLU   HB3  H N N 210 
GLU   HG2  H N N 211 
GLU   HG3  H N N 212 
GLU   HE2  H N N 213 
GLU   HXT  H N N 214 
GLY   N    N N N 215 
GLY   CA   C N N 216 
GLY   C    C N N 217 
GLY   O    O N N 218 
GLY   OXT  O N N 219 
GLY   H    H N N 220 
GLY   H2   H N N 221 
GLY   HA2  H N N 222 
GLY   HA3  H N N 223 
GLY   HXT  H N N 224 
HIS   N    N N N 225 
HIS   CA   C N S 226 
HIS   C    C N N 227 
HIS   O    O N N 228 
HIS   CB   C N N 229 
HIS   CG   C Y N 230 
HIS   ND1  N Y N 231 
HIS   CD2  C Y N 232 
HIS   CE1  C Y N 233 
HIS   NE2  N Y N 234 
HIS   OXT  O N N 235 
HIS   H    H N N 236 
HIS   H2   H N N 237 
HIS   HA   H N N 238 
HIS   HB2  H N N 239 
HIS   HB3  H N N 240 
HIS   HD1  H N N 241 
HIS   HD2  H N N 242 
HIS   HE1  H N N 243 
HIS   HE2  H N N 244 
HIS   HXT  H N N 245 
HOH   O    O N N 246 
HOH   H1   H N N 247 
HOH   H2   H N N 248 
ILE   N    N N N 249 
ILE   CA   C N S 250 
ILE   C    C N N 251 
ILE   O    O N N 252 
ILE   CB   C N S 253 
ILE   CG1  C N N 254 
ILE   CG2  C N N 255 
ILE   CD1  C N N 256 
ILE   OXT  O N N 257 
ILE   H    H N N 258 
ILE   H2   H N N 259 
ILE   HA   H N N 260 
ILE   HB   H N N 261 
ILE   HG12 H N N 262 
ILE   HG13 H N N 263 
ILE   HG21 H N N 264 
ILE   HG22 H N N 265 
ILE   HG23 H N N 266 
ILE   HD11 H N N 267 
ILE   HD12 H N N 268 
ILE   HD13 H N N 269 
ILE   HXT  H N N 270 
LEU   N    N N N 271 
LEU   CA   C N S 272 
LEU   C    C N N 273 
LEU   O    O N N 274 
LEU   CB   C N N 275 
LEU   CG   C N N 276 
LEU   CD1  C N N 277 
LEU   CD2  C N N 278 
LEU   OXT  O N N 279 
LEU   H    H N N 280 
LEU   H2   H N N 281 
LEU   HA   H N N 282 
LEU   HB2  H N N 283 
LEU   HB3  H N N 284 
LEU   HG   H N N 285 
LEU   HD11 H N N 286 
LEU   HD12 H N N 287 
LEU   HD13 H N N 288 
LEU   HD21 H N N 289 
LEU   HD22 H N N 290 
LEU   HD23 H N N 291 
LEU   HXT  H N N 292 
LYS   N    N N N 293 
LYS   CA   C N S 294 
LYS   C    C N N 295 
LYS   O    O N N 296 
LYS   CB   C N N 297 
LYS   CG   C N N 298 
LYS   CD   C N N 299 
LYS   CE   C N N 300 
LYS   NZ   N N N 301 
LYS   OXT  O N N 302 
LYS   H    H N N 303 
LYS   H2   H N N 304 
LYS   HA   H N N 305 
LYS   HB2  H N N 306 
LYS   HB3  H N N 307 
LYS   HG2  H N N 308 
LYS   HG3  H N N 309 
LYS   HD2  H N N 310 
LYS   HD3  H N N 311 
LYS   HE2  H N N 312 
LYS   HE3  H N N 313 
LYS   HZ1  H N N 314 
LYS   HZ2  H N N 315 
LYS   HZ3  H N N 316 
LYS   HXT  H N N 317 
MET   N    N N N 318 
MET   CA   C N S 319 
MET   C    C N N 320 
MET   O    O N N 321 
MET   CB   C N N 322 
MET   CG   C N N 323 
MET   SD   S N N 324 
MET   CE   C N N 325 
MET   OXT  O N N 326 
MET   H    H N N 327 
MET   H2   H N N 328 
MET   HA   H N N 329 
MET   HB2  H N N 330 
MET   HB3  H N N 331 
MET   HG2  H N N 332 
MET   HG3  H N N 333 
MET   HE1  H N N 334 
MET   HE2  H N N 335 
MET   HE3  H N N 336 
MET   HXT  H N N 337 
PHE   N    N N N 338 
PHE   CA   C N S 339 
PHE   C    C N N 340 
PHE   O    O N N 341 
PHE   CB   C N N 342 
PHE   CG   C Y N 343 
PHE   CD1  C Y N 344 
PHE   CD2  C Y N 345 
PHE   CE1  C Y N 346 
PHE   CE2  C Y N 347 
PHE   CZ   C Y N 348 
PHE   OXT  O N N 349 
PHE   H    H N N 350 
PHE   H2   H N N 351 
PHE   HA   H N N 352 
PHE   HB2  H N N 353 
PHE   HB3  H N N 354 
PHE   HD1  H N N 355 
PHE   HD2  H N N 356 
PHE   HE1  H N N 357 
PHE   HE2  H N N 358 
PHE   HZ   H N N 359 
PHE   HXT  H N N 360 
PRO   N    N N N 361 
PRO   CA   C N S 362 
PRO   C    C N N 363 
PRO   O    O N N 364 
PRO   CB   C N N 365 
PRO   CG   C N N 366 
PRO   CD   C N N 367 
PRO   OXT  O N N 368 
PRO   H    H N N 369 
PRO   HA   H N N 370 
PRO   HB2  H N N 371 
PRO   HB3  H N N 372 
PRO   HG2  H N N 373 
PRO   HG3  H N N 374 
PRO   HD2  H N N 375 
PRO   HD3  H N N 376 
PRO   HXT  H N N 377 
SER   N    N N N 378 
SER   CA   C N S 379 
SER   C    C N N 380 
SER   O    O N N 381 
SER   CB   C N N 382 
SER   OG   O N N 383 
SER   OXT  O N N 384 
SER   H    H N N 385 
SER   H2   H N N 386 
SER   HA   H N N 387 
SER   HB2  H N N 388 
SER   HB3  H N N 389 
SER   HG   H N N 390 
SER   HXT  H N N 391 
THR   N    N N N 392 
THR   CA   C N S 393 
THR   C    C N N 394 
THR   O    O N N 395 
THR   CB   C N R 396 
THR   OG1  O N N 397 
THR   CG2  C N N 398 
THR   OXT  O N N 399 
THR   H    H N N 400 
THR   H2   H N N 401 
THR   HA   H N N 402 
THR   HB   H N N 403 
THR   HG1  H N N 404 
THR   HG21 H N N 405 
THR   HG22 H N N 406 
THR   HG23 H N N 407 
THR   HXT  H N N 408 
TRP   N    N N N 409 
TRP   CA   C N S 410 
TRP   C    C N N 411 
TRP   O    O N N 412 
TRP   CB   C N N 413 
TRP   CG   C Y N 414 
TRP   CD1  C Y N 415 
TRP   CD2  C Y N 416 
TRP   NE1  N Y N 417 
TRP   CE2  C Y N 418 
TRP   CE3  C Y N 419 
TRP   CZ2  C Y N 420 
TRP   CZ3  C Y N 421 
TRP   CH2  C Y N 422 
TRP   OXT  O N N 423 
TRP   H    H N N 424 
TRP   H2   H N N 425 
TRP   HA   H N N 426 
TRP   HB2  H N N 427 
TRP   HB3  H N N 428 
TRP   HD1  H N N 429 
TRP   HE1  H N N 430 
TRP   HE3  H N N 431 
TRP   HZ2  H N N 432 
TRP   HZ3  H N N 433 
TRP   HH2  H N N 434 
TRP   HXT  H N N 435 
TYR   N    N N N 436 
TYR   CA   C N S 437 
TYR   C    C N N 438 
TYR   O    O N N 439 
TYR   CB   C N N 440 
TYR   CG   C Y N 441 
TYR   CD1  C Y N 442 
TYR   CD2  C Y N 443 
TYR   CE1  C Y N 444 
TYR   CE2  C Y N 445 
TYR   CZ   C Y N 446 
TYR   OH   O N N 447 
TYR   OXT  O N N 448 
TYR   H    H N N 449 
TYR   H2   H N N 450 
TYR   HA   H N N 451 
TYR   HB2  H N N 452 
TYR   HB3  H N N 453 
TYR   HD1  H N N 454 
TYR   HD2  H N N 455 
TYR   HE1  H N N 456 
TYR   HE2  H N N 457 
TYR   HH   H N N 458 
TYR   HXT  H N N 459 
VAL   N    N N N 460 
VAL   CA   C N S 461 
VAL   C    C N N 462 
VAL   O    O N N 463 
VAL   CB   C N N 464 
VAL   CG1  C N N 465 
VAL   CG2  C N N 466 
VAL   OXT  O N N 467 
VAL   H    H N N 468 
VAL   H2   H N N 469 
VAL   HA   H N N 470 
VAL   HB   H N N 471 
VAL   HG11 H N N 472 
VAL   HG12 H N N 473 
VAL   HG13 H N N 474 
VAL   HG21 H N N 475 
VAL   HG22 H N N 476 
VAL   HG23 H N N 477 
VAL   HXT  H N N 478 
# 
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 
A1INX C21 C22  sing N N 1   
A1INX C21 C20  sing N N 2   
A1INX C29 C28  sing N N 3   
A1INX C29 C30  sing N N 4   
A1INX C22 C23  sing N N 5   
A1INX C28 C27  sing N N 6   
A1INX C23 C24  sing N N 7   
A1INX C20 N4   sing N N 8   
A1INX C20 C19  sing N N 9   
A1INX C30 C31  sing N N 10  
A1INX N4  C24  sing N N 11  
A1INX N4  C25  sing N N 12  
A1INX C25 O6   doub N N 13  
A1INX C25 C26  sing N N 14  
A1INX O5  C19  doub N N 15  
A1INX C27 C26  sing N N 16  
A1INX C27 C32  sing N N 17  
A1INX C19 O4   sing N N 18  
A1INX C26 C4   sing N N 19  
A1INX C31 C32  sing N N 20  
A1INX O4  C18  sing N N 21  
A1INX C4  C5   doub Y N 22  
A1INX C4  C3   sing Y N 23  
A1INX C18 C16  sing N N 24  
A1INX C5  C6   sing Y N 25  
A1INX C3  C2   doub Y N 26  
A1INX C15 C14  sing N N 27  
A1INX C15 C16  sing N N 28  
A1INX C13 C14  doub Y N 29  
A1INX C13 N1   sing Y N 30  
A1INX C14 N2   sing Y N 31  
A1INX C16 C17  sing N N 32  
A1INX C6  O3   sing N N 33  
A1INX C6  C7   doub Y N 34  
A1INX C11 N1   sing N N 35  
A1INX C11 C10  sing N N 36  
A1INX C11 C12  sing N N 37  
A1INX N1  N3   sing Y N 38  
A1INX C9  O3   sing N N 39  
A1INX C9  C10  sing N N 40  
A1INX C2  C7   sing Y N 41  
A1INX C2  O1   sing N N 42  
A1INX C1  O1   sing N N 43  
A1INX C7  O2   sing N N 44  
A1INX N2  N3   doub Y N 45  
A1INX O2  C8   sing N N 46  
A1INX C5  H5   sing N N 47  
A1INX C11 H13  sing N N 48  
A1INX C8  H7   sing N N 49  
A1INX C8  H8   sing N N 50  
A1INX C8  H6   sing N N 51  
A1INX C9  H9   sing N N 52  
A1INX C9  H10  sing N N 53  
A1INX C10 H12  sing N N 54  
A1INX C10 H11  sing N N 55  
A1INX C12 H15  sing N N 56  
A1INX C12 H16  sing N N 57  
A1INX C12 H14  sing N N 58  
A1INX C13 H17  sing N N 59  
A1INX C3  H4   sing N N 60  
A1INX C1  H2   sing N N 61  
A1INX C1  H3   sing N N 62  
A1INX C1  H1   sing N N 63  
A1INX C15 H18  sing N N 64  
A1INX C15 H19  sing N N 65  
A1INX C16 H20  sing N N 66  
A1INX C17 H23  sing N N 67  
A1INX C17 H21  sing N N 68  
A1INX C17 H22  sing N N 69  
A1INX C18 H25  sing N N 70  
A1INX C18 H24  sing N N 71  
A1INX C20 H26  sing N N 72  
A1INX C21 H28  sing N N 73  
A1INX C21 H27  sing N N 74  
A1INX C22 H29  sing N N 75  
A1INX C22 H30  sing N N 76  
A1INX C23 H31  sing N N 77  
A1INX C23 H32  sing N N 78  
A1INX C24 H33  sing N N 79  
A1INX C24 H34  sing N N 80  
A1INX C26 H35  sing N N 81  
A1INX C27 H36  sing N N 82  
A1INX C28 H38  sing N N 83  
A1INX C28 H37  sing N N 84  
A1INX C29 H39  sing N N 85  
A1INX C29 H40  sing N N 86  
A1INX C30 H41  sing N N 87  
A1INX C30 H42  sing N N 88  
A1INX C31 H43  sing N N 89  
A1INX C31 H44  sing N N 90  
A1INX C32 H46  sing N N 91  
A1INX C32 H45  sing N N 92  
ALA   N   CA   sing N N 93  
ALA   N   H    sing N N 94  
ALA   N   H2   sing N N 95  
ALA   CA  C    sing N N 96  
ALA   CA  CB   sing N N 97  
ALA   CA  HA   sing N N 98  
ALA   C   O    doub N N 99  
ALA   C   OXT  sing N N 100 
ALA   CB  HB1  sing N N 101 
ALA   CB  HB2  sing N N 102 
ALA   CB  HB3  sing N N 103 
ALA   OXT HXT  sing N N 104 
ARG   N   CA   sing N N 105 
ARG   N   H    sing N N 106 
ARG   N   H2   sing N N 107 
ARG   CA  C    sing N N 108 
ARG   CA  CB   sing N N 109 
ARG   CA  HA   sing N N 110 
ARG   C   O    doub N N 111 
ARG   C   OXT  sing N N 112 
ARG   CB  CG   sing N N 113 
ARG   CB  HB2  sing N N 114 
ARG   CB  HB3  sing N N 115 
ARG   CG  CD   sing N N 116 
ARG   CG  HG2  sing N N 117 
ARG   CG  HG3  sing N N 118 
ARG   CD  NE   sing N N 119 
ARG   CD  HD2  sing N N 120 
ARG   CD  HD3  sing N N 121 
ARG   NE  CZ   sing N N 122 
ARG   NE  HE   sing N N 123 
ARG   CZ  NH1  sing N N 124 
ARG   CZ  NH2  doub N N 125 
ARG   NH1 HH11 sing N N 126 
ARG   NH1 HH12 sing N N 127 
ARG   NH2 HH21 sing N N 128 
ARG   NH2 HH22 sing N N 129 
ARG   OXT HXT  sing N N 130 
ASN   N   CA   sing N N 131 
ASN   N   H    sing N N 132 
ASN   N   H2   sing N N 133 
ASN   CA  C    sing N N 134 
ASN   CA  CB   sing N N 135 
ASN   CA  HA   sing N N 136 
ASN   C   O    doub N N 137 
ASN   C   OXT  sing N N 138 
ASN   CB  CG   sing N N 139 
ASN   CB  HB2  sing N N 140 
ASN   CB  HB3  sing N N 141 
ASN   CG  OD1  doub N N 142 
ASN   CG  ND2  sing N N 143 
ASN   ND2 HD21 sing N N 144 
ASN   ND2 HD22 sing N N 145 
ASN   OXT HXT  sing N N 146 
ASP   N   CA   sing N N 147 
ASP   N   H    sing N N 148 
ASP   N   H2   sing N N 149 
ASP   CA  C    sing N N 150 
ASP   CA  CB   sing N N 151 
ASP   CA  HA   sing N N 152 
ASP   C   O    doub N N 153 
ASP   C   OXT  sing N N 154 
ASP   CB  CG   sing N N 155 
ASP   CB  HB2  sing N N 156 
ASP   CB  HB3  sing N N 157 
ASP   CG  OD1  doub N N 158 
ASP   CG  OD2  sing N N 159 
ASP   OD2 HD2  sing N N 160 
ASP   OXT HXT  sing N N 161 
CYS   N   CA   sing N N 162 
CYS   N   H    sing N N 163 
CYS   N   H2   sing N N 164 
CYS   CA  C    sing N N 165 
CYS   CA  CB   sing N N 166 
CYS   CA  HA   sing N N 167 
CYS   C   O    doub N N 168 
CYS   C   OXT  sing N N 169 
CYS   CB  SG   sing N N 170 
CYS   CB  HB2  sing N N 171 
CYS   CB  HB3  sing N N 172 
CYS   SG  HG   sing N N 173 
CYS   OXT HXT  sing N N 174 
GLN   N   CA   sing N N 175 
GLN   N   H    sing N N 176 
GLN   N   H2   sing N N 177 
GLN   CA  C    sing N N 178 
GLN   CA  CB   sing N N 179 
GLN   CA  HA   sing N N 180 
GLN   C   O    doub N N 181 
GLN   C   OXT  sing N N 182 
GLN   CB  CG   sing N N 183 
GLN   CB  HB2  sing N N 184 
GLN   CB  HB3  sing N N 185 
GLN   CG  CD   sing N N 186 
GLN   CG  HG2  sing N N 187 
GLN   CG  HG3  sing N N 188 
GLN   CD  OE1  doub N N 189 
GLN   CD  NE2  sing N N 190 
GLN   NE2 HE21 sing N N 191 
GLN   NE2 HE22 sing N N 192 
GLN   OXT HXT  sing N N 193 
GLU   N   CA   sing N N 194 
GLU   N   H    sing N N 195 
GLU   N   H2   sing N N 196 
GLU   CA  C    sing N N 197 
GLU   CA  CB   sing N N 198 
GLU   CA  HA   sing N N 199 
GLU   C   O    doub N N 200 
GLU   C   OXT  sing N N 201 
GLU   CB  CG   sing N N 202 
GLU   CB  HB2  sing N N 203 
GLU   CB  HB3  sing N N 204 
GLU   CG  CD   sing N N 205 
GLU   CG  HG2  sing N N 206 
GLU   CG  HG3  sing N N 207 
GLU   CD  OE1  doub N N 208 
GLU   CD  OE2  sing N N 209 
GLU   OE2 HE2  sing N N 210 
GLU   OXT HXT  sing N N 211 
GLY   N   CA   sing N N 212 
GLY   N   H    sing N N 213 
GLY   N   H2   sing N N 214 
GLY   CA  C    sing N N 215 
GLY   CA  HA2  sing N N 216 
GLY   CA  HA3  sing N N 217 
GLY   C   O    doub N N 218 
GLY   C   OXT  sing N N 219 
GLY   OXT HXT  sing N N 220 
HIS   N   CA   sing N N 221 
HIS   N   H    sing N N 222 
HIS   N   H2   sing N N 223 
HIS   CA  C    sing N N 224 
HIS   CA  CB   sing N N 225 
HIS   CA  HA   sing N N 226 
HIS   C   O    doub N N 227 
HIS   C   OXT  sing N N 228 
HIS   CB  CG   sing N N 229 
HIS   CB  HB2  sing N N 230 
HIS   CB  HB3  sing N N 231 
HIS   CG  ND1  sing Y N 232 
HIS   CG  CD2  doub Y N 233 
HIS   ND1 CE1  doub Y N 234 
HIS   ND1 HD1  sing N N 235 
HIS   CD2 NE2  sing Y N 236 
HIS   CD2 HD2  sing N N 237 
HIS   CE1 NE2  sing Y N 238 
HIS   CE1 HE1  sing N N 239 
HIS   NE2 HE2  sing N N 240 
HIS   OXT HXT  sing N N 241 
HOH   O   H1   sing N N 242 
HOH   O   H2   sing N N 243 
ILE   N   CA   sing N N 244 
ILE   N   H    sing N N 245 
ILE   N   H2   sing N N 246 
ILE   CA  C    sing N N 247 
ILE   CA  CB   sing N N 248 
ILE   CA  HA   sing N N 249 
ILE   C   O    doub N N 250 
ILE   C   OXT  sing N N 251 
ILE   CB  CG1  sing N N 252 
ILE   CB  CG2  sing N N 253 
ILE   CB  HB   sing N N 254 
ILE   CG1 CD1  sing N N 255 
ILE   CG1 HG12 sing N N 256 
ILE   CG1 HG13 sing N N 257 
ILE   CG2 HG21 sing N N 258 
ILE   CG2 HG22 sing N N 259 
ILE   CG2 HG23 sing N N 260 
ILE   CD1 HD11 sing N N 261 
ILE   CD1 HD12 sing N N 262 
ILE   CD1 HD13 sing N N 263 
ILE   OXT HXT  sing N N 264 
LEU   N   CA   sing N N 265 
LEU   N   H    sing N N 266 
LEU   N   H2   sing N N 267 
LEU   CA  C    sing N N 268 
LEU   CA  CB   sing N N 269 
LEU   CA  HA   sing N N 270 
LEU   C   O    doub N N 271 
LEU   C   OXT  sing N N 272 
LEU   CB  CG   sing N N 273 
LEU   CB  HB2  sing N N 274 
LEU   CB  HB3  sing N N 275 
LEU   CG  CD1  sing N N 276 
LEU   CG  CD2  sing N N 277 
LEU   CG  HG   sing N N 278 
LEU   CD1 HD11 sing N N 279 
LEU   CD1 HD12 sing N N 280 
LEU   CD1 HD13 sing N N 281 
LEU   CD2 HD21 sing N N 282 
LEU   CD2 HD22 sing N N 283 
LEU   CD2 HD23 sing N N 284 
LEU   OXT HXT  sing N N 285 
LYS   N   CA   sing N N 286 
LYS   N   H    sing N N 287 
LYS   N   H2   sing N N 288 
LYS   CA  C    sing N N 289 
LYS   CA  CB   sing N N 290 
LYS   CA  HA   sing N N 291 
LYS   C   O    doub N N 292 
LYS   C   OXT  sing N N 293 
LYS   CB  CG   sing N N 294 
LYS   CB  HB2  sing N N 295 
LYS   CB  HB3  sing N N 296 
LYS   CG  CD   sing N N 297 
LYS   CG  HG2  sing N N 298 
LYS   CG  HG3  sing N N 299 
LYS   CD  CE   sing N N 300 
LYS   CD  HD2  sing N N 301 
LYS   CD  HD3  sing N N 302 
LYS   CE  NZ   sing N N 303 
LYS   CE  HE2  sing N N 304 
LYS   CE  HE3  sing N N 305 
LYS   NZ  HZ1  sing N N 306 
LYS   NZ  HZ2  sing N N 307 
LYS   NZ  HZ3  sing N N 308 
LYS   OXT HXT  sing N N 309 
MET   N   CA   sing N N 310 
MET   N   H    sing N N 311 
MET   N   H2   sing N N 312 
MET   CA  C    sing N N 313 
MET   CA  CB   sing N N 314 
MET   CA  HA   sing N N 315 
MET   C   O    doub N N 316 
MET   C   OXT  sing N N 317 
MET   CB  CG   sing N N 318 
MET   CB  HB2  sing N N 319 
MET   CB  HB3  sing N N 320 
MET   CG  SD   sing N N 321 
MET   CG  HG2  sing N N 322 
MET   CG  HG3  sing N N 323 
MET   SD  CE   sing N N 324 
MET   CE  HE1  sing N N 325 
MET   CE  HE2  sing N N 326 
MET   CE  HE3  sing N N 327 
MET   OXT HXT  sing N N 328 
PHE   N   CA   sing N N 329 
PHE   N   H    sing N N 330 
PHE   N   H2   sing N N 331 
PHE   CA  C    sing N N 332 
PHE   CA  CB   sing N N 333 
PHE   CA  HA   sing N N 334 
PHE   C   O    doub N N 335 
PHE   C   OXT  sing N N 336 
PHE   CB  CG   sing N N 337 
PHE   CB  HB2  sing N N 338 
PHE   CB  HB3  sing N N 339 
PHE   CG  CD1  doub Y N 340 
PHE   CG  CD2  sing Y N 341 
PHE   CD1 CE1  sing Y N 342 
PHE   CD1 HD1  sing N N 343 
PHE   CD2 CE2  doub Y N 344 
PHE   CD2 HD2  sing N N 345 
PHE   CE1 CZ   doub Y N 346 
PHE   CE1 HE1  sing N N 347 
PHE   CE2 CZ   sing Y N 348 
PHE   CE2 HE2  sing N N 349 
PHE   CZ  HZ   sing N N 350 
PHE   OXT HXT  sing N N 351 
PRO   N   CA   sing N N 352 
PRO   N   CD   sing N N 353 
PRO   N   H    sing N N 354 
PRO   CA  C    sing N N 355 
PRO   CA  CB   sing N N 356 
PRO   CA  HA   sing N N 357 
PRO   C   O    doub N N 358 
PRO   C   OXT  sing N N 359 
PRO   CB  CG   sing N N 360 
PRO   CB  HB2  sing N N 361 
PRO   CB  HB3  sing N N 362 
PRO   CG  CD   sing N N 363 
PRO   CG  HG2  sing N N 364 
PRO   CG  HG3  sing N N 365 
PRO   CD  HD2  sing N N 366 
PRO   CD  HD3  sing N N 367 
PRO   OXT HXT  sing N N 368 
SER   N   CA   sing N N 369 
SER   N   H    sing N N 370 
SER   N   H2   sing N N 371 
SER   CA  C    sing N N 372 
SER   CA  CB   sing N N 373 
SER   CA  HA   sing N N 374 
SER   C   O    doub N N 375 
SER   C   OXT  sing N N 376 
SER   CB  OG   sing N N 377 
SER   CB  HB2  sing N N 378 
SER   CB  HB3  sing N N 379 
SER   OG  HG   sing N N 380 
SER   OXT HXT  sing N N 381 
THR   N   CA   sing N N 382 
THR   N   H    sing N N 383 
THR   N   H2   sing N N 384 
THR   CA  C    sing N N 385 
THR   CA  CB   sing N N 386 
THR   CA  HA   sing N N 387 
THR   C   O    doub N N 388 
THR   C   OXT  sing N N 389 
THR   CB  OG1  sing N N 390 
THR   CB  CG2  sing N N 391 
THR   CB  HB   sing N N 392 
THR   OG1 HG1  sing N N 393 
THR   CG2 HG21 sing N N 394 
THR   CG2 HG22 sing N N 395 
THR   CG2 HG23 sing N N 396 
THR   OXT HXT  sing N N 397 
TRP   N   CA   sing N N 398 
TRP   N   H    sing N N 399 
TRP   N   H2   sing N N 400 
TRP   CA  C    sing N N 401 
TRP   CA  CB   sing N N 402 
TRP   CA  HA   sing N N 403 
TRP   C   O    doub N N 404 
TRP   C   OXT  sing N N 405 
TRP   CB  CG   sing N N 406 
TRP   CB  HB2  sing N N 407 
TRP   CB  HB3  sing N N 408 
TRP   CG  CD1  doub Y N 409 
TRP   CG  CD2  sing Y N 410 
TRP   CD1 NE1  sing Y N 411 
TRP   CD1 HD1  sing N N 412 
TRP   CD2 CE2  doub Y N 413 
TRP   CD2 CE3  sing Y N 414 
TRP   NE1 CE2  sing Y N 415 
TRP   NE1 HE1  sing N N 416 
TRP   CE2 CZ2  sing Y N 417 
TRP   CE3 CZ3  doub Y N 418 
TRP   CE3 HE3  sing N N 419 
TRP   CZ2 CH2  doub Y N 420 
TRP   CZ2 HZ2  sing N N 421 
TRP   CZ3 CH2  sing Y N 422 
TRP   CZ3 HZ3  sing N N 423 
TRP   CH2 HH2  sing N N 424 
TRP   OXT HXT  sing N N 425 
TYR   N   CA   sing N N 426 
TYR   N   H    sing N N 427 
TYR   N   H2   sing N N 428 
TYR   CA  C    sing N N 429 
TYR   CA  CB   sing N N 430 
TYR   CA  HA   sing N N 431 
TYR   C   O    doub N N 432 
TYR   C   OXT  sing N N 433 
TYR   CB  CG   sing N N 434 
TYR   CB  HB2  sing N N 435 
TYR   CB  HB3  sing N N 436 
TYR   CG  CD1  doub Y N 437 
TYR   CG  CD2  sing Y N 438 
TYR   CD1 CE1  sing Y N 439 
TYR   CD1 HD1  sing N N 440 
TYR   CD2 CE2  doub Y N 441 
TYR   CD2 HD2  sing N N 442 
TYR   CE1 CZ   doub Y N 443 
TYR   CE1 HE1  sing N N 444 
TYR   CE2 CZ   sing Y N 445 
TYR   CE2 HE2  sing N N 446 
TYR   CZ  OH   sing N N 447 
TYR   OH  HH   sing N N 448 
TYR   OXT HXT  sing N N 449 
VAL   N   CA   sing N N 450 
VAL   N   H    sing N N 451 
VAL   N   H2   sing N N 452 
VAL   CA  C    sing N N 453 
VAL   CA  CB   sing N N 454 
VAL   CA  HA   sing N N 455 
VAL   C   O    doub N N 456 
VAL   C   OXT  sing N N 457 
VAL   CB  CG1  sing N N 458 
VAL   CB  CG2  sing N N 459 
VAL   CB  HB   sing N N 460 
VAL   CG1 HG11 sing N N 461 
VAL   CG1 HG12 sing N N 462 
VAL   CG1 HG13 sing N N 463 
VAL   CG2 HG21 sing N N 464 
VAL   CG2 HG22 sing N N 465 
VAL   CG2 HG23 sing N N 466 
VAL   OXT HXT  sing N N 467 
# 
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                    9GPX 
_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]   0.020328 
_atom_sites.fract_transf_matrix[1][2]   0.011736 
_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]   0.023473 
_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]   0.005091 
_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   ? 2.824  -4.771  3.423   1   50.238  ? 13  GLY   B N    1 ? 1 
ATOM   2    C CA   . GLY   A 1 1   ? 3.979  -5.668  3.245   1   49.472  ? 13  GLY   B CA   1 ? 1 
ATOM   3    C C    . GLY   A 1 1   ? 5.263  -4.853  3.233   1   50.855  ? 13  GLY   B C    1 ? 1 
ATOM   4    O O    . GLY   A 1 1   ? 5.339  -3.768  3.828   1   46.315  ? 13  GLY   B O    1 ? 1 
ATOM   5    H H1   . GLY   A 1 1   ? 2.057  -5.252  3.424   1   52.329  ? 13  GLY   B H1   1 c 1 
ATOM   6    H H2   . GLY   A 1 1   ? 2.792  -4.169  2.748   1   49.074  ? 13  GLY   B H2   1 c 1 
ATOM   7    H H3   . GLY   A 1 1   ? 2.893  -4.328  4.209   1   50.161  ? 13  GLY   B H3   1 c 1 
ATOM   8    H HA2  . GLY   A 1 1   ? 4.003  -6.323  3.982   1   51.9    ? 13  GLY   B HA2  1 c 1 
ATOM   9    H HA3  . GLY   A 1 1   ? 3.884  -6.161  2.396   1   50.754  ? 13  GLY   B HA3  1 c 1 
ATOM   10   N N    . ALA   A 1 2   ? 6.276  -5.371  2.528   1   48.58   ? 14  ALA   B N    1 ? 1 
ATOM   11   C CA   . ALA   A 1 2   ? 7.619  -4.884  2.788   1   44.248  ? 14  ALA   B CA   1 ? 1 
ATOM   12   C C    . ALA   A 1 2   ? 7.696  -3.418  2.38    1   34.677  ? 14  ALA   B C    1 ? 1 
ATOM   13   O O    . ALA   A 1 2   ? 8.277  -2.621  3.071   1   33.673  ? 14  ALA   B O    1 ? 1 
ATOM   14   C CB   . ALA   A 1 2   ? 8.663  -5.735  2.079   1   42.52   ? 14  ALA   B CB   1 ? 1 
ATOM   15   H H    . ALA   A 1 2   ? 6.136  -6.018  1.898   1   48.999  ? 14  ALA   B H    1 c 1 
ATOM   16   H HA   . ALA   A 1 2   ? 7.779  -4.937  3.771   1   43.401  ? 14  ALA   B HA   1 c 1 
ATOM   17   H HB1  . ALA   A 1 2   ? 8.659  -6.633  2.45    1   44.434  ? 14  ALA   B HB1  1 c 1 
ATOM   18   H HB2  . ALA   A 1 2   ? 8.462  -5.78   1.13    1   42.695  ? 14  ALA   B HB2  1 c 1 
ATOM   19   H HB3  . ALA   A 1 2   ? 9.544  -5.341  2.202   1   41.645  ? 14  ALA   B HB3  1 c 1 
ATOM   20   N N    . PRO   A 1 3   ? 7.169  -2.971  1.236   1   37.538  ? 15  PRO   B N    1 ? 1 
ATOM   21   C CA   . PRO   A 1 3   ? 7.233  -1.535  0.943   1   37.771  ? 15  PRO   B CA   1 ? 1 
ATOM   22   C C    . PRO   A 1 3   ? 6.648  -0.615  2.024   1   36.272  ? 15  PRO   B C    1 ? 1 
ATOM   23   O O    . PRO   A 1 3   ? 7.295  0.373   2.403   1   32.953  ? 15  PRO   B O    1 ? 1 
ATOM   24   C CB   . PRO   A 1 3   ? 6.479  -1.399  -0.436  1   41.522  ? 15  PRO   B CB   1 ? 1 
ATOM   25   C CG   . PRO   A 1 3   ? 6.365  -2.823  -0.996  1   43.41   ? 15  PRO   B CG   1 ? 1 
ATOM   26   C CD   . PRO   A 1 3   ? 6.507  -3.769  0.184   1   42.153  ? 15  PRO   B CD   1 ? 1 
ATOM   27   H HA   . PRO   A 1 3   ? 8.185  -1.3    0.806   1   36.273  ? 15  PRO   B HA   1 c 1 
ATOM   28   H HB2  . PRO   A 1 3   ? 5.585  -1.004  -0.306  1   41.65   ? 15  PRO   B HB2  1 c 1 
ATOM   29   H HB3  . PRO   A 1 3   ? 6.987  -0.822  -1.054  1   39.553  ? 15  PRO   B HB3  1 c 1 
ATOM   30   H HG2  . PRO   A 1 3   ? 5.497  -2.951  -1.433  1   43.885  ? 15  PRO   B HG2  1 c 1 
ATOM   31   H HG3  . PRO   A 1 3   ? 7.071  -2.99   -1.654  1   41.868  ? 15  PRO   B HG3  1 c 1 
ATOM   32   H HD2  . PRO   A 1 3   ? 5.625  -4.082  0.482   1   43.63   ? 15  PRO   B HD2  1 c 1 
ATOM   33   H HD3  . PRO   A 1 3   ? 7.052  -4.548  -0.061  1   42.072  ? 15  PRO   B HD3  1 c 1 
ATOM   34   N N    . ALA   A 1 4   ? 5.472  -0.97   2.56    1   34.769  ? 16  ALA   B N    1 ? 1 
ATOM   35   C CA   . ALA   A 1 4   ? 4.823  -0.168  3.572   1   38.728  ? 16  ALA   B CA   1 ? 1 
ATOM   36   C C    . ALA   A 1 4   ? 5.728  -0.096  4.805   1   39.795  ? 16  ALA   B C    1 ? 1 
ATOM   37   O O    . ALA   A 1 4   ? 5.704  0.908   5.523   1   35.998  ? 16  ALA   B O    1 ? 1 
ATOM   38   C CB   . ALA   A 1 4   ? 3.486  -0.797  3.933   1   44.281  ? 16  ALA   B CB   1 ? 1 
ATOM   39   H H    . ALA   A 1 4   ? 5.064  -1.738  2.278   1   37.432  ? 16  ALA   B H    1 c 1 
ATOM   40   H HA   . ALA   A 1 4   ? 4.683  0.753   3.216   1   38.089  ? 16  ALA   B HA   1 c 1 
ATOM   41   H HB1  . ALA   A 1 4   ? 2.925  -0.85   3.141   1   43.856  ? 16  ALA   B HB1  1 c 1 
ATOM   42   H HB2  . ALA   A 1 4   ? 3.63   -1.692  4.285   1   44.328  ? 16  ALA   B HB2  1 c 1 
ATOM   43   H HB3  . ALA   A 1 4   ? 3.041  -0.255  4.606   1   44.245  ? 16  ALA   B HB3  1 c 1 
ATOM   44   N N    . THR   A 1 5   ? 6.371  -1.247  5.141   1   39.701  ? 17  THR   B N    1 ? 1 
ATOM   45   C CA   . THR   A 1 5   ? 7.235  -1.325  6.309   1   34.505  ? 17  THR   B CA   1 ? 1 
ATOM   46   C C    . THR   A 1 5   ? 8.357  -0.319  6.119   1   32.872  ? 17  THR   B C    1 ? 1 
ATOM   47   O O    . THR   A 1 5   ? 8.737  0.371   7.054   1   35.263  ? 17  THR   B O    1 ? 1 
ATOM   48   C CB   . THR   A 1 5   ? 7.739  -2.768  6.478   1   41.082  ? 17  THR   B CB   1 ? 1 
ATOM   49   O OG1  . THR   A 1 5   ? 6.533  -3.472  6.773   1   43.995  ? 17  THR   B OG1  1 ? 1 
ATOM   50   C CG2  . THR   A 1 5   ? 8.772  -2.953  7.585   1   41.427  ? 17  THR   B CG2  1 ? 1 
ATOM   51   H H    . THR   A 1 5   ? 6.255  -1.995  4.628   1   38.923  ? 17  THR   B H    1 c 1 
ATOM   52   H HA   . THR   A 1 5   ? 6.713  -1.076  7.103   1   37.748  ? 17  THR   B HA   1 c 1 
ATOM   53   H HB   . THR   A 1 5   ? 8.111  -3.097  5.625   1   39.17   ? 17  THR   B HB   1 c 1 
ATOM   54   H HG1  . THR   A 1 5   ? 6.179  -3.14   7.493   0   30      ? 17  THR   B HG1  1 c 1 
ATOM   55   H HG21 . THR   A 1 5   ? 8.856  -3.898  7.796   1   42.608  ? 17  THR   B HG21 1 c 1 
ATOM   56   H HG22 . THR   A 1 5   ? 8.489  -2.469  8.378   1   42.075  ? 17  THR   B HG22 1 c 1 
ATOM   57   H HG23 . THR   A 1 5   ? 9.632  -2.612  7.288   1   39.871  ? 17  THR   B HG23 1 c 1 
ATOM   58   N N    . VAL   A 1 6   ? 8.9    -0.226  4.882   1   32.715  ? 18  VAL   B N    1 ? 1 
ATOM   59   C CA   . VAL   A 1 6   ? 9.997  0.709   4.657   1   31.132  ? 18  VAL   B CA   1 ? 1 
ATOM   60   C C    . VAL   A 1 6   ? 9.502  2.155   4.783   1   32.406  ? 18  VAL   B C    1 ? 1 
ATOM   61   O O    . VAL   A 1 6   ? 10.148 2.986   5.417   1   32.067  ? 18  VAL   B O    1 ? 1 
ATOM   62   C CB   . VAL   A 1 6   ? 10.687 0.528   3.289   1   30.32   ? 18  VAL   B CB   1 ? 1 
ATOM   63   C CG1  . VAL   A 1 6   ? 11.81  1.537   3.161   1   27.254  ? 18  VAL   B CG1  1 ? 1 
ATOM   64   C CG2  . VAL   A 1 6   ? 11.186 -0.898  3.135   1   32.602  ? 18  VAL   B CG2  1 ? 1 
ATOM   65   H H    . VAL   A 1 6   ? 8.59   -0.738  4.192   1   32.576  ? 18  VAL   B H    1 c 1 
ATOM   66   H HA   . VAL   A 1 6   ? 10.666 0.558   5.351   1   31.64   ? 18  VAL   B HA   1 c 1 
ATOM   67   H HB   . VAL   A 1 6   ? 10.016 0.708   2.59    1   30.132  ? 18  VAL   B HB   1 c 1 
ATOM   68   H HG11 . VAL   A 1 6   ? 12.254 1.643   4.019   1   28.092  ? 18  VAL   B HG11 1 c 1 
ATOM   69   H HG12 . VAL   A 1 6   ? 11.448 2.393   2.877   1   27.446  ? 18  VAL   B HG12 1 c 1 
ATOM   70   H HG13 . VAL   A 1 6   ? 12.453 1.226   2.502   1   27.232  ? 18  VAL   B HG13 1 c 1 
ATOM   71   H HG21 . VAL   A 1 6   ? 11.75  -0.962  2.346   1   31.274  ? 18  VAL   B HG21 1 c 1 
ATOM   72   H HG22 . VAL   A 1 6   ? 10.431 -1.499  3.039   1   32.991  ? 18  VAL   B HG22 1 c 1 
ATOM   73   H HG23 . VAL   A 1 6   ? 11.701 -1.149  3.921   1   32.474  ? 18  VAL   B HG23 1 c 1 
ATOM   74   N N    . THR   A 1 7   ? 8.311  2.46    4.235   1   34.568  ? 19  THR   B N    1 ? 1 
ATOM   75   C CA   . THR   A 1 7   ? 7.685  3.759   4.399   1   32.493  ? 19  THR   B CA   1 ? 1 
ATOM   76   C C    . THR   A 1 7   ? 7.586  4.067   5.883   1   35.544  ? 19  THR   B C    1 ? 1 
ATOM   77   O O    . THR   A 1 7   ? 7.934  5.176   6.3     1   32.474  ? 19  THR   B O    1 ? 1 
ATOM   78   C CB   . THR   A 1 7   ? 6.306  3.769   3.73    1   37.056  ? 19  THR   B CB   1 ? 1 
ATOM   79   O OG1  . THR   A 1 7   ? 6.551  3.605   2.326   1   34.433  ? 19  THR   B OG1  1 ? 1 
ATOM   80   C CG2  . THR   A 1 7   ? 5.507  5.02    4.05    1   37.819  ? 19  THR   B CG2  1 ? 1 
ATOM   81   H H    . THR   A 1 7   ? 7.88   1.828   3.735   1   33.953  ? 19  THR   B H    1 c 1 
ATOM   82   H HA   . THR   A 1 7   ? 8.252  4.436   3.969   1   32.84   ? 19  THR   B HA   1 c 1 
ATOM   83   H HB   . THR   A 1 7   ? 5.791  2.992   4.053   1   37.171  ? 19  THR   B HB   1 c 1 
ATOM   84   H HG1  . THR   A 1 7   ? 7.057  4.261   2.032   0   30      ? 19  THR   B HG1  1 c 1 
ATOM   85   H HG21 . THR   A 1 7   ? 4.835  5.16    3.361   1   38.238  ? 19  THR   B HG21 1 c 1 
ATOM   86   H HG22 . THR   A 1 7   ? 6.102  5.788   4.08    1   37.047  ? 19  THR   B HG22 1 c 1 
ATOM   87   H HG23 . THR   A 1 7   ? 5.069  4.916   4.911   1   39.115  ? 19  THR   B HG23 1 c 1 
ATOM   88   N N    . GLU   A 1 8   ? 7.218  3.06    6.699   1   35.589  ? 20  GLU   B N    1 ? 1 
ATOM   89   C CA   . GLU   A 1 8   ? 6.917  3.357   8.109   1   39.449  ? 20  GLU   B CA   1 ? 1 
ATOM   90   C C    . GLU   A 1 8   ? 8.203  3.478   8.946   1   42.767  ? 20  GLU   B C    1 ? 1 
ATOM   91   O O    . GLU   A 1 8   ? 8.243  4.244   9.936   1   39.583  ? 20  GLU   B O    1 ? 1 
ATOM   92   C CB   . GLU   A 1 8   ? 6.006  2.378   8.882   1   44.802  ? 20  GLU   B CB   1 ? 1 
ATOM   93   H H    . GLU   A 1 8   ? 7.139  2.205   6.388   1   36.533  ? 20  GLU   B H    1 c 1 
ATOM   94   H HA   . GLU   A 1 8   ? 6.462  4.237   8.135   1   40.44   ? 20  GLU   B HA   1 c 1 
ATOM   95   H HB2  . GLU   A 1 8   ? 6.562  1.708   9.354   0   30      ? 20  GLU   B HB2  1 c 1 
ATOM   96   H HB3  . GLU   A 1 8   ? 5.061  2.58    8.699   0   30      ? 20  GLU   B HB3  1 c 1 
ATOM   97   N N    . GLN   A 1 9   ? 9.203  2.637   8.66    1   38.891  ? 21  GLN   B N    1 ? 1 
ATOM   98   C CA   . GLN   A 1 9   ? 10.293 2.426   9.617   1   40.193  ? 21  GLN   B CA   1 ? 1 
ATOM   99   C C    . GLN   A 1 9   ? 11.675 2.669   9.006   1   38.144  ? 21  GLN   B C    1 ? 1 
ATOM   100  O O    . GLN   A 1 9   ? 12.671 2.548   9.754   1   35.765  ? 21  GLN   B O    1 ? 1 
ATOM   101  C CB   . GLN   A 1 9   ? 10.356 1.002   10.153  1   41.534  ? 21  GLN   B CB   1 ? 1 
ATOM   102  C CG   . GLN   A 1 9   ? 9.068  0.663   10.903  1   47.311  ? 21  GLN   B CG   1 ? 1 
ATOM   103  C CD   . GLN   A 1 9   ? 8.989  -0.793  11.268  1   52.577  ? 21  GLN   B CD   1 ? 1 
ATOM   104  O OE1  . GLN   A 1 9   ? 9.978  -1.524  11.225  1   49.131  ? 21  GLN   B OE1  1 ? 1 
ATOM   105  N NE2  . GLN   A 1 9   ? 7.817  -1.196  11.699  1   60.519  ? 21  GLN   B NE2  1 ? 1 
ATOM   106  H H    . GLN   A 1 9   ? 9.2    2.169   7.875   1   38.986  ? 21  GLN   B H    1 c 1 
ATOM   107  H HA   . GLN   A 1 9   ? 10.173 3.046   10.379  1   40.808  ? 21  GLN   B HA   1 c 1 
ATOM   108  H HB2  . GLN   A 1 9   ? 10.476 0.376   9.408   1   41.622  ? 21  GLN   B HB2  1 c 1 
ATOM   109  H HB3  . GLN   A 1 9   ? 11.119 0.908   10.76   1   42.593  ? 21  GLN   B HB3  1 c 1 
ATOM   110  H HG2  . GLN   A 1 9   ? 9.016  1.202   11.719  1   48.162  ? 21  GLN   B HG2  1 c 1 
ATOM   111  H HG3  . GLN   A 1 9   ? 8.296  0.891   10.343  1   47.064  ? 21  GLN   B HG3  1 c 1 
ATOM   112  H HE21 . GLN   A 1 9   ? 7.665  -2.062  11.821  1   59.752  ? 21  GLN   B HE21 1 c 1 
ATOM   113  H HE22 . GLN   A 1 9   ? 7.177  -0.605  11.869  1   59.058  ? 21  GLN   B HE22 1 c 1 
ATOM   114  N N    . GLY   A 1 10  ? 11.743 2.911   7.681   1   33.567  ? 22  GLY   B N    1 ? 1 
ATOM   115  C CA   . GLY   A 1 10  ? 13.074 2.945   7.09    1   32.711  ? 22  GLY   B CA   1 ? 1 
ATOM   116  C C    . GLY   A 1 10  ? 13.735 4.288   7.35    1   29.379  ? 22  GLY   B C    1 ? 1 
ATOM   117  O O    . GLY   A 1 10  ? 13.089 5.303   7.684   1   30.297  ? 22  GLY   B O    1 ? 1 
ATOM   118  H H    . GLY   A 1 10  ? 11.002 3.061   7.168   1   34.209  ? 22  GLY   B H    1 c 1 
ATOM   119  H HA2  . GLY   A 1 10  ? 13.623 2.22    7.473   1   32.344  ? 22  GLY   B HA2  1 c 1 
ATOM   120  H HA3  . GLY   A 1 10  ? 13.002 2.794   6.118   1   31.03   ? 22  GLY   B HA3  1 c 1 
ATOM   121  N N    . GLU   A 1 11  ? 15.076 4.239   7.338   1   30.753  ? 23  GLU   B N    1 ? 1 
ATOM   122  C CA   . GLU   A 1 11  ? 15.871 5.444   7.517   1   29.029  ? 23  GLU   B CA   1 ? 1 
ATOM   123  C C    . GLU   A 1 11  ? 15.968 6.193   6.198   1   27.208  ? 23  GLU   B C    1 ? 1 
ATOM   124  O O    . GLU   A 1 11  ? 16.203 5.552   5.185   1   27.793  ? 23  GLU   B O    1 ? 1 
ATOM   125  C CB   . GLU   A 1 11  ? 17.229 4.854   7.97    1   31.29   ? 23  GLU   B CB   1 ? 1 
ATOM   126  C CG   . GLU   A 1 11  ? 18.407 5.828   7.942   1   38.218  ? 23  GLU   B CG   1 ? 1 
ATOM   127  C CD   . GLU   A 1 11  ? 19.808 5.236   8.236   1   46.418  ? 23  GLU   B CD   1 ? 1 
ATOM   128  O OE1  . GLU   A 1 11  ? 20.154 3.995   8.222   1   48.733  ? 23  GLU   B OE1  1 ? 1 
ATOM   129  O OE2  . GLU   A 1 11  ? 20.607 6.149   8.51    1   45.182  ? 23  GLU   B OE2  1 ? 1 
ATOM   130  H H    . GLU   A 1 11  ? 15.498 3.438   7.209   1   29.942  ? 23  GLU   B H    1 c 1 
ATOM   131  H HA   . GLU   A 1 11  ? 15.465 6.015   8.218   1   30.322  ? 23  GLU   B HA   1 c 1 
ATOM   132  H HB2  . GLU   A 1 11  ? 17.131 4.509   8.882   1   33.265  ? 23  GLU   B HB2  1 c 1 
ATOM   133  H HB3  . GLU   A 1 11  ? 17.456 4.098   7.389   1   31.715  ? 23  GLU   B HB3  1 c 1 
ATOM   134  H HG2  . GLU   A 1 11  ? 18.441 6.253   7.059   1   37.119  ? 23  GLU   B HG2  1 c 1 
ATOM   135  H HG3  . GLU   A 1 11  ? 18.236 6.541   8.593   1   38.784  ? 23  GLU   B HG3  1 c 1 
ATOM   136  N N    . ASP   A 1 12  ? 15.996 7.507   6.236   1   25.576  ? 24  ASP   B N    1 ? 1 
ATOM   137  C CA   . ASP   A 1 12  ? 16.18  8.313   5.037   1   26.295  ? 24  ASP   B CA   1 ? 1 
ATOM   138  C C    . ASP   A 1 12  ? 17.681 8.497   4.827   1   25.428  ? 24  ASP   B C    1 ? 1 
ATOM   139  O O    . ASP   A 1 12  ? 18.339 9.074   5.682   1   28.673  ? 24  ASP   B O    1 ? 1 
ATOM   140  C CB   . ASP   A 1 12  ? 15.533 9.672   5.249   1   27.415  ? 24  ASP   B CB   1 ? 1 
ATOM   141  C CG   . ASP   A 1 12  ? 15.653 10.676  4.118   1   28.17   ? 24  ASP   B CG   1 ? 1 
ATOM   142  O OD1  . ASP   A 1 12  ? 16.289 10.342  3.125   1   25.338  ? 24  ASP   B OD1  1 ? 1 
ATOM   143  O OD2  . ASP   A 1 12  ? 15.053 11.761  4.201   1   27.422  ? 24  ASP   B OD2  1 ? 1 
ATOM   144  H H    . ASP   A 1 12  ? 15.899 7.932   7.04    1   27.273  ? 24  ASP   B H    1 c 1 
ATOM   145  H HA   . ASP   A 1 12  ? 15.786 7.852   4.265   1   25.156  ? 24  ASP   B HA   1 c 1 
ATOM   146  H HB2  . ASP   A 1 12  ? 14.578 9.532   5.422   1   27.628  ? 24  ASP   B HB2  1 c 1 
ATOM   147  H HB3  . ASP   A 1 12  ? 15.92  10.08   6.052   1   28.481  ? 24  ASP   B HB3  1 c 1 
ATOM   148  N N    . ILE   A 1 13  ? 18.258 7.926   3.779   1   26.136  ? 25  ILE   B N    1 ? 1 
ATOM   149  C CA   . ILE   A 1 13  ? 19.709 7.994   3.574   1   28.28   ? 25  ILE   B CA   1 ? 1 
ATOM   150  C C    . ILE   A 1 13  ? 20.02  9.011   2.469   1   30.824  ? 25  ILE   B C    1 ? 1 
ATOM   151  O O    . ILE   A 1 13  ? 21.148 9.005   1.935   1   27.335  ? 25  ILE   B O    1 ? 1 
ATOM   152  C CB   . ILE   A 1 13  ? 20.264 6.599   3.222   1   29.371  ? 25  ILE   B CB   1 ? 1 
ATOM   153  C CG1  . ILE   A 1 13  ? 19.505 5.978   2.003   1   28.168  ? 25  ILE   B CG1  1 ? 1 
ATOM   154  C CG2  . ILE   A 1 13  ? 20.172 5.618   4.421   1   35.111  ? 25  ILE   B CG2  1 ? 1 
ATOM   155  C CD1  . ILE   A 1 13  ? 20.194 4.765   1.433   1   31.008  ? 25  ILE   B CD1  1 ? 1 
ATOM   156  H H    . ILE   A 1 13  ? 17.741 7.496   3.161   1   25.437  ? 25  ILE   B H    1 c 1 
ATOM   157  H HA   . ILE   A 1 13  ? 20.131 8.293   4.402   1   29.547  ? 25  ILE   B HA   1 c 1 
ATOM   158  H HB   . ILE   A 1 13  ? 21.206 6.696   2.977   1   30.46   ? 25  ILE   B HB   1 c 1 
ATOM   159  H HG12 . ILE   A 1 13  ? 18.604 5.724   2.286   1   28.474  ? 25  ILE   B HG12 1 c 1 
ATOM   160  H HG13 . ILE   A 1 13  ? 19.422 6.654   1.3     1   28.603  ? 25  ILE   B HG13 1 c 1 
ATOM   161  H HG21 . ILE   A 1 13  ? 20.699 4.823   4.234   1   33.582  ? 25  ILE   B HG21 1 c 1 
ATOM   162  H HG22 . ILE   A 1 13  ? 19.245 5.363   4.563   1   33.069  ? 25  ILE   B HG22 1 c 1 
ATOM   163  H HG23 . ILE   A 1 13  ? 20.514 6.05    5.222   1   34.356  ? 25  ILE   B HG23 1 c 1 
ATOM   164  H HD11 . ILE   A 1 13  ? 21.153 4.932   1.374   1   30.666  ? 25  ILE   B HD11 1 c 1 
ATOM   165  H HD12 . ILE   A 1 13  ? 19.844 4.575   0.542   1   29.549  ? 25  ILE   B HD12 1 c 1 
ATOM   166  H HD13 . ILE   A 1 13  ? 20.034 3.997   2.014   1   30.28   ? 25  ILE   B HD13 1 c 1 
ATOM   167  N N    . THR   A 1 14  ? 19.056 9.889   2.128   1   26.781  ? 26  THR   B N    1 ? 1 
ATOM   168  C CA   . THR   A 1 14  ? 19.334 11.016  1.211   1   32.048  ? 26  THR   B CA   1 ? 1 
ATOM   169  C C    . THR   A 1 14  ? 20.114 12.116  1.938   1   31.304  ? 26  THR   B C    1 ? 1 
ATOM   170  O O    . THR   A 1 14  ? 19.84  12.376  3.115   1   34.502  ? 26  THR   B O    1 ? 1 
ATOM   171  C CB   . THR   A 1 14  ? 18.071 11.595  0.564   1   27.569  ? 26  THR   B CB   1 ? 1 
ATOM   172  O OG1  . THR   A 1 14  ? 17.215 12.151  1.553   1   27.785  ? 26  THR   B OG1  1 ? 1 
ATOM   173  C CG2  . THR   A 1 14  ? 17.432 10.518  -0.287  1   28.666  ? 26  THR   B CG2  1 ? 1 
ATOM   174  H H    . THR   A 1 14  ? 18.211 9.792   2.461   1   28.329  ? 26  THR   B H    1 c 1 
ATOM   175  H HA   . THR   A 1 14  ? 19.901 10.671  0.49    1   29.734  ? 26  THR   B HA   1 c 1 
ATOM   176  H HB   . THR   A 1 14  ? 18.347 12.32   -0.047  1   29.269  ? 26  THR   B HB   1 c 1 
ATOM   177  H HG1  . THR   A 1 14  ? 16.978 11.534  2.104   0   30      ? 26  THR   B HG1  1 c 1 
ATOM   178  H HG21 . THR   A 1 14  ? 16.619 10.863  -0.692  1   27.844  ? 26  THR   B HG21 1 c 1 
ATOM   179  H HG22 . THR   A 1 14  ? 17.215 9.751   0.269   1   27.501  ? 26  THR   B HG22 1 c 1 
ATOM   180  H HG23 . THR   A 1 14  ? 18.05  10.246  -0.986  1   27.81   ? 26  THR   B HG23 1 c 1 
ATOM   181  N N    . SER   A 1 15  ? 20.913 12.889  1.163   1   31.397  ? 27  SER   B N    1 ? 1 
ATOM   182  C CA   . SER   A 1 15  ? 21.639 14.033  1.696   1   35.837  ? 27  SER   B CA   1 ? 1 
ATOM   183  C C    . SER   A 1 15  ? 20.678 15.166  1.985   1   34.965  ? 27  SER   B C    1 ? 1 
ATOM   184  O O    . SER   A 1 15  ? 20.852 15.916  2.953   1   32.345  ? 27  SER   B O    1 ? 1 
ATOM   185  C CB   . SER   A 1 15  ? 22.771 14.495  0.798   1   43.738  ? 27  SER   B CB   1 ? 1 
ATOM   186  O OG   . SER   A 1 15  ? 23.743 13.437  0.727   1   47.537  ? 27  SER   B OG   1 ? 1 
ATOM   187  H H    . SER   A 1 15  ? 21.001 12.689  0.276   1   31.781  ? 27  SER   B H    1 c 1 
ATOM   188  H HA   . SER   A 1 15  ? 22.038 13.754  2.559   1   36.555  ? 27  SER   B HA   1 c 1 
ATOM   189  H HB2  . SER   A 1 15  ? 22.428 14.692  -0.094  1   42.633  ? 27  SER   B HB2  1 c 1 
ATOM   190  H HB3  . SER   A 1 15  ? 23.181 15.3    1.167   1   44.556  ? 27  SER   B HB3  1 c 1 
ATOM   191  H HG   . SER   A 1 15  ? 24.381 13.685  0.287   0   30      ? 27  SER   B HG   1 c 1 
ATOM   192  N N    . LYS   A 1 16  ? 19.691 15.279  1.125   1   36.637  ? 28  LYS   B N    1 ? 1 
ATOM   193  C CA   . LYS   A 1 16  ? 18.704 16.335  1.208   1   41.054  ? 28  LYS   B CA   1 ? 1 
ATOM   194  C C    . LYS   A 1 16  ? 17.672 16.048  2.3     1   37.56   ? 28  LYS   B C    1 ? 1 
ATOM   195  O O    . LYS   A 1 16  ? 16.924 16.949  2.661   1   34.295  ? 28  LYS   B O    1 ? 1 
ATOM   196  C CB   . LYS   A 1 16  ? 17.951 16.559  -0.108  1   43.418  ? 28  LYS   B CB   1 ? 1 
ATOM   197  C CG   . LYS   A 1 16  ? 18.813 17.218  -1.168  1   51.434  ? 28  LYS   B CG   1 ? 1 
ATOM   198  C CD   . LYS   A 1 16  ? 18.038 17.473  -2.449  1   57.52   ? 28  LYS   B CD   1 ? 1 
ATOM   199  C CE   . LYS   A 1 16  ? 18.962 17.375  -3.599  1   66.219  ? 28  LYS   B CE   1 ? 1 
ATOM   200  N NZ   . LYS   A 1 16  ? 18.215 17.713  -4.817  1   80.385  ? 28  LYS   B NZ   1 ? 1 
ATOM   201  H H    . LYS   A 1 16  ? 19.624 14.677  0.441   1   35.715  ? 28  LYS   B H    1 c 1 
ATOM   202  H HA   . LYS   A 1 16  ? 19.174 17.178  1.438   1   41.737  ? 28  LYS   B HA   1 c 1 
ATOM   203  H HB2  . LYS   A 1 16  ? 17.635 15.696  -0.449  1   42.803  ? 28  LYS   B HB2  1 c 1 
ATOM   204  H HB3  . LYS   A 1 16  ? 17.168 17.126  0.058   1   44.595  ? 28  LYS   B HB3  1 c 1 
ATOM   205  H HG2  . LYS   A 1 16  ? 19.153 18.071  -0.818  1   52.679  ? 28  LYS   B HG2  1 c 1 
ATOM   206  H HG3  . LYS   A 1 16  ? 19.581 16.636  -1.359  1   50.8    ? 28  LYS   B HG3  1 c 1 
ATOM   207  H HD2  . LYS   A 1 16  ? 17.323 16.807  -2.546  1   56.289  ? 28  LYS   B HD2  1 c 1 
ATOM   208  H HD3  . LYS   A 1 16  ? 17.64  18.37   -2.423  1   59.089  ? 28  LYS   B HD3  1 c 1 
ATOM   209  H HE2  . LYS   A 1 16  ? 19.705 17.996  -3.489  1   68.512  ? 28  LYS   B HE2  1 c 1 
ATOM   210  H HE3  . LYS   A 1 16  ? 19.314 16.471  -3.675  1   65.802  ? 28  LYS   B HE3  1 c 1 
ATOM   211  H HZ1  . LYS   A 1 16  ? 17.884 18.554  -4.754  1   76.654  ? 28  LYS   B HZ1  1 c 1 
ATOM   212  H HZ2  . LYS   A 1 16  ? 17.531 17.13   -4.93   1   74.353  ? 28  LYS   B HZ2  1 c 1 
ATOM   213  H HZ3  . LYS   A 1 16  ? 18.766 17.665  -5.534  1   76.104  ? 28  LYS   B HZ3  1 c 1 
ATOM   214  N N    . LYS   A 1 17  ? 17.606 14.818  2.809   1   35.962  ? 29  LYS   B N    1 ? 1 
ATOM   215  C CA   . LYS   A 1 17  ? 16.519 14.445  3.73    1   33.539  ? 29  LYS   B CA   1 ? 1 
ATOM   216  C C    . LYS   A 1 17  ? 15.109 14.781  3.166   1   37.5    ? 29  LYS   B C    1 ? 1 
ATOM   217  O O    . LYS   A 1 17  ? 14.241 15.352  3.867   1   33.601  ? 29  LYS   B O    1 ? 1 
ATOM   218  C CB   . LYS   A 1 17  ? 16.66  15.085  5.108   1   35.699  ? 29  LYS   B CB   1 ? 1 
ATOM   219  C CG   . LYS   A 1 17  ? 17.94  14.559  5.815   1   39.418  ? 29  LYS   B CG   1 ? 1 
ATOM   220  C CD   . LYS   A 1 17  ? 17.99  13.063  6.131   1   49.161  ? 29  LYS   B CD   1 ? 1 
ATOM   221  C CE   . LYS   A 1 17  ? 19.11  12.645  7.118   1   59.846  ? 29  LYS   B CE   1 ? 1 
ATOM   222  N NZ   . LYS   A 1 17  ? 20.116 11.839  6.399   1   59.109  ? 29  LYS   B NZ   1 ? 1 
ATOM   223  H H    . LYS   A 1 17  ? 18.23  14.191  2.585   1   34.932  ? 29  LYS   B H    1 c 1 
ATOM   224  H HA   . LYS   A 1 17  ? 16.565 13.467  3.854   1   33.839  ? 29  LYS   B HA   1 c 1 
ATOM   225  H HB2  . LYS   A 1 17  ? 16.716 16.061  5.022   1   37.497  ? 29  LYS   B HB2  1 c 1 
ATOM   226  H HB3  . LYS   A 1 17  ? 15.878 14.867  5.659   1   36.315  ? 29  LYS   B HB3  1 c 1 
ATOM   227  H HG2  . LYS   A 1 17  ? 18.711 14.782  5.25    1   40.97   ? 29  LYS   B HG2  1 c 1 
ATOM   228  H HG3  . LYS   A 1 17  ? 18.046 15.056  6.655   1   42.246  ? 29  LYS   B HG3  1 c 1 
ATOM   229  H HD2  . LYS   A 1 17  ? 17.123 12.794  6.506   1   47.877  ? 29  LYS   B HD2  1 c 1 
ATOM   230  H HD3  . LYS   A 1 17  ? 18.11  12.57   5.29    1   47.046  ? 29  LYS   B HD3  1 c 1 
ATOM   231  H HE2  . LYS   A 1 17  ? 19.538 13.435  7.494   1   58.655  ? 29  LYS   B HE2  1 c 1 
ATOM   232  H HE3  . LYS   A 1 17  ? 18.733 12.118  7.845   1   57.524  ? 29  LYS   B HE3  1 c 1 
ATOM   233  H HZ1  . LYS   A 1 17  ? 20.434 12.305  5.69    1   58.96   ? 29  LYS   B HZ1  1 c 1 
ATOM   234  H HZ2  . LYS   A 1 17  ? 19.74  11.068  6.106   1   57.84   ? 29  LYS   B HZ2  1 c 1 
ATOM   235  H HZ3  . LYS   A 1 17  ? 20.802 11.641  6.956   1   59.84   ? 29  LYS   B HZ3  1 c 1 
ATOM   236  N N    . ASP   A 1 18  ? 14.873 14.293  1.949   1   36.077  ? 30  ASP   B N    1 ? 1 
ATOM   237  C CA   . ASP   A 1 18  ? 13.583 14.386  1.262   1   28.707  ? 30  ASP   B CA   1 ? 1 
ATOM   238  C C    . ASP   A 1 18  ? 12.862 13.045  1.207   1   30.542  ? 30  ASP   B C    1 ? 1 
ATOM   239  O O    . ASP   A 1 18  ? 11.979 12.824  0.348   1   29.3    ? 30  ASP   B O    1 ? 1 
ATOM   240  C CB   . ASP   A 1 18  ? 13.801 14.91   -0.155  1   30.407  ? 30  ASP   B CB   1 ? 1 
ATOM   241  C CG   . ASP   A 1 18  ? 14.778 14.097  -1.022  1   32.978  ? 30  ASP   B CG   1 ? 1 
ATOM   242  O OD1  . ASP   A 1 18  ? 14.996 12.932  -0.695  1   26.661  ? 30  ASP   B OD1  1 ? 1 
ATOM   243  O OD2  . ASP   A 1 18  ? 15.318 14.657  -2.012  1   31.462  ? 30  ASP   B OD2  1 ? 1 
ATOM   244  H H    . ASP   A 1 18  ? 15.556 13.865  1.52    1   33.679  ? 30  ASP   B H    1 c 1 
ATOM   245  H HA   . ASP   A 1 18  ? 13.016 15.03   1.742   1   31.854  ? 30  ASP   B HA   1 c 1 
ATOM   246  H HB2  . ASP   A 1 18  ? 12.939 14.95   -0.619  1   30.855  ? 30  ASP   B HB2  1 c 1 
ATOM   247  H HB3  . ASP   A 1 18  ? 14.146 15.825  -0.093  1   31.936  ? 30  ASP   B HB3  1 c 1 
ATOM   248  N N    . ARG   A 1 19  ? 13.353 12.07   1.982   1   28.369  ? 31  ARG   B N    1 ? 1 
ATOM   249  C CA   . ARG   A 1 19  ? 12.79  10.719  2.033   1   29.059  ? 31  ARG   B CA   1 ? 1 
ATOM   250  C C    . ARG   A 1 19  ? 12.726 10.031  0.65    1   28.158  ? 31  ARG   B C    1 ? 1 
ATOM   251  O O    . ARG   A 1 19  ? 11.97  9.071   0.437   1   31.054  ? 31  ARG   B O    1 ? 1 
ATOM   252  C CB   . ARG   A 1 19  ? 11.398 10.81   2.685   1   29.136  ? 31  ARG   B CB   1 ? 1 
ATOM   253  C CG   . ARG   A 1 19  ? 11.475 11.125  4.184   1   32.7    ? 31  ARG   B CG   1 ? 1 
ATOM   254  C CD   . ARG   A 1 19  ? 10.114 11.202  4.903   1   34.491  ? 31  ARG   B CD   1 ? 1 
ATOM   255  N NE   . ARG   A 1 19  ? 9.265  10.028  4.684   1   36.187  ? 31  ARG   B NE   1 ? 1 
ATOM   256  C CZ   . ARG   A 1 19  ? 9.263  8.804   5.267   1   35.364  ? 31  ARG   B CZ   1 ? 1 
ATOM   257  N NH1  . ARG   A 1 19  ? 10.107 8.516   6.251   1   31.379  ? 31  ARG   B NH1  1 ? 1 
ATOM   258  N NH2  . ARG   A 1 19  ? 8.34   7.895   4.858   1   40.737  ? 31  ARG   B NH2  1 ? 1 
ATOM   259  H H    . ARG   A 1 19  ? 14.075 12.252  2.51    1   29.438  ? 31  ARG   B H    1 c 1 
ATOM   260  H HA   . ARG   A 1 19  ? 13.366 10.171  2.622   1   28.442  ? 31  ARG   B HA   1 c 1 
ATOM   261  H HB2  . ARG   A 1 19  ? 10.872 11.507  2.239   1   30.331  ? 31  ARG   B HB2  1 c 1 
ATOM   262  H HB3  . ARG   A 1 19  ? 10.931 9.956   2.565   1   29.555  ? 31  ARG   B HB3  1 c 1 
ATOM   263  H HG2  . ARG   A 1 19  ? 12.022 10.438  4.622   1   31.936  ? 31  ARG   B HG2  1 c 1 
ATOM   264  H HG3  . ARG   A 1 19  ? 11.939 11.982  4.303   1   32.742  ? 31  ARG   B HG3  1 c 1 
ATOM   265  H HD2  . ARG   A 1 19  ? 10.269 11.308  5.863   1   35.644  ? 31  ARG   B HD2  1 c 1 
ATOM   266  H HD3  . ARG   A 1 19  ? 9.64   11.999  4.591   1   35.454  ? 31  ARG   B HD3  1 c 1 
ATOM   267  H HE   . ARG   A 1 19  ? 8.653  10.13   4.073   1   35.659  ? 31  ARG   B HE   1 c 1 
ATOM   268  H HH11 . ARG   A 1 19  ? 10.868 8.96    6.325   1   32.374  ? 31  ARG   B HH11 1 c 1 
ATOM   269  H HH12 . ARG   A 1 19  ? 9.904  7.877   6.828   1   33.136  ? 31  ARG   B HH12 1 c 1 
ATOM   270  H HH21 . ARG   A 1 19  ? 7.695  8.135   4.303   1   39.183  ? 31  ARG   B HH21 1 c 1 
ATOM   271  H HH22 . ARG   A 1 19  ? 8.389  7.062   5.15    1   39.003  ? 31  ARG   B HH22 1 c 1 
ATOM   272  N N    . GLY   A 1 20  ? 13.633 10.416  -0.247  1   31.961  ? 32  GLY   B N    1 ? 1 
ATOM   273  C CA   . GLY   A 1 20  ? 13.654 9.872   -1.6    1   30.283  ? 32  GLY   B CA   1 ? 1 
ATOM   274  C C    . GLY   A 1 20  ? 14.214 8.445   -1.67   1   30.95   ? 32  GLY   B C    1 ? 1 
ATOM   275  O O    . GLY   A 1 20  ? 13.952 7.71    -2.624  1   26.929  ? 32  GLY   B O    1 ? 1 
ATOM   276  H H    . GLY   A 1 20  ? 14.273 11.024  -0.01   1   31.024  ? 32  GLY   B H    1 c 1 
ATOM   277  H HA2  . GLY   A 1 20  ? 12.736 9.878   -1.959  1   30.97   ? 32  GLY   B HA2  1 c 1 
ATOM   278  H HA3  . GLY   A 1 20  ? 14.198 10.461  -2.167  1   31.036  ? 32  GLY   B HA3  1 c 1 
ATOM   279  N N    . VAL   A 1 21  ? 15.024 8.051   -0.679  1   26.488  ? 33  VAL   B N    1 ? 1 
ATOM   280  C CA   . VAL   A 1 21  ? 15.568 6.725   -0.549  1   23.794  ? 33  VAL   B CA   1 ? 1 
ATOM   281  C C    . VAL   A 1 21  ? 15.487 6.329   0.92    1   27.075  ? 33  VAL   B C    1 ? 1 
ATOM   282  O O    . VAL   A 1 21  ? 16.137 6.943   1.744   1   23.4    ? 33  VAL   B O    1 ? 1 
ATOM   283  C CB   . VAL   A 1 21  ? 17.003 6.615   -1.063  1   25.275  ? 33  VAL   B CB   1 ? 1 
ATOM   284  C CG1  . VAL   A 1 21  ? 17.56  5.19    -0.998  1   26.019  ? 33  VAL   B CG1  1 ? 1 
ATOM   285  C CG2  . VAL   A 1 21  ? 17.226 7.21    -2.467  1   27.596  ? 33  VAL   B CG2  1 ? 1 
ATOM   286  H H    . VAL   A 1 21  ? 15.25  8.666   -0.042  1   27.334  ? 33  VAL   B H    1 c 1 
ATOM   287  H HA   . VAL   A 1 21  ? 15.011 6.113   -1.066  1   24.839  ? 33  VAL   B HA   1 c 1 
ATOM   288  H HB   . VAL   A 1 21  ? 17.558 7.153   -0.45   1   25.946  ? 33  VAL   B HB   1 c 1 
ATOM   289  H HG11 . VAL   A 1 21  ? 16.973 4.59    -1.488  1   25.558  ? 33  VAL   B HG11 1 c 1 
ATOM   290  H HG12 . VAL   A 1 21  ? 17.615 4.903   -0.072  1   26.018  ? 33  VAL   B HG12 1 c 1 
ATOM   291  H HG13 . VAL   A 1 21  ? 18.447 5.169   -1.395  1   25.997  ? 33  VAL   B HG13 1 c 1 
ATOM   292  H HG21 . VAL   A 1 21  ? 18.134 7.023   -2.759  1   27.119  ? 33  VAL   B HG21 1 c 1 
ATOM   293  H HG22 . VAL   A 1 21  ? 17.088 8.171   -2.439  1   27.226  ? 33  VAL   B HG22 1 c 1 
ATOM   294  H HG23 . VAL   A 1 21  ? 16.597 6.811   -3.092  1   26.661  ? 33  VAL   B HG23 1 c 1 
ATOM   295  N N    . LEU   A 1 22  ? 14.67  5.308   1.188   1   24.586  ? 34  LEU   B N    1 ? 1 
ATOM   296  C CA   . LEU   A 1 22  ? 14.37  4.825   2.505   1   26.734  ? 34  LEU   B CA   1 ? 1 
ATOM   297  C C    . LEU   A 1 22  ? 14.93  3.415   2.584   1   23.65   ? 34  LEU   B C    1 ? 1 
ATOM   298  O O    . LEU   A 1 22  ? 14.787 2.625   1.648   1   25.793  ? 34  LEU   B O    1 ? 1 
ATOM   299  C CB   . LEU   A 1 22  ? 12.895 4.926   2.83    1   25.873  ? 34  LEU   B CB   1 ? 1 
ATOM   300  C CG   . LEU   A 1 22  ? 12.327 6.336   2.845   1   29.082  ? 34  LEU   B CG   1 ? 1 
ATOM   301  C CD1  . LEU   A 1 22  ? 10.817 6.066   2.896   1   34.162  ? 34  LEU   B CD1  1 ? 1 
ATOM   302  C CD2  . LEU   A 1 22  ? 12.735 7.226   3.987   1   31.348  ? 34  LEU   B CD2  1 ? 1 
ATOM   303  H H    . LEU   A 1 22  ? 14.272 4.884   0.482   1   25.258  ? 34  LEU   B H    1 c 1 
ATOM   304  H HA   . LEU   A 1 22  ? 14.868 5.384   3.15    1   25.86   ? 34  LEU   B HA   1 c 1 
ATOM   305  H HB2  . LEU   A 1 22  ? 12.399 4.395   2.164   1   26.77   ? 34  LEU   B HB2  1 c 1 
ATOM   306  H HB3  . LEU   A 1 22  ? 12.746 4.52    3.714   1   27.523  ? 34  LEU   B HB3  1 c 1 
ATOM   307  H HG   . LEU   A 1 22  ? 12.548 6.782   1.986   1   29.005  ? 34  LEU   B HG   1 c 1 
ATOM   308  H HD11 . LEU   A 1 22  ? 10.531 5.651   2.065   1   32.419  ? 34  LEU   B HD11 1 c 1 
ATOM   309  H HD12 . LEU   A 1 22  ? 10.342 6.905   3.018   1   33.23   ? 34  LEU   B HD12 1 c 1 
ATOM   310  H HD13 . LEU   A 1 22  ? 10.616 5.472   3.64    1   33.306  ? 34  LEU   B HD13 1 c 1 
ATOM   311  H HD21 . LEU   A 1 22  ? 13.7   7.333   3.985   1   30.557  ? 34  LEU   B HD21 1 c 1 
ATOM   312  H HD22 . LEU   A 1 22  ? 12.456 6.826   4.827   1   31.502  ? 34  LEU   B HD22 1 c 1 
ATOM   313  H HD23 . LEU   A 1 22  ? 12.314 8.097   3.887   1   31.176  ? 34  LEU   B HD23 1 c 1 
ATOM   314  N N    . LYS   A 1 23  ? 15.615 3.105   3.727   1   25.734  ? 35  LYS   B N    1 ? 1 
ATOM   315  C CA   . LYS   A 1 23  ? 16.346 1.865   3.864   1   26.414  ? 35  LYS   B CA   1 ? 1 
ATOM   316  C C    . LYS   A 1 23  ? 16.065 1.129   5.164   1   28.314  ? 35  LYS   B C    1 ? 1 
ATOM   317  O O    . LYS   A 1 23  ? 15.939 1.73    6.205   1   29.918  ? 35  LYS   B O    1 ? 1 
ATOM   318  C CB   . LYS   A 1 23  ? 17.863 2.125   3.838   1   27.224  ? 35  LYS   B CB   1 ? 1 
ATOM   319  C CG   . LYS   A 1 23  ? 18.761 0.929   3.971   1   25.78   ? 35  LYS   B CG   1 ? 1 
ATOM   320  C CD   . LYS   A 1 23  ? 20.264 1.141   4.078   1   27.473  ? 35  LYS   B CD   1 ? 1 
ATOM   321  C CE   . LYS   A 1 23  ? 21.059 -0.099  4.103   1   28.882  ? 35  LYS   B CE   1 ? 1 
ATOM   322  N NZ   . LYS   A 1 23  ? 22.476 -0.043  4.489   1   31.693  ? 35  LYS   B NZ   1 ? 1 
ATOM   323  H H    . LYS   A 1 23  ? 15.611 3.693   4.427   1   25.849  ? 35  LYS   B H    1 c 1 
ATOM   324  H HA   . LYS   A 1 23  ? 16.112 1.277   3.105   1   26.355  ? 35  LYS   B HA   1 c 1 
ATOM   325  H HB2  . LYS   A 1 23  ? 18.081 2.575   2.994   1   25.916  ? 35  LYS   B HB2  1 c 1 
ATOM   326  H HB3  . LYS   A 1 23  ? 18.078 2.747   4.565   1   26.92   ? 35  LYS   B HB3  1 c 1 
ATOM   327  H HG2  . LYS   A 1 23  ? 18.474 0.427   4.763   1   27.272  ? 35  LYS   B HG2  1 c 1 
ATOM   328  H HG3  . LYS   A 1 23  ? 18.592 0.347   3.198   1   26.252  ? 35  LYS   B HG3  1 c 1 
ATOM   329  H HD2  . LYS   A 1 23  ? 20.557 1.689   3.318   1   26.777  ? 35  LYS   B HD2  1 c 1 
ATOM   330  H HD3  . LYS   A 1 23  ? 20.449 1.651   4.896   1   27.822  ? 35  LYS   B HD3  1 c 1 
ATOM   331  H HE2  . LYS   A 1 23  ? 20.614 -0.72   4.708   1   29.692  ? 35  LYS   B HE2  1 c 1 
ATOM   332  H HE3  . LYS   A 1 23  ? 21.012 -0.495  3.215   1   28.766  ? 35  LYS   B HE3  1 c 1 
ATOM   333  H HZ1  . LYS   A 1 23  ? 22.547 0.183   5.364   1   31.808  ? 35  LYS   B HZ1  1 c 1 
ATOM   334  H HZ2  . LYS   A 1 23  ? 22.906 0.574   3.985   1   30.907  ? 35  LYS   B HZ2  1 c 1 
ATOM   335  H HZ3  . LYS   A 1 23  ? 22.861 -0.853  4.359   1   31.849  ? 35  LYS   B HZ3  1 c 1 
ATOM   336  N N    . ILE   A 1 24  ? 15.92  -0.176  5.04    1   29.074  ? 36  ILE   B N    1 ? 1 
ATOM   337  C CA   . ILE   A 1 24  ? 15.956 -1.076  6.223   1   31.143  ? 36  ILE   B CA   1 ? 1 
ATOM   338  C C    . ILE   A 1 24  ? 16.992 -2.164  5.981   1   30.899  ? 36  ILE   B C    1 ? 1 
ATOM   339  O O    . ILE   A 1 24  ? 17.037 -2.825  4.922   1   32.24   ? 36  ILE   B O    1 ? 1 
ATOM   340  C CB   . ILE   A 1 24  ? 14.586 -1.69   6.517   1   32.048  ? 36  ILE   B CB   1 ? 1 
ATOM   341  C CG1  . ILE   A 1 24  ? 13.515 -0.654  6.903   1   31.403  ? 36  ILE   B CG1  1 ? 1 
ATOM   342  C CG2  . ILE   A 1 24  ? 14.729 -2.641  7.705   1   39.17   ? 36  ILE   B CG2  1 ? 1 
ATOM   343  C CD1  . ILE   A 1 24  ? 12.087 -1.244  7.03    1   34.854  ? 36  ILE   B CD1  1 ? 1 
ATOM   344  H H    . ILE   A 1 24  ? 15.789 -0.542  4.212   1   28.729  ? 36  ILE   B H    1 c 1 
ATOM   345  H HA   . ILE   A 1 24  ? 16.23  -0.554  7.001   1   31.269  ? 36  ILE   B HA   1 c 1 
ATOM   346  H HB   . ILE   A 1 24  ? 14.282 -2.192  5.735   1   32.614  ? 36  ILE   B HB   1 c 1 
ATOM   347  H HG12 . ILE   A 1 24  ? 13.765 -0.246  7.757   1   32.551  ? 36  ILE   B HG12 1 c 1 
ATOM   348  H HG13 . ILE   A 1 24  ? 13.503 0.054   6.226   1   30.88   ? 36  ILE   B HG13 1 c 1 
ATOM   349  H HG21 . ILE   A 1 24  ? 13.851 -2.911  8.019   1   38.36   ? 36  ILE   B HG21 1 c 1 
ATOM   350  H HG22 . ILE   A 1 24  ? 15.205 -2.193  8.425   1   37.792  ? 36  ILE   B HG22 1 c 1 
ATOM   351  H HG23 . ILE   A 1 24  ? 15.226 -3.431  7.434   1   37.832  ? 36  ILE   B HG23 1 c 1 
ATOM   352  H HD11 . ILE   A 1 24  ? 11.876 -1.766  6.233   1   33.981  ? 36  ILE   B HD11 1 c 1 
ATOM   353  H HD12 . ILE   A 1 24  ? 11.443 -0.516  7.119   1   34.109  ? 36  ILE   B HD12 1 c 1 
ATOM   354  H HD13 . ILE   A 1 24  ? 12.03  -1.819  7.817   1   35.591  ? 36  ILE   B HD13 1 c 1 
ATOM   355  N N    . VAL   A 1 25  ? 17.842 -2.36   6.983   1   33.805  ? 37  VAL   B N    1 ? 1 
ATOM   356  C CA   . VAL   A 1 25  ? 18.713 -3.524  7.024   1   36.531  ? 37  VAL   B CA   1 ? 1 
ATOM   357  C C    . VAL   A 1 25  ? 17.887 -4.718  7.477   1   36.374  ? 37  VAL   B C    1 ? 1 
ATOM   358  O O    . VAL   A 1 25  ? 17.279 -4.726  8.55    1   32.595  ? 37  VAL   B O    1 ? 1 
ATOM   359  C CB   . VAL   A 1 25  ? 19.958 -3.291  7.893   1   38.026  ? 37  VAL   B CB   1 ? 1 
ATOM   360  C CG1  . VAL   A 1 25  ? 20.796 -4.558  8.002   1   38.247  ? 37  VAL   B CG1  1 ? 1 
ATOM   361  C CG2  . VAL   A 1 25  ? 20.815 -2.145  7.363   1   36.65   ? 37  VAL   B CG2  1 ? 1 
ATOM   362  H H    . VAL   A 1 25  ? 17.888 -1.752  7.664   1   33.905  ? 37  VAL   B H    1 c 1 
ATOM   363  H HA   . VAL   A 1 25  ? 19.02  -3.696  6.113   1   35.306  ? 37  VAL   B HA   1 c 1 
ATOM   364  H HB   . VAL   A 1 25  ? 19.645 -3.05   8.797   1   38.294  ? 37  VAL   B HB   1 c 1 
ATOM   365  H HG11 . VAL   A 1 25  ? 20.84  -4.994  7.134   1   38.283  ? 37  VAL   B HG11 1 c 1 
ATOM   366  H HG12 . VAL   A 1 25  ? 20.391 -5.162  8.647   1   39.912  ? 37  VAL   B HG12 1 c 1 
ATOM   367  H HG13 . VAL   A 1 25  ? 21.695 -4.33   8.295   1   39.256  ? 37  VAL   B HG13 1 c 1 
ATOM   368  H HG21 . VAL   A 1 25  ? 21.612 -2.053  7.911   1   37.651  ? 37  VAL   B HG21 1 c 1 
ATOM   369  H HG22 . VAL   A 1 25  ? 20.305 -1.317  7.393   1   35.868  ? 37  VAL   B HG22 1 c 1 
ATOM   370  H HG23 . VAL   A 1 25  ? 21.073 -2.331  6.445   1   36.081  ? 37  VAL   B HG23 1 c 1 
ATOM   371  N N    . LYS   A 1 26  ? 17.827 -5.725  6.598   1   34.754  ? 38  LYS   B N    1 ? 1 
ATOM   372  C CA   . LYS   A 1 26  ? 17.085 -6.955  6.902   1   39.292  ? 38  LYS   B CA   1 ? 1 
ATOM   373  C C    . LYS   A 1 26  ? 17.992 -8.048  7.404   1   42.229  ? 38  LYS   B C    1 ? 1 
ATOM   374  O O    . LYS   A 1 26  ? 17.532 -8.931  8.166   1   42.216  ? 38  LYS   B O    1 ? 1 
ATOM   375  C CB   . LYS   A 1 26  ? 16.333 -7.472  5.669   1   45.313  ? 38  LYS   B CB   1 ? 1 
ATOM   376  C CG   . LYS   A 1 26  ? 15.206 -6.536  5.333   1   45.157  ? 38  LYS   B CG   1 ? 1 
ATOM   377  C CD   . LYS   A 1 26  ? 14.168 -6.219  6.412   1   46.303  ? 38  LYS   B CD   1 ? 1 
ATOM   378  C CE   . LYS   A 1 26  ? 12.886 -6.938  6.244   1   49.065  ? 38  LYS   B CE   1 ? 1 
ATOM   379  N NZ   . LYS   A 1 26  ? 12.003 -6.653  7.371   1   55.092  ? 38  LYS   B NZ   1 ? 1 
ATOM   380  H H    . LYS   A 1 26  ? 18.249 -5.651  5.791   1   35.009  ? 38  LYS   B H    1 c 1 
ATOM   381  H HA   . LYS   A 1 26  ? 16.431 -6.755  7.614   1   40.511  ? 38  LYS   B HA   1 c 1 
ATOM   382  H HB2  . LYS   A 1 26  ? 16.944 -7.534  4.904   1   43.401  ? 38  LYS   B HB2  1 c 1 
ATOM   383  H HB3  . LYS   A 1 26  ? 15.967 -8.363  5.85    1   45.59   ? 38  LYS   B HB3  1 c 1 
ATOM   384  H HG2  . LYS   A 1 26  ? 15.604 -5.688  5.037   1   43.382  ? 38  LYS   B HG2  1 c 1 
ATOM   385  H HG3  . LYS   A 1 26  ? 14.734 -6.908  4.556   1   44.923  ? 38  LYS   B HG3  1 c 1 
ATOM   386  H HD2  . LYS   A 1 26  ? 14.538 -6.439  7.292   1   47.507  ? 38  LYS   B HD2  1 c 1 
ATOM   387  H HD3  . LYS   A 1 26  ? 13.992 -5.253  6.402   1   45.306  ? 38  LYS   B HD3  1 c 1 
ATOM   388  H HE2  . LYS   A 1 26  ? 12.452 -6.654  5.422   1   48.846  ? 38  LYS   B HE2  1 c 1 
ATOM   389  H HE3  . LYS   A 1 26  ? 13.047 -7.898  6.196   1   51.151  ? 38  LYS   B HE3  1 c 1 
ATOM   390  H HZ1  . LYS   A 1 26  ? 11.863 -5.76   7.433   1   52.411  ? 38  LYS   B HZ1  1 c 1 
ATOM   391  H HZ2  . LYS   A 1 26  ? 12.38  -6.95   8.139   1   54.543  ? 38  LYS   B HZ2  1 c 1 
ATOM   392  H HZ3  . LYS   A 1 26  ? 11.208 -7.07   7.249   1   54.593  ? 38  LYS   B HZ3  1 c 1 
ATOM   393  N N    . ARG   A 1 27  ? 19.195 -8.138  6.816   1   38.966  ? 39  ARG   B N    1 ? 1 
ATOM   394  C CA   . ARG   A 1 27  ? 20.164 -9.071  7.387   1   41.157  ? 39  ARG   B CA   1 ? 1 
ATOM   395  C C    . ARG   A 1 27  ? 21.504 -8.347  7.481   1   44.636  ? 39  ARG   B C    1 ? 1 
ATOM   396  O O    . ARG   A 1 27  ? 21.978 -7.809  6.472   1   42.065  ? 39  ARG   B O    1 ? 1 
ATOM   397  C CB   . ARG   A 1 27  ? 20.401 -10.32  6.547   1   41.624  ? 39  ARG   B CB   1 ? 1 
ATOM   398  C CG   . ARG   A 1 27  ? 21.279 -11.376 7.252   1   46.496  ? 39  ARG   B CG   1 ? 1 
ATOM   399  C CD   . ARG   A 1 27  ? 21.583 -12.588 6.344   1   46.464  ? 39  ARG   B CD   1 ? 1 
ATOM   400  N NE   . ARG   A 1 27  ? 22.516 -12.226 5.264   1   49.601  ? 39  ARG   B NE   1 ? 1 
ATOM   401  C CZ   . ARG   A 1 27  ? 22.658 -12.893 4.105   1   51.149  ? 39  ARG   B CZ   1 ? 1 
ATOM   402  N NH1  . ARG   A 1 27  ? 23.393 -12.387 3.093   1   50.323  ? 39  ARG   B NH1  1 ? 1 
ATOM   403  N NH2  . ARG   A 1 27  ? 21.983 -14.027 3.947   1   48.091  ? 39  ARG   B NH2  1 ? 1 
ATOM   404  H H    . ARG   A 1 27  ? 19.409 -7.646  6.075   1   38.241  ? 39  ARG   B H    1 c 1 
ATOM   405  H HA   . ARG   A 1 27  ? 19.87  -9.329  8.297   1   43.058  ? 39  ARG   B HA   1 c 1 
ATOM   406  H HB2  . ARG   A 1 27  ? 19.534 -10.724 6.33    1   42.522  ? 39  ARG   B HB2  1 c 1 
ATOM   407  H HB3  . ARG   A 1 27  ? 20.831 -10.062 5.703   1   41.199  ? 39  ARG   B HB3  1 c 1 
ATOM   408  H HG2  . ARG   A 1 27  ? 22.126 -10.964 7.527   1   45.652  ? 39  ARG   B HG2  1 c 1 
ATOM   409  H HG3  . ARG   A 1 27  ? 20.819 -11.69  8.06    1   46.983  ? 39  ARG   B HG3  1 c 1 
ATOM   410  H HD2  . ARG   A 1 27  ? 21.973 -13.308 6.881   1   49.976  ? 39  ARG   B HD2  1 c 1 
ATOM   411  H HD3  . ARG   A 1 27  ? 20.747 -12.918 5.954   1   47.758  ? 39  ARG   B HD3  1 c 1 
ATOM   412  H HE   . ARG   A 1 27  ? 23.018 -11.524 5.381   1   47.798  ? 39  ARG   B HE   1 c 1 
ATOM   413  H HH11 . ARG   A 1 27  ? 23.395 -11.516 2.945   1   48.425  ? 39  ARG   B HH11 1 c 1 
ATOM   414  H HH12 . ARG   A 1 27  ? 23.87  -12.929 2.583   1   51.307  ? 39  ARG   B HH12 1 c 1 
ATOM   415  H HH21 . ARG   A 1 27  ? 22.139 -14.71  4.486   1   51.491  ? 39  ARG   B HH21 1 c 1 
ATOM   416  H HH22 . ARG   A 1 27  ? 21.382 -14.094 3.302   1   48.914  ? 39  ARG   B HH22 1 c 1 
ATOM   417  N N    . VAL   A 1 28  ? 22.127 -8.351  8.668   1   43.536  ? 40  VAL   B N    1 ? 1 
ATOM   418  C CA   . VAL   A 1 28  ? 23.382 -7.628  8.867   1   47.115  ? 40  VAL   B CA   1 ? 1 
ATOM   419  C C    . VAL   A 1 28  ? 24.511 -8.398  8.169   1   49.461  ? 40  VAL   B C    1 ? 1 
ATOM   420  O O    . VAL   A 1 28  ? 24.59  -9.626  8.365   1   47.458  ? 40  VAL   B O    1 ? 1 
ATOM   421  C CB   . VAL   A 1 28  ? 23.689 -7.395  10.375  1   51.066  ? 40  VAL   B CB   1 ? 1 
ATOM   422  C CG1  . VAL   A 1 28  ? 25.058 -6.783  10.672  1   53.185  ? 40  VAL   B CG1  1 ? 1 
ATOM   423  C CG2  . VAL   A 1 28  ? 22.626 -6.536  11.061  1   48.809  ? 40  VAL   B CG2  1 ? 1 
ATOM   424  H H    . VAL   A 1 28  ? 21.767 -8.815  9.369   1   46.292  ? 40  VAL   B H    1 c 1 
ATOM   425  H HA   . VAL   A 1 28  ? 23.296 -6.754  8.438   1   45.218  ? 40  VAL   B HA   1 c 1 
ATOM   426  H HB   . VAL   A 1 28  ? 23.669 -8.281  10.808  1   52.498  ? 40  VAL   B HB   1 c 1 
ATOM   427  H HG11 . VAL   A 1 28  ? 25.247 -6.081  10.026  1   51.237  ? 40  VAL   B HG11 1 c 1 
ATOM   428  H HG12 . VAL   A 1 28  ? 25.741 -7.471  10.611  1   54.272  ? 40  VAL   B HG12 1 c 1 
ATOM   429  H HG13 . VAL   A 1 28  ? 25.06  -6.406  11.568  1   53.519  ? 40  VAL   B HG13 1 c 1 
ATOM   430  H HG21 . VAL   A 1 28  ? 22.798 -6.506  12.017  1   50.637  ? 40  VAL   B HG21 1 c 1 
ATOM   431  H HG22 . VAL   A 1 28  ? 21.746 -6.919  10.904  1   48.917  ? 40  VAL   B HG22 1 c 1 
ATOM   432  H HG23 . VAL   A 1 28  ? 22.654 -5.634  10.7    1   47.577  ? 40  VAL   B HG23 1 c 1 
ATOM   433  N N    . GLY   A 1 29  ? 25.418 -7.651  7.48    1   49.787  ? 41  GLY   B N    1 ? 1 
ATOM   434  C CA   . GLY   A 1 29  ? 26.687 -8.105  6.901   1   56.392  ? 41  GLY   B CA   1 ? 1 
ATOM   435  C C    . GLY   A 1 29  ? 27.921 -8.085  7.86    1   65.691  ? 41  GLY   B C    1 ? 1 
ATOM   436  O O    . GLY   A 1 29  ? 27.817 -7.699  9.024   1   55.236  ? 41  GLY   B O    1 ? 1 
ATOM   437  H H    . GLY   A 1 29  ? 25.211 -6.768  7.365   1   49.026  ? 41  GLY   B H    1 c 1 
ATOM   438  H HA2  . GLY   A 1 29  ? 26.562 -9.025  6.569   1   57.272  ? 41  GLY   B HA2  1 c 1 
ATOM   439  H HA3  . GLY   A 1 29  ? 26.887 -7.538  6.12    1   55.046  ? 41  GLY   B HA3  1 c 1 
ATOM   440  N N    . ASN   A 1 30  ? 29.127 -8.516  7.394   1   71.362  ? 42  ASN   B N    1 ? 1 
ATOM   441  C CA   . ASN   A 1 30  ? 30.408 -8.422  8.124   1   66.228  ? 42  ASN   B CA   1 ? 1 
ATOM   442  C C    . ASN   A 1 30  ? 31.274 -7.301  7.523   1   73.312  ? 42  ASN   B C    1 ? 1 
ATOM   443  O O    . ASN   A 1 30  ? 31.066 -6.907  6.384   1   62.4    ? 42  ASN   B O    1 ? 1 
ATOM   444  C CB   . ASN   A 1 30  ? 31.218 -9.717  8.076   1   61.646  ? 42  ASN   B CB   1 ? 1 
ATOM   445  H H    . ASN   A 1 30  ? 29.143 -8.89   6.561   1   68.236  ? 42  ASN   B H    1 c 1 
ATOM   446  H HA   . ASN   A 1 30  ? 30.224 -8.215  9.068   1   67.665  ? 42  ASN   B HA   1 c 1 
ATOM   447  H HB2  . ASN   A 1 30  ? 32.102 -9.484  8.089   0   30      ? 42  ASN   B HB2  1 c 1 
ATOM   448  H HB3  . ASN   A 1 30  ? 30.519 -10.437 8.062   0   30      ? 42  ASN   B HB3  1 c 1 
ATOM   449  N N    . GLY   A 1 31  ? 32.238 -6.736  8.262   1   74.302  ? 43  GLY   B N    1 ? 1 
ATOM   450  C CA   . GLY   A 1 31  ? 33.365 -6.083  7.597   1   74.656  ? 43  GLY   B CA   1 ? 1 
ATOM   451  C C    . GLY   A 1 31  ? 33.817 -4.761  8.218   1   84.38   ? 43  GLY   B C    1 ? 1 
ATOM   452  O O    . GLY   A 1 31  ? 34.897 -4.712  8.814   1   110.573 ? 43  GLY   B O    1 ? 1 
ATOM   453  H H    . GLY   A 1 31  ? 32.199 -6.754  9.175   1   75.381  ? 43  GLY   B H    1 c 1 
ATOM   454  H HA2  . GLY   A 1 31  ? 34.128 -6.708  7.599   1   79.106  ? 43  GLY   B HA2  1 c 1 
ATOM   455  H HA3  . GLY   A 1 31  ? 33.125 -5.921  6.655   1   75.111  ? 43  GLY   B HA3  1 c 1 
ATOM   456  N N    . GLU   A 1 32  ? 33.039 -3.689  8.03    1   75.644  ? 44  GLU   B N    1 ? 1 
ATOM   457  C CA   . GLU   A 1 32  ? 33.445 -2.334  8.404   1   86.059  ? 44  GLU   B CA   1 ? 1 
ATOM   458  C C    . GLU   A 1 32  ? 33.811 -1.529  7.147   1   83.433  ? 44  GLU   B C    1 ? 1 
ATOM   459  O O    . GLU   A 1 32  ? 33.851 -0.301  7.227   1   78.483  ? 44  GLU   B O    1 ? 1 
ATOM   460  C CB   . GLU   A 1 32  ? 34.594 -2.138  9.41    1   82.304  ? 44  GLU   B CB   1 ? 1 
ATOM   461  H H    . GLU   A 1 32  ? 32.216 -3.806  7.651   1   77.228  ? 44  GLU   B H    1 c 1 
ATOM   462  H HA   . GLU   A 1 32  ? 32.653 -1.898  8.809   1   80.839  ? 44  GLU   B HA   1 c 1 
ATOM   463  H HB2  . GLU   A 1 32  ? 34.919 -2.137  9.415   0   30      ? 44  GLU   B HB2  1 c 1 
ATOM   464  H HB3  . GLU   A 1 32  ? 33.356 -1.993  10.406  0   30      ? 44  GLU   B HB3  1 c 1 
ATOM   465  N N    . GLU   A 1 33  ? 34.107 -2.186  6.006   1   69.035  ? 45  GLU   B N    1 ? 1 
ATOM   466  C CA   . GLU   A 1 33  ? 34.117 -1.489  4.731   1   61.041  ? 45  GLU   B CA   1 ? 1 
ATOM   467  C C    . GLU   A 1 33  ? 32.713 -1.552  4.117   1   56.622  ? 45  GLU   B C    1 ? 1 
ATOM   468  O O    . GLU   A 1 33  ? 32.103 -2.599  4       1   53.453  ? 45  GLU   B O    1 ? 1 
ATOM   469  C CB   . GLU   A 1 33  ? 35.145 -1.945  3.692   1   59.925  ? 45  GLU   B CB   1 ? 1 
ATOM   470  H H    . GLU   A 1 33  ? 34.315 -3.075  6.028   1   71.409  ? 45  GLU   B H    1 c 1 
ATOM   471  H HA   . GLU   A 1 33  ? 34.322 -0.538  4.914   1   61.765  ? 45  GLU   B HA   1 c 1 
ATOM   472  H HB2  . GLU   A 1 33  ? 36.047 -1.814  4.041   0   30      ? 45  GLU   B HB2  1 c 1 
ATOM   473  H HB3  . GLU   A 1 33  ? 34.625 -2.325  2.961   0   30      ? 45  GLU   B HB3  1 c 1 
ATOM   474  N N    . THR   A 1 34  ? 32.242 -0.395  3.659   1   54.677  ? 46  THR   B N    1 ? 1 
ATOM   475  C CA   . THR   A 1 34  ? 31.237 -0.281  2.616   1   49.755  ? 46  THR   B CA   1 ? 1 
ATOM   476  C C    . THR   A 1 34  ? 31.951 -0.005  1.288   1   58.367  ? 46  THR   B C    1 ? 1 
ATOM   477  O O    . THR   A 1 34  ? 33.057 0.486   1.264   1   66.959  ? 46  THR   B O    1 ? 1 
ATOM   478  C CB   . THR   A 1 34  ? 30.316 0.878   2.977   1   43.804  ? 46  THR   B CB   1 ? 1 
ATOM   479  O OG1  . THR   A 1 34  ? 31.283 1.904   2.944   1   41.779  ? 46  THR   B OG1  1 ? 1 
ATOM   480  C CG2  . THR   A 1 34  ? 29.736 0.856   4.388   1   41.807  ? 46  THR   B CG2  1 ? 1 
ATOM   481  H H    . THR   A 1 34  ? 32.568 0.377   4.025   1   54.733  ? 46  THR   B H    1 c 1 
ATOM   482  H HA   . THR   A 1 34  ? 30.721 -1.113  2.559   1   50.062  ? 46  THR   B HA   1 c 1 
ATOM   483  H HB   . THR   A 1 34  ? 29.626 1.023   2.287   1   41.785  ? 46  THR   B HB   1 c 1 
ATOM   484  H HG1  . THR   A 1 34  ? 31.894 1.769   3.469   0   30      ? 46  THR   B HG1  1 c 1 
ATOM   485  H HG21 . THR   A 1 34  ? 29.059 1.548   4.471   1   41.12   ? 46  THR   B HG21 1 c 1 
ATOM   486  H HG22 . THR   A 1 34  ? 30.444 1.018   5.034   1   44.006  ? 46  THR   B HG22 1 c 1 
ATOM   487  H HG23 . THR   A 1 34  ? 29.334 -0.012  4.56    1   42.09   ? 46  THR   B HG23 1 c 1 
ATOM   488  N N    . PRO   A 1 35  ? 31.339 -0.213  0.107   1   59.629  ? 47  PRO   B N    1 ? 1 
ATOM   489  C CA   . PRO   A 1 35  ? 32.034 0.053   -1.144  1   61.178  ? 47  PRO   B CA   1 ? 1 
ATOM   490  C C    . PRO   A 1 35  ? 32.212 1.546   -1.371  1   68.025  ? 47  PRO   B C    1 ? 1 
ATOM   491  O O    . PRO   A 1 35  ? 31.372 2.358   -0.983  1   74.812  ? 47  PRO   B O    1 ? 1 
ATOM   492  C CB   . PRO   A 1 35  ? 31.114 -0.569  -2.229  1   55.355  ? 47  PRO   B CB   1 ? 1 
ATOM   493  C CG   . PRO   A 1 35  ? 29.952 -1.22   -1.508  1   46.78   ? 47  PRO   B CG   1 ? 1 
ATOM   494  C CD   . PRO   A 1 35  ? 29.978 -0.708  -0.089  1   54.715  ? 47  PRO   B CD   1 ? 1 
ATOM   495  H HA   . PRO   A 1 35  ? 32.913 -0.404  -1.144  1   63.407  ? 47  PRO   B HA   1 c 1 
ATOM   496  H HB2  . PRO   A 1 35  ? 30.79  0.125   -2.848  1   53.667  ? 47  PRO   B HB2  1 c 1 
ATOM   497  H HB3  . PRO   A 1 35  ? 31.609 -1.238  -2.757  1   55.739  ? 47  PRO   B HB3  1 c 1 
ATOM   498  H HG2  . PRO   A 1 35  ? 29.105 -0.984  -1.941  1   48.366  ? 47  PRO   B HG2  1 c 1 
ATOM   499  H HG3  . PRO   A 1 35  ? 30.044 -2.196  -1.52   1   50.627  ? 47  PRO   B HG3  1 c 1 
ATOM   500  H HD2  . PRO   A 1 35  ? 29.321 0.014   0.034   1   51.932  ? 47  PRO   B HD2  1 c 1 
ATOM   501  H HD3  . PRO   A 1 35  ? 29.774 -1.431  0.542   1   53.286  ? 47  PRO   B HD3  1 c 1 
ATOM   502  N N    . MET   A 1 36  ? 33.265 1.932   -2.079  1   68.279  ? 48  MET   B N    1 ? 1 
ATOM   503  C CA   . MET   A 1 36  ? 33.281 3.332   -2.443  1   65.99   ? 48  MET   B CA   1 ? 1 
ATOM   504  C C    . MET   A 1 36  ? 33.228 3.488   -3.936  1   58.992  ? 48  MET   B C    1 ? 1 
ATOM   505  O O    . MET   A 1 36  ? 33.368 2.512   -4.654  1   66.349  ? 48  MET   B O    1 ? 1 
ATOM   506  C CB   . MET   A 1 36  ? 34.491 4.051   -1.887  1   68.188  ? 48  MET   B CB   1 ? 1 
ATOM   507  C CG   . MET   A 1 36  ? 34.214 4.508   -0.505  1   70.283  ? 48  MET   B CG   1 ? 1 
ATOM   508  S SD   . MET   A 1 36  ? 35.859 4.875   0.103   1   63.06   ? 48  MET   B SD   1 ? 1 
ATOM   509  C CE   . MET   A 1 36  ? 36.558 3.218   0.151   1   62.449  ? 48  MET   B CE   1 ? 1 
ATOM   510  H H    . MET   A 1 36  ? 33.944 1.369   -2.317  1   69.53   ? 48  MET   B H    1 c 1 
ATOM   511  H HA   . MET   A 1 36  ? 32.466 3.756   -2.075  1   63.268  ? 48  MET   B HA   1 c 1 
ATOM   512  H HB2  . MET   A 1 36  ? 35.256 3.439   -1.894  1   70.354  ? 48  MET   B HB2  1 c 1 
ATOM   513  H HB3  . MET   A 1 36  ? 34.707 4.823   -2.452  1   69.369  ? 48  MET   B HB3  1 c 1 
ATOM   514  H HG2  . MET   A 1 36  ? 33.653 5.308   -0.499  1   66.229  ? 48  MET   B HG2  1 c 1 
ATOM   515  H HG3  . MET   A 1 36  ? 33.797 3.801   0.027   1   66.299  ? 48  MET   B HG3  1 c 1 
ATOM   516  H HE1  . MET   A 1 36  ? 37.202 3.159   0.881   1   64.849  ? 48  MET   B HE1  1 c 1 
ATOM   517  H HE2  . MET   A 1 36  ? 35.845 2.568   0.291   1   61.136  ? 48  MET   B HE2  1 c 1 
ATOM   518  H HE3  . MET   A 1 36  ? 37.011 3.031   -0.693  1   64.037  ? 48  MET   B HE3  1 c 1 
ATOM   519  N N    . ILE   A 1 37  ? 33.036 4.744   -4.331  1   55.546  ? 49  ILE   B N    1 ? 1 
ATOM   520  C CA   . ILE   A 1 37  ? 32.809 5.1     -5.708  1   55.905  ? 49  ILE   B CA   1 ? 1 
ATOM   521  C C    . ILE   A 1 37  ? 33.928 4.547   -6.58   1   56.127  ? 49  ILE   B C    1 ? 1 
ATOM   522  O O    . ILE   A 1 37  ? 35.092 4.71    -6.239  1   60.314  ? 49  ILE   B O    1 ? 1 
ATOM   523  C CB   . ILE   A 1 37  ? 32.744 6.623   -5.792  1   58.958  ? 49  ILE   B CB   1 ? 1 
ATOM   524  C CG1  . ILE   A 1 37  ? 31.686 7.142   -4.832  1   53.27   ? 49  ILE   B CG1  1 ? 1 
ATOM   525  C CG2  . ILE   A 1 37  ? 32.603 7.07    -7.258  1   56.216  ? 49  ILE   B CG2  1 ? 1 
ATOM   526  C CD1  . ILE   A 1 37  ? 31.206 8.53    -5.194  1   52.242  ? 49  ILE   B CD1  1 ? 1 
ATOM   527  H H    . ILE   A 1 37  ? 33.053 5.408   -3.704  1   56.766  ? 49  ILE   B H    1 c 1 
ATOM   528  H HA   . ILE   A 1 37  ? 31.955 4.726   -5.998  1   53.873  ? 49  ILE   B HA   1 c 1 
ATOM   529  H HB   . ILE   A 1 37  ? 33.604 6.961   -5.472  1   59.194  ? 49  ILE   B HB   1 c 1 
ATOM   530  H HG12 . ILE   A 1 37  ? 30.922 6.529   -4.833  1   51.946  ? 49  ILE   B HG12 1 c 1 
ATOM   531  H HG13 . ILE   A 1 37  ? 32.057 7.165   -3.926  1   54.386  ? 49  ILE   B HG13 1 c 1 
ATOM   532  H HG21 . ILE   A 1 37  ? 32.666 8.039   -7.312  1   57.868  ? 49  ILE   B HG21 1 c 1 
ATOM   533  H HG22 . ILE   A 1 37  ? 31.741 6.785   -7.604  1   55.314  ? 49  ILE   B HG22 1 c 1 
ATOM   534  H HG23 . ILE   A 1 37  ? 33.311 6.675   -7.792  1   58.767  ? 49  ILE   B HG23 1 c 1 
ATOM   535  H HD11 . ILE   A 1 37  ? 31.968 9.124   -5.317  1   54.612  ? 49  ILE   B HD11 1 c 1 
ATOM   536  H HD12 . ILE   A 1 37  ? 30.646 8.868   -4.47   1   51.478  ? 49  ILE   B HD12 1 c 1 
ATOM   537  H HD13 . ILE   A 1 37  ? 30.683 8.497   -6.017  1   51.745  ? 49  ILE   B HD13 1 c 1 
ATOM   538  N N    . GLY   A 1 38  ? 33.576 3.922   -7.706  1   48.549  ? 50  GLY   B N    1 ? 1 
ATOM   539  C CA   . GLY   A 1 38  ? 34.535 3.267   -8.589  1   55.619  ? 50  GLY   B CA   1 ? 1 
ATOM   540  C C    . GLY   A 1 38  ? 34.592 1.743   -8.428  1   54.906  ? 50  GLY   B C    1 ? 1 
ATOM   541  O O    . GLY   A 1 38  ? 35.091 1.056   -9.327  1   60.935  ? 50  GLY   B O    1 ? 1 
ATOM   542  H H    . GLY   A 1 38  ? 32.692 3.904   -7.939  1   49.371  ? 50  GLY   B H    1 c 1 
ATOM   543  H HA2  . GLY   A 1 38  ? 34.297 3.481   -9.522  1   54.439  ? 50  GLY   B HA2  1 c 1 
ATOM   544  H HA3  . GLY   A 1 38  ? 35.431 3.641   -8.42   1   56.532  ? 50  GLY   B HA3  1 c 1 
ATOM   545  N N    . ASP   A 1 39  ? 34.174 1.216   -7.272  1   49.003  ? 51  ASP   B N    1 ? 1 
ATOM   546  C CA   . ASP   A 1 39  ? 34.301 -0.207  -7.003  1   49.026  ? 51  ASP   B CA   1 ? 1 
ATOM   547  C C    . ASP   A 1 39  ? 33.398 -1.027  -7.926  1   52.952  ? 51  ASP   B C    1 ? 1 
ATOM   548  O O    . ASP   A 1 39  ? 32.309 -0.598  -8.365  1   50.199  ? 51  ASP   B O    1 ? 1 
ATOM   549  C CB   . ASP   A 1 39  ? 33.95  -0.567  -5.564  1   52.247  ? 51  ASP   B CB   1 ? 1 
ATOM   550  C CG   . ASP   A 1 39  ? 34.905 -0.088  -4.464  1   54.148  ? 51  ASP   B CG   1 ? 1 
ATOM   551  O OD1  . ASP   A 1 39  ? 35.879 0.606   -4.771  1   57.618  ? 51  ASP   B OD1  1 ? 1 
ATOM   552  O OD2  . ASP   A 1 39  ? 34.703 -0.428  -3.306  1   54.913  ? 51  ASP   B OD2  1 ? 1 
ATOM   553  H H    . ASP   A 1 39  ? 33.801 1.753   -6.635  1   48.758  ? 51  ASP   B H    1 c 1 
ATOM   554  H HA   . ASP   A 1 39  ? 35.236 -0.468  -7.162  1   53.189  ? 51  ASP   B HA   1 c 1 
ATOM   555  H HB2  . ASP   A 1 39  ? 33.062 -0.201  -5.367  1   49.076  ? 51  ASP   B HB2  1 c 1 
ATOM   556  H HB3  . ASP   A 1 39  ? 33.888 -1.543  -5.496  1   51.441  ? 51  ASP   B HB3  1 c 1 
ATOM   557  N N    . LYS   A 1 40  ? 33.867 -2.241  -8.213  1   50.463  ? 52  LYS   B N    1 ? 1 
ATOM   558  C CA   . LYS   A 1 40  ? 33.047 -3.192  -8.934  1   51.016  ? 52  LYS   B CA   1 ? 1 
ATOM   559  C C    . LYS   A 1 40  ? 32.212 -3.935  -7.91   1   49.466  ? 52  LYS   B C    1 ? 1 
ATOM   560  O O    . LYS   A 1 40  ? 32.786 -4.493  -6.988  1   49.029  ? 52  LYS   B O    1 ? 1 
ATOM   561  C CB   . LYS   A 1 40  ? 33.956 -4.132  -9.744  1   57.71   ? 52  LYS   B CB   1 ? 1 
ATOM   562  C CG   . LYS   A 1 40  ? 33.233 -5.07   -10.669 1   60.906  ? 52  LYS   B CG   1 ? 1 
ATOM   563  C CD   . LYS   A 1 40  ? 34.158 -6.128  -11.256 1   74.066  ? 52  LYS   B CD   1 ? 1 
ATOM   564  C CE   . LYS   A 1 40  ? 33.375 -7.155  -12.036 1   79.335  ? 52  LYS   B CE   1 ? 1 
ATOM   565  N NZ   . LYS   A 1 40  ? 34.163 -8.271  -12.592 1   89.515  ? 52  LYS   B NZ   1 ? 1 
ATOM   566  H H    . LYS   A 1 40  ? 34.711 -2.483  -7.956  1   53.612  ? 52  LYS   B H    1 c 1 
ATOM   567  H HA   . LYS   A 1 40  ? 32.45  -2.699  -9.552  1   50.257  ? 52  LYS   B HA   1 c 1 
ATOM   568  H HB2  . LYS   A 1 40  ? 34.574 -3.588  -10.276 1   58.978  ? 52  LYS   B HB2  1 c 1 
ATOM   569  H HB3  . LYS   A 1 40  ? 34.492 -4.665  -9.118  1   58.837  ? 52  LYS   B HB3  1 c 1 
ATOM   570  H HG2  . LYS   A 1 40  ? 32.51  -5.513  -10.173 1   60.635  ? 52  LYS   B HG2  1 c 1 
ATOM   571  H HG3  . LYS   A 1 40  ? 32.831 -4.55   -11.398 1   61.386  ? 52  LYS   B HG3  1 c 1 
ATOM   572  H HD2  . LYS   A 1 40  ? 34.808 -5.697  -11.852 1   74.246  ? 52  LYS   B HD2  1 c 1 
ATOM   573  H HD3  . LYS   A 1 40  ? 34.648 -6.572  -10.532 1   73.558  ? 52  LYS   B HD3  1 c 1 
ATOM   574  H HE2  . LYS   A 1 40  ? 32.677 -7.521  -11.465 1   77.65   ? 52  LYS   B HE2  1 c 1 
ATOM   575  H HE3  . LYS   A 1 40  ? 32.931 -6.702  -12.774 1   78.77   ? 52  LYS   B HE3  1 c 1 
ATOM   576  H HZ1  . LYS   A 1 40  ? 34.569 -8.724  -11.92  1   88.201  ? 52  LYS   B HZ1  1 c 1 
ATOM   577  H HZ2  . LYS   A 1 40  ? 34.794 -7.948  -13.156 1   88.939  ? 52  LYS   B HZ2  1 c 1 
ATOM   578  H HZ3  . LYS   A 1 40  ? 33.619 -8.835  -13.045 1   87.385  ? 52  LYS   B HZ3  1 c 1 
ATOM   579  N N    . VAL   A 1 41  ? 30.886 -3.949  -8.085  1   45.427  ? 53  VAL   B N    1 ? 1 
ATOM   580  C CA   . VAL   A 1 41  ? 29.991 -4.48   -7.064  1   46.563  ? 53  VAL   B CA   1 ? 1 
ATOM   581  C C    . VAL   A 1 41  ? 29.138 -5.637  -7.626  1   50.062  ? 53  VAL   B C    1 ? 1 
ATOM   582  O O    . VAL   A 1 41  ? 28.661 -5.657  -8.792  1   45.394  ? 53  VAL   B O    1 ? 1 
ATOM   583  C CB   . VAL   A 1 41  ? 29.098 -3.383  -6.449  1   46.367  ? 53  VAL   B CB   1 ? 1 
ATOM   584  C CG1  . VAL   A 1 41  ? 28.104 -4.005  -5.491  1   45.19   ? 53  VAL   B CG1  1 ? 1 
ATOM   585  C CG2  . VAL   A 1 41  ? 29.892 -2.32   -5.717  1   47.299  ? 53  VAL   B CG2  1 ? 1 
ATOM   586  H H    . VAL   A 1 41  ? 30.528 -3.622  -8.86   1   45.965  ? 53  VAL   B H    1 c 1 
ATOM   587  H HA   . VAL   A 1 41  ? 30.544 -4.842  -6.346  1   47.969  ? 53  VAL   B HA   1 c 1 
ATOM   588  H HB   . VAL   A 1 41  ? 28.601 -2.955  -7.185  1   45.248  ? 53  VAL   B HB   1 c 1 
ATOM   589  H HG11 . VAL   A 1 41  ? 28.542 -4.702  -4.975  1   46.142  ? 53  VAL   B HG11 1 c 1 
ATOM   590  H HG12 . VAL   A 1 41  ? 27.365 -4.388  -5.991  1   44.529  ? 53  VAL   B HG12 1 c 1 
ATOM   591  H HG13 . VAL   A 1 41  ? 27.764 -3.323  -4.887  1   43.9    ? 53  VAL   B HG13 1 c 1 
ATOM   592  H HG21 . VAL   A 1 41  ? 29.293 -1.613  -5.421  1   45.618  ? 53  VAL   B HG21 1 c 1 
ATOM   593  H HG22 . VAL   A 1 41  ? 30.562 -1.945  -6.313  1   48.234  ? 53  VAL   B HG22 1 c 1 
ATOM   594  H HG23 . VAL   A 1 41  ? 30.331 -2.715  -4.946  1   47.938  ? 53  VAL   B HG23 1 c 1 
ATOM   595  N N    . TYR   A 1 42  ? 29.001 -6.668  -6.781  1   44.96   ? 54  TYR   B N    1 ? 1 
ATOM   596  C CA   . TYR   A 1 42  ? 28.269 -7.876  -7.136  1   46.355  ? 54  TYR   B CA   1 ? 1 
ATOM   597  C C    . TYR   A 1 42  ? 27.056 -7.977  -6.218  1   44.466  ? 54  TYR   B C    1 ? 1 
ATOM   598  O O    . TYR   A 1 42  ? 27.266 -8.076  -4.994  1   42.492  ? 54  TYR   B O    1 ? 1 
ATOM   599  C CB   . TYR   A 1 42  ? 29.156 -9.127  -6.939  1   52.653  ? 54  TYR   B CB   1 ? 1 
ATOM   600  C CG   . TYR   A 1 42  ? 30.481 -9.095  -7.693  1   56.886  ? 54  TYR   B CG   1 ? 1 
ATOM   601  C CD1  . TYR   A 1 42  ? 31.54  -8.3    -7.27   1   55.935  ? 54  TYR   B CD1  1 ? 1 
ATOM   602  C CD2  . TYR   A 1 42  ? 30.635 -9.809  -8.882  1   64.812  ? 54  TYR   B CD2  1 ? 1 
ATOM   603  C CE1  . TYR   A 1 42  ? 32.72  -8.221  -7.995  1   61.358  ? 54  TYR   B CE1  1 ? 1 
ATOM   604  C CE2  . TYR   A 1 42  ? 31.824 -9.765  -9.596  1   68.09   ? 54  TYR   B CE2  1 ? 1 
ATOM   605  C CZ   . TYR   A 1 42  ? 32.858 -8.963  -9.144  1   63.65   ? 54  TYR   B CZ   1 ? 1 
ATOM   606  O OH   . TYR   A 1 42  ? 33.998 -8.877  -9.857  1   74.727  ? 54  TYR   B OH   1 ? 1 
ATOM   607  H H    . TYR   A 1 42  ? 29.38  -6.618  -5.951  1   46.679  ? 54  TYR   B H    1 c 1 
ATOM   608  H HA   . TYR   A 1 42  ? 27.971 -7.825  -8.082  1   46.701  ? 54  TYR   B HA   1 c 1 
ATOM   609  H HB2  . TYR   A 1 42  ? 29.344 -9.228  -5.979  1   52.322  ? 54  TYR   B HB2  1 c 1 
ATOM   610  H HB3  . TYR   A 1 42  ? 28.647 -9.917  -7.227  1   52.879  ? 54  TYR   B HB3  1 c 1 
ATOM   611  H HD1  . TYR   A 1 42  ? 31.447 -7.784  -6.485  1   55.82   ? 54  TYR   B HD1  1 c 1 
ATOM   612  H HD2  . TYR   A 1 42  ? 29.93  -10.354 -9.191  1   63.217  ? 54  TYR   B HD2  1 c 1 
ATOM   613  H HE1  . TYR   A 1 42  ? 33.431 -7.684  -7.69   1   61.445  ? 54  TYR   B HE1  1 c 1 
ATOM   614  H HE2  . TYR   A 1 42  ? 31.918 -10.253 -10.396 1   68.069  ? 54  TYR   B HE2  1 c 1 
ATOM   615  H HH   . TYR   A 1 42  ? 34.517 -9.533  -9.597  0   30      ? 54  TYR   B HH   1 c 1 
ATOM   616  N N    . VAL   A 1 43  ? 25.836 -8.079  -6.796  1   39.953  ? 55  VAL   B N    1 ? 1 
ATOM   617  C CA   . VAL   A 1 43  ? 24.665 -8.278  -5.936  1   39.932  ? 55  VAL   B CA   1 ? 1 
ATOM   618  C C    . VAL   A 1 43  ? 23.75  -9.367  -6.468  1   40.35   ? 55  VAL   B C    1 ? 1 
ATOM   619  O O    . VAL   A 1 43  ? 23.927 -9.767  -7.639  1   40.478  ? 55  VAL   B O    1 ? 1 
ATOM   620  C CB   . VAL   A 1 43  ? 23.893 -6.95   -5.824  1   38.877  ? 55  VAL   B CB   1 ? 1 
ATOM   621  C CG1  . VAL   A 1 43  ? 24.793 -5.843  -5.353  1   38.322  ? 55  VAL   B CG1  1 ? 1 
ATOM   622  C CG2  . VAL   A 1 43  ? 23.2   -6.614  -7.138  1   36.484  ? 55  VAL   B CG2  1 ? 1 
ATOM   623  H H    . VAL   A 1 43  ? 25.736 -8.031  -7.703  1   41.222  ? 55  VAL   B H    1 c 1 
ATOM   624  H HA   . VAL   A 1 43  ? 24.97  -8.537  -5.047  1   40.287  ? 55  VAL   B HA   1 c 1 
ATOM   625  H HB   . VAL   A 1 43  ? 23.193 -7.078  -5.142  1   37.661  ? 55  VAL   B HB   1 c 1 
ATOM   626  H HG11 . VAL   A 1 43  ? 25.336 -5.528  -6.096  1   38.74   ? 55  VAL   B HG11 1 c 1 
ATOM   627  H HG12 . VAL   A 1 43  ? 25.373 -6.173  -4.646  1   39.137  ? 55  VAL   B HG12 1 c 1 
ATOM   628  H HG13 . VAL   A 1 43  ? 24.255 -5.109  -5.013  1   36.914  ? 55  VAL   B HG13 1 c 1 
ATOM   629  H HG21 . VAL   A 1 43  ? 22.976 -5.67   -7.153  1   35.709  ? 55  VAL   B HG21 1 c 1 
ATOM   630  H HG22 . VAL   A 1 43  ? 22.387 -7.139  -7.222  1   37.092  ? 55  VAL   B HG22 1 c 1 
ATOM   631  H HG23 . VAL   A 1 43  ? 23.793 -6.815  -7.881  1   38.044  ? 55  VAL   B HG23 1 c 1 
ATOM   632  N N    . HIS   A 1 44  ? 22.793 -9.813  -5.618  1   36.077  ? 56  HIS   B N    1 ? 1 
ATOM   633  C CA   . HIS   A 1 44  ? 21.549 -10.422 -6.098  1   40.807  ? 56  HIS   B CA   1 ? 1 
ATOM   634  C C    . HIS   A 1 44  ? 20.475 -9.434  -5.696  1   37.347  ? 56  HIS   B C    1 ? 1 
ATOM   635  O O    . HIS   A 1 44  ? 20.614 -8.785  -4.685  1   35.23   ? 56  HIS   B O    1 ? 1 
ATOM   636  C CB   . HIS   A 1 44  ? 21.277 -11.864 -5.601  1   43.226  ? 56  HIS   B CB   1 ? 1 
ATOM   637  C CG   . HIS   A 1 44  ? 21.879 -12.935 -6.436  1   43.764  ? 56  HIS   B CG   1 ? 1 
ATOM   638  N ND1  . HIS   A 1 44  ? 21.523 -13.057 -7.78   1   45.581  ? 56  HIS   B ND1  1 ? 1 
ATOM   639  C CD2  . HIS   A 1 44  ? 22.827 -13.879 -6.194  1   48.763  ? 56  HIS   B CD2  1 ? 1 
ATOM   640  C CE1  . HIS   A 1 44  ? 22.195 -14.078 -8.326  1   52.808  ? 56  HIS   B CE1  1 ? 1 
ATOM   641  N NE2  . HIS   A 1 44  ? 22.975 -14.646 -7.377  1   47.279  ? 56  HIS   B NE2  1 ? 1 
ATOM   642  H H    . HIS   A 1 44  ? 22.925 -9.735  -4.717  1   37.733  ? 56  HIS   B H    1 c 1 
ATOM   643  H HA   . HIS   A 1 44  ? 21.59  -10.441 -7.084  1   40.038  ? 56  HIS   B HA   1 c 1 
ATOM   644  H HB2  . HIS   A 1 44  ? 21.619 -11.948 -4.685  1   42.87   ? 56  HIS   B HB2  1 c 1 
ATOM   645  H HB3  . HIS   A 1 44  ? 20.305 -12.003 -5.563  1   42.56   ? 56  HIS   B HB3  1 c 1 
ATOM   646  H HD1  . HIS   A 1 44  ? 21.006 -12.491 -8.233  0   30      ? 56  HIS   B HD1  1 c 1 
ATOM   647  H HD2  . HIS   A 1 44  ? 23.24  -14.059 -5.372  1   47.802  ? 56  HIS   B HD2  1 c 1 
ATOM   648  H HE1  . HIS   A 1 44  ? 22.109 -14.371 -9.217  1   51.104  ? 56  HIS   B HE1  1 c 1 
ATOM   649  H HE2  . HIS   A 1 44  ? 23.453 -15.359 -7.474  0   30      ? 56  HIS   B HE2  1 c 1 
ATOM   650  N N    . TYR   A 1 45  ? 19.424 -9.306  -6.529  1   35.819  ? 57  TYR   B N    1 ? 1 
ATOM   651  C CA   . TYR   A 1 45  ? 18.361 -8.393  -6.164  1   34.821  ? 57  TYR   B CA   1 ? 1 
ATOM   652  C C    . TYR   A 1 45  ? 17.039 -8.98   -6.632  1   35.182  ? 57  TYR   B C    1 ? 1 
ATOM   653  O O    . TYR   A 1 45  ? 16.977 -9.664  -7.669  1   38.501  ? 57  TYR   B O    1 ? 1 
ATOM   654  C CB   . TYR   A 1 45  ? 18.655 -6.944  -6.644  1   28.007  ? 57  TYR   B CB   1 ? 1 
ATOM   655  C CG   . TYR   A 1 45  ? 18.518 -6.811  -8.178  1   30.732  ? 57  TYR   B CG   1 ? 1 
ATOM   656  C CD1  . TYR   A 1 45  ? 17.285 -6.56   -8.754  1   31.357  ? 57  TYR   B CD1  1 ? 1 
ATOM   657  C CD2  . TYR   A 1 45  ? 19.538 -7.192  -9.046  1   32.303  ? 57  TYR   B CD2  1 ? 1 
ATOM   658  C CE1  . TYR   A 1 45  ? 17.141 -6.475  -10.126 1   35.994  ? 57  TYR   B CE1  1 ? 1 
ATOM   659  C CE2  . TYR   A 1 45  ? 19.381 -7.115  -10.431 1   35.779  ? 57  TYR   B CE2  1 ? 1 
ATOM   660  C CZ   . TYR   A 1 45  ? 18.189 -6.726  -10.973 1   33.59   ? 57  TYR   B CZ   1 ? 1 
ATOM   661  O OH   . TYR   A 1 45  ? 17.947 -6.689  -12.361 1   37.887  ? 57  TYR   B OH   1 ? 1 
ATOM   662  H H    . TYR   A 1 45  ? 19.375 -9.78   -7.309  1   37.328  ? 57  TYR   B H    1 c 1 
ATOM   663  H HA   . TYR   A 1 45  ? 18.33  -8.368  -5.173  1   33.355  ? 57  TYR   B HA   1 c 1 
ATOM   664  H HB2  . TYR   A 1 45  ? 18.024 -6.33   -6.207  1   28.465  ? 57  TYR   B HB2  1 c 1 
ATOM   665  H HB3  . TYR   A 1 45  ? 19.569 -6.7    -6.377  1   29.378  ? 57  TYR   B HB3  1 c 1 
ATOM   666  H HD1  . TYR   A 1 45  ? 16.558 -6.322  -8.201  1   31.39   ? 57  TYR   B HD1  1 c 1 
ATOM   667  H HD2  . TYR   A 1 45  ? 20.386 -7.406  -8.692  1   33.277  ? 57  TYR   B HD2  1 c 1 
ATOM   668  H HE1  . TYR   A 1 45  ? 16.307 -6.23   -10.486 1   34.064  ? 57  TYR   B HE1  1 c 1 
ATOM   669  H HE2  . TYR   A 1 45  ? 20.108 -7.306  -10.996 1   35.656  ? 57  TYR   B HE2  1 c 1 
ATOM   670  H HH   . TYR   A 1 45  ? 18.056 -5.906  -12.666 0   30      ? 57  TYR   B HH   1 c 1 
ATOM   671  N N    . LYS   A 1 46  ? 15.996 -8.407  -6.025  1   34.861  ? 58  LYS   B N    1 ? 1 
ATOM   672  C CA   . LYS   A 1 46  ? 14.602 -8.554  -6.388  1   40.512  ? 58  LYS   B CA   1 ? 1 
ATOM   673  C C    . LYS   A 1 46  ? 14.069 -7.131  -6.436  1   36.886  ? 58  LYS   B C    1 ? 1 
ATOM   674  O O    . LYS   A 1 46  ? 14.252 -6.412  -5.476  1   34.387  ? 58  LYS   B O    1 ? 1 
ATOM   675  C CB   . LYS   A 1 46  ? 13.826 -9.38   -5.318  1   35.821  ? 58  LYS   B CB   1 ? 1 
ATOM   676  H H    . LYS   A 1 46  ? 16.181 -7.871  -5.307  1   34.729  ? 58  LYS   B H    1 c 1 
ATOM   677  H HA   . LYS   A 1 46  ? 14.535 -8.972  -7.284  1   38.99   ? 58  LYS   B HA   1 c 1 
ATOM   678  H HB2  . LYS   A 1 46  ? 14.444 -9.808  -4.746  0   30      ? 58  LYS   B HB2  1 c 1 
ATOM   679  H HB3  . LYS   A 1 46  ? 12.845 -9.237  -5.503  0   30      ? 58  LYS   B HB3  1 c 1 
ATOM   680  N N    . GLY   A 1 47  ? 13.508 -6.674  -7.578  1   35.684  ? 59  GLY   B N    1 ? 1 
ATOM   681  C CA   . GLY   A 1 47  ? 13.006 -5.314  -7.617  1   37.308  ? 59  GLY   B CA   1 ? 1 
ATOM   682  C C    . GLY   A 1 47  ? 11.621 -5.289  -8.24   1   39.66   ? 59  GLY   B C    1 ? 1 
ATOM   683  O O    . GLY   A 1 47  ? 11.269 -6.224  -8.958  1   49.919  ? 59  GLY   B O    1 ? 1 
ATOM   684  H H    . GLY   A 1 47  ? 13.443 -7.206  -8.318  1   37.766  ? 59  GLY   B H    1 c 1 
ATOM   685  H HA2  . GLY   A 1 47  ? 12.966 -4.949  -6.704  1   35.984  ? 59  GLY   B HA2  1 c 1 
ATOM   686  H HA3  . GLY   A 1 47  ? 13.62  -4.754  -8.146  1   36.1    ? 59  GLY   B HA3  1 c 1 
ATOM   687  N N    . LYS   A 1 48  ? 10.816 -4.268  -7.913  1   33.472  ? 60  LYS   B N    1 ? 1 
ATOM   688  C CA   . LYS   A 1 48  ? 9.441  -4.246  -8.42   1   36.44   ? 60  LYS   B CA   1 ? 1 
ATOM   689  C C    . LYS   A 1 48  ? 8.916  -2.837  -8.307  1   37.373  ? 60  LYS   B C    1 ? 1 
ATOM   690  O O    . LYS   A 1 48  ? 9.507  -2.071  -7.522  1   33.788  ? 60  LYS   B O    1 ? 1 
ATOM   691  C CB   . LYS   A 1 48  ? 8.555  -5.218  -7.629  1   40.199  ? 60  LYS   B CB   1 ? 1 
ATOM   692  C CG   . LYS   A 1 48  ? 8.353  -4.929  -6.213  1   42.147  ? 60  LYS   B CG   1 ? 1 
ATOM   693  C CD   . LYS   A 1 48  ? 7.28   -5.73   -5.53   1   44.296  ? 60  LYS   B CD   1 ? 1 
ATOM   694  C CE   . LYS   A 1 48  ? 6.897  -5.254  -4.176  1   53.468  ? 60  LYS   B CE   1 ? 1 
ATOM   695  N NZ   . LYS   A 1 48  ? 5.675  -5.969  -3.754  1   60.015  ? 60  LYS   B NZ   1 ? 1 
ATOM   696  H H    . LYS   A 1 48  ? 11.116 -3.59   -7.379  1   33.907  ? 60  LYS   B H    1 c 1 
ATOM   697  H HA   . LYS   A 1 48  ? 9.45   -4.509  -9.376  1   37.696  ? 60  LYS   B HA   1 c 1 
ATOM   698  H HB2  . LYS   A 1 48  ? 7.675  -5.245  -8.061  1   41.481  ? 60  LYS   B HB2  1 c 1 
ATOM   699  H HB3  . LYS   A 1 48  ? 8.943  -6.116  -7.702  1   41.212  ? 60  LYS   B HB3  1 c 1 
ATOM   700  H HG2  . LYS   A 1 48  ? 9.203  -5.082  -5.746  1   40.778  ? 60  LYS   B HG2  1 c 1 
ATOM   701  H HG3  . LYS   A 1 48  ? 8.137  -3.977  -6.12   1   40.559  ? 60  LYS   B HG3  1 c 1 
ATOM   702  H HD2  . LYS   A 1 48  ? 6.481  -5.729  -6.101  1   47.46   ? 60  LYS   B HD2  1 c 1 
ATOM   703  H HD3  . LYS   A 1 48  ? 7.585  -6.661  -5.46   1   47.281  ? 60  LYS   B HD3  1 c 1 
ATOM   704  H HE2  . LYS   A 1 48  ? 7.613  -5.432  -3.541  1   51.242  ? 60  LYS   B HE2  1 c 1 
ATOM   705  H HE3  . LYS   A 1 48  ? 6.723  -4.296  -4.193  1   50.845  ? 60  LYS   B HE3  1 c 1 
ATOM   706  H HZ1  . LYS   A 1 48  ? 5.806  -6.864  -3.81   1   59.806  ? 60  LYS   B HZ1  1 c 1 
ATOM   707  H HZ2  . LYS   A 1 48  ? 4.981  -5.735  -4.288  1   59.321  ? 60  LYS   B HZ2  1 c 1 
ATOM   708  H HZ3  . LYS   A 1 48  ? 5.475  -5.752  -2.897  1   58.726  ? 60  LYS   B HZ3  1 c 1 
ATOM   709  N N    . LEU   A 1 49  ? 7.959  -2.465  -9.169  1   33.328  ? 61  LEU   B N    1 ? 1 
ATOM   710  C CA   . LEU   A 1 49  ? 7.159  -1.265  -8.924  1   39.78   ? 61  LEU   B CA   1 ? 1 
ATOM   711  C C    . LEU   A 1 49  ? 6.534  -1.395  -7.536  1   34.74   ? 61  LEU   B C    1 ? 1 
ATOM   712  O O    . LEU   A 1 49  ? 6.128  -2.478  -7.147  1   41.474  ? 61  LEU   B O    1 ? 1 
ATOM   713  C CB   . LEU   A 1 49  ? 6.08   -1.067  -9.991  1   40.914  ? 61  LEU   B CB   1 ? 1 
ATOM   714  C CG   . LEU   A 1 49  ? 6.575  -1.034  -11.441 1   41.292  ? 61  LEU   B CG   1 ? 1 
ATOM   715  C CD1  . LEU   A 1 49  ? 5.481  -0.745  -12.46  1   43.102  ? 61  LEU   B CD1  1 ? 1 
ATOM   716  C CD2  . LEU   A 1 49  ? 7.683  -0.03   -11.635 1   42.914  ? 61  LEU   B CD2  1 ? 1 
ATOM   717  H H    . LEU   A 1 49  ? 7.795  -2.969  -9.913  1   37.068  ? 61  LEU   B H    1 c 1 
ATOM   718  H HA   . LEU   A 1 49  ? 7.766  -0.482  -8.924  1   36.009  ? 61  LEU   B HA   1 c 1 
ATOM   719  H HB2  . LEU   A 1 49  ? 5.424  -1.796  -9.904  1   42.447  ? 61  LEU   B HB2  1 c 1 
ATOM   720  H HB3  . LEU   A 1 49  ? 5.614  -0.221  -9.802  1   40.848  ? 61  LEU   B HB3  1 c 1 
ATOM   721  H HG   . LEU   A 1 49  ? 6.946  -1.928  -11.654 1   42.326  ? 61  LEU   B HG   1 c 1 
ATOM   722  H HD11 . LEU   A 1 49  ? 4.756  -1.382  -12.347 1   44.563  ? 61  LEU   B HD11 1 c 1 
ATOM   723  H HD12 . LEU   A 1 49  ? 5.844  -0.825  -13.358 1   43.581  ? 61  LEU   B HD12 1 c 1 
ATOM   724  H HD13 . LEU   A 1 49  ? 5.143  0.157   -12.327 1   42.809  ? 61  LEU   B HD13 1 c 1 
ATOM   725  H HD21 . LEU   A 1 49  ? 8.493  -0.35   -11.203 1   40.906  ? 61  LEU   B HD21 1 c 1 
ATOM   726  H HD22 . LEU   A 1 49  ? 7.423  0.821   -11.243 1   41.262  ? 61  LEU   B HD22 1 c 1 
ATOM   727  H HD23 . LEU   A 1 49  ? 7.851  0.091   -12.585 1   42.362  ? 61  LEU   B HD23 1 c 1 
ATOM   728  N N    . SER   A 1 50  ? 6.499  -0.311  -6.752  1   38.842  ? 62  SER   B N    1 ? 1 
ATOM   729  C CA   . SER   A 1 50  ? 6.066  -0.532  -5.376  1   44.694  ? 62  SER   B CA   1 ? 1 
ATOM   730  C C    . SER   A 1 50  ? 4.606  -0.996  -5.356  1   46.899  ? 62  SER   B C    1 ? 1 
ATOM   731  O O    . SER   A 1 50  ? 4.235  -1.764  -4.499  1   57.405  ? 62  SER   B O    1 ? 1 
ATOM   732  C CB   . SER   A 1 50  ? 6.229  0.687   -4.507  1   48.095  ? 62  SER   B CB   1 ? 1 
ATOM   733  O OG   . SER   A 1 50  ? 5.391  1.709   -5      1   51.271  ? 62  SER   B OG   1 ? 1 
ATOM   734  H H    . SER   A 1 50  ? 6.73   0.523   -7.047  1   37.86   ? 62  SER   B H    1 c 1 
ATOM   735  H HA   . SER   A 1 50  ? 6.623  -1.257  -4.993  1   44.064  ? 62  SER   B HA   1 c 1 
ATOM   736  H HB2  . SER   A 1 50  ? 5.982  0.471   -3.587  1   47.983  ? 62  SER   B HB2  1 c 1 
ATOM   737  H HB3  . SER   A 1 50  ? 7.158  0.982   -4.524  1   46.22   ? 62  SER   B HB3  1 c 1 
ATOM   738  H HG   . SER   A 1 50  ? 5.431  2.478   -4.68   0   30      ? 62  SER   B HG   1 c 1 
ATOM   739  N N    . ASN   A 1 51  ? 3.773  -0.445  -6.232  1   47.939  ? 63  ASN   B N    1 ? 1 
ATOM   740  C CA   . ASN   A 1 51  ? 2.376  -0.843  -6.391  1   55.698  ? 63  ASN   B CA   1 ? 1 
ATOM   741  C C    . ASN   A 1 51  ? 2.184  -2.029  -7.326  1   61.779  ? 63  ASN   B C    1 ? 1 
ATOM   742  O O    . ASN   A 1 51  ? 1.1    -2.19   -7.847  1   71.122  ? 63  ASN   B O    1 ? 1 
ATOM   743  C CB   . ASN   A 1 51  ? 1.557  0.181   -7.177  1   53.624  ? 63  ASN   B CB   1 ? 1 
ATOM   744  H H    . ASN   A 1 51  ? 4.09   0.228   -6.763  1   48.121  ? 63  ASN   B H    1 c 1 
ATOM   745  H HA   . ASN   A 1 51  ? 1.954  -1.001  -5.516  1   55.561  ? 63  ASN   B HA   1 c 1 
ATOM   746  H HB2  . ASN   A 1 51  ? 2.011  1.01    -7.131  0   30      ? 63  ASN   B HB2  1 c 1 
ATOM   747  H HB3  . ASN   A 1 51  ? 0.542  -0.029  -6.715  0   30      ? 63  ASN   B HB3  1 c 1 
ATOM   748  N N    . GLY   A 1 52  ? 3.217  -2.807  -7.606  1   61.659  ? 64  GLY   B N    1 ? 1 
ATOM   749  C CA   . GLY   A 1 52  ? 3.168  -3.854  -8.614  1   60.946  ? 64  GLY   B CA   1 ? 1 
ATOM   750  C C    . GLY   A 1 52  ? 3.33   -5.196  -7.905  1   59.2    ? 64  GLY   B C    1 ? 1 
ATOM   751  O O    . GLY   A 1 52  ? 3.478  -5.19   -6.691  1   52.327  ? 64  GLY   B O    1 ? 1 
ATOM   752  H H    . GLY   A 1 52  ? 3.99   -2.705  -7.129  1   59.158  ? 64  GLY   B H    1 c 1 
ATOM   753  H HA2  . GLY   A 1 52  ? 2.307  -3.824  -9.094  1   62.561  ? 64  GLY   B HA2  1 c 1 
ATOM   754  H HA3  . GLY   A 1 52  ? 3.896  -3.723  -9.266  1   59.849  ? 64  GLY   B HA3  1 c 1 
ATOM   755  N N    . LYS   A 1 53  ? 3.321  -6.311  -8.651  1   66.127  ? 65  LYS   B N    1 ? 1 
ATOM   756  C CA   . LYS   A 1 53  ? 3.348  -7.65   -8.049  1   70.702  ? 65  LYS   B CA   1 ? 1 
ATOM   757  C C    . LYS   A 1 53  ? 4.625  -8.39   -8.479  1   70.082  ? 65  LYS   B C    1 ? 1 
ATOM   758  O O    . LYS   A 1 53  ? 5.348  -8.891  -7.622  1   78.473  ? 65  LYS   B O    1 ? 1 
ATOM   759  C CB   . LYS   A 1 53  ? 2.046  -8.449  -8.274  1   62.94   ? 65  LYS   B CB   1 ? 1 
ATOM   760  H H    . LYS   A 1 53  ? 3.291  -6.238  -9.561  1   65.97   ? 65  LYS   B H    1 c 1 
ATOM   761  H HA   . LYS   A 1 53  ? 3.41   -7.528  -7.068  1   67.061  ? 65  LYS   B HA   1 c 1 
ATOM   762  H HB2  . LYS   A 1 53  ? 2.386  -9.56   -8.267  0   30      ? 65  LYS   B HB2  1 c 1 
ATOM   763  H HB3  . LYS   A 1 53  ? 1.337  -8.041  -8.048  0   30      ? 65  LYS   B HB3  1 c 1 
ATOM   764  N N    . LYS   A 1 54  ? 4.949  -8.415  -9.79   1   62.581  ? 66  LYS   B N    1 ? 1 
ATOM   765  C CA   . LYS   A 1 54  ? 6.062  -9.195  -10.315 1   56.092  ? 66  LYS   B CA   1 ? 1 
ATOM   766  C C    . LYS   A 1 54  ? 7.39   -8.436  -10.194 1   53.043  ? 66  LYS   B C    1 ? 1 
ATOM   767  O O    . LYS   A 1 54  ? 7.521  -7.22   -10.5   1   49.267  ? 66  LYS   B O    1 ? 1 
ATOM   768  C CB   . LYS   A 1 54  ? 5.909  -9.666  -11.768 1   64.165  ? 66  LYS   B CB   1 ? 1 
ATOM   769  H H    . LYS   A 1 54  ? 4.448  -7.925  -10.377 1   63.016  ? 66  LYS   B H    1 c 1 
ATOM   770  H HA   . LYS   A 1 54  ? 6.132  -10.015 -9.763  1   59.527  ? 66  LYS   B HA   1 c 1 
ATOM   771  H HB2  . LYS   A 1 54  ? 6.841  -9.772  -12.208 0   30      ? 66  LYS   B HB2  1 c 1 
ATOM   772  H HB3  . LYS   A 1 54  ? 4.991  -9.717  -12.037 0   30      ? 66  LYS   B HB3  1 c 1 
ATOM   773  N N    . PHE   A 1 55  ? 8.422  -9.221  -9.854  1   48.946  ? 67  PHE   B N    1 ? 1 
ATOM   774  C CA   . PHE   A 1 55  ? 9.757  -8.685  -9.689  1   53.093  ? 67  PHE   B CA   1 ? 1 
ATOM   775  C C    . PHE   A 1 55  ? 10.507 -8.832  -10.998 1   48.682  ? 67  PHE   B C    1 ? 1 
ATOM   776  O O    . PHE   A 1 55  ? 10.297 -9.764  -11.744 1   53.414  ? 67  PHE   B O    1 ? 1 
ATOM   777  C CB   . PHE   A 1 55  ? 10.552 -9.385  -8.573  1   58.519  ? 67  PHE   B CB   1 ? 1 
ATOM   778  C CG   . PHE   A 1 55  ? 9.996  -9.243  -7.157  1   64.349  ? 67  PHE   B CG   1 ? 1 
ATOM   779  C CD1  . PHE   A 1 55  ? 8.909  -10.006 -6.737  1   65.269  ? 67  PHE   B CD1  1 ? 1 
ATOM   780  C CD2  . PHE   A 1 55  ? 10.535 -8.319  -6.244  1   64.298  ? 67  PHE   B CD2  1 ? 1 
ATOM   781  C CE1  . PHE   A 1 55  ? 8.386  -9.854  -5.45   1   63.489  ? 67  PHE   B CE1  1 ? 1 
ATOM   782  C CE2  . PHE   A 1 55  ? 10.018 -8.197  -4.951  1   59.802  ? 67  PHE   B CE2  1 ? 1 
ATOM   783  C CZ   . PHE   A 1 55  ? 8.967  -9.004  -4.55   1   53.962  ? 67  PHE   B CZ   1 ? 1 
ATOM   784  H H    . PHE   A 1 55  ? 8.288  -10.116 -9.725  1   53.016  ? 67  PHE   B H    1 c 1 
ATOM   785  H HA   . PHE   A 1 55  ? 9.684  -7.722  -9.467  1   49.966  ? 67  PHE   B HA   1 c 1 
ATOM   786  H HB2  . PHE   A 1 55  ? 10.607 -10.342 -8.791  1   60.274  ? 67  PHE   B HB2  1 c 1 
ATOM   787  H HB3  . PHE   A 1 55  ? 11.47  -9.032  -8.584  1   57.121  ? 67  PHE   B HB3  1 c 1 
ATOM   788  H HD1  . PHE   A 1 55  ? 8.515  -10.624 -7.333  1   66.856  ? 67  PHE   B HD1  1 c 1 
ATOM   789  H HD2  . PHE   A 1 55  ? 11.276 -7.795  -6.501  1   60.832  ? 67  PHE   B HD2  1 c 1 
ATOM   790  H HE1  . PHE   A 1 55  ? 7.666  -10.4   -5.176  1   63.921  ? 67  PHE   B HE1  1 c 1 
ATOM   791  H HE2  . PHE   A 1 55  ? 10.407 -7.589  -4.343  1   57.342  ? 67  PHE   B HE2  1 c 1 
ATOM   792  H HZ   . PHE   A 1 55  ? 8.594  -8.902  -3.689  1   57.7    ? 67  PHE   B HZ   1 c 1 
ATOM   793  N N    . ASP   A 1 56  ? 11.456 -7.933  -11.208 1   44.566  ? 68  ASP   B N    1 ? 1 
ATOM   794  C CA   . ASP   A 1 56  ? 12.669 -8.234  -11.94  1   40.415  ? 68  ASP   B CA   1 ? 1 
ATOM   795  C C    . ASP   A 1 56  ? 13.624 -8.81   -10.908 1   41.935  ? 68  ASP   B C    1 ? 1 
ATOM   796  O O    . ASP   A 1 56  ? 13.934 -8.132  -9.907  1   37.475  ? 68  ASP   B O    1 ? 1 
ATOM   797  C CB   . ASP   A 1 56  ? 13.227 -6.978  -12.579 1   39.153  ? 68  ASP   B CB   1 ? 1 
ATOM   798  C CG   . ASP   A 1 56  ? 14.665 -7.045  -13.084 1   43.84   ? 68  ASP   B CG   1 ? 1 
ATOM   799  O OD1  . ASP   A 1 56  ? 15.002 -7.998  -13.791 1   43.875  ? 68  ASP   B OD1  1 ? 1 
ATOM   800  O OD2  . ASP   A 1 56  ? 15.463 -6.156  -12.767 1   36.203  ? 68  ASP   B OD2  1 ? 1 
ATOM   801  H H    . ASP   A 1 56  ? 11.342 -7.087  -10.881 1   42.544  ? 68  ASP   B H    1 c 1 
ATOM   802  H HA   . ASP   A 1 56  ? 12.474 -8.908  -12.629 1   43.483  ? 68  ASP   B HA   1 c 1 
ATOM   803  H HB2  . ASP   A 1 56  ? 12.654 -6.739  -13.337 1   40.701  ? 68  ASP   B HB2  1 c 1 
ATOM   804  H HB3  . ASP   A 1 56  ? 13.175 -6.249  -11.927 1   38.534  ? 68  ASP   B HB3  1 c 1 
ATOM   805  N N    . SER   A 1 57  ? 14.161 -9.997  -11.182 1   42.848  ? 69  SER   B N    1 ? 1 
ATOM   806  C CA   . SER   A 1 57  ? 15.113 -10.605 -10.23  1   50.113  ? 69  SER   B CA   1 ? 1 
ATOM   807  C C    . SER   A 1 57  ? 16.334 -11.205 -10.948 1   51.163  ? 69  SER   B C    1 ? 1 
ATOM   808  O O    . SER   A 1 57  ? 16.204 -11.925 -11.954 1   52.8    ? 69  SER   B O    1 ? 1 
ATOM   809  C CB   . SER   A 1 57  ? 14.476 -11.741 -9.377  1   63.966  ? 69  SER   B CB   1 ? 1 
ATOM   810  O OG   . SER   A 1 57  ? 15.402 -12.255 -8.421  1   63.51   ? 69  SER   B OG   1 ? 1 
ATOM   811  H H    . SER   A 1 57  ? 13.947 -10.44  -11.953 1   45.997  ? 69  SER   B H    1 c 1 
ATOM   812  H HA   . SER   A 1 57  ? 15.432 -9.898  -9.617  1   48.366  ? 69  SER   B HA   1 c 1 
ATOM   813  H HB2  . SER   A 1 57  ? 13.691 -11.393 -8.913  1   60.188  ? 69  SER   B HB2  1 c 1 
ATOM   814  H HB3  . SER   A 1 57  ? 14.186 -12.462 -9.966  1   62.721  ? 69  SER   B HB3  1 c 1 
ATOM   815  H HG   . SER   A 1 57  ? 15.073 -12.801 -7.869  0   30      ? 69  SER   B HG   1 c 1 
ATOM   816  N N    . SER   A 1 58  ? 17.492 -11.004 -10.328 1   44.983  ? 70  SER   B N    1 ? 1 
ATOM   817  C CA   . SER   A 1 58  ? 18.744 -11.545 -10.814 1   46.403  ? 70  SER   B CA   1 ? 1 
ATOM   818  C C    . SER   A 1 58  ? 18.74  -13.076 -10.756 1   52.366  ? 70  SER   B C    1 ? 1 
ATOM   819  O O    . SER   A 1 58  ? 19.345 -13.75  -11.614 1   60.604  ? 70  SER   B O    1 ? 1 
ATOM   820  C CB   . SER   A 1 58  ? 19.879 -10.953 -10.032 1   43.509  ? 70  SER   B CB   1 ? 1 
ATOM   821  O OG   . SER   A 1 58  ? 19.679 -11.095 -8.604  1   39.852  ? 70  SER   B OG   1 ? 1 
ATOM   822  H H    . SER   A 1 58  ? 17.502 -10.507 -9.561  1   44.805  ? 70  SER   B H    1 c 1 
ATOM   823  H HA   . SER   A 1 58  ? 18.845 -11.275 -11.762 1   46.916  ? 70  SER   B HA   1 c 1 
ATOM   824  H HB2  . SER   A 1 58  ? 20.711 -11.396 -10.287 1   44.402  ? 70  SER   B HB2  1 c 1 
ATOM   825  H HB3  . SER   A 1 58  ? 19.962 -10.006 -10.253 1   41.62   ? 70  SER   B HB3  1 c 1 
ATOM   826  H HG   . SER   A 1 58  ? 20.382 -10.74  -8.26   0   30      ? 70  SER   B HG   1 c 1 
ATOM   827  N N    . HIS   A 1 59  ? 18.018 -13.631 -9.766  1   54.136  ? 71  HIS   B N    1 ? 1 
ATOM   828  C CA   . HIS   A 1 59  ? 18.001 -15.08  -9.571  1   56.828  ? 71  HIS   B CA   1 ? 1 
ATOM   829  C C    . HIS   A 1 59  ? 17.314 -15.75  -10.742 1   59.556  ? 71  HIS   B C    1 ? 1 
ATOM   830  O O    . HIS   A 1 59  ? 17.656 -16.869 -11.098 1   62.811  ? 71  HIS   B O    1 ? 1 
ATOM   831  C CB   . HIS   A 1 59  ? 17.22  -15.502 -8.314  1   56.445  ? 71  HIS   B CB   1 ? 1 
ATOM   832  C CG   . HIS   A 1 59  ? 17.923 -15.178 -7.041  1   55.273  ? 71  HIS   B CG   1 ? 1 
ATOM   833  N ND1  . HIS   A 1 59  ? 19.138 -15.748 -6.737  1   57.661  ? 71  HIS   B ND1  1 ? 1 
ATOM   834  C CD2  . HIS   A 1 59  ? 17.657 -14.29  -6.075  1   54.968  ? 71  HIS   B CD2  1 ? 1 
ATOM   835  C CE1  . HIS   A 1 59  ? 19.555 -15.282 -5.561  1   61.268  ? 71  HIS   B CE1  1 ? 1 
ATOM   836  N NE2  . HIS   A 1 59  ? 18.678 -14.368 -5.157  1   63.463  ? 71  HIS   B NE2  1 ? 1 
ATOM   837  H H    . HIS   A 1 59  ? 17.539 -13.102 -9.196  1   52.193  ? 71  HIS   B H    1 c 1 
ATOM   838  H HA   . HIS   A 1 59  ? 18.931 -15.41  -9.518  1   57.683  ? 71  HIS   B HA   1 c 1 
ATOM   839  H HB2  . HIS   A 1 59  ? 16.347 -15.051 -8.32   1   55.691  ? 71  HIS   B HB2  1 c 1 
ATOM   840  H HB3  . HIS   A 1 59  ? 17.059 -16.47  -8.351  1   59.048  ? 71  HIS   B HB3  1 c 1 
ATOM   841  H HD1  . HIS   A 1 59  ? 19.606 -16.292 -7.262  0   30      ? 71  HIS   B HD1  1 c 1 
ATOM   842  H HD2  . HIS   A 1 59  ? 16.905 -13.735 -6.013  1   54.992  ? 71  HIS   B HD2  1 c 1 
ATOM   843  H HE1  . HIS   A 1 59  ? 20.354 -15.518 -5.121  1   61.624  ? 71  HIS   B HE1  1 c 1 
ATOM   844  H HE2  . HIS   A 1 59  ? 18.776 -13.963 -4.367  0   30      ? 71  HIS   B HE2  1 c 1 
ATOM   845  N N    . ASP   A 1 60  ? 16.311 -15.069 -11.302 1   62.326  ? 72  ASP   B N    1 ? 1 
ATOM   846  C CA   . ASP   A 1 60  ? 15.573 -15.626 -12.429 1   80.11   ? 72  ASP   B CA   1 ? 1 
ATOM   847  C C    . ASP   A 1 60  ? 16.493 -15.859 -13.642 1   82.057  ? 72  ASP   B C    1 ? 1 
ATOM   848  O O    . ASP   A 1 60  ? 16.188 -16.71  -14.477 1   91.795  ? 72  ASP   B O    1 ? 1 
ATOM   849  C CB   . ASP   A 1 60  ? 14.284 -14.858 -12.712 1   73.412  ? 72  ASP   B CB   1 ? 1 
ATOM   850  C CG   . ASP   A 1 60  ? 13.163 -15.104 -11.708 1   76.08   ? 72  ASP   B CG   1 ? 1 
ATOM   851  O OD1  . ASP   A 1 60  ? 13.317 -15.976 -10.81  1   65.928  ? 72  ASP   B OD1  1 ? 1 
ATOM   852  O OD2  . ASP   A 1 60  ? 12.152 -14.391 -11.816 1   79.732  ? 72  ASP   B OD2  1 ? 1 
ATOM   853  H H    . ASP   A 1 60  ? 16.071 -14.25  -10.975 1   62.172  ? 72  ASP   B H    1 c 1 
ATOM   854  H HA   . ASP   A 1 60  ? 15.259 -16.515 -12.15  1   77.505  ? 72  ASP   B HA   1 c 1 
ATOM   855  H HB2  . ASP   A 1 60  ? 14.488 -13.901 -12.716 1   72.854  ? 72  ASP   B HB2  1 c 1 
ATOM   856  H HB3  . ASP   A 1 60  ? 13.957 -15.103 -13.603 1   76.718  ? 72  ASP   B HB3  1 c 1 
ATOM   857  N N    . ARG   A 1 61  ? 17.613 -15.12  -13.731 1   79.862  ? 73  ARG   B N    1 ? 1 
ATOM   858  C CA   . ARG   A 1 61  ? 18.623 -15.31  -14.763 1   72.164  ? 73  ARG   B CA   1 ? 1 
ATOM   859  C C    . ARG   A 1 61  ? 19.788 -16.142 -14.219 1   69.817  ? 73  ARG   B C    1 ? 1 
ATOM   860  O O    . ARG   A 1 61  ? 20.798 -16.298 -14.907 1   72.674  ? 73  ARG   B O    1 ? 1 
ATOM   861  C CB   . ARG   A 1 61  ? 19.043 -13.903 -15.198 1   74.175  ? 73  ARG   B CB   1 ? 1 
ATOM   862  C CG   . ARG   A 1 61  ? 17.862 -13.126 -15.778 1   68.659  ? 73  ARG   B CG   1 ? 1 
ATOM   863  C CD   . ARG   A 1 61  ? 18.245 -11.73  -16.228 1   62.7    ? 73  ARG   B CD   1 ? 1 
ATOM   864  N NE   . ARG   A 1 61  ? 18.828 -10.957 -15.117 1   68.035  ? 73  ARG   B NE   1 ? 1 
ATOM   865  C CZ   . ARG   A 1 61  ? 18.198 -10.036 -14.374 1   54.167  ? 73  ARG   B CZ   1 ? 1 
ATOM   866  N NH1  . ARG   A 1 61  ? 16.882 -9.919  -14.453 1   56.713  ? 73  ARG   B NH1  1 ? 1 
ATOM   867  N NH2  . ARG   A 1 61  ? 18.868 -9.264  -13.523 1   48.355  ? 73  ARG   B NH2  1 ? 1 
ATOM   868  H H    . ARG   A 1 61  ? 17.741 -14.448 -13.125 1   75.027  ? 73  ARG   B H    1 c 1 
ATOM   869  H HA   . ARG   A 1 61  ? 18.214 -15.785 -15.53  1   75.919  ? 73  ARG   B HA   1 c 1 
ATOM   870  H HB2  . ARG   A 1 61  ? 19.403 -13.418 -14.425 1   70.287  ? 73  ARG   B HB2  1 c 1 
ATOM   871  H HB3  . ARG   A 1 61  ? 19.751 -13.969 -15.874 1   73.194  ? 73  ARG   B HB3  1 c 1 
ATOM   872  H HG2  . ARG   A 1 61  ? 17.499 -13.619 -16.546 1   70.673  ? 73  ARG   B HG2  1 c 1 
ATOM   873  H HG3  . ARG   A 1 61  ? 17.154 -13.058 -15.102 1   67.791  ? 73  ARG   B HG3  1 c 1 
ATOM   874  H HD2  . ARG   A 1 61  ? 18.897 -11.79  -16.956 1   66.461  ? 73  ARG   B HD2  1 c 1 
ATOM   875  H HD3  . ARG   A 1 61  ? 17.453 -11.266 -16.568 1   64.731  ? 73  ARG   B HD3  1 c 1 
ATOM   876  H HE   . ARG   A 1 61  ? 19.663 -11.111 -14.922 1   63.346  ? 73  ARG   B HE   1 c 1 
ATOM   877  H HH11 . ARG   A 1 61  ? 16.37  -10.626 -14.311 1   56.96   ? 73  ARG   B HH11 1 c 1 
ATOM   878  H HH12 . ARG   A 1 61  ? 16.522 -9.136  -14.647 1   54.763  ? 73  ARG   B HH12 1 c 1 
ATOM   879  H HH21 . ARG   A 1 61  ? 19.751 -9.302  -13.493 1   49.912  ? 73  ARG   B HH21 1 c 1 
ATOM   880  H HH22 . ARG   A 1 61  ? 18.427 -8.715  -12.99  1   47.999  ? 73  ARG   B HH22 1 c 1 
ATOM   881  N N    . ASN   A 1 62  ? 19.665 -16.602 -12.957 1   63.223  ? 74  ASN   B N    1 ? 1 
ATOM   882  C CA   . ASN   A 1 62  ? 20.64  -17.436 -12.268 1   66.649  ? 74  ASN   B CA   1 ? 1 
ATOM   883  C C    . ASN   A 1 62  ? 22.062 -16.84  -12.35  1   68.97   ? 74  ASN   B C    1 ? 1 
ATOM   884  O O    . ASN   A 1 62  ? 23.039 -17.602 -12.378 1   74.351  ? 74  ASN   B O    1 ? 1 
ATOM   885  C CB   . ASN   A 1 62  ? 20.498 -18.909 -12.738 1   65.673  ? 74  ASN   B CB   1 ? 1 
ATOM   886  H H    . ASN   A 1 62  ? 18.913 -16.374 -12.495 1   64.272  ? 74  ASN   B H    1 c 1 
ATOM   887  H HA   . ASN   A 1 62  ? 20.392 -17.429 -11.316 1   64.956  ? 74  ASN   B HA   1 c 1 
ATOM   888  H HB2  . ASN   A 1 62  ? 21.384 -19.314 -12.88  0   30      ? 74  ASN   B HB2  1 c 1 
ATOM   889  H HB3  . ASN   A 1 62  ? 19.545 -19.145 -12.826 0   30      ? 74  ASN   B HB3  1 c 1 
ATOM   890  N N    . GLU   A 1 63  ? 22.22  -15.497 -12.423 1   68.231  ? 75  GLU   B N    1 ? 1 
ATOM   891  C CA   . GLU   A 1 63  ? 23.558 -14.912 -12.342 1   69.016  ? 75  GLU   B CA   1 ? 1 
ATOM   892  C C    . GLU   A 1 63  ? 23.509 -13.571 -11.602 1   62.479  ? 75  GLU   B C    1 ? 1 
ATOM   893  O O    . GLU   A 1 63  ? 22.558 -12.781 -11.794 1   56.696  ? 75  GLU   B O    1 ? 1 
ATOM   894  C CB   . GLU   A 1 63  ? 24.293 -14.723 -13.677 1   74.664  ? 75  GLU   B CB   1 ? 1 
ATOM   895  C CG   . GLU   A 1 63  ? 23.876 -13.527 -14.532 1   76.015  ? 75  GLU   B CG   1 ? 1 
ATOM   896  C CD   . GLU   A 1 63  ? 24.66  -13.341 -15.838 1   84.479  ? 75  GLU   B CD   1 ? 1 
ATOM   897  O OE1  . GLU   A 1 63  ? 24.424 -12.34  -16.561 1   77.957  ? 75  GLU   B OE1  1 ? 1 
ATOM   898  O OE2  . GLU   A 1 63  ? 25.498 -14.216 -16.164 1   90.725  ? 75  GLU   B OE2  1 ? 1 
ATOM   899  H H    . GLU   A 1 63  ? 21.495 -14.948 -12.51  1   66.339  ? 75  GLU   B H    1 c 1 
ATOM   900  H HA   . GLU   A 1 63  ? 24.112 -15.528 -11.804 1   70.067  ? 75  GLU   B HA   1 c 1 
ATOM   901  H HB2  . GLU   A 1 63  ? 25.251 -14.638 -13.492 1   74.947  ? 75  GLU   B HB2  1 c 1 
ATOM   902  H HB3  . GLU   A 1 63  ? 24.168 -15.533 -14.214 1   76.709  ? 75  GLU   B HB3  1 c 1 
ATOM   903  H HG2  . GLU   A 1 63  ? 22.925 -13.616 -14.755 1   76.336  ? 75  GLU   B HG2  1 c 1 
ATOM   904  H HG3  . GLU   A 1 63  ? 23.973 -12.708 -14.002 1   74.373  ? 75  GLU   B HG3  1 c 1 
ATOM   905  N N    . PRO   A 1 64  ? 24.584 -13.24  -10.837 1   56.183  ? 76  PRO   B N    1 ? 1 
ATOM   906  C CA   . PRO   A 1 64  ? 24.617 -11.977 -10.077 1   51.766  ? 76  PRO   B CA   1 ? 1 
ATOM   907  C C    . PRO   A 1 64  ? 24.654 -10.799 -11.043 1   52.808  ? 76  PRO   B C    1 ? 1 
ATOM   908  O O    . PRO   A 1 64  ? 25.052 -10.959 -12.218 1   48.955  ? 76  PRO   B O    1 ? 1 
ATOM   909  C CB   . PRO   A 1 64  ? 25.892 -12.029 -9.247  1   55.819  ? 76  PRO   B CB   1 ? 1 
ATOM   910  C CG   . PRO   A 1 64  ? 26.376 -13.446 -9.372  1   59.69   ? 76  PRO   B CG   1 ? 1 
ATOM   911  C CD   . PRO   A 1 64  ? 25.817 -14.026 -10.684 1   59.968  ? 76  PRO   B CD   1 ? 1 
ATOM   912  H HA   . PRO   A 1 64  ? 23.825 -11.918 -9.485  1   51.851  ? 76  PRO   B HA   1 c 1 
ATOM   913  H HB2  . PRO   A 1 64  ? 26.565 -11.398 -9.595  1   55.004  ? 76  PRO   B HB2  1 c 1 
ATOM   914  H HB3  . PRO   A 1 64  ? 25.706 -11.805 -8.306  1   54.003  ? 76  PRO   B HB3  1 c 1 
ATOM   915  H HG2  . PRO   A 1 64  ? 27.356 -13.469 -9.385  1   60.484  ? 76  PRO   B HG2  1 c 1 
ATOM   916  H HG3  . PRO   A 1 64  ? 26.068 -13.978 -8.609  1   59.609  ? 76  PRO   B HG3  1 c 1 
ATOM   917  H HD2  . PRO   A 1 64  ? 26.434 -13.878 -11.434 1   60.909  ? 76  PRO   B HD2  1 c 1 
ATOM   918  H HD3  . PRO   A 1 64  ? 25.628 -14.986 -10.592 1   61.842  ? 76  PRO   B HD3  1 c 1 
ATOM   919  N N    . PHE   A 1 65  ? 24.194 -9.638  -10.527 1   44.384  ? 77  PHE   B N    1 ? 1 
ATOM   920  C CA   . PHE   A 1 65  ? 24.154 -8.382  -11.25  1   42.227  ? 77  PHE   B CA   1 ? 1 
ATOM   921  C C    . PHE   A 1 65  ? 25.394 -7.623  -10.826 1   42.839  ? 77  PHE   B C    1 ? 1 
ATOM   922  O O    . PHE   A 1 65  ? 25.64  -7.417  -9.627  1   38.496  ? 77  PHE   B O    1 ? 1 
ATOM   923  C CB   . PHE   A 1 65  ? 22.89  -7.592  -10.958 1   38.679  ? 77  PHE   B CB   1 ? 1 
ATOM   924  C CG   . PHE   A 1 65  ? 22.827 -6.26   -11.671 1   37.709  ? 77  PHE   B CG   1 ? 1 
ATOM   925  C CD1  . PHE   A 1 65  ? 22.801 -6.198  -13.061 1   45.191  ? 77  PHE   B CD1  1 ? 1 
ATOM   926  C CD2  . PHE   A 1 65  ? 22.975 -5.08   -10.957 1   39.332  ? 77  PHE   B CD2  1 ? 1 
ATOM   927  C CE1  . PHE   A 1 65  ? 22.766 -4.974  -13.714 1   45.975  ? 77  PHE   B CE1  1 ? 1 
ATOM   928  C CE2  . PHE   A 1 65  ? 22.993 -3.862  -11.598 1   40.218  ? 77  PHE   B CE2  1 ? 1 
ATOM   929  C CZ   . PHE   A 1 65  ? 22.869 -3.813  -12.987 1   40.959  ? 77  PHE   B CZ   1 ? 1 
ATOM   930  H H    . PHE   A 1 65  ? 23.889 -9.643  -9.665  1   44.64   ? 77  PHE   B H    1 c 1 
ATOM   931  H HA   . PHE   A 1 65  ? 24.198 -8.569  -12.225 1   43.451  ? 77  PHE   B HA   1 c 1 
ATOM   932  H HB2  . PHE   A 1 65  ? 22.116 -8.135  -11.227 1   39.391  ? 77  PHE   B HB2  1 c 1 
ATOM   933  H HB3  . PHE   A 1 65  ? 22.833 -7.441  -9.988  1   38.072  ? 77  PHE   B HB3  1 c 1 
ATOM   934  H HD1  . PHE   A 1 65  ? 22.706 -6.995  -13.559 1   45.26   ? 77  PHE   B HD1  1 c 1 
ATOM   935  H HD2  . PHE   A 1 65  ? 23.043 -5.112  -10.016 1   38.259  ? 77  PHE   B HD2  1 c 1 
ATOM   936  H HE1  . PHE   A 1 65  ? 22.707 -4.941  -14.655 1   45.684  ? 77  PHE   B HE1  1 c 1 
ATOM   937  H HE2  . PHE   A 1 65  ? 23.044 -3.064  -11.097 1   38.709  ? 77  PHE   B HE2  1 c 1 
ATOM   938  H HZ   . PHE   A 1 65  ? 22.875 -2.979  -13.431 1   41.493  ? 77  PHE   B HZ   1 c 1 
ATOM   939  N N    . VAL   A 1 66  ? 26.206 -7.326  -11.829 1   40.26   ? 78  VAL   B N    1 ? 1 
ATOM   940  C CA   . VAL   A 1 66  ? 27.456 -6.628  -11.586 1   45.602  ? 78  VAL   B CA   1 ? 1 
ATOM   941  C C    . VAL   A 1 66  ? 27.362 -5.19   -12.114 1   46.567  ? 78  VAL   B C    1 ? 1 
ATOM   942  O O    . VAL   A 1 66  ? 26.83  -4.991  -13.213 1   42.002  ? 78  VAL   B O    1 ? 1 
ATOM   943  C CB   . VAL   A 1 66  ? 28.562 -7.428  -12.268 1   52.77   ? 78  VAL   B CB   1 ? 1 
ATOM   944  C CG1  . VAL   A 1 66  ? 29.904 -6.689  -12.189 1   53.952  ? 78  VAL   B CG1  1 ? 1 
ATOM   945  C CG2  . VAL   A 1 66  ? 28.608 -8.846  -11.671 1   54.95   ? 78  VAL   B CG2  1 ? 1 
ATOM   946  H H    . VAL   A 1 66  ? 25.985 -7.558  -12.685 1   43.051  ? 78  VAL   B H    1 c 1 
ATOM   947  H HA   . VAL   A 1 66  ? 27.626 -6.607  -10.629 1   45.042  ? 78  VAL   B HA   1 c 1 
ATOM   948  H HB   . VAL   A 1 66  ? 28.318 -7.509  -13.22  1   52.721  ? 78  VAL   B HB   1 c 1 
ATOM   949  H HG11 . VAL   A 1 66  ? 30.034 -6.346  -11.289 1   53.036  ? 78  VAL   B HG11 1 c 1 
ATOM   950  H HG12 . VAL   A 1 66  ? 29.908 -5.951  -12.821 1   53.794  ? 78  VAL   B HG12 1 c 1 
ATOM   951  H HG13 . VAL   A 1 66  ? 30.623 -7.303  -12.408 1   56.265  ? 78  VAL   B HG13 1 c 1 
ATOM   952  H HG21 . VAL   A 1 66  ? 29.448 -9.273  -11.911 1   56.773  ? 78  VAL   B HG21 1 c 1 
ATOM   953  H HG22 . VAL   A 1 66  ? 27.868 -9.371  -12.021 1   54.659  ? 78  VAL   B HG22 1 c 1 
ATOM   954  H HG23 . VAL   A 1 66  ? 28.538 -8.794  -10.703 1   53.683  ? 78  VAL   B HG23 1 c 1 
ATOM   955  N N    . PHE   A 1 67  ? 27.92  -4.235  -11.349 1   42.229  ? 79  PHE   B N    1 ? 1 
ATOM   956  C CA   . PHE   A 1 67  ? 28.035 -2.834  -11.772 1   42.479  ? 79  PHE   B CA   1 ? 1 
ATOM   957  C C    . PHE   A 1 67  ? 29.173 -2.128  -11.016 1   46.365  ? 79  PHE   B C    1 ? 1 
ATOM   958  O O    . PHE   A 1 67  ? 29.546 -2.584  -9.967  1   44.195  ? 79  PHE   B O    1 ? 1 
ATOM   959  C CB   . PHE   A 1 67  ? 26.721 -2.079  -11.5   1   38.779  ? 79  PHE   B CB   1 ? 1 
ATOM   960  C CG   . PHE   A 1 67  ? 26.408 -1.708  -10.046 1   36.453  ? 79  PHE   B CG   1 ? 1 
ATOM   961  C CD1  . PHE   A 1 67  ? 25.938 -2.653  -9.139  1   42.923  ? 79  PHE   B CD1  1 ? 1 
ATOM   962  C CD2  . PHE   A 1 67  ? 26.525 -0.401  -9.604  1   38.193  ? 79  PHE   B CD2  1 ? 1 
ATOM   963  C CE1  . PHE   A 1 67  ? 25.626 -2.286  -7.83   1   39.501  ? 79  PHE   B CE1  1 ? 1 
ATOM   964  C CE2  . PHE   A 1 67  ? 26.202 -0.042  -8.303  1   35.048  ? 79  PHE   B CE2  1 ? 1 
ATOM   965  C CZ   . PHE   A 1 67  ? 25.763 -0.987  -7.426  1   37.911  ? 79  PHE   B CZ   1 ? 1 
ATOM   966  H H    . PHE   A 1 67  ? 28.241 -4.466  -10.525 1   43.26   ? 79  PHE   B H    1 c 1 
ATOM   967  H HA   . PHE   A 1 67  ? 28.228 -2.806  -12.747 1   43.844  ? 79  PHE   B HA   1 c 1 
ATOM   968  H HB2  . PHE   A 1 67  ? 26.732 -1.254  -12.033 1   38.932  ? 79  PHE   B HB2  1 c 1 
ATOM   969  H HB3  . PHE   A 1 67  ? 25.981 -2.628  -11.843 1   38.634  ? 79  PHE   B HB3  1 c 1 
ATOM   970  H HD1  . PHE   A 1 67  ? 25.838 -3.552  -9.411  1   41.32   ? 79  PHE   B HD1  1 c 1 
ATOM   971  H HD2  . PHE   A 1 67  ? 26.824 0.262   -10.206 1   37.779  ? 79  PHE   B HD2  1 c 1 
ATOM   972  H HE1  . PHE   A 1 67  ? 25.321 -2.939  -7.22   1   39.515  ? 79  PHE   B HE1  1 c 1 
ATOM   973  H HE2  . PHE   A 1 67  ? 26.305 0.853   -8.022  1   35.934  ? 79  PHE   B HE2  1 c 1 
ATOM   974  H HZ   . PHE   A 1 67  ? 25.556 -0.746  -6.537  1   36.495  ? 79  PHE   B HZ   1 c 1 
ATOM   975  N N    . SER   A 1 68  ? 29.63  -0.968  -11.503 1   45.561  ? 80  SER   B N    1 ? 1 
ATOM   976  C CA   . SER   A 1 68  ? 30.617 -0.119  -10.856 1   43.515  ? 80  SER   B CA   1 ? 1 
ATOM   977  C C    . SER   A 1 68  ? 29.915 1.008   -10.083 1   45.635  ? 80  SER   B C    1 ? 1 
ATOM   978  O O    . SER   A 1 68  ? 29.133 1.758   -10.659 1   37.836  ? 80  SER   B O    1 ? 1 
ATOM   979  C CB   . SER   A 1 68  ? 31.576 0.487   -11.87  1   50.299  ? 80  SER   B CB   1 ? 1 
ATOM   980  O OG   . SER   A 1 68  ? 32.304 -0.52   -12.593 1   51.284  ? 80  SER   B OG   1 ? 1 
ATOM   981  H H    . SER   A 1 68  ? 29.295 -0.689  -12.306 1   45.229  ? 80  SER   B H    1 c 1 
ATOM   982  H HA   . SER   A 1 68  ? 31.134 -0.669  -10.22  1   46.287  ? 80  SER   B HA   1 c 1 
ATOM   983  H HB2  . SER   A 1 68  ? 31.07  1.034   -12.501 1   48.436  ? 80  SER   B HB2  1 c 1 
ATOM   984  H HB3  . SER   A 1 68  ? 32.207 1.07    -11.406 1   49.682  ? 80  SER   B HB3  1 c 1 
ATOM   985  H HG   . SER   A 1 68  ? 32.847 -0.085  -13.134 0   30      ? 80  SER   B HG   1 c 1 
ATOM   986  N N    . LEU   A 1 69  ? 30.247 1.182   -8.81   1   45.213  ? 81  LEU   B N    1 ? 1 
ATOM   987  C CA   . LEU   A 1 69  ? 29.51  2.118   -7.963  1   40.979  ? 81  LEU   B CA   1 ? 1 
ATOM   988  C C    . LEU   A 1 69  ? 29.793 3.576   -8.312  1   46.614  ? 81  LEU   B C    1 ? 1 
ATOM   989  O O    . LEU   A 1 69  ? 30.944 3.99    -8.445  1   46.79   ? 81  LEU   B O    1 ? 1 
ATOM   990  C CB   . LEU   A 1 69  ? 29.883 1.859   -6.504  1   43.676  ? 81  LEU   B CB   1 ? 1 
ATOM   991  C CG   . LEU   A 1 69  ? 29.139 2.704   -5.459  1   41.884  ? 81  LEU   B CG   1 ? 1 
ATOM   992  C CD1  . LEU   A 1 69  ? 27.717 2.346   -5.355  1   40.471  ? 81  LEU   B CD1  1 ? 1 
ATOM   993  C CD2  . LEU   A 1 69  ? 29.743 2.645   -4.071  1   45.985  ? 81  LEU   B CD2  1 ? 1 
ATOM   994  H H    . LEU   A 1 69  ? 30.947 0.715   -8.453  1   45.85   ? 81  LEU   B H    1 c 1 
ATOM   995  H HA   . LEU   A 1 69  ? 28.541 1.945   -8.084  1   41.283  ? 81  LEU   B HA   1 c 1 
ATOM   996  H HB2  . LEU   A 1 69  ? 29.716 0.907   -6.309  1   42.824  ? 81  LEU   B HB2  1 c 1 
ATOM   997  H HB3  . LEU   A 1 69  ? 30.85  2.019   -6.402  1   44.745  ? 81  LEU   B HB3  1 c 1 
ATOM   998  H HG   . LEU   A 1 69  ? 29.18  3.65    -5.753  1   42.859  ? 81  LEU   B HG   1 c 1 
ATOM   999  H HD11 . LEU   A 1 69  ? 27.266 2.558   -6.189  1   39.754  ? 81  LEU   B HD11 1 c 1 
ATOM   1000 H HD12 . LEU   A 1 69  ? 27.307 2.846   -4.63   1   39.364  ? 81  LEU   B HD12 1 c 1 
ATOM   1001 H HD13 . LEU   A 1 69  ? 27.635 1.394   -5.177  1   40.176  ? 81  LEU   B HD13 1 c 1 
ATOM   1002 H HD21 . LEU   A 1 69  ? 30.71  2.62    -4.138  1   46.79   ? 81  LEU   B HD21 1 c 1 
ATOM   1003 H HD22 . LEU   A 1 69  ? 29.43  1.847   -3.613  1   44.467  ? 81  LEU   B HD22 1 c 1 
ATOM   1004 H HD23 . LEU   A 1 69  ? 29.475 3.432   -3.566  1   44.445  ? 81  LEU   B HD23 1 c 1 
ATOM   1005 N N    . GLY   A 1 70  ? 28.718 4.373   -8.398  1   48.045  ? 82  GLY   B N    1 ? 1 
ATOM   1006 C CA   . GLY   A 1 70  ? 28.815 5.816   -8.509  1   48.798  ? 82  GLY   B CA   1 ? 1 
ATOM   1007 C C    . GLY   A 1 70  ? 29.148 6.293   -9.918  1   53.071  ? 82  GLY   B C    1 ? 1 
ATOM   1008 O O    . GLY   A 1 70  ? 29.453 7.468   -10.089 1   58.671  ? 82  GLY   B O    1 ? 1 
ATOM   1009 H H    . GLY   A 1 70  ? 27.887 3.993   -8.39   1   45.731  ? 82  GLY   B H    1 c 1 
ATOM   1010 H HA2  . GLY   A 1 70  ? 27.959 6.215   -8.228  1   47.775  ? 82  GLY   B HA2  1 c 1 
ATOM   1011 H HA3  . GLY   A 1 70  ? 29.509 6.136   -7.887  1   50.226  ? 82  GLY   B HA3  1 c 1 
ATOM   1012 N N    . LYS   A 1 71  ? 29.179 5.374   -10.908 1   48.38   ? 83  LYS   B N    1 ? 1 
ATOM   1013 C CA   . LYS   A 1 71  ? 29.577 5.671   -12.265 1   49.166  ? 83  LYS   B CA   1 ? 1 
ATOM   1014 C C    . LYS   A 1 71  ? 28.31  5.908   -13.104 1   53.173  ? 83  LYS   B C    1 ? 1 
ATOM   1015 O O    . LYS   A 1 71  ? 28.4   6.011   -14.325 1   55.938  ? 83  LYS   B O    1 ? 1 
ATOM   1016 C CB   . LYS   A 1 71  ? 30.541 4.604   -12.833 1   48.895  ? 83  LYS   B CB   1 ? 1 
ATOM   1017 H H    . LYS   A 1 71  ? 28.917 4.52    -10.717 1   48.438  ? 83  LYS   B H    1 c 1 
ATOM   1018 H HA   . LYS   A 1 71  ? 30.083 6.522   -12.249 1   51.205  ? 83  LYS   B HA   1 c 1 
ATOM   1019 H HB2  . LYS   A 1 71  ? 31.46  4.859   -12.651 0   30      ? 83  LYS   B HB2  1 c 1 
ATOM   1020 H HB3  . LYS   A 1 71  ? 30.009 3.825   -13.182 0   30      ? 83  LYS   B HB3  1 c 1 
ATOM   1021 N N    . GLY   A 1 72  ? 27.152 6.013   -12.428 1   50.597  ? 84  GLY   B N    1 ? 1 
ATOM   1022 C CA   . GLY   A 1 72  ? 25.845 6.216   -13.049 1   59.222  ? 84  GLY   B CA   1 ? 1 
ATOM   1023 C C    . GLY   A 1 72  ? 25.4   5.085   -13.993 1   53.827  ? 84  GLY   B C    1 ? 1 
ATOM   1024 O O    . GLY   A 1 72  ? 24.675 5.327   -14.951 1   51.095  ? 84  GLY   B O    1 ? 1 
ATOM   1025 H H    . GLY   A 1 72  ? 27.177 5.953   -11.517 1   51.655  ? 84  GLY   B H    1 c 1 
ATOM   1026 H HA2  . GLY   A 1 72  ? 25.173 6.318   -12.335 1   53.883  ? 84  GLY   B HA2  1 c 1 
ATOM   1027 H HA3  . GLY   A 1 72  ? 25.868 7.063   -13.554 1   56.357  ? 84  GLY   B HA3  1 c 1 
ATOM   1028 N N    . GLN   A 1 73  ? 25.801 3.836   -13.718 1   46.679  ? 85  GLN   B N    1 ? 1 
ATOM   1029 C CA   . GLN   A 1 73  ? 25.371 2.687   -14.496 1   41.334  ? 85  GLN   B CA   1 ? 1 
ATOM   1030 C C    . GLN   A 1 73  ? 24.025 2.187   -13.967 1   39.739  ? 85  GLN   B C    1 ? 1 
ATOM   1031 O O    . GLN   A 1 73  ? 23.345 1.412   -14.63  1   38.113  ? 85  GLN   B O    1 ? 1 
ATOM   1032 C CB   . GLN   A 1 73  ? 26.372 1.53    -14.386 1   41.414  ? 85  GLN   B CB   1 ? 1 
ATOM   1033 C CG   . GLN   A 1 73  ? 27.773 1.944   -14.817 1   47.814  ? 85  GLN   B CG   1 ? 1 
ATOM   1034 C CD   . GLN   A 1 73  ? 28.808 0.883   -14.557 1   49.902  ? 85  GLN   B CD   1 ? 1 
ATOM   1035 O OE1  . GLN   A 1 73  ? 28.533 -0.141  -13.93  1   58.631  ? 85  GLN   B OE1  1 ? 1 
ATOM   1036 N NE2  . GLN   A 1 73  ? 30.003 1.128   -15.047 1   54.144  ? 85  GLN   B NE2  1 ? 1 
ATOM   1037 H H    . GLN   A 1 73  ? 26.362 3.698   -13.011 1   46.736  ? 85  GLN   B H    1 c 1 
ATOM   1038 H HA   . GLN   A 1 73  ? 25.273 2.956   -15.444 1   43.322  ? 85  GLN   B HA   1 c 1 
ATOM   1039 H HB2  . GLN   A 1 73  ? 26.398 1.217   -13.457 1   41.681  ? 85  GLN   B HB2  1 c 1 
ATOM   1040 H HB3  . GLN   A 1 73  ? 26.067 0.787   -14.947 1   42.983  ? 85  GLN   B HB3  1 c 1 
ATOM   1041 H HG2  . GLN   A 1 73  ? 27.768 2.151   -15.775 1   48.189  ? 85  GLN   B HG2  1 c 1 
ATOM   1042 H HG3  . GLN   A 1 73  ? 28.034 2.758   -14.337 1   46.835  ? 85  GLN   B HG3  1 c 1 
ATOM   1043 H HE21 . GLN   A 1 73  ? 30.683 0.598   -14.838 1   54.785  ? 85  GLN   B HE21 1 c 1 
ATOM   1044 H HE22 . GLN   A 1 73  ? 30.13  1.821   -15.586 1   54.426  ? 85  GLN   B HE22 1 c 1 
ATOM   1045 N N    . VAL   A 1 74  ? 23.623 2.652   -12.793 1   34.022  ? 86  VAL   B N    1 ? 1 
ATOM   1046 C CA   . VAL   A 1 74  ? 22.386 2.259   -12.172 1   33.058  ? 86  VAL   B CA   1 ? 1 
ATOM   1047 C C    . VAL   A 1 74  ? 21.727 3.554   -11.68  1   32.754  ? 86  VAL   B C    1 ? 1 
ATOM   1048 O O    . VAL   A 1 74  ? 22.358 4.613   -11.736 1   31.782  ? 86  VAL   B O    1 ? 1 
ATOM   1049 C CB   . VAL   A 1 74  ? 22.636 1.337   -10.995 1   34.658  ? 86  VAL   B CB   1 ? 1 
ATOM   1050 C CG1  . VAL   A 1 74  ? 23.104 -0.033  -11.523 1   34.619  ? 86  VAL   B CG1  1 ? 1 
ATOM   1051 C CG2  . VAL   A 1 74  ? 23.654 1.953   -10.037 1   37.077  ? 86  VAL   B CG2  1 ? 1 
ATOM   1052 H H    . VAL   A 1 74  ? 24.155 3.25    -12.351 1   35.433  ? 86  VAL   B H    1 c 1 
ATOM   1053 H HA   . VAL   A 1 74  ? 21.807 1.82    -12.825 1   33.703  ? 86  VAL   B HA   1 c 1 
ATOM   1054 H HB   . VAL   A 1 74  ? 21.781 1.217   -10.518 1   33.293  ? 86  VAL   B HB   1 c 1 
ATOM   1055 H HG11 . VAL   A 1 74  ? 23.97  0.063   -11.954 1   36.183  ? 86  VAL   B HG11 1 c 1 
ATOM   1056 H HG12 . VAL   A 1 74  ? 22.459 -0.372  -12.167 1   35.169  ? 86  VAL   B HG12 1 c 1 
ATOM   1057 H HG13 . VAL   A 1 74  ? 23.18  -0.659  -10.783 1   34.775  ? 86  VAL   B HG13 1 c 1 
ATOM   1058 H HG21 . VAL   A 1 74  ? 23.665 1.446   -9.207  1   35.919  ? 86  VAL   B HG21 1 c 1 
ATOM   1059 H HG22 . VAL   A 1 74  ? 23.412 2.874   -9.847  1   35.835  ? 86  VAL   B HG22 1 c 1 
ATOM   1060 H HG23 . VAL   A 1 74  ? 24.538 1.927   -10.44  1   37.55   ? 86  VAL   B HG23 1 c 1 
ATOM   1061 N N    . ILE   A 1 75  ? 20.483 3.425   -11.227 1   27.881  ? 87  ILE   B N    1 ? 1 
ATOM   1062 C CA   . ILE   A 1 75  ? 19.742 4.564   -10.7   1   28.987  ? 87  ILE   B CA   1 ? 1 
ATOM   1063 C C    . ILE   A 1 75  ? 20.468 5.216   -9.513  1   27.332  ? 87  ILE   B C    1 ? 1 
ATOM   1064 O O    . ILE   A 1 75  ? 21.198 4.558   -8.789  1   28.227  ? 87  ILE   B O    1 ? 1 
ATOM   1065 C CB   . ILE   A 1 75  ? 18.279 4.197   -10.328 1   29.656  ? 87  ILE   B CB   1 ? 1 
ATOM   1066 C CG1  . ILE   A 1 75  ? 18.181 3.033   -9.443  1   27.438  ? 87  ILE   B CG1  1 ? 1 
ATOM   1067 C CG2  . ILE   A 1 75  ? 17.351 4.067   -11.56  1   32.99   ? 87  ILE   B CG2  1 ? 1 
ATOM   1068 C CD1  . ILE   A 1 75  ? 16.766 2.815   -8.911  1   27.098  ? 87  ILE   B CD1  1 ? 1 
ATOM   1069 H H    . ILE   A 1 75  ? 20.076 2.608   -11.263 1   29.09   ? 87  ILE   B H    1 c 1 
ATOM   1070 H HA   . ILE   A 1 75  ? 19.698 5.23    -11.413 1   29.281  ? 87  ILE   B HA   1 c 1 
ATOM   1071 H HB   . ILE   A 1 75  ? 17.938 4.953   -9.812  1   28.969  ? 87  ILE   B HB   1 c 1 
ATOM   1072 H HG12 . ILE   A 1 75  ? 18.46  2.233   -9.933  1   28.443  ? 87  ILE   B HG12 1 c 1 
ATOM   1073 H HG13 . ILE   A 1 75  ? 18.79  3.153   -8.686  1   27.632  ? 87  ILE   B HG13 1 c 1 
ATOM   1074 H HG21 . ILE   A 1 75  ? 16.423 4.105   -11.277 1   31.717  ? 87  ILE   B HG21 1 c 1 
ATOM   1075 H HG22 . ILE   A 1 75  ? 17.518 3.219   -12.005 1   32.67   ? 87  ILE   B HG22 1 c 1 
ATOM   1076 H HG23 . ILE   A 1 75  ? 17.528 4.795   -12.179 1   32.748  ? 87  ILE   B HG23 1 c 1 
ATOM   1077 H HD11 . ILE   A 1 75  ? 16.365 3.673   -8.676  1   26.716  ? 87  ILE   B HD11 1 c 1 
ATOM   1078 H HD12 . ILE   A 1 75  ? 16.801 2.246   -8.118  1   26.737  ? 87  ILE   B HD12 1 c 1 
ATOM   1079 H HD13 . ILE   A 1 75  ? 16.222 2.381   -9.595  1   27.49   ? 87  ILE   B HD13 1 c 1 
ATOM   1080 N N    . LYS   A 1 76  ? 20.229 6.513   -9.277  1   28.575  ? 88  LYS   B N    1 ? 1 
ATOM   1081 C CA   . LYS   A 1 76  ? 20.84  7.276   -8.2    1   32.22   ? 88  LYS   B CA   1 ? 1 
ATOM   1082 C C    . LYS   A 1 76  ? 20.591 6.57    -6.87   1   30.783  ? 88  LYS   B C    1 ? 1 
ATOM   1083 O O    . LYS   A 1 76  ? 21.538 6.47    -6.096  1   26.088  ? 88  LYS   B O    1 ? 1 
ATOM   1084 C CB   . LYS   A 1 76  ? 20.291 8.72    -8.082  1   32.734  ? 88  LYS   B CB   1 ? 1 
ATOM   1085 H H    . LYS   A 1 76  ? 19.644 6.947   -9.829  1   29.187  ? 88  LYS   B H    1 c 1 
ATOM   1086 H HA   . LYS   A 1 76  ? 21.817 7.315   -8.361  1   32.292  ? 88  LYS   B HA   1 c 1 
ATOM   1087 H HB2  . LYS   A 1 76  ? 21.093 9.343   -8.029  0   30      ? 88  LYS   B HB2  1 c 1 
ATOM   1088 H HB3  . LYS   A 1 76  ? 19.343 8.718   -8.081  0   30      ? 88  LYS   B HB3  1 c 1 
ATOM   1089 N N    . ALA   A 1 77  ? 19.379 6.014   -6.642  1   29.641  ? 89  ALA   B N    1 ? 1 
ATOM   1090 C CA   . ALA   A 1 77  ? 19.129 5.36    -5.352  1   28.507  ? 89  ALA   B CA   1 ? 1 
ATOM   1091 C C    . ALA   A 1 77  ? 20.044 4.159   -5.084  1   27.677  ? 89  ALA   B C    1 ? 1 
ATOM   1092 O O    . ALA   A 1 77  ? 20.379 3.875   -3.957  1   27.236  ? 89  ALA   B O    1 ? 1 
ATOM   1093 C CB   . ALA   A 1 77  ? 17.695 5.008   -5.207  1   27.169  ? 89  ALA   B CB   1 ? 1 
ATOM   1094 H H    . ALA   A 1 77  ? 18.72  6.043   -7.274  1   29.49   ? 89  ALA   B H    1 c 1 
ATOM   1095 H HA   . ALA   A 1 77  ? 19.339 6.036   -4.648  1   28.294  ? 89  ALA   B HA   1 c 1 
ATOM   1096 H HB1  . ALA   A 1 77  ? 17.161 5.818   -5.161  1   27.307  ? 89  ALA   B HB1  1 c 1 
ATOM   1097 H HB2  . ALA   A 1 77  ? 17.411 4.48    -5.972  1   27.472  ? 89  ALA   B HB2  1 c 1 
ATOM   1098 H HB3  . ALA   A 1 77  ? 17.565 4.491   -4.394  1   27.176  ? 89  ALA   B HB3  1 c 1 
ATOM   1099 N N    . TRP   A 1 78  ? 20.535 3.448   -6.097  1   28.305  ? 90  TRP   B N    1 ? 1 
ATOM   1100 C CA   . TRP   A 1 78  ? 21.414 2.307   -5.873  1   24.728  ? 90  TRP   B CA   1 ? 1 
ATOM   1101 C C    . TRP   A 1 78  ? 22.796 2.814   -5.555  1   28.511  ? 90  TRP   B C    1 ? 1 
ATOM   1102 O O    . TRP   A 1 78  ? 23.502 2.218   -4.731  1   29.608  ? 90  TRP   B O    1 ? 1 
ATOM   1103 C CB   . TRP   A 1 78  ? 21.436 1.411   -7.107  1   26.521  ? 90  TRP   B CB   1 ? 1 
ATOM   1104 C CG   . TRP   A 1 78  ? 20.399 0.314   -7.061  1   29.001  ? 90  TRP   B CG   1 ? 1 
ATOM   1105 C CD1  . TRP   A 1 78  ? 19.07  0.319   -6.719  1   32.177  ? 90  TRP   B CD1  1 ? 1 
ATOM   1106 C CD2  . TRP   A 1 78  ? 20.73  -1.075  -7.325  1   29.321  ? 90  TRP   B CD2  1 ? 1 
ATOM   1107 N NE1  . TRP   A 1 78  ? 18.539 -0.952  -6.816  1   30.286  ? 90  TRP   B NE1  1 ? 1 
ATOM   1108 C CE2  . TRP   A 1 78  ? 19.538 -1.835  -7.147  1   29.822  ? 90  TRP   B CE2  1 ? 1 
ATOM   1109 C CE3  . TRP   A 1 78  ? 21.916 -1.734  -7.627  1   31.94   ? 90  TRP   B CE3  1 ? 1 
ATOM   1110 C CZ2  . TRP   A 1 78  ? 19.495 -3.224  -7.297  1   27.862  ? 90  TRP   B CZ2  1 ? 1 
ATOM   1111 C CZ3  . TRP   A 1 78  ? 21.886 -3.118  -7.734  1   32.072  ? 90  TRP   B CZ3  1 ? 1 
ATOM   1112 C CH2  . TRP   A 1 78  ? 20.68  -3.851  -7.575  1   28.689  ? 90  TRP   B CH2  1 ? 1 
ATOM   1113 H H    . TRP   A 1 78  ? 20.317 3.677   -6.954  1   27.425  ? 90  TRP   B H    1 c 1 
ATOM   1114 H HA   . TRP   A 1 78  ? 21.073 1.781   -5.099  1   25.941  ? 90  TRP   B HA   1 c 1 
ATOM   1115 H HB2  . TRP   A 1 78  ? 21.282 1.964   -7.902  1   26.995  ? 90  TRP   B HB2  1 c 1 
ATOM   1116 H HB3  . TRP   A 1 78  ? 22.326 1.006   -7.185  1   27.741  ? 90  TRP   B HB3  1 c 1 
ATOM   1117 H HD1  . TRP   A 1 78  ? 18.562 1.094   -6.535  1   30.006  ? 90  TRP   B HD1  1 c 1 
ATOM   1118 H HE1  . TRP   A 1 78  ? 17.713 -1.161  -6.651  1   30.225  ? 90  TRP   B HE1  1 c 1 
ATOM   1119 H HE3  . TRP   A 1 78  ? 22.722 -1.257  -7.726  1   31.722  ? 90  TRP   B HE3  1 c 1 
ATOM   1120 H HZ2  . TRP   A 1 78  ? 18.698 -3.709  -7.167  1   28.618  ? 90  TRP   B HZ2  1 c 1 
ATOM   1121 H HZ3  . TRP   A 1 78  ? 22.675 -3.577  -7.97   1   32.588  ? 90  TRP   B HZ3  1 c 1 
ATOM   1122 H HH2  . TRP   A 1 78  ? 20.689 -4.785  -7.693  1   30.531  ? 90  TRP   B HH2  1 c 1 
ATOM   1123 N N    . ASP   A 1 79  ? 23.21  3.888   -6.282  1   27.501  ? 91  ASP   B N    1 ? 1 
ATOM   1124 C CA   . ASP   A 1 79  ? 24.48  4.489   -6.032  1   31.556  ? 91  ASP   B CA   1 ? 1 
ATOM   1125 C C    . ASP   A 1 79  ? 24.555 4.947   -4.586  1   29.984  ? 91  ASP   B C    1 ? 1 
ATOM   1126 O O    . ASP   A 1 79  ? 25.544 4.669   -3.919  1   30.246  ? 91  ASP   B O    1 ? 1 
ATOM   1127 C CB   . ASP   A 1 79  ? 24.885 5.568   -7.019  1   34.237  ? 91  ASP   B CB   1 ? 1 
ATOM   1128 C CG   . ASP   A 1 79  ? 25.472 5.073   -8.326  1   33.856  ? 91  ASP   B CG   1 ? 1 
ATOM   1129 O OD1  . ASP   A 1 79  ? 25.982 3.92    -8.379  1   35.65   ? 91  ASP   B OD1  1 ? 1 
ATOM   1130 O OD2  . ASP   A 1 79  ? 25.476 5.879   -9.216  1   37.446  ? 91  ASP   B OD2  1 ? 1 
ATOM   1131 H H    . ASP   A 1 79  ? 22.68  4.227   -6.945  1   28.283  ? 91  ASP   B H    1 c 1 
ATOM   1132 H HA   . ASP   A 1 79  ? 25.157 3.783   -6.14   1   31.813  ? 91  ASP   B HA   1 c 1 
ATOM   1133 H HB2  . ASP   A 1 79  ? 24.096 6.112   -7.226  1   32.791  ? 91  ASP   B HB2  1 c 1 
ATOM   1134 H HB3  . ASP   A 1 79  ? 25.547 6.152   -6.594  1   34.273  ? 91  ASP   B HB3  1 c 1 
ATOM   1135 N N    . ILE   A 1 80  ? 23.483 5.56    -4.111  1   26.132  ? 92  ILE   B N    1 ? 1 
ATOM   1136 C CA   . ILE   A 1 80  ? 23.404 6.009   -2.73   1   25.653  ? 92  ILE   B CA   1 ? 1 
ATOM   1137 C C    . ILE   A 1 80  ? 23.261 4.848   -1.73   1   27.168  ? 92  ILE   B C    1 ? 1 
ATOM   1138 O O    . ILE   A 1 80  ? 23.946 4.83    -0.688  1   31.289  ? 92  ILE   B O    1 ? 1 
ATOM   1139 C CB   . ILE   A 1 80  ? 22.217 6.963   -2.568  1   25.411  ? 92  ILE   B CB   1 ? 1 
ATOM   1140 C CG1  . ILE   A 1 80  ? 22.53  8.306   -3.256  1   28.458  ? 92  ILE   B CG1  1 ? 1 
ATOM   1141 C CG2  . ILE   A 1 80  ? 21.901 7.312   -1.1    1   27.644  ? 92  ILE   B CG2  1 ? 1 
ATOM   1142 C CD1  . ILE   A 1 80  ? 21.246 9.107   -3.552  1   33.678  ? 92  ILE   B CD1  1 ? 1 
ATOM   1143 H H    . ILE   A 1 80  ? 22.772 5.714   -4.664  1   26.121  ? 92  ILE   B H    1 c 1 
ATOM   1144 H HA   . ILE   A 1 80  ? 24.223 6.5     -2.519  1   27.209  ? 92  ILE   B HA   1 c 1 
ATOM   1145 H HB   . ILE   A 1 80  ? 21.425 6.566   -2.984  1   25.334  ? 92  ILE   B HB   1 c 1 
ATOM   1146 H HG12 . ILE   A 1 80  ? 23.115 8.837   -2.677  1   29.966  ? 92  ILE   B HG12 1 c 1 
ATOM   1147 H HG13 . ILE   A 1 80  ? 23.004 8.136   -4.096  1   29.549  ? 92  ILE   B HG13 1 c 1 
ATOM   1148 H HG21 . ILE   A 1 80  ? 21.31  8.082   -1.064  1   26.895  ? 92  ILE   B HG21 1 c 1 
ATOM   1149 H HG22 . ILE   A 1 80  ? 22.726 7.518   -0.629  1   27.873  ? 92  ILE   B HG22 1 c 1 
ATOM   1150 H HG23 . ILE   A 1 80  ? 21.466 6.557   -0.67   1   26.449  ? 92  ILE   B HG23 1 c 1 
ATOM   1151 H HD11 . ILE   A 1 80  ? 20.585 8.523   -3.97   1   31.011  ? 92  ILE   B HD11 1 c 1 
ATOM   1152 H HD12 . ILE   A 1 80  ? 21.457 9.841   -4.16   1   32.539  ? 92  ILE   B HD12 1 c 1 
ATOM   1153 H HD13 . ILE   A 1 80  ? 20.88  9.469   -2.724  1   31.74   ? 92  ILE   B HD13 1 c 1 
ATOM   1154 N N    . GLY   A 1 81  ? 22.357 3.93    -2.031  1   24.552  ? 93  GLY   B N    1 ? 1 
ATOM   1155 C CA   . GLY   A 1 81  ? 22.051 2.862   -1.069  1   28.635  ? 93  GLY   B CA   1 ? 1 
ATOM   1156 C C    . GLY   A 1 81  ? 23.11  1.789   -0.951  1   25.786  ? 93  GLY   B C    1 ? 1 
ATOM   1157 O O    . GLY   A 1 81  ? 23.445 1.38    0.162   1   26.76   ? 93  GLY   B O    1 ? 1 
ATOM   1158 H H    . GLY   A 1 81  ? 21.916 3.955   -2.832  1   25.432  ? 93  GLY   B H    1 c 1 
ATOM   1159 H HA2  . GLY   A 1 81  ? 21.911 3.27    -0.183  1   26.74   ? 93  GLY   B HA2  1 c 1 
ATOM   1160 H HA3  . GLY   A 1 81  ? 21.201 2.44    -1.335  1   26.083  ? 93  GLY   B HA3  1 c 1 
ATOM   1161 N N    . VAL   A 1 82  ? 23.613 1.271   -2.09   1   30.167  ? 94  VAL   B N    1 ? 1 
ATOM   1162 C CA   . VAL   A 1 82  ? 24.653 0.29    -2.028  1   29.722  ? 94  VAL   B CA   1 ? 1 
ATOM   1163 C C    . VAL   A 1 82  ? 25.934 0.832   -1.374  1   36.487  ? 94  VAL   B C    1 ? 1 
ATOM   1164 O O    . VAL   A 1 82  ? 26.599 0.044   -0.727  1   35.588  ? 94  VAL   B O    1 ? 1 
ATOM   1165 C CB   . VAL   A 1 82  ? 24.939 -0.355  -3.405  1   32.272  ? 94  VAL   B CB   1 ? 1 
ATOM   1166 C CG1  . VAL   A 1 82  ? 26.052 -1.354  -3.318  1   36.314  ? 94  VAL   B CG1  1 ? 1 
ATOM   1167 C CG2  . VAL   A 1 82  ? 23.641 -0.945  -3.996  1   26.573  ? 94  VAL   B CG2  1 ? 1 
ATOM   1168 H H    . VAL   A 1 82  ? 23.302 1.551   -2.902  1   28.321  ? 94  VAL   B H    1 c 1 
ATOM   1169 H HA   . VAL   A 1 82  ? 24.325 -0.426  -1.449  1   31.38   ? 94  VAL   B HA   1 c 1 
ATOM   1170 H HB   . VAL   A 1 82  ? 25.238 0.367   -4.005  1   31.43   ? 94  VAL   B HB   1 c 1 
ATOM   1171 H HG11 . VAL   A 1 82  ? 25.974 -1.857  -2.49   1   35.802  ? 94  VAL   B HG11 1 c 1 
ATOM   1172 H HG12 . VAL   A 1 82  ? 26.907 -0.893  -3.338  1   36.464  ? 94  VAL   B HG12 1 c 1 
ATOM   1173 H HG13 . VAL   A 1 82  ? 26     -1.965  -4.072  1   35.945  ? 94  VAL   B HG13 1 c 1 
ATOM   1174 H HG21 . VAL   A 1 82  ? 23.854 -1.479  -4.78   1   28.519  ? 94  VAL   B HG21 1 c 1 
ATOM   1175 H HG22 . VAL   A 1 82  ? 23.041 -0.225  -4.252  1   27.013  ? 94  VAL   B HG22 1 c 1 
ATOM   1176 H HG23 . VAL   A 1 82  ? 23.207 -1.506  -3.331  1   27.759  ? 94  VAL   B HG23 1 c 1 
ATOM   1177 N N    . ALA   A 1 83  ? 26.246 2.148   -1.48   1   31.208  ? 95  ALA   B N    1 ? 1 
ATOM   1178 C CA   . ALA   A 1 83  ? 27.366 2.771   -0.788  1   33.184  ? 95  ALA   B CA   1 ? 1 
ATOM   1179 C C    . ALA   A 1 83  ? 27.275 2.671   0.735   1   30.803  ? 95  ALA   B C    1 ? 1 
ATOM   1180 O O    . ALA   A 1 83  ? 28.325 2.678   1.379   1   35.9    ? 95  ALA   B O    1 ? 1 
ATOM   1181 C CB   . ALA   A 1 83  ? 27.567 4.26    -1.217  1   32.013  ? 95  ALA   B CB   1 ? 1 
ATOM   1182 H H    . ALA   A 1 83  ? 25.729 2.674   -2.019  1   31.69   ? 95  ALA   B H    1 c 1 
ATOM   1183 H HA   . ALA   A 1 83  ? 28.183 2.269   -1.059  1   33.549  ? 95  ALA   B HA   1 c 1 
ATOM   1184 H HB1  . ALA   A 1 83  ? 27.659 4.312   -2.183  1   32.481  ? 95  ALA   B HB1  1 c 1 
ATOM   1185 H HB2  . ALA   A 1 83  ? 26.799 4.787   -0.939  1   31.418  ? 95  ALA   B HB2  1 c 1 
ATOM   1186 H HB3  . ALA   A 1 83  ? 28.369 4.616   -0.799  1   33.766  ? 95  ALA   B HB3  1 c 1 
ATOM   1187 N N    . THR   A 1 84  ? 26.079 2.44    1.281   1   36.467  ? 96  THR   B N    1 ? 1 
ATOM   1188 C CA   . THR   A 1 84  ? 25.889 2.255   2.714   1   34.794  ? 96  THR   B CA   1 ? 1 
ATOM   1189 C C    . THR   A 1 84  ? 25.975 0.794   3.17    1   38.218  ? 96  THR   B C    1 ? 1 
ATOM   1190 O O    . THR   A 1 84  ? 25.902 0.565   4.376   1   33.82   ? 96  THR   B O    1 ? 1 
ATOM   1191 C CB   . THR   A 1 84  ? 24.53  2.775   3.189   1   33.729  ? 96  THR   B CB   1 ? 1 
ATOM   1192 O OG1  . THR   A 1 84  ? 23.47  1.893   2.778   1   32.018  ? 96  THR   B OG1  1 ? 1 
ATOM   1193 C CG2  . THR   A 1 84  ? 24.392 4.224   2.857   1   33.215  ? 96  THR   B CG2  1 ? 1 
ATOM   1194 H H    . THR   A 1 84  ? 25.342 2.414   0.741   1   32.978  ? 96  THR   B H    1 c 1 
ATOM   1195 H HA   . THR   A 1 84  ? 26.587 2.764   3.181   1   36.762  ? 96  THR   B HA   1 c 1 
ATOM   1196 H HB   . THR   A 1 84  ? 24.556 2.754   4.175   1   34.183  ? 96  THR   B HB   1 c 1 
ATOM   1197 H HG1  . THR   A 1 84  ? 23.485 1.833   1.936   0   30      ? 96  THR   B HG1  1 c 1 
ATOM   1198 H HG21 . THR   A 1 84  ? 23.612 4.588   3.308   1   32.728  ? 96  THR   B HG21 1 c 1 
ATOM   1199 H HG22 . THR   A 1 84  ? 24.288 4.329   1.896   1   32.678  ? 96  THR   B HG22 1 c 1 
ATOM   1200 H HG23 . THR   A 1 84  ? 25.186 4.702   3.15    1   34.356  ? 96  THR   B HG23 1 c 1 
ATOM   1201 N N    . MET   A 1 85  ? 26.061 -0.204  2.26    1   36.333  ? 97  MET   B N    1 ? 1 
ATOM   1202 C CA   . MET   A 1 85  ? 25.885 -1.623  2.597   1   35.239  ? 97  MET   B CA   1 ? 1 
ATOM   1203 C C    . MET   A 1 85  ? 27.203 -2.332  2.95    1   36.671  ? 97  MET   B C    1 ? 1 
ATOM   1204 O O    . MET   A 1 85  ? 28.208 -2.014  2.33    1   34.164  ? 97  MET   B O    1 ? 1 
ATOM   1205 C CB   . MET   A 1 85  ? 25.188 -2.352  1.436   1   32.592  ? 97  MET   B CB   1 ? 1 
ATOM   1206 C CG   . MET   A 1 85  ? 23.696 -1.89   1.25    1   29.694  ? 97  MET   B CG   1 ? 1 
ATOM   1207 S SD   . MET   A 1 85  ? 22.959 -2.88   -0.056  1   32.797  ? 97  MET   B SD   1 ? 1 
ATOM   1208 C CE   . MET   A 1 85  ? 22.762 -4.537  0.645   1   30.541  ? 97  MET   B CE   1 ? 1 
ATOM   1209 H H    . MET   A 1 85  ? 26.241 0.012   1.391   1   36.014  ? 97  MET   B H    1 c 1 
ATOM   1210 H HA   . MET   A 1 85  ? 25.298 -1.669  3.393   1   34.889  ? 97  MET   B HA   1 c 1 
ATOM   1211 H HB2  . MET   A 1 85  ? 25.685 -2.18   0.608   1   32.894  ? 97  MET   B HB2  1 c 1 
ATOM   1212 H HB3  . MET   A 1 85  ? 25.209 -3.317  1.609   1   33.605  ? 97  MET   B HB3  1 c 1 
ATOM   1213 H HG2  . MET   A 1 85  ? 23.197 -2.017  2.079   1   30.583  ? 97  MET   B HG2  1 c 1 
ATOM   1214 H HG3  . MET   A 1 85  ? 23.663 -0.947  1.005   1   29.815  ? 97  MET   B HG3  1 c 1 
ATOM   1215 H HE1  . MET   A 1 85  ? 22.515 -5.161  -0.063  1   31.675  ? 97  MET   B HE1  1 c 1 
ATOM   1216 H HE2  . MET   A 1 85  ? 23.603 -4.823  1.047   1   32.554  ? 97  MET   B HE2  1 c 1 
ATOM   1217 H HE3  . MET   A 1 85  ? 22.065 -4.522  1.326   1   31.199  ? 97  MET   B HE3  1 c 1 
ATOM   1218 N N    . LYS   A 1 86  ? 27.195 -3.28   3.907   1   37.35   ? 98  LYS   B N    1 ? 1 
ATOM   1219 C CA   . LYS   A 1 86  ? 28.394 -4.091  4.185   1   39.877  ? 98  LYS   B CA   1 ? 1 
ATOM   1220 C C    . LYS   A 1 86  ? 28.281 -5.387  3.359   1   39.04   ? 98  LYS   B C    1 ? 1 
ATOM   1221 O O    . LYS   A 1 86  ? 27.195 -5.837  2.981   1   42.228  ? 98  LYS   B O    1 ? 1 
ATOM   1222 C CB   . LYS   A 1 86  ? 28.642 -4.299  5.699   1   38.495  ? 98  LYS   B CB   1 ? 1 
ATOM   1223 H H    . LYS   A 1 86  ? 26.435 -3.428  4.393   1   37      ? 98  LYS   B H    1 c 1 
ATOM   1224 H HA   . LYS   A 1 86  ? 29.179 -3.592  3.844   1   39.533  ? 98  LYS   B HA   1 c 1 
ATOM   1225 H HB2  . LYS   A 1 86  ? 29.725 -4.584  5.687   0   30      ? 98  LYS   B HB2  1 c 1 
ATOM   1226 H HB3  . LYS   A 1 86  ? 27.909 -4.696  6.068   0   30      ? 98  LYS   B HB3  1 c 1 
ATOM   1227 N N    . LYS   A 1 87  ? 29.392 -6.072  3.115   1   43.242  ? 99  LYS   B N    1 ? 1 
ATOM   1228 C CA   . LYS   A 1 87  ? 29.348 -7.359  2.42    1   43.86   ? 99  LYS   B CA   1 ? 1 
ATOM   1229 C C    . LYS   A 1 87  ? 28.502 -8.344  3.219   1   44.94   ? 99  LYS   B C    1 ? 1 
ATOM   1230 O O    . LYS   A 1 87  ? 28.684 -8.452  4.435   1   44.686  ? 99  LYS   B O    1 ? 1 
ATOM   1231 C CB   . LYS   A 1 87  ? 30.748 -7.95   2.216   1   50.199  ? 99  LYS   B CB   1 ? 1 
ATOM   1232 C CG   . LYS   A 1 87  ? 30.836 -9.189  1.294   1   50.538  ? 99  LYS   B CG   1 ? 1 
ATOM   1233 C CD   . LYS   A 1 87  ? 32.245 -9.68   0.972   1   58.724  ? 99  LYS   B CD   1 ? 1 
ATOM   1234 C CE   . LYS   A 1 87  ? 32.222 -11.159 0.683   1   58.121  ? 99  LYS   B CE   1 ? 1 
ATOM   1235 N NZ   . LYS   A 1 87  ? 33.564 -11.711 0.498   1   65.718  ? 99  LYS   B NZ   1 ? 1 
ATOM   1236 H H    . LYS   A 1 87  ? 30.199 -5.739  3.385   1   43.76   ? 99  LYS   B H    1 c 1 
ATOM   1237 H HA   . LYS   A 1 87  ? 28.928 -7.219  1.534   1   43.404  ? 99  LYS   B HA   1 c 1 
ATOM   1238 H HB2  . LYS   A 1 87  ? 31.326 -7.251  1.843   1   49.059  ? 99  LYS   B HB2  1 c 1 
ATOM   1239 H HB3  . LYS   A 1 87  ? 31.112 -8.195  3.093   1   50.527  ? 99  LYS   B HB3  1 c 1 
ATOM   1240 H HG2  . LYS   A 1 87  ? 30.337 -9.921  1.718   1   52.352  ? 99  LYS   B HG2  1 c 1 
ATOM   1241 H HG3  . LYS   A 1 87  ? 30.379 -8.976  0.452   1   50.541  ? 99  LYS   B HG3  1 c 1 
ATOM   1242 H HD2  . LYS   A 1 87  ? 32.591 -9.2    0.188   1   56.537  ? 99  LYS   B HD2  1 c 1 
ATOM   1243 H HD3  . LYS   A 1 87  ? 32.838 -9.506  1.736   1   58.021  ? 99  LYS   B HD3  1 c 1 
ATOM   1244 H HE2  . LYS   A 1 87  ? 31.79  -11.628 1.42    1   59.983  ? 99  LYS   B HE2  1 c 1 
ATOM   1245 H HE3  . LYS   A 1 87  ? 31.704 -11.325 -0.123  1   58.819  ? 99  LYS   B HE3  1 c 1 
ATOM   1246 H HZ1  . LYS   A 1 87  ? 34.013 -11.694 1.284   1   65.527  ? 99  LYS   B HZ1  1 c 1 
ATOM   1247 H HZ2  . LYS   A 1 87  ? 34.016 -11.219 -0.114  1   64.273  ? 99  LYS   B HZ2  1 c 1 
ATOM   1248 H HZ3  . LYS   A 1 87  ? 33.505 -12.567 0.206   1   65.666  ? 99  LYS   B HZ3  1 c 1 
ATOM   1249 N N    . GLY   A 1 88  ? 27.621 -9.087  2.509   1   42.524  ? 100 GLY   B N    1 ? 1 
ATOM   1250 C CA   . GLY   A 1 88  ? 26.727 -10.072 3.123   1   43.676  ? 100 GLY   B CA   1 ? 1 
ATOM   1251 C C    . GLY   A 1 88  ? 25.402 -9.446  3.565   1   42.871  ? 100 GLY   B C    1 ? 1 
ATOM   1252 O O    . GLY   A 1 88  ? 24.506 -10.162 4.018   1   44.853  ? 100 GLY   B O    1 ? 1 
ATOM   1253 H H    . GLY   A 1 88  ? 27.58  -8.974  1.603   1   42.392  ? 100 GLY   B H    1 c 1 
ATOM   1254 H HA2  . GLY   A 1 88  ? 26.549 -10.791 2.474   1   44.511  ? 100 GLY   B HA2  1 c 1 
ATOM   1255 H HA3  . GLY   A 1 88  ? 27.176 -10.474 3.904   1   45.581  ? 100 GLY   B HA3  1 c 1 
ATOM   1256 N N    . GLU   A 1 89  ? 25.278 -8.112  3.448   1   40.096  ? 101 GLU   B N    1 ? 1 
ATOM   1257 C CA   . GLU   A 1 89  ? 24.084 -7.417  3.96    1   40.745  ? 101 GLU   B CA   1 ? 1 
ATOM   1258 C C    . GLU   A 1 89  ? 22.908 -7.651  3.027   1   38.989  ? 101 GLU   B C    1 ? 1 
ATOM   1259 O O    . GLU   A 1 89  ? 23.079 -7.578  1.786   1   43.106  ? 101 GLU   B O    1 ? 1 
ATOM   1260 C CB   . GLU   A 1 89  ? 24.398 -5.94   4.153   1   38.982  ? 101 GLU   B CB   1 ? 1 
ATOM   1261 C CG   . GLU   A 1 89  ? 23.242 -5.115  4.711   1   41.294  ? 101 GLU   B CG   1 ? 1 
ATOM   1262 C CD   . GLU   A 1 89  ? 23.578 -3.625  4.792   1   37.71   ? 101 GLU   B CD   1 ? 1 
ATOM   1263 O OE1  . GLU   A 1 89  ? 24.674 -3.366  5.357   1   34.688  ? 101 GLU   B OE1  1 ? 1 
ATOM   1264 O OE2  . GLU   A 1 89  ? 22.713 -2.738  4.396   1   33.172  ? 101 GLU   B OE2  1 ? 1 
ATOM   1265 H H    . GLU   A 1 89  ? 25.931 -7.623  3.036   1   40.477  ? 101 GLU   B H    1 c 1 
ATOM   1266 H HA   . GLU   A 1 89  ? 23.864 -7.801  4.845   1   41.09   ? 101 GLU   B HA   1 c 1 
ATOM   1267 H HB2  . GLU   A 1 89  ? 25.166 -5.859  4.757   1   40.939  ? 101 GLU   B HB2  1 c 1 
ATOM   1268 H HB3  . GLU   A 1 89  ? 24.658 -5.559  3.289   1   39.109  ? 101 GLU   B HB3  1 c 1 
ATOM   1269 H HG2  . GLU   A 1 89  ? 22.454 -5.229  4.139   1   38.917  ? 101 GLU   B HG2  1 c 1 
ATOM   1270 H HG3  . GLU   A 1 89  ? 23.017 -5.438  5.609   1   40.732  ? 101 GLU   B HG3  1 c 1 
ATOM   1271 N N    . ILE   A 1 90  ? 21.713 -7.809  3.619   1   37.046  ? 102 ILE   B N    1 ? 1 
ATOM   1272 C CA   . ILE   A 1 90  ? 20.489 -7.726  2.818   1   35.497  ? 102 ILE   B CA   1 ? 1 
ATOM   1273 C C    . ILE   A 1 90  ? 19.739 -6.489  3.295   1   38.531  ? 102 ILE   B C    1 ? 1 
ATOM   1274 O O    . ILE   A 1 90  ? 19.487 -6.342  4.514   1   39.273  ? 102 ILE   B O    1 ? 1 
ATOM   1275 C CB   . ILE   A 1 90  ? 19.603 -8.969  2.945   1   38.098  ? 102 ILE   B CB   1 ? 1 
ATOM   1276 C CG1  . ILE   A 1 90  ? 20.299 -10.292 2.568   1   41.794  ? 102 ILE   B CG1  1 ? 1 
ATOM   1277 C CG2  . ILE   A 1 90  ? 18.281 -8.822  2.193   1   38.777  ? 102 ILE   B CG2  1 ? 1 
ATOM   1278 C CD1  . ILE   A 1 90  ? 19.374 -11.494 2.763   1   38.097  ? 102 ILE   B CD1  1 ? 1 
ATOM   1279 H H    . ILE   A 1 90  ? 21.654 -7.969  4.517   1   38.25   ? 102 ILE   B H    1 c 1 
ATOM   1280 H HA   . ILE   A 1 90  ? 20.731 -7.612  1.883   1   35.957  ? 102 ILE   B HA   1 c 1 
ATOM   1281 H HB   . ILE   A 1 90  ? 19.373 -9.043  3.893   1   39.189  ? 102 ILE   B HB   1 c 1 
ATOM   1282 H HG12 . ILE   A 1 90  ? 20.581 -10.252 1.632   1   39.532  ? 102 ILE   B HG12 1 c 1 
ATOM   1283 H HG13 . ILE   A 1 90  ? 21.096 -10.406 3.124   1   40.853  ? 102 ILE   B HG13 1 c 1 
ATOM   1284 H HG21 . ILE   A 1 90  ? 17.65  -9.49   2.508   1   39.475  ? 102 ILE   B HG21 1 c 1 
ATOM   1285 H HG22 . ILE   A 1 90  ? 18.433 -8.946  1.241   1   38.025  ? 102 ILE   B HG22 1 c 1 
ATOM   1286 H HG23 . ILE   A 1 90  ? 17.911 -7.937  2.346   1   36.964  ? 102 ILE   B HG23 1 c 1 
ATOM   1287 H HD11 . ILE   A 1 90  ? 18.889 -11.393 3.603   1   39.914  ? 102 ILE   B HD11 1 c 1 
ATOM   1288 H HD12 . ILE   A 1 90  ? 19.906 -12.311 2.794   1   41.4    ? 102 ILE   B HD12 1 c 1 
ATOM   1289 H HD13 . ILE   A 1 90  ? 18.739 -11.55  2.025   1   39.251  ? 102 ILE   B HD13 1 c 1 
ATOM   1290 N N    . ALA   A 1 91  ? 19.413 -5.617  2.322   1   29.559  ? 103 ALA   B N    1 ? 1 
ATOM   1291 C CA   . ALA   A 1 91  ? 18.689 -4.406  2.644   1   34.687  ? 103 ALA   B CA   1 ? 1 
ATOM   1292 C C    . ALA   A 1 91  ? 17.451 -4.271  1.742   1   28.837  ? 103 ALA   B C    1 ? 1 
ATOM   1293 O O    . ALA   A 1 91  ? 17.397 -4.839  0.609   1   32.826  ? 103 ALA   B O    1 ? 1 
ATOM   1294 C CB   . ALA   A 1 91  ? 19.644 -3.23   2.504   1   32.146  ? 103 ALA   B CB   1 ? 1 
ATOM   1295 H H    . ALA   A 1 91  ? 19.645 -5.782  1.453   1   32.319  ? 103 ALA   B H    1 c 1 
ATOM   1296 H HA   . ALA   A 1 91  ? 18.382 -4.466  3.589   1   32.606  ? 103 ALA   B HA   1 c 1 
ATOM   1297 H HB1  . ALA   A 1 91  ? 20.393 -3.343  3.112   1   33.357  ? 103 ALA   B HB1  1 c 1 
ATOM   1298 H HB2  . ALA   A 1 91  ? 19.975 -3.184  1.591   1   32.222  ? 103 ALA   B HB2  1 c 1 
ATOM   1299 H HB3  . ALA   A 1 91  ? 19.178 -2.404  2.718   1   31.836  ? 103 ALA   B HB3  1 c 1 
ATOM   1300 N N    . HIS   A 1 92  ? 16.432 -3.638  2.305   1   25.803  ? 104 HIS   B N    1 ? 1 
ATOM   1301 C CA   . HIS   A 1 92  ? 15.274 -3.166  1.578   1   28.195  ? 104 HIS   B CA   1 ? 1 
ATOM   1302 C C    . HIS   A 1 92  ? 15.375 -1.676  1.286   1   28.681  ? 104 HIS   B C    1 ? 1 
ATOM   1303 O O    . HIS   A 1 92  ? 15.643 -0.924  2.171   1   27.328  ? 104 HIS   B O    1 ? 1 
ATOM   1304 C CB   . HIS   A 1 92  ? 13.975 -3.464  2.314   1   28.999  ? 104 HIS   B CB   1 ? 1 
ATOM   1305 C CG   . HIS   A 1 92  ? 13.597 -4.894  2.29    1   34.827  ? 104 HIS   B CG   1 ? 1 
ATOM   1306 N ND1  . HIS   A 1 92  ? 12.524 -5.376  2.979   1   40.52   ? 104 HIS   B ND1  1 ? 1 
ATOM   1307 C CD2  . HIS   A 1 92  ? 14.173 -5.95   1.677   1   36.742  ? 104 HIS   B CD2  1 ? 1 
ATOM   1308 C CE1  . HIS   A 1 92  ? 12.482 -6.693  2.806   1   42.405  ? 104 HIS   B CE1  1 ? 1 
ATOM   1309 N NE2  . HIS   A 1 92  ? 13.44  -7.047  1.96    1   37.074  ? 104 HIS   B NE2  1 ? 1 
ATOM   1310 H H    . HIS   A 1 92  ? 16.459 -3.49   3.207   1   27.54   ? 104 HIS   B H    1 c 1 
ATOM   1311 H HA   . HIS   A 1 92  ? 15.251 -3.644  0.716   1   28.077  ? 104 HIS   B HA   1 c 1 
ATOM   1312 H HB2  . HIS   A 1 92  ? 14.068 -3.175  3.247   1   30.183  ? 104 HIS   B HB2  1 c 1 
ATOM   1313 H HB3  . HIS   A 1 92  ? 13.253 -2.938  1.906   1   29.475  ? 104 HIS   B HB3  1 c 1 
ATOM   1314 H HD1  . HIS   A 1 92  ? 11.969 -4.893  3.486   0   30      ? 104 HIS   B HD1  1 c 1 
ATOM   1315 H HD2  . HIS   A 1 92  ? 14.919 -5.93   1.11    1   35.492  ? 104 HIS   B HD2  1 c 1 
ATOM   1316 H HE1  . HIS   A 1 92  ? 11.816 -7.263  3.153   1   42.595  ? 104 HIS   B HE1  1 c 1 
ATOM   1317 H HE2  . HIS   A 1 92  ? 13.58  -7.828  1.637   0   30      ? 104 HIS   B HE2  1 c 1 
ATOM   1318 N N    . LEU   A 1 93  ? 15.14  -1.264  0.028   1   26.195  ? 105 LEU   B N    1 ? 1 
ATOM   1319 C CA   . LEU   A 1 93  ? 15.088 0.136   -0.327  1   28.41   ? 105 LEU   B CA   1 ? 1 
ATOM   1320 C C    . LEU   A 1 93  ? 13.701 0.438   -0.877  1   26.319  ? 105 LEU   B C    1 ? 1 
ATOM   1321 O O    . LEU   A 1 93  ? 13.189 -0.278  -1.78   1   29.641  ? 105 LEU   B O    1 ? 1 
ATOM   1322 C CB   . LEU   A 1 93  ? 16.121 0.54    -1.402  1   26.484  ? 105 LEU   B CB   1 ? 1 
ATOM   1323 C CG   . LEU   A 1 93  ? 17.613 0.328   -1.13   1   26.415  ? 105 LEU   B CG   1 ? 1 
ATOM   1324 C CD1  . LEU   A 1 93  ? 18.588 0.764   -2.211  1   29.558  ? 105 LEU   B CD1  1 ? 1 
ATOM   1325 C CD2  . LEU   A 1 93  ? 17.978 1.035   0.12    1   24.93   ? 105 LEU   B CD2  1 ? 1 
ATOM   1326 H H    . LEU   A 1 93  ? 15.01  -1.887  -0.628  1   27.595  ? 105 LEU   B H    1 c 1 
ATOM   1327 H HA   . LEU   A 1 93  ? 15.236 0.674   0.487   1   27.018  ? 105 LEU   B HA   1 c 1 
ATOM   1328 H HB2  . LEU   A 1 93  ? 15.895 0.057   -2.23   1   26.854  ? 105 LEU   B HB2  1 c 1 
ATOM   1329 H HB3  . LEU   A 1 93  ? 15.985 1.494   -1.604  1   26.235  ? 105 LEU   B HB3  1 c 1 
ATOM   1330 H HG   . LEU   A 1 93  ? 17.757 -0.642  -0.976  1   27.353  ? 105 LEU   B HG   1 c 1 
ATOM   1331 H HD11 . LEU   A 1 93  ? 18.324 0.376   -3.062  1   28.604  ? 105 LEU   B HD11 1 c 1 
ATOM   1332 H HD12 . LEU   A 1 93  ? 19.483 0.463   -1.982  1   29.01   ? 105 LEU   B HD12 1 c 1 
ATOM   1333 H HD13 . LEU   A 1 93  ? 18.582 1.734   -2.282  1   28.14   ? 105 LEU   B HD13 1 c 1 
ATOM   1334 H HD21 . LEU   A 1 93  ? 17.566 0.59    0.879   1   25.806  ? 105 LEU   B HD21 1 c 1 
ATOM   1335 H HD22 . LEU   A 1 93  ? 17.665 1.955   0.077   1   24.982  ? 105 LEU   B HD22 1 c 1 
ATOM   1336 H HD23 . LEU   A 1 93  ? 18.944 1.028   0.23    1   25.764  ? 105 LEU   B HD23 1 c 1 
ATOM   1337 N N    . LEU   A 1 94  ? 13.208 1.628   -0.525  1   26.687  ? 106 LEU   B N    1 ? 1 
ATOM   1338 C CA   . LEU   A 1 94  ? 12.035 2.187   -1.204  1   26.104  ? 106 LEU   B CA   1 ? 1 
ATOM   1339 C C    . LEU   A 1 94  ? 12.396 3.556   -1.739  1   25.111  ? 106 LEU   B C    1 ? 1 
ATOM   1340 O O    . LEU   A 1 94  ? 12.91  4.388   -0.995  1   26.509  ? 106 LEU   B O    1 ? 1 
ATOM   1341 C CB   . LEU   A 1 94  ? 10.865 2.276   -0.236  1   28.104  ? 106 LEU   B CB   1 ? 1 
ATOM   1342 C CG   . LEU   A 1 94  ? 9.537  2.683   -0.841  1   27.497  ? 106 LEU   B CG   1 ? 1 
ATOM   1343 C CD1  . LEU   A 1 94  ? 9.045  1.575   -1.708  1   30.442  ? 106 LEU   B CD1  1 ? 1 
ATOM   1344 C CD2  . LEU   A 1 94  ? 8.586  2.986   0.225   1   26.596  ? 106 LEU   B CD2  1 ? 1 
ATOM   1345 H H    . LEU   A 1 94  ? 13.6   2.105   0.149   1   26.263  ? 106 LEU   B H    1 c 1 
ATOM   1346 H HA   . LEU   A 1 94  ? 11.794 1.597   -1.96   1   26.608  ? 106 LEU   B HA   1 c 1 
ATOM   1347 H HB2  . LEU   A 1 94  ? 10.755 1.397   0.196   1   28.162  ? 106 LEU   B HB2  1 c 1 
ATOM   1348 H HB3  . LEU   A 1 94  ? 11.098 2.924   0.468   1   27.39   ? 106 LEU   B HB3  1 c 1 
ATOM   1349 H HG   . LEU   A 1 94  ? 9.67   3.494   -1.396  1   27.255  ? 106 LEU   B HG   1 c 1 
ATOM   1350 H HD11 . LEU   A 1 94  ? 9.609  1.501   -2.494  1   29.167  ? 106 LEU   B HD11 1 c 1 
ATOM   1351 H HD12 . LEU   A 1 94  ? 8.132  1.76    -1.985  1   30.394  ? 106 LEU   B HD12 1 c 1 
ATOM   1352 H HD13 . LEU   A 1 94  ? 9.068  0.739   -1.213  1   30.25   ? 106 LEU   B HD13 1 c 1 
ATOM   1353 H HD21 . LEU   A 1 94  ? 8.907  3.745   0.742   1   26.879  ? 106 LEU   B HD21 1 c 1 
ATOM   1354 H HD22 . LEU   A 1 94  ? 8.495  2.214   0.809   1   27.805  ? 106 LEU   B HD22 1 c 1 
ATOM   1355 H HD23 . LEU   A 1 94  ? 7.721  3.203   -0.161  1   27.818  ? 106 LEU   B HD23 1 c 1 
ATOM   1356 N N    . ILE   A 1 95  ? 12.114 3.769   -3.035  1   23.342  ? 107 ILE   B N    1 ? 1 
ATOM   1357 C CA   . ILE   A 1 95  ? 12.711 4.839   -3.816  1   24.634  ? 107 ILE   B CA   1 ? 1 
ATOM   1358 C C    . ILE   A 1 95  ? 11.696 5.693   -4.53   1   26.262  ? 107 ILE   B C    1 ? 1 
ATOM   1359 O O    . ILE   A 1 95  ? 10.932 5.177   -5.322  1   28.839  ? 107 ILE   B O    1 ? 1 
ATOM   1360 C CB   . ILE   A 1 95  ? 13.65  4.186   -4.833  1   24.531  ? 107 ILE   B CB   1 ? 1 
ATOM   1361 C CG1  . ILE   A 1 95  ? 14.675 3.235   -4.13   1   26.74   ? 107 ILE   B CG1  1 ? 1 
ATOM   1362 C CG2  . ILE   A 1 95  ? 14.284 5.282   -5.673  1   25.062  ? 107 ILE   B CG2  1 ? 1 
ATOM   1363 C CD1  . ILE   A 1 95  ? 15.382 2.222   -5.037  1   27.543  ? 107 ILE   B CD1  1 ? 1 
ATOM   1364 H H    . ILE   A 1 95  ? 11.513 3.218   -3.448  1   24.539  ? 107 ILE   B H    1 c 1 
ATOM   1365 H HA   . ILE   A 1 95  ? 13.24  5.402   -3.223  1   24.354  ? 107 ILE   B HA   1 c 1 
ATOM   1366 H HB   . ILE   A 1 95  ? 13.102 3.636   -5.427  1   25.389  ? 107 ILE   B HB   1 c 1 
ATOM   1367 H HG12 . ILE   A 1 95  ? 15.358 3.786   -3.695  1   26.119  ? 107 ILE   B HG12 1 c 1 
ATOM   1368 H HG13 . ILE   A 1 95  ? 14.21  2.738   -3.428  1   26.414  ? 107 ILE   B HG13 1 c 1 
ATOM   1369 H HG21 . ILE   A 1 95  ? 15.104 4.95    -6.073  1   24.973  ? 107 ILE   B HG21 1 c 1 
ATOM   1370 H HG22 . ILE   A 1 95  ? 14.487 6.05    -5.113  1   24.844  ? 107 ILE   B HG22 1 c 1 
ATOM   1371 H HG23 . ILE   A 1 95  ? 13.67  5.549   -6.378  1   25.247  ? 107 ILE   B HG23 1 c 1 
ATOM   1372 H HD11 . ILE   A 1 95  ? 14.717 1.735   -5.559  1   27.735  ? 107 ILE   B HD11 1 c 1 
ATOM   1373 H HD12 . ILE   A 1 95  ? 15.89  1.592   -4.491  1   27.519  ? 107 ILE   B HD12 1 c 1 
ATOM   1374 H HD13 . ILE   A 1 95  ? 15.989 2.689   -5.641  1   27.404  ? 107 ILE   B HD13 1 c 1 
ATOM   1375 N N    . LYS   A 1 96  ? 11.688 7.013   -4.242  1   24.872  ? 108 LYS   B N    1 ? 1 
ATOM   1376 C CA   . LYS   A 1 96  ? 10.797 7.948   -4.965  1   25.822  ? 108 LYS   B CA   1 ? 1 
ATOM   1377 C C    . LYS   A 1 96  ? 11.377 8.192   -6.354  1   22.892  ? 108 LYS   B C    1 ? 1 
ATOM   1378 O O    . LYS   A 1 96  ? 12.543 7.887   -6.634  1   26.224  ? 108 LYS   B O    1 ? 1 
ATOM   1379 C CB   . LYS   A 1 96  ? 10.778 9.307   -4.249  1   31.043  ? 108 LYS   B CB   1 ? 1 
ATOM   1380 C CG   . LYS   A 1 96  ? 9.993  9.331   -2.935  1   30.273  ? 108 LYS   B CG   1 ? 1 
ATOM   1381 C CD   . LYS   A 1 96  ? 9.879  10.747  -2.326  1   31.622  ? 108 LYS   B CD   1 ? 1 
ATOM   1382 C CE   . LYS   A 1 96  ? 9.178  10.626  -0.969  1   39.529  ? 108 LYS   B CE   1 ? 1 
ATOM   1383 N NZ   . LYS   A 1 96  ? 9.298  11.941  -0.324  1   44.098  ? 108 LYS   B NZ   1 ? 1 
ATOM   1384 H H    . LYS   A 1 96  ? 12.239 7.34    -3.59   1   25.119  ? 108 LYS   B H    1 c 1 
ATOM   1385 H HA   . LYS   A 1 96  ? 9.889  7.557   -5.03   1   26.438  ? 108 LYS   B HA   1 c 1 
ATOM   1386 H HB2  . LYS   A 1 96  ? 11.703 9.575   -4.062  1   29.28   ? 108 LYS   B HB2  1 c 1 
ATOM   1387 H HB3  . LYS   A 1 96  ? 10.392 9.977   -4.851  1   30.182  ? 108 LYS   B HB3  1 c 1 
ATOM   1388 H HG2  . LYS   A 1 96  ? 9.092  8.98    -3.101  1   31.156  ? 108 LYS   B HG2  1 c 1 
ATOM   1389 H HG3  . LYS   A 1 96  ? 10.437 8.738   -2.291  1   30.234  ? 108 LYS   B HG3  1 c 1 
ATOM   1390 H HD2  . LYS   A 1 96  ? 10.773 11.133  -2.203  1   32.823  ? 108 LYS   B HD2  1 c 1 
ATOM   1391 H HD3  . LYS   A 1 96  ? 9.353  11.326  -2.919  1   33.706  ? 108 LYS   B HD3  1 c 1 
ATOM   1392 H HE2  . LYS   A 1 96  ? 8.237  10.401  -1.087  1   39.065  ? 108 LYS   B HE2  1 c 1 
ATOM   1393 H HE3  . LYS   A 1 96  ? 9.605  9.947   -0.418  1   37.899  ? 108 LYS   B HE3  1 c 1 
ATOM   1394 H HZ1  . LYS   A 1 96  ? 8.953  12.583  -0.863  1   43.45   ? 108 LYS   B HZ1  1 c 1 
ATOM   1395 H HZ2  . LYS   A 1 96  ? 10.17  12.126  -0.16   1   42.44   ? 108 LYS   B HZ2  1 c 1 
ATOM   1396 H HZ3  . LYS   A 1 96  ? 8.844  11.938  0.46    1   43.453  ? 108 LYS   B HZ3  1 c 1 
ATOM   1397 N N    . PRO   A 1 97  ? 10.536 8.656   -7.318  1   27.62   ? 109 PRO   B N    1 ? 1 
ATOM   1398 C CA   . PRO   A 1 97  ? 10.917 8.692   -8.728  1   28.386  ? 109 PRO   B CA   1 ? 1 
ATOM   1399 C C    . PRO   A 1 97  ? 12.105 9.604   -8.972  1   25.471  ? 109 PRO   B C    1 ? 1 
ATOM   1400 O O    . PRO   A 1 97  ? 12.903 9.355   -9.862  1   30.729  ? 109 PRO   B O    1 ? 1 
ATOM   1401 C CB   . PRO   A 1 97  ? 9.618  9.096   -9.457  1   32.661  ? 109 PRO   B CB   1 ? 1 
ATOM   1402 C CG   . PRO   A 1 97  ? 8.572  9.528   -8.443  1   30.912  ? 109 PRO   B CG   1 ? 1 
ATOM   1403 C CD   . PRO   A 1 97  ? 9.096  8.906   -7.136  1   30.144  ? 109 PRO   B CD   1 ? 1 
ATOM   1404 H HA   . PRO   A 1 97  ? 11.159 7.771   -8.999  1   27.948  ? 109 PRO   B HA   1 c 1 
ATOM   1405 H HB2  . PRO   A 1 97  ? 9.798  9.832   -10.088 1   32.121  ? 109 PRO   B HB2  1 c 1 
ATOM   1406 H HB3  . PRO   A 1 97  ? 9.279  8.338   -9.987  1   31.758  ? 109 PRO   B HB3  1 c 1 
ATOM   1407 H HG2  . PRO   A 1 97  ? 8.523  10.504  -8.376  1   31.999  ? 109 PRO   B HG2  1 c 1 
ATOM   1408 H HG3  . PRO   A 1 97  ? 7.687  9.175   -8.672  1   32.171  ? 109 PRO   B HG3  1 c 1 
ATOM   1409 H HD2  . PRO   A 1 97  ? 8.944  9.519   -6.385  1   29.78   ? 109 PRO   B HD2  1 c 1 
ATOM   1410 H HD3  . PRO   A 1 97  ? 8.624  8.066   -6.945  1   29.64   ? 109 PRO   B HD3  1 c 1 
ATOM   1411 N N    . GLU   A 1 98  ? 12.29  10.615  -8.137  1   26.106  ? 110 GLU   B N    1 ? 1 
ATOM   1412 C CA   . GLU   A 1 98  ? 13.45  11.482  -8.341  1   30.673  ? 110 GLU   B CA   1 ? 1 
ATOM   1413 C C    . GLU   A 1 98  ? 14.822 10.778  -8.184  1   26.797  ? 110 GLU   B C    1 ? 1 
ATOM   1414 O O    . GLU   A 1 98  ? 15.82  11.31   -8.706  1   31.179  ? 110 GLU   B O    1 ? 1 
ATOM   1415 C CB   . GLU   A 1 98  ? 13.518 12.636  -7.33   1   34.825  ? 110 GLU   B CB   1 ? 1 
ATOM   1416 C CG   . GLU   A 1 98  ? 12.351 13.628  -7.394  1   44.7    ? 110 GLU   B CG   1 ? 1 
ATOM   1417 C CD   . GLU   A 1 98  ? 10.926 13.105  -7.124  1   48.813  ? 110 GLU   B CD   1 ? 1 
ATOM   1418 O OE1  . GLU   A 1 98  ? 10.708 12.178  -6.264  1   32.259  ? 110 GLU   B OE1  1 ? 1 
ATOM   1419 O OE2  . GLU   A 1 98  ? 9.993  13.699  -7.749  1   50.329  ? 110 GLU   B OE2  1 ? 1 
ATOM   1420 H H    . GLU   A 1 98  ? 11.719 10.77   -7.442  1   26.921  ? 110 GLU   B H    1 c 1 
ATOM   1421 H HA   . GLU   A 1 98  ? 13.395 11.865  -9.254  1   30.652  ? 110 GLU   B HA   1 c 1 
ATOM   1422 H HB2  . GLU   A 1 98  ? 13.555 12.259  -6.426  1   34.912  ? 110 GLU   B HB2  1 c 1 
ATOM   1423 H HB3  . GLU   A 1 98  ? 14.349 13.135  -7.476  1   36.093  ? 110 GLU   B HB3  1 c 1 
ATOM   1424 H HG2  . GLU   A 1 98  ? 12.528 14.349  -6.753  1   43.832  ? 110 GLU   B HG2  1 c 1 
ATOM   1425 H HG3  . GLU   A 1 98  ? 12.351 14.042  -8.283  1   44.266  ? 110 GLU   B HG3  1 c 1 
ATOM   1426 N N    . TYR   A 1 99  ? 14.876 9.611   -7.524  1   23.409  ? 111 TYR   B N    1 ? 1 
ATOM   1427 C CA   . TYR   A 1 99  ? 16.103 8.865   -7.334  1   28.749  ? 111 TYR   B CA   1 ? 1 
ATOM   1428 C C    . TYR   A 1 99  ? 16.047 7.596   -8.176  1   27.952  ? 111 TYR   B C    1 ? 1 
ATOM   1429 O O    . TYR   A 1 99  ? 16.87  6.684   -8.031  1   26.391  ? 111 TYR   B O    1 ? 1 
ATOM   1430 C CB   . TYR   A 1 99  ? 16.285 8.608   -5.851  1   27.279  ? 111 TYR   B CB   1 ? 1 
ATOM   1431 C CG   . TYR   A 1 99  ? 16.585 9.877   -5.062  1   26.375  ? 111 TYR   B CG   1 ? 1 
ATOM   1432 C CD1  . TYR   A 1 99  ? 15.549 10.654  -4.527  1   26.396  ? 111 TYR   B CD1  1 ? 1 
ATOM   1433 C CD2  . TYR   A 1 99  ? 17.881 10.292  -4.805  1   29.74   ? 111 TYR   B CD2  1 ? 1 
ATOM   1434 C CE1  . TYR   A 1 99  ? 15.797 11.812  -3.842  1   27.796  ? 111 TYR   B CE1  1 ? 1 
ATOM   1435 C CE2  . TYR   A 1 99  ? 18.142 11.489  -4.156  1   29.672  ? 111 TYR   B CE2  1 ? 1 
ATOM   1436 C CZ   . TYR   A 1 99  ? 17.103 12.258  -3.699  1   31.55   ? 111 TYR   B CZ   1 ? 1 
ATOM   1437 O OH   . TYR   A 1 99  ? 17.41  13.402  -3.002  1   28.985  ? 111 TYR   B OH   1 ? 1 
ATOM   1438 H H    . TYR   A 1 99  ? 14.109 9.277   -7.157  1   24.871  ? 111 TYR   B H    1 c 1 
ATOM   1439 H HA   . TYR   A 1 99  ? 16.865 9.419   -7.651  1   27.851  ? 111 TYR   B HA   1 c 1 
ATOM   1440 H HB2  . TYR   A 1 99  ? 15.464 8.197   -5.499  1   26.725  ? 111 TYR   B HB2  1 c 1 
ATOM   1441 H HB3  . TYR   A 1 99  ? 17.025 7.974   -5.73   1   26.963  ? 111 TYR   B HB3  1 c 1 
ATOM   1442 H HD1  . TYR   A 1 99  ? 14.654 10.391  -4.675  1   26.437  ? 111 TYR   B HD1  1 c 1 
ATOM   1443 H HD2  . TYR   A 1 99  ? 18.6   9.807   -5.178  1   28.893  ? 111 TYR   B HD2  1 c 1 
ATOM   1444 H HE1  . TYR   A 1 99  ? 15.082 12.339  -3.528  1   28.681  ? 111 TYR   B HE1  1 c 1 
ATOM   1445 H HE2  . TYR   A 1 99  ? 19.031 11.771  -4.023  1   30.883  ? 111 TYR   B HE2  1 c 1 
ATOM   1446 H HH   . TYR   A 1 99  ? 17.55  13.214  -2.175  0   30      ? 111 TYR   B HH   1 c 1 
ATOM   1447 N N    . ALA   A 1 100 ? 15.082 7.559   -9.101  1   26.389  ? 112 ALA   B N    1 ? 1 
ATOM   1448 C CA   . ALA   A 1 100 ? 14.987 6.426   -10.004 1   27.319  ? 112 ALA   B CA   1 ? 1 
ATOM   1449 C C    . ALA   A 1 100 ? 14.772 6.927   -11.442 1   28.103  ? 112 ALA   B C    1 ? 1 
ATOM   1450 O O    . ALA   A 1 100 ? 15.748 7.42    -12.035 1   30.227  ? 112 ALA   B O    1 ? 1 
ATOM   1451 C CB   . ALA   A 1 100 ? 13.878 5.493   -9.541  1   27.061  ? 112 ALA   B CB   1 ? 1 
ATOM   1452 H H    . ALA   A 1 100 ? 14.482 8.242   -9.181  1   27.247  ? 112 ALA   B H    1 c 1 
ATOM   1453 H HA   . ALA   A 1 100 ? 15.851 5.934   -9.98   1   27.115  ? 112 ALA   B HA   1 c 1 
ATOM   1454 H HB1  . ALA   A 1 100 ? 14.141 5.061   -8.712  1   26.474  ? 112 ALA   B HB1  1 c 1 
ATOM   1455 H HB2  . ALA   A 1 100 ? 13.063 6.001   -9.392  1   27.149  ? 112 ALA   B HB2  1 c 1 
ATOM   1456 H HB3  . ALA   A 1 100 ? 13.716 4.814   -10.218 1   27.471  ? 112 ALA   B HB3  1 c 1 
ATOM   1457 N N    . TYR   A 1 101 ? 13.549 6.766   -12.011 1   27.676  ? 113 TYR   B N    1 ? 1 
ATOM   1458 C CA   . TYR   A 1 101 ? 13.375 7.117   -13.427 1   28.179  ? 113 TYR   B CA   1 ? 1 
ATOM   1459 C C    . TYR   A 1 101 ? 12.549 8.386   -13.688 1   29.861  ? 113 TYR   B C    1 ? 1 
ATOM   1460 O O    . TYR   A 1 101 ? 12.254 8.704   -14.841 1   32.468  ? 113 TYR   B O    1 ? 1 
ATOM   1461 C CB   . TYR   A 1 101 ? 12.773 5.963   -14.212 1   29.638  ? 113 TYR   B CB   1 ? 1 
ATOM   1462 C CG   . TYR   A 1 101 ? 13.619 4.713   -14.203 1   29.071  ? 113 TYR   B CG   1 ? 1 
ATOM   1463 C CD1  . TYR   A 1 101 ? 14.726 4.594   -15.024 1   31.098  ? 113 TYR   B CD1  1 ? 1 
ATOM   1464 C CD2  . TYR   A 1 101 ? 13.429 3.761   -13.211 1   28.456  ? 113 TYR   B CD2  1 ? 1 
ATOM   1465 C CE1  . TYR   A 1 101 ? 15.583 3.501   -14.875 1   31.811  ? 113 TYR   B CE1  1 ? 1 
ATOM   1466 C CE2  . TYR   A 1 101 ? 14.271 2.654   -13.079 1   30.63   ? 113 TYR   B CE2  1 ? 1 
ATOM   1467 C CZ   . TYR   A 1 101 ? 15.308 2.494   -13.963 1   29.875  ? 113 TYR   B CZ   1 ? 1 
ATOM   1468 O OH   . TYR   A 1 101 ? 16.179 1.383   -13.898 1   33.897  ? 113 TYR   B OH   1 ? 1 
ATOM   1469 H H    . TYR   A 1 101 ? 12.836 6.46    -11.53  1   27.409  ? 113 TYR   B H    1 c 1 
ATOM   1470 H HA   . TYR   A 1 101 ? 14.28  7.279   -13.803 1   28.991  ? 113 TYR   B HA   1 c 1 
ATOM   1471 H HB2  . TYR   A 1 101 ? 11.891 5.753   -13.833 1   29.278  ? 113 TYR   B HB2  1 c 1 
ATOM   1472 H HB3  . TYR   A 1 101 ? 12.642 6.249   -15.143 1   30.554  ? 113 TYR   B HB3  1 c 1 
ATOM   1473 H HD1  . TYR   A 1 101 ? 14.914 5.259   -15.667 1   31.795  ? 113 TYR   B HD1  1 c 1 
ATOM   1474 H HD2  . TYR   A 1 101 ? 12.701 3.855   -12.618 1   28.545  ? 113 TYR   B HD2  1 c 1 
ATOM   1475 H HE1  . TYR   A 1 101 ? 16.289 3.383   -15.487 1   32.164  ? 113 TYR   B HE1  1 c 1 
ATOM   1476 H HE2  . TYR   A 1 101 ? 14.079 1.983   -12.449 1   29.39   ? 113 TYR   B HE2  1 c 1 
ATOM   1477 H HH   . TYR   A 1 101 ? 16.801 1.566   -13.317 0   30      ? 113 TYR   B HH   1 c 1 
ATOM   1478 N N    . GLY   A 1 102 ? 12.054 9.062   -12.652 1   28.912  ? 114 GLY   B N    1 ? 1 
ATOM   1479 C CA   . GLY   A 1 102 ? 11.645 10.445  -12.777 1   32.593  ? 114 GLY   B CA   1 ? 1 
ATOM   1480 C C    . GLY   A 1 102 ? 10.258 10.547  -13.409 1   38.005  ? 114 GLY   B C    1 ? 1 
ATOM   1481 O O    . GLY   A 1 102 ? 9.531  9.564   -13.554 1   33.143  ? 114 GLY   B O    1 ? 1 
ATOM   1482 H H    . GLY   A 1 102 ? 11.962 8.646   -11.843 1   28.68   ? 114 GLY   B H    1 c 1 
ATOM   1483 H HA2  . GLY   A 1 102 ? 11.634 10.862  -11.884 1   32.222  ? 114 GLY   B HA2  1 c 1 
ATOM   1484 H HA3  . GLY   A 1 102 ? 12.3   10.929  -13.333 1   33.421  ? 114 GLY   B HA3  1 c 1 
ATOM   1485 N N    . SER   A 1 103 ? 9.904  11.754  -13.849 1   35.894  ? 115 SER   B N    1 ? 1 
ATOM   1486 C CA   . SER   A 1 103 ? 8.584  11.889  -14.482 1   35.848  ? 115 SER   B CA   1 ? 1 
ATOM   1487 C C    . SER   A 1 103 ? 8.635  11.378  -15.898 1   34.466  ? 115 SER   B C    1 ? 1 
ATOM   1488 O O    . SER   A 1 103 ? 7.611  11.097  -16.475 1   34.344  ? 115 SER   B O    1 ? 1 
ATOM   1489 C CB   . SER   A 1 103 ? 8.065  13.3    -14.38  1   47.455  ? 115 SER   B CB   1 ? 1 
ATOM   1490 O OG   . SER   A 1 103 ? 9.099  14.118  -14.9   1   50.642  ? 115 SER   B OG   1 ? 1 
ATOM   1491 H H    . SER   A 1 103 ? 10.454 12.479  -13.765 1   36.549  ? 115 SER   B H    1 c 1 
ATOM   1492 H HA   . SER   A 1 103 ? 7.957  11.308  -13.986 1   36.771  ? 115 SER   B HA   1 c 1 
ATOM   1493 H HB2  . SER   A 1 103 ? 7.252  13.401  -14.91  1   46.592  ? 115 SER   B HB2  1 c 1 
ATOM   1494 H HB3  . SER   A 1 103 ? 7.886  13.53   -13.449 1   44.646  ? 115 SER   B HB3  1 c 1 
ATOM   1495 H HG   . SER   A 1 103 ? 8.926  14.921  -14.897 0   30      ? 115 SER   B HG   1 c 1 
ATOM   1496 N N    . ALA   A 1 104 ? 9.815  11.228  -16.485 1   35.536  ? 116 ALA   B N    1 ? 1 
ATOM   1497 C CA   . ALA   A 1 104 ? 9.894  10.728  -17.828 1   38.623  ? 116 ALA   B CA   1 ? 1 
ATOM   1498 C C    . ALA   A 1 104 ? 9.606  9.245   -17.833 1   32.447  ? 116 ALA   B C    1 ? 1 
ATOM   1499 O O    . ALA   A 1 104 ? 9.015  8.715   -18.763 1   32.855  ? 116 ALA   B O    1 ? 1 
ATOM   1500 C CB   . ALA   A 1 104 ? 11.217 11.053  -18.464 1   43.445  ? 116 ALA   B CB   1 ? 1 
ATOM   1501 H H    . ALA   A 1 104 ? 10.584 11.453  -16.046 1   34.912  ? 116 ALA   B H    1 c 1 
ATOM   1502 H HA   . ALA   A 1 104 ? 9.178  11.175  -18.36  1   39.332  ? 116 ALA   B HA   1 c 1 
ATOM   1503 H HB1  . ALA   A 1 104 ? 11.338 12.017  -18.493 1   42.853  ? 116 ALA   B HB1  1 c 1 
ATOM   1504 H HB2  . ALA   A 1 104 ? 11.936 10.655  -17.944 1   40.796  ? 116 ALA   B HB2  1 c 1 
ATOM   1505 H HB3  . ALA   A 1 104 ? 11.241 10.699  -19.369 1   43.248  ? 116 ALA   B HB3  1 c 1 
ATOM   1506 N N    . GLY   A 1 105 ? 9.992  8.582   -16.785 1   33.408  ? 117 GLY   B N    1 ? 1 
ATOM   1507 C CA   . GLY   A 1 105 ? 9.911  7.141   -16.739 1   30.818  ? 117 GLY   B CA   1 ? 1 
ATOM   1508 C C    . GLY   A 1 105 ? 10.972 6.496   -17.621 1   33.321  ? 117 GLY   B C    1 ? 1 
ATOM   1509 O O    . GLY   A 1 105 ? 11.84  7.155   -18.201 1   32.958  ? 117 GLY   B O    1 ? 1 
ATOM   1510 H H    . GLY   A 1 105 ? 10.33  9.027   -16.062 1   31.289  ? 117 GLY   B H    1 c 1 
ATOM   1511 H HA2  . GLY   A 1 105 ? 10.032 6.842   -15.808 1   30.443  ? 117 GLY   B HA2  1 c 1 
ATOM   1512 H HA3  . GLY   A 1 105 ? 9.014  6.857   -17.035 1   32.658  ? 117 GLY   B HA3  1 c 1 
ATOM   1513 N N    . SER   A 1 106 ? 10.693 5.229   -17.91  1   33.167  ? 118 SER   B N    1 ? 1 
ATOM   1514 C CA   . SER   A 1 106 ? 11.516 4.371   -18.725 1   34.343  ? 118 SER   B CA   1 ? 1 
ATOM   1515 C C    . SER   A 1 106 ? 10.679 3.198   -19.258 1   36.808  ? 118 SER   B C    1 ? 1 
ATOM   1516 O O    . SER   A 1 106 ? 10.828 2.049   -18.859 1   35.636  ? 118 SER   B O    1 ? 1 
ATOM   1517 C CB   . SER   A 1 106 ? 12.724 3.827   -17.984 1   32.695  ? 118 SER   B CB   1 ? 1 
ATOM   1518 O OG   . SER   A 1 106 ? 13.644 3.412   -18.988 1   38.041  ? 118 SER   B OG   1 ? 1 
ATOM   1519 H H    . SER   A 1 106 ? 9.926  4.873   -17.562 1   33.326  ? 118 SER   B H    1 c 1 
ATOM   1520 H HA   . SER   A 1 106 ? 11.837 4.898   -19.501 1   35.523  ? 118 SER   B HA   1 c 1 
ATOM   1521 H HB2  . SER   A 1 106 ? 13.121 4.526   -17.431 1   32.676  ? 118 SER   B HB2  1 c 1 
ATOM   1522 H HB3  . SER   A 1 106 ? 12.469 3.071   -17.422 1   33.022  ? 118 SER   B HB3  1 c 1 
ATOM   1523 H HG   . SER   A 1 106 ? 14.308 3.07    -18.55  0   30      ? 118 SER   B HG   1 c 1 
ATOM   1524 N N    . LEU   A 1 107 ? 9.828  3.494   -20.247 1   39.723  ? 119 LEU   B N    1 ? 1 
ATOM   1525 C CA   . LEU   A 1 107 ? 8.875  2.497   -20.733 1   38.33   ? 119 LEU   B CA   1 ? 1 
ATOM   1526 C C    . LEU   A 1 107 ? 9.606  1.523   -21.646 1   39.586  ? 119 LEU   B C    1 ? 1 
ATOM   1527 O O    . LEU   A 1 107 ? 10.557 1.893   -22.321 1   39.327  ? 119 LEU   B O    1 ? 1 
ATOM   1528 C CB   . LEU   A 1 107 ? 7.779  3.253   -21.496 1   43.745  ? 119 LEU   B CB   1 ? 1 
ATOM   1529 C CG   . LEU   A 1 107 ? 6.742  3.983   -20.633 1   42.026  ? 119 LEU   B CG   1 ? 1 
ATOM   1530 C CD1  . LEU   A 1 107 ? 5.704  4.638   -21.484 1   46.046  ? 119 LEU   B CD1  1 ? 1 
ATOM   1531 C CD2  . LEU   A 1 107 ? 6.014  3.069   -19.669 1   43.63   ? 119 LEU   B CD2  1 ? 1 
ATOM   1532 H H    . LEU   A 1 107 ? 9.84   4.326   -20.625 1   39.278  ? 119 LEU   B H    1 c 1 
ATOM   1533 H HA   . LEU   A 1 107 ? 8.486  2.017   -19.962 1   38.721  ? 119 LEU   B HA   1 c 1 
ATOM   1534 H HB2  . LEU   A 1 107 ? 8.212  3.912   -22.086 1   43.24   ? 119 LEU   B HB2  1 c 1 
ATOM   1535 H HB3  . LEU   A 1 107 ? 7.305  2.611   -22.072 1   44.348  ? 119 LEU   B HB3  1 c 1 
ATOM   1536 H HG   . LEU   A 1 107 ? 7.208  4.685   -20.11  1   41.461  ? 119 LEU   B HG   1 c 1 
ATOM   1537 H HD11 . LEU   A 1 107 ? 6.137  5.188   -22.158 1   46.274  ? 119 LEU   B HD11 1 c 1 
ATOM   1538 H HD12 . LEU   A 1 107 ? 5.134  5.196   -20.93  1   45.242  ? 119 LEU   B HD12 1 c 1 
ATOM   1539 H HD13 . LEU   A 1 107 ? 5.164  3.957   -21.921 1   47.118  ? 119 LEU   B HD13 1 c 1 
ATOM   1540 H HD21 . LEU   A 1 107 ? 6.62   2.793   -18.961 1   41.237  ? 119 LEU   B HD21 1 c 1 
ATOM   1541 H HD22 . LEU   A 1 107 ? 5.693  2.284   -20.145 1   44.369  ? 119 LEU   B HD22 1 c 1 
ATOM   1542 H HD23 . LEU   A 1 107 ? 5.259  3.542   -19.279 1   43.101  ? 119 LEU   B HD23 1 c 1 
ATOM   1543 N N    . PRO   A 1 108 ? 9.139  0.272   -21.829 1   42.041  ? 120 PRO   B N    1 ? 1 
ATOM   1544 C CA   . PRO   A 1 108 ? 7.884  -0.209  -21.233 1   45.069  ? 120 PRO   B CA   1 ? 1 
ATOM   1545 C C    . PRO   A 1 108 ? 7.987  -0.613  -19.755 1   41.66   ? 120 PRO   B C    1 ? 1 
ATOM   1546 O O    . PRO   A 1 108 ? 6.971  -0.757  -19.068 1   42.863  ? 120 PRO   B O    1 ? 1 
ATOM   1547 C CB   . PRO   A 1 108 ? 7.489  -1.413  -22.065 1   46.938  ? 120 PRO   B CB   1 ? 1 
ATOM   1548 C CG   . PRO   A 1 108 ? 8.75   -1.802  -22.799 1   49.504  ? 120 PRO   B CG   1 ? 1 
ATOM   1549 C CD   . PRO   A 1 108 ? 9.875  -0.752  -22.538 1   46.146  ? 120 PRO   B CD   1 ? 1 
ATOM   1550 H HA   . PRO   A 1 108 ? 7.194  0.492   -21.334 1   44.547  ? 120 PRO   B HA   1 c 1 
ATOM   1551 H HB2  . PRO   A 1 108 ? 7.175  -2.151  -21.491 1   47.52   ? 120 PRO   B HB2  1 c 1 
ATOM   1552 H HB3  . PRO   A 1 108 ? 6.772  -1.179  -22.7   1   49.334  ? 120 PRO   B HB3  1 c 1 
ATOM   1553 H HG2  . PRO   A 1 108 ? 9.049  -2.686  -22.499 1   48.714  ? 120 PRO   B HG2  1 c 1 
ATOM   1554 H HG3  . PRO   A 1 108 ? 8.569  -1.858  -23.761 1   50.818  ? 120 PRO   B HG3  1 c 1 
ATOM   1555 H HD2  . PRO   A 1 108 ? 10.594 -1.127  -21.983 1   44.467  ? 120 PRO   B HD2  1 c 1 
ATOM   1556 H HD3  . PRO   A 1 108 ? 10.248 -0.411  -23.381 1   46.821  ? 120 PRO   B HD3  1 c 1 
ATOM   1557 N N    . LYS   A 1 109 ? 9.183  -0.776  -19.219 1   41.786  ? 121 LYS   B N    1 ? 1 
ATOM   1558 C CA   . LYS   A 1 109 ? 9.257  -1.363  -17.883 1   40.255  ? 121 LYS   B CA   1 ? 1 
ATOM   1559 C C    . LYS   A 1 109 ? 8.809  -0.411  -16.777 1   43.249  ? 121 LYS   B C    1 ? 1 
ATOM   1560 O O    . LYS   A 1 109 ? 8.26   -0.84   -15.806 1   39.149  ? 121 LYS   B O    1 ? 1 
ATOM   1561 C CB   . LYS   A 1 109 ? 10.659 -1.863  -17.537 1   45.274  ? 121 LYS   B CB   1 ? 1 
ATOM   1562 C CG   . LYS   A 1 109 ? 11.105 -2.999  -18.52  1   49.044  ? 121 LYS   B CG   1 ? 1 
ATOM   1563 C CD   . LYS   A 1 109 ? 12.468 -3.577  -18.101 1   52.496  ? 121 LYS   B CD   1 ? 1 
ATOM   1564 C CE   . LYS   A 1 109 ? 13.043 -4.635  -18.994 1   59.315  ? 121 LYS   B CE   1 ? 1 
ATOM   1565 N NZ   . LYS   A 1 109 ? 12.312 -5.863  -18.695 1   67.086  ? 121 LYS   B NZ   1 ? 1 
ATOM   1566 H H    . LYS   A 1 109 ? 9.946  -0.534  -19.659 1   41.221  ? 121 LYS   B H    1 c 1 
ATOM   1567 H HA   . LYS   A 1 109 ? 8.657  -2.152  -17.865 1   43.236  ? 121 LYS   B HA   1 c 1 
ATOM   1568 H HB2  . LYS   A 1 109 ? 11.297 -1.12   -17.594 1   43.188  ? 121 LYS   B HB2  1 c 1 
ATOM   1569 H HB3  . LYS   A 1 109 ? 10.669 -2.21   -16.62  1   43.134  ? 121 LYS   B HB3  1 c 1 
ATOM   1570 H HG2  . LYS   A 1 109 ? 10.429 -3.711  -18.516 1   50.783  ? 121 LYS   B HG2  1 c 1 
ATOM   1571 H HG3  . LYS   A 1 109 ? 11.169 -2.632  -19.429 1   50.538  ? 121 LYS   B HG3  1 c 1 
ATOM   1572 H HD2  . LYS   A 1 109 ? 13.109 -2.835  -18.045 1   51.463  ? 121 LYS   B HD2  1 c 1 
ATOM   1573 H HD3  . LYS   A 1 109 ? 12.379 -3.944  -17.194 1   51.754  ? 121 LYS   B HD3  1 c 1 
ATOM   1574 H HE2  . LYS   A 1 109 ? 12.921 -4.398  -19.931 1   60.875  ? 121 LYS   B HE2  1 c 1 
ATOM   1575 H HE3  . LYS   A 1 109 ? 13.991 -4.762  -18.812 1   59.167  ? 121 LYS   B HE3  1 c 1 
ATOM   1576 H HZ1  . LYS   A 1 109 ? 11.427 -5.75   -18.849 1   65.3    ? 121 LYS   B HZ1  1 c 1 
ATOM   1577 H HZ2  . LYS   A 1 109 ? 12.438 -6.098  -17.829 1   63.797  ? 121 LYS   B HZ2  1 c 1 
ATOM   1578 H HZ3  . LYS   A 1 109 ? 12.617 -6.531  -19.225 1   66.446  ? 121 LYS   B HZ3  1 c 1 
ATOM   1579 N N    . ILE   A 1 110 ? 9.106  0.869   -16.844 1   36.43   ? 122 ILE   B N    1 ? 1 
ATOM   1580 C CA   . ILE   A 1 110 ? 8.865  1.752   -15.716 1   35.074  ? 122 ILE   B CA   1 ? 1 
ATOM   1581 C C    . ILE   A 1 110 ? 8.006  2.927   -16.176 1   34.312  ? 122 ILE   B C    1 ? 1 
ATOM   1582 O O    . ILE   A 1 110 ? 8.491  3.646   -17.069 1   34.732  ? 122 ILE   B O    1 ? 1 
ATOM   1583 C CB   . ILE   A 1 110 ? 10.19  2.36    -15.208 1   35.372  ? 122 ILE   B CB   1 ? 1 
ATOM   1584 C CG1  . ILE   A 1 110 ? 11.33  1.352   -15.079 1   40.018  ? 122 ILE   B CG1  1 ? 1 
ATOM   1585 C CG2  . ILE   A 1 110 ? 9.946  3.188   -13.953 1   34.421  ? 122 ILE   B CG2  1 ? 1 
ATOM   1586 C CD1  . ILE   A 1 110 ? 11.077 0.309   -14.033 1   46.861  ? 122 ILE   B CD1  1 ? 1 
ATOM   1587 H H    . ILE   A 1 110 ? 9.472  1.214   -17.607 1   38.341  ? 122 ILE   B H    1 c 1 
ATOM   1588 H HA   . ILE   A 1 110 ? 8.424  1.269   -14.994 1   34.9    ? 122 ILE   B HA   1 c 1 
ATOM   1589 H HB   . ILE   A 1 110 ? 10.478 2.993   -15.895 1   36.338  ? 122 ILE   B HB   1 c 1 
ATOM   1590 H HG12 . ILE   A 1 110 ? 11.466 0.911   -15.942 1   41.374  ? 122 ILE   B HG12 1 c 1 
ATOM   1591 H HG13 . ILE   A 1 110 ? 12.153 1.832   -14.854 1   39.347  ? 122 ILE   B HG13 1 c 1 
ATOM   1592 H HG21 . ILE   A 1 110 ? 10.746 3.188   -13.402 1   33.171  ? 122 ILE   B HG21 1 c 1 
ATOM   1593 H HG22 . ILE   A 1 110 ? 9.209  2.807   -13.447 1   34.343  ? 122 ILE   B HG22 1 c 1 
ATOM   1594 H HG23 . ILE   A 1 110 ? 9.728  4.102   -14.202 1   34.445  ? 122 ILE   B HG23 1 c 1 
ATOM   1595 H HD11 . ILE   A 1 110 ? 11.079 0.722   -13.149 1   43.251  ? 122 ILE   B HD11 1 c 1 
ATOM   1596 H HD12 . ILE   A 1 110 ? 11.781 -0.363  -14.077 1   44.369  ? 122 ILE   B HD12 1 c 1 
ATOM   1597 H HD13 . ILE   A 1 110 ? 10.213 -0.117  -14.189 1   45.266  ? 122 ILE   B HD13 1 c 1 
ATOM   1598 N N    . PRO   A 1 111 ? 6.833  3.195   -15.558 1   36.643  ? 123 PRO   B N    1 ? 1 
ATOM   1599 C CA   . PRO   A 1 111 ? 5.995  4.333   -15.948 1   33.323  ? 123 PRO   B CA   1 ? 1 
ATOM   1600 C C    . PRO   A 1 111 ? 6.555  5.587   -15.357 1   32.49   ? 123 PRO   B C    1 ? 1 
ATOM   1601 O O    . PRO   A 1 111 ? 7.453  5.535   -14.509 1   32.482  ? 123 PRO   B O    1 ? 1 
ATOM   1602 C CB   . PRO   A 1 111 ? 4.592  4.072   -15.502 1   36.797  ? 123 PRO   B CB   1 ? 1 
ATOM   1603 C CG   . PRO   A 1 111 ? 4.72   2.729   -14.758 1   38.513  ? 123 PRO   B CG   1 ? 1 
ATOM   1604 C CD   . PRO   A 1 111 ? 6.163  2.307   -14.586 1   38.208  ? 123 PRO   B CD   1 ? 1 
ATOM   1605 H HA   . PRO   A 1 111 ? 6.009  4.403   -16.936 1   35.863  ? 123 PRO   B HA   1 c 1 
ATOM   1606 H HB2  . PRO   A 1 111 ? 4.27   4.783   -14.899 1   36.322  ? 123 PRO   B HB2  1 c 1 
ATOM   1607 H HB3  . PRO   A 1 111 ? 3.983  3.995   -16.273 1   38.514  ? 123 PRO   B HB3  1 c 1 
ATOM   1608 H HG2  . PRO   A 1 111 ? 4.299  2.804   -13.877 1   37.91   ? 123 PRO   B HG2  1 c 1 
ATOM   1609 H HG3  . PRO   A 1 111 ? 4.238  2.035   -15.255 1   39.808  ? 123 PRO   B HG3  1 c 1 
ATOM   1610 H HD2  . PRO   A 1 111 ? 6.479  2.472   -13.67  1   36.105  ? 123 PRO   B HD2  1 c 1 
ATOM   1611 H HD3  . PRO   A 1 111 ? 6.286  1.36    -14.816 1   38.02   ? 123 PRO   B HD3  1 c 1 
ATOM   1612 N N    . SER   A 1 112 ? 5.952  6.678   -15.805 1   32.33   ? 124 SER   B N    1 ? 1 
ATOM   1613 C CA   . SER   A 1 112 ? 6.181  7.971   -15.217 1   29.766  ? 124 SER   B CA   1 ? 1 
ATOM   1614 C C    . SER   A 1 112 ? 5.919  7.935   -13.712 1   30.925  ? 124 SER   B C    1 ? 1 
ATOM   1615 O O    . SER   A 1 112 ? 4.945  7.37    -13.307 1   30.145  ? 124 SER   B O    1 ? 1 
ATOM   1616 C CB   . SER   A 1 112 ? 5.285  8.996   -15.926 1   31.722  ? 124 SER   B CB   1 ? 1 
ATOM   1617 O OG   . SER   A 1 112 ? 5.457  10.26   -15.29  1   33.093  ? 124 SER   B OG   1 ? 1 
ATOM   1618 H H    . SER   A 1 112 ? 5.374  6.613   -16.51  1   33.764  ? 124 SER   B H    1 c 1 
ATOM   1619 H HA   . SER   A 1 112 ? 7.129  8.218   -15.369 1   29.848  ? 124 SER   B HA   1 c 1 
ATOM   1620 H HB2  . SER   A 1 112 ? 5.537  9.06    -16.865 1   33.148  ? 124 SER   B HB2  1 c 1 
ATOM   1621 H HB3  . SER   A 1 112 ? 4.351  8.717   -15.865 1   33.143  ? 124 SER   B HB3  1 c 1 
ATOM   1622 H HG   . SER   A 1 112 ? 4.937  10.813  -15.665 0   30      ? 124 SER   B HG   1 c 1 
ATOM   1623 N N    . ASN   A 1 113 ? 6.793  8.573   -12.965 1   30.057  ? 125 ASN   B N    1 ? 1 
ATOM   1624 C CA   . ASN   A 1 113 ? 6.537  8.892   -11.555 1   32.962  ? 125 ASN   B CA   1 ? 1 
ATOM   1625 C C    . ASN   A 1 113 ? 6.357  7.586   -10.729 1   33.158  ? 125 ASN   B C    1 ? 1 
ATOM   1626 O O    . ASN   A 1 113 ? 5.611  7.53    -9.769  1   32.544  ? 125 ASN   B O    1 ? 1 
ATOM   1627 C CB   . ASN   A 1 113 ? 5.349  9.829   -11.402 1   32.409  ? 125 ASN   B CB   1 ? 1 
ATOM   1628 C CG   . ASN   A 1 113 ? 5.7    11.218  -11.904 1   36.226  ? 125 ASN   B CG   1 ? 1 
ATOM   1629 O OD1  . ASN   A 1 113 ? 6.868  11.593  -11.996 1   38.726  ? 125 ASN   B OD1  1 ? 1 
ATOM   1630 N ND2  . ASN   A 1 113 ? 4.709  11.963  -12.276 1   39.288  ? 125 ASN   B ND2  1 ? 1 
ATOM   1631 H H    . ASN   A 1 113 ? 7.592  8.827   -13.331 1   30.338  ? 125 ASN   B H    1 c 1 
ATOM   1632 H HA   . ASN   A 1 113 ? 7.328  9.361   -11.205 1   31.145  ? 125 ASN   B HA   1 c 1 
ATOM   1633 H HB2  . ASN   A 1 113 ? 4.587  9.483   -11.906 1   34.67   ? 125 ASN   B HB2  1 c 1 
ATOM   1634 H HB3  . ASN   A 1 113 ? 5.095  9.882   -10.459 1   33.163  ? 125 ASN   B HB3  1 c 1 
ATOM   1635 H HD21 . ASN   A 1 113 ? 4.843  12.619  -12.858 1   39.828  ? 125 ASN   B HD21 1 c 1 
ATOM   1636 H HD22 . ASN   A 1 113 ? 3.897  11.817  -11.949 1   39.547  ? 125 ASN   B HD22 1 c 1 
ATOM   1637 N N    . ALA   A 1 114 ? 7.139  6.573   -11.034 1   28.387  ? 126 ALA   B N    1 ? 1 
ATOM   1638 C CA   . ALA   A 1 114 ? 7.111  5.285   -10.367 1   34.064  ? 126 ALA   B CA   1 ? 1 
ATOM   1639 C C    . ALA   A 1 114 ? 8.011  5.302   -9.116  1   27.941  ? 126 ALA   B C    1 ? 1 
ATOM   1640 O O    . ALA   A 1 114 ? 9.197  5.756   -9.121  1   27.053  ? 126 ALA   B O    1 ? 1 
ATOM   1641 C CB   . ALA   A 1 114 ? 7.536  4.167   -11.328 1   32.884  ? 126 ALA   B CB   1 ? 1 
ATOM   1642 H H    . ALA   A 1 114 ? 7.748  6.689   -11.706 1   30.559  ? 126 ALA   B H    1 c 1 
ATOM   1643 H HA   . ALA   A 1 114 ? 6.175  5.112   -10.075 1   32.47   ? 126 ALA   B HA   1 c 1 
ATOM   1644 H HB1  . ALA   A 1 114 ? 6.951  4.164   -12.104 1   34.555  ? 126 ALA   B HB1  1 c 1 
ATOM   1645 H HB2  . ALA   A 1 114 ? 8.452  4.316   -11.618 1   32.71   ? 126 ALA   B HB2  1 c 1 
ATOM   1646 H HB3  . ALA   A 1 114 ? 7.477  3.308   -10.878 1   33.252  ? 126 ALA   B HB3  1 c 1 
ATOM   1647 N N    . THR   A 1 115 ? 7.381  4.859   -8.019  1   27.472  ? 127 THR   B N    1 ? 1 
ATOM   1648 C CA   . THR   A 1 115 ? 8.148  4.475   -6.817  1   26.426  ? 127 THR   B CA   1 ? 1 
ATOM   1649 C C    . THR   A 1 115 ? 8.552  2.992   -6.95   1   28.159  ? 127 THR   B C    1 ? 1 
ATOM   1650 O O    . THR   A 1 115 ? 7.709  2.127   -7.269  1   31.296  ? 127 THR   B O    1 ? 1 
ATOM   1651 C CB   . THR   A 1 115 ? 7.262  4.687   -5.6    1   27.611  ? 127 THR   B CB   1 ? 1 
ATOM   1652 O OG1  . THR   A 1 115 ? 7.064  6.138   -5.496  1   28.791  ? 127 THR   B OG1  1 ? 1 
ATOM   1653 C CG2  . THR   A 1 115 ? 7.851  4.108   -4.321  1   31.398  ? 127 THR   B CG2  1 ? 1 
ATOM   1654 H H    . THR   A 1 115 ? 6.469  4.794   -8.007  1   28.651  ? 127 THR   B H    1 c 1 
ATOM   1655 H HA   . THR   A 1 115 ? 8.947  5.037   -6.745  1   26.097  ? 127 THR   B HA   1 c 1 
ATOM   1656 H HB   . THR   A 1 115 ? 6.389  4.255   -5.759  1   29.488  ? 127 THR   B HB   1 c 1 
ATOM   1657 H HG1  . THR   A 1 115 ? 7.83   6.506   -5.39   0   30      ? 127 THR   B HG1  1 c 1 
ATOM   1658 H HG21 . THR   A 1 115 ? 7.343  4.428   -3.557  1   30.405  ? 127 THR   B HG21 1 c 1 
ATOM   1659 H HG22 . THR   A 1 115 ? 8.776  4.388   -4.233  1   29.117  ? 127 THR   B HG22 1 c 1 
ATOM   1660 H HG23 . THR   A 1 115 ? 7.808  3.138   -4.351  1   30.359  ? 127 THR   B HG23 1 c 1 
ATOM   1661 N N    . LEU   A 1 116 ? 9.757  2.669   -6.496  1   27.133  ? 128 LEU   B N    1 ? 1 
ATOM   1662 C CA   . LEU   A 1 116 ? 10.336 1.331   -6.698  1   27.027  ? 128 LEU   B CA   1 ? 1 
ATOM   1663 C C    . LEU   A 1 116 ? 10.774 0.753   -5.35   1   28.933  ? 128 LEU   B C    1 ? 1 
ATOM   1664 O O    . LEU   A 1 116 ? 11.105 1.513   -4.459  1   25.486  ? 128 LEU   B O    1 ? 1 
ATOM   1665 C CB   . LEU   A 1 116 ? 11.613 1.378   -7.568  1   32.16   ? 128 LEU   B CB   1 ? 1 
ATOM   1666 C CG   . LEU   A 1 116 ? 11.572 2.072   -8.931  1   33.117  ? 128 LEU   B CG   1 ? 1 
ATOM   1667 C CD1  . LEU   A 1 116 ? 12.824 1.648   -9.734  1   31.438  ? 128 LEU   B CD1  1 ? 1 
ATOM   1668 C CD2  . LEU   A 1 116 ? 10.383 1.659   -9.678  1   31.003  ? 128 LEU   B CD2  1 ? 1 
ATOM   1669 H H    . LEU   A 1 116 ? 10.245 3.293   -6.04   1   26.384  ? 128 LEU   B H    1 c 1 
ATOM   1670 H HA   . LEU   A 1 116 ? 9.663  0.736   -7.116  1   29.359  ? 128 LEU   B HA   1 c 1 
ATOM   1671 H HB2  . LEU   A 1 116 ? 12.322 1.807   -7.034  1   30.147  ? 128 LEU   B HB2  1 c 1 
ATOM   1672 H HB3  . LEU   A 1 116 ? 11.911 0.45    -7.71   1   31.264  ? 128 LEU   B HB3  1 c 1 
ATOM   1673 H HG   . LEU   A 1 116 ? 11.568 3.055   -8.803  1   31.627  ? 128 LEU   B HG   1 c 1 
ATOM   1674 H HD11 . LEU   A 1 116 ? 13.623 1.833   -9.212  1   31.294  ? 128 LEU   B HD11 1 c 1 
ATOM   1675 H HD12 . LEU   A 1 116 ? 12.859 2.147   -10.566 1   32.265  ? 128 LEU   B HD12 1 c 1 
ATOM   1676 H HD13 . LEU   A 1 116 ? 12.779 0.697   -9.929  1   32.496  ? 128 LEU   B HD13 1 c 1 
ATOM   1677 H HD21 . LEU   A 1 116 ? 9.604  2.125   -9.334  1   32.115  ? 128 LEU   B HD21 1 c 1 
ATOM   1678 H HD22 . LEU   A 1 116 ? 10.255 0.7     -9.582  1   32.507  ? 128 LEU   B HD22 1 c 1 
ATOM   1679 H HD23 . LEU   A 1 116 ? 10.498 1.876   -10.619 1   32.466  ? 128 LEU   B HD23 1 c 1 
ATOM   1680 N N    . PHE   A 1 117 ? 10.766 -0.581  -5.249  1   26.95   ? 129 PHE   B N    1 ? 1 
ATOM   1681 C CA   . PHE   A 1 117 ? 11.105 -1.288  -4.03   1   27.425  ? 129 PHE   B CA   1 ? 1 
ATOM   1682 C C    . PHE   A 1 117 ? 12.132 -2.32   -4.47   1   26.573  ? 129 PHE   B C    1 ? 1 
ATOM   1683 O O    . PHE   A 1 117 ? 11.965 -2.989  -5.518  1   30.255  ? 129 PHE   B O    1 ? 1 
ATOM   1684 C CB   . PHE   A 1 117 ? 9.873  -1.926  -3.378  1   31.245  ? 129 PHE   B CB   1 ? 1 
ATOM   1685 C CG   . PHE   A 1 117 ? 10.309 -2.93   -2.335  1   34.338  ? 129 PHE   B CG   1 ? 1 
ATOM   1686 C CD1  . PHE   A 1 117 ? 10.592 -4.24   -2.715  1   37.259  ? 129 PHE   B CD1  1 ? 1 
ATOM   1687 C CD2  . PHE   A 1 117 ? 10.55  -2.556  -1.015  1   34.964  ? 129 PHE   B CD2  1 ? 1 
ATOM   1688 C CE1  . PHE   A 1 117 ? 11.048 -5.135  -1.783  1   40.41   ? 129 PHE   B CE1  1 ? 1 
ATOM   1689 C CE2  . PHE   A 1 117 ? 10.967 -3.483  -0.073  1   36.135  ? 129 PHE   B CE2  1 ? 1 
ATOM   1690 C CZ   . PHE   A 1 117 ? 11.205 -4.76   -0.448  1   34.938  ? 129 PHE   B CZ   1 ? 1 
ATOM   1691 H H    . PHE   A 1 117 ? 10.532 -1.073  -5.984  1   28.341  ? 129 PHE   B H    1 c 1 
ATOM   1692 H HA   . PHE   A 1 117 ? 11.523 -0.657  -3.392  1   26.826  ? 129 PHE   B HA   1 c 1 
ATOM   1693 H HB2  . PHE   A 1 117 ? 9.331  -1.224  -2.954  1   31.061  ? 129 PHE   B HB2  1 c 1 
ATOM   1694 H HB3  . PHE   A 1 117 ? 9.339  -2.378  -4.068  1   32.079  ? 129 PHE   B HB3  1 c 1 
ATOM   1695 H HD1  . PHE   A 1 117 ? 10.472 -4.509  -3.612  1   37.631  ? 129 PHE   B HD1  1 c 1 
ATOM   1696 H HD2  . PHE   A 1 117 ? 10.362 -1.672  -0.744  1   34.187  ? 129 PHE   B HD2  1 c 1 
ATOM   1697 H HE1  . PHE   A 1 117 ? 11.202 -6.031  -2.036  1   39.57   ? 129 PHE   B HE1  1 c 1 
ATOM   1698 H HE2  . PHE   A 1 117 ? 11.095 -3.22   0.824   1   35.483  ? 129 PHE   B HE2  1 c 1 
ATOM   1699 H HZ   . PHE   A 1 117 ? 11.514 -5.388  0.186   1   37.424  ? 129 PHE   B HZ   1 c 1 
ATOM   1700 N N    . PHE   A 1 118 ? 13.223 -2.411  -3.722  1   26.667  ? 130 PHE   B N    1 ? 1 
ATOM   1701 C CA   . PHE   A 1 118 ? 14.15  -3.519  -3.944  1   26.366  ? 130 PHE   B CA   1 ? 1 
ATOM   1702 C C    . PHE   A 1 118 ? 14.518 -4.201  -2.64   1   27.744  ? 130 PHE   B C    1 ? 1 
ATOM   1703 O O    . PHE   A 1 118 ? 14.664 -3.523  -1.614  1   32.053  ? 130 PHE   B O    1 ? 1 
ATOM   1704 C CB   . PHE   A 1 118 ? 15.469 -3.028  -4.539  1   24.854  ? 130 PHE   B CB   1 ? 1 
ATOM   1705 C CG   . PHE   A 1 118 ? 15.417 -2.41   -5.931  1   28.868  ? 130 PHE   B CG   1 ? 1 
ATOM   1706 C CD1  . PHE   A 1 118 ? 14.941 -1.111  -6.152  1   29.247  ? 130 PHE   B CD1  1 ? 1 
ATOM   1707 C CD2  . PHE   A 1 118 ? 15.835 -3.141  -7.004  1   29.648  ? 130 PHE   B CD2  1 ? 1 
ATOM   1708 C CE1  . PHE   A 1 118 ? 14.995 -0.546  -7.399  1   28.605  ? 130 PHE   B CE1  1 ? 1 
ATOM   1709 C CE2  . PHE   A 1 118 ? 15.805 -2.58   -8.278  1   29.975  ? 130 PHE   B CE2  1 ? 1 
ATOM   1710 C CZ   . PHE   A 1 118 ? 15.412 -1.301  -8.449  1   27.879  ? 130 PHE   B CZ   1 ? 1 
ATOM   1711 H H    . PHE   A 1 118 ? 13.403 -1.792  -3.074  1   25.704  ? 130 PHE   B H    1 c 1 
ATOM   1712 H HA   . PHE   A 1 118 ? 13.737 -4.179  -4.558  1   27.496  ? 130 PHE   B HA   1 c 1 
ATOM   1713 H HB2  . PHE   A 1 118 ? 15.852 -2.366  -3.922  1   25.275  ? 130 PHE   B HB2  1 c 1 
ATOM   1714 H HB3  . PHE   A 1 118 ? 16.093 -3.788  -4.562  1   26.68   ? 130 PHE   B HB3  1 c 1 
ATOM   1715 H HD1  . PHE   A 1 118 ? 14.691 -0.581  -5.413  1   28.227  ? 130 PHE   B HD1  1 c 1 
ATOM   1716 H HD2  . PHE   A 1 118 ? 16.139 -4.026  -6.883  1   30.517  ? 130 PHE   B HD2  1 c 1 
ATOM   1717 H HE1  . PHE   A 1 118 ? 14.673 0.33    -7.538  1   27.925  ? 130 PHE   B HE1  1 c 1 
ATOM   1718 H HE2  . PHE   A 1 118 ? 16.11  -3.081  -9.017  1   30.449  ? 130 PHE   B HE2  1 c 1 
ATOM   1719 H HZ   . PHE   A 1 118 ? 15.386 -0.937  -9.32   1   28.789  ? 130 PHE   B HZ   1 c 1 
ATOM   1720 N N    . GLU   A 1 119 ? 14.841 -5.488  -2.779  1   30.646  ? 131 GLU   B N    1 ? 1 
ATOM   1721 C CA   . GLU   A 1 119 ? 15.699 -6.224  -1.873  1   30.109  ? 131 GLU   B CA   1 ? 1 
ATOM   1722 C C    . GLU   A 1 119 ? 17.009 -6.499  -2.579  1   27.79   ? 131 GLU   B C    1 ? 1 
ATOM   1723 O O    . GLU   A 1 119 ? 17.021 -7.056  -3.704  1   34.108  ? 131 GLU   B O    1 ? 1 
ATOM   1724 C CB   . GLU   A 1 119 ? 15.007 -7.512  -1.429  1   30.613  ? 131 GLU   B CB   1 ? 1 
ATOM   1725 C CG   . GLU   A 1 119 ? 15.85  -8.392  -0.495  1   35.871  ? 131 GLU   B CG   1 ? 1 
ATOM   1726 C CD   . GLU   A 1 119 ? 15.134 -9.603  0.087   1   35.309  ? 131 GLU   B CD   1 ? 1 
ATOM   1727 O OE1  . GLU   A 1 119 ? 14.412 -9.465  1.081   1   38.612  ? 131 GLU   B OE1  1 ? 1 
ATOM   1728 O OE2  . GLU   A 1 119 ? 15.344 -10.702 -0.504  1   35.497  ? 131 GLU   B OE2  1 ? 1 
ATOM   1729 H H    . GLU   A 1 119 ? 14.494 -5.94   -3.493  1   30.585  ? 131 GLU   B H    1 c 1 
ATOM   1730 H HA   . GLU   A 1 119 ? 15.869 -5.662  -1.077  1   29.082  ? 131 GLU   B HA   1 c 1 
ATOM   1731 H HB2  . GLU   A 1 119 ? 14.172 -7.278  -0.972  1   31.794  ? 131 GLU   B HB2  1 c 1 
ATOM   1732 H HB3  . GLU   A 1 119 ? 14.773 -8.033  -2.226  1   32.506  ? 131 GLU   B HB3  1 c 1 
ATOM   1733 H HG2  . GLU   A 1 119 ? 16.638 -8.709  -0.986  1   34.496  ? 131 GLU   B HG2  1 c 1 
ATOM   1734 H HG3  . GLU   A 1 119 ? 16.175 -7.84   0.249   1   33.586  ? 131 GLU   B HG3  1 c 1 
ATOM   1735 N N    . ILE   A 1 120 ? 18.063 -6.188  -1.837  1   31.616  ? 132 ILE   B N    1 ? 1 
ATOM   1736 C CA   . ILE   A 1 120 ? 19.414 -6.235  -2.339  1   27.887  ? 132 ILE   B CA   1 ? 1 
ATOM   1737 C C    . ILE   A 1 120 ? 20.251 -7.02   -1.376  1   31.739  ? 132 ILE   B C    1 ? 1 
ATOM   1738 O O    . ILE   A 1 120 ? 20.38  -6.619  -0.184  1   31.118  ? 132 ILE   B O    1 ? 1 
ATOM   1739 C CB   . ILE   A 1 120 ? 20.083 -4.849  -2.571  1   28.519  ? 132 ILE   B CB   1 ? 1 
ATOM   1740 C CG1  . ILE   A 1 120 ? 19.206 -3.895  -3.41   1   28.667  ? 132 ILE   B CG1  1 ? 1 
ATOM   1741 C CG2  . ILE   A 1 120 ? 21.43  -5.047  -3.26   1   31.617  ? 132 ILE   B CG2  1 ? 1 
ATOM   1742 C CD1  . ILE   A 1 120 ? 19.896 -2.555  -3.668  1   26.887  ? 132 ILE   B CD1  1 ? 1 
ATOM   1743 H H    . ILE   A 1 120 ? 17.934 -5.936  -0.968  1   29.451  ? 132 ILE   B H    1 c 1 
ATOM   1744 H HA   . ILE   A 1 120 ? 19.403 -6.707  -3.194  1   29.997  ? 132 ILE   B HA   1 c 1 
ATOM   1745 H HB   . ILE   A 1 120 ? 20.239 -4.433  -1.7    1   28.496  ? 132 ILE   B HB   1 c 1 
ATOM   1746 H HG12 . ILE   A 1 120 ? 19     -4.32   -4.268  1   28.553  ? 132 ILE   B HG12 1 c 1 
ATOM   1747 H HG13 . ILE   A 1 120 ? 18.363 -3.736  -2.939  1   27.748  ? 132 ILE   B HG13 1 c 1 
ATOM   1748 H HG21 . ILE   A 1 120 ? 21.905 -4.2    -3.299  1   30.345  ? 132 ILE   B HG21 1 c 1 
ATOM   1749 H HG22 . ILE   A 1 120 ? 21.288 -5.377  -4.163  1   31.267  ? 132 ILE   B HG22 1 c 1 
ATOM   1750 H HG23 . ILE   A 1 120 ? 21.963 -5.688  -2.763  1   31.965  ? 132 ILE   B HG23 1 c 1 
ATOM   1751 H HD11 . ILE   A 1 120 ? 20.415 -2.298  -2.883  1   27.154  ? 132 ILE   B HD11 1 c 1 
ATOM   1752 H HD12 . ILE   A 1 120 ? 19.223 -1.872  -3.848  1   26.344  ? 132 ILE   B HD12 1 c 1 
ATOM   1753 H HD13 . ILE   A 1 120 ? 20.49  -2.635  -4.438  1   27.562  ? 132 ILE   B HD13 1 c 1 
ATOM   1754 N N    . GLU   A 1 121 ? 20.895 -8.014  -1.992  1   31.137  ? 133 GLU   B N    1 ? 1 
ATOM   1755 C CA   . GLU   A 1 121 ? 21.938 -8.695  -1.228  1   37.109  ? 133 GLU   B CA   1 ? 1 
ATOM   1756 C C    . GLU   A 1 121 ? 23.292 -8.311  -1.821  1   36.509  ? 133 GLU   B C    1 ? 1 
ATOM   1757 O O    . GLU   A 1 121 ? 23.559 -8.581  -3.026  1   36.093  ? 133 GLU   B O    1 ? 1 
ATOM   1758 C CB   . GLU   A 1 121 ? 21.782 -10.213 -1.185  1   36.394  ? 133 GLU   B CB   1 ? 1 
ATOM   1759 C CG   . GLU   A 1 121 ? 22.955 -10.898 -0.464  1   42.766  ? 133 GLU   B CG   1 ? 1 
ATOM   1760 C CD   . GLU   A 1 121 ? 22.87  -12.392 -0.292  1   45.894  ? 133 GLU   B CD   1 ? 1 
ATOM   1761 O OE1  . GLU   A 1 121 ? 21.836 -12.971 -0.733  1   50.268  ? 133 GLU   B OE1  1 ? 1 
ATOM   1762 O OE2  . GLU   A 1 121 ? 23.851 -13.002 0.25    1   43.323  ? 133 GLU   B OE2  1 ? 1 
ATOM   1763 H H    . GLU   A 1 121 ? 20.702 -8.271  -2.848  1   32.742  ? 133 GLU   B H    1 c 1 
ATOM   1764 H HA   . GLU   A 1 121 ? 21.901 -8.369  -0.296  1   35.182  ? 133 GLU   B HA   1 c 1 
ATOM   1765 H HB2  . GLU   A 1 121 ? 20.944 -10.434 -0.728  1   38.097  ? 133 GLU   B HB2  1 c 1 
ATOM   1766 H HB3  . GLU   A 1 121 ? 21.722 -10.553 -2.103  1   38.394  ? 133 GLU   B HB3  1 c 1 
ATOM   1767 H HG2  . GLU   A 1 121 ? 23.782 -10.701 -0.953  1   41.958  ? 133 GLU   B HG2  1 c 1 
ATOM   1768 H HG3  . GLU   A 1 121 ? 23.05  -10.497 0.426   1   41.444  ? 133 GLU   B HG3  1 c 1 
ATOM   1769 N N    . LEU   A 1 122 ? 24.14  -7.744  -0.972  1   32.436  ? 134 LEU   B N    1 ? 1 
ATOM   1770 C CA   . LEU   A 1 122 ? 25.518 -7.426  -1.359  1   39.681  ? 134 LEU   B CA   1 ? 1 
ATOM   1771 C C    . LEU   A 1 122 ? 26.449 -8.625  -1.244  1   44.788  ? 134 LEU   B C    1 ? 1 
ATOM   1772 O O    . LEU   A 1 122 ? 26.843 -8.937  -0.138  1   41.032  ? 134 LEU   B O    1 ? 1 
ATOM   1773 C CB   . LEU   A 1 122 ? 26.094 -6.265  -0.543  1   40.1    ? 134 LEU   B CB   1 ? 1 
ATOM   1774 C CG   . LEU   A 1 122 ? 27.504 -5.764  -0.925  1   40.635  ? 134 LEU   B CG   1 ? 1 
ATOM   1775 C CD1  . LEU   A 1 122 ? 27.605 -5.512  -2.449  1   39.449  ? 134 LEU   B CD1  1 ? 1 
ATOM   1776 C CD2  . LEU   A 1 122 ? 27.829 -4.501  -0.143  1   37.642  ? 134 LEU   B CD2  1 ? 1 
ATOM   1777 H H    . LEU   A 1 122 ? 23.864 -7.542  -0.124  1   34.398  ? 134 LEU   B H    1 c 1 
ATOM   1778 H HA   . LEU   A 1 122 ? 25.499 -7.154  -2.311  1   38.37   ? 134 LEU   B HA   1 c 1 
ATOM   1779 H HB2  . LEU   A 1 122 ? 25.47  -5.506  -0.613  1   38.157  ? 134 LEU   B HB2  1 c 1 
ATOM   1780 H HB3  . LEU   A 1 122 ? 26.109 -6.534  0.404   1   40.313  ? 134 LEU   B HB3  1 c 1 
ATOM   1781 H HG   . LEU   A 1 122 ? 28.164 -6.462  -0.677  1   41.863  ? 134 LEU   B HG   1 c 1 
ATOM   1782 H HD11 . LEU   A 1 122 ? 27.679 -6.361  -2.915  1   40.727  ? 134 LEU   B HD11 1 c 1 
ATOM   1783 H HD12 . LEU   A 1 122 ? 28.389 -4.97   -2.637  1   40.274  ? 134 LEU   B HD12 1 c 1 
ATOM   1784 H HD13 . LEU   A 1 122 ? 26.809 -5.044  -2.754  1   38.179  ? 134 LEU   B HD13 1 c 1 
ATOM   1785 H HD21 . LEU   A 1 122 ? 27.655 -4.648  0.8     1   38.499  ? 134 LEU   B HD21 1 c 1 
ATOM   1786 H HD22 . LEU   A 1 122 ? 27.274 -3.769  -0.463  1   36.822  ? 134 LEU   B HD22 1 c 1 
ATOM   1787 H HD23 . LEU   A 1 122 ? 28.766 -4.273  -0.267  1   39.419  ? 134 LEU   B HD23 1 c 1 
ATOM   1788 N N    . LEU   A 1 123 ? 26.875 -9.21   -2.392  1   45.281  ? 135 LEU   B N    1 ? 1 
ATOM   1789 C CA   . LEU   A 1 123 ? 27.659 -10.434 -2.4    1   48.709  ? 135 LEU   B CA   1 ? 1 
ATOM   1790 C C    . LEU   A 1 123 ? 29.141 -10.112 -2.202  1   51.61   ? 135 LEU   B C    1 ? 1 
ATOM   1791 O O    . LEU   A 1 123 ? 29.812 -10.81  -1.434  1   60.019  ? 135 LEU   B O    1 ? 1 
ATOM   1792 C CB   . LEU   A 1 123 ? 27.468 -11.177 -3.723  1   47.673  ? 135 LEU   B CB   1 ? 1 
ATOM   1793 C CG   . LEU   A 1 123 ? 26.025 -11.55  -4.05   1   48.272  ? 135 LEU   B CG   1 ? 1 
ATOM   1794 C CD1  . LEU   A 1 123 ? 25.942 -12.098 -5.508  1   49.015  ? 135 LEU   B CD1  1 ? 1 
ATOM   1795 C CD2  . LEU   A 1 123 ? 25.455 -12.527 -3.014  1   53.157  ? 135 LEU   B CD2  1 ? 1 
ATOM   1796 H H    . LEU   A 1 123 ? 26.666 -8.821  -3.192  1   44.68   ? 135 LEU   B H    1 c 1 
ATOM   1797 H HA   . LEU   A 1 123 ? 27.354 -11.009 -1.653  1   49.125  ? 135 LEU   B HA   1 c 1 
ATOM   1798 H HB2  . LEU   A 1 123 ? 27.818 -10.61  -4.448  1   48.043  ? 135 LEU   B HB2  1 c 1 
ATOM   1799 H HB3  . LEU   A 1 123 ? 28.005 -12.002 -3.694  1   50.627  ? 135 LEU   B HB3  1 c 1 
ATOM   1800 H HG   . LEU   A 1 123 ? 25.48  -10.723 -4.011  1   46.52   ? 135 LEU   B HG   1 c 1 
ATOM   1801 H HD11 . LEU   A 1 123 ? 26.419 -11.499 -6.107  1   48.745  ? 135 LEU   B HD11 1 c 1 
ATOM   1802 H HD12 . LEU   A 1 123 ? 25.011 -12.154 -5.781  1   48.376  ? 135 LEU   B HD12 1 c 1 
ATOM   1803 H HD13 . LEU   A 1 123 ? 26.344 -12.982 -5.547  1   51.258  ? 135 LEU   B HD13 1 c 1 
ATOM   1804 H HD21 . LEU   A 1 123 ? 25.303 -12.061 -2.175  1   50.973  ? 135 LEU   B HD21 1 c 1 
ATOM   1805 H HD22 . LEU   A 1 123 ? 26.085 -13.252 -2.87   1   54.067  ? 135 LEU   B HD22 1 c 1 
ATOM   1806 H HD23 . LEU   A 1 123 ? 24.614 -12.89  -3.339  1   51.942  ? 135 LEU   B HD23 1 c 1 
ATOM   1807 N N    . ASP   A 1 124 ? 29.634 -9.048  -2.88   1   45.817  ? 136 ASP   B N    1 ? 1 
ATOM   1808 C CA   . ASP   A 1 124 ? 31.056 -8.71   -2.885  1   50.407  ? 136 ASP   B CA   1 ? 1 
ATOM   1809 C C    . ASP   A 1 124 ? 31.258 -7.356  -3.575  1   50.838  ? 136 ASP   B C    1 ? 1 
ATOM   1810 O O    . ASP   A 1 124 ? 30.395 -6.895  -4.323  1   47.892  ? 136 ASP   B O    1 ? 1 
ATOM   1811 C CB   . ASP   A 1 124 ? 31.819 -9.83   -3.583  1   56.794  ? 136 ASP   B CB   1 ? 1 
ATOM   1812 C CG   . ASP   A 1 124 ? 33.304 -9.968  -3.357  1   63.058  ? 136 ASP   B CG   1 ? 1 
ATOM   1813 O OD1  . ASP   A 1 124 ? 33.861 -9.196  -2.521  1   63.679  ? 136 ASP   B OD1  1 ? 1 
ATOM   1814 O OD2  . ASP   A 1 124 ? 33.866 -10.88  -4.036  1   66.218  ? 136 ASP   B OD2  1 ? 1 
ATOM   1815 H H    . ASP   A 1 124 ? 29.059 -8.522  -3.358  1   45.95   ? 136 ASP   B H    1 c 1 
ATOM   1816 H HA   . ASP   A 1 124 ? 31.364 -8.643  -1.953  1   51.324  ? 136 ASP   B HA   1 c 1 
ATOM   1817 H HB2  . ASP   A 1 124 ? 31.418 -10.689 -3.34   1   57.282  ? 136 ASP   B HB2  1 c 1 
ATOM   1818 H HB3  . ASP   A 1 124 ? 31.686 -9.718  -4.548  1   56.384  ? 136 ASP   B HB3  1 c 1 
ATOM   1819 N N    . PHE   A 1 125 ? 32.435 -6.753  -3.348  1   57.978  ? 137 PHE   B N    1 ? 1 
ATOM   1820 C CA   . PHE   A 1 125 ? 32.92  -5.596  -4.095  1   56.207  ? 137 PHE   B CA   1 ? 1 
ATOM   1821 C C    . PHE   A 1 125 ? 34.45  -5.562  -4.099  1   59.038  ? 137 PHE   B C    1 ? 1 
ATOM   1822 O O    . PHE   A 1 125 ? 35.077 -5.935  -3.12   1   68.503  ? 137 PHE   B O    1 ? 1 
ATOM   1823 C CB   . PHE   A 1 125 ? 32.359 -4.314  -3.481  1   56.59   ? 137 PHE   B CB   1 ? 1 
ATOM   1824 C CG   . PHE   A 1 125 ? 32.634 -4.071  -2.003  1   56.222  ? 137 PHE   B CG   1 ? 1 
ATOM   1825 C CD1  . PHE   A 1 125 ? 31.768 -4.547  -1.021  1   54.519  ? 137 PHE   B CD1  1 ? 1 
ATOM   1826 C CD2  . PHE   A 1 125 ? 33.687 -3.249  -1.617  1   58.342  ? 137 PHE   B CD2  1 ? 1 
ATOM   1827 C CE1  . PHE   A 1 125 ? 31.999 -4.269  0.314   1   52.125  ? 137 PHE   B CE1  1 ? 1 
ATOM   1828 C CE2  . PHE   A 1 125 ? 33.923 -2.978  -0.273  1   54.181  ? 137 PHE   B CE2  1 ? 1 
ATOM   1829 C CZ   . PHE   A 1 125 ? 33.084 -3.486  0.684   1   55.476  ? 137 PHE   B CZ   1 ? 1 
ATOM   1830 H H    . PHE   A 1 125 ? 32.967 -7.086  -2.683  1   57.488  ? 137 PHE   B H    1 c 1 
ATOM   1831 H HA   . PHE   A 1 125 ? 32.598 -5.67   -5.03   1   56.424  ? 137 PHE   B HA   1 c 1 
ATOM   1832 H HB2  . PHE   A 1 125 ? 32.716 -3.553  -3.991  1   55.964  ? 137 PHE   B HB2  1 c 1 
ATOM   1833 H HB3  . PHE   A 1 125 ? 31.385 -4.315  -3.617  1   53.927  ? 137 PHE   B HB3  1 c 1 
ATOM   1834 H HD1  . PHE   A 1 125 ? 31.032 -5.084  -1.268  1   53.035  ? 137 PHE   B HD1  1 c 1 
ATOM   1835 H HD2  . PHE   A 1 125 ? 34.271 -2.902  -2.273  1   58.034  ? 137 PHE   B HD2  1 c 1 
ATOM   1836 H HE1  . PHE   A 1 125 ? 31.425 -4.625  0.975   1   52.648  ? 137 PHE   B HE1  1 c 1 
ATOM   1837 H HE2  . PHE   A 1 125 ? 34.66  -2.445  -0.021  1   57.174  ? 137 PHE   B HE2  1 c 1 
ATOM   1838 H HZ   . PHE   A 1 125 ? 33.243 -3.303  1.596   1   55.061  ? 137 PHE   B HZ   1 c 1 
ATOM   1839 N N    . LYS   A 1 126 ? 35.051 -5.138  -5.216  1   64.869  ? 138 LYS   B N    1 ? 1 
ATOM   1840 C CA   . LYS   A 1 126 ? 36.506 -5.071  -5.374  1   64.934  ? 138 LYS   B CA   1 ? 1 
ATOM   1841 C C    . LYS   A 1 126 ? 36.844 -3.656  -5.852  1   62.814  ? 138 LYS   B C    1 ? 1 
ATOM   1842 O O    . LYS   A 1 126 ? 36.073 -3.069  -6.586  1   53.798  ? 138 LYS   B O    1 ? 1 
ATOM   1843 C CB   . LYS   A 1 126 ? 37.026 -6.132  -6.365  1   61.337  ? 138 LYS   B CB   1 ? 1 
ATOM   1844 H H    . LYS   A 1 126 ? 34.529 -4.876  -5.919  1   61.68   ? 138 LYS   B H    1 c 1 
ATOM   1845 H HA   . LYS   A 1 126 ? 36.93  -5.217  -4.491  1   64.96   ? 138 LYS   B HA   1 c 1 
ATOM   1846 H HB2  . LYS   A 1 126 ? 38.06  -6.007  -6.374  0   30      ? 138 LYS   B HB2  1 c 1 
ATOM   1847 H HB3  . LYS   A 1 126 ? 36.334 -6.494  -6.864  0   30      ? 138 LYS   B HB3  1 c 1 
ATOM   1848 N N    . GLY   A 1 127 ? 38.01  -3.124  -5.464  1   68.228  ? 139 GLY   B N    1 ? 1 
ATOM   1849 C CA   . GLY   A 1 127 ? 38.373 -1.749  -5.794  1   68.898  ? 139 GLY   B CA   1 ? 1 
ATOM   1850 C C    . GLY   A 1 127 ? 38.679 -1.627  -7.281  1   74.768  ? 139 GLY   B C    1 ? 1 
ATOM   1851 O O    . GLY   A 1 127 ? 39.148 -2.596  -7.865  1   73.466  ? 139 GLY   B O    1 ? 1 
ATOM   1852 H H    . GLY   A 1 127 ? 38.597 -3.631  -4.98   1   69.36   ? 139 GLY   B H    1 c 1 
ATOM   1853 H HA2  . GLY   A 1 127 ? 37.629 -1.149  -5.556  1   67.352  ? 139 GLY   B HA2  1 c 1 
ATOM   1854 H HA3  . GLY   A 1 127 ? 39.163 -1.484  -5.267  1   71.71   ? 139 GLY   B HA3  1 c 1 
ATOM   1855 N N    . GLU   A 1 128 ? 38.407 -0.473  -7.905  1   78.046  ? 140 GLU   B N    1 ? 1 
ATOM   1856 C CA   . GLU   A 1 128 ? 39.021 -0.207  -9.201  1   76.376  ? 140 GLU   B CA   1 ? 1 
ATOM   1857 C C    . GLU   A 1 128 ? 40.497 -0.632  -9.045  1   81.216  ? 140 GLU   B C    1 ? 1 
ATOM   1858 O O    . GLU   A 1 128 ? 41.052 -0.447  -7.932  1   82.984  ? 140 GLU   B O    1 ? 1 
ATOM   1859 C CB   . GLU   A 1 128 ? 38.763 1.209   -9.732  1   74.867  ? 140 GLU   B CB   1 ? 1 
ATOM   1860 O OXT  . GLU   A 1 128 ? 41.002 -1.257  -9.983  1   78.161  ? 140 GLU   B OXT  1 ? 1 
ATOM   1861 H H    . GLU   A 1 128 ? 37.845 0.142   -7.53   1   74.119  ? 140 GLU   B H    1 c 1 
ATOM   1862 H HA   . GLU   A 1 128 ? 38.605 -0.826  -9.854  1   76.439  ? 140 GLU   B HA   1 c 1 
ATOM   1863 H HB2  . GLU   A 1 128 ? 39.605 1.66    -9.871  0   30      ? 140 GLU   B HB2  1 c 1 
ATOM   1864 H HB3  . GLU   A 1 128 ? 37.776 1.359   -9.76   0   30      ? 140 GLU   B HB3  1 c 1 
ATOM   1865 N N    . GLY   B 1 1   ? -5.105 20.651  -38.621 1   49.218  ? 13  GLY   A N    1 ? 2 
ATOM   1866 C CA   . GLY   B 1 1   ? -3.931 21.49   -38.35  1   49.908  ? 13  GLY   A CA   1 ? 2 
ATOM   1867 C C    . GLY   B 1 1   ? -2.64  20.682  -38.337 1   49.818  ? 13  GLY   A C    1 ? 2 
ATOM   1868 O O    . GLY   B 1 1   ? -2.528 19.63   -38.988 1   43.888  ? 13  GLY   A O    1 ? 2 
ATOM   1869 H H1   . GLY   B 1 1   ? -5.859 21.15   -38.576 1   51.751  ? 13  GLY   A H1   1 c 2 
ATOM   1870 H H2   . GLY   B 1 1   ? -5.158 19.984  -38.011 1   47.995  ? 13  GLY   A H2   1 c 2 
ATOM   1871 H H3   . GLY   B 1 1   ? -5.042 20.288  -39.448 1   50.569  ? 13  GLY   A H3   1 c 2 
ATOM   1872 H HA2  . GLY   B 1 1   ? -3.87  22.186  -39.043 1   52.238  ? 13  GLY   A HA2  1 c 2 
ATOM   1873 H HA3  . GLY   B 1 1   ? -4.05  21.937  -37.479 1   49.645  ? 13  GLY   A HA3  1 c 2 
ATOM   1874 N N    . ALA   B 1 2   ? -1.659 21.191  -37.594 1   49.886  ? 14  ALA   A N    1 ? 2 
ATOM   1875 C CA   . ALA   B 1 2   ? -0.314 20.652  -37.766 1   43.641  ? 14  ALA   A CA   1 ? 2 
ATOM   1876 C C    . ALA   B 1 2   ? -0.275 19.171  -37.355 1   42.943  ? 14  ALA   A C    1 ? 2 
ATOM   1877 O O    . ALA   B 1 2   ? 0.316  18.356  -38.06  1   44.813  ? 14  ALA   A O    1 ? 2 
ATOM   1878 C CB   . ALA   B 1 2   ? 0.674  21.464  -36.977 1   44.411  ? 14  ALA   A CB   1 ? 2 
ATOM   1879 H H    . ALA   B 1 2   ? -1.814 21.861  -36.991 1   48.763  ? 14  ALA   A H    1 c 2 
ATOM   1880 H HA   . ALA   B 1 2   ? -0.079 20.71   -38.733 1   46.357  ? 14  ALA   A HA   1 c 2 
ATOM   1881 H HB1  . ALA   B 1 2   ? 0.754  22.35   -37.368 1   45.675  ? 14  ALA   A HB1  1 c 2 
ATOM   1882 H HB2  . ALA   B 1 2   ? 0.373  21.547  -36.058 1   43.115  ? 14  ALA   A HB2  1 c 2 
ATOM   1883 H HB3  . ALA   B 1 2   ? 1.542  21.027  -36.992 1   42.428  ? 14  ALA   A HB3  1 c 2 
ATOM   1884 N N    . PRO   B 1 3   ? -0.903 18.747  -36.253 1   40.182  ? 15  PRO   A N    1 ? 2 
ATOM   1885 C CA   . PRO   B 1 3   ? -0.99  17.333  -35.925 1   38.348  ? 15  PRO   A CA   1 ? 2 
ATOM   1886 C C    . PRO   B 1 3   ? -1.558 16.446  -37.038 1   39.934  ? 15  PRO   A C    1 ? 2 
ATOM   1887 O O    . PRO   B 1 3   ? -0.897 15.473  -37.461 1   38.415  ? 15  PRO   A O    1 ? 2 
ATOM   1888 C CB   . PRO   B 1 3   ? -1.778 17.283  -34.616 1   40.764  ? 15  PRO   A CB   1 ? 2 
ATOM   1889 C CG   . PRO   B 1 3   ? -1.619 18.699  -34.041 1   41.964  ? 15  PRO   A CG   1 ? 2 
ATOM   1890 C CD   . PRO   B 1 3   ? -1.577 19.582  -35.244 1   46.259  ? 15  PRO   A CD   1 ? 2 
ATOM   1891 H HA   . PRO   B 1 3   ? -0.066 17.031  -35.735 1   37.437  ? 15  PRO   A HA   1 c 2 
ATOM   1892 H HB2  . PRO   B 1 3   ? -2.728 17.075  -34.783 1   41.422  ? 15  PRO   A HB2  1 c 2 
ATOM   1893 H HB3  . PRO   B 1 3   ? -1.403 16.609  -34.003 1   38.59   ? 15  PRO   A HB3  1 c 2 
ATOM   1894 H HG2  . PRO   B 1 3   ? -2.378 18.93   -33.465 1   42.991  ? 15  PRO   A HG2  1 c 2 
ATOM   1895 H HG3  . PRO   B 1 3   ? -0.791 18.775  -33.523 1   40.871  ? 15  PRO   A HG3  1 c 2 
ATOM   1896 H HD2  . PRO   B 1 3   ? -2.484 19.826  -35.532 1   46.28   ? 15  PRO   A HD2  1 c 2 
ATOM   1897 H HD3  . PRO   B 1 3   ? -1.068 20.4    -35.058 1   44.548  ? 15  PRO   A HD3  1 c 2 
ATOM   1898 N N    . ALA   B 1 4   ? -2.634 16.901  -37.679 1   42.771  ? 16  ALA   A N    1 ? 2 
ATOM   1899 C CA   . ALA   B 1 4   ? -3.256 16.075  -38.702 1   43.643  ? 16  ALA   A CA   1 ? 2 
ATOM   1900 C C    . ALA   B 1 4   ? -2.329 15.95   -39.902 1   46.184  ? 16  ALA   A C    1 ? 2 
ATOM   1901 O O    . ALA   B 1 4   ? -2.365 14.946  -40.591 1   42.93   ? 16  ALA   A O    1 ? 2 
ATOM   1902 C CB   . ALA   B 1 4   ? -4.577 16.669  -39.146 1   47.417  ? 16  ALA   A CB   1 ? 2 
ATOM   1903 H H    . ALA   B 1 4   ? -2.987 17.72   -37.481 1   43.454  ? 16  ALA   A H    1 c 2 
ATOM   1904 H HA   . ALA   B 1 4   ? -3.412 15.165  -38.325 1   43.283  ? 16  ALA   A HA   1 c 2 
ATOM   1905 H HB1  . ALA   B 1 4   ? -5.178 16.736  -38.385 1   47.049  ? 16  ALA   A HB1  1 c 2 
ATOM   1906 H HB2  . ALA   B 1 4   ? -4.429 17.556  -39.516 1   48.444  ? 16  ALA   A HB2  1 c 2 
ATOM   1907 H HB3  . ALA   B 1 4   ? -4.979 16.102  -39.824 1   48.636  ? 16  ALA   A HB3  1 c 2 
ATOM   1908 N N    . THR   B 1 5   ? -1.616 17.034  -40.218 1   45.186  ? 17  THR   A N    1 ? 2 
ATOM   1909 C CA   . THR   B 1 5   ? -0.706 17.03   -41.339 1   47.106  ? 17  THR   A CA   1 ? 2 
ATOM   1910 C C    . THR   B 1 5   ? 0.392  15.991  -41.046 1   43.327  ? 17  THR   A C    1 ? 2 
ATOM   1911 O O    . THR   B 1 5   ? 0.844  15.303  -41.953 1   42.003  ? 17  THR   A O    1 ? 2 
ATOM   1912 C CB   . THR   B 1 5   ? -0.081 18.415  -41.579 1   49.178  ? 17  THR   A CB   1 ? 2 
ATOM   1913 O OG1  . THR   B 1 5   ? -1.153 19.3    -41.856 1   50.157  ? 17  THR   A OG1  1 ? 2 
ATOM   1914 C CG2  . THR   B 1 5   ? 0.919  18.411  -42.732 1   50.286  ? 17  THR   A CG2  1 ? 2 
ATOM   1915 H H    . THR   B 1 5   ? -1.707 17.798  -39.726 1   45.663  ? 17  THR   A H    1 c 2 
ATOM   1916 H HA   . THR   B 1 5   ? -1.198 16.759  -42.144 1   48.873  ? 17  THR   A HA   1 c 2 
ATOM   1917 H HB   . THR   B 1 5   ? 0.38   18.712  -40.758 1   46.785  ? 17  THR   A HB   1 c 2 
ATOM   1918 H HG1  . THR   B 1 5   ? -1.574 19.011  -42.553 0   30      ? 17  THR   A HG1  1 c 2 
ATOM   1919 H HG21 . THR   B 1 5   ? 1.049  19.32   -43.052 1   51.958  ? 17  THR   A HG21 1 c 2 
ATOM   1920 H HG22 . THR   B 1 5   ? 0.577  17.86   -43.456 1   51.776  ? 17  THR   A HG22 1 c 2 
ATOM   1921 H HG23 . THR   B 1 5   ? 1.768  18.052  -42.426 1   48.541  ? 17  THR   A HG23 1 c 2 
ATOM   1922 N N    . VAL   B 1 6   ? 0.846  15.881  -39.811 1   41.439  ? 18  VAL   A N    1 ? 2 
ATOM   1923 C CA   . VAL   B 1 6   ? 1.84   14.862  -39.484 1   36.254  ? 18  VAL   A CA   1 ? 2 
ATOM   1924 C C    . VAL   B 1 6   ? 1.254  13.455  -39.611 1   36.514  ? 18  VAL   A C    1 ? 2 
ATOM   1925 O O    . VAL   B 1 6   ? 1.884  12.611  -40.194 1   37.207  ? 18  VAL   A O    1 ? 2 
ATOM   1926 C CB   . VAL   B 1 6   ? 2.467  15.003  -38.098 1   34.846  ? 18  VAL   A CB   1 ? 2 
ATOM   1927 C CG1  . VAL   B 1 6   ? 3.524  13.926  -37.878 1   31.969  ? 18  VAL   A CG1  1 ? 2 
ATOM   1928 C CG2  . VAL   B 1 6   ? 3.069  16.38   -37.914 1   31.238  ? 18  VAL   A CG2  1 ? 2 
ATOM   1929 H H    . VAL   B 1 6   ? 0.542  16.44   -39.155 1   39.995  ? 18  VAL   A H    1 c 2 
ATOM   1930 H HA   . VAL   B 1 6   ? 2.561  14.94   -40.137 1   37.723  ? 18  VAL   A HA   1 c 2 
ATOM   1931 H HB   . VAL   B 1 6   ? 1.749  14.88   -37.433 1   33.16   ? 18  VAL   A HB   1 c 2 
ATOM   1932 H HG11 . VAL   B 1 6   ? 4.017  13.78   -38.703 1   33.301  ? 18  VAL   A HG11 1 c 2 
ATOM   1933 H HG12 . VAL   B 1 6   ? 3.094  13.097  -37.607 1   32.006  ? 18  VAL   A HG12 1 c 2 
ATOM   1934 H HG13 . VAL   B 1 6   ? 4.14   14.211  -37.182 1   31.132  ? 18  VAL   A HG13 1 c 2 
ATOM   1935 H HG21 . VAL   B 1 6   ? 3.565  16.41   -37.078 1   30.826  ? 18  VAL   A HG21 1 c 2 
ATOM   1936 H HG22 . VAL   B 1 6   ? 2.362  17.044  -37.891 1   33.334  ? 18  VAL   A HG22 1 c 2 
ATOM   1937 H HG23 . VAL   B 1 6   ? 3.67   16.573  -38.653 1   33.162  ? 18  VAL   A HG23 1 c 2 
ATOM   1938 N N    . THR   B 1 7   ? 0.036  13.208  -39.135 1   38.494  ? 19  THR   A N    1 ? 2 
ATOM   1939 C CA   . THR   B 1 7   ? -0.632 11.943  -39.394 1   41.917  ? 19  THR   A CA   1 ? 2 
ATOM   1940 C C    . THR   B 1 7   ? -0.638 11.681  -40.906 1   49.529  ? 19  THR   A C    1 ? 2 
ATOM   1941 O O    . THR   B 1 7   ? -0.271 10.588  -41.311 1   49.22   ? 19  THR   A O    1 ? 2 
ATOM   1942 C CB   . THR   B 1 7   ? -2.067 12.001  -38.887 1   46.557  ? 19  THR   A CB   1 ? 2 
ATOM   1943 O OG1  . THR   B 1 7   ? -2.055 12.121  -37.489 1   38.281  ? 19  THR   A OG1  1 ? 2 
ATOM   1944 C CG2  . THR   B 1 7   ? -2.875 10.759  -39.226 1   54.002  ? 19  THR   A CG2  1 ? 2 
ATOM   1945 H H    . THR   B 1 7   ? -0.391 13.841  -38.633 1   38.487  ? 19  THR   A H    1 c 2 
ATOM   1946 H HA   . THR   B 1 7   ? -0.15  11.221  -38.935 1   41.587  ? 19  THR   A HA   1 c 2 
ATOM   1947 H HB   . THR   B 1 7   ? -2.52  12.787  -39.275 1   46.769  ? 19  THR   A HB   1 c 2 
ATOM   1948 H HG1  . THR   B 1 7   ? -1.632 11.534  -37.112 0   30      ? 19  THR   A HG1  1 c 2 
ATOM   1949 H HG21 . THR   B 1 7   ? -3.607 10.665  -38.593 1   52.027  ? 19  THR   A HG21 1 c 2 
ATOM   1950 H HG22 . THR   B 1 7   ? -2.302 9.975   -39.176 1   51.302  ? 19  THR   A HG22 1 c 2 
ATOM   1951 H HG23 . THR   B 1 7   ? -3.235 10.84   -40.125 1   54.118  ? 19  THR   A HG23 1 c 2 
ATOM   1952 N N    . GLU   B 1 8   ? -0.931 12.718  -41.734 1   50.854  ? 20  GLU   A N    1 ? 2 
ATOM   1953 C CA   . GLU   B 1 8   ? -1.091 12.569  -43.172 1   57.361  ? 20  GLU   A CA   1 ? 2 
ATOM   1954 C C    . GLU   B 1 8   ? 0.254  12.453  -43.931 1   56.249  ? 20  GLU   A C    1 ? 2 
ATOM   1955 O O    . GLU   B 1 8   ? 0.278  11.957  -45.055 1   61.631  ? 20  GLU   A O    1 ? 2 
ATOM   1956 C CB   . GLU   B 1 8   ? -1.974 13.714  -43.724 1   59.622  ? 20  GLU   A CB   1 ? 2 
ATOM   1957 H H    . GLU   B 1 8   ? -1.041 13.549  -41.37  1   51.221  ? 20  GLU   A H    1 c 2 
ATOM   1958 H HA   . GLU   B 1 8   ? -1.58  11.729  -43.325 1   57.123  ? 20  GLU   A HA   1 c 2 
ATOM   1959 H HB2  . GLU   B 1 8   ? -1.359 14.43   -44.08  0   30      ? 20  GLU   A HB2  1 c 2 
ATOM   1960 H HB3  . GLU   B 1 8   ? -2.907 13.507  -43.634 0   30      ? 20  GLU   A HB3  1 c 2 
ATOM   1961 N N    . GLN   B 1 9   ? 1.299  13.152  -43.503 1   49.534  ? 21  GLN   A N    1 ? 2 
ATOM   1962 C CA   . GLN   B 1 9   ? 2.492  13.324  -44.313 1   51.514  ? 21  GLN   A CA   1 ? 2 
ATOM   1963 C C    . GLN   B 1 9   ? 3.755  12.857  -43.577 1   45.232  ? 21  GLN   A C    1 ? 2 
ATOM   1964 O O    . GLN   B 1 9   ? 4.793  12.779  -44.214 1   49.932  ? 21  GLN   A O    1 ? 2 
ATOM   1965 C CB   . GLN   B 1 9   ? 2.731  14.748  -44.831 1   53.86   ? 21  GLN   A CB   1 ? 2 
ATOM   1966 H H    . GLN   B 1 9   ? 1.259  13.559  -42.686 1   49.217  ? 21  GLN   A H    1 c 2 
ATOM   1967 H HA   . GLN   B 1 9   ? 2.396  12.751  -45.115 1   52.67   ? 21  GLN   A HA   1 c 2 
ATOM   1968 H HB2  . GLN   B 1 9   ? 3.677  14.912  -44.907 0   30      ? 21  GLN   A HB2  1 c 2 
ATOM   1969 H HB3  . GLN   B 1 9   ? 1.84   15.166  -45.001 0   30      ? 21  GLN   A HB3  1 c 2 
ATOM   1970 N N    . GLY   B 1 10  ? 3.675  12.563  -42.278 1   43.275  ? 22  GLY   A N    1 ? 2 
ATOM   1971 C CA   . GLY   B 1 10  ? 4.87   12.386  -41.455 1   43.61   ? 22  GLY   A CA   1 ? 2 
ATOM   1972 C C    . GLY   B 1 10  ? 5.629  11.1    -41.827 1   40.798  ? 22  GLY   A C    1 ? 2 
ATOM   1973 O O    . GLY   B 1 10  ? 4.979  10.128  -42.125 1   41.741  ? 22  GLY   A O    1 ? 2 
ATOM   1974 H H    . GLY   B 1 10  ? 2.856  12.454  -41.887 1   43.365  ? 22  GLY   A H    1 c 2 
ATOM   1975 H HA2  . GLY   B 1 10  ? 5.461  13.165  -41.576 1   42.283  ? 22  GLY   A HA2  1 c 2 
ATOM   1976 H HA3  . GLY   B 1 10  ? 4.606  12.349  -40.506 1   40.518  ? 22  GLY   A HA3  1 c 2 
ATOM   1977 N N    . GLU   B 1 11  ? 6.966  11.126  -41.778 1   38.249  ? 23  GLU   A N    1 ? 2 
ATOM   1978 C CA   . GLU   B 1 11  ? 7.836  9.966   -41.918 1   38.934  ? 23  GLU   A CA   1 ? 2 
ATOM   1979 C C    . GLU   B 1 11  ? 7.825  9.194   -40.588 1   35.24   ? 23  GLU   A C    1 ? 2 
ATOM   1980 O O    . GLU   B 1 11  ? 7.902  9.791   -39.503 1   30.818  ? 23  GLU   A O    1 ? 2 
ATOM   1981 C CB   . GLU   B 1 11  ? 9.277  10.318  -42.353 1   41.478  ? 23  GLU   A CB   1 ? 2 
ATOM   1982 H H    . GLU   B 1 11  ? 7.365  11.938  -41.642 1   38.522  ? 23  GLU   A H    1 c 2 
ATOM   1983 H HA   . GLU   B 1 11  ? 7.449  9.382   -42.618 1   40.484  ? 23  GLU   A HA   1 c 2 
ATOM   1984 H HB2  . GLU   B 1 11  ? 9.891  9.846   -41.795 0   30      ? 23  GLU   A HB2  1 c 2 
ATOM   1985 H HB3  . GLU   B 1 11  ? 9.195  10.924  -43.137 0   30      ? 23  GLU   A HB3  1 c 2 
ATOM   1986 N N    . ASP   B 1 12  ? 7.667  7.877   -40.694 1   33.678  ? 24  ASP   A N    1 ? 2 
ATOM   1987 C CA   . ASP   B 1 12  ? 7.705  7       -39.531 1   32.001  ? 24  ASP   A CA   1 ? 2 
ATOM   1988 C C    . ASP   B 1 12  ? 9.149  6.696   -39.14  1   31.039  ? 24  ASP   A C    1 ? 2 
ATOM   1989 O O    . ASP   B 1 12  ? 9.856  6.067   -39.925 1   33.005  ? 24  ASP   A O    1 ? 2 
ATOM   1990 C CB   . ASP   B 1 12  ? 6.925  5.718   -39.827 1   32.47   ? 24  ASP   A CB   1 ? 2 
ATOM   1991 C CG   . ASP   B 1 12  ? 6.941  4.705   -38.671 1   31.494  ? 24  ASP   A CG   1 ? 2 
ATOM   1992 O OD1  . ASP   B 1 12  ? 7.616  4.976   -37.608 1   30.686  ? 24  ASP   A OD1  1 ? 2 
ATOM   1993 O OD2  . ASP   B 1 12  ? 6.296  3.657   -38.839 1   33.565  ? 24  ASP   A OD2  1 ? 2 
ATOM   1994 H H    . ASP   B 1 12  ? 7.531  7.507   -41.519 1   35.935  ? 24  ASP   A H    1 c 2 
ATOM   1995 H HA   . ASP   B 1 12  ? 7.265  7.457   -38.781 1   30.337  ? 24  ASP   A HA   1 c 2 
ATOM   1996 H HB2  . ASP   B 1 12  ? 5.993  5.95    -40.023 1   32.954  ? 24  ASP   A HB2  1 c 2 
ATOM   1997 H HB3  . ASP   B 1 12  ? 7.306  5.289   -40.621 1   34.385  ? 24  ASP   A HB3  1 c 2 
ATOM   1998 N N    . ILE   B 1 13  ? 9.642  7.258   -38.041 1   32.106  ? 25  ILE   A N    1 ? 2 
ATOM   1999 C CA   . ILE   B 1 13  ? 11.087 7.184   -37.741 1   32.087  ? 25  ILE   A CA   1 ? 2 
ATOM   2000 C C    . ILE   B 1 13  ? 11.338 6.154   -36.633 1   33.33   ? 25  ILE   A C    1 ? 2 
ATOM   2001 O O    . ILE   B 1 13  ? 12.491 6.057   -36.206 1   37.214  ? 25  ILE   A O    1 ? 2 
ATOM   2002 C CB   . ILE   B 1 13  ? 11.657 8.572   -37.347 1   28.057  ? 25  ILE   A CB   1 ? 2 
ATOM   2003 C CG1  . ILE   B 1 13  ? 10.929 9.137   -36.191 1   29.027  ? 25  ILE   A CG1  1 ? 2 
ATOM   2004 C CG2  . ILE   B 1 13  ? 11.647 9.569   -38.535 1   32.914  ? 25  ILE   A CG2  1 ? 2 
ATOM   2005 C CD1  . ILE   B 1 13  ? 11.611 10.314  -35.486 1   28.655  ? 25  ILE   A CD1  1 ? 2 
ATOM   2006 H H    . ILE   B 1 13  ? 9.084  7.682   -37.456 1   30.123  ? 25  ILE   A H    1 c 2 
ATOM   2007 H HA   . ILE   B 1 13  ? 11.553 6.886   -38.545 1   33.333  ? 25  ILE   A HA   1 c 2 
ATOM   2008 H HB   . ILE   B 1 13  ? 12.588 8.445   -37.075 1   29.996  ? 25  ILE   A HB   1 c 2 
ATOM   2009 H HG12 . ILE   B 1 13  ? 10.048 9.433   -36.498 1   28.372  ? 25  ILE   A HG12 1 c 2 
ATOM   2010 H HG13 . ILE   B 1 13  ? 10.787 8.426   -35.534 1   28.023  ? 25  ILE   A HG13 1 c 2 
ATOM   2011 H HG21 . ILE   B 1 13  ? 12.135 10.373  -38.291 1   31.371  ? 25  ILE   A HG21 1 c 2 
ATOM   2012 H HG22 . ILE   B 1 13  ? 10.729 9.803   -38.755 1   31.657  ? 25  ILE   A HG22 1 c 2 
ATOM   2013 H HG23 . ILE   B 1 13  ? 12.069 9.158   -39.308 1   33.289  ? 25  ILE   A HG23 1 c 2 
ATOM   2014 H HD11 . ILE   B 1 13  ? 12.545 10.092  -35.315 1   28.861  ? 25  ILE   A HD11 1 c 2 
ATOM   2015 H HD12 . ILE   B 1 13  ? 11.161 10.496  -34.64  1   27.443  ? 25  ILE   A HD12 1 c 2 
ATOM   2016 H HD13 . ILE   B 1 13  ? 11.565 11.106  -36.054 1   28.896  ? 25  ILE   A HD13 1 c 2 
ATOM   2017 N N    . THR   B 1 14  ? 10.357 5.273   -36.353 1   32.809  ? 26  THR   A N    1 ? 2 
ATOM   2018 C CA   . THR   B 1 14  ? 10.554 4.105   -35.51  1   34.343  ? 26  THR   A CA   1 ? 2 
ATOM   2019 C C    . THR   B 1 14  ? 11.257 2.981   -36.264 1   36.047  ? 26  THR   A C    1 ? 2 
ATOM   2020 O O    . THR   B 1 14  ? 11.075 2.803   -37.497 1   35.067  ? 26  THR   A O    1 ? 2 
ATOM   2021 C CB   . THR   B 1 14  ? 9.234  3.599   -34.907 1   32.172  ? 26  THR   A CB   1 ? 2 
ATOM   2022 O OG1  . THR   B 1 14  ? 8.373  3.047   -35.917 1   34.142  ? 26  THR   A OG1  1 ? 2 
ATOM   2023 C CG2  . THR   B 1 14  ? 8.546  4.666   -34.091 1   31.159  ? 26  THR   A CG2  1 ? 2 
ATOM   2024 H H    . THR   B 1 14  ? 9.525  5.413   -36.704 1   33.174  ? 26  THR   A H    1 c 2 
ATOM   2025 H HA   . THR   B 1 14  ? 11.133 4.377   -34.766 1   32.991  ? 26  THR   A HA   1 c 2 
ATOM   2026 H HB   . THR   B 1 14  ? 9.462  2.875   -34.276 1   33.304  ? 26  THR   A HB   1 c 2 
ATOM   2027 H HG1  . THR   B 1 14  ? 8.189  3.673   -36.513 0   30      ? 26  THR   A HG1  1 c 2 
ATOM   2028 H HG21 . THR   B 1 14  ? 7.731  4.307   -33.705 1   30.847  ? 26  THR   A HG21 1 c 2 
ATOM   2029 H HG22 . THR   B 1 14  ? 8.328  5.421   -34.661 1   30.498  ? 26  THR   A HG22 1 c 2 
ATOM   2030 H HG23 . THR   B 1 14  ? 9.138  4.961   -33.378 1   30.086  ? 26  THR   A HG23 1 c 2 
ATOM   2031 N N    . SER   B 1 15  ? 12.043 2.187   -35.497 1   39.414  ? 27  SER   A N    1 ? 2 
ATOM   2032 C CA   . SER   B 1 15  ? 12.719 1.01    -36.033 1   41.073  ? 27  SER   A CA   1 ? 2 
ATOM   2033 C C    . SER   B 1 15  ? 11.697 -0.062  -36.369 1   43.064  ? 27  SER   A C    1 ? 2 
ATOM   2034 O O    . SER   B 1 15  ? 11.851 -0.809  -37.366 1   45.466  ? 27  SER   A O    1 ? 2 
ATOM   2035 C CB   . SER   B 1 15  ? 13.773 0.477   -35.029 1   42.618  ? 27  SER   A CB   1 ? 2 
ATOM   2036 O OG   . SER   B 1 15  ? 14.711 1.525   -34.772 1   46.023  ? 27  SER   A OG   1 ? 2 
ATOM   2037 H H    . SER   B 1 15  ? 12.154 2.391   -34.612 1   37.457  ? 27  SER   A H    1 c 2 
ATOM   2038 H HA   . SER   B 1 15  ? 13.183 1.272   -36.869 1   42.287  ? 27  SER   A HA   1 c 2 
ATOM   2039 H HB2  . SER   B 1 15  ? 13.336 0.209   -34.199 1   42.898  ? 27  SER   A HB2  1 c 2 
ATOM   2040 H HB3  . SER   B 1 15  ? 14.233 -0.295  -35.411 1   45.57   ? 27  SER   A HB3  1 c 2 
ATOM   2041 H HG   . SER   B 1 15  ? 15.263 1.199   -34.229 0   30      ? 27  SER   A HG   1 c 2 
ATOM   2042 N N    . LYS   B 1 16  ? 10.681 -0.18   -35.496 1   38.946  ? 28  LYS   A N    1 ? 2 
ATOM   2043 C CA   . LYS   B 1 16  ? 9.684  -1.216  -35.683 1   44.973  ? 28  LYS   A CA   1 ? 2 
ATOM   2044 C C    . LYS   B 1 16  ? 8.696  -0.828  -36.783 1   42.318  ? 28  LYS   A C    1 ? 2 
ATOM   2045 O O    . LYS   B 1 16  ? 7.866  -1.624  -37.125 1   41.204  ? 28  LYS   A O    1 ? 2 
ATOM   2046 C CB   . LYS   B 1 16  ? 8.826  -1.433  -34.439 1   49.358  ? 28  LYS   A CB   1 ? 2 
ATOM   2047 C CG   . LYS   B 1 16  ? 9.513  -1.891  -33.155 1   53.618  ? 28  LYS   A CG   1 ? 2 
ATOM   2048 C CD   . LYS   B 1 16  ? 8.404  -2.496  -32.293 1   67.488  ? 28  LYS   A CD   1 ? 2 
ATOM   2049 C CE   . LYS   B 1 16  ? 8.249  -1.955  -30.874 1   68.842  ? 28  LYS   A CE   1 ? 2 
ATOM   2050 N NZ   . LYS   B 1 16  ? 9.027  -2.763  -29.931 1   74.143  ? 28  LYS   A NZ   1 ? 2 
ATOM   2051 H H    . LYS   B 1 16  ? 10.615 0.382   -34.778 1   38.922  ? 28  LYS   A H    1 c 2 
ATOM   2052 H HA   . LYS   B 1 16  ? 10.138 -2.062  -35.931 1   46.465  ? 28  LYS   A HA   1 c 2 
ATOM   2053 H HB2  . LYS   B 1 16  ? 8.36   -0.591  -34.245 1   46.981  ? 28  LYS   A HB2  1 c 2 
ATOM   2054 H HB3  . LYS   B 1 16  ? 8.14   -2.097  -34.666 1   50.309  ? 28  LYS   A HB3  1 c 2 
ATOM   2055 H HG2  . LYS   B 1 16  ? 10.194 -2.567  -33.361 1   57.041  ? 28  LYS   A HG2  1 c 2 
ATOM   2056 H HG3  . LYS   B 1 16  ? 9.923  -1.127  -32.7   1   53.689  ? 28  LYS   A HG3  1 c 2 
ATOM   2057 H HD2  . LYS   B 1 16  ? 7.548  -2.378  -32.759 1   64.208  ? 28  LYS   A HD2  1 c 2 
ATOM   2058 H HD3  . LYS   B 1 16  ? 8.561  -3.464  -32.24  1   66.787  ? 28  LYS   A HD3  1 c 2 
ATOM   2059 H HE2  . LYS   B 1 16  ? 8.555  -1.032  -30.834 1   67.041  ? 28  LYS   A HE2  1 c 2 
ATOM   2060 H HE3  . LYS   B 1 16  ? 7.31   -1.979  -30.615 1   68.778  ? 28  LYS   A HE3  1 c 2 
ATOM   2061 H HZ1  . LYS   B 1 16  ? 9.886  -2.824  -30.215 1   73.446  ? 28  LYS   A HZ1  1 c 2 
ATOM   2062 H HZ2  . LYS   B 1 16  ? 8.673  -3.595  -29.873 1   74.703  ? 28  LYS   A HZ2  1 c 2 
ATOM   2063 H HZ3  . LYS   B 1 16  ? 9.012  -2.376  -29.112 1   72.072  ? 28  LYS   A HZ3  1 c 2 
ATOM   2064 N N    . LYS   B 1 17  ? 8.715  0.435   -37.268 1   40.731  ? 29  LYS   A N    1 ? 2 
ATOM   2065 C CA   . LYS   B 1 17  ? 7.764  0.862   -38.301 1   43.344  ? 29  LYS   A CA   1 ? 2 
ATOM   2066 C C    . LYS   B 1 17  ? 6.307  0.662   -37.846 1   43.134  ? 29  LYS   A C    1 ? 2 
ATOM   2067 O O    . LYS   B 1 17  ? 5.46   0.166   -38.574 1   44.113  ? 29  LYS   A O    1 ? 2 
ATOM   2068 C CB   . LYS   B 1 17  ? 8.046  0.148   -39.621 1   46.099  ? 29  LYS   A CB   1 ? 2 
ATOM   2069 C CG   . LYS   B 1 17  ? 9.429  0.399   -40.214 1   47.663  ? 29  LYS   A CG   1 ? 2 
ATOM   2070 C CD   . LYS   B 1 17  ? 9.677  1.86    -40.597 1   49.397  ? 29  LYS   A CD   1 ? 2 
ATOM   2071 C CE   . LYS   B 1 17  ? 10.405 1.726   -41.927 1   56.314  ? 29  LYS   A CE   1 ? 2 
ATOM   2072 N NZ   . LYS   B 1 17  ? 11.222 2.902   -42.122 1   57.411  ? 29  LYS   A NZ   1 ? 2 
ATOM   2073 H H    . LYS   B 1 17  ? 9.316  1.041   -36.945 1   39.895  ? 29  LYS   A H    1 c 2 
ATOM   2074 H HA   . LYS   B 1 17  ? 7.904  1.83    -38.451 1   41.574  ? 29  LYS   A HA   1 c 2 
ATOM   2075 H HB2  . LYS   B 1 17  ? 7.937  -0.818  -39.49  1   47.811  ? 29  LYS   A HB2  1 c 2 
ATOM   2076 H HB3  . LYS   B 1 17  ? 7.376  0.434   -40.278 1   46.909  ? 29  LYS   A HB3  1 c 2 
ATOM   2077 H HG2  . LYS   B 1 17  ? 10.106 0.121   -39.56  1   47.814  ? 29  LYS   A HG2  1 c 2 
ATOM   2078 H HG3  . LYS   B 1 17  ? 9.53   -0.168  -41.01  1   50.623  ? 29  LYS   A HG3  1 c 2 
ATOM   2079 H HD2  . LYS   B 1 17  ? 8.832  2.344   -40.718 1   48.783  ? 29  LYS   A HD2  1 c 2 
ATOM   2080 H HD3  . LYS   B 1 17  ? 10.251 2.306   -39.937 1   47.899  ? 29  LYS   A HD3  1 c 2 
ATOM   2081 H HE2  . LYS   B 1 17  ? 10.981 0.94    -41.934 1   57.148  ? 29  LYS   A HE2  1 c 2 
ATOM   2082 H HE3  . LYS   B 1 17  ? 9.763  1.652   -42.656 1   57.126  ? 29  LYS   A HE3  1 c 2 
ATOM   2083 H HZ1  . LYS   B 1 17  ? 11.872 2.933   -41.492 1   55.793  ? 29  LYS   A HZ1  1 c 2 
ATOM   2084 H HZ2  . LYS   B 1 17  ? 10.71  3.646   -42.06  1   55.459  ? 29  LYS   A HZ2  1 c 2 
ATOM   2085 H HZ3  . LYS   B 1 17  ? 11.606 2.874   -42.942 1   58.593  ? 29  LYS   A HZ3  1 c 2 
ATOM   2086 N N    . ASP   B 1 18  ? 6.002  1.151   -36.658 1   38.684  ? 30  ASP   A N    1 ? 2 
ATOM   2087 C CA   . ASP   B 1 18  ? 4.701  1.071   -36.011 1   38.4    ? 30  ASP   A CA   1 ? 2 
ATOM   2088 C C    . ASP   B 1 18  ? 3.992  2.42    -35.941 1   34.748  ? 30  ASP   A C    1 ? 2 
ATOM   2089 O O    . ASP   B 1 18  ? 2.974  2.548   -35.214 1   33.628  ? 30  ASP   A O    1 ? 2 
ATOM   2090 C CB   . ASP   B 1 18  ? 4.869  0.477   -34.637 1   36.431  ? 30  ASP   A CB   1 ? 2 
ATOM   2091 C CG   . ASP   B 1 18  ? 5.766  1.272   -33.696 1   38.109  ? 30  ASP   A CG   1 ? 2 
ATOM   2092 O OD1  . ASP   B 1 18  ? 6.071  2.435   -34     1   31.384  ? 30  ASP   A OD1  1 ? 2 
ATOM   2093 O OD2  . ASP   B 1 18  ? 6.205  0.728   -32.738 1   36.198  ? 30  ASP   A OD2  1 ? 2 
ATOM   2094 H H    . ASP   B 1 18  ? 6.666  1.587   -36.207 1   37.953  ? 30  ASP   A H    1 c 2 
ATOM   2095 H HA   . ASP   B 1 18  ? 4.137  0.453   -36.526 1   39.632  ? 30  ASP   A HA   1 c 2 
ATOM   2096 H HB2  . ASP   B 1 18  ? 3.988  0.383   -34.218 1   37.761  ? 30  ASP   A HB2  1 c 2 
ATOM   2097 H HB3  . ASP   B 1 18  ? 5.251  -0.421  -34.732 1   39.159  ? 30  ASP   A HB3  1 c 2 
ATOM   2098 N N    . ARG   B 1 19  ? 4.534  3.408   -36.691 1   32.785  ? 31  ARG   A N    1 ? 2 
ATOM   2099 C CA   . ARG   B 1 19  ? 3.946  4.752   -36.74  1   33.817  ? 31  ARG   A CA   1 ? 2 
ATOM   2100 C C    . ARG   B 1 19  ? 3.911  5.412   -35.363 1   31.416  ? 31  ARG   A C    1 ? 2 
ATOM   2101 O O    . ARG   B 1 19  ? 3.213  6.389   -35.15  1   31.915  ? 31  ARG   A O    1 ? 2 
ATOM   2102 C CB   . ARG   B 1 19  ? 2.538  4.799   -37.402 1   31.955  ? 31  ARG   A CB   1 ? 2 
ATOM   2103 C CG   . ARG   B 1 19  ? 2.723  4.528   -38.87  1   35.996  ? 31  ARG   A CG   1 ? 2 
ATOM   2104 C CD   . ARG   B 1 19  ? 1.498  4.546   -39.826 1   37.577  ? 31  ARG   A CD   1 ? 2 
ATOM   2105 N NE   . ARG   B 1 19  ? 0.773  5.803   -39.649 1   36.319  ? 31  ARG   A NE   1 ? 2 
ATOM   2106 C CZ   . ARG   B 1 19  ? 0.869  6.951   -40.255 1   38.761  ? 31  ARG   A CZ   1 ? 2 
ATOM   2107 N NH1  . ARG   B 1 19  ? 1.781  7.207   -41.169 1   39.394  ? 31  ARG   A NH1  1 ? 2 
ATOM   2108 N NH2  . ARG   B 1 19  ? 0.016  7.926   -39.934 1   40.955  ? 31  ARG   A NH2  1 ? 2 
ATOM   2109 H H    . ARG   B 1 19  ? 5.283  3.24    -37.185 1   34.221  ? 31  ARG   A H    1 c 2 
ATOM   2110 H HA   . ARG   B 1 19  ? 4.538  5.306   -37.308 1   32.579  ? 31  ARG   A HA   1 c 2 
ATOM   2111 H HB2  . ARG   B 1 19  ? 1.951  4.12    -37.009 1   33.771  ? 31  ARG   A HB2  1 c 2 
ATOM   2112 H HB3  . ARG   B 1 19  ? 2.13   5.682   -37.276 1   32.403  ? 31  ARG   A HB3  1 c 2 
ATOM   2113 H HG2  . ARG   B 1 19  ? 3.375  5.178   -39.213 1   34.963  ? 31  ARG   A HG2  1 c 2 
ATOM   2114 H HG3  . ARG   B 1 19  ? 3.156  3.651   -38.959 1   36.229  ? 31  ARG   A HG3  1 c 2 
ATOM   2115 H HD2  . ARG   B 1 19  ? 1.796  4.467   -40.755 1   39.11   ? 31  ARG   A HD2  1 c 2 
ATOM   2116 H HD3  . ARG   B 1 19  ? 0.904  3.794   -39.624 1   38.542  ? 31  ARG   A HD3  1 c 2 
ATOM   2117 H HE   . ARG   B 1 19  ? 0.168  5.786   -39.023 1   36.529  ? 31  ARG   A HE   1 c 2 
ATOM   2118 H HH11 . ARG   B 1 19  ? 2.551  6.772   -41.157 1   39.145  ? 31  ARG   A HH11 1 c 2 
ATOM   2119 H HH12 . ARG   B 1 19  ? 1.621  7.815   -41.792 1   40.459  ? 31  ARG   A HH12 1 c 2 
ATOM   2120 H HH21 . ARG   B 1 19  ? -0.735 7.739   -39.506 1   40.196  ? 31  ARG   A HH21 1 c 2 
ATOM   2121 H HH22 . ARG   B 1 19  ? 0.207  8.763   -40.149 1   39.941  ? 31  ARG   A HH22 1 c 2 
ATOM   2122 N N    . GLY   B 1 20  ? 4.719  4.925   -34.435 1   29.137  ? 32  GLY   A N    1 ? 2 
ATOM   2123 C CA   . GLY   B 1 20  ? 4.701  5.464   -33.08  1   27.444  ? 32  GLY   A CA   1 ? 2 
ATOM   2124 C C    . GLY   B 1 20  ? 5.285  6.867   -32.923 1   25.055  ? 32  GLY   A C    1 ? 2 
ATOM   2125 O O    . GLY   B 1 20  ? 4.97   7.582   -31.975 1   27.148  ? 32  GLY   A O    1 ? 2 
ATOM   2126 H H    . GLY   B 1 20  ? 5.314  4.264   -34.64  1   30.181  ? 32  GLY   A H    1 c 2 
ATOM   2127 H HA2  . GLY   B 1 20  ? 3.77   5.472   -32.761 1   27.503  ? 32  GLY   A HA2  1 c 2 
ATOM   2128 H HA3  . GLY   B 1 20  ? 5.202  4.848   -32.5   1   27.378  ? 32  GLY   A HA3  1 c 2 
ATOM   2129 N N    . VAL   B 1 21  ? 6.207  7.22    -33.805 1   25.62   ? 33  VAL   A N    1 ? 2 
ATOM   2130 C CA   . VAL   B 1 21  ? 6.788  8.548   -33.805 1   25.612  ? 33  VAL   A CA   1 ? 2 
ATOM   2131 C C    . VAL   B 1 21  ? 6.801  8.956   -35.267 1   26.186  ? 33  VAL   A C    1 ? 2 
ATOM   2132 O O    . VAL   B 1 21  ? 7.501  8.333   -36.075 1   24.287  ? 33  VAL   A O    1 ? 2 
ATOM   2133 C CB   . VAL   B 1 21  ? 8.203  8.619   -33.167 1   24.895  ? 33  VAL   A CB   1 ? 2 
ATOM   2134 C CG1  . VAL   B 1 21  ? 8.71   10.053  -33.165 1   26.154  ? 33  VAL   A CG1  1 ? 2 
ATOM   2135 C CG2  . VAL   B 1 21  ? 8.268  7.988   -31.77  1   30.586  ? 33  VAL   A CG2  1 ? 2 
ATOM   2136 H H    . VAL   B 1 21  ? 6.487  6.617   -34.432 1   26.686  ? 33  VAL   A H    1 c 2 
ATOM   2137 H HA   . VAL   B 1 21  ? 6.195  9.151   -33.316 1   24.745  ? 33  VAL   A HA   1 c 2 
ATOM   2138 H HB   . VAL   B 1 21  ? 8.805  8.098   -33.749 1   27.032  ? 33  VAL   A HB   1 c 2 
ATOM   2139 H HG11 . VAL   B 1 21  ? 8.031  10.636  -32.785 1   25.146  ? 33  VAL   A HG11 1 c 2 
ATOM   2140 H HG12 . VAL   B 1 21  ? 8.903  10.332  -34.075 1   26.235  ? 33  VAL   A HG12 1 c 2 
ATOM   2141 H HG13 . VAL   B 1 21  ? 9.52   10.11   -32.631 1   25.366  ? 33  VAL   A HG13 1 c 2 
ATOM   2142 H HG21 . VAL   B 1 21  ? 9.164  8.093   -31.407 1   28.414  ? 33  VAL   A HG21 1 c 2 
ATOM   2143 H HG22 . VAL   B 1 21  ? 8.053  7.042   -31.83  1   29.196  ? 33  VAL   A HG22 1 c 2 
ATOM   2144 H HG23 . VAL   B 1 21  ? 7.629  8.428   -31.185 1   28.009  ? 33  VAL   A HG23 1 c 2 
ATOM   2145 N N    . LEU   B 1 22  ? 5.903  9.903   -35.604 1   26.186  ? 34  LEU   A N    1 ? 2 
ATOM   2146 C CA   . LEU   B 1 22  ? 5.865  10.526  -36.875 1   26.232  ? 34  LEU   A CA   1 ? 2 
ATOM   2147 C C    . LEU   B 1 22  ? 6.477  11.912  -36.925 1   27.335  ? 34  LEU   A C    1 ? 2 
ATOM   2148 O O    . LEU   B 1 22  ? 6.19   12.725  -36.05  1   27.362  ? 34  LEU   A O    1 ? 2 
ATOM   2149 C CB   . LEU   B 1 22  ? 4.374  10.525  -37.213 1   28.346  ? 34  LEU   A CB   1 ? 2 
ATOM   2150 C CG   . LEU   B 1 22  ? 3.715  9.14    -37.39  1   30.38   ? 34  LEU   A CG   1 ? 2 
ATOM   2151 C CD1  . LEU   B 1 22  ? 2.274  9.482   -37.567 1   32.546  ? 34  LEU   A CD1  1 ? 2 
ATOM   2152 C CD2  . LEU   B 1 22  ? 4.296  8.269   -38.547 1   34.399  ? 34  LEU   A CD2  1 ? 2 
ATOM   2153 H H    . LEU   B 1 22  ? 5.29   10.162  -34.978 1   25.392  ? 34  LEU   A H    1 c 2 
ATOM   2154 H HA   . LEU   B 1 22  ? 6.341  9.947   -37.52  1   27.786  ? 34  LEU   A HA   1 c 2 
ATOM   2155 H HB2  . LEU   B 1 22  ? 3.897  11.01   -36.501 1   27.609  ? 34  LEU   A HB2  1 c 2 
ATOM   2156 H HB3  . LEU   B 1 22  ? 4.251  11.035  -38.047 1   29.49   ? 34  LEU   A HB3  1 c 2 
ATOM   2157 H HG   . LEU   B 1 22  ? 3.813  8.636   -36.541 1   29.852  ? 34  LEU   A HG   1 c 2 
ATOM   2158 H HD11 . LEU   B 1 22  ? 1.925  9.858   -36.741 1   31.217  ? 34  LEU   A HD11 1 c 2 
ATOM   2159 H HD12 . LEU   B 1 22  ? 1.775  8.679   -37.79  1   33.125  ? 34  LEU   A HD12 1 c 2 
ATOM   2160 H HD13 . LEU   B 1 22  ? 2.176  10.131  -38.284 1   33.088  ? 34  LEU   A HD13 1 c 2 
ATOM   2161 H HD21 . LEU   B 1 22  ? 5.192  7.977   -38.314 1   33.132  ? 34  LEU   A HD21 1 c 2 
ATOM   2162 H HD22 . LEU   B 1 22  ? 4.329  8.794   -39.365 1   34.721  ? 34  LEU   A HD22 1 c 2 
ATOM   2163 H HD23 . LEU   B 1 22  ? 3.729  7.492   -38.685 1   34.584  ? 34  LEU   A HD23 1 c 2 
ATOM   2164 N N    . LYS   B 1 23  ? 7.248  12.177  -37.968 1   26.878  ? 35  LYS   A N    1 ? 2 
ATOM   2165 C CA   . LYS   B 1 23  ? 8.018  13.411  -38.122 1   31.146  ? 35  LYS   A CA   1 ? 2 
ATOM   2166 C C    . LYS   B 1 23  ? 7.89   14.125  -39.466 1   33.666  ? 35  LYS   A C    1 ? 2 
ATOM   2167 O O    . LYS   B 1 23  ? 7.981  13.53   -40.547 1   31.67   ? 35  LYS   A O    1 ? 2 
ATOM   2168 C CB   . LYS   B 1 23  ? 9.49   13.111  -37.859 1   33.763  ? 35  LYS   A CB   1 ? 2 
ATOM   2169 C CG   . LYS   B 1 23  ? 10.481 14.273  -38.104 1   32.895  ? 35  LYS   A CG   1 ? 2 
ATOM   2170 C CD   . LYS   B 1 23  ? 11.952 13.962  -37.924 1   31.319  ? 35  LYS   A CD   1 ? 2 
ATOM   2171 C CE   . LYS   B 1 23  ? 12.767 15.132  -38.173 1   35.7    ? 35  LYS   A CE   1 ? 2 
ATOM   2172 N NZ   . LYS   B 1 23  ? 14.196 14.911  -38.389 1   34.617  ? 35  LYS   A NZ   1 ? 2 
ATOM   2173 H H    . LYS   B 1 23  ? 7.302  11.555  -38.635 1   29.076  ? 35  LYS   A H    1 c 2 
ATOM   2174 H HA   . LYS   B 1 23  ? 7.722  14.037  -37.419 1   30.04   ? 35  LYS   A HA   1 c 2 
ATOM   2175 H HB2  . LYS   B 1 23  ? 9.584  12.821  -36.927 1   31.397  ? 35  LYS   A HB2  1 c 2 
ATOM   2176 H HB3  . LYS   B 1 23  ? 9.757  12.357  -38.428 1   33.449  ? 35  LYS   A HB3  1 c 2 
ATOM   2177 H HG2  . LYS   B 1 23  ? 10.347 14.601  -39.019 1   34.292  ? 35  LYS   A HG2  1 c 2 
ATOM   2178 H HG3  . LYS   B 1 23  ? 10.243 15.008  -37.497 1   32.206  ? 35  LYS   A HG3  1 c 2 
ATOM   2179 H HD2  . LYS   B 1 23  ? 12.108 13.647  -37.007 1   31.218  ? 35  LYS   A HD2  1 c 2 
ATOM   2180 H HD3  . LYS   B 1 23  ? 12.211 13.248  -38.546 1   33.314  ? 35  LYS   A HD3  1 c 2 
ATOM   2181 H HE2  . LYS   B 1 23  ? 12.414 15.592  -38.955 1   35.575  ? 35  LYS   A HE2  1 c 2 
ATOM   2182 H HE3  . LYS   B 1 23  ? 12.667 15.738  -37.416 1   33.546  ? 35  LYS   A HE3  1 c 2 
ATOM   2183 H HZ1  . LYS   B 1 23  ? 14.316 14.246  -38.992 1   36.031  ? 35  LYS   A HZ1  1 c 2 
ATOM   2184 H HZ2  . LYS   B 1 23  ? 14.592 14.679  -37.608 1   34.361  ? 35  LYS   A HZ2  1 c 2 
ATOM   2185 H HZ3  . LYS   B 1 23  ? 14.579 15.669  -38.703 1   36.304  ? 35  LYS   A HZ3  1 c 2 
ATOM   2186 N N    . ILE   B 1 24  ? 7.762  15.468  -39.401 1   33.76   ? 36  ILE   A N    1 ? 2 
ATOM   2187 C CA   . ILE   B 1 24  ? 7.887  16.343  -40.549 1   34.838  ? 36  ILE   A CA   1 ? 2 
ATOM   2188 C C    . ILE   B 1 24  ? 8.954  17.378  -40.233 1   37.126  ? 36  ILE   A C    1 ? 2 
ATOM   2189 O O    . ILE   B 1 24  ? 8.943  18.059  -39.184 1   35.915  ? 36  ILE   A O    1 ? 2 
ATOM   2190 C CB   . ILE   B 1 24  ? 6.565  17.042  -40.925 1   37.163  ? 36  ILE   A CB   1 ? 2 
ATOM   2191 C CG1  . ILE   B 1 24  ? 5.454  16.035  -41.269 1   39.822  ? 36  ILE   A CG1  1 ? 2 
ATOM   2192 C CG2  . ILE   B 1 24  ? 6.757  18.152  -41.988 1   44.093  ? 36  ILE   A CG2  1 ? 2 
ATOM   2193 C CD1  . ILE   B 1 24  ? 4.173  16.655  -41.772 1   45.46   ? 36  ILE   A CD1  1 ? 2 
ATOM   2194 H H    . ILE   B 1 24  ? 7.583  15.849  -38.589 1   32.464  ? 36  ILE   A H    1 c 2 
ATOM   2195 H HA   . ILE   B 1 24  ? 8.181  15.813  -41.314 1   36.709  ? 36  ILE   A HA   1 c 2 
ATOM   2196 H HB   . ILE   B 1 24  ? 6.266  17.498  -40.113 1   37.066  ? 36  ILE   A HB   1 c 2 
ATOM   2197 H HG12 . ILE   B 1 24  ? 5.793  15.422  -41.953 1   40.901  ? 36  ILE   A HG12 1 c 2 
ATOM   2198 H HG13 . ILE   B 1 24  ? 5.253  15.507  -40.47  1   38.285  ? 36  ILE   A HG13 1 c 2 
ATOM   2199 H HG21 . ILE   B 1 24  ? 5.93   18.653  -42.09  1   43.865  ? 36  ILE   A HG21 1 c 2 
ATOM   2200 H HG22 . ILE   B 1 24  ? 6.996  17.749  -42.84  1   44.232  ? 36  ILE   A HG22 1 c 2 
ATOM   2201 H HG23 . ILE   B 1 24  ? 7.462  18.757  -41.709 1   42.714  ? 36  ILE   A HG23 1 c 2 
ATOM   2202 H HD11 . ILE   B 1 24  ? 3.874  17.343  -41.148 1   43.812  ? 36  ILE   A HD11 1 c 2 
ATOM   2203 H HD12 . ILE   B 1 24  ? 3.486  15.966  -41.848 1   44.383  ? 36  ILE   A HD12 1 c 2 
ATOM   2204 H HD13 . ILE   B 1 24  ? 4.322  17.056  -42.649 1   46.365  ? 36  ILE   A HD13 1 c 2 
ATOM   2205 N N    . VAL   B 1 25  ? 9.861  17.507  -41.199 1   36.565  ? 37  VAL   A N    1 ? 2 
ATOM   2206 C CA   . VAL   B 1 25  ? 10.8   18.603  -41.159 1   39.756  ? 37  VAL   A CA   1 ? 2 
ATOM   2207 C C    . VAL   B 1 25  ? 10.062 19.853  -41.652 1   41.275  ? 37  VAL   A C    1 ? 2 
ATOM   2208 O O    . VAL   B 1 25  ? 9.635  19.917  -42.832 1   43.131  ? 37  VAL   A O    1 ? 2 
ATOM   2209 C CB   . VAL   B 1 25  ? 12.072 18.266  -41.964 1   42.114  ? 37  VAL   A CB   1 ? 2 
ATOM   2210 C CG1  . VAL   B 1 25  ? 13.044 19.422  -41.917 1   46.673  ? 37  VAL   A CG1  1 ? 2 
ATOM   2211 C CG2  . VAL   B 1 25  ? 12.789 16.993  -41.452 1   40.675  ? 37  VAL   A CG2  1 ? 2 
ATOM   2212 H H    . VAL   B 1 25  ? 9.898  16.908  -41.889 1   38.51   ? 37  VAL   A H    1 c 2 
ATOM   2213 H HA   . VAL   B 1 25  ? 11.063 18.745  -40.229 1   37.779  ? 37  VAL   A HA   1 c 2 
ATOM   2214 H HB   . VAL   B 1 25  ? 11.802 18.12   -42.901 1   44.306  ? 37  VAL   A HB   1 c 2 
ATOM   2215 H HG11 . VAL   B 1 25  ? 13.109 19.755  -41.006 1   44.286  ? 37  VAL   A HG11 1 c 2 
ATOM   2216 H HG12 . VAL   B 1 25  ? 12.731 20.134  -42.5   1   47.514  ? 37  VAL   A HG12 1 c 2 
ATOM   2217 H HG13 . VAL   B 1 25  ? 13.92  19.124  -42.215 1   46.418  ? 37  VAL   A HG13 1 c 2 
ATOM   2218 H HG21 . VAL   B 1 25  ? 13.549 16.795  -42.024 1   41.99   ? 37  VAL   A HG21 1 c 2 
ATOM   2219 H HG22 . VAL   B 1 25  ? 12.172 16.243  -41.466 1   39.855  ? 37  VAL   A HG22 1 c 2 
ATOM   2220 H HG23 . VAL   B 1 25  ? 13.1   17.139  -40.543 1   39.196  ? 37  VAL   A HG23 1 c 2 
ATOM   2221 N N    . LYS   B 1 26  ? 10.016 20.855  -40.777 1   37.146  ? 38  LYS   A N    1 ? 2 
ATOM   2222 C CA   . LYS   B 1 26  ? 9.473  22.16   -41.078 1   44.474  ? 38  LYS   A CA   1 ? 2 
ATOM   2223 C C    . LYS   B 1 26  ? 10.516 23.104  -41.613 1   48.08   ? 38  LYS   A C    1 ? 2 
ATOM   2224 O O    . LYS   B 1 26  ? 10.176 23.857  -42.493 1   52.197  ? 38  LYS   A O    1 ? 2 
ATOM   2225 C CB   . LYS   B 1 26  ? 8.778  22.754  -39.847 1   42.727  ? 38  LYS   A CB   1 ? 2 
ATOM   2226 C CG   . LYS   B 1 26  ? 7.575  21.915  -39.403 1   44.675  ? 38  LYS   A CG   1 ? 2 
ATOM   2227 C CD   . LYS   B 1 26  ? 6.622  21.422  -40.492 1   48.559  ? 38  LYS   A CD   1 ? 2 
ATOM   2228 C CE   . LYS   B 1 26  ? 5.867  22.515  -41.046 1   47.273  ? 38  LYS   A CE   1 ? 2 
ATOM   2229 N NZ   . LYS   B 1 26  ? 4.765  22.216  -41.967 1   49.963  ? 38  LYS   A NZ   1 ? 2 
ATOM   2230 H H    . LYS   B 1 26  ? 10.345 20.713  -39.937 1   37.395  ? 38  LYS   A H    1 c 2 
ATOM   2231 H HA   . LYS   B 1 26  ? 8.789  22.049  -41.784 1   44.819  ? 38  LYS   A HA   1 c 2 
ATOM   2232 H HB2  . LYS   B 1 26  ? 9.419  22.808  -39.107 1   42.435  ? 38  LYS   A HB2  1 c 2 
ATOM   2233 H HB3  . LYS   B 1 26  ? 8.472  23.663  -40.053 1   45.515  ? 38  LYS   A HB3  1 c 2 
ATOM   2234 H HG2  . LYS   B 1 26  ? 7.918  21.134  -38.917 1   42.286  ? 38  LYS   A HG2  1 c 2 
ATOM   2235 H HG3  . LYS   B 1 26  ? 7.06   22.446  -38.757 1   44.085  ? 38  LYS   A HG3  1 c 2 
ATOM   2236 H HD2  . LYS   B 1 26  ? 7.127  20.979  -41.206 1   47.448  ? 38  LYS   A HD2  1 c 2 
ATOM   2237 H HD3  . LYS   B 1 26  ? 6.002  20.767  -40.104 1   45.54   ? 38  LYS   A HD3  1 c 2 
ATOM   2238 H HE2  . LYS   B 1 26  ? 5.497  23.027  -40.304 1   47.977  ? 38  LYS   A HE2  1 c 2 
ATOM   2239 H HE3  . LYS   B 1 26  ? 6.49   23.103  -41.51  1   49.997  ? 38  LYS   A HE3  1 c 2 
ATOM   2240 H HZ1  . LYS   B 1 26  ? 4.166  21.671  -41.561 1   48.425  ? 38  LYS   A HZ1  1 c 2 
ATOM   2241 H HZ2  . LYS   B 1 26  ? 5.087  21.806  -42.708 1   50.51   ? 38  LYS   A HZ2  1 c 2 
ATOM   2242 H HZ3  . LYS   B 1 26  ? 4.351  22.985  -42.209 1   51.718  ? 38  LYS   A HZ3  1 c 2 
ATOM   2243 N N    . ARG   B 1 27  ? 11.704 23.134  -41.03  1   45.447  ? 39  ARG   A N    1 ? 2 
ATOM   2244 C CA   . ARG   B 1 27  ? 12.785 23.963  -41.544 1   50.859  ? 39  ARG   A CA   1 ? 2 
ATOM   2245 C C    . ARG   B 1 27  ? 14.068 23.143  -41.49  1   50.948  ? 39  ARG   A C    1 ? 2 
ATOM   2246 O O    . ARG   B 1 27  ? 14.396 22.568  -40.429 1   49.101  ? 39  ARG   A O    1 ? 2 
ATOM   2247 C CB   . ARG   B 1 27  ? 13.033 25.185  -40.655 1   51.316  ? 39  ARG   A CB   1 ? 2 
ATOM   2248 C CG   . ARG   B 1 27  ? 14.14  26.099  -41.147 1   55.662  ? 39  ARG   A CG   1 ? 2 
ATOM   2249 C CD   . ARG   B 1 27  ? 14.283 27.295  -40.248 1   60.681  ? 39  ARG   A CD   1 ? 2 
ATOM   2250 N NE   . ARG   B 1 27  ? 14.931 27      -38.955 1   63.535  ? 39  ARG   A NE   1 ? 2 
ATOM   2251 C CZ   . ARG   B 1 27  ? 14.847 27.857  -37.909 1   60.701  ? 39  ARG   A CZ   1 ? 2 
ATOM   2252 N NH1  . ARG   B 1 27  ? 15.357 27.549  -36.726 1   55.938  ? 39  ARG   A NH1  1 ? 2 
ATOM   2253 N NH2  . ARG   B 1 27  ? 14.161 28.972  -38.061 1   58.985  ? 39  ARG   A NH2  1 ? 2 
ATOM   2254 H H    . ARG   B 1 27  ? 11.852 22.629  -40.282 1   44.282  ? 39  ARG   A H    1 c 2 
ATOM   2255 H HA   . ARG   B 1 27  ? 12.589 24.229  -42.478 1   52.758  ? 39  ARG   A HA   1 c 2 
ATOM   2256 H HB2  . ARG   B 1 27  ? 12.202 25.702  -40.596 1   52.211  ? 39  ARG   A HB2  1 c 2 
ATOM   2257 H HB3  . ARG   B 1 27  ? 13.257 24.877  -39.751 1   49.513  ? 39  ARG   A HB3  1 c 2 
ATOM   2258 H HG2  . ARG   B 1 27  ? 14.99  25.609  -41.166 1   55.872  ? 39  ARG   A HG2  1 c 2 
ATOM   2259 H HG3  . ARG   B 1 27  ? 13.935 26.401  -42.058 1   58.623  ? 39  ARG   A HG3  1 c 2 
ATOM   2260 H HD2  . ARG   B 1 27  ? 14.805 27.978  -40.717 1   63.445  ? 39  ARG   A HD2  1 c 2 
ATOM   2261 H HD3  . ARG   B 1 27  ? 13.392 27.666  -40.083 1   60.795  ? 39  ARG   A HD3  1 c 2 
ATOM   2262 H HE   . ARG   B 1 27  ? 15.378 26.258  -38.863 1   60.098  ? 39  ARG   A HE   1 c 2 
ATOM   2263 H HH11 . ARG   B 1 27  ? 15.584 26.713  -36.55  1   54.957  ? 39  ARG   A HH11 1 c 2 
ATOM   2264 H HH12 . ARG   B 1 27  ? 15.468 28.181  -36.118 1   57.458  ? 39  ARG   A HH12 1 c 2 
ATOM   2265 H HH21 . ARG   B 1 27  ? 14.492 29.627  -38.555 1   62.727  ? 39  ARG   A HH21 1 c 2 
ATOM   2266 H HH22 . ARG   B 1 27  ? 13.374 29.061  -37.67  1   59.432  ? 39  ARG   A HH22 1 c 2 
ATOM   2267 N N    . VAL   B 1 28  ? 14.738 23.001  -42.638 1   51.185  ? 40  VAL   A N    1 ? 2 
ATOM   2268 C CA   . VAL   B 1 28  ? 15.936 22.177  -42.681 1   54.446  ? 40  VAL   A CA   1 ? 2 
ATOM   2269 C C    . VAL   B 1 28  ? 16.998 22.861  -41.822 1   54.036  ? 40  VAL   A C    1 ? 2 
ATOM   2270 O O    . VAL   B 1 28  ? 17.013 24.087  -41.712 1   58.448  ? 40  VAL   A O    1 ? 2 
ATOM   2271 C CB   . VAL   B 1 28  ? 16.526 21.864  -44.088 1   57.056  ? 40  VAL   A CB   1 ? 2 
ATOM   2272 C CG1  . VAL   B 1 28  ? 17.79  21.008  -44.02  1   60.852  ? 40  VAL   A CG1  1 ? 2 
ATOM   2273 C CG2  . VAL   B 1 28  ? 15.526 21.152  -44.994 1   54.757  ? 40  VAL   A CG2  1 ? 2 
ATOM   2274 H H    . VAL   B 1 28  ? 14.452 23.419  -43.399 1   54.625  ? 40  VAL   A H    1 c 2 
ATOM   2275 H HA   . VAL   B 1 28  ? 15.717 21.322  -42.26  1   51.298  ? 40  VAL   A HA   1 c 2 
ATOM   2276 H HB   . VAL   B 1 28  ? 16.76  22.726  -44.506 1   59.717  ? 40  VAL   A HB   1 c 2 
ATOM   2277 H HG11 . VAL   B 1 28  ? 17.672 20.304  -43.361 1   57.132  ? 40  VAL   A HG11 1 c 2 
ATOM   2278 H HG12 . VAL   B 1 28  ? 18.546 21.562  -43.772 1   60.525  ? 40  VAL   A HG12 1 c 2 
ATOM   2279 H HG13 . VAL   B 1 28  ? 17.958 20.608  -44.89  1   61.286  ? 40  VAL   A HG13 1 c 2 
ATOM   2280 H HG21 . VAL   B 1 28  ? 15.888 21.093  -45.894 1   58.009  ? 40  VAL   A HG21 1 c 2 
ATOM   2281 H HG22 . VAL   B 1 28  ? 14.693 21.651  -45.014 1   55.673  ? 40  VAL   A HG22 1 c 2 
ATOM   2282 H HG23 . VAL   B 1 28  ? 15.359 20.257  -44.654 1   53.48   ? 40  VAL   A HG23 1 c 2 
ATOM   2283 N N    . GLY   B 1 29  ? 17.906 22.044  -41.284 1   51.918  ? 41  GLY   A N    1 ? 2 
ATOM   2284 C CA   . GLY   B 1 29  ? 19.052 22.525  -40.547 1   52.154  ? 41  GLY   A CA   1 ? 2 
ATOM   2285 C C    . GLY   B 1 29  ? 20.357 22.5    -41.326 1   55.79   ? 41  GLY   A C    1 ? 2 
ATOM   2286 O O    . GLY   B 1 29  ? 20.374 22.636  -42.544 1   62.484  ? 41  GLY   A O    1 ? 2 
ATOM   2287 H H    . GLY   B 1 29  ? 17.79  21.141  -41.361 1   50.931  ? 41  GLY   A H    1 c 2 
ATOM   2288 H HA2  . GLY   B 1 29  ? 18.874 23.448  -40.251 1   53.038  ? 41  GLY   A HA2  1 c 2 
ATOM   2289 H HA3  . GLY   B 1 29  ? 19.153 21.972  -39.737 1   50.324  ? 41  GLY   A HA3  1 c 2 
ATOM   2290 N N    . ASN   B 1 30  ? 21.461 22.428  -40.565 1   56.209  ? 42  ASN   A N    1 ? 2 
ATOM   2291 C CA   . ASN   B 1 30  ? 22.789 22.776  -41.052 1   60.107  ? 42  ASN   A CA   1 ? 2 
ATOM   2292 C C    . ASN   B 1 30  ? 23.701 21.587  -40.927 1   61.157  ? 42  ASN   A C    1 ? 2 
ATOM   2293 O O    . ASN   B 1 30  ? 23.718 20.945  -39.9   1   63.987  ? 42  ASN   A O    1 ? 2 
ATOM   2294 C CB   . ASN   B 1 30  ? 23.483 23.864  -40.234 1   62.835  ? 42  ASN   A CB   1 ? 2 
ATOM   2295 C CG   . ASN   B 1 30  ? 22.632 25.101  -40.133 1   64.494  ? 42  ASN   A CG   1 ? 2 
ATOM   2296 O OD1  . ASN   B 1 30  ? 22.063 25.396  -39.072 1   68.993  ? 42  ASN   A OD1  1 ? 2 
ATOM   2297 N ND2  . ASN   B 1 30  ? 22.43  25.763  -41.248 1   66.221  ? 42  ASN   A ND2  1 ? 2 
ATOM   2298 H H    . ASN   B 1 30  ? 21.379 22.146  -39.7   1   54.218  ? 42  ASN   A H    1 c 2 
ATOM   2299 H HA   . ASN   B 1 30  ? 22.736 23.07   -41.989 1   62.66   ? 42  ASN   A HA   1 c 2 
ATOM   2300 H HB2  . ASN   B 1 30  ? 23.669 23.527  -39.335 1   61.092  ? 42  ASN   A HB2  1 c 2 
ATOM   2301 H HB3  . ASN   B 1 30  ? 24.336 24.092  -40.657 1   65.36   ? 42  ASN   A HB3  1 c 2 
ATOM   2302 H HD21 . ASN   B 1 30  ? 21.889 26.466  -41.253 1   67.168  ? 42  ASN   A HD21 1 c 2 
ATOM   2303 H HD22 . ASN   B 1 30  ? 22.835 25.509  -41.996 1   68.202  ? 42  ASN   A HD22 1 c 2 
ATOM   2304 N N    . GLY   B 1 31  ? 24.528 21.37   -41.938 1   63.476  ? 43  GLY   A N    1 ? 2 
ATOM   2305 C CA   . GLY   B 1 31  ? 25.577 20.38   -41.86  1   66.314  ? 43  GLY   A CA   1 ? 2 
ATOM   2306 C C    . GLY   B 1 31  ? 25.011 18.968  -41.992 1   65.367  ? 43  GLY   A C    1 ? 2 
ATOM   2307 O O    . GLY   B 1 31  ? 23.84  18.795  -42.328 1   68.178  ? 43  GLY   A O    1 ? 2 
ATOM   2308 H H    . GLY   B 1 31  ? 24.438 21.856  -42.707 1   66.107  ? 43  GLY   A H    1 c 2 
ATOM   2309 H HA2  . GLY   B 1 31  ? 26.23  20.544  -42.58  1   68.974  ? 43  GLY   A HA2  1 c 2 
ATOM   2310 H HA3  . GLY   B 1 31  ? 26.046 20.47   -40.997 1   65.491  ? 43  GLY   A HA3  1 c 2 
ATOM   2311 N N    . GLU   B 1 32  ? 25.882 17.986  -41.733 1   66.371  ? 44  GLU   A N    1 ? 2 
ATOM   2312 C CA   . GLU   B 1 32  ? 25.53  16.576  -41.789 1   65.413  ? 44  GLU   A CA   1 ? 2 
ATOM   2313 C C    . GLU   B 1 32  ? 25.261 16.032  -40.359 1   57.711  ? 44  GLU   A C    1 ? 2 
ATOM   2314 O O    . GLU   B 1 32  ? 24.429 15.163  -40.204 1   57.502  ? 44  GLU   A O    1 ? 2 
ATOM   2315 C CB   . GLU   B 1 32  ? 26.604 15.985  -42.726 1   65.299  ? 44  GLU   A CB   1 ? 2 
ATOM   2316 H H    . GLU   B 1 32  ? 26.738 18.212  -41.506 1   67.784  ? 44  GLU   A H    1 c 2 
ATOM   2317 H HA   . GLU   B 1 32  ? 24.676 16.501  -42.286 1   63.009  ? 44  GLU   A HA   1 c 2 
ATOM   2318 H HB2  . GLU   B 1 32  ? 27.438 16.145  -42.485 0   30      ? 44  GLU   A HB2  1 c 2 
ATOM   2319 H HB3  . GLU   B 1 32  ? 26.048 15.488  -43.526 0   30      ? 44  GLU   A HB3  1 c 2 
ATOM   2320 N N    . GLU   B 1 33  ? 25.871 16.584  -39.295 1   54.57   ? 45  GLU   A N    1 ? 2 
ATOM   2321 C CA   . GLU   B 1 33  ? 25.93  15.925  -37.991 1   53.487  ? 45  GLU   A CA   1 ? 2 
ATOM   2322 C C    . GLU   B 1 33  ? 24.609 15.978  -37.255 1   48.154  ? 45  GLU   A C    1 ? 2 
ATOM   2323 O O    . GLU   B 1 33  ? 23.953 17.016  -37.183 1   46.2    ? 45  GLU   A O    1 ? 2 
ATOM   2324 C CB   . GLU   B 1 33  ? 26.956 16.506  -37.013 1   54.658  ? 45  GLU   A CB   1 ? 2 
ATOM   2325 H H    . GLU   B 1 33  ? 26.262 17.405  -39.386 1   56.922  ? 45  GLU   A H    1 c 2 
ATOM   2326 H HA   . GLU   B 1 33  ? 26.164 14.975  -38.144 1   53.435  ? 45  GLU   A HA   1 c 2 
ATOM   2327 H HB2  . GLU   B 1 33  ? 27.826 16.348  -37.382 0   30      ? 45  GLU   A HB2  1 c 2 
ATOM   2328 H HB3  . GLU   B 1 33  ? 26.437 17.023  -36.351 0   30      ? 45  GLU   A HB3  1 c 2 
ATOM   2329 N N    . THR   B 1 34  ? 24.169 14.823  -36.734 1   50.979  ? 46  THR   A N    1 ? 2 
ATOM   2330 C CA   . THR   B 1 34  ? 23.022 14.742  -35.825 1   45.455  ? 46  THR   A CA   1 ? 2 
ATOM   2331 C C    . THR   B 1 34  ? 23.533 14.269  -34.477 1   44.185  ? 46  THR   A C    1 ? 2 
ATOM   2332 O O    . THR   B 1 34  ? 24.568 13.709  -34.405 1   47.617  ? 46  THR   A O    1 ? 2 
ATOM   2333 C CB   . THR   B 1 34  ? 21.997 13.766  -36.379 1   44.59   ? 46  THR   A CB   1 ? 2 
ATOM   2334 O OG1  . THR   B 1 34  ? 22.741 12.546  -36.413 1   42.579  ? 46  THR   A OG1  1 ? 2 
ATOM   2335 C CG2  . THR   B 1 34  ? 21.499 14.27   -37.72  1   45.596  ? 46  THR   A CG2  1 ? 2 
ATOM   2336 H H    . THR   B 1 34  ? 24.601 14.049  -36.954 1   50.18   ? 46  THR   A H    1 c 2 
ATOM   2337 H HA   . THR   B 1 34  ? 22.613 15.629  -35.732 1   45.234  ? 46  THR   A HA   1 c 2 
ATOM   2338 H HB   . THR   B 1 34  ? 21.24  13.679  -35.752 1   41.954  ? 46  THR   A HB   1 c 2 
ATOM   2339 H HG1  . THR   B 1 34  ? 23.421 12.649  -36.991 0   30      ? 46  THR   A HG1  1 c 2 
ATOM   2340 H HG21 . THR   B 1 34  ? 20.722 13.754  -37.993 1   44.666  ? 46  THR   A HG21 1 c 2 
ATOM   2341 H HG22 . THR   B 1 34  ? 22.201 14.173  -38.386 1   47.596  ? 46  THR   A HG22 1 c 2 
ATOM   2342 H HG23 . THR   B 1 34  ? 21.253 15.208  -37.645 1   45.319  ? 46  THR   A HG23 1 c 2 
ATOM   2343 N N    . PRO   B 1 35  ? 22.872 14.483  -33.343 1   43.643  ? 47  PRO   A N    1 ? 2 
ATOM   2344 C CA   . PRO   B 1 35  ? 23.506 14.171  -32.064 1   42.023  ? 47  PRO   A CA   1 ? 2 
ATOM   2345 C C    . PRO   B 1 35  ? 23.616 12.678  -31.777 1   39.014  ? 47  PRO   A C    1 ? 2 
ATOM   2346 O O    . PRO   B 1 35  ? 22.724 11.935  -32.128 1   36.608  ? 47  PRO   A O    1 ? 2 
ATOM   2347 C CB   . PRO   B 1 35  ? 22.582 14.851  -31.036 1   39.325  ? 47  PRO   A CB   1 ? 2 
ATOM   2348 C CG   . PRO   B 1 35  ? 21.313 15.22   -31.758 1   39.859  ? 47  PRO   A CG   1 ? 2 
ATOM   2349 C CD   . PRO   B 1 35  ? 21.517 15.071  -33.229 1   41.273  ? 47  PRO   A CD   1 ? 2 
ATOM   2350 H HA   . PRO   B 1 35  ? 24.402 14.591  -32.033 1   43.368  ? 47  PRO   A HA   1 c 2 
ATOM   2351 H HB2  . PRO   B 1 35  ? 22.388 14.243  -30.287 1   39.337  ? 47  PRO   A HB2  1 c 2 
ATOM   2352 H HB3  . PRO   B 1 35  ? 23.013 15.657  -30.666 1   40.834  ? 47  PRO   A HB3  1 c 2 
ATOM   2353 H HG2  . PRO   B 1 35  ? 20.581 14.64   -31.464 1   37.998  ? 47  PRO   A HG2  1 c 2 
ATOM   2354 H HG3  . PRO   B 1 35  ? 21.067 16.146  -31.549 1   39.238  ? 47  PRO   A HG3  1 c 2 
ATOM   2355 H HD2  . PRO   B 1 35  ? 20.839 14.476  -33.618 1   40.315  ? 47  PRO   A HD2  1 c 2 
ATOM   2356 H HD3  . PRO   B 1 35  ? 21.473 15.944  -33.679 1   41.767  ? 47  PRO   A HD3  1 c 2 
ATOM   2357 N N    . MET   B 1 36  ? 24.606 12.348  -30.964 1   39.754  ? 48  MET   A N    1 ? 2 
ATOM   2358 C CA   . MET   B 1 36  ? 24.953 11.008  -30.503 1   41.976  ? 48  MET   A CA   1 ? 2 
ATOM   2359 C C    . MET   B 1 36  ? 24.341 10.806  -29.117 1   39.409  ? 48  MET   A C    1 ? 2 
ATOM   2360 O O    . MET   B 1 36  ? 24.101 11.756  -28.393 1   37.551  ? 48  MET   A O    1 ? 2 
ATOM   2361 C CB   . MET   B 1 36  ? 26.457 10.825  -30.414 1   47.814  ? 48  MET   A CB   1 ? 2 
ATOM   2362 C CG   . MET   B 1 36  ? 27.278 10.653  -31.716 1   55.533  ? 48  MET   A CG   1 ? 2 
ATOM   2363 S SD   . MET   B 1 36  ? 26.687 9.431   -32.934 1   50.008  ? 48  MET   A SD   1 ? 2 
ATOM   2364 C CE   . MET   B 1 36  ? 27.805 9.937   -34.238 1   58.808  ? 48  MET   A CE   1 ? 2 
ATOM   2365 H H    . MET   B 1 36  ? 25.129 13.033  -30.66  1   41.214  ? 48  MET   A H    1 c 2 
ATOM   2366 H HA   . MET   B 1 36  ? 24.568 10.344  -31.129 1   41.572  ? 48  MET   A HA   1 c 2 
ATOM   2367 H HB2  . MET   B 1 36  ? 26.82  11.599  -29.933 1   48.694  ? 48  MET   A HB2  1 c 2 
ATOM   2368 H HB3  . MET   B 1 36  ? 26.625 10.04   -29.851 1   48.908  ? 48  MET   A HB3  1 c 2 
ATOM   2369 H HG2  . MET   B 1 36  ? 27.325 11.521  -32.165 1   53.056  ? 48  MET   A HG2  1 c 2 
ATOM   2370 H HG3  . MET   B 1 36  ? 28.193 10.409  -31.47  1   55.309  ? 48  MET   A HG3  1 c 2 
ATOM   2371 H HE1  . MET   B 1 36  ? 27.826 9.251   -34.932 1   58.271  ? 48  MET   A HE1  1 c 2 
ATOM   2372 H HE2  . MET   B 1 36  ? 27.496 10.778  -34.622 1   56.432  ? 48  MET   A HE2  1 c 2 
ATOM   2373 H HE3  . MET   B 1 36  ? 28.7   10.058  -33.871 1   59.138  ? 48  MET   A HE3  1 c 2 
ATOM   2374 N N    . ILE   B 1 37  ? 24.124 9.55    -28.704 1   38.145  ? 49  ILE   A N    1 ? 2 
ATOM   2375 C CA   . ILE   B 1 37  ? 23.694 9.276   -27.344 1   36.994  ? 49  ILE   A CA   1 ? 2 
ATOM   2376 C C    . ILE   B 1 37  ? 24.749 9.814   -26.376 1   37.764  ? 49  ILE   A C    1 ? 2 
ATOM   2377 O O    . ILE   B 1 37  ? 25.901 9.631   -26.607 1   40.127  ? 49  ILE   A O    1 ? 2 
ATOM   2378 C CB   . ILE   B 1 37  ? 23.464 7.779   -27.109 1   37.743  ? 49  ILE   A CB   1 ? 2 
ATOM   2379 C CG1  . ILE   B 1 37  ? 22.206 7.343   -27.795 1   41.33   ? 49  ILE   A CG1  1 ? 2 
ATOM   2380 C CG2  . ILE   B 1 37  ? 23.43  7.505   -25.616 1   38.815  ? 49  ILE   A CG2  1 ? 2 
ATOM   2381 C CD1  . ILE   B 1 37  ? 22.098 5.875   -28.046 1   42.826  ? 49  ILE   A CD1  1 ? 2 
ATOM   2382 H H    . ILE   B 1 37  ? 24.247 8.853   -29.283 1   39.052  ? 49  ILE   A H    1 c 2 
ATOM   2383 H HA   . ILE   B 1 37  ? 22.853 9.746   -27.185 1   35.056  ? 49  ILE   A HA   1 c 2 
ATOM   2384 H HB   . ILE   B 1 37  ? 24.215 7.288   -27.499 1   40.616  ? 49  ILE   A HB   1 c 2 
ATOM   2385 H HG12 . ILE   B 1 37  ? 21.443 7.622   -27.25  1   38.396  ? 49  ILE   A HG12 1 c 2 
ATOM   2386 H HG13 . ILE   B 1 37  ? 22.142 7.809   -28.654 1   39.23   ? 49  ILE   A HG13 1 c 2 
ATOM   2387 H HG21 . ILE   B 1 37  ? 23.028 6.635   -25.455 1   38.938  ? 49  ILE   A HG21 1 c 2 
ATOM   2388 H HG22 . ILE   B 1 37  ? 22.903 8.188   -25.168 1   37.367  ? 49  ILE   A HG22 1 c 2 
ATOM   2389 H HG23 . ILE   B 1 37  ? 24.334 7.509   -25.26  1   40.723  ? 49  ILE   A HG23 1 c 2 
ATOM   2390 H HD11 . ILE   B 1 37  ? 22.909 5.563   -28.489 1   44.497  ? 49  ILE   A HD11 1 c 2 
ATOM   2391 H HD12 . ILE   B 1 37  ? 21.327 5.696   -28.618 1   41.522  ? 49  ILE   A HD12 1 c 2 
ATOM   2392 H HD13 . ILE   B 1 37  ? 21.988 5.403   -27.199 1   43.21   ? 49  ILE   A HD13 1 c 2 
ATOM   2393 N N    . GLY   B 1 38  ? 24.321 10.526  -25.332 1   38.314  ? 50  GLY   A N    1 ? 2 
ATOM   2394 C CA   . GLY   B 1 38  ? 25.212 11.2    -24.397 1   39.03   ? 50  GLY   A CA   1 ? 2 
ATOM   2395 C C    . GLY   B 1 38  ? 25.357 12.697  -24.667 1   39.623  ? 50  GLY   A C    1 ? 2 
ATOM   2396 O O    . GLY   B 1 38  ? 25.97  13.395  -23.851 1   42.85   ? 50  GLY   A O    1 ? 2 
ATOM   2397 H H    . GLY   B 1 38  ? 23.421 10.593  -25.191 1   35.935  ? 50  GLY   A H    1 c 2 
ATOM   2398 H HA2  . GLY   B 1 38  ? 24.866 11.07   -23.483 1   39.522  ? 50  GLY   A HA2  1 c 2 
ATOM   2399 H HA3  . GLY   B 1 38  ? 26.102 10.777  -24.44  1   41.64   ? 50  GLY   A HA3  1 c 2 
ATOM   2400 N N    . ASP   B 1 39  ? 25.138 13.142  -25.906 1   38.987  ? 51  ASP   A N    1 ? 2 
ATOM   2401 C CA   . ASP   B 1 39  ? 25.337 14.549  -26.244 1   40.619  ? 51  ASP   A CA   1 ? 2 
ATOM   2402 C C    . ASP   B 1 39  ? 24.353 15.396  -25.443 1   37.085  ? 51  ASP   A C    1 ? 2 
ATOM   2403 O O    . ASP   B 1 39  ? 23.218 15      -25.129 1   37.069  ? 51  ASP   A O    1 ? 2 
ATOM   2404 C CB   . ASP   B 1 39  ? 25.185 14.9    -27.723 1   37.775  ? 51  ASP   A CB   1 ? 2 
ATOM   2405 C CG   . ASP   B 1 39  ? 26.299 14.432  -28.645 1   39.877  ? 51  ASP   A CG   1 ? 2 
ATOM   2406 O OD1  . ASP   B 1 39  ? 27.346 13.978  -28.158 1   41.92   ? 51  ASP   A OD1  1 ? 2 
ATOM   2407 O OD2  . ASP   B 1 39  ? 26.138 14.548  -29.893 1   38.178  ? 51  ASP   A OD2  1 ? 2 
ATOM   2408 H H    . ASP   B 1 39  ? 24.861 12.566  -26.558 1   38.39   ? 51  ASP   A H    1 c 2 
ATOM   2409 H HA   . ASP   B 1 39  ? 26.251 14.798  -25.978 1   41.666  ? 51  ASP   A HA   1 c 2 
ATOM   2410 H HB2  . ASP   B 1 39  ? 24.344 14.515  -28.047 1   36.423  ? 51  ASP   A HB2  1 c 2 
ATOM   2411 H HB3  . ASP   B 1 39  ? 25.118 15.875  -27.809 1   38.291  ? 51  ASP   A HB3  1 c 2 
ATOM   2412 N N    . LYS   B 1 40  ? 24.822 16.597  -25.157 1   41.674  ? 52  LYS   A N    1 ? 2 
ATOM   2413 C CA   . LYS   B 1 40  ? 24.02  17.567  -24.451 1   41.363  ? 52  LYS   A CA   1 ? 2 
ATOM   2414 C C    . LYS   B 1 40  ? 23.271 18.36   -25.497 1   39.253  ? 52  LYS   A C    1 ? 2 
ATOM   2415 O O    . LYS   B 1 40  ? 23.864 18.904  -26.424 1   41.533  ? 52  LYS   A O    1 ? 2 
ATOM   2416 C CB   . LYS   B 1 40  ? 24.968 18.447  -23.639 1   49.518  ? 52  LYS   A CB   1 ? 2 
ATOM   2417 C CG   . LYS   B 1 40  ? 24.242 19.208  -22.533 1   54.779  ? 52  LYS   A CG   1 ? 2 
ATOM   2418 C CD   . LYS   B 1 40  ? 25.131 19.307  -21.28  1   60.797  ? 52  LYS   A CD   1 ? 2 
ATOM   2419 C CE   . LYS   B 1 40  ? 24.781 20.487  -20.463 1   63.668  ? 52  LYS   A CE   1 ? 2 
ATOM   2420 N NZ   . LYS   B 1 40  ? 24.958 21.693  -21.28  1   67.975  ? 52  LYS   A NZ   1 ? 2 
ATOM   2421 H H    . LYS   B 1 40  ? 25.669 16.827  -25.413 1   42.703  ? 52  LYS   A H    1 c 2 
ATOM   2422 H HA   . LYS   B 1 40  ? 23.382 17.096  -23.858 1   40.943  ? 52  LYS   A HA   1 c 2 
ATOM   2423 H HB2  . LYS   B 1 40  ? 25.664 17.885  -23.236 1   50.705  ? 52  LYS   A HB2  1 c 2 
ATOM   2424 H HB3  . LYS   B 1 40  ? 25.405 19.093  -24.234 1   50.158  ? 52  LYS   A HB3  1 c 2 
ATOM   2425 H HG2  . LYS   B 1 40  ? 24.016 20.105  -22.858 1   54.261  ? 52  LYS   A HG2  1 c 2 
ATOM   2426 H HG3  . LYS   B 1 40  ? 23.41  18.737  -22.308 1   52.243  ? 52  LYS   A HG3  1 c 2 
ATOM   2427 H HD2  . LYS   B 1 40  ? 25.02  18.496  -20.739 1   60.268  ? 52  LYS   A HD2  1 c 2 
ATOM   2428 H HD3  . LYS   B 1 40  ? 26.073 19.37   -21.55  1   62.153  ? 52  LYS   A HD3  1 c 2 
ATOM   2429 H HE2  . LYS   B 1 40  ? 23.855 20.428  -20.167 1   62.57   ? 52  LYS   A HE2  1 c 2 
ATOM   2430 H HE3  . LYS   B 1 40  ? 25.358 20.537  -19.68  1   66.251  ? 52  LYS   A HE3  1 c 2 
ATOM   2431 H HZ1  . LYS   B 1 40  ? 24.168 21.93   -21.655 1   64.993  ? 52  LYS   A HZ1  1 c 2 
ATOM   2432 H HZ2  . LYS   B 1 40  ? 25.574 21.56   -21.931 1   67.094  ? 52  LYS   A HZ2  1 c 2 
ATOM   2433 H HZ3  . LYS   B 1 40  ? 25.24  22.372  -20.75  1   68.665  ? 52  LYS   A HZ3  1 c 2 
ATOM   2434 N N    . VAL   B 1 41  ? 21.954 18.393  -25.374 1   38.316  ? 53  VAL   A N    1 ? 2 
ATOM   2435 C CA   . VAL   B 1 41  ? 21.186 18.903  -26.494 1   38.283  ? 53  VAL   A CA   1 ? 2 
ATOM   2436 C C    . VAL   B 1 41  ? 20.42  20.13   -25.971 1   39.888  ? 53  VAL   A C    1 ? 2 
ATOM   2437 O O    . VAL   B 1 41  ? 19.898 20.099  -24.839 1   35.522  ? 53  VAL   A O    1 ? 2 
ATOM   2438 C CB   . VAL   B 1 41  ? 20.237 17.835  -27.094 1   38.302  ? 53  VAL   A CB   1 ? 2 
ATOM   2439 C CG1  . VAL   B 1 41  ? 19.358 18.451  -28.167 1   39.279  ? 53  VAL   A CG1  1 ? 2 
ATOM   2440 C CG2  . VAL   B 1 41  ? 21.003 16.646  -27.688 1   41.09   ? 53  VAL   A CG2  1 ? 2 
ATOM   2441 H H    . VAL   B 1 41  ? 21.532 18.112  -24.614 1   37.766  ? 53  VAL   A H    1 c 2 
ATOM   2442 H HA   . VAL   B 1 41  ? 21.803 19.194  -27.193 1   39.717  ? 53  VAL   A HA   1 c 2 
ATOM   2443 H HB   . VAL   B 1 41  ? 19.661 17.506  -26.364 1   37.764  ? 53  VAL   A HB   1 c 2 
ATOM   2444 H HG11 . VAL   B 1 41  ? 19.859 19.133  -28.644 1   39.774  ? 53  VAL   A HG11 1 c 2 
ATOM   2445 H HG12 . VAL   B 1 41  ? 18.576 18.853  -27.754 1   37.978  ? 53  VAL   A HG12 1 c 2 
ATOM   2446 H HG13 . VAL   B 1 41  ? 19.075 17.762  -28.791 1   37.855  ? 53  VAL   A HG13 1 c 2 
ATOM   2447 H HG21 . VAL   B 1 41  ? 20.372 15.98   -28.008 1   39.093  ? 53  VAL   A HG21 1 c 2 
ATOM   2448 H HG22 . VAL   B 1 41  ? 21.571 16.251  -27.005 1   41.176  ? 53  VAL   A HG22 1 c 2 
ATOM   2449 H HG23 . VAL   B 1 41  ? 21.554 16.952  -28.428 1   41.324  ? 53  VAL   A HG23 1 c 2 
ATOM   2450 N N    . TYR   B 1 42  ? 20.388 21.178  -26.809 1   38.184  ? 54  TYR   A N    1 ? 2 
ATOM   2451 C CA   . TYR   B 1 42  ? 19.628 22.388  -26.507 1   40.467  ? 54  TYR   A CA   1 ? 2 
ATOM   2452 C C    . TYR   B 1 42  ? 18.496 22.539  -27.503 1   37.066  ? 54  TYR   A C    1 ? 2 
ATOM   2453 O O    . TYR   B 1 42  ? 18.769 22.627  -28.715 1   35.343  ? 54  TYR   A O    1 ? 2 
ATOM   2454 C CB   . TYR   B 1 42  ? 20.566 23.593  -26.686 1   46.326  ? 54  TYR   A CB   1 ? 2 
ATOM   2455 C CG   . TYR   B 1 42  ? 21.742 23.625  -25.734 1   47.47   ? 54  TYR   A CG   1 ? 2 
ATOM   2456 C CD1  . TYR   B 1 42  ? 22.863 22.841  -25.971 1   50.985  ? 54  TYR   A CD1  1 ? 2 
ATOM   2457 C CD2  . TYR   B 1 42  ? 21.717 24.437  -24.611 1   48.357  ? 54  TYR   A CD2  1 ? 2 
ATOM   2458 C CE1  . TYR   B 1 42  ? 23.946 22.866  -25.107 1   55.147  ? 54  TYR   A CE1  1 ? 2 
ATOM   2459 C CE2  . TYR   B 1 42  ? 22.794 24.479  -23.745 1   55.94   ? 54  TYR   A CE2  1 ? 2 
ATOM   2460 C CZ   . TYR   B 1 42  ? 23.889 23.661  -23.98  1   58.083  ? 54  TYR   A CZ   1 ? 2 
ATOM   2461 O OH   . TYR   B 1 42  ? 24.961 23.731  -23.145 1   66.05   ? 54  TYR   A OH   1 ? 2 
ATOM   2462 H H    . TYR   B 1 42  ? 20.853 21.138  -27.595 1   39.672  ? 54  TYR   A H    1 c 2 
ATOM   2463 H HA   . TYR   B 1 42  ? 19.276 22.358  -25.578 1   39.984  ? 54  TYR   A HA   1 c 2 
ATOM   2464 H HB2  . TYR   B 1 42  ? 20.908 23.587  -27.608 1   45.696  ? 54  TYR   A HB2  1 c 2 
ATOM   2465 H HB3  . TYR   B 1 42  ? 20.041 24.416  -26.568 1   45.934  ? 54  TYR   A HB3  1 c 2 
ATOM   2466 H HD1  . TYR   B 1 42  ? 22.889 22.282  -26.73  1   49.796  ? 54  TYR   A HD1  1 c 2 
ATOM   2467 H HD2  . TYR   B 1 42  ? 20.961 24.977  -24.441 1   49.577  ? 54  TYR   A HD2  1 c 2 
ATOM   2468 H HE1  . TYR   B 1 42  ? 24.702 22.329  -25.273 1   55.645  ? 54  TYR   A HE1  1 c 2 
ATOM   2469 H HE2  . TYR   B 1 42  ? 22.769 25.03   -22.981 1   56.316  ? 54  TYR   A HE2  1 c 2 
ATOM   2470 H HH   . TYR   B 1 42  ? 25.474 24.346  -23.343 0   30      ? 54  TYR   A HH   1 c 2 
ATOM   2471 N N    . VAL   B 1 43  ? 17.249 22.709  -27.026 1   37.746  ? 55  VAL   A N    1 ? 2 
ATOM   2472 C CA   . VAL   B 1 43  ? 16.147 22.924  -27.953 1   36.794  ? 55  VAL   A CA   1 ? 2 
ATOM   2473 C C    . VAL   B 1 43  ? 15.234 24.046  -27.5   1   37.072  ? 55  VAL   A C    1 ? 2 
ATOM   2474 O O    . VAL   B 1 43  ? 15.262 24.393  -26.35  1   38.463  ? 55  VAL   A O    1 ? 2 
ATOM   2475 C CB   . VAL   B 1 43  ? 15.327 21.626  -28.074 1   35.603  ? 55  VAL   A CB   1 ? 2 
ATOM   2476 C CG1  . VAL   B 1 43  ? 16.197 20.439  -28.485 1   33.076  ? 55  VAL   A CG1  1 ? 2 
ATOM   2477 C CG2  . VAL   B 1 43  ? 14.571 21.287  -26.806 1   35.205  ? 55  VAL   A CG2  1 ? 2 
ATOM   2478 H H    . VAL   B 1 43  ? 17.087 22.695  -26.126 1   37.31   ? 55  VAL   A H    1 c 2 
ATOM   2479 H HA   . VAL   B 1 43  ? 16.51  23.15   -28.829 1   37.598  ? 55  VAL   A HA   1 c 2 
ATOM   2480 H HB   . VAL   B 1 43  ? 14.662 21.77   -28.787 1   34.826  ? 55  VAL   A HB   1 c 2 
ATOM   2481 H HG11 . VAL   B 1 43  ? 16.704 20.128  -27.718 1   33.814  ? 55  VAL   A HG11 1 c 2 
ATOM   2482 H HG12 . VAL   B 1 43  ? 16.809 20.713  -29.189 1   34.58   ? 55  VAL   A HG12 1 c 2 
ATOM   2483 H HG13 . VAL   B 1 43  ? 15.631 19.719  -28.812 1   32.414  ? 55  VAL   A HG13 1 c 2 
ATOM   2484 H HG21 . VAL   B 1 43  ? 14.237 20.378  -26.863 1   33.683  ? 55  VAL   A HG21 1 c 2 
ATOM   2485 H HG22 . VAL   B 1 43  ? 13.823 21.898  -26.697 1   35.29   ? 55  VAL   A HG22 1 c 2 
ATOM   2486 H HG23 . VAL   B 1 43  ? 15.165 21.364  -26.041 1   35.684  ? 55  VAL   A HG23 1 c 2 
ATOM   2487 N N    . HIS   B 1 44  ? 14.364 24.534  -28.406 1   40.518  ? 56  HIS   A N    1 ? 2 
ATOM   2488 C CA   . HIS   B 1 44  ? 13.105 25.172  -28.05  1   37.436  ? 56  HIS   A CA   1 ? 2 
ATOM   2489 C C    . HIS   B 1 44  ? 12.018 24.225  -28.476 1   33.214  ? 56  HIS   A C    1 ? 2 
ATOM   2490 O O    . HIS   B 1 44  ? 12.175 23.537  -29.434 1   33.862  ? 56  HIS   A O    1 ? 2 
ATOM   2491 C CB   . HIS   B 1 44  ? 12.964 26.595  -28.641 1   39.131  ? 56  HIS   A CB   1 ? 2 
ATOM   2492 C CG   . HIS   B 1 44  ? 13.51  27.668  -27.748 1   42.22   ? 56  HIS   A CG   1 ? 2 
ATOM   2493 N ND1  . HIS   B 1 44  ? 13.094 27.867  -26.448 1   42.019  ? 56  HIS   A ND1  1 ? 2 
ATOM   2494 C CD2  . HIS   B 1 44  ? 14.459 28.585  -27.984 1   45.127  ? 56  HIS   A CD2  1 ? 2 
ATOM   2495 C CE1  . HIS   B 1 44  ? 13.751 28.867  -25.943 1   46.818  ? 56  HIS   A CE1  1 ? 2 
ATOM   2496 N NE2  . HIS   B 1 44  ? 14.568 29.336  -26.868 1   45.787  ? 56  HIS   A NE2  1 ? 2 
ATOM   2497 H H    . HIS   B 1 44  ? 14.575 24.462  -29.293 1   39.032  ? 56  HIS   A H    1 c 2 
ATOM   2498 H HA   . HIS   B 1 44  ? 13.077 25.243  -27.066 1   37.585  ? 56  HIS   A HA   1 c 2 
ATOM   2499 H HB2  . HIS   B 1 44  ? 13.435 26.626  -29.503 1   39.972  ? 56  HIS   A HB2  1 c 2 
ATOM   2500 H HB3  . HIS   B 1 44  ? 12.014 26.773  -28.81  1   39.555  ? 56  HIS   A HB3  1 c 2 
ATOM   2501 H HD1  . HIS   B 1 44  ? 12.497 27.371  -26.026 0   30      ? 56  HIS   A HD1  1 c 2 
ATOM   2502 H HD2  . HIS   B 1 44  ? 14.927 28.717  -28.785 1   45.461  ? 56  HIS   A HD2  1 c 2 
ATOM   2503 H HE1  . HIS   B 1 44  ? 13.645 29.211  -25.074 1   46.708  ? 56  HIS   A HE1  1 c 2 
ATOM   2504 H HE2  . HIS   B 1 44  ? 15.043 30.077  -26.76  0   30      ? 56  HIS   A HE2  1 c 2 
ATOM   2505 N N    . TYR   B 1 45  ? 10.895 24.224  -27.757 1   33.181  ? 57  TYR   A N    1 ? 2 
ATOM   2506 C CA   . TYR   B 1 45  ? 9.795  23.365  -28.094 1   29.752  ? 57  TYR   A CA   1 ? 2 
ATOM   2507 C C    . TYR   B 1 45  ? 8.483  23.977  -27.604 1   32.821  ? 57  TYR   A C    1 ? 2 
ATOM   2508 O O    . TYR   B 1 45  ? 8.438  24.666  -26.582 1   33.293  ? 57  TYR   A O    1 ? 2 
ATOM   2509 C CB   . TYR   B 1 45  ? 9.985  21.957  -27.505 1   28.195  ? 57  TYR   A CB   1 ? 2 
ATOM   2510 C CG   . TYR   B 1 45  ? 9.705  21.824  -26.008 1   27.015  ? 57  TYR   A CG   1 ? 2 
ATOM   2511 C CD1  . TYR   B 1 45  ? 8.455  21.596  -25.522 1   27.836  ? 57  TYR   A CD1  1 ? 2 
ATOM   2512 C CD2  . TYR   B 1 45  ? 10.721 22.089  -25.087 1   33.915  ? 57  TYR   A CD2  1 ? 2 
ATOM   2513 C CE1  . TYR   B 1 45  ? 8.186  21.553  -24.16  1   28.97   ? 57  TYR   A CE1  1 ? 2 
ATOM   2514 C CE2  . TYR   B 1 45  ? 10.476 22.062  -23.714 1   32.284  ? 57  TYR   A CE2  1 ? 2 
ATOM   2515 C CZ   . TYR   B 1 45  ? 9.222  21.731  -23.251 1   33.484  ? 57  TYR   A CZ   1 ? 2 
ATOM   2516 O OH   . TYR   B 1 45  ? 8.89   21.737  -21.924 1   30.984  ? 57  TYR   A OH   1 ? 2 
ATOM   2517 H H    . TYR   B 1 45  ? 10.819 24.779  -27.034 1   33.658  ? 57  TYR   A H    1 c 2 
ATOM   2518 H HA   . TYR   B 1 45  ? 9.756  23.29   -29.081 1   30.614  ? 57  TYR   A HA   1 c 2 
ATOM   2519 H HB2  . TYR   B 1 45  ? 9.394  21.339  -27.99  1   26.925  ? 57  TYR   A HB2  1 c 2 
ATOM   2520 H HB3  . TYR   B 1 45  ? 10.91  21.673  -27.678 1   27.63   ? 57  TYR   A HB3  1 c 2 
ATOM   2521 H HD1  . TYR   B 1 45  ? 7.75   21.439  -26.13  1   27.457  ? 57  TYR   A HD1  1 c 2 
ATOM   2522 H HD2  . TYR   B 1 45  ? 11.591 22.282  -25.398 1   32.2    ? 57  TYR   A HD2  1 c 2 
ATOM   2523 H HE1  . TYR   B 1 45  ? 7.319  21.355  -23.856 1   29.635  ? 57  TYR   A HE1  1 c 2 
ATOM   2524 H HE2  . TYR   B 1 45  ? 11.18  22.202  -23.105 1   33.798  ? 57  TYR   A HE2  1 c 2 
ATOM   2525 H HH   . TYR   B 1 45  ? 8.928  20.941  -21.595 0   30      ? 57  TYR   A HH   1 c 2 
ATOM   2526 N N    . LYS   B 1 46  ? 7.413  23.5    -28.244 1   31.845  ? 58  LYS   A N    1 ? 2 
ATOM   2527 C CA   . LYS   B 1 46  ? 6.054  23.637  -27.775 1   30.194  ? 58  LYS   A CA   1 ? 2 
ATOM   2528 C C    . LYS   B 1 46  ? 5.422  22.248  -27.819 1   31.339  ? 58  LYS   A C    1 ? 2 
ATOM   2529 O O    . LYS   B 1 46  ? 5.611  21.532  -28.752 1   30.646  ? 58  LYS   A O    1 ? 2 
ATOM   2530 C CB   . LYS   B 1 46  ? 5.208  24.578  -28.657 1   34.848  ? 58  LYS   A CB   1 ? 2 
ATOM   2531 C CG   . LYS   B 1 46  ? 5.72   25.976  -28.889 1   38.105  ? 58  LYS   A CG   1 ? 2 
ATOM   2532 C CD   . LYS   B 1 46  ? 4.867  26.92   -29.753 1   42.023  ? 58  LYS   A CD   1 ? 2 
ATOM   2533 C CE   . LYS   B 1 46  ? 5.559  28.224  -30.088 1   44.721  ? 58  LYS   A CE   1 ? 2 
ATOM   2534 N NZ   . LYS   B 1 46  ? 4.58   29.012  -30.809 1   45.518  ? 58  LYS   A NZ   1 ? 2 
ATOM   2535 H H    . LYS   B 1 46  ? 7.547  23.059  -29.034 1   30.785  ? 58  LYS   A H    1 c 2 
ATOM   2536 H HA   . LYS   B 1 46  ? 6.066  23.966  -26.842 1   32.206  ? 58  LYS   A HA   1 c 2 
ATOM   2537 H HB2  . LYS   B 1 46  ? 5.097  24.151  -29.534 1   33.903  ? 58  LYS   A HB2  1 c 2 
ATOM   2538 H HB3  . LYS   B 1 46  ? 4.316  24.647  -28.255 1   34.919  ? 58  LYS   A HB3  1 c 2 
ATOM   2539 H HG2  . LYS   B 1 46  ? 5.847  26.397  -28.011 1   38.971  ? 58  LYS   A HG2  1 c 2 
ATOM   2540 H HG3  . LYS   B 1 46  ? 6.609  25.905  -29.299 1   37.855  ? 58  LYS   A HG3  1 c 2 
ATOM   2541 H HD2  . LYS   B 1 46  ? 4.634  26.459  -30.588 1   41.199  ? 58  LYS   A HD2  1 c 2 
ATOM   2542 H HD3  . LYS   B 1 46  ? 4.032  27.116  -29.276 1   42.456  ? 58  LYS   A HD3  1 c 2 
ATOM   2543 H HE2  . LYS   B 1 46  ? 5.831  28.691  -29.278 1   44.94   ? 58  LYS   A HE2  1 c 2 
ATOM   2544 H HE3  . LYS   B 1 46  ? 6.339  28.068  -30.651 1   43.801  ? 58  LYS   A HE3  1 c 2 
ATOM   2545 H HZ1  . LYS   B 1 46  ? 3.88   29.205  -30.268 1   46.776  ? 58  LYS   A HZ1  1 c 2 
ATOM   2546 H HZ2  . LYS   B 1 46  ? 4.282  28.556  -31.533 1   45.6    ? 58  LYS   A HZ2  1 c 2 
ATOM   2547 H HZ3  . LYS   B 1 46  ? 4.961  29.785  -31.085 1   47.971  ? 58  LYS   A HZ3  1 c 2 
ATOM   2548 N N    . GLY   B 1 47  ? 4.713  21.851  -26.78  1   30.139  ? 59  GLY   A N    1 ? 2 
ATOM   2549 C CA   . GLY   B 1 47  ? 4.112  20.547  -26.714 1   28.07   ? 59  GLY   A CA   1 ? 2 
ATOM   2550 C C    . GLY   B 1 47  ? 2.684  20.66   -26.23  1   26.918  ? 59  GLY   A C    1 ? 2 
ATOM   2551 O O    . GLY   B 1 47  ? 2.304  21.584  -25.496 1   29.894  ? 59  GLY   A O    1 ? 2 
ATOM   2552 H H    . GLY   B 1 47  ? 4.597  22.422  -26.076 1   31.156  ? 59  GLY   A H    1 c 2 
ATOM   2553 H HA2  . GLY   B 1 47  ? 4.131  20.13   -27.604 1   27.161  ? 59  GLY   A HA2  1 c 2 
ATOM   2554 H HA3  . GLY   B 1 47  ? 4.631  19.98   -26.096 1   26.891  ? 59  GLY   A HA3  1 c 2 
ATOM   2555 N N    . LYS   B 1 48  ? 1.847  19.73   -26.692 1   27.751  ? 60  LYS   A N    1 ? 2 
ATOM   2556 C CA   . LYS   B 1 48  ? 0.473  19.678  -26.275 1   29.013  ? 60  LYS   A CA   1 ? 2 
ATOM   2557 C C    . LYS   B 1 48  ? -0.069 18.248  -26.363 1   29.061  ? 60  LYS   A C    1 ? 2 
ATOM   2558 O O    . LYS   B 1 48  ? 0.536  17.421  -27.022 1   26.377  ? 60  LYS   A O    1 ? 2 
ATOM   2559 C CB   . LYS   B 1 48  ? -0.372 20.645  -27.091 1   32.61   ? 60  LYS   A CB   1 ? 2 
ATOM   2560 C CG   . LYS   B 1 48  ? -0.361 20.4    -28.561 1   34.497  ? 60  LYS   A CG   1 ? 2 
ATOM   2561 C CD   . LYS   B 1 48  ? -1.373 21.28   -29.299 1   40.429  ? 60  LYS   A CD   1 ? 2 
ATOM   2562 C CE   . LYS   B 1 48  ? -1.283 21.066  -30.785 1   47.727  ? 60  LYS   A CE   1 ? 2 
ATOM   2563 N NZ   . LYS   B 1 48  ? -2.618 21.565  -31.268 1   59.367  ? 60  LYS   A NZ   1 ? 2 
ATOM   2564 H H    . LYS   B 1 48  ? 2.15   19.108  -27.29  1   26.494  ? 60  LYS   A H    1 c 2 
ATOM   2565 H HA   . LYS   B 1 48  ? 0.433  19.96   -25.328 1   30.134  ? 60  LYS   A HA   1 c 2 
ATOM   2566 H HB2  . LYS   B 1 48  ? -1.3   20.596  -26.776 1   33.713  ? 60  LYS   A HB2  1 c 2 
ATOM   2567 H HB3  . LYS   B 1 48  ? -0.05  21.557  -26.927 1   33.682  ? 60  LYS   A HB3  1 c 2 
ATOM   2568 H HG2  . LYS   B 1 48  ? 0.54   20.583  -28.907 1   34.025  ? 60  LYS   A HG2  1 c 2 
ATOM   2569 H HG3  . LYS   B 1 48  ? -0.569 19.456  -28.73  1   33.803  ? 60  LYS   A HG3  1 c 2 
ATOM   2570 H HD2  . LYS   B 1 48  ? -2.28  21.06   -28.991 1   42.02   ? 60  LYS   A HD2  1 c 2 
ATOM   2571 H HD3  . LYS   B 1 48  ? -1.195 22.224  -29.096 1   42.19   ? 60  LYS   A HD3  1 c 2 
ATOM   2572 H HE2  . LYS   B 1 48  ? -0.562 21.589  -31.179 1   47.762  ? 60  LYS   A HE2  1 c 2 
ATOM   2573 H HE3  . LYS   B 1 48  ? -1.174 20.123  -31.005 1   46.357  ? 60  LYS   A HE3  1 c 2 
ATOM   2574 H HZ1  . LYS   B 1 48  ? -2.799 22.376  -30.906 1   57.4    ? 60  LYS   A HZ1  1 c 2 
ATOM   2575 H HZ2  . LYS   B 1 48  ? -3.27  20.98   -31.035 1   56.074  ? 60  LYS   A HZ2  1 c 2 
ATOM   2576 H HZ3  . LYS   B 1 48  ? -2.602 21.643  -32.17  1   56.935  ? 60  LYS   A HZ3  1 c 2 
ATOM   2577 N N    . LEU   B 1 49  ? -1.158 17.975  -25.64  1   28.594  ? 61  LEU   A N    1 ? 2 
ATOM   2578 C CA   . LEU   B 1 49  ? -1.923 16.746  -25.869 1   31.733  ? 61  LEU   A CA   1 ? 2 
ATOM   2579 C C    . LEU   B 1 49  ? -2.56  16.91   -27.245 1   42.151  ? 61  LEU   A C    1 ? 2 
ATOM   2580 O O    . LEU   B 1 49  ? -2.788 18.053  -27.693 1   37.728  ? 61  LEU   A O    1 ? 2 
ATOM   2581 C CB   . LEU   B 1 49  ? -2.96  16.505  -24.785 1   35.405  ? 61  LEU   A CB   1 ? 2 
ATOM   2582 C CG   . LEU   B 1 49  ? -2.38  16.414  -23.371 1   40.253  ? 61  LEU   A CG   1 ? 2 
ATOM   2583 C CD1  . LEU   B 1 49  ? -3.527 16.124  -22.362 1   46.8    ? 61  LEU   A CD1  1 ? 2 
ATOM   2584 C CD2  . LEU   B 1 49  ? -1.313 15.39   -23.359 1   43.185  ? 61  LEU   A CD2  1 ? 2 
ATOM   2585 H H    . LEU   B 1 49  ? -1.437 18.562  -24.997 1   30.844  ? 61  LEU   A H    1 c 2 
ATOM   2586 H HA   . LEU   B 1 49  ? -1.293 15.983  -25.898 1   31.773  ? 61  LEU   A HA   1 c 2 
ATOM   2587 H HB2  . LEU   B 1 49  ? -3.613 17.242  -24.81  1   37.339  ? 61  LEU   A HB2  1 c 2 
ATOM   2588 H HB3  . LEU   B 1 49  ? -3.431 15.664  -24.986 1   35.962  ? 61  LEU   A HB3  1 c 2 
ATOM   2589 H HG   . LEU   B 1 49  ? -1.976 17.29   -23.141 1   40.963  ? 61  LEU   A HG   1 c 2 
ATOM   2590 H HD11 . LEU   B 1 49  ? -4.179 16.844  -22.395 1   46.803  ? 61  LEU   A HD11 1 c 2 
ATOM   2591 H HD12 . LEU   B 1 49  ? -3.161 16.061  -21.464 1   45.603  ? 61  LEU   A HD12 1 c 2 
ATOM   2592 H HD13 . LEU   B 1 49  ? -3.96  15.285  -22.594 1   45.369  ? 61  LEU   A HD13 1 c 2 
ATOM   2593 H HD21 . LEU   B 1 49  ? -0.482 15.781  -23.677 1   40.585  ? 61  LEU   A HD21 1 c 2 
ATOM   2594 H HD22 . LEU   B 1 49  ? -1.564 14.649  -23.937 1   40.978  ? 61  LEU   A HD22 1 c 2 
ATOM   2595 H HD23 . LEU   B 1 49  ? -1.189 15.062  -22.453 1   41.895  ? 61  LEU   A HD23 1 c 2 
ATOM   2596 N N    . SER   B 1 50  ? -2.633 15.828  -28.013 1   38.216  ? 62  SER   A N    1 ? 2 
ATOM   2597 C CA   . SER   B 1 50  ? -3.278 15.94   -29.32  1   45.595  ? 62  SER   A CA   1 ? 2 
ATOM   2598 C C    . SER   B 1 50  ? -4.679 16.562  -29.173 1   43.769  ? 62  SER   A C    1 ? 2 
ATOM   2599 O O    . SER   B 1 50  ? -5.085 17.367  -29.981 1   55.088  ? 62  SER   A O    1 ? 2 
ATOM   2600 C CB   . SER   B 1 50  ? -3.323 14.548  -30.014 1   45.626  ? 62  SER   A CB   1 ? 2 
ATOM   2601 O OG   . SER   B 1 50  ? -4.34  13.794  -29.351 1   46.583  ? 62  SER   A OG   1 ? 2 
ATOM   2602 H H    . SER   B 1 50  ? -2.29  15.027  -27.737 1   39.308  ? 62  SER   A H    1 c 2 
ATOM   2603 H HA   . SER   B 1 50  ? -2.73  16.547  -29.879 1   43.352  ? 62  SER   A HA   1 c 2 
ATOM   2604 H HB2  . SER   B 1 50  ? -3.542 14.652  -30.96  1   46.228  ? 62  SER   A HB2  1 c 2 
ATOM   2605 H HB3  . SER   B 1 50  ? -2.46  14.101  -29.926 1   43.99   ? 62  SER   A HB3  1 c 2 
ATOM   2606 H HG   . SER   B 1 50  ? -4.284 13.015  -29.74  0   30      ? 62  SER   A HG   1 c 2 
ATOM   2607 N N    . ASN   B 1 51  ? -5.428 16.204  -28.121 1   56.816  ? 63  ASN   A N    1 ? 2 
ATOM   2608 C CA   . ASN   B 1 51  ? -6.667 16.842  -27.637 1   54.67   ? 63  ASN   A CA   1 ? 2 
ATOM   2609 C C    . ASN   B 1 51  ? -6.56  18.311  -27.209 1   58.56   ? 63  ASN   A C    1 ? 2 
ATOM   2610 O O    . ASN   B 1 51  ? -7.518 18.864  -26.708 1   62.052  ? 63  ASN   A O    1 ? 2 
ATOM   2611 C CB   . ASN   B 1 51  ? -7.084 16.253  -26.288 1   52.987  ? 63  ASN   A CB   1 ? 2 
ATOM   2612 H H    . ASN   B 1 51  ? -5.138 15.471  -27.657 1   51.328  ? 63  ASN   A H    1 c 2 
ATOM   2613 H HA   . ASN   B 1 51  ? -7.396 16.713  -28.285 1   56.907  ? 63  ASN   A HA   1 c 2 
ATOM   2614 H HB2  . ASN   B 1 51  ? -6.32  15.923  -25.781 0   30      ? 63  ASN   A HB2  1 c 2 
ATOM   2615 H HB3  . ASN   B 1 51  ? -8.083 16.157  -26.278 0   30      ? 63  ASN   A HB3  1 c 2 
ATOM   2616 N N    . GLY   B 1 52  ? -5.39  18.95   -27.335 1   65.255  ? 64  GLY   A N    1 ? 2 
ATOM   2617 C CA   . GLY   B 1 52  ? -5.188 20.367  -27.055 1   61.594  ? 64  GLY   A CA   1 ? 2 
ATOM   2618 C C    . GLY   B 1 52  ? -5.567 20.836  -25.647 1   71.163  ? 64  GLY   A C    1 ? 2 
ATOM   2619 O O    . GLY   B 1 52  ? -5.789 22.034  -25.46  1   68.248  ? 64  GLY   A O    1 ? 2 
ATOM   2620 H H    . GLY   B 1 52  ? -4.665 18.468  -27.607 1   60.065  ? 64  GLY   A H    1 c 2 
ATOM   2621 H HA2  . GLY   B 1 52  ? -4.237 20.577  -27.21  1   63.228  ? 64  GLY   A HA2  1 c 2 
ATOM   2622 H HA3  . GLY   B 1 52  ? -5.711 20.887  -27.71  1   66.07   ? 64  GLY   A HA3  1 c 2 
ATOM   2623 N N    . LYS   B 1 53  ? -5.572 19.944  -24.642 1   72.093  ? 65  LYS   A N    1 ? 2 
ATOM   2624 C CA   . LYS   B 1 53  ? -6.068 20.263  -23.298 1   65.334  ? 65  LYS   A CA   1 ? 2 
ATOM   2625 C C    . LYS   B 1 53  ? -4.966 20.808  -22.343 1   56.922  ? 65  LYS   A C    1 ? 2 
ATOM   2626 O O    . LYS   B 1 53  ? -5.245 21.522  -21.385 1   58.741  ? 65  LYS   A O    1 ? 2 
ATOM   2627 C CB   . LYS   B 1 53  ? -6.798 18.986  -22.858 1   68.671  ? 65  LYS   A CB   1 ? 2 
ATOM   2628 H H    . LYS   B 1 53  ? -5.235 19.108  -24.794 1   67.796  ? 65  LYS   A H    1 c 2 
ATOM   2629 H HA   . LYS   B 1 53  ? -6.757 20.969  -23.391 1   68.008  ? 65  LYS   A HA   1 c 2 
ATOM   2630 H HB2  . LYS   B 1 53  ? -6.147 18.313  -22.683 0   30      ? 65  LYS   A HB2  1 c 2 
ATOM   2631 H HB3  . LYS   B 1 53  ? -7.752 19.202  -22.981 0   30      ? 65  LYS   A HB3  1 c 2 
ATOM   2632 N N    . LYS   B 1 54  ? -3.699 20.5    -22.603 1   46.903  ? 66  LYS   A N    1 ? 2 
ATOM   2633 C CA   . LYS   B 1 54  ? -2.553 20.965  -21.84  1   44.696  ? 66  LYS   A CA   1 ? 2 
ATOM   2634 C C    . LYS   B 1 54  ? -1.487 21.393  -22.862 1   51.183  ? 66  LYS   A C    1 ? 2 
ATOM   2635 O O    . LYS   B 1 54  ? -1.29  20.693  -23.859 1   49.818  ? 66  LYS   A O    1 ? 2 
ATOM   2636 C CB   . LYS   B 1 54  ? -2.165 19.724  -21.019 1   46.581  ? 66  LYS   A CB   1 ? 2 
ATOM   2637 H H    . LYS   B 1 54  ? -3.536 19.95   -23.315 1   47.004  ? 66  LYS   A H    1 c 2 
ATOM   2638 H HA   . LYS   B 1 54  ? -2.815 21.728  -21.266 1   48.84   ? 66  LYS   A HA   1 c 2 
ATOM   2639 H HB2  . LYS   B 1 54  ? -1.152 19.675  -20.946 0   30      ? 66  LYS   A HB2  1 c 2 
ATOM   2640 H HB3  . LYS   B 1 54  ? -2.947 19.276  -20.676 0   30      ? 66  LYS   A HB3  1 c 2 
ATOM   2641 N N    . PHE   B 1 55  ? -0.812 22.515  -22.632 1   44.418  ? 67  PHE   A N    1 ? 2 
ATOM   2642 C CA   . PHE   B 1 55  ? 0.16   23.116  -23.526 1   42.449  ? 67  PHE   A CA   1 ? 2 
ATOM   2643 C C    . PHE   B 1 55  ? 1.396  23.448  -22.686 1   43.266  ? 67  PHE   A C    1 ? 2 
ATOM   2644 O O    . PHE   B 1 55  ? 1.238  23.727  -21.508 1   48.813  ? 67  PHE   A O    1 ? 2 
ATOM   2645 C CB   . PHE   B 1 55  ? -0.499 24.359  -24.145 1   45.68   ? 67  PHE   A CB   1 ? 2 
ATOM   2646 C CG   . PHE   B 1 55  ? 0.204  24.93   -25.385 1   55.923  ? 67  PHE   A CG   1 ? 2 
ATOM   2647 C CD1  . PHE   B 1 55  ? -0.103 24.454  -26.661 1   59.893  ? 67  PHE   A CD1  1 ? 2 
ATOM   2648 C CD2  . PHE   B 1 55  ? 1.099  26.011  -25.295 1   66.369  ? 67  PHE   A CD2  1 ? 2 
ATOM   2649 C CE1  . PHE   B 1 55  ? 0.498  25.001  -27.805 1   68.556  ? 67  PHE   A CE1  1 ? 2 
ATOM   2650 C CE2  . PHE   B 1 55  ? 1.682  26.58   -26.441 1   72.267  ? 67  PHE   A CE2  1 ? 2 
ATOM   2651 C CZ   . PHE   B 1 55  ? 1.369  26.081  -27.699 1   71.811  ? 67  PHE   A CZ   1 ? 2 
ATOM   2652 H H    . PHE   B 1 55  ? -0.975 22.945  -21.842 1   47.169  ? 67  PHE   A H    1 c 2 
ATOM   2653 H HA   . PHE   B 1 55  ? 0.4    22.472  -24.241 1   41.39   ? 67  PHE   A HA   1 c 2 
ATOM   2654 H HB2  . PHE   B 1 55  ? -1.422 24.129  -24.388 1   48.247  ? 67  PHE   A HB2  1 c 2 
ATOM   2655 H HB3  . PHE   B 1 55  ? -0.542 25.061  -23.458 1   49.257  ? 67  PHE   A HB3  1 c 2 
ATOM   2656 H HD1  . PHE   B 1 55  ? -0.711 23.738  -26.753 1   59.61   ? 67  PHE   A HD1  1 c 2 
ATOM   2657 H HD2  . PHE   B 1 55  ? 1.297  26.375  -24.446 1   65.961  ? 67  PHE   A HD2  1 c 2 
ATOM   2658 H HE1  . PHE   B 1 55  ? 0.282  24.655  -28.656 1   66.485  ? 67  PHE   A HE1  1 c 2 
ATOM   2659 H HE2  . PHE   B 1 55  ? 2.292  27.295  -26.355 1   71.825  ? 67  PHE   A HE2  1 c 2 
ATOM   2660 H HZ   . PHE   B 1 55  ? 1.786  26.434  -28.469 1   71.464  ? 67  PHE   A HZ   1 c 2 
ATOM   2661 N N    . ASP   B 1 56  ? 2.592  23.299  -23.238 1   35.579  ? 68  ASP   A N    1 ? 2 
ATOM   2662 C CA   . ASP   B 1 56  ? 3.828  23.541  -22.548 1   37.656  ? 68  ASP   A CA   1 ? 2 
ATOM   2663 C C    . ASP   B 1 56  ? 4.819  24.092  -23.567 1   35.335  ? 68  ASP   A C    1 ? 2 
ATOM   2664 O O    . ASP   B 1 56  ? 5.05   23.467  -24.601 1   36.986  ? 68  ASP   A O    1 ? 2 
ATOM   2665 C CB   . ASP   B 1 56  ? 4.296  22.226  -21.948 1   33.31   ? 68  ASP   A CB   1 ? 2 
ATOM   2666 C CG   . ASP   B 1 56  ? 5.664  22.27   -21.302 1   35.06   ? 68  ASP   A CG   1 ? 2 
ATOM   2667 O OD1  . ASP   B 1 56  ? 5.991  23.274  -20.563 1   34.189  ? 68  ASP   A OD1  1 ? 2 
ATOM   2668 O OD2  . ASP   B 1 56  ? 6.446  21.354  -21.584 1   36.482  ? 68  ASP   A OD2  1 ? 2 
ATOM   2669 H H    . ASP   B 1 56  ? 2.634  23.024  -24.109 1   36.46   ? 68  ASP   A H    1 c 2 
ATOM   2670 H HA   . ASP   B 1 56  ? 3.678  24.207  -21.839 1   38.19   ? 68  ASP   A HA   1 c 2 
ATOM   2671 H HB2  . ASP   B 1 56  ? 3.647  21.946  -21.269 1   34.775  ? 68  ASP   A HB2  1 c 2 
ATOM   2672 H HB3  . ASP   B 1 56  ? 4.308  21.545  -22.653 1   32.795  ? 68  ASP   A HB3  1 c 2 
ATOM   2673 N N    . SER   B 1 57  ? 5.482  25.202  -23.272 1   37.539  ? 69  SER   A N    1 ? 2 
ATOM   2674 C CA   . SER   B 1 57  ? 6.558  25.66   -24.151 1   40.643  ? 69  SER   A CA   1 ? 2 
ATOM   2675 C C    . SER   B 1 57  ? 7.759  26.303  -23.412 1   37.028  ? 69  SER   A C    1 ? 2 
ATOM   2676 O O    . SER   B 1 57  ? 7.624  27.105  -22.501 1   39.685  ? 69  SER   A O    1 ? 2 
ATOM   2677 C CB   . SER   B 1 57  ? 6.093  26.611  -25.227 1   46.374  ? 69  SER   A CB   1 ? 2 
ATOM   2678 O OG   . SER   B 1 57  ? 5.698  27.815  -24.628 1   51.931  ? 69  SER   A OG   1 ? 2 
ATOM   2679 H H    . SER   B 1 57  ? 5.273  25.685  -22.525 1   39.589  ? 69  SER   A H    1 c 2 
ATOM   2680 H HA   . SER   B 1 57  ? 6.907  24.857  -24.61  1   37.812  ? 69  SER   A HA   1 c 2 
ATOM   2681 H HB2  . SER   B 1 57  ? 6.819  26.776  -25.857 1   45.84   ? 69  SER   A HB2  1 c 2 
ATOM   2682 H HB3  . SER   B 1 57  ? 5.34   26.219  -25.709 1   45.264  ? 69  SER   A HB3  1 c 2 
ATOM   2683 H HG   . SER   B 1 57  ? 5.34   28.321  -25.185 0   30      ? 69  SER   A HG   1 c 2 
ATOM   2684 N N    . SER   B 1 58  ? 8.949  25.983  -23.941 1   35.137  ? 70  SER   A N    1 ? 2 
ATOM   2685 C CA   . SER   B 1 58  ? 10.179 26.563  -23.476 1   38.527  ? 70  SER   A CA   1 ? 2 
ATOM   2686 C C    . SER   B 1 58  ? 10.194 28.072  -23.698 1   41.738  ? 70  SER   A C    1 ? 2 
ATOM   2687 O O    . SER   B 1 58  ? 10.867 28.826  -22.992 1   44.873  ? 70  SER   A O    1 ? 2 
ATOM   2688 C CB   . SER   B 1 58  ? 11.302 25.861  -24.141 1   36.777  ? 70  SER   A CB   1 ? 2 
ATOM   2689 O OG   . SER   B 1 58  ? 11.248 25.963  -25.553 1   41.123  ? 70  SER   A OG   1 ? 2 
ATOM   2690 H H    . SER   B 1 58  ? 8.984  25.377  -24.624 1   34.375  ? 70  SER   A H    1 c 2 
ATOM   2691 H HA   . SER   B 1 58  ? 10.245 26.396  -22.502 1   38.48   ? 70  SER   A HA   1 c 2 
ATOM   2692 H HB2  . SER   B 1 58  ? 12.144 26.238  -23.825 1   39.007  ? 70  SER   A HB2  1 c 2 
ATOM   2693 H HB3  . SER   B 1 58  ? 11.283 24.919  -23.887 1   36.284  ? 70  SER   A HB3  1 c 2 
ATOM   2694 H HG   . SER   B 1 58  ? 11.919 25.562  -25.875 0   30      ? 70  SER   A HG   1 c 2 
ATOM   2695 N N    . HIS   B 1 59  ? 9.488  28.533  -24.727 1   42.867  ? 71  HIS   A N    1 ? 2 
ATOM   2696 C CA   . HIS   B 1 59  ? 9.494  29.925  -25.123 1   49.171  ? 71  HIS   A CA   1 ? 2 
ATOM   2697 C C    . HIS   B 1 59  ? 8.807  30.743  -24.042 1   54.963  ? 71  HIS   A C    1 ? 2 
ATOM   2698 O O    . HIS   B 1 59  ? 9.152  31.892  -23.801 1   55.219  ? 71  HIS   A O    1 ? 2 
ATOM   2699 C CB   . HIS   B 1 59  ? 8.736  30.12   -26.433 1   51.23   ? 71  HIS   A CB   1 ? 2 
ATOM   2700 C CG   . HIS   B 1 59  ? 9.544  29.73   -27.621 1   56.86   ? 71  HIS   A CG   1 ? 2 
ATOM   2701 N ND1  . HIS   B 1 59  ? 10.736 30.344  -27.944 1   59.828  ? 71  HIS   A ND1  1 ? 2 
ATOM   2702 C CD2  . HIS   B 1 59  ? 9.344  28.748  -28.519 1   57.376  ? 71  HIS   A CD2  1 ? 2 
ATOM   2703 C CE1  . HIS   B 1 59  ? 11.21  29.756  -29.029 1   59.061  ? 71  HIS   A CE1  1 ? 2 
ATOM   2704 N NE2  . HIS   B 1 59  ? 10.375 28.784  -29.38  1   57.054  ? 71  HIS   A NE2  1 ? 2 
ATOM   2705 H H    . HIS   B 1 59  ? 8.988  27.947  -25.218 1   41.889  ? 71  HIS   A H    1 c 2 
ATOM   2706 H HA   . HIS   B 1 59  ? 10.428 30.237  -25.215 1   50.274  ? 71  HIS   A HA   1 c 2 
ATOM   2707 H HB2  . HIS   B 1 59  ? 7.916  29.581  -26.41  1   50.905  ? 71  HIS   A HB2  1 c 2 
ATOM   2708 H HB3  . HIS   B 1 59  ? 8.481  31.065  -26.515 1   54.668  ? 71  HIS   A HB3  1 c 2 
ATOM   2709 H HD1  . HIS   B 1 59  ? 10.949 30.643  -27.928 0   30      ? 71  HIS   A HD1  1 c 2 
ATOM   2710 H HD2  . HIS   B 1 59  ? 8.618  28.155  -28.552 1   55.174  ? 71  HIS   A HD2  1 c 2 
ATOM   2711 H HE1  . HIS   B 1 59  ? 12.009 29.985  -29.472 1   59.901  ? 71  HIS   A HE1  1 c 2 
ATOM   2712 H HE2  . HIS   B 1 59  ? 9.814  27.667  -30.043 0   30      ? 71  HIS   A HE2  1 c 2 
ATOM   2713 N N    . ASP   B 1 60  ? 7.818  30.135  -23.38  1   54.01   ? 72  ASP   A N    1 ? 2 
ATOM   2714 C CA   . ASP   B 1 60  ? 7.145  30.793  -22.268 1   59.576  ? 72  ASP   A CA   1 ? 2 
ATOM   2715 C C    . ASP   B 1 60  ? 8.098  31.108  -21.128 1   56.037  ? 72  ASP   A C    1 ? 2 
ATOM   2716 O O    . ASP   B 1 60  ? 7.794  31.988  -20.362 1   59.29   ? 72  ASP   A O    1 ? 2 
ATOM   2717 C CB   . ASP   B 1 60  ? 6.086  29.904  -21.648 1   62.713  ? 72  ASP   A CB   1 ? 2 
ATOM   2718 C CG   . ASP   B 1 60  ? 4.783  29.951  -22.396 1   64.932  ? 72  ASP   A CG   1 ? 2 
ATOM   2719 O OD1  . ASP   B 1 60  ? 4.428  31.09   -22.805 1   84.243  ? 72  ASP   A OD1  1 ? 2 
ATOM   2720 O OD2  . ASP   B 1 60  ? 4.107  28.894  -22.43  1   67.063  ? 72  ASP   A OD2  1 ? 2 
ATOM   2721 H H    . ASP   B 1 60  ? 7.546  29.3    -23.631 1   52.41   ? 72  ASP   A H    1 c 2 
ATOM   2722 H HA   . ASP   B 1 60  ? 6.743  31.631  -22.591 1   60.974  ? 72  ASP   A HA   1 c 2 
ATOM   2723 H HB2  . ASP   B 1 60  ? 6.404  28.979  -21.625 1   59.546  ? 72  ASP   A HB2  1 c 2 
ATOM   2724 H HB3  . ASP   B 1 60  ? 5.914  30.188  -20.726 1   63.5    ? 72  ASP   A HB3  1 c 2 
ATOM   2725 N N    . ARG   B 1 61  ? 9.17   30.343  -20.98  1   50.588  ? 73  ARG   A N    1 ? 2 
ATOM   2726 C CA   . ARG   B 1 61  ? 10.217 30.576  -19.999 1   56.805  ? 73  ARG   A CA   1 ? 2 
ATOM   2727 C C    . ARG   B 1 61  ? 11.376 31.365  -20.618 1   57.508  ? 73  ARG   A C    1 ? 2 
ATOM   2728 O O    . ARG   B 1 61  ? 12.357 31.642  -19.933 1   55.844  ? 73  ARG   A O    1 ? 2 
ATOM   2729 C CB   . ARG   B 1 61  ? 10.631 29.204  -19.442 1   55.484  ? 73  ARG   A CB   1 ? 2 
ATOM   2730 C CG   . ARG   B 1 61  ? 9.409  28.5    -18.829 1   59.139  ? 73  ARG   A CG   1 ? 2 
ATOM   2731 C CD   . ARG   B 1 61  ? 9.535  27.055  -18.395 1   54.049  ? 73  ARG   A CD   1 ? 2 
ATOM   2732 N NE   . ARG   B 1 61  ? 10     26.137  -19.438 1   52.812  ? 73  ARG   A NE   1 ? 2 
ATOM   2733 C CZ   . ARG   B 1 61  ? 9.286  25.153  -20.019 1   48.799  ? 73  ARG   A CZ   1 ? 2 
ATOM   2734 N NH1  . ARG   B 1 61  ? 7.954  25.111  -19.953 1   44.543  ? 73  ARG   A NH1  1 ? 2 
ATOM   2735 N NH2  . ARG   B 1 61  ? 9.941  24.24   -20.718 1   43.849  ? 73  ARG   A NH2  1 ? 2 
ATOM   2736 H H    . ARG   B 1 61  ? 9.25   29.609  -21.518 1   50.225  ? 73  ARG   A H    1 c 2 
ATOM   2737 H HA   . ARG   B 1 61  ? 9.836  31.11   -19.256 1   58.061  ? 73  ARG   A HA   1 c 2 
ATOM   2738 H HB2  . ARG   B 1 61  ? 11     28.651  -20.163 1   54.163  ? 73  ARG   A HB2  1 c 2 
ATOM   2739 H HB3  . ARG   B 1 61  ? 11.321 29.32   -18.755 1   57.425  ? 73  ARG   A HB3  1 c 2 
ATOM   2740 H HG2  . ARG   B 1 61  ? 9.12   29.024  -18.05  1   59.58   ? 73  ARG   A HG2  1 c 2 
ATOM   2741 H HG3  . ARG   B 1 61  ? 8.671  28.554  -19.473 1   56.605  ? 73  ARG   A HG3  1 c 2 
ATOM   2742 H HD2  . ARG   B 1 61  ? 10.156 27.015  -17.639 1   56.08   ? 73  ARG   A HD2  1 c 2 
ATOM   2743 H HD3  . ARG   B 1 61  ? 8.662  26.753  -18.07  1   54.794  ? 73  ARG   A HD3  1 c 2 
ATOM   2744 H HE   . ARG   B 1 61  ? 10.821 26.238  -19.713 1   52.026  ? 73  ARG   A HE   1 c 2 
ATOM   2745 H HH11 . ARG   B 1 61  ? 7.486  25.853  -20.062 1   47.077  ? 73  ARG   A HH11 1 c 2 
ATOM   2746 H HH12 . ARG   B 1 61  ? 7.546  24.342  -19.801 1   44.662  ? 73  ARG   A HH12 1 c 2 
ATOM   2747 H HH21 . ARG   B 1 61  ? 10.782 24.379  -20.954 1   44.865  ? 73  ARG   A HH21 1 c 2 
ATOM   2748 H HH22 . ARG   B 1 61  ? 9.533  23.491  -20.949 1   43.128  ? 73  ARG   A HH22 1 c 2 
ATOM   2749 N N    . ASN   B 1 62  ? 11.249 31.665  -21.927 1   57.505  ? 74  ASN   A N    1 ? 2 
ATOM   2750 C CA   . ASN   B 1 62  ? 12.233 32.36   -22.766 1   58.569  ? 74  ASN   A CA   1 ? 2 
ATOM   2751 C C    . ASN   B 1 62  ? 13.656 31.818  -22.563 1   55.77   ? 74  ASN   A C    1 ? 2 
ATOM   2752 O O    . ASN   B 1 62  ? 14.622 32.585  -22.63  1   58.957  ? 74  ASN   A O    1 ? 2 
ATOM   2753 C CB   . ASN   B 1 62  ? 11.987 33.86   -22.634 1   63.337  ? 74  ASN   A CB   1 ? 2 
ATOM   2754 C CG   . ASN   B 1 62  ? 12.705 34.712  -23.667 1   63.932  ? 74  ASN   A CG   1 ? 2 
ATOM   2755 O OD1  . ASN   B 1 62  ? 12.716 34.398  -24.86  1   65.721  ? 74  ASN   A OD1  1 ? 2 
ATOM   2756 N ND2  . ASN   B 1 62  ? 13.354 35.771  -23.238 1   66.253  ? 74  ASN   A ND2  1 ? 2 
ATOM   2757 H H    . ASN   B 1 62  ? 10.474 31.412  -22.335 1   56.124  ? 74  ASN   A H    1 c 2 
ATOM   2758 H HA   . ASN   B 1 62  ? 12     32.137  -23.696 1   57.098  ? 74  ASN   A HA   1 c 2 
ATOM   2759 H HB2  . ASN   B 1 62  ? 11.026 34.027  -22.706 1   63.094  ? 74  ASN   A HB2  1 c 2 
ATOM   2760 H HB3  . ASN   B 1 62  ? 12.269 34.145  -21.742 1   64.44   ? 74  ASN   A HB3  1 c 2 
ATOM   2761 H HD21 . ASN   B 1 62  ? 13.984 36.138  -23.743 1   67.997  ? 74  ASN   A HD21 1 c 2 
ATOM   2762 H HD22 . ASN   B 1 62  ? 13.161 36.122  -22.446 1   68.355  ? 74  ASN   A HD22 1 c 2 
ATOM   2763 N N    . GLU   B 1 63  ? 13.793 30.493  -22.367 1   53.401  ? 75  GLU   A N    1 ? 2 
ATOM   2764 C CA   . GLU   B 1 63  ? 15.103 29.861  -22.211 1   51.416  ? 75  GLU   A CA   1 ? 2 
ATOM   2765 C C    . GLU   B 1 63  ? 15.073 28.462  -22.821 1   46.233  ? 75  GLU   A C    1 ? 2 
ATOM   2766 O O    . GLU   B 1 63  ? 14.075 27.779  -22.791 1   38.506  ? 75  GLU   A O    1 ? 2 
ATOM   2767 C CB   . GLU   B 1 63  ? 15.573 29.627  -20.775 1   53.694  ? 75  GLU   A CB   1 ? 2 
ATOM   2768 C CG   . GLU   B 1 63  ? 15.978 30.925  -20.086 1   57.286  ? 75  GLU   A CG   1 ? 2 
ATOM   2769 C CD   . GLU   B 1 63  ? 17.128 31.725  -20.7   1   62.581  ? 75  GLU   A CD   1 ? 2 
ATOM   2770 O OE1  . GLU   B 1 63  ? 17.128 32.94   -20.481 1   70.466  ? 75  GLU   A OE1  1 ? 2 
ATOM   2771 O OE2  . GLU   B 1 63  ? 18.053 31.214  -21.356 1   64.582  ? 75  GLU   A OE2  1 ? 2 
ATOM   2772 H H    . GLU   B 1 63  ? 13.048 29.965  -22.341 1   51.231  ? 75  GLU   A H    1 c 2 
ATOM   2773 H HA   . GLU   B 1 63  ? 15.772 30.407  -22.692 1   53.121  ? 75  GLU   A HA   1 c 2 
ATOM   2774 H HB2  . GLU   B 1 63  ? 14.85  29.199  -20.269 1   52.261  ? 75  GLU   A HB2  1 c 2 
ATOM   2775 H HB3  . GLU   B 1 63  ? 16.338 29.014  -20.783 1   52.475  ? 75  GLU   A HB3  1 c 2 
ATOM   2776 H HG2  . GLU   B 1 63  ? 15.192 31.511  -20.047 1   59.033  ? 75  GLU   A HG2  1 c 2 
ATOM   2777 H HG3  . GLU   B 1 63  ? 16.219 30.718  -19.158 1   58.814  ? 75  GLU   A HG3  1 c 2 
ATOM   2778 N N    . PRO   B 1 64  ? 16.177 27.97   -23.416 1   46.22   ? 76  PRO   A N    1 ? 2 
ATOM   2779 C CA   . PRO   B 1 64  ? 16.148 26.642  -24.033 1   44.08   ? 76  PRO   A CA   1 ? 2 
ATOM   2780 C C    . PRO   B 1 64  ? 15.986 25.551  -22.967 1   43.284  ? 76  PRO   A C    1 ? 2 
ATOM   2781 O O    . PRO   B 1 64  ? 16.337 25.76   -21.83  1   45.14   ? 76  PRO   A O    1 ? 2 
ATOM   2782 C CB   . PRO   B 1 64  ? 17.467 26.542  -24.776 1   45.516  ? 76  PRO   A CB   1 ? 2 
ATOM   2783 C CG   . PRO   B 1 64  ? 18.16  27.872  -24.622 1   50.412  ? 76  PRO   A CG   1 ? 2 
ATOM   2784 C CD   . PRO   B 1 64  ? 17.462 28.653  -23.52  1   51.496  ? 76  PRO   A CD   1 ? 2 
ATOM   2785 H HA   . PRO   B 1 64  ? 15.399 26.599  -24.679 1   43.077  ? 76  PRO   A HA   1 c 2 
ATOM   2786 H HB2  . PRO   B 1 64  ? 18.022 25.819  -24.401 1   45.092  ? 76  PRO   A HB2  1 c 2 
ATOM   2787 H HB3  . PRO   B 1 64  ? 17.31  26.342  -25.725 1   44.807  ? 76  PRO   A HB3  1 c 2 
ATOM   2788 H HG2  . PRO   B 1 64  ? 19.103 27.737  -24.392 1   50.891  ? 76  PRO   A HG2  1 c 2 
ATOM   2789 H HG3  . PRO   B 1 64  ? 18.121 28.371  -25.465 1   50.66   ? 76  PRO   A HG3  1 c 2 
ATOM   2790 H HD2  . PRO   B 1 64  ? 17.963 28.602  -22.676 1   51.917  ? 76  PRO   A HD2  1 c 2 
ATOM   2791 H HD3  . PRO   B 1 64  ? 17.348 29.595  -23.776 1   52.809  ? 76  PRO   A HD3  1 c 2 
ATOM   2792 N N    . PHE   B 1 65  ? 15.487 24.39   -23.4   1   38.121  ? 77  PHE   A N    1 ? 2 
ATOM   2793 C CA   . PHE   B 1 65  ? 15.324 23.175  -22.644 1   37.716  ? 77  PHE   A CA   1 ? 2 
ATOM   2794 C C    . PHE   B 1 65  ? 16.548 22.318  -23     1   40.241  ? 77  PHE   A C    1 ? 2 
ATOM   2795 O O    . PHE   B 1 65  ? 16.94  22.146  -24.185 1   35.024  ? 77  PHE   A O    1 ? 2 
ATOM   2796 C CB   . PHE   B 1 65  ? 14.082 22.427  -23.112 1   33.539  ? 77  PHE   A CB   1 ? 2 
ATOM   2797 C CG   . PHE   B 1 65  ? 13.852 21.119  -22.408 1   32.371  ? 77  PHE   A CG   1 ? 2 
ATOM   2798 C CD1  . PHE   B 1 65  ? 13.557 21.054  -21.065 1   35.044  ? 77  PHE   A CD1  1 ? 2 
ATOM   2799 C CD2  . PHE   B 1 65  ? 14.123 19.95   -23.074 1   27.813  ? 77  PHE   A CD2  1 ? 2 
ATOM   2800 C CE1  . PHE   B 1 65  ? 13.385 19.81   -20.47  1   36.461  ? 77  PHE   A CE1  1 ? 2 
ATOM   2801 C CE2  . PHE   B 1 65  ? 14.006 18.698  -22.463 1   31.109  ? 77  PHE   A CE2  1 ? 2 
ATOM   2802 C CZ   . PHE   B 1 65  ? 13.625 18.655  -21.153 1   30.8    ? 77  PHE   A CZ   1 ? 2 
ATOM   2803 H H    . PHE   B 1 65  ? 15.222 24.366  -24.275 1   38.156  ? 77  PHE   A H    1 c 2 
ATOM   2804 H HA   . PHE   B 1 65  ? 15.284 23.364  -21.669 1   38.742  ? 77  PHE   A HA   1 c 2 
ATOM   2805 H HB2  . PHE   B 1 65  ? 13.301 23.006  -22.971 1   34.403  ? 77  PHE   A HB2  1 c 2 
ATOM   2806 H HB3  . PHE   B 1 65  ? 14.162 22.262  -24.078 1   33.215  ? 77  PHE   A HB3  1 c 2 
ATOM   2807 H HD1  . PHE   B 1 65  ? 13.369 21.843  -20.583 1   36.371  ? 77  PHE   A HD1  1 c 2 
ATOM   2808 H HD2  . PHE   B 1 65  ? 14.379 19.993  -23.981 1   29.064  ? 77  PHE   A HD2  1 c 2 
ATOM   2809 H HE1  . PHE   B 1 65  ? 13.142 19.765  -19.558 1   35.7    ? 77  PHE   A HE1  1 c 2 
ATOM   2810 H HE2  . PHE   B 1 65  ? 14.151 17.905  -22.954 1   28.987  ? 77  PHE   A HE2  1 c 2 
ATOM   2811 H HZ   . PHE   B 1 65  ? 13.526 17.822  -20.719 1   31.725  ? 77  PHE   A HZ   1 c 2 
ATOM   2812 N N    . VAL   B 1 66  ? 17.206 21.867  -21.953 1   41.494  ? 78  VAL   A N    1 ? 2 
ATOM   2813 C CA   . VAL   B 1 66  ? 18.481 21.173  -22.125 1   41.381  ? 78  VAL   A CA   1 ? 2 
ATOM   2814 C C    . VAL   B 1 66  ? 18.303 19.753  -21.615 1   37.661  ? 78  VAL   A C    1 ? 2 
ATOM   2815 O O    . VAL   B 1 66  ? 17.698 19.543  -20.556 1   37.694  ? 78  VAL   A O    1 ? 2 
ATOM   2816 C CB   . VAL   B 1 66  ? 19.573 21.908  -21.34  1   41.676  ? 78  VAL   A CB   1 ? 2 
ATOM   2817 C CG1  . VAL   B 1 66  ? 20.888 21.126  -21.438 1   43.864  ? 78  VAL   A CG1  1 ? 2 
ATOM   2818 C CG2  . VAL   B 1 66  ? 19.738 23.348  -21.811 1   46.878  ? 78  VAL   A CG2  1 ? 2 
ATOM   2819 H H    . VAL   B 1 66  ? 16.869 21.98   -21.111 1   41.816  ? 78  VAL   A H    1 c 2 
ATOM   2820 H HA   . VAL   B 1 66  ? 18.718 21.154  -23.069 1   39.942  ? 78  VAL   A HA   1 c 2 
ATOM   2821 H HB   . VAL   B 1 66  ? 19.295 21.924  -20.394 1   43.674  ? 78  VAL   A HB   1 c 2 
ATOM   2822 H HG11 . VAL   B 1 66  ? 20.981 20.756  -22.332 1   42.421  ? 78  VAL   A HG11 1 c 2 
ATOM   2823 H HG12 . VAL   B 1 66  ? 20.887 20.404  -20.787 1   43.423  ? 78  VAL   A HG12 1 c 2 
ATOM   2824 H HG13 . VAL   B 1 66  ? 21.636 21.721  -21.256 1   45.51   ? 78  VAL   A HG13 1 c 2 
ATOM   2825 H HG21 . VAL   B 1 66  ? 20.536 23.733  -21.411 1   47.798  ? 78  VAL   A HG21 1 c 2 
ATOM   2826 H HG22 . VAL   B 1 66  ? 18.961 23.868  -21.546 1   45.756  ? 78  VAL   A HG22 1 c 2 
ATOM   2827 H HG23 . VAL   B 1 66  ? 19.822 23.364  -22.779 1   45.087  ? 78  VAL   A HG23 1 c 2 
ATOM   2828 N N    . PHE   B 1 67  ? 18.845 18.777  -22.356 1   37.244  ? 79  PHE   A N    1 ? 2 
ATOM   2829 C CA   . PHE   B 1 67  ? 18.782 17.385  -21.875 1   35.368  ? 79  PHE   A CA   1 ? 2 
ATOM   2830 C C    . PHE   B 1 67  ? 19.913 16.593  -22.529 1   35.252  ? 79  PHE   A C    1 ? 2 
ATOM   2831 O O    . PHE   B 1 67  ? 20.464 17.019  -23.56  1   31.336  ? 79  PHE   A O    1 ? 2 
ATOM   2832 C CB   . PHE   B 1 67  ? 17.451 16.669  -22.098 1   34.613  ? 79  PHE   A CB   1 ? 2 
ATOM   2833 C CG   . PHE   B 1 67  ? 17.074 16.267  -23.518 1   33.091  ? 79  PHE   A CG   1 ? 2 
ATOM   2834 C CD1  . PHE   B 1 67  ? 16.675 17.221  -24.449 1   36.784  ? 79  PHE   A CD1  1 ? 2 
ATOM   2835 C CD2  . PHE   B 1 67  ? 17.216 14.952  -23.953 1   30.43   ? 79  PHE   A CD2  1 ? 2 
ATOM   2836 C CE1  . PHE   B 1 67  ? 16.455 16.896  -25.768 1   35.847  ? 79  PHE   A CE1  1 ? 2 
ATOM   2837 C CE2  . PHE   B 1 67  ? 16.9   14.616  -25.253 1   31.622  ? 79  PHE   A CE2  1 ? 2 
ATOM   2838 C CZ   . PHE   B 1 67  ? 16.595 15.571  -26.179 1   30.859  ? 79  PHE   A CZ   1 ? 2 
ATOM   2839 H H    . PHE   B 1 67  ? 19.25  18.964  -23.154 1   36.908  ? 79  PHE   A H    1 c 2 
ATOM   2840 H HA   . PHE   B 1 67  ? 18.953 17.399  -20.896 1   36.963  ? 79  PHE   A HA   1 c 2 
ATOM   2841 H HB2  . PHE   B 1 67  ? 17.451 15.859  -21.542 1   34.505  ? 79  PHE   A HB2  1 c 2 
ATOM   2842 H HB3  . PHE   B 1 67  ? 16.738 17.247  -21.746 1   34.155  ? 79  PHE   A HB3  1 c 2 
ATOM   2843 H HD1  . PHE   B 1 67  ? 16.64  18.127  -24.187 1   36.34   ? 79  PHE   A HD1  1 c 2 
ATOM   2844 H HD2  . PHE   B 1 67  ? 17.473 14.28   -23.342 1   32.095  ? 79  PHE   A HD2  1 c 2 
ATOM   2845 H HE1  . PHE   B 1 67  ? 16.176 17.558  -26.38  1   34.569  ? 79  PHE   A HE1  1 c 2 
ATOM   2846 H HE2  . PHE   B 1 67  ? 17.006 13.72   -25.533 1   30.898  ? 79  PHE   A HE2  1 c 2 
ATOM   2847 H HZ   . PHE   B 1 67  ? 16.362 15.321  -27.059 1   31.337  ? 79  PHE   A HZ   1 c 2 
ATOM   2848 N N    . SER   B 1 68  ? 20.219 15.439  -21.906 1   35.227  ? 80  SER   A N    1 ? 2 
ATOM   2849 C CA   . SER   B 1 68  ? 21.248 14.537  -22.421 1   37.974  ? 80  SER   A CA   1 ? 2 
ATOM   2850 C C    . SER   B 1 68  ? 20.583 13.433  -23.231 1   33.899  ? 80  SER   A C    1 ? 2 
ATOM   2851 O O    . SER   B 1 68  ? 19.753 12.706  -22.715 1   35.25   ? 80  SER   A O    1 ? 2 
ATOM   2852 C CB   . SER   B 1 68  ? 22.08  13.909  -21.336 1   39.344  ? 80  SER   A CB   1 ? 2 
ATOM   2853 O OG   . SER   B 1 68  ? 22.738 14.954  -20.655 1   46.332  ? 80  SER   A OG   1 ? 2 
ATOM   2854 H H    . SER   B 1 68  ? 19.774 15.21   -21.142 1   35.857  ? 80  SER   A H    1 c 2 
ATOM   2855 H HA   . SER   B 1 68  ? 21.846 15.052  -23.017 1   37.524  ? 80  SER   A HA   1 c 2 
ATOM   2856 H HB2  . SER   B 1 68  ? 21.508 13.415  -20.719 1   40.426  ? 80  SER   A HB2  1 c 2 
ATOM   2857 H HB3  . SER   B 1 68  ? 22.735 13.3    -21.727 1   41.449  ? 80  SER   A HB3  1 c 2 
ATOM   2858 H HG   . SER   B 1 68  ? 23.177 14.57   -20.018 0   30      ? 80  SER   A HG   1 c 2 
ATOM   2859 N N    . LEU   B 1 69  ? 20.981 13.309  -24.492 1   35.895  ? 81  LEU   A N    1 ? 2 
ATOM   2860 C CA   . LEU   B 1 69  ? 20.281 12.448  -25.434 1   32.504  ? 81  LEU   A CA   1 ? 2 
ATOM   2861 C C    . LEU   B 1 69  ? 20.515 10.974  -25.076 1   30.067  ? 81  LEU   A C    1 ? 2 
ATOM   2862 O O    . LEU   B 1 69  ? 21.633 10.526  -24.756 1   33.98   ? 81  LEU   A O    1 ? 2 
ATOM   2863 C CB   . LEU   B 1 69  ? 20.761 12.667  -26.866 1   35.786  ? 81  LEU   A CB   1 ? 2 
ATOM   2864 C CG   . LEU   B 1 69  ? 19.976 11.893  -27.947 1   35.384  ? 81  LEU   A CG   1 ? 2 
ATOM   2865 C CD1  . LEU   B 1 69  ? 18.672 12.622  -28.26  1   34.694  ? 81  LEU   A CD1  1 ? 2 
ATOM   2866 C CD2  . LEU   B 1 69  ? 20.863 11.7    -29.218 1   42.898  ? 81  LEU   A CD2  1 ? 2 
ATOM   2867 H H    . LEU   B 1 69  ? 21.716 13.77   -24.78  1   35.961  ? 81  LEU   A H    1 c 2 
ATOM   2868 H HA   . LEU   B 1 69  ? 19.312 12.647  -25.38  1   31.291  ? 81  LEU   A HA   1 c 2 
ATOM   2869 H HB2  . LEU   B 1 69  ? 20.704 13.63   -27.067 1   35.061  ? 81  LEU   A HB2  1 c 2 
ATOM   2870 H HB3  . LEU   B 1 69  ? 21.708 12.402  -26.918 1   36.779  ? 81  LEU   A HB3  1 c 2 
ATOM   2871 H HG   . LEU   B 1 69  ? 19.75  10.997  -27.59  1   36.332  ? 81  LEU   A HG   1 c 2 
ATOM   2872 H HD11 . LEU   B 1 69  ? 18.134 12.688  -27.453 1   33.671  ? 81  LEU   A HD11 1 c 2 
ATOM   2873 H HD12 . LEU   B 1 69  ? 18.179 12.129  -28.938 1   33.737  ? 81  LEU   A HD12 1 c 2 
ATOM   2874 H HD13 . LEU   B 1 69  ? 18.87  13.515  -28.59  1   34.524  ? 81  LEU   A HD13 1 c 2 
ATOM   2875 H HD21 . LEU   B 1 69  ? 21.527 11.012  -29.049 1   42.156  ? 81  LEU   A HD21 1 c 2 
ATOM   2876 H HD22 . LEU   B 1 69  ? 21.311 12.535  -29.431 1   41.48   ? 81  LEU   A HD22 1 c 2 
ATOM   2877 H HD23 . LEU   B 1 69  ? 20.304 11.433  -29.967 1   40.185  ? 81  LEU   A HD23 1 c 2 
ATOM   2878 N N    . GLY   B 1 70  ? 19.425 10.239  -25.038 1   31.056  ? 82  GLY   A N    1 ? 2 
ATOM   2879 C CA   . GLY   B 1 70  ? 19.485 8.798   -24.967 1   35.225  ? 82  GLY   A CA   1 ? 2 
ATOM   2880 C C    . GLY   B 1 70  ? 19.566 8.266   -23.552 1   45.527  ? 82  GLY   A C    1 ? 2 
ATOM   2881 O O    . GLY   B 1 70  ? 19.795 7.058   -23.417 1   54.689  ? 82  GLY   A O    1 ? 2 
ATOM   2882 H H    . GLY   B 1 70  ? 18.607 10.645  -25.051 1   29.843  ? 82  GLY   A H    1 c 2 
ATOM   2883 H HA2  . GLY   B 1 70  ? 18.684 8.427   -25.405 1   34.933  ? 82  GLY   A HA2  1 c 2 
ATOM   2884 H HA3  . GLY   B 1 70  ? 20.27  8.486   -25.474 1   37.124  ? 82  GLY   A HA3  1 c 2 
ATOM   2885 N N    . LYS   B 1 71  ? 19.482 9.15    -22.543 1   40.63   ? 83  LYS   A N    1 ? 2 
ATOM   2886 C CA   . LYS   B 1 71  ? 19.425 8.731   -21.153 1   46.233  ? 83  LYS   A CA   1 ? 2 
ATOM   2887 C C    . LYS   B 1 71  ? 17.967 8.502   -20.673 1   45.732  ? 83  LYS   A C    1 ? 2 
ATOM   2888 O O    . LYS   B 1 71  ? 17.699 8.121   -19.556 1   43.652  ? 83  LYS   A O    1 ? 2 
ATOM   2889 C CB   . LYS   B 1 71  ? 20.266 9.691   -20.312 1   41.769  ? 83  LYS   A CB   1 ? 2 
ATOM   2890 H H    . LYS   B 1 71  ? 19.45  10.044  -22.731 1   41.644  ? 83  LYS   A H    1 c 2 
ATOM   2891 H HA   . LYS   B 1 71  ? 19.885 7.856   -21.092 1   45.816  ? 83  LYS   A HA   1 c 2 
ATOM   2892 H HB2  . LYS   B 1 71  ? 21.296 9.461   -20.555 0   30      ? 83  LYS   A HB2  1 c 2 
ATOM   2893 H HB3  . LYS   B 1 71  ? 19.786 10.289  -19.858 0   30      ? 83  LYS   A HB3  1 c 2 
ATOM   2894 N N    . GLY   B 1 72  ? 16.94  8.494   -21.506 1   54.015  ? 84  GLY   A N    1 ? 2 
ATOM   2895 C CA   . GLY   B 1 72  ? 15.605 8.381   -20.912 1   50.579  ? 84  GLY   A CA   1 ? 2 
ATOM   2896 C C    . GLY   B 1 72  ? 15.282 9.48    -19.866 1   52.512  ? 84  GLY   A C    1 ? 2 
ATOM   2897 O O    . GLY   B 1 72  ? 14.356 9.284   -19.094 1   50.538  ? 84  GLY   A O    1 ? 2 
ATOM   2898 H H    . GLY   B 1 72  ? 17.042 8.554   -22.412 1   49.661  ? 84  GLY   A H    1 c 2 
ATOM   2899 H HA2  . GLY   B 1 72  ? 14.937 8.423   -21.635 1   50.103  ? 84  GLY   A HA2  1 c 2 
ATOM   2900 H HA3  . GLY   B 1 72  ? 15.522 7.495   -20.485 1   52.585  ? 84  GLY   A HA3  1 c 2 
ATOM   2901 N N    . GLN   B 1 73  ? 15.909 10.683  -19.985 1   44.11   ? 85  GLN   A N    1 ? 2 
ATOM   2902 C CA   . GLN   B 1 73  ? 15.576 11.878  -19.23  1   36.633  ? 85  GLN   A CA   1 ? 2 
ATOM   2903 C C    . GLN   B 1 73  ? 14.318 12.519  -19.86  1   34.277  ? 85  GLN   A C    1 ? 2 
ATOM   2904 O O    . GLN   B 1 73  ? 13.741 13.45   -19.321 1   32.349  ? 85  GLN   A O    1 ? 2 
ATOM   2905 C CB   . GLN   B 1 73  ? 16.691 12.913  -19.355 1   36.62   ? 85  GLN   A CB   1 ? 2 
ATOM   2906 C CG   . GLN   B 1 73  ? 18.017 12.589  -18.665 1   39.629  ? 85  GLN   A CG   1 ? 2 
ATOM   2907 C CD   . GLN   B 1 73  ? 19.047 13.678  -18.864 1   40.438  ? 85  GLN   A CD   1 ? 2 
ATOM   2908 O OE1  . GLN   B 1 73  ? 18.908 14.714  -19.546 1   42.864  ? 85  GLN   A OE1  1 ? 2 
ATOM   2909 N NE2  . GLN   B 1 73  ? 20.225 13.377  -18.352 1   52.435  ? 85  GLN   A NE2  1 ? 2 
ATOM   2910 H H    . GLN   B 1 73  ? 16.585 10.748  -20.596 1   43.711  ? 85  GLN   A H    1 c 2 
ATOM   2911 H HA   . GLN   B 1 73  ? 15.402 11.638  -18.285 1   39.026  ? 85  GLN   A HA   1 c 2 
ATOM   2912 H HB2  . GLN   B 1 73  ? 16.866 13.054  -20.309 1   35.95   ? 85  GLN   A HB2  1 c 2 
ATOM   2913 H HB3  . GLN   B 1 73  ? 16.358 13.762  -18.995 1   37.014  ? 85  GLN   A HB3  1 c 2 
ATOM   2914 H HG2  . GLN   B 1 73  ? 17.862 12.468  -17.704 1   40.753  ? 85  GLN   A HG2  1 c 2 
ATOM   2915 H HG3  . GLN   B 1 73  ? 18.37  11.746  -19.021 1   39.648  ? 85  GLN   A HG3  1 c 2 
ATOM   2916 H HE21 . GLN   B 1 73  ? 20.887 13.966  -18.39  1   50.028  ? 85  GLN   A HE21 1 c 2 
ATOM   2917 H HE22 . GLN   B 1 73  ? 20.357 12.586  -17.971 1   49.888  ? 85  GLN   A HE22 1 c 2 
ATOM   2918 N N    . VAL   B 1 74  ? 13.922 12.054  -21.04  1   29.897  ? 86  VAL   A N    1 ? 2 
ATOM   2919 C CA   . VAL   B 1 74  ? 12.723 12.521  -21.719 1   27.2    ? 86  VAL   A CA   1 ? 2 
ATOM   2920 C C    . VAL   B 1 74  ? 12.029 11.269  -22.189 1   26.792  ? 86  VAL   A C    1 ? 2 
ATOM   2921 O O    . VAL   B 1 74  ? 12.607 10.165  -22.09  1   30.044  ? 86  VAL   A O    1 ? 2 
ATOM   2922 C CB   . VAL   B 1 74  ? 13.072 13.453  -22.894 1   28.678  ? 86  VAL   A CB   1 ? 2 
ATOM   2923 C CG1  . VAL   B 1 74  ? 13.6   14.797  -22.38  1   30.065  ? 86  VAL   A CG1  1 ? 2 
ATOM   2924 C CG2  . VAL   B 1 74  ? 14.058 12.766  -23.859 1   25.714  ? 86  VAL   A CG2  1 ? 2 
ATOM   2925 H H    . VAL   B 1 74  ? 14.431 11.42   -21.456 1   30.515  ? 86  VAL   A H    1 c 2 
ATOM   2926 H HA   . VAL   B 1 74  ? 12.15  12.992  -21.084 1   28.155  ? 86  VAL   A HA   1 c 2 
ATOM   2927 H HB   . VAL   B 1 74  ? 12.237 13.626  -23.388 1   26.836  ? 86  VAL   A HB   1 c 2 
ATOM   2928 H HG11 . VAL   B 1 74  ? 14.414 14.653  -21.87  1   30.987  ? 86  VAL   A HG11 1 c 2 
ATOM   2929 H HG12 . VAL   B 1 74  ? 12.93  15.212  -21.81  1   30.125  ? 86  VAL   A HG12 1 c 2 
ATOM   2930 H HG13 . VAL   B 1 74  ? 13.79  15.382  -23.133 1   29.647  ? 86  VAL   A HG13 1 c 2 
ATOM   2931 H HG21 . VAL   B 1 74  ? 14.23  13.351  -24.616 1   26.231  ? 86  VAL   A HG21 1 c 2 
ATOM   2932 H HG22 . VAL   B 1 74  ? 13.677 11.931  -24.178 1   26.136  ? 86  VAL   A HG22 1 c 2 
ATOM   2933 H HG23 . VAL   B 1 74  ? 14.894 12.585  -23.398 1   27.57   ? 86  VAL   A HG23 1 c 2 
ATOM   2934 N N    . ILE   B 1 75  ? 10.818 11.44   -22.715 1   23.223  ? 87  ILE   A N    1 ? 2 
ATOM   2935 C CA   . ILE   B 1 75  ? 10.1   10.311  -23.282 1   23.41   ? 87  ILE   A CA   1 ? 2 
ATOM   2936 C C    . ILE   B 1 75  ? 10.891 9.688   -24.449 1   21.776  ? 87  ILE   A C    1 ? 2 
ATOM   2937 O O    . ILE   B 1 75  ? 11.661 10.372  -25.112 1   24.809  ? 87  ILE   A O    1 ? 2 
ATOM   2938 C CB   . ILE   B 1 75  ? 8.656  10.729  -23.692 1   23.46   ? 87  ILE   A CB   1 ? 2 
ATOM   2939 C CG1  . ILE   B 1 75  ? 8.664  11.927  -24.622 1   25.73   ? 87  ILE   A CG1  1 ? 2 
ATOM   2940 C CG2  . ILE   B 1 75  ? 7.766  10.947  -22.472 1   26.359  ? 87  ILE   A CG2  1 ? 2 
ATOM   2941 C CD1  . ILE   B 1 75  ? 7.246  12.225  -25.159 1   28.157  ? 87  ILE   A CD1  1 ? 2 
ATOM   2942 H H    . ILE   B 1 75  ? 10.427 12.266  -22.703 1   23.742  ? 87  ILE   A H    1 c 2 
ATOM   2943 H HA   . ILE   B 1 75  ? 10.022 9.633   -22.583 1   24.029  ? 87  ILE   A HA   1 c 2 
ATOM   2944 H HB   . ILE   B 1 75  ? 8.277  9.982   -24.195 1   24.132  ? 87  ILE   A HB   1 c 2 
ATOM   2945 H HG12 . ILE   B 1 75  ? 8.994  12.712  -24.14  1   25.761  ? 87  ILE   A HG12 1 c 2 
ATOM   2946 H HG13 . ILE   B 1 75  ? 9.264  11.751  -25.375 1   25.273  ? 87  ILE   A HG13 1 c 2 
ATOM   2947 H HG21 . ILE   B 1 75  ? 6.832  10.912  -22.739 1   25.529  ? 87  ILE   A HG21 1 c 2 
ATOM   2948 H HG22 . ILE   B 1 75  ? 7.957  11.816  -22.081 1   25.887  ? 87  ILE   A HG22 1 c 2 
ATOM   2949 H HG23 . ILE   B 1 75  ? 7.938  10.253  -21.814 1   26.491  ? 87  ILE   A HG23 1 c 2 
ATOM   2950 H HD11 . ILE   B 1 75  ? 6.819  11.393  -25.438 1   27.256  ? 87  ILE   A HD11 1 c 2 
ATOM   2951 H HD12 . ILE   B 1 75  ? 7.309  12.828  -25.924 1   27.016  ? 87  ILE   A HD12 1 c 2 
ATOM   2952 H HD13 . ILE   B 1 75  ? 6.71   12.645  -24.46  1   27.668  ? 87  ILE   A HD13 1 c 2 
ATOM   2953 N N    . LYS   B 1 76  ? 10.628 8.404   -24.76  1   26.805  ? 88  LYS   A N    1 ? 2 
ATOM   2954 C CA   . LYS   B 1 76  ? 11.368 7.619   -25.759 1   26.481  ? 88  LYS   A CA   1 ? 2 
ATOM   2955 C C    . LYS   B 1 76  ? 11.259 8.327   -27.11  1   25.975  ? 88  LYS   A C    1 ? 2 
ATOM   2956 O O    . LYS   B 1 76  ? 12.292 8.451   -27.808 1   27.952  ? 88  LYS   A O    1 ? 2 
ATOM   2957 C CB   . LYS   B 1 76  ? 10.934 6.115   -25.725 1   28.531  ? 88  LYS   A CB   1 ? 2 
ATOM   2958 H H    . LYS   B 1 76  ? 9.94   7.994   -24.32  1   25.674  ? 88  LYS   A H    1 c 2 
ATOM   2959 H HA   . LYS   B 1 76  ? 12.323 7.637   -25.495 1   27.509  ? 88  LYS   A HA   1 c 2 
ATOM   2960 H HB2  . LYS   B 1 76  ? 11.73  5.54    -25.692 0   30      ? 88  LYS   A HB2  1 c 2 
ATOM   2961 H HB3  . LYS   B 1 76  ? 9.946  6.059   -25.711 0   30      ? 88  LYS   A HB3  1 c 2 
ATOM   2962 N N    . ALA   B 1 77  ? 10.102 8.956   -27.413 1   26.007  ? 89  ALA   A N    1 ? 2 
ATOM   2963 C CA   . ALA   B 1 77  ? 9.909  9.67    -28.69  1   23.708  ? 89  ALA   A CA   1 ? 2 
ATOM   2964 C C    . ALA   B 1 77  ? 10.924 10.782  -28.912 1   25.508  ? 89  ALA   A C    1 ? 2 
ATOM   2965 O O    . ALA   B 1 77  ? 11.358 11.02   -30.024 1   25.1    ? 89  ALA   A O    1 ? 2 
ATOM   2966 C CB   . ALA   B 1 77  ? 8.518  10.233  -28.856 1   23.243  ? 89  ALA   A CB   1 ? 2 
ATOM   2967 H H    . ALA   B 1 77  ? 9.411  8.933   -26.816 1   25.259  ? 89  ALA   A H    1 c 2 
ATOM   2968 H HA   . ALA   B 1 77  ? 10.051 9.002   -29.416 1   24.814  ? 89  ALA   A HA   1 c 2 
ATOM   2969 H HB1  . ALA   B 1 77  ? 7.881  9.505   -28.947 1   23.484  ? 89  ALA   A HB1  1 c 2 
ATOM   2970 H HB2  . ALA   B 1 77  ? 8.287  10.766  -28.078 1   23.061  ? 89  ALA   A HB2  1 c 2 
ATOM   2971 H HB3  . ALA   B 1 77  ? 8.483  10.791  -29.651 1   23.218  ? 89  ALA   A HB3  1 c 2 
ATOM   2972 N N    . TRP   B 1 78  ? 11.36  11.466  -27.819 1   25.68   ? 90  TRP   A N    1 ? 2 
ATOM   2973 C CA   . TRP   B 1 78  ? 12.307 12.522  -27.978 1   25.894  ? 90  TRP   A CA   1 ? 2 
ATOM   2974 C C    . TRP   B 1 78  ? 13.697 11.99   -28.184 1   25.862  ? 90  TRP   A C    1 ? 2 
ATOM   2975 O O    . TRP   B 1 78  ? 14.416 12.575  -29.026 1   26.01   ? 90  TRP   A O    1 ? 2 
ATOM   2976 C CB   . TRP   B 1 78  ? 12.276 13.487  -26.781 1   27.391  ? 90  TRP   A CB   1 ? 2 
ATOM   2977 C CG   . TRP   B 1 78  ? 11.293 14.601  -26.882 1   27.336  ? 90  TRP   A CG   1 ? 2 
ATOM   2978 C CD1  . TRP   B 1 78  ? 9.956  14.591  -27.19  1   27.309  ? 90  TRP   A CD1  1 ? 2 
ATOM   2979 C CD2  . TRP   B 1 78  ? 11.661 15.983  -26.697 1   26.184  ? 90  TRP   A CD2  1 ? 2 
ATOM   2980 N NE1  . TRP   B 1 78  ? 9.474  15.876  -27.231 1   26.991  ? 90  TRP   A NE1  1 ? 2 
ATOM   2981 C CE2  . TRP   B 1 78  ? 10.49  16.749  -26.915 1   25.785  ? 90  TRP   A CE2  1 ? 2 
ATOM   2982 C CE3  . TRP   B 1 78  ? 12.843 16.622  -26.368 1   24.939  ? 90  TRP   A CE3  1 ? 2 
ATOM   2983 C CZ2  . TRP   B 1 78  ? 10.484 18.115  -26.736 1   26.566  ? 90  TRP   A CZ2  1 ? 2 
ATOM   2984 C CZ3  . TRP   B 1 78  ? 12.846 18      -26.287 1   26.043  ? 90  TRP   A CZ3  1 ? 2 
ATOM   2985 C CH2  . TRP   B 1 78  ? 11.679 18.721  -26.466 1   29.458  ? 90  TRP   A CH2  1 ? 2 
ATOM   2986 H H    . TRP   B 1 78  ? 11.05  11.257  -26.985 1   25.638  ? 90  TRP   A H    1 c 2 
ATOM   2987 H HA   . TRP   B 1 78  ? 12.053 13.041  -28.788 1   25.847  ? 90  TRP   A HA   1 c 2 
ATOM   2988 H HB2  . TRP   B 1 78  ? 12.082 12.97   -25.971 1   27.182  ? 90  TRP   A HB2  1 c 2 
ATOM   2989 H HB3  . TRP   B 1 78  ? 13.173 13.868  -26.67  1   27.644  ? 90  TRP   A HB3  1 c 2 
ATOM   2990 H HD1  . TRP   B 1 78  ? 9.447  13.824  -27.397 1   26.686  ? 90  TRP   A HD1  1 c 2 
ATOM   2991 H HE1  . TRP   B 1 78  ? 8.648  16.098  -27.373 1   26.574  ? 90  TRP   A HE1  1 c 2 
ATOM   2992 H HE3  . TRP   B 1 78  ? 13.636 16.129  -26.241 1   25.831  ? 90  TRP   A HE3  1 c 2 
ATOM   2993 H HZ2  . TRP   B 1 78  ? 9.71   18.622  -26.913 1   27.264  ? 90  TRP   A HZ2  1 c 2 
ATOM   2994 H HZ3  . TRP   B 1 78  ? 13.636 18.449  -26.04  1   27.692  ? 90  TRP   A HZ3  1 c 2 
ATOM   2995 H HH2  . TRP   B 1 78  ? 11.703 19.658  -26.374 1   29.019  ? 90  TRP   A HH2  1 c 2 
ATOM   2996 N N    . ASP   B 1 79  ? 14.033 10.926  -27.432 1   25.697  ? 91  ASP   A N    1 ? 2 
ATOM   2997 C CA   . ASP   B 1 79  ? 15.31  10.267  -27.654 1   28.038  ? 91  ASP   A CA   1 ? 2 
ATOM   2998 C C    . ASP   B 1 79  ? 15.45  9.842   -29.124 1   28.997  ? 91  ASP   A C    1 ? 2 
ATOM   2999 O O    . ASP   B 1 79  ? 16.488 10.087  -29.734 1   28.443  ? 91  ASP   A O    1 ? 2 
ATOM   3000 C CB   . ASP   B 1 79  ? 15.658 9.196   -26.657 1   29.302  ? 91  ASP   A CB   1 ? 2 
ATOM   3001 C CG   . ASP   B 1 79  ? 16.124 9.631   -25.263 1   29.299  ? 91  ASP   A CG   1 ? 2 
ATOM   3002 O OD1  . ASP   B 1 79  ? 16.659 10.726  -25.182 1   28.947  ? 91  ASP   A OD1  1 ? 2 
ATOM   3003 O OD2  . ASP   B 1 79  ? 15.992 8.799   -24.288 1   31.143  ? 91  ASP   A OD2  1 ? 2 
ATOM   3004 H H    . ASP   B 1 79  ? 13.473 10.618  -26.779 1   25.925  ? 91  ASP   A H    1 c 2 
ATOM   3005 H HA   . ASP   B 1 79  ? 16.004 10.948  -27.502 1   28.431  ? 91  ASP   A HA   1 c 2 
ATOM   3006 H HB2  . ASP   B 1 79  ? 14.87  8.626   -26.539 1   28.704  ? 91  ASP   A HB2  1 c 2 
ATOM   3007 H HB3  . ASP   B 1 79  ? 16.367 8.64    -27.042 1   30.044  ? 91  ASP   A HB3  1 c 2 
ATOM   3008 N N    . ILE   B 1 80  ? 14.366 9.34    -29.7   1   25.888  ? 92  ILE   A N    1 ? 2 
ATOM   3009 C CA   . ILE   B 1 80  ? 14.35  8.844   -31.076 1   28.701  ? 92  ILE   A CA   1 ? 2 
ATOM   3010 C C    . ILE   B 1 80  ? 14.366 10.017  -32.066 1   26.387  ? 92  ILE   A C    1 ? 2 
ATOM   3011 O O    . ILE   B 1 80  ? 15.173 10.048  -33.001 1   29.28   ? 92  ILE   A O    1 ? 2 
ATOM   3012 C CB   . ILE   B 1 80  ? 13.137 7.906   -31.349 1   28.997  ? 92  ILE   A CB   1 ? 2 
ATOM   3013 C CG1  . ILE   B 1 80  ? 13.239 6.602   -30.565 1   34.631  ? 92  ILE   A CG1  1 ? 2 
ATOM   3014 C CG2  . ILE   B 1 80  ? 12.938 7.597   -32.864 1   32.745  ? 92  ILE   A CG2  1 ? 2 
ATOM   3015 C CD1  . ILE   B 1 80  ? 11.898 5.907   -30.431 1   31.948  ? 92  ILE   A CD1  1 ? 2 
ATOM   3016 H H    . ILE   B 1 80  ? 13.592 9.291   -29.215 1   26.336  ? 92  ILE   A H    1 c 2 
ATOM   3017 H HA   . ILE   B 1 80  ? 15.165 8.323   -31.214 1   28.993  ? 92  ILE   A HA   1 c 2 
ATOM   3018 H HB   . ILE   B 1 80  ? 12.336 8.372   -31.037 1   29.33   ? 92  ILE   A HB   1 c 2 
ATOM   3019 H HG12 . ILE   B 1 80  ? 13.866 6.004   -31.02  1   34.037  ? 92  ILE   A HG12 1 c 2 
ATOM   3020 H HG13 . ILE   B 1 80  ? 13.592 6.792   -29.672 1   32.734  ? 92  ILE   A HG13 1 c 2 
ATOM   3021 H HG21 . ILE   B 1 80  ? 12.353 6.829   -32.968 1   32.185  ? 92  ILE   A HG21 1 c 2 
ATOM   3022 H HG22 . ILE   B 1 80  ? 13.799 7.403   -33.272 1   32.852  ? 92  ILE   A HG22 1 c 2 
ATOM   3023 H HG23 . ILE   B 1 80  ? 12.538 8.366   -33.304 1   31.38   ? 92  ILE   A HG23 1 c 2 
ATOM   3024 H HD11 . ILE   B 1 80  ? 11.224 6.546   -30.131 1   31.627  ? 92  ILE   A HD11 1 c 2 
ATOM   3025 H HD12 . ILE   B 1 80  ? 11.972 5.185   -29.778 1   33.283  ? 92  ILE   A HD12 1 c 2 
ATOM   3026 H HD13 . ILE   B 1 80  ? 11.63  5.535   -31.293 1   33.135  ? 92  ILE   A HD13 1 c 2 
ATOM   3027 N N    . GLY   B 1 81  ? 13.531 10.998  -31.802 1   26.524  ? 93  GLY   A N    1 ? 2 
ATOM   3028 C CA   . GLY   B 1 81  ? 13.257 12.049  -32.756 1   29.124  ? 93  GLY   A CA   1 ? 2 
ATOM   3029 C C    . GLY   B 1 81  ? 14.318 13.101  -32.855 1   28.469  ? 93  GLY   A C    1 ? 2 
ATOM   3030 O O    . GLY   B 1 81  ? 14.78  13.443  -33.941 1   29.043  ? 93  GLY   A O    1 ? 2 
ATOM   3031 H H    . GLY   B 1 81  ? 13.104 11.019  -30.994 1   26.111  ? 93  GLY   A H    1 c 2 
ATOM   3032 H HA2  . GLY   B 1 81  ? 13.132 11.64   -33.643 1   28.733  ? 93  GLY   A HA2  1 c 2 
ATOM   3033 H HA3  . GLY   B 1 81  ? 12.405 12.479  -32.509 1   27.522  ? 93  GLY   A HA3  1 c 2 
ATOM   3034 N N    . VAL   B 1 82  ? 14.729 13.607  -31.687 1   29.317  ? 94  VAL   A N    1 ? 2 
ATOM   3035 C CA   . VAL   B 1 82  ? 15.815 14.571  -31.676 1   32.583  ? 94  VAL   A CA   1 ? 2 
ATOM   3036 C C    . VAL   B 1 82  ? 17.126 14.002  -32.232 1   31.355  ? 94  VAL   A C    1 ? 2 
ATOM   3037 O O    . VAL   B 1 82  ? 17.866 14.745  -32.846 1   35.305  ? 94  VAL   A O    1 ? 2 
ATOM   3038 C CB   . VAL   B 1 82  ? 15.976 15.198  -30.296 1   30.55   ? 94  VAL   A CB   1 ? 2 
ATOM   3039 C CG1  . VAL   B 1 82  ? 17.197 16.107  -30.238 1   38.387  ? 94  VAL   A CG1  1 ? 2 
ATOM   3040 C CG2  . VAL   B 1 82  ? 14.742 15.901  -29.869 1   30.522  ? 94  VAL   A CG2  1 ? 2 
ATOM   3041 H H    . VAL   B 1 82  ? 14.341 13.348  -30.901 1   28.836  ? 94  VAL   A H    1 c 2 
ATOM   3042 H HA   . VAL   B 1 82  ? 15.549 15.293  -32.278 1   31.571  ? 94  VAL   A HA   1 c 2 
ATOM   3043 H HB   . VAL   B 1 82  ? 16.13  14.46   -29.662 1   31.893  ? 94  VAL   A HB   1 c 2 
ATOM   3044 H HG11 . VAL   B 1 82  ? 17.254 16.628  -31.057 1   36.869  ? 94  VAL   A HG11 1 c 2 
ATOM   3045 H HG12 . VAL   B 1 82  ? 18     15.569  -30.139 1   36.966  ? 94  VAL   A HG12 1 c 2 
ATOM   3046 H HG13 . VAL   B 1 82  ? 17.118 16.709  -29.479 1   36.32   ? 94  VAL   A HG13 1 c 2 
ATOM   3047 H HG21 . VAL   B 1 82  ? 14.919 16.404  -29.056 1   30.542  ? 94  VAL   A HG21 1 c 2 
ATOM   3048 H HG22 . VAL   B 1 82  ? 14.039 15.252  -29.698 1   29.436  ? 94  VAL   A HG22 1 c 2 
ATOM   3049 H HG23 . VAL   B 1 82  ? 14.456 16.51   -30.57  1   30.543  ? 94  VAL   A HG23 1 c 2 
ATOM   3050 N N    . ALA   B 1 83  ? 17.41  12.713  -32.066 1   32.765  ? 95  ALA   A N    1 ? 2 
ATOM   3051 C CA   . ALA   B 1 83  ? 18.549 12.041  -32.692 1   31.422  ? 95  ALA   A CA   1 ? 2 
ATOM   3052 C C    . ALA   B 1 83  ? 18.567 12.148  -34.227 1   35.274  ? 95  ALA   A C    1 ? 2 
ATOM   3053 O O    . ALA   B 1 83  ? 19.624 12.093  -34.805 1   38.325  ? 95  ALA   A O    1 ? 2 
ATOM   3054 C CB   . ALA   B 1 83  ? 18.634 10.588  -32.265 1   31.961  ? 95  ALA   A CB   1 ? 2 
ATOM   3055 H H    . ALA   B 1 83  ? 16.866 12.218  -31.525 1   30.905  ? 95  ALA   A H    1 c 2 
ATOM   3056 H HA   . ALA   B 1 83  ? 19.371 12.5    -32.362 1   33.385  ? 95  ALA   A HA   1 c 2 
ATOM   3057 H HB1  . ALA   B 1 83  ? 18.598 10.529  -31.296 1   31.451  ? 95  ALA   A HB1  1 c 2 
ATOM   3058 H HB2  . ALA   B 1 83  ? 17.889 10.092  -32.645 1   31.341  ? 95  ALA   A HB2  1 c 2 
ATOM   3059 H HB3  . ALA   B 1 83  ? 19.469 10.202  -32.58  1   33.325  ? 95  ALA   A HB3  1 c 2 
ATOM   3060 N N    . THR   B 1 84  ? 17.423 12.311  -34.885 1   33.923  ? 96  THR   A N    1 ? 2 
ATOM   3061 C CA   . THR   B 1 84  ? 17.352 12.456  -36.353 1   35.956  ? 96  THR   A CA   1 ? 2 
ATOM   3062 C C    . THR   B 1 84  ? 17.558 13.897  -36.804 1   35.916  ? 96  THR   A C    1 ? 2 
ATOM   3063 O O    . THR   B 1 84  ? 17.723 14.096  -38.014 1   36.902  ? 96  THR   A O    1 ? 2 
ATOM   3064 C CB   . THR   B 1 84  ? 15.973 12.005  -36.865 1   35.821  ? 96  THR   A CB   1 ? 2 
ATOM   3065 O OG1  . THR   B 1 84  ? 14.971 12.982  -36.543 1   33.873  ? 96  THR   A OG1  1 ? 2 
ATOM   3066 C CG2  . THR   B 1 84  ? 15.681 10.608  -36.371 1   37.975  ? 96  THR   A CG2  1 ? 2 
ATOM   3067 H H    . THR   B 1 84  ? 16.642 12.33   -34.411 1   32.952  ? 96  THR   A H    1 c 2 
ATOM   3068 H HA   . THR   B 1 84  ? 18.042 11.889  -36.762 1   37.103  ? 96  THR   A HA   1 c 2 
ATOM   3069 H HB   . THR   B 1 84  ? 16.031 11.945  -37.849 1   37.377  ? 96  THR   A HB   1 c 2 
ATOM   3070 H HG1  . THR   B 1 84  ? 14.935 13.059  -35.689 0   30      ? 96  THR   A HG1  1 c 2 
ATOM   3071 H HG21 . THR   B 1 84  ? 15.005 10.198  -36.938 1   37.305  ? 96  THR   A HG21 1 c 2 
ATOM   3072 H HG22 . THR   B 1 84  ? 15.354 10.649  -35.458 1   35.774  ? 96  THR   A HG22 1 c 2 
ATOM   3073 H HG23 . THR   B 1 84  ? 16.493 10.075  -36.401 1   38.094  ? 96  THR   A HG23 1 c 2 
ATOM   3074 N N    . MET   B 1 85  ? 17.707 14.877  -35.895 1   35.1    ? 97  MET   A N    1 ? 2 
ATOM   3075 C CA   . MET   B 1 85  ? 17.624 16.282  -36.271 1   38.703  ? 97  MET   A CA   1 ? 2 
ATOM   3076 C C    . MET   B 1 85  ? 19.012 16.926  -36.417 1   37.176  ? 97  MET   A C    1 ? 2 
ATOM   3077 O O    . MET   B 1 85  ? 19.953 16.624  -35.67  1   39.902  ? 97  MET   A O    1 ? 2 
ATOM   3078 C CB   . MET   B 1 85  ? 16.828 17.123  -35.266 1   34.135  ? 97  MET   A CB   1 ? 2 
ATOM   3079 C CG   . MET   B 1 85  ? 15.356 16.705  -35.168 1   32.262  ? 97  MET   A CG   1 ? 2 
ATOM   3080 S SD   . MET   B 1 85  ? 14.453 17.602  -33.897 1   34.131  ? 97  MET   A SD   1 ? 2 
ATOM   3081 C CE   . MET   B 1 85  ? 14.427 19.271  -34.589 1   32.448  ? 97  MET   A CE   1 ? 2 
ATOM   3082 H H    . MET   B 1 85  ? 17.866 14.665  -35.021 1   34.957  ? 97  MET   A H    1 c 2 
ATOM   3083 H HA   . MET   B 1 85  ? 17.172 16.332  -37.151 1   37.463  ? 97  MET   A HA   1 c 2 
ATOM   3084 H HB2  . MET   B 1 85  ? 17.246 17.038  -34.383 1   34.3    ? 97  MET   A HB2  1 c 2 
ATOM   3085 H HB3  . MET   B 1 85  ? 16.877 18.065  -35.534 1   35.731  ? 97  MET   A HB3  1 c 2 
ATOM   3086 H HG2  . MET   B 1 85  ? 14.92  16.857  -36.028 1   33.575  ? 97  MET   A HG2  1 c 2 
ATOM   3087 H HG3  . MET   B 1 85  ? 15.305 15.75   -34.972 1   32.146  ? 97  MET   A HG3  1 c 2 
ATOM   3088 H HE1  . MET   B 1 85  ? 14.055 19.887  -33.932 1   33.091  ? 97  MET   A HE1  1 c 2 
ATOM   3089 H HE2  . MET   B 1 85  ? 15.335 19.546  -34.812 1   34.452  ? 97  MET   A HE2  1 c 2 
ATOM   3090 H HE3  . MET   B 1 85  ? 13.876 19.28   -35.394 1   33.76   ? 97  MET   A HE3  1 c 2 
ATOM   3091 N N    . LYS   B 1 86  ? 19.122 17.862  -37.367 1   40.948  ? 98  LYS   A N    1 ? 2 
ATOM   3092 C CA   . LYS   B 1 86  ? 20.346 18.607  -37.623 1   43.935  ? 98  LYS   A CA   1 ? 2 
ATOM   3093 C C    . LYS   B 1 86  ? 20.296 19.916  -36.846 1   43.02   ? 98  LYS   A C    1 ? 2 
ATOM   3094 O O    . LYS   B 1 86  ? 19.229 20.415  -36.525 1   43.372  ? 98  LYS   A O    1 ? 2 
ATOM   3095 C CB   . LYS   B 1 86  ? 20.46  18.843  -39.135 1   52.037  ? 98  LYS   A CB   1 ? 2 
ATOM   3096 C CG   . LYS   B 1 86  ? 20.562 17.622  -40.033 1   56.955  ? 98  LYS   A CG   1 ? 2 
ATOM   3097 C CD   . LYS   B 1 86  ? 20.843 18.039  -41.483 1   67.407  ? 98  LYS   A CD   1 ? 2 
ATOM   3098 C CE   . LYS   B 1 86  ? 21.032 16.889  -42.438 1   66.889  ? 98  LYS   A CE   1 ? 2 
ATOM   3099 N NZ   . LYS   B 1 86  ? 19.851 16.029  -42.293 1   64.511  ? 98  LYS   A NZ   1 ? 2 
ATOM   3100 H H    . LYS   B 1 86  ? 18.39  18.048  -37.882 1   40.634  ? 98  LYS   A H    1 c 2 
ATOM   3101 H HA   . LYS   B 1 86  ? 21.12  18.071  -37.311 1   44.819  ? 98  LYS   A HA   1 c 2 
ATOM   3102 H HB2  . LYS   B 1 86  ? 19.676 19.361  -39.419 1   51.376  ? 98  LYS   A HB2  1 c 2 
ATOM   3103 H HB3  . LYS   B 1 86  ? 21.25  19.401  -39.294 1   53.466  ? 98  LYS   A HB3  1 c 2 
ATOM   3104 H HG2  . LYS   B 1 86  ? 21.288 17.044  -39.711 1   57.531  ? 98  LYS   A HG2  1 c 2 
ATOM   3105 H HG3  . LYS   B 1 86  ? 19.719 17.122  -39.989 1   55.927  ? 98  LYS   A HG3  1 c 2 
ATOM   3106 H HD2  . LYS   B 1 86  ? 20.096 18.594  -41.799 1   65.236  ? 98  LYS   A HD2  1 c 2 
ATOM   3107 H HD3  . LYS   B 1 86  ? 21.647 18.599  -41.496 1   66.783  ? 98  LYS   A HD3  1 c 2 
ATOM   3108 H HE2  . LYS   B 1 86  ? 21.096 17.21   -43.355 1   69.519  ? 98  LYS   A HE2  1 c 2 
ATOM   3109 H HE3  . LYS   B 1 86  ? 21.836 16.386  -42.216 1   67.8    ? 98  LYS   A HE3  1 c 2 
ATOM   3110 H HZ1  . LYS   B 1 86  ? 19.104 16.526  -42.169 1   63.494  ? 98  LYS   A HZ1  1 c 2 
ATOM   3111 H HZ2  . LYS   B 1 86  ? 19.959 15.466  -41.591 1   62.954  ? 98  LYS   A HZ2  1 c 2 
ATOM   3112 H HZ3  . LYS   B 1 86  ? 19.748 15.535  -43.046 1   65.659  ? 98  LYS   A HZ3  1 c 2 
ATOM   3113 N N    . LYS   B 1 87  ? 21.429 20.554  -36.613 1   45.538  ? 99  LYS   A N    1 ? 2 
ATOM   3114 C CA   . LYS   B 1 87  ? 21.455 21.844  -35.929 1   45.087  ? 99  LYS   A CA   1 ? 2 
ATOM   3115 C C    . LYS   B 1 87  ? 20.72  22.881  -36.78  1   46.186  ? 99  LYS   A C    1 ? 2 
ATOM   3116 O O    . LYS   B 1 87  ? 20.957 22.98   -37.98  1   49.721  ? 99  LYS   A O    1 ? 2 
ATOM   3117 C CB   . LYS   B 1 87  ? 22.888 22.345  -35.703 1   53.374  ? 99  LYS   A CB   1 ? 2 
ATOM   3118 C CG   . LYS   B 1 87  ? 23.002 23.582  -34.777 1   58.261  ? 99  LYS   A CG   1 ? 2 
ATOM   3119 C CD   . LYS   B 1 87  ? 24.296 24.365  -34.902 1   68.148  ? 99  LYS   A CD   1 ? 2 
ATOM   3120 C CE   . LYS   B 1 87  ? 24.374 25.468  -33.899 1   70.564  ? 99  LYS   A CE   1 ? 2 
ATOM   3121 N NZ   . LYS   B 1 87  ? 25.716 26.026  -33.894 1   75.034  ? 99  LYS   A NZ   1 ? 2 
ATOM   3122 H H    . LYS   B 1 87  ? 22.218 20.182  -36.886 1   46.334  ? 99  LYS   A H    1 c 2 
ATOM   3123 H HA   . LYS   B 1 87  ? 20.995 21.749  -35.057 1   44.482  ? 99  LYS   A HA   1 c 2 
ATOM   3124 H HB2  . LYS   B 1 87  ? 23.417 21.617  -35.314 1   52.306  ? 99  LYS   A HB2  1 c 2 
ATOM   3125 H HB3  . LYS   B 1 87  ? 23.284 22.569  -36.572 1   54.66   ? 99  LYS   A HB3  1 c 2 
ATOM   3126 H HG2  . LYS   B 1 87  ? 22.252 24.184  -34.969 1   58.41   ? 99  LYS   A HG2  1 c 2 
ATOM   3127 H HG3  . LYS   B 1 87  ? 22.906 23.28   -33.848 1   57.175  ? 99  LYS   A HG3  1 c 2 
ATOM   3128 H HD2  . LYS   B 1 87  ? 25.056 23.756  -34.773 1   67.265  ? 99  LYS   A HD2  1 c 2 
ATOM   3129 H HD3  . LYS   B 1 87  ? 24.357 24.746  -35.806 1   68.554  ? 99  LYS   A HD3  1 c 2 
ATOM   3130 H HE2  . LYS   B 1 87  ? 23.734 26.168  -34.122 1   70.759  ? 99  LYS   A HE2  1 c 2 
ATOM   3131 H HE3  . LYS   B 1 87  ? 24.166 25.126  -33.012 1   68.687  ? 99  LYS   A HE3  1 c 2 
ATOM   3132 H HZ1  . LYS   B 1 87  ? 25.933 26.315  -34.724 1   76.412  ? 99  LYS   A HZ1  1 c 2 
ATOM   3133 H HZ2  . LYS   B 1 87  ? 26.311 25.394  -33.633 1   74.582  ? 99  LYS   A HZ2  1 c 2 
ATOM   3134 H HZ3  . LYS   B 1 87  ? 25.753 26.724  -33.317 1   75.652  ? 99  LYS   A HZ3  1 c 2 
ATOM   3135 N N    . GLY   B 1 88  ? 19.882 23.692  -36.128 1   45.824  ? 100 GLY   A N    1 ? 2 
ATOM   3136 C CA   . GLY   B 1 88  ? 19.016 24.661  -36.794 1   47.032  ? 100 GLY   A CA   1 ? 2 
ATOM   3137 C C    . GLY   B 1 88  ? 17.717 24.072  -37.327 1   45.766  ? 100 GLY   A C    1 ? 2 
ATOM   3138 O O    . GLY   B 1 88  ? 16.906 24.822  -37.859 1   46.664  ? 100 GLY   A O    1 ? 2 
ATOM   3139 H H    . GLY   B 1 88  ? 19.848 23.642  -35.216 1   44.608  ? 100 GLY   A H    1 c 2 
ATOM   3140 H HA2  . GLY   B 1 88  ? 18.802 25.381  -36.155 1   47.395  ? 100 GLY   A HA2  1 c 2 
ATOM   3141 H HA3  . GLY   B 1 88  ? 19.514 25.069  -37.541 1   49.449  ? 100 GLY   A HA3  1 c 2 
ATOM   3142 N N    . GLU   B 1 89  ? 17.527 22.737  -37.24  1   41.672  ? 101 GLU   A N    1 ? 2 
ATOM   3143 C CA   . GLU   B 1 89  ? 16.357 22.097  -37.834 1   42.106  ? 101 GLU   A CA   1 ? 2 
ATOM   3144 C C    . GLU   B 1 89  ? 15.114 22.402  -36.981 1   43.29   ? 101 GLU   A C    1 ? 2 
ATOM   3145 O O    . GLU   B 1 89  ? 15.225 22.466  -35.77  1   42.707  ? 101 GLU   A O    1 ? 2 
ATOM   3146 C CB   . GLU   B 1 89  ? 16.548 20.576  -37.922 1   41.137  ? 101 GLU   A CB   1 ? 2 
ATOM   3147 C CG   . GLU   B 1 89  ? 15.404 19.803  -38.575 1   38.955  ? 101 GLU   A CG   1 ? 2 
ATOM   3148 C CD   . GLU   B 1 89  ? 15.674 18.341  -38.813 1   38.794  ? 101 GLU   A CD   1 ? 2 
ATOM   3149 O OE1  . GLU   B 1 89  ? 16.789 17.979  -39.192 1   40.611  ? 101 GLU   A OE1  1 ? 2 
ATOM   3150 O OE2  . GLU   B 1 89  ? 14.788 17.533  -38.528 1   45.531  ? 101 GLU   A OE2  1 ? 2 
ATOM   3151 H H    . GLU   B 1 89  ? 18.132 22.218  -36.793 1   41.769  ? 101 GLU   A H    1 c 2 
ATOM   3152 H HA   . GLU   B 1 89  ? 16.226 22.465  -38.743 1   44.173  ? 101 GLU   A HA   1 c 2 
ATOM   3153 H HB2  . GLU   B 1 89  ? 17.369 20.396  -38.425 1   41.995  ? 101 GLU   A HB2  1 c 2 
ATOM   3154 H HB3  . GLU   B 1 89  ? 16.672 20.225  -37.016 1   39.183  ? 101 GLU   A HB3  1 c 2 
ATOM   3155 H HG2  . GLU   B 1 89  ? 14.606 19.88   -38.01  1   38.134  ? 101 GLU   A HG2  1 c 2 
ATOM   3156 H HG3  . GLU   B 1 89  ? 15.192 20.221  -39.437 1   41.085  ? 101 GLU   A HG3  1 c 2 
ATOM   3157 N N    . ILE   B 1 90  ? 13.932 22.616  -37.609 1   44.546  ? 102 ILE   A N    1 ? 2 
ATOM   3158 C CA   . ILE   B 1 90  ? 12.678 22.598  -36.853 1   42.134  ? 102 ILE   A CA   1 ? 2 
ATOM   3159 C C    . ILE   B 1 90  ? 11.845 21.47   -37.41  1   41.15   ? 102 ILE   A C    1 ? 2 
ATOM   3160 O O    . ILE   B 1 90  ? 11.69  21.363  -38.623 1   42.058  ? 102 ILE   A O    1 ? 2 
ATOM   3161 C CB   . ILE   B 1 90  ? 11.88  23.933  -36.865 1   43.384  ? 102 ILE   A CB   1 ? 2 
ATOM   3162 C CG1  . ILE   B 1 90  ? 12.741 25.126  -36.54  1   47.632  ? 102 ILE   A CG1  1 ? 2 
ATOM   3163 C CG2  . ILE   B 1 90  ? 10.679 23.888  -35.91  1   39.638  ? 102 ILE   A CG2  1 ? 2 
ATOM   3164 C CD1  . ILE   B 1 90  ? 12.038 26.477  -36.517 1   49.134  ? 102 ILE   A CD1  1 ? 2 
ATOM   3165 H H    . ILE   B 1 90  ? 13.911 22.773  -38.509 1   45.689  ? 102 ILE   A H    1 c 2 
ATOM   3166 H HA   . ILE   B 1 90  ? 12.891 22.39   -35.926 1   40.771  ? 102 ILE   A HA   1 c 2 
ATOM   3167 H HB   . ILE   B 1 90  ? 11.533 24.06   -37.771 1   44.846  ? 102 ILE   A HB   1 c 2 
ATOM   3168 H HG12 . ILE   B 1 90  ? 13.147 24.978  -35.662 1   45.709  ? 102 ILE   A HG12 1 c 2 
ATOM   3169 H HG13 . ILE   B 1 90  ? 13.467 25.17   -37.195 1   48.153  ? 102 ILE   A HG13 1 c 2 
ATOM   3170 H HG21 . ILE   B 1 90  ? 10.144 24.69   -36.016 1   41.749  ? 102 ILE   A HG21 1 c 2 
ATOM   3171 H HG22 . ILE   B 1 90  ? 10.995 23.831  -34.992 1   39.205  ? 102 ILE   A HG22 1 c 2 
ATOM   3172 H HG23 . ILE   B 1 90  ? 10.131 23.111  -36.109 1   39.157  ? 102 ILE   A HG23 1 c 2 
ATOM   3173 H HD11 . ILE   B 1 90  ? 11.556 26.609  -37.355 1   50.65   ? 102 ILE   A HD11 1 c 2 
ATOM   3174 H HD12 . ILE   B 1 90  ? 12.7   27.186  -36.41  1   50.991  ? 102 ILE   A HD12 1 c 2 
ATOM   3175 H HD13 . ILE   B 1 90  ? 11.409 26.513  -35.773 1   48.335  ? 102 ILE   A HD13 1 c 2 
ATOM   3176 N N    . ALA   B 1 91  ? 11.288 20.671  -36.51  1   34.196  ? 103 ALA   A N    1 ? 2 
ATOM   3177 C CA   . ALA   B 1 91  ? 10.496 19.491  -36.817 1   34.384  ? 103 ALA   A CA   1 ? 2 
ATOM   3178 C C    . ALA   B 1 91  ? 9.22   19.395  -35.966 1   33.016  ? 103 ALA   A C    1 ? 2 
ATOM   3179 O O    . ALA   B 1 91  ? 9.106  19.982  -34.879 1   35.179  ? 103 ALA   A O    1 ? 2 
ATOM   3180 C CB   . ALA   B 1 91  ? 11.369 18.275  -36.663 1   32.374  ? 103 ALA   A CB   1 ? 2 
ATOM   3181 H H    . ALA   B 1 91  ? 11.408 20.878  -35.628 1   34.799  ? 103 ALA   A H    1 c 2 
ATOM   3182 H HA   . ALA   B 1 91  ? 10.217 19.558  -37.77  1   35.258  ? 103 ALA   A HA   1 c 2 
ATOM   3183 H HB1  . ALA   B 1 91  ? 12.126 18.337  -37.271 1   33.733  ? 103 ALA   A HB1  1 c 2 
ATOM   3184 H HB2  . ALA   B 1 91  ? 11.695 18.22   -35.749 1   31.607  ? 103 ALA   A HB2  1 c 2 
ATOM   3185 H HB3  . ALA   B 1 91  ? 10.856 17.476  -36.87  1   32.091  ? 103 ALA   A HB3  1 c 2 
ATOM   3186 N N    . HIS   B 1 92  ? 8.205  18.781  -36.576 1   29.632  ? 104 HIS   A N    1 ? 2 
ATOM   3187 C CA   . HIS   B 1 92  ? 6.989  18.429  -35.912 1   29.485  ? 104 HIS   A CA   1 ? 2 
ATOM   3188 C C    . HIS   B 1 92  ? 6.977  16.923  -35.629 1   30.946  ? 104 HIS   A C    1 ? 2 
ATOM   3189 O O    . HIS   B 1 92  ? 7.257  16.128  -36.517 1   33.425  ? 104 HIS   A O    1 ? 2 
ATOM   3190 C CB   . HIS   B 1 92  ? 5.782  18.773  -36.781 1   30.076  ? 104 HIS   A CB   1 ? 2 
ATOM   3191 C CG   . HIS   B 1 92  ? 5.424  20.209  -36.762 1   32.846  ? 104 HIS   A CG   1 ? 2 
ATOM   3192 N ND1  . HIS   B 1 92  ? 4.419  20.715  -37.529 1   32.724  ? 104 HIS   A ND1  1 ? 2 
ATOM   3193 C CD2  . HIS   B 1 92  ? 5.941  21.223  -36.033 1   32.229  ? 104 HIS   A CD2  1 ? 2 
ATOM   3194 C CE1  . HIS   B 1 92  ? 4.365  22.039  -37.348 1   34.753  ? 104 HIS   A CE1  1 ? 2 
ATOM   3195 N NE2  . HIS   B 1 92  ? 5.251  22.352  -36.369 1   33.823  ? 104 HIS   A NE2  1 ? 2 
ATOM   3196 H H    . HIS   B 1 92  ? 8.288  18.572  -37.462 1   31.592  ? 104 HIS   A H    1 c 2 
ATOM   3197 H HA   . HIS   B 1 92  ? 6.933  18.912  -35.055 1   29.192  ? 104 HIS   A HA   1 c 2 
ATOM   3198 H HB2  . HIS   B 1 92  ? 5.973  18.505  -37.706 1   31.521  ? 104 HIS   A HB2  1 c 2 
ATOM   3199 H HB3  . HIS   B 1 92  ? 5.011  18.25   -36.472 1   30.013  ? 104 HIS   A HB3  1 c 2 
ATOM   3200 H HD1  . HIS   B 1 92  ? 3.901  20.25   -38.069 0   30      ? 104 HIS   A HD1  1 c 2 
ATOM   3201 H HD2  . HIS   B 1 92  ? 6.629  21.171  -35.399 1   31.222  ? 104 HIS   A HD2  1 c 2 
ATOM   3202 H HE1  . HIS   B 1 92  ? 3.741  22.624  -37.738 1   36.621  ? 104 HIS   A HE1  1 c 2 
ATOM   3203 H HE2  . HIS   B 1 92  ? 5.35   23.12   -35.984 0   30      ? 104 HIS   A HE2  1 c 2 
ATOM   3204 N N    . LEU   B 1 93  ? 6.647  16.545  -34.402 1   28.116  ? 105 LEU   A N    1 ? 2 
ATOM   3205 C CA   . LEU   B 1 93  ? 6.516  15.156  -33.993 1   27.486  ? 105 LEU   A CA   1 ? 2 
ATOM   3206 C C    . LEU   B 1 93  ? 5.094  14.918  -33.525 1   27.675  ? 105 LEU   A C    1 ? 2 
ATOM   3207 O O    . LEU   B 1 93  ? 4.585  15.655  -32.696 1   26.069  ? 105 LEU   A O    1 ? 2 
ATOM   3208 C CB   . LEU   B 1 93  ? 7.45   14.719  -32.855 1   26.041  ? 105 LEU   A CB   1 ? 2 
ATOM   3209 C CG   . LEU   B 1 93  ? 8.951  14.795  -33.064 1   25.412  ? 105 LEU   A CG   1 ? 2 
ATOM   3210 C CD1  . LEU   B 1 93  ? 9.771  14.238  -31.927 1   27.28   ? 105 LEU   A CD1  1 ? 2 
ATOM   3211 C CD2  . LEU   B 1 93  ? 9.374  13.981  -34.291 1   27.899  ? 105 LEU   A CD2  1 ? 2 
ATOM   3212 H H    . LEU   B 1 93  ? 6.491  17.192  -33.775 1   28.442  ? 105 LEU   A H    1 c 2 
ATOM   3213 H HA   . LEU   B 1 93  ? 6.686  14.587  -34.781 1   27.865  ? 105 LEU   A HA   1 c 2 
ATOM   3214 H HB2  . LEU   B 1 93  ? 7.228  15.259  -32.061 1   25.646  ? 105 LEU   A HB2  1 c 2 
ATOM   3215 H HB3  . LEU   B 1 93  ? 7.224  13.789  -32.622 1   25.492  ? 105 LEU   A HB3  1 c 2 
ATOM   3216 H HG   . LEU   B 1 93  ? 9.205  15.744  -33.208 1   26.881  ? 105 LEU   A HG   1 c 2 
ATOM   3217 H HD11 . LEU   B 1 93  ? 9.509  14.668  -31.096 1   26.127  ? 105 LEU   A HD11 1 c 2 
ATOM   3218 H HD12 . LEU   B 1 93  ? 10.714 14.406  -32.093 1   26.817  ? 105 LEU   A HD12 1 c 2 
ATOM   3219 H HD13 . LEU   B 1 93  ? 9.621  13.28   -31.856 1   26.19   ? 105 LEU   A HD13 1 c 2 
ATOM   3220 H HD21 . LEU   B 1 93  ? 9.007  14.387  -35.094 1   28.223  ? 105 LEU   A HD21 1 c 2 
ATOM   3221 H HD22 . LEU   B 1 93  ? 9.04   13.072  -34.208 1   27.099  ? 105 LEU   A HD22 1 c 2 
ATOM   3222 H HD23 . LEU   B 1 93  ? 10.344 13.964  -34.353 1   27.629  ? 105 LEU   A HD23 1 c 2 
ATOM   3223 N N    . LEU   B 1 94  ? 4.563  13.774  -33.944 1   27.346  ? 106 LEU   A N    1 ? 2 
ATOM   3224 C CA   . LEU   B 1 94  ? 3.32   13.242  -33.446 1   25.053  ? 106 LEU   A CA   1 ? 2 
ATOM   3225 C C    . LEU   B 1 94  ? 3.594  11.851  -32.872 1   26.673  ? 106 LEU   A C    1 ? 2 
ATOM   3226 O O    . LEU   B 1 94  ? 4.139  10.982  -33.539 1   24.896  ? 106 LEU   A O    1 ? 2 
ATOM   3227 C CB   . LEU   B 1 94  ? 2.207  13.236  -34.5   1   26.314  ? 106 LEU   A CB   1 ? 2 
ATOM   3228 C CG   . LEU   B 1 94  ? 0.834  12.74   -34.011 1   30.999  ? 106 LEU   A CG   1 ? 2 
ATOM   3229 C CD1  . LEU   B 1 94  ? 0.178  13.782  -33.092 1   31.807  ? 106 LEU   A CD1  1 ? 2 
ATOM   3230 C CD2  . LEU   B 1 94  ? -0.119 12.476  -35.186 1   33.44   ? 106 LEU   A CD2  1 ? 2 
ATOM   3231 H H    . LEU   B 1 94  ? 5.006  13.296  -34.585 1   27.177  ? 106 LEU   A H    1 c 2 
ATOM   3232 H HA   . LEU   B 1 94  ? 3.029  13.819  -32.696 1   25.647  ? 106 LEU   A HA   1 c 2 
ATOM   3233 H HB2  . LEU   B 1 94  ? 2.103  14.153  -34.843 1   27.947  ? 106 LEU   A HB2  1 c 2 
ATOM   3234 H HB3  . LEU   B 1 94  ? 2.496  12.665  -35.249 1   27.703  ? 106 LEU   A HB3  1 c 2 
ATOM   3235 H HG   . LEU   B 1 94  ? 0.958  11.897  -33.504 1   29.732  ? 106 LEU   A HG   1 c 2 
ATOM   3236 H HD11 . LEU   B 1 94  ? 0.706  13.881  -32.283 1   30.517  ? 106 LEU   A HD11 1 c 2 
ATOM   3237 H HD12 . LEU   B 1 94  ? -0.719 13.49   -32.858 1   32.237  ? 106 LEU   A HD12 1 c 2 
ATOM   3238 H HD13 . LEU   B 1 94  ? 0.128  14.637  -33.552 1   32.333  ? 106 LEU   A HD13 1 c 2 
ATOM   3239 H HD21 . LEU   B 1 94  ? 0.259  11.792  -35.764 1   33.511  ? 106 LEU   A HD21 1 c 2 
ATOM   3240 H HD22 . LEU   B 1 94  ? -0.243 13.296  -35.695 1   34.171  ? 106 LEU   A HD22 1 c 2 
ATOM   3241 H HD23 . LEU   B 1 94  ? -0.978 12.174  -34.846 1   33.823  ? 106 LEU   A HD23 1 c 2 
ATOM   3242 N N    . ILE   B 1 95  ? 3.162  11.623  -31.639 1   24.01   ? 107 ILE   A N    1 ? 2 
ATOM   3243 C CA   . ILE   B 1 95  ? 3.63   10.531  -30.783 1   25.513  ? 107 ILE   A CA   1 ? 2 
ATOM   3244 C C    . ILE   B 1 95  ? 2.507  9.716   -30.178 1   25.538  ? 107 ILE   A C    1 ? 2 
ATOM   3245 O O    . ILE   B 1 95  ? 1.758  10.194  -29.357 1   26.53   ? 107 ILE   A O    1 ? 2 
ATOM   3246 C CB   . ILE   B 1 95  ? 4.531  11.078  -29.643 1   22.834  ? 107 ILE   A CB   1 ? 2 
ATOM   3247 C CG1  . ILE   B 1 95  ? 5.646  11.93   -30.168 1   25.104  ? 107 ILE   A CG1  1 ? 2 
ATOM   3248 C CG2  . ILE   B 1 95  ? 5.038  9.95    -28.789 1   24.317  ? 107 ILE   A CG2  1 ? 2 
ATOM   3249 C CD1  . ILE   B 1 95  ? 6.295  12.862  -29.152 1   23.052  ? 107 ILE   A CD1  1 ? 2 
ATOM   3250 H H    . ILE   B 1 95  ? 2.523  12.183  -31.301 1   25.163  ? 107 ILE   A H    1 c 2 
ATOM   3251 H HA   . ILE   B 1 95  ? 4.175  9.936   -31.329 1   24.822  ? 107 ILE   A HA   1 c 2 
ATOM   3252 H HB   . ILE   B 1 95  ? 3.973  11.647  -29.077 1   24      ? 107 ILE   A HB   1 c 2 
ATOM   3253 H HG12 . ILE   B 1 95  ? 6.338  11.342  -30.534 1   24.083  ? 107 ILE   A HG12 1 c 2 
ATOM   3254 H HG13 . ILE   B 1 95  ? 5.303  12.475  -30.905 1   24.448  ? 107 ILE   A HG13 1 c 2 
ATOM   3255 H HG21 . ILE   B 1 95  ? 5.794  10.254  -28.261 1   23.532  ? 107 ILE   A HG21 1 c 2 
ATOM   3256 H HG22 . ILE   B 1 95  ? 5.317  9.211   -29.356 1   24.116  ? 107 ILE   A HG22 1 c 2 
ATOM   3257 H HG23 . ILE   B 1 95  ? 4.333  9.65    -28.193 1   24.175  ? 107 ILE   A HG23 1 c 2 
ATOM   3258 H HD11 . ILE   B 1 95  ? 5.618  13.465  -28.791 1   23.709  ? 107 ILE   A HD11 1 c 2 
ATOM   3259 H HD12 . ILE   B 1 95  ? 6.995  13.385  -29.587 1   23.563  ? 107 ILE   A HD12 1 c 2 
ATOM   3260 H HD13 . ILE   B 1 95  ? 6.684  12.343  -28.424 1   23.357  ? 107 ILE   A HD13 1 c 2 
ATOM   3261 N N    . LYS   B 1 96  ? 2.46   8.425   -30.544 1   29.646  ? 108 LYS   A N    1 ? 2 
ATOM   3262 C CA   . LYS   B 1 96  ? 1.577  7.472   -29.922 1   29.242  ? 108 LYS   A CA   1 ? 2 
ATOM   3263 C C    . LYS   B 1 96  ? 2.004  7.138   -28.477 1   29.907  ? 108 LYS   A C    1 ? 2 
ATOM   3264 O O    . LYS   B 1 96  ? 3.132  7.315   -28.094 1   26.128  ? 108 LYS   A O    1 ? 2 
ATOM   3265 C CB   . LYS   B 1 96  ? 1.543  6.188   -30.756 1   31.135  ? 108 LYS   A CB   1 ? 2 
ATOM   3266 C CG   . LYS   B 1 96  ? 0.999  6.32    -32.145 1   33.795  ? 108 LYS   A CG   1 ? 2 
ATOM   3267 C CD   . LYS   B 1 96  ? 0.807  5.002   -32.958 1   39.486  ? 108 LYS   A CD   1 ? 2 
ATOM   3268 C CE   . LYS   B 1 96  ? 0.153  5.082   -34.339 1   43.695  ? 108 LYS   A CE   1 ? 2 
ATOM   3269 N NZ   . LYS   B 1 96  ? 0.318  3.708   -34.879 1   48.293  ? 108 LYS   A NZ   1 ? 2 
ATOM   3270 H H    . LYS   B 1 96  ? 3.01   8.135   -31.215 1   28.568  ? 108 LYS   A H    1 c 2 
ATOM   3271 H HA   . LYS   B 1 96  ? 0.669  7.863   -29.907 1   30.239  ? 108 LYS   A HA   1 c 2 
ATOM   3272 H HB2  . LYS   B 1 96  ? 2.457  5.837   -30.818 1   31.051  ? 108 LYS   A HB2  1 c 2 
ATOM   3273 H HB3  . LYS   B 1 96  ? 1.005  5.522   -30.279 1   32.163  ? 108 LYS   A HB3  1 c 2 
ATOM   3274 H HG2  . LYS   B 1 96  ? 0.131  6.776   -32.087 1   34.534  ? 108 LYS   A HG2  1 c 2 
ATOM   3275 H HG3  . LYS   B 1 96  ? 1.599  6.91    -32.65  1   33.616  ? 108 LYS   A HG3  1 c 2 
ATOM   3276 H HD2  . LYS   B 1 96  ? 1.691  4.588   -33.061 1   38.935  ? 108 LYS   A HD2  1 c 2 
ATOM   3277 H HD3  . LYS   B 1 96  ? 0.278  4.388   -32.405 1   39.839  ? 108 LYS   A HD3  1 c 2 
ATOM   3278 H HE2  . LYS   B 1 96  ? -0.792 5.307   -34.27  1   44.321  ? 108 LYS   A HE2  1 c 2 
ATOM   3279 H HE3  . LYS   B 1 96  ? 0.608  5.727   -34.91  1   43.221  ? 108 LYS   A HE3  1 c 2 
ATOM   3280 H HZ1  . LYS   B 1 96  ? -0.112 3.113   -34.347 1   47.859  ? 108 LYS   A HZ1  1 c 2 
ATOM   3281 H HZ2  . LYS   B 1 96  ? 1.196  3.489   -34.922 1   46.758  ? 108 LYS   A HZ2  1 c 2 
ATOM   3282 H HZ3  . LYS   B 1 96  ? -0.037 3.666   -35.712 1   48.531  ? 108 LYS   A HZ3  1 c 2 
ATOM   3283 N N    . PRO   B 1 97  ? 1.052  6.705   -27.626 1   28.495  ? 109 PRO   A N    1 ? 2 
ATOM   3284 C CA   . PRO   B 1 97  ? 1.26   6.626   -26.186 1   32.372  ? 109 PRO   A CA   1 ? 2 
ATOM   3285 C C    . PRO   B 1 97  ? 2.419  5.711   -25.825 1   32.153  ? 109 PRO   A C    1 ? 2 
ATOM   3286 O O    . PRO   B 1 97  ? 3.171  5.954   -24.885 1   30.649  ? 109 PRO   A O    1 ? 2 
ATOM   3287 C CB   . PRO   B 1 97  ? -0.06  6.187   -25.609 1   31.929  ? 109 PRO   A CB   1 ? 2 
ATOM   3288 C CG   . PRO   B 1 97  ? -1.091 6.181   -26.718 1   33.536  ? 109 PRO   A CG   1 ? 2 
ATOM   3289 C CD   . PRO   B 1 97  ? -0.363 6.513   -27.959 1   33.08   ? 109 PRO   A CD   1 ? 2 
ATOM   3290 H HA   . PRO   B 1 97  ? 1.46   7.539   -25.86  1   30.453  ? 109 PRO   A HA   1 c 2 
ATOM   3291 H HB2  . PRO   B 1 97  ? 0.02   5.287   -25.214 1   33.489  ? 109 PRO   A HB2  1 c 2 
ATOM   3292 H HB3  . PRO   B 1 97  ? -0.338 6.801   -24.889 1   32.656  ? 109 PRO   A HB3  1 c 2 
ATOM   3293 H HG2  . PRO   B 1 97  ? -1.512 5.299   -26.793 1   34.635  ? 109 PRO   A HG2  1 c 2 
ATOM   3294 H HG3  . PRO   B 1 97  ? -1.789 6.845   -26.545 1   33.664  ? 109 PRO   A HG3  1 c 2 
ATOM   3295 H HD2  . PRO   B 1 97  ? -0.465 5.788   -28.614 1   32.823  ? 109 PRO   A HD2  1 c 2 
ATOM   3296 H HD3  . PRO   B 1 97  ? -0.735 7.332   -28.355 1   31.907  ? 109 PRO   A HD3  1 c 2 
ATOM   3297 N N    . GLU   B 1 98  ? 2.646  4.694   -26.634 1   31.892  ? 110 GLU   A N    1 ? 2 
ATOM   3298 C CA   . GLU   B 1 98  ? 3.718  3.746   -26.355 1   33.138  ? 110 GLU   A CA   1 ? 2 
ATOM   3299 C C    . GLU   B 1 98  ? 5.096  4.389   -26.373 1   29.271  ? 110 GLU   A C    1 ? 2 
ATOM   3300 O O    . GLU   B 1 98  ? 5.965  3.866   -25.681 1   30.029  ? 110 GLU   A O    1 ? 2 
ATOM   3301 C CB   . GLU   B 1 98  ? 3.731  2.551   -27.326 1   35.13   ? 110 GLU   A CB   1 ? 2 
ATOM   3302 C CG   . GLU   B 1 98  ? 2.391  1.842   -27.251 1   45.96   ? 110 GLU   A CG   1 ? 2 
ATOM   3303 C CD   . GLU   B 1 98  ? 1.089  2.45    -27.835 1   45.586  ? 110 GLU   A CD   1 ? 2 
ATOM   3304 O OE1  . GLU   B 1 98  ? 1.073  3.388   -28.683 1   33.756  ? 110 GLU   A OE1  1 ? 2 
ATOM   3305 O OE2  . GLU   B 1 98  ? 0.043  1.926   -27.366 1   51.45   ? 110 GLU   A OE2  1 ? 2 
ATOM   3306 H H    . GLU   B 1 98  ? 2.141  4.586   -27.387 1   32.589  ? 110 GLU   A H    1 c 2 
ATOM   3307 H HA   . GLU   B 1 98  ? 3.567  3.383   -25.445 1   33.495  ? 110 GLU   A HA   1 c 2 
ATOM   3308 H HB2  . GLU   B 1 98  ? 3.898  2.874   -28.236 1   36.196  ? 110 GLU   A HB2  1 c 2 
ATOM   3309 H HB3  . GLU   B 1 98  ? 4.457  1.94    -27.081 1   37.443  ? 110 GLU   A HB3  1 c 2 
ATOM   3310 H HG2  . GLU   B 1 98  ? 2.504  0.963   -27.671 1   44.68   ? 110 GLU   A HG2  1 c 2 
ATOM   3311 H HG3  . GLU   B 1 98  ? 2.215  1.654   -26.304 1   43.999  ? 110 GLU   A HG3  1 c 2 
ATOM   3312 N N    . TYR   B 1 99  ? 5.272  5.55    -27.023 1   28.617  ? 111 TYR   A N    1 ? 2 
ATOM   3313 C CA   . TYR   B 1 99  ? 6.553  6.225   -27.077 1   25.042  ? 111 TYR   A CA   1 ? 2 
ATOM   3314 C C    . TYR   B 1 99  ? 6.54   7.482   -26.18  1   24.46   ? 111 TYR   A C    1 ? 2 
ATOM   3315 O O    . TYR   B 1 99  ? 7.406  8.347   -26.25  1   28.222  ? 111 TYR   A O    1 ? 2 
ATOM   3316 C CB   . TYR   B 1 99  ? 6.96   6.516   -28.497 1   26.898  ? 111 TYR   A CB   1 ? 2 
ATOM   3317 C CG   . TYR   B 1 99  ? 7.208  5.222   -29.267 1   27.296  ? 111 TYR   A CG   1 ? 2 
ATOM   3318 C CD1  . TYR   B 1 99  ? 6.177  4.481   -29.872 1   28.692  ? 111 TYR   A CD1  1 ? 2 
ATOM   3319 C CD2  . TYR   B 1 99  ? 8.512  4.807   -29.5   1   29.575  ? 111 TYR   A CD2  1 ? 2 
ATOM   3320 C CE1  . TYR   B 1 99  ? 6.451  3.349   -30.639 1   28.452  ? 111 TYR   A CE1  1 ? 2 
ATOM   3321 C CE2  . TYR   B 1 99  ? 8.789  3.629   -30.166 1   29.105  ? 111 TYR   A CE2  1 ? 2 
ATOM   3322 C CZ   . TYR   B 1 99  ? 7.761  2.913   -30.765 1   29.931  ? 111 TYR   A CZ   1 ? 2 
ATOM   3323 O OH   . TYR   B 1 99  ? 8.164  1.778   -31.421 1   36.657  ? 111 TYR   A OH   1 ? 2 
ATOM   3324 H H    . TYR   B 1 99  ? 4.566  5.925   -27.466 1   27.586  ? 111 TYR   A H    1 c 2 
ATOM   3325 H HA   . TYR   B 1 99  ? 7.232  5.605   -26.701 1   26.65   ? 111 TYR   A HA   1 c 2 
ATOM   3326 H HB2  . TYR   B 1 99  ? 6.245  7.027   -28.937 1   25.847  ? 111 TYR   A HB2  1 c 2 
ATOM   3327 H HB3  . TYR   B 1 99  ? 7.781  7.056   -28.492 1   25.759  ? 111 TYR   A HB3  1 c 2 
ATOM   3328 H HD1  . TYR   B 1 99  ? 5.284  4.775   -29.787 1   28.005  ? 111 TYR   A HD1  1 c 2 
ATOM   3329 H HD2  . TYR   B 1 99  ? 9.221  5.27    -29.083 1   28.259  ? 111 TYR   A HD2  1 c 2 
ATOM   3330 H HE1  . TYR   B 1 99  ? 5.746  2.837   -30.997 1   29.969  ? 111 TYR   A HE1  1 c 2 
ATOM   3331 H HE2  . TYR   B 1 99  ? 9.681  3.351   -30.28  1   30.168  ? 111 TYR   A HE2  1 c 2 
ATOM   3332 H HH   . TYR   B 1 99  ? 8.301  1.964   -32.223 0   30      ? 111 TYR   A HH   1 c 2 
ATOM   3333 N N    . ALA   B 1 100 ? 5.505  7.606   -25.397 1   25.383  ? 112 ALA   A N    1 ? 2 
ATOM   3334 C CA   . ALA   B 1 100 ? 5.35   8.804   -24.553 1   26.422  ? 112 ALA   A CA   1 ? 2 
ATOM   3335 C C    . ALA   B 1 100 ? 5.085  8.337   -23.125 1   25.643  ? 112 ALA   A C    1 ? 2 
ATOM   3336 O O    . ALA   B 1 100 ? 6.033  7.901   -22.434 1   28.535  ? 112 ALA   A O    1 ? 2 
ATOM   3337 C CB   . ALA   B 1 100 ? 4.25   9.687   -25.055 1   25.277  ? 112 ALA   A CB   1 ? 2 
ATOM   3338 H H    . ALA   B 1 100 ? 4.872  6.95    -25.355 1   26.219  ? 112 ALA   A H    1 c 2 
ATOM   3339 H HA   . ALA   B 1 100 ? 6.205  9.313   -24.559 1   25.238  ? 112 ALA   A HA   1 c 2 
ATOM   3340 H HB1  . ALA   B 1 100 ? 4.531  10.119  -25.879 1   24.956  ? 112 ALA   A HB1  1 c 2 
ATOM   3341 H HB2  . ALA   B 1 100 ? 3.456  9.155   -25.229 1   26.04   ? 112 ALA   A HB2  1 c 2 
ATOM   3342 H HB3  . ALA   B 1 100 ? 4.045  10.368  -24.392 1   25.702  ? 112 ALA   A HB3  1 c 2 
ATOM   3343 N N    . TYR   B 1 101 ? 3.852  8.447   -22.613 1   27.133  ? 113 TYR   A N    1 ? 2 
ATOM   3344 C CA   . TYR   B 1 101 ? 3.571  8.066   -21.256 1   28.648  ? 113 TYR   A CA   1 ? 2 
ATOM   3345 C C    . TYR   B 1 101 ? 2.713  6.806   -21.109 1   33.208  ? 113 TYR   A C    1 ? 2 
ATOM   3346 O O    . TYR   B 1 101 ? 2.371  6.4     -19.998 1   31.599  ? 113 TYR   A O    1 ? 2 
ATOM   3347 C CB   . TYR   B 1 101 ? 2.936  9.238   -20.468 1   31.438  ? 113 TYR   A CB   1 ? 2 
ATOM   3348 C CG   . TYR   B 1 101 ? 3.887  10.426  -20.403 1   32.886  ? 113 TYR   A CG   1 ? 2 
ATOM   3349 C CD1  . TYR   B 1 101 ? 4.945  10.477  -19.485 1   30.004  ? 113 TYR   A CD1  1 ? 2 
ATOM   3350 C CD2  . TYR   B 1 101 ? 3.825  11.423  -21.384 1   28.076  ? 113 TYR   A CD2  1 ? 2 
ATOM   3351 C CE1  . TYR   B 1 101 ? 5.806  11.546  -19.452 1   28.081  ? 113 TYR   A CE1  1 ? 2 
ATOM   3352 C CE2  . TYR   B 1 101 ? 4.703  12.482  -21.371 1   27.661  ? 113 TYR   A CE2  1 ? 2 
ATOM   3353 C CZ   . TYR   B 1 101 ? 5.674  12.58   -20.358 1   30.848  ? 113 TYR   A CZ   1 ? 2 
ATOM   3354 O OH   . TYR   B 1 101 ? 6.613  13.579  -20.359 1   24.522  ? 113 TYR   A OH   1 ? 2 
ATOM   3355 H H    . TYR   B 1 101 ? 3.167  8.756   -23.131 1   26.715  ? 113 TYR   A H    1 c 2 
ATOM   3356 H HA   . TYR   B 1 101 ? 4.441  7.871   -20.822 1   29.91   ? 113 TYR   A HA   1 c 2 
ATOM   3357 H HB2  . TYR   B 1 101 ? 2.103  9.51    -20.914 1   31.254  ? 113 TYR   A HB2  1 c 2 
ATOM   3358 H HB3  . TYR   B 1 101 ? 2.727  8.937   -19.556 1   32.692  ? 113 TYR   A HB3  1 c 2 
ATOM   3359 H HD1  . TYR   B 1 101 ? 5.011  9.811   -18.821 1   31.426  ? 113 TYR   A HD1  1 c 2 
ATOM   3360 H HD2  . TYR   B 1 101 ? 3.139  11.397  -22.033 1   28.564  ? 113 TYR   A HD2  1 c 2 
ATOM   3361 H HE1  . TYR   B 1 101 ? 6.482  11.583  -18.797 1   30.025  ? 113 TYR   A HE1  1 c 2 
ATOM   3362 H HE2  . TYR   B 1 101 ? 4.618  13.171  -22.006 1   27.641  ? 113 TYR   A HE2  1 c 2 
ATOM   3363 H HH   . TYR   B 1 101 ? 7.246  13.377  -20.909 0   30      ? 113 TYR   A HH   1 c 2 
ATOM   3364 N N    . GLY   B 1 102 ? 2.342  6.116   -22.202 1   30.874  ? 114 GLY   A N    1 ? 2 
ATOM   3365 C CA   . GLY   B 1 102 ? 1.865  4.756   -22.052 1   32.36   ? 114 GLY   A CA   1 ? 2 
ATOM   3366 C C    . GLY   B 1 102 ? 0.416  4.616   -21.653 1   34.43   ? 114 GLY   A C    1 ? 2 
ATOM   3367 O O    . GLY   B 1 102 ? -0.305 5.594   -21.488 1   36.485  ? 114 GLY   A O    1 ? 2 
ATOM   3368 H H    . GLY   B 1 102 ? 2.381  6.494   -23.033 1   30.26   ? 114 GLY   A H    1 c 2 
ATOM   3369 H HA2  . GLY   B 1 102 ? 2.001  4.287   -22.908 1   32.271  ? 114 GLY   A HA2  1 c 2 
ATOM   3370 H HA3  . GLY   B 1 102 ? 2.425  4.301   -21.379 1   33.398  ? 114 GLY   A HA3  1 c 2 
ATOM   3371 N N    . SER   B 1 103 ? 0.096  3.397   -21.229 1   38.085  ? 115 SER   A N    1 ? 2 
ATOM   3372 C CA   . SER   B 1 103 ? -1.206 3.132   -20.659 1   41.572  ? 115 SER   A CA   1 ? 2 
ATOM   3373 C C    . SER   B 1 103 ? -1.332 3.746   -19.288 1   42.381  ? 115 SER   A C    1 ? 2 
ATOM   3374 O O    . SER   B 1 103 ? -2.431 4.087   -18.88  1   42.183  ? 115 SER   A O    1 ? 2 
ATOM   3375 C CB   . SER   B 1 103 ? -1.596 1.691   -20.678 1   44.535  ? 115 SER   A CB   1 ? 2 
ATOM   3376 O OG   . SER   B 1 103 ? -0.814 0.88    -19.839 1   49.585  ? 115 SER   A OG   1 ? 2 
ATOM   3377 H H    . SER   B 1 103 ? 0.7    2.714   -21.298 1   38.365  ? 115 SER   A H    1 c 2 
ATOM   3378 H HA   . SER   B 1 103 ? -1.859 3.605   -21.232 1   40.75   ? 115 SER   A HA   1 c 2 
ATOM   3379 H HB2  . SER   B 1 103 ? -2.531 1.616   -20.408 1   46.635  ? 115 SER   A HB2  1 c 2 
ATOM   3380 H HB3  . SER   B 1 103 ? -1.528 1.359   -21.593 1   44.685  ? 115 SER   A HB3  1 c 2 
ATOM   3381 H HG   . SER   B 1 103 ? -1.17  0.088   -19.918 0   30      ? 115 SER   A HG   1 c 2 
ATOM   3382 N N    . ALA   B 1 104 ? -0.212 3.918   -18.569 1   43.845  ? 116 ALA   A N    1 ? 2 
ATOM   3383 C CA   . ALA   B 1 104 ? -0.333 4.411   -17.226 1   43.166  ? 116 ALA   A CA   1 ? 2 
ATOM   3384 C C    . ALA   B 1 104 ? -0.589 5.928   -17.249 1   41.279  ? 116 ALA   A C    1 ? 2 
ATOM   3385 O O    . ALA   B 1 104 ? -1.198 6.494   -16.313 1   40.646  ? 116 ALA   A O    1 ? 2 
ATOM   3386 C CB   . ALA   B 1 104 ? 0.943  4.055   -16.474 1   47.131  ? 116 ALA   A CB   1 ? 2 
ATOM   3387 H H    . ALA   B 1 104 ? 0.612  3.722   -18.913 1   42.011  ? 116 ALA   A H    1 c 2 
ATOM   3388 H HA   . ALA   B 1 104 ? -1.109 3.963   -16.789 1   45.954  ? 116 ALA   A HA   1 c 2 
ATOM   3389 H HB1  . ALA   B 1 104 ? 1.062  3.09    -16.47  1   47.284  ? 116 ALA   A HB1  1 c 2 
ATOM   3390 H HB2  . ALA   B 1 104 ? 1.706  4.47    -16.91  1   44.418  ? 116 ALA   A HB2  1 c 2 
ATOM   3391 H HB3  . ALA   B 1 104 ? 0.883  4.375   -15.558 1   47.402  ? 116 ALA   A HB3  1 c 2 
ATOM   3392 N N    . GLY   B 1 105 ? 0.001  6.575   -18.236 1   38.451  ? 117 GLY   A N    1 ? 2 
ATOM   3393 C CA   . GLY   B 1 105 ? -0.027 8.021   -18.305 1   39.241  ? 117 GLY   A CA   1 ? 2 
ATOM   3394 C C    . GLY   B 1 105 ? 0.866  8.622   -17.212 1   38.12   ? 117 GLY   A C    1 ? 2 
ATOM   3395 O O    . GLY   B 1 105 ? 1.763  7.972   -16.746 1   36.903  ? 117 GLY   A O    1 ? 2 
ATOM   3396 H H    . GLY   B 1 105 ? 0.443  6.111   -18.888 1   38.11   ? 117 GLY   A H    1 c 2 
ATOM   3397 H HA2  . GLY   B 1 105 ? 0.291  8.312   -19.192 1   36.791  ? 117 GLY   A HA2  1 c 2 
ATOM   3398 H HA3  . GLY   B 1 105 ? -0.955 8.336   -18.191 1   39.157  ? 117 GLY   A HA3  1 c 2 
ATOM   3399 N N    . SER   B 1 106 ? 0.598  9.865   -16.836 1   34.309  ? 118 SER   A N    1 ? 2 
ATOM   3400 C CA   . SER   B 1 106 ? 1.362  10.616  -15.865 1   33.387  ? 118 SER   A CA   1 ? 2 
ATOM   3401 C C    . SER   B 1 106 ? 0.395  11.563  -15.198 1   33.518  ? 118 SER   A C    1 ? 2 
ATOM   3402 O O    . SER   B 1 106 ? 0.514  12.758  -15.321 1   36.309  ? 118 SER   A O    1 ? 2 
ATOM   3403 C CB   . SER   B 1 106 ? 2.496  11.331  -16.485 1   29.474  ? 118 SER   A CB   1 ? 2 
ATOM   3404 O OG   . SER   B 1 106 ? 3.293  11.961  -15.514 1   33.748  ? 118 SER   A OG   1 ? 2 
ATOM   3405 H H    . SER   B 1 106 ? -0.12  10.278  -17.223 1   34.631  ? 118 SER   A H    1 c 2 
ATOM   3406 H HA   . SER   B 1 106 ? 1.712  9.989   -15.182 1   34.25   ? 118 SER   A HA   1 c 2 
ATOM   3407 H HB2  . SER   B 1 106 ? 3.041  10.696  -16.988 1   29.642  ? 118 SER   A HB2  1 c 2 
ATOM   3408 H HB3  . SER   B 1 106 ? 2.157  11.999  -17.11  1   29.753  ? 118 SER   A HB3  1 c 2 
ATOM   3409 H HG   . SER   B 1 106 ? 3.926  12.333  -15.934 0   30      ? 118 SER   A HG   1 c 2 
ATOM   3410 N N    . LEU   B 1 107 ? -0.513 10.994  -14.449 1   36.694  ? 119 LEU   A N    1 ? 2 
ATOM   3411 C CA   . LEU   B 1 107 ? -1.649 11.717  -13.899 1   40.759  ? 119 LEU   A CA   1 ? 2 
ATOM   3412 C C    . LEU   B 1 107 ? -1.238 12.614  -12.755 1   45.074  ? 119 LEU   A C    1 ? 2 
ATOM   3413 O O    . LEU   B 1 107 ? -0.38  12.246  -11.973 1   46.888  ? 119 LEU   A O    1 ? 2 
ATOM   3414 C CB   . LEU   B 1 107 ? -2.708 10.707  -13.546 1   44.439  ? 119 LEU   A CB   1 ? 2 
ATOM   3415 C CG   . LEU   B 1 107 ? -3.466 10.166  -14.771 1   51.91   ? 119 LEU   A CG   1 ? 2 
ATOM   3416 C CD1  . LEU   B 1 107 ? -4.302 8.937   -14.357 1   62.077  ? 119 LEU   A CD1  1 ? 2 
ATOM   3417 C CD2  . LEU   B 1 107 ? -4.364 11.274  -15.32  1   51.86   ? 119 LEU   A CD2  1 ? 2 
ATOM   3418 H H    . LEU   B 1 107 ? -0.431 10.104  -14.26  1   37.493  ? 119 LEU   A H    1 c 2 
ATOM   3419 H HA   . LEU   B 1 107 ? -1.996 12.295  -14.62  1   40.171  ? 119 LEU   A HA   1 c 2 
ATOM   3420 H HB2  . LEU   B 1 107 ? -2.28  9.952   -13.08  1   46.433  ? 119 LEU   A HB2  1 c 2 
ATOM   3421 H HB3  . LEU   B 1 107 ? -3.354 11.129  -12.934 1   47.777  ? 119 LEU   A HB3  1 c 2 
ATOM   3422 H HG   . LEU   B 1 107 ? -2.81  9.899   -15.465 1   49.097  ? 119 LEU   A HG   1 c 2 
ATOM   3423 H HD11 . LEU   B 1 107 ? -3.709 8.212   -14.098 1   59.688  ? 119 LEU   A HD11 1 c 2 
ATOM   3424 H HD12 . LEU   B 1 107 ? -4.853 8.652   -15.105 1   59.056  ? 119 LEU   A HD12 1 c 2 
ATOM   3425 H HD13 . LEU   B 1 107 ? -4.874 9.171   -13.606 1   61.766  ? 119 LEU   A HD13 1 c 2 
ATOM   3426 H HD21 . LEU   B 1 107 ? -3.82  11.949  -15.757 1   50.079  ? 119 LEU   A HD21 1 c 2 
ATOM   3427 H HD22 . LEU   B 1 107 ? -4.862 11.681  -14.591 1   53.631  ? 119 LEU   A HD22 1 c 2 
ATOM   3428 H HD23 . LEU   B 1 107 ? -4.987 10.896  -15.963 1   51.534  ? 119 LEU   A HD23 1 c 2 
ATOM   3429 N N    . PRO   B 1 108 ? -1.928 13.752  -12.537 1   48.445  ? 120 PRO   A N    1 ? 2 
ATOM   3430 C CA   . PRO   B 1 108 ? -3.125 14.12   -13.313 1   46.767  ? 120 PRO   A CA   1 ? 2 
ATOM   3431 C C    . PRO   B 1 108 ? -2.807 14.874  -14.604 1   43.911  ? 120 PRO   A C    1 ? 2 
ATOM   3432 O O    . PRO   B 1 108 ? -3.685 15.202  -15.382 1   45.885  ? 120 PRO   A O    1 ? 2 
ATOM   3433 C CB   . PRO   B 1 108 ? -3.899 15.006  -12.33  1   48.649  ? 120 PRO   A CB   1 ? 2 
ATOM   3434 C CG   . PRO   B 1 108 ? -2.959 15.346  -11.276 1   49.845  ? 120 PRO   A CG   1 ? 2 
ATOM   3435 C CD   . PRO   B 1 108 ? -1.666 14.667  -11.417 1   47.557  ? 120 PRO   A CD   1 ? 2 
ATOM   3436 H HA   . PRO   B 1 108 ? -3.655 13.313  -13.514 1   46.853  ? 120 PRO   A HA   1 c 2 
ATOM   3437 H HB2  . PRO   B 1 108 ? -4.23  15.82   -12.777 1   48.812  ? 120 PRO   A HB2  1 c 2 
ATOM   3438 H HB3  . PRO   B 1 108 ? -4.673 14.519  -11.96  1   50.672  ? 120 PRO   A HB3  1 c 2 
ATOM   3439 H HG2  . PRO   B 1 108 ? -2.812 16.315  -11.278 1   50.127  ? 120 PRO   A HG2  1 c 2 
ATOM   3440 H HG3  . PRO   B 1 108 ? -3.35  15.113  -10.408 1   52.324  ? 120 PRO   A HG3  1 c 2 
ATOM   3441 H HD2  . PRO   B 1 108 ? -0.953 15.305  -11.632 1   47.523  ? 120 PRO   A HD2  1 c 2 
ATOM   3442 H HD3  . PRO   B 1 108 ? -1.432 14.175  -10.599 1   49.967  ? 120 PRO   A HD3  1 c 2 
ATOM   3443 N N    . LYS   B 1 109 ? -1.55  15.183  -14.856 1   42.958  ? 121 LYS   A N    1 ? 2 
ATOM   3444 C CA   . LYS   B 1 109 ? -1.203 16.052  -15.965 1   39.927  ? 121 LYS   A CA   1 ? 2 
ATOM   3445 C C    . LYS   B 1 109 ? -1.387 15.356  -17.315 1   38.986  ? 121 LYS   A C    1 ? 2 
ATOM   3446 O O    . LYS   B 1 109 ? -1.774 16.026  -18.253 1   36.814  ? 121 LYS   A O    1 ? 2 
ATOM   3447 C CB   . LYS   B 1 109 ? 0.245  16.501  -15.899 1   41.059  ? 121 LYS   A CB   1 ? 2 
ATOM   3448 C CG   . LYS   B 1 109 ? 0.749  17.416  -17.053 1   44.226  ? 121 LYS   A CG   1 ? 2 
ATOM   3449 C CD   . LYS   B 1 109 ? 2.235  17.711  -16.873 1   47.18   ? 121 LYS   A CD   1 ? 2 
ATOM   3450 C CE   . LYS   B 1 109 ? 2.626  18.399  -15.563 1   52.844  ? 121 LYS   A CE   1 ? 2 
ATOM   3451 N NZ   . LYS   B 1 109 ? 2.384  19.833  -15.607 1   53.816  ? 121 LYS   A NZ   1 ? 2 
ATOM   3452 H H    . LYS   B 1 109 ? -0.881 14.85   -14.331 1   42.676  ? 121 LYS   A H    1 c 2 
ATOM   3453 H HA   . LYS   B 1 109 ? -1.789 16.851  -15.934 1   41.953  ? 121 LYS   A HA   1 c 2 
ATOM   3454 H HB2  . LYS   B 1 109 ? 0.373  16.978  -15.052 1   43.304  ? 121 LYS   A HB2  1 c 2 
ATOM   3455 H HB3  . LYS   B 1 109 ? 0.814  15.702  -15.873 1   40.668  ? 121 LYS   A HB3  1 c 2 
ATOM   3456 H HG2  . LYS   B 1 109 ? 0.607  16.966  -17.914 1   42.259  ? 121 LYS   A HG2  1 c 2 
ATOM   3457 H HG3  . LYS   B 1 109 ? 0.241  18.256  -17.046 1   44.899  ? 121 LYS   A HG3  1 c 2 
ATOM   3458 H HD2  . LYS   B 1 109 ? 2.727  16.864  -16.941 1   45.995  ? 121 LYS   A HD2  1 c 2 
ATOM   3459 H HD3  . LYS   B 1 109 ? 2.529  18.275  -17.622 1   46.138  ? 121 LYS   A HD3  1 c 2 
ATOM   3460 H HE2  . LYS   B 1 109 ? 2.14   18.016  -14.813 1   53.191  ? 121 LYS   A HE2  1 c 2 
ATOM   3461 H HE3  . LYS   B 1 109 ? 3.576  18.255  -15.406 1   51.647  ? 121 LYS   A HE3  1 c 2 
ATOM   3462 H HZ1  . LYS   B 1 109 ? 1.506  19.99   -15.768 1   54.479  ? 121 LYS   A HZ1  1 c 2 
ATOM   3463 H HZ2  . LYS   B 1 109 ? 2.879  20.208  -16.266 1   52.911  ? 121 LYS   A HZ2  1 c 2 
ATOM   3464 H HZ3  . LYS   B 1 109 ? 2.612  20.206  -14.813 1   55.623  ? 121 LYS   A HZ3  1 c 2 
ATOM   3465 N N    . ILE   B 1 110 ? -1.061 14.058  -17.433 1   35.02   ? 122 ILE   A N    1 ? 2 
ATOM   3466 C CA   . ILE   B 1 110 ? -1.161 13.419  -18.754 1   35.463  ? 122 ILE   A CA   1 ? 2 
ATOM   3467 C C    . ILE   B 1 110 ? -2.026 12.195  -18.6   1   35.523  ? 122 ILE   A C    1 ? 2 
ATOM   3468 O O    . ILE   B 1 110 ? -1.686 11.342  -17.784 1   41.909  ? 122 ILE   A O    1 ? 2 
ATOM   3469 C CB   . ILE   B 1 110 ? 0.216  12.978  -19.279 1   33.671  ? 122 ILE   A CB   1 ? 2 
ATOM   3470 C CG1  . ILE   B 1 110 ? 1.276  14.042  -19.292 1   34.414  ? 122 ILE   A CG1  1 ? 2 
ATOM   3471 C CG2  . ILE   B 1 110 ? 0.121  12.261  -20.65  1   31.721  ? 122 ILE   A CG2  1 ? 2 
ATOM   3472 C CD1  . ILE   B 1 110 ? 1.055  15.119  -20.277 1   35.241  ? 122 ILE   A CD1  1 ? 2 
ATOM   3473 H H    . ILE   B 1 110 ? -0.779 13.574  -16.712 1   36.893  ? 122 ILE   A H    1 c 2 
ATOM   3474 H HA   . ILE   B 1 110 ? -1.567 14.036  -19.391 1   34.73   ? 122 ILE   A HA   1 c 2 
ATOM   3475 H HB   . ILE   B 1 110 ? 0.534  12.302  -18.648 1   34.281  ? 122 ILE   A HB   1 c 2 
ATOM   3476 H HG12 . ILE   B 1 110 ? 1.331  14.441  -18.4   1   35.598  ? 122 ILE   A HG12 1 c 2 
ATOM   3477 H HG13 . ILE   B 1 110 ? 2.139  13.62   -19.481 1   33.452  ? 122 ILE   A HG13 1 c 2 
ATOM   3478 H HG21 . ILE   B 1 110 ? 0.973  12.328  -21.114 1   30.679  ? 122 ILE   A HG21 1 c 2 
ATOM   3479 H HG22 . ILE   B 1 110 ? -0.572 12.678  -21.189 1   31.973  ? 122 ILE   A HG22 1 c 2 
ATOM   3480 H HG23 . ILE   B 1 110 ? -0.097 11.323  -20.515 1   32.215  ? 122 ILE   A HG23 1 c 2 
ATOM   3481 H HD11 . ILE   B 1 110 ? 1.064  14.753  -21.182 1   33.695  ? 122 ILE   A HD11 1 c 2 
ATOM   3482 H HD12 . ILE   B 1 110 ? 1.769  15.778  -20.189 1   34.589  ? 122 ILE   A HD12 1 c 2 
ATOM   3483 H HD13 . ILE   B 1 110 ? 0.195  15.549  -20.11  1   35.88   ? 122 ILE   A HD13 1 c 2 
ATOM   3484 N N    . PRO   B 1 111 ? -3.149 12.056  -19.35  1   38.279  ? 123 PRO   A N    1 ? 2 
ATOM   3485 C CA   . PRO   B 1 111 ? -4.046 10.928  -19.206 1   37.278  ? 123 PRO   A CA   1 ? 2 
ATOM   3486 C C    . PRO   B 1 111 ? -3.344 9.708   -19.79  1   35.209  ? 123 PRO   A C    1 ? 2 
ATOM   3487 O O    . PRO   B 1 111 ? -2.352 9.798   -20.472 1   31.962  ? 123 PRO   A O    1 ? 2 
ATOM   3488 C CB   . PRO   B 1 111 ? -5.314 11.241  -20.044 1   42.984  ? 123 PRO   A CB   1 ? 2 
ATOM   3489 C CG   . PRO   B 1 111 ? -5.09  12.583  -20.666 1   43.446  ? 123 PRO   A CG   1 ? 2 
ATOM   3490 C CD   . PRO   B 1 111 ? -3.685 13.068  -20.28  1   43.57   ? 123 PRO   A CD   1 ? 2 
ATOM   3491 H HA   . PRO   B 1 111 ? -4.279 10.786  -18.255 1   40.018  ? 123 PRO   A HA   1 c 2 
ATOM   3492 H HB2  . PRO   B 1 111 ? -5.451 10.556  -20.74  1   41.638  ? 123 PRO   A HB2  1 c 2 
ATOM   3493 H HB3  . PRO   B 1 111 ? -6.114 11.257  -19.468 1   44.023  ? 123 PRO   A HB3  1 c 2 
ATOM   3494 H HG2  . PRO   B 1 111 ? -5.167 12.521  -21.641 1   42.664  ? 123 PRO   A HG2  1 c 2 
ATOM   3495 H HG3  . PRO   B 1 111 ? -5.764 13.22   -20.348 1   44.954  ? 123 PRO   A HG3  1 c 2 
ATOM   3496 H HD2  . PRO   B 1 111 ? -3.115 13.144  -21.077 1   40.232  ? 123 PRO   A HD2  1 c 2 
ATOM   3497 H HD3  . PRO   B 1 111 ? -3.734 13.948  -19.846 1   42.467  ? 123 PRO   A HD3  1 c 2 
ATOM   3498 N N    . SER   B 1 112 ? -3.962 8.602   -19.458 1   37.009  ? 124 SER   A N    1 ? 2 
ATOM   3499 C CA   . SER   B 1 112 ? -3.752 7.282   -19.995 1   35.22   ? 124 SER   A CA   1 ? 2 
ATOM   3500 C C    . SER   B 1 112 ? -3.903 7.355   -21.506 1   34.349  ? 124 SER   A C    1 ? 2 
ATOM   3501 O O    . SER   B 1 112 ? -4.831 8       -21.954 1   35.455  ? 124 SER   A O    1 ? 2 
ATOM   3502 C CB   . SER   B 1 112 ? -4.74  6.395   -19.36  1   41.361  ? 124 SER   A CB   1 ? 2 
ATOM   3503 O OG   . SER   B 1 112 ? -4.52  5.05    -19.705 1   52.354  ? 124 SER   A OG   1 ? 2 
ATOM   3504 H H    . SER   B 1 112 ? -4.603 8.682   -18.811 1   38.302  ? 124 SER   A H    1 c 2 
ATOM   3505 H HA   . SER   B 1 112 ? -2.837 6.979   -19.766 1   35.567  ? 124 SER   A HA   1 c 2 
ATOM   3506 H HB2  . SER   B 1 112 ? -4.683 6.491   -18.39  1   43.608  ? 124 SER   A HB2  1 c 2 
ATOM   3507 H HB3  . SER   B 1 112 ? -5.637 6.659   -19.639 1   43.273  ? 124 SER   A HB3  1 c 2 
ATOM   3508 H HG   . SER   B 1 112 ? -5.089 4.601   -19.223 0   30      ? 124 SER   A HG   1 c 2 
ATOM   3509 N N    . ASN   B 1 113 ? -3.012 6.673   -22.207 1   32.389  ? 125 ASN   A N    1 ? 2 
ATOM   3510 C CA   . ASN   B 1 113 ? -3.18  6.425   -23.63  1   33.525  ? 125 ASN   A CA   1 ? 2 
ATOM   3511 C C    . ASN   B 1 113 ? -3.241 7.756   -24.425 1   30.425  ? 125 ASN   A C    1 ? 2 
ATOM   3512 O O    . ASN   B 1 113 ? -3.962 7.832   -25.447 1   30.708  ? 125 ASN   A O    1 ? 2 
ATOM   3513 C CB   . ASN   B 1 113 ? -4.385 5.528   -23.844 1   38.489  ? 125 ASN   A CB   1 ? 2 
ATOM   3514 C CG   . ASN   B 1 113 ? -4.235 4.155   -23.188 1   36.735  ? 125 ASN   A CG   1 ? 2 
ATOM   3515 O OD1  . ASN   B 1 113 ? -5.159 3.694   -22.536 1   38.435  ? 125 ASN   A OD1  1 ? 2 
ATOM   3516 N ND2  . ASN   B 1 113 ? -3.143 3.462   -23.442 1   37.113  ? 125 ASN   A ND2  1 ? 2 
ATOM   3517 H H    . ASN   B 1 113 ? -2.267 6.346   -21.79  1   32.693  ? 125 ASN   A H    1 c 2 
ATOM   3518 H HA   . ASN   B 1 113 ? -2.391 5.929   -23.941 1   32.587  ? 125 ASN   A HA   1 c 2 
ATOM   3519 H HB2  . ASN   B 1 113 ? -5.181 5.967   -23.486 1   37.973  ? 125 ASN   A HB2  1 c 2 
ATOM   3520 H HB3  . ASN   B 1 113 ? -4.52  5.404   -24.804 1   36.79   ? 125 ASN   A HB3  1 c 2 
ATOM   3521 H HD21 . ASN   B 1 113 ? -2.969 2.729   -22.975 1   37.848  ? 125 ASN   A HD21 1 c 2 
ATOM   3522 H HD22 . ASN   B 1 113 ? -2.591 3.717   -24.087 1   35.418  ? 125 ASN   A HD22 1 c 2 
ATOM   3523 N N    . ALA   B 1 114 ? -2.383 8.713   -24.032 1   26.572  ? 126 ALA   A N    1 ? 2 
ATOM   3524 C CA   . ALA   B 1 114 ? -2.31  10.057  -24.58  1   28.897  ? 126 ALA   A CA   1 ? 2 
ATOM   3525 C C    . ALA   B 1 114 ? -1.373 10.094  -25.791 1   27.012  ? 126 ALA   A C    1 ? 2 
ATOM   3526 O O    . ALA   B 1 114 ? -0.268 9.548   -25.796 1   29.051  ? 126 ALA   A O    1 ? 2 
ATOM   3527 C CB   . ALA   B 1 114 ? -1.949 11.035  -23.542 1   33.552  ? 126 ALA   A CB   1 ? 2 
ATOM   3528 H H    . ALA   B 1 114 ? -1.791 8.499   -23.369 1   27.758  ? 126 ALA   A H    1 c 2 
ATOM   3529 H HA   . ALA   B 1 114 ? -3.223 10.287  -24.907 1   29.854  ? 126 ALA   A HA   1 c 2 
ATOM   3530 H HB1  . ALA   B 1 114 ? -2.638 11.055  -22.858 1   33.233  ? 126 ALA   A HB1  1 c 2 
ATOM   3531 H HB2  . ALA   B 1 114 ? -1.101 10.784  -23.137 1   31.33   ? 126 ALA   A HB2  1 c 2 
ATOM   3532 H HB3  . ALA   B 1 114 ? -1.866 11.918  -23.94  1   31.586  ? 126 ALA   A HB3  1 c 2 
ATOM   3533 N N    . THR   B 1 115 ? -1.874 10.697  -26.878 1   26.902  ? 127 THR   A N    1 ? 2 
ATOM   3534 C CA   . THR   B 1 115 ? -1.076 11.085  -28.037 1   24.227  ? 127 THR   A CA   1 ? 2 
ATOM   3535 C C    . THR   B 1 115 ? -0.557 12.507  -27.842 1   23.154  ? 127 THR   A C    1 ? 2 
ATOM   3536 O O    . THR   B 1 115 ? -1.331 13.354  -27.438 1   26.718  ? 127 THR   A O    1 ? 2 
ATOM   3537 C CB   . THR   B 1 115 ? -1.992 10.976  -29.268 1   27.582  ? 127 THR   A CB   1 ? 2 
ATOM   3538 O OG1  . THR   B 1 115 ? -2.133 9.595   -29.549 1   29.413  ? 127 THR   A OG1  1 ? 2 
ATOM   3539 C CG2  . THR   B 1 115 ? -1.306 11.331  -30.559 1   29.085  ? 127 THR   A CG2  1 ? 2 
ATOM   3540 H H    . THR   B 1 115 ? -2.77  10.878  -26.897 1   27.654  ? 127 THR   A H    1 c 2 
ATOM   3541 H HA   . THR   B 1 115 ? -0.324 10.466  -28.134 1   24.214  ? 127 THR   A HA   1 c 2 
ATOM   3542 H HB   . THR   B 1 115 ? -2.87  11.412  -29.155 1   28.789  ? 127 THR   A HB   1 c 2 
ATOM   3543 H HG1  . THR   B 1 115 ? -1.35  9.231   -29.706 0   30      ? 127 THR   A HG1  1 c 2 
ATOM   3544 H HG21 . THR   B 1 115 ? -1.878 11.093  -31.308 1   29.504  ? 127 THR   A HG21 1 c 2 
ATOM   3545 H HG22 . THR   B 1 115 ? -0.467 10.844  -30.626 1   27.688  ? 127 THR   A HG22 1 c 2 
ATOM   3546 H HG23 . THR   B 1 115 ? -1.127 12.286  -30.581 1   28.387  ? 127 THR   A HG23 1 c 2 
ATOM   3547 N N    . LEU   B 1 116 ? 0.724  12.74   -28.092 1   24.444  ? 128 LEU   A N    1 ? 2 
ATOM   3548 C CA   . LEU   B 1 116 ? 1.343  14.03   -27.908 1   26.347  ? 128 LEU   A CA   1 ? 2 
ATOM   3549 C C    . LEU   B 1 116 ? 1.79   14.6    -29.243 1   23.808  ? 128 LEU   A C    1 ? 2 
ATOM   3550 O O    . LEU   B 1 116 ? 2.213  13.845  -30.123 1   25.124  ? 128 LEU   A O    1 ? 2 
ATOM   3551 C CB   . LEU   B 1 116 ? 2.549  13.952  -26.967 1   25.726  ? 128 LEU   A CB   1 ? 2 
ATOM   3552 C CG   . LEU   B 1 116 ? 2.182  13.92   -25.495 1   28.359  ? 128 LEU   A CG   1 ? 2 
ATOM   3553 C CD1  . LEU   B 1 116 ? 1.226  12.96   -24.896 1   34.631  ? 128 LEU   A CD1  1 ? 2 
ATOM   3554 C CD2  . LEU   B 1 116 ? 3.463  13.911  -24.601 1   27.754  ? 128 LEU   A CD2  1 ? 2 
ATOM   3555 H H    . LEU   B 1 116 ? 1.243  12.052  -28.398 1   23.78   ? 128 LEU   A H    1 c 2 
ATOM   3556 H HA   . LEU   B 1 116 ? 0.671  14.644  -27.516 1   26.175  ? 128 LEU   A HA   1 c 2 
ATOM   3557 H HB2  . LEU   B 1 116 ? 3.06   13.138  -27.182 1   25.607  ? 128 LEU   A HB2  1 c 2 
ATOM   3558 H HB3  . LEU   B 1 116 ? 3.124  14.736  -27.13  1   25.987  ? 128 LEU   A HB3  1 c 2 
ATOM   3559 H HG   . LEU   B 1 116 ? 1.767  14.803  -25.316 1   29.518  ? 128 LEU   A HG   1 c 2 
ATOM   3560 H HD11 . LEU   B 1 116 ? 0.336  13.128  -25.246 1   33.363  ? 128 LEU   A HD11 1 c 2 
ATOM   3561 H HD12 . LEU   B 1 116 ? 1.217  13.066  -23.93  1   33.245  ? 128 LEU   A HD12 1 c 2 
ATOM   3562 H HD13 . LEU   B 1 116 ? 1.495  12.052  -25.119 1   32.425  ? 128 LEU   A HD13 1 c 2 
ATOM   3563 H HD21 . LEU   B 1 116 ? 4.101  14.56   -24.941 1   27.532  ? 128 LEU   A HD21 1 c 2 
ATOM   3564 H HD22 . LEU   B 1 116 ? 3.864  13.025  -24.616 1   27.451  ? 128 LEU   A HD22 1 c 2 
ATOM   3565 H HD23 . LEU   B 1 116 ? 3.224  14.142  -23.687 1   28.511  ? 128 LEU   A HD23 1 c 2 
ATOM   3566 N N    . PHE   B 1 117 ? 1.784  15.96   -29.308 1   22.883  ? 129 PHE   A N    1 ? 2 
ATOM   3567 C CA   . PHE   B 1 117 ? 2.388  16.645  -30.415 1   22.979  ? 129 PHE   A CA   1 ? 2 
ATOM   3568 C C    . PHE   B 1 117 ? 3.488  17.584  -29.904 1   24.644  ? 129 PHE   A C    1 ? 2 
ATOM   3569 O O    . PHE   B 1 117 ? 3.278  18.313  -28.928 1   28.689  ? 129 PHE   A O    1 ? 2 
ATOM   3570 C CB   . PHE   B 1 117 ? 1.249  17.383  -31.145 1   25.165  ? 129 PHE   A CB   1 ? 2 
ATOM   3571 C CG   . PHE   B 1 117 ? 1.799  18.244  -32.27  1   29.024  ? 129 PHE   A CG   1 ? 2 
ATOM   3572 C CD1  . PHE   B 1 117 ? 1.932  17.779  -33.566 1   29.361  ? 129 PHE   A CD1  1 ? 2 
ATOM   3573 C CD2  . PHE   B 1 117 ? 2.066  19.584  -32.028 1   31.227  ? 129 PHE   A CD2  1 ? 2 
ATOM   3574 C CE1  . PHE   B 1 117 ? 2.485  18.59   -34.553 1   29.852  ? 129 PHE   A CE1  1 ? 2 
ATOM   3575 C CE2  . PHE   B 1 117 ? 2.609  20.391  -33.023 1   33.88   ? 129 PHE   A CE2  1 ? 2 
ATOM   3576 C CZ   . PHE   B 1 117 ? 2.842  19.885  -34.27  1   34.202  ? 129 PHE   A CZ   1 ? 2 
ATOM   3577 H H    . PHE   B 1 117 ? 1.393  16.449  -28.642 1   23.742  ? 129 PHE   A H    1 c 2 
ATOM   3578 H HA   . PHE   B 1 117 ? 2.788  15.979  -31.031 1   23.035  ? 129 PHE   A HA   1 c 2 
ATOM   3579 H HB2  . PHE   B 1 117 ? 0.623  16.722  -31.515 1   25.943  ? 129 PHE   A HB2  1 c 2 
ATOM   3580 H HB3  . PHE   B 1 117 ? 0.771  17.952  -30.501 1   26.325  ? 129 PHE   A HB3  1 c 2 
ATOM   3581 H HD1  . PHE   B 1 117 ? 1.758  16.87   -33.752 1   28.794  ? 129 PHE   A HD1  1 c 2 
ATOM   3582 H HD2  . PHE   B 1 117 ? 1.978  19.922  -31.151 1   31.17   ? 129 PHE   A HD2  1 c 2 
ATOM   3583 H HE1  . PHE   B 1 117 ? 2.614  18.247  -35.423 1   31.303  ? 129 PHE   A HE1  1 c 2 
ATOM   3584 H HE2  . PHE   B 1 117 ? 2.833  21.286  -32.831 1   34.341  ? 129 PHE   A HE2  1 c 2 
ATOM   3585 H HZ   . PHE   B 1 117 ? 3.149  20.451  -34.959 1   34.448  ? 129 PHE   A HZ   1 c 2 
ATOM   3586 N N    . PHE   B 1 118 ? 4.576  17.689  -30.663 1   26.511  ? 130 PHE   A N    1 ? 2 
ATOM   3587 C CA   . PHE   B 1 118 ? 5.591  18.684  -30.412 1   24.194  ? 130 PHE   A CA   1 ? 2 
ATOM   3588 C C    . PHE   B 1 118 ? 6.087  19.391  -31.658 1   27.153  ? 130 PHE   A C    1 ? 2 
ATOM   3589 O O    . PHE   B 1 118 ? 6.21   18.791  -32.705 1   27.644  ? 130 PHE   A O    1 ? 2 
ATOM   3590 C CB   . PHE   B 1 118 ? 6.851  18.087  -29.759 1   22.701  ? 130 PHE   A CB   1 ? 2 
ATOM   3591 C CG   . PHE   B 1 118 ? 6.55   17.587  -28.369 1   22.377  ? 130 PHE   A CG   1 ? 2 
ATOM   3592 C CD1  . PHE   B 1 118 ? 6.19   16.242  -28.176 1   23.149  ? 130 PHE   A CD1  1 ? 2 
ATOM   3593 C CD2  . PHE   B 1 118 ? 6.829  18.349  -27.231 1   27.107  ? 130 PHE   A CD2  1 ? 2 
ATOM   3594 C CE1  . PHE   B 1 118 ? 5.966  15.719  -26.918 1   22.812  ? 130 PHE   A CE1  1 ? 2 
ATOM   3595 C CE2  . PHE   B 1 118 ? 6.719  17.757  -25.958 1   24.311  ? 130 PHE   A CE2  1 ? 2 
ATOM   3596 C CZ   . PHE   B 1 118 ? 6.261  16.484  -25.815 1   27.177  ? 130 PHE   A CZ   1 ? 2 
ATOM   3597 H H    . PHE   B 1 118 ? 4.688  17.116  -31.366 1   25.15   ? 130 PHE   A H    1 c 2 
ATOM   3598 H HA   . PHE   B 1 118 ? 5.215  19.364  -29.796 1   25.596  ? 130 PHE   A HA   1 c 2 
ATOM   3599 H HB2  . PHE   B 1 118 ? 7.175  17.341  -30.311 1   22.388  ? 130 PHE   A HB2  1 c 2 
ATOM   3600 H HB3  . PHE   B 1 118 ? 7.549  18.778  -29.713 1   23.357  ? 130 PHE   A HB3  1 c 2 
ATOM   3601 H HD1  . PHE   B 1 118 ? 5.994  15.712  -28.933 1   22.617  ? 130 PHE   A HD1  1 c 2 
ATOM   3602 H HD2  . PHE   B 1 118 ? 7.171  19.224  -27.321 1   26.203  ? 130 PHE   A HD2  1 c 2 
ATOM   3603 H HE1  . PHE   B 1 118 ? 5.688  14.823  -26.818 1   23.368  ? 130 PHE   A HE1  1 c 2 
ATOM   3604 H HE2  . PHE   B 1 118 ? 6.85   18.29   -25.189 1   26.304  ? 130 PHE   A HE2  1 c 2 
ATOM   3605 H HZ   . PHE   B 1 118 ? 6.122  16.131  -24.95  1   25.431  ? 130 PHE   A HZ   1 c 2 
ATOM   3606 N N    . GLU   B 1 119 ? 6.42   20.68   -31.458 1   28.274  ? 131 GLU   A N    1 ? 2 
ATOM   3607 C CA   . GLU   B 1 119 ? 7.289  21.383  -32.382 1   30.53   ? 131 GLU   A CA   1 ? 2 
ATOM   3608 C C    . GLU   B 1 119 ? 8.609  21.629  -31.654 1   31.022  ? 131 GLU   A C    1 ? 2 
ATOM   3609 O O    . GLU   B 1 119 ? 8.603  22.08   -30.497 1   31.948  ? 131 GLU   A O    1 ? 2 
ATOM   3610 C CB   . GLU   B 1 119 ? 6.63   22.683  -32.807 1   31.426  ? 131 GLU   A CB   1 ? 2 
ATOM   3611 C CG   . GLU   B 1 119 ? 7.486  23.553  -33.714 1   36.698  ? 131 GLU   A CG   1 ? 2 
ATOM   3612 C CD   . GLU   B 1 119 ? 6.672  24.754  -34.155 1   36.938  ? 131 GLU   A CD   1 ? 2 
ATOM   3613 O OE1  . GLU   B 1 119 ? 5.825  24.729  -35.116 1   40.91   ? 131 GLU   A OE1  1 ? 2 
ATOM   3614 O OE2  . GLU   B 1 119 ? 6.775  25.8    -33.446 1   40.665  ? 131 GLU   A OE2  1 ? 2 
ATOM   3615 H H    . GLU   B 1 119 ? 6.093  21.128  -30.73  1   28.812  ? 131 GLU   A H    1 c 2 
ATOM   3616 H HA   . GLU   B 1 119 ? 7.447  20.813  -33.174 1   30.045  ? 131 GLU   A HA   1 c 2 
ATOM   3617 H HB2  . GLU   B 1 119 ? 5.793  22.473  -33.271 1   32.796  ? 131 GLU   A HB2  1 c 2 
ATOM   3618 H HB3  . GLU   B 1 119 ? 6.403  23.197  -32.004 1   32.786  ? 131 GLU   A HB3  1 c 2 
ATOM   3619 H HG2  . GLU   B 1 119 ? 8.282  23.86   -33.232 1   35.302  ? 131 GLU   A HG2  1 c 2 
ATOM   3620 H HG3  . GLU   B 1 119 ? 7.765  23.04   -34.503 1   35.156  ? 131 GLU   A HG3  1 c 2 
ATOM   3621 N N    . ILE   B 1 120 ? 9.691  21.282  -32.337 1   33.038  ? 132 ILE   A N    1 ? 2 
ATOM   3622 C CA   . ILE   B 1 120 ? 11.043 21.203  -31.773 1   28.162  ? 132 ILE   A CA   1 ? 2 
ATOM   3623 C C    . ILE   B 1 120 ? 11.964 21.914  -32.717 1   32.818  ? 132 ILE   A C    1 ? 2 
ATOM   3624 O O    . ILE   B 1 120 ? 12.095 21.51   -33.87  1   33.691  ? 132 ILE   A O    1 ? 2 
ATOM   3625 C CB   . ILE   B 1 120 ? 11.565 19.788  -31.485 1   28.77   ? 132 ILE   A CB   1 ? 2 
ATOM   3626 C CG1  . ILE   B 1 120 ? 10.561 18.969  -30.629 1   25.771  ? 132 ILE   A CG1  1 ? 2 
ATOM   3627 C CG2  . ILE   B 1 120 ? 12.956 19.871  -30.823 1   27.59   ? 132 ILE   A CG2  1 ? 2 
ATOM   3628 C CD1  . ILE   B 1 120 ? 10.882 17.506  -30.435 1   24.971  ? 132 ILE   A CD1  1 ? 2 
ATOM   3629 H H    . ILE   B 1 120 ? 9.589  21.08   -33.222 1   31.745  ? 132 ILE   A H    1 c 2 
ATOM   3630 H HA   . ILE   B 1 120 ? 11.04  21.691  -30.928 1   30.136  ? 132 ILE   A HA   1 c 2 
ATOM   3631 H HB   . ILE   B 1 120 ? 11.667 19.328  -32.342 1   27.835  ? 132 ILE   A HB   1 c 2 
ATOM   3632 H HG12 . ILE   B 1 120 ? 10.499 19.389  -29.747 1   26.298  ? 132 ILE   A HG12 1 c 2 
ATOM   3633 H HG13 . ILE   B 1 120 ? 9.678  19.034  -31.046 1   26.287  ? 132 ILE   A HG13 1 c 2 
ATOM   3634 H HG21 . ILE   B 1 120 ? 13.212 18.995  -30.489 1   27.191  ? 132 ILE   A HG21 1 c 2 
ATOM   3635 H HG22 . ILE   B 1 120 ? 12.929 20.502  -30.084 1   28.444  ? 132 ILE   A HG22 1 c 2 
ATOM   3636 H HG23 . ILE   B 1 120 ? 13.612 20.168  -31.476 1   29.016  ? 132 ILE   A HG23 1 c 2 
ATOM   3637 H HD11 . ILE   B 1 120 ? 11.074 17.096  -31.299 1   24.98   ? 132 ILE   A HD11 1 c 2 
ATOM   3638 H HD12 . ILE   B 1 120 ? 10.118 17.057  -30.026 1   24.218  ? 132 ILE   A HD12 1 c 2 
ATOM   3639 H HD13 . ILE   B 1 120 ? 11.66  17.413  -29.853 1   24.881  ? 132 ILE   A HD13 1 c 2 
ATOM   3640 N N    . GLU   B 1 121 ? 12.643 22.898  -32.159 1   32.4    ? 133 GLU   A N    1 ? 2 
ATOM   3641 C CA   . GLU   B 1 121 ? 13.793 23.49   -32.803 1   35.182  ? 133 GLU   A CA   1 ? 2 
ATOM   3642 C C    . GLU   B 1 121 ? 15.071 23.004  -32.143 1   36.07   ? 133 GLU   A C    1 ? 2 
ATOM   3643 O O    . GLU   B 1 121 ? 15.255 23.218  -30.952 1   40.401  ? 133 GLU   A O    1 ? 2 
ATOM   3644 C CB   . GLU   B 1 121 ? 13.752 25.006  -32.702 1   39.177  ? 133 GLU   A CB   1 ? 2 
ATOM   3645 C CG   . GLU   B 1 121 ? 14.889 25.73   -33.427 1   41.123  ? 133 GLU   A CG   1 ? 2 
ATOM   3646 C CD   . GLU   B 1 121 ? 14.788 27.236  -33.337 1   48.19   ? 133 GLU   A CD   1 ? 2 
ATOM   3647 O OE1  . GLU   B 1 121 ? 14.023 27.785  -32.498 1   50.092  ? 133 GLU   A OE1  1 ? 2 
ATOM   3648 O OE2  . GLU   B 1 121 ? 15.488 27.872  -34.166 1   45.251  ? 133 GLU   A OE2  1 ? 2 
ATOM   3649 H H    . GLU   B 1 121 ? 12.381 23.223  -31.346 1   32.901  ? 133 GLU   A H    1 c 2 
ATOM   3650 H HA   . GLU   B 1 121 ? 13.797 23.228  -33.758 1   35.879  ? 133 GLU   A HA   1 c 2 
ATOM   3651 H HB2  . GLU   B 1 121 ? 12.9   25.32   -33.072 1   39.105  ? 133 GLU   A HB2  1 c 2 
ATOM   3652 H HB3  . GLU   B 1 121 ? 13.774 25.257  -31.755 1   38.576  ? 133 GLU   A HB3  1 c 2 
ATOM   3653 H HG2  . GLU   B 1 121 ? 15.747 25.452  -33.042 1   41.991  ? 133 GLU   A HG2  1 c 2 
ATOM   3654 H HG3  . GLU   B 1 121 ? 14.888 25.47   -34.372 1   42.541  ? 133 GLU   A HG3  1 c 2 
ATOM   3655 N N    . LEU   B 1 122 ? 15.978 22.43   -32.949 1   35.689  ? 134 LEU   A N    1 ? 2 
ATOM   3656 C CA   . LEU   B 1 122 ? 17.283 22.025  -32.432 1   37.425  ? 134 LEU   A CA   1 ? 2 
ATOM   3657 C C    . LEU   B 1 122 ? 18.264 23.19   -32.525 1   41.56   ? 134 LEU   A C    1 ? 2 
ATOM   3658 O O    . LEU   B 1 122 ? 18.773 23.579  -33.584 1   43.903  ? 134 LEU   A O    1 ? 2 
ATOM   3659 C CB   . LEU   B 1 122 ? 17.799 20.771  -33.135 1   38.422  ? 134 LEU   A CB   1 ? 2 
ATOM   3660 C CG   . LEU   B 1 122 ? 19.164 20.225  -32.663 1   36.833  ? 134 LEU   A CG   1 ? 2 
ATOM   3661 C CD1  . LEU   B 1 122 ? 19.229 20.001  -31.21  1   31.613  ? 134 LEU   A CD1  1 ? 2 
ATOM   3662 C CD2  . LEU   B 1 122 ? 19.483 18.927  -33.433 1   38.516  ? 134 LEU   A CD2  1 ? 2 
ATOM   3663 H H    . LEU   B 1 122 ? 15.783 22.286  -33.831 1   36.506  ? 134 LEU   A H    1 c 2 
ATOM   3664 H HA   . LEU   B 1 122 ? 17.166 21.81   -31.472 1   36.711  ? 134 LEU   A HA   1 c 2 
ATOM   3665 H HB2  . LEU   B 1 122 ? 17.126 20.06   -33.024 1   35.987  ? 134 LEU   A HB2  1 c 2 
ATOM   3666 H HB3  . LEU   B 1 122 ? 17.861 20.966  -34.099 1   38.592  ? 134 LEU   A HB3  1 c 2 
ATOM   3667 H HG   . LEU   B 1 122 ? 19.859 20.893  -32.897 1   38.393  ? 134 LEU   A HG   1 c 2 
ATOM   3668 H HD11 . LEU   B 1 122 ? 19.248 20.856  -30.749 1   33.607  ? 134 LEU   A HD11 1 c 2 
ATOM   3669 H HD12 . LEU   B 1 122 ? 20.033 19.499  -30.995 1   33.387  ? 134 LEU   A HD12 1 c 2 
ATOM   3670 H HD13 . LEU   B 1 122 ? 18.448 19.497  -30.924 1   31.276  ? 134 LEU   A HD13 1 c 2 
ATOM   3671 H HD21 . LEU   B 1 122 ? 19.216 19.024  -34.362 1   38.412  ? 134 LEU   A HD21 1 c 2 
ATOM   3672 H HD22 . LEU   B 1 122 ? 18.998 18.185  -33.035 1   36.392  ? 134 LEU   A HD22 1 c 2 
ATOM   3673 H HD23 . LEU   B 1 122 ? 20.438 18.749  -33.389 1   39.034  ? 134 LEU   A HD23 1 c 2 
ATOM   3674 N N    . LEU   B 1 123 ? 18.622 23.741  -31.36  1   42.96   ? 135 LEU   A N    1 ? 2 
ATOM   3675 C CA   . LEU   B 1 123 ? 19.462 24.936  -31.323 1   48.28   ? 135 LEU   A CA   1 ? 2 
ATOM   3676 C C    . LEU   B 1 123 ? 20.93  24.554  -31.447 1   47.939  ? 135 LEU   A C    1 ? 2 
ATOM   3677 O O    . LEU   B 1 123 ? 21.69  25.23   -32.141 1   50.047  ? 135 LEU   A O    1 ? 2 
ATOM   3678 C CB   . LEU   B 1 123 ? 19.201 25.673  -30.012 1   47.186  ? 135 LEU   A CB   1 ? 2 
ATOM   3679 C CG   . LEU   B 1 123 ? 17.753 26.117  -29.806 1   48.431  ? 135 LEU   A CG   1 ? 2 
ATOM   3680 C CD1  . LEU   B 1 123 ? 17.575 26.695  -28.435 1   49.634  ? 135 LEU   A CD1  1 ? 2 
ATOM   3681 C CD2  . LEU   B 1 123 ? 17.371 27.152  -30.865 1   47.542  ? 135 LEU   A CD2  1 ? 2 
ATOM   3682 H H    . LEU   B 1 123 ? 18.342 23.37   -30.573 1   42.026  ? 135 LEU   A H    1 c 2 
ATOM   3683 H HA   . LEU   B 1 123 ? 19.218 25.522  -32.084 1   48.299  ? 135 LEU   A HA   1 c 2 
ATOM   3684 H HB2  . LEU   B 1 123 ? 19.458 25.082  -29.268 1   47.067  ? 135 LEU   A HB2  1 c 2 
ATOM   3685 H HB3  . LEU   B 1 123 ? 19.78  26.47   -29.984 1   50.183  ? 135 LEU   A HB3  1 c 2 
ATOM   3686 H HG   . LEU   B 1 123 ? 17.16  25.327  -29.9   1   45.533  ? 135 LEU   A HG   1 c 2 
ATOM   3687 H HD11 . LEU   B 1 123 ? 18.003 26.117  -27.782 1   48.725  ? 135 LEU   A HD11 1 c 2 
ATOM   3688 H HD12 . LEU   B 1 123 ? 16.627 26.765  -28.233 1   48.643  ? 135 LEU   A HD12 1 c 2 
ATOM   3689 H HD13 . LEU   B 1 123 ? 17.979 27.578  -28.4   1   51.635  ? 135 LEU   A HD13 1 c 2 
ATOM   3690 H HD21 . LEU   B 1 123 ? 17.24  26.71   -31.72  1   47.763  ? 135 LEU   A HD21 1 c 2 
ATOM   3691 H HD22 . LEU   B 1 123 ? 18.081 27.811  -30.948 1   50.495  ? 135 LEU   A HD22 1 c 2 
ATOM   3692 H HD23 . LEU   B 1 123 ? 16.548 27.597  -30.603 1   48.434  ? 135 LEU   A HD23 1 c 2 
ATOM   3693 N N    . ASP   B 1 124 ? 21.301 23.462  -30.754 1   44.257  ? 136 ASP   A N    1 ? 2 
ATOM   3694 C CA   . ASP   B 1 124 ? 22.691 23.069  -30.623 1   47.593  ? 136 ASP   A CA   1 ? 2 
ATOM   3695 C C    . ASP   B 1 124 ? 22.781 21.7    -29.928 1   42.918  ? 136 ASP   A C    1 ? 2 
ATOM   3696 O O    . ASP   B 1 124 ? 21.854 21.283  -29.223 1   42.869  ? 136 ASP   A O    1 ? 2 
ATOM   3697 C CB   . ASP   B 1 124 ? 23.491 24.122  -29.878 1   51.538  ? 136 ASP   A CB   1 ? 2 
ATOM   3698 C CG   . ASP   B 1 124 ? 25.005 24.151  -30.148 1   58.18   ? 136 ASP   A CG   1 ? 2 
ATOM   3699 O OD1  . ASP   B 1 124 ? 25.493 23.367  -30.99  1   55.23   ? 136 ASP   A OD1  1 ? 2 
ATOM   3700 O OD2  . ASP   B 1 124 ? 25.675 24.993  -29.536 1   61.835  ? 136 ASP   A OD2  1 ? 2 
ATOM   3701 H H    . ASP   B 1 124 ? 20.662 22.951  -30.347 1   43.38   ? 136 ASP   A H    1 c 2 
ATOM   3702 H HA   . ASP   B 1 124 ? 23.069 22.984  -31.526 1   47.874  ? 136 ASP   A HA   1 c 2 
ATOM   3703 H HB2  . ASP   B 1 124 ? 23.139 25.011  -30.087 1   52.868  ? 136 ASP   A HB2  1 c 2 
ATOM   3704 H HB3  . ASP   B 1 124 ? 23.366 23.978  -28.916 1   51.403  ? 136 ASP   A HB3  1 c 2 
ATOM   3705 N N    . PHE   B 1 125 ? 23.961 21.064  -30.072 1   44.908  ? 137 PHE   A N    1 ? 2 
ATOM   3706 C CA   . PHE   B 1 125 ? 24.312 19.888  -29.294 1   43.039  ? 137 PHE   A CA   1 ? 2 
ATOM   3707 C C    . PHE   B 1 125 ? 25.833 19.799  -29.176 1   47.428  ? 137 PHE   A C    1 ? 2 
ATOM   3708 O O    . PHE   B 1 125 ? 26.565 20.12   -30.101 1   49.496  ? 137 PHE   A O    1 ? 2 
ATOM   3709 C CB   . PHE   B 1 125 ? 23.717 18.629  -29.927 1   40.947  ? 137 PHE   A CB   1 ? 2 
ATOM   3710 C CG   . PHE   B 1 125 ? 24.057 18.367  -31.391 1   45.64   ? 137 PHE   A CG   1 ? 2 
ATOM   3711 C CD1  . PHE   B 1 125 ? 25.146 17.575  -31.751 1   46.373  ? 137 PHE   A CD1  1 ? 2 
ATOM   3712 C CD2  . PHE   B 1 125 ? 23.273 18.898  -32.419 1   46.464  ? 137 PHE   A CD2  1 ? 2 
ATOM   3713 C CE1  . PHE   B 1 125 ? 25.418 17.269  -33.08  1   45.3    ? 137 PHE   A CE1  1 ? 2 
ATOM   3714 C CE2  . PHE   B 1 125 ? 23.614 18.651  -33.744 1   49.758  ? 137 PHE   A CE2  1 ? 2 
ATOM   3715 C CZ   . PHE   B 1 125 ? 24.62  17.758  -34.062 1   46.977  ? 137 PHE   A CZ   1 ? 2 
ATOM   3716 H H    . PHE   B 1 125 ? 24.562 21.377  -30.686 1   46.202  ? 137 PHE   A H    1 c 2 
ATOM   3717 H HA   . PHE   B 1 125 ? 23.931 19.994  -28.386 1   42.884  ? 137 PHE   A HA   1 c 2 
ATOM   3718 H HB2  . PHE   B 1 125 ? 24.011 17.855  -29.397 1   41.704  ? 137 PHE   A HB2  1 c 2 
ATOM   3719 H HB3  . PHE   B 1 125 ? 22.739 18.679  -29.84  1   40.047  ? 137 PHE   A HB3  1 c 2 
ATOM   3720 H HD1  . PHE   B 1 125 ? 25.659 17.167  -31.071 1   46.644  ? 137 PHE   A HD1  1 c 2 
ATOM   3721 H HD2  . PHE   B 1 125 ? 22.543 19.46   -32.213 1   45.6    ? 137 PHE   A HD2  1 c 2 
ATOM   3722 H HE1  . PHE   B 1 125 ? 26.15  16.713  -33.296 1   47.768  ? 137 PHE   A HE1  1 c 2 
ATOM   3723 H HE2  . PHE   B 1 125 ? 23.061 18.988  -34.432 1   47.986  ? 137 PHE   A HE2  1 c 2 
ATOM   3724 H HZ   . PHE   B 1 125 ? 24.856 17.622  -34.964 1   48.447  ? 137 PHE   A HZ   1 c 2 
ATOM   3725 N N    . LYS   B 1 126 ? 26.318 19.361  -28.029 1   49.614  ? 138 LYS   A N    1 ? 2 
ATOM   3726 C CA   . LYS   B 1 126 ? 27.755 19.31   -27.776 1   52.146  ? 138 LYS   A CA   1 ? 2 
ATOM   3727 C C    . LYS   B 1 126 ? 28.041 17.983  -27.071 1   51.887  ? 138 LYS   A C    1 ? 2 
ATOM   3728 O O    . LYS   B 1 126 ? 27.204 17.48   -26.348 1   48.005  ? 138 LYS   A O    1 ? 2 
ATOM   3729 C CB   . LYS   B 1 126 ? 28.245 20.555  -27.002 1   52.211  ? 138 LYS   A CB   1 ? 2 
ATOM   3730 H H    . LYS   B 1 126 ? 25.744 19.081  -27.374 1   47.696  ? 138 LYS   A H    1 c 2 
ATOM   3731 H HA   . LYS   B 1 126 ? 28.223 19.297  -28.649 1   52.865  ? 138 LYS   A HA   1 c 2 
ATOM   3732 H HB2  . LYS   B 1 126 ? 29.239 20.497  -27.05  0   30      ? 138 LYS   A HB2  1 c 2 
ATOM   3733 H HB3  . LYS   B 1 126 ? 27.486 21.027  -26.732 0   30      ? 138 LYS   A HB3  1 c 2 
ATOM   3734 N N    . GLY   B 1 127 ? 29.282 17.48   -27.211 1   60.417  ? 139 GLY   A N    1 ? 2 
ATOM   3735 C CA   . GLY   B 1 127 ? 29.764 16.291  -26.52  1   63.889  ? 139 GLY   A CA   1 ? 2 
ATOM   3736 C C    . GLY   B 1 127 ? 29.709 16.433  -25.001 1   66.523  ? 139 GLY   A C    1 ? 2 
ATOM   3737 O O    . GLY   B 1 127 ? 29.821 17.544  -24.487 1   62.913  ? 139 GLY   A O    1 ? 2 
ATOM   3738 H H    . GLY   B 1 127 ? 29.859 17.911  -27.773 1   60.944  ? 139 GLY   A H    1 c 2 
ATOM   3739 H HA2  . GLY   B 1 127 ? 29.22  15.518  -26.799 1   62.088  ? 139 GLY   A HA2  1 c 2 
ATOM   3740 H HA3  . GLY   B 1 127 ? 30.691 16.123  -26.797 1   66.058  ? 139 GLY   A HA3  1 c 2 
ATOM   3741 N N    . GLU   B 1 128 ? 29.466 15.298  -24.323 1   69.509  ? 140 GLU   A N    1 ? 2 
ATOM   3742 C CA   . GLU   B 1 128 ? 29.656 15.164  -22.884 1   76.879  ? 140 GLU   A CA   1 ? 2 
ATOM   3743 C C    . GLU   B 1 128 ? 31.133 15.42   -22.474 1   80.668  ? 140 GLU   A C    1 ? 2 
ATOM   3744 O O    . GLU   B 1 128 ? 31.366 15.371  -21.267 1   86.083  ? 140 GLU   A O    1 ? 2 
ATOM   3745 C CB   . GLU   B 1 128 ? 29.178 13.784  -22.405 1   80.051  ? 140 GLU   A CB   1 ? 2 
ATOM   3746 O OXT  . GLU   B 1 128 ? 32.014 15.642  -23.349 1   77.452  ? 140 GLU   A OXT  1 ? 2 
ATOM   3747 H H    . GLU   B 1 128 ? 29.163 14.572  -24.788 1   68.659  ? 140 GLU   A H    1 c 2 
ATOM   3748 H HA   . GLU   B 1 128 ? 29.094 15.848  -22.44  1   75.3    ? 140 GLU   A HA   1 c 2 
ATOM   3749 H HB2  . GLU   B 1 128 ? 29.597 13.398  -21.955 0   30      ? 140 GLU   A HB2  1 c 2 
ATOM   3750 H HB3  . GLU   B 1 128 ? 27.947 14.172  -22.312 0   30      ? 140 GLU   A HB3  1 c 2 
HETATM 3751 C C4   . A1INX C 2 .   ? 15.432 -2.734  -14.549 1   34.134  ? 201 A1INX B C4   1 ? 1 
HETATM 3752 C C14  . A1INX C 2 .   ? 20.348 -3.579  -15.866 1   41.935  ? 201 A1INX B C14  1 ? 1 
HETATM 3753 C C5   . A1INX C 2 .   ? 15.917 -3.901  -15.119 1   35.136  ? 201 A1INX B C5   1 ? 1 
HETATM 3754 C C6   . A1INX C 2 .   ? 16.213 -3.984  -16.477 1   40.025  ? 201 A1INX B C6   1 ? 1 
HETATM 3755 C C11  . A1INX C 2 .   ? 19.199 -6.976  -16.203 1   55.307  ? 201 A1INX B C11  1 ? 1 
HETATM 3756 C C7   . A1INX C 2 .   ? 16.028 -2.887  -17.296 1   42.796  ? 201 A1INX B C7   1 ? 1 
HETATM 3757 C C8   . A1INX C 2 .   ? 17.695 -2.781  -18.933 1   47.039  ? 201 A1INX B C8   1 ? 1 
HETATM 3758 C C9   . A1INX C 2 .   ? 16.855 -6.29   -16.347 1   52.035  ? 201 A1INX B C9   1 ? 1 
HETATM 3759 C C10  . A1INX C 2 .   ? 17.92  -7.142  -16.989 1   50.002  ? 201 A1INX B C10  1 ? 1 
HETATM 3760 C C12  . A1INX C 2 .   ? 20.292 -7.998  -16.569 1   58.134  ? 201 A1INX B C12  1 ? 1 
HETATM 3761 C C13  . A1INX C 2 .   ? 19.683 -4.648  -15.336 1   48.138  ? 201 A1INX B C13  1 ? 1 
HETATM 3762 N N1   . A1INX C 2 .   ? 19.761 -5.616  -16.274 1   53.14   ? 201 A1INX B N1   1 ? 1 
HETATM 3763 N N2   . A1INX C 2 .   ? 20.918 -3.973  -17.043 1   46.424  ? 201 A1INX B N2   1 ? 1 
HETATM 3764 C C3   . A1INX C 2 .   ? 15.275 -1.623  -15.369 1   35.214  ? 201 A1INX B C3   1 ? 1 
HETATM 3765 N N3   . A1INX C 2 .   ? 20.511 -5.196  -17.322 1   51.334  ? 201 A1INX B N3   1 ? 1 
HETATM 3766 C C1   . A1INX C 2 .   ? 14.837 0.52    -17.139 1   37.367  ? 201 A1INX B C1   1 ? 1 
HETATM 3767 O O1   . A1INX C 2 .   ? 15.48  -0.651  -17.609 1   37.877  ? 201 A1INX B O1   1 ? 1 
HETATM 3768 C C2   . A1INX C 2 .   ? 15.585 -1.693  -16.729 1   37.043  ? 201 A1INX B C2   1 ? 1 
HETATM 3769 O O2   . A1INX C 2 .   ? 16.316 -2.962  -18.652 1   46.644  ? 201 A1INX B O2   1 ? 1 
HETATM 3770 O O3   . A1INX C 2 .   ? 16.731 -5.084  -17.113 1   47.343  ? 201 A1INX B O3   1 ? 1 
HETATM 3771 C C15  . A1INX C 2 .   ? 20.539 -2.217  -15.282 1   44.79   ? 201 A1INX B C15  1 ? 1 
HETATM 3772 C C16  . A1INX C 2 .   ? 19.55  -1.217  -15.873 1   37.945  ? 201 A1INX B C16  1 ? 1 
HETATM 3773 C C17  . A1INX C 2 .   ? 20.081 -0.645  -17.198 1   43.272  ? 201 A1INX B C17  1 ? 1 
HETATM 3774 C C18  . A1INX C 2 .   ? 19.208 -0.148  -14.876 1   33.921  ? 201 A1INX B C18  1 ? 1 
HETATM 3775 O O4   . A1INX C 2 .   ? 18.534 -0.69   -13.694 1   33.309  ? 201 A1INX B O4   1 ? 1 
HETATM 3776 C C19  . A1INX C 2 .   ? 18.646 -0.008  -12.554 1   31.127  ? 201 A1INX B C19  1 ? 1 
HETATM 3777 O O5   . A1INX C 2 .   ? 19.28  1.004   -12.442 1   32.645  ? 201 A1INX B O5   1 ? 1 
HETATM 3778 C C20  . A1INX C 2 .   ? 17.912 -0.67   -11.409 1   28.195  ? 201 A1INX B C20  1 ? 1 
HETATM 3779 C C21  . A1INX C 2 .   ? 18.924 -1.107  -10.357 1   30.257  ? 201 A1INX B C21  1 ? 1 
HETATM 3780 C C22  . A1INX C 2 .   ? 19.788 -2.308  -10.815 1   33.714  ? 201 A1INX B C22  1 ? 1 
HETATM 3781 C C23  . A1INX C 2 .   ? 18.867 -3.476  -11.186 1   34.379  ? 201 A1INX B C23  1 ? 1 
HETATM 3782 C C24  . A1INX C 2 .   ? 17.877 -3.08   -12.307 1   30.959  ? 201 A1INX B C24  1 ? 1 
HETATM 3783 N N4   . A1INX C 2 .   ? 17.124 -1.806  -11.979 1   33.522  ? 201 A1INX B N4   1 ? 1 
HETATM 3784 C C25  . A1INX C 2 .   ? 15.888 -1.531  -12.4   1   32.413  ? 201 A1INX B C25  1 ? 1 
HETATM 3785 O O6   . A1INX C 2 .   ? 15.438 -0.351  -12.323 1   32.755  ? 201 A1INX B O6   1 ? 1 
HETATM 3786 C C26  . A1INX C 2 .   ? 15.096 -2.678  -13.052 1   32.178  ? 201 A1INX B C26  1 ? 1 
HETATM 3787 C C27  . A1INX C 2 .   ? 13.584 -2.476  -12.757 1   35.431  ? 201 A1INX B C27  1 ? 1 
HETATM 3788 C C28  . A1INX C 2 .   ? 13.249 -2.641  -11.28  1   32.808  ? 201 A1INX B C28  1 ? 1 
HETATM 3789 C C29  . A1INX C 2 .   ? 11.764 -2.547  -10.948 1   36.101  ? 201 A1INX B C29  1 ? 1 
HETATM 3790 C C30  . A1INX C 2 .   ? 10.923 -3.484  -11.777 1   35.87   ? 201 A1INX B C30  1 ? 1 
HETATM 3791 C C31  . A1INX C 2 .   ? 11.204 -3.313  -13.249 1   40.422  ? 201 A1INX B C31  1 ? 1 
HETATM 3792 C C32  . A1INX C 2 .   ? 12.715 -3.46   -13.586 1   38.506  ? 201 A1INX B C32  1 ? 1 
HETATM 3793 H H5   . A1INX C 2 .   ? 16.028 -4.659  -14.571 1   36.384  ? 201 A1INX B H5   1 c 1 
HETATM 3794 H H13  . A1INX C 2 .   ? 18.968 -7.135  -15.254 1   52.889  ? 201 A1INX B H13  1 c 1 
HETATM 3795 H H7   . A1INX C 2 .   ? 17.838 -2.828  -19.892 1   48.651  ? 201 A1INX B H7   1 c 1 
HETATM 3796 H H8   . A1INX C 2 .   ? 18.212 -3.477  -18.495 1   47.089  ? 201 A1INX B H8   1 c 1 
HETATM 3797 H H6   . A1INX C 2 .   ? 17.98  -1.912  -18.607 1   45.94   ? 201 A1INX B H6   1 c 1 
HETATM 3798 H H9   . A1INX C 2 .   ? 15.998 -6.77   -16.336 1   50.61   ? 201 A1INX B H9   1 c 1 
HETATM 3799 H H10  . A1INX C 2 .   ? 17.106 -6.082  -15.422 1   48.46   ? 201 A1INX B H10  1 c 1 
HETATM 3800 H H12  . A1INX C 2 .   ? 17.646 -8.083  -16.975 1   53.514  ? 201 A1INX B H12  1 c 1 
HETATM 3801 H H11  . A1INX C 2 .   ? 18.064 -6.857  -17.915 1   53.169  ? 201 A1INX B H11  1 c 1 
HETATM 3802 H H15  . A1INX C 2 .   ? 20.508 -7.918  -17.513 1   59.228  ? 201 A1INX B H15  1 c 1 
HETATM 3803 H H16  . A1INX C 2 .   ? 19.97  -8.897  -16.386 1   58.941  ? 201 A1INX B H16  1 c 1 
HETATM 3804 H H14  . A1INX C 2 .   ? 21.088 -7.826  -16.039 1   57.458  ? 201 A1INX B H14  1 c 1 
HETATM 3805 H H17  . A1INX C 2 .   ? 19.178 -4.674  -14.542 1   46.053  ? 201 A1INX B H17  1 c 1 
HETATM 3806 H H4   . A1INX C 2 .   ? 14.95  -0.818  -14.998 1   34.091  ? 201 A1INX B H4   1 c 1 
HETATM 3807 H H2   . A1INX C 2 .   ? 14.745 1.152   -17.87  1   37.884  ? 201 A1INX B H2   1 c 1 
HETATM 3808 H H3   . A1INX C 2 .   ? 15.369 0.921   -16.432 1   35.952  ? 201 A1INX B H3   1 c 1 
HETATM 3809 H H1   . A1INX C 2 .   ? 13.957 0.293   -16.796 1   36.893  ? 201 A1INX B H1   1 c 1 
HETATM 3810 H H18  . A1INX C 2 .   ? 21.453 -1.908  -15.463 1   42.706  ? 201 A1INX B H18  1 c 1 
HETATM 3811 H H19  . A1INX C 2 .   ? 20.415 -2.258  -14.309 1   40.914  ? 201 A1INX B H19  1 c 1 
HETATM 3812 H H20  . A1INX C 2 .   ? 18.714 -1.704  -16.076 1   39.48   ? 201 A1INX B H20  1 c 1 
HETATM 3813 H H23  . A1INX C 2 .   ? 20.919 -0.18   -17.038 1   42.214  ? 201 A1INX B H23  1 c 1 
HETATM 3814 H H21  . A1INX C 2 .   ? 19.43  -0.024  -17.566 1   42.033  ? 201 A1INX B H21  1 c 1 
HETATM 3815 H H22  . A1INX C 2 .   ? 20.228 -1.371  -17.828 1   43.556  ? 201 A1INX B H22  1 c 1 
HETATM 3816 H H25  . A1INX C 2 .   ? 20.032 0.307   -14.603 1   34.416  ? 201 A1INX B H25  1 c 1 
HETATM 3817 H H24  . A1INX C 2 .   ? 18.627 0.515   -15.304 1   34.499  ? 201 A1INX B H24  1 c 1 
HETATM 3818 H H26  . A1INX C 2 .   ? 17.283 -0.013  -11.008 1   28.943  ? 201 A1INX B H26  1 c 1 
HETATM 3819 H H28  . A1INX C 2 .   ? 19.517 -0.346  -10.141 1   29.778  ? 201 A1INX B H28  1 c 1 
HETATM 3820 H H27  . A1INX C 2 .   ? 18.441 -1.354  -9.534  1   29.583  ? 201 A1INX B H27  1 c 1 
HETATM 3821 H H29  . A1INX C 2 .   ? 20.396 -2.579  -10.089 1   33.171  ? 201 A1INX B H29  1 c 1 
HETATM 3822 H H30  . A1INX C 2 .   ? 20.334 -2.052  -11.594 1   33.908  ? 201 A1INX B H30  1 c 1 
HETATM 3823 H H31  . A1INX C 2 .   ? 18.364 -3.76   -10.393 1   33.06   ? 201 A1INX B H31  1 c 1 
HETATM 3824 H H32  . A1INX C 2 .   ? 19.411 -4.235  -11.487 1   34.679  ? 201 A1INX B H32  1 c 1 
HETATM 3825 H H33  . A1INX C 2 .   ? 17.238 -3.815  -12.44  1   33.336  ? 201 A1INX B H33  1 c 1 
HETATM 3826 H H34  . A1INX C 2 .   ? 18.373 -2.957  -13.148 1   33.493  ? 201 A1INX B H34  1 c 1 
HETATM 3827 H H35  . A1INX C 2 .   ? 15.386 -3.534  -12.644 1   33.523  ? 201 A1INX B H35  1 c 1 
HETATM 3828 H H36  . A1INX C 2 .   ? 13.338 -1.553  -13.025 1   34.28   ? 201 A1INX B H36  1 c 1 
HETATM 3829 H H38  . A1INX C 2 .   ? 13.582 -3.511  -10.979 1   34.305  ? 201 A1INX B H38  1 c 1 
HETATM 3830 H H37  . A1INX C 2 .   ? 13.725 -1.954  -10.771 1   32.689  ? 201 A1INX B H37  1 c 1 
HETATM 3831 H H39  . A1INX C 2 .   ? 11.459 -1.624  -11.097 1   34.353  ? 201 A1INX B H39  1 c 1 
HETATM 3832 H H40  . A1INX C 2 .   ? 11.634 -2.755  -9.996  1   34.467  ? 201 A1INX B H40  1 c 1 
HETATM 3833 H H41  . A1INX C 2 .   ? 9.972  -3.308  -11.604 1   37.539  ? 201 A1INX B H41  1 c 1 
HETATM 3834 H H42  . A1INX C 2 .   ? 11.113 -4.411  -11.514 1   37.85   ? 201 A1INX B H42  1 c 1 
HETATM 3835 H H43  . A1INX C 2 .   ? 10.894 -2.426  -13.536 1   38.903  ? 201 A1INX B H43  1 c 1 
HETATM 3836 H H44  . A1INX C 2 .   ? 10.696 -3.987  -13.754 1   40.746  ? 201 A1INX B H44  1 c 1 
HETATM 3837 H H46  . A1INX C 2 .   ? 13     -4.377  -13.404 1   39.243  ? 201 A1INX B H46  1 c 1 
HETATM 3838 H H45  . A1INX C 2 .   ? 12.848 -3.287  -14.54  1   39.357  ? 201 A1INX B H45  1 c 1 
HETATM 3839 C C4   . A1INX D 2 .   ? 5.964  17.737  -19.867 1   27.443  ? 201 A1INX A C4   1 ? 2 
HETATM 3840 C C14  . A1INX D 2 .   ? 10.613 18.677  -18.33  1   39.695  ? 201 A1INX A C14  1 ? 2 
HETATM 3841 C C5   . A1INX D 2 .   ? 6.444  18.91   -19.279 1   30.193  ? 201 A1INX A C5   1 ? 2 
HETATM 3842 C C6   . A1INX D 2 .   ? 6.652  18.971  -17.918 1   35.565  ? 201 A1INX A C6   1 ? 2 
HETATM 3843 C C11  . A1INX D 2 .   ? 9.626  22.112  -17.915 1   43.508  ? 201 A1INX A C11  1 ? 2 
HETATM 3844 C C7   . A1INX D 2 .   ? 6.32   17.886  -17.107 1   36.967  ? 201 A1INX A C7   1 ? 2 
HETATM 3845 C C8   . A1INX D 2 .   ? 7.839  17.874  -15.314 1   36.604  ? 201 A1INX A C8   1 ? 2 
HETATM 3846 C C9   . A1INX D 2 .   ? 7.091  21.387  -17.78  1   41.739  ? 201 A1INX A C9   1 ? 2 
HETATM 3847 C C10  . A1INX D 2 .   ? 8.219  22.24   -17.246 1   42.768  ? 201 A1INX A C10  1 ? 2 
HETATM 3848 C C12  . A1INX D 2 .   ? 10.619 23.064  -17.209 1   45.057  ? 201 A1INX A C12  1 ? 2 
HETATM 3849 C C13  . A1INX D 2 .   ? 10.149 19.836  -18.895 1   39.448  ? 201 A1INX A C13  1 ? 2 
HETATM 3850 N N1   . A1INX D 2 .   ? 10.131 20.729  -17.914 1   39.586  ? 201 A1INX A N1   1 ? 2 
HETATM 3851 N N2   . A1INX D 2 .   ? 10.84  18.898  -17.02  1   41.317  ? 201 A1INX A N2   1 ? 2 
HETATM 3852 C C3   . A1INX D 2 .   ? 5.627  16.645  -19.077 1   29.901  ? 201 A1INX A C3   1 ? 2 
HETATM 3853 N N3   . A1INX D 2 .   ? 10.545 20.146  -16.768 1   41.665  ? 201 A1INX A N3   1 ? 2 
HETATM 3854 C C1   . A1INX D 2 .   ? 5.258  14.455  -17.339 1   31.874  ? 201 A1INX A C1   1 ? 2 
HETATM 3855 O O1   . A1INX D 2 .   ? 5.567  15.706  -16.809 1   31.452  ? 201 A1INX A O1   1 ? 2 
HETATM 3856 C C2   . A1INX D 2 .   ? 5.863  16.706  -17.69  1   34.309  ? 201 A1INX A C2   1 ? 2 
HETATM 3857 O O2   . A1INX D 2 .   ? 6.481  17.997  -15.725 1   37.339  ? 201 A1INX A O2   1 ? 2 
HETATM 3858 O O3   . A1INX D 2 .   ? 7.193  20.05   -17.247 1   38.494  ? 201 A1INX A O3   1 ? 2 
HETATM 3859 C C15  . A1INX D 2 .   ? 10.86  17.339  -18.913 1   33.715  ? 201 A1INX A C15  1 ? 2 
HETATM 3860 C C16  . A1INX D 2 .   ? 9.933  16.275  -18.327 1   34.345  ? 201 A1INX A C16  1 ? 2 
HETATM 3861 C C17  . A1INX D 2 .   ? 10.551 15.707  -17.022 1   38.262  ? 201 A1INX A C17  1 ? 2 
HETATM 3862 C C18  . A1INX D 2 .   ? 9.739  15.185  -19.37  1   32.941  ? 201 A1INX A C18  1 ? 2 
HETATM 3863 O O4   . A1INX D 2 .   ? 9.074  15.696  -20.536 1   28.81   ? 201 A1INX A O4   1 ? 2 
HETATM 3864 C C19  . A1INX D 2 .   ? 9.221  14.994  -21.653 1   28.652  ? 201 A1INX A C19  1 ? 2 
HETATM 3865 O O5   . A1INX D 2 .   ? 9.817  13.973  -21.716 1   27.795  ? 201 A1INX A O5   1 ? 2 
HETATM 3866 C C20  . A1INX D 2 .   ? 8.572  15.669  -22.853 1   25.94   ? 201 A1INX A C20  1 ? 2 
HETATM 3867 C C21  . A1INX D 2 .   ? 9.658  16.053  -23.833 1   24.708  ? 201 A1INX A C21  1 ? 2 
HETATM 3868 C C22  . A1INX D 2 .   ? 10.524 17.153  -23.372 1   26.282  ? 201 A1INX A C22  1 ? 2 
HETATM 3869 C C23  . A1INX D 2 .   ? 9.675  18.395  -23.063 1   24.938  ? 201 A1INX A C23  1 ? 2 
HETATM 3870 C C24  . A1INX D 2 .   ? 8.531  18.037  -22.12  1   25.658  ? 201 A1INX A C24  1 ? 2 
HETATM 3871 N N4   . A1INX D 2 .   ? 7.789  16.84   -22.431 1   25.973  ? 201 A1INX A N4   1 ? 2 
HETATM 3872 C C25  . A1INX D 2 .   ? 6.533  16.598  -21.977 1   24.915  ? 201 A1INX A C25  1 ? 2 
HETATM 3873 O O6   . A1INX D 2 .   ? 6.061  15.455  -21.939 1   25.804  ? 201 A1INX A O6   1 ? 2 
HETATM 3874 C C26  . A1INX D 2 .   ? 5.728  17.716  -21.378 1   26.336  ? 201 A1INX A C26  1 ? 2 
HETATM 3875 C C27  . A1INX D 2 .   ? 4.219  17.64   -21.658 1   25.138  ? 201 A1INX A C27  1 ? 2 
HETATM 3876 C C28  . A1INX D 2 .   ? 3.904  17.703  -23.152 1   23.967  ? 201 A1INX A C28  1 ? 2 
HETATM 3877 C C29  . A1INX D 2 .   ? 2.44   17.717  -23.491 1   26.091  ? 201 A1INX A C29  1 ? 2 
HETATM 3878 C C30  . A1INX D 2 .   ? 1.609  18.721  -22.73  1   28.377  ? 201 A1INX A C30  1 ? 2 
HETATM 3879 C C31  . A1INX D 2 .   ? 1.972  18.636  -21.271 1   31.255  ? 201 A1INX A C31  1 ? 2 
HETATM 3880 C C32  . A1INX D 2 .   ? 3.448  18.754  -20.991 1   28.012  ? 201 A1INX A C32  1 ? 2 
HETATM 3881 H H5   . A1INX D 2 .   ? 6.677  19.642  -19.827 1   30.805  ? 201 A1INX A H5   1 c 2 
HETATM 3882 H H13  . A1INX D 2 .   ? 9.537  22.405  -18.855 1   41.648  ? 201 A1INX A H13  1 c 2 
HETATM 3883 H H7   . A1INX D 2 .   ? 7.879  17.843  -14.344 1   38.822  ? 201 A1INX A H7   1 c 2 
HETATM 3884 H H8   . A1INX D 2 .   ? 8.348  18.636  -15.633 1   37.062  ? 201 A1INX A H8   1 c 2 
HETATM 3885 H H6   . A1INX D 2 .   ? 8.214  17.057  -15.679 1   35.875  ? 201 A1INX A H6   1 c 2 
HETATM 3886 H H9   . A1INX D 2 .   ? 6.228  21.779  -17.523 1   41.951  ? 201 A1INX A H9   1 c 2 
HETATM 3887 H H10  . A1INX D 2 .   ? 7.135  21.362  -18.76  1   39.461  ? 201 A1INX A H10  1 c 2 
HETATM 3888 H H12  . A1INX D 2 .   ? 7.944  23.179  -17.306 1   44.578  ? 201 A1INX A H12  1 c 2 
HETATM 3889 H H11  . A1INX D 2 .   ? 8.323  22.043  -16.292 1   44.586  ? 201 A1INX A H11  1 c 2 
HETATM 3890 H H15  . A1INX D 2 .   ? 10.628 22.876  -16.256 1   46.603  ? 201 A1INX A H15  1 c 2 
HETATM 3891 H H16  . A1INX D 2 .   ? 10.344 23.985  -17.354 1   46.443  ? 201 A1INX A H16  1 c 2 
HETATM 3892 H H14  . A1INX D 2 .   ? 11.511 22.931  -17.573 1   44.91   ? 201 A1INX A H14  1 c 2 
HETATM 3893 H H17  . A1INX D 2 .   ? 9.877  19.973  -19.787 1   37.969  ? 201 A1INX A H17  1 c 2 
HETATM 3894 H H4   . A1INX D 2 .   ? 5.282  15.861  -19.475 1   29.094  ? 201 A1INX A H4   1 c 2 
HETATM 3895 H H2   . A1INX D 2 .   ? 5.156  13.816  -16.615 1   32.422  ? 201 A1INX A H2   1 c 2 
HETATM 3896 H H3   . A1INX D 2 .   ? 5.974  14.165  -17.926 1   30.277  ? 201 A1INX A H3   1 c 2 
HETATM 3897 H H1   . A1INX D 2 .   ? 4.428  14.51   -17.839 1   30.92   ? 201 A1INX A H1   1 c 2 
HETATM 3898 H H18  . A1INX D 2 .   ? 11.792 17.079  -18.746 1   35.284  ? 201 A1INX A H18  1 c 2 
HETATM 3899 H H19  . A1INX D 2 .   ? 10.728 17.381  -19.884 1   33.527  ? 201 A1INX A H19  1 c 2 
HETATM 3900 H H20  . A1INX D 2 .   ? 9.055  16.685  -18.13  1   34.963  ? 201 A1INX A H20  1 c 2 
HETATM 3901 H H23  . A1INX D 2 .   ? 11.52  15.708  -17.092 1   37.937  ? 201 A1INX A H23  1 c 2 
HETATM 3902 H H21  . A1INX D 2 .   ? 10.239 14.797  -16.888 1   37.532  ? 201 A1INX A H21  1 c 2 
HETATM 3903 H H22  . A1INX D 2 .   ? 10.281 16.257  -16.268 1   39.026  ? 201 A1INX A H22  1 c 2 
HETATM 3904 H H25  . A1INX D 2 .   ? 10.615 14.822  -19.62  1   31.966  ? 201 A1INX A H25  1 c 2 
HETATM 3905 H H24  . A1INX D 2 .   ? 9.209  14.457  -18.983 1   32.324  ? 201 A1INX A H24  1 c 2 
HETATM 3906 H H26  . A1INX D 2 .   ? 7.957  15.02   -23.288 1   25.314  ? 201 A1INX A H26  1 c 2 
HETATM 3907 H H28  . A1INX D 2 .   ? 10.22  15.261  -24.018 1   24.732  ? 201 A1INX A H28  1 c 2 
HETATM 3908 H H27  . A1INX D 2 .   ? 9.234  16.32   -24.681 1   24.638  ? 201 A1INX A H27  1 c 2 
HETATM 3909 H H29  . A1INX D 2 .   ? 11.185 17.369  -24.069 1   25.601  ? 201 A1INX A H29  1 c 2 
HETATM 3910 H H30  . A1INX D 2 .   ? 11.013 16.876  -22.563 1   26.261  ? 201 A1INX A H30  1 c 2 
HETATM 3911 H H31  . A1INX D 2 .   ? 9.31   18.76   -23.897 1   25.229  ? 201 A1INX A H31  1 c 2 
HETATM 3912 H H32  . A1INX D 2 .   ? 10.238 19.082  -22.648 1   26.545  ? 201 A1INX A H32  1 c 2 
HETATM 3913 H H33  . A1INX D 2 .   ? 7.906  18.796  -22.107 1   26.513  ? 201 A1INX A H33  1 c 2 
HETATM 3914 H H34  . A1INX D 2 .   ? 8.895  17.95   -21.211 1   26.719  ? 201 A1INX A H34  1 c 2 
HETATM 3915 H H35  . A1INX D 2 .   ? 6.069  18.572  -21.744 1   26.295  ? 201 A1INX A H35  1 c 2 
HETATM 3916 H H36  . A1INX D 2 .   ? 3.879  16.776  -21.307 1   25.43   ? 201 A1INX A H36  1 c 2 
HETATM 3917 H H38  . A1INX D 2 .   ? 4.318  18.508  -23.526 1   24.579  ? 201 A1INX A H38  1 c 2 
HETATM 3918 H H37  . A1INX D 2 .   ? 4.317  16.932  -23.593 1   23.338  ? 201 A1INX A H37  1 c 2 
HETATM 3919 H H39  . A1INX D 2 .   ? 2.074  16.82   -23.325 1   25.51   ? 201 A1INX A H39  1 c 2 
HETATM 3920 H H40  . A1INX D 2 .   ? 2.345  17.898  -24.452 1   25.506  ? 201 A1INX A H40  1 c 2 
HETATM 3921 H H41  . A1INX D 2 .   ? 0.655  18.524  -22.849 1   29.295  ? 201 A1INX A H41  1 c 2 
HETATM 3922 H H42  . A1INX D 2 .   ? 1.787  19.626  -23.067 1   29.3    ? 201 A1INX A H42  1 c 2 
HETATM 3923 H H43  . A1INX D 2 .   ? 1.65   17.78   -20.915 1   30.035  ? 201 A1INX A H43  1 c 2 
HETATM 3924 H H44  . A1INX D 2 .   ? 1.502  19.352  -20.787 1   31.658  ? 201 A1INX A H44  1 c 2 
HETATM 3925 H H46  . A1INX D 2 .   ? 3.773  19.616  -21.319 1   28.745  ? 201 A1INX A H46  1 c 2 
HETATM 3926 H H45  . A1INX D 2 .   ? 3.595  18.722  -20.024 1   29.257  ? 201 A1INX A H45  1 c 2 
HETATM 3927 O O    . HOH   E 3 .   ? 3.006  -6.098  -10.97  1   62.337  ? 301 HOH   B O    1 ? ? 
HETATM 3928 O O    . HOH   E 3 .   ? 25.06  -1.25   6.495   1   36.808  ? 302 HOH   B O    1 ? ? 
HETATM 3929 O O    . HOH   E 3 .   ? 30.93  3.98    0.908   1   45.251  ? 303 HOH   B O    1 ? ? 
HETATM 3930 O O    . HOH   E 3 .   ? 13.776 16.872  5.864   1   48.829  ? 304 HOH   B O    1 ? ? 
HETATM 3931 O O    . HOH   E 3 .   ? 10.714 -4.2    4.369   1   46.155  ? 305 HOH   B O    1 ? ? 
HETATM 3932 O O    . HOH   E 3 .   ? 13.738 12.284  6.381   1   30.753  ? 306 HOH   B O    1 ? ? 
HETATM 3933 O O    . HOH   E 3 .   ? 12.107 12.784  -4.125  1   38.057  ? 307 HOH   B O    1 ? ? 
HETATM 3934 O O    . HOH   E 3 .   ? 9.367  6.815   -13.211 1   28.08   ? 308 HOH   B O    1 ? ? 
HETATM 3935 O O    . HOH   E 3 .   ? 25.287 6.734   0.574   1   28.281  ? 309 HOH   B O    1 ? ? 
HETATM 3936 O O    . HOH   E 3 .   ? 23.639 8.208   2.369   1   37.538  ? 310 HOH   B O    1 ? ? 
HETATM 3937 O O    . HOH   E 3 .   ? 10.91  5.682   -11.167 1   26.607  ? 311 HOH   B O    1 ? ? 
HETATM 3938 O O    . HOH   E 3 .   ? 8.155  12.065  -5.492  1   32.173  ? 312 HOH   B O    1 ? ? 
HETATM 3939 O O    . HOH   E 3 .   ? 4.96   3.744   -8.274  1   42.622  ? 313 HOH   B O    1 ? ? 
HETATM 3940 O O    . HOH   E 3 .   ? 7.179  7.464   -3.172  1   32.861  ? 314 HOH   B O    1 ? ? 
HETATM 3941 O O    . HOH   E 3 .   ? 25.229 -4.78   7.585   1   38.781  ? 315 HOH   B O    1 ? ? 
HETATM 3942 O O    . HOH   E 3 .   ? 19.67  13.875  -1.565  1   30.252  ? 316 HOH   B O    1 ? ? 
HETATM 3943 O O    . HOH   E 3 .   ? 6.798  7.515   -19.801 1   31.661  ? 317 HOH   B O    1 ? ? 
HETATM 3944 O O    . HOH   E 3 .   ? 10.416 5.84    7.672   1   32.346  ? 318 HOH   B O    1 ? ? 
HETATM 3945 O O    . HOH   E 3 .   ? 13.286 -11.733 -13.107 1   48.408  ? 319 HOH   B O    1 ? ? 
HETATM 3946 O O    . HOH   E 3 .   ? 18.294 7.753   -11.089 1   26.778  ? 320 HOH   B O    1 ? ? 
HETATM 3947 O O    . HOH   E 3 .   ? 22.334 1.18    6.938   1   38.82   ? 321 HOH   B O    1 ? ? 
HETATM 3948 O O    . HOH   E 3 .   ? 11.128 6.693   -0.655  1   30.851  ? 322 HOH   B O    1 ? ? 
HETATM 3949 O O    . HOH   E 3 .   ? 16.012 4.751   -18.588 1   37.968  ? 323 HOH   B O    1 ? ? 
HETATM 3950 O O    . HOH   E 3 .   ? 6.839  5.937   0.85    1   35.427  ? 324 HOH   B O    1 ? ? 
HETATM 3951 O O    . HOH   E 3 .   ? 21.529 11.606  -1.232  1   43.868  ? 325 HOH   B O    1 ? ? 
HETATM 3952 O O    . HOH   E 3 .   ? 27.001 3.514   -11.13  1   41.633  ? 326 HOH   B O    1 ? ? 
HETATM 3953 O O    . HOH   E 3 .   ? 11.621 13.916  -13.221 1   36.607  ? 327 HOH   B O    1 ? ? 
HETATM 3954 O O    . HOH   E 3 .   ? 21.395 -15.16  1.01    1   38.397  ? 328 HOH   B O    1 ? ? 
HETATM 3955 O O    . HOH   E 3 .   ? 27.055 2.043   6.504   1   44.754  ? 329 HOH   B O    1 ? ? 
HETATM 3956 O O    . HOH   E 3 .   ? 12.176 10.184  7.276   1   33.874  ? 330 HOH   B O    1 ? ? 
HETATM 3957 O O    . HOH   E 3 .   ? 9.615  6.263   -20.928 1   29.455  ? 331 HOH   B O    1 ? ? 
HETATM 3958 O O    . HOH   E 3 .   ? 13.026 3.325   -22.012 1   37.964  ? 332 HOH   B O    1 ? ? 
HETATM 3959 O O    . HOH   E 3 .   ? 17.801 -0.582  9.24    1   36.891  ? 333 HOH   B O    1 ? ? 
HETATM 3960 O O    . HOH   E 3 .   ? 21.47  -10.521 -13.328 1   50.165  ? 334 HOH   B O    1 ? ? 
HETATM 3961 O O    . HOH   E 3 .   ? 6.903  8.139   2.34    1   40.302  ? 335 HOH   B O    1 ? ? 
HETATM 3962 O O    . HOH   E 3 .   ? 20.831 8.883   7.495   1   46.278  ? 336 HOH   B O    1 ? ? 
HETATM 3963 O O    . HOH   E 3 .   ? 12.423 12.397  -15.712 1   40.118  ? 337 HOH   B O    1 ? ? 
HETATM 3964 O O    . HOH   E 3 .   ? 13.077 8.188   8.48    1   34.699  ? 338 HOH   B O    1 ? ? 
HETATM 3965 O O    . HOH   E 3 .   ? 7.545  7.169   8.59    1   40.907  ? 339 HOH   B O    1 ? ? 
HETATM 3966 O O    . HOH   E 3 .   ? 3.389  -2.862  1.076   1   40.795  ? 340 HOH   B O    1 ? ? 
HETATM 3967 O O    . HOH   E 3 .   ? 7.561  10.626  2.127   1   38.762  ? 341 HOH   B O    1 ? ? 
HETATM 3968 O O    . HOH   E 3 .   ? 10.691 16.36   -13.266 1   43.661  ? 342 HOH   B O    1 ? ? 
HETATM 3969 O O    . HOH   E 3 .   ? 10.677 14.304  -2.369  1   38.739  ? 343 HOH   B O    1 ? ? 
HETATM 3970 O O    . HOH   E 3 .   ? 7.333  9.517   8.032   1   47.926  ? 344 HOH   B O    1 ? ? 
HETATM 3971 O O    . HOH   E 3 .   ? 18.1   -10.781 -2.841  1   52.811  ? 345 HOH   B O    1 ? ? 
HETATM 3972 O O    . HOH   E 3 .   ? 8.335  13.964  -3.33   1   40.796  ? 346 HOH   B O    1 ? ? 
HETATM 3973 O O    . HOH   E 3 .   ? 20.137 3.736   -15.447 1   51.237  ? 347 HOH   B O    1 ? ? 
HETATM 3974 O O    . HOH   E 3 .   ? 8.352  -2.200  15.810  1   45.806  ? 348 HOH   B O    1 ? ? 
HETATM 3975 O O    . HOH   E 3 .   ? 8.502  6.369   -0.884  1   33.831  ? 349 HOH   B O    1 ? ? 
HETATM 3976 O O    . HOH   F 3 .   ? 17.334 15.877  -40.116 1   40.121  ? 301 HOH   A O    1 ? ? 
HETATM 3977 O O    . HOH   F 3 .   ? 27.478 14.542  -31.988 1   47.902  ? 302 HOH   A O    1 ? ? 
HETATM 3978 O O    . HOH   F 3 .   ? 1.87   1.634   -33.17  1   41.884  ? 303 HOH   A O    1 ? ? 
HETATM 3979 O O    . HOH   F 3 .   ? -1.899 9.875   -36.375 1   37.811  ? 304 HOH   A O    1 ? ? 
HETATM 3980 O O    . HOH   F 3 .   ? 29.68  13.562  -29.16  1   34.464  ? 305 HOH   A O    1 ? ? 
HETATM 3981 O O    . HOH   F 3 .   ? 5.942  20.324  -14.747 1   48.741  ? 306 HOH   A O    1 ? ? 
HETATM 3982 O O    . HOH   F 3 .   ? 5.887  28.185  -33.916 1   40.643  ? 307 HOH   A O    1 ? ? 
HETATM 3983 O O    . HOH   F 3 .   ? 16.682 17.7    -19.043 1   43.36   ? 308 HOH   A O    1 ? ? 
HETATM 3984 O O    . HOH   F 3 .   ? 12.939 26.501  -20.837 1   42.901  ? 309 HOH   A O    1 ? ? 
HETATM 3985 O O    . HOH   F 3 .   ? 14.9   6.449   -24.488 1   40.943  ? 310 HOH   A O    1 ? ? 
HETATM 3986 O O    . HOH   F 3 .   ? -4.088 8.53    -28.001 1   34.424  ? 311 HOH   A O    1 ? ? 
HETATM 3987 O O    . HOH   F 3 .   ? 5.282  3.153   -41.236 1   39.3    ? 312 HOH   A O    1 ? ? 
HETATM 3988 O O    . HOH   F 3 .   ? 12.065 7.788   -21.04  1   26.939  ? 313 HOH   A O    1 ? ? 
HETATM 3989 O O    . HOH   F 3 .   ? 13.183 -0.539  -39.657 1   45.807  ? 314 HOH   A O    1 ? ? 
HETATM 3990 O O    . HOH   F 3 .   ? 1.116  11.786  -9.816  1   41.158  ? 315 HOH   A O    1 ? ? 
HETATM 3991 O O    . HOH   F 3 .   ? 2.762  19.593  -39.296 1   42.686  ? 316 HOH   A O    1 ? ? 
HETATM 3992 O O    . HOH   F 3 .   ? 17.467 11.318  -22.577 1   29.098  ? 317 HOH   A O    1 ? ? 
HETATM 3993 O O    . HOH   F 3 .   ? -7.452 8.411   -21.546 1   49.987  ? 318 HOH   A O    1 ? ? 
HETATM 3994 O O    . HOH   F 3 .   ? 2.855  0.805   -38.816 1   54.907  ? 319 HOH   A O    1 ? ? 
HETATM 3995 O O    . HOH   F 3 .   ? 4.606  26.681  -20.972 1   41.67   ? 320 HOH   A O    1 ? ? 
HETATM 3996 O O    . HOH   F 3 .   ? 14.926 7.212   -36.404 1   44.04   ? 321 HOH   A O    1 ? ? 
HETATM 3997 O O    . HOH   F 3 .   ? 2.185  9.628   -42.3   1   37.274  ? 322 HOH   A O    1 ? ? 
HETATM 3998 O O    . HOH   F 3 .   ? 2.522  8.886   -34.139 1   31.237  ? 323 HOH   A O    1 ? ? 
HETATM 3999 O O    . HOH   F 3 .   ? 4.832  16.469  -14.2   1   45.755  ? 324 HOH   A O    1 ? ? 
HETATM 4000 O O    . HOH   F 3 .   ? -0.319 8.306   -21.799 1   29.8    ? 325 HOH   A O    1 ? ? 
HETATM 4001 O O    . HOH   F 3 .   ? 3.182  14.282  -14.063 1   40.965  ? 326 HOH   A O    1 ? ? 
HETATM 4002 O O    . HOH   F 3 .   ? 1.339  9.357   -23.572 1   28.828  ? 327 HOH   A O    1 ? ? 
HETATM 4003 O O    . HOH   F 3 .   ? 4.458  6.433   -18.195 1   36.753  ? 328 HOH   A O    1 ? ? 
HETATM 4004 O O    . HOH   F 3 .   ? -7.403 5.117   -21.777 1   37.05   ? 329 HOH   A O    1 ? ? 
HETATM 4005 O O    . HOH   F 3 .   ? 7.31   13.925  -44.351 1   55.461  ? 330 HOH   A O    1 ? ? 
HETATM 4006 O O    . HOH   F 3 .   ? -4.714 18.904  -36.498 1   42.071  ? 331 HOH   A O    1 ? ? 
HETATM 4007 O O    . HOH   F 3 .   ? -2.225 8.283   -32.006 1   35.361  ? 332 HOH   A O    1 ? ? 
HETATM 4008 O O    . HOH   F 3 .   ? 16.433 7.935   -34.311 1   36.392  ? 333 HOH   A O    1 ? ? 
HETATM 4009 O O    . HOH   F 3 .   ? 8.539  6.965   -23.243 1   28.354  ? 334 HOH   A O    1 ? ? 
HETATM 4010 O O    . HOH   F 3 .   ? 6.198  1.377   -24.288 1   38.692  ? 335 HOH   A O    1 ? ? 
HETATM 4011 O O    . HOH   F 3 .   ? 16.558 22.8    -19.318 1   36.667  ? 336 HOH   A O    1 ? ? 
HETATM 4012 O O    . HOH   F 3 .   ? 2.717  2.743   -30.959 1   36.223  ? 337 HOH   A O    1 ? ? 
HETATM 4013 O O    . HOH   F 3 .   ? 10.601 1.033   -32.775 1   39.163  ? 338 HOH   A O    1 ? ? 
HETATM 4014 O O    . HOH   F 3 .   ? -3.963 24.017  -24.383 1   57.715  ? 339 HOH   A O    1 ? ? 
HETATM 4015 O O    . HOH   F 3 .   ? 12.743 3.344   -32.918 1   41.391  ? 340 HOH   A O    1 ? ? 
HETATM 4016 O O    . HOH   F 3 .   ? 9.859  21.191  -14.029 1   47.491  ? 341 HOH   A O    1 ? ? 
HETATM 4017 O O    . HOH   F 3 .   ? 0.883  15.025  -13.051 1   33.062  ? 342 HOH   A O    1 ? ? 
HETATM 4018 O O    . HOH   F 3 .   ? 1.795  13.748  -10.455 1   40.388  ? 343 HOH   A O    1 ? ? 
HETATM 4019 O O    . HOH   F 3 .   ? -1.286 5.654   -37.403 1   35.526  ? 344 HOH   A O    1 ? ? 
HETATM 4020 O O    . HOH   F 3 .   ? -4.66  12.019  -26.713 1   41.042  ? 345 HOH   A O    1 ? ? 
HETATM 4021 O O    . HOH   F 3 .   ? -6.467 9.053   -17.673 1   42.984  ? 346 HOH   A O    1 ? ? 
HETATM 4022 O O    . HOH   F 3 .   ? 4.014  5.32    -42.276 1   34.953  ? 347 HOH   A O    1 ? ? 
HETATM 4023 O O    . HOH   F 3 .   ? 8.83   26.125  -31.092 1   48.798  ? 348 HOH   A O    1 ? ? 
HETATM 4024 O O    . HOH   F 3 .   ? -1.08  1.871   -32.74  0.5 43.564  ? 349 HOH   A O    1 ? ? 
HETATM 4025 O O    . HOH   F 3 .   ? -4.327 0.228   -21.76  1   42.346  ? 350 HOH   A O    1 ? ? 
HETATM 4026 O O    . HOH   F 3 .   ? 8.023  29.179  -34.506 1   42.947  ? 351 HOH   A O    1 ? ? 
HETATM 4027 O O    . HOH   F 3 .   ? 12.372 32.266  -38.456 1   42.319  ? 352 HOH   A O    1 ? ? 
HETATM 4028 O O    . HOH   F 3 .   ? 2.904  1.157   -22.573 1   44.849  ? 353 HOH   A O    1 ? ? 
HETATM 4029 O O    . HOH   F 3 .   ? 10.129 30.408  -32.886 1   43.176  ? 354 HOH   A O    1 ? ? 
HETATM 4030 O O    . HOH   F 3 .   ? 12.818 5.848   -22.714 1   42.449  ? 355 HOH   A O    1 ? ? 
HETATM 4031 O O    . HOH   F 3 .   ? 0.76   17.316  -12.07  1   54.541  ? 356 HOH   A O    1 ? ? 
HETATM 4032 O O    . HOH   F 3 .   ? -4.137 5.827   -29.21  1   46.299  ? 357 HOH   A O    1 ? ? 
HETATM 4033 O O    . HOH   F 3 .   ? -2.497 5.737   -31.402 1   36.538  ? 358 HOH   A O    1 ? ? 
HETATM 4034 O O    . HOH   F 3 .   ? -0.437 8.99    -34.248 1   38.063  ? 359 HOH   A O    1 ? ? 
HETATM 4035 O O    . HOH   F 3 .   ? 3.793  17.952  -10.878 1   49.82   ? 360 HOH   A O    1 ? ? 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N    . GLY   A 1   ? 0.520479 0.692325 0.69601  -0.177611   0.0529917   0.110449    13  GLY   B N    
2    C CA   . GLY   A 1   ? 0.541571 0.647908 0.690248 -0.179842   0.0463404   0.116043    13  GLY   B CA   
3    C C    . GLY   A 1   ? 0.578332 0.66251  0.69142  -0.150441   0.0386569   0.109446    13  GLY   B C    
4    O O    . GLY   A 1   ? 0.516193 0.626356 0.617194 -0.131771   0.0433881   0.107961    13  GLY   B O    
5    H H1   . GLY   A 1   ? 0.532451 0.722622 0.733177 -0.196279   0.0577261   0.114223    13  GLY   B H1   
6    H H2   . GLY   A 1   ? 0.501116 0.682814 0.680654 -0.167318   0.0423678   0.0959463   13  GLY   B H2   
7    H H3   . GLY   A 1   ? 0.519296 0.704445 0.682153 -0.167165   0.0630112   0.117523    13  GLY   B H3   
8    H HA2  . GLY   A 1   ? 0.578921 0.671904 0.721139 -0.189848   0.0573482   0.132815    13  GLY   B HA2  
9    H HA3  . GLY   A 1   ? 0.559172 0.649617 0.719619 -0.190481   0.0358379   0.107288    13  GLY   B HA3  
10   N N    . ALA   A 2   ? 0.570655 0.607188 0.667988 -0.146586   0.0266507   0.104202    14  ALA   B N    
11   C CA   . ALA   A 2   ? 0.533534 0.548287 0.599401 -0.123462   0.023013    0.104186    14  ALA   B CA   
12   C C    . ALA   A 2   ? 0.403986 0.445926 0.467643 -0.105205   0.0167891   0.0881453   14  ALA   B C    
13   O O    . ALA   A 2   ? 0.395658 0.443486 0.440258 -0.089479   0.0191928   0.0898926   14  ALA   B O    
14   C CB   . ALA   A 2   ? 0.532537 0.497314 0.585732 -0.120986   0.0130964   0.101245    14  ALA   B CB   
15   H H    . ALA   A 2   ? 0.57854  0.597888 0.68533  -0.158063   0.0207404   0.10003     14  ALA   B H    
16   H HA   . ALA   A 2   ? 0.526554 0.542621 0.579866 -0.120676   0.0318367   0.117304    14  ALA   B HA   
17   H HB1  . ALA   A 2   ? 0.565019 0.507731 0.615531 -0.130402   0.017311    0.112802    14  ALA   B HB1  
18   H HB2  . ALA   A 2   ? 0.532483 0.494141 0.595583 -0.124603   0.00516097  0.0887599   14  ALA   B HB2  
19   H HB3  . ALA   A 2   ? 0.529171 0.486896 0.566249 -0.105645   0.0104388   0.100116    14  ALA   B HB3  
20   N N    . PRO   A 3   ? 0.430511 0.48588  0.509896 -0.105536   0.0071419   0.0716568   15  PRO   B N    
21   C CA   . PRO   A 3   ? 0.429327 0.504227 0.501556 -0.0868623  0.0023935   0.0595743   15  PRO   B CA   
22   C C    . PRO   A 3   ? 0.39894  0.509329 0.4699   -0.0778162  0.0126473   0.0635246   15  PRO   B C    
23   O O    . PRO   A 3   ? 0.365345 0.47194  0.414788 -0.0609871  0.011839    0.0601772   15  PRO   B O    
24   C CB   . PRO   A 3   ? 0.467146 0.55306  0.557433 -0.0902857  -0.00959    0.0439509   15  PRO   B CB   
25   C CG   . PRO   A 3   ? 0.495009 0.55735  0.597031 -0.110249   -0.0140147  0.044444    15  PRO   B CG   
26   C CD   . PRO   A 3   ? 0.483696 0.533331 0.584587 -0.122545   -0.00117757 0.0633568   15  PRO   B CD   
27   H HA   . PRO   A 3   ? 0.422962 0.477249 0.478014 -0.077477   -0.00126838 0.0576843   15  PRO   B HA   
28   H HB2  . PRO   A 3   ? 0.453146 0.57075  0.558631 -0.0905969  -0.00776423 0.0419034   15  PRO   B HB2  
29   H HB3  . PRO   A 3   ? 0.450129 0.525072 0.527642 -0.0790194  -0.0163469  0.0359532   15  PRO   B HB3  
30   H HG2  . PRO   A 3   ? 0.488073 0.569476 0.609869 -0.11929    -0.0184004  0.0384657   15  PRO   B HG2  
31   H HG3  . PRO   A 3   ? 0.48878  0.52429  0.577727 -0.105458   -0.0207016  0.0387277   15  PRO   B HG3  
32   H HD2  . PRO   A 3   ? 0.488926 0.559413 0.609402 -0.136241   0.00405513  0.0679187   15  PRO   B HD2  
33   H HD3  . PRO   A 3   ? 0.496207 0.512901 0.589441 -0.126932   -0.00407226 0.0650712   15  PRO   B HD3  
34   N N    . ALA   A 4   ? 0.361269 0.505215 0.454589 -0.0895594  0.0230002   0.0704963   16  ALA   B N    
35   C CA   . ALA   A 4   ? 0.399218 0.580747 0.491523 -0.0791499  0.0350608   0.0734701   16  ALA   B CA   
36   C C    . ALA   A 4   ? 0.429984 0.593078 0.488978 -0.0703077  0.0430619   0.0847327   16  ALA   B C    
37   O O    . ALA   A 4   ? 0.382439 0.560832 0.42448  -0.0531239  0.047417    0.0810392   16  ALA   B O    
38   C CB   . ALA   A 4   ? 0.444647 0.667517 0.570328 -0.0970474  0.0476911   0.0818876   16  ALA   B CB   
39   H H    . ALA   A 4   ? 0.389535 0.533307 0.499415 -0.104641   0.0229238   0.0730449   16  ALA   B H    
40   H HA   . ALA   A 4   ? 0.388211 0.580295 0.478692 -0.0654457  0.0294686   0.0622857   16  ALA   B HA   
41   H HB1  . ALA   A 4   ? 0.427078 0.663862 0.575376 -0.102934   0.0403417   0.0735041   16  ALA   B HB1  
42   H HB2  . ALA   A 4   ? 0.450307 0.658277 0.575661 -0.111455   0.0536598   0.0940456   16  ALA   B HB2  
43   H HB3  . ALA   A 4   ? 0.435162 0.686034 0.559898 -0.0882058  0.0572546   0.0835349   16  ALA   B HB3  
44   N N    . THR   A 5   ? 0.44204  0.574476 0.49194  -0.0822457  0.045584    0.0992215   17  THR   B N    
45   C CA   . THR   A 5   ? 0.39264  0.508222 0.410157 -0.0734278  0.0508113   0.111351    17  THR   B CA   
46   C C    . THR   A 5   ? 0.384445 0.484174 0.380352 -0.0544896  0.0378103   0.0980716   17  THR   B C    
47   O O    . THR   A 5   ? 0.421267 0.525745 0.392828 -0.0409787  0.039554    0.097945    17  THR   B O    
48   C CB   . THR   A 5   ? 0.489437 0.569677 0.501802 -0.0870945  0.0525782   0.128503    17  THR   B CB   
49   O OG1  . THR   A 5   ? 0.512536 0.612953 0.546133 -0.107023   0.067097    0.140782    17  THR   B OG1  
50   C CG2  . THR   A 5   ? 0.512724 0.571911 0.489409 -0.0752117  0.0538515   0.141599    17  THR   B CG2  
51   H H    . THR   A 5   ? 0.431623 0.552633 0.494642 -0.0951467  0.0430577   0.101131    17  THR   B H    
52   H HA   . THR   A 5   ? 0.4276   0.565921 0.440721 -0.0706893  0.0615841   0.116736    17  THR   B HA   
53   H HB   . THR   A 5   ? 0.469648 0.529368 0.489263 -0.0904559  0.0430862   0.122232    17  THR   B HB   
55   H HG21 . THR   A 5   ? 0.535343 0.574668 0.508905 -0.0838466  0.0575999   0.155172    17  THR   B HG21 
56   H HG22 . THR   A 5   ? 0.51819  0.597281 0.48319  -0.0687202  0.0614117   0.144561    17  THR   B HG22 
57   H HG23 . THR   A 5   ? 0.500364 0.546186 0.468352 -0.0649543  0.0430146   0.133311    17  THR   B HG23 
58   N N    . VAL   A 6   ? 0.386134 0.466732 0.390171 -0.0544572  0.02474     0.0863091   18  VAL   B N    
59   C CA   . VAL   A 6   ? 0.376417 0.442943 0.36351  -0.0405069  0.0142531   0.0754586   18  VAL   B CA   
60   C C    . VAL   A 6   ? 0.387955 0.474064 0.369267 -0.0280337  0.0138749   0.0630311   18  VAL   B C    
61   O O    . VAL   A 6   ? 0.392471 0.473558 0.352368 -0.0170169  0.0107382   0.0584622   18  VAL   B O    
62   C CB   . VAL   A 6   ? 0.37109  0.415006 0.365943 -0.042588   0.00365457  0.0669745   18  VAL   B CB   
63   C CG1  . VAL   A 6   ? 0.340404 0.374573 0.320561 -0.0313918  -0.00408874 0.0581919   18  VAL   B CG1  
64   C CG2  . VAL   A 6   ? 0.406971 0.42681  0.404953 -0.0512102  0.003476    0.0769175   18  VAL   B CG2  
65   H H    . VAL   A 6   ? 0.380529 0.457186 0.400032 -0.0637094  0.0227476   0.085081    18  VAL   B H    
66   H HA   . VAL   A 6   ? 0.390657 0.448792 0.362716 -0.036695   0.0142924   0.0815845   18  VAL   B HA   
67   H HB   . VAL   A 6   ? 0.361983 0.41398  0.368901 -0.0452747  0.00228223  0.0604428   18  VAL   B HB   
68   H HG11 . VAL   A 6   ? 0.354702 0.389694 0.322968 -0.0272664  -0.00344844 0.0622976   18  VAL   B HG11 
69   H HG12 . VAL   A 6   ? 0.34067  0.38183  0.320308 -0.0271229  -0.00556788 0.0500448   18  VAL   B HG12 
70   H HG13 . VAL   A 6   ? 0.343964 0.363963 0.326753 -0.0325714  -0.00831518 0.0565188   18  VAL   B HG13 
71   H HG21 . VAL   A 6   ? 0.394342 0.400346 0.393594 -0.0494519  -0.0025034  0.0708156   18  VAL   B HG21 
72   H HG22 . VAL   A 6   ? 0.407024 0.429964 0.416524 -0.0612498  0.00738566  0.0808184   18  VAL   B HG22 
73   H HG23 . VAL   A 6   ? 0.411074 0.425447 0.397329 -0.0478323  0.00526878  0.0853581   18  VAL   B HG23 
74   N N    . THR   A 7   ? 0.401533 0.510305 0.401582 -0.0287787  0.016194    0.0568747   19  THR   B N    
75   C CA   . THR   A 7   ? 0.371018 0.49813  0.365435 -0.0134415  0.0167629   0.0459242   19  THR   B CA   
76   C C    . THR   A 7   ? 0.411933 0.552289 0.386271 -0.00461426 0.0268798   0.0505108   19  THR   B C    
77   O O    . THR   A 7   ? 0.383392 0.515715 0.334759 0.0103403   0.0230416   0.0405353   19  THR   B O    
78   C CB   . THR   A 7   ? 0.408931 0.567462 0.431549 -0.0150091  0.0185206   0.0415214   19  THR   B CB   
79   O OG1  . THR   A 7   ? 0.378641 0.519204 0.410455 -0.0201083  0.00623007  0.0350543   19  THR   B OG1  
80   C CG2  . THR   A 7   ? 0.41223  0.594528 0.430184 0.00500244  0.0211314   0.0315649   19  THR   B CG2  
81   H H    . THR   A 7   ? 0.386906 0.499365 0.403798 -0.0383984  0.0165489   0.059015    19  THR   B H    
82   H HA   . THR   A 7   ? 0.384707 0.494417 0.368659 -0.00688128 0.00878965  0.03797     19  THR   B HA   
83   H HB   . THR   A 7   ? 0.399932 0.575234 0.437177 -0.0257587  0.0263154   0.0500313   19  THR   B HB   
85   H HG21 . THR   A 7   ? 0.406903 0.604222 0.441728 0.00682333  0.0174589   0.0264029   19  THR   B HG21 
86   H HG22 . THR   A 7   ? 0.41638  0.577593 0.413651 0.015139    0.0157621   0.0252356   19  THR   B HG22 
87   H HG23 . THR   A 7   ? 0.421665 0.6249   0.439642 0.00660354  0.0317301   0.0364821   19  THR   B HG23 
88   N N    . GLU   A 8   ? 0.406335 0.56123  0.384642 -0.0144449  0.0394129   0.066029    20  GLU   B N    
89   C CA   . GLU   A 8   ? 0.456419 0.629654 0.412826 -0.00426292 0.0518663   0.0710446   20  GLU   B CA   
90   C C    . GLU   A 8   ? 0.519507 0.665509 0.439933 0.00266703  0.0452846   0.0729535   20  GLU   B C    
91   O O    . GLU   A 8   ? 0.486804 0.638414 0.378742 0.0177258   0.0477895   0.0674685   20  GLU   B O    
92   C CB   . GLU   A 8   ? 0.511187 0.712876 0.478205 -0.015628   0.0714099   0.0893693   20  GLU   B CB   
93   H H    . GLU   A 8   ? 0.41459  0.566536 0.406971 -0.0271216  0.0406851   0.073547    20  GLU   B H    
94   H HA   . GLU   A 8   ? 0.465406 0.651855 0.419275 0.00811145  0.0523719   0.0604887   20  GLU   B HA   
97   N N    . GLN   A 9   ? 0.479131 0.59874  0.39981  -0.00715011 0.0373172   0.0810531   21  GLN   B N    
98   C CA   . GLN   A 9   ? 0.511025 0.614168 0.401966 -0.0015567  0.0323773   0.0876948   21  GLN   B CA   
99   C C    . GLN   A 9   ? 0.49367  0.571775 0.383858 -0.00047943 0.0144919   0.0788708   21  GLN   B C    
100  O O    . GLN   A 9   ? 0.473552 0.542512 0.342854 0.00515075  0.00694541  0.0823259   21  GLN   B O    
101  C CB   . GLN   A 9   ? 0.531538 0.62758  0.418974 -0.0109851  0.040606    0.110585    21  GLN   B CB   
102  C CG   . GLN   A 9   ? 0.595777 0.718702 0.483132 -0.0152394  0.061563    0.123496    21  GLN   B CG   
103  C CD   . GLN   A 9   ? 0.666933 0.776928 0.553807 -0.0292515  0.0715887   0.148454    21  GLN   B CD   
104  O OE1  . GLN   A 9   ? 0.636975 0.715663 0.51411  -0.0299506  0.0621446   0.156732    21  GLN   B OE1  
105  N NE2  . GLN   A 9   ? 0.756288 0.890769 0.652386 -0.0393694  0.0916371   0.161316    21  GLN   B NE2  
106  H H    . GLN   A 9   ? 0.476521 0.589292 0.415493 -0.0161501  0.0344951   0.0821671   21  GLN   B H    
107  H HA   . GLN   A 9   ? 0.522564 0.634546 0.393418 0.00876239  0.0346432   0.0834066   21  GLN   B HA   
108  H HB2  . GLN   A 9   ? 0.530619 0.614615 0.436222 -0.0205235  0.0378935   0.113591    21  GLN   B HB2  
109  H HB3  . GLN   A 9   ? 0.555509 0.640985 0.421843 -0.00460202 0.0352012   0.114436    21  GLN   B HB3  
110  H HG2  . GLN   A 9   ? 0.610694 0.743967 0.475271 -0.00393838 0.0650903   0.121449    21  GLN   B HG2  
111  H HG3  . GLN   A 9   ? 0.579614 0.719055 0.489539 -0.0197242  0.0656606   0.11742     21  GLN   B HG3  
112  H HE21 . GLN   A 9   ? 0.748622 0.873907 0.647771 -0.0508362  0.0985715   0.176436    21  GLN   B HE21 
113  H HE22 . GLN   A 9   ? 0.727887 0.888324 0.627737 -0.0348449  0.0986609   0.155088    21  GLN   B HE22 
114  N N    . GLY   A 10  ? 0.430817 0.500887 0.343697 -0.00585544 0.0083299   0.0692781   22  GLY   B N    
115  C CA   . GLY   A 10  ? 0.42563  0.476286 0.340958 -0.00679375 -0.00459511 0.0644913   22  GLY   B CA   
116  C C    . GLY   A 10  ? 0.389696 0.436793 0.289779 0.0008841   -0.0144981  0.0495692   22  GLY   B C    
117  O O    . GLY   A 10  ? 0.403525 0.456027 0.291596 0.00810744  -0.0126356  0.0396648   22  GLY   B O    
118  H H    . GLY   A 10  ? 0.431846 0.510122 0.357823 -0.00815799 0.0121046   0.0659044   22  GLY   B H    
119  H HA2  . GLY   A 10  ? 0.424269 0.46944  0.33522  -0.00732573 -0.00589652 0.0736482   22  GLY   B HA2  
120  H HA3  . GLY   A 10  ? 0.400831 0.445913 0.332248 -0.0120079  -0.00559821 0.0618627   22  GLY   B HA3  
121  N N    . GLU   A 11  ? 0.410116 0.448603 0.309743 -5.601e-05  -0.0254117  0.0482173   23  GLU   B N    
122  C CA   . GLU   A 11  ? 0.393143 0.426688 0.283152 0.00190772  -0.0367224  0.033856    23  GLU   B CA   
123  C C    . GLU   A 11  ? 0.369102 0.390524 0.274156 -0.0042159  -0.0381647  0.0244339   23  GLU   B C    
124  O O    . GLU   A 11  ? 0.371156 0.389702 0.295136 -0.00978746 -0.0357536  0.0294648   23  GLU   B O    
125  C CB   . GLU   A 11  ? 0.420029 0.457461 0.311371 0.00190994  -0.0470593  0.0388735   23  GLU   B CB   
126  C CG   . GLU   A 11  ? 0.507036 0.543936 0.401141 -0.00205657 -0.061093   0.0253945   23  GLU   B CG   
127  C CD   . GLU   A 11  ? 0.602856 0.653107 0.507699 -0.00152461 -0.0726973  0.0293169   23  GLU   B CD   
128  O OE1  . GLU   A 11  ? 0.62758  0.683263 0.540792 0.00360742  -0.0712061  0.0428388   23  GLU   B OE1  
129  O OE2  . GLU   A 11  ? 0.585714 0.640451 0.490557 -0.00615217 -0.0851568  0.0167584   23  GLU   B OE2  
130  H H    . GLU   A 11  ? 0.398326 0.434331 0.304997 -0.00227276 -0.0259846  0.0560668   23  GLU   B H    
131  H HA   . GLU   A 11  ? 0.41455  0.450446 0.287098 0.00773496  -0.0363984  0.0287      23  GLU   B HA   
132  H HB2  . GLU   A 11  ? 0.448448 0.491309 0.324161 0.00765108  -0.0470601  0.0446758   23  GLU   B HB2  
133  H HB3  . GLU   A 11  ? 0.420912 0.456837 0.327285 -0.00083757 -0.0447396  0.0459635   23  GLU   B HB3  
134  H HG2  . GLU   A 11  ? 0.491391 0.521104 0.397873 -0.00811226 -0.059354   0.0206021   23  GLU   B HG2  
135  H HG3  . GLU   A 11  ? 0.520672 0.555804 0.397156 0.00089222  -0.06507    0.0173468   23  GLU   B HG3  
136  N N    . ASP   A 12  ? 0.355934 0.36649  0.24936  -0.00293588 -0.0432826  0.0111429   24  ASP   B N    
137  C CA   . ASP   A 12  ? 0.36796  0.361345 0.269776 -0.00878653 -0.0445764  0.0043665   24  ASP   B CA   
138  C C    . ASP   A 12  ? 0.354183 0.345325 0.266641 -0.0194314  -0.0529837  0.00205952  24  ASP   B C    
139  O O    . ASP   A 12  ? 0.398503 0.389588 0.301341 -0.0213348  -0.0628224  -0.00568796 24  ASP   B O    
140  C CB   . ASP   A 12  ? 0.394631 0.371035 0.275969 -0.00180885 -0.046392   -0.00809881 24  ASP   B CB   
141  C CG   . ASP   A 12  ? 0.412827 0.363117 0.294385 -0.0061491  -0.0479341  -0.0138071  24  ASP   B CG   
142  O OD1  . ASP   A 12  ? 0.372064 0.320628 0.270053 -0.0158746  -0.0464397  -0.00804933 24  ASP   B OD1  
143  O OD2  . ASP   A 12  ? 0.416255 0.346532 0.27913  0.00219901  -0.0494605  -0.023127   24  ASP   B OD2  
144  H H    . ASP   A 12  ? 0.38263  0.393798 0.259819 0.00208592  -0.0460001  0.00624109  24  ASP   B H    
145  H HA   . ASP   A 12  ? 0.349488 0.343929 0.262402 -0.00980817 -0.0390803  0.00938215  24  ASP   B HA   
146  H HB2  . ASP   A 12  ? 0.39613  0.380077 0.273543 0.00636388  -0.0404684  -0.00669962 24  ASP   B HB2  
147  H HB3  . ASP   A 12  ? 0.413226 0.387185 0.281725 -0.00085496 -0.0525413  -0.0142941  24  ASP   B HB3  
148  N N    . ILE   A 13  ? 0.355373 0.349185 0.288483 -0.0259185  -0.0495417  0.00821788  25  ILE   B N    
149  C CA   . ILE   A 13  ? 0.374417 0.376132 0.323977 -0.0354463  -0.0551019  0.00721027  25  ILE   B CA   
150  C C    . ILE   A 13  ? 0.411301 0.395239 0.364632 -0.0459071  -0.0521579  0.00280901  25  ILE   B C    
151  O O    . ILE   A 13  ? 0.357475 0.351093 0.330033 -0.0557963  -0.051643   0.00424931  25  ILE   B O    
152  C CB   . ILE   A 13  ? 0.376043 0.394963 0.344958 -0.0326215  -0.051595   0.0175279   25  ILE   B CB   
153  C CG1  . ILE   A 13  ? 0.362975 0.371603 0.335659 -0.0303028  -0.040675   0.0227599   25  ILE   B CG1  
154  C CG2  . ILE   A 13  ? 0.446828 0.478379 0.408834 -0.0230209  -0.0556926  0.0244502   25  ILE   B CG2  
155  C CD1  . ILE   A 13  ? 0.39037  0.407954 0.379851 -0.0273969  -0.0372158  0.0294635   25  ILE   B CD1  
156  H H    . ILE   A 13  ? 0.345461 0.337875 0.283163 -0.0241788  -0.0435125  0.0124753   25  ILE   B H    
157  H HA   . ILE   A 13  ? 0.390294 0.397423 0.334936 -0.0363293  -0.0631336  0.00266775  25  ILE   B HA   
158  H HB   . ILE   A 13  ? 0.382294 0.41011  0.364933 -0.0378557  -0.053948   0.0164319   25  ILE   B HB   
159  H HG12 . ILE   A 13  ? 0.370804 0.376187 0.334902 -0.0259043  -0.0386939  0.0246468   25  ILE   B HG12 
160  H HG13 . ILE   A 13  ? 0.372487 0.370784 0.343496 -0.0344348  -0.0381653  0.0192227   25  ILE   B HG13 
161  H HG21 . ILE   A 13  ? 0.420937 0.460422 0.394618 -0.0205074  -0.0553138  0.0302047   25  ILE   B HG21 
162  H HG22 . ILE   A 13  ? 0.426301 0.451761 0.37842  -0.0191062  -0.0507368  0.0276242   25  ILE   B HG22 
163  H HG23 . ILE   A 13  ? 0.437818 0.474979 0.392561 -0.0229761  -0.0636198  0.0200611   25  ILE   B HG23 
164  H HD11 . ILE   A 13  ? 0.378846 0.406971 0.379345 -0.0301724  -0.0394436  0.0281584   25  ILE   B HD11 
165  H HD12 . ILE   A 13  ? 0.374505 0.383486 0.364738 -0.0274341  -0.0315288  0.0298104   25  ILE   B HD12 
166  H HD13 . ILE   A 13  ? 0.380543 0.401643 0.368329 -0.0220089  -0.0385393  0.0345717   25  ILE   B HD13 
167  N N    . THR   A 14  ? 0.374481 0.333614 0.30947  -0.0428963  -0.0495399  -0.00150851 26  THR   B N    
168  C CA   . THR   A 14  ? 0.451255 0.384702 0.381704 -0.0522587  -0.0475593  -0.0042727  26  THR   B CA   
169  C C    . THR   A 14  ? 0.447467 0.369005 0.372951 -0.0641018  -0.0574437  -0.0141574  26  THR   B C    
170  O O    . THR   A 14  ? 0.493001 0.413823 0.404094 -0.0583071  -0.0662616  -0.0227937  26  THR   B O    
171  C CB   . THR   A 14  ? 0.409741 0.317695 0.320077 -0.0419687  -0.043361   -0.00490407 26  THR   B CB   
172  O OG1  . THR   A 14  ? 0.421694 0.321276 0.312752 -0.0309379  -0.048587   -0.0133012  26  THR   B OG1  
173  C CG2  . THR   A 14  ? 0.416337 0.337712 0.335119 -0.0344621  -0.0360406  0.00304491  26  THR   B CG2  
174  H H    . THR   A 14  ? 0.397874 0.355795 0.322703 -0.0343813  -0.0485773  -0.00201459 26  THR   B H    
175  H HA   . THR   A 14  ? 0.415108 0.355515 0.359133 -0.0579401  -0.0426924  0.00098156  26  THR   B HA   
176  H HB   . THR   A 14  ? 0.439768 0.327583 0.344726 -0.0481762  -0.0420084  -0.00491777 26  THR   B HB   
178  H HG21 . THR   A 14  ? 0.413492 0.323101 0.321352 -0.0271807  -0.0350058  0.0022132   26  THR   B HG21 
179  H HG22 . THR   A 14  ? 0.39353  0.332573 0.318802 -0.0306061  -0.0365108  0.00448923  26  THR   B HG22 
180  H HG23 . THR   A 14  ? 0.401652 0.325392 0.329594 -0.0405524  -0.0321909  0.00725234  26  THR   B HG23 
181  N N    . SER   A 15  ? 0.451542 0.357655 0.383759 -0.0805227  -0.0550798  -0.0134641  27  SER   B N    
182  C CA   . SER   A 15  ? 0.514738 0.40319  0.443697 -0.0967927  -0.0647113  -0.0234506  27  SER   B CA   
183  C C    . SER   A 15  ? 0.530411 0.373674 0.424441 -0.0887267  -0.0690191  -0.0326428  27  SER   B C    
184  O O    . SER   A 15  ? 0.506912 0.334488 0.387579 -0.0927282  -0.0811812  -0.0461767  27  SER   B O    
185  C CB   . SER   A 15  ? 0.608614 0.495383 0.55783  -0.119828   -0.0587353  -0.0181096  27  SER   B CB   
186  O OG   . SER   A 15  ? 0.628907 0.564419 0.612876 -0.123865   -0.0562091  -0.0123537  27  SER   B OG   
187  H H    . SER   A 15  ? 0.454402 0.360349 0.392764 -0.0823809  -0.0470102  -0.00653798 27  SER   B H    
188  H HA   . SER   A 15  ? 0.514854 0.423271 0.450783 -0.0975682  -0.0732922  -0.0286165  27  SER   B HA   
189  H HB2  . SER   A 15  ? 0.603694 0.471926 0.544258 -0.118328   -0.0494221  -0.011321   27  SER   B HB2  
190  H HB3  . SER   A 15  ? 0.624839 0.496463 0.571637 -0.132678   -0.0658228  -0.0253371  27  SER   B HB3  
192  N N    . LYS   A 16  ? 0.563551 0.386277 0.442211 -0.0759051  -0.0601553  -0.0263392  28  LYS   B N    
193  C CA   . LYS   A 16  ? 0.644777 0.424482 0.490597 -0.0631027  -0.062948   -0.0334875  28  LYS   B CA   
194  C C    . LYS   A 16  ? 0.600592 0.393822 0.432701 -0.0411008  -0.0673277  -0.0421962  28  LYS   B C    
195  O O    . LYS   A 16  ? 0.578719 0.34083  0.383508 -0.0276103  -0.0711284  -0.0519055  28  LYS   B O    
196  C CB   . LYS   A 16  ? 0.686517 0.443294 0.519867 -0.0532583  -0.0537249  -0.0234033  28  LYS   B CB   
197  C CG   . LYS   A 16  ? 0.797531 0.525978 0.630745 -0.0729527  -0.0477032  -0.0145571  28  LYS   B CG   
198  C CD   . LYS   A 16  ? 0.890002 0.59262  0.702884 -0.0600202  -0.040041   -0.00396256 28  LYS   B CD   
199  C CE   . LYS   A 16  ? 0.997117 0.699375 0.819517 -0.0779813  -0.028557   0.00978731  28  LYS   B CE   
200  N NZ   . LYS   A 16  ? 1.19563  0.868104 0.990526 -0.0639017  -0.0228264  0.0200373   28  LYS   B NZ   
201  H H    . LYS   A 16  ? 0.544245 0.380174 0.432599 -0.0737097  -0.0527305  -0.0177533  28  LYS   B H    
202  H HA   . LYS   A 16  ? 0.664661 0.418748 0.502425 -0.0740509  -0.0685294  -0.0399728  28  LYS   B HA   
203  H HB2  . LYS   A 16  ? 0.66633  0.449164 0.510838 -0.0464812  -0.0488066  -0.0172425  28  LYS   B HB2  
204  H HB3  . LYS   A 16  ? 0.715776 0.450218 0.528417 -0.0394521  -0.0564944  -0.0285474  28  LYS   B HB3  
205  H HG2  . LYS   A 16  ? 0.825886 0.526363 0.649299 -0.0823504  -0.0529016  -0.0206297  28  LYS   B HG2  
206  H HG3  . LYS   A 16  ? 0.773193 0.528136 0.628821 -0.0851397  -0.0437297  -0.00960787 28  LYS   B HG3  
207  H HD2  . LYS   A 16  ? 0.866339 0.590454 0.681919 -0.0450192  -0.0392284  -0.00306391 28  LYS   B HD2  
208  H HD3  . LYS   A 16  ? 0.930198 0.595039 0.719861 -0.0540753  -0.0435743  -0.00714924 28  LYS   B HD3  
209  H HE2  . LYS   A 16  ? 1.03127  0.716531 0.855347 -0.0955514  -0.0284753  0.00958488  28  LYS   B HE2  
210  H HE3  . LYS   A 16  ? 0.97253  0.711185 0.816473 -0.0807707  -0.0248226  0.0123563   28  LYS   B HE3  
211  H HZ1  . LYS   A 16  ? 1.16742  0.803988 0.941104 -0.059501   -0.026533   0.018263    28  LYS   B HZ1  
212  H HZ2  . LYS   A 16  ? 1.11288  0.803617 0.908598 -0.0488781  -0.0240286  0.0192872   28  LYS   B HZ2  
213  H HZ3  . LYS   A 16  ? 1.14096  0.812433 0.938219 -0.0740347  -0.0145626  0.0289821   28  LYS   B HZ3  
214  N N    . LYS   A 17  ? 0.560096 0.397288 0.408993 -0.0362451  -0.0655157  -0.0380462  29  LYS   B N    
215  C CA   . LYS   A 17  ? 0.527969 0.38173  0.364647 -0.0160225  -0.0650088  -0.0421834  29  LYS   B CA   
216  C C    . LYS   A 17  ? 0.586407 0.42827  0.41015  0.00360034  -0.0587325  -0.0415144  29  LYS   B C    
217  O O    . LYS   A 17  ? 0.546729 0.380508 0.349434 0.021362    -0.0600325  -0.0512442  29  LYS   B O    
218  C CB   . LYS   A 17  ? 0.565823 0.410239 0.380331 -0.0122319  -0.0752363  -0.0574058  29  LYS   B CB   
219  C CG   . LYS   A 17  ? 0.600163 0.468248 0.429291 -0.0277997  -0.0841284  -0.0581872  29  LYS   B CG   
220  C CD   . LYS   A 17  ? 0.702853 0.614856 0.550169 -0.0240644  -0.0794556  -0.0457888  29  LYS   B CD   
221  C CE   . LYS   A 17  ? 0.828753 0.763438 0.681668 -0.0314364  -0.0915774  -0.0485941  29  LYS   B CE   
222  N NZ   . LYS   A 17  ? 0.800508 0.75777  0.687577 -0.0440042  -0.0900875  -0.0374048  29  LYS   B NZ   
223  H H    . LYS   A 17  ? 0.534197 0.391155 0.401896 -0.0451383  -0.0637076  -0.0319093  29  LYS   B H    
224  H HA   . LYS   A 17  ? 0.517259 0.399802 0.36867  -0.0161437  -0.0618011  -0.0352384  29  LYS   B HA   
225  H HB2  . LYS   A 17  ? 0.604525 0.416327 0.403875 -0.0137065  -0.0796572  -0.0655346  29  LYS   B HB2  
226  H HB3  . LYS   A 17  ? 0.573072 0.429045 0.377706 0.00253657  -0.0723351  -0.059178   29  LYS   B HB3  
227  H HG2  . LYS   A 17  ? 0.617692 0.478795 0.460192 -0.0428888  -0.0859401  -0.0564124  29  LYS   B HG2  
228  H HG3  . LYS   A 17  ? 0.644738 0.503807 0.456609 -0.025718   -0.0925159  -0.0695725  29  LYS   B HG3  
229  H HD2  . LYS   A 17  ? 0.687743 0.606862 0.524492 -0.0107373  -0.0743928  -0.0445615  29  LYS   B HD2  
230  H HD3  . LYS   A 17  ? 0.667585 0.586776 0.533189 -0.0288336  -0.0731997  -0.0362962  29  LYS   B HD3  
231  H HE2  . LYS   A 17  ? 0.821805 0.741816 0.664997 -0.0374652  -0.101311   -0.0600931  29  LYS   B HE2  
232  H HE3  . LYS   A 17  ? 0.797784 0.747098 0.640755 -0.020917   -0.0908202  -0.0464489  29  LYS   B HE3  
233  H HZ1  . LYS   A 17  ? 0.79963  0.745021 0.695578 -0.0537909  -0.0886348  -0.0381046  29  LYS   B HZ1  
234  H HZ2  . LYS   A 17  ? 0.778444 0.746817 0.672403 -0.0380876  -0.0822164  -0.0278705  29  LYS   B HZ2  
235  H HZ3  . LYS   A 17  ? 0.803168 0.775343 0.69512  -0.0473194  -0.0984884  -0.039458   29  LYS   B HZ3  
236  N N    . ASP   A 18  ? 0.561731 0.409509 0.399508 0.0023891   -0.0521743  -0.0304704  30  ASP   B N    
237  C CA   . ASP   A 18  ? 0.470387 0.317423 0.302936 0.0201809   -0.0482424  -0.0283406  30  ASP   B CA   
238  C C    . ASP   A 18  ? 0.471739 0.362313 0.32641  0.0243498   -0.0423112  -0.021087   30  ASP   B C    
239  O O    . ASP   A 18  ? 0.451471 0.35004  0.311744 0.033106    -0.0402372  -0.0175065  30  ASP   B O    
240  C CB   . ASP   A 18  ? 0.503955 0.320998 0.330364 0.0161181   -0.0473601  -0.0220513  30  ASP   B CB   
241  C CG   . ASP   A 18  ? 0.526069 0.354986 0.37194  -0.00207146 -0.0425414  -0.0115012  30  ASP   B CG   
242  O OD1  . ASP   A 18  ? 0.42757  0.290899 0.29453  -0.00698411 -0.0402329  -0.00835096 30  ASP   B OD1  
243  O OD2  . ASP   A 18  ? 0.518848 0.320328 0.356231 -0.0100382  -0.0402016  -0.00605576 30  ASP   B OD2  
244  H H    . ASP   A 18  ? 0.524569 0.379087 0.37599  -0.00937131 -0.0506778  -0.0245505  30  ASP   B H    
245  H HA   . ASP   A 18  ? 0.519119 0.355239 0.335962 0.032845    -0.0503614  -0.0359634  30  ASP   B HA   
246  H HB2  . ASP   A 18  ? 0.510408 0.328982 0.332966 0.0293451   -0.046655   -0.0209202  30  ASP   B HB2  
247  H HB3  . ASP   A 18  ? 0.539185 0.324452 0.349783 0.0134693   -0.0506007  -0.0261219  30  ASP   B HB3  
248  N N    . ARG   A 19  ? 0.430903 0.347677 0.29933  0.0155645   -0.0406595  -0.0176451  31  ARG   B N    
249  C CA   . ARG   A 19  ? 0.421365 0.372918 0.309808 0.0155045   -0.0347137  -0.00940539 31  ARG   B CA   
250  C C    . ARG   A 19  ? 0.40397  0.357899 0.308004 0.00998508  -0.0327523  -0.00241323 31  ARG   B C    
251  O O    . ARG   A 19  ? 0.428012 0.404525 0.347392 0.0106813   -0.0294201  0.00202092  31  ARG   B O    
252  C CB   . ARG   A 19  ? 0.416711 0.388483 0.301855 0.0314606   -0.0304386  -0.0127461  31  ARG   B CB   
253  C CG   . ARG   A 19  ? 0.466062 0.442344 0.334027 0.0375998   -0.0300105  -0.0185571  31  ARG   B CG   
254  C CD   . ARG   A 19  ? 0.481285 0.483447 0.345774 0.0549468   -0.0220697  -0.0214304  31  ARG   B CD   
255  N NE   . ARG   A 19  ? 0.48157  0.520581 0.372771 0.050982    -0.013194   -0.010559   31  ARG   B NE   
256  C CZ   . ARG   A 19  ? 0.459151 0.52199  0.362528 0.0407556   -0.00583015 0.00098996  31  ARG   B CZ   
257  N NH1  . ARG   A 19  ? 0.415299 0.473126 0.303834 0.0364419   -0.00640598 0.00426155  31  ARG   B NH1  
258  N NH2  . ARG   A 19  ? 0.508933 0.600128 0.438775 0.0352706   0.0012639   0.00911233  31  ARG   B NH2  
259  H H    . ARG   A 19  ? 0.447584 0.358832 0.312097 0.00911137  -0.0439827  -0.0203734  31  ARG   B H    
260  H HA   . ARG   A 19  ? 0.40881  0.369999 0.301864 0.00899855  -0.034711   -0.00652147 31  ARG   B HA   
261  H HB2  . ARG   A 19  ? 0.437657 0.398967 0.315815 0.040936    -0.0320043  -0.0172329  31  ARG   B HB2  
262  H HB3  . ARG   A 19  ? 0.409548 0.403154 0.310265 0.0292477   -0.0261507  -0.00673353 31  ARG   B HB3  
263  H HG2  . ARG   A 19  ? 0.451542 0.437366 0.324501 0.0292909   -0.0294952  -0.0132532  31  ARG   B HG2  
264  H HG3  . ARG   A 19  ? 0.479815 0.432162 0.332075 0.0387424   -0.0356557  -0.0261358  31  ARG   B HG3  
265  H HD2  . ARG   A 19  ? 0.499653 0.504352 0.350289 0.0583437   -0.021136   -0.0244582  31  ARG   B HD2  
266  H HD3  . ARG   A 19  ? 0.499813 0.490874 0.356396 0.0663203   -0.0239073  -0.0283582  31  ARG   B HD3  
267  H HE   . ARG   A 19  ? 0.469707 0.514905 0.370252 0.0553252   -0.0129922  -0.0114302  31  ARG   B HE   
268  H HH11 . ARG   A 19  ? 0.43792  0.47719  0.314945 0.0353945   -0.013418   -0.0006177  31  ARG   B HH11 
269  H HH12 . ARG   A 19  ? 0.431782 0.505284 0.321954 0.0344558   -0.00010741 0.0116247   31  ARG   B HH12 
270  H HH21 . ARG   A 19  ? 0.483384 0.582658 0.422747 0.0400789   0.00069771  0.00576804  31  ARG   B HH21 
271  H HH22 . ARG   A 19  ? 0.481185 0.582108 0.41866  0.026562    0.00580431  0.0176632   31  ARG   B HH22 
272  N N    . GLY   A 20  ? 0.4608   0.392321 0.361244 0.00211552  -0.0343738  -0.00123672 32  GLY   B N    
273  C CA   . GLY   A 20  ? 0.43765  0.367741 0.34523  -0.00087518 -0.0322926  0.00387906  32  GLY   B CA   
274  C C    . GLY   A 20  ? 0.433523 0.382086 0.360345 -0.00980974 -0.0291272  0.00966977  32  GLY   B C    
275  O O    . GLY   A 20  ? 0.379547 0.33119  0.312452 -0.0100147  -0.0279213  0.011743    32  GLY   B O    
276  H H    . GLY   A 20  ? 0.456256 0.37344  0.349087 -0.0020306  -0.0365185  -0.00382393 32  GLY   B H    
277  H HA2  . GLY   A 20  ? 0.445205 0.379755 0.351744 0.00731104  -0.0332234  0.00274738  32  GLY   B HA2  
278  H HA3  . GLY   A 20  ? 0.456477 0.367323 0.35541  -0.00414388 -0.0322769  0.00435823  32  GLY   B HA3  
279  N N    . VAL   A 21  ? 0.371512 0.329624 0.305292 -0.0156763  -0.0291559  0.011501    33  VAL   B N    
280  C CA   . VAL   A 21  ? 0.327705 0.299649 0.276701 -0.0202905  -0.027114   0.0175231   33  VAL   B CA   
281  C C    . VAL   A 21  ? 0.36441  0.350688 0.313614 -0.0187562  -0.0283545  0.020067    33  VAL   B C    
282  O O    . VAL   A 21  ? 0.320289 0.30627  0.262531 -0.0195247  -0.0325743  0.0170138   33  VAL   B O    
283  C CB   . VAL   A 21  ? 0.344903 0.314118 0.301316 -0.0268942  -0.0259772  0.0192828   33  VAL   B CB   
284  C CG1  . VAL   A 21  ? 0.345683 0.326535 0.316381 -0.0266526  -0.024281   0.0249023   33  VAL   B CG1  
285  C CG2  . VAL   A 21  ? 0.381652 0.335086 0.331766 -0.0288348  -0.0222029  0.0182627   33  VAL   B CG2  
286  H H    . VAL   A 21  ? 0.385846 0.339957 0.312767 -0.0156463  -0.0315027  0.00842903  33  VAL   B H    
287  H HA   . VAL   A 21  ? 0.338567 0.313012 0.292173 -0.0191017  -0.0254858  0.0189991   33  VAL   B HA   
288  H HB   . VAL   A 21  ? 0.353466 0.323725 0.308624 -0.0298481  -0.0288716  0.0174769   33  VAL   B HB   
289  H HG11 . VAL   A 21  ? 0.340556 0.318518 0.312001 -0.0247506  -0.0224633  0.0257585   33  VAL   B HG11 
290  H HG12 . VAL   A 21  ? 0.342582 0.331372 0.314608 -0.0255984  -0.0267099  0.0271727   33  VAL   B HG12 
291  H HG13 . VAL   A 21  ? 0.34281  0.325331 0.319614 -0.0288203  -0.0227374  0.0252743   33  VAL   B HG13 
292  H HG21 . VAL   A 21  ? 0.371974 0.328958 0.329482 -0.0329876  -0.019399   0.0201111   33  VAL   B HG21 
293  H HG22 . VAL   A 21  ? 0.38424  0.326118 0.324112 -0.0293666  -0.02364    0.0157871   33  VAL   B HG22 
294  H HG23 . VAL   A 21  ? 0.37133  0.322494 0.319164 -0.0249281  -0.0211546  0.018361    33  VAL   B HG23 
295  N N    . LEU   A 22  ? 0.326993 0.324418 0.282742 -0.0176192  -0.0248361  0.0257001   34  LEU   B N    
296  C CA   . LEU   A 22  ? 0.351095 0.361308 0.303351 -0.0157565  -0.0229092  0.0314078   34  LEU   B CA   
297  C C    . LEU   A 22  ? 0.309137 0.318913 0.270541 -0.0194423  -0.0217229  0.0414281   34  LEU   B C    
298  O O    . LEU   A 22  ? 0.335045 0.337829 0.307159 -0.0230812  -0.0200102  0.0430761   34  LEU   B O    
299  C CB   . LEU   A 22  ? 0.33585  0.359537 0.287686 -0.0121197  -0.017478   0.0312997   34  LEU   B CB   
300  C CG   . LEU   A 22  ? 0.380956 0.403126 0.320911 -0.00299932 -0.0191344  0.0207718   34  LEU   B CG   
301  C CD1  . LEU   A 22  ? 0.434244 0.479216 0.384544 0.00059836  -0.0125492  0.02223     34  LEU   B CD1  
302  C CD2  . LEU   A 22  ? 0.417783 0.436142 0.337164 0.00341013  -0.0219313  0.0151403   34  LEU   B CD2  
303  H H    . LEU   A 22  ? 0.333874 0.330035 0.295776 -0.0188088  -0.0233394  0.0263281   34  LEU   B H    
304  H HA   . LEU   A 22  ? 0.343239 0.353099 0.286233 -0.0137045  -0.0262465  0.0286632   34  LEU   B HA   
305  H HB2  . LEU   A 22  ? 0.342805 0.368421 0.305893 -0.015654   -0.0157679  0.0329174   34  LEU   B HB2  
306  H HB3  . LEU   A 22  ? 0.354949 0.387506 0.303309 -0.0116462  -0.0141764  0.0369859   34  LEU   B HB3  
307  H HG   . LEU   A 22  ? 0.384091 0.393812 0.324154 -0.0033395  -0.0224667  0.0165791   34  LEU   B HG   
308  H HD11 . LEU   A 22  ? 0.407812 0.453555 0.370418 -0.00360114 -0.0133945  0.0229458   34  LEU   B HD11 
309  H HD12 . LEU   A 22  ? 0.424234 0.471352 0.367014 0.0096122   -0.012833   0.0157891   34  LEU   B HD12 
310  H HD13 . LEU   A 22  ? 0.418769 0.475936 0.370781 -0.00166323 -0.00731055 0.0287619   34  LEU   B HD13 
311  H HD21 . LEU   A 22  ? 0.41186  0.4203   0.328863 -0.00087285 -0.0268957  0.0142391   34  LEU   B HD21 
312  H HD22 . LEU   A 22  ? 0.41671  0.44776  0.33245  0.00540789  -0.0180014  0.0194356   34  LEU   B HD22 
313  H HD23 . LEU   A 22  ? 0.420199 0.432977 0.331353 0.0102268   -0.0229896  0.00778238  34  LEU   B HD23 
314  N N    . LYS   A 23  ? 0.336508 0.350997 0.29028  -0.0165833  -0.0241319  0.0474333   35  LYS   B N    
315  C CA   . LYS   A 23  ? 0.344914 0.35492  0.303777 -0.0158394  -0.0249813  0.0573374   35  LYS   B CA   
316  C C    . LYS   A 23  ? 0.372144 0.385367 0.318275 -0.0127435  -0.0224381  0.0700673   35  LYS   B C    
317  O O    . LYS   A 23  ? 0.394515 0.417733 0.324498 -0.00847994 -0.0235557  0.0694952   35  LYS   B O    
318  C CB   . LYS   A 23  ? 0.352541 0.366141 0.315707 -0.012498   -0.0330616  0.0538353   35  LYS   B CB   
319  C CG   . LYS   A 23  ? 0.332985 0.344515 0.302022 -0.00636362 -0.0355611  0.0628037   35  LYS   B CG   
320  C CD   . LYS   A 23  ? 0.346273 0.372462 0.325112 -0.00128028 -0.0442041  0.0595947   35  LYS   B CD   
321  C CE   . LYS   A 23  ? 0.3625   0.386896 0.348006 0.00947791  -0.0463707  0.0682186   35  LYS   B CE   
322  N NZ   . LYS   A 23  ? 0.386547 0.433983 0.383676 0.0178989   -0.0564909  0.066983    35  LYS   B NZ   
323  H H    . LYS   A 23  ? 0.339797 0.35919  0.28315  -0.0136138  -0.0259923  0.0448507   35  LYS   B H    
324  H HA   . LYS   A 23  ? 0.343875 0.346009 0.311493 -0.0188104  -0.0222293  0.058476    35  LYS   B HA   
325  H HB2  . LYS   A 23  ? 0.334305 0.34556  0.304834 -0.015426   -0.0327909  0.047386    35  LYS   B HB2  
326  H HB3  . LYS   A 23  ? 0.349115 0.369967 0.303738 -0.0109363  -0.0374976  0.0509781   35  LYS   B HB3  
327  H HG2  . LYS   A 23  ? 0.35575  0.365591 0.314866 -0.00349986 -0.0351082  0.071075    35  LYS   B HG2  
328  H HG3  . LYS   A 23  ? 0.34001  0.341318 0.31612  -0.00752865 -0.0316069  0.0637172   35  LYS   B HG3  
329  H HD2  . LYS   A 23  ? 0.333318 0.362167 0.321933 -0.0056764  -0.0430515  0.0524004   35  LYS   B HD2  
330  H HD3  . LYS   A 23  ? 0.350138 0.385827 0.321131 -0.00045816 -0.0500772  0.0580434   35  LYS   B HD3  
331  H HE2  . LYS   A 23  ? 0.379889 0.394738 0.353543 0.0126731   -0.0455515  0.0770563   35  LYS   B HE2  
332  H HE3  . LYS   A 23  ? 0.361571 0.37654  0.35486  0.00906025  -0.0412946  0.0669009   35  LYS   B HE3  
333  H HZ1  . LYS   A 23  ? 0.388643 0.443548 0.376358 0.0197657   -0.0628948  0.0685184   35  LYS   B HZ1  
334  H HZ2  . LYS   A 23  ? 0.368817 0.427214 0.378286 0.0129334   -0.0565323  0.0594087   35  LYS   B HZ2  
335  H HZ3  . LYS   A 23  ? 0.388255 0.432222 0.389645 0.0265713   -0.0565863  0.0720986   35  LYS   B HZ3  
336  N N    . ILE   A 24  ? 0.384444 0.385238 0.33501  -0.0149319  -0.0184463  0.0814335   36  ILE   B N    
337  C CA   . ILE   A 24  ? 0.417381 0.413368 0.352546 -0.0110501  -0.0162305  0.0979023   36  ILE   B CA   
338  C C    . ILE   A 24  ? 0.419314 0.397142 0.357547 -0.00445012 -0.0214629  0.105115    36  ILE   B C    
339  O O    . ILE   A 24  ? 0.437381 0.398435 0.389157 -0.00750377 -0.0203125  0.102731    36  ILE   B O    
340  C CB   . ILE   A 24  ? 0.429831 0.423734 0.364121 -0.0209468  -0.00384365 0.108721    36  ILE   B CB   
341  C CG1  . ILE   A 24  ? 0.414449 0.432707 0.346023 -0.0229888  0.00284228  0.102343    36  ILE   B CG1  
342  C CG2  . ILE   A 24  ? 0.530471 0.513638 0.444162 -0.017122   -0.00015813 0.128913    36  ILE   B CG2  
343  C CD1  . ILE   A 24  ? 0.452293 0.478807 0.39318  -0.0351731  0.0167513   0.112001    36  ILE   B CD1  
344  H H    . ILE   A 24  ? 0.379458 0.371694 0.34042  -0.0187005  -0.0171819  0.0794057   36  ILE   B H    
345  H HA   . ILE   A 24  ? 0.41978  0.426077 0.342225 -0.00544661 -0.0195671  0.0972474   36  ILE   B HA   
346  H HB   . ILE   A 24  ? 0.436016 0.419571 0.383604 -0.0279753  -0.00209175 0.107798    36  ILE   B HB   
347  H HG12 . ILE   A 24  ? 0.432145 0.457791 0.346856 -0.0157439  0.00163156  0.103493    36  ILE   B HG12 
348  H HG13 . ILE   A 24  ? 0.403437 0.426151 0.343709 -0.022816   -0.00081966 0.0900494   36  ILE   B HG13 
349  H HG21 . ILE   A 24  ? 0.519849 0.505528 0.432139 -0.0246605  0.00949845  0.136764    36  ILE   B HG21 
350  H HG22 . ILE   A 24  ? 0.515043 0.507179 0.413688 -0.00819145 -0.00460225 0.12873     36  ILE   B HG22 
351  H HG23 . ILE   A 24  ? 0.519144 0.483391 0.434901 -0.0155359  -0.00310455 0.134369    36  ILE   B HG23 
352  H HD11 . ILE   A 24  ? 0.439156 0.456122 0.395838 -0.0433926  0.0162881   0.111022    36  ILE   B HD11 
353  H HD12 . ILE   A 24  ? 0.435872 0.481316 0.378804 -0.0340343  0.0203365   0.105471    36  ILE   B HD12 
354  H HD13 . ILE   A 24  ? 0.466811 0.489743 0.395752 -0.0357354  0.0224063   0.125472    36  ILE   B HD13 
355  N N    . VAL   A 25  ? 0.46003  0.441076 0.383339 0.00725111  -0.0283483  0.113081    37  VAL   B N    
356  C CA   . VAL   A 25  ? 0.501134 0.464192 0.422685 0.0182413   -0.0331296  0.123698    37  VAL   B CA   
357  C C    . VAL   A 25  ? 0.513376 0.44813  0.420558 0.013802    -0.0238451  0.142825    37  VAL   B C    
358  O O    . VAL   A 25  ? 0.47141  0.40898  0.358063 0.0118887   -0.0181419  0.155093    37  VAL   B O    
359  C CB   . VAL   A 25  ? 0.5173   0.497698 0.42983  0.034259    -0.0466051  0.124895    37  VAL   B CB   
360  C CG1  . VAL   A 25  ? 0.527498 0.489189 0.436514 0.0503412   -0.0520015  0.137577    37  VAL   B CG1  
361  C CG2  . VAL   A 25  ? 0.483997 0.492045 0.416498 0.0335863   -0.0551374  0.106075    37  VAL   B CG2  
362  H H    . VAL   A 25  ? 0.460409 0.454718 0.373101 0.00993193  -0.0310383  0.111349    37  VAL   B H    
363  H HA   . VAL   A 25  ? 0.482505 0.439921 0.419025 0.01802     -0.0337259  0.117036    37  VAL   B HA   
364  H HB   . VAL   A 25  ? 0.524911 0.51094  0.419158 0.035094    -0.0466254  0.130036    37  VAL   B HB   
365  H HG11 . VAL   A 25  ? 0.52792  0.476426 0.450219 0.0490682   -0.0487387  0.13448     37  VAL   B HG11 
366  H HG12 . VAL   A 25  ? 0.560482 0.505404 0.450574 0.0520711   -0.0486529  0.151706    37  VAL   B HG12 
367  H HG13 . VAL   A 25  ? 0.533582 0.512805 0.445162 0.0609244   -0.0622334  0.134594    37  VAL   B HG13 
368  H HG21 . VAL   A 25  ? 0.49293  0.514607 0.423015 0.0425112   -0.0649338  0.106309    37  VAL   B HG21 
369  H HG22 . VAL   A 25  ? 0.472224 0.487855 0.402737 0.0253446   -0.0528012  0.098724    37  VAL   B HG22 
370  H HG23 . VAL   A 25  ? 0.472546 0.476736 0.421646 0.0325199   -0.0530902  0.101245    37  VAL   B HG23 
371  N N    . LYS   A 26  ? 0.499252 0.404708 0.416529 0.0108085   -0.0212432  0.144782    38  LYS   B N    
372  C CA   . LYS   A 26  ? 0.572256 0.442532 0.478131 0.00288234  -0.0128398  0.162878    38  LYS   B CA   
373  C C    . LYS   A 26  ? 0.625601 0.465415 0.513481 0.0206255   -0.0187168  0.178416    38  LYS   B C    
374  O O    . LYS   A 26  ? 0.642104 0.452953 0.508969 0.0174643   -0.0122686  0.199776    38  LYS   B O    
375  C CB   . LYS   A 26  ? 0.649352 0.498365 0.57397  -0.0132092  -0.00798274 0.154684    38  LYS   B CB   
376  C CG   . LYS   A 26  ? 0.632609 0.510804 0.572354 -0.0301064  -0.00190195 0.143819    38  LYS   B CG   
377  C CD   . LYS   A 26  ? 0.643264 0.541198 0.57485  -0.0402684  0.00890556  0.155699    38  LYS   B CD   
378  C CE   . LYS   A 26  ? 0.677915 0.565353 0.620996 -0.0625537  0.0196257   0.163421    38  LYS   B CE   
379  N NZ   . LYS   A 26  ? 0.748868 0.660672 0.683701 -0.0696682  0.0328286   0.176804    38  LYS   B NZ   
380  H H    . LYS   A 26  ? 0.49805  0.403647 0.428489 0.0131193   -0.0244445  0.134572    38  LYS   B H    
381  H HA   . LYS   A 26  ? 0.587985 0.467064 0.484166 -0.00380665 -0.00640398 0.170861    38  LYS   B HA   
382  H HB2  . LYS   A 26  ? 0.624134 0.467882 0.557024 -0.00598332 -0.0134731  0.14443     38  LYS   B HB2  
383  H HB3  . LYS   A 26  ? 0.664388 0.485635 0.582187 -0.0191497  -0.00376299 0.166457    38  LYS   B HB3  
384  H HG2  . LYS   A 26  ? 0.601411 0.500174 0.546718 -0.0241532  -0.00649518 0.131856    38  LYS   B HG2  
385  H HG3  . LYS   A 26  ? 0.629981 0.495646 0.581248 -0.0400344  -0.00071655 0.138364    38  LYS   B HG3  
386  H HD2  . LYS   A 26  ? 0.666166 0.559545 0.579346 -0.0322543  0.00933988  0.168042    38  LYS   B HD2  
387  H HD3  . LYS   A 26  ? 0.620176 0.545026 0.556226 -0.0391947  0.0084736   0.145846    38  LYS   B HD3  
388  H HE2  . LYS   A 26  ? 0.666168 0.562612 0.627161 -0.0700523  0.0180118   0.150495    38  LYS   B HE2  
389  H HE3  . LYS   A 26  ? 0.716576 0.572145 0.65478  -0.0651196  0.0196492   0.172387    38  LYS   B HE3  
390  H HZ1  . LYS   A 26  ? 0.704945 0.64396  0.642474 -0.0654301  0.0324702   0.16764     38  LYS   B HZ1  
391  H HZ2  . LYS   A 26  ? 0.751829 0.653681 0.666886 -0.0626128  0.0344418   0.189689    38  LYS   B HZ2  
392  H HZ3  . LYS   A 26  ? 0.7394   0.649436 0.685431 -0.0849859  0.0400398   0.181445    38  LYS   B HZ3  
393  N N    . ARG   A 27  ? 0.580617 0.421601 0.478315 0.0383647   -0.0291717  0.168608    39  ARG   B N    
394  C CA   . ARG   A 27  ? 0.621482 0.440106 0.502179 0.0614822   -0.0371369  0.182769    39  ARG   B CA   
395  C C    . ARG   A 27  ? 0.648114 0.507726 0.540111 0.0812235   -0.0505677  0.171746    39  ARG   B C    
396  O O    . ARG   A 27  ? 0.599804 0.480666 0.517799 0.0808896   -0.0521223  0.153035    39  ARG   B O    
397  C CB   . ARG   A 27  ? 0.642622 0.413806 0.525088 0.0686972   -0.0369009  0.183779    39  ARG   B CB   
398  C CG   . ARG   A 27  ? 0.722257 0.462548 0.581836 0.0955874   -0.0448323  0.201828    39  ARG   B CG   
399  C CD   . ARG   A 27  ? 0.739095 0.427477 0.598834 0.106711    -0.0453164  0.199431    39  ARG   B CD   
400  N NE   . ARG   A 27  ? 0.76097  0.47669  0.646949 0.121374    -0.0502935  0.176557    39  ARG   B NE   
401  C CZ   . ARG   A 27  ? 0.788893 0.473258 0.681296 0.127032    -0.0483334  0.163952    39  ARG   B CZ   
402  N NH1  . ARG   A 27  ? 0.759485 0.477061 0.67551  0.137046    -0.0490707  0.142919    39  ARG   B NH1  
403  N NH2  . ARG   A 27  ? 0.778183 0.397031 0.652042 0.119693    -0.0445217  0.171981    39  ARG   B NH2  
404  H H    . ARG   A 27  ? 0.56096  0.416778 0.475228 0.037138    -0.0308952  0.154136    39  ARG   B H    
405  H HA   . ARG   A 27  ? 0.655567 0.465006 0.51542  0.0615676   -0.0349904  0.198514    39  ARG   B HA   
406  H HB2  . ARG   A 27  ? 0.663008 0.409382 0.543249 0.0524275   -0.0292303  0.187325    39  ARG   B HB2  
407  H HB3  . ARG   A 27  ? 0.627347 0.410542 0.527494 0.0725675   -0.0392918  0.168419    39  ARG   B HB3  
408  H HG2  . ARG   A 27  ? 0.700296 0.470319 0.563967 0.111674    -0.0536588  0.198345    39  ARG   B HG2  
409  H HG3  . ARG   A 27  ? 0.74102  0.464547 0.579577 0.091227    -0.0413328  0.218897    39  ARG   B HG3  
410  H HD2  . ARG   A 27  ? 0.798697 0.460454 0.639717 0.122961    -0.0494231  0.213758    39  ARG   B HD2  
411  H HD3  . ARG   A 27  ? 0.76456  0.42614  0.623901 0.0881692   -0.037933   0.199149    39  ARG   B HD3  
412  H HE   . ARG   A 27  ? 0.721158 0.476402 0.618563 0.12666     -0.0543383  0.170537    39  ARG   B HE   
413  H HH11 . ARG   A 27  ? 0.718248 0.473257 0.648432 0.128426    -0.0479155  0.134949    39  ARG   B HH11 
414  H HH12 . ARG   A 27  ? 0.777449 0.478301 0.693667 0.152421    -0.0500324  0.13755     39  ARG   B HH12 
415  H HH21 . ARG   A 27  ? 0.83721  0.425657 0.693543 0.130081    -0.0468386  0.186055    39  ARG   B HH21 
416  H HH22 . ARG   A 27  ? 0.79167  0.396518 0.67033  0.104114    -0.0402408  0.163214    39  ARG   B HH22 
417  N N    . VAL   A 28  ? 0.636591 0.508339 0.509245 0.0978238   -0.0604166  0.183527    40  VAL   B N    
418  C CA   . VAL   A 28  ? 0.662069 0.579143 0.548931 0.113735    -0.0755643  0.172368    40  VAL   B CA   
419  C C    . VAL   A 28  ? 0.687592 0.5998   0.591911 0.136366    -0.0821937  0.16922     40  VAL   B C    
420  O O    . VAL   A 28  ? 0.682504 0.552732 0.567955 0.152098    -0.0825696  0.184949    40  VAL   B O    
421  C CB   . VAL   A 28  ? 0.715897 0.649881 0.574478 0.125698    -0.087173   0.18402     40  VAL   B CB   
422  C CG1  . VAL   A 28  ? 0.721327 0.703359 0.596099 0.142467    -0.106921   0.172668    40  VAL   B CG1  
423  C CG2  . VAL   A 28  ? 0.690316 0.633744 0.53046  0.106628    -0.0794938  0.184051    40  VAL   B CG2  
424  H H    . VAL   A 28  ? 0.685446 0.537811 0.535634 0.0987564   -0.0580229  0.198884    40  VAL   B H    
425  H HA   . VAL   A 28  ? 0.624275 0.565647 0.528165 0.102076    -0.0740412  0.158097    40  VAL   B HA   
426  H HB   . VAL   A 28  ? 0.750567 0.655932 0.588171 0.136605    -0.0872351  0.200592    40  VAL   B HB   
427  H HG11 . VAL   A 28  ? 0.680341 0.685651 0.580792 0.132802    -0.106205   0.156826    40  VAL   B HG11 
428  H HG12 . VAL   A 28  ? 0.735863 0.712579 0.613644 0.160775    -0.11335    0.178008    40  VAL   B HG12 
429  H HG13 . VAL   A 28  ? 0.727376 0.722467 0.583651 0.144665    -0.114026   0.175769    40  VAL   B HG13 
430  H HG21 . VAL   A 28  ? 0.719222 0.66853  0.536209 0.115891    -0.0862133  0.192292    40  VAL   B HG21 
431  H HG22 . VAL   A 28  ? 0.702177 0.620863 0.535576 0.0951796   -0.066848   0.191552    40  VAL   B HG22 
432  H HG23 . VAL   A 28  ? 0.660591 0.628936 0.518193 0.0973532   -0.0805172  0.168144    40  VAL   B HG23 
433  N N    . GLY   A 29  ? 0.665904 0.621869 0.603916 0.139341    -0.0873759  0.150385    41  GLY   B N    
434  C CA   . GLY   A 29  ? 0.736132 0.708792 0.697707 0.163184    -0.0938869  0.144348    41  GLY   B CA   
435  C C    . GLY   A 29  ? 0.839465 0.851296 0.805188 0.188194    -0.113404   0.148658    41  GLY   B C    
436  O O    . GLY   A 29  ? 0.709858 0.733452 0.655389 0.187124    -0.1236     0.155951    41  GLY   B O    
437  H H    . GLY   A 29  ? 0.645852 0.62377  0.593135 0.125026    -0.0857782  0.140849    41  GLY   B H    
438  H HA2  . GLY   A 29  ? 0.762189 0.698828 0.71505  0.172243    -0.0895595  0.150256    41  GLY   B HA2  
439  H HA3  . GLY   A 29  ? 0.703963 0.698627 0.688918 0.154979    -0.0895498  0.130564    41  GLY   B HA3  
440  N N    . ASN   A 30  ? 0.894599 0.930455 0.886369 0.213286    -0.119742   0.143439    42  ASN   B N    
441  C CA   . ASN   A 30  ? 0.8074   0.894166 0.814793 0.237504    -0.139971   0.14366     42  ASN   B CA   
442  C C    . ASN   A 30  ? 0.8573   1.01369  0.91452  0.226367    -0.141876   0.122894    42  ASN   B C    
443  O O    . ASN   A 30  ? 0.711878 0.869803 0.78922  0.209554    -0.12589    0.111074    42  ASN   B O    
444  C CB   . ASN   A 30  ? 0.754913 0.826546 0.760798 0.27716     -0.146385   0.153034    42  ASN   B CB   
445  H H    . ASN   A 30  ? 0.856659 0.878349 0.857659 0.216041    -0.111105   0.138763    42  ASN   B H    
446  H HA   . ASN   A 30  ? 0.831906 0.920204 0.818838 0.236004    -0.149171   0.150939    42  ASN   B HA   
449  N N    . GLY   A 31  ? 0.843591 1.05858  0.920978 0.233396    -0.161482   0.118203    43  GLY   B N    
450  C CA   . GLY   A 31  ? 0.806954 1.08997  0.939649 0.23114     -0.163223   0.101636    43  GLY   B CA   
451  C C    . GLY   A 31  ? 0.904092 1.24349  1.05845  0.209697    -0.178682   0.089527    43  GLY   B C    
452  O O    . GLY   A 31  ? 1.20941  1.60354  1.38833  0.225286    -0.199409   0.0864921   43  GLY   B O    
453  H H    . GLY   A 31  ? 0.864333 1.07833  0.921484 0.238843    -0.173706   0.125215    43  GLY   B H    
454  H HA2  . GLY   A 31  ? 0.852664 1.15387  0.999131 0.256849    -0.169722   0.104205    43  GLY   B HA2  
455  H HA3  . GLY   A 31  ? 0.811573 1.08647  0.955846 0.219062    -0.147048   0.0952627   43  GLY   B HA3  
456  N N    . GLU   A 32  ? 0.799736 1.12701  0.947386 0.174895    -0.169737   0.0811763   44  GLU   B N    
457  C CA   . GLU   A 32  ? 0.90917  1.28182  1.07884  0.150103    -0.181824   0.0664457   44  GLU   B CA   
458  C C    . GLU   A 32  ? 0.85201  1.25242  1.06566  0.126488    -0.16549    0.0534743   44  GLU   B C    
459  O O    . GLU   A 32  ? 0.779044 1.19785  1.00508  0.0979798   -0.16918    0.0417275   44  GLU   B O    
460  C CB   . GLU   A 32  ? 0.834688 1.26736  1.02513  0.1621      -0.211012   0.0614254   44  GLU   B CB   
461  H H    . GLU   A 32  ? 0.839447 1.12715  0.967713 0.166479    -0.156187   0.0843779   44  GLU   B H    
462  H HA   . GLU   A 32  ? 0.861884 1.20678  1.00286  0.136225    -0.181288   0.0665737   44  GLU   B HA   
465  N N    . GLU   A 33  ? 0.662229 1.06402  0.896774 0.138452    -0.147559   0.0554055   45  GLU   B N    
466  C CA   . GLU   A 33  ? 0.549818 0.959979 0.809478 0.115579    -0.126349   0.0468746   45  GLU   B CA   
467  C C    . GLU   A 33  ? 0.530071 0.871765 0.749557 0.104233    -0.108007   0.0507043   45  GLU   B C    
468  O O    . GLU   A 33  ? 0.513995 0.811539 0.705441 0.122012    -0.102271   0.0595142   45  GLU   B O    
469  C CB   . GLU   A 33  ? 0.507287 0.959628 0.809975 0.130612    -0.113402   0.0442226   45  GLU   B CB   
470  H H    . GLU   A 33  ? 0.695492 1.09152  0.926193 0.162162    -0.148623   0.062166    45  GLU   B H    
471  H HA   . GLU   A 33  ? 0.546416 0.979739 0.820636 0.0944094   -0.131651   0.0393779   45  GLU   B HA   
474  N N    . THR   A 34  ? 0.50777  0.842288 0.727434 0.0737722   -0.0991301  0.0434308   46  THR   B N    
475  C CA   . THR   A 34  ? 0.467284 0.756876 0.666316 0.0622195   -0.078776   0.0436567   46  THR   B CA   
476  C C    . THR   A 34  ? 0.556155 0.873947 0.787586 0.0566326   -0.0609764  0.0384766   46  THR   B C    
477  O O    . THR   A 34  ? 0.633716 1.00565  0.904786 0.0507331   -0.0635015  0.0338429   46  THR   B O    
478  C CB   . THR   A 34  ? 0.407471 0.672591 0.584303 0.0359722   -0.0810973  0.0395943   46  THR   B CB   
479  O OG1  . THR   A 34  ? 0.355298 0.665371 0.56676  0.0184747   -0.0855539  0.031056    46  THR   B OG1  
480  C CG2  . THR   A 34  ? 0.397812 0.646155 0.544502 0.0392483   -0.097951   0.0428754   46  THR   B CG2  
481  H H    . THR   A 34  ? 0.496365 0.854419 0.728836 0.0597999   -0.107317   0.0377468   46  THR   B H    
482  H HA   . THR   A 34  ? 0.488466 0.746915 0.666731 0.0757442   -0.0755438  0.0495455   46  THR   B HA   
483  H HB   . THR   A 34  ? 0.395468 0.633036 0.559149 0.028542    -0.068937   0.0395242   46  THR   B HB   
485  H HG21 . THR   A 34  ? 0.400691 0.630026 0.531645 0.0248272   -0.0962475  0.0396211   46  THR   B HG21 
486  H HG22 . THR   A 34  ? 0.411214 0.689702 0.571098 0.0417418   -0.111442   0.040309    46  THR   B HG22 
487  H HG23 . THR   A 34  ? 0.414636 0.641041 0.543554 0.0537576   -0.0968383  0.0507736   46  THR   B HG23 
488  N N    . PRO   A 35  ? 0.588196 0.873204 0.804218 0.0556812   -0.0417188  0.0386708   47  PRO   B N    
489  C CA   . PRO   A 35  ? 0.590315 0.902619 0.831565 0.0519708   -0.0230068  0.0348999   47  PRO   B CA   
490  C C    . PRO   A 35  ? 0.665992 0.996342 0.922315 0.0194276   -0.0185987  0.0312273   47  PRO   B C    
491  O O    . PRO   A 35  ? 0.770005 1.06918  1.00331  0.00043472  -0.0245444  0.0302888   47  PRO   B O    
492  C CB   . PRO   A 35  ? 0.544359 0.806163 0.752716 0.0599962   -0.00733084 0.0353653   47  PRO   B CB   
493  C CG   . PRO   A 35  ? 0.464863 0.675642 0.63691  0.0661317   -0.0184708  0.0396818   47  PRO   B CG   
494  C CD   . PRO   A 35  ? 0.560034 0.784346 0.734546 0.057705    -0.0371981  0.0422024   47  PRO   B CD   
495  H HA   . PRO   A 35  ? 0.598588 0.945932 0.864672 0.0667576   -0.0234966  0.0346052   47  PRO   B HA   
496  H HB2  . PRO   A 35  ? 0.528181 0.780798 0.730125 0.044099    0.00199803  0.0337036   47  PRO   B HB2  
497  H HB3  . PRO   A 35  ? 0.54287  0.815185 0.759783 0.0771664   0.00025898  0.0344033   47  PRO   B HB3  
498  H HG2  . PRO   A 35  ? 0.501933 0.682322 0.653424 0.0562678   -0.0129523  0.0387729   47  PRO   B HG2  
499  H HG3  . PRO   A 35  ? 0.518729 0.71895  0.685898 0.0854989   -0.019145   0.041622    47  PRO   B HG3  
500  H HD2  . PRO   A 35  ? 0.534569 0.742831 0.695772 0.0409235   -0.0378268  0.040963    47  PRO   B HD2  
501  H HD3  . PRO   A 35  ? 0.550883 0.760844 0.712901 0.0709543   -0.0453888  0.0470586   47  PRO   B HD3  
502  N N    . MET   A 36  ? 0.641132 1.01862  0.934529 0.0126014   -0.0059274  0.0295538   48  MET   B N    
503  C CA   . MET   A 36  ? 0.609163 0.988869 0.909287 -0.0208561  0.00137245  0.0283147   48  MET   B CA   
504  C C    . MET   A 36  ? 0.526225 0.896146 0.819046 -0.0245452  0.0281053   0.0313348   48  MET   B C    
505  O O    . MET   A 36  ? 0.619901 0.992004 0.909051 -0.00054209 0.0402199   0.0319283   48  MET   B O    
506  C CB   . MET   A 36  ? 0.600033 1.0414   0.949406 -0.0386177  -0.00740667 0.024716    48  MET   B CB   
507  C CG   . MET   A 36  ? 0.632359 1.06483  0.973256 -0.0480406  -0.03399    0.0198157   48  MET   B CG   
508  S SD   . MET   A 36  ? 0.489683 1.00928  0.897024 -0.059067   -0.0476428  0.0136367   48  MET   B SD   
509  C CE   . MET   A 36  ? 0.46153  1.02233  0.888898 -0.0135789  -0.0492273  0.0171925   48  MET   B CE   
510  H H    . MET   A 36  ? 0.640575 1.04712  0.954121 0.0278384   -0.00149395 0.0295847   48  MET   B H    
511  H HA   . MET   A 36  ? 0.595507 0.938979 0.869429 -0.0304047  -0.00582907 0.0277939   48  MET   B HA   
512  H HB2  . MET   A 36  ? 0.605057 1.08663  0.981441 -0.0230446  -0.00694142 0.0246215   48  MET   B HB2  
513  H HB3  . MET   A 36  ? 0.609439 1.05719  0.969083 -0.0591196  0.0041351   0.0254359   48  MET   B HB3  
514  H HG2  . MET   A 36  ? 0.597439 0.999323 0.919632 -0.0665904  -0.0340079  0.0184474   48  MET   B HG2  
515  H HG3  . MET   A 36  ? 0.59408  1.00952  0.915474 -0.0292753  -0.043547   0.021032    48  MET   B HG3  
516  H HE1  . MET   A 36  ? 0.470566 1.07069  0.92271  -0.00980317 -0.0659034  0.0137753   48  MET   B HE1  
517  H HE2  . MET   A 36  ? 0.469691 0.990361 0.862833 0.0040576   -0.0511576  0.0204558   48  MET   B HE2  
518  H HE3  . MET   A 36  ? 0.467668 1.05096  0.914494 -0.00960574 -0.031686   0.0191596   48  MET   B HE3  
519  N N    . ILE   A 37  ? 0.488975 0.845069 0.776446 -0.0539293  0.035788    0.0329697   49  ILE   B N    
520  C CA   . ILE   A 37  ? 0.506173 0.842506 0.775445 -0.0604141  0.0600901   0.0379094   49  ILE   B CA   
521  C C    . ILE   A 37  ? 0.481331 0.869404 0.781839 -0.0479694  0.0810138   0.0398672   49  ILE   B C    
522  O O    . ILE   A 37  ? 0.49741  0.946844 0.847415 -0.0550235  0.0807358   0.0392893   49  ILE   B O    
523  C CB   . ILE   A 37  ? 0.550238 0.872092 0.817788 -0.095648   0.0629737   0.0410011   49  ILE   B CB   
524  C CG1  . ILE   A 37  ? 0.50388  0.778482 0.741646 -0.10313    0.0415872   0.0367777   49  ILE   B CG1  
525  C CG2  . ILE   A 37  ? 0.52931  0.831244 0.775408 -0.102762   0.0896226   0.0492221   49  ILE   B CG2  
526  C CD1  . ILE   A 37  ? 0.511655 0.746002 0.727283 -0.129571   0.0465905   0.040017    49  ILE   B CD1  
527  H H    . ILE   A 37  ? 0.502192 0.859248 0.795405 -0.0698997  0.024913    0.0310063   49  ILE   B H    
528  H HA   . ILE   A 37  ? 0.504529 0.801885 0.740531 -0.0494783  0.0606485   0.0378532   49  ILE   B HA   
529  H HB   . ILE   A 37  ? 0.528187 0.889731 0.831184 -0.108316   0.061262    0.0402347   49  ILE   B HB   
530  H HG12 . ILE   A 37  ? 0.504431 0.752564 0.716703 -0.0863704  0.0383228   0.036022    49  ILE   B HG12 
531  H HG13 . ILE   A 37  ? 0.504484 0.80041  0.761539 -0.106057   0.0268794   0.0323568   49  ILE   B HG13 
532  H HG21 . ILE   A 37  ? 0.553045 0.845891 0.799797 -0.125583   0.0922556   0.0526419   49  ILE   B HG21 
533  H HG22 . ILE   A 37  ? 0.542341 0.805984 0.753368 -0.0910124  0.0898919   0.0491397   49  ILE   B HG22 
534  H HG23 . ILE   A 37  ? 0.543644 0.879961 0.809269 -0.0957263  0.103611    0.0511788   49  ILE   B HG23 
535  H HD11 . ILE   A 37  ? 0.525772 0.78327  0.765972 -0.148208   0.052385    0.0419701   49  ILE   B HD11 
536  H HD12 . ILE   A 37  ? 0.514727 0.725315 0.715874 -0.13293    0.0320227   0.0356843   49  ILE   B HD12 
537  H HD13 . ILE   A 37  ? 0.522747 0.730574 0.712755 -0.124101   0.0582318   0.0444337   49  ILE   B HD13 
538  N N    . GLY   A 38  ? 0.40221  0.768155 0.674276 -0.0293924  0.0987563   0.041038    50  GLY   B N    
539  C CA   . GLY   A 38  ? 0.469863 0.880124 0.763264 -0.0107792  0.12046     0.0411834   50  GLY   B CA   
540  C C    . GLY   A 38  ? 0.461543 0.872941 0.751711 0.0284988   0.113926    0.0342525   50  GLY   B C    
541  O O    . GLY   A 38  ? 0.531482 0.961088 0.822698 0.0510267   0.132658    0.0319548   50  GLY   B O    
542  H H    . GLY   A 38  ? 0.438832 0.760975 0.676068 -0.0274258  0.0970623   0.0409156   50  GLY   B H    
543  H HA2  . GLY   A 38  ? 0.468456 0.860816 0.739146 -0.0130271  0.136915    0.0442137   50  GLY   B HA2  
544  H HA3  . GLY   A 38  ? 0.45221  0.910889 0.784848 -0.0216579  0.124554    0.0429799   50  GLY   B HA3  
545  N N    . ASP   A 39  ? 0.393945 0.787482 0.68047  0.0377654   0.0885735   0.0313205   51  ASP   B N    
546  C CA   . ASP   A 39  ? 0.395996 0.786655 0.680108 0.0738583   0.080977    0.0268982   51  ASP   B CA   
547  C C    . ASP   A 39  ? 0.481496 0.813577 0.716853 0.0921886   0.0893175   0.0227186   51  ASP   B C    
548  O O    . ASP   A 39  ? 0.475679 0.75862  0.673017 0.0774801   0.0904844   0.0231047   51  ASP   B O    
549  C CB   . ASP   A 39  ? 0.442061 0.818288 0.724785 0.0781335   0.0530684   0.0276328   51  ASP   B CB   
550  C CG   . ASP   A 39  ? 0.431158 0.866184 0.760018 0.069253    0.0376897   0.0286617   51  ASP   B CG   
551  O OD1  . ASP   A 39  ? 0.442464 0.934496 0.812263 0.0550214   0.0479316   0.0285417   51  ASP   B OD1  
552  O OD2  . ASP   A 39  ? 0.445367 0.871427 0.769642 0.0763476   0.0153919   0.0296106   51  ASP   B OD2  
553  H H    . ASP   A 39  ? 0.396163 0.776871 0.679554 0.0218271   0.07617     0.0325113   51  ASP   B H    
554  H HA   . ASP   A 39  ? 0.423378 0.85979  0.737758 0.085733    0.0884515   0.0258935   51  ASP   B HA   
555  H HB2  . ASP   A 39  ? 0.423354 0.761024 0.680284 0.0643534   0.046888    0.0288091   51  ASP   B HB2  
556  H HB3  . ASP   A 39  ? 0.440049 0.801729 0.712746 0.101985    0.0494995   0.0261045   51  ASP   B HB3  
557  N N    . LYS   A 40  ? 0.447658 0.785282 0.684405 0.126338    0.0935209   0.0174046   52  LYS   B N    
558  C CA   . LYS   A 40  ? 0.489784 0.767954 0.680631 0.145652    0.0964073   0.0105604   52  LYS   B CA   
559  C C    . LYS   A 40  ? 0.492453 0.722885 0.664154 0.151403    0.0727006   0.0115749   52  LYS   B C    
560  O O    . LYS   A 40  ? 0.473188 0.723146 0.666546 0.167259    0.0604761   0.0142962   52  LYS   B O    
561  C CB   . LYS   A 40  ? 0.56461  0.865738 0.762351 0.180812    0.11282     0.00293405  52  LYS   B CB   
562  C CG   . LYS   A 40  ? 0.641774 0.882107 0.790252 0.20089     0.117526    -0.007598   52  LYS   B CG   
563  C CD   . LYS   A 40  ? 0.800778 1.05901  0.954375 0.241657    0.130355    -0.0171232  52  LYS   B CD   
564  C CE   . LYS   A 40  ? 0.908902 1.09606  1.00943  0.261591    0.129749    -0.0303688  52  LYS   B CE   
565  N NZ   . LYS   A 40  ? 1.0378   1.22878  1.13459  0.305012    0.140385    -0.0423829  52  LYS   B NZ   
566  H H    . LYS   A 40  ? 0.463957 0.842408 0.730663 0.138164    0.0937724   0.0172684   52  LYS   B H    
567  H HA   . LYS   A 40  ? 0.495662 0.750637 0.663249 0.131552    0.103212    0.010293    52  LYS   B HA   
568  H HB2  . LYS   A 40  ? 0.561468 0.90226  0.777162 0.175207    0.129024    0.00423089  52  LYS   B HB2  
569  H HB3  . LYS   A 40  ? 0.565375 0.885999 0.784171 0.197408    0.104507    0.0032375   52  LYS   B HB3  
570  H HG2  . LYS   A 40  ? 0.658497 0.856638 0.788707 0.200548    0.102035    -0.0079402  52  LYS   B HG2  
571  H HG3  . LYS   A 40  ? 0.658464 0.886802 0.787105 0.187844    0.127215    -0.00846566 52  LYS   B HG3  
572  H HD2  . LYS   A 40  ? 0.784008 1.08398  0.953023 0.241798    0.148441    -0.0169791  52  LYS   B HD2  
573  H HD3  . LYS   A 40  ? 0.780898 1.05668  0.957276 0.255784    0.121002    -0.0151652  52  LYS   B HD3  
574  H HE2  . LYS   A 40  ? 0.90601  1.05187  0.992456 0.256978    0.112851    -0.0293772  52  LYS   B HE2  
575  H HE3  . LYS   A 40  ? 0.913626 1.08759  0.991684 0.249086    0.138327    -0.0326693  52  LYS   B HE3  
576  H HZ1  . LYS   A 40  ? 1.01143  1.21245  1.12736  0.319077    0.131678    -0.0400315  52  LYS   B HZ1  
577  H HZ2  . LYS   A 40  ? 1.01293  1.24414  1.1222   0.309971    0.157846    -0.0434265  52  LYS   B HZ2  
578  H HZ3  . LYS   A 40  ? 1.03844  1.18126  1.10054  0.313698    0.138194    -0.0513742  52  LYS   B HZ3  
579  N N    . VAL   A 41  ? 0.47418  0.645511 0.606317 0.139199    0.0667747   0.0102091   53  VAL   B N    
580  C CA   . VAL   A 41  ? 0.507916 0.637352 0.623903 0.137241    0.0467649   0.0138429   53  VAL   B CA   
581  C C    . VAL   A 41  ? 0.585479 0.652954 0.66371  0.151392    0.0450423   0.00646134  53  VAL   B C    
582  O O    . VAL   A 41  ? 0.542907 0.586236 0.595612 0.15057     0.0546721   -0.00236744 53  VAL   B O    
583  C CB   . VAL   A 41  ? 0.510245 0.630907 0.620579 0.105739    0.0378308   0.0197456   53  VAL   B CB   
584  C CG1  . VAL   A 41  ? 0.515705 0.594383 0.606937 0.104617    0.0212981   0.0239629   53  VAL   B CG1  
585  C CG2  . VAL   A 41  ? 0.493305 0.665787 0.638056 0.0906331   0.034855    0.0251857   53  VAL   B CG2  
586  H H    . VAL   A 41  ? 0.490898 0.649522 0.606052 0.131998    0.0757086   0.00738632  53  VAL   B H    
587  H HA   . VAL   A 41  ? 0.514008 0.661185 0.647423 0.148429    0.0394441   0.0172796   53  VAL   B HA   
588  H HB   . VAL   A 41  ? 0.506145 0.612518 0.600573 0.0958175   0.0449262   0.0168537   53  VAL   B HB   
589  H HG11 . VAL   A 41  ? 0.524509 0.605961 0.622728 0.120106    0.0157154   0.0264573   53  VAL   B HG11 
590  H HG12 . VAL   A 41  ? 0.526356 0.570227 0.595308 0.104448    0.0225093   0.0201608   53  VAL   B HG12 
591  H HG13 . VAL   A 41  ? 0.496873 0.580621 0.590501 0.0887354   0.0151643   0.0281081   53  VAL   B HG13 
592  H HG21 . VAL   A 41  ? 0.478241 0.63992  0.615106 0.0722672   0.0301546   0.0272915   53  VAL   B HG21 
593  H HG22 . VAL   A 41  ? 0.490334 0.69194  0.650385 0.0896306   0.0466082   0.0236765   53  VAL   B HG22 
594  H HG23 . VAL   A 41  ? 0.491777 0.678983 0.650652 0.100427    0.0255911   0.0278162   53  VAL   B HG23 
595  N N    . TYR   A 42  ? 0.53172  0.571607 0.604941 0.165605    0.0317548   0.0100032   54  TYR   B N    
596  C CA   . TYR   A 42  ? 0.581218 0.558176 0.621901 0.177527    0.0277233   0.00369815  54  TYR   B CA   
597  C C    . TYR   A 42  ? 0.574829 0.513579 0.601078 0.15727     0.0133574   0.0121786   54  TYR   B C    
598  O O    . TYR   A 42  ? 0.542909 0.491022 0.580569 0.158731    0.00341752  0.0241272   54  TYR   B O    
599  C CB   . TYR   A 42  ? 0.662572 0.631328 0.706656 0.213592    0.0258684   0.00239142  54  TYR   B CB   
600  C CG   . TYR   A 42  ? 0.692835 0.710556 0.758022 0.238456    0.0411425   -0.00517278 54  TYR   B CG   
601  C CD1  . TYR   A 42  ? 0.642612 0.73315  0.749522 0.237652    0.0448416   0.00120157  54  TYR   B CD1  
602  C CD2  . TYR   A 42  ? 0.808577 0.802038 0.851929 0.260827    0.0527355   -0.0199744  54  TYR   B CD2  
603  C CE1  . TYR   A 42  ? 0.685606 0.828817 0.81692  0.257309    0.061477    -0.00499325 54  TYR   B CE1  
604  C CE2  . TYR   A 42  ? 0.827318 0.87013  0.889681 0.28464     0.0699689   -0.026724   54  TYR   B CE2  
605  C CZ   . TYR   A 42  ? 0.729765 0.85011  0.838545 0.281929    0.0751885   -0.0182042  54  TYR   B CZ   
606  O OH   . TYR   A 42  ? 0.843605 1.01969  0.976003 0.302266    0.0943553   -0.0238647  54  TYR   B OH   
607  H H    . TYR   A 42  ? 0.541591 0.600862 0.631142 0.167422    0.0245489   0.0167725   54  TYR   B H    
608  H HA   . TYR   A 42  ? 0.595328 0.558858 0.620254 0.175747    0.0352183   -0.00518125 54  TYR   B HA   
609  H HB2  . TYR   A 42  ? 0.652135 0.628708 0.707155 0.215596    0.0165378   0.0119919   54  TYR   B HB2  
610  H HB3  . TYR   A 42  ? 0.689352 0.610349 0.709476 0.21991     0.0232148   -0.00279316 54  TYR   B HB3  
611  H HD1  . TYR   A 42  ? 0.63176  0.737873 0.751287 0.222467    0.0362032   0.00938026  54  TYR   B HD1  
612  H HD2  . TYR   A 42  ? 0.814394 0.757876 0.8297   0.260349    0.0488244   -0.0260019  54  TYR   B HD2  
613  H HE1  . TYR   A 42  ? 0.658703 0.853947 0.821986 0.254321    0.0633861   -0.00070703 54  TYR   B HE1  
614  H HE2  . TYR   A 42  ? 0.838838 0.8643   0.883184 0.301481    0.0783992   -0.0375601  54  TYR   B HE2  
616  N N    . VAL   A 43  ? 0.540118 0.437011 0.540915 0.14158     0.0119924   0.00587828  55  VAL   B N    
617  C CA   . VAL   A 43  ? 0.553879 0.418645 0.544712 0.122666    0.00055704  0.0142618   55  VAL   B CA   
618  C C    . VAL   A 43  ? 0.58797  0.39228  0.552881 0.121602    -0.00371773 0.00616818  55  VAL   B C    
619  O O    . VAL   A 43  ? 0.599976 0.387556 0.550435 0.133801    0.0014307   -0.00896241 55  VAL   B O    
620  C CB   . VAL   A 43  ? 0.531352 0.41906  0.526755 0.095264    0.00047091  0.0168356   55  VAL   B CB   
621  C CG1  . VAL   A 43  ? 0.498522 0.439588 0.517941 0.0931933   0.0036468   0.0226208   55  VAL   B CG1  
622  C CG2  . VAL   A 43  ? 0.510925 0.385745 0.489563 0.0865387   0.00520495  0.00398916  55  VAL   B CG2  
623  H H    . VAL   A 43  ? 0.561748 0.452486 0.552031 0.142814    0.0181096   -0.00340858 55  VAL   B H    
624  H HA   . VAL   A 43  ? 0.554752 0.423168 0.55282  0.128271    -0.00450298 0.0237448   55  VAL   B HA   
625  H HB   . VAL   A 43  ? 0.521987 0.395087 0.51387  0.0846464   -0.00596225 0.0233377   55  VAL   B HB   
626  H HG11 . VAL   A 43  ? 0.496511 0.455063 0.52038  0.0980362   0.0118547   0.0169187   55  VAL   B HG11 
627  H HG12 . VAL   A 43  ? 0.502264 0.453166 0.531613 0.103187    -0.00024673 0.0286663   55  VAL   B HG12 
628  H HG13 . VAL   A 43  ? 0.47812  0.42622  0.498242 0.0770731   0.00115051  0.0258221   55  VAL   B HG13 
629  H HG21 . VAL   A 43  ? 0.492999 0.387804 0.475969 0.0742093   0.00672986  0.00578864  55  VAL   B HG21 
630  H HG22 . VAL   A 43  ? 0.53303  0.37698  0.499298 0.0804901   -0.00024688 0.00114418  55  VAL   B HG22 
631  H HG23 . VAL   A 43  ? 0.53104  0.408443 0.506001 0.0998175   0.0118673   -0.00324252 55  VAL   B HG23 
632  N N    . HIS   A 44  ? 0.546187 0.319611 0.504952 0.106174    -0.0124934  0.0157959   56  HIS   B N    
633  C CA   . HIS   A 44  ? 0.627563 0.354223 0.568685 0.089884    -0.0175946  0.00830742  56  HIS   B CA   
634  C C    . HIS   A 44  ? 0.572992 0.3231   0.522907 0.0618433   -0.0196148  0.014071    56  HIS   B C    
635  O O    . HIS   A 44  ? 0.531988 0.311979 0.494604 0.0570813   -0.0192398  0.0273171   56  HIS   B O    
636  C CB   . HIS   A 44  ? 0.682553 0.349954 0.609877 0.0936223   -0.0240424  0.0138668   56  HIS   B CB   
637  C CG   . HIS   A 44  ? 0.709221 0.334994 0.618633 0.118208    -0.023917   -3.455e-05  56  HIS   B CG   
638  N ND1  . HIS   A 44  ? 0.743657 0.350953 0.637269 0.117086    -0.0238528  -0.0218867  56  HIS   B ND1  
639  C CD2  . HIS   A 44  ? 0.78349  0.383687 0.685606 0.147663    -0.0240803  0.00267974  56  HIS   B CD2  
640  C CE1  . HIS   A 44  ? 0.854326 0.422356 0.729782 0.144007    -0.0233619  -0.0333194  56  HIS   B CE1  
641  N NE2  . HIS   A 44  ? 0.785295 0.345202 0.665907 0.1637      -0.0235465  -0.0184851  56  HIS   B NE2  
642  H H    . HIS   A 44  ? 0.561297 0.34481  0.527559 0.1052      -0.0152555  0.0273046   56  HIS   B H    
643  H HA   . HIS   A 44  ? 0.622662 0.343685 0.554914 0.0946519   -0.0152005  -0.00518431 56  HIS   B HA   
644  H HB2  . HIS   A 44  ? 0.674045 0.347836 0.606982 0.0986139   -0.0248758  0.0276405   56  HIS   B HB2  
645  H HB3  . HIS   A 44  ? 0.68152  0.330233 0.60534  0.0738638   -0.0278214  0.0140145   56  HIS   B HB3  
647  H HD2  . HIS   A 44  ? 0.768451 0.372067 0.67575  0.156366    -0.0255128  0.0159202   56  HIS   B HD2  
648  H HE1  . HIS   A 44  ? 0.844928 0.392374 0.70442  0.149387    -0.0236786  -0.0494777  56  HIS   B HE1  
650  N N    . TYR   A 45  ? 0.56032  0.298261 0.502384 0.0456795   -0.0226983  0.0023517   57  TYR   B N    
651  C CA   . TYR   A 45  ? 0.536368 0.298523 0.488154 0.0226564   -0.0248838  0.00712669  57  TYR   B CA   
652  C C    . TYR   A 45  ? 0.552408 0.285567 0.498776 0.00397557  -0.0327227  -0.00143028 57  TYR   B C    
653  O O    . TYR   A 45  ? 0.609747 0.311998 0.541116 0.00856082  -0.0369572  -0.0173324  57  TYR   B O    
654  C CB   . TYR   A 45  ? 0.434201 0.239369 0.390555 0.0237223   -0.0198419  0.0034851   57  TYR   B CB   
655  C CG   . TYR   A 45  ? 0.476699 0.274267 0.416696 0.0278682   -0.01958    -0.0139569  57  TYR   B CG   
656  C CD1  . TYR   A 45  ? 0.48808  0.281255 0.422085 0.0131184   -0.027049   -0.0222509  57  TYR   B CD1  
657  C CD2  . TYR   A 45  ? 0.503135 0.293122 0.431123 0.0482968   -0.0132272  -0.0231913  57  TYR   B CD2  
658  C CE1  . TYR   A 45  ? 0.556331 0.341069 0.470219 0.0186285   -0.0289831  -0.0380505  57  TYR   B CE1  
659  C CE2  . TYR   A 45  ? 0.557366 0.338236 0.46385  0.0534718   -0.0125076  -0.03898    57  TYR   B CE2  
660  C CZ   . TYR   A 45  ? 0.533811 0.311203 0.43127  0.0386311   -0.0211721  -0.0461922  57  TYR   B CZ   
661  O OH   . TYR   A 45  ? 0.600921 0.367038 0.471585 0.04473     -0.0234165  -0.0625334  57  TYR   B OH   
662  H H    . TYR   A 45  ? 0.590675 0.306506 0.521104 0.0503534   -0.0240398  -0.00910748 57  TYR   B H    
663  H HA   . TYR   A 45  ? 0.513025 0.281955 0.472352 0.0187251   -0.0246835  0.0198147   57  TYR   B HA   
664  H HB2  . TYR   A 45  ? 0.432588 0.253297 0.395638 0.011378    -0.0213812  0.00835417  57  TYR   B HB2  
665  H HB3  . TYR   A 45  ? 0.444148 0.266    0.406095 0.034438    -0.015255   0.00795591  57  TYR   B HB3  
666  H HD1  . TYR   A 45  ? 0.482548 0.283831 0.426282 0.00028986  -0.0305688  -0.0167204  57  TYR   B HD1  
667  H HD2  . TYR   A 45  ? 0.511329 0.30735  0.445689 0.0600491   -0.00863952 -0.0183986  57  TYR   B HD2  
668  H HE1  . TYR   A 45  ? 0.532512 0.31855  0.443216 0.00954505  -0.0356079  -0.0433334  57  TYR   B HE1  
669  H HE2  . TYR   A 45  ? 0.559181 0.338768 0.456806 0.0684234   -0.00605614 -0.044661   57  TYR   B HE2  
671  N N    . LYS   A 46  ? 0.536841 0.29135  0.49636  -0.0161931  -0.0344883  0.00601502  58  LYS   B N    
672  C CA   . LYS   A 46  ? 0.608237 0.357949 0.573085 -0.0376495  -0.0419337  -0.00122148 58  LYS   B CA   
673  C C    . LYS   A 46  ? 0.543938 0.339559 0.518021 -0.0425242  -0.0412413  -0.00145825 58  LYS   B C    
674  O O    . LYS   A 46  ? 0.500836 0.322468 0.483259 -0.0417327  -0.0353371  0.0113631   58  LYS   B O    
675  C CB   . LYS   A 46  ? 0.550776 0.283462 0.526796 -0.0569223  -0.0420197  0.0128477   58  LYS   B CB   
676  H H    . LYS   A 46  ? 0.525482 0.301802 0.492242 -0.015852   -0.0308776  0.0160004   58  LYS   B H    
677  H HA   . LYS   A 46  ? 0.598988 0.328733 0.553719 -0.0356439  -0.0469939  -0.0146893  58  LYS   B HA   
680  N N    . GLY   A 47  ? 0.528065 0.33138  0.496374 -0.0441145  -0.0479698  -0.0166558  59  GLY   B N    
681  C CA   . GLY   A 47  ? 0.534069 0.375457 0.508001 -0.045438   -0.0479314  -0.015743   59  GLY   B CA   
682  C C    . GLY   A 47  ? 0.558481 0.409055 0.539371 -0.0586162  -0.0596441  -0.0267625  59  GLY   B C    
683  O O    . GLY   A 47  ? 0.698352 0.524107 0.674246 -0.0647811  -0.0687903  -0.039279   59  GLY   B O    
684  H H    . GLY   A 47  ? 0.564325 0.347444 0.523151 -0.043135   -0.0531414  -0.0276141  59  GLY   B H    
685  H HA2  . GLY   A 47  ? 0.508592 0.36588  0.492764 -0.0484051  -0.0432565  -0.00475791 59  GLY   B HA2  
686  H HA3  . GLY   A 47  ? 0.52119  0.366883 0.483565 -0.0339311  -0.0451642  -0.0189949  59  GLY   B HA3  
687  N N    . LYS   A 48  ? 0.464034 0.350186 0.457565 -0.0625903  -0.0605475  -0.0230328  60  LYS   B N    
688  C CA   . LYS   A 48  ? 0.491327 0.395396 0.497834 -0.0740534  -0.0729484  -0.0331086  60  LYS   B CA   
689  C C    . LYS   A 48  ? 0.489424 0.430424 0.500143 -0.0665222  -0.0729256  -0.0303945  60  LYS   B C    
690  O O    . LYS   A 48  ? 0.442223 0.391316 0.450235 -0.0586269  -0.0621453  -0.0189568  60  LYS   B O    
691  C CB   . LYS   A 48  ? 0.529047 0.435407 0.562939 -0.0970454  -0.0737652  -0.0279827  60  LYS   B CB   
692  C CG   . LYS   A 48  ? 0.540279 0.469462 0.591646 -0.102751   -0.0616036  -0.0101203  60  LYS   B CG   
693  C CD   . LYS   A 48  ? 0.554392 0.494391 0.634257 -0.127338   -0.0604398  -0.00380561 60  LYS   B CD   
694  C CE   . LYS   A 48  ? 0.654756 0.62708  0.749721 -0.130699   -0.0469857  0.0132314   60  LYS   B CE   
695  N NZ   . LYS   A 48  ? 0.72087  0.712019 0.84741  -0.156897   -0.0454304  0.0177595   60  LYS   B NZ   
696  H H    . LYS   A 48  ? 0.464588 0.364573 0.459167 -0.0575131  -0.0542236  -0.0150641  60  LYS   B H    
697  H HA   . LYS   A 48  ? 0.51625  0.406267 0.509751 -0.0709751  -0.0809226  -0.0452002  60  LYS   B HA   
698  H HB2  . LYS   A 48  ? 0.536655 0.457546 0.581906 -0.105451   -0.0831921  -0.0364592  60  LYS   B HB2  
699  H HB3  . LYS   A 48  ? 0.554017 0.429978 0.58189  -0.100777   -0.0739221  -0.0292387  60  LYS   B HB3  
700  H HG2  . LYS   A 48  ? 0.531943 0.444509 0.572912 -0.0963209  -0.0541697  -0.00205115 60  LYS   B HG2  
701  H HG3  . LYS   A 48  ? 0.511005 0.466035 0.564004 -0.0952561  -0.0604826  -0.00932098 60  LYS   B HG3  
702  H HD2  . LYS   A 48  ? 0.585146 0.540539 0.677561 -0.135046   -0.0697842  -0.013873   60  LYS   B HD2  
703  H HD3  . LYS   A 48  ? 0.603952 0.512723 0.679782 -0.134632   -0.0598308  -0.00167586 60  LYS   B HD3  
704  H HE2  . LYS   A 48  ? 0.635995 0.591516 0.719435 -0.125965   -0.0390761  0.0235834   60  LYS   B HE2  
705  H HE3  . LYS   A 48  ? 0.612813 0.611111 0.707964 -0.120299   -0.046956   0.0110506   60  LYS   B HE3  
706  H HZ1  . LYS   A 48  ? 0.728137 0.690712 0.853491 -0.16781    -0.0465202  0.0190532   60  LYS   B HZ1  
707  H HZ2  . LYS   A 48  ? 0.700035 0.713453 0.840451 -0.160666   -0.0533958  0.0079834   60  LYS   B HZ2  
708  H HZ3  . LYS   A 48  ? 0.696152 0.705657 0.829525 -0.158517   -0.0353016  0.0291351   60  LYS   B HZ3  
709  N N    . LEU   A 49  ? 0.431728 0.390437 0.444134 -0.0657968  -0.0861942  -0.0421152  61  LEU   B N    
710  C CA   . LEU   A 49  ? 0.497722 0.493676 0.520069 -0.0590113  -0.0879217  -0.0394094  61  LEU   B CA   
711  C C    . LEU   A 49  ? 0.414411 0.437453 0.468087 -0.0715805  -0.0791379  -0.0281152  61  LEU   B C    
712  O O    . LEU   A 49  ? 0.493272 0.515206 0.567342 -0.0906387  -0.0787493  -0.0265892  61  LEU   B O    
713  C CB   . LEU   A 49  ? 0.504857 0.520146 0.529556 -0.0567085  -0.106388   -0.0538871  61  LEU   B CB   
714  C CG   . LEU   A 49  ? 0.530853 0.51907  0.518991 -0.0439328  -0.11613    -0.0658586  61  LEU   B CG   
715  C CD1  . LEU   A 49  ? 0.54705  0.556969 0.533673 -0.0385521  -0.137125   -0.0798745  61  LEU   B CD1  
716  C CD2  . LEU   A 49  ? 0.568252 0.538211 0.524092 -0.0252474  -0.104606   -0.0574648  61  LEU   B CD2  
717  H H    . LEU   A 49  ? 0.48494  0.432099 0.491387 -0.0682541  -0.0950901  -0.0524946  61  LEU   B H    
718  H HA   . LEU   A 49  ? 0.457268 0.447914 0.463007 -0.0465703  -0.0822618  -0.034989   61  LEU   B HA   
719  H HB2  . LEU   A 49  ? 0.513844 0.539037 0.559911 -0.071482   -0.112254   -0.0583227  61  LEU   B HB2  
720  H HB3  . LEU   A 49  ? 0.494482 0.533278 0.524264 -0.048651   -0.10696    -0.0512912  61  LEU   B HB3  
721  H HG   . LEU   A 49  ? 0.552884 0.518621 0.536678 -0.0511383  -0.116589   -0.07064    61  LEU   B HG   
722  H HD11 . LEU   A 49  ? 0.552342 0.577414 0.563431 -0.0527579  -0.145245   -0.0860095  61  LEU   B HD11 
723  H HD12 . LEU   A 49  ? 0.56894  0.558512 0.528408 -0.0306779  -0.142631   -0.0872964  61  LEU   B HD12 
724  H HD13 . LEU   A 49  ? 0.536549 0.565744 0.524248 -0.0282228  -0.137293   -0.0754178  61  LEU   B HD13 
725  H HD21 . LEU   A 49  ? 0.54852  0.502944 0.50277  -0.0279361  -0.0938907  -0.0515532  61  LEU   B HD21 
726  H HD22 . LEU   A 49  ? 0.540567 0.526574 0.500632 -0.0193043  -0.102204   -0.0513336  61  LEU   B HD22 
727  H HD23 . LEU   A 49  ? 0.573351 0.530913 0.505295 -0.0163863  -0.110289   -0.0640871  61  LEU   B HD23 
728  N N    . SER   A 50  ? 0.459276 0.502817 0.513731 -0.0611159  -0.0707813  -0.0195925  62  SER   B N    
729  C CA   . SER   A 50  ? 0.518378 0.583984 0.595815 -0.0714579  -0.0594827  -0.0081033  62  SER   B CA   
730  C C    . SER   A 50  ? 0.521699 0.625486 0.634765 -0.0866429  -0.0650905  -0.0121469  62  SER   B C    
731  O O    . SER   A 50  ? 0.644437 0.758012 0.778695 -0.104242   -0.0563516  -0.00315845 62  SER   B O    
732  C CB   . SER   A 50  ? 0.559277 0.639311 0.628811 -0.0566717  -0.0503513  -0.00105589 62  SER   B CB   
733  O OG   . SER   A 50  ? 0.590272 0.695556 0.662246 -0.0432242  -0.0581951  -0.00882698 62  SER   B OG   
734  H H    . SER   A 50  ? 0.452309 0.494362 0.491823 -0.0481207  -0.0716873  -0.0207622  62  SER   B H    
735  H HA   . SER   A 50  ? 0.517856 0.563489 0.5929   -0.079187   -0.0538857  -0.00215617 62  SER   B HA   
736  H HB2  . SER   A 50  ? 0.549483 0.64294  0.630719 -0.0628888  -0.0421117  0.00650745  62  SER   B HB2  
737  H HB3  . SER   A 50  ? 0.549453 0.607238 0.599461 -0.0495675  -0.047603   0.00104143  62  SER   B HB3  
739  N N    . ASN   A 51  ? 0.524143 0.653033 0.644279 -0.0789822  -0.0789197  -0.0242001  63  ASN   B N    
740  C CA   . ASN   A 51  ? 0.594819 0.767764 0.753686 -0.0930087  -0.0878973  -0.0310349  63  ASN   B CA   
741  C C    . ASN   A 51  ? 0.675198 0.830805 0.841305 -0.112462   -0.102769   -0.0429531  63  ASN   B C    
742  O O    . ASN   A 51  ? 0.772644 0.963492 0.966163 -0.120974   -0.117118   -0.0539787  63  ASN   B O    
743  C CB   . ASN   A 51  ? 0.556237 0.763149 0.718089 -0.0737296  -0.102792   -0.0423493  63  ASN   B CB   
744  H H    . ASN   A 51  ? 0.53622  0.655653 0.636502 -0.0640945  -0.0833847  -0.0281088  63  ASN   B H    
745  H HA   . ASN   A 51  ? 0.578366 0.774233 0.758469 -0.101985   -0.0776358  -0.0228702  63  ASN   B HA   
748  N N    . GLY   A 52  ? 0.699624 0.802499 0.840638 -0.117233   -0.101378   -0.043011   64  GLY   B N    
749  C CA   . GLY   A 52  ? 0.700814 0.776643 0.838196 -0.130627   -0.1169     -0.0578078  64  GLY   B CA   
750  C C    . GLY   A 52  ? 0.683439 0.731743 0.834147 -0.1563     -0.108125   -0.0495751  64  GLY   B C    
751  O O    . GLY   A 52  ? 0.591226 0.645842 0.751138 -0.160588   -0.0903181  -0.0315047  64  GLY   B O    
752  H H    . GLY   A 52  ? 0.679813 0.762611 0.805293 -0.111413   -0.090597   -0.0341542  64  GLY   B H    
753  H HA2  . GLY   A 52  ? 0.70644  0.809325 0.861286 -0.135605   -0.129818   -0.067851   64  GLY   B HA2  
754  H HA3  . GLY   A 52  ? 0.706458 0.753614 0.81392  -0.117544   -0.120179   -0.0630369  64  GLY   B HA3  
755  N N    . LYS   A 53  ? 0.78385  0.797749 0.930926 -0.171547   -0.120841   -0.0626894  65  LYS   B N    
756  C CA   . LYS   A 53  ? 0.848761 0.82958  1.008    -0.197885   -0.114614   -0.0553082  65  LYS   B CA   
757  C C    . LYS   A 53  ? 0.877226 0.789119 0.996466 -0.187721   -0.114361   -0.0592343  65  LYS   B C    
758  O O    . LYS   A 53  ? 0.99658  0.877749 1.1073   -0.188251   -0.0996262  -0.0430555  65  LYS   B O    
759  C CB   . LYS   A 53  ? 0.7302   0.731559 0.929672 -0.231475   -0.127847   -0.0652573  65  LYS   B CB   
760  H H    . LYS   A 53  ? 0.787991 0.796136 0.922429 -0.165011   -0.134013   -0.0766747  65  LYS   B H    
761  H HA   . LYS   A 53  ? 0.79623  0.787475 0.964305 -0.20014    -0.099586   -0.0387045  65  LYS   B HA   
764  N N    . LYS   A 54  ? 0.79888  0.688213 0.890688 -0.174632   -0.129938   -0.0802202  66  LYS   B N    
765  C CA   . LYS   A 54  ? 0.749602 0.576795 0.804853 -0.163734   -0.130185   -0.0875415  66  LYS   B CA   
766  C C    . LYS   A 54  ? 0.72318  0.543357 0.748847 -0.133143   -0.11552    -0.0776969  66  LYS   B C    
767  O O    . LYS   A 54  ? 0.667984 0.519264 0.684682 -0.115122   -0.114043   -0.077259   66  LYS   B O    
768  C CB   . LYS   A 54  ? 0.867664 0.669375 0.900944 -0.161902   -0.151624   -0.115534   66  LYS   B CB   
769  H H    . LYS   A 54  ? 0.794932 0.709484 0.889893 -0.170956   -0.14058    -0.0903604  66  LYS   B H    
770  H HA   . LYS   A 54  ? 0.799464 0.600762 0.861547 -0.177253   -0.12521    -0.0804538  66  LYS   B HA   
773  N N    . PHE   A 55  ? 0.692102 0.466814 0.700824 -0.12684    -0.106124   -0.0713203  67  PHE   B N    
774  C CA   . PHE   A 55  ? 0.753778 0.523168 0.740336 -0.100592   -0.0925766  -0.0623679  67  PHE   B CA   
775  C C    . PHE   A 55  ? 0.71858  0.460549 0.67055  -0.0806077  -0.0979091  -0.0808595  67  PHE   B C    
776  O O    . PHE   A 55  ? 0.794412 0.50114  0.733934 -0.0854991  -0.109567   -0.098216   67  PHE   B O    
777  C CB   . PHE   A 55  ? 0.831245 0.573622 0.818569 -0.0993243  -0.0795898  -0.044437   67  PHE   B CB   
778  C CG   . PHE   A 55  ? 0.888124 0.655123 0.901704 -0.115358   -0.0704463  -0.0228705  67  PHE   B CG   
779  C CD1  . PHE   A 55  ? 0.893796 0.656261 0.92987  -0.143635   -0.073687   -0.0192826  67  PHE   B CD1  
780  C CD2  . PHE   A 55  ? 0.877117 0.673527 0.892395 -0.103241   -0.0582203  -0.00663036 67  PHE   B CD2  
781  C CE1  . PHE   A 55  ? 0.855418 0.643916 0.912961 -0.157298   -0.0622729  0.00157245  67  PHE   B CE1  
782  C CE2  . PHE   A 55  ? 0.806878 0.625082 0.840246 -0.115538   -0.0493415  0.011875    67  PHE   B CE2  
783  C CZ   . PHE   A 55  ? 0.727902 0.541432 0.780991 -0.141667   -0.0499694  0.0169951   67  PHE   B CZ   
784  H H    . PHE   A 55  ? 0.751841 0.498642 0.763898 -0.139249   -0.10868    -0.0726708  67  PHE   B H    
785  H HA   . PHE   A 55  ? 0.701201 0.503958 0.693335 -0.0950646  -0.0883182  -0.055989   67  PHE   B HA   
786  H HB2  . PHE   A 55  ? 0.868169 0.573414 0.848548 -0.103999   -0.0839695  -0.05041    67  PHE   B HB2  
787  H HB3  . PHE   A 55  ? 0.818033 0.560227 0.792088 -0.0811478  -0.0726501  -0.0412183  67  PHE   B HB3  
788  H HD1  . PHE   A 55  ? 0.920425 0.662841 0.956964 -0.154248   -0.0833171  -0.0312454  67  PHE   B HD1  
789  H HD2  . PHE   A 55  ? 0.835923 0.636525 0.838878 -0.0868377  -0.0557528  -0.00848888 67  PHE   B HD2  
790  H HE1  . PHE   A 55  ? 0.856282 0.642426 0.929984 -0.177861   -0.0626719  0.00518836  67  PHE   B HE1  
791  H HE2  . PHE   A 55  ? 0.770653 0.606046 0.80202  -0.106535   -0.0424234  0.020977    67  PHE   B HE2  
792  H HZ   . PHE   A 55  ? 0.765706 0.596606 0.830013 -0.149683   -0.0421574  0.0301479   67  PHE   B HZ   
793  N N    . ASP   A 56  ? 0.667149 0.42353  0.602628 -0.0582065  -0.0876888  -0.076351   68  ASP   B N    
794  C CA   . ASP   A 56  ? 0.633719 0.362613 0.539249 -0.0356638  -0.0818867  -0.0842121  68  ASP   B CA   
795  C C    . ASP   A 56  ? 0.656134 0.368352 0.568868 -0.029713   -0.069563   -0.0691106  68  ASP   B C    
796  O O    . ASP   A 56  ? 0.584926 0.325103 0.513861 -0.0294401  -0.0597911  -0.0509297  68  ASP   B O    
797  C CB   . ASP   A 56  ? 0.614103 0.370448 0.503074 -0.0179934  -0.0746655  -0.0834034  68  ASP   B CB   
798  C CG   . ASP   A 56  ? 0.685356 0.4291   0.551251 0.00573771  -0.061452   -0.0849513  68  ASP   B CG   
799  O OD1  . ASP   A 56  ? 0.704286 0.41374  0.549007 0.015496    -0.0642093  -0.0997912  68  ASP   B OD1  
800  O OD2  . ASP   A 56  ? 0.578872 0.347793 0.448888 0.0144765   -0.048145   -0.0721364  68  ASP   B OD2  
801  H H    . ASP   A 56  ? 0.629095 0.41441  0.572981 -0.0571361  -0.083572   -0.0680638  68  ASP   B H    
802  H HA   . ASP   A 56  ? 0.685703 0.388763 0.577677 -0.0363195  -0.0907337  -0.0990988  68  ASP   B HA   
803  H HB2  . ASP   A 56  ? 0.635865 0.396271 0.514315 -0.0189129  -0.0838748  -0.0940036  68  ASP   B HB2  
804  H HB3  . ASP   A 56  ? 0.592887 0.374631 0.496592 -0.0211418  -0.069328   -0.0708698  68  ASP   B HB3  
805  N N    . SER   A 57  ? 0.688164 0.354502 0.585351 -0.0214415  -0.0707523  -0.077545   69  SER   B N    
806  C CA   . SER   A 57  ? 0.784836 0.433036 0.68619  -0.0110794  -0.0607761  -0.0629071  69  SER   B CA   
807  C C    . SER   A 57  ? 0.815964 0.435774 0.692233 0.0174344   -0.0555803  -0.0739877  69  SER   B C    
808  O O    . SER   A 57  ? 0.856765 0.439797 0.70958  0.0226805   -0.063291   -0.0946881  69  SER   B O    
809  C CB   . SER   A 57  ? 0.969062 0.580062 0.881289 -0.030565   -0.0661014  -0.0550171  69  SER   B CB   
810  O OG   . SER   A 57  ? 0.969024 0.562858 0.881193 -0.0172519  -0.0573882  -0.0384601  69  SER   B OG   
811  H H    . SER   A 57  ? 0.740081 0.385013 0.622567 -0.0207083  -0.0784829  -0.0927478  69  SER   B H    
812  H HA   . SER   A 57  ? 0.748751 0.42728  0.661658 -0.00855568 -0.0532726  -0.0497818  69  SER   B HA   
813  H HB2  . SER   A 57  ? 0.90836  0.540579 0.83793  -0.0485572  -0.0677555  -0.0478109  69  SER   B HB2  
814  H HB3  . SER   A 57  ? 0.968225 0.545635 0.869268 -0.0343946  -0.0742304  -0.0686653  69  SER   B HB3  
816  N N    . SER   A 58  ? 0.730162 0.366219 0.612762 0.0357688   -0.0434424  -0.0605141  70  SER   B N    
817  C CA   . SER   A 58  ? 0.759082 0.378686 0.625348 0.0657289   -0.0359836  -0.0679069  70  SER   B CA   
818  C C    . SER   A 58  ? 0.861222 0.415802 0.712627 0.0717846   -0.0429778  -0.0748649  70  SER   B C    
819  O O    . SER   A 58  ? 0.983877 0.507736 0.811049 0.0948136   -0.0418614  -0.0919455  70  SER   B O    
820  C CB   . SER   A 58  ? 0.702952 0.362759 0.587421 0.0803623   -0.0239653  -0.0509185  70  SER   B CB   
821  O OG   . SER   A 58  ? 0.649937 0.311037 0.553229 0.0691266   -0.0264842  -0.0307726  70  SER   B OG   
822  H H    . SER   A 58  ? 0.714433 0.374986 0.612956 0.0300192   -0.0399853  -0.0467127  70  SER   B H    
823  H HA   . SER   A 58  ? 0.768747 0.393568 0.620275 0.073162    -0.0345005  -0.0807111  70  SER   B HA   
824  H HB2  . SER   A 58  ? 0.719532 0.37073  0.596797 0.10123     -0.0190588  -0.0552424  70  SER   B HB2  
825  H HB3  . SER   A 58  ? 0.665507 0.360518 0.555348 0.0777289   -0.0192018  -0.0494737  70  SER   B HB3  
827  N N    . HIS   A 59  ? 0.887776 0.418081 0.751053 0.0509226   -0.0495385  -0.061811   71  HIS   B N    
828  C CA   . HIS   A 59  ? 0.949832 0.410945 0.798444 0.0538454   -0.055775   -0.064251   71  HIS   B CA   
829  C C    . HIS   A 59  ? 1.00708  0.42258  0.833199 0.0457861   -0.0678303  -0.0910679  71  HIS   B C    
830  O O    . HIS   A 59  ? 1.07641  0.431166 0.878945 0.0603699   -0.0719971  -0.103311   71  HIS   B O    
831  C CB   . HIS   A 59  ? 0.945743 0.38896  0.809965 0.0274641   -0.0589022  -0.0427843  71  HIS   B CB   
832  C CG   . HIS   A 59  ? 0.91732  0.388009 0.794795 0.0382086   -0.0499694  -0.0168173  71  HIS   B CG   
833  N ND1  . HIS   A 59  ? 0.957409 0.40909  0.824375 0.0704624   -0.0461093  -0.0110807  71  HIS   B ND1  
834  C CD2  . HIS   A 59  ? 0.890326 0.409533 0.788672 0.0249618   -0.0452303  0.00214016  71  HIS   B CD2  
835  C CE1  . HIS   A 59  ? 0.986813 0.472928 0.868164 0.0742306   -0.0411661  0.0117327   71  HIS   B CE1  
836  N NE2  . HIS   A 59  ? 0.995267 0.521892 0.894145 0.0466812   -0.0401215  0.0192441   71  HIS   B NE2  
837  H H    . HIS   A 59  ? 0.849374 0.404885 0.72883  0.0349799   -0.0493748  -0.0506666  71  HIS   B H    
838  H HA   . HIS   A 59  ? 0.966397 0.418003 0.807309 0.0785021   -0.0506063  -0.0631205  71  HIS   B HA   
839  H HB2  . HIS   A 59  ? 0.925189 0.389111 0.801685 0.00451991  -0.0621618  -0.0428497  71  HIS   B HB2  
840  H HB3  . HIS   A 59  ? 1.00025  0.391101 0.852214 0.0251853   -0.064183   -0.0465093  71  HIS   B HB3  
842  H HD2  . HIS   A 59  ? 0.878717 0.422152 0.78856  0.0056041   -0.0459869  0.00315057  71  HIS   B HD2  
843  H HE1  . HIS   A 59  ? 0.992462 0.477298 0.871663 0.0946919   -0.039314   0.0198754   71  HIS   B HE1  
845  N N    . ASP   A 60  ? 1.03062  0.474168 0.863311 0.0230234   -0.0751103  -0.100624   72  ASP   B N    
846  C CA   . ASP   A 60  ? 1.27505  0.681678 1.08708  0.0132276   -0.0902091  -0.127994   72  ASP   B CA   
847  C C    . ASP   A 60  ? 1.3185   0.705647 1.09364  0.0475879   -0.0875978  -0.151242   72  ASP   B C    
848  O O    . ASP   A 60  ? 1.46822  0.803204 1.21635  0.0480731   -0.100064   -0.175911   72  ASP   B O    
849  C CB   . ASP   A 60  ? 1.17144  0.61719  1.00069  -0.0164054  -0.10068    -0.132426   72  ASP   B CB   
850  C CG   . ASP   A 60  ? 1.19415  0.640904 1.05565  -0.0531581  -0.106045   -0.117132   72  ASP   B CG   
851  O OD1  . ASP   A 60  ? 1.07728  0.484453 0.943233 -0.0589158  -0.102312   -0.102634   72  ASP   B OD1  
852  O OD2  . ASP   A 60  ? 1.21945  0.708933 1.10107  -0.0743273  -0.112799   -0.118383   72  ASP   B OD2  
853  H H    . ASP   A 60  ? 1.00899  0.494716 0.858549 0.0141465   -0.0717859  -0.0906603  72  ASP   B H    
854  H HA   . ASP   A 60  ? 1.25767  0.619298 1.06788  0.00241956  -0.0965773  -0.128655   72  ASP   B HA   
855  H HB2  . ASP   A 60  ? 1.147    0.638201 0.98293  -0.00986294 -0.0936179  -0.125651   72  ASP   B HB2  
856  H HB3  . ASP   A 60  ? 1.22495  0.653065 1.03692  -0.0173249  -0.111162   -0.1529     72  ASP   B HB3  
857  N N    . ARG   A 61  ? 1.27708  0.706206 1.0511   0.075433    -0.0711258  -0.144064   73  ARG   B N    
858  C CA   . ARG   A 61  ? 1.1933   0.612924 0.935695 0.110895    -0.0630425  -0.162119   73  ARG   B CA   
859  C C    . ARG   A 61  ? 1.17332  0.565792 0.913614 0.140383    -0.0534955  -0.155427   73  ARG   B C    
860  O O    . ARG   A 61  ? 1.21599  0.609124 0.936169 0.174551    -0.0428937  -0.167189   73  ARG   B O    
861  C CB   . ARG   A 61  ? 1.19404  0.682854 0.941398 0.118542    -0.0497719  -0.156202   73  ARG   B CB   
862  C CG   . ARG   A 61  ? 1.11813  0.627901 0.862705 0.0940007   -0.0613584  -0.163142   73  ARG   B CG   
863  C CD   . ARG   A 61  ? 1.0233   0.591598 0.767435 0.101361    -0.0483851  -0.155544   73  ARG   B CD   
864  N NE   . ARG   A 61  ? 1.06439  0.676877 0.843773 0.0988504   -0.0350067  -0.129      73  ARG   B NE   
865  C CZ   . ARG   A 61  ? 0.868292 0.51539  0.674418 0.0765786   -0.0373115  -0.112358   73  ARG   B CZ   
866  N NH1  . ARG   A 61  ? 0.900936 0.543986 0.709928 0.0534025   -0.0528911  -0.117209   73  ARG   B NH1  
867  N NH2  . ARG   A 61  ? 0.773324 0.45954  0.60439  0.0778645   -0.0251172  -0.0922055  73  ARG   B NH2  
868  H H    . ARG   A 61  ? 1.1963   0.663543 0.990839 0.0713996   -0.064187   -0.127401   73  ARG   B H    
869  H HA   . ARG   A 61  ? 1.25977  0.646183 0.978634 0.109769    -0.0729918  -0.182382   73  ARG   B HA   
870  H HB2  . ARG   A 61  ? 1.12626  0.64672  0.897614 0.117157    -0.0416551  -0.137507   73  ARG   B HB2  
871  H HB3  . ARG   A 61  ? 1.18823  0.676891 0.915913 0.141918    -0.0415371  -0.166242   73  ARG   B HB3  
872  H HG2  . ARG   A 61  ? 1.1619   0.641186 0.882178 0.0951313   -0.0712833  -0.182736   73  ARG   B HG2  
873  H HG3  . ARG   A 61  ? 1.0985   0.612364 0.864875 0.0716091   -0.0684868  -0.15341    73  ARG   B HG3  
874  H HD2  . ARG   A 61  ? 1.07925  0.645179 0.800769 0.122193    -0.0402429  -0.165072   73  ARG   B HD2  
875  H HD3  . ARG   A 61  ? 1.04664  0.625146 0.787706 0.0874309   -0.0572739  -0.159379   73  ARG   B HD3  
876  H HE   . ARG   A 61  ? 1.00242  0.619303 0.785137 0.114019    -0.0252134  -0.124614   73  ARG   B HE   
877  H HH11 . ARG   A 61  ? 0.912394 0.529087 0.722753 0.0439128   -0.0624378  -0.12271    73  ARG   B HH11 
878  H HH12 . ARG   A 61  ? 0.867707 0.534963 0.678072 0.0475531   -0.0537572  -0.114816   73  ARG   B HH12 
879  H HH21 . ARG   A 61  ? 0.789925 0.484374 0.622144 0.0928054   -0.0152912  -0.0893524  73  ARG   B HH21 
880  H HH22 . ARG   A 61  ? 0.75746  0.462124 0.604149 0.0639477   -0.0273224  -0.0824938  73  ARG   B HH22 
881  N N    . ASN   A 62  ? 1.08864  0.46329  0.850233 0.128881    -0.0560503  -0.134706   74  ASN   B N    
882  C CA   . ASN   A 62  ? 1.1424   0.487377 0.902592 0.155692    -0.0505732  -0.124654   74  ASN   B CA   
883  C C    . ASN   A 62  ? 1.15038  0.551016 0.91915  0.191339    -0.0332288  -0.119605   74  ASN   B C    
884  O O    . ASN   A 62  ? 1.23035  0.606927 0.98774  0.226385    -0.0283178  -0.123698   74  ASN   B O    
885  C CB   . ASN   A 62  ? 1.1719   0.425487 0.89787  0.165546    -0.06148    -0.144749   74  ASN   B CB   
886  H H    . ASN   A 62  ? 1.09434  0.476461 0.871249 0.103578    -0.0615414  -0.125763   74  ASN   B H    
887  H HA   . ASN   A 62  ? 1.11408  0.461727 0.892223 0.141354    -0.0520262  -0.105844   74  ASN   B HA   
890  N N    . GLU   A 63  ? 1.10955  0.584089 0.898833 0.183884    -0.0236809  -0.111498   75  GLU   B N    
891  C CA   . GLU   A 63  ? 1.09489  0.626696 0.900719 0.211128    -0.00725304 -0.103563   75  GLU   B CA   
892  C C    . GLU   A 63  ? 0.978271 0.577607 0.81803  0.189812    -0.00257044 -0.0826489  75  GLU   B C    
893  O O    . GLU   A 63  ? 0.899544 0.51367  0.740961 0.16162     -0.00672745 -0.0823711  75  GLU   B O    
894  C CB   . GLU   A 63  ? 1.16701  0.717299 0.952594 0.237639    0.00603028  -0.123214   75  GLU   B CB   
895  C CG   . GLU   A 63  ? 1.17206  0.763605 0.952545 0.220739    0.0117297   -0.127836   75  GLU   B CG   
896  C CD   . GLU   A 63  ? 1.28096  0.891698 1.03717  0.248069    0.0282317   -0.144275   75  GLU   B CD   
897  O OE1  . GLU   A 63  ? 1.19026  0.833665 0.938094 0.237108    0.0349016   -0.145342   75  GLU   B OE1  
898  O OE2  . GLU   A 63  ? 1.37132  0.962193 1.11361  0.282296    0.0351874   -0.156019   75  GLU   B OE2  
899  H H    . GLU   A 63  ? 1.07911  0.568262 0.873191 0.161425    -0.0276407  -0.110711   75  GLU   B H    
900  H HA   . GLU   A 63  ? 1.11209  0.628446 0.921684 0.22823     -0.00717045 -0.0975241  75  GLU   B HA   
901  H HB2  . GLU   A 63  ? 1.15613  0.736327 0.955196 0.258491    0.0164107   -0.117551   75  GLU   B HB2  
902  H HB3  . GLU   A 63  ? 1.21727  0.720649 0.976683 0.248902    0.00137506  -0.139424   75  GLU   B HB3  
903  H HG2  . GLU   A 63  ? 1.18922  0.754223 0.956991 0.201946    0.00027404  -0.134642   75  GLU   B HG2  
904  H HG3  . GLU   A 63  ? 1.12901  0.762702 0.934126 0.20878     0.0158434   -0.112386   75  GLU   B HG3  
905  N N    . PRO   A 64  ? 0.874778 0.518744 0.741186 0.205365    0.00572162  -0.0671529  76  PRO   B N    
906  C CA   . PRO   A 64  ? 0.788585 0.492685 0.685602 0.185751    0.00866617  -0.0492126  76  PRO   B CA   
907  C C    . PRO   A 64  ? 0.787709 0.53448  0.684283 0.17777     0.0194362   -0.0559152  76  PRO   B C    
908  O O    . PRO   A 64  ? 0.746545 0.490217 0.623306 0.195396    0.0287165   -0.0716321  76  PRO   B O    
909  C CB   . PRO   A 64  ? 0.819395 0.559585 0.741895 0.208569    0.0133473   -0.0366019  76  PRO   B CB   
910  C CG   . PRO   A 64  ? 0.890673 0.581736 0.795541 0.240342    0.0108717   -0.0443415  76  PRO   B CG   
911  C CD   . PRO   A 64  ? 0.922884 0.563861 0.791767 0.243384    0.011215    -0.0677552  76  PRO   B CD   
912  H HA   . PRO   A 64  ? 0.793068 0.484301 0.692727 0.165103    0.00034051  -0.041438   76  PRO   B HA   
913  H HB2  . PRO   A 64  ? 0.790189 0.574179 0.725524 0.215109    0.0233266   -0.0378466  76  PRO   B HB2  
914  H HB3  . PRO   A 64  ? 0.788935 0.538216 0.72473  0.196805    0.00744797  -0.0229307  76  PRO   B HB3  
915  H HG2  . PRO   A 64  ? 0.886884 0.607089 0.804144 0.263336    0.0177367   -0.0440558  76  PRO   B HG2  
916  H HG3  . PRO   A 64  ? 0.900438 0.561403 0.803041 0.236812    0.00179496  -0.0351328  76  PRO   B HG3  
917  H HD2  . PRO   A 64  ? 0.928978 0.590913 0.794379 0.260721    0.0216622   -0.0777411  76  PRO   B HD2  
918  H HD3  . PRO   A 64  ? 0.969334 0.558687 0.821694 0.25159     0.0040783   -0.0718368  76  PRO   B HD3  
919  N N    . PHE   A 65  ? 0.663547 0.445064 0.577761 0.151969    0.0181531   -0.0436046  77  PHE   B N    
920  C CA   . PHE   A 65  ? 0.624131 0.442262 0.538035 0.140912    0.027195    -0.0449686  77  PHE   B CA   
921  C C    . PHE   A 65  ? 0.602665 0.478218 0.546792 0.147717    0.0390659   -0.0338252  77  PHE   B C    
922  O O    . PHE   A 65  ? 0.532551 0.428204 0.501902 0.141864    0.0334942   -0.0204936  77  PHE   B O    
923  C CB   . PHE   A 65  ? 0.57978  0.396408 0.493426 0.111087    0.0176758   -0.0396549  77  PHE   B CB   
924  C CG   . PHE   A 65  ? 0.558645 0.406037 0.468096 0.101373    0.0259063   -0.039126   77  PHE   B CG   
925  C CD1  . PHE   A 65  ? 0.665976 0.504523 0.546554 0.110036    0.0325423   -0.0521062  77  PHE   B CD1  
926  C CD2  . PHE   A 65  ? 0.559678 0.443551 0.491217 0.0868076   0.0283768   -0.0252912  77  PHE   B CD2  
927  C CE1  . PHE   A 65  ? 0.670893 0.532914 0.543052 0.102139    0.0409316   -0.0485708  77  PHE   B CE1  
928  C CE2  . PHE   A 65  ? 0.565838 0.470905 0.491368 0.0784904   0.0366196   -0.0231515  77  PHE   B CE2  
929  C CZ   . PHE   A 65  ? 0.58929  0.482528 0.484433 0.0860889   0.043306    -0.0334844  77  PHE   B CZ   
930  H H    . PHE   A 65  ? 0.663909 0.443414 0.588808 0.141674    0.0114211   -0.0335257  77  PHE   B H    
931  H HA   . PHE   A 65  ? 0.650098 0.45701  0.543844 0.150317    0.0320779   -0.0569667  77  PHE   B HA   
932  H HB2  . PHE   A 65  ? 0.604924 0.388595 0.503157 0.106216    0.00944123  -0.04737    77  PHE   B HB2  
933  H HB3  . PHE   A 65  ? 0.563151 0.38946  0.49396  0.10302     0.0134885   -0.0285888  77  PHE   B HB3  
934  H HD1  . PHE   A 65  ? 0.68154  0.493458 0.54467  0.120513    0.0300274   -0.0634544  77  PHE   B HD1  
935  H HD2  . PHE   A 65  ? 0.538118 0.429073 0.486478 0.0825415   0.0238498   -0.0172959  77  PHE   B HD2  
936  H HE1  . PHE   A 65  ? 0.677633 0.531978 0.526188 0.108596    0.045136    -0.0564728  77  PHE   B HE1  
937  H HE2  . PHE   A 65  ? 0.535922 0.460059 0.474767 0.0677219   0.0370934   -0.0146937  77  PHE   B HE2  
938  H HZ   . PHE   A 65  ? 0.594642 0.499287 0.482605 0.0808242   0.0493451   -0.0302459  77  PHE   B HZ   
939  N N    . VAL   A 66  ? 0.562892 0.463751 0.503072 0.161618    0.055324    -0.0403748  78  VAL   B N    
940  C CA   . VAL   A 66  ? 0.599702 0.560386 0.572585 0.166556    0.0685886   -0.0313168  78  VAL   B CA   
941  C C    . VAL   A 66  ? 0.601989 0.591908 0.57542  0.145145    0.0789979   -0.0259234  78  VAL   B C    
942  O O    . VAL   A 66  ? 0.561498 0.531535 0.502836 0.143381    0.084397    -0.03363    78  VAL   B O    
943  C CB   . VAL   A 66  ? 0.68676  0.659148 0.659126 0.200118    0.0824341   -0.0409034  78  VAL   B CB   
944  C CG1  . VAL   A 66  ? 0.66477  0.709129 0.676037 0.204322    0.0988971   -0.0326655  78  VAL   B CG1  
945  C CG2  . VAL   A 66  ? 0.72863  0.662261 0.696951 0.222554    0.0700334   -0.0450306  78  VAL   B CG2  
946  H H    . VAL   A 66  ? 0.612172 0.494368 0.529202 0.167572    0.0585077   -0.0507432  78  VAL   B H    
947  H HA   . VAL   A 66  ? 0.581622 0.55432  0.57545  0.162847    0.0613349   -0.0227574  78  VAL   B HA   
948  H HB   . VAL   A 66  ? 0.700501 0.655963 0.646711 0.20458     0.0888696   -0.0505547  78  VAL   B HB   
949  H HG11 . VAL   A 66  ? 0.638501 0.702367 0.674245 0.193698    0.0912201   -0.0231695  78  VAL   B HG11 
950  H HG12 . VAL   A 66  ? 0.659393 0.719207 0.665327 0.193807    0.109932    -0.0318491  78  VAL   B HG12 
951  H HG13 . VAL   A 66  ? 0.688574 0.743989 0.705261 0.228245    0.105896    -0.0378684  78  VAL   B HG13 
952  H HG21 . VAL   A 66  ? 0.744295 0.693552 0.719249 0.24613     0.0784327   -0.0492595  78  VAL   B HG21 
953  H HG22 . VAL   A 66  ? 0.749203 0.637185 0.690397 0.221578    0.0634459   -0.0534076  78  VAL   B HG22 
954  H HG23 . VAL   A 66  ? 0.70539  0.643668 0.690646 0.214603    0.0602858   -0.0349526  78  VAL   B HG23 
955  N N    . PHE   A 67  ? 0.521124 0.555066 0.528323 0.13049     0.0809154   -0.0132616  79  PHE   B N    
956  C CA   . PHE   A 67  ? 0.514115 0.574805 0.525097 0.109983    0.0921807   -0.00623113 79  PHE   B CA   
957  C C    . PHE   A 67  ? 0.529284 0.646673 0.58569  0.101683    0.0971738   0.00387382  79  PHE   B C    
958  O O    . PHE   A 67  ? 0.488946 0.620154 0.570097 0.10783     0.0858674   0.00623613  79  PHE   B O    
959  C CB   . PHE   A 67  ? 0.483053 0.514118 0.476258 0.0860654   0.0791578   -0.00263993 79  PHE   B CB   
960  C CG   . PHE   A 67  ? 0.444407 0.480901 0.459741 0.0704663   0.0633826   0.00563162  79  PHE   B CG   
961  C CD1  . PHE   A 67  ? 0.533117 0.548025 0.549738 0.0764258   0.0483042   0.00497133  79  PHE   B CD1  
962  C CD2  . PHE   A 67  ? 0.454465 0.51248  0.484222 0.0495336   0.0639051   0.0140002   79  PHE   B CD2  
963  C CE1  . PHE   A 67  ? 0.483227 0.503541 0.51409  0.0635088   0.0356566   0.0129506   79  PHE   B CE1  
964  C CE2  . PHE   A 67  ? 0.409152 0.469654 0.452868 0.037301    0.0493533   0.0191704   79  PHE   B CE2  
965  C CZ   . PHE   A 67  ? 0.450947 0.495001 0.494486 0.0452319   0.0359684   0.0187843   79  PHE   B CZ   
966  H H    . PHE   A 67  ? 0.523674 0.569105 0.550895 0.133185    0.0742847   -0.00889318 79  PHE   B H    
967  H HA   . PHE   A 67  ? 0.536552 0.59792  0.53141  0.117142    0.10507     -0.0104846  79  PHE   B HA   
968  H HB2  . PHE   A 67  ? 0.484909 0.523317 0.470996 0.076552    0.0876339   0.00054031  79  PHE   B HB2  
969  H HB3  . PHE   A 67  ? 0.499874 0.498325 0.469717 0.0907763   0.0729386   -0.00962382 79  PHE   B HB3  
970  H HD1  . PHE   A 67  ? 0.523114 0.51792  0.528932 0.0894662   0.0471094   -0.00072927 79  PHE   B HD1  
971  H HD2  . PHE   A 67  ? 0.446274 0.515138 0.474002 0.0435942   0.0745905   0.016067    79  PHE   B HD2  
972  H HE1  . PHE   A 67  ? 0.488787 0.494176 0.518446 0.067584    0.0270581   0.0142049   79  PHE   B HE1  
973  H HE2  . PHE   A 67  ? 0.413822 0.48604  0.465456 0.0236876   0.0492191   0.0231477   79  PHE   B HE2  
974  H HZ   . PHE   A 67  ? 0.429862 0.476617 0.48016  0.0380197   0.0271862   0.0226927   79  PHE   B HZ   
975  N N    . SER   A 68  ? 0.506457 0.652962 0.571697 0.0850763   0.112035    0.0104331   80  SER   B N    
976  C CA   . SER   A 68  ? 0.448503 0.647315 0.557536 0.0694785   0.115715    0.019131    80  SER   B CA   
977  C C    . SER   A 68  ? 0.480786 0.664297 0.588828 0.0403996   0.102115    0.0256794   80  SER   B C    
978  O O    . SER   A 68  ? 0.401919 0.555102 0.48056  0.0268545   0.105205    0.0280707   80  SER   B O    
979  C CB   . SER   A 68  ? 0.51744  0.755743 0.63795  0.0655896   0.142352    0.0233438   80  SER   B CB   
980  O OG   . SER   A 68  ? 0.522689 0.781037 0.64482  0.0956907   0.157482    0.0161623   80  SER   B OG   
981  H H    . SER   A 68  ? 0.515287 0.64653  0.55669  0.0825711   0.120006    0.00943466  80  SER   B H    
982  H HA   . SER   A 68  ? 0.469011 0.68832  0.60137  0.0804768   0.109333    0.0179354   80  SER   B HA   
983  H HB2  . SER   A 68  ? 0.510291 0.725711 0.604347 0.0556724   0.148586    0.0258298   80  SER   B HB2  
984  H HB3  . SER   A 68  ? 0.4872   0.760625 0.639872 0.0519031   0.143523    0.0288188   80  SER   B HB3  
986  N N    . LEU   A 69  ? 0.457881 0.663629 0.596371 0.0325965   0.0873122   0.0281892   81  LEU   B N    
987  C CA   . LEU   A 69  ? 0.412781 0.598878 0.545373 0.00979397  0.0724472   0.0314819   81  LEU   B CA   
988  C C    . LEU   A 69  ? 0.478838 0.674915 0.617378 -0.0169622  0.0823665   0.0373399   81  LEU   B C    
989  O O    . LEU   A 69  ? 0.454862 0.695962 0.626989 -0.0259013  0.0934601   0.0405755   81  LEU   B O    
990  C CB   . LEU   A 69  ? 0.430519 0.638904 0.590063 0.0113779   0.0537328   0.0314386   81  LEU   B CB   
991  C CG   . LEU   A 69  ? 0.417253 0.606011 0.568121 -0.00769148 0.0370191   0.0326387   81  LEU   B CG   
992  C CD1  . LEU   A 69  ? 0.427952 0.567382 0.542378 -0.00318763 0.0293355   0.031559    81  LEU   B CD1  
993  C CD2  . LEU   A 69  ? 0.450255 0.66934  0.627617 -0.00780365 0.0197256   0.032346    81  LEU   B CD2  
994  H H    . LEU   A 69  ? 0.448732 0.682587 0.61077  0.0430477   0.0859565   0.0272882   81  LEU   B H    
995  H HA   . LEU   A 69  ? 0.438175 0.587453 0.542931 0.0118309   0.0672089   0.0297122   81  LEU   B HA   
996  H HB2  . LEU   A 69  ? 0.425176 0.623324 0.578601 0.028837    0.0484606   0.0294489   81  LEU   B HB2  
997  H HB3  . LEU   A 69  ? 0.420769 0.669138 0.610185 0.00969192  0.0574872   0.0322903   81  LEU   B HB3  
998  H HG   . LEU   A 69  ? 0.429576 0.618395 0.580473 -0.0245194  0.0424316   0.0341684   81  LEU   B HG   
999  H HD11 . LEU   A 69  ? 0.431251 0.551564 0.527646 -0.00544769 0.0375547   0.0311109   81  LEU   B HD11 
1000 H HD12 . LEU   A 69  ? 0.417787 0.549478 0.528403 -0.012708   0.0196107   0.0320111   81  LEU   B HD12 
1001 H HD13 . LEU   A 69  ? 0.426855 0.560869 0.538792 0.0118037   0.0256814   0.0307554   81  LEU   B HD13 
1002 H HD21 . LEU   A 69  ? 0.438556 0.695345 0.643901 -0.00627277 0.0234762   0.032247    81  LEU   B HD21 
1003 H HD22 . LEU   A 69  ? 0.437847 0.645187 0.606499 0.00637951  0.0118189   0.0325288   81  LEU   B HD22 
1004 H HD23 . LEU   A 69  ? 0.434041 0.646542 0.608131 -0.0230561  0.0124529   0.0319465   81  LEU   B HD23 
1005 N N    . GLY   A 70  ? 0.521557 0.675102 0.628814 -0.0303482  0.0774666   0.0390503   82  GLY   B N    
1006 C CA   . GLY   A 70  ? 0.532903 0.681405 0.639805 -0.0562431  0.0822823   0.0450606   82  GLY   B CA   
1007 C C    . GLY   A 70  ? 0.592253 0.739168 0.68504  -0.0611892  0.106288    0.0522283   82  GLY   B C    
1008 O O    . GLY   A 70  ? 0.662895 0.80768  0.758652 -0.0842896  0.113902    0.0597645   82  GLY   B O    
1009 H H    . GLY   A 70  ? 0.508756 0.634592 0.594221 -0.0225968  0.0706788   0.0363385   82  GLY   B H    
1010 H HA2  . GLY   A 70  ? 0.537157 0.654564 0.623528 -0.0607105  0.0727703   0.0443489   82  GLY   B HA2  
1011 H HA3  . GLY   A 70  ? 0.532259 0.708269 0.667832 -0.0667848  0.0786109   0.0453529   82  GLY   B HA3  
1012 N N    . LYS   A 71  ? 0.537784 0.685734 0.614712 -0.0397537  0.118954    0.050032    83  LYS   B N    
1013 C CA   . LYS   A 71  ? 0.552347 0.703401 0.612318 -0.0399002  0.14387     0.056732    83  LYS   B CA   
1014 C C    . LYS   A 71  ? 0.640325 0.735937 0.644064 -0.0344876  0.142051    0.0573471   83  LYS   B C    
1015 O O    . LYS   A 71  ? 0.687309 0.775431 0.662647 -0.0288991  0.16041     0.061978    83  LYS   B O    
1016 C CB   . LYS   A 71  ? 0.529422 0.721527 0.606838 -0.0181042  0.160218    0.0526057   83  LYS   B CB   
1017 H H    . LYS   A 71  ? 0.540774 0.684891 0.614769 -0.0240769  0.111585    0.0439226   83  LYS   B H    
1018 H HA   . LYS   A 71  ? 0.56914  0.732995 0.643408 -0.0590269  0.151645    0.0642535   83  LYS   B HA   
1021 N N    . GLY   A 72  ? 0.624365 0.68528  0.612805 -0.0354157  0.119964    0.0528508   84  GLY   B N    
1022 C CA   . GLY   A 72  ? 0.764714 0.779047 0.706421 -0.0290933  0.112884    0.0517098   84  GLY   B CA   
1023 C C    . GLY   A 72  ? 0.709826 0.712307 0.623031 -0.00540046 0.114483    0.0426213   84  GLY   B C    
1024 O O    . GLY   A 72  ? 0.698711 0.672085 0.570563 0.00053865  0.115632    0.0431479   84  GLY   B O    
1025 H H    . GLY   A 72  ? 0.628084 0.697495 0.637066 -0.0395035  0.108533    0.050231    84  GLY   B H    
1026 H HA2  . GLY   A 72  ? 0.701274 0.702039 0.644013 -0.0316633  0.0974379   0.0486225   84  GLY   B HA2  
1027 H HA3  . GLY   A 72  ? 0.737833 0.739854 0.66363  -0.0381993  0.121379    0.0598768   84  GLY   B HA3  
1028 N N    . GLN   A 73  ? 0.606618 0.62802  0.53896  0.00940431  0.112498    0.0333297   85  GLN   B N    
1029 C CA   . GLN   A 73  ? 0.553567 0.557684 0.45924  0.0312162   0.110993    0.0216202   85  GLN   B CA   
1030 C C    . GLN   A 73  ? 0.547133 0.520471 0.442294 0.0329616   0.087041    0.0131935   85  GLN   B C    
1031 O O    . GLN   A 73  ? 0.543285 0.493216 0.411637 0.0456554   0.080762    0.00252109  85  GLN   B O    
1032 C CB   . GLN   A 73  ? 0.537492 0.568949 0.46709  0.0482313   0.118429    0.0148606   85  GLN   B CB   
1033 C CG   . GLN   A 73  ? 0.597268 0.671889 0.547563 0.0469299   0.143375    0.022769    85  GLN   B CG   
1034 C CD   . GLN   A 73  ? 0.601888 0.711132 0.583021 0.0660622   0.149369    0.0164225   85  GLN   B CD   
1035 O OE1  . GLN   A 73  ? 0.71467  0.811273 0.701775 0.0793956   0.133714    0.00767086  85  GLN   B OE1  
1036 N NE2  . GLN   A 73  ? 0.634397 0.787621 0.63521  0.0680056   0.172873    0.0217805   85  GLN   B NE2  
1037 H H    . GLN   A 73  ? 0.589961 0.63386  0.551922 0.00618375  0.111051    0.0338802   85  GLN   B H    
1038 H HA   . GLN   A 73  ? 0.591668 0.58516  0.469224 0.0347064   0.120114    0.0229799   85  GLN   B HA   
1039 H HB2  . GLN   A 73  ? 0.530828 0.568989 0.483871 0.0465146   0.10776     0.0139476   85  GLN   B HB2  
1040 H HB3  . GLN   A 73  ? 0.570276 0.5846   0.478298 0.0628272   0.117187    0.00585409  85  GLN   B HB3  
1041 H HG2  . GLN   A 73  ? 0.613303 0.680586 0.537073 0.0507366   0.155791    0.0240311   85  GLN   B HG2  
1042 H HG3  . GLN   A 73  ? 0.573744 0.662324 0.543468 0.0295643   0.144121    0.0313747   85  GLN   B HG3  
1043 H HE21 . GLN   A 73  ? 0.625846 0.805842 0.649899 0.079324    0.176641    0.0188387   85  GLN   B HE21 
1044 H HE22 . GLN   A 73  ? 0.639889 0.796873 0.631193 0.0582207   0.185373    0.0288207   85  GLN   B HE22 
1045 N N    . VAL   A 74  ? 0.467513 0.44193  0.383224 0.0193608   0.0739954   0.0174023   86  VAL   B N    
1046 C CA   . VAL   A 74  ? 0.463648 0.417048 0.375357 0.0186318   0.0543911   0.0117616   86  VAL   B CA   
1047 C C    . VAL   A 74  ? 0.463137 0.409157 0.372202 0.00400581  0.0476298   0.0187954   86  VAL   B C    
1048 O O    . VAL   A 74  ? 0.447259 0.400888 0.359433 -0.00606589 0.0572185   0.0274288   86  VAL   B O    
1049 C CB   . VAL   A 74  ? 0.470531 0.435039 0.411262 0.0210132   0.0462495   0.00987192  86  VAL   B CB   
1050 C CG1  . VAL   A 74  ? 0.472419 0.433183 0.409764 0.0393305   0.0504513   0.00124267  86  VAL   B CG1  
1051 C CG2  . VAL   A 74  ? 0.480223 0.475634 0.45289  0.0116871   0.0499798   0.0181838   86  VAL   B CG2  
1052 H H    . VAL   A 74  ? 0.474189 0.464523 0.407569 0.00971386  0.0779766   0.0238882   86  VAL   B H    
1053 H HA   . VAL   A 74  ? 0.484484 0.420844 0.375217 0.0260263   0.0509093   0.00515026  86  VAL   B HA   
1054 H HB   . VAL   A 74  ? 0.458008 0.410142 0.396821 0.017421    0.0349088   0.0083595   86  VAL   B HB   
1055 H HG11 . VAL   A 74  ? 0.48538  0.462703 0.426705 0.0444546   0.062767    0.00260702  86  VAL   B HG11 
1056 H HG12 . VAL   A 74  ? 0.493616 0.433506 0.409143 0.0437697   0.0469172   -0.00554007 86  VAL   B HG12 
1057 H HG13 . VAL   A 74  ? 0.469038 0.431107 0.421143 0.0419693   0.0441858   0.00097368  86  VAL   B HG13 
1058 H HG21 . VAL   A 74  ? 0.459347 0.459185 0.446229 0.0134658   0.0422792   0.017851    86  VAL   B HG21 
1059 H HG22 . VAL   A 74  ? 0.465887 0.45922  0.43645  0.00055799  0.0484975   0.0223371   86  VAL   B HG22 
1060 H HG23 . VAL   A 74  ? 0.477769 0.490681 0.45828  0.0153681   0.061159    0.019388    86  VAL   B HG23 
1061 N N    . ILE   A 75  ? 0.408115 0.339206 0.312025 0.00320813  0.0319774   0.0146333   87  ILE   B N    
1062 C CA   . ILE   A 75  ? 0.425855 0.349279 0.326247 -0.00571632 0.0244969   0.019072    87  ILE   B CA   
1063 C C    . ILE   A 75  ? 0.391337 0.330425 0.316732 -0.0172842  0.0256688   0.0250455   87  ILE   B C    
1064 O O    . ILE   A 75  ? 0.388124 0.346658 0.337724 -0.0175193  0.0260599   0.0247517   87  ILE   B O    
1065 C CB   . ILE   A 75  ? 0.438318 0.352819 0.335669 -0.00327937 0.00866865  0.0128743   87  ILE   B CB   
1066 C CG1  . ILE   A 75  ? 0.400167 0.323289 0.319075 -0.00353801 0.0029466   0.00952674  87  ILE   B CG1  
1067 C CG2  . ILE   A 75  ? 0.495407 0.393751 0.364306 0.0053629   0.00305637  0.00650168  87  ILE   B CG2  
1068 C CD1  . ILE   A 75  ? 0.39556  0.316361 0.317695 -0.00587343 -0.00974536 0.00610238  87  ILE   B CD1  
1069 H H    . ILE   A 75  ? 0.425729 0.351242 0.328331 0.00866527  0.0261714   0.00857248  87  ILE   B H    
1070 H HA   . ILE   A 75  ? 0.439246 0.352486 0.320801 -0.00547377 0.0289905   0.0220838   87  ILE   B HA   
1071 H HB   . ILE   A 75  ? 0.429398 0.343017 0.32828  -0.0076611  0.00515981  0.0158623   87  ILE   B HB   
1072 H HG12 . ILE   A 75  ? 0.414815 0.33478  0.331108 0.00191472  0.00526412  0.00554335  87  ILE   B HG12 
1073 H HG13 . ILE   A 75  ? 0.39393  0.327954 0.327995 -0.00735418 0.00538398  0.0137039   87  ILE   B HG13 
1074 H HG21 . ILE   A 75  ? 0.478952 0.376561 0.34957  0.00499989  -0.00686813 0.00376457  87  ILE   B HG21 
1075 H HG22 . ILE   A 75  ? 0.492876 0.389514 0.358927 0.010081    0.0039608   0.00101857  87  ILE   B HG22 
1076 H HG23 . ILE   A 75  ? 0.500807 0.391446 0.35204  0.00694617  0.0081604   0.0104848   87  ILE   B HG23 
1077 H HD11 . ILE   A 75  ? 0.39146  0.313178 0.310456 -0.00778597 -0.011909   0.00837188  87  ILE   B HD11 
1078 H HD12 . ILE   A 75  ? 0.384162 0.310748 0.320968 -0.00848581 -0.0114569  0.00738792  87  ILE   B HD12 
1079 H HD13 . ILE   A 75  ? 0.406262 0.319433 0.318802 -0.00257174 -0.0139518  0.00031441  87  ILE   B HD13 
1080 N N    . LYS   A 76  ? 0.413357 0.341482 0.330878 -0.0256855  0.0240893   0.0295134   88  LYS   B N    
1081 C CA   . LYS   A 76  ? 0.450295 0.38758  0.386339 -0.0380475  0.0226477   0.0324532   88  LYS   B CA   
1082 C C    . LYS   A 76  ? 0.420717 0.372793 0.376101 -0.0361546  0.0117247   0.0282432   88  LYS   B C    
1083 O O    . LYS   A 76  ? 0.347042 0.319652 0.324536 -0.0416906  0.0115475   0.0291294   88  LYS   B O    
1084 C CB   . LYS   A 76  ? 0.471498 0.383163 0.389095 -0.0442817  0.018898    0.0349628   88  LYS   B CB   
1085 H H    . LYS   A 76  ? 0.432986 0.345144 0.330846 -0.0228344  0.0228772   0.0300487   88  LYS   B H    
1086 H HA   . LYS   A 76  ? 0.442915 0.393382 0.390654 -0.0433956  0.0309736   0.0354395   88  LYS   B HA   
1089 N N    . ALA   A 77  ? 0.411063 0.355962 0.359204 -0.0284776  0.00321951  0.0244328   89  ALA   B N    
1090 C CA   . ALA   A 77  ? 0.387639 0.344866 0.350627 -0.0277373  -0.00445743 0.0234321   89  ALA   B CA   
1091 C C    . ALA   A 77  ? 0.365791 0.339048 0.346752 -0.0241176  -0.00233666 0.0248657   89  ALA   B C    
1092 O O    . ALA   A 77  ? 0.351864 0.337752 0.345232 -0.0245853  -0.00720718 0.026872    89  ALA   B O    
1093 C CB   . ALA   A 77  ? 0.375392 0.325944 0.330974 -0.0230947  -0.0110762  0.0207027   89  ALA   B CB   
1094 H H    . ALA   A 77  ? 0.417514 0.351219 0.351754 -0.024165   0.00233086  0.0229797   89  ALA   B H    
1095 H HA   . ALA   A 77  ? 0.383015 0.343084 0.348944 -0.0327324  -0.00698901 0.0239329   89  ALA   B HA   
1096 H HB1  . ALA   A 77  ? 0.382288 0.32634  0.328905 -0.0232391  -0.0133877  0.0197386   89  ALA   B HB1  
1097 H HB2  . ALA   A 77  ? 0.382568 0.327894 0.333361 -0.0195683  -0.0102864  0.0187527   89  ALA   B HB2  
1098 H HB3  . ALA   A 77  ? 0.369949 0.328333 0.334286 -0.023198   -0.0139664  0.0217372   89  ALA   B HB3  
1099 N N    . TRP   A 78  ? 0.374165 0.3468   0.354494 -0.0179365  0.00475941  0.0237089   90  TRP   B N    
1100 C CA   . TRP   A 78  ? 0.319431 0.304732 0.315376 -0.010047   0.00663556  0.0243584   90  TRP   B CA   
1101 C C    . TRP   A 78  ? 0.351634 0.363776 0.367871 -0.0137151  0.0111358   0.0273751   90  TRP   B C    
1102 O O    . TRP   A 78  ? 0.35342  0.383835 0.387726 -0.00858346 0.00702336  0.0292692   90  TRP   B O    
1103 C CB   . TRP   A 78  ? 0.349758 0.323069 0.33486  0.00038034  0.0128309   0.0194703   90  TRP   B CB   
1104 C CG   . TRP   A 78  ? 0.391143 0.34309  0.367676 0.00450895  0.00502396  0.015527    90  TRP   B CG   
1105 C CD1  . TRP   A 78  ? 0.437268 0.377602 0.40771  -0.00204417 -0.0034975  0.0147022   90  TRP   B CD1  
1106 C CD2  . TRP   A 78  ? 0.398989 0.339473 0.375602 0.0161286   0.00563744  0.0118228   90  TRP   B CD2  
1107 N NE1  . TRP   A 78  ? 0.41991  0.342703 0.388135 0.00078812  -0.00795296 0.0111208   90  TRP   B NE1  
1108 C CE2  . TRP   A 78  ? 0.415227 0.333006 0.384882 0.0122382   -0.00322668 0.00921004  90  TRP   B CE2  
1109 C CE3  . TRP   A 78  ? 0.427391 0.375323 0.410847 0.0298512   0.0127641   0.0104712   90  TRP   B CE3  
1110 C CZ2  . TRP   A 78  ? 0.399566 0.293672 0.365409 0.019487    -0.00587957 0.00516888  90  TRP   B CZ2  
1111 C CZ3  . TRP   A 78  ? 0.438425 0.363512 0.416653 0.0416643   0.00994156  0.00604928  90  TRP   B CZ3  
1112 C CH2  . TRP   A 78  ? 0.409303 0.303635 0.377111 0.0353654   0.00031576  0.00345581  90  TRP   B CH2  
1113 H H    . TRP   A 78  ? 0.37029  0.333493 0.338227 -0.016864   0.0083875   0.0222342   90  TRP   B H    
1114 H HA   . TRP   A 78  ? 0.334032 0.317968 0.333639 -0.00853716 0.00033628  0.0256581   90  TRP   B HA   
1115 H HB2  . TRP   A 78  ? 0.361918 0.329324 0.334453 -0.00139514 0.0172768   0.0181301   90  TRP   B HB2  
1116 H HB3  . TRP   A 78  ? 0.357761 0.343095 0.353176 0.00649552  0.0178112   0.019859    90  TRP   B HB3  
1117 H HD1  . TRP   A 78  ? 0.409791 0.352858 0.377454 -0.00754354 -0.00568788 0.0157326   90  TRP   B HD1  
1118 H HE1  . TRP   A 78  ? 0.421559 0.337981 0.388874 -0.00406819 -0.0128779  0.0102966   90  TRP   B HE1  
1119 H HE3  . TRP   A 78  ? 0.41499  0.38295  0.407338 0.0311885   0.0192996   0.0125003   90  TRP   B HE3  
1120 H HZ2  . TRP   A 78  ? 0.415089 0.293982 0.37828  0.0137472   -0.0116062  0.0038783   90  TRP   B HZ2  
1121 H HZ3  . TRP   A 78  ? 0.442426 0.371715 0.42407  0.0538857   0.0148628   0.004242    90  TRP   B HZ3  
1122 H HH2  . TRP   A 78  ? 0.440983 0.315146 0.403897 0.0422063   -0.00158632 0.00011377  90  TRP   B HH2  
1123 N N    . ASP   A 79  ? 0.338872 0.353793 0.352229 -0.0226134  0.0197495   0.0284555   91  ASP   B N    
1124 C CA   . ASP   A 79  ? 0.373056 0.416096 0.409849 -0.0314362  0.0244088   0.0311508   91  ASP   B CA   
1125 C C    . ASP   A 79  ? 0.345756 0.39865  0.394862 -0.0395284  0.0109687   0.0307254   91  ASP   B C    
1126 O O    . ASP   A 79  ? 0.330612 0.413739 0.40487  -0.0387744  0.00715633  0.0309361   91  ASP   B O    
1127 C CB   . ASP   A 79  ? 0.409833 0.450382 0.44065  -0.0431921  0.0374477   0.0346689   91  ASP   B CB   
1128 C CG   . ASP   A 79  ? 0.403166 0.452367 0.430856 -0.0345278  0.0544329   0.0360087   91  ASP   B CG   
1129 O OD1  . ASP   A 79  ? 0.415618 0.482787 0.456133 -0.0193998  0.056776    0.03289     91  ASP   B OD1  
1130 O OD2  . ASP   A 79  ? 0.457956 0.495407 0.46941  -0.042111   0.0654307   0.0405492   91  ASP   B OD2  
1131 H H    . ASP   A 79  ? 0.359675 0.358651 0.35631  -0.0235599  0.0224912   0.0278883   91  ASP   B H    
1132 H HA   . ASP   A 79  ? 0.365852 0.426555 0.416352 -0.0233129  0.0281181   0.0309787   91  ASP   B HA   
1133 H HB2  . ASP   A 79  ? 0.406472 0.422672 0.416748 -0.0462645  0.0352917   0.0349091   91  ASP   B HB2  
1134 H HB3  . ASP   A 79  ? 0.399321 0.45581  0.447092 -0.0542306  0.037227    0.0361919   91  ASP   B HB3  
1135 N N    . ILE   A 80  ? 0.31127  0.340363 0.341261 -0.0440242  0.0031319   0.0292107   92  ILE   B N    
1136 C CA   . ILE   A 80  ? 0.302521 0.336355 0.335831 -0.0491761  -0.00952716 0.0270223   92  ILE   B CA   
1137 C C    . ILE   A 80  ? 0.316923 0.360813 0.354524 -0.0371297  -0.0178883  0.0284646   92  ILE   B C    
1138 O O    . ILE   A 80  ? 0.358092 0.422545 0.408207 -0.0375542  -0.0269804  0.0280817   92  ILE   B O    
1139 C CB   . ILE   A 80  ? 0.317387 0.322175 0.325948 -0.0529752  -0.013448   0.0243092   92  ILE   B CB   
1140 C CG1  . ILE   A 80  ? 0.36319  0.352776 0.365318 -0.0663372  -0.00791817 0.024303    92  ILE   B CG1  
1141 C CG2  . ILE   A 80  ? 0.346739 0.352834 0.350778 -0.0536726  -0.0258373  0.0203077   92  ILE   B CG2  
1142 C CD1  . ILE   A 80  ? 0.450657 0.405541 0.423429 -0.0631534  -0.00935439 0.0228534   92  ILE   B CD1  
1143 H H    . ILE   A 80  ? 0.322955 0.333192 0.336323 -0.0426122  0.00554304  0.0289618   92  ILE   B H    
1144 H HA   . ILE   A 80  ? 0.312547 0.361358 0.359901 -0.0576478  -0.0104047  0.0262749   92  ILE   B HA   
1145 H HB   . ILE   A 80  ? 0.324073 0.317113 0.321394 -0.0460595  -0.011456   0.024955    92  ILE   B HB   
1146 H HG12 . ILE   A 80  ? 0.376718 0.373697 0.388148 -0.0755602  -0.0124173  0.0220666   92  ILE   B HG12 
1147 H HG13 . ILE   A 80  ? 0.373646 0.368248 0.380823 -0.0674484  0.00108371  0.0276413   92  ILE   B HG13 
1148 H HG21 . ILE   A 80  ? 0.347944 0.336455 0.337505 -0.0559449  -0.0272447  0.0174867   92  ILE   B HG21 
1149 H HG22 . ILE   A 80  ? 0.340543 0.361453 0.357063 -0.0594372  -0.0300319  0.018766    92  ILE   B HG22 
1150 H HG23 . ILE   A 80  ? 0.331097 0.340694 0.333144 -0.0454965  -0.028156   0.0219671   92  ILE   B HG23 
1151 H HD11 . ILE   A 80  ? 0.420296 0.371949 0.386023 -0.0539202  -0.00778524 0.0237306   92  ILE   B HD11 
1152 H HD12 . ILE   A 80  ? 0.443283 0.384134 0.408903 -0.0699103  -0.00441149 0.0249443   92  ILE   B HD12 
1153 H HD13 . ILE   A 80  ? 0.429359 0.379524 0.39709  -0.062898   -0.016923   0.0188821   92  ILE   B HD13 
1154 N N    . GLY   A 81  ? 0.293215 0.320912 0.318747 -0.0275587  -0.0158015  0.03034     93  GLY   B N    
1155 C CA   . GLY   A 81  ? 0.345022 0.373449 0.369511 -0.0184423  -0.0222314  0.0344142   93  GLY   B CA   
1156 C C    . GLY   A 81  ? 0.298312 0.342649 0.338783 -0.00719147 -0.0228423  0.0379655   93  GLY   B C    
1157 O O    . GLY   A 81  ? 0.30609  0.361041 0.34962  -0.001349   -0.0313603  0.0421489   93  GLY   B O    
1158 H H    . GLY   A 81  ? 0.311372 0.326472 0.328447 -0.0272621  -0.010672   0.0294327   93  GLY   B H    
1159 H HA2  . GLY   A 81  ? 0.321009 0.353121 0.341886 -0.0211044  -0.0283903  0.0344036   93  GLY   B HA2  
1160 H HA3  . GLY   A 81  ? 0.321127 0.334145 0.335754 -0.0163564  -0.0203964  0.0350789   93  GLY   B HA3  
1161 N N    . VAL   A 82  ? 0.351319 0.396167 0.398706 -0.00089434 -0.013989   0.0363692   94  VAL   B N    
1162 C CA   . VAL   A 82  ? 0.335094 0.396046 0.398157 0.0138074   -0.0139663  0.038527    94  VAL   B CA   
1163 C C    . VAL   A 82  ? 0.398839 0.500145 0.48734  0.0122004   -0.0193785  0.0386181   94  VAL   B C    
1164 O O    . VAL   A 82  ? 0.378826 0.495343 0.477999 0.0263965   -0.0262378  0.0421198   94  VAL   B O    
1165 C CB   . VAL   A 82  ? 0.369907 0.423746 0.432537 0.0237102   -0.00217945 0.0346248   94  VAL   B CB   
1166 C CG1  . VAL   A 82  ? 0.409621 0.481226 0.48892  0.0432399   -0.00181035 0.0358146   94  VAL   B CG1  
1167 C CG2  . VAL   A 82  ? 0.31922  0.333364 0.357067 0.0238943   -0.00104043 0.0322129   94  VAL   B CG2  
1168 H H    . VAL   A 82  ? 0.333371 0.368587 0.374105 -0.00429854 -0.00805885 0.0336708   94  VAL   B H    
1169 H HA   . VAL   A 82  ? 0.362165 0.411713 0.418432 0.0204595   -0.0190922  0.0424489   94  VAL   B HA   
1170 H HB   . VAL   A 82  ? 0.3542   0.418786 0.421202 0.01673     0.00450202  0.0322099   94  VAL   B HB   
1171 H HG11 . VAL   A 82  ? 0.405222 0.472079 0.482997 0.0490216   -0.0101238  0.0402247   94  VAL   B HG11 
1172 H HG12 . VAL   A 82  ? 0.395075 0.497046 0.493347 0.0419604   0.00047817  0.0352011   94  VAL   B HG12 
1173 H HG13 . VAL   A 82  ? 0.412055 0.469545 0.48413  0.0522176   0.0043183   0.0326817   94  VAL   B HG13 
1174 H HG21 . VAL   A 82  ? 0.347188 0.354406 0.381981 0.0323067   0.00454585  0.0285495   94  VAL   B HG21 
1175 H HG22 . VAL   A 82  ? 0.32949  0.337794 0.359083 0.0137149   -0.00012853 0.0305177   94  VAL   B HG22 
1176 H HG23 . VAL   A 82  ? 0.339813 0.341874 0.373041 0.0259826   -0.00712017 0.0358292   94  VAL   B HG23 
1177 N N    . ALA   A 83  ? 0.323912 0.440493 0.421367 -0.00505286 -0.0181407  0.0349407   95  ALA   B N    
1178 C CA   . ALA   A 83  ? 0.327433 0.482436 0.450967 -0.0121227  -0.0260864  0.0330667   95  ALA   B CA   
1179 C C    . ALA   A 83  ? 0.297624 0.457362 0.415398 -0.00851704 -0.0440116  0.0340319   95  ALA   B C    
1180 O O    . ALA   A 83  ? 0.342307 0.538571 0.483152 -0.00594412 -0.0542605  0.0327265   95  ALA   B O    
1181 C CB   . ALA   A 83  ? 0.309252 0.468152 0.43896  -0.0357663  -0.0212758  0.0289474   95  ALA   B CB   
1182 H H    . ALA   A 83  ? 0.33885  0.439852 0.425366 -0.013128   -0.0127677  0.0333722   95  ALA   B H    
1183 H HA   . ALA   A 83  ? 0.317842 0.496296 0.460567 -0.00320338 -0.0229111  0.0337603   95  ALA   B HA   
1184 H HB1  . ALA   A 83  ? 0.315657 0.471969 0.446496 -0.0372529  -0.00903392 0.029897    95  ALA   B HB1  
1185 H HB2  . ALA   A 83  ? 0.315848 0.451403 0.426501 -0.0424334  -0.0249363  0.0275346   95  ALA   B HB2  
1186 H HB3  . ALA   A 83  ? 0.315325 0.50172  0.465914 -0.0421901  -0.0269064  0.0268937   95  ALA   B HB3  
1187 N N    . THR   A 84  ? 0.389941 0.517386 0.478246 -0.00582322 -0.0473608  0.0369177   96  THR   B N    
1188 C CA   . THR   A 84  ? 0.372756 0.501435 0.447812 -9.946e-05  -0.0615302  0.0397406   96  THR   B CA   
1189 C C    . THR   A 84  ? 0.419406 0.54371  0.489003 0.0207644   -0.0646961  0.0497715   96  THR   B C    
1190 O O    . THR   A 84  ? 0.368021 0.493641 0.423349 0.0276034   -0.0759593  0.0546384   96  THR   B O    
1191 C CB   . THR   A 84  ? 0.378908 0.478497 0.424141 -0.007174   -0.0613693  0.0390928   96  THR   B CB   
1192 O OG1  . THR   A 84  ? 0.371411 0.443452 0.401667 -0.00113521 -0.0521981  0.0457913   96  THR   B OG1  
1193 C CG2  . THR   A 84  ? 0.373917 0.469496 0.418588 -0.0243498  -0.0601409  0.0295691   96  THR   B CG2  
1194 H H    . THR   A 84  ? 0.357319 0.46276  0.432917 -0.00770959 -0.0402375  0.0372679   96  THR   B H    
1195 H HA   . THR   A 84  ? 0.386077 0.537559 0.473135 -0.00443499 -0.0700812  0.0356713   96  THR   B HA   
1196 H HB   . THR   A 84  ? 0.385889 0.490737 0.422171 -0.00348801 -0.0704821  0.0403089   96  THR   B HB   
1198 H HG21 . THR   A 84  ? 0.378829 0.459681 0.404994 -0.0259302  -0.0617426  0.0281065   96  THR   B HG21 
1199 H HG22 . THR   A 84  ? 0.368166 0.456193 0.417242 -0.0280943  -0.050928   0.029206    96  THR   B HG22 
1200 H HG23 . THR   A 84  ? 0.377831 0.492252 0.435273 -0.0298047  -0.0670757  0.0251854   96  THR   B HG23 
1201 N N    . MET   A 85  ? 0.397481 0.510654 0.472366 0.0319173   -0.0550917  0.053201    97  MET   B N    
1202 C CA   . MET   A 85  ? 0.394914 0.486881 0.457124 0.0504653   -0.0566268  0.0632934   97  MET   B CA   
1203 C C    . MET   A 85  ? 0.397888 0.517145 0.478296 0.0717039   -0.0651417  0.066629    97  MET   B C    
1204 O O    . MET   A 85  ? 0.345065 0.498537 0.454462 0.0732311   -0.0626714  0.0596909   97  MET   B O    
1205 C CB   . MET   A 85  ? 0.37552  0.433325 0.429495 0.0517731   -0.043804   0.0627594   97  MET   B CB   
1206 C CG   . MET   A 85  ? 0.354273 0.385067 0.388903 0.0344061   -0.0383677  0.0614633   97  MET   B CG   
1207 S SD   . MET   A 85  ? 0.40881  0.402406 0.434938 0.036454    -0.0283663  0.058847    97  MET   B SD   
1208 C CE   . MET   A 85  ? 0.396076 0.356064 0.408289 0.05014     -0.0322158  0.0713421   97  MET   B CE   
1209 H H    . MET   A 85  ? 0.389095 0.50544  0.47385  0.0279869   -0.0472048  0.0489889   97  MET   B H    
1210 H HA   . MET   A 85  ? 0.400435 0.480178 0.445012 0.0489188   -0.0610893  0.068518    97  MET   B HA   
1211 H HB2  . MET   A 85  ? 0.370962 0.440355 0.438498 0.0523828   -0.0379865  0.0568377   97  MET   B HB2  
1212 H HB3  . MET   A 85  ? 0.395897 0.437692 0.443231 0.0641045   -0.0451061  0.0687698   97  MET   B HB3  
1213 H HG2  . MET   A 85  ? 0.37224  0.395231 0.394553 0.0332899   -0.0422943  0.0674903   97  MET   B HG2  
1214 H HG3  . MET   A 85  ? 0.350598 0.392676 0.389576 0.0241909   -0.0369084  0.0555526   97  MET   B HG3  
1215 H HE1  . MET   A 85  ? 0.419161 0.356821 0.427539 0.0522196   -0.0284127  0.0683478   97  MET   B HE1  
1216 H HE2  . MET   A 85  ? 0.415959 0.387253 0.433689 0.0629537   -0.0365882  0.0748787   97  MET   B HE2  
1217 H HE3  . MET   A 85  ? 0.410537 0.362356 0.412509 0.0429114   -0.033741   0.0777033   97  MET   B HE3  
1218 N N    . LYS   A 86  ? 0.416656 0.522082 0.480377 0.0886548   -0.0741926  0.0780733   98  LYS   B N    
1219 C CA   . LYS   A 86  ? 0.436482 0.563742 0.514935 0.114654    -0.083232   0.0822708   98  LYS   B CA   
1220 C C    . LYS   A 86  ? 0.44046  0.530855 0.512033 0.132017    -0.0733839  0.0861214   98  LYS   B C    
1221 O O    . LYS   A 86  ? 0.50396  0.547456 0.55307  0.124026    -0.0644455  0.08903     98  LYS   B O    
1222 C CB   . LYS   A 86  ? 0.421613 0.557115 0.483919 0.126765    -0.101305   0.0923663   98  LYS   B CB   
1223 H H    . LYS   A 86  ? 0.426925 0.509443 0.469469 0.0849402   -0.0744565  0.0840139   98  LYS   B H    
1224 H HA   . LYS   A 86  ? 0.411262 0.574687 0.516116 0.113249    -0.0839542  0.0745124   98  LYS   B HA   
1227 N N    . LYS   A 87  ? 0.480999 0.590851 0.571164 0.157665    -0.0761669  0.0856349   99  LYS   B N    
1228 C CA   . LYS   A 87  ? 0.506139 0.575179 0.58517  0.178431    -0.0687111  0.0878476   99  LYS   B CA   
1229 C C    . LYS   A 87  ? 0.552052 0.562554 0.592899 0.183857    -0.0735136  0.103582    99  LYS   B C    
1230 O O    . LYS   A 87  ? 0.550791 0.567063 0.580003 0.192291    -0.0864983  0.115668    99  LYS   B O    
1231 C CB   . LYS   A 87  ? 0.566636 0.669549 0.671144 0.211178    -0.0724881  0.0853671   99  LYS   B CB   
1232 C CG   . LYS   A 87  ? 0.588034 0.649909 0.68226  0.235803    -0.0630893  0.0827281   99  LYS   B CG   
1233 C CD   . LYS   A 87  ? 0.6685   0.771245 0.791503 0.271241    -0.064064   0.0777391   99  LYS   B CD   
1234 C CE   . LYS   A 87  ? 0.689135 0.732566 0.786619 0.303109    -0.0627989  0.0807502   99  LYS   B CE   
1235 N NZ   . LYS   A 87  ? 0.764049 0.845855 0.887091 0.343616    -0.0649788  0.0767571   99  LYS   B NZ   
1236 H H    . LYS   A 87  ? 0.467561 0.616999 0.578116 0.163027    -0.083247   0.0830785   99  LYS   B H    
1237 H HA   . LYS   A 87  ? 0.50501  0.560638 0.583516 0.167859    -0.0575871  0.0805328   99  LYS   B HA   
1238 H HB2  . LYS   A 87  ? 0.528296 0.675539 0.660202 0.205218    -0.0694848  0.0769597   99  LYS   B HB2  
1239 H HB3  . LYS   A 87  ? 0.568679 0.680544 0.670574 0.224143    -0.0849849  0.0933824   99  LYS   B HB3  
1240 H HG2  . LYS   A 87  ? 0.634833 0.651365 0.702926 0.241787    -0.0671404  0.0919535   99  LYS   B HG2  
1241 H HG3  . LYS   A 87  ? 0.593285 0.64212  0.684915 0.22249     -0.0517752  0.0747628   99  LYS   B HG3  
1242 H HD2  . LYS   A 87  ? 0.623469 0.75697  0.767718 0.265848    -0.0537532  0.0674568   99  LYS   B HD2  
1243 H HD3  . LYS   A 87  ? 0.643359 0.780974 0.780192 0.279425    -0.0759364  0.0825543   99  LYS   B HD3  
1244 H HE2  . LYS   A 87  ? 0.732905 0.739759 0.806433 0.305246    -0.0713375  0.0924529   99  LYS   B HE2  
1245 H HE3  . LYS   A 87  ? 0.712444 0.724508 0.797888 0.295435    -0.0520253  0.0736581   99  LYS   B HE3  
1246 H HZ1  . LYS   A 87  ? 0.750842 0.85677  0.88211  0.353728    -0.077229   0.0840284   99  LYS   B HZ1  
1247 H HZ2  . LYS   A 87  ? 0.723629 0.846608 0.871851 0.340579    -0.0563714  0.0670604   99  LYS   B HZ2  
1248 H HZ3  . LYS   A 87  ? 0.782854 0.82388  0.888274 0.362581    -0.0627587  0.0765604   99  LYS   B HZ3  
1249 N N    . GLY   A 88  ? 0.546813 0.501185 0.567719 0.179056    -0.0632585  0.103408    100 GLY   B N    
1250 C CA   . GLY   A 88  ? 0.5932   0.486501 0.579795 0.178566    -0.0646404  0.118903    100 GLY   B CA   
1251 C C    . GLY   A 88  ? 0.591271 0.474007 0.563616 0.146493    -0.0604809  0.123572    100 GLY   B C    
1252 O O    . GLY   A 88  ? 0.640273 0.476471 0.587481 0.139212    -0.0582062  0.136751    100 GLY   B O    
1253 H H    . GLY   A 88  ? 0.542513 0.496776 0.571407 0.174989    -0.0551733  0.0932477   100 GLY   B H    
1254 H HA2  . GLY   A 88  ? 0.617892 0.475989 0.59734  0.183954    -0.0596015  0.115975    100 GLY   B HA2  
1255 H HA3  . GLY   A 88  ? 0.619995 0.512922 0.598948 0.195072    -0.0732546  0.129609    100 GLY   B HA3  
1256 N N    . GLU   A 89  ? 0.536392 0.461994 0.525073 0.127644    -0.0588053  0.113332    101 GLU   B N    
1257 C CA   . GLU   A 89  ? 0.549872 0.472262 0.525991 0.102057    -0.0554877  0.116743    101 GLU   B CA   
1258 C C    . GLU   A 89  ? 0.540338 0.42908  0.511975 0.0836706   -0.0445778  0.111317    101 GLU   B C    
1259 O O    . GLU   A 89  ? 0.588125 0.477309 0.572388 0.0834615   -0.0396391  0.097179    101 GLU   B O    
1260 C CB   . GLU   A 89  ? 0.505461 0.47803  0.497658 0.0913066   -0.0590092  0.106664    101 GLU   B CB   
1261 C CG   . GLU   A 89  ? 0.539281 0.511806 0.517903 0.0698593   -0.0559399  0.107884    101 GLU   B CG   
1262 C CD   . GLU   A 89  ? 0.47593  0.488833 0.468032 0.059751    -0.0600179  0.095458    101 GLU   B CD   
1263 O OE1  . GLU   A 89  ? 0.424401 0.467671 0.425918 0.0702437   -0.0713789  0.0942837   101 GLU   B OE1  
1264 O OE2  . GLU   A 89  ? 0.418778 0.431301 0.410314 0.0419285   -0.0534384  0.0875688   101 GLU   B OE2  
1265 H H    . GLU   A 89  ? 0.524579 0.481061 0.532294 0.130937    -0.059115   0.104184    101 GLU   B H    
1266 H HA   . GLU   A 89  ? 0.564567 0.473341 0.52332  0.105237    -0.0588781  0.129608    101 GLU   B HA   
1267 H HB2  . GLU   A 89  ? 0.521669 0.516099 0.517739 0.102639    -0.0678339  0.109243    101 GLU   B HB2  
1268 H HB3  . GLU   A 89  ? 0.497503 0.482646 0.505802 0.088056    -0.0548419  0.0958169   101 GLU   B HB3  
1269 H HG2  . GLU   A 89  ? 0.516155 0.469798 0.492708 0.059275    -0.0481828  0.105705    101 GLU   B HG2  
1270 H HG3  . GLU   A 89  ? 0.540814 0.504439 0.50237  0.0732028   -0.0589222  0.119023    101 GLU   B HG3  
1271 N N    . ILE   A 90  ? 0.528665 0.39533  0.483595 0.067309    -0.0407523  0.121557    102 ILE   B N    
1272 C CA   . ILE   A 90  ? 0.513738 0.36403  0.470942 0.0455824   -0.0325573  0.114222    102 ILE   B CA   
1273 C C    . ILE   A 90  ? 0.540933 0.422803 0.500262 0.0290178   -0.0301886  0.112233    102 ILE   B C    
1274 O O    . ILE   A 90  ? 0.552352 0.441528 0.498298 0.0279529   -0.0308044  0.124618    102 ILE   B O    
1275 C CB   . ILE   A 90  ? 0.568217 0.368657 0.510694 0.0371975   -0.0285481  0.125854    102 ILE   B CB   
1276 C CG1  . ILE   A 90  ? 0.632436 0.389149 0.566399 0.05589     -0.0317023  0.128394    102 ILE   B CG1  
1277 C CG2  . ILE   A 90  ? 0.576789 0.36983  0.526723 0.0124788   -0.0225645  0.117146    102 ILE   B CG2  
1278 C CD1  . ILE   A 90  ? 0.609874 0.310021 0.527618 0.0431405   -0.0280219  0.140991    102 ILE   B CD1  
1279 H H    . ILE   A 90  ? 0.548892 0.412987 0.491464 0.0699026   -0.0432034  0.133161    102 ILE   B H    
1280 H HA   . ILE   A 90  ? 0.51556  0.368165 0.482495 0.047238    -0.0315076  0.102334    102 ILE   B HA   
1281 H HB   . ILE   A 90  ? 0.585888 0.38574  0.517394 0.0354007   -0.0279792  0.139195    102 ILE   B HB   
1282 H HG12 . ILE   A 90  ? 0.600594 0.358185 0.543274 0.059976    -0.0316609  0.114662    102 ILE   B HG12 
1283 H HG13 . ILE   A 90  ? 0.619548 0.383408 0.549256 0.0730438   -0.0363731  0.135254    102 ILE   B HG13 
1284 H HG21 . ILE   A 90  ? 0.596361 0.364358 0.539133 0.00307801  -0.0197156  0.126696    102 ILE   B HG21 
1285 H HG22 . ILE   A 90  ? 0.568029 0.3531   0.523632 0.0145315   -0.0235208  0.105067    102 ILE   B HG22 
1286 H HG23 . ILE   A 90  ? 0.542339 0.363964 0.49816  0.00444125  -0.0209418  0.113927    102 ILE   B HG23 
1287 H HD11 . ILE   A 90  ? 0.633944 0.338061 0.544529 0.0339698   -0.025141   0.154082    102 ILE   B HD11 
1288 H HD12 . ILE   A 90  ? 0.66533  0.334917 0.572771 0.0583236   -0.0310262  0.14594     102 ILE   B HD12 
1289 H HD13 . ILE   A 90  ? 0.62566  0.315773 0.54991  0.0290446   -0.0256129  0.131114    102 ILE   B HD13 
1290 N N    . ALA   A 91  ? 0.417537 0.315631 0.389938 0.0189576   -0.0274783  0.096693    103 ALA   B N    
1291 C CA   . ALA   A 91  ? 0.473617 0.397198 0.44715  0.00640505  -0.0255891  0.092798    103 ALA   B CA   
1292 C C    . ALA   A 91  ? 0.400125 0.316311 0.37925  -0.00908867 -0.0204036  0.0847723   103 ALA   B C    
1293 O O    . ALA   A 91  ? 0.455593 0.352498 0.439158 -0.0099142  -0.0201186  0.0769495   103 ALA   B O    
1294 C CB   . ALA   A 91  ? 0.428045 0.382616 0.410732 0.0115943   -0.03007    0.0826373   103 ALA   B CB   
1295 H H    . ALA   A 91  ? 0.452669 0.344249 0.431068 0.0214673   -0.0267895  0.0886324   103 ALA   B H    
1296 H HA   . ALA   A 91  ? 0.449986 0.375137 0.413773 0.0051603   -0.0251486  0.102404    103 ALA   B HA   
1297 H HB1  . ALA   A 91  ? 0.441068 0.403888 0.422467 0.0207262   -0.0349666  0.0871317   103 ALA   B HB1  
1298 H HB2  . ALA   A 91  ? 0.426424 0.380318 0.417539 0.012964    -0.0287869  0.0748648   103 ALA   B HB2  
1299 H HB3  . ALA   A 91  ? 0.420631 0.387334 0.401644 0.00443384  -0.0294122  0.0793351   103 ALA   B HB3  
1300 N N    . HIS   A 92  ? 0.357331 0.288447 0.334636 -0.0194855  -0.0170093  0.0868399   104 HIS   B N    
1301 C CA   . HIS   A 92  ? 0.382534 0.320463 0.368274 -0.0314486  -0.0142782  0.0778812   104 HIS   B CA   
1302 C C    . HIS   A 92  ? 0.380662 0.341506 0.367595 -0.0287616  -0.0162371  0.0665639   104 HIS   B C    
1303 O O    . HIS   A 92  ? 0.36079  0.336673 0.340868 -0.0247646  -0.0170598  0.0683981   104 HIS   B O    
1304 C CB   . HIS   A 92  ? 0.390692 0.333669 0.377486 -0.0437646  -0.00775971 0.0872958   104 HIS   B CB   
1305 C CG   . HIS   A 92  ? 0.473458 0.38795  0.461874 -0.0531525  -0.00508188 0.0969691   104 HIS   B CG   
1306 N ND1  . HIS   A 92  ? 0.54375  0.460568 0.535259 -0.0675187  0.00299756  0.108979    104 HIS   B ND1  
1307 C CD2  . HIS   A 92  ? 0.509814 0.390128 0.496105 -0.0502895  -0.00882514 0.0964916   104 HIS   B CD2  
1308 C CE1  . HIS   A 92  ? 0.579859 0.460597 0.570722 -0.0755981  0.0034277   0.116641    104 HIS   B CE1  
1309 N NE2  . HIS   A 92  ? 0.521779 0.378124 0.508732 -0.0642938  -0.00462442 0.107421    104 HIS   B NE2  
1310 H H    . HIS   A 92  ? 0.379172 0.318199 0.349028 -0.0175029  -0.0166482  0.0940056   104 HIS   B H    
1311 H HA   . HIS   A 92  ? 0.384397 0.307936 0.374453 -0.0331566  -0.0154866  0.0725463   104 HIS   B HA   
1312 H HB2  . HIS   A 92  ? 0.40501  0.358479 0.383316 -0.0402253  -0.00569714 0.0941434   104 HIS   B HB2  
1313 H HB3  . HIS   A 92  ? 0.389779 0.345901 0.384223 -0.0491319  -0.00706847 0.0800998   104 HIS   B HB3  
1315 H HD2  . HIS   A 92  ? 0.496582 0.370392 0.481549 -0.0407789  -0.0129746  0.0893451   104 HIS   B HD2  
1316 H HE1  . HIS   A 92  ? 0.583558 0.457371 0.577477 -0.0883613  0.00904866  0.126054    104 HIS   B HE1  
1318 N N    . LEU   A 93  ? 0.347917 0.307261 0.340119 -0.0307141  -0.0176196  0.0548029   105 LEU   B N    
1319 C CA   . LEU   A 93  ? 0.372149 0.345269 0.362051 -0.0288505  -0.0188901  0.0459956   105 LEU   B CA   
1320 C C    . LEU   A 93  ? 0.342298 0.321485 0.336206 -0.0343297  -0.0189702  0.0403439   105 LEU   B C    
1321 O O    . LEU   A 93  ? 0.38562  0.355463 0.385136 -0.0391116  -0.0208892  0.0363057   105 LEU   B O    
1322 C CB   . LEU   A 93  ? 0.349949 0.317457 0.338866 -0.0239393  -0.019977   0.0386558   105 LEU   B CB   
1323 C CG   . LEU   A 93  ? 0.347095 0.317311 0.339227 -0.0174638  -0.0202271  0.0416774   105 LEU   B CG   
1324 C CD1  . LEU   A 93  ? 0.385502 0.357289 0.38027  -0.0143278  -0.017646   0.0354902   105 LEU   B CD1  
1325 C CD2  . LEU   A 93  ? 0.323907 0.309314 0.313998 -0.017063   -0.0233125  0.045138    105 LEU   B CD2  
1326 H H    . LEU   A 93  ? 0.368969 0.315621 0.363885 -0.0327764  -0.0181278  0.052399    105 LEU   B H    
1327 H HA   . LEU   A 93  ? 0.352692 0.335503 0.338359 -0.0269197  -0.0189474  0.04838     105 LEU   B HA   
1328 H HB2  . LEU   A 93  ? 0.357721 0.315355 0.347236 -0.0246033  -0.0199367  0.0350818   105 LEU   B HB2  
1329 H HB3  . LEU   A 93  ? 0.346254 0.318938 0.331611 -0.0241414  -0.0203892  0.0343893   105 LEU   B HB3  
1330 H HG   . LEU   A 93  ? 0.36118  0.323131 0.35496  -0.0147824  -0.0202121  0.0460359   105 LEU   B HG   
1331 H HD11 . LEU   A 93  ? 0.377865 0.33914  0.369801 -0.0133922  -0.0158845  0.0319444   105 LEU   B HD11 
1332 H HD12 . LEU   A 93  ? 0.374362 0.352399 0.375468 -0.00971537 -0.0176537  0.0377846   105 LEU   B HD12 
1333 H HD13 . LEU   A 93  ? 0.366579 0.343748 0.358869 -0.0175689  -0.0175624  0.0328509   105 LEU   B HD13 
1334 H HD21 . LEU   A 93  ? 0.336222 0.321304 0.322975 -0.0169959  -0.0236281  0.051039    105 LEU   B HD21 
1335 H HD22 . LEU   A 93  ? 0.324624 0.313672 0.310914 -0.0199372  -0.0236317  0.0407486   105 LEU   B HD22 
1336 H HD23 . LEU   A 93  ? 0.33071  0.322549 0.325637 -0.0135674  -0.0249835  0.0456202   105 LEU   B HD23 
1337 N N    . LEU   A 94  ? 0.34349  0.337256 0.333253 -0.0313948  -0.018922   0.0370451   106 LEU   B N    
1338 C CA   . LEU   A 94  ? 0.331867 0.334832 0.325144 -0.031134   -0.0209832  0.029801    106 LEU   B CA   
1339 C C    . LEU   A 94  ? 0.325577 0.322669 0.305855 -0.0230271  -0.0238259  0.0228635   106 LEU   B C    
1340 O O    . LEU   A 94  ? 0.346406 0.343099 0.317727 -0.0194104  -0.0230582  0.0232093   106 LEU   B O    
1341 C CB   . LEU   A 94  ? 0.346912 0.373255 0.347673 -0.0326511  -0.0167744  0.0333149   106 LEU   B CB   
1342 C CG   . LEU   A 94  ? 0.329386 0.374519 0.340865 -0.0311434  -0.0195186  0.0262577   106 LEU   B CG   
1343 C CD1  . LEU   A 94  ? 0.362122 0.40551  0.389043 -0.0423054  -0.0235154  0.0244942   106 LEU   B CD1  
1344 C CD2  . LEU   A 94  ? 0.306276 0.379658 0.324587 -0.0289004  -0.0127357  0.0294569   106 LEU   B CD2  
1345 H H    . LEU   A 94  ? 0.338727 0.336431 0.322709 -0.0283205  -0.0184855  0.0386604   106 LEU   B H    
1346 H HA   . LEU   A 94  ? 0.338353 0.335753 0.336881 -0.0347685  -0.0232312  0.0272763   106 LEU   B HA   
1347 H HB2  . LEU   A 94  ? 0.34524  0.372368 0.352416 -0.0394713  -0.0134494  0.0401874   106 LEU   B HB2  
1348 H HB3  . LEU   A 94  ? 0.339634 0.369609 0.331452 -0.0272211  -0.0150824  0.0339847   106 LEU   B HB3  
1349 H HG   . LEU   A 94  ? 0.331369 0.370426 0.333775 -0.0234207  -0.023604   0.0202064   106 LEU   B HG   
1350 H HD11 . LEU   A 94  ? 0.354388 0.380196 0.373647 -0.0406982  -0.0278334  0.0204815   106 LEU   B HD11 
1351 H HD12 . LEU   A 94  ? 0.352003 0.413315 0.38951  -0.042366   -0.0261262  0.0202419   106 LEU   B HD12 
1352 H HD13 . LEU   A 94  ? 0.35815  0.399684 0.391519 -0.0508985  -0.0194853  0.031297    106 LEU   B HD13 
1353 H HD21 . LEU   A 94  ? 0.315008 0.386184 0.32009  -0.0205153  -0.0114814  0.0283528   106 LEU   B HD21 
1354 H HD22 . LEU   A 94  ? 0.317915 0.395838 0.342723 -0.0370553  -0.00733566 0.0372207   106 LEU   B HD22 
1355 H HD23 . LEU   A 94  ? 0.312664 0.402735 0.341542 -0.0270974  -0.0147607  0.0248387   106 LEU   B HD23 
1356 N N    . ILE   A 95  ? 0.306884 0.296433 0.283588 -0.0206702  -0.0278084  0.0166209   107 ILE   B N    
1357 C CA   . ILE   A 95  ? 0.333803 0.307998 0.294193 -0.0148484  -0.0289221  0.0132349   107 ILE   B CA   
1358 C C    . ILE   A 95  ? 0.357317 0.331674 0.308848 -0.0062929  -0.0341687  0.00793953  107 ILE   B C    
1359 O O    . ILE   A 95  ? 0.386521 0.366806 0.342435 -0.00560334 -0.0393054  0.00403207  107 ILE   B O    
1360 C CB   . ILE   A 95  ? 0.338246 0.298531 0.295285 -0.0170555  -0.0271949  0.0129894   107 ILE   B CB   
1361 C CG1  . ILE   A 95  ? 0.362267 0.323949 0.329787 -0.0214555  -0.0231424  0.0182606   107 ILE   B CG1  
1362 C CG2  . ILE   A 95  ? 0.35589  0.301101 0.295242 -0.0132377  -0.0252045  0.0122828   107 ILE   B CG2  
1363 C CD1  . ILE   A 95  ? 0.376056 0.326867 0.343576 -0.0204011  -0.021087   0.0166535   107 ILE   B CD1  
1364 H H    . ILE   A 95  ? 0.318427 0.311885 0.302046 -0.0232934  -0.0300224  0.0147848   107 ILE   B H    
1365 H HA   . ILE   A 95  ? 0.332438 0.304286 0.288612 -0.0144984  -0.027123   0.014834    107 ILE   B HA   
1366 H HB   . ILE   A 95  ? 0.348613 0.308779 0.307258 -0.017173   -0.0302406  0.00977531  107 ILE   B HB   
1367 H HG12 . ILE   A 95  ? 0.354479 0.317379 0.320532 -0.0214852  -0.0213921  0.0202579   107 ILE   B HG12 
1368 H HG13 . ILE   A 95  ? 0.353207 0.322028 0.328377 -0.0239553  -0.0237436  0.0208668   107 ILE   B HG13 
1369 H HG21 . ILE   A 95  ? 0.356478 0.297087 0.295306 -0.0148548  -0.021259   0.0134313   107 ILE   B HG21 
1370 H HG22 . ILE   A 95  ? 0.354387 0.298437 0.291116 -0.0135186  -0.024455   0.0137089   107 ILE   B HG22 
1371 H HG23 . ILE   A 95  ? 0.362717 0.303538 0.293035 -0.00871864 -0.0285313  0.0094103   107 ILE   B HG23 
1372 H HD11 . ILE   A 95  ? 0.380194 0.326781 0.34681  -0.0209283  -0.0241848  0.0128288   107 ILE   B HD11 
1373 H HD12 . ILE   A 95  ? 0.372962 0.324991 0.347641 -0.0209357  -0.0196136  0.0203303   107 ILE   B HD12 
1374 H HD13 . ILE   A 95  ? 0.3781   0.324688 0.33845  -0.0179867  -0.0182014  0.0155163   107 ILE   B HD13 
1375 N N    . LYS   A 96  ? 0.347097 0.313055 0.284875 0.0011877   -0.0344641  0.00702583  108 LYS   B N    
1376 C CA   . LYS   A 96  ? 0.365408 0.325829 0.289882 0.0139512   -0.0403686  0.00301715  108 LYS   B CA   
1377 C C    . LYS   A 96  ? 0.342898 0.279062 0.247837 0.0152634   -0.0412459  0.00426533  108 LYS   B C    
1378 O O    . LYS   A 96  ? 0.389831 0.314554 0.291999 0.00664225  -0.0351091  0.00783763  108 LYS   B O    
1379 C CB   . LYS   A 96  ? 0.440744 0.388142 0.350589 0.022646    -0.0400318  0.0017087   108 LYS   B CB   
1380 C CG   . LYS   A 96  ? 0.419112 0.390806 0.340336 0.0276868   -0.0385633  -0.00111053 108 LYS   B CG   
1381 C CD   . LYS   A 96  ? 0.449109 0.402372 0.350006 0.0405547   -0.0396843  -0.00588942 108 LYS   B CD   
1382 C CE   . LYS   A 96  ? 0.536839 0.518081 0.447    0.0464344   -0.0356688  -0.00905321 108 LYS   B CE   
1383 N NZ   . LYS   A 96  ? 0.611087 0.567491 0.496939 0.058342    -0.0371548  -0.0159865  108 LYS   B NZ   
1384 H H    . LYS   A 96  ? 0.352314 0.314292 0.287783 -0.00085517 -0.0319058  0.00855212  108 LYS   B H    
1385 H HA   . LYS   A 96  ? 0.363349 0.34228  0.298889 0.0166086   -0.0439471  0.00042396  108 LYS   B HA   
1386 H HB2  . LYS   A 96  ? 0.425613 0.357841 0.329037 0.0163282   -0.0369195  0.00382526  108 LYS   B HB2  
1387 H HB3  . LYS   A 96  ? 0.438145 0.373897 0.334735 0.032176    -0.0438497  0.00034268  108 LYS   B HB3  
1388 H HG2  . LYS   A 96  ? 0.419624 0.411846 0.352321 0.0318381   -0.0405691  -0.00266146 108 LYS   B HG2  
1389 H HG3  . LYS   A 96  ? 0.413117 0.392615 0.343022 0.0188809   -0.0347308  0.00151662  108 LYS   B HG3  
1390 H HD2  . LYS   A 96  ? 0.474955 0.40679  0.365362 0.0343248   -0.0388084  -0.00505752 108 LYS   B HD2  
1391 H HD3  . LYS   A 96  ? 0.481398 0.426322 0.372959 0.0517258   -0.0437568  -0.00789167 108 LYS   B HD3  
1392 H HE2  . LYS   A 96  ? 0.519437 0.523661 0.441175 0.0532231   -0.0358997  -0.0101431  108 LYS   B HE2  
1393 H HE3  . LYS   A 96  ? 0.510169 0.501041 0.42876  0.0362012   -0.0319704  -0.00565265 108 LYS   B HE3  
1394 H HZ1  . LYS   A 96  ? 0.610815 0.553427 0.486662 0.0685199   -0.0407766  -0.0182818  108 LYS   B HZ1  
1395 H HZ2  . LYS   A 96  ? 0.599037 0.536708 0.476791 0.0498659   -0.0375586  -0.0155233  108 LYS   B HZ2  
1396 H HZ3  . LYS   A 96  ? 0.596781 0.569543 0.484707 0.0644426   -0.0342483  -0.0187718  108 LYS   B HZ3  
1397 N N    . PRO   A 97  ? 0.408972 0.340593 0.299873 0.0276196   -0.0488312  0.00157902  109 PRO   B N    
1398 C CA   . PRO   A 97  ? 0.432922 0.344401 0.301206 0.0304725   -0.0498882  0.00316041  109 PRO   B CA   
1399 C C    . PRO   A 97  ? 0.414004 0.293622 0.260149 0.0270243   -0.0407386  0.0108948   109 PRO   B C    
1400 O O    . PRO   A 97  ? 0.488693 0.356481 0.322374 0.0228996   -0.0346262  0.0145132   109 PRO   B O    
1401 C CB   . PRO   A 97  ? 0.488596 0.405919 0.346469 0.0473018   -0.0626573  -0.0012882  109 PRO   B CB   
1402 C CG   . PRO   A 97  ? 0.453013 0.393095 0.328407 0.0557242   -0.0669501  -0.0048933  109 PRO   B CG   
1403 C CD   . PRO   A 97  ? 0.430699 0.384543 0.330111 0.0402348   -0.0573965  -0.00363799 109 PRO   B CD   
1404 H HA   . PRO   A 97  ? 0.422301 0.340883 0.298701 0.0238788   -0.0488935  0.00146592  109 PRO   B HA   
1405 H HB2  . PRO   A 97  ? 0.497647 0.392185 0.330615 0.054995    -0.0630369  0.00240988  109 PRO   B HB2  
1406 H HB3  . PRO   A 97  ? 0.471195 0.400667 0.334781 0.0459762   -0.0679732  -0.0056922  109 PRO   B HB3  
1407 H HG2  . PRO   A 97  ? 0.477809 0.400965 0.337061 0.0657677   -0.067326   -0.00295388 109 PRO   B HG2  
1408 H HG3  . PRO   A 97  ? 0.457594 0.420192 0.344564 0.0605812   -0.0748272  -0.00976995 109 PRO   B HG3  
1409 H HD2  . PRO   A 97  ? 0.426007 0.380194 0.325312 0.0449479   -0.0555448  -0.00369087 109 PRO   B HD2  
1410 H HD3  . PRO   A 97  ? 0.40975  0.387077 0.32935  0.0348206   -0.0590372  -0.00623989 109 PRO   B HD3  
1411 N N    . GLU   A 98  ? 0.427537 0.294196 0.270164 0.0269425   -0.0386978  0.0129217   110 GLU   B N    
1412 C CA   . GLU   A 98  ? 0.501234 0.337313 0.326869 0.0185472   -0.0302226  0.0201971   110 GLU   B CA   
1413 C C    . GLU   A 98  ? 0.442781 0.289594 0.285772 0.00114103  -0.0200365  0.0231354   110 GLU   B C    
1414 O O    . GLU   A 98  ? 0.507948 0.33666  0.340033 -0.00752542 -0.0110651  0.0301483   110 GLU   B O    
1415 C CB   . GLU   A 98  ? 0.561792 0.379075 0.382309 0.0181011   -0.0313687  0.0190689   110 GLU   B CB   
1416 C CG   . GLU   A 98  ? 0.700037 0.498855 0.499508 0.038454    -0.0400192  0.0165009   110 GLU   B CG   
1417 C CD   . GLU   A 98  ? 0.735735 0.56891  0.550025 0.0546736   -0.0488793  0.00881627  110 GLU   B CD   
1418 O OE1  . GLU   A 98  ? 0.504448 0.373783 0.347449 0.0485575   -0.0479793  0.00409479  110 GLU   B OE1  
1419 O OE2  . GLU   A 98  ? 0.763985 0.587695 0.560585 0.0743642   -0.0568048  0.00835034  110 GLU   B OE2  
1420 H H    . GLU   A 98  ? 0.431874 0.308399 0.282601 0.0312791   -0.042195   0.00949085  110 GLU   B H    
1421 H HA   . GLU   A 98  ? 0.514055 0.33213  0.318435 0.0240832   -0.0299317  0.0242527   110 GLU   B HA   
1422 H HB2  . GLU   A 98  ? 0.550817 0.38646  0.389204 0.0139051   -0.0319224  0.014952    110 GLU   B HB2  
1423 H HB3  . GLU   A 98  ? 0.586935 0.384862 0.399587 0.00869887  -0.0258558  0.0237425   110 GLU   B HB3  
1424 H HG2  . GLU   A 98  ? 0.696468 0.478567 0.490392 0.0374523   -0.0400345  0.0148545   110 GLU   B HG2  
1425 H HG3  . GLU   A 98  ? 0.708722 0.485987 0.487195 0.0433798   -0.039954   0.0218293   110 GLU   B HG3  
1426 N N    . TYR   A 99  ? 0.381485 0.257209 0.250737 -0.0032677  -0.0207405  0.0190054   111 TYR   B N    
1427 C CA   . TYR   A 99  ? 0.438956 0.32766  0.325714 -0.0145626  -0.0130755  0.021195    111 TYR   B CA   
1428 C C    . TYR   A 99  ? 0.42449  0.323288 0.314265 -0.0108649  -0.0117154  0.0191425   111 TYR   B C    
1429 O O    . TYR   A 99  ? 0.395245 0.306838 0.300638 -0.015148   -0.00674673 0.0193252   111 TYR   B O    
1430 C CB   . TYR   A 99  ? 0.407579 0.313571 0.315308 -0.0198654  -0.0160361  0.0189149   111 TYR   B CB   
1431 C CG   . TYR   A 99  ? 0.402803 0.295061 0.304263 -0.0247118  -0.0178239  0.0182804   111 TYR   B CG   
1432 C CD1  . TYR   A 99  ? 0.410669 0.292496 0.299773 -0.0155816  -0.0243744  0.0138427   111 TYR   B CD1  
1433 C CD2  . TYR   A 99  ? 0.443242 0.334314 0.352411 -0.0380034  -0.013832   0.0204613   111 TYR   B CD2  
1434 C CE1  . TYR   A 99  ? 0.438427 0.300654 0.317026 -0.0184484  -0.0270502  0.0108199   111 TYR   B CE1  
1435 C CE2  . TYR   A 99  ? 0.451032 0.323894 0.35249  -0.0447871  -0.0174131  0.017789    111 TYR   B CE2  
1436 C CZ   . TYR   A 99  ? 0.487144 0.341232 0.370391 -0.0345214  -0.0241864  0.012565    111 TYR   B CZ   
1437 O OH   . TYR   A 99  ? 0.465748 0.296804 0.33873  -0.0406594  -0.028772   0.00753922  111 TYR   B OH   
1438 H H    . TYR   A 99  ? 0.393465 0.281383 0.270135 0.00156806  -0.0261239  0.0151719   111 TYR   B H    
1439 H HA   . TYR   A 99  ? 0.433238 0.311216 0.31376  -0.0203175  -0.00701638 0.0253988   111 TYR   B HA   
1440 H HB2  . TYR   A 99  ? 0.396058 0.311197 0.308165 -0.0148584  -0.020605   0.0161498   111 TYR   B HB2  
1441 H HB3  . TYR   A 99  ? 0.395564 0.312865 0.316025 -0.0246863  -0.012594   0.020261    111 TYR   B HB3  
1442 H HD1  . TYR   A 99  ? 0.409556 0.297617 0.297327 -0.00676235 -0.0272147  0.012141    111 TYR   B HD1  
1443 H HD2  . TYR   A 99  ? 0.425741 0.327198 0.344872 -0.0426668  -0.00853947 0.023362    111 TYR   B HD2  
1444 H HE1  . TYR   A 99  ? 0.456018 0.309558 0.32417  -0.00956796 -0.031018   0.0070152   111 TYR   B HE1  
1445 H HE2  . TYR   A 99  ? 0.463479 0.337228 0.372706 -0.0561142  -0.0155012  0.018738    111 TYR   B HE2  
1447 N N    . ALA   A 100 ? 0.412903 0.304201 0.28556  -0.00117917 -0.0174857  0.016109    112 ALA   B N    
1448 C CA   . ALA   A 100 ? 0.424329 0.319507 0.29415  0.00244053  -0.0183748  0.0112865   112 ALA   B CA   
1449 C C    . ALA   A 100 ? 0.45164  0.328333 0.287828 0.0118586   -0.0186081  0.0120318   112 ALA   B C    
1450 O O    . ALA   A 100 ? 0.487974 0.352107 0.308424 0.00998554  -0.0066412  0.019156    112 ALA   B O    
1451 C CB   . ALA   A 100 ? 0.40996  0.320961 0.29729  0.00288151  -0.0290815  0.00399901  112 ALA   B CB   
1452 H H    . ALA   A 100 ? 0.430158 0.313267 0.291841 0.00408814  -0.0218543  0.0162205   112 ALA   B H    
1453 H HA   . ALA   A 100 ? 0.417985 0.316901 0.295355 -0.00160506 -0.0113198  0.0125103   112 ALA   B HA   
1454 H HB1  . ALA   A 100 ? 0.393728 0.313763 0.2984   -0.00280645 -0.0270357  0.00521233  112 ALA   B HB1  
1455 H HB2  . ALA   A 100 ? 0.410666 0.32454  0.296335 0.006758    -0.0352509  0.00294982  112 ALA   B HB2  
1456 H HB3  . ALA   A 100 ? 0.417248 0.326592 0.29992  0.00497224  -0.0318005  -0.00081155 112 ALA   B HB3  
1457 N N    . TYR   A 101 ? 0.449426 0.327102 0.275026 0.0214988   -0.0317644  0.00527278  113 TYR   B N    
1458 C CA   . TYR   A 101 ? 0.473994 0.334183 0.262497 0.032934    -0.0338765  0.00564492  113 TYR   B CA   
1459 C C    . TYR   A 101 ? 0.507522 0.353757 0.273306 0.0448484   -0.0420262  0.0103164   113 TYR   B C    
1460 O O    . TYR   A 101 ? 0.557164 0.388208 0.28827  0.0572123   -0.0465415  0.0115535   113 TYR   B O    
1461 C CB   . TYR   A 101 ? 0.491437 0.359036 0.275654 0.0378668   -0.044748   -0.00697521 113 TYR   B CB   
1462 C CG   . TYR   A 101 ? 0.479115 0.349921 0.275516 0.0309559   -0.0368204  -0.0121827  113 TYR   B CG   
1463 C CD1  . TYR   A 101 ? 0.515986 0.374967 0.290632 0.0345229   -0.022791   -0.00949812 113 TYR   B CD1  
1464 C CD2  . TYR   A 101 ? 0.454955 0.340402 0.285853 0.0212666   -0.0403252  -0.0170244  113 TYR   B CD2  
1465 C CE1  . TYR   A 101 ? 0.518773 0.3822   0.307705 0.0314627   -0.0144363  -0.0140385  113 TYR   B CE1  
1466 C CE2  . TYR   A 101 ? 0.479591 0.363195 0.321002 0.0174079   -0.0330189  -0.0201545  113 TYR   B CE2  
1467 C CZ   . TYR   A 101 ? 0.480737 0.353478 0.300882 0.0243029   -0.0213269  -0.0202322  113 TYR   B CZ   
1468 O OH   . TYR   A 101 ? 0.52926  0.400234 0.35843  0.0253572   -0.0138811  -0.0245085  113 TYR   B OH   
1469 H H    . TYR   A 101 ? 0.436715 0.327162 0.277545 0.0210836   -0.0394214  0.00078854  113 TYR   B H    
1470 H HA   . TYR   A 101 ? 0.49151  0.341586 0.268445 0.0306254   -0.0222526  0.0113279   113 TYR   B HA   
1471 H HB2  . TYR   A 101 ? 0.477138 0.358243 0.277057 0.0376876   -0.0558062  -0.0125005  113 TYR   B HB2  
1472 H HB3  . TYR   A 101 ? 0.516308 0.372333 0.272261 0.0469495   -0.0471957  -0.00694228 113 TYR   B HB3  
1473 H HD1  . TYR   A 101 ? 0.536645 0.384784 0.286639 0.0398696   -0.018021   -0.00394204 113 TYR   B HD1  
1474 H HD2  . TYR   A 101 ? 0.447319 0.343535 0.293728 0.0182702   -0.0474826  -0.0177317  113 TYR   B HD2  
1475 H HE1  . TYR   A 101 ? 0.529798 0.388306 0.303989 0.0360237   -0.00451836 -0.0134068  113 TYR   B HE1  
1476 H HE2  . TYR   A 101 ? 0.455423 0.344651 0.316599 0.0115145   -0.0361848  -0.0225044  113 TYR   B HE2  
1478 N N    . GLY   A 102 ? 0.488531 0.339576 0.270435 0.0447466   -0.0458484  0.0117246   114 GLY   B N    
1479 C CA   . GLY   A 102 ? 0.551074 0.378861 0.308464 0.0565768   -0.0491415  0.0184366   114 GLY   B CA   
1480 C C    . GLY   A 102 ? 0.62078  0.45702  0.366234 0.0760709   -0.0671609  0.0123788   114 GLY   B C    
1481 O O    . GLY   A 102 ? 0.543319 0.408764 0.307191 0.0766117   -0.0779933  0.00155924  114 GLY   B O    
1482 H H    . GLY   A 102 ? 0.47186  0.339271 0.278581 0.0383135   -0.0463062  0.00836802  114 GLY   B H    
1483 H HA2  . GLY   A 102 ? 0.541584 0.370432 0.312264 0.0533897   -0.0478124  0.0190664   114 GLY   B HA2  
1484 H HA3  . GLY   A 102 ? 0.576932 0.381606 0.311315 0.0556454   -0.0410644  0.0264297   114 GLY   B HA3  
1485 N N    . SER   A 103 ? 0.61391  0.422782 0.327121 0.0923565   -0.0714154  0.0195782   115 SER   B N    
1486 C CA   . SER   A 103 ? 0.61305  0.433931 0.315078 0.114588    -0.0908856  0.0137993   115 SER   B CA   
1487 C C    . SER   A 103 ? 0.607637 0.422773 0.279124 0.120564    -0.0963795  0.0127246   115 SER   B C    
1488 O O    . SER   A 103 ? 0.600339 0.435525 0.269068 0.134773    -0.115115   0.00390828  115 SER   B O    
1489 C CB   . SER   A 103 ? 0.776771 0.571098 0.455221 0.134839    -0.0960892  0.0207978   115 SER   B CB   
1490 O OG   . SER   A 103 ? 0.847303 0.590804 0.486069 0.131027    -0.0826089  0.0359737   115 SER   B OG   
1491 H H    . SER   A 103 ? 0.635646 0.4188   0.334242 0.0900808   -0.0632985  0.0278497   115 SER   B H    
1492 H HA   . SER   A 103 ? 0.603713 0.4572   0.33622  0.11263     -0.097873   0.0046      115 SER   B HA   
1493 H HB2  . SER   A 103 ? 0.766478 0.568904 0.434884 0.151848    -0.109585   0.0178106   115 SER   B HB2  
1494 H HB3  . SER   A 103 ? 0.731427 0.534217 0.430716 0.13314     -0.0945936  0.0181281   115 SER   B HB3  
1496 N N    . ALA   A 104 ? 0.636775 0.428106 0.285339 0.110422    -0.0805706  0.0204927   116 ALA   B N    
1497 C CA   . ALA   A 104 ? 0.689441 0.474476 0.303599 0.11811     -0.0842123  0.0183822   116 ALA   B CA   
1498 C C    . ALA   A 104 ? 0.590079 0.409416 0.233325 0.109676    -0.0928964  0.00050294  116 ALA   B C    
1499 O O    . ALA   A 104 ? 0.598727 0.42558  0.224045 0.119843    -0.108283   -0.00978845 116 ALA   B O    
1500 C CB   . ALA   A 104 ? 0.772599 0.525115 0.352998 0.111405    -0.0620169  0.0326814   116 ALA   B CB   
1501 H H    . ALA   A 104 ? 0.630736 0.410998 0.284757 0.0991131   -0.0672597  0.0267954   116 ALA   B H    
1502 H HA   . ALA   A 104 ? 0.707735 0.487281 0.299436 0.135067    -0.0970645  0.0188794   116 ALA   B HA   
1503 H HB1  . ALA   A 104 ? 0.780177 0.507318 0.340738 0.115509    -0.0574044  0.0445926   116 ALA   B HB1  
1504 H HB2  . ALA   A 104 ? 0.728545 0.489072 0.332439 0.0961759   -0.0500609  0.0322065   116 ALA   B HB2  
1505 H HB3  . ALA   A 104 ? 0.779902 0.528988 0.334323 0.118394    -0.0639756  0.030587    116 ALA   B HB3  
1506 N N    . GLY   A 105 ? 0.581956 0.419396 0.268006 0.0913618   -0.0846608  -0.00353307 117 GLY   B N    
1507 C CA   . GLY   A 105 ? 0.533405 0.392956 0.2446   0.0807313   -0.0895074  -0.0180546  117 GLY   B CA   
1508 C C    . GLY   A 105 ? 0.579592 0.421766 0.26467  0.0787797   -0.0775268  -0.0191361  117 GLY   B C    
1509 O O    . GLY   A 105 ? 0.59394  0.412512 0.245812 0.08311     -0.0623936  -0.00698803 117 GLY   B O    
1510 H H    . GLY   A 105 ? 0.552174 0.385857 0.250815 0.0852866   -0.0761092  0.00293793  117 GLY   B H    
1511 H HA2  . GLY   A 105 ? 0.513919 0.385947 0.256829 0.0694      -0.0848154  -0.0184646  117 GLY   B HA2  
1512 H HA3  . GLY   A 105 ? 0.550872 0.424893 0.265073 0.0864676   -0.105687   -0.0273623  117 GLY   B HA3  
1513 N N    . SER   A 106 ? 0.570721 0.424016 0.265441 0.0750266   -0.0872601  -0.0352569  118 SER   B N    
1514 C CA   . SER   A 106 ? 0.597808 0.437209 0.26985  0.0761105   -0.0792157  -0.0420732  118 SER   B CA   
1515 C C    . SER   A 106 ? 0.62634  0.472763 0.29945  0.076461    -0.100609   -0.0638628  118 SER   B C    
1516 O O    . SER   A 106 ? 0.60234  0.451346 0.300312 0.0649798   -0.101014   -0.0743222  118 SER   B O    
1517 C CB   . SER   A 106 ? 0.568676 0.408069 0.265505 0.0637517   -0.0588195  -0.0376564  118 SER   B CB   
1518 O OG   . SER   A 106 ? 0.652605 0.476668 0.316096 0.0718145   -0.046533   -0.040321   118 SER   B OG   
1519 H H    . SER   A 106 ? 0.559608 0.42982  0.276789 0.0715629   -0.0996094  -0.0429731  118 SER   B H    
1520 H HA   . SER   A 106 ? 0.629682 0.454073 0.265943 0.086175    -0.0737356  -0.0361335  118 SER   B HA   
1521 H HB2  . SER   A 106 ? 0.565153 0.405259 0.271138 0.0597728   -0.0487483  -0.0257796  118 SER   B HB2  
1522 H HB3  . SER   A 106 ? 0.560557 0.409547 0.284575 0.0555807   -0.0644711  -0.0451008  118 SER   B HB3  
1524 N N    . LEU   A 107 ? 0.673981 0.519804 0.31551  0.0905237   -0.119597   -0.0710521  119 LEU   B N    
1525 C CA   . LEU   A 107 ? 0.651396 0.507734 0.297249 0.0888109   -0.144912   -0.0937137  119 LEU   B CA   
1526 C C    . LEU   A 107 ? 0.68676  0.518683 0.298644 0.0927749   -0.140844   -0.107236   119 LEU   B C    
1527 O O    . LEU   A 107 ? 0.704132 0.51569  0.274434 0.10507     -0.12317    -0.098901   119 LEU   B O    
1528 C CB   . LEU   A 107 ? 0.724632 0.591568 0.345916 0.105757    -0.168084   -0.0964696  119 LEU   B CB   
1529 C CG   . LEU   A 107 ? 0.679296 0.577519 0.339967 0.104591    -0.178672   -0.0901882  119 LEU   B CG   
1530 C CD1  . LEU   A 107 ? 0.735021 0.644787 0.369715 0.125626    -0.203445   -0.0943412  119 LEU   B CD1  
1531 C CD2  . LEU   A 107 ? 0.668453 0.598759 0.390516 0.0829871   -0.187843   -0.101556   119 LEU   B CD2  
1532 H H    . LEU   A 107 ? 0.679258 0.517339 0.295807 0.101064    -0.117661   -0.0618668  119 LEU   B H    
1533 H HA   . LEU   A 107 ? 0.637857 0.509954 0.323414 0.0751503   -0.149299   -0.0978895  119 LEU   B HA   
1534 H HB2  . LEU   A 107 ? 0.737122 0.586258 0.319561 0.119084    -0.16028    -0.0868923  119 LEU   B HB2  
1535 H HB3  . LEU   A 107 ? 0.73377  0.604035 0.347227 0.106663    -0.185055   -0.11274    119 LEU   B HB3  
1536 H HG   . LEU   A 107 ? 0.673793 0.564674 0.33688  0.105237    -0.162993   -0.0750474  119 LEU   B HG   
1537 H HD11 . LEU   A 107 ? 0.760319 0.646668 0.351231 0.139764    -0.197961   -0.0862695  119 LEU   B HD11 
1538 H HD12 . LEU   A 107 ? 0.710823 0.639504 0.368658 0.128111    -0.207469   -0.0889141  119 LEU   B HD12 
1539 H HD13 . LEU   A 107 ? 0.743621 0.665423 0.381231 0.1234      -0.221357   -0.1106     119 LEU   B HD13 
1540 H HD21 . LEU   A 107 ? 0.63402  0.558268 0.374521 0.071307    -0.17195    -0.0957501  119 LEU   B HD21 
1541 H HD22 . LEU   A 107 ? 0.677279 0.610068 0.398477 0.0784518   -0.201364   -0.1168     119 LEU   B HD22 
1542 H HD23 . LEU   A 107 ? 0.646653 0.600994 0.389985 0.0854645   -0.196015   -0.0992906  119 LEU   B HD23 
1543 N N    . PRO   A 108 ? 0.714367 0.545714 0.337274 0.0841655   -0.157826   -0.129753   120 PRO   B N    
1544 C CA   . PRO   A 108 ? 0.728217 0.586188 0.398027 0.0677475   -0.180779   -0.140992   120 PRO   B CA   
1545 C C    . PRO   A 108 ? 0.661826 0.531798 0.389253 0.0460744   -0.168822   -0.132328   120 PRO   B C    
1546 O O    . PRO   A 108 ? 0.653172 0.551572 0.423842 0.0318098   -0.18153    -0.134838   120 PRO   B O    
1547 C CB   . PRO   A 108 ? 0.761375 0.606158 0.41589  0.0643598   -0.202057   -0.16846    120 PRO   B CB   
1548 C CG   . PRO   A 108 ? 0.822353 0.629681 0.42888  0.077763    -0.184356   -0.171574   120 PRO   B CG   
1549 C CD   . PRO   A 108 ? 0.785422 0.589143 0.378754 0.0884441   -0.152988   -0.144808   120 PRO   B CD   
1550 H HA   . PRO   A 108 ? 0.715502 0.591433 0.385666 0.0740462   -0.191617   -0.137639   120 PRO   B HA   
1551 H HB2  . PRO   A 108 ? 0.755547 0.605049 0.444948 0.0470114   -0.207128   -0.175298   120 PRO   B HB2  
1552 H HB3  . PRO   A 108 ? 0.793283 0.648513 0.432661 0.0716711   -0.22135    -0.177042   120 PRO   B HB3  
1553 H HG2  . PRO   A 108 ? 0.811999 0.606142 0.432754 0.068161    -0.181049   -0.17935    120 PRO   B HG2  
1554 H HG3  . PRO   A 108 ? 0.854689 0.652904 0.423268 0.0896029   -0.196099   -0.183409   120 PRO   B HG3  
1555 H HD2  . PRO   A 108 ? 0.760739 0.55778  0.371041 0.0820992   -0.137038   -0.140089   120 PRO   B HD2  
1556 H HD3  . PRO   A 108 ? 0.812427 0.603886 0.362673 0.103818    -0.148219   -0.143786   120 PRO   B HD3  
1557 N N    . LYS   A 109 ? 0.668392 0.521088 0.398179 0.0439277   -0.14428    -0.121225   121 LYS   B N    
1558 C CA   . LYS   A 109 ? 0.630349 0.490543 0.408604 0.0246409   -0.136252   -0.115232   121 LYS   B CA   
1559 C C    . LYS   A 109 ? 0.647216 0.536972 0.459072 0.0192651   -0.131417   -0.0984188  121 LYS   B C    
1560 O O    . LYS   A 109 ? 0.576217 0.482868 0.428395 0.00314599  -0.133692   -0.0970376  121 LYS   B O    
1561 C CB   . LYS   A 109 ? 0.702887 0.540032 0.477283 0.0257753   -0.113813   -0.108673   121 LYS   B CB   
1562 C CG   . LYS   A 109 ? 0.771736 0.576749 0.514966 0.0326061   -0.117607   -0.128007   121 LYS   B CG   
1563 C CD   . LYS   A 109 ? 0.820938 0.607574 0.56608  0.0366029   -0.0958627  -0.122078   121 LYS   B CD   
1564 C CE   . LYS   A 109 ? 0.929082 0.68264  0.641984 0.0482769   -0.0958112  -0.140485   121 LYS   B CE   
1565 N NZ   . LYS   A 109 ? 1.02747  0.762137 0.759342 0.0325049   -0.113391   -0.155737   121 LYS   B NZ   
1566 H H    . LYS   A 109 ? 0.67533  0.513352 0.377534 0.0543935   -0.132485   -0.116897   121 LYS   B H    
1567 H HA   . LYS   A 109 ? 0.66276  0.523844 0.456155 0.0137862   -0.149274   -0.127251   121 LYS   B HA   
1568 H HB2  . LYS   A 109 ? 0.680723 0.51836  0.441858 0.034571    -0.100748   -0.0975332  121 LYS   B HB2  
1569 H HB3  . LYS   A 109 ? 0.664173 0.506188 0.468534 0.0142828   -0.10972    -0.103395   121 LYS   B HB3  
1570 H HG2  . LYS   A 109 ? 0.791045 0.592518 0.545965 0.02245     -0.132375   -0.140206   121 LYS   B HG2  
1571 H HG3  . LYS   A 109 ? 0.803485 0.603652 0.513067 0.0454541   -0.119826   -0.132403   121 LYS   B HG3  
1572 H HD2  . LYS   A 109 ? 0.807079 0.602091 0.546189 0.0438416   -0.0815653  -0.109578   121 LYS   B HD2  
1573 H HD3  . LYS   A 109 ? 0.800303 0.590176 0.575955 0.0248087   -0.0947851  -0.117      121 LYS   B HD3  
1574 H HE2  . LYS   A 109 ? 0.960979 0.710349 0.641627 0.0586857   -0.100719   -0.148602   121 LYS   B HE2  
1575 H HE3  . LYS   A 109 ? 0.929316 0.677627 0.641149 0.0556615   -0.0797176  -0.134493   121 LYS   B HE3  
1576 H HZ1  . LYS   A 109 ? 1.00005  0.744062 0.736993 0.0243238   -0.128506   -0.161552   121 LYS   B HZ1  
1577 H HZ2  . LYS   A 109 ? 0.976176 0.71279  0.735023 0.0234932   -0.107936   -0.146866   121 LYS   B HZ2  
1578 H HZ3  . LYS   A 109 ? 1.03436  0.74487  0.745407 0.0398118   -0.114865   -0.1686     121 LYS   B HZ3  
1579 N N    . ILE   A 110 ? 0.565686 0.458511 0.359982 0.0323244   -0.122531   -0.084694   122 ILE   B N    
1580 C CA   . ILE   A 110 ? 0.532477 0.445691 0.354471 0.0289091   -0.11565    -0.0700752  122 ILE   B CA   
1581 C C    . ILE   A 110 ? 0.523471 0.449673 0.330571 0.0439628   -0.127543   -0.0677847  122 ILE   B C    
1582 O O    . ILE   A 110 ? 0.549929 0.455316 0.314429 0.0592927   -0.123859   -0.0627663  122 ILE   B O    
1583 C CB   . ILE   A 110 ? 0.543673 0.442064 0.358228 0.0307802   -0.0922484  -0.0539896  122 ILE   B CB   
1584 C CG1  . ILE   A 110 ? 0.607181 0.489349 0.423979 0.0246978   -0.0792102  -0.055316   122 ILE   B CG1  
1585 C CG2  . ILE   A 110 ? 0.516927 0.432647 0.358277 0.0265093   -0.0867992  -0.0420648  122 ILE   B CG2  
1586 C CD1  . ILE   A 110 ? 0.678641 0.568626 0.533236 0.00902974  -0.081052   -0.0577623  122 ILE   B CD1  
1587 H H    . ILE   A 110 ? 0.604832 0.484677 0.367257 0.0437747   -0.120354   -0.0844015  122 ILE   B H    
1588 H HA   . ILE   A 110 ? 0.51515  0.442761 0.368125 0.0170674   -0.118313   -0.0716852  122 ILE   B HA   
1589 H HB   . ILE   A 110 ? 0.569265 0.45641  0.355019 0.0414133   -0.0895492  -0.0505469  122 ILE   B HB   
1590 H HG12 . ILE   A 110 ? 0.635791 0.505314 0.430913 0.0302633   -0.0824818  -0.0640166  122 ILE   B HG12 
1591 H HG13 . ILE   A 110 ? 0.601551 0.479291 0.414153 0.026695    -0.0657423  -0.0455805  122 ILE   B HG13 
1592 H HG21 . ILE   A 110 ? 0.500956 0.411004 0.348397 0.0219478   -0.0743822  -0.0351089  122 ILE   B HG21 
1593 H HG22 . ILE   A 110 ? 0.501814 0.43517  0.367905 0.0194979   -0.0940492  -0.0459816  122 ILE   B HG22 
1594 H HG23 . ILE   A 110 ? 0.522496 0.437071 0.349175 0.0359027   -0.0885837  -0.0377191  122 ILE   B HG23 
1595 H HD11 . ILE   A 110 ? 0.622966 0.524594 0.495765 0.00463951  -0.0756278  -0.048558   122 ILE   B HD11 
1596 H HD12 . ILE   A 110 ? 0.652683 0.528794 0.50434  0.00846145  -0.0745717  -0.0595885  122 ILE   B HD12 
1597 H HD13 . ILE   A 110 ? 0.653403 0.550096 0.516415 0.0040767   -0.0940309  -0.0665556  122 ILE   B HD13 
1598 N N    . PRO   A 111 ? 0.53127  0.490324 0.370682 0.0416142   -0.139012   -0.0691355  123 PRO   B N    
1599 C CA   . PRO   A 111 ? 0.489081 0.461539 0.315499 0.0604906   -0.151236   -0.0669879  123 PRO   B CA   
1600 C C    . PRO   A 111 ? 0.487132 0.444934 0.302401 0.0694016   -0.135232   -0.0499816  123 PRO   B C    
1601 O O    . PRO   A 111 ? 0.486967 0.433957 0.313237 0.0582065   -0.116894   -0.0414852  123 PRO   B O    
1602 C CB   . PRO   A 111 ? 0.503537 0.521688 0.372909 0.0554176   -0.167932   -0.0759758  123 PRO   B CB   
1603 C CG   . PRO   A 111 ? 0.510508 0.535614 0.417181 0.028547    -0.161925   -0.0809142  123 PRO   B CG   
1604 C CD   . PRO   A 111 ? 0.525497 0.511986 0.414254 0.0218982   -0.142208   -0.0740117  123 PRO   B CD   
1605 H HA   . PRO   A 111 ? 0.535776 0.495787 0.331074 0.0708176   -0.15932    -0.0714099  123 PRO   B HA   
1606 H HB2  . PRO   A 111 ? 0.488821 0.520904 0.370342 0.0616073   -0.164645   -0.0690683  123 PRO   B HB2  
1607 H HB3  . PRO   A 111 ? 0.52489  0.552809 0.385669 0.0624825   -0.185      -0.0854103  123 PRO   B HB3  
1608 H HG2  . PRO   A 111 ? 0.484982 0.533145 0.422276 0.0221142   -0.157908   -0.0767392  123 PRO   B HG2  
1609 H HG3  . PRO   A 111 ? 0.52219  0.555278 0.435061 0.0221193   -0.175583   -0.0930491  123 PRO   B HG3  
1610 H HD2  . PRO   A 111 ? 0.492835 0.481753 0.397255 0.0165893   -0.129669   -0.0646935  123 PRO   B HD2  
1611 H HD3  . PRO   A 111 ? 0.524946 0.502985 0.416666 0.0119233   -0.14526    -0.0822009  123 PRO   B HD3  
1612 N N    . SER   A 112 ? 0.492207 0.449987 0.286192 0.0900311   -0.144905   -0.0464028  124 SER   B N    
1613 C CA   . SER   A 112 ? 0.467863 0.410671 0.25243  0.100217    -0.134424   -0.0325825  124 SER   B CA   
1614 C C    . SER   A 112 ? 0.459128 0.427336 0.288553 0.0894253   -0.126747   -0.031469   124 SER   B C    
1615 O O    . SER   A 112 ? 0.423977 0.431749 0.28966  0.0848237   -0.136328   -0.040187   124 SER   B O    
1616 C CB   . SER   A 112 ? 0.50169  0.443757 0.259845 0.127242    -0.150919   -0.0313382  124 SER   B CB   
1617 O OG   . SER   A 112 ? 0.529251 0.450595 0.277544 0.137724    -0.14141    -0.0190906  124 SER   B OG   
1618 H H    . SER   A 112 ? 0.511298 0.476747 0.294816 0.0987504   -0.159529   -0.0532947  124 SER   B H    
1619 H HA   . SER   A 112 ? 0.485666 0.399946 0.248478 0.0976167   -0.121522   -0.0245496  124 SER   B HA   
1620 H HB2  . SER   A 112 ? 0.53774  0.459891 0.26186  0.13457     -0.154227   -0.0301511  124 SER   B HB2  
1621 H HB3  . SER   A 112 ? 0.501035 0.475963 0.282283 0.130444    -0.164797   -0.0402497  124 SER   B HB3  
1623 N N    . ASN   A 113 ? 0.457648 0.402888 0.281474 0.0855784   -0.109861   -0.0207849  125 ASN   B N    
1624 C CA   . ASN   A 113 ? 0.478816 0.441598 0.331996 0.0821562   -0.103088   -0.0188648  125 ASN   B CA   
1625 C C    . ASN   A 113 ? 0.456152 0.451795 0.351889 0.0617146   -0.0999743  -0.0243353  125 ASN   B C    
1626 O O    . ASN   A 113 ? 0.427839 0.455015 0.353676 0.0602196   -0.0995326  -0.0260829  125 ASN   B O    
1627 C CB   . ASN   A 113 ? 0.465318 0.445381 0.320703 0.104302    -0.114011   -0.0210305  125 ASN   B CB   
1628 C CG   . ASN   A 113 ? 0.543492 0.478753 0.354181 0.12328     -0.113328   -0.0121656  125 ASN   B CG   
1629 O OD1  . ASN   A 113 ? 0.596721 0.491835 0.382856 0.115071    -0.100753   -0.00318558 125 ASN   B OD1  
1630 N ND2  . ASN   A 113 ? 0.583665 0.525261 0.383852 0.148291    -0.126968   -0.0139981  125 ASN   B ND2  
1631 H H    . ASN   A 113 ? 0.477925 0.396315 0.278474 0.0847659   -0.102103   -0.0147998  125 ASN   B H    
1632 H HA   . ASN   A 113 ? 0.467244 0.406923 0.309198 0.0789737   -0.0923541  -0.0120337  125 ASN   B HA   
1633 H HB2  . ASN   A 113 ? 0.483471 0.486555 0.34726  0.109424    -0.126418   -0.0276111  125 ASN   B HB2  
1634 H HB3  . ASN   A 113 ? 0.461802 0.459251 0.338983 0.101927    -0.10927    -0.0216777  125 ASN   B HB3  
1635 H HD21 . ASN   A 113 ? 0.610195 0.523565 0.379506 0.160313    -0.129504   -0.0086293  125 ASN   B HD21 
1636 H HD22 . ASN   A 113 ? 0.567971 0.542696 0.391931 0.153931    -0.133579   -0.0201488  125 ASN   B HD22 
1637 N N    . ALA   A 114 ? 0.399659 0.383892 0.295008 0.0465939   -0.0952371  -0.0253934  126 ALA   B N    
1638 C CA   . ALA   A 114 ? 0.454677 0.457098 0.382517 0.0274154   -0.0920219  -0.0285545  126 ALA   B CA   
1639 C C    . ALA   A 114 ? 0.376608 0.371567 0.313458 0.0181074   -0.0757895  -0.0193963  126 ALA   B C    
1640 O O    . ALA   A 114 ? 0.380852 0.349076 0.297967 0.0186951   -0.0660668  -0.0129677  126 ALA   B O    
1641 C CB   . ALA   A 114 ? 0.447809 0.435326 0.366308 0.0193416   -0.0961529  -0.0355971  126 ALA   B CB   
1642 H H    . ALA   A 114 ? 0.442485 0.404301 0.314309 0.0490801   -0.0932411  -0.0235295  126 ALA   B H    
1643 H HA   . ALA   A 114 ? 0.417825 0.447985 0.367901 0.0263191   -0.0983876  -0.032509   126 ALA   B HA   
1644 H HB1  . ALA   A 114 ? 0.469697 0.462503 0.380728 0.0254323   -0.108043   -0.0425433  126 ALA   B HB1  
1645 H HB2  . ALA   A 114 ? 0.459974 0.424449 0.358416 0.0212424   -0.0885077  -0.0316535  126 ALA   B HB2  
1646 H HB3  . ALA   A 114 ? 0.443027 0.438311 0.382074 0.00680505  -0.0946623  -0.0373899  126 ALA   B HB3  
1647 N N    . THR   A 115 ? 0.351166 0.373887 0.318746 0.00963149  -0.0733023  -0.0186192  127 THR   B N    
1648 C CA   . THR   A 115 ? 0.335994 0.354896 0.31319  -0.00112862 -0.0604329  -0.0108273  127 THR   B CA   
1649 C C    . THR   A 115 ? 0.357016 0.36825  0.344635 -0.0164741  -0.0593268  -0.0113711  127 THR   B C    
1650 O O    . THR   A 115 ? 0.386478 0.411268 0.391375 -0.025293   -0.0668745  -0.0172617  127 THR   B O    
1651 C CB   . THR   A 115 ? 0.333321 0.383486 0.332299 -0.00115065 -0.0566041  -0.00837301 127 THR   B CB   
1652 O OG1  . THR   A 115 ? 0.354591 0.402053 0.337289 0.0169077   -0.0574997  -0.0092166  127 THR   B OG1  
1653 C CG2  . THR   A 115 ? 0.378395 0.428504 0.386069 -0.0122061  -0.0450299  3.948e-05   127 THR   B CG2  
1654 H H    . THR   A 115 ? 0.35349  0.399219 0.3359   0.0108584   -0.0794747  -0.0224705  127 THR   B H    
1655 H HA   . THR   A 115 ? 0.343096 0.343956 0.304535 0.00266242  -0.0554735  -0.0072142  127 THR   B HA   
1656 H HB   . THR   A 115 ? 0.34381  0.416061 0.360533 -0.00470123 -0.0616462  -0.0120307  127 THR   B HB   
1658 H HG21 . THR   A 115 ? 0.357243 0.425536 0.372482 -0.00934387 -0.041318   0.00173213  127 THR   B HG21 
1659 H HG22 . THR   A 115 ? 0.360955 0.391263 0.354108 -0.0105433  -0.0417381  0.00266507  127 THR   B HG22 
1660 H HG23 . THR   A 115 ? 0.36092  0.412471 0.380099 -0.0231949  -0.0448401  0.00112661  127 THR   B HG23 
1661 N N    . LEU   A 116 ? 0.352321 0.344788 0.333832 -0.0205133  -0.0501594  -0.00504527 128 LEU   B N    
1662 C CA   . LEU   A 116 ? 0.355129 0.3317   0.340072 -0.0296944  -0.0488745  -0.00549919 128 LEU   B CA   
1663 C C    . LEU   A 116 ? 0.374609 0.35279  0.371924 -0.0371729  -0.04025    0.00473856  128 LEU   B C    
1664 O O    . LEU   A 116 ? 0.329181 0.314851 0.324305 -0.0331634  -0.0347184  0.0109351   128 LEU   B O    
1665 C CB   . LEU   A 116 ? 0.435835 0.387464 0.398624 -0.0226309  -0.0454706  -0.00703452 128 LEU   B CB   
1666 C CG   . LEU   A 116 ? 0.458955 0.401451 0.397882 -0.0124438  -0.0502538  -0.0135845  128 LEU   B CG   
1667 C CD1  . LEU   A 116 ? 0.450671 0.371894 0.371942 -0.00823094 -0.0435288  -0.0149266  128 LEU   B CD1  
1668 C CD2  . LEU   A 116 ? 0.429006 0.378844 0.370134 -0.0133749  -0.0635894  -0.0238771  128 LEU   B CD2  
1669 H H    . LEU   A 116 ? 0.346129 0.335173 0.321177 -0.0167136  -0.0452318  -0.00084162 128 LEU   B H    
1670 H HA   . LEU   A 116 ? 0.380883 0.361113 0.373504 -0.0349957  -0.0554092  -0.0111419  128 LEU   B HA   
1671 H HB2  . LEU   A 116 ? 0.411309 0.361871 0.37227  -0.0208248  -0.0389663  -0.0010653  128 LEU   B HB2  
1672 H HB3  . LEU   A 116 ? 0.427271 0.368374 0.392228 -0.0263699  -0.0452056  -0.00872456 128 LEU   B HB3  
1673 H HG   . LEU   A 116 ? 0.441361 0.386666 0.373671 -0.00730381 -0.0486322  -0.0100936  128 LEU   B HG   
1674 H HD11 . LEU   A 116 ? 0.447741 0.368787 0.372519 -0.00875384 -0.0355752  -0.00861496 128 LEU   B HD11 
1675 H HD12 . LEU   A 116 ? 0.469438 0.38429  0.372205 -0.00153366 -0.044509   -0.0172041  128 LEU   B HD12 
1676 H HD13 . LEU   A 116 ? 0.465111 0.379835 0.389735 -0.011161   -0.0461637  -0.0199191  128 LEU   B HD13 
1677 H HD21 . LEU   A 116 ? 0.434031 0.401224 0.384961 -0.0128136  -0.0674175  -0.0232884  128 LEU   B HD21 
1678 H HD22 . LEU   A 116 ? 0.445225 0.392787 0.397122 -0.021475   -0.0656388  -0.0270544  128 LEU   B HD22 
1679 H HD23 . LEU   A 116 ? 0.457364 0.397232 0.378966 -0.00617248 -0.066937   -0.0283834  128 LEU   B HD23 
1680 N N    . PHE   A 117 ? 0.350079 0.317315 0.356593 -0.0471923  -0.0404024  0.00592047  129 PHE   B N    
1681 C CA   . PHE   A 117 ? 0.354623 0.318596 0.368809 -0.0534111  -0.0331584  0.01759     129 PHE   B CA   
1682 C C    . PHE   A 117 ? 0.357033 0.290109 0.362529 -0.0513364  -0.0330504  0.0168237   129 PHE   B C    
1683 O O    . PHE   A 117 ? 0.410736 0.326367 0.41245  -0.0533397  -0.0391976  0.00672316  129 PHE   B O    
1684 C CB   . PHE   A 117 ? 0.391021 0.370492 0.425643 -0.0683149  -0.0321583  0.022331    129 PHE   B CB   
1685 C CG   . PHE   A 117 ? 0.43511  0.399035 0.470553 -0.0750414  -0.0248072  0.036049    129 PHE   B CG   
1686 C CD1  . PHE   A 117 ? 0.483514 0.414559 0.517612 -0.0820373  -0.0273378  0.0359688   129 PHE   B CD1  
1687 C CD2  . PHE   A 117 ? 0.440203 0.416485 0.471794 -0.0713629  -0.0164425  0.0484666   129 PHE   B CD2  
1688 C CE1  . PHE   A 117 ? 0.531508 0.44229  0.561614 -0.0849674  -0.0212618  0.0502102   129 PHE   B CE1  
1689 C CE2  . PHE   A 117 ? 0.462094 0.421845 0.489044 -0.0750268  -0.0106819  0.062748    129 PHE   B CE2  
1690 C CZ   . PHE   A 117 ? 0.458134 0.384703 0.484639 -0.0816038  -0.0128743  0.0647678   129 PHE   B CZ   
1691 H H    . PHE   A 117 ? 0.370745 0.329643 0.376449 -0.0497875  -0.0458111  -0.00083227 129 PHE   B H    
1692 H HA   . PHE   A 117 ? 0.346058 0.317166 0.356049 -0.0480284  -0.0289131  0.0226419   129 PHE   B HA   
1693 H HB2  . PHE   A 117 ? 0.379283 0.381653 0.419234 -0.0665173  -0.0301529  0.0236839   129 PHE   B HB2  
1694 H HB3  . PHE   A 117 ? 0.400394 0.376997 0.441476 -0.0749111  -0.0382897  0.0152463   129 PHE   B HB3  
1695 H HD1  . PHE   A 117 ? 0.491986 0.412388 0.525434 -0.0835617  -0.0337125  0.0259768   129 PHE   B HD1  
1696 H HD2  . PHE   A 117 ? 0.424497 0.419596 0.454852 -0.0658574  -0.0151131  0.0471081   129 PHE   B HD2  
1697 H HE1  . PHE   A 117 ? 0.530426 0.414751 0.558301 -0.0889872  -0.0232382  0.0501514   129 PHE   B HE1  
1698 H HE2  . PHE   A 117 ? 0.452552 0.421595 0.474047 -0.0717246  -0.00575868 0.0708786   129 PHE   B HE2  
1699 H HZ   . PHE   A 117 ? 0.496536 0.408059 0.517331 -0.0823811  -0.00932934 0.0755448   129 PHE   B HZ   
1700 N N    . PHE   A 118 ? 0.361816 0.288865 0.362538 -0.0448255  -0.0273083  0.0256576   130 PHE   B N    
1701 C CA   . PHE   A 118 ? 0.368961 0.268744 0.364074 -0.0398656  -0.0267273  0.0264496   130 PHE   B CA   
1702 C C    . PHE   A 118 ? 0.387864 0.281152 0.38512  -0.0402616  -0.0228968  0.041168    130 PHE   B C    
1703 O O    . PHE   A 118 ? 0.435565 0.348866 0.433421 -0.0384804  -0.0198782  0.04955     130 PHE   B O    
1704 C CB   . PHE   A 118 ? 0.352778 0.252783 0.338774 -0.0254771  -0.0241022  0.0222592   130 PHE   B CB   
1705 C CG   . PHE   A 118 ? 0.406988 0.307253 0.382613 -0.0214667  -0.025531   0.0100889   130 PHE   B CG   
1706 C CD1  . PHE   A 118 ? 0.406989 0.324721 0.37956  -0.022676   -0.0263252  0.00826238  130 PHE   B CD1  
1707 C CD2  . PHE   A 118 ? 0.42743  0.307024 0.392017 -0.0144153  -0.0260184  0.00081129  130 PHE   B CD2  
1708 C CE1  . PHE   A 118 ? 0.405061 0.319146 0.362635 -0.0170806  -0.0269452  0.00021902  130 PHE   B CE1  
1709 C CE2  . PHE   A 118 ? 0.436875 0.316086 0.385943 -0.00919674 -0.0264938  -0.00912157 130 PHE   B CE2  
1710 C CZ   . PHE   A 118 ? 0.405901 0.302109 0.351281 -0.0108189  -0.0267457  -0.00798114 130 PHE   B CZ   
1711 H H    . PHE   A 118 ? 0.345394 0.285276 0.345949 -0.0422601  -0.0245479  0.0304773   130 PHE   B H    
1712 H HA   . PHE   A 118 ? 0.38847  0.273035 0.38321  -0.0444224  -0.0304467  0.0202912   130 PHE   B HA   
1713 H HB2  . PHE   A 118 ? 0.352377 0.267482 0.340484 -0.0232882  -0.0217358  0.0274853   130 PHE   B HB2  
1714 H HB3  . PHE   A 118 ? 0.381526 0.266696 0.365486 -0.0198361  -0.0231632  0.023345    130 PHE   B HB3  
1715 H HD1  . PHE   A 118 ? 0.388017 0.31837  0.366126 -0.0255404  -0.0257601  0.013302    130 PHE   B HD1  
1716 H HD2  . PHE   A 118 ? 0.443623 0.307435 0.40846  -0.0118984  -0.0259454  0.001188    130 PHE   B HD2  
1717 H HE1  . PHE   A 118 ? 0.395267 0.317198 0.348551 -0.0167452  -0.027814   0.00014199  130 PHE   B HE1  
1718 H HE2  . PHE   A 118 ? 0.451093 0.316271 0.389552 -0.00295058 -0.0262007  -0.0162315  130 PHE   B HE2  
1719 H HZ   . PHE   A 118 ? 0.422944 0.316303 0.354615 -0.0065032  -0.0270573  -0.0132228  130 PHE   B HZ   
1720 N N    . GLU   A 119 ? 0.436516 0.298018 0.429866 -0.0389437  -0.023909   0.0429054   131 GLU   B N    
1721 C CA   . GLU   A 119 ? 0.436629 0.282766 0.424621 -0.0300263  -0.0217232  0.0557235   131 GLU   B CA   
1722 C C    . GLU   A 119 ? 0.412947 0.247958 0.394971 -0.0111932  -0.0225249  0.0486874   131 GLU   B C    
1723 O O    . GLU   A 119 ? 0.502393 0.31476  0.47878  -0.0082514  -0.0244689  0.0363954   131 GLU   B O    
1724 C CB   . GLU   A 119 ? 0.454389 0.267841 0.440922 -0.0419619  -0.0214262  0.0651292   131 GLU   B CB   
1725 C CG   . GLU   A 119 ? 0.532915 0.32189  0.508145 -0.0302057  -0.0200467  0.0808729   131 GLU   B CG   
1726 C CD   . GLU   A 119 ? 0.539955 0.291524 0.510091 -0.0442221  -0.0177976  0.0947963   131 GLU   B CD   
1727 O OE1  . GLU   A 119 ? 0.576661 0.341739 0.548664 -0.0570614  -0.01183    0.109278    131 GLU   B OE1  
1728 O OE2  . GLU   A 119 ? 0.560111 0.266061 0.522563 -0.0415439  -0.0213992  0.0905766   131 GLU   B OE2  
1729 H H    . GLU   A 119 ? 0.440967 0.28766  0.433459 -0.0428959  -0.0270457  0.0352132   131 GLU   B H    
1730 H HA   . GLU   A 119 ? 0.41691  0.282403 0.405672 -0.0281584  -0.0197899  0.0629943   131 GLU   B HA   
1731 H HB2  . GLU   A 119 ? 0.462631 0.289722 0.455666 -0.0544617  -0.0190784  0.0700909   131 GLU   B HB2  
1732 H HB3  . GLU   A 119 ? 0.485371 0.278543 0.471163 -0.045535   -0.0246846  0.0560546   131 GLU   B HB3  
1733 H HG2  . GLU   A 119 ? 0.521509 0.297091 0.49211  -0.0167098  -0.0223783  0.0752559   131 GLU   B HG2  
1734 H HG3  . GLU   A 119 ? 0.497044 0.307749 0.47133  -0.0248926  -0.018451   0.0881543   131 GLU   B HG3  
1735 N N    . ILE   A 120 ? 0.455393 0.307267 0.438587 0.0016583   -0.0214161  0.0564685   132 ILE   B N    
1736 C CA   . ILE   A 120 ? 0.40583  0.263208 0.390541 0.020499    -0.0206285  0.051207    132 ILE   B CA   
1737 C C    . ILE   A 120 ? 0.458026 0.307131 0.440764 0.0353612   -0.0230887  0.0635316   132 ILE   B C    
1738 O O    . ILE   A 120 ? 0.443471 0.311679 0.427199 0.0346704   -0.0254379  0.0749652   132 ILE   B O    
1739 C CB   . ILE   A 120 ? 0.397371 0.294683 0.391526 0.0221717   -0.0181608  0.0460023   132 ILE   B CB   
1740 C CG1  . ILE   A 120 ? 0.397736 0.302054 0.389441 0.00918628  -0.016457   0.0366708   132 ILE   B CG1  
1741 C CG2  . ILE   A 120 ? 0.431759 0.337864 0.431663 0.0400023   -0.0145917  0.0402352   132 ILE   B CG2  
1742 C CD1  . ILE   A 120 ? 0.363367 0.297307 0.360895 0.00949433  -0.0130875  0.0334497   132 ILE   B CD1  
1743 H H    . ILE   A 120 ? 0.424105 0.286995 0.407898 -0.00127525 -0.021263   0.0651224   132 ILE   B H    
1744 H HA   . ILE   A 120 ? 0.440036 0.279449 0.420275 0.0237241   -0.0201005  0.0428511   132 ILE   B HA   
1745 H HB   . ILE   A 120 ? 0.39055  0.303922 0.388247 0.0208673   -0.0200192  0.0528281   132 ILE   B HB   
1746 H HG12 . ILE   A 120 ? 0.403547 0.291906 0.389442 0.0104745   -0.015925   0.0293816   132 ILE   B HG12 
1747 H HG13 . ILE   A 120 ? 0.386361 0.290549 0.37738  -0.00056838 -0.0183316  0.0400549   132 ILE   B HG13 
1748 H HG21 . ILE   A 120 ? 0.404229 0.336333 0.412393 0.0388072   -0.0125546  0.0389126   132 ILE   B HG21 
1749 H HG22 . ILE   A 120 ? 0.434547 0.325479 0.427964 0.0423383   -0.0120821  0.0322571   132 ILE   B HG22 
1750 H HG23 . ILE   A 120 ? 0.437183 0.338657 0.438667 0.0508082   -0.0167308  0.0457342   132 ILE   B HG23 
1751 H HD11 . ILE   A 120 ? 0.35956  0.308393 0.363792 0.0111769   -0.0145467  0.0388655   132 ILE   B HD11 
1752 H HD12 . ILE   A 120 ? 0.356684 0.293564 0.350714 0.00126406  -0.0134398  0.031015    132 ILE   B HD12 
1753 H HD13 . ILE   A 120 ? 0.371742 0.306315 0.369156 0.0162886   -0.0091699  0.028417    132 ILE   B HD13 
1754 N N    . GLU   A 121 ? 0.460548 0.283935 0.438587 0.0517409   -0.0230632  0.0589657   133 GLU   B N    
1755 C CA   . GLU   A 121 ? 0.537627 0.357514 0.514816 0.073221    -0.0264196  0.0692599   133 GLU   B CA   
1756 C C    . GLU   A 121 ? 0.513703 0.367741 0.505745 0.092738    -0.0240368  0.0601896   133 GLU   B C    
1757 O O    . GLU   A 121 ? 0.512023 0.356786 0.50255  0.101233    -0.018699   0.0468338   133 GLU   B O    
1758 C CB   . GLU   A 121 ? 0.553182 0.316203 0.513417 0.082298    -0.028677   0.0745954   133 GLU   B CB   
1759 C CG   . GLU   A 121 ? 0.636034 0.39539  0.593492 0.110758    -0.0333501  0.0853152   133 GLU   B CG   
1760 C CD   . GLU   A 121 ? 0.704039 0.399511 0.640216 0.122705    -0.0362274  0.0934429   133 GLU   B CD   
1761 O OE1  . GLU   A 121 ? 0.778462 0.428592 0.702899 0.104501    -0.0345381  0.0902112   133 GLU   B OE1  
1762 O OE2  . GLU   A 121 ? 0.675109 0.364389 0.606587 0.150838    -0.0411996  0.102429    133 GLU   B OE2  
1763 H H    . GLU   A 121 ? 0.487268 0.295406 0.461363 0.0513775   -0.0216659  0.0493949   133 GLU   B H    
1764 H HA   . GLU   A 121 ? 0.508053 0.342611 0.486074 0.0698015   -0.0289788  0.0792555   133 GLU   B HA   
1765 H HB2  . GLU   A 121 ? 0.58319  0.327874 0.536434 0.0675231   -0.0291137  0.0823885   133 GLU   B HB2  
1766 H HB3  . GLU   A 121 ? 0.58576  0.330522 0.542516 0.084608    -0.0269598  0.063104    133 GLU   B HB3  
1767 H HG2  . GLU   A 121 ? 0.614948 0.396495 0.582782 0.125389    -0.0321757  0.0769546   133 GLU   B HG2  
1768 H HG3  . GLU   A 121 ? 0.611457 0.392102 0.571133 0.108958    -0.0362081  0.0955568   133 GLU   B HG3  
1769 N N    . LEU   A 122 ? 0.444323 0.338072 0.45004  0.0999796   -0.0279751  0.0670837   134 LEU   B N    
1770 C CA   . LEU   A 122 ? 0.515287 0.450061 0.542331 0.117484    -0.0259957  0.0606679   134 LEU   B CA   
1771 C C    . LEU   A 122 ? 0.584246 0.506446 0.611046 0.148629    -0.0292144  0.0638428   134 LEU   B C    
1772 O O    . LEU   A 122 ? 0.535199 0.462376 0.561468 0.159941    -0.0387735  0.0760336   134 LEU   B O    
1773 C CB   . LEU   A 122 ? 0.496753 0.483781 0.543068 0.11034     -0.0311819  0.0640284   134 LEU   B CB   
1774 C CG   . LEU   A 122 ? 0.475708 0.515741 0.552506 0.121562    -0.0286792  0.0573941   134 LEU   B CG   
1775 C CD1  . LEU   A 122 ? 0.458181 0.501176 0.539511 0.119164    -0.0136845  0.0450581   134 LEU   B CD1  
1776 C CD2  . LEU   A 122 ? 0.417525 0.501469 0.511221 0.105835    -0.0355465  0.058479    134 LEU   B CD2  
1777 H H    . LEU   A 122 ? 0.468878 0.366677 0.471415 0.0936053   -0.0320785  0.0756074   134 LEU   B H    
1778 H HA   . LEU   A 122 ? 0.496704 0.434876 0.526297 0.114213    -0.0188048  0.0508251   134 LEU   B HA   
1779 H HB2  . LEU   A 122 ? 0.471982 0.462016 0.515813 0.0921153   -0.0291859  0.061733    134 LEU   B HB2  
1780 H HB3  . LEU   A 122 ? 0.50238  0.486272 0.543042 0.114777    -0.0389926  0.0733106   134 LEU   B HB3  
1781 H HG   . LEU   A 122 ? 0.488443 0.532053 0.570124 0.141706    -0.0325445  0.0604365   134 LEU   B HG   
1782 H HD11 . LEU   A 122 ? 0.484348 0.505543 0.557551 0.134101    -0.0106015  0.0424149   134 LEU   B HD11 
1783 H HD12 . LEU   A 122 ? 0.448974 0.530035 0.551225 0.119824    -0.0102463  0.0422158   134 LEU   B HD12 
1784 H HD13 . LEU   A 122 ? 0.450659 0.479084 0.520876 0.102578    -0.0107999  0.0427846   134 LEU   B HD13 
1785 H HD21 . LEU   A 122 ? 0.432924 0.511801 0.518069 0.107227    -0.0448317  0.0656348   134 LEU   B HD21 
1786 H HD22 . LEU   A 122 ? 0.409535 0.490297 0.499221 0.0882261   -0.031079   0.0547701   134 LEU   B HD22 
1787 H HD23 . LEU   A 122 ? 0.420575 0.540332 0.536827 0.112243    -0.0353552  0.0554091   134 LEU   B HD23 
1788 N N    . LEU   A 123 ? 0.594832 0.50464  0.621017 0.165169    -0.0214543  0.0521335   135 LEU   B N    
1789 C CA   . LEU   A 123 ? 0.646709 0.53556  0.668439 0.19852     -0.0238123  0.0530021   135 LEU   B CA   
1790 C C    . LEU   A 123 ? 0.651701 0.603975 0.705265 0.22112     -0.024431   0.0526062   135 LEU   B C    
1791 O O    . LEU   A 123 ? 0.757385 0.710097 0.812981 0.246577    -0.0339044  0.0614782   135 LEU   B O    
1792 C CB   . LEU   A 123 ? 0.652761 0.500999 0.657588 0.20848     -0.0152498  0.0377841   135 LEU   B CB   
1793 C CG   . LEU   A 123 ? 0.689287 0.478029 0.666807 0.185138    -0.01656    0.0349117   135 LEU   B CG   
1794 C CD1  . LEU   A 123 ? 0.714912 0.471875 0.675578 0.194827    -0.00943977 0.0149059   135 LEU   B CD1  
1795 C CD2  . LEU   A 123 ? 0.775015 0.510888 0.733822 0.184022    -0.0262445  0.050452    135 LEU   B CD2  
1796 H H    . LEU   A 123 ? 0.585819 0.49947  0.612347 0.156747    -0.0145078  0.0431488   135 LEU   B H    
1797 H HA   . LEU   A 123 ? 0.666342 0.525725 0.674467 0.200967    -0.0311357  0.0636216   135 LEU   B HA   
1798 H HB2  . LEU   A 123 ? 0.643444 0.522391 0.659593 0.207773    -0.00698606 0.0285315   135 LEU   B HB2  
1799 H HB3  . LEU   A 123 ? 0.697241 0.528686 0.697678 0.232972    -0.0170554  0.0379048   135 LEU   B HB3  
1800 H HG   . LEU   A 123 ? 0.659106 0.466679 0.641759 0.16292     -0.0155021  0.0355678   135 LEU   B HG   
1801 H HD11 . LEU   A 123 ? 0.695958 0.488813 0.667316 0.198263    -0.00176386 0.0074934   135 LEU   B HD11 
1802 H HD12 . LEU   A 123 ? 0.72064  0.449346 0.668095 0.176508    -0.0113032  0.0112365   135 LEU   B HD12 
1803 H HD13 . LEU   A 123 ? 0.755595 0.484841 0.70712  0.216293    -0.0109887  0.0132279   135 LEU   B HD13 
1804 H HD21 . LEU   A 123 ? 0.738661 0.494372 0.703691 0.173515    -0.0297203  0.0617992   135 LEU   B HD21 
1805 H HD22 . LEU   A 123 ? 0.793105 0.51359  0.747623 0.207801    -0.0286175  0.0527128   135 LEU   B HD22 
1806 H HD23 . LEU   A 123 ? 0.777357 0.47476  0.721441 0.170283    -0.0264552  0.046898    135 LEU   B HD23 
1807 N N    . ASP   A 124 ? 0.551861 0.558279 0.630703 0.211062    -0.0146859  0.0433367   136 ASP   B N    
1808 C CA   . ASP   A 124 ? 0.574947 0.649122 0.691179 0.228683    -0.0124673  0.0409556   136 ASP   B CA   
1809 C C    . ASP   A 124 ? 0.556558 0.679624 0.695434 0.204318    -0.0002945  0.0339469   136 ASP   B C    
1810 O O    . ASP   A 124 ? 0.533726 0.63178  0.654156 0.183388    0.00829736  0.0288906   136 ASP   B O    
1811 C CB   . ASP   A 124 ? 0.659192 0.723927 0.774791 0.266817    -0.0058626  0.0336113   136 ASP   B CB   
1812 C CG   . ASP   A 124 ? 0.70471  0.833165 0.858045 0.297101    -0.00710955 0.0335024   136 ASP   B CG   
1813 O OD1  . ASP   A 124 ? 0.683062 0.869024 0.867434 0.287688    -0.0164493  0.0398045   136 ASP   B OD1  
1814 O OD2  . ASP   A 124 ? 0.748988 0.867634 0.899359 0.331049    0.0005525   0.0256247   136 ASP   B OD2  
1815 H H    . ASP   A 124 ? 0.55718  0.558397 0.630299 0.192225    -0.00910418 0.0388934   136 ASP   B H    
1816 H HA   . ASP   A 124 ? 0.57726  0.669808 0.702995 0.231864    -0.0236271  0.0489899   136 ASP   B HA   
1817 H HB2  . ASP   A 124 ? 0.6896   0.705278 0.78159  0.277414    -0.0118978  0.0370367   136 ASP   B HB2  
1818 H HB3  . ASP   A 124 ? 0.657512 0.717115 0.767697 0.26358     0.00626928  0.0241078   136 ASP   B HB3  
1819 N N    . PHE   A 125 ? 0.610146 0.80313  0.789628 0.20795     2.411e-05   0.0339868   137 PHE   B N    
1820 C CA   . PHE   A 125 ? 0.562129 0.805299 0.768172 0.188536    0.0145559   0.028466    137 PHE   B CA   
1821 C C    . PHE   A 125 ? 0.556574 0.875605 0.810983 0.206721    0.0182873   0.026588    137 PHE   B C    
1822 O O    . PHE   A 125 ? 0.661204 1.00676  0.934834 0.223469    0.00223733  0.0310928   137 PHE   B O    
1823 C CB   . PHE   A 125 ? 0.564414 0.813895 0.771872 0.151851    0.00714028  0.0325946   137 PHE   B CB   
1824 C CG   . PHE   A 125 ? 0.547201 0.820128 0.76886  0.148629    -0.0141451  0.0392609   137 PHE   B CG   
1825 C CD1  . PHE   A 125 ? 0.55098  0.778764 0.741734 0.150139    -0.0290409  0.0466843   137 PHE   B CD1  
1826 C CD2  . PHE   A 125 ? 0.537381 0.877725 0.801615 0.139754    -0.0187842  0.0377806   137 PHE   B CD2  
1827 C CE1  . PHE   A 125 ? 0.511584 0.760204 0.70873  0.147935    -0.0480296  0.0524259   137 PHE   B CE1  
1828 C CE2  . PHE   A 125 ? 0.474547 0.836076 0.747996 0.136416    -0.0408081  0.0414701   137 PHE   B CE2  
1829 C CZ   . PHE   A 125 ? 0.518531 0.83353  0.755763 0.142079    -0.055236   0.0487104   137 PHE   B CZ   
1830 H H    . PHE   A 125 ? 0.594136 0.804464 0.785673 0.222736    -0.00960874 0.0382023   137 PHE   B H    
1831 H HA   . PHE   A 125 ? 0.576956 0.799544 0.767363 0.187733    0.0272289   0.0230204   137 PHE   B HA   
1832 H HB2  . PHE   A 125 ? 0.540941 0.820096 0.765339 0.138563    0.0170889   0.0298557   137 PHE   B HB2  
1833 H HB3  . PHE   A 125 ? 0.55454  0.760708 0.73373  0.1416      0.00723112  0.0329177   137 PHE   B HB3  
1834 H HD1  . PHE   A 125 ? 0.555645 0.739061 0.720388 0.152857    -0.0260103  0.047812    137 PHE   B HD1  
1835 H HD2  . PHE   A 125 ? 0.514953 0.888053 0.802034 0.136301    -0.00710443 0.0340039   137 PHE   B HD2  
1836 H HE1  . PHE   A 125 ? 0.536007 0.754403 0.70997  0.150151    -0.0562953  0.0586758   137 PHE   B HE1  
1837 H HE2  . PHE   A 125 ? 0.486612 0.895146 0.790589 0.129814    -0.0456438  0.0389775   137 PHE   B HE2  
1838 H HZ   . PHE   A 125 ? 0.507897 0.836787 0.747399 0.14116     -0.0699658  0.0511767   137 PHE   B HZ   
1839 N N    . LYS   A 126 ? 0.611542 0.967821 0.885361 0.204616    0.0399044   0.0204362   138 LYS   B N    
1840 C CA   . LYS   A 126 ? 0.568096 1.00541  0.893688 0.22005     0.0480851   0.0182091   138 LYS   B CA   
1841 C C    . LYS   A 126 ? 0.515899 1.00091  0.869838 0.183804    0.0626036   0.0188703   138 LYS   B C    
1842 O O    . LYS   A 126 ? 0.423354 0.872184 0.748526 0.161555    0.0747659   0.0187474   138 LYS   B O    
1843 C CB   . LYS   A 126 ? 0.523979 0.961504 0.845045 0.259268    0.0653182   0.0104268   138 LYS   B CB   
1844 H H    . LYS   A 126 ? 0.585701 0.917897 0.839942 0.193143    0.0505516   0.0178977   138 LYS   B H    
1845 H HA   . LYS   A 126 ? 0.553922 1.01533  0.89892  0.227907    0.0324435   0.0214095   138 LYS   B HA   
1848 N N    . GLY   A 127 ? 0.538571 1.10454  0.94923  0.178066    0.0610318   0.0198172   139 GLY   B N    
1849 C CA   . GLY   A 127 ? 0.522775 1.13174  0.963297 0.139018    0.0731789   0.0218192   139 GLY   B CA   
1850 C C    . GLY   A 127 ? 0.592187 1.2161   1.03256  0.1404      0.10713     0.0206003   139 GLY   B C    
1851 O O    . GLY   A 127 ? 0.570774 1.20805  1.01257  0.176485    0.119503    0.0158603   139 GLY   B O    
1852 H H    . GLY   A 127 ? 0.536326 1.13103  0.968004 0.198539    0.05166     0.0193359   139 GLY   B H    
1853 H HA2  . GLY   A 127 ? 0.52296  1.09519  0.94091  0.115369    0.0665983   0.024043    139 GLY   B HA2  
1854 H HA3  . GLY   A 127 ? 0.525845 1.19051  1.0083   0.135235    0.065533    0.0218887   139 GLY   B HA3  
1855 N N    . GLU   A 128 ? 0.637963 1.25566  1.07178  0.104057    0.122658    0.0250228   140 GLU   B N    
1856 C CA   . GLU   A 128 ? 0.601022 1.25443  1.04649  0.102674    0.156574    0.0266717   140 GLU   B CA   
1857 C C    . GLU   A 128 ? 0.608642 1.35703  1.12017  0.123581    0.162703    0.0241766   140 GLU   B C    
1858 O O    . GLU   A 128 ? 0.601176 1.39466  1.1572   0.116671    0.140346    0.0239704   140 GLU   B O    
1859 C CB   . GLU   A 128 ? 0.587079 1.23159  1.02592  0.0581122   0.171355    0.0351443   140 GLU   B CB   
1860 O OXT  . GLU   A 128 ? 0.561376 1.33376  1.07464  0.151573    0.186847    0.0208919   140 GLU   B OXT  
1861 H H    . GLU   A 128 ? 0.601857 1.19215  1.02217  0.081368    0.112865    0.0275066   140 GLU   B H    
1862 H HA   . GLU   A 128 ? 0.62563  1.24305  1.03567  0.122869    0.165511    0.0232692   140 GLU   B HA   
1865 N N    . GLY   B 1   ? 0.484267 0.826355 0.559436 0.251944    -0.0982243  0.159787    13  GLY   A N    
1866 C CA   . GLY   B 1   ? 0.5149   0.792532 0.588838 0.257054    -0.0772716  0.173478    13  GLY   A CA   
1867 C C    . GLY   B 1   ? 0.539752 0.782672 0.570429 0.231314    -0.0655589  0.161408    13  GLY   A C    
1868 O O    . GLY   B 1   ? 0.471198 0.734236 0.462127 0.216196    -0.0747387  0.153273    13  GLY   A O    
1869 H H1   . GLY   B 1   ? 0.498245 0.863429 0.604631 0.268234    -0.104693   0.166232    13  GLY   A H1   
1870 H H2   . GLY   B 1   ? 0.467323 0.813002 0.543275 0.234153    -0.0944039  0.135933    13  GLY   A H2   
1871 H H3   . GLY   B 1   ? 0.506544 0.86347  0.551373 0.249699    -0.108746   0.168252    13  GLY   A H3   
1872 H HA2  . GLY   B 1   ? 0.54717  0.819031 0.618596 0.274821    -0.0807786  0.201239    13  GLY   A HA2  
1873 H HA3  . GLY   B 1   ? 0.505461 0.76854  0.612286 0.260305    -0.0670063  0.163351    13  GLY   A HA3  
1874 N N    . ALA   B 2   ? 0.554036 0.74563  0.595769 0.226954    -0.0454855  0.158644    14  ALA   A N    
1875 C CA   . ALA   B 2   ? 0.497189 0.656875 0.504105 0.208882    -0.0345354  0.155228    14  ALA   A CA   
1876 C C    . ALA   B 2   ? 0.490721 0.664431 0.476495 0.183548    -0.0388653  0.123377    14  ALA   A C    
1877 O O    . ALA   B 2   ? 0.52669  0.700838 0.475175 0.172986    -0.0402801  0.121064    14  ALA   A O    
1878 C CB   . ALA   B 2   ? 0.51652  0.625363 0.545543 0.207089    -0.0148949  0.155739    14  ALA   A CB   
1879 H H    . ALA   B 2   ? 0.534224 0.712303 0.60626  0.234993    -0.0386937  0.157561    14  ALA   A H    
1880 H HA   . ALA   B 2   ? 0.538344 0.702226 0.5208   0.214357    -0.0376136  0.17408     14  ALA   A HA   
1881 H HB1  . ALA   B 2   ? 0.533902 0.628813 0.57271  0.221405    -0.0112438  0.177929    14  ALA   A HB1  
1882 H HB2  . ALA   B 2   ? 0.493263 0.599359 0.545567 0.20402     -0.0121708  0.138844    14  ALA   A HB2  
1883 H HB3  . ALA   B 2   ? 0.502658 0.595683 0.513725 0.194187    -0.00841209 0.150439    14  ALA   A HB3  
1884 N N    . PRO   B 3   ? 0.444947 0.629617 0.452182 0.172738    -0.0400315  0.0983967   15  PRO   A N    
1885 C CA   . PRO   B 3   ? 0.424437 0.62072  0.411889 0.148622    -0.045364   0.0729152   15  PRO   A CA   
1886 C C    . PRO   B 3   ? 0.441589 0.675338 0.40037  0.144159    -0.0619875  0.0713402   15  PRO   A C    
1887 O O    . PRO   B 3   ? 0.437282 0.659681 0.362643 0.129879    -0.0620625  0.0615615   15  PRO   A O    
1888 C CB   . PRO   B 3   ? 0.441087 0.648588 0.459171 0.140524    -0.0426673  0.0530668   15  PRO   A CB   
1889 C CG   . PRO   B 3   ? 0.452771 0.637477 0.504207 0.15817     -0.0301642  0.0623318   15  PRO   A CG   
1890 C CD   . PRO   B 3   ? 0.506937 0.692503 0.558174 0.182111    -0.0343849  0.0924362   15  PRO   A CD   
1891 H HA   . PRO   B 3   ? 0.426634 0.594951 0.400846 0.139476    -0.0378137  0.0687268   15  PRO   A HA   
1892 H HB2  . PRO   B 3   ? 0.434739 0.677596 0.461518 0.141463    -0.0517904  0.0494101   15  PRO   A HB2  
1893 H HB3  . PRO   B 3   ? 0.4216   0.614692 0.429943 0.123538    -0.0390234  0.0387608   15  PRO   A HB3  
1894 H HG2  . PRO   B 3   ? 0.451911 0.653998 0.527536 0.160879    -0.0291197  0.0534956   15  PRO   A HG2  
1895 H HG3  . PRO   B 3   ? 0.450612 0.603846 0.498462 0.150864    -0.0208424  0.0579086   15  PRO   A HG3  
1896 H HD2  . PRO   B 3   ? 0.491984 0.707975 0.558471 0.194205    -0.0430369  0.0980063   15  PRO   A HD2  
1897 H HD3  . PRO   B 3   ? 0.490687 0.647367 0.554572 0.190297    -0.0245216  0.101387    15  PRO   A HD3  
1898 N N    . ALA   B 4   ? 0.459543 0.735692 0.429877 0.159602    -0.0759919  0.0836327   16  ALA   A N    
1899 C CA   . ALA   B 4   ? 0.465499 0.783649 0.409092 0.153202    -0.0947404  0.0789755   16  ALA   A CA   
1900 C C    . ALA   B 4   ? 0.518214 0.82184  0.414718 0.15579     -0.0937221  0.0922282   16  ALA   A C    
1901 O O    . ALA   B 4   ? 0.482811 0.802971 0.345368 0.141908    -0.102613   0.0775814   16  ALA   A O    
1902 C CB   . ALA   B 4   ? 0.486656 0.8591   0.455875 0.171394    -0.11277    0.091904    16  ALA   A CB   
1903 H H    . ALA   B 4   ? 0.458444 0.73829  0.454309 0.174271    -0.074684   0.0941224   16  ALA   A H    
1904 H HA   . ALA   B 4   ? 0.46106  0.783091 0.400398 0.134164    -0.0962603  0.0574493   16  ALA   A HA   
1905 H HB1  . ALA   B 4   ? 0.467043 0.852109 0.468483 0.169699    -0.111377   0.0816324   16  ALA   A HB1  
1906 H HB2  . ALA   B 4   ? 0.500583 0.865998 0.474066 0.190952    -0.111798   0.115139    16  ALA   A HB2  
1907 H HB3  . ALA   B 4   ? 0.498169 0.901178 0.448601 0.165277    -0.126865   0.0872457   16  ALA   A HB3  
1908 N N    . THR   B 5   ? 0.514669 0.791714 0.410478 0.173957    -0.0829187  0.120358    17  THR   A N    
1909 C CA   . THR   B 5   ? 0.557554 0.822774 0.409482 0.176246    -0.077525   0.135753    17  THR   A CA   
1910 C C    . THR   B 5   ? 0.526712 0.76065  0.358848 0.15522     -0.0635423  0.110501    17  THR   A C    
1911 O O    . THR   B 5   ? 0.521736 0.761101 0.313072 0.14838     -0.0630428  0.104073    17  THR   A O    
1912 C CB   . THR   B 5   ? 0.590442 0.826773 0.451331 0.196018    -0.0645563  0.171883    17  THR   A CB   
1913 O OG1  . THR   B 5   ? 0.58657  0.850525 0.468631 0.21803     -0.0795543  0.195626    17  THR   A OG1  
1914 C CG2  . THR   B 5   ? 0.623587 0.849626 0.437441 0.195625    -0.0545988  0.189128    17  THR   A CG2  
1915 H H    . THR   B 5   ? 0.515075 0.781131 0.438771 0.184403    -0.0776953  0.12971     17  THR   A H    
1916 H HA   . THR   B 5   ? 0.576927 0.873852 0.406176 0.17767     -0.0910599  0.138335    17  THR   A HA   
1917 H HB   . THR   B 5   ? 0.562001 0.768299 0.447328 0.193591    -0.0520711  0.167217    17  THR   A HB   
1919 H HG21 . THR   B 5   ? 0.646809 0.863112 0.464229 0.209041    -0.050467   0.216932    17  THR   A HG21 
1920 H HG22 . THR   B 5   ? 0.643066 0.897644 0.426528 0.19257     -0.0657273  0.184704    17  THR   A HG22 
1921 H HG23 . THR   B 5   ? 0.610537 0.812131 0.421667 0.184667    -0.040799   0.176543    17  THR   A HG23 
1922 N N    . VAL   B 6   ? 0.504053 0.706335 0.364117 0.146175    -0.0523567  0.0962086   18  VAL   A N    
1923 C CA   . VAL   B 6   ? 0.452064 0.626715 0.29869  0.128946    -0.0424717  0.0743079   18  VAL   A CA   
1924 C C    . VAL   B 6   ? 0.455349 0.648638 0.28337  0.111401    -0.0549854  0.0462925   18  VAL   A C    
1925 O O    . VAL   B 6   ? 0.476518 0.661084 0.276088 0.10362     -0.0512784  0.0332431   18  VAL   A O    
1926 C CB   . VAL   B 6   ? 0.435643 0.574995 0.313348 0.1223      -0.0313291  0.0664017   18  VAL   A CB   
1927 C CG1  . VAL   B 6   ? 0.411937 0.525809 0.276934 0.108229    -0.0242189  0.0479065   18  VAL   A CG1  
1928 C CG2  . VAL   B 6   ? 0.389917 0.507357 0.289615 0.135942    -0.018546   0.0893719   18  VAL   A CG2  
1929 H H    . VAL   B 6   ? 0.477865 0.676014 0.365757 0.151278    -0.0511756  0.0998551   18  VAL   A H    
1930 H HA   . VAL   B 6   ? 0.479778 0.646073 0.307455 0.13221     -0.034526   0.0822234   18  VAL   A HA   
1931 H HB   . VAL   B 6   ? 0.406018 0.554573 0.29934  0.117676    -0.037663   0.0574972   18  VAL   A HB   
1932 H HG11 . VAL   B 6   ? 0.435226 0.549934 0.28014  0.111139    -0.0197135  0.0511423   18  VAL   A HG11 
1933 H HG12 . VAL   B 6   ? 0.412153 0.530994 0.272932 0.0974448   -0.0316725  0.0317148   18  VAL   A HG12 
1934 H HG13 . VAL   B 6   ? 0.402783 0.495048 0.285048 0.10713     -0.0166475  0.0489321   18  VAL   A HG13 
1935 H HG21 . VAL   B 6   ? 0.386328 0.482606 0.302297 0.129846    -0.0121512  0.081859    18  VAL   A HG21 
1936 H HG22 . VAL   B 6   ? 0.407854 0.537187 0.321487 0.145772    -0.0230983  0.099485    18  VAL   A HG22 
1937 H HG23 . VAL   B 6   ? 0.42095  0.533665 0.305394 0.140481    -0.0119313  0.101269    18  VAL   A HG23 
1938 N N    . THR   B 7   ? 0.465618 0.685861 0.311112 0.104802    -0.068649   0.0360742   19  THR   A N    
1939 C CA   . THR   B 7   ? 0.507379 0.748506 0.336784 0.0860041   -0.0815018  0.0109564   19  THR   A CA   
1940 C C    . THR   B 7   ? 0.609538 0.874977 0.397357 0.0893112   -0.0897129  0.0113168   19  THR   A C    
1941 O O    . THR   B 7   ? 0.617969 0.873031 0.379124 0.0750632   -0.0889585  -0.0114571  19  THR   A O    
1942 C CB   . THR   B 7   ? 0.543345 0.823747 0.401875 0.0811957   -0.0950443  0.0059631   19  THR   A CB   
1943 O OG1  . THR   B 7   ? 0.435281 0.694565 0.324674 0.0749362   -0.0853078  0.00174295  19  THR   A OG1  
1944 C CG2  . THR   B 7   ? 0.63268  0.94028  0.478886 0.058873    -0.109675   -0.0196063  19  THR   A CG2  
1945 H H    . THR   B 7   ? 0.455499 0.681476 0.325349 0.111374    -0.0690928  0.0438287   19  THR   A H    
1946 H HA   . THR   B 7   ? 0.512578 0.728021 0.339503 0.0737442   -0.0757866  -0.00347777 19  THR   A HA   
1947 H HB   . THR   B 7   ? 0.535171 0.840123 0.401712 0.0964066   -0.100872   0.0220053   19  THR   A HB   
1949 H HG21 . THR   B 7   ? 0.594232 0.917909 0.464653 0.0509301   -0.113185   -0.0256532  19  THR   A HG21 
1950 H HG22 . THR   B 7   ? 0.612951 0.893158 0.44313  0.0468646   -0.104487   -0.033357   19  THR   A HG22 
1951 H HG23 . THR   B 7   ? 0.629511 0.966285 0.460441 0.0639471   -0.120592   -0.0165782  19  THR   A HG23 
1952 N N    . GLU   B 8   ? 0.619815 0.912493 0.399915 0.109169    -0.0957006  0.0382896   20  GLU   A N    
1953 C CA   . GLU   B 8   ? 0.706506 1.03097  0.441997 0.112451    -0.106475   0.0419328   20  GLU   A CA   
1954 C C    . GLU   B 8   ? 0.714981 1.01151  0.410693 0.114478    -0.0878955  0.0446545   20  GLU   A C    
1955 O O    . GLU   B 8   ? 0.79133  1.10886  0.441503 0.11035     -0.0928507  0.035698    20  GLU   A O    
1956 C CB   . GLU   B 8   ? 0.718922 1.08477  0.461684 0.133946    -0.122339   0.0741047   20  GLU   A CB   
1957 H H    . GLU   B 8   ? 0.61763  0.908172 0.420379 0.120995    -0.093171   0.0552717   20  GLU   A H    
1958 H HA   . GLU   B 8   ? 0.700827 1.04252  0.427054 0.0981997   -0.116933   0.0197754   20  GLU   A HA   
1961 N N    . GLN   B 9   ? 0.6375   0.896214 0.348358 0.123729    -0.0671281  0.0622162   21  GLN   A N    
1962 C CA   . GLN   B 9   ? 0.67844  0.921126 0.357735 0.12856     -0.0480392  0.0722888   21  GLN   A CA   
1963 C C    . GLN   B 9   ? 0.607477 0.806201 0.304921 0.121089    -0.0267658  0.0565485   21  GLN   A C    
1964 O O    . GLN   B 9   ? 0.677525 0.866343 0.353323 0.122564    -0.00885391 0.0575106   21  GLN   A O    
1965 C CB   . GLN   B 9   ? 0.708773 0.952725 0.384946 0.147559    -0.0409846  0.115458    21  GLN   A CB   
1966 H H    . GLN   B 9   ? 0.62759  0.872244 0.370191 0.126443    -0.0642406  0.0677286   21  GLN   A H    
1967 H HA   . GLN   B 9   ? 0.698634 0.959527 0.343064 0.123451    -0.0524256  0.060351    21  GLN   A HA   
1970 N N    . GLY   B 10  ? 0.577168 0.753809 0.313284 0.11355     -0.0286744  0.0434125   22  GLY   A N    
1971 C CA   . GLY   B 10  ? 0.586431 0.72414  0.346394 0.110137    -0.0119778  0.0368309   22  GLY   A CA   
1972 C C    . GLY   B 10  ? 0.561646 0.686549 0.301926 0.101238    -0.004193   0.00881183  22  GLY   A C    
1973 O O    . GLY   B 10  ? 0.576467 0.712021 0.297489 0.0912299   -0.0157086  -0.0140209  22  GLY   A O    
1974 H H    . GLY   B 10  ? 0.570537 0.758891 0.318249 0.10999     -0.0410543  0.0385015   22  GLY   A H    
1975 H HA2  . GLY   B 10  ? 0.570087 0.700213 0.336247 0.118252    -0.0007467  0.0552174   22  GLY   A HA2  
1976 H HA3  . GLY   B 10  ? 0.542322 0.669734 0.327438 0.105693    -0.0167885  0.0323771   22  GLY   A HA3  
1977 N N    . GLU   B 11  ? 0.5333   0.636278 0.283699 0.104923    0.0151605   0.00970839  23  GLU   A N    
1978 C CA   . GLU   B 11  ? 0.549108 0.635011 0.295178 0.100518    0.0249755   -0.0168245  23  GLU   A CA   
1979 C C    . GLU   B 11  ? 0.501376 0.55856  0.279034 0.0916338   0.0155783   -0.0317824  23  GLU   A C    
1980 O O    . GLU   B 11  ? 0.438855 0.484233 0.24784  0.091666    0.0126719   -0.0180563  23  GLU   A O    
1981 C CB   . GLU   B 11  ? 0.581011 0.661427 0.333527 0.109046    0.0499354   -0.00936716 23  GLU   A CB   
1982 H H    . GLU   B 11  ? 0.533546 0.632423 0.297676 0.111015    0.0229634   0.0279059   23  GLU   A H    
1983 H HA   . GLU   B 11  ? 0.574129 0.672151 0.29193  0.096971    0.0211431   -0.0314688  23  GLU   A HA   
1986 N N    . ASP   B 12  ? 0.489329 0.534844 0.255436 0.0829604   0.0103944   -0.0597469  24  ASP   A N    
1987 C CA   . ASP   B 12  ? 0.470419 0.48432  0.261143 0.0739255   0.00205888  -0.0716881  24  ASP   A CA   
1988 C C    . ASP   B 12  ? 0.458086 0.446109 0.275154 0.0824108   0.0147431   -0.0740371  24  ASP   A C    
1989 O O    . ASP   B 12  ? 0.487258 0.471005 0.295782 0.088401    0.0271283   -0.0911365  24  ASP   A O    
1990 C CB   . ASP   B 12  ? 0.4853   0.492469 0.255941 0.0599754   -0.00851193 -0.0993177  24  ASP   A CB   
1991 C CG   . ASP   B 12  ? 0.478439 0.447039 0.271167 0.0489797   -0.0165976  -0.108785   24  ASP   A CG   
1992 O OD1  . ASP   B 12  ? 0.464971 0.41467  0.286301 0.0535141   -0.0154942  -0.0936529  24  ASP   A OD1  
1993 O OD2  . ASP   B 12  ? 0.512522 0.469938 0.292842 0.0348772   -0.024513   -0.130385   24  ASP   A OD2  
1994 H H    . ASP   B 12  ? 0.522732 0.578852 0.263775 0.0821395   0.0121045   -0.0715205  24  ASP   A H    
1995 H HA   . ASP   B 12  ? 0.444378 0.459277 0.249024 0.0706578   -0.00550983 -0.0597401  24  ASP   A HA   
1996 H HB2  . ASP   B 12  ? 0.488301 0.516942 0.246877 0.0539876   -0.0180177  -0.0972346  24  ASP   A HB2  
1997 H HB3  . ASP   B 12  ? 0.514984 0.522179 0.26932  0.0631246   -0.00066569 -0.113906   24  ASP   A HB3  
1998 N N    . ILE   B 13  ? 0.464464 0.441607 0.313827 0.0844662   0.0132376   -0.0573623  25  ILE   A N    
1999 C CA   . ILE   B 13  ? 0.458524 0.422281 0.338342 0.0941956   0.0241637   -0.0561651  25  ILE   A CA   
2000 C C    . ILE   B 13  ? 0.4781   0.409486 0.378796 0.0899688   0.0118198   -0.0639232  25  ILE   A C    
2001 O O    . ILE   B 13  ? 0.51999  0.442364 0.451625 0.0986393   0.015772    -0.0613123  25  ILE   A O    
2002 C CB   . ILE   B 13  ? 0.395324 0.371591 0.299109 0.0988899   0.0309076   -0.0324543  25  ILE   A CB   
2003 C CG1  . ILE   B 13  ? 0.406162 0.37798  0.318766 0.0903163   0.0162704   -0.0206609  25  ILE   A CG1  
2004 C CG2  . ILE   B 13  ? 0.454326 0.456804 0.339435 0.104883    0.0463937   -0.0200171  25  ILE   A CG2  
2005 C CD1  . ILE   B 13  ? 0.390543 0.364654 0.333578 0.0921523   0.0203171   -0.00385882 25  ILE   A CD1  
2006 H H    . ILE   B 13  ? 0.436854 0.416877 0.290808 0.0795777   0.00507003  -0.0478878  25  ILE   A H    
2007 H HA   . ILE   B 13  ? 0.47533  0.443579 0.347582 0.100291    0.0355656   -0.0660709  25  ILE   A HA   
2008 H HB   . ILE   B 13  ? 0.414098 0.384069 0.341534 0.103541    0.0358581   -0.0332404  25  ILE   A HB   
2009 H HG12 . ILE   B 13  ? 0.400066 0.383135 0.294805 0.0876624   0.0130181   -0.0178187  25  ILE   A HG12 
2010 H HG13 . ILE   B 13  ? 0.397503 0.353853 0.313396 0.084758    0.00630983  -0.0277114  25  ILE   A HG13 
2011 H HG21 . ILE   B 13  ? 0.427419 0.432835 0.331683 0.107066    0.0524698   -0.00616733 25  ILE   A HG21 
2012 H HG22 . ILE   B 13  ? 0.442174 0.453457 0.307186 0.101805    0.0394872   -0.0162199  25  ILE   A HG22 
2013 H HG23 . ILE   B 13  ? 0.460898 0.468542 0.335375 0.109256    0.0570983   -0.0295346  25  ILE   A HG23 
2014 H HD11 . ILE   B 13  ? 0.388219 0.357444 0.350928 0.0954502   0.0241361   -0.0060987  25  ILE   A HD11 
2015 H HD12 . ILE   B 13  ? 0.375543 0.344191 0.322989 0.0858834   0.0104441   -0.0011713  25  ILE   A HD12 
2016 H HD13 . ILE   B 13  ? 0.390801 0.37718  0.32995  0.0957999   0.0291069   0.00594547  25  ILE   A HD13 
2017 N N    . THR   B 14  ? 0.482467 0.397637 0.366481 0.0774572   -0.00151444 -0.0746864  26  THR   A N    
2018 C CA   . THR   B 14  ? 0.509781 0.388244 0.40687  0.0728781   -0.0118797  -0.0814493  26  THR   A CA   
2019 C C    . THR   B 14  ? 0.537251 0.394905 0.437451 0.0824331   -0.00308022 -0.104129   26  THR   A C    
2020 O O    . THR   B 14  ? 0.528282 0.398652 0.405456 0.0844403   0.00794265  -0.122769   26  THR   A O    
2021 C CB   . THR   B 14  ? 0.491629 0.358953 0.371818 0.0527252   -0.026788   -0.082861   26  THR   A CB   
2022 O OG1  . THR   B 14  ? 0.523325 0.397034 0.376896 0.044372    -0.0259466  -0.103134   26  THR   A OG1  
2023 C CG2  . THR   B 14  ? 0.471452 0.360057 0.352395 0.0448643   -0.0330846  -0.0639484  26  THR   A CG2  
2024 H H    . THR   B 14  ? 0.489334 0.417096 0.354034 0.071096    -0.00446827 -0.0766511  26  THR   A H    
2025 H HA   . THR   B 14  ? 0.4873   0.36105  0.405146 0.076558    -0.0148028  -0.0695806  26  THR   A HA   
2026 H HB   . THR   B 14  ? 0.511994 0.351893 0.4015   0.0498067   -0.0331412  -0.0829177  26  THR   A HB   
2028 H HG21 . THR   B 14  ? 0.471794 0.356068 0.344185 0.0316565   -0.040642   -0.0656325  26  THR   A HG21 
2029 H HG22 . THR   B 14  ? 0.457    0.370137 0.331666 0.0491667   -0.0276506  -0.0612599  26  THR   A HG22 
2030 H HG23 . THR   B 14  ? 0.45448  0.337115 0.351546 0.0485759   -0.0346763  -0.0532341  26  THR   A HG23 
2031 N N    . SER   B 15  ? 0.581403 0.406565 0.50959  0.088803    -0.0088255  -0.103158   27  SER   A N    
2032 C CA   . SER   B 15  ? 0.607778 0.405319 0.547476 0.100314    -0.0014554  -0.125495   27  SER   A CA   
2033 C C    . SER   B 15  ? 0.651202 0.420729 0.564291 0.084965    -0.00697299 -0.14662    27  SER   A C    
2034 O O    . SER   B 15  ? 0.688093 0.446637 0.592782 0.0900149   0.00441238  -0.175522   27  SER   A O    
2035 C CB   . SER   B 15  ? 0.6226   0.392799 0.603893 0.113125    -0.0100964  -0.114167   27  SER   A CB   
2036 O OG   . SER   B 15  ? 0.645893 0.448664 0.654123 0.124328    -0.00546942 -0.0976046  27  SER   A OG   
2037 H H    . SER   B 15  ? 0.554117 0.374349 0.494746 0.0865891   -0.0178868  -0.0882564  27  SER   A H    
2038 H HA   . SER   B 15  ? 0.616977 0.433539 0.556184 0.110083    0.0133556   -0.134996   27  SER   A HA   
2039 H HB2  . SER   B 15  ? 0.63361  0.384622 0.611715 0.102989    -0.0244946  -0.102978   27  SER   A HB2  
2040 H HB3  . SER   B 15  ? 0.662398 0.413657 0.655387 0.123285    -0.00433887 -0.129558   27  SER   A HB3  
2042 N N    . LYS   B 16  ? 0.606877 0.364267 0.508645 0.064787    -0.023431   -0.134181   28  LYS   A N    
2043 C CA   . LYS   B 16  ? 0.698841 0.428933 0.581006 0.04562     -0.0296315  -0.152542   28  LYS   A CA   
2044 C C    . LYS   B 16  ? 0.663949 0.431251 0.512701 0.0342867   -0.0254117  -0.169836   28  LYS   A C    
2045 O O    . LYS   B 16  ? 0.659968 0.41312  0.492473 0.0169186   -0.0299738  -0.189992   28  LYS   A O    
2046 C CB   . LYS   B 16  ? 0.76109  0.473392 0.640896 0.0240836   -0.0459512  -0.133169   28  LYS   A CB   
2047 C CG   . LYS   B 16  ? 0.819906 0.494345 0.722985 0.0287776   -0.0562358  -0.110496   28  LYS   A CG   
2048 C CD   . LYS   B 16  ? 1.00851  0.658449 0.89729  0.00063332  -0.0680587  -0.10099    28  LYS   A CD   
2049 C CE   . LYS   B 16  ? 1.02351  0.68067  0.911502 -0.00823385 -0.0787264  -0.0690086  28  LYS   A CE   
2050 N NZ   . LYS   B 16  ? 1.10139  0.71157  1.00414  -0.00208115 -0.0893864  -0.0502444  28  LYS   A NZ   
2051 H H    . LYS   B 16  ? 0.601674 0.368459 0.508708 0.0618947   -0.0299121  -0.115282   28  LYS   A H    
2052 H HA   . LYS   B 16  ? 0.72471  0.424765 0.615976 0.0521666   -0.0260249  -0.16752    28  LYS   A HA   
2053 H HB2  . LYS   B 16  ? 0.723138 0.466754 0.595167 0.018732    -0.0477995  -0.12171    28  LYS   A HB2  
2054 H HB3  . LYS   B 16  ? 0.782123 0.479288 0.65011  0.00940959  -0.048436   -0.146857   28  LYS   A HB3  
2055 H HG2  . LYS   B 16  ? 0.867474 0.514496 0.785336 0.0408656   -0.0536726  -0.119007   28  LYS   A HG2  
2056 H HG3  . LYS   B 16  ? 0.811168 0.505978 0.722782 0.0362755   -0.0576712  -0.0940671  28  LYS   A HG3  
2057 H HD2  . LYS   B 16  ? 0.966099 0.634572 0.838955 -0.0129119  -0.0659015  -0.112544   28  LYS   A HD2  
2058 H HD3  . LYS   B 16  ? 1.01128  0.620268 0.906047 -0.00074398 -0.0703401  -0.106524   28  LYS   A HD3  
2059 H HE2  . LYS   B 16  ? 0.988994 0.67749  0.880757 0.00120782  -0.0763936  -0.0623762  28  LYS   A HE2  
2060 H HE3  . LYS   B 16  ? 1.02546  0.688576 0.899194 -0.0279713  -0.0808942  -0.06741    28  LYS   A HE3  
2061 H HZ1  . LYS   B 16  ? 1.08847  0.693588 1.00856  0.0168576   -0.0874308  -0.0536355  28  LYS   A HZ1  
2062 H HZ2  . LYS   B 16  ? 1.12064  0.69852  1.0192   -0.0128523  -0.0917808  -0.0532993  28  LYS   A HZ2  
2063 H HZ3  . LYS   B 16  ? 1.07346  0.692111 0.972826 -0.00643755 -0.0957794  -0.0317947  28  LYS   A HZ3  
2064 N N    . LYS   B 17  ? 0.630942 0.446504 0.470144 0.0422645   -0.0189607  -0.159209   29  LYS   A N    
2065 C CA   . LYS   B 17  ? 0.661909 0.516547 0.46843  0.0336581   -0.0184758  -0.170293   29  LYS   A CA   
2066 C C    . LYS   B 17  ? 0.660496 0.521278 0.457131 0.00873005  -0.0345796  -0.169603   29  LYS   A C    
2067 O O    . LYS   B 17  ? 0.676559 0.547621 0.451923 -0.00570376 -0.0392436  -0.19158    29  LYS   A O    
2068 C CB   . LYS   B 17  ? 0.70476  0.556403 0.490371 0.0378538   -0.00711438 -0.204004   29  LYS   A CB   
2069 C CG   . LYS   B 17  ? 0.719989 0.576081 0.514897 0.0618726   0.0132618   -0.207187   29  LYS   A CG   
2070 C CD   . LYS   B 17  ? 0.728886 0.631553 0.516407 0.0722335   0.021756    -0.183128   29  LYS   A CD   
2071 C CE   . LYS   B 17  ? 0.818056 0.735811 0.585798 0.0841275   0.0433546   -0.204891   29  LYS   A CE   
2072 N NZ   . LYS   B 17  ? 0.819224 0.766051 0.596093 0.0981518   0.0583161   -0.180726   29  LYS   A NZ   
2073 H H    . LYS   B 17  ? 0.612687 0.436788 0.46635  0.0528265   -0.0158033  -0.143863   29  LYS   A H    
2074 H HA   . LYS   B 17  ? 0.630429 0.513648 0.435544 0.0417894   -0.014446   -0.15552    29  LYS   A HA   
2075 H HB2  . LYS   B 17  ? 0.736021 0.555465 0.525127 0.0301922   -0.0103288  -0.220411   29  LYS   A HB2  
2076 H HB3  . LYS   B 17  ? 0.713651 0.593897 0.474775 0.0310284   -0.00949439 -0.210054   29  LYS   A HB3  
2077 H HG2  . LYS   B 17  ? 0.720921 0.552094 0.543695 0.0697007   0.0140648   -0.200972   29  LYS   A HG2  
2078 H HG3  . LYS   B 17  ? 0.763896 0.615871 0.543687 0.0627431   0.0210504   -0.232337   29  LYS   A HG3  
2079 H HD2  . LYS   B 17  ? 0.719572 0.644631 0.489312 0.0634952   0.013374    -0.175334   29  LYS   A HD2  
2080 H HD3  . LYS   B 17  ? 0.702617 0.601828 0.515498 0.0798539   0.0230586   -0.164602   29  LYS   A HD3  
2081 H HE2  . LYS   B 17  ? 0.832382 0.725045 0.613946 0.0898637   0.0500911   -0.222718   29  LYS   A HE2  
2082 H HE3  . LYS   B 17  ? 0.833601 0.767858 0.569086 0.0762964   0.0413031   -0.21738    29  LYS   A HE3  
2083 H HZ1  . LYS   B 17  ? 0.792672 0.726518 0.600681 0.105065    0.0602408   -0.172005   29  LYS   A HZ1  
2084 H HZ2  . LYS   B 17  ? 0.791375 0.75713  0.558676 0.094022    0.0519115   -0.162836   29  LYS   A HZ2  
2085 H HZ3  . LYS   B 17  ? 0.834938 0.794649 0.596689 0.103811    0.0726031   -0.192123   29  LYS   A HZ3  
2086 N N    . ASP   B 18  ? 0.598528 0.460319 0.410962 0.00304371  -0.0423561  -0.14484    30  ASP   A N    
2087 C CA   . ASP   B 18  ? 0.592278 0.464064 0.402697 -0.019972   -0.0542626  -0.140214   30  ASP   A CA   
2088 C C    . ASP   B 18  ? 0.529283 0.451942 0.339047 -0.0175421  -0.056637   -0.122775   30  ASP   A C    
2089 O O    . ASP   B 18  ? 0.508284 0.445486 0.323926 -0.0337178  -0.0640438  -0.115763   30  ASP   A O    
2090 C CB   . ASP   B 18  ? 0.575398 0.406577 0.402224 -0.0296337  -0.059388   -0.126766   30  ASP   A CB   
2091 C CG   . ASP   B 18  ? 0.591785 0.420711 0.435456 -0.0143799  -0.0576424  -0.101203   30  ASP   A CG   
2092 O OD1  . ASP   B 18  ? 0.494925 0.356432 0.341107 0.00042395  -0.0519687  -0.0923944  30  ASP   A OD1  
2093 O OD2  . ASP   B 18  ? 0.575729 0.370126 0.429512 -0.0171581  -0.0622852  -0.0905875  30  ASP   A OD2  
2094 H H    . ASP   B 18  ? 0.585885 0.444152 0.411997 0.0139323   -0.0391707  -0.130479   30  ASP   A H    
2095 H HA   . ASP   B 18  ? 0.611795 0.483042 0.410996 -0.0320707  -0.0574517  -0.158466   30  ASP   A HA   
2096 H HB2  . ASP   B 18  ? 0.590334 0.429236 0.415175 -0.0468075  -0.0650631  -0.124463   30  ASP   A HB2  
2097 H HB3  . ASP   B 18  ? 0.620872 0.417426 0.449563 -0.0305829  -0.058789   -0.137535   30  ASP   A HB3  
2098 N N    . ARG   B 19  ? 0.497523 0.445937 0.302211 0.00265585  -0.0488019  -0.115518   31  ARG   A N    
2099 C CA   . ARG   B 19  ? 0.495712 0.487076 0.302121 0.00924377  -0.0502854  -0.0973466  31  ARG   A CA   
2100 C C    . ARG   B 19  ? 0.459161 0.446006 0.288501 0.00817812  -0.0512379  -0.0773777  31  ARG   A C    
2101 O O    . ARG   B 19  ? 0.452966 0.470178 0.289477 0.0103773   -0.0531342  -0.0655814  31  ARG   A O    
2102 C CB   . ARG   B 19  ? 0.46278  0.495739 0.255635 -0.00190168 -0.0611653  -0.105928   31  ARG   A CB   
2103 C CG   . ARG   B 19  ? 0.519141 0.565562 0.282991 0.0035668   -0.0594236  -0.12226    31  ARG   A CG   
2104 C CD   . ARG   B 19  ? 0.530046 0.623891 0.273807 -0.00526331 -0.0729243  -0.133087   31  ARG   A CD   
2105 N NE   . ARG   B 19  ? 0.49603  0.631151 0.252764 0.00404286  -0.0791456  -0.108371   31  ARG   A NE   
2106 C CZ   . ARG   B 19  ? 0.520263 0.68266  0.269833 0.0234771   -0.0774815  -0.087571   31  ARG   A CZ   
2107 N NH1  . ARG   B 19  ? 0.537944 0.695977 0.262886 0.0373293   -0.0669641  -0.0836776  31  ARG   A NH1  
2108 N NH2  . ARG   B 19  ? 0.53039  0.725768 0.299928 0.030097    -0.0852047  -0.0683333  31  ARG   A NH2  
2109 H H    . ARG   B 19  ? 0.520306 0.458423 0.321514 0.012631    -0.041615   -0.12157    31  ARG   A H    
2110 H HA   . ARG   B 19  ? 0.478743 0.478254 0.280842 0.0235295   -0.0428949  -0.0917959  31  ARG   A HA   
2111 H HB2  . ARG   B 19  ? 0.486907 0.513157 0.283071 -0.0184957  -0.067379   -0.115296   31  ARG   A HB2  
2112 H HB3  . ARG   B 19  ? 0.457516 0.51608  0.257574 0.00395763  -0.0628332  -0.0918543  31  ARG   A HB3  
2113 H HG2  . ARG   B 19  ? 0.505753 0.556422 0.266268 0.0190485   -0.0511578  -0.111179   31  ARG   A HG2  
2114 H HG3  . ARG   B 19  ? 0.532929 0.551353 0.29227  -0.00130069 -0.056278   -0.138383   31  ARG   A HG3  
2115 H HD2  . ARG   B 19  ? 0.554627 0.655965 0.275403 0.00031054  -0.0701768  -0.141686   31  ARG   A HD2  
2116 H HD3  . ARG   B 19  ? 0.542722 0.632592 0.289091 -0.0227653  -0.0802576  -0.148186   31  ARG   A HD3  
2117 H HE   . ARG   B 19  ? 0.491086 0.632442 0.264389 -0.00452882 -0.0843441  -0.106737   31  ARG   A HE   
2118 H HH11 . ARG   B 19  ? 0.544665 0.676508 0.266146 0.0376033   -0.057456   -0.0918645  31  ARG   A HH11 
2119 H HH12 . ARG   B 19  ? 0.547544 0.729705 0.260001 0.0464566   -0.0690028  -0.0722064  31  ARG   A HH12 
2120 H HH21 . ARG   B 19  ? 0.511709 0.720194 0.295352 0.0201767   -0.0927233  -0.0731846  31  ARG   A HH21 
2121 H HH22 . ARG   B 19  ? 0.514539 0.718231 0.284804 0.0446391   -0.0820086  -0.0508091  31  ARG   A HH22 
2122 N N    . GLY   B 20  ? 0.438754 0.388487 0.279826 0.00664677  -0.0499194  -0.0736995  32  GLY   A N    
2123 C CA   . GLY   B 20  ? 0.413561 0.35945  0.269749 0.00283071  -0.0518259  -0.0576249  32  GLY   A CA   
2124 C C    . GLY   B 20  ? 0.373756 0.334907 0.243322 0.0192391   -0.045036   -0.0422074  32  GLY   A C    
2125 O O    . GLY   B 20  ? 0.394268 0.363493 0.273753 0.0159069   -0.0457725  -0.0329173  32  GLY   A O    
2126 H H    . GLY   B 20  ? 0.45999  0.38725  0.299502 0.00877841  -0.0480181  -0.0814023  32  GLY   A H    
2127 H HA2  . GLY   B 20  ? 0.410064 0.370061 0.264875 -0.00887225 -0.0557966  -0.0583229  32  GLY   A HA2  
2128 H HA3  . GLY   B 20  ? 0.420863 0.338916 0.280473 -0.00084446 -0.0538784  -0.0567578  32  GLY   A HA3  
2129 N N    . VAL   B 21  ? 0.380191 0.342437 0.250806 0.035454    -0.0367178  -0.0408807  33  VAL   A N    
2130 C CA   . VAL   B 21  ? 0.371383 0.345538 0.256203 0.048857    -0.0285729  -0.0261026  33  VAL   A CA   
2131 C C    . VAL   B 21  ? 0.376393 0.371336 0.247207 0.0603848   -0.0206504  -0.0252461  33  VAL   A C    
2132 O O    . VAL   B 21  ? 0.357905 0.345617 0.219278 0.0653258   -0.01424    -0.0345208  33  VAL   A O    
2133 C CB   . VAL   B 21  ? 0.362431 0.315364 0.268105 0.0547197   -0.0249042  -0.0206736  33  VAL   A CB   
2134 C CG1  . VAL   B 21  ? 0.368519 0.333755 0.291474 0.0641505   -0.015972   -0.00703072 33  VAL   A CG1  
2135 C CG2  . VAL   B 21  ? 0.439792 0.370922 0.35141  0.0429471   -0.0359387  -0.020428   33  VAL   A CG2  
2136 H H    . VAL   B 21  ? 0.398797 0.353689 0.261472 0.037377    -0.0349107  -0.0500457  33  VAL   A H    
2137 H HA   . VAL   B 21  ? 0.355111 0.340184 0.244894 0.0460055   -0.0307452  -0.0203904  33  VAL   A HA   
2138 H HB   . VAL   B 21  ? 0.392314 0.338124 0.296659 0.0601827   -0.0207773  -0.0265607  33  VAL   A HB   
2139 H HG11 . VAL   B 21  ? 0.352687 0.326439 0.276293 0.0610784   -0.018178   -0.00301981 33  VAL   A HG11 
2140 H HG12 . VAL   B 21  ? 0.367884 0.342521 0.286417 0.0719695   -0.00797061 -0.00471054 33  VAL   A HG12 
2141 H HG13 . VAL   B 21  ? 0.356637 0.31192  0.295252 0.0649831   -0.0158287  -0.00479833 33  VAL   A HG13 
2142 H HG21 . VAL   B 21  ? 0.410349 0.332986 0.33625  0.0476526   -0.0356675  -0.0163422  33  VAL   A HG21 
2143 H HG22 . VAL   B 21  ? 0.429552 0.347767 0.331991 0.0371589   -0.0404243  -0.0275949  33  VAL   A HG22 
2144 H HG23 . VAL   B 21  ? 0.404865 0.344169 0.315193 0.0362246   -0.038653   -0.0170176  33  VAL   A HG23 
2145 N N    . LEU   B 22  ? 0.368485 0.390567 0.23588  0.0641917   -0.0219914  -0.0152411  34  LEU   A N    
2146 C CA   . LEU   B 22  ? 0.366917 0.410607 0.219184 0.075932    -0.0162178  -0.00657902 34  LEU   A CA   
2147 C C    . LEU   B 22  ? 0.375453 0.419505 0.243657 0.0886358   -0.00504504 0.0152775   34  LEU   A C    
2148 O O    . LEU   B 22  ? 0.3694   0.410713 0.259502 0.089075    -0.00654407 0.0238331   34  LEU   A O    
2149 C CB   . LEU   B 22  ? 0.387482 0.461671 0.227869 0.0717338   -0.0289858  -0.00886512 34  LEU   A CB   
2150 C CG   . LEU   B 22  ? 0.418073 0.494637 0.241586 0.0556455   -0.0395182  -0.0323595  34  LEU   A CG   
2151 C CD1  . LEU   B 22  ? 0.432491 0.547637 0.256473 0.0527144   -0.051978   -0.0301496  34  LEU   A CD1  
2152 C CD2  . LEU   B 22  ? 0.480227 0.551376 0.275394 0.0559485   -0.0351648  -0.0484872  34  LEU   A CD2  
2153 H H    . LEU   B 22  ? 0.354086 0.381388 0.229315 0.059575    -0.0268237  -0.0130056  34  LEU   A H    
2154 H HA   . LEU   B 22  ? 0.392496 0.432231 0.231005 0.0768563   -0.012009   -0.0149975  34  LEU   A HA   
2155 H HB2  . LEU   B 22  ? 0.371297 0.449353 0.228351 0.0707538   -0.0319608  -0.00323011 34  LEU   A HB2  
2156 H HB3  . LEU   B 22  ? 0.399981 0.491618 0.228888 0.08062     -0.0275849  0.00033614  34  LEU   A HB3  
2157 H HG   . LEU   B 22  ? 0.414328 0.471385 0.248523 0.0464651   -0.0408871  -0.0384959  34  LEU   A HG   
2158 H HD11 . LEU   B 22  ? 0.408904 0.524833 0.252374 0.0509487   -0.0528583  -0.0249333  34  LEU   A HD11 
2159 H HD12 . LEU   B 22  ? 0.441044 0.562812 0.254737 0.041164    -0.0592978  -0.0451554  34  LEU   A HD12 
2160 H HD13 . LEU   B 22  ? 0.43561  0.569721 0.251849 0.0639364   -0.0519057  -0.0191501  34  LEU   A HD13 
2161 H HD21 . LEU   B 22  ? 0.47008  0.51715  0.271646 0.0580679   -0.027248   -0.0513862  34  LEU   A HD21 
2162 H HD22 . LEU   B 22  ? 0.482871 0.572292 0.264093 0.0649553   -0.032192   -0.0406195  34  LEU   A HD22 
2163 H HD23 . LEU   B 22  ? 0.484775 0.558976 0.270279 0.0447577   -0.0429632  -0.0641133  34  LEU   A HD23 
2164 N N    . LYS   B 23  ? 0.372413 0.42021  0.22863  0.0974856   0.00727617  0.0230122   35  LYS   A N    
2165 C CA   . LYS   B 23  ? 0.42256  0.466261 0.294576 0.106621    0.0213074   0.0447306   35  LYS   A CA   
2166 C C    . LYS   B 23  ? 0.456233 0.519041 0.30389  0.116844    0.029035    0.0645097   35  LYS   A C    
2167 O O    . LYS   B 23  ? 0.437173 0.514407 0.251753 0.11775     0.0325465   0.0583885   35  LYS   A O    
2168 C CB   . LYS   B 23  ? 0.455299 0.481471 0.346077 0.10507     0.0338568   0.038919    35  LYS   A CB   
2169 C CG   . LYS   B 23  ? 0.438688 0.461869 0.349321 0.110296    0.0515411   0.0589957   35  LYS   A CG   
2170 C CD   . LYS   B 23  ? 0.412946 0.428664 0.348386 0.108565    0.0640565   0.0521906   35  LYS   A CD   
2171 C CE   . LYS   B 23  ? 0.461303 0.47717  0.417951 0.109743    0.081317    0.0718699   35  LYS   A CE   
2172 N NZ   . LYS   B 23  ? 0.438158 0.458949 0.418172 0.108952    0.098121    0.0676579   35  LYS   A NZ   
2173 H H    . LYS   B 23  ? 0.40498  0.45805  0.241722 0.0967248   0.008109    0.013849    35  LYS   A H    
2174 H HA   . LYS   B 23  ? 0.403979 0.442817 0.29457  0.10657     0.018049    0.0512011   35  LYS   A HA   
2175 H HB2  . LYS   B 23  ? 0.423884 0.437816 0.33125  0.0995415   0.0273451   0.0310939   35  LYS   A HB2  
2176 H HB3  . LYS   B 23  ? 0.455405 0.484608 0.330884 0.105201    0.0370317   0.028127    35  LYS   A HB3  
2177 H HG2  . LYS   B 23  ? 0.458961 0.493573 0.350395 0.115383    0.0582093   0.0699997   35  LYS   A HG2  
2178 H HG3  . LYS   B 23  ? 0.42652  0.442967 0.354178 0.109664    0.0485312   0.0672095   35  LYS   A HG3  
2179 H HD2  . LYS   B 23  ? 0.409082 0.414361 0.36268  0.104081    0.0555545   0.0432269   35  LYS   A HD2  
2180 H HD3  . LYS   B 23  ? 0.441049 0.463082 0.361635 0.110649    0.0690293   0.0426563   35  LYS   A HD3  
2181 H HE2  . LYS   B 23  ? 0.463811 0.487267 0.400606 0.113845    0.08721     0.0854327   35  LYS   A HE2  
2182 H HE3  . LYS   B 23  ? 0.430665 0.43643  0.407508 0.106542    0.0763971   0.0763802   35  LYS   A HE3  
2183 H HZ1  . LYS   B 23  ? 0.458866 0.487995 0.422134 0.112214    0.102848    0.0592087   35  LYS   A HZ1  
2184 H HZ2  . LYS   B 23  ? 0.429135 0.443473 0.432966 0.105689    0.091913    0.0591041   35  LYS   A HZ2  
2185 H HZ3  . LYS   B 23  ? 0.455858 0.478918 0.444597 0.108301    0.110372    0.0817794   35  LYS   A HZ3  
2186 N N    . ILE   B 24  ? 0.452996 0.513256 0.316459 0.124667    0.0331994   0.0895845   36  ILE   A N    
2187 C CA   . ILE   B 24  ? 0.469538 0.539474 0.314665 0.134569    0.043348    0.116876    36  ILE   A CA   
2188 C C    . ILE   B 24  ? 0.495911 0.542506 0.372209 0.134853    0.0615309   0.134213    36  ILE   A C    
2189 O O    . ILE   B 24  ? 0.474912 0.502131 0.387556 0.13336     0.059898    0.135499    36  ILE   A O    
2190 C CB   . ILE   B 24  ? 0.496063 0.584254 0.331696 0.145533    0.0290958   0.135911    36  ILE   A CB   
2191 C CG1  . ILE   B 24  ? 0.528698 0.647069 0.337273 0.142506    0.00932955  0.117481    36  ILE   A CG1  
2192 C CG2  . ILE   B 24  ? 0.588227 0.678879 0.408222 0.157249    0.0393142   0.17299     36  ILE   A CG2  
2193 C CD1  . ILE   B 24  ? 0.593131 0.739944 0.394187 0.154684    -0.00712488 0.136378    36  ILE   A CD1  
2194 H H    . ILE   B 24  ? 0.432312 0.482731 0.318454 0.123502    0.0298161   0.0898362   36  ILE   A H    
2195 H HA   . ILE   B 24  ? 0.498272 0.578788 0.31771  0.133619    0.0482846   0.112163    36  ILE   A HA   
2196 H HB   . ILE   B 24  ? 0.489147 0.566716 0.35247  0.146668    0.025438    0.136446    36  ILE   A HB   
2197 H HG12 . ILE   B 24  ? 0.548791 0.675072 0.330202 0.138981    0.0129286   0.109566    36  ILE   A HG12 
2198 H HG13 . ILE   B 24  ? 0.506073 0.618692 0.329896 0.134893    0.00347759  0.0988899   36  ILE   A HG13 
2199 H HG21 . ILE   B 24  ? 0.581919 0.681519 0.403249 0.166298    0.0287252   0.186501    36  ILE   A HG21 
2200 H HG22 . ILE   B 24  ? 0.596017 0.700517 0.384086 0.156151    0.0434201   0.173517    36  ILE   A HG22 
2201 H HG23 . ILE   B 24  ? 0.570757 0.640487 0.411691 0.156372    0.0524123   0.182715    36  ILE   A HG23 
2202 H HD11 . ILE   B 24  ? 0.565562 0.703495 0.395615 0.160404    -0.0083656  0.144884    36  ILE   A HD11 
2203 H HD12 . ILE   B 24  ? 0.576253 0.743529 0.366561 0.149803    -0.0202467  0.120904    36  ILE   A HD12 
2204 H HD13 . ILE   B 24  ? 0.609319 0.76407  0.388254 0.161719    -0.00357645 0.155552    36  ILE   A HD13 
2205 N N    . VAL   B 25  ? 0.492698 0.543506 0.353104 0.135263    0.0801815   0.146384    37  VAL   A N    
2206 C CA   . VAL   B 25  ? 0.530072 0.562931 0.417553 0.133828    0.099419    0.168154    37  VAL   A CA   
2207 C C    . VAL   B 25  ? 0.553274 0.581108 0.433884 0.144449    0.098004    0.203309    37  VAL   A C    
2208 O O    . VAL   B 25  ? 0.584371 0.631292 0.423137 0.152029    0.0977709   0.222738    37  VAL   A O    
2209 C CB   . VAL   B 25  ? 0.559968 0.602415 0.437768 0.128762    0.123031    0.168002    37  VAL   A CB   
2210 C CG1  . VAL   B 25  ? 0.612275 0.638322 0.522767 0.123524    0.144206    0.191229    37  VAL   A CG1  
2211 C CG2  . VAL   B 25  ? 0.535884 0.582082 0.427508 0.12259     0.12282     0.133021    37  VAL   A CG2  
2212 H H    . VAL   B 25  ? 0.521657 0.587055 0.354508 0.135265    0.0819626   0.140159    37  VAL   A H    
2213 H HA   . VAL   B 25  ? 0.49933  0.517292 0.418817 0.129011    0.0975458   0.159136    37  VAL   A HA   
2214 H HB   . VAL   B 25  ? 0.594605 0.652896 0.435935 0.132829    0.125514    0.175883    37  VAL   A HB   
2215 H HG11 . VAL   B 25  ? 0.57638  0.586111 0.520174 0.12        0.138808    0.186054    37  VAL   A HG11 
2216 H HG12 . VAL   B 25  ? 0.628706 0.652523 0.524103 0.127936    0.148362    0.216337    37  VAL   A HG12 
2217 H HG13 . VAL   B 25  ? 0.604983 0.639457 0.519248 0.118679    0.159337    0.186054    37  VAL   A HG13 
2218 H HG21 . VAL   B 25  ? 0.55094  0.606468 0.438003 0.121328    0.138994    0.132217    37  VAL   A HG21 
2219 H HG22 . VAL   B 25  ? 0.529834 0.582545 0.401946 0.124212    0.109965    0.118012    37  VAL   A HG22 
2220 H HG23 . VAL   B 25  ? 0.510334 0.543325 0.435619 0.118334    0.119413    0.126924    37  VAL   A HG23 
2221 N N    . LYS   B 26  ? 0.496243 0.497349 0.417776 0.144891    0.0981482   0.211648    38  LYS   A N    
2222 C CA   . LYS   B 26  ? 0.591978 0.577381 0.520441 0.156201    0.099227    0.245344    38  LYS   A CA   
2223 C C    . LYS   B 26  ? 0.641234 0.60607  0.579527 0.151016    0.123828    0.274109    38  LYS   A C    
2224 O O    . LYS   B 26  ? 0.701029 0.662205 0.620013 0.160915    0.127437    0.309939    38  LYS   A O    
2225 C CB   . LYS   B 26  ? 0.563183 0.5281   0.532158 0.160163    0.0878871   0.235309    38  LYS   A CB   
2226 C CG   . LYS   B 26  ? 0.582974 0.572646 0.541812 0.16508     0.0651745   0.211971    38  LYS   A CG   
2227 C CD   . LYS   B 26  ? 0.63451  0.6595   0.551025 0.175956    0.0511661   0.222471    38  LYS   A CD   
2228 C CE   . LYS   B 26  ? 0.618046 0.641206 0.536918 0.194517    0.0465472   0.256654    38  LYS   A CE   
2229 N NZ   . LYS   B 26  ? 0.650437 0.712341 0.535603 0.207353    0.0273189   0.268611    38  LYS   A NZ   
2230 H H    . LYS   B 26  ? 0.494339 0.485373 0.441109 0.138025    0.0972919   0.194861    38  LYS   A H    
2231 H HA   . LYS   B 26  ? 0.600246 0.603374 0.499299 0.165391    0.0908129   0.256903    38  LYS   A HA   
2232 H HB2  . LYS   B 26  ? 0.555896 0.505776 0.550682 0.149962    0.0939415   0.221163    38  LYS   A HB2  
2233 H HB3  . LYS   B 26  ? 0.600252 0.550804 0.578319 0.169141    0.0900428   0.257804    38  LYS   A HB3  
2234 H HG2  . LYS   B 26  ? 0.551128 0.545033 0.5105   0.154781    0.063614    0.188638    38  LYS   A HG2  
2235 H HG3  . LYS   B 26  ? 0.570987 0.549864 0.55416  0.169935    0.0605186   0.209989    38  LYS   A HG3  
2236 H HD2  . LYS   B 26  ? 0.62614  0.661039 0.515628 0.171719    0.0573968   0.224991    38  LYS   A HD2  
2237 H HD3  . LYS   B 26  ? 0.591611 0.632413 0.506292 0.174237    0.0383996   0.202634    38  LYS   A HD3  
2238 H HE2  . LYS   B 26  ? 0.621042 0.630227 0.57165  0.199004    0.0440027   0.252843    38  LYS   A HE2  
2239 H HE3  . LYS   B 26  ? 0.658837 0.665708 0.575109 0.194827    0.0597469   0.278418    38  LYS   A HE3  
2240 H HZ1  . LYS   B 26  ? 0.623961 0.702622 0.513345 0.205778    0.0155018   0.248546    38  LYS   A HZ1  
2241 H HZ2  . LYS   B 26  ? 0.663939 0.738688 0.516525 0.203499    0.0300401   0.272656    38  LYS   A HZ2  
2242 H HZ3  . LYS   B 26  ? 0.671496 0.729032 0.564526 0.22047     0.0242368   0.291864    38  LYS   A HZ3  
2243 N N    . ARG   B 27  ? 0.601273 0.552721 0.57277  0.135642    0.138918    0.260738    39  ARG   A N    
2244 C CA   . ARG   B 27  ? 0.670277 0.606453 0.655685 0.126205    0.165013    0.286046    39  ARG   A CA   
2245 C C    . ARG   B 27  ? 0.661569 0.616678 0.65753  0.111459    0.179366    0.263416    39  ARG   A C    
2246 O O    . ARG   B 27  ? 0.62796  0.584172 0.653473 0.104609    0.170064    0.230997    39  ARG   A O    
2247 C CB   . ARG   B 27  ? 0.67204  0.56729  0.710452 0.119734    0.170353    0.29207     39  ARG   A CB   
2248 C CG   . ARG   B 27  ? 0.726607 0.602954 0.785327 0.106065    0.198251    0.318923    39  ARG   A CG   
2249 C CD   . ARG   B 27  ? 0.78736  0.619178 0.899048 0.0984801   0.201612    0.320681    39  ARG   A CD   
2250 N NE   . ARG   B 27  ? 0.809242 0.641124 0.963686 0.0827793   0.196381    0.280532    39  ARG   A NE   
2251 C CZ   . ARG   B 27  ? 0.770866 0.567774 0.967712 0.0765485   0.192538    0.268278    39  ARG   A CZ   
2252 N NH1  . ARG   B 27  ? 0.698647 0.500268 0.926459 0.0624753   0.184233    0.231493    39  ARG   A NH1  
2253 N NH2  . ARG   B 27  ? 0.759416 0.517748 0.963995 0.0867095   0.195039    0.292253    39  ARG   A NH2  
2254 H H    . ARG   B 27  ? 0.580737 0.533859 0.567925 0.130085    0.132618    0.235866    39  ARG   A H    
2255 H HA   . ARG   B 27  ? 0.702368 0.643715 0.658499 0.132253    0.170765    0.311979    39  ARG   A HA   
2256 H HB2  . ARG   B 27  ? 0.688209 0.569749 0.725832 0.131029    0.161116    0.303514    39  ARG   A HB2  
2257 H HB3  . ARG   B 27  ? 0.64151  0.535557 0.70421  0.112734    0.164079    0.265412    39  ARG   A HB3  
2258 H HG2  . ARG   B 27  ? 0.721454 0.614537 0.786884 0.0949539   0.208146    0.306175    39  ARG   A HG2  
2259 H HG3  . ARG   B 27  ? 0.773089 0.650209 0.804103 0.11239     0.205176    0.34798     39  ARG   A HG3  
2260 H HD2  . ARG   B 27  ? 0.824677 0.640757 0.945196 0.0911019   0.219257    0.34469     39  ARG   A HD2  
2261 H HD3  . ARG   B 27  ? 0.794587 0.611545 0.9038   0.111469    0.189975    0.326448    39  ARG   A HD3  
2262 H HE   . ARG   B 27  ? 0.758876 0.614065 0.910517 0.0776359   0.195318    0.264017    39  ARG   A HE   
2263 H HH11 . ARG   B 27  ? 0.680526 0.507546 0.900032 0.0606491   0.177484    0.215002    39  ARG   A HH11 
2264 H HH12 . ARG   B 27  ? 0.716037 0.49503  0.972079 0.0550011   0.184985    0.22368     39  ARG   A HH12 
2265 H HH21 . ARG   B 27  ? 0.810539 0.550344 1.02244  0.0825856   0.209256    0.316179    39  ARG   A HH21 
2266 H HH22 . ARG   B 27  ? 0.767828 0.518702 0.971603 0.0979114   0.182977    0.284782    39  ARG   A HH22 
2267 N N    . VAL   B 28  ? 0.667152 0.641102 0.636541 0.108135    0.200809    0.279561    40  VAL   A N    
2268 C CA   . VAL   B 28  ? 0.696196 0.693659 0.678833 0.0975416   0.216323    0.256817    40  VAL   A CA   
2269 C C    . VAL   B 28  ? 0.675164 0.655857 0.722109 0.0814335   0.227839    0.253308    40  VAL   A C    
2270 O O    . VAL   B 28  ? 0.733434 0.68496  0.802371 0.0755868   0.23539     0.277809    40  VAL   A O    
2271 C CB   . VAL   B 28  ? 0.732936 0.75909  0.675826 0.0961238   0.242038    0.270314    40  VAL   A CB   
2272 C CG1  . VAL   B 28  ? 0.763713 0.815825 0.732569 0.0877461   0.259186    0.242237    40  VAL   A CG1  
2273 C CG2  . VAL   B 28  ? 0.719442 0.766493 0.594593 0.109498    0.229748    0.270016    40  VAL   A CG2  
2274 H H    . VAL   B 28  ? 0.719566 0.693084 0.662855 0.113022    0.206182    0.30497     40  VAL   A H    
2275 H HA   . VAL   B 28  ? 0.653939 0.661175 0.633959 0.100911    0.202199    0.231103    40  VAL   A HA   
2276 H HB   . VAL   B 28  ? 0.769636 0.78534  0.714002 0.091394    0.257148    0.298668    40  VAL   A HB   
2277 H HG11 . VAL   B 28  ? 0.711878 0.765826 0.693068 0.0909294   0.243335    0.21601     40  VAL   A HG11 
2278 H HG12 . VAL   B 28  ? 0.748795 0.795576 0.755321 0.077288    0.272888    0.249009    40  VAL   A HG12 
2279 H HG13 . VAL   B 28  ? 0.773036 0.846137 0.709429 0.0897259   0.27244     0.243617    40  VAL   A HG13 
2280 H HG21 . VAL   B 28  ? 0.764446 0.828256 0.611383 0.107691    0.247313    0.280683    40  VAL   A HG21 
2281 H HG22 . VAL   B 28  ? 0.739399 0.774258 0.601681 0.11655     0.216506    0.287085    40  VAL   A HG22 
2282 H HG23 . VAL   B 28  ? 0.700562 0.757274 0.574143 0.112313    0.217526    0.24168     40  VAL   A HG23 
2283 N N    . GLY   B 29  ? 0.631678 0.63195  0.709028 0.0744236   0.229143    0.223188    41  GLY   A N    
2284 C CA   . GLY   B 29  ? 0.614973 0.612004 0.754622 0.0576622   0.238908    0.216114    41  GLY   A CA   
2285 C C    . GLY   B 29  ? 0.645592 0.670631 0.80355  0.0469078   0.270898    0.222969    41  GLY   A C    
2286 O O    . GLY   B 29  ? 0.739204 0.774921 0.85997  0.0487776   0.292716    0.246085    41  GLY   A O    
2287 H H    . GLY   B 29  ? 0.619476 0.636026 0.679655 0.080564    0.222218    0.205938    41  GLY   A H    
2288 H HA2  . GLY   B 29  ? 0.629207 0.601211 0.784782 0.0523198   0.238813    0.229458    41  GLY   A HA2  
2289 H HA3  . GLY   B 29  ? 0.584071 0.585609 0.742402 0.0576773   0.223666    0.191987    41  GLY   A HA3  
2290 N N    . ASN   B 30  ? 0.626142 0.664812 0.844731 0.0340872   0.273645    0.203968    42  ASN   A N    
2291 C CA   . ASN   B 30  ? 0.653968 0.71745  0.912359 0.0181809   0.305334    0.212153    42  ASN   A CA   
2292 C C    . ASN   B 30  ? 0.643636 0.75051  0.929548 0.0226299   0.307252    0.181926    42  ASN   A C    
2293 O O    . ASN   B 30  ? 0.670882 0.780063 0.980273 0.0275632   0.280954    0.155557    42  ASN   A O    
2294 C CB   . ASN   B 30  ? 0.671956 0.719965 0.995539 -0.00438447 0.308196    0.215319    42  ASN   A CB   
2295 C CG   . ASN   B 30  ? 0.714528 0.711523 1.02442  -0.00832637 0.304398    0.240784    42  ASN   A CG   
2296 O OD1  . ASN   B 30  ? 0.776639 0.745636 1.09915  -0.00781851 0.279374    0.227105    42  ASN   A OD1  
2297 N ND2  . ASN   B 30  ? 0.751258 0.735431 1.0294   -0.00922787 0.327866    0.27784     42  ASN   A ND2  
2298 H H    . ASN   B 30  ? 0.596206 0.631051 0.83277  0.0348405   0.254604    0.185267    42  ASN   A H    
2299 H HA   . ASN   B 30  ? 0.695113 0.760307 0.925372 0.0178587   0.325101    0.234174    42  ASN   A HA   
2300 H HB2  . ASN   B 30  ? 0.638769 0.69188  0.990582 -0.00531954 0.289662    0.192371    42  ASN   A HB2  
2301 H HB3  . ASN   B 30  ? 0.688972 0.756222 1.0382   -0.0160834  0.33133     0.222606    42  ASN   A HB3  
2302 H HD21 . ASN   B 30  ? 0.776796 0.729612 1.04567  -0.00864857 0.32532     0.295179    42  ASN   A HD21 
2303 H HD22 . ASN   B 30  ? 0.773004 0.779904 1.03846  -0.0100463  0.346385    0.286037    42  ASN   A HD22 
2304 N N    . GLY   B 31  ? 0.660804 0.802313 0.948673 0.0200182   0.340033    0.187231    43  GLY   A N    
2305 C CA   . GLY   B 31  ? 0.668247 0.854157 0.99721  0.0243903   0.347475    0.159356    43  GLY   A CA   
2306 C C    . GLY   B 31  ? 0.66806  0.85981  0.955765 0.0481585   0.331261    0.134288    43  GLY   A C    
2307 O O    . GLY   B 31  ? 0.733093 0.900758 0.95661  0.0581908   0.318838    0.140225    43  GLY   A O    
2308 H H    . GLY   B 31  ? 0.703438 0.841624 0.966693 0.0159917   0.35898     0.209275    43  GLY   A H    
2309 H HA2  . GLY   B 31  ? 0.691057 0.900779 1.02886  0.0178506   0.37636     0.167647    43  GLY   A HA2  
2310 H HA3  . GLY   B 31  ? 0.640143 0.829797 1.01842  0.0177826   0.335012    0.148046    43  GLY   A HA3  
2311 N N    . GLU   B 32  ? 0.655611 0.880211 0.985991 0.0565298   0.33174     0.106529    44  GLU   A N    
2312 C CA   . GLU   B 32  ? 0.651302 0.878696 0.955393 0.078325    0.318001    0.0795974   44  GLU   A CA   
2313 C C    . GLU   B 32  ? 0.551649 0.759751 0.881349 0.0845      0.276185    0.0623715   44  GLU   A C    
2314 O O    . GLU   B 32  ? 0.56871  0.756648 0.859444 0.0977818   0.255579    0.0495772   44  GLU   A O    
2315 C CB   . GLU   B 32  ? 0.627405 0.900971 0.952676 0.0844333   0.35419     0.0659133   44  GLU   A CB   
2316 H H    . GLU   B 32  ? 0.649689 0.895287 1.03053  0.0483032   0.340828    0.104376    44  GLU   A H    
2317 H HA   . GLU   B 32  ? 0.645212 0.855619 0.893241 0.0829725   0.31598     0.0855365   44  GLU   A HA   
2320 N N    . GLU   B 33  ? 0.490513 0.70283  0.880076 0.0725052   0.262266    0.0632349   45  GLU   A N    
2321 C CA   . GLU   B 33  ? 0.468704 0.675602 0.887953 0.0787991   0.226094    0.0456042   45  GLU   A CA   
2322 C C    . GLU   B 33  ? 0.431542 0.594896 0.803199 0.0788156   0.195162    0.0484174   45  GLU   A C    
2323 O O    . GLU   B 33  ? 0.421891 0.561508 0.772002 0.0667489   0.194761    0.0648093   45  GLU   A O    
2324 C CB   . GLU   B 33  ? 0.451208 0.680222 0.94532  0.0641716   0.216433    0.0437843   45  GLU   A CB   
2325 H H    . GLU   B 33  ? 0.510964 0.72972  0.922105 0.058959    0.275435    0.0756678   45  GLU   A H    
2326 H HA   . GLU   B 33  ? 0.46282  0.681374 0.886111 0.0931655   0.225498    0.0310785   45  GLU   A HA   
2329 N N    . THR   B 34  ? 0.476841 0.628249 0.831896 0.0931407   0.170528    0.0325879   46  THR   A N    
2330 C CA   . THR   B 34  ? 0.430424 0.546865 0.749812 0.0916514   0.139775    0.0324443   46  THR   A CA   
2331 C C    . THR   B 34  ? 0.399641 0.520587 0.758607 0.091621    0.1105      0.0217026   46  THR   A C    
2332 O O    . THR   B 34  ? 0.419069 0.566575 0.823598 0.0991209   0.111369    0.0131378   46  THR   A O    
2333 C CB   . THR   B 34  ? 0.445041 0.542652 0.706515 0.10493     0.136019    0.0254958   46  THR   A CB   
2334 O OG1  . THR   B 34  ? 0.40637  0.518103 0.69333  0.119389    0.135004    0.00799187  46  THR   A OG1  
2335 C CG2  . THR   B 34  ? 0.47175  0.570338 0.690356 0.104491    0.161853    0.0374812   46  THR   A CG2  
2336 H H    . THR   B 34  ? 0.457985 0.623242 0.825399 0.104016    0.174122    0.0214754   46  THR   A H    
2337 H HA   . THR   B 34  ? 0.435108 0.539339 0.744225 0.0813946   0.14095     0.0435621   46  THR   A HA   
2338 H HB   . THR   B 34  ? 0.425309 0.50257  0.666167 0.102989    0.116498    0.0251846   46  THR   A HB   
2340 H HG21 . THR   B 34  ? 0.476949 0.563412 0.656731 0.110348    0.155808    0.0329005   46  THR   A HG21 
2341 H HG22 . THR   B 34  ? 0.485564 0.604797 0.718056 0.107331    0.182225    0.0356065   46  THR   A HG22 
2342 H HG23 . THR   B 34  ? 0.47146  0.562883 0.687557 0.0952661   0.164044    0.0517551   46  THR   A HG23 
2343 N N    . PRO   B 35  ? 0.404881 0.503774 0.74958  0.0836142   0.0834312   0.0220816   47  PRO   A N    
2344 C CA   . PRO   B 35  ? 0.368406 0.477792 0.750478 0.0809364   0.0558943   0.0147593   47  PRO   A CA   
2345 C C    . PRO   B 35  ? 0.33141  0.438566 0.712396 0.0988553   0.0381174   0.00630154  47  PRO   A C    
2346 O O    . PRO   B 35  ? 0.324379 0.406667 0.65988  0.107644    0.0372985   0.00417315  47  PRO   A O    
2347 C CB   . PRO   B 35  ? 0.352435 0.436106 0.705644 0.0664127   0.0361644   0.0168366   47  PRO   A CB   
2348 C CG   . PRO   B 35  ? 0.385725 0.442908 0.685813 0.0671786   0.0498488   0.0242034   47  PRO   A CG   
2349 C CD   . PRO   B 35  ? 0.4022   0.469726 0.696246 0.0769158   0.0784877   0.0294848   47  PRO   A CD   
2350 H HA   . PRO   B 35  ? 0.362903 0.49639  0.788494 0.0753766   0.0619644   0.0145603   47  PRO   A HA   
2351 H HB2  . PRO   B 35  ? 0.35785  0.434933 0.70184  0.0689125   0.0150003   0.0126812   47  PRO   A HB2  
2352 H HB3  . PRO   B 35  ? 0.359849 0.452275 0.739385 0.0540495   0.0361503   0.0171625   47  PRO   A HB3  
2353 H HG2  . PRO   B 35  ? 0.377477 0.419413 0.646846 0.0714192   0.0371724   0.0213632   47  PRO   A HG2  
2354 H HG3  . PRO   B 35  ? 0.380549 0.429829 0.680488 0.0567054   0.0524407   0.0282412   47  PRO   A HG3  
2355 H HD2  . PRO   B 35  ? 0.405439 0.46174  0.664595 0.085197    0.0779261   0.0278639   47  PRO   A HD2  
2356 H HD3  . PRO   B 35  ? 0.408731 0.475356 0.702854 0.070259    0.0938048   0.0387883   47  PRO   A HD3  
2357 N N    . MET   B 36  ? 0.316768 0.446784 0.74691  0.101357    0.0192956   0.00276848  48  MET   A N    
2358 C CA   . MET   B 36  ? 0.340527 0.469946 0.784437 0.119402    -0.00175704 -0.0015118  48  MET   A CA   
2359 C C    . MET   B 36  ? 0.324836 0.432048 0.740486 0.111354    -0.0374344  0.00341541  48  MET   A C    
2360 O O    . MET   B 36  ? 0.303839 0.411628 0.711302 0.0923218   -0.0467638  0.0055315   48  MET   A O    
2361 C CB   . MET   B 36  ? 0.373986 0.548403 0.894325 0.128427    -0.00320264 -0.0053132  48  MET   A CB   
2362 C CG   . MET   B 36  ? 0.449204 0.653139 1.00767  0.141656    0.032162    -0.0130055  48  MET   A CG   
2363 S SD   . MET   B 36  ? 0.402328 0.57852  0.919244 0.164531    0.0540118   -0.0238033  48  MET   A SD   
2364 C CE   . MET   B 36  ? 0.480843 0.707198 1.04639  0.167006    0.0990048   -0.0308399  48  MET   A CE   
2365 H H    . MET   B 36  ? 0.319507 0.467248 0.779203 0.0908909   0.0186385   0.00380306  48  MET   A H    
2366 H HA   . MET   B 36  ? 0.348228 0.462141 0.769173 0.130595    0.00775179  -0.0049625  48  MET   A HA   
2367 H HB2  . MET   B 36  ? 0.371824 0.563864 0.914472 0.114365    -0.00921847 -0.00325397 48  MET   A HB2  
2368 H HB3  . MET   B 36  ? 0.386112 0.557082 0.915097 0.139202    -0.0242211  -0.00502504 48  MET   A HB3  
2369 H HG2  . MET   B 36  ? 0.414083 0.628131 0.97368  0.128992    0.0513302   -0.0103883  48  MET   A HG2  
2370 H HG3  . MET   B 36  ? 0.419177 0.652566 1.02974  0.149165    0.0259189   -0.015868   48  MET   A HG3  
2371 H HE1  . MET   B 36  ? 0.477144 0.700957 1.03593  0.181429    0.113878    -0.0410648  48  MET   A HE1  
2372 H HE2  . MET   B 36  ? 0.458259 0.683713 1.00218  0.152334    0.11387     -0.0240102  48  MET   A HE2  
2373 H HE3  . MET   B 36  ? 0.456079 0.714092 1.07682  0.168016    0.0943032   -0.0312949  48  MET   A HE3  
2374 N N    . ILE   B 37  ? 0.320448 0.407194 0.721712 0.12523     -0.0571045  0.00499134  49  ILE   A N    
2375 C CA   . ILE   B 37  ? 0.319808 0.389925 0.695869 0.117242    -0.0908973  0.0128424   49  ILE   A CA   
2376 C C    . ILE   B 37  ? 0.3015   0.408918 0.724432 0.10956     -0.112775   0.0149832   49  ILE   A C    
2377 O O    . ILE   B 37  ? 0.300564 0.441328 0.782748 0.121326    -0.112159   0.0129864   49  ILE   A O    
2378 C CB   . ILE   B 37  ? 0.34406  0.385121 0.70487  0.13406     -0.107442   0.0179875   49  ILE   A CB   
2379 C CG1  . ILE   B 37  ? 0.420663 0.423198 0.72648  0.133293    -0.0919526  0.0141535   49  ILE   A CG1  
2380 C CG2  . ILE   B 37  ? 0.363832 0.39924  0.711729 0.126739    -0.144665   0.0308187   49  ILE   A CG2  
2381 C CD1  . ILE   B 37  ? 0.451504 0.42346  0.752216 0.151167    -0.0964146  0.0133599   49  ILE   A CD1  
2382 H H    . ILE   B 37  ? 0.331853 0.413866 0.738072 0.139328    -0.0485215  0.00125497  49  ILE   A H    
2383 H HA   . ILE   B 37  ? 0.313263 0.36732  0.651397 0.10451     -0.0888194  0.013354    49  ILE   A HA   
2384 H HB   . ILE   B 37  ? 0.363811 0.41725  0.762158 0.149994    -0.103713   0.0152418   49  ILE   A HB   
2385 H HG12 . ILE   B 37  ? 0.399702 0.38888  0.670296 0.119671    -0.100018   0.0182426   49  ILE   A HG12 
2386 H HG13 . ILE   B 37  ? 0.391201 0.401866 0.697502 0.132869    -0.0695189  0.00730111  49  ILE   A HG13 
2387 H HG21 . ILE   B 37  ? 0.381623 0.389934 0.707905 0.133259    -0.153314   0.036647    49  ILE   A HG21 
2388 H HG22 . ILE   B 37  ? 0.355132 0.388802 0.675845 0.109745    -0.147126   0.030804    49  ILE   A HG22 
2389 H HG23 . ILE   B 37  ? 0.365985 0.427167 0.754119 0.132149    -0.157468   0.0332986   49  ILE   A HG23 
2390 H HD11 . ILE   B 37  ? 0.455053 0.441105 0.794522 0.166399    -0.0897814  0.00833511  49  ILE   A HD11 
2391 H HD12 . ILE   B 37  ? 0.452202 0.404568 0.72086  0.14865     -0.0837903  0.00765204  49  ILE   A HD12 
2392 H HD13 . ILE   B 37  ? 0.464215 0.421735 0.755844 0.149901    -0.118353   0.0232478   49  ILE   A HD13 
2393 N N    . GLY   B 38  ? 0.318159 0.422836 0.714775 0.0886961   -0.130383   0.0164241   50  GLY   A N    
2394 C CA   . GLY   B 38  ? 0.302697 0.443718 0.736561 0.0756946   -0.151552   0.0142332   50  GLY   A CA   
2395 C C    . GLY   B 38  ? 0.299019 0.455783 0.750689 0.0549257   -0.131687   0.00353619  50  GLY   A C    
2396 O O    . GLY   B 38  ? 0.322177 0.505876 0.800063 0.0385139   -0.148594   -0.00254584 50  GLY   A O    
2397 H H    . GLY   B 38  ? 0.31052  0.390929 0.663936 0.0816571   -0.129023   0.0172071   50  GLY   A H    
2398 H HA2  . GLY   B 38  ? 0.321416 0.453568 0.726685 0.0683083   -0.17323    0.0179553   50  GLY   A HA2  
2399 H HA3  . GLY   B 38  ? 0.313038 0.478341 0.790751 0.0874645   -0.159176   0.0160937   50  GLY   A HA3  
2400 N N    . ASP   B 39  ? 0.292815 0.441785 0.746744 0.0572447   -0.0962096  0.001555    51  ASP   A N    
2401 C CA   . ASP   B 39  ? 0.303104 0.462118 0.77812  0.0383718   -0.0753823  -0.0042825  51  ASP   A CA   
2402 C C    . ASP   B 39  ? 0.282326 0.414493 0.712239 0.0187806   -0.0829281  -0.00943433 51  ASP   A C    
2403 O O    . ASP   B 39  ? 0.31127  0.412602 0.684571 0.0214166   -0.0893726  -0.00715765 51  ASP   A O    
2404 C CB   . ASP   B 39  ? 0.269037 0.421158 0.745099 0.0438876   -0.0360573  -0.00048706 51  ASP   A CB   
2405 C CG   . ASP   B 39  ? 0.266509 0.452892 0.795738 0.0581341   -0.018283   4.44e-06    51  ASP   A CG   
2406 O OD1  . ASP   B 39  ? 0.263453 0.485059 0.844268 0.0636626   -0.0355926  -0.00329624 51  ASP   A OD1  
2407 O OD2  . ASP   B 39  ? 0.249613 0.431092 0.769873 0.0640513   0.0142491   0.00359181  51  ASP   A OD2  
2408 H H    . ASP   B 39  ? 0.29376  0.429896 0.734997 0.0702154   -0.0847949  0.00437008  51  ASP   A H    
2409 H HA   . ASP   B 39  ? 0.291027 0.480603 0.8115   0.0329224   -0.0823141  -0.00785562 51  ASP   A HA   
2410 H HB2  . ASP   B 39  ? 0.274301 0.401002 0.708596 0.0515384   -0.0311321  0.00274323  51  ASP   A HB2  
2411 H HB3  . ASP   B 39  ? 0.275051 0.424369 0.755463 0.0296914   -0.0248214  -0.00154239 51  ASP   A HB3  
2412 N N    . LYS   B 40  ? 0.325916 0.471299 0.786214 -0.00180135 -0.0793322  -0.0182428  52  LYS   A N    
2413 C CA   . LYS   B 40  ? 0.34088  0.461921 0.768793 -0.0207268  -0.0820245  -0.0280152  52  LYS   A CA   
2414 C C    . LYS   B 40  ? 0.329118 0.420593 0.741712 -0.0202013  -0.0483145  -0.0226288  52  LYS   A C    
2415 O O    . LYS   B 40  ? 0.342808 0.443209 0.792039 -0.0219578  -0.0244918  -0.0170454  52  LYS   A O    
2416 C CB   . LYS   B 40  ? 0.420169 0.568546 0.892743 -0.0439871  -0.0956582  -0.0428877  52  LYS   A CB   
2417 C CG   . LYS   B 40  ? 0.505889 0.633573 0.941885 -0.0634919  -0.107844   -0.0595083  52  LYS   A CG   
2418 C CD   . LYS   B 40  ? 0.562429 0.725882 1.02168  -0.0813573  -0.141363   -0.074747   52  LYS   A CD   
2419 C CE   . LYS   B 40  ? 0.608269 0.756813 1.054    -0.107063   -0.143065   -0.0985278  52  LYS   A CE   
2420 N NZ   . LYS   B 40  ? 0.655193 0.787645 1.13991  -0.118185   -0.111698   -0.103069   52  LYS   A NZ   
2421 H H    . LYS   B 40  ? 0.315956 0.486107 0.820462 -0.00453051 -0.0740345  -0.0194597  52  LYS   A H    
2422 H HA   . LYS   B 40  ? 0.352872 0.460799 0.741979 -0.0182444  -0.0967289  -0.0283109  52  LYS   A HA   
2423 H HB2  . LYS   B 40  ? 0.41864  0.594823 0.913093 -0.0408738  -0.115172   -0.0426402  52  LYS   A HB2  
2424 H HB3  . LYS   B 40  ? 0.415172 0.56917  0.92145  -0.0502546  -0.0769392  -0.0429546  52  LYS   A HB3  
2425 H HG2  . LYS   B 40  ? 0.502952 0.613677 0.945034 -0.0723375  -0.0892445  -0.0641989  52  LYS   A HG2  
2426 H HG3  . LYS   B 40  ? 0.495021 0.603939 0.88605  -0.0559075  -0.112391   -0.0561876  52  LYS   A HG3  
2427 H HD2  . LYS   B 40  ? 0.561654 0.731658 0.99658  -0.0737457  -0.162313   -0.0698449  52  LYS   A HD2  
2428 H HD3  . LYS   B 40  ? 0.553707 0.745461 1.06236  -0.0834119  -0.141583   -0.0739807  52  LYS   A HD3  
2429 H HE2  . LYS   B 40  ? 0.618112 0.741992 1.01726  -0.104655   -0.142003   -0.100559   52  LYS   A HE2  
2430 H HE3  . LYS   B 40  ? 0.628328 0.80223  1.08666  -0.11953    -0.165513   -0.109511   52  LYS   A HE3  
2431 H HZ1  . LYS   B 40  ? 0.636029 0.737972 1.09544  -0.112365   -0.0948053  -0.0992768  52  LYS   A HZ1  
2432 H HZ2  . LYS   B 40  ? 0.626861 0.77538  1.14702  -0.113324   -0.10301    -0.0933374  52  LYS   A HZ2  
2433 H HZ3  . LYS   B 40  ? 0.657607 0.794242 1.15709  -0.136715   -0.117472   -0.119717   52  LYS   A HZ3  
2434 N N    . VAL   B 41  ? 0.346223 0.404767 0.704826 -0.017162   -0.0461484  -0.0222079  53  VAL   A N    
2435 C CA   . VAL   B 41  ? 0.35962  0.393634 0.701342 -0.0101087  -0.0176118  -0.0120658  53  VAL   A CA   
2436 C C    . VAL   B 41  ? 0.393198 0.400698 0.72165  -0.0238045  -0.0130031  -0.0216594  53  VAL   A C    
2437 O O    . VAL   B 41  ? 0.348332 0.349903 0.651432 -0.0312959  -0.0311411  -0.0355037  53  VAL   A O    
2438 C CB   . VAL   B 41  ? 0.379348 0.400549 0.675399 0.00938613  -0.0153999  -0.00226143 53  VAL   A CB   
2439 C CG1  . VAL   B 41  ? 0.405721 0.405736 0.680963 0.0157141   0.00944299  0.00828515  53  VAL   A CG1  
2440 C CG2  . VAL   B 41  ? 0.40246  0.444235 0.714522 0.0243663   -0.0164618  0.00369751  53  VAL   A CG2  
2441 H H    . VAL   B 41  ? 0.349525 0.402887 0.682505 -0.0194753  -0.0621182  -0.0273752  53  VAL   A H    
2442 H HA   . VAL   B 41  ? 0.36482  0.408486 0.735775 -0.0101507  -0.00250302 -0.00619707 53  VAL   A HA   
2443 H HB   . VAL   B 41  ? 0.384099 0.39748  0.65329  0.00783744  -0.0301124  -0.00738401 53  VAL   A HB   
2444 H HG11 . VAL   B 41  ? 0.402588 0.405388 0.703264 0.0113826   0.0238724   0.0128401   53  VAL   A HG11 
2445 H HG12 . VAL   B 41  ? 0.401237 0.385457 0.6563   0.012235    0.00679779  0.00437955  53  VAL   A HG12 
2446 H HG13 . VAL   B 41  ? 0.393649 0.393863 0.650796 0.0274492   0.0134712   0.0145307   53  VAL   A HG13 
2447 H HG21 . VAL   B 41  ? 0.390762 0.421554 0.673029 0.0345026   -0.0160035  0.00714522  53  VAL   A HG21 
2448 H HG22 . VAL   B 41  ? 0.39353  0.44947  0.721512 0.0223282   -0.0339863  -0.00078797 53  VAL   A HG22 
2449 H HG23 . VAL   B 41  ? 0.393667 0.44575  0.73071  0.0257197   0.00023065  0.00807385  53  VAL   A HG23 
2450 N N    . TYR   B 42  ? 0.371086 0.362666 0.717054 -0.0264752  0.0122577   -0.0136773  54  TYR   A N    
2451 C CA   . TYR   B 42  ? 0.412886 0.372715 0.751949 -0.0349426  0.02085     -0.0207621  54  TYR   A CA   
2452 C C    . TYR   B 42  ? 0.387863 0.323958 0.696509 -0.0176691  0.0388075   -0.00305319 54  TYR   A C    
2453 O O    . TYR   B 42  ? 0.362736 0.299933 0.680197 -0.0101512  0.0578129   0.017203    54  TYR   A O    
2454 C CB   . TYR   B 42  ? 0.471179 0.426943 0.862056 -0.0531675  0.0353561   -0.0224953  54  TYR   A CB   
2455 C CG   . TYR   B 42  ? 0.463324 0.447577 0.892734 -0.0736003  0.0169938   -0.0418669  54  TYR   A CG   
2456 C CD1  . TYR   B 42  ? 0.484123 0.508894 0.944184 -0.0720539  0.0102995   -0.0364838  54  TYR   A CD1  
2457 C CD2  . TYR   B 42  ? 0.475903 0.449145 0.912288 -0.0936801  0.00596844  -0.0671764  54  TYR   A CD2  
2458 C CE1  . TYR   B 42  ? 0.512592 0.570224 1.01252  -0.0896572  -0.00973579 -0.0530409  54  TYR   A CE1  
2459 C CE2  . TYR   B 42  ? 0.550263 0.554496 1.02071  -0.114014   -0.0139194  -0.0859305  54  TYR   A CE2  
2460 C CZ   . TYR   B 42  ? 0.552122 0.600562 1.05421  -0.111252   -0.0237203  -0.0773532  54  TYR   A CZ   
2461 O OH   . TYR   B 42  ? 0.627949 0.712776 1.16889  -0.130626   -0.0457205  -0.0947483  54  TYR   A OH   
2462 H H    . TYR   B 42  ? 0.381506 0.381303 0.744533 -0.0224523  0.0251509   -0.0030334  54  TYR   A H    
2463 H HA   . TYR   B 42  ? 0.412845 0.36997  0.736398 -0.0406061  0.00653943  -0.0356184  54  TYR   A HA   
2464 H HB2  . TYR   B 42  ? 0.457481 0.417667 0.861102 -0.0481509  0.0508095   -0.00631843 54  TYR   A HB2  
2465 H HB3  . TYR   B 42  ? 0.476023 0.405337 0.863932 -0.0570373  0.0429874   -0.0262608  54  TYR   A HB3  
2466 H HD1  . TYR   B 42  ? 0.468385 0.500263 0.923376 -0.0583542  0.0191261   -0.0222866  54  TYR   A HD1  
2467 H HD2  . TYR   B 42  ? 0.506386 0.452209 0.925108 -0.0934516  0.0119139   -0.0728457  54  TYR   A HD2  
2468 H HE1  . TYR   B 42  ? 0.500489 0.58815  1.02562  -0.0865513  -0.0146005  -0.0490539  54  TYR   A HE1  
2469 H HE2  . TYR   B 42  ? 0.556708 0.554155 1.02888  -0.128877   -0.0217937  -0.105496   54  TYR   A HE2  
2471 N N    . VAL   B 43  ? 0.413765 0.330536 0.689873 -0.012547   0.0346525   -0.0103781  55  VAL   A N    
2472 C CA   . VAL   B 43  ? 0.415277 0.314609 0.668123 0.00455479  0.0488567   0.00668863  55  VAL   A CA   
2473 C C    . VAL   B 43  ? 0.428243 0.298546 0.681774 0.00416485  0.0548748   -0.00213139 55  VAL   A C    
2474 O O    . VAL   B 43  ? 0.445492 0.311203 0.704711 -0.0088216  0.0461583   -0.026214   55  VAL   A O    
2475 C CB   . VAL   B 43  ? 0.409533 0.323011 0.620201 0.0181536   0.0376461   0.00938728  55  VAL   A CB   
2476 C CG1  . VAL   B 43  ? 0.36929  0.306703 0.580727 0.0210445   0.0318166   0.014933    55  VAL   A CG1  
2477 C CG2  . VAL   B 43  ? 0.412276 0.326296 0.599062 0.0129768   0.0210791   -0.0105252  55  VAL   A CG2  
2478 H H    . VAL   B 43  ? 0.410456 0.327624 0.679514 -0.0196833  0.0228952   -0.0260149  55  VAL   A H    
2479 H HA   . VAL   B 43  ? 0.42192  0.320183 0.686438 0.00790802  0.0619535   0.0224604   55  VAL   A HA   
2480 H HB   . VAL   B 43  ? 0.406248 0.312868 0.604113 0.0291292   0.0463592   0.0213893   55  VAL   A HB   
2481 H HG11 . VAL   B 43  ? 0.372829 0.319443 0.592488 0.0129084   0.0190809   0.00410215  55  VAL   A HG11 
2482 H HG12 . VAL   B 43  ? 0.381059 0.32156  0.61127  0.0216392   0.0439221   0.0248454   55  VAL   A HG12 
2483 H HG13 . VAL   B 43  ? 0.368279 0.309094 0.55421  0.0304049   0.0289862   0.0190184   55  VAL   A HG13 
2484 H HG21 . VAL   B 43  ? 0.397309 0.320992 0.561518 0.0184263   0.0136191   -0.00801613 55  VAL   A HG21 
2485 H HG22 . VAL   B 43  ? 0.419059 0.320115 0.601694 0.0156913   0.0268305   -0.0137071  55  VAL   A HG22 
2486 H HG23 . VAL   B 43  ? 0.413016 0.331506 0.61132  0.00107761  0.0124937   -0.0227297  55  VAL   A HG23 
2487 N N    . HIS   B 44  ? 0.480418 0.333645 0.725451 0.0203147   0.0685657   0.0168674   56  HIS   A N    
2488 C CA   . HIS   B 44  ? 0.450561 0.284444 0.687395 0.0297461   0.0707711   0.00979667  56  HIS   A CA   
2489 C C    . HIS   B 44  ? 0.403034 0.256112 0.602844 0.0466108   0.0639344   0.0184716   56  HIS   A C    
2490 O O    . HIS   B 44  ? 0.411268 0.279007 0.596343 0.0540503   0.0645711   0.0369117   56  HIS   A O    
2491 C CB   . HIS   B 44  ? 0.474735 0.272417 0.739652 0.0354253   0.0894033   0.0246849   56  HIS   A CB   
2492 C CG   . HIS   B 44  ? 0.511126 0.281827 0.811215 0.0174      0.0941488   0.00215672  56  HIS   A CG   
2493 N ND1  . HIS   B 44  ? 0.510586 0.27724  0.808696 0.00953547  0.0863909   -0.032405   56  HIS   A ND1  
2494 C CD2  . HIS   B 44  ? 0.543241 0.290643 0.880727 0.00336429  0.106673    0.00768314  56  HIS   A CD2  
2495 C CE1  . HIS   B 44  ? 0.568689 0.309612 0.900555 -0.0077738  0.0928368   -0.049174   56  HIS   A CE1  
2496 N NE2  . HIS   B 44  ? 0.551246 0.278495 0.909944 -0.0121064  0.105215    -0.0245039  56  HIS   A NE2  
2497 H H    . HIS   B 44  ? 0.460695 0.316511 0.705827 0.026331    0.0767522   0.0352492   56  HIS   A H    
2498 H HA   . HIS   B 44  ? 0.452216 0.285614 0.690241 0.0201631   0.0636575   -0.0123019  56  HIS   A HA   
2499 H HB2  . HIS   B 44  ? 0.48377  0.28166  0.753334 0.0372394   0.0973452   0.0457088   56  HIS   A HB2  
2500 H HB3  . HIS   B 44  ? 0.485326 0.277002 0.740599 0.0496982   0.0908593   0.0294044   56  HIS   A HB3  
2502 H HD2  . HIS   B 44  ? 0.545226 0.290026 0.89206  0.00346115  0.116036    0.0293675   56  HIS   A HD2  
2503 H HE1  . HIS   B 44  ? 0.568515 0.301846 0.904333 -0.0166265  0.0901332   -0.0752124  56  HIS   A HE1  
2505 N N    . TYR   B 45  ? 0.406634 0.260987 0.593095 0.0513438   0.058778    0.00280517  57  TYR   A N    
2506 C CA   . TYR   B 45  ? 0.36615  0.241564 0.52274  0.0641998   0.0522465   0.00871427  57  TYR   A CA   
2507 C C    . TYR   B 45  ? 0.405087 0.276565 0.565413 0.0740423   0.0557349   -0.00273918 57  TYR   A C    
2508 O O    . TYR   B 45  ? 0.41083  0.268654 0.585488 0.0662447   0.0592728   -0.025849   57  TYR   A O    
2509 C CB   . TYR   B 45  ? 0.34773  0.246535 0.477006 0.0534634   0.0367696   -0.00250621 57  TYR   A CB   
2510 C CG   . TYR   B 45  ? 0.334625 0.237313 0.454511 0.039791    0.0285431   -0.0293317  57  TYR   A CG   
2511 C CD1  . TYR   B 45  ? 0.347044 0.261038 0.449561 0.0429888   0.0275743   -0.0394601  57  TYR   A CD1  
2512 C CD2  . TYR   B 45  ? 0.4202   0.317    0.551412 0.0225448   0.0233552   -0.045157   57  TYR   A CD2  
2513 C CE1  . TYR   B 45  ? 0.363867 0.282834 0.454039 0.0292611   0.0236949   -0.0638576  57  TYR   A CE1  
2514 C CE2  . TYR   B 45  ? 0.402753 0.304282 0.51962  0.0088626   0.0161563   -0.0700323  57  TYR   A CE2  
2515 C CZ   . TYR   B 45  ? 0.422318 0.334812 0.51511  0.0118899   0.0170137   -0.0785974  57  TYR   A CZ   
2516 O OH   . TYR   B 45  ? 0.394608 0.314047 0.468602 -0.0020168  0.0137115   -0.102975   57  TYR   A OH   
2517 H H    . TYR   B 45  ? 0.41273  0.255879 0.61024  0.0453667   0.0601082   -0.0133106  57  TYR   A H    
2518 H HA   . TYR   B 45  ? 0.377518 0.255448 0.530225 0.0740142   0.0560248   0.0284217   57  TYR   A HA   
2519 H HB2  . TYR   B 45  ? 0.333391 0.244716 0.444904 0.0611788   0.0338285   0.00518752  57  TYR   A HB2  
2520 H HB3  . TYR   B 45  ? 0.338447 0.23868  0.472685 0.0476105   0.034878    0.00153527  57  TYR   A HB3  
2521 H HD1  . TYR   B 45  ? 0.341251 0.262794 0.439183 0.0540144   0.0297231   -0.0297741  57  TYR   A HD1  
2522 H HD2  . TYR   B 45  ? 0.39438  0.286559 0.542508 0.0192439   0.0245718   -0.0392261  57  TYR   A HD2  
2523 H HE1  . TYR   B 45  ? 0.372521 0.302356 0.451113 0.0307256   0.0249889   -0.0702685  57  TYR   A HE1  
2524 H HE2  . TYR   B 45  ? 0.420478 0.321164 0.542521 -0.00343242 0.0102848   -0.0807122  57  TYR   A HE2  
2526 N N    . LYS   B 46  ? 0.391596 0.282581 0.53579  0.0891187   0.0526995   0.00904698  58  LYS   A N    
2527 C CA   . LYS   B 46  ? 0.36613  0.270049 0.511045 0.0982873   0.0529553   -0.00310081 58  LYS   A CA   
2528 C C    . LYS   B 46  ? 0.37984  0.317714 0.493188 0.0946754   0.0411462   -0.00435192 58  LYS   A C    
2529 O O    . LYS   B 46  ? 0.373091 0.32126  0.470046 0.0975282   0.035386    0.0125067   58  LYS   A O    
2530 C CB   . LYS   B 46  ? 0.419908 0.317579 0.586592 0.123159    0.0602045   0.0161445   58  LYS   A CB   
2531 C CG   . LYS   B 46  ? 0.463578 0.320947 0.663294 0.129956    0.0730089   0.0256658   58  LYS   A CG   
2532 C CD   . LYS   B 46  ? 0.509131 0.356181 0.731381 0.15747     0.0784063   0.0498414   58  LYS   A CD   
2533 C CE   . LYS   B 46  ? 0.549247 0.348029 0.801913 0.161075    0.0917211   0.0653649   58  LYS   A CE   
2534 N NZ   . LYS   B 46  ? 0.555184 0.346431 0.827877 0.190306    0.0937339   0.0895021   58  LYS   A NZ   
2535 H H    . LYS   B 46  ? 0.379069 0.278198 0.512439 0.0935069   0.0505674   0.0246724   58  LYS   A H    
2536 H HA   . LYS   B 46  ? 0.391667 0.28851  0.543502 0.0902305   0.0556753   -0.0233584  58  LYS   A HA   
2537 H HB2  . LYS   B 46  ? 0.40799  0.318469 0.561702 0.129994    0.0555542   0.0347142   58  LYS   A HB2  
2538 H HB3  . LYS   B 46  ? 0.414919 0.325109 0.586735 0.129274    0.0605067   0.00511218  58  LYS   A HB3  
2539 H HG2  . LYS   B 46  ? 0.474779 0.318785 0.687147 0.121947    0.0775394   0.00415481  58  LYS   A HG2  
2540 H HG3  . LYS   B 46  ? 0.464779 0.312658 0.660892 0.122498    0.0740017   0.0369895   58  LYS   A HG3  
2541 H HD2  . LYS   B 46  ? 0.497974 0.363637 0.703768 0.165198    0.0720359   0.0696122   58  LYS   A HD2  
2542 H HD3  . LYS   B 46  ? 0.508045 0.363273 0.741807 0.165792    0.0791455   0.0362281   58  LYS   A HD3  
2543 H HE2  . LYS   B 46  ? 0.552993 0.332099 0.822438 0.151832    0.0978482   0.043696    58  LYS   A HE2  
2544 H HE3  . LYS   B 46  ? 0.542503 0.336194 0.785552 0.153682    0.0926637   0.0814568   58  LYS   A HE3  
2545 H HZ1  . LYS   B 46  ? 0.564751 0.361073 0.851445 0.197996    0.0943447   0.073138    58  LYS   A HZ1  
2546 H HZ2  . LYS   B 46  ? 0.554737 0.368169 0.809686 0.198265    0.0863044   0.108103    58  LYS   A HZ2  
2547 H HZ3  . LYS   B 46  ? 0.591027 0.350524 0.881112 0.193243    0.101801    0.102843    58  LYS   A HZ3  
2548 N N    . GLY   B 47  ? 0.362407 0.316398 0.466332 0.086013    0.0389237   -0.025873   59  GLY   A N    
2549 C CA   . GLY   B 47  ? 0.336033 0.317993 0.412505 0.078408    0.0292206   -0.0275635  59  GLY   A CA   
2550 C C    . GLY   B 47  ? 0.310643 0.318031 0.394076 0.0828479   0.0337546   -0.0406258  59  GLY   A C    
2551 O O    . GLY   B 47  ? 0.343194 0.345829 0.446796 0.0865896   0.0445885   -0.0572528  59  GLY   A O    
2552 H H    . GLY   B 47  ? 0.374115 0.320699 0.488982 0.0836733   0.0447021   -0.0406181  59  GLY   A H    
2553 H HA2  . GLY   B 47  ? 0.324832 0.312862 0.394288 0.084208    0.0247761   -0.0126928  59  GLY   A HA2  
2554 H HA3  . GLY   B 47  ? 0.32719  0.306357 0.388203 0.0638091   0.0242892   -0.0352587  59  GLY   A HA3  
2555 N N    . LYS   B 48  ? 0.315757 0.352552 0.386117 0.0827262   0.0265853   -0.0348367  60  LYS   A N    
2556 C CA   . LYS   B 48  ? 0.317434 0.387336 0.397585 0.0843811   0.0307254   -0.0469151  60  LYS   A CA   
2557 C C    . LYS   B 48  ? 0.317462 0.41402  0.372715 0.0687899   0.0211388   -0.0462678  60  LYS   A C    
2558 O O    . LYS   B 48  ? 0.293515 0.380845 0.327851 0.063431    0.0108525   -0.0343845  60  LYS   A O    
2559 C CB   . LYS   B 48  ? 0.346895 0.430277 0.461867 0.111532    0.0343767   -0.0369634  60  LYS   A CB   
2560 C CG   . LYS   B 48  ? 0.370003 0.4608   0.479943 0.124342    0.0230856   -0.0110949  60  LYS   A CG   
2561 C CD   . LYS   B 48  ? 0.426956 0.538832 0.570321 0.152047    0.0228525   0.00138886  60  LYS   A CD   
2562 C CE   . LYS   B 48  ? 0.521179 0.641171 0.651076 0.163476    0.0101444   0.0289329   60  LYS   A CE   
2563 N NZ   . LYS   B 48  ? 0.645342 0.804038 0.806279 0.186497    0.00457668  0.036798    60  LYS   A NZ   
2564 H H    . LYS   B 48  ? 0.304239 0.341576 0.360835 0.0808606   0.0194613   -0.0242928  60  LYS   A H    
2565 H HA   . LYS   B 48  ? 0.332107 0.398862 0.413994 0.0770589   0.038064    -0.0632614  60  LYS   A HA   
2566 H HB2  . LYS   B 48  ? 0.348261 0.458333 0.474334 0.112949    0.0374228   -0.0466012  60  LYS   A HB2  
2567 H HB3  . LYS   B 48  ? 0.361947 0.423722 0.494085 0.120007    0.041877    -0.0387316  60  LYS   A HB3  
2568 H HG2  . LYS   B 48  ? 0.374892 0.440216 0.477701 0.124821    0.0230018   -0.00121528 60  LYS   A HG2  
2569 H HG3  . LYS   B 48  ? 0.361648 0.469763 0.452944 0.113888    0.0154223   -0.0115575  60  LYS   A HG3  
2570 H HD2  . LYS   B 48  ? 0.433417 0.57577  0.587363 0.151698    0.0227021   -0.00891588 60  LYS   A HD2  
2571 H HD3  . LYS   B 48  ? 0.449386 0.540189 0.613469 0.162852    0.031312    0.00143182  60  LYS   A HD3  
2572 H HE2  . LYS   B 48  ? 0.531056 0.623812 0.659888 0.169791    0.0132139   0.0422649   60  LYS   A HE2  
2573 H HE3  . LYS   B 48  ? 0.508438 0.639078 0.613831 0.15044     0.00282964  0.0273189   60  LYS   A HE3  
2574 H HZ1  . LYS   B 48  ? 0.614953 0.764082 0.801915 0.19818     0.0125846   0.0341914   60  LYS   A HZ1  
2575 H HZ2  . LYS   B 48  ? 0.593611 0.782216 0.754742 0.178912    0.00077172  0.0256917   60  LYS   A HZ2  
2576 H HZ3  . LYS   B 48  ? 0.615131 0.778306 0.769819 0.196598    -0.00325334 0.0555072   60  LYS   A HZ3  
2577 N N    . LEU   B 49  ? 0.299948 0.427397 0.359101 0.0600363   0.026681    -0.0610463  61  LEU   A N    
2578 C CA   . LEU   B 49  ? 0.334472 0.491396 0.379839 0.045911    0.0191057   -0.0596541  61  LEU   A CA   
2579 C C    . LEU   B 49  ? 0.451744 0.633211 0.516592 0.065484    0.0107446   -0.0461176  61  LEU   A C    
2580 O O    . LEU   B 49  ? 0.384866 0.569597 0.479038 0.0901541   0.0143278   -0.0400833  61  LEU   A O    
2581 C CB   . LEU   B 49  ? 0.369243 0.557697 0.418274 0.0304894   0.0300187   -0.0777269  61  LEU   A CB   
2582 C CG   . LEU   B 49  ? 0.446141 0.614035 0.469238 0.0106439   0.038134    -0.0906029  61  LEU   A CG   
2583 C CD1  . LEU   B 49  ? 0.516414 0.722065 0.539693 -0.00652364 0.0522261   -0.107471   61  LEU   A CD1  
2584 C CD2  . LEU   B 49  ? 0.506123 0.642206 0.492488 -0.00548872 0.024783    -0.0787503  61  LEU   A CD2  
2585 H H    . LEU   B 49  ? 0.323179 0.453907 0.394844 0.0619245   0.0363304   -0.0731924  61  LEU   A H    
2586 H HA   . LEU   B 49  ? 0.348814 0.488453 0.369949 0.033854    0.0120397   -0.0548147  61  LEU   A HA   
2587 H HB2  . LEU   B 49  ? 0.377743 0.586077 0.45491  0.0444382   0.0374109   -0.0835377  61  LEU   A HB2  
2588 H HB3  . LEU   B 49  ? 0.372973 0.579145 0.414283 0.0190593   0.0248365   -0.0756102  61  LEU   A HB3  
2589 H HG   . LEU   B 49  ? 0.456874 0.609566 0.489962 0.0207653   0.0436978   -0.0961581  61  LEU   A HG   
2590 H HD11 . LEU   B 49  ? 0.4996   0.726704 0.552002 0.00704916  0.0615081   -0.116339   61  LEU   A HD11 
2591 H HD12 . LEU   B 49  ? 0.512455 0.706185 0.514085 -0.0198657  0.0570398   -0.114783   61  LEU   A HD12 
2592 H HD13 . LEU   B 49  ? 0.495519 0.716252 0.512049 -0.0179587  0.0474237   -0.102034   61  LEU   A HD13 
2593 H HD21 . LEU   B 49  ? 0.480474 0.593226 0.468332 0.00400728  0.0206986   -0.0731147  61  LEU   A HD21 
2594 H HD22 . LEU   B 49  ? 0.47734  0.62053  0.45911  -0.00942357 0.0175028   -0.0709818  61  LEU   A HD22 
2595 H HD23 . LEU   B 49  ? 0.497894 0.629763 0.464148 -0.0217189  0.0274746   -0.0845195  61  LEU   A HD23 
2596 N N    . SER   B 50  ? 0.405298 0.595809 0.450929 0.0561333   -0.0019072  -0.0389258  62  SER   A N    
2597 C CA   . SER   B 50  ? 0.484682 0.70452  0.543213 0.0725148   -0.012412   -0.0275365  62  SER   A CA   
2598 C C    . SER   B 50  ? 0.431986 0.700357 0.530674 0.0845031   -0.00874009 -0.0338762  62  SER   A C    
2599 O O    . SER   B 50  ? 0.561581 0.847285 0.684238 0.10962     -0.0137393  -0.0216911  62  SER   A O    
2600 C CB   . SER   B 50  ? 0.491675 0.71906  0.522833 0.055066    -0.0257647  -0.027237   62  SER   A CB   
2601 O OG   . SER   B 50  ? 0.491441 0.749824 0.528692 0.0338503   -0.0244574  -0.0415698  62  SER   A OG   
2602 H H    . SER   B 50  ? 0.430253 0.608753 0.454536 0.0398519   -0.00465409 -0.0412779  62  SER   A H    
2603 H HA   . SER   B 50  ? 0.461553 0.664234 0.52138  0.0878579   -0.0132415  -0.0157944  62  SER   A HA   
2604 H HB2  . SER   B 50  ? 0.493579 0.736218 0.526662 0.0660527   -0.0339675  -0.0192125  62  SER   A HB2  
2605 H HB3  . SER   B 50  ? 0.488456 0.68505  0.497902 0.0470387   -0.0260897  -0.0260483  62  SER   A HB3  
2607 N N    . ASN   B 51  ? 0.58617  0.878538 0.694041 0.0672423   0.000772    -0.0518996  63  ASN   A N    
2608 C CA   . ASN   B 51  ? 0.529147 0.867657 0.680394 0.0768994   0.0110643   -0.0639717  63  ASN   A CA   
2609 C C    . ASN   B 51  ? 0.57328  0.896871 0.754865 0.102649    0.0249799   -0.0674663  63  ASN   A C    
2610 O O    . ASN   B 51  ? 0.593118 0.951582 0.812997 0.112231    0.03664     -0.0810168  63  ASN   A O    
2611 C CB   . ASN   B 51  ? 0.505851 0.857438 0.649985 0.0489235   0.026203    -0.0842693  63  ASN   A CB   
2612 H H    . ASN   B 51  ? 0.528421 0.808072 0.613755 0.0473835   0.00170929  -0.0569333  63  ASN   A H    
2613 H HA   . ASN   B 51  ? 0.53976  0.914127 0.708337 0.0829967   0.00215847  -0.0601366  63  ASN   A HA   
2616 N N    . GLY   B 52  ? 0.680068 0.951398 0.847939 0.1125      0.0259675   -0.0580582  64  GLY   A N    
2617 C CA   . GLY   B 52  ? 0.631782 0.879469 0.829045 0.135904    0.0382177   -0.0606147  64  GLY   A CA   
2618 C C    . GLY   B 52  ? 0.746023 0.998711 0.959145 0.129973    0.0594      -0.089669   64  GLY   A C    
2619 O O    . GLY   B 52  ? 0.699618 0.944005 0.949478 0.152913    0.070954    -0.0968263  64  GLY   A O    
2620 H H    . GLY   B 52  ? 0.631123 0.879549 0.771532 0.103375    0.019199    -0.0503951  64  GLY   A H    
2621 H HA2  . GLY   B 52  ? 0.670548 0.880209 0.85162  0.135958    0.0368371   -0.0525881  64  GLY   A HA2  
2622 H HA3  . GLY   B 52  ? 0.673861 0.938249 0.898256 0.157324    0.0339543   -0.0503354  64  GLY   A HA3  
2623 N N    . LYS   B 53  ? 0.764911 1.02604  0.94827  0.09944     0.0656641   -0.106349   65  LYS   A N    
2624 C CA   . LYS   B 53  ? 0.671582 0.947723 0.863082 0.0903629   0.0873136   -0.135371   65  LYS   A CA   
2625 C C    . LYS   B 53  ? 0.589331 0.816881 0.756557 0.08149     0.0966461   -0.149735   65  LYS   A C    
2626 O O    . LYS   B 53  ? 0.607152 0.837625 0.787106 0.0828992   0.115821    -0.175999   65  LYS   A O    
2627 C CB   . LYS   B 53  ? 0.706438 1.02395  0.878809 0.0615002   0.0882564   -0.140839   65  LYS   A CB   
2628 H H    . LYS   B 53  ? 0.721476 0.977575 0.876884 0.083575    0.0566994   -0.0990905  65  LYS   A H    
2629 H HA   . LYS   B 53  ? 0.685892 0.982161 0.915953 0.11006     0.0949582   -0.141714   65  LYS   A HA   
2632 N N    . LYS   B 54  ? 0.487484 0.672731 0.62187  0.0723677   0.083268    -0.134979   66  LYS   A N    
2633 C CA   . LYS   B 54  ? 0.480429 0.623359 0.594461 0.0629098   0.0867508   -0.145955   66  LYS   A CA   
2634 C C    . LYS   B 54  ? 0.573765 0.677058 0.693916 0.076824    0.0746932   -0.123622   66  LYS   A C    
2635 O O    . LYS   B 54  ? 0.559116 0.66458  0.669177 0.0784529   0.0602371   -0.0998285  66  LYS   A O    
2636 C CB   . LYS   B 54  ? 0.520425 0.665892 0.583535 0.0299674   0.0807892   -0.147629   66  LYS   A CB   
2637 H H    . LYS   B 54  ? 0.491798 0.676912 0.617237 0.0716998   0.0708535   -0.117852   66  LYS   A H    
2638 H HA   . LYS   B 54  ? 0.527366 0.670267 0.658076 0.0686548   0.100417    -0.16519    66  LYS   A HA   
2641 N N    . PHE   B 55  ? 0.494432 0.562525 0.63073  0.0849666   0.0819395   -0.132369   67  PHE   A N    
2642 C CA   . PHE   B 55  ? 0.478009 0.508482 0.626382 0.0969946   0.0757022   -0.112414   67  PHE   A CA   
2643 C C    . PHE   B 55  ? 0.50458  0.500814 0.638526 0.0790576   0.0769212   -0.127572   67  PHE   A C    
2644 O O    . PHE   B 55  ? 0.576061 0.574664 0.703931 0.0675842   0.0866615   -0.156822   67  PHE   A O    
2645 C CB   . PHE   B 55  ? 0.505047 0.528964 0.701618 0.127939    0.0851706   -0.107449   67  PHE   A CB   
2646 C CG   . PHE   B 55  ? 0.640808 0.632865 0.851136 0.1441      0.0790653   -0.0764526  67  PHE   A CG   
2647 C CD1  . PHE   B 55  ? 0.686171 0.697157 0.892333 0.15671     0.0667552   -0.0457364  67  PHE   A CD1  
2648 C CD2  . PHE   B 55  ? 0.782875 0.727428 1.01143  0.146216    0.0870593   -0.0784631  67  PHE   A CD2  
2649 C CE1  . PHE   B 55  ? 0.802186 0.786786 1.01585  0.170841    0.0633445   -0.0155823  67  PHE   A CE1  
2650 C CE2  . PHE   B 55  ? 0.862664 0.778565 1.10457  0.159736    0.084655    -0.0471309  67  PHE   A CE2  
2651 C CZ   . PHE   B 55  ? 0.8531   0.789835 1.08555  0.172721    0.0733689   -0.0144499  67  PHE   A CZ   
2652 H H    . PHE   B 55  ? 0.528123 0.595755 0.668324 0.0814068   0.0927219   -0.153373   67  PHE   A H    
2653 H HA   . PHE   B 55  ? 0.467771 0.501984 0.602891 0.0959871   0.0646524   -0.0928892  67  PHE   A HA   
2654 H HB2  . PHE   B 55  ? 0.523884 0.578646 0.730651 0.137081    0.0848058   -0.104773   67  PHE   A HB2  
2655 H HB3  . PHE   B 55  ? 0.549725 0.561152 0.760649 0.128898    0.096801    -0.128074   67  PHE   A HB3  
2656 H HD1  . PHE   B 55  ? 0.675379 0.718022 0.871516 0.154007    0.060893    -0.045565   67  PHE   A HD1  
2657 H HD2  . PHE   B 55  ? 0.780878 0.712869 1.01245  0.137249    0.0948431   -0.101569   67  PHE   A HD2  
2658 H HE1  . PHE   B 55  ? 0.77339  0.77337  0.979348 0.178301    0.0548038   0.00394561  67  PHE   A HE1  
2659 H HE2  . PHE   B 55  ? 0.863412 0.746541 1.11909  0.158498    0.091017    -0.0486053  67  PHE   A HE2  
2660 H HZ   . PHE   B 55  ? 0.853328 0.772274 1.08969  0.180309    0.0725216   0.00767889  67  PHE   A HZ   
2661 N N    . ASP   B 56  ? 0.41817  0.389862 0.543804 0.0741337   0.0666004   -0.109661   68  ASP   A N    
2662 C CA   . ASP   B 56  ? 0.455963 0.402104 0.572707 0.0563917   0.0640771   -0.121676   68  ASP   A CA   
2663 C C    . ASP   B 56  ? 0.429343 0.345935 0.567282 0.064703    0.0622148   -0.0996032  68  ASP   A C    
2664 O O    . ASP   B 56  ? 0.450733 0.37338  0.581192 0.0705702   0.0542693   -0.0730236  68  ASP   A O    
2665 C CB   . ASP   B 56  ? 0.409642 0.371652 0.484316 0.0336956   0.0498352   -0.121658   68  ASP   A CB   
2666 C CG   . ASP   B 56  ? 0.441124 0.385377 0.505624 0.0153398   0.0409333   -0.129572   68  ASP   A CG   
2667 O OD1  . ASP   B 56  ? 0.431194 0.359239 0.508585 0.0090005   0.0482248   -0.153675   68  ASP   A OD1  
2668 O OD2  . ASP   B 56  ? 0.463829 0.410104 0.512203 0.00820892  0.0264788   -0.112833   68  ASP   A OD2  
2669 H H    . ASP   B 56  ? 0.428272 0.402232 0.554795 0.0820996   0.0607673   -0.0893379  68  ASP   A H    
2670 H HA   . ASP   B 56  ? 0.462106 0.401045 0.587912 0.0541262   0.0731839   -0.143438   68  ASP   A HA   
2671 H HB2  . ASP   B 56  ? 0.4271   0.406601 0.487595 0.0269618   0.0531276   -0.134834   68  ASP   A HB2  
2672 H HB3  . ASP   B 56  ? 0.403131 0.372304 0.47062  0.0372759   0.0424666   -0.102768   68  ASP   A HB3  
2673 N N    . SER   B 57  ? 0.459735 0.344625 0.621964 0.062084    0.0701446   -0.111509   69  SER   A N    
2674 C CA   . SER   B 57  ? 0.501594 0.359791 0.682882 0.0637981   0.0698477   -0.0901003  69  SER   A CA   
2675 C C    . SER   B 57  ? 0.459739 0.293311 0.653853 0.0434335   0.070644    -0.109658   69  SER   A C    
2676 O O    . SER   B 57  ? 0.494462 0.313056 0.700335 0.0369076   0.0785311   -0.13951    69  SER   A O    
2677 C CB   . SER   B 57  ? 0.570466 0.408155 0.783372 0.0883277   0.08074     -0.0680843  69  SER   A CB   
2678 O OG   . SER   B 57  ? 0.63941  0.451241 0.882488 0.094185    0.0943659   -0.0900377  69  SER   A OG   
2679 H H    . SER   B 57  ? 0.485624 0.365435 0.653129 0.0580572   0.0768018   -0.133865   69  SER   A H    
2680 H HA   . SER   B 57  ? 0.466955 0.338057 0.631672 0.0610408   0.0609667   -0.0743501  69  SER   A HA   
2681 H HB2  . SER   B 57  ? 0.566116 0.389563 0.786048 0.0873379   0.0808873   -0.0506503  69  SER   A HB2  
2682 H HB3  . SER   B 57  ? 0.552351 0.409323 0.75814  0.100966    0.0782027   -0.0560318  69  SER   A HB3  
2684 N N    . SER   B 58  ? 0.436109 0.266806 0.632114 0.0343823   0.0634427   -0.092184   70  SER   A N    
2685 C CA   . SER   B 58  ? 0.478358 0.291412 0.694069 0.0148808   0.0626637   -0.105477   70  SER   A CA   
2686 C C    . SER   B 58  ? 0.519245 0.29054  0.776053 0.0196188   0.0800426   -0.109613   70  SER   A C    
2687 O O    . SER   B 58  ? 0.558924 0.310416 0.835615 0.00168569  0.0825478   -0.13402    70  SER   A O    
2688 C CB   . SER   B 58  ? 0.452247 0.277598 0.667516 0.0085264   0.0538677   -0.0833105  70  SER   A CB   
2689 O OG   . SER   B 58  ? 0.506341 0.324331 0.731819 0.0253537   0.0631717   -0.050052   70  SER   A OG   
2690 H H    . SER   B 58  ? 0.425862 0.268172 0.612056 0.0403607   0.0592197   -0.072438   70  SER   A H    
2691 H HA   . SER   B 58  ? 0.479264 0.301254 0.681531 0.00172313  0.0562528   -0.128543   70  SER   A HA   
2692 H HB2  . SER   B 58  ? 0.477243 0.295327 0.709514 -0.00545095 0.05264     -0.0924064  70  SER   A HB2  
2693 H HB3  . SER   B 58  ? 0.446696 0.294421 0.637514 0.00552874  0.0425012   -0.0834795  70  SER   A HB3  
2695 N N    . HIS   B 59  ? 0.533896 0.289861 0.80499  0.0433849   0.0911669   -0.0841476  71  HIS   A N    
2696 C CA   . HIS   B 59  ? 0.615499 0.325819 0.926949 0.0513991   0.107615    -0.0785469  71  HIS   A CA   
2697 C C    . HIS   B 59  ? 0.69045  0.381465 1.01643  0.0520532   0.116145    -0.117287   71  HIS   A C    
2698 O O    . HIS   B 59  ? 0.696404 0.34512  1.05653  0.0460532   0.127852    -0.131737   71  HIS   A O    
2699 C CB   . HIS   B 59  ? 0.64188  0.345798 0.958832 0.0801648   0.113881    -0.0392027  71  HIS   A CB   
2700 C CG   . HIS   B 59  ? 0.713621 0.423282 1.02351  0.0786755   0.112647    -0.00170916 71  HIS   A CG   
2701 N ND1  . HIS   B 59  ? 0.751787 0.435149 1.08625  0.0629538   0.121433    0.00844997  71  HIS   A ND1  
2702 C CD2  . HIS   B 59  ? 0.719302 0.461075 0.999636 0.0887474   0.1049      0.0242044   71  HIS   A CD2  
2703 C CE1  . HIS   B 59  ? 0.741192 0.442453 1.0604   0.0653888   0.120897    0.0409026   71  HIS   A CE1  
2704 N NE2  . HIS   B 59  ? 0.715851 0.45126  1.00069  0.0812928   0.110443    0.0492083   71  HIS   A NE2  
2705 H H    . HIS   B 59  ? 0.520809 0.294976 0.775796 0.0549956   0.0875597   -0.068419   71  HIS   A H    
2706 H HA   . HIS   B 59  ? 0.629161 0.325058 0.955963 0.0373607   0.109486    -0.0762728  71  HIS   A HA   
2707 H HB2  . HIS   B 59  ? 0.635495 0.363934 0.934734 0.09153     0.108641    -0.0396597  71  HIS   A HB2  
2708 H HB3  . HIS   B 59  ? 0.687165 0.359439 1.03055  0.089011    0.124388    -0.0384917  71  HIS   A HB3  
2710 H HD2  . HIS   B 59  ? 0.690118 0.455074 0.951158 0.098263    0.0979191   0.0239674   71  HIS   A HD2  
2711 H HE1  . HIS   B 59  ? 0.750765 0.44316  1.08206  0.0562186   0.127706    0.0543877   71  HIS   A HE1  
2713 N N    . ASP   B 60  ? 0.676451 0.398747 0.976926 0.0582298   0.111983    -0.136022   72  ASP   A N    
2714 C CA   . ASP   B 60  ? 0.747322 0.459647 1.05664  0.0578275   0.12224     -0.177853   72  ASP   A CA   
2715 C C    . ASP   B 60  ? 0.707185 0.408415 1.01354  0.0268365   0.119787    -0.216237   72  ASP   A C    
2716 O O    . ASP   B 60  ? 0.750583 0.428608 1.07355  0.0246557   0.132085    -0.252259   72  ASP   A O    
2717 C CB   . ASP   B 60  ? 0.783084 0.540423 1.05932  0.0622071   0.118419    -0.192267   72  ASP   A CB   
2718 C CG   . ASP   B 60  ? 0.80237  0.571399 1.09334  0.0940733   0.124984    -0.172438   72  ASP   A CG   
2719 O OD1  . ASP   B 60  ? 1.04478  0.778409 1.37768  0.114574    0.138221    -0.168643   72  ASP   A OD1  
2720 O OD2  . ASP   B 60  ? 0.824137 0.636923 1.08703  0.0967928   0.116953    -0.165006   72  ASP   A OD2  
2721 H H    . ASP   B 60  ? 0.654381 0.404862 0.932092 0.0622883   0.10396     -0.123335   72  ASP   A H    
2722 H HA   . ASP   B 60  ? 0.764384 0.44901  1.10333  0.0736062   0.133878    -0.174668   72  ASP   A HA   
2723 H HB2  . ASP   B 60  ? 0.744017 0.526775 0.991688 0.0515823   0.106013    -0.183558   72  ASP   A HB2  
2724 H HB3  . ASP   B 60  ? 0.794386 0.550775 1.06755  0.0536768   0.123949    -0.224771   72  ASP   A HB3  
2725 N N    . ARG   B 61  ? 0.638437 0.3605   0.923194 0.00422825  0.10316     -0.210928   73  ARG   A N    
2726 C CA   . ARG   B 61  ? 0.718685 0.437607 1.00204  -0.0265558  0.0954055   -0.242719   73  ARG   A CA   
2727 C C    . ARG   B 61  ? 0.724671 0.409996 1.05036  -0.0375288  0.0991121   -0.230539   73  ARG   A C    
2728 O O    . ARG   B 61  ? 0.701495 0.384913 1.03541  -0.0647841  0.0917413   -0.255211   73  ARG   A O    
2729 C CB   . ARG   B 61  ? 0.701286 0.468234 0.938601 -0.0420864  0.0728228   -0.241321   73  ARG   A CB   
2730 C CG   . ARG   B 61  ? 0.751293 0.547337 0.948368 -0.0338192  0.0731611   -0.252009   73  ARG   A CG   
2731 C CD   . ARG   B 61  ? 0.688832 0.527005 0.83779  -0.0443162  0.053153    -0.242572   73  ARG   A CD   
2732 N NE   . ARG   B 61  ? 0.669509 0.519319 0.817804 -0.0363708  0.0418947   -0.202047   73  ARG   A NE   
2733 C CZ   . ARG   B 61  ? 0.618966 0.488394 0.746786 -0.0221031  0.0393691   -0.177428   73  ARG   A CZ   
2734 N NH1  . ARG   B 61  ? 0.565327 0.443718 0.683388 -0.00915689 0.0502546   -0.182115   73  ARG   A NH1  
2735 N NH2  . ARG   B 61  ? 0.554388 0.435012 0.676655 -0.020908   0.0267825   -0.149511   73  ARG   A NH2  
2736 H H    . ARG   B 61  ? 0.632039 0.373566 0.902704 0.00858034  0.0952315   -0.186653   73  ARG   A H    
2737 H HA   . ARG   B 61  ? 0.737596 0.446165 1.02227  -0.0301118  0.10287     -0.274166   73  ARG   A HA   
2738 H HB2  . ARG   B 61  ? 0.681327 0.458085 0.918546 -0.0376503  0.0662804   -0.21279    73  ARG   A HB2  
2739 H HB3  . ARG   B 61  ? 0.725824 0.49574  0.960333 -0.062333   0.0647503   -0.26181    73  ARG   A HB3  
2740 H HG2  . ARG   B 61  ? 0.759711 0.549253 0.954818 -0.0401173  0.0802523   -0.282996   73  ARG   A HG2  
2741 H HG3  . ARG   B 61  ? 0.717315 0.509483 0.923919 -0.0138544  0.082246    -0.23611    73  ARG   A HG3  
2742 H HD2  . ARG   B 61  ? 0.716437 0.561369 0.852973 -0.0631521  0.0431473   -0.259984   73  ARG   A HD2  
2743 H HD3  . ARG   B 61  ? 0.700318 0.552618 0.828989 -0.0389778  0.0577124   -0.248895   73  ARG   A HD3  
2744 H HE   . ARG   B 61  ? 0.656431 0.500382 0.819944 -0.0420482  0.0369754   -0.194777   73  ARG   A HE   
2745 H HH11 . ARG   B 61  ? 0.595283 0.460401 0.73304  0.00034449  0.0626019   -0.189855   73  ARG   A HH11 
2746 H HH12 . ARG   B 61  ? 0.568269 0.466249 0.662415 -0.0101374  0.0452341   -0.177361   73  ARG   A HH12 
2747 H HH21 . ARG   B 61  ? 0.564068 0.438851 0.701756 -0.0257985  0.0229335   -0.144098   73  ARG   A HH21 
2748 H HH22 . ARG   B 61  ? 0.546614 0.440855 0.651194 -0.0153909  0.0229906   -0.137419   73  ARG   A HH22 
2749 N N    . ASN   B 62  ? 0.723692 0.387433 1.07379  -0.0175092  0.10965     -0.190744   74  ASN   A N    
2750 C CA   . ASN   B 62  ? 0.73465  0.367055 1.12366  -0.025195   0.117492    -0.168009   74  ASN   A CA   
2751 C C    . ASN   B 62  ? 0.690111 0.349526 1.07936  -0.0536086  0.102767    -0.169856   74  ASN   A C    
2752 O O    . ASN   B 62  ? 0.725751 0.361746 1.15261  -0.0734754  0.108485    -0.174275   74  ASN   A O    
2753 C CB   . ASN   B 62  ? 0.800775 0.373792 1.23194  -0.0232635  0.136912    -0.18516    74  ASN   A CB   
2754 C CG   . ASN   B 62  ? 0.808514 0.338841 1.28178  -0.0261493  0.150466    -0.153183   74  ASN   A CG   
2755 O OD1  . ASN   B 62  ? 0.830457 0.366632 1.30002  -0.0111103  0.153032    -0.1067     74  ASN   A OD1  
2756 N ND2  . ASN   B 62  ? 0.839145 0.327404 1.35077  -0.0482045  0.15968     -0.177471   74  ASN   A ND2  
2757 H H    . ASN   B 62  ? 0.707024 0.377769 1.04764  0.00181043  0.112339    -0.175761   74  ASN   A H    
2758 H HA   . ASN   B 62  ? 0.715977 0.350161 1.10334  -0.00876713 0.120631    -0.134926   74  ASN   A HA   
2759 H HB2  . ASN   B 62  ? 0.801082 0.36628  1.22993  -0.00221268 0.143596    -0.18432    74  ASN   A HB2  
2760 H HB3  . ASN   B 62  ? 0.815135 0.384089 1.24922  -0.0413506  0.134765    -0.220374   74  ASN   A HB3  
2761 H HD21 . ASN   B 62  ? 0.859525 0.329839 1.39422  -0.0573628  0.165748    -0.160459   74  ASN   A HD21 
2762 H HD22 . ASN   B 62  ? 0.86829  0.346035 1.38285  -0.0548742  0.160517    -0.211613   74  ASN   A HD22 
2763 N N    . GLU   B 63  ? 0.656139 0.364758 1.00811  -0.0549325  0.084065    -0.164382   75  GLU   A N    
2764 C CA   . GLU   B 63  ? 0.61937  0.359465 0.974749 -0.0763469  0.0679003   -0.163025   75  GLU   A CA   
2765 C C    . GLU   B 63  ? 0.550978 0.329546 0.876119 -0.0624142  0.0566976   -0.133332   75  GLU   A C    
2766 O O    . GLU   B 63  ? 0.46077  0.251742 0.750522 -0.0460215  0.0533529   -0.128686   75  GLU   A O    
2767 C CB   . GLU   B 63  ? 0.645338 0.409441 0.985345 -0.101066   0.0482462   -0.202413   75  GLU   A CB   
2768 C CG   . GLU   B 63  ? 0.690461 0.422812 1.06335  -0.123707   0.0552374   -0.238933   75  GLU   A CG   
2769 C CD   . GLU   B 63  ? 0.74572  0.457844 1.17425  -0.140817   0.0639564   -0.229685   75  GLU   A CD   
2770 O OE1  . GLU   B 63  ? 0.84965  0.518294 1.30945  -0.151991   0.0780586   -0.251729   75  GLU   A OE1  
2771 O OE2  . GLU   B 63  ? 0.757082 0.494577 1.20218  -0.145199   0.0587078   -0.203637   75  GLU   A OE2  
2772 H H    . GLU   B 63  ? 0.632455 0.355289 0.958808 -0.0415999  0.0813271   -0.160756   75  GLU   A H    
2773 H HA   . GLU   B 63  ? 0.635373 0.35994  1.02303  -0.084018   0.0758802   -0.153723   75  GLU   A HA   
2774 H HB2  . GLU   B 63  ? 0.634323 0.409608 0.941745 -0.0945675  0.0434145   -0.212082   75  GLU   A HB2  
2775 H HB3  . GLU   B 63  ? 0.62084  0.41209  0.960887 -0.109395   0.0350159   -0.194832   75  GLU   A HB3  
2776 H HG2  . GLU   B 63  ? 0.721672 0.425906 1.09542  -0.113496   0.0687376   -0.247879   75  GLU   A HG2  
2777 H HG3  . GLU   B 63  ? 0.708681 0.460654 1.06533  -0.139204   0.0410001   -0.264618   75  GLU   A HG3  
2778 N N    . PRO   B 64  ? 0.538506 0.337958 0.879673 -0.0689151  0.051759    -0.113642   76  PRO   A N    
2779 C CA   . PRO   B 64  ? 0.509658 0.340887 0.824282 -0.0543375  0.0431637   -0.0887301  76  PRO   A CA   
2780 C C    . PRO   B 64  ? 0.501825 0.363865 0.778912 -0.0587775  0.0194728   -0.105371   76  PRO   A C    
2781 O O    . PRO   B 64  ? 0.523272 0.392078 0.799745 -0.0773625  0.00691701  -0.13279    76  PRO   A O    
2782 C CB   . PRO   B 64  ? 0.511588 0.357332 0.860483 -0.062386   0.0463966   -0.071077   76  PRO   A CB   
2783 C CG   . PRO   B 64  ? 0.566422 0.387034 0.961965 -0.0829109  0.0578848   -0.083052   76  PRO   A CG   
2784 C CD   . PRO   B 64  ? 0.591256 0.385881 0.979459 -0.0906556  0.0557594   -0.116651   76  PRO   A CD   
2785 H HA   . PRO   B 64  ? 0.504326 0.326052 0.806355 -0.0373735  0.0521934   -0.072734   76  PRO   A HA   
2786 H HB2  . PRO   B 64  ? 0.498127 0.371499 0.843678 -0.0681157  0.0313962   -0.07587    76  PRO   A HB2  
2787 H HB3  . PRO   B 64  ? 0.504279 0.348611 0.84956  -0.049098   0.0565034   -0.0477094  76  PRO   A HB3  
2788 H HG2  . PRO   B 64  ? 0.558499 0.399612 0.975507 -0.0976412  0.050159    -0.0891433  76  PRO   A HG2  
2789 H HG3  . PRO   B 64  ? 0.571298 0.372206 0.981356 -0.0770668  0.0749492   -0.0636834  76  PRO   A HG3  
2790 H HD2  . PRO   B 64  ? 0.590466 0.399958 0.982193 -0.107579   0.0422354   -0.139281   76  PRO   A HD2  
2791 H HD3  . PRO   B 64  ? 0.611311 0.373393 1.0218   -0.0923553  0.0708456   -0.116355   76  PRO   A HD3  
2792 N N    . PHE   B 65  ? 0.441166 0.320678 0.686597 -0.0427291  0.0137077   -0.0870266  77  PHE   A N    
2793 C CA   . PHE   B 65  ? 0.439798 0.344683 0.64855  -0.0442963  -0.00699349 -0.0921099  77  PHE   A CA   
2794 C C    . PHE   B 65  ? 0.45817  0.387763 0.68304  -0.045739   -0.0191012  -0.0778672  77  PHE   A C    
2795 O O    . PHE   B 65  ? 0.385429 0.316592 0.628727 -0.0348367  -0.00771462 -0.0565433  77  PHE   A O    
2796 C CB   . PHE   B 65  ? 0.398546 0.303816 0.571963 -0.0259066  -0.00314    -0.0783877  77  PHE   A CB   
2797 C CG   . PHE   B 65  ? 0.389698 0.315386 0.524856 -0.0285302  -0.0221945  -0.0794763  77  PHE   A CG   
2798 C CD1  . PHE   B 65  ? 0.430053 0.36242  0.53905  -0.0425544  -0.0335668  -0.100343   77  PHE   A CD1  
2799 C CD2  . PHE   B 65  ? 0.33075  0.268024 0.458005 -0.0189783  -0.0290263  -0.0595047  77  PHE   A CD2  
2800 C CE1  . PHE   B 65  ? 0.455027 0.403154 0.527187 -0.0457199  -0.0507159  -0.0950994  77  PHE   A CE1  
2801 C CE2  . PHE   B 65  ? 0.378878 0.328542 0.474578 -0.0214922  -0.0469288  -0.057      77  PHE   A CE2  
2802 C CZ   . PHE   B 65  ? 0.382754 0.336964 0.45054  -0.035299   -0.0578751  -0.0726993  77  PHE   A CZ   
2803 H H    . PHE   B 65  ? 0.443188 0.316536 0.690017 -0.0301798  0.0239751   -0.0689059  77  PHE   A H    
2804 H HA   . PHE   B 65  ? 0.45517  0.362432 0.654405 -0.0562807  -0.0152971  -0.112298   77  PHE   A HA   
2805 H HB2  . PHE   B 65  ? 0.415124 0.307604 0.584428 -0.0227062  0.00590327  -0.0863536  77  PHE   A HB2  
2806 H HB3  . PHE   B 65  ? 0.392242 0.296375 0.573388 -0.0152072  0.00417284  -0.0601442  77  PHE   A HB3  
2807 H HD1  . PHE   B 65  ? 0.448041 0.372486 0.561388 -0.0493643  -0.0280372  -0.117542   77  PHE   A HD1  
2808 H HD2  . PHE   B 65  ? 0.342133 0.27716  0.485012 -0.0104597  -0.0205108  -0.0470137  77  PHE   A HD2  
2809 H HE1  . PHE   B 65  ? 0.451053 0.404503 0.500873 -0.0559957  -0.0573995  -0.107539   77  PHE   A HE1  
2810 H HE2  . PHE   B 65  ? 0.351963 0.305309 0.444111 -0.0140112  -0.0503294  -0.0445974  77  PHE   A HE2  
2811 H HZ   . PHE   B 65  ? 0.400144 0.360732 0.444526 -0.0379543  -0.0696432  -0.0683756  77  PHE   A HZ   
2812 N N    . VAL   B 66  ? 0.468448 0.419148 0.688999 -0.0595204  -0.0416633  -0.0908872  78  VAL   A N    
2813 C CA   . VAL   B 66  ? 0.449213 0.427094 0.695968 -0.060822   -0.0554907  -0.0809368  78  VAL   A CA   
2814 C C    . VAL   B 66  ? 0.408971 0.402477 0.619505 -0.0540198  -0.0773311  -0.0733809  78  VAL   A C    
2815 O O    . VAL   B 66  ? 0.42235  0.415443 0.594411 -0.0618942  -0.0903332  -0.0845678  78  VAL   A O    
2816 C CB   . VAL   B 66  ? 0.436067 0.429047 0.718366 -0.0834034  -0.0672326  -0.100668   78  VAL   A CB   
2817 C CG1  . VAL   B 66  ? 0.440676 0.470199 0.755749 -0.0828327  -0.0844088  -0.0906483  78  VAL   A CG1  
2818 C CG2  . VAL   B 66  ? 0.49687  0.466965 0.817312 -0.0931661  -0.0441846  -0.108415   78  VAL   A CG2  
2819 H H    . VAL   B 66  ? 0.479    0.429331 0.680479 -0.0677186  -0.0490471  -0.10603    78  VAL   A H    
2820 H HA   . VAL   B 66  ? 0.425297 0.401742 0.69057  -0.0518578  -0.0428667  -0.0668218  78  VAL   A HA   
2821 H HB   . VAL   B 66  ? 0.468668 0.463616 0.727115 -0.0926167  -0.0798699  -0.115823   78  VAL   A HB   
2822 H HG11 . VAL   B 66  ? 0.419033 0.448708 0.744062 -0.0695635  -0.0732723  -0.0743416  78  VAL   A HG11 
2823 H HG12 . VAL   B 66  ? 0.438046 0.480664 0.731169 -0.0821068  -0.104258   -0.0910181  78  VAL   A HG12 
2824 H HG13 . VAL   B 66  ? 0.446517 0.486966 0.795697 -0.0964701  -0.0864879  -0.100437   78  VAL   A HG13 
2825 H HG21 . VAL   B 66  ? 0.495097 0.477685 0.843309 -0.108716   -0.0517753  -0.120261   78  VAL   A HG21 
2826 H HG22 . VAL   B 66  ? 0.495808 0.444217 0.798476 -0.0940626  -0.0368244  -0.1187     78  VAL   A HG22 
2827 H HG23 . VAL   B 66  ? 0.470984 0.435603 0.806499 -0.0832922  -0.0290041  -0.0911656  78  VAL   A HG23 
2828 N N    . PHE   B 67  ? 0.39543  0.401376 0.618286 -0.0399454  -0.0800346  -0.0546078  79  PHE   A N    
2829 C CA   . PHE   B 67  ? 0.378211 0.393235 0.572395 -0.0329926  -0.101689   -0.045512   79  PHE   A CA   
2830 C C    . PHE   B 67  ? 0.357774 0.392378 0.589276 -0.0204643  -0.106815   -0.0320999  79  PHE   A C    
2831 O O    . PHE   B 67  ? 0.293884 0.333556 0.563178 -0.0151545  -0.0875273  -0.0280859  79  PHE   A O    
2832 C CB   . PHE   B 67  ? 0.391121 0.386294 0.53773  -0.0230649  -0.0955579  -0.0374379  79  PHE   A CB   
2833 C CG   . PHE   B 67  ? 0.374516 0.359386 0.523413 -0.00514066 -0.0762228  -0.0235736  79  PHE   A CG   
2834 C CD1  . PHE   B 67  ? 0.421089 0.395467 0.581052 -0.00109037 -0.0520783  -0.022749   79  PHE   A CD1  
2835 C CD2  . PHE   B 67  ? 0.342948 0.328473 0.484767 0.00775482  -0.0827784  -0.0113459  79  PHE   A CD2  
2836 C CE1  . PHE   B 67  ? 0.410653 0.380982 0.570374 0.0139077   -0.0361728  -0.00986889 79  PHE   A CE1  
2837 C CE2  . PHE   B 67  ? 0.36074  0.339046 0.5017   0.0220408   -0.0651181  -0.00327982 79  PHE   A CE2  
2838 C CZ   . PHE   B 67  ? 0.349601 0.323855 0.499041 0.0248738   -0.0425779  -0.002158   79  PHE   A CZ   
2839 H H    . PHE   B 67  ? 0.382045 0.389525 0.630774 -0.0346759  -0.0677652  -0.0474517  79  PHE   A H    
2840 H HA   . PHE   B 67  ? 0.398777 0.422715 0.582933 -0.0441647  -0.118843   -0.054053   79  PHE   A HA   
2841 H HB2  . PHE   B 67  ? 0.394939 0.393855 0.522255 -0.0233785  -0.111788   -0.0331116  79  PHE   A HB2  
2842 H HB3  . PHE   B 67  ? 0.394265 0.380187 0.523267 -0.0297749  -0.0895204  -0.0469236  79  PHE   A HB3  
2843 H HD1  . PHE   B 67  ? 0.413693 0.383917 0.58315  -0.00895099 -0.046875   -0.0308702  79  PHE   A HD1  
2844 H HD2  . PHE   B 67  ? 0.365087 0.354429 0.499938 0.00649879  -0.09959    -0.00899944 79  PHE   A HD2  
2845 H HE1  . PHE   B 67  ? 0.395097 0.358772 0.559577 0.0167178   -0.0212958  -0.0066746  79  PHE   A HE1  
2846 H HE2  . PHE   B 67  ? 0.353473 0.330272 0.490237 0.0302065   -0.069033   0.00190114  79  PHE   A HE2  
2847 H HZ   . PHE   B 67  ? 0.358317 0.32991  0.502449 0.0340661   -0.0319114  0.00372035  79  PHE   A HZ   
2848 N N    . SER   B 68  ? 0.357965 0.402724 0.577775 -0.0154357  -0.131768   -0.0244527  80  SER   A N    
2849 C CA   . SER   B 68  ? 0.374423 0.437155 0.63127  0.00037946  -0.138675   -0.0128499  80  SER   A CA   
2850 C C    . SER   B 68  ? 0.338564 0.379019 0.570432 0.0190234   -0.129016   -0.00072225 80  SER   A C    
2851 O O    . SER   B 68  ? 0.376805 0.398271 0.564254 0.0189135   -0.139701   0.0045067   80  SER   A O    
2852 C CB   . SER   B 68  ? 0.380501 0.466694 0.647699 -0.00157889 -0.173343   -0.00932144 80  SER   A CB   
2853 O OG   . SER   B 68  ? 0.452254 0.563171 0.744996 -0.0209468  -0.182746   -0.0240946  80  SER   A OG   
2854 H H    . SER   B 68  ? 0.377927 0.41786  0.56662  -0.0214384  -0.144176   -0.026076   80  SER   A H    
2855 H HA   . SER   B 68  ? 0.352323 0.427175 0.646251 0.00081096  -0.125875   -0.0153118  80  SER   A HA   
2856 H HB2  . SER   B 68  ? 0.411408 0.484971 0.639637 -0.00340064 -0.185716   -0.00486813 80  SER   A HB2  
2857 H HB3  . SER   B 68  ? 0.393748 0.49132  0.689808 0.0117838   -0.176621   -0.00167321 80  SER   A HB3  
2859 N N    . LEU   B 69  ? 0.352965 0.397237 0.613662 0.0329711   -0.108103   0.00251918  81  LEU   A N    
2860 C CA   . LEU   B 69  ? 0.325568 0.34839  0.561041 0.0480647   -0.0943862  0.0084107   81  LEU   A CA   
2861 C C    . LEU   B 69  ? 0.29855  0.314188 0.529675 0.0608318   -0.114784   0.0161835   81  LEU   A C    
2862 O O    . LEU   B 69  ? 0.32828  0.363959 0.59883  0.0689817   -0.130469   0.0195389   81  LEU   A O    
2863 C CB   . LEU   B 69  ? 0.354098 0.386739 0.618867 0.0590757   -0.0666189  0.0083047   81  LEU   A CB   
2864 C CG   . LEU   B 69  ? 0.366126 0.378743 0.599577 0.0723348   -0.0508803  0.0101463   81  LEU   A CG   
2865 C CD1  . LEU   B 69  ? 0.37667  0.372164 0.569382 0.0642987   -0.0382181  0.0104323   81  LEU   A CD1  
2866 C CD2  . LEU   B 69  ? 0.443922 0.474337 0.711681 0.086469    -0.0284304  0.00870399  81  LEU   A CD2  
2867 H H    . LEU   B 69  ? 0.335925 0.397923 0.632524 0.0319524   -0.101711   1.982e-05   81  LEU   A H    
2868 H HA   . LEU   B 69  ? 0.327264 0.333328 0.528309 0.0426038   -0.0897225  0.0073634   81  LEU   A HA   
2869 H HB2  . LEU   B 69  ? 0.341821 0.377719 0.612633 0.0506576   -0.0544677  0.0063413   81  LEU   A HB2  
2870 H HB3  . LEU   B 69  ? 0.348274 0.399808 0.649358 0.0652382   -0.0700695  0.0084016   81  LEU   A HB3  
2871 H HG   . LEU   B 69  ? 0.387163 0.387772 0.605498 0.0769518   -0.0641834  0.0115001   81  LEU   A HG   
2872 H HD11 . LEU   B 69  ? 0.373077 0.359983 0.54628  0.0560556   -0.0505166  0.00948316  81  LEU   A HD11 
2873 H HD12 . LEU   B 69  ? 0.374107 0.360579 0.547157 0.0714884   -0.0303762  0.0108163   81  LEU   A HD12 
2874 H HD13 . LEU   B 69  ? 0.367236 0.370296 0.574221 0.0602187   -0.0256651  0.011094    81  LEU   A HD13 
2875 H HD21 . LEU   B 69  ? 0.42411  0.462526 0.715093 0.0953209   -0.0371115  0.00759831  81  LEU   A HD21 
2876 H HD22 . LEU   B 69  ? 0.413389 0.45889  0.703786 0.0806562   -0.0175349  0.00930186  81  LEU   A HD22 
2877 H HD23 . LEU   B 69  ? 0.421289 0.440607 0.664942 0.0919069   -0.016198   0.0079755   81  LEU   A HD23 
2878 N N    . GLY   B 70  ? 0.336132 0.322828 0.521026 0.0615558   -0.11637    0.0198845   82  GLY   A N    
2879 C CA   . GLY   B 70  ? 0.397128 0.365498 0.575769 0.074337    -0.129383   0.0279681   82  GLY   A CA   
2880 C C    . GLY   B 70  ? 0.534724 0.497945 0.697167 0.0675757   -0.160774   0.0395228   82  GLY   A C    
2881 O O    . GLY   B 70  ? 0.655853 0.601702 0.820397 0.0798483   -0.174446   0.0501849   82  GLY   A O    
2882 H H    . GLY   B 70  ? 0.332716 0.31013  0.491065 0.0535603   -0.108951   0.0172395   82  GLY   A H    
2883 H HA2  . GLY   B 70  ? 0.408942 0.357669 0.560674 0.0749471   -0.120277   0.026885    82  GLY   A HA2  
2884 H HA3  . GLY   B 70  ? 0.406652 0.384806 0.619094 0.0875298   -0.125797   0.0271375   82  GLY   A HA3  
2885 N N    . LYS   B 71  ? 0.472163 0.450339 0.621269 0.0493868   -0.171972   0.03731     83  LYS   A N    
2886 C CA   . LYS   B 71  ? 0.553525 0.529049 0.674072 0.0392913   -0.20105    0.0485292   83  LYS   A CA   
2887 C C    . LYS   B 71  ? 0.577128 0.525811 0.634676 0.0242096   -0.197354   0.0512593   83  LYS   A C    
2888 O O    . LYS   B 71  ? 0.56448  0.507519 0.586575 0.0128924   -0.216689   0.061938    83  LYS   A O    
2889 C CB   . LYS   B 71  ? 0.478058 0.488997 0.619969 0.0276213   -0.216989   0.0418311   83  LYS   A CB   
2890 H H    . LYS   B 71  ? 0.478863 0.468331 0.635084 0.042655    -0.160693   0.0283397   83  LYS   A H    
2891 H HA   . LYS   B 71  ? 0.546306 0.515802 0.678679 0.0511251   -0.21406    0.0597525   83  LYS   A HA   
2894 N N    . GLY   B 72  ? 0.694012 0.624788 0.73351  0.0241816   -0.173823   0.0448763   84  GLY   A N    
2895 C CA   . GLY   B 72  ? 0.673121 0.588544 0.660106 0.00731882  -0.171163   0.0460568   84  GLY   A CA   
2896 C C    . GLY   B 72  ? 0.698759 0.63286  0.663585 -0.0120908  -0.173547   0.0359767   84  GLY   A C    
2897 O O    . GLY   B 72  ? 0.690767 0.617633 0.611798 -0.0271356  -0.175009   0.0384408   84  GLY   A O    
2898 H H    . GLY   B 72  ? 0.632553 0.563098 0.691232 0.0336902   -0.159735   0.0398404   84  GLY   A H    
2899 H HA2  . GLY   B 72  ? 0.671278 0.579044 0.653364 0.00902321  -0.154407   0.0402911   84  GLY   A HA2  
2900 H HA3  . GLY   B 72  ? 0.709358 0.609266 0.679357 0.00646827  -0.183554   0.0587778   84  GLY   A HA3  
2901 N N    . GLN   B 73  ? 0.574657 0.530942 0.570372 -0.0126844  -0.168223   0.0215889   85  GLN   A N    
2902 C CA   . GLN   B 73  ? 0.480064 0.44988  0.46196  -0.0295425  -0.164404   0.00481175  85  GLN   A CA   
2903 C C    . GLN   B 73  ? 0.457047 0.417849 0.427457 -0.0305496  -0.136821   -0.0064599  85  GLN   A C    
2904 O O    . GLN   B 73  ? 0.435296 0.401659 0.392164 -0.0421273  -0.128439   -0.0220044  85  GLN   A O    
2905 C CB   . GLN   B 73  ? 0.457674 0.44843  0.485274 -0.0294269  -0.165381   -0.00707386 85  GLN   A CB   
2906 C CG   . GLN   B 73  ? 0.481374 0.4935   0.530842 -0.030038   -0.194307   -0.00067195 85  GLN   A CG   
2907 C CD   . GLN   B 73  ? 0.466733 0.502682 0.567061 -0.0335948  -0.19216    -0.0151259  85  GLN   A CD   
2908 O OE1  . GLN   B 73  ? 0.491117 0.524053 0.613485 -0.0354488  -0.168516   -0.0280453  85  GLN   A OE1  
2909 N NE2  . GLN   B 73  ? 0.601136 0.662618 0.728527 -0.0330204  -0.218267   -0.00990449 85  GLN   A NE2  
2910 H H    . GLN   B 73  ? 0.556722 0.518787 0.58532  -0.00225915 -0.165575   0.0214216   85  GLN   A H    
2911 H HA   . GLN   B 73  ? 0.519674 0.491204 0.471916 -0.0404385  -0.177404   0.00757881  85  GLN   A HA   
2912 H HB2  . GLN   B 73  ? 0.441098 0.429505 0.495338 -0.0188444  -0.15177    -0.00664137 85  GLN   A HB2  
2913 H HB3  . GLN   B 73  ? 0.464092 0.458337 0.483943 -0.0400521  -0.158714   -0.0209692  85  GLN   A HB3  
2914 H HG2  . GLN   B 73  ? 0.504402 0.52025  0.523781 -0.0411734  -0.209173   -8.827e-05  85  GLN   A HG2  
2915 H HG3  . GLN   B 73  ? 0.479143 0.487028 0.540254 -0.0173805  -0.200666   0.0128994   85  GLN   A HG3  
2916 H HE21 . GLN   B 73  ? 0.554041 0.633155 0.713622 -0.0371723  -0.219383   -0.0185042  85  GLN   A HE21 
2917 H HE22 . GLN   B 73  ? 0.57295  0.634556 0.687993 -0.0285153  -0.235174   0.00276692  85  GLN   A HE22 
2918 N N    . VAL   B 74  ? 0.402756 0.351619 0.381588 -0.0171456  -0.123006   -9.163e-05  86  VAL   A N    
2919 C CA   . VAL   B 74  ? 0.373064 0.317624 0.342804 -0.0155574  -0.10111    -0.00702191 86  VAL   A CA   
2920 C C    . VAL   B 74  ? 0.37939  0.309889 0.328696 -0.0119382  -0.100998   0.00349301  86  VAL   A C    
2921 O O    . VAL   B 74  ? 0.424699 0.344024 0.372802 -0.00841407 -0.115332   0.0153739   86  VAL   A O    
2922 C CB   . VAL   B 74  ? 0.378404 0.326785 0.384458 -0.00333954 -0.0837863  -0.0111165  86  VAL   A CB   
2923 C CG1  . VAL   B 74  ? 0.386031 0.343058 0.413235 -0.0109787  -0.0813493  -0.0237724  86  VAL   A CG1  
2924 C CG2  . VAL   B 74  ? 0.332508 0.279846 0.364672 0.0111255   -0.0850394  -0.00119184 86  VAL   A CG2  
2925 H H    . VAL   B 74  ? 0.407609 0.352392 0.399417 -0.00803371 -0.12795    0.00830557  86  VAL   A H    
2926 H HA   . VAL   B 74  ? 0.389329 0.33783  0.342586 -0.0253745  -0.0984038  -0.0151958  86  VAL   A HA   
2927 H HB   . VAL   B 74  ? 0.358587 0.30439  0.356662 -0.00033744 -0.0719609  -0.0124668  86  VAL   A HB   
2928 H HG11 . VAL   B 74  ? 0.392638 0.356202 0.428526 -0.0152031  -0.0945404  -0.0235404  86  VAL   A HG11 
2929 H HG12 . VAL   B 74  ? 0.392442 0.34923  0.402925 -0.0188184  -0.078464   -0.0325789  86  VAL   A HG12 
2930 H HG13 . VAL   B 74  ? 0.373512 0.329985 0.42295  -0.00425369 -0.0693201  -0.0236866  86  VAL   A HG13 
2931 H HG21 . VAL   B 74  ? 0.331744 0.282381 0.382544 0.0173436   -0.0722894  -0.00233785 86  VAL   A HG21 
2932 H HG22 . VAL   B 74  ? 0.345379 0.284171 0.363486 0.0151709   -0.0858599  0.00389931  86  VAL   A HG22 
2933 H HG23 . VAL   B 74  ? 0.349932 0.302681 0.394925 0.00987695  -0.0972785  0.00065421  86  VAL   A HG23 
2934 N N    . ILE   B 75  ? 0.337957 0.268983 0.275424 -0.0122931  -0.0856777  -0.00132084 87  ILE   A N    
2935 C CA   . ILE   B 75  ? 0.349402 0.269055 0.271001 -0.0113912  -0.0844979  0.00498121  87  ILE   A CA   
2936 C C    . ILE   B 75  ? 0.324887 0.234762 0.267726 0.00481877  -0.0842158  0.00971039  87  ILE   A C    
2937 O O    . ILE   B 75  ? 0.351431 0.269638 0.32156  0.0162748   -0.0773464  0.00750171  87  ILE   A O    
2938 C CB   . ILE   B 75  ? 0.349419 0.280685 0.261278 -0.0144487  -0.069247   -0.00288979 87  ILE   A CB   
2939 C CG1  . ILE   B 75  ? 0.365978 0.30893  0.302724 -0.00075412 -0.0553909  -0.00844439 87  ILE   A CG1  
2940 C CG2  . ILE   B 75  ? 0.390976 0.331757 0.278773 -0.0318545  -0.0680877  -0.00838909 87  ILE   A CG2  
2941 C CD1  . ILE   B 75  ? 0.393494 0.35103  0.325329 0.00059619  -0.0439748  -0.0131031  87  ILE   A CD1  
2942 H H    . ILE   B 75  ? 0.340755 0.279709 0.281641 -0.0134128  -0.0765186  -0.00922933 87  ILE   A H    
2943 H HA   . ILE   B 75  ? 0.366058 0.277678 0.269265 -0.020384   -0.0942276  0.0108349   87  ILE   A HA   
2944 H HB   . ILE   B 75  ? 0.362148 0.28737  0.267381 -0.0140294  -0.0691738  -5.173e-05  87  ILE   A HB   
2945 H HG12 . ILE   B 75  ? 0.362295 0.30879  0.307707 -0.0021487  -0.0542369  -0.0127747  87  ILE   A HG12 
2946 H HG13 . ILE   B 75  ? 0.357608 0.296114 0.306531 0.00878811  -0.0548565  -0.00442823 87  ILE   A HG13 
2947 H HG21 . ILE   B 75  ? 0.379271 0.3282   0.262507 -0.0341098  -0.060157   -0.0117477  87  ILE   A HG21 
2948 H HG22 . ILE   B 75  ? 0.380184 0.328586 0.274811 -0.0318882  -0.0650859  -0.015532   87  ILE   A HG22 
2949 H HG23 . ILE   B 75  ? 0.401342 0.333356 0.271845 -0.041072   -0.0778325  -0.00175841 87  ILE   A HG23 
2950 H HD11 . ILE   B 75  ? 0.386521 0.342181 0.306901 -0.00267464 -0.046655   -0.0110279  87  ILE   A HD11 
2951 H HD12 . ILE   B 75  ? 0.372733 0.334703 0.319042 0.0116134   -0.0370315  -0.0122423  87  ILE   A HD12 
2952 H HD13 . ILE   B 75  ? 0.386333 0.351752 0.313183 -0.00638916 -0.0410476  -0.0191149  87  ILE   A HD13 
2953 N N    . LYS   B 76  ? 0.398781 0.290523 0.329156 0.00473599  -0.0887327  0.014504    88  LYS   A N    
2954 C CA   . LYS   B 76  ? 0.393125 0.272162 0.340881 0.0197199   -0.0881541  0.015167    88  LYS   A CA   
2955 C C    . LYS   B 76  ? 0.37742  0.271919 0.337609 0.0310166   -0.0704307  0.006862    88  LYS   A C    
2956 O O    . LYS   B 76  ? 0.392829 0.291438 0.377789 0.0448105   -0.0650217  0.00609803  88  LYS   A O    
2957 C CB   . LYS   B 76  ? 0.43473  0.285027 0.364294 0.0143145   -0.0957005  0.0190815   88  LYS   A CB   
2958 H H    . LYS   B 76  ? 0.392847 0.279296 0.303359 -0.00588336 -0.0911951  0.0162365   88  LYS   A H    
2959 H HA   . LYS   B 76  ? 0.400262 0.279529 0.365409 0.0257905   -0.095022   0.0190632   88  LYS   A HA   
2962 N N    . ALA   B 77  ? 0.377948 0.285877 0.324339 0.0258044   -0.0610955  0.00239236  89  ALA   A N    
2963 C CA   . ALA   B 77  ? 0.341439 0.264765 0.294607 0.0367997   -0.0465808  -0.00071369 89  ALA   A CA   
2964 C C    . ALA   B 77  ? 0.352238 0.285032 0.331932 0.0461134   -0.0385361  0.00303483  89  ALA   A C    
2965 O O    . ALA   B 77  ? 0.341914 0.281177 0.33058  0.0570448   -0.0271615  0.00431502  89  ALA   A O    
2966 C CB   . ALA   B 77  ? 0.334676 0.274042 0.274402 0.0319373   -0.0413728  -0.00325274 89  ALA   A CB   
2967 H H    . ALA   B 77  ? 0.372759 0.28162  0.305347 0.0155686   -0.0639685  0.00225935  89  ALA   A H    
2968 H HA   . ALA   B 77  ? 0.358272 0.27593  0.308631 0.0419613   -0.0448452  -0.00351937 89  ALA   A HA   
2969 H HB1  . ALA   B 77  ? 0.343231 0.280075 0.268969 0.0258208   -0.0447249  -0.0065731  89  ALA   A HB1  
2970 H HB2  . ALA   B 77  ? 0.330593 0.273884 0.271751 0.026233    -0.0424546  -0.00302353 89  ALA   A HB2  
2971 H HB3  . ALA   B 77  ? 0.329351 0.27874  0.274079 0.0405391   -0.0335152  -0.00197033 89  ALA   A HB3  
2972 N N    . TRP   B 78  ? 0.34988  0.284075 0.341769 0.0395823   -0.0440414  0.0041551   90  TRP   A N    
2973 C CA   . TRP   B 78  ? 0.340392 0.282399 0.361069 0.0443423   -0.0365605  0.00608486  90  TRP   A CA   
2974 C C    . TRP   B 78  ? 0.331527 0.274175 0.376919 0.0511974   -0.0395713  0.00811433  90  TRP   A C    
2975 O O    . TRP   B 78  ? 0.322516 0.274682 0.391075 0.0587262   -0.0258267  0.0106232   90  TRP   A O    
2976 C CB   . TRP   B 78  ? 0.356628 0.30099  0.383101 0.0332349   -0.0410505  0.00162034  90  TRP   A CB   
2977 C CG   . TRP   B 78  ? 0.355976 0.303408 0.379252 0.0328493   -0.0295689  -0.00135163 90  TRP   A CG   
2978 C CD1  . TRP   B 78  ? 0.360505 0.312012 0.365098 0.0348273   -0.0247557  -0.00203162 90  TRP   A CD1  
2979 C CD2  . TRP   B 78  ? 0.333626 0.28035  0.380914 0.031544    -0.0211488  -0.00429259 90  TRP   A CD2  
2980 N NE1  . TRP   B 78  ? 0.351635 0.305308 0.368583 0.0383455   -0.0141581  -0.0037096  90  TRP   A NE1  
2981 C CE2  . TRP   B 78  ? 0.330388 0.277128 0.372199 0.0358092   -0.0110986  -0.00550399 90  TRP   A CE2  
2982 C CE3  . TRP   B 78  ? 0.308416 0.254831 0.384313 0.0266003   -0.021586   -0.00676481 90  TRP   A CE3  
2983 C CZ2  . TRP   B 78  ? 0.335634 0.275287 0.39847  0.0360938   -0.00121749 -0.00941985 90  TRP   A CZ2  
2984 C CZ3  . TRP   B 78  ? 0.317794 0.257752 0.413951 0.0240457   -0.0106587  -0.0110569  90  TRP   A CZ3  
2985 C CH2  . TRP   B 78  ? 0.36569  0.29903  0.454538 0.029525    -0.00033385 -0.0120803  90  TRP   A CH2  
2986 H H    . TRP   B 78  ? 0.354115 0.284749 0.335247 0.0307958   -0.0521297  0.00311409  90  TRP   A H    
2987 H HA   . TRP   B 78  ? 0.337599 0.28451  0.359941 0.0503152   -0.0250384  0.00836572  90  TRP   A HA   
2988 H HB2  . TRP   B 78  ? 0.359885 0.300834 0.37206  0.0255397   -0.0520353  -0.00027737 90  TRP   A HB2  
2989 H HB3  . TRP   B 78  ? 0.351503 0.299053 0.399778 0.0333788   -0.0414519  0.00180311  90  TRP   A HB3  
2990 H HD1  . TRP   B 78  ? 0.357512 0.31028  0.346138 0.0343389   -0.028075   -0.00147506 90  TRP   A HD1  
2991 H HE1  . TRP   B 78  ? 0.346326 0.30506  0.358291 0.041206    -0.0105373  -0.00434888 90  TRP   A HE1  
2992 H HE3  . TRP   B 78  ? 0.315592 0.266029 0.399836 0.0252294   -0.0289935  -0.00560624 90  TRP   A HE3  
2993 H HZ2  . TRP   B 78  ? 0.344694 0.283737 0.407483 0.0416364   0.00534278  -0.00928579 90  TRP   A HZ2  
2994 H HZ3  . TRP   B 78  ? 0.331706 0.27158  0.448877 0.0181796   -0.0110467  -0.0143131  90  TRP   A HZ3  
2995 H HH2  . TRP   B 78  ? 0.357599 0.282513 0.462471 0.0285545   0.00709386  -0.0153636  90  TRP   A HH2  
2996 N N    . ASP   B 79  ? 0.333711 0.267238 0.375421 0.0488351   -0.0563757  0.00863682  91  ASP   A N    
2997 C CA   . ASP   B 79  ? 0.353179 0.288628 0.423522 0.0593968   -0.0605439  0.0103554   91  ASP   A CA   
2998 C C    . ASP   B 79  ? 0.363819 0.299875 0.438072 0.0730936   -0.0432616  0.00685065  91  ASP   A C    
2999 O O    . ASP   B 79  ? 0.341501 0.292034 0.447158 0.0822018   -0.0325845  0.0062876   91  ASP   A O    
3000 C CB   . ASP   B 79  ? 0.374064 0.297218 0.442065 0.057991    -0.0828277  0.0152119   91  ASP   A CB   
3001 C CG   . ASP   B 79  ? 0.369065 0.30145  0.442706 0.0471555   -0.101741   0.0191397   91  ASP   A CG   
3002 O OD1  . ASP   B 79  ? 0.350582 0.301893 0.44739  0.0436407   -0.0970834  0.0148584   91  ASP   A OD1  
3003 O OD2  . ASP   B 79  ? 0.403307 0.322709 0.457292 0.0417211   -0.121645   0.0271261   91  ASP   A OD2  
3004 H H    . ASP   B 79  ? 0.345201 0.271837 0.368012 0.0411647   -0.0649064  0.00877895  91  ASP   A H    
3005 H HA   . ASP   B 79  ? 0.345937 0.294168 0.440139 0.0587936   -0.0591147  0.0106298   91  ASP   A HA   
3006 H HB2  . ASP   B 79  ? 0.380176 0.288536 0.421928 0.0535998   -0.085874   0.0159486   91  ASP   A HB2  
3007 H HB3  . ASP   B 79  ? 0.376977 0.299657 0.464919 0.0689086   -0.0830541  0.0155152   91  ASP   A HB3  
3008 N N    . ILE   B 80  ? 0.338834 0.26398  0.380823 0.0722985   -0.0388994  0.00316615  92  ILE   A N    
3009 C CA   . ILE   B 80  ? 0.376398 0.302204 0.411892 0.0828373   -0.0242189  -0.00374985 92  ILE   A CA   
3010 C C    . ILE   B 80  ? 0.339629 0.285736 0.377209 0.0863576   -0.00470603 -0.00014135 92  ILE   A C    
3011 O O    . ILE   B 80  ? 0.367757 0.32511  0.419641 0.0960002   0.0107705   -0.00188875 92  ILE   A O    
3012 C CB   . ILE   B 80  ? 0.397463 0.307113 0.397188 0.0774656   -0.0285588  -0.0109419  92  ILE   A CB   
3013 C CG1  . ILE   B 80  ? 0.478183 0.360619 0.477004 0.0747404   -0.0446612  -0.0121591  92  ILE   A CG1  
3014 C CG2  . ILE   B 80  ? 0.447926 0.363659 0.432586 0.0854093   -0.0131597  -0.0215467  92  ILE   A CG2  
3015 C CD1  . ILE   B 80  ? 0.46049  0.327119 0.426262 0.0610851   -0.0509889  -0.016118   92  ILE   A CD1  
3016 H H    . ILE   B 80  ? 0.353009 0.271929 0.3757   0.0639294   -0.0452986  0.00377179  92  ILE   A H    
3017 H HA   . ILE   B 80  ? 0.37442  0.298521 0.428645 0.0909699   -0.0237699  -0.0064804  92  ILE   A HA   
3018 H HB   . ILE   B 80  ? 0.405089 0.318697 0.390619 0.0690982   -0.031115   -0.0079207  92  ILE   A HB   
3019 H HG12 . ILE   B 80  ? 0.468722 0.344542 0.480002 0.0846931   -0.0412785  -0.0177065  92  ILE   A HG12 
3020 H HG13 . ILE   B 80  ? 0.450903 0.332718 0.46014  0.0716836   -0.0544056  -0.00451251 92  ILE   A HG13 
3021 H HG21 . ILE   B 80  ? 0.450663 0.354059 0.418148 0.0813664   -0.0179251  -0.0289172  92  ILE   A HG21 
3022 H HG22 . ILE   B 80  ? 0.442979 0.360955 0.444287 0.0948166   -0.0057197  -0.0250017  92  ILE   A HG22 
3023 H HG23 . ILE   B 80  ? 0.428681 0.359224 0.404387 0.0846488   -0.00604293 -0.0177225  92  ILE   A HG23 
3024 H HD11 . ILE   B 80  ? 0.456138 0.334235 0.411322 0.0527905   -0.0513083  -0.012575   92  ILE   A HD11 
3025 H HD12 . ILE   B 80  ? 0.48411  0.331144 0.449341 0.0572612   -0.0616051  -0.0128307  92  ILE   A HD12 
3026 H HD13 . ILE   B 80  ? 0.479041 0.344384 0.43557  0.0638064   -0.0440002  -0.0257046  92  ILE   A HD13 
3027 N N    . GLY   B 81  ? 0.343864 0.294317 0.369622 0.0788551   -0.00469261 0.00604015  93  GLY   A N    
3028 C CA   . GLY   B 81  ? 0.374088 0.337457 0.395017 0.0826937   0.011335    0.0136488   93  GLY   A CA   
3029 C C    . GLY   B 81  ? 0.352049 0.324244 0.405396 0.0839445   0.0236483   0.022044    93  GLY   A C    
3030 O O    . GLY   B 81  ? 0.354802 0.337605 0.411113 0.0902076   0.0414139   0.0280788   93  GLY   A O    
3031 H H    . GLY   B 81  ? 0.342262 0.287064 0.362774 0.0715985   -0.0147476  0.00616999  93  GLY   A H    
3032 H HA2  . GLY   B 81  ? 0.372688 0.339867 0.379163 0.0880745   0.0180311   0.01107     93  GLY   A HA2  
3033 H HA3  . GLY   B 81  ? 0.357917 0.320887 0.366908 0.0786481   0.00780195  0.0161452   93  GLY   A HA3  
3034 N N    . VAL   B 82  ? 0.355996 0.324927 0.433    0.0756895   0.0144027   0.0217683   94  VAL   A N    
3035 C CA   . VAL   B 82  ? 0.382062 0.359703 0.496249 0.072964    0.0245622   0.0269954   94  VAL   A CA   
3036 C C    . VAL   B 82  ? 0.352272 0.344788 0.49428  0.0797761   0.0331925   0.0250277   94  VAL   A C    
3037 O O    . VAL   B 82  ? 0.390291 0.395017 0.556104 0.0792485   0.0511026   0.0319025   94  VAL   A O    
3038 C CB   . VAL   B 82  ? 0.351757 0.325119 0.483876 0.0606171   0.0111478   0.0225052   94  VAL   A CB   
3039 C CG1  . VAL   B 82  ? 0.432734 0.416693 0.609099 0.0543441   0.0197199   0.0246034   94  VAL   A CG1  
3040 C CG2  . VAL   B 82  ? 0.362552 0.324208 0.472918 0.0557888   0.00905436  0.0221158   94  VAL   A CG2  
3041 H H    . VAL   B 82  ? 0.35459  0.316899 0.424137 0.0704315   0.00203581  0.01776     94  VAL   A H    
3042 H HA   . VAL   B 82  ? 0.370544 0.348501 0.480507 0.0742173   0.0366034   0.0348671   94  VAL   A HA   
3043 H HB   . VAL   B 82  ? 0.369488 0.342334 0.499984 0.0592867   -0.00283148 0.0170126   94  VAL   A HB   
3044 H HG11 . VAL   B 82  ? 0.411961 0.397082 0.591808 0.0570435   0.0359318   0.0326333   94  VAL   A HG11 
3045 H HG12 . VAL   B 82  ? 0.404699 0.399789 0.600034 0.0560817   0.0154126   0.0216851   94  VAL   A HG12 
3046 H HG13 . VAL   B 82  ? 0.405842 0.385052 0.589092 0.0453004   0.0134754   0.0205761   94  VAL   A HG13 
3047 H HG21 . VAL   B 82  ? 0.359563 0.318917 0.481966 0.0474827   0.00351734  0.0171341   94  VAL   A HG21 
3048 H HG22 . VAL   B 82  ? 0.357668 0.316125 0.444657 0.0567705   0.00124762  0.0189901   94  VAL   A HG22 
3049 H HG23 . VAL   B 82  ? 0.363913 0.324208 0.472378 0.0598546   0.0212997   0.0296393   94  VAL   A HG23 
3050 N N    . ALA   B 83  ? 0.370645 0.361918 0.512346 0.0865122   0.0227626   0.0162597   95  ALA   A N    
3051 C CA   . ALA   B 83  ? 0.339447 0.345519 0.508912 0.0973931   0.0328402   0.0112993   95  ALA   A CA   
3052 C C    . ALA   B 83  ? 0.389527 0.406113 0.544605 0.104794    0.0597551   0.0125599   95  ALA   A C    
3053 O O    . ALA   B 83  ? 0.411674 0.448051 0.596431 0.110634    0.076271    0.0103742   95  ALA   A O    
3054 C CB   . ALA   B 83  ? 0.350837 0.344925 0.518595 0.10576     0.0162139   0.00193424  95  ALA   A CB   
3055 H H    . ALA   B 83  ? 0.356447 0.336446 0.481359 0.0845646   0.00933266  0.0131119   95  ALA   A H    
3056 H HA   . ALA   B 83  ? 0.348563 0.367757 0.55217  0.0941836   0.0335491   0.0132354   95  ALA   A HA   
3057 H HB1  . ALA   B 83  ? 0.345008 0.333002 0.51698  0.100384    -0.00116021 0.00377498  95  ALA   A HB1  
3058 H HB2  . ALA   B 83  ? 0.357413 0.338807 0.494609 0.10764     0.0167686   -0.00172256 95  ALA   A HB2  
3059 H HB3  . ALA   B 83  ? 0.3558   0.360889 0.549515 0.114441    0.022431    -0.00222809 95  ALA   A HB3  
3060 N N    . THR   B 84  ? 0.390273 0.398151 0.50051  0.104262    0.0642563   0.01618     96  THR   A N    
3061 C CA   . THR   B 84  ? 0.419831 0.439946 0.5064   0.109998    0.0875139   0.0194261   96  THR   A CA   
3062 C C    . THR   B 84  ? 0.413586 0.443035 0.508029 0.104286    0.104963    0.0393304   96  THR   A C    
3063 O O    . THR   B 84  ? 0.427378 0.470275 0.504472 0.107936    0.126628    0.0461355   96  THR   A O    
3064 C CB   . THR   B 84  ? 0.438775 0.449412 0.472842 0.111259    0.0805128   0.0158267   96  THR   A CB   
3065 O OG1  . THR   B 84  ? 0.420942 0.425645 0.440449 0.104977    0.0727369   0.030005    96  THR   A OG1  
3066 C CG2  . THR   B 84  ? 0.473836 0.468578 0.500478 0.113223    0.0635666   -0.00264152 96  THR   A CG2  
3067 H H    . THR   B 84  ? 0.387675 0.383949 0.480418 0.100015    0.0520903   0.0168338   96  THR   A H    
3068 H HA   . THR   B 84  ? 0.42732  0.456626 0.525794 0.116415    0.0967437   0.0109308   96  THR   A HA   
3069 H HB   . THR   B 84  ? 0.460848 0.481899 0.477407 0.115492    0.0946193   0.0154538   96  THR   A HB   
3071 H HG21 . THR   B 84  ? 0.47595  0.469064 0.472414 0.113962    0.0634764   -0.00862841 96  THR   A HG21 
3072 H HG22 . THR   B 84  ? 0.447735 0.431894 0.479624 0.107682    0.0486119   -0.00054576 96  THR   A HG22 
3073 H HG23 . THR   B 84  ? 0.46776  0.464506 0.515134 0.118921    0.0678897   -0.010602   96  THR   A HG23 
3074 N N    . MET   B 85  ? 0.396178 0.418937 0.518537 0.0946772   0.0984035   0.0480017   97  MET   A N    
3075 C CA   . MET   B 85  ? 0.441557 0.461731 0.567262 0.0885229   0.112796    0.0680739   97  MET   A CA   
3076 C C    . MET   B 85  ? 0.401359 0.436875 0.574278 0.0810739   0.132036    0.0742371   97  MET   A C    
3077 O O    . MET   B 85  ? 0.41804  0.464698 0.633351 0.077178    0.12527     0.0624336   97  MET   A O    
3078 C CB   . MET   B 85  ? 0.38991  0.389322 0.517741 0.081404    0.0973775   0.0718137   97  MET   A CB   
3079 C CG   . MET   B 85  ? 0.383435 0.372876 0.469501 0.0870608   0.0817892   0.0685123   97  MET   A CG   
3080 S SD   . MET   B 85  ? 0.411193 0.381274 0.504352 0.0800971   0.0668062   0.0672109   97  MET   A SD   
3081 C CE   . MET   B 85  ? 0.389671 0.348342 0.494862 0.0807814   0.0863153   0.0916731   97  MET   A CE   
3082 H H    . MET   B 85  ? 0.390272 0.408553 0.529393 0.0916114   0.0846232   0.0411553   97  MET   A H    
3083 H HA   . MET   B 85  ? 0.434882 0.457366 0.531179 0.0933877   0.121901    0.0760947   97  MET   A HA   
3084 H HB2  . MET   B 85  ? 0.384361 0.382803 0.536088 0.0756845   0.0872679   0.0626263   97  MET   A HB2  
3085 H HB3  . MET   B 85  ? 0.409259 0.403741 0.544633 0.0780419   0.108228    0.085124    97  MET   A HB3  
3086 H HG2  . MET   B 85  ? 0.40661  0.399323 0.469749 0.0925077   0.0896568   0.0782501   97  MET   A HG2  
3087 H HG3  . MET   B 85  ? 0.383936 0.375922 0.461526 0.0891235   0.0725612   0.0564092   97  MET   A HG3  
3088 H HE1  . MET   B 85  ? 0.398672 0.344503 0.514121 0.0776094   0.0814484   0.0896187   97  MET   A HE1  
3089 H HE2  . MET   B 85  ? 0.407068 0.36881  0.533142 0.0760715   0.0976574   0.0961779   97  MET   A HE2  
3090 H HE3  . MET   B 85  ? 0.413136 0.375161 0.494426 0.0887548   0.09049     0.102682    97  MET   A HE3  
3091 N N    . LYS   B 86  ? 0.450443 0.487894 0.617504 0.0779924   0.155373    0.094949    98  LYS   A N    
3092 C CA   . LYS   B 86  ? 0.468933 0.52064  0.679772 0.0671571   0.178005    0.104483    98  LYS   A CA   
3093 C C    . LYS   B 86  ? 0.45537  0.484654 0.694542 0.052855    0.173797    0.114278    98  LYS   A C    
3094 O O    . LYS   B 86  ? 0.476405 0.479313 0.692226 0.0547953   0.161825    0.120145    98  LYS   A O    
3095 C CB   . LYS   B 86  ? 0.577008 0.641079 0.759095 0.0700514   0.207825    0.123685    98  LYS   A CB   
3096 C CG   . LYS   B 86  ? 0.641765 0.729004 0.793273 0.0827981   0.216904    0.110218    98  LYS   A CG   
3097 C CD   . LYS   B 86  ? 0.777752 0.881681 0.901736 0.0814708   0.250088    0.130331    98  LYS   A CD   
3098 C CE   . LYS   B 86  ? 0.773148 0.90251  0.865812 0.0926052   0.263625    0.112653    98  LYS   A CE   
3099 N NZ   . LYS   B 86  ? 0.762895 0.876984 0.811243 0.103537    0.237148    0.0973852   98  LYS   A NZ   
3100 H H    . LYS   B 86  ? 0.459723 0.4899   0.594274 0.082202    0.157134    0.104765    98  LYS   A H    
3101 H HA   . LYS   B 86  ? 0.46461  0.533289 0.705    0.0669176   0.176528    0.0910856   98  LYS   A HA   
3102 H HB2  . LYS   B 86  ? 0.58377  0.631467 0.736836 0.0715855   0.206463    0.13876     98  LYS   A HB2  
3103 H HB3  . LYS   B 86  ? 0.582078 0.655052 0.794316 0.0606927   0.224718    0.131985    98  LYS   A HB3  
3104 H HG2  . LYS   B 86  ? 0.633879 0.735743 0.816287 0.084096    0.216576    0.0942528   98  LYS   A HG2  
3105 H HG3  . LYS   B 86  ? 0.643004 0.720294 0.761654 0.0902955   0.201633    0.103669    98  LYS   A HG3  
3106 H HD2  . LYS   B 86  ? 0.765743 0.854821 0.858104 0.0816823   0.247899    0.148293    98  LYS   A HD2  
3107 H HD3  . LYS   B 86  ? 0.755404 0.868181 0.913863 0.0719114   0.266182    0.138561    98  LYS   A HD3  
3108 H HE2  . LYS   B 86  ? 0.811602 0.951315 0.87848  0.0908413   0.283889    0.126805    98  LYS   A HE2  
3109 H HE3  . LYS   B 86  ? 0.767728 0.913051 0.895304 0.0939887   0.26903     0.096424    98  LYS   A HE3  
3110 H HZ1  . LYS   B 86  ? 0.761273 0.85987  0.791324 0.102191    0.226141    0.110476    98  LYS   A HZ1  
3111 H HZ2  . LYS   B 86  ? 0.737379 0.847118 0.807455 0.106226    0.223093    0.0806868   98  LYS   A HZ2  
3112 H HZ3  . LYS   B 86  ? 0.784033 0.909399 0.801319 0.108697    0.246027    0.0909621   98  LYS   A HZ3  
3113 N N    . LYS   B 87  ? 0.466238 0.506064 0.757943 0.0378614   0.185938    0.115791    99  LYS   A N    
3114 C CA   . LYS   B 87  ? 0.458735 0.474161 0.780187 0.021477    0.184398    0.122008    99  LYS   A CA   
3115 C C    . LYS   B 87  ? 0.491913 0.478406 0.784552 0.0225892   0.201181    0.151552    99  LYS   A C    
3116 O O    . LYS   B 87  ? 0.538907 0.535555 0.814699 0.0246588   0.225402    0.172565    99  LYS   A O    
3117 C CB   . LYS   B 87  ? 0.53499  0.571462 0.92153  0.00188695  0.197519    0.118819    99  LYS   A CB   
3118 C CG   . LYS   B 87  ? 0.593151 0.603791 1.0167   -0.0187129  0.191573    0.116012    99  LYS   A CG   
3119 C CD   . LYS   B 87  ? 0.69251  0.719092 1.1777   -0.042375   0.21226     0.12056     99  LYS   A CD   
3120 C CE   . LYS   B 87  ? 0.720372 0.719774 1.24097  -0.0638378  0.20288     0.110657    99  LYS   A CE   
3121 N NZ   . LYS   B 87  ? 0.746735 0.770322 1.33388  -0.0893879  0.218437    0.108966    99  LYS   A NZ   
3122 H H    . LYS   B 87  ? 0.461649 0.525038 0.773778 0.037223    0.195949    0.111421    99  LYS   A H    
3123 H HA   . LYS   B 87  ? 0.455904 0.459513 0.774715 0.0219342   0.163858    0.109271    99  LYS   A HA   
3124 H HB2  . LYS   B 87  ? 0.507074 0.567542 0.912776 0.00405681  0.187791    0.102781    99  LYS   A HB2  
3125 H HB3  . LYS   B 87  ? 0.547374 0.593386 0.936087 -0.00050136 0.220676    0.133659    99  LYS   A HB3  
3126 H HG2  . LYS   B 87  ? 0.612749 0.593482 1.01308  -0.0163597  0.194709    0.128541    99  LYS   A HG2  
3127 H HG3  . LYS   B 87  ? 0.577041 0.588751 1.0066   -0.0192905  0.169729    0.097395    99  LYS   A HG3  
3128 H HD2  . LYS   B 87  ? 0.661075 0.722019 1.17265  -0.0431069  0.209819    0.108835    99  LYS   A HD2  
3129 H HD3  . LYS   B 87  ? 0.701752 0.724112 1.17887  -0.0436191  0.235444    0.141471    99  LYS   A HD3  
3130 H HE2  . LYS   B 87  ? 0.740595 0.705089 1.24285  -0.0634362  0.209739    0.124094    99  LYS   A HE2  
3131 H HE3  . LYS   B 87  ? 0.696714 0.697597 1.21549  -0.0619141  0.179528    0.0910245   99  LYS   A HE3  
3132 H HZ1  . LYS   B 87  ? 0.763775 0.787628 1.35192  -0.0921583  0.241756    0.128094    99  LYS   A HZ1  
3133 H HZ2  . LYS   B 87  ? 0.72242  0.780526 1.33082  -0.0887502  0.210199    0.095772    99  LYS   A HZ2  
3134 H HZ3  . LYS   B 87  ? 0.7538   0.758767 1.36186  -0.103924   0.21333     0.101712    99  LYS   A HZ3  
3135 N N    . GLY   B 88  ? 0.500136 0.451232 0.789733 0.0210852   0.188944    0.153385    100 GLY   A N    
3136 C CA   . GLY   B 88  ? 0.534452 0.453538 0.798997 0.0270796   0.198939    0.181908    100 GLY   A CA   
3137 C C    . GLY   B 88  ? 0.537501 0.457282 0.744112 0.0489853   0.187423    0.188629    100 GLY   A C    
3138 O O    . GLY   B 88  ? 0.563337 0.460531 0.74916  0.0575511   0.191214    0.213272    100 GLY   A O    
3139 H H    . GLY   B 88  ? 0.481118 0.428198 0.785567 0.0168962   0.173552    0.136035    100 GLY   A H    
3140 H HA2  . GLY   B 88  ? 0.540973 0.435434 0.824375 0.0212036   0.193722    0.178678    100 GLY   A HA2  
3141 H HA3  . GLY   B 88  ? 0.562702 0.483671 0.83245  0.0216032   0.219262    0.201179    100 GLY   A HA3  
3142 N N    . GLU   B 89  ? 0.48498  0.430826 0.667541 0.0580011   0.173305    0.168281    101 GLU   A N    
3143 C CA   . GLU   B 89  ? 0.506223 0.457917 0.635704 0.0752563   0.163026    0.172249    101 GLU   A CA   
3144 C C    . GLU   B 89  ? 0.530004 0.460867 0.653946 0.0816597   0.141801    0.165287    101 GLU   A C    
3145 O O    . GLU   B 89  ? 0.516585 0.43839  0.667681 0.0736122   0.130154    0.144677    101 GLU   A O    
3146 C CB   . GLU   B 89  ? 0.490759 0.470584 0.601692 0.0803446   0.155067    0.149441    101 GLU   A CB   
3147 C CG   . GLU   B 89  ? 0.477973 0.466779 0.535342 0.0942666   0.144381    0.148793    101 GLU   A CG   
3148 C CD   . GLU   B 89  ? 0.474434 0.484747 0.514816 0.0980367   0.140854    0.126228    101 GLU   A CD   
3149 O OE1  . GLU   B 89  ? 0.486847 0.513046 0.543132 0.0953042   0.157138    0.121074    101 GLU   A OE1  
3150 O OE2  . GLU   B 89  ? 0.567611 0.577899 0.584464 0.103149    0.121855    0.111487    101 GLU   A OE2  
3151 H H    . GLU   B 89  ? 0.475333 0.435122 0.676593 0.0529175   0.169279    0.15158     101 GLU   A H    
3152 H HA   . GLU   B 89  ? 0.539023 0.490366 0.648965 0.0793144   0.175341    0.194087    101 GLU   A HA   
3153 H HB2  . GLU   B 89  ? 0.49402  0.488655 0.612959 0.0772062   0.170031    0.151314    101 GLU   A HB2  
3154 H HB3  . GLU   B 89  ? 0.46035  0.43899  0.589427 0.0766576   0.142051    0.13124     101 GLU   A HB3  
3155 H HG2  . GLU   B 89  ? 0.472277 0.450816 0.525816 0.0969561   0.129215    0.144247    101 GLU   A HG2  
3156 H HG3  . GLU   B 89  ? 0.511457 0.501779 0.547815 0.0982908   0.154518    0.168369    101 GLU   A HG3  
3157 N N    . ILE   B 90  ? 0.55862  0.485603 0.64832  0.0961031   0.136966    0.182226    102 ILE   A N    
3158 C CA   . ILE   B 90  ? 0.532484 0.452162 0.616261 0.104295    0.116674    0.170544    102 ILE   A CA   
3159 C C    . ILE   B 90  ? 0.525697 0.471773 0.566058 0.114432    0.104037    0.164837    102 ILE   A C    
3160 O O    . ILE   B 90  ? 0.543267 0.503099 0.551642 0.122016    0.11031     0.183502    102 ILE   A O    
3161 C CB   . ILE   B 90  ? 0.553503 0.445924 0.648958 0.113521    0.118413    0.191276    102 ILE   A CB   
3162 C CG1  . ILE   B 90  ? 0.603962 0.464548 0.741304 0.101789    0.134374    0.199664    102 ILE   A CG1  
3163 C CG2  . ILE   B 90  ? 0.505632 0.39585  0.604568 0.120927    0.100171    0.172402    102 ILE   A CG2  
3164 C CD1  . ILE   B 90  ? 0.628993 0.453666 0.784218 0.111575    0.137889    0.219114    102 ILE   A CD1  
3165 H H    . ILE   B 90  ? 0.577889 0.509515 0.648575 0.100717    0.146369    0.201202    102 ILE   A H    
3166 H HA   . ILE   B 90  ? 0.510148 0.426903 0.612053 0.0967674   0.109618    0.15058     102 ILE   A HA   
3167 H HB   . ILE   B 90  ? 0.577662 0.475467 0.650814 0.122951    0.121522    0.212583    102 ILE   A HB   
3168 H HG12 . ILE   B 90  ? 0.573288 0.432097 0.731355 0.0911972   0.130299    0.177503    102 ILE   A HG12 
3169 H HG13 . ILE   B 90  ? 0.609703 0.474485 0.745422 0.0964604   0.147732    0.21344     102 ILE   A HG13 
3170 H HG21 . ILE   B 90  ? 0.534598 0.409689 0.641966 0.129908    0.101743    0.185792    102 ILE   A HG21 
3171 H HG22 . ILE   B 90  ? 0.495934 0.379937 0.613722 0.111123    0.0973677   0.152371    102 ILE   A HG22 
3172 H HG23 . ILE   B 90  ? 0.500675 0.411875 0.575254 0.126087    0.090191    0.166674    102 ILE   A HG23 
3173 H HD11 . ILE   B 90  ? 0.654298 0.482274 0.787906 0.1239      0.138848    0.242733    102 ILE   A HD11 
3174 H HD12 . ILE   B 90  ? 0.651076 0.453852 0.832482 0.101513    0.150023    0.224891    102 ILE   A HD12 
3175 H HD13 . ILE   B 90  ? 0.617677 0.437895 0.780946 0.115604    0.127297    0.202191    102 ILE   A HD13 
3176 N N    . ALA   B 91  ? 0.436176 0.388845 0.474272 0.112701    0.0864274   0.139307    103 ALA   A N    
3177 C CA   . ALA   B 91  ? 0.442707 0.417661 0.446052 0.117453    0.0728172   0.12769     103 ALA   A CA   
3178 C C    . ALA   B 91  ? 0.424572 0.401383 0.428503 0.119849    0.0555198   0.115096    103 ALA   A C    
3179 O O    . ALA   B 91  ? 0.448203 0.409671 0.478764 0.115803    0.0534102   0.106733    103 ALA   A O    
3180 C CB   . ALA   B 91  ? 0.415336 0.398696 0.416016 0.109254    0.0725391   0.107652    103 ALA   A CB   
3181 H H    . ALA   B 91  ? 0.440244 0.382348 0.499622 0.106746    0.0828912   0.128095    103 ALA   A H    
3182 H HA   . ALA   B 91  ? 0.457916 0.442769 0.438976 0.124689    0.0760636   0.142174    103 ALA   A HA   
3183 H HB1  . ALA   B 91  ? 0.431211 0.417907 0.432589 0.108885    0.0852287   0.114928    103 ALA   A HB1  
3184 H HB2  . ALA   B 91  ? 0.401475 0.376505 0.422931 0.102419    0.0681436   0.0960715   103 ALA   A HB2  
3185 H HB3  . ALA   B 91  ? 0.415541 0.40975  0.394039 0.111141    0.0641622   0.0988064   103 ALA   A HB3  
3186 N N    . HIS   B 92  ? 0.384265 0.382947 0.358667 0.126592    0.0449099   0.114956    104 HIS   A N    
3187 C CA   . HIS   B 92  ? 0.378863 0.38901  0.352415 0.12663     0.0296602   0.101065    104 HIS   A CA   
3188 C C    . HIS   B 92  ? 0.400285 0.419971 0.355546 0.115089    0.0201239   0.0778347   104 HIS   A C    
3189 O O    . HIS   B 92  ? 0.43678  0.46618  0.367046 0.114732    0.0208088   0.0758256   104 HIS   A O    
3190 C CB   . HIS   B 92  ? 0.383682 0.416363 0.34271  0.140868    0.0219298   0.116797    104 HIS   A CB   
3191 C CG   . HIS   B 92  ? 0.414579 0.435053 0.398383 0.154724    0.0267019   0.137817    104 HIS   A CG   
3192 N ND1  . HIS   B 92  ? 0.408775 0.447909 0.386692 0.171624    0.0188698   0.157844    104 HIS   A ND1  
3193 C CD2  . HIS   B 92  ? 0.405944 0.395764 0.422862 0.154094    0.0376034   0.140404    104 HIS   A CD2  
3194 C CE1  . HIS   B 92  ? 0.432349 0.448157 0.439931 0.183665    0.0263315   0.175948    104 HIS   A CE1  
3195 N NE2  . HIS   B 92  ? 0.422801 0.407054 0.455266 0.171638    0.0383262   0.162198    104 HIS   A NE2  
3196 H H    . HIS   B 92  ? 0.412439 0.421424 0.366474 0.130244    0.0478687   0.123311    104 HIS   A H    
3197 H HA   . HIS   B 92  ? 0.371857 0.370087 0.367219 0.124334    0.0301403   0.0958367   104 HIS   A HA   
3198 H HB2  . HIS   B 92  ? 0.40636  0.448889 0.34239  0.143335    0.023405    0.125115    104 HIS   A HB2  
3199 H HB3  . HIS   B 92  ? 0.379057 0.426793 0.334507 0.138417    0.0114559   0.104323    104 HIS   A HB3  
3201 H HD2  . HIS   B 92  ? 0.3942   0.369338 0.422773 0.143786    0.0427348   0.12896     104 HIS   A HD2  
3202 H HE1  . HIS   B 92  ? 0.452374 0.473621 0.465422 0.198106    0.0222258   0.192938    104 HIS   A HE1  
3204 N N    . LEU   B 93  ? 0.3623   0.377321 0.328673 0.105342    0.0123496   0.0604588   105 LEU   A N    
3205 C CA   . LEU   B 93  ? 0.358373 0.376392 0.309586 0.0933141   0.00262248  0.0417381   105 LEU   A CA   
3206 C C    . LEU   B 93  ? 0.355729 0.391703 0.304073 0.0891778   -0.00778662 0.0333391   105 LEU   A C    
3207 O O    . LEU   B 93  ? 0.328932 0.365548 0.296007 0.0897328   -0.00679902 0.0322091   105 LEU   A O    
3208 C CB   . LEU   B 93  ? 0.342738 0.340399 0.306294 0.0819508   0.00164014  0.0306668   105 LEU   A CB   
3209 C CG   . LEU   B 93  ? 0.334827 0.319656 0.311046 0.0833685   0.0103558   0.034607    105 LEU   A CG   
3210 C CD1  . LEU   B 93  ? 0.358719 0.330147 0.347658 0.0733551   0.00371734  0.0242404   105 LEU   A CD1  
3211 C CD2  . LEU   B 93  ? 0.370369 0.361762 0.32789  0.0885085   0.0150824   0.0344107   105 LEU   A CD2  
3212 H H    . LEU   B 93  ? 0.362951 0.371178 0.346525 0.105711    0.0137646   0.0605636   105 LEU   A H    
3213 H HA   . LEU   B 93  ? 0.366963 0.390519 0.301271 0.0946848   0.00279185  0.0413947   105 LEU   A HA   
3214 H HB2  . LEU   B 93  ? 0.334744 0.328753 0.310921 0.0791918   0.0010838   0.0287958   105 LEU   A HB2  
3215 H HB3  . LEU   B 93  ? 0.339532 0.337446 0.291595 0.0748386   -0.00556688 0.0211336   105 LEU   A HB3  
3216 H HG   . LEU   B 93  ? 0.34978  0.332007 0.339551 0.0877402   0.0182183   0.0442223   105 LEU   A HG   
3217 H HD11 . LEU   B 93  ? 0.342729 0.311022 0.338943 0.0682992   0.00038136  0.0216169   105 LEU   A HD11 
3218 H HD12 . LEU   B 93  ? 0.349286 0.31746  0.352197 0.075255    0.00944197  0.0272266   105 LEU   A HD12 
3219 H HD13 . LEU   B 93  ? 0.349593 0.319556 0.325963 0.0698667   -0.00311627 0.0172828   105 LEU   A HD13 
3220 H HD21 . LEU   B 93  ? 0.374605 0.376111 0.321623 0.095011    0.019526    0.0432367   105 LEU   A HD21 
3221 H HD22 . LEU   B 93  ? 0.364541 0.356007 0.309104 0.0842424   0.00753576  0.0241614   105 LEU   A HD22 
3222 H HD23 . LEU   B 93  ? 0.364776 0.350807 0.334211 0.089259    0.0215407   0.0351454   105 LEU   A HD23 
3223 N N    . LEU   B 94  ? 0.354384 0.403247 0.281389 0.0821757   -0.0164362  0.023438    106 LEU   A N    
3224 C CA   . LEU   B 94  ? 0.319675 0.386971 0.245239 0.0720865   -0.0259155  0.0122616   106 LEU   A CA   
3225 C C    . LEU   B 94  ? 0.350083 0.400297 0.263084 0.0541775   -0.0309703  -0.0025449  106 LEU   A C    
3226 O O    . LEU   B 94  ? 0.336385 0.376195 0.233343 0.052425    -0.0321362  -0.00775801 106 LEU   A O    
3227 C CB   . LEU   B 94  ? 0.327027 0.429568 0.243202 0.0782123   -0.0338489  0.0150251   106 LEU   A CB   
3228 C CG   . LEU   B 94  ? 0.374881 0.505255 0.297674 0.066278    -0.0430869  0.00275792  106 LEU   A CG   
3229 C CD1  . LEU   B 94  ? 0.371206 0.513055 0.324262 0.0725208   -0.0383628  0.00592058  106 LEU   A CD1  
3230 C CD2  . LEU   B 94  ? 0.39663  0.565785 0.308143 0.0692444   -0.0549858  0.00235338  106 LEU   A CD2  
3231 H H    . LEU   B 94  ? 0.357515 0.40387  0.271226 0.082791    -0.0154422  0.0225678   106 LEU   A H    
3232 H HA   . LEU   B 94  ? 0.321711 0.389662 0.263079 0.0721391   -0.0237656  0.0124858   106 LEU   A HA   
3233 H HB2  . LEU   B 94  ? 0.342336 0.452281 0.267236 0.091491    -0.0311462  0.0279369   106 LEU   A HB2  
3234 H HB3  . LEU   B 94  ? 0.350988 0.453242 0.248374 0.077141    -0.0356606  0.0125508   106 LEU   A HB3  
3235 H HG   . LEU   B 94  ? 0.36528  0.483049 0.281363 0.0516088   -0.0443103  -0.0080673  106 LEU   A HG   
3236 H HD11 . LEU   B 94  ? 0.360647 0.480819 0.318039 0.0676794   -0.0322047  0.00305092  106 LEU   A HD11 
3237 H HD12 . LEU   B 94  ? 0.366762 0.531772 0.326321 0.0654906   -0.0427904  -0.00167826 106 LEU   A HD12 
3238 H HD13 . LEU   B 94  ? 0.37273  0.520916 0.334859 0.0881891   -0.036743   0.0178446   106 LEU   A HD13 
3239 H HD21 . LEU   B 94  ? 0.406827 0.568923 0.297508 0.0642602   -0.0571559  -0.00325246 106 LEU   A HD21 
3240 H HD22 . LEU   B 94  ? 0.400106 0.581517 0.316721 0.084617    -0.0551154  0.0158267   106 LEU   A HD22 
3241 H HD23 . LEU   B 94  ? 0.391665 0.581269 0.312192 0.0603603   -0.0603797  -0.00603199 106 LEU   A HD23 
3242 N N    . ILE   B 95  ? 0.315299 0.362172 0.234797 0.040887    -0.0332417  -0.00927048 107 ILE   A N    
3243 C CA   . ILE   B 95  ? 0.345833 0.36743  0.25612  0.0248539   -0.0372633  -0.0162388  107 ILE   A CA   
3244 C C    . ILE   B 95  ? 0.345108 0.376743 0.248468 0.00532611  -0.0425093  -0.024806   107 ILE   A C    
3245 O O    . ILE   B 95  ? 0.349258 0.397449 0.261319 -0.00064925 -0.0395606  -0.0261321  107 ILE   A O    
3246 C CB   . ILE   B 95  ? 0.314914 0.317065 0.235592 0.0244246   -0.0341949  -0.0121344  107 ILE   A CB   
3247 C CG1  . ILE   B 95  ? 0.341997 0.336103 0.275734 0.0399919   -0.0276376  -0.00410146 107 ILE   A CG1  
3248 C CG2  . ILE   B 95  ? 0.345766 0.323048 0.255135 0.0102067   -0.041501   -0.0143351  107 ILE   A CG2  
3249 C CD1  . ILE   B 95  ? 0.313634 0.298326 0.263896 0.0396043   -0.0242993  -0.00245291 107 ILE   A CD1  
3250 H H    . ILE   B 95  ? 0.321593 0.383038 0.25146  0.0421175   -0.031961   -0.00868115 107 ILE   A H    
3251 H HA   . ILE   B 95  ? 0.343885 0.353302 0.245941 0.0263908   -0.0386144  -0.0178104  107 ILE   A HA   
3252 H HB   . ILE   B 95  ? 0.323768 0.337129 0.250991 0.0222276   -0.0317184  -0.0133983  107 ILE   A HB   
3253 H HG12 . ILE   B 95  ? 0.334346 0.316816 0.263893 0.0413754   -0.028852   -0.00414654 107 ILE   A HG12 
3254 H HG13 . ILE   B 95  ? 0.328347 0.335711 0.264862 0.0492187   -0.0237846  5.766e-05   107 ILE   A HG13 
3255 H HG21 . ILE   B 95  ? 0.337366 0.30397  0.252776 0.0120328   -0.0417247  -0.0111204  107 ILE   A HG21 
3256 H HG22 . ILE   B 95  ? 0.348643 0.315852 0.251811 0.0110408   -0.0441574  -0.0158892  107 ILE   A HG22 
3257 H HG23 . ILE   B 95  ? 0.344561 0.326715 0.24728  -0.0018538  -0.0434004  -0.0172054  107 ILE   A HG23 
3258 H HD11 . ILE   B 95  ? 0.31692  0.311733 0.272178 0.0391476   -0.0215178  -0.00458916 107 ILE   A HD11 
3259 H HD12 . ILE   B 95  ? 0.317983 0.298347 0.278956 0.0480485   -0.0193736  0.00288431  107 ILE   A HD12 
3260 H HD13 . ILE   B 95  ? 0.322693 0.29631  0.268439 0.0309172   -0.0297689  -0.00510163 107 ILE   A HD13 
3261 N N    . LYS   B 96  ? 0.406398 0.425005 0.295026 -0.00616771 -0.0485831  -0.0319552  108 LYS   A N    
3262 C CA   . LYS   B 96  ? 0.403358 0.422329 0.28537  -0.0293379  -0.0526282  -0.0385778  108 LYS   A CA   
3263 C C    . LYS   B 96  ? 0.422479 0.414904 0.298965 -0.0421965  -0.0524874  -0.0321995  108 LYS   A C    
3264 O O    . LYS   B 96  ? 0.382466 0.351405 0.258877 -0.0336642  -0.0532556  -0.0251721  108 LYS   A O    
3265 C CB   . LYS   B 96  ? 0.436842 0.440373 0.30578  -0.0382966  -0.0587091  -0.0491098  108 LYS   A CB   
3266 C CG   . LYS   B 96  ? 0.461486 0.494916 0.327639 -0.0311239  -0.0615353  -0.0580544  108 LYS   A CG   
3267 C CD   . LYS   B 96  ? 0.542778 0.563399 0.394115 -0.0444176  -0.0676385  -0.0755042  108 LYS   A CD   
3268 C CE   . LYS   B 96  ? 0.58673  0.64405  0.42944  -0.0409775  -0.0733609  -0.0873111  108 LYS   A CE   
3269 N NZ   . LYS   B 96  ? 0.659651 0.688336 0.486924 -0.0550548  -0.0767833  -0.107696   108 LYS   A NZ   
3270 H H    . LYS   B 96  ? 0.398045 0.406149 0.281277 0.00015501  -0.0491144  -0.0331978  108 LYS   A H    
3271 H HA   . LYS   B 96  ? 0.403706 0.451809 0.293444 -0.0320398  -0.0514176  -0.0408963  108 LYS   A HA   
3272 H HB2  . LYS   B 96  ? 0.446447 0.422229 0.311132 -0.0327436  -0.0588978  -0.0475813  108 LYS   A HB2  
3273 H HB3  . LYS   B 96  ? 0.452429 0.451386 0.318234 -0.0559652  -0.0608464  -0.0523257  108 LYS   A HB3  
3274 H HG2  . LYS   B 96  ? 0.457606 0.522166 0.332378 -0.0334351  -0.0623554  -0.0578534  108 LYS   A HG2  
3275 H HG3  . LYS   B 96  ? 0.458933 0.493304 0.325012 -0.0144735  -0.0585043  -0.0530565  108 LYS   A HG3  
3276 H HD2  . LYS   B 96  ? 0.547926 0.537978 0.393451 -0.0391714  -0.0657211  -0.0765281  108 LYS   A HD2  
3277 H HD3  . LYS   B 96  ? 0.548739 0.563439 0.401504 -0.0626612  -0.0698749  -0.0790898  108 LYS   A HD3  
3278 H HE2  . LYS   B 96  ? 0.581327 0.670242 0.432409 -0.0480524  -0.0774841  -0.0882487  108 LYS   A HE2  
3279 H HE3  . LYS   B 96  ? 0.579349 0.644664 0.418203 -0.0236876  -0.0706366  -0.0814465  108 LYS   A HE3  
3280 H HZ1  . LYS   B 96  ? 0.656047 0.674798 0.48759  -0.0722213  -0.0789982  -0.111595   108 LYS   A HZ1  
3281 H HZ2  . LYS   B 96  ? 0.651201 0.651362 0.47401  -0.047009   -0.0723549  -0.107318   108 LYS   A HZ2  
3282 H HZ3  . LYS   B 96  ? 0.658586 0.708257 0.477113 -0.0549461  -0.0809519  -0.117417   108 LYS   A HZ3  
3283 N N    . PRO   B 97  ? 0.403154 0.404537 0.274997 -0.0641007  -0.0514576  -0.0337799  109 PRO   A N    
3284 C CA   . PRO   B 97  ? 0.460689 0.447334 0.321951 -0.0770779  -0.0498876  -0.0258614  109 PRO   A CA   
3285 C C    . PRO   B 97  ? 0.478265 0.417821 0.3256   -0.0789004  -0.0587282  -0.0159424  109 PRO   A C    
3286 O O    . PRO   B 97  ? 0.466092 0.391864 0.306583 -0.0777184  -0.0615891  -0.00667918 109 PRO   A O    
3287 C CB   . PRO   B 97  ? 0.448933 0.457339 0.306903 -0.102027   -0.0448033  -0.0296378  109 PRO   A CB   
3288 C CG   . PRO   B 97  ? 0.452102 0.495525 0.326577 -0.101496   -0.0447228  -0.041448   109 PRO   A CG   
3289 C CD   . PRO   B 97  ? 0.446877 0.484157 0.325854 -0.077233   -0.0501407  -0.0430736  109 PRO   A CD   
3290 H HA   . PRO   B 97  ? 0.430631 0.428178 0.298275 -0.0676763  -0.0458109  -0.0250488  109 PRO   A HA   
3291 H HB2  . PRO   B 97  ? 0.481167 0.465663 0.32559  -0.117297   -0.0480337  -0.0244868  109 PRO   A HB2  
3292 H HB3  . PRO   B 97  ? 0.452093 0.477326 0.311351 -0.104186   -0.0381834  -0.0296565  109 PRO   A HB3  
3293 H HG2  . PRO   B 97  ? 0.469683 0.507033 0.339245 -0.118528   -0.0471176  -0.0441733  109 PRO   A HG2  
3294 H HG3  . PRO   B 97  ? 0.438344 0.515109 0.325629 -0.100183   -0.0387147  -0.0452083  109 PRO   A HG3  
3295 H HD2  . PRO   B 97  ? 0.447437 0.47766  0.322034 -0.0824099  -0.0550532  -0.0485391  109 PRO   A HD2  
3296 H HD3  . PRO   B 97  ? 0.418152 0.484104 0.310072 -0.0652443  -0.0477185  -0.0451196  109 PRO   A HD3  
3297 N N    . GLU   B 98  ? 0.483599 0.399044 0.329113 -0.0791387  -0.0641262  -0.0191284  110 GLU   A N    
3298 C CA   . GLU   B 98  ? 0.517125 0.386035 0.355945 -0.0775288  -0.0727024  -0.00997907 110 GLU   A CA   
3299 C C    . GLU   B 98  ? 0.466587 0.328942 0.316621 -0.0542899  -0.0754527  -0.00449066 110 GLU   A C    
3300 O O    . GLU   B 98  ? 0.486759 0.320285 0.333914 -0.0532913  -0.0844018  0.0073888   110 GLU   A O    
3301 C CB   . GLU   B 98  ? 0.551437 0.392881 0.390474 -0.079581   -0.075728   -0.0196609  110 GLU   A CB   
3302 C CG   . GLU   B 98  ? 0.689393 0.536194 0.52067  -0.107272   -0.0740141  -0.0257636  110 GLU   A CG   
3303 C CD   . GLU   B 98  ? 0.66472  0.564039 0.503307 -0.114387   -0.0681195  -0.0395836  110 GLU   A CD   
3304 O OE1  . GLU   B 98  ? 0.500668 0.433107 0.3488   -0.0955246  -0.0658612  -0.0469949  110 GLU   A OE1  
3305 O OE2  . GLU   B 98  ? 0.737258 0.644549 0.573053 -0.140904   -0.0660541  -0.040575   110 GLU   A OE2  
3306 H H    . GLU   B 98  ? 0.486802 0.415049 0.336366 -0.0793839  -0.0628678  -0.0278972  110 GLU   A H    
3307 H HA   . GLU   B 98  ? 0.529295 0.386673 0.356679 -0.0915713  -0.0751329  -0.00067252 110 GLU   A HA   
3308 H HB2  . GLU   B 98  ? 0.55842  0.41222  0.404658 -0.0664027  -0.0730408  -0.0291644  110 GLU   A HB2  
3309 H HB3  . GLU   B 98  ? 0.591871 0.400796 0.430001 -0.076398   -0.081133   -0.0129286  110 GLU   A HB3  
3310 H HG2  . GLU   B 98  ? 0.682605 0.502345 0.512679 -0.111264   -0.0769872  -0.0311691  110 GLU   A HG2  
3311 H HG3  . GLU   B 98  ? 0.670171 0.508759 0.492822 -0.120667   -0.0745383  -0.0144709  110 GLU   A HG3  
3312 N N    . TYR   B 99  ? 0.444397 0.334635 0.308265 -0.0375189  -0.0685852  -0.0103639  111 TYR   A N    
3313 C CA   . TYR   B 99  ? 0.394966 0.282565 0.273941 -0.0188491  -0.0690133  -0.00591278 111 TYR   A CA   
3314 C C    . TYR   B 99  ? 0.379465 0.287602 0.262291 -0.019709   -0.0662406  -0.00267316 111 TYR   A C    
3315 O O    . TYR   B 99  ? 0.419885 0.333437 0.318995 -0.00703001 -0.0642804  -0.00147504 111 TYR   A O    
3316 C CB   . TYR   B 99  ? 0.411596 0.307746 0.302657 -0.00084247 -0.0617795  -0.0133472  111 TYR   A CB   
3317 C CG   . TYR   B 99  ? 0.426317 0.297562 0.313247 0.00068968  -0.0640537  -0.0209339  111 TYR   A CG   
3318 C CD1  . TYR   B 99  ? 0.448601 0.31987  0.321704 -0.0110637  -0.0638623  -0.0323024  111 TYR   A CD1  
3319 C CD2  . TYR   B 99  ? 0.457124 0.308097 0.35849  0.0152737   -0.065119   -0.020043   111 TYR   A CD2  
3320 C CE1  . TYR   B 99  ? 0.455105 0.300818 0.325135 -0.00952645 -0.0644834  -0.044237   111 TYR   A CE1  
3321 C CE2  . TYR   B 99  ? 0.460005 0.28493  0.360938 0.0188661   -0.0653165  -0.030216   111 TYR   A CE2  
3322 C CZ   . TYR   B 99  ? 0.477887 0.297916 0.361439 0.0062957   -0.0643643  -0.0436025  111 TYR   A CZ   
3323 O OH   . TYR   B 99  ? 0.572561 0.362442 0.457786 0.0108389   -0.063361   -0.0573447  111 TYR   A OH   
3324 H H    . TYR   B 99  ? 0.423631 0.3355   0.289026 -0.038188   -0.0635925  -0.0165906  111 TYR   A H    
3325 H HA   . TYR   B 99  ? 0.422859 0.287926 0.301778 -0.018458   -0.0762287  1.9e-07     111 TYR   A HA   
3326 H HB2  . TYR   B 99  ? 0.391811 0.309029 0.281228 -0.00079253 -0.0566109  -0.0173239  111 TYR   A HB2  
3327 H HB3  . TYR   B 99  ? 0.392464 0.290165 0.29611  0.00968687  -0.0601869  -0.00977607 111 TYR   A HB3  
3328 H HD1  . TYR   B 99  ? 0.435269 0.325742 0.303037 -0.0200541  -0.0629712  -0.0336933  111 TYR   A HD1  
3329 H HD2  . TYR   B 99  ? 0.43552  0.289156 0.349056 0.0218249   -0.0665038  -0.0129969  111 TYR   A HD2  
3330 H HE1  . TYR   B 99  ? 0.477566 0.322624 0.338507 -0.0199813  -0.0652341  -0.0536161  111 TYR   A HE1  
3331 H HE2  . TYR   B 99  ? 0.472973 0.28568  0.38761  0.0303286   -0.0653121  -0.030161   111 TYR   A HE2  
3333 N N    . ALA   B 100 ? 0.391166 0.312332 0.260924 -0.0357069  -0.0639202  -0.00388641 112 ALA   A N    
3334 C CA   . ALA   B 100 ? 0.396828 0.337836 0.26924  -0.0371141  -0.0585385  -0.00654513 112 ALA   A CA   
3335 C C    . ALA   B 100 ? 0.397126 0.332376 0.244827 -0.0579326  -0.0632047  -0.00150981 112 ALA   A C    
3336 O O    . ALA   B 100 ? 0.443835 0.358489 0.281874 -0.0603188  -0.0752582  0.00861732  112 ALA   A O    
3337 C CB   . ALA   B 100 ? 0.368318 0.340087 0.252016 -0.0328032  -0.046609   -0.015772   112 ALA   A CB   
3338 H H    . ALA   B 100 ? 0.406065 0.324279 0.265849 -0.0468489  -0.064574   -0.00442421 112 ALA   A H    
3339 H HA   . ALA   B 100 ? 0.379536 0.31669  0.262706 -0.0274114  -0.0601328  -0.00520812 112 ALA   A HA   
3340 H HB1  . ALA   B 100 ? 0.35888  0.333673 0.255673 -0.0189626  -0.044259   -0.0160136  112 ALA   A HB1  
3341 H HB2  . ALA   B 100 ? 0.377468 0.356571 0.255348 -0.041159   -0.0457602  -0.0177903  112 ALA   A HB2  
3342 H HB3  . ALA   B 100 ? 0.369777 0.35208  0.25469  -0.0353445  -0.0420205  -0.0195479  112 ALA   A HB3  
3343 N N    . TYR   B 101 ? 0.412512 0.368764 0.249668 -0.0730824  -0.0540675  -0.00720004 113 TYR   A N    
3344 C CA   . TYR   B 101 ? 0.441779 0.396163 0.25056  -0.0947195  -0.0550995  -0.00180266 113 TYR   A CA   
3345 C C    . TYR   B 101 ? 0.50826  0.454276 0.299205 -0.116443   -0.0546283  0.00593354  113 TYR   A C    
3346 O O    . TYR   B 101 ? 0.497563 0.442114 0.260935 -0.137751   -0.0532873  0.0137844   113 TYR   A O    
3347 C CB   . TYR   B 101 ? 0.466879 0.452899 0.274733 -0.0989751  -0.0414358  -0.0158956  113 TYR   A CB   
3348 C CG   . TYR   B 101 ? 0.480202 0.466047 0.303264 -0.0825988  -0.0429566  -0.0234209  113 TYR   A CG   
3349 C CD1  . TYR   B 101 ? 0.453622 0.426058 0.260321 -0.0871538  -0.0548814  -0.0188137  113 TYR   A CD1  
3350 C CD2  . TYR   B 101 ? 0.404677 0.401417 0.26068  -0.0623339  -0.0349373  -0.0324733  113 TYR   A CD2  
3351 C CE1  . TYR   B 101 ? 0.422833 0.396463 0.247645 -0.0756414  -0.0564216  -0.0278666  113 TYR   A CE1  
3352 C CE2  . TYR   B 101 ? 0.395362 0.387447 0.268187 -0.050126   -0.0350137  -0.0381318  113 TYR   A CE2  
3353 C CZ   . TYR   B 101 ? 0.443918 0.425654 0.302497 -0.0583234  -0.0449108  -0.0382925  113 TYR   A CZ   
3354 O OH   . TYR   B 101 ? 0.358429 0.335931 0.237371 -0.0494895  -0.0461852  -0.045244   113 TYR   A OH   
3355 H H    . TYR   B 101 ? 0.397657 0.371796 0.245605 -0.069929   -0.0467834  -0.0141123  113 TYR   A H    
3356 H HA   . TYR   B 101 ? 0.466511 0.403244 0.266702 -0.0936755  -0.0653117  0.00647019  113 TYR   A HA   
3357 H HB2  . TYR   B 101 ? 0.453193 0.45939  0.274926 -0.0969214  -0.0317456  -0.023986   113 TYR   A HB2  
3358 H HB3  . TYR   B 101 ? 0.490342 0.477046 0.274746 -0.115109   -0.0408585  -0.012597   113 TYR   A HB3  
3359 H HD1  . TYR   B 101 ? 0.482358 0.446892 0.264812 -0.0999251  -0.0618116  -0.00971377 113 TYR   A HD1  
3360 H HD2  . TYR   B 101 ? 0.403433 0.411629 0.270226 -0.0580982  -0.0293955  -0.0342943  113 TYR   A HD2  
3361 H HE1  . TYR   B 101 ? 0.452532 0.421449 0.266838 -0.0804126  -0.0657443  -0.0262653  113 TYR   A HE1  
3362 H HE2  . TYR   B 101 ? 0.386377 0.383506 0.280368 -0.0374233  -0.0286083  -0.0419929  113 TYR   A HE2  
3364 N N    . GLY   B 102 ? 0.476633 0.416032 0.280414 -0.114436   -0.0553558  0.00396472  114 GLY   A N    
3365 C CA   . GLY   B 102 ? 0.508077 0.425226 0.296241 -0.13619    -0.0583634  0.0130192   114 GLY   A CA   
3366 C C    . GLY   B 102 ? 0.526008 0.472689 0.309491 -0.160893   -0.0452058  0.00780566  114 GLY   A C    
3367 O O    . GLY   B 102 ? 0.534231 0.523198 0.328841 -0.159138   -0.0329245  -0.00454611 114 GLY   A O    
3368 H H    . GLY   B 102 ? 0.460172 0.408223 0.281332 -0.100653   -0.0538748  -0.00318469 114 GLY   A H    
3369 H HA2  . GLY   B 102 ? 0.507959 0.411864 0.306336 -0.129832   -0.0622682  0.0102667   114 GLY   A HA2  
3370 H HA3  . GLY   B 102 ? 0.534998 0.427802 0.306183 -0.141533   -0.0658636  0.026174    114 GLY   A HA3  
3371 N N    . SER   B 103 ? 0.586984 0.508046 0.352032 -0.18565    -0.0471396  0.0202232   115 SER   A N    
3372 C CA   . SER   B 103 ? 0.62443  0.572094 0.383008 -0.21496    -0.0331019  0.018756    115 SER   A CA   
3373 C C    . SER   B 103 ? 0.636089 0.603977 0.370216 -0.225443   -0.0233012  0.0237798   115 SER   A C    
3374 O O    . SER   B 103 ? 0.618273 0.62822  0.356263 -0.241114   -0.00593005 0.0141266   115 SER   A O    
3375 C CB   . SER   B 103 ? 0.676231 0.590614 0.425267 -0.241564   -0.0354536  0.0299508   115 SER   A CB   
3376 O OG   . SER   B 103 ? 0.767417 0.631083 0.485496 -0.250215   -0.045174   0.0555717   115 SER   A OG   
3377 H H    . SER   B 103 ? 0.604429 0.490581 0.362684 -0.18447    -0.056624   0.0301175   115 SER   A H    
3378 H HA   . SER   B 103 ? 0.595483 0.576758 0.376075 -0.210395   -0.0264847  0.00386371  115 SER   A HA   
3379 H HB2  . SER   B 103 ? 0.693841 0.633611 0.444484 -0.261319   -0.0242117  0.0264554   115 SER   A HB2  
3380 H HB3  . SER   B 103 ? 0.676428 0.580057 0.441344 -0.234336   -0.0410517  0.0222411   115 SER   A HB3  
3382 N N    . ALA   B 104 ? 0.671019 0.613763 0.38113  -0.216784   -0.0341352  0.0366669   116 ALA   A N    
3383 C CA   . ALA   B 104 ? 0.666496 0.628043 0.345572 -0.230262   -0.0257969  0.039833    116 ALA   A CA   
3384 C C    . ALA   B 104 ? 0.620647 0.6275   0.320262 -0.213544   -0.0130859  0.0139642   116 ALA   A C    
3385 O O    . ALA   B 104 ? 0.606973 0.646104 0.291273 -0.226396   0.00326786  0.00452884  116 ALA   A O    
3386 C CB   . ALA   B 104 ? 0.740321 0.663227 0.38722  -0.22728    -0.0453663  0.0620865   116 ALA   A CB   
3387 H H    . ALA   B 104 ? 0.655469 0.572027 0.368713 -0.203095   -0.0465988  0.0423989   116 ALA   A H    
3388 H HA   . ALA   B 104 ? 0.703015 0.673659 0.369377 -0.253098   -0.0153834  0.0442607   116 ALA   A HA   
3389 H HB1  . ALA   B 104 ? 0.755991 0.647903 0.39269  -0.236407   -0.0529858  0.0794667   116 ALA   A HB1  
3390 H HB2  . ALA   B 104 ? 0.702764 0.619299 0.365611 -0.206161   -0.0548687  0.0572739   116 ALA   A HB2  
3391 H HB3  . ALA   B 104 ? 0.747759 0.684222 0.369093 -0.237486   -0.0410003  0.0638013   116 ALA   A HB3  
3392 N N    . GLY   B 105 ? 0.575235 0.579558 0.306189 -0.184845   -0.020524   0.00389002  117 GLY   A N    
3393 C CA   . GLY   B 105 ? 0.568087 0.602428 0.320462 -0.166019   -0.0112713  -0.0168102  117 GLY   A CA   
3394 C C    . GLY   B 105 ? 0.565028 0.592008 0.291346 -0.165926   -0.0159651  -0.0171962  117 GLY   A C    
3395 O O    . GLY   B 105 ? 0.568213 0.565434 0.26849  -0.171357   -0.0324256  0.0007894   117 GLY   A O    
3396 H H    . GLY   B 105 ? 0.575565 0.557505 0.314922 -0.176865   -0.0307891  0.0101463   117 GLY   A H    
3397 H HA2  . GLY   B 105 ? 0.530553 0.560584 0.306741 -0.147499   -0.0162288  -0.0202589  117 GLY   A HA2  
3398 H HA3  . GLY   B 105 ? 0.553877 0.618587 0.315312 -0.171964   0.0031542   -0.0278597  117 GLY   A HA3  
3399 N N    . SER   B 106 ? 0.504222 0.559038 0.240344 -0.159097   -0.00230039 -0.0389247  118 SER   A N    
3400 C CA   . SER   B 106 ? 0.500063 0.553028 0.215447 -0.159527   -0.00529221 -0.0473582  118 SER   A CA   
3401 C C    . SER   B 106 ? 0.48881  0.579103 0.2056   -0.164959   0.0192619   -0.0735358  118 SER   A C    
3402 O O    . SER   B 106 ? 0.513018 0.61172  0.25485  -0.148482   0.0265719   -0.0947077  118 SER   A O    
3403 C CB   . SER   B 106 ? 0.447563 0.483182 0.189118 -0.136075   -0.01772    -0.0508718  118 SER   A CB   
3404 O OG   . SER   B 106 ? 0.508886 0.542881 0.230489 -0.14035    -0.0237147  -0.0597328  118 SER   A OG   
3405 H H    . SER   B 106 ? 0.493465 0.570092 0.252251 -0.153625   0.00936784  -0.0503947  118 SER   A H    
3406 H HA   . SER   B 106 ? 0.526169 0.566772 0.208406 -0.173828   -0.014217   -0.0338841  118 SER   A HA   
3407 H HB2  . SER   B 106 ? 0.455426 0.470681 0.20015  -0.131375   -0.0308744  -0.035699   118 SER   A HB2  
3408 H HB3  . SER   B 106 ? 0.437619 0.483834 0.209009 -0.122371   -0.00861684 -0.0623117  118 SER   A HB3  
3410 N N    . LEU   B 107 ? 0.531444 0.641739 0.221016 -0.189095   0.0327725   -0.0715915  119 LEU   A N    
3411 C CA   . LEU   B 107 ? 0.566421 0.719428 0.262811 -0.195133   0.0609005   -0.0973291  119 LEU   A CA   
3412 C C    . LEU   B 107 ? 0.628253 0.788061 0.296308 -0.1996     0.0676933   -0.118756   119 LEU   A C    
3413 O O    . LEU   B 107 ? 0.672977 0.813775 0.294788 -0.213152   0.0522965   -0.10692    119 LEU   A O    
3414 C CB   . LEU   B 107 ? 0.612154 0.785657 0.290681 -0.222269   0.0740119   -0.0861839  119 LEU   A CB   
3415 C CG   . LEU   B 107 ? 0.689369 0.871575 0.411386 -0.216336   0.0739283   -0.0791019  119 LEU   A CG   
3416 C CD1  . LEU   B 107 ? 0.822319 1.01456  0.521766 -0.250104   0.0827672   -0.0629947  119 LEU   A CD1  
3417 C CD2  . LEU   B 107 ? 0.656687 0.88091  0.43286  -0.195107   0.0918567   -0.106107   119 LEU   A CD2  
3418 H H    . LEU   B 107 ? 0.553628 0.650622 0.220328 -0.202771   0.0252717   -0.0532705  119 LEU   A H    
3419 H HA   . LEU   B 107 ? 0.541841 0.706119 0.278361 -0.17715    0.0668115   -0.108632   119 LEU   A HA   
3420 H HB2  . LEU   B 107 ? 0.656557 0.809421 0.298259 -0.238005   0.0635439   -0.0669967  119 LEU   A HB2  
3421 H HB3  . LEU   B 107 ? 0.645967 0.849349 0.319992 -0.230223   0.0936792   -0.102878   119 LEU   A HB3  
3422 H HG   . LEU   B 107 ? 0.66048  0.814524 0.390467 -0.204737   0.0562135   -0.0674012  119 LEU   A HG   
3423 H HD11 . LEU   B 107 ? 0.813116 0.973473 0.481298 -0.260879   0.0695069   -0.0429057  119 LEU   A HD11 
3424 H HD12 . LEU   B 107 ? 0.770577 0.973399 0.499883 -0.248065   0.0834991   -0.0626315  119 LEU   A HD12 
3425 H HD13 . LEU   B 107 ? 0.813102 1.03331  0.500426 -0.26327    0.101164    -0.0733031  119 LEU   A HD13 
3426 H HD21 . LEU   B 107 ? 0.632665 0.843927 0.426195 -0.173681   0.0844638   -0.111689   119 LEU   A HD21 
3427 H HD22 . LEU   B 107 ? 0.672493 0.922639 0.442618 -0.202648   0.10979     -0.121222   119 LEU   A HD22 
3428 H HD23 . LEU   B 107 ? 0.639648 0.878298 0.440096 -0.195438   0.0927604   -0.102541   119 LEU   A HD23 
3429 N N    . PRO   B 108 ? 0.652702 0.842823 0.345174 -0.190532   0.0917264   -0.151863   120 PRO   A N    
3430 C CA   . PRO   B 108 ? 0.60273  0.82453  0.349689 -0.17578    0.11083     -0.164174   120 PRO   A CA   
3431 C C    . PRO   B 108 ? 0.553193 0.759583 0.355644 -0.141771   0.101222    -0.165846   120 PRO   A C    
3432 O O    . PRO   B 108 ? 0.554478 0.785002 0.403947 -0.125383   0.111026    -0.171622   120 PRO   A O    
3433 C CB   . PRO   B 108 ? 0.614757 0.873884 0.359803 -0.180589   0.141282    -0.199418   120 PRO   A CB   
3434 C CG   . PRO   B 108 ? 0.652532 0.893112 0.348226 -0.192026   0.135469    -0.20974    120 PRO   A CG   
3435 C CD   . PRO   B 108 ? 0.647393 0.846181 0.313391 -0.196412   0.102448    -0.180456   120 PRO   A CD   
3436 H HA   . PRO   B 108 ? 0.601083 0.832682 0.346423 -0.18706    0.111805    -0.149938   120 PRO   A HA   
3437 H HB2  . PRO   B 108 ? 0.599381 0.868326 0.386912 -0.159782   0.150223    -0.216149   120 PRO   A HB2  
3438 H HB3  . PRO   B 108 ? 0.634927 0.920881 0.369509 -0.197167   0.155377    -0.19848    120 PRO   A HB3  
3439 H HG2  . PRO   B 108 ? 0.649689 0.888393 0.366503 -0.177184   0.141562    -0.232573   120 PRO   A HG2  
3440 H HG3  . PRO   B 108 ? 0.688762 0.94924  0.350077 -0.212135   0.148743    -0.215865   120 PRO   A HG3  
3441 H HD2  . PRO   B 108 ? 0.648403 0.828956 0.328296 -0.18253    0.092947    -0.188324   120 PRO   A HD2  
3442 H HD3  . PRO   B 108 ? 0.694033 0.891914 0.312581 -0.21689    0.0985025   -0.172714   120 PRO   A HD3  
3443 N N    . LYS   B 109 ? 0.554826 0.723732 0.353645 -0.130888   0.0818483   -0.159645   121 LYS   A N    
3444 C CA   . LYS   B 109 ? 0.505315 0.659158 0.352574 -0.100816   0.0767325   -0.161844   121 LYS   A CA   
3445 C C    . LYS   B 109 ? 0.486497 0.636952 0.357856 -0.0897439  0.0646316   -0.13781    121 LYS   A C    
3446 O O    . LYS   B 109 ? 0.441957 0.600214 0.356584 -0.0663178  0.0684087   -0.140616   121 LYS   A O    
3447 C CB   . LYS   B 109 ? 0.534655 0.65188  0.373516 -0.0958022  0.060062    -0.160392   121 LYS   A CB   
3448 C CG   . LYS   B 109 ? 0.565715 0.662519 0.452142 -0.0675321  0.0557948   -0.158855   121 LYS   A CG   
3449 C CD   . LYS   B 109 ? 0.616672 0.681983 0.493954 -0.0691981  0.0396525   -0.156864   121 LYS   A CD   
3450 C CE   . LYS   B 109 ? 0.696224 0.76106  0.550534 -0.0835574  0.0443028   -0.183946   121 LYS   A CE   
3451 N NZ   . LYS   B 109 ? 0.697749 0.758146 0.588883 -0.068682   0.0617786   -0.211403   121 LYS   A NZ   
3452 H H    . LYS   B 109 ? 0.567343 0.720691 0.333448 -0.142718   0.071453    -0.152772   121 LYS   A H    
3453 H HA   . LYS   B 109 ? 0.516906 0.687349 0.389772 -0.0901008  0.0922897   -0.180467   121 LYS   A HA   
3454 H HB2  . LYS   B 109 ? 0.56741  0.687424 0.390517 -0.103596   0.066623    -0.178163   121 LYS   A HB2  
3455 H HB3  . LYS   B 109 ? 0.542073 0.645542 0.357597 -0.105308   0.0448546   -0.14253    121 LYS   A HB3  
3456 H HG2  . LYS   B 109 ? 0.536685 0.632987 0.435981 -0.0597371  0.0497053   -0.142317   121 LYS   A HG2  
3457 H HG3  . LYS   B 109 ? 0.563096 0.669069 0.473788 -0.0567959  0.0699549   -0.175618   121 LYS   A HG3  
3458 H HD2  . LYS   B 109 ? 0.610736 0.668051 0.468818 -0.076822   0.0252445   -0.139207   121 LYS   A HD2  
3459 H HD3  . LYS   B 109 ? 0.597676 0.650333 0.505011 -0.0530928  0.0389995   -0.154286   121 LYS   A HD3  
3460 H HE2  . LYS   B 109 ? 0.70456  0.786302 0.530168 -0.0981555  0.0500633   -0.189734   121 LYS   A HE2  
3461 H HE3  . LYS   B 109 ? 0.689867 0.740089 0.532377 -0.0892603  0.029247    -0.177741   121 LYS   A HE3  
3462 H HZ1  . LYS   B 109 ? 0.696114 0.771577 0.602247 -0.0610841  0.0752637   -0.216925   121 LYS   A HZ1  
3463 H HZ2  . LYS   B 109 ? 0.683929 0.726696 0.599757 -0.0568716  0.0566526   -0.204548   121 LYS   A HZ2  
3464 H HZ3  . LYS   B 109 ? 0.725957 0.786047 0.601417 -0.0788352  0.0646208   -0.230192   121 LYS   A HZ3  
3465 N N    . ILE   B 110 ? 0.450397 0.586589 0.293613 -0.105358   0.0493088   -0.114629   122 ILE   A N    
3466 C CA   . ILE   B 110 ? 0.450876 0.581358 0.315187 -0.0951769  0.0378862   -0.0969096  122 ILE   A CA   
3467 C C    . ILE   B 110 ? 0.451657 0.598192 0.299866 -0.118342   0.0401879   -0.0877739  122 ILE   A C    
3468 O O    . ILE   B 110 ? 0.551384 0.681669 0.359304 -0.140918   0.0350842   -0.0767193  122 ILE   A O    
3469 C CB   . ILE   B 110 ? 0.445217 0.534954 0.299187 -0.089056   0.0163617   -0.0788922  122 ILE   A CB   
3470 C CG1  . ILE   B 110 ? 0.45686  0.527757 0.322952 -0.0731895  0.0127159   -0.0854442  122 ILE   A CG1  
3471 C CG2  . ILE   B 110 ? 0.417011 0.500865 0.287362 -0.079891   0.00647353  -0.0644949  122 ILE   A CG2  
3472 C CD1  . ILE   B 110 ? 0.451293 0.527899 0.359788 -0.0478287  0.0199134   -0.0915409  122 ILE   A CD1  
3473 H H    . ILE   B 110 ? 0.487259 0.616439 0.298084 -0.121905   0.0457895   -0.110116   122 ILE   A H    
3474 H HA   . ILE   B 110 ? 0.426766 0.570355 0.322457 -0.0784798  0.0430367   -0.102897   122 ILE   A HA   
3475 H HB   . ILE   B 110 ? 0.466385 0.544875 0.29125  -0.104806   0.0102297   -0.0712451  122 ILE   A HB   
3476 H HG12 . ILE   B 110 ? 0.474954 0.549631 0.327966 -0.0811345  0.0181251   -0.0969702  122 ILE   A HG12 
3477 H HG13 . ILE   B 110 ? 0.454532 0.504179 0.312325 -0.0729387  -0.00039864 -0.0738162  122 ILE   A HG13 
3478 H HG21 . ILE   B 110 ? 0.409587 0.472647 0.283442 -0.0695253  -0.0027001  -0.0579133  122 ILE   A HG21 
3479 H HG22 . ILE   B 110 ? 0.405348 0.510098 0.299372 -0.0700566  0.0132614   -0.070295   122 ILE   A HG22 
3480 H HG23 . ILE   B 110 ? 0.429866 0.510602 0.283547 -0.0947082  0.00278554  -0.0567266  122 ILE   A HG23 
3481 H HD11 . ILE   B 110 ? 0.429548 0.503235 0.347455 -0.0400208  0.0137347   -0.0800342  122 ILE   A HD11 
3482 H HD12 . ILE   B 110 ? 0.445848 0.507543 0.36083  -0.0412652  0.0185139   -0.0955788  122 ILE   A HD12 
3483 H HD13 . ILE   B 110 ? 0.447923 0.54631  0.369061 -0.0455487  0.0323023   -0.10289    122 ILE   A HD13 
3484 N N    . PRO   B 111 ? 0.465532 0.644225 0.344673 -0.114968   0.0467356   -0.0906623  123 PRO   A N    
3485 C CA   . PRO   B 111 ? 0.449792 0.646969 0.319635 -0.140633   0.0506361   -0.0845452  123 PRO   A CA   
3486 C C    . PRO   B 111 ? 0.443581 0.600436 0.29376  -0.148537   0.0304589   -0.0636566  123 PRO   A C    
3487 O O    . PRO   B 111 ? 0.412112 0.538172 0.264138 -0.130798   0.0157839   -0.0565152  123 PRO   A O    
3488 C CB   . PRO   B 111 ? 0.489819 0.73571  0.407662 -0.130341   0.0585392   -0.0950712  123 PRO   A CB   
3489 C CG   . PRO   B 111 ? 0.483156 0.732862 0.43474  -0.0954432  0.0582684   -0.103745   123 PRO   A CG   
3490 C CD   . PRO   B 111 ? 0.508361 0.711664 0.435445 -0.0871832  0.0514224   -0.100597   123 PRO   A CD   
3491 H HA   . PRO   B 111 ? 0.488921 0.694094 0.33747  -0.158229   0.060871    -0.08755    123 PRO   A HA   
3492 H HB2  . PRO   B 111 ? 0.472286 0.7155   0.394267 -0.134481   0.0487502   -0.0868873  123 PRO   A HB2  
3493 H HB3  . PRO   B 111 ? 0.490892 0.768081 0.41369  -0.142597   0.0733637   -0.104079   123 PRO   A HB3  
3494 H HG2  . PRO   B 111 ? 0.466408 0.718806 0.435821 -0.0835731  0.0485758   -0.0978777  123 PRO   A HG2  
3495 H HG3  . PRO   B 111 ? 0.485155 0.765017 0.457864 -0.0901406  0.0722194   -0.117301   123 PRO   A HG3  
3496 H HD2  . PRO   B 111 ? 0.470146 0.654316 0.404189 -0.0731413  0.0398586   -0.0920668  123 PRO   A HD2  
3497 H HD3  . PRO   B 111 ? 0.488692 0.699186 0.425658 -0.0784561  0.0617413   -0.113554   123 PRO   A HD3  
3498 N N    . SER   B 112 ? 0.470419 0.630934 0.304812 -0.176655   0.0333984   -0.055949   124 SER   A N    
3499 C CA   . SER   B 112 ? 0.462133 0.590967 0.285084 -0.190032   0.0194199   -0.0402774  124 SER   A CA   
3500 C C    . SER   B 112 ? 0.437081 0.574045 0.293966 -0.170435   0.00977364  -0.046106   124 SER   A C    
3501 O O    . SER   B 112 ? 0.424694 0.607839 0.314605 -0.161755   0.0176159   -0.0592948  124 SER   A O    
3502 C CB   . SER   B 112 ? 0.538453 0.683171 0.349916 -0.22463    0.0310448   -0.0362971  124 SER   A CB   
3503 O OG   . SER   B 112 ? 0.695489 0.800666 0.493069 -0.241573   0.0188018   -0.0207224  124 SER   A OG   
3504 H H    . SER   B 112 ? 0.479742 0.664567 0.310976 -0.189781   0.0468909   -0.0618818  124 SER   A H    
3505 H HA   . SER   B 112 ? 0.486081 0.578507 0.286802 -0.188796   0.00916557  -0.0290045  124 SER   A HA   
3506 H HB2  . SER   B 112 ? 0.574649 0.719735 0.362535 -0.235777   0.0390802   -0.033311   124 SER   A HB2  
3507 H HB3  . SER   B 112 ? 0.540692 0.724715 0.378755 -0.225651   0.040343    -0.047993   124 SER   A HB3  
3509 N N    . ASN   B 113 ? 0.429626 0.524164 0.276853 -0.164253   -0.00658027 -0.0362401  125 ASN   A N    
3510 C CA   . ASN   B 113 ? 0.435427 0.534661 0.303711 -0.153037   -0.0159132  -0.0416121  125 ASN   A CA   
3511 C C    . ASN   B 113 ? 0.376389 0.506499 0.27312  -0.121932   -0.0148669  -0.0504148  125 ASN   A C    
3512 O O    . ASN   B 113 ? 0.362063 0.523336 0.281353 -0.115329   -0.0183877  -0.0575001  125 ASN   A O    
3513 C CB   . ASN   B 113 ? 0.487384 0.609954 0.365074 -0.17945    -0.0131008  -0.0471263  125 ASN   A CB   
3514 C CG   . ASN   B 113 ? 0.488478 0.568991 0.33828  -0.210121   -0.0147552  -0.0346724  125 ASN   A CG   
3515 O OD1  . ASN   B 113 ? 0.504016 0.603643 0.352706 -0.238845   -0.00389419 -0.0341073  125 ASN   A OD1  
3516 N ND2  . ASN   B 113 ? 0.51782  0.542819 0.349504 -0.204424   -0.0275502  -0.0246057  125 ASN   A ND2  
3517 H H    . ASN   B 113 ? 0.450885 0.513804 0.27748  -0.16671    -0.0122127  -0.0265059  125 ASN   A H    
3518 H HA   . ASN   B 113 ? 0.439184 0.503121 0.295856 -0.149064   -0.0254367  -0.035089   125 ASN   A HA   
3519 H HB2  . ASN   B 113 ? 0.463527 0.624129 0.355161 -0.184471   -0.00269275 -0.0535701  125 ASN   A HB2  
3520 H HB3  . ASN   B 113 ? 0.459398 0.588718 0.34975  -0.172268   -0.0204084  -0.0528787  125 ASN   A HB3  
3521 H HD21 . ASN   B 113 ? 0.542205 0.538415 0.357447 -0.219459   -0.0290574  -0.0146031  125 ASN   A HD21 
3522 H HD22 . ASN   B 113 ? 0.497325 0.514026 0.334386 -0.185385   -0.034207   -0.0274576  125 ASN   A HD22 
3523 N N    . ALA   B 114 ? 0.333098 0.449508 0.226991 -0.103618   -0.0127277  -0.0480975  126 ALA   A N    
3524 C CA   . ALA   B 114 ? 0.348043 0.482754 0.267146 -0.0753524  -0.00971158 -0.0529056  126 ALA   A CA   
3525 C C    . ALA   B 114 ? 0.331855 0.442789 0.251671 -0.0554201  -0.0210955  -0.0456626  126 ALA   A C    
3526 O O    . ALA   B 114 ? 0.376567 0.448972 0.27826  -0.0562368  -0.0283483  -0.0383472  126 ALA   A O    
3527 C CB   . ALA   B 114 ? 0.408473 0.540164 0.326174 -0.0702777  0.00017525  -0.0573048  126 ALA   A CB   
3528 H H    . ALA   B 114 ? 0.3623   0.454925 0.237465 -0.11002    -0.0137956  -0.0424876  126 ALA   A H    
3529 H HA   . ALA   B 114 ? 0.342229 0.510942 0.281137 -0.0732868  -0.00609754 -0.0589437  126 ALA   A HA   
3530 H HB1  . ALA   B 114 ? 0.397499 0.549785 0.315401 -0.0819866  0.00956329  -0.0639709  126 ALA   A HB1  
3531 H HB2  . ALA   B 114 ? 0.396292 0.499329 0.294793 -0.0743418  -0.0046018  -0.0516223  126 ALA   A HB2  
3532 H HB3  . ALA   B 114 ? 0.375215 0.513495 0.311426 -0.0515505  0.00228344  -0.0597963  126 ALA   A HB3  
3533 N N    . THR   B 115 ? 0.314083 0.452248 0.255806 -0.0372675  -0.0226659  -0.0470784  127 THR   A N    
3534 C CA   . THR   B 115 ? 0.284495 0.408597 0.227427 -0.0155012  -0.0289148  -0.0394283  127 THR   A CA   
3535 C C    . THR   B 115 ? 0.267422 0.385987 0.226328 0.00517169  -0.0212814  -0.0353757  127 THR   A C    
3536 O O    . THR   B 115 ? 0.29716  0.440585 0.27741  0.0114591   -0.0133103  -0.0406325  127 THR   A O    
3537 C CB   . THR   B 115 ? 0.311658 0.471321 0.265001 -0.0092084  -0.0360607  -0.0409323  127 THR   A CB   
3538 O OG1  . THR   B 115 ? 0.343436 0.495196 0.278933 -0.0295952  -0.043813   -0.0467633  127 THR   A OG1  
3539 C CG2  . THR   B 115 ? 0.335311 0.486472 0.283321 0.0113278   -0.0415565  -0.0319243  127 THR   A CG2  
3540 H H    . THR   B 115 ? 0.308381 0.47744  0.264896 -0.038677   -0.0195527  -0.0521689  127 THR   A H    
3541 H HA   . THR   B 115 ? 0.298693 0.395564 0.225778 -0.0197884  -0.0333465  -0.0364995  127 THR   A HA   
3542 H HB   . THR   B 115 ? 0.310065 0.501704 0.282095 -0.00686953 -0.0334033  -0.0442616  127 THR   A HB   
3544 H HG21 . THR   B 115 ? 0.332973 0.506819 0.281227 0.0119422   -0.0481856  -0.0337559  127 THR   A HG21 
3545 H HG22 . THR   B 115 ? 0.33233  0.454896 0.264777 0.00820825  -0.0426391  -0.0307508  127 THR   A HG22 
3546 H HG23 . THR   B 115 ? 0.32204  0.4744   0.282133 0.0267567   -0.0370545  -0.0254704  127 THR   A HG23 
3547 N N    . LEU   B 116 ? 0.296697 0.383219 0.248847 0.0144559   -0.022553   -0.0277631  128 LEU   A N    
3548 C CA   . LEU   B 116 ? 0.31921  0.394406 0.287457 0.0298564   -0.0151823  -0.0243258  128 LEU   A CA   
3549 C C    . LEU   B 116 ? 0.285602 0.357808 0.261172 0.0501246   -0.015873   -0.0112999  128 LEU   A C    
3550 O O    . LEU   B 116 ? 0.30945  0.376038 0.269128 0.0499144   -0.0218504  -0.00647944 128 LEU   A O    
3551 C CB   . LEU   B 116 ? 0.325164 0.368996 0.283294 0.020912    -0.0152497  -0.0257876  128 LEU   A CB   
3552 C CG   . LEU   B 116 ? 0.35993  0.407319 0.310245 0.0042693   -0.0115044  -0.0371188  128 LEU   A CG   
3553 C CD1  . LEU   B 116 ? 0.439293 0.502815 0.373718 -0.0154635  -0.0120715  -0.0422744  128 LEU   A CD1  
3554 C CD2  . LEU   B 116 ? 0.365217 0.385275 0.304016 -0.00359589 -0.0158258  -0.0372442  128 LEU   A CD2  
3555 H H    . LEU   B 116 ? 0.297844 0.368852 0.236847 0.0104239   -0.0277116  -0.0253723  128 LEU   A H    
3556 H HA   . LEU   B 116 ? 0.306921 0.398176 0.289444 0.0328834   -0.00929201 -0.0295789  128 LEU   A HA   
3557 H HB2  . LEU   B 116 ? 0.332331 0.363373 0.277232 0.0156677   -0.0216166  -0.0222533  128 LEU   A HB2  
3558 H HB3  . LEU   B 116 ? 0.327831 0.361897 0.297677 0.0311895   -0.0116398  -0.0225492  128 LEU   A HB3  
3559 H HG   . LEU   B 116 ? 0.36571  0.423968 0.331855 0.01158     -0.00362848 -0.0428105  128 LEU   A HG   
3560 H HD11 . LEU   B 116 ? 0.411203 0.498583 0.357866 -0.011835   -0.00835018 -0.0453794  128 LEU   A HD11 
3561 H HD12 . LEU   B 116 ? 0.424737 0.487418 0.35099  -0.0253534  -0.00838173 -0.048022   128 LEU   A HD12 
3562 H HD13 . LEU   B 116 ? 0.419905 0.47161  0.340488 -0.0227374  -0.0195389  -0.0368529  128 LEU   A HD13 
3563 H HD21 . LEU   B 116 ? 0.361063 0.371883 0.31316  0.00688474  -0.0143818  -0.0348382  128 LEU   A HD21 
3564 H HD22 . LEU   B 116 ? 0.369868 0.378651 0.29451  -0.0105356  -0.0238079  -0.0316305  128 LEU   A HD22 
3565 H HD23 . LEU   B 116 ? 0.375122 0.399774 0.308402 -0.0123051  -0.0121635  -0.0454917  128 LEU   A HD23 
3566 N N    . PHE   B 117 ? 0.266398 0.337972 0.265092 0.0666912   -0.0079622  -0.00611012 129 PHE   A N    
3567 C CA   . PHE   B 117 ? 0.269109 0.330763 0.273217 0.0839908   -0.0059375  0.0105057   129 PHE   A CA   
3568 C C    . PHE   B 117 ? 0.295616 0.326442 0.314295 0.0862081   0.00317182  0.0122322   129 PHE   A C    
3569 O O    . PHE   B 117 ? 0.343033 0.36856  0.378454 0.0847509   0.00941877  0.00158342  129 PHE   A O    
3570 C CB   . PHE   B 117 ? 0.2819   0.371325 0.30293  0.102385    -0.00688378 0.0197586   129 PHE   A CB   
3571 C CG   . PHE   B 117 ? 0.333591 0.41111  0.358079 0.12098     -0.00385177 0.0423598   129 PHE   A CG   
3572 C CD1  . PHE   B 117 ? 0.341948 0.430326 0.343308 0.125671    -0.0102464  0.0556236   129 PHE   A CD1  
3573 C CD2  . PHE   B 117 ? 0.359778 0.415978 0.410745 0.133447    0.00646345  0.050198    129 PHE   A CD2  
3574 C CE1  . PHE   B 117 ? 0.352462 0.429494 0.352282 0.140559    -0.00502889 0.0791181   129 PHE   A CE1  
3575 C CE2  . PHE   B 117 ? 0.397652 0.438284 0.451331 0.147943    0.0111073   0.0746265   129 PHE   A CE2  
3576 C CZ   . PHE   B 117 ? 0.407076 0.458995 0.433464 0.150963    0.00586707  0.0904439   129 PHE   A CZ   
3577 H H    . PHE   B 117 ? 0.271695 0.347919 0.28246  0.0665005   -0.00290819 -0.0130707  129 PHE   A H    
3578 H HA   . PHE   B 117 ? 0.276115 0.335241 0.263877 0.0815251   -0.010277   0.0143791   129 PHE   A HA   
3579 H HB2  . PHE   B 117 ? 0.287409 0.399192 0.299098 0.0988812   -0.0143609  0.0176551   129 PHE   A HB2  
3580 H HB3  . PHE   B 117 ? 0.28895  0.382709 0.328582 0.105259    -0.00201139 0.0132739   129 PHE   A HB3  
3581 H HD1  . PHE   B 117 ? 0.336527 0.436825 0.32067  0.116697    -0.016885   0.047995    129 PHE   A HD1  
3582 H HD2  . PHE   B 117 ? 0.3567   0.405511 0.422125 0.129939    0.0114514   0.03829     129 PHE   A HD2  
3583 H HE1  . PHE   B 117 ? 0.374712 0.460376 0.354277 0.142467    -0.0082792  0.0870866   129 PHE   A HE1  
3584 H HE2  . PHE   B 117 ? 0.403472 0.4248   0.47652  0.154564    0.0187922   0.0798747   129 PHE   A HE2  
3585 H HZ   . PHE   B 117 ? 0.413224 0.456811 0.438816 0.160421    0.00983511  0.109032    129 PHE   A HZ   
3586 N N    . PHE   B 118 ? 0.325962 0.339897 0.341422 0.0905972   0.00559972  0.0248382   130 PHE   A N    
3587 C CA   . PHE   B 118 ? 0.298549 0.287007 0.33369  0.0924198   0.0148485   0.0288804   130 PHE   A CA   
3588 C C    . PHE   B 118 ? 0.3367   0.317322 0.377657 0.106007    0.022533    0.0514      130 PHE   A C    
3589 O O    . PHE   B 118 ? 0.345959 0.337389 0.366983 0.109767    0.0203964   0.0618174   130 PHE   A O    
3590 C CB   . PHE   B 118 ? 0.28598  0.25953  0.317019 0.0773625   0.0122134   0.0203931   130 PHE   A CB   
3591 C CG   . PHE   B 118 ? 0.283739 0.259468 0.307034 0.0623351   0.00531869  0.00183049  130 PHE   A CG   
3592 C CD1  . PHE   B 118 ? 0.29832  0.283838 0.297416 0.0526986   -0.00458967 -0.00284548 130 PHE   A CD1  
3593 C CD2  . PHE   B 118 ? 0.342847 0.307648 0.379458 0.054673    0.00841424  -0.0109894  130 PHE   A CD2  
3594 C CE1  . PHE   B 118 ? 0.297958 0.28408  0.284723 0.0370494   -0.0103647  -0.0150648  130 PHE   A CE1  
3595 C CE2  . PHE   B 118 ? 0.311652 0.280105 0.331937 0.0383905   0.00118028  -0.0261097  130 PHE   A CE2  
3596 C CZ   . PHE   B 118 ? 0.352804 0.331889 0.347911 0.0302359   -0.00758539 -0.0257809  130 PHE   A CZ   
3597 H H    . PHE   B 118 ? 0.311568 0.331143 0.312891 0.0914295   0.00218683  0.02997     130 PHE   A H    
3598 H HA   . PHE   B 118 ? 0.312458 0.297467 0.362602 0.0937694   0.0185715   0.0223031   130 PHE   A HA   
3599 H HB2  . PHE   B 118 ? 0.28517  0.262238 0.30323  0.0768545   0.00901732  0.0244477   130 PHE   A HB2  
3600 H HB3  . PHE   B 118 ? 0.293515 0.253468 0.340473 0.0779418   0.0182684   0.0235023   130 PHE   A HB3  
3601 H HD1  . PHE   B 118 ? 0.292458 0.284508 0.282369 0.0565052   -0.00676919 0.00261383  130 PHE   A HD1  
3602 H HD2  . PHE   B 118 ? 0.329028 0.282888 0.383663 0.0589971   0.0151069   -0.00931305 130 PHE   A HD2  
3603 H HE1  . PHE   B 118 ? 0.308978 0.298816 0.280065 0.0299352   -0.016244   -0.0159416  130 PHE   A HE1  
3604 H HE2  . PHE   B 118 ? 0.336697 0.300244 0.362485 0.0326313   0.00330101  -0.0367923  130 PHE   A HE2  
3605 H HZ   . PHE   B 118 ? 0.334319 0.31536  0.316582 0.018834    -0.0114362  -0.0333942  130 PHE   A HZ   
3606 N N    . GLU   B 119 ? 0.34916  0.308271 0.416835 0.111082    0.0327797   0.0572435   131 GLU   A N    
3607 C CA   . GLU   B 119 ? 0.380436 0.323189 0.456382 0.116879    0.0434066   0.0789723   131 GLU   A CA   
3608 C C    . GLU   B 119 ? 0.387152 0.309351 0.482174 0.101588    0.0493661   0.0689256   131 GLU   A C    
3609 O O    . GLU   B 119 ? 0.397048 0.307534 0.509298 0.0934446   0.0488389   0.0505827   131 GLU   A O    
3610 C CB   . GLU   B 119 ? 0.389263 0.320135 0.484645 0.134064    0.0501775   0.0969346   131 GLU   A CB   
3611 C CG   . GLU   B 119 ? 0.460457 0.368852 0.565058 0.138242    0.0634705   0.123883    131 GLU   A CG   
3612 C CD   . GLU   B 119 ? 0.462364 0.356604 0.5845   0.158266    0.0673184   0.145702    131 GLU   A CD   
3613 O OE1  . GLU   B 119 ? 0.511728 0.425287 0.617383 0.175694    0.0604646   0.167373    131 GLU   A OE1  
3614 O OE2  . GLU   B 119 ? 0.508666 0.371358 0.665071 0.158067    0.075833    0.139353    131 GLU   A OE2  
3615 H H    . GLU   B 119 ? 0.353287 0.307161 0.434275 0.109985    0.0341869   0.047015    131 GLU   A H    
3616 H HA   . GLU   B 119 ? 0.376779 0.330932 0.433879 0.118794    0.0419417   0.0878229   131 GLU   A HA   
3617 H HB2  . GLU   B 119 ? 0.404114 0.353471 0.488516 0.144163    0.0439054   0.103439    131 GLU   A HB2  
3618 H HB3  . GLU   B 119 ? 0.403821 0.323683 0.5182   0.132824    0.0521646   0.0845734   131 GLU   A HB3  
3619 H HG2  . GLU   B 119 ? 0.443108 0.33397  0.564232 0.127534    0.0700197   0.116777    131 GLU   A HG2  
3620 H HG3  . GLU   B 119 ? 0.443755 0.364556 0.527464 0.138584    0.0633355   0.134745    131 GLU   A HG3  
3621 N N    . ILE   B 120 ? 0.413645 0.336688 0.504954 0.097439    0.0545987   0.0787959   132 ILE   A N    
3622 C CA   . ILE   B 120 ? 0.347912 0.263712 0.458419 0.0824801   0.0571184   0.0690795   132 ILE   A CA   
3623 C C    . ILE   B 120 ? 0.404521 0.311314 0.531097 0.0830997   0.0738679   0.0898726   132 ILE   A C    
3624 O O    . ILE   B 120 ? 0.417866 0.337117 0.525134 0.0902242   0.0801265   0.105939    132 ILE   A O    
3625 C CB   . ILE   B 120 ? 0.354937 0.287412 0.450791 0.0751774   0.0461374   0.0560618   132 ILE   A CB   
3626 C CG1  . ILE   B 120 ? 0.321456 0.261943 0.395773 0.0725562   0.0306442   0.0398121   132 ILE   A CG1  
3627 C CG2  . ILE   B 120 ? 0.331499 0.260832 0.455965 0.0617388   0.0462251   0.0472517   132 ILE   A CG2  
3628 C CD1  . ILE   B 120 ? 0.313883 0.264206 0.370679 0.067312    0.0191514   0.0312736   132 ILE   A CD1  
3629 H H    . ILE   B 120 ? 0.399273 0.330711 0.476182 0.104449    0.0568144   0.0919303   132 ILE   A H    
3630 H HA   . ILE   B 120 ? 0.371308 0.276503 0.497227 0.0762275   0.0556423   0.0576349   132 ILE   A HA   
3631 H HB   . ILE   B 120 ? 0.344534 0.285909 0.427167 0.0808344   0.0494684   0.0647918   132 ILE   A HB   
3632 H HG12 . ILE   B 120 ? 0.327021 0.260657 0.411531 0.0661137   0.0282054   0.0296567   132 ILE   A HG12 
3633 H HG13 . ILE   B 120 ? 0.330197 0.275857 0.392722 0.0804674   0.0309368   0.0449597   132 ILE   A HG13 
3634 H HG21 . ILE   B 120 ? 0.32584  0.264077 0.443211 0.0586304   0.0368201   0.0390057   132 ILE   A HG21 
3635 H HG22 . ILE   B 120 ? 0.340976 0.260445 0.479321 0.0552662   0.044816    0.0391643   132 ILE   A HG22 
3636 H HG23 . ILE   B 120 ? 0.345374 0.27488  0.482217 0.0624852   0.0569817   0.0577765   132 ILE   A HG23 
3637 H HD11 . ILE   B 120 ? 0.314821 0.270724 0.363578 0.0730688   0.0229467   0.0382104   132 ILE   A HD11 
3638 H HD12 . ILE   B 120 ? 0.308149 0.262277 0.349742 0.0652628   0.0115465   0.0245658   132 ILE   A HD12 
3639 H HD13 . ILE   B 120 ? 0.309514 0.256878 0.378961 0.0600734   0.015633    0.0254508   132 ILE   A HD13 
3640 N N    . GLU   B 121 ? 0.394492 0.281287 0.555258 0.0727284   0.081298    0.0865884   133 GLU   A N    
3641 C CA   . GLU   B 121 ? 0.424191 0.303987 0.608568 0.065637    0.098091    0.102209    133 GLU   A CA   
3642 C C    . GLU   B 121 ? 0.422997 0.316421 0.631086 0.0491428   0.0942451   0.0846348   133 GLU   A C    
3643 O O    . GLU   B 121 ? 0.473741 0.361342 0.69996  0.0374036   0.0841225   0.0634275   133 GLU   A O    
3644 C CB   . GLU   B 121 ? 0.476384 0.32189  0.690259 0.0628676   0.110241    0.111752    133 GLU   A CB   
3645 C CG   . GLU   B 121 ? 0.495758 0.330736 0.736005 0.0524814   0.130803    0.132077    133 GLU   A CG   
3646 C CD   . GLU   B 121 ? 0.589298 0.381864 0.859821 0.0490252   0.143207    0.142964    133 GLU   A CD   
3647 O OE1  . GLU   B 121 ? 0.617741 0.388095 0.897424 0.0526302   0.135958    0.126976    133 GLU   A OE1  
3648 O OE2  . GLU   B 121 ? 0.551148 0.331572 0.836612 0.0425735   0.162579    0.168563    133 GLU   A OE2  
3649 H H    . GLU   B 121 ? 0.400695 0.278429 0.570982 0.0686485   0.0765856   0.0732149   133 GLU   A H    
3650 H HA   . GLU   B 121 ? 0.435504 0.324708 0.603027 0.072915    0.104632    0.118402    133 GLU   A HA   
3651 H HB2  . GLU   B 121 ? 0.482302 0.31956  0.683934 0.075755    0.11084     0.123532    133 GLU   A HB2  
3652 H HB3  . GLU   B 121 ? 0.466459 0.303278 0.695984 0.0547212   0.104362    0.0924573   133 GLU   A HB3  
3653 H HG2  . GLU   B 121 ? 0.497044 0.343593 0.754821 0.0396642   0.129901    0.119483    133 GLU   A HG2  
3654 H HG3  . GLU   B 121 ? 0.516592 0.36199  0.737784 0.0599049   0.137853    0.151072    133 GLU   A HG3  
3655 N N    . LEU   B 122 ? 0.410852 0.324384 0.620801 0.048595    0.103261    0.09365     134 LEU   A N    
3656 C CA   . LEU   B 122 ? 0.416016 0.347774 0.658196 0.035453    0.100426    0.0797247   134 LEU   A CA   
3657 C C    . LEU   B 122 ? 0.456398 0.37916  0.743527 0.019762    0.117455    0.0872271   134 LEU   A C    
3658 O O    . LEU   B 122 ? 0.482532 0.407703 0.777883 0.0189381   0.139542    0.108358    134 LEU   A O    
3659 C CB   . LEU   B 122 ? 0.423276 0.383389 0.653206 0.0435764   0.102217    0.0804296   134 LEU   A CB   
3660 C CG   . LEU   B 122 ? 0.381803 0.36685  0.650828 0.0349754   0.0979804   0.0670914   134 LEU   A CG   
3661 C CD1  . LEU   B 122 ? 0.311743 0.296755 0.59264  0.0265693   0.0729956   0.0468444   134 LEU   A CD1  
3662 C CD2  . LEU   B 122 ? 0.400201 0.408423 0.654801 0.0482172   0.101418    0.0659366   134 LEU   A CD2  
3663 H H    . LEU   B 122 ? 0.425663 0.343905 0.617479 0.0569184   0.111177    0.107988    134 LEU   A H    
3664 H HA   . LEU   B 122 ? 0.406264 0.337746 0.650847 0.0307568   0.085112    0.0630221   134 LEU   A HA   
3665 H HB2  . LEU   B 122 ? 0.401145 0.362644 0.603563 0.0515635   0.0908561   0.0746021   134 LEU   A HB2  
3666 H HB3  . LEU   B 122 ? 0.427356 0.389516 0.649431 0.0479659   0.118041    0.0959049   134 LEU   A HB3  
3667 H HG   . LEU   B 122 ? 0.390904 0.37888  0.688993 0.026178    0.111386    0.0733725   134 LEU   A HG   
3668 H HD11 . LEU   B 122 ? 0.335707 0.309058 0.632155 0.0162107   0.0733903   0.0441975   134 LEU   A HD11 
3669 H HD12 . LEU   B 122 ? 0.320621 0.324731 0.623199 0.0246895   0.0676794   0.0404737   134 LEU   A HD12 
3670 H HD13 . LEU   B 122 ? 0.319484 0.297811 0.571041 0.0328757   0.0614449   0.0423901   134 LEU   A HD13 
3671 H HD21 . LEU   B 122 ? 0.40574  0.413104 0.64062  0.0541888   0.115757    0.0777408   134 LEU   A HD21 
3672 H HD22 . LEU   B 122 ? 0.380754 0.386614 0.615365 0.053922    0.0860778   0.0570054   134 LEU   A HD22 
3673 H HD23 . LEU   B 122 ? 0.390277 0.416622 0.676199 0.0446896   0.104838    0.0617516   134 LEU   A HD23 
3674 N N    . LEU   B 123 ? 0.466659 0.381    0.784621 0.00384622  0.107505    0.0681174   135 LEU   A N    
3675 C CA   . LEU   B 123 ? 0.523068 0.424075 0.887266 -0.0150817  0.122239    0.071188    135 LEU   A CA   
3676 C C    . LEU   B 123 ? 0.493528 0.430303 0.897621 -0.0276136  0.126821    0.0679342   135 LEU   A C    
3677 O O    . LEU   B 123 ? 0.509706 0.446912 0.944941 -0.038682   0.149483    0.0831782   135 LEU   A O    
3678 C CB   . LEU   B 123 ? 0.511601 0.390307 0.890926 -0.0282683  0.109006    0.0466678   135 LEU   A CB   
3679 C CG   . LEU   B 123 ? 0.548425 0.394746 0.897002 -0.0148973  0.106619    0.0461444   135 LEU   A CG   
3680 C CD1  . LEU   B 123 ? 0.564738 0.395162 0.92598  -0.0284141  0.0946134   0.0152427   135 LEU   A CD1  
3681 C CD2  . LEU   B 123 ? 0.54679  0.360117 0.899454 -0.00733493 0.129535    0.0755254   135 LEU   A CD2  
3682 H H    . LEU   B 123 ? 0.4568   0.373769 0.766213 0.00336589  0.091482    0.0524378   135 LEU   A H    
3683 H HA   . LEU   B 123 ? 0.530477 0.414139 0.890507 -0.0112657  0.138399    0.0910193   135 LEU   A HA   
3684 H HB2  . LEU   B 123 ? 0.503604 0.401432 0.883305 -0.0325877  0.0922538   0.0290068   135 LEU   A HB2  
3685 H HB3  . LEU   B 123 ? 0.542159 0.410189 0.954366 -0.0427098  0.118679    0.0467712   135 LEU   A HB3  
3686 H HG   . LEU   B 123 ? 0.518045 0.37668  0.835307 -0.00183974 0.0981424   0.0472142   135 LEU   A HG   
3687 H HD11 . LEU   B 123 ? 0.545688 0.398318 0.907309 -0.036129   0.0801985   -0.00051733 135 LEU   A HD11 
3688 H HD12 . LEU   B 123 ? 0.563516 0.381197 0.903506 -0.0179964  0.0918029   0.0117415   135 LEU   A HD12 
3689 H HD13 . LEU   B 123 ? 0.586666 0.398039 0.977197 -0.040278   0.104266    0.0139232   135 LEU   A HD13 
3690 H HD21 . LEU   B 123 ? 0.552465 0.377288 0.885013 0.00394394  0.135076    0.0943945   135 LEU   A HD21 
3691 H HD22 . LEU   B 123 ? 0.57718  0.380324 0.961088 -0.0212316  0.140414    0.0788175   135 LEU   A HD22 
3692 H HD23 . LEU   B 123 ? 0.568134 0.359463 0.912666 -6.467e-05  0.127725    0.0723782   135 LEU   A HD23 
3693 N N    . ASP   B 124 ? 0.436502 0.403811 0.841235 -0.025427   0.105266    0.0493258   136 ASP   A N    
3694 C CA   . ASP   B 124 ? 0.450236 0.456565 0.901506 -0.0355008  0.103556    0.0417472   136 ASP   A CA   
3695 C C    . ASP   B 124 ? 0.386378 0.41882  0.825484 -0.0246384  0.0764014   0.0268067   136 ASP   A C    
3696 O O    . ASP   B 124 ? 0.40381  0.421087 0.803928 -0.0179859  0.0568725   0.0182026   136 ASP   A O    
3697 C CB   . ASP   B 124 ? 0.483038 0.488778 0.98639  -0.0622771  0.102102    0.0288544   136 ASP   A CB   
3698 C CG   . ASP   B 124 ? 0.53256  0.57955  1.09845  -0.0768553  0.112207    0.0287553   136 ASP   A CG   
3699 O OD1  . ASP   B 124 ? 0.483573 0.56067  1.05426  -0.064262   0.12419     0.0394312   136 ASP   A OD1  
3700 O OD2  . ASP   B 124 ? 0.562728 0.612412 1.17429  -0.101587   0.109624    0.016231    136 ASP   A OD2  
3701 H H    . ASP   B 124 ? 0.435698 0.399823 0.812729 -0.0171013  0.0910217   0.0421015   136 ASP   A H    
3702 H HA   . ASP   B 124 ? 0.447818 0.465318 0.905848 -0.0317912  0.121895    0.0554516   136 ASP   A HA   
3703 H HB2  . ASP   B 124 ? 0.50985  0.486453 1.01243  -0.0682286  0.114787    0.0359053   136 ASP   A HB2  
3704 H HB3  . ASP   B 124 ? 0.482058 0.489062 0.981961 -0.0664818  0.0810218   0.0114077   136 ASP   A HB3  
3705 N N    . PHE   B 125 ? 0.385081 0.457578 0.863657 -0.0242237  0.0757667   0.0240996   137 PHE   A N    
3706 C CA   . PHE   B 125 ? 0.351729 0.44946  0.8341   -0.0157016  0.0478819   0.0115121   137 PHE   A CA   
3707 C C    . PHE   B 125 ? 0.368822 0.513223 0.919991 -0.0237852  0.0462237   0.00562623  137 PHE   A C    
3708 O O    . PHE   B 125 ? 0.376764 0.540348 0.963498 -0.0269897  0.073042    0.013966    137 PHE   A O    
3709 C CB   . PHE   B 125 ? 0.34049  0.43436  0.780948 0.00898524  0.0484859   0.0179275   137 PHE   A CB   
3710 C CG   . PHE   B 125 ? 0.394295 0.500895 0.838919 0.0205488   0.0788496   0.0298705   137 PHE   A CG   
3711 C CD1  . PHE   B 125 ? 0.377888 0.522003 0.862058 0.0297726   0.0838834   0.0258856   137 PHE   A CD1  
3712 C CD2  . PHE   B 125 ? 0.424787 0.508128 0.832515 0.0233731   0.102463    0.0449047   137 PHE   A CD2  
3713 C CE1  . PHE   B 125 ? 0.360463 0.517963 0.842766 0.0406465   0.11379     0.0329484   137 PHE   A CE1  
3714 C CE2  . PHE   B 125 ? 0.462322 0.560891 0.867365 0.0321692   0.130294    0.0551938   137 PHE   A CE2  
3715 C CZ   . PHE   B 125 ? 0.404328 0.538831 0.841748 0.0413128   0.136118    0.0470174   137 PHE   A CZ   
3716 H H    . PHE   B 125 ? 0.388615 0.473136 0.893719 -0.0287973  0.0938209   0.0314385   137 PHE   A H    
3717 H HA   . PHE   B 125 ? 0.357961 0.444929 0.826517 -0.0217128  0.0288931   0.00197261  137 PHE   A HA   
3718 H HB2  . PHE   B 125 ? 0.343257 0.451037 0.79028  0.0146854   0.030097    0.0112007   137 PHE   A HB2  
3719 H HB3  . PHE   B 125 ? 0.350979 0.419376 0.751258 0.0120115   0.0453315   0.0196029   137 PHE   A HB3  
3720 H HD1  . PHE   B 125 ? 0.367128 0.528198 0.876918 0.0303873   0.0658013   0.0175844   137 PHE   A HD1  
3721 H HD2  . PHE   B 125 ? 0.429211 0.488369 0.815001 0.0191701   0.0998341   0.0482108   137 PHE   A HD2  
3722 H HE1  . PHE   B 125 ? 0.373241 0.557103 0.884625 0.0481477   0.118202    0.0277881   137 PHE   A HE1  
3723 H HE2  . PHE   B 125 ? 0.454414 0.538583 0.83027  0.0343223   0.14396     0.0669006   137 PHE   A HE2  
3724 H HZ   . PHE   B 125 ? 0.420064 0.566212 0.854502 0.046488    0.157303    0.0520021   137 PHE   A HZ   
3725 N N    . LYS   B 126 ? 0.382497 0.549178 0.953417 -0.0274877  0.0143774   -0.00790902 138 LYS   A N    
3726 C CA   . LYS   B 126 ? 0.373615 0.591377 1.01632  -0.0354825  0.00697897  -0.0148703  138 LYS   A CA   
3727 C C    . LYS   B 126 ? 0.362197 0.60325  1.00602  -0.0173724  -0.0258368  -0.0187026  138 LYS   A C    
3728 O O    . LYS   B 126 ? 0.338474 0.55437  0.931122 -0.0112933  -0.0484352  -0.0198389  138 LYS   A O    
3729 C CB   . LYS   B 126 ? 0.359588 0.58439  1.0398   -0.0670379  -0.00022059 -0.0279866  138 LYS   A CB   
3730 H H    . LYS   B 126 ? 0.37347  0.525747 0.913013 -0.0251732  -0.00394269 -0.0123921  138 LYS   A H    
3731 H HA   . LYS   B 126 ? 0.369498 0.602508 1.03663  -0.0313352  0.0298183   -0.00791094 138 LYS   A HA   
3734 N N    . GLY   B 127 ? 0.432004 0.723518 1.14003  -0.0102941  -0.0290327  -0.0201931  139 GLY   A N    
3735 C CA   . GLY   B 127 ? 0.461704 0.779738 1.18603  0.00799221  -0.0621102  -0.0214575  139 GLY   A CA   
3736 C C    . GLY   B 127 ? 0.497717 0.819628 1.21023  -0.00636511 -0.104377   -0.0291979  139 GLY   A C    
3737 O O    . GLY   B 127 ? 0.447238 0.772621 1.17055  -0.0338915  -0.107502   -0.0401783  139 GLY   A O    
3738 H H    . GLY   B 127 ? 0.419798 0.73056  1.16524  -0.0168094  -0.00907753 -0.0194428  139 GLY   A H    
3739 H HA2  . GLY   B 127 ? 0.457847 0.754085 1.14712  0.0261399   -0.0608585  -0.0156588  139 GLY   A HA2  
3740 H HA3  . GLY   B 127 ? 0.457968 0.814697 1.23722  0.0124752   -0.0577085  -0.0227008  139 GLY   A HA3  
3741 N N    . GLU   B 128 ? 0.54672  0.863117 1.23119  0.0117618   -0.135027   -0.0232114  140 GLU   A N    
3742 C CA   . GLU   B 128 ? 0.63682  0.969482 1.31474  0.00256779  -0.179288   -0.0267222  140 GLU   A CA   
3743 C C    . GLU   B 128 ? 0.634193 1.03428  1.39652  -0.00592723 -0.198826   -0.0341527  140 GLU   A C    
3744 O O    . GLU   B 128 ? 0.697609 1.11786  1.4553   -0.0154859  -0.238493   -0.0376036  140 GLU   A O    
3745 C CB   . GLU   B 128 ? 0.698196 1.01037  1.333    0.0262626   -0.204769   -0.0123991  140 GLU   A CB   
3746 O OXT  . GLU   B 128 ? 0.55928  0.994047 1.38951  -0.00355805 -0.17479    -0.0362743  140 GLU   A OXT  
3747 H H    . GLU   B 128 ? 0.546935 0.847877 1.21391  0.0300794   -0.127843   -0.0160509  140 GLU   A H    
3748 H HA   . GLU   B 128 ? 0.634617 0.947335 1.2791   -0.0155923  -0.180631   -0.0340046  140 GLU   A HA   
3751 C C4   . A1INX C .   ? 0.548434 0.371817 0.376692 0.0287407   -0.0383267  -0.065015   201 A1INX B C4   
3752 C C14  . A1INX C .   ? 0.653574 0.484917 0.454836 0.084107    0.0250513   -0.062566   201 A1INX B C14  
3753 C C5   . A1INX C .   ? 0.574401 0.372861 0.387739 0.0381807   -0.037647   -0.0779696  201 A1INX B C5   
3754 C C6   . A1INX C .   ? 0.653653 0.438676 0.428429 0.05354     -0.0354997  -0.0903853  201 A1INX B C6   
3755 C C11  . A1INX C .   ? 0.862391 0.600451 0.638574 0.0950507   -0.00776703 -0.104096   201 A1INX B C11  
3756 C C7   . A1INX C .   ? 0.6936   0.489437 0.44303  0.0587714   -0.0337716  -0.0874172  201 A1INX B C7   
3757 C C8   . A1INX C .   ? 0.767462 0.556621 0.463188 0.0884919   -0.00616389 -0.0910481  201 A1INX B C8   
3758 C C9   . A1INX C .   ? 0.821643 0.559103 0.596344 0.0631542   -0.0375441  -0.108985   201 A1INX B C9   
3759 C C10  . A1INX C .   ? 0.810911 0.52629  0.562656 0.0859603   -0.0270009  -0.120408   201 A1INX B C10  
3760 C C12  . A1INX C .   ? 0.908807 0.627966 0.672065 0.120424    0.00269447  -0.114334   201 A1INX B C12  
3761 C C13  . A1INX C .   ? 0.73748  0.54414  0.547414 0.0798556   0.00937659  -0.0708957  201 A1INX B C13  
3762 N N1   . A1INX C .   ? 0.819829 0.598129 0.601105 0.0950484   0.00754791  -0.0888833  201 A1INX B N1   
3763 N N2   . A1INX C .   ? 0.723869 0.5463   0.493742 0.103137    0.0353502   -0.0737007  201 A1INX B N2   
3764 C C3   . A1INX C .   ? 0.567451 0.398792 0.371718 0.0348294   -0.0370596  -0.0629542  201 A1INX B C3   
3765 N N3   . A1INX C .   ? 0.802106 0.59105  0.557316 0.110888    0.023429    -0.0913424  201 A1INX B N3   
3766 C C1   . A1INX C .   ? 0.613798 0.448098 0.357862 0.0501077   -0.0366876  -0.0565931  201 A1INX B C1   
3767 O O1   . A1INX C .   ? 0.628358 0.448491 0.362292 0.0570486   -0.0321177  -0.0685894  201 A1INX B O1   
3768 C C2   . A1INX C .   ? 0.608407 0.42589  0.373176 0.0492899   -0.0344313  -0.0726099  201 A1INX B C2   
3769 O O2   . A1INX C .   ? 0.761581 0.543814 0.466867 0.0752438   -0.0305524  -0.0984568  201 A1INX B O2   
3770 O O3   . A1INX C .   ? 0.761976 0.520411 0.516414 0.0667966   -0.0338833  -0.105554   201 A1INX B O3   
3771 C C15  . A1INX C .   ? 0.673574 0.534285 0.49394  0.0709913   0.0319749   -0.044521   201 A1INX B C15  
3772 C C16  . A1INX C .   ? 0.596408 0.451836 0.393481 0.0633929   0.0246822   -0.0430007  201 A1INX B C16  
3773 C C17  . A1INX C .   ? 0.675896 0.53179  0.436466 0.074728    0.0396843   -0.0423369  201 A1INX B C17  
3774 C C18  . A1INX C .   ? 0.53238  0.40343  0.353032 0.0473641   0.0213632   -0.0288952  201 A1INX B C18  
3775 O O4   . A1INX C .   ? 0.515749 0.385909 0.363943 0.0375539   0.00767905  -0.029486   201 A1INX B O4   
3776 C C19  . A1INX C .   ? 0.473956 0.3612   0.347546 0.0270087   0.0085686   -0.017706   201 A1INX B C19  
3777 O O5   . A1INX C .   ? 0.487354 0.388501 0.364497 0.0236735   0.018314    -0.00810022 201 A1INX B O5   
3778 C C20  . A1INX C .   ? 0.430005 0.315399 0.325893 0.0186153   -0.00344847 -0.0177942  201 A1INX B C20  
3779 C C21  . A1INX C .   ? 0.444147 0.341111 0.364372 0.0196274   0.00260959  -0.0104375  201 A1INX B C21  
3780 C C22  . A1INX C .   ? 0.492671 0.378927 0.409377 0.0340964   0.00814462  -0.0170579  201 A1INX B C22  
3781 C C23  . A1INX C .   ? 0.515802 0.3705   0.419959 0.0347001   -0.00328301 -0.0288424  201 A1INX B C23  
3782 C C24  . A1INX C .   ? 0.483929 0.328937 0.363437 0.0319238   -0.0103935  -0.0389243  201 A1INX B C24  
3783 N N4   . A1INX C .   ? 0.508668 0.371681 0.393323 0.0206321   -0.0142255  -0.0310024  201 A1INX B N4   
3784 C C25  . A1INX C .   ? 0.498787 0.358576 0.374181 0.0151713   -0.0264207  -0.0369702  201 A1INX B C25  
3785 O O6   . A1INX C .   ? 0.499117 0.372369 0.373041 0.0120523   -0.0276026  -0.0307299  201 A1INX B O6   
3786 C C26  . A1INX C .   ? 0.506422 0.344434 0.371776 0.0142111   -0.0397754  -0.052957   201 A1INX B C26  
3787 C C27  . A1INX C .   ? 0.539464 0.388348 0.418393 0.0007214   -0.0552816  -0.0551689  201 A1INX B C27  
3788 C C28  . A1INX C .   ? 0.490912 0.352594 0.403063 -0.0127247  -0.0542734  -0.0439494  201 A1INX B C28  
3789 C C29  . A1INX C .   ? 0.520576 0.399718 0.451385 -0.0261068  -0.0666008  -0.0459693  201 A1INX B C29  
3790 C C30  . A1INX C .   ? 0.523185 0.389065 0.45063  -0.0331479  -0.0819496  -0.062494   201 A1INX B C30  
3791 C C31  . A1INX C .   ? 0.597482 0.449066 0.489321 -0.0185055  -0.0871092  -0.0758228  201 A1INX B C31  
3792 C C32  . A1INX C .   ? 0.587662 0.418531 0.456852 -0.00326906 -0.0717348  -0.0735455  201 A1INX B C32  
3793 H H5   . A1INX C .   ? 0.588923 0.377364 0.416138 0.0350913   -0.0387534  -0.0785352  201 A1INX B H5   
3794 H H13  . A1INX C .   ? 0.823125 0.562276 0.62413  0.0839564   -0.01258    -0.0956956  201 A1INX B H13  
3795 H H7   . A1INX C .   ? 0.802032 0.582152 0.46432  0.100445    -0.00312392 -0.0985895  201 A1INX B H7   
3796 H H8   . A1INX C .   ? 0.76381  0.5498   0.475543 0.0905996   -0.00164802 -0.0930978  201 A1INX B H8   
3797 H H6   . A1INX C .   ? 0.744224 0.550766 0.450509 0.0838212   0.00295785  -0.0764659  201 A1INX B H6   
3798 H H9   . A1INX C .   ? 0.807946 0.530486 0.584511 0.0526488   -0.0522928  -0.117498   201 A1INX B H9   
3799 H H10  . A1INX C .   ? 0.762988 0.514843 0.563433 0.0571563   -0.0321478  -0.0954757  201 A1INX B H10  
3800 H H12  . A1INX C .   ? 0.866115 0.552582 0.614591 0.0850925   -0.036356   -0.131394   201 A1INX B H12  
3801 H H11  . A1INX C .   ? 0.859963 0.576015 0.584203 0.0963969   -0.0233393  -0.12745    201 A1INX B H11  
3802 H H15  . A1INX C .   ? 0.93238  0.649238 0.66878  0.132517    0.00817584  -0.123752   201 A1INX B H15  
3803 H H16  . A1INX C .   ? 0.929853 0.618138 0.691501 0.119597    -0.00735666 -0.122604   201 A1INX B H16  
3804 H H14  . A1INX C .   ? 0.886638 0.626975 0.669531 0.125952    0.0138105   -0.103289   201 A1INX B H14  
3805 H H17  . A1INX C .   ? 0.704664 0.511808 0.533335 0.0679343   0.00113177  -0.065776   201 A1INX B H17  
3806 H H4   . A1INX C .   ? 0.546259 0.390529 0.358513 0.0301183   -0.0378302  -0.0546939  201 A1INX B H4   
3807 H H2   . A1INX C .   ? 0.6307   0.460949 0.347756 0.0575594   -0.0362091  -0.0544957  201 A1INX B H2   
3808 H H3   . A1INX C .   ? 0.586719 0.430101 0.349195 0.0450569   -0.0264469  -0.0455856  201 A1INX B H3   
3809 H H1   . A1INX C .   ? 0.601531 0.440102 0.360144 0.0436172   -0.0506338  -0.0616537  201 A1INX B H1   
3810 H H18  . A1INX C .   ? 0.640548 0.518126 0.463954 0.0763651   0.046603    -0.0391099  201 A1INX B H18  
3811 H H19  . A1INX C .   ? 0.614349 0.480983 0.459217 0.0624362   0.026616    -0.0387977  201 A1INX B H19  
3812 H H20  . A1INX C .   ? 0.624511 0.463587 0.41197  0.062779    0.0111031   -0.0528283  201 A1INX B H20  
3813 H H23  . A1INX C .   ? 0.652816 0.526367 0.424754 0.0735648   0.0541595   -0.0324784  201 A1INX B H23  
3814 H H21  . A1INX C .   ? 0.668054 0.517784 0.41121  0.0716334   0.0336798   -0.0405987  201 A1INX B H21  
3815 H H22  . A1INX C .   ? 0.689301 0.533822 0.43182  0.0865325   0.0408195   -0.0533861  201 A1INX B H22  
3816 H H25  . A1INX C .   ? 0.529484 0.416039 0.362112 0.0457401   0.0330096   -0.0201354  201 A1INX B H25  
3817 H H24  . A1INX C .   ? 0.546795 0.413245 0.350747 0.0455352   0.017314    -0.0276646  201 A1INX B H24  
3818 H H26  . A1INX C .   ? 0.435974 0.32751  0.33621  0.0114486   -0.00829361 -0.0139513  201 A1INX B H26  
3819 H H28  . A1INX C .   ? 0.430757 0.343269 0.357386 0.0178687   0.00913493  -0.00392143 201 A1INX B H28  
3820 H H27  . A1INX C .   ? 0.431796 0.328336 0.363874 0.0133508   -0.00388364 -0.00759547 201 A1INX B H27  
3821 H H29  . A1INX C .   ? 0.477402 0.372484 0.410463 0.0363061   0.0103264   -0.0116816  201 A1INX B H29  
3822 H H30  . A1INX C .   ? 0.497387 0.387939 0.40301  0.041217    0.0167215   -0.01936    201 A1INX B H30  
3823 H H31  . A1INX C .   ? 0.495992 0.3475   0.412637 0.0264087   -0.00987476 -0.0249666  201 A1INX B H31  
3824 H H32  . A1INX C .   ? 0.525194 0.368312 0.424126 0.0454988   -0.00012177 -0.0341499  201 A1INX B H32  
3825 H H33  . A1INX C .   ? 0.521188 0.348458 0.396962 0.0291661   -0.019747   -0.0470378  201 A1INX B H33  
3826 H H34  . A1INX C .   ? 0.522277 0.365845 0.384463 0.0416363   -0.0035563  -0.0431905  201 A1INX B H34  
3827 H H35  . A1INX C .   ? 0.524081 0.351016 0.398606 0.0132431   -0.0388562  -0.0538464  201 A1INX B H35  
3828 H H36  . A1INX C .   ? 0.523537 0.384145 0.394815 0.00371179  -0.0558944  -0.0524345  201 A1INX B H36  
3829 H H38  . A1INX C .   ? 0.51285  0.36032  0.430245 -0.0145685  -0.0525823  -0.044224   201 A1INX B H38  
3830 H H37  . A1INX C .   ? 0.48398  0.357468 0.400576 -0.0103674  -0.0462939  -0.0342818  201 A1INX B H37  
3831 H H39  . A1INX C .   ? 0.494595 0.388946 0.421711 -0.02211    -0.0678226  -0.04412    201 A1INX B H39  
3832 H H40  . A1INX C .   ? 0.49139  0.377191 0.441004 -0.0341997  -0.0634255  -0.0380841  201 A1INX B H40  
3833 H H41  . A1INX C .   ? 0.53312  0.417428 0.475768 -0.0415626  -0.0897613  -0.0636516  201 A1INX B H41  
3834 H H42  . A1INX C .   ? 0.552446 0.400353 0.485347 -0.0391001  -0.0812658  -0.0637327  201 A1INX B H42  
3835 H H43  . A1INX C .   ? 0.575336 0.442338 0.46045  -0.0131945  -0.0893884  -0.0740823  201 A1INX B H43  
3836 H H44  . A1INX C .   ? 0.606244 0.447158 0.494763 -0.0233238  -0.0985227  -0.0883062  201 A1INX B H44  
3837 H H46  . A1INX C .   ? 0.601755 0.41473  0.474569 -0.00541951 -0.0709931  -0.0768839  201 A1INX B H46  
3838 H H45  . A1INX C .   ? 0.609103 0.433013 0.453273 0.00649456  -0.0734876  -0.0812139  201 A1INX B H45  
3839 C C4   . A1INX D .   ? 0.370736 0.360387 0.31159  -0.0330295  -0.00522659 -0.101203   201 A1INX A C4   
3840 C C14  . A1INX D .   ? 0.526583 0.491709 0.489929 -0.0620112  -0.0514237  -0.11513    201 A1INX A C14  
3841 C C5   . A1INX D .   ? 0.403835 0.385006 0.358375 -0.0356842  -4.927e-05  -0.121525   201 A1INX A C5   
3842 C C6   . A1INX D .   ? 0.479199 0.466431 0.405672 -0.055025   -0.00418791 -0.140257   201 A1INX A C6   
3843 C C11  . A1INX D .   ? 0.566877 0.504084 0.582133 -0.059798   -0.00619338 -0.177535   201 A1INX A C11  
3844 C C7   . A1INX D .   ? 0.506811 0.508554 0.389208 -0.0713206  -0.0121696  -0.135004   201 A1INX A C7   
3845 C C8   . A1INX D .   ? 0.5156   0.51948  0.35572  -0.100421   -0.0381506  -0.149022   201 A1INX A C8   
3846 C C9   . A1INX D .   ? 0.548245 0.510558 0.527074 -0.0478104  0.014897    -0.177876   201 A1INX A C9   
3847 C C10  . A1INX D .   ? 0.561905 0.509455 0.553614 -0.0596154  0.0092577   -0.196878   201 A1INX A C10  
3848 C C12  . A1INX D .   ? 0.584355 0.512361 0.615241 -0.0762754  -0.0108493  -0.203191   201 A1INX A C12  
3849 C C13  . A1INX D .   ? 0.517456 0.470867 0.510515 -0.051939   -0.0309871  -0.125968   201 A1INX A C13  
3850 N N1   . A1INX D .   ? 0.520624 0.473114 0.510352 -0.0644634  -0.0269505  -0.154221   201 A1INX A N1   
3851 N N2   . A1INX D .   ? 0.552256 0.526518 0.491091 -0.0806857  -0.0605468  -0.134504   201 A1INX A N2   
3852 C C3   . A1INX D .   ? 0.411124 0.411584 0.313398 -0.0498344  -0.0125991  -0.0976201  201 A1INX A C3   
3853 N N3   . A1INX D .   ? 0.553889 0.521374 0.507827 -0.083009   -0.0449849  -0.160736   201 A1INX A N3   
3854 C C1   . A1INX D .   ? 0.460192 0.471693 0.27917  -0.0880598  -0.0297388  -0.0821881  201 A1INX A C1   
3855 O O1   . A1INX D .   ? 0.450522 0.465123 0.279376 -0.0874276  -0.0233004  -0.105364   201 A1INX A O1   
3856 C C2   . A1INX D .   ? 0.475391 0.480892 0.347286 -0.0688887  -0.0166496  -0.111701   201 A1INX A C2   
3857 O O2   . A1INX D .   ? 0.520159 0.530918 0.367633 -0.0914789  -0.0157941  -0.153066   201 A1INX A O2   
3858 O O3   . A1INX D .   ? 0.5158   0.495085 0.451705 -0.0618044  -0.00130767 -0.16485    201 A1INX A O3   
3859 C C15  . A1INX D .   ? 0.453146 0.419804 0.408076 -0.055184   -0.0636197  -0.0880991  201 A1INX A C15  
3860 C C16  . A1INX D .   ? 0.473636 0.447019 0.384292 -0.0629284  -0.0673484  -0.0814051  201 A1INX A C16  
3861 C C17  . A1INX D .   ? 0.531928 0.513416 0.408437 -0.0808225  -0.0892537  -0.0806911  201 A1INX A C17  
3862 C C18  . A1INX D .   ? 0.457194 0.423923 0.370506 -0.0508623  -0.0688457  -0.0583983  201 A1INX A C18  
3863 O O4   . A1INX D .   ? 0.397684 0.362078 0.33489  -0.0355713  -0.0508558  -0.0582906  201 A1INX A O4   
3864 C C19  . A1INX D .   ? 0.394333 0.35311  0.341207 -0.0235922  -0.0520396  -0.0420719  201 A1INX A C19  
3865 O O5   . A1INX D .   ? 0.387687 0.34081  0.32757  -0.0240261  -0.0650779  -0.0299106  201 A1INX A O5   
3866 C C20  . A1INX D .   ? 0.352405 0.31235  0.320839 -0.00797155 -0.0353077  -0.0410168  201 A1INX A C20  
3867 C C21  . A1INX D .   ? 0.329506 0.281707 0.327576 0.00374727  -0.0333835  -0.0323384  201 A1INX A C21  
3868 C C22  . A1INX D .   ? 0.343053 0.290813 0.364741 -0.00065649 -0.0317734  -0.0416678  201 A1INX A C22  
3869 C C23  . A1INX D .   ? 0.324432 0.269434 0.353654 -0.00018428 -0.0175971  -0.0561881  201 A1INX A C23  
3870 C C24  . A1INX D .   ? 0.339958 0.295855 0.339088 -0.00894757 -0.0178792  -0.0679241  201 A1INX A C24  
3871 N N4   . A1INX D .   ? 0.348604 0.313712 0.324525 -0.00812387 -0.0219257  -0.0567198  201 A1INX A N4   
3872 C C25  . A1INX D .   ? 0.336732 0.315566 0.294359 -0.0133296  -0.0162527  -0.0637586  201 A1INX A C25  
3873 O O6   . A1INX D .   ? 0.353533 0.338585 0.2883   -0.0202286  -0.0222202  -0.0559076  201 A1INX A O6   
3874 C C26  . A1INX D .   ? 0.349098 0.335703 0.31584  -0.0129531  -0.00143965 -0.0838445  201 A1INX A C26  
3875 C C27  . A1INX D .   ? 0.326126 0.333982 0.295015 -0.00670017 0.00985551  -0.0861018  201 A1INX A C27  
3876 C C28  . A1INX D .   ? 0.303193 0.313103 0.294347 0.0132354   0.0113421   -0.0695864  201 A1INX A C28  
3877 C C29  . A1INX D .   ? 0.317786 0.355055 0.3185   0.021045    0.0193295   -0.0717268  201 A1INX A C29  
3878 C C30  . A1INX D .   ? 0.336619 0.386592 0.354968 0.0247899   0.034758    -0.0923863  201 A1INX A C30  
3879 C C31  . A1INX D .   ? 0.383002 0.428672 0.375868 0.00353825  0.0367295   -0.110912   201 A1INX A C31  
3880 C C32  . A1INX D .   ? 0.354699 0.371654 0.337975 -0.00385725 0.0263766   -0.108986   201 A1INX A C32  
3881 H H5   . A1INX D .   ? 0.406138 0.376442 0.387853 -0.0253256  0.00557393  -0.122031   201 A1INX A H5   
3882 H H13  . A1INX D .   ? 0.538334 0.464186 0.579916 -0.0455398  0.00223598  -0.164832   201 A1INX A H13  
3883 H H7   . A1INX D .   ? 0.550753 0.563896 0.360393 -0.115382   -0.042521   -0.159591   201 A1INX A H7   
3884 H H8   . A1INX D .   ? 0.514772 0.509602 0.383827 -0.0943965  -0.0365612  -0.157493   201 A1INX A H8   
3885 H H6   . A1INX D .   ? 0.508517 0.508613 0.345975 -0.0978761  -0.050661   -0.12739    201 A1INX A H6   
3886 H H9   . A1INX D .   ? 0.548749 0.516668 0.528511 -0.044384   0.0288543   -0.192267   201 A1INX A H9   
3887 H H10  . A1INX D .   ? 0.514713 0.469725 0.514912 -0.0341888  0.0160262   -0.16014    201 A1INX A H10  
3888 H H12  . A1INX D .   ? 0.58145  0.516413 0.595883 -0.0537249  0.0230577   -0.212222   201 A1INX A H12  
3889 H H11  . A1INX D .   ? 0.590803 0.549118 0.554157 -0.0750566  0.00283559  -0.210764   201 A1INX A H11  
3890 H H15  . A1INX D .   ? 0.609322 0.549669 0.611697 -0.0903536  -0.0184611  -0.218305   201 A1INX A H15  
3891 H H16  . A1INX D .   ? 0.599839 0.511424 0.653365 -0.0714961  0.00378607  -0.216503   201 A1INX A H16  
3892 H H14  . A1INX D .   ? 0.577334 0.50435  0.624681 -0.0778984  -0.0207657  -0.191367   201 A1INX A H14  
3893 H H17  . A1INX D .   ? 0.49498  0.441914 0.505771 -0.0387335  -0.0219101  -0.115633   201 A1INX A H17  
3894 H H4   . A1INX D .   ? 0.402336 0.405667 0.29742  -0.0494152  -0.0153882  -0.0851847  201 A1INX A H4   
3895 H H2   . A1INX D .   ? 0.476692 0.490784 0.264428 -0.102774   -0.0348883  -0.0767192  201 A1INX A H2   
3896 H H3   . A1INX D .   ? 0.440304 0.438474 0.271621 -0.080013   -0.0404218  -0.0700359  201 A1INX A H3   
3897 H H1   . A1INX D .   ? 0.440974 0.461369 0.272462 -0.0823129  -0.0182441  -0.0840498  201 A1INX A H1   
3898 H H18  . A1INX D .   ? 0.470188 0.439298 0.431132 -0.0584327  -0.0777266  -0.0830901  201 A1INX A H18  
3899 H H19  . A1INX D .   ? 0.446416 0.407109 0.420336 -0.0424696  -0.0550524  -0.0790355  201 A1INX A H19  
3900 H H20  . A1INX D .   ? 0.482601 0.459941 0.385892 -0.0645967  -0.0541652  -0.0928074  201 A1INX A H20  
3901 H H23  . A1INX D .   ? 0.522297 0.503686 0.415436 -0.0791903  -0.101565   -0.0764956  201 A1INX A H23  
3902 H H21  . A1INX D .   ? 0.530671 0.511246 0.384125 -0.0835031  -0.0948407  -0.0671882  201 A1INX A H21  
3903 H H22  . A1INX D .   ? 0.544249 0.5326   0.405947 -0.0912173  -0.0852547  -0.097745   201 A1INX A H22  
3904 H H25  . A1INX D .   ? 0.442357 0.405119 0.3671   -0.0470303  -0.079683   -0.0488161  201 A1INX A H25  
3905 H H24  . A1INX D .   ? 0.457577 0.426179 0.344401 -0.057903   -0.0719281  -0.0530744  201 A1INX A H24  
3906 H H26  . A1INX D .   ? 0.346831 0.310059 0.304909 -0.00555163 -0.0346943  -0.0350005  201 A1INX A H26  
3907 H H28  . A1INX D .   ? 0.33149  0.281658 0.326568 0.0042611   -0.041761   -0.0246302  201 A1INX A H28  
3908 H H27  . A1INX D .   ? 0.325804 0.278687 0.331651 0.0139205   -0.0242638  -0.0274908  201 A1INX A H27  
3909 H H29  . A1INX D .   ? 0.328708 0.27317  0.370847 0.00587852  -0.028519   -0.0344993  201 A1INX A H29  
3910 H H30  . A1INX D .   ? 0.344609 0.294762 0.358442 -0.0107835  -0.0429988  -0.046268   201 A1INX A H30  
3911 H H31  . A1INX D .   ? 0.325066 0.267177 0.366328 0.0114336   -0.00795382 -0.0490713  201 A1INX A H31  
3912 H H32  . A1INX D .   ? 0.341942 0.281532 0.385125 -0.00588291 -0.0171697  -0.0654088  201 A1INX A H32  
3913 H H33  . A1INX D .   ? 0.347675 0.303406 0.356309 -0.00448472 -0.00664665 -0.0767045  201 A1INX A H33  
3914 H H34  . A1INX D .   ? 0.356928 0.314532 0.343753 -0.0212659  -0.0255242  -0.0766779  201 A1INX A H34  
3915 H H35  . A1INX D .   ? 0.344057 0.320678 0.334346 -0.00396298 0.00386186  -0.0859275  201 A1INX A H35  
3916 H H36  . A1INX D .   ? 0.334151 0.351342 0.280745 -0.0178139  0.005614    -0.0836395  201 A1INX A H36  
3917 H H38  . A1INX D .   ? 0.308352 0.306214 0.319332 0.023343    0.0152193   -0.0682043  201 A1INX A H38  
3918 H H37  . A1INX D .   ? 0.300154 0.305722 0.280864 0.0112497   0.0025119   -0.0578961  201 A1INX A H37  
3919 H H39  . A1INX D .   ? 0.312665 0.361192 0.295395 0.0102635   0.0149848   -0.0699773  201 A1INX A H39  
3920 H H40  . A1INX D .   ? 0.305447 0.343569 0.320087 0.0347969   0.0185711   -0.0607165  201 A1INX A H40  
3921 H H41  . A1INX D .   ? 0.338545 0.412156 0.362383 0.0272461   0.0386709   -0.0939311  201 A1INX A H41  
3922 H H42  . A1INX D .   ? 0.344584 0.382826 0.385861 0.0384436   0.0397762   -0.0925937  201 A1INX A H42  
3923 H H43  . A1INX D .   ? 0.370816 0.429053 0.341328 -0.00961179 0.0334971   -0.109099   201 A1INX A H43  
3924 H H44  . A1INX D .   ? 0.382027 0.434249 0.386599 0.00644838  0.0485283   -0.12747    201 A1INX A H44  
3925 H H46  . A1INX D .   ? 0.360722 0.364288 0.367162 0.00678438  0.0307814   -0.111108   201 A1INX A H46  
3926 H H45  . A1INX D .   ? 0.376153 0.394439 0.341054 -0.0176731  0.0263767   -0.121587   201 A1INX A H45  
# 
