data_7IAO
# 
_entry.id   7IAO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7IAO         pdb_00007iao 10.2210/pdb7iao/pdb 
WWPDB D_1001408527 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.entry_id                        7IAO 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ni, X.'              1  ? 
'Marples, P.G.'       2  ? 
'Godoy, A.S.'         3  ? 
'Koekemoer, L.'       4  ? 
'Aschenbrenner, J.C.' 5  ? 
'Balcomb, B.H.'       6  ? 
'Fairhead, M.'        7  ? 
'Lithgo, R.M.'        8  ? 
'Lee, A.'             9  ? 
'Kenton, N.'          10 ? 
'Thompson, W.'        11 ? 
'Tomlinson, C.W.E.'   12 ? 
'Wild, C.'            13 ? 
'Winokan, M.'         14 ? 
'Williams, E.P.'      15 ? 
'Chandran, A.V.'      16 ? 
'Walsh, M.A.'         17 ? 
'Fearon, D.'          18 ? 
'von Delft, F.'       19 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
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 'Serine protease subunit NS2B'                                                                             
5067.486  1  ?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                                                                      
18117.629 1  3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                       
78.133    1  ?                           ?    ? ? 
4 non-polymer syn '(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-[(oxan-4-yl)methyl]acetamide' 
439.938   1  ?                           ?    ? ? 
5 water       nat water                                                                                                      
18.015    58 ?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                                       DMS   
4 '(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-[(oxan-4-yl)methyl]acetamide' A1B8X 
5 water                                                                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1B8X non-polymer         . 
'(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-[(oxan-4-yl)methyl]acetamide' ? 'C23 H26 Cl N5 O2' 
439.938 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'        78.133  
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   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  ?   ?   ?   A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  ?   ?   ?   B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
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 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1B8X 1  202 203 A1B8X LIG B . 
E 5 HOH   1  101 124 HOH   HOH A . 
E 5 HOH   2  102 105 HOH   HOH A . 
E 5 HOH   3  103 20  HOH   HOH A . 
E 5 HOH   4  104 34  HOH   HOH A . 
E 5 HOH   5  105 126 HOH   HOH A . 
E 5 HOH   6  106 121 HOH   HOH A . 
E 5 HOH   7  107 27  HOH   HOH A . 
E 5 HOH   8  108 118 HOH   HOH A . 
E 5 HOH   9  109 119 HOH   HOH A . 
E 5 HOH   10 110 29  HOH   HOH A . 
E 5 HOH   11 111 120 HOH   HOH A . 
E 5 HOH   12 112 48  HOH   HOH A . 
E 5 HOH   13 113 128 HOH   HOH A . 
F 5 HOH   1  301 79  HOH   HOH B . 
F 5 HOH   2  302 4   HOH   HOH B . 
F 5 HOH   3  303 69  HOH   HOH B . 
F 5 HOH   4  304 35  HOH   HOH B . 
F 5 HOH   5  305 31  HOH   HOH B . 
F 5 HOH   6  306 122 HOH   HOH B . 
F 5 HOH   7  307 46  HOH   HOH B . 
F 5 HOH   8  308 14  HOH   HOH B . 
F 5 HOH   9  309 11  HOH   HOH B . 
F 5 HOH   10 310 1   HOH   HOH B . 
F 5 HOH   11 311 51  HOH   HOH B . 
F 5 HOH   12 312 32  HOH   HOH B . 
F 5 HOH   13 313 24  HOH   HOH B . 
F 5 HOH   14 314 10  HOH   HOH B . 
F 5 HOH   15 315 49  HOH   HOH B . 
F 5 HOH   16 316 102 HOH   HOH B . 
F 5 HOH   17 317 2   HOH   HOH B . 
F 5 HOH   18 318 23  HOH   HOH B . 
F 5 HOH   19 319 36  HOH   HOH B . 
F 5 HOH   20 320 30  HOH   HOH B . 
F 5 HOH   21 321 5   HOH   HOH B . 
F 5 HOH   22 322 89  HOH   HOH B . 
F 5 HOH   23 323 3   HOH   HOH B . 
F 5 HOH   24 324 73  HOH   HOH B . 
F 5 HOH   25 325 123 HOH   HOH B . 
F 5 HOH   26 326 58  HOH   HOH B . 
F 5 HOH   27 327 21  HOH   HOH B . 
F 5 HOH   28 328 94  HOH   HOH B . 
F 5 HOH   29 329 43  HOH   HOH B . 
F 5 HOH   30 330 62  HOH   HOH B . 
F 5 HOH   31 331 18  HOH   HOH B . 
F 5 HOH   32 332 87  HOH   HOH B . 
F 5 HOH   33 333 67  HOH   HOH B . 
F 5 HOH   34 334 64  HOH   HOH B . 
F 5 HOH   35 335 131 HOH   HOH B . 
F 5 HOH   36 336 130 HOH   HOH B . 
F 5 HOH   37 337 26  HOH   HOH B . 
F 5 HOH   38 338 100 HOH   HOH B . 
F 5 HOH   39 339 129 HOH   HOH B . 
F 5 HOH   40 340 80  HOH   HOH B . 
F 5 HOH   41 341 125 HOH   HOH B . 
F 5 HOH   42 342 83  HOH   HOH B . 
F 5 HOH   43 343 109 HOH   HOH B . 
F 5 HOH   44 344 127 HOH   HOH B . 
F 5 HOH   45 345 75  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      '2.10.4 (23-JAN-2024)' ?               program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.7.15                 02/11/23        program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 PDB_EXTRACT 3.23                   'SEP. 23, 2016' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
4 XDS         .                      ?               program ?                 ?                                'data reduction'  
?                                                   ?   ? 
5 PHASER      .                      ?               program ?                 ?                                phasing           
?                                                   ?   ? 
# 
_cell.entry_id           7IAO 
_cell.length_a           42.120 
_cell.length_b           42.120 
_cell.length_c           216.191 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7IAO 
_symmetry.Int_Tables_number                95 
_symmetry.space_group_name_H-M             'P 43 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.entry_id          7IAO 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.240 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.07 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   40.52 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-07-31 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92134 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7IAO 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             54.050 
_reflns.d_resolution_high            2.240 
_reflns.number_obs                   10299 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.635 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        5.300 
_reflns.B_iso_Wilson_estimate        44.100 
_reflns.pdbx_redundancy              24.400 
_reflns.pdbx_Rrim_I_all              0.648 
_reflns.pdbx_Rpim_I_all              0.130 
_reflns.pdbx_CC_half                 0.993 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     251201 
_reflns.pdbx_scaling_rejects         295 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 2.240 2.360  ? 35667 ? ? 9.175 ? ? ? 24.600 ? 0.600  ? 1451 ? ? ? ? 100.000 9.367 1.867 0.529 ? 
1 2 7.070 54.050 ? 7509  ? ? 0.115 ? ? ? 17.800 ? 16.200 ? 421  ? ? ? ? 100.000 0.119 0.028 0.994 ? 
# 
_refine.entry_id                                 7IAO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.2370 
_refine.ls_d_res_low                             54.0500 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.5000 
_refine.ls_number_reflns_obs                     9977 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2420 
_refine.ls_R_factor_R_work                       0.2388 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.3021 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.7700 
_refine.ls_number_reflns_R_free                  476 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               52.5600 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -5.8014 
_refine.aniso_B[2][2]                            -5.8014 
_refine.aniso_B[3][3]                            11.6029 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9310 
_refine.correlation_coeff_Fo_to_Fc_free          0.8860 
_refine.overall_SU_R_Cruickshank_DPI             0.3540 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2710 
_refine.pdbx_overall_SU_R_Blow_DPI               0.4090 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2800 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      5GPI 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                96.160 
_refine.B_iso_min                                25.870 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_analyze.entry_id                        7IAO 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.400 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       2.2370 
_refine_hist.d_res_low                        54.0500 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             58 
_refine_hist.number_atoms_total               1556 
_refine_hist.pdbx_number_residues_total       193 
_refine_hist.pdbx_B_iso_mean_ligand           60.64 
_refine_hist.pdbx_B_iso_mean_solvent          46.24 
_refine_hist.pdbx_number_atoms_protein        1463 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        539  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              266  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1560 ?      ? 10.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     0    ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 194  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1196 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1560 0.007  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2124 0.960  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    2.850  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    19.850 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.2400 
_refine_ls_shell.d_res_low                        2.2800 
_refine_ls_shell.pdbx_total_number_of_bins_used   24 
_refine_ls_shell.percent_reflns_obs               85.6600 
_refine_ls_shell.number_reflns_R_work             419 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3989 
_refine_ls_shell.R_factor_R_free                  0.4165 
_refine_ls_shell.percent_reflns_R_free            3.4600 
_refine_ls_shell.number_reflns_R_free             15 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                434 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7IAO 
_struct.title                     
;Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0029543-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7IAO 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, XChemExplorer, ASAP Discovery Consortium, VIRAL PROTEIN' 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
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 7IAO A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7IAO B 2 ? 168 ? Q32ZE1 1509 ? 1675 ? 11 177 
# 
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 7IAO SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7IAO MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7IAO MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7IAO LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4230 ? 
1 MORE         -27  ? 
1 'SSA (A^2)'  9630 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 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 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 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 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
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 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
AA1 4 5 N GLY B 12  ? N GLY B 21  O MET B 32  ? O MET B 41  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TRP B 60  ? N TRP B 69  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N SER B 128 ? N SER B 137 O TYR B 141 ? O TYR B 150 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N GLY B 105 ? N GLY B 114 O ALA B 116 ? O ALA B 125 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7IAO 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   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 LYS B 54 ? ? 58.97 19.42 
2 1 CYS B 80 ? ? 76.81 -3.76 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     335 
_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.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.5896 -2.3696 -19.4179 0.0403 -0.1513 -0.3261 0.1143 0.0885 0.0372 5.0862 2.3129 4.3144 -1.2295 
-0.0516 -0.1889 0.2706 -0.1356 -0.1350 0.3710 0.1426 -0.1689 -0.3714 0.0043 0.3050 
'X-RAY DIFFRACTION' 2 ? refined -17.5010 -0.2092 -15.5597 0.0413 0.0250  -0.1251 0.1241 0.0481 0.0566 1.0229 1.0606 3.1534 -0.5115 
-0.2597 -0.0753 0.1105 -0.1124 0.0019  0.0832 0.1249 0.1007  -0.1074 0.0491 0.1763 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 50 A 87  '{ A|* }' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 17 B 171 '{ B|* }' ? ? ? ? ? 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 88  ? A GLU 45  
8  1 Y 1 A GLU 89  ? A GLU 46  
9  1 Y 1 B MET 10  ? B MET 1   
10 1 Y 1 B LYS 11  ? B LYS 2   
11 1 Y 1 B GLU 12  ? B GLU 3   
12 1 Y 1 B VAL 13  ? B VAL 4   
13 1 Y 1 B LYS 14  ? B LYS 5   
14 1 Y 1 B LYS 15  ? B LYS 6   
15 1 Y 1 B GLY 16  ? B GLY 7   
16 1 Y 1 B GLU 172 ? B GLU 163 
17 1 Y 1 B GLU 173 ? B GLU 164 
18 1 Y 1 B THR 174 ? B THR 165 
19 1 Y 1 B PRO 175 ? B PRO 166 
20 1 Y 1 B VAL 176 ? B VAL 167 
21 1 Y 1 B GLU 177 ? B GLU 168 
# 
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 
A1B8X N1   N  N N 1   
A1B8X N3   N  N N 2   
A1B8X C4   C  N N 3   
A1B8X C5   C  N N 4   
A1B8X C6   C  N N 5   
A1B8X C7   C  N N 6   
A1B8X C8   C  N R 7   
A1B8X C10  C  Y N 8   
A1B8X C13  C  Y N 9   
A1B8X C15  C  N N 10  
A1B8X C17  C  Y N 11  
A1B8X C20  C  Y N 12  
A1B8X C21  C  Y N 13  
A1B8X C22  C  Y N 14  
A1B8X O1   O  N N 15  
A1B8X C1   C  N N 16  
A1B8X C2   C  N N 17  
A1B8X C3   C  N N 18  
A1B8X O2   O  N N 19  
A1B8X N2   N  N N 20  
A1B8X C9   C  Y N 21  
A1B8X C11  C  Y N 22  
A1B8X C12  C  Y N 23  
A1B8X C14  C  Y N 24  
A1B8X C16  C  N N 25  
A1B8X C18  C  Y N 26  
A1B8X C19  C  Y N 27  
A1B8X CL1  CL N N 28  
A1B8X N4   N  Y N 29  
A1B8X N5   N  Y N 30  
A1B8X C23  C  Y N 31  
A1B8X H1   H  N N 32  
A1B8X H2   H  N N 33  
A1B8X H4   H  N N 34  
A1B8X H5   H  N N 35  
A1B8X H6   H  N N 36  
A1B8X H7   H  N N 37  
A1B8X H8   H  N N 38  
A1B8X H9   H  N N 39  
A1B8X H10  H  N N 40  
A1B8X H11  H  N N 41  
A1B8X H12  H  N N 42  
A1B8X H13  H  N N 43  
A1B8X H14  H  N N 44  
A1B8X H15  H  N N 45  
A1B8X H16  H  N N 46  
A1B8X H17  H  N N 47  
A1B8X H18  H  N N 48  
A1B8X H19  H  N N 49  
A1B8X H20  H  N N 50  
A1B8X H21  H  N N 51  
A1B8X H22  H  N N 52  
A1B8X H23  H  N N 53  
A1B8X H24  H  N N 54  
A1B8X H25  H  N N 55  
A1B8X H26  H  N N 56  
A1B8X H27  H  N N 57  
ALA   N    N  N N 58  
ALA   CA   C  N S 59  
ALA   C    C  N N 60  
ALA   O    O  N N 61  
ALA   CB   C  N N 62  
ALA   OXT  O  N N 63  
ALA   H    H  N N 64  
ALA   H2   H  N N 65  
ALA   HA   H  N N 66  
ALA   HB1  H  N N 67  
ALA   HB2  H  N N 68  
ALA   HB3  H  N N 69  
ALA   HXT  H  N N 70  
ARG   N    N  N N 71  
ARG   CA   C  N S 72  
ARG   C    C  N N 73  
ARG   O    O  N N 74  
ARG   CB   C  N N 75  
ARG   CG   C  N N 76  
ARG   CD   C  N N 77  
ARG   NE   N  N N 78  
ARG   CZ   C  N N 79  
ARG   NH1  N  N N 80  
ARG   NH2  N  N N 81  
ARG   OXT  O  N N 82  
ARG   H    H  N N 83  
ARG   H2   H  N N 84  
ARG   HA   H  N N 85  
ARG   HB2  H  N N 86  
ARG   HB3  H  N N 87  
ARG   HG2  H  N N 88  
ARG   HG3  H  N N 89  
ARG   HD2  H  N N 90  
ARG   HD3  H  N N 91  
ARG   HE   H  N N 92  
ARG   HH11 H  N N 93  
ARG   HH12 H  N N 94  
ARG   HH21 H  N N 95  
ARG   HH22 H  N N 96  
ARG   HXT  H  N N 97  
ASN   N    N  N N 98  
ASN   CA   C  N S 99  
ASN   C    C  N N 100 
ASN   O    O  N N 101 
ASN   CB   C  N N 102 
ASN   CG   C  N N 103 
ASN   OD1  O  N N 104 
ASN   ND2  N  N N 105 
ASN   OXT  O  N N 106 
ASN   H    H  N N 107 
ASN   H2   H  N N 108 
ASN   HA   H  N N 109 
ASN   HB2  H  N N 110 
ASN   HB3  H  N N 111 
ASN   HD21 H  N N 112 
ASN   HD22 H  N N 113 
ASN   HXT  H  N N 114 
ASP   N    N  N N 115 
ASP   CA   C  N S 116 
ASP   C    C  N N 117 
ASP   O    O  N N 118 
ASP   CB   C  N N 119 
ASP   CG   C  N N 120 
ASP   OD1  O  N N 121 
ASP   OD2  O  N N 122 
ASP   OXT  O  N N 123 
ASP   H    H  N N 124 
ASP   H2   H  N N 125 
ASP   HA   H  N N 126 
ASP   HB2  H  N N 127 
ASP   HB3  H  N N 128 
ASP   HD2  H  N N 129 
ASP   HXT  H  N N 130 
CYS   N    N  N N 131 
CYS   CA   C  N R 132 
CYS   C    C  N N 133 
CYS   O    O  N N 134 
CYS   CB   C  N N 135 
CYS   SG   S  N N 136 
CYS   OXT  O  N N 137 
CYS   H    H  N N 138 
CYS   H2   H  N N 139 
CYS   HA   H  N N 140 
CYS   HB2  H  N N 141 
CYS   HB3  H  N N 142 
CYS   HG   H  N N 143 
CYS   HXT  H  N N 144 
DMS   S    S  N N 145 
DMS   O    O  N N 146 
DMS   C1   C  N N 147 
DMS   C2   C  N N 148 
DMS   H11  H  N N 149 
DMS   H12  H  N N 150 
DMS   H13  H  N N 151 
DMS   H21  H  N N 152 
DMS   H22  H  N N 153 
DMS   H23  H  N N 154 
GLN   N    N  N N 155 
GLN   CA   C  N S 156 
GLN   C    C  N N 157 
GLN   O    O  N N 158 
GLN   CB   C  N N 159 
GLN   CG   C  N N 160 
GLN   CD   C  N N 161 
GLN   OE1  O  N N 162 
GLN   NE2  N  N N 163 
GLN   OXT  O  N N 164 
GLN   H    H  N N 165 
GLN   H2   H  N N 166 
GLN   HA   H  N N 167 
GLN   HB2  H  N N 168 
GLN   HB3  H  N N 169 
GLN   HG2  H  N N 170 
GLN   HG3  H  N N 171 
GLN   HE21 H  N N 172 
GLN   HE22 H  N N 173 
GLN   HXT  H  N N 174 
GLU   N    N  N N 175 
GLU   CA   C  N S 176 
GLU   C    C  N N 177 
GLU   O    O  N N 178 
GLU   CB   C  N N 179 
GLU   CG   C  N N 180 
GLU   CD   C  N N 181 
GLU   OE1  O  N N 182 
GLU   OE2  O  N N 183 
GLU   OXT  O  N N 184 
GLU   H    H  N N 185 
GLU   H2   H  N N 186 
GLU   HA   H  N N 187 
GLU   HB2  H  N N 188 
GLU   HB3  H  N N 189 
GLU   HG2  H  N N 190 
GLU   HG3  H  N N 191 
GLU   HE2  H  N N 192 
GLU   HXT  H  N N 193 
GLY   N    N  N N 194 
GLY   CA   C  N N 195 
GLY   C    C  N N 196 
GLY   O    O  N N 197 
GLY   OXT  O  N N 198 
GLY   H    H  N N 199 
GLY   H2   H  N N 200 
GLY   HA2  H  N N 201 
GLY   HA3  H  N N 202 
GLY   HXT  H  N N 203 
HIS   N    N  N N 204 
HIS   CA   C  N S 205 
HIS   C    C  N N 206 
HIS   O    O  N N 207 
HIS   CB   C  N N 208 
HIS   CG   C  Y N 209 
HIS   ND1  N  Y N 210 
HIS   CD2  C  Y N 211 
HIS   CE1  C  Y N 212 
HIS   NE2  N  Y N 213 
HIS   OXT  O  N N 214 
HIS   H    H  N N 215 
HIS   H2   H  N N 216 
HIS   HA   H  N N 217 
HIS   HB2  H  N N 218 
HIS   HB3  H  N N 219 
HIS   HD1  H  N N 220 
HIS   HD2  H  N N 221 
HIS   HE1  H  N N 222 
HIS   HE2  H  N N 223 
HIS   HXT  H  N N 224 
HOH   O    O  N N 225 
HOH   H1   H  N N 226 
HOH   H2   H  N N 227 
ILE   N    N  N N 228 
ILE   CA   C  N S 229 
ILE   C    C  N N 230 
ILE   O    O  N N 231 
ILE   CB   C  N S 232 
ILE   CG1  C  N N 233 
ILE   CG2  C  N N 234 
ILE   CD1  C  N N 235 
ILE   OXT  O  N N 236 
ILE   H    H  N N 237 
ILE   H2   H  N N 238 
ILE   HA   H  N N 239 
ILE   HB   H  N N 240 
ILE   HG12 H  N N 241 
ILE   HG13 H  N N 242 
ILE   HG21 H  N N 243 
ILE   HG22 H  N N 244 
ILE   HG23 H  N N 245 
ILE   HD11 H  N N 246 
ILE   HD12 H  N N 247 
ILE   HD13 H  N N 248 
ILE   HXT  H  N N 249 
LEU   N    N  N N 250 
LEU   CA   C  N S 251 
LEU   C    C  N N 252 
LEU   O    O  N N 253 
LEU   CB   C  N N 254 
LEU   CG   C  N N 255 
LEU   CD1  C  N N 256 
LEU   CD2  C  N N 257 
LEU   OXT  O  N N 258 
LEU   H    H  N N 259 
LEU   H2   H  N N 260 
LEU   HA   H  N N 261 
LEU   HB2  H  N N 262 
LEU   HB3  H  N N 263 
LEU   HG   H  N N 264 
LEU   HD11 H  N N 265 
LEU   HD12 H  N N 266 
LEU   HD13 H  N N 267 
LEU   HD21 H  N N 268 
LEU   HD22 H  N N 269 
LEU   HD23 H  N N 270 
LEU   HXT  H  N N 271 
LYS   N    N  N N 272 
LYS   CA   C  N S 273 
LYS   C    C  N N 274 
LYS   O    O  N N 275 
LYS   CB   C  N N 276 
LYS   CG   C  N N 277 
LYS   CD   C  N N 278 
LYS   CE   C  N N 279 
LYS   NZ   N  N N 280 
LYS   OXT  O  N N 281 
LYS   H    H  N N 282 
LYS   H2   H  N N 283 
LYS   HA   H  N N 284 
LYS   HB2  H  N N 285 
LYS   HB3  H  N N 286 
LYS   HG2  H  N N 287 
LYS   HG3  H  N N 288 
LYS   HD2  H  N N 289 
LYS   HD3  H  N N 290 
LYS   HE2  H  N N 291 
LYS   HE3  H  N N 292 
LYS   HZ1  H  N N 293 
LYS   HZ2  H  N N 294 
LYS   HZ3  H  N N 295 
LYS   HXT  H  N N 296 
MET   N    N  N N 297 
MET   CA   C  N S 298 
MET   C    C  N N 299 
MET   O    O  N N 300 
MET   CB   C  N N 301 
MET   CG   C  N N 302 
MET   SD   S  N N 303 
MET   CE   C  N N 304 
MET   OXT  O  N N 305 
MET   H    H  N N 306 
MET   H2   H  N N 307 
MET   HA   H  N N 308 
MET   HB2  H  N N 309 
MET   HB3  H  N N 310 
MET   HG2  H  N N 311 
MET   HG3  H  N N 312 
MET   HE1  H  N N 313 
MET   HE2  H  N N 314 
MET   HE3  H  N N 315 
MET   HXT  H  N N 316 
PHE   N    N  N N 317 
PHE   CA   C  N S 318 
PHE   C    C  N N 319 
PHE   O    O  N N 320 
PHE   CB   C  N N 321 
PHE   CG   C  Y N 322 
PHE   CD1  C  Y N 323 
PHE   CD2  C  Y N 324 
PHE   CE1  C  Y N 325 
PHE   CE2  C  Y N 326 
PHE   CZ   C  Y N 327 
PHE   OXT  O  N N 328 
PHE   H    H  N N 329 
PHE   H2   H  N N 330 
PHE   HA   H  N N 331 
PHE   HB2  H  N N 332 
PHE   HB3  H  N N 333 
PHE   HD1  H  N N 334 
PHE   HD2  H  N N 335 
PHE   HE1  H  N N 336 
PHE   HE2  H  N N 337 
PHE   HZ   H  N N 338 
PHE   HXT  H  N N 339 
PRO   N    N  N N 340 
PRO   CA   C  N S 341 
PRO   C    C  N N 342 
PRO   O    O  N N 343 
PRO   CB   C  N N 344 
PRO   CG   C  N N 345 
PRO   CD   C  N N 346 
PRO   OXT  O  N N 347 
PRO   H    H  N N 348 
PRO   HA   H  N N 349 
PRO   HB2  H  N N 350 
PRO   HB3  H  N N 351 
PRO   HG2  H  N N 352 
PRO   HG3  H  N N 353 
PRO   HD2  H  N N 354 
PRO   HD3  H  N N 355 
PRO   HXT  H  N N 356 
SER   N    N  N N 357 
SER   CA   C  N S 358 
SER   C    C  N N 359 
SER   O    O  N N 360 
SER   CB   C  N N 361 
SER   OG   O  N N 362 
SER   OXT  O  N N 363 
SER   H    H  N N 364 
SER   H2   H  N N 365 
SER   HA   H  N N 366 
SER   HB2  H  N N 367 
SER   HB3  H  N N 368 
SER   HG   H  N N 369 
SER   HXT  H  N N 370 
THR   N    N  N N 371 
THR   CA   C  N S 372 
THR   C    C  N N 373 
THR   O    O  N N 374 
THR   CB   C  N R 375 
THR   OG1  O  N N 376 
THR   CG2  C  N N 377 
THR   OXT  O  N N 378 
THR   H    H  N N 379 
THR   H2   H  N N 380 
THR   HA   H  N N 381 
THR   HB   H  N N 382 
THR   HG1  H  N N 383 
THR   HG21 H  N N 384 
THR   HG22 H  N N 385 
THR   HG23 H  N N 386 
THR   HXT  H  N N 387 
TRP   N    N  N N 388 
TRP   CA   C  N S 389 
TRP   C    C  N N 390 
TRP   O    O  N N 391 
TRP   CB   C  N N 392 
TRP   CG   C  Y N 393 
TRP   CD1  C  Y N 394 
TRP   CD2  C  Y N 395 
TRP   NE1  N  Y N 396 
TRP   CE2  C  Y N 397 
TRP   CE3  C  Y N 398 
TRP   CZ2  C  Y N 399 
TRP   CZ3  C  Y N 400 
TRP   CH2  C  Y N 401 
TRP   OXT  O  N N 402 
TRP   H    H  N N 403 
TRP   H2   H  N N 404 
TRP   HA   H  N N 405 
TRP   HB2  H  N N 406 
TRP   HB3  H  N N 407 
TRP   HD1  H  N N 408 
TRP   HE1  H  N N 409 
TRP   HE3  H  N N 410 
TRP   HZ2  H  N N 411 
TRP   HZ3  H  N N 412 
TRP   HH2  H  N N 413 
TRP   HXT  H  N N 414 
TYR   N    N  N N 415 
TYR   CA   C  N S 416 
TYR   C    C  N N 417 
TYR   O    O  N N 418 
TYR   CB   C  N N 419 
TYR   CG   C  Y N 420 
TYR   CD1  C  Y N 421 
TYR   CD2  C  Y N 422 
TYR   CE1  C  Y N 423 
TYR   CE2  C  Y N 424 
TYR   CZ   C  Y N 425 
TYR   OH   O  N N 426 
TYR   OXT  O  N N 427 
TYR   H    H  N N 428 
TYR   H2   H  N N 429 
TYR   HA   H  N N 430 
TYR   HB2  H  N N 431 
TYR   HB3  H  N N 432 
TYR   HD1  H  N N 433 
TYR   HD2  H  N N 434 
TYR   HE1  H  N N 435 
TYR   HE2  H  N N 436 
TYR   HH   H  N N 437 
TYR   HXT  H  N N 438 
VAL   N    N  N N 439 
VAL   CA   C  N S 440 
VAL   C    C  N N 441 
VAL   O    O  N N 442 
VAL   CB   C  N N 443 
VAL   CG1  C  N N 444 
VAL   CG2  C  N N 445 
VAL   OXT  O  N N 446 
VAL   H    H  N N 447 
VAL   H2   H  N N 448 
VAL   HA   H  N N 449 
VAL   HB   H  N N 450 
VAL   HG11 H  N N 451 
VAL   HG12 H  N N 452 
VAL   HG13 H  N N 453 
VAL   HG21 H  N N 454 
VAL   HG22 H  N N 455 
VAL   HG23 H  N N 456 
VAL   HXT  H  N N 457 
# 
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 
A1B8X CL1 C19  sing N N 1   
A1B8X C20 C21  doub Y N 2   
A1B8X C20 C19  sing Y N 3   
A1B8X N4  C21  sing Y N 4   
A1B8X N4  N5   sing Y N 5   
A1B8X C21 C23  sing Y N 6   
A1B8X C19 C18  doub Y N 7   
A1B8X N5  C22  doub Y N 8   
A1B8X C23 C22  sing Y N 9   
A1B8X C23 C17  doub Y N 10  
A1B8X C18 C17  sing Y N 11  
A1B8X C17 C8   sing N N 12  
A1B8X O1  C1   doub N N 13  
A1B8X C8  C1   sing N N 14  
A1B8X C8  N2   sing N N 15  
A1B8X C1  N1   sing N N 16  
A1B8X N1  C2   sing N N 17  
A1B8X N2  C9   sing N N 18  
A1B8X C2  C3   sing N N 19  
A1B8X C9  C14  doub Y N 20  
A1B8X C9  C10  sing Y N 21  
A1B8X C3  C7   sing N N 22  
A1B8X C3  C4   sing N N 23  
A1B8X C7  C6   sing N N 24  
A1B8X C14 C13  sing Y N 25  
A1B8X C10 C11  doub Y N 26  
A1B8X C4  C5   sing N N 27  
A1B8X C6  O2   sing N N 28  
A1B8X C13 C12  doub Y N 29  
A1B8X C13 C15  sing N N 30  
A1B8X C11 C12  sing Y N 31  
A1B8X O2  C5   sing N N 32  
A1B8X C12 C16  sing N N 33  
A1B8X C15 N3   sing N N 34  
A1B8X N3  C16  sing N N 35  
A1B8X N1  H1   sing N N 36  
A1B8X N3  H2   sing N N 37  
A1B8X C4  H4   sing N N 38  
A1B8X C4  H5   sing N N 39  
A1B8X C5  H6   sing N N 40  
A1B8X C5  H7   sing N N 41  
A1B8X C6  H8   sing N N 42  
A1B8X C6  H9   sing N N 43  
A1B8X C7  H10  sing N N 44  
A1B8X C7  H11  sing N N 45  
A1B8X C8  H12  sing N N 46  
A1B8X C10 H13  sing N N 47  
A1B8X C15 H14  sing N N 48  
A1B8X C15 H15  sing N N 49  
A1B8X C20 H16  sing N N 50  
A1B8X C22 H17  sing N N 51  
A1B8X C2  H18  sing N N 52  
A1B8X C2  H19  sing N N 53  
A1B8X C3  H20  sing N N 54  
A1B8X N2  H21  sing N N 55  
A1B8X C11 H22  sing N N 56  
A1B8X C14 H23  sing N N 57  
A1B8X C16 H24  sing N N 58  
A1B8X C16 H25  sing N N 59  
A1B8X C18 H26  sing N N 60  
A1B8X N4  H27  sing N N 61  
ALA   N   CA   sing N N 62  
ALA   N   H    sing N N 63  
ALA   N   H2   sing N N 64  
ALA   CA  C    sing N N 65  
ALA   CA  CB   sing N N 66  
ALA   CA  HA   sing N N 67  
ALA   C   O    doub N N 68  
ALA   C   OXT  sing N N 69  
ALA   CB  HB1  sing N N 70  
ALA   CB  HB2  sing N N 71  
ALA   CB  HB3  sing N N 72  
ALA   OXT HXT  sing N N 73  
ARG   N   CA   sing N N 74  
ARG   N   H    sing N N 75  
ARG   N   H2   sing N N 76  
ARG   CA  C    sing N N 77  
ARG   CA  CB   sing N N 78  
ARG   CA  HA   sing N N 79  
ARG   C   O    doub N N 80  
ARG   C   OXT  sing N N 81  
ARG   CB  CG   sing N N 82  
ARG   CB  HB2  sing N N 83  
ARG   CB  HB3  sing N N 84  
ARG   CG  CD   sing N N 85  
ARG   CG  HG2  sing N N 86  
ARG   CG  HG3  sing N N 87  
ARG   CD  NE   sing N N 88  
ARG   CD  HD2  sing N N 89  
ARG   CD  HD3  sing N N 90  
ARG   NE  CZ   sing N N 91  
ARG   NE  HE   sing N N 92  
ARG   CZ  NH1  sing N N 93  
ARG   CZ  NH2  doub N N 94  
ARG   NH1 HH11 sing N N 95  
ARG   NH1 HH12 sing N N 96  
ARG   NH2 HH21 sing N N 97  
ARG   NH2 HH22 sing N N 98  
ARG   OXT HXT  sing N N 99  
ASN   N   CA   sing N N 100 
ASN   N   H    sing N N 101 
ASN   N   H2   sing N N 102 
ASN   CA  C    sing N N 103 
ASN   CA  CB   sing N N 104 
ASN   CA  HA   sing N N 105 
ASN   C   O    doub N N 106 
ASN   C   OXT  sing N N 107 
ASN   CB  CG   sing N N 108 
ASN   CB  HB2  sing N N 109 
ASN   CB  HB3  sing N N 110 
ASN   CG  OD1  doub N N 111 
ASN   CG  ND2  sing N N 112 
ASN   ND2 HD21 sing N N 113 
ASN   ND2 HD22 sing N N 114 
ASN   OXT HXT  sing N N 115 
ASP   N   CA   sing N N 116 
ASP   N   H    sing N N 117 
ASP   N   H2   sing N N 118 
ASP   CA  C    sing N N 119 
ASP   CA  CB   sing N N 120 
ASP   CA  HA   sing N N 121 
ASP   C   O    doub N N 122 
ASP   C   OXT  sing N N 123 
ASP   CB  CG   sing N N 124 
ASP   CB  HB2  sing N N 125 
ASP   CB  HB3  sing N N 126 
ASP   CG  OD1  doub N N 127 
ASP   CG  OD2  sing N N 128 
ASP   OD2 HD2  sing N N 129 
ASP   OXT HXT  sing N N 130 
CYS   N   CA   sing N N 131 
CYS   N   H    sing N N 132 
CYS   N   H2   sing N N 133 
CYS   CA  C    sing N N 134 
CYS   CA  CB   sing N N 135 
CYS   CA  HA   sing N N 136 
CYS   C   O    doub N N 137 
CYS   C   OXT  sing N N 138 
CYS   CB  SG   sing N N 139 
CYS   CB  HB2  sing N N 140 
CYS   CB  HB3  sing N N 141 
CYS   SG  HG   sing N N 142 
CYS   OXT HXT  sing N N 143 
DMS   S   O    doub N N 144 
DMS   S   C1   sing N N 145 
DMS   S   C2   sing N N 146 
DMS   C1  H11  sing N N 147 
DMS   C1  H12  sing N N 148 
DMS   C1  H13  sing N N 149 
DMS   C2  H21  sing N N 150 
DMS   C2  H22  sing N N 151 
DMS   C2  H23  sing N N 152 
GLN   N   CA   sing N N 153 
GLN   N   H    sing N N 154 
GLN   N   H2   sing N N 155 
GLN   CA  C    sing N N 156 
GLN   CA  CB   sing N N 157 
GLN   CA  HA   sing N N 158 
GLN   C   O    doub N N 159 
GLN   C   OXT  sing N N 160 
GLN   CB  CG   sing N N 161 
GLN   CB  HB2  sing N N 162 
GLN   CB  HB3  sing N N 163 
GLN   CG  CD   sing N N 164 
GLN   CG  HG2  sing N N 165 
GLN   CG  HG3  sing N N 166 
GLN   CD  OE1  doub N N 167 
GLN   CD  NE2  sing N N 168 
GLN   NE2 HE21 sing N N 169 
GLN   NE2 HE22 sing N N 170 
GLN   OXT HXT  sing N N 171 
GLU   N   CA   sing N N 172 
GLU   N   H    sing N N 173 
GLU   N   H2   sing N N 174 
GLU   CA  C    sing N N 175 
GLU   CA  CB   sing N N 176 
GLU   CA  HA   sing N N 177 
GLU   C   O    doub N N 178 
GLU   C   OXT  sing N N 179 
GLU   CB  CG   sing N N 180 
GLU   CB  HB2  sing N N 181 
GLU   CB  HB3  sing N N 182 
GLU   CG  CD   sing N N 183 
GLU   CG  HG2  sing N N 184 
GLU   CG  HG3  sing N N 185 
GLU   CD  OE1  doub N N 186 
GLU   CD  OE2  sing N N 187 
GLU   OE2 HE2  sing N N 188 
GLU   OXT HXT  sing N N 189 
GLY   N   CA   sing N N 190 
GLY   N   H    sing N N 191 
GLY   N   H2   sing N N 192 
GLY   CA  C    sing N N 193 
GLY   CA  HA2  sing N N 194 
GLY   CA  HA3  sing N N 195 
GLY   C   O    doub N N 196 
GLY   C   OXT  sing N N 197 
GLY   OXT HXT  sing N N 198 
HIS   N   CA   sing N N 199 
HIS   N   H    sing N N 200 
HIS   N   H2   sing N N 201 
HIS   CA  C    sing N N 202 
HIS   CA  CB   sing N N 203 
HIS   CA  HA   sing N N 204 
HIS   C   O    doub N N 205 
HIS   C   OXT  sing N N 206 
HIS   CB  CG   sing N N 207 
HIS   CB  HB2  sing N N 208 
HIS   CB  HB3  sing N N 209 
HIS   CG  ND1  sing Y N 210 
HIS   CG  CD2  doub Y N 211 
HIS   ND1 CE1  doub Y N 212 
HIS   ND1 HD1  sing N N 213 
HIS   CD2 NE2  sing Y N 214 
HIS   CD2 HD2  sing N N 215 
HIS   CE1 NE2  sing Y N 216 
HIS   CE1 HE1  sing N N 217 
HIS   NE2 HE2  sing N N 218 
HIS   OXT HXT  sing N N 219 
HOH   O   H1   sing N N 220 
HOH   O   H2   sing N N 221 
ILE   N   CA   sing N N 222 
ILE   N   H    sing N N 223 
ILE   N   H2   sing N N 224 
ILE   CA  C    sing N N 225 
ILE   CA  CB   sing N N 226 
ILE   CA  HA   sing N N 227 
ILE   C   O    doub N N 228 
ILE   C   OXT  sing N N 229 
ILE   CB  CG1  sing N N 230 
ILE   CB  CG2  sing N N 231 
ILE   CB  HB   sing N N 232 
ILE   CG1 CD1  sing N N 233 
ILE   CG1 HG12 sing N N 234 
ILE   CG1 HG13 sing N N 235 
ILE   CG2 HG21 sing N N 236 
ILE   CG2 HG22 sing N N 237 
ILE   CG2 HG23 sing N N 238 
ILE   CD1 HD11 sing N N 239 
ILE   CD1 HD12 sing N N 240 
ILE   CD1 HD13 sing N N 241 
ILE   OXT HXT  sing N N 242 
LEU   N   CA   sing N N 243 
LEU   N   H    sing N N 244 
LEU   N   H2   sing N N 245 
LEU   CA  C    sing N N 246 
LEU   CA  CB   sing N N 247 
LEU   CA  HA   sing N N 248 
LEU   C   O    doub N N 249 
LEU   C   OXT  sing N N 250 
LEU   CB  CG   sing N N 251 
LEU   CB  HB2  sing N N 252 
LEU   CB  HB3  sing N N 253 
LEU   CG  CD1  sing N N 254 
LEU   CG  CD2  sing N N 255 
LEU   CG  HG   sing N N 256 
LEU   CD1 HD11 sing N N 257 
LEU   CD1 HD12 sing N N 258 
LEU   CD1 HD13 sing N N 259 
LEU   CD2 HD21 sing N N 260 
LEU   CD2 HD22 sing N N 261 
LEU   CD2 HD23 sing N N 262 
LEU   OXT HXT  sing N N 263 
LYS   N   CA   sing N N 264 
LYS   N   H    sing N N 265 
LYS   N   H2   sing N N 266 
LYS   CA  C    sing N N 267 
LYS   CA  CB   sing N N 268 
LYS   CA  HA   sing N N 269 
LYS   C   O    doub N N 270 
LYS   C   OXT  sing N N 271 
LYS   CB  CG   sing N N 272 
LYS   CB  HB2  sing N N 273 
LYS   CB  HB3  sing N N 274 
LYS   CG  CD   sing N N 275 
LYS   CG  HG2  sing N N 276 
LYS   CG  HG3  sing N N 277 
LYS   CD  CE   sing N N 278 
LYS   CD  HD2  sing N N 279 
LYS   CD  HD3  sing N N 280 
LYS   CE  NZ   sing N N 281 
LYS   CE  HE2  sing N N 282 
LYS   CE  HE3  sing N N 283 
LYS   NZ  HZ1  sing N N 284 
LYS   NZ  HZ2  sing N N 285 
LYS   NZ  HZ3  sing N N 286 
LYS   OXT HXT  sing N N 287 
MET   N   CA   sing N N 288 
MET   N   H    sing N N 289 
MET   N   H2   sing N N 290 
MET   CA  C    sing N N 291 
MET   CA  CB   sing N N 292 
MET   CA  HA   sing N N 293 
MET   C   O    doub N N 294 
MET   C   OXT  sing N N 295 
MET   CB  CG   sing N N 296 
MET   CB  HB2  sing N N 297 
MET   CB  HB3  sing N N 298 
MET   CG  SD   sing N N 299 
MET   CG  HG2  sing N N 300 
MET   CG  HG3  sing N N 301 
MET   SD  CE   sing N N 302 
MET   CE  HE1  sing N N 303 
MET   CE  HE2  sing N N 304 
MET   CE  HE3  sing N N 305 
MET   OXT HXT  sing N N 306 
PHE   N   CA   sing N N 307 
PHE   N   H    sing N N 308 
PHE   N   H2   sing N N 309 
PHE   CA  C    sing N N 310 
PHE   CA  CB   sing N N 311 
PHE   CA  HA   sing N N 312 
PHE   C   O    doub N N 313 
PHE   C   OXT  sing N N 314 
PHE   CB  CG   sing N N 315 
PHE   CB  HB2  sing N N 316 
PHE   CB  HB3  sing N N 317 
PHE   CG  CD1  doub Y N 318 
PHE   CG  CD2  sing Y N 319 
PHE   CD1 CE1  sing Y N 320 
PHE   CD1 HD1  sing N N 321 
PHE   CD2 CE2  doub Y N 322 
PHE   CD2 HD2  sing N N 323 
PHE   CE1 CZ   doub Y N 324 
PHE   CE1 HE1  sing N N 325 
PHE   CE2 CZ   sing Y N 326 
PHE   CE2 HE2  sing N N 327 
PHE   CZ  HZ   sing N N 328 
PHE   OXT HXT  sing N N 329 
PRO   N   CA   sing N N 330 
PRO   N   CD   sing N N 331 
PRO   N   H    sing N N 332 
PRO   CA  C    sing N N 333 
PRO   CA  CB   sing N N 334 
PRO   CA  HA   sing N N 335 
PRO   C   O    doub N N 336 
PRO   C   OXT  sing N N 337 
PRO   CB  CG   sing N N 338 
PRO   CB  HB2  sing N N 339 
PRO   CB  HB3  sing N N 340 
PRO   CG  CD   sing N N 341 
PRO   CG  HG2  sing N N 342 
PRO   CG  HG3  sing N N 343 
PRO   CD  HD2  sing N N 344 
PRO   CD  HD3  sing N N 345 
PRO   OXT HXT  sing N N 346 
SER   N   CA   sing N N 347 
SER   N   H    sing N N 348 
SER   N   H2   sing N N 349 
SER   CA  C    sing N N 350 
SER   CA  CB   sing N N 351 
SER   CA  HA   sing N N 352 
SER   C   O    doub N N 353 
SER   C   OXT  sing N N 354 
SER   CB  OG   sing N N 355 
SER   CB  HB2  sing N N 356 
SER   CB  HB3  sing N N 357 
SER   OG  HG   sing N N 358 
SER   OXT HXT  sing N N 359 
THR   N   CA   sing N N 360 
THR   N   H    sing N N 361 
THR   N   H2   sing N N 362 
THR   CA  C    sing N N 363 
THR   CA  CB   sing N N 364 
THR   CA  HA   sing N N 365 
THR   C   O    doub N N 366 
THR   C   OXT  sing N N 367 
THR   CB  OG1  sing N N 368 
THR   CB  CG2  sing N N 369 
THR   CB  HB   sing N N 370 
THR   OG1 HG1  sing N N 371 
THR   CG2 HG21 sing N N 372 
THR   CG2 HG22 sing N N 373 
THR   CG2 HG23 sing N N 374 
THR   OXT HXT  sing N N 375 
TRP   N   CA   sing N N 376 
TRP   N   H    sing N N 377 
TRP   N   H2   sing N N 378 
TRP   CA  C    sing N N 379 
TRP   CA  CB   sing N N 380 
TRP   CA  HA   sing N N 381 
TRP   C   O    doub N N 382 
TRP   C   OXT  sing N N 383 
TRP   CB  CG   sing N N 384 
TRP   CB  HB2  sing N N 385 
TRP   CB  HB3  sing N N 386 
TRP   CG  CD1  doub Y N 387 
TRP   CG  CD2  sing Y N 388 
TRP   CD1 NE1  sing Y N 389 
TRP   CD1 HD1  sing N N 390 
TRP   CD2 CE2  doub Y N 391 
TRP   CD2 CE3  sing Y N 392 
TRP   NE1 CE2  sing Y N 393 
TRP   NE1 HE1  sing N N 394 
TRP   CE2 CZ2  sing Y N 395 
TRP   CE3 CZ3  doub Y N 396 
TRP   CE3 HE3  sing N N 397 
TRP   CZ2 CH2  doub Y N 398 
TRP   CZ2 HZ2  sing N N 399 
TRP   CZ3 CH2  sing Y N 400 
TRP   CZ3 HZ3  sing N N 401 
TRP   CH2 HH2  sing N N 402 
TRP   OXT HXT  sing N N 403 
TYR   N   CA   sing N N 404 
TYR   N   H    sing N N 405 
TYR   N   H2   sing N N 406 
TYR   CA  C    sing N N 407 
TYR   CA  CB   sing N N 408 
TYR   CA  HA   sing N N 409 
TYR   C   O    doub N N 410 
TYR   C   OXT  sing N N 411 
TYR   CB  CG   sing N N 412 
TYR   CB  HB2  sing N N 413 
TYR   CB  HB3  sing N N 414 
TYR   CG  CD1  doub Y N 415 
TYR   CG  CD2  sing Y N 416 
TYR   CD1 CE1  sing Y N 417 
TYR   CD1 HD1  sing N N 418 
TYR   CD2 CE2  doub Y N 419 
TYR   CD2 HD2  sing N N 420 
TYR   CE1 CZ   doub Y N 421 
TYR   CE1 HE1  sing N N 422 
TYR   CE2 CZ   sing Y N 423 
TYR   CE2 HE2  sing N N 424 
TYR   CZ  OH   sing N N 425 
TYR   OH  HH   sing N N 426 
TYR   OXT HXT  sing N N 427 
VAL   N   CA   sing N N 428 
VAL   N   H    sing N N 429 
VAL   N   H2   sing N N 430 
VAL   CA  C    sing N N 431 
VAL   CA  CB   sing N N 432 
VAL   CA  HA   sing N N 433 
VAL   C   O    doub N N 434 
VAL   C   OXT  sing N N 435 
VAL   CB  CG1  sing N N 436 
VAL   CB  CG2  sing N N 437 
VAL   CB  HB   sing N N 438 
VAL   CG1 HG11 sing N N 439 
VAL   CG1 HG12 sing N N 440 
VAL   CG1 HG13 sing N N 441 
VAL   CG2 HG21 sing N N 442 
VAL   CG2 HG22 sing N N 443 
VAL   CG2 HG23 sing N N 444 
VAL   OXT HXT  sing N N 445 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002345 
_pdbx_deposit_group.group_description   
;XDomainX of XOrganismX None screened against the XXX Fragment Library by X-ray Crystallography at the XChem facility of Diamond Light Source beamline I04-1
;
_pdbx_deposit_group.group_title         
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7IAO 
_atom_sites.fract_transf_matrix[1][1]   0.023742 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.023742 
_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]   0.004626 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
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   1    N  N   . ASP   A 1 7   ? -20.845 18.712  -7.504  1.00 54.74 ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -21.833 17.645  -7.668  1.00 54.89 ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -21.663 16.894  -8.994  1.00 54.07 ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -21.286 17.467  -10.019 1.00 54.18 ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.275 18.178  -7.522  1.00 56.95 ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.235 17.188  -6.880  1.00 63.63 ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.048 17.614  -6.021  1.00 64.43 ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.156 15.976  -7.213  1.00 66.88 ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -21.943 15.597  -8.955  1.00 52.85 ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -21.848 14.741  -10.118 1.00 51.78 ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.221 14.495  -10.717 1.00 50.83 ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.229 14.492  -10.006 1.00 50.56 ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.190 13.410  -9.765  1.00 52.20 ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -19.736 13.538  -9.406  1.00 53.78 ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -18.955 11.914  -9.238  1.00 55.37 ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.250 12.425  -9.033  1.00 55.20 ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.253 14.253  -12.037 1.00 49.87 ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -24.498 14.018  -12.757 1.00 48.91 ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.336 13.030  -13.908 1.00 48.25 ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.215 12.710  -14.285 1.00 47.79 ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.115 15.347  -13.217 1.00 48.36 ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -24.311 16.072  -14.270 1.00 48.57 ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -23.310 16.967  -13.917 1.00 49.22 ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -24.604 15.925  -15.617 1.00 49.32 ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -22.580 17.649  -14.882 1.00 49.99 ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -23.901 16.622  -16.589 1.00 50.11 ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -22.896 17.494  -16.219 1.00 50.65 ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -22.177 18.141  -17.191 1.00 51.66 ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -25.454 12.511  -14.447 1.00 48.26 ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -25.382 11.528  -15.522 1.00 48.66 ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.162 11.944  -16.763 1.00 49.55 ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.211 12.590  -16.671 1.00 50.35 ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -25.766 10.099  -15.048 1.00 48.70 ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.215 10.027  -14.522 1.00 49.66 ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -24.770 9.574   -14.023 1.00 48.66 ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -27.759 8.615   -14.388 1.00 50.54 ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -25.603 11.601  -17.928 1.00 49.40 ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -26.152 11.825  -19.263 1.00 49.51 ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -26.119 10.476  -20.010 1.00 49.37 ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -25.114 9.781   -19.966 1.00 48.51 ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -25.291 12.827  -20.041 1.00 51.79 ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -25.361 14.256  -19.534 1.00 57.83 ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -24.460 15.230  -20.272 1.00 66.29 ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -23.528 14.769  -20.975 1.00 67.47 ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -24.685 16.458  -20.146 1.00 69.14 ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -27.196 10.128  -20.716 1.00 49.47 ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -27.265 8.872   -21.448 1.00 49.25 ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -26.321 8.874   -22.633 1.00 49.77 ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -26.248 9.862   -23.371 1.00 49.82 ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -28.702 8.583   -21.887 1.00 49.59 ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -28.933 7.106   -22.080 1.00 50.50 ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -30.366 6.757   -22.408 1.00 51.93 ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -30.484 5.307   -22.560 1.00 53.31 ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -30.423 4.669   -23.719 1.00 54.52 ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -30.300 5.348   -24.854 1.00 53.93 ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -30.493 3.346   -23.758 1.00 54.18 ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -25.590 7.760   -22.807 1.00 49.69 ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -24.597 7.573   -23.856 1.00 50.10 ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -25.011 6.591   -24.962 1.00 50.37 ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -24.415 6.633   -26.024 1.00 50.63 ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -23.270 7.145   -23.245 1.00 50.20 ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -25.998 5.724   -24.722 1.00 50.23 ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -26.452 4.789   -25.751 1.00 50.26 ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -27.084 3.491   -25.278 1.00 50.52 ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -27.232 3.255   -24.074 1.00 50.22 ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -27.479 2.629   -26.238 1.00 50.57 ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -28.070 1.329   -25.898 1.00 51.11 ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -26.979 0.294   -25.630 1.00 52.54 ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -25.890 0.395   -26.193 1.00 52.69 ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -28.972 0.807   -27.029 1.00 51.06 ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -30.302 1.529   -27.194 1.00 52.36 ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -30.569 2.462   -26.412 1.00 52.84 ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -31.070 1.171   -28.130 1.00 51.39 ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -27.275 -0.725  -24.814 1.00 53.36 ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -26.312 -1.795  -24.563 1.00 54.75 ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -26.646 -2.988  -25.458 1.00 56.57 ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -27.413 -3.867  -25.087 1.00 56.32 ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -26.201 -2.119  -23.058 1.00 55.05 ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -25.738 -0.875  -22.291 1.00 55.69 ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -25.254 -3.273  -22.819 1.00 55.46 ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -25.824 -1.004  -20.809 1.00 56.86 ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -26.103 -2.983  -26.670 0.50 57.76 ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -26.094 -2.984  -26.669 0.50 57.69 ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -26.301 -4.061  -27.640 0.50 59.46 ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -26.349 -4.008  -27.682 0.50 59.34 ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -24.980 -4.440  -28.303 0.50 61.00 ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -25.048 -4.390  -28.413 0.50 61.03 ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -24.064 -3.620  -28.382 0.50 61.16 ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -24.189 -3.529  -28.604 0.50 61.32 ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -27.327 -3.676  -28.731 0.50 60.61 ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -27.441 -3.477  -28.643 0.50 60.25 ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -27.005 -2.392  -29.265 0.50 61.39 ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -28.671 -3.359  -27.926 0.50 61.19 ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -28.763 -3.715  -28.234 0.50 61.00 ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -27.643 -4.351  -29.860 0.50 60.26 ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -24.890 -5.673  -28.801 1.00 61.93 ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -23.706 -6.132  -29.524 1.00 64.49 ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -23.888 -5.697  -30.977 1.00 67.05 ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -24.877 -6.077  -31.607 1.00 67.41 ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -23.601 -7.666  -29.468 1.00 64.39 ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -22.466 -8.257  -30.260 1.00 64.76 ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -22.397 -8.403  -31.615 1.00 65.68 ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -21.304 -8.907  -29.729 1.00 64.77 ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -21.238 -9.056  -31.962 1.00 65.93 ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -20.552 -9.382  -30.821 1.00 65.62 ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -20.821 -9.125  -28.437 1.00 65.08 ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -19.344 -10.058 -30.655 1.00 66.11 ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -19.625 -9.791  -28.277 1.00 65.84 ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -18.891 -10.231 -29.375 1.00 66.01 ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -22.943 -4.918  -31.518 1.00 68.52 ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -23.040 -4.458  -32.901 1.00 70.12 ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -22.209 -5.336  -33.815 1.00 72.01 ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -21.015 -5.505  -33.570 1.00 72.45 ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -22.592 -2.994  -33.038 1.00 72.50 ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -23.190 -2.044  -32.007 1.00 79.52 ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -24.693 -1.812  -32.007 1.00 87.54 ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -25.334 -1.988  -33.071 1.00 87.90 ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -25.226 -1.429  -30.938 1.00 90.69 ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -22.827 -5.907  -34.862 1.00 72.84 ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -22.088 -6.744  -35.806 1.00 74.41 ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -21.235 -5.860  -36.699 1.00 75.55 ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -21.624 -4.729  -37.016 1.00 75.86 ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -23.039 -7.587  -36.666 1.00 76.82 ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -23.982 -8.466  -35.854 1.00 82.11 ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -25.032 -9.155  -36.739 1.00 86.80 ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -25.997 -9.990  -35.925 1.00 90.69 ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -27.307 -10.150 -36.611 1.00 93.14 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -20.076 -6.370  -37.108 1.00 76.10 ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -19.147 -5.613  -37.948 1.00 77.35 ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -18.652 -4.370  -37.200 1.00 77.55 ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -18.795 -3.239  -37.666 1.00 77.72 ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -19.738 -5.250  -39.336 1.00 80.05 ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -20.316 -6.413  -40.132 1.00 85.65 ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -19.639 -7.468  -40.228 1.00 86.59 ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -21.439 -6.263  -40.671 1.00 87.97 ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -18.138 -4.597  -35.998 1.00 77.24 ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -17.556 -3.557  -35.157 1.00 77.21 ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -16.024 -3.644  -35.280 1.00 77.05 ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -15.510 -4.668  -35.738 1.00 77.16 ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -17.976 -3.783  -33.714 1.00 77.34 ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -15.283 -2.592  -34.883 1.00 76.84 ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -13.811 -2.632  -34.948 1.00 77.08 ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -13.261 -3.785  -34.095 1.00 76.48 ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -13.498 -3.811  -32.895 1.00 76.85 ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -13.185 -1.300  -34.494 1.00 79.54 ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -11.665 -1.317  -34.540 1.00 85.15 ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -10.969 -0.078  -34.014 1.00 93.09 ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -11.666 0.829   -33.505 1.00 95.28 ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -9.722  -0.013  -34.109 1.00 95.34 ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -12.595 -4.760  -34.718 1.00 75.42 ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -12.044 -5.901  -33.992 1.00 74.78 ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -10.553 -5.671  -33.764 1.00 74.17 ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -9.759  -5.868  -34.674 1.00 74.59 ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -12.295 -7.267  -34.691 1.00 75.25 ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -12.101 -8.411  -33.713 1.00 75.86 ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -13.682 -7.346  -35.320 1.00 75.54 ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -10.171 -5.232  -32.571 1.00 73.30 ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -8.766  -4.974  -32.243 1.00 72.89 ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -8.455  -5.360  -30.784 1.00 71.77 ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -9.371  -5.569  -29.991 1.00 71.85 ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -8.434  -3.495  -32.513 1.00 74.35 ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -7.063  -3.261  -32.183 1.00 75.58 ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -9.297  -2.562  -31.703 1.00 74.48 ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -7.175  -5.454  -30.441 1.00 70.61 ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -6.771  -5.782  -29.082 1.00 70.24 ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -6.138  -7.145  -28.909 1.00 69.67 ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -6.432  -8.087  -29.647 1.00 69.61 ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -5.284  -7.266  -27.898 1.00 69.14 ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -4.607  -8.524  -27.618 1.00 68.56 ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -5.212  -9.268  -26.389 1.00 66.44 ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -6.145  -8.780  -25.756 1.00 66.00 ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -3.082  -8.313  -27.520 1.00 70.75 ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -2.638  -7.201  -26.605 1.00 75.54 ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.041  -6.038  -26.743 1.00 77.33 ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -1.762  -7.535  -25.666 1.00 76.70 ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -4.735  -10.491 -26.130 1.00 65.23 ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -5.177  -11.357 -25.042 1.00 64.78 ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -3.964  -11.735 -24.149 1.00 64.30 ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -3.503  -12.880 -24.192 1.00 64.71 ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -5.816  -12.630 -25.604 1.00 65.83 ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -6.422  -12.491 -26.878 1.00 67.98 ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -3.401  -10.797 -23.361 1.00 63.47 ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -2.223  -11.141 -22.548 1.00 63.29 ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -2.547  -11.981 -21.316 1.00 63.20 ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -3.648  -11.879 -20.796 1.00 63.36 ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -1.693  -9.770  -22.129 1.00 63.88 ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -2.904  -8.925  -22.046 1.00 64.11 ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -3.786  -9.384  -23.173 1.00 62.82 ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -1.592  -12.798 -20.833 1.00 62.57 ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -1.807  -13.578 -19.616 1.00 62.48 ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -0.830  -13.098 -18.573 1.00 61.51 ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? 0.365   -13.377 -18.649 1.00 61.72 ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -1.745  -15.082 -19.866 1.00 64.68 ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -2.845  -15.508 -20.822 1.00 69.76 ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -3.136  -16.990 -20.801 1.00 74.86 ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -3.891  -17.379 -21.993 1.00 79.69 ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -4.427  -18.580 -22.185 1.00 83.08 ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -4.326  -19.519 -21.246 1.00 84.00 ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -5.081  -18.850 -23.308 1.00 81.97 ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -1.343  -12.291 -17.643 1.00 60.24 ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -0.550  -11.607 -16.634 1.00 59.37 ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -0.764  -12.119 -15.228 1.00 58.59 ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -1.897  -12.359 -14.831 1.00 58.41 ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -0.896  -10.104 -16.657 1.00 59.06 ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -0.929  -9.422  -18.023 1.00 59.54 ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -1.498  -8.028  -17.910 1.00 60.19 ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? 0.438   -9.383  -18.638 1.00 59.61 ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? 0.324   -12.208 -14.453 1.00 58.03 ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? 0.296   -12.579 -13.037 1.00 58.10 ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? 0.112   -11.262 -12.261 1.00 57.33 ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? 0.990   -10.407 -12.329 1.00 57.76 ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 1.641   -13.229 -12.636 1.00 60.37 ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 1.791   -14.691 -13.029 1.00 66.45 ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? 0.798   -15.287 -13.501 1.00 67.35 ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 2.899   -15.249 -12.836 1.00 69.51 ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -1.023  -11.063 -11.578 1.00 56.24 ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -1.265  -9.803  -10.851 1.00 55.96 ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -1.634  -10.006 -9.366  1.00 55.23 ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.002  -11.108 -8.978  1.00 55.44 ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -2.353  -8.973  -11.574 1.00 56.56 ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -1.844  -8.414  -12.898 1.00 56.45 ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -3.610  -9.806  -11.778 1.00 57.18 ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -1.549  -8.939  -8.541  1.00 54.40 ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -1.938  -8.974  -7.124  1.00 54.18 ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -2.922  -7.840  -6.808  1.00 53.44 ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -2.727  -6.723  -7.268  1.00 53.56 ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -0.716  -8.877  -6.216  1.00 54.27 ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -3.971  -8.117  -6.029  1.00 52.54 ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -4.977  -7.106  -5.690  1.00 51.83 ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -4.854  -6.740  -4.212  1.00 52.26 ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.015  -7.600  -3.350  1.00 52.61 ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -6.382  -7.650  -6.020  1.00 51.10 ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -7.579  -6.767  -5.693  1.00 51.01 ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -7.505  -5.459  -6.415  1.00 51.19 ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -8.883  -7.474  -6.007  1.00 50.83 ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -4.518  -5.473  -3.915  1.00 52.14 ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -4.334  -5.017  -2.538  1.00 52.12 ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -5.684  -4.651  -1.870  1.00 52.44 ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -6.737  -4.776  -2.498  1.00 52.26 ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.265  -3.887  -2.444  1.00 52.62 ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -3.670  -2.495  -2.916  1.00 54.55 ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -4.850  -2.310  -3.279  1.00 54.59 ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -2.803  -1.584  -2.905  1.00 54.93 ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -5.647  -4.228  -0.594  1.00 52.69 ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -6.846  -3.872  0.151   1.00 53.63 ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -7.542  -2.626  -0.360  1.00 54.00 ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -8.739  -2.488  -0.156  1.00 54.45 ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -6.568  -3.760  1.649   1.00 56.20 ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -7.669  -4.405  2.466   1.00 61.54 ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.553  -4.233  3.965   1.00 67.09 ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.180  -3.125  4.417   1.00 67.87 ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.850  -5.209  4.690   1.00 69.45 ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -6.822  -1.735  -1.047  1.00 53.38 ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.431  -0.543  -1.628  1.00 52.88 ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.035  -0.783  -3.021  1.00 52.19 ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.372  0.185   -3.696  1.00 52.45 ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.417  0.589   -1.699  1.00 54.53 ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -5.812  0.789   -0.434  1.00 57.44 ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.177  -2.042  -3.441  1.00 51.21 ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -8.741  -2.370  -4.744  1.00 50.82 ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -7.807  -2.081  -5.904  1.00 50.46 ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.255  -1.916  -7.043  1.00 50.38 ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.489  -2.032  -5.628  1.00 49.92 ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -5.490  -1.754  -6.649  1.00 49.70 ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -4.765  -3.012  -7.088  1.00 49.58 ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.323  -3.819  -6.265  1.00 49.61 ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.465  -0.699  -6.175  1.00 50.59 ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.039  0.678   -5.939  1.00 53.80 ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.161  0.933   -6.394  1.00 53.79 ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -4.346  1.513   -5.313  1.00 56.51 ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -4.630  -3.158  -8.396  1.00 49.04 ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -3.920  -4.252  -9.013  1.00 49.01 ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -2.484  -3.828  -9.276  1.00 50.69 ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.202  -2.649  -9.519  1.00 51.06 ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -4.567  -4.600  -10.346 1.00 47.63 ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -5.869  -5.363  -10.290 1.00 46.62 ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -5.879  -6.729  -10.068 1.00 46.42 ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.067  -4.741  -10.598 1.00 46.30 ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -7.073  -7.442  -10.084 1.00 46.44 ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -8.256  -5.459  -10.614 1.00 46.23 ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -8.253  -6.801  -10.346 1.00 45.74 ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -1.577  -4.799  -9.252  1.00 51.50 ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -0.169  -4.574  -9.537  1.00 52.80 ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? 0.425   -5.838  -10.142 1.00 54.07 ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? 0.027   -6.934  -9.762  1.00 54.13 ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? 0.585   -4.155  -8.280  1.00 54.42 ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? 0.733   -5.218  -7.356  1.00 57.39 ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 1.347   -5.696  -11.106 1.00 54.96 ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.948   -6.863  -11.751 1.00 56.44 ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.977   -7.576  -10.875 1.00 56.73 ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 3.835   -6.928  -10.284 1.00 57.07 ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.547   -6.502  -13.115 1.00 57.52 ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 2.131   -7.417  -14.265 1.00 60.03 ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 1.949   -6.634  -15.535 1.00 60.89 ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 3.123   -8.565  -14.456 1.00 61.14 ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 2.903   -8.915  -10.826 1.00 56.43 ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 3.769   -9.772  -10.024 1.00 57.00 ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 5.040   -10.243 -10.765 1.00 57.49 ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 5.142   -10.120 -11.987 1.00 57.98 ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 2.941   -10.952 -9.472  1.00 57.69 ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 3.827   -11.997 -8.816  1.00 58.14 ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 1.879   -10.454 -8.496  1.00 58.19 ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   B 2 8   ? -34.000 10.158  -14.973 1.00 66.78 ? 17  GLU   B N   1 
ATOM   304  C  CA  . GLU   B 2 8   ? -34.043 9.147   -16.032 1.00 67.39 ? 17  GLU   B CA  1 
ATOM   305  C  C   . GLU   B 2 8   ? -33.590 7.752   -15.567 1.00 66.79 ? 17  GLU   B C   1 
ATOM   306  O  O   . GLU   B 2 8   ? -32.412 7.513   -15.298 1.00 67.30 ? 17  GLU   B O   1 
ATOM   307  C  CB  . GLU   B 2 8   ? -33.264 9.597   -17.278 1.00 70.60 ? 17  GLU   B CB  1 
ATOM   308  C  CG  . GLU   B 2 8   ? -33.325 8.604   -18.427 1.00 77.28 ? 17  GLU   B CG  1 
ATOM   309  C  CD  . GLU   B 2 8   ? -32.522 8.998   -19.652 1.00 85.57 ? 17  GLU   B CD  1 
ATOM   310  O  OE1 . GLU   B 2 8   ? -31.461 9.643   -19.489 1.00 86.94 ? 17  GLU   B OE1 1 
ATOM   311  O  OE2 . GLU   B 2 8   ? -32.957 8.665   -20.779 1.00 88.60 ? 17  GLU   B OE2 1 
ATOM   312  N  N   . THR   B 2 9   ? -34.547 6.837   -15.479 1.00 65.47 ? 18  THR   B N   1 
ATOM   313  C  CA  . THR   B 2 9   ? -34.324 5.451   -15.064 1.00 64.33 ? 18  THR   B CA  1 
ATOM   314  C  C   . THR   B 2 9   ? -34.194 4.479   -16.239 1.00 61.82 ? 18  THR   B C   1 
ATOM   315  O  O   . THR   B 2 9   ? -34.227 3.266   -16.026 1.00 61.74 ? 18  THR   B O   1 
ATOM   316  C  CB  . THR   B 2 9   ? -35.512 5.000   -14.213 1.00 66.51 ? 18  THR   B CB  1 
ATOM   317  O  OG1 . THR   B 2 9   ? -36.724 5.247   -14.951 1.00 67.53 ? 18  THR   B OG1 1 
ATOM   318  C  CG2 . THR   B 2 9   ? -35.548 5.691   -12.854 1.00 67.15 ? 18  THR   B CG2 1 
ATOM   319  N  N   . THR   B 2 10  ? -34.070 5.003   -17.466 1.00 59.82 ? 19  THR   B N   1 
ATOM   320  C  CA  . THR   B 2 10  ? -33.990 4.246   -18.704 1.00 58.18 ? 19  THR   B CA  1 
ATOM   321  C  C   . THR   B 2 10  ? -32.775 3.344   -18.760 1.00 55.73 ? 19  THR   B C   1 
ATOM   322  O  O   . THR   B 2 10  ? -31.662 3.779   -18.470 1.00 55.41 ? 19  THR   B O   1 
ATOM   323  C  CB  . THR   B 2 10  ? -34.032 5.224   -19.887 1.00 60.27 ? 19  THR   B CB  1 
ATOM   324  O  OG1 . THR   B 2 10  ? -35.215 6.021   -19.773 1.00 62.34 ? 19  THR   B OG1 1 
ATOM   325  C  CG2 . THR   B 2 10  ? -34.003 4.526   -21.240 1.00 60.47 ? 19  THR   B CG2 1 
ATOM   326  N  N   . ASP   B 2 11  ? -32.988 2.078   -19.149 1.00 53.69 ? 20  ASP   B N   1 
ATOM   327  C  CA  . ASP   B 2 11  ? -31.925 1.096   -19.339 1.00 51.94 ? 20  ASP   B CA  1 
ATOM   328  C  C   . ASP   B 2 11  ? -30.936 1.619   -20.393 1.00 49.77 ? 20  ASP   B C   1 
ATOM   329  O  O   . ASP   B 2 11  ? -31.359 2.224   -21.369 1.00 49.91 ? 20  ASP   B O   1 
ATOM   330  C  CB  . ASP   B 2 11  ? -32.526 -0.231  -19.842 1.00 53.63 ? 20  ASP   B CB  1 
ATOM   331  C  CG  . ASP   B 2 11  ? -32.768 -1.282  -18.780 1.00 57.45 ? 20  ASP   B CG  1 
ATOM   332  O  OD1 . ASP   B 2 11  ? -33.202 -0.912  -17.665 1.00 57.94 ? 20  ASP   B OD1 1 
ATOM   333  O  OD2 . ASP   B 2 11  ? -32.527 -2.484  -19.067 1.00 58.72 ? 20  ASP   B OD2 1 
ATOM   334  N  N   . GLY   B 2 12  ? -29.645 1.420   -20.171 1.00 47.63 ? 21  GLY   B N   1 
ATOM   335  C  CA  . GLY   B 2 12  ? -28.633 1.860   -21.121 1.00 45.89 ? 21  GLY   B CA  1 
ATOM   336  C  C   . GLY   B 2 12  ? -27.338 2.312   -20.493 1.00 43.93 ? 21  GLY   B C   1 
ATOM   337  O  O   . GLY   B 2 12  ? -27.215 2.312   -19.272 1.00 43.39 ? 21  GLY   B O   1 
ATOM   338  N  N   . VAL   B 2 13  ? -26.344 2.677   -21.324 1.00 42.81 ? 22  VAL   B N   1 
ATOM   339  C  CA  . VAL   B 2 13  ? -25.057 3.146   -20.803 1.00 42.13 ? 22  VAL   B CA  1 
ATOM   340  C  C   . VAL   B 2 13  ? -25.086 4.670   -20.586 1.00 40.90 ? 22  VAL   B C   1 
ATOM   341  O  O   . VAL   B 2 13  ? -25.741 5.378   -21.348 1.00 39.91 ? 22  VAL   B O   1 
ATOM   342  C  CB  . VAL   B 2 13  ? -23.850 2.671   -21.655 1.00 42.92 ? 22  VAL   B CB  1 
ATOM   343  C  CG1 . VAL   B 2 13  ? -23.961 3.117   -23.113 1.00 42.69 ? 22  VAL   B CG1 1 
ATOM   344  C  CG2 . VAL   B 2 13  ? -22.524 3.119   -21.040 1.00 43.56 ? 22  VAL   B CG2 1 
ATOM   345  N  N   . TYR   B 2 14  ? -24.473 5.155   -19.487 1.00 40.36 ? 23  TYR   B N   1 
ATOM   346  C  CA  . TYR   B 2 14  ? -24.460 6.577   -19.149 1.00 40.08 ? 23  TYR   B CA  1 
ATOM   347  C  C   . TYR   B 2 14  ? -23.056 7.133   -18.906 1.00 41.46 ? 23  TYR   B C   1 
ATOM   348  O  O   . TYR   B 2 14  ? -22.151 6.417   -18.487 1.00 42.07 ? 23  TYR   B O   1 
ATOM   349  C  CB  . TYR   B 2 14  ? -25.306 6.831   -17.888 1.00 38.81 ? 23  TYR   B CB  1 
ATOM   350  C  CG  . TYR   B 2 14  ? -26.792 6.684   -18.111 1.00 38.07 ? 23  TYR   B CG  1 
ATOM   351  C  CD1 . TYR   B 2 14  ? -27.357 5.444   -18.355 1.00 38.03 ? 23  TYR   B CD1 1 
ATOM   352  C  CD2 . TYR   B 2 14  ? -27.635 7.779   -18.049 1.00 38.60 ? 23  TYR   B CD2 1 
ATOM   353  C  CE1 . TYR   B 2 14  ? -28.697 5.311   -18.653 1.00 38.53 ? 23  TYR   B CE1 1 
ATOM   354  C  CE2 . TYR   B 2 14  ? -28.986 7.657   -18.319 1.00 39.46 ? 23  TYR   B CE2 1 
ATOM   355  C  CZ  . TYR   B 2 14  ? -29.520 6.412   -18.594 1.00 40.04 ? 23  TYR   B CZ  1 
ATOM   356  O  OH  . TYR   B 2 14  ? -30.870 6.244   -18.773 1.00 41.69 ? 23  TYR   B OH  1 
ATOM   357  N  N   . ARG   B 2 15  ? -22.899 8.434   -19.123 1.00 41.75 ? 24  ARG   B N   1 
ATOM   358  C  CA  . ARG   B 2 15  ? -21.685 9.181   -18.832 1.00 42.20 ? 24  ARG   B CA  1 
ATOM   359  C  C   . ARG   B 2 15  ? -21.774 9.703   -17.405 1.00 42.55 ? 24  ARG   B C   1 
ATOM   360  O  O   . ARG   B 2 15  ? -22.820 10.220  -17.024 1.00 42.49 ? 24  ARG   B O   1 
ATOM   361  C  CB  . ARG   B 2 15  ? -21.608 10.412  -19.734 1.00 42.82 ? 24  ARG   B CB  1 
ATOM   362  C  CG  . ARG   B 2 15  ? -21.292 10.135  -21.166 1.00 44.21 ? 24  ARG   B CG  1 
ATOM   363  C  CD  . ARG   B 2 15  ? -20.956 11.446  -21.824 1.00 47.36 ? 24  ARG   B CD  1 
ATOM   364  N  NE  . ARG   B 2 15  ? -21.143 11.363  -23.269 1.00 50.26 ? 24  ARG   B NE  1 
ATOM   365  C  CZ  . ARG   B 2 15  ? -20.186 11.051  -24.132 1.00 51.40 ? 24  ARG   B CZ  1 
ATOM   366  N  NH1 . ARG   B 2 15  ? -18.942 10.834  -23.708 1.00 49.91 ? 24  ARG   B NH1 1 
ATOM   367  N  NH2 . ARG   B 2 15  ? -20.456 10.976  -25.427 1.00 51.40 ? 24  ARG   B NH2 1 
ATOM   368  N  N   . VAL   B 2 16  ? -20.683 9.633   -16.637 1.00 43.08 ? 25  VAL   B N   1 
ATOM   369  C  CA  . VAL   B 2 16  ? -20.637 10.194  -15.276 1.00 44.48 ? 25  VAL   B CA  1 
ATOM   370  C  C   . VAL   B 2 16  ? -19.848 11.505  -15.352 1.00 45.57 ? 25  VAL   B C   1 
ATOM   371  O  O   . VAL   B 2 16  ? -18.651 11.489  -15.627 1.00 45.55 ? 25  VAL   B O   1 
ATOM   372  C  CB  . VAL   B 2 16  ? -20.056 9.234   -14.205 1.00 44.70 ? 25  VAL   B CB  1 
ATOM   373  C  CG1 . VAL   B 2 16  ? -20.154 9.860   -12.821 1.00 44.63 ? 25  VAL   B CG1 1 
ATOM   374  C  CG2 . VAL   B 2 16  ? -20.769 7.888   -14.234 1.00 45.06 ? 25  VAL   B CG2 1 
ATOM   375  N  N   . MET   B 2 17  ? -20.530 12.633  -15.158 1.00 46.29 ? 26  MET   B N   1 
ATOM   376  C  CA  . MET   B 2 17  ? -19.934 13.949  -15.326 1.00 47.75 ? 26  MET   B CA  1 
ATOM   377  C  C   . MET   B 2 17  ? -19.793 14.727  -14.044 1.00 50.35 ? 26  MET   B C   1 
ATOM   378  O  O   . MET   B 2 17  ? -20.584 14.539  -13.128 1.00 50.62 ? 26  MET   B O   1 
ATOM   379  C  CB  . MET   B 2 17  ? -20.824 14.768  -16.275 1.00 47.55 ? 26  MET   B CB  1 
ATOM   380  C  CG  . MET   B 2 17  ? -21.109 14.086  -17.588 1.00 47.85 ? 26  MET   B CG  1 
ATOM   381  S  SD  . MET   B 2 17  ? -19.631 13.985  -18.616 1.00 45.70 ? 26  MET   B SD  1 
ATOM   382  C  CE  . MET   B 2 17  ? -19.401 15.681  -19.012 1.00 39.52 ? 26  MET   B CE  1 
ATOM   383  N  N   . THR   B 2 18  ? -18.839 15.662  -13.997 1.00 52.29 ? 27  THR   B N   1 
ATOM   384  C  CA  . THR   B 2 18  ? -18.694 16.542  -12.847 1.00 54.84 ? 27  THR   B CA  1 
ATOM   385  C  C   . THR   B 2 18  ? -18.508 17.999  -13.261 1.00 57.86 ? 27  THR   B C   1 
ATOM   386  O  O   . THR   B 2 18  ? -17.995 18.290  -14.347 1.00 57.84 ? 27  THR   B O   1 
ATOM   387  C  CB  . THR   B 2 18  ? -17.615 16.079  -11.869 1.00 55.96 ? 27  THR   B CB  1 
ATOM   388  O  OG1 . THR   B 2 18  ? -17.905 16.655  -10.588 1.00 57.49 ? 27  THR   B OG1 1 
ATOM   389  C  CG2 . THR   B 2 18  ? -16.216 16.469  -12.310 1.00 55.84 ? 27  THR   B CG2 1 
ATOM   390  N  N   . ARG   B 2 19  ? -18.929 18.920  -12.389 1.00 60.13 ? 28  ARG   B N   1 
ATOM   391  C  CA  . ARG   B 2 19  ? -18.741 20.342  -12.646 1.00 62.70 ? 28  ARG   B CA  1 
ATOM   392  C  C   . ARG   B 2 19  ? -17.754 21.004  -11.638 1.00 64.24 ? 28  ARG   B C   1 
ATOM   393  O  O   . ARG   B 2 19  ? -17.532 22.216  -11.719 1.00 64.89 ? 28  ARG   B O   1 
ATOM   394  C  CB  . ARG   B 2 19  ? -20.089 21.072  -12.734 1.00 65.23 ? 28  ARG   B CB  1 
ATOM   395  C  CG  . ARG   B 2 19  ? -20.702 20.992  -14.136 1.00 70.58 ? 28  ARG   B CG  1 
ATOM   396  C  CD  . ARG   B 2 19  ? -22.104 21.578  -14.199 1.00 75.66 ? 28  ARG   B CD  1 
ATOM   397  N  NE  . ARG   B 2 19  ? -22.682 21.503  -15.544 1.00 80.13 ? 28  ARG   B NE  1 
ATOM   398  C  CZ  . ARG   B 2 19  ? -23.830 20.895  -15.840 1.00 83.07 ? 28  ARG   B CZ  1 
ATOM   399  N  NH1 . ARG   B 2 19  ? -24.533 20.287  -14.891 1.00 82.99 ? 28  ARG   B NH1 1 
ATOM   400  N  NH2 . ARG   B 2 19  ? -24.279 20.884  -17.090 1.00 82.98 ? 28  ARG   B NH2 1 
ATOM   401  N  N   . ARG   B 2 20  ? -17.111 20.193  -10.757 1.00 64.64 ? 29  ARG   B N   1 
ATOM   402  C  CA  . ARG   B 2 20  ? -16.147 20.617  -9.737  1.00 65.79 ? 29  ARG   B CA  1 
ATOM   403  C  C   . ARG   B 2 20  ? -14.823 21.079  -10.354 1.00 65.52 ? 29  ARG   B C   1 
ATOM   404  O  O   . ARG   B 2 20  ? -14.238 22.071  -9.911  1.00 65.88 ? 29  ARG   B O   1 
ATOM   405  C  CB  . ARG   B 2 20  ? -15.891 19.461  -8.751  1.00 68.64 ? 29  ARG   B CB  1 
ATOM   406  C  CG  . ARG   B 2 20  ? -15.116 19.874  -7.499  1.00 74.52 ? 29  ARG   B CG  1 
ATOM   407  C  CD  . ARG   B 2 20  ? -14.725 18.687  -6.626  1.00 79.78 ? 29  ARG   B CD  1 
ATOM   408  N  NE  . ARG   B 2 20  ? -13.721 17.827  -7.264  1.00 84.31 ? 29  ARG   B NE  1 
ATOM   409  C  CZ  . ARG   B 2 20  ? -12.406 17.967  -7.113  1.00 87.41 ? 29  ARG   B CZ  1 
ATOM   410  N  NH1 . ARG   B 2 20  ? -11.918 18.936  -6.345  1.00 87.86 ? 29  ARG   B NH1 1 
ATOM   411  N  NH2 . ARG   B 2 20  ? -11.569 17.136  -7.723  1.00 87.08 ? 29  ARG   B NH2 1 
ATOM   412  N  N   . LEU   B 2 21  ? -14.350 20.356  -11.371 1.00 64.68 ? 30  LEU   B N   1 
ATOM   413  C  CA  . LEU   B 2 21  ? -13.109 20.674  -12.077 1.00 64.40 ? 30  LEU   B CA  1 
ATOM   414  C  C   . LEU   B 2 21  ? -13.374 21.736  -13.188 1.00 63.91 ? 30  LEU   B C   1 
ATOM   415  O  O   . LEU   B 2 21  ? -14.454 22.350  -13.198 1.00 64.65 ? 30  LEU   B O   1 
ATOM   416  C  CB  . LEU   B 2 21  ? -12.494 19.376  -12.646 1.00 64.67 ? 30  LEU   B CB  1 
ATOM   417  C  CG  . LEU   B 2 21  ? -11.829 18.451  -11.627 1.00 66.46 ? 30  LEU   B CG  1 
ATOM   418  C  CD1 . LEU   B 2 21  ? -12.809 17.455  -11.074 1.00 67.09 ? 30  LEU   B CD1 1 
ATOM   419  C  CD2 . LEU   B 2 21  ? -10.683 17.687  -12.250 1.00 67.26 ? 30  LEU   B CD2 1 
ATOM   420  N  N   . LEU   B 2 22  ? -12.401 21.987  -14.093 1.00 62.30 ? 31  LEU   B N   1 
ATOM   421  C  CA  . LEU   B 2 22  ? -12.603 22.965  -15.165 1.00 61.28 ? 31  LEU   B CA  1 
ATOM   422  C  C   . LEU   B 2 22  ? -13.689 22.468  -16.112 1.00 60.12 ? 31  LEU   B C   1 
ATOM   423  O  O   . LEU   B 2 22  ? -13.653 21.297  -16.490 1.00 60.26 ? 31  LEU   B O   1 
ATOM   424  C  CB  . LEU   B 2 22  ? -11.303 23.169  -15.942 1.00 60.88 ? 31  LEU   B CB  1 
ATOM   425  C  CG  . LEU   B 2 22  ? -11.387 24.205  -17.020 1.00 61.14 ? 31  LEU   B CG  1 
ATOM   426  C  CD1 . LEU   B 2 22  ? -10.921 25.543  -16.508 1.00 61.04 ? 31  LEU   B CD1 1 
ATOM   427  C  CD2 . LEU   B 2 22  ? -10.630 23.759  -18.233 1.00 61.61 ? 31  LEU   B CD2 1 
ATOM   428  N  N   . GLY   B 2 23  ? -14.654 23.337  -16.437 1.00 58.76 ? 32  GLY   B N   1 
ATOM   429  C  CA  . GLY   B 2 23  ? -15.783 23.024  -17.313 1.00 58.28 ? 32  GLY   B CA  1 
ATOM   430  C  C   . GLY   B 2 23  ? -16.552 21.776  -16.924 1.00 57.67 ? 32  GLY   B C   1 
ATOM   431  O  O   . GLY   B 2 23  ? -16.631 21.449  -15.743 1.00 58.08 ? 32  GLY   B O   1 
ATOM   432  N  N   . SER   B 2 24  ? -17.095 21.046  -17.904 1.00 56.78 ? 33  SER   B N   1 
ATOM   433  C  CA  . SER   B 2 24  ? -17.787 19.784  -17.626 1.00 56.69 ? 33  SER   B CA  1 
ATOM   434  C  C   . SER   B 2 24  ? -16.825 18.632  -17.913 1.00 55.14 ? 33  SER   B C   1 
ATOM   435  O  O   . SER   B 2 24  ? -16.552 18.339  -19.072 1.00 54.53 ? 33  SER   B O   1 
ATOM   436  C  CB  . SER   B 2 24  ? -19.034 19.642  -18.494 1.00 59.26 ? 33  SER   B CB  1 
ATOM   437  O  OG  . SER   B 2 24  ? -20.208 20.070  -17.818 1.00 62.90 ? 33  SER   B OG  1 
ATOM   438  N  N   . THR   B 2 25  ? -16.287 17.992  -16.862 1.00 54.28 ? 34  THR   B N   1 
ATOM   439  C  CA  . THR   B 2 25  ? -15.329 16.895  -17.044 1.00 53.32 ? 34  THR   B CA  1 
ATOM   440  C  C   . THR   B 2 25  ? -15.988 15.535  -16.860 1.00 51.42 ? 34  THR   B C   1 
ATOM   441  O  O   . THR   B 2 25  ? -16.726 15.348  -15.901 1.00 51.79 ? 34  THR   B O   1 
ATOM   442  C  CB  . THR   B 2 25  ? -14.130 17.070  -16.083 1.00 55.02 ? 34  THR   B CB  1 
ATOM   443  O  OG1 . THR   B 2 25  ? -13.473 18.315  -16.353 1.00 56.22 ? 34  THR   B OG1 1 
ATOM   444  C  CG2 . THR   B 2 25  ? -13.131 15.922  -16.156 1.00 55.32 ? 34  THR   B CG2 1 
ATOM   445  N  N   . GLN   B 2 26  ? -15.724 14.585  -17.768 1.00 49.45 ? 35  GLN   B N   1 
ATOM   446  C  CA  . GLN   B 2 26  ? -16.247 13.233  -17.621 1.00 47.98 ? 35  GLN   B CA  1 
ATOM   447  C  C   . GLN   B 2 26  ? -15.291 12.474  -16.732 1.00 47.08 ? 35  GLN   B C   1 
ATOM   448  O  O   . GLN   B 2 26  ? -14.112 12.352  -17.068 1.00 47.14 ? 35  GLN   B O   1 
ATOM   449  C  CB  . GLN   B 2 26  ? -16.371 12.524  -18.976 1.00 48.34 ? 35  GLN   B CB  1 
ATOM   450  C  CG  . GLN   B 2 26  ? -16.864 11.081  -18.886 1.00 49.43 ? 35  GLN   B CG  1 
ATOM   451  C  CD  . GLN   B 2 26  ? -17.149 10.489  -20.250 1.00 50.76 ? 35  GLN   B CD  1 
ATOM   452  O  OE1 . GLN   B 2 26  ? -17.730 11.132  -21.125 1.00 51.54 ? 35  GLN   B OE1 1 
ATOM   453  N  NE2 . GLN   B 2 26  ? -16.762 9.244   -20.460 1.00 49.71 ? 35  GLN   B NE2 1 
ATOM   454  N  N   . VAL   B 2 27  ? -15.780 11.996  -15.578 1.00 45.85 ? 36  VAL   B N   1 
ATOM   455  C  CA  . VAL   B 2 27  ? -14.958 11.226  -14.657 1.00 45.00 ? 36  VAL   B CA  1 
ATOM   456  C  C   . VAL   B 2 27  ? -15.063 9.711   -14.881 1.00 43.71 ? 36  VAL   B C   1 
ATOM   457  O  O   . VAL   B 2 27  ? -14.185 8.959   -14.446 1.00 43.22 ? 36  VAL   B O   1 
ATOM   458  C  CB  . VAL   B 2 27  ? -15.246 11.612  -13.181 1.00 46.10 ? 36  VAL   B CB  1 
ATOM   459  C  CG1 . VAL   B 2 27  ? -15.011 13.095  -12.955 1.00 46.79 ? 36  VAL   B CG1 1 
ATOM   460  C  CG2 . VAL   B 2 27  ? -16.660 11.228  -12.761 1.00 46.70 ? 36  VAL   B CG2 1 
ATOM   461  N  N   . GLY   B 2 28  ? -16.143 9.267   -15.516 1.00 42.97 ? 37  GLY   B N   1 
ATOM   462  C  CA  . GLY   B 2 28  ? -16.358 7.845   -15.733 1.00 42.87 ? 37  GLY   B CA  1 
ATOM   463  C  C   . GLY   B 2 28  ? -17.609 7.530   -16.514 1.00 42.31 ? 37  GLY   B C   1 
ATOM   464  O  O   . GLY   B 2 28  ? -18.192 8.413   -17.147 1.00 42.71 ? 37  GLY   B O   1 
ATOM   465  N  N   . VAL   B 2 29  ? -18.016 6.259   -16.482 1.00 41.06 ? 38  VAL   B N   1 
ATOM   466  C  CA  . VAL   B 2 29  ? -19.153 5.694   -17.222 1.00 40.58 ? 38  VAL   B CA  1 
ATOM   467  C  C   . VAL   B 2 29  ? -19.918 4.711   -16.304 1.00 40.30 ? 38  VAL   B C   1 
ATOM   468  O  O   . VAL   B 2 29  ? -19.372 4.248   -15.308 1.00 40.07 ? 38  VAL   B O   1 
ATOM   469  C  CB  . VAL   B 2 29  ? -18.609 4.963   -18.487 1.00 40.61 ? 38  VAL   B CB  1 
ATOM   470  C  CG1 . VAL   B 2 29  ? -19.718 4.325   -19.299 1.00 40.95 ? 38  VAL   B CG1 1 
ATOM   471  C  CG2 . VAL   B 2 29  ? -17.774 5.892   -19.354 1.00 40.74 ? 38  VAL   B CG2 1 
ATOM   472  N  N   . GLY   B 2 30  ? -21.168 4.411   -16.639 1.00 40.03 ? 39  GLY   B N   1 
ATOM   473  C  CA  . GLY   B 2 30  ? -21.968 3.482   -15.859 1.00 39.97 ? 39  GLY   B CA  1 
ATOM   474  C  C   . GLY   B 2 30  ? -23.103 2.823   -16.613 1.00 39.58 ? 39  GLY   B C   1 
ATOM   475  O  O   . GLY   B 2 30  ? -23.417 3.207   -17.731 1.00 39.10 ? 39  GLY   B O   1 
ATOM   476  N  N   . VAL   B 2 31  ? -23.752 1.830   -15.993 1.00 39.47 ? 40  VAL   B N   1 
ATOM   477  C  CA  . VAL   B 2 31  ? -24.831 1.079   -16.630 1.00 39.30 ? 40  VAL   B CA  1 
ATOM   478  C  C   . VAL   B 2 31  ? -26.133 1.152   -15.839 1.00 39.32 ? 40  VAL   B C   1 
ATOM   479  O  O   . VAL   B 2 31  ? -26.162 0.812   -14.658 1.00 39.49 ? 40  VAL   B O   1 
ATOM   480  C  CB  . VAL   B 2 31  ? -24.359 -0.379  -16.790 1.00 39.48 ? 40  VAL   B CB  1 
ATOM   481  C  CG1 . VAL   B 2 31  ? -25.497 -1.316  -17.185 1.00 40.06 ? 40  VAL   B CG1 1 
ATOM   482  C  CG2 . VAL   B 2 31  ? -23.216 -0.454  -17.779 1.00 40.00 ? 40  VAL   B CG2 1 
ATOM   483  N  N   . MET   B 2 32  ? -27.209 1.565   -16.488 1.00 39.11 ? 41  MET   B N   1 
ATOM   484  C  CA  . MET   B 2 32  ? -28.514 1.622   -15.840 1.00 39.30 ? 41  MET   B CA  1 
ATOM   485  C  C   . MET   B 2 32  ? -29.285 0.424   -16.329 1.00 40.42 ? 41  MET   B C   1 
ATOM   486  O  O   . MET   B 2 32  ? -29.437 0.246   -17.521 1.00 40.77 ? 41  MET   B O   1 
ATOM   487  C  CB  . MET   B 2 32  ? -29.244 2.930   -16.138 1.00 38.65 ? 41  MET   B CB  1 
ATOM   488  C  CG  . MET   B 2 32  ? -30.542 3.067   -15.393 1.00 39.68 ? 41  MET   B CG  1 
ATOM   489  S  SD  . MET   B 2 32  ? -30.354 3.767   -13.743 1.00 41.71 ? 41  MET   B SD  1 
ATOM   490  C  CE  . MET   B 2 32  ? -29.754 5.437   -14.197 1.00 39.45 ? 41  MET   B CE  1 
ATOM   491  N  N   . GLN   B 2 33  ? -29.658 -0.461  -15.415 1.00 41.33 ? 42  GLN   B N   1 
ATOM   492  C  CA  . GLN   B 2 33  ? -30.371 -1.700  -15.708 1.00 41.84 ? 42  GLN   B CA  1 
ATOM   493  C  C   . GLN   B 2 33  ? -31.255 -2.030  -14.518 1.00 42.32 ? 42  GLN   B C   1 
ATOM   494  O  O   . GLN   B 2 33  ? -30.804 -1.947  -13.372 1.00 42.22 ? 42  GLN   B O   1 
ATOM   495  C  CB  . GLN   B 2 33  ? -29.379 -2.842  -15.917 1.00 42.88 ? 42  GLN   B CB  1 
ATOM   496  C  CG  . GLN   B 2 33  ? -30.048 -4.150  -16.315 1.00 46.33 ? 42  GLN   B CG  1 
ATOM   497  C  CD  . GLN   B 2 33  ? -29.001 -5.191  -16.614 1.00 52.05 ? 42  GLN   B CD  1 
ATOM   498  O  OE1 . GLN   B 2 33  ? -28.873 -6.209  -15.916 1.00 53.76 ? 42  GLN   B OE1 1 
ATOM   499  N  NE2 . GLN   B 2 33  ? -28.201 -4.937  -17.640 1.00 52.31 ? 42  GLN   B NE2 1 
ATOM   500  N  N   . GLU   B 2 34  ? -32.522 -2.350  -14.789 1.00 42.40 ? 43  GLU   B N   1 
ATOM   501  C  CA  . GLU   B 2 34  ? -33.511 -2.691  -13.786 1.00 42.78 ? 43  GLU   B CA  1 
ATOM   502  C  C   . GLU   B 2 34  ? -33.634 -1.623  -12.696 1.00 42.85 ? 43  GLU   B C   1 
ATOM   503  O  O   . GLU   B 2 34  ? -33.740 -1.945  -11.512 1.00 42.48 ? 43  GLU   B O   1 
ATOM   504  C  CB  . GLU   B 2 34  ? -33.216 -4.067  -13.181 1.00 45.09 ? 43  GLU   B CB  1 
ATOM   505  C  CG  . GLU   B 2 34  ? -33.109 -5.160  -14.221 1.00 49.96 ? 43  GLU   B CG  1 
ATOM   506  C  CD  . GLU   B 2 34  ? -32.903 -6.539  -13.637 1.00 55.83 ? 43  GLU   B CD  1 
ATOM   507  O  OE1 . GLU   B 2 34  ? -33.814 -7.028  -12.928 1.00 58.20 ? 43  GLU   B OE1 1 
ATOM   508  O  OE2 . GLU   B 2 34  ? -31.831 -7.132  -13.889 1.00 57.26 ? 43  GLU   B OE2 1 
ATOM   509  N  N   . GLY   B 2 35  ? -33.619 -0.363  -13.106 1.00 42.59 ? 44  GLY   B N   1 
ATOM   510  C  CA  . GLY   B 2 35  ? -33.735 0.743   -12.165 1.00 42.46 ? 44  GLY   B CA  1 
ATOM   511  C  C   . GLY   B 2 35  ? -32.530 0.949   -11.270 1.00 42.15 ? 44  GLY   B C   1 
ATOM   512  O  O   . GLY   B 2 35  ? -32.595 1.773   -10.359 1.00 43.43 ? 44  GLY   B O   1 
ATOM   513  N  N   . VAL   B 2 36  ? -31.426 0.211   -11.506 1.00 40.66 ? 45  VAL   B N   1 
ATOM   514  C  CA  . VAL   B 2 36  ? -30.188 0.291   -10.719 1.00 39.69 ? 45  VAL   B CA  1 
ATOM   515  C  C   . VAL   B 2 36  ? -29.018 0.814   -11.583 1.00 38.22 ? 45  VAL   B C   1 
ATOM   516  O  O   . VAL   B 2 36  ? -28.835 0.391   -12.728 1.00 37.62 ? 45  VAL   B O   1 
ATOM   517  C  CB  . VAL   B 2 36  ? -29.834 -1.056  -10.010 1.00 40.52 ? 45  VAL   B CB  1 
ATOM   518  C  CG1 . VAL   B 2 36  ? -28.493 -0.970  -9.292  1.00 40.87 ? 45  VAL   B CG1 1 
ATOM   519  C  CG2 . VAL   B 2 36  ? -30.929 -1.481  -9.040  1.00 40.73 ? 45  VAL   B CG2 1 
ATOM   520  N  N   . PHE   B 2 37  ? -28.276 1.790   -11.052 1.00 37.09 ? 46  PHE   B N   1 
ATOM   521  C  CA  . PHE   B 2 37  ? -27.148 2.363   -11.756 1.00 36.30 ? 46  PHE   B CA  1 
ATOM   522  C  C   . PHE   B 2 37  ? -25.867 1.720   -11.240 1.00 35.79 ? 46  PHE   B C   1 
ATOM   523  O  O   . PHE   B 2 37  ? -25.678 1.644   -10.045 1.00 35.43 ? 46  PHE   B O   1 
ATOM   524  C  CB  . PHE   B 2 37  ? -27.097 3.882   -11.568 1.00 35.87 ? 46  PHE   B CB  1 
ATOM   525  C  CG  . PHE   B 2 37  ? -26.089 4.461   -12.530 1.00 36.60 ? 46  PHE   B CG  1 
ATOM   526  C  CD1 . PHE   B 2 37  ? -26.266 4.339   -13.900 1.00 37.26 ? 46  PHE   B CD1 1 
ATOM   527  C  CD2 . PHE   B 2 37  ? -24.924 5.042   -12.069 1.00 37.25 ? 46  PHE   B CD2 1 
ATOM   528  C  CE1 . PHE   B 2 37  ? -25.342 4.865   -14.786 1.00 37.66 ? 46  PHE   B CE1 1 
ATOM   529  C  CE2 . PHE   B 2 37  ? -23.996 5.559   -12.958 1.00 37.94 ? 46  PHE   B CE2 1 
ATOM   530  C  CZ  . PHE   B 2 37  ? -24.227 5.491   -14.312 1.00 37.60 ? 46  PHE   B CZ  1 
ATOM   531  N  N   . HIS   B 2 38  ? -25.002 1.237   -12.132 1.00 35.62 ? 47  HIS   B N   1 
ATOM   532  C  CA  . HIS   B 2 38  ? -23.794 0.531   -11.735 1.00 35.43 ? 47  HIS   B CA  1 
ATOM   533  C  C   . HIS   B 2 38  ? -22.602 1.274   -12.249 1.00 37.35 ? 47  HIS   B C   1 
ATOM   534  O  O   . HIS   B 2 38  ? -22.594 1.663   -13.414 1.00 37.91 ? 47  HIS   B O   1 
ATOM   535  C  CB  . HIS   B 2 38  ? -23.773 -0.861  -12.375 1.00 34.41 ? 47  HIS   B CB  1 
ATOM   536  C  CG  . HIS   B 2 38  ? -25.013 -1.666  -12.167 1.00 34.33 ? 47  HIS   B CG  1 
ATOM   537  N  ND1 . HIS   B 2 38  ? -26.230 -1.253  -12.658 1.00 35.21 ? 47  HIS   B ND1 1 
ATOM   538  C  CD2 . HIS   B 2 38  ? -25.168 -2.874  -11.582 1.00 35.54 ? 47  HIS   B CD2 1 
ATOM   539  C  CE1 . HIS   B 2 38  ? -27.096 -2.194  -12.318 1.00 35.97 ? 47  HIS   B CE1 1 
ATOM   540  N  NE2 . HIS   B 2 38  ? -26.505 -3.189  -11.670 1.00 36.37 ? 47  HIS   B NE2 1 
ATOM   541  N  N   . THR   B 2 39  ? -21.576 1.477   -11.409 1.00 37.69 ? 48  THR   B N   1 
ATOM   542  C  CA  . THR   B 2 39  ? -20.342 2.111   -11.885 1.00 38.08 ? 48  THR   B CA  1 
ATOM   543  C  C   . THR   B 2 39  ? -19.154 1.585   -11.023 1.00 37.76 ? 48  THR   B C   1 
ATOM   544  O  O   . THR   B 2 39  ? -19.299 0.584   -10.326 1.00 37.36 ? 48  THR   B O   1 
ATOM   545  C  CB  . THR   B 2 39  ? -20.486 3.670   -12.033 1.00 39.27 ? 48  THR   B CB  1 
ATOM   546  O  OG1 . THR   B 2 39  ? -19.353 4.166   -12.753 1.00 39.33 ? 48  THR   B OG1 1 
ATOM   547  C  CG2 . THR   B 2 39  ? -20.629 4.381   -10.687 1.00 39.92 ? 48  THR   B CG2 1 
ATOM   548  N  N   . MET   B 2 40  ? -17.960 2.160   -11.186 1.00 38.04 ? 49  MET   B N   1 
ATOM   549  C  CA  . MET   B 2 40  ? -16.799 1.744   -10.433 1.00 38.69 ? 49  MET   B CA  1 
ATOM   550  C  C   . MET   B 2 40  ? -16.687 2.681   -9.243  1.00 40.18 ? 49  MET   B C   1 
ATOM   551  O  O   . MET   B 2 40  ? -16.989 3.881   -9.358  1.00 40.45 ? 49  MET   B O   1 
ATOM   552  C  CB  . MET   B 2 40  ? -15.540 1.744   -11.320 1.00 38.45 ? 49  MET   B CB  1 
ATOM   553  C  CG  . MET   B 2 40  ? -15.759 1.014   -12.628 1.00 39.84 ? 49  MET   B CG  1 
ATOM   554  S  SD  . MET   B 2 40  ? -14.383 -0.011  -13.224 1.00 40.81 ? 49  MET   B SD  1 
ATOM   555  C  CE  . MET   B 2 40  ? -14.424 -1.355  -12.048 1.00 32.46 ? 49  MET   B CE  1 
ATOM   556  N  N   . TRP   B 2 41  ? -16.274 2.135   -8.080  1.00 40.23 ? 50  TRP   B N   1 
ATOM   557  C  CA  A TRP   B 2 41  ? -16.120 2.920   -6.868  0.50 40.74 ? 50  TRP   B CA  1 
ATOM   558  C  CA  B TRP   B 2 41  ? -16.140 2.940   -6.874  0.50 40.66 ? 50  TRP   B CA  1 
ATOM   559  C  C   . TRP   B 2 41  ? -15.189 4.118   -7.055  1.00 41.28 ? 50  TRP   B C   1 
ATOM   560  O  O   . TRP   B 2 41  ? -15.500 5.203   -6.573  1.00 42.20 ? 50  TRP   B O   1 
ATOM   561  C  CB  A TRP   B 2 41  ? -15.622 2.041   -5.713  0.50 40.69 ? 50  TRP   B CB  1 
ATOM   562  C  CB  B TRP   B 2 41  ? -15.740 2.088   -5.652  0.50 40.48 ? 50  TRP   B CB  1 
ATOM   563  C  CG  A TRP   B 2 41  ? -16.021 2.559   -4.370  0.50 41.18 ? 50  TRP   B CG  1 
ATOM   564  C  CG  B TRP   B 2 41  ? -15.599 2.881   -4.382  0.50 40.81 ? 50  TRP   B CG  1 
ATOM   565  C  CD1 A TRP   B 2 41  ? -17.134 2.218   -3.661  0.50 42.04 ? 50  TRP   B CD1 1 
ATOM   566  C  CD1 B TRP   B 2 41  ? -14.483 3.528   -3.936  0.50 41.62 ? 50  TRP   B CD1 1 
ATOM   567  C  CD2 A TRP   B 2 41  ? -15.339 3.553   -3.592  0.50 41.38 ? 50  TRP   B CD2 1 
ATOM   568  C  CD2 B TRP   B 2 41  ? -16.616 3.111   -3.395  0.50 40.99 ? 50  TRP   B CD2 1 
ATOM   569  N  NE1 A TRP   B 2 41  ? -17.178 2.923   -2.483  0.50 42.36 ? 50  TRP   B NE1 1 
ATOM   570  N  NE1 B TRP   B 2 41  ? -14.744 4.151   -2.736  0.50 41.88 ? 50  TRP   B NE1 1 
ATOM   571  C  CE2 A TRP   B 2 41  ? -16.087 3.750   -2.415  0.50 42.11 ? 50  TRP   B CE2 1 
ATOM   572  C  CE2 B TRP   B 2 41  ? -16.047 3.910   -2.382  0.50 41.67 ? 50  TRP   B CE2 1 
ATOM   573  C  CE3 A TRP   B 2 41  ? -14.150 4.271   -3.757  0.50 41.95 ? 50  TRP   B CE3 1 
ATOM   574  C  CE3 B TRP   B 2 41  ? -17.954 2.720   -3.269  0.50 41.60 ? 50  TRP   B CE3 1 
ATOM   575  C  CZ2 A TRP   B 2 41  ? -15.706 4.658   -1.434  0.50 42.75 ? 50  TRP   B CZ2 1 
ATOM   576  C  CZ2 B TRP   B 2 41  ? -16.773 4.328   -1.267  0.50 42.30 ? 50  TRP   B CZ2 1 
ATOM   577  C  CZ3 A TRP   B 2 41  ? -13.777 5.173   -2.781  0.50 42.76 ? 50  TRP   B CZ3 1 
ATOM   578  C  CZ3 B TRP   B 2 41  ? -18.668 3.133   -2.158  0.50 42.50 ? 50  TRP   B CZ3 1 
ATOM   579  C  CH2 A TRP   B 2 41  ? -14.537 5.340   -1.625  0.50 42.87 ? 50  TRP   B CH2 1 
ATOM   580  C  CH2 B TRP   B 2 41  ? -18.076 3.921   -1.171  0.50 42.43 ? 50  TRP   B CH2 1 
ATOM   581  N  N   . HIS   B 2 42  ? -14.039 3.929   -7.741  1.00 40.76 ? 51  HIS   B N   1 
ATOM   582  C  CA  . HIS   B 2 42  ? -13.087 5.037   -7.907  1.00 41.19 ? 51  HIS   B CA  1 
ATOM   583  C  C   . HIS   B 2 42  ? -13.659 6.227   -8.736  1.00 41.32 ? 51  HIS   B C   1 
ATOM   584  O  O   . HIS   B 2 42  ? -13.176 7.347   -8.600  1.00 41.45 ? 51  HIS   B O   1 
ATOM   585  C  CB  . HIS   B 2 42  ? -11.729 4.549   -8.453  1.00 41.57 ? 51  HIS   B CB  1 
ATOM   586  C  CG  . HIS   B 2 42  ? -11.714 4.345   -9.930  1.00 43.59 ? 51  HIS   B CG  1 
ATOM   587  N  ND1 . HIS   B 2 42  ? -11.993 3.112   -10.492 1.00 45.55 ? 51  HIS   B ND1 1 
ATOM   588  C  CD2 . HIS   B 2 42  ? -11.476 5.232   -10.920 1.00 44.07 ? 51  HIS   B CD2 1 
ATOM   589  C  CE1 . HIS   B 2 42  ? -11.956 3.301   -11.796 1.00 45.33 ? 51  HIS   B CE1 1 
ATOM   590  N  NE2 . HIS   B 2 42  ? -11.630 4.555   -12.096 1.00 45.25 ? 51  HIS   B NE2 1 
ATOM   591  N  N   . VAL   B 2 43  ? -14.687 5.992   -9.551  1.00 41.19 ? 52  VAL   B N   1 
ATOM   592  C  CA  . VAL   B 2 43  ? -15.316 7.052   -10.351 1.00 41.99 ? 52  VAL   B CA  1 
ATOM   593  C  C   . VAL   B 2 43  ? -16.088 8.063   -9.455  1.00 42.72 ? 52  VAL   B C   1 
ATOM   594  O  O   . VAL   B 2 43  ? -15.809 9.271   -9.479  1.00 42.65 ? 52  VAL   B O   1 
ATOM   595  C  CB  . VAL   B 2 43  ? -16.238 6.453   -11.455 1.00 42.66 ? 52  VAL   B CB  1 
ATOM   596  C  CG1 . VAL   B 2 43  ? -17.000 7.542   -12.193 1.00 43.22 ? 52  VAL   B CG1 1 
ATOM   597  C  CG2 . VAL   B 2 43  ? -15.459 5.572   -12.433 1.00 43.11 ? 52  VAL   B CG2 1 
ATOM   598  N  N   . THR   B 2 44  ? -17.032 7.561   -8.637  1.00 42.69 ? 53  THR   B N   1 
ATOM   599  C  CA  . THR   B 2 44  ? -17.871 8.423   -7.813  1.00 43.02 ? 53  THR   B CA  1 
ATOM   600  C  C   . THR   B 2 44  ? -17.411 8.614   -6.380  1.00 43.42 ? 53  THR   B C   1 
ATOM   601  O  O   . THR   B 2 44  ? -17.881 9.545   -5.723  1.00 43.35 ? 53  THR   B O   1 
ATOM   602  C  CB  . THR   B 2 44  ? -19.320 7.891   -7.814  1.00 44.02 ? 53  THR   B CB  1 
ATOM   603  O  OG1 . THR   B 2 44  ? -19.365 6.609   -7.181  1.00 44.71 ? 53  THR   B OG1 1 
ATOM   604  C  CG2 . THR   B 2 44  ? -19.910 7.793   -9.206  1.00 44.26 ? 53  THR   B CG2 1 
ATOM   605  N  N   . LYS   B 2 45  ? -16.519 7.736   -5.890  1.00 43.80 ? 54  LYS   B N   1 
ATOM   606  C  CA  . LYS   B 2 45  ? -16.087 7.637   -4.484  1.00 45.08 ? 54  LYS   B CA  1 
ATOM   607  C  C   . LYS   B 2 45  ? -17.290 7.359   -3.541  1.00 45.57 ? 54  LYS   B C   1 
ATOM   608  O  O   . LYS   B 2 45  ? -17.188 7.584   -2.343  1.00 45.71 ? 54  LYS   B O   1 
ATOM   609  C  CB  . LYS   B 2 45  ? -15.299 8.860   -3.987  1.00 47.84 ? 54  LYS   B CB  1 
ATOM   610  C  CG  . LYS   B 2 45  ? -14.304 9.434   -4.981  1.00 53.75 ? 54  LYS   B CG  1 
ATOM   611  C  CD  . LYS   B 2 45  ? -13.026 8.637   -5.069  1.00 59.57 ? 54  LYS   B CD  1 
ATOM   612  C  CE  . LYS   B 2 45  ? -12.110 9.278   -6.094  1.00 64.76 ? 54  LYS   B CE  1 
ATOM   613  N  NZ  . LYS   B 2 45  ? -11.242 8.273   -6.784  1.00 67.94 ? 54  LYS   B NZ  1 
ATOM   614  N  N   . GLY   B 2 46  ? -18.403 6.864   -4.086  1.00 45.65 ? 55  GLY   B N   1 
ATOM   615  C  CA  . GLY   B 2 46  ? -19.611 6.582   -3.326  1.00 45.93 ? 55  GLY   B CA  1 
ATOM   616  C  C   . GLY   B 2 46  ? -20.518 7.787   -3.171  1.00 46.50 ? 55  GLY   B C   1 
ATOM   617  O  O   . GLY   B 2 46  ? -21.517 7.700   -2.467  1.00 47.08 ? 55  GLY   B O   1 
ATOM   618  N  N   . ALA   B 2 47  ? -20.198 8.921   -3.805  1.00 46.48 ? 56  ALA   B N   1 
ATOM   619  C  CA  . ALA   B 2 47  ? -21.011 10.132  -3.690  1.00 47.05 ? 56  ALA   B CA  1 
ATOM   620  C  C   . ALA   B 2 47  ? -22.333 10.021  -4.446  1.00 47.30 ? 56  ALA   B C   1 
ATOM   621  O  O   . ALA   B 2 47  ? -22.414 9.300   -5.428  1.00 46.93 ? 56  ALA   B O   1 
ATOM   622  C  CB  . ALA   B 2 47  ? -20.228 11.339  -4.186  1.00 47.14 ? 56  ALA   B CB  1 
ATOM   623  N  N   . ALA   B 2 48  ? -23.364 10.749  -3.995  1.00 47.73 ? 57  ALA   B N   1 
ATOM   624  C  CA  . ALA   B 2 48  ? -24.674 10.749  -4.653  1.00 48.35 ? 57  ALA   B CA  1 
ATOM   625  C  C   . ALA   B 2 48  ? -24.592 11.350  -6.050  1.00 48.64 ? 57  ALA   B C   1 
ATOM   626  O  O   . ALA   B 2 48  ? -23.752 12.211  -6.314  1.00 48.76 ? 57  ALA   B O   1 
ATOM   627  C  CB  . ALA   B 2 48  ? -25.686 11.515  -3.815  1.00 48.73 ? 57  ALA   B CB  1 
ATOM   628  N  N   . LEU   B 2 49  ? -25.443 10.869  -6.956  1.00 48.63 ? 58  LEU   B N   1 
ATOM   629  C  CA  . LEU   B 2 49  ? -25.458 11.315  -8.350  1.00 49.01 ? 58  LEU   B CA  1 
ATOM   630  C  C   . LEU   B 2 49  ? -26.736 12.078  -8.685  1.00 50.44 ? 58  LEU   B C   1 
ATOM   631  O  O   . LEU   B 2 49  ? -27.742 11.928  -7.997  1.00 50.41 ? 58  LEU   B O   1 
ATOM   632  C  CB  . LEU   B 2 49  ? -25.305 10.108  -9.278  1.00 48.15 ? 58  LEU   B CB  1 
ATOM   633  C  CG  . LEU   B 2 49  ? -24.036 9.311   -9.062  1.00 48.80 ? 58  LEU   B CG  1 
ATOM   634  C  CD1 . LEU   B 2 49  ? -24.078 8.023   -9.809  1.00 49.03 ? 58  LEU   B CD1 1 
ATOM   635  C  CD2 . LEU   B 2 49  ? -22.817 10.114  -9.441  1.00 49.22 ? 58  LEU   B CD2 1 
ATOM   636  N  N   . ARG   B 2 50  ? -26.687 12.925  -9.707  1.00 51.40 ? 59  ARG   B N   1 
ATOM   637  C  CA  . ARG   B 2 50  ? -27.853 13.695  -10.121 1.00 53.26 ? 59  ARG   B CA  1 
ATOM   638  C  C   . ARG   B 2 50  ? -28.311 13.200  -11.487 1.00 54.30 ? 59  ARG   B C   1 
ATOM   639  O  O   . ARG   B 2 50  ? -27.491 13.010  -12.377 1.00 54.13 ? 59  ARG   B O   1 
ATOM   640  C  CB  . ARG   B 2 50  ? -27.518 15.194  -10.147 1.00 55.46 ? 59  ARG   B CB  1 
ATOM   641  C  CG  . ARG   B 2 50  ? -28.555 16.077  -10.811 1.00 59.91 ? 59  ARG   B CG  1 
ATOM   642  C  CD  . ARG   B 2 50  ? -28.234 17.555  -10.641 1.00 65.40 ? 59  ARG   B CD  1 
ATOM   643  N  NE  . ARG   B 2 50  ? -26.921 17.944  -11.170 1.00 69.57 ? 59  ARG   B NE  1 
ATOM   644  C  CZ  . ARG   B 2 50  ? -26.725 18.484  -12.371 1.00 72.75 ? 59  ARG   B CZ  1 
ATOM   645  N  NH1 . ARG   B 2 50  ? -27.746 18.673  -13.196 1.00 72.80 ? 59  ARG   B NH1 1 
ATOM   646  N  NH2 . ARG   B 2 50  ? -25.501 18.828  -12.760 1.00 72.91 ? 59  ARG   B NH2 1 
ATOM   647  N  N   . SER   B 2 51  ? -29.606 12.941  -11.640 1.00 55.17 ? 60  SER   B N   1 
ATOM   648  C  CA  . SER   B 2 51  ? -30.153 12.482  -12.912 1.00 56.58 ? 60  SER   B CA  1 
ATOM   649  C  C   . SER   B 2 51  ? -31.308 13.405  -13.270 1.00 58.13 ? 60  SER   B C   1 
ATOM   650  O  O   . SER   B 2 51  ? -32.448 13.135  -12.893 1.00 58.15 ? 60  SER   B O   1 
ATOM   651  C  CB  . SER   B 2 51  ? -30.635 11.041  -12.788 1.00 57.45 ? 60  SER   B CB  1 
ATOM   652  O  OG  . SER   B 2 51  ? -31.149 10.577  -14.023 1.00 58.85 ? 60  SER   B OG  1 
ATOM   653  N  N   . GLY   B 2 52  ? -30.996 14.515  -13.939 1.00 59.13 ? 61  GLY   B N   1 
ATOM   654  C  CA  . GLY   B 2 52  ? -31.986 15.532  -14.286 1.00 60.09 ? 61  GLY   B CA  1 
ATOM   655  C  C   . GLY   B 2 52  ? -32.454 16.217  -13.019 1.00 61.03 ? 61  GLY   B C   1 
ATOM   656  O  O   . GLY   B 2 52  ? -31.623 16.580  -12.177 1.00 61.39 ? 61  GLY   B O   1 
ATOM   657  N  N   . GLU   B 2 53  ? -33.785 16.345  -12.834 1.00 60.91 ? 62  GLU   B N   1 
ATOM   658  C  CA  . GLU   B 2 53  ? -34.312 16.879  -11.575 1.00 61.29 ? 62  GLU   B CA  1 
ATOM   659  C  C   . GLU   B 2 53  ? -34.085 15.852  -10.423 1.00 60.26 ? 62  GLU   B C   1 
ATOM   660  O  O   . GLU   B 2 53  ? -33.828 16.245  -9.281  1.00 60.66 ? 62  GLU   B O   1 
ATOM   661  C  CB  . GLU   B 2 53  ? -35.811 17.221  -11.703 1.00 64.88 ? 62  GLU   B CB  1 
ATOM   662  C  CG  . GLU   B 2 53  ? -36.422 17.776  -10.421 1.00 71.74 ? 62  GLU   B CG  1 
ATOM   663  C  CD  . GLU   B 2 53  ? -37.886 18.185  -10.505 1.00 80.47 ? 62  GLU   B CD  1 
ATOM   664  O  OE1 . GLU   B 2 53  ? -38.522 18.322  -9.433  1.00 81.92 ? 62  GLU   B OE1 1 
ATOM   665  O  OE2 . GLU   B 2 53  ? -38.398 18.362  -11.636 1.00 82.67 ? 62  GLU   B OE2 1 
ATOM   666  N  N   . GLY   B 2 54  ? -34.150 14.557  -10.758 1.00 58.66 ? 63  GLY   B N   1 
ATOM   667  C  CA  . GLY   B 2 54  ? -33.975 13.443  -9.836  1.00 57.63 ? 63  GLY   B CA  1 
ATOM   668  C  C   . GLY   B 2 54  ? -32.575 13.276  -9.283  1.00 56.30 ? 63  GLY   B C   1 
ATOM   669  O  O   . GLY   B 2 54  ? -31.633 13.922  -9.748  1.00 56.08 ? 63  GLY   B O   1 
ATOM   670  N  N   . ARG   B 2 55  ? -32.438 12.396  -8.279  1.00 55.16 ? 64  ARG   B N   1 
ATOM   671  C  CA  . ARG   B 2 55  ? -31.177 12.128  -7.593  1.00 54.63 ? 64  ARG   B CA  1 
ATOM   672  C  C   . ARG   B 2 55  ? -31.002 10.605  -7.337  1.00 53.79 ? 64  ARG   B C   1 
ATOM   673  O  O   . ARG   B 2 55  ? -31.975 9.914   -7.026  1.00 54.44 ? 64  ARG   B O   1 
ATOM   674  C  CB  . ARG   B 2 55  ? -31.180 12.902  -6.260  1.00 56.00 ? 64  ARG   B CB  1 
ATOM   675  C  CG  . ARG   B 2 55  ? -30.043 12.585  -5.305  1.00 58.70 ? 64  ARG   B CG  1 
ATOM   676  C  CD  . ARG   B 2 55  ? -30.401 12.953  -3.882  1.00 62.06 ? 64  ARG   B CD  1 
ATOM   677  N  NE  . ARG   B 2 55  ? -29.280 12.730  -2.974  1.00 65.23 ? 64  ARG   B NE  1 
ATOM   678  C  CZ  . ARG   B 2 55  ? -28.847 13.612  -2.081  1.00 68.86 ? 64  ARG   B CZ  1 
ATOM   679  N  NH1 . ARG   B 2 55  ? -29.459 14.784  -1.942  1.00 69.58 ? 64  ARG   B NH1 1 
ATOM   680  N  NH2 . ARG   B 2 55  ? -27.810 13.322  -1.302  1.00 68.80 ? 64  ARG   B NH2 1 
ATOM   681  N  N   . LEU   B 2 56  ? -29.765 10.091  -7.445  1.00 51.98 ? 65  LEU   B N   1 
ATOM   682  C  CA  . LEU   B 2 56  ? -29.469 8.683   -7.200  1.00 50.74 ? 65  LEU   B CA  1 
ATOM   683  C  C   . LEU   B 2 56  ? -28.588 8.553   -5.954  1.00 49.25 ? 65  LEU   B C   1 
ATOM   684  O  O   . LEU   B 2 56  ? -27.501 9.132   -5.903  1.00 49.36 ? 65  LEU   B O   1 
ATOM   685  C  CB  . LEU   B 2 56  ? -28.741 8.044   -8.395  1.00 50.92 ? 65  LEU   B CB  1 
ATOM   686  C  CG  . LEU   B 2 56  ? -29.185 8.411   -9.805  1.00 52.59 ? 65  LEU   B CG  1 
ATOM   687  C  CD1 . LEU   B 2 56  ? -28.302 7.744   -10.812 1.00 53.48 ? 65  LEU   B CD1 1 
ATOM   688  C  CD2 . LEU   B 2 56  ? -30.578 7.968   -10.070 1.00 53.31 ? 65  LEU   B CD2 1 
ATOM   689  N  N   . ASP   B 2 57  ? -29.037 7.788   -4.959  1.00 47.67 ? 66  ASP   B N   1 
ATOM   690  C  CA  . ASP   B 2 57  ? -28.254 7.578   -3.742  1.00 47.05 ? 66  ASP   B CA  1 
ATOM   691  C  C   . ASP   B 2 57  ? -27.583 6.219   -3.793  1.00 45.88 ? 66  ASP   B C   1 
ATOM   692  O  O   . ASP   B 2 57  ? -28.177 5.278   -4.319  1.00 46.40 ? 66  ASP   B O   1 
ATOM   693  C  CB  . ASP   B 2 57  ? -29.164 7.625   -2.514  1.00 48.92 ? 66  ASP   B CB  1 
ATOM   694  C  CG  . ASP   B 2 57  ? -29.775 8.980   -2.277  1.00 53.50 ? 66  ASP   B CG  1 
ATOM   695  O  OD1 . ASP   B 2 57  ? -29.132 9.985   -2.634  1.00 53.51 ? 66  ASP   B OD1 1 
ATOM   696  O  OD2 . ASP   B 2 57  ? -30.894 9.035   -1.723  1.00 56.31 ? 66  ASP   B OD2 1 
ATOM   697  N  N   . PRO   B 2 58  ? -26.365 6.067   -3.242  1.00 44.12 ? 67  PRO   B N   1 
ATOM   698  C  CA  . PRO   B 2 58  ? -25.720 4.743   -3.275  1.00 43.10 ? 67  PRO   B CA  1 
ATOM   699  C  C   . PRO   B 2 58  ? -26.482 3.708   -2.443  1.00 42.11 ? 67  PRO   B C   1 
ATOM   700  O  O   . PRO   B 2 58  ? -27.259 4.062   -1.555  1.00 42.45 ? 67  PRO   B O   1 
ATOM   701  C  CB  . PRO   B 2 58  ? -24.308 5.014   -2.743  1.00 43.56 ? 67  PRO   B CB  1 
ATOM   702  C  CG  . PRO   B 2 58  ? -24.442 6.257   -1.936  1.00 44.10 ? 67  PRO   B CG  1 
ATOM   703  C  CD  . PRO   B 2 58  ? -25.514 7.076   -2.583  1.00 43.06 ? 67  PRO   B CD  1 
ATOM   704  N  N   . TYR   B 2 59  ? -26.316 2.423   -2.779  1.00 40.47 ? 68  TYR   B N   1 
ATOM   705  C  CA  . TYR   B 2 59  ? -27.015 1.358   -2.073  1.00 38.57 ? 68  TYR   B CA  1 
ATOM   706  C  C   . TYR   B 2 59  ? -26.017 0.290   -1.635  1.00 38.88 ? 68  TYR   B C   1 
ATOM   707  O  O   . TYR   B 2 59  ? -26.085 -0.189  -0.501  1.00 39.30 ? 68  TYR   B O   1 
ATOM   708  C  CB  . TYR   B 2 59  ? -28.106 0.783   -2.980  1.00 36.75 ? 68  TYR   B CB  1 
ATOM   709  C  CG  . TYR   B 2 59  ? -28.921 -0.350  -2.392  1.00 35.56 ? 68  TYR   B CG  1 
ATOM   710  C  CD1 . TYR   B 2 59  ? -28.403 -1.641  -2.316  1.00 35.69 ? 68  TYR   B CD1 1 
ATOM   711  C  CD2 . TYR   B 2 59  ? -30.255 -0.169  -2.056  1.00 35.01 ? 68  TYR   B CD2 1 
ATOM   712  C  CE1 . TYR   B 2 59  ? -29.150 -2.688  -1.802  1.00 35.94 ? 68  TYR   B CE1 1 
ATOM   713  C  CE2 . TYR   B 2 59  ? -31.021 -1.216  -1.571  1.00 35.51 ? 68  TYR   B CE2 1 
ATOM   714  C  CZ  . TYR   B 2 59  ? -30.463 -2.474  -1.438  1.00 36.30 ? 68  TYR   B CZ  1 
ATOM   715  O  OH  . TYR   B 2 59  ? -31.236 -3.530  -1.029  1.00 37.20 ? 68  TYR   B OH  1 
ATOM   716  N  N   . TRP   B 2 60  ? -25.088 -0.078  -2.529  1.00 38.20 ? 69  TRP   B N   1 
ATOM   717  C  CA  . TRP   B 2 60  ? -24.059 -1.059  -2.233  1.00 38.33 ? 69  TRP   B CA  1 
ATOM   718  C  C   . TRP   B 2 60  ? -22.720 -0.589  -2.815  1.00 39.10 ? 69  TRP   B C   1 
ATOM   719  O  O   . TRP   B 2 60  ? -22.699 0.071   -3.836  1.00 40.20 ? 69  TRP   B O   1 
ATOM   720  C  CB  . TRP   B 2 60  ? -24.458 -2.456  -2.757  1.00 37.89 ? 69  TRP   B CB  1 
ATOM   721  C  CG  . TRP   B 2 60  ? -23.349 -3.453  -2.657  1.00 38.06 ? 69  TRP   B CG  1 
ATOM   722  C  CD1 . TRP   B 2 60  ? -22.968 -4.145  -1.547  1.00 38.99 ? 69  TRP   B CD1 1 
ATOM   723  C  CD2 . TRP   B 2 60  ? -22.358 -3.719  -3.655  1.00 38.08 ? 69  TRP   B CD2 1 
ATOM   724  N  NE1 . TRP   B 2 60  ? -21.839 -4.888  -1.818  1.00 39.22 ? 69  TRP   B NE1 1 
ATOM   725  C  CE2 . TRP   B 2 60  ? -21.448 -4.647  -3.108  1.00 38.84 ? 69  TRP   B CE2 1 
ATOM   726  C  CE3 . TRP   B 2 60  ? -22.158 -3.276  -4.969  1.00 37.92 ? 69  TRP   B CE3 1 
ATOM   727  C  CZ2 . TRP   B 2 60  ? -20.365 -5.140  -3.833  1.00 39.06 ? 69  TRP   B CZ2 1 
ATOM   728  C  CZ3 . TRP   B 2 60  ? -21.085 -3.768  -5.678  1.00 38.14 ? 69  TRP   B CZ3 1 
ATOM   729  C  CH2 . TRP   B 2 60  ? -20.200 -4.680  -5.109  1.00 38.26 ? 69  TRP   B CH2 1 
ATOM   730  N  N   . GLY   B 2 61  ? -21.618 -0.965  -2.187  1.00 38.90 ? 70  GLY   B N   1 
ATOM   731  C  CA  . GLY   B 2 61  ? -20.293 -0.588  -2.647  1.00 39.59 ? 70  GLY   B CA  1 
ATOM   732  C  C   . GLY   B 2 61  ? -19.203 -1.386  -1.967  1.00 40.57 ? 70  GLY   B C   1 
ATOM   733  O  O   . GLY   B 2 61  ? -19.401 -1.895  -0.865  1.00 40.83 ? 70  GLY   B O   1 
ATOM   734  N  N   . ASP   B 2 62  ? -18.041 -1.496  -2.608  1.00 40.89 ? 71  ASP   B N   1 
ATOM   735  C  CA  . ASP   B 2 62  ? -16.909 -2.217  -2.034  1.00 41.42 ? 71  ASP   B CA  1 
ATOM   736  C  C   . ASP   B 2 62  ? -15.641 -1.660  -2.697  1.00 41.40 ? 71  ASP   B C   1 
ATOM   737  O  O   . ASP   B 2 62  ? -15.512 -1.770  -3.903  1.00 41.49 ? 71  ASP   B O   1 
ATOM   738  C  CB  . ASP   B 2 62  ? -17.058 -3.719  -2.313  1.00 43.33 ? 71  ASP   B CB  1 
ATOM   739  C  CG  . ASP   B 2 62  ? -16.032 -4.613  -1.645  1.00 48.43 ? 71  ASP   B CG  1 
ATOM   740  O  OD1 . ASP   B 2 62  ? -14.822 -4.394  -1.859  1.00 48.99 ? 71  ASP   B OD1 1 
ATOM   741  O  OD2 . ASP   B 2 62  ? -16.440 -5.563  -0.946  1.00 51.89 ? 71  ASP   B OD2 1 
ATOM   742  N  N   . VAL   B 2 63  ? -14.719 -1.070  -1.914  1.00 40.92 ? 72  VAL   B N   1 
ATOM   743  C  CA  . VAL   B 2 63  ? -13.478 -0.489  -2.418  1.00 40.38 ? 72  VAL   B CA  1 
ATOM   744  C  C   . VAL   B 2 63  ? -12.584 -1.552  -3.008  1.00 40.39 ? 72  VAL   B C   1 
ATOM   745  O  O   . VAL   B 2 63  ? -12.030 -1.311  -4.080  1.00 40.85 ? 72  VAL   B O   1 
ATOM   746  C  CB  . VAL   B 2 63  ? -12.768 0.392   -1.353  1.00 40.73 ? 72  VAL   B CB  1 
ATOM   747  C  CG1 . VAL   B 2 63  ? -11.270 0.560   -1.621  1.00 41.06 ? 72  VAL   B CG1 1 
ATOM   748  C  CG2 . VAL   B 2 63  ? -13.444 1.747   -1.235  1.00 40.91 ? 72  VAL   B CG2 1 
ATOM   749  N  N   . LYS   B 2 64  ? -12.485 -2.744  -2.385  1.00 39.71 ? 73  LYS   B N   1 
ATOM   750  C  CA  . LYS   B 2 64  ? -11.629 -3.801  -2.952  1.00 39.88 ? 73  LYS   B CA  1 
ATOM   751  C  C   . LYS   B 2 64  ? -12.142 -4.296  -4.309  1.00 40.26 ? 73  LYS   B C   1 
ATOM   752  O  O   . LYS   B 2 64  ? -11.360 -4.399  -5.268  1.00 40.60 ? 73  LYS   B O   1 
ATOM   753  C  CB  . LYS   B 2 64  ? -11.410 -4.965  -1.973  1.00 41.07 ? 73  LYS   B CB  1 
ATOM   754  C  CG  . LYS   B 2 64  ? -10.321 -5.905  -2.447  1.00 43.40 ? 73  LYS   B CG  1 
ATOM   755  C  CD  . LYS   B 2 64  ? -10.088 -6.975  -1.450  1.00 47.23 ? 73  LYS   B CD  1 
ATOM   756  C  CE  . LYS   B 2 64  ? -9.120  -8.003  -1.964  1.00 51.63 ? 73  LYS   B CE  1 
ATOM   757  N  NZ  . LYS   B 2 64  ? -8.715  -8.940  -0.873  1.00 54.19 ? 73  LYS   B NZ  1 
ATOM   758  N  N   . GLN   B 2 65  ? -13.462 -4.554  -4.422  1.00 39.89 ? 74  GLN   B N   1 
ATOM   759  C  CA  . GLN   B 2 65  ? -14.033 -4.946  -5.721  1.00 39.56 ? 74  GLN   B CA  1 
ATOM   760  C  C   . GLN   B 2 65  ? -14.103 -3.760  -6.690  1.00 38.52 ? 74  GLN   B C   1 
ATOM   761  O  O   . GLN   B 2 65  ? -14.342 -3.966  -7.875  1.00 39.04 ? 74  GLN   B O   1 
ATOM   762  C  CB  . GLN   B 2 65  ? -15.444 -5.537  -5.566  1.00 42.45 ? 74  GLN   B CB  1 
ATOM   763  C  CG  . GLN   B 2 65  ? -15.559 -6.753  -4.642  1.00 47.11 ? 74  GLN   B CG  1 
ATOM   764  C  CD  . GLN   B 2 65  ? -16.944 -7.363  -4.761  1.00 53.15 ? 74  GLN   B CD  1 
ATOM   765  O  OE1 . GLN   B 2 65  ? -17.455 -7.605  -5.872  1.00 54.38 ? 74  GLN   B OE1 1 
ATOM   766  N  NE2 . GLN   B 2 65  ? -17.587 -7.624  -3.624  1.00 54.30 ? 74  GLN   B NE2 1 
ATOM   767  N  N   . ASP   B 2 66  ? -13.926 -2.520  -6.189  1.00 37.37 ? 75  ASP   B N   1 
ATOM   768  C  CA  . ASP   B 2 66  ? -13.978 -1.260  -6.920  1.00 36.20 ? 75  ASP   B CA  1 
ATOM   769  C  C   . ASP   B 2 66  ? -15.301 -1.153  -7.649  1.00 35.11 ? 75  ASP   B C   1 
ATOM   770  O  O   . ASP   B 2 66  ? -15.330 -0.820  -8.819  1.00 35.80 ? 75  ASP   B O   1 
ATOM   771  C  CB  . ASP   B 2 66  ? -12.775 -1.093  -7.861  1.00 37.79 ? 75  ASP   B CB  1 
ATOM   772  C  CG  . ASP   B 2 66  ? -12.699 0.271   -8.524  1.00 41.69 ? 75  ASP   B CG  1 
ATOM   773  O  OD1 . ASP   B 2 66  ? -13.125 1.256   -7.903  1.00 43.75 ? 75  ASP   B OD1 1 
ATOM   774  O  OD2 . ASP   B 2 66  ? -12.242 0.343   -9.658  1.00 42.79 ? 75  ASP   B OD2 1 
ATOM   775  N  N   . LEU   B 2 67  ? -16.410 -1.440  -6.962  1.00 33.60 ? 76  LEU   B N   1 
ATOM   776  C  CA  . LEU   B 2 67  ? -17.738 -1.361  -7.571  1.00 32.51 ? 76  LEU   B CA  1 
ATOM   777  C  C   . LEU   B 2 67  ? -18.712 -0.624  -6.669  1.00 32.33 ? 76  LEU   B C   1 
ATOM   778  O  O   . LEU   B 2 67  ? -18.444 -0.480  -5.472  1.00 32.06 ? 76  LEU   B O   1 
ATOM   779  C  CB  . LEU   B 2 67  ? -18.279 -2.750  -7.886  1.00 32.23 ? 76  LEU   B CB  1 
ATOM   780  C  CG  . LEU   B 2 67  ? -17.622 -3.486  -9.015  1.00 33.66 ? 76  LEU   B CG  1 
ATOM   781  C  CD1 . LEU   B 2 67  ? -18.074 -4.921  -9.027  1.00 34.70 ? 76  LEU   B CD1 1 
ATOM   782  C  CD2 . LEU   B 2 67  ? -17.843 -2.775  -10.377 1.00 33.51 ? 76  LEU   B CD2 1 
ATOM   783  N  N   . VAL   B 2 68  ? -19.841 -0.139  -7.255  1.00 31.85 ? 77  VAL   B N   1 
ATOM   784  C  CA  . VAL   B 2 68  ? -20.890 0.591   -6.559  1.00 32.45 ? 77  VAL   B CA  1 
ATOM   785  C  C   . VAL   B 2 68  ? -22.228 0.536   -7.353  1.00 32.71 ? 77  VAL   B C   1 
ATOM   786  O  O   . VAL   B 2 68  ? -22.248 0.533   -8.578  1.00 32.01 ? 77  VAL   B O   1 
ATOM   787  C  CB  . VAL   B 2 68  ? -20.457 2.043   -6.177  1.00 33.44 ? 77  VAL   B CB  1 
ATOM   788  C  CG1 . VAL   B 2 68  ? -20.348 2.931   -7.402  1.00 33.57 ? 77  VAL   B CG1 1 
ATOM   789  C  CG2 . VAL   B 2 68  ? -21.392 2.667   -5.143  1.00 34.01 ? 77  VAL   B CG2 1 
ATOM   790  N  N   . SER   B 2 69  ? -23.344 0.396   -6.631  1.00 33.09 ? 78  SER   B N   1 
ATOM   791  C  CA  . SER   B 2 69  ? -24.677 0.348   -7.240  1.00 32.37 ? 78  SER   B CA  1 
ATOM   792  C  C   . SER   B 2 69  ? -25.529 1.447   -6.604  1.00 32.40 ? 78  SER   B C   1 
ATOM   793  O  O   . SER   B 2 69  ? -25.310 1.799   -5.453  1.00 32.23 ? 78  SER   B O   1 
ATOM   794  C  CB  . SER   B 2 69  ? -25.313 -1.037  -7.083  1.00 31.52 ? 78  SER   B CB  1 
ATOM   795  O  OG  . SER   B 2 69  ? -25.967 -1.225  -5.840  1.00 31.51 ? 78  SER   B OG  1 
ATOM   796  N  N   . TYR   B 2 70  ? -26.477 2.004   -7.355  1.00 33.15 ? 79  TYR   B N   1 
ATOM   797  C  CA  . TYR   B 2 70  ? -27.317 3.120   -6.902  1.00 33.99 ? 79  TYR   B CA  1 
ATOM   798  C  C   . TYR   B 2 70  ? -28.784 2.783   -7.091  1.00 34.61 ? 79  TYR   B C   1 
ATOM   799  O  O   . TYR   B 2 70  ? -29.143 2.221   -8.129  1.00 34.87 ? 79  TYR   B O   1 
ATOM   800  C  CB  . TYR   B 2 70  ? -26.991 4.375   -7.729  1.00 33.95 ? 79  TYR   B CB  1 
ATOM   801  C  CG  . TYR   B 2 70  ? -25.687 5.041   -7.345  1.00 34.62 ? 79  TYR   B CG  1 
ATOM   802  C  CD1 . TYR   B 2 70  ? -24.464 4.523   -7.763  1.00 35.35 ? 79  TYR   B CD1 1 
ATOM   803  C  CD2 . TYR   B 2 70  ? -25.675 6.214   -6.603  1.00 35.08 ? 79  TYR   B CD2 1 
ATOM   804  C  CE1 . TYR   B 2 70  ? -23.264 5.135   -7.416  1.00 35.98 ? 79  TYR   B CE1 1 
ATOM   805  C  CE2 . TYR   B 2 70  ? -24.484 6.807   -6.209  1.00 35.73 ? 79  TYR   B CE2 1 
ATOM   806  C  CZ  . TYR   B 2 70  ? -23.279 6.269   -6.623  1.00 36.71 ? 79  TYR   B CZ  1 
ATOM   807  O  OH  . TYR   B 2 70  ? -22.109 6.885   -6.252  1.00 37.58 ? 79  TYR   B OH  1 
ATOM   808  N  N   . CYS   B 2 71  ? -29.633 3.126   -6.085  1.00 34.38 ? 80  CYS   B N   1 
ATOM   809  C  CA  . CYS   B 2 71  ? -31.083 2.900   -6.072  1.00 34.44 ? 80  CYS   B CA  1 
ATOM   810  C  C   . CYS   B 2 71  ? -31.483 1.449   -5.775  1.00 32.93 ? 80  CYS   B C   1 
ATOM   811  O  O   . CYS   B 2 71  ? -32.676 1.167   -5.711  1.00 33.52 ? 80  CYS   B O   1 
ATOM   812  C  CB  . CYS   B 2 71  ? -31.754 3.394   -7.355  1.00 37.31 ? 80  CYS   B CB  1 
ATOM   813  S  SG  . CYS   B 2 71  ? -31.294 5.077   -7.869  1.00 47.89 ? 80  CYS   B SG  1 
ATOM   814  N  N   . GLY   B 2 72  ? -30.527 0.540   -5.638  1.00 30.96 ? 81  GLY   B N   1 
ATOM   815  C  CA  . GLY   B 2 72  ? -30.833 -0.867  -5.423  1.00 30.81 ? 81  GLY   B CA  1 
ATOM   816  C  C   . GLY   B 2 72  ? -29.613 -1.758  -5.508  1.00 31.70 ? 81  GLY   B C   1 
ATOM   817  O  O   . GLY   B 2 72  ? -28.494 -1.287  -5.739  1.00 30.71 ? 81  GLY   B O   1 
ATOM   818  N  N   . PRO   B 2 73  ? -29.808 -3.070  -5.290  1.00 33.76 ? 82  PRO   B N   1 
ATOM   819  C  CA  . PRO   B 2 73  ? -28.656 -4.003  -5.313  1.00 35.53 ? 82  PRO   B CA  1 
ATOM   820  C  C   . PRO   B 2 73  ? -28.010 -4.229  -6.681  1.00 37.77 ? 82  PRO   B C   1 
ATOM   821  O  O   . PRO   B 2 73  ? -28.619 -3.922  -7.703  1.00 38.19 ? 82  PRO   B O   1 
ATOM   822  C  CB  . PRO   B 2 73  ? -29.242 -5.304  -4.747  1.00 35.97 ? 82  PRO   B CB  1 
ATOM   823  C  CG  . PRO   B 2 73  ? -30.732 -5.203  -5.002  1.00 35.70 ? 82  PRO   B CG  1 
ATOM   824  C  CD  . PRO   B 2 73  ? -31.075 -3.751  -4.952  1.00 33.46 ? 82  PRO   B CD  1 
ATOM   825  N  N   . TRP   B 2 74  ? -26.782 -4.799  -6.722  1.00 38.85 ? 83  TRP   B N   1 
ATOM   826  C  CA  . TRP   B 2 74  ? -26.106 -5.086  -7.998  1.00 39.88 ? 83  TRP   B CA  1 
ATOM   827  C  C   . TRP   B 2 74  ? -26.940 -6.066  -8.799  1.00 41.30 ? 83  TRP   B C   1 
ATOM   828  O  O   . TRP   B 2 74  ? -27.399 -7.059  -8.229  1.00 42.48 ? 83  TRP   B O   1 
ATOM   829  C  CB  . TRP   B 2 74  ? -24.699 -5.656  -7.767  1.00 39.91 ? 83  TRP   B CB  1 
ATOM   830  C  CG  . TRP   B 2 74  ? -23.877 -5.799  -9.017  1.00 40.74 ? 83  TRP   B CG  1 
ATOM   831  C  CD1 . TRP   B 2 74  ? -23.713 -6.927  -9.774  1.00 41.50 ? 83  TRP   B CD1 1 
ATOM   832  C  CD2 . TRP   B 2 74  ? -23.038 -4.795  -9.605  1.00 40.84 ? 83  TRP   B CD2 1 
ATOM   833  N  NE1 . TRP   B 2 74  ? -22.799 -6.695  -10.770 1.00 41.85 ? 83  TRP   B NE1 1 
ATOM   834  C  CE2 . TRP   B 2 74  ? -22.383 -5.389  -10.701 1.00 41.66 ? 83  TRP   B CE2 1 
ATOM   835  C  CE3 . TRP   B 2 74  ? -22.709 -3.482  -9.253  1.00 41.30 ? 83  TRP   B CE3 1 
ATOM   836  C  CZ2 . TRP   B 2 74  ? -21.471 -4.692  -11.484 1.00 42.63 ? 83  TRP   B CZ2 1 
ATOM   837  C  CZ3 . TRP   B 2 74  ? -21.809 -2.794  -10.030 1.00 42.34 ? 83  TRP   B CZ3 1 
ATOM   838  C  CH2 . TRP   B 2 74  ? -21.244 -3.378  -11.164 1.00 42.89 ? 83  TRP   B CH2 1 
ATOM   839  N  N   . LYS   B 2 75  ? -27.196 -5.751  -10.088 1.00 41.32 ? 84  LYS   B N   1 
ATOM   840  C  CA  . LYS   B 2 75  ? -28.072 -6.509  -10.973 1.00 41.87 ? 84  LYS   B CA  1 
ATOM   841  C  C   . LYS   B 2 75  ? -27.374 -7.274  -12.080 1.00 43.59 ? 84  LYS   B C   1 
ATOM   842  O  O   . LYS   B 2 75  ? -28.029 -8.078  -12.733 1.00 44.11 ? 84  LYS   B O   1 
ATOM   843  C  CB  . LYS   B 2 75  ? -29.107 -5.568  -11.617 1.00 42.50 ? 84  LYS   B CB  1 
ATOM   844  C  CG  . LYS   B 2 75  ? -30.023 -4.861  -10.627 1.00 44.58 ? 84  LYS   B CG  1 
ATOM   845  C  CD  . LYS   B 2 75  ? -30.990 -5.821  -9.958  1.00 47.04 ? 84  LYS   B CD  1 
ATOM   846  C  CE  . LYS   B 2 75  ? -31.715 -5.188  -8.793  1.00 50.67 ? 84  LYS   B CE  1 
ATOM   847  N  NZ  . LYS   B 2 75  ? -32.903 -4.405  -9.217  1.00 53.52 ? 84  LYS   B NZ  1 
ATOM   848  N  N   . LEU   B 2 76  ? -26.080 -7.022  -12.337 1.00 44.44 ? 85  LEU   B N   1 
ATOM   849  C  CA  . LEU   B 2 76  ? -25.369 -7.677  -13.447 1.00 45.45 ? 85  LEU   B CA  1 
ATOM   850  C  C   . LEU   B 2 76  ? -24.821 -9.041  -13.043 1.00 47.27 ? 85  LEU   B C   1 
ATOM   851  O  O   . LEU   B 2 76  ? -23.943 -9.124  -12.191 1.00 47.53 ? 85  LEU   B O   1 
ATOM   852  C  CB  . LEU   B 2 76  ? -24.252 -6.778  -14.009 1.00 45.01 ? 85  LEU   B CB  1 
ATOM   853  C  CG  . LEU   B 2 76  ? -24.573 -5.288  -14.122 1.00 45.77 ? 85  LEU   B CG  1 
ATOM   854  C  CD1 . LEU   B 2 76  ? -23.368 -4.513  -14.546 1.00 46.16 ? 85  LEU   B CD1 1 
ATOM   855  C  CD2 . LEU   B 2 76  ? -25.719 -5.039  -15.077 1.00 46.30 ? 85  LEU   B CD2 1 
ATOM   856  N  N   . ASP   B 2 77  ? -25.324 -10.114 -13.664 1.00 48.59 ? 86  ASP   B N   1 
ATOM   857  C  CA  . ASP   B 2 77  ? -24.921 -11.470 -13.292 1.00 50.25 ? 86  ASP   B CA  1 
ATOM   858  C  C   . ASP   B 2 77  ? -24.286 -12.304 -14.406 1.00 51.40 ? 86  ASP   B C   1 
ATOM   859  O  O   . ASP   B 2 77  ? -23.844 -13.419 -14.116 1.00 52.16 ? 86  ASP   B O   1 
ATOM   860  C  CB  . ASP   B 2 77  ? -26.089 -12.258 -12.650 1.00 52.36 ? 86  ASP   B CB  1 
ATOM   861  C  CG  . ASP   B 2 77  ? -27.435 -12.268 -13.375 1.00 58.37 ? 86  ASP   B CG  1 
ATOM   862  O  OD1 . ASP   B 2 77  ? -27.611 -11.477 -14.324 1.00 59.00 ? 86  ASP   B OD1 1 
ATOM   863  O  OD2 . ASP   B 2 77  ? -28.318 -13.059 -12.974 1.00 61.96 ? 86  ASP   B OD2 1 
ATOM   864  N  N   . ALA   B 2 78  ? -24.221 -11.800 -15.647 1.00 51.28 ? 87  ALA   B N   1 
ATOM   865  C  CA  . ALA   B 2 78  ? -23.600 -12.569 -16.732 1.00 51.93 ? 87  ALA   B CA  1 
ATOM   866  C  C   . ALA   B 2 78  ? -22.092 -12.649 -16.550 1.00 52.10 ? 87  ALA   B C   1 
ATOM   867  O  O   . ALA   B 2 78  ? -21.495 -11.733 -15.992 1.00 52.47 ? 87  ALA   B O   1 
ATOM   868  C  CB  . ALA   B 2 78  ? -23.929 -11.960 -18.084 1.00 52.05 ? 87  ALA   B CB  1 
ATOM   869  N  N   . ALA   B 2 79  ? -21.476 -13.743 -17.001 1.00 51.49 ? 88  ALA   B N   1 
ATOM   870  C  CA  . ALA   B 2 79  ? -20.032 -13.902 -16.873 1.00 51.45 ? 88  ALA   B CA  1 
ATOM   871  C  C   . ALA   B 2 79  ? -19.398 -14.298 -18.194 1.00 51.53 ? 88  ALA   B C   1 
ATOM   872  O  O   . ALA   B 2 79  ? -20.057 -14.932 -19.015 1.00 51.66 ? 88  ALA   B O   1 
ATOM   873  C  CB  . ALA   B 2 79  ? -19.722 -14.948 -15.830 1.00 51.58 ? 88  ALA   B CB  1 
ATOM   874  N  N   . TRP   B 2 80  ? -18.116 -13.938 -18.397 1.00 51.23 ? 89  TRP   B N   1 
ATOM   875  C  CA  . TRP   B 2 80  ? -17.378 -14.298 -19.608 1.00 51.58 ? 89  TRP   B CA  1 
ATOM   876  C  C   . TRP   B 2 80  ? -17.188 -15.813 -19.602 1.00 51.93 ? 89  TRP   B C   1 
ATOM   877  O  O   . TRP   B 2 80  ? -16.847 -16.370 -18.562 1.00 52.31 ? 89  TRP   B O   1 
ATOM   878  C  CB  . TRP   B 2 80  ? -16.015 -13.590 -19.628 1.00 51.27 ? 89  TRP   B CB  1 
ATOM   879  C  CG  . TRP   B 2 80  ? -15.140 -13.965 -20.790 1.00 51.25 ? 89  TRP   B CG  1 
ATOM   880  C  CD1 . TRP   B 2 80  ? -15.475 -13.928 -22.106 1.00 51.81 ? 89  TRP   B CD1 1 
ATOM   881  C  CD2 . TRP   B 2 80  ? -13.748 -14.310 -20.742 1.00 51.12 ? 89  TRP   B CD2 1 
ATOM   882  N  NE1 . TRP   B 2 80  ? -14.398 -14.271 -22.878 1.00 51.99 ? 89  TRP   B NE1 1 
ATOM   883  C  CE2 . TRP   B 2 80  ? -13.322 -14.513 -22.067 1.00 51.61 ? 89  TRP   B CE2 1 
ATOM   884  C  CE3 . TRP   B 2 80  ? -12.825 -14.491 -19.704 1.00 51.36 ? 89  TRP   B CE3 1 
ATOM   885  C  CZ2 . TRP   B 2 80  ? -12.019 -14.902 -22.383 1.00 51.82 ? 89  TRP   B CZ2 1 
ATOM   886  C  CZ3 . TRP   B 2 80  ? -11.538 -14.883 -20.020 1.00 51.86 ? 89  TRP   B CZ3 1 
ATOM   887  C  CH2 . TRP   B 2 80  ? -11.149 -15.085 -21.344 1.00 51.78 ? 89  TRP   B CH2 1 
ATOM   888  N  N   . ASP   B 2 81  ? -17.447 -16.483 -20.720 1.00 51.72 ? 90  ASP   B N   1 
ATOM   889  C  CA  . ASP   B 2 81  ? -17.330 -17.943 -20.792 1.00 52.78 ? 90  ASP   B CA  1 
ATOM   890  C  C   . ASP   B 2 81  ? -15.872 -18.480 -20.862 1.00 53.36 ? 90  ASP   B C   1 
ATOM   891  O  O   . ASP   B 2 81  ? -15.656 -19.697 -20.826 1.00 53.00 ? 90  ASP   B O   1 
ATOM   892  C  CB  . ASP   B 2 81  ? -18.177 -18.512 -21.959 1.00 54.57 ? 90  ASP   B CB  1 
ATOM   893  C  CG  . ASP   B 2 81  ? -17.813 -17.990 -23.337 1.00 59.46 ? 90  ASP   B CG  1 
ATOM   894  O  OD1 . ASP   B 2 81  ? -16.800 -17.264 -23.451 1.00 59.98 ? 90  ASP   B OD1 1 
ATOM   895  O  OD2 . ASP   B 2 81  ? -18.538 -18.315 -24.313 1.00 62.10 ? 90  ASP   B OD2 1 
ATOM   896  N  N   . GLY   B 2 82  ? -14.901 -17.576 -20.972 1.00 53.76 ? 91  GLY   B N   1 
ATOM   897  C  CA  . GLY   B 2 82  ? -13.499 -17.948 -21.088 1.00 54.51 ? 91  GLY   B CA  1 
ATOM   898  C  C   . GLY   B 2 82  ? -13.073 -18.285 -22.507 1.00 55.29 ? 91  GLY   B C   1 
ATOM   899  O  O   . GLY   B 2 82  ? -11.893 -18.536 -22.747 1.00 55.50 ? 91  GLY   B O   1 
ATOM   900  N  N   . LEU   B 2 83  ? -14.016 -18.300 -23.470 1.00 55.56 ? 92  LEU   B N   1 
ATOM   901  C  CA  . LEU   B 2 83  ? -13.699 -18.651 -24.850 1.00 56.16 ? 92  LEU   B CA  1 
ATOM   902  C  C   . LEU   B 2 83  ? -14.034 -17.584 -25.862 1.00 56.74 ? 92  LEU   B C   1 
ATOM   903  O  O   . LEU   B 2 83  ? -13.258 -17.366 -26.788 1.00 57.27 ? 92  LEU   B O   1 
ATOM   904  C  CB  . LEU   B 2 83  ? -14.481 -19.904 -25.282 1.00 56.48 ? 92  LEU   B CB  1 
ATOM   905  C  CG  . LEU   B 2 83  ? -14.028 -21.266 -24.846 1.00 57.78 ? 92  LEU   B CG  1 
ATOM   906  C  CD1 . LEU   B 2 83  ? -14.825 -22.307 -25.584 1.00 58.17 ? 92  LEU   B CD1 1 
ATOM   907  C  CD2 . LEU   B 2 83  ? -12.565 -21.462 -25.121 1.00 58.14 ? 92  LEU   B CD2 1 
ATOM   908  N  N   . SER   B 2 84  ? -15.246 -17.027 -25.792 1.00 56.49 ? 93  SER   B N   1 
ATOM   909  C  CA  . SER   B 2 84  ? -15.739 -16.131 -26.828 1.00 56.43 ? 93  SER   B CA  1 
ATOM   910  C  C   . SER   B 2 84  ? -15.139 -14.748 -26.822 1.00 55.65 ? 93  SER   B C   1 
ATOM   911  O  O   . SER   B 2 84  ? -14.644 -14.268 -25.801 1.00 55.45 ? 93  SER   B O   1 
ATOM   912  C  CB  . SER   B 2 84  ? -17.265 -16.031 -26.766 1.00 57.96 ? 93  SER   B CB  1 
ATOM   913  O  OG  . SER   B 2 84  ? -17.887 -17.298 -26.633 1.00 60.31 ? 93  SER   B OG  1 
ATOM   914  N  N   . GLU   B 2 85  ? -15.195 -14.105 -27.984 1.00 55.10 ? 94  GLU   B N   1 
ATOM   915  C  CA  . GLU   B 2 85  ? -14.814 -12.715 -28.123 1.00 54.92 ? 94  GLU   B CA  1 
ATOM   916  C  C   . GLU   B 2 85  ? -15.911 -11.888 -27.421 1.00 54.34 ? 94  GLU   B C   1 
ATOM   917  O  O   . GLU   B 2 85  ? -17.088 -12.275 -27.359 1.00 54.58 ? 94  GLU   B O   1 
ATOM   918  C  CB  . GLU   B 2 85  ? -14.717 -12.312 -29.607 1.00 56.38 ? 94  GLU   B CB  1 
ATOM   919  C  CG  . GLU   B 2 85  ? -13.464 -12.821 -30.304 1.00 60.33 ? 94  GLU   B CG  1 
ATOM   920  C  CD  . GLU   B 2 85  ? -12.932 -11.938 -31.422 1.00 64.01 ? 94  GLU   B CD  1 
ATOM   921  O  OE1 . GLU   B 2 85  ? -13.636 -10.982 -31.807 1.00 63.72 ? 94  GLU   B OE1 1 
ATOM   922  O  OE2 . GLU   B 2 85  ? -11.810 -12.200 -31.912 1.00 66.05 ? 94  GLU   B OE2 1 
ATOM   923  N  N   . VAL   B 2 86  ? -15.502 -10.785 -26.839 1.00 53.12 ? 95  VAL   B N   1 
ATOM   924  C  CA  . VAL   B 2 86  ? -16.400 -9.893  -26.132 1.00 52.28 ? 95  VAL   B CA  1 
ATOM   925  C  C   . VAL   B 2 86  ? -16.412 -8.532  -26.877 1.00 51.61 ? 95  VAL   B C   1 
ATOM   926  O  O   . VAL   B 2 86  ? -15.766 -8.394  -27.917 1.00 51.26 ? 95  VAL   B O   1 
ATOM   927  C  CB  . VAL   B 2 86  ? -15.975 -9.775  -24.636 1.00 52.21 ? 95  VAL   B CB  1 
ATOM   928  C  CG1 . VAL   B 2 86  ? -15.834 -11.144 -23.992 1.00 52.56 ? 95  VAL   B CG1 1 
ATOM   929  C  CG2 . VAL   B 2 86  ? -14.685 -8.977  -24.504 1.00 52.49 ? 95  VAL   B CG2 1 
ATOM   930  N  N   . GLN   B 2 87  ? -17.177 -7.542  -26.373 1.00 50.85 ? 96  GLN   B N   1 
ATOM   931  C  CA  . GLN   B 2 87  ? -17.200 -6.221  -26.965 1.00 50.20 ? 96  GLN   B CA  1 
ATOM   932  C  C   . GLN   B 2 87  ? -17.167 -5.165  -25.862 1.00 49.16 ? 96  GLN   B C   1 
ATOM   933  O  O   . GLN   B 2 87  ? -18.005 -5.187  -24.965 1.00 48.81 ? 96  GLN   B O   1 
ATOM   934  C  CB  . GLN   B 2 87  ? -18.435 -6.036  -27.859 1.00 51.73 ? 96  GLN   B CB  1 
ATOM   935  C  CG  . GLN   B 2 87  ? -18.260 -6.601  -29.271 1.00 54.52 ? 96  GLN   B CG  1 
ATOM   936  C  CD  . GLN   B 2 87  ? -19.215 -6.025  -30.282 1.00 58.03 ? 96  GLN   B CD  1 
ATOM   937  O  OE1 . GLN   B 2 87  ? -20.096 -5.211  -29.974 1.00 58.09 ? 96  GLN   B OE1 1 
ATOM   938  N  NE2 . GLN   B 2 87  ? -19.038 -6.425  -31.534 1.00 59.96 ? 96  GLN   B NE2 1 
ATOM   939  N  N   . LEU   B 2 88  ? -16.205 -4.240  -25.929 1.00 48.26 ? 97  LEU   B N   1 
ATOM   940  C  CA  . LEU   B 2 88  ? -16.146 -3.136  -24.986 1.00 47.61 ? 97  LEU   B CA  1 
ATOM   941  C  C   . LEU   B 2 88  ? -17.006 -2.016  -25.582 1.00 46.88 ? 97  LEU   B C   1 
ATOM   942  O  O   . LEU   B 2 88  ? -16.772 -1.615  -26.717 1.00 47.31 ? 97  LEU   B O   1 
ATOM   943  C  CB  . LEU   B 2 88  ? -14.696 -2.639  -24.807 1.00 47.57 ? 97  LEU   B CB  1 
ATOM   944  C  CG  . LEU   B 2 88  ? -14.521 -1.328  -24.023 1.00 48.33 ? 97  LEU   B CG  1 
ATOM   945  C  CD1 . LEU   B 2 88  ? -15.158 -1.410  -22.652 1.00 48.98 ? 97  LEU   B CD1 1 
ATOM   946  C  CD2 . LEU   B 2 88  ? -13.074 -0.983  -23.857 1.00 48.47 ? 97  LEU   B CD2 1 
ATOM   947  N  N   . LEU   B 2 89  ? -18.008 -1.547  -24.852 1.00 45.69 ? 98  LEU   B N   1 
ATOM   948  C  CA  . LEU   B 2 89  ? -18.849 -0.458  -25.315 1.00 45.35 ? 98  LEU   B CA  1 
ATOM   949  C  C   . LEU   B 2 89  ? -18.242 0.790   -24.688 1.00 44.58 ? 98  LEU   B C   1 
ATOM   950  O  O   . LEU   B 2 89  ? -18.712 1.273   -23.657 1.00 44.09 ? 98  LEU   B O   1 
ATOM   951  C  CB  . LEU   B 2 89  ? -20.307 -0.694  -24.879 1.00 45.67 ? 98  LEU   B CB  1 
ATOM   952  C  CG  . LEU   B 2 89  ? -21.354 0.394   -25.143 1.00 46.89 ? 98  LEU   B CG  1 
ATOM   953  C  CD1 . LEU   B 2 89  ? -21.264 0.966   -26.526 1.00 47.19 ? 98  LEU   B CD1 1 
ATOM   954  C  CD2 . LEU   B 2 89  ? -22.747 -0.126  -24.875 1.00 47.69 ? 98  LEU   B CD2 1 
ATOM   955  N  N   . ALA   B 2 90  ? -17.148 1.280   -25.297 1.00 43.66 ? 99  ALA   B N   1 
ATOM   956  C  CA  . ALA   B 2 90  ? -16.411 2.412   -24.765 1.00 43.16 ? 99  ALA   B CA  1 
ATOM   957  C  C   . ALA   B 2 90  ? -17.085 3.762   -24.962 1.00 43.03 ? 99  ALA   B C   1 
ATOM   958  O  O   . ALA   B 2 90  ? -17.504 4.091   -26.063 1.00 43.21 ? 99  ALA   B O   1 
ATOM   959  C  CB  . ALA   B 2 90  ? -15.008 2.431   -25.327 1.00 42.74 ? 99  ALA   B CB  1 
ATOM   960  N  N   . VAL   B 2 91  ? -17.186 4.545   -23.886 1.00 42.73 ? 100 VAL   B N   1 
ATOM   961  C  CA  . VAL   B 2 91  ? -17.755 5.884   -23.936 1.00 43.09 ? 100 VAL   B CA  1 
ATOM   962  C  C   . VAL   B 2 91  ? -16.641 6.843   -23.548 1.00 43.90 ? 100 VAL   B C   1 
ATOM   963  O  O   . VAL   B 2 91  ? -16.455 7.119   -22.368 1.00 44.37 ? 100 VAL   B O   1 
ATOM   964  C  CB  . VAL   B 2 91  ? -18.971 6.032   -22.995 1.00 43.03 ? 100 VAL   B CB  1 
ATOM   965  C  CG1 . VAL   B 2 91  ? -19.612 7.407   -23.141 1.00 43.02 ? 100 VAL   B CG1 1 
ATOM   966  C  CG2 . VAL   B 2 91  ? -19.986 4.926   -23.232 1.00 43.31 ? 100 VAL   B CG2 1 
ATOM   967  N  N   . PRO   B 2 92  ? -15.826 7.302   -24.509 1.00 44.07 ? 101 PRO   B N   1 
ATOM   968  C  CA  . PRO   B 2 92  ? -14.707 8.188   -24.146 1.00 44.37 ? 101 PRO   B CA  1 
ATOM   969  C  C   . PRO   B 2 92  ? -15.132 9.643   -23.936 1.00 44.90 ? 101 PRO   B C   1 
ATOM   970  O  O   . PRO   B 2 92  ? -16.075 10.111  -24.574 1.00 45.04 ? 101 PRO   B O   1 
ATOM   971  C  CB  . PRO   B 2 92  ? -13.717 8.013   -25.308 1.00 44.42 ? 101 PRO   B CB  1 
ATOM   972  C  CG  . PRO   B 2 92  ? -14.395 7.060   -26.288 1.00 45.09 ? 101 PRO   B CG  1 
ATOM   973  C  CD  . PRO   B 2 92  ? -15.847 7.030   -25.953 1.00 43.50 ? 101 PRO   B CD  1 
ATOM   974  N  N   . PRO   B 2 93  ? -14.443 10.393  -23.056 1.00 44.88 ? 102 PRO   B N   1 
ATOM   975  C  CA  . PRO   B 2 93  ? -14.800 11.813  -22.874 1.00 45.24 ? 102 PRO   B CA  1 
ATOM   976  C  C   . PRO   B 2 93  ? -14.897 12.577  -24.197 1.00 46.35 ? 102 PRO   B C   1 
ATOM   977  O  O   . PRO   B 2 93  ? -14.054 12.405  -25.081 1.00 46.12 ? 102 PRO   B O   1 
ATOM   978  C  CB  . PRO   B 2 93  ? -13.676 12.348  -21.990 1.00 45.49 ? 102 PRO   B CB  1 
ATOM   979  C  CG  . PRO   B 2 93  ? -13.192 11.134  -21.241 1.00 45.57 ? 102 PRO   B CG  1 
ATOM   980  C  CD  . PRO   B 2 93  ? -13.303 9.999   -22.204 1.00 43.94 ? 102 PRO   B CD  1 
ATOM   981  N  N   . GLY   B 2 94  ? -15.998 13.308  -24.360 1.00 46.95 ? 103 GLY   B N   1 
ATOM   982  C  CA  . GLY   B 2 94  ? -16.275 14.113  -25.543 1.00 47.45 ? 103 GLY   B CA  1 
ATOM   983  C  C   . GLY   B 2 94  ? -16.526 13.348  -26.824 1.00 48.00 ? 103 GLY   B C   1 
ATOM   984  O  O   . GLY   B 2 94  ? -16.612 13.949  -27.887 1.00 48.58 ? 103 GLY   B O   1 
ATOM   985  N  N   . GLU   B 2 95  ? -16.626 12.023  -26.748 1.00 48.20 ? 104 GLU   B N   1 
ATOM   986  C  CA  . GLU   B 2 95  ? -16.779 11.187  -27.935 1.00 48.41 ? 104 GLU   B CA  1 
ATOM   987  C  C   . GLU   B 2 95  ? -17.957 10.241  -27.866 1.00 49.35 ? 104 GLU   B C   1 
ATOM   988  O  O   . GLU   B 2 95  ? -18.371 9.823   -26.778 1.00 49.64 ? 104 GLU   B O   1 
ATOM   989  C  CB  . GLU   B 2 95  ? -15.492 10.394  -28.179 1.00 48.74 ? 104 GLU   B CB  1 
ATOM   990  C  CG  . GLU   B 2 95  ? -14.399 11.259  -28.759 1.00 50.12 ? 104 GLU   B CG  1 
ATOM   991  C  CD  . GLU   B 2 95  ? -13.003 10.702  -28.601 1.00 53.01 ? 104 GLU   B CD  1 
ATOM   992  O  OE1 . GLU   B 2 95  ? -12.862 9.494   -28.289 1.00 54.02 ? 104 GLU   B OE1 1 
ATOM   993  O  OE2 . GLU   B 2 95  ? -12.044 11.487  -28.782 1.00 52.58 ? 104 GLU   B OE2 1 
ATOM   994  N  N   . ARG   B 2 96  ? -18.467 9.872   -29.043 1.00 49.38 ? 105 ARG   B N   1 
ATOM   995  C  CA  . ARG   B 2 96  ? -19.604 8.978   -29.180 1.00 50.03 ? 105 ARG   B CA  1 
ATOM   996  C  C   . ARG   B 2 96  ? -19.273 7.554   -28.725 1.00 49.41 ? 105 ARG   B C   1 
ATOM   997  O  O   . ARG   B 2 96  ? -18.139 7.106   -28.888 1.00 48.88 ? 105 ARG   B O   1 
ATOM   998  C  CB  . ARG   B 2 96  ? -20.077 8.995   -30.641 1.00 52.71 ? 105 ARG   B CB  1 
ATOM   999  C  CG  . ARG   B 2 96  ? -21.505 8.508   -30.846 1.00 58.18 ? 105 ARG   B CG  1 
ATOM   1000 C  CD  . ARG   B 2 96  ? -22.146 9.097   -32.088 1.00 63.33 ? 105 ARG   B CD  1 
ATOM   1001 N  NE  . ARG   B 2 96  ? -21.387 8.812   -33.304 1.00 68.77 ? 105 ARG   B NE  1 
ATOM   1002 C  CZ  . ARG   B 2 96  ? -20.674 9.714   -33.974 1.00 73.42 ? 105 ARG   B CZ  1 
ATOM   1003 N  NH1 . ARG   B 2 96  ? -20.607 10.974  -33.545 1.00 73.46 ? 105 ARG   B NH1 1 
ATOM   1004 N  NH2 . ARG   B 2 96  ? -20.025 9.367   -35.081 1.00 74.44 ? 105 ARG   B NH2 1 
ATOM   1005 N  N   . ALA   B 2 97  ? -20.268 6.855   -28.141 1.00 49.53 ? 106 ALA   B N   1 
ATOM   1006 C  CA  . ALA   B 2 97  ? -20.145 5.468   -27.683 1.00 50.18 ? 106 ALA   B CA  1 
ATOM   1007 C  C   . ALA   B 2 97  ? -19.729 4.574   -28.858 1.00 50.76 ? 106 ALA   B C   1 
ATOM   1008 O  O   . ALA   B 2 97  ? -20.249 4.737   -29.963 1.00 51.09 ? 106 ALA   B O   1 
ATOM   1009 C  CB  . ALA   B 2 97  ? -21.465 4.997   -27.098 1.00 50.18 ? 106 ALA   B CB  1 
ATOM   1010 N  N   . LYS   B 2 98  ? -18.752 3.687   -28.648 1.00 50.70 ? 107 LYS   B N   1 
ATOM   1011 C  CA  . LYS   B 2 98  ? -18.218 2.873   -29.744 1.00 51.16 ? 107 LYS   B CA  1 
ATOM   1012 C  C   . LYS   B 2 98  ? -17.965 1.402   -29.330 1.00 50.49 ? 107 LYS   B C   1 
ATOM   1013 O  O   . LYS   B 2 98  ? -17.349 1.162   -28.301 1.00 50.54 ? 107 LYS   B O   1 
ATOM   1014 C  CB  . LYS   B 2 98  ? -16.914 3.536   -30.207 1.00 54.15 ? 107 LYS   B CB  1 
ATOM   1015 C  CG  . LYS   B 2 98  ? -16.246 2.902   -31.413 1.00 60.47 ? 107 LYS   B CG  1 
ATOM   1016 C  CD  . LYS   B 2 98  ? -14.939 3.645   -31.790 1.00 66.46 ? 107 LYS   B CD  1 
ATOM   1017 C  CE  . LYS   B 2 98  ? -14.001 3.876   -30.606 1.00 70.55 ? 107 LYS   B CE  1 
ATOM   1018 N  NZ  . LYS   B 2 98  ? -12.609 3.418   -30.893 1.00 72.93 ? 107 LYS   B NZ  1 
ATOM   1019 N  N   . ASN   B 2 99  ? -18.433 0.424   -30.129 1.00 49.47 ? 108 ASN   B N   1 
ATOM   1020 C  CA  . ASN   B 2 99  ? -18.253 -0.992  -29.796 1.00 48.42 ? 108 ASN   B CA  1 
ATOM   1021 C  C   . ASN   B 2 99  ? -16.966 -1.539  -30.353 1.00 48.06 ? 108 ASN   B C   1 
ATOM   1022 O  O   . ASN   B 2 99  ? -16.771 -1.535  -31.554 1.00 48.44 ? 108 ASN   B O   1 
ATOM   1023 C  CB  . ASN   B 2 99  ? -19.396 -1.832  -30.322 1.00 48.36 ? 108 ASN   B CB  1 
ATOM   1024 C  CG  . ASN   B 2 99  ? -20.674 -1.667  -29.570 1.00 50.65 ? 108 ASN   B CG  1 
ATOM   1025 O  OD1 . ASN   B 2 99  ? -21.283 -0.588  -29.550 1.00 52.41 ? 108 ASN   B OD1 1 
ATOM   1026 N  ND2 . ASN   B 2 99  ? -21.137 -2.745  -28.973 1.00 50.24 ? 108 ASN   B ND2 1 
ATOM   1027 N  N   . ILE   B 2 100 ? -16.096 -2.038  -29.491 1.00 47.53 ? 109 ILE   B N   1 
ATOM   1028 C  CA  . ILE   B 2 100 ? -14.819 -2.606  -29.908 1.00 47.46 ? 109 ILE   B CA  1 
ATOM   1029 C  C   . ILE   B 2 100 ? -14.764 -4.062  -29.531 1.00 47.36 ? 109 ILE   B C   1 
ATOM   1030 O  O   . ILE   B 2 100 ? -14.754 -4.405  -28.362 1.00 47.88 ? 109 ILE   B O   1 
ATOM   1031 C  CB  . ILE   B 2 100 ? -13.639 -1.850  -29.286 1.00 47.88 ? 109 ILE   B CB  1 
ATOM   1032 C  CG1 . ILE   B 2 100 ? -13.762 -0.335  -29.497 1.00 49.21 ? 109 ILE   B CG1 1 
ATOM   1033 C  CG2 . ILE   B 2 100 ? -12.320 -2.407  -29.795 1.00 48.09 ? 109 ILE   B CG2 1 
ATOM   1034 C  CD1 . ILE   B 2 100 ? -13.803 0.112   -30.923 1.00 50.76 ? 109 ILE   B CD1 1 
ATOM   1035 N  N   . GLN   B 2 101 ? -14.714 -4.916  -30.519 1.00 47.39 ? 110 GLN   B N   1 
ATOM   1036 C  CA  . GLN   B 2 101 ? -14.689 -6.348  -30.333 1.00 47.64 ? 110 GLN   B CA  1 
ATOM   1037 C  C   . GLN   B 2 101 ? -13.268 -6.838  -30.064 1.00 47.81 ? 110 GLN   B C   1 
ATOM   1038 O  O   . GLN   B 2 101 ? -12.344 -6.423  -30.754 1.00 47.87 ? 110 GLN   B O   1 
ATOM   1039 C  CB  . GLN   B 2 101 ? -15.272 -7.006  -31.580 1.00 48.94 ? 110 GLN   B CB  1 
ATOM   1040 C  CG  . GLN   B 2 101 ? -15.396 -8.494  -31.440 1.00 52.52 ? 110 GLN   B CG  1 
ATOM   1041 C  CD  . GLN   B 2 101 ? -16.424 -9.081  -32.351 1.00 56.80 ? 110 GLN   B CD  1 
ATOM   1042 O  OE1 . GLN   B 2 101 ? -17.377 -8.419  -32.779 1.00 58.93 ? 110 GLN   B OE1 1 
ATOM   1043 N  NE2 . GLN   B 2 101 ? -16.260 -10.357 -32.646 1.00 57.20 ? 110 GLN   B NE2 1 
ATOM   1044 N  N   . THR   B 2 102 ? -13.083 -7.702  -29.049 1.00 47.51 ? 111 THR   B N   1 
ATOM   1045 C  CA  . THR   B 2 102 ? -11.764 -8.223  -28.704 1.00 48.14 ? 111 THR   B CA  1 
ATOM   1046 C  C   . THR   B 2 102 ? -11.854 -9.618  -28.056 1.00 48.17 ? 111 THR   B C   1 
ATOM   1047 O  O   . THR   B 2 102 ? -12.934 -10.026 -27.650 1.00 47.90 ? 111 THR   B O   1 
ATOM   1048 C  CB  . THR   B 2 102 ? -11.067 -7.223  -27.748 1.00 50.40 ? 111 THR   B CB  1 
ATOM   1049 O  OG1 . THR   B 2 102 ? -9.682  -7.553  -27.595 1.00 52.29 ? 111 THR   B OG1 1 
ATOM   1050 C  CG2 . THR   B 2 102 ? -11.746 -7.129  -26.401 1.00 50.79 ? 111 THR   B CG2 1 
ATOM   1051 N  N   . LEU   B 2 103 ? -10.727 -10.367 -27.977 1.00 48.37 ? 112 LEU   B N   1 
ATOM   1052 C  CA  . LEU   B 2 103 ? -10.717 -11.648 -27.271 1.00 48.91 ? 112 LEU   B CA  1 
ATOM   1053 C  C   . LEU   B 2 103 ? -9.950  -11.371 -26.018 1.00 50.51 ? 112 LEU   B C   1 
ATOM   1054 O  O   . LEU   B 2 103 ? -8.774  -11.016 -26.097 1.00 50.54 ? 112 LEU   B O   1 
ATOM   1055 C  CB  . LEU   B 2 103 ? -10.041 -12.807 -27.998 1.00 48.46 ? 112 LEU   B CB  1 
ATOM   1056 C  CG  . LEU   B 2 103 ? -9.977  -14.087 -27.127 1.00 49.47 ? 112 LEU   B CG  1 
ATOM   1057 C  CD1 . LEU   B 2 103 ? -11.266 -14.847 -27.159 1.00 49.83 ? 112 LEU   B CD1 1 
ATOM   1058 C  CD2 . LEU   B 2 103 ? -8.784  -14.933 -27.436 1.00 49.62 ? 112 LEU   B CD2 1 
ATOM   1059 N  N   . PRO   B 2 104 ? -10.584 -11.576 -24.850 1.00 51.51 ? 113 PRO   B N   1 
ATOM   1060 C  CA  . PRO   B 2 104 ? -9.898  -11.275 -23.595 1.00 52.43 ? 113 PRO   B CA  1 
ATOM   1061 C  C   . PRO   B 2 104 ? -8.704  -12.152 -23.232 1.00 54.07 ? 113 PRO   B C   1 
ATOM   1062 O  O   . PRO   B 2 104 ? -8.558  -13.306 -23.666 1.00 54.83 ? 113 PRO   B O   1 
ATOM   1063 C  CB  . PRO   B 2 104 ? -11.010 -11.403 -22.547 1.00 52.80 ? 113 PRO   B CB  1 
ATOM   1064 C  CG  . PRO   B 2 104 ? -12.281 -11.318 -23.315 1.00 52.78 ? 113 PRO   B CG  1 
ATOM   1065 C  CD  . PRO   B 2 104 ? -11.986 -11.969 -24.614 1.00 50.80 ? 113 PRO   B CD  1 
ATOM   1066 N  N   . GLY   B 2 105 ? -7.842  -11.551 -22.431 1.00 54.31 ? 114 GLY   B N   1 
ATOM   1067 C  CA  . GLY   B 2 105 ? -6.699  -12.185 -21.811 1.00 55.03 ? 114 GLY   B CA  1 
ATOM   1068 C  C   . GLY   B 2 105 ? -7.064  -12.612 -20.397 1.00 55.84 ? 114 GLY   B C   1 
ATOM   1069 O  O   . GLY   B 2 105 ? -8.245  -12.661 -20.041 1.00 56.26 ? 114 GLY   B O   1 
ATOM   1070 N  N   . ILE   B 2 106 ? -6.064  -12.940 -19.574 1.00 55.82 ? 115 ILE   B N   1 
ATOM   1071 C  CA  . ILE   B 2 106 ? -6.302  -13.422 -18.222 1.00 56.23 ? 115 ILE   B CA  1 
ATOM   1072 C  C   . ILE   B 2 106 ? -5.465  -12.659 -17.202 1.00 56.27 ? 115 ILE   B C   1 
ATOM   1073 O  O   . ILE   B 2 106 ? -4.320  -12.299 -17.465 1.00 56.72 ? 115 ILE   B O   1 
ATOM   1074 C  CB  . ILE   B 2 106 ? -5.951  -14.939 -18.157 1.00 57.29 ? 115 ILE   B CB  1 
ATOM   1075 C  CG1 . ILE   B 2 106 ? -6.817  -15.790 -19.097 1.00 58.55 ? 115 ILE   B CG1 1 
ATOM   1076 C  CG2 . ILE   B 2 106 ? -5.971  -15.484 -16.743 1.00 58.01 ? 115 ILE   B CG2 1 
ATOM   1077 C  CD1 . ILE   B 2 106 ? -8.229  -15.718 -18.846 1.00 59.88 ? 115 ILE   B CD1 1 
ATOM   1078 N  N   . PHE   B 2 107 ? -6.035  -12.457 -16.021 1.00 55.56 ? 116 PHE   B N   1 
ATOM   1079 C  CA  . PHE   B 2 107 ? -5.396  -11.884 -14.863 1.00 55.09 ? 116 PHE   B CA  1 
ATOM   1080 C  C   . PHE   B 2 107 ? -5.320  -13.068 -13.923 1.00 55.45 ? 116 PHE   B C   1 
ATOM   1081 O  O   . PHE   B 2 107 ? -6.329  -13.427 -13.325 1.00 55.60 ? 116 PHE   B O   1 
ATOM   1082 C  CB  . PHE   B 2 107 ? -6.294  -10.806 -14.240 1.00 54.44 ? 116 PHE   B CB  1 
ATOM   1083 C  CG  . PHE   B 2 107 ? -5.935  -9.379  -14.568 1.00 54.60 ? 116 PHE   B CG  1 
ATOM   1084 C  CD1 . PHE   B 2 107 ? -5.235  -9.070  -15.721 1.00 55.15 ? 116 PHE   B CD1 1 
ATOM   1085 C  CD2 . PHE   B 2 107 ? -6.323  -8.342  -13.738 1.00 55.42 ? 116 PHE   B CD2 1 
ATOM   1086 C  CE1 . PHE   B 2 107 ? -4.915  -7.753  -16.031 1.00 55.70 ? 116 PHE   B CE1 1 
ATOM   1087 C  CE2 . PHE   B 2 107 ? -6.002  -7.023  -14.050 1.00 56.14 ? 116 PHE   B CE2 1 
ATOM   1088 C  CZ  . PHE   B 2 107 ? -5.304  -6.739  -15.197 1.00 55.72 ? 116 PHE   B CZ  1 
ATOM   1089 N  N   . LYS   B 2 108 ? -4.168  -13.735 -13.855 1.00 55.45 ? 117 LYS   B N   1 
ATOM   1090 C  CA  . LYS   B 2 108 ? -3.969  -14.862 -12.955 1.00 55.95 ? 117 LYS   B CA  1 
ATOM   1091 C  C   . LYS   B 2 108 ? -3.643  -14.305 -11.557 1.00 56.28 ? 117 LYS   B C   1 
ATOM   1092 O  O   . LYS   B 2 108 ? -2.624  -13.637 -11.405 1.00 56.30 ? 117 LYS   B O   1 
ATOM   1093 C  CB  . LYS   B 2 108 ? -2.803  -15.738 -13.461 1.00 58.11 ? 117 LYS   B CB  1 
ATOM   1094 C  CG  . LYS   B 2 108 ? -3.201  -16.851 -14.428 1.00 62.46 ? 117 LYS   B CG  1 
ATOM   1095 C  CD  . LYS   B 2 108 ? -2.727  -18.212 -13.893 1.00 67.90 ? 117 LYS   B CD  1 
ATOM   1096 C  CE  . LYS   B 2 108 ? -3.130  -19.414 -14.725 1.00 72.60 ? 117 LYS   B CE  1 
ATOM   1097 N  NZ  . LYS   B 2 108 ? -2.384  -19.509 -16.020 1.00 76.49 ? 117 LYS   B NZ  1 
ATOM   1098 N  N   . THR   B 2 109 ? -4.509  -14.545 -10.547 1.00 56.49 ? 118 THR   B N   1 
ATOM   1099 C  CA  . THR   B 2 109 ? -4.282  -14.049 -9.177  1.00 57.41 ? 118 THR   B CA  1 
ATOM   1100 C  C   . THR   B 2 109 ? -4.177  -15.206 -8.135  1.00 58.03 ? 118 THR   B C   1 
ATOM   1101 O  O   . THR   B 2 109 ? -4.471  -16.349 -8.465  1.00 57.99 ? 118 THR   B O   1 
ATOM   1102 C  CB  . THR   B 2 109 ? -5.349  -12.985 -8.753  1.00 58.91 ? 118 THR   B CB  1 
ATOM   1103 O  OG1 . THR   B 2 109 ? -6.483  -13.623 -8.154  1.00 59.97 ? 118 THR   B OG1 1 
ATOM   1104 C  CG2 . THR   B 2 109 ? -5.769  -12.046 -9.880  1.00 59.45 ? 118 THR   B CG2 1 
ATOM   1105 N  N   . LYS   B 2 110 ? -3.812  -14.902 -6.868  1.00 58.53 ? 119 LYS   B N   1 
ATOM   1106 C  CA  . LYS   B 2 110 ? -3.744  -15.923 -5.812  1.00 59.11 ? 119 LYS   B CA  1 
ATOM   1107 C  C   . LYS   B 2 110 ? -5.127  -16.496 -5.428  1.00 59.62 ? 119 LYS   B C   1 
ATOM   1108 O  O   . LYS   B 2 110 ? -5.198  -17.546 -4.799  1.00 59.93 ? 119 LYS   B O   1 
ATOM   1109 C  CB  . LYS   B 2 110 ? -2.991  -15.405 -4.579  1.00 60.68 ? 119 LYS   B CB  1 
ATOM   1110 C  CG  . LYS   B 2 110 ? -3.812  -14.484 -3.670  1.00 64.92 ? 119 LYS   B CG  1 
ATOM   1111 C  CD  . LYS   B 2 110 ? -2.939  -13.777 -2.630  1.00 68.44 ? 119 LYS   B CD  1 
ATOM   1112 C  CE  . LYS   B 2 110 ? -3.708  -13.370 -1.397  1.00 72.32 ? 119 LYS   B CE  1 
ATOM   1113 N  NZ  . LYS   B 2 110 ? -4.758  -12.365 -1.700  1.00 74.89 ? 119 LYS   B NZ  1 
ATOM   1114 N  N   . ASP   B 2 111 ? -6.218  -15.836 -5.834  1.00 59.67 ? 120 ASP   B N   1 
ATOM   1115 C  CA  . ASP   B 2 111 ? -7.567  -16.313 -5.536  1.00 59.96 ? 120 ASP   B CA  1 
ATOM   1116 C  C   . ASP   B 2 111 ? -8.345  -16.795 -6.779  1.00 59.45 ? 120 ASP   B C   1 
ATOM   1117 O  O   . ASP   B 2 111 ? -9.553  -16.990 -6.701  1.00 59.62 ? 120 ASP   B O   1 
ATOM   1118 C  CB  . ASP   B 2 111 ? -8.363  -15.226 -4.800  1.00 62.10 ? 120 ASP   B CB  1 
ATOM   1119 C  CG  . ASP   B 2 111 ? -7.717  -14.785 -3.504  1.00 68.12 ? 120 ASP   B CG  1 
ATOM   1120 O  OD1 . ASP   B 2 111 ? -7.384  -15.666 -2.672  1.00 69.61 ? 120 ASP   B OD1 1 
ATOM   1121 O  OD2 . ASP   B 2 111 ? -7.547  -13.565 -3.315  1.00 70.27 ? 120 ASP   B OD2 1 
ATOM   1122 N  N   . GLY   B 2 112 ? -7.666  -16.985 -7.901  1.00 58.75 ? 121 GLY   B N   1 
ATOM   1123 C  CA  . GLY   B 2 112 ? -8.321  -17.443 -9.122  1.00 58.61 ? 121 GLY   B CA  1 
ATOM   1124 C  C   . GLY   B 2 112 ? -8.128  -16.511 -10.296 1.00 57.89 ? 121 GLY   B C   1 
ATOM   1125 O  O   . GLY   B 2 112 ? -7.574  -15.423 -10.138 1.00 58.21 ? 121 GLY   B O   1 
ATOM   1126 N  N   . ASP   B 2 113 ? -8.572  -16.936 -11.485 1.00 56.60 ? 122 ASP   B N   1 
ATOM   1127 C  CA  . ASP   B 2 113 ? -8.397  -16.141 -12.684 1.00 56.02 ? 122 ASP   B CA  1 
ATOM   1128 C  C   . ASP   B 2 113 ? -9.630  -15.312 -13.055 1.00 54.94 ? 122 ASP   B C   1 
ATOM   1129 O  O   . ASP   B 2 113 ? -10.755 -15.667 -12.714 1.00 55.31 ? 122 ASP   B O   1 
ATOM   1130 C  CB  . ASP   B 2 113 ? -7.967  -17.026 -13.860 1.00 58.26 ? 122 ASP   B CB  1 
ATOM   1131 C  CG  . ASP   B 2 113 ? -6.692  -17.819 -13.645 1.00 64.02 ? 122 ASP   B CG  1 
ATOM   1132 O  OD1 . ASP   B 2 113 ? -6.053  -17.642 -12.595 1.00 64.78 ? 122 ASP   B OD1 1 
ATOM   1133 O  OD2 . ASP   B 2 113 ? -6.337  -18.617 -14.533 1.00 67.91 ? 122 ASP   B OD2 1 
ATOM   1134 N  N   . ILE   B 2 114 ? -9.401  -14.212 -13.784 1.00 53.17 ? 123 ILE   B N   1 
ATOM   1135 C  CA  . ILE   B 2 114 ? -10.421 -13.279 -14.237 1.00 51.72 ? 123 ILE   B CA  1 
ATOM   1136 C  C   . ILE   B 2 114 ? -10.008 -12.734 -15.610 1.00 50.76 ? 123 ILE   B C   1 
ATOM   1137 O  O   . ILE   B 2 114 ? -8.823  -12.559 -15.876 1.00 49.76 ? 123 ILE   B O   1 
ATOM   1138 C  CB  . ILE   B 2 114 ? -10.600 -12.204 -13.135 1.00 51.92 ? 123 ILE   B CB  1 
ATOM   1139 C  CG1 . ILE   B 2 114 ? -11.822 -12.507 -12.275 1.00 53.50 ? 123 ILE   B CG1 1 
ATOM   1140 C  CG2 . ILE   B 2 114 ? -10.587 -10.769 -13.593 1.00 51.74 ? 123 ILE   B CG2 1 
ATOM   1141 C  CD1 . ILE   B 2 114 ? -11.477 -12.613 -10.783 1.00 54.97 ? 123 ILE   B CD1 1 
ATOM   1142 N  N   . GLY   B 2 115 ? -10.986 -12.515 -16.486 1.00 50.48 ? 124 GLY   B N   1 
ATOM   1143 C  CA  . GLY   B 2 115 ? -10.724 -11.980 -17.815 1.00 50.44 ? 124 GLY   B CA  1 
ATOM   1144 C  C   . GLY   B 2 115 ? -10.102 -10.598 -17.775 1.00 50.22 ? 124 GLY   B C   1 
ATOM   1145 O  O   . GLY   B 2 115 ? -10.218 -9.879  -16.778 1.00 50.71 ? 124 GLY   B O   1 
ATOM   1146 N  N   . ALA   B 2 116 ? -9.415  -10.233 -18.845 1.00 49.75 ? 125 ALA   B N   1 
ATOM   1147 C  CA  . ALA   B 2 116 ? -8.755  -8.941  -18.981 1.00 49.85 ? 125 ALA   B CA  1 
ATOM   1148 C  C   . ALA   B 2 116 ? -8.900  -8.406  -20.402 1.00 49.94 ? 125 ALA   B C   1 
ATOM   1149 O  O   . ALA   B 2 116 ? -8.699  -9.141  -21.360 1.00 50.00 ? 125 ALA   B O   1 
ATOM   1150 C  CB  . ALA   B 2 116 ? -7.285  -9.060  -18.625 1.00 49.87 ? 125 ALA   B CB  1 
ATOM   1151 N  N   . VAL   B 2 117 ? -9.256  -7.135  -20.542 1.00 49.62 ? 126 VAL   B N   1 
ATOM   1152 C  CA  A VAL   B 2 117 ? -9.390  -6.521  -21.860 0.50 50.05 ? 126 VAL   B CA  1 
ATOM   1153 C  CA  B VAL   B 2 117 ? -9.421  -6.502  -21.843 0.50 50.13 ? 126 VAL   B CA  1 
ATOM   1154 C  C   . VAL   B 2 117 ? -8.223  -5.583  -22.090 1.00 50.52 ? 126 VAL   B C   1 
ATOM   1155 O  O   . VAL   B 2 117 ? -7.952  -4.727  -21.253 1.00 50.90 ? 126 VAL   B O   1 
ATOM   1156 C  CB  A VAL   B 2 117 ? -10.768 -5.874  -22.128 0.50 50.75 ? 126 VAL   B CB  1 
ATOM   1157 C  CB  B VAL   B 2 117 ? -10.757 -5.731  -21.867 0.50 50.97 ? 126 VAL   B CB  1 
ATOM   1158 C  CG1 A VAL   B 2 117 ? -11.779 -6.922  -22.577 0.50 51.12 ? 126 VAL   B CG1 1 
ATOM   1159 C  CG1 B VAL   B 2 117 ? -10.849 -4.813  -23.074 0.50 51.68 ? 126 VAL   B CG1 1 
ATOM   1160 C  CG2 A VAL   B 2 117 ? -11.278 -5.118  -20.907 0.50 51.45 ? 126 VAL   B CG2 1 
ATOM   1161 C  CG2 B VAL   B 2 117 ? -11.940 -6.691  -21.815 0.50 51.32 ? 126 VAL   B CG2 1 
ATOM   1162 N  N   . ALA   B 2 118 ? -7.468  -5.794  -23.191 1.00 50.45 ? 127 ALA   B N   1 
ATOM   1163 C  CA  . ALA   B 2 118 ? -6.295  -4.964  -23.457 1.00 50.67 ? 127 ALA   B CA  1 
ATOM   1164 C  C   . ALA   B 2 118 ? -6.585  -3.838  -24.438 1.00 51.50 ? 127 ALA   B C   1 
ATOM   1165 O  O   . ALA   B 2 118 ? -6.034  -3.787  -25.540 1.00 51.39 ? 127 ALA   B O   1 
ATOM   1166 C  CB  . ALA   B 2 118 ? -5.125  -5.810  -23.912 1.00 50.14 ? 127 ALA   B CB  1 
ATOM   1167 N  N   . LEU   B 2 119 ? -7.445  -2.905  -24.009 1.00 51.50 ? 128 LEU   B N   1 
ATOM   1168 C  CA  . LEU   B 2 119 ? -7.799  -1.769  -24.844 1.00 51.62 ? 128 LEU   B CA  1 
ATOM   1169 C  C   . LEU   B 2 119 ? -7.382  -0.482  -24.147 1.00 52.09 ? 128 LEU   B C   1 
ATOM   1170 O  O   . LEU   B 2 119 ? -7.772  -0.257  -23.021 1.00 52.31 ? 128 LEU   B O   1 
ATOM   1171 C  CB  . LEU   B 2 119 ? -9.303  -1.800  -25.140 1.00 51.41 ? 128 LEU   B CB  1 
ATOM   1172 C  CG  . LEU   B 2 119 ? -9.708  -2.864  -26.166 1.00 52.23 ? 128 LEU   B CG  1 
ATOM   1173 C  CD1 . LEU   B 2 119 ? -11.207 -3.019  -26.243 1.00 52.20 ? 128 LEU   B CD1 1 
ATOM   1174 C  CD2 . LEU   B 2 119 ? -9.148  -2.538  -27.547 1.00 52.80 ? 128 LEU   B CD2 1 
ATOM   1175 N  N   . ASP   B 2 120 ? -6.542  0.334   -24.786 1.00 52.49 ? 129 ASP   B N   1 
ATOM   1176 C  CA  . ASP   B 2 120 ? -6.067  1.600   -24.218 1.00 53.09 ? 129 ASP   B CA  1 
ATOM   1177 C  C   . ASP   B 2 120 ? -7.083  2.720   -24.397 1.00 52.80 ? 129 ASP   B C   1 
ATOM   1178 O  O   . ASP   B 2 120 ? -7.349  3.115   -25.526 1.00 52.87 ? 129 ASP   B O   1 
ATOM   1179 C  CB  . ASP   B 2 120 ? -4.785  2.032   -24.925 1.00 56.20 ? 129 ASP   B CB  1 
ATOM   1180 C  CG  . ASP   B 2 120 ? -3.572  1.297   -24.435 1.00 63.45 ? 129 ASP   B CG  1 
ATOM   1181 O  OD1 . ASP   B 2 120 ? -2.857  1.850   -23.567 1.00 65.81 ? 129 ASP   B OD1 1 
ATOM   1182 O  OD2 . ASP   B 2 120 ? -3.352  0.147   -24.882 1.00 65.36 ? 129 ASP   B OD2 1 
ATOM   1183 N  N   . TYR   B 2 121 ? -7.617  3.268   -23.297 1.00 52.10 ? 130 TYR   B N   1 
ATOM   1184 C  CA  . TYR   B 2 121 ? -8.575  4.378   -23.358 1.00 51.64 ? 130 TYR   B CA  1 
ATOM   1185 C  C   . TYR   B 2 121 ? -8.310  5.351   -22.209 1.00 51.30 ? 130 TYR   B C   1 
ATOM   1186 O  O   . TYR   B 2 121 ? -7.823  4.934   -21.149 1.00 51.72 ? 130 TYR   B O   1 
ATOM   1187 C  CB  . TYR   B 2 121 ? -10.008 3.851   -23.238 1.00 51.60 ? 130 TYR   B CB  1 
ATOM   1188 C  CG  . TYR   B 2 121 ? -10.621 3.419   -24.545 1.00 52.57 ? 130 TYR   B CG  1 
ATOM   1189 C  CD1 . TYR   B 2 121 ? -11.343 4.312   -25.324 1.00 53.72 ? 130 TYR   B CD1 1 
ATOM   1190 C  CD2 . TYR   B 2 121 ? -10.539 2.101   -24.971 1.00 53.43 ? 130 TYR   B CD2 1 
ATOM   1191 C  CE1 . TYR   B 2 121 ? -11.920 3.917   -26.524 1.00 54.69 ? 130 TYR   B CE1 1 
ATOM   1192 C  CE2 . TYR   B 2 121 ? -11.127 1.688   -26.157 1.00 54.35 ? 130 TYR   B CE2 1 
ATOM   1193 C  CZ  . TYR   B 2 121 ? -11.796 2.605   -26.944 1.00 55.28 ? 130 TYR   B CZ  1 
ATOM   1194 O  OH  . TYR   B 2 121 ? -12.406 2.196   -28.099 1.00 56.26 ? 130 TYR   B OH  1 
ATOM   1195 N  N   . PRO   B 2 122 ? -8.684  6.636   -22.356 1.00 50.18 ? 131 PRO   B N   1 
ATOM   1196 C  CA  . PRO   B 2 122 ? -8.476  7.583   -21.254 1.00 49.57 ? 131 PRO   B CA  1 
ATOM   1197 C  C   . PRO   B 2 122 ? -9.199  7.177   -19.975 1.00 49.01 ? 131 PRO   B C   1 
ATOM   1198 O  O   . PRO   B 2 122 ? -10.236 6.510   -20.045 1.00 49.48 ? 131 PRO   B O   1 
ATOM   1199 C  CB  . PRO   B 2 122 ? -9.042  8.897   -21.812 1.00 50.11 ? 131 PRO   B CB  1 
ATOM   1200 C  CG  . PRO   B 2 122 ? -8.976  8.749   -23.276 1.00 50.35 ? 131 PRO   B CG  1 
ATOM   1201 C  CD  . PRO   B 2 122 ? -9.283  7.305   -23.525 1.00 49.29 ? 131 PRO   B CD  1 
ATOM   1202 N  N   . ALA   B 2 123 ? -8.666  7.605   -18.808 1.00 47.67 ? 132 ALA   B N   1 
ATOM   1203 C  CA  . ALA   B 2 123 ? -9.226  7.330   -17.482 1.00 46.64 ? 132 ALA   B CA  1 
ATOM   1204 C  C   . ALA   B 2 123 ? -10.733 7.593   -17.357 1.00 45.62 ? 132 ALA   B C   1 
ATOM   1205 O  O   . ALA   B 2 123 ? -11.431 6.791   -16.751 1.00 45.96 ? 132 ALA   B O   1 
ATOM   1206 C  CB  . ALA   B 2 123 ? -8.459  8.097   -16.413 1.00 46.55 ? 132 ALA   B CB  1 
ATOM   1207 N  N   . GLY   B 2 124 ? -11.223 8.668   -17.973 1.00 44.36 ? 133 GLY   B N   1 
ATOM   1208 C  CA  . GLY   B 2 124 ? -12.636 9.039   -17.968 1.00 43.42 ? 133 GLY   B CA  1 
ATOM   1209 C  C   . GLY   B 2 124 ? -13.588 8.052   -18.618 1.00 42.21 ? 133 GLY   B C   1 
ATOM   1210 O  O   . GLY   B 2 124 ? -14.800 8.260   -18.613 1.00 42.05 ? 133 GLY   B O   1 
ATOM   1211 N  N   . THR   B 2 125 ? -13.047 6.976   -19.190 1.00 41.33 ? 134 THR   B N   1 
ATOM   1212 C  CA  . THR   B 2 125 ? -13.805 5.899   -19.832 1.00 40.54 ? 134 THR   B CA  1 
ATOM   1213 C  C   . THR   B 2 125 ? -14.068 4.743   -18.822 1.00 40.22 ? 134 THR   B C   1 
ATOM   1214 O  O   . THR   B 2 125 ? -14.831 3.842   -19.139 1.00 39.82 ? 134 THR   B O   1 
ATOM   1215 C  CB  . THR   B 2 125 ? -13.076 5.454   -21.158 1.00 40.91 ? 134 THR   B CB  1 
ATOM   1216 O  OG1 . THR   B 2 125 ? -12.588 6.601   -21.849 1.00 41.76 ? 134 THR   B OG1 1 
ATOM   1217 C  CG2 . THR   B 2 125 ? -13.961 4.673   -22.113 1.00 40.30 ? 134 THR   B CG2 1 
ATOM   1218 N  N   . SER   B 2 126 ? -13.476 4.786   -17.586 1.00 40.82 ? 135 SER   B N   1 
ATOM   1219 C  CA  . SER   B 2 126 ? -13.664 3.754   -16.546 1.00 41.45 ? 135 SER   B CA  1 
ATOM   1220 C  C   . SER   B 2 126 ? -15.137 3.605   -16.240 1.00 41.31 ? 135 SER   B C   1 
ATOM   1221 O  O   . SER   B 2 126 ? -15.810 4.600   -15.997 1.00 41.48 ? 135 SER   B O   1 
ATOM   1222 C  CB  . SER   B 2 126 ? -12.959 4.127   -15.247 1.00 43.82 ? 135 SER   B CB  1 
ATOM   1223 O  OG  . SER   B 2 126 ? -11.827 4.966   -15.397 1.00 47.98 ? 135 SER   B OG  1 
ATOM   1224 N  N   . GLY   B 2 127 ? -15.623 2.378   -16.258 1.00 40.58 ? 136 GLY   B N   1 
ATOM   1225 C  CA  . GLY   B 2 127 ? -17.024 2.079   -16.001 1.00 40.89 ? 136 GLY   B CA  1 
ATOM   1226 C  C   . GLY   B 2 127 ? -17.796 1.629   -17.231 1.00 41.12 ? 136 GLY   B C   1 
ATOM   1227 O  O   . GLY   B 2 127 ? -18.982 1.300   -17.116 1.00 41.90 ? 136 GLY   B O   1 
ATOM   1228 N  N   . SER   B 2 128 ? -17.142 1.640   -18.425 1.00 39.65 ? 137 SER   B N   1 
ATOM   1229 C  CA  . SER   B 2 128 ? -17.732 1.216   -19.682 1.00 38.85 ? 137 SER   B CA  1 
ATOM   1230 C  C   . SER   B 2 128 ? -18.003 -0.274  -19.645 1.00 38.66 ? 137 SER   B C   1 
ATOM   1231 O  O   . SER   B 2 128 ? -17.151 -1.049  -19.213 1.00 38.74 ? 137 SER   B O   1 
ATOM   1232 C  CB  . SER   B 2 128 ? -16.808 1.558   -20.846 1.00 39.18 ? 137 SER   B CB  1 
ATOM   1233 O  OG  . SER   B 2 128 ? -16.707 2.963   -20.984 1.00 39.68 ? 137 SER   B OG  1 
ATOM   1234 N  N   . PRO   B 2 129 ? -19.207 -0.693  -20.057 1.00 38.39 ? 138 PRO   B N   1 
ATOM   1235 C  CA  . PRO   B 2 129 ? -19.545 -2.117  -19.974 1.00 38.64 ? 138 PRO   B CA  1 
ATOM   1236 C  C   . PRO   B 2 129 ? -18.855 -3.016  -20.985 1.00 39.83 ? 138 PRO   B C   1 
ATOM   1237 O  O   . PRO   B 2 129 ? -18.559 -2.594  -22.092 1.00 39.47 ? 138 PRO   B O   1 
ATOM   1238 C  CB  . PRO   B 2 129 ? -21.059 -2.129  -20.194 1.00 38.66 ? 138 PRO   B CB  1 
ATOM   1239 C  CG  . PRO   B 2 129 ? -21.349 -0.901  -20.953 1.00 38.76 ? 138 PRO   B CG  1 
ATOM   1240 C  CD  . PRO   B 2 129 ? -20.340 0.114   -20.558 1.00 37.50 ? 138 PRO   B CD  1 
ATOM   1241 N  N   . ILE   B 2 130 ? -18.629 -4.276  -20.596 1.00 40.89 ? 139 ILE   B N   1 
ATOM   1242 C  CA  . ILE   B 2 130 ? -18.089 -5.327  -21.456 1.00 42.10 ? 139 ILE   B CA  1 
ATOM   1243 C  C   . ILE   B 2 130 ? -19.269 -6.284  -21.720 1.00 43.11 ? 139 ILE   B C   1 
ATOM   1244 O  O   . ILE   B 2 130 ? -19.943 -6.692  -20.782 1.00 42.70 ? 139 ILE   B O   1 
ATOM   1245 C  CB  . ILE   B 2 130 ? -16.899 -6.031  -20.792 1.00 42.75 ? 139 ILE   B CB  1 
ATOM   1246 C  CG1 . ILE   B 2 130 ? -15.741 -5.039  -20.587 1.00 43.93 ? 139 ILE   B CG1 1 
ATOM   1247 C  CG2 . ILE   B 2 130 ? -16.452 -7.231  -21.613 1.00 43.30 ? 139 ILE   B CG2 1 
ATOM   1248 C  CD1 . ILE   B 2 130 ? -14.715 -5.498  -19.523 1.00 45.01 ? 139 ILE   B CD1 1 
ATOM   1249 N  N   . LEU   B 2 131 ? -19.563 -6.577  -22.991 1.00 43.85 ? 140 LEU   B N   1 
ATOM   1250 C  CA  . LEU   B 2 131 ? -20.738 -7.366  -23.351 1.00 45.41 ? 140 LEU   B CA  1 
ATOM   1251 C  C   . LEU   B 2 131 ? -20.443 -8.700  -24.024 1.00 47.24 ? 140 LEU   B C   1 
ATOM   1252 O  O   . LEU   B 2 131 ? -19.472 -8.832  -24.773 1.00 47.15 ? 140 LEU   B O   1 
ATOM   1253 C  CB  . LEU   B 2 131 ? -21.704 -6.563  -24.260 1.00 45.70 ? 140 LEU   B CB  1 
ATOM   1254 C  CG  . LEU   B 2 131 ? -21.456 -5.065  -24.445 1.00 46.82 ? 140 LEU   B CG  1 
ATOM   1255 C  CD1 . LEU   B 2 131 ? -22.091 -4.559  -25.691 1.00 46.83 ? 140 LEU   B CD1 1 
ATOM   1256 C  CD2 . LEU   B 2 131 ? -21.938 -4.302  -23.253 1.00 47.88 ? 140 LEU   B CD2 1 
ATOM   1257 N  N   . ASP   B 2 132 ? -21.323 -9.683  -23.783 1.00 48.80 ? 141 ASP   B N   1 
ATOM   1258 C  CA  . ASP   B 2 132 ? -21.248 -10.998 -24.429 1.00 50.50 ? 141 ASP   B CA  1 
ATOM   1259 C  C   . ASP   B 2 132 ? -22.105 -10.976 -25.704 1.00 51.99 ? 141 ASP   B C   1 
ATOM   1260 O  O   . ASP   B 2 132 ? -22.749 -9.955  -25.977 1.00 52.03 ? 141 ASP   B O   1 
ATOM   1261 C  CB  . ASP   B 2 132 ? -21.648 -12.139 -23.459 1.00 51.97 ? 141 ASP   B CB  1 
ATOM   1262 C  CG  . ASP   B 2 132 ? -23.112 -12.220 -23.066 1.00 55.79 ? 141 ASP   B CG  1 
ATOM   1263 O  OD1 . ASP   B 2 132 ? -23.938 -11.505 -23.685 1.00 55.66 ? 141 ASP   B OD1 1 
ATOM   1264 O  OD2 . ASP   B 2 132 ? -23.435 -13.007 -22.138 1.00 58.21 ? 141 ASP   B OD2 1 
ATOM   1265 N  N   . LYS   B 2 133 ? -22.150 -12.088 -26.475 1.00 53.08 ? 142 LYS   B N   1 
ATOM   1266 C  CA  . LYS   B 2 133 ? -22.913 -12.122 -27.733 1.00 54.13 ? 142 LYS   B CA  1 
ATOM   1267 C  C   . LYS   B 2 133 ? -24.418 -11.953 -27.564 1.00 54.51 ? 142 LYS   B C   1 
ATOM   1268 O  O   . LYS   B 2 133 ? -25.065 -11.507 -28.500 1.00 54.99 ? 142 LYS   B O   1 
ATOM   1269 C  CB  . LYS   B 2 133 ? -22.604 -13.374 -28.553 1.00 56.65 ? 142 LYS   B CB  1 
ATOM   1270 C  CG  . LYS   B 2 133 ? -21.424 -13.184 -29.496 1.00 61.92 ? 142 LYS   B CG  1 
ATOM   1271 C  CD  . LYS   B 2 133 ? -20.237 -14.086 -29.142 1.00 66.30 ? 142 LYS   B CD  1 
ATOM   1272 C  CE  . LYS   B 2 133 ? -19.176 -14.032 -30.215 1.00 69.49 ? 142 LYS   B CE  1 
ATOM   1273 N  NZ  . LYS   B 2 133 ? -18.071 -14.986 -29.948 1.00 71.55 ? 142 LYS   B NZ  1 
ATOM   1274 N  N   . CYS   B 2 134 ? -24.982 -12.280 -26.387 1.00 54.28 ? 143 CYS   B N   1 
ATOM   1275 C  CA  . CYS   B 2 134 ? -26.409 -12.048 -26.142 1.00 54.54 ? 143 CYS   B CA  1 
ATOM   1276 C  C   . CYS   B 2 134 ? -26.720 -10.571 -25.807 1.00 53.73 ? 143 CYS   B C   1 
ATOM   1277 O  O   . CYS   B 2 134 ? -27.876 -10.247 -25.568 1.00 53.85 ? 143 CYS   B O   1 
ATOM   1278 C  CB  . CYS   B 2 134 ? -26.923 -12.962 -25.033 1.00 56.73 ? 143 CYS   B CB  1 
ATOM   1279 S  SG  . CYS   B 2 134 ? -26.793 -14.734 -25.390 1.00 63.65 ? 143 CYS   B SG  1 
ATOM   1280 N  N   . GLY   B 2 135 ? -25.701 -9.714  -25.727 1.00 52.78 ? 144 GLY   B N   1 
ATOM   1281 C  CA  . GLY   B 2 135 ? -25.843 -8.321  -25.320 1.00 52.04 ? 144 GLY   B CA  1 
ATOM   1282 C  C   . GLY   B 2 135 ? -25.885 -8.147  -23.810 1.00 50.93 ? 144 GLY   B C   1 
ATOM   1283 O  O   . GLY   B 2 135 ? -26.364 -7.126  -23.321 1.00 51.14 ? 144 GLY   B O   1 
ATOM   1284 N  N   . ARG   B 2 136 ? -25.406 -9.145  -23.046 1.00 49.73 ? 145 ARG   B N   1 
ATOM   1285 C  CA  . ARG   B 2 136 ? -25.445 -9.090  -21.585 1.00 48.81 ? 145 ARG   B CA  1 
ATOM   1286 C  C   . ARG   B 2 136 ? -24.166 -8.514  -21.005 1.00 47.23 ? 145 ARG   B C   1 
ATOM   1287 O  O   . ARG   B 2 136 ? -23.081 -8.804  -21.506 1.00 47.56 ? 145 ARG   B O   1 
ATOM   1288 C  CB  . ARG   B 2 136 ? -25.702 -10.480 -21.000 1.00 50.58 ? 145 ARG   B CB  1 
ATOM   1289 C  CG  . ARG   B 2 136 ? -27.128 -10.966 -21.158 1.00 54.46 ? 145 ARG   B CG  1 
ATOM   1290 C  CD  . ARG   B 2 136 ? -27.255 -12.355 -20.576 1.00 59.23 ? 145 ARG   B CD  1 
ATOM   1291 N  NE  . ARG   B 2 136 ? -26.560 -13.342 -21.402 1.00 64.07 ? 145 ARG   B NE  1 
ATOM   1292 C  CZ  . ARG   B 2 136 ? -26.227 -14.565 -21.001 1.00 67.79 ? 145 ARG   B CZ  1 
ATOM   1293 N  NH1 . ARG   B 2 136 ? -26.484 -14.958 -19.757 1.00 68.51 ? 145 ARG   B NH1 1 
ATOM   1294 N  NH2 . ARG   B 2 136 ? -25.599 -15.392 -21.828 1.00 68.05 ? 145 ARG   B NH2 1 
ATOM   1295 N  N   . VAL   B 2 137 ? -24.285 -7.695  -19.963 1.00 45.60 ? 146 VAL   B N   1 
ATOM   1296 C  CA  . VAL   B 2 137 ? -23.114 -7.090  -19.350 1.00 44.86 ? 146 VAL   B CA  1 
ATOM   1297 C  C   . VAL   B 2 137 ? -22.368 -8.092  -18.480 1.00 44.32 ? 146 VAL   B C   1 
ATOM   1298 O  O   . VAL   B 2 137 ? -22.865 -8.505  -17.441 1.00 44.47 ? 146 VAL   B O   1 
ATOM   1299 C  CB  . VAL   B 2 137 ? -23.430 -5.789  -18.604 1.00 44.66 ? 146 VAL   B CB  1 
ATOM   1300 C  CG1 . VAL   B 2 137 ? -22.154 -5.183  -18.035 1.00 45.09 ? 146 VAL   B CG1 1 
ATOM   1301 C  CG2 . VAL   B 2 137 ? -24.132 -4.805  -19.521 1.00 44.36 ? 146 VAL   B CG2 1 
ATOM   1302 N  N   . ILE   B 2 138 ? -21.204 -8.529  -18.947 1.00 43.78 ? 147 ILE   B N   1 
ATOM   1303 C  CA  . ILE   B 2 138 ? -20.374 -9.495  -18.226 1.00 43.50 ? 147 ILE   B CA  1 
ATOM   1304 C  C   . ILE   B 2 138 ? -19.372 -8.826  -17.247 1.00 43.57 ? 147 ILE   B C   1 
ATOM   1305 O  O   . ILE   B 2 138 ? -18.758 -9.517  -16.429 1.00 43.57 ? 147 ILE   B O   1 
ATOM   1306 C  CB  . ILE   B 2 138 ? -19.683 -10.451 -19.225 1.00 43.28 ? 147 ILE   B CB  1 
ATOM   1307 C  CG1 . ILE   B 2 138 ? -18.821 -9.672  -20.219 1.00 43.98 ? 147 ILE   B CG1 1 
ATOM   1308 C  CG2 . ILE   B 2 138 ? -20.725 -11.288 -19.957 1.00 43.44 ? 147 ILE   B CG2 1 
ATOM   1309 C  CD1 . ILE   B 2 138 ? -17.951 -10.556 -21.116 1.00 45.08 ? 147 ILE   B CD1 1 
ATOM   1310 N  N   . GLY   B 2 139 ? -19.261 -7.495  -17.293 1.00 42.94 ? 148 GLY   B N   1 
ATOM   1311 C  CA  . GLY   B 2 139 ? -18.394 -6.759  -16.384 1.00 42.61 ? 148 GLY   B CA  1 
ATOM   1312 C  C   . GLY   B 2 139 ? -18.192 -5.312  -16.778 1.00 42.06 ? 148 GLY   B C   1 
ATOM   1313 O  O   . GLY   B 2 139 ? -18.782 -4.851  -17.754 1.00 42.39 ? 148 GLY   B O   1 
ATOM   1314 N  N   . LEU   B 2 140 ? -17.376 -4.573  -16.004 1.00 40.97 ? 149 LEU   B N   1 
ATOM   1315 C  CA  . LEU   B 2 140 ? -17.080 -3.174  -16.280 1.00 40.37 ? 149 LEU   B CA  1 
ATOM   1316 C  C   . LEU   B 2 140 ? -15.575 -2.989  -16.422 1.00 40.73 ? 149 LEU   B C   1 
ATOM   1317 O  O   . LEU   B 2 140 ? -14.807 -3.580  -15.675 1.00 40.52 ? 149 LEU   B O   1 
ATOM   1318 C  CB  . LEU   B 2 140 ? -17.601 -2.262  -15.171 1.00 40.22 ? 149 LEU   B CB  1 
ATOM   1319 C  CG  . LEU   B 2 140 ? -19.106 -2.242  -14.891 1.00 40.74 ? 149 LEU   B CG  1 
ATOM   1320 C  CD1 . LEU   B 2 140 ? -19.423 -1.170  -13.901 1.00 40.59 ? 149 LEU   B CD1 1 
ATOM   1321 C  CD2 . LEU   B 2 140 ? -19.918 -1.984  -16.160 1.00 41.28 ? 149 LEU   B CD2 1 
ATOM   1322 N  N   . TYR   B 2 141 ? -15.167 -2.168  -17.399 1.00 41.30 ? 150 TYR   B N   1 
ATOM   1323 C  CA  . TYR   B 2 141 ? -13.779 -1.850  -17.768 1.00 41.67 ? 150 TYR   B CA  1 
ATOM   1324 C  C   . TYR   B 2 141 ? -13.307 -0.606  -16.997 1.00 41.02 ? 150 TYR   B C   1 
ATOM   1325 O  O   . TYR   B 2 141 ? -14.101 0.303   -16.827 1.00 40.12 ? 150 TYR   B O   1 
ATOM   1326 C  CB  . TYR   B 2 141 ? -13.747 -1.621  -19.303 1.00 41.85 ? 150 TYR   B CB  1 
ATOM   1327 C  CG  . TYR   B 2 141 ? -12.544 -0.888  -19.863 1.00 42.99 ? 150 TYR   B CG  1 
ATOM   1328 C  CD1 . TYR   B 2 141 ? -12.574 0.487   -20.063 1.00 44.12 ? 150 TYR   B CD1 1 
ATOM   1329 C  CD2 . TYR   B 2 141 ? -11.429 -1.584  -20.313 1.00 43.87 ? 150 TYR   B CD2 1 
ATOM   1330 C  CE1 . TYR   B 2 141 ? -11.496 1.159   -20.628 1.00 45.23 ? 150 TYR   B CE1 1 
ATOM   1331 C  CE2 . TYR   B 2 141 ? -10.324 -0.919  -20.836 1.00 44.63 ? 150 TYR   B CE2 1 
ATOM   1332 C  CZ  . TYR   B 2 141 ? -10.365 0.454   -20.999 1.00 45.95 ? 150 TYR   B CZ  1 
ATOM   1333 O  OH  . TYR   B 2 141 ? -9.290  1.119   -21.531 1.00 47.57 ? 150 TYR   B OH  1 
ATOM   1334 N  N   . GLY   B 2 142 ? -12.059 -0.576  -16.520 1.00 41.11 ? 151 GLY   B N   1 
ATOM   1335 C  CA  . GLY   B 2 142 ? -11.568 0.594   -15.792 1.00 42.05 ? 151 GLY   B CA  1 
ATOM   1336 C  C   . GLY   B 2 142 ? -10.799 0.371   -14.501 1.00 42.73 ? 151 GLY   B C   1 
ATOM   1337 O  O   . GLY   B 2 142 ? -10.416 1.337   -13.829 1.00 42.58 ? 151 GLY   B O   1 
ATOM   1338 N  N   . ASN   B 2 143 ? -10.532 -0.887  -14.155 1.00 43.05 ? 152 ASN   B N   1 
ATOM   1339 C  CA  . ASN   B 2 143 ? -9.695  -1.198  -13.009 1.00 44.39 ? 152 ASN   B CA  1 
ATOM   1340 C  C   . ASN   B 2 143 ? -8.724  -2.227  -13.501 1.00 45.65 ? 152 ASN   B C   1 
ATOM   1341 O  O   . ASN   B 2 143 ? -9.132  -3.332  -13.820 1.00 45.82 ? 152 ASN   B O   1 
ATOM   1342 C  CB  . ASN   B 2 143 ? -10.480 -1.715  -11.807 1.00 45.52 ? 152 ASN   B CB  1 
ATOM   1343 C  CG  . ASN   B 2 143 ? -9.620  -1.847  -10.574 1.00 48.75 ? 152 ASN   B CG  1 
ATOM   1344 O  OD1 . ASN   B 2 143 ? -8.542  -1.244  -10.464 1.00 49.98 ? 152 ASN   B OD1 1 
ATOM   1345 N  ND2 . ASN   B 2 143 ? -10.081 -2.621  -9.603  1.00 49.16 ? 152 ASN   B ND2 1 
ATOM   1346 N  N   . GLY   B 2 144 ? -7.466  -1.841  -13.628 1.00 46.27 ? 153 GLY   B N   1 
ATOM   1347 C  CA  . GLY   B 2 144 ? -6.459  -2.740  -14.150 1.00 47.85 ? 153 GLY   B CA  1 
ATOM   1348 C  C   . GLY   B 2 144 ? -5.049  -2.276  -13.899 1.00 49.37 ? 153 GLY   B C   1 
ATOM   1349 O  O   . GLY   B 2 144 ? -4.775  -1.639  -12.881 1.00 49.40 ? 153 GLY   B O   1 
ATOM   1350 N  N   . VAL   B 2 145 ? -4.150  -2.600  -14.837 1.00 50.40 ? 154 VAL   B N   1 
ATOM   1351 C  CA  . VAL   B 2 145 ? -2.728  -2.312  -14.701 1.00 52.22 ? 154 VAL   B CA  1 
ATOM   1352 C  C   . VAL   B 2 145 ? -2.061  -1.831  -16.023 1.00 54.05 ? 154 VAL   B C   1 
ATOM   1353 O  O   . VAL   B 2 145 ? -2.608  -2.031  -17.099 1.00 53.52 ? 154 VAL   B O   1 
ATOM   1354 C  CB  . VAL   B 2 145 ? -2.059  -3.581  -14.104 1.00 52.92 ? 154 VAL   B CB  1 
ATOM   1355 C  CG1 . VAL   B 2 145 ? -1.649  -4.571  -15.190 1.00 53.22 ? 154 VAL   B CG1 1 
ATOM   1356 C  CG2 . VAL   B 2 145 ? -0.898  -3.227  -13.187 1.00 53.52 ? 154 VAL   B CG2 1 
ATOM   1357 N  N   . VAL   B 2 146 ? -0.911  -1.147  -15.925 1.00 56.08 ? 155 VAL   B N   1 
ATOM   1358 C  CA  . VAL   B 2 146 ? -0.143  -0.671  -17.083 1.00 58.53 ? 155 VAL   B CA  1 
ATOM   1359 C  C   . VAL   B 2 146 ? 1.062   -1.614  -17.243 1.00 61.40 ? 155 VAL   B C   1 
ATOM   1360 O  O   . VAL   B 2 146 ? 1.750   -1.886  -16.257 1.00 61.79 ? 155 VAL   B O   1 
ATOM   1361 C  CB  . VAL   B 2 146 ? 0.311   0.803   -16.942 1.00 59.28 ? 155 VAL   B CB  1 
ATOM   1362 C  CG1 . VAL   B 2 146 ? 0.811   1.339   -18.278 1.00 60.03 ? 155 VAL   B CG1 1 
ATOM   1363 C  CG2 . VAL   B 2 146 ? -0.814  1.683   -16.408 1.00 59.68 ? 155 VAL   B CG2 1 
ATOM   1364 N  N   . ILE   B 2 147 ? 1.295   -2.151  -18.453 1.00 63.31 ? 156 ILE   B N   1 
ATOM   1365 C  CA  . ILE   B 2 147 ? 2.354   -3.143  -18.633 1.00 65.75 ? 156 ILE   B CA  1 
ATOM   1366 C  C   . ILE   B 2 147 ? 3.627   -2.549  -19.333 1.00 67.78 ? 156 ILE   B C   1 
ATOM   1367 O  O   . ILE   B 2 147 ? 3.704   -1.334  -19.518 1.00 68.31 ? 156 ILE   B O   1 
ATOM   1368 C  CB  . ILE   B 2 147 ? 1.753   -4.412  -19.310 1.00 66.72 ? 156 ILE   B CB  1 
ATOM   1369 C  CG1 . ILE   B 2 147 ? 1.332   -4.149  -20.742 1.00 67.85 ? 156 ILE   B CG1 1 
ATOM   1370 C  CG2 . ILE   B 2 147 ? 0.573   -4.946  -18.477 1.00 67.66 ? 156 ILE   B CG2 1 
ATOM   1371 C  CD1 . ILE   B 2 147 ? 0.799   -5.397  -21.474 1.00 69.44 ? 156 ILE   B CD1 1 
ATOM   1372 N  N   . LYS   B 2 148 ? 4.654   -3.383  -19.615 1.00 68.73 ? 157 LYS   B N   1 
ATOM   1373 C  CA  . LYS   B 2 148 ? 5.940   -2.959  -20.184 1.00 70.07 ? 157 LYS   B CA  1 
ATOM   1374 C  C   . LYS   B 2 148 ? 5.839   -1.927  -21.302 1.00 71.10 ? 157 LYS   B C   1 
ATOM   1375 O  O   . LYS   B 2 148 ? 6.426   -0.854  -21.176 1.00 72.09 ? 157 LYS   B O   1 
ATOM   1376 C  CB  . LYS   B 2 148 ? 6.826   -4.145  -20.649 1.00 72.28 ? 157 LYS   B CB  1 
ATOM   1377 C  CG  . LYS   B 2 148 ? 6.187   -5.532  -20.605 1.00 76.51 ? 157 LYS   B CG  1 
ATOM   1378 C  CD  . LYS   B 2 148 ? 6.882   -6.446  -19.584 1.00 80.28 ? 157 LYS   B CD  1 
ATOM   1379 C  CE  . LYS   B 2 148 ? 6.546   -6.128  -18.137 1.00 82.00 ? 157 LYS   B CE  1 
ATOM   1380 N  NZ  . LYS   B 2 148 ? 7.778   -5.933  -17.332 1.00 82.26 ? 157 LYS   B NZ  1 
ATOM   1381 N  N   . ASN   B 2 149 ? 5.089   -2.216  -22.374 1.00 70.56 ? 158 ASN   B N   1 
ATOM   1382 C  CA  . ASN   B 2 149 ? 4.982   -1.288  -23.503 1.00 70.27 ? 158 ASN   B CA  1 
ATOM   1383 C  C   . ASN   B 2 149 ? 4.053   -0.081  -23.255 1.00 68.59 ? 158 ASN   B C   1 
ATOM   1384 O  O   . ASN   B 2 149 ? 3.632   0.569   -24.214 1.00 68.74 ? 158 ASN   B O   1 
ATOM   1385 C  CB  . ASN   B 2 149 ? 4.591   -2.027  -24.806 1.00 72.45 ? 158 ASN   B CB  1 
ATOM   1386 C  CG  . ASN   B 2 149 ? 3.350   -2.904  -24.723 1.00 76.76 ? 158 ASN   B CG  1 
ATOM   1387 O  OD1 . ASN   B 2 149 ? 2.935   -3.361  -23.651 1.00 78.29 ? 158 ASN   B OD1 1 
ATOM   1388 N  ND2 . ASN   B 2 149 ? 2.738   -3.181  -25.874 1.00 77.27 ? 158 ASN   B ND2 1 
ATOM   1389 N  N   . GLY   B 2 150 ? 3.750   0.211   -21.988 1.00 66.85 ? 159 GLY   B N   1 
ATOM   1390 C  CA  . GLY   B 2 150 ? 2.886   1.334   -21.619 1.00 65.35 ? 159 GLY   B CA  1 
ATOM   1391 C  C   . GLY   B 2 150 ? 1.408   1.161   -21.932 1.00 63.04 ? 159 GLY   B C   1 
ATOM   1392 O  O   . GLY   B 2 150 ? 0.614   2.085   -21.730 1.00 63.36 ? 159 GLY   B O   1 
ATOM   1393 N  N   . SER   B 2 151 ? 1.025   -0.024  -22.424 1.00 60.37 ? 160 SER   B N   1 
ATOM   1394 C  CA  A SER   B 2 151 ? -0.358  -0.327  -22.757 0.50 59.56 ? 160 SER   B CA  1 
ATOM   1395 C  CA  B SER   B 2 151 ? -0.360  -0.305  -22.750 0.50 59.42 ? 160 SER   B CA  1 
ATOM   1396 C  C   . SER   B 2 151 ? -1.166  -0.689  -21.501 1.00 58.25 ? 160 SER   B C   1 
ATOM   1397 O  O   . SER   B 2 151 ? -0.683  -1.404  -20.618 1.00 58.63 ? 160 SER   B O   1 
ATOM   1398 C  CB  A SER   B 2 151 ? -0.422  -1.458  -23.780 0.50 61.21 ? 160 SER   B CB  1 
ATOM   1399 C  CB  B SER   B 2 151 ? -0.447  -1.397  -23.808 0.50 60.64 ? 160 SER   B CB  1 
ATOM   1400 O  OG  A SER   B 2 151 ? -1.756  -1.792  -24.131 0.50 63.72 ? 160 SER   B OG  1 
ATOM   1401 O  OG  B SER   B 2 151 ? 0.092   -2.616  -23.327 0.50 62.45 ? 160 SER   B OG  1 
ATOM   1402 N  N   . TYR   B 2 152 ? -2.388  -0.200  -21.418 1.00 54.81 ? 161 TYR   B N   1 
ATOM   1403 C  CA  . TYR   B 2 152 ? -3.273  -0.461  -20.303 1.00 51.44 ? 161 TYR   B CA  1 
ATOM   1404 C  C   . TYR   B 2 152 ? -4.049  -1.769  -20.518 1.00 49.37 ? 161 TYR   B C   1 
ATOM   1405 O  O   . TYR   B 2 152 ? -4.568  -1.994  -21.607 1.00 49.06 ? 161 TYR   B O   1 
ATOM   1406 C  CB  . TYR   B 2 152 ? -4.247  0.716   -20.193 1.00 50.01 ? 161 TYR   B CB  1 
ATOM   1407 C  CG  . TYR   B 2 152 ? -5.292  0.556   -19.124 1.00 48.91 ? 161 TYR   B CG  1 
ATOM   1408 C  CD1 . TYR   B 2 152 ? -4.941  0.525   -17.781 1.00 49.28 ? 161 TYR   B CD1 1 
ATOM   1409 C  CD2 . TYR   B 2 152 ? -6.636  0.471   -19.449 1.00 49.17 ? 161 TYR   B CD2 1 
ATOM   1410 C  CE1 . TYR   B 2 152 ? -5.898  0.392   -16.788 1.00 49.45 ? 161 TYR   B CE1 1 
ATOM   1411 C  CE2 . TYR   B 2 152 ? -7.606  0.347   -18.463 1.00 49.75 ? 161 TYR   B CE2 1 
ATOM   1412 C  CZ  . TYR   B 2 152 ? -7.230  0.311   -17.132 1.00 50.22 ? 161 TYR   B CZ  1 
ATOM   1413 O  OH  . TYR   B 2 152 ? -8.175  0.182   -16.153 1.00 51.27 ? 161 TYR   B OH  1 
ATOM   1414 N  N   . VAL   B 2 153 ? -4.114  -2.628  -19.483 1.00 47.68 ? 162 VAL   B N   1 
ATOM   1415 C  CA  . VAL   B 2 153 ? -4.865  -3.885  -19.481 1.00 46.61 ? 162 VAL   B CA  1 
ATOM   1416 C  C   . VAL   B 2 153 ? -5.853  -3.813  -18.301 1.00 45.45 ? 162 VAL   B C   1 
ATOM   1417 O  O   . VAL   B 2 153 ? -5.416  -3.809  -17.161 1.00 45.34 ? 162 VAL   B O   1 
ATOM   1418 C  CB  . VAL   B 2 153 ? -3.947  -5.124  -19.322 1.00 47.30 ? 162 VAL   B CB  1 
ATOM   1419 C  CG1 . VAL   B 2 153 ? -4.729  -6.415  -19.541 1.00 47.23 ? 162 VAL   B CG1 1 
ATOM   1420 C  CG2 . VAL   B 2 153 ? -2.737  -5.054  -20.254 1.00 48.53 ? 162 VAL   B CG2 1 
ATOM   1421 N  N   . SER   B 2 154 ? -7.160  -3.736  -18.561 1.00 44.42 ? 163 SER   B N   1 
ATOM   1422 C  CA  . SER   B 2 154 ? -8.160  -3.687  -17.489 1.00 43.96 ? 163 SER   B CA  1 
ATOM   1423 C  C   . SER   B 2 154 ? -8.668  -5.079  -17.130 1.00 44.11 ? 163 SER   B C   1 
ATOM   1424 O  O   . SER   B 2 154 ? -8.725  -5.930  -17.999 1.00 44.64 ? 163 SER   B O   1 
ATOM   1425 C  CB  . SER   B 2 154 ? -9.354  -2.841  -17.922 1.00 43.96 ? 163 SER   B CB  1 
ATOM   1426 O  OG  . SER   B 2 154 ? -10.491 -2.988  -17.079 1.00 45.42 ? 163 SER   B OG  1 
ATOM   1427 N  N   . ALA   B 2 155 ? -9.137  -5.287  -15.895 1.00 43.50 ? 164 ALA   B N   1 
ATOM   1428 C  CA  . ALA   B 2 155 ? -9.781  -6.553  -15.543 1.00 44.27 ? 164 ALA   B CA  1 
ATOM   1429 C  C   . ALA   B 2 155 ? -11.266 -6.533  -16.067 1.00 44.68 ? 164 ALA   B C   1 
ATOM   1430 O  O   . ALA   B 2 155 ? -11.760 -5.480  -16.505 1.00 44.87 ? 164 ALA   B O   1 
ATOM   1431 C  CB  . ALA   B 2 155 ? -9.751  -6.742  -14.027 1.00 44.85 ? 164 ALA   B CB  1 
ATOM   1432 N  N   . ILE   B 2 156 ? -11.955 -7.694  -16.068 1.00 44.37 ? 165 ILE   B N   1 
ATOM   1433 C  CA  . ILE   B 2 156 ? -13.370 -7.717  -16.405 1.00 44.86 ? 165 ILE   B CA  1 
ATOM   1434 C  C   . ILE   B 2 156 ? -14.066 -7.779  -15.043 1.00 45.99 ? 165 ILE   B C   1 
ATOM   1435 O  O   . ILE   B 2 156 ? -14.318 -8.867  -14.510 1.00 46.09 ? 165 ILE   B O   1 
ATOM   1436 C  CB  . ILE   B 2 156 ? -13.818 -8.852  -17.351 1.00 45.18 ? 165 ILE   B CB  1 
ATOM   1437 C  CG1 . ILE   B 2 156 ? -13.026 -8.837  -18.675 1.00 45.93 ? 165 ILE   B CG1 1 
ATOM   1438 C  CG2 . ILE   B 2 156 ? -15.321 -8.730  -17.617 1.00 45.56 ? 165 ILE   B CG2 1 
ATOM   1439 C  CD1 . ILE   B 2 156 ? -13.403 -9.956  -19.686 1.00 46.64 ? 165 ILE   B CD1 1 
ATOM   1440 N  N   . THR   B 2 157 ? -14.293 -6.598  -14.435 1.00 46.39 ? 166 THR   B N   1 
ATOM   1441 C  CA  . THR   B 2 157 ? -14.890 -6.501  -13.103 1.00 47.11 ? 166 THR   B CA  1 
ATOM   1442 C  C   . THR   B 2 157 ? -16.379 -6.776  -13.033 1.00 47.22 ? 166 THR   B C   1 
ATOM   1443 O  O   . THR   B 2 157 ? -17.168 -5.979  -13.528 1.00 47.43 ? 166 THR   B O   1 
ATOM   1444 C  CB  . THR   B 2 157 ? -14.626 -5.139  -12.504 1.00 49.17 ? 166 THR   B CB  1 
ATOM   1445 O  OG1 . THR   B 2 157 ? -13.232 -4.861  -12.580 1.00 50.83 ? 166 THR   B OG1 1 
ATOM   1446 C  CG2 . THR   B 2 157 ? -15.063 -5.067  -11.071 1.00 49.88 ? 166 THR   B CG2 1 
ATOM   1447 N  N   . GLN   B 2 158 ? -16.772 -7.851  -12.355 1.00 47.12 ? 167 GLN   B N   1 
ATOM   1448 C  CA  . GLN   B 2 158 ? -18.179 -8.170  -12.192 1.00 47.88 ? 167 GLN   B CA  1 
ATOM   1449 C  C   . GLN   B 2 158 ? -18.530 -8.347  -10.704 1.00 50.68 ? 167 GLN   B C   1 
ATOM   1450 O  O   . GLN   B 2 158 ? -17.755 -8.933  -9.948  1.00 50.93 ? 167 GLN   B O   1 
ATOM   1451 C  CB  . GLN   B 2 158 ? -18.565 -9.417  -13.019 1.00 46.99 ? 167 GLN   B CB  1 
ATOM   1452 C  CG  . GLN   B 2 158 ? -20.045 -9.826  -12.967 1.00 46.19 ? 167 GLN   B CG  1 
ATOM   1453 C  CD  . GLN   B 2 158 ? -20.966 -8.810  -13.604 1.00 48.52 ? 167 GLN   B CD  1 
ATOM   1454 O  OE1 . GLN   B 2 158 ? -21.065 -7.662  -13.176 1.00 48.72 ? 167 GLN   B OE1 1 
ATOM   1455 N  NE2 . GLN   B 2 158 ? -21.670 -9.208  -14.646 1.00 49.96 ? 167 GLN   B NE2 1 
ATOM   1456 N  N   . GLY   B 2 159 ? -19.688 -7.836  -10.302 1.00 52.68 ? 168 GLY   B N   1 
ATOM   1457 C  CA  . GLY   B 2 159 ? -20.175 -8.001  -8.946  1.00 55.79 ? 168 GLY   B CA  1 
ATOM   1458 C  C   . GLY   B 2 159 ? -20.994 -9.269  -8.788  1.00 59.27 ? 168 GLY   B C   1 
ATOM   1459 O  O   . GLY   B 2 159 ? -21.178 -10.037 -9.740  1.00 59.50 ? 168 GLY   B O   1 
ATOM   1460 N  N   . LYS   B 2 160 ? -21.500 -9.495  -7.576  1.00 61.87 ? 169 LYS   B N   1 
ATOM   1461 C  CA  . LYS   B 2 160 ? -22.329 -10.657 -7.248  1.00 64.58 ? 169 LYS   B CA  1 
ATOM   1462 C  C   . LYS   B 2 160 ? -23.813 -10.240 -7.215  1.00 66.83 ? 169 LYS   B C   1 
ATOM   1463 O  O   . LYS   B 2 160 ? -24.134 -9.154  -6.716  1.00 67.41 ? 169 LYS   B O   1 
ATOM   1464 C  CB  . LYS   B 2 160 ? -21.899 -11.226 -5.876  1.00 66.70 ? 169 LYS   B CB  1 
ATOM   1465 C  CG  . LYS   B 2 160 ? -22.735 -12.402 -5.372  1.00 71.26 ? 169 LYS   B CG  1 
ATOM   1466 C  CD  . LYS   B 2 160 ? -22.323 -12.811 -3.951  1.00 75.92 ? 169 LYS   B CD  1 
ATOM   1467 C  CE  . LYS   B 2 160 ? -23.200 -13.893 -3.354  1.00 79.66 ? 169 LYS   B CE  1 
ATOM   1468 N  NZ  . LYS   B 2 160 ? -22.958 -14.056 -1.889  1.00 81.90 ? 169 LYS   B NZ  1 
ATOM   1469 N  N   . ARG   B 2 161 ? -24.711 -11.074 -7.763  1.00 67.72 ? 170 ARG   B N   1 
ATOM   1470 C  CA  . ARG   B 2 161 ? -26.143 -10.763 -7.736  1.00 69.15 ? 170 ARG   B CA  1 
ATOM   1471 C  C   . ARG   B 2 161 ? -26.811 -11.689 -6.706  1.00 70.38 ? 170 ARG   B C   1 
ATOM   1472 O  O   . ARG   B 2 161 ? -26.531 -12.888 -6.707  1.00 70.84 ? 170 ARG   B O   1 
ATOM   1473 C  CB  . ARG   B 2 161 ? -26.779 -10.908 -9.141  1.00 70.27 ? 170 ARG   B CB  1 
ATOM   1474 C  CG  . ARG   B 2 161 ? -28.142 -10.227 -9.253  1.00 72.71 ? 170 ARG   B CG  1 
ATOM   1475 C  CD  . ARG   B 2 161 ? -28.964 -10.685 -10.448 1.00 74.93 ? 170 ARG   B CD  1 
ATOM   1476 N  NE  . ARG   B 2 161 ? -30.390 -10.403 -10.256 1.00 77.36 ? 170 ARG   B NE  1 
ATOM   1477 C  CZ  . ARG   B 2 161 ? -31.123 -9.629  -11.054 1.00 79.34 ? 170 ARG   B CZ  1 
ATOM   1478 N  NH1 . ARG   B 2 161 ? -30.577 -9.051  -12.115 1.00 78.97 ? 170 ARG   B NH1 1 
ATOM   1479 N  NH2 . ARG   B 2 161 ? -32.409 -9.426  -10.794 1.00 78.97 ? 170 ARG   B NH2 1 
ATOM   1480 N  N   . GLU   B 2 162 ? -27.643 -11.143 -5.801  1.00 70.78 ? 171 GLU   B N   1 
ATOM   1481 C  CA  . GLU   B 2 162 ? -28.289 -11.971 -4.774  1.00 71.98 ? 171 GLU   B CA  1 
ATOM   1482 C  C   . GLU   B 2 162 ? -29.392 -12.889 -5.333  1.00 72.38 ? 171 GLU   B C   1 
ATOM   1483 O  O   . GLU   B 2 162 ? -29.968 -13.700 -4.601  1.00 72.53 ? 171 GLU   B O   1 
ATOM   1484 C  CB  . GLU   B 2 162 ? -28.819 -11.112 -3.609  1.00 75.02 ? 171 GLU   B CB  1 
ATOM   1485 C  CG  . GLU   B 2 162 ? -27.770 -10.237 -2.928  1.00 81.09 ? 171 GLU   B CG  1 
ATOM   1486 C  CD  . GLU   B 2 162 ? -26.745 -10.942 -2.053  1.00 88.41 ? 171 GLU   B CD  1 
ATOM   1487 O  OE1 . GLU   B 2 162 ? -26.967 -11.022 -0.820  1.00 89.79 ? 171 GLU   B OE1 1 
ATOM   1488 O  OE2 . GLU   B 2 162 ? -25.710 -11.394 -2.596  1.00 90.33 ? 171 GLU   B OE2 1 
HETATM 1489 S  S   . DMS   C 3 .   ? -18.432 11.050  -0.178  1.00 72.16 ? 201 DMS   B S   1 
HETATM 1490 O  O   . DMS   C 3 .   ? -19.429 9.932   -0.180  1.00 72.06 ? 201 DMS   B O   1 
HETATM 1491 C  C1  . DMS   C 3 .   ? -19.321 12.587  -0.548  1.00 72.13 ? 201 DMS   B C1  1 
HETATM 1492 C  C2  . DMS   C 3 .   ? -17.466 11.027  -1.710  1.00 72.17 ? 201 DMS   B C2  1 
HETATM 1493 N  N1  . A1B8X D 4 .   ? -5.530  1.832   -13.099 1.00 60.44 ? 202 A1B8X B N1  1 
HETATM 1494 N  N3  . A1B8X D 4 .   ? -8.429  1.781   -7.179  1.00 56.46 ? 202 A1B8X B N3  1 
HETATM 1495 C  C4  . A1B8X D 4 .   ? -4.968  2.757   -10.128 1.00 63.34 ? 202 A1B8X B C4  1 
HETATM 1496 C  C5  . A1B8X D 4 .   ? -4.347  2.411   -8.790  1.00 63.62 ? 202 A1B8X B C5  1 
HETATM 1497 C  C6  . A1B8X D 4 .   ? -3.108  0.672   -9.835  1.00 63.64 ? 202 A1B8X B C6  1 
HETATM 1498 C  C7  . A1B8X D 4 .   ? -3.406  1.132   -11.250 1.00 63.19 ? 202 A1B8X B C7  1 
HETATM 1499 C  C8  . A1B8X D 4 .   ? -7.277  3.490   -13.614 1.00 58.64 ? 202 A1B8X B C8  1 
HETATM 1500 C  C10 . A1B8X D 4 .   ? -7.931  4.784   -10.656 1.00 57.30 ? 202 A1B8X B C10 1 
HETATM 1501 C  C13 . A1B8X D 4 .   ? -8.727  2.461   -9.358  1.00 57.03 ? 202 A1B8X B C13 1 
HETATM 1502 C  C15 . A1B8X D 4 .   ? -9.113  1.361   -8.409  1.00 56.67 ? 202 A1B8X B C15 1 
HETATM 1503 C  C17 . A1B8X D 4 .   ? -7.453  3.810   -15.093 1.00 58.25 ? 202 A1B8X B C17 1 
HETATM 1504 C  C20 . A1B8X D 4 .   ? -7.615  4.176   -17.920 1.00 57.85 ? 202 A1B8X B C20 1 
HETATM 1505 C  C21 . A1B8X D 4 .   ? -6.495  4.578   -17.201 1.00 58.62 ? 202 A1B8X B C21 1 
HETATM 1506 C  C22 . A1B8X D 4 .   ? -5.111  4.911   -15.487 1.00 59.28 ? 202 A1B8X B C22 1 
HETATM 1507 O  O1  . A1B8X D 4 .   ? -7.574  1.100   -13.664 1.00 59.84 ? 202 A1B8X B O1  1 
HETATM 1508 C  C1  . A1B8X D 4 .   ? -6.807  2.028   -13.446 1.00 59.65 ? 202 A1B8X B C1  1 
HETATM 1509 C  C2  . A1B8X D 4 .   ? -4.630  2.876   -12.629 1.00 61.53 ? 202 A1B8X B C2  1 
HETATM 1510 C  C3  . A1B8X D 4 .   ? -3.990  2.548   -11.285 1.00 62.76 ? 202 A1B8X B C3  1 
HETATM 1511 O  O2  . A1B8X D 4 .   ? -3.082  1.756   -8.904  1.00 63.77 ? 202 A1B8X B O2  1 
HETATM 1512 N  N2  . A1B8X D 4 .   ? -8.435  3.753   -12.783 1.00 58.21 ? 202 A1B8X B N2  1 
HETATM 1513 C  C9  . A1B8X D 4 .   ? -8.391  3.680   -11.394 1.00 57.63 ? 202 A1B8X B C9  1 
HETATM 1514 C  C11 . A1B8X D 4 .   ? -7.902  4.734   -9.272  1.00 57.18 ? 202 A1B8X B C11 1 
HETATM 1515 C  C12 . A1B8X D 4 .   ? -8.275  3.557   -8.633  1.00 57.00 ? 202 A1B8X B C12 1 
HETATM 1516 C  C14 . A1B8X D 4 .   ? -8.784  2.501   -10.744 1.00 57.18 ? 202 A1B8X B C14 1 
HETATM 1517 C  C16 . A1B8X D 4 .   ? -8.374  3.252   -7.167  1.00 56.66 ? 202 A1B8X B C16 1 
HETATM 1518 C  C18 . A1B8X D 4 .   ? -8.592  3.440   -15.808 1.00 57.55 ? 202 A1B8X B C18 1 
HETATM 1519 C  C19 . A1B8X D 4 .   ? -8.664  3.639   -17.196 1.00 57.25 ? 202 A1B8X B C19 1 
HETATM 1520 CL CL1 . A1B8X D 4 .   ? -10.092 3.166   -18.087 1.00 55.84 ? 202 A1B8X B CL1 1 
HETATM 1521 N  N4  . A1B8X D 4 .   ? -5.349  5.165   -17.610 1.00 59.30 ? 202 A1B8X B N4  1 
HETATM 1522 N  N5  . A1B8X D 4 .   ? -4.502  5.373   -16.564 1.00 59.39 ? 202 A1B8X B N5  1 
HETATM 1523 C  C23 . A1B8X D 4 .   ? -6.389  4.399   -15.812 1.00 58.77 ? 202 A1B8X B C23 1 
HETATM 1524 O  O   . HOH   E 5 .   ? -8.666  2.672   -3.568  1.00 35.12 ? 101 HOH   A O   1 
HETATM 1525 O  O   . HOH   E 5 .   ? -27.042 -7.499  -28.412 1.00 55.83 ? 102 HOH   A O   1 
HETATM 1526 O  O   . HOH   E 5 .   ? -6.433  -9.976  -2.634  1.00 33.35 ? 103 HOH   A O   1 
HETATM 1527 O  O   . HOH   E 5 .   ? -1.550  -3.387  -5.539  1.00 42.31 ? 104 HOH   A O   1 
HETATM 1528 O  O   . HOH   E 5 .   ? -21.559 14.199  -6.418  1.00 38.09 ? 105 HOH   A O   1 
HETATM 1529 O  O   . HOH   E 5 .   ? -30.204 -1.015  -29.928 1.00 51.64 ? 106 HOH   A O   1 
HETATM 1530 O  O   . HOH   E 5 .   ? -2.243  -8.265  -2.515  1.00 36.37 ? 107 HOH   A O   1 
HETATM 1531 O  O   . HOH   E 5 .   ? -3.354  -15.749 -24.950 1.00 52.35 ? 108 HOH   A O   1 
HETATM 1532 O  O   . HOH   E 5 .   ? -3.568  -0.949  0.598   1.00 46.13 ? 109 HOH   A O   1 
HETATM 1533 O  O   . HOH   E 5 .   ? -3.832  -11.041 -5.160  1.00 36.54 ? 110 HOH   A O   1 
HETATM 1534 O  O   . HOH   E 5 .   ? -20.251 -9.640  -34.835 1.00 43.61 ? 111 HOH   A O   1 
HETATM 1535 O  O   . HOH   E 5 .   ? -8.021  0.385   2.166   1.00 59.05 ? 112 HOH   A O   1 
HETATM 1536 O  O   . HOH   E 5 .   ? -1.086  2.606   -5.646  1.00 39.60 ? 113 HOH   A O   1 
HETATM 1537 O  O   . HOH   F 5 .   ? -23.266 -7.662  -4.887  1.00 54.39 ? 301 HOH   B O   1 
HETATM 1538 O  O   . HOH   F 5 .   ? -17.344 -11.674 -16.204 1.00 48.42 ? 302 HOH   B O   1 
HETATM 1539 O  O   . HOH   F 5 .   ? -6.253  -11.686 -4.544  1.00 42.03 ? 303 HOH   B O   1 
HETATM 1540 O  O   . HOH   F 5 .   ? -16.105 -16.593 -30.545 1.00 49.19 ? 304 HOH   B O   1 
HETATM 1541 O  O   . HOH   F 5 .   ? -11.267 0.886   -5.300  1.00 36.30 ? 305 HOH   B O   1 
HETATM 1542 O  O   . HOH   F 5 .   ? -21.027 -17.364 -18.809 1.00 35.70 ? 306 HOH   B O   1 
HETATM 1543 O  O   . HOH   F 5 .   ? -15.668 19.506  -14.226 1.00 38.70 ? 307 HOH   B O   1 
HETATM 1544 O  O   . HOH   F 5 .   ? -5.934  -1.246  -10.120 1.00 25.87 ? 308 HOH   B O   1 
HETATM 1545 O  O   . HOH   F 5 .   ? -32.719 1.079   -15.924 1.00 30.08 ? 309 HOH   B O   1 
HETATM 1546 O  O   . HOH   F 5 .   ? -12.267 -3.197  -14.456 1.00 28.65 ? 310 HOH   B O   1 
HETATM 1547 O  O   . HOH   F 5 .   ? -29.776 11.725  -19.202 1.00 58.86 ? 311 HOH   B O   1 
HETATM 1548 O  O   . HOH   F 5 .   ? -11.885 -4.671  -9.555  1.00 56.41 ? 312 HOH   B O   1 
HETATM 1549 O  O   . HOH   F 5 .   ? -15.649 -8.240  -7.880  1.00 59.01 ? 313 HOH   B O   1 
HETATM 1550 O  O   . HOH   F 5 .   ? -17.791 13.774  -22.151 1.00 36.72 ? 314 HOH   B O   1 
HETATM 1551 O  O   . HOH   F 5 .   ? -34.156 -2.690  -7.338  1.00 46.36 ? 315 HOH   B O   1 
HETATM 1552 O  O   . HOH   F 5 .   ? -30.011 3.789   -2.268  1.00 59.29 ? 316 HOH   B O   1 
HETATM 1553 O  O   . HOH   F 5 .   ? -26.761 -7.302  -18.516 1.00 42.60 ? 317 HOH   B O   1 
HETATM 1554 O  O   . HOH   F 5 .   ? -31.620 6.437   -4.885  1.00 54.71 ? 318 HOH   B O   1 
HETATM 1555 O  O   . HOH   F 5 .   ? -30.219 10.966  -16.769 1.00 47.49 ? 319 HOH   B O   1 
HETATM 1556 O  O   . HOH   F 5 .   ? -10.283 11.298  -18.879 1.00 40.19 ? 320 HOH   B O   1 
HETATM 1557 O  O   . HOH   F 5 .   ? -25.651 -9.195  -16.698 1.00 35.37 ? 321 HOH   B O   1 
HETATM 1558 O  O   . HOH   F 5 .   ? -28.233 -4.996  -22.444 1.00 50.10 ? 322 HOH   B O   1 
HETATM 1559 O  O   . HOH   F 5 .   ? -25.732 -5.975  -4.208  1.00 37.90 ? 323 HOH   B O   1 
HETATM 1560 O  O   . HOH   F 5 .   ? -9.048  6.648   -13.252 1.00 49.29 ? 324 HOH   B O   1 
HETATM 1561 O  O   . HOH   F 5 .   ? -6.025  9.014   -19.093 1.00 38.50 ? 325 HOH   B O   1 
HETATM 1562 O  O   . HOH   F 5 .   ? -16.568 12.170  -5.057  1.00 39.70 ? 326 HOH   B O   1 
HETATM 1563 O  O   . HOH   F 5 .   ? -13.874 15.282  -20.039 1.00 47.72 ? 327 HOH   B O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -11.648 23.704  -10.273 1.00 56.31 ? 328 HOH   B O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -17.961 24.207  -14.038 1.00 54.61 ? 329 HOH   B O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -13.957 -7.413  -1.045  1.00 45.18 ? 330 HOH   B O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -19.391 -14.744 -22.547 1.00 44.16 ? 331 HOH   B O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -0.433  -15.199 -9.682  1.00 56.07 ? 332 HOH   B O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -23.310 -16.173 -18.020 1.00 49.05 ? 333 HOH   B O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -19.415 -6.882  -0.790  1.00 48.87 ? 334 HOH   B O   1 
HETATM 1571 O  O   . HOH   F 5 .   ? -17.151 17.149  -27.025 0.50 96.16 ? 335 HOH   B O   1 
HETATM 1572 O  O   . HOH   F 5 .   ? -20.626 14.521  -24.306 1.00 50.84 ? 336 HOH   B O   1 
HETATM 1573 O  O   . HOH   F 5 .   ? -16.088 15.734  -21.810 1.00 40.83 ? 337 HOH   B O   1 
HETATM 1574 O  O   . HOH   F 5 .   ? -34.583 4.582   -9.357  1.00 64.86 ? 338 HOH   B O   1 
HETATM 1575 O  O   . HOH   F 5 .   ? -9.461  8.212   -10.018 1.00 53.09 ? 339 HOH   B O   1 
HETATM 1576 O  O   . HOH   F 5 .   ? -31.019 -8.032  -7.169  1.00 40.65 ? 340 HOH   B O   1 
HETATM 1577 O  O   . HOH   F 5 .   ? -30.761 16.589  -6.795  1.00 50.91 ? 341 HOH   B O   1 
HETATM 1578 O  O   . HOH   F 5 .   ? -10.859 5.013   -4.550  1.00 51.05 ? 342 HOH   B O   1 
HETATM 1579 O  O   . HOH   F 5 .   ? -11.214 -7.688  2.036   1.00 40.23 ? 343 HOH   B O   1 
HETATM 1580 O  O   . HOH   F 5 .   ? -21.863 -16.094 -25.416 1.00 40.93 ? 344 HOH   B O   1 
HETATM 1581 O  O   . HOH   F 5 .   ? -10.660 11.303  -14.467 1.00 38.82 ? 345 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP   A 7   ? 1.0068 0.3146 0.7586 0.1717  0.1382  -0.2069 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.9928 0.3657 0.7271 0.1940  0.1381  -0.1839 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.9760 0.3657 0.7129 0.1840  0.1406  -0.1372 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.9897 0.3313 0.7375 0.1769  0.1475  -0.1132 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.0252 0.3889 0.7499 0.2369  0.1438  -0.1867 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.0885 0.5320 0.7972 0.2567  0.1412  -0.1879 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.0987 0.5504 0.7987 0.2846  0.1435  -0.2136 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.1125 0.6107 0.8181 0.2440  0.1374  -0.1638 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.9413 0.3994 0.6673 0.1840  0.1355  -0.1247 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.9207 0.4010 0.6458 0.1766  0.1359  -0.0867 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.9047 0.4055 0.6212 0.2064  0.1377  -0.0633 51  MET   A C   
12   O  O   . MET   A 8   ? 0.8947 0.4207 0.6056 0.2291  0.1370  -0.0761 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.9083 0.4456 0.6295 0.1555  0.1279  -0.0877 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.9279 0.4548 0.6607 0.1251  0.1251  -0.1045 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.9278 0.5198 0.6562 0.1058  0.1165  -0.0972 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.9248 0.4983 0.6742 0.0727  0.1148  -0.1145 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.8941 0.3911 0.6096 0.2064  0.1397  -0.0291 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.8762 0.3970 0.5852 0.2330  0.1390  -0.0057 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.8600 0.4108 0.5626 0.2234  0.1347  0.0229  52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.8563 0.3998 0.5596 0.1991  0.1354  0.0280  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.8860 0.3541 0.5976 0.2603  0.1468  0.0038  52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.9065 0.3174 0.6215 0.2503  0.1544  0.0270  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.9303 0.2825 0.6572 0.2314  0.1607  0.0123  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.9169 0.3333 0.6237 0.2607  0.1557  0.0642  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.9551 0.2559 0.6885 0.2201  0.1699  0.0376  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.9430 0.3098 0.6511 0.2535  0.1651  0.0900  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.9646 0.2725 0.6874 0.2327  0.1733  0.0784  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 0.9911 0.2534 0.7183 0.2225  0.1846  0.1079  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.8489 0.4383 0.5465 0.2425  0.1297  0.0392  53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.8466 0.4662 0.5362 0.2347  0.1234  0.0610  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.8614 0.4773 0.5442 0.2587  0.1233  0.0885  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.8704 0.4859 0.5567 0.2863  0.1242  0.0912  53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.8268 0.5068 0.5168 0.2250  0.1131  0.0534  53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.8236 0.5427 0.5206 0.2466  0.1098  0.0495  53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.8241 0.5083 0.5165 0.2004  0.1127  0.0332  53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.8138 0.5918 0.5146 0.2364  0.0999  0.0505  53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.8634 0.4784 0.5351 0.2504  0.1226  0.1090  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.8676 0.4867 0.5267 0.2709  0.1210  0.1376  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.8535 0.5214 0.5010 0.2604  0.1094  0.1421  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.8426 0.5127 0.4877 0.2363  0.1096  0.1343  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.9169 0.4810 0.5699 0.2699  0.1343  0.1593  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 1.0094 0.5146 0.6732 0.2836  0.1455  0.1593  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 1.1366 0.5828 0.7992 0.2773  0.1601  0.1829  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 1.1513 0.6059 0.8064 0.2577  0.1635  0.1960  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.1886 0.5795 0.8590 0.2924  0.1691  0.1890  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.8439 0.5507 0.4849 0.2794  0.0985  0.1532  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.8299 0.5809 0.4603 0.2703  0.0853  0.1532  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.8493 0.5844 0.4574 0.2665  0.0900  0.1702  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.8623 0.5710 0.4596 0.2832  0.0991  0.1939  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.8169 0.6177 0.4495 0.2907  0.0706  0.1580  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.8126 0.6602 0.4459 0.2735  0.0545  0.1447  55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.8089 0.7126 0.4516 0.2878  0.0382  0.1457  55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.8132 0.7528 0.4593 0.2658  0.0227  0.1305  55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.8283 0.7871 0.4560 0.2650  0.0098  0.1313  55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.8308 0.7847 0.4334 0.2868  0.0106  0.1497  55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.8144 0.7968 0.4474 0.2435  -0.0040 0.1138  55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.8451 0.5965 0.4464 0.2459  0.0852  0.1593  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.8596 0.6044 0.4397 0.2413  0.0907  0.1715  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.8559 0.6433 0.4145 0.2483  0.0755  0.1714  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.8671 0.6546 0.4022 0.2536  0.0804  0.1855  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.8639 0.5916 0.4519 0.2153  0.0990  0.1581  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.8391 0.6633 0.4062 0.2474  0.0576  0.1551  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.8323 0.6961 0.3814 0.2521  0.0402  0.1499  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.8199 0.7147 0.3852 0.2363  0.0221  0.1249  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.8091 0.6992 0.3999 0.2221  0.0237  0.1139  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.8146 0.7422 0.3648 0.2385  0.0045  0.1159  58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.8072 0.7602 0.3747 0.2203  -0.0137 0.0920  58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.8344 0.7634 0.3984 0.1998  -0.0111 0.0752  58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.8507 0.7602 0.3911 0.2040  -0.0010 0.0791  58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.7957 0.7933 0.3511 0.2294  -0.0366 0.0845  58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.7957 0.8316 0.3622 0.2487  -0.0452 0.0972  58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.7998 0.8243 0.3834 0.2570  -0.0323 0.1118  58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.7719 0.8512 0.3293 0.2573  -0.0657 0.0910  58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.8356 0.7685 0.4233 0.1790  -0.0199 0.0584  59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.8619 0.7714 0.4469 0.1625  -0.0191 0.0432  59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.8831 0.8081 0.4580 0.1580  -0.0399 0.0226  59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.8685 0.8055 0.4659 0.1417  -0.0543 0.0096  59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.8610 0.7561 0.4746 0.1443  -0.0123 0.0412  59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.8733 0.7516 0.4911 0.1509  0.0071  0.0564  59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.8751 0.7465 0.4858 0.1308  -0.0126 0.0280  59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.8812 0.7558 0.5236 0.1378  0.0128  0.0549  59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.9091 0.8355 0.4500 0.1726  -0.0411 0.0195  60  THR   A N   
83   N  N   B THR   A 17  ? 0.9083 0.8346 0.4491 0.1726  -0.0411 0.0195  60  THR   A N   
84   C  CA  A THR   A 17  ? 0.9318 0.8714 0.4560 0.1719  -0.0611 -0.0046 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.9298 0.8714 0.4534 0.1729  -0.0615 -0.0039 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.9687 0.8877 0.4611 0.1804  -0.0527 -0.0129 60  THR   A C   
87   C  C   B THR   A 17  ? 0.9687 0.8912 0.4589 0.1821  -0.0537 -0.0126 60  THR   A C   
88   O  O   A THR   A 17  ? 0.9792 0.8873 0.4573 0.1915  -0.0324 0.0055  60  THR   A O   
89   O  O   B THR   A 17  ? 0.9807 0.8950 0.4541 0.1950  -0.0342 0.0064  60  THR   A O   
90   C  CB  A THR   A 17  ? 0.9371 0.9200 0.4459 0.1882  -0.0772 -0.0035 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.9306 0.9160 0.4426 0.1891  -0.0761 0.0005  60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.9531 0.9400 0.4393 0.2117  -0.0616 0.0235  60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.9225 0.9313 0.4712 0.1787  -0.0854 0.0035  60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.9198 0.9344 0.4637 0.1775  -0.0930 -0.0052 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.9324 0.9390 0.4181 0.1942  -0.0977 -0.0249 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.9851 0.9000 0.4679 0.1753  -0.0682 -0.0413 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 1.0328 0.9338 0.4836 0.1873  -0.0618 -0.0536 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 1.0674 1.0027 0.4776 0.2110  -0.0676 -0.0539 61  TRP   A C   
99   O  O   . TRP   A 18  ? 1.0649 1.0267 0.4696 0.2117  -0.0908 -0.0706 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 1.0372 0.9154 0.4937 0.1748  -0.0774 -0.0869 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 1.0571 0.9231 0.4802 0.1908  -0.0728 -0.1050 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 1.0749 0.9632 0.4573 0.2108  -0.0812 -0.1222 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 1.0671 0.8989 0.4950 0.1896  -0.0608 -0.1109 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 1.0912 0.9613 0.4524 0.2231  -0.0729 -0.1385 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 1.0893 0.9245 0.4795 0.2106  -0.0607 -0.1315 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 1.0702 0.8733 0.5293 0.1754  -0.0502 -0.1002 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 1.1051 0.9156 0.4912 0.2185  -0.0497 -0.1415 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 1.0894 0.8686 0.5436 0.1828  -0.0407 -0.1089 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 1.1018 0.8848 0.5214 0.2045  -0.0400 -0.1288 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 1.0941 1.0327 0.4764 0.2297  -0.0471 -0.0348 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.1171 1.0908 0.4565 0.2549  -0.0494 -0.0294 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.1521 1.1287 0.4554 0.2678  -0.0512 -0.0554 62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.1649 1.1212 0.4667 0.2689  -0.0323 -0.0534 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.1488 1.1270 0.4788 0.2687  -0.0241 0.0124  62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.2299 1.1952 0.5964 0.2578  -0.0178 0.0369  62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.3187 1.3094 0.6979 0.2592  -0.0381 0.0374  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.3200 1.3473 0.6726 0.2745  -0.0558 0.0290  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.3505 1.3292 0.7662 0.2464  -0.0362 0.0460  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.1628 1.1673 0.4376 0.2786  -0.0745 -0.0820 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.1942 1.2036 0.4294 0.2950  -0.0774 -0.1115 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.2134 1.2498 0.4073 0.3225  -0.0534 -0.0842 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.2122 1.2741 0.3959 0.3331  -0.0467 -0.0506 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.2232 1.2570 0.4385 0.2983  -0.1112 -0.1513 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.2826 1.2939 0.5432 0.2676  -0.1356 -0.1759 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.3369 1.3786 0.5824 0.2678  -0.1711 -0.2149 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.3748 1.3989 0.6720 0.2333  -0.1939 -0.2340 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.3909 1.4624 0.6855 0.2305  -0.2273 -0.2571 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.2296 1.2611 0.4006 0.3350  -0.0394 -0.0965 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.2481 1.3086 0.3824 0.3597  -0.0129 -0.0691 64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.2451 1.2922 0.4092 0.3491  0.0153  -0.0202 64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.2448 1.3131 0.3951 0.3596  0.0269  0.0167  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.2827 1.3949 0.3641 0.3869  -0.0227 -0.0659 64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.3582 1.4884 0.4078 0.3973  -0.0541 -0.1183 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.3787 1.4924 0.4188 0.4010  -0.0555 -0.1546 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.3821 1.5437 0.4165 0.4028  -0.0780 -0.1241 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.2395 1.2493 0.4460 0.3277  0.0240  -0.0212 65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.2338 1.2269 0.4727 0.3142  0.0488  0.0165  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.2314 1.2305 0.4658 0.3209  0.0752  0.0230  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.2370 1.2453 0.4496 0.3344  0.0717  -0.0060 65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.2317 1.1872 0.5198 0.2869  0.0396  0.0090  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.2227 1.2180 0.4791 0.3119  0.1013  0.0592  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.2202 1.2285 0.4801 0.3153  0.1266  0.0667  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.2112 1.1988 0.4957 0.3067  0.1191  0.0343  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.2135 1.1702 0.5362 0.2851  0.1118  0.0319  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.2430 1.2470 0.5321 0.3002  0.1530  0.1090  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.3034 1.3288 0.6032 0.3006  0.1788  0.1174  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.3935 1.4141 0.7293 0.2803  0.2036  0.1551  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.4249 1.4170 0.7784 0.2658  0.2007  0.1734  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.4094 1.4555 0.7575 0.2790  0.2258  0.1650  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.2002 1.2048 0.4605 0.3263  0.1199  0.0091  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.1926 1.1757 0.4729 0.3236  0.1129  -0.0207 67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.1716 1.1756 0.4709 0.3257  0.1400  -0.0052 67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.1739 1.2134 0.4469 0.3485  0.1550  -0.0074 67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.2110 1.1913 0.4570 0.3447  0.0936  -0.0647 67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.2227 1.1636 0.4962 0.3370  0.0807  -0.0926 67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.2239 1.2034 0.4428 0.3468  0.0691  -0.0783 67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.1507 1.1387 0.4956 0.3027  0.1465  0.0098  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.1287 1.1415 0.4994 0.3009  0.1700  0.0241  68  THR   A CA  
159  C  C   . THR   A 25  ? 1.1080 1.0958 0.5231 0.2827  0.1628  0.0164  68  THR   A C   
160  O  O   . THR   A 25  ? 1.1174 1.0683 0.5445 0.2682  0.1435  0.0078  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.1363 1.1730 0.5157 0.2898  0.1940  0.0653  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.1320 1.1981 0.5417 0.2847  0.2161  0.0778  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.1410 1.1445 0.5445 0.2639  0.1870  0.0829  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 1.0769 1.0902 0.5159 0.2847  0.1785  0.0205  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 1.0636 1.0623 0.5428 0.2705  0.1723  0.0155  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 1.0568 1.0547 0.5355 0.2916  0.1659  -0.0103 69  GLY   A C   
167  O  O   . GLY   A 26  ? 1.0706 1.0574 0.5167 0.3142  0.1568  -0.0342 69  GLY   A O   
168  N  N   . ASN   A 27  ? 1.0344 1.0427 0.5499 0.2851  0.1692  -0.0069 70  ASN   A N   
169  C  CA  . ASN   A 27  ? 1.0262 1.0334 0.5455 0.3074  0.1638  -0.0276 70  ASN   A CA  
170  C  C   . ASN   A 27  ? 1.0102 0.9695 0.5447 0.2980  0.1415  -0.0379 70  ASN   A C   
171  O  O   . ASN   A 27  ? 1.0107 0.9437 0.5531 0.2738  0.1314  -0.0298 70  ASN   A O   
172  C  CB  . ASN   A 27  ? 1.0258 1.0901 0.5724 0.3155  0.1842  -0.0169 70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 1.0644 1.1521 0.6537 0.2854  0.1921  0.0068  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 1.0856 1.1740 0.6787 0.2622  0.1993  0.0257  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 1.0612 1.1691 0.6838 0.2865  0.1905  0.0054  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.9987 0.9455 0.5342 0.3199  0.1345  -0.0554 71  SER   A N   
177  C  CA  . SER   A 28  ? 1.0037 0.9058 0.5518 0.3159  0.1158  -0.0624 71  SER   A CA  
178  C  C   . SER   A 28  ? 0.9790 0.9067 0.5572 0.3273  0.1204  -0.0565 71  SER   A C   
179  O  O   . SER   A 28  ? 0.9903 0.9045 0.5638 0.3547  0.1164  -0.0711 71  SER   A O   
180  C  CB  . SER   A 28  ? 1.0427 0.8962 0.5624 0.3345  0.1007  -0.0896 71  SER   A CB  
181  O  OG  . SER   A 28  ? 1.0824 0.9321 0.5683 0.3372  0.0992  -0.1019 71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.9452 0.9114 0.5549 0.3084  0.1283  -0.0367 72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.9217 0.9221 0.5609 0.3201  0.1310  -0.0318 72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.9300 0.8934 0.5780 0.3216  0.1131  -0.0320 72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.9476 0.8701 0.5898 0.3015  0.1012  -0.0292 72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.9027 0.9523 0.5721 0.2932  0.1421  -0.0132 72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.9202 0.9361 0.5797 0.2643  0.1367  -0.0072 72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.9286 0.9088 0.5495 0.2764  0.1341  -0.0193 72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.9113 0.8921 0.5741 0.3466  0.1121  -0.0328 73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.9177 0.8675 0.5889 0.3501  0.0966  -0.0273 73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.8750 0.8826 0.5796 0.3462  0.0983  -0.0127 73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.8567 0.9111 0.5774 0.3701  0.1052  -0.0131 73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.9659 0.8703 0.6215 0.3844  0.0896  -0.0403 73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 1.0607 0.9052 0.6847 0.3816  0.0837  -0.0582 73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 1.1513 0.9303 0.7627 0.4048  0.0716  -0.0711 73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.2364 0.9736 0.8178 0.4078  0.0677  -0.0963 73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.3067 0.9756 0.8744 0.4197  0.0550  -0.1136 73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.3270 0.9563 0.9082 0.4298  0.0465  -0.1040 73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.3117 0.9506 0.8523 0.4211  0.0501  -0.1403 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.8543 0.8648 0.5699 0.3155  0.0922  -0.0016 74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.8140 0.8816 0.5603 0.3041  0.0916  0.0086  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.8065 0.8625 0.5570 0.3059  0.0763  0.0185  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.8270 0.8317 0.5606 0.2951  0.0676  0.0220  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.8013 0.8860 0.5567 0.2668  0.0976  0.0112  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.8085 0.8978 0.5557 0.2596  0.1134  0.0075  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.8148 0.9034 0.5686 0.2240  0.1168  0.0129  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.7828 0.9329 0.5491 0.2757  0.1280  0.0072  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.7731 0.8842 0.5476 0.3182  0.0734  0.0245  75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.7710 0.8869 0.5498 0.3216  0.0591  0.0365  75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.7454 0.8950 0.5378 0.2863  0.0563  0.0365  75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.7221 0.9315 0.5408 0.2756  0.0615  0.0313  75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.7751 0.9446 0.5741 0.3544  0.0564  0.0416  75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.8702 0.9996 0.6551 0.3951  0.0559  0.0432  75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.9153 0.9693 0.6744 0.3955  0.0545  0.0408  75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.8887 1.0622 0.6903 0.4269  0.0560  0.0461  75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.7494 0.8616 0.5260 0.2676  0.0490  0.0409  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.7338 0.8723 0.5202 0.2365  0.0462  0.0370  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.7253 0.8690 0.5043 0.2362  0.0327  0.0462  76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.7437 0.8562 0.5065 0.2553  0.0271  0.0599  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.7590 0.8564 0.5335 0.2105  0.0540  0.0305  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.7496 0.8608 0.5344 0.2059  0.0683  0.0232  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.7984 0.8291 0.5452 0.2160  0.0512  0.0360  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.6984 0.8803 0.4884 0.2145  0.0278  0.0388  77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.6950 0.8892 0.4741 0.2134  0.0157  0.0449  77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.6937 0.8718 0.4651 0.1840  0.0167  0.0343  77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.6860 0.8757 0.4733 0.1623  0.0219  0.0186  77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.6649 0.9340 0.4634 0.2227  0.0050  0.0424  77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.6988 0.8504 0.4472 0.1841  0.0127  0.0440  78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.6975 0.8347 0.4371 0.1612  0.0142  0.0340  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.6897 0.8723 0.4238 0.1606  0.0032  0.0295  78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.6965 0.8880 0.4145 0.1780  -0.0029 0.0472  78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.7148 0.7930 0.4337 0.1607  0.0195  0.0469  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.7223 0.7847 0.4311 0.1422  0.0222  0.0397  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.7215 0.7802 0.4435 0.1230  0.0283  0.0199  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.7410 0.7554 0.4349 0.1429  0.0263  0.0548  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.6738 0.8862 0.4212 0.1413  0.0004  0.0059  79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.6595 0.9198 0.4009 0.1402  -0.0117 -0.0055 79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.6802 0.9168 0.3954 0.1345  -0.0098 -0.0069 79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.6982 0.8836 0.4040 0.1308  0.0006  0.0026  79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.6407 0.9473 0.4112 0.1217  -0.0181 -0.0338 79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.6708 0.9490 0.4528 0.0931  -0.0111 -0.0566 79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.6944 0.9201 0.4595 0.0891  -0.0016 -0.0520 79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.6559 0.9653 0.4659 0.0745  -0.0154 -0.0786 79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.6730 0.9525 0.3767 0.1355  -0.0200 -0.0193 80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.6971 0.9655 0.3751 0.1339  -0.0176 -0.0220 80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.7117 0.9441 0.3960 0.1127  -0.0097 -0.0451 80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.7313 0.9401 0.3974 0.1133  -0.0029 -0.0415 80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.7155 1.0446 0.3753 0.1441  -0.0308 -0.0310 80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.7950 1.1220 0.4213 0.1594  -0.0263 -0.0072 80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.8533 1.2416 0.4542 0.1711  -0.0372 -0.0162 80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.8528 1.2692 0.4568 0.1602  -0.0461 -0.0541 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 0.8849 1.2922 0.4618 0.1914  -0.0369 0.0148  80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.6962 0.9243 0.4076 0.0948  -0.0095 -0.0660 81  SER   A N   
254  C  CA  . SER   A 38  ? 0.7011 0.8882 0.4200 0.0760  -0.0011 -0.0843 81  SER   A CA  
255  C  C   . SER   A 38  ? 0.7091 0.8413 0.4325 0.0736  0.0130  -0.0659 81  SER   A C   
256  O  O   . SER   A 38  ? 0.7204 0.8189 0.4535 0.0594  0.0205  -0.0768 81  SER   A O   
257  C  CB  . SER   A 38  ? 0.7064 0.9113 0.4540 0.0552  -0.0066 -0.1136 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.7251 0.9872 0.4703 0.0570  -0.0226 -0.1336 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.7026 0.8248 0.4183 0.0880  0.0158  -0.0390 82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.7129 0.7880 0.4301 0.0872  0.0265  -0.0244 82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.7023 0.7725 0.4423 0.0791  0.0316  -0.0278 82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.7133 0.7466 0.4544 0.0749  0.0410  -0.0223 82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.6748 0.7882 0.4336 0.0776  0.0254  -0.0358 83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.6612 0.7817 0.4455 0.0695  0.0317  -0.0376 83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.6535 0.7902 0.4402 0.0892  0.0315  -0.0214 83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.6444 0.8135 0.4271 0.1051  0.0217  -0.0157 83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.6497 0.8104 0.4620 0.0505  0.0263  -0.0597 83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.6978 0.8337 0.5128 0.0296  0.0279  -0.0794 83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.7193 0.8072 0.5172 0.0303  0.0359  -0.0739 83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.7152 0.8804 0.5513 0.0127  0.0207  -0.1016 83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.6521 0.7671 0.4442 0.0902  0.0427  -0.0140 84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.6470 0.7732 0.4420 0.1101  0.0448  -0.0025 84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.6402 0.8181 0.4679 0.1044  0.0475  -0.0093 84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.6350 0.8220 0.4831 0.0808  0.0529  -0.0196 84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.6499 0.7290 0.4308 0.1153  0.0557  0.0060  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.6618 0.6944 0.4152 0.1240  0.0525  0.0149  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.6657 0.6899 0.4081 0.1452  0.0468  0.0258  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.6739 0.6700 0.4155 0.1114  0.0563  0.0135  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.6872 0.6677 0.4097 0.1490  0.0445  0.0347  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.6916 0.6515 0.4135 0.1172  0.0534  0.0218  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.6906 0.6429 0.4043 0.1338  0.0475  0.0322  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.6366 0.8484 0.4717 0.1264  0.0443  -0.0024 85  SER   A N   
283  C  CA  . SER   A 42  ? 0.6221 0.8927 0.4913 0.1251  0.0473  -0.0066 85  SER   A CA  
284  C  C   . SER   A 42  ? 0.6359 0.9160 0.5026 0.1571  0.0509  0.0050  85  SER   A C   
285  O  O   . SER   A 42  ? 0.6518 0.9090 0.4959 0.1808  0.0438  0.0144  85  SER   A O   
286  C  CB  . SER   A 42  ? 0.6155 0.9463 0.5060 0.1169  0.0326  -0.0182 85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.6513 1.0016 0.5276 0.1436  0.0191  -0.0101 85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.6292 0.9404 0.5187 0.1588  0.0632  0.0051  86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.6455 0.9669 0.5322 0.1926  0.0681  0.0130  86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.6236 1.0040 0.5277 0.2162  0.0562  0.0155  86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.5953 1.0410 0.5322 0.2025  0.0507  0.0089  86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.6477 0.9879 0.5501 0.1898  0.0874  0.0132  86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.7039 0.9998 0.5770 0.2153  0.0974  0.0173  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.7170 1.0065 0.5900 0.1999  0.1162  0.0182  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.7051 1.0337 0.5841 0.2544  0.0977  0.0192  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.6342 0.9918 0.5182 0.2520  0.0518  0.0251  87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.6223 1.0265 0.5170 0.2823  0.0404  0.0322  87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.6033 1.0587 0.5224 0.3095  0.0495  0.0325  87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.6141 1.0562 0.5327 0.3105  0.0659  0.0287  87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6622 1.0074 0.5222 0.3062  0.0308  0.0458  87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6524 1.0366 0.5199 0.3448  0.0208  0.0578  87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.6837 1.0017 0.5254 0.2815  0.0215  0.0470  87  VAL   A CG2 
303  N  N   . GLU   B 8   ? 0.8537 0.9094 0.7744 0.2397  0.0527  0.0568  17  GLU   B N   
304  C  CA  . GLU   B 8   ? 0.8514 0.9278 0.7811 0.2317  0.0429  0.0569  17  GLU   B CA  
305  C  C   . GLU   B 8   ? 0.8376 0.9222 0.7780 0.2087  0.0412  0.0522  17  GLU   B C   
306  O  O   . GLU   B 8   ? 0.8557 0.9153 0.7861 0.1970  0.0438  0.0517  17  GLU   B O   
307  C  CB  . GLU   B 8   ? 0.9065 0.9585 0.8175 0.2366  0.0394  0.0621  17  GLU   B CB  
308  C  CG  . GLU   B 8   ? 0.9823 1.0545 0.8994 0.2310  0.0290  0.0617  17  GLU   B CG  
309  C  CD  . GLU   B 8   ? 1.1014 1.1506 0.9991 0.2359  0.0263  0.0673  17  GLU   B CD  
310  O  OE1 . GLU   B 8   ? 1.1358 1.1504 1.0170 0.2336  0.0331  0.0706  17  GLU   B OE1 
311  O  OE2 . GLU   B 8   ? 1.1337 1.2004 1.0322 0.2414  0.0175  0.0682  17  GLU   B OE2 
312  N  N   . THR   B 9   ? 0.8023 0.9228 0.7623 0.2027  0.0369  0.0489  18  THR   B N   
313  C  CA  . THR   B 9   ? 0.7824 0.9106 0.7513 0.1818  0.0354  0.0447  18  THR   B CA  
314  C  C   . THR   B 9   ? 0.7481 0.8838 0.7171 0.1732  0.0251  0.0434  18  THR   B C   
315  O  O   . THR   B 9   ? 0.7425 0.8856 0.7179 0.1566  0.0229  0.0396  18  THR   B O   
316  C  CB  . THR   B 9   ? 0.7919 0.9537 0.7814 0.1779  0.0381  0.0418  18  THR   B CB  
317  O  OG1 . THR   B 9   ? 0.7885 0.9860 0.7914 0.1888  0.0320  0.0424  18  THR   B OG1 
318  C  CG2 . THR   B 9   ? 0.8036 0.9564 0.7913 0.1841  0.0491  0.0419  18  THR   B CG2 
319  N  N   . THR   B 10  ? 0.7271 0.8589 0.6868 0.1848  0.0191  0.0465  19  THR   B N   
320  C  CA  . THR   B 10  ? 0.7054 0.8435 0.6618 0.1804  0.0088  0.0453  19  THR   B CA  
321  C  C   . THR   B 10  ? 0.6866 0.7998 0.6310 0.1659  0.0088  0.0438  19  THR   B C   
322  O  O   . THR   B 10  ? 0.6963 0.7815 0.6276 0.1666  0.0151  0.0467  19  THR   B O   
323  C  CB  . THR   B 10  ? 0.7373 0.8710 0.6818 0.1991  0.0047  0.0504  19  THR   B CB  
324  O  OG1 . THR   B 10  ? 0.7521 0.9099 0.7067 0.2153  0.0049  0.0520  19  THR   B OG1 
325  C  CG2 . THR   B 10  ? 0.7390 0.8806 0.6782 0.1971  -0.0065 0.0489  19  THR   B CG2 
326  N  N   . ASP   B 11  ? 0.6562 0.7797 0.6039 0.1530  0.0017  0.0390  20  ASP   B N   
327  C  CA  . ASP   B 11  ? 0.6464 0.7470 0.5802 0.1419  0.0007  0.0372  20  ASP   B CA  
328  C  C   . ASP   B 11  ? 0.6319 0.7122 0.5469 0.1523  -0.0008 0.0417  20  ASP   B C   
329  O  O   . ASP   B 11  ? 0.6315 0.7206 0.5441 0.1645  -0.0058 0.0442  20  ASP   B O   
330  C  CB  . ASP   B 11  ? 0.6622 0.7761 0.5993 0.1289  -0.0083 0.0310  20  ASP   B CB  
331  C  CG  . ASP   B 11  ? 0.7078 0.8227 0.6524 0.1113  -0.0048 0.0269  20  ASP   B CG  
332  O  OD1 . ASP   B 11  ? 0.7063 0.8313 0.6639 0.1102  0.0027  0.0280  20  ASP   B OD1 
333  O  OD2 . ASP   B 11  ? 0.7307 0.8343 0.6659 0.0990  -0.0090 0.0227  20  ASP   B OD2 
334  N  N   . GLY   B 12  ? 0.6173 0.6730 0.5193 0.1483  0.0041  0.0433  21  GLY   B N   
335  C  CA  . GLY   B 12  ? 0.6066 0.6453 0.4915 0.1563  0.0041  0.0481  21  GLY   B CA  
336  C  C   . GLY   B 12  ? 0.5915 0.6094 0.4685 0.1546  0.0132  0.0519  21  GLY   B C   
337  O  O   . GLY   B 12  ? 0.5831 0.5986 0.4669 0.1481  0.0191  0.0504  21  GLY   B O   
338  N  N   . VAL   B 13  ? 0.5864 0.5911 0.4488 0.1599  0.0143  0.0568  22  VAL   B N   
339  C  CA  . VAL   B 13  ? 0.5851 0.5743 0.4411 0.1568  0.0226  0.0604  22  VAL   B CA  
340  C  C   . VAL   B 13  ? 0.5727 0.5530 0.4283 0.1627  0.0286  0.0655  22  VAL   B C   
341  O  O   . VAL   B 13  ? 0.5607 0.5422 0.4135 0.1733  0.0263  0.0687  22  VAL   B O   
342  C  CB  . VAL   B 13  ? 0.6027 0.5842 0.4439 0.1573  0.0224  0.0632  22  VAL   B CB  
343  C  CG1 . VAL   B 13  ? 0.6036 0.5844 0.4341 0.1681  0.0186  0.0678  22  VAL   B CG1 
344  C  CG2 . VAL   B 13  ? 0.6150 0.5872 0.4528 0.1524  0.0307  0.0667  22  VAL   B CG2 
345  N  N   . TYR   B 14  ? 0.5685 0.5392 0.4257 0.1563  0.0360  0.0654  23  TYR   B N   
346  C  CA  . TYR   B 14  ? 0.5709 0.5275 0.4247 0.1600  0.0421  0.0689  23  TYR   B CA  
347  C  C   . TYR   B 14  ? 0.5964 0.5374 0.4414 0.1523  0.0488  0.0721  23  TYR   B C   
348  O  O   . TYR   B 14  ? 0.6022 0.5476 0.4486 0.1432  0.0497  0.0700  23  TYR   B O   
349  C  CB  . TYR   B 14  ? 0.5500 0.5102 0.4144 0.1594  0.0446  0.0643  23  TYR   B CB  
350  C  CG  . TYR   B 14  ? 0.5314 0.5093 0.4057 0.1683  0.0396  0.0625  23  TYR   B CG  
351  C  CD1 . TYR   B 14  ? 0.5212 0.5191 0.4048 0.1645  0.0328  0.0585  23  TYR   B CD1 
352  C  CD2 . TYR   B 14  ? 0.5394 0.5143 0.4131 0.1804  0.0417  0.0645  23  TYR   B CD2 
353  C  CE1 . TYR   B 14  ? 0.5170 0.5359 0.4110 0.1711  0.0275  0.0567  23  TYR   B CE1 
354  C  CE2 . TYR   B 14  ? 0.5393 0.5366 0.4234 0.1899  0.0368  0.0631  23  TYR   B CE2 
355  C  CZ  . TYR   B 14  ? 0.5346 0.5563 0.4306 0.1840  0.0295  0.0590  23  TYR   B CZ  
356  O  OH  . TYR   B 14  ? 0.5420 0.5910 0.4511 0.1906  0.0243  0.0570  23  TYR   B OH  
357  N  N   . ARG   B 15  ? 0.6095 0.5322 0.4448 0.1556  0.0537  0.0771  24  ARG   B N   
358  C  CA  . ARG   B 15  ? 0.6230 0.5299 0.4503 0.1458  0.0606  0.0799  24  ARG   B CA  
359  C  C   . ARG   B 15  ? 0.6292 0.5274 0.4599 0.1396  0.0647  0.0746  24  ARG   B C   
360  O  O   . ARG   B 15  ? 0.6301 0.5226 0.4617 0.1477  0.0651  0.0728  24  ARG   B O   
361  C  CB  . ARG   B 15  ? 0.6431 0.5286 0.4551 0.1516  0.0646  0.0879  24  ARG   B CB  
362  C  CG  . ARG   B 15  ? 0.6618 0.5520 0.4661 0.1576  0.0622  0.0944  24  ARG   B CG  
363  C  CD  . ARG   B 15  ? 0.7160 0.5806 0.5029 0.1597  0.0687  0.1030  24  ARG   B CD  
364  N  NE  . ARG   B 15  ? 0.7554 0.6221 0.5324 0.1715  0.0660  0.1099  24  ARG   B NE  
365  C  CZ  . ARG   B 15  ? 0.7702 0.6418 0.5408 0.1681  0.0677  0.1153  24  ARG   B CZ  
366  N  NH1 . ARG   B 15  ? 0.7483 0.6253 0.5227 0.1531  0.0723  0.1150  24  ARG   B NH1 
367  N  NH2 . ARG   B 15  ? 0.7733 0.6464 0.5331 0.1806  0.0649  0.1211  24  ARG   B NH2 
368  N  N   . VAL   B 16  ? 0.6359 0.5338 0.4673 0.1263  0.0678  0.0723  25  VAL   B N   
369  C  CA  . VAL   B 16  ? 0.6569 0.5447 0.4885 0.1195  0.0716  0.0668  25  VAL   B CA  
370  C  C   . VAL   B 16  ? 0.6835 0.5465 0.5014 0.1115  0.0775  0.0701  25  VAL   B C   
371  O  O   . VAL   B 16  ? 0.6826 0.5494 0.4986 0.1004  0.0792  0.0727  25  VAL   B O   
372  C  CB  . VAL   B 16  ? 0.6509 0.5558 0.4915 0.1102  0.0703  0.0608  25  VAL   B CB  
373  C  CG1 . VAL   B 16  ? 0.6544 0.5483 0.4932 0.1049  0.0737  0.0548  25  VAL   B CG1 
374  C  CG2 . VAL   B 16  ? 0.6455 0.5702 0.4965 0.1164  0.0652  0.0585  25  VAL   B CG2 
375  N  N   . MET   B 17  ? 0.7046 0.5421 0.5119 0.1175  0.0810  0.0702  26  MET   B N   
376  C  CA  . MET   B 17  ? 0.7394 0.5456 0.5294 0.1105  0.0871  0.0738  26  MET   B CA  
377  C  C   . MET   B 17  ? 0.7816 0.5674 0.5642 0.1019  0.0908  0.0668  26  MET   B C   
378  O  O   . MET   B 17  ? 0.7821 0.5717 0.5695 0.1086  0.0896  0.0604  26  MET   B O   
379  C  CB  . MET   B 17  ? 0.7487 0.5331 0.5251 0.1268  0.0888  0.0804  26  MET   B CB  
380  C  CG  . MET   B 17  ? 0.7447 0.5476 0.5256 0.1373  0.0844  0.0869  26  MET   B CG  
381  S  SD  . MET   B 17  ? 0.7181 0.5241 0.4942 0.1241  0.0870  0.0946  26  MET   B SD  
382  C  CE  . MET   B 17  ? 0.6636 0.4240 0.4139 0.1212  0.0959  0.1018  26  MET   B CE  
383  N  N   . THR   B 18  ? 0.8184 0.5808 0.5876 0.0870  0.0957  0.0680  27  THR   B N   
384  C  CA  . THR   B 18  ? 0.8631 0.5999 0.6206 0.0779  0.0990  0.0606  27  THR   B CA  
385  C  C   . THR   B 18  ? 0.9251 0.6159 0.6573 0.0735  0.1057  0.0648  27  THR   B C   
386  O  O   . THR   B 18  ? 0.9293 0.6130 0.6552 0.0696  0.1084  0.0737  27  THR   B O   
387  C  CB  . THR   B 18  ? 0.8674 0.6243 0.6346 0.0589  0.0970  0.0536  27  THR   B CB  
388  O  OG1 . THR   B 18  ? 0.8956 0.6344 0.6542 0.0566  0.0981  0.0442  27  THR   B OG1 
389  C  CG2 . THR   B 18  ? 0.8674 0.6232 0.6310 0.0381  0.0995  0.0571  27  THR   B CG2 
390  N  N   . ARG   B 19  ? 0.9708 0.6279 0.6860 0.0747  0.1089  0.0586  28  ARG   B N   
391  C  CA  . ARG   B 19  ? 1.0300 0.6359 0.7165 0.0697  0.1157  0.0616  28  ARG   B CA  
392  C  C   . ARG   B 19  ? 1.0605 0.6449 0.7355 0.0444  0.1180  0.0532  28  ARG   B C   
393  O  O   . ARG   B 19  ? 1.0932 0.6305 0.7418 0.0362  0.1239  0.0545  28  ARG   B O   
394  C  CB  . ARG   B 19  ? 1.0787 0.6528 0.7470 0.0951  0.1186  0.0631  28  ARG   B CB  
395  C  CG  . ARG   B 19  ? 1.1456 0.7231 0.8130 0.1139  0.1187  0.0748  28  ARG   B CG  
396  C  CD  . ARG   B 19  ? 1.2221 0.7778 0.8748 0.1423  0.1205  0.0762  28  ARG   B CD  
397  N  NE  . ARG   B 19  ? 1.2771 0.8390 0.9285 0.1609  0.1195  0.0871  28  ARG   B NE  
398  C  CZ  . ARG   B 19  ? 1.2997 0.8915 0.9652 0.1836  0.1144  0.0882  28  ARG   B CZ  
399  N  NH1 . ARG   B 19  ? 1.2839 0.9024 0.9668 0.1900  0.1109  0.0798  28  ARG   B NH1 
400  N  NH2 . ARG   B 19  ? 1.2981 0.8947 0.9601 0.1994  0.1129  0.0978  28  ARG   B NH2 
401  N  N   . ARG   B 20  ? 1.0477 0.6669 0.7413 0.0314  0.1130  0.0450  29  ARG   B N   
402  C  CA  . ARG   B 20  ? 1.0671 0.6780 0.7545 0.0072  0.1128  0.0356  29  ARG   B CA  
403  C  C   . ARG   B 20  ? 1.0661 0.6734 0.7501 -0.0188 0.1156  0.0404  29  ARG   B C   
404  O  O   . ARG   B 20  ? 1.0873 0.6627 0.7530 -0.0389 0.1185  0.0353  29  ARG   B O   
405  C  CB  . ARG   B 20  ? 1.0802 0.7373 0.7907 0.0047  0.1061  0.0276  29  ARG   B CB  
406  C  CG  . ARG   B 20  ? 1.1589 0.8102 0.8623 -0.0163 0.1043  0.0159  29  ARG   B CG  
407  C  CD  . ARG   B 20  ? 1.2022 0.9016 0.9274 -0.0183 0.0977  0.0098  29  ARG   B CD  
408  N  NE  . ARG   B 20  ? 1.2382 0.9807 0.9844 -0.0279 0.0948  0.0158  29  ARG   B NE  
409  C  CZ  . ARG   B 20  ? 1.2708 1.0297 1.0208 -0.0515 0.0933  0.0136  29  ARG   B CZ  
410  N  NH1 . ARG   B 20  ? 1.2898 1.0242 1.0241 -0.0706 0.0937  0.0048  29  ARG   B NH1 
411  N  NH2 . ARG   B 20  ? 1.2461 1.0473 1.0154 -0.0559 0.0912  0.0196  29  ARG   B NH2 
412  N  N   . LEU   B 21  ? 1.0387 0.6792 0.7398 -0.0190 0.1149  0.0498  30  LEU   B N   
413  C  CA  . LEU   B 21  ? 1.0329 0.6792 0.7347 -0.0418 0.1183  0.0562  30  LEU   B CA  
414  C  C   . LEU   B 21  ? 1.0502 0.6503 0.7277 -0.0393 0.1265  0.0670  30  LEU   B C   
415  O  O   . LEU   B 21  ? 1.0798 0.6394 0.7373 -0.0214 0.1290  0.0674  30  LEU   B O   
416  C  CB  . LEU   B 21  ? 1.0078 0.7118 0.7373 -0.0397 0.1143  0.0615  30  LEU   B CB  
417  C  CG  . LEU   B 21  ? 1.0085 0.7578 0.7590 -0.0472 0.1075  0.0527  30  LEU   B CG  
418  C  CD1 . LEU   B 21  ? 1.0107 0.7699 0.7685 -0.0262 0.1022  0.0464  30  LEU   B CD1 
419  C  CD2 . LEU   B 21  ? 0.9956 0.7934 0.7666 -0.0500 0.1059  0.0592  30  LEU   B CD2 
420  N  N   . LEU   B 22  ? 1.0281 0.6334 0.7056 -0.0561 0.1312  0.0762  31  LEU   B N   
421  C  CA  . LEU   B 22  ? 1.0382 0.5991 0.6909 -0.0538 0.1398  0.0877  31  LEU   B CA  
422  C  C   . LEU   B 22  ? 1.0214 0.5873 0.6757 -0.0217 0.1386  0.0961  31  LEU   B C   
423  O  O   . LEU   B 22  ? 0.9990 0.6130 0.6774 -0.0123 0.1333  0.0981  31  LEU   B O   
424  C  CB  . LEU   B 22  ? 1.0278 0.6018 0.6836 -0.0788 0.1454  0.0965  31  LEU   B CB  
425  C  CG  . LEU   B 22  ? 1.0564 0.5824 0.6843 -0.0797 0.1554  0.1091  31  LEU   B CG  
426  C  CD1 . LEU   B 22  ? 1.0820 0.5544 0.6827 -0.1057 0.1619  0.1054  31  LEU   B CD1 
427  C  CD2 . LEU   B 22  ? 1.0476 0.6062 0.6871 -0.0852 0.1594  0.1219  31  LEU   B CD2 
428  N  N   . GLY   B 23  ? 1.0294 0.5461 0.6571 -0.0047 0.1429  0.1003  32  GLY   B N   
429  C  CA  . GLY   B 23  ? 1.0233 0.5417 0.6494 0.0267  0.1414  0.1078  32  GLY   B CA  
430  C  C   . GLY   B 23  ? 0.9914 0.5556 0.6441 0.0454  0.1320  0.1016  32  GLY   B C   
431  O  O   . GLY   B 23  ? 0.9889 0.5657 0.6523 0.0415  0.1278  0.0902  32  GLY   B O   
432  N  N   . SER   B 24  ? 0.9684 0.5579 0.6311 0.0646  0.1287  0.1087  33  SER   B N   
433  C  CA  . SER   B 24  ? 0.9443 0.5776 0.6321 0.0797  0.1199  0.1032  33  SER   B CA  
434  C  C   . SER   B 24  ? 0.9014 0.5814 0.6124 0.0679  0.1162  0.1038  33  SER   B C   
435  O  O   . SER   B 24  ? 0.8893 0.5816 0.6010 0.0717  0.1169  0.1127  33  SER   B O   
436  C  CB  . SER   B 24  ? 0.9779 0.6116 0.6621 0.1081  0.1172  0.1090  33  SER   B CB  
437  O  OG  . SER   B 24  ? 1.0325 0.6481 0.7093 0.1250  0.1165  0.1038  33  SER   B OG  
438  N  N   . THR   B 25  ? 0.8764 0.5817 0.6042 0.0548  0.1127  0.0945  34  THR   B N   
439  C  CA  . THR   B 25  ? 0.8429 0.5922 0.5908 0.0454  0.1094  0.0947  34  THR   B CA  
440  C  C   . THR   B 25  ? 0.8011 0.5848 0.5678 0.0606  0.1015  0.0902  34  THR   B C   
441  O  O   . THR   B 25  ? 0.8043 0.5878 0.5756 0.0664  0.0983  0.0822  34  THR   B O   
442  C  CB  . THR   B 25  ? 0.8601 0.6174 0.6129 0.0202  0.1107  0.0883  34  THR   B CB  
443  O  OG1 . THR   B 25  ? 0.8913 0.6179 0.6267 0.0026  0.1183  0.0932  34  THR   B OG1 
444  C  CG2 . THR   B 25  ? 0.8407 0.6468 0.6145 0.0134  0.1070  0.0878  34  THR   B CG2 
445  N  N   . GLN   B 26  ? 0.7639 0.5753 0.5397 0.0668  0.0988  0.0954  35  GLN   B N   
446  C  CA  . GLN   B 26  ? 0.7302 0.5714 0.5215 0.0784  0.0915  0.0910  35  GLN   B CA  
447  C  C   . GLN   B 26  ? 0.7053 0.5735 0.5098 0.0660  0.0896  0.0849  35  GLN   B C   
448  O  O   . GLN   B 26  ? 0.6999 0.5841 0.5070 0.0551  0.0918  0.0884  35  GLN   B O   
449  C  CB  . GLN   B 26  ? 0.7295 0.5857 0.5214 0.0906  0.0890  0.0980  35  GLN   B CB  
450  C  CG  . GLN   B 26  ? 0.7300 0.6130 0.5350 0.1007  0.0814  0.0931  35  GLN   B CG  
451  C  CD  . GLN   B 26  ? 0.7449 0.6369 0.5466 0.1136  0.0782  0.0987  35  GLN   B CD  
452  O  OE1 . GLN   B 26  ? 0.7637 0.6398 0.5546 0.1230  0.0792  0.1045  35  GLN   B OE1 
453  N  NE2 . GLN   B 26  ? 0.7213 0.6374 0.5300 0.1155  0.0742  0.0970  35  GLN   B NE2 
454  N  N   . VAL   B 27  ? 0.6851 0.5596 0.4973 0.0680  0.0859  0.0763  36  VAL   B N   
455  C  CA  . VAL   B 27  ? 0.6624 0.5621 0.4853 0.0590  0.0835  0.0706  36  VAL   B CA  
456  C  C   . VAL   B 27  ? 0.6337 0.5606 0.4665 0.0694  0.0784  0.0702  36  VAL   B C   
457  O  O   . VAL   B 27  ? 0.6175 0.5677 0.4568 0.0645  0.0769  0.0682  36  VAL   B O   
458  C  CB  . VAL   B 27  ? 0.6799 0.5693 0.5022 0.0534  0.0833  0.0615  36  VAL   B CB  
459  C  CG1 . VAL   B 27  ? 0.7029 0.5627 0.5121 0.0408  0.0884  0.0608  36  VAL   B CG1 
460  C  CG2 . VAL   B 27  ? 0.6892 0.5719 0.5133 0.0682  0.0809  0.0578  36  VAL   B CG2 
461  N  N   . GLY   B 28  ? 0.6256 0.5489 0.4583 0.0836  0.0755  0.0718  37  GLY   B N   
462  C  CA  . GLY   B 28  ? 0.6156 0.5585 0.4547 0.0923  0.0705  0.0706  37  GLY   B CA  
463  C  C   . GLY   B 28  ? 0.6104 0.5484 0.4487 0.1055  0.0668  0.0720  37  GLY   B C   
464  O  O   . GLY   B 28  ? 0.6227 0.5452 0.4549 0.1104  0.0682  0.0759  37  GLY   B O   
465  N  N   . VAL   B 29  ? 0.5886 0.5396 0.4318 0.1112  0.0620  0.0690  38  VAL   B N   
466  C  CA  . VAL   B 29  ? 0.5820 0.5341 0.4258 0.1215  0.0570  0.0690  38  VAL   B CA  
467  C  C   . VAL   B 29  ? 0.5735 0.5328 0.4251 0.1216  0.0538  0.0625  38  VAL   B C   
468  O  O   . VAL   B 29  ? 0.5682 0.5323 0.4219 0.1158  0.0553  0.0593  38  VAL   B O   
469  C  CB  . VAL   B 29  ? 0.5820 0.5418 0.4191 0.1266  0.0543  0.0729  38  VAL   B CB  
470  C  CG1 . VAL   B 29  ? 0.5862 0.5475 0.4223 0.1359  0.0479  0.0719  38  VAL   B CG1 
471  C  CG2 . VAL   B 29  ? 0.5879 0.5429 0.4171 0.1252  0.0589  0.0803  38  VAL   B CG2 
472  N  N   . GLY   B 30  ? 0.5681 0.5294 0.4235 0.1278  0.0497  0.0609  39  GLY   B N   
473  C  CA  . GLY   B 30  ? 0.5624 0.5310 0.4254 0.1261  0.0474  0.0556  39  GLY   B CA  
474  C  C   . GLY   B 30  ? 0.5539 0.5298 0.4203 0.1308  0.0412  0.0542  39  GLY   B C   
475  O  O   . GLY   B 30  ? 0.5488 0.5248 0.4122 0.1375  0.0381  0.0572  39  GLY   B O   
476  N  N   . VAL   B 31  ? 0.5484 0.5308 0.4206 0.1265  0.0394  0.0498  40  VAL   B N   
477  C  CA  . VAL   B 31  ? 0.5419 0.5331 0.4181 0.1272  0.0330  0.0473  40  VAL   B CA  
478  C  C   . VAL   B 31  ? 0.5336 0.5365 0.4240 0.1248  0.0337  0.0443  40  VAL   B C   
479  O  O   . VAL   B 31  ? 0.5345 0.5372 0.4287 0.1187  0.0381  0.0421  40  VAL   B O   
480  C  CB  . VAL   B 31  ? 0.5488 0.5354 0.4159 0.1224  0.0300  0.0449  40  VAL   B CB  
481  C  CG1 . VAL   B 31  ? 0.5527 0.5460 0.4232 0.1184  0.0236  0.0407  40  VAL   B CG1 
482  C  CG2 . VAL   B 31  ? 0.5624 0.5418 0.4156 0.1277  0.0288  0.0481  40  VAL   B CG2 
483  N  N   . MET   B 32  ? 0.5243 0.5395 0.4221 0.1305  0.0296  0.0444  41  MET   B N   
484  C  CA  . MET   B 32  ? 0.5158 0.5485 0.4290 0.1294  0.0303  0.0419  41  MET   B CA  
485  C  C   . MET   B 32  ? 0.5238 0.5699 0.4419 0.1221  0.0232  0.0381  41  MET   B C   
486  O  O   . MET   B 32  ? 0.5284 0.5782 0.4424 0.1253  0.0159  0.0380  41  MET   B O   
487  C  CB  . MET   B 32  ? 0.5031 0.5437 0.4216 0.1420  0.0307  0.0445  41  MET   B CB  
488  C  CG  . MET   B 32  ? 0.5037 0.5656 0.4383 0.1433  0.0326  0.0424  41  MET   B CG  
489  S  SD  . MET   B 32  ? 0.5324 0.5846 0.4678 0.1433  0.0436  0.0420  41  MET   B SD  
490  C  CE  . MET   B 32  ? 0.5160 0.5455 0.4373 0.1573  0.0466  0.0465  41  MET   B CE  
491  N  N   . GLN   B 33  ? 0.5320 0.5822 0.4561 0.1110  0.0257  0.0351  42  GLN   B N   
492  C  CA  . GLN   B 33  ? 0.5345 0.5936 0.4618 0.0998  0.0200  0.0310  42  GLN   B CA  
493  C  C   . GLN   B 33  ? 0.5312 0.6043 0.4725 0.0905  0.0254  0.0294  42  GLN   B C   
494  O  O   . GLN   B 33  ? 0.5339 0.5972 0.4730 0.0892  0.0335  0.0307  42  GLN   B O   
495  C  CB  . GLN   B 33  ? 0.5617 0.5970 0.4705 0.0932  0.0186  0.0296  42  GLN   B CB  
496  C  CG  . GLN   B 33  ? 0.6055 0.6423 0.5125 0.0805  0.0125  0.0248  42  GLN   B CG  
497  C  CD  . GLN   B 33  ? 0.6951 0.7035 0.5791 0.0779  0.0114  0.0237  42  GLN   B CD  
498  O  OE1 . GLN   B 33  ? 0.7244 0.7181 0.6003 0.0682  0.0148  0.0223  42  GLN   B OE1 
499  N  NE2 . GLN   B 33  ? 0.7057 0.7051 0.5769 0.0880  0.0075  0.0249  42  GLN   B NE2 
500  N  N   . GLU   B 34  ? 0.5187 0.6175 0.4749 0.0844  0.0210  0.0268  43  GLU   B N   
501  C  CA  . GLU   B 34  ? 0.5117 0.6300 0.4836 0.0745  0.0261  0.0257  43  GLU   B CA  
502  C  C   . GLU   B 34  ? 0.5077 0.6328 0.4875 0.0843  0.0356  0.0287  43  GLU   B C   
503  O  O   . GLU   B 34  ? 0.5023 0.6268 0.4848 0.0774  0.0435  0.0291  43  GLU   B O   
504  C  CB  . GLU   B 34  ? 0.5505 0.6502 0.5125 0.0575  0.0290  0.0240  43  GLU   B CB  
505  C  CG  . GLU   B 34  ? 0.6203 0.7079 0.5703 0.0479  0.0199  0.0202  43  GLU   B CG  
506  C  CD  . GLU   B 34  ? 0.7065 0.7713 0.6433 0.0315  0.0231  0.0186  43  GLU   B CD  
507  O  OE1 . GLU   B 34  ? 0.7283 0.8067 0.6765 0.0176  0.0271  0.0180  43  GLU   B OE1 
508  O  OE2 . GLU   B 34  ? 0.7430 0.7759 0.6569 0.0333  0.0220  0.0184  43  GLU   B OE2 
509  N  N   . GLY   B 35  ? 0.5027 0.6318 0.4838 0.1008  0.0348  0.0309  44  GLY   B N   
510  C  CA  . GLY   B 35  ? 0.4991 0.6302 0.4839 0.1118  0.0433  0.0330  44  GLY   B CA  
511  C  C   . GLY   B 35  ? 0.5100 0.6115 0.4799 0.1116  0.0503  0.0340  44  GLY   B C   
512  O  O   . GLY   B 35  ? 0.5263 0.6267 0.4971 0.1184  0.0577  0.0346  44  GLY   B O   
513  N  N   . VAL   B 36  ? 0.5036 0.5822 0.4590 0.1047  0.0481  0.0338  45  VAL   B N   
514  C  CA  . VAL   B 36  ? 0.5041 0.5585 0.4454 0.1040  0.0534  0.0345  45  VAL   B CA  
515  C  C   . VAL   B 36  ? 0.4959 0.5322 0.4240 0.1102  0.0500  0.0363  45  VAL   B C   
516  O  O   . VAL   B 36  ? 0.4902 0.5252 0.4142 0.1101  0.0433  0.0367  45  VAL   B O   
517  C  CB  . VAL   B 36  ? 0.5199 0.5651 0.4545 0.0914  0.0558  0.0334  45  VAL   B CB  
518  C  CG1 . VAL   B 36  ? 0.5363 0.5605 0.4561 0.0928  0.0600  0.0342  45  VAL   B CG1 
519  C  CG2 . VAL   B 36  ? 0.5131 0.5749 0.4596 0.0842  0.0613  0.0327  45  VAL   B CG2 
520  N  N   . PHE   B 37  ? 0.4881 0.5117 0.4095 0.1155  0.0547  0.0373  46  PHE   B N   
521  C  CA  . PHE   B 37  ? 0.4870 0.4952 0.3970 0.1193  0.0530  0.0396  46  PHE   B CA  
522  C  C   . PHE   B 37  ? 0.4881 0.4843 0.3876 0.1128  0.0547  0.0392  46  PHE   B C   
523  O  O   . PHE   B 37  ? 0.4847 0.4785 0.3831 0.1095  0.0596  0.0375  46  PHE   B O   
524  C  CB  . PHE   B 37  ? 0.4851 0.4851 0.3927 0.1275  0.0570  0.0408  46  PHE   B CB  
525  C  CG  . PHE   B 37  ? 0.5026 0.4887 0.3994 0.1300  0.0551  0.0441  46  PHE   B CG  
526  C  CD1 . PHE   B 37  ? 0.5100 0.4998 0.4058 0.1346  0.0494  0.0469  46  PHE   B CD1 
527  C  CD2 . PHE   B 37  ? 0.5190 0.4899 0.4064 0.1265  0.0590  0.0445  46  PHE   B CD2 
528  C  CE1 . PHE   B 37  ? 0.5227 0.5003 0.4078 0.1369  0.0489  0.0509  46  PHE   B CE1 
529  C  CE2 . PHE   B 37  ? 0.5342 0.4947 0.4127 0.1269  0.0582  0.0482  46  PHE   B CE2 
530  C  CZ  . PHE   B 37  ? 0.5295 0.4927 0.4066 0.1326  0.0537  0.0519  46  PHE   B CZ  
531  N  N   . HIS   B 38  ? 0.4907 0.4811 0.3816 0.1123  0.0508  0.0409  47  HIS   B N   
532  C  CA  . HIS   B 38  ? 0.4944 0.4771 0.3749 0.1086  0.0519  0.0409  47  HIS   B CA  
533  C  C   . HIS   B 38  ? 0.5227 0.5001 0.3963 0.1113  0.0522  0.0436  47  HIS   B C   
534  O  O   . HIS   B 38  ? 0.5304 0.5073 0.4026 0.1154  0.0493  0.0463  47  HIS   B O   
535  C  CB  . HIS   B 38  ? 0.4842 0.4650 0.3583 0.1067  0.0474  0.0405  47  HIS   B CB  
536  C  CG  . HIS   B 38  ? 0.4793 0.4652 0.3598 0.1012  0.0462  0.0380  47  HIS   B CG  
537  N  ND1 . HIS   B 38  ? 0.4821 0.4808 0.3750 0.1019  0.0434  0.0372  47  HIS   B ND1 
538  C  CD2 . HIS   B 38  ? 0.4982 0.4786 0.3736 0.0946  0.0474  0.0365  47  HIS   B CD2 
539  C  CE1 . HIS   B 38  ? 0.4885 0.4923 0.3859 0.0939  0.0430  0.0349  47  HIS   B CE1 
540  N  NE2 . HIS   B 38  ? 0.5017 0.4922 0.3878 0.0887  0.0458  0.0346  47  HIS   B NE2 
541  N  N   . THR   B 39  ? 0.5293 0.5043 0.3984 0.1084  0.0557  0.0432  48  THR   B N   
542  C  CA  . THR   B 39  ? 0.5365 0.5102 0.4002 0.1083  0.0563  0.0460  48  THR   B CA  
543  C  C   . THR   B 39  ? 0.5329 0.5110 0.3910 0.1051  0.0579  0.0449  48  THR   B C   
544  O  O   . THR   B 39  ? 0.5283 0.5072 0.3838 0.1053  0.0580  0.0431  48  THR   B O   
545  C  CB  . THR   B 39  ? 0.5532 0.5199 0.4189 0.1081  0.0588  0.0471  48  THR   B CB  
546  O  OG1 . THR   B 39  ? 0.5561 0.5218 0.4163 0.1062  0.0594  0.0508  48  THR   B OG1 
547  C  CG2 . THR   B 39  ? 0.5626 0.5245 0.4297 0.1045  0.0629  0.0432  48  THR   B CG2 
548  N  N   . MET   B 40  ? 0.5358 0.5183 0.3912 0.1027  0.0589  0.0468  49  MET   B N   
549  C  CA  . MET   B 40  ? 0.5421 0.5345 0.3935 0.1007  0.0597  0.0459  49  MET   B CA  
550  C  C   . MET   B 40  ? 0.5606 0.5518 0.4143 0.0937  0.0623  0.0420  49  MET   B C   
551  O  O   . MET   B 40  ? 0.5662 0.5485 0.4224 0.0897  0.0640  0.0415  49  MET   B O   
552  C  CB  . MET   B 40  ? 0.5365 0.5400 0.3847 0.1016  0.0592  0.0500  49  MET   B CB  
553  C  CG  . MET   B 40  ? 0.5564 0.5574 0.4001 0.1093  0.0568  0.0535  49  MET   B CG  
554  S  SD  . MET   B 40  ? 0.5671 0.5825 0.4011 0.1172  0.0560  0.0569  49  MET   B SD  
555  C  CE  . MET   B 40  ? 0.4646 0.4775 0.2910 0.1219  0.0552  0.0534  49  MET   B CE  
556  N  N   . TRP   B 41  ? 0.5601 0.5578 0.4105 0.0932  0.0627  0.0391  50  TRP   B N   
557  C  CA  A TRP   B 41  ? 0.5669 0.5640 0.4172 0.0870  0.0645  0.0343  50  TRP   B CA  
558  C  CA  B TRP   B 41  ? 0.5659 0.5627 0.4163 0.0870  0.0645  0.0343  50  TRP   B CA  
559  C  C   . TRP   B 41  ? 0.5724 0.5726 0.4236 0.0780  0.0648  0.0337  50  TRP   B C   
560  O  O   . TRP   B 41  ? 0.5883 0.5765 0.4388 0.0721  0.0666  0.0302  50  TRP   B O   
561  C  CB  A TRP   B 41  ? 0.5649 0.5717 0.4093 0.0894  0.0641  0.0321  50  TRP   B CB  
562  C  CB  B TRP   B 41  ? 0.5627 0.5680 0.4073 0.0892  0.0644  0.0318  50  TRP   B CB  
563  C  CG  A TRP   B 41  ? 0.5737 0.5752 0.4160 0.0861  0.0662  0.0267  50  TRP   B CG  
564  C  CG  B TRP   B 41  ? 0.5679 0.5726 0.4103 0.0833  0.0656  0.0260  50  TRP   B CG  
565  C  CD1 A TRP   B 41  ? 0.5880 0.5804 0.4291 0.0895  0.0689  0.0252  50  TRP   B CD1 
566  C  CD1 B TRP   B 41  ? 0.5748 0.5906 0.4158 0.0759  0.0641  0.0230  50  TRP   B CD1 
567  C  CD2 A TRP   B 41  ? 0.5758 0.5806 0.4160 0.0782  0.0659  0.0217  50  TRP   B CD2 
568  C  CD2 B TRP   B 41  ? 0.5745 0.5679 0.4151 0.0841  0.0685  0.0222  50  TRP   B CD2 
569  N  NE1 A TRP   B 41  ? 0.5942 0.5837 0.4315 0.0862  0.0707  0.0198  50  TRP   B NE1 
570  N  NE1 B TRP   B 41  ? 0.5818 0.5909 0.4185 0.0719  0.0652  0.0167  50  TRP   B NE1 
571  C  CE2 A TRP   B 41  ? 0.5895 0.5852 0.4254 0.0790  0.0684  0.0170  50  TRP   B CE2 
572  C  CE2 B TRP   B 41  ? 0.5842 0.5792 0.4200 0.0779  0.0684  0.0164  50  TRP   B CE2 
573  C  CE3 A TRP   B 41  ? 0.5790 0.5947 0.4201 0.0695  0.0639  0.0205  50  TRP   B CE3 
574  C  CE3 B TRP   B 41  ? 0.5846 0.5686 0.4272 0.0890  0.0713  0.0229  50  TRP   B CE3 
575  C  CZ2 A TRP   B 41  ? 0.5999 0.5938 0.4305 0.0724  0.0683  0.0104  50  TRP   B CZ2 
576  C  CZ2 B TRP   B 41  ? 0.5971 0.5821 0.4281 0.0784  0.0713  0.0114  50  TRP   B CZ2 
577  C  CZ3 A TRP   B 41  ? 0.5910 0.6056 0.4281 0.0607  0.0635  0.0139  50  TRP   B CZ3 
578  C  CZ3 B TRP   B 41  ? 0.5991 0.5767 0.4392 0.0892  0.0749  0.0187  50  TRP   B CZ3 
579  C  CH2 A TRP   B 41  ? 0.5985 0.6013 0.4293 0.0627  0.0654  0.0085  50  TRP   B CH2 
580  C  CH2 B TRP   B 41  ? 0.6007 0.5776 0.4340 0.0849  0.0750  0.0130  50  TRP   B CH2 
581  N  N   . HIS   B 42  ? 0.5604 0.5762 0.4122 0.0765  0.0635  0.0373  51  HIS   B N   
582  C  CA  . HIS   B 42  ? 0.5634 0.5848 0.4169 0.0650  0.0643  0.0372  51  HIS   B CA  
583  C  C   . HIS   B 42  ? 0.5721 0.5723 0.4254 0.0606  0.0669  0.0394  51  HIS   B C   
584  O  O   . HIS   B 42  ? 0.5763 0.5708 0.4279 0.0489  0.0686  0.0380  51  HIS   B O   
585  C  CB  . HIS   B 42  ? 0.5587 0.6067 0.4142 0.0648  0.0631  0.0412  51  HIS   B CB  
586  C  CG  . HIS   B 42  ? 0.5842 0.6319 0.4403 0.0701  0.0640  0.0481  51  HIS   B CG  
587  N  ND1 . HIS   B 42  ? 0.6096 0.6589 0.4622 0.0834  0.0625  0.0510  51  HIS   B ND1 
588  C  CD2 . HIS   B 42  ? 0.5911 0.6348 0.4485 0.0637  0.0665  0.0524  51  HIS   B CD2 
589  C  CE1 . HIS   B 42  ? 0.6076 0.6549 0.4599 0.0855  0.0635  0.0564  51  HIS   B CE1 
590  N  NE2 . HIS   B 42  ? 0.6063 0.6512 0.4617 0.0742  0.0663  0.0580  51  HIS   B NE2 
591  N  N   . VAL   B 43  ? 0.5745 0.5624 0.4281 0.0697  0.0671  0.0426  52  VAL   B N   
592  C  CA  . VAL   B 43  ? 0.5921 0.5599 0.4435 0.0692  0.0694  0.0454  52  VAL   B CA  
593  C  C   . VAL   B 43  ? 0.6098 0.5564 0.4571 0.0666  0.0717  0.0401  52  VAL   B C   
594  O  O   . VAL   B 43  ? 0.6163 0.5469 0.4574 0.0585  0.0744  0.0398  52  VAL   B O   
595  C  CB  . VAL   B 43  ? 0.6012 0.5659 0.4539 0.0811  0.0677  0.0498  52  VAL   B CB  
596  C  CG1 . VAL   B 43  ? 0.6162 0.5607 0.4652 0.0836  0.0697  0.0528  52  VAL   B CG1 
597  C  CG2 . VAL   B 43  ? 0.6015 0.5823 0.4541 0.0847  0.0658  0.0547  52  VAL   B CG2 
598  N  N   . THR   B 44  ? 0.6090 0.5546 0.4582 0.0733  0.0712  0.0361  53  THR   B N   
599  C  CA  . THR   B 44  ? 0.6210 0.5482 0.4656 0.0742  0.0739  0.0313  53  THR   B CA  
600  C  C   . THR   B 44  ? 0.6272 0.5552 0.4673 0.0672  0.0744  0.0241  53  THR   B C   
601  O  O   . THR   B 44  ? 0.6351 0.5443 0.4676 0.0665  0.0770  0.0195  53  THR   B O   
602  C  CB  . THR   B 44  ? 0.6319 0.5591 0.4816 0.0862  0.0740  0.0316  53  THR   B CB  
603  O  OG1 . THR   B 44  ? 0.6336 0.5773 0.4881 0.0877  0.0724  0.0301  53  THR   B OG1 
604  C  CG2 . THR   B 44  ? 0.6339 0.5606 0.4872 0.0937  0.0725  0.0376  53  THR   B CG2 
605  N  N   . LYS   B 45  ? 0.6242 0.5731 0.4669 0.0637  0.0718  0.0230  54  LYS   B N   
606  C  CA  . LYS   B 45  ? 0.6398 0.5950 0.4781 0.0595  0.0711  0.0163  54  LYS   B CA  
607  C  C   . LYS   B 45  ? 0.6492 0.5967 0.4855 0.0681  0.0735  0.0129  54  LYS   B C   
608  O  O   . LYS   B 45  ? 0.6538 0.5994 0.4834 0.0658  0.0742  0.0068  54  LYS   B O   
609  C  CB  . LYS   B 45  ? 0.6801 0.6266 0.5109 0.0460  0.0712  0.0108  54  LYS   B CB  
610  C  CG  . LYS   B 45  ? 0.7532 0.7034 0.5858 0.0351  0.0707  0.0146  54  LYS   B CG  
611  C  CD  . LYS   B 45  ? 0.8137 0.7966 0.6532 0.0315  0.0672  0.0167  54  LYS   B CD  
612  C  CE  . LYS   B 45  ? 0.8766 0.8649 0.7189 0.0201  0.0680  0.0212  54  LYS   B CE  
613  N  NZ  . LYS   B 45  ? 0.9038 0.9231 0.7544 0.0245  0.0662  0.0273  54  LYS   B NZ  
614  N  N   . GLY   B 46  ? 0.6489 0.5944 0.4911 0.0775  0.0749  0.0169  55  GLY   B N   
615  C  CA  . GLY   B 46  ? 0.6532 0.5958 0.4961 0.0850  0.0780  0.0149  55  GLY   B CA  
616  C  C   . GLY   B 46  ? 0.6680 0.5919 0.5069 0.0889  0.0817  0.0122  55  GLY   B C   
617  O  O   . GLY   B 46  ? 0.6755 0.5988 0.5148 0.0958  0.0852  0.0103  55  GLY   B O   
618  N  N   . ALA   B 47  ? 0.6749 0.5825 0.5084 0.0853  0.0817  0.0125  56  ALA   B N   
619  C  CA  . ALA   B 47  ? 0.6926 0.5771 0.5178 0.0910  0.0856  0.0102  56  ALA   B CA  
620  C  C   . ALA   B 47  ? 0.6922 0.5795 0.5255 0.1042  0.0871  0.0150  56  ALA   B C   
621  O  O   . ALA   B 47  ? 0.6795 0.5806 0.5230 0.1056  0.0841  0.0205  56  ALA   B O   
622  C  CB  . ALA   B 47  ? 0.7047 0.5674 0.5190 0.0826  0.0857  0.0100  56  ALA   B CB  
623  N  N   . ALA   B 48  ? 0.7034 0.5788 0.5314 0.1144  0.0914  0.0125  57  ALA   B N   
624  C  CA  . ALA   B 48  ? 0.7061 0.5883 0.5425 0.1282  0.0926  0.0167  57  ALA   B CA  
625  C  C   . ALA   B 48  ? 0.7144 0.5853 0.5484 0.1312  0.0906  0.0224  57  ALA   B C   
626  O  O   . ALA   B 48  ? 0.7278 0.5759 0.5488 0.1248  0.0910  0.0222  57  ALA   B O   
627  C  CB  . ALA   B 48  ? 0.7166 0.5890 0.5457 0.1403  0.0983  0.0128  57  ALA   B CB  
628  N  N   . LEU   B 49  ? 0.7047 0.5923 0.5507 0.1398  0.0883  0.0274  58  LEU   B N   
629  C  CA  . LEU   B 49  ? 0.7128 0.5930 0.5564 0.1447  0.0860  0.0334  58  LEU   B CA  
630  C  C   . LEU   B 49  ? 0.7331 0.6089 0.5744 0.1629  0.0882  0.0355  58  LEU   B C   
631  O  O   . LEU   B 49  ? 0.7261 0.6153 0.5741 0.1715  0.0907  0.0328  58  LEU   B O   
632  C  CB  . LEU   B 49  ? 0.6896 0.5934 0.5467 0.1409  0.0801  0.0375  58  LEU   B CB  
633  C  CG  . LEU   B 49  ? 0.6956 0.6050 0.5536 0.1265  0.0780  0.0364  58  LEU   B CG  
634  C  CD1 . LEU   B 49  ? 0.6878 0.6184 0.5567 0.1253  0.0730  0.0392  58  LEU   B CD1 
635  C  CD2 . LEU   B 49  ? 0.7111 0.6017 0.5572 0.1186  0.0787  0.0382  58  LEU   B CD2 
636  N  N   . ARG   B 50  ? 0.7547 0.6126 0.5856 0.1696  0.0879  0.0405  59  ARG   B N   
637  C  CA  . ARG   B 50  ? 0.7814 0.6346 0.6076 0.1896  0.0896  0.0433  59  ARG   B CA  
638  C  C   . ARG   B 50  ? 0.7843 0.6580 0.6208 0.1963  0.0837  0.0496  59  ARG   B C   
639  O  O   . ARG   B 50  ? 0.7849 0.6533 0.6183 0.1884  0.0806  0.0535  59  ARG   B O   
640  C  CB  . ARG   B 50  ? 0.8327 0.6418 0.6326 0.1946  0.0949  0.0442  59  ARG   B CB  
641  C  CG  . ARG   B 50  ? 0.8961 0.6944 0.6858 0.2176  0.0966  0.0490  59  ARG   B CG  
642  C  CD  . ARG   B 50  ? 0.9928 0.7403 0.7519 0.2223  0.1031  0.0490  59  ARG   B CD  
643  N  NE  . ARG   B 50  ? 1.0597 0.7787 0.8049 0.2050  0.1035  0.0518  59  ARG   B NE  
644  C  CZ  . ARG   B 50  ? 1.1106 0.8107 0.8430 0.2095  0.1037  0.0600  59  ARG   B CZ  
645  N  NH1 . ARG   B 50  ? 1.1091 0.8163 0.8405 0.2318  0.1024  0.0660  59  ARG   B NH1 
646  N  NH2 . ARG   B 50  ? 1.1243 0.8008 0.8450 0.1916  0.1053  0.0625  59  ARG   B NH2 
647  N  N   . SER   B 51  ? 0.7823 0.6824 0.6315 0.2102  0.0818  0.0503  60  SER   B N   
648  C  CA  . SER   B 51  ? 0.7895 0.7120 0.6482 0.2172  0.0750  0.0551  60  SER   B CA  
649  C  C   . SER   B 51  ? 0.8106 0.7340 0.6641 0.2409  0.0763  0.0582  60  SER   B C   
650  O  O   . SER   B 51  ? 0.7960 0.7491 0.6642 0.2504  0.0761  0.0562  60  SER   B O   
651  C  CB  . SER   B 51  ? 0.7797 0.7413 0.6620 0.2086  0.0699  0.0523  60  SER   B CB  
652  O  OG  . SER   B 51  ? 0.7876 0.7705 0.6779 0.2139  0.0623  0.0557  60  SER   B OG  
653  N  N   . GLY   B 52  ? 0.8414 0.7322 0.6730 0.2508  0.0784  0.0634  61  GLY   B N   
654  C  CA  . GLY   B 52  ? 0.8596 0.7437 0.6799 0.2764  0.0805  0.0672  61  GLY   B CA  
655  C  C   . GLY   B 52  ? 0.8784 0.7493 0.6912 0.2853  0.0883  0.0625  61  GLY   B C   
656  O  O   . GLY   B 52  ? 0.8978 0.7374 0.6974 0.2733  0.0936  0.0586  61  GLY   B O   
657  N  N   . GLU   B 53  ? 0.8649 0.7628 0.6868 0.3059  0.0888  0.0624  62  GLU   B N   
658  C  CA  . GLU   B 53  ? 0.8739 0.7649 0.6900 0.3158  0.0966  0.0575  62  GLU   B CA  
659  C  C   . GLU   B 53  ? 0.8469 0.7602 0.6824 0.2955  0.0976  0.0505  62  GLU   B C   
660  O  O   . GLU   B 53  ? 0.8627 0.7550 0.6870 0.2931  0.1043  0.0453  62  GLU   B O   
661  C  CB  . GLU   B 53  ? 0.9074 0.8278 0.7298 0.3447  0.0973  0.0599  62  GLU   B CB  
662  C  CG  . GLU   B 53  ? 0.9974 0.9145 0.8140 0.3578  0.1061  0.0551  62  GLU   B CG  
663  C  CD  . GLU   B 53  ? 1.0959 1.0438 0.9176 0.3890  0.1078  0.0577  62  GLU   B CD  
664  O  OE1 . GLU   B 53  ? 1.1090 1.0696 0.9338 0.3987  0.1146  0.0537  62  GLU   B OE1 
665  O  OE2 . GLU   B 53  ? 1.1190 1.0807 0.9416 0.4048  0.1025  0.0640  62  GLU   B OE2 
666  N  N   . GLY   B 54  ? 0.8052 0.7573 0.6663 0.2813  0.0909  0.0504  63  GLY   B N   
667  C  CA  . GLY   B 54  ? 0.7789 0.7530 0.6578 0.2625  0.0913  0.0454  63  GLY   B CA  
668  C  C   . GLY   B 54  ? 0.7758 0.7199 0.6436 0.2420  0.0929  0.0420  63  GLY   B C   
669  O  O   . GLY   B 54  ? 0.7909 0.7000 0.6400 0.2384  0.0927  0.0438  63  GLY   B O   
670  N  N   . ARG   B 55  ? 0.7524 0.7118 0.6315 0.2283  0.0945  0.0375  64  ARG   B N   
671  C  CA  . ARG   B 55  ? 0.7555 0.6940 0.6261 0.2100  0.0957  0.0338  64  ARG   B CA  
672  C  C   . ARG   B 55  ? 0.7295 0.6958 0.6186 0.1933  0.0924  0.0327  64  ARG   B C   
673  O  O   . ARG   B 55  ? 0.7218 0.7190 0.6275 0.1951  0.0932  0.0324  64  ARG   B O   
674  C  CB  . ARG   B 55  ? 0.7849 0.7024 0.6405 0.2147  0.1035  0.0283  64  ARG   B CB  
675  C  CG  . ARG   B 55  ? 0.8262 0.7296 0.6747 0.1970  0.1046  0.0232  64  ARG   B CG  
676  C  CD  . ARG   B 55  ? 0.8733 0.7712 0.7135 0.2026  0.1117  0.0173  64  ARG   B CD  
677  N  NE  . ARG   B 55  ? 0.9212 0.8050 0.7521 0.1867  0.1119  0.0120  64  ARG   B NE  
678  C  CZ  . ARG   B 55  ? 0.9840 0.8385 0.7936 0.1870  0.1158  0.0058  64  ARG   B CZ  
679  N  NH1 . ARG   B 55  ? 1.0064 0.8380 0.7994 0.2033  0.1207  0.0040  64  ARG   B NH1 
680  N  NH2 . ARG   B 55  ? 0.9878 0.8353 0.7909 0.1718  0.1146  0.0009  64  ARG   B NH2 
681  N  N   . LEU   B 56  ? 0.7118 0.6666 0.5967 0.1775  0.0893  0.0323  65  LEU   B N   
682  C  CA  . LEU   B 56  ? 0.6859 0.6595 0.5826 0.1634  0.0867  0.0315  65  LEU   B CA  
683  C  C   . LEU   B 56  ? 0.6744 0.6351 0.5619 0.1537  0.0905  0.0271  65  LEU   B C   
684  O  O   . LEU   B 56  ? 0.6882 0.6256 0.5618 0.1488  0.0904  0.0257  65  LEU   B O   
685  C  CB  . LEU   B 56  ? 0.6875 0.6616 0.5857 0.1552  0.0797  0.0348  65  LEU   B CB  
686  C  CG  . LEU   B 56  ? 0.7068 0.6844 0.6068 0.1643  0.0748  0.0393  65  LEU   B CG  
687  C  CD1 . LEU   B 56  ? 0.7188 0.6956 0.6178 0.1555  0.0689  0.0418  65  LEU   B CD1 
688  C  CD2 . LEU   B 56  ? 0.7005 0.7081 0.6168 0.1718  0.0729  0.0399  65  LEU   B CD2 
689  N  N   . ASP   B 57  ? 0.6465 0.6235 0.5414 0.1505  0.0938  0.0250  66  ASP   B N   
690  C  CA  . ASP   B 57  ? 0.6449 0.6124 0.5303 0.1427  0.0969  0.0210  66  ASP   B CA  
691  C  C   . ASP   B 57  ? 0.6257 0.6023 0.5154 0.1304  0.0934  0.0225  66  ASP   B C   
692  O  O   . ASP   B 57  ? 0.6224 0.6163 0.5242 0.1281  0.0912  0.0255  66  ASP   B O   
693  C  CB  . ASP   B 57  ? 0.6648 0.6421 0.5518 0.1489  0.1042  0.0184  66  ASP   B CB  
694  C  CG  . ASP   B 57  ? 0.7300 0.6947 0.6081 0.1634  0.1088  0.0161  66  ASP   B CG  
695  O  OD1 . ASP   B 57  ? 0.7439 0.6819 0.6074 0.1649  0.1073  0.0147  66  ASP   B OD1 
696  O  OD2 . ASP   B 57  ? 0.7581 0.7389 0.6425 0.1733  0.1144  0.0160  66  ASP   B OD2 
697  N  N   . PRO   B 58  ? 0.6107 0.5760 0.4896 0.1227  0.0927  0.0202  67  PRO   B N   
698  C  CA  . PRO   B 58  ? 0.5949 0.5676 0.4751 0.1141  0.0898  0.0221  67  PRO   B CA  
699  C  C   . PRO   B 58  ? 0.5763 0.5622 0.4615 0.1125  0.0939  0.0227  67  PRO   B C   
700  O  O   . PRO   B 58  ? 0.5790 0.5690 0.4650 0.1171  0.0998  0.0209  67  PRO   B O   
701  C  CB  . PRO   B 58  ? 0.6090 0.5700 0.4762 0.1087  0.0886  0.0192  67  PRO   B CB  
702  C  CG  . PRO   B 58  ? 0.6228 0.5713 0.4815 0.1124  0.0925  0.0143  67  PRO   B CG  
703  C  CD  . PRO   B 58  ? 0.6089 0.5546 0.4728 0.1215  0.0942  0.0156  67  PRO   B CD  
704  N  N   . TYR   B 59  ? 0.5529 0.5443 0.4404 0.1064  0.0913  0.0256  68  TYR   B N   
705  C  CA  . TYR   B 59  ? 0.5249 0.5253 0.4153 0.1026  0.0957  0.0271  68  TYR   B CA  
706  C  C   . TYR   B 59  ? 0.5358 0.5278 0.4136 0.0975  0.0950  0.0283  68  TYR   B C   
707  O  O   . TYR   B 59  ? 0.5437 0.5350 0.4146 0.0965  0.1003  0.0284  68  TYR   B O   
708  C  CB  . TYR   B 59  ? 0.4924 0.5067 0.3972 0.0999  0.0937  0.0297  68  TYR   B CB  
709  C  CG  . TYR   B 59  ? 0.4728 0.4966 0.3817 0.0926  0.0985  0.0317  68  TYR   B CG  
710  C  CD1 . TYR   B 59  ? 0.4812 0.4947 0.3802 0.0848  0.0977  0.0338  68  TYR   B CD1 
711  C  CD2 . TYR   B 59  ? 0.4547 0.4982 0.3774 0.0934  0.1037  0.0322  68  TYR   B CD2 
712  C  CE1 . TYR   B 59  ? 0.4824 0.5002 0.3827 0.0764  0.1027  0.0362  68  TYR   B CE1 
713  C  CE2 . TYR   B 59  ? 0.4561 0.5096 0.3835 0.0841  0.1086  0.0346  68  TYR   B CE2 
714  C  CZ  . TYR   B 59  ? 0.4751 0.5137 0.3905 0.0747  0.1083  0.0367  68  TYR   B CZ  
715  O  OH  . TYR   B 59  ? 0.4836 0.5280 0.4017 0.0635  0.1135  0.0395  68  TYR   B OH  
716  N  N   . TRP   B 60  ? 0.5309 0.5167 0.4041 0.0960  0.0888  0.0295  69  TRP   B N   
717  C  CA  . TRP   B 60  ? 0.5394 0.5177 0.3991 0.0945  0.0876  0.0309  69  TRP   B CA  
718  C  C   . TRP   B 60  ? 0.5520 0.5274 0.4064 0.0965  0.0823  0.0302  69  TRP   B C   
719  O  O   . TRP   B 60  ? 0.5632 0.5397 0.4243 0.0971  0.0788  0.0303  69  TRP   B O   
720  C  CB  . TRP   B 60  ? 0.5357 0.5104 0.3936 0.0901  0.0867  0.0343  69  TRP   B CB  
721  C  CG  . TRP   B 60  ? 0.5472 0.5109 0.3881 0.0917  0.0851  0.0362  69  TRP   B CG  
722  C  CD1 . TRP   B 60  ? 0.5659 0.5229 0.3926 0.0931  0.0892  0.0375  69  TRP   B CD1 
723  C  CD2 . TRP   B 60  ? 0.5508 0.5105 0.3856 0.0948  0.0791  0.0371  69  TRP   B CD2 
724  N  NE1 . TRP   B 60  ? 0.5765 0.5253 0.3884 0.0977  0.0859  0.0393  69  TRP   B NE1 
725  C  CE2 . TRP   B 60  ? 0.5691 0.5203 0.3862 0.0988  0.0799  0.0390  69  TRP   B CE2 
726  C  CE3 . TRP   B 60  ? 0.5455 0.5084 0.3870 0.0959  0.0737  0.0369  69  TRP   B CE3 
727  C  CZ2 . TRP   B 60  ? 0.5765 0.5242 0.3834 0.1045  0.0756  0.0405  69  TRP   B CZ2 
728  C  CZ3 . TRP   B 60  ? 0.5529 0.5119 0.3843 0.1002  0.0697  0.0385  69  TRP   B CZ3 
729  C  CH2 . TRP   B 60  ? 0.5621 0.5145 0.3770 0.1047  0.0707  0.0401  69  TRP   B CH2 
730  N  N   . GLY   B 61  ? 0.5540 0.5277 0.3963 0.0978  0.0819  0.0300  70  GLY   B N   
731  C  CA  . GLY   B 61  ? 0.5630 0.5397 0.4015 0.0989  0.0773  0.0296  70  GLY   B CA  
732  C  C   . GLY   B 61  ? 0.5792 0.5582 0.4042 0.1021  0.0767  0.0304  70  GLY   B C   
733  O  O   . GLY   B 61  ? 0.5861 0.5624 0.4028 0.1037  0.0803  0.0303  70  GLY   B O   
734  N  N   . ASP   B 62  ? 0.5821 0.5675 0.4039 0.1042  0.0725  0.0317  71  ASP   B N   
735  C  CA  . ASP   B 62  ? 0.5909 0.5829 0.3999 0.1099  0.0712  0.0327  71  ASP   B CA  
736  C  C   . ASP   B 62  ? 0.5843 0.5917 0.3969 0.1095  0.0669  0.0326  71  ASP   B C   
737  O  O   . ASP   B 62  ? 0.5842 0.5915 0.4007 0.1103  0.0650  0.0353  71  ASP   B O   
738  C  CB  . ASP   B 62  ? 0.6228 0.6036 0.4200 0.1162  0.0720  0.0372  71  ASP   B CB  
739  C  CG  . ASP   B 62  ? 0.6921 0.6760 0.4720 0.1257  0.0717  0.0393  71  ASP   B CG  
740  O  OD1 . ASP   B 62  ? 0.6940 0.6944 0.4732 0.1299  0.0680  0.0393  71  ASP   B OD1 
741  O  OD2 . ASP   B 62  ? 0.7449 0.7153 0.5114 0.1293  0.0753  0.0415  71  ASP   B OD2 
742  N  N   . VAL   B 63  ? 0.5739 0.5958 0.3851 0.1075  0.0654  0.0293  72  VAL   B N   
743  C  CA  . VAL   B 63  ? 0.5590 0.5999 0.3752 0.1044  0.0618  0.0290  72  VAL   B CA  
744  C  C   . VAL   B 63  ? 0.5575 0.6098 0.3672 0.1145  0.0599  0.0338  72  VAL   B C   
745  O  O   . VAL   B 63  ? 0.5585 0.6195 0.3741 0.1135  0.0585  0.0363  72  VAL   B O   
746  C  CB  . VAL   B 63  ? 0.5588 0.6136 0.3749 0.0976  0.0601  0.0231  72  VAL   B CB  
747  C  CG1 . VAL   B 63  ? 0.5528 0.6355 0.3719 0.0957  0.0560  0.0234  72  VAL   B CG1 
748  C  CG2 . VAL   B 63  ? 0.5634 0.6050 0.3859 0.0868  0.0617  0.0183  72  VAL   B CG2 
749  N  N   . LYS   B 64  ? 0.5547 0.6040 0.3500 0.1254  0.0605  0.0359  73  LYS   B N   
750  C  CA  . LYS   B 64  ? 0.5576 0.6146 0.3429 0.1381  0.0591  0.0407  73  LYS   B CA  
751  C  C   . LYS   B 64  ? 0.5680 0.6089 0.3530 0.1405  0.0597  0.0441  73  LYS   B C   
752  O  O   . LYS   B 64  ? 0.5680 0.6210 0.3536 0.1454  0.0581  0.0468  73  LYS   B O   
753  C  CB  . LYS   B 64  ? 0.5807 0.6331 0.3465 0.1510  0.0602  0.0426  73  LYS   B CB  
754  C  CG  . LYS   B 64  ? 0.6104 0.6745 0.3640 0.1667  0.0586  0.0471  73  LYS   B CG  
755  C  CD  . LYS   B 64  ? 0.6684 0.7258 0.4002 0.1808  0.0598  0.0495  73  LYS   B CD  
756  C  CE  . LYS   B 64  ? 0.7280 0.7903 0.4433 0.1999  0.0591  0.0545  73  LYS   B CE  
757  N  NZ  . LYS   B 64  ? 0.7692 0.8284 0.4613 0.2159  0.0600  0.0571  73  LYS   B NZ  
758  N  N   . GLN   B 65  ? 0.5717 0.5877 0.3562 0.1365  0.0620  0.0439  74  GLN   B N   
759  C  CA  . GLN   B 65  ? 0.5723 0.5739 0.3570 0.1371  0.0614  0.0459  74  GLN   B CA  
760  C  C   . GLN   B 65  ? 0.5507 0.5609 0.3519 0.1290  0.0598  0.0452  74  GLN   B C   
761  O  O   . GLN   B 65  ? 0.5595 0.5631 0.3607 0.1307  0.0585  0.0470  74  GLN   B O   
762  C  CB  . GLN   B 65  ? 0.6182 0.5953 0.3995 0.1331  0.0636  0.0455  74  GLN   B CB  
763  C  CG  . GLN   B 65  ? 0.6885 0.6503 0.4510 0.1393  0.0665  0.0471  74  GLN   B CG  
764  C  CD  . GLN   B 65  ? 0.7733 0.7122 0.5341 0.1323  0.0689  0.0471  74  GLN   B CD  
765  O  OE1 . GLN   B 65  ? 0.7914 0.7210 0.5539 0.1298  0.0666  0.0471  74  GLN   B OE1 
766  N  NE2 . GLN   B 65  ? 0.7916 0.7226 0.5491 0.1285  0.0734  0.0471  74  GLN   B NE2 
767  N  N   . ASP   B 66  ? 0.5284 0.5503 0.3413 0.1203  0.0601  0.0424  75  ASP   B N   
768  C  CA  . ASP   B 66  ? 0.5079 0.5337 0.3336 0.1119  0.0597  0.0419  75  ASP   B CA  
769  C  C   . ASP   B 66  ? 0.4985 0.5067 0.3288 0.1100  0.0601  0.0422  75  ASP   B C   
770  O  O   . ASP   B 66  ? 0.5062 0.5138 0.3402 0.1099  0.0589  0.0445  75  ASP   B O   
771  C  CB  . ASP   B 66  ? 0.5218 0.5652 0.3488 0.1140  0.0583  0.0453  75  ASP   B CB  
772  C  CG  . ASP   B 66  ? 0.5666 0.6132 0.4044 0.1038  0.0589  0.0455  75  ASP   B CG  
773  O  OD1 . ASP   B 66  ? 0.5930 0.6334 0.4360 0.0949  0.0600  0.0419  75  ASP   B OD1 
774  O  OD2 . ASP   B 66  ? 0.5781 0.6307 0.4169 0.1056  0.0589  0.0495  75  ASP   B OD2 
775  N  N   . LEU   B 67  ? 0.4835 0.4796 0.3136 0.1088  0.0617  0.0402  76  LEU   B N   
776  C  CA  . LEU   B 67  ? 0.4713 0.4563 0.3077 0.1068  0.0617  0.0402  76  LEU   B CA  
777  C  C   . LEU   B 67  ? 0.4676 0.4493 0.3114 0.1022  0.0648  0.0370  76  LEU   B C   
778  O  O   . LEU   B 67  ? 0.4645 0.4485 0.3051 0.1010  0.0671  0.0347  76  LEU   B O   
779  C  CB  . LEU   B 67  ? 0.4740 0.4485 0.3021 0.1104  0.0608  0.0415  76  LEU   B CB  
780  C  CG  . LEU   B 67  ? 0.4957 0.4685 0.3147 0.1166  0.0577  0.0441  76  LEU   B CG  
781  C  CD1 . LEU   B 67  ? 0.5187 0.4756 0.3241 0.1194  0.0573  0.0443  76  LEU   B CD1 
782  C  CD2 . LEU   B 67  ? 0.4903 0.4656 0.3171 0.1159  0.0549  0.0452  76  LEU   B CD2 
783  N  N   . VAL   B 68  ? 0.4599 0.4376 0.3127 0.1009  0.0647  0.0369  77  VAL   B N   
784  C  CA  . VAL   B 68  ? 0.4657 0.4417 0.3257 0.0991  0.0680  0.0343  77  VAL   B CA  
785  C  C   . VAL   B 68  ? 0.4657 0.4422 0.3349 0.1001  0.0668  0.0353  77  VAL   B C   
786  O  O   . VAL   B 68  ? 0.4562 0.4329 0.3271 0.1019  0.0630  0.0373  77  VAL   B O   
787  C  CB  . VAL   B 68  ? 0.4784 0.4528 0.3393 0.0973  0.0696  0.0320  77  VAL   B CB  
788  C  CG1 . VAL   B 68  ? 0.4801 0.4513 0.3441 0.0977  0.0676  0.0342  77  VAL   B CG1 
789  C  CG2 . VAL   B 68  ? 0.4859 0.4569 0.3494 0.0977  0.0740  0.0285  77  VAL   B CG2 
790  N  N   . SER   B 69  ? 0.4676 0.4469 0.3426 0.0991  0.0702  0.0338  78  SER   B N   
791  C  CA  . SER   B 69  ? 0.4525 0.4387 0.3385 0.0995  0.0691  0.0343  78  SER   B CA  
792  C  C   . SER   B 69  ? 0.4487 0.4397 0.3425 0.1031  0.0734  0.0325  78  SER   B C   
793  O  O   . SER   B 69  ? 0.4491 0.4369 0.3386 0.1032  0.0781  0.0305  78  SER   B O   
794  C  CB  . SER   B 69  ? 0.4410 0.4294 0.3273 0.0940  0.0693  0.0347  78  SER   B CB  
795  O  OG  . SER   B 69  ? 0.4389 0.4310 0.3274 0.0913  0.0755  0.0339  78  SER   B OG  
796  N  N   . TYR   B 70  ? 0.4525 0.4511 0.3560 0.1076  0.0717  0.0332  79  TYR   B N   
797  C  CA  . TYR   B 70  ? 0.4600 0.4625 0.3690 0.1146  0.0759  0.0320  79  TYR   B CA  
798  C  C   . TYR   B 70  ? 0.4561 0.4792 0.3797 0.1161  0.0760  0.0325  79  TYR   B C   
799  O  O   . TYR   B 70  ? 0.4545 0.4863 0.3841 0.1141  0.0703  0.0339  79  TYR   B O   
800  C  CB  . TYR   B 70  ? 0.4644 0.4563 0.3690 0.1216  0.0739  0.0331  79  TYR   B CB  
801  C  CG  . TYR   B 70  ? 0.4833 0.4570 0.3749 0.1189  0.0753  0.0319  79  TYR   B CG  
802  C  CD1 . TYR   B 70  ? 0.4960 0.4655 0.3816 0.1128  0.0720  0.0333  79  TYR   B CD1 
803  C  CD2 . TYR   B 70  ? 0.4956 0.4569 0.3804 0.1226  0.0799  0.0292  79  TYR   B CD2 
804  C  CE1 . TYR   B 70  ? 0.5109 0.4693 0.3869 0.1086  0.0731  0.0321  79  TYR   B CE1 
805  C  CE2 . TYR   B 70  ? 0.5129 0.4587 0.3859 0.1172  0.0807  0.0272  79  TYR   B CE2 
806  C  CZ  . TYR   B 70  ? 0.5260 0.4727 0.3961 0.1095  0.0771  0.0287  79  TYR   B CZ  
807  O  OH  . TYR   B 70  ? 0.5435 0.4800 0.4043 0.1028  0.0776  0.0266  79  TYR   B OH  
808  N  N   . CYS   B 71  ? 0.4482 0.4808 0.3774 0.1196  0.0824  0.0312  80  CYS   B N   
809  C  CA  . CYS   B 71  ? 0.4349 0.4934 0.3804 0.1213  0.0841  0.0318  80  CYS   B CA  
810  C  C   . CYS   B 71  ? 0.4097 0.4800 0.3616 0.1081  0.0848  0.0323  80  CYS   B C   
811  O  O   . CYS   B 71  ? 0.4040 0.4988 0.3707 0.1063  0.0866  0.0328  80  CYS   B O   
812  C  CB  . CYS   B 71  ? 0.4642 0.5351 0.4185 0.1291  0.0781  0.0332  80  CYS   B CB  
813  S  SG  . CYS   B 71  ? 0.6088 0.6596 0.5513 0.1446  0.0778  0.0339  80  CYS   B SG  
814  N  N   . GLY   B 72  ? 0.3942 0.4478 0.3345 0.0992  0.0834  0.0325  81  GLY   B N   
815  C  CA  . GLY   B 72  ? 0.3907 0.4478 0.3322 0.0866  0.0842  0.0334  81  GLY   B CA  
816  C  C   . GLY   B 72  ? 0.4154 0.4493 0.3397 0.0812  0.0817  0.0339  81  GLY   B C   
817  O  O   . GLY   B 72  ? 0.4111 0.4309 0.3250 0.0868  0.0791  0.0336  81  GLY   B O   
818  N  N   . PRO   B 73  ? 0.4445 0.4739 0.3643 0.0703  0.0830  0.0350  82  PRO   B N   
819  C  CA  . PRO   B 73  ? 0.4815 0.4869 0.3816 0.0679  0.0812  0.0359  82  PRO   B CA  
820  C  C   . PRO   B 73  ? 0.5149 0.5112 0.4090 0.0696  0.0724  0.0353  82  PRO   B C   
821  O  O   . PRO   B 73  ? 0.5127 0.5208 0.4177 0.0696  0.0670  0.0341  82  PRO   B O   
822  C  CB  . PRO   B 73  ? 0.4903 0.4906 0.3857 0.0559  0.0858  0.0376  82  PRO   B CB  
823  C  CG  . PRO   B 73  ? 0.4714 0.4971 0.3880 0.0485  0.0864  0.0369  82  PRO   B CG  
824  C  CD  . PRO   B 73  ? 0.4315 0.4771 0.3628 0.0598  0.0869  0.0358  82  PRO   B CD  
825  N  N   . TRP   B 74  ? 0.5412 0.5180 0.4169 0.0724  0.0710  0.0361  83  TRP   B N   
826  C  CA  . TRP   B 74  ? 0.5599 0.5278 0.4274 0.0754  0.0637  0.0358  83  TRP   B CA  
827  C  C   . TRP   B 74  ? 0.5788 0.5441 0.4463 0.0664  0.0594  0.0344  83  TRP   B C   
828  O  O   . TRP   B 74  ? 0.5984 0.5553 0.4603 0.0571  0.0629  0.0347  83  TRP   B O   
829  C  CB  . TRP   B 74  ? 0.5730 0.5233 0.4202 0.0808  0.0642  0.0374  83  TRP   B CB  
830  C  CG  . TRP   B 74  ? 0.5885 0.5325 0.4269 0.0867  0.0579  0.0375  83  TRP   B CG  
831  C  CD1 . TRP   B 74  ? 0.6084 0.5367 0.4319 0.0860  0.0542  0.0371  83  TRP   B CD1 
832  C  CD2 . TRP   B 74  ? 0.5861 0.5378 0.4277 0.0943  0.0555  0.0382  83  TRP   B CD2 
833  N  NE1 . TRP   B 74  ? 0.6150 0.5427 0.4323 0.0945  0.0499  0.0377  83  TRP   B NE1 
834  C  CE2 . TRP   B 74  ? 0.6035 0.5466 0.4327 0.0989  0.0509  0.0388  83  TRP   B CE2 
835  C  CE3 . TRP   B 74  ? 0.5853 0.5477 0.4362 0.0974  0.0576  0.0385  83  TRP   B CE3 
836  C  CZ2 . TRP   B 74  ? 0.6140 0.5629 0.4427 0.1059  0.0486  0.0404  83  TRP   B CZ2 
837  C  CZ3 . TRP   B 74  ? 0.5978 0.5632 0.4476 0.1026  0.0551  0.0399  83  TRP   B CZ3 
838  C  CH2 . TRP   B 74  ? 0.6096 0.5701 0.4497 0.1066  0.0509  0.0412  83  TRP   B CH2 
839  N  N   . LYS   B 75  ? 0.5747 0.5472 0.4481 0.0683  0.0521  0.0329  84  LYS   B N   
840  C  CA  . LYS   B 75  ? 0.5805 0.5547 0.4557 0.0593  0.0462  0.0302  84  LYS   B CA  
841  C  C   . LYS   B 75  ? 0.6151 0.5698 0.4714 0.0615  0.0397  0.0288  84  LYS   B C   
842  O  O   . LYS   B 75  ? 0.6243 0.5746 0.4770 0.0524  0.0346  0.0256  84  LYS   B O   
843  C  CB  . LYS   B 75  ? 0.5721 0.5737 0.4688 0.0606  0.0420  0.0289  84  LYS   B CB  
844  C  CG  . LYS   B 75  ? 0.5849 0.6083 0.5005 0.0596  0.0484  0.0298  84  LYS   B CG  
845  C  CD  . LYS   B 75  ? 0.6124 0.6416 0.5334 0.0445  0.0523  0.0291  84  LYS   B CD  
846  C  CE  . LYS   B 75  ? 0.6462 0.6960 0.5832 0.0453  0.0606  0.0308  84  LYS   B CE  
847  N  NZ  . LYS   B 75  ? 0.6636 0.7469 0.6231 0.0483  0.0578  0.0297  84  LYS   B NZ  
848  N  N   . LEU   B 76  ? 0.6332 0.5779 0.4773 0.0731  0.0395  0.0308  85  LEU   B N   
849  C  CA  . LEU   B 76  ? 0.6578 0.5861 0.4831 0.0781  0.0339  0.0297  85  LEU   B CA  
850  C  C   . LEU   B 76  ? 0.6981 0.5986 0.4993 0.0763  0.0362  0.0296  85  LEU   B C   
851  O  O   . LEU   B 76  ? 0.7067 0.5999 0.4994 0.0819  0.0419  0.0326  85  LEU   B O   
852  C  CB  . LEU   B 76  ? 0.6511 0.5844 0.4746 0.0914  0.0332  0.0326  85  LEU   B CB  
853  C  CG  . LEU   B 76  ? 0.6471 0.6017 0.4904 0.0948  0.0335  0.0342  85  LEU   B CG  
854  C  CD1 . LEU   B 76  ? 0.6532 0.6088 0.4919 0.1048  0.0343  0.0375  85  LEU   B CD1 
855  C  CD2 . LEU   B 76  ? 0.6460 0.6131 0.5000 0.0922  0.0271  0.0319  85  LEU   B CD2 
856  N  N   . ASP   B 77  ? 0.7249 0.6082 0.5129 0.0688  0.0316  0.0259  86  ASP   B N   
857  C  CA  . ASP   B 77  ? 0.7659 0.6164 0.5268 0.0668  0.0343  0.0257  86  ASP   B CA  
858  C  C   . ASP   B 77  ? 0.7978 0.6233 0.5319 0.0737  0.0287  0.0230  86  ASP   B C   
859  O  O   . ASP   B 77  ? 0.8269 0.6207 0.5342 0.0751  0.0313  0.0231  86  ASP   B O   
860  C  CB  . ASP   B 77  ? 0.7949 0.6370 0.5575 0.0482  0.0370  0.0240  86  ASP   B CB  
861  C  CG  . ASP   B 77  ? 0.8610 0.7178 0.6391 0.0328  0.0305  0.0190  86  ASP   B CG  
862  O  OD1 . ASP   B 77  ? 0.8566 0.7358 0.6493 0.0376  0.0239  0.0171  86  ASP   B OD1 
863  O  OD2 . ASP   B 77  ? 0.9104 0.7577 0.6862 0.0156  0.0322  0.0171  86  ASP   B OD2 
864  N  N   . ALA   B 78  ? 0.7910 0.6281 0.5293 0.0796  0.0218  0.0210  87  ALA   B N   
865  C  CA  . ALA   B 78  ? 0.8162 0.6298 0.5271 0.0881  0.0168  0.0182  87  ALA   B CA  
866  C  C   . ALA   B 78  ? 0.8270 0.6318 0.5206 0.1065  0.0217  0.0229  87  ALA   B C   
867  O  O   . ALA   B 78  ? 0.8195 0.6459 0.5283 0.1132  0.0262  0.0277  87  ALA   B O   
868  C  CB  . ALA   B 78  ? 0.8093 0.6398 0.5287 0.0907  0.0086  0.0154  87  ALA   B CB  
869  N  N   . ALA   B 79  ? 0.8404 0.6144 0.5017 0.1149  0.0207  0.0212  88  ALA   B N   
870  C  CA  . ALA   B 79  ? 0.8475 0.6161 0.4913 0.1345  0.0252  0.0257  88  ALA   B CA  
871  C  C   . ALA   B 79  ? 0.8599 0.6170 0.4812 0.1484  0.0209  0.0237  88  ALA   B C   
872  O  O   . ALA   B 79  ? 0.8730 0.6098 0.4801 0.1422  0.0148  0.0175  88  ALA   B O   
873  C  CB  . ALA   B 79  ? 0.8667 0.6058 0.4875 0.1363  0.0310  0.0273  88  ALA   B CB  
874  N  N   . TRP   B 80  ? 0.8526 0.6238 0.4701 0.1669  0.0241  0.0285  89  TRP   B N   
875  C  CA  . TRP   B 80  ? 0.8674 0.6303 0.4623 0.1830  0.0216  0.0276  89  TRP   B CA  
876  C  C   . TRP   B 80  ? 0.9002 0.6181 0.4548 0.1904  0.0220  0.0242  89  TRP   B C   
877  O  O   . TRP   B 80  ? 0.9133 0.6171 0.4570 0.1938  0.0274  0.0269  89  TRP   B O   
878  C  CB  . TRP   B 80  ? 0.8512 0.6437 0.4532 0.1999  0.0265  0.0345  89  TRP   B CB  
879  C  CG  . TRP   B 80  ? 0.8602 0.6481 0.4389 0.2188  0.0258  0.0349  89  TRP   B CG  
880  C  CD1 . TRP   B 80  ? 0.8714 0.6546 0.4424 0.2200  0.0202  0.0313  89  TRP   B CD1 
881  C  CD2 . TRP   B 80  ? 0.8622 0.6559 0.4244 0.2405  0.0312  0.0396  89  TRP   B CD2 
882  N  NE1 . TRP   B 80  ? 0.8813 0.6640 0.4303 0.2411  0.0224  0.0334  89  TRP   B NE1 
883  C  CE2 . TRP   B 80  ? 0.8755 0.6660 0.4195 0.2542  0.0292  0.0387  89  TRP   B CE2 
884  C  CE3 . TRP   B 80  ? 0.8626 0.6660 0.4230 0.2508  0.0372  0.0445  89  TRP   B CE3 
885  C  CZ2 . TRP   B 80  ? 0.8824 0.6794 0.4069 0.2780  0.0339  0.0427  89  TRP   B CZ2 
886  C  CZ3 . TRP   B 80  ? 0.8725 0.6838 0.4143 0.2743  0.0411  0.0484  89  TRP   B CZ3 
887  C  CH2 . TRP   B 80  ? 0.8781 0.6867 0.4027 0.2878  0.0398  0.0476  89  TRP   B CH2 
888  N  N   . ASP   B 81  ? 0.9139 0.6068 0.4443 0.1926  0.0163  0.0182  90  ASP   B N   
889  C  CA  . ASP   B 81  ? 0.9584 0.6012 0.4457 0.1990  0.0164  0.0140  90  ASP   B CA  
890  C  C   . ASP   B 81  ? 0.9787 0.6120 0.4369 0.2278  0.0220  0.0184  90  ASP   B C   
891  O  O   . ASP   B 81  ? 1.0022 0.5910 0.4208 0.2371  0.0234  0.0159  90  ASP   B O   
892  C  CB  . ASP   B 81  ? 0.9963 0.6123 0.4649 0.1899  0.0075  0.0044  90  ASP   B CB  
893  C  CG  . ASP   B 81  ? 1.0522 0.6866 0.5203 0.2020  0.0027  0.0032  90  ASP   B CG  
894  O  OD1 . ASP   B 81  ? 1.0446 0.7102 0.5242 0.2184  0.0074  0.0103  90  ASP   B OD1 
895  O  OD2 . ASP   B 81  ? 1.0954 0.7134 0.5509 0.1944  -0.0056 -0.0050 90  ASP   B OD2 
896  N  N   . GLY   B 82  ? 0.9635 0.6385 0.4406 0.2416  0.0253  0.0249  91  GLY   B N   
897  C  CA  . GLY   B 82  ? 0.9792 0.6571 0.4347 0.2693  0.0307  0.0297  91  GLY   B CA  
898  C  C   . GLY   B 82  ? 1.0010 0.6688 0.4311 0.2857  0.0280  0.0267  91  GLY   B C   
899  O  O   . GLY   B 82  ? 1.0070 0.6819 0.4197 0.3106  0.0327  0.0308  91  GLY   B O   
900  N  N   . LEU   B 83  ? 1.0102 0.6636 0.4374 0.2731  0.0204  0.0195  92  LEU   B N   
901  C  CA  . LEU   B 83  ? 1.0310 0.6717 0.4311 0.2881  0.0172  0.0156  92  LEU   B CA  
902  C  C   . LEU   B 83  ? 1.0197 0.6925 0.4436 0.2815  0.0124  0.0155  92  LEU   B C   
903  O  O   . LEU   B 83  ? 1.0249 0.7118 0.4394 0.2995  0.0140  0.0180  92  LEU   B O   
904  C  CB  . LEU   B 83  ? 1.0678 0.6499 0.4284 0.2824  0.0111  0.0051  92  LEU   B CB  
905  C  CG  . LEU   B 83  ? 1.1161 0.6485 0.4308 0.2981  0.0152  0.0034  92  LEU   B CG  
906  C  CD1 . LEU   B 83  ? 1.1525 0.6295 0.4280 0.2911  0.0079  -0.0082 92  LEU   B CD1 
907  C  CD2 . LEU   B 83  ? 1.1230 0.6673 0.4187 0.3319  0.0221  0.0096  92  LEU   B CD2 
908  N  N   . SER   B 84  ? 1.0054 0.6859 0.4552 0.2571  0.0063  0.0120  93  SER   B N   
909  C  CA  . SER   B 84  ? 0.9910 0.6952 0.4578 0.2513  0.0005  0.0109  93  SER   B CA  
910  C  C   . SER   B 84  ? 0.9539 0.7066 0.4539 0.2550  0.0057  0.0206  93  SER   B C   
911  O  O   . SER   B 84  ? 0.9373 0.7111 0.4584 0.2537  0.0123  0.0271  93  SER   B O   
912  C  CB  . SER   B 84  ? 1.0074 0.7053 0.4895 0.2257  -0.0082 0.0038  93  SER   B CB  
913  O  OG  . SER   B 84  ? 1.0616 0.7143 0.5154 0.2170  -0.0125 -0.0051 93  SER   B OG  
914  N  N   . GLU   B 85  ? 0.9406 0.7094 0.4436 0.2590  0.0025  0.0213  94  GLU   B N   
915  C  CA  . GLU   B 85  ? 0.9144 0.7247 0.4476 0.2589  0.0069  0.0302  94  GLU   B CA  
916  C  C   . GLU   B 85  ? 0.8912 0.7149 0.4584 0.2367  0.0037  0.0299  94  GLU   B C   
917  O  O   . GLU   B 85  ? 0.9000 0.7067 0.4669 0.2228  -0.0038 0.0223  94  GLU   B O   
918  C  CB  . GLU   B 85  ? 0.9334 0.7522 0.4565 0.2690  0.0042  0.0312  94  GLU   B CB  
919  C  CG  . GLU   B 85  ? 0.9932 0.8106 0.4886 0.2932  0.0100  0.0343  94  GLU   B CG  
920  C  CD  . GLU   B 85  ? 1.0302 0.8737 0.5282 0.3034  0.0132  0.0413  94  GLU   B CD  
921  O  OE1 . GLU   B 85  ? 1.0157 0.8727 0.5325 0.2925  0.0095  0.0429  94  GLU   B OE1 
922  O  OE2 . GLU   B 85  ? 1.0594 0.9104 0.5398 0.3233  0.0199  0.0459  94  GLU   B OE2 
923  N  N   . VAL   B 86  ? 0.8562 0.7103 0.4518 0.2334  0.0099  0.0378  95  VAL   B N   
924  C  CA  . VAL   B 86  ? 0.8306 0.6987 0.4573 0.2157  0.0085  0.0384  95  VAL   B CA  
925  C  C   . VAL   B 86  ? 0.8079 0.7014 0.4517 0.2161  0.0095  0.0447  95  VAL   B C   
926  O  O   . VAL   B 86  ? 0.8056 0.7051 0.4368 0.2288  0.0113  0.0484  95  VAL   B O   
927  C  CB  . VAL   B 86  ? 0.8219 0.6976 0.4640 0.2103  0.0152  0.0416  95  VAL   B CB  
928  C  CG1 . VAL   B 86  ? 0.8432 0.6910 0.4629 0.2134  0.0154  0.0371  95  VAL   B CG1 
929  C  CG2 . VAL   B 86  ? 0.8130 0.7160 0.4652 0.2187  0.0234  0.0504  95  VAL   B CG2 
930  N  N   . GLN   B 87  ? 0.7850 0.6917 0.4553 0.2032  0.0087  0.0460  96  GLN   B N   
931  C  CA  . GLN   B 87  ? 0.7658 0.6915 0.4500 0.2038  0.0105  0.0526  96  GLN   B CA  
932  C  C   . GLN   B 87  ? 0.7388 0.6796 0.4496 0.1938  0.0163  0.0572  96  GLN   B C   
933  O  O   . GLN   B 87  ? 0.7308 0.6688 0.4548 0.1831  0.0142  0.0533  96  GLN   B O   
934  C  CB  . GLN   B 87  ? 0.7864 0.7093 0.4698 0.2015  0.0014  0.0486  96  GLN   B CB  
935  C  CG  . GLN   B 87  ? 0.8337 0.7473 0.4904 0.2140  -0.0033 0.0465  96  GLN   B CG  
936  C  CD  . GLN   B 87  ? 0.8764 0.7949 0.5335 0.2146  -0.0112 0.0453  96  GLN   B CD  
937  O  OE1 . GLN   B 87  ? 0.8667 0.7960 0.5443 0.2065  -0.0136 0.0460  96  GLN   B OE1 
938  N  NE2 . GLN   B 87  ? 0.9114 0.8227 0.5442 0.2261  -0.0154 0.0436  96  GLN   B NE2 
939  N  N   . LEU   B 88  ? 0.7199 0.6764 0.4374 0.1966  0.0238  0.0654  97  LEU   B N   
940  C  CA  . LEU   B 88  ? 0.7004 0.6685 0.4400 0.1866  0.0291  0.0693  97  LEU   B CA  
941  C  C   . LEU   B 88  ? 0.6880 0.6573 0.4358 0.1842  0.0270  0.0719  97  LEU   B C   
942  O  O   . LEU   B 88  ? 0.6959 0.6672 0.4344 0.1917  0.0274  0.0766  97  LEU   B O   
943  C  CB  . LEU   B 88  ? 0.6935 0.6781 0.4357 0.1887  0.0380  0.0766  97  LEU   B CB  
944  C  CG  . LEU   B 88  ? 0.6932 0.6880 0.4552 0.1772  0.0435  0.0808  97  LEU   B CG  
945  C  CD1 . LEU   B 88  ? 0.6986 0.6889 0.4734 0.1677  0.0420  0.0752  97  LEU   B CD1 
946  C  CD2 . LEU   B 88  ? 0.6879 0.7015 0.4524 0.1769  0.0513  0.0869  97  LEU   B CD2 
947  N  N   . LEU   B 89  ? 0.6682 0.6362 0.4315 0.1755  0.0250  0.0691  98  LEU   B N   
948  C  CA  . LEU   B 89  ? 0.6611 0.6304 0.4315 0.1755  0.0233  0.0719  98  LEU   B CA  
949  C  C   . LEU   B 89  ? 0.6465 0.6197 0.4276 0.1700  0.0319  0.0782  98  LEU   B C   
950  O  O   . LEU   B 89  ? 0.6361 0.6086 0.4307 0.1626  0.0334  0.0764  98  LEU   B O   
951  C  CB  . LEU   B 89  ? 0.6622 0.6302 0.4429 0.1704  0.0165  0.0650  98  LEU   B CB  
952  C  CG  . LEU   B 89  ? 0.6734 0.6453 0.4630 0.1722  0.0142  0.0670  98  LEU   B CG  
953  C  CD1 . LEU   B 89  ? 0.6815 0.6529 0.4585 0.1828  0.0127  0.0726  98  LEU   B CD1 
954  C  CD2 . LEU   B 89  ? 0.6789 0.6558 0.4775 0.1682  0.0064  0.0596  98  LEU   B CD2 
955  N  N   . ALA   B 90  ? 0.6359 0.6131 0.4097 0.1731  0.0380  0.0855  99  ALA   B N   
956  C  CA  . ALA   B 90  ? 0.6260 0.6063 0.4078 0.1653  0.0464  0.0914  99  ALA   B CA  
957  C  C   . ALA   B 90  ? 0.6267 0.5971 0.4113 0.1640  0.0482  0.0956  99  ALA   B C   
958  O  O   . ALA   B 90  ? 0.6338 0.5993 0.4087 0.1725  0.0462  0.0996  99  ALA   B O   
959  C  CB  . ALA   B 90  ? 0.6196 0.6105 0.3937 0.1673  0.0529  0.0980  99  ALA   B CB  
960  N  N   . VAL   B 91  ? 0.6208 0.5867 0.4162 0.1547  0.0518  0.0948  100 VAL   B N   
961  C  CA  . VAL   B 91  ? 0.6300 0.5820 0.4252 0.1541  0.0547  0.0988  100 VAL   B CA  
962  C  C   . VAL   B 91  ? 0.6416 0.5898 0.4369 0.1430  0.0638  0.1041  100 VAL   B C   
963  O  O   . VAL   B 91  ? 0.6450 0.5920 0.4490 0.1330  0.0662  0.1002  100 VAL   B O   
964  C  CB  . VAL   B 91  ? 0.6274 0.5745 0.4330 0.1534  0.0511  0.0924  100 VAL   B CB  
965  C  CG1 . VAL   B 91  ? 0.6341 0.5647 0.4359 0.1568  0.0541  0.0968  100 VAL   B CG1 
966  C  CG2 . VAL   B 91  ? 0.6272 0.5828 0.4356 0.1602  0.0421  0.0863  100 VAL   B CG2 
967  N  N   . PRO   B 92  ? 0.6472 0.5950 0.4324 0.1433  0.0693  0.1127  101 PRO   B N   
968  C  CA  . PRO   B 92  ? 0.6511 0.5976 0.4372 0.1293  0.0782  0.1176  101 PRO   B CA  
969  C  C   . PRO   B 92  ? 0.6683 0.5884 0.4492 0.1240  0.0829  0.1209  101 PRO   B C   
970  O  O   . PRO   B 92  ? 0.6786 0.5822 0.4503 0.1349  0.0812  0.1239  101 PRO   B O   
971  C  CB  . PRO   B 92  ? 0.6507 0.6092 0.4279 0.1320  0.0828  0.1260  101 PRO   B CB  
972  C  CG  . PRO   B 92  ? 0.6607 0.6228 0.4297 0.1492  0.0755  0.1246  101 PRO   B CG  
973  C  CD  . PRO   B 92  ? 0.6437 0.5934 0.4157 0.1553  0.0678  0.1182  101 PRO   B CD  
974  N  N   . PRO   B 93  ? 0.6686 0.5833 0.4533 0.1077  0.0887  0.1204  102 PRO   B N   
975  C  CA  . PRO   B 93  ? 0.6868 0.5700 0.4620 0.1026  0.0939  0.1234  102 PRO   B CA  
976  C  C   . PRO   B 93  ? 0.7133 0.5776 0.4704 0.1096  0.0987  0.1346  102 PRO   B C   
977  O  O   . PRO   B 93  ? 0.7080 0.5839 0.4606 0.1079  0.1027  0.1419  102 PRO   B O   
978  C  CB  . PRO   B 93  ? 0.6879 0.5728 0.4679 0.0812  0.0996  0.1219  102 PRO   B CB  
979  C  CG  . PRO   B 93  ? 0.6725 0.5901 0.4688 0.0789  0.0947  0.1144  102 PRO   B CG  
980  C  CD  . PRO   B 93  ? 0.6457 0.5821 0.4418 0.0938  0.0906  0.1168  102 PRO   B CD  
981  N  N   . GLY   B 94  ? 0.7332 0.5708 0.4796 0.1203  0.0979  0.1359  103 GLY   B N   
982  C  CA  . GLY   B 94  ? 0.7540 0.5689 0.4801 0.1302  0.1020  0.1465  103 GLY   B CA  
983  C  C   . GLY   B 94  ? 0.7570 0.5883 0.4785 0.1464  0.0975  0.1510  103 GLY   B C   
984  O  O   . GLY   B 94  ? 0.7756 0.5911 0.4789 0.1546  0.1014  0.1609  103 GLY   B O   
985  N  N   . GLU   B 95  ? 0.7451 0.6057 0.4804 0.1510  0.0894  0.1437  104 GLU   B N   
986  C  CA  . GLU   B 95  ? 0.7447 0.6207 0.4741 0.1650  0.0843  0.1462  104 GLU   B CA  
987  C  C   . GLU   B 95  ? 0.7497 0.6384 0.4871 0.1775  0.0725  0.1372  104 GLU   B C   
988  O  O   . GLU   B 95  ? 0.7461 0.6415 0.4985 0.1726  0.0684  0.1281  104 GLU   B O   
989  C  CB  . GLU   B 95  ? 0.7396 0.6392 0.4731 0.1576  0.0873  0.1475  104 GLU   B CB  
990  C  CG  . GLU   B 95  ? 0.7631 0.6557 0.4856 0.1484  0.0990  0.1591  104 GLU   B CG  
991  C  CD  . GLU   B 95  ? 0.7877 0.7074 0.5191 0.1371  0.1037  0.1599  104 GLU   B CD  
992  O  OE1 . GLU   B 95  ? 0.7893 0.7321 0.5311 0.1409  0.0975  0.1522  104 GLU   B OE1 
993  O  OE2 . GLU   B 95  ? 0.7843 0.7019 0.5115 0.1243  0.1140  0.1684  104 GLU   B OE2 
994  N  N   . ARG   B 96  ? 0.7521 0.6452 0.4788 0.1927  0.0670  0.1397  105 ARG   B N   
995  C  CA  . ARG   B 96  ? 0.7541 0.6604 0.4864 0.2036  0.0551  0.1315  105 ARG   B CA  
996  C  C   . ARG   B 96  ? 0.7356 0.6621 0.4796 0.1977  0.0499  0.1224  105 ARG   B C   
997  O  O   . ARG   B 96  ? 0.7274 0.6612 0.4687 0.1927  0.0541  0.1244  105 ARG   B O   
998  C  CB  . ARG   B 96  ? 0.7941 0.6997 0.5088 0.2204  0.0507  0.1369  105 ARG   B CB  
999  C  CG  . ARG   B 96  ? 0.8584 0.7748 0.5773 0.2323  0.0382  0.1297  105 ARG   B CG  
1000 C  CD  . ARG   B 96  ? 0.9317 0.8422 0.6323 0.2502  0.0351  0.1368  105 ARG   B CD  
1001 N  NE  . ARG   B 96  ? 1.0064 0.9176 0.6888 0.2558  0.0368  0.1429  105 ARG   B NE  
1002 C  CZ  . ARG   B 96  ? 1.0769 0.9713 0.7413 0.2587  0.0468  0.1554  105 ARG   B CZ  
1003 N  NH1 . ARG   B 96  ? 1.0861 0.9581 0.7469 0.2555  0.0559  0.1628  105 ARG   B NH1 
1004 N  NH2 . ARG   B 96  ? 1.0941 0.9922 0.7420 0.2647  0.0483  0.1606  105 ARG   B NH2 
1005 N  N   . ALA   B 97  ? 0.7301 0.6654 0.4863 0.1985  0.0413  0.1127  106 ALA   B N   
1006 C  CA  . ALA   B 97  ? 0.7310 0.6801 0.4954 0.1935  0.0359  0.1037  106 ALA   B CA  
1007 C  C   . ALA   B 97  ? 0.7411 0.6964 0.4911 0.2013  0.0320  0.1041  106 ALA   B C   
1008 O  O   . ALA   B 97  ? 0.7496 0.7037 0.4878 0.2126  0.0275  0.1067  106 ALA   B O   
1009 C  CB  . ALA   B 97  ? 0.7247 0.6806 0.5015 0.1937  0.0276  0.0949  106 ALA   B CB  
1010 N  N   . LYS   B 98  ? 0.7387 0.7001 0.4875 0.1969  0.0342  0.1021  107 LYS   B N   
1011 C  CA  . LYS   B 98  ? 0.7488 0.7141 0.4810 0.2058  0.0320  0.1027  107 LYS   B CA  
1012 C  C   . LYS   B 98  ? 0.7391 0.7086 0.4707 0.2041  0.0277  0.0939  107 LYS   B C   
1013 O  O   . LYS   B 98  ? 0.7354 0.7084 0.4766 0.1959  0.0321  0.0923  107 LYS   B O   
1014 C  CB  . LYS   B 98  ? 0.7888 0.7557 0.5130 0.2060  0.0429  0.1133  107 LYS   B CB  
1015 C  CG  . LYS   B 98  ? 0.8735 0.8455 0.5787 0.2170  0.0431  0.1160  107 LYS   B CG  
1016 C  CD  . LYS   B 98  ? 0.9491 0.9269 0.6492 0.2155  0.0556  0.1277  107 LYS   B CD  
1017 C  CE  . LYS   B 98  ? 0.9923 0.9798 0.7086 0.2012  0.0635  0.1287  107 LYS   B CE  
1018 N  NZ  . LYS   B 98  ? 1.0179 1.0237 0.7293 0.2035  0.0704  0.1329  107 LYS   B NZ  
1019 N  N   . ASN   B 99  ? 0.7314 0.6987 0.4494 0.2120  0.0191  0.0882  108 ASN   B N   
1020 C  CA  . ASN   B 99  ? 0.7210 0.6855 0.4333 0.2111  0.0151  0.0798  108 ASN   B CA  
1021 C  C   . ASN   B 99  ? 0.7215 0.6876 0.4169 0.2196  0.0203  0.0831  108 ASN   B C   
1022 O  O   . ASN   B 99  ? 0.7322 0.6977 0.4105 0.2303  0.0196  0.0863  108 ASN   B O   
1023 C  CB  . ASN   B 99  ? 0.7250 0.6835 0.4292 0.2133  0.0029  0.0706  108 ASN   B CB  
1024 C  CG  . ASN   B 99  ? 0.7468 0.7081 0.4694 0.2037  -0.0027 0.0651  108 ASN   B CG  
1025 O  OD1 . ASN   B 99  ? 0.7633 0.7307 0.4974 0.2037  -0.0023 0.0691  108 ASN   B OD1 
1026 N  ND2 . ASN   B 99  ? 0.7429 0.6991 0.4670 0.1962  -0.0078 0.0562  108 ASN   B ND2 
1027 N  N   . ILE   B 100 ? 0.7125 0.6820 0.4116 0.2163  0.0255  0.0824  109 ILE   B N   
1028 C  CA  . ILE   B 100 ? 0.7146 0.6898 0.3989 0.2260  0.0310  0.0856  109 ILE   B CA  
1029 C  C   . ILE   B 100 ? 0.7211 0.6852 0.3932 0.2298  0.0267  0.0770  109 ILE   B C   
1030 O  O   . ILE   B 100 ? 0.7246 0.6875 0.4070 0.2224  0.0275  0.0736  109 ILE   B O   
1031 C  CB  . ILE   B 100 ? 0.7095 0.7026 0.4071 0.2209  0.0421  0.0938  109 ILE   B CB  
1032 C  CG1 . ILE   B 100 ? 0.7213 0.7188 0.4298 0.2140  0.0470  0.1022  109 ILE   B CG1 
1033 C  CG2 . ILE   B 100 ? 0.7128 0.7180 0.3962 0.2326  0.0481  0.0979  109 ILE   B CG2 
1034 C  CD1 . ILE   B 100 ? 0.7466 0.7423 0.4398 0.2238  0.0478  0.1084  109 ILE   B CD1 
1035 N  N   . GLN   B 101 ? 0.7331 0.6867 0.3809 0.2419  0.0225  0.0735  110 GLN   B N   
1036 C  CA  . GLN   B 101 ? 0.7484 0.6843 0.3775 0.2472  0.0183  0.0651  110 GLN   B CA  
1037 C  C   . GLN   B 101 ? 0.7506 0.6951 0.3710 0.2579  0.0269  0.0692  110 GLN   B C   
1038 O  O   . GLN   B 101 ? 0.7472 0.7084 0.3632 0.2675  0.0337  0.0770  110 GLN   B O   
1039 C  CB  . GLN   B 101 ? 0.7792 0.6981 0.3824 0.2561  0.0097  0.0590  110 GLN   B CB  
1040 C  CG  . GLN   B 101 ? 0.8408 0.7336 0.4210 0.2595  0.0044  0.0489  110 GLN   B CG  
1041 C  CD  . GLN   B 101 ? 0.9079 0.7812 0.4693 0.2593  -0.0073 0.0395  110 GLN   B CD  
1042 O  OE1 . GLN   B 101 ? 0.9287 0.8096 0.5010 0.2526  -0.0136 0.0388  110 GLN   B OE1 
1043 N  NE2 . GLN   B 101 ? 0.9317 0.7787 0.4628 0.2669  -0.0108 0.0316  110 GLN   B NE2 
1044 N  N   . THR   B 102 ? 0.7506 0.6857 0.3688 0.2568  0.0271  0.0647  111 THR   B N   
1045 C  CA  . THR   B 102 ? 0.7579 0.7033 0.3678 0.2690  0.0346  0.0684  111 THR   B CA  
1046 C  C   . THR   B 102 ? 0.7736 0.6926 0.3642 0.2739  0.0316  0.0607  111 THR   B C   
1047 O  O   . THR   B 102 ? 0.7778 0.6741 0.3682 0.2627  0.0248  0.0534  111 THR   B O   
1048 C  CB  . THR   B 102 ? 0.7670 0.7420 0.4059 0.2595  0.0422  0.0758  111 THR   B CB  
1049 O  OG1 . THR   B 102 ? 0.7856 0.7817 0.4193 0.2723  0.0500  0.0811  111 THR   B OG1 
1050 C  CG2 . THR   B 102 ? 0.7685 0.7367 0.4245 0.2446  0.0398  0.0715  111 THR   B CG2 
1051 N  N   . LEU   B 103 ? 0.7811 0.7027 0.3540 0.2912  0.0370  0.0627  112 LEU   B N   
1052 C  CA  . LEU   B 103 ? 0.8040 0.6982 0.3561 0.2974  0.0354  0.0569  112 LEU   B CA  
1053 C  C   . LEU   B 103 ? 0.8100 0.7282 0.3808 0.2961  0.0418  0.0622  112 LEU   B C   
1054 O  O   . LEU   B 103 ? 0.7981 0.7479 0.3742 0.3068  0.0488  0.0693  112 LEU   B O   
1055 C  CB  . LEU   B 103 ? 0.8179 0.6923 0.3310 0.3212  0.0364  0.0545  112 LEU   B CB  
1056 C  CG  . LEU   B 103 ? 0.8490 0.6915 0.3391 0.3279  0.0361  0.0495  112 LEU   B CG  
1057 C  CD1 . LEU   B 103 ? 0.8737 0.6716 0.3481 0.3152  0.0273  0.0394  112 LEU   B CD1 
1058 C  CD2 . LEU   B 103 ? 0.8624 0.7015 0.3215 0.3560  0.0416  0.0516  112 LEU   B CD2 
1059 N  N   . PRO   B 104 ? 0.8241 0.7291 0.4040 0.2833  0.0396  0.0586  113 PRO   B N   
1060 C  CA  . PRO   B 104 ? 0.8221 0.7505 0.4197 0.2813  0.0449  0.0631  113 PRO   B CA  
1061 C  C   . PRO   B 104 ? 0.8480 0.7807 0.4257 0.3028  0.0498  0.0656  113 PRO   B C   
1062 O  O   . PRO   B 104 ? 0.8784 0.7825 0.4224 0.3197  0.0490  0.0624  113 PRO   B O   
1063 C  CB  . PRO   B 104 ? 0.8302 0.7383 0.4375 0.2636  0.0410  0.0581  113 PRO   B CB  
1064 C  CG  . PRO   B 104 ? 0.8371 0.7247 0.4437 0.2521  0.0341  0.0526  113 PRO   B CG  
1065 C  CD  . PRO   B 104 ? 0.8265 0.6994 0.4043 0.2680  0.0323  0.0508  113 PRO   B CD  
1066 N  N   . GLY   B 105 ? 0.8319 0.8013 0.4303 0.3023  0.0547  0.0713  114 GLY   B N   
1067 C  CA  . GLY   B 105 ? 0.8398 0.8239 0.4272 0.3208  0.0592  0.0745  114 GLY   B CA  
1068 C  C   . GLY   B 105 ? 0.8549 0.8237 0.4431 0.3145  0.0578  0.0719  114 GLY   B C   
1069 O  O   . GLY   B 105 ? 0.8683 0.8092 0.4601 0.2979  0.0537  0.0670  114 GLY   B O   
1070 N  N   . ILE   B 106 ? 0.8493 0.8378 0.4338 0.3286  0.0614  0.0754  115 ILE   B N   
1071 C  CA  . ILE   B 106 ? 0.8606 0.8344 0.4414 0.3261  0.0608  0.0738  115 ILE   B CA  
1072 C  C   . ILE   B 106 ? 0.8367 0.8578 0.4436 0.3226  0.0631  0.0780  115 ILE   B C   
1073 O  O   . ILE   B 106 ? 0.8252 0.8889 0.4408 0.3328  0.0664  0.0828  115 ILE   B O   
1074 C  CB  . ILE   B 106 ? 0.8994 0.8393 0.4382 0.3516  0.0621  0.0731  115 ILE   B CB  
1075 C  CG1 . ILE   B 106 ? 0.9429 0.8301 0.4515 0.3535  0.0591  0.0675  115 ILE   B CG1 
1076 C  CG2 . ILE   B 106 ? 0.9153 0.8423 0.4466 0.3533  0.0627  0.0733  115 ILE   B CG2 
1077 C  CD1 . ILE   B 106 ? 0.9679 0.8235 0.4835 0.3290  0.0545  0.0619  115 ILE   B CD1 
1078 N  N   . PHE   B 107 ? 0.8262 0.8404 0.4444 0.3082  0.0616  0.0759  116 PHE   B N   
1079 C  CA  . PHE   B 107 ? 0.8014 0.8521 0.4394 0.3040  0.0625  0.0781  116 PHE   B CA  
1080 C  C   . PHE   B 107 ? 0.8231 0.8495 0.4341 0.3198  0.0630  0.0779  116 PHE   B C   
1081 O  O   . PHE   B 107 ? 0.8397 0.8296 0.4433 0.3099  0.0617  0.0747  116 PHE   B O   
1082 C  CB  . PHE   B 107 ? 0.7838 0.8352 0.4495 0.2762  0.0604  0.0750  116 PHE   B CB  
1083 C  CG  . PHE   B 107 ? 0.7626 0.8524 0.4594 0.2606  0.0610  0.0767  116 PHE   B CG  
1084 C  CD1 . PHE   B 107 ? 0.7607 0.8738 0.4610 0.2665  0.0632  0.0805  116 PHE   B CD1 
1085 C  CD2 . PHE   B 107 ? 0.7619 0.8616 0.4823 0.2399  0.0599  0.0745  116 PHE   B CD2 
1086 C  CE1 . PHE   B 107 ? 0.7483 0.8929 0.4751 0.2506  0.0646  0.0827  116 PHE   B CE1 
1087 C  CE2 . PHE   B 107 ? 0.7529 0.8819 0.4984 0.2247  0.0609  0.0760  116 PHE   B CE2 
1088 C  CZ  . PHE   B 107 ? 0.7394 0.8898 0.4878 0.2294  0.0634  0.0803  116 PHE   B CZ  
1089 N  N   . LYS   B 108 ? 0.8229 0.8671 0.4168 0.3455  0.0654  0.0818  117 LYS   B N   
1090 C  CA  . LYS   B 108 ? 0.8465 0.8681 0.4113 0.3643  0.0664  0.0829  117 LYS   B CA  
1091 C  C   . LYS   B 108 ? 0.8333 0.8873 0.4176 0.3572  0.0655  0.0839  117 LYS   B C   
1092 O  O   . LYS   B 108 ? 0.8086 0.9169 0.4138 0.3594  0.0654  0.0864  117 LYS   B O   
1093 C  CB  . LYS   B 108 ? 0.8794 0.9111 0.4173 0.3980  0.0694  0.0872  117 LYS   B CB  
1094 C  CG  . LYS   B 108 ? 0.9648 0.9435 0.4647 0.4126  0.0704  0.0853  117 LYS   B CG  
1095 C  CD  . LYS   B 108 ? 1.0584 1.0062 0.5151 0.4425  0.0730  0.0877  117 LYS   B CD  
1096 C  CE  . LYS   B 108 ? 1.1526 1.0410 0.5650 0.4584  0.0742  0.0852  117 LYS   B CE  
1097 N  NZ  . LYS   B 108 ? 1.1974 1.1068 0.6020 0.4787  0.0763  0.0868  117 LYS   B NZ  
1098 N  N   . THR   B 109 ? 0.8487 0.8711 0.4266 0.3473  0.0648  0.0817  118 THR   B N   
1099 C  CA  . THR   B 109 ? 0.8468 0.8951 0.4396 0.3409  0.0638  0.0819  118 THR   B CA  
1100 C  C   . THR   B 109 ? 0.8748 0.8958 0.4342 0.3604  0.0655  0.0844  118 THR   B C   
1101 O  O   . THR   B 109 ? 0.9013 0.8754 0.4265 0.3744  0.0679  0.0855  118 THR   B O   
1102 C  CB  . THR   B 109 ? 0.8576 0.9022 0.4784 0.3093  0.0620  0.0774  118 THR   B CB  
1103 O  OG1 . THR   B 109 ? 0.8933 0.8882 0.4971 0.3030  0.0632  0.0757  118 THR   B OG1 
1104 C  CG2 . THR   B 109 ? 0.8532 0.9074 0.4984 0.2913  0.0609  0.0753  118 THR   B CG2 
1105 N  N   . LYS   B 110 ? 0.8701 0.9165 0.4373 0.3603  0.0644  0.0852  119 LYS   B N   
1106 C  CA  . LYS   B 110 ? 0.8964 0.9175 0.4319 0.3784  0.0664  0.0883  119 LYS   B CA  
1107 C  C   . LYS   B 110 ? 0.9298 0.8883 0.4472 0.3656  0.0691  0.0869  119 LYS   B C   
1108 O  O   . LYS   B 110 ? 0.9567 0.8801 0.4402 0.3810  0.0723  0.0904  119 LYS   B O   
1109 C  CB  . LYS   B 110 ? 0.8962 0.9638 0.4454 0.3808  0.0637  0.0890  119 LYS   B CB  
1110 C  CG  . LYS   B 110 ? 0.9412 1.0110 0.5147 0.3524  0.0621  0.0844  119 LYS   B CG  
1111 C  CD  . LYS   B 110 ? 0.9625 1.0855 0.5526 0.3530  0.0581  0.0835  119 LYS   B CD  
1112 C  CE  . LYS   B 110 ? 1.0143 1.1244 0.6089 0.3366  0.0578  0.0804  119 LYS   B CE  
1113 N  NZ  . LYS   B 110 ? 1.0407 1.1421 0.6628 0.3058  0.0577  0.0749  119 LYS   B NZ  
1114 N  N   . ASP   B 111 ? 0.9278 0.8728 0.4667 0.3381  0.0684  0.0824  120 ASP   B N   
1115 C  CA  . ASP   B 111 ? 0.9528 0.8458 0.4794 0.3233  0.0711  0.0809  120 ASP   B CA  
1116 C  C   . ASP   B 111 ? 0.9633 0.8164 0.4791 0.3168  0.0713  0.0785  120 ASP   B C   
1117 O  O   . ASP   B 111 ? 0.9785 0.7954 0.4913 0.2994  0.0727  0.0762  120 ASP   B O   
1118 C  CB  . ASP   B 111 ? 0.9643 0.8727 0.5225 0.2969  0.0701  0.0774  120 ASP   B CB  
1119 C  CG  . ASP   B 111 ? 1.0269 0.9690 0.5924 0.3014  0.0694  0.0785  120 ASP   B CG  
1120 O  OD1 . ASP   B 111 ? 1.0600 0.9876 0.5973 0.3193  0.0718  0.0827  120 ASP   B OD1 
1121 O  OD2 . ASP   B 111 ? 1.0306 1.0115 0.6279 0.2871  0.0663  0.0751  120 ASP   B OD2 
1122 N  N   . GLY   B 112 ? 0.9536 0.8151 0.4635 0.3305  0.0700  0.0787  121 GLY   B N   
1123 C  CA  . GLY   B 112 ? 0.9680 0.7934 0.4654 0.3260  0.0693  0.0757  121 GLY   B CA  
1124 C  C   . GLY   B 112 ? 0.9392 0.7971 0.4633 0.3188  0.0660  0.0733  121 GLY   B C   
1125 O  O   . GLY   B 112 ? 0.9166 0.8239 0.4714 0.3139  0.0647  0.0740  121 GLY   B O   
1126 N  N   . ASP   B 113 ? 0.9369 0.7659 0.4477 0.3180  0.0648  0.0704  122 ASP   B N   
1127 C  CA  . ASP   B 113 ? 0.9140 0.7695 0.4451 0.3135  0.0622  0.0689  122 ASP   B CA  
1128 C  C   . ASP   B 113 ? 0.8924 0.7451 0.4501 0.2854  0.0590  0.0644  122 ASP   B C   
1129 O  O   . ASP   B 113 ? 0.9099 0.7292 0.4625 0.2709  0.0584  0.0614  122 ASP   B O   
1130 C  CB  . ASP   B 113 ? 0.9607 0.7930 0.4601 0.3338  0.0624  0.0685  122 ASP   B CB  
1131 C  CG  . ASP   B 113 ? 1.0401 0.8797 0.5128 0.3658  0.0658  0.0733  122 ASP   B CG  
1132 O  OD1 . ASP   B 113 ? 1.0378 0.9054 0.5182 0.3726  0.0675  0.0772  122 ASP   B OD1 
1133 O  OD2 . ASP   B 113 ? 1.1065 0.9245 0.5493 0.3852  0.0667  0.0730  122 ASP   B OD2 
1134 N  N   . ILE   B 114 ? 0.8488 0.7373 0.4340 0.2783  0.0573  0.0645  123 ILE   B N   
1135 C  CA  . ILE   B 114 ? 0.8204 0.7131 0.4318 0.2554  0.0543  0.0613  123 ILE   B CA  
1136 C  C   . ILE   B 114 ? 0.7996 0.7112 0.4178 0.2593  0.0530  0.0621  123 ILE   B C   
1137 O  O   . ILE   B 114 ? 0.7766 0.7181 0.3959 0.2733  0.0553  0.0661  123 ILE   B O   
1138 C  CB  . ILE   B 114 ? 0.8034 0.7242 0.4450 0.2403  0.0551  0.0619  123 ILE   B CB  
1139 C  CG1 . ILE   B 114 ? 0.8333 0.7268 0.4725 0.2277  0.0556  0.0594  123 ILE   B CG1 
1140 C  CG2 . ILE   B 114 ? 0.7812 0.7308 0.4540 0.2258  0.0537  0.0617  123 ILE   B CG2 
1141 C  CD1 . ILE   B 114 ? 0.8440 0.7547 0.4900 0.2280  0.0582  0.0614  123 ILE   B CD1 
1142 N  N   . GLY   B 115 ? 0.8001 0.6958 0.4221 0.2477  0.0494  0.0585  124 GLY   B N   
1143 C  CA  . GLY   B 115 ? 0.7930 0.7035 0.4199 0.2507  0.0482  0.0594  124 GLY   B CA  
1144 C  C   . GLY   B 115 ? 0.7655 0.7201 0.4226 0.2442  0.0504  0.0638  124 GLY   B C   
1145 O  O   . GLY   B 115 ? 0.7596 0.7294 0.4378 0.2319  0.0513  0.0642  124 GLY   B O   
1146 N  N   . ALA   B 116 ? 0.7530 0.7269 0.4106 0.2523  0.0518  0.0671  125 ALA   B N   
1147 C  CA  . ALA   B 116 ? 0.7324 0.7460 0.4157 0.2453  0.0548  0.0719  125 ALA   B CA  
1148 C  C   . ALA   B 116 ? 0.7322 0.7487 0.4165 0.2449  0.0545  0.0738  125 ALA   B C   
1149 O  O   . ALA   B 116 ? 0.7445 0.7488 0.4064 0.2596  0.0540  0.0736  125 ALA   B O   
1150 C  CB  . ALA   B 116 ? 0.7214 0.7689 0.4045 0.2588  0.0593  0.0767  125 ALA   B CB  
1151 N  N   . VAL   B 117 ? 0.7161 0.7460 0.4234 0.2291  0.0548  0.0757  126 VAL   B N   
1152 C  CA  A VAL   B 117 ? 0.7203 0.7533 0.4282 0.2287  0.0551  0.0786  126 VAL   B CA  
1153 C  CA  B VAL   B 117 ? 0.7212 0.7538 0.4297 0.2281  0.0550  0.0785  126 VAL   B CA  
1154 C  C   . VAL   B 117 ? 0.7090 0.7794 0.4310 0.2276  0.0616  0.0861  126 VAL   B C   
1155 O  O   . VAL   B 117 ? 0.7009 0.7901 0.4431 0.2147  0.0638  0.0876  126 VAL   B O   
1156 C  CB  A VAL   B 117 ? 0.7322 0.7467 0.4494 0.2146  0.0506  0.0757  126 VAL   B CB  
1157 C  CB  B VAL   B 117 ? 0.7324 0.7497 0.4544 0.2116  0.0511  0.0757  126 VAL   B CB  
1158 C  CG1 A VAL   B 117 ? 0.7544 0.7361 0.4519 0.2193  0.0442  0.0692  126 VAL   B CG1 
1159 C  CG1 B VAL   B 117 ? 0.7377 0.7618 0.4641 0.2094  0.0522  0.0803  126 VAL   B CG1 
1160 C  CG2 A VAL   B 117 ? 0.7332 0.7500 0.4718 0.1982  0.0505  0.0739  126 VAL   B CG2 
1161 C  CG2 B VAL   B 117 ? 0.7524 0.7366 0.4611 0.2115  0.0446  0.0685  126 VAL   B CG2 
1162 N  N   . ALA   B 118 ? 0.7083 0.7905 0.4181 0.2411  0.0650  0.0907  127 ALA   B N   
1163 C  CA  . ALA   B 118 ? 0.6937 0.8148 0.4167 0.2394  0.0722  0.0986  127 ALA   B CA  
1164 C  C   . ALA   B 118 ? 0.7015 0.8234 0.4319 0.2295  0.0745  0.1035  127 ALA   B C   
1165 O  O   . ALA   B 118 ? 0.6989 0.8328 0.4207 0.2388  0.0789  0.1092  127 ALA   B O   
1166 C  CB  . ALA   B 118 ? 0.6855 0.8269 0.3928 0.2611  0.0763  0.1020  127 ALA   B CB  
1167 N  N   . LEU   B 119 ? 0.7009 0.8097 0.4460 0.2117  0.0722  0.1018  128 LEU   B N   
1168 C  CA  . LEU   B 119 ? 0.7020 0.8071 0.4523 0.2027  0.0745  0.1068  128 LEU   B CA  
1169 C  C   . LEU   B 119 ? 0.6951 0.8167 0.4672 0.1833  0.0792  0.1105  128 LEU   B C   
1170 O  O   . LEU   B 119 ? 0.6964 0.8117 0.4795 0.1728  0.0765  0.1056  128 LEU   B O   
1171 C  CB  . LEU   B 119 ? 0.7125 0.7838 0.4569 0.2012  0.0671  0.1016  128 LEU   B CB  
1172 C  CG  . LEU   B 119 ? 0.7367 0.7903 0.4575 0.2177  0.0623  0.0983  128 LEU   B CG  
1173 C  CD1 . LEU   B 119 ? 0.7465 0.7720 0.4647 0.2137  0.0538  0.0916  128 LEU   B CD1 
1174 C  CD2 . LEU   B 119 ? 0.7445 0.8078 0.4540 0.2269  0.0669  0.1057  128 LEU   B CD2 
1175 N  N   . ASP   B 120 ? 0.6917 0.8341 0.4685 0.1782  0.0868  0.1189  129 ASP   B N   
1176 C  CA  . ASP   B 120 ? 0.6889 0.8447 0.4837 0.1574  0.0919  0.1225  129 ASP   B CA  
1177 C  C   . ASP   B 120 ? 0.6945 0.8210 0.4908 0.1457  0.0913  0.1233  129 ASP   B C   
1178 O  O   . ASP   B 120 ? 0.7022 0.8180 0.4887 0.1497  0.0938  0.1292  129 ASP   B O   
1179 C  CB  . ASP   B 120 ? 0.7160 0.9051 0.5141 0.1550  0.1011  0.1320  129 ASP   B CB  
1180 C  CG  . ASP   B 120 ? 0.7930 1.0213 0.5966 0.1618  0.1030  0.1319  129 ASP   B CG  
1181 O  OD1 . ASP   B 120 ? 0.8087 1.0623 0.6294 0.1463  0.1054  0.1320  129 ASP   B OD1 
1182 O  OD2 . ASP   B 120 ? 0.8203 1.0534 0.6098 0.1832  0.1017  0.1311  129 ASP   B OD2 
1183 N  N   . TYR   B 121 ? 0.6863 0.8002 0.4933 0.1324  0.0886  0.1180  130 TYR   B N   
1184 C  CA  . TYR   B 121 ? 0.6896 0.7752 0.4971 0.1227  0.0886  0.1186  130 TYR   B CA  
1185 C  C   . TYR   B 121 ? 0.6805 0.7675 0.5011 0.1030  0.0910  0.1164  130 TYR   B C   
1186 O  O   . TYR   B 121 ? 0.6771 0.7815 0.5066 0.0991  0.0891  0.1112  130 TYR   B O   
1187 C  CB  . TYR   B 121 ? 0.6996 0.7590 0.5020 0.1317  0.0804  0.1117  130 TYR   B CB  
1188 C  CG  . TYR   B 121 ? 0.7207 0.7684 0.5083 0.1465  0.0775  0.1140  130 TYR   B CG  
1189 C  CD1 . TYR   B 121 ? 0.7437 0.7723 0.5253 0.1467  0.0781  0.1183  130 TYR   B CD1 
1190 C  CD2 . TYR   B 121 ? 0.7331 0.7865 0.5105 0.1612  0.0736  0.1112  130 TYR   B CD2 
1191 C  CE1 . TYR   B 121 ? 0.7637 0.7835 0.5310 0.1607  0.0745  0.1199  130 TYR   B CE1 
1192 C  CE2 . TYR   B 121 ? 0.7538 0.7954 0.5159 0.1740  0.0700  0.1119  130 TYR   B CE2 
1193 C  CZ  . TYR   B 121 ? 0.7718 0.7988 0.5297 0.1736  0.0702  0.1163  130 TYR   B CZ  
1194 O  OH  . TYR   B 121 ? 0.7927 0.8099 0.5350 0.1866  0.0655  0.1164  130 TYR   B OH  
1195 N  N   . PRO   B 122 ? 0.6738 0.7395 0.4932 0.0914  0.0946  0.1197  131 PRO   B N   
1196 C  CA  . PRO   B 122 ? 0.6645 0.7260 0.4928 0.0722  0.0965  0.1164  131 PRO   B CA  
1197 C  C   . PRO   B 122 ? 0.6582 0.7116 0.4922 0.0733  0.0897  0.1060  131 PRO   B C   
1198 O  O   . PRO   B 122 ? 0.6699 0.7100 0.4999 0.0867  0.0842  0.1024  131 PRO   B O   
1199 C  CB  . PRO   B 122 ? 0.6851 0.7143 0.5044 0.0653  0.1010  0.1217  131 PRO   B CB  
1200 C  CG  . PRO   B 122 ? 0.6919 0.7212 0.5002 0.0767  0.1040  0.1306  131 PRO   B CG  
1201 C  CD  . PRO   B 122 ? 0.6745 0.7167 0.4817 0.0958  0.0972  0.1266  131 PRO   B CD  
1202 N  N   . ALA   B 123 ? 0.6357 0.6972 0.4784 0.0583  0.0902  0.1013  132 ALA   B N   
1203 C  CA  . ALA   B 123 ? 0.6232 0.6784 0.4704 0.0576  0.0850  0.0918  132 ALA   B CA  
1204 C  C   . ALA   B 123 ? 0.6233 0.6448 0.4652 0.0641  0.0821  0.0884  132 ALA   B C   
1205 O  O   . ALA   B 123 ? 0.6277 0.6474 0.4713 0.0728  0.0772  0.0826  132 ALA   B O   
1206 C  CB  . ALA   B 123 ? 0.6168 0.6807 0.4710 0.0383  0.0866  0.0878  132 ALA   B CB  
1207 N  N   . GLY   B 124 ? 0.6183 0.6145 0.4528 0.0609  0.0856  0.0927  133 GLY   B N   
1208 C  CA  . GLY   B 124 ? 0.6179 0.5851 0.4469 0.0689  0.0835  0.0906  133 GLY   B CA  
1209 C  C   . GLY   B 124 ? 0.6029 0.5706 0.4304 0.0866  0.0782  0.0905  133 GLY   B C   
1210 O  O   . GLY   B 124 ? 0.6075 0.5577 0.4328 0.0939  0.0757  0.0885  133 GLY   B O   
1211 N  N   . THR   B 125 ? 0.5847 0.5731 0.4126 0.0937  0.0763  0.0923  134 THR   B N   
1212 C  CA  . THR   B 125 ? 0.5757 0.5648 0.3999 0.1087  0.0707  0.0912  134 THR   B CA  
1213 C  C   . THR   B 125 ? 0.5670 0.5641 0.3969 0.1114  0.0659  0.0834  134 THR   B C   
1214 O  O   . THR   B 125 ? 0.5640 0.5581 0.3910 0.1208  0.0609  0.0808  134 THR   B O   
1215 C  CB  . THR   B 125 ? 0.5790 0.5802 0.3951 0.1162  0.0722  0.0980  134 THR   B CB  
1216 O  OG1 . THR   B 125 ? 0.5931 0.5891 0.4046 0.1100  0.0788  0.1060  134 THR   B OG1 
1217 C  CG2 . THR   B 125 ? 0.5762 0.5710 0.3840 0.1308  0.0665  0.0975  134 THR   B CG2 
1218 N  N   . SER   B 126 ? 0.5694 0.5754 0.4061 0.1024  0.0673  0.0794  135 SER   B N   
1219 C  CA  . SER   B 126 ? 0.5745 0.5862 0.4142 0.1049  0.0638  0.0730  135 SER   B CA  
1220 C  C   . SER   B 126 ? 0.5778 0.5730 0.4189 0.1088  0.0604  0.0687  135 SER   B C   
1221 O  O   . SER   B 126 ? 0.5834 0.5656 0.4272 0.1050  0.0618  0.0680  135 SER   B O   
1222 C  CB  . SER   B 126 ? 0.5996 0.6202 0.4453 0.0943  0.0658  0.0694  135 SER   B CB  
1223 O  OG  . SER   B 126 ? 0.6471 0.6809 0.4950 0.0845  0.0698  0.0730  135 SER   B OG  
1224 N  N   . GLY   B 127 ? 0.5693 0.5650 0.4076 0.1161  0.0564  0.0660  136 GLY   B N   
1225 C  CA  . GLY   B 127 ? 0.5758 0.5610 0.4169 0.1184  0.0531  0.0620  136 GLY   B CA  
1226 C  C   . GLY   B 127 ? 0.5818 0.5623 0.4182 0.1260  0.0487  0.0632  136 GLY   B C   
1227 O  O   . GLY   B 127 ? 0.5920 0.5680 0.4319 0.1270  0.0453  0.0599  136 GLY   B O   
1228 N  N   . SER   B 128 ? 0.5649 0.5483 0.3933 0.1310  0.0487  0.0680  137 SER   B N   
1229 C  CA  . SER   B 128 ? 0.5585 0.5380 0.3795 0.1390  0.0439  0.0689  137 SER   B CA  
1230 C  C   . SER   B 128 ? 0.5591 0.5365 0.3735 0.1423  0.0392  0.0640  137 SER   B C   
1231 O  O   . SER   B 128 ? 0.5611 0.5412 0.3697 0.1434  0.0408  0.0633  137 SER   B O   
1232 C  CB  . SER   B 128 ? 0.5644 0.5479 0.3763 0.1439  0.0463  0.0754  137 SER   B CB  
1233 O  OG  . SER   B 128 ? 0.5707 0.5509 0.3861 0.1399  0.0509  0.0805  137 SER   B OG  
1234 N  N   . PRO   B 129 ? 0.5574 0.5294 0.3717 0.1436  0.0333  0.0604  138 PRO   B N   
1235 C  CA  . PRO   B 129 ? 0.5655 0.5309 0.3718 0.1438  0.0289  0.0551  138 PRO   B CA  
1236 C  C   . PRO   B 129 ? 0.5885 0.5488 0.3761 0.1522  0.0265  0.0555  138 PRO   B C   
1237 O  O   . PRO   B 129 ? 0.5851 0.5482 0.3665 0.1588  0.0259  0.0591  138 PRO   B O   
1238 C  CB  . PRO   B 129 ? 0.5634 0.5286 0.3771 0.1407  0.0231  0.0512  138 PRO   B CB  
1239 C  CG  . PRO   B 129 ? 0.5611 0.5319 0.3795 0.1453  0.0228  0.0554  138 PRO   B CG  
1240 C  CD  . PRO   B 129 ? 0.5438 0.5160 0.3649 0.1447  0.0304  0.0608  138 PRO   B CD  
1241 N  N   . ILE   B 130 ? 0.6090 0.5596 0.3851 0.1531  0.0257  0.0519  139 ILE   B N   
1242 C  CA  . ILE   B 130 ? 0.6351 0.5754 0.3891 0.1624  0.0232  0.0507  139 ILE   B CA  
1243 C  C   . ILE   B 130 ? 0.6557 0.5802 0.4021 0.1577  0.0159  0.0436  139 ILE   B C   
1244 O  O   . ILE   B 130 ? 0.6504 0.5692 0.4030 0.1484  0.0158  0.0401  139 ILE   B O   
1245 C  CB  . ILE   B 130 ? 0.6474 0.5861 0.3910 0.1680  0.0281  0.0520  139 ILE   B CB  
1246 C  CG1 . ILE   B 130 ? 0.6520 0.6118 0.4055 0.1702  0.0346  0.0585  139 ILE   B CG1 
1247 C  CG2 . ILE   B 130 ? 0.6682 0.5916 0.3855 0.1795  0.0257  0.0500  139 ILE   B CG2 
1248 C  CD1 . ILE   B 130 ? 0.6644 0.6304 0.4152 0.1731  0.0393  0.0595  139 ILE   B CD1 
1249 N  N   . LEU   B 131 ? 0.6714 0.5899 0.4048 0.1628  0.0098  0.0414  140 LEU   B N   
1250 C  CA  . LEU   B 131 ? 0.6971 0.6035 0.4246 0.1559  0.0016  0.0339  140 LEU   B CA  
1251 C  C   . LEU   B 131 ? 0.7380 0.6208 0.4360 0.1616  -0.0024 0.0288  140 LEU   B C   
1252 O  O   . LEU   B 131 ? 0.7436 0.6234 0.4246 0.1751  -0.0008 0.0314  140 LEU   B O   
1253 C  CB  . LEU   B 131 ? 0.6926 0.6128 0.4311 0.1545  -0.0048 0.0333  140 LEU   B CB  
1254 C  CG  . LEU   B 131 ? 0.6959 0.6343 0.4486 0.1600  -0.0007 0.0409  140 LEU   B CG  
1255 C  CD1 . LEU   B 131 ? 0.6942 0.6398 0.4453 0.1649  -0.0076 0.0408  140 LEU   B CD1 
1256 C  CD2 . LEU   B 131 ? 0.6981 0.6471 0.4740 0.1518  0.0039  0.0428  140 LEU   B CD2 
1257 N  N   . ASP   B 132 ? 0.7659 0.6313 0.4569 0.1509  -0.0074 0.0215  141 ASP   B N   
1258 C  CA  . ASP   B 132 ? 0.8075 0.6439 0.4674 0.1538  -0.0123 0.0149  141 ASP   B CA  
1259 C  C   . ASP   B 132 ? 0.8272 0.6659 0.4824 0.1516  -0.0228 0.0092  141 ASP   B C   
1260 O  O   . ASP   B 132 ? 0.8118 0.6758 0.4891 0.1489  -0.0256 0.0112  141 ASP   B O   
1261 C  CB  . ASP   B 132 ? 0.8378 0.6489 0.4880 0.1421  -0.0113 0.0102  141 ASP   B CB  
1262 C  CG  . ASP   B 132 ? 0.8786 0.6947 0.5463 0.1215  -0.0161 0.0051  141 ASP   B CG  
1263 O  OD1 . ASP   B 132 ? 0.8639 0.7024 0.5488 0.1171  -0.0224 0.0035  141 ASP   B OD1 
1264 O  OD2 . ASP   B 132 ? 0.9164 0.7152 0.5802 0.1104  -0.0131 0.0032  141 ASP   B OD2 
1265 N  N   . LYS   B 133 ? 0.8600 0.6717 0.4852 0.1534  -0.0290 0.0017  142 LYS   B N   
1266 C  CA  . LYS   B 133 ? 0.8750 0.6890 0.4928 0.1519  -0.0401 -0.0047 142 LYS   B CA  
1267 C  C   . LYS   B 133 ? 0.8672 0.6968 0.5071 0.1327  -0.0479 -0.0102 142 LYS   B C   
1268 O  O   . LYS   B 133 ? 0.8659 0.7127 0.5110 0.1333  -0.0563 -0.0127 142 LYS   B O   
1269 C  CB  . LYS   B 133 ? 0.9321 0.7108 0.5096 0.1581  -0.0450 -0.0125 142 LYS   B CB  
1270 C  CG  . LYS   B 133 ? 1.0058 0.7837 0.5633 0.1814  -0.0416 -0.0078 142 LYS   B CG  
1271 C  CD  . LYS   B 133 ? 1.0806 0.8295 0.6089 0.1944  -0.0342 -0.0068 142 LYS   B CD  
1272 C  CE  . LYS   B 133 ? 1.1276 0.8782 0.6347 0.2177  -0.0314 -0.0029 142 LYS   B CE  
1273 N  NZ  . LYS   B 133 ? 1.1725 0.8968 0.6494 0.2332  -0.0246 -0.0023 142 LYS   B NZ  
1274 N  N   . CYS   B 134 ? 0.8607 0.6876 0.5141 0.1165  -0.0449 -0.0115 143 CYS   B N   
1275 C  CA  . CYS   B 134 ? 0.8483 0.6972 0.5269 0.0983  -0.0509 -0.0156 143 CYS   B CA  
1276 C  C   . CYS   B 134 ? 0.8135 0.7012 0.5266 0.1022  -0.0475 -0.0079 143 CYS   B C   
1277 O  O   . CYS   B 134 ? 0.7996 0.7107 0.5358 0.0905  -0.0514 -0.0101 143 CYS   B O   
1278 C  CB  . CYS   B 134 ? 0.8813 0.7135 0.5608 0.0793  -0.0479 -0.0191 143 CYS   B CB  
1279 S  SG  . CYS   B 134 ? 1.0006 0.7808 0.6369 0.0714  -0.0522 -0.0290 143 CYS   B SG  
1280 N  N   . GLY   B 135 ? 0.7987 0.6921 0.5145 0.1178  -0.0397 0.0009  144 GLY   B N   
1281 C  CA  . GLY   B 135 ? 0.7709 0.6924 0.5140 0.1219  -0.0349 0.0084  144 GLY   B CA  
1282 C  C   . GLY   B 135 ? 0.7497 0.6748 0.5106 0.1138  -0.0260 0.0116  144 GLY   B C   
1283 O  O   . GLY   B 135 ? 0.7372 0.6843 0.5215 0.1136  -0.0229 0.0157  144 GLY   B O   
1284 N  N   . ARG   B 136 ? 0.7465 0.6485 0.4945 0.1081  -0.0216 0.0099  145 ARG   B N   
1285 C  CA  . ARG   B 136 ? 0.7296 0.6334 0.4914 0.1007  -0.0133 0.0127  145 ARG   B CA  
1286 C  C   . ARG   B 136 ? 0.7100 0.6134 0.4711 0.1123  -0.0042 0.0200  145 ARG   B C   
1287 O  O   . ARG   B 136 ? 0.7249 0.6156 0.4666 0.1236  -0.0030 0.0217  145 ARG   B O   
1288 C  CB  . ARG   B 136 ? 0.7655 0.6439 0.5126 0.0881  -0.0129 0.0077  145 ARG   B CB  
1289 C  CG  . ARG   B 136 ? 0.8097 0.6942 0.5651 0.0701  -0.0200 0.0008  145 ARG   B CG  
1290 C  CD  . ARG   B 136 ? 0.8870 0.7399 0.6233 0.0568  -0.0183 -0.0034 145 ARG   B CD  
1291 N  NE  . ARG   B 136 ? 0.9718 0.7899 0.6727 0.0633  -0.0221 -0.0075 145 ARG   B NE  
1292 C  CZ  . ARG   B 136 ? 1.0410 0.8205 0.7144 0.0590  -0.0190 -0.0097 145 ARG   B CZ  
1293 N  NH1 . ARG   B 136 ? 1.0515 0.8225 0.7290 0.0477  -0.0117 -0.0075 145 ARG   B NH1 
1294 N  NH2 . ARG   B 136 ? 1.0663 0.8136 0.7055 0.0676  -0.0226 -0.0137 145 ARG   B NH2 
1295 N  N   . VAL   B 137 ? 0.6774 0.5960 0.4592 0.1095  0.0020  0.0239  146 VAL   B N   
1296 C  CA  . VAL   B 137 ? 0.6669 0.5877 0.4497 0.1179  0.0098  0.0299  146 VAL   B CA  
1297 C  C   . VAL   B 137 ? 0.6717 0.5735 0.4389 0.1180  0.0148  0.0299  146 VAL   B C   
1298 O  O   . VAL   B 137 ? 0.6738 0.5707 0.4451 0.1087  0.0177  0.0286  146 VAL   B O   
1299 C  CB  . VAL   B 137 ? 0.6498 0.5906 0.4564 0.1161  0.0143  0.0334  146 VAL   B CB  
1300 C  CG1 . VAL   B 137 ? 0.6550 0.5975 0.4609 0.1226  0.0215  0.0385  146 VAL   B CG1 
1301 C  CG2 . VAL   B 137 ? 0.6370 0.5935 0.4548 0.1195  0.0097  0.0343  146 VAL   B CG2 
1302 N  N   . ILE   B 138 ? 0.6750 0.5660 0.4224 0.1296  0.0159  0.0317  147 ILE   B N   
1303 C  CA  . ILE   B 138 ? 0.6836 0.5566 0.4125 0.1341  0.0205  0.0324  147 ILE   B CA  
1304 C  C   . ILE   B 138 ? 0.6765 0.5644 0.4144 0.1394  0.0277  0.0379  147 ILE   B C   
1305 O  O   . ILE   B 138 ? 0.6842 0.5616 0.4097 0.1434  0.0317  0.0389  147 ILE   B O   
1306 C  CB  . ILE   B 138 ? 0.6973 0.5501 0.3969 0.1456  0.0177  0.0308  147 ILE   B CB  
1307 C  CG1 . ILE   B 138 ? 0.7002 0.5700 0.4009 0.1580  0.0175  0.0347  147 ILE   B CG1 
1308 C  CG2 . ILE   B 138 ? 0.7102 0.5428 0.3974 0.1372  0.0103  0.0237  147 ILE   B CG2 
1309 C  CD1 . ILE   B 138 ? 0.7295 0.5829 0.4006 0.1729  0.0165  0.0341  147 ILE   B CD1 
1310 N  N   . GLY   B 139 ? 0.6542 0.5651 0.4123 0.1389  0.0290  0.0410  148 GLY   B N   
1311 C  CA  . GLY   B 139 ? 0.6418 0.5676 0.4096 0.1408  0.0349  0.0449  148 GLY   B CA  
1312 C  C   . GLY   B 139 ? 0.6231 0.5681 0.4071 0.1403  0.0358  0.0481  148 GLY   B C   
1313 O  O   . GLY   B 139 ? 0.6253 0.5721 0.4132 0.1401  0.0322  0.0481  148 GLY   B O   
1314 N  N   . LEU   B 140 ? 0.6019 0.5603 0.3943 0.1398  0.0406  0.0509  149 LEU   B N   
1315 C  CA  . LEU   B 140 ? 0.5856 0.5578 0.3907 0.1375  0.0426  0.0542  149 LEU   B CA  
1316 C  C   . LEU   B 140 ? 0.5869 0.5728 0.3878 0.1428  0.0459  0.0583  149 LEU   B C   
1317 O  O   . LEU   B 140 ? 0.5846 0.5751 0.3800 0.1459  0.0478  0.0582  149 LEU   B O   
1318 C  CB  . LEU   B 140 ? 0.5773 0.5533 0.3977 0.1287  0.0452  0.0529  149 LEU   B CB  
1319 C  CG  . LEU   B 140 ? 0.5834 0.5528 0.4120 0.1235  0.0432  0.0494  149 LEU   B CG  
1320 C  CD1 . LEU   B 140 ? 0.5757 0.5495 0.4169 0.1178  0.0469  0.0487  149 LEU   B CD1 
1321 C  CD2 . LEU   B 140 ? 0.5901 0.5582 0.4202 0.1257  0.0387  0.0498  149 LEU   B CD2 
1322 N  N   . TYR   B 141 ? 0.5907 0.5846 0.3940 0.1440  0.0468  0.0625  150 TYR   B N   
1323 C  CA  . TYR   B 141 ? 0.5902 0.6013 0.3916 0.1474  0.0506  0.0674  150 TYR   B CA  
1324 C  C   . TYR   B 141 ? 0.5733 0.5965 0.3887 0.1365  0.0546  0.0688  150 TYR   B C   
1325 O  O   . TYR   B 141 ? 0.5621 0.5766 0.3857 0.1291  0.0547  0.0679  150 TYR   B O   
1326 C  CB  . TYR   B 141 ? 0.5951 0.6052 0.3897 0.1534  0.0499  0.0715  150 TYR   B CB  
1327 C  CG  . TYR   B 141 ? 0.6028 0.6316 0.3992 0.1536  0.0551  0.0781  150 TYR   B CG  
1328 C  CD1 . TYR   B 141 ? 0.6133 0.6440 0.4191 0.1444  0.0584  0.0820  150 TYR   B CD1 
1329 C  CD2 . TYR   B 141 ? 0.6124 0.6556 0.3990 0.1637  0.0572  0.0810  150 TYR   B CD2 
1330 C  CE1 . TYR   B 141 ? 0.6216 0.6684 0.4284 0.1421  0.0640  0.0887  150 TYR   B CE1 
1331 C  CE2 . TYR   B 141 ? 0.6136 0.6784 0.4035 0.1628  0.0628  0.0877  150 TYR   B CE2 
1332 C  CZ  . TYR   B 141 ? 0.6264 0.6928 0.4268 0.1506  0.0662  0.0916  150 TYR   B CZ  
1333 O  OH  . TYR   B 141 ? 0.6391 0.7261 0.4424 0.1472  0.0725  0.0987  150 TYR   B OH  
1334 N  N   . GLY   B 142 ? 0.5672 0.6103 0.3844 0.1358  0.0577  0.0705  151 GLY   B N   
1335 C  CA  . GLY   B 142 ? 0.5714 0.6256 0.4006 0.1231  0.0608  0.0708  151 GLY   B CA  
1336 C  C   . GLY   B 142 ? 0.5735 0.6441 0.4061 0.1202  0.0612  0.0679  151 GLY   B C   
1337 O  O   . GLY   B 142 ? 0.5657 0.6448 0.4073 0.1081  0.0630  0.0667  151 GLY   B O   
1338 N  N   . ASN   B 143 ? 0.5793 0.6535 0.4029 0.1314  0.0595  0.0667  152 ASN   B N   
1339 C  CA  . ASN   B 143 ? 0.5898 0.6826 0.4142 0.1321  0.0596  0.0649  152 ASN   B CA  
1340 C  C   . ASN   B 143 ? 0.6041 0.7128 0.4177 0.1475  0.0599  0.0683  152 ASN   B C   
1341 O  O   . ASN   B 143 ? 0.6168 0.7081 0.4159 0.1598  0.0585  0.0680  152 ASN   B O   
1342 C  CB  . ASN   B 143 ? 0.6106 0.6875 0.4315 0.1322  0.0578  0.0598  152 ASN   B CB  
1343 C  CG  . ASN   B 143 ? 0.6445 0.7417 0.4660 0.1324  0.0577  0.0579  152 ASN   B CG  
1344 O  OD1 . ASN   B 143 ? 0.6483 0.7731 0.4776 0.1272  0.0583  0.0590  152 ASN   B OD1 
1345 N  ND2 . ASN   B 143 ? 0.6566 0.7418 0.4696 0.1375  0.0568  0.0552  152 ASN   B ND2 
1346 N  N   . GLY   B 144 ? 0.5989 0.7402 0.4190 0.1465  0.0620  0.0716  153 GLY   B N   
1347 C  CA  . GLY   B 144 ? 0.6153 0.7770 0.4258 0.1631  0.0632  0.0755  153 GLY   B CA  
1348 C  C   . GLY   B 144 ? 0.6160 0.8220 0.4379 0.1598  0.0652  0.0782  153 GLY   B C   
1349 O  O   . GLY   B 144 ? 0.6078 0.8284 0.4409 0.1474  0.0641  0.0750  153 GLY   B O   
1350 N  N   . VAL   B 145 ? 0.6223 0.8516 0.4410 0.1708  0.0682  0.0838  154 VAL   B N   
1351 C  CA  . VAL   B 145 ? 0.6251 0.9039 0.4550 0.1696  0.0706  0.0872  154 VAL   B CA  
1352 C  C   . VAL   B 145 ? 0.6394 0.9397 0.4746 0.1681  0.0761  0.0943  154 VAL   B C   
1353 O  O   . VAL   B 145 ? 0.6442 0.9205 0.4689 0.1748  0.0777  0.0969  154 VAL   B O   
1354 C  CB  . VAL   B 145 ? 0.6325 0.9285 0.4498 0.1922  0.0689  0.0869  154 VAL   B CB  
1355 C  CG1 . VAL   B 145 ? 0.6410 0.9397 0.4414 0.2160  0.0717  0.0919  154 VAL   B CG1 
1356 C  CG2 . VAL   B 145 ? 0.6188 0.9639 0.4508 0.1868  0.0680  0.0865  154 VAL   B CG2 
1357 N  N   . VAL   B 146 ? 0.6444 0.9902 0.4960 0.1576  0.0791  0.0975  155 VAL   B N   
1358 C  CA  . VAL   B 146 ? 0.6646 1.0368 0.5225 0.1547  0.0857  0.1053  155 VAL   B CA  
1359 C  C   . VAL   B 146 ? 0.6872 1.1042 0.5416 0.1765  0.0878  0.1093  155 VAL   B C   
1360 O  O   . VAL   B 146 ? 0.6790 1.1285 0.5401 0.1790  0.0851  0.1069  155 VAL   B O   
1361 C  CB  . VAL   B 146 ? 0.6604 1.0529 0.5391 0.1250  0.0888  0.1066  155 VAL   B CB  
1362 C  CG1 . VAL   B 146 ? 0.6641 1.0707 0.5458 0.1204  0.0968  0.1157  155 VAL   B CG1 
1363 C  CG2 . VAL   B 146 ? 0.6790 1.0289 0.5595 0.1059  0.0857  0.1009  155 VAL   B CG2 
1364 N  N   . ILE   B 147 ? 0.7151 1.1336 0.5569 0.1946  0.0923  0.1152  156 ILE   B N   
1365 C  CA  . ILE   B 147 ? 0.7357 1.1926 0.5700 0.2201  0.0946  0.1189  156 ILE   B CA  
1366 C  C   . ILE   B 147 ? 0.7364 1.2516 0.5874 0.2147  0.1025  0.1273  156 ILE   B C   
1367 O  O   . ILE   B 147 ? 0.7347 1.2577 0.6029 0.1882  0.1059  0.1298  156 ILE   B O   
1368 C  CB  . ILE   B 147 ? 0.7712 1.1889 0.5751 0.2485  0.0937  0.1183  156 ILE   B CB  
1369 C  CG1 . ILE   B 147 ? 0.7953 1.1919 0.5907 0.2488  0.0981  0.1225  156 ILE   B CG1 
1370 C  CG2 . ILE   B 147 ? 0.8044 1.1710 0.5953 0.2494  0.0865  0.1103  156 ILE   B CG2 
1371 C  CD1 . ILE   B 147 ? 0.8384 1.1981 0.6020 0.2761  0.0968  0.1210  156 ILE   B CD1 
1372 N  N   . LYS   B 148 ? 0.7360 1.2934 0.5819 0.2391  0.1057  0.1316  157 LYS   B N   
1373 C  CA  . LYS   B 148 ? 0.7261 1.3475 0.5888 0.2365  0.1136  0.1398  157 LYS   B CA  
1374 C  C   . LYS   B 148 ? 0.7378 1.3555 0.6083 0.2170  0.1213  0.1465  157 LYS   B C   
1375 O  O   . LYS   B 148 ? 0.7309 1.3828 0.6253 0.1901  0.1249  0.1495  157 LYS   B O   
1376 C  CB  . LYS   B 148 ? 0.7477 1.4030 0.5956 0.2731  0.1173  0.1444  157 LYS   B CB  
1377 C  CG  . LYS   B 148 ? 0.8293 1.4352 0.6427 0.3052  0.1132  0.1402  157 LYS   B CG  
1378 C  CD  . LYS   B 148 ? 0.8711 1.5021 0.6772 0.3291  0.1092  0.1378  157 LYS   B CD  
1379 C  CE  . LYS   B 148 ? 0.8907 1.5161 0.7089 0.3119  0.1010  0.1308  157 LYS   B CE  
1380 N  NZ  . LYS   B 148 ? 0.8632 1.5603 0.7019 0.3124  0.1003  0.1323  157 LYS   B NZ  
1381 N  N   . ASN   B 149 ? 0.7522 1.3271 0.6015 0.2291  0.1236  0.1486  158 ASN   B N   
1382 C  CA  . ASN   B 149 ? 0.7491 1.3187 0.6020 0.2139  0.1313  0.1559  158 ASN   B CA  
1383 C  C   . ASN   B 149 ? 0.7380 1.2681 0.5999 0.1825  0.1290  0.1532  158 ASN   B C   
1384 O  O   . ASN   B 149 ? 0.7492 1.2566 0.6061 0.1741  0.1339  0.1583  158 ASN   B O   
1385 C  CB  . ASN   B 149 ? 0.7952 1.3371 0.6206 0.2398  0.1345  0.1592  158 ASN   B CB  
1386 C  CG  . ASN   B 149 ? 0.8791 1.3581 0.6792 0.2551  0.1258  0.1508  158 ASN   B CG  
1387 O  OD1 . ASN   B 149 ? 0.9049 1.3653 0.7044 0.2550  0.1179  0.1429  158 ASN   B OD1 
1388 N  ND2 . ASN   B 149 ? 0.9039 1.3499 0.6819 0.2682  0.1273  0.1524  158 ASN   B ND2 
1389 N  N   . GLY   B 150 ? 0.7151 1.2368 0.5880 0.1670  0.1219  0.1454  159 GLY   B N   
1390 C  CA  . GLY   B 150 ? 0.7064 1.1905 0.5861 0.1394  0.1195  0.1420  159 GLY   B CA  
1391 C  C   . GLY   B 150 ? 0.7048 1.1245 0.5660 0.1459  0.1148  0.1378  159 GLY   B C   
1392 O  O   . GLY   B 150 ? 0.7188 1.1052 0.5834 0.1265  0.1131  0.1353  159 GLY   B O   
1393 N  N   . SER   B 151 ? 0.6839 1.0854 0.5245 0.1734  0.1124  0.1367  160 SER   B N   
1394 C  CA  A SER   B 151 ? 0.6983 1.0434 0.5213 0.1802  0.1072  0.1322  160 SER   B CA  
1395 C  CA  B SER   B 151 ? 0.6964 1.0415 0.5198 0.1797  0.1072  0.1322  160 SER   B CA  
1396 C  C   . SER   B 151 ? 0.6905 1.0092 0.5136 0.1777  0.0985  0.1224  160 SER   B C   
1397 O  O   . SER   B 151 ? 0.6887 1.0262 0.5130 0.1863  0.0956  0.1189  160 SER   B O   
1398 C  CB  A SER   B 151 ? 0.7305 1.0655 0.5297 0.2083  0.1077  0.1338  160 SER   B CB  
1399 C  CB  B SER   B 151 ? 0.7234 1.0576 0.5231 0.2072  0.1078  0.1340  160 SER   B CB  
1400 O  OG  A SER   B 151 ? 0.7849 1.0686 0.5676 0.2134  0.1019  0.1289  160 SER   B OG  
1401 O  OG  B SER   B 151 ? 0.7437 1.0945 0.5346 0.2287  0.1056  0.1311  160 SER   B OG  
1402 N  N   . TYR   B 152 ? 0.6616 0.9381 0.4827 0.1673  0.0948  0.1186  161 TYR   B N   
1403 C  CA  . TYR   B 152 ? 0.6279 0.8778 0.4489 0.1641  0.0877  0.1100  161 TYR   B CA  
1404 C  C   . TYR   B 152 ? 0.6187 0.8381 0.4189 0.1847  0.0827  0.1057  161 TYR   B C   
1405 O  O   . TYR   B 152 ? 0.6261 0.8248 0.4131 0.1930  0.0826  0.1074  161 TYR   B O   
1406 C  CB  . TYR   B 152 ? 0.6169 0.8380 0.4454 0.1440  0.0869  0.1084  161 TYR   B CB  
1407 C  CG  . TYR   B 152 ? 0.6124 0.8052 0.4410 0.1403  0.0805  0.1001  161 TYR   B CG  
1408 C  CD1 . TYR   B 152 ? 0.6093 0.8163 0.4469 0.1338  0.0783  0.0953  161 TYR   B CD1 
1409 C  CD2 . TYR   B 152 ? 0.6311 0.7857 0.4513 0.1431  0.0769  0.0972  161 TYR   B CD2 
1410 C  CE1 . TYR   B 152 ? 0.6201 0.8018 0.4569 0.1308  0.0735  0.0883  161 TYR   B CE1 
1411 C  CE2 . TYR   B 152 ? 0.6455 0.7777 0.4672 0.1391  0.0720  0.0902  161 TYR   B CE2 
1412 C  CZ  . TYR   B 152 ? 0.6445 0.7895 0.4741 0.1332  0.0709  0.0860  161 TYR   B CZ  
1413 O  OH  . TYR   B 152 ? 0.6648 0.7884 0.4947 0.1300  0.0671  0.0797  161 TYR   B OH  
1414 N  N   . VAL   B 153 ? 0.6000 0.8158 0.3957 0.1922  0.0784  0.1002  162 VAL   B N   
1415 C  CA  . VAL   B 153 ? 0.6043 0.7874 0.3792 0.2084  0.0738  0.0955  162 VAL   B CA  
1416 C  C   . VAL   B 153 ? 0.5960 0.7548 0.3759 0.1972  0.0691  0.0888  162 VAL   B C   
1417 O  O   . VAL   B 153 ? 0.5870 0.7617 0.3741 0.1942  0.0685  0.0869  162 VAL   B O   
1418 C  CB  . VAL   B 153 ? 0.6129 0.8119 0.3723 0.2313  0.0746  0.0963  162 VAL   B CB  
1419 C  CG1 . VAL   B 153 ? 0.6346 0.7924 0.3674 0.2473  0.0707  0.0919  162 VAL   B CG1 
1420 C  CG2 . VAL   B 153 ? 0.6161 0.8522 0.3754 0.2418  0.0806  0.1035  162 VAL   B CG2 
1421 N  N   . SER   B 154 ? 0.5957 0.7197 0.3723 0.1915  0.0658  0.0855  163 SER   B N   
1422 C  CA  . SER   B 154 ? 0.5954 0.6981 0.3769 0.1817  0.0622  0.0796  163 SER   B CA  
1423 C  C   . SER   B 154 ? 0.6118 0.6899 0.3743 0.1941  0.0589  0.0755  163 SER   B C   
1424 O  O   . SER   B 154 ? 0.6289 0.6937 0.3734 0.2072  0.0580  0.0759  163 SER   B O   
1425 C  CB  . SER   B 154 ? 0.6002 0.6812 0.3888 0.1695  0.0606  0.0784  163 SER   B CB  
1426 O  OG  . SER   B 154 ? 0.6255 0.6843 0.4160 0.1633  0.0572  0.0728  163 SER   B OG  
1427 N  N   . ALA   B 155 ? 0.6067 0.6747 0.3714 0.1888  0.0573  0.0715  164 ALA   B N   
1428 C  CA  . ALA   B 155 ? 0.6324 0.6713 0.3783 0.1972  0.0549  0.0680  164 ALA   B CA  
1429 C  C   . ALA   B 155 ? 0.6476 0.6567 0.3932 0.1886  0.0515  0.0645  164 ALA   B C   
1430 O  O   . ALA   B 155 ? 0.6436 0.6567 0.4044 0.1777  0.0511  0.0649  164 ALA   B O   
1431 C  CB  . ALA   B 155 ? 0.6386 0.6789 0.3867 0.1943  0.0552  0.0658  164 ALA   B CB  
1432 N  N   . ILE   B 156 ? 0.6597 0.6395 0.3869 0.1936  0.0492  0.0612  165 ILE   B N   
1433 C  CA  . ILE   B 156 ? 0.6728 0.6298 0.4019 0.1835  0.0455  0.0572  165 ILE   B CA  
1434 C  C   . ILE   B 156 ? 0.6874 0.6365 0.4234 0.1737  0.0463  0.0546  165 ILE   B C   
1435 O  O   . ILE   B 156 ? 0.7011 0.6295 0.4207 0.1771  0.0466  0.0529  165 ILE   B O   
1436 C  CB  . ILE   B 156 ? 0.6938 0.6235 0.3995 0.1909  0.0419  0.0543  165 ILE   B CB  
1437 C  CG1 . ILE   B 156 ? 0.7036 0.6420 0.3995 0.2034  0.0418  0.0571  165 ILE   B CG1 
1438 C  CG2 . ILE   B 156 ? 0.7014 0.6155 0.4143 0.1775  0.0374  0.0499  165 ILE   B CG2 
1439 C  CD1 . ILE   B 156 ? 0.7313 0.6409 0.3999 0.2122  0.0379  0.0534  165 ILE   B CD1 
1440 N  N   . THR   B 157 ? 0.6800 0.6447 0.4380 0.1625  0.0477  0.0548  166 THR   B N   
1441 C  CA  . THR   B 157 ? 0.6878 0.6490 0.4534 0.1539  0.0493  0.0526  166 THR   B CA  
1442 C  C   . THR   B 157 ? 0.6945 0.6369 0.4626 0.1447  0.0475  0.0491  166 THR   B C   
1443 O  O   . THR   B 157 ? 0.6912 0.6375 0.4733 0.1376  0.0457  0.0481  166 THR   B O   
1444 C  CB  . THR   B 157 ? 0.7003 0.6825 0.4855 0.1460  0.0513  0.0532  166 THR   B CB  
1445 O  OG1 . THR   B 157 ? 0.7142 0.7180 0.4991 0.1518  0.0528  0.0562  166 THR   B OG1 
1446 C  CG2 . THR   B 157 ? 0.7084 0.6884 0.4985 0.1396  0.0534  0.0508  166 THR   B CG2 
1447 N  N   . GLN   B 158 ? 0.7038 0.6275 0.4590 0.1446  0.0485  0.0477  167 GLN   B N   
1448 C  CA  . GLN   B 158 ? 0.7172 0.6263 0.4758 0.1336  0.0476  0.0446  167 GLN   B CA  
1449 C  C   . GLN   B 158 ? 0.7533 0.6589 0.5134 0.1283  0.0522  0.0446  167 GLN   B C   
1450 O  O   . GLN   B 158 ? 0.7630 0.6634 0.5088 0.1356  0.0551  0.0465  167 GLN   B O   
1451 C  CB  . GLN   B 158 ? 0.7209 0.6049 0.4595 0.1351  0.0442  0.0425  167 GLN   B CB  
1452 C  CG  . GLN   B 158 ? 0.7136 0.5850 0.4564 0.1211  0.0425  0.0389  167 GLN   B CG  
1453 C  CD  . GLN   B 158 ? 0.7294 0.6190 0.4951 0.1135  0.0388  0.0371  167 GLN   B CD  
1454 O  OE1 . GLN   B 158 ? 0.7188 0.6282 0.5041 0.1116  0.0409  0.0385  167 GLN   B OE1 
1455 N  NE2 . GLN   B 158 ? 0.7514 0.6335 0.5132 0.1097  0.0329  0.0338  167 GLN   B NE2 
1456 N  N   . GLY   B 159 ? 0.7717 0.6816 0.5481 0.1170  0.0531  0.0428  168 GLY   B N   
1457 C  CA  . GLY   B 159 ? 0.8117 0.7185 0.5895 0.1114  0.0581  0.0429  168 GLY   B CA  
1458 C  C   . GLY   B 159 ? 0.8682 0.7516 0.6324 0.1050  0.0594  0.0423  168 GLY   B C   
1459 O  O   . GLY   B 159 ? 0.8803 0.7478 0.6325 0.1047  0.0556  0.0410  168 GLY   B O   
1460 N  N   . LYS   B 160 ? 0.9022 0.7819 0.6667 0.0990  0.0649  0.0432  169 LYS   B N   
1461 C  CA  . LYS   B 160 ? 0.9483 0.8053 0.7003 0.0899  0.0679  0.0435  169 LYS   B CA  
1462 C  C   . LYS   B 160 ? 0.9649 0.8353 0.7392 0.0750  0.0686  0.0415  169 LYS   B C   
1463 O  O   . LYS   B 160 ? 0.9581 0.8510 0.7521 0.0742  0.0709  0.0413  169 LYS   B O   
1464 C  CB  . LYS   B 160 ? 0.9851 0.8292 0.7199 0.0942  0.0749  0.0472  169 LYS   B CB  
1465 C  CG  . LYS   B 160 ? 1.0561 0.8748 0.7767 0.0832  0.0801  0.0488  169 LYS   B CG  
1466 C  CD  . LYS   B 160 ? 1.1247 0.9319 0.8279 0.0892  0.0877  0.0534  169 LYS   B CD  
1467 C  CE  . LYS   B 160 ? 1.1858 0.9666 0.8742 0.0768  0.0945  0.0562  169 LYS   B CE  
1468 N  NZ  . LYS   B 160 ? 1.2205 0.9955 0.8959 0.0821  0.1027  0.0612  169 LYS   B NZ  
1469 N  N   . ARG   B 161 ? 0.9814 0.8394 0.7523 0.0633  0.0665  0.0395  170 ARG   B N   
1470 C  CA  . ARG   B 161 ? 0.9861 0.8621 0.7794 0.0488  0.0671  0.0377  170 ARG   B CA  
1471 C  C   . ARG   B 161 ? 1.0092 0.8708 0.7940 0.0367  0.0750  0.0401  170 ARG   B C   
1472 O  O   . ARG   B 161 ? 1.0345 0.8638 0.7932 0.0345  0.0765  0.0413  170 ARG   B O   
1473 C  CB  . ARG   B 161 ? 0.9971 0.8764 0.7964 0.0418  0.0585  0.0333  170 ARG   B CB  
1474 C  CG  . ARG   B 161 ? 1.0078 0.9184 0.8364 0.0318  0.0573  0.0314  170 ARG   B CG  
1475 C  CD  . ARG   B 161 ? 1.0339 0.9471 0.8660 0.0210  0.0490  0.0267  170 ARG   B CD  
1476 N  NE  . ARG   B 161 ? 1.0465 0.9890 0.9039 0.0079  0.0497  0.0254  170 ARG   B NE  
1477 C  CZ  . ARG   B 161 ? 1.0543 1.0268 0.9332 0.0086  0.0432  0.0228  170 ARG   B CZ  
1478 N  NH1 . ARG   B 161 ? 1.0499 1.0240 0.9266 0.0209  0.0357  0.0214  170 ARG   B NH1 
1479 N  NH2 . ARG   B 161 ? 1.0319 1.0344 0.9340 -0.0021 0.0445  0.0220  170 ARG   B NH2 
1480 N  N   . GLU   B 162 ? 1.0006 0.8839 0.8047 0.0301  0.0810  0.0414  171 GLU   B N   
1481 C  CA  . GLU   B 162 ? 1.0221 0.8940 0.8187 0.0182  0.0900  0.0447  171 GLU   B CA  
1482 C  C   . GLU   B 162 ? 1.0292 0.8940 0.8268 -0.0022 0.0888  0.0429  171 GLU   B C   
1483 O  O   . GLU   B 162 ? 1.0378 0.8904 0.8276 -0.0154 0.0965  0.0460  171 GLU   B O   
1484 C  CB  . GLU   B 162 ? 1.0458 0.9438 0.8608 0.0190  0.0978  0.0469  171 GLU   B CB  
1485 C  CG  . GLU   B 162 ? 1.1224 1.0248 0.9338 0.0363  0.0992  0.0479  171 GLU   B CG  
1486 C  CD  . GLU   B 162 ? 1.2334 1.1095 1.0164 0.0444  0.1038  0.0518  171 GLU   B CD  
1487 O  OE1 . GLU   B 162 ? 1.2526 1.1283 1.0309 0.0436  0.1124  0.0552  171 GLU   B OE1 
1488 O  OE2 . GLU   B 162 ? 1.2700 1.1273 1.0347 0.0530  0.0989  0.0517  171 GLU   B OE2 
1489 S  S   . DMS   C .   ? 1.0239 0.9004 0.8175 0.0621  0.0826  -0.0131 201 DMS   B S   
1490 O  O   . DMS   C .   ? 1.0134 0.9064 0.8180 0.0749  0.0844  -0.0083 201 DMS   B O   
1491 C  C1  . DMS   C .   ? 1.0408 0.8785 0.8213 0.0679  0.0877  -0.0145 201 DMS   B C1  
1492 C  C2  . DMS   C .   ? 1.0184 0.9025 0.8214 0.0528  0.0794  -0.0055 201 DMS   B C2  
1493 N  N1  . A1B8X D .   ? 0.7446 0.9453 0.6066 0.0951  0.0681  0.0732  202 A1B8X B N1  
1494 N  N3  . A1B8X D .   ? 0.7194 0.8551 0.5708 0.0837  0.0564  0.0427  202 A1B8X B N3  
1495 C  C4  . A1B8X D .   ? 0.7700 0.9924 0.6441 0.0710  0.0621  0.0591  202 A1B8X B C4  
1496 C  C5  . A1B8X D .   ? 0.7650 1.0122 0.6402 0.0716  0.0579  0.0537  202 A1B8X B C5  
1497 C  C6  . A1B8X D .   ? 0.7533 1.0423 0.6225 0.1022  0.0592  0.0634  202 A1B8X B C6  
1498 C  C7  . A1B8X D .   ? 0.7516 1.0266 0.6227 0.0982  0.0639  0.0691  202 A1B8X B C7  
1499 C  C8  . A1B8X D .   ? 0.7403 0.8850 0.6028 0.0773  0.0704  0.0722  202 A1B8X B C8  
1500 C  C10 . A1B8X D .   ? 0.7279 0.8534 0.5960 0.0527  0.0661  0.0556  202 A1B8X B C10 
1501 C  C13 . A1B8X D .   ? 0.7294 0.8514 0.5860 0.0802  0.0604  0.0507  202 A1B8X B C13 
1502 C  C15 . A1B8X D .   ? 0.7290 0.8465 0.5776 0.0917  0.0582  0.0477  202 A1B8X B C15 
1503 C  C17 . A1B8X D .   ? 0.7397 0.8747 0.5987 0.0796  0.0739  0.0793  202 A1B8X B C17 
1504 C  C20 . A1B8X D .   ? 0.7427 0.8648 0.5907 0.0888  0.0805  0.0935  202 A1B8X B C20 
1505 C  C21 . A1B8X D .   ? 0.7397 0.8899 0.5977 0.0761  0.0826  0.0929  202 A1B8X B C21 
1506 C  C22 . A1B8X D .   ? 0.7290 0.9208 0.6027 0.0582  0.0814  0.0869  202 A1B8X B C22 
1507 O  O1  . A1B8X D .   ? 0.7608 0.9052 0.6079 0.1089  0.0660  0.0718  202 A1B8X B O1  
1508 C  C1  . A1B8X D .   ? 0.7487 0.9121 0.6056 0.0952  0.0679  0.0723  202 A1B8X B C1  
1509 C  C2  . A1B8X D .   ? 0.7459 0.9718 0.6203 0.0761  0.0695  0.0723  202 A1B8X B C2  
1510 C  C3  . A1B8X D .   ? 0.7516 1.0032 0.6297 0.0755  0.0654  0.0668  202 A1B8X B C3  
1511 O  O2  . A1B8X D .   ? 0.7511 1.0424 0.6293 0.0812  0.0572  0.0572  202 A1B8X B O2  
1512 N  N2  . A1B8X D .   ? 0.7450 0.8610 0.6057 0.0742  0.0681  0.0661  202 A1B8X B N2  
1513 C  C9  . A1B8X D .   ? 0.7356 0.8559 0.5981 0.0703  0.0655  0.0595  202 A1B8X B C9  
1514 C  C11 . A1B8X D .   ? 0.7250 0.8546 0.5930 0.0494  0.0631  0.0485  202 A1B8X B C11 
1515 C  C12 . A1B8X D .   ? 0.7247 0.8540 0.5871 0.0640  0.0604  0.0465  202 A1B8X B C12 
1516 C  C14 . A1B8X D .   ? 0.7328 0.8506 0.5893 0.0834  0.0625  0.0567  202 A1B8X B C14 
1517 C  C16 . A1B8X D .   ? 0.7208 0.8522 0.5797 0.0652  0.0575  0.0399  202 A1B8X B C16 
1518 C  C18 . A1B8X D .   ? 0.7428 0.8504 0.5935 0.0903  0.0725  0.0801  202 A1B8X B C18 
1519 C  C19 . A1B8X D .   ? 0.7427 0.8445 0.5881 0.0947  0.0752  0.0867  202 A1B8X B C19 
1520 CL CL1 . A1B8X D .   ? 0.7382 0.8098 0.5734 0.1077  0.0717  0.0866  202 A1B8X B CL1 
1521 N  N4  . A1B8X D .   ? 0.7373 0.9143 0.6015 0.0656  0.0880  0.0987  202 A1B8X B N4  
1522 N  N5  . A1B8X D .   ? 0.7260 0.9298 0.6009 0.0537  0.0872  0.0948  202 A1B8X B N5  
1523 C  C23 . A1B8X D .   ? 0.7371 0.8950 0.6008 0.0716  0.0788  0.0856  202 A1B8X B C23 
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