data_7I9Q
# 
_entry.id   7I9Q 
# 
_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   7I9Q         pdb_00007i9q 10.2210/pdb7i9q/pdb 
WWPDB D_1001408493 ?            ?                   
# 
_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                        7I9Q 
_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    2   ? ?    ? ? 
4 non-polymer syn '(2R)-(6-chloro-1H-indazol-4-yl)[(2,3-dihydro-1H-isoindol-5-yl)amino]acetonitrile' 323.780   1   ? ?    ? ? 
5 water       nat water                                                                              18.015    100 ? ?    ? ? 
# 
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)-(6-chloro-1H-indazol-4-yl)[(2,3-dihydro-1H-isoindol-5-yl)amino]acetonitrile' A1B9L 
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 
A1B9L non-polymer         . '(2R)-(6-chloro-1H-indazol-4-yl)[(2,3-dihydro-1H-isoindol-5-yl)amino]acetonitrile' ? 'C17 H14 Cl N5'  
323.780 
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  88  GLU GLU 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 A1B9L 1  202 203 A1B9L LIG B . 
E 3 DMS   1  203 204 DMS   DMS B . 
F 5 HOH   1  101 118 HOH   HOH A . 
F 5 HOH   2  102 48  HOH   HOH A . 
F 5 HOH   3  103 83  HOH   HOH A . 
F 5 HOH   4  104 34  HOH   HOH A . 
F 5 HOH   5  105 98  HOH   HOH A . 
F 5 HOH   6  106 65  HOH   HOH A . 
F 5 HOH   7  107 28  HOH   HOH A . 
F 5 HOH   8  108 153 HOH   HOH A . 
F 5 HOH   9  109 120 HOH   HOH A . 
F 5 HOH   10 110 105 HOH   HOH A . 
F 5 HOH   11 111 40  HOH   HOH A . 
F 5 HOH   12 112 27  HOH   HOH A . 
F 5 HOH   13 113 110 HOH   HOH A . 
F 5 HOH   14 114 140 HOH   HOH A . 
F 5 HOH   15 115 138 HOH   HOH A . 
F 5 HOH   16 116 121 HOH   HOH A . 
F 5 HOH   17 117 29  HOH   HOH A . 
F 5 HOH   18 118 50  HOH   HOH A . 
F 5 HOH   19 119 119 HOH   HOH A . 
F 5 HOH   20 120 124 HOH   HOH A . 
F 5 HOH   21 121 155 HOH   HOH A . 
F 5 HOH   22 122 144 HOH   HOH A . 
F 5 HOH   23 123 139 HOH   HOH A . 
G 5 HOH   1  301 14  HOH   HOH B . 
G 5 HOH   2  302 58  HOH   HOH B . 
G 5 HOH   3  303 39  HOH   HOH B . 
G 5 HOH   4  304 51  HOH   HOH B . 
G 5 HOH   5  305 11  HOH   HOH B . 
G 5 HOH   6  306 100 HOH   HOH B . 
G 5 HOH   7  307 5   HOH   HOH B . 
G 5 HOH   8  308 81  HOH   HOH B . 
G 5 HOH   9  309 92  HOH   HOH B . 
G 5 HOH   10 310 123 HOH   HOH B . 
G 5 HOH   11 311 115 HOH   HOH B . 
G 5 HOH   12 312 60  HOH   HOH B . 
G 5 HOH   13 313 12  HOH   HOH B . 
G 5 HOH   14 314 31  HOH   HOH B . 
G 5 HOH   15 315 157 HOH   HOH B . 
G 5 HOH   16 316 63  HOH   HOH B . 
G 5 HOH   17 317 1   HOH   HOH B . 
G 5 HOH   18 318 32  HOH   HOH B . 
G 5 HOH   19 319 130 HOH   HOH B . 
G 5 HOH   20 320 4   HOH   HOH B . 
G 5 HOH   21 321 131 HOH   HOH B . 
G 5 HOH   22 322 13  HOH   HOH B . 
G 5 HOH   23 323 20  HOH   HOH B . 
G 5 HOH   24 324 69  HOH   HOH B . 
G 5 HOH   25 325 133 HOH   HOH B . 
G 5 HOH   26 326 56  HOH   HOH B . 
G 5 HOH   27 327 42  HOH   HOH B . 
G 5 HOH   28 328 108 HOH   HOH B . 
G 5 HOH   29 329 24  HOH   HOH B . 
G 5 HOH   30 330 68  HOH   HOH B . 
G 5 HOH   31 331 117 HOH   HOH B . 
G 5 HOH   32 332 151 HOH   HOH B . 
G 5 HOH   33 333 137 HOH   HOH B . 
G 5 HOH   34 334 2   HOH   HOH B . 
G 5 HOH   35 335 132 HOH   HOH B . 
G 5 HOH   36 336 154 HOH   HOH B . 
G 5 HOH   37 337 16  HOH   HOH B . 
G 5 HOH   38 338 10  HOH   HOH B . 
G 5 HOH   39 339 21  HOH   HOH B . 
G 5 HOH   40 340 143 HOH   HOH B . 
G 5 HOH   41 341 9   HOH   HOH B . 
G 5 HOH   42 342 23  HOH   HOH B . 
G 5 HOH   43 343 80  HOH   HOH B . 
G 5 HOH   44 344 156 HOH   HOH B . 
G 5 HOH   45 345 30  HOH   HOH B . 
G 5 HOH   46 346 102 HOH   HOH B . 
G 5 HOH   47 347 158 HOH   HOH B . 
G 5 HOH   48 348 116 HOH   HOH B . 
G 5 HOH   49 349 3   HOH   HOH B . 
G 5 HOH   50 350 142 HOH   HOH B . 
G 5 HOH   51 351 64  HOH   HOH B . 
G 5 HOH   52 352 18  HOH   HOH B . 
G 5 HOH   53 353 135 HOH   HOH B . 
G 5 HOH   54 354 35  HOH   HOH B . 
G 5 HOH   55 355 152 HOH   HOH B . 
G 5 HOH   56 356 43  HOH   HOH B . 
G 5 HOH   57 357 112 HOH   HOH B . 
G 5 HOH   58 358 127 HOH   HOH B . 
G 5 HOH   59 359 62  HOH   HOH B . 
G 5 HOH   60 360 61  HOH   HOH B . 
G 5 HOH   61 361 107 HOH   HOH B . 
G 5 HOH   62 362 148 HOH   HOH B . 
G 5 HOH   63 363 82  HOH   HOH B . 
G 5 HOH   64 364 87  HOH   HOH B . 
G 5 HOH   65 365 72  HOH   HOH B . 
G 5 HOH   66 366 26  HOH   HOH B . 
G 5 HOH   67 367 141 HOH   HOH B . 
G 5 HOH   68 368 149 HOH   HOH B . 
G 5 HOH   69 369 145 HOH   HOH B . 
G 5 HOH   70 370 45  HOH   HOH B . 
G 5 HOH   71 371 129 HOH   HOH B . 
G 5 HOH   72 372 126 HOH   HOH B . 
G 5 HOH   73 373 150 HOH   HOH B . 
G 5 HOH   74 374 59  HOH   HOH B . 
G 5 HOH   75 375 134 HOH   HOH B . 
G 5 HOH   76 376 147 HOH   HOH B . 
G 5 HOH   77 377 44  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           7I9Q 
_cell.length_a           42.581 
_cell.length_b           42.581 
_cell.length_c           216.957 
_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                         7I9Q 
_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.crystals_number   1 
_exptl.entry_id          7I9Q 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.120 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.12 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   42.00 
_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   2024-07-17 
_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                     7I9Q 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             41.780 
_reflns.d_resolution_high            2.020 
_reflns.number_obs                   13967 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.293 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.800 
_reflns.B_iso_Wilson_estimate        40.960 
_reflns.pdbx_redundancy              12.900 
_reflns.pdbx_Rrim_I_all              0.305 
_reflns.pdbx_Rpim_I_all              0.083 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     180388 
_reflns.pdbx_scaling_rejects         143 
_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 2.020 2.130  ? 26859 ? ? 7.229 ? ? ? 13.600 ? 0.500  ? 1978 ? ? ? ? 100.000 7.507 1.995 0.451 ? 
1 2 6.400 41.780 ? 5491  ? ? 0.071 ? ? ? 10.300 ? 23.000 ? 531  ? ? ? ? 99.300  0.074 0.022 0.998 ? 
# 
_refine.entry_id                                 7I9Q 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.0240 
_refine.ls_d_res_low                             41.7800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.7000 
_refine.ls_number_reflns_obs                     13651 
_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                          0.2266 
_refine.ls_R_factor_R_work                       0.2239 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2775 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.7300 
_refine.ls_number_reflns_R_free                  646 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               51.5200 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -4.9791 
_refine.aniso_B[2][2]                            -4.9791 
_refine.aniso_B[3][3]                            9.9582 
_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               0.9430 
_refine.correlation_coeff_Fo_to_Fc_free          0.9220 
_refine.overall_SU_R_Cruickshank_DPI             0.2180 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.1950 
_refine.pdbx_overall_SU_R_Blow_DPI               0.2440 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2040 
_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                                120.240 
_refine.B_iso_min                                28.670 
_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                        7I9Q 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.340 
_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                       2.0240 
_refine_hist.d_res_low                        41.7800 
_refine_hist.pdbx_number_atoms_ligand         31 
_refine_hist.number_atoms_solvent             100 
_refine_hist.number_atoms_total               1603 
_refine_hist.pdbx_number_residues_total       194 
_refine_hist.pdbx_B_iso_mean_ligand           60.64 
_refine_hist.pdbx_B_iso_mean_solvent          51.85 
_refine_hist.pdbx_number_atoms_protein        1472 
_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        533  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              267  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1566 ?      ? 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 196  ?      ? 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      1206 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1566 0.008  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2131 0.990  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.320  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    18.620 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.0200 
_refine_ls_shell.d_res_low                        2.0600 
_refine_ls_shell.pdbx_total_number_of_bins_used   33 
_refine_ls_shell.percent_reflns_obs               70.2300 
_refine_ls_shell.number_reflns_R_work             415 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3884 
_refine_ls_shell.R_factor_R_free                  0.3160 
_refine_ls_shell.percent_reflns_R_free            2.8100 
_refine_ls_shell.number_reflns_R_free             12 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                427 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7I9Q 
_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-0028904-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I9Q 
_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 3 ? 
F N N 5 ? 
G 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 7I9Q A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I9Q 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 7I9Q SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I9Q MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I9Q MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I9Q 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)' 4400 ? 
1 MORE         -26  ? 
1 'SSA (A^2)'  9740 ? 
# 
_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,G 
# 
_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 ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
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 PHE B 37  ? N PHE B 46  O TYR B 70  ? O TYR B 79  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
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 LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
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 PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
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                   7I9Q 
_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 ASP B 71 ? ? -160.25 119.14 
2 1 CYS B 80 ? ? 80.44   -14.73 
3 1 LEU B 92 ? ? -131.80 -41.85 
# 
_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     377 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   G 
_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 -13.7556 -1.7961 -19.4719 -0.0827 -0.1038 -0.2642 0.1661 0.1587 0.1474 4.4713 5.0148 4.2656 
-2.3955 0.5349 1.2047  0.4801 -0.5057 0.0256 0.5260 0.3748 -0.4654 -0.5881 -0.0143 0.3938 
'X-RAY DIFFRACTION' 2 ? refined -18.4049 0.6921  -15.6408 0.0769  0.0114  -0.0830 0.1874 0.0379 0.0372 1.9322 1.5978 2.4087 
-0.6972 0.4282 -0.2571 0.3523 -0.3560 0.0038 0.1489 0.0777 0.0195  -0.1859 0.1832  0.2094 
# 
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 88  '{ 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 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLY 16  ? B GLY 7   
15 1 Y 1 B GLU 172 ? B GLU 163 
16 1 Y 1 B GLU 173 ? B GLU 164 
17 1 Y 1 B THR 174 ? B THR 165 
18 1 Y 1 B PRO 175 ? B PRO 166 
19 1 Y 1 B VAL 176 ? B VAL 167 
20 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 
A1B9L N1   N  N N 1   
A1B9L N3   N  N N 2   
A1B9L C4   C  Y N 3   
A1B9L C5   C  Y N 4   
A1B9L C6   C  Y N 5   
A1B9L C7   C  Y N 6   
A1B9L C8   C  Y N 7   
A1B9L C10  C  N N 8   
A1B9L C13  C  Y N 9   
A1B9L C15  C  Y N 10  
A1B9L C17  C  Y N 11  
A1B9L C1   C  N N 12  
A1B9L C2   C  N R 13  
A1B9L N2   N  N N 14  
A1B9L C3   C  Y N 15  
A1B9L C9   C  N N 16  
A1B9L C11  C  Y N 17  
A1B9L C12  C  Y N 18  
A1B9L CL1  CL N N 19  
A1B9L C14  C  Y N 20  
A1B9L N4   N  Y N 21  
A1B9L N5   N  Y N 22  
A1B9L C16  C  Y N 23  
A1B9L H1   H  N N 24  
A1B9L H3   H  N N 25  
A1B9L H4   H  N N 26  
A1B9L H5   H  N N 27  
A1B9L H6   H  N N 28  
A1B9L H7   H  N N 29  
A1B9L H8   H  N N 30  
A1B9L H9   H  N N 31  
A1B9L H10  H  N N 32  
A1B9L H11  H  N N 33  
A1B9L H12  H  N N 34  
A1B9L H13  H  N N 35  
A1B9L H14  H  N N 36  
A1B9L H15  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
# 
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 
A1B9L CL1 C13  sing N N 1   
A1B9L C14 C13  doub Y N 2   
A1B9L C14 C15  sing Y N 3   
A1B9L C13 C12  sing Y N 4   
A1B9L N4  C15  sing Y N 5   
A1B9L N4  N5   sing Y N 6   
A1B9L C15 C17  doub Y N 7   
A1B9L C12 C11  doub Y N 8   
A1B9L N5  C16  doub Y N 9   
A1B9L C17 C11  sing Y N 10  
A1B9L C17 C16  sing Y N 11  
A1B9L C11 C2   sing N N 12  
A1B9L C2  C1   sing N N 13  
A1B9L C2  N2   sing N N 14  
A1B9L C1  N1   trip N N 15  
A1B9L N2  C3   sing N N 16  
A1B9L C3  C8   doub Y N 17  
A1B9L C3  C4   sing Y N 18  
A1B9L C8  C7   sing Y N 19  
A1B9L C4  C5   doub Y N 20  
A1B9L C7  C6   doub Y N 21  
A1B9L C7  C9   sing N N 22  
A1B9L C5  C6   sing Y N 23  
A1B9L C6  C10  sing N N 24  
A1B9L C9  N3   sing N N 25  
A1B9L N3  C10  sing N N 26  
A1B9L N3  H1   sing N N 27  
A1B9L C4  H3   sing N N 28  
A1B9L C5  H4   sing N N 29  
A1B9L C8  H5   sing N N 30  
A1B9L C10 H6   sing N N 31  
A1B9L C10 H7   sing N N 32  
A1B9L C2  H8   sing N N 33  
A1B9L N2  H9   sing N N 34  
A1B9L C9  H10  sing N N 35  
A1B9L C9  H11  sing N N 36  
A1B9L C12 H12  sing N N 37  
A1B9L C14 H13  sing N N 38  
A1B9L N4  H14  sing N N 39  
A1B9L C16 H15  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_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                    7I9Q 
_atom_sites.fract_transf_matrix[1][1]   0.023485 
_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]   0.023485 
_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]   0.004609 
_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   ? -21.413 19.343  -7.498  1.00 57.16  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.458 18.315  -7.489  1.00 56.84  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.429 17.536  -8.815  1.00 54.60  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.405 18.148  -9.888  1.00 55.47  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.850 18.954  -7.244  1.00 59.71  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.708 18.247  -6.202  1.00 67.03  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.708 18.848  -5.745  1.00 68.68  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.383 17.093  -5.843  1.00 70.15  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.415 16.199  -8.745  1.00 51.55  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.381 15.381  -9.946  1.00 49.40  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.770 15.154  -10.523 1.00 47.29  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.745 15.125  -9.780  1.00 47.63  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.661 14.046  -9.700  1.00 49.43  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.197 14.207  -9.408  1.00 50.24  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.324 12.632  -9.216  1.00 50.59  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.646 13.254  -8.980  1.00 48.43  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.862 15.011  -11.851 1.00 45.19  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.131 14.785  -12.534 1.00 44.24  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.996 13.824  -13.710 1.00 43.28  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.898 13.611  -14.217 1.00 42.87  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.811 16.099  -12.960 1.00 44.33  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -25.071 16.885  -14.019 1.00 45.57  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.145 17.858  -13.668 1.00 46.26  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.371 16.728  -15.369 1.00 46.69  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.472 18.594  -14.634 1.00 47.61  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.721 17.477  -16.345 1.00 47.75  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.774 18.414  -15.972 1.00 48.95  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -23.091 19.135  -16.923 1.00 51.15  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.115 13.225  -14.135 1.00 42.45  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -26.090 12.274  -15.228 1.00 42.72  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.916 12.743  -16.436 1.00 42.79  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.879 13.498  -16.290 1.00 43.37  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.486 10.860  -14.718 1.00 42.90  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.948 10.827  -14.224 1.00 43.19  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.523 10.407  -13.616 1.00 43.41  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.470 9.491   -13.985 1.00 43.91  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.499 12.332  -17.634 1.00 42.69  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.163 12.638  -18.911 1.00 43.21  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.206 11.336  -19.717 1.00 43.65  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -26.181 10.657  -19.816 1.00 42.72  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.356 13.654  -19.731 1.00 45.05  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.306 15.060  -19.177 1.00 51.24  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.437 15.999  -19.994 1.00 59.24  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.485 15.510  -20.646 1.00 60.16  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.701 17.224  -19.979 1.00 62.01  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.352 11.011  -20.336 1.00 44.34  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.441 9.790   -21.126 1.00 45.61  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.522 9.877   -22.349 1.00 46.95  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.457 10.930  -22.987 1.00 47.71  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.888 9.491   -21.518 1.00 47.20  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -30.073 8.043   -21.932 1.00 51.17  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.531 7.645   -21.987 1.00 54.43  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.690 6.211   -22.227 1.00 56.83  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.685 5.656   -23.436 1.00 59.75  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.517 6.405   -24.519 1.00 61.37  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.810 4.341   -23.570 1.00 58.67  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.767 8.803   -22.635 1.00 46.82  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.851 8.761   -23.783 1.00 47.79  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.184 7.672   -24.821 1.00 48.53  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.521 7.611   -25.847 1.00 49.63  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.401 8.632   -23.320 1.00 48.11  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.200 6.848   -24.572 1.00 48.05  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.613 5.853   -25.552 1.00 48.31  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.199 4.581   -24.996 1.00 49.13  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.317 4.424   -23.776 1.00 49.35  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.588 3.667   -25.903 1.00 49.24  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.121 2.353   -25.542 1.00 50.29  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -28.003 1.353   -25.369 1.00 51.39  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.966 1.467   -26.025 1.00 51.35  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.046 1.809   -26.646 1.00 51.30  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.403 2.442   -26.702 1.00 55.94  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.615 3.445   -26.005 1.00 57.21  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.246 1.968   -27.487 1.00 57.62  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.247 0.320   -24.559 1.00 52.14  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.288 -0.749  -24.411 1.00 53.21  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.703 -1.892  -25.328 1.00 55.58  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.604 -2.671  -25.005 1.00 55.47  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -27.092 -1.128  -22.944 1.00 53.23  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.406 0.039   -22.211 1.00 53.59  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.302 -2.413  -22.826 1.00 53.56  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.337 -0.094  -20.768 1.00 54.41  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -27.082 -1.948  -26.518 0.50 56.55  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -27.066 -1.954  -26.508 0.50 56.55  ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -27.327 -2.981  -27.521 0.50 58.09  ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -27.362 -2.927  -27.554 0.50 58.10  ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -26.020 -3.428  -28.176 0.50 59.70  ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -26.063 -3.385  -28.254 0.50 59.78  ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -25.063 -2.659  -28.254 0.50 59.77  ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -25.127 -2.598  -28.385 0.50 59.93  ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -28.263 -2.479  -28.640 0.50 59.41  ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -28.344 -2.266  -28.551 0.50 59.32  ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -27.677 -1.347  -29.288 0.50 60.37  ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -29.495 -1.791  -27.849 0.50 60.20  ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -29.678 -2.192  -28.160 0.50 59.82  ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -28.785 -3.188  -29.664 0.50 59.69  ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -26.000 -4.650  -28.702 1.00 60.92  ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -24.845 -5.148  -29.443 1.00 63.97  ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -24.974 -4.575  -30.890 1.00 67.35  ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -26.068 -4.571  -31.458 1.00 67.33  ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -24.874 -6.687  -29.468 1.00 63.97  ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -23.800 -7.357  -30.282 1.00 64.88  ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -23.876 -7.715  -31.601 1.00 65.92  ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -22.574 -7.925  -29.786 1.00 64.88  ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -22.732 -8.378  -31.977 1.00 65.98  ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -21.922 -8.531  -30.880 1.00 65.68  ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -21.920 -7.896  -28.548 1.00 65.22  ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -20.674 -9.146  -30.757 1.00 66.26  ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -20.695 -8.522  -28.426 1.00 66.06  ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -20.072 -9.114  -29.524 1.00 66.13  ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -23.881 -4.052  -31.463 1.00 69.89  ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -23.899 -3.533  -32.830 1.00 72.61  ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -23.222 -4.555  -33.730 1.00 75.36  ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -22.018 -4.761  -33.593 1.00 75.64  ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -23.145 -2.188  -32.949 1.00 75.97  ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -23.096 -1.680  -34.393 1.00 84.88  ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -22.151 -0.550  -34.773 1.00 94.09  ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -21.264 -0.202  -33.959 1.00 96.56  ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -22.295 -0.019  -35.900 1.00 96.60  ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -23.967 -5.195  -34.644 1.00 77.22  ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -23.356 -6.152  -35.568 1.00 79.96  ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -22.517 -5.347  -36.559 1.00 82.03  ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -22.937 -4.263  -36.976 1.00 82.35  ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -24.426 -6.972  -36.309 1.00 82.98  ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -25.477 -7.587  -35.382 1.00 88.05  ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -26.809 -7.822  -36.115 1.00 92.99  ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -26.801 -9.047  -36.998 1.00 97.25  ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -28.070 -9.175  -37.770 1.00 100.76 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -21.323 -5.836  -36.889 1.00 83.51  ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -20.421 -5.126  -37.800 1.00 85.86  ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -19.863 -3.848  -37.155 1.00 86.74  ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -19.783 -2.798  -37.798 1.00 87.38  ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -21.068 -4.825  -39.175 1.00 89.07  ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -21.360 -6.049  -40.020 1.00 97.91  ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -20.529 -6.990  -40.011 1.00 100.49 ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -22.407 -6.057  -40.715 1.00 100.41 ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -19.485 -3.942  -35.879 1.00 86.47  ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -18.851 -2.824  -35.185 1.00 86.24  ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -17.321 -2.906  -35.448 1.00 85.83  ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -16.836 -3.929  -35.944 1.00 85.94  ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -19.143 -2.910  -33.690 1.00 86.20  ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -16.568 -1.836  -35.151 1.00 85.25  ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -15.117 -1.848  -35.333 1.00 85.22  ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -14.448 -2.883  -34.380 1.00 83.89  ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -14.502 -2.731  -33.162 1.00 83.28  ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -14.544 -0.438  -35.112 1.00 88.69  ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -13.031 -0.373  -35.208 1.00 95.84  ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -12.390 0.617   -34.257 1.00 104.54 ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -13.087 1.565   -33.823 1.00 106.52 ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -11.186 0.451   -33.952 1.00 107.01 ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -13.859 -3.950  -34.951 1.00 82.82  ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -13.203 -5.007  -34.181 1.00 81.90  ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -11.721 -4.674  -33.989 1.00 80.36  ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -10.969 -4.700  -34.958 1.00 80.13  ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -13.377 -6.401  -34.837 1.00 82.86  ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -12.881 -7.491  -33.907 1.00 83.50  ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -14.831 -6.657  -35.219 1.00 83.39  ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -11.295 -4.364  -32.750 1.00 78.81  ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -9.897  -4.006  -32.466 1.00 77.79  ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -9.440  -4.574  -31.095 1.00 76.66  ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -10.226 -5.214  -30.411 1.00 76.13  ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -9.717  -2.469  -32.600 1.00 79.09  ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -8.329  -2.156  -32.724 1.00 80.29  ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -10.292 -1.713  -31.420 1.00 79.44  ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -8.172  -4.396  -30.736 1.00 75.90  ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -7.657  -4.860  -29.457 1.00 75.47  ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -7.176  -6.292  -29.415 1.00 74.71  ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -7.749  -7.171  -30.059 1.00 75.02  ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -6.125  -6.523  -28.621 1.00 73.65  ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -5.498  -7.830  -28.409 1.00 73.08  ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -6.041  -8.550  -27.125 1.00 70.96  ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -6.917  -8.002  -26.459 1.00 70.96  ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -3.959  -7.675  -28.410 1.00 74.79  ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -3.401  -7.040  -27.157 1.00 78.98  ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.814  -5.953  -26.739 1.00 80.32  ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -2.436  -7.705  -26.530 1.00 79.97  ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -5.586  -9.795  -26.822 1.00 69.30  ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -6.046  -10.578 -25.653 1.00 68.35  ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -4.893  -11.003 -24.730 1.00 66.92  ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -4.483  -12.170 -24.739 1.00 67.36  ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -6.808  -11.820 -26.110 1.00 69.86  ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -7.892  -11.496 -26.956 1.00 73.05  ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -4.331  -10.082 -23.937 1.00 65.41  ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -3.167  -10.452 -23.117 1.00 64.75  ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -3.474  -11.255 -21.856 1.00 63.45  ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -4.510  -11.048 -21.232 1.00 62.87  ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -2.522  -9.104  -22.796 1.00 65.83  ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -3.665  -8.137  -22.807 1.00 66.25  ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -4.654  -8.646  -23.819 1.00 64.76  ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -2.567  -12.174 -21.487 1.00 62.72  ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -2.679  -12.952 -20.247 1.00 62.74  ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -1.675  -12.332 -19.277 1.00 61.15  ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.475  -12.389 -19.518 1.00 60.92  ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -2.411  -14.446 -20.480 1.00 65.39  ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -3.563  -15.144 -21.199 1.00 71.41  ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -3.383  -16.658 -21.271 1.00 77.80  ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -4.040  -17.233 -22.454 1.00 82.87  ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -5.292  -17.687 -22.471 1.00 85.67  ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -6.034  -17.657 -21.367 1.00 85.73  ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -5.809  -18.180 -23.590 1.00 84.67  ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -2.172  -11.642 -18.246 1.00 59.90  ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -1.336  -10.879 -17.322 1.00 58.78  ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -1.413  -11.357 -15.881 1.00 57.04  ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -2.511  -11.572 -15.385 1.00 56.68  ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -1.800  -9.410  -17.365 1.00 58.93  ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.774  -8.754  -18.741 1.00 60.50  ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -2.461  -7.400  -18.718 1.00 60.81  ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? -0.353  -8.649  -19.255 1.00 60.84  ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? -0.270  -11.447 -15.183 1.00 55.76  ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? -0.283  -11.800 -13.763 1.00 55.16  ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.522  -10.516 -12.969 1.00 52.99  ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? 0.337   -9.633  -12.995 1.00 53.87  ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 1.050   -12.434 -13.339 1.00 58.89  ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 1.101   -13.954 -13.445 1.00 66.79  ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? 0.119   -14.549 -13.951 1.00 68.49  ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 2.121   -14.551 -13.007 1.00 69.64  ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -1.689  -10.376 -12.295 1.00 50.15  ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -1.973  -9.143  -11.560 1.00 48.36  ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -2.266  -9.396  -10.053 1.00 47.52  ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.479  -10.534 -9.621  1.00 47.34  ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -3.085  -8.263  -12.241 1.00 47.93  ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -2.906  -8.190  -13.756 1.00 48.45  ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -4.483  -8.748  -11.887 1.00 47.46  ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -2.233  -8.312  -9.261  1.00 46.79  ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.556  -8.290  -7.843  1.00 46.73  ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.568  -7.162  -7.602  1.00 45.77  ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -3.514  -6.139  -8.282  1.00 46.08  ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -1.301  -8.054  -7.018  1.00 47.35  ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.514  -7.362  -6.677  1.00 44.25  ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.513  -6.349  -6.357  1.00 43.19  ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -5.386  -6.001  -4.869  1.00 43.09  ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.463  -6.887  -3.990  1.00 44.08  ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -6.920  -6.846  -6.710  1.00 42.75  ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -8.082  -5.934  -6.296  1.00 42.60  ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -8.142  -4.720  -7.174  1.00 42.74  ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.388  -6.674  -6.342  1.00 42.00  ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -5.083  -4.738  -4.584  1.00 42.02  ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -4.874  -4.317  -3.207  1.00 42.14  ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -6.199  -3.884  -2.509  1.00 43.40  ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -7.251  -3.824  -3.160  1.00 43.63  ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.757  -3.251  -3.137  1.00 42.69  ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -4.094  -1.856  -3.633  1.00 45.99  ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.282  -1.605  -3.957  1.00 45.24  ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.172  -1.013  -3.695  1.00 48.19  ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -6.134  -3.576  -1.200  1.00 44.08  ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.273  -3.140  -0.397  1.00 44.93  ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -7.943  -1.864  -0.956  1.00 44.99  ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -9.140  -1.683  -0.782  1.00 45.78  ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -6.852  -2.969  1.072   1.00 47.88  ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -7.999  -3.127  2.061   1.00 54.89  ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.635  -3.003  3.529   1.00 62.97  ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.144  -1.926  3.936   1.00 64.11  ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.840  -3.987  4.276   1.00 65.96  ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.200  -1.017  -1.676  1.00 43.98  ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.758  0.189   -2.284  1.00 43.06  ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.421  -0.049  -3.656  1.00 41.59  ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.885  0.914   -4.279  1.00 41.04  ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.679  1.253   -2.435  1.00 45.22  ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.051  1.524   -1.195  1.00 48.86  ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.481  -1.301  -4.117  1.00 40.44  ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -9.083  -1.610  -5.411  1.00 40.16  ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.191  -1.266  -6.595  1.00 40.25  ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.662  -1.193  -7.725  1.00 40.02  ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.885  -1.090  -6.358  1.00 40.45  ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -5.941  -0.760  -7.405  1.00 41.05  ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.217  -1.998  -7.888  1.00 42.08  ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.697  -2.769  -7.071  1.00 42.03  ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.933  0.291   -6.902  1.00 41.72  ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.586  1.622   -6.604  1.00 45.94  ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.622  1.924   -7.222  1.00 46.82  ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -5.068  2.357   -5.753  1.00 47.94  ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -5.173  -2.188  -9.219  1.00 42.19  ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.460  -3.321  -9.778  1.00 42.96  ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -2.998  -2.962  -10.013 1.00 45.50  ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.646  -1.810  -10.305 1.00 45.75  ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -5.085  -3.804  -11.095 1.00 41.67  ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.415  -4.515  -10.996 1.00 41.04  ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.485  -5.840  -10.607 1.00 41.21  ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.596  -3.866  -11.330 1.00 41.10  ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -7.718  -6.497  -10.543 1.00 41.52  ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -8.822  -4.530  -11.269 1.00 40.96  ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -8.875  -5.837  -10.883 1.00 40.54  ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -2.147  -3.954  -9.880  1.00 46.93  ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -0.731  -3.809  -10.167 1.00 49.40  ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? -0.242  -5.070  -10.877 1.00 52.22  ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -0.872  -6.127  -10.766 1.00 51.75  ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? 0.074   -3.531  -8.901  1.00 50.07  ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? -0.063  -4.564  -7.940  1.00 52.65  ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 0.846   -4.955  -11.649 1.00 54.90  ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.395   -6.111  -12.354 1.00 57.97  ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.434   -6.824  -11.529 1.00 60.84  ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 3.275   -6.183  -10.900 1.00 61.28  ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.035   -5.698  -13.689 1.00 58.49  ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 1.065   -5.366  -14.803 1.00 60.75  ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 1.791   -4.909  -16.030 1.00 61.25  ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 0.169   -6.557  -15.136 1.00 61.99  ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 2.436   -8.151  -11.592 1.00 62.73  ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 3.466   -8.956  -10.939 1.00 64.61  ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 4.445   -9.404  -12.046 1.00 67.09  ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.993   -9.944  -13.056 1.00 67.50  ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 2.845   -10.162 -10.203 1.00 64.93  ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 3.928   -10.996 -9.523  1.00 65.63  ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 1.789   -9.706  -9.200  1.00 64.86  ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.756   -9.124  -11.893 1.00 68.78  ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.809   -9.459  -12.870 1.00 70.86  ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 6.466   -9.135  -14.353 1.00 71.86  ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 6.040   -8.024  -14.693 1.00 72.24  ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 7.240   -10.929 -12.735 1.00 74.57  ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 7.791   -11.257 -11.358 1.00 81.71  ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 7.694   -12.714 -10.955 1.00 90.42  ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 6.650   -13.099 -10.378 1.00 91.90  ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 8.663   -13.469 -11.210 1.00 93.75  ? 88  GLU   A OE2 1 
ATOM   312  N  N   . GLU   B 2 8   ? -34.719 11.264  -14.898 1.00 57.58  ? 17  GLU   B N   1 
ATOM   313  C  CA  . GLU   B 2 8   ? -34.792 10.223  -15.924 1.00 58.01  ? 17  GLU   B CA  1 
ATOM   314  C  C   . GLU   B 2 8   ? -34.322 8.861   -15.419 1.00 57.60  ? 17  GLU   B C   1 
ATOM   315  O  O   . GLU   B 2 8   ? -33.172 8.711   -14.992 1.00 58.45  ? 17  GLU   B O   1 
ATOM   316  C  CB  . GLU   B 2 8   ? -34.007 10.606  -17.193 1.00 60.81  ? 17  GLU   B CB  1 
ATOM   317  C  CG  . GLU   B 2 8   ? -34.264 9.636   -18.336 1.00 66.24  ? 17  GLU   B CG  1 
ATOM   318  C  CD  . GLU   B 2 8   ? -33.564 9.945   -19.644 1.00 74.47  ? 17  GLU   B CD  1 
ATOM   319  O  OE1 . GLU   B 2 8   ? -32.513 10.623  -19.605 1.00 76.34  ? 17  GLU   B OE1 1 
ATOM   320  O  OE2 . GLU   B 2 8   ? -34.077 9.526   -20.709 1.00 77.42  ? 17  GLU   B OE2 1 
ATOM   321  N  N   A THR   B 2 9   ? -35.208 7.865   -15.465 0.50 56.73  ? 18  THR   B N   1 
ATOM   322  N  N   B THR   B 2 9   ? -35.207 7.866   -15.464 0.50 56.87  ? 18  THR   B N   1 
ATOM   323  C  CA  A THR   B 2 9   ? -34.853 6.514   -15.019 0.50 56.32  ? 18  THR   B CA  1 
ATOM   324  C  CA  B THR   B 2 9   ? -34.864 6.508   -15.036 0.50 56.57  ? 18  THR   B CA  1 
ATOM   325  C  C   A THR   B 2 9   ? -34.954 5.497   -16.169 0.50 55.28  ? 18  THR   B C   1 
ATOM   326  C  C   B THR   B 2 9   ? -34.931 5.496   -16.174 0.50 55.39  ? 18  THR   B C   1 
ATOM   327  O  O   A THR   B 2 9   ? -35.136 4.309   -15.919 0.50 55.46  ? 18  THR   B O   1 
ATOM   328  O  O   B THR   B 2 9   ? -35.074 4.304   -15.916 0.50 55.56  ? 18  THR   B O   1 
ATOM   329  C  CB  A THR   B 2 9   ? -35.643 6.076   -13.750 0.50 57.91  ? 18  THR   B CB  1 
ATOM   330  C  CB  B THR   B 2 9   ? -35.738 6.052   -13.858 0.50 58.44  ? 18  THR   B CB  1 
ATOM   331  O  OG1 A THR   B 2 9   ? -36.200 7.202   -13.051 0.50 59.21  ? 18  THR   B OG1 1 
ATOM   332  O  OG1 B THR   B 2 9   ? -37.100 6.451   -14.070 0.50 59.62  ? 18  THR   B OG1 1 
ATOM   333  C  CG2 A THR   B 2 9   ? -34.791 5.243   -12.787 0.50 58.13  ? 18  THR   B CG2 1 
ATOM   334  C  CG2 B THR   B 2 9   ? -35.220 6.560   -12.517 0.50 59.07  ? 18  THR   B CG2 1 
ATOM   335  N  N   . THR   B 2 10  ? -34.821 5.953   -17.423 1.00 54.14  ? 19  THR   B N   1 
ATOM   336  C  CA  . THR   B 2 10  ? -34.885 5.073   -18.572 1.00 52.06  ? 19  THR   B CA  1 
ATOM   337  C  C   . THR   B 2 10  ? -33.641 4.209   -18.596 1.00 49.06  ? 19  THR   B C   1 
ATOM   338  O  O   . THR   B 2 10  ? -32.543 4.708   -18.386 1.00 48.62  ? 19  THR   B O   1 
ATOM   339  C  CB  . THR   B 2 10  ? -34.980 5.905   -19.881 1.00 53.58  ? 19  THR   B CB  1 
ATOM   340  O  OG1 . THR   B 2 10  ? -36.067 6.827   -19.801 1.00 55.41  ? 19  THR   B OG1 1 
ATOM   341  C  CG2 . THR   B 2 10  ? -35.148 5.037   -21.117 1.00 53.65  ? 19  THR   B CG2 1 
ATOM   342  N  N   . ASP   B 2 11  ? -33.800 2.918   -18.898 1.00 47.14  ? 20  ASP   B N   1 
ATOM   343  C  CA  . ASP   B 2 11  ? -32.693 1.987   -19.080 1.00 46.28  ? 20  ASP   B CA  1 
ATOM   344  C  C   . ASP   B 2 11  ? -31.746 2.532   -20.173 1.00 44.58  ? 20  ASP   B C   1 
ATOM   345  O  O   . ASP   B 2 11  ? -32.217 3.159   -21.122 1.00 44.31  ? 20  ASP   B O   1 
ATOM   346  C  CB  . ASP   B 2 11  ? -33.243 0.632   -19.559 1.00 48.42  ? 20  ASP   B CB  1 
ATOM   347  C  CG  . ASP   B 2 11  ? -33.443 -0.386  -18.463 1.00 54.16  ? 20  ASP   B CG  1 
ATOM   348  O  OD1 . ASP   B 2 11  ? -33.868 0.013   -17.356 1.00 53.95  ? 20  ASP   B OD1 1 
ATOM   349  O  OD2 . ASP   B 2 11  ? -33.159 -1.591  -18.710 1.00 57.27  ? 20  ASP   B OD2 1 
ATOM   350  N  N   . GLY   B 2 12  ? -30.445 2.339   -20.005 1.00 42.62  ? 21  GLY   B N   1 
ATOM   351  C  CA  . GLY   B 2 12  ? -29.475 2.835   -20.966 1.00 41.07  ? 21  GLY   B CA  1 
ATOM   352  C  C   . GLY   B 2 12  ? -28.154 3.221   -20.338 1.00 40.15  ? 21  GLY   B C   1 
ATOM   353  O  O   . GLY   B 2 12  ? -27.927 2.994   -19.143 1.00 40.41  ? 21  GLY   B O   1 
ATOM   354  N  N   . VAL   B 2 13  ? -27.263 3.800   -21.150 1.00 38.64  ? 22  VAL   B N   1 
ATOM   355  C  CA  . VAL   B 2 13  ? -25.948 4.236   -20.707 1.00 37.59  ? 22  VAL   B CA  1 
ATOM   356  C  C   . VAL   B 2 13  ? -25.956 5.750   -20.492 1.00 37.55  ? 22  VAL   B C   1 
ATOM   357  O  O   . VAL   B 2 13  ? -26.610 6.467   -21.234 1.00 37.76  ? 22  VAL   B O   1 
ATOM   358  C  CB  . VAL   B 2 13  ? -24.828 3.725   -21.634 1.00 37.31  ? 22  VAL   B CB  1 
ATOM   359  C  CG1 . VAL   B 2 13  ? -25.007 4.190   -23.098 1.00 36.85  ? 22  VAL   B CG1 1 
ATOM   360  C  CG2 . VAL   B 2 13  ? -23.453 4.065   -21.093 1.00 37.73  ? 22  VAL   B CG2 1 
ATOM   361  N  N   . TYR   B 2 14  ? -25.347 6.222   -19.403 1.00 37.52  ? 23  TYR   B N   1 
ATOM   362  C  CA  . TYR   B 2 14  ? -25.371 7.634   -19.038 1.00 37.64  ? 23  TYR   B CA  1 
ATOM   363  C  C   . TYR   B 2 14  ? -23.970 8.179   -18.772 1.00 37.96  ? 23  TYR   B C   1 
ATOM   364  O  O   . TYR   B 2 14  ? -23.133 7.480   -18.230 1.00 37.94  ? 23  TYR   B O   1 
ATOM   365  C  CB  . TYR   B 2 14  ? -26.207 7.834   -17.747 1.00 37.11  ? 23  TYR   B CB  1 
ATOM   366  C  CG  . TYR   B 2 14  ? -27.706 7.692   -17.923 1.00 37.21  ? 23  TYR   B CG  1 
ATOM   367  C  CD1 . TYR   B 2 14  ? -28.277 6.469   -18.230 1.00 37.64  ? 23  TYR   B CD1 1 
ATOM   368  C  CD2 . TYR   B 2 14  ? -28.560 8.762   -17.682 1.00 38.27  ? 23  TYR   B CD2 1 
ATOM   369  C  CE1 . TYR   B 2 14  ? -29.644 6.337   -18.424 1.00 38.62  ? 23  TYR   B CE1 1 
ATOM   370  C  CE2 . TYR   B 2 14  ? -29.938 8.643   -17.868 1.00 39.17  ? 23  TYR   B CE2 1 
ATOM   371  C  CZ  . TYR   B 2 14  ? -30.475 7.421   -18.232 1.00 40.08  ? 23  TYR   B CZ  1 
ATOM   372  O  OH  . TYR   B 2 14  ? -31.832 7.244   -18.364 1.00 41.93  ? 23  TYR   B OH  1 
ATOM   373  N  N   . ARG   B 2 15  ? -23.755 9.457   -19.054 1.00 38.01  ? 24  ARG   B N   1 
ATOM   374  C  CA  . ARG   B 2 15  ? -22.508 10.126  -18.722 1.00 38.14  ? 24  ARG   B CA  1 
ATOM   375  C  C   . ARG   B 2 15  ? -22.648 10.644  -17.298 1.00 38.17  ? 24  ARG   B C   1 
ATOM   376  O  O   . ARG   B 2 15  ? -23.719 11.074  -16.919 1.00 38.09  ? 24  ARG   B O   1 
ATOM   377  C  CB  . ARG   B 2 15  ? -22.275 11.329  -19.651 1.00 39.31  ? 24  ARG   B CB  1 
ATOM   378  C  CG  . ARG   B 2 15  ? -22.266 11.026  -21.148 1.00 41.37  ? 24  ARG   B CG  1 
ATOM   379  C  CD  . ARG   B 2 15  ? -21.882 12.275  -21.929 1.00 43.89  ? 24  ARG   B CD  1 
ATOM   380  N  NE  . ARG   B 2 15  ? -22.116 12.108  -23.368 1.00 45.81  ? 24  ARG   B NE  1 
ATOM   381  C  CZ  . ARG   B 2 15  ? -21.195 11.705  -24.236 1.00 47.99  ? 24  ARG   B CZ  1 
ATOM   382  N  NH1 . ARG   B 2 15  ? -19.953 11.461  -23.833 1.00 47.87  ? 24  ARG   B NH1 1 
ATOM   383  N  NH2 . ARG   B 2 15  ? -21.506 11.543  -25.515 1.00 48.81  ? 24  ARG   B NH2 1 
ATOM   384  N  N   . VAL   B 2 16  ? -21.565 10.636  -16.521 1.00 38.10  ? 25  VAL   B N   1 
ATOM   385  C  CA  . VAL   B 2 16  ? -21.504 11.192  -15.176 1.00 38.25  ? 25  VAL   B CA  1 
ATOM   386  C  C   . VAL   B 2 16  ? -20.649 12.460  -15.292 1.00 38.74  ? 25  VAL   B C   1 
ATOM   387  O  O   . VAL   B 2 16  ? -19.471 12.386  -15.624 1.00 38.81  ? 25  VAL   B O   1 
ATOM   388  C  CB  . VAL   B 2 16  ? -20.901 10.189  -14.162 1.00 38.59  ? 25  VAL   B CB  1 
ATOM   389  C  CG1 . VAL   B 2 16  ? -20.903 10.780  -12.756 1.00 38.59  ? 25  VAL   B CG1 1 
ATOM   390  C  CG2 . VAL   B 2 16  ? -21.653 8.860   -14.198 1.00 38.72  ? 25  VAL   B CG2 1 
ATOM   391  N  N   . MET   B 2 17  ? -21.248 13.612  -15.063 1.00 39.46  ? 26  MET   B N   1 
ATOM   392  C  CA  . MET   B 2 17  ? -20.612 14.913  -15.244 1.00 40.95  ? 26  MET   B CA  1 
ATOM   393  C  C   . MET   B 2 17  ? -20.445 15.690  -13.947 1.00 43.36  ? 26  MET   B C   1 
ATOM   394  O  O   . MET   B 2 17  ? -21.190 15.476  -12.997 1.00 44.18  ? 26  MET   B O   1 
ATOM   395  C  CB  . MET   B 2 17  ? -21.479 15.771  -16.195 1.00 40.77  ? 26  MET   B CB  1 
ATOM   396  C  CG  . MET   B 2 17  ? -21.955 15.065  -17.460 1.00 41.60  ? 26  MET   B CG  1 
ATOM   397  S  SD  . MET   B 2 17  ? -20.627 14.804  -18.651 1.00 45.59  ? 26  MET   B SD  1 
ATOM   398  C  CE  . MET   B 2 17  ? -20.159 16.484  -18.966 1.00 40.32  ? 26  MET   B CE  1 
ATOM   399  N  N   . THR   B 2 18  ? -19.527 16.655  -13.937 1.00 44.92  ? 27  THR   B N   1 
ATOM   400  C  CA  . THR   B 2 18  ? -19.341 17.571  -12.818 1.00 47.35  ? 27  THR   B CA  1 
ATOM   401  C  C   . THR   B 2 18  ? -19.183 19.031  -13.311 1.00 49.82  ? 27  THR   B C   1 
ATOM   402  O  O   . THR   B 2 18  ? -18.615 19.280  -14.381 1.00 49.32  ? 27  THR   B O   1 
ATOM   403  C  CB  . THR   B 2 18  ? -18.155 17.156  -11.917 1.00 48.79  ? 27  THR   B CB  1 
ATOM   404  O  OG1 . THR   B 2 18  ? -18.156 18.007  -10.768 1.00 50.27  ? 27  THR   B OG1 1 
ATOM   405  C  CG2 . THR   B 2 18  ? -16.805 17.272  -12.619 1.00 48.95  ? 27  THR   B CG2 1 
ATOM   406  N  N   . ARG   B 2 19  ? -19.672 19.992  -12.516 1.00 52.02  ? 28  ARG   B N   1 
ATOM   407  C  CA  . ARG   B 2 19  ? -19.484 21.411  -12.821 1.00 54.97  ? 28  ARG   B CA  1 
ATOM   408  C  C   . ARG   B 2 19  ? -18.479 22.108  -11.844 1.00 56.94  ? 28  ARG   B C   1 
ATOM   409  O  O   . ARG   B 2 19  ? -18.259 23.318  -11.933 1.00 56.86  ? 28  ARG   B O   1 
ATOM   410  C  CB  . ARG   B 2 19  ? -20.832 22.149  -12.875 1.00 57.52  ? 28  ARG   B CB  1 
ATOM   411  C  CG  . ARG   B 2 19  ? -21.679 21.740  -14.072 1.00 62.21  ? 28  ARG   B CG  1 
ATOM   412  C  CD  . ARG   B 2 19  ? -22.596 22.855  -14.533 1.00 66.99  ? 28  ARG   B CD  1 
ATOM   413  N  NE  . ARG   B 2 19  ? -23.600 22.388  -15.494 1.00 71.49  ? 28  ARG   B NE  1 
ATOM   414  C  CZ  . ARG   B 2 19  ? -24.793 21.900  -15.159 1.00 74.96  ? 28  ARG   B CZ  1 
ATOM   415  N  NH1 . ARG   B 2 19  ? -25.148 21.807  -13.879 1.00 75.00  ? 28  ARG   B NH1 1 
ATOM   416  N  NH2 . ARG   B 2 19  ? -25.641 21.501  -16.099 1.00 74.97  ? 28  ARG   B NH2 1 
ATOM   417  N  N   . ARG   B 2 20  ? -17.866 21.323  -10.936 1.00 58.57  ? 29  ARG   B N   1 
ATOM   418  C  CA  . ARG   B 2 20  ? -16.901 21.739  -9.908  1.00 60.55  ? 29  ARG   B CA  1 
ATOM   419  C  C   . ARG   B 2 20  ? -15.608 22.309  -10.514 1.00 61.19  ? 29  ARG   B C   1 
ATOM   420  O  O   . ARG   B 2 20  ? -14.979 23.218  -9.949  1.00 61.57  ? 29  ARG   B O   1 
ATOM   421  C  CB  . ARG   B 2 20  ? -16.593 20.535  -8.993  1.00 63.07  ? 29  ARG   B CB  1 
ATOM   422  C  CG  . ARG   B 2 20  ? -15.617 20.827  -7.868  1.00 68.12  ? 29  ARG   B CG  1 
ATOM   423  C  CD  . ARG   B 2 20  ? -15.330 19.584  -7.048  1.00 72.87  ? 29  ARG   B CD  1 
ATOM   424  N  NE  . ARG   B 2 20  ? -14.410 18.657  -7.712  1.00 76.68  ? 29  ARG   B NE  1 
ATOM   425  C  CZ  . ARG   B 2 20  ? -13.086 18.695  -7.583  1.00 80.03  ? 29  ARG   B CZ  1 
ATOM   426  N  NH1 . ARG   B 2 20  ? -12.508 19.639  -6.847  1.00 80.49  ? 29  ARG   B NH1 1 
ATOM   427  N  NH2 . ARG   B 2 20  ? -12.326 17.806  -8.213  1.00 79.84  ? 29  ARG   B NH2 1 
ATOM   428  N  N   . LEU   B 2 21  ? -15.232 21.785  -11.677 1.00 61.03  ? 30  LEU   B N   1 
ATOM   429  C  CA  . LEU   B 2 21  ? -14.043 22.195  -12.403 1.00 61.30  ? 30  LEU   B CA  1 
ATOM   430  C  C   . LEU   B 2 21  ? -14.398 23.216  -13.518 1.00 61.01  ? 30  LEU   B C   1 
ATOM   431  O  O   . LEU   B 2 21  ? -15.492 23.800  -13.486 1.00 61.48  ? 30  LEU   B O   1 
ATOM   432  C  CB  . LEU   B 2 21  ? -13.367 20.909  -12.944 1.00 61.66  ? 30  LEU   B CB  1 
ATOM   433  C  CG  . LEU   B 2 21  ? -12.271 20.218  -12.098 1.00 63.07  ? 30  LEU   B CG  1 
ATOM   434  C  CD1 . LEU   B 2 21  ? -12.403 20.475  -10.592 1.00 63.73  ? 30  LEU   B CD1 1 
ATOM   435  C  CD2 . LEU   B 2 21  ? -12.228 18.734  -12.383 1.00 63.64  ? 30  LEU   B CD2 1 
ATOM   436  N  N   . LEU   B 2 22  ? -13.469 23.476  -14.469 1.00 60.09  ? 31  LEU   B N   1 
ATOM   437  C  CA  . LEU   B 2 22  ? -13.711 24.402  -15.575 1.00 59.41  ? 31  LEU   B CA  1 
ATOM   438  C  C   . LEU   B 2 22  ? -14.786 23.822  -16.474 1.00 58.61  ? 31  LEU   B C   1 
ATOM   439  O  O   . LEU   B 2 22  ? -14.670 22.665  -16.884 1.00 58.47  ? 31  LEU   B O   1 
ATOM   440  C  CB  . LEU   B 2 22  ? -12.435 24.578  -16.391 1.00 59.34  ? 31  LEU   B CB  1 
ATOM   441  C  CG  . LEU   B 2 22  ? -12.531 25.634  -17.449 1.00 60.44  ? 31  LEU   B CG  1 
ATOM   442  C  CD1 . LEU   B 2 22  ? -12.154 26.993  -16.896 1.00 60.22  ? 31  LEU   B CD1 1 
ATOM   443  C  CD2 . LEU   B 2 22  ? -11.704 25.253  -18.652 1.00 61.37  ? 31  LEU   B CD2 1 
ATOM   444  N  N   . GLY   B 2 23  ? -15.828 24.608  -16.755 1.00 57.68  ? 32  GLY   B N   1 
ATOM   445  C  CA  . GLY   B 2 23  ? -16.947 24.167  -17.584 1.00 56.99  ? 32  GLY   B CA  1 
ATOM   446  C  C   . GLY   B 2 23  ? -17.593 22.877  -17.103 1.00 55.97  ? 32  GLY   B C   1 
ATOM   447  O  O   . GLY   B 2 23  ? -17.624 22.598  -15.900 1.00 55.81  ? 32  GLY   B O   1 
ATOM   448  N  N   . SER   B 2 24  ? -18.088 22.065  -18.044 1.00 55.01  ? 33  SER   B N   1 
ATOM   449  C  CA  . SER   B 2 24  ? -18.689 20.770  -17.726 1.00 54.07  ? 33  SER   B CA  1 
ATOM   450  C  C   . SER   B 2 24  ? -17.674 19.679  -18.034 1.00 52.29  ? 33  SER   B C   1 
ATOM   451  O  O   . SER   B 2 24  ? -17.194 19.590  -19.164 1.00 52.20  ? 33  SER   B O   1 
ATOM   452  C  CB  . SER   B 2 24  ? -19.962 20.555  -18.538 1.00 55.72  ? 33  SER   B CB  1 
ATOM   453  O  OG  . SER   B 2 24  ? -21.026 21.319  -17.993 1.00 58.44  ? 33  SER   B OG  1 
ATOM   454  N  N   . THR   B 2 25  ? -17.325 18.863  -17.029 1.00 50.58  ? 34  THR   B N   1 
ATOM   455  C  CA  . THR   B 2 25  ? -16.323 17.824  -17.215 1.00 49.66  ? 34  THR   B CA  1 
ATOM   456  C  C   . THR   B 2 25  ? -16.893 16.433  -16.988 1.00 48.24  ? 34  THR   B C   1 
ATOM   457  O  O   . THR   B 2 25  ? -17.562 16.213  -15.985 1.00 48.36  ? 34  THR   B O   1 
ATOM   458  C  CB  . THR   B 2 25  ? -15.125 18.080  -16.278 1.00 51.08  ? 34  THR   B CB  1 
ATOM   459  O  OG1 . THR   B 2 25  ? -14.666 19.434  -16.434 1.00 52.59  ? 34  THR   B OG1 1 
ATOM   460  C  CG2 . THR   B 2 25  ? -13.985 17.115  -16.527 1.00 51.05  ? 34  THR   B CG2 1 
ATOM   461  N  N   . GLN   B 2 26  ? -16.602 15.482  -17.891 1.00 46.42  ? 35  GLN   B N   1 
ATOM   462  C  CA  . GLN   B 2 26  ? -17.074 14.112  -17.724 1.00 45.16  ? 35  GLN   B CA  1 
ATOM   463  C  C   . GLN   B 2 26  ? -16.089 13.304  -16.874 1.00 45.02  ? 35  GLN   B C   1 
ATOM   464  O  O   . GLN   B 2 26  ? -14.965 13.072  -17.305 1.00 45.79  ? 35  GLN   B O   1 
ATOM   465  C  CB  . GLN   B 2 26  ? -17.287 13.423  -19.079 1.00 44.15  ? 35  GLN   B CB  1 
ATOM   466  C  CG  . GLN   B 2 26  ? -17.802 11.995  -18.936 1.00 44.28  ? 35  GLN   B CG  1 
ATOM   467  C  CD  . GLN   B 2 26  ? -18.070 11.362  -20.268 1.00 45.66  ? 35  GLN   B CD  1 
ATOM   468  O  OE1 . GLN   B 2 26  ? -18.701 11.964  -21.144 1.00 46.14  ? 35  GLN   B OE1 1 
ATOM   469  N  NE2 . GLN   B 2 26  ? -17.587 10.140  -20.456 1.00 44.39  ? 35  GLN   B NE2 1 
ATOM   470  N  N   . VAL   B 2 27  ? -16.507 12.884  -15.679 1.00 43.78  ? 36  VAL   B N   1 
ATOM   471  C  CA  . VAL   B 2 27  ? -15.691 12.086  -14.758 1.00 42.49  ? 36  VAL   B CA  1 
ATOM   472  C  C   . VAL   B 2 27  ? -15.840 10.559  -15.001 1.00 41.58  ? 36  VAL   B C   1 
ATOM   473  O  O   . VAL   B 2 27  ? -14.941 9.764   -14.677 1.00 41.28  ? 36  VAL   B O   1 
ATOM   474  C  CB  . VAL   B 2 27  ? -15.987 12.457  -13.276 1.00 42.95  ? 36  VAL   B CB  1 
ATOM   475  C  CG1 . VAL   B 2 27  ? -15.705 13.927  -13.013 1.00 43.86  ? 36  VAL   B CG1 1 
ATOM   476  C  CG2 . VAL   B 2 27  ? -17.414 12.118  -12.875 1.00 42.78  ? 36  VAL   B CG2 1 
ATOM   477  N  N   . GLY   B 2 28  ? -16.979 10.164  -15.557 1.00 40.35  ? 37  GLY   B N   1 
ATOM   478  C  CA  . GLY   B 2 28  ? -17.250 8.765   -15.801 1.00 39.11  ? 37  GLY   B CA  1 
ATOM   479  C  C   . GLY   B 2 28  ? -18.540 8.534   -16.536 1.00 37.58  ? 37  GLY   B C   1 
ATOM   480  O  O   . GLY   B 2 28  ? -19.099 9.439   -17.147 1.00 36.45  ? 37  GLY   B O   1 
ATOM   481  N  N   . VAL   B 2 29  ? -19.003 7.288   -16.471 1.00 37.38  ? 38  VAL   B N   1 
ATOM   482  C  CA  . VAL   B 2 29  ? -20.146 6.717   -17.174 1.00 37.30  ? 38  VAL   B CA  1 
ATOM   483  C  C   . VAL   B 2 29  ? -20.791 5.688   -16.234 1.00 37.60  ? 38  VAL   B C   1 
ATOM   484  O  O   . VAL   B 2 29  ? -20.134 5.142   -15.334 1.00 38.47  ? 38  VAL   B O   1 
ATOM   485  C  CB  . VAL   B 2 29  ? -19.638 5.988   -18.485 1.00 37.34  ? 38  VAL   B CB  1 
ATOM   486  C  CG1 . VAL   B 2 29  ? -20.775 5.343   -19.267 1.00 37.66  ? 38  VAL   B CG1 1 
ATOM   487  C  CG2 . VAL   B 2 29  ? -18.818 6.900   -19.394 1.00 37.06  ? 38  VAL   B CG2 1 
ATOM   488  N  N   . GLY   B 2 30  ? -22.048 5.374   -16.489 1.00 36.53  ? 39  GLY   B N   1 
ATOM   489  C  CA  . GLY   B 2 30  ? -22.743 4.339   -15.742 1.00 36.23  ? 39  GLY   B CA  1 
ATOM   490  C  C   . GLY   B 2 30  ? -23.910 3.752   -16.501 1.00 36.00  ? 39  GLY   B C   1 
ATOM   491  O  O   . GLY   B 2 30  ? -24.304 4.273   -17.552 1.00 35.74  ? 39  GLY   B O   1 
ATOM   492  N  N   . VAL   B 2 31  ? -24.482 2.667   -15.960 1.00 35.67  ? 40  VAL   B N   1 
ATOM   493  C  CA  . VAL   B 2 31  ? -25.609 1.949   -16.553 1.00 35.94  ? 40  VAL   B CA  1 
ATOM   494  C  C   . VAL   B 2 31  ? -26.874 2.089   -15.725 1.00 35.86  ? 40  VAL   B C   1 
ATOM   495  O  O   . VAL   B 2 31  ? -26.856 1.813   -14.537 1.00 35.58  ? 40  VAL   B O   1 
ATOM   496  C  CB  . VAL   B 2 31  ? -25.268 0.452   -16.746 1.00 36.67  ? 40  VAL   B CB  1 
ATOM   497  C  CG1 . VAL   B 2 31  ? -26.481 -0.346  -17.209 1.00 36.72  ? 40  VAL   B CG1 1 
ATOM   498  C  CG2 . VAL   B 2 31  ? -24.100 0.276   -17.708 1.00 37.59  ? 40  VAL   B CG2 1 
ATOM   499  N  N   . MET   B 2 32  ? -27.992 2.412   -16.367 1.00 35.70  ? 41  MET   B N   1 
ATOM   500  C  CA  . MET   B 2 32  ? -29.279 2.469   -15.696 1.00 36.17  ? 41  MET   B CA  1 
ATOM   501  C  C   . MET   B 2 32  ? -30.020 1.188   -16.087 1.00 37.80  ? 41  MET   B C   1 
ATOM   502  O  O   . MET   B 2 32  ? -30.208 0.918   -17.275 1.00 38.20  ? 41  MET   B O   1 
ATOM   503  C  CB  . MET   B 2 32  ? -30.060 3.724   -16.121 1.00 35.58  ? 41  MET   B CB  1 
ATOM   504  C  CG  . MET   B 2 32  ? -31.287 4.008   -15.287 1.00 37.57  ? 41  MET   B CG  1 
ATOM   505  S  SD  . MET   B 2 32  ? -30.978 4.548   -13.566 1.00 42.18  ? 41  MET   B SD  1 
ATOM   506  C  CE  . MET   B 2 32  ? -30.526 6.230   -13.860 1.00 40.27  ? 41  MET   B CE  1 
ATOM   507  N  N   . GLN   B 2 33  ? -30.338 0.343   -15.106 1.00 38.33  ? 42  GLN   B N   1 
ATOM   508  C  CA  . GLN   B 2 33  ? -31.048 -0.906  -15.384 1.00 39.11  ? 42  GLN   B CA  1 
ATOM   509  C  C   . GLN   B 2 33  ? -31.965 -1.194  -14.229 1.00 39.97  ? 42  GLN   B C   1 
ATOM   510  O  O   . GLN   B 2 33  ? -31.550 -1.058  -13.077 1.00 40.74  ? 42  GLN   B O   1 
ATOM   511  C  CB  . GLN   B 2 33  ? -30.078 -2.077  -15.612 1.00 41.17  ? 42  GLN   B CB  1 
ATOM   512  C  CG  . GLN   B 2 33  ? -30.820 -3.351  -16.016 1.00 47.42  ? 42  GLN   B CG  1 
ATOM   513  C  CD  . GLN   B 2 33  ? -29.920 -4.465  -16.484 1.00 53.76  ? 42  GLN   B CD  1 
ATOM   514  O  OE1 . GLN   B 2 33  ? -29.949 -5.589  -15.952 1.00 56.77  ? 42  GLN   B OE1 1 
ATOM   515  N  NE2 . GLN   B 2 33  ? -29.090 -4.185  -17.479 1.00 53.63  ? 42  GLN   B NE2 1 
ATOM   516  N  N   . GLU   B 2 34  ? -33.224 -1.520  -14.513 1.00 39.96  ? 43  GLU   B N   1 
ATOM   517  C  CA  . GLU   B 2 34  ? -34.205 -1.827  -13.479 1.00 40.66  ? 43  GLU   B CA  1 
ATOM   518  C  C   . GLU   B 2 34  ? -34.296 -0.774  -12.351 1.00 40.80  ? 43  GLU   B C   1 
ATOM   519  O  O   . GLU   B 2 34  ? -34.370 -1.132  -11.178 1.00 41.42  ? 43  GLU   B O   1 
ATOM   520  C  CB  . GLU   B 2 34  ? -33.949 -3.231  -12.906 1.00 43.57  ? 43  GLU   B CB  1 
ATOM   521  C  CG  . GLU   B 2 34  ? -34.058 -4.330  -13.952 1.00 47.83  ? 43  GLU   B CG  1 
ATOM   522  C  CD  . GLU   B 2 34  ? -33.413 -5.659  -13.590 1.00 54.12  ? 43  GLU   B CD  1 
ATOM   523  O  OE1 . GLU   B 2 34  ? -33.659 -6.159  -12.471 1.00 54.84  ? 43  GLU   B OE1 1 
ATOM   524  O  OE2 . GLU   B 2 34  ? -32.673 -6.213  -14.435 1.00 57.21  ? 43  GLU   B OE2 1 
ATOM   525  N  N   . GLY   B 2 35  ? -34.261 0.506   -12.717 1.00 39.74  ? 44  GLY   B N   1 
ATOM   526  C  CA  . GLY   B 2 35  ? -34.371 1.602   -11.760 1.00 39.12  ? 44  GLY   B CA  1 
ATOM   527  C  C   . GLY   B 2 35  ? -33.144 1.861   -10.912 1.00 38.16  ? 44  GLY   B C   1 
ATOM   528  O  O   . GLY   B 2 35  ? -33.185 2.704   -10.013 1.00 38.67  ? 44  GLY   B O   1 
ATOM   529  N  N   . VAL   B 2 36  ? -32.034 1.152   -11.190 1.00 36.26  ? 45  VAL   B N   1 
ATOM   530  C  CA  . VAL   B 2 36  ? -30.799 1.277   -10.429 1.00 34.71  ? 45  VAL   B CA  1 
ATOM   531  C  C   . VAL   B 2 36  ? -29.683 1.819   -11.315 1.00 33.77  ? 45  VAL   B C   1 
ATOM   532  O  O   . VAL   B 2 36  ? -29.495 1.342   -12.446 1.00 33.45  ? 45  VAL   B O   1 
ATOM   533  C  CB  . VAL   B 2 36  ? -30.426 -0.079  -9.738  1.00 35.10  ? 45  VAL   B CB  1 
ATOM   534  C  CG1 . VAL   B 2 36  ? -29.014 -0.065  -9.155  1.00 35.29  ? 45  VAL   B CG1 1 
ATOM   535  C  CG2 . VAL   B 2 36  ? -31.424 -0.410  -8.643  1.00 35.73  ? 45  VAL   B CG2 1 
ATOM   536  N  N   . PHE   B 2 37  ? -28.971 2.853   -10.826 1.00 32.86  ? 46  PHE   B N   1 
ATOM   537  C  CA  . PHE   B 2 37  ? -27.851 3.386   -11.584 1.00 32.73  ? 46  PHE   B CA  1 
ATOM   538  C  C   . PHE   B 2 37  ? -26.584 2.662   -11.095 1.00 31.83  ? 46  PHE   B C   1 
ATOM   539  O  O   . PHE   B 2 37  ? -26.372 2.575   -9.902  1.00 31.54  ? 46  PHE   B O   1 
ATOM   540  C  CB  . PHE   B 2 37  ? -27.746 4.910   -11.409 1.00 32.41  ? 46  PHE   B CB  1 
ATOM   541  C  CG  . PHE   B 2 37  ? -26.719 5.497   -12.343 1.00 33.14  ? 46  PHE   B CG  1 
ATOM   542  C  CD1 . PHE   B 2 37  ? -26.916 5.479   -13.714 1.00 33.52  ? 46  PHE   B CD1 1 
ATOM   543  C  CD2 . PHE   B 2 37  ? -25.530 6.010   -11.858 1.00 33.85  ? 46  PHE   B CD2 1 
ATOM   544  C  CE1 . PHE   B 2 37  ? -25.976 6.035   -14.579 1.00 34.14  ? 46  PHE   B CE1 1 
ATOM   545  C  CE2 . PHE   B 2 37  ? -24.581 6.534   -12.725 1.00 34.35  ? 46  PHE   B CE2 1 
ATOM   546  C  CZ  . PHE   B 2 37  ? -24.802 6.526   -14.083 1.00 33.95  ? 46  PHE   B CZ  1 
ATOM   547  N  N   . HIS   B 2 38  ? -25.783 2.104   -11.993 1.00 31.71  ? 47  HIS   B N   1 
ATOM   548  C  CA  . HIS   B 2 38  ? -24.571 1.364   -11.641 1.00 31.83  ? 47  HIS   B CA  1 
ATOM   549  C  C   . HIS   B 2 38  ? -23.358 2.071   -12.232 1.00 32.67  ? 47  HIS   B C   1 
ATOM   550  O  O   . HIS   B 2 38  ? -23.320 2.310   -13.428 1.00 31.77  ? 47  HIS   B O   1 
ATOM   551  C  CB  . HIS   B 2 38  ? -24.603 -0.060  -12.238 1.00 32.01  ? 47  HIS   B CB  1 
ATOM   552  C  CG  . HIS   B 2 38  ? -25.844 -0.853  -11.959 1.00 34.78  ? 47  HIS   B CG  1 
ATOM   553  N  ND1 . HIS   B 2 38  ? -27.078 -0.498  -12.502 1.00 36.11  ? 47  HIS   B ND1 1 
ATOM   554  C  CD2 . HIS   B 2 38  ? -25.993 -2.003  -11.262 1.00 36.13  ? 47  HIS   B CD2 1 
ATOM   555  C  CE1 . HIS   B 2 38  ? -27.933 -1.417  -12.083 1.00 36.04  ? 47  HIS   B CE1 1 
ATOM   556  N  NE2 . HIS   B 2 38  ? -27.329 -2.331  -11.322 1.00 37.15  ? 47  HIS   B NE2 1 
ATOM   557  N  N   . THR   B 2 39  ? -22.324 2.328   -11.422 1.00 33.80  ? 48  THR   B N   1 
ATOM   558  C  CA  . THR   B 2 39  ? -21.082 2.910   -11.934 1.00 34.16  ? 48  THR   B CA  1 
ATOM   559  C  C   . THR   B 2 39  ? -19.871 2.347   -11.130 1.00 34.41  ? 48  THR   B C   1 
ATOM   560  O  O   . THR   B 2 39  ? -20.033 1.445   -10.302 1.00 33.32  ? 48  THR   B O   1 
ATOM   561  C  CB  . THR   B 2 39  ? -21.198 4.457   -11.997 1.00 35.07  ? 48  THR   B CB  1 
ATOM   562  O  OG1 . THR   B 2 39  ? -20.057 4.953   -12.692 1.00 36.27  ? 48  THR   B OG1 1 
ATOM   563  C  CG2 . THR   B 2 39  ? -21.290 5.093   -10.613 1.00 35.44  ? 48  THR   B CG2 1 
ATOM   564  N  N   . MET   B 2 40  ? -18.655 2.859   -11.392 1.00 35.24  ? 49  MET   B N   1 
ATOM   565  C  CA  . MET   B 2 40  ? -17.472 2.473   -10.643 1.00 35.43  ? 49  MET   B CA  1 
ATOM   566  C  C   . MET   B 2 40  ? -17.277 3.451   -9.475  1.00 35.63  ? 49  MET   B C   1 
ATOM   567  O  O   . MET   B 2 40  ? -17.563 4.640   -9.607  1.00 36.38  ? 49  MET   B O   1 
ATOM   568  C  CB  . MET   B 2 40  ? -16.247 2.426   -11.563 1.00 36.02  ? 49  MET   B CB  1 
ATOM   569  C  CG  . MET   B 2 40  ? -16.485 1.583   -12.793 1.00 38.45  ? 49  MET   B CG  1 
ATOM   570  S  SD  . MET   B 2 40  ? -14.973 0.911   -13.516 1.00 39.93  ? 49  MET   B SD  1 
ATOM   571  C  CE  . MET   B 2 40  ? -14.727 -0.477  -12.495 1.00 38.13  ? 49  MET   B CE  1 
ATOM   572  N  N   . TRP   B 2 41  ? -16.801 2.950   -8.331  1.00 35.07  ? 50  TRP   B N   1 
ATOM   573  C  CA  A TRP   B 2 41  ? -16.611 3.771   -7.140  0.50 35.83  ? 50  TRP   B CA  1 
ATOM   574  C  CA  B TRP   B 2 41  ? -16.598 3.754   -7.135  0.50 34.82  ? 50  TRP   B CA  1 
ATOM   575  C  C   . TRP   B 2 41  ? -15.675 4.950   -7.370  1.00 35.87  ? 50  TRP   B C   1 
ATOM   576  O  O   . TRP   B 2 41  ? -15.939 6.026   -6.855  1.00 35.84  ? 50  TRP   B O   1 
ATOM   577  C  CB  A TRP   B 2 41  ? -16.124 2.934   -5.940  0.50 36.16  ? 50  TRP   B CB  1 
ATOM   578  C  CB  B TRP   B 2 41  ? -16.055 2.892   -5.976  0.50 33.69  ? 50  TRP   B CB  1 
ATOM   579  C  CG  A TRP   B 2 41  ? -16.262 3.649   -4.627  0.50 37.43  ? 50  TRP   B CG  1 
ATOM   580  C  CG  B TRP   B 2 41  ? -15.897 3.668   -4.707  0.50 32.96  ? 50  TRP   B CG  1 
ATOM   581  C  CD1 A TRP   B 2 41  ? -17.355 3.659   -3.814  0.50 38.45  ? 50  TRP   B CD1 1 
ATOM   582  C  CD1 B TRP   B 2 41  ? -14.840 4.449   -4.347  0.50 33.46  ? 50  TRP   B CD1 1 
ATOM   583  C  CD2 A TRP   B 2 41  ? -15.291 4.503   -4.005  0.50 38.03  ? 50  TRP   B CD2 1 
ATOM   584  C  CD2 B TRP   B 2 41  ? -16.876 3.819   -3.681  0.50 32.42  ? 50  TRP   B CD2 1 
ATOM   585  N  NE1 A TRP   B 2 41  ? -17.119 4.450   -2.715  0.50 39.10  ? 50  TRP   B NE1 1 
ATOM   586  N  NE1 B TRP   B 2 41  ? -15.094 5.065   -3.150  0.50 33.48  ? 50  TRP   B NE1 1 
ATOM   587  C  CE2 A TRP   B 2 41  ? -15.862 4.988   -2.812  0.50 38.98  ? 50  TRP   B CE2 1 
ATOM   588  C  CE2 B TRP   B 2 41  ? -16.337 4.691   -2.714  0.50 33.06  ? 50  TRP   B CE2 1 
ATOM   589  C  CE3 A TRP   B 2 41  ? -13.991 4.904   -4.339  0.50 39.07  ? 50  TRP   B CE3 1 
ATOM   590  C  CE3 B TRP   B 2 41  ? -18.151 3.289   -3.475  0.50 32.77  ? 50  TRP   B CE3 1 
ATOM   591  C  CZ2 A TRP   B 2 41  ? -15.182 5.853   -1.956  0.50 39.96  ? 50  TRP   B CZ2 1 
ATOM   592  C  CZ2 B TRP   B 2 41  ? -17.033 5.051   -1.565  0.50 33.26  ? 50  TRP   B CZ2 1 
ATOM   593  C  CZ3 A TRP   B 2 41  ? -13.317 5.759   -3.486  0.50 40.24  ? 50  TRP   B CZ3 1 
ATOM   594  C  CZ3 B TRP   B 2 41  ? -18.819 3.611   -2.312  0.50 33.47  ? 50  TRP   B CZ3 1 
ATOM   595  C  CH2 A TRP   B 2 41  ? -13.902 6.202   -2.298  0.50 40.29  ? 50  TRP   B CH2 1 
ATOM   596  C  CH2 B TRP   B 2 41  ? -18.266 4.496   -1.380  0.50 33.35  ? 50  TRP   B CH2 1 
ATOM   597  N  N   . HIS   B 2 42  ? -14.560 4.744   -8.081  1.00 36.28  ? 51  HIS   B N   1 
ATOM   598  C  CA  . HIS   B 2 42  ? -13.600 5.827   -8.295  1.00 36.69  ? 51  HIS   B CA  1 
ATOM   599  C  C   . HIS   B 2 42  ? -14.163 7.024   -9.102  1.00 36.92  ? 51  HIS   B C   1 
ATOM   600  O  O   . HIS   B 2 42  ? -13.574 8.099   -9.057  1.00 36.80  ? 51  HIS   B O   1 
ATOM   601  C  CB  . HIS   B 2 42  ? -12.283 5.321   -8.891  1.00 36.24  ? 51  HIS   B CB  1 
ATOM   602  C  CG  . HIS   B 2 42  ? -12.359 4.996   -10.347 1.00 36.55  ? 51  HIS   B CG  1 
ATOM   603  N  ND1 . HIS   B 2 42  ? -12.588 3.709   -10.783 1.00 37.76  ? 51  HIS   B ND1 1 
ATOM   604  C  CD2 . HIS   B 2 42  ? -12.235 5.806   -11.420 1.00 37.43  ? 51  HIS   B CD2 1 
ATOM   605  C  CE1 . HIS   B 2 42  ? -12.598 3.775   -12.099 1.00 38.19  ? 51  HIS   B CE1 1 
ATOM   606  N  NE2 . HIS   B 2 42  ? -12.419 5.024   -12.525 1.00 38.60  ? 51  HIS   B NE2 1 
ATOM   607  N  N   . VAL   B 2 43  ? -15.306 6.848   -9.781  1.00 37.03  ? 52  VAL   B N   1 
ATOM   608  C  CA  . VAL   B 2 43  ? -15.971 7.912   -10.523 1.00 37.55  ? 52  VAL   B CA  1 
ATOM   609  C  C   . VAL   B 2 43  ? -16.729 8.878   -9.584  1.00 38.56  ? 52  VAL   B C   1 
ATOM   610  O  O   . VAL   B 2 43  ? -16.558 10.094  -9.692  1.00 39.53  ? 52  VAL   B O   1 
ATOM   611  C  CB  . VAL   B 2 43  ? -16.916 7.307   -11.583 1.00 38.12  ? 52  VAL   B CB  1 
ATOM   612  C  CG1 . VAL   B 2 43  ? -17.818 8.368   -12.209 1.00 38.40  ? 52  VAL   B CG1 1 
ATOM   613  C  CG2 . VAL   B 2 43  ? -16.136 6.559   -12.646 1.00 38.38  ? 52  VAL   B CG2 1 
ATOM   614  N  N   . THR   B 2 44  ? -17.580 8.352   -8.682  1.00 38.17  ? 53  THR   B N   1 
ATOM   615  C  CA  . THR   B 2 44  ? -18.384 9.209   -7.809  1.00 38.47  ? 53  THR   B CA  1 
ATOM   616  C  C   . THR   B 2 44  ? -17.862 9.368   -6.405  1.00 40.32  ? 53  THR   B C   1 
ATOM   617  O  O   . THR   B 2 44  ? -18.257 10.327  -5.724  1.00 40.99  ? 53  THR   B O   1 
ATOM   618  C  CB  . THR   B 2 44  ? -19.842 8.720   -7.751  1.00 37.42  ? 53  THR   B CB  1 
ATOM   619  O  OG1 . THR   B 2 44  ? -19.907 7.511   -6.990  1.00 37.44  ? 53  THR   B OG1 1 
ATOM   620  C  CG2 . THR   B 2 44  ? -20.449 8.490   -9.147  1.00 37.23  ? 53  THR   B CG2 1 
ATOM   621  N  N   . LYS   B 2 45  ? -17.019 8.421   -5.947  1.00 40.58  ? 54  LYS   B N   1 
ATOM   622  C  CA  . LYS   B 2 45  ? -16.518 8.331   -4.562  1.00 41.25  ? 54  LYS   B CA  1 
ATOM   623  C  C   . LYS   B 2 45  ? -17.674 8.117   -3.560  1.00 41.22  ? 54  LYS   B C   1 
ATOM   624  O  O   . LYS   B 2 45  ? -17.543 8.445   -2.378  1.00 41.62  ? 54  LYS   B O   1 
ATOM   625  C  CB  . LYS   B 2 45  ? -15.654 9.544   -4.164  1.00 43.80  ? 54  LYS   B CB  1 
ATOM   626  C  CG  . LYS   B 2 45  ? -14.569 9.904   -5.169  1.00 51.03  ? 54  LYS   B CG  1 
ATOM   627  C  CD  . LYS   B 2 45  ? -13.236 9.289   -4.824  1.00 58.80  ? 54  LYS   B CD  1 
ATOM   628  C  CE  . LYS   B 2 45  ? -12.135 9.932   -5.638  1.00 65.37  ? 54  LYS   B CE  1 
ATOM   629  N  NZ  . LYS   B 2 45  ? -12.238 9.607   -7.096  1.00 68.96  ? 54  LYS   B NZ  1 
ATOM   630  N  N   . GLY   B 2 46  ? -18.790 7.573   -4.038  1.00 40.40  ? 55  GLY   B N   1 
ATOM   631  C  CA  . GLY   B 2 46  ? -19.975 7.348   -3.238  1.00 40.47  ? 55  GLY   B CA  1 
ATOM   632  C  C   . GLY   B 2 46  ? -20.841 8.574   -3.034  1.00 41.17  ? 55  GLY   B C   1 
ATOM   633  O  O   . GLY   B 2 46  ? -21.782 8.512   -2.246  1.00 42.03  ? 55  GLY   B O   1 
ATOM   634  N  N   . ALA   B 2 47  ? -20.558 9.705   -3.715  1.00 40.82  ? 56  ALA   B N   1 
ATOM   635  C  CA  . ALA   B 2 47  ? -21.371 10.930  -3.536  1.00 40.35  ? 56  ALA   B CA  1 
ATOM   636  C  C   . ALA   B 2 47  ? -22.735 10.854  -4.250  1.00 40.94  ? 56  ALA   B C   1 
ATOM   637  O  O   . ALA   B 2 47  ? -22.882 10.091  -5.193  1.00 41.32  ? 56  ALA   B O   1 
ATOM   638  C  CB  . ALA   B 2 47  ? -20.597 12.155  -4.018  1.00 39.84  ? 56  ALA   B CB  1 
ATOM   639  N  N   . ALA   B 2 48  ? -23.714 11.674  -3.837  1.00 41.11  ? 57  ALA   B N   1 
ATOM   640  C  CA  . ALA   B 2 48  ? -25.048 11.694  -4.441  1.00 41.80  ? 57  ALA   B CA  1 
ATOM   641  C  C   . ALA   B 2 48  ? -25.000 12.202  -5.880  1.00 42.79  ? 57  ALA   B C   1 
ATOM   642  O  O   . ALA   B 2 48  ? -24.084 12.935  -6.251  1.00 43.33  ? 57  ALA   B O   1 
ATOM   643  C  CB  . ALA   B 2 48  ? -26.004 12.550  -3.601  1.00 41.36  ? 57  ALA   B CB  1 
ATOM   644  N  N   . LEU   B 2 49  ? -25.950 11.771  -6.706  1.00 43.02  ? 58  LEU   B N   1 
ATOM   645  C  CA  . LEU   B 2 49  ? -25.991 12.169  -8.108  1.00 44.22  ? 58  LEU   B CA  1 
ATOM   646  C  C   . LEU   B 2 49  ? -27.294 12.888  -8.417  1.00 46.04  ? 58  LEU   B C   1 
ATOM   647  O  O   . LEU   B 2 49  ? -28.305 12.655  -7.767  1.00 46.82  ? 58  LEU   B O   1 
ATOM   648  C  CB  . LEU   B 2 49  ? -25.856 10.944  -9.029  1.00 44.28  ? 58  LEU   B CB  1 
ATOM   649  C  CG  . LEU   B 2 49  ? -24.600 10.098  -8.877  1.00 45.34  ? 58  LEU   B CG  1 
ATOM   650  C  CD1 . LEU   B 2 49  ? -24.635 8.915   -9.829  1.00 45.99  ? 58  LEU   B CD1 1 
ATOM   651  C  CD2 . LEU   B 2 49  ? -23.338 10.917  -9.093  1.00 45.38  ? 58  LEU   B CD2 1 
ATOM   652  N  N   . ARG   B 2 50  ? -27.277 13.749  -9.411  1.00 46.65  ? 59  ARG   B N   1 
ATOM   653  C  CA  . ARG   B 2 50  ? -28.451 14.493  -9.818  1.00 47.88  ? 59  ARG   B CA  1 
ATOM   654  C  C   . ARG   B 2 50  ? -28.906 14.033  -11.213 1.00 48.89  ? 59  ARG   B C   1 
ATOM   655  O  O   . ARG   B 2 50  ? -28.080 13.698  -12.048 1.00 48.37  ? 59  ARG   B O   1 
ATOM   656  C  CB  . ARG   B 2 50  ? -28.100 15.979  -9.779  1.00 49.81  ? 59  ARG   B CB  1 
ATOM   657  C  CG  . ARG   B 2 50  ? -29.105 16.906  -10.415 1.00 55.20  ? 59  ARG   B CG  1 
ATOM   658  C  CD  . ARG   B 2 50  ? -28.824 18.359  -10.052 1.00 59.73  ? 59  ARG   B CD  1 
ATOM   659  N  NE  . ARG   B 2 50  ? -27.453 18.779  -10.374 1.00 63.41  ? 59  ARG   B NE  1 
ATOM   660  C  CZ  . ARG   B 2 50  ? -27.068 19.247  -11.556 1.00 66.56  ? 59  ARG   B CZ  1 
ATOM   661  N  NH1 . ARG   B 2 50  ? -27.938 19.343  -12.558 1.00 66.32  ? 59  ARG   B NH1 1 
ATOM   662  N  NH2 . ARG   B 2 50  ? -25.809 19.624  -11.748 1.00 67.32  ? 59  ARG   B NH2 1 
ATOM   663  N  N   . SER   B 2 51  ? -30.212 13.936  -11.438 1.00 50.41  ? 60  SER   B N   1 
ATOM   664  C  CA  . SER   B 2 51  ? -30.757 13.564  -12.748 1.00 52.58  ? 60  SER   B CA  1 
ATOM   665  C  C   . SER   B 2 51  ? -31.962 14.475  -12.997 1.00 55.04  ? 60  SER   B C   1 
ATOM   666  O  O   . SER   B 2 51  ? -33.082 14.151  -12.596 1.00 55.57  ? 60  SER   B O   1 
ATOM   667  C  CB  . SER   B 2 51  ? -31.182 12.101  -12.764 1.00 53.33  ? 60  SER   B CB  1 
ATOM   668  O  OG  . SER   B 2 51  ? -31.860 11.790  -13.969 1.00 54.89  ? 60  SER   B OG  1 
ATOM   669  N  N   . GLY   B 2 52  ? -31.711 15.632  -13.600 1.00 56.22  ? 61  GLY   B N   1 
ATOM   670  C  CA  . GLY   B 2 52  ? -32.743 16.639  -13.795 1.00 57.73  ? 61  GLY   B CA  1 
ATOM   671  C  C   . GLY   B 2 52  ? -33.000 17.284  -12.453 1.00 59.05  ? 61  GLY   B C   1 
ATOM   672  O  O   . GLY   B 2 52  ? -32.051 17.704  -11.784 1.00 59.65  ? 61  GLY   B O   1 
ATOM   673  N  N   . GLU   B 2 53  ? -34.261 17.302  -12.007 1.00 59.33  ? 62  GLU   B N   1 
ATOM   674  C  CA  . GLU   B 2 53  ? -34.576 17.817  -10.666 1.00 59.71  ? 62  GLU   B CA  1 
ATOM   675  C  C   . GLU   B 2 53  ? -34.377 16.730  -9.571  1.00 59.05  ? 62  GLU   B C   1 
ATOM   676  O  O   . GLU   B 2 53  ? -34.190 17.069  -8.401  1.00 59.57  ? 62  GLU   B O   1 
ATOM   677  C  CB  . GLU   B 2 53  ? -36.007 18.375  -10.606 1.00 62.84  ? 62  GLU   B CB  1 
ATOM   678  C  CG  . GLU   B 2 53  ? -36.104 19.877  -10.818 1.00 70.34  ? 62  GLU   B CG  1 
ATOM   679  C  CD  . GLU   B 2 53  ? -37.527 20.409  -10.879 1.00 80.82  ? 62  GLU   B CD  1 
ATOM   680  O  OE1 . GLU   B 2 53  ? -38.417 19.667  -11.357 1.00 82.93  ? 62  GLU   B OE1 1 
ATOM   681  O  OE2 . GLU   B 2 53  ? -37.751 21.571  -10.462 1.00 84.06  ? 62  GLU   B OE2 1 
ATOM   682  N  N   . GLY   B 2 54  ? -34.420 15.452  -9.961  1.00 57.67  ? 63  GLY   B N   1 
ATOM   683  C  CA  . GLY   B 2 54  ? -34.298 14.317  -9.052  1.00 56.74  ? 63  GLY   B CA  1 
ATOM   684  C  C   . GLY   B 2 54  ? -32.926 14.062  -8.461  1.00 55.30  ? 63  GLY   B C   1 
ATOM   685  O  O   . GLY   B 2 54  ? -31.910 14.520  -8.990  1.00 55.65  ? 63  GLY   B O   1 
ATOM   686  N  N   . ARG   B 2 55  ? -32.899 13.328  -7.340  1.00 53.34  ? 64  ARG   B N   1 
ATOM   687  C  CA  . ARG   B 2 55  ? -31.674 12.966  -6.629  1.00 51.59  ? 64  ARG   B CA  1 
ATOM   688  C  C   . ARG   B 2 55  ? -31.515 11.440  -6.585  1.00 49.11  ? 64  ARG   B C   1 
ATOM   689  O  O   . ARG   B 2 55  ? -32.477 10.714  -6.333  1.00 48.94  ? 64  ARG   B O   1 
ATOM   690  C  CB  . ARG   B 2 55  ? -31.701 13.529  -5.185  1.00 52.74  ? 64  ARG   B CB  1 
ATOM   691  C  CG  . ARG   B 2 55  ? -30.395 13.370  -4.399  1.00 55.38  ? 64  ARG   B CG  1 
ATOM   692  C  CD  . ARG   B 2 55  ? -30.495 14.016  -3.018  1.00 59.59  ? 64  ARG   B CD  1 
ATOM   693  N  NE  . ARG   B 2 55  ? -29.365 13.689  -2.143  1.00 62.62  ? 64  ARG   B NE  1 
ATOM   694  C  CZ  . ARG   B 2 55  ? -28.685 14.580  -1.423  1.00 65.23  ? 64  ARG   B CZ  1 
ATOM   695  N  NH1 . ARG   B 2 55  ? -29.002 15.870  -1.475  1.00 64.32  ? 64  ARG   B NH1 1 
ATOM   696  N  NH2 . ARG   B 2 55  ? -27.677 14.189  -0.651  1.00 65.38  ? 64  ARG   B NH2 1 
ATOM   697  N  N   . LEU   B 2 56  ? -30.304 10.964  -6.834  1.00 46.69  ? 65  LEU   B N   1 
ATOM   698  C  CA  . LEU   B 2 56  ? -29.982 9.551   -6.743  1.00 45.18  ? 65  LEU   B CA  1 
ATOM   699  C  C   . LEU   B 2 56  ? -29.037 9.394   -5.547  1.00 43.35  ? 65  LEU   B C   1 
ATOM   700  O  O   . LEU   B 2 56  ? -27.938 9.951   -5.558  1.00 42.88  ? 65  LEU   B O   1 
ATOM   701  C  CB  . LEU   B 2 56  ? -29.277 9.036   -8.024  1.00 45.21  ? 65  LEU   B CB  1 
ATOM   702  C  CG  . LEU   B 2 56  ? -29.950 9.259   -9.380  1.00 47.46  ? 65  LEU   B CG  1 
ATOM   703  C  CD1 . LEU   B 2 56  ? -29.277 8.446   -10.443 1.00 47.53  ? 65  LEU   B CD1 1 
ATOM   704  C  CD2 . LEU   B 2 56  ? -31.432 8.879   -9.356  1.00 48.71  ? 65  LEU   B CD2 1 
ATOM   705  N  N   . ASP   B 2 57  ? -29.459 8.669   -4.518  1.00 42.50  ? 66  ASP   B N   1 
ATOM   706  C  CA  . ASP   B 2 57  ? -28.607 8.443   -3.352  1.00 42.49  ? 66  ASP   B CA  1 
ATOM   707  C  C   . ASP   B 2 57  ? -27.938 7.064   -3.450  1.00 41.27  ? 66  ASP   B C   1 
ATOM   708  O  O   . ASP   B 2 57  ? -28.534 6.118   -3.975  1.00 41.24  ? 66  ASP   B O   1 
ATOM   709  C  CB  . ASP   B 2 57  ? -29.425 8.575   -2.070  1.00 46.59  ? 66  ASP   B CB  1 
ATOM   710  C  CG  . ASP   B 2 57  ? -29.976 9.976   -1.875  1.00 55.56  ? 66  ASP   B CG  1 
ATOM   711  O  OD1 . ASP   B 2 57  ? -29.172 10.939  -1.893  1.00 56.82  ? 66  ASP   B OD1 1 
ATOM   712  O  OD2 . ASP   B 2 57  ? -31.207 10.111  -1.713  1.00 59.10  ? 66  ASP   B OD2 1 
ATOM   713  N  N   . PRO   B 2 58  ? -26.686 6.924   -2.978  1.00 39.96  ? 67  PRO   B N   1 
ATOM   714  C  CA  . PRO   B 2 58  ? -26.024 5.609   -3.044  1.00 38.73  ? 67  PRO   B CA  1 
ATOM   715  C  C   . PRO   B 2 58  ? -26.736 4.545   -2.201  1.00 37.94  ? 67  PRO   B C   1 
ATOM   716  O  O   . PRO   B 2 58  ? -27.337 4.851   -1.171  1.00 37.87  ? 67  PRO   B O   1 
ATOM   717  C  CB  . PRO   B 2 58  ? -24.623 5.900   -2.507  1.00 39.62  ? 67  PRO   B CB  1 
ATOM   718  C  CG  . PRO   B 2 58  ? -24.804 7.101   -1.638  1.00 40.10  ? 67  PRO   B CG  1 
ATOM   719  C  CD  . PRO   B 2 58  ? -25.828 7.932   -2.322  1.00 39.02  ? 67  PRO   B CD  1 
ATOM   720  N  N   . TYR   B 2 59  ? -26.676 3.291   -2.641  1.00 36.81  ? 68  TYR   B N   1 
ATOM   721  C  CA  . TYR   B 2 59  ? -27.335 2.199   -1.954  1.00 36.07  ? 68  TYR   B CA  1 
ATOM   722  C  C   . TYR   B 2 59  ? -26.322 1.180   -1.471  1.00 35.77  ? 68  TYR   B C   1 
ATOM   723  O  O   . TYR   B 2 59  ? -26.405 0.714   -0.345  1.00 36.59  ? 68  TYR   B O   1 
ATOM   724  C  CB  . TYR   B 2 59  ? -28.356 1.546   -2.898  1.00 35.42  ? 68  TYR   B CB  1 
ATOM   725  C  CG  . TYR   B 2 59  ? -29.177 0.446   -2.253  1.00 35.83  ? 68  TYR   B CG  1 
ATOM   726  C  CD1 . TYR   B 2 59  ? -28.692 -0.856  -2.168  1.00 36.39  ? 68  TYR   B CD1 1 
ATOM   727  C  CD2 . TYR   B 2 59  ? -30.475 0.685   -1.820  1.00 35.67  ? 68  TYR   B CD2 1 
ATOM   728  C  CE1 . TYR   B 2 59  ? -29.449 -1.871  -1.592  1.00 36.99  ? 68  TYR   B CE1 1 
ATOM   729  C  CE2 . TYR   B 2 59  ? -31.257 -0.333  -1.294  1.00 36.28  ? 68  TYR   B CE2 1 
ATOM   730  C  CZ  . TYR   B 2 59  ? -30.745 -1.612  -1.190  1.00 37.82  ? 68  TYR   B CZ  1 
ATOM   731  O  OH  . TYR   B 2 59  ? -31.518 -2.605  -0.629  1.00 39.63  ? 68  TYR   B OH  1 
ATOM   732  N  N   . TRP   B 2 60  ? -25.393 0.811   -2.329  1.00 35.23  ? 69  TRP   B N   1 
ATOM   733  C  CA  . TRP   B 2 60  ? -24.377 -0.198  -2.046  1.00 34.78  ? 69  TRP   B CA  1 
ATOM   734  C  C   . TRP   B 2 60  ? -23.076 0.253   -2.688  1.00 34.75  ? 69  TRP   B C   1 
ATOM   735  O  O   . TRP   B 2 60  ? -23.084 0.811   -3.777  1.00 34.49  ? 69  TRP   B O   1 
ATOM   736  C  CB  . TRP   B 2 60  ? -24.800 -1.595  -2.593  1.00 34.11  ? 69  TRP   B CB  1 
ATOM   737  C  CG  . TRP   B 2 60  ? -23.679 -2.589  -2.595  1.00 34.49  ? 69  TRP   B CG  1 
ATOM   738  C  CD1 . TRP   B 2 60  ? -23.200 -3.289  -1.524  1.00 35.59  ? 69  TRP   B CD1 1 
ATOM   739  C  CD2 . TRP   B 2 60  ? -22.769 -2.843  -3.681  1.00 34.51  ? 69  TRP   B CD2 1 
ATOM   740  N  NE1 . TRP   B 2 60  ? -22.065 -3.982  -1.881  1.00 35.66  ? 69  TRP   B NE1 1 
ATOM   741  C  CE2 . TRP   B 2 60  ? -21.779 -3.725  -3.202  1.00 35.07  ? 69  TRP   B CE2 1 
ATOM   742  C  CE3 . TRP   B 2 60  ? -22.678 -2.379  -5.001  1.00 35.10  ? 69  TRP   B CE3 1 
ATOM   743  C  CZ2 . TRP   B 2 60  ? -20.732 -4.168  -3.998  1.00 35.39  ? 69  TRP   B CZ2 1 
ATOM   744  C  CZ3 . TRP   B 2 60  ? -21.637 -2.820  -5.792  1.00 35.69  ? 69  TRP   B CZ3 1 
ATOM   745  C  CH2 . TRP   B 2 60  ? -20.700 -3.734  -5.301  1.00 35.83  ? 69  TRP   B CH2 1 
ATOM   746  N  N   . GLY   B 2 61  ? -21.966 -0.015  -2.020  1.00 35.00  ? 70  GLY   B N   1 
ATOM   747  C  CA  . GLY   B 2 61  ? -20.661 0.340   -2.559  1.00 35.37  ? 70  GLY   B CA  1 
ATOM   748  C  C   . GLY   B 2 61  ? -19.554 -0.444  -1.920  1.00 34.94  ? 70  GLY   B C   1 
ATOM   749  O  O   . GLY   B 2 61  ? -19.710 -0.943  -0.794  1.00 35.02  ? 70  GLY   B O   1 
ATOM   750  N  N   . ASP   B 2 62  ? -18.423 -0.523  -2.626  1.00 34.43  ? 71  ASP   B N   1 
ATOM   751  C  CA  . ASP   B 2 62  ? -17.247 -1.248  -2.176  1.00 34.68  ? 71  ASP   B CA  1 
ATOM   752  C  C   . ASP   B 2 62  ? -16.022 -0.740  -2.944  1.00 34.83  ? 71  ASP   B C   1 
ATOM   753  O  O   . ASP   B 2 62  ? -15.972 -0.866  -4.166  1.00 34.36  ? 71  ASP   B O   1 
ATOM   754  C  CB  . ASP   B 2 62  ? -17.450 -2.741  -2.443  1.00 37.28  ? 71  ASP   B CB  1 
ATOM   755  C  CG  . ASP   B 2 62  ? -16.477 -3.639  -1.731  1.00 44.26  ? 71  ASP   B CG  1 
ATOM   756  O  OD1 . ASP   B 2 62  ? -15.305 -3.668  -2.124  1.00 45.21  ? 71  ASP   B OD1 1 
ATOM   757  O  OD2 . ASP   B 2 62  ? -16.899 -4.340  -0.802  1.00 49.26  ? 71  ASP   B OD2 1 
ATOM   758  N  N   . VAL   B 2 63  ? -15.032 -0.189  -2.218  1.00 35.04  ? 72  VAL   B N   1 
ATOM   759  C  CA  . VAL   B 2 63  ? -13.801 0.380   -2.775  1.00 34.99  ? 72  VAL   B CA  1 
ATOM   760  C  C   . VAL   B 2 63  ? -12.932 -0.699  -3.434  1.00 35.61  ? 72  VAL   B C   1 
ATOM   761  O  O   . VAL   B 2 63  ? -12.391 -0.461  -4.512  1.00 36.16  ? 72  VAL   B O   1 
ATOM   762  C  CB  . VAL   B 2 63  ? -13.055 1.205   -1.681  1.00 34.54  ? 72  VAL   B CB  1 
ATOM   763  C  CG1 . VAL   B 2 63  ? -11.580 1.383   -1.987  1.00 34.28  ? 72  VAL   B CG1 1 
ATOM   764  C  CG2 . VAL   B 2 63  ? -13.725 2.558   -1.468  1.00 34.91  ? 72  VAL   B CG2 1 
ATOM   765  N  N   . LYS   B 2 64  ? -12.848 -1.892  -2.838  1.00 35.95  ? 73  LYS   B N   1 
ATOM   766  C  CA  . LYS   B 2 64  ? -12.024 -2.965  -3.411  1.00 36.48  ? 73  LYS   B CA  1 
ATOM   767  C  C   . LYS   B 2 64  ? -12.585 -3.517  -4.726  1.00 36.51  ? 73  LYS   B C   1 
ATOM   768  O  O   . LYS   B 2 64  ? -11.838 -3.666  -5.679  1.00 36.52  ? 73  LYS   B O   1 
ATOM   769  C  CB  . LYS   B 2 64  ? -11.747 -4.079  -2.407  1.00 38.34  ? 73  LYS   B CB  1 
ATOM   770  C  CG  . LYS   B 2 64  ? -10.669 -5.021  -2.924  1.00 41.13  ? 73  LYS   B CG  1 
ATOM   771  C  CD  . LYS   B 2 64  ? -10.303 -6.046  -1.885  1.00 43.76  ? 73  LYS   B CD  1 
ATOM   772  C  CE  . LYS   B 2 64  ? -9.162  -6.851  -2.413  1.00 46.72  ? 73  LYS   B CE  1 
ATOM   773  N  NZ  . LYS   B 2 64  ? -8.573  -7.707  -1.367  1.00 49.35  ? 73  LYS   B NZ  1 
ATOM   774  N  N   . GLN   B 2 65  ? -13.895 -3.799  -4.791  1.00 36.24  ? 74  GLN   B N   1 
ATOM   775  C  CA  . GLN   B 2 65  ? -14.526 -4.210  -6.052  1.00 35.45  ? 74  GLN   B CA  1 
ATOM   776  C  C   . GLN   B 2 65  ? -14.558 -3.023  -7.034  1.00 34.94  ? 74  GLN   B C   1 
ATOM   777  O  O   . GLN   B 2 65  ? -14.640 -3.236  -8.250  1.00 34.86  ? 74  GLN   B O   1 
ATOM   778  C  CB  . GLN   B 2 65  ? -15.975 -4.675  -5.829  1.00 37.34  ? 74  GLN   B CB  1 
ATOM   779  C  CG  . GLN   B 2 65  ? -16.123 -5.877  -4.905  1.00 43.08  ? 74  GLN   B CG  1 
ATOM   780  C  CD  . GLN   B 2 65  ? -17.570 -6.381  -4.843  1.00 47.92  ? 74  GLN   B CD  1 
ATOM   781  O  OE1 . GLN   B 2 65  ? -18.294 -6.448  -5.862  1.00 48.22  ? 74  GLN   B OE1 1 
ATOM   782  N  NE2 . GLN   B 2 65  ? -18.009 -6.764  -3.643  1.00 48.17  ? 74  GLN   B NE2 1 
ATOM   783  N  N   . ASP   B 2 66  ? -14.535 -1.776  -6.502  1.00 34.42  ? 75  ASP   B N   1 
ATOM   784  C  CA  . ASP   B 2 66  ? -14.564 -0.507  -7.234  1.00 34.29  ? 75  ASP   B CA  1 
ATOM   785  C  C   . ASP   B 2 66  ? -15.893 -0.355  -7.934  1.00 33.91  ? 75  ASP   B C   1 
ATOM   786  O  O   . ASP   B 2 66  ? -15.940 0.055   -9.090  1.00 33.81  ? 75  ASP   B O   1 
ATOM   787  C  CB  . ASP   B 2 66  ? -13.377 -0.344  -8.223  1.00 34.72  ? 75  ASP   B CB  1 
ATOM   788  C  CG  . ASP   B 2 66  ? -13.302 1.066   -8.780  1.00 34.61  ? 75  ASP   B CG  1 
ATOM   789  O  OD1 . ASP   B 2 66  ? -13.560 2.016   -8.014  1.00 36.25  ? 75  ASP   B OD1 1 
ATOM   790  O  OD2 . ASP   B 2 66  ? -13.019 1.213   -9.986  1.00 34.41  ? 75  ASP   B OD2 1 
ATOM   791  N  N   . LEU   B 2 67  ? -16.992 -0.673  -7.223  1.00 33.65  ? 76  LEU   B N   1 
ATOM   792  C  CA  . LEU   B 2 67  ? -18.338 -0.563  -7.774  1.00 33.10  ? 76  LEU   B CA  1 
ATOM   793  C  C   . LEU   B 2 67  ? -19.269 0.160   -6.804  1.00 33.03  ? 76  LEU   B C   1 
ATOM   794  O  O   . LEU   B 2 67  ? -18.990 0.222   -5.609  1.00 32.61  ? 76  LEU   B O   1 
ATOM   795  C  CB  . LEU   B 2 67  ? -18.889 -1.951  -8.071  1.00 33.18  ? 76  LEU   B CB  1 
ATOM   796  C  CG  . LEU   B 2 67  ? -18.203 -2.711  -9.171  1.00 34.91  ? 76  LEU   B CG  1 
ATOM   797  C  CD1 . LEU   B 2 67  ? -18.683 -4.128  -9.202  1.00 35.46  ? 76  LEU   B CD1 1 
ATOM   798  C  CD2 . LEU   B 2 67  ? -18.370 -2.004  -10.554 1.00 35.73  ? 76  LEU   B CD2 1 
ATOM   799  N  N   . VAL   B 2 68  ? -20.384 0.709   -7.318  1.00 32.87  ? 77  VAL   B N   1 
ATOM   800  C  CA  . VAL   B 2 68  ? -21.384 1.429   -6.490  1.00 32.38  ? 77  VAL   B CA  1 
ATOM   801  C  C   . VAL   B 2 68  ? -22.722 1.446   -7.262  1.00 32.49  ? 77  VAL   B C   1 
ATOM   802  O  O   . VAL   B 2 68  ? -22.725 1.519   -8.485  1.00 32.50  ? 77  VAL   B O   1 
ATOM   803  C  CB  . VAL   B 2 68  ? -20.899 2.867   -6.091  1.00 31.28  ? 77  VAL   B CB  1 
ATOM   804  C  CG1 . VAL   B 2 68  ? -20.567 3.710   -7.330  1.00 31.22  ? 77  VAL   B CG1 1 
ATOM   805  C  CG2 . VAL   B 2 68  ? -21.877 3.576   -5.168  1.00 30.56  ? 77  VAL   B CG2 1 
ATOM   806  N  N   . SER   B 2 69  ? -23.833 1.274   -6.546  1.00 32.57  ? 78  SER   B N   1 
ATOM   807  C  CA  . SER   B 2 69  ? -25.191 1.259   -7.098  1.00 32.79  ? 78  SER   B CA  1 
ATOM   808  C  C   . SER   B 2 69  ? -26.034 2.374   -6.425  1.00 32.93  ? 78  SER   B C   1 
ATOM   809  O  O   . SER   B 2 69  ? -25.814 2.722   -5.271  1.00 32.52  ? 78  SER   B O   1 
ATOM   810  C  CB  . SER   B 2 69  ? -25.838 -0.129  -6.959  1.00 32.80  ? 78  SER   B CB  1 
ATOM   811  O  OG  . SER   B 2 69  ? -26.173 -0.481  -5.623  1.00 34.93  ? 78  SER   B OG  1 
ATOM   812  N  N   . TYR   B 2 70  ? -26.935 2.984   -7.184  1.00 33.05  ? 79  TYR   B N   1 
ATOM   813  C  CA  . TYR   B 2 70  ? -27.749 4.104   -6.718  1.00 33.18  ? 79  TYR   B CA  1 
ATOM   814  C  C   . TYR   B 2 70  ? -29.210 3.706   -6.851  1.00 33.93  ? 79  TYR   B C   1 
ATOM   815  O  O   . TYR   B 2 70  ? -29.575 3.111   -7.863  1.00 33.94  ? 79  TYR   B O   1 
ATOM   816  C  CB  . TYR   B 2 70  ? -27.459 5.345   -7.585  1.00 32.85  ? 79  TYR   B CB  1 
ATOM   817  C  CG  . TYR   B 2 70  ? -26.129 5.998   -7.266  1.00 32.86  ? 79  TYR   B CG  1 
ATOM   818  C  CD1 . TYR   B 2 70  ? -24.934 5.476   -7.757  1.00 33.09  ? 79  TYR   B CD1 1 
ATOM   819  C  CD2 . TYR   B 2 70  ? -26.064 7.122   -6.452  1.00 33.57  ? 79  TYR   B CD2 1 
ATOM   820  C  CE1 . TYR   B 2 70  ? -23.708 6.050   -7.438  1.00 33.89  ? 79  TYR   B CE1 1 
ATOM   821  C  CE2 . TYR   B 2 70  ? -24.848 7.686   -6.102  1.00 34.45  ? 79  TYR   B CE2 1 
ATOM   822  C  CZ  . TYR   B 2 70  ? -23.671 7.154   -6.603  1.00 35.56  ? 79  TYR   B CZ  1 
ATOM   823  O  OH  . TYR   B 2 70  ? -22.481 7.753   -6.256  1.00 36.82  ? 79  TYR   B OH  1 
ATOM   824  N  N   . CYS   B 2 71  ? -30.020 3.963   -5.797  1.00 34.16  ? 80  CYS   B N   1 
ATOM   825  C  CA  . CYS   B 2 71  ? -31.462 3.684   -5.730  1.00 35.79  ? 80  CYS   B CA  1 
ATOM   826  C  C   . CYS   B 2 71  ? -31.809 2.236   -5.409  1.00 36.06  ? 80  CYS   B C   1 
ATOM   827  O  O   . CYS   B 2 71  ? -32.969 1.969   -5.085  1.00 37.56  ? 80  CYS   B O   1 
ATOM   828  C  CB  . CYS   B 2 71  ? -32.203 4.151   -6.983  1.00 38.72  ? 80  CYS   B CB  1 
ATOM   829  S  SG  . CYS   B 2 71  ? -31.841 5.857   -7.474  1.00 47.26  ? 80  CYS   B SG  1 
ATOM   830  N  N   . GLY   B 2 72  ? -30.852 1.314   -5.514  1.00 34.26  ? 81  GLY   B N   1 
ATOM   831  C  CA  . GLY   B 2 72  ? -31.151 -0.082  -5.230  1.00 33.46  ? 81  GLY   B CA  1 
ATOM   832  C  C   . GLY   B 2 72  ? -29.942 -0.973  -5.302  1.00 32.82  ? 81  GLY   B C   1 
ATOM   833  O  O   . GLY   B 2 72  ? -28.815 -0.519  -5.527  1.00 31.19  ? 81  GLY   B O   1 
ATOM   834  N  N   . PRO   B 2 73  ? -30.154 -2.257  -5.000  1.00 33.49  ? 82  PRO   B N   1 
ATOM   835  C  CA  . PRO   B 2 73  ? -29.027 -3.194  -5.041  1.00 34.09  ? 82  PRO   B CA  1 
ATOM   836  C  C   . PRO   B 2 73  ? -28.510 -3.419  -6.464  1.00 35.06  ? 82  PRO   B C   1 
ATOM   837  O  O   . PRO   B 2 73  ? -29.246 -3.226  -7.438  1.00 35.60  ? 82  PRO   B O   1 
ATOM   838  C  CB  . PRO   B 2 73  ? -29.607 -4.472  -4.431  1.00 34.48  ? 82  PRO   B CB  1 
ATOM   839  C  CG  . PRO   B 2 73  ? -31.080 -4.372  -4.657  1.00 34.58  ? 82  PRO   B CG  1 
ATOM   840  C  CD  . PRO   B 2 73  ? -31.429 -2.922  -4.658  1.00 32.72  ? 82  PRO   B CD  1 
ATOM   841  N  N   . TRP   B 2 74  ? -27.249 -3.885  -6.585  1.00 34.85  ? 83  TRP   B N   1 
ATOM   842  C  CA  . TRP   B 2 74  ? -26.642 -4.198  -7.875  1.00 35.27  ? 83  TRP   B CA  1 
ATOM   843  C  C   . TRP   B 2 74  ? -27.527 -5.211  -8.669  1.00 36.55  ? 83  TRP   B C   1 
ATOM   844  O  O   . TRP   B 2 74  ? -27.955 -6.232  -8.123  1.00 36.88  ? 83  TRP   B O   1 
ATOM   845  C  CB  . TRP   B 2 74  ? -25.211 -4.716  -7.653  1.00 34.26  ? 83  TRP   B CB  1 
ATOM   846  C  CG  . TRP   B 2 74  ? -24.417 -4.869  -8.912  1.00 33.32  ? 83  TRP   B CG  1 
ATOM   847  C  CD1 . TRP   B 2 74  ? -24.353 -5.972  -9.708  1.00 33.38  ? 83  TRP   B CD1 1 
ATOM   848  C  CD2 . TRP   B 2 74  ? -23.534 -3.897  -9.496  1.00 33.03  ? 83  TRP   B CD2 1 
ATOM   849  N  NE1 . TRP   B 2 74  ? -23.533 -5.729  -10.786 1.00 33.84  ? 83  TRP   B NE1 1 
ATOM   850  C  CE2 . TRP   B 2 74  ? -23.026 -4.457  -10.689 1.00 33.48  ? 83  TRP   B CE2 1 
ATOM   851  C  CE3 . TRP   B 2 74  ? -23.195 -2.574  -9.175  1.00 33.10  ? 83  TRP   B CE3 1 
ATOM   852  C  CZ2 . TRP   B 2 74  ? -22.166 -3.759  -11.536 1.00 33.54  ? 83  TRP   B CZ2 1 
ATOM   853  C  CZ3 . TRP   B 2 74  ? -22.350 -1.878  -10.021 1.00 33.70  ? 83  TRP   B CZ3 1 
ATOM   854  C  CH2 . TRP   B 2 74  ? -21.870 -2.459  -11.203 1.00 33.77  ? 83  TRP   B CH2 1 
ATOM   855  N  N   . LYS   B 2 75  ? -27.879 -4.869  -9.916  1.00 37.08  ? 84  LYS   B N   1 
ATOM   856  C  CA  . LYS   B 2 75  ? -28.771 -5.699  -10.723 1.00 37.77  ? 84  LYS   B CA  1 
ATOM   857  C  C   . LYS   B 2 75  ? -28.083 -6.516  -11.799 1.00 39.04  ? 84  LYS   B C   1 
ATOM   858  O  O   . LYS   B 2 75  ? -28.732 -7.371  -12.385 1.00 39.09  ? 84  LYS   B O   1 
ATOM   859  C  CB  . LYS   B 2 75  ? -29.795 -4.806  -11.440 1.00 38.66  ? 84  LYS   B CB  1 
ATOM   860  C  CG  . LYS   B 2 75  ? -30.595 -3.923  -10.511 1.00 40.01  ? 84  LYS   B CG  1 
ATOM   861  C  CD  . LYS   B 2 75  ? -31.710 -4.699  -9.890  1.00 42.53  ? 84  LYS   B CD  1 
ATOM   862  C  CE  . LYS   B 2 75  ? -32.381 -3.880  -8.835  1.00 45.26  ? 84  LYS   B CE  1 
ATOM   863  N  NZ  . LYS   B 2 75  ? -33.532 -4.593  -8.259  1.00 48.47  ? 84  LYS   B NZ  1 
ATOM   864  N  N   . LEU   B 2 76  ? -26.828 -6.197  -12.136 1.00 40.28  ? 85  LEU   B N   1 
ATOM   865  C  CA  . LEU   B 2 76  ? -26.106 -6.784  -13.263 1.00 41.64  ? 85  LEU   B CA  1 
ATOM   866  C  C   . LEU   B 2 76  ? -25.400 -8.073  -12.876 1.00 44.26  ? 85  LEU   B C   1 
ATOM   867  O  O   . LEU   B 2 76  ? -24.491 -8.027  -12.054 1.00 44.94  ? 85  LEU   B O   1 
ATOM   868  C  CB  . LEU   B 2 76  ? -25.102 -5.770  -13.848 1.00 41.11  ? 85  LEU   B CB  1 
ATOM   869  C  CG  . LEU   B 2 76  ? -25.597 -4.331  -14.048 1.00 42.35  ? 85  LEU   B CG  1 
ATOM   870  C  CD1 . LEU   B 2 76  ? -24.498 -3.428  -14.607 1.00 42.20  ? 85  LEU   B CD1 1 
ATOM   871  C  CD2 . LEU   B 2 76  ? -26.774 -4.283  -14.984 1.00 43.31  ? 85  LEU   B CD2 1 
ATOM   872  N  N   . ASP   B 2 77  ? -25.786 -9.213  -13.474 1.00 45.53  ? 86  ASP   B N   1 
ATOM   873  C  CA  . ASP   B 2 77  ? -25.158 -10.488 -13.104 1.00 47.83  ? 86  ASP   B CA  1 
ATOM   874  C  C   . ASP   B 2 77  ? -24.692 -11.343 -14.268 1.00 48.72  ? 86  ASP   B C   1 
ATOM   875  O  O   . ASP   B 2 77  ? -24.172 -12.436 -14.017 1.00 49.76  ? 86  ASP   B O   1 
ATOM   876  C  CB  . ASP   B 2 77  ? -26.051 -11.327 -12.172 1.00 50.77  ? 86  ASP   B CB  1 
ATOM   877  C  CG  . ASP   B 2 77  ? -27.459 -11.576 -12.686 1.00 58.72  ? 86  ASP   B CG  1 
ATOM   878  O  OD1 . ASP   B 2 77  ? -27.791 -11.082 -13.794 1.00 60.16  ? 86  ASP   B OD1 1 
ATOM   879  O  OD2 . ASP   B 2 77  ? -28.239 -12.248 -11.974 1.00 62.28  ? 86  ASP   B OD2 1 
ATOM   880  N  N   . ALA   B 2 78  ? -24.821 -10.868 -15.519 1.00 48.18  ? 87  ALA   B N   1 
ATOM   881  C  CA  . ALA   B 2 78  ? -24.326 -11.640 -16.658 1.00 48.39  ? 87  ALA   B CA  1 
ATOM   882  C  C   . ALA   B 2 78  ? -22.789 -11.753 -16.571 1.00 48.60  ? 87  ALA   B C   1 
ATOM   883  O  O   . ALA   B 2 78  ? -22.130 -10.873 -16.001 1.00 48.69  ? 87  ALA   B O   1 
ATOM   884  C  CB  . ALA   B 2 78  ? -24.741 -10.989 -17.978 1.00 48.28  ? 87  ALA   B CB  1 
ATOM   885  N  N   . ALA   B 2 79  ? -22.229 -12.838 -17.112 1.00 48.42  ? 88  ALA   B N   1 
ATOM   886  C  CA  . ALA   B 2 79  ? -20.795 -13.053 -17.056 1.00 48.73  ? 88  ALA   B CA  1 
ATOM   887  C  C   . ALA   B 2 79  ? -20.203 -13.392 -18.418 1.00 49.26  ? 88  ALA   B C   1 
ATOM   888  O  O   . ALA   B 2 79  ? -20.854 -14.060 -19.215 1.00 48.87  ? 88  ALA   B O   1 
ATOM   889  C  CB  . ALA   B 2 79  ? -20.502 -14.184 -16.088 1.00 49.04  ? 88  ALA   B CB  1 
ATOM   890  N  N   . TRP   B 2 80  ? -18.930 -13.003 -18.651 1.00 49.83  ? 89  TRP   B N   1 
ATOM   891  C  CA  . TRP   B 2 80  ? -18.169 -13.377 -19.839 1.00 50.96  ? 89  TRP   B CA  1 
ATOM   892  C  C   . TRP   B 2 80  ? -18.018 -14.915 -19.802 1.00 52.17  ? 89  TRP   B C   1 
ATOM   893  O  O   . TRP   B 2 80  ? -17.784 -15.481 -18.726 1.00 51.34  ? 89  TRP   B O   1 
ATOM   894  C  CB  . TRP   B 2 80  ? -16.770 -12.730 -19.817 1.00 51.03  ? 89  TRP   B CB  1 
ATOM   895  C  CG  . TRP   B 2 80  ? -15.937 -13.064 -21.025 1.00 51.92  ? 89  TRP   B CG  1 
ATOM   896  C  CD1 . TRP   B 2 80  ? -16.332 -13.010 -22.328 1.00 52.89  ? 89  TRP   B CD1 1 
ATOM   897  C  CD2 . TRP   B 2 80  ? -14.558 -13.475 -21.041 1.00 51.71  ? 89  TRP   B CD2 1 
ATOM   898  N  NE1 . TRP   B 2 80  ? -15.300 -13.395 -23.152 1.00 52.95  ? 89  TRP   B NE1 1 
ATOM   899  C  CE2 . TRP   B 2 80  ? -14.184 -13.634 -22.391 1.00 52.35  ? 89  TRP   B CE2 1 
ATOM   900  C  CE3 . TRP   B 2 80  ? -13.595 -13.696 -20.047 1.00 51.94  ? 89  TRP   B CE3 1 
ATOM   901  C  CZ2 . TRP   B 2 80  ? -12.906 -14.058 -22.770 1.00 52.69  ? 89  TRP   B CZ2 1 
ATOM   902  C  CZ3 . TRP   B 2 80  ? -12.324 -14.094 -20.426 1.00 52.45  ? 89  TRP   B CZ3 1 
ATOM   903  C  CH2 . TRP   B 2 80  ? -11.992 -14.281 -21.772 1.00 52.64  ? 89  TRP   B CH2 1 
ATOM   904  N  N   . ASP   B 2 81  ? -18.233 -15.588 -20.943 1.00 53.46  ? 90  ASP   B N   1 
ATOM   905  C  CA  . ASP   B 2 81  ? -18.136 -17.052 -20.962 1.00 54.69  ? 90  ASP   B CA  1 
ATOM   906  C  C   . ASP   B 2 81  ? -16.704 -17.596 -21.099 1.00 56.25  ? 90  ASP   B C   1 
ATOM   907  O  O   . ASP   B 2 81  ? -16.518 -18.818 -21.120 1.00 56.66  ? 90  ASP   B O   1 
ATOM   908  C  CB  . ASP   B 2 81  ? -19.053 -17.650 -22.031 1.00 55.81  ? 90  ASP   B CB  1 
ATOM   909  C  CG  . ASP   B 2 81  ? -18.730 -17.277 -23.456 1.00 60.02  ? 90  ASP   B CG  1 
ATOM   910  O  OD1 . ASP   B 2 81  ? -17.767 -16.510 -23.671 1.00 60.37  ? 90  ASP   B OD1 1 
ATOM   911  O  OD2 . ASP   B 2 81  ? -19.441 -17.752 -24.366 1.00 63.15  ? 90  ASP   B OD2 1 
ATOM   912  N  N   . GLY   B 2 82  ? -15.722 -16.705 -21.225 1.00 56.99  ? 91  GLY   B N   1 
ATOM   913  C  CA  . GLY   B 2 82  ? -14.321 -17.084 -21.376 1.00 58.36  ? 91  GLY   B CA  1 
ATOM   914  C  C   . GLY   B 2 82  ? -13.916 -17.501 -22.779 1.00 59.57  ? 91  GLY   B C   1 
ATOM   915  O  O   . GLY   B 2 82  ? -12.782 -17.938 -22.990 1.00 60.03  ? 91  GLY   B O   1 
ATOM   916  N  N   . LEU   B 2 83  ? -14.831 -17.399 -23.746 1.00 60.11  ? 92  LEU   B N   1 
ATOM   917  C  CA  . LEU   B 2 83  ? -14.549 -17.820 -25.110 1.00 61.31  ? 92  LEU   B CA  1 
ATOM   918  C  C   . LEU   B 2 83  ? -14.939 -16.808 -26.162 1.00 62.27  ? 92  LEU   B C   1 
ATOM   919  O  O   . LEU   B 2 83  ? -14.216 -16.647 -27.142 1.00 63.39  ? 92  LEU   B O   1 
ATOM   920  C  CB  . LEU   B 2 83  ? -15.262 -19.143 -25.402 1.00 61.96  ? 92  LEU   B CB  1 
ATOM   921  C  CG  . LEU   B 2 83  ? -14.582 -20.373 -24.870 1.00 64.61  ? 92  LEU   B CG  1 
ATOM   922  C  CD1 . LEU   B 2 83  ? -15.578 -21.302 -24.209 1.00 66.03  ? 92  LEU   B CD1 1 
ATOM   923  C  CD2 . LEU   B 2 83  ? -13.814 -21.078 -25.957 1.00 64.79  ? 92  LEU   B CD2 1 
ATOM   924  N  N   . SER   B 2 84  ? -16.103 -16.175 -26.013 1.00 61.83  ? 93  SER   B N   1 
ATOM   925  C  CA  . SER   B 2 84  ? -16.638 -15.269 -27.030 1.00 61.47  ? 93  SER   B CA  1 
ATOM   926  C  C   . SER   B 2 84  ? -16.083 -13.848 -26.975 1.00 60.49  ? 93  SER   B C   1 
ATOM   927  O  O   . SER   B 2 84  ? -15.603 -13.389 -25.920 1.00 60.77  ? 93  SER   B O   1 
ATOM   928  C  CB  . SER   B 2 84  ? -18.164 -15.201 -26.936 1.00 63.14  ? 93  SER   B CB  1 
ATOM   929  O  OG  . SER   B 2 84  ? -18.761 -16.398 -26.465 1.00 65.53  ? 93  SER   B OG  1 
ATOM   930  N  N   . GLU   B 2 85  ? -16.183 -13.146 -28.124 1.00 58.70  ? 94  GLU   B N   1 
ATOM   931  C  CA  . GLU   B 2 85  ? -15.842 -11.735 -28.255 1.00 57.89  ? 94  GLU   B CA  1 
ATOM   932  C  C   . GLU   B 2 85  ? -16.963 -10.915 -27.578 1.00 55.98  ? 94  GLU   B C   1 
ATOM   933  O  O   . GLU   B 2 85  ? -18.088 -11.385 -27.381 1.00 56.27  ? 94  GLU   B O   1 
ATOM   934  C  CB  . GLU   B 2 85  ? -15.666 -11.306 -29.742 1.00 60.50  ? 94  GLU   B CB  1 
ATOM   935  C  CG  . GLU   B 2 85  ? -14.319 -11.696 -30.354 1.00 66.05  ? 94  GLU   B CG  1 
ATOM   936  C  CD  . GLU   B 2 85  ? -13.837 -10.916 -31.571 1.00 72.73  ? 94  GLU   B CD  1 
ATOM   937  O  OE1 . GLU   B 2 85  ? -14.680 -10.318 -32.282 1.00 73.36  ? 94  GLU   B OE1 1 
ATOM   938  O  OE2 . GLU   B 2 85  ? -12.607 -10.902 -31.813 1.00 74.77  ? 94  GLU   B OE2 1 
ATOM   939  N  N   . VAL   B 2 86  ? -16.626 -9.715  -27.154 1.00 53.77  ? 95  VAL   B N   1 
ATOM   940  C  CA  . VAL   B 2 86  ? -17.545 -8.838  -26.431 1.00 51.56  ? 95  VAL   B CA  1 
ATOM   941  C  C   . VAL   B 2 86  ? -17.487 -7.430  -27.034 1.00 49.44  ? 95  VAL   B C   1 
ATOM   942  O  O   . VAL   B 2 86  ? -16.570 -7.129  -27.792 1.00 49.12  ? 95  VAL   B O   1 
ATOM   943  C  CB  . VAL   B 2 86  ? -17.167 -8.797  -24.908 1.00 50.94  ? 95  VAL   B CB  1 
ATOM   944  C  CG1 . VAL   B 2 86  ? -17.000 -10.198 -24.326 1.00 51.40  ? 95  VAL   B CG1 1 
ATOM   945  C  CG2 . VAL   B 2 86  ? -15.908 -7.967  -24.677 1.00 50.79  ? 95  VAL   B CG2 1 
ATOM   946  N  N   . GLN   B 2 87  ? -18.415 -6.544  -26.630 1.00 48.45  ? 96  GLN   B N   1 
ATOM   947  C  CA  . GLN   B 2 87  ? -18.377 -5.168  -27.068 1.00 48.07  ? 96  GLN   B CA  1 
ATOM   948  C  C   . GLN   B 2 87  ? -18.260 -4.181  -25.918 1.00 47.76  ? 96  GLN   B C   1 
ATOM   949  O  O   . GLN   B 2 87  ? -19.041 -4.224  -24.967 1.00 48.18  ? 96  GLN   B O   1 
ATOM   950  C  CB  . GLN   B 2 87  ? -19.563 -4.837  -27.984 1.00 48.63  ? 96  GLN   B CB  1 
ATOM   951  C  CG  . GLN   B 2 87  ? -19.253 -5.234  -29.407 1.00 51.26  ? 96  GLN   B CG  1 
ATOM   952  C  CD  . GLN   B 2 87  ? -20.367 -4.963  -30.383 1.00 54.73  ? 96  GLN   B CD  1 
ATOM   953  O  OE1 . GLN   B 2 87  ? -21.350 -4.272  -30.092 1.00 54.20  ? 96  GLN   B OE1 1 
ATOM   954  N  NE2 . GLN   B 2 87  ? -20.229 -5.522  -31.583 1.00 56.03  ? 96  GLN   B NE2 1 
ATOM   955  N  N   . LEU   B 2 88  ? -17.291 -3.271  -26.022 1.00 46.49  ? 97  LEU   B N   1 
ATOM   956  C  CA  . LEU   B 2 88  ? -17.176 -2.191  -25.068 1.00 45.73  ? 97  LEU   B CA  1 
ATOM   957  C  C   . LEU   B 2 88  ? -18.031 -1.072  -25.666 1.00 45.02  ? 97  LEU   B C   1 
ATOM   958  O  O   . LEU   B 2 88  ? -17.802 -0.655  -26.817 1.00 45.14  ? 97  LEU   B O   1 
ATOM   959  C  CB  . LEU   B 2 88  ? -15.709 -1.737  -24.897 1.00 45.68  ? 97  LEU   B CB  1 
ATOM   960  C  CG  . LEU   B 2 88  ? -15.501 -0.384  -24.200 1.00 46.63  ? 97  LEU   B CG  1 
ATOM   961  C  CD1 . LEU   B 2 88  ? -16.105 -0.383  -22.780 1.00 46.93  ? 97  LEU   B CD1 1 
ATOM   962  C  CD2 . LEU   B 2 88  ? -14.040 -0.016  -24.145 1.00 47.01  ? 97  LEU   B CD2 1 
ATOM   963  N  N   . LEU   B 2 89  ? -19.064 -0.642  -24.930 1.00 43.66  ? 98  LEU   B N   1 
ATOM   964  C  CA  . LEU   B 2 89  ? -19.874 0.470   -25.364 1.00 43.26  ? 98  LEU   B CA  1 
ATOM   965  C  C   . LEU   B 2 89  ? -19.186 1.667   -24.739 1.00 43.93  ? 98  LEU   B C   1 
ATOM   966  O  O   . LEU   B 2 89  ? -19.527 2.100   -23.626 1.00 43.83  ? 98  LEU   B O   1 
ATOM   967  C  CB  . LEU   B 2 89  ? -21.349 0.316   -24.935 1.00 43.27  ? 98  LEU   B CB  1 
ATOM   968  C  CG  . LEU   B 2 89  ? -22.373 1.473   -25.199 1.00 44.75  ? 98  LEU   B CG  1 
ATOM   969  C  CD1 . LEU   B 2 89  ? -22.117 2.212   -26.477 1.00 46.01  ? 98  LEU   B CD1 1 
ATOM   970  C  CD2 . LEU   B 2 89  ? -23.778 0.946   -25.238 1.00 45.05  ? 98  LEU   B CD2 1 
ATOM   971  N  N   . ALA   B 2 90  ? -18.114 2.123   -25.416 1.00 44.28  ? 99  ALA   B N   1 
ATOM   972  C  CA  . ALA   B 2 90  ? -17.307 3.253   -24.967 1.00 44.52  ? 99  ALA   B CA  1 
ATOM   973  C  C   . ALA   B 2 90  ? -18.087 4.537   -25.101 1.00 44.58  ? 99  ALA   B C   1 
ATOM   974  O  O   . ALA   B 2 90  ? -18.573 4.816   -26.192 1.00 45.08  ? 99  ALA   B O   1 
ATOM   975  C  CB  . ALA   B 2 90  ? -16.050 3.359   -25.809 1.00 44.27  ? 99  ALA   B CB  1 
ATOM   976  N  N   . VAL   B 2 91  ? -18.179 5.342   -24.008 1.00 43.71  ? 100 VAL   B N   1 
ATOM   977  C  CA  . VAL   B 2 91  ? -18.834 6.650   -24.026 1.00 43.75  ? 100 VAL   B CA  1 
ATOM   978  C  C   . VAL   B 2 91  ? -17.753 7.667   -23.627 1.00 44.86  ? 100 VAL   B C   1 
ATOM   979  O  O   . VAL   B 2 91  ? -17.597 7.990   -22.452 1.00 45.44  ? 100 VAL   B O   1 
ATOM   980  C  CB  . VAL   B 2 91  ? -20.067 6.687   -23.095 1.00 43.19  ? 100 VAL   B CB  1 
ATOM   981  C  CG1 . VAL   B 2 91  ? -20.745 8.055   -23.130 1.00 43.55  ? 100 VAL   B CG1 1 
ATOM   982  C  CG2 . VAL   B 2 91  ? -21.051 5.583   -23.464 1.00 42.90  ? 100 VAL   B CG2 1 
ATOM   983  N  N   . PRO   B 2 92  ? -16.952 8.136   -24.598 1.00 45.19  ? 101 PRO   B N   1 
ATOM   984  C  CA  . PRO   B 2 92  ? -15.821 9.019   -24.252 1.00 45.36  ? 101 PRO   B CA  1 
ATOM   985  C  C   . PRO   B 2 92  ? -16.198 10.483  -24.060 1.00 45.36  ? 101 PRO   B C   1 
ATOM   986  O  O   . PRO   B 2 92  ? -17.179 10.937  -24.640 1.00 45.24  ? 101 PRO   B O   1 
ATOM   987  C  CB  . PRO   B 2 92  ? -14.825 8.802   -25.415 1.00 46.35  ? 101 PRO   B CB  1 
ATOM   988  C  CG  . PRO   B 2 92  ? -15.583 8.054   -26.490 1.00 46.77  ? 101 PRO   B CG  1 
ATOM   989  C  CD  . PRO   B 2 92  ? -17.006 7.849   -26.046 1.00 44.82  ? 101 PRO   B CD  1 
ATOM   990  N  N   . PRO   B 2 93  ? -15.430 11.244  -23.254 1.00 45.57  ? 102 PRO   B N   1 
ATOM   991  C  CA  . PRO   B 2 93  ? -15.798 12.650  -23.014 1.00 45.92  ? 102 PRO   B CA  1 
ATOM   992  C  C   . PRO   B 2 93  ? -15.926 13.466  -24.296 1.00 47.00  ? 102 PRO   B C   1 
ATOM   993  O  O   . PRO   B 2 93  ? -15.071 13.353  -25.170 1.00 47.52  ? 102 PRO   B O   1 
ATOM   994  C  CB  . PRO   B 2 93  ? -14.682 13.167  -22.102 1.00 46.54  ? 102 PRO   B CB  1 
ATOM   995  C  CG  . PRO   B 2 93  ? -14.138 11.922  -21.421 1.00 47.07  ? 102 PRO   B CG  1 
ATOM   996  C  CD  . PRO   B 2 93  ? -14.250 10.837  -22.458 1.00 45.36  ? 102 PRO   B CD  1 
ATOM   997  N  N   . GLY   B 2 94  ? -17.038 14.198  -24.425 1.00 46.94  ? 103 GLY   B N   1 
ATOM   998  C  CA  . GLY   B 2 94  ? -17.366 15.047  -25.569 1.00 46.83  ? 103 GLY   B CA  1 
ATOM   999  C  C   . GLY   B 2 94  ? -17.645 14.328  -26.881 1.00 47.12  ? 103 GLY   B C   1 
ATOM   1000 O  O   . GLY   B 2 94  ? -17.861 14.968  -27.914 1.00 46.70  ? 103 GLY   B O   1 
ATOM   1001 N  N   . GLU   B 2 95  ? -17.591 12.994  -26.873 1.00 47.52  ? 104 GLU   B N   1 
ATOM   1002 C  CA  . GLU   B 2 95  ? -17.770 12.205  -28.083 1.00 48.30  ? 104 GLU   B CA  1 
ATOM   1003 C  C   . GLU   B 2 95  ? -18.935 11.233  -27.937 1.00 49.00  ? 104 GLU   B C   1 
ATOM   1004 O  O   . GLU   B 2 95  ? -19.247 10.810  -26.829 1.00 48.78  ? 104 GLU   B O   1 
ATOM   1005 C  CB  . GLU   B 2 95  ? -16.463 11.454  -28.429 1.00 50.61  ? 104 GLU   B CB  1 
ATOM   1006 C  CG  . GLU   B 2 95  ? -15.235 12.356  -28.485 1.00 55.47  ? 104 GLU   B CG  1 
ATOM   1007 C  CD  . GLU   B 2 95  ? -13.884 11.680  -28.672 1.00 61.20  ? 104 GLU   B CD  1 
ATOM   1008 O  OE1 . GLU   B 2 95  ? -13.782 10.454  -28.434 1.00 59.80  ? 104 GLU   B OE1 1 
ATOM   1009 O  OE2 . GLU   B 2 95  ? -12.921 12.386  -29.056 1.00 63.73  ? 104 GLU   B OE2 1 
ATOM   1010 N  N   . ARG   B 2 96  ? -19.551 10.859  -29.064 1.00 49.90  ? 105 ARG   B N   1 
ATOM   1011 C  CA  . ARG   B 2 96  ? -20.700 9.959   -29.147 1.00 51.68  ? 105 ARG   B CA  1 
ATOM   1012 C  C   . ARG   B 2 96  ? -20.394 8.544   -28.658 1.00 52.88  ? 105 ARG   B C   1 
ATOM   1013 O  O   . ARG   B 2 96  ? -19.251 8.098   -28.762 1.00 53.17  ? 105 ARG   B O   1 
ATOM   1014 C  CB  . ARG   B 2 96  ? -21.171 9.906   -30.613 1.00 54.38  ? 105 ARG   B CB  1 
ATOM   1015 C  CG  . ARG   B 2 96  ? -22.516 9.234   -30.840 1.00 59.58  ? 105 ARG   B CG  1 
ATOM   1016 C  CD  . ARG   B 2 96  ? -23.306 9.913   -31.940 1.00 64.76  ? 105 ARG   B CD  1 
ATOM   1017 N  NE  . ARG   B 2 96  ? -22.633 9.854   -33.235 1.00 69.69  ? 105 ARG   B NE  1 
ATOM   1018 C  CZ  . ARG   B 2 96  ? -22.161 10.912  -33.891 1.00 74.19  ? 105 ARG   B CZ  1 
ATOM   1019 N  NH1 . ARG   B 2 96  ? -22.274 12.130  -33.372 1.00 74.47  ? 105 ARG   B NH1 1 
ATOM   1020 N  NH2 . ARG   B 2 96  ? -21.585 10.760  -35.078 1.00 74.85  ? 105 ARG   B NH2 1 
ATOM   1021 N  N   . ALA   B 2 97  ? -21.418 7.831   -28.130 1.00 53.28  ? 106 ALA   B N   1 
ATOM   1022 C  CA  . ALA   B 2 97  ? -21.323 6.433   -27.702 1.00 53.74  ? 106 ALA   B CA  1 
ATOM   1023 C  C   . ALA   B 2 97  ? -20.875 5.574   -28.906 1.00 54.99  ? 106 ALA   B C   1 
ATOM   1024 O  O   . ALA   B 2 97  ? -21.313 5.830   -30.029 1.00 55.77  ? 106 ALA   B O   1 
ATOM   1025 C  CB  . ALA   B 2 97  ? -22.677 5.960   -27.206 1.00 53.35  ? 106 ALA   B CB  1 
ATOM   1026 N  N   . LYS   B 2 98  ? -20.010 4.577   -28.691 1.00 55.54  ? 107 LYS   B N   1 
ATOM   1027 C  CA  . LYS   B 2 98  ? -19.447 3.796   -29.799 1.00 56.44  ? 107 LYS   B CA  1 
ATOM   1028 C  C   . LYS   B 2 98  ? -19.118 2.336   -29.409 1.00 55.82  ? 107 LYS   B C   1 
ATOM   1029 O  O   . LYS   B 2 98  ? -18.406 2.122   -28.436 1.00 56.05  ? 107 LYS   B O   1 
ATOM   1030 C  CB  . LYS   B 2 98  ? -18.184 4.548   -30.248 1.00 60.21  ? 107 LYS   B CB  1 
ATOM   1031 C  CG  . LYS   B 2 98  ? -17.371 3.967   -31.390 1.00 67.22  ? 107 LYS   B CG  1 
ATOM   1032 C  CD  . LYS   B 2 98  ? -16.022 4.733   -31.546 1.00 73.61  ? 107 LYS   B CD  1 
ATOM   1033 C  CE  . LYS   B 2 98  ? -15.335 5.012   -30.207 1.00 78.39  ? 107 LYS   B CE  1 
ATOM   1034 N  NZ  . LYS   B 2 98  ? -13.897 5.373   -30.353 1.00 81.24  ? 107 LYS   B NZ  1 
ATOM   1035 N  N   . ASN   B 2 99  ? -19.654 1.337   -30.143 1.00 54.92  ? 108 ASN   B N   1 
ATOM   1036 C  CA  . ASN   B 2 99  ? -19.400 -0.081  -29.837 1.00 54.54  ? 108 ASN   B CA  1 
ATOM   1037 C  C   . ASN   B 2 99  ? -18.082 -0.546  -30.430 1.00 55.02  ? 108 ASN   B C   1 
ATOM   1038 O  O   . ASN   B 2 99  ? -17.835 -0.371  -31.630 1.00 56.23  ? 108 ASN   B O   1 
ATOM   1039 C  CB  . ASN   B 2 99  ? -20.529 -1.000  -30.318 1.00 54.84  ? 108 ASN   B CB  1 
ATOM   1040 C  CG  . ASN   B 2 99  ? -21.850 -0.794  -29.614 1.00 57.61  ? 108 ASN   B CG  1 
ATOM   1041 O  OD1 . ASN   B 2 99  ? -22.413 0.301   -29.620 1.00 59.57  ? 108 ASN   B OD1 1 
ATOM   1042 N  ND2 . ASN   B 2 99  ? -22.397 -1.842  -29.022 1.00 56.72  ? 108 ASN   B ND2 1 
ATOM   1043 N  N   . ILE   B 2 100 ? -17.236 -1.141  -29.604 1.00 53.49  ? 109 ILE   B N   1 
ATOM   1044 C  CA  . ILE   B 2 100 ? -15.930 -1.604  -30.028 1.00 53.44  ? 109 ILE   B CA  1 
ATOM   1045 C  C   . ILE   B 2 100 ? -15.764 -3.073  -29.663 1.00 53.42  ? 109 ILE   B C   1 
ATOM   1046 O  O   . ILE   B 2 100 ? -15.584 -3.406  -28.493 1.00 53.70  ? 109 ILE   B O   1 
ATOM   1047 C  CB  . ILE   B 2 100 ? -14.814 -0.770  -29.378 1.00 53.65  ? 109 ILE   B CB  1 
ATOM   1048 C  CG1 . ILE   B 2 100 ? -15.073 0.748   -29.481 1.00 54.65  ? 109 ILE   B CG1 1 
ATOM   1049 C  CG2 . ILE   B 2 100 ? -13.461 -1.174  -29.948 1.00 53.74  ? 109 ILE   B CG2 1 
ATOM   1050 C  CD1 . ILE   B 2 100 ? -14.864 1.348   -30.879 1.00 56.20  ? 109 ILE   B CD1 1 
ATOM   1051 N  N   . GLN   B 2 101 ? -15.839 -3.947  -30.654 1.00 52.83  ? 110 GLN   B N   1 
ATOM   1052 C  CA  . GLN   B 2 101 ? -15.735 -5.378  -30.453 1.00 53.19  ? 110 GLN   B CA  1 
ATOM   1053 C  C   . GLN   B 2 101 ? -14.305 -5.806  -30.246 1.00 53.98  ? 110 GLN   B C   1 
ATOM   1054 O  O   . GLN   B 2 101 ? -13.422 -5.362  -30.975 1.00 54.65  ? 110 GLN   B O   1 
ATOM   1055 C  CB  . GLN   B 2 101 ? -16.321 -6.103  -31.659 1.00 54.37  ? 110 GLN   B CB  1 
ATOM   1056 C  CG  . GLN   B 2 101 ? -16.473 -7.594  -31.468 1.00 56.67  ? 110 GLN   B CG  1 
ATOM   1057 C  CD  . GLN   B 2 101 ? -17.460 -8.142  -32.451 1.00 61.18  ? 110 GLN   B CD  1 
ATOM   1058 O  OE1 . GLN   B 2 101 ? -18.489 -7.521  -32.752 1.00 61.97  ? 110 GLN   B OE1 1 
ATOM   1059 N  NE2 . GLN   B 2 101 ? -17.163 -9.317  -32.982 1.00 62.91  ? 110 GLN   B NE2 1 
ATOM   1060 N  N   . THR   B 2 102 ? -14.069 -6.699  -29.265 1.00 53.51  ? 111 THR   B N   1 
ATOM   1061 C  CA  . THR   B 2 102 ? -12.734 -7.222  -28.973 1.00 53.34  ? 111 THR   B CA  1 
ATOM   1062 C  C   . THR   B 2 102 ? -12.812 -8.597  -28.309 1.00 53.51  ? 111 THR   B C   1 
ATOM   1063 O  O   . THR   B 2 102 ? -13.865 -8.960  -27.786 1.00 54.01  ? 111 THR   B O   1 
ATOM   1064 C  CB  . THR   B 2 102 ? -11.979 -6.240  -28.041 1.00 53.30  ? 111 THR   B CB  1 
ATOM   1065 O  OG1 . THR   B 2 102 ? -10.603 -6.630  -27.957 1.00 52.79  ? 111 THR   B OG1 1 
ATOM   1066 C  CG2 . THR   B 2 102 ? -12.612 -6.123  -26.650 1.00 53.28  ? 111 THR   B CG2 1 
ATOM   1067 N  N   . LEU   B 2 103 ? -11.717 -9.372  -28.336 1.00 53.10  ? 112 LEU   B N   1 
ATOM   1068 C  CA  . LEU   B 2 103 ? -11.694 -10.640 -27.604 1.00 53.06  ? 112 LEU   B CA  1 
ATOM   1069 C  C   . LEU   B 2 103 ? -10.892 -10.356 -26.350 1.00 53.44  ? 112 LEU   B C   1 
ATOM   1070 O  O   . LEU   B 2 103 ? -9.705  -10.008 -26.440 1.00 52.97  ? 112 LEU   B O   1 
ATOM   1071 C  CB  . LEU   B 2 103 ? -11.057 -11.818 -28.356 1.00 53.20  ? 112 LEU   B CB  1 
ATOM   1072 C  CG  . LEU   B 2 103 ? -10.985 -13.106 -27.518 1.00 54.50  ? 112 LEU   B CG  1 
ATOM   1073 C  CD1 . LEU   B 2 103 ? -12.281 -13.852 -27.563 1.00 54.71  ? 112 LEU   B CD1 1 
ATOM   1074 C  CD2 . LEU   B 2 103 ? -9.859  -13.994 -27.952 1.00 55.80  ? 112 LEU   B CD2 1 
ATOM   1075 N  N   . PRO   B 2 104 ? -11.507 -10.550 -25.171 1.00 53.51  ? 113 PRO   B N   1 
ATOM   1076 C  CA  . PRO   B 2 104 ? -10.782 -10.286 -23.925 1.00 53.71  ? 113 PRO   B CA  1 
ATOM   1077 C  C   . PRO   B 2 104 ? -9.656  -11.254 -23.587 1.00 54.58  ? 113 PRO   B C   1 
ATOM   1078 O  O   . PRO   B 2 104 ? -9.647  -12.426 -23.969 1.00 55.08  ? 113 PRO   B O   1 
ATOM   1079 C  CB  . PRO   B 2 104 ? -11.880 -10.314 -22.846 1.00 53.87  ? 113 PRO   B CB  1 
ATOM   1080 C  CG  . PRO   B 2 104 ? -13.186 -10.260 -23.582 1.00 54.23  ? 113 PRO   B CG  1 
ATOM   1081 C  CD  . PRO   B 2 104 ? -12.906 -10.931 -24.913 1.00 52.93  ? 113 PRO   B CD  1 
ATOM   1082 N  N   . GLY   B 2 105 ? -8.688  -10.708 -22.875 1.00 54.79  ? 114 GLY   B N   1 
ATOM   1083 C  CA  . GLY   B 2 105 ? -7.580  -11.426 -22.278 1.00 55.43  ? 114 GLY   B CA  1 
ATOM   1084 C  C   . GLY   B 2 105 ? -7.946  -11.846 -20.863 1.00 56.14  ? 114 GLY   B C   1 
ATOM   1085 O  O   . GLY   B 2 105 ? -9.127  -11.878 -20.506 1.00 56.53  ? 114 GLY   B O   1 
ATOM   1086 N  N   . ILE   B 2 106 ? -6.942  -12.159 -20.041 1.00 55.84  ? 115 ILE   B N   1 
ATOM   1087 C  CA  . ILE   B 2 106 ? -7.121  -12.646 -18.675 1.00 56.39  ? 115 ILE   B CA  1 
ATOM   1088 C  C   . ILE   B 2 106 ? -6.227  -11.905 -17.685 1.00 55.54  ? 115 ILE   B C   1 
ATOM   1089 O  O   . ILE   B 2 106 ? -5.040  -11.724 -17.940 1.00 55.54  ? 115 ILE   B O   1 
ATOM   1090 C  CB  . ILE   B 2 106 ? -6.728  -14.168 -18.623 1.00 57.96  ? 115 ILE   B CB  1 
ATOM   1091 C  CG1 . ILE   B 2 106 ? -7.634  -15.050 -19.487 1.00 59.77  ? 115 ILE   B CG1 1 
ATOM   1092 C  CG2 . ILE   B 2 106 ? -6.675  -14.702 -17.197 1.00 58.97  ? 115 ILE   B CG2 1 
ATOM   1093 C  CD1 . ILE   B 2 106 ? -9.067  -15.002 -19.064 1.00 61.68  ? 115 ILE   B CD1 1 
ATOM   1094 N  N   . PHE   B 2 107 ? -6.775  -11.582 -16.514 1.00 54.85  ? 116 PHE   B N   1 
ATOM   1095 C  CA  . PHE   B 2 107 ? -6.051  -11.077 -15.358 1.00 54.13  ? 116 PHE   B CA  1 
ATOM   1096 C  C   . PHE   B 2 107 ? -5.978  -12.305 -14.470 1.00 54.92  ? 116 PHE   B C   1 
ATOM   1097 O  O   . PHE   B 2 107 ? -7.017  -12.783 -14.018 1.00 55.29  ? 116 PHE   B O   1 
ATOM   1098 C  CB  . PHE   B 2 107 ? -6.870  -10.010 -14.613 1.00 53.30  ? 116 PHE   B CB  1 
ATOM   1099 C  CG  . PHE   B 2 107 ? -6.654  -8.570  -15.013 1.00 52.83  ? 116 PHE   B CG  1 
ATOM   1100 C  CD1 . PHE   B 2 107 ? -5.912  -8.249  -16.141 1.00 53.10  ? 116 PHE   B CD1 1 
ATOM   1101 C  CD2 . PHE   B 2 107 ? -7.192  -7.539  -14.260 1.00 52.96  ? 116 PHE   B CD2 1 
ATOM   1102 C  CE1 . PHE   B 2 107 ? -5.733  -6.926  -16.519 1.00 53.67  ? 116 PHE   B CE1 1 
ATOM   1103 C  CE2 . PHE   B 2 107 ? -7.001  -6.215  -14.631 1.00 53.75  ? 116 PHE   B CE2 1 
ATOM   1104 C  CZ  . PHE   B 2 107 ? -6.287  -5.916  -15.768 1.00 53.62  ? 116 PHE   B CZ  1 
ATOM   1105 N  N   . LYS   B 2 108 ? -4.783  -12.860 -14.261 1.00 55.06  ? 117 LYS   B N   1 
ATOM   1106 C  CA  . LYS   B 2 108 ? -4.614  -14.023 -13.406 1.00 55.60  ? 117 LYS   B CA  1 
ATOM   1107 C  C   . LYS   B 2 108 ? -4.329  -13.483 -12.017 1.00 55.30  ? 117 LYS   B C   1 
ATOM   1108 O  O   . LYS   B 2 108 ? -3.379  -12.721 -11.857 1.00 55.40  ? 117 LYS   B O   1 
ATOM   1109 C  CB  . LYS   B 2 108 ? -3.424  -14.898 -13.878 1.00 58.62  ? 117 LYS   B CB  1 
ATOM   1110 C  CG  . LYS   B 2 108 ? -3.306  -15.049 -15.400 1.00 64.21  ? 117 LYS   B CG  1 
ATOM   1111 C  CD  . LYS   B 2 108 ? -2.349  -16.167 -15.800 1.00 71.31  ? 117 LYS   B CD  1 
ATOM   1112 C  CE  . LYS   B 2 108 ? -1.597  -15.861 -17.081 1.00 77.40  ? 117 LYS   B CE  1 
ATOM   1113 N  NZ  . LYS   B 2 108 ? -1.261  -17.091 -17.868 1.00 80.79  ? 117 LYS   B NZ  1 
ATOM   1114 N  N   . THR   B 2 109 ? -5.173  -13.813 -11.026 1.00 54.71  ? 118 THR   B N   1 
ATOM   1115 C  CA  . THR   B 2 109 ? -4.980  -13.347 -9.642  1.00 54.91  ? 118 THR   B CA  1 
ATOM   1116 C  C   . THR   B 2 109 ? -4.879  -14.529 -8.665  1.00 54.64  ? 118 THR   B C   1 
ATOM   1117 O  O   . THR   B 2 109 ? -5.248  -15.649 -9.025  1.00 54.20  ? 118 THR   B O   1 
ATOM   1118 C  CB  . THR   B 2 109 ? -6.097  -12.341 -9.202  1.00 55.94  ? 118 THR   B CB  1 
ATOM   1119 O  OG1 . THR   B 2 109 ? -7.260  -13.029 -8.727  1.00 56.56  ? 118 THR   B OG1 1 
ATOM   1120 C  CG2 . THR   B 2 109 ? -6.459  -11.333 -10.275 1.00 56.16  ? 118 THR   B CG2 1 
ATOM   1121 N  N   . LYS   B 2 110 ? -4.430  -14.275 -7.409  1.00 54.77  ? 119 LYS   B N   1 
ATOM   1122 C  CA  . LYS   B 2 110 ? -4.376  -15.311 -6.375  1.00 55.13  ? 119 LYS   B CA  1 
ATOM   1123 C  C   . LYS   B 2 110 ? -5.798  -15.814 -6.012  1.00 56.17  ? 119 LYS   B C   1 
ATOM   1124 O  O   . LYS   B 2 110 ? -5.946  -16.936 -5.528  1.00 56.98  ? 119 LYS   B O   1 
ATOM   1125 C  CB  . LYS   B 2 110 ? -3.630  -14.808 -5.121  1.00 55.96  ? 119 LYS   B CB  1 
ATOM   1126 C  CG  . LYS   B 2 110 ? -4.387  -13.743 -4.336  1.00 58.60  ? 119 LYS   B CG  1 
ATOM   1127 C  CD  . LYS   B 2 110 ? -3.524  -13.089 -3.276  1.00 62.36  ? 119 LYS   B CD  1 
ATOM   1128 C  CE  . LYS   B 2 110 ? -4.291  -12.705 -2.034  1.00 65.73  ? 119 LYS   B CE  1 
ATOM   1129 N  NZ  . LYS   B 2 110 ? -5.103  -11.473 -2.220  1.00 68.13  ? 119 LYS   B NZ  1 
ATOM   1130 N  N   . ASP   B 2 111 ? -6.834  -15.007 -6.270  1.00 56.13  ? 120 ASP   B N   1 
ATOM   1131 C  CA  . ASP   B 2 111 ? -8.219  -15.370 -6.011  1.00 57.00  ? 120 ASP   B CA  1 
ATOM   1132 C  C   . ASP   B 2 111 ? -8.983  -15.801 -7.268  1.00 57.96  ? 120 ASP   B C   1 
ATOM   1133 O  O   . ASP   B 2 111 ? -10.202 -15.915 -7.203  1.00 59.10  ? 120 ASP   B O   1 
ATOM   1134 C  CB  . ASP   B 2 111 ? -8.957  -14.191 -5.368  1.00 58.87  ? 120 ASP   B CB  1 
ATOM   1135 C  CG  . ASP   B 2 111 ? -8.373  -13.765 -4.043  1.00 63.33  ? 120 ASP   B CG  1 
ATOM   1136 O  OD1 . ASP   B 2 111 ? -7.946  -14.657 -3.268  1.00 63.88  ? 120 ASP   B OD1 1 
ATOM   1137 O  OD2 . ASP   B 2 111 ? -8.347  -12.540 -3.773  1.00 65.46  ? 120 ASP   B OD2 1 
ATOM   1138 N  N   . GLY   B 2 112 ? -8.302  -16.006 -8.395  1.00 57.30  ? 121 GLY   B N   1 
ATOM   1139 C  CA  . GLY   B 2 112 ? -8.965  -16.434 -9.621  1.00 56.97  ? 121 GLY   B CA  1 
ATOM   1140 C  C   . GLY   B 2 112 ? -8.736  -15.568 -10.840 1.00 55.82  ? 121 GLY   B C   1 
ATOM   1141 O  O   . GLY   B 2 112 ? -8.265  -14.439 -10.725 1.00 55.62  ? 121 GLY   B O   1 
ATOM   1142 N  N   . ASP   B 2 113 ? -9.076  -16.099 -12.021 1.00 55.07  ? 122 ASP   B N   1 
ATOM   1143 C  CA  . ASP   B 2 113 ? -8.948  -15.386 -13.297 1.00 54.69  ? 122 ASP   B CA  1 
ATOM   1144 C  C   . ASP   B 2 113 ? -10.167 -14.524 -13.562 1.00 53.79  ? 122 ASP   B C   1 
ATOM   1145 O  O   . ASP   B 2 113 ? -11.287 -14.931 -13.246 1.00 54.07  ? 122 ASP   B O   1 
ATOM   1146 C  CB  . ASP   B 2 113 ? -8.800  -16.365 -14.464 1.00 56.46  ? 122 ASP   B CB  1 
ATOM   1147 C  CG  . ASP   B 2 113 ? -7.517  -17.153 -14.483 1.00 62.35  ? 122 ASP   B CG  1 
ATOM   1148 O  OD1 . ASP   B 2 113 ? -6.595  -16.807 -13.716 1.00 63.82  ? 122 ASP   B OD1 1 
ATOM   1149 O  OD2 . ASP   B 2 113 ? -7.428  -18.118 -15.275 1.00 65.40  ? 122 ASP   B OD2 1 
ATOM   1150 N  N   . ILE   B 2 114 ? -9.945  -13.347 -14.182 1.00 52.33  ? 123 ILE   B N   1 
ATOM   1151 C  CA  . ILE   B 2 114 ? -10.969 -12.367 -14.541 1.00 51.38  ? 123 ILE   B CA  1 
ATOM   1152 C  C   . ILE   B 2 114 ? -10.717 -11.968 -16.001 1.00 50.11  ? 123 ILE   B C   1 
ATOM   1153 O  O   . ILE   B 2 114 ? -9.569  -11.764 -16.384 1.00 49.20  ? 123 ILE   B O   1 
ATOM   1154 C  CB  . ILE   B 2 114 ? -10.839 -11.070 -13.668 1.00 51.79  ? 123 ILE   B CB  1 
ATOM   1155 C  CG1 . ILE   B 2 114 ? -10.619 -11.349 -12.193 1.00 53.50  ? 123 ILE   B CG1 1 
ATOM   1156 C  CG2 . ILE   B 2 114 ? -12.006 -10.112 -13.853 1.00 52.23  ? 123 ILE   B CG2 1 
ATOM   1157 C  CD1 . ILE   B 2 114 ? -10.048 -10.106 -11.460 1.00 55.14  ? 123 ILE   B CD1 1 
ATOM   1158 N  N   . GLY   B 2 115 ? -11.780 -11.744 -16.768 1.00 49.72  ? 124 GLY   B N   1 
ATOM   1159 C  CA  . GLY   B 2 115 ? -11.645 -11.247 -18.135 1.00 49.66  ? 124 GLY   B CA  1 
ATOM   1160 C  C   . GLY   B 2 115 ? -11.066 -9.840  -18.136 1.00 49.54  ? 124 GLY   B C   1 
ATOM   1161 O  O   . GLY   B 2 115 ? -11.177 -9.108  -17.138 1.00 48.94  ? 124 GLY   B O   1 
ATOM   1162 N  N   . ALA   B 2 116 ? -10.392 -9.467  -19.221 1.00 49.64  ? 125 ALA   B N   1 
ATOM   1163 C  CA  . ALA   B 2 116 ? -9.777  -8.148  -19.314 1.00 50.09  ? 125 ALA   B CA  1 
ATOM   1164 C  C   . ALA   B 2 116 ? -9.794  -7.604  -20.751 1.00 50.46  ? 125 ALA   B C   1 
ATOM   1165 O  O   . ALA   B 2 116 ? -9.341  -8.287  -21.644 1.00 50.09  ? 125 ALA   B O   1 
ATOM   1166 C  CB  . ALA   B 2 116 ? -8.349  -8.206  -18.781 1.00 49.94  ? 125 ALA   B CB  1 
ATOM   1167 N  N   . VAL   B 2 117 ? -10.303 -6.386  -20.971 1.00 50.97  ? 126 VAL   B N   1 
ATOM   1168 C  CA  . VAL   B 2 117 ? -10.340 -5.791  -22.296 1.00 52.69  ? 126 VAL   B CA  1 
ATOM   1169 C  C   . VAL   B 2 117 ? -9.136  -4.861  -22.525 1.00 53.53  ? 126 VAL   B C   1 
ATOM   1170 O  O   . VAL   B 2 117 ? -8.858  -3.976  -21.707 1.00 53.91  ? 126 VAL   B O   1 
ATOM   1171 C  CB  . VAL   B 2 117 ? -11.694 -5.121  -22.641 1.00 53.98  ? 126 VAL   B CB  1 
ATOM   1172 C  CG1 . VAL   B 2 117 ? -12.791 -6.169  -22.773 1.00 54.93  ? 126 VAL   B CG1 1 
ATOM   1173 C  CG2 . VAL   B 2 117 ? -12.073 -4.076  -21.612 1.00 54.46  ? 126 VAL   B CG2 1 
ATOM   1174 N  N   . ALA   B 2 118 ? -8.400  -5.091  -23.619 1.00 53.12  ? 127 ALA   B N   1 
ATOM   1175 C  CA  . ALA   B 2 118 ? -7.219  -4.293  -23.922 1.00 54.38  ? 127 ALA   B CA  1 
ATOM   1176 C  C   . ALA   B 2 118 ? -7.538  -3.186  -24.920 1.00 55.64  ? 127 ALA   B C   1 
ATOM   1177 O  O   . ALA   B 2 118 ? -7.198  -3.273  -26.105 1.00 56.65  ? 127 ALA   B O   1 
ATOM   1178 C  CB  . ALA   B 2 118 ? -6.110  -5.186  -24.451 1.00 54.89  ? 127 ALA   B CB  1 
ATOM   1179 N  N   . LEU   B 2 119 ? -8.250  -2.158  -24.448 1.00 55.11  ? 128 LEU   B N   1 
ATOM   1180 C  CA  . LEU   B 2 119 ? -8.661  -1.022  -25.261 1.00 54.73  ? 128 LEU   B CA  1 
ATOM   1181 C  C   . LEU   B 2 119 ? -8.256  0.273   -24.535 1.00 54.53  ? 128 LEU   B C   1 
ATOM   1182 O  O   . LEU   B 2 119 ? -8.325  0.337   -23.310 1.00 54.16  ? 128 LEU   B O   1 
ATOM   1183 C  CB  . LEU   B 2 119 ? -10.188 -1.073  -25.492 1.00 54.83  ? 128 LEU   B CB  1 
ATOM   1184 C  CG  . LEU   B 2 119 ? -10.686 -2.229  -26.366 1.00 55.60  ? 128 LEU   B CG  1 
ATOM   1185 C  CD1 . LEU   B 2 119 ? -12.196 -2.287  -26.416 1.00 55.51  ? 128 LEU   B CD1 1 
ATOM   1186 C  CD2 . LEU   B 2 119 ? -10.132 -2.123  -27.769 1.00 56.37  ? 128 LEU   B CD2 1 
ATOM   1187 N  N   . ASP   B 2 120 ? -7.850  1.302   -25.283 1.00 54.76  ? 129 ASP   B N   1 
ATOM   1188 C  CA  . ASP   B 2 120 ? -7.405  2.556   -24.684 1.00 55.65  ? 129 ASP   B CA  1 
ATOM   1189 C  C   . ASP   B 2 120 ? -8.345  3.713   -24.816 1.00 55.08  ? 129 ASP   B C   1 
ATOM   1190 O  O   . ASP   B 2 120 ? -8.563  4.192   -25.926 1.00 55.97  ? 129 ASP   B O   1 
ATOM   1191 C  CB  . ASP   B 2 120 ? -6.070  2.977   -25.266 1.00 58.94  ? 129 ASP   B CB  1 
ATOM   1192 C  CG  . ASP   B 2 120 ? -4.974  2.783   -24.262 1.00 65.09  ? 129 ASP   B CG  1 
ATOM   1193 O  OD1 . ASP   B 2 120 ? -4.883  3.602   -23.311 1.00 66.41  ? 129 ASP   B OD1 1 
ATOM   1194 O  OD2 . ASP   B 2 120 ? -4.230  1.800   -24.397 1.00 67.52  ? 129 ASP   B OD2 1 
ATOM   1195 N  N   . TYR   B 2 121 ? -8.795  4.247   -23.682 1.00 53.58  ? 130 TYR   B N   1 
ATOM   1196 C  CA  . TYR   B 2 121 ? -9.713  5.373   -23.623 1.00 53.02  ? 130 TYR   B CA  1 
ATOM   1197 C  C   . TYR   B 2 121 ? -9.353  6.334   -22.486 1.00 52.39  ? 130 TYR   B C   1 
ATOM   1198 O  O   . TYR   B 2 121 ? -8.720  5.930   -21.500 1.00 52.75  ? 130 TYR   B O   1 
ATOM   1199 C  CB  . TYR   B 2 121 ? -11.153 4.854   -23.461 1.00 53.38  ? 130 TYR   B CB  1 
ATOM   1200 C  CG  . TYR   B 2 121 ? -11.710 4.297   -24.748 1.00 54.59  ? 130 TYR   B CG  1 
ATOM   1201 C  CD1 . TYR   B 2 121 ? -12.168 5.139   -25.751 1.00 55.66  ? 130 TYR   B CD1 1 
ATOM   1202 C  CD2 . TYR   B 2 121 ? -11.709 2.932   -24.994 1.00 55.41  ? 130 TYR   B CD2 1 
ATOM   1203 C  CE1 . TYR   B 2 121 ? -12.633 4.635   -26.957 1.00 56.61  ? 130 TYR   B CE1 1 
ATOM   1204 C  CE2 . TYR   B 2 121 ? -12.177 2.416   -26.193 1.00 56.43  ? 130 TYR   B CE2 1 
ATOM   1205 C  CZ  . TYR   B 2 121 ? -12.638 3.273   -27.172 1.00 57.73  ? 130 TYR   B CZ  1 
ATOM   1206 O  OH  . TYR   B 2 121 ? -13.093 2.772   -28.359 1.00 59.98  ? 130 TYR   B OH  1 
ATOM   1207 N  N   . PRO   B 2 122 ? -9.776  7.613   -22.587 1.00 51.35  ? 131 PRO   B N   1 
ATOM   1208 C  CA  . PRO   B 2 122 ? -9.490  8.565   -21.499 1.00 50.25  ? 131 PRO   B CA  1 
ATOM   1209 C  C   . PRO   B 2 122 ? -10.076 8.104   -20.160 1.00 48.21  ? 131 PRO   B C   1 
ATOM   1210 O  O   . PRO   B 2 122 ? -11.064 7.361   -20.153 1.00 49.03  ? 131 PRO   B O   1 
ATOM   1211 C  CB  . PRO   B 2 122 ? -10.169 9.863   -21.972 1.00 51.43  ? 131 PRO   B CB  1 
ATOM   1212 C  CG  . PRO   B 2 122 ? -10.336 9.715   -23.452 1.00 52.37  ? 131 PRO   B CG  1 
ATOM   1213 C  CD  . PRO   B 2 122 ? -10.551 8.244   -23.676 1.00 51.13  ? 131 PRO   B CD  1 
ATOM   1214 N  N   . ALA   B 2 123 ? -9.487  8.541   -19.031 1.00 45.09  ? 132 ALA   B N   1 
ATOM   1215 C  CA  . ALA   B 2 123 ? -9.980  8.140   -17.716 1.00 42.80  ? 132 ALA   B CA  1 
ATOM   1216 C  C   . ALA   B 2 123 ? -11.474 8.430   -17.496 1.00 40.36  ? 132 ALA   B C   1 
ATOM   1217 O  O   . ALA   B 2 123 ? -12.143 7.639   -16.842 1.00 38.80  ? 132 ALA   B O   1 
ATOM   1218 C  CB  . ALA   B 2 123 ? -9.134  8.752   -16.615 1.00 42.65  ? 132 ALA   B CB  1 
ATOM   1219 N  N   . GLY   B 2 124 ? -11.995 9.486   -18.140 1.00 39.88  ? 133 GLY   B N   1 
ATOM   1220 C  CA  . GLY   B 2 124 ? -13.409 9.852   -18.090 1.00 39.38  ? 133 GLY   B CA  1 
ATOM   1221 C  C   . GLY   B 2 124 ? -14.356 8.857   -18.742 1.00 38.90  ? 133 GLY   B C   1 
ATOM   1222 O  O   . GLY   B 2 124 ? -15.565 8.972   -18.600 1.00 38.60  ? 133 GLY   B O   1 
ATOM   1223 N  N   . THR   B 2 125 ? -13.831 7.876   -19.473 1.00 39.44  ? 134 THR   B N   1 
ATOM   1224 C  CA  . THR   B 2 125 ? -14.624 6.784   -20.065 1.00 40.22  ? 134 THR   B CA  1 
ATOM   1225 C  C   . THR   B 2 125 ? -14.997 5.695   -18.985 1.00 39.68  ? 134 THR   B C   1 
ATOM   1226 O  O   . THR   B 2 125 ? -15.769 4.784   -19.287 1.00 40.60  ? 134 THR   B O   1 
ATOM   1227 C  CB  . THR   B 2 125 ? -13.853 6.185   -21.279 1.00 42.24  ? 134 THR   B CB  1 
ATOM   1228 O  OG1 . THR   B 2 125 ? -13.508 7.233   -22.191 1.00 43.11  ? 134 THR   B OG1 1 
ATOM   1229 C  CG2 . THR   B 2 125 ? -14.641 5.128   -22.041 1.00 43.10  ? 134 THR   B CG2 1 
ATOM   1230 N  N   . SER   B 2 126 ? -14.444 5.780   -17.753 1.00 38.27  ? 135 SER   B N   1 
ATOM   1231 C  CA  . SER   B 2 126 ? -14.692 4.815   -16.665 1.00 38.37  ? 135 SER   B CA  1 
ATOM   1232 C  C   . SER   B 2 126 ? -16.164 4.577   -16.388 1.00 38.00  ? 135 SER   B C   1 
ATOM   1233 O  O   . SER   B 2 126 ? -16.901 5.527   -16.240 1.00 38.66  ? 135 SER   B O   1 
ATOM   1234 C  CB  . SER   B 2 126 ? -14.048 5.287   -15.368 1.00 39.08  ? 135 SER   B CB  1 
ATOM   1235 O  OG  . SER   B 2 126 ? -12.652 5.486   -15.496 1.00 41.67  ? 135 SER   B OG  1 
ATOM   1236 N  N   . GLY   B 2 127 ? -16.564 3.321   -16.290 1.00 36.61  ? 136 GLY   B N   1 
ATOM   1237 C  CA  . GLY   B 2 127 ? -17.941 2.935   -16.051 1.00 36.44  ? 136 GLY   B CA  1 
ATOM   1238 C  C   . GLY   B 2 127 ? -18.669 2.474   -17.302 1.00 36.87  ? 136 GLY   B C   1 
ATOM   1239 O  O   . GLY   B 2 127 ? -19.818 2.038   -17.209 1.00 36.71  ? 136 GLY   B O   1 
ATOM   1240 N  N   . SER   B 2 128 ? -18.018 2.571   -18.495 1.00 37.03  ? 137 SER   B N   1 
ATOM   1241 C  CA  . SER   B 2 128 ? -18.606 2.163   -19.768 1.00 37.54  ? 137 SER   B CA  1 
ATOM   1242 C  C   . SER   B 2 128 ? -18.866 0.661   -19.737 1.00 38.09  ? 137 SER   B C   1 
ATOM   1243 O  O   . SER   B 2 128 ? -17.995 -0.106  -19.361 1.00 38.22  ? 137 SER   B O   1 
ATOM   1244 C  CB  . SER   B 2 128 ? -17.687 2.539   -20.932 1.00 38.83  ? 137 SER   B CB  1 
ATOM   1245 O  OG  . SER   B 2 128 ? -17.757 3.929   -21.221 1.00 40.84  ? 137 SER   B OG  1 
ATOM   1246 N  N   . PRO   B 2 129 ? -20.090 0.235   -20.080 1.00 38.31  ? 138 PRO   B N   1 
ATOM   1247 C  CA  . PRO   B 2 129 ? -20.406 -1.197  -20.018 1.00 38.30  ? 138 PRO   B CA  1 
ATOM   1248 C  C   . PRO   B 2 129 ? -19.775 -2.058  -21.095 1.00 40.34  ? 138 PRO   B C   1 
ATOM   1249 O  O   . PRO   B 2 129 ? -19.548 -1.616  -22.235 1.00 41.15  ? 138 PRO   B O   1 
ATOM   1250 C  CB  . PRO   B 2 129 ? -21.927 -1.221  -20.134 1.00 38.03  ? 138 PRO   B CB  1 
ATOM   1251 C  CG  . PRO   B 2 129 ? -22.252 0.022   -20.969 1.00 38.60  ? 138 PRO   B CG  1 
ATOM   1252 C  CD  . PRO   B 2 129 ? -21.245 1.044   -20.540 1.00 37.34  ? 138 PRO   B CD  1 
ATOM   1253 N  N   . ILE   B 2 130 ? -19.536 -3.322  -20.731 1.00 40.46  ? 139 ILE   B N   1 
ATOM   1254 C  CA  . ILE   B 2 130 ? -19.015 -4.351  -21.612 1.00 41.14  ? 139 ILE   B CA  1 
ATOM   1255 C  C   . ILE   B 2 130 ? -20.178 -5.319  -21.803 1.00 42.90  ? 139 ILE   B C   1 
ATOM   1256 O  O   . ILE   B 2 130 ? -20.825 -5.708  -20.835 1.00 42.73  ? 139 ILE   B O   1 
ATOM   1257 C  CB  . ILE   B 2 130 ? -17.766 -5.013  -21.011 1.00 40.54  ? 139 ILE   B CB  1 
ATOM   1258 C  CG1 . ILE   B 2 130 ? -16.651 -3.980  -20.824 1.00 41.24  ? 139 ILE   B CG1 1 
ATOM   1259 C  CG2 . ILE   B 2 130 ? -17.297 -6.195  -21.860 1.00 40.56  ? 139 ILE   B CG2 1 
ATOM   1260 C  CD1 . ILE   B 2 130 ? -15.741 -4.328  -19.701 1.00 42.46  ? 139 ILE   B CD1 1 
ATOM   1261 N  N   . LEU   B 2 131 ? -20.485 -5.654  -23.049 1.00 44.30  ? 140 LEU   B N   1 
ATOM   1262 C  CA  . LEU   B 2 131 ? -21.670 -6.432  -23.390 1.00 46.50  ? 140 LEU   B CA  1 
ATOM   1263 C  C   . LEU   B 2 131 ? -21.386 -7.762  -24.057 1.00 48.15  ? 140 LEU   B C   1 
ATOM   1264 O  O   . LEU   B 2 131 ? -20.421 -7.886  -24.800 1.00 48.58  ? 140 LEU   B O   1 
ATOM   1265 C  CB  . LEU   B 2 131 ? -22.558 -5.623  -24.366 1.00 46.94  ? 140 LEU   B CB  1 
ATOM   1266 C  CG  . LEU   B 2 131 ? -22.540 -4.104  -24.265 1.00 48.60  ? 140 LEU   B CG  1 
ATOM   1267 C  CD1 . LEU   B 2 131 ? -23.223 -3.478  -25.452 1.00 48.76  ? 140 LEU   B CD1 1 
ATOM   1268 C  CD2 . LEU   B 2 131 ? -23.110 -3.641  -22.944 1.00 49.15  ? 140 LEU   B CD2 1 
ATOM   1269 N  N   . ASP   B 2 132 ? -22.280 -8.734  -23.859 1.00 49.00  ? 141 ASP   B N   1 
ATOM   1270 C  CA  . ASP   B 2 132 ? -22.179 -10.017 -24.545 1.00 50.17  ? 141 ASP   B CA  1 
ATOM   1271 C  C   . ASP   B 2 132 ? -23.014 -9.963  -25.855 1.00 52.31  ? 141 ASP   B C   1 
ATOM   1272 O  O   . ASP   B 2 132 ? -23.688 -8.963  -26.115 1.00 52.36  ? 141 ASP   B O   1 
ATOM   1273 C  CB  . ASP   B 2 132 ? -22.576 -11.194 -23.631 1.00 50.76  ? 141 ASP   B CB  1 
ATOM   1274 C  CG  . ASP   B 2 132 ? -24.008 -11.217 -23.143 1.00 54.84  ? 141 ASP   B CG  1 
ATOM   1275 O  OD1 . ASP   B 2 132 ? -24.873 -10.609 -23.802 1.00 55.66  ? 141 ASP   B OD1 1 
ATOM   1276 O  OD2 . ASP   B 2 132 ? -24.266 -11.850 -22.101 1.00 57.05  ? 141 ASP   B OD2 1 
ATOM   1277 N  N   . LYS   B 2 133 ? -22.978 -11.024 -26.667 1.00 53.71  ? 142 LYS   B N   1 
ATOM   1278 C  CA  . LYS   B 2 133 ? -23.709 -11.077 -27.928 1.00 55.40  ? 142 LYS   B CA  1 
ATOM   1279 C  C   . LYS   B 2 133 ? -25.211 -10.791 -27.771 1.00 55.83  ? 142 LYS   B C   1 
ATOM   1280 O  O   . LYS   B 2 133 ? -25.836 -10.352 -28.728 1.00 55.86  ? 142 LYS   B O   1 
ATOM   1281 C  CB  . LYS   B 2 133 ? -23.448 -12.413 -28.661 1.00 58.40  ? 142 LYS   B CB  1 
ATOM   1282 C  CG  . LYS   B 2 133 ? -22.211 -12.379 -29.576 1.00 64.15  ? 142 LYS   B CG  1 
ATOM   1283 C  CD  . LYS   B 2 133 ? -21.128 -13.395 -29.189 1.00 69.62  ? 142 LYS   B CD  1 
ATOM   1284 C  CE  . LYS   B 2 133 ? -19.989 -13.397 -30.194 1.00 74.38  ? 142 LYS   B CE  1 
ATOM   1285 N  NZ  . LYS   B 2 133 ? -19.325 -14.738 -30.332 1.00 77.13  ? 142 LYS   B NZ  1 
ATOM   1286 N  N   . CYS   B 2 134 ? -25.776 -10.976 -26.563 1.00 55.92  ? 143 CYS   B N   1 
ATOM   1287 C  CA  . CYS   B 2 134 ? -27.203 -10.686 -26.339 1.00 56.57  ? 143 CYS   B CA  1 
ATOM   1288 C  C   . CYS   B 2 134 ? -27.490 -9.273  -25.841 1.00 55.39  ? 143 CYS   B C   1 
ATOM   1289 O  O   . CYS   B 2 134 ? -28.636 -8.986  -25.512 1.00 56.27  ? 143 CYS   B O   1 
ATOM   1290 C  CB  . CYS   B 2 134 ? -27.823 -11.710 -25.399 1.00 59.07  ? 143 CYS   B CB  1 
ATOM   1291 S  SG  . CYS   B 2 134 ? -27.537 -13.422 -25.882 1.00 67.41  ? 143 CYS   B SG  1 
ATOM   1292 N  N   . GLY   B 2 135 ? -26.478 -8.424  -25.740 1.00 53.64  ? 144 GLY   B N   1 
ATOM   1293 C  CA  . GLY   B 2 135 ? -26.649 -7.071  -25.224 1.00 52.61  ? 144 GLY   B CA  1 
ATOM   1294 C  C   . GLY   B 2 135 ? -26.660 -6.964  -23.708 1.00 50.91  ? 144 GLY   B C   1 
ATOM   1295 O  O   . GLY   B 2 135 ? -26.915 -5.880  -23.167 1.00 50.87  ? 144 GLY   B O   1 
ATOM   1296 N  N   . ARG   B 2 136 ? -26.397 -8.081  -23.005 1.00 49.43  ? 145 ARG   B N   1 
ATOM   1297 C  CA  . ARG   B 2 136 ? -26.373 -8.118  -21.538 1.00 48.51  ? 145 ARG   B CA  1 
ATOM   1298 C  C   . ARG   B 2 136 ? -25.075 -7.542  -20.993 1.00 46.79  ? 145 ARG   B C   1 
ATOM   1299 O  O   . ARG   B 2 136 ? -24.013 -7.812  -21.554 1.00 47.24  ? 145 ARG   B O   1 
ATOM   1300 C  CB  . ARG   B 2 136 ? -26.546 -9.560  -21.052 1.00 50.21  ? 145 ARG   B CB  1 
ATOM   1301 C  CG  . ARG   B 2 136 ? -27.983 -10.046 -21.108 1.00 53.95  ? 145 ARG   B CG  1 
ATOM   1302 C  CD  . ARG   B 2 136 ? -28.065 -11.473 -20.643 1.00 58.42  ? 145 ARG   B CD  1 
ATOM   1303 N  NE  . ARG   B 2 136 ? -27.568 -12.373 -21.676 1.00 64.21  ? 145 ARG   B NE  1 
ATOM   1304 C  CZ  . ARG   B 2 136 ? -26.900 -13.498 -21.444 1.00 68.12  ? 145 ARG   B CZ  1 
ATOM   1305 N  NH1 . ARG   B 2 136 ? -26.616 -13.867 -20.197 1.00 67.87  ? 145 ARG   B NH1 1 
ATOM   1306 N  NH2 . ARG   B 2 136 ? -26.487 -14.251 -22.458 1.00 68.98  ? 145 ARG   B NH2 1 
ATOM   1307 N  N   . VAL   B 2 137 ? -25.141 -6.772  -19.898 1.00 44.97  ? 146 VAL   B N   1 
ATOM   1308 C  CA  . VAL   B 2 137 ? -23.940 -6.176  -19.330 1.00 43.69  ? 146 VAL   B CA  1 
ATOM   1309 C  C   . VAL   B 2 137 ? -23.153 -7.184  -18.507 1.00 43.39  ? 146 VAL   B C   1 
ATOM   1310 O  O   . VAL   B 2 137 ? -23.589 -7.603  -17.431 1.00 43.25  ? 146 VAL   B O   1 
ATOM   1311 C  CB  . VAL   B 2 137 ? -24.224 -4.873  -18.562 1.00 43.67  ? 146 VAL   B CB  1 
ATOM   1312 C  CG1 . VAL   B 2 137 ? -22.929 -4.237  -18.061 1.00 43.59  ? 146 VAL   B CG1 1 
ATOM   1313 C  CG2 . VAL   B 2 137 ? -25.009 -3.896  -19.435 1.00 44.12  ? 146 VAL   B CG2 1 
ATOM   1314 N  N   . ILE   B 2 138 ? -22.012 -7.618  -19.049 1.00 42.72  ? 147 ILE   B N   1 
ATOM   1315 C  CA  . ILE   B 2 138 ? -21.143 -8.558  -18.353 1.00 41.93  ? 147 ILE   B CA  1 
ATOM   1316 C  C   . ILE   B 2 138 ? -20.132 -7.862  -17.407 1.00 40.29  ? 147 ILE   B C   1 
ATOM   1317 O  O   . ILE   B 2 138 ? -19.393 -8.554  -16.706 1.00 40.17  ? 147 ILE   B O   1 
ATOM   1318 C  CB  . ILE   B 2 138 ? -20.447 -9.516  -19.337 1.00 42.65  ? 147 ILE   B CB  1 
ATOM   1319 C  CG1 . ILE   B 2 138 ? -19.499 -8.740  -20.261 1.00 43.71  ? 147 ILE   B CG1 1 
ATOM   1320 C  CG2 . ILE   B 2 138 ? -21.477 -10.337 -20.132 1.00 43.48  ? 147 ILE   B CG2 1 
ATOM   1321 C  CD1 . ILE   B 2 138 ? -18.700 -9.617  -21.183 1.00 45.05  ? 147 ILE   B CD1 1 
ATOM   1322 N  N   . GLY   B 2 139 ? -20.117 -6.525  -17.368 1.00 38.67  ? 148 GLY   B N   1 
ATOM   1323 C  CA  . GLY   B 2 139 ? -19.222 -5.805  -16.467 1.00 38.34  ? 148 GLY   B CA  1 
ATOM   1324 C  C   . GLY   B 2 139 ? -18.935 -4.383  -16.889 1.00 38.03  ? 148 GLY   B C   1 
ATOM   1325 O  O   . GLY   B 2 139 ? -19.426 -3.944  -17.925 1.00 38.30  ? 148 GLY   B O   1 
ATOM   1326 N  N   . LEU   B 2 140 ? -18.141 -3.647  -16.091 1.00 37.69  ? 149 LEU   B N   1 
ATOM   1327 C  CA  . LEU   B 2 140 ? -17.775 -2.252  -16.380 1.00 37.79  ? 149 LEU   B CA  1 
ATOM   1328 C  C   . LEU   B 2 140 ? -16.260 -2.073  -16.618 1.00 38.10  ? 149 LEU   B C   1 
ATOM   1329 O  O   . LEU   B 2 140 ? -15.421 -2.780  -16.046 1.00 37.91  ? 149 LEU   B O   1 
ATOM   1330 C  CB  . LEU   B 2 140 ? -18.255 -1.283  -15.275 1.00 37.67  ? 149 LEU   B CB  1 
ATOM   1331 C  CG  . LEU   B 2 140 ? -19.727 -1.326  -14.853 1.00 37.85  ? 149 LEU   B CG  1 
ATOM   1332 C  CD1 . LEU   B 2 140 ? -20.023 -0.248  -13.786 1.00 38.37  ? 149 LEU   B CD1 1 
ATOM   1333 C  CD2 . LEU   B 2 140 ? -20.649 -1.195  -16.033 1.00 37.77  ? 149 LEU   B CD2 1 
ATOM   1334 N  N   . TYR   B 2 141 ? -15.936 -1.110  -17.477 1.00 38.25  ? 150 TYR   B N   1 
ATOM   1335 C  CA  . TYR   B 2 141 ? -14.585 -0.783  -17.919 1.00 39.09  ? 150 TYR   B CA  1 
ATOM   1336 C  C   . TYR   B 2 141 ? -14.062 0.423   -17.142 1.00 38.80  ? 150 TYR   B C   1 
ATOM   1337 O  O   . TYR   B 2 141 ? -14.813 1.362   -16.937 1.00 38.73  ? 150 TYR   B O   1 
ATOM   1338 C  CB  . TYR   B 2 141 ? -14.645 -0.506  -19.451 1.00 39.79  ? 150 TYR   B CB  1 
ATOM   1339 C  CG  . TYR   B 2 141 ? -13.429 0.165   -20.057 1.00 41.32  ? 150 TYR   B CG  1 
ATOM   1340 C  CD1 . TYR   B 2 141 ? -13.336 1.549   -20.128 1.00 42.41  ? 150 TYR   B CD1 1 
ATOM   1341 C  CD2 . TYR   B 2 141 ? -12.399 -0.586  -20.609 1.00 42.67  ? 150 TYR   B CD2 1 
ATOM   1342 C  CE1 . TYR   B 2 141 ? -12.216 2.168   -20.671 1.00 44.05  ? 150 TYR   B CE1 1 
ATOM   1343 C  CE2 . TYR   B 2 141 ? -11.286 0.021   -21.185 1.00 43.81  ? 150 TYR   B CE2 1 
ATOM   1344 C  CZ  . TYR   B 2 141 ? -11.194 1.399   -21.209 1.00 45.16  ? 150 TYR   B CZ  1 
ATOM   1345 O  OH  . TYR   B 2 141 ? -10.101 2.006   -21.791 1.00 46.78  ? 150 TYR   B OH  1 
ATOM   1346 N  N   . GLY   B 2 142 ? -12.797 0.407   -16.730 1.00 38.72  ? 151 GLY   B N   1 
ATOM   1347 C  CA  . GLY   B 2 142 ? -12.238 1.533   -15.982 1.00 39.49  ? 151 GLY   B CA  1 
ATOM   1348 C  C   . GLY   B 2 142 ? -11.364 1.190   -14.790 1.00 39.85  ? 151 GLY   B C   1 
ATOM   1349 O  O   . GLY   B 2 142 ? -10.835 2.100   -14.133 1.00 39.81  ? 151 GLY   B O   1 
ATOM   1350 N  N   . ASN   B 2 143 ? -11.183 -0.119  -14.495 1.00 39.48  ? 152 ASN   B N   1 
ATOM   1351 C  CA  . ASN   B 2 143 ? -10.279 -0.519  -13.422 1.00 40.02  ? 152 ASN   B CA  1 
ATOM   1352 C  C   . ASN   B 2 143 ? -9.306  -1.575  -13.924 1.00 41.59  ? 152 ASN   B C   1 
ATOM   1353 O  O   . ASN   B 2 143 ? -9.692  -2.708  -14.209 1.00 41.22  ? 152 ASN   B O   1 
ATOM   1354 C  CB  . ASN   B 2 143 ? -10.987 -1.016  -12.166 1.00 39.87  ? 152 ASN   B CB  1 
ATOM   1355 C  CG  . ASN   B 2 143 ? -10.064 -1.059  -10.964 1.00 41.35  ? 152 ASN   B CG  1 
ATOM   1356 O  OD1 . ASN   B 2 143 ? -9.029  -0.394  -10.921 1.00 40.92  ? 152 ASN   B OD1 1 
ATOM   1357 N  ND2 . ASN   B 2 143 ? -10.422 -1.829  -9.944  1.00 42.21  ? 152 ASN   B ND2 1 
ATOM   1358 N  N   . GLY   B 2 144 ? -8.055  -1.181  -14.046 1.00 42.79  ? 153 GLY   B N   1 
ATOM   1359 C  CA  . GLY   B 2 144 ? -7.043  -2.085  -14.544 1.00 45.00  ? 153 GLY   B CA  1 
ATOM   1360 C  C   . GLY   B 2 144 ? -5.621  -1.657  -14.327 1.00 47.67  ? 153 GLY   B C   1 
ATOM   1361 O  O   . GLY   B 2 144 ? -5.253  -1.135  -13.266 1.00 47.80  ? 153 GLY   B O   1 
ATOM   1362 N  N   . VAL   B 2 145 ? -4.806  -1.917  -15.339 1.00 49.76  ? 154 VAL   B N   1 
ATOM   1363 C  CA  . VAL   B 2 145 ? -3.381  -1.706  -15.226 1.00 51.80  ? 154 VAL   B CA  1 
ATOM   1364 C  C   . VAL   B 2 145 ? -2.739  -1.105  -16.495 1.00 54.04  ? 154 VAL   B C   1 
ATOM   1365 O  O   . VAL   B 2 145 ? -3.332  -1.134  -17.565 1.00 53.87  ? 154 VAL   B O   1 
ATOM   1366 C  CB  . VAL   B 2 145 ? -2.775  -3.072  -14.811 1.00 51.89  ? 154 VAL   B CB  1 
ATOM   1367 C  CG1 . VAL   B 2 145 ? -2.383  -3.934  -16.011 1.00 51.77  ? 154 VAL   B CG1 1 
ATOM   1368 C  CG2 . VAL   B 2 145 ? -1.632  -2.893  -13.832 1.00 52.83  ? 154 VAL   B CG2 1 
ATOM   1369 N  N   . VAL   B 2 146 ? -1.527  -0.555  -16.356 1.00 56.26  ? 155 VAL   B N   1 
ATOM   1370 C  CA  . VAL   B 2 146 ? -0.768  -0.003  -17.471 1.00 58.88  ? 155 VAL   B CA  1 
ATOM   1371 C  C   . VAL   B 2 146 ? 0.378   -0.955  -17.767 1.00 61.51  ? 155 VAL   B C   1 
ATOM   1372 O  O   . VAL   B 2 146 ? 1.168   -1.243  -16.873 1.00 61.76  ? 155 VAL   B O   1 
ATOM   1373 C  CB  . VAL   B 2 146 ? -0.273  1.425   -17.177 1.00 60.02  ? 155 VAL   B CB  1 
ATOM   1374 C  CG1 . VAL   B 2 146 ? 0.548   1.956   -18.343 1.00 61.09  ? 155 VAL   B CG1 1 
ATOM   1375 C  CG2 . VAL   B 2 146 ? -1.453  2.350   -16.897 1.00 60.51  ? 155 VAL   B CG2 1 
ATOM   1376 N  N   . ILE   B 2 147 ? 0.435   -1.512  -18.987 1.00 63.67  ? 156 ILE   B N   1 
ATOM   1377 C  CA  . ILE   B 2 147 ? 1.471   -2.494  -19.325 1.00 66.69  ? 156 ILE   B CA  1 
ATOM   1378 C  C   . ILE   B 2 147 ? 2.776   -1.828  -19.825 1.00 69.64  ? 156 ILE   B C   1 
ATOM   1379 O  O   . ILE   B 2 147 ? 2.791   -0.611  -20.005 1.00 70.22  ? 156 ILE   B O   1 
ATOM   1380 C  CB  . ILE   B 2 147 ? 0.908   -3.563  -20.309 1.00 67.53  ? 156 ILE   B CB  1 
ATOM   1381 C  CG1 . ILE   B 2 147 ? 0.473   -2.936  -21.654 1.00 68.78  ? 156 ILE   B CG1 1 
ATOM   1382 C  CG2 . ILE   B 2 147 ? -0.230  -4.359  -19.648 1.00 67.83  ? 156 ILE   B CG2 1 
ATOM   1383 C  CD1 . ILE   B 2 147 ? -0.059  -3.938  -22.669 1.00 70.01  ? 156 ILE   B CD1 1 
ATOM   1384 N  N   . LYS   B 2 148 ? 3.876   -2.614  -20.023 1.00 71.28  ? 157 LYS   B N   1 
ATOM   1385 C  CA  . LYS   B 2 148 ? 5.184   -2.129  -20.507 1.00 73.26  ? 157 LYS   B CA  1 
ATOM   1386 C  C   . LYS   B 2 148 ? 5.072   -1.145  -21.669 1.00 74.52  ? 157 LYS   B C   1 
ATOM   1387 O  O   . LYS   B 2 148 ? 5.793   -0.149  -21.716 1.00 75.23  ? 157 LYS   B O   1 
ATOM   1388 C  CB  . LYS   B 2 148 ? 6.079   -3.303  -20.950 1.00 75.80  ? 157 LYS   B CB  1 
ATOM   1389 C  CG  . LYS   B 2 148 ? 6.687   -4.084  -19.802 1.00 80.76  ? 157 LYS   B CG  1 
ATOM   1390 C  CD  . LYS   B 2 148 ? 7.692   -5.128  -20.282 1.00 85.88  ? 157 LYS   B CD  1 
ATOM   1391 C  CE  . LYS   B 2 148 ? 9.075   -4.553  -20.501 1.00 89.42  ? 157 LYS   B CE  1 
ATOM   1392 N  NZ  . LYS   B 2 148 ? 10.135  -5.475  -20.002 1.00 91.10  ? 157 LYS   B NZ  1 
ATOM   1393 N  N   . ASN   B 2 149 ? 4.150   -1.435  -22.594 1.00 74.52  ? 158 ASN   B N   1 
ATOM   1394 C  CA  . ASN   B 2 149 ? 3.843   -0.676  -23.804 1.00 74.90  ? 158 ASN   B CA  1 
ATOM   1395 C  C   . ASN   B 2 149 ? 3.319   0.751   -23.557 1.00 73.97  ? 158 ASN   B C   1 
ATOM   1396 O  O   . ASN   B 2 149 ? 3.190   1.523   -24.514 1.00 74.26  ? 158 ASN   B O   1 
ATOM   1397 C  CB  . ASN   B 2 149 ? 2.757   -1.419  -24.609 1.00 77.18  ? 158 ASN   B CB  1 
ATOM   1398 C  CG  . ASN   B 2 149 ? 3.030   -2.875  -24.914 1.00 81.84  ? 158 ASN   B CG  1 
ATOM   1399 O  OD1 . ASN   B 2 149 ? 3.958   -3.503  -24.376 1.00 83.57  ? 158 ASN   B OD1 1 
ATOM   1400 N  ND2 . ASN   B 2 149 ? 2.211   -3.446  -25.796 1.00 82.54  ? 158 ASN   B ND2 1 
ATOM   1401 N  N   . GLY   B 2 150 ? 2.946   1.058   -22.315 1.00 72.49  ? 159 GLY   B N   1 
ATOM   1402 C  CA  . GLY   B 2 150 ? 2.334   2.335   -21.964 1.00 71.14  ? 159 GLY   B CA  1 
ATOM   1403 C  C   . GLY   B 2 150 ? 0.820   2.320   -22.133 1.00 69.11  ? 159 GLY   B C   1 
ATOM   1404 O  O   . GLY   B 2 150 ? 0.124   3.213   -21.632 1.00 69.20  ? 159 GLY   B O   1 
ATOM   1405 N  N   . SER   B 2 151 ? 0.297   1.289   -22.851 1.00 66.70  ? 160 SER   B N   1 
ATOM   1406 C  CA  A SER   B 2 151 ? -1.126  1.082   -23.119 0.50 65.70  ? 160 SER   B CA  1 
ATOM   1407 C  CA  B SER   B 2 151 ? -1.131  1.135   -23.103 0.50 65.75  ? 160 SER   B CA  1 
ATOM   1408 C  C   . SER   B 2 151 ? -1.914  0.703   -21.842 1.00 64.32  ? 160 SER   B C   1 
ATOM   1409 O  O   . SER   B 2 151 ? -1.317  0.400   -20.802 1.00 64.47  ? 160 SER   B O   1 
ATOM   1410 C  CB  A SER   B 2 151 ? -1.295  0.013   -24.201 0.50 66.94  ? 160 SER   B CB  1 
ATOM   1411 C  CB  B SER   B 2 151 ? -1.369  0.194   -24.285 0.50 67.15  ? 160 SER   B CB  1 
ATOM   1412 O  OG  A SER   B 2 151 ? -2.657  -0.307  -24.438 0.50 68.97  ? 160 SER   B OG  1 
ATOM   1413 O  OG  B SER   B 2 151 ? -0.622  -1.006  -24.181 0.50 69.49  ? 160 SER   B OG  1 
ATOM   1414 N  N   . TYR   B 2 152 ? -3.254  0.712   -21.923 1.00 61.41  ? 161 TYR   B N   1 
ATOM   1415 C  CA  . TYR   B 2 152 ? -4.157  0.396   -20.837 1.00 59.22  ? 161 TYR   B CA  1 
ATOM   1416 C  C   . TYR   B 2 152 ? -4.938  -0.908  -21.038 1.00 56.62  ? 161 TYR   B C   1 
ATOM   1417 O  O   . TYR   B 2 152 ? -5.453  -1.156  -22.121 1.00 56.90  ? 161 TYR   B O   1 
ATOM   1418 C  CB  . TYR   B 2 152 ? -5.140  1.563   -20.681 1.00 59.01  ? 161 TYR   B CB  1 
ATOM   1419 C  CG  . TYR   B 2 152 ? -6.028  1.415   -19.476 1.00 59.21  ? 161 TYR   B CG  1 
ATOM   1420 C  CD1 . TYR   B 2 152 ? -5.499  1.442   -18.195 1.00 59.58  ? 161 TYR   B CD1 1 
ATOM   1421 C  CD2 . TYR   B 2 152 ? -7.396  1.222   -19.616 1.00 59.85  ? 161 TYR   B CD2 1 
ATOM   1422 C  CE1 . TYR   B 2 152 ? -6.304  1.274   -17.083 1.00 60.25  ? 161 TYR   B CE1 1 
ATOM   1423 C  CE2 . TYR   B 2 152 ? -8.212  1.047   -18.510 1.00 60.56  ? 161 TYR   B CE2 1 
ATOM   1424 C  CZ  . TYR   B 2 152 ? -7.658  1.068   -17.244 1.00 61.16  ? 161 TYR   B CZ  1 
ATOM   1425 O  OH  . TYR   B 2 152 ? -8.446  0.935   -16.136 1.00 62.43  ? 161 TYR   B OH  1 
ATOM   1426 N  N   . VAL   B 2 153 ? -5.044  -1.730  -19.980 1.00 53.97  ? 162 VAL   B N   1 
ATOM   1427 C  CA  . VAL   B 2 153 ? -5.804  -2.985  -19.995 1.00 51.57  ? 162 VAL   B CA  1 
ATOM   1428 C  C   . VAL   B 2 153 ? -6.734  -3.024  -18.758 1.00 48.92  ? 162 VAL   B C   1 
ATOM   1429 O  O   . VAL   B 2 153 ? -6.280  -2.978  -17.622 1.00 48.21  ? 162 VAL   B O   1 
ATOM   1430 C  CB  . VAL   B 2 153 ? -4.906  -4.252  -20.160 1.00 51.58  ? 162 VAL   B CB  1 
ATOM   1431 C  CG1 . VAL   B 2 153 ? -5.713  -5.537  -19.987 1.00 51.47  ? 162 VAL   B CG1 1 
ATOM   1432 C  CG2 . VAL   B 2 153 ? -4.200  -4.252  -21.517 1.00 52.53  ? 162 VAL   B CG2 1 
ATOM   1433 N  N   . SER   B 2 154 ? -8.037  -3.024  -18.996 1.00 47.39  ? 163 SER   B N   1 
ATOM   1434 C  CA  . SER   B 2 154 ? -9.035  -2.969  -17.935 1.00 45.70  ? 163 SER   B CA  1 
ATOM   1435 C  C   . SER   B 2 154 ? -9.636  -4.324  -17.629 1.00 44.65  ? 163 SER   B C   1 
ATOM   1436 O  O   . SER   B 2 154 ? -9.933  -5.064  -18.547 1.00 45.30  ? 163 SER   B O   1 
ATOM   1437 C  CB  . SER   B 2 154 ? -10.165 -2.029  -18.352 1.00 45.48  ? 163 SER   B CB  1 
ATOM   1438 O  OG  . SER   B 2 154 ? -11.339 -2.165  -17.560 1.00 44.88  ? 163 SER   B OG  1 
ATOM   1439 N  N   . ALA   B 2 155 ? -9.968  -4.577  -16.367 1.00 42.94  ? 164 ALA   B N   1 
ATOM   1440 C  CA  . ALA   B 2 155 ? -10.674 -5.791  -15.993 1.00 42.16  ? 164 ALA   B CA  1 
ATOM   1441 C  C   . ALA   B 2 155 ? -12.139 -5.696  -16.481 1.00 41.83  ? 164 ALA   B C   1 
ATOM   1442 O  O   . ALA   B 2 155 ? -12.658 -4.594  -16.733 1.00 41.33  ? 164 ALA   B O   1 
ATOM   1443 C  CB  . ALA   B 2 155 ? -10.661 -5.933  -14.479 1.00 42.19  ? 164 ALA   B CB  1 
ATOM   1444 N  N   . ILE   B 2 156 ? -12.811 -6.848  -16.601 1.00 41.37  ? 165 ILE   B N   1 
ATOM   1445 C  CA  . ILE   B 2 156 ? -14.243 -6.858  -16.859 1.00 41.21  ? 165 ILE   B CA  1 
ATOM   1446 C  C   . ILE   B 2 156 ? -14.816 -6.953  -15.424 1.00 40.10  ? 165 ILE   B C   1 
ATOM   1447 O  O   . ILE   B 2 156 ? -14.974 -8.053  -14.899 1.00 39.77  ? 165 ILE   B O   1 
ATOM   1448 C  CB  . ILE   B 2 156 ? -14.701 -8.033  -17.748 1.00 41.74  ? 165 ILE   B CB  1 
ATOM   1449 C  CG1 . ILE   B 2 156 ? -13.995 -7.989  -19.132 1.00 42.60  ? 165 ILE   B CG1 1 
ATOM   1450 C  CG2 . ILE   B 2 156 ? -16.230 -7.971  -17.919 1.00 41.98  ? 165 ILE   B CG2 1 
ATOM   1451 C  CD1 . ILE   B 2 156 ? -14.248 -9.182  -19.977 1.00 43.36  ? 165 ILE   B CD1 1 
ATOM   1452 N  N   . THR   B 2 157 ? -14.989 -5.793  -14.761 1.00 39.39  ? 166 THR   B N   1 
ATOM   1453 C  CA  . THR   B 2 157 ? -15.445 -5.711  -13.361 1.00 39.30  ? 166 THR   B CA  1 
ATOM   1454 C  C   . THR   B 2 157 ? -16.942 -5.900  -13.241 1.00 39.19  ? 166 THR   B C   1 
ATOM   1455 O  O   . THR   B 2 157 ? -17.695 -5.032  -13.663 1.00 39.11  ? 166 THR   B O   1 
ATOM   1456 C  CB  . THR   B 2 157 ? -15.086 -4.348  -12.759 1.00 40.14  ? 166 THR   B CB  1 
ATOM   1457 O  OG1 . THR   B 2 157 ? -13.673 -4.172  -12.832 1.00 40.80  ? 166 THR   B OG1 1 
ATOM   1458 C  CG2 . THR   B 2 157 ? -15.529 -4.232  -11.319 1.00 40.32  ? 166 THR   B CG2 1 
ATOM   1459 N  N   . GLN   B 2 158 ? -17.375 -7.004  -12.637 1.00 38.76  ? 167 GLN   B N   1 
ATOM   1460 C  CA  . GLN   B 2 158 ? -18.796 -7.294  -12.476 1.00 38.95  ? 167 GLN   B CA  1 
ATOM   1461 C  C   . GLN   B 2 158 ? -19.149 -7.379  -10.970 1.00 40.41  ? 167 GLN   B C   1 
ATOM   1462 O  O   . GLN   B 2 158 ? -18.335 -7.821  -10.161 1.00 39.95  ? 167 GLN   B O   1 
ATOM   1463 C  CB  . GLN   B 2 158 ? -19.137 -8.630  -13.209 1.00 38.99  ? 167 GLN   B CB  1 
ATOM   1464 C  CG  . GLN   B 2 158 ? -20.608 -9.068  -13.206 1.00 39.36  ? 167 GLN   B CG  1 
ATOM   1465 C  CD  . GLN   B 2 158 ? -21.566 -8.008  -13.743 1.00 42.23  ? 167 GLN   B CD  1 
ATOM   1466 O  OE1 . GLN   B 2 158 ? -21.770 -6.937  -13.143 1.00 43.19  ? 167 GLN   B OE1 1 
ATOM   1467 N  NE2 . GLN   B 2 158 ? -22.208 -8.287  -14.855 1.00 41.89  ? 167 GLN   B NE2 1 
ATOM   1468 N  N   . GLY   B 2 159 ? -20.350 -6.947  -10.615 1.00 41.81  ? 168 GLY   B N   1 
ATOM   1469 C  CA  . GLY   B 2 159 ? -20.830 -7.050  -9.251  1.00 44.19  ? 168 GLY   B CA  1 
ATOM   1470 C  C   . GLY   B 2 159 ? -21.531 -8.371  -9.009  1.00 47.45  ? 168 GLY   B C   1 
ATOM   1471 O  O   . GLY   B 2 159 ? -21.416 -9.313  -9.795  1.00 47.77  ? 168 GLY   B O   1 
ATOM   1472 N  N   . LYS   B 2 160 ? -22.237 -8.459  -7.897  1.00 50.07  ? 169 LYS   B N   1 
ATOM   1473 C  CA  . LYS   B 2 160 ? -22.995 -9.650  -7.527  1.00 52.66  ? 169 LYS   B CA  1 
ATOM   1474 C  C   . LYS   B 2 160 ? -24.450 -9.224  -7.310  1.00 54.64  ? 169 LYS   B C   1 
ATOM   1475 O  O   . LYS   B 2 160 ? -24.702 -8.211  -6.657  1.00 54.79  ? 169 LYS   B O   1 
ATOM   1476 C  CB  . LYS   B 2 160 ? -22.417 -10.270 -6.234  1.00 55.36  ? 169 LYS   B CB  1 
ATOM   1477 C  CG  . LYS   B 2 160 ? -23.156 -11.513 -5.765  1.00 60.94  ? 169 LYS   B CG  1 
ATOM   1478 C  CD  . LYS   B 2 160 ? -22.632 -12.031 -4.430  1.00 66.15  ? 169 LYS   B CD  1 
ATOM   1479 C  CE  . LYS   B 2 160 ? -23.312 -13.313 -3.990  1.00 69.89  ? 169 LYS   B CE  1 
ATOM   1480 N  NZ  . LYS   B 2 160 ? -22.979 -13.648 -2.571  1.00 72.71  ? 169 LYS   B NZ  1 
ATOM   1481 N  N   . ARG   B 2 161 ? -25.397 -9.955  -7.890  1.00 56.15  ? 170 ARG   B N   1 
ATOM   1482 C  CA  . ARG   B 2 161 ? -26.812 -9.659  -7.710  1.00 58.27  ? 170 ARG   B CA  1 
ATOM   1483 C  C   . ARG   B 2 161 ? -27.318 -10.605 -6.623  1.00 60.78  ? 170 ARG   B C   1 
ATOM   1484 O  O   . ARG   B 2 161 ? -27.135 -11.820 -6.733  1.00 61.31  ? 170 ARG   B O   1 
ATOM   1485 C  CB  . ARG   B 2 161 ? -27.594 -9.842  -9.026  1.00 59.50  ? 170 ARG   B CB  1 
ATOM   1486 C  CG  . ARG   B 2 161 ? -29.099 -9.777  -8.850  1.00 62.38  ? 170 ARG   B CG  1 
ATOM   1487 C  CD  . ARG   B 2 161 ? -29.863 -9.789  -10.157 1.00 65.81  ? 170 ARG   B CD  1 
ATOM   1488 N  NE  . ARG   B 2 161 ? -31.241 -9.334  -9.949  1.00 69.36  ? 170 ARG   B NE  1 
ATOM   1489 C  CZ  . ARG   B 2 161 ? -31.939 -8.618  -10.827 1.00 71.48  ? 170 ARG   B CZ  1 
ATOM   1490 N  NH1 . ARG   B 2 161 ? -31.405 -8.280  -11.994 1.00 70.15  ? 170 ARG   B NH1 1 
ATOM   1491 N  NH2 . ARG   B 2 161 ? -33.176 -8.232  -10.542 1.00 72.32  ? 170 ARG   B NH2 1 
ATOM   1492 N  N   . GLU   B 2 162 ? -27.896 -10.055 -5.553  1.00 62.04  ? 171 GLU   B N   1 
ATOM   1493 C  CA  . GLU   B 2 162 ? -28.417 -10.858 -4.449  1.00 63.93  ? 171 GLU   B CA  1 
ATOM   1494 C  C   . GLU   B 2 162 ? -29.745 -11.531 -4.834  1.00 64.77  ? 171 GLU   B C   1 
ATOM   1495 O  O   . GLU   B 2 162 ? -30.731 -11.448 -4.097  1.00 65.43  ? 171 GLU   B O   1 
ATOM   1496 C  CB  . GLU   B 2 162 ? -28.587 -9.982  -3.197  1.00 67.54  ? 171 GLU   B CB  1 
ATOM   1497 C  CG  . GLU   B 2 162 ? -27.311 -9.270  -2.778  1.00 74.61  ? 171 GLU   B CG  1 
ATOM   1498 C  CD  . GLU   B 2 162 ? -26.296 -10.165 -2.091  1.00 84.21  ? 171 GLU   B CD  1 
ATOM   1499 O  OE1 . GLU   B 2 162 ? -26.365 -10.293 -0.845  1.00 85.85  ? 171 GLU   B OE1 1 
ATOM   1500 O  OE2 . GLU   B 2 162 ? -25.438 -10.745 -2.797  1.00 87.08  ? 171 GLU   B OE2 1 
HETATM 1501 S  S   . DMS   C 3 .   ? -18.655 11.590  -0.237  1.00 83.02  ? 201 DMS   B S   1 
HETATM 1502 O  O   . DMS   C 3 .   ? -19.595 10.424  -0.370  1.00 82.77  ? 201 DMS   B O   1 
HETATM 1503 C  C1  . DMS   C 3 .   ? -19.574 13.112  -0.544  1.00 83.12  ? 201 DMS   B C1  1 
HETATM 1504 C  C2  . DMS   C 3 .   ? -17.668 11.810  -1.751  1.00 82.83  ? 201 DMS   B C2  1 
HETATM 1505 N  N1  . A1B9L D 4 .   ? -9.964  7.512   -13.602 1.00 47.79  ? 202 A1B9L B N1  1 
HETATM 1506 N  N3  . A1B9L D 4 .   ? -9.266  2.339   -7.441  1.00 42.39  ? 202 A1B9L B N3  1 
HETATM 1507 C  C4  . A1B9L D 4 .   ? -8.482  5.475   -10.736 1.00 43.75  ? 202 A1B9L B C4  1 
HETATM 1508 C  C5  . A1B9L D 4 .   ? -8.684  5.385   -9.372  1.00 43.20  ? 202 A1B9L B C5  1 
HETATM 1509 C  C6  . A1B9L D 4 .   ? -9.044  4.159   -8.824  1.00 42.94  ? 202 A1B9L B C6  1 
HETATM 1510 C  C7  . A1B9L D 4 .   ? -9.250  3.047   -9.632  1.00 42.90  ? 202 A1B9L B C7  1 
HETATM 1511 C  C8  . A1B9L D 4 .   ? -9.044  3.119   -11.004 1.00 43.43  ? 202 A1B9L B C8  1 
HETATM 1512 C  C10 . A1B9L D 4 .   ? -9.350  3.805   -7.397  1.00 42.57  ? 202 A1B9L B C10 1 
HETATM 1513 C  C13 . A1B9L D 4 .   ? -9.422  4.381   -17.631 1.00 48.70  ? 202 A1B9L B C13 1 
HETATM 1514 C  C15 . A1B9L D 4 .   ? -7.158  4.898   -17.247 1.00 49.04  ? 202 A1B9L B C15 1 
HETATM 1515 C  C17 . A1B9L D 4 .   ? -7.404  5.042   -15.862 1.00 48.89  ? 202 A1B9L B C17 1 
HETATM 1516 C  C1  . A1B9L D 4 .   ? -9.587  6.428   -13.720 1.00 47.99  ? 202 A1B9L B C1  1 
HETATM 1517 C  C2  . A1B9L D 4 .   ? -9.190  5.005   -13.932 1.00 47.76  ? 202 A1B9L B C2  1 
HETATM 1518 N  N2  . A1B9L D 4 .   ? -8.329  4.450   -12.906 1.00 46.33  ? 202 A1B9L B N2  1 
HETATM 1519 C  C3  . A1B9L D 4 .   ? -8.687  4.358   -11.556 1.00 44.45  ? 202 A1B9L B C3  1 
HETATM 1520 C  C9  . A1B9L D 4 .   ? -9.679  1.889   -8.778  1.00 42.26  ? 202 A1B9L B C9  1 
HETATM 1521 C  C11 . A1B9L D 4 .   ? -8.711  4.809   -15.360 1.00 48.38  ? 202 A1B9L B C11 1 
HETATM 1522 C  C12 . A1B9L D 4 .   ? -9.693  4.502   -16.278 1.00 48.69  ? 202 A1B9L B C12 1 
HETATM 1523 CL CL1 . A1B9L D 4 .   ? -10.772 3.960   -18.636 1.00 49.20  ? 202 A1B9L B CL1 1 
HETATM 1524 C  C14 . A1B9L D 4 .   ? -8.155  4.543   -18.158 1.00 48.61  ? 202 A1B9L B C14 1 
HETATM 1525 N  N4  . A1B9L D 4 .   ? -5.833  5.102   -17.438 1.00 49.17  ? 202 A1B9L B N4  1 
HETATM 1526 N  N5  . A1B9L D 4 .   ? -5.203  5.359   -16.257 1.00 49.48  ? 202 A1B9L B N5  1 
HETATM 1527 C  C16 . A1B9L D 4 .   ? -6.129  5.330   -15.312 1.00 49.34  ? 202 A1B9L B C16 1 
HETATM 1528 S  S   . DMS   E 3 .   ? -12.170 -13.424 -9.373  1.00 120.24 ? 203 DMS   B S   1 
HETATM 1529 O  O   . DMS   E 3 .   ? -11.564 -13.357 -8.001  1.00 120.19 ? 203 DMS   B O   1 
HETATM 1530 C  C1  . DMS   E 3 .   ? -13.898 -12.876 -9.262  1.00 120.15 ? 203 DMS   B C1  1 
HETATM 1531 C  C2  . DMS   E 3 .   ? -12.538 -15.167 -9.736  1.00 120.23 ? 203 DMS   B C2  1 
HETATM 1532 O  O   . HOH   F 5 .   ? -4.159  -14.633 -25.530 1.00 39.86  ? 101 HOH   A O   1 
HETATM 1533 O  O   . HOH   F 5 .   ? -7.983  0.510   3.472   1.00 38.39  ? 102 HOH   A O   1 
HETATM 1534 O  O   . HOH   F 5 .   ? -9.275  3.470   -3.715  1.00 46.40  ? 103 HOH   A O   1 
HETATM 1535 O  O   . HOH   F 5 .   ? -1.975  -3.952  -6.176  1.00 53.01  ? 104 HOH   A O   1 
HETATM 1536 O  O   . HOH   F 5 .   ? -23.516 18.830  -19.588 1.00 51.40  ? 105 HOH   A O   1 
HETATM 1537 O  O   . HOH   F 5 .   ? -23.987 9.285   -27.432 1.00 44.79  ? 106 HOH   A O   1 
HETATM 1538 O  O   . HOH   F 5 .   ? -2.859  -11.681 -7.028  1.00 41.26  ? 107 HOH   A O   1 
HETATM 1539 O  O   . HOH   F 5 .   ? -21.308 2.301   -32.496 1.00 49.14  ? 108 HOH   A O   1 
HETATM 1540 O  O   . HOH   F 5 .   ? -21.774 -9.289  -34.595 1.00 54.22  ? 109 HOH   A O   1 
HETATM 1541 O  O   . HOH   F 5 .   ? -28.372 -6.250  -28.008 1.00 49.00  ? 110 HOH   A O   1 
HETATM 1542 O  O   . HOH   F 5 .   ? -5.507  2.181   -10.038 1.00 41.72  ? 111 HOH   A O   1 
HETATM 1543 O  O   . HOH   F 5 .   ? -2.727  -8.143  -3.512  1.00 58.81  ? 112 HOH   A O   1 
HETATM 1544 O  O   . HOH   F 5 .   ? -3.556  -3.981  0.386   1.00 62.59  ? 113 HOH   A O   1 
HETATM 1545 O  O   . HOH   F 5 .   ? -6.802  -15.906 -25.389 1.00 51.06  ? 114 HOH   A O   1 
HETATM 1546 O  O   . HOH   F 5 .   ? -6.776  4.649   -4.500  1.00 51.18  ? 115 HOH   A O   1 
HETATM 1547 O  O   . HOH   F 5 .   ? -30.001 0.414   -30.406 1.00 65.14  ? 116 HOH   A O   1 
HETATM 1548 O  O   . HOH   F 5 .   ? -4.678  -10.362 -5.572  1.00 41.56  ? 117 HOH   A O   1 
HETATM 1549 O  O   . HOH   F 5 .   ? -31.126 0.465   -23.146 1.00 47.68  ? 118 HOH   A O   1 
HETATM 1550 O  O   . HOH   F 5 .   ? -3.770  -0.655  -0.198  1.00 50.20  ? 119 HOH   A O   1 
HETATM 1551 O  O   . HOH   F 5 .   ? -3.429  4.904   -7.253  1.00 53.37  ? 120 HOH   A O   1 
HETATM 1552 O  O   . HOH   F 5 .   ? 6.153   -7.711  -8.346  1.00 58.37  ? 121 HOH   A O   1 
HETATM 1553 O  O   . HOH   F 5 .   ? -5.259  5.857   -8.682  1.00 68.34  ? 122 HOH   A O   1 
HETATM 1554 O  O   . HOH   F 5 .   ? -0.102  -11.632 -5.469  1.00 52.59  ? 123 HOH   A O   1 
HETATM 1555 O  O   . HOH   G 5 .   ? -6.618  -0.474  -11.031 1.00 33.42  ? 301 HOH   B O   1 
HETATM 1556 O  O   . HOH   G 5 .   ? -17.279 12.595  -5.510  1.00 47.74  ? 302 HOH   B O   1 
HETATM 1557 O  O   . HOH   G 5 .   ? -21.904 6.962   -0.224  0.50 28.67  ? 303 HOH   B O   1 
HETATM 1558 O  O   . HOH   G 5 .   ? -30.991 12.650  -19.253 1.00 51.14  ? 304 HOH   B O   1 
HETATM 1559 O  O   . HOH   G 5 .   ? -34.128 1.669   -15.412 1.00 46.27  ? 305 HOH   B O   1 
HETATM 1560 O  O   . HOH   G 5 .   ? -35.057 4.280   -9.180  1.00 55.15  ? 306 HOH   B O   1 
HETATM 1561 O  O   . HOH   G 5 .   ? -26.006 -8.147  -16.679 1.00 43.56  ? 307 HOH   B O   1 
HETATM 1562 O  O   . HOH   G 5 .   ? -35.225 -5.857  -10.404 1.00 58.99  ? 308 HOH   B O   1 
HETATM 1563 O  O   . HOH   G 5 .   ? -15.813 -10.549 -14.889 1.00 51.52  ? 309 HOH   B O   1 
HETATM 1564 O  O   . HOH   G 5 .   ? -7.310  1.718   -13.887 1.00 47.06  ? 310 HOH   B O   1 
HETATM 1565 O  O   . HOH   G 5 .   ? -15.637 9.224   -0.706  1.00 53.90  ? 311 HOH   B O   1 
HETATM 1566 O  O   . HOH   G 5 .   ? -20.790 5.887   -32.654 1.00 68.83  ? 312 HOH   B O   1 
HETATM 1567 O  O   . HOH   G 5 .   ? -7.250  -6.585  0.697   1.00 51.76  ? 313 HOH   B O   1 
HETATM 1568 O  O   . HOH   G 5 .   ? -11.809 1.849   -5.793  1.00 31.40  ? 314 HOH   B O   1 
HETATM 1569 O  O   . HOH   G 5 .   ? -14.378 8.641   -30.360 1.00 56.85  ? 315 HOH   B O   1 
HETATM 1570 O  O   . HOH   G 5 .   ? -27.844 -7.164  -5.568  1.00 52.62  ? 316 HOH   B O   1 
HETATM 1571 O  O   . HOH   G 5 .   ? -12.969 -2.408  -14.801 1.00 32.60  ? 317 HOH   B O   1 
HETATM 1572 O  O   . HOH   G 5 .   ? -12.523 -3.635  -9.945  1.00 42.42  ? 318 HOH   B O   1 
HETATM 1573 O  O   . HOH   G 5 .   ? -23.810 -6.536  -4.673  1.00 52.19  ? 319 HOH   B O   1 
HETATM 1574 O  O   . HOH   G 5 .   ? -18.064 -10.965 -16.401 1.00 45.53  ? 320 HOH   B O   1 
HETATM 1575 O  O   . HOH   G 5 .   ? -20.897 -7.328  -5.494  1.00 61.96  ? 321 HOH   B O   1 
HETATM 1576 O  O   . HOH   G 5 .   ? -29.492 -2.053  -19.205 1.00 44.59  ? 322 HOH   B O   1 
HETATM 1577 O  O   . HOH   G 5 .   ? -7.014  -9.173  -3.141  1.00 42.51  ? 323 HOH   B O   1 
HETATM 1578 O  O   . HOH   G 5 .   ? -7.324  -10.583 -5.472  1.00 48.23  ? 324 HOH   B O   1 
HETATM 1579 O  O   . HOH   G 5 .   ? -22.478 7.292   -34.324 1.00 66.77  ? 325 HOH   B O   1 
HETATM 1580 O  O   . HOH   G 5 .   ? -16.101 -14.775 -16.598 1.00 47.60  ? 326 HOH   B O   1 
HETATM 1581 O  O   . HOH   G 5 .   ? -20.268 -7.962  -2.470  1.00 55.05  ? 327 HOH   B O   1 
HETATM 1582 O  O   . HOH   G 5 .   ? -21.540 -12.500 -13.007 1.00 51.83  ? 328 HOH   B O   1 
HETATM 1583 O  O   . HOH   G 5 .   ? -16.547 -7.375  -8.024  1.00 56.01  ? 329 HOH   B O   1 
HETATM 1584 O  O   . HOH   G 5 .   ? -22.385 -14.117 -21.586 1.00 46.21  ? 330 HOH   B O   1 
HETATM 1585 O  O   . HOH   G 5 .   ? -9.506  -7.113  -25.386 1.00 41.94  ? 331 HOH   B O   1 
HETATM 1586 O  O   . HOH   G 5 .   ? 12.494  -7.033  -20.310 1.00 69.55  ? 332 HOH   B O   1 
HETATM 1587 O  O   . HOH   G 5 .   ? -27.856 19.847  -15.379 1.00 57.77  ? 333 HOH   B O   1 
HETATM 1588 O  O   . HOH   G 5 .   ? -28.018 -6.659  -18.445 1.00 46.60  ? 334 HOH   B O   1 
HETATM 1589 O  O   . HOH   G 5 .   ? -20.741 14.562  -33.634 1.00 57.50  ? 335 HOH   B O   1 
HETATM 1590 O  O   . HOH   G 5 .   ? 3.752   -5.349  -19.076 1.00 69.58  ? 336 HOH   B O   1 
HETATM 1591 O  O   . HOH   G 5 .   ? -29.336 15.871  -15.248 1.00 58.78  ? 337 HOH   B O   1 
HETATM 1592 O  O   . HOH   G 5 .   ? -18.787 14.784  -22.184 1.00 41.57  ? 338 HOH   B O   1 
HETATM 1593 O  O   . HOH   G 5 .   ? -15.076 16.223  -20.249 1.00 52.52  ? 339 HOH   B O   1 
HETATM 1594 O  O   . HOH   G 5 .   ? -7.108  8.070   -13.431 1.00 57.83  ? 340 HOH   B O   1 
HETATM 1595 O  O   . HOH   G 5 .   ? -15.073 -4.981  1.393   1.00 47.31  ? 341 HOH   B O   1 
HETATM 1596 O  O   . HOH   G 5 .   ? -32.002 7.217   -4.500  1.00 56.56  ? 342 HOH   B O   1 
HETATM 1597 O  O   . HOH   G 5 .   ? -32.152 -6.951  -7.179  1.00 52.92  ? 343 HOH   B O   1 
HETATM 1598 O  O   . HOH   G 5 .   ? -16.980 8.391   -30.633 1.00 63.00  ? 344 HOH   B O   1 
HETATM 1599 O  O   . HOH   G 5 .   ? -10.761 11.979  -19.207 1.00 44.44  ? 345 HOH   B O   1 
HETATM 1600 O  O   . HOH   G 5 .   ? -30.681 4.537   -2.558  1.00 41.79  ? 346 HOH   B O   1 
HETATM 1601 O  O   . HOH   G 5 .   ? -18.543 -10.833 -9.997  1.00 63.11  ? 347 HOH   B O   1 
HETATM 1602 O  O   . HOH   G 5 .   ? -14.705 -12.465 -16.367 1.00 48.14  ? 348 HOH   B O   1 
HETATM 1603 O  O   . HOH   G 5 .   ? -25.809 -4.886  -4.074  1.00 43.99  ? 349 HOH   B O   1 
HETATM 1604 O  O   . HOH   G 5 .   ? -21.990 15.152  -5.855  1.00 61.69  ? 350 HOH   B O   1 
HETATM 1605 O  O   . HOH   G 5 .   ? -19.384 -6.149  -0.608  1.00 41.66  ? 351 HOH   B O   1 
HETATM 1606 O  O   . HOH   G 5 .   ? -20.182 -13.985 -22.739 1.00 45.17  ? 352 HOH   B O   1 
HETATM 1607 O  O   . HOH   G 5 .   ? -18.669 11.811  -31.888 1.00 53.01  ? 353 HOH   B O   1 
HETATM 1608 O  O   . HOH   G 5 .   ? -16.055 -14.650 -30.883 1.00 61.44  ? 354 HOH   B O   1 
HETATM 1609 O  O   . HOH   G 5 .   ? -31.468 -9.567  -14.872 1.00 63.18  ? 355 HOH   B O   1 
HETATM 1610 O  O   . HOH   G 5 .   ? -18.916 25.324  -14.281 1.00 62.36  ? 356 HOH   B O   1 
HETATM 1611 O  O   . HOH   G 5 .   ? -30.095 -7.750  -5.741  1.00 58.79  ? 357 HOH   B O   1 
HETATM 1612 O  O   . HOH   G 5 .   ? -5.305  4.113   -11.928 1.00 51.19  ? 358 HOH   B O   1 
HETATM 1613 O  O   . HOH   G 5 .   ? -14.397 -6.697  -1.657  1.00 53.96  ? 359 HOH   B O   1 
HETATM 1614 O  O   . HOH   G 5 .   ? -30.318 -5.540  -1.163  1.00 51.99  ? 360 HOH   B O   1 
HETATM 1615 O  O   . HOH   G 5 .   ? -9.671  -10.769 -7.588  1.00 60.97  ? 361 HOH   B O   1 
HETATM 1616 O  O   . HOH   G 5 .   ? -15.142 -9.043  -11.455 1.00 55.08  ? 362 HOH   B O   1 
HETATM 1617 O  O   . HOH   G 5 .   ? -11.928 -5.638  -8.272  1.00 37.96  ? 363 HOH   B O   1 
HETATM 1618 O  O   . HOH   G 5 .   ? -1.117  -14.370 -10.098 1.00 59.53  ? 364 HOH   B O   1 
HETATM 1619 O  O   . HOH   G 5 .   ? -17.521 14.094  -31.141 1.00 54.75  ? 365 HOH   B O   1 
HETATM 1620 O  O   . HOH   G 5 .   ? -16.894 16.523  -21.903 1.00 35.37  ? 366 HOH   B O   1 
HETATM 1621 O  O   . HOH   G 5 .   ? -9.882  -15.864 -24.246 1.00 59.22  ? 367 HOH   B O   1 
HETATM 1622 O  O   . HOH   G 5 .   ? -4.425  2.177   -13.961 1.00 57.84  ? 368 HOH   B O   1 
HETATM 1623 O  O   . HOH   G 5 .   ? -10.281 6.927   -5.993  1.00 53.33  ? 369 HOH   B O   1 
HETATM 1624 O  O   . HOH   G 5 .   ? -30.931 -10.080 -27.917 0.50 47.35  ? 370 HOH   B O   1 
HETATM 1625 O  O   . HOH   G 5 .   ? -7.781  11.795  -18.786 1.00 65.50  ? 371 HOH   B O   1 
HETATM 1626 O  O   . HOH   G 5 .   ? -21.220 15.755  -23.108 1.00 50.00  ? 372 HOH   B O   1 
HETATM 1627 O  O   . HOH   G 5 .   ? -11.802 -8.955  0.556   1.00 56.91  ? 373 HOH   B O   1 
HETATM 1628 O  O   . HOH   G 5 .   ? -18.802 -12.145 -14.011 1.00 50.07  ? 374 HOH   B O   1 
HETATM 1629 O  O   . HOH   G 5 .   ? -18.942 7.836   -32.846 1.00 57.72  ? 375 HOH   B O   1 
HETATM 1630 O  O   . HOH   G 5 .   ? -16.954 -11.648 -12.025 1.00 51.63  ? 376 HOH   B O   1 
HETATM 1631 O  O   . HOH   G 5 .   ? -21.291 4.114   -0.001  0.50 59.75  ? 377 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   ? 0.8470 0.4241 0.9008 0.1392  -0.0262 -0.1336 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.8350 0.4705 0.8541 0.1571  -0.0150 -0.1354 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.8053 0.4532 0.8162 0.1525  0.0050  -0.0932 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.8304 0.4336 0.8435 0.1583  0.0093  -0.0678 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 0.8787 0.5098 0.8801 0.1929  -0.0232 -0.1626 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 0.9576 0.6521 0.9370 0.2064  -0.0205 -0.1929 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 0.9808 0.6770 0.9517 0.2350  -0.0279 -0.2226 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 0.9844 0.7260 0.9549 0.1895  -0.0095 -0.1858 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.7525 0.4561 0.7503 0.1438  0.0166  -0.0857 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.7241 0.4413 0.7117 0.1415  0.0328  -0.0513 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.6984 0.4346 0.6637 0.1689  0.0348  -0.0538 51  MET   A C   
12   O  O   . MET   A 8   ? 0.6952 0.4597 0.6549 0.1836  0.0296  -0.0826 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.7103 0.4712 0.6967 0.1202  0.0421  -0.0418 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.7156 0.4631 0.7302 0.0948  0.0394  -0.0359 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.7047 0.5012 0.7165 0.0760  0.0484  -0.0234 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.6678 0.4439 0.7283 0.0501  0.0418  -0.0190 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.6802 0.4032 0.6336 0.1777  0.0423  -0.0251 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.6678 0.4100 0.6031 0.2056  0.0397  -0.0285 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.6562 0.4140 0.5743 0.2057  0.0495  -0.0014 52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.6572 0.3977 0.5739 0.1892  0.0605  0.0259  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.6865 0.3817 0.6160 0.2355  0.0276  -0.0326 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.7276 0.3563 0.6477 0.2370  0.0320  0.0032  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.7477 0.3227 0.6873 0.2201  0.0318  0.0093  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.7554 0.3723 0.6462 0.2578  0.0356  0.0297  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.7876 0.2995 0.7219 0.2185  0.0408  0.0459  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.7955 0.3483 0.6704 0.2615  0.0440  0.0667  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.8205 0.3202 0.7191 0.2401  0.0489  0.0766  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 0.8736 0.3091 0.7609 0.2392  0.0626  0.1172  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.6370 0.4310 0.5452 0.2250  0.0450  -0.0116 53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.6411 0.4509 0.5312 0.2286  0.0497  0.0072  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.6558 0.4474 0.5228 0.2651  0.0385  0.0132  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.6629 0.4508 0.5342 0.2892  0.0250  -0.0059 53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.6197 0.4901 0.5203 0.2140  0.0531  -0.0090 53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.6040 0.5159 0.5211 0.2291  0.0442  -0.0415 53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.6191 0.4985 0.5316 0.1824  0.0633  -0.0093 53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.5910 0.5566 0.5210 0.2158  0.0492  -0.0533 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.6682 0.4468 0.5071 0.2726  0.0433  0.0396  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.6923 0.4523 0.4970 0.3108  0.0316  0.0487  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.6922 0.4868 0.4795 0.3135  0.0312  0.0516  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.6815 0.4774 0.4644 0.2914  0.0473  0.0695  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.7494 0.4392 0.5229 0.3210  0.0416  0.0870  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.8405 0.4796 0.6268 0.3224  0.0393  0.0873  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 0.9753 0.5407 0.7348 0.3270  0.0536  0.1299  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 0.9935 0.5547 0.7376 0.3142  0.0738  0.1603  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.0303 0.5409 0.7850 0.3437  0.0462  0.1335  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.6949 0.5163 0.4735 0.3428  0.0110  0.0325  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.7063 0.5573 0.4694 0.3474  0.0059  0.0300  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.7557 0.5635 0.4646 0.3628  0.0162  0.0669  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.7929 0.5524 0.4676 0.3886  0.0162  0.0886  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.7097 0.6010 0.4827 0.3756  -0.0218 -0.0030 55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.7440 0.6771 0.5229 0.3681  -0.0289 -0.0178 55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.7563 0.7423 0.5694 0.3841  -0.0554 -0.0578 55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.7688 0.7922 0.5981 0.3696  -0.0620 -0.0747 55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.8195 0.8377 0.6129 0.3939  -0.0790 -0.0758 55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.8732 0.8515 0.6070 0.4351  -0.0887 -0.0575 55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.7896 0.8375 0.6023 0.3782  -0.0860 -0.0942 55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.7523 0.5743 0.4522 0.3472  0.0276  0.0759  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.7927 0.5822 0.4411 0.3622  0.0418  0.1099  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.8057 0.6179 0.4203 0.3864  0.0273  0.0988  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.8446 0.6327 0.4084 0.4057  0.0384  0.1246  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.7951 0.5744 0.4584 0.3271  0.0717  0.1349  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.7752 0.6324 0.4181 0.3860  0.0033  0.0603  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.7807 0.6578 0.3971 0.4098  -0.0167 0.0431  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.7584 0.6849 0.4235 0.3865  -0.0307 0.0064  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.7362 0.6844 0.4542 0.3509  -0.0221 -0.0040 57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.7613 0.7030 0.4065 0.4076  -0.0526 -0.0136 58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.7461 0.7280 0.4367 0.3857  -0.0671 -0.0481 58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.7650 0.7380 0.4496 0.3608  -0.0475 -0.0352 58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.7911 0.7347 0.4252 0.3752  -0.0320 -0.0076 58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.7580 0.7580 0.4330 0.4213  -0.1049 -0.0806 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.7988 0.8259 0.5009 0.4430  -0.1330 -0.1079 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.8089 0.8339 0.5308 0.4372  -0.1221 -0.0981 58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.8122 0.8626 0.5146 0.4695  -0.1683 -0.1410 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.7492 0.7479 0.4839 0.3266  -0.0487 -0.0556 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.7680 0.7568 0.4969 0.3070  -0.0355 -0.0475 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.7994 0.7949 0.5173 0.3242  -0.0623 -0.0760 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.7738 0.7944 0.5393 0.3074  -0.0801 -0.1075 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.7485 0.7479 0.5261 0.2615  -0.0170 -0.0447 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.7586 0.7439 0.5338 0.2514  0.0075  -0.0159 59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.7572 0.7466 0.5312 0.2453  -0.0107 -0.0426 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.7519 0.7484 0.5669 0.2143  0.0224  -0.0151 59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.8401 0.8133 0.4950 0.3597  -0.0654 -0.0662 60  THR   A N   
83   N  N   B THR   A 17  ? 0.8401 0.8132 0.4952 0.3592  -0.0650 -0.0659 60  THR   A N   
84   C  CA  A THR   A 17  ? 0.8676 0.8412 0.4984 0.3841  -0.0926 -0.0941 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.8679 0.8417 0.4977 0.3856  -0.0933 -0.0942 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.9157 0.8630 0.4897 0.4008  -0.0758 -0.0734 60  THR   A C   
87   C  C   B THR   A 17  ? 0.9176 0.8649 0.4887 0.4037  -0.0772 -0.0740 60  THR   A C   
88   O  O   A THR   A 17  ? 0.9331 0.8635 0.4742 0.4071  -0.0465 -0.0360 60  THR   A O   
89   O  O   B THR   A 17  ? 0.9370 0.8670 0.4731 0.4118  -0.0485 -0.0366 60  THR   A O   
90   C  CB  A THR   A 17  ? 0.8933 0.8731 0.4908 0.4306  -0.1249 -0.1140 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.8904 0.8717 0.4918 0.4297  -0.1237 -0.1119 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.9361 0.8894 0.4683 0.4632  -0.1079 -0.0783 60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.8714 0.8828 0.5330 0.4139  -0.1359 -0.1304 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.8664 0.8813 0.5253 0.4211  -0.1483 -0.1438 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.9029 0.8877 0.4773 0.4620  -0.1604 -0.1482 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.9354 0.8800 0.4994 0.4100  -0.0949 -0.0996 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 0.9999 0.9237 0.5070 0.4337  -0.0821 -0.0862 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 1.0715 0.9864 0.5010 0.4912  -0.0944 -0.0853 61  TRP   A C   
99   O  O   . TRP   A 18  ? 1.0697 0.9943 0.4943 0.5144  -0.1308 -0.1171 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 0.9956 0.9151 0.5198 0.4254  -0.1024 -0.1194 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 1.0327 0.9332 0.4993 0.4552  -0.0949 -0.1151 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 1.0692 0.9615 0.4739 0.5042  -0.1172 -0.1366 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 1.0350 0.9248 0.5053 0.4390  -0.0680 -0.0953 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 1.0874 0.9654 0.4541 0.5207  -0.1010 -0.1284 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 1.0695 0.9470 0.4791 0.4809  -0.0714 -0.1036 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 1.0242 0.9154 0.5386 0.3979  -0.0411 -0.0707 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 1.0830 0.9524 0.4822 0.4815  -0.0489 -0.0896 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 1.0415 0.9235 0.5451 0.3986  -0.0222 -0.0574 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 1.0637 0.9365 0.5125 0.4399  -0.0249 -0.0661 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 1.1291 1.0270 0.4993 0.5145  -0.0633 -0.0480 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.1963 1.0808 0.4817 0.5711  -0.0686 -0.0406 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.2516 1.1287 0.4830 0.6030  -0.0712 -0.0533 62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.2589 1.1322 0.4830 0.5948  -0.0363 -0.0275 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.2559 1.1237 0.5069 0.5780  -0.0270 0.0137  62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.4082 1.2562 0.5605 0.6390  -0.0268 0.0280  62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.5485 1.3732 0.6532 0.6513  0.0204  0.0858  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.5640 1.3903 0.7147 0.6110  0.0579  0.1168  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.6152 1.4192 0.6358 0.7021  0.0196  0.1001  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.2871 1.1642 0.4826 0.6411  -0.1133 -0.0952 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.3448 1.2124 0.4810 0.6782  -0.1188 -0.1117 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.4067 1.2607 0.4494 0.7243  -0.0846 -0.0699 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.4260 1.2722 0.4306 0.7471  -0.0834 -0.0498 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.3867 1.2569 0.5093 0.7088  -0.1776 -0.1718 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.4124 1.2986 0.6344 0.6616  -0.2108 -0.2112 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.4718 1.3698 0.6915 0.6913  -0.2698 -0.2649 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.5412 1.4276 0.7264 0.7240  -0.3061 -0.3127 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.5819 1.4827 0.7639 0.7568  -0.3668 -0.3669 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.4378 1.2886 0.4465 0.7369  -0.0538 -0.0539 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.4986 1.3405 0.4233 0.7771  -0.0122 -0.0100 64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.5002 1.3404 0.4550 0.7436  0.0357  0.0477  64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.5331 1.3575 0.4296 0.7708  0.0569  0.0839  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.5782 1.4055 0.4006 0.8449  -0.0373 -0.0217 64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.7059 1.5328 0.4813 0.8885  -0.0797 -0.0767 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.7359 1.5675 0.5145 0.8874  -0.0671 -0.0866 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.7530 1.5746 0.4877 0.9266  -0.1277 -0.1119 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.4628 1.3157 0.5068 0.6856  0.0509  0.0556  65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.4475 1.3000 0.5294 0.6504  0.0939  0.1047  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.4437 1.3067 0.5106 0.6545  0.1446  0.1390  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.4509 1.3238 0.4907 0.6785  0.1426  0.1197  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.4103 1.2741 0.5909 0.5904  0.0837  0.0933  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.4300 1.2920 0.5170 0.6328  0.1894  0.1878  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.4230 1.3032 0.5120 0.6315  0.2398  0.2207  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.3725 1.2809 0.5341 0.5981  0.2367  0.1990  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.3372 1.2514 0.5757 0.5501  0.2303  0.1968  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.4620 1.3339 0.5740 0.6071  0.2846  0.2745  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.5365 1.4350 0.6700 0.5981  0.3391  0.3090  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.6178 1.5211 0.8333 0.5455  0.3693  0.3425  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.6473 1.5216 0.8782 0.5261  0.3577  0.3516  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.6210 1.5579 0.8870 0.5255  0.4028  0.3573  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.3642 1.2874 0.4950 0.6280  0.2386  0.1812  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.3265 1.2711 0.5142 0.6061  0.2337  0.1603  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.2841 1.2608 0.5082 0.5927  0.2854  0.1966  67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.2924 1.2838 0.4686 0.6291  0.3183  0.2135  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.3554 1.2958 0.4972 0.6459  0.2037  0.1165  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.3394 1.2909 0.5422 0.6207  0.1922  0.0940  67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.3832 1.2959 0.4893 0.6629  0.1528  0.0792  67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.2313 1.2222 0.5407 0.5424  0.2924  0.2070  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.1896 1.2168 0.5493 0.5251  0.3374  0.2377  68  THR   A CA  
159  C  C   . THR   A 25  ? 1.1410 1.1871 0.5846 0.4853  0.3225  0.2215  68  THR   A C   
160  O  O   . THR   A 25  ? 1.1369 1.1636 0.5923 0.4717  0.2819  0.1909  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.2049 1.2269 0.5734 0.5081  0.3743  0.2839  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.1945 1.2555 0.6005 0.5015  0.4240  0.3148  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.1953 1.2001 0.6231 0.4602  0.3554  0.2850  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 1.0997 1.1849 0.5993 0.4697  0.3551  0.2411  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 1.0628 1.1673 0.6373 0.4369  0.3406  0.2275  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 1.0498 1.1677 0.6211 0.4599  0.3246  0.1986  69  GLY   A C   
167  O  O   . GLY   A 26  ? 1.0812 1.1757 0.5935 0.4928  0.3028  0.1736  69  GLY   A O   
168  N  N   . ASN   A 27  ? 1.0024 1.1561 0.6398 0.4430  0.3322  0.1997  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 0.9879 1.1557 0.6331 0.4635  0.3175  0.1746  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 0.9635 1.1008 0.6319 0.4391  0.2724  0.1495  70  ASN   A C   
171  O  O   . ASN   A 27  ? 0.9691 1.0801 0.6469 0.4072  0.2559  0.1515  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 0.9696 1.2006 0.6715 0.4672  0.3540  0.1907  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 0.9848 1.2419 0.7741 0.4227  0.3540  0.2008  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 0.9976 1.2436 0.8106 0.3877  0.3580  0.2181  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 0.9694 1.2613 0.8077 0.4261  0.3468  0.1879  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.9417 1.0784 0.6130 0.4571  0.2533  0.1266  71  SER   A N   
177  C  CA  . SER   A 28  ? 0.9367 1.0387 0.6216 0.4380  0.2141  0.1068  71  SER   A CA  
178  C  C   . SER   A 28  ? 0.8907 1.0228 0.6291 0.4346  0.2115  0.1055  71  SER   A C   
179  O  O   . SER   A 28  ? 0.9033 1.0268 0.6293 0.4619  0.1963  0.0867  71  SER   A O   
180  C  CB  . SER   A 28  ? 0.9904 1.0443 0.6194 0.4640  0.1845  0.0773  71  SER   A CB  
181  O  OG  . SER   A 28  ? 1.0551 1.0841 0.6362 0.4708  0.1808  0.0730  71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.8399 1.0068 0.6384 0.4042  0.2236  0.1230  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.8017 1.0048 0.6538 0.4055  0.2186  0.1192  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.7984 0.9632 0.6491 0.3949  0.1795  0.1041  72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.8103 0.9337 0.6445 0.3681  0.1622  0.1041  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.7768 1.0293 0.6950 0.3756  0.2436  0.1408  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.8005 1.0187 0.6980 0.3468  0.2449  0.1525  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.8204 0.9970 0.6431 0.3709  0.2414  0.1452  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.7794 0.9581 0.6456 0.4184  0.1669  0.0923  73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.7930 0.9352 0.6555 0.4128  0.1316  0.0822  73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.7336 0.9276 0.6624 0.3983  0.1308  0.0883  73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.6973 0.9483 0.6690 0.4192  0.1423  0.0858  73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.8484 0.9599 0.6762 0.4529  0.1127  0.0635  73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 0.9673 1.0145 0.7315 0.4610  0.1025  0.0519  73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 1.0740 1.0771 0.8050 0.4968  0.0784  0.0316  73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.1663 1.1348 0.8477 0.5193  0.0770  0.0147  73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.2356 1.1390 0.8803 0.5046  0.0574  0.0051  73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.2472 1.1129 0.8974 0.4671  0.0420  0.0137  73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.2451 1.1231 0.8489 0.5282  0.0530  -0.0148 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.7181 0.8984 0.6593 0.3626  0.1190  0.0946  74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.6670 0.8948 0.6715 0.3452  0.1151  0.0972  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.6588 0.8566 0.6519 0.3404  0.0794  0.0899  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.6893 0.8292 0.6350 0.3253  0.0664  0.0919  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.6558 0.8969 0.6863 0.3076  0.1342  0.1107  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.6651 0.9313 0.7024 0.3097  0.1724  0.1241  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.6671 0.9266 0.7169 0.2739  0.1860  0.1382  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.6257 0.9635 0.7225 0.3270  0.1951  0.1261  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.6131 0.8536 0.6517 0.3524  0.0644  0.0821  75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.6196 0.8336 0.6426 0.3511  0.0295  0.0763  75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.5762 0.8069 0.6304 0.3142  0.0277  0.0790  75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.5422 0.8365 0.6680 0.3046  0.0357  0.0755  75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.6420 0.8964 0.6992 0.3847  0.0091  0.0635  75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.7750 0.9834 0.7794 0.4245  -0.0074 0.0582  75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.8378 0.9826 0.7821 0.4241  -0.0019 0.0635  75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.7953 1.0300 0.8208 0.4568  -0.0281 0.0471  75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.5747 0.7505 0.5802 0.2925  0.0188  0.0840  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.5396 0.7279 0.5700 0.2605  0.0166  0.0836  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.5528 0.7075 0.5451 0.2597  -0.0146 0.0785  76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.5839 0.6936 0.5212 0.2793  -0.0302 0.0809  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.5435 0.7135 0.5641 0.2321  0.0424  0.0941  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.5383 0.7289 0.5738 0.2400  0.0728  0.1020  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.5825 0.6868 0.5339 0.2238  0.0367  0.0984  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.5270 0.7026 0.5482 0.2383  -0.0232 0.0715  77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.5473 0.6969 0.5314 0.2364  -0.0496 0.0655  77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.5414 0.6770 0.5207 0.2039  -0.0384 0.0665  77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.5189 0.6832 0.5487 0.1841  -0.0200 0.0664  77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.5235 0.7217 0.5540 0.2499  -0.0790 0.0473  77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.5581 0.6479 0.4752 0.1998  -0.0470 0.0692  78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.5519 0.6288 0.4604 0.1737  -0.0379 0.0676  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.5581 0.6337 0.4456 0.1777  -0.0649 0.0539  78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.6005 0.6457 0.4285 0.1965  -0.0805 0.0579  78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.5805 0.6085 0.4351 0.1647  -0.0179 0.0823  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.5884 0.6022 0.4279 0.1422  -0.0087 0.0800  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.5639 0.6038 0.4561 0.1244  0.0065  0.0765  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.6133 0.5825 0.3998 0.1369  0.0056  0.0923  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.5177 0.6253 0.4534 0.1630  -0.0726 0.0371  79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.5237 0.6345 0.4427 0.1698  -0.1023 0.0181  79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.5710 0.6447 0.4332 0.1584  -0.0946 0.0185  79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.5858 0.6373 0.4345 0.1426  -0.0666 0.0323  79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.4842 0.6490 0.4886 0.1624  -0.1210 -0.0060 79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.5047 0.6802 0.5626 0.1315  -0.1048 -0.0120 79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.5176 0.6596 0.5416 0.1181  -0.0816 -0.0001 79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.4925 0.7094 0.6292 0.1210  -0.1160 -0.0289 79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.5912 0.6622 0.4214 0.1691  -0.1201 0.0014  80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.6295 0.6725 0.4050 0.1635  -0.1140 -0.0017 80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.6136 0.6636 0.4321 0.1365  -0.0961 -0.0096 80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.6445 0.6705 0.4244 0.1287  -0.0777 -0.0043 80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.6791 0.7244 0.4155 0.1855  -0.1489 -0.0233 80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.8100 0.8179 0.4575 0.1924  -0.1392 -0.0171 80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.9310 0.9375 0.5240 0.2199  -0.1726 -0.0372 80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.9234 0.9576 0.5548 0.2198  -0.1992 -0.0706 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 1.0073 0.9820 0.5169 0.2425  -0.1730 -0.0197 80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.5630 0.6450 0.4629 0.1224  -0.0989 -0.0201 81  SER   A N   
254  C  CA  . SER   A 38  ? 0.5381 0.6198 0.4782 0.0987  -0.0823 -0.0242 81  SER   A CA  
255  C  C   . SER   A 38  ? 0.5210 0.5910 0.4684 0.0865  -0.0473 0.0012  81  SER   A C   
256  O  O   . SER   A 38  ? 0.5051 0.5717 0.4825 0.0699  -0.0328 0.0013  81  SER   A O   
257  C  CB  . SER   A 38  ? 0.5260 0.6413 0.5509 0.0867  -0.0985 -0.0440 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.5680 0.6969 0.5916 0.0990  -0.1361 -0.0732 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.5195 0.5799 0.4370 0.0967  -0.0363 0.0211  82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.5188 0.5684 0.4388 0.0893  -0.0080 0.0410  82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.4898 0.5668 0.4729 0.0841  0.0021  0.0472  82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.4874 0.5575 0.4757 0.0785  0.0249  0.0611  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.4648 0.5758 0.4963 0.0876  -0.0143 0.0369  83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.4391 0.5833 0.5371 0.0818  -0.0013 0.0435  83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.4482 0.6081 0.5426 0.1022  0.0006  0.0530  83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.4516 0.6169 0.5284 0.1201  -0.0230 0.0443  83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.4121 0.5908 0.5821 0.0696  -0.0188 0.0239  83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.4682 0.6277 0.6495 0.0494  -0.0191 0.0139  83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.4985 0.6282 0.6523 0.0425  0.0027  0.0274  83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.4768 0.6504 0.6944 0.0426  -0.0436 -0.0099 83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.4433 0.6090 0.5507 0.1030  0.0276  0.0701  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.4481 0.6299 0.5543 0.1252  0.0308  0.0766  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.4341 0.6744 0.6204 0.1259  0.0308  0.0709  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.4090 0.6736 0.6556 0.1047  0.0427  0.0710  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.4483 0.6105 0.5246 0.1314  0.0581  0.0941  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.4813 0.5922 0.4859 0.1346  0.0568  0.0980  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.5061 0.5934 0.4664 0.1529  0.0434  0.0973  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.4965 0.5829 0.4823 0.1193  0.0696  0.1026  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.5442 0.5850 0.4482 0.1513  0.0450  0.1016  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.5259 0.5730 0.4574 0.1204  0.0694  0.1043  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.5405 0.5656 0.4343 0.1341  0.0583  0.1041  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.4434 0.7059 0.6338 0.1503  0.0178  0.0659  85  SER   A N   
283  C  CA  . SER   A 42  ? 0.4265 0.7532 0.6973 0.1553  0.0191  0.0595  85  SER   A CA  
284  C  C   . SER   A 42  ? 0.4640 0.8014 0.7187 0.1868  0.0268  0.0659  85  SER   A C   
285  O  O   . SER   A 42  ? 0.4978 0.7891 0.6794 0.2056  0.0187  0.0698  85  SER   A O   
286  C  CB  . SER   A 42  ? 0.4110 0.7689 0.7226 0.1562  -0.0181 0.0349  85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.4741 0.8044 0.7220 0.1824  -0.0494 0.0269  85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.4551 0.8518 0.7789 0.1921  0.0449  0.0672  86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.4924 0.9050 0.8052 0.2261  0.0528  0.0700  86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.5087 0.9557 0.8472 0.2525  0.0191  0.0506  86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.4733 0.9711 0.8839 0.2428  0.0027  0.0351  86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.4636 0.9263 0.8323 0.2238  0.0947  0.0828  86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.5199 0.9447 0.8434 0.2140  0.1295  0.1045  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.4922 0.9678 0.8673 0.2142  0.1722  0.1194  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.5863 0.9525 0.8166 0.2394  0.1232  0.1065  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.5592 0.9805 0.8437 0.2880  0.0078  0.0498  87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.5665 1.0182 0.8701 0.3216  -0.0242 0.0326  87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.5623 1.0719 0.9151 0.3467  -0.0008 0.0319  87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.5913 1.0729 0.9004 0.3587  0.0242  0.0441  87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6272 1.0047 0.8351 0.3472  -0.0535 0.0335  87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6225 1.0266 0.8444 0.3873  -0.0890 0.0168  87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.6623 0.9847 0.8173 0.3224  -0.0682 0.0371  87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.5243 1.1180 0.9710 0.3541  -0.0075 0.0162  88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.5066 1.1711 1.0146 0.3781  0.0173  0.0135  88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.5196 1.1872 1.0237 0.3672  0.0723  0.0354  88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.5161 1.1853 1.0432 0.3284  0.0993  0.0499  88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.5712 1.2236 1.0386 0.4318  -0.0083 0.0017  88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.6560 1.3161 1.1325 0.4506  -0.0618 -0.0193 88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.8136 1.4145 1.2076 0.4983  -0.0935 -0.0232 88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 0.8938 1.4040 1.1939 0.4936  -0.1093 -0.0124 88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.8309 1.4753 1.2557 0.5406  -0.1015 -0.0367 88  GLU   A OE2 
312  N  N   . GLU   B 8   ? 0.7327 0.7317 0.7234 0.2161  0.0527  -0.0425 17  GLU   B N   
313  C  CA  . GLU   B 8   ? 0.7372 0.7421 0.7249 0.2176  0.0413  -0.0393 17  GLU   B CA  
314  C  C   . GLU   B 8   ? 0.7318 0.7401 0.7166 0.1999  0.0388  -0.0393 17  GLU   B C   
315  O  O   . GLU   B 8   ? 0.7515 0.7448 0.7244 0.1912  0.0434  -0.0350 17  GLU   B O   
316  C  CB  . GLU   B 8   ? 0.7850 0.7697 0.7556 0.2306  0.0378  -0.0301 17  GLU   B CB  
317  C  CG  . GLU   B 8   ? 0.8532 0.8447 0.8188 0.2365  0.0249  -0.0292 17  GLU   B CG  
318  C  CD  . GLU   B 8   ? 0.9693 0.9444 0.9158 0.2514  0.0218  -0.0200 17  GLU   B CD  
319  O  OE1 . GLU   B 8   ? 1.0026 0.9593 0.9386 0.2517  0.0304  -0.0117 17  GLU   B OE1 
320  O  OE2 . GLU   B 8   ? 1.0058 0.9876 0.9481 0.2627  0.0106  -0.0208 17  GLU   B OE2 
321  N  N   A THR   B 9   ? 0.7104 0.7382 0.7069 0.1942  0.0309  -0.0437 18  THR   B N   
322  N  N   B THR   B 9   ? 0.7122 0.7400 0.7087 0.1942  0.0309  -0.0437 18  THR   B N   
323  C  CA  A THR   B 9   ? 0.7061 0.7342 0.6998 0.1775  0.0274  -0.0431 18  THR   B CA  
324  C  CA  B THR   B 9   ? 0.7091 0.7374 0.7029 0.1777  0.0272  -0.0431 18  THR   B CA  
325  C  C   A THR   B 9   ? 0.6954 0.7213 0.6836 0.1809  0.0127  -0.0429 18  THR   B C   
326  C  C   B THR   B 9   ? 0.6970 0.7225 0.6849 0.1809  0.0127  -0.0428 18  THR   B C   
327  O  O   A THR   B 9   ? 0.6952 0.7252 0.6868 0.1680  0.0064  -0.0446 18  THR   B O   
328  O  O   B THR   B 9   ? 0.6970 0.7261 0.6878 0.1680  0.0066  -0.0443 18  THR   B O   
329  C  CB  A THR   B 9   ? 0.7133 0.7629 0.7242 0.1620  0.0325  -0.0476 18  THR   B CB  
330  C  CB  B THR   B 9   ? 0.7193 0.7701 0.7312 0.1629  0.0314  -0.0478 18  THR   B CB  
331  O  OG1 A THR   B 9   ? 0.7225 0.7834 0.7438 0.1670  0.0430  -0.0516 18  THR   B OG1 
332  O  OG1 B THR   B 9   ? 0.7192 0.7946 0.7516 0.1703  0.0292  -0.0532 18  THR   B OG1 
333  C  CG2 A THR   B 9   ? 0.7223 0.7628 0.7236 0.1450  0.0365  -0.0442 18  THR   B CG2 
334  C  CG2 B THR   B 9   ? 0.7295 0.7768 0.7379 0.1547  0.0450  -0.0478 18  THR   B CG2 
335  N  N   . THR   B 10  ? 0.6871 0.7047 0.6652 0.1983  0.0068  -0.0407 19  THR   B N   
336  C  CA  . THR   B 10  ? 0.6650 0.6790 0.6339 0.2042  -0.0077 -0.0419 19  THR   B CA  
337  C  C   . THR   B 10  ? 0.6403 0.6342 0.5895 0.1987  -0.0084 -0.0377 19  THR   B C   
338  O  O   . THR   B 10  ? 0.6431 0.6237 0.5806 0.2003  0.0013  -0.0310 19  THR   B O   
339  C  CB  . THR   B 10  ? 0.6887 0.6988 0.6481 0.2266  -0.0120 -0.0394 19  THR   B CB  
340  O  OG1 . THR   B 10  ? 0.7002 0.7277 0.6774 0.2339  -0.0104 -0.0426 19  THR   B OG1 
341  C  CG2 . THR   B 10  ? 0.6943 0.7021 0.6420 0.2351  -0.0283 -0.0424 19  THR   B CG2 
342  N  N   . ASP   B 11  ? 0.6180 0.6094 0.5637 0.1929  -0.0205 -0.0416 20  ASP   B N   
343  C  CA  . ASP   B 11  ? 0.6205 0.5920 0.5459 0.1913  -0.0235 -0.0387 20  ASP   B CA  
344  C  C   . ASP   B 11  ? 0.6106 0.5692 0.5141 0.2107  -0.0218 -0.0328 20  ASP   B C   
345  O  O   . ASP   B 11  ? 0.6063 0.5696 0.5077 0.2258  -0.0258 -0.0333 20  ASP   B O   
346  C  CB  . ASP   B 11  ? 0.6492 0.6175 0.5732 0.1868  -0.0403 -0.0459 20  ASP   B CB  
347  C  CG  . ASP   B 11  ? 0.7186 0.6865 0.6527 0.1652  -0.0410 -0.0471 20  ASP   B CG  
348  O  OD1 . ASP   B 11  ? 0.7050 0.6877 0.6570 0.1527  -0.0310 -0.0455 20  ASP   B OD1 
349  O  OD2 . ASP   B 11  ? 0.7674 0.7187 0.6898 0.1615  -0.0515 -0.0493 20  ASP   B OD2 
350  N  N   . GLY   B 12  ? 0.5952 0.5404 0.4837 0.2105  -0.0154 -0.0264 21  GLY   B N   
351  C  CA  . GLY   B 12  ? 0.5849 0.5212 0.4544 0.2275  -0.0117 -0.0188 21  GLY   B CA  
352  C  C   . GLY   B 12  ? 0.5766 0.5071 0.4418 0.2228  0.0014  -0.0096 21  GLY   B C   
353  O  O   . GLY   B 12  ? 0.5766 0.5081 0.4507 0.2069  0.0063  -0.0100 21  GLY   B O   
354  N  N   . VAL   B 13  ? 0.5635 0.4896 0.4152 0.2365  0.0070  -0.0006 22  VAL   B N   
355  C  CA  . VAL   B 13  ? 0.5518 0.4753 0.4012 0.2327  0.0190  0.0093  22  VAL   B CA  
356  C  C   . VAL   B 13  ? 0.5472 0.4723 0.4072 0.2317  0.0296  0.0157  22  VAL   B C   
357  O  O   . VAL   B 13  ? 0.5499 0.4754 0.4095 0.2428  0.0284  0.0166  22  VAL   B O   
358  C  CB  . VAL   B 13  ? 0.5565 0.4757 0.3855 0.2465  0.0189  0.0161  22  VAL   B CB  
359  C  CG1 . VAL   B 13  ? 0.5555 0.4744 0.3702 0.2672  0.0171  0.0203  22  VAL   B CG1 
360  C  CG2 . VAL   B 13  ? 0.5605 0.4818 0.3913 0.2406  0.0305  0.0264  22  VAL   B CG2 
361  N  N   . TYR   B 14  ? 0.5436 0.4686 0.4133 0.2180  0.0385  0.0186  23  TYR   B N   
362  C  CA  . TYR   B 14  ? 0.5425 0.4650 0.4226 0.2148  0.0474  0.0225  23  TYR   B CA  
363  C  C   . TYR   B 14  ? 0.5477 0.4671 0.4275 0.2093  0.0568  0.0331  23  TYR   B C   
364  O  O   . TYR   B 14  ? 0.5467 0.4696 0.4251 0.2013  0.0573  0.0340  23  TYR   B O   
365  C  CB  . TYR   B 14  ? 0.5295 0.4557 0.4250 0.2010  0.0482  0.0125  23  TYR   B CB  
366  C  CG  . TYR   B 14  ? 0.5259 0.4593 0.4285 0.2055  0.0413  0.0032  23  TYR   B CG  
367  C  CD1 . TYR   B 14  ? 0.5303 0.4697 0.4303 0.2061  0.0310  -0.0027 23  TYR   B CD1 
368  C  CD2 . TYR   B 14  ? 0.5352 0.4700 0.4489 0.2080  0.0447  -0.0002 23  TYR   B CD2 
369  C  CE1 . TYR   B 14  ? 0.5362 0.4855 0.4458 0.2090  0.0237  -0.0107 23  TYR   B CE1 
370  C  CE2 . TYR   B 14  ? 0.5398 0.4858 0.4626 0.2131  0.0383  -0.0081 23  TYR   B CE2 
371  C  CZ  . TYR   B 14  ? 0.5486 0.5035 0.4707 0.2126  0.0277  -0.0132 23  TYR   B CZ  
372  O  OH  . TYR   B 14  ? 0.5631 0.5326 0.4976 0.2152  0.0205  -0.0210 23  TYR   B OH  
373  N  N   . ARG   B 15  ? 0.5494 0.4622 0.4327 0.2121  0.0638  0.0409  24  ARG   B N   
374  C  CA  . ARG   B 15  ? 0.5505 0.4606 0.4380 0.2036  0.0724  0.0508  24  ARG   B CA  
375  C  C   . ARG   B 15  ? 0.5477 0.4543 0.4482 0.1868  0.0746  0.0428  24  ARG   B C   
376  O  O   . ARG   B 15  ? 0.5462 0.4488 0.4521 0.1868  0.0732  0.0339  24  ARG   B O   
377  C  CB  . ARG   B 15  ? 0.5688 0.4701 0.4546 0.2126  0.0787  0.0636  24  ARG   B CB  
378  C  CG  . ARG   B 15  ? 0.5992 0.5034 0.4692 0.2321  0.0773  0.0722  24  ARG   B CG  
379  C  CD  . ARG   B 15  ? 0.6347 0.5299 0.5032 0.2385  0.0854  0.0879  24  ARG   B CD  
380  N  NE  . ARG   B 15  ? 0.6641 0.5614 0.5151 0.2594  0.0838  0.0954  24  ARG   B NE  
381  C  CZ  . ARG   B 15  ? 0.6929 0.5991 0.5314 0.2685  0.0879  0.1072  24  ARG   B CZ  
382  N  NH1 . ARG   B 15  ? 0.6862 0.6018 0.5307 0.2584  0.0943  0.1138  24  ARG   B NH1 
383  N  NH2 . ARG   B 15  ? 0.7091 0.6170 0.5286 0.2890  0.0856  0.1122  24  ARG   B NH2 
384  N  N   . VAL   B 16  ? 0.5443 0.4537 0.4495 0.1738  0.0779  0.0457  25  VAL   B N   
385  C  CA  . VAL   B 16  ? 0.5444 0.4498 0.4592 0.1581  0.0797  0.0384  25  VAL   B CA  
386  C  C   . VAL   B 16  ? 0.5517 0.4472 0.4732 0.1529  0.0858  0.0480  25  VAL   B C   
387  O  O   . VAL   B 16  ? 0.5500 0.4520 0.4728 0.1502  0.0887  0.0592  25  VAL   B O   
388  C  CB  . VAL   B 16  ? 0.5452 0.4615 0.4596 0.1465  0.0770  0.0341  25  VAL   B CB  
389  C  CG1 . VAL   B 16  ? 0.5441 0.4567 0.4653 0.1316  0.0781  0.0254  25  VAL   B CG1 
390  C  CG2 . VAL   B 16  ? 0.5469 0.4702 0.4541 0.1513  0.0707  0.0276  25  VAL   B CG2 
391  N  N   . MET   B 17  ? 0.5644 0.4443 0.4906 0.1521  0.0878  0.0440  26  MET   B N   
392  C  CA  . MET   B 17  ? 0.5864 0.4508 0.5188 0.1474  0.0927  0.0529  26  MET   B CA  
393  C  C   . MET   B 17  ? 0.6182 0.4711 0.5582 0.1319  0.0924  0.0431  26  MET   B C   
394  O  O   . MET   B 17  ? 0.6287 0.4827 0.5674 0.1293  0.0897  0.0283  26  MET   B O   
395  C  CB  . MET   B 17  ? 0.5904 0.4391 0.5194 0.1622  0.0944  0.0570  26  MET   B CB  
396  C  CG  . MET   B 17  ? 0.6012 0.4597 0.5197 0.1803  0.0926  0.0631  26  MET   B CG  
397  S  SD  . MET   B 17  ? 0.6504 0.5183 0.5634 0.1848  0.0977  0.0839  26  MET   B SD  
398  C  CE  . MET   B 17  ? 0.5889 0.4344 0.5088 0.1806  0.1051  0.0980  26  MET   B CE  
399  N  N   . THR   B 18  ? 0.6394 0.4804 0.5870 0.1220  0.0952  0.0514  27  THR   B N   
400  C  CA  . THR   B 18  ? 0.6736 0.4984 0.6272 0.1077  0.0937  0.0416  27  THR   B CA  
401  C  C   . THR   B 18  ? 0.7124 0.5094 0.6710 0.1066  0.0967  0.0500  27  THR   B C   
402  O  O   . THR   B 18  ? 0.7054 0.5019 0.6666 0.1099  0.1010  0.0679  27  THR   B O   
403  C  CB  . THR   B 18  ? 0.6850 0.5239 0.6449 0.0901  0.0909  0.0405  27  THR   B CB  
404  O  OG1 . THR   B 18  ? 0.7085 0.5305 0.6711 0.0777  0.0877  0.0276  27  THR   B OG1 
405  C  CG2 . THR   B 18  ? 0.6807 0.5288 0.6505 0.0834  0.0940  0.0591  27  THR   B CG2 
406  N  N   . ARG   B 19  ? 0.7481 0.5213 0.7071 0.1024  0.0946  0.0372  28  ARG   B N   
407  C  CA  . ARG   B 19  ? 0.7947 0.5358 0.7582 0.0994  0.0962  0.0437  28  ARG   B CA  
408  C  C   . ARG   B 19  ? 0.8208 0.5490 0.7936 0.0769  0.0923  0.0391  28  ARG   B C   
409  O  O   . ARG   B 19  ? 0.8286 0.5261 0.8058 0.0708  0.0921  0.0426  28  ARG   B O   
410  C  CB  . ARG   B 19  ? 0.8374 0.5547 0.7934 0.1152  0.0962  0.0341  28  ARG   B CB  
411  C  CG  . ARG   B 19  ? 0.8959 0.6223 0.8454 0.1365  0.0990  0.0429  28  ARG   B CG  
412  C  CD  . ARG   B 19  ? 0.9677 0.6647 0.9130 0.1514  0.0997  0.0427  28  ARG   B CD  
413  N  NE  . ARG   B 19  ? 1.0226 0.7323 0.9612 0.1729  0.1002  0.0464  28  ARG   B NE  
414  C  CZ  . ARG   B 19  ? 1.0630 0.7862 0.9990 0.1846  0.0976  0.0317  28  ARG   B CZ  
415  N  NH1 . ARG   B 19  ? 1.0617 0.7881 0.9997 0.1778  0.0959  0.0129  28  ARG   B NH1 
416  N  NH2 . ARG   B 19  ? 1.0605 0.7960 0.9921 0.2029  0.0965  0.0358  28  ARG   B NH2 
417  N  N   . ARG   B 20  ? 0.8331 0.5839 0.8083 0.0646  0.0885  0.0316  29  ARG   B N   
418  C  CA  . ARG   B 20  ? 0.8570 0.6032 0.8403 0.0432  0.0826  0.0250  29  ARG   B CA  
419  C  C   . ARG   B 20  ? 0.8602 0.6045 0.8601 0.0285  0.0840  0.0442  29  ARG   B C   
420  O  O   . ARG   B 20  ? 0.8684 0.5938 0.8773 0.0111  0.0790  0.0409  29  ARG   B O   
421  C  CB  . ARG   B 20  ? 0.8797 0.6569 0.8599 0.0377  0.0786  0.0157  29  ARG   B CB  
422  C  CG  . ARG   B 20  ? 0.9412 0.7190 0.9280 0.0170  0.0710  0.0076  29  ARG   B CG  
423  C  CD  . ARG   B 20  ? 0.9925 0.8017 0.9744 0.0142  0.0673  0.0011  29  ARG   B CD  
424  N  NE  . ARG   B 20  ? 1.0276 0.8672 1.0185 0.0134  0.0694  0.0182  29  ARG   B NE  
425  C  CZ  . ARG   B 20  ? 1.0601 0.9148 1.0659 -0.0019 0.0660  0.0267  29  ARG   B CZ  
426  N  NH1 . ARG   B 20  ? 1.0679 0.9084 1.0821 -0.0195 0.0591  0.0197  29  ARG   B NH1 
427  N  NH2 . ARG   B 20  ? 1.0455 0.9296 1.0584 0.0009  0.0689  0.0418  29  ARG   B NH2 
428  N  N   . LEU   B 21  ? 0.8504 0.6142 0.8541 0.0356  0.0907  0.0642  30  LEU   B N   
429  C  CA  . LEU   B 21  ? 0.8467 0.6160 0.8666 0.0241  0.0946  0.0858  30  LEU   B CA  
430  C  C   . LEU   B 21  ? 0.8527 0.5936 0.8718 0.0319  0.1010  0.1011  30  LEU   B C   
431  O  O   . LEU   B 21  ? 0.8721 0.5840 0.8798 0.0432  0.1001  0.0914  30  LEU   B O   
432  C  CB  . LEU   B 21  ? 0.8362 0.6477 0.8587 0.0291  0.0986  0.0980  30  LEU   B CB  
433  C  CG  . LEU   B 21  ? 0.8405 0.6820 0.8741 0.0140  0.0934  0.0949  30  LEU   B CG  
434  C  CD1 . LEU   B 21  ? 0.8532 0.6828 0.8855 0.0005  0.0831  0.0727  30  LEU   B CD1 
435  C  CD2 . LEU   B 21  ? 0.8393 0.7140 0.8647 0.0276  0.0952  0.0968  30  LEU   B CD2 
436  N  N   . LEU   B 22  ? 0.8343 0.5835 0.8656 0.0261  0.1078  0.1253  31  LEU   B N   
437  C  CA  . LEU   B 22  ? 0.8348 0.5585 0.8641 0.0334  0.1148  0.1433  31  LEU   B CA  
438  C  C   . LEU   B 22  ? 0.8295 0.5582 0.8393 0.0612  0.1192  0.1449  31  LEU   B C   
439  O  O   . LEU   B 22  ? 0.8182 0.5805 0.8228 0.0713  0.1218  0.1479  31  LEU   B O   
440  C  CB  . LEU   B 22  ? 0.8226 0.5633 0.8689 0.0218  0.1226  0.1705  31  LEU   B CB  
441  C  CG  . LEU   B 22  ? 0.8461 0.5586 0.8917 0.0254  0.1300  0.1916  31  LEU   B CG  
442  C  CD1 . LEU   B 22  ? 0.8514 0.5255 0.9113 0.0027  0.1252  0.1917  31  LEU   B CD1 
443  C  CD2 . LEU   B 22  ? 0.8458 0.5891 0.8968 0.0292  0.1418  0.2197  31  LEU   B CD2 
444  N  N   . GLY   B 23  ? 0.8326 0.5277 0.8314 0.0738  0.1189  0.1418  32  GLY   B N   
445  C  CA  . GLY   B 23  ? 0.8286 0.5269 0.8098 0.1003  0.1212  0.1420  32  GLY   B CA  
446  C  C   . GLY   B 23  ? 0.8095 0.5349 0.7822 0.1101  0.1168  0.1236  32  GLY   B C   
447  O  O   . GLY   B 23  ? 0.8052 0.5343 0.7812 0.0999  0.1109  0.1049  32  GLY   B O   
448  N  N   . SER   B 24  ? 0.7950 0.5393 0.7558 0.1296  0.1193  0.1293  33  SER   B N   
449  C  CA  . SER   B 24  ? 0.7773 0.5467 0.7305 0.1385  0.1149  0.1143  33  SER   B CA  
450  C  C   . SER   B 24  ? 0.7431 0.5455 0.6983 0.1352  0.1174  0.1234  33  SER   B C   
451  O  O   . SER   B 24  ? 0.7401 0.5517 0.6916 0.1432  0.1234  0.1420  33  SER   B O   
452  C  CB  . SER   B 24  ? 0.8036 0.5710 0.7425 0.1623  0.1137  0.1121  33  SER   B CB  
453  O  OG  . SER   B 24  ? 0.8462 0.5902 0.7842 0.1666  0.1100  0.0981  33  SER   B OG  
454  N  N   . THR   B 25  ? 0.7140 0.5340 0.6738 0.1245  0.1129  0.1110  34  THR   B N   
455  C  CA  . THR   B 25  ? 0.6914 0.5419 0.6536 0.1220  0.1146  0.1185  34  THR   B CA  
456  C  C   . THR   B 25  ? 0.6710 0.5395 0.6224 0.1316  0.1094  0.1056  34  THR   B C   
457  O  O   . THR   B 25  ? 0.6742 0.5386 0.6246 0.1272  0.1037  0.0882  34  THR   B O   
458  C  CB  . THR   B 25  ? 0.7015 0.5587 0.6807 0.0991  0.1136  0.1191  34  THR   B CB  
459  O  OG1 . THR   B 25  ? 0.7237 0.5599 0.7144 0.0876  0.1170  0.1300  34  THR   B OG1 
460  C  CG2 . THR   B 25  ? 0.6884 0.5788 0.6726 0.0976  0.1160  0.1294  34  THR   B CG2 
461  N  N   . GLN   B 26  ? 0.6443 0.5324 0.5871 0.1444  0.1113  0.1141  35  GLN   B N   
462  C  CA  . GLN   B 26  ? 0.6272 0.5293 0.5596 0.1528  0.1055  0.1027  35  GLN   B CA  
463  C  C   . GLN   B 26  ? 0.6168 0.5379 0.5558 0.1411  0.1033  0.1001  35  GLN   B C   
464  O  O   . GLN   B 26  ? 0.6196 0.5575 0.5627 0.1409  0.1076  0.1129  35  GLN   B O   
465  C  CB  . GLN   B 26  ? 0.6166 0.5273 0.5337 0.1736  0.1067  0.1104  35  GLN   B CB  
466  C  CG  . GLN   B 26  ? 0.6184 0.5394 0.5246 0.1814  0.0992  0.0981  35  GLN   B CG  
467  C  CD  . GLN   B 26  ? 0.6398 0.5659 0.5291 0.2024  0.0984  0.1032  35  GLN   B CD  
468  O  OE1 . GLN   B 26  ? 0.6514 0.5679 0.5337 0.2140  0.0997  0.1078  35  GLN   B OE1 
469  N  NE2 . GLN   B 26  ? 0.6219 0.5620 0.5026 0.2088  0.0957  0.1020  35  GLN   B NE2 
470  N  N   . VAL   B 27  ? 0.6013 0.5212 0.5410 0.1323  0.0971  0.0844  36  VAL   B N   
471  C  CA  . VAL   B 27  ? 0.5781 0.5145 0.5218 0.1221  0.0937  0.0809  36  VAL   B CA  
472  C  C   . VAL   B 27  ? 0.5665 0.5157 0.4975 0.1338  0.0897  0.0778  36  VAL   B C   
473  O  O   . VAL   B 27  ? 0.5570 0.5223 0.4890 0.1314  0.0880  0.0804  36  VAL   B O   
474  C  CB  . VAL   B 27  ? 0.5850 0.5130 0.5339 0.1063  0.0892  0.0664  36  VAL   B CB  
475  C  CG1 . VAL   B 27  ? 0.5978 0.5104 0.5584 0.0942  0.0916  0.0684  36  VAL   B CG1 
476  C  CG2 . VAL   B 27  ? 0.5892 0.5076 0.5285 0.1116  0.0856  0.0518  36  VAL   B CG2 
477  N  N   . GLY   B 28  ? 0.5575 0.4986 0.4770 0.1465  0.0872  0.0721  37  GLY   B N   
478  C  CA  . GLY   B 28  ? 0.5437 0.4915 0.4508 0.1566  0.0818  0.0677  37  GLY   B CA  
479  C  C   . GLY   B 28  ? 0.5307 0.4693 0.4278 0.1694  0.0783  0.0619  37  GLY   B C   
480  O  O   . GLY   B 28  ? 0.5190 0.4487 0.4170 0.1750  0.0811  0.0644  37  GLY   B O   
481  N  N   . VAL   B 29  ? 0.5306 0.4711 0.4185 0.1740  0.0714  0.0543  38  VAL   B N   
482  C  CA  . VAL   B 29  ? 0.5347 0.4696 0.4129 0.1856  0.0651  0.0477  38  VAL   B CA  
483  C  C   . VAL   B 29  ? 0.5388 0.4731 0.4166 0.1772  0.0580  0.0363  38  VAL   B C   
484  O  O   . VAL   B 29  ? 0.5481 0.4865 0.4269 0.1678  0.0574  0.0360  38  VAL   B O   
485  C  CB  . VAL   B 29  ? 0.5390 0.4776 0.4020 0.2035  0.0635  0.0545  38  VAL   B CB  
486  C  CG1 . VAL   B 29  ? 0.5490 0.4813 0.4008 0.2158  0.0548  0.0465  38  VAL   B CG1 
487  C  CG2 . VAL   B 29  ? 0.5341 0.4772 0.3970 0.2113  0.0725  0.0690  38  VAL   B CG2 
488  N  N   . GLY   B 30  ? 0.5272 0.4575 0.4032 0.1810  0.0521  0.0281  39  GLY   B N   
489  C  CA  . GLY   B 30  ? 0.5235 0.4535 0.3996 0.1730  0.0453  0.0191  39  GLY   B CA  
490  C  C   . GLY   B 30  ? 0.5227 0.4501 0.3951 0.1810  0.0367  0.0124  39  GLY   B C   
491  O  O   . GLY   B 30  ? 0.5206 0.4470 0.3903 0.1935  0.0359  0.0136  39  GLY   B O   
492  N  N   . VAL   B 31  ? 0.5189 0.4451 0.3914 0.1733  0.0297  0.0059  40  VAL   B N   
493  C  CA  . VAL   B 31  ? 0.5233 0.4475 0.3948 0.1772  0.0194  -0.0014 40  VAL   B CA  
494  C  C   . VAL   B 31  ? 0.5141 0.4466 0.4017 0.1649  0.0193  -0.0083 40  VAL   B C   
495  O  O   . VAL   B 31  ? 0.5079 0.4432 0.4009 0.1508  0.0226  -0.0089 40  VAL   B O   
496  C  CB  . VAL   B 31  ? 0.5404 0.4544 0.3987 0.1785  0.0099  -0.0029 40  VAL   B CB  
497  C  CG1 . VAL   B 31  ? 0.5416 0.4523 0.4013 0.1784  -0.0025 -0.0116 40  VAL   B CG1 
498  C  CG2 . VAL   B 31  ? 0.5596 0.4680 0.4008 0.1947  0.0100  0.0029  40  VAL   B CG2 
499  N  N   . MET   B 32  ? 0.5078 0.4460 0.4025 0.1710  0.0148  -0.0133 41  MET   B N   
500  C  CA  . MET   B 32  ? 0.5038 0.4544 0.4159 0.1610  0.0142  -0.0197 41  MET   B CA  
501  C  C   . MET   B 32  ? 0.5246 0.4744 0.4373 0.1579  0.0010  -0.0250 41  MET   B C   
502  O  O   . MET   B 32  ? 0.5338 0.4789 0.4388 0.1701  -0.0087 -0.0275 41  MET   B O   
503  C  CB  . MET   B 32  ? 0.4899 0.4497 0.4122 0.1705  0.0175  -0.0218 41  MET   B CB  
504  C  CG  . MET   B 32  ? 0.5030 0.4796 0.4450 0.1618  0.0203  -0.0279 41  MET   B CG  
505  S  SD  . MET   B 32  ? 0.5579 0.5389 0.5059 0.1471  0.0341  -0.0277 41  MET   B SD  
506  C  CE  . MET   B 32  ? 0.5370 0.5103 0.4827 0.1592  0.0426  -0.0254 41  MET   B CE  
507  N  N   . GLN   B 33  ? 0.5284 0.4802 0.4478 0.1415  0.0000  -0.0262 42  GLN   B N   
508  C  CA  . GLN   B 33  ? 0.5385 0.4871 0.4603 0.1351  -0.0130 -0.0306 42  GLN   B CA  
509  C  C   . GLN   B 33  ? 0.5384 0.5015 0.4790 0.1164  -0.0097 -0.0314 42  GLN   B C   
510  O  O   . GLN   B 33  ? 0.5474 0.5127 0.4881 0.1067  0.0007  -0.0271 42  GLN   B O   
511  C  CB  . GLN   B 33  ? 0.5787 0.5047 0.4807 0.1362  -0.0202 -0.0284 42  GLN   B CB  
512  C  CG  . GLN   B 33  ? 0.6606 0.5776 0.5634 0.1304  -0.0358 -0.0341 42  GLN   B CG  
513  C  CD  . GLN   B 33  ? 0.7572 0.6481 0.6375 0.1364  -0.0449 -0.0339 42  GLN   B CD  
514  O  OE1 . GLN   B 33  ? 0.8004 0.6776 0.6788 0.1242  -0.0510 -0.0333 42  GLN   B OE1 
515  N  NE2 . GLN   B 33  ? 0.7643 0.6472 0.6263 0.1560  -0.0457 -0.0338 42  GLN   B NE2 
516  N  N   . GLU   B 34  ? 0.5284 0.5043 0.4856 0.1115  -0.0178 -0.0367 43  GLU   B N   
517  C  CA  . GLU   B 34  ? 0.5241 0.5186 0.5021 0.0932  -0.0141 -0.0363 43  GLU   B CA  
518  C  C   . GLU   B 34  ? 0.5169 0.5294 0.5038 0.0900  0.0029  -0.0341 43  GLU   B C   
519  O  O   . GLU   B 34  ? 0.5215 0.5399 0.5123 0.0753  0.0102  -0.0302 43  GLU   B O   
520  C  CB  . GLU   B 34  ? 0.5683 0.5471 0.5402 0.0771  -0.0192 -0.0321 43  GLU   B CB  
521  C  CG  . GLU   B 34  ? 0.6309 0.5908 0.5957 0.0788  -0.0376 -0.0364 43  GLU   B CG  
522  C  CD  . GLU   B 34  ? 0.7244 0.6574 0.6744 0.0690  -0.0437 -0.0321 43  GLU   B CD  
523  O  OE1 . GLU   B 34  ? 0.7296 0.6663 0.6876 0.0509  -0.0383 -0.0258 43  GLU   B OE1 
524  O  OE2 . GLU   B 34  ? 0.7788 0.6868 0.7082 0.0804  -0.0538 -0.0347 43  GLU   B OE2 
525  N  N   . GLY   B 35  ? 0.5012 0.5199 0.4889 0.1045  0.0088  -0.0366 44  GLY   B N   
526  C  CA  . GLY   B 35  ? 0.4866 0.5189 0.4809 0.1043  0.0234  -0.0368 44  GLY   B CA  
527  C  C   . GLY   B 35  ? 0.4845 0.5029 0.4624 0.1012  0.0327  -0.0325 44  GLY   B C   
528  O  O   . GLY   B 35  ? 0.4870 0.5141 0.4679 0.0999  0.0440  -0.0338 44  GLY   B O   
529  N  N   . VAL   B 36  ? 0.4734 0.4707 0.4336 0.1009  0.0276  -0.0278 45  VAL   B N   
530  C  CA  . VAL   B 36  ? 0.4624 0.4484 0.4080 0.0978  0.0343  -0.0232 45  VAL   B CA  
531  C  C   . VAL   B 36  ? 0.4598 0.4309 0.3923 0.1115  0.0332  -0.0208 45  VAL   B C   
532  O  O   . VAL   B 36  ? 0.4613 0.4229 0.3870 0.1206  0.0243  -0.0201 45  VAL   B O   
533  C  CB  . VAL   B 36  ? 0.4728 0.4505 0.4103 0.0844  0.0309  -0.0180 45  VAL   B CB  
534  C  CG1 . VAL   B 36  ? 0.4847 0.4504 0.4056 0.0839  0.0350  -0.0129 45  VAL   B CG1 
535  C  CG2 . VAL   B 36  ? 0.4709 0.4656 0.4210 0.0693  0.0360  -0.0179 45  VAL   B CG2 
536  N  N   . PHE   B 37  ? 0.4498 0.4196 0.3790 0.1132  0.0421  -0.0196 46  PHE   B N   
537  C  CA  . PHE   B 37  ? 0.4555 0.4135 0.3746 0.1238  0.0424  -0.0153 46  PHE   B CA  
538  C  C   . PHE   B 37  ? 0.4509 0.4008 0.3577 0.1182  0.0418  -0.0095 46  PHE   B C   
539  O  O   . PHE   B 37  ? 0.4463 0.3996 0.3525 0.1071  0.0461  -0.0094 46  PHE   B O   
540  C  CB  . PHE   B 37  ? 0.4495 0.4085 0.3735 0.1280  0.0509  -0.0167 46  PHE   B CB  
541  C  CG  . PHE   B 37  ? 0.4648 0.4131 0.3813 0.1384  0.0514  -0.0103 46  PHE   B CG  
542  C  CD1 . PHE   B 37  ? 0.4718 0.4168 0.3852 0.1521  0.0463  -0.0080 46  PHE   B CD1 
543  C  CD2 . PHE   B 37  ? 0.4768 0.4200 0.3892 0.1341  0.0566  -0.0060 46  PHE   B CD2 
544  C  CE1 . PHE   B 37  ? 0.4847 0.4219 0.3906 0.1619  0.0484  -0.0003 46  PHE   B CE1 
545  C  CE2 . PHE   B 37  ? 0.4869 0.4232 0.3948 0.1422  0.0579  0.0017  46  PHE   B CE2 
546  C  CZ  . PHE   B 37  ? 0.4840 0.4176 0.3882 0.1563  0.0546  0.0052  46  PHE   B CZ  
547  N  N   . HIS   B 38  ? 0.4561 0.3965 0.3522 0.1268  0.0363  -0.0048 47  HIS   B N   
548  C  CA  . HIS   B 38  ? 0.4635 0.3976 0.3483 0.1245  0.0350  0.0009  47  HIS   B CA  
549  C  C   . HIS   B 38  ? 0.4759 0.4090 0.3564 0.1338  0.0389  0.0069  47  HIS   B C   
550  O  O   . HIS   B 38  ? 0.4663 0.3968 0.3440 0.1466  0.0374  0.0086  47  HIS   B O   
551  C  CB  . HIS   B 38  ? 0.4726 0.3962 0.3474 0.1287  0.0247  0.0013  47  HIS   B CB  
552  C  CG  . HIS   B 38  ? 0.5059 0.4292 0.3866 0.1198  0.0189  -0.0035 47  HIS   B CG  
553  N  ND1 . HIS   B 38  ? 0.5165 0.4470 0.4086 0.1215  0.0167  -0.0094 47  HIS   B ND1 
554  C  CD2 . HIS   B 38  ? 0.5263 0.4431 0.4035 0.1092  0.0144  -0.0023 47  HIS   B CD2 
555  C  CE1 . HIS   B 38  ? 0.5137 0.4444 0.4113 0.1104  0.0114  -0.0116 47  HIS   B CE1 
556  N  NE2 . HIS   B 38  ? 0.5339 0.4552 0.4225 0.1022  0.0102  -0.0070 47  HIS   B NE2 
557  N  N   . THR   B 39  ? 0.4894 0.4256 0.3690 0.1274  0.0433  0.0109  48  THR   B N   
558  C  CA  . THR   B 39  ? 0.4938 0.4321 0.3722 0.1341  0.0469  0.0182  48  THR   B CA  
559  C  C   . THR   B 39  ? 0.4971 0.4395 0.3710 0.1286  0.0462  0.0230  48  THR   B C   
560  O  O   . THR   B 39  ? 0.4855 0.4260 0.3544 0.1216  0.0424  0.0212  48  THR   B O   
561  C  CB  . THR   B 39  ? 0.5012 0.4413 0.3898 0.1328  0.0540  0.0178  48  THR   B CB  
562  O  OG1 . THR   B 39  ? 0.5158 0.4581 0.4044 0.1393  0.0573  0.0268  48  THR   B OG1 
563  C  CG2 . THR   B 39  ? 0.5030 0.4459 0.3978 0.1187  0.0579  0.0128  48  THR   B CG2 
564  N  N   . MET   B 40  ? 0.5044 0.4537 0.3808 0.1318  0.0497  0.0303  49  MET   B N   
565  C  CA  . MET   B 40  ? 0.5045 0.4620 0.3797 0.1271  0.0487  0.0350  49  MET   B CA  
566  C  C   . MET   B 40  ? 0.5021 0.4653 0.3862 0.1123  0.0522  0.0321  49  MET   B C   
567  O  O   . MET   B 40  ? 0.5094 0.4709 0.4020 0.1092  0.0569  0.0300  49  MET   B O   
568  C  CB  . MET   B 40  ? 0.5091 0.4753 0.3841 0.1387  0.0504  0.0446  49  MET   B CB  
569  C  CG  . MET   B 40  ? 0.5461 0.5053 0.4096 0.1555  0.0471  0.0456  49  MET   B CG  
570  S  SD  . MET   B 40  ? 0.5630 0.5339 0.4204 0.1712  0.0474  0.0557  49  MET   B SD  
571  C  CE  . MET   B 40  ? 0.5451 0.5108 0.3929 0.1685  0.0392  0.0532  49  MET   B CE  
572  N  N   . TRP   B 41  ? 0.4947 0.4627 0.3751 0.1039  0.0492  0.0317  50  TRP   B N   
573  C  CA  A TRP   B 41  ? 0.5010 0.4740 0.3863 0.0904  0.0507  0.0273  50  TRP   B CA  
574  C  CA  B TRP   B 41  ? 0.4882 0.4613 0.3734 0.0904  0.0506  0.0274  50  TRP   B CA  
575  C  C   . TRP   B 41  ? 0.4950 0.4752 0.3928 0.0872  0.0537  0.0308  50  TRP   B C   
576  O  O   . TRP   B 41  ? 0.4939 0.4704 0.3974 0.0784  0.0561  0.0246  50  TRP   B O   
577  C  CB  A TRP   B 41  ? 0.5062 0.4848 0.3828 0.0840  0.0458  0.0278  50  TRP   B CB  
578  C  CB  B TRP   B 41  ? 0.4748 0.4538 0.3514 0.0845  0.0456  0.0283  50  TRP   B CB  
579  C  CG  A TRP   B 41  ? 0.5214 0.5028 0.3979 0.0709  0.0466  0.0204  50  TRP   B CG  
580  C  CG  B TRP   B 41  ? 0.4634 0.4475 0.3415 0.0714  0.0459  0.0223  50  TRP   B CG  
581  C  CD1 A TRP   B 41  ? 0.5381 0.5145 0.4083 0.0648  0.0485  0.0126  50  TRP   B CD1 
582  C  CD1 B TRP   B 41  ? 0.4637 0.4577 0.3500 0.0651  0.0447  0.0232  50  TRP   B CD1 
583  C  CD2 A TRP   B 41  ? 0.5238 0.5144 0.4068 0.0626  0.0453  0.0194  50  TRP   B CD2 
584  C  CD2 B TRP   B 41  ? 0.4602 0.4398 0.3316 0.0634  0.0475  0.0136  50  TRP   B CD2 
585  N  NE1 A TRP   B 41  ? 0.5453 0.5259 0.4145 0.0550  0.0487  0.0061  50  TRP   B NE1 
586  N  NE1 B TRP   B 41  ? 0.4652 0.4586 0.3481 0.0540  0.0441  0.0142  50  TRP   B NE1 
587  C  CE2 A TRP   B 41  ? 0.5387 0.5267 0.4158 0.0529  0.0458  0.0095  50  TRP   B CE2 
588  C  CE2 B TRP   B 41  ? 0.4660 0.4513 0.3388 0.0537  0.0466  0.0083  50  TRP   B CE2 
589  C  CE3 A TRP   B 41  ? 0.5295 0.5317 0.4234 0.0622  0.0435  0.0259  50  TRP   B CE3 
590  C  CE3 B TRP   B 41  ? 0.4690 0.4421 0.3338 0.0632  0.0495  0.0099  50  TRP   B CE3 
591  C  CZ2 A TRP   B 41  ? 0.5484 0.5417 0.4281 0.0431  0.0432  0.0043  50  TRP   B CZ2 
592  C  CZ2 B TRP   B 41  ? 0.4718 0.4554 0.3366 0.0461  0.0483  -0.0012 50  TRP   B CZ2 
593  C  CZ3 A TRP   B 41  ? 0.5399 0.5492 0.4398 0.0506  0.0408  0.0218  50  TRP   B CZ3 
594  C  CZ3 B TRP   B 41  ? 0.4793 0.4540 0.3385 0.0548  0.0523  0.0022  50  TRP   B CZ3 
595  C  CH2 A TRP   B 41  ? 0.5452 0.5487 0.4368 0.0413  0.0398  0.0105  50  TRP   B CH2 
596  C  CH2 B TRP   B 41  ? 0.4767 0.4561 0.3345 0.0474  0.0519  -0.0037 50  TRP   B CH2 
597  N  N   . HIS   B 42  ? 0.4952 0.4858 0.3975 0.0939  0.0536  0.0406  51  HIS   B N   
598  C  CA  . HIS   B 42  ? 0.4924 0.4923 0.4093 0.0888  0.0567  0.0461  51  HIS   B CA  
599  C  C   . HIS   B 42  ? 0.4965 0.4853 0.4208 0.0897  0.0628  0.0460  51  HIS   B C   
600  O  O   . HIS   B 42  ? 0.4902 0.4812 0.4269 0.0814  0.0651  0.0489  51  HIS   B O   
601  C  CB  . HIS   B 42  ? 0.4789 0.4972 0.4009 0.0963  0.0565  0.0579  51  HIS   B CB  
602  C  CG  . HIS   B 42  ? 0.4843 0.5015 0.4028 0.1129  0.0606  0.0652  51  HIS   B CG  
603  N  ND1 . HIS   B 42  ? 0.5057 0.5193 0.4097 0.1267  0.0574  0.0653  51  HIS   B ND1 
604  C  CD2 . HIS   B 42  ? 0.4927 0.5109 0.4186 0.1177  0.0673  0.0724  51  HIS   B CD2 
605  C  CE1 . HIS   B 42  ? 0.5119 0.5252 0.4140 0.1403  0.0618  0.0711  51  HIS   B CE1 
606  N  NE2 . HIS   B 42  ? 0.5118 0.5284 0.4264 0.1355  0.0683  0.0761  51  HIS   B NE2 
607  N  N   . VAL   B 43  ? 0.5045 0.4809 0.4214 0.0991  0.0645  0.0428  52  VAL   B N   
608  C  CA  . VAL   B 43  ? 0.5134 0.4782 0.4350 0.1021  0.0694  0.0426  52  VAL   B CA  
609  C  C   . VAL   B 43  ? 0.5291 0.4823 0.4538 0.0914  0.0699  0.0314  52  VAL   B C   
610  O  O   . VAL   B 43  ? 0.5411 0.4866 0.4744 0.0867  0.0730  0.0324  52  VAL   B O   
611  C  CB  . VAL   B 43  ? 0.5259 0.4842 0.4381 0.1172  0.0692  0.0426  52  VAL   B CB  
612  C  CG1 . VAL   B 43  ? 0.5326 0.4785 0.4480 0.1213  0.0730  0.0407  52  VAL   B CG1 
613  C  CG2 . VAL   B 43  ? 0.5278 0.4952 0.4352 0.1302  0.0694  0.0530  52  VAL   B CG2 
614  N  N   . THR   B 44  ? 0.5274 0.4784 0.4444 0.0882  0.0673  0.0211  53  THR   B N   
615  C  CA  . THR   B 44  ? 0.5341 0.4759 0.4518 0.0811  0.0687  0.0095  53  THR   B CA  
616  C  C   . THR   B 44  ? 0.5568 0.5025 0.4726 0.0680  0.0659  0.0030  53  THR   B C   
617  O  O   . THR   B 44  ? 0.5681 0.5047 0.4845 0.0623  0.0671  -0.0066 53  THR   B O   
618  C  CB  . THR   B 44  ? 0.5236 0.4627 0.4355 0.0868  0.0693  0.0021  53  THR   B CB  
619  O  OG1 . THR   B 44  ? 0.5238 0.4714 0.4275 0.0829  0.0660  0.0006  53  THR   B OG1 
620  C  CG2 . THR   B 44  ? 0.5219 0.4580 0.4345 0.1005  0.0699  0.0071  53  THR   B CG2 
621  N  N   . LYS   B 45  ? 0.5572 0.5157 0.4690 0.0646  0.0616  0.0074  54  LYS   B N   
622  C  CA  . LYS   B 45  ? 0.5652 0.5302 0.4719 0.0534  0.0574  0.0017  54  LYS   B CA  
623  C  C   . LYS   B 45  ? 0.5698 0.5313 0.4649 0.0513  0.0586  -0.0093 54  LYS   B C   
624  O  O   . LYS   B 45  ? 0.5765 0.5393 0.4654 0.0428  0.0566  -0.0173 54  LYS   B O   
625  C  CB  . LYS   B 45  ? 0.5950 0.5581 0.5109 0.0428  0.0555  -0.0010 54  LYS   B CB  
626  C  CG  . LYS   B 45  ? 0.6799 0.6481 0.6108 0.0432  0.0563  0.0111  54  LYS   B CG  
627  C  CD  . LYS   B 45  ? 0.7702 0.7590 0.7049 0.0401  0.0512  0.0193  54  LYS   B CD  
628  C  CE  . LYS   B 45  ? 0.8445 0.8416 0.7975 0.0370  0.0527  0.0305  54  LYS   B CE  
629  N  NZ  . LYS   B 45  ? 0.8872 0.8905 0.8425 0.0512  0.0581  0.0434  54  LYS   B NZ  
630  N  N   . GLY   B 46  ? 0.5614 0.5199 0.4537 0.0589  0.0617  -0.0095 55  GLY   B N   
631  C  CA  . GLY   B 46  ? 0.5647 0.5235 0.4494 0.0574  0.0645  -0.0178 55  GLY   B CA  
632  C  C   . GLY   B 46  ? 0.5751 0.5260 0.4632 0.0582  0.0695  -0.0287 55  GLY   B C   
633  O  O   . GLY   B 46  ? 0.5867 0.5411 0.4690 0.0573  0.0730  -0.0364 55  GLY   B O   
634  N  N   . ALA   B 47  ? 0.5712 0.5112 0.4684 0.0606  0.0704  -0.0291 56  ALA   B N   
635  C  CA  . ALA   B 47  ? 0.5685 0.4969 0.4678 0.0633  0.0745  -0.0399 56  ALA   B CA  
636  C  C   . ALA   B 47  ? 0.5744 0.5030 0.4780 0.0744  0.0789  -0.0410 56  ALA   B C   
637  O  O   . ALA   B 47  ? 0.5766 0.5099 0.4836 0.0801  0.0778  -0.0325 56  ALA   B O   
638  C  CB  . ALA   B 47  ? 0.5643 0.4778 0.4716 0.0614  0.0734  -0.0385 56  ALA   B CB  
639  N  N   . ALA   B 48  ? 0.5782 0.5019 0.4818 0.0786  0.0833  -0.0520 57  ALA   B N   
640  C  CA  . ALA   B 48  ? 0.5836 0.5109 0.4936 0.0897  0.0870  -0.0539 57  ALA   B CA  
641  C  C   . ALA   B 48  ? 0.5971 0.5133 0.5155 0.0993  0.0860  -0.0465 57  ALA   B C   
642  O  O   . ALA   B 48  ? 0.6082 0.5102 0.5280 0.0974  0.0846  -0.0423 57  ALA   B O   
643  C  CB  . ALA   B 48  ? 0.5792 0.5052 0.4871 0.0937  0.0924  -0.0678 57  ALA   B CB  
644  N  N   . LEU   B 49  ? 0.5956 0.5194 0.5197 0.1089  0.0861  -0.0439 58  LEU   B N   
645  C  CA  . LEU   B 49  ? 0.6120 0.5269 0.5414 0.1198  0.0847  -0.0364 58  LEU   B CA  
646  C  C   . LEU   B 49  ? 0.6332 0.5472 0.5689 0.1323  0.0873  -0.0429 58  LEU   B C   
647  O  O   . LEU   B 49  ? 0.6376 0.5652 0.5762 0.1332  0.0897  -0.0512 58  LEU   B O   
648  C  CB  . LEU   B 49  ? 0.6097 0.5342 0.5386 0.1225  0.0802  -0.0269 58  LEU   B CB  
649  C  CG  . LEU   B 49  ? 0.6243 0.5513 0.5470 0.1137  0.0772  -0.0196 58  LEU   B CG  
650  C  CD1 . LEU   B 49  ? 0.6313 0.5647 0.5516 0.1195  0.0723  -0.0125 58  LEU   B CD1 
651  C  CD2 . LEU   B 49  ? 0.6285 0.5444 0.5514 0.1106  0.0781  -0.0133 58  LEU   B CD2 
652  N  N   . ARG   B 50  ? 0.6449 0.5444 0.5831 0.1425  0.0871  -0.0381 59  ARG   B N   
653  C  CA  . ARG   B 50  ? 0.6594 0.5566 0.6033 0.1569  0.0886  -0.0430 59  ARG   B CA  
654  C  C   . ARG   B 50  ? 0.6689 0.5728 0.6159 0.1687  0.0843  -0.0346 59  ARG   B C   
655  O  O   . ARG   B 50  ? 0.6654 0.5645 0.6078 0.1685  0.0816  -0.0238 59  ARG   B O   
656  C  CB  . ARG   B 50  ? 0.6933 0.5640 0.6354 0.1603  0.0912  -0.0445 59  ARG   B CB  
657  C  CG  . ARG   B 50  ? 0.7631 0.6250 0.7093 0.1779  0.0921  -0.0466 59  ARG   B CG  
658  C  CD  . ARG   B 50  ? 0.8314 0.6635 0.7744 0.1796  0.0945  -0.0512 59  ARG   B CD  
659  N  NE  . ARG   B 50  ? 0.8862 0.6974 0.8258 0.1694  0.0934  -0.0407 59  ARG   B NE  
660  C  CZ  . ARG   B 50  ? 0.9309 0.7274 0.8706 0.1756  0.0928  -0.0267 59  ARG   B CZ  
661  N  NH1 . ARG   B 50  ? 0.9266 0.7257 0.8676 0.1930  0.0921  -0.0221 59  ARG   B NH1 
662  N  NH2 . ARG   B 50  ? 0.9459 0.7271 0.8849 0.1644  0.0929  -0.0167 59  ARG   B NH2 
663  N  N   . SER   B 51  ? 0.6809 0.5988 0.6356 0.1789  0.0833  -0.0400 60  SER   B N   
664  C  CA  . SER   B 51  ? 0.7052 0.6302 0.6625 0.1912  0.0774  -0.0340 60  SER   B CA  
665  C  C   . SER   B 51  ? 0.7331 0.6599 0.6985 0.2072  0.0782  -0.0396 60  SER   B C   
666  O  O   . SER   B 51  ? 0.7288 0.6775 0.7050 0.2095  0.0781  -0.0477 60  SER   B O   
667  C  CB  . SER   B 51  ? 0.7060 0.6533 0.6668 0.1852  0.0722  -0.0351 60  SER   B CB  
668  O  OG  . SER   B 51  ? 0.7222 0.6773 0.6860 0.1976  0.0650  -0.0323 60  SER   B OG  
669  N  N   . GLY   B 52  ? 0.7569 0.6613 0.7179 0.2180  0.0795  -0.0346 61  GLY   B N   
670  C  CA  . GLY   B 52  ? 0.7751 0.6763 0.7420 0.2350  0.0803  -0.0394 61  GLY   B CA  
671  C  C   . GLY   B 52  ? 0.7922 0.6896 0.7617 0.2313  0.0870  -0.0518 61  GLY   B C   
672  O  O   . GLY   B 52  ? 0.8090 0.6866 0.7709 0.2205  0.0905  -0.0526 61  GLY   B O   
673  N  N   . GLU   B 53  ? 0.7850 0.7039 0.7654 0.2395  0.0885  -0.0621 62  GLU   B N   
674  C  CA  . GLU   B 53  ? 0.7894 0.7088 0.7705 0.2376  0.0957  -0.0753 62  GLU   B CA  
675  C  C   . GLU   B 53  ? 0.7738 0.7145 0.7552 0.2189  0.0987  -0.0799 62  GLU   B C   
676  O  O   . GLU   B 53  ? 0.7838 0.7200 0.7594 0.2131  0.1045  -0.0891 62  GLU   B O   
677  C  CB  . GLU   B 53  ? 0.8199 0.7550 0.8126 0.2567  0.0978  -0.0841 62  GLU   B CB  
678  C  CG  . GLU   B 53  ? 0.9273 0.8310 0.9143 0.2738  0.0993  -0.0868 62  GLU   B CG  
679  C  CD  . GLU   B 53  ? 1.0503 0.9713 1.0493 0.2961  0.1006  -0.0946 62  GLU   B CD  
680  O  OE1 . GLU   B 53  ? 1.0604 1.0163 1.0742 0.3009  0.0971  -0.0928 62  GLU   B OE1 
681  O  OE2 . GLU   B 53  ? 1.1001 0.9996 1.0942 0.3091  0.1045  -0.1028 62  GLU   B OE2 
682  N  N   . GLY   B 54  ? 0.7478 0.7093 0.7341 0.2104  0.0942  -0.0736 63  GLY   B N   
683  C  CA  . GLY   B 54  ? 0.7295 0.7103 0.7160 0.1934  0.0962  -0.0753 63  GLY   B CA  
684  C  C   . GLY   B 54  ? 0.7215 0.6856 0.6939 0.1775  0.0968  -0.0722 63  GLY   B C   
685  O  O   . GLY   B 54  ? 0.7368 0.6767 0.7009 0.1770  0.0943  -0.0658 63  GLY   B O   
686  N  N   . ARG   B 55  ? 0.6926 0.6714 0.6626 0.1644  0.1004  -0.0760 64  ARG   B N   
687  C  CA  . ARG   B 55  ? 0.6784 0.6464 0.6354 0.1493  0.1004  -0.0737 64  ARG   B CA  
688  C  C   . ARG   B 55  ? 0.6414 0.6257 0.5988 0.1371  0.0969  -0.0665 64  ARG   B C   
689  O  O   . ARG   B 55  ? 0.6286 0.6361 0.5950 0.1352  0.0982  -0.0678 64  ARG   B O   
690  C  CB  . ARG   B 55  ? 0.6957 0.6633 0.6448 0.1456  0.1074  -0.0851 64  ARG   B CB  
691  C  CG  . ARG   B 55  ? 0.7379 0.6935 0.6728 0.1313  0.1062  -0.0842 64  ARG   B CG  
692  C  CD  . ARG   B 55  ? 0.7951 0.7494 0.7198 0.1300  0.1120  -0.0974 64  ARG   B CD  
693  N  NE  . ARG   B 55  ? 0.8399 0.7887 0.7507 0.1157  0.1098  -0.0972 64  ARG   B NE  
694  C  CZ  . ARG   B 55  ? 0.8829 0.8133 0.7822 0.1129  0.1091  -0.1061 64  ARG   B CZ  
695  N  NH1 . ARG   B 55  ? 0.8777 0.7894 0.7767 0.1234  0.1106  -0.1160 64  ARG   B NH1 
696  N  NH2 . ARG   B 55  ? 0.8890 0.8184 0.7768 0.1000  0.1057  -0.1055 64  ARG   B NH2 
697  N  N   . LEU   B 56  ? 0.6178 0.5897 0.5663 0.1291  0.0924  -0.0587 65  LEU   B N   
698  C  CA  . LEU   B 56  ? 0.5964 0.5779 0.5422 0.1185  0.0885  -0.0520 65  LEU   B CA  
699  C  C   . LEU   B 56  ? 0.5788 0.5563 0.5122 0.1062  0.0907  -0.0528 65  LEU   B C   
700  O  O   . LEU   B 56  ? 0.5804 0.5420 0.5068 0.1045  0.0894  -0.0512 65  LEU   B O   
701  C  CB  . LEU   B 56  ? 0.6008 0.5725 0.5445 0.1216  0.0808  -0.0422 65  LEU   B CB  
702  C  CG  . LEU   B 56  ? 0.6267 0.5986 0.5782 0.1353  0.0767  -0.0404 65  LEU   B CG  
703  C  CD1 . LEU   B 56  ? 0.6314 0.5974 0.5771 0.1371  0.0692  -0.0317 65  LEU   B CD1 
704  C  CD2 . LEU   B 56  ? 0.6310 0.6240 0.5959 0.1378  0.0763  -0.0457 65  LEU   B CD2 
705  N  N   . ASP   B 57  ? 0.5637 0.5565 0.4947 0.0976  0.0940  -0.0547 66  ASP   B N   
706  C  CA  . ASP   B 57  ? 0.5688 0.5597 0.4861 0.0869  0.0953  -0.0550 66  ASP   B CA  
707  C  C   . ASP   B 57  ? 0.5550 0.5465 0.4667 0.0783  0.0894  -0.0445 66  ASP   B C   
708  O  O   . ASP   B 57  ? 0.5499 0.5487 0.4682 0.0777  0.0866  -0.0395 66  ASP   B O   
709  C  CB  . ASP   B 57  ? 0.6165 0.6230 0.5307 0.0841  0.1035  -0.0630 66  ASP   B CB  
710  C  CG  . ASP   B 57  ? 0.7305 0.7335 0.6471 0.0945  0.1091  -0.0750 66  ASP   B CG  
711  O  OD1 . ASP   B 57  ? 0.7552 0.7382 0.6655 0.0967  0.1070  -0.0792 66  ASP   B OD1 
712  O  OD2 . ASP   B 57  ? 0.7667 0.7868 0.6921 0.1005  0.1152  -0.0799 66  ASP   B OD2 
713  N  N   . PRO   B 58  ? 0.5450 0.5283 0.4451 0.0721  0.0865  -0.0413 67  PRO   B N   
714  C  CA  . PRO   B 58  ? 0.5317 0.5146 0.4254 0.0662  0.0807  -0.0314 67  PRO   B CA  
715  C  C   . PRO   B 58  ? 0.5188 0.5139 0.4088 0.0580  0.0829  -0.0288 67  PRO   B C   
716  O  O   . PRO   B 58  ? 0.5153 0.5212 0.4023 0.0545  0.0899  -0.0343 67  PRO   B O   
717  C  CB  . PRO   B 58  ? 0.5486 0.5246 0.4321 0.0619  0.0781  -0.0302 67  PRO   B CB  
718  C  CG  . PRO   B 58  ? 0.5556 0.5316 0.4363 0.0609  0.0832  -0.0412 67  PRO   B CG  
719  C  CD  . PRO   B 58  ? 0.5385 0.5130 0.4309 0.0700  0.0874  -0.0471 67  PRO   B CD  
720  N  N   . TYR   B 59  ? 0.5056 0.4983 0.3949 0.0553  0.0773  -0.0201 68  TYR   B N   
721  C  CA  . TYR   B 59  ? 0.4941 0.4953 0.3811 0.0461  0.0786  -0.0152 68  TYR   B CA  
722  C  C   . TYR   B 59  ? 0.4982 0.4908 0.3700 0.0403  0.0734  -0.0063 68  TYR   B C   
723  O  O   . TYR   B 59  ? 0.5099 0.5085 0.3719 0.0321  0.0768  -0.0030 68  TYR   B O   
724  C  CB  . TYR   B 59  ? 0.4803 0.4841 0.3813 0.0470  0.0751  -0.0132 68  TYR   B CB  
725  C  CG  . TYR   B 59  ? 0.4818 0.4948 0.3847 0.0354  0.0767  -0.0073 68  TYR   B CG  
726  C  CD1 . TYR   B 59  ? 0.4962 0.4969 0.3895 0.0287  0.0700  0.0024  68  TYR   B CD1 
727  C  CD2 . TYR   B 59  ? 0.4685 0.5025 0.3844 0.0316  0.0846  -0.0105 68  TYR   B CD2 
728  C  CE1 . TYR   B 59  ? 0.5012 0.5076 0.3967 0.0165  0.0713  0.0095  68  TYR   B CE1 
729  C  CE2 . TYR   B 59  ? 0.4712 0.5156 0.3918 0.0193  0.0865  -0.0032 68  TYR   B CE2 
730  C  CZ  . TYR   B 59  ? 0.4992 0.5283 0.4095 0.0109  0.0797  0.0072  68  TYR   B CZ  
731  O  OH  . TYR   B 59  ? 0.5178 0.5550 0.4329 -0.0029 0.0819  0.0159  68  TYR   B OH  
732  N  N   . TRP   B 60  ? 0.4967 0.4760 0.3659 0.0458  0.0655  -0.0019 69  TRP   B N   
733  C  CA  . TRP   B 60  ? 0.4985 0.4687 0.3541 0.0436  0.0593  0.0068  69  TRP   B CA  
734  C  C   . TRP   B 60  ? 0.5008 0.4647 0.3547 0.0521  0.0549  0.0073  69  TRP   B C   
735  O  O   . TRP   B 60  ? 0.4955 0.4566 0.3585 0.0602  0.0542  0.0047  69  TRP   B O   
736  C  CB  . TRP   B 60  ? 0.4935 0.4535 0.3489 0.0421  0.0528  0.0138  69  TRP   B CB  
737  C  CG  . TRP   B 60  ? 0.5075 0.4539 0.3492 0.0446  0.0451  0.0221  69  TRP   B CG  
738  C  CD1 . TRP   B 60  ? 0.5268 0.4710 0.3543 0.0384  0.0443  0.0293  69  TRP   B CD1 
739  C  CD2 . TRP   B 60  ? 0.5122 0.4473 0.3517 0.0562  0.0379  0.0238  69  TRP   B CD2 
740  N  NE1 . TRP   B 60  ? 0.5350 0.4670 0.3528 0.0459  0.0363  0.0352  69  TRP   B NE1 
741  C  CE2 . TRP   B 60  ? 0.5267 0.4538 0.3519 0.0571  0.0327  0.0317  69  TRP   B CE2 
742  C  CE3 . TRP   B 60  ? 0.5180 0.4504 0.3652 0.0672  0.0358  0.0200  69  TRP   B CE3 
743  C  CZ2 . TRP   B 60  ? 0.5356 0.4535 0.3555 0.0691  0.0260  0.0351  69  TRP   B CZ2 
744  C  CZ3 . TRP   B 60  ? 0.5307 0.4541 0.3712 0.0785  0.0298  0.0238  69  TRP   B CZ3 
745  C  CH2 . TRP   B 60  ? 0.5390 0.4556 0.3666 0.0796  0.0250  0.0310  69  TRP   B CH2 
746  N  N   . GLY   B 61  ? 0.5078 0.4714 0.3506 0.0503  0.0521  0.0118  70  GLY   B N   
747  C  CA  . GLY   B 61  ? 0.5127 0.4749 0.3562 0.0572  0.0482  0.0138  70  GLY   B CA  
748  C  C   . GLY   B 61  ? 0.5113 0.4737 0.3427 0.0565  0.0427  0.0212  70  GLY   B C   
749  O  O   . GLY   B 61  ? 0.5153 0.4797 0.3356 0.0493  0.0429  0.0234  70  GLY   B O   
750  N  N   . ASP   B 62  ? 0.5042 0.4664 0.3375 0.0648  0.0382  0.0256  71  ASP   B N   
751  C  CA  . ASP   B 62  ? 0.5097 0.4744 0.3336 0.0673  0.0321  0.0331  71  ASP   B CA  
752  C  C   . ASP   B 62  ? 0.5056 0.4788 0.3388 0.0753  0.0304  0.0355  71  ASP   B C   
753  O  O   . ASP   B 62  ? 0.4996 0.4683 0.3378 0.0853  0.0304  0.0375  71  ASP   B O   
754  C  CB  . ASP   B 62  ? 0.5510 0.5011 0.3644 0.0724  0.0268  0.0400  71  ASP   B CB  
755  C  CG  . ASP   B 62  ? 0.6437 0.5937 0.4441 0.0747  0.0205  0.0481  71  ASP   B CG  
756  O  OD1 . ASP   B 62  ? 0.6529 0.6096 0.4553 0.0840  0.0168  0.0518  71  ASP   B OD1 
757  O  OD2 . ASP   B 62  ? 0.7131 0.6572 0.5014 0.0680  0.0195  0.0518  71  ASP   B OD2 
758  N  N   . VAL   B 63  ? 0.5031 0.4901 0.3382 0.0708  0.0287  0.0357  72  VAL   B N   
759  C  CA  . VAL   B 63  ? 0.4939 0.4942 0.3412 0.0753  0.0274  0.0391  72  VAL   B CA  
760  C  C   . VAL   B 63  ? 0.5023 0.5046 0.3463 0.0888  0.0228  0.0485  72  VAL   B C   
761  O  O   . VAL   B 63  ? 0.5040 0.5122 0.3578 0.0977  0.0247  0.0521  72  VAL   B O   
762  C  CB  . VAL   B 63  ? 0.4822 0.4972 0.3330 0.0645  0.0250  0.0357  72  VAL   B CB  
763  C  CG1 . VAL   B 63  ? 0.4687 0.5022 0.3315 0.0680  0.0212  0.0422  72  VAL   B CG1 
764  C  CG2 . VAL   B 63  ? 0.4857 0.4972 0.3435 0.0549  0.0302  0.0254  72  VAL   B CG2 
765  N  N   . LYS   B 64  ? 0.5135 0.5097 0.3426 0.0918  0.0172  0.0529  73  LYS   B N   
766  C  CA  . LYS   B 64  ? 0.5222 0.5177 0.3461 0.1069  0.0121  0.0610  73  LYS   B CA  
767  C  C   . LYS   B 64  ? 0.5290 0.5078 0.3503 0.1187  0.0134  0.0610  73  LYS   B C   
768  O  O   . LYS   B 64  ? 0.5258 0.5108 0.3509 0.1324  0.0132  0.0648  73  LYS   B O   
769  C  CB  . LYS   B 64  ? 0.5529 0.5433 0.3603 0.1079  0.0050  0.0664  73  LYS   B CB  
770  C  CG  . LYS   B 64  ? 0.5887 0.5819 0.3924 0.1255  -0.0006 0.0745  73  LYS   B CG  
771  C  CD  . LYS   B 64  ? 0.6292 0.6171 0.4162 0.1275  -0.0083 0.0808  73  LYS   B CD  
772  C  CE  . LYS   B 64  ? 0.6654 0.6591 0.4506 0.1469  -0.0138 0.0881  73  LYS   B CE  
773  N  NZ  . LYS   B 64  ? 0.7036 0.6969 0.4745 0.1504  -0.0220 0.0953  73  LYS   B NZ  
774  N  N   . GLN   B 65  ? 0.5341 0.4938 0.3493 0.1137  0.0144  0.0563  74  GLN   B N   
775  C  CA  . GLN   B 65  ? 0.5298 0.4741 0.3432 0.1235  0.0142  0.0542  74  GLN   B CA  
776  C  C   . GLN   B 65  ? 0.5151 0.4697 0.3427 0.1263  0.0207  0.0511  74  GLN   B C   
777  O  O   . GLN   B 65  ? 0.5167 0.4650 0.3427 0.1388  0.0205  0.0509  74  GLN   B O   
778  C  CB  . GLN   B 65  ? 0.5618 0.4875 0.3696 0.1147  0.0134  0.0498  74  GLN   B CB  
779  C  CG  . GLN   B 65  ? 0.6439 0.5557 0.4372 0.1102  0.0077  0.0546  74  GLN   B CG  
780  C  CD  . GLN   B 65  ? 0.7116 0.6064 0.5026 0.1007  0.0071  0.0517  74  GLN   B CD  
781  O  OE1 . GLN   B 65  ? 0.7171 0.6025 0.5123 0.1045  0.0059  0.0468  74  GLN   B OE1 
782  N  NE2 . GLN   B 65  ? 0.7177 0.6102 0.5024 0.0881  0.0078  0.0552  74  GLN   B NE2 
783  N  N   . ASP   B 66  ? 0.5000 0.4682 0.3395 0.1148  0.0261  0.0484  75  ASP   B N   
784  C  CA  . ASP   B 66  ? 0.4912 0.4671 0.3445 0.1147  0.0325  0.0464  75  ASP   B CA  
785  C  C   . ASP   B 66  ? 0.4911 0.4534 0.3441 0.1160  0.0347  0.0406  75  ASP   B C   
786  O  O   . ASP   B 66  ? 0.4885 0.4504 0.3456 0.1251  0.0374  0.0414  75  ASP   B O   
787  C  CB  . ASP   B 66  ? 0.4901 0.4792 0.3498 0.1272  0.0342  0.0539  75  ASP   B CB  
788  C  CG  . ASP   B 66  ? 0.4810 0.4783 0.3556 0.1238  0.0413  0.0542  75  ASP   B CG  
789  O  OD1 . ASP   B 66  ? 0.4987 0.4976 0.3810 0.1099  0.0434  0.0496  75  ASP   B OD1 
790  O  OD2 . ASP   B 66  ? 0.4767 0.4771 0.3537 0.1356  0.0448  0.0591  75  ASP   B OD2 
791  N  N   . LEU   B 67  ? 0.4923 0.4454 0.3409 0.1069  0.0336  0.0352  76  LEU   B N   
792  C  CA  . LEU   B 67  ? 0.4877 0.4314 0.3385 0.1069  0.0348  0.0294  76  LEU   B CA  
793  C  C   . LEU   B 67  ? 0.4838 0.4311 0.3402 0.0936  0.0395  0.0229  76  LEU   B C   
794  O  O   . LEU   B 67  ? 0.4776 0.4304 0.3309 0.0843  0.0404  0.0228  76  LEU   B O   
795  C  CB  . LEU   B 67  ? 0.4971 0.4261 0.3375 0.1109  0.0279  0.0298  76  LEU   B CB  
796  C  CG  . LEU   B 67  ? 0.5242 0.4459 0.3564 0.1271  0.0227  0.0334  76  LEU   B CG  
797  C  CD1 . LEU   B 67  ? 0.5414 0.4442 0.3615 0.1287  0.0143  0.0330  76  LEU   B CD1 
798  C  CD2 . LEU   B 67  ? 0.5322 0.4559 0.3693 0.1383  0.0253  0.0315  76  LEU   B CD2 
799  N  N   . VAL   B 68  ? 0.4800 0.4251 0.3437 0.0942  0.0424  0.0172  77  VAL   B N   
800  C  CA  . VAL   B 68  ? 0.4702 0.4202 0.3399 0.0845  0.0478  0.0102  77  VAL   B CA  
801  C  C   . VAL   B 68  ? 0.4701 0.4177 0.3468 0.0882  0.0478  0.0057  77  VAL   B C   
802  O  O   . VAL   B 68  ? 0.4711 0.4142 0.3497 0.0988  0.0454  0.0066  77  VAL   B O   
803  C  CB  . VAL   B 68  ? 0.4522 0.4081 0.3282 0.0814  0.0533  0.0068  77  VAL   B CB  
804  C  CG1 . VAL   B 68  ? 0.4498 0.4031 0.3334 0.0909  0.0548  0.0087  77  VAL   B CG1 
805  C  CG2 . VAL   B 68  ? 0.4408 0.4006 0.3197 0.0737  0.0587  -0.0018 77  VAL   B CG2 
806  N  N   . SER   B 69  ? 0.4685 0.4207 0.3485 0.0800  0.0501  0.0015  78  SER   B N   
807  C  CA  . SER   B 69  ? 0.4670 0.4220 0.3568 0.0816  0.0497  -0.0030 78  SER   B CA  
808  C  C   . SER   B 69  ? 0.4619 0.4285 0.3610 0.0780  0.0581  -0.0102 78  SER   B C   
809  O  O   . SER   B 69  ? 0.4564 0.4281 0.3513 0.0708  0.0633  -0.0119 78  SER   B O   
810  C  CB  . SER   B 69  ? 0.4689 0.4207 0.3567 0.0750  0.0441  -0.0004 78  SER   B CB  
811  O  OG  . SER   B 69  ? 0.4942 0.4531 0.3799 0.0623  0.0485  0.0011  78  SER   B OG  
812  N  N   . TYR   B 70  ? 0.4584 0.4288 0.3685 0.0849  0.0589  -0.0148 79  TYR   B N   
813  C  CA  . TYR   B 70  ? 0.4538 0.4340 0.3729 0.0856  0.0665  -0.0223 79  TYR   B CA  
814  C  C   . TYR   B 70  ? 0.4546 0.4482 0.3864 0.0844  0.0662  -0.0253 79  TYR   B C   
815  O  O   . TYR   B 70  ? 0.4540 0.4455 0.3901 0.0886  0.0587  -0.0236 79  TYR   B O   
816  C  CB  . TYR   B 70  ? 0.4511 0.4237 0.3734 0.0972  0.0676  -0.0242 79  TYR   B CB  
817  C  CG  . TYR   B 70  ? 0.4570 0.4200 0.3714 0.0957  0.0695  -0.0220 79  TYR   B CG  
818  C  CD1 . TYR   B 70  ? 0.4647 0.4206 0.3719 0.0967  0.0650  -0.0141 79  TYR   B CD1 
819  C  CD2 . TYR   B 70  ? 0.4662 0.4282 0.3810 0.0931  0.0755  -0.0283 79  TYR   B CD2 
820  C  CE1 . TYR   B 70  ? 0.4776 0.4291 0.3811 0.0938  0.0664  -0.0115 79  TYR   B CE1 
821  C  CE2 . TYR   B 70  ? 0.4819 0.4358 0.3912 0.0893  0.0757  -0.0269 79  TYR   B CE2 
822  C  CZ  . TYR   B 70  ? 0.4985 0.4489 0.4037 0.0889  0.0712  -0.0179 79  TYR   B CZ  
823  O  OH  . TYR   B 70  ? 0.5165 0.4627 0.4199 0.0840  0.0711  -0.0161 79  TYR   B OH  
824  N  N   . CYS   B 71  ? 0.4505 0.4596 0.3879 0.0783  0.0739  -0.0297 80  CYS   B N   
825  C  CA  . CYS   B 71  ? 0.4594 0.4880 0.4125 0.0758  0.0757  -0.0322 80  CYS   B CA  
826  C  C   . CYS   B 71  ? 0.4607 0.4944 0.4152 0.0627  0.0721  -0.0257 80  CYS   B C   
827  O  O   . CYS   B 71  ? 0.4682 0.5220 0.4370 0.0568  0.0753  -0.0264 80  CYS   B O   
828  C  CB  . CYS   B 71  ? 0.4909 0.5228 0.4575 0.0879  0.0711  -0.0358 80  CYS   B CB  
829  S  SG  . CYS   B 71  ? 0.6032 0.6248 0.5679 0.1038  0.0749  -0.0413 80  CYS   B SG  
830  N  N   . GLY   B 72  ? 0.4481 0.4645 0.3892 0.0584  0.0653  -0.0189 81  GLY   B N   
831  C  CA  . GLY   B 72  ? 0.4382 0.4538 0.3792 0.0460  0.0609  -0.0121 81  GLY   B CA  
832  C  C   . GLY   B 72  ? 0.4435 0.4368 0.3666 0.0445  0.0537  -0.0053 81  GLY   B C   
833  O  O   . GLY   B 72  ? 0.4304 0.4125 0.3423 0.0527  0.0529  -0.0054 81  GLY   B O   
834  N  N   . PRO   B 73  ? 0.4547 0.4423 0.3754 0.0334  0.0492  0.0016  82  PRO   B N   
835  C  CA  . PRO   B 73  ? 0.4759 0.4406 0.3786 0.0337  0.0418  0.0084  82  PRO   B CA  
836  C  C   . PRO   B 73  ? 0.4952 0.4426 0.3941 0.0464  0.0309  0.0059  82  PRO   B C   
837  O  O   . PRO   B 73  ? 0.4971 0.4480 0.4074 0.0515  0.0264  0.0004  82  PRO   B O   
838  C  CB  . PRO   B 73  ? 0.4818 0.4432 0.3850 0.0184  0.0394  0.0163  82  PRO   B CB  
839  C  CG  . PRO   B 73  ? 0.4693 0.4495 0.3950 0.0119  0.0410  0.0127  82  PRO   B CG  
840  C  CD  . PRO   B 73  ? 0.4355 0.4367 0.3710 0.0204  0.0501  0.0042  82  PRO   B CD  
841  N  N   . TRP   B 74  ? 0.5041 0.4342 0.3861 0.0525  0.0263  0.0103  83  TRP   B N   
842  C  CA  . TRP   B 74  ? 0.5171 0.4312 0.3919 0.0663  0.0170  0.0087  83  TRP   B CA  
843  C  C   . TRP   B 74  ? 0.5358 0.4384 0.4147 0.0641  0.0057  0.0064  83  TRP   B C   
844  O  O   . TRP   B 74  ? 0.5428 0.4373 0.4212 0.0516  0.0019  0.0107  83  TRP   B O   
845  C  CB  . TRP   B 74  ? 0.5148 0.4153 0.3717 0.0719  0.0146  0.0150  83  TRP   B CB  
846  C  CG  . TRP   B 74  ? 0.5097 0.3982 0.3580 0.0887  0.0079  0.0137  83  TRP   B CG  
847  C  CD1 . TRP   B 74  ? 0.5204 0.3889 0.3590 0.0955  -0.0032 0.0132  83  TRP   B CD1 
848  C  CD2 . TRP   B 74  ? 0.5039 0.3999 0.3514 0.1014  0.0122  0.0131  83  TRP   B CD2 
849  N  NE1 . TRP   B 74  ? 0.5300 0.3951 0.3608 0.1132  -0.0054 0.0117  83  TRP   B NE1 
850  C  CE2 . TRP   B 74  ? 0.5174 0.4003 0.3546 0.1165  0.0045  0.0127  83  TRP   B CE2 
851  C  CE3 . TRP   B 74  ? 0.4971 0.4088 0.3519 0.1012  0.0216  0.0127  83  TRP   B CE3 
852  C  CZ2 . TRP   B 74  ? 0.5172 0.4055 0.3517 0.1311  0.0075  0.0137  83  TRP   B CZ2 
853  C  CZ3 . TRP   B 74  ? 0.5042 0.4185 0.3578 0.1139  0.0236  0.0138  83  TRP   B CZ3 
854  C  CH2 . TRP   B 74  ? 0.5115 0.4160 0.3557 0.1286  0.0173  0.0151  83  TRP   B CH2 
855  N  N   . LYS   B 75  ? 0.5408 0.4435 0.4244 0.0751  0.0003  -0.0004 84  LYS   B N   
856  C  CA  . LYS   B 75  ? 0.5510 0.4447 0.4395 0.0733  -0.0120 -0.0048 84  LYS   B CA  
857  C  C   . LYS   B 75  ? 0.5813 0.4500 0.4520 0.0867  -0.0243 -0.0069 84  LYS   B C   
858  O  O   . LYS   B 75  ? 0.5858 0.4420 0.4574 0.0841  -0.0366 -0.0113 84  LYS   B O   
859  C  CB  . LYS   B 75  ? 0.5504 0.4627 0.4558 0.0777  -0.0118 -0.0123 84  LYS   B CB  
860  C  CG  . LYS   B 75  ? 0.5527 0.4913 0.4764 0.0680  0.0002  -0.0122 84  LYS   B CG  
861  C  CD  . LYS   B 75  ? 0.5767 0.5237 0.5154 0.0498  -0.0018 -0.0105 84  LYS   B CD  
862  C  CE  . LYS   B 75  ? 0.5972 0.5715 0.5509 0.0416  0.0122  -0.0095 84  LYS   B CE  
863  N  NZ  . LYS   B 75  ? 0.6273 0.6155 0.5987 0.0237  0.0118  -0.0067 84  LYS   B NZ  
864  N  N   . LEU   B 76  ? 0.6038 0.4672 0.4597 0.1016  -0.0214 -0.0048 85  LEU   B N   
865  C  CA  . LEU   B 76  ? 0.6334 0.4776 0.4713 0.1189  -0.0308 -0.0073 85  LEU   B CA  
866  C  C   . LEU   B 76  ? 0.6799 0.5001 0.5016 0.1180  -0.0374 -0.0031 85  LEU   B C   
867  O  O   . LEU   B 76  ? 0.6897 0.5120 0.5060 0.1170  -0.0304 0.0043  85  LEU   B O   
868  C  CB  . LEU   B 76  ? 0.6253 0.4795 0.4571 0.1358  -0.0229 -0.0055 85  LEU   B CB  
869  C  CG  . LEU   B 76  ? 0.6289 0.5048 0.4754 0.1370  -0.0143 -0.0073 85  LEU   B CG  
870  C  CD1 . LEU   B 76  ? 0.6270 0.5094 0.4671 0.1519  -0.0067 -0.0032 85  LEU   B CD1 
871  C  CD2 . LEU   B 76  ? 0.6384 0.5158 0.4914 0.1405  -0.0225 -0.0152 85  LEU   B CD2 
872  N  N   . ASP   B 77  ? 0.7068 0.5029 0.5202 0.1191  -0.0517 -0.0080 86  ASP   B N   
873  C  CA  . ASP   B 77  ? 0.7507 0.5191 0.5475 0.1190  -0.0590 -0.0040 86  ASP   B CA  
874  C  C   . ASP   B 77  ? 0.7781 0.5193 0.5538 0.1378  -0.0723 -0.0109 86  ASP   B C   
875  O  O   . ASP   B 77  ? 0.8052 0.5198 0.5656 0.1399  -0.0794 -0.0084 86  ASP   B O   
876  C  CB  . ASP   B 77  ? 0.7886 0.5465 0.5941 0.0958  -0.0631 0.0000  86  ASP   B CB  
877  C  CG  . ASP   B 77  ? 0.8846 0.6415 0.7049 0.0846  -0.0727 -0.0077 86  ASP   B CG  
878  O  OD1 . ASP   B 77  ? 0.8998 0.6639 0.7223 0.0959  -0.0773 -0.0171 86  ASP   B OD1 
879  O  OD2 . ASP   B 77  ? 0.9284 0.6792 0.7587 0.0642  -0.0757 -0.0034 86  ASP   B OD2 
880  N  N   . ALA   B 78  ? 0.7707 0.5171 0.5429 0.1532  -0.0757 -0.0194 87  ALA   B N   
881  C  CA  . ALA   B 78  ? 0.7894 0.5112 0.5381 0.1740  -0.0878 -0.0271 87  ALA   B CA  
882  C  C   . ALA   B 78  ? 0.7986 0.5179 0.5300 0.1918  -0.0813 -0.0205 87  ALA   B C   
883  O  O   . ALA   B 78  ? 0.7888 0.5327 0.5286 0.1912  -0.0670 -0.0118 87  ALA   B O   
884  C  CB  . ALA   B 78  ? 0.7850 0.5173 0.5320 0.1881  -0.0911 -0.0362 87  ALA   B CB  
885  N  N   . ALA   B 79  ? 0.8138 0.5040 0.5220 0.2075  -0.0922 -0.0250 88  ALA   B N   
886  C  CA  . ALA   B 79  ? 0.8232 0.5123 0.5158 0.2262  -0.0870 -0.0191 88  ALA   B CA  
887  C  C   . ALA   B 79  ? 0.8417 0.5195 0.5104 0.2552  -0.0932 -0.0275 88  ALA   B C   
888  O  O   . ALA   B 79  ? 0.8492 0.5022 0.5056 0.2601  -0.1077 -0.0394 88  ALA   B O   
889  C  CB  . ALA   B 79  ? 0.8383 0.5014 0.5236 0.2186  -0.0927 -0.0137 88  ALA   B CB  
890  N  N   . TRP   B 80  ? 0.8454 0.5412 0.5067 0.2749  -0.0827 -0.0213 89  TRP   B N   
891  C  CA  . TRP   B 80  ? 0.8704 0.5589 0.5070 0.3055  -0.0860 -0.0272 89  TRP   B CA  
892  C  C   . TRP   B 80  ? 0.9075 0.5530 0.5217 0.3138  -0.1015 -0.0339 89  TRP   B C   
893  O  O   . TRP   B 80  ? 0.8997 0.5333 0.5176 0.3025  -0.1025 -0.0270 89  TRP   B O   
894  C  CB  . TRP   B 80  ? 0.8604 0.5801 0.4985 0.3210  -0.0702 -0.0160 89  TRP   B CB  
895  C  CG  . TRP   B 80  ? 0.8805 0.5983 0.4939 0.3540  -0.0710 -0.0205 89  TRP   B CG  
896  C  CD1 . TRP   B 80  ? 0.9002 0.6123 0.4971 0.3702  -0.0762 -0.0308 89  TRP   B CD1 
897  C  CD2 . TRP   B 80  ? 0.8792 0.6043 0.4813 0.3761  -0.0657 -0.0147 89  TRP   B CD2 
898  N  NE1 . TRP   B 80  ? 0.9081 0.6217 0.4821 0.4015  -0.0741 -0.0322 89  TRP   B NE1 
899  C  CE2 . TRP   B 80  ? 0.8954 0.6195 0.4740 0.4057  -0.0667 -0.0218 89  TRP   B CE2 
900  C  CE3 . TRP   B 80  ? 0.8764 0.6112 0.4861 0.3747  -0.0602 -0.0040 89  TRP   B CE3 
901  C  CZ2 . TRP   B 80  ? 0.9021 0.6346 0.4652 0.4342  -0.0618 -0.0188 89  TRP   B CZ2 
902  C  CZ3 . TRP   B 80  ? 0.8842 0.6281 0.4803 0.4024  -0.0562 -0.0008 89  TRP   B CZ3 
903  C  CH2 . TRP   B 80  ? 0.8944 0.6375 0.4680 0.4320  -0.0565 -0.0081 89  TRP   B CH2 
904  N  N   . ASP   B 81  ? 0.9402 0.5603 0.5307 0.3324  -0.1145 -0.0478 90  ASP   B N   
905  C  CA  . ASP   B 81  ? 0.9789 0.5527 0.5464 0.3409  -0.1309 -0.0558 90  ASP   B CA  
906  C  C   . ASP   B 81  ? 1.0070 0.5767 0.5534 0.3702  -0.1275 -0.0528 90  ASP   B C   
907  O  O   . ASP   B 81  ? 1.0329 0.5620 0.5579 0.3808  -0.1408 -0.0594 90  ASP   B O   
908  C  CB  . ASP   B 81  ? 1.0092 0.5518 0.5595 0.3463  -0.1496 -0.0741 90  ASP   B CB  
909  C  CG  . ASP   B 81  ? 1.0656 0.6195 0.5955 0.3755  -0.1487 -0.0833 90  ASP   B CG  
910  O  OD1 . ASP   B 81  ? 1.0582 0.6468 0.5889 0.3917  -0.1318 -0.0741 90  ASP   B OD1 
911  O  OD2 . ASP   B 81  ? 1.1191 0.6481 0.6322 0.3819  -0.1650 -0.0994 90  ASP   B OD2 
912  N  N   . GLY   B 82  ? 1.0005 0.6115 0.5535 0.3834  -0.1102 -0.0431 91  GLY   B N   
913  C  CA  . GLY   B 82  ? 1.0209 0.6381 0.5584 0.4119  -0.1047 -0.0388 91  GLY   B CA  
914  C  C   . GLY   B 82  ? 1.0499 0.6568 0.5568 0.4468  -0.1094 -0.0510 91  GLY   B C   
915  O  O   . GLY   B 82  ? 1.0596 0.6701 0.5512 0.4739  -0.1057 -0.0491 91  GLY   B O   
916  N  N   . LEU   B 83  ? 1.0643 0.6590 0.5608 0.4479  -0.1181 -0.0641 92  LEU   B N   
917  C  CA  . LEU   B 83  ? 1.0946 0.6770 0.5580 0.4814  -0.1242 -0.0776 92  LEU   B CA  
918  C  C   . LEU   B 83  ? 1.0977 0.7078 0.5606 0.4873  -0.1176 -0.0800 92  LEU   B C   
919  O  O   . LEU   B 83  ? 1.1133 0.7391 0.5562 0.5175  -0.1107 -0.0815 92  LEU   B O   
920  C  CB  . LEU   B 83  ? 1.1307 0.6544 0.5692 0.4840  -0.1487 -0.0964 92  LEU   B CB  
921  C  CG  . LEU   B 83  ? 1.1815 0.6695 0.6038 0.4958  -0.1569 -0.0975 92  LEU   B CG  
922  C  CD1 . LEU   B 83  ? 1.2151 0.6539 0.6399 0.4699  -0.1760 -0.1037 92  LEU   B CD1 
923  C  CD2 . LEU   B 83  ? 1.2026 0.6728 0.5861 0.5378  -0.1623 -0.1105 92  LEU   B CD2 
924  N  N   . SER   B 84  ? 1.0836 0.6990 0.5665 0.4605  -0.1202 -0.0806 93  SER   B N   
925  C  CA  . SER   B 84  ? 1.0727 0.7094 0.5533 0.4660  -0.1169 -0.0837 93  SER   B CA  
926  C  C   . SER   B 84  ? 1.0363 0.7238 0.5383 0.4638  -0.0937 -0.0658 93  SER   B C   
927  O  O   . SER   B 84  ? 1.0244 0.7325 0.5520 0.4475  -0.0814 -0.0513 93  SER   B O   
928  C  CB  . SER   B 84  ? 1.0950 0.7160 0.5880 0.4402  -0.1311 -0.0929 93  SER   B CB  
929  O  OG  . SER   B 84  ? 1.1406 0.7187 0.6307 0.4260  -0.1498 -0.1029 93  SER   B OG  
930  N  N   . GLU   B 85  ? 1.0113 0.7172 0.5017 0.4799  -0.0887 -0.0670 94  GLU   B N   
931  C  CA  . GLU   B 85  ? 0.9805 0.7300 0.4892 0.4771  -0.0686 -0.0507 94  GLU   B CA  
932  C  C   . GLU   B 85  ? 0.9440 0.6997 0.4834 0.4440  -0.0693 -0.0475 94  GLU   B C   
933  O  O   . GLU   B 85  ? 0.9552 0.6857 0.4969 0.4286  -0.0854 -0.0593 94  GLU   B O   
934  C  CB  . GLU   B 85  ? 1.0173 0.7809 0.5004 0.5058  -0.0642 -0.0526 94  GLU   B CB  
935  C  CG  . GLU   B 85  ? 1.0916 0.8667 0.5511 0.5392  -0.0547 -0.0492 94  GLU   B CG  
936  C  CD  . GLU   B 85  ? 1.1716 0.9770 0.6150 0.5641  -0.0406 -0.0414 94  GLU   B CD  
937  O  OE1 . GLU   B 85  ? 1.1809 0.9878 0.6185 0.5630  -0.0439 -0.0443 94  GLU   B OE1 
938  O  OE2 . GLU   B 85  ? 1.1915 1.0209 0.6285 0.5851  -0.0259 -0.0313 94  GLU   B OE2 
939  N  N   . VAL   B 86  ? 0.8965 0.6857 0.4607 0.4324  -0.0516 -0.0313 95  VAL   B N   
940  C  CA  . VAL   B 86  ? 0.8557 0.6538 0.4494 0.4032  -0.0494 -0.0270 95  VAL   B CA  
941  C  C   . VAL   B 86  ? 0.8162 0.6446 0.4179 0.4068  -0.0349 -0.0158 95  VAL   B C   
942  O  O   . VAL   B 86  ? 0.8106 0.6565 0.3994 0.4281  -0.0239 -0.0079 95  VAL   B O   
943  C  CB  . VAL   B 86  ? 0.8372 0.6412 0.4571 0.3798  -0.0428 -0.0178 95  VAL   B CB  
944  C  CG1 . VAL   B 86  ? 0.8563 0.6309 0.4657 0.3796  -0.0551 -0.0254 95  VAL   B CG1 
945  C  CG2 . VAL   B 86  ? 0.8201 0.6575 0.4521 0.3838  -0.0234 -0.0009 95  VAL   B CG2 
946  N  N   . GLN   B 87  ? 0.7937 0.6292 0.4179 0.3856  -0.0336 -0.0135 96  GLN   B N   
947  C  CA  . GLN   B 87  ? 0.7776 0.6379 0.4111 0.3868  -0.0200 -0.0017 96  GLN   B CA  
948  C  C   . GLN   B 87  ? 0.7572 0.6344 0.4231 0.3624  -0.0076 0.0102  96  GLN   B C   
949  O  O   . GLN   B 87  ? 0.7592 0.6284 0.4429 0.3404  -0.0131 0.0054  96  GLN   B O   
950  C  CB  . GLN   B 87  ? 0.7895 0.6440 0.4141 0.3919  -0.0296 -0.0099 96  GLN   B CB  
951  C  CG  . GLN   B 87  ? 0.8356 0.6866 0.4253 0.4228  -0.0335 -0.0146 96  GLN   B CG  
952  C  CD  . GLN   B 87  ? 0.8854 0.7312 0.4627 0.4307  -0.0448 -0.0233 96  GLN   B CD  
953  O  OE1 . GLN   B 87  ? 0.8709 0.7206 0.4679 0.4145  -0.0472 -0.0234 96  GLN   B OE1 
954  N  NE2 . GLN   B 87  ? 0.9161 0.7538 0.4589 0.4578  -0.0524 -0.0316 96  GLN   B NE2 
955  N  N   . LEU   B 88  ? 0.7307 0.6317 0.4041 0.3663  0.0092  0.0258  97  LEU   B N   
956  C  CA  . LEU   B 88  ? 0.7065 0.6224 0.4088 0.3445  0.0203  0.0364  97  LEU   B CA  
957  C  C   . LEU   B 88  ? 0.6949 0.6144 0.4012 0.3435  0.0228  0.0390  97  LEU   B C   
958  O  O   . LEU   B 88  ? 0.6989 0.6260 0.3902 0.3621  0.0279  0.0452  97  LEU   B O   
959  C  CB  . LEU   B 88  ? 0.6952 0.6348 0.4058 0.3475  0.0360  0.0523  97  LEU   B CB  
960  C  CG  . LEU   B 88  ? 0.6925 0.6485 0.4307 0.3277  0.0483  0.0645  97  LEU   B CG  
961  C  CD1 . LEU   B 88  ? 0.6928 0.6397 0.4505 0.3021  0.0430  0.0578  97  LEU   B CD1 
962  C  CD2 . LEU   B 88  ? 0.6860 0.6669 0.4332 0.3306  0.0619  0.0798  97  LEU   B CD2 
963  N  N   . LEU   B 89  ? 0.6736 0.5871 0.3980 0.3239  0.0187  0.0338  98  LEU   B N   
964  C  CA  . LEU   B 89  ? 0.6653 0.5824 0.3961 0.3228  0.0211  0.0366  98  LEU   B CA  
965  C  C   . LEU   B 89  ? 0.6622 0.5934 0.4136 0.3103  0.0367  0.0509  98  LEU   B C   
966  O  O   . LEU   B 89  ? 0.6542 0.5847 0.4265 0.2900  0.0381  0.0493  98  LEU   B O   
967  C  CB  . LEU   B 89  ? 0.6659 0.5719 0.4062 0.3103  0.0088  0.0234  98  LEU   B CB  
968  C  CG  . LEU   B 89  ? 0.6799 0.5899 0.4305 0.3081  0.0099  0.0246  98  LEU   B CG  
969  C  CD1 . LEU   B 89  ? 0.6991 0.6147 0.4341 0.3282  0.0155  0.0341  98  LEU   B CD1 
970  C  CD2 . LEU   B 89  ? 0.6857 0.5877 0.4384 0.3043  -0.0056 0.0098  98  LEU   B CD2 
971  N  N   . ALA   B 90  ? 0.6642 0.6088 0.4093 0.3224  0.0484  0.0650  99  ALA   B N   
972  C  CA  . ALA   B 90  ? 0.6562 0.6146 0.4207 0.3109  0.0629  0.0802  99  ALA   B CA  
973  C  C   . ALA   B 90  ? 0.6553 0.6093 0.4294 0.3049  0.0663  0.0842  99  ALA   B C   
974  O  O   . ALA   B 90  ? 0.6675 0.6186 0.4266 0.3205  0.0649  0.0861  99  ALA   B O   
975  C  CB  . ALA   B 90  ? 0.6504 0.6260 0.4056 0.3265  0.0744  0.0951  99  ALA   B CB  
976  N  N   . VAL   B 91  ? 0.6368 0.5898 0.4341 0.2837  0.0704  0.0855  100 VAL   B N   
977  C  CA  . VAL   B 91  ? 0.6360 0.5828 0.4436 0.2780  0.0743  0.0897  100 VAL   B CA  
978  C  C   . VAL   B 91  ? 0.6419 0.5967 0.4660 0.2661  0.0874  0.1047  100 VAL   B C   
979  O  O   . VAL   B 91  ? 0.6436 0.5973 0.4856 0.2470  0.0884  0.1017  100 VAL   B O   
980  C  CB  . VAL   B 91  ? 0.6285 0.5647 0.4478 0.2647  0.0660  0.0750  100 VAL   B CB  
981  C  CG1 . VAL   B 91  ? 0.6323 0.5611 0.4611 0.2617  0.0700  0.0786  100 VAL   B CG1 
982  C  CG2 . VAL   B 91  ? 0.6309 0.5617 0.4373 0.2736  0.0523  0.0608  100 VAL   B CG2 
983  N  N   . PRO   B 92  ? 0.6451 0.6091 0.4628 0.2770  0.0972  0.1214  101 PRO   B N   
984  C  CA  . PRO   B 92  ? 0.6379 0.6120 0.4736 0.2641  0.1093  0.1370  101 PRO   B CA  
985  C  C   . PRO   B 92  ? 0.6379 0.5985 0.4871 0.2527  0.1141  0.1436  101 PRO   B C   
986  O  O   . PRO   B 92  ? 0.6440 0.5909 0.4840 0.2620  0.1114  0.1420  101 PRO   B O   
987  C  CB  . PRO   B 92  ? 0.6487 0.6410 0.4716 0.2815  0.1185  0.1528  101 PRO   B CB  
988  C  CG  . PRO   B 92  ? 0.6653 0.6518 0.4601 0.3054  0.1114  0.1458  101 PRO   B CG  
989  C  CD  . PRO   B 92  ? 0.6474 0.6147 0.4409 0.3015  0.0978  0.1270  101 PRO   B CD  
990  N  N   . PRO   B 93  ? 0.6326 0.5957 0.5032 0.2331  0.1202  0.1505  102 PRO   B N   
991  C  CA  . PRO   B 93  ? 0.6392 0.5841 0.5216 0.2219  0.1235  0.1552  102 PRO   B CA  
992  C  C   . PRO   B 93  ? 0.6585 0.5969 0.5306 0.2356  0.1308  0.1719  102 PRO   B C   
993  O  O   . PRO   B 93  ? 0.6617 0.6161 0.5276 0.2448  0.1393  0.1880  102 PRO   B O   
994  C  CB  . PRO   B 93  ? 0.6369 0.5892 0.5422 0.1999  0.1286  0.1615  102 PRO   B CB  
995  C  CG  . PRO   B 93  ? 0.6369 0.6078 0.5436 0.1970  0.1237  0.1522  102 PRO   B CG  
996  C  CD  . PRO   B 93  ? 0.6191 0.6002 0.5041 0.2201  0.1225  0.1525  102 PRO   B CD  
997  N  N   . GLY   B 94  ? 0.6662 0.5828 0.5346 0.2394  0.1273  0.1677  103 GLY   B N   
998  C  CA  . GLY   B 94  ? 0.6723 0.5780 0.5292 0.2533  0.1324  0.1825  103 GLY   B CA  
999  C  C   . GLY   B 94  ? 0.6811 0.5970 0.5121 0.2789  0.1311  0.1860  103 GLY   B C   
1000 O  O   . GLY   B 94  ? 0.6824 0.5916 0.5004 0.2927  0.1356  0.1999  103 GLY   B O   
1001 N  N   . GLU   B 95  ? 0.6844 0.6153 0.5058 0.2861  0.1248  0.1741  104 GLU   B N   
1002 C  CA  . GLU   B 95  ? 0.7001 0.6401 0.4950 0.3107  0.1221  0.1749  104 GLU   B CA  
1003 C  C   . GLU   B 95  ? 0.7140 0.6488 0.4989 0.3181  0.1064  0.1521  104 GLU   B C   
1004 O  O   . GLU   B 95  ? 0.7076 0.6396 0.5063 0.3035  0.0997  0.1369  104 GLU   B O   
1005 C  CB  . GLU   B 95  ? 0.7232 0.6867 0.5129 0.3158  0.1299  0.1840  104 GLU   B CB  
1006 C  CG  . GLU   B 95  ? 0.7762 0.7503 0.5811 0.3052  0.1457  0.2072  104 GLU   B CG  
1007 C  CD  . GLU   B 95  ? 0.8389 0.8414 0.6448 0.3083  0.1544  0.2166  104 GLU   B CD  
1008 O  OE1 . GLU   B 95  ? 0.8207 0.8323 0.6190 0.3148  0.1472  0.2025  104 GLU   B OE1 
1009 O  OE2 . GLU   B 95  ? 0.8636 0.8794 0.6785 0.3044  0.1685  0.2388  104 GLU   B OE2 
1010 N  N   . ARG   B 96  ? 0.7336 0.6682 0.4942 0.3404  0.1004  0.1502  105 ARG   B N   
1011 C  CA  . ARG   B 96  ? 0.7610 0.6915 0.5112 0.3488  0.0841  0.1299  105 ARG   B CA  
1012 C  C   . ARG   B 96  ? 0.7744 0.7120 0.5227 0.3454  0.0770  0.1157  105 ARG   B C   
1013 O  O   . ARG   B 96  ? 0.7757 0.7246 0.5198 0.3475  0.0843  0.1230  105 ARG   B O   
1014 C  CB  . ARG   B 96  ? 0.8045 0.7353 0.5262 0.3751  0.0799  0.1337  105 ARG   B CB  
1015 C  CG  . ARG   B 96  ? 0.8751 0.8009 0.5878 0.3839  0.0617  0.1140  105 ARG   B CG  
1016 C  CD  . ARG   B 96  ? 0.9477 0.8693 0.6437 0.4033  0.0580  0.1199  105 ARG   B CD  
1017 N  NE  . ARG   B 96  ? 1.0176 0.9459 0.6844 0.4252  0.0640  0.1337  105 ARG   B NE  
1018 C  CZ  . ARG   B 96  ? 1.0771 1.0049 0.7368 0.4329  0.0773  0.1562  105 ARG   B CZ  
1019 N  NH1 . ARG   B 96  ? 1.0773 0.9947 0.7573 0.4199  0.0850  0.1669  105 ARG   B NH1 
1020 N  NH2 . ARG   B 96  ? 1.0921 1.0287 0.7233 0.4541  0.0830  0.1684  105 ARG   B NH2 
1021 N  N   . ALA   B 97  ? 0.7803 0.7116 0.5323 0.3405  0.0629  0.0961  106 ALA   B N   
1022 C  CA  . ALA   B 97  ? 0.7869 0.7198 0.5352 0.3377  0.0538  0.0818  106 ALA   B CA  
1023 C  C   . ALA   B 97  ? 0.8111 0.7481 0.5301 0.3610  0.0506  0.0823  106 ALA   B C   
1024 O  O   . ALA   B 97  ? 0.8275 0.7636 0.5277 0.3793  0.0477  0.0849  106 ALA   B O   
1025 C  CB  . ALA   B 97  ? 0.7821 0.7074 0.5377 0.3307  0.0391  0.0635  106 ALA   B CB  
1026 N  N   . LYS   B 98  ? 0.8185 0.7599 0.5317 0.3620  0.0509  0.0796  107 LYS   B N   
1027 C  CA  . LYS   B 98  ? 0.8383 0.7838 0.5224 0.3859  0.0496  0.0801  107 LYS   B CA  
1028 C  C   . LYS   B 98  ? 0.8345 0.7751 0.5113 0.3868  0.0406  0.0667  107 LYS   B C   
1029 O  O   . LYS   B 98  ? 0.8305 0.7756 0.5235 0.3727  0.0458  0.0690  107 LYS   B O   
1030 C  CB  . LYS   B 98  ? 0.8809 0.8431 0.5638 0.3927  0.0684  0.1022  107 LYS   B CB  
1031 C  CG  . LYS   B 98  ? 0.9756 0.9485 0.6300 0.4183  0.0727  0.1074  107 LYS   B CG  
1032 C  CD  . LYS   B 98  ? 1.0463 1.0412 0.7093 0.4184  0.0936  0.1312  107 LYS   B CD  
1033 C  CE  . LYS   B 98  ? 1.0934 1.0954 0.7898 0.3925  0.1005  0.1359  107 LYS   B CE  
1034 N  NZ  . LYS   B 98  ? 1.1184 1.1456 0.8227 0.3940  0.1179  0.1559  107 LYS   B NZ  
1035 N  N   . ASN   B 99  ? 0.8350 0.7647 0.4871 0.4029  0.0259  0.0523  108 ASN   B N   
1036 C  CA  . ASN   B 99  ? 0.8369 0.7562 0.4794 0.4051  0.0157  0.0388  108 ASN   B CA  
1037 C  C   . ASN   B 99  ? 0.8460 0.7755 0.4690 0.4253  0.0246  0.0462  108 ASN   B C   
1038 O  O   . ASN   B 99  ? 0.8671 0.8034 0.4660 0.4484  0.0285  0.0515  108 ASN   B O   
1039 C  CB  . ASN   B 99  ? 0.8527 0.7530 0.4781 0.4121  -0.0054 0.0189  108 ASN   B CB  
1040 C  CG  . ASN   B 99  ? 0.8827 0.7757 0.5304 0.3911  -0.0156 0.0098  108 ASN   B CG  
1041 O  OD1 . ASN   B 99  ? 0.9003 0.8012 0.5619 0.3850  -0.0105 0.0165  108 ASN   B OD1 
1042 N  ND2 . ASN   B 99  ? 0.8753 0.7531 0.5267 0.3804  -0.0300 -0.0052 108 ASN   B ND2 
1043 N  N   . ILE   B 100 ? 0.8226 0.7546 0.4550 0.4180  0.0280  0.0469  109 ILE   B N   
1044 C  CA  . ILE   B 100 ? 0.8225 0.7676 0.4405 0.4368  0.0371  0.0541  109 ILE   B CA  
1045 C  C   . ILE   B 100 ? 0.8319 0.7598 0.4381 0.4418  0.0246  0.0391  109 ILE   B C   
1046 O  O   . ILE   B 100 ? 0.8303 0.7544 0.4557 0.4236  0.0231  0.0376  109 ILE   B O   
1047 C  CB  . ILE   B 100 ? 0.8080 0.7786 0.4519 0.4245  0.0559  0.0736  109 ILE   B CB  
1048 C  CG1 . ILE   B 100 ? 0.8115 0.7927 0.4723 0.4131  0.0669  0.0882  109 ILE   B CG1 
1049 C  CG2 . ILE   B 100 ? 0.8069 0.7977 0.4374 0.4462  0.0667  0.0828  109 ILE   B CG2 
1050 C  CD1 . ILE   B 100 ? 0.8341 0.8271 0.4743 0.4353  0.0763  0.1004  109 ILE   B CD1 
1051 N  N   . GLN   B 101 ? 0.8396 0.7550 0.4127 0.4668  0.0150  0.0278  110 GLN   B N   
1052 C  CA  . GLN   B 101 ? 0.8569 0.7499 0.4142 0.4746  0.0013  0.0122  110 GLN   B CA  
1053 C  C   . GLN   B 101 ? 0.8625 0.7704 0.4179 0.4867  0.0123  0.0206  110 GLN   B C   
1054 O  O   . GLN   B 101 ? 0.8655 0.7985 0.4124 0.5053  0.0270  0.0331  110 GLN   B O   
1055 C  CB  . GLN   B 101 ? 0.8909 0.7637 0.4112 0.4986  -0.0139 -0.0041 110 GLN   B CB  
1056 C  CG  . GLN   B 101 ? 0.9365 0.7772 0.4396 0.5042  -0.0321 -0.0231 110 GLN   B CG  
1057 C  CD  . GLN   B 101 ? 1.0111 0.8275 0.4857 0.5174  -0.0517 -0.0420 110 GLN   B CD  
1058 O  OE1 . GLN   B 101 ? 1.0190 0.8363 0.4993 0.5087  -0.0575 -0.0444 110 GLN   B OE1 
1059 N  NE2 . GLN   B 101 ? 1.0511 0.8452 0.4940 0.5398  -0.0632 -0.0565 110 GLN   B NE2 
1060 N  N   . THR   B 102 ? 0.8589 0.7525 0.4219 0.4773  0.0052  0.0143  111 THR   B N   
1061 C  CA  . THR   B 102 ? 0.8525 0.7596 0.4147 0.4895  0.0134  0.0210  111 THR   B CA  
1062 C  C   . THR   B 102 ? 0.8680 0.7436 0.4216 0.4889  -0.0025 0.0068  111 THR   B C   
1063 O  O   . THR   B 102 ? 0.8821 0.7301 0.4400 0.4705  -0.0171 -0.0044 111 THR   B O   
1064 C  CB  . THR   B 102 ? 0.8293 0.7685 0.4275 0.4692  0.0301  0.0401  111 THR   B CB  
1065 O  OG1 . THR   B 102 ? 0.8156 0.7764 0.4137 0.4846  0.0397  0.0487  111 THR   B OG1 
1066 C  CG2 . THR   B 102 ? 0.8243 0.7511 0.4491 0.4363  0.0236  0.0377  111 THR   B CG2 
1067 N  N   . LEU   B 103 ? 0.8654 0.7452 0.4072 0.5092  0.0003  0.0079  112 LEU   B N   
1068 C  CA  . LEU   B 103 ? 0.8774 0.7263 0.4124 0.5081  -0.0138 -0.0030 112 LEU   B CA  
1069 C  C   . LEU   B 103 ? 0.8647 0.7357 0.4299 0.4910  -0.0039 0.0113  112 LEU   B C   
1070 O  O   . LEU   B 103 ? 0.8448 0.7505 0.4174 0.5032  0.0109  0.0244  112 LEU   B O   
1071 C  CB  . LEU   B 103 ? 0.8962 0.7291 0.3960 0.5436  -0.0201 -0.0133 112 LEU   B CB  
1072 C  CG  . LEU   B 103 ? 0.9263 0.7244 0.4201 0.5419  -0.0345 -0.0226 112 LEU   B CG  
1073 C  CD1 . LEU   B 103 ? 0.9497 0.6996 0.4293 0.5315  -0.0565 -0.0411 112 LEU   B CD1 
1074 C  CD2 . LEU   B 103 ? 0.9510 0.7486 0.4205 0.5769  -0.0332 -0.0252 112 LEU   B CD2 
1075 N  N   . PRO   B 104 ? 0.8660 0.7188 0.4483 0.4635  -0.0124 0.0088  113 PRO   B N   
1076 C  CA  . PRO   B 104 ? 0.8530 0.7259 0.4619 0.4470  -0.0046 0.0214  113 PRO   B CA  
1077 C  C   . PRO   B 104 ? 0.8669 0.7398 0.4672 0.4652  -0.0058 0.0231  113 PRO   B C   
1078 O  O   . PRO   B 104 ? 0.8923 0.7351 0.4655 0.4853  -0.0175 0.0115  113 PRO   B O   
1079 C  CB  . PRO   B 104 ? 0.8576 0.7079 0.4814 0.4152  -0.0143 0.0168  113 PRO   B CB  
1080 C  CG  . PRO   B 104 ? 0.8731 0.7015 0.4860 0.4120  -0.0238 0.0047  113 PRO   B CG  
1081 C  CD  . PRO   B 104 ? 0.8715 0.6883 0.4513 0.4451  -0.0287 -0.0044 113 PRO   B CD  
1082 N  N   . GLY   B 105 ? 0.8498 0.7577 0.4741 0.4583  0.0060  0.0377  114 GLY   B N   
1083 C  CA  . GLY   B 105 ? 0.8549 0.7711 0.4800 0.4702  0.0059  0.0425  114 GLY   B CA  
1084 C  C   . GLY   B 105 ? 0.8670 0.7627 0.5031 0.4461  -0.0038 0.0419  114 GLY   B C   
1085 O  O   . GLY   B 105 ? 0.8812 0.7490 0.5175 0.4251  -0.0125 0.0346  114 GLY   B O   
1086 N  N   . ILE   B 106 ? 0.8548 0.7666 0.5005 0.4490  -0.0021 0.0502  115 ILE   B N   
1087 C  CA  . ILE   B 106 ? 0.8652 0.7595 0.5179 0.4301  -0.0110 0.0513  115 ILE   B CA  
1088 C  C   . ILE   B 106 ? 0.8309 0.7667 0.5127 0.4164  -0.0019 0.0655  115 ILE   B C   
1089 O  O   . ILE   B 106 ? 0.8162 0.7881 0.5062 0.4330  0.0067  0.0741  115 ILE   B O   
1090 C  CB  . ILE   B 106 ? 0.9043 0.7666 0.5312 0.4536  -0.0232 0.0454  115 ILE   B CB  
1091 C  CG1 . ILE   B 106 ? 0.9535 0.7678 0.5497 0.4660  -0.0358 0.0294  115 ILE   B CG1 
1092 C  CG2 . ILE   B 106 ? 0.9199 0.7680 0.5528 0.4377  -0.0312 0.0499  115 ILE   B CG2 
1093 C  CD1 . ILE   B 106 ? 0.9874 0.7700 0.5860 0.4371  -0.0449 0.0225  115 ILE   B CD1 
1094 N  N   . PHE   B 107 ? 0.8194 0.7491 0.5154 0.3874  -0.0051 0.0673  116 PHE   B N   
1095 C  CA  . PHE   B 107 ? 0.7925 0.7525 0.5117 0.3725  -0.0012 0.0780  116 PHE   B CA  
1096 C  C   . PHE   B 107 ? 0.8168 0.7487 0.5214 0.3759  -0.0136 0.0768  116 PHE   B C   
1097 O  O   . PHE   B 107 ? 0.8375 0.7319 0.5312 0.3621  -0.0226 0.0705  116 PHE   B O   
1098 C  CB  . PHE   B 107 ? 0.7743 0.7384 0.5126 0.3392  0.0019  0.0787  116 PHE   B CB  
1099 C  CG  . PHE   B 107 ? 0.7490 0.7484 0.5100 0.3297  0.0149  0.0845  116 PHE   B CG  
1100 C  CD1 . PHE   B 107 ? 0.7432 0.7681 0.5062 0.3494  0.0243  0.0894  116 PHE   B CD1 
1101 C  CD2 . PHE   B 107 ? 0.7422 0.7484 0.5217 0.3018  0.0180  0.0856  116 PHE   B CD2 
1102 C  CE1 . PHE   B 107 ? 0.7336 0.7882 0.5173 0.3394  0.0364  0.0966  116 PHE   B CE1 
1103 C  CE2 . PHE   B 107 ? 0.7363 0.7701 0.5358 0.2929  0.0291  0.0911  116 PHE   B CE2 
1104 C  CZ  . PHE   B 107 ? 0.7263 0.7831 0.5281 0.3109  0.0381  0.0972  116 PHE   B CZ  
1105 N  N   . LYS   B 108 ? 0.8131 0.7621 0.5168 0.3953  -0.0145 0.0832  117 LYS   B N   
1106 C  CA  . LYS   B 108 ? 0.8335 0.7563 0.5226 0.4009  -0.0264 0.0838  117 LYS   B CA  
1107 C  C   . LYS   B 108 ? 0.8153 0.7612 0.5246 0.3779  -0.0258 0.0928  117 LYS   B C   
1108 O  O   . LYS   B 108 ? 0.7937 0.7859 0.5253 0.3776  -0.0181 0.1008  117 LYS   B O   
1109 C  CB  . LYS   B 108 ? 0.8731 0.8041 0.5501 0.4369  -0.0280 0.0861  117 LYS   B CB  
1110 C  CG  . LYS   B 108 ? 0.9495 0.8782 0.6118 0.4636  -0.0236 0.0789  117 LYS   B CG  
1111 C  CD  . LYS   B 108 ? 1.0474 0.9716 0.6905 0.5013  -0.0278 0.0781  117 LYS   B CD  
1112 C  CE  . LYS   B 108 ? 1.1132 1.0713 0.7564 0.5285  -0.0159 0.0784  117 LYS   B CE  
1113 N  NZ  . LYS   B 108 ? 1.1754 1.1074 0.7869 0.5675  -0.0223 0.0698  117 LYS   B NZ  
1114 N  N   . THR   B 109 ? 0.8201 0.7359 0.5226 0.3575  -0.0336 0.0915  118 THR   B N   
1115 C  CA  . THR   B 109 ? 0.8116 0.7462 0.5286 0.3361  -0.0341 0.0989  118 THR   B CA  
1116 C  C   . THR   B 109 ? 0.8236 0.7303 0.5222 0.3402  -0.0458 0.1031  118 THR   B C   
1117 O  O   . THR   B 109 ? 0.8397 0.7047 0.5150 0.3535  -0.0538 0.0991  118 THR   B O   
1118 C  CB  . THR   B 109 ? 0.8213 0.7542 0.5501 0.3041  -0.0296 0.0954  118 THR   B CB  
1119 O  OG1 . THR   B 109 ? 0.8491 0.7388 0.5612 0.2919  -0.0370 0.0914  118 THR   B OG1 
1120 C  CG2 . THR   B 109 ? 0.8152 0.7623 0.5562 0.3012  -0.0197 0.0905  118 THR   B CG2 
1121 N  N   . LYS   B 110 ? 0.8154 0.7425 0.5233 0.3278  -0.0476 0.1110  119 LYS   B N   
1122 C  CA  . LYS   B 110 ? 0.8346 0.7360 0.5243 0.3296  -0.0583 0.1169  119 LYS   B CA  
1123 C  C   . LYS   B 110 ? 0.8694 0.7226 0.5423 0.3111  -0.0628 0.1135  119 LYS   B C   
1124 O  O   . LYS   B 110 ? 0.8984 0.7160 0.5505 0.3163  -0.0722 0.1176  119 LYS   B O   
1125 C  CB  . LYS   B 110 ? 0.8287 0.7660 0.5316 0.3195  -0.0593 0.1256  119 LYS   B CB  
1126 C  CG  . LYS   B 110 ? 0.8542 0.8026 0.5697 0.2874  -0.0543 0.1238  119 LYS   B CG  
1127 C  CD  . LYS   B 110 ? 0.8834 0.8726 0.6136 0.2793  -0.0555 0.1299  119 LYS   B CD  
1128 C  CE  . LYS   B 110 ? 0.9297 0.9120 0.6558 0.2530  -0.0566 0.1301  119 LYS   B CE  
1129 N  NZ  . LYS   B 110 ? 0.9520 0.9431 0.6936 0.2306  -0.0472 0.1220  119 LYS   B NZ  
1130 N  N   . ASP   B 111 ? 0.8660 0.7181 0.5487 0.2902  -0.0562 0.1067  120 ASP   B N   
1131 C  CA  . ASP   B 111 ? 0.8932 0.7070 0.5653 0.2716  -0.0592 0.1033  120 ASP   B CA  
1132 C  C   . ASP   B 111 ? 0.9189 0.7015 0.5819 0.2791  -0.0613 0.0933  120 ASP   B C   
1133 O  O   . ASP   B 111 ? 0.9424 0.7002 0.6028 0.2614  -0.0627 0.0893  120 ASP   B O   
1134 C  CB  . ASP   B 111 ? 0.9045 0.7386 0.5935 0.2431  -0.0511 0.1019  120 ASP   B CB  
1135 C  CG  . ASP   B 111 ? 0.9503 0.8107 0.6450 0.2329  -0.0504 0.1098  120 ASP   B CG  
1136 O  OD1 . ASP   B 111 ? 0.9667 0.8142 0.6462 0.2391  -0.0581 0.1181  120 ASP   B OD1 
1137 O  OD2 . ASP   B 111 ? 0.9606 0.8530 0.6737 0.2190  -0.0431 0.1075  120 ASP   B OD2 
1138 N  N   . GLY   B 112 ? 0.9106 0.6970 0.5696 0.3047  -0.0615 0.0891  121 GLY   B N   
1139 C  CA  . GLY   B 112 ? 0.9201 0.6770 0.5674 0.3143  -0.0650 0.0783  121 GLY   B CA  
1140 C  C   . GLY   B 112 ? 0.8928 0.6773 0.5507 0.3249  -0.0562 0.0721  121 GLY   B C   
1141 O  O   . GLY   B 112 ? 0.8692 0.6960 0.5480 0.3186  -0.0459 0.0761  121 GLY   B O   
1142 N  N   . ASP   B 113 ? 0.8970 0.6560 0.5393 0.3410  -0.0608 0.0622  122 ASP   B N   
1143 C  CA  . ASP   B 113 ? 0.8835 0.6639 0.5305 0.3535  -0.0530 0.0562  122 ASP   B CA  
1144 C  C   . ASP   B 113 ? 0.8682 0.6490 0.5266 0.3311  -0.0492 0.0505  122 ASP   B C   
1145 O  O   . ASP   B 113 ? 0.8838 0.6335 0.5373 0.3142  -0.0567 0.0459  122 ASP   B O   
1146 C  CB  . ASP   B 113 ? 0.9241 0.6757 0.5454 0.3829  -0.0607 0.0469  122 ASP   B CB  
1147 C  CG  . ASP   B 113 ? 1.0016 0.7565 0.6108 0.4124  -0.0630 0.0510  122 ASP   B CG  
1148 O  OD1 . ASP   B 113 ? 1.0039 0.7928 0.6282 0.4117  -0.0572 0.0622  122 ASP   B OD1 
1149 O  OD2 . ASP   B 113 ? 1.0589 0.7827 0.6432 0.4371  -0.0713 0.0425  122 ASP   B OD2 
1150 N  N   . ILE   B 114 ? 0.8327 0.6491 0.5065 0.3317  -0.0376 0.0513  123 ILE   B N   
1151 C  CA  . ILE   B 114 ? 0.8147 0.6371 0.5005 0.3143  -0.0326 0.0468  123 ILE   B CA  
1152 C  C   . ILE   B 114 ? 0.7961 0.6312 0.4767 0.3350  -0.0272 0.0429  123 ILE   B C   
1153 O  O   . ILE   B 114 ? 0.7747 0.6370 0.4576 0.3530  -0.0198 0.0490  123 ILE   B O   
1154 C  CB  . ILE   B 114 ? 0.7993 0.6570 0.5116 0.2922  -0.0219 0.0548  123 ILE   B CB  
1155 C  CG1 . ILE   B 114 ? 0.8195 0.6771 0.5363 0.2776  -0.0248 0.0613  123 ILE   B CG1 
1156 C  CG2 . ILE   B 114 ? 0.8004 0.6596 0.5243 0.2733  -0.0177 0.0500  123 ILE   B CG2 
1157 C  CD1 . ILE   B 114 ? 0.8192 0.7165 0.5596 0.2633  -0.0148 0.0688  123 ILE   B CD1 
1158 N  N   . GLY   B 115 ? 0.7975 0.6180 0.4736 0.3312  -0.0297 0.0340  124 GLY   B N   
1159 C  CA  . GLY   B 115 ? 0.7943 0.6280 0.4644 0.3494  -0.0240 0.0311  124 GLY   B CA  
1160 C  C   . GLY   B 115 ? 0.7707 0.6477 0.4638 0.3432  -0.0083 0.0418  124 GLY   B C   
1161 O  O   . GLY   B 115 ? 0.7514 0.6426 0.4655 0.3201  -0.0036 0.0476  124 GLY   B O   
1162 N  N   . ALA   B 116 ? 0.7665 0.6644 0.4551 0.3639  0.0000  0.0450  125 ALA   B N   
1163 C  CA  . ALA   B 116 ? 0.7515 0.6895 0.4621 0.3583  0.0151  0.0569  125 ALA   B CA  
1164 C  C   . ALA   B 116 ? 0.7555 0.7044 0.4573 0.3754  0.0225  0.0574  125 ALA   B C   
1165 O  O   . ALA   B 116 ? 0.7591 0.7044 0.4396 0.4020  0.0212  0.0543  125 ALA   B O   
1166 C  CB  . ALA   B 116 ? 0.7357 0.7037 0.4580 0.3649  0.0214  0.0679  125 ALA   B CB  
1167 N  N   . VAL   B 117 ? 0.7531 0.7143 0.4691 0.3615  0.0302  0.0615  126 VAL   B N   
1168 C  CA  . VAL   B 117 ? 0.7743 0.7461 0.4816 0.3767  0.0378  0.0642  126 VAL   B CA  
1169 C  C   . VAL   B 117 ? 0.7652 0.7787 0.4899 0.3804  0.0547  0.0812  126 VAL   B C   
1170 O  O   . VAL   B 117 ? 0.7550 0.7867 0.5064 0.3589  0.0612  0.0901  126 VAL   B O   
1171 C  CB  . VAL   B 117 ? 0.7957 0.7520 0.5032 0.3644  0.0347  0.0581  126 VAL   B CB  
1172 C  CG1 . VAL   B 117 ? 0.8270 0.7458 0.5144 0.3669  0.0178  0.0414  126 VAL   B CG1 
1173 C  CG2 . VAL   B 117 ? 0.7899 0.7541 0.5253 0.3350  0.0390  0.0631  126 VAL   B CG2 
1174 N  N   . ALA   B 118 ? 0.7599 0.7889 0.4695 0.4076  0.0615  0.0857  127 ALA   B N   
1175 C  CA  . ALA   B 118 ? 0.7560 0.8276 0.4827 0.4121  0.0784  0.1034  127 ALA   B CA  
1176 C  C   . ALA   B 118 ? 0.7688 0.8503 0.4949 0.4134  0.0890  0.1116  127 ALA   B C   
1177 O  O   . ALA   B 118 ? 0.7848 0.8763 0.4915 0.4385  0.0956  0.1150  127 ALA   B O   
1178 C  CB  . ALA   B 118 ? 0.7612 0.8501 0.4742 0.4418  0.0818  0.1059  127 ALA   B CB  
1179 N  N   . LEU   B 119 ? 0.7574 0.8341 0.5023 0.3876  0.0901  0.1142  128 LEU   B N   
1180 C  CA  . LEU   B 119 ? 0.7506 0.8322 0.4968 0.3857  0.0991  0.1226  128 LEU   B CA  
1181 C  C   . LEU   B 119 ? 0.7300 0.8313 0.5106 0.3592  0.1088  0.1365  128 LEU   B C   
1182 O  O   . LEU   B 119 ? 0.7210 0.8172 0.5197 0.3376  0.1032  0.1323  128 LEU   B O   
1183 C  CB  . LEU   B 119 ? 0.7687 0.8152 0.4992 0.3823  0.0871  0.1081  128 LEU   B CB  
1184 C  CG  . LEU   B 119 ? 0.7974 0.8220 0.4931 0.4073  0.0760  0.0936  128 LEU   B CG  
1185 C  CD1 . LEU   B 119 ? 0.8097 0.8030 0.4964 0.3994  0.0625  0.0792  128 LEU   B CD1 
1186 C  CD2 . LEU   B 119 ? 0.8083 0.8502 0.4834 0.4352  0.0861  0.1020  128 LEU   B CD2 
1187 N  N   . ASP   B 120 ? 0.7236 0.8453 0.5118 0.3606  0.1229  0.1529  129 ASP   B N   
1188 C  CA  . ASP   B 120 ? 0.7185 0.8569 0.5392 0.3357  0.1318  0.1666  129 ASP   B CA  
1189 C  C   . ASP   B 120 ? 0.7159 0.8360 0.5410 0.3214  0.1331  0.1685  129 ASP   B C   
1190 O  O   . ASP   B 120 ? 0.7314 0.8516 0.5434 0.3342  0.1401  0.1765  129 ASP   B O   
1191 C  CB  . ASP   B 120 ? 0.7423 0.9210 0.5759 0.3431  0.1482  0.1875  129 ASP   B CB  
1192 C  CG  . ASP   B 120 ? 0.8029 1.0076 0.6626 0.3313  0.1487  0.1917  129 ASP   B CG  
1193 O  OD1 . ASP   B 120 ? 0.8098 1.0167 0.6968 0.3038  0.1481  0.1949  129 ASP   B OD1 
1194 O  OD2 . ASP   B 120 ? 0.8306 1.0523 0.6826 0.3501  0.1485  0.1905  129 ASP   B OD2 
1195 N  N   . TYR   B 121 ? 0.6949 0.8018 0.5392 0.2957  0.1274  0.1627  130 TYR   B N   
1196 C  CA  . TYR   B 121 ? 0.6922 0.7796 0.5428 0.2811  0.1275  0.1627  130 TYR   B CA  
1197 C  C   . TYR   B 121 ? 0.6727 0.7643 0.5537 0.2527  0.1295  0.1669  130 TYR   B C   
1198 O  O   . TYR   B 121 ? 0.6690 0.7718 0.5633 0.2423  0.1257  0.1635  130 TYR   B O   
1199 C  CB  . TYR   B 121 ? 0.7128 0.7689 0.5463 0.2831  0.1140  0.1434  130 TYR   B CB  
1200 C  CG  . TYR   B 121 ? 0.7407 0.7884 0.5449 0.3086  0.1115  0.1399  130 TYR   B CG  
1201 C  CD1 . TYR   B 121 ? 0.7585 0.8020 0.5543 0.3165  0.1172  0.1481  130 TYR   B CD1 
1202 C  CD2 . TYR   B 121 ? 0.7595 0.8031 0.5429 0.3261  0.1033  0.1289  130 TYR   B CD2 
1203 C  CE1 . TYR   B 121 ? 0.7822 0.8197 0.5491 0.3412  0.1143  0.1448  130 TYR   B CE1 
1204 C  CE2 . TYR   B 121 ? 0.7847 0.8201 0.5394 0.3502  0.0997  0.1243  130 TYR   B CE2 
1205 C  CZ  . TYR   B 121 ? 0.8046 0.8382 0.5509 0.3578  0.1052  0.1321  130 TYR   B CZ  
1206 O  OH  . TYR   B 121 ? 0.8455 0.8718 0.5615 0.3823  0.1007  0.1270  130 TYR   B OH  
1207 N  N   . PRO   B 122 ? 0.6600 0.7404 0.5508 0.2404  0.1341  0.1734  131 PRO   B N   
1208 C  CA  . PRO   B 122 ? 0.6373 0.7170 0.5550 0.2135  0.1343  0.1751  131 PRO   B CA  
1209 C  C   . PRO   B 122 ? 0.6158 0.6805 0.5356 0.2005  0.1219  0.1560  131 PRO   B C   
1210 O  O   . PRO   B 122 ? 0.6379 0.6853 0.5396 0.2095  0.1136  0.1421  131 PRO   B O   
1211 C  CB  . PRO   B 122 ? 0.6582 0.7184 0.5777 0.2081  0.1391  0.1817  131 PRO   B CB  
1212 C  CG  . PRO   B 122 ? 0.6761 0.7392 0.5746 0.2320  0.1457  0.1915  131 PRO   B CG  
1213 C  CD  . PRO   B 122 ? 0.6667 0.7326 0.5432 0.2514  0.1382  0.1788  131 PRO   B CD  
1214 N  N   . ALA   B 123 ? 0.5666 0.6385 0.5081 0.1792  0.1202  0.1556  132 ALA   B N   
1215 C  CA  . ALA   B 123 ? 0.5415 0.6013 0.4835 0.1672  0.1094  0.1387  132 ALA   B CA  
1216 C  C   . ALA   B 123 ? 0.5241 0.5535 0.4558 0.1648  0.1041  0.1252  132 ALA   B C   
1217 O  O   . ALA   B 123 ? 0.5107 0.5305 0.4331 0.1648  0.0958  0.1113  132 ALA   B O   
1218 C  CB  . ALA   B 123 ? 0.5278 0.5994 0.4933 0.1449  0.1084  0.1406  132 ALA   B CB  
1219 N  N   . GLY   B 124 ? 0.5223 0.5382 0.4548 0.1652  0.1093  0.1305  133 GLY   B N   
1220 C  CA  . GLY   B 124 ? 0.5273 0.5177 0.4513 0.1661  0.1052  0.1193  133 GLY   B CA  
1221 C  C   . GLY   B 124 ? 0.5305 0.5141 0.4335 0.1845  0.0998  0.1111  133 GLY   B C   
1222 O  O   . GLY   B 124 ? 0.5340 0.5010 0.4317 0.1850  0.0949  0.1003  133 GLY   B O   
1223 N  N   . THR   B 125 ? 0.5369 0.5337 0.4281 0.2001  0.1002  0.1156  134 THR   B N   
1224 C  CA  . THR   B 125 ? 0.5563 0.5455 0.4265 0.2171  0.0929  0.1063  134 THR   B CA  
1225 C  C   . THR   B 125 ? 0.5519 0.5358 0.4199 0.2101  0.0827  0.0915  134 THR   B C   
1226 O  O   . THR   B 125 ? 0.5718 0.5459 0.4250 0.2197  0.0749  0.0820  134 THR   B O   
1227 C  CB  . THR   B 125 ? 0.5818 0.5853 0.4379 0.2381  0.0973  0.1162  134 THR   B CB  
1228 O  OG1 . THR   B 125 ? 0.5900 0.5994 0.4486 0.2428  0.1079  0.1319  134 THR   B OG1 
1229 C  CG2 . THR   B 125 ? 0.6043 0.5973 0.4362 0.2571  0.0888  0.1061  134 THR   B CG2 
1230 N  N   . SER   B 126 ? 0.5274 0.5175 0.4092 0.1932  0.0824  0.0901  135 SER   B N   
1231 C  CA  . SER   B 126 ? 0.5309 0.5170 0.4102 0.1857  0.0740  0.0790  135 SER   B CA  
1232 C  C   . SER   B 126 ? 0.5340 0.5024 0.4072 0.1832  0.0673  0.0660  135 SER   B C   
1233 O  O   . SER   B 126 ? 0.5425 0.5034 0.4228 0.1764  0.0694  0.0630  135 SER   B O   
1234 C  CB  . SER   B 126 ? 0.5319 0.5259 0.4270 0.1667  0.0749  0.0792  135 SER   B CB  
1235 O  OG  . SER   B 126 ? 0.5546 0.5692 0.4596 0.1664  0.0800  0.0911  135 SER   B OG  
1236 N  N   . GLY   B 127 ? 0.5226 0.4846 0.3839 0.1882  0.0593  0.0586  136 GLY   B N   
1237 C  CA  . GLY   B 127 ? 0.5263 0.4747 0.3837 0.1849  0.0525  0.0472  136 GLY   B CA  
1238 C  C   . GLY   B 127 ? 0.5389 0.4791 0.3831 0.2011  0.0474  0.0440  136 GLY   B C   
1239 O  O   . GLY   B 127 ? 0.5405 0.4715 0.3827 0.1988  0.0403  0.0346  136 GLY   B O   
1240 N  N   . SER   B 128 ? 0.5422 0.4874 0.3774 0.2177  0.0508  0.0519  137 SER   B N   
1241 C  CA  . SER   B 128 ? 0.5565 0.4945 0.3755 0.2354  0.0454  0.0487  137 SER   B CA  
1242 C  C   . SER   B 128 ? 0.5716 0.4986 0.3770 0.2401  0.0339  0.0393  137 SER   B C   
1243 O  O   . SER   B 128 ? 0.5742 0.5028 0.3753 0.2413  0.0332  0.0413  137 SER   B O   
1244 C  CB  . SER   B 128 ? 0.5724 0.5204 0.3827 0.2524  0.0530  0.0604  137 SER   B CB  
1245 O  OG  . SER   B 128 ? 0.5931 0.5454 0.4132 0.2496  0.0619  0.0689  137 SER   B OG  
1246 N  N   . PRO   B 129 ? 0.5801 0.4953 0.3801 0.2419  0.0240  0.0290  138 PRO   B N   
1247 C  CA  . PRO   B 129 ? 0.5887 0.4896 0.3770 0.2437  0.0116  0.0197  138 PRO   B CA  
1248 C  C   . PRO   B 129 ? 0.6243 0.5187 0.3895 0.2654  0.0068  0.0190  138 PRO   B C   
1249 O  O   . PRO   B 129 ? 0.6363 0.5363 0.3908 0.2824  0.0101  0.0228  138 PRO   B O   
1250 C  CB  . PRO   B 129 ? 0.5861 0.4798 0.3792 0.2379  0.0028  0.0096  138 PRO   B CB  
1251 C  CG  . PRO   B 129 ? 0.5894 0.4921 0.3852 0.2465  0.0085  0.0135  138 PRO   B CG  
1252 C  CD  . PRO   B 129 ? 0.5663 0.4809 0.3717 0.2422  0.0228  0.0254  138 PRO   B CD  
1253 N  N   . ILE   B 130 ? 0.6334 0.5145 0.3892 0.2657  -0.0015 0.0140  139 ILE   B N   
1254 C  CA  . ILE   B 130 ? 0.6539 0.5236 0.3856 0.2866  -0.0085 0.0103  139 ILE   B CA  
1255 C  C   . ILE   B 130 ? 0.6869 0.5331 0.4100 0.2841  -0.0252 -0.0037 139 ILE   B C   
1256 O  O   . ILE   B 130 ? 0.6836 0.5214 0.4186 0.2649  -0.0303 -0.0073 139 ILE   B O   
1257 C  CB  . ILE   B 130 ? 0.6469 0.5183 0.3750 0.2897  -0.0053 0.0160  139 ILE   B CB  
1258 C  CG1 . ILE   B 130 ? 0.6425 0.5410 0.3835 0.2895  0.0106  0.0300  139 ILE   B CG1 
1259 C  CG2 . ILE   B 130 ? 0.6613 0.5172 0.3626 0.3129  -0.0137 0.0101  139 ILE   B CG2 
1260 C  CD1 . ILE   B 130 ? 0.6530 0.5579 0.4024 0.2811  0.0134  0.0356  139 ILE   B CD1 
1261 N  N   . LEU   B 131 ? 0.7142 0.5512 0.4177 0.3024  -0.0337 -0.0112 140 LEU   B N   
1262 C  CA  . LEU   B 131 ? 0.7511 0.5676 0.4481 0.2997  -0.0511 -0.0253 140 LEU   B CA  
1263 C  C   . LEU   B 131 ? 0.7895 0.5809 0.4591 0.3167  -0.0646 -0.0353 140 LEU   B C   
1264 O  O   . LEU   B 131 ? 0.8009 0.5945 0.4504 0.3394  -0.0605 -0.0329 140 LEU   B O   
1265 C  CB  . LEU   B 131 ? 0.7536 0.5791 0.4507 0.3061  -0.0536 -0.0289 140 LEU   B CB  
1266 C  CG  . LEU   B 131 ? 0.7608 0.6107 0.4749 0.3021  -0.0384 -0.0176 140 LEU   B CG  
1267 C  CD1 . LEU   B 131 ? 0.7639 0.6191 0.4697 0.3159  -0.0421 -0.0204 140 LEU   B CD1 
1268 C  CD2 . LEU   B 131 ? 0.7560 0.6131 0.4984 0.2762  -0.0336 -0.0152 140 LEU   B CD2 
1269 N  N   . ASP   B 132 ? 0.8086 0.5762 0.4770 0.3063  -0.0812 -0.0469 141 ASP   B N   
1270 C  CA  . ASP   B 132 ? 0.8424 0.5801 0.4837 0.3216  -0.0972 -0.0591 141 ASP   B CA  
1271 C  C   . ASP   B 132 ? 0.8759 0.6091 0.5027 0.3347  -0.1100 -0.0716 141 ASP   B C   
1272 O  O   . ASP   B 132 ? 0.8652 0.6188 0.5053 0.3301  -0.1061 -0.0693 141 ASP   B O   
1273 C  CB  . ASP   B 132 ? 0.8576 0.5675 0.5036 0.3033  -0.1093 -0.0642 141 ASP   B CB  
1274 C  CG  . ASP   B 132 ? 0.9024 0.6101 0.5709 0.2772  -0.1184 -0.0691 141 ASP   B CG  
1275 O  OD1 . ASP   B 132 ? 0.9067 0.6269 0.5813 0.2775  -0.1223 -0.0744 141 ASP   B OD1 
1276 O  OD2 . ASP   B 132 ? 0.9308 0.6258 0.6110 0.2569  -0.1214 -0.0668 141 ASP   B OD2 
1277 N  N   . LYS   B 133 ? 0.9121 0.6178 0.5106 0.3515  -0.1260 -0.0851 142 LYS   B N   
1278 C  CA  . LYS   B 133 ? 0.9416 0.6411 0.5224 0.3655  -0.1404 -0.0986 142 LYS   B CA  
1279 C  C   . LYS   B 133 ? 0.9374 0.6419 0.5419 0.3433  -0.1512 -0.1046 142 LYS   B C   
1280 O  O   . LYS   B 133 ? 0.9374 0.6503 0.5349 0.3533  -0.1584 -0.1113 142 LYS   B O   
1281 C  CB  . LYS   B 133 ? 1.0033 0.6666 0.5491 0.3850  -0.1582 -0.1146 142 LYS   B CB  
1282 C  CG  . LYS   B 133 ? 1.0852 0.7535 0.5988 0.4198  -0.1491 -0.1124 142 LYS   B CG  
1283 C  CD  . LYS   B 133 ? 1.1673 0.8133 0.6645 0.4309  -0.1487 -0.1129 142 LYS   B CD  
1284 C  CE  . LYS   B 133 ? 1.2356 0.8898 0.7006 0.4676  -0.1401 -0.1120 142 LYS   B CE  
1285 N  NZ  . LYS   B 133 ? 1.2918 0.9113 0.7275 0.4870  -0.1507 -0.1232 142 LYS   B NZ  
1286 N  N   . CYS   B 134 ? 0.9294 0.6326 0.5625 0.3141  -0.1514 -0.1012 143 CYS   B N   
1287 C  CA  . CYS   B 134 ? 0.9254 0.6389 0.5850 0.2926  -0.1598 -0.1056 143 CYS   B CA  
1288 C  C   . CYS   B 134 ? 0.8895 0.6389 0.5764 0.2826  -0.1424 -0.0932 143 CYS   B C   
1289 O  O   . CYS   B 134 ? 0.8882 0.6499 0.6000 0.2648  -0.1470 -0.0955 143 CYS   B O   
1290 C  CB  . CYS   B 134 ? 0.9588 0.6516 0.6341 0.2664  -0.1709 -0.1094 143 CYS   B CB  
1291 S  SG  . CYS   B 134 ? 1.0913 0.7343 0.7354 0.2756  -0.1934 -0.1246 143 CYS   B SG  
1292 N  N   . GLY   B 135 ? 0.8628 0.6285 0.5467 0.2931  -0.1230 -0.0803 144 GLY   B N   
1293 C  CA  . GLY   B 135 ? 0.8320 0.6270 0.5400 0.2839  -0.1065 -0.0687 144 GLY   B CA  
1294 C  C   . GLY   B 135 ? 0.7996 0.6011 0.5335 0.2590  -0.0963 -0.0605 144 GLY   B C   
1295 O  O   . GLY   B 135 ? 0.7850 0.6084 0.5396 0.2498  -0.0839 -0.0529 144 GLY   B O   
1296 N  N   . ARG   B 136 ? 0.7886 0.5696 0.5198 0.2488  -0.1018 -0.0622 145 ARG   B N   
1297 C  CA  . ARG   B 136 ? 0.7688 0.5540 0.5203 0.2259  -0.0931 -0.0542 145 ARG   B CA  
1298 C  C   . ARG   B 136 ? 0.7443 0.5401 0.4936 0.2310  -0.0755 -0.0417 145 ARG   B C   
1299 O  O   . ARG   B 136 ? 0.7594 0.5478 0.4877 0.2499  -0.0741 -0.0401 145 ARG   B O   
1300 C  CB  . ARG   B 136 ? 0.8014 0.5583 0.5482 0.2145  -0.1062 -0.0592 145 ARG   B CB  
1301 C  CG  . ARG   B 136 ? 0.8456 0.5973 0.6069 0.1980  -0.1214 -0.0685 145 ARG   B CG  
1302 C  CD  . ARG   B 136 ? 0.9147 0.6347 0.6703 0.1861  -0.1341 -0.0717 145 ARG   B CD  
1303 N  NE  . ARG   B 136 ? 1.0084 0.6979 0.7334 0.2064  -0.1486 -0.0821 145 ARG   B NE  
1304 C  CZ  . ARG   B 136 ? 1.0748 0.7319 0.7816 0.2095  -0.1551 -0.0827 145 ARG   B CZ  
1305 N  NH1 . ARG   B 136 ? 1.0705 0.7220 0.7864 0.1931  -0.1481 -0.0722 145 ARG   B NH1 
1306 N  NH2 . ARG   B 136 ? 1.1046 0.7342 0.7820 0.2307  -0.1686 -0.0940 145 ARG   B NH2 
1307 N  N   . VAL   B 137 ? 0.7080 0.5219 0.4786 0.2146  -0.0627 -0.0334 146 VAL   B N   
1308 C  CA  . VAL   B 137 ? 0.6879 0.5133 0.4589 0.2172  -0.0475 -0.0223 146 VAL   B CA  
1309 C  C   . VAL   B 137 ? 0.6916 0.5021 0.4549 0.2127  -0.0488 -0.0187 146 VAL   B C   
1310 O  O   . VAL   B 137 ? 0.6878 0.4939 0.4617 0.1937  -0.0500 -0.0175 146 VAL   B O   
1311 C  CB  . VAL   B 137 ? 0.6724 0.5211 0.4659 0.2041  -0.0340 -0.0161 146 VAL   B CB  
1312 C  CG1 . VAL   B 137 ? 0.6675 0.5275 0.4613 0.2065  -0.0203 -0.0055 146 VAL   B CG1 
1313 C  CG2 . VAL   B 137 ? 0.6720 0.5329 0.4716 0.2110  -0.0336 -0.0192 146 VAL   B CG2 
1314 N  N   . ILE   B 138 ? 0.6922 0.4953 0.4359 0.2316  -0.0488 -0.0168 147 ILE   B N   
1315 C  CA  . ILE   B 138 ? 0.6897 0.4792 0.4243 0.2317  -0.0502 -0.0128 147 ILE   B CA  
1316 C  C   . ILE   B 138 ? 0.6584 0.4690 0.4035 0.2266  -0.0357 -0.0009 147 ILE   B C   
1317 O  O   . ILE   B 138 ? 0.6612 0.4643 0.4007 0.2260  -0.0364 0.0037  147 ILE   B O   
1318 C  CB  . ILE   B 138 ? 0.7144 0.4840 0.4221 0.2558  -0.0590 -0.0179 147 ILE   B CB  
1319 C  CG1 . ILE   B 138 ? 0.7237 0.5135 0.4235 0.2778  -0.0488 -0.0132 147 ILE   B CG1 
1320 C  CG2 . ILE   B 138 ? 0.7371 0.4813 0.4335 0.2582  -0.0764 -0.0316 147 ILE   B CG2 
1321 C  CD1 . ILE   B 138 ? 0.7548 0.5297 0.4271 0.3043  -0.0548 -0.0176 147 ILE   B CD1 
1322 N  N   . GLY   B 139 ? 0.6247 0.4598 0.3846 0.2227  -0.0240 0.0039  148 GLY   B N   
1323 C  CA  . GLY   B 139 ? 0.6102 0.4648 0.3815 0.2158  -0.0119 0.0138  148 GLY   B CA  
1324 C  C   . GLY   B 139 ? 0.5954 0.4724 0.3773 0.2189  -0.0003 0.0189  148 GLY   B C   
1325 O  O   . GLY   B 139 ? 0.5995 0.4772 0.3784 0.2282  -0.0009 0.0158  148 GLY   B O   
1326 N  N   . LEU   B 140 ? 0.5814 0.4756 0.3753 0.2109  0.0095  0.0269  149 LEU   B N   
1327 C  CA  . LEU   B 140 ? 0.5724 0.4855 0.3779 0.2112  0.0206  0.0331  149 LEU   B CA  
1328 C  C   . LEU   B 140 ? 0.5712 0.5005 0.3760 0.2216  0.0276  0.0432  149 LEU   B C   
1329 O  O   . LEU   B 140 ? 0.5692 0.5005 0.3708 0.2226  0.0258  0.0462  149 LEU   B O   
1330 C  CB  . LEU   B 140 ? 0.5622 0.4830 0.3859 0.1908  0.0261  0.0329  149 LEU   B CB  
1331 C  CG  . LEU   B 140 ? 0.5658 0.4776 0.3948 0.1790  0.0217  0.0242  149 LEU   B CG  
1332 C  CD1 . LEU   B 140 ? 0.5638 0.4855 0.4087 0.1624  0.0291  0.0241  149 LEU   B CD1 
1333 C  CD2 . LEU   B 140 ? 0.5677 0.4741 0.3931 0.1891  0.0177  0.0191  149 LEU   B CD2 
1334 N  N   . TYR   B 141 ? 0.5677 0.5094 0.3761 0.2295  0.0358  0.0494  150 TYR   B N   
1335 C  CA  . TYR   B 141 ? 0.5711 0.5325 0.3816 0.2396  0.0442  0.0607  150 TYR   B CA  
1336 C  C   . TYR   B 141 ? 0.5545 0.5328 0.3869 0.2228  0.0530  0.0683  150 TYR   B C   
1337 O  O   . TYR   B 141 ? 0.5519 0.5260 0.3938 0.2114  0.0554  0.0661  150 TYR   B O   
1338 C  CB  . TYR   B 141 ? 0.5833 0.5465 0.3821 0.2591  0.0477  0.0637  150 TYR   B CB  
1339 C  CG  . TYR   B 141 ? 0.5929 0.5800 0.3971 0.2680  0.0597  0.0779  150 TYR   B CG  
1340 C  CD1 . TYR   B 141 ? 0.5977 0.5958 0.4180 0.2584  0.0695  0.0870  150 TYR   B CD1 
1341 C  CD2 . TYR   B 141 ? 0.6099 0.6083 0.4030 0.2868  0.0615  0.0827  150 TYR   B CD2 
1342 C  CE1 . TYR   B 141 ? 0.6083 0.6294 0.4360 0.2642  0.0810  0.1019  150 TYR   B CE1 
1343 C  CE2 . TYR   B 141 ? 0.6132 0.6380 0.4134 0.2948  0.0738  0.0972  150 TYR   B CE2 
1344 C  CZ  . TYR   B 141 ? 0.6203 0.6569 0.4387 0.2822  0.0836  0.1074  150 TYR   B CZ  
1345 O  OH  . TYR   B 141 ? 0.6289 0.6924 0.4562 0.2881  0.0963  0.1235  150 TYR   B OH  
1346 N  N   . GLY   B 142 ? 0.5445 0.5416 0.3851 0.2218  0.0570  0.0765  151 GLY   B N   
1347 C  CA  . GLY   B 142 ? 0.5419 0.5545 0.4039 0.2047  0.0635  0.0829  151 GLY   B CA  
1348 C  C   . GLY   B 142 ? 0.5396 0.5645 0.4101 0.1948  0.0608  0.0844  151 GLY   B C   
1349 O  O   . GLY   B 142 ? 0.5287 0.5670 0.4169 0.1799  0.0645  0.0886  151 GLY   B O   
1350 N  N   . ASN   B 143 ? 0.5410 0.5605 0.3985 0.2032  0.0534  0.0810  152 ASN   B N   
1351 C  CA  . ASN   B 143 ? 0.5414 0.5740 0.4050 0.1970  0.0501  0.0837  152 ASN   B CA  
1352 C  C   . ASN   B 143 ? 0.5612 0.6037 0.4155 0.2177  0.0484  0.0889  152 ASN   B C   
1353 O  O   . ASN   B 143 ? 0.5694 0.5926 0.4043 0.2306  0.0417  0.0834  152 ASN   B O   
1354 C  CB  . ASN   B 143 ? 0.5469 0.5629 0.4049 0.1836  0.0421  0.0753  152 ASN   B CB  
1355 C  CG  . ASN   B 143 ? 0.5573 0.5899 0.4240 0.1740  0.0394  0.0788  152 ASN   B CG  
1356 O  OD1 . ASN   B 143 ? 0.5383 0.5957 0.4209 0.1712  0.0436  0.0861  152 ASN   B OD1 
1357 N  ND2 . ASN   B 143 ? 0.5757 0.5957 0.4324 0.1681  0.0321  0.0742  152 ASN   B ND2 
1358 N  N   . GLY   B 144 ? 0.5614 0.6341 0.4303 0.2208  0.0543  0.0993  153 GLY   B N   
1359 C  CA  . GLY   B 144 ? 0.5867 0.6743 0.4490 0.2424  0.0543  0.1050  153 GLY   B CA  
1360 C  C   . GLY   B 144 ? 0.6002 0.7269 0.4842 0.2414  0.0596  0.1167  153 GLY   B C   
1361 O  O   . GLY   B 144 ? 0.5918 0.7313 0.4929 0.2228  0.0573  0.1181  153 GLY   B O   
1362 N  N   . VAL   B 145 ? 0.6202 0.7675 0.5031 0.2624  0.0663  0.1248  154 VAL   B N   
1363 C  CA  . VAL   B 145 ? 0.6248 0.8142 0.5292 0.2650  0.0714  0.1369  154 VAL   B CA  
1364 C  C   . VAL   B 145 ? 0.6407 0.8581 0.5545 0.2767  0.0855  0.1495  154 VAL   B C   
1365 O  O   . VAL   B 145 ? 0.6493 0.8515 0.5460 0.2898  0.0901  0.1480  154 VAL   B O   
1366 C  CB  . VAL   B 145 ? 0.6292 0.8208 0.5216 0.2829  0.0631  0.1349  154 VAL   B CB  
1367 C  CG1 . VAL   B 145 ? 0.6323 0.8279 0.5069 0.3153  0.0672  0.1370  154 VAL   B CG1 
1368 C  CG2 . VAL   B 145 ? 0.6215 0.8479 0.5378 0.2735  0.0606  0.1421  154 VAL   B CG2 
1369 N  N   . VAL   B 146 ? 0.6454 0.9053 0.5870 0.2715  0.0919  0.1625  155 VAL   B N   
1370 C  CA  . VAL   B 146 ? 0.6632 0.9564 0.6175 0.2813  0.1066  0.1775  155 VAL   B CA  
1371 C  C   . VAL   B 146 ? 0.6858 1.0115 0.6397 0.3070  0.1088  0.1837  155 VAL   B C   
1372 O  O   . VAL   B 146 ? 0.6763 1.0243 0.6461 0.3027  0.1029  0.1855  155 VAL   B O   
1373 C  CB  . VAL   B 146 ? 0.6576 0.9761 0.6468 0.2543  0.1132  0.1890  155 VAL   B CB  
1374 C  CG1 . VAL   B 146 ? 0.6544 1.0090 0.6576 0.2639  0.1296  0.2072  155 VAL   B CG1 
1375 C  CG2 . VAL   B 146 ? 0.6765 0.9592 0.6635 0.2317  0.1104  0.1814  155 VAL   B CG2 
1376 N  N   . ILE   B 147 ? 0.7196 1.0467 0.6529 0.3358  0.1162  0.1857  156 ILE   B N   
1377 C  CA  . ILE   B 147 ? 0.7498 1.1054 0.6787 0.3648  0.1185  0.1900  156 ILE   B CA  
1378 C  C   . ILE   B 147 ? 0.7570 1.1723 0.7167 0.3677  0.1341  0.2100  156 ILE   B C   
1379 O  O   . ILE   B 147 ? 0.7525 1.1815 0.7339 0.3469  0.1431  0.2207  156 ILE   B O   
1380 C  CB  . ILE   B 147 ? 0.7843 1.1093 0.6723 0.3969  0.1167  0.1795  156 ILE   B CB  
1381 C  CG1 . ILE   B 147 ? 0.8046 1.1275 0.6811 0.4050  0.1292  0.1846  156 ILE   B CG1 
1382 C  CG2 . ILE   B 147 ? 0.8146 1.0852 0.6774 0.3922  0.0998  0.1610  156 ILE   B CG2 
1383 C  CD1 . ILE   B 147 ? 0.8433 1.1381 0.6786 0.4371  0.1266  0.1734  156 ILE   B CD1 
1384 N  N   . LYS   B 148 ? 0.7645 1.2161 0.7275 0.3930  0.1373  0.2158  157 LYS   B N   
1385 C  CA  . LYS   B 148 ? 0.7582 1.2731 0.7521 0.3984  0.1527  0.2356  157 LYS   B CA  
1386 C  C   . LYS   B 148 ? 0.7688 1.2960 0.7667 0.3959  0.1703  0.2490  157 LYS   B C   
1387 O  O   . LYS   B 148 ? 0.7520 1.3205 0.7858 0.3781  0.1811  0.2665  157 LYS   B O   
1388 C  CB  . LYS   B 148 ? 0.7850 1.3274 0.7679 0.4371  0.1556  0.2369  157 LYS   B CB  
1389 C  CG  . LYS   B 148 ? 0.8431 1.3921 0.8332 0.4401  0.1412  0.2309  157 LYS   B CG  
1390 C  CD  . LYS   B 148 ? 0.8983 1.4820 0.8829 0.4791  0.1456  0.2347  157 LYS   B CD  
1391 C  CE  . LYS   B 148 ? 0.9033 1.5630 0.9311 0.4784  0.1597  0.2555  157 LYS   B CE  
1392 N  NZ  . LYS   B 148 ? 0.9099 1.6053 0.9463 0.5031  0.1549  0.2569  157 LYS   B NZ  
1393 N  N   . ASN   B 149 ? 0.7935 1.2838 0.7543 0.4131  0.1722  0.2409  158 ASN   B N   
1394 C  CA  . ASN   B 149 ? 0.8001 1.2924 0.7532 0.4168  0.1873  0.2513  158 ASN   B CA  
1395 C  C   . ASN   B 149 ? 0.7850 1.2663 0.7593 0.3804  0.1899  0.2586  158 ASN   B C   
1396 O  O   . ASN   B 149 ? 0.7872 1.2746 0.7599 0.3809  0.2035  0.2711  158 ASN   B O   
1397 C  CB  . ASN   B 149 ? 0.8612 1.3057 0.7656 0.4411  0.1822  0.2353  158 ASN   B CB  
1398 C  CG  . ASN   B 149 ? 0.9316 1.3713 0.8066 0.4779  0.1767  0.2239  158 ASN   B CG  
1399 O  OD1 . ASN   B 149 ? 0.9399 1.4073 0.8279 0.4876  0.1746  0.2256  158 ASN   B OD1 
1400 N  ND2 . ASN   B 149 ? 0.9666 1.3692 0.8002 0.5001  0.1733  0.2113  158 ASN   B ND2 
1401 N  N   . GLY   B 150 ? 0.7680 1.2289 0.7574 0.3515  0.1765  0.2498  159 GLY   B N   
1402 C  CA  . GLY   B 150 ? 0.7518 1.1939 0.7573 0.3184  0.1762  0.2525  159 GLY   B CA  
1403 C  C   . GLY   B 150 ? 0.7557 1.1407 0.7295 0.3175  0.1683  0.2368  159 GLY   B C   
1404 O  O   . GLY   B 150 ? 0.7620 1.1226 0.7446 0.2914  0.1641  0.2337  159 GLY   B O   
1405 N  N   . SER   B 151 ? 0.7448 1.1082 0.6813 0.3469  0.1655  0.2261  160 SER   B N   
1406 C  CA  A SER   B 151 ? 0.7597 1.0722 0.6645 0.3503  0.1568  0.2103  160 SER   B CA  
1407 C  CA  B SER   B 151 ? 0.7599 1.0726 0.6658 0.3491  0.1570  0.2107  160 SER   B CA  
1408 C  C   . SER   B 151 ? 0.7546 1.0321 0.6572 0.3327  0.1392  0.1924  160 SER   B C   
1409 O  O   . SER   B 151 ? 0.7464 1.0373 0.6657 0.3234  0.1329  0.1909  160 SER   B O   
1410 C  CB  A SER   B 151 ? 0.7908 1.0942 0.6585 0.3867  0.1573  0.2036  160 SER   B CB  
1411 C  CB  B SER   B 151 ? 0.7933 1.0962 0.6618 0.3847  0.1586  0.2050  160 SER   B CB  
1412 O  OG  A SER   B 151 ? 0.8422 1.0980 0.6803 0.3901  0.1465  0.1870  160 SER   B OG  
1413 O  OG  B SER   B 151 ? 0.8206 1.1389 0.6810 0.4076  0.1555  0.2010  160 SER   B OG  
1414 N  N   . TYR   B 152 ? 0.7389 0.9737 0.6209 0.3289  0.1314  0.1793  161 TYR   B N   
1415 C  CA  . TYR   B 152 ? 0.7237 0.9247 0.6015 0.3130  0.1166  0.1632  161 TYR   B CA  
1416 C  C   . TYR   B 152 ? 0.7129 0.8808 0.5577 0.3318  0.1050  0.1468  161 TYR   B C   
1417 O  O   . TYR   B 152 ? 0.7287 0.8832 0.5500 0.3504  0.1064  0.1435  161 TYR   B O   
1418 C  CB  . TYR   B 152 ? 0.7258 0.9056 0.6108 0.2906  0.1170  0.1616  161 TYR   B CB  
1419 C  CG  . TYR   B 152 ? 0.7380 0.8890 0.6229 0.2717  0.1041  0.1469  161 TYR   B CG  
1420 C  CD1 . TYR   B 152 ? 0.7327 0.8944 0.6365 0.2541  0.0991  0.1461  161 TYR   B CD1 
1421 C  CD2 . TYR   B 152 ? 0.7643 0.8796 0.6300 0.2720  0.0968  0.1339  161 TYR   B CD2 
1422 C  CE1 . TYR   B 152 ? 0.7504 0.8873 0.6515 0.2383  0.0883  0.1333  161 TYR   B CE1 
1423 C  CE2 . TYR   B 152 ? 0.7809 0.8733 0.6470 0.2553  0.0863  0.1215  161 TYR   B CE2 
1424 C  CZ  . TYR   B 152 ? 0.7793 0.8823 0.6620 0.2390  0.0827  0.1214  161 TYR   B CZ  
1425 O  OH  . TYR   B 152 ? 0.8026 0.8850 0.6843 0.2230  0.0738  0.1103  161 TYR   B OH  
1426 N  N   . VAL   B 153 ? 0.6849 0.8383 0.5274 0.3262  0.0928  0.1366  162 VAL   B N   
1427 C  CA  . VAL   B 153 ? 0.6758 0.7939 0.4896 0.3393  0.0802  0.1214  162 VAL   B CA  
1428 C  C   . VAL   B 153 ? 0.6502 0.7408 0.4676 0.3151  0.0690  0.1110  162 VAL   B C   
1429 O  O   . VAL   B 153 ? 0.6325 0.7333 0.4658 0.3003  0.0662  0.1130  162 VAL   B O   
1430 C  CB  . VAL   B 153 ? 0.6778 0.8041 0.4779 0.3654  0.0771  0.1207  162 VAL   B CB  
1431 C  CG1 . VAL   B 153 ? 0.6997 0.7836 0.4721 0.3743  0.0621  0.1048  162 VAL   B CG1 
1432 C  CG2 . VAL   B 153 ? 0.6847 0.8354 0.4759 0.3925  0.0888  0.1290  162 VAL   B CG2 
1433 N  N   . SER   B 154 ? 0.6459 0.7051 0.4497 0.3108  0.0633  0.1006  163 SER   B N   
1434 C  CA  . SER   B 154 ? 0.6309 0.6668 0.4385 0.2883  0.0548  0.0916  163 SER   B CA  
1435 C  C   . SER   B 154 ? 0.6347 0.6400 0.4217 0.2942  0.0417  0.0800  163 SER   B C   
1436 O  O   . SER   B 154 ? 0.6556 0.6444 0.4212 0.3133  0.0373  0.0740  163 SER   B O   
1437 C  CB  . SER   B 154 ? 0.6316 0.6552 0.4413 0.2781  0.0572  0.0883  163 SER   B CB  
1438 O  OG  . SER   B 154 ? 0.6326 0.6316 0.4411 0.2617  0.0487  0.0776  163 SER   B OG  
1439 N  N   . ALA   B 155 ? 0.6150 0.6093 0.4074 0.2763  0.0350  0.0762  164 ALA   B N   
1440 C  CA  . ALA   B 155 ? 0.6216 0.5840 0.3964 0.2775  0.0227  0.0667  164 ALA   B CA  
1441 C  C   . ALA   B 155 ? 0.6281 0.5659 0.3953 0.2718  0.0183  0.0568  164 ALA   B C   
1442 O  O   . ALA   B 155 ? 0.6154 0.5612 0.3939 0.2624  0.0246  0.0575  164 ALA   B O   
1443 C  CB  . ALA   B 155 ? 0.6195 0.5804 0.4031 0.2582  0.0187  0.0676  164 ALA   B CB  
1444 N  N   . ILE   B 156 ? 0.6385 0.5460 0.3873 0.2773  0.0068  0.0478  165 ILE   B N   
1445 C  CA  . ILE   B 156 ? 0.6449 0.5309 0.3901 0.2684  0.0006  0.0382  165 ILE   B CA  
1446 C  C   . ILE   B 156 ? 0.6297 0.5084 0.3854 0.2441  -0.0024 0.0378  165 ILE   B C   
1447 O  O   . ILE   B 156 ? 0.6360 0.4936 0.3815 0.2424  -0.0114 0.0353  165 ILE   B O   
1448 C  CB  . ILE   B 156 ? 0.6694 0.5261 0.3905 0.2849  -0.0114 0.0283  165 ILE   B CB  
1449 C  CG1 . ILE   B 156 ? 0.6820 0.5480 0.3888 0.3123  -0.0076 0.0289  165 ILE   B CG1 
1450 C  CG2 . ILE   B 156 ? 0.6778 0.5168 0.4004 0.2721  -0.0187 0.0187  165 ILE   B CG2 
1451 C  CD1 . ILE   B 156 ? 0.7102 0.5471 0.3902 0.3315  -0.0201 0.0180  165 ILE   B CD1 
1452 N  N   . THR   B 157 ? 0.6082 0.5053 0.3832 0.2267  0.0058  0.0413  166 THR   B N   
1453 C  CA  . THR   B 157 ? 0.6044 0.5000 0.3889 0.2048  0.0053  0.0414  166 THR   B CA  
1454 C  C   . THR   B 157 ? 0.6087 0.4868 0.3936 0.1925  0.0001  0.0335  166 THR   B C   
1455 O  O   . THR   B 157 ? 0.6027 0.4867 0.3967 0.1885  0.0039  0.0300  166 THR   B O   
1456 C  CB  . THR   B 157 ? 0.6004 0.5208 0.4038 0.1923  0.0154  0.0463  166 THR   B CB  
1457 O  OG1 . THR   B 157 ? 0.6010 0.5413 0.4078 0.2014  0.0198  0.0545  166 THR   B OG1 
1458 C  CG2 . THR   B 157 ? 0.6007 0.5207 0.4107 0.1719  0.0152  0.0453  166 THR   B CG2 
1459 N  N   . GLN   B 158 ? 0.6128 0.4707 0.3894 0.1862  -0.0082 0.0316  167 GLN   B N   
1460 C  CA  . GLN   B 158 ? 0.6190 0.4625 0.3985 0.1728  -0.0134 0.0252  167 GLN   B CA  
1461 C  C   . GLN   B 158 ? 0.6347 0.4800 0.4208 0.1524  -0.0112 0.0289  167 GLN   B C   
1462 O  O   . GLN   B 158 ? 0.6310 0.4758 0.4110 0.1517  -0.0114 0.0353  167 GLN   B O   
1463 C  CB  . GLN   B 158 ? 0.6348 0.4489 0.3976 0.1825  -0.0265 0.0197  167 GLN   B CB  
1464 C  CG  . GLN   B 158 ? 0.6433 0.4418 0.4102 0.1688  -0.0342 0.0130  167 GLN   B CG  
1465 C  CD  . GLN   B 158 ? 0.6695 0.4840 0.4512 0.1646  -0.0302 0.0075  167 GLN   B CD  
1466 O  OE1 . GLN   B 158 ? 0.6694 0.5052 0.4664 0.1544  -0.0200 0.0101  167 GLN   B OE1 
1467 N  NE2 . GLN   B 158 ? 0.6705 0.4742 0.4471 0.1727  -0.0390 -0.0007 167 GLN   B NE2 
1468 N  N   . GLY   B 159 ? 0.6472 0.4964 0.4451 0.1372  -0.0090 0.0252  168 GLY   B N   
1469 C  CA  . GLY   B 159 ? 0.6748 0.5267 0.4776 0.1186  -0.0061 0.0285  168 GLY   B CA  
1470 C  C   . GLY   B 159 ? 0.7263 0.5549 0.5219 0.1109  -0.0152 0.0293  168 GLY   B C   
1471 O  O   . GLY   B 159 ? 0.7414 0.5480 0.5255 0.1210  -0.0251 0.0272  168 GLY   B O   
1472 N  N   . LYS   B 160 ? 0.7563 0.5886 0.5577 0.0930  -0.0117 0.0326  169 LYS   B N   
1473 C  CA  . LYS   B 160 ? 0.7971 0.6090 0.5948 0.0813  -0.0189 0.0356  169 LYS   B CA  
1474 C  C   . LYS   B 160 ? 0.8114 0.6370 0.6275 0.0652  -0.0146 0.0322  169 LYS   B C   
1475 O  O   . LYS   B 160 ? 0.8019 0.6516 0.6284 0.0588  -0.0038 0.0318  169 LYS   B O   
1476 C  CB  . LYS   B 160 ? 0.8372 0.6430 0.6234 0.0743  -0.0175 0.0465  169 LYS   B CB  
1477 C  CG  . LYS   B 160 ? 0.9171 0.6996 0.6987 0.0610  -0.0240 0.0525  169 LYS   B CG  
1478 C  CD  . LYS   B 160 ? 0.9888 0.7669 0.7577 0.0542  -0.0215 0.0648  169 LYS   B CD  
1479 C  CE  . LYS   B 160 ? 1.0471 0.7983 0.8102 0.0408  -0.0281 0.0731  169 LYS   B CE  
1480 N  NZ  . LYS   B 160 ? 1.0865 0.8383 0.8381 0.0321  -0.0232 0.0867  169 LYS   B NZ  
1481 N  N   . ARG   B 161 ? 0.8337 0.6450 0.6546 0.0597  -0.0236 0.0287  170 ARG   B N   
1482 C  CA  . ARG   B 161 ? 0.8486 0.6758 0.6897 0.0444  -0.0205 0.0261  170 ARG   B CA  
1483 C  C   . ARG   B 161 ? 0.8831 0.7021 0.7243 0.0251  -0.0203 0.0360  170 ARG   B C   
1484 O  O   . ARG   B 161 ? 0.9034 0.6929 0.7331 0.0233  -0.0308 0.0401  170 ARG   B O   
1485 C  CB  . ARG   B 161 ? 0.8637 0.6841 0.7128 0.0487  -0.0314 0.0163  170 ARG   B CB  
1486 C  CG  . ARG   B 161 ? 0.8871 0.7237 0.7593 0.0316  -0.0307 0.0144  170 ARG   B CG  
1487 C  CD  . ARG   B 161 ? 0.9280 0.7631 0.8094 0.0370  -0.0421 0.0037  170 ARG   B CD  
1488 N  NE  . ARG   B 161 ? 0.9549 0.8174 0.8629 0.0234  -0.0383 0.0016  170 ARG   B NE  
1489 C  CZ  . ARG   B 161 ? 0.9717 0.8511 0.8932 0.0304  -0.0409 -0.0075 170 ARG   B CZ  
1490 N  NH1 . ARG   B 161 ? 0.9617 0.8323 0.8713 0.0503  -0.0472 -0.0149 170 ARG   B NH1 
1491 N  NH2 . ARG   B 161 ? 0.9645 0.8717 0.9116 0.0186  -0.0369 -0.0086 170 ARG   B NH2 
1492 N  N   . GLU   B 162 ? 0.8871 0.7306 0.7393 0.0118  -0.0081 0.0404  171 GLU   B N   
1493 C  CA  . GLU   B 162 ? 0.9121 0.7524 0.7646 -0.0070 -0.0054 0.0518  171 GLU   B CA  
1494 C  C   . GLU   B 162 ? 0.9174 0.7553 0.7883 -0.0222 -0.0119 0.0512  171 GLU   B C   
1495 O  O   . GLU   B 162 ? 0.9140 0.7721 0.8001 -0.0391 -0.0037 0.0568  171 GLU   B O   
1496 C  CB  . GLU   B 162 ? 0.9465 0.8169 0.8027 -0.0141 0.0108  0.0559  171 GLU   B CB  
1497 C  CG  . GLU   B 162 ? 1.0400 0.9146 0.8803 -0.0013 0.0159  0.0554  171 GLU   B CG  
1498 C  CD  . GLU   B 162 ? 1.1760 1.0298 0.9938 -0.0003 0.0121  0.0664  171 GLU   B CD  
1499 O  OE1 . GLU   B 162 ? 1.1964 1.0581 1.0072 -0.0104 0.0196  0.0756  171 GLU   B OE1 
1500 O  OE2 . GLU   B 162 ? 1.2241 1.0544 1.0302 0.0119  0.0017  0.0659  171 GLU   B OE2 
1501 S  S   . DMS   C .   ? 1.1136 1.0479 0.9930 0.0308  0.0594  -0.0551 201 DMS   B S   
1502 O  O   . DMS   C .   ? 1.1088 1.0535 0.9827 0.0380  0.0641  -0.0505 201 DMS   B O   
1503 C  C1  . DMS   C .   ? 1.1211 1.0327 1.0045 0.0364  0.0645  -0.0669 201 DMS   B C1  
1504 C  C2  . DMS   C .   ? 1.1057 1.0370 1.0046 0.0318  0.0581  -0.0400 201 DMS   B C2  
1505 N  N1  . A1B9L D .   ? 0.6012 0.6556 0.5590 0.1233  0.0855  0.1064  202 A1B9L B N1  
1506 N  N3  . A1B9L D .   ? 0.5433 0.6101 0.4571 0.1084  0.0395  0.0723  202 A1B9L B N3  
1507 C  C4  . A1B9L D .   ? 0.5395 0.6251 0.4976 0.1106  0.0655  0.0950  202 A1B9L B C4  
1508 C  C5  . A1B9L D .   ? 0.5353 0.6157 0.4906 0.0978  0.0578  0.0850  202 A1B9L B C5  
1509 C  C6  . A1B9L D .   ? 0.5400 0.6138 0.4779 0.1046  0.0515  0.0794  202 A1B9L B C6  
1510 C  C7  . A1B9L D .   ? 0.5459 0.6147 0.4695 0.1232  0.0518  0.0820  202 A1B9L B C7  
1511 C  C8  . A1B9L D .   ? 0.5506 0.6240 0.4756 0.1371  0.0586  0.0899  202 A1B9L B C8  
1512 C  C10 . A1B9L D .   ? 0.5402 0.6079 0.4693 0.0943  0.0438  0.0701  202 A1B9L B C10 
1513 C  C13 . A1B9L D .   ? 0.6228 0.6995 0.5281 0.2043  0.0947  0.1246  202 A1B9L B C13 
1514 C  C15 . A1B9L D .   ? 0.5990 0.7264 0.5381 0.1943  0.1036  0.1448  202 A1B9L B C15 
1515 C  C17 . A1B9L D .   ? 0.5973 0.7155 0.5447 0.1744  0.0952  0.1347  202 A1B9L B C17 
1516 C  C1  . A1B9L D .   ? 0.6027 0.6680 0.5525 0.1347  0.0832  0.1075  202 A1B9L B C1  
1517 C  C2  . A1B9L D .   ? 0.6007 0.6761 0.5378 0.1512  0.0799  0.1081  202 A1B9L B C2  
1518 N  N2  . A1B9L D .   ? 0.5750 0.6668 0.5184 0.1451  0.0740  0.1075  202 A1B9L B N2  
1519 C  C3  . A1B9L D .   ? 0.5548 0.6374 0.4968 0.1309  0.0661  0.0970  202 A1B9L B C3  
1520 C  C9  . A1B9L D .   ? 0.5473 0.6047 0.4539 0.1248  0.0439  0.0755  202 A1B9L B C9  
1521 C  C11 . A1B9L D .   ? 0.6059 0.6936 0.5387 0.1706  0.0876  0.1197  202 A1B9L B C11 
1522 C  C12 . A1B9L D .   ? 0.6225 0.6912 0.5363 0.1851  0.0878  0.1155  202 A1B9L B C12 
1523 CL CL1 . A1B9L D .   ? 0.6464 0.6971 0.5261 0.2210  0.0914  0.1161  202 A1B9L B CL1 
1524 C  C14 . A1B9L D .   ? 0.6083 0.7142 0.5243 0.2104  0.1033  0.1395  202 A1B9L B C14 
1525 N  N4  . A1B9L D .   ? 0.5832 0.7447 0.5405 0.1945  0.1107  0.1591  202 A1B9L B N4  
1526 N  N5  . A1B9L D .   ? 0.5759 0.7505 0.5535 0.1754  0.1058  0.1581  202 A1B9L B N5  
1527 C  C16 . A1B9L D .   ? 0.5855 0.7334 0.5557 0.1638  0.0965  0.1434  202 A1B9L B C16 
1528 S  S   . DMS   E .   ? 1.6953 1.4829 1.3904 0.2400  -0.0450 0.0665  203 DMS   B S   
1529 O  O   . DMS   E .   ? 1.6880 1.4919 1.3869 0.2318  -0.0435 0.0765  203 DMS   B O   
1530 C  C1  . DMS   E .   ? 1.6937 1.4722 1.3992 0.2123  -0.0428 0.0602  203 DMS   B C1  
1531 C  C2  . DMS   E .   ? 1.7223 1.4553 1.3904 0.2519  -0.0601 0.0632  203 DMS   B C2  
# 
