data_7I9U
# 
_entry.id   7I9U 
# 
_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   7I9U         pdb_00007i9u 10.2210/pdb7i9u/pdb 
WWPDB D_1001408497 ?            ?                   
# 
_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                        7I9U 
_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)-2-(3-chloro-5-cyclopropylphenyl)-N-(2,2-difluoroethyl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]acetamide' 
405.869   1  ?                           ?    ? ? 
5 water       nat water                                                                                                          
18.015    74 ?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                                           DMS   
4 '(2R)-2-(3-chloro-5-cyclopropylphenyl)-N-(2,2-difluoroethyl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]acetamide' A1B9E 
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 
A1B9E non-polymer         . 
'(2R)-2-(3-chloro-5-cyclopropylphenyl)-N-(2,2-difluoroethyl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]acetamide' ? 
'C21 H22 Cl F2 N3 O' 405.869 
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  16  GLY GLY 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 A1B9E 1  202 203 A1B9E LIG B . 
E 3 DMS   1  203 204 DMS   DMS B . 
F 5 HOH   1  101 34  HOH   HOH A . 
F 5 HOH   2  102 98  HOH   HOH A . 
F 5 HOH   3  103 65  HOH   HOH A . 
F 5 HOH   4  104 118 HOH   HOH A . 
F 5 HOH   5  105 129 HOH   HOH A . 
F 5 HOH   6  106 20  HOH   HOH A . 
F 5 HOH   7  107 133 HOH   HOH A . 
F 5 HOH   8  108 130 HOH   HOH A . 
F 5 HOH   9  109 28  HOH   HOH A . 
F 5 HOH   10 110 48  HOH   HOH A . 
F 5 HOH   11 111 119 HOH   HOH A . 
F 5 HOH   12 112 29  HOH   HOH A . 
F 5 HOH   13 113 127 HOH   HOH A . 
F 5 HOH   14 114 50  HOH   HOH A . 
F 5 HOH   15 115 120 HOH   HOH A . 
F 5 HOH   16 116 132 HOH   HOH A . 
F 5 HOH   17 117 27  HOH   HOH A . 
F 5 HOH   18 118 135 HOH   HOH A . 
G 5 HOH   1  301 11  HOH   HOH B . 
G 5 HOH   2  302 4   HOH   HOH B . 
G 5 HOH   3  303 14  HOH   HOH B . 
G 5 HOH   4  304 79  HOH   HOH B . 
G 5 HOH   5  305 81  HOH   HOH B . 
G 5 HOH   6  306 46  HOH   HOH B . 
G 5 HOH   7  307 31  HOH   HOH B . 
G 5 HOH   8  308 57  HOH   HOH B . 
G 5 HOH   9  309 58  HOH   HOH B . 
G 5 HOH   10 310 13  HOH   HOH B . 
G 5 HOH   11 311 1   HOH   HOH B . 
G 5 HOH   12 312 5   HOH   HOH B . 
G 5 HOH   13 313 63  HOH   HOH B . 
G 5 HOH   14 314 117 HOH   HOH B . 
G 5 HOH   15 315 124 HOH   HOH B . 
G 5 HOH   16 316 32  HOH   HOH B . 
G 5 HOH   17 317 138 HOH   HOH B . 
G 5 HOH   18 318 56  HOH   HOH B . 
G 5 HOH   19 319 61  HOH   HOH B . 
G 5 HOH   20 320 2   HOH   HOH B . 
G 5 HOH   21 321 102 HOH   HOH B . 
G 5 HOH   22 322 35  HOH   HOH B . 
G 5 HOH   23 323 9   HOH   HOH B . 
G 5 HOH   24 324 108 HOH   HOH B . 
G 5 HOH   25 325 137 HOH   HOH B . 
G 5 HOH   26 326 26  HOH   HOH B . 
G 5 HOH   27 327 16  HOH   HOH B . 
G 5 HOH   28 328 67  HOH   HOH B . 
G 5 HOH   29 329 69  HOH   HOH B . 
G 5 HOH   30 330 39  HOH   HOH B . 
G 5 HOH   31 331 30  HOH   HOH B . 
G 5 HOH   32 332 23  HOH   HOH B . 
G 5 HOH   33 333 107 HOH   HOH B . 
G 5 HOH   34 334 136 HOH   HOH B . 
G 5 HOH   35 335 43  HOH   HOH B . 
G 5 HOH   36 336 103 HOH   HOH B . 
G 5 HOH   37 337 21  HOH   HOH B . 
G 5 HOH   38 338 134 HOH   HOH B . 
G 5 HOH   39 339 64  HOH   HOH B . 
G 5 HOH   40 340 116 HOH   HOH B . 
G 5 HOH   41 341 3   HOH   HOH B . 
G 5 HOH   42 342 131 HOH   HOH B . 
G 5 HOH   43 343 125 HOH   HOH B . 
G 5 HOH   44 344 45  HOH   HOH B . 
G 5 HOH   45 345 18  HOH   HOH B . 
G 5 HOH   46 346 73  HOH   HOH B . 
G 5 HOH   47 347 72  HOH   HOH B . 
G 5 HOH   48 348 90  HOH   HOH B . 
G 5 HOH   49 349 80  HOH   HOH B . 
G 5 HOH   50 350 128 HOH   HOH B . 
G 5 HOH   51 351 126 HOH   HOH B . 
G 5 HOH   52 352 54  HOH   HOH B . 
G 5 HOH   53 353 123 HOH   HOH B . 
G 5 HOH   54 354 75  HOH   HOH B . 
G 5 HOH   55 355 109 HOH   HOH B . 
G 5 HOH   56 356 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           7I9U 
_cell.length_a           42.593 
_cell.length_b           42.593 
_cell.length_c           216.322 
_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                         7I9U 
_symmetry.Int_Tables_number                95 
_symmetry.space_group_name_H-M             'P 43 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.entry_id          7I9U 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.070 
_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   41.87 
_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   2024-07-23 
_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                     7I9U 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             33.460 
_reflns.d_resolution_high            2.160 
_reflns.number_obs                   11594 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.457 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.000 
_reflns.B_iso_Wilson_estimate        51.530 
_reflns.pdbx_redundancy              19.100 
_reflns.pdbx_Rrim_I_all              0.470 
_reflns.pdbx_Rpim_I_all              0.108 
_reflns.pdbx_CC_half                 0.992 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     220890 
_reflns.pdbx_scaling_rejects         113 
_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 2.160 2.280  ? 32034 ? ? 9.954 ? ? ? 19.800 ? 0.300  ? 1616 ? ? ? ? 100.000 10.231 2.320 0.529 ? 
1 2 6.830 33.460 ? 6566  ? ? 0.075 ? ? ? 14.800 ? 21.300 ? 443  ? ? ? ? 99.100  0.078  0.019 0.998 ? 
# 
_refine.entry_id                                 7I9U 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.1590 
_refine.ls_d_res_low                             33.4600 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    97.3000 
_refine.ls_number_reflns_obs                     11255 
_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                          0.2350 
_refine.ls_R_factor_R_work                       0.2329 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2741 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.7400 
_refine.ls_number_reflns_R_free                  534 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               59.1900 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -7.1112 
_refine.aniso_B[2][2]                            -7.1112 
_refine.aniso_B[3][3]                            14.2225 
_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               0.9300 
_refine.correlation_coeff_Fo_to_Fc_free          0.9180 
_refine.overall_SU_R_Cruickshank_DPI             0.2930 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2250 
_refine.pdbx_overall_SU_R_Blow_DPI               0.3320 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2340 
_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                                111.200 
_refine.B_iso_min                                26.420 
_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                        7I9U 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.380 
_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                       2.1590 
_refine_hist.d_res_low                        33.4600 
_refine_hist.pdbx_number_atoms_ligand         36 
_refine_hist.number_atoms_solvent             74 
_refine_hist.number_atoms_total               1586 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           67.69 
_refine_hist.pdbx_B_iso_mean_solvent          53.55 
_refine_hist.pdbx_number_atoms_protein        1476 
_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        542  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              269  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1572 ?      ? 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 195  ?      ? 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      1169 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1572 0.007  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2139 0.950  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    2.940  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    20.520 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.1600 
_refine_ls_shell.d_res_low                        2.1900 
_refine_ls_shell.pdbx_total_number_of_bins_used   27 
_refine_ls_shell.percent_reflns_obs               83.5600 
_refine_ls_shell.number_reflns_R_work             415 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.4121 
_refine_ls_shell.R_factor_R_free                  0.4249 
_refine_ls_shell.percent_reflns_R_free            4.1600 
_refine_ls_shell.number_reflns_R_free             18 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                433 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7I9U 
_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-0029491-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I9U 
_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 7I9U A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I9U 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 7I9U SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I9U MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I9U MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I9U 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)' 4450 ? 
1 MORE         -22  ? 
1 'SSA (A^2)'  9710 ? 
# 
_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 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
AA1 4 5 N GLY B 12  ? N GLY B 21  O MET B 32  ? O MET B 41  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N 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 O GLU A 23  ? O GLU A 66  N GLN B 101 ? N GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O ILE B 138 ? O ILE B 147 
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 ILE B 106 ? O ILE B 115 
AA3 3 4 N GLY B 105 ? N GLY B 114 O ALA B 116 ? O ALA B 125 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7I9U 
_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 LEU B 30  ? ? -79.37  -157.89 
2 1 CYS B 80  ? ? 83.71   -16.97  
3 1 ALA B 127 ? ? -102.43 74.42   
# 
_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     356 
_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 -13.7243 -2.0193 -19.4447 -0.0942 -0.0682 -0.2786 0.2029 0.1710 0.1416 4.8565 4.6172 5.2704 
-1.6511 0.7699 1.3842  0.4760 -0.4810 0.0050  0.5932 0.2946 -0.4141 -0.5962 -0.1429 0.5181 
'X-RAY DIFFRACTION' 2 ? refined -18.2844 0.5493  -15.6429 0.0772  -0.0183 -0.0534 0.2189 0.0346 0.0486 2.4518 1.9759 2.9574 
-1.4074 0.1990 -0.3588 0.5074 -0.4704 -0.0370 0.2000 0.1701 0.0021  -0.1589 0.1063  0.1865 
# 
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 16 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 GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 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 
A1B9E N1   N  N N 1   
A1B9E N3   N  N N 2   
A1B9E C4   C  N R 3   
A1B9E C5   C  Y N 4   
A1B9E C6   C  Y N 5   
A1B9E C7   C  Y N 6   
A1B9E C8   C  Y N 7   
A1B9E C10  C  Y N 8   
A1B9E C13  C  Y N 9   
A1B9E C15  C  Y N 10  
A1B9E C17  C  Y N 11  
A1B9E C20  C  N N 12  
A1B9E C21  C  Y N 13  
A1B9E O1   O  N N 14  
A1B9E C1   C  N N 15  
A1B9E C2   C  N N 16  
A1B9E C3   C  N N 17  
A1B9E F1   F  N N 18  
A1B9E F2   F  N N 19  
A1B9E N2   N  N N 20  
A1B9E C9   C  Y N 21  
A1B9E C11  C  N N 22  
A1B9E C12  C  N N 23  
A1B9E C14  C  Y N 24  
A1B9E CL1  CL N N 25  
A1B9E C16  C  Y N 26  
A1B9E C18  C  N N 27  
A1B9E C19  C  N N 28  
A1B9E H1   H  N N 29  
A1B9E H2   H  N N 30  
A1B9E H4   H  N N 31  
A1B9E H5   H  N N 32  
A1B9E H6   H  N N 33  
A1B9E H7   H  N N 34  
A1B9E H8   H  N N 35  
A1B9E H9   H  N N 36  
A1B9E H10  H  N N 37  
A1B9E H11  H  N N 38  
A1B9E H12  H  N N 39  
A1B9E H13  H  N N 40  
A1B9E H14  H  N N 41  
A1B9E H15  H  N N 42  
A1B9E H16  H  N N 43  
A1B9E H17  H  N N 44  
A1B9E H18  H  N N 45  
A1B9E H19  H  N N 46  
A1B9E H20  H  N N 47  
A1B9E H21  H  N N 48  
A1B9E H22  H  N N 49  
A1B9E H23  H  N N 50  
ALA   N    N  N N 51  
ALA   CA   C  N S 52  
ALA   C    C  N N 53  
ALA   O    O  N N 54  
ALA   CB   C  N N 55  
ALA   OXT  O  N N 56  
ALA   H    H  N N 57  
ALA   H2   H  N N 58  
ALA   HA   H  N N 59  
ALA   HB1  H  N N 60  
ALA   HB2  H  N N 61  
ALA   HB3  H  N N 62  
ALA   HXT  H  N N 63  
ARG   N    N  N N 64  
ARG   CA   C  N S 65  
ARG   C    C  N N 66  
ARG   O    O  N N 67  
ARG   CB   C  N N 68  
ARG   CG   C  N N 69  
ARG   CD   C  N N 70  
ARG   NE   N  N N 71  
ARG   CZ   C  N N 72  
ARG   NH1  N  N N 73  
ARG   NH2  N  N N 74  
ARG   OXT  O  N N 75  
ARG   H    H  N N 76  
ARG   H2   H  N N 77  
ARG   HA   H  N N 78  
ARG   HB2  H  N N 79  
ARG   HB3  H  N N 80  
ARG   HG2  H  N N 81  
ARG   HG3  H  N N 82  
ARG   HD2  H  N N 83  
ARG   HD3  H  N N 84  
ARG   HE   H  N N 85  
ARG   HH11 H  N N 86  
ARG   HH12 H  N N 87  
ARG   HH21 H  N N 88  
ARG   HH22 H  N N 89  
ARG   HXT  H  N N 90  
ASN   N    N  N N 91  
ASN   CA   C  N S 92  
ASN   C    C  N N 93  
ASN   O    O  N N 94  
ASN   CB   C  N N 95  
ASN   CG   C  N N 96  
ASN   OD1  O  N N 97  
ASN   ND2  N  N N 98  
ASN   OXT  O  N N 99  
ASN   H    H  N N 100 
ASN   H2   H  N N 101 
ASN   HA   H  N N 102 
ASN   HB2  H  N N 103 
ASN   HB3  H  N N 104 
ASN   HD21 H  N N 105 
ASN   HD22 H  N N 106 
ASN   HXT  H  N N 107 
ASP   N    N  N N 108 
ASP   CA   C  N S 109 
ASP   C    C  N N 110 
ASP   O    O  N N 111 
ASP   CB   C  N N 112 
ASP   CG   C  N N 113 
ASP   OD1  O  N N 114 
ASP   OD2  O  N N 115 
ASP   OXT  O  N N 116 
ASP   H    H  N N 117 
ASP   H2   H  N N 118 
ASP   HA   H  N N 119 
ASP   HB2  H  N N 120 
ASP   HB3  H  N N 121 
ASP   HD2  H  N N 122 
ASP   HXT  H  N N 123 
CYS   N    N  N N 124 
CYS   CA   C  N R 125 
CYS   C    C  N N 126 
CYS   O    O  N N 127 
CYS   CB   C  N N 128 
CYS   SG   S  N N 129 
CYS   OXT  O  N N 130 
CYS   H    H  N N 131 
CYS   H2   H  N N 132 
CYS   HA   H  N N 133 
CYS   HB2  H  N N 134 
CYS   HB3  H  N N 135 
CYS   HG   H  N N 136 
CYS   HXT  H  N N 137 
DMS   S    S  N N 138 
DMS   O    O  N N 139 
DMS   C1   C  N N 140 
DMS   C2   C  N N 141 
DMS   H11  H  N N 142 
DMS   H12  H  N N 143 
DMS   H13  H  N N 144 
DMS   H21  H  N N 145 
DMS   H22  H  N N 146 
DMS   H23  H  N N 147 
GLN   N    N  N N 148 
GLN   CA   C  N S 149 
GLN   C    C  N N 150 
GLN   O    O  N N 151 
GLN   CB   C  N N 152 
GLN   CG   C  N N 153 
GLN   CD   C  N N 154 
GLN   OE1  O  N N 155 
GLN   NE2  N  N N 156 
GLN   OXT  O  N N 157 
GLN   H    H  N N 158 
GLN   H2   H  N N 159 
GLN   HA   H  N N 160 
GLN   HB2  H  N N 161 
GLN   HB3  H  N N 162 
GLN   HG2  H  N N 163 
GLN   HG3  H  N N 164 
GLN   HE21 H  N N 165 
GLN   HE22 H  N N 166 
GLN   HXT  H  N N 167 
GLU   N    N  N N 168 
GLU   CA   C  N S 169 
GLU   C    C  N N 170 
GLU   O    O  N N 171 
GLU   CB   C  N N 172 
GLU   CG   C  N N 173 
GLU   CD   C  N N 174 
GLU   OE1  O  N N 175 
GLU   OE2  O  N N 176 
GLU   OXT  O  N N 177 
GLU   H    H  N N 178 
GLU   H2   H  N N 179 
GLU   HA   H  N N 180 
GLU   HB2  H  N N 181 
GLU   HB3  H  N N 182 
GLU   HG2  H  N N 183 
GLU   HG3  H  N N 184 
GLU   HE2  H  N N 185 
GLU   HXT  H  N N 186 
GLY   N    N  N N 187 
GLY   CA   C  N N 188 
GLY   C    C  N N 189 
GLY   O    O  N N 190 
GLY   OXT  O  N N 191 
GLY   H    H  N N 192 
GLY   H2   H  N N 193 
GLY   HA2  H  N N 194 
GLY   HA3  H  N N 195 
GLY   HXT  H  N N 196 
HIS   N    N  N N 197 
HIS   CA   C  N S 198 
HIS   C    C  N N 199 
HIS   O    O  N N 200 
HIS   CB   C  N N 201 
HIS   CG   C  Y N 202 
HIS   ND1  N  Y N 203 
HIS   CD2  C  Y N 204 
HIS   CE1  C  Y N 205 
HIS   NE2  N  Y N 206 
HIS   OXT  O  N N 207 
HIS   H    H  N N 208 
HIS   H2   H  N N 209 
HIS   HA   H  N N 210 
HIS   HB2  H  N N 211 
HIS   HB3  H  N N 212 
HIS   HD1  H  N N 213 
HIS   HD2  H  N N 214 
HIS   HE1  H  N N 215 
HIS   HE2  H  N N 216 
HIS   HXT  H  N N 217 
HOH   O    O  N N 218 
HOH   H1   H  N N 219 
HOH   H2   H  N N 220 
ILE   N    N  N N 221 
ILE   CA   C  N S 222 
ILE   C    C  N N 223 
ILE   O    O  N N 224 
ILE   CB   C  N S 225 
ILE   CG1  C  N N 226 
ILE   CG2  C  N N 227 
ILE   CD1  C  N N 228 
ILE   OXT  O  N N 229 
ILE   H    H  N N 230 
ILE   H2   H  N N 231 
ILE   HA   H  N N 232 
ILE   HB   H  N N 233 
ILE   HG12 H  N N 234 
ILE   HG13 H  N N 235 
ILE   HG21 H  N N 236 
ILE   HG22 H  N N 237 
ILE   HG23 H  N N 238 
ILE   HD11 H  N N 239 
ILE   HD12 H  N N 240 
ILE   HD13 H  N N 241 
ILE   HXT  H  N N 242 
LEU   N    N  N N 243 
LEU   CA   C  N S 244 
LEU   C    C  N N 245 
LEU   O    O  N N 246 
LEU   CB   C  N N 247 
LEU   CG   C  N N 248 
LEU   CD1  C  N N 249 
LEU   CD2  C  N N 250 
LEU   OXT  O  N N 251 
LEU   H    H  N N 252 
LEU   H2   H  N N 253 
LEU   HA   H  N N 254 
LEU   HB2  H  N N 255 
LEU   HB3  H  N N 256 
LEU   HG   H  N N 257 
LEU   HD11 H  N N 258 
LEU   HD12 H  N N 259 
LEU   HD13 H  N N 260 
LEU   HD21 H  N N 261 
LEU   HD22 H  N N 262 
LEU   HD23 H  N N 263 
LEU   HXT  H  N N 264 
LYS   N    N  N N 265 
LYS   CA   C  N S 266 
LYS   C    C  N N 267 
LYS   O    O  N N 268 
LYS   CB   C  N N 269 
LYS   CG   C  N N 270 
LYS   CD   C  N N 271 
LYS   CE   C  N N 272 
LYS   NZ   N  N N 273 
LYS   OXT  O  N N 274 
LYS   H    H  N N 275 
LYS   H2   H  N N 276 
LYS   HA   H  N N 277 
LYS   HB2  H  N N 278 
LYS   HB3  H  N N 279 
LYS   HG2  H  N N 280 
LYS   HG3  H  N N 281 
LYS   HD2  H  N N 282 
LYS   HD3  H  N N 283 
LYS   HE2  H  N N 284 
LYS   HE3  H  N N 285 
LYS   HZ1  H  N N 286 
LYS   HZ2  H  N N 287 
LYS   HZ3  H  N N 288 
LYS   HXT  H  N N 289 
MET   N    N  N N 290 
MET   CA   C  N S 291 
MET   C    C  N N 292 
MET   O    O  N N 293 
MET   CB   C  N N 294 
MET   CG   C  N N 295 
MET   SD   S  N N 296 
MET   CE   C  N N 297 
MET   OXT  O  N N 298 
MET   H    H  N N 299 
MET   H2   H  N N 300 
MET   HA   H  N N 301 
MET   HB2  H  N N 302 
MET   HB3  H  N N 303 
MET   HG2  H  N N 304 
MET   HG3  H  N N 305 
MET   HE1  H  N N 306 
MET   HE2  H  N N 307 
MET   HE3  H  N N 308 
MET   HXT  H  N N 309 
PHE   N    N  N N 310 
PHE   CA   C  N S 311 
PHE   C    C  N N 312 
PHE   O    O  N N 313 
PHE   CB   C  N N 314 
PHE   CG   C  Y N 315 
PHE   CD1  C  Y N 316 
PHE   CD2  C  Y N 317 
PHE   CE1  C  Y N 318 
PHE   CE2  C  Y N 319 
PHE   CZ   C  Y N 320 
PHE   OXT  O  N N 321 
PHE   H    H  N N 322 
PHE   H2   H  N N 323 
PHE   HA   H  N N 324 
PHE   HB2  H  N N 325 
PHE   HB3  H  N N 326 
PHE   HD1  H  N N 327 
PHE   HD2  H  N N 328 
PHE   HE1  H  N N 329 
PHE   HE2  H  N N 330 
PHE   HZ   H  N N 331 
PHE   HXT  H  N N 332 
PRO   N    N  N N 333 
PRO   CA   C  N S 334 
PRO   C    C  N N 335 
PRO   O    O  N N 336 
PRO   CB   C  N N 337 
PRO   CG   C  N N 338 
PRO   CD   C  N N 339 
PRO   OXT  O  N N 340 
PRO   H    H  N N 341 
PRO   HA   H  N N 342 
PRO   HB2  H  N N 343 
PRO   HB3  H  N N 344 
PRO   HG2  H  N N 345 
PRO   HG3  H  N N 346 
PRO   HD2  H  N N 347 
PRO   HD3  H  N N 348 
PRO   HXT  H  N N 349 
SER   N    N  N N 350 
SER   CA   C  N S 351 
SER   C    C  N N 352 
SER   O    O  N N 353 
SER   CB   C  N N 354 
SER   OG   O  N N 355 
SER   OXT  O  N N 356 
SER   H    H  N N 357 
SER   H2   H  N N 358 
SER   HA   H  N N 359 
SER   HB2  H  N N 360 
SER   HB3  H  N N 361 
SER   HG   H  N N 362 
SER   HXT  H  N N 363 
THR   N    N  N N 364 
THR   CA   C  N S 365 
THR   C    C  N N 366 
THR   O    O  N N 367 
THR   CB   C  N R 368 
THR   OG1  O  N N 369 
THR   CG2  C  N N 370 
THR   OXT  O  N N 371 
THR   H    H  N N 372 
THR   H2   H  N N 373 
THR   HA   H  N N 374 
THR   HB   H  N N 375 
THR   HG1  H  N N 376 
THR   HG21 H  N N 377 
THR   HG22 H  N N 378 
THR   HG23 H  N N 379 
THR   HXT  H  N N 380 
TRP   N    N  N N 381 
TRP   CA   C  N S 382 
TRP   C    C  N N 383 
TRP   O    O  N N 384 
TRP   CB   C  N N 385 
TRP   CG   C  Y N 386 
TRP   CD1  C  Y N 387 
TRP   CD2  C  Y N 388 
TRP   NE1  N  Y N 389 
TRP   CE2  C  Y N 390 
TRP   CE3  C  Y N 391 
TRP   CZ2  C  Y N 392 
TRP   CZ3  C  Y N 393 
TRP   CH2  C  Y N 394 
TRP   OXT  O  N N 395 
TRP   H    H  N N 396 
TRP   H2   H  N N 397 
TRP   HA   H  N N 398 
TRP   HB2  H  N N 399 
TRP   HB3  H  N N 400 
TRP   HD1  H  N N 401 
TRP   HE1  H  N N 402 
TRP   HE3  H  N N 403 
TRP   HZ2  H  N N 404 
TRP   HZ3  H  N N 405 
TRP   HH2  H  N N 406 
TRP   HXT  H  N N 407 
TYR   N    N  N N 408 
TYR   CA   C  N S 409 
TYR   C    C  N N 410 
TYR   O    O  N N 411 
TYR   CB   C  N N 412 
TYR   CG   C  Y N 413 
TYR   CD1  C  Y N 414 
TYR   CD2  C  Y N 415 
TYR   CE1  C  Y N 416 
TYR   CE2  C  Y N 417 
TYR   CZ   C  Y N 418 
TYR   OH   O  N N 419 
TYR   OXT  O  N N 420 
TYR   H    H  N N 421 
TYR   H2   H  N N 422 
TYR   HA   H  N N 423 
TYR   HB2  H  N N 424 
TYR   HB3  H  N N 425 
TYR   HD1  H  N N 426 
TYR   HD2  H  N N 427 
TYR   HE1  H  N N 428 
TYR   HE2  H  N N 429 
TYR   HH   H  N N 430 
TYR   HXT  H  N N 431 
VAL   N    N  N N 432 
VAL   CA   C  N S 433 
VAL   C    C  N N 434 
VAL   O    O  N N 435 
VAL   CB   C  N N 436 
VAL   CG1  C  N N 437 
VAL   CG2  C  N N 438 
VAL   OXT  O  N N 439 
VAL   H    H  N N 440 
VAL   H2   H  N N 441 
VAL   HA   H  N N 442 
VAL   HB   H  N N 443 
VAL   HG11 H  N N 444 
VAL   HG12 H  N N 445 
VAL   HG13 H  N N 446 
VAL   HG21 H  N N 447 
VAL   HG22 H  N N 448 
VAL   HG23 H  N N 449 
VAL   HXT  H  N N 450 
# 
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 
A1B9E CL1 C15  sing N N 1   
A1B9E C19 C18  sing N N 2   
A1B9E C19 C20  sing N N 3   
A1B9E C16 C15  doub Y N 4   
A1B9E C16 C17  sing Y N 5   
A1B9E C18 C17  sing N N 6   
A1B9E C18 C20  sing N N 7   
A1B9E C15 C14  sing Y N 8   
A1B9E C17 C21  doub Y N 9   
A1B9E C14 C13  doub Y N 10  
A1B9E C21 C13  sing Y N 11  
A1B9E C13 C4   sing N N 12  
A1B9E F1  C3   sing N N 13  
A1B9E C3  F2   sing N N 14  
A1B9E C3  C2   sing N N 15  
A1B9E O1  C1   doub N N 16  
A1B9E C4  C1   sing N N 17  
A1B9E C4  N2   sing N N 18  
A1B9E C1  N1   sing N N 19  
A1B9E N2  C5   sing N N 20  
A1B9E C2  N1   sing N N 21  
A1B9E C5  C10  doub Y N 22  
A1B9E C5  C6   sing Y N 23  
A1B9E C10 C9   sing Y N 24  
A1B9E C6  C7   doub Y N 25  
A1B9E C9  C8   doub Y N 26  
A1B9E C9  C11  sing N N 27  
A1B9E C7  C8   sing Y N 28  
A1B9E C8  C12  sing N N 29  
A1B9E C11 N3   sing N N 30  
A1B9E C12 N3   sing N N 31  
A1B9E N1  H1   sing N N 32  
A1B9E N3  H2   sing N N 33  
A1B9E C4  H4   sing N N 34  
A1B9E C6  H5   sing N N 35  
A1B9E C7  H6   sing N N 36  
A1B9E C10 H7   sing N N 37  
A1B9E C20 H8   sing N N 38  
A1B9E C20 H9   sing N N 39  
A1B9E C21 H10  sing N N 40  
A1B9E C2  H11  sing N N 41  
A1B9E C2  H12  sing N N 42  
A1B9E C3  H13  sing N N 43  
A1B9E N2  H14  sing N N 44  
A1B9E C11 H15  sing N N 45  
A1B9E C11 H16  sing N N 46  
A1B9E C12 H17  sing N N 47  
A1B9E C12 H18  sing N N 48  
A1B9E C14 H19  sing N N 49  
A1B9E C16 H20  sing N N 50  
A1B9E C18 H21  sing N N 51  
A1B9E C19 H22  sing N N 52  
A1B9E C19 H23  sing N N 53  
ALA   N   CA   sing N N 54  
ALA   N   H    sing N N 55  
ALA   N   H2   sing N N 56  
ALA   CA  C    sing N N 57  
ALA   CA  CB   sing N N 58  
ALA   CA  HA   sing N N 59  
ALA   C   O    doub N N 60  
ALA   C   OXT  sing N N 61  
ALA   CB  HB1  sing N N 62  
ALA   CB  HB2  sing N N 63  
ALA   CB  HB3  sing N N 64  
ALA   OXT HXT  sing N N 65  
ARG   N   CA   sing N N 66  
ARG   N   H    sing N N 67  
ARG   N   H2   sing N N 68  
ARG   CA  C    sing N N 69  
ARG   CA  CB   sing N N 70  
ARG   CA  HA   sing N N 71  
ARG   C   O    doub N N 72  
ARG   C   OXT  sing N N 73  
ARG   CB  CG   sing N N 74  
ARG   CB  HB2  sing N N 75  
ARG   CB  HB3  sing N N 76  
ARG   CG  CD   sing N N 77  
ARG   CG  HG2  sing N N 78  
ARG   CG  HG3  sing N N 79  
ARG   CD  NE   sing N N 80  
ARG   CD  HD2  sing N N 81  
ARG   CD  HD3  sing N N 82  
ARG   NE  CZ   sing N N 83  
ARG   NE  HE   sing N N 84  
ARG   CZ  NH1  sing N N 85  
ARG   CZ  NH2  doub N N 86  
ARG   NH1 HH11 sing N N 87  
ARG   NH1 HH12 sing N N 88  
ARG   NH2 HH21 sing N N 89  
ARG   NH2 HH22 sing N N 90  
ARG   OXT HXT  sing N N 91  
ASN   N   CA   sing N N 92  
ASN   N   H    sing N N 93  
ASN   N   H2   sing N N 94  
ASN   CA  C    sing N N 95  
ASN   CA  CB   sing N N 96  
ASN   CA  HA   sing N N 97  
ASN   C   O    doub N N 98  
ASN   C   OXT  sing N N 99  
ASN   CB  CG   sing N N 100 
ASN   CB  HB2  sing N N 101 
ASN   CB  HB3  sing N N 102 
ASN   CG  OD1  doub N N 103 
ASN   CG  ND2  sing N N 104 
ASN   ND2 HD21 sing N N 105 
ASN   ND2 HD22 sing N N 106 
ASN   OXT HXT  sing N N 107 
ASP   N   CA   sing N N 108 
ASP   N   H    sing N N 109 
ASP   N   H2   sing N N 110 
ASP   CA  C    sing N N 111 
ASP   CA  CB   sing N N 112 
ASP   CA  HA   sing N N 113 
ASP   C   O    doub N N 114 
ASP   C   OXT  sing N N 115 
ASP   CB  CG   sing N N 116 
ASP   CB  HB2  sing N N 117 
ASP   CB  HB3  sing N N 118 
ASP   CG  OD1  doub N N 119 
ASP   CG  OD2  sing N N 120 
ASP   OD2 HD2  sing N N 121 
ASP   OXT HXT  sing N N 122 
CYS   N   CA   sing N N 123 
CYS   N   H    sing N N 124 
CYS   N   H2   sing N N 125 
CYS   CA  C    sing N N 126 
CYS   CA  CB   sing N N 127 
CYS   CA  HA   sing N N 128 
CYS   C   O    doub N N 129 
CYS   C   OXT  sing N N 130 
CYS   CB  SG   sing N N 131 
CYS   CB  HB2  sing N N 132 
CYS   CB  HB3  sing N N 133 
CYS   SG  HG   sing N N 134 
CYS   OXT HXT  sing N N 135 
DMS   S   O    doub N N 136 
DMS   S   C1   sing N N 137 
DMS   S   C2   sing N N 138 
DMS   C1  H11  sing N N 139 
DMS   C1  H12  sing N N 140 
DMS   C1  H13  sing N N 141 
DMS   C2  H21  sing N N 142 
DMS   C2  H22  sing N N 143 
DMS   C2  H23  sing N N 144 
GLN   N   CA   sing N N 145 
GLN   N   H    sing N N 146 
GLN   N   H2   sing N N 147 
GLN   CA  C    sing N N 148 
GLN   CA  CB   sing N N 149 
GLN   CA  HA   sing N N 150 
GLN   C   O    doub N N 151 
GLN   C   OXT  sing N N 152 
GLN   CB  CG   sing N N 153 
GLN   CB  HB2  sing N N 154 
GLN   CB  HB3  sing N N 155 
GLN   CG  CD   sing N N 156 
GLN   CG  HG2  sing N N 157 
GLN   CG  HG3  sing N N 158 
GLN   CD  OE1  doub N N 159 
GLN   CD  NE2  sing N N 160 
GLN   NE2 HE21 sing N N 161 
GLN   NE2 HE22 sing N N 162 
GLN   OXT HXT  sing N N 163 
GLU   N   CA   sing N N 164 
GLU   N   H    sing N N 165 
GLU   N   H2   sing N N 166 
GLU   CA  C    sing N N 167 
GLU   CA  CB   sing N N 168 
GLU   CA  HA   sing N N 169 
GLU   C   O    doub N N 170 
GLU   C   OXT  sing N N 171 
GLU   CB  CG   sing N N 172 
GLU   CB  HB2  sing N N 173 
GLU   CB  HB3  sing N N 174 
GLU   CG  CD   sing N N 175 
GLU   CG  HG2  sing N N 176 
GLU   CG  HG3  sing N N 177 
GLU   CD  OE1  doub N N 178 
GLU   CD  OE2  sing N N 179 
GLU   OE2 HE2  sing N N 180 
GLU   OXT HXT  sing N N 181 
GLY   N   CA   sing N N 182 
GLY   N   H    sing N N 183 
GLY   N   H2   sing N N 184 
GLY   CA  C    sing N N 185 
GLY   CA  HA2  sing N N 186 
GLY   CA  HA3  sing N N 187 
GLY   C   O    doub N N 188 
GLY   C   OXT  sing N N 189 
GLY   OXT HXT  sing N N 190 
HIS   N   CA   sing N N 191 
HIS   N   H    sing N N 192 
HIS   N   H2   sing N N 193 
HIS   CA  C    sing N N 194 
HIS   CA  CB   sing N N 195 
HIS   CA  HA   sing N N 196 
HIS   C   O    doub N N 197 
HIS   C   OXT  sing N N 198 
HIS   CB  CG   sing N N 199 
HIS   CB  HB2  sing N N 200 
HIS   CB  HB3  sing N N 201 
HIS   CG  ND1  sing Y N 202 
HIS   CG  CD2  doub Y N 203 
HIS   ND1 CE1  doub Y N 204 
HIS   ND1 HD1  sing N N 205 
HIS   CD2 NE2  sing Y N 206 
HIS   CD2 HD2  sing N N 207 
HIS   CE1 NE2  sing Y N 208 
HIS   CE1 HE1  sing N N 209 
HIS   NE2 HE2  sing N N 210 
HIS   OXT HXT  sing N N 211 
HOH   O   H1   sing N N 212 
HOH   O   H2   sing N N 213 
ILE   N   CA   sing N N 214 
ILE   N   H    sing N N 215 
ILE   N   H2   sing N N 216 
ILE   CA  C    sing N N 217 
ILE   CA  CB   sing N N 218 
ILE   CA  HA   sing N N 219 
ILE   C   O    doub N N 220 
ILE   C   OXT  sing N N 221 
ILE   CB  CG1  sing N N 222 
ILE   CB  CG2  sing N N 223 
ILE   CB  HB   sing N N 224 
ILE   CG1 CD1  sing N N 225 
ILE   CG1 HG12 sing N N 226 
ILE   CG1 HG13 sing N N 227 
ILE   CG2 HG21 sing N N 228 
ILE   CG2 HG22 sing N N 229 
ILE   CG2 HG23 sing N N 230 
ILE   CD1 HD11 sing N N 231 
ILE   CD1 HD12 sing N N 232 
ILE   CD1 HD13 sing N N 233 
ILE   OXT HXT  sing N N 234 
LEU   N   CA   sing N N 235 
LEU   N   H    sing N N 236 
LEU   N   H2   sing N N 237 
LEU   CA  C    sing N N 238 
LEU   CA  CB   sing N N 239 
LEU   CA  HA   sing N N 240 
LEU   C   O    doub N N 241 
LEU   C   OXT  sing N N 242 
LEU   CB  CG   sing N N 243 
LEU   CB  HB2  sing N N 244 
LEU   CB  HB3  sing N N 245 
LEU   CG  CD1  sing N N 246 
LEU   CG  CD2  sing N N 247 
LEU   CG  HG   sing N N 248 
LEU   CD1 HD11 sing N N 249 
LEU   CD1 HD12 sing N N 250 
LEU   CD1 HD13 sing N N 251 
LEU   CD2 HD21 sing N N 252 
LEU   CD2 HD22 sing N N 253 
LEU   CD2 HD23 sing N N 254 
LEU   OXT HXT  sing N N 255 
LYS   N   CA   sing N N 256 
LYS   N   H    sing N N 257 
LYS   N   H2   sing N N 258 
LYS   CA  C    sing N N 259 
LYS   CA  CB   sing N N 260 
LYS   CA  HA   sing N N 261 
LYS   C   O    doub N N 262 
LYS   C   OXT  sing N N 263 
LYS   CB  CG   sing N N 264 
LYS   CB  HB2  sing N N 265 
LYS   CB  HB3  sing N N 266 
LYS   CG  CD   sing N N 267 
LYS   CG  HG2  sing N N 268 
LYS   CG  HG3  sing N N 269 
LYS   CD  CE   sing N N 270 
LYS   CD  HD2  sing N N 271 
LYS   CD  HD3  sing N N 272 
LYS   CE  NZ   sing N N 273 
LYS   CE  HE2  sing N N 274 
LYS   CE  HE3  sing N N 275 
LYS   NZ  HZ1  sing N N 276 
LYS   NZ  HZ2  sing N N 277 
LYS   NZ  HZ3  sing N N 278 
LYS   OXT HXT  sing N N 279 
MET   N   CA   sing N N 280 
MET   N   H    sing N N 281 
MET   N   H2   sing N N 282 
MET   CA  C    sing N N 283 
MET   CA  CB   sing N N 284 
MET   CA  HA   sing N N 285 
MET   C   O    doub N N 286 
MET   C   OXT  sing N N 287 
MET   CB  CG   sing N N 288 
MET   CB  HB2  sing N N 289 
MET   CB  HB3  sing N N 290 
MET   CG  SD   sing N N 291 
MET   CG  HG2  sing N N 292 
MET   CG  HG3  sing N N 293 
MET   SD  CE   sing N N 294 
MET   CE  HE1  sing N N 295 
MET   CE  HE2  sing N N 296 
MET   CE  HE3  sing N N 297 
MET   OXT HXT  sing N N 298 
PHE   N   CA   sing N N 299 
PHE   N   H    sing N N 300 
PHE   N   H2   sing N N 301 
PHE   CA  C    sing N N 302 
PHE   CA  CB   sing N N 303 
PHE   CA  HA   sing N N 304 
PHE   C   O    doub N N 305 
PHE   C   OXT  sing N N 306 
PHE   CB  CG   sing N N 307 
PHE   CB  HB2  sing N N 308 
PHE   CB  HB3  sing N N 309 
PHE   CG  CD1  doub Y N 310 
PHE   CG  CD2  sing Y N 311 
PHE   CD1 CE1  sing Y N 312 
PHE   CD1 HD1  sing N N 313 
PHE   CD2 CE2  doub Y N 314 
PHE   CD2 HD2  sing N N 315 
PHE   CE1 CZ   doub Y N 316 
PHE   CE1 HE1  sing N N 317 
PHE   CE2 CZ   sing Y N 318 
PHE   CE2 HE2  sing N N 319 
PHE   CZ  HZ   sing N N 320 
PHE   OXT HXT  sing N N 321 
PRO   N   CA   sing N N 322 
PRO   N   CD   sing N N 323 
PRO   N   H    sing N N 324 
PRO   CA  C    sing N N 325 
PRO   CA  CB   sing N N 326 
PRO   CA  HA   sing N N 327 
PRO   C   O    doub N N 328 
PRO   C   OXT  sing N N 329 
PRO   CB  CG   sing N N 330 
PRO   CB  HB2  sing N N 331 
PRO   CB  HB3  sing N N 332 
PRO   CG  CD   sing N N 333 
PRO   CG  HG2  sing N N 334 
PRO   CG  HG3  sing N N 335 
PRO   CD  HD2  sing N N 336 
PRO   CD  HD3  sing N N 337 
PRO   OXT HXT  sing N N 338 
SER   N   CA   sing N N 339 
SER   N   H    sing N N 340 
SER   N   H2   sing N N 341 
SER   CA  C    sing N N 342 
SER   CA  CB   sing N N 343 
SER   CA  HA   sing N N 344 
SER   C   O    doub N N 345 
SER   C   OXT  sing N N 346 
SER   CB  OG   sing N N 347 
SER   CB  HB2  sing N N 348 
SER   CB  HB3  sing N N 349 
SER   OG  HG   sing N N 350 
SER   OXT HXT  sing N N 351 
THR   N   CA   sing N N 352 
THR   N   H    sing N N 353 
THR   N   H2   sing N N 354 
THR   CA  C    sing N N 355 
THR   CA  CB   sing N N 356 
THR   CA  HA   sing N N 357 
THR   C   O    doub N N 358 
THR   C   OXT  sing N N 359 
THR   CB  OG1  sing N N 360 
THR   CB  CG2  sing N N 361 
THR   CB  HB   sing N N 362 
THR   OG1 HG1  sing N N 363 
THR   CG2 HG21 sing N N 364 
THR   CG2 HG22 sing N N 365 
THR   CG2 HG23 sing N N 366 
THR   OXT HXT  sing N N 367 
TRP   N   CA   sing N N 368 
TRP   N   H    sing N N 369 
TRP   N   H2   sing N N 370 
TRP   CA  C    sing N N 371 
TRP   CA  CB   sing N N 372 
TRP   CA  HA   sing N N 373 
TRP   C   O    doub N N 374 
TRP   C   OXT  sing N N 375 
TRP   CB  CG   sing N N 376 
TRP   CB  HB2  sing N N 377 
TRP   CB  HB3  sing N N 378 
TRP   CG  CD1  doub Y N 379 
TRP   CG  CD2  sing Y N 380 
TRP   CD1 NE1  sing Y N 381 
TRP   CD1 HD1  sing N N 382 
TRP   CD2 CE2  doub Y N 383 
TRP   CD2 CE3  sing Y N 384 
TRP   NE1 CE2  sing Y N 385 
TRP   NE1 HE1  sing N N 386 
TRP   CE2 CZ2  sing Y N 387 
TRP   CE3 CZ3  doub Y N 388 
TRP   CE3 HE3  sing N N 389 
TRP   CZ2 CH2  doub Y N 390 
TRP   CZ2 HZ2  sing N N 391 
TRP   CZ3 CH2  sing Y N 392 
TRP   CZ3 HZ3  sing N N 393 
TRP   CH2 HH2  sing N N 394 
TRP   OXT HXT  sing N N 395 
TYR   N   CA   sing N N 396 
TYR   N   H    sing N N 397 
TYR   N   H2   sing N N 398 
TYR   CA  C    sing N N 399 
TYR   CA  CB   sing N N 400 
TYR   CA  HA   sing N N 401 
TYR   C   O    doub N N 402 
TYR   C   OXT  sing N N 403 
TYR   CB  CG   sing N N 404 
TYR   CB  HB2  sing N N 405 
TYR   CB  HB3  sing N N 406 
TYR   CG  CD1  doub Y N 407 
TYR   CG  CD2  sing Y N 408 
TYR   CD1 CE1  sing Y N 409 
TYR   CD1 HD1  sing N N 410 
TYR   CD2 CE2  doub Y N 411 
TYR   CD2 HD2  sing N N 412 
TYR   CE1 CZ   doub Y N 413 
TYR   CE1 HE1  sing N N 414 
TYR   CE2 CZ   sing Y N 415 
TYR   CE2 HE2  sing N N 416 
TYR   CZ  OH   sing N N 417 
TYR   OH  HH   sing N N 418 
TYR   OXT HXT  sing N N 419 
VAL   N   CA   sing N N 420 
VAL   N   H    sing N N 421 
VAL   N   H2   sing N N 422 
VAL   CA  C    sing N N 423 
VAL   CA  CB   sing N N 424 
VAL   CA  HA   sing N N 425 
VAL   C   O    doub N N 426 
VAL   C   OXT  sing N N 427 
VAL   CB  CG1  sing N N 428 
VAL   CB  CG2  sing N N 429 
VAL   CB  HB   sing N N 430 
VAL   CG1 HG11 sing N N 431 
VAL   CG1 HG12 sing N N 432 
VAL   CG1 HG13 sing N N 433 
VAL   CG2 HG21 sing N N 434 
VAL   CG2 HG22 sing N N 435 
VAL   CG2 HG23 sing N N 436 
VAL   OXT HXT  sing N N 437 
# 
_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                    7I9U 
_atom_sites.fract_transf_matrix[1][1]   0.023478 
_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]   0.023478 
_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]   0.004623 
_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 
F  
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   ? -21.103 19.033  -7.223  1.00 60.74  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.209 18.085  -7.388  1.00 60.85  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.138 17.405  -8.759  1.00 59.49  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -21.897 18.062  -9.777  1.00 59.59  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.581 18.783  -7.180  1.00 63.41  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.564 18.030  -6.283  1.00 69.45  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.274 18.690  -5.497  1.00 70.35  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.620 16.774  -6.372  1.00 72.25  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.333 16.079  -8.777  1.00 57.79  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.293 15.304  -10.011 1.00 56.41  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.691 15.057  -10.584 1.00 55.32  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.666 15.048  -9.839  1.00 55.25  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.562 13.964  -9.796  1.00 56.11  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.080 14.116  -9.563  1.00 56.44  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.224 12.546  -9.264  1.00 55.25  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.553 13.141  -9.037  1.00 56.23  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.782 14.830  -11.909 1.00 54.27  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.055 14.555  -12.573 1.00 53.65  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.930 13.553  -13.718 1.00 52.59  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.834 13.309  -14.214 1.00 52.31  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.757 15.837  -13.027 1.00 54.10  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -24.984 16.647  -14.041 1.00 55.58  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.031 17.571  -13.640 1.00 56.62  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.246 16.530  -15.400 1.00 56.95  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.296 18.294  -14.566 1.00 57.96  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.533 17.267  -16.338 1.00 57.99  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.570 18.161  -15.914 1.00 59.28  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -22.859 18.897  -16.827 1.00 61.70  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.053 12.955  -14.129 1.00 51.95  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -26.050 11.981  -15.210 1.00 51.80  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.874 12.454  -16.419 1.00 52.52  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.916 13.122  -16.281 1.00 53.38  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.442 10.555  -14.733 1.00 51.52  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.898 10.487  -14.250 1.00 51.90  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.468 10.043  -13.659 1.00 51.62  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.400 9.126   -14.066 1.00 52.67  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.345 12.162  -17.604 1.00 52.13  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -26.937 12.473  -18.905 1.00 52.77  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -26.973 11.186  -19.711 1.00 52.53  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -25.936 10.550  -19.827 1.00 52.60  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.037 13.446  -19.672 1.00 55.31  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.254 14.923  -19.375 1.00 61.02  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.242 15.833  -20.051 1.00 69.25  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.329 15.321  -20.743 1.00 69.64  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.364 17.067  -19.887 1.00 74.22  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.113 10.831  -20.318 1.00 52.24  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.188 9.619   -21.137 1.00 52.71  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.257 9.691   -22.349 1.00 52.83  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.079 10.766  -22.947 1.00 52.83  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.636 9.320   -21.570 1.00 54.53  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -29.896 7.826   -21.755 1.00 58.16  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.370 7.457   -21.867 1.00 61.39  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.513 6.037   -22.193 1.00 64.88  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.538 5.558   -23.435 1.00 68.87  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.489 6.384   -24.474 1.00 69.77  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.616 4.251   -23.649 1.00 68.44  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.637 8.561   -22.696 1.00 52.19  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.751 8.512   -23.858 1.00 52.66  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.119 7.417   -24.883 1.00 53.66  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.469 7.329   -25.922 1.00 54.26  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.295 8.378   -23.432 1.00 52.44  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.135 6.600   -24.597 1.00 53.47  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.560 5.578   -25.540 1.00 54.12  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.130 4.308   -24.954 1.00 54.58  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.253 4.177   -23.740 1.00 54.68  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.520 3.382   -25.846 1.00 54.81  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.087 2.084   -25.514 1.00 55.64  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -27.988 1.054   -25.351 1.00 57.05  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.933 1.162   -25.984 1.00 56.49  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.011 1.603   -26.645 1.00 56.52  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.352 2.288   -26.718 1.00 62.00  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.569 3.251   -25.958 1.00 63.74  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.185 1.876   -27.548 1.00 64.32  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.263 0.015   -24.558 1.00 58.23  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.313 -1.071  -24.406 1.00 59.90  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.715 -2.200  -25.348 1.00 62.30  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.592 -3.008  -25.037 1.00 62.17  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -27.131 -1.460  -22.937 1.00 59.88  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.436 -0.313  -22.207 1.00 60.47  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.350 -2.760  -22.800 1.00 60.28  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.566 -0.385  -20.754 1.00 61.81  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -27.103 -2.205  -26.544 0.50 63.30  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -27.095 -2.218  -26.536 0.50 63.32  ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -27.358 -3.183  -27.602 0.50 64.81  ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -27.384 -3.190  -27.590 0.50 64.83  ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -26.053 -3.673  -28.225 0.50 66.20  ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -26.083 -3.657  -28.259 0.50 66.23  ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -25.072 -2.931  -28.284 0.50 66.29  ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -25.120 -2.895  -28.347 0.50 66.34  ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -28.203 -2.555  -28.730 0.50 66.01  ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -28.325 -2.555  -28.643 0.50 66.01  ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -27.523 -1.417  -29.269 0.50 66.95  ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -29.416 -1.901  -27.996 0.50 66.85  ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -29.601 -2.173  -28.283 0.50 66.34  ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -28.866 -3.563  -29.639 0.50 66.38  ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -26.057 -4.903  -28.737 1.00 67.09  ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -24.898 -5.444  -29.437 1.00 69.37  ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -24.989 -4.886  -30.884 1.00 72.30  ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -26.067 -4.907  -31.480 1.00 72.00  ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -24.981 -6.985  -29.431 1.00 69.32  ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -23.929 -7.722  -30.226 1.00 70.20  ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -24.049 -8.194  -31.504 1.00 71.15  ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -22.665 -8.201  -29.741 1.00 70.27  ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -22.908 -8.873  -31.866 1.00 71.44  ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -22.048 -8.903  -30.798 1.00 71.19  ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -21.966 -8.055  -28.535 1.00 70.39  ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -20.782 -9.477  -30.670 1.00 71.61  ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -20.722 -8.636  -28.409 1.00 70.89  ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -20.139 -9.329  -29.465 1.00 71.17  ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -23.892 -4.328  -31.425 1.00 74.72  ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -23.889 -3.832  -32.803 1.00 77.07  ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -23.213 -4.858  -33.695 1.00 79.39  ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -22.006 -5.050  -33.587 1.00 79.26  ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -23.155 -2.483  -32.959 1.00 79.77  ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -23.247 -1.952  -34.391 1.00 86.38  ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -22.118 -1.078  -34.920 1.00 94.21  ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -21.236 -0.690  -34.119 1.00 96.75  ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -22.119 -0.781  -36.138 1.00 95.50  ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -23.970 -5.495  -34.596 1.00 81.35  ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -23.387 -6.445  -35.538 1.00 83.84  ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -22.536 -5.649  -36.528 1.00 86.16  ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -22.928 -4.546  -36.910 1.00 86.93  ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -24.489 -7.211  -36.276 1.00 86.58  ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -24.292 -8.718  -36.256 1.00 91.86  ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -24.297 -9.320  -37.661 1.00 96.67  ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -24.169 -10.825 -37.636 1.00 100.49 ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -24.419 -11.418 -38.977 1.00 103.27 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -21.363 -6.166  -36.899 1.00 87.42  ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -20.456 -5.456  -37.806 1.00 89.18  ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -19.877 -4.187  -37.163 1.00 89.68  ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -19.877 -3.116  -37.765 1.00 89.91  ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -21.101 -5.160  -39.177 1.00 92.64  ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -21.175 -6.361  -40.101 1.00 100.51 ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -20.251 -7.217  -40.045 1.00 102.25 ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -22.147 -6.442  -40.892 1.00 103.17 ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -19.404 -4.310  -35.926 1.00 89.74  ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -18.761 -3.199  -35.229 1.00 89.88  ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -17.228 -3.256  -35.517 1.00 89.71  ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -16.752 -4.227  -36.107 1.00 89.80  ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -19.041 -3.307  -33.731 1.00 90.00  ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -16.469 -2.212  -35.152 1.00 89.34  ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -15.025 -2.194  -35.367 1.00 89.41  ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -14.328 -3.205  -34.420 1.00 88.54  ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -14.312 -2.990  -33.212 1.00 88.18  ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -14.495 -0.771  -35.140 1.00 92.55  ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -12.996 -0.625  -35.324 1.00 99.39  ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -12.368 0.516   -34.545 1.00 108.44 ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -13.118 1.349   -33.982 1.00 110.29 ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -11.117 0.570   -34.491 1.00 111.20 ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -13.772 -4.310  -34.978 1.00 87.84  ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -13.106 -5.364  -34.204 1.00 87.48  ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -11.621 -5.106  -34.004 1.00 87.00  ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -10.832 -5.450  -34.865 1.00 87.39  ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -13.320 -6.795  -34.762 1.00 88.15  ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -12.971 -7.830  -33.704 1.00 88.61  ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -14.745 -7.006  -35.257 1.00 88.63  ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -11.230 -4.551  -32.860 1.00 86.50  ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -9.820  -4.288  -32.562 1.00 86.29  ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -9.465  -4.745  -31.136 1.00 85.54  ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -10.357 -5.044  -30.349 1.00 85.65  ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -9.503  -2.800  -32.801 1.00 87.80  ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -8.087  -2.608  -32.820 1.00 89.08  ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -10.132 -1.900  -31.767 1.00 87.74  ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -8.176  -4.829  -30.821 1.00 84.55  ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -7.738  -5.209  -29.485 1.00 83.94  ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -7.121  -6.584  -29.338 1.00 82.82  ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -7.613  -7.565  -29.895 1.00 82.67  ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -6.062  -6.666  -28.534 1.00 81.74  ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -5.385  -7.925  -28.257 1.00 81.00  ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -5.934  -8.618  -26.965 1.00 79.14  ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -6.724  -8.015  -26.234 1.00 78.89  ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -3.860  -7.719  -28.238 1.00 82.70  ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -3.318  -7.115  -26.964 1.00 86.84  ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.731  -6.033  -26.527 1.00 88.19  ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -2.368  -7.804  -26.342 1.00 87.67  ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -5.558  -9.898  -26.718 1.00 77.54  ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -6.010  -10.677 -25.549 1.00 76.38  ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -4.820  -11.128 -24.673 1.00 75.29  ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -4.409  -12.288 -24.744 1.00 75.65  ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -6.806  -11.908 -25.990 1.00 77.26  ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -7.611  -11.708 -27.136 1.00 79.40  ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -4.247  -10.244 -23.841 1.00 74.06  ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -3.080  -10.656 -23.040 1.00 73.29  ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -3.401  -11.442 -21.774 1.00 72.51  ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -4.426  -11.202 -21.145 1.00 72.38  ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -2.385  -9.333  -22.729 1.00 74.14  ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -3.492  -8.309  -22.743 1.00 74.67  ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -4.595  -8.822  -23.625 1.00 73.30  ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -2.519  -12.379 -21.395 1.00 71.93  ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -2.661  -13.149 -20.152 1.00 71.98  ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -1.685  -12.520 -19.157 1.00 70.13  ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.477  -12.647 -19.317 1.00 70.49  ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -2.351  -14.643 -20.370 1.00 75.18  ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -3.301  -15.316 -21.365 1.00 81.11  ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -3.128  -16.830 -21.408 1.00 86.20  ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -3.882  -17.456 -22.501 1.00 90.40  ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -5.149  -17.854 -22.410 1.00 92.93  ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -5.824  -17.692 -21.277 1.00 92.98  ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -5.749  -18.418 -23.451 1.00 92.31  ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -2.205  -11.778 -18.185 1.00 68.44  ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -1.382  -11.031 -17.240 1.00 67.22  ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -1.533  -11.477 -15.791 1.00 65.76  ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -2.655  -11.656 -15.330 1.00 65.79  ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -1.763  -9.545  -17.324 1.00 67.11  ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.617  -8.901  -18.682 1.00 68.27  ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -2.211  -7.517  -18.684 1.00 68.80  ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? -0.161  -8.865  -19.101 1.00 68.69  ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? -0.412  -11.576 -15.053 1.00 64.21  ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? -0.461  -11.908 -13.637 1.00 63.74  ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.617  -10.628 -12.834 1.00 61.74  ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? 0.247   -9.753  -12.889 1.00 62.15  ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 0.781   -12.692 -13.203 1.00 67.07  ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 0.673   -14.152 -13.578 1.00 75.01  ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? 0.107   -14.447 -14.656 1.00 77.31  ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 1.129   -15.001 -12.790 1.00 78.17  ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -1.748  -10.482 -12.139 1.00 59.61  ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -2.029  -9.250  -11.408 1.00 58.28  ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -2.372  -9.489  -9.932  1.00 57.00  ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.687  -10.611 -9.538  1.00 57.61  ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -3.122  -8.383  -12.118 1.00 58.22  ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -2.771  -8.099  -13.578 1.00 58.52  ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -4.500  -9.021  -11.993 1.00 58.21  ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -2.284  -8.432  -9.114  1.00 55.32  ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.634  -8.487  -7.698  1.00 54.51  ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.607  -7.354  -7.399  1.00 53.61  ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -3.453  -6.261  -7.935  1.00 53.99  ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -1.394  -8.361  -6.830  1.00 54.33  ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.632  -7.621  -6.581  1.00 52.40  ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.641  -6.626  -6.212  1.00 51.28  ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -5.475  -6.269  -4.727  1.00 51.31  ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.566  -7.149  -3.859  1.00 51.73  ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -7.046  -7.195  -6.486  1.00 50.45  ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -8.232  -6.280  -6.184  1.00 50.41  ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -8.199  -5.032  -7.041  1.00 50.02  ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.545  -7.020  -6.352  1.00 50.48  ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -5.183  -5.000  -4.433  1.00 50.94  ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -5.003  -4.580  -3.045  1.00 51.32  ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -6.349  -4.162  -2.391  1.00 52.06  ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -7.386  -4.140  -3.054  1.00 52.26  ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.881  -3.518  -2.897  1.00 52.25  ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -4.162  -2.130  -3.434  1.00 56.13  ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.349  -1.824  -3.709  1.00 57.14  ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.199  -1.341  -3.569  1.00 57.41  ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -6.326  -3.877  -1.083  1.00 52.47  ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.486  -3.471  -0.304  1.00 53.11  ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -8.155  -2.196  -0.833  1.00 53.57  ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -9.325  -1.959  -0.546  1.00 53.40  ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -7.049  -3.262  1.148   1.00 55.92  ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -8.201  -3.234  2.137   1.00 61.12  ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.777  -3.116  3.582   1.00 66.60  ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.431  -1.991  4.011   1.00 68.36  ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.782  -4.153  4.283   1.00 68.66  ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.433  -1.395  -1.632  1.00 53.60  ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.956  -0.152  -2.176  1.00 53.85  ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.548  -0.262  -3.581  1.00 53.60  ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.915  0.763   -4.157  1.00 54.16  ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.869  0.912   -2.155  1.00 55.65  ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.328  1.022   -0.849  1.00 58.91  ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.643  -1.474  -4.128  1.00 52.72  ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -9.181  -1.687  -5.470  1.00 52.01  ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.209  -1.310  -6.578  1.00 51.56  ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.621  -0.973  -7.690  1.00 51.65  ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.901  -1.353  -6.284  1.00 50.50  ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -5.879  -1.000  -7.257  1.00 49.66  ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.153  -2.260  -7.726  1.00 49.70  ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.594  -3.003  -6.910  1.00 49.41  ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.867  0.010   -6.662  1.00 49.62  ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.485  1.311   -6.180  1.00 51.68  ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.443  1.767   -6.797  1.00 51.10  ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -5.006  1.860   -5.178  1.00 54.57  ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -5.196  -2.516  -9.037  1.00 49.45  ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.503  -3.647  -9.616  1.00 49.96  ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -3.044  -3.273  -9.846  1.00 52.35  ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.702  -2.108  -10.059 1.00 52.34  ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -5.141  -4.082  -10.941 1.00 48.84  ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.473  -4.787  -10.818 1.00 48.40  ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.542  -6.107  -10.406 1.00 48.50  ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.656  -4.134  -11.134 1.00 48.14  ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -7.768  -6.757  -10.318 1.00 48.56  ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -8.873  -4.793  -11.058 1.00 48.02  ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -8.923  -6.096  -10.650 1.00 47.71  ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -2.183  -4.260  -9.761  1.00 54.23  ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -0.762  -4.080  -10.004 1.00 57.38  ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? -0.238  -5.291  -10.767 1.00 60.87  ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -0.899  -6.331  -10.780 1.00 60.78  ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? -0.001  -3.903  -8.689  1.00 58.68  ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? -0.348  -4.886  -7.727  1.00 60.73  ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 0.939   -5.171  -11.410 1.00 63.61  ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.509   -6.312  -12.121 1.00 66.54  ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.464   -7.090  -11.254 1.00 69.37  ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 3.390   -6.523  -10.663 1.00 69.76  ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.182   -5.901  -13.430 1.00 67.17  ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 1.223   -5.630  -14.569 1.00 69.48  ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 1.956   -5.119  -15.771 1.00 69.97  ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 0.442   -6.886  -14.945 1.00 70.69  ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 2.253   -8.401  -11.189 1.00 71.30  ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 3.121   -9.292  -10.425 1.00 73.44  ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 4.156   -9.887  -11.378 1.00 75.92  ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.795   -10.302 -12.484 1.00 76.44  ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 2.288   -10.402 -9.754  1.00 74.03  ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 3.172   -11.335 -8.935  1.00 74.78  ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 1.183   -9.806  -8.897  1.00 74.22  ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.436   -9.907  -10.983 1.00 77.34  ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.477   -10.482 -11.840 1.00 79.36  ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 7.430   -11.419 -11.080 1.00 80.46  ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 6.997   -12.372 -10.430 1.00 80.96  ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 7.264   -9.385  -12.584 1.00 82.51  ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 6.431   -8.488  -13.492 1.00 87.38  ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 6.099   -9.068  -14.853 1.00 92.53  ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 7.034   -9.509  -15.564 1.00 92.11  ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 4.898   -9.074  -15.209 1.00 94.64  ? 88  GLU   A OE2 1 
ATOM   312  N  N   . GLY   B 2 7   ? -35.477 11.646  -11.596 1.00 73.69  ? 16  GLY   B N   1 
ATOM   313  C  CA  . GLY   B 2 7   ? -35.844 12.132  -12.923 1.00 74.11  ? 16  GLY   B CA  1 
ATOM   314  C  C   . GLY   B 2 7   ? -35.770 11.075  -14.017 1.00 74.24  ? 16  GLY   B C   1 
ATOM   315  O  O   . GLY   B 2 7   ? -36.732 10.329  -14.228 1.00 74.69  ? 16  GLY   B O   1 
ATOM   316  N  N   . GLU   B 2 8   ? -34.624 11.004  -14.735 1.00 73.34  ? 17  GLU   B N   1 
ATOM   317  C  CA  . GLU   B 2 8   ? -34.432 10.034  -15.818 1.00 72.77  ? 17  GLU   B CA  1 
ATOM   318  C  C   . GLU   B 2 8   ? -34.194 8.608   -15.289 1.00 71.54  ? 17  GLU   B C   1 
ATOM   319  O  O   . GLU   B 2 8   ? -33.145 8.308   -14.716 1.00 71.53  ? 17  GLU   B O   1 
ATOM   320  C  CB  . GLU   B 2 8   ? -33.328 10.485  -16.790 1.00 74.98  ? 17  GLU   B CB  1 
ATOM   321  C  CG  . GLU   B 2 8   ? -33.553 9.978   -18.206 1.00 80.07  ? 17  GLU   B CG  1 
ATOM   322  C  CD  . GLU   B 2 8   ? -32.617 10.533  -19.264 1.00 87.41  ? 17  GLU   B CD  1 
ATOM   323  O  OE1 . GLU   B 2 8   ? -31.739 11.361  -18.923 1.00 88.10  ? 17  GLU   B OE1 1 
ATOM   324  O  OE2 . GLU   B 2 8   ? -32.782 10.155  -20.447 1.00 90.37  ? 17  GLU   B OE2 1 
ATOM   325  N  N   . THR   B 2 9   ? -35.205 7.748   -15.457 1.00 70.28  ? 18  THR   B N   1 
ATOM   326  C  CA  . THR   B 2 9   ? -35.223 6.357   -14.994 1.00 69.23  ? 18  THR   B CA  1 
ATOM   327  C  C   . THR   B 2 9   ? -34.967 5.330   -16.108 1.00 67.03  ? 18  THR   B C   1 
ATOM   328  O  O   . THR   B 2 9   ? -34.875 4.141   -15.814 1.00 67.38  ? 18  THR   B O   1 
ATOM   329  C  CB  . THR   B 2 9   ? -36.609 6.059   -14.366 1.00 71.45  ? 18  THR   B CB  1 
ATOM   330  O  OG1 . THR   B 2 9   ? -37.618 6.116   -15.386 1.00 72.80  ? 18  THR   B OG1 1 
ATOM   331  C  CG2 . THR   B 2 9   ? -36.977 7.031   -13.243 1.00 72.02  ? 18  THR   B CG2 1 
ATOM   332  N  N   . THR   B 2 10  ? -34.917 5.777   -17.375 1.00 64.72  ? 19  THR   B N   1 
ATOM   333  C  CA  . THR   B 2 10  ? -34.777 4.948   -18.562 1.00 63.07  ? 19  THR   B CA  1 
ATOM   334  C  C   . THR   B 2 10  ? -33.555 4.045   -18.524 1.00 60.73  ? 19  THR   B C   1 
ATOM   335  O  O   . THR   B 2 10  ? -32.463 4.527   -18.231 1.00 60.67  ? 19  THR   B O   1 
ATOM   336  C  CB  . THR   B 2 10  ? -34.680 5.838   -19.829 1.00 64.88  ? 19  THR   B CB  1 
ATOM   337  O  OG1 . THR   B 2 10  ? -35.609 6.921   -19.774 1.00 67.02  ? 19  THR   B OG1 1 
ATOM   338  C  CG2 . THR   B 2 10  ? -34.887 5.049   -21.116 1.00 65.00  ? 19  THR   B CG2 1 
ATOM   339  N  N   . ASP   B 2 11  ? -33.704 2.758   -18.911 1.00 58.47  ? 20  ASP   B N   1 
ATOM   340  C  CA  . ASP   B 2 11  ? -32.555 1.859   -19.008 1.00 57.17  ? 20  ASP   B CA  1 
ATOM   341  C  C   . ASP   B 2 11  ? -31.594 2.387   -20.089 1.00 55.38  ? 20  ASP   B C   1 
ATOM   342  O  O   . ASP   B 2 11  ? -32.042 3.016   -21.048 1.00 55.45  ? 20  ASP   B O   1 
ATOM   343  C  CB  . ASP   B 2 11  ? -33.007 0.441   -19.404 1.00 59.41  ? 20  ASP   B CB  1 
ATOM   344  C  CG  . ASP   B 2 11  ? -33.598 -0.383  -18.283 1.00 63.83  ? 20  ASP   B CG  1 
ATOM   345  O  OD1 . ASP   B 2 11  ? -34.229 0.206   -17.390 1.00 63.85  ? 20  ASP   B OD1 1 
ATOM   346  O  OD2 . ASP   B 2 11  ? -33.441 -1.628  -18.313 1.00 66.60  ? 20  ASP   B OD2 1 
ATOM   347  N  N   . GLY   B 2 12  ? -30.295 2.144   -19.928 1.00 53.63  ? 21  GLY   B N   1 
ATOM   348  C  CA  . GLY   B 2 12  ? -29.317 2.601   -20.905 1.00 52.26  ? 21  GLY   B CA  1 
ATOM   349  C  C   . GLY   B 2 12  ? -27.981 2.991   -20.319 1.00 50.71  ? 21  GLY   B C   1 
ATOM   350  O  O   . GLY   B 2 12  ? -27.735 2.776   -19.141 1.00 50.38  ? 21  GLY   B O   1 
ATOM   351  N  N   . VAL   B 2 13  ? -27.086 3.526   -21.159 1.00 49.66  ? 22  VAL   B N   1 
ATOM   352  C  CA  . VAL   B 2 13  ? -25.757 3.947   -20.735 1.00 48.82  ? 22  VAL   B CA  1 
ATOM   353  C  C   . VAL   B 2 13  ? -25.776 5.466   -20.492 1.00 48.58  ? 22  VAL   B C   1 
ATOM   354  O  O   . VAL   B 2 13  ? -26.476 6.188   -21.206 1.00 49.18  ? 22  VAL   B O   1 
ATOM   355  C  CB  . VAL   B 2 13  ? -24.661 3.458   -21.717 1.00 49.03  ? 22  VAL   B CB  1 
ATOM   356  C  CG1 . VAL   B 2 13  ? -24.786 4.105   -23.088 1.00 49.57  ? 22  VAL   B CG1 1 
ATOM   357  C  CG2 . VAL   B 2 13  ? -23.262 3.633   -21.140 1.00 48.93  ? 22  VAL   B CG2 1 
ATOM   358  N  N   . TYR   B 2 14  ? -25.160 5.930   -19.387 1.00 47.07  ? 23  TYR   B N   1 
ATOM   359  C  CA  . TYR   B 2 14  ? -25.188 7.349   -19.026 1.00 46.20  ? 23  TYR   B CA  1 
ATOM   360  C  C   . TYR   B 2 14  ? -23.788 7.906   -18.815 1.00 45.96  ? 23  TYR   B C   1 
ATOM   361  O  O   . TYR   B 2 14  ? -22.875 7.174   -18.478 1.00 46.18  ? 23  TYR   B O   1 
ATOM   362  C  CB  . TYR   B 2 14  ? -26.015 7.582   -17.724 1.00 45.33  ? 23  TYR   B CB  1 
ATOM   363  C  CG  . TYR   B 2 14  ? -27.509 7.424   -17.881 1.00 44.86  ? 23  TYR   B CG  1 
ATOM   364  C  CD1 . TYR   B 2 14  ? -28.072 6.188   -18.155 1.00 45.51  ? 23  TYR   B CD1 1 
ATOM   365  C  CD2 . TYR   B 2 14  ? -28.362 8.498   -17.704 1.00 46.10  ? 23  TYR   B CD2 1 
ATOM   366  C  CE1 . TYR   B 2 14  ? -29.440 6.041   -18.331 1.00 46.12  ? 23  TYR   B CE1 1 
ATOM   367  C  CE2 . TYR   B 2 14  ? -29.737 8.362   -17.861 1.00 47.00  ? 23  TYR   B CE2 1 
ATOM   368  C  CZ  . TYR   B 2 14  ? -30.272 7.130   -18.187 1.00 47.45  ? 23  TYR   B CZ  1 
ATOM   369  O  OH  . TYR   B 2 14  ? -31.630 6.972   -18.328 1.00 48.86  ? 23  TYR   B OH  1 
ATOM   370  N  N   . ARG   B 2 15  ? -23.626 9.205   -18.992 1.00 45.62  ? 24  ARG   B N   1 
ATOM   371  C  CA  . ARG   B 2 15  ? -22.378 9.885   -18.699 1.00 45.98  ? 24  ARG   B CA  1 
ATOM   372  C  C   . ARG   B 2 15  ? -22.496 10.410  -17.271 1.00 46.11  ? 24  ARG   B C   1 
ATOM   373  O  O   . ARG   B 2 15  ? -23.580 10.776  -16.843 1.00 46.13  ? 24  ARG   B O   1 
ATOM   374  C  CB  . ARG   B 2 15  ? -22.165 11.076  -19.644 1.00 47.42  ? 24  ARG   B CB  1 
ATOM   375  C  CG  . ARG   B 2 15  ? -22.148 10.705  -21.107 1.00 49.65  ? 24  ARG   B CG  1 
ATOM   376  C  CD  . ARG   B 2 15  ? -21.861 11.914  -21.970 1.00 52.70  ? 24  ARG   B CD  1 
ATOM   377  N  NE  . ARG   B 2 15  ? -22.143 11.593  -23.364 1.00 56.29  ? 24  ARG   B NE  1 
ATOM   378  C  CZ  . ARG   B 2 15  ? -21.236 11.196  -24.247 1.00 58.72  ? 24  ARG   B CZ  1 
ATOM   379  N  NH1 . ARG   B 2 15  ? -19.950 11.139  -23.911 1.00 57.80  ? 24  ARG   B NH1 1 
ATOM   380  N  NH2 . ARG   B 2 15  ? -21.600 10.889  -25.485 1.00 59.35  ? 24  ARG   B NH2 1 
ATOM   381  N  N   . VAL   B 2 16  ? -21.389 10.448  -16.535 1.00 45.97  ? 25  VAL   B N   1 
ATOM   382  C  CA  . VAL   B 2 16  ? -21.332 10.965  -15.169 1.00 45.81  ? 25  VAL   B CA  1 
ATOM   383  C  C   . VAL   B 2 16  ? -20.478 12.219  -15.278 1.00 46.57  ? 25  VAL   B C   1 
ATOM   384  O  O   . VAL   B 2 16  ? -19.297 12.140  -15.602 1.00 46.21  ? 25  VAL   B O   1 
ATOM   385  C  CB  . VAL   B 2 16  ? -20.740 9.923   -14.177 1.00 45.69  ? 25  VAL   B CB  1 
ATOM   386  C  CG1 . VAL   B 2 16  ? -20.814 10.416  -12.734 1.00 45.68  ? 25  VAL   B CG1 1 
ATOM   387  C  CG2 . VAL   B 2 16  ? -21.429 8.572   -14.330 1.00 45.60  ? 25  VAL   B CG2 1 
ATOM   388  N  N   . MET   B 2 17  ? -21.112 13.371  -15.121 1.00 47.73  ? 26  MET   B N   1 
ATOM   389  C  CA  . MET   B 2 17  ? -20.511 14.683  -15.285 1.00 49.77  ? 26  MET   B CA  1 
ATOM   390  C  C   . MET   B 2 17  ? -20.384 15.445  -13.963 1.00 52.56  ? 26  MET   B C   1 
ATOM   391  O  O   . MET   B 2 17  ? -21.086 15.144  -13.002 1.00 52.69  ? 26  MET   B O   1 
ATOM   392  C  CB  . MET   B 2 17  ? -21.398 15.540  -16.227 1.00 49.91  ? 26  MET   B CB  1 
ATOM   393  C  CG  . MET   B 2 17  ? -21.914 14.834  -17.465 1.00 50.22  ? 26  MET   B CG  1 
ATOM   394  S  SD  . MET   B 2 17  ? -20.613 14.564  -18.671 1.00 52.42  ? 26  MET   B SD  1 
ATOM   395  C  CE  . MET   B 2 17  ? -20.202 16.255  -19.067 1.00 43.49  ? 26  MET   B CE  1 
ATOM   396  N  N   . THR   B 2 18  ? -19.520 16.468  -13.935 1.00 54.77  ? 27  THR   B N   1 
ATOM   397  C  CA  . THR   B 2 18  ? -19.351 17.352  -12.785 1.00 57.88  ? 27  THR   B CA  1 
ATOM   398  C  C   . THR   B 2 18  ? -19.154 18.805  -13.262 1.00 60.53  ? 27  THR   B C   1 
ATOM   399  O  O   . THR   B 2 18  ? -18.579 19.044  -14.331 1.00 60.30  ? 27  THR   B O   1 
ATOM   400  C  CB  . THR   B 2 18  ? -18.230 16.863  -11.839 1.00 60.10  ? 27  THR   B CB  1 
ATOM   401  O  OG1 . THR   B 2 18  ? -18.403 17.478  -10.557 1.00 61.90  ? 27  THR   B OG1 1 
ATOM   402  C  CG2 . THR   B 2 18  ? -16.826 17.157  -12.370 1.00 60.35  ? 27  THR   B CG2 1 
ATOM   403  N  N   . ARG   B 2 19  ? -19.664 19.773  -12.495 1.00 62.72  ? 28  ARG   B N   1 
ATOM   404  C  CA  . ARG   B 2 19  ? -19.479 21.187  -12.846 1.00 65.38  ? 28  ARG   B CA  1 
ATOM   405  C  C   . ARG   B 2 19  ? -18.453 21.904  -11.925 1.00 67.02  ? 28  ARG   B C   1 
ATOM   406  O  O   . ARG   B 2 19  ? -18.296 23.121  -12.014 1.00 67.42  ? 28  ARG   B O   1 
ATOM   407  C  CB  . ARG   B 2 19  ? -20.832 21.928  -12.909 1.00 67.69  ? 28  ARG   B CB  1 
ATOM   408  C  CG  . ARG   B 2 19  ? -21.689 21.485  -14.096 1.00 72.55  ? 28  ARG   B CG  1 
ATOM   409  C  CD  . ARG   B 2 19  ? -22.581 22.598  -14.632 1.00 78.03  ? 28  ARG   B CD  1 
ATOM   410  N  NE  . ARG   B 2 19  ? -23.549 22.132  -15.635 1.00 82.61  ? 28  ARG   B NE  1 
ATOM   411  C  CZ  . ARG   B 2 19  ? -24.755 21.640  -15.346 1.00 85.50  ? 28  ARG   B CZ  1 
ATOM   412  N  NH1 . ARG   B 2 19  ? -25.147 21.518  -14.080 1.00 85.17  ? 28  ARG   B NH1 1 
ATOM   413  N  NH2 . ARG   B 2 19  ? -25.569 21.246  -16.320 1.00 85.14  ? 28  ARG   B NH2 1 
ATOM   414  N  N   . ARG   B 2 20  ? -17.740 21.134  -11.073 1.00 68.09  ? 29  ARG   B N   1 
ATOM   415  C  CA  . ARG   B 2 20  ? -16.753 21.597  -10.095 1.00 69.57  ? 29  ARG   B CA  1 
ATOM   416  C  C   . ARG   B 2 20  ? -15.490 22.153  -10.747 1.00 69.46  ? 29  ARG   B C   1 
ATOM   417  O  O   . ARG   B 2 20  ? -15.045 23.249  -10.387 1.00 69.85  ? 29  ARG   B O   1 
ATOM   418  C  CB  . ARG   B 2 20  ? -16.406 20.465  -9.102  1.00 72.35  ? 29  ARG   B CB  1 
ATOM   419  C  CG  . ARG   B 2 20  ? -15.490 20.912  -7.972  1.00 77.68  ? 29  ARG   B CG  1 
ATOM   420  C  CD  . ARG   B 2 20  ? -15.119 19.767  -7.043  1.00 82.73  ? 29  ARG   B CD  1 
ATOM   421  N  NE  . ARG   B 2 20  ? -13.950 19.005  -7.495  1.00 87.25  ? 29  ARG   B NE  1 
ATOM   422  C  CZ  . ARG   B 2 20  ? -12.688 19.306  -7.184  1.00 90.48  ? 29  ARG   B CZ  1 
ATOM   423  N  NH1 . ARG   B 2 20  ? -12.414 20.382  -6.455  1.00 90.28  ? 29  ARG   B NH1 1 
ATOM   424  N  NH2 . ARG   B 2 20  ? -11.691 18.543  -7.619  1.00 90.61  ? 29  ARG   B NH2 1 
ATOM   425  N  N   . LEU   B 2 21  ? -14.936 21.432  -11.732 1.00 68.59  ? 30  LEU   B N   1 
ATOM   426  C  CA  . LEU   B 2 21  ? -13.736 21.882  -12.442 1.00 68.44  ? 30  LEU   B CA  1 
ATOM   427  C  C   . LEU   B 2 21  ? -14.093 22.959  -13.525 1.00 68.09  ? 30  LEU   B C   1 
ATOM   428  O  O   . LEU   B 2 21  ? -15.119 23.637  -13.391 1.00 68.53  ? 30  LEU   B O   1 
ATOM   429  C  CB  . LEU   B 2 21  ? -13.004 20.653  -13.032 1.00 68.74  ? 30  LEU   B CB  1 
ATOM   430  C  CG  . LEU   B 2 21  ? -12.744 19.495  -12.061 1.00 70.43  ? 30  LEU   B CG  1 
ATOM   431  C  CD1 . LEU   B 2 21  ? -12.031 18.344  -12.755 1.00 71.03  ? 30  LEU   B CD1 1 
ATOM   432  C  CD2 . LEU   B 2 21  ? -11.945 19.954  -10.855 1.00 71.20  ? 30  LEU   B CD2 1 
ATOM   433  N  N   . LEU   B 2 22  ? -13.245 23.159  -14.556 1.00 66.99  ? 31  LEU   B N   1 
ATOM   434  C  CA  . LEU   B 2 22  ? -13.538 24.127  -15.613 1.00 66.39  ? 31  LEU   B CA  1 
ATOM   435  C  C   . LEU   B 2 22  ? -14.637 23.545  -16.502 1.00 65.49  ? 31  LEU   B C   1 
ATOM   436  O  O   . LEU   B 2 22  ? -14.570 22.353  -16.843 1.00 66.12  ? 31  LEU   B O   1 
ATOM   437  C  CB  . LEU   B 2 22  ? -12.286 24.359  -16.448 1.00 66.47  ? 31  LEU   B CB  1 
ATOM   438  C  CG  . LEU   B 2 22  ? -12.408 25.446  -17.464 1.00 67.79  ? 31  LEU   B CG  1 
ATOM   439  C  CD1 . LEU   B 2 22  ? -11.994 26.780  -16.878 1.00 68.13  ? 31  LEU   B CD1 1 
ATOM   440  C  CD2 . LEU   B 2 22  ? -11.609 25.103  -18.698 1.00 68.58  ? 31  LEU   B CD2 1 
ATOM   441  N  N   . GLY   B 2 23  ? -15.652 24.358  -16.820 1.00 63.53  ? 32  GLY   B N   1 
ATOM   442  C  CA  . GLY   B 2 23  ? -16.798 23.937  -17.625 1.00 62.25  ? 32  GLY   B CA  1 
ATOM   443  C  C   . GLY   B 2 23  ? -17.477 22.678  -17.113 1.00 60.33  ? 32  GLY   B C   1 
ATOM   444  O  O   . GLY   B 2 23  ? -17.597 22.482  -15.902 1.00 60.02  ? 32  GLY   B O   1 
ATOM   445  N  N   . SER   B 2 24  ? -17.878 21.790  -18.028 1.00 59.08  ? 33  SER   B N   1 
ATOM   446  C  CA  . SER   B 2 24  ? -18.452 20.492  -17.649 1.00 58.30  ? 33  SER   B CA  1 
ATOM   447  C  C   . SER   B 2 24  ? -17.394 19.416  -17.947 1.00 56.49  ? 33  SER   B C   1 
ATOM   448  O  O   . SER   B 2 24  ? -16.773 19.442  -19.008 1.00 55.75  ? 33  SER   B O   1 
ATOM   449  C  CB  . SER   B 2 24  ? -19.741 20.213  -18.422 1.00 60.04  ? 33  SER   B CB  1 
ATOM   450  O  OG  . SER   B 2 24  ? -20.712 21.229  -18.213 1.00 62.92  ? 33  SER   B OG  1 
ATOM   451  N  N   . THR   B 2 25  ? -17.159 18.497  -17.004 1.00 55.82  ? 34  THR   B N   1 
ATOM   452  C  CA  . THR   B 2 25  ? -16.160 17.443  -17.175 1.00 55.21  ? 34  THR   B CA  1 
ATOM   453  C  C   . THR   B 2 25  ? -16.783 16.055  -16.993 1.00 54.02  ? 34  THR   B C   1 
ATOM   454  O  O   . THR   B 2 25  ? -17.493 15.835  -16.015 1.00 54.12  ? 34  THR   B O   1 
ATOM   455  C  CB  . THR   B 2 25  ? -15.014 17.671  -16.167 1.00 56.68  ? 34  THR   B CB  1 
ATOM   456  O  OG1 . THR   B 2 25  ? -14.280 18.840  -16.531 1.00 58.02  ? 34  THR   B OG1 1 
ATOM   457  C  CG2 . THR   B 2 25  ? -14.072 16.474  -16.048 1.00 56.99  ? 34  THR   B CG2 1 
ATOM   458  N  N   . GLN   B 2 26  ? -16.501 15.112  -17.907 1.00 52.70  ? 35  GLN   B N   1 
ATOM   459  C  CA  . GLN   B 2 26  ? -16.990 13.744  -17.755 1.00 51.63  ? 35  GLN   B CA  1 
ATOM   460  C  C   . GLN   B 2 26  ? -15.992 12.938  -16.925 1.00 51.80  ? 35  GLN   B C   1 
ATOM   461  O  O   . GLN   B 2 26  ? -14.853 12.709  -17.352 1.00 52.23  ? 35  GLN   B O   1 
ATOM   462  C  CB  . GLN   B 2 26  ? -17.235 13.071  -19.102 1.00 51.16  ? 35  GLN   B CB  1 
ATOM   463  C  CG  . GLN   B 2 26  ? -17.698 11.639  -18.956 1.00 50.99  ? 35  GLN   B CG  1 
ATOM   464  C  CD  . GLN   B 2 26  ? -18.035 11.054  -20.281 1.00 51.49  ? 35  GLN   B CD  1 
ATOM   465  O  OE1 . GLN   B 2 26  ? -18.641 11.706  -21.121 1.00 51.87  ? 35  GLN   B OE1 1 
ATOM   466  N  NE2 . GLN   B 2 26  ? -17.628 9.818   -20.501 1.00 51.54  ? 35  GLN   B NE2 1 
ATOM   467  N  N   . VAL   B 2 27  ? -16.428 12.520  -15.730 1.00 50.76  ? 36  VAL   B N   1 
ATOM   468  C  CA  . VAL   B 2 27  ? -15.614 11.776  -14.763 1.00 49.93  ? 36  VAL   B CA  1 
ATOM   469  C  C   . VAL   B 2 27  ? -15.728 10.235  -14.918 1.00 48.95  ? 36  VAL   B C   1 
ATOM   470  O  O   . VAL   B 2 27  ? -14.829 9.481   -14.526 1.00 48.78  ? 36  VAL   B O   1 
ATOM   471  C  CB  . VAL   B 2 27  ? -15.956 12.268  -13.326 1.00 50.42  ? 36  VAL   B CB  1 
ATOM   472  C  CG1 . VAL   B 2 27  ? -15.750 13.770  -13.218 1.00 50.95  ? 36  VAL   B CG1 1 
ATOM   473  C  CG2 . VAL   B 2 27  ? -17.383 11.922  -12.930 1.00 50.25  ? 36  VAL   B CG2 1 
ATOM   474  N  N   . GLY   B 2 28  ? -16.810 9.791   -15.532 1.00 47.97  ? 37  GLY   B N   1 
ATOM   475  C  CA  . GLY   B 2 28  ? -17.053 8.383   -15.753 1.00 47.57  ? 37  GLY   B CA  1 
ATOM   476  C  C   . GLY   B 2 28  ? -18.358 8.139   -16.478 1.00 47.16  ? 37  GLY   B C   1 
ATOM   477  O  O   . GLY   B 2 28  ? -19.007 9.067   -16.969 1.00 46.67  ? 37  GLY   B O   1 
ATOM   478  N  N   . VAL   B 2 29  ? -18.744 6.863   -16.543 1.00 46.40  ? 38  VAL   B N   1 
ATOM   479  C  CA  . VAL   B 2 29  ? -19.937 6.357   -17.220 1.00 45.16  ? 38  VAL   B CA  1 
ATOM   480  C  C   . VAL   B 2 29  ? -20.643 5.337   -16.287 1.00 44.13  ? 38  VAL   B C   1 
ATOM   481  O  O   . VAL   B 2 29  ? -20.023 4.778   -15.381 1.00 43.89  ? 38  VAL   B O   1 
ATOM   482  C  CB  . VAL   B 2 29  ? -19.471 5.706   -18.566 1.00 44.81  ? 38  VAL   B CB  1 
ATOM   483  C  CG1 . VAL   B 2 29  ? -20.584 4.961   -19.280 1.00 45.07  ? 38  VAL   B CG1 1 
ATOM   484  C  CG2 . VAL   B 2 29  ? -18.845 6.731   -19.495 1.00 44.44  ? 38  VAL   B CG2 1 
ATOM   485  N  N   . GLY   B 2 30  ? -21.925 5.105   -16.516 1.00 43.30  ? 39  GLY   B N   1 
ATOM   486  C  CA  . GLY   B 2 30  ? -22.663 4.099   -15.768 1.00 43.05  ? 39  GLY   B CA  1 
ATOM   487  C  C   . GLY   B 2 30  ? -23.761 3.440   -16.575 1.00 42.85  ? 39  GLY   B C   1 
ATOM   488  O  O   . GLY   B 2 30  ? -24.042 3.855   -17.693 1.00 43.04  ? 39  GLY   B O   1 
ATOM   489  N  N   . VAL   B 2 31  ? -24.417 2.442   -15.989 1.00 42.73  ? 40  VAL   B N   1 
ATOM   490  C  CA  . VAL   B 2 31  ? -25.489 1.670   -16.611 1.00 43.43  ? 40  VAL   B CA  1 
ATOM   491  C  C   . VAL   B 2 31  ? -26.745 1.800   -15.779 1.00 44.30  ? 40  VAL   B C   1 
ATOM   492  O  O   . VAL   B 2 31  ? -26.720 1.468   -14.606 1.00 44.95  ? 40  VAL   B O   1 
ATOM   493  C  CB  . VAL   B 2 31  ? -25.098 0.157   -16.682 1.00 44.09  ? 40  VAL   B CB  1 
ATOM   494  C  CG1 . VAL   B 2 31  ? -26.256 -0.706  -17.158 1.00 44.66  ? 40  VAL   B CG1 1 
ATOM   495  C  CG2 . VAL   B 2 31  ? -23.863 -0.070  -17.533 1.00 44.37  ? 40  VAL   B CG2 1 
ATOM   496  N  N   . MET   B 2 32  ? -27.845 2.226   -16.371 1.00 44.82  ? 41  MET   B N   1 
ATOM   497  C  CA  . MET   B 2 32  ? -29.132 2.240   -15.688 1.00 45.56  ? 41  MET   B CA  1 
ATOM   498  C  C   . MET   B 2 32  ? -29.827 0.930   -16.096 1.00 46.13  ? 41  MET   B C   1 
ATOM   499  O  O   . MET   B 2 32  ? -29.820 0.573   -17.273 1.00 46.47  ? 41  MET   B O   1 
ATOM   500  C  CB  . MET   B 2 32  ? -29.957 3.462   -16.110 1.00 46.32  ? 41  MET   B CB  1 
ATOM   501  C  CG  . MET   B 2 32  ? -31.230 3.646   -15.311 1.00 48.57  ? 41  MET   B CG  1 
ATOM   502  S  SD  . MET   B 2 32  ? -30.943 4.266   -13.638 1.00 52.58  ? 41  MET   B SD  1 
ATOM   503  C  CE  . MET   B 2 32  ? -30.592 5.968   -13.994 1.00 48.85  ? 41  MET   B CE  1 
ATOM   504  N  N   . GLN   B 2 33  ? -30.347 0.172   -15.133 1.00 46.46  ? 42  GLN   B N   1 
ATOM   505  C  CA  . GLN   B 2 33  ? -31.027 -1.097  -15.435 1.00 47.02  ? 42  GLN   B CA  1 
ATOM   506  C  C   . GLN   B 2 33  ? -31.916 -1.461  -14.272 1.00 46.92  ? 42  GLN   B C   1 
ATOM   507  O  O   . GLN   B 2 33  ? -31.446 -1.397  -13.147 1.00 47.61  ? 42  GLN   B O   1 
ATOM   508  C  CB  . GLN   B 2 33  ? -30.015 -2.226  -15.689 1.00 49.15  ? 42  GLN   B CB  1 
ATOM   509  C  CG  . GLN   B 2 33  ? -30.709 -3.552  -15.992 1.00 54.57  ? 42  GLN   B CG  1 
ATOM   510  C  CD  . GLN   B 2 33  ? -29.791 -4.564  -16.616 1.00 60.53  ? 42  GLN   B CD  1 
ATOM   511  O  OE1 . GLN   B 2 33  ? -29.630 -5.686  -16.113 1.00 62.48  ? 42  GLN   B OE1 1 
ATOM   512  N  NE2 . GLN   B 2 33  ? -29.177 -4.190  -17.737 1.00 61.42  ? 42  GLN   B NE2 1 
ATOM   513  N  N   . GLU   B 2 34  ? -33.194 -1.805  -14.512 1.00 46.24  ? 43  GLU   B N   1 
ATOM   514  C  CA  . GLU   B 2 34  ? -34.106 -2.174  -13.431 1.00 46.27  ? 43  GLU   B CA  1 
ATOM   515  C  C   . GLU   B 2 34  ? -34.216 -1.086  -12.321 1.00 46.29  ? 43  GLU   B C   1 
ATOM   516  O  O   . GLU   B 2 34  ? -34.357 -1.399  -11.145 1.00 46.78  ? 43  GLU   B O   1 
ATOM   517  C  CB  . GLU   B 2 34  ? -33.745 -3.555  -12.851 1.00 48.67  ? 43  GLU   B CB  1 
ATOM   518  C  CG  . GLU   B 2 34  ? -33.939 -4.717  -13.819 1.00 53.77  ? 43  GLU   B CG  1 
ATOM   519  C  CD  . GLU   B 2 34  ? -33.312 -6.039  -13.400 1.00 59.79  ? 43  GLU   B CD  1 
ATOM   520  O  OE1 . GLU   B 2 34  ? -33.622 -6.520  -12.287 1.00 61.70  ? 43  GLU   B OE1 1 
ATOM   521  O  OE2 . GLU   B 2 34  ? -32.507 -6.595  -14.182 1.00 61.28  ? 43  GLU   B OE2 1 
ATOM   522  N  N   . GLY   B 2 35  ? -34.150 0.180   -12.717 1.00 45.76  ? 44  GLY   B N   1 
ATOM   523  C  CA  . GLY   B 2 35  ? -34.260 1.308   -11.803 1.00 45.36  ? 44  GLY   B CA  1 
ATOM   524  C  C   . GLY   B 2 35  ? -33.048 1.561   -10.931 1.00 44.95  ? 44  GLY   B C   1 
ATOM   525  O  O   . GLY   B 2 35  ? -33.114 2.394   -10.022 1.00 45.37  ? 44  GLY   B O   1 
ATOM   526  N  N   . VAL   B 2 36  ? -31.923 0.856   -11.206 1.00 43.79  ? 45  VAL   B N   1 
ATOM   527  C  CA  . VAL   B 2 36  ? -30.680 0.956   -10.449 1.00 42.76  ? 45  VAL   B CA  1 
ATOM   528  C  C   . VAL   B 2 36  ? -29.550 1.500   -11.333 1.00 42.17  ? 45  VAL   B C   1 
ATOM   529  O  O   . VAL   B 2 36  ? -29.311 0.961   -12.408 1.00 42.50  ? 45  VAL   B O   1 
ATOM   530  C  CB  . VAL   B 2 36  ? -30.304 -0.423  -9.835  1.00 42.89  ? 45  VAL   B CB  1 
ATOM   531  C  CG1 . VAL   B 2 36  ? -28.907 -0.417  -9.202  1.00 43.14  ? 45  VAL   B CG1 1 
ATOM   532  C  CG2 . VAL   B 2 36  ? -31.346 -0.879  -8.831  1.00 43.07  ? 45  VAL   B CG2 1 
ATOM   533  N  N   . PHE   B 2 37  ? -28.851 2.567   -10.881 1.00 40.80  ? 46  PHE   B N   1 
ATOM   534  C  CA  . PHE   B 2 37  ? -27.709 3.097   -11.622 1.00 39.72  ? 46  PHE   B CA  1 
ATOM   535  C  C   . PHE   B 2 37  ? -26.414 2.413   -11.123 1.00 38.91  ? 46  PHE   B C   1 
ATOM   536  O  O   . PHE   B 2 37  ? -26.132 2.469   -9.944  1.00 38.82  ? 46  PHE   B O   1 
ATOM   537  C  CB  . PHE   B 2 37  ? -27.605 4.629   -11.477 1.00 38.74  ? 46  PHE   B CB  1 
ATOM   538  C  CG  . PHE   B 2 37  ? -26.554 5.209   -12.401 1.00 38.76  ? 46  PHE   B CG  1 
ATOM   539  C  CD1 . PHE   B 2 37  ? -26.713 5.162   -13.773 1.00 39.08  ? 46  PHE   B CD1 1 
ATOM   540  C  CD2 . PHE   B 2 37  ? -25.392 5.768   -11.897 1.00 38.93  ? 46  PHE   B CD2 1 
ATOM   541  C  CE1 . PHE   B 2 37  ? -25.736 5.681   -14.622 1.00 39.20  ? 46  PHE   B CE1 1 
ATOM   542  C  CE2 . PHE   B 2 37  ? -24.414 6.270   -12.752 1.00 38.73  ? 46  PHE   B CE2 1 
ATOM   543  C  CZ  . PHE   B 2 37  ? -24.598 6.232   -14.104 1.00 38.26  ? 46  PHE   B CZ  1 
ATOM   544  N  N   . HIS   B 2 38  ? -25.640 1.771   -12.021 1.00 38.88  ? 47  HIS   B N   1 
ATOM   545  C  CA  . HIS   B 2 38  ? -24.406 1.052   -11.706 1.00 38.57  ? 47  HIS   B CA  1 
ATOM   546  C  C   . HIS   B 2 38  ? -23.195 1.747   -12.290 1.00 39.23  ? 47  HIS   B C   1 
ATOM   547  O  O   . HIS   B 2 38  ? -23.090 1.803   -13.492 1.00 39.36  ? 47  HIS   B O   1 
ATOM   548  C  CB  . HIS   B 2 38  ? -24.432 -0.346  -12.346 1.00 38.25  ? 47  HIS   B CB  1 
ATOM   549  C  CG  . HIS   B 2 38  ? -25.671 -1.129  -12.076 1.00 38.56  ? 47  HIS   B CG  1 
ATOM   550  N  ND1 . HIS   B 2 38  ? -26.896 -0.768  -12.636 1.00 39.45  ? 47  HIS   B ND1 1 
ATOM   551  C  CD2 . HIS   B 2 38  ? -25.839 -2.248  -11.338 1.00 38.80  ? 47  HIS   B CD2 1 
ATOM   552  C  CE1 . HIS   B 2 38  ? -27.761 -1.669  -12.199 1.00 39.65  ? 47  HIS   B CE1 1 
ATOM   553  N  NE2 . HIS   B 2 38  ? -27.167 -2.582  -11.424 1.00 39.62  ? 47  HIS   B NE2 1 
ATOM   554  N  N   . THR   B 2 39  ? -22.211 2.141   -11.463 1.00 39.66  ? 48  THR   B N   1 
ATOM   555  C  CA  . THR   B 2 39  ? -20.976 2.724   -11.980 1.00 39.69  ? 48  THR   B CA  1 
ATOM   556  C  C   . THR   B 2 39  ? -19.734 2.178   -11.180 1.00 40.11  ? 48  THR   B C   1 
ATOM   557  O  O   . THR   B 2 39  ? -19.871 1.234   -10.404 1.00 39.70  ? 48  THR   B O   1 
ATOM   558  C  CB  . THR   B 2 39  ? -21.105 4.264   -12.062 1.00 40.06  ? 48  THR   B CB  1 
ATOM   559  O  OG1 . THR   B 2 39  ? -19.945 4.753   -12.735 1.00 39.79  ? 48  THR   B OG1 1 
ATOM   560  C  CG2 . THR   B 2 39  ? -21.190 4.923   -10.684 1.00 40.78  ? 48  THR   B CG2 1 
ATOM   561  N  N   . MET   B 2 40  ? -18.529 2.735   -11.420 1.00 40.69  ? 49  MET   B N   1 
ATOM   562  C  CA  . MET   B 2 40  ? -17.304 2.384   -10.708 1.00 41.48  ? 49  MET   B CA  1 
ATOM   563  C  C   . MET   B 2 40  ? -17.200 3.311   -9.528  1.00 41.78  ? 49  MET   B C   1 
ATOM   564  O  O   . MET   B 2 40  ? -17.457 4.499   -9.664  1.00 41.40  ? 49  MET   B O   1 
ATOM   565  C  CB  . MET   B 2 40  ? -16.058 2.606   -11.589 1.00 42.27  ? 49  MET   B CB  1 
ATOM   566  C  CG  . MET   B 2 40  ? -16.197 2.067   -12.969 1.00 45.19  ? 49  MET   B CG  1 
ATOM   567  S  SD  . MET   B 2 40  ? -15.166 0.633   -13.264 1.00 52.66  ? 49  MET   B SD  1 
ATOM   568  C  CE  . MET   B 2 40  ? -16.118 -0.560  -12.604 1.00 55.43  ? 49  MET   B CE  1 
ATOM   569  N  N   . TRP   B 2 41  ? -16.783 2.772   -8.371  1.00 42.34  ? 50  TRP   B N   1 
ATOM   570  C  CA  A TRP   B 2 41  ? -16.641 3.550   -7.149  0.50 42.78  ? 50  TRP   B CA  1 
ATOM   571  C  CA  B TRP   B 2 41  ? -16.639 3.540   -7.147  0.50 42.38  ? 50  TRP   B CA  1 
ATOM   572  C  C   . TRP   B 2 41  ? -15.711 4.740   -7.314  1.00 42.87  ? 50  TRP   B C   1 
ATOM   573  O  O   . TRP   B 2 41  ? -16.035 5.822   -6.829  1.00 42.90  ? 50  TRP   B O   1 
ATOM   574  C  CB  A TRP   B 2 41  ? -16.169 2.676   -5.967  0.50 42.81  ? 50  TRP   B CB  1 
ATOM   575  C  CB  B TRP   B 2 41  ? -16.144 2.639   -5.998  0.50 41.84  ? 50  TRP   B CB  1 
ATOM   576  C  CG  A TRP   B 2 41  ? -16.325 3.371   -4.649  0.50 43.38  ? 50  TRP   B CG  1 
ATOM   577  C  CG  B TRP   B 2 41  ? -15.973 3.376   -4.708  0.50 41.61  ? 50  TRP   B CG  1 
ATOM   578  C  CD1 A TRP   B 2 41  ? -17.435 3.378   -3.860  0.50 44.27  ? 50  TRP   B CD1 1 
ATOM   579  C  CD1 B TRP   B 2 41  ? -14.923 4.167   -4.347  0.50 42.24  ? 50  TRP   B CD1 1 
ATOM   580  C  CD2 A TRP   B 2 41  ? -15.386 4.263   -4.030  0.50 43.64  ? 50  TRP   B CD2 1 
ATOM   581  C  CD2 B TRP   B 2 41  ? -16.915 3.447   -3.639  0.50 41.47  ? 50  TRP   B CD2 1 
ATOM   582  N  NE1 A TRP   B 2 41  ? -17.232 4.187   -2.769  0.50 44.82  ? 50  TRP   B NE1 1 
ATOM   583  N  NE1 B TRP   B 2 41  ? -15.163 4.741   -3.126  0.50 42.40  ? 50  TRP   B NE1 1 
ATOM   584  C  CE2 A TRP   B 2 41  ? -15.983 4.747   -2.852  0.50 44.51  ? 50  TRP   B CE2 1 
ATOM   585  C  CE2 B TRP   B 2 41  ? -16.365 4.288   -2.651  0.50 42.25  ? 50  TRP   B CE2 1 
ATOM   586  C  CE3 A TRP   B 2 41  ? -14.081 4.666   -4.335  0.50 44.45  ? 50  TRP   B CE3 1 
ATOM   587  C  CE3 B TRP   B 2 41  ? -18.165 2.869   -3.409  0.50 42.01  ? 50  TRP   B CE3 1 
ATOM   588  C  CZ2 A TRP   B 2 41  ? -15.329 5.629   -1.991  0.50 45.28  ? 50  TRP   B CZ2 1 
ATOM   589  C  CZ2 B TRP   B 2 41  ? -17.027 4.570   -1.459  0.50 42.90  ? 50  TRP   B CZ2 1 
ATOM   590  C  CZ3 A TRP   B 2 41  ? -13.445 5.556   -3.493  0.50 45.42  ? 50  TRP   B CZ3 1 
ATOM   591  C  CZ3 B TRP   B 2 41  ? -18.801 3.127   -2.211  0.50 43.17  ? 50  TRP   B CZ3 1 
ATOM   592  C  CH2 A TRP   B 2 41  ? -14.056 6.005   -2.321  0.50 45.49  ? 50  TRP   B CH2 1 
ATOM   593  C  CH2 B TRP   B 2 41  ? -18.227 3.964   -1.251  0.50 43.06  ? 50  TRP   B CH2 1 
ATOM   594  N  N   . HIS   B 2 42  ? -14.531 4.541   -7.935  1.00 42.32  ? 51  HIS   B N   1 
ATOM   595  C  CA  . HIS   B 2 42  ? -13.567 5.632   -8.065  1.00 42.51  ? 51  HIS   B CA  1 
ATOM   596  C  C   . HIS   B 2 42  ? -14.091 6.858   -8.830  1.00 44.13  ? 51  HIS   B C   1 
ATOM   597  O  O   . HIS   B 2 42  ? -13.550 7.947   -8.651  1.00 45.25  ? 51  HIS   B O   1 
ATOM   598  C  CB  . HIS   B 2 42  ? -12.243 5.136   -8.648  1.00 41.12  ? 51  HIS   B CB  1 
ATOM   599  C  CG  . HIS   B 2 42  ? -12.260 4.909   -10.125 1.00 41.08  ? 51  HIS   B CG  1 
ATOM   600  N  ND1 . HIS   B 2 42  ? -12.384 3.637   -10.661 1.00 41.45  ? 51  HIS   B ND1 1 
ATOM   601  C  CD2 . HIS   B 2 42  ? -12.090 5.794   -11.132 1.00 41.68  ? 51  HIS   B CD2 1 
ATOM   602  C  CE1 . HIS   B 2 42  ? -12.342 3.801   -11.960 1.00 41.94  ? 51  HIS   B CE1 1 
ATOM   603  N  NE2 . HIS   B 2 42  ? -12.196 5.090   -12.290 1.00 42.66  ? 51  HIS   B NE2 1 
ATOM   604  N  N   . VAL   B 2 43  ? -15.143 6.683   -9.656  1.00 44.11  ? 52  VAL   B N   1 
ATOM   605  C  CA  . VAL   B 2 43  ? -15.790 7.724   -10.448 1.00 44.64  ? 52  VAL   B CA  1 
ATOM   606  C  C   . VAL   B 2 43  ? -16.577 8.723   -9.573  1.00 46.39  ? 52  VAL   B C   1 
ATOM   607  O  O   . VAL   B 2 43  ? -16.377 9.934   -9.700  1.00 47.08  ? 52  VAL   B O   1 
ATOM   608  C  CB  . VAL   B 2 43  ? -16.689 7.083   -11.546 1.00 44.61  ? 52  VAL   B CB  1 
ATOM   609  C  CG1 . VAL   B 2 43  ? -17.604 8.110   -12.209 1.00 44.94  ? 52  VAL   B CG1 1 
ATOM   610  C  CG2 . VAL   B 2 43  ? -15.856 6.341   -12.579 1.00 44.82  ? 52  VAL   B CG2 1 
ATOM   611  N  N   . THR   B 2 44  ? -17.487 8.225   -8.703  1.00 46.78  ? 53  THR   B N   1 
ATOM   612  C  CA  . THR   B 2 44  ? -18.324 9.088   -7.865  1.00 47.50  ? 53  THR   B CA  1 
ATOM   613  C  C   . THR   B 2 44  ? -17.817 9.278   -6.436  1.00 48.27  ? 53  THR   B C   1 
ATOM   614  O  O   . THR   B 2 44  ? -18.212 10.235  -5.760  1.00 48.01  ? 53  THR   B O   1 
ATOM   615  C  CB  . THR   B 2 44  ? -19.759 8.540   -7.816  1.00 48.70  ? 53  THR   B CB  1 
ATOM   616  O  OG1 . THR   B 2 44  ? -19.781 7.318   -7.070  1.00 49.46  ? 53  THR   B OG1 1 
ATOM   617  C  CG2 . THR   B 2 44  ? -20.340 8.296   -9.192  1.00 49.31  ? 53  THR   B CG2 1 
ATOM   618  N  N   . LYS   B 2 45  ? -16.972 8.340   -5.972  1.00 48.71  ? 54  LYS   B N   1 
ATOM   619  C  CA  . LYS   B 2 45  ? -16.454 8.229   -4.605  1.00 49.28  ? 54  LYS   B CA  1 
ATOM   620  C  C   . LYS   B 2 45  ? -17.588 8.048   -3.578  1.00 49.41  ? 54  LYS   B C   1 
ATOM   621  O  O   . LYS   B 2 45  ? -17.425 8.387   -2.408  1.00 49.59  ? 54  LYS   B O   1 
ATOM   622  C  CB  . LYS   B 2 45  ? -15.481 9.361   -4.234  1.00 51.09  ? 54  LYS   B CB  1 
ATOM   623  C  CG  . LYS   B 2 45  ? -14.097 9.093   -4.818  1.00 55.94  ? 54  LYS   B CG  1 
ATOM   624  C  CD  . LYS   B 2 45  ? -13.056 10.130  -4.423  1.00 61.68  ? 54  LYS   B CD  1 
ATOM   625  C  CE  . LYS   B 2 45  ? -12.006 10.329  -5.499  1.00 66.52  ? 54  LYS   B CE  1 
ATOM   626  N  NZ  . LYS   B 2 45  ? -11.426 9.035   -5.984  1.00 69.51  ? 54  LYS   B NZ  1 
ATOM   627  N  N   . GLY   B 2 46  ? -18.696 7.449   -4.026  1.00 49.50  ? 55  GLY   B N   1 
ATOM   628  C  CA  . GLY   B 2 46  ? -19.889 7.193   -3.235  1.00 49.92  ? 55  GLY   B CA  1 
ATOM   629  C  C   . GLY   B 2 46  ? -20.850 8.362   -3.129  1.00 50.70  ? 55  GLY   B C   1 
ATOM   630  O  O   . GLY   B 2 46  ? -21.928 8.210   -2.560  1.00 51.56  ? 55  GLY   B O   1 
ATOM   631  N  N   . ALA   B 2 47  ? -20.490 9.538   -3.656  1.00 50.49  ? 56  ALA   B N   1 
ATOM   632  C  CA  . ALA   B 2 47  ? -21.340 10.726  -3.563  1.00 51.03  ? 56  ALA   B CA  1 
ATOM   633  C  C   . ALA   B 2 47  ? -22.656 10.592  -4.310  1.00 51.39  ? 56  ALA   B C   1 
ATOM   634  O  O   . ALA   B 2 47  ? -22.721 9.846   -5.283  1.00 51.71  ? 56  ALA   B O   1 
ATOM   635  C  CB  . ALA   B 2 47  ? -20.588 11.948  -4.062  1.00 51.17  ? 56  ALA   B CB  1 
ATOM   636  N  N   . ALA   B 2 48  ? -23.704 11.315  -3.852  1.00 51.20  ? 57  ALA   B N   1 
ATOM   637  C  CA  . ALA   B 2 48  ? -25.026 11.316  -4.477  1.00 51.74  ? 57  ALA   B CA  1 
ATOM   638  C  C   . ALA   B 2 48  ? -24.955 11.919  -5.875  1.00 52.43  ? 57  ALA   B C   1 
ATOM   639  O  O   . ALA   B 2 48  ? -24.090 12.754  -6.148  1.00 52.79  ? 57  ALA   B O   1 
ATOM   640  C  CB  . ALA   B 2 48  ? -26.015 12.097  -3.630  1.00 51.86  ? 57  ALA   B CB  1 
ATOM   641  N  N   . LEU   B 2 49  ? -25.854 11.477  -6.773  1.00 52.23  ? 58  LEU   B N   1 
ATOM   642  C  CA  . LEU   B 2 49  ? -25.889 11.931  -8.158  1.00 52.25  ? 58  LEU   B CA  1 
ATOM   643  C  C   . LEU   B 2 49  ? -27.206 12.630  -8.499  1.00 53.27  ? 58  LEU   B C   1 
ATOM   644  O  O   . LEU   B 2 49  ? -28.245 12.280  -7.969  1.00 53.13  ? 58  LEU   B O   1 
ATOM   645  C  CB  . LEU   B 2 49  ? -25.698 10.733  -9.091  1.00 51.81  ? 58  LEU   B CB  1 
ATOM   646  C  CG  . LEU   B 2 49  ? -24.399 9.965   -8.940  1.00 52.34  ? 58  LEU   B CG  1 
ATOM   647  C  CD1 . LEU   B 2 49  ? -24.454 8.690   -9.726  1.00 52.88  ? 58  LEU   B CD1 1 
ATOM   648  C  CD2 . LEU   B 2 49  ? -23.218 10.792  -9.388  1.00 52.20  ? 58  LEU   B CD2 1 
ATOM   649  N  N   . ARG   B 2 50  ? -27.167 13.584  -9.412  1.00 54.21  ? 59  ARG   B N   1 
ATOM   650  C  CA  . ARG   B 2 50  ? -28.352 14.319  -9.835  1.00 55.79  ? 59  ARG   B CA  1 
ATOM   651  C  C   . ARG   B 2 50  ? -28.796 13.816  -11.213 1.00 57.04  ? 59  ARG   B C   1 
ATOM   652  O  O   . ARG   B 2 50  ? -27.964 13.462  -12.037 1.00 56.00  ? 59  ARG   B O   1 
ATOM   653  C  CB  . ARG   B 2 50  ? -28.023 15.824  -9.833  1.00 57.73  ? 59  ARG   B CB  1 
ATOM   654  C  CG  . ARG   B 2 50  ? -28.964 16.710  -10.608 1.00 62.97  ? 59  ARG   B CG  1 
ATOM   655  C  CD  . ARG   B 2 50  ? -28.796 18.173  -10.234 1.00 68.11  ? 59  ARG   B CD  1 
ATOM   656  N  NE  . ARG   B 2 50  ? -27.454 18.696  -10.509 1.00 72.95  ? 59  ARG   B NE  1 
ATOM   657  C  CZ  . ARG   B 2 50  ? -27.066 19.186  -11.684 1.00 77.75  ? 59  ARG   B CZ  1 
ATOM   658  N  NH1 . ARG   B 2 50  ? -27.901 19.187  -12.721 1.00 78.45  ? 59  ARG   B NH1 1 
ATOM   659  N  NH2 . ARG   B 2 50  ? -25.834 19.659  -11.841 1.00 78.38  ? 59  ARG   B NH2 1 
ATOM   660  N  N   . SER   B 2 51  ? -30.100 13.721  -11.442 1.00 59.17  ? 60  SER   B N   1 
ATOM   661  C  CA  . SER   B 2 51  ? -30.626 13.285  -12.735 1.00 62.01  ? 60  SER   B CA  1 
ATOM   662  C  C   . SER   B 2 51  ? -31.678 14.302  -13.155 1.00 65.47  ? 60  SER   B C   1 
ATOM   663  O  O   . SER   B 2 51  ? -32.877 14.015  -13.174 1.00 66.21  ? 60  SER   B O   1 
ATOM   664  C  CB  . SER   B 2 51  ? -31.219 11.886  -12.633 1.00 63.30  ? 60  SER   B CB  1 
ATOM   665  O  OG  . SER   B 2 51  ? -31.619 11.412  -13.905 1.00 65.89  ? 60  SER   B OG  1 
ATOM   666  N  N   . GLY   B 2 52  ? -31.219 15.518  -13.414 1.00 67.06  ? 61  GLY   B N   1 
ATOM   667  C  CA  . GLY   B 2 52  ? -32.100 16.621  -13.759 1.00 68.55  ? 61  GLY   B CA  1 
ATOM   668  C  C   . GLY   B 2 52  ? -32.616 17.246  -12.488 1.00 70.17  ? 61  GLY   B C   1 
ATOM   669  O  O   . GLY   B 2 52  ? -31.878 17.940  -11.779 1.00 70.82  ? 61  GLY   B O   1 
ATOM   670  N  N   . GLU   B 2 53  ? -33.874 16.969  -12.165 1.00 70.51  ? 62  GLU   B N   1 
ATOM   671  C  CA  . GLU   B 2 53  ? -34.462 17.466  -10.926 1.00 71.06  ? 62  GLU   B CA  1 
ATOM   672  C  C   . GLU   B 2 53  ? -34.476 16.407  -9.795  1.00 70.58  ? 62  GLU   B C   1 
ATOM   673  O  O   . GLU   B 2 53  ? -34.768 16.751  -8.648  1.00 71.60  ? 62  GLU   B O   1 
ATOM   674  C  CB  . GLU   B 2 53  ? -35.872 17.996  -11.189 1.00 74.39  ? 62  GLU   B CB  1 
ATOM   675  C  CG  . GLU   B 2 53  ? -36.215 19.247  -10.404 1.00 80.74  ? 62  GLU   B CG  1 
ATOM   676  C  CD  . GLU   B 2 53  ? -37.580 19.833  -10.719 1.00 91.07  ? 62  GLU   B CD  1 
ATOM   677  O  OE1 . GLU   B 2 53  ? -38.392 19.146  -11.385 1.00 92.63  ? 62  GLU   B OE1 1 
ATOM   678  O  OE2 . GLU   B 2 53  ? -37.840 20.984  -10.295 1.00 95.06  ? 62  GLU   B OE2 1 
ATOM   679  N  N   . GLY   B 2 54  ? -34.171 15.152  -10.122 1.00 68.93  ? 63  GLY   B N   1 
ATOM   680  C  CA  . GLY   B 2 54  ? -34.159 14.054  -9.168  1.00 68.11  ? 63  GLY   B CA  1 
ATOM   681  C  C   . GLY   B 2 54  ? -32.798 13.734  -8.577  1.00 66.51  ? 63  GLY   B C   1 
ATOM   682  O  O   . GLY   B 2 54  ? -31.761 14.135  -9.108  1.00 67.11  ? 63  GLY   B O   1 
ATOM   683  N  N   . ARG   B 2 55  ? -32.798 13.000  -7.467  1.00 64.10  ? 64  ARG   B N   1 
ATOM   684  C  CA  . ARG   B 2 55  ? -31.568 12.656  -6.772  1.00 62.09  ? 64  ARG   B CA  1 
ATOM   685  C  C   . ARG   B 2 55  ? -31.437 11.149  -6.630  1.00 59.26  ? 64  ARG   B C   1 
ATOM   686  O  O   . ARG   B 2 55  ? -32.389 10.468  -6.253  1.00 59.20  ? 64  ARG   B O   1 
ATOM   687  C  CB  . ARG   B 2 55  ? -31.569 13.309  -5.383  1.00 63.26  ? 64  ARG   B CB  1 
ATOM   688  C  CG  . ARG   B 2 55  ? -30.261 13.200  -4.629  1.00 66.34  ? 64  ARG   B CG  1 
ATOM   689  C  CD  . ARG   B 2 55  ? -30.489 13.562  -3.172  1.00 70.57  ? 64  ARG   B CD  1 
ATOM   690  N  NE  . ARG   B 2 55  ? -29.325 13.271  -2.331  1.00 74.32  ? 64  ARG   B NE  1 
ATOM   691  C  CZ  . ARG   B 2 55  ? -28.762 14.143  -1.498  1.00 77.11  ? 64  ARG   B CZ  1 
ATOM   692  N  NH1 . ARG   B 2 55  ? -29.245 15.375  -1.387  1.00 77.33  ? 64  ARG   B NH1 1 
ATOM   693  N  NH2 . ARG   B 2 55  ? -27.710 13.788  -0.768  1.00 76.84  ? 64  ARG   B NH2 1 
ATOM   694  N  N   . LEU   B 2 56  ? -30.256 10.639  -6.926  1.00 56.71  ? 65  LEU   B N   1 
ATOM   695  C  CA  . LEU   B 2 56  ? -29.932 9.234   -6.812  1.00 54.82  ? 65  LEU   B CA  1 
ATOM   696  C  C   . LEU   B 2 56  ? -29.020 9.082   -5.622  1.00 52.86  ? 65  LEU   B C   1 
ATOM   697  O  O   . LEU   B 2 56  ? -27.916 9.637   -5.613  1.00 52.40  ? 65  LEU   B O   1 
ATOM   698  C  CB  . LEU   B 2 56  ? -29.177 8.754   -8.055  1.00 54.75  ? 65  LEU   B CB  1 
ATOM   699  C  CG  . LEU   B 2 56  ? -29.753 9.077   -9.406  1.00 56.52  ? 65  LEU   B CG  1 
ATOM   700  C  CD1 . LEU   B 2 56  ? -28.909 8.458   -10.479 1.00 57.64  ? 65  LEU   B CD1 1 
ATOM   701  C  CD2 . LEU   B 2 56  ? -31.153 8.543   -9.546  1.00 57.17  ? 65  LEU   B CD2 1 
ATOM   702  N  N   . ASP   B 2 57  ? -29.458 8.330   -4.628  1.00 51.63  ? 66  ASP   B N   1 
ATOM   703  C  CA  . ASP   B 2 57  ? -28.637 8.095   -3.438  1.00 50.91  ? 66  ASP   B CA  1 
ATOM   704  C  C   . ASP   B 2 57  ? -27.944 6.739   -3.550  1.00 48.62  ? 66  ASP   B C   1 
ATOM   705  O  O   . ASP   B 2 57  ? -28.525 5.785   -4.079  1.00 48.72  ? 66  ASP   B O   1 
ATOM   706  C  CB  . ASP   B 2 57  ? -29.503 8.148   -2.182  1.00 54.24  ? 66  ASP   B CB  1 
ATOM   707  C  CG  . ASP   B 2 57  ? -30.240 9.456   -2.047  1.00 62.77  ? 66  ASP   B CG  1 
ATOM   708  O  OD1 . ASP   B 2 57  ? -29.573 10.510  -2.040  1.00 64.47  ? 66  ASP   B OD1 1 
ATOM   709  O  OD2 . ASP   B 2 57  ? -31.494 9.428   -1.959  1.00 66.21  ? 66  ASP   B OD2 1 
ATOM   710  N  N   . PRO   B 2 58  ? -26.685 6.637   -3.098  1.00 46.46  ? 67  PRO   B N   1 
ATOM   711  C  CA  . PRO   B 2 58  ? -25.995 5.342   -3.158  1.00 45.15  ? 67  PRO   B CA  1 
ATOM   712  C  C   . PRO   B 2 58  ? -26.690 4.308   -2.267  1.00 44.34  ? 67  PRO   B C   1 
ATOM   713  O  O   . PRO   B 2 58  ? -27.307 4.659   -1.261  1.00 44.95  ? 67  PRO   B O   1 
ATOM   714  C  CB  . PRO   B 2 58  ? -24.584 5.666   -2.661  1.00 45.71  ? 67  PRO   B CB  1 
ATOM   715  C  CG  . PRO   B 2 58  ? -24.730 6.879   -1.878  1.00 46.37  ? 67  PRO   B CG  1 
ATOM   716  C  CD  . PRO   B 2 58  ? -25.847 7.670   -2.464  1.00 45.54  ? 67  PRO   B CD  1 
ATOM   717  N  N   . TYR   B 2 59  ? -26.619 3.038   -2.649  1.00 42.86  ? 68  TYR   B N   1 
ATOM   718  C  CA  . TYR   B 2 59  ? -27.277 1.980   -1.918  1.00 41.78  ? 68  TYR   B CA  1 
ATOM   719  C  C   . TYR   B 2 59  ? -26.285 0.939   -1.442  1.00 42.13  ? 68  TYR   B C   1 
ATOM   720  O  O   . TYR   B 2 59  ? -26.330 0.531   -0.290  1.00 43.65  ? 68  TYR   B O   1 
ATOM   721  C  CB  . TYR   B 2 59  ? -28.382 1.391   -2.792  1.00 40.65  ? 68  TYR   B CB  1 
ATOM   722  C  CG  . TYR   B 2 59  ? -29.104 0.203   -2.195  1.00 40.60  ? 68  TYR   B CG  1 
ATOM   723  C  CD1 . TYR   B 2 59  ? -28.499 -1.048  -2.139  1.00 40.74  ? 68  TYR   B CD1 1 
ATOM   724  C  CD2 . TYR   B 2 59  ? -30.444 0.287   -1.846  1.00 40.50  ? 68  TYR   B CD2 1 
ATOM   725  C  CE1 . TYR   B 2 59  ? -29.168 -2.151  -1.634  1.00 41.67  ? 68  TYR   B CE1 1 
ATOM   726  C  CE2 . TYR   B 2 59  ? -31.135 -0.819  -1.382  1.00 41.40  ? 68  TYR   B CE2 1 
ATOM   727  C  CZ  . TYR   B 2 59  ? -30.493 -2.040  -1.281  1.00 42.66  ? 68  TYR   B CZ  1 
ATOM   728  O  OH  . TYR   B 2 59  ? -31.157 -3.137  -0.790  1.00 44.88  ? 68  TYR   B OH  1 
ATOM   729  N  N   . TRP   B 2 60  ? -25.400 0.501   -2.321  1.00 41.57  ? 69  TRP   B N   1 
ATOM   730  C  CA  . TRP   B 2 60  ? -24.374 -0.489  -2.043  1.00 41.13  ? 69  TRP   B CA  1 
ATOM   731  C  C   . TRP   B 2 60  ? -23.053 0.009   -2.674  1.00 41.12  ? 69  TRP   B C   1 
ATOM   732  O  O   . TRP   B 2 60  ? -23.069 0.593   -3.744  1.00 40.61  ? 69  TRP   B O   1 
ATOM   733  C  CB  . TRP   B 2 60  ? -24.767 -1.853  -2.660  1.00 40.65  ? 69  TRP   B CB  1 
ATOM   734  C  CG  . TRP   B 2 60  ? -23.639 -2.830  -2.619  1.00 40.67  ? 69  TRP   B CG  1 
ATOM   735  C  CD1 . TRP   B 2 60  ? -23.203 -3.523  -1.533  1.00 41.54  ? 69  TRP   B CD1 1 
ATOM   736  C  CD2 . TRP   B 2 60  ? -22.691 -3.083  -3.662  1.00 40.73  ? 69  TRP   B CD2 1 
ATOM   737  N  NE1 . TRP   B 2 60  ? -22.087 -4.260  -1.860  1.00 41.64  ? 69  TRP   B NE1 1 
ATOM   738  C  CE2 . TRP   B 2 60  ? -21.748 -4.002  -3.158  1.00 41.15  ? 69  TRP   B CE2 1 
ATOM   739  C  CE3 . TRP   B 2 60  ? -22.571 -2.658  -4.994  1.00 41.20  ? 69  TRP   B CE3 1 
ATOM   740  C  CZ2 . TRP   B 2 60  ? -20.688 -4.470  -3.919  1.00 41.55  ? 69  TRP   B CZ2 1 
ATOM   741  C  CZ3 . TRP   B 2 60  ? -21.541 -3.161  -5.759  1.00 41.66  ? 69  TRP   B CZ3 1 
ATOM   742  C  CH2 . TRP   B 2 60  ? -20.632 -4.078  -5.230  1.00 41.53  ? 69  TRP   B CH2 1 
ATOM   743  N  N   . GLY   B 2 61  ? -21.932 -0.268  -2.027  1.00 41.31  ? 70  GLY   B N   1 
ATOM   744  C  CA  . GLY   B 2 61  ? -20.631 0.137   -2.535  1.00 41.96  ? 70  GLY   B CA  1 
ATOM   745  C  C   . GLY   B 2 61  ? -19.501 -0.673  -1.946  1.00 42.28  ? 70  GLY   B C   1 
ATOM   746  O  O   . GLY   B 2 61  ? -19.636 -1.208  -0.854  1.00 42.59  ? 70  GLY   B O   1 
ATOM   747  N  N   . ASP   B 2 62  ? -18.396 -0.799  -2.670  1.00 42.67  ? 71  ASP   B N   1 
ATOM   748  C  CA  . ASP   B 2 62  ? -17.237 -1.558  -2.196  1.00 43.19  ? 71  ASP   B CA  1 
ATOM   749  C  C   . ASP   B 2 62  ? -16.000 -1.031  -2.914  1.00 42.47  ? 71  ASP   B C   1 
ATOM   750  O  O   . ASP   B 2 62  ? -15.913 -1.146  -4.114  1.00 42.69  ? 71  ASP   B O   1 
ATOM   751  C  CB  . ASP   B 2 62  ? -17.424 -3.059  -2.487  1.00 45.66  ? 71  ASP   B CB  1 
ATOM   752  C  CG  . ASP   B 2 62  ? -16.468 -3.967  -1.748  1.00 51.78  ? 71  ASP   B CG  1 
ATOM   753  O  OD1 . ASP   B 2 62  ? -15.284 -4.038  -2.147  1.00 51.71  ? 71  ASP   B OD1 1 
ATOM   754  O  OD2 . ASP   B 2 62  ? -16.905 -4.622  -0.779  1.00 56.15  ? 71  ASP   B OD2 1 
ATOM   755  N  N   . VAL   B 2 63  ? -15.066 -0.431  -2.183  1.00 42.13  ? 72  VAL   B N   1 
ATOM   756  C  CA  . VAL   B 2 63  ? -13.826 0.123   -2.730  1.00 41.51  ? 72  VAL   B CA  1 
ATOM   757  C  C   . VAL   B 2 63  ? -12.935 -0.965  -3.351  1.00 41.78  ? 72  VAL   B C   1 
ATOM   758  O  O   . VAL   B 2 63  ? -12.356 -0.709  -4.398  1.00 42.33  ? 72  VAL   B O   1 
ATOM   759  C  CB  . VAL   B 2 63  ? -13.109 0.971   -1.644  1.00 41.32  ? 72  VAL   B CB  1 
ATOM   760  C  CG1 . VAL   B 2 63  ? -11.624 1.139   -1.906  1.00 40.81  ? 72  VAL   B CG1 1 
ATOM   761  C  CG2 . VAL   B 2 63  ? -13.791 2.327   -1.478  1.00 41.95  ? 72  VAL   B CG2 1 
ATOM   762  N  N   . LYS   B 2 64  ? -12.858 -2.179  -2.766  1.00 41.59  ? 73  LYS   B N   1 
ATOM   763  C  CA  . LYS   B 2 64  ? -12.019 -3.245  -3.353  1.00 41.82  ? 73  LYS   B CA  1 
ATOM   764  C  C   . LYS   B 2 64  ? -12.558 -3.712  -4.696  1.00 42.43  ? 73  LYS   B C   1 
ATOM   765  O  O   . LYS   B 2 64  ? -11.804 -3.843  -5.652  1.00 42.10  ? 73  LYS   B O   1 
ATOM   766  C  CB  . LYS   B 2 64  ? -11.862 -4.435  -2.401  1.00 43.38  ? 73  LYS   B CB  1 
ATOM   767  C  CG  . LYS   B 2 64  ? -10.615 -5.268  -2.706  1.00 46.26  ? 73  LYS   B CG  1 
ATOM   768  C  CD  . LYS   B 2 64  ? -10.624 -6.577  -1.970  1.00 48.93  ? 73  LYS   B CD  1 
ATOM   769  C  CE  . LYS   B 2 64  ? -9.407  -7.395  -2.300  1.00 52.50  ? 73  LYS   B CE  1 
ATOM   770  N  NZ  . LYS   B 2 64  ? -8.500  -7.515  -1.122  1.00 55.62  ? 73  LYS   B NZ  1 
ATOM   771  N  N   . GLN   B 2 65  ? -13.880 -3.938  -4.780  1.00 42.91  ? 74  GLN   B N   1 
ATOM   772  C  CA  . GLN   B 2 65  ? -14.515 -4.328  -6.034  1.00 43.16  ? 74  GLN   B CA  1 
ATOM   773  C  C   . GLN   B 2 65  ? -14.531 -3.176  -7.041  1.00 42.43  ? 74  GLN   B C   1 
ATOM   774  O  O   . GLN   B 2 65  ? -14.609 -3.428  -8.234  1.00 42.81  ? 74  GLN   B O   1 
ATOM   775  C  CB  . GLN   B 2 65  ? -15.955 -4.789  -5.785  1.00 45.77  ? 74  GLN   B CB  1 
ATOM   776  C  CG  . GLN   B 2 65  ? -16.083 -6.130  -5.063  1.00 50.45  ? 74  GLN   B CG  1 
ATOM   777  C  CD  . GLN   B 2 65  ? -17.539 -6.577  -4.962  1.00 55.88  ? 74  GLN   B CD  1 
ATOM   778  O  OE1 . GLN   B 2 65  ? -18.257 -6.696  -5.972  1.00 57.25  ? 74  GLN   B OE1 1 
ATOM   779  N  NE2 . GLN   B 2 65  ? -18.007 -6.842  -3.740  1.00 56.43  ? 74  GLN   B NE2 1 
ATOM   780  N  N   . ASP   B 2 66  ? -14.449 -1.926  -6.553  1.00 41.33  ? 75  ASP   B N   1 
ATOM   781  C  CA  . ASP   B 2 66  ? -14.490 -0.675  -7.295  1.00 40.55  ? 75  ASP   B CA  1 
ATOM   782  C  C   . ASP   B 2 66  ? -15.828 -0.540  -7.991  1.00 39.66  ? 75  ASP   B C   1 
ATOM   783  O  O   . ASP   B 2 66  ? -15.891 -0.142  -9.135  1.00 38.73  ? 75  ASP   B O   1 
ATOM   784  C  CB  . ASP   B 2 66  ? -13.305 -0.497  -8.264  1.00 41.06  ? 75  ASP   B CB  1 
ATOM   785  C  CG  . ASP   B 2 66  ? -13.162 0.933   -8.760  1.00 43.20  ? 75  ASP   B CG  1 
ATOM   786  O  OD1 . ASP   B 2 66  ? -13.465 1.867   -7.980  1.00 42.99  ? 75  ASP   B OD1 1 
ATOM   787  O  OD2 . ASP   B 2 66  ? -12.761 1.117   -9.925  1.00 44.26  ? 75  ASP   B OD2 1 
ATOM   788  N  N   . LEU   B 2 67  ? -16.908 -0.841  -7.272  1.00 39.39  ? 76  LEU   B N   1 
ATOM   789  C  CA  . LEU   B 2 67  ? -18.262 -0.768  -7.799  1.00 38.53  ? 76  LEU   B CA  1 
ATOM   790  C  C   . LEU   B 2 67  ? -19.164 -0.036  -6.828  1.00 38.24  ? 76  LEU   B C   1 
ATOM   791  O  O   . LEU   B 2 67  ? -18.869 0.030   -5.646  1.00 38.36  ? 76  LEU   B O   1 
ATOM   792  C  CB  . LEU   B 2 67  ? -18.800 -2.187  -8.042  1.00 38.34  ? 76  LEU   B CB  1 
ATOM   793  C  CG  . LEU   B 2 67  ? -18.093 -2.989  -9.132  1.00 39.18  ? 76  LEU   B CG  1 
ATOM   794  C  CD1 . LEU   B 2 67  ? -18.641 -4.363  -9.211  1.00 39.40  ? 76  LEU   B CD1 1 
ATOM   795  C  CD2 . LEU   B 2 67  ? -18.228 -2.318  -10.488 1.00 40.06  ? 76  LEU   B CD2 1 
ATOM   796  N  N   . VAL   B 2 68  ? -20.270 0.518   -7.325  1.00 38.09  ? 77  VAL   B N   1 
ATOM   797  C  CA  . VAL   B 2 68  ? -21.269 1.233   -6.514  1.00 37.51  ? 77  VAL   B CA  1 
ATOM   798  C  C   . VAL   B 2 68  ? -22.614 1.210   -7.253  1.00 37.70  ? 77  VAL   B C   1 
ATOM   799  O  O   . VAL   B 2 68  ? -22.646 1.280   -8.468  1.00 37.88  ? 77  VAL   B O   1 
ATOM   800  C  CB  . VAL   B 2 68  ? -20.827 2.686   -6.166  1.00 37.11  ? 77  VAL   B CB  1 
ATOM   801  C  CG1 . VAL   B 2 68  ? -20.597 3.517   -7.425  1.00 37.51  ? 77  VAL   B CG1 1 
ATOM   802  C  CG2 . VAL   B 2 68  ? -21.815 3.366   -5.232  1.00 36.61  ? 77  VAL   B CG2 1 
ATOM   803  N  N   . SER   B 2 69  ? -23.709 1.048   -6.531  1.00 38.18  ? 78  SER   B N   1 
ATOM   804  C  CA  . SER   B 2 69  ? -25.045 1.062   -7.119  1.00 38.53  ? 78  SER   B CA  1 
ATOM   805  C  C   . SER   B 2 69  ? -25.882 2.177   -6.439  1.00 38.30  ? 78  SER   B C   1 
ATOM   806  O  O   . SER   B 2 69  ? -25.656 2.486   -5.277  1.00 37.89  ? 78  SER   B O   1 
ATOM   807  C  CB  . SER   B 2 69  ? -25.708 -0.304  -6.973  1.00 39.30  ? 78  SER   B CB  1 
ATOM   808  O  OG  . SER   B 2 69  ? -26.214 -0.475  -5.661  1.00 39.81  ? 78  SER   B OG  1 
ATOM   809  N  N   . TYR   B 2 70  ? -26.813 2.782   -7.182  1.00 38.41  ? 79  TYR   B N   1 
ATOM   810  C  CA  . TYR   B 2 70  ? -27.677 3.875   -6.729  1.00 39.07  ? 79  TYR   B CA  1 
ATOM   811  C  C   . TYR   B 2 70  ? -29.138 3.445   -6.877  1.00 40.55  ? 79  TYR   B C   1 
ATOM   812  O  O   . TYR   B 2 70  ? -29.482 2.876   -7.898  1.00 41.02  ? 79  TYR   B O   1 
ATOM   813  C  CB  . TYR   B 2 70  ? -27.428 5.131   -7.597  1.00 38.40  ? 79  TYR   B CB  1 
ATOM   814  C  CG  . TYR   B 2 70  ? -26.089 5.778   -7.326  1.00 38.50  ? 79  TYR   B CG  1 
ATOM   815  C  CD1 . TYR   B 2 70  ? -24.913 5.223   -7.816  1.00 39.14  ? 79  TYR   B CD1 1 
ATOM   816  C  CD2 . TYR   B 2 70  ? -25.993 6.919   -6.544  1.00 39.14  ? 79  TYR   B CD2 1 
ATOM   817  C  CE1 . TYR   B 2 70  ? -23.674 5.752   -7.486  1.00 39.61  ? 79  TYR   B CE1 1 
ATOM   818  C  CE2 . TYR   B 2 70  ? -24.761 7.459   -6.211  1.00 39.88  ? 79  TYR   B CE2 1 
ATOM   819  C  CZ  . TYR   B 2 70  ? -23.602 6.871   -6.686  1.00 40.98  ? 79  TYR   B CZ  1 
ATOM   820  O  OH  . TYR   B 2 70  ? -22.386 7.433   -6.408  1.00 43.02  ? 79  TYR   B OH  1 
ATOM   821  N  N   . CYS   B 2 71  ? -29.970 3.656   -5.844  1.00 41.37  ? 80  CYS   B N   1 
ATOM   822  C  CA  . CYS   B 2 71  ? -31.417 3.367   -5.821  1.00 42.46  ? 80  CYS   B CA  1 
ATOM   823  C  C   . CYS   B 2 71  ? -31.773 1.908   -5.481  1.00 41.46  ? 80  CYS   B C   1 
ATOM   824  O  O   . CYS   B 2 71  ? -32.913 1.640   -5.082  1.00 41.79  ? 80  CYS   B O   1 
ATOM   825  C  CB  . CYS   B 2 71  ? -32.111 3.828   -7.100  1.00 44.90  ? 80  CYS   B CB  1 
ATOM   826  S  SG  . CYS   B 2 71  ? -31.869 5.589   -7.480  1.00 53.38  ? 80  CYS   B SG  1 
ATOM   827  N  N   . GLY   B 2 72  ? -30.812 0.999   -5.584  1.00 39.71  ? 81  GLY   B N   1 
ATOM   828  C  CA  . GLY   B 2 72  ? -31.073 -0.395  -5.268  1.00 38.72  ? 81  GLY   B CA  1 
ATOM   829  C  C   . GLY   B 2 72  ? -29.846 -1.260  -5.331  1.00 37.91  ? 81  GLY   B C   1 
ATOM   830  O  O   . GLY   B 2 72  ? -28.744 -0.784  -5.613  1.00 38.07  ? 81  GLY   B O   1 
ATOM   831  N  N   . PRO   B 2 73  ? -30.006 -2.549  -5.029  1.00 37.34  ? 82  PRO   B N   1 
ATOM   832  C  CA  . PRO   B 2 73  ? -28.839 -3.449  -5.090  1.00 37.76  ? 82  PRO   B CA  1 
ATOM   833  C  C   . PRO   B 2 73  ? -28.341 -3.663  -6.514  1.00 39.01  ? 82  PRO   B C   1 
ATOM   834  O  O   . PRO   B 2 73  ? -29.102 -3.497  -7.475  1.00 38.88  ? 82  PRO   B O   1 
ATOM   835  C  CB  . PRO   B 2 73  ? -29.363 -4.760  -4.488  1.00 38.31  ? 82  PRO   B CB  1 
ATOM   836  C  CG  . PRO   B 2 73  ? -30.864 -4.704  -4.668  1.00 38.39  ? 82  PRO   B CG  1 
ATOM   837  C  CD  . PRO   B 2 73  ? -31.256 -3.250  -4.665  1.00 36.28  ? 82  PRO   B CD  1 
ATOM   838  N  N   . TRP   B 2 74  ? -27.075 -4.112  -6.670  1.00 39.79  ? 83  TRP   B N   1 
ATOM   839  C  CA  . TRP   B 2 74  ? -26.486 -4.442  -7.974  1.00 40.68  ? 83  TRP   B CA  1 
ATOM   840  C  C   . TRP   B 2 74  ? -27.411 -5.409  -8.749  1.00 42.61  ? 83  TRP   B C   1 
ATOM   841  O  O   . TRP   B 2 74  ? -27.862 -6.392  -8.167  1.00 43.19  ? 83  TRP   B O   1 
ATOM   842  C  CB  . TRP   B 2 74  ? -25.112 -5.081  -7.761  1.00 40.46  ? 83  TRP   B CB  1 
ATOM   843  C  CG  . TRP   B 2 74  ? -24.274 -5.146  -8.991  1.00 40.75  ? 83  TRP   B CG  1 
ATOM   844  C  CD1 . TRP   B 2 74  ? -24.144 -6.203  -9.839  1.00 41.27  ? 83  TRP   B CD1 1 
ATOM   845  C  CD2 . TRP   B 2 74  ? -23.471 -4.091  -9.534  1.00 40.95  ? 83  TRP   B CD2 1 
ATOM   846  N  NE1 . TRP   B 2 74  ? -23.281 -5.886  -10.856 1.00 41.60  ? 83  TRP   B NE1 1 
ATOM   847  C  CE2 . TRP   B 2 74  ? -22.867 -4.587  -10.706 1.00 41.51  ? 83  TRP   B CE2 1 
ATOM   848  C  CE3 . TRP   B 2 74  ? -23.206 -2.767  -9.142  1.00 41.41  ? 83  TRP   B CE3 1 
ATOM   849  C  CZ2 . TRP   B 2 74  ? -22.027 -3.805  -11.503 1.00 42.50  ? 83  TRP   B CZ2 1 
ATOM   850  C  CZ3 . TRP   B 2 74  ? -22.362 -1.999  -9.920  1.00 42.24  ? 83  TRP   B CZ3 1 
ATOM   851  C  CH2 . TRP   B 2 74  ? -21.792 -2.511  -11.094 1.00 42.60  ? 83  TRP   B CH2 1 
ATOM   852  N  N   . LYS   B 2 75  ? -27.773 -5.074  -10.008 1.00 43.40  ? 84  LYS   B N   1 
ATOM   853  C  CA  . LYS   B 2 75  ? -28.718 -5.851  -10.813 1.00 44.57  ? 84  LYS   B CA  1 
ATOM   854  C  C   . LYS   B 2 75  ? -28.073 -6.652  -11.951 1.00 46.42  ? 84  LYS   B C   1 
ATOM   855  O  O   . LYS   B 2 75  ? -28.728 -7.528  -12.517 1.00 46.68  ? 84  LYS   B O   1 
ATOM   856  C  CB  . LYS   B 2 75  ? -29.783 -4.919  -11.415 1.00 45.29  ? 84  LYS   B CB  1 
ATOM   857  C  CG  . LYS   B 2 75  ? -30.648 -4.186  -10.402 1.00 47.49  ? 84  LYS   B CG  1 
ATOM   858  C  CD  . LYS   B 2 75  ? -31.680 -5.094  -9.779  1.00 49.86  ? 84  LYS   B CD  1 
ATOM   859  C  CE  . LYS   B 2 75  ? -32.313 -4.479  -8.559  1.00 52.21  ? 84  LYS   B CE  1 
ATOM   860  N  NZ  . LYS   B 2 75  ? -33.676 -3.986  -8.857  1.00 54.12  ? 84  LYS   B NZ  1 
ATOM   861  N  N   . LEU   B 2 76  ? -26.825 -6.311  -12.330 1.00 47.40  ? 85  LEU   B N   1 
ATOM   862  C  CA  . LEU   B 2 76  ? -26.082 -6.913  -13.448 1.00 48.05  ? 85  LEU   B CA  1 
ATOM   863  C  C   . LEU   B 2 76  ? -25.430 -8.239  -13.050 1.00 50.47  ? 85  LEU   B C   1 
ATOM   864  O  O   . LEU   B 2 76  ? -24.507 -8.244  -12.245 1.00 50.98  ? 85  LEU   B O   1 
ATOM   865  C  CB  . LEU   B 2 76  ? -25.018 -5.925  -13.949 1.00 47.02  ? 85  LEU   B CB  1 
ATOM   866  C  CG  . LEU   B 2 76  ? -25.476 -4.497  -14.202 1.00 47.66  ? 85  LEU   B CG  1 
ATOM   867  C  CD1 . LEU   B 2 76  ? -24.321 -3.598  -14.560 1.00 47.69  ? 85  LEU   B CD1 1 
ATOM   868  C  CD2 . LEU   B 2 76  ? -26.517 -4.438  -15.285 1.00 48.43  ? 85  LEU   B CD2 1 
ATOM   869  N  N   . ASP   B 2 77  ? -25.864 -9.359  -13.641 1.00 52.47  ? 86  ASP   B N   1 
ATOM   870  C  CA  . ASP   B 2 77  ? -25.348 -10.682 -13.255 1.00 54.98  ? 86  ASP   B CA  1 
ATOM   871  C  C   . ASP   B 2 77  ? -24.704 -11.525 -14.370 1.00 56.54  ? 86  ASP   B C   1 
ATOM   872  O  O   . ASP   B 2 77  ? -24.033 -12.513 -14.054 1.00 57.31  ? 86  ASP   B O   1 
ATOM   873  C  CB  . ASP   B 2 77  ? -26.442 -11.516 -12.566 1.00 57.60  ? 86  ASP   B CB  1 
ATOM   874  C  CG  . ASP   B 2 77  ? -27.760 -11.602 -13.320 1.00 65.37  ? 86  ASP   B CG  1 
ATOM   875  O  OD1 . ASP   B 2 77  ? -27.873 -10.977 -14.408 1.00 66.77  ? 86  ASP   B OD1 1 
ATOM   876  O  OD2 . ASP   B 2 77  ? -28.686 -12.290 -12.822 1.00 68.82  ? 86  ASP   B OD2 1 
ATOM   877  N  N   . ALA   B 2 78  ? -24.885 -11.155 -15.643 1.00 56.63  ? 87  ALA   B N   1 
ATOM   878  C  CA  . ALA   B 2 78  ? -24.306 -11.901 -16.761 1.00 57.06  ? 87  ALA   B CA  1 
ATOM   879  C  C   . ALA   B 2 78  ? -22.768 -12.012 -16.665 1.00 57.68  ? 87  ALA   B C   1 
ATOM   880  O  O   . ALA   B 2 78  ? -22.109 -11.119 -16.126 1.00 57.49  ? 87  ALA   B O   1 
ATOM   881  C  CB  . ALA   B 2 78  ? -24.715 -11.264 -18.078 1.00 56.82  ? 87  ALA   B CB  1 
ATOM   882  N  N   . ALA   B 2 79  ? -22.209 -13.135 -17.129 1.00 58.16  ? 88  ALA   B N   1 
ATOM   883  C  CA  . ALA   B 2 79  ? -20.766 -13.342 -17.058 1.00 59.03  ? 88  ALA   B CA  1 
ATOM   884  C  C   . ALA   B 2 79  ? -20.148 -13.722 -18.390 1.00 60.00  ? 88  ALA   B C   1 
ATOM   885  O  O   . ALA   B 2 79  ? -20.822 -14.317 -19.230 1.00 60.20  ? 88  ALA   B O   1 
ATOM   886  C  CB  . ALA   B 2 79  ? -20.450 -14.392 -16.019 1.00 59.42  ? 88  ALA   B CB  1 
ATOM   887  N  N   . TRP   B 2 80  ? -18.868 -13.352 -18.597 1.00 60.57  ? 89  TRP   B N   1 
ATOM   888  C  CA  . TRP   B 2 80  ? -18.126 -13.709 -19.806 1.00 61.79  ? 89  TRP   B CA  1 
ATOM   889  C  C   . TRP   B 2 80  ? -17.943 -15.235 -19.814 1.00 62.38  ? 89  TRP   B C   1 
ATOM   890  O  O   . TRP   B 2 80  ? -17.715 -15.821 -18.760 1.00 62.20  ? 89  TRP   B O   1 
ATOM   891  C  CB  . TRP   B 2 80  ? -16.759 -12.997 -19.846 1.00 62.10  ? 89  TRP   B CB  1 
ATOM   892  C  CG  . TRP   B 2 80  ? -15.922 -13.332 -21.057 1.00 62.82  ? 89  TRP   B CG  1 
ATOM   893  C  CD1 . TRP   B 2 80  ? -16.307 -13.264 -22.363 1.00 63.81  ? 89  TRP   B CD1 1 
ATOM   894  C  CD2 . TRP   B 2 80  ? -14.532 -13.677 -21.066 1.00 62.79  ? 89  TRP   B CD2 1 
ATOM   895  N  NE1 . TRP   B 2 80  ? -15.256 -13.589 -23.184 1.00 64.14  ? 89  TRP   B NE1 1 
ATOM   896  C  CE2 . TRP   B 2 80  ? -14.153 -13.853 -22.412 1.00 63.82  ? 89  TRP   B CE2 1 
ATOM   897  C  CE3 . TRP   B 2 80  ? -13.582 -13.907 -20.065 1.00 63.37  ? 89  TRP   B CE3 1 
ATOM   898  C  CZ2 . TRP   B 2 80  ? -12.869 -14.272 -22.779 1.00 64.19  ? 89  TRP   B CZ2 1 
ATOM   899  C  CZ3 . TRP   B 2 80  ? -12.309 -14.306 -20.432 1.00 64.23  ? 89  TRP   B CZ3 1 
ATOM   900  C  CH2 . TRP   B 2 80  ? -11.958 -14.457 -21.774 1.00 64.29  ? 89  TRP   B CH2 1 
ATOM   901  N  N   . ASP   B 2 81  ? -18.096 -15.882 -20.977 1.00 63.28  ? 90  ASP   B N   1 
ATOM   902  C  CA  . ASP   B 2 81  ? -17.996 -17.344 -21.050 1.00 64.66  ? 90  ASP   B CA  1 
ATOM   903  C  C   . ASP   B 2 81  ? -16.571 -17.892 -21.196 1.00 65.65  ? 90  ASP   B C   1 
ATOM   904  O  O   . ASP   B 2 81  ? -16.404 -19.102 -21.248 1.00 65.81  ? 90  ASP   B O   1 
ATOM   905  C  CB  . ASP   B 2 81  ? -18.903 -17.917 -22.150 1.00 66.61  ? 90  ASP   B CB  1 
ATOM   906  C  CG  . ASP   B 2 81  ? -18.653 -17.381 -23.549 1.00 71.64  ? 90  ASP   B CG  1 
ATOM   907  O  OD1 . ASP   B 2 81  ? -17.691 -16.605 -23.726 1.00 73.01  ? 90  ASP   B OD1 1 
ATOM   908  O  OD2 . ASP   B 2 81  ? -19.421 -17.735 -24.467 1.00 72.96  ? 90  ASP   B OD2 1 
ATOM   909  N  N   . GLY   B 2 82  ? -15.576 -17.015 -21.286 1.00 66.46  ? 91  GLY   B N   1 
ATOM   910  C  CA  . GLY   B 2 82  ? -14.183 -17.413 -21.434 1.00 67.88  ? 91  GLY   B CA  1 
ATOM   911  C  C   . GLY   B 2 82  ? -13.755 -17.725 -22.857 1.00 69.30  ? 91  GLY   B C   1 
ATOM   912  O  O   . GLY   B 2 82  ? -12.567 -17.950 -23.112 1.00 69.89  ? 91  GLY   B O   1 
ATOM   913  N  N   . LEU   B 2 83  ? -14.710 -17.762 -23.805 1.00 69.40  ? 92  LEU   B N   1 
ATOM   914  C  CA  . LEU   B 2 83  ? -14.398 -18.092 -25.186 1.00 70.18  ? 92  LEU   B CA  1 
ATOM   915  C  C   . LEU   B 2 83  ? -14.841 -17.030 -26.180 1.00 71.04  ? 92  LEU   B C   1 
ATOM   916  O  O   . LEU   B 2 83  ? -14.132 -16.782 -27.152 1.00 71.68  ? 92  LEU   B O   1 
ATOM   917  C  CB  . LEU   B 2 83  ? -15.073 -19.416 -25.571 1.00 70.67  ? 92  LEU   B CB  1 
ATOM   918  C  CG  . LEU   B 2 83  ? -14.749 -20.626 -24.733 1.00 72.75  ? 92  LEU   B CG  1 
ATOM   919  C  CD1 . LEU   B 2 83  ? -15.544 -21.825 -25.204 1.00 73.68  ? 92  LEU   B CD1 1 
ATOM   920  C  CD2 . LEU   B 2 83  ? -13.271 -20.925 -24.773 1.00 73.40  ? 92  LEU   B CD2 1 
ATOM   921  N  N   . SER   B 2 84  ? -16.044 -16.469 -26.002 1.00 70.84  ? 93  SER   B N   1 
ATOM   922  C  CA  . SER   B 2 84  ? -16.617 -15.510 -26.947 1.00 70.96  ? 93  SER   B CA  1 
ATOM   923  C  C   . SER   B 2 84  ? -16.011 -14.120 -26.918 1.00 70.15  ? 93  SER   B C   1 
ATOM   924  O  O   . SER   B 2 84  ? -15.525 -13.660 -25.882 1.00 70.64  ? 93  SER   B O   1 
ATOM   925  C  CB  . SER   B 2 84  ? -18.123 -15.378 -26.727 1.00 73.11  ? 93  SER   B CB  1 
ATOM   926  O  OG  . SER   B 2 84  ? -18.766 -16.638 -26.744 1.00 76.43  ? 93  SER   B OG  1 
ATOM   927  N  N   . GLU   B 2 85  ? -16.106 -13.429 -28.063 1.00 68.72  ? 94  GLU   B N   1 
ATOM   928  C  CA  . GLU   B 2 85  ? -15.711 -12.040 -28.202 1.00 67.58  ? 94  GLU   B CA  1 
ATOM   929  C  C   . GLU   B 2 85  ? -16.808 -11.209 -27.509 1.00 65.51  ? 94  GLU   B C   1 
ATOM   930  O  O   . GLU   B 2 85  ? -17.936 -11.675 -27.309 1.00 65.77  ? 94  GLU   B O   1 
ATOM   931  C  CB  . GLU   B 2 85  ? -15.583 -11.634 -29.699 1.00 69.78  ? 94  GLU   B CB  1 
ATOM   932  C  CG  . GLU   B 2 85  ? -14.458 -12.326 -30.465 1.00 73.15  ? 94  GLU   B CG  1 
ATOM   933  C  CD  . GLU   B 2 85  ? -13.788 -11.492 -31.550 1.00 75.09  ? 94  GLU   B CD  1 
ATOM   934  O  OE1 . GLU   B 2 85  ? -14.433 -10.555 -32.075 1.00 73.11  ? 94  GLU   B OE1 1 
ATOM   935  O  OE2 . GLU   B 2 85  ? -12.612 -11.779 -31.872 1.00 75.90  ? 94  GLU   B OE2 1 
ATOM   936  N  N   . VAL   B 2 86  ? -16.458 -10.005 -27.089 1.00 63.36  ? 95  VAL   B N   1 
ATOM   937  C  CA  . VAL   B 2 86  ? -17.363 -9.117  -26.364 1.00 61.90  ? 95  VAL   B CA  1 
ATOM   938  C  C   . VAL   B 2 86  ? -17.350 -7.718  -27.008 1.00 61.34  ? 95  VAL   B C   1 
ATOM   939  O  O   . VAL   B 2 86  ? -16.483 -7.421  -27.840 1.00 61.75  ? 95  VAL   B O   1 
ATOM   940  C  CB  . VAL   B 2 86  ? -16.976 -9.040  -24.850 1.00 61.16  ? 95  VAL   B CB  1 
ATOM   941  C  CG1 . VAL   B 2 86  ? -16.808 -10.426 -24.232 1.00 61.12  ? 95  VAL   B CG1 1 
ATOM   942  C  CG2 . VAL   B 2 86  ? -15.724 -8.195  -24.652 1.00 61.14  ? 95  VAL   B CG2 1 
ATOM   943  N  N   . GLN   B 2 87  ? -18.292 -6.845  -26.610 1.00 60.12  ? 96  GLN   B N   1 
ATOM   944  C  CA  . GLN   B 2 87  ? -18.296 -5.484  -27.120 1.00 59.08  ? 96  GLN   B CA  1 
ATOM   945  C  C   . GLN   B 2 87  ? -18.160 -4.489  -25.998 1.00 57.54  ? 96  GLN   B C   1 
ATOM   946  O  O   . GLN   B 2 87  ? -18.865 -4.597  -25.006 1.00 57.57  ? 96  GLN   B O   1 
ATOM   947  C  CB  . GLN   B 2 87  ? -19.519 -5.200  -28.005 1.00 60.29  ? 96  GLN   B CB  1 
ATOM   948  C  CG  . GLN   B 2 87  ? -19.207 -5.445  -29.469 1.00 63.79  ? 96  GLN   B CG  1 
ATOM   949  C  CD  . GLN   B 2 87  ? -20.397 -5.324  -30.387 1.00 67.70  ? 96  GLN   B CD  1 
ATOM   950  O  OE1 . GLN   B 2 87  ? -21.325 -4.551  -30.162 1.00 67.92  ? 96  GLN   B OE1 1 
ATOM   951  N  NE2 . GLN   B 2 87  ? -20.390 -6.090  -31.459 1.00 68.59  ? 96  GLN   B NE2 1 
ATOM   952  N  N   . LEU   B 2 88  ? -17.239 -3.537  -26.138 1.00 55.98  ? 97  LEU   B N   1 
ATOM   953  C  CA  . LEU   B 2 88  ? -17.119 -2.468  -25.169 1.00 54.87  ? 97  LEU   B CA  1 
ATOM   954  C  C   . LEU   B 2 88  ? -17.959 -1.321  -25.727 1.00 54.17  ? 97  LEU   B C   1 
ATOM   955  O  O   . LEU   B 2 88  ? -17.622 -0.760  -26.768 1.00 54.27  ? 97  LEU   B O   1 
ATOM   956  C  CB  . LEU   B 2 88  ? -15.662 -2.016  -24.959 1.00 54.66  ? 97  LEU   B CB  1 
ATOM   957  C  CG  . LEU   B 2 88  ? -15.474 -0.706  -24.169 1.00 55.74  ? 97  LEU   B CG  1 
ATOM   958  C  CD1 . LEU   B 2 88  ? -16.140 -0.762  -22.799 1.00 56.36  ? 97  LEU   B CD1 1 
ATOM   959  C  CD2 . LEU   B 2 88  ? -14.021 -0.318  -24.069 1.00 56.12  ? 97  LEU   B CD2 1 
ATOM   960  N  N   . LEU   B 2 89  ? -19.069 -1.003  -25.065 1.00 53.28  ? 98  LEU   B N   1 
ATOM   961  C  CA  . LEU   B 2 89  ? -19.889 0.122   -25.468 1.00 52.40  ? 98  LEU   B CA  1 
ATOM   962  C  C   . LEU   B 2 89  ? -19.207 1.294   -24.783 1.00 52.90  ? 98  LEU   B C   1 
ATOM   963  O  O   . LEU   B 2 89  ? -19.548 1.650   -23.650 1.00 53.03  ? 98  LEU   B O   1 
ATOM   964  C  CB  . LEU   B 2 89  ? -21.337 -0.064  -24.989 1.00 51.62  ? 98  LEU   B CB  1 
ATOM   965  C  CG  . LEU   B 2 89  ? -22.355 1.088   -25.177 1.00 51.75  ? 98  LEU   B CG  1 
ATOM   966  C  CD1 . LEU   B 2 89  ? -22.144 1.869   -26.463 1.00 51.48  ? 98  LEU   B CD1 1 
ATOM   967  C  CD2 . LEU   B 2 89  ? -23.760 0.566   -25.103 1.00 52.13  ? 98  LEU   B CD2 1 
ATOM   968  N  N   . ALA   B 2 90  ? -18.158 1.821   -25.434 1.00 52.58  ? 99  ALA   B N   1 
ATOM   969  C  CA  . ALA   B 2 90  ? -17.358 2.899   -24.876 1.00 52.78  ? 99  ALA   B CA  1 
ATOM   970  C  C   . ALA   B 2 90  ? -18.084 4.226   -25.004 1.00 53.17  ? 99  ALA   B C   1 
ATOM   971  O  O   . ALA   B 2 90  ? -18.574 4.536   -26.078 1.00 54.15  ? 99  ALA   B O   1 
ATOM   972  C  CB  . ALA   B 2 90  ? -16.020 2.976   -25.589 1.00 52.39  ? 99  ALA   B CB  1 
ATOM   973  N  N   . VAL   B 2 91  ? -18.156 5.011   -23.925 1.00 52.47  ? 100 VAL   B N   1 
ATOM   974  C  CA  . VAL   B 2 91  ? -18.769 6.329   -23.967 1.00 52.71  ? 100 VAL   B CA  1 
ATOM   975  C  C   . VAL   B 2 91  ? -17.678 7.357   -23.608 1.00 53.47  ? 100 VAL   B C   1 
ATOM   976  O  O   . VAL   B 2 91  ? -17.505 7.708   -22.439 1.00 53.59  ? 100 VAL   B O   1 
ATOM   977  C  CB  . VAL   B 2 91  ? -19.997 6.398   -23.037 1.00 52.43  ? 100 VAL   B CB  1 
ATOM   978  C  CG1 . VAL   B 2 91  ? -20.650 7.771   -23.091 1.00 52.68  ? 100 VAL   B CG1 1 
ATOM   979  C  CG2 . VAL   B 2 91  ? -21.001 5.307   -23.380 1.00 52.32  ? 100 VAL   B CG2 1 
ATOM   980  N  N   . PRO   B 2 92  ? -16.885 7.804   -24.599 1.00 53.55  ? 101 PRO   B N   1 
ATOM   981  C  CA  . PRO   B 2 92  ? -15.753 8.687   -24.284 1.00 53.98  ? 101 PRO   B CA  1 
ATOM   982  C  C   . PRO   B 2 92  ? -16.121 10.143  -24.062 1.00 54.80  ? 101 PRO   B C   1 
ATOM   983  O  O   . PRO   B 2 92  ? -17.105 10.614  -24.625 1.00 55.23  ? 101 PRO   B O   1 
ATOM   984  C  CB  . PRO   B 2 92  ? -14.801 8.491   -25.480 1.00 54.79  ? 101 PRO   B CB  1 
ATOM   985  C  CG  . PRO   B 2 92  ? -15.453 7.454   -26.382 1.00 55.11  ? 101 PRO   B CG  1 
ATOM   986  C  CD  . PRO   B 2 92  ? -16.910 7.460   -26.029 1.00 53.29  ? 101 PRO   B CD  1 
ATOM   987  N  N   . PRO   B 2 93  ? -15.350 10.879  -23.237 1.00 54.97  ? 102 PRO   B N   1 
ATOM   988  C  CA  . PRO   B 2 93  ? -15.689 12.300  -22.993 1.00 55.16  ? 102 PRO   B CA  1 
ATOM   989  C  C   . PRO   B 2 93  ? -15.824 13.125  -24.262 1.00 56.14  ? 102 PRO   B C   1 
ATOM   990  O  O   . PRO   B 2 93  ? -14.959 13.064  -25.146 1.00 56.11  ? 102 PRO   B O   1 
ATOM   991  C  CB  . PRO   B 2 93  ? -14.531 12.806  -22.122 1.00 55.81  ? 102 PRO   B CB  1 
ATOM   992  C  CG  . PRO   B 2 93  ? -13.951 11.557  -21.472 1.00 55.99  ? 102 PRO   B CG  1 
ATOM   993  C  CD  . PRO   B 2 93  ? -14.167 10.443  -22.460 1.00 54.23  ? 102 PRO   B CD  1 
ATOM   994  N  N   . GLY   B 2 94  ? -16.938 13.854  -24.367 1.00 56.58  ? 103 GLY   B N   1 
ATOM   995  C  CA  . GLY   B 2 94  ? -17.232 14.705  -25.516 1.00 57.17  ? 103 GLY   B CA  1 
ATOM   996  C  C   . GLY   B 2 94  ? -17.451 13.996  -26.844 1.00 57.82  ? 103 GLY   B C   1 
ATOM   997  O  O   . GLY   B 2 94  ? -17.603 14.646  -27.871 1.00 57.57  ? 103 GLY   B O   1 
ATOM   998  N  N   . GLU   B 2 95  ? -17.420 12.666  -26.853 1.00 58.86  ? 104 GLU   B N   1 
ATOM   999  C  CA  . GLU   B 2 95  ? -17.604 11.883  -28.072 1.00 60.03  ? 104 GLU   B CA  1 
ATOM   1000 C  C   . GLU   B 2 95  ? -18.840 10.979  -27.953 1.00 61.01  ? 104 GLU   B C   1 
ATOM   1001 O  O   . GLU   B 2 95  ? -19.288 10.692  -26.849 1.00 61.27  ? 104 GLU   B O   1 
ATOM   1002 C  CB  . GLU   B 2 95  ? -16.324 11.066  -28.387 1.00 61.81  ? 104 GLU   B CB  1 
ATOM   1003 C  CG  . GLU   B 2 95  ? -15.118 11.941  -28.718 1.00 66.66  ? 104 GLU   B CG  1 
ATOM   1004 C  CD  . GLU   B 2 95  ? -13.748 11.279  -28.658 1.00 73.69  ? 104 GLU   B CD  1 
ATOM   1005 O  OE1 . GLU   B 2 95  ? -13.676 10.074  -28.324 1.00 73.50  ? 104 GLU   B OE1 1 
ATOM   1006 O  OE2 . GLU   B 2 95  ? -12.741 11.971  -28.941 1.00 76.03  ? 104 GLU   B OE2 1 
ATOM   1007 N  N   . ARG   B 2 96  ? -19.385 10.527  -29.077 1.00 61.62  ? 105 ARG   B N   1 
ATOM   1008 C  CA  . ARG   B 2 96  ? -20.558 9.658   -29.102 1.00 63.19  ? 105 ARG   B CA  1 
ATOM   1009 C  C   . ARG   B 2 96  ? -20.243 8.229   -28.619 1.00 63.93  ? 105 ARG   B C   1 
ATOM   1010 O  O   . ARG   B 2 96  ? -19.092 7.783   -28.719 1.00 63.86  ? 105 ARG   B O   1 
ATOM   1011 C  CB  . ARG   B 2 96  ? -21.062 9.588   -30.544 1.00 66.39  ? 105 ARG   B CB  1 
ATOM   1012 C  CG  . ARG   B 2 96  ? -22.554 9.314   -30.706 1.00 73.19  ? 105 ARG   B CG  1 
ATOM   1013 C  CD  . ARG   B 2 96  ? -23.155 9.979   -31.945 1.00 79.55  ? 105 ARG   B CD  1 
ATOM   1014 N  NE  . ARG   B 2 96  ? -22.322 9.833   -33.146 1.00 85.90  ? 105 ARG   B NE  1 
ATOM   1015 C  CZ  . ARG   B 2 96  ? -21.853 10.855  -33.861 1.00 90.01  ? 105 ARG   B CZ  1 
ATOM   1016 N  NH1 . ARG   B 2 96  ? -22.135 12.103  -33.513 1.00 89.32  ? 105 ARG   B NH1 1 
ATOM   1017 N  NH2 . ARG   B 2 96  ? -21.100 10.634  -34.933 1.00 90.85  ? 105 ARG   B NH2 1 
ATOM   1018 N  N   . ALA   B 2 97  ? -21.282 7.496   -28.150 1.00 63.80  ? 106 ALA   B N   1 
ATOM   1019 C  CA  . ALA   B 2 97  ? -21.191 6.091   -27.750 1.00 64.08  ? 106 ALA   B CA  1 
ATOM   1020 C  C   . ALA   B 2 97  ? -20.661 5.254   -28.932 1.00 64.96  ? 106 ALA   B C   1 
ATOM   1021 O  O   . ALA   B 2 97  ? -21.087 5.461   -30.062 1.00 65.49  ? 106 ALA   B O   1 
ATOM   1022 C  CB  . ALA   B 2 97  ? -22.566 5.591   -27.343 1.00 63.73  ? 106 ALA   B CB  1 
ATOM   1023 N  N   . LYS   B 2 98  ? -19.734 4.325   -28.683 1.00 65.38  ? 107 LYS   B N   1 
ATOM   1024 C  CA  . LYS   B 2 98  ? -19.122 3.522   -29.740 1.00 65.74  ? 107 LYS   B CA  1 
ATOM   1025 C  C   . LYS   B 2 98  ? -18.959 2.063   -29.335 1.00 65.29  ? 107 LYS   B C   1 
ATOM   1026 O  O   . LYS   B 2 98  ? -18.342 1.811   -28.320 1.00 65.95  ? 107 LYS   B O   1 
ATOM   1027 C  CB  . LYS   B 2 98  ? -17.732 4.104   -30.024 1.00 68.69  ? 107 LYS   B CB  1 
ATOM   1028 C  CG  . LYS   B 2 98  ? -17.228 3.907   -31.447 1.00 74.13  ? 107 LYS   B CG  1 
ATOM   1029 C  CD  . LYS   B 2 98  ? -15.960 4.727   -31.737 1.00 78.89  ? 107 LYS   B CD  1 
ATOM   1030 C  CE  . LYS   B 2 98  ? -14.875 4.554   -30.693 1.00 81.80  ? 107 LYS   B CE  1 
ATOM   1031 N  NZ  . LYS   B 2 98  ? -13.507 4.613   -31.282 1.00 83.35  ? 107 LYS   B NZ  1 
ATOM   1032 N  N   . ASN   B 2 99  ? -19.445 1.098   -30.132 1.00 64.52  ? 108 ASN   B N   1 
ATOM   1033 C  CA  . ASN   B 2 99  ? -19.262 -0.329  -29.817 1.00 64.05  ? 108 ASN   B CA  1 
ATOM   1034 C  C   . ASN   B 2 99  ? -17.934 -0.854  -30.395 1.00 64.45  ? 108 ASN   B C   1 
ATOM   1035 O  O   . ASN   B 2 99  ? -17.728 -0.806  -31.599 1.00 64.75  ? 108 ASN   B O   1 
ATOM   1036 C  CB  . ASN   B 2 99  ? -20.433 -1.181  -30.329 1.00 63.90  ? 108 ASN   B CB  1 
ATOM   1037 C  CG  . ASN   B 2 99  ? -21.710 -1.046  -29.530 1.00 65.40  ? 108 ASN   B CG  1 
ATOM   1038 O  OD1 . ASN   B 2 99  ? -22.232 0.049   -29.330 1.00 66.43  ? 108 ASN   B OD1 1 
ATOM   1039 N  ND2 . ASN   B 2 99  ? -22.266 -2.155  -29.074 1.00 64.55  ? 108 ASN   B ND2 1 
ATOM   1040 N  N   . ILE   B 2 100 ? -17.032 -1.335  -29.542 1.00 64.27  ? 109 ILE   B N   1 
ATOM   1041 C  CA  . ILE   B 2 100 ? -15.738 -1.852  -29.984 1.00 64.58  ? 109 ILE   B CA  1 
ATOM   1042 C  C   . ILE   B 2 100 ? -15.625 -3.316  -29.657 1.00 64.65  ? 109 ILE   B C   1 
ATOM   1043 O  O   . ILE   B 2 100 ? -15.404 -3.662  -28.504 1.00 64.89  ? 109 ILE   B O   1 
ATOM   1044 C  CB  . ILE   B 2 100 ? -14.570 -1.091  -29.335 1.00 65.31  ? 109 ILE   B CB  1 
ATOM   1045 C  CG1 . ILE   B 2 100 ? -14.739 0.424   -29.474 1.00 66.57  ? 109 ILE   B CG1 1 
ATOM   1046 C  CG2 . ILE   B 2 100 ? -13.226 -1.578  -29.895 1.00 65.89  ? 109 ILE   B CG2 1 
ATOM   1047 C  CD1 . ILE   B 2 100 ? -14.751 0.903   -30.909 1.00 68.02  ? 109 ILE   B CD1 1 
ATOM   1048 N  N   . GLN   B 2 101 ? -15.735 -4.179  -30.662 1.00 64.68  ? 110 GLN   B N   1 
ATOM   1049 C  CA  . GLN   B 2 101 ? -15.659 -5.612  -30.440 1.00 64.86  ? 110 GLN   B CA  1 
ATOM   1050 C  C   . GLN   B 2 101 ? -14.227 -6.065  -30.244 1.00 64.87  ? 110 GLN   B C   1 
ATOM   1051 O  O   . GLN   B 2 101 ? -13.336 -5.643  -30.968 1.00 64.76  ? 110 GLN   B O   1 
ATOM   1052 C  CB  . GLN   B 2 101 ? -16.338 -6.367  -31.579 1.00 66.47  ? 110 GLN   B CB  1 
ATOM   1053 C  CG  . GLN   B 2 101 ? -16.705 -7.789  -31.206 1.00 69.31  ? 110 GLN   B CG  1 
ATOM   1054 C  CD  . GLN   B 2 101 ? -17.488 -8.408  -32.326 1.00 71.76  ? 110 GLN   B CD  1 
ATOM   1055 O  OE1 . GLN   B 2 101 ? -18.490 -7.859  -32.801 1.00 71.21  ? 110 GLN   B OE1 1 
ATOM   1056 N  NE2 . GLN   B 2 101 ? -17.043 -9.565  -32.768 1.00 72.23  ? 110 GLN   B NE2 1 
ATOM   1057 N  N   . THR   B 2 102 ? -13.991 -6.883  -29.216 1.00 64.84  ? 111 THR   B N   1 
ATOM   1058 C  CA  . THR   B 2 102 ? -12.664 -7.393  -28.900 1.00 64.58  ? 111 THR   B CA  1 
ATOM   1059 C  C   . THR   B 2 102 ? -12.773 -8.772  -28.265 1.00 64.27  ? 111 THR   B C   1 
ATOM   1060 O  O   . THR   B 2 102 ? -13.855 -9.144  -27.822 1.00 64.61  ? 111 THR   B O   1 
ATOM   1061 C  CB  . THR   B 2 102 ? -11.961 -6.404  -27.961 1.00 66.35  ? 111 THR   B CB  1 
ATOM   1062 O  OG1 . THR   B 2 102 ? -10.588 -6.773  -27.814 1.00 68.30  ? 111 THR   B OG1 1 
ATOM   1063 C  CG2 . THR   B 2 102 ? -12.645 -6.282  -26.604 1.00 66.54  ? 111 THR   B CG2 1 
ATOM   1064 N  N   . LEU   B 2 103 ? -11.676 -9.554  -28.244 1.00 63.62  ? 112 LEU   B N   1 
ATOM   1065 C  CA  . LEU   B 2 103 ? -11.663 -10.833 -27.532 1.00 63.55  ? 112 LEU   B CA  1 
ATOM   1066 C  C   . LEU   B 2 103 ? -10.862 -10.586 -26.270 1.00 63.77  ? 112 LEU   B C   1 
ATOM   1067 O  O   . LEU   B 2 103 ? -9.688  -10.210 -26.345 1.00 64.06  ? 112 LEU   B O   1 
ATOM   1068 C  CB  . LEU   B 2 103 ? -10.989 -11.979 -28.299 1.00 63.49  ? 112 LEU   B CB  1 
ATOM   1069 C  CG  . LEU   B 2 103 ? -11.050 -13.311 -27.551 1.00 64.17  ? 112 LEU   B CG  1 
ATOM   1070 C  CD1 . LEU   B 2 103 ? -12.250 -14.097 -27.955 1.00 64.55  ? 112 LEU   B CD1 1 
ATOM   1071 C  CD2 . LEU   B 2 103 ? -9.805  -14.125 -27.750 1.00 64.49  ? 112 LEU   B CD2 1 
ATOM   1072 N  N   . PRO   B 2 104 ? -11.460 -10.811 -25.099 1.00 63.45  ? 113 PRO   B N   1 
ATOM   1073 C  CA  . PRO   B 2 104 ? -10.737 -10.545 -23.862 1.00 63.66  ? 113 PRO   B CA  1 
ATOM   1074 C  C   . PRO   B 2 104 ? -9.611  -11.513 -23.530 1.00 64.78  ? 113 PRO   B C   1 
ATOM   1075 O  O   . PRO   B 2 104 ? -9.606  -12.686 -23.913 1.00 64.98  ? 113 PRO   B O   1 
ATOM   1076 C  CB  . PRO   B 2 104 ? -11.831 -10.566 -22.790 1.00 64.13  ? 113 PRO   B CB  1 
ATOM   1077 C  CG  . PRO   B 2 104 ? -13.106 -10.625 -23.511 1.00 64.63  ? 113 PRO   B CG  1 
ATOM   1078 C  CD  . PRO   B 2 104 ? -12.841 -11.236 -24.835 1.00 62.85  ? 113 PRO   B CD  1 
ATOM   1079 N  N   . GLY   B 2 105 ? -8.656  -10.970 -22.794 1.00 64.86  ? 114 GLY   B N   1 
ATOM   1080 C  CA  . GLY   B 2 105 ? -7.535  -11.683 -22.230 1.00 65.05  ? 114 GLY   B CA  1 
ATOM   1081 C  C   . GLY   B 2 105 ? -7.878  -12.133 -20.825 1.00 65.06  ? 114 GLY   B C   1 
ATOM   1082 O  O   . GLY   B 2 105 ? -9.054  -12.323 -20.496 1.00 65.37  ? 114 GLY   B O   1 
ATOM   1083 N  N   . ILE   B 2 106 ? -6.861  -12.324 -19.983 1.00 64.34  ? 115 ILE   B N   1 
ATOM   1084 C  CA  . ILE   B 2 106 ? -7.057  -12.825 -18.625 1.00 64.09  ? 115 ILE   B CA  1 
ATOM   1085 C  C   . ILE   B 2 106 ? -6.221  -12.054 -17.618 1.00 63.57  ? 115 ILE   B C   1 
ATOM   1086 O  O   . ILE   B 2 106 ? -5.072  -11.718 -17.884 1.00 63.54  ? 115 ILE   B O   1 
ATOM   1087 C  CB  . ILE   B 2 106 ? -6.658  -14.336 -18.571 1.00 64.85  ? 115 ILE   B CB  1 
ATOM   1088 C  CG1 . ILE   B 2 106 ? -7.574  -15.225 -19.424 1.00 66.29  ? 115 ILE   B CG1 1 
ATOM   1089 C  CG2 . ILE   B 2 106 ? -6.551  -14.874 -17.149 1.00 65.56  ? 115 ILE   B CG2 1 
ATOM   1090 C  CD1 . ILE   B 2 106 ? -8.957  -15.305 -18.952 1.00 67.78  ? 115 ILE   B CD1 1 
ATOM   1091 N  N   . PHE   B 2 107 ? -6.795  -11.818 -16.441 1.00 63.13  ? 116 PHE   B N   1 
ATOM   1092 C  CA  . PHE   B 2 107 ? -6.115  -11.277 -15.275 1.00 63.01  ? 116 PHE   B CA  1 
ATOM   1093 C  C   . PHE   B 2 107 ? -6.032  -12.479 -14.357 1.00 63.41  ? 116 PHE   B C   1 
ATOM   1094 O  O   . PHE   B 2 107 ? -7.074  -12.958 -13.926 1.00 63.18  ? 116 PHE   B O   1 
ATOM   1095 C  CB  . PHE   B 2 107 ? -6.977  -10.212 -14.574 1.00 62.30  ? 116 PHE   B CB  1 
ATOM   1096 C  CG  . PHE   B 2 107 ? -6.683  -8.772  -14.912 1.00 61.84  ? 116 PHE   B CG  1 
ATOM   1097 C  CD1 . PHE   B 2 107 ? -5.918  -8.443  -16.020 1.00 62.14  ? 116 PHE   B CD1 1 
ATOM   1098 C  CD2 . PHE   B 2 107 ? -7.182  -7.747  -14.131 1.00 61.90  ? 116 PHE   B CD2 1 
ATOM   1099 C  CE1 . PHE   B 2 107 ? -5.672  -7.117  -16.342 1.00 62.63  ? 116 PHE   B CE1 1 
ATOM   1100 C  CE2 . PHE   B 2 107 ? -6.914  -6.425  -14.443 1.00 62.45  ? 116 PHE   B CE2 1 
ATOM   1101 C  CZ  . PHE   B 2 107 ? -6.163  -6.118  -15.546 1.00 62.34  ? 116 PHE   B CZ  1 
ATOM   1102 N  N   . LYS   B 2 108 ? -4.830  -13.003 -14.095 1.00 63.92  ? 117 LYS   B N   1 
ATOM   1103 C  CA  . LYS   B 2 108 ? -4.659  -14.127 -13.183 1.00 64.93  ? 117 LYS   B CA  1 
ATOM   1104 C  C   . LYS   B 2 108 ? -4.316  -13.579 -11.815 1.00 65.19  ? 117 LYS   B C   1 
ATOM   1105 O  O   . LYS   B 2 108 ? -3.292  -12.911 -11.669 1.00 65.21  ? 117 LYS   B O   1 
ATOM   1106 C  CB  . LYS   B 2 108 ? -3.511  -15.039 -13.638 1.00 68.23  ? 117 LYS   B CB  1 
ATOM   1107 C  CG  . LYS   B 2 108 ? -3.765  -15.840 -14.911 1.00 73.81  ? 117 LYS   B CG  1 
ATOM   1108 C  CD  . LYS   B 2 108 ? -2.816  -17.038 -14.940 1.00 79.40  ? 117 LYS   B CD  1 
ATOM   1109 C  CE  . LYS   B 2 108 ? -3.099  -18.029 -16.041 1.00 83.90  ? 117 LYS   B CE  1 
ATOM   1110 N  NZ  . LYS   B 2 108 ? -1.928  -18.930 -16.289 1.00 86.08  ? 117 LYS   B NZ  1 
ATOM   1111 N  N   . THR   B 2 109 ? -5.153  -13.866 -10.804 1.00 65.26  ? 118 THR   B N   1 
ATOM   1112 C  CA  . THR   B 2 109 ? -4.945  -13.425 -9.417  1.00 65.61  ? 118 THR   B CA  1 
ATOM   1113 C  C   . THR   B 2 109 ? -4.865  -14.632 -8.459  1.00 65.91  ? 118 THR   B C   1 
ATOM   1114 O  O   . THR   B 2 109 ? -5.224  -15.745 -8.846  1.00 66.15  ? 118 THR   B O   1 
ATOM   1115 C  CB  . THR   B 2 109 ? -6.089  -12.479 -8.981  1.00 66.92  ? 118 THR   B CB  1 
ATOM   1116 O  OG1 . THR   B 2 109 ? -7.310  -13.213 -8.911  1.00 68.39  ? 118 THR   B OG1 1 
ATOM   1117 C  CG2 . THR   B 2 109 ? -6.242  -11.281 -9.878  1.00 66.96  ? 118 THR   B CG2 1 
ATOM   1118 N  N   . LYS   B 2 110 ? -4.437  -14.412 -7.199  1.00 65.80  ? 119 LYS   B N   1 
ATOM   1119 C  CA  . LYS   B 2 110 ? -4.384  -15.476 -6.186  1.00 66.43  ? 119 LYS   B CA  1 
ATOM   1120 C  C   . LYS   B 2 110 ? -5.790  -16.043 -5.840  1.00 66.86  ? 119 LYS   B C   1 
ATOM   1121 O  O   . LYS   B 2 110 ? -5.892  -17.138 -5.275  1.00 67.02  ? 119 LYS   B O   1 
ATOM   1122 C  CB  . LYS   B 2 110 ? -3.678  -14.972 -4.909  1.00 67.61  ? 119 LYS   B CB  1 
ATOM   1123 C  CG  . LYS   B 2 110 ? -4.475  -13.919 -4.139  1.00 70.94  ? 119 LYS   B CG  1 
ATOM   1124 C  CD  . LYS   B 2 110 ? -3.639  -13.271 -3.045  1.00 74.76  ? 119 LYS   B CD  1 
ATOM   1125 C  CE  . LYS   B 2 110 ? -4.427  -12.960 -1.798  1.00 78.48  ? 119 LYS   B CE  1 
ATOM   1126 N  NZ  . LYS   B 2 110 ? -5.440  -11.896 -2.024  1.00 81.10  ? 119 LYS   B NZ  1 
ATOM   1127 N  N   . ASP   B 2 111 ? -6.861  -15.302 -6.189  1.00 66.54  ? 120 ASP   B N   1 
ATOM   1128 C  CA  . ASP   B 2 111 ? -8.238  -15.690 -5.924  1.00 66.81  ? 120 ASP   B CA  1 
ATOM   1129 C  C   . ASP   B 2 111 ? -9.017  -16.155 -7.155  1.00 67.00  ? 120 ASP   B C   1 
ATOM   1130 O  O   . ASP   B 2 111 ? -10.229 -16.344 -7.044  1.00 67.57  ? 120 ASP   B O   1 
ATOM   1131 C  CB  . ASP   B 2 111 ? -8.985  -14.525 -5.270  1.00 68.37  ? 120 ASP   B CB  1 
ATOM   1132 C  CG  . ASP   B 2 111 ? -8.425  -14.154 -3.919  1.00 73.23  ? 120 ASP   B CG  1 
ATOM   1133 O  OD1 . ASP   B 2 111 ? -7.970  -15.069 -3.194  1.00 73.89  ? 120 ASP   B OD1 1 
ATOM   1134 O  OD2 . ASP   B 2 111 ? -8.440  -12.948 -3.582  1.00 75.60  ? 120 ASP   B OD2 1 
ATOM   1135 N  N   . GLY   B 2 112 ? -8.350  -16.305 -8.306  1.00 66.01  ? 121 GLY   B N   1 
ATOM   1136 C  CA  . GLY   B 2 112 ? -9.000  -16.742 -9.538  1.00 65.09  ? 121 GLY   B CA  1 
ATOM   1137 C  C   . GLY   B 2 112 ? -8.760  -15.852 -10.740 1.00 63.63  ? 121 GLY   B C   1 
ATOM   1138 O  O   . GLY   B 2 112 ? -8.173  -14.781 -10.611 1.00 63.36  ? 121 GLY   B O   1 
ATOM   1139 N  N   . ASP   B 2 113 ? -9.209  -16.293 -11.928 1.00 62.66  ? 122 ASP   B N   1 
ATOM   1140 C  CA  . ASP   B 2 113 ? -9.030  -15.540 -13.170 1.00 62.15  ? 122 ASP   B CA  1 
ATOM   1141 C  C   . ASP   B 2 113 ? -10.232 -14.667 -13.530 1.00 61.53  ? 122 ASP   B C   1 
ATOM   1142 O  O   . ASP   B 2 113 ? -11.376 -15.030 -13.277 1.00 61.30  ? 122 ASP   B O   1 
ATOM   1143 C  CB  . ASP   B 2 113 ? -8.679  -16.462 -14.346 1.00 63.56  ? 122 ASP   B CB  1 
ATOM   1144 C  CG  . ASP   B 2 113 ? -7.390  -17.248 -14.187 1.00 68.64  ? 122 ASP   B CG  1 
ATOM   1145 O  OD1 . ASP   B 2 113 ? -6.656  -17.002 -13.195 1.00 67.84  ? 122 ASP   B OD1 1 
ATOM   1146 O  OD2 . ASP   B 2 113 ? -7.110  -18.108 -15.055 1.00 72.14  ? 122 ASP   B OD2 1 
ATOM   1147 N  N   . ILE   B 2 114 ? -9.957  -13.509 -14.128 1.00 60.93  ? 123 ILE   B N   1 
ATOM   1148 C  CA  . ILE   B 2 114 ? -10.979 -12.549 -14.543 1.00 61.19  ? 123 ILE   B CA  1 
ATOM   1149 C  C   . ILE   B 2 114 ? -10.742 -12.223 -16.023 1.00 60.51  ? 123 ILE   B C   1 
ATOM   1150 O  O   . ILE   B 2 114 ? -9.596  -12.212 -16.475 1.00 60.56  ? 123 ILE   B O   1 
ATOM   1151 C  CB  . ILE   B 2 114 ? -10.909 -11.215 -13.707 1.00 62.22  ? 123 ILE   B CB  1 
ATOM   1152 C  CG1 . ILE   B 2 114 ? -10.496 -11.422 -12.236 1.00 63.96  ? 123 ILE   B CG1 1 
ATOM   1153 C  CG2 . ILE   B 2 114 ? -12.197 -10.414 -13.786 1.00 62.60  ? 123 ILE   B CG2 1 
ATOM   1154 C  CD1 . ILE   B 2 114 ? -10.062 -10.106 -11.552 1.00 65.53  ? 123 ILE   B CD1 1 
ATOM   1155 N  N   . GLY   B 2 115 ? -11.806 -11.889 -16.747 1.00 59.60  ? 124 GLY   B N   1 
ATOM   1156 C  CA  . GLY   B 2 115 ? -11.665 -11.427 -18.123 1.00 59.32  ? 124 GLY   B CA  1 
ATOM   1157 C  C   . GLY   B 2 115 ? -10.977 -10.071 -18.154 1.00 58.78  ? 124 GLY   B C   1 
ATOM   1158 O  O   . GLY   B 2 115 ? -10.938 -9.360  -17.135 1.00 58.89  ? 124 GLY   B O   1 
ATOM   1159 N  N   . ALA   B 2 116 ? -10.418 -9.697  -19.307 1.00 58.02  ? 125 ALA   B N   1 
ATOM   1160 C  CA  . ALA   B 2 116 ? -9.712  -8.419  -19.413 1.00 57.84  ? 125 ALA   B CA  1 
ATOM   1161 C  C   . ALA   B 2 116 ? -9.757  -7.817  -20.818 1.00 57.08  ? 125 ALA   B C   1 
ATOM   1162 O  O   . ALA   B 2 116 ? -9.365  -8.455  -21.763 1.00 56.10  ? 125 ALA   B O   1 
ATOM   1163 C  CB  . ALA   B 2 116 ? -8.268  -8.560  -18.914 1.00 57.81  ? 125 ALA   B CB  1 
ATOM   1164 N  N   . VAL   B 2 117 ? -10.243 -6.582  -20.945 1.00 58.03  ? 126 VAL   B N   1 
ATOM   1165 C  CA  A VAL   B 2 117 ? -10.340 -5.917  -22.242 0.50 58.73  ? 126 VAL   B CA  1 
ATOM   1166 C  CA  B VAL   B 2 117 ? -10.367 -5.887  -22.223 0.50 58.55  ? 126 VAL   B CA  1 
ATOM   1167 C  C   . VAL   B 2 117 ? -9.167  -4.948  -22.456 1.00 59.25  ? 126 VAL   B C   1 
ATOM   1168 O  O   . VAL   B 2 117 ? -8.873  -4.103  -21.608 1.00 58.94  ? 126 VAL   B O   1 
ATOM   1169 C  CB  A VAL   B 2 117 ? -11.723 -5.283  -22.491 0.50 59.52  ? 126 VAL   B CB  1 
ATOM   1170 C  CB  B VAL   B 2 117 ? -11.752 -5.198  -22.304 0.50 58.96  ? 126 VAL   B CB  1 
ATOM   1171 C  CG1 A VAL   B 2 117 ? -12.755 -6.366  -22.786 0.50 59.90  ? 126 VAL   B CG1 1 
ATOM   1172 C  CG1 B VAL   B 2 117 ? -11.772 -4.042  -23.297 0.50 59.33  ? 126 VAL   B CG1 1 
ATOM   1173 C  CG2 A VAL   B 2 117 ? -12.161 -4.433  -21.306 0.50 60.29  ? 126 VAL   B CG2 1 
ATOM   1174 C  CG2 B VAL   B 2 117 ? -12.837 -6.218  -22.627 0.50 59.29  ? 126 VAL   B CG2 1 
ATOM   1175 N  N   . ALA   B 2 118 ? -8.438  -5.128  -23.581 1.00 60.16  ? 127 ALA   B N   1 
ATOM   1176 C  CA  . ALA   B 2 118 ? -7.254  -4.313  -23.842 1.00 61.44  ? 127 ALA   B CA  1 
ATOM   1177 C  C   . ALA   B 2 118 ? -7.486  -3.222  -24.840 1.00 62.56  ? 127 ALA   B C   1 
ATOM   1178 O  O   . ALA   B 2 118 ? -7.070  -3.319  -25.988 1.00 63.44  ? 127 ALA   B O   1 
ATOM   1179 C  CB  . ALA   B 2 118 ? -6.078  -5.190  -24.250 1.00 61.70  ? 127 ALA   B CB  1 
ATOM   1180 N  N   . LEU   B 2 119 ? -8.188  -2.176  -24.403 1.00 62.47  ? 128 LEU   B N   1 
ATOM   1181 C  CA  . LEU   B 2 119 ? -8.515  -1.029  -25.229 1.00 62.22  ? 128 LEU   B CA  1 
ATOM   1182 C  C   . LEU   B 2 119 ? -8.089  0.247   -24.495 1.00 62.19  ? 128 LEU   B C   1 
ATOM   1183 O  O   . LEU   B 2 119 ? -8.208  0.322   -23.274 1.00 62.13  ? 128 LEU   B O   1 
ATOM   1184 C  CB  . LEU   B 2 119 ? -10.029 -1.027  -25.519 1.00 62.48  ? 128 LEU   B CB  1 
ATOM   1185 C  CG  . LEU   B 2 119 ? -10.529 -2.224  -26.339 1.00 63.81  ? 128 LEU   B CG  1 
ATOM   1186 C  CD1 . LEU   B 2 119 ? -12.039 -2.233  -26.445 1.00 64.01  ? 128 LEU   B CD1 1 
ATOM   1187 C  CD2 . LEU   B 2 119 ? -9.908  -2.240  -27.725 1.00 64.48  ? 128 LEU   B CD2 1 
ATOM   1188 N  N   . ASP   B 2 120 ? -7.569  1.243   -25.226 1.00 62.26  ? 129 ASP   B N   1 
ATOM   1189 C  CA  . ASP   B 2 120 ? -7.122  2.493   -24.613 1.00 62.57  ? 129 ASP   B CA  1 
ATOM   1190 C  C   . ASP   B 2 120 ? -8.129  3.632   -24.784 1.00 62.11  ? 129 ASP   B C   1 
ATOM   1191 O  O   . ASP   B 2 120 ? -8.419  4.021   -25.912 1.00 62.44  ? 129 ASP   B O   1 
ATOM   1192 C  CB  . ASP   B 2 120 ? -5.777  2.923   -25.199 1.00 64.55  ? 129 ASP   B CB  1 
ATOM   1193 C  CG  . ASP   B 2 120 ? -4.641  1.946   -25.000 1.00 70.39  ? 129 ASP   B CG  1 
ATOM   1194 O  OD1 . ASP   B 2 120 ? -4.832  0.953   -24.273 1.00 71.37  ? 129 ASP   B OD1 1 
ATOM   1195 O  OD2 . ASP   B 2 120 ? -3.553  2.178   -25.573 1.00 73.43  ? 129 ASP   B OD2 1 
ATOM   1196 N  N   . TYR   B 2 121 ? -8.589  4.215   -23.671 1.00 61.63  ? 130 TYR   B N   1 
ATOM   1197 C  CA  . TYR   B 2 121 ? -9.559  5.321   -23.640 1.00 61.79  ? 130 TYR   B CA  1 
ATOM   1198 C  C   . TYR   B 2 121 ? -9.263  6.295   -22.488 1.00 60.79  ? 130 TYR   B C   1 
ATOM   1199 O  O   . TYR   B 2 121 ? -8.796  5.855   -21.437 1.00 61.03  ? 130 TYR   B O   1 
ATOM   1200 C  CB  . TYR   B 2 121 ? -10.982 4.758   -23.455 1.00 62.56  ? 130 TYR   B CB  1 
ATOM   1201 C  CG  . TYR   B 2 121 ? -11.592 4.273   -24.748 1.00 64.24  ? 130 TYR   B CG  1 
ATOM   1202 C  CD1 . TYR   B 2 121 ? -12.241 5.150   -25.603 1.00 65.33  ? 130 TYR   B CD1 1 
ATOM   1203 C  CD2 . TYR   B 2 121 ? -11.458 2.950   -25.149 1.00 65.60  ? 130 TYR   B CD2 1 
ATOM   1204 C  CE1 . TYR   B 2 121 ? -12.750 4.722   -26.821 1.00 66.68  ? 130 TYR   B CE1 1 
ATOM   1205 C  CE2 . TYR   B 2 121 ? -11.937 2.518   -26.378 1.00 66.67  ? 130 TYR   B CE2 1 
ATOM   1206 C  CZ  . TYR   B 2 121 ? -12.590 3.405   -27.207 1.00 67.93  ? 130 TYR   B CZ  1 
ATOM   1207 O  OH  . TYR   B 2 121 ? -13.093 2.968   -28.404 1.00 69.94  ? 130 TYR   B OH  1 
ATOM   1208 N  N   . PRO   B 2 122 ? -9.598  7.602   -22.612 1.00 59.46  ? 131 PRO   B N   1 
ATOM   1209 C  CA  . PRO   B 2 122 ? -9.365  8.529   -21.484 1.00 58.25  ? 131 PRO   B CA  1 
ATOM   1210 C  C   . PRO   B 2 122 ? -10.020 8.072   -20.172 1.00 56.63  ? 131 PRO   B C   1 
ATOM   1211 O  O   . PRO   B 2 122 ? -11.024 7.359   -20.205 1.00 56.90  ? 131 PRO   B O   1 
ATOM   1212 C  CB  . PRO   B 2 122 ? -9.986  9.846   -21.964 1.00 59.02  ? 131 PRO   B CB  1 
ATOM   1213 C  CG  . PRO   B 2 122 ? -10.055 9.746   -23.430 1.00 59.82  ? 131 PRO   B CG  1 
ATOM   1214 C  CD  . PRO   B 2 122 ? -10.205 8.292   -23.767 1.00 58.77  ? 131 PRO   B CD  1 
ATOM   1215 N  N   . ALA   B 2 123 ? -9.468  8.496   -19.026 1.00 54.43  ? 132 ALA   B N   1 
ATOM   1216 C  CA  . ALA   B 2 123 ? -9.965  8.108   -17.706 1.00 52.84  ? 132 ALA   B CA  1 
ATOM   1217 C  C   . ALA   B 2 123 ? -11.475 8.346   -17.475 1.00 51.44  ? 132 ALA   B C   1 
ATOM   1218 O  O   . ALA   B 2 123 ? -12.083 7.553   -16.771 1.00 51.22  ? 132 ALA   B O   1 
ATOM   1219 C  CB  . ALA   B 2 123 ? -9.144  8.772   -16.623 1.00 52.60  ? 132 ALA   B CB  1 
ATOM   1220 N  N   . GLY   B 2 124 ? -12.070 9.359   -18.132 1.00 50.30  ? 133 GLY   B N   1 
ATOM   1221 C  CA  . GLY   B 2 124 ? -13.501 9.644   -18.047 1.00 48.98  ? 133 GLY   B CA  1 
ATOM   1222 C  C   . GLY   B 2 124 ? -14.402 8.619   -18.726 1.00 48.15  ? 133 GLY   B C   1 
ATOM   1223 O  O   . GLY   B 2 124 ? -15.625 8.749   -18.711 1.00 47.33  ? 133 GLY   B O   1 
ATOM   1224 N  N   . THR   B 2 125 ? -13.807 7.598   -19.356 1.00 48.29  ? 134 THR   B N   1 
ATOM   1225 C  CA  . THR   B 2 125 ? -14.514 6.494   -20.004 1.00 48.60  ? 134 THR   B CA  1 
ATOM   1226 C  C   . THR   B 2 125 ? -14.807 5.350   -18.983 1.00 47.80  ? 134 THR   B C   1 
ATOM   1227 O  O   . THR   B 2 125 ? -15.618 4.481   -19.303 1.00 47.87  ? 134 THR   B O   1 
ATOM   1228 C  CB  . THR   B 2 125 ? -13.719 6.004   -21.261 1.00 50.35  ? 134 THR   B CB  1 
ATOM   1229 O  OG1 . THR   B 2 125 ? -13.333 7.126   -22.053 1.00 51.35  ? 134 THR   B OG1 1 
ATOM   1230 C  CG2 . THR   B 2 125 ? -14.494 5.019   -22.127 1.00 50.64  ? 134 THR   B CG2 1 
ATOM   1231 N  N   . SER   B 2 126 ? -14.164 5.345   -17.766 1.00 46.94  ? 135 SER   B N   1 
ATOM   1232 C  CA  . SER   B 2 126 ? -14.416 4.302   -16.745 1.00 47.09  ? 135 SER   B CA  1 
ATOM   1233 C  C   . SER   B 2 126 ? -15.899 4.253   -16.380 1.00 46.22  ? 135 SER   B C   1 
ATOM   1234 O  O   . SER   B 2 126 ? -16.499 5.290   -16.134 1.00 45.89  ? 135 SER   B O   1 
ATOM   1235 C  CB  . SER   B 2 126 ? -13.589 4.494   -15.470 1.00 49.07  ? 135 SER   B CB  1 
ATOM   1236 O  OG  . SER   B 2 126 ? -12.619 5.529   -15.507 1.00 52.83  ? 135 SER   B OG  1 
ATOM   1237 N  N   . GLY   B 2 127 ? -16.466 3.053   -16.382 1.00 45.35  ? 136 GLY   B N   1 
ATOM   1238 C  CA  . GLY   B 2 127 ? -17.876 2.794   -16.130 1.00 45.31  ? 136 GLY   B CA  1 
ATOM   1239 C  C   . GLY   B 2 127 ? -18.593 2.223   -17.344 1.00 45.85  ? 136 GLY   B C   1 
ATOM   1240 O  O   . GLY   B 2 127 ? -19.677 1.645   -17.209 1.00 46.64  ? 136 GLY   B O   1 
ATOM   1241 N  N   . SER   B 2 128 ? -18.000 2.387   -18.548 1.00 45.10  ? 137 SER   B N   1 
ATOM   1242 C  CA  . SER   B 2 128 ? -18.525 1.877   -19.812 1.00 44.90  ? 137 SER   B CA  1 
ATOM   1243 C  C   . SER   B 2 128 ? -18.808 0.371   -19.761 1.00 44.28  ? 137 SER   B C   1 
ATOM   1244 O  O   . SER   B 2 128 ? -17.940 -0.409  -19.388 1.00 43.65  ? 137 SER   B O   1 
ATOM   1245 C  CB  . SER   B 2 128 ? -17.570 2.213   -20.955 1.00 46.12  ? 137 SER   B CB  1 
ATOM   1246 O  OG  . SER   B 2 128 ? -17.565 3.608   -21.224 1.00 48.71  ? 137 SER   B OG  1 
ATOM   1247 N  N   . PRO   B 2 129 ? -20.035 -0.044  -20.123 1.00 44.56  ? 138 PRO   B N   1 
ATOM   1248 C  CA  . PRO   B 2 129 ? -20.382 -1.469  -20.054 1.00 45.47  ? 138 PRO   B CA  1 
ATOM   1249 C  C   . PRO   B 2 129 ? -19.745 -2.357  -21.127 1.00 47.13  ? 138 PRO   B C   1 
ATOM   1250 O  O   . PRO   B 2 129 ? -19.458 -1.915  -22.230 1.00 47.56  ? 138 PRO   B O   1 
ATOM   1251 C  CB  . PRO   B 2 129 ? -21.914 -1.449  -20.182 1.00 45.04  ? 138 PRO   B CB  1 
ATOM   1252 C  CG  . PRO   B 2 129 ? -22.197 -0.257  -20.988 1.00 44.55  ? 138 PRO   B CG  1 
ATOM   1253 C  CD  . PRO   B 2 129 ? -21.193 0.767   -20.559 1.00 43.19  ? 138 PRO   B CD  1 
ATOM   1254 N  N   . ILE   B 2 130 ? -19.530 -3.623  -20.782 1.00 48.09  ? 139 ILE   B N   1 
ATOM   1255 C  CA  . ILE   B 2 130 ? -18.987 -4.643  -21.667 1.00 49.12  ? 139 ILE   B CA  1 
ATOM   1256 C  C   . ILE   B 2 130 ? -20.125 -5.645  -21.880 1.00 50.77  ? 139 ILE   B C   1 
ATOM   1257 O  O   . ILE   B 2 130 ? -20.754 -6.074  -20.916 1.00 50.24  ? 139 ILE   B O   1 
ATOM   1258 C  CB  . ILE   B 2 130 ? -17.751 -5.290  -21.027 1.00 49.54  ? 139 ILE   B CB  1 
ATOM   1259 C  CG1 . ILE   B 2 130 ? -16.627 -4.269  -20.797 1.00 50.09  ? 139 ILE   B CG1 1 
ATOM   1260 C  CG2 . ILE   B 2 130 ? -17.269 -6.483  -21.845 1.00 49.96  ? 139 ILE   B CG2 1 
ATOM   1261 C  CD1 . ILE   B 2 130 ? -15.531 -4.807  -19.771 1.00 50.55  ? 139 ILE   B CD1 1 
ATOM   1262 N  N   . LEU   B 2 131 ? -20.438 -5.972  -23.143 1.00 52.66  ? 140 LEU   B N   1 
ATOM   1263 C  CA  . LEU   B 2 131 ? -21.603 -6.791  -23.476 1.00 55.01  ? 140 LEU   B CA  1 
ATOM   1264 C  C   . LEU   B 2 131 ? -21.315 -8.129  -24.130 1.00 57.39  ? 140 LEU   B C   1 
ATOM   1265 O  O   . LEU   B 2 131 ? -20.288 -8.302  -24.776 1.00 58.34  ? 140 LEU   B O   1 
ATOM   1266 C  CB  . LEU   B 2 131 ? -22.536 -6.005  -24.424 1.00 55.56  ? 140 LEU   B CB  1 
ATOM   1267 C  CG  . LEU   B 2 131 ? -22.608 -4.496  -24.268 1.00 57.05  ? 140 LEU   B CG  1 
ATOM   1268 C  CD1 . LEU   B 2 131 ? -23.438 -3.896  -25.370 1.00 57.30  ? 140 LEU   B CD1 1 
ATOM   1269 C  CD2 . LEU   B 2 131 ? -23.106 -4.112  -22.870 1.00 57.89  ? 140 LEU   B CD2 1 
ATOM   1270 N  N   . ASP   B 2 132 ? -22.268 -9.062  -24.015 1.00 58.59  ? 141 ASP   B N   1 
ATOM   1271 C  CA  . ASP   B 2 132 ? -22.211 -10.354 -24.691 1.00 60.32  ? 141 ASP   B CA  1 
ATOM   1272 C  C   . ASP   B 2 132 ? -23.120 -10.322 -25.962 1.00 61.63  ? 141 ASP   B C   1 
ATOM   1273 O  O   . ASP   B 2 132 ? -23.785 -9.317  -26.213 1.00 61.76  ? 141 ASP   B O   1 
ATOM   1274 C  CB  . ASP   B 2 132 ? -22.586 -11.497 -23.728 1.00 62.10  ? 141 ASP   B CB  1 
ATOM   1275 C  CG  . ASP   B 2 132 ? -24.046 -11.545 -23.316 1.00 67.87  ? 141 ASP   B CG  1 
ATOM   1276 O  OD1 . ASP   B 2 132 ? -24.847 -10.755 -23.858 1.00 67.65  ? 141 ASP   B OD1 1 
ATOM   1277 O  OD2 . ASP   B 2 132 ? -24.391 -12.392 -22.469 1.00 71.52  ? 141 ASP   B OD2 1 
ATOM   1278 N  N   . LYS   B 2 133 ? -23.185 -11.428 -26.722 1.00 62.63  ? 142 LYS   B N   1 
ATOM   1279 C  CA  . LYS   B 2 133 ? -23.967 -11.544 -27.957 1.00 64.07  ? 142 LYS   B CA  1 
ATOM   1280 C  C   . LYS   B 2 133 ? -25.464 -11.270 -27.786 1.00 64.01  ? 142 LYS   B C   1 
ATOM   1281 O  O   . LYS   B 2 133 ? -26.115 -10.925 -28.769 1.00 64.13  ? 142 LYS   B O   1 
ATOM   1282 C  CB  . LYS   B 2 133 ? -23.726 -12.908 -28.631 1.00 67.55  ? 142 LYS   B CB  1 
ATOM   1283 C  CG  . LYS   B 2 133 ? -22.245 -13.143 -28.905 1.00 74.50  ? 142 LYS   B CG  1 
ATOM   1284 C  CD  . LYS   B 2 133 ? -21.909 -14.604 -29.223 1.00 81.13  ? 142 LYS   B CD  1 
ATOM   1285 C  CE  . LYS   B 2 133 ? -20.472 -14.746 -29.659 1.00 86.16  ? 142 LYS   B CE  1 
ATOM   1286 N  NZ  . LYS   B 2 133 ? -20.083 -16.172 -29.833 1.00 89.87  ? 142 LYS   B NZ  1 
ATOM   1287 N  N   . CYS   B 2 134 ? -26.005 -11.394 -26.558 1.00 63.83  ? 143 CYS   B N   1 
ATOM   1288 C  CA  . CYS   B 2 134 ? -27.420 -11.070 -26.280 1.00 63.63  ? 143 CYS   B CA  1 
ATOM   1289 C  C   . CYS   B 2 134 ? -27.645 -9.602  -25.922 1.00 61.96  ? 143 CYS   B C   1 
ATOM   1290 O  O   . CYS   B 2 134 ? -28.796 -9.190  -25.775 1.00 62.44  ? 143 CYS   B O   1 
ATOM   1291 C  CB  . CYS   B 2 134 ? -27.987 -11.967 -25.184 1.00 66.02  ? 143 CYS   B CB  1 
ATOM   1292 S  SG  . CYS   B 2 134 ? -27.840 -13.740 -25.512 1.00 74.35  ? 143 CYS   B SG  1 
ATOM   1293 N  N   . GLY   B 2 135 ? -26.575 -8.843  -25.718 1.00 59.99  ? 144 GLY   B N   1 
ATOM   1294 C  CA  . GLY   B 2 135 ? -26.663 -7.462  -25.267 1.00 58.87  ? 144 GLY   B CA  1 
ATOM   1295 C  C   . GLY   B 2 135 ? -26.650 -7.336  -23.747 1.00 57.29  ? 144 GLY   B C   1 
ATOM   1296 O  O   . GLY   B 2 135 ? -26.888 -6.250  -23.214 1.00 57.43  ? 144 GLY   B O   1 
ATOM   1297 N  N   . ARG   B 2 136 ? -26.376 -8.442  -23.024 1.00 55.37  ? 145 ARG   B N   1 
ATOM   1298 C  CA  . ARG   B 2 136 ? -26.346 -8.430  -21.570 1.00 54.44  ? 145 ARG   B CA  1 
ATOM   1299 C  C   . ARG   B 2 136 ? -25.037 -7.855  -21.043 1.00 52.61  ? 145 ARG   B C   1 
ATOM   1300 O  O   . ARG   B 2 136 ? -23.967 -8.147  -21.591 1.00 52.49  ? 145 ARG   B O   1 
ATOM   1301 C  CB  . ARG   B 2 136 ? -26.581 -9.833  -21.014 1.00 56.10  ? 145 ARG   B CB  1 
ATOM   1302 C  CG  . ARG   B 2 136 ? -27.893 -10.444 -21.470 1.00 59.75  ? 145 ARG   B CG  1 
ATOM   1303 C  CD  . ARG   B 2 136 ? -28.057 -11.828 -20.879 1.00 65.62  ? 145 ARG   B CD  1 
ATOM   1304 N  NE  . ARG   B 2 136 ? -27.008 -12.760 -21.314 1.00 71.20  ? 145 ARG   B NE  1 
ATOM   1305 C  CZ  . ARG   B 2 136 ? -26.503 -13.730 -20.550 1.00 76.11  ? 145 ARG   B CZ  1 
ATOM   1306 N  NH1 . ARG   B 2 136 ? -26.927 -13.892 -19.300 1.00 76.40  ? 145 ARG   B NH1 1 
ATOM   1307 N  NH2 . ARG   B 2 136 ? -25.551 -14.529 -21.022 1.00 76.67  ? 145 ARG   B NH2 1 
ATOM   1308 N  N   . VAL   B 2 137 ? -25.119 -7.013  -20.000 1.00 50.77  ? 146 VAL   B N   1 
ATOM   1309 C  CA  . VAL   B 2 137 ? -23.920 -6.421  -19.418 1.00 49.49  ? 146 VAL   B CA  1 
ATOM   1310 C  C   . VAL   B 2 137 ? -23.192 -7.476  -18.568 1.00 48.11  ? 146 VAL   B C   1 
ATOM   1311 O  O   . VAL   B 2 137 ? -23.721 -7.941  -17.562 1.00 48.27  ? 146 VAL   B O   1 
ATOM   1312 C  CB  . VAL   B 2 137 ? -24.222 -5.132  -18.626 1.00 49.87  ? 146 VAL   B CB  1 
ATOM   1313 C  CG1 . VAL   B 2 137 ? -22.932 -4.438  -18.213 1.00 50.36  ? 146 VAL   B CG1 1 
ATOM   1314 C  CG2 . VAL   B 2 137 ? -25.110 -4.183  -19.433 1.00 50.33  ? 146 VAL   B CG2 1 
ATOM   1315 N  N   . ILE   B 2 138 ? -22.003 -7.882  -19.013 1.00 46.57  ? 147 ILE   B N   1 
ATOM   1316 C  CA  . ILE   B 2 138 ? -21.176 -8.880  -18.338 1.00 45.58  ? 147 ILE   B CA  1 
ATOM   1317 C  C   . ILE   B 2 138 ? -20.084 -8.263  -17.422 1.00 44.61  ? 147 ILE   B C   1 
ATOM   1318 O  O   . ILE   B 2 138 ? -19.319 -9.001  -16.800 1.00 44.27  ? 147 ILE   B O   1 
ATOM   1319 C  CB  . ILE   B 2 138 ? -20.576 -9.878  -19.376 1.00 45.81  ? 147 ILE   B CB  1 
ATOM   1320 C  CG1 . ILE   B 2 138 ? -19.708 -9.154  -20.414 1.00 46.15  ? 147 ILE   B CG1 1 
ATOM   1321 C  CG2 . ILE   B 2 138 ? -21.683 -10.692 -20.065 1.00 46.16  ? 147 ILE   B CG2 1 
ATOM   1322 C  CD1 . ILE   B 2 138 ? -18.866 -10.068 -21.174 1.00 47.37  ? 147 ILE   B CD1 1 
ATOM   1323 N  N   . GLY   B 2 139 ? -20.058 -6.935  -17.298 1.00 43.42  ? 148 GLY   B N   1 
ATOM   1324 C  CA  . GLY   B 2 139 ? -19.081 -6.249  -16.462 1.00 43.20  ? 148 GLY   B CA  1 
ATOM   1325 C  C   . GLY   B 2 139 ? -18.866 -4.801  -16.868 1.00 43.20  ? 148 GLY   B C   1 
ATOM   1326 O  O   . GLY   B 2 139 ? -19.470 -4.339  -17.834 1.00 42.89  ? 148 GLY   B O   1 
ATOM   1327 N  N   . LEU   B 2 140 ? -18.007 -4.063  -16.137 1.00 42.96  ? 149 LEU   B N   1 
ATOM   1328 C  CA  . LEU   B 2 140 ? -17.735 -2.653  -16.440 1.00 42.46  ? 149 LEU   B CA  1 
ATOM   1329 C  C   . LEU   B 2 140 ? -16.243 -2.445  -16.704 1.00 43.04  ? 149 LEU   B C   1 
ATOM   1330 O  O   . LEU   B 2 140 ? -15.399 -3.083  -16.090 1.00 42.93  ? 149 LEU   B O   1 
ATOM   1331 C  CB  . LEU   B 2 140 ? -18.187 -1.723  -15.303 1.00 41.79  ? 149 LEU   B CB  1 
ATOM   1332 C  CG  . LEU   B 2 140 ? -19.679 -1.634  -14.909 1.00 41.75  ? 149 LEU   B CG  1 
ATOM   1333 C  CD1 . LEU   B 2 140 ? -19.918 -0.412  -13.985 1.00 40.69  ? 149 LEU   B CD1 1 
ATOM   1334 C  CD2 . LEU   B 2 140 ? -20.583 -1.498  -16.129 1.00 42.12  ? 149 LEU   B CD2 1 
ATOM   1335 N  N   . TYR   B 2 141 ? -15.932 -1.577  -17.656 1.00 43.56  ? 150 TYR   B N   1 
ATOM   1336 C  CA  . TYR   B 2 141 ? -14.581 -1.232  -18.079 1.00 44.09  ? 150 TYR   B CA  1 
ATOM   1337 C  C   . TYR   B 2 141 ? -14.137 0.006   -17.296 1.00 43.81  ? 150 TYR   B C   1 
ATOM   1338 O  O   . TYR   B 2 141 ? -14.918 0.945   -17.178 1.00 43.10  ? 150 TYR   B O   1 
ATOM   1339 C  CB  . TYR   B 2 141 ? -14.625 -0.939  -19.600 1.00 45.30  ? 150 TYR   B CB  1 
ATOM   1340 C  CG  . TYR   B 2 141 ? -13.435 -0.196  -20.178 1.00 46.99  ? 150 TYR   B CG  1 
ATOM   1341 C  CD1 . TYR   B 2 141 ? -13.456 1.187   -20.329 1.00 48.10  ? 150 TYR   B CD1 1 
ATOM   1342 C  CD2 . TYR   B 2 141 ? -12.306 -0.879  -20.600 1.00 48.69  ? 150 TYR   B CD2 1 
ATOM   1343 C  CE1 . TYR   B 2 141 ? -12.361 1.872   -20.848 1.00 49.69  ? 150 TYR   B CE1 1 
ATOM   1344 C  CE2 . TYR   B 2 141 ? -11.209 -0.209  -21.131 1.00 50.17  ? 150 TYR   B CE2 1 
ATOM   1345 C  CZ  . TYR   B 2 141 ? -11.244 1.165   -21.275 1.00 50.84  ? 150 TYR   B CZ  1 
ATOM   1346 O  OH  . TYR   B 2 141 ? -10.141 1.799   -21.804 1.00 51.72  ? 150 TYR   B OH  1 
ATOM   1347 N  N   . GLY   B 2 142 ? -12.920 0.006   -16.756 1.00 44.39  ? 151 GLY   B N   1 
ATOM   1348 C  CA  . GLY   B 2 142 ? -12.437 1.177   -16.038 1.00 45.63  ? 151 GLY   B CA  1 
ATOM   1349 C  C   . GLY   B 2 142 ? -11.586 0.969   -14.814 1.00 47.02  ? 151 GLY   B C   1 
ATOM   1350 O  O   . GLY   B 2 142 ? -11.275 1.940   -14.121 1.00 47.66  ? 151 GLY   B O   1 
ATOM   1351 N  N   . ASN   B 2 143 ? -11.168 -0.270  -14.552 1.00 47.27  ? 152 ASN   B N   1 
ATOM   1352 C  CA  . ASN   B 2 143 ? -10.260 -0.539  -13.453 1.00 47.87  ? 152 ASN   B CA  1 
ATOM   1353 C  C   . ASN   B 2 143 ? -9.312  -1.643  -13.869 1.00 49.26  ? 152 ASN   B C   1 
ATOM   1354 O  O   . ASN   B 2 143 ? -9.729  -2.785  -14.060 1.00 49.59  ? 152 ASN   B O   1 
ATOM   1355 C  CB  . ASN   B 2 143 ? -10.980 -0.870  -12.162 1.00 48.68  ? 152 ASN   B CB  1 
ATOM   1356 C  CG  . ASN   B 2 143 ? -10.042 -0.938  -10.981 1.00 51.04  ? 152 ASN   B CG  1 
ATOM   1357 O  OD1 . ASN   B 2 143 ? -9.029  -0.231  -10.915 1.00 52.16  ? 152 ASN   B OD1 1 
ATOM   1358 N  ND2 . ASN   B 2 143 ? -10.345 -1.798  -10.031 1.00 51.03  ? 152 ASN   B ND2 1 
ATOM   1359 N  N   . GLY   B 2 144 ? -8.053  -1.286  -14.040 1.00 49.73  ? 153 GLY   B N   1 
ATOM   1360 C  CA  . GLY   B 2 144 ? -7.065  -2.252  -14.451 1.00 51.55  ? 153 GLY   B CA  1 
ATOM   1361 C  C   . GLY   B 2 144 ? -5.645  -1.823  -14.213 1.00 54.16  ? 153 GLY   B C   1 
ATOM   1362 O  O   . GLY   B 2 144 ? -5.289  -1.359  -13.125 1.00 54.46  ? 153 GLY   B O   1 
ATOM   1363 N  N   . VAL   B 2 145 ? -4.822  -1.992  -15.243 1.00 56.02  ? 154 VAL   B N   1 
ATOM   1364 C  CA  . VAL   B 2 145 ? -3.398  -1.769  -15.135 1.00 58.58  ? 154 VAL   B CA  1 
ATOM   1365 C  C   . VAL   B 2 145 ? -2.787  -1.183  -16.410 1.00 61.64  ? 154 VAL   B C   1 
ATOM   1366 O  O   . VAL   B 2 145 ? -3.400  -1.192  -17.474 1.00 62.04  ? 154 VAL   B O   1 
ATOM   1367 C  CB  . VAL   B 2 145 ? -2.761  -3.135  -14.742 1.00 58.89  ? 154 VAL   B CB  1 
ATOM   1368 C  CG1 . VAL   B 2 145 ? -2.558  -4.037  -15.952 1.00 58.89  ? 154 VAL   B CG1 1 
ATOM   1369 C  CG2 . VAL   B 2 145 ? -1.481  -2.957  -13.944 1.00 59.73  ? 154 VAL   B CG2 1 
ATOM   1370 N  N   . VAL   B 2 146 ? -1.592  -0.628  -16.281 1.00 63.73  ? 155 VAL   B N   1 
ATOM   1371 C  CA  . VAL   B 2 146 ? -0.844  -0.090  -17.394 1.00 66.35  ? 155 VAL   B CA  1 
ATOM   1372 C  C   . VAL   B 2 146 ? 0.327   -1.035  -17.608 1.00 69.39  ? 155 VAL   B C   1 
ATOM   1373 O  O   . VAL   B 2 146 ? 1.078   -1.319  -16.668 1.00 69.55  ? 155 VAL   B O   1 
ATOM   1374 C  CB  . VAL   B 2 146 ? -0.385  1.357   -17.142 1.00 67.05  ? 155 VAL   B CB  1 
ATOM   1375 C  CG1 . VAL   B 2 146 ? 0.387   1.884   -18.342 1.00 67.85  ? 155 VAL   B CG1 1 
ATOM   1376 C  CG2 . VAL   B 2 146 ? -1.579  2.250   -16.846 1.00 67.46  ? 155 VAL   B CG2 1 
ATOM   1377 N  N   . ILE   B 2 147 ? 0.430   -1.606  -18.813 1.00 71.67  ? 156 ILE   B N   1 
ATOM   1378 C  CA  . ILE   B 2 147 ? 1.506   -2.553  -19.106 1.00 74.21  ? 156 ILE   B CA  1 
ATOM   1379 C  C   . ILE   B 2 147 ? 2.784   -1.817  -19.581 1.00 76.18  ? 156 ILE   B C   1 
ATOM   1380 O  O   . ILE   B 2 147 ? 2.746   -0.602  -19.792 1.00 76.39  ? 156 ILE   B O   1 
ATOM   1381 C  CB  . ILE   B 2 147 ? 1.017   -3.672  -20.065 1.00 75.43  ? 156 ILE   B CB  1 
ATOM   1382 C  CG1 . ILE   B 2 147 ? 0.444   -3.085  -21.365 1.00 77.25  ? 156 ILE   B CG1 1 
ATOM   1383 C  CG2 . ILE   B 2 147 ? -0.008  -4.558  -19.358 1.00 75.82  ? 156 ILE   B CG2 1 
ATOM   1384 C  CD1 . ILE   B 2 147 ? 0.014   -4.151  -22.412 1.00 79.01  ? 156 ILE   B CD1 1 
ATOM   1385 N  N   . LYS   B 2 148 ? 3.914   -2.544  -19.711 1.00 77.38  ? 157 LYS   B N   1 
ATOM   1386 C  CA  . LYS   B 2 148 ? 5.235   -2.013  -20.075 1.00 79.00  ? 157 LYS   B CA  1 
ATOM   1387 C  C   . LYS   B 2 148 ? 5.274   -1.049  -21.285 1.00 79.45  ? 157 LYS   B C   1 
ATOM   1388 O  O   . LYS   B 2 148 ? 6.136   -0.164  -21.326 1.00 79.73  ? 157 LYS   B O   1 
ATOM   1389 C  CB  . LYS   B 2 148 ? 6.275   -3.139  -20.271 1.00 82.59  ? 157 LYS   B CB  1 
ATOM   1390 C  CG  . LYS   B 2 148 ? 5.722   -4.533  -20.590 1.00 88.96  ? 157 LYS   B CG  1 
ATOM   1391 C  CD  . LYS   B 2 148 ? 5.208   -4.664  -22.031 1.00 94.98  ? 157 LYS   B CD  1 
ATOM   1392 C  CE  . LYS   B 2 148 ? 6.239   -4.301  -23.085 1.00 99.89  ? 157 LYS   B CE  1 
ATOM   1393 N  NZ  . LYS   B 2 148 ? 7.465   -5.138  -22.977 1.00 102.44 ? 157 LYS   B NZ  1 
ATOM   1394 N  N   . ASN   B 2 149 ? 4.355   -1.193  -22.245 1.00 79.16  ? 158 ASN   B N   1 
ATOM   1395 C  CA  . ASN   B 2 149 ? 4.325   -0.311  -23.412 1.00 79.24  ? 158 ASN   B CA  1 
ATOM   1396 C  C   . ASN   B 2 149 ? 3.414   0.924   -23.252 1.00 78.40  ? 158 ASN   B C   1 
ATOM   1397 O  O   . ASN   B 2 149 ? 3.125   1.606   -24.243 1.00 78.94  ? 158 ASN   B O   1 
ATOM   1398 C  CB  . ASN   B 2 149 ? 3.973   -1.087  -24.698 1.00 81.45  ? 158 ASN   B CB  1 
ATOM   1399 C  CG  . ASN   B 2 149 ? 2.915   -2.162  -24.539 1.00 85.74  ? 158 ASN   B CG  1 
ATOM   1400 O  OD1 . ASN   B 2 149 ? 3.103   -3.149  -23.823 1.00 87.31  ? 158 ASN   B OD1 1 
ATOM   1401 N  ND2 . ASN   B 2 149 ? 1.784   -2.007  -25.213 1.00 86.43  ? 158 ASN   B ND2 1 
ATOM   1402 N  N   . GLY   B 2 150 ? 2.981   1.208   -22.023 1.00 76.63  ? 159 GLY   B N   1 
ATOM   1403 C  CA  . GLY   B 2 150 ? 2.116   2.346   -21.730 1.00 75.28  ? 159 GLY   B CA  1 
ATOM   1404 C  C   . GLY   B 2 150 ? 0.642   2.125   -22.013 1.00 73.45  ? 159 GLY   B C   1 
ATOM   1405 O  O   . GLY   B 2 150 ? -0.184  2.977   -21.670 1.00 73.70  ? 159 GLY   B O   1 
ATOM   1406 N  N   . SER   B 2 151 ? 0.293   0.983   -22.644 1.00 71.43  ? 160 SER   B N   1 
ATOM   1407 C  CA  A SER   B 2 151 ? -1.091  0.647   -22.981 0.50 70.85  ? 160 SER   B CA  1 
ATOM   1408 C  CA  B SER   B 2 151 ? -1.102  0.709   -22.968 0.50 70.85  ? 160 SER   B CA  1 
ATOM   1409 C  C   . SER   B 2 151 ? -1.912  0.260   -21.751 1.00 69.72  ? 160 SER   B C   1 
ATOM   1410 O  O   . SER   B 2 151 ? -1.359  -0.237  -20.763 1.00 69.54  ? 160 SER   B O   1 
ATOM   1411 C  CB  A SER   B 2 151 ? -1.138  -0.473  -24.017 0.50 72.30  ? 160 SER   B CB  1 
ATOM   1412 C  CB  B SER   B 2 151 ? -1.235  -0.262  -24.141 0.50 72.28  ? 160 SER   B CB  1 
ATOM   1413 O  OG  A SER   B 2 151 ? -2.473  -0.797  -24.374 0.50 74.59  ? 160 SER   B OG  1 
ATOM   1414 O  OG  B SER   B 2 151 ? -0.282  -1.310  -24.113 0.50 74.49  ? 160 SER   B OG  1 
ATOM   1415 N  N   . TYR   B 2 152 ? -3.231  0.479   -21.824 1.00 66.98  ? 161 TYR   B N   1 
ATOM   1416 C  CA  . TYR   B 2 152 ? -4.186  0.193   -20.775 1.00 64.56  ? 161 TYR   B CA  1 
ATOM   1417 C  C   . TYR   B 2 152 ? -4.940  -1.134  -20.927 1.00 62.46  ? 161 TYR   B C   1 
ATOM   1418 O  O   . TYR   B 2 152 ? -5.520  -1.404  -21.970 1.00 62.42  ? 161 TYR   B O   1 
ATOM   1419 C  CB  . TYR   B 2 152 ? -5.183  1.361   -20.688 1.00 63.96  ? 161 TYR   B CB  1 
ATOM   1420 C  CG  . TYR   B 2 152 ? -6.148  1.219   -19.539 1.00 63.75  ? 161 TYR   B CG  1 
ATOM   1421 C  CD1 . TYR   B 2 152 ? -5.706  1.285   -18.225 1.00 64.38  ? 161 TYR   B CD1 1 
ATOM   1422 C  CD2 . TYR   B 2 152 ? -7.495  0.976   -19.763 1.00 64.07  ? 161 TYR   B CD2 1 
ATOM   1423 C  CE1 . TYR   B 2 152 ? -6.577  1.103   -17.162 1.00 64.93  ? 161 TYR   B CE1 1 
ATOM   1424 C  CE2 . TYR   B 2 152 ? -8.378  0.809   -18.710 1.00 64.83  ? 161 TYR   B CE2 1 
ATOM   1425 C  CZ  . TYR   B 2 152 ? -7.911  0.856   -17.410 1.00 65.81  ? 161 TYR   B CZ  1 
ATOM   1426 O  OH  . TYR   B 2 152 ? -8.774  0.700   -16.363 1.00 67.29  ? 161 TYR   B OH  1 
ATOM   1427 N  N   . VAL   B 2 153 ? -4.978  -1.940  -19.853 1.00 60.71  ? 162 VAL   B N   1 
ATOM   1428 C  CA  . VAL   B 2 153 ? -5.731  -3.199  -19.828 1.00 58.91  ? 162 VAL   B CA  1 
ATOM   1429 C  C   . VAL   B 2 153 ? -6.705  -3.151  -18.658 1.00 56.10  ? 162 VAL   B C   1 
ATOM   1430 O  O   . VAL   B 2 153 ? -6.284  -2.916  -17.537 1.00 55.35  ? 162 VAL   B O   1 
ATOM   1431 C  CB  . VAL   B 2 153 ? -4.848  -4.468  -19.795 1.00 59.52  ? 162 VAL   B CB  1 
ATOM   1432 C  CG1 . VAL   B 2 153 ? -5.702  -5.714  -19.988 1.00 59.70  ? 162 VAL   B CG1 1 
ATOM   1433 C  CG2 . VAL   B 2 153 ? -3.771  -4.401  -20.870 1.00 60.61  ? 162 VAL   B CG2 1 
ATOM   1434 N  N   . SER   B 2 154 ? -8.005  -3.302  -18.922 1.00 54.55  ? 163 SER   B N   1 
ATOM   1435 C  CA  . SER   B 2 154 ? -9.014  -3.221  -17.866 1.00 53.59  ? 163 SER   B CA  1 
ATOM   1436 C  C   . SER   B 2 154 ? -9.590  -4.575  -17.544 1.00 52.64  ? 163 SER   B C   1 
ATOM   1437 O  O   . SER   B 2 154 ? -9.815  -5.375  -18.443 1.00 53.06  ? 163 SER   B O   1 
ATOM   1438 C  CB  . SER   B 2 154 ? -10.158 -2.295  -18.289 1.00 54.33  ? 163 SER   B CB  1 
ATOM   1439 O  OG  . SER   B 2 154 ? -11.330 -2.424  -17.490 1.00 55.00  ? 163 SER   B OG  1 
ATOM   1440 N  N   . ALA   B 2 155 ? -9.933  -4.788  -16.288 1.00 51.21  ? 164 ALA   B N   1 
ATOM   1441 C  CA  . ALA   B 2 155 ? -10.632 -5.996  -15.881 1.00 50.51  ? 164 ALA   B CA  1 
ATOM   1442 C  C   . ALA   B 2 155 ? -12.107 -5.900  -16.349 1.00 50.31  ? 164 ALA   B C   1 
ATOM   1443 O  O   . ALA   B 2 155 ? -12.627 -4.800  -16.615 1.00 49.29  ? 164 ALA   B O   1 
ATOM   1444 C  CB  . ALA   B 2 155 ? -10.592 -6.114  -14.368 1.00 50.05  ? 164 ALA   B CB  1 
ATOM   1445 N  N   . ILE   B 2 156 ? -12.772 -7.055  -16.462 1.00 50.74  ? 165 ILE   B N   1 
ATOM   1446 C  CA  . ILE   B 2 156 ? -14.199 -7.067  -16.749 1.00 51.51  ? 165 ILE   B CA  1 
ATOM   1447 C  C   . ILE   B 2 156 ? -14.778 -7.187  -15.344 1.00 51.13  ? 165 ILE   B C   1 
ATOM   1448 O  O   . ILE   B 2 156 ? -14.845 -8.294  -14.798 1.00 51.14  ? 165 ILE   B O   1 
ATOM   1449 C  CB  . ILE   B 2 156 ? -14.650 -8.233  -17.659 1.00 53.00  ? 165 ILE   B CB  1 
ATOM   1450 C  CG1 . ILE   B 2 156 ? -13.871 -8.255  -18.992 1.00 54.57  ? 165 ILE   B CG1 1 
ATOM   1451 C  CG2 . ILE   B 2 156 ? -16.153 -8.124  -17.903 1.00 53.65  ? 165 ILE   B CG2 1 
ATOM   1452 C  CD1 . ILE   B 2 156 ? -14.159 -9.439  -19.850 1.00 55.94  ? 165 ILE   B CD1 1 
ATOM   1453 N  N   . THR   B 2 157 ? -15.038 -6.024  -14.707 1.00 50.36  ? 166 THR   B N   1 
ATOM   1454 C  CA  . THR   B 2 157 ? -15.508 -5.925  -13.324 1.00 50.12  ? 166 THR   B CA  1 
ATOM   1455 C  C   . THR   B 2 157 ? -16.997 -6.121  -13.193 1.00 49.91  ? 166 THR   B C   1 
ATOM   1456 O  O   . THR   B 2 157 ? -17.769 -5.244  -13.574 1.00 49.95  ? 166 THR   B O   1 
ATOM   1457 C  CB  . THR   B 2 157 ? -15.102 -4.591  -12.690 1.00 50.66  ? 166 THR   B CB  1 
ATOM   1458 O  OG1 . THR   B 2 157 ? -13.691 -4.438  -12.787 1.00 51.09  ? 166 THR   B OG1 1 
ATOM   1459 C  CG2 . THR   B 2 157 ? -15.470 -4.524  -11.250 1.00 51.12  ? 166 THR   B CG2 1 
ATOM   1460 N  N   . GLN   B 2 158 ? -17.398 -7.234  -12.593 1.00 49.50  ? 167 GLN   B N   1 
ATOM   1461 C  CA  . GLN   B 2 158 ? -18.800 -7.536  -12.399 1.00 49.90  ? 167 GLN   B CA  1 
ATOM   1462 C  C   . GLN   B 2 158 ? -19.155 -7.667  -10.895 1.00 52.36  ? 167 GLN   B C   1 
ATOM   1463 O  O   . GLN   B 2 158 ? -18.398 -8.241  -10.116 1.00 52.95  ? 167 GLN   B O   1 
ATOM   1464 C  CB  . GLN   B 2 158 ? -19.170 -8.815  -13.192 1.00 48.01  ? 167 GLN   B CB  1 
ATOM   1465 C  CG  . GLN   B 2 158 ? -20.628 -9.243  -13.147 1.00 46.36  ? 167 GLN   B CG  1 
ATOM   1466 C  CD  . GLN   B 2 158 ? -21.581 -8.224  -13.739 1.00 48.22  ? 167 GLN   B CD  1 
ATOM   1467 O  OE1 . GLN   B 2 158 ? -21.650 -7.071  -13.310 1.00 48.79  ? 167 GLN   B OE1 1 
ATOM   1468 N  NE2 . GLN   B 2 158 ? -22.372 -8.636  -14.705 1.00 47.68  ? 167 GLN   B NE2 1 
ATOM   1469 N  N   . GLY   B 2 159 ? -20.313 -7.152  -10.516 1.00 53.66  ? 168 GLY   B N   1 
ATOM   1470 C  CA  . GLY   B 2 159 ? -20.807 -7.288  -9.159  1.00 55.85  ? 168 GLY   B CA  1 
ATOM   1471 C  C   . GLY   B 2 159 ? -21.522 -8.609  -8.944  1.00 58.30  ? 168 GLY   B C   1 
ATOM   1472 O  O   . GLY   B 2 159 ? -21.538 -9.471  -9.824  1.00 58.16  ? 168 GLY   B O   1 
ATOM   1473 N  N   . LYS   B 2 160 ? -22.103 -8.785  -7.753  1.00 60.48  ? 169 LYS   B N   1 
ATOM   1474 C  CA  . LYS   B 2 160 ? -22.848 -9.988  -7.384  1.00 62.87  ? 169 LYS   B CA  1 
ATOM   1475 C  C   . LYS   B 2 160 ? -24.326 -9.622  -7.164  1.00 65.30  ? 169 LYS   B C   1 
ATOM   1476 O  O   . LYS   B 2 160 ? -24.614 -8.621  -6.507  1.00 65.71  ? 169 LYS   B O   1 
ATOM   1477 C  CB  . LYS   B 2 160 ? -22.255 -10.610 -6.103  1.00 64.88  ? 169 LYS   B CB  1 
ATOM   1478 C  CG  . LYS   B 2 160 ? -22.897 -11.938 -5.721  1.00 69.15  ? 169 LYS   B CG  1 
ATOM   1479 C  CD  . LYS   B 2 160 ? -22.676 -12.304 -4.267  1.00 73.59  ? 169 LYS   B CD  1 
ATOM   1480 C  CE  . LYS   B 2 160 ? -23.512 -13.495 -3.853  1.00 77.22  ? 169 LYS   B CE  1 
ATOM   1481 N  NZ  . LYS   B 2 160 ? -23.512 -13.682 -2.372  1.00 79.24  ? 169 LYS   B NZ  1 
ATOM   1482 N  N   . ARG   B 2 161 ? -25.256 -10.407 -7.719  1.00 66.82  ? 170 ARG   B N   1 
ATOM   1483 C  CA  . ARG   B 2 161 ? -26.686 -10.132 -7.553  1.00 68.75  ? 170 ARG   B CA  1 
ATOM   1484 C  C   . ARG   B 2 161 ? -27.242 -10.934 -6.364  1.00 70.67  ? 170 ARG   B C   1 
ATOM   1485 O  O   . ARG   B 2 161 ? -26.830 -12.076 -6.142  1.00 71.10  ? 170 ARG   B O   1 
ATOM   1486 C  CB  . ARG   B 2 161 ? -27.455 -10.462 -8.851  1.00 69.90  ? 170 ARG   B CB  1 
ATOM   1487 C  CG  . ARG   B 2 161 ? -28.715 -9.630  -9.053  1.00 71.90  ? 170 ARG   B CG  1 
ATOM   1488 C  CD  . ARG   B 2 161 ? -29.639 -10.210 -10.109 1.00 74.85  ? 170 ARG   B CD  1 
ATOM   1489 N  NE  . ARG   B 2 161 ? -31.038 -9.880  -9.823  1.00 77.50  ? 170 ARG   B NE  1 
ATOM   1490 C  CZ  . ARG   B 2 161 ? -31.779 -9.042  -10.543 1.00 79.00  ? 170 ARG   B CZ  1 
ATOM   1491 N  NH1 . ARG   B 2 161 ? -31.280 -8.471  -11.633 1.00 77.76  ? 170 ARG   B NH1 1 
ATOM   1492 N  NH2 . ARG   B 2 161 ? -33.032 -8.786  -10.192 1.00 79.01  ? 170 ARG   B NH2 1 
ATOM   1493 N  N   . GLU   B 2 162 ? -28.169 -10.342 -5.599  1.00 71.57  ? 171 GLU   B N   1 
ATOM   1494 C  CA  . GLU   B 2 162 ? -28.763 -11.002 -4.434  1.00 72.96  ? 171 GLU   B CA  1 
ATOM   1495 C  C   . GLU   B 2 162 ? -30.141 -11.593 -4.750  1.00 73.32  ? 171 GLU   B C   1 
ATOM   1496 O  O   . GLU   B 2 162 ? -30.639 -12.452 -4.018  1.00 73.47  ? 171 GLU   B O   1 
ATOM   1497 C  CB  . GLU   B 2 162 ? -28.855 -10.019 -3.256  1.00 76.43  ? 171 GLU   B CB  1 
ATOM   1498 C  CG  . GLU   B 2 162 ? -27.517 -9.419  -2.857  1.00 83.16  ? 171 GLU   B CG  1 
ATOM   1499 C  CD  . GLU   B 2 162 ? -26.540 -10.414 -2.263  1.00 92.77  ? 171 GLU   B CD  1 
ATOM   1500 O  OE1 . GLU   B 2 162 ? -26.976 -11.275 -1.463  1.00 94.76  ? 171 GLU   B OE1 1 
ATOM   1501 O  OE2 . GLU   B 2 162 ? -25.335 -10.333 -2.598  1.00 95.96  ? 171 GLU   B OE2 1 
HETATM 1502 S  S   . DMS   C 3 .   ? -18.727 11.721  -0.374  1.00 92.53  ? 201 DMS   B S   1 
HETATM 1503 O  O   . DMS   C 3 .   ? -19.643 10.545  -0.559  1.00 92.55  ? 201 DMS   B O   1 
HETATM 1504 C  C1  . DMS   C 3 .   ? -19.631 13.239  -0.770  1.00 92.56  ? 201 DMS   B C1  1 
HETATM 1505 C  C2  . DMS   C 3 .   ? -17.604 11.831  -1.802  1.00 92.38  ? 201 DMS   B C2  1 
HETATM 1506 N  N1  . A1B9E D 4 .   ? -6.309  2.443   -12.773 1.00 60.30  ? 202 A1B9E B N1  1 
HETATM 1507 N  N3  . A1B9E D 4 .   ? -9.040  2.496   -7.215  1.00 54.86  ? 202 A1B9E B N3  1 
HETATM 1508 C  C4  . A1B9E D 4 .   ? -7.798  4.118   -13.723 1.00 58.68  ? 202 A1B9E B C4  1 
HETATM 1509 C  C5  . A1B9E D 4 .   ? -8.806  4.372   -11.458 1.00 56.13  ? 202 A1B9E B C5  1 
HETATM 1510 C  C6  . A1B9E D 4 .   ? -8.492  5.516   -10.712 1.00 55.66  ? 202 A1B9E B C6  1 
HETATM 1511 C  C7  . A1B9E D 4 .   ? -8.485  5.460   -9.328  1.00 55.23  ? 202 A1B9E B C7  1 
HETATM 1512 C  C8  . A1B9E D 4 .   ? -8.794  4.259   -8.698  1.00 55.06  ? 202 A1B9E B C8  1 
HETATM 1513 C  C10 . A1B9E D 4 .   ? -9.183  3.185   -10.822 1.00 55.48  ? 202 A1B9E B C10 1 
HETATM 1514 C  C13 . A1B9E D 4 .   ? -8.027  4.441   -15.196 1.00 59.26  ? 202 A1B9E B C13 1 
HETATM 1515 C  C15 . A1B9E D 4 .   ? -9.192  4.311   -17.297 1.00 58.41  ? 202 A1B9E B C15 1 
HETATM 1516 C  C17 . A1B9E D 4 .   ? -7.065  5.403   -17.202 1.00 59.91  ? 202 A1B9E B C17 1 
HETATM 1517 C  C20 . A1B9E D 4 .   ? -4.682  6.466   -17.100 1.00 60.97  ? 202 A1B9E B C20 1 
HETATM 1518 C  C21 . A1B9E D 4 .   ? -6.990  5.078   -15.857 1.00 59.73  ? 202 A1B9E B C21 1 
HETATM 1519 O  O1  . A1B9E D 4 .   ? -7.985  1.738   -14.092 1.00 59.27  ? 202 A1B9E B O1  1 
HETATM 1520 C  C1  . A1B9E D 4 .   ? -7.359  2.649   -13.569 1.00 59.30  ? 202 A1B9E B C1  1 
HETATM 1521 C  C2  . A1B9E D 4 .   ? -5.077  3.213   -12.834 1.00 61.52  ? 202 A1B9E B C2  1 
HETATM 1522 C  C3  . A1B9E D 4 .   ? -4.360  3.054   -14.154 1.00 62.68  ? 202 A1B9E B C3  1 
HETATM 1523 F  F1  . A1B9E D 4 .   ? -4.673  1.886   -14.772 1.00 62.99  ? 202 A1B9E B F1  1 
HETATM 1524 F  F2  . A1B9E D 4 .   ? -3.017  3.016   -13.965 1.00 63.38  ? 202 A1B9E B F2  1 
HETATM 1525 N  N2  . A1B9E D 4 .   ? -8.889  4.461   -12.840 1.00 57.45  ? 202 A1B9E B N2  1 
HETATM 1526 C  C9  . A1B9E D 4 .   ? -9.164  3.141   -9.436  1.00 55.18  ? 202 A1B9E B C9  1 
HETATM 1527 C  C11 . A1B9E D 4 .   ? -9.529  2.013   -8.514  1.00 55.05  ? 202 A1B9E B C11 1 
HETATM 1528 C  C12 . A1B9E D 4 .   ? -8.941  3.965   -7.232  1.00 54.73  ? 202 A1B9E B C12 1 
HETATM 1529 C  C14 . A1B9E D 4 .   ? -9.146  4.062   -15.935 1.00 58.99  ? 202 A1B9E B C14 1 
HETATM 1530 CL CL1 . A1B9E D 4 .   ? -10.572 3.831   -18.259 1.00 57.42  ? 202 A1B9E B CL1 1 
HETATM 1531 C  C16 . A1B9E D 4 .   ? -8.163  4.968   -17.927 1.00 59.18  ? 202 A1B9E B C16 1 
HETATM 1532 C  C18 . A1B9E D 4 .   ? -5.907  6.070   -17.858 1.00 60.67  ? 202 A1B9E B C18 1 
HETATM 1533 C  C19 . A1B9E D 4 .   ? -4.612  5.359   -18.065 1.00 61.02  ? 202 A1B9E B C19 1 
HETATM 1534 S  S   . DMS   E 3 .   ? -30.667 17.875  -6.684  1.00 107.12 ? 203 DMS   B S   1 
HETATM 1535 O  O   . DMS   E 3 .   ? -31.325 17.967  -8.036  1.00 107.05 ? 203 DMS   B O   1 
HETATM 1536 C  C1  . DMS   E 3 .   ? -29.323 19.100  -6.599  1.00 107.08 ? 203 DMS   B C1  1 
HETATM 1537 C  C2  . DMS   E 3 .   ? -29.593 16.409  -6.658  1.00 107.16 ? 203 DMS   B C2  1 
HETATM 1538 O  O   . HOH   F 5 .   ? -2.233  -3.993  -6.127  1.00 49.05  ? 101 HOH   A O   1 
HETATM 1539 O  O   . HOH   F 5 .   ? -23.343 19.108  -19.448 1.00 64.63  ? 102 HOH   A O   1 
HETATM 1540 O  O   . HOH   F 5 .   ? -23.944 8.773   -27.672 1.00 48.29  ? 103 HOH   A O   1 
HETATM 1541 O  O   . HOH   F 5 .   ? -4.619  -15.032 -25.175 1.00 40.96  ? 104 HOH   A O   1 
HETATM 1542 O  O   . HOH   F 5 .   ? -6.506  -5.053  6.623   1.00 42.05  ? 105 HOH   A O   1 
HETATM 1543 O  O   . HOH   F 5 .   ? -7.013  -9.526  -3.158  1.00 55.94  ? 106 HOH   A O   1 
HETATM 1544 O  O   . HOH   F 5 .   ? -9.202  3.540   -3.299  1.00 50.14  ? 107 HOH   A O   1 
HETATM 1545 O  O   . HOH   F 5 .   ? -5.714  1.735   -9.717  1.00 51.94  ? 108 HOH   A O   1 
HETATM 1546 O  O   . HOH   F 5 .   ? -2.601  -11.955 -6.842  1.00 48.86  ? 109 HOH   A O   1 
HETATM 1547 O  O   . HOH   F 5 .   ? -8.654  1.304   1.146   1.00 49.90  ? 110 HOH   A O   1 
HETATM 1548 O  O   . HOH   F 5 .   ? -3.894  -0.629  0.141   1.00 57.52  ? 111 HOH   A O   1 
HETATM 1549 O  O   . HOH   F 5 .   ? -4.578  -10.545 -5.476  1.00 46.29  ? 112 HOH   A O   1 
HETATM 1550 O  O   . HOH   F 5 .   ? -23.889 21.149  -4.079  1.00 56.10  ? 113 HOH   A O   1 
HETATM 1551 O  O   . HOH   F 5 .   ? -31.057 0.040   -23.061 1.00 57.10  ? 114 HOH   A O   1 
HETATM 1552 O  O   . HOH   F 5 .   ? -21.554 -9.381  -34.733 1.00 52.31  ? 115 HOH   A O   1 
HETATM 1553 O  O   . HOH   F 5 .   ? 1.292   -1.998  -11.965 1.00 62.26  ? 116 HOH   A O   1 
HETATM 1554 O  O   . HOH   F 5 .   ? -3.034  -9.118  -3.123  1.00 49.56  ? 117 HOH   A O   1 
HETATM 1555 O  O   . HOH   F 5 .   ? -0.898  -15.109 -9.976  1.00 62.29  ? 118 HOH   A O   1 
HETATM 1556 O  O   . HOH   G 5 .   ? -33.949 1.527   -15.284 1.00 49.66  ? 301 HOH   B O   1 
HETATM 1557 O  O   . HOH   G 5 .   ? -18.064 -11.161 -16.438 1.00 43.52  ? 302 HOH   B O   1 
HETATM 1558 O  O   . HOH   G 5 .   ? -6.519  -0.657  -10.788 1.00 38.68  ? 303 HOH   B O   1 
HETATM 1559 O  O   . HOH   G 5 .   ? -23.844 -6.806  -4.891  1.00 53.63  ? 304 HOH   B O   1 
HETATM 1560 O  O   . HOH   G 5 .   ? -35.253 -5.828  -10.393 1.00 53.50  ? 305 HOH   B O   1 
HETATM 1561 O  O   . HOH   G 5 .   ? -16.327 20.405  -14.398 1.00 60.87  ? 306 HOH   B O   1 
HETATM 1562 O  O   . HOH   G 5 .   ? -11.644 1.486   -5.691  1.00 38.88  ? 307 HOH   B O   1 
HETATM 1563 O  O   . HOH   G 5 .   ? -16.451 25.644  -12.261 1.00 61.71  ? 308 HOH   B O   1 
HETATM 1564 O  O   . HOH   G 5 .   ? -17.008 12.592  -5.378  1.00 43.44  ? 309 HOH   B O   1 
HETATM 1565 O  O   . HOH   G 5 .   ? -29.428 -2.031  -19.328 1.00 55.45  ? 310 HOH   B O   1 
HETATM 1566 O  O   . HOH   G 5 .   ? -12.985 -2.598  -14.629 1.00 46.00  ? 311 HOH   B O   1 
HETATM 1567 O  O   . HOH   G 5 .   ? -26.274 -8.317  -16.721 1.00 60.53  ? 312 HOH   B O   1 
HETATM 1568 O  O   . HOH   G 5 .   ? -28.444 -7.507  -5.755  1.00 60.28  ? 313 HOH   B O   1 
HETATM 1569 O  O   . HOH   G 5 .   ? -9.536  -7.389  -25.377 1.00 53.09  ? 314 HOH   B O   1 
HETATM 1570 O  O   . HOH   G 5 .   ? -20.511 14.323  -33.349 1.00 57.59  ? 315 HOH   B O   1 
HETATM 1571 O  O   . HOH   G 5 .   ? -12.316 -3.822  -9.736  1.00 53.75  ? 316 HOH   B O   1 
HETATM 1572 O  O   . HOH   G 5 .   ? -7.168  -11.054 -0.028  1.00 65.27  ? 317 HOH   B O   1 
HETATM 1573 O  O   . HOH   G 5 .   ? -16.219 -15.395 -16.407 1.00 60.25  ? 318 HOH   B O   1 
HETATM 1574 O  O   . HOH   G 5 .   ? -30.002 -5.704  -1.133  1.00 37.74  ? 319 HOH   B O   1 
HETATM 1575 O  O   . HOH   G 5 .   ? -27.823 -6.437  -18.846 1.00 55.37  ? 320 HOH   B O   1 
HETATM 1576 O  O   . HOH   G 5 .   ? -30.814 4.597   -2.859  1.00 48.89  ? 321 HOH   B O   1 
HETATM 1577 O  O   . HOH   G 5 .   ? -17.361 -16.234 -30.744 1.00 55.66  ? 322 HOH   B O   1 
HETATM 1578 O  O   . HOH   G 5 .   ? -15.058 -5.249  1.350   1.00 51.08  ? 323 HOH   B O   1 
HETATM 1579 O  O   . HOH   G 5 .   ? -21.348 -12.527 -12.989 1.00 51.29  ? 324 HOH   B O   1 
HETATM 1580 O  O   . HOH   G 5 .   ? -1.357  -17.909 -18.936 1.00 60.65  ? 325 HOH   B O   1 
HETATM 1581 O  O   . HOH   G 5 .   ? -17.855 15.168  -21.955 1.00 56.63  ? 326 HOH   B O   1 
HETATM 1582 O  O   . HOH   G 5 .   ? -28.800 15.601  -15.032 1.00 64.73  ? 327 HOH   B O   1 
HETATM 1583 O  O   . HOH   G 5 .   ? -23.850 -15.426 -17.922 1.00 60.33  ? 328 HOH   B O   1 
HETATM 1584 O  O   . HOH   G 5 .   ? -7.119  -11.086 -5.458  1.00 53.07  ? 329 HOH   B O   1 
HETATM 1585 O  O   . HOH   G 5 .   ? -22.391 6.650   -0.063  0.50 26.42  ? 330 HOH   B O   1 
HETATM 1586 O  O   . HOH   G 5 .   ? -10.737 11.880  -19.006 1.00 42.87  ? 331 HOH   B O   1 
HETATM 1587 O  O   . HOH   G 5 .   ? -32.082 6.886   -4.252  1.00 63.88  ? 332 HOH   B O   1 
HETATM 1588 O  O   . HOH   G 5 .   ? -9.242  -11.289 -7.583  1.00 59.22  ? 333 HOH   B O   1 
HETATM 1589 O  O   . HOH   G 5 .   ? -33.750 7.244   -11.916 1.00 67.34  ? 334 HOH   B O   1 
HETATM 1590 O  O   . HOH   G 5 .   ? -18.890 25.062  -14.322 1.00 63.95  ? 335 HOH   B O   1 
HETATM 1591 O  O   . HOH   G 5 .   ? -20.919 2.343   -32.563 1.00 58.13  ? 336 HOH   B O   1 
HETATM 1592 O  O   . HOH   G 5 .   ? -15.280 16.230  -20.546 1.00 53.72  ? 337 HOH   B O   1 
HETATM 1593 O  O   . HOH   G 5 .   ? -15.115 -9.199  -11.769 1.00 49.60  ? 338 HOH   B O   1 
HETATM 1594 O  O   . HOH   G 5 .   ? -19.647 -6.161  -0.714  1.00 53.88  ? 339 HOH   B O   1 
HETATM 1595 O  O   . HOH   G 5 .   ? -14.782 -12.896 -16.582 1.00 56.93  ? 340 HOH   B O   1 
HETATM 1596 O  O   . HOH   G 5 .   ? -25.746 -5.062  -3.980  1.00 41.30  ? 341 HOH   B O   1 
HETATM 1597 O  O   . HOH   G 5 .   ? -0.710  0.472   -13.431 1.00 50.97  ? 342 HOH   B O   1 
HETATM 1598 O  O   . HOH   G 5 .   ? -9.899  -15.873 -24.212 1.00 49.13  ? 343 HOH   B O   1 
HETATM 1599 O  O   . HOH   G 5 .   ? -31.045 -10.191 -27.969 0.50 31.58  ? 344 HOH   B O   1 
HETATM 1600 O  O   . HOH   G 5 .   ? -20.628 -14.159 -22.530 1.00 54.62  ? 345 HOH   B O   1 
HETATM 1601 O  O   . HOH   G 5 .   ? -9.375  7.728   -13.225 1.00 42.77  ? 346 HOH   B O   1 
HETATM 1602 O  O   . HOH   G 5 .   ? -17.182 14.026  -31.220 1.00 54.09  ? 347 HOH   B O   1 
HETATM 1603 O  O   . HOH   G 5 .   ? -21.735 -14.407 -25.773 1.00 56.60  ? 348 HOH   B O   1 
HETATM 1604 O  O   . HOH   G 5 .   ? -32.716 -7.515  -6.910  1.00 66.54  ? 349 HOH   B O   1 
HETATM 1605 O  O   . HOH   G 5 .   ? -35.284 0.609   -7.830  1.00 56.33  ? 350 HOH   B O   1 
HETATM 1606 O  O   . HOH   G 5 .   ? -28.688 -8.751  -17.770 1.00 62.37  ? 351 HOH   B O   1 
HETATM 1607 O  O   . HOH   G 5 .   ? -35.378 -4.647  -17.068 1.00 51.71  ? 352 HOH   B O   1 
HETATM 1608 O  O   . HOH   G 5 .   ? -11.581 -13.059 -8.453  1.00 60.61  ? 353 HOH   B O   1 
HETATM 1609 O  O   . HOH   G 5 .   ? -11.168 11.431  -15.015 1.00 49.15  ? 354 HOH   B O   1 
HETATM 1610 O  O   . HOH   G 5 .   ? -11.207 -7.818  2.029   1.00 57.12  ? 355 HOH   B O   1 
HETATM 1611 O  O   . HOH   G 5 .   ? -21.296 4.279   -0.000  0.50 67.63  ? 356 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   ? 0.9757 0.4105 0.9218 0.1735  0.0070  -0.1603 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.9601 0.4630 0.8889 0.2017  0.0161  -0.1616 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.9427 0.4539 0.8638 0.2006  0.0305  -0.1136 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.9677 0.4139 0.8825 0.2038  0.0307  -0.0838 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.0008 0.4897 0.9187 0.2484  0.0045  -0.1954 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.0495 0.6261 0.9632 0.2670  0.0100  -0.2290 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.0623 0.6371 0.9736 0.2941  0.0003  -0.2715 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.0621 0.7082 0.9750 0.2542  0.0253  -0.2125 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.8965 0.4846 0.8145 0.1962  0.0426  -0.1060 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.8769 0.4807 0.7855 0.1972  0.0546  -0.0671 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.8597 0.4873 0.7551 0.2362  0.0515  -0.0732 51  MET   A C   
12   O  O   . MET   A 8   ? 0.8456 0.5081 0.7457 0.2556  0.0462  -0.1082 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.8502 0.5164 0.7653 0.1688  0.0671  -0.0545 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.8539 0.5035 0.7869 0.1322  0.0698  -0.0419 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.8128 0.5340 0.7526 0.1064  0.0806  -0.0292 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.8231 0.5188 0.7946 0.0690  0.0787  -0.0207 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.8562 0.4702 0.7357 0.2482  0.0550  -0.0404 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.8432 0.4830 0.7124 0.2856  0.0482  -0.0458 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.8259 0.4915 0.6807 0.2848  0.0559  -0.0152 52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.8315 0.4781 0.6780 0.2615  0.0675  0.0165  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.8745 0.4506 0.7303 0.3243  0.0317  -0.0508 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.9304 0.4200 0.7614 0.3220  0.0327  -0.0098 52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.9636 0.3867 0.8011 0.2970  0.0346  -0.0031 52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.9637 0.4364 0.7638 0.3456  0.0313  0.0214  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 1.0136 0.3575 0.8311 0.2892  0.0402  0.0384  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 1.0135 0.4057 0.7842 0.3430  0.0366  0.0637  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 1.0480 0.3749 0.8292 0.3133  0.0427  0.0736  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 1.1143 0.3607 0.8693 0.3058  0.0520  0.1185  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.8021 0.5150 0.6568 0.3106  0.0492  -0.0275 53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.7964 0.5352 0.6365 0.3136  0.0523  -0.0058 53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.8223 0.5363 0.6371 0.3572  0.0361  0.0021  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.8318 0.5435 0.6530 0.3901  0.0199  -0.0218 53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.7587 0.5780 0.6208 0.2981  0.0582  -0.0236 53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.7384 0.6088 0.6247 0.3204  0.0483  -0.0611 53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.7503 0.5854 0.6257 0.2580  0.0728  -0.0239 53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.7176 0.6592 0.6245 0.3065  0.0539  -0.0731 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.8349 0.5282 0.6176 0.3599  0.0402  0.0360  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.8638 0.5318 0.6094 0.4013  0.0252  0.0503  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.8478 0.5657 0.5824 0.4020  0.0260  0.0556  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.8488 0.5716 0.5782 0.3728  0.0443  0.0757  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.9388 0.5202 0.6425 0.4028  0.0335  0.0937  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 1.0374 0.5453 0.7357 0.4197  0.0235  0.0929  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 1.1842 0.6016 0.8453 0.4111  0.0363  0.1399  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 1.1953 0.6144 0.8362 0.3910  0.0563  0.1737  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.2744 0.6180 0.9274 0.4244  0.0274  0.1428  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.8335 0.5865 0.5647 0.4368  0.0047  0.0369  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.8289 0.6251 0.5488 0.4394  0.0012  0.0374  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.8654 0.6149 0.5271 0.4464  0.0104  0.0793  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.9005 0.5854 0.5212 0.4683  0.0091  0.1065  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.8312 0.6765 0.5642 0.4761  -0.0276 0.0046  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.8478 0.7596 0.6024 0.4614  -0.0305 -0.0144 55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.8553 0.8311 0.6462 0.4856  -0.0573 -0.0554 55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.8773 0.9035 0.6844 0.4694  -0.0611 -0.0704 55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.9406 0.9653 0.7108 0.4928  -0.0782 -0.0667 55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.9867 0.9658 0.6983 0.5350  -0.0919 -0.0462 55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.9161 0.9807 0.7035 0.4753  -0.0820 -0.0833 55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.8491 0.6283 0.5055 0.4280  0.0215  0.0858  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.8842 0.6312 0.4854 0.4359  0.0336  0.1226  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.8926 0.6778 0.4683 0.4583  0.0196  0.1117  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.9248 0.6888 0.4480 0.4712  0.0289  0.1392  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.8825 0.6171 0.4929 0.3943  0.0652  0.1474  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.8591 0.7006 0.4721 0.4621  -0.0016 0.0713  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.8618 0.7381 0.4562 0.4827  -0.0199 0.0546  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.8286 0.7667 0.4784 0.4603  -0.0291 0.0157  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.8053 0.7643 0.5079 0.4286  -0.0196 0.0022  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.8275 0.7926 0.4623 0.4782  -0.0486 -0.0029 58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.8045 0.8217 0.4879 0.4581  -0.0602 -0.0396 58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.8255 0.8370 0.5053 0.4282  -0.0395 -0.0290 58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.8456 0.8253 0.4755 0.4367  -0.0243 -0.0002 58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.8114 0.8563 0.4797 0.4944  -0.0963 -0.0685 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.8650 0.9358 0.5548 0.5245  -0.1250 -0.0925 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.8842 0.9445 0.5932 0.5225  -0.1162 -0.0843 58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.8845 0.9871 0.5722 0.5528  -0.1586 -0.1219 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.8125 0.8559 0.5441 0.3954  -0.0393 -0.0525 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.8370 0.8731 0.5660 0.3713  -0.0248 -0.0461 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.8654 0.9174 0.5845 0.3865  -0.0490 -0.0735 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.8381 0.9207 0.6032 0.3708  -0.0652 -0.1057 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.8170 0.8627 0.5955 0.3270  -0.0068 -0.0466 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.8338 0.8561 0.6077 0.3176  0.0158  -0.0184 59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.8242 0.8631 0.6030 0.3063  0.0008  -0.0457 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.8313 0.8679 0.6493 0.2831  0.0281  -0.0237 59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.9053 0.9368 0.5631 0.4180  -0.0514 -0.0617 60  THR   A N   
83   N  N   B THR   A 17  ? 0.9054 0.9370 0.5635 0.4177  -0.0513 -0.0618 60  THR   A N   
84   C  CA  A THR   A 17  ? 0.9291 0.9702 0.5634 0.4404  -0.0760 -0.0886 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.9287 0.9706 0.5640 0.4404  -0.0766 -0.0894 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.9717 0.9886 0.5552 0.4502  -0.0588 -0.0700 60  THR   A C   
87   C  C   B THR   A 17  ? 0.9723 0.9896 0.5543 0.4520  -0.0599 -0.0705 60  THR   A C   
88   O  O   A THR   A 17  ? 0.9910 0.9861 0.5417 0.4541  -0.0315 -0.0327 60  THR   A O   
89   O  O   B THR   A 17  ? 0.9927 0.9879 0.5400 0.4574  -0.0333 -0.0332 60  THR   A O   
90   C  CB  A THR   A 17  ? 0.9543 1.0036 0.5503 0.4873  -0.1052 -0.1008 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.9506 1.0034 0.5541 0.4853  -0.1069 -0.1035 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.9976 1.0139 0.5323 0.5131  -0.0880 -0.0607 60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.9357 1.0144 0.5900 0.4788  -0.1190 -0.1179 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.9283 1.0135 0.5789 0.4857  -0.1292 -0.1289 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.9546 1.0253 0.5421 0.5089  -0.1408 -0.1418 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.9829 1.0050 0.5611 0.4558  -0.0753 -0.0980 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 1.0339 1.0392 0.5626 0.4727  -0.0621 -0.0878 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 1.0971 1.0998 0.5501 0.5241  -0.0735 -0.0845 61  TRP   A C   
99   O  O   . TRP   A 18  ? 1.0906 1.1082 0.5368 0.5473  -0.1081 -0.1141 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 1.0253 1.0316 0.5769 0.4621  -0.0801 -0.1242 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 1.0573 1.0498 0.5601 0.4858  -0.0730 -0.1252 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 1.0865 1.0802 0.5367 0.5266  -0.0947 -0.1507 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 1.0611 1.0404 0.5683 0.4713  -0.0456 -0.1065 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 1.1043 1.0866 0.5234 0.5397  -0.0790 -0.1477 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 1.0913 1.0660 0.5477 0.5064  -0.0493 -0.1208 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 1.0513 1.0252 0.5978 0.4359  -0.0193 -0.0799 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 1.1011 1.0687 0.5511 0.5072  -0.0270 -0.1101 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 1.0625 1.0288 0.6023 0.4363  -0.0002 -0.0692 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 1.0816 1.0462 0.5762 0.4717  -0.0035 -0.0840 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 1.1519 1.1384 0.5487 0.5418  -0.0442 -0.0475 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.2114 1.1916 0.5253 0.5911  -0.0498 -0.0385 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.2548 1.2390 0.5229 0.6157  -0.0495 -0.0548 62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.2568 1.2377 0.5172 0.6071  -0.0158 -0.0325 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.2666 1.2243 0.5401 0.5966  -0.0145 0.0160  62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.3857 1.3318 0.5647 0.6491  -0.0199 0.0297  62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.5123 1.4360 0.6313 0.6585  0.0239  0.0842  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.5336 1.4510 0.6917 0.6212  0.0597  0.1141  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.5608 1.4745 0.5932 0.7027  0.0225  0.0970  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.2864 1.2804 0.5241 0.6489  -0.0876 -0.0957 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.3347 1.3308 0.5201 0.6796  -0.0910 -0.1166 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.3963 1.3857 0.4916 0.7164  -0.0599 -0.0758 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.4223 1.4026 0.4779 0.7349  -0.0601 -0.0500 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.3695 1.3771 0.5429 0.7074  -0.1439 -0.1734 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.4284 1.4344 0.6274 0.6997  -0.1600 -0.2178 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.5134 1.5229 0.6367 0.7534  -0.1882 -0.2560 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.5563 1.5557 0.7062 0.7464  -0.2065 -0.3028 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.6130 1.6160 0.6947 0.7986  -0.2428 -0.3503 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.4211 1.4145 0.4861 0.7259  -0.0308 -0.0672 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.4707 1.4636 0.4541 0.7561  0.0071  -0.0254 64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.4740 1.4550 0.4783 0.7245  0.0495  0.0340  64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.5019 1.4678 0.4466 0.7437  0.0656  0.0722  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.5482 1.5380 0.4339 0.8131  -0.0169 -0.0334 64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.6587 1.6625 0.4977 0.8540  -0.0454 -0.0855 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.6749 1.6897 0.5204 0.8525  -0.0253 -0.0963 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.7067 1.7111 0.5024 0.8903  -0.0898 -0.1178 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.4461 1.4300 0.5336 0.6762  0.0657  0.0410  65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.4415 1.4156 0.5578 0.6426  0.1040  0.0910  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.4384 1.4319 0.5382 0.6420  0.1527  0.1198  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.4410 1.4559 0.5149 0.6670  0.1538  0.0966  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.4121 1.3843 0.6230 0.5935  0.0950  0.0811  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.4303 1.4184 0.5460 0.6154  0.1925  0.1678  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.4225 1.4381 0.5364 0.6097  0.2407  0.1953  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.3763 1.4214 0.5665 0.5846  0.2415  0.1701  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.3497 1.3891 0.6116 0.5439  0.2378  0.1727  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.4651 1.4639 0.5876 0.5809  0.2790  0.2510  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.5356 1.5698 0.6710 0.5670  0.3321  0.2818  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.6375 1.6594 0.8232 0.5201  0.3638  0.3252  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.6708 1.6487 0.8709 0.5020  0.3456  0.3347  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.6505 1.7092 0.8653 0.5016  0.4059  0.3470  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.3646 1.4386 0.5343 0.6129  0.2443  0.1446  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.3316 1.4287 0.5633 0.5989  0.2414  0.1190  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.3012 1.4390 0.5653 0.5838  0.2887  0.1480  67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.3076 1.4788 0.5338 0.6138  0.3149  0.1499  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.3481 1.4494 0.5517 0.6370  0.2129  0.0689  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.3297 1.4336 0.6036 0.6166  0.1981  0.0426  67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.3784 1.4485 0.5407 0.6582  0.1682  0.0389  67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.2698 1.4102 0.6065 0.5387  0.2986  0.1668  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.2371 1.4224 0.6191 0.5196  0.3398  0.1910  68  THR   A CA  
159  C  C   . THR   A 25  ? 1.1964 1.3904 0.6635 0.4867  0.3251  0.1766  68  THR   A C   
160  O  O   . THR   A 25  ? 1.2027 1.3623 0.6893 0.4736  0.2886  0.1562  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.2605 1.4415 0.6339 0.4971  0.3770  0.2417  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.2455 1.4801 0.6592 0.4822  0.4211  0.2635  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.2605 1.4000 0.6733 0.4571  0.3602  0.2544  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 1.1512 1.3941 0.6674 0.4751  0.3532  0.1867  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 1.1142 1.3687 0.7065 0.4474  0.3392  0.1754  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 1.0858 1.3658 0.6951 0.4735  0.3259  0.1424  69  GLY   A C   
167  O  O   . GLY   A 26  ? 1.1051 1.3655 0.6705 0.5083  0.3045  0.1133  69  GLY   A O   
168  N  N   . ASN   A 27  ? 1.0365 1.3572 0.7120 0.4573  0.3349  0.1444  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 1.0115 1.3559 0.7103 0.4827  0.3208  0.1151  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 0.9937 1.2933 0.7200 0.4673  0.2774  0.0959  70  ASN   A C   
171  O  O   . ASN   A 27  ? 1.0003 1.2626 0.7347 0.4338  0.2635  0.1065  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 0.9882 1.4121 0.7418 0.4818  0.3553  0.1262  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 1.0095 1.4522 0.8379 0.4372  0.3555  0.1420  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 1.0310 1.4515 0.8682 0.3991  0.3613  0.1660  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 0.9882 1.4718 0.8712 0.4440  0.3465  0.1264  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.9707 1.2700 0.7056 0.4942  0.2565  0.0681  71  SER   A N   
177  C  CA  . SER   A 28  ? 0.9656 1.2179 0.7184 0.4830  0.2179  0.0531  71  SER   A CA  
178  C  C   . SER   A 28  ? 0.9210 1.2108 0.7290 0.4863  0.2143  0.0499  71  SER   A C   
179  O  O   . SER   A 28  ? 0.9278 1.2144 0.7321 0.5212  0.1989  0.0266  71  SER   A O   
180  C  CB  . SER   A 28  ? 1.0100 1.2083 0.7171 0.5125  0.1881  0.0218  71  SER   A CB  
181  O  OG  . SER   A 28  ? 1.0608 1.2422 0.7139 0.5261  0.1915  0.0160  71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.8766 1.2009 0.7362 0.4530  0.2252  0.0705  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.8343 1.2023 0.7482 0.4597  0.2186  0.0648  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.8399 1.1578 0.7576 0.4556  0.1786  0.0552  72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.8627 1.1256 0.7617 0.4276  0.1627  0.0619  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.8084 1.2329 0.7758 0.4235  0.2448  0.0885  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.8397 1.2174 0.7799 0.3883  0.2486  0.1068  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.8623 1.1884 0.7343 0.4107  0.2421  0.0972  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.8181 1.1561 0.7587 0.4852  0.1633  0.0403  73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.8344 1.1252 0.7755 0.4847  0.1261  0.0354  73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.7717 1.1204 0.7724 0.4669  0.1256  0.0454  73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.7384 1.1574 0.7827 0.4899  0.1338  0.0375  73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.8909 1.1541 0.8117 0.5341  0.1038  0.0116  73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 1.0050 1.2080 0.8687 0.5515  0.0994  -0.0040 73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 1.0935 1.2473 0.9345 0.5953  0.0705  -0.0286 73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.1781 1.2862 0.9706 0.6160  0.0671  -0.0503 73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.2489 1.2764 1.0054 0.5969  0.0475  -0.0539 73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.2628 1.2468 1.0233 0.5566  0.0336  -0.0348 73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.2654 1.2589 0.9829 0.6181  0.0418  -0.0786 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.7562 1.0824 0.7618 0.4263  0.1173  0.0601  74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.7048 1.0838 0.7653 0.4045  0.1150  0.0670  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.7022 1.0423 0.7540 0.3996  0.0786  0.0672  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.7415 1.0102 0.7478 0.3838  0.0660  0.0735  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.6939 1.0864 0.7695 0.3593  0.1391  0.0836  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.6961 1.1230 0.7749 0.3587  0.1778  0.0909  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.7061 1.1210 0.7868 0.3156  0.1954  0.1094  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.6519 1.1698 0.7882 0.3758  0.1981  0.0860  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.6504 1.0424 0.7469 0.4115  0.0630  0.0610  75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.6593 1.0193 0.7431 0.4089  0.0280  0.0630  75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.6200 0.9988 0.7269 0.3638  0.0307  0.0713  75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.5798 1.0331 0.7484 0.3500  0.0427  0.0676  75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.6767 1.0798 0.7916 0.4496  0.0033  0.0498  75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.8094 1.1589 0.8817 0.4958  -0.0127 0.0420  75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.8586 1.1765 0.9022 0.5024  0.0054  0.0394  75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.8570 1.1916 0.9217 0.5268  -0.0455 0.0378  75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.6309 0.9430 0.6908 0.3393  0.0219  0.0811  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.6060 0.9278 0.6807 0.2989  0.0245  0.0858  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.6142 0.8973 0.6543 0.2934  -0.0058 0.0882  76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.6551 0.8860 0.6480 0.3149  -0.0244 0.0926  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.6201 0.9139 0.6780 0.2686  0.0525  0.0946  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.6039 0.9339 0.6858 0.2756  0.0835  0.0956  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.6680 0.8822 0.6614 0.2668  0.0465  0.1006  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.5778 0.8848 0.6394 0.2653  -0.0106 0.0852  77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.5903 0.8662 0.6146 0.2589  -0.0366 0.0863  77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.5897 0.8448 0.6023 0.2205  -0.0230 0.0881  77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.5692 0.8567 0.6252 0.1982  -0.0041 0.0837  77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.5560 0.8896 0.6187 0.2707  -0.0647 0.0731  77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.6128 0.8120 0.5660 0.2133  -0.0307 0.0953  78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.6104 0.7896 0.5485 0.1819  -0.0190 0.0943  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.6150 0.7996 0.5348 0.1766  -0.0428 0.0863  78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.6464 0.8027 0.5165 0.1927  -0.0614 0.0938  78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.6372 0.7555 0.5241 0.1772  -0.0046 0.1066  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.6488 0.7474 0.5190 0.1497  0.0089  0.1045  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.6203 0.7450 0.5351 0.1331  0.0269  0.0972  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.6812 0.7291 0.5078 0.1465  0.0200  0.1149  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.5867 0.8051 0.5438 0.1554  -0.0437 0.0709  79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.5946 0.8214 0.5341 0.1516  -0.0686 0.0575  79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.6364 0.8193 0.5224 0.1349  -0.0591 0.0584  79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.6539 0.8054 0.5264 0.1246  -0.0340 0.0682  79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.5628 0.8503 0.5723 0.1393  -0.0816 0.0348  79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.5957 0.8889 0.6481 0.1069  -0.0607 0.0260  79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.6338 0.8832 0.6540 0.0951  -0.0401 0.0335  79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.5735 0.9143 0.6934 0.0932  -0.0657 0.0113  79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.6514 0.8364 0.5059 0.1351  -0.0802 0.0465  80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.6869 0.8412 0.4900 0.1231  -0.0724 0.0434  80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.6822 0.8354 0.5177 0.0982  -0.0514 0.0305  80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.7011 0.8275 0.5005 0.0900  -0.0366 0.0305  80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.7284 0.8974 0.4988 0.1318  -0.1027 0.0272  80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.8295 0.9664 0.5265 0.1286  -0.0951 0.0290  80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.9103 1.0595 0.5608 0.1424  -0.1256 0.0144  80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.9143 1.0917 0.5913 0.1345  -0.1414 -0.0172 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 0.9654 1.0928 0.5505 0.1620  -0.1350 0.0345  80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.6506 0.8319 0.5541 0.0869  -0.0487 0.0210  81  SER   A N   
254  C  CA  . SER   A 38  ? 0.6467 0.8194 0.5801 0.0652  -0.0309 0.0116  81  SER   A CA  
255  C  C   . SER   A 38  ? 0.6455 0.7994 0.5917 0.0621  -0.0016 0.0304  81  SER   A C   
256  O  O   . SER   A 38  ? 0.6475 0.7917 0.6187 0.0473  0.0126  0.0261  81  SER   A O   
257  C  CB  . SER   A 38  ? 0.6365 0.8439 0.6341 0.0501  -0.0441 -0.0087 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.6757 0.9024 0.6602 0.0549  -0.0757 -0.0308 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.6438 0.7889 0.5704 0.0777  0.0051  0.0498  82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.6379 0.7670 0.5712 0.0788  0.0290  0.0646  82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.6045 0.7623 0.5924 0.0769  0.0384  0.0685  82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.6065 0.7528 0.6031 0.0738  0.0592  0.0773  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.5648 0.7639 0.5900 0.0796  0.0235  0.0619  83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.5219 0.7592 0.6057 0.0755  0.0354  0.0654  83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.5132 0.7745 0.6007 0.1018  0.0328  0.0737  83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.5070 0.7836 0.5866 0.1182  0.0085  0.0678  83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.4894 0.7666 0.6295 0.0560  0.0218  0.0478  83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.5246 0.7746 0.6645 0.0315  0.0209  0.0350  83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.5363 0.7478 0.6573 0.0250  0.0408  0.0440  83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.5495 0.8166 0.7073 0.0217  -0.0022 0.0135  83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.5076 0.7695 0.6017 0.1095  0.0564  0.0865  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.5045 0.7896 0.6042 0.1373  0.0562  0.0911  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.4880 0.8431 0.6580 0.1353  0.0584  0.0848  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.4651 0.8437 0.6800 0.1085  0.0719  0.0837  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.5070 0.7671 0.5816 0.1493  0.0797  0.1033  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.5418 0.7418 0.5552 0.1561  0.0751  0.1070  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.5613 0.7392 0.5423 0.1777  0.0577  0.1070  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.5574 0.7230 0.5488 0.1405  0.0881  0.1105  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.5966 0.7202 0.5284 0.1783  0.0560  0.1111  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.5862 0.7065 0.5318 0.1445  0.0850  0.1117  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.5981 0.6983 0.5162 0.1606  0.0702  0.1123  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.4965 0.8851 0.6790 0.1631  0.0443  0.0801  85  SER   A N   
283  C  CA  . SER   A 42  ? 0.4859 0.9528 0.7413 0.1660  0.0462  0.0718  85  SER   A CA  
284  C  C   . SER   A 42  ? 0.5234 1.0119 0.7775 0.2050  0.0503  0.0736  85  SER   A C   
285  O  O   . SER   A 42  ? 0.5593 0.9958 0.7542 0.2296  0.0414  0.0782  85  SER   A O   
286  C  CB  . SER   A 42  ? 0.4797 0.9831 0.7666 0.1625  0.0117  0.0534  85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.5371 1.0038 0.7666 0.1879  -0.0198 0.0512  85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.5103 1.0754 0.8311 0.2106  0.0647  0.0686  86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.5377 1.1300 0.8603 0.2524  0.0683  0.0658  86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.5517 1.1848 0.8995 0.2826  0.0325  0.0492  86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.5123 1.2123 0.9260 0.2703  0.0202  0.0361  86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.5089 1.1626 0.8806 0.2494  0.1089  0.0707  86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.5705 1.1751 0.8945 0.2410  0.1421  0.0886  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.5406 1.2085 0.9094 0.2363  0.1840  0.0966  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.6307 1.1735 0.8815 0.2776  0.1324  0.0880  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.6072 1.1983 0.9034 0.3233  0.0136  0.0486  87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.6220 1.2392 0.9293 0.3619  -0.0233 0.0352  87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.6146 1.3005 0.9694 0.3987  -0.0104 0.0241  87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.6370 1.3011 0.9664 0.4124  0.0155  0.0294  87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6907 1.2120 0.9102 0.3855  -0.0509 0.0437  87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6943 1.2315 0.9155 0.4301  -0.0916 0.0332  87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.7299 1.1892 0.9011 0.3491  -0.0568 0.0548  87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.5797 1.3537 1.0053 0.4160  -0.0281 0.0061  88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.5621 1.4135 1.0398 0.4545  -0.0153 -0.0077 88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.5577 1.4443 1.0551 0.5060  -0.0596 -0.0269 88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.6133 1.4213 1.0416 0.5334  -0.0954 -0.0227 88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.5362 1.4918 1.1070 0.4224  0.0245  -0.0113 88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.6163 1.5381 1.1655 0.3793  0.0706  0.0099  88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.7000 1.6046 1.2111 0.4049  0.1048  0.0169  88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 0.6543 1.6357 1.2097 0.4378  0.1198  0.0043  88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.7800 1.5981 1.2177 0.3934  0.1157  0.0327  88  GLU   A OE2 
312  N  N   . GLY   B 7   ? 0.9460 0.9316 0.9224 0.2708  0.1283  -0.0378 16  GLY   B N   
313  C  CA  . GLY   B 7   ? 0.9504 0.9378 0.9276 0.2956  0.1252  -0.0337 16  GLY   B CA  
314  C  C   . GLY   B 7   ? 0.9438 0.9476 0.9292 0.2955  0.1092  -0.0302 16  GLY   B C   
315  O  O   . GLY   B 7   ? 0.9311 0.9713 0.9355 0.2957  0.0998  -0.0340 16  GLY   B O   
316  N  N   . GLU   B 8   ? 0.9457 0.9236 0.9171 0.2955  0.1055  -0.0232 17  GLU   B N   
317  C  CA  . GLU   B 8   ? 0.9343 0.9232 0.9075 0.2986  0.0902  -0.0208 17  GLU   B CA  
318  C  C   . GLU   B 8   ? 0.9122 0.9121 0.8941 0.2735  0.0793  -0.0245 17  GLU   B C   
319  O  O   . GLU   B 8   ? 0.9216 0.9016 0.8945 0.2566  0.0812  -0.0218 17  GLU   B O   
320  C  CB  . GLU   B 8   ? 0.9777 0.9387 0.9323 0.3111  0.0921  -0.0104 17  GLU   B CB  
321  C  CG  . GLU   B 8   ? 1.0381 1.0139 0.9902 0.3299  0.0785  -0.0086 17  GLU   B CG  
322  C  CD  . GLU   B 8   ? 1.1451 1.0984 1.0776 0.3482  0.0828  0.0039  17  GLU   B CD  
323  O  OE1 . GLU   B 8   ? 1.1662 1.0908 1.0903 0.3436  0.0967  0.0126  17  GLU   B OE1 
324  O  OE2 . GLU   B 8   ? 1.1808 1.1462 1.1069 0.3676  0.0721  0.0052  17  GLU   B OE2 
325  N  N   . THR   B 9   ? 0.8791 0.9113 0.8798 0.2710  0.0676  -0.0306 18  THR   B N   
326  C  CA  . THR   B 9   ? 0.8582 0.9018 0.8705 0.2477  0.0565  -0.0339 18  THR   B CA  
327  C  C   . THR   B 9   ? 0.8310 0.8748 0.8409 0.2513  0.0374  -0.0356 18  THR   B C   
328  O  O   . THR   B 9   ? 0.8325 0.8784 0.8492 0.2327  0.0270  -0.0381 18  THR   B O   
329  C  CB  . THR   B 9   ? 0.8649 0.9456 0.9043 0.2397  0.0563  -0.0393 18  THR   B CB  
330  O  OG1 . THR   B 9   ? 0.8681 0.9763 0.9217 0.2581  0.0461  -0.0436 18  THR   B OG1 
331  C  CG2 . THR   B 9   ? 0.8710 0.9546 0.9109 0.2394  0.0753  -0.0389 18  THR   B CG2 
332  N  N   . THR   B 10  ? 0.8061 0.8475 0.8052 0.2766  0.0326  -0.0344 19  THR   B N   
333  C  CA  . THR   B 10  ? 0.7869 0.8300 0.7795 0.2871  0.0141  -0.0377 19  THR   B CA  
334  C  C   . THR   B 10  ? 0.7702 0.7893 0.7480 0.2749  0.0084  -0.0351 19  THR   B C   
335  O  O   . THR   B 10  ? 0.7821 0.7783 0.7447 0.2730  0.0206  -0.0265 19  THR   B O   
336  C  CB  . THR   B 10  ? 0.8169 0.8560 0.7924 0.3198  0.0156  -0.0331 19  THR   B CB  
337  O  OG1 . THR   B 10  ? 0.8358 0.8904 0.8202 0.3340  0.0251  -0.0328 19  THR   B OG1 
338  C  CG2 . THR   B 10  ? 0.8171 0.8664 0.7863 0.3361  -0.0055 -0.0396 19  THR   B CG2 
339  N  N   . ASP   B 11  ? 0.7387 0.7624 0.7203 0.2686  -0.0110 -0.0429 20  ASP   B N   
340  C  CA  . ASP   B 11  ? 0.7359 0.7360 0.7005 0.2621  -0.0177 -0.0410 20  ASP   B CA  
341  C  C   . ASP   B 11  ? 0.7269 0.7120 0.6651 0.2879  -0.0146 -0.0338 20  ASP   B C   
342  O  O   . ASP   B 11  ? 0.7262 0.7212 0.6594 0.3121  -0.0159 -0.0340 20  ASP   B O   
343  C  CB  . ASP   B 11  ? 0.7604 0.7649 0.7319 0.2555  -0.0412 -0.0523 20  ASP   B CB  
344  C  CG  . ASP   B 11  ? 0.8069 0.8172 0.8012 0.2250  -0.0441 -0.0553 20  ASP   B CG  
345  O  OD1 . ASP   B 11  ? 0.7957 0.8222 0.8081 0.2133  -0.0310 -0.0523 20  ASP   B OD1 
346  O  OD2 . ASP   B 11  ? 0.8466 0.8442 0.8396 0.2139  -0.0594 -0.0603 20  ASP   B OD2 
347  N  N   . GLY   B 12  ? 0.7172 0.6812 0.6393 0.2838  -0.0098 -0.0263 21  GLY   B N   
348  C  CA  . GLY   B 12  ? 0.7110 0.6641 0.6106 0.3070  -0.0048 -0.0170 21  GLY   B CA  
349  C  C   . GLY   B 12  ? 0.6992 0.6359 0.5915 0.2980  0.0107  -0.0044 21  GLY   B C   
350  O  O   . GLY   B 12  ? 0.6937 0.6255 0.5952 0.2741  0.0151  -0.0045 21  GLY   B O   
351  N  N   . VAL   B 13  ? 0.6936 0.6238 0.5696 0.3176  0.0183  0.0071  22  VAL   B N   
352  C  CA  . VAL   B 13  ? 0.6879 0.6066 0.5604 0.3101  0.0326  0.0203  22  VAL   B CA  
353  C  C   . VAL   B 13  ? 0.6840 0.5981 0.5638 0.3101  0.0512  0.0296  22  VAL   B C   
354  O  O   . VAL   B 13  ? 0.6910 0.6090 0.5687 0.3286  0.0542  0.0310  22  VAL   B O   
355  C  CB  . VAL   B 13  ? 0.6980 0.6141 0.5509 0.3289  0.0301  0.0285  22  VAL   B CB  
356  C  CG1 . VAL   B 13  ? 0.7080 0.6288 0.5467 0.3605  0.0341  0.0363  22  VAL   B CG1 
357  C  CG2 . VAL   B 13  ? 0.6982 0.6082 0.5527 0.3166  0.0418  0.0408  22  VAL   B CG2 
358  N  N   . TYR   B 14  ? 0.6647 0.5697 0.5538 0.2883  0.0620  0.0335  23  TYR   B N   
359  C  CA  . TYR   B 14  ? 0.6548 0.5496 0.5508 0.2853  0.0781  0.0398  23  TYR   B CA  
360  C  C   . TYR   B 14  ? 0.6551 0.5387 0.5525 0.2765  0.0898  0.0529  23  TYR   B C   
361  O  O   . TYR   B 14  ? 0.6570 0.5435 0.5540 0.2655  0.0856  0.0543  23  TYR   B O   
362  C  CB  . TYR   B 14  ? 0.6397 0.5342 0.5482 0.2656  0.0794  0.0282  23  TYR   B CB  
363  C  CG  . TYR   B 14  ? 0.6273 0.5362 0.5411 0.2739  0.0724  0.0176  23  TYR   B CG  
364  C  CD1 . TYR   B 14  ? 0.6299 0.5540 0.5453 0.2740  0.0563  0.0088  23  TYR   B CD1 
365  C  CD2 . TYR   B 14  ? 0.6417 0.5494 0.5607 0.2805  0.0815  0.0159  23  TYR   B CD2 
366  C  CE1 . TYR   B 14  ? 0.6285 0.5703 0.5535 0.2801  0.0489  -0.0007 23  TYR   B CE1 
367  C  CE2 . TYR   B 14  ? 0.6440 0.5708 0.5709 0.2892  0.0751  0.0068  23  TYR   B CE2 
368  C  CZ  . TYR   B 14  ? 0.6417 0.5877 0.5733 0.2881  0.0586  -0.0013 23  TYR   B CZ  
369  O  OH  . TYR   B 14  ? 0.6477 0.6169 0.5920 0.2943  0.0512  -0.0102 23  TYR   B OH  
370  N  N   . ARG   B 15  ? 0.6542 0.5249 0.5544 0.2809  0.1041  0.0626  24  ARG   B N   
371  C  CA  . ARG   B 15  ? 0.6601 0.5196 0.5673 0.2685  0.1154  0.0747  24  ARG   B CA  
372  C  C   . ARG   B 15  ? 0.6623 0.5098 0.5800 0.2438  0.1179  0.0643  24  ARG   B C   
373  O  O   . ARG   B 15  ? 0.6640 0.5070 0.5818 0.2445  0.1179  0.0538  24  ARG   B O   
374  C  CB  . ARG   B 15  ? 0.6830 0.5304 0.5885 0.2852  0.1302  0.0918  24  ARG   B CB  
375  C  CG  . ARG   B 15  ? 0.7121 0.5714 0.6030 0.3144  0.1293  0.1027  24  ARG   B CG  
376  C  CD  . ARG   B 15  ? 0.7557 0.6022 0.6445 0.3302  0.1463  0.1230  24  ARG   B CD  
377  N  NE  . ARG   B 15  ? 0.8035 0.6622 0.6733 0.3631  0.1444  0.1308  24  ARG   B NE  
378  C  CZ  . ARG   B 15  ? 0.8332 0.7038 0.6940 0.3773  0.1478  0.1455  24  ARG   B CZ  
379  N  NH1 . ARG   B 15  ? 0.8165 0.6903 0.6895 0.3608  0.1545  0.1561  24  ARG   B NH1 
380  N  NH2 . ARG   B 15  ? 0.8447 0.7261 0.6842 0.4098  0.1445  0.1499  24  ARG   B NH2 
381  N  N   . VAL   B 16  ? 0.6588 0.5032 0.5846 0.2235  0.1195  0.0668  25  VAL   B N   
382  C  CA  . VAL   B 16  ? 0.6583 0.4908 0.5914 0.2005  0.1207  0.0564  25  VAL   B CA  
383  C  C   . VAL   B 16  ? 0.6709 0.4848 0.6139 0.1941  0.1326  0.0677  25  VAL   B C   
384  O  O   . VAL   B 16  ? 0.6613 0.4821 0.6125 0.1893  0.1348  0.0803  25  VAL   B O   
385  C  CB  . VAL   B 16  ? 0.6522 0.4976 0.5863 0.1818  0.1103  0.0489  25  VAL   B CB  
386  C  CG1 . VAL   B 16  ? 0.6547 0.4895 0.5915 0.1613  0.1102  0.0360  25  VAL   B CG1 
387  C  CG2 . VAL   B 16  ? 0.6486 0.5102 0.5738 0.1894  0.0989  0.0425  25  VAL   B CG2 
388  N  N   . MET   B 17  ? 0.6933 0.4840 0.6362 0.1964  0.1406  0.0647  26  MET   B N   
389  C  CA  . MET   B 17  ? 0.7245 0.4899 0.6765 0.1914  0.1524  0.0752  26  MET   B CA  
390  C  C   . MET   B 17  ? 0.7656 0.5088 0.7228 0.1690  0.1517  0.0611  26  MET   B C   
391  O  O   . MET   B 17  ? 0.7691 0.5143 0.7184 0.1641  0.1451  0.0433  26  MET   B O   
392  C  CB  . MET   B 17  ? 0.7346 0.4831 0.6785 0.2156  0.1626  0.0831  26  MET   B CB  
393  C  CG  . MET   B 17  ? 0.7351 0.5048 0.6682 0.2425  0.1607  0.0913  26  MET   B CG  
394  S  SD  . MET   B 17  ? 0.7572 0.5408 0.6939 0.2507  0.1667  0.1160  26  MET   B SD  
395  C  CE  . MET   B 17  ? 0.6527 0.4019 0.5980 0.2506  0.1858  0.1351  26  MET   B CE  
396  N  N   . THR   B 18  ? 0.7967 0.5178 0.7667 0.1563  0.1588  0.0693  27  THR   B N   
397  C  CA  . THR   B 18  ? 0.8439 0.5377 0.8178 0.1361  0.1573  0.0551  27  THR   B CA  
398  C  C   . THR   B 18  ? 0.8877 0.5430 0.8692 0.1366  0.1697  0.0660  27  THR   B C   
399  O  O   . THR   B 18  ? 0.8810 0.5373 0.8728 0.1424  0.1791  0.0886  27  THR   B O   
400  C  CB  . THR   B 18  ? 0.8629 0.5719 0.8485 0.1098  0.1468  0.0483  27  THR   B CB  
401  O  OG1 . THR   B 18  ? 0.8948 0.5810 0.8760 0.0944  0.1415  0.0277  27  THR   B OG1 
402  C  CG2 . THR   B 18  ? 0.8567 0.5707 0.8658 0.0972  0.1510  0.0672  27  THR   B CG2 
403  N  N   . ARG   B 19  ? 0.9295 0.5495 0.9040 0.1324  0.1706  0.0510  28  ARG   B N   
404  C  CA  . ARG   B 19  ? 0.9759 0.5518 0.9565 0.1314  0.1815  0.0600  28  ARG   B CA  
405  C  C   . ARG   B 19  ? 0.9996 0.5507 0.9962 0.1000  0.1762  0.0512  28  ARG   B C   
406  O  O   . ARG   B 19  ? 1.0174 0.5250 1.0193 0.0948  0.1831  0.0545  28  ARG   B O   
407  C  CB  . ARG   B 19  ? 1.0216 0.5685 0.9818 0.1548  0.1881  0.0524  28  ARG   B CB  
408  C  CG  . ARG   B 19  ? 1.0798 0.6471 1.0298 0.1860  0.1947  0.0665  28  ARG   B CG  
409  C  CD  . ARG   B 19  ? 1.1653 0.6966 1.1028 0.2096  0.2062  0.0715  28  ARG   B CD  
410  N  NE  . ARG   B 19  ? 1.2194 0.7748 1.1448 0.2412  0.2092  0.0801  28  ARG   B NE  
411  C  CZ  . ARG   B 19  ? 1.2531 0.8293 1.1663 0.2568  0.2035  0.0648  28  ARG   B CZ  
412  N  NH1 . ARG   B 19  ? 1.2501 0.8264 1.1595 0.2451  0.1963  0.0418  28  ARG   B NH1 
413  N  NH2 . ARG   B 19  ? 1.2435 0.8428 1.1487 0.2843  0.2046  0.0728  28  ARG   B NH2 
414  N  N   . ARG   B 20  ? 1.0013 0.5799 1.0059 0.0794  0.1631  0.0404  29  ARG   B N   
415  C  CA  . ARG   B 20  ? 1.0194 0.5849 1.0392 0.0490  0.1535  0.0286  29  ARG   B CA  
416  C  C   . ARG   B 20  ? 1.0087 0.5701 1.0605 0.0311  0.1593  0.0504  29  ARG   B C   
417  O  O   . ARG   B 20  ? 1.0218 0.5456 1.0865 0.0124  0.1588  0.0462  29  ARG   B O   
418  C  CB  . ARG   B 20  ? 1.0432 0.6464 1.0595 0.0373  0.1379  0.0129  29  ARG   B CB  
419  C  CG  . ARG   B 20  ? 1.1104 0.7029 1.1384 0.0082  0.1249  -0.0037 29  ARG   B CG  
420  C  CD  . ARG   B 20  ? 1.1630 0.7947 1.1858 -0.0005 0.1100  -0.0163 29  ARG   B CD  
421  N  NE  . ARG   B 20  ? 1.1987 0.8708 1.2456 -0.0105 0.1071  0.0010  29  ARG   B NE  
422  C  CZ  . ARG   B 20  ? 1.2282 0.9078 1.3019 -0.0355 0.0993  0.0022  29  ARG   B CZ  
423  N  NH1 . ARG   B 20  ? 1.2347 0.8805 1.3151 -0.0551 0.0924  -0.0137 29  ARG   B NH1 
424  N  NH2 . ARG   B 20  ? 1.2089 0.9303 1.3037 -0.0407 0.0978  0.0189  29  ARG   B NH2 
425  N  N   . LEU   B 21  ? 0.9809 0.5796 1.0456 0.0376  0.1654  0.0741  30  LEU   B N   
426  C  CA  . LEU   B 21  ? 0.9669 0.5698 1.0639 0.0231  0.1738  0.0990  30  LEU   B CA  
427  C  C   . LEU   B 21  ? 0.9749 0.5396 1.0727 0.0367  0.1927  0.1205  30  LEU   B C   
428  O  O   . LEU   B 21  ? 1.0008 0.5254 1.0777 0.0493  0.1957  0.1098  30  LEU   B O   
429  C  CB  . LEU   B 21  ? 0.9486 0.6077 1.0553 0.0287  0.1737  0.1157  30  LEU   B CB  
430  C  CG  . LEU   B 21  ? 0.9598 0.6553 1.0609 0.0209  0.1563  0.0971  30  LEU   B CG  
431  C  CD1 . LEU   B 21  ? 0.9487 0.6937 1.0565 0.0310  0.1576  0.1149  30  LEU   B CD1 
432  C  CD2 . LEU   B 21  ? 0.9650 0.6552 1.0850 -0.0114 0.1428  0.0809  30  LEU   B CD2 
433  N  N   . LEU   B 22  ? 0.9492 0.5256 1.0704 0.0350  0.2061  0.1514  31  LEU   B N   
434  C  CA  . LEU   B 22  ? 0.9534 0.4954 1.0739 0.0495  0.2254  0.1752  31  LEU   B CA  
435  C  C   . LEU   B 22  ? 0.9483 0.5030 1.0369 0.0893  0.2323  0.1816  31  LEU   B C   
436  O  O   . LEU   B 22  ? 0.9428 0.5443 1.0251 0.1019  0.2284  0.1843  31  LEU   B O   
437  C  CB  . LEU   B 22  ? 0.9372 0.4964 1.0920 0.0371  0.2385  0.2083  31  LEU   B CB  
438  C  CG  . LEU   B 22  ? 0.9655 0.4869 1.1231 0.0478  0.2596  0.2362  31  LEU   B CG  
439  C  CD1 . LEU   B 22  ? 0.9798 0.4482 1.1607 0.0168  0.2600  0.2332  31  LEU   B CD1 
440  C  CD2 . LEU   B 22  ? 0.9575 0.5174 1.1309 0.0581  0.2763  0.2732  31  LEU   B CD2 
441  N  N   . GLY   B 23  ? 0.9441 0.4575 1.0123 0.1091  0.2407  0.1817  32  GLY   B N   
442  C  CA  . GLY   B 23  ? 0.9344 0.4580 0.9729 0.1472  0.2455  0.1854  32  GLY   B CA  
443  C  C   . GLY   B 23  ? 0.9035 0.4643 0.9244 0.1563  0.2300  0.1621  32  GLY   B C   
444  O  O   . GLY   B 23  ? 0.9004 0.4595 0.9205 0.1389  0.2165  0.1363  32  GLY   B O   
445  N  N   . SER   B 24  ? 0.8810 0.4760 0.8877 0.1827  0.2313  0.1714  33  SER   B N   
446  C  CA  . SER   B 24  ? 0.8636 0.4948 0.8568 0.1896  0.2165  0.1520  33  SER   B CA  
447  C  C   . SER   B 24  ? 0.8224 0.4966 0.8274 0.1829  0.2125  0.1622  33  SER   B C   
448  O  O   . SER   B 24  ? 0.8072 0.4933 0.8179 0.1935  0.2236  0.1873  33  SER   B O   
449  C  CB  . SER   B 24  ? 0.8917 0.5296 0.8600 0.2240  0.2174  0.1507  33  SER   B CB  
450  O  OG  . SER   B 24  ? 0.9443 0.5447 0.9016 0.2338  0.2223  0.1434  33  SER   B OG  
451  N  N   . THR   B 25  ? 0.8054 0.5025 0.8131 0.1668  0.1977  0.1438  34  THR   B N   
452  C  CA  . THR   B 25  ? 0.7812 0.5178 0.7987 0.1612  0.1926  0.1513  34  THR   B CA  
453  C  C   . THR   B 25  ? 0.7630 0.5273 0.7621 0.1728  0.1789  0.1359  34  THR   B C   
454  O  O   . THR   B 25  ? 0.7689 0.5276 0.7597 0.1653  0.1688  0.1139  34  THR   B O   
455  C  CB  . THR   B 25  ? 0.7911 0.5291 0.8336 0.1273  0.1871  0.1464  34  THR   B CB  
456  O  OG1 . THR   B 25  ? 0.8077 0.5245 0.8723 0.1155  0.2001  0.1648  34  THR   B OG1 
457  C  CG2 . THR   B 25  ? 0.7779 0.5589 0.8288 0.1212  0.1786  0.1487  34  THR   B CG2 
458  N  N   . GLN   B 26  ? 0.7388 0.5322 0.7313 0.1909  0.1786  0.1477  35  GLN   B N   
459  C  CA  . GLN   B 26  ? 0.7227 0.5393 0.6996 0.1998  0.1646  0.1338  35  GLN   B CA  
460  C  C   . GLN   B 26  ? 0.7143 0.5519 0.7021 0.1794  0.1548  0.1284  35  GLN   B C   
461  O  O   . GLN   B 26  ? 0.7092 0.5664 0.7089 0.1781  0.1586  0.1439  35  GLN   B O   
462  C  CB  . GLN   B 26  ? 0.7163 0.5504 0.6771 0.2304  0.1662  0.1453  35  GLN   B CB  
463  C  CG  . GLN   B 26  ? 0.7126 0.5661 0.6586 0.2377  0.1503  0.1303  35  GLN   B CG  
464  C  CD  . GLN   B 26  ? 0.7208 0.5870 0.6486 0.2688  0.1496  0.1381  35  GLN   B CD  
465  O  OE1 . GLN   B 26  ? 0.7316 0.5884 0.6508 0.2884  0.1575  0.1459  35  GLN   B OE1 
466  N  NE2 . GLN   B 26  ? 0.7174 0.6041 0.6369 0.2755  0.1397  0.1358  35  GLN   B NE2 
467  N  N   . VAL   B 27  ? 0.7033 0.5386 0.6867 0.1651  0.1430  0.1073  36  VAL   B N   
468  C  CA  . VAL   B 27  ? 0.6848 0.5374 0.6750 0.1462  0.1322  0.0996  36  VAL   B CA  
469  C  C   . VAL   B 27  ? 0.6696 0.5451 0.6450 0.1581  0.1213  0.0958  36  VAL   B C   
470  O  O   . VAL   B 27  ? 0.6596 0.5543 0.6394 0.1502  0.1143  0.0966  36  VAL   B O   
471  C  CB  . VAL   B 27  ? 0.6965 0.5316 0.6878 0.1246  0.1263  0.0799  36  VAL   B CB  
472  C  CG1 . VAL   B 27  ? 0.7078 0.5154 0.7126 0.1132  0.1357  0.0826  36  VAL   B CG1 
473  C  CG2 . VAL   B 27  ? 0.7033 0.5307 0.6753 0.1329  0.1214  0.0636  36  VAL   B CG2 
474  N  N   . GLY   B 28  ? 0.6637 0.5366 0.6223 0.1776  0.1194  0.0919  37  GLY   B N   
475  C  CA  . GLY   B 28  ? 0.6585 0.5464 0.6026 0.1890  0.1081  0.0870  37  GLY   B CA  
476  C  C   . GLY   B 28  ? 0.6598 0.5427 0.5893 0.2088  0.1057  0.0816  37  GLY   B C   
477  O  O   . GLY   B 28  ? 0.6577 0.5286 0.5871 0.2180  0.1140  0.0844  37  GLY   B O   
478  N  N   . VAL   B 29  ? 0.6512 0.5430 0.5688 0.2154  0.0933  0.0736  38  VAL   B N   
479  C  CA  . VAL   B 29  ? 0.6396 0.5313 0.5450 0.2326  0.0864  0.0664  38  VAL   B CA  
480  C  C   . VAL   B 29  ? 0.6270 0.5199 0.5297 0.2198  0.0737  0.0509  38  VAL   B C   
481  O  O   . VAL   B 29  ? 0.6228 0.5179 0.5269 0.2042  0.0694  0.0487  38  VAL   B O   
482  C  CB  . VAL   B 29  ? 0.6362 0.5377 0.5288 0.2576  0.0835  0.0758  38  VAL   B CB  
483  C  CG1 . VAL   B 29  ? 0.6435 0.5464 0.5224 0.2751  0.0716  0.0656  38  VAL   B CG1 
484  C  CG2 . VAL   B 29  ? 0.6304 0.5326 0.5256 0.2714  0.0985  0.0939  38  VAL   B CG2 
485  N  N   . GLY   B 30  ? 0.6175 0.5103 0.5172 0.2266  0.0680  0.0415  39  GLY   B N   
486  C  CA  . GLY   B 30  ? 0.6137 0.5090 0.5132 0.2150  0.0569  0.0294  39  GLY   B CA  
487  C  C   . GLY   B 30  ? 0.6107 0.5112 0.5064 0.2289  0.0461  0.0221  39  GLY   B C   
488  O  O   . GLY   B 30  ? 0.6138 0.5167 0.5050 0.2495  0.0471  0.0251  39  GLY   B O   
489  N  N   . VAL   B 31  ? 0.6075 0.5101 0.5058 0.2173  0.0355  0.0128  40  VAL   B N   
490  C  CA  . VAL   B 31  ? 0.6143 0.5226 0.5134 0.2251  0.0222  0.0038  40  VAL   B CA  
491  C  C   . VAL   B 31  ? 0.6169 0.5342 0.5320 0.2108  0.0234  -0.0039 40  VAL   B C   
492  O  O   . VAL   B 31  ? 0.6240 0.5399 0.5439 0.1910  0.0258  -0.0047 40  VAL   B O   
493  C  CB  . VAL   B 31  ? 0.6280 0.5292 0.5179 0.2225  0.0071  0.0006  40  VAL   B CB  
494  C  CG1 . VAL   B 31  ? 0.6328 0.5373 0.5270 0.2249  -0.0088 -0.0107 40  VAL   B CG1 
495  C  CG2 . VAL   B 31  ? 0.6393 0.5346 0.5119 0.2399  0.0058  0.0080  40  VAL   B CG2 
496  N  N   . MET   B 32  ? 0.6171 0.5460 0.5400 0.2220  0.0216  -0.0089 41  MET   B N   
497  C  CA  . MET   B 32  ? 0.6155 0.5593 0.5564 0.2105  0.0219  -0.0159 41  MET   B CA  
498  C  C   . MET   B 32  ? 0.6180 0.5689 0.5657 0.2075  0.0034  -0.0240 41  MET   B C   
499  O  O   . MET   B 32  ? 0.6253 0.5753 0.5650 0.2247  -0.0087 -0.0274 41  MET   B O   
500  C  CB  . MET   B 32  ? 0.6193 0.5741 0.5667 0.2257  0.0303  -0.0167 41  MET   B CB  
501  C  CG  . MET   B 32  ? 0.6349 0.6090 0.6017 0.2159  0.0337  -0.0226 41  MET   B CG  
502  S  SD  . MET   B 32  ? 0.6876 0.6551 0.6551 0.1964  0.0508  -0.0203 41  MET   B SD  
503  C  CE  . MET   B 32  ? 0.6481 0.6020 0.6061 0.2141  0.0656  -0.0162 41  MET   B CE  
504  N  N   . GLN   B 33  ? 0.6162 0.5720 0.5770 0.1858  0.0006  -0.0266 42  GLN   B N   
505  C  CA  . GLN   B 33  ? 0.6187 0.5781 0.5896 0.1786  -0.0173 -0.0339 42  GLN   B CA  
506  C  C   . GLN   B 33  ? 0.6056 0.5788 0.5983 0.1549  -0.0132 -0.0337 42  GLN   B C   
507  O  O   . GLN   B 33  ? 0.6181 0.5845 0.6062 0.1413  -0.0017 -0.0271 42  GLN   B O   
508  C  CB  . GLN   B 33  ? 0.6599 0.5948 0.6127 0.1776  -0.0289 -0.0331 42  GLN   B CB  
509  C  CG  . GLN   B 33  ? 0.7264 0.6584 0.6888 0.1689  -0.0488 -0.0417 42  GLN   B CG  
510  C  CD  . GLN   B 33  ? 0.8181 0.7235 0.7581 0.1772  -0.0630 -0.0440 42  GLN   B CD  
511  O  OE1 . GLN   B 33  ? 0.8490 0.7369 0.7881 0.1620  -0.0711 -0.0439 42  GLN   B OE1 
512  N  NE2 . GLN   B 33  ? 0.8374 0.7386 0.7575 0.2032  -0.0657 -0.0452 42  GLN   B NE2 
513  N  N   . GLU   B 34  ? 0.5816 0.5769 0.5985 0.1504  -0.0220 -0.0402 43  GLU   B N   
514  C  CA  . GLU   B 34  ? 0.5678 0.5812 0.6090 0.1275  -0.0166 -0.0377 43  GLU   B CA  
515  C  C   . GLU   B 34  ? 0.5637 0.5891 0.6059 0.1249  0.0062  -0.0315 43  GLU   B C   
516  O  O   . GLU   B 34  ? 0.5667 0.5959 0.6147 0.1068  0.0154  -0.0255 43  GLU   B O   
517  C  CB  . GLU   B 34  ? 0.6054 0.5990 0.6450 0.1063  -0.0242 -0.0339 43  GLU   B CB  
518  C  CG  . GLU   B 34  ? 0.6726 0.6546 0.7159 0.1058  -0.0481 -0.0424 43  GLU   B CG  
519  C  CD  . GLU   B 34  ? 0.7622 0.7136 0.7959 0.0899  -0.0566 -0.0386 43  GLU   B CD  
520  O  OE1 . GLU   B 34  ? 0.7815 0.7352 0.8277 0.0675  -0.0487 -0.0300 43  GLU   B OE1 
521  O  OE2 . GLU   B 34  ? 0.7971 0.7219 0.8093 0.1015  -0.0704 -0.0436 43  GLU   B OE2 
522  N  N   . GLY   B 35  ? 0.5583 0.5876 0.5929 0.1444  0.0149  -0.0329 44  GLY   B N   
523  C  CA  . GLY   B 35  ? 0.5517 0.5877 0.5842 0.1457  0.0346  -0.0298 44  GLY   B CA  
524  C  C   . GLY   B 35  ? 0.5623 0.5735 0.5722 0.1389  0.0448  -0.0244 44  GLY   B C   
525  O  O   . GLY   B 35  ? 0.5680 0.5817 0.5740 0.1377  0.0596  -0.0235 44  GLY   B O   
526  N  N   . VAL   B 36  ? 0.5606 0.5485 0.5547 0.1359  0.0360  -0.0217 45  VAL   B N   
527  C  CA  . VAL   B 36  ? 0.5609 0.5283 0.5353 0.1293  0.0425  -0.0167 45  VAL   B CA  
528  C  C   . VAL   B 36  ? 0.5648 0.5145 0.5231 0.1446  0.0409  -0.0152 45  VAL   B C   
529  O  O   . VAL   B 36  ? 0.5718 0.5164 0.5266 0.1546  0.0293  -0.0158 45  VAL   B O   
530  C  CB  . VAL   B 36  ? 0.5668 0.5250 0.5377 0.1119  0.0352  -0.0124 45  VAL   B CB  
531  C  CG1 . VAL   B 36  ? 0.5836 0.5225 0.5331 0.1082  0.0386  -0.0074 45  VAL   B CG1 
532  C  CG2 . VAL   B 36  ? 0.5579 0.5338 0.5448 0.0954  0.0405  -0.0103 45  VAL   B CG2 
533  N  N   . PHE   B 37  ? 0.5537 0.4942 0.5022 0.1465  0.0527  -0.0131 46  PHE   B N   
534  C  CA  . PHE   B 37  ? 0.5489 0.4746 0.4856 0.1578  0.0533  -0.0089 46  PHE   B CA  
535  C  C   . PHE   B 37  ? 0.5465 0.4604 0.4715 0.1476  0.0498  -0.0041 46  PHE   B C   
536  O  O   . PHE   B 37  ? 0.5470 0.4593 0.4687 0.1339  0.0549  -0.0042 46  PHE   B O   
537  C  CB  . PHE   B 37  ? 0.5389 0.4587 0.4744 0.1641  0.0668  -0.0089 46  PHE   B CB  
538  C  CG  . PHE   B 37  ? 0.5459 0.4528 0.4739 0.1761  0.0685  -0.0020 46  PHE   B CG  
539  C  CD1 . PHE   B 37  ? 0.5495 0.4590 0.4764 0.1950  0.0637  0.0011  46  PHE   B CD1 
540  C  CD2 . PHE   B 37  ? 0.5540 0.4482 0.4767 0.1684  0.0747  0.0019  46  PHE   B CD2 
541  C  CE1 . PHE   B 37  ? 0.5566 0.4565 0.4765 0.2069  0.0675  0.0102  46  PHE   B CE1 
542  C  CE2 . PHE   B 37  ? 0.5553 0.4411 0.4752 0.1777  0.0775  0.0108  46  PHE   B CE2 
543  C  CZ  . PHE   B 37  ? 0.5489 0.4377 0.4670 0.1973  0.0752  0.0159  46  PHE   B CZ  
544  N  N   . HIS   B 38  ? 0.5508 0.4583 0.4683 0.1563  0.0408  -0.0001 47  HIS   B N   
545  C  CA  . HIS   B 38  ? 0.5532 0.4524 0.4598 0.1508  0.0364  0.0051  47  HIS   B CA  
546  C  C   . HIS   B 38  ? 0.5645 0.4599 0.4660 0.1608  0.0411  0.0119  47  HIS   B C   
547  O  O   . HIS   B 38  ? 0.5671 0.4626 0.4659 0.1778  0.0388  0.0147  47  HIS   B O   
548  C  CB  . HIS   B 38  ? 0.5527 0.4471 0.4536 0.1558  0.0219  0.0045  47  HIS   B CB  
549  C  CG  . HIS   B 38  ? 0.5523 0.4503 0.4624 0.1464  0.0151  -0.0013 47  HIS   B CG  
550  N  ND1 . HIS   B 38  ? 0.5552 0.4650 0.4787 0.1519  0.0142  -0.0072 47  HIS   B ND1 
551  C  CD2 . HIS   B 38  ? 0.5575 0.4498 0.4670 0.1322  0.0091  -0.0006 47  HIS   B CD2 
552  C  CE1 . HIS   B 38  ? 0.5531 0.4665 0.4867 0.1388  0.0076  -0.0103 47  HIS   B CE1 
553  N  NE2 . HIS   B 38  ? 0.5597 0.4609 0.4848 0.1263  0.0049  -0.0058 47  HIS   B NE2 
554  N  N   . THR   B 39  ? 0.5712 0.4648 0.4709 0.1504  0.0464  0.0153  48  THR   B N   
555  C  CA  . THR   B 39  ? 0.5717 0.4651 0.4713 0.1568  0.0507  0.0236  48  THR   B CA  
556  C  C   . THR   B 39  ? 0.5775 0.4738 0.4727 0.1465  0.0470  0.0274  48  THR   B C   
557  O  O   . THR   B 39  ? 0.5750 0.4702 0.4633 0.1383  0.0403  0.0245  48  THR   B O   
558  C  CB  . THR   B 39  ? 0.5747 0.4644 0.4830 0.1571  0.0628  0.0241  48  THR   B CB  
559  O  OG1 . THR   B 39  ? 0.5699 0.4607 0.4813 0.1636  0.0674  0.0348  48  THR   B OG1 
560  C  CG2 . THR   B 39  ? 0.5843 0.4700 0.4951 0.1392  0.0678  0.0172  48  THR   B CG2 
561  N  N   . MET   B 40  ? 0.5815 0.4829 0.4815 0.1480  0.0512  0.0353  49  MET   B N   
562  C  CA  . MET   B 40  ? 0.5891 0.4984 0.4883 0.1393  0.0476  0.0390  49  MET   B CA  
563  C  C   . MET   B 40  ? 0.5913 0.4994 0.4969 0.1212  0.0520  0.0330  49  MET   B C   
564  O  O   . MET   B 40  ? 0.5855 0.4874 0.5001 0.1188  0.0602  0.0313  49  MET   B O   
565  C  CB  . MET   B 40  ? 0.5930 0.5139 0.4989 0.1496  0.0505  0.0512  49  MET   B CB  
566  C  CG  . MET   B 40  ? 0.6326 0.5537 0.5309 0.1720  0.0491  0.0568  49  MET   B CG  
567  S  SD  . MET   B 40  ? 0.7282 0.6586 0.6140 0.1852  0.0395  0.0631  49  MET   B SD  
568  C  CE  . MET   B 40  ? 0.7735 0.6883 0.6445 0.1798  0.0277  0.0523  49  MET   B CE  
569  N  N   . TRP   B 41  ? 0.5991 0.5116 0.4981 0.1098  0.0459  0.0297  50  TRP   B N   
570  C  CA  A TRP   B 41  ? 0.6044 0.5160 0.5051 0.0938  0.0475  0.0218  50  TRP   B CA  
571  C  CA  B TRP   B 41  ? 0.5993 0.5110 0.4999 0.0938  0.0474  0.0218  50  TRP   B CA  
572  C  C   . TRP   B 41  ? 0.5990 0.5138 0.5159 0.0878  0.0517  0.0240  50  TRP   B C   
573  O  O   . TRP   B 41  ? 0.6016 0.5059 0.5225 0.0788  0.0564  0.0159  50  TRP   B O   
574  C  CB  A TRP   B 41  ? 0.6065 0.5253 0.4949 0.0859  0.0391  0.0199  50  TRP   B CB  
575  C  CB  B TRP   B 41  ? 0.5940 0.5131 0.4824 0.0863  0.0389  0.0203  50  TRP   B CB  
576  C  CG  A TRP   B 41  ? 0.6161 0.5324 0.4998 0.0721  0.0398  0.0089  50  TRP   B CG  
577  C  CG  B TRP   B 41  ? 0.5918 0.5113 0.4778 0.0719  0.0386  0.0105  50  TRP   B CG  
578  C  CD1 A TRP   B 41  ? 0.6336 0.5423 0.5060 0.0685  0.0432  0.0009  50  TRP   B CD1 
579  C  CD1 B TRP   B 41  ? 0.5939 0.5208 0.4900 0.0627  0.0362  0.0083  50  TRP   B CD1 
580  C  CD2 A TRP   B 41  ? 0.6151 0.5368 0.5061 0.0611  0.0375  0.0039  50  TRP   B CD2 
581  C  CD2 B TRP   B 41  ? 0.5969 0.5092 0.4696 0.0657  0.0406  0.0008  50  TRP   B CD2 
582  N  NE1 A TRP   B 41  ? 0.6425 0.5502 0.5102 0.0582  0.0430  -0.0094 50  TRP   B NE1 
583  N  NE1 B TRP   B 41  ? 0.6006 0.5224 0.4882 0.0517  0.0350  -0.0044 50  TRP   B NE1 
584  C  CE2 A TRP   B 41  ? 0.6327 0.5467 0.5119 0.0527  0.0384  -0.0089 50  TRP   B CE2 
585  C  CE2 B TRP   B 41  ? 0.6067 0.5205 0.4781 0.0547  0.0384  -0.0086 50  TRP   B CE2 
586  C  CE3 A TRP   B 41  ? 0.6158 0.5499 0.5231 0.0572  0.0343  0.0090  50  TRP   B CE3 
587  C  CE3 B TRP   B 41  ? 0.6089 0.5157 0.4716 0.0683  0.0440  -0.0006 50  TRP   B CE3 
588  C  CZ2 A TRP   B 41  ? 0.6417 0.5563 0.5225 0.0410  0.0343  -0.0191 50  TRP   B CZ2 
589  C  CZ2 B TRP   B 41  ? 0.6218 0.5305 0.4778 0.0493  0.0400  -0.0198 50  TRP   B CZ2 
590  C  CZ3 A TRP   B 41  ? 0.6252 0.5617 0.5389 0.0430  0.0305  0.0000  50  TRP   B CZ3 
591  C  CZ3 B TRP   B 41  ? 0.6282 0.5333 0.4788 0.0617  0.0472  -0.0092 50  TRP   B CZ3 
592  C  CH2 A TRP   B 41  ? 0.6347 0.5602 0.5337 0.0352  0.0293  -0.0150 50  TRP   B CH2 
593  C  CH2 B TRP   B 41  ? 0.6284 0.5340 0.4735 0.0538  0.0454  -0.0189 50  TRP   B CH2 
594  N  N   . HIS   B 42  ? 0.5839 0.5133 0.5106 0.0921  0.0500  0.0351  51  HIS   B N   
595  C  CA  . HIS   B 42  ? 0.5776 0.5131 0.5246 0.0834  0.0540  0.0393  51  HIS   B CA  
596  C  C   . HIS   B 42  ? 0.6000 0.5192 0.5574 0.0858  0.0655  0.0414  51  HIS   B C   
597  O  O   . HIS   B 42  ? 0.6101 0.5255 0.5835 0.0736  0.0691  0.0414  51  HIS   B O   
598  C  CB  . HIS   B 42  ? 0.5483 0.5079 0.5061 0.0893  0.0517  0.0531  51  HIS   B CB  
599  C  CG  . HIS   B 42  ? 0.5464 0.5090 0.5056 0.1091  0.0585  0.0663  51  HIS   B CG  
600  N  ND1 . HIS   B 42  ? 0.5550 0.5218 0.4981 0.1269  0.0535  0.0701  51  HIS   B ND1 
601  C  CD2 . HIS   B 42  ? 0.5493 0.5113 0.5229 0.1144  0.0695  0.0768  51  HIS   B CD2 
602  C  CE1 . HIS   B 42  ? 0.5594 0.5286 0.5055 0.1434  0.0609  0.0807  51  HIS   B CE1 
603  N  NE2 . HIS   B 42  ? 0.5633 0.5303 0.5272 0.1370  0.0716  0.0862  51  HIS   B NE2 
604  N  N   . VAL   B 43  ? 0.6063 0.5152 0.5546 0.1010  0.0703  0.0427  52  VAL   B N   
605  C  CA  . VAL   B 43  ? 0.6164 0.5096 0.5702 0.1080  0.0810  0.0454  52  VAL   B CA  
606  C  C   . VAL   B 43  ? 0.6459 0.5187 0.5978 0.0971  0.0841  0.0316  52  VAL   B C   
607  O  O   . VAL   B 43  ? 0.6558 0.5144 0.6188 0.0918  0.0912  0.0330  52  VAL   B O   
608  C  CB  . VAL   B 43  ? 0.6198 0.5126 0.5627 0.1296  0.0821  0.0494  52  VAL   B CB  
609  C  CG1 . VAL   B 43  ? 0.6288 0.5055 0.5731 0.1389  0.0919  0.0499  52  VAL   B CG1 
610  C  CG2 . VAL   B 43  ? 0.6170 0.5261 0.5599 0.1439  0.0807  0.0631  52  VAL   B CG2 
611  N  N   . THR   B 44  ? 0.6564 0.5269 0.5940 0.0947  0.0795  0.0190  53  THR   B N   
612  C  CA  . THR   B 44  ? 0.6730 0.5265 0.6053 0.0885  0.0831  0.0054  53  THR   B CA  
613  C  C   . THR   B 44  ? 0.6845 0.5372 0.6123 0.0712  0.0769  -0.0064 53  THR   B C   
614  O  O   . THR   B 44  ? 0.6882 0.5238 0.6122 0.0657  0.0798  -0.0183 53  THR   B O   
615  C  CB  . THR   B 44  ? 0.6918 0.5463 0.6125 0.0983  0.0841  -0.0003 53  THR   B CB  
616  O  OG1 . THR   B 44  ? 0.7001 0.5681 0.6110 0.0933  0.0761  -0.0028 53  THR   B OG1 
617  C  CG2 . THR   B 44  ? 0.6976 0.5546 0.6212 0.1162  0.0874  0.0085  53  THR   B CG2 
618  N  N   . LYS   B 45  ? 0.6848 0.5555 0.6105 0.0649  0.0677  -0.0040 54  LYS   B N   
619  C  CA  . LYS   B 45  ? 0.6930 0.5688 0.6106 0.0513  0.0593  -0.0144 54  LYS   B CA  
620  C  C   . LYS   B 45  ? 0.7035 0.5732 0.6007 0.0520  0.0603  -0.0267 54  LYS   B C   
621  O  O   . LYS   B 45  ? 0.7101 0.5770 0.5971 0.0430  0.0560  -0.0388 54  LYS   B O   
622  C  CB  . LYS   B 45  ? 0.7136 0.5828 0.6446 0.0368  0.0567  -0.0199 54  LYS   B CB  
623  C  CG  . LYS   B 45  ? 0.7619 0.6510 0.7126 0.0326  0.0524  -0.0067 54  LYS   B CG  
624  C  CD  . LYS   B 45  ? 0.8291 0.7155 0.7989 0.0150  0.0485  -0.0112 54  LYS   B CD  
625  C  CE  . LYS   B 45  ? 0.8765 0.7771 0.8740 0.0137  0.0525  0.0068  54  LYS   B CE  
626  N  NZ  . LYS   B 45  ? 0.9042 0.8350 0.9017 0.0244  0.0492  0.0203  54  LYS   B NZ  
627  N  N   . GLY   B 46  ? 0.7060 0.5767 0.5979 0.0631  0.0653  -0.0230 55  GLY   B N   
628  C  CA  . GLY   B 46  ? 0.7164 0.5866 0.5936 0.0651  0.0688  -0.0308 55  GLY   B CA  
629  C  C   . GLY   B 46  ? 0.7319 0.5867 0.6078 0.0696  0.0780  -0.0407 55  GLY   B C   
630  O  O   . GLY   B 46  ? 0.7451 0.6031 0.6108 0.0734  0.0828  -0.0462 55  GLY   B O   
631  N  N   . ALA   B 47  ? 0.7312 0.5696 0.6174 0.0698  0.0813  -0.0421 56  ALA   B N   
632  C  CA  . ALA   B 47  ? 0.7456 0.5644 0.6288 0.0760  0.0898  -0.0517 56  ALA   B CA  
633  C  C   . ALA   B 47  ? 0.7480 0.5711 0.6336 0.0916  0.0980  -0.0474 56  ALA   B C   
634  O  O   . ALA   B 47  ? 0.7451 0.5803 0.6393 0.0976  0.0966  -0.0359 56  ALA   B O   
635  C  CB  . ALA   B 47  ? 0.7508 0.5476 0.6459 0.0720  0.0914  -0.0515 56  ALA   B CB  
636  N  N   . ALA   B 48  ? 0.7513 0.5656 0.6286 0.0993  0.1056  -0.0576 57  ALA   B N   
637  C  CA  . ALA   B 48  ? 0.7542 0.5760 0.6357 0.1151  0.1132  -0.0550 57  ALA   B CA  
638  C  C   . ALA   B 48  ? 0.7628 0.5729 0.6565 0.1258  0.1165  -0.0461 57  ALA   B C   
639  O  O   . ALA   B 48  ? 0.7734 0.5621 0.6705 0.1218  0.1170  -0.0446 57  ALA   B O   
640  C  CB  . ALA   B 48  ? 0.7619 0.5771 0.6313 0.1227  0.1214  -0.0681 57  ALA   B CB  
641  N  N   . LEU   B 49  ? 0.7527 0.5780 0.6538 0.1393  0.1184  -0.0393 58  LEU   B N   
642  C  CA  . LEU   B 49  ? 0.7526 0.5708 0.6621 0.1533  0.1212  -0.0296 58  LEU   B CA  
643  C  C   . LEU   B 49  ? 0.7656 0.5830 0.6752 0.1721  0.1291  -0.0329 58  LEU   B C   
644  O  O   . LEU   B 49  ? 0.7580 0.5938 0.6670 0.1754  0.1305  -0.0393 58  LEU   B O   
645  C  CB  . LEU   B 49  ? 0.7379 0.5762 0.6543 0.1559  0.1136  -0.0190 58  LEU   B CB  
646  C  CG  . LEU   B 49  ? 0.7436 0.5852 0.6600 0.1420  0.1058  -0.0137 58  LEU   B CG  
647  C  CD1 . LEU   B 49  ? 0.7435 0.6030 0.6628 0.1475  0.0979  -0.0063 58  LEU   B CD1 
648  C  CD2 . LEU   B 49  ? 0.7461 0.5703 0.6668 0.1391  0.1087  -0.0067 58  LEU   B CD2 
649  N  N   . ARG   B 50  ? 0.7834 0.5819 0.6946 0.1854  0.1349  -0.0270 59  ARG   B N   
650  C  CA  . ARG   B 50  ? 0.8043 0.6008 0.7145 0.2067  0.1423  -0.0289 59  ARG   B CA  
651  C  C   . ARG   B 50  ? 0.8114 0.6268 0.7291 0.2232  0.1391  -0.0182 59  ARG   B C   
652  O  O   . ARG   B 50  ? 0.7979 0.6119 0.7180 0.2221  0.1353  -0.0075 59  ARG   B O   
653  C  CB  . ARG   B 50  ? 0.8444 0.6013 0.7478 0.2118  0.1511  -0.0300 59  ARG   B CB  
654  C  CG  . ARG   B 50  ? 0.9146 0.6622 0.8159 0.2375  0.1592  -0.0266 59  ARG   B CG  
655  C  CD  . ARG   B 50  ? 0.9975 0.7012 0.8890 0.2412  0.1679  -0.0315 59  ARG   B CD  
656  N  NE  . ARG   B 50  ? 1.0680 0.7411 0.9626 0.2272  0.1684  -0.0230 59  ARG   B NE  
657  C  CZ  . ARG   B 50  ? 1.1325 0.7904 1.0313 0.2368  0.1736  -0.0062 59  ARG   B CZ  
658  N  NH1 . ARG   B 50  ? 1.1378 0.8078 1.0353 0.2620  0.1772  0.0028  59  ARG   B NH1 
659  N  NH2 . ARG   B 50  ? 1.1467 0.7797 1.0519 0.2215  0.1751  0.0024  59  ARG   B NH2 
660  N  N   . SER   B 51  ? 0.8300 0.6664 0.7517 0.2388  0.1398  -0.0216 60  SER   B N   
661  C  CA  . SER   B 51  ? 0.8575 0.7131 0.7854 0.2561  0.1346  -0.0142 60  SER   B CA  
662  C  C   . SER   B 51  ? 0.9026 0.7560 0.8291 0.2809  0.1422  -0.0150 60  SER   B C   
663  O  O   . SER   B 51  ? 0.8996 0.7818 0.8344 0.2912  0.1401  -0.0202 60  SER   B O   
664  C  CB  . SER   B 51  ? 0.8584 0.7498 0.7969 0.2489  0.1236  -0.0180 60  SER   B CB  
665  O  OG  . SER   B 51  ? 0.8840 0.7923 0.8273 0.2647  0.1155  -0.0130 60  SER   B OG  
666  N  N   . GLY   B 52  ? 0.9375 0.7559 0.8544 0.2897  0.1516  -0.0095 61  GLY   B N   
667  C  CA  . GLY   B 52  ? 0.9616 0.7696 0.8735 0.3149  0.1602  -0.0094 61  GLY   B CA  
668  C  C   . GLY   B 52  ? 0.9870 0.7850 0.8940 0.3118  0.1674  -0.0228 61  GLY   B C   
669  O  O   . GLY   B 52  ? 1.0100 0.7729 0.9079 0.3000  0.1724  -0.0266 61  GLY   B O   
670  N  N   . GLU   B 53  ? 0.9782 0.8089 0.8919 0.3221  0.1672  -0.0307 62  GLU   B N   
671  C  CA  . GLU   B 53  ? 0.9881 0.8160 0.8959 0.3221  0.1748  -0.0436 62  GLU   B CA  
672  C  C   . GLU   B 53  ? 0.9709 0.8258 0.8848 0.2989  0.1705  -0.0514 62  GLU   B C   
673  O  O   . GLU   B 53  ? 0.9882 0.8389 0.8934 0.2962  0.1769  -0.0619 62  GLU   B O   
674  C  CB  . GLU   B 53  ? 1.0226 0.8704 0.9334 0.3510  0.1806  -0.0461 62  GLU   B CB  
675  C  CG  . GLU   B 53  ? 1.1187 0.9362 1.0129 0.3646  0.1926  -0.0554 62  GLU   B CG  
676  C  CD  . GLU   B 53  ? 1.2424 1.0791 1.1386 0.3974  0.1990  -0.0566 62  GLU   B CD  
677  O  OE1 . GLU   B 53  ? 1.2406 1.1238 1.1552 0.4068  0.1931  -0.0520 62  GLU   B OE1 
678  O  OE2 . GLU   B 53  ? 1.3092 1.1141 1.1885 0.4143  0.2091  -0.0630 62  GLU   B OE2 
679  N  N   . GLY   B 54  ? 0.9373 0.8179 0.8637 0.2842  0.1600  -0.0460 63  GLY   B N   
680  C  CA  . GLY   B 54  ? 0.9169 0.8215 0.8493 0.2626  0.1557  -0.0501 63  GLY   B CA  
681  C  C   . GLY   B 54  ? 0.9077 0.7893 0.8301 0.2392  0.1520  -0.0503 63  GLY   B C   
682  O  O   . GLY   B 54  ? 0.9270 0.7795 0.8434 0.2365  0.1504  -0.0452 63  GLY   B O   
683  N  N   . ARG   B 55  ? 0.8723 0.7692 0.7939 0.2225  0.1510  -0.0550 64  ARG   B N   
684  C  CA  . ARG   B 55  ? 0.8560 0.7358 0.7674 0.2015  0.1466  -0.0561 64  ARG   B CA  
685  C  C   . ARG   B 55  ? 0.8086 0.7141 0.7288 0.1853  0.1379  -0.0507 64  ARG   B C   
686  O  O   . ARG   B 55  ? 0.7948 0.7303 0.7244 0.1840  0.1390  -0.0508 64  ARG   B O   
687  C  CB  . ARG   B 55  ? 0.8810 0.7474 0.7753 0.1984  0.1539  -0.0681 64  ARG   B CB  
688  C  CG  . ARG   B 55  ? 0.9308 0.7772 0.8127 0.1789  0.1485  -0.0715 64  ARG   B CG  
689  C  CD  . ARG   B 55  ? 0.9918 0.8344 0.8551 0.1773  0.1540  -0.0846 64  ARG   B CD  
690  N  NE  . ARG   B 55  ? 1.0472 0.8784 0.8982 0.1587  0.1467  -0.0887 64  ARG   B NE  
691  C  CZ  . ARG   B 55  ? 1.0978 0.9016 0.9306 0.1558  0.1463  -0.1019 64  ARG   B CZ  
692  N  NH1 . ARG   B 55  ? 1.1117 0.8919 0.9346 0.1704  0.1534  -0.1125 64  ARG   B NH1 
693  N  NH2 . ARG   B 55  ? 1.0989 0.8981 0.9225 0.1390  0.1377  -0.1055 64  ARG   B NH2 
694  N  N   . LEU   B 56  ? 0.7810 0.6745 0.6991 0.1733  0.1297  -0.0452 65  LEU   B N   
695  C  CA  . LEU   B 56  ? 0.7502 0.6598 0.6728 0.1588  0.1206  -0.0399 65  LEU   B CA  
696  C  C   . LEU   B 56  ? 0.7336 0.6326 0.6421 0.1427  0.1199  -0.0433 65  LEU   B C   
697  O  O   . LEU   B 56  ? 0.7377 0.6144 0.6387 0.1384  0.1182  -0.0442 65  LEU   B O   
698  C  CB  . LEU   B 56  ? 0.7495 0.6538 0.6771 0.1605  0.1113  -0.0312 65  LEU   B CB  
699  C  CG  . LEU   B 56  ? 0.7677 0.6761 0.7039 0.1793  0.1105  -0.0275 65  LEU   B CG  
700  C  CD1 . LEU   B 56  ? 0.7830 0.6876 0.7195 0.1810  0.1012  -0.0192 65  LEU   B CD1 
701  C  CD2 . LEU   B 56  ? 0.7615 0.6993 0.7114 0.1852  0.1088  -0.0299 65  LEU   B CD2 
702  N  N   . ASP   B 57  ? 0.7131 0.6296 0.6190 0.1338  0.1210  -0.0443 66  ASP   B N   
703  C  CA  . ASP   B 57  ? 0.7117 0.6213 0.6013 0.1204  0.1196  -0.0472 66  ASP   B CA  
704  C  C   . ASP   B 57  ? 0.6800 0.5958 0.5715 0.1083  0.1094  -0.0379 66  ASP   B C   
705  O  O   . ASP   B 57  ? 0.6721 0.6031 0.5761 0.1077  0.1057  -0.0311 66  ASP   B O   
706  C  CB  . ASP   B 57  ? 0.7520 0.6761 0.6327 0.1207  0.1289  -0.0527 66  ASP   B CB  
707  C  CG  . ASP   B 57  ? 0.8636 0.7814 0.7401 0.1359  0.1392  -0.0626 66  ASP   B CG  
708  O  OD1 . ASP   B 57  ? 0.8977 0.7876 0.7643 0.1392  0.1389  -0.0703 66  ASP   B OD1 
709  O  OD2 . ASP   B 57  ? 0.8969 0.8377 0.7812 0.1446  0.1477  -0.0624 66  ASP   B OD2 
710  N  N   . PRO   B 58  ? 0.6607 0.5642 0.5405 0.0991  0.1035  -0.0381 67  PRO   B N   
711  C  CA  . PRO   B 58  ? 0.6427 0.5510 0.5218 0.0902  0.0940  -0.0292 67  PRO   B CA  
712  C  C   . PRO   B 58  ? 0.6286 0.5526 0.5035 0.0833  0.0962  -0.0252 67  PRO   B C   
713  O  O   . PRO   B 58  ? 0.6367 0.5679 0.5033 0.0832  0.1049  -0.0299 67  PRO   B O   
714  C  CB  . PRO   B 58  ? 0.6578 0.5537 0.5254 0.0833  0.0888  -0.0319 67  PRO   B CB  
715  C  CG  . PRO   B 58  ? 0.6724 0.5591 0.5306 0.0844  0.0953  -0.0438 67  PRO   B CG  
716  C  CD  . PRO   B 58  ? 0.6593 0.5447 0.5265 0.0963  0.1043  -0.0472 67  PRO   B CD  
717  N  N   . TYR   B 59  ? 0.6065 0.5350 0.4869 0.0784  0.0888  -0.0158 68  TYR   B N   
718  C  CA  . TYR   B 59  ? 0.5890 0.5297 0.4686 0.0704  0.0909  -0.0089 68  TYR   B CA  
719  C  C   . TYR   B 59  ? 0.6007 0.5336 0.4664 0.0624  0.0830  -0.0014 68  TYR   B C   
720  O  O   . TYR   B 59  ? 0.6229 0.5605 0.4750 0.0564  0.0871  0.0023  68  TYR   B O   
721  C  CB  . TYR   B 59  ? 0.5636 0.5157 0.4653 0.0714  0.0894  -0.0049 68  TYR   B CB  
722  C  CG  . TYR   B 59  ? 0.5572 0.5210 0.4644 0.0602  0.0909  0.0045  68  TYR   B CG  
723  C  CD1 . TYR   B 59  ? 0.5649 0.5172 0.4658 0.0519  0.0819  0.0133  68  TYR   B CD1 
724  C  CD2 . TYR   B 59  ? 0.5433 0.5298 0.4655 0.0586  0.1010  0.0057  68  TYR   B CD2 
725  C  CE1 . TYR   B 59  ? 0.5723 0.5312 0.4797 0.0405  0.0835  0.0235  68  TYR   B CE1 
726  C  CE2 . TYR   B 59  ? 0.5475 0.5459 0.4798 0.0463  0.1031  0.0165  68  TYR   B CE2 
727  C  CZ  . TYR   B 59  ? 0.5712 0.5536 0.4960 0.0364  0.0942  0.0257  68  TYR   B CZ  
728  O  OH  . TYR   B 59  ? 0.5936 0.5835 0.5283 0.0229  0.0968  0.0381  68  TYR   B OH  
729  N  N   . TRP   B 60  ? 0.5967 0.5187 0.4642 0.0646  0.0722  0.0017  69  TRP   B N   
730  C  CA  . TRP   B 60  ? 0.5981 0.5120 0.4527 0.0606  0.0635  0.0090  69  TRP   B CA  
731  C  C   . TRP   B 60  ? 0.6011 0.5076 0.4537 0.0666  0.0566  0.0065  69  TRP   B C   
732  O  O   . TRP   B 60  ? 0.5914 0.4959 0.4558 0.0739  0.0563  0.0037  69  TRP   B O   
733  C  CB  . TRP   B 60  ? 0.5913 0.5002 0.4532 0.0587  0.0562  0.0175  69  TRP   B CB  
734  C  CG  . TRP   B 60  ? 0.6003 0.4969 0.4482 0.0591  0.0462  0.0246  69  TRP   B CG  
735  C  CD1 . TRP   B 60  ? 0.6180 0.5118 0.4486 0.0536  0.0460  0.0318  69  TRP   B CD1 
736  C  CD2 . TRP   B 60  ? 0.6042 0.4917 0.4518 0.0683  0.0361  0.0252  69  TRP   B CD2 
737  N  NE1 . TRP   B 60  ? 0.6263 0.5090 0.4469 0.0589  0.0354  0.0368  69  TRP   B NE1 
738  C  CE2 . TRP   B 60  ? 0.6176 0.4972 0.4487 0.0681  0.0296  0.0326  69  TRP   B CE2 
739  C  CE3 . TRP   B 60  ? 0.6069 0.4931 0.4652 0.0788  0.0326  0.0212  69  TRP   B CE3 
740  C  CZ2 . TRP   B 60  ? 0.6268 0.4990 0.4530 0.0783  0.0200  0.0354  69  TRP   B CZ2 
741  C  CZ3 . TRP   B 60  ? 0.6172 0.4959 0.4697 0.0885  0.0236  0.0247  69  TRP   B CZ3 
742  C  CH2 . TRP   B 60  ? 0.6229 0.4950 0.4601 0.0883  0.0174  0.0315  69  TRP   B CH2 
743  N  N   . GLY   B 61  ? 0.6087 0.5135 0.4473 0.0640  0.0515  0.0090  70  GLY   B N   
744  C  CA  . GLY   B 61  ? 0.6169 0.5204 0.4570 0.0680  0.0453  0.0084  70  GLY   B CA  
745  C  C   . GLY   B 61  ? 0.6250 0.5302 0.4513 0.0668  0.0370  0.0143  70  GLY   B C   
746  O  O   . GLY   B 61  ? 0.6334 0.5401 0.4446 0.0619  0.0374  0.0166  70  GLY   B O   
747  N  N   . ASP   B 62  ? 0.6279 0.5348 0.4586 0.0728  0.0302  0.0182  71  ASP   B N   
748  C  CA  . ASP   B 62  ? 0.6367 0.5487 0.4557 0.0744  0.0216  0.0242  71  ASP   B CA  
749  C  C   . ASP   B 62  ? 0.6201 0.5423 0.4512 0.0793  0.0177  0.0254  71  ASP   B C   
750  O  O   . ASP   B 62  ? 0.6205 0.5404 0.4610 0.0884  0.0177  0.0295  71  ASP   B O   
751  C  CB  . ASP   B 62  ? 0.6748 0.5758 0.4841 0.0805  0.0162  0.0339  71  ASP   B CB  
752  C  CG  . ASP   B 62  ? 0.7574 0.6606 0.5494 0.0834  0.0085  0.0411  71  ASP   B CG  
753  O  OD1 . ASP   B 62  ? 0.7531 0.6647 0.5470 0.0916  0.0021  0.0443  71  ASP   B OD1 
754  O  OD2 . ASP   B 62  ? 0.8198 0.7174 0.5961 0.0787  0.0096  0.0450  71  ASP   B OD2 
755  N  N   . VAL   B 63  ? 0.6115 0.5464 0.4429 0.0733  0.0145  0.0217  72  VAL   B N   
756  C  CA  . VAL   B 63  ? 0.5933 0.5429 0.4409 0.0747  0.0112  0.0239  72  VAL   B CA  
757  C  C   . VAL   B 63  ? 0.5947 0.5524 0.4402 0.0877  0.0046  0.0356  72  VAL   B C   
758  O  O   . VAL   B 63  ? 0.5940 0.5598 0.4545 0.0949  0.0061  0.0410  72  VAL   B O   
759  C  CB  . VAL   B 63  ? 0.5862 0.5483 0.4355 0.0627  0.0069  0.0152  72  VAL   B CB  
760  C  CG1 . VAL   B 63  ? 0.5669 0.5515 0.4323 0.0628  0.0001  0.0201  72  VAL   B CG1 
761  C  CG2 . VAL   B 63  ? 0.5952 0.5466 0.4520 0.0531  0.0141  0.0033  72  VAL   B CG2 
762  N  N   . LYS   B 64  ? 0.6001 0.5543 0.4258 0.0927  -0.0017 0.0404  73  LYS   B N   
763  C  CA  . LYS   B 64  ? 0.6033 0.5618 0.4239 0.1081  -0.0083 0.0509  73  LYS   B CA  
764  C  C   . LYS   B 64  ? 0.6155 0.5586 0.4379 0.1203  -0.0059 0.0546  73  LYS   B C   
765  O  O   . LYS   B 64  ? 0.6061 0.5584 0.4350 0.1335  -0.0072 0.0605  73  LYS   B O   
766  C  CB  . LYS   B 64  ? 0.6330 0.5859 0.4295 0.1117  -0.0154 0.0558  73  LYS   B CB  
767  C  CG  . LYS   B 64  ? 0.6668 0.6320 0.4587 0.1278  -0.0236 0.0652  73  LYS   B CG  
768  C  CD  . LYS   B 64  ? 0.7145 0.6651 0.4796 0.1348  -0.0297 0.0720  73  LYS   B CD  
769  C  CE  . LYS   B 64  ? 0.7579 0.7199 0.5169 0.1539  -0.0378 0.0811  73  LYS   B CE  
770  N  NZ  . LYS   B 64  ? 0.7936 0.7768 0.5430 0.1541  -0.0450 0.0835  73  LYS   B NZ  
771  N  N   . GLN   B 65  ? 0.6305 0.5524 0.4476 0.1165  -0.0024 0.0508  74  GLN   B N   
772  C  CA  . GLN   B 65  ? 0.6377 0.5453 0.4567 0.1272  -0.0022 0.0514  74  GLN   B CA  
773  C  C   . GLN   B 65  ? 0.6193 0.5360 0.4569 0.1300  0.0049  0.0492  74  GLN   B C   
774  O  O   . GLN   B 65  ? 0.6254 0.5373 0.4638 0.1441  0.0041  0.0513  74  GLN   B O   
775  C  CB  . GLN   B 65  ? 0.6795 0.5669 0.4929 0.1197  -0.0011 0.0476  74  GLN   B CB  
776  C  CG  . GLN   B 65  ? 0.7501 0.6218 0.5450 0.1184  -0.0072 0.0529  74  GLN   B CG  
777  C  CD  . GLN   B 65  ? 0.8245 0.6786 0.6202 0.1095  -0.0055 0.0508  74  GLN   B CD  
778  O  OE1 . GLN   B 65  ? 0.8420 0.6873 0.6458 0.1137  -0.0073 0.0469  74  GLN   B OE1 
779  N  NE2 . GLN   B 65  ? 0.8350 0.6862 0.6228 0.0973  -0.0020 0.0538  74  GLN   B NE2 
780  N  N   . ASP   B 66  ? 0.5974 0.5251 0.4479 0.1178  0.0113  0.0449  75  ASP   B N   
781  C  CA  . ASP   B 66  ? 0.5799 0.5128 0.4482 0.1173  0.0194  0.0436  75  ASP   B CA  
782  C  C   . ASP   B 66  ? 0.5734 0.4914 0.4422 0.1213  0.0238  0.0393  75  ASP   B C   
783  O  O   . ASP   B 66  ? 0.5591 0.4774 0.4353 0.1320  0.0276  0.0421  75  ASP   B O   
784  C  CB  . ASP   B 66  ? 0.5773 0.5264 0.4564 0.1290  0.0204  0.0531  75  ASP   B CB  
785  C  CG  . ASP   B 66  ? 0.5958 0.5507 0.4950 0.1244  0.0301  0.0540  75  ASP   B CG  
786  O  OD1 . ASP   B 66  ? 0.5922 0.5431 0.4980 0.1087  0.0333  0.0463  75  ASP   B OD1 
787  O  OD2 . ASP   B 66  ? 0.6044 0.5661 0.5112 0.1375  0.0347  0.0628  75  ASP   B OD2 
788  N  N   . LEU   B 67  ? 0.5758 0.4834 0.4375 0.1129  0.0236  0.0331  76  LEU   B N   
789  C  CA  . LEU   B 67  ? 0.5669 0.4651 0.4319 0.1151  0.0266  0.0285  76  LEU   B CA  
790  C  C   . LEU   B 67  ? 0.5624 0.4601 0.4303 0.1021  0.0337  0.0210  76  LEU   B C   
791  O  O   . LEU   B 67  ? 0.5652 0.4660 0.4264 0.0918  0.0341  0.0191  76  LEU   B O   
792  C  CB  . LEU   B 67  ? 0.5715 0.4585 0.4266 0.1198  0.0180  0.0299  76  LEU   B CB  
793  C  CG  . LEU   B 67  ? 0.5858 0.4688 0.4342 0.1370  0.0101  0.0349  76  LEU   B CG  
794  C  CD1 . LEU   B 67  ? 0.5978 0.4640 0.4354 0.1390  0.0004  0.0342  76  LEU   B CD1 
795  C  CD2 . LEU   B 67  ? 0.5931 0.4796 0.4493 0.1509  0.0134  0.0345  76  LEU   B CD2 
796  N  N   . VAL   B 68  ? 0.5587 0.4539 0.4349 0.1048  0.0391  0.0165  77  VAL   B N   
797  C  CA  . VAL   B 68  ? 0.5501 0.4463 0.4290 0.0964  0.0470  0.0092  77  VAL   B CA  
798  C  C   . VAL   B 68  ? 0.5493 0.4459 0.4371 0.1027  0.0489  0.0065  77  VAL   B C   
799  O  O   . VAL   B 68  ? 0.5503 0.4456 0.4434 0.1148  0.0466  0.0082  77  VAL   B O   
800  C  CB  . VAL   B 68  ? 0.5440 0.4395 0.4267 0.0927  0.0543  0.0042  77  VAL   B CB  
801  C  CG1 . VAL   B 68  ? 0.5464 0.4388 0.4401 0.1032  0.0578  0.0072  77  VAL   B CG1 
802  C  CG2 . VAL   B 68  ? 0.5384 0.4333 0.4192 0.0869  0.0621  -0.0046 77  VAL   B CG2 
803  N  N   . SER   B 69  ? 0.5533 0.4545 0.4427 0.0955  0.0526  0.0031  78  SER   B N   
804  C  CA  . SER   B 69  ? 0.5515 0.4592 0.4534 0.1001  0.0541  0.0002  78  SER   B CA  
805  C  C   . SER   B 69  ? 0.5447 0.4597 0.4508 0.0984  0.0661  -0.0062 78  SER   B C   
806  O  O   . SER   B 69  ? 0.5427 0.4576 0.4396 0.0905  0.0716  -0.0083 78  SER   B O   
807  C  CB  . SER   B 69  ? 0.5597 0.4695 0.4642 0.0930  0.0473  0.0032  78  SER   B CB  
808  O  OG  . SER   B 69  ? 0.5645 0.4813 0.4668 0.0806  0.0542  0.0043  78  SER   B OG  
809  N  N   . TYR   B 70  ? 0.5401 0.4612 0.4580 0.1083  0.0695  -0.0096 79  TYR   B N   
810  C  CA  . TYR   B 70  ? 0.5450 0.4726 0.4669 0.1116  0.0809  -0.0158 79  TYR   B CA  
811  C  C   . TYR   B 70  ? 0.5519 0.4996 0.4894 0.1129  0.0816  -0.0167 79  TYR   B C   
812  O  O   . TYR   B 70  ? 0.5527 0.5053 0.5005 0.1179  0.0729  -0.0151 79  TYR   B O   
813  C  CB  . TYR   B 70  ? 0.5397 0.4568 0.4626 0.1255  0.0848  -0.0179 79  TYR   B CB  
814  C  CG  . TYR   B 70  ? 0.5500 0.4498 0.4628 0.1216  0.0861  -0.0174 79  TYR   B CG  
815  C  CD1 . TYR   B 70  ? 0.5609 0.4555 0.4708 0.1198  0.0785  -0.0107 79  TYR   B CD1 
816  C  CD2 . TYR   B 70  ? 0.5635 0.4532 0.4703 0.1196  0.0943  -0.0242 79  TYR   B CD2 
817  C  CE1 . TYR   B 70  ? 0.5718 0.4562 0.4769 0.1138  0.0791  -0.0097 79  TYR   B CE1 
818  C  CE2 . TYR   B 70  ? 0.5798 0.4550 0.4803 0.1126  0.0935  -0.0250 79  TYR   B CE2 
819  C  CZ  . TYR   B 70  ? 0.5934 0.4683 0.4952 0.1089  0.0859  -0.0171 79  TYR   B CZ  
820  O  OH  . TYR   B 70  ? 0.6228 0.4883 0.5235 0.1013  0.0848  -0.0171 79  TYR   B OH  
821  N  N   . CYS   B 71  ? 0.5570 0.5183 0.4966 0.1082  0.0914  -0.0190 80  CYS   B N   
822  C  CA  . CYS   B 71  ? 0.5558 0.5429 0.5144 0.1083  0.0947  -0.0189 80  CYS   B CA  
823  C  C   . CYS   B 71  ? 0.5365 0.5343 0.5044 0.0927  0.0890  -0.0117 80  CYS   B C   
824  O  O   . CYS   B 71  ? 0.5271 0.5492 0.5115 0.0877  0.0947  -0.0096 80  CYS   B O   
825  C  CB  . CYS   B 71  ? 0.5788 0.5745 0.5526 0.1235  0.0911  -0.0221 80  CYS   B CB  
826  S  SG  . CYS   B 71  ? 0.6947 0.6752 0.6584 0.1429  0.1000  -0.0280 80  CYS   B SG  
827  N  N   . GLY   B 72  ? 0.5234 0.5037 0.4815 0.0851  0.0790  -0.0071 81  GLY   B N   
828  C  CA  . GLY   B 72  ? 0.5077 0.4909 0.4724 0.0705  0.0732  0.0005  81  GLY   B CA  
829  C  C   . GLY   B 72  ? 0.5111 0.4703 0.4590 0.0661  0.0629  0.0050  81  GLY   B C   
830  O  O   . GLY   B 72  ? 0.5231 0.4674 0.4559 0.0740  0.0605  0.0027  81  GLY   B O   
831  N  N   . PRO   B 73  ? 0.5042 0.4594 0.4551 0.0534  0.0575  0.0126  82  PRO   B N   
832  C  CA  . PRO   B 73  ? 0.5236 0.4543 0.4567 0.0516  0.0473  0.0174  82  PRO   B CA  
833  C  C   . PRO   B 73  ? 0.5440 0.4612 0.4769 0.0634  0.0330  0.0124  82  PRO   B C   
834  O  O   . PRO   B 73  ? 0.5342 0.4599 0.4832 0.0694  0.0280  0.0064  82  PRO   B O   
835  C  CB  . PRO   B 73  ? 0.5295 0.4576 0.4684 0.0355  0.0455  0.0273  82  PRO   B CB  
836  C  CG  . PRO   B 73  ? 0.5127 0.4649 0.4811 0.0291  0.0492  0.0260  82  PRO   B CG  
837  C  CD  . PRO   B 73  ? 0.4777 0.4506 0.4502 0.0403  0.0603  0.0181  82  PRO   B CD  
838  N  N   . TRP   B 74  ? 0.5667 0.4643 0.4806 0.0683  0.0258  0.0151  83  TRP   B N   
839  C  CA  . TRP   B 74  ? 0.5841 0.4685 0.4933 0.0819  0.0129  0.0117  83  TRP   B CA  
840  C  C   . TRP   B 74  ? 0.6056 0.4853 0.5281 0.0794  0.0002  0.0083  83  TRP   B C   
841  O  O   . TRP   B 74  ? 0.6138 0.4867 0.5407 0.0649  -0.0026 0.0132  83  TRP   B O   
842  C  CB  . TRP   B 74  ? 0.5943 0.4609 0.4821 0.0853  0.0077  0.0175  83  TRP   B CB  
843  C  CG  . TRP   B 74  ? 0.6038 0.4614 0.4832 0.1031  -0.0014 0.0149  83  TRP   B CG  
844  C  CD1 . TRP   B 74  ? 0.6184 0.4588 0.4911 0.1111  -0.0155 0.0134  83  TRP   B CD1 
845  C  CD2 . TRP   B 74  ? 0.6049 0.4700 0.4810 0.1162  0.0036  0.0141  83  TRP   B CD2 
846  N  NE1 . TRP   B 74  ? 0.6260 0.4654 0.4893 0.1305  -0.0187 0.0120  83  TRP   B NE1 
847  C  CE2 . TRP   B 74  ? 0.6182 0.4737 0.4853 0.1331  -0.0065 0.0137  83  TRP   B CE2 
848  C  CE3 . TRP   B 74  ? 0.6053 0.4828 0.4852 0.1152  0.0157  0.0139  83  TRP   B CE3 
849  C  CZ2 . TRP   B 74  ? 0.6298 0.4917 0.4934 0.1487  -0.0029 0.0154  83  TRP   B CZ2 
850  C  CZ3 . TRP   B 74  ? 0.6155 0.4957 0.4937 0.1283  0.0180  0.0152  83  TRP   B CZ3 
851  C  CH2 . TRP   B 74  ? 0.6243 0.4988 0.4954 0.1448  0.0097  0.0171  83  TRP   B CH2 
852  N  N   . LYS   B 75  ? 0.6115 0.4959 0.5415 0.0928  -0.0070 0.0001  84  LYS   B N   
853  C  CA  . LYS   B 75  ? 0.6220 0.5051 0.5663 0.0912  -0.0213 -0.0064 84  LYS   B CA  
854  C  C   . LYS   B 75  ? 0.6582 0.5186 0.5870 0.1057  -0.0387 -0.0115 84  LYS   B C   
855  O  O   . LYS   B 75  ? 0.6614 0.5137 0.5985 0.1026  -0.0539 -0.0180 84  LYS   B O   
856  C  CB  . LYS   B 75  ? 0.6159 0.5248 0.5802 0.0978  -0.0189 -0.0137 84  LYS   B CB  
857  C  CG  . LYS   B 75  ? 0.6300 0.5634 0.6111 0.0864  -0.0027 -0.0104 84  LYS   B CG  
858  C  CD  . LYS   B 75  ? 0.6494 0.5925 0.6525 0.0655  -0.0046 -0.0073 84  LYS   B CD  
859  C  CE  . LYS   B 75  ? 0.6682 0.6342 0.6815 0.0553  0.0143  -0.0011 84  LYS   B CE  
860  N  NZ  . LYS   B 75  ? 0.6716 0.6704 0.7145 0.0548  0.0165  -0.0055 84  LYS   B NZ  
861  N  N   . LEU   B 76  ? 0.6805 0.5324 0.5880 0.1223  -0.0367 -0.0092 85  LEU   B N   
862  C  CA  . LEU   B 76  ? 0.7010 0.5348 0.5898 0.1416  -0.0504 -0.0133 85  LEU   B CA  
863  C  C   . LEU   B 76  ? 0.7461 0.5524 0.6194 0.1366  -0.0593 -0.0095 85  LEU   B C   
864  O  O   . LEU   B 76  ? 0.7574 0.5600 0.6196 0.1336  -0.0512 -0.0003 85  LEU   B O   
865  C  CB  . LEU   B 76  ? 0.6897 0.5312 0.5655 0.1610  -0.0415 -0.0095 85  LEU   B CB  
866  C  CG  . LEU   B 76  ? 0.6864 0.5501 0.5745 0.1660  -0.0296 -0.0101 85  LEU   B CG  
867  C  CD1 . LEU   B 76  ? 0.6891 0.5567 0.5662 0.1808  -0.0196 -0.0033 85  LEU   B CD1 
868  C  CD2 . LEU   B 76  ? 0.6906 0.5622 0.5873 0.1767  -0.0391 -0.0198 85  LEU   B CD2 
869  N  N   . ASP   B 77  ? 0.7789 0.5645 0.6502 0.1373  -0.0771 -0.0172 86  ASP   B N   
870  C  CA  . ASP   B 77  ? 0.8265 0.5800 0.6825 0.1326  -0.0864 -0.0137 86  ASP   B CA  
871  C  C   . ASP   B 77  ? 0.8634 0.5899 0.6950 0.1553  -0.1037 -0.0217 86  ASP   B C   
872  O  O   . ASP   B 77  ? 0.8885 0.5873 0.7019 0.1568  -0.1092 -0.0174 86  ASP   B O   
873  C  CB  . ASP   B 77  ? 0.8567 0.6001 0.7319 0.1063  -0.0914 -0.0128 86  ASP   B CB  
874  C  CG  . ASP   B 77  ? 0.9444 0.6963 0.8432 0.1004  -0.1034 -0.0252 86  ASP   B CG  
875  O  OD1 . ASP   B 77  ? 0.9575 0.7238 0.8557 0.1187  -0.1081 -0.0353 86  ASP   B OD1 
876  O  OD2 . ASP   B 77  ? 0.9833 0.7293 0.9024 0.0774  -0.1081 -0.0240 86  ASP   B OD2 
877  N  N   . ALA   B 78  ? 0.8633 0.5969 0.6916 0.1749  -0.1119 -0.0328 87  ALA   B N   
878  C  CA  . ALA   B 78  ? 0.8855 0.5953 0.6874 0.2003  -0.1282 -0.0419 87  ALA   B CA  
879  C  C   . ALA   B 78  ? 0.9045 0.6072 0.6798 0.2189  -0.1214 -0.0321 87  ALA   B C   
880  O  O   . ALA   B 78  ? 0.8932 0.6191 0.6721 0.2182  -0.1037 -0.0204 87  ALA   B O   
881  C  CB  . ALA   B 78  ? 0.8772 0.6035 0.6782 0.2209  -0.1342 -0.0532 87  ALA   B CB  
882  N  N   . ALA   B 79  ? 0.9299 0.6002 0.6797 0.2348  -0.1360 -0.0373 88  ALA   B N   
883  C  CA  . ALA   B 79  ? 0.9506 0.6164 0.6760 0.2545  -0.1306 -0.0280 88  ALA   B CA  
884  C  C   . ALA   B 79  ? 0.9760 0.6309 0.6727 0.2901  -0.1415 -0.0367 88  ALA   B C   
885  O  O   . ALA   B 79  ? 0.9884 0.6219 0.6770 0.2980  -0.1599 -0.0527 88  ALA   B O   
886  C  CB  . ALA   B 79  ? 0.9677 0.6046 0.6855 0.2414  -0.1336 -0.0210 88  ALA   B CB  
887  N  N   . TRP   B 80  ? 0.9825 0.6544 0.6645 0.3124  -0.1305 -0.0265 89  TRP   B N   
888  C  CA  . TRP   B 80  ? 1.0100 0.6755 0.6621 0.3500  -0.1376 -0.0318 89  TRP   B CA  
889  C  C   . TRP   B 80  ? 1.0419 0.6604 0.6679 0.3588  -0.1564 -0.0403 89  TRP   B C   
890  O  O   . TRP   B 80  ? 1.0446 0.6466 0.6723 0.3429  -0.1552 -0.0326 89  TRP   B O   
891  C  CB  . TRP   B 80  ? 1.0045 0.7029 0.6522 0.3679  -0.1193 -0.0154 89  TRP   B CB  
892  C  CG  . TRP   B 80  ? 1.0242 0.7215 0.6411 0.4089  -0.1235 -0.0179 89  TRP   B CG  
893  C  CD1 . TRP   B 80  ? 1.0429 0.7379 0.6435 0.4332  -0.1320 -0.0298 89  TRP   B CD1 
894  C  CD2 . TRP   B 80  ? 1.0275 0.7320 0.6263 0.4324  -0.1175 -0.0071 89  TRP   B CD2 
895  N  NE1 . TRP   B 80  ? 1.0560 0.7539 0.6271 0.4712  -0.1314 -0.0272 89  TRP   B NE1 
896  C  CE2 . TRP   B 80  ? 1.0497 0.7546 0.6206 0.4712  -0.1222 -0.0130 89  TRP   B CE2 
897  C  CE3 . TRP   B 80  ? 1.0312 0.7430 0.6337 0.4259  -0.1097 0.0065  89  TRP   B CE3 
898  C  CZ2 . TRP   B 80  ? 1.0597 0.7720 0.6072 0.5038  -0.1183 -0.0052 89  TRP   B CZ2 
899  C  CZ3 . TRP   B 80  ? 1.0461 0.7668 0.6275 0.4573  -0.1068 0.0140  89  TRP   B CZ3 
900  C  CH2 . TRP   B 80  ? 1.0549 0.7774 0.6104 0.4956  -0.1100 0.0088  89  TRP   B CH2 
901  N  N   . ASP   B 81  ? 1.0697 0.6642 0.6706 0.3841  -0.1743 -0.0568 90  ASP   B N   
902  C  CA  . ASP   B 81  ? 1.1131 0.6560 0.6877 0.3929  -0.1942 -0.0675 90  ASP   B CA  
903  C  C   . ASP   B 81  ? 1.1392 0.6738 0.6812 0.4255  -0.1915 -0.0604 90  ASP   B C   
904  O  O   . ASP   B 81  ? 1.1650 0.6538 0.6817 0.4363  -0.2076 -0.0690 90  ASP   B O   
905  C  CB  . ASP   B 81  ? 1.1519 0.6658 0.7133 0.4030  -0.2187 -0.0920 90  ASP   B CB  
906  C  CG  . ASP   B 81  ? 1.2159 0.7501 0.7558 0.4405  -0.2203 -0.1003 90  ASP   B CG  
907  O  OD1 . ASP   B 81  ? 1.2226 0.7934 0.7582 0.4596  -0.2007 -0.0852 90  ASP   B OD1 
908  O  OD2 . ASP   B 81  ? 1.2432 0.7577 0.7711 0.4506  -0.2412 -0.1215 90  ASP   B OD2 
909  N  N   . GLY   B 82  ? 1.1344 0.7127 0.6782 0.4413  -0.1719 -0.0451 91  GLY   B N   
910  C  CA  . GLY   B 82  ? 1.1599 0.7415 0.6777 0.4732  -0.1671 -0.0363 91  GLY   B CA  
911  C  C   . GLY   B 82  ? 1.1912 0.7681 0.6739 0.5181  -0.1749 -0.0468 91  GLY   B C   
912  O  O   . GLY   B 82  ? 1.2015 0.7903 0.6636 0.5491  -0.1681 -0.0381 91  GLY   B O   
913  N  N   . LEU   B 83  ? 1.2003 0.7618 0.6747 0.5241  -0.1896 -0.0658 92  LEU   B N   
914  C  CA  . LEU   B 83  ? 1.2252 0.7798 0.6616 0.5687  -0.1989 -0.0782 92  LEU   B CA  
915  C  C   . LEU   B 83  ? 1.2226 0.8124 0.6643 0.5795  -0.1927 -0.0804 92  LEU   B C   
916  O  O   . LEU   B 83  ? 1.2318 0.8426 0.6492 0.6183  -0.1858 -0.0771 92  LEU   B O   
917  C  CB  . LEU   B 83  ? 1.2617 0.7534 0.6698 0.5758  -0.2291 -0.1042 92  LEU   B CB  
918  C  CG  . LEU   B 83  ? 1.3080 0.7522 0.7039 0.5692  -0.2391 -0.1047 92  LEU   B CG  
919  C  CD1 . LEU   B 83  ? 1.3498 0.7297 0.7201 0.5744  -0.2701 -0.1320 92  LEU   B CD1 
920  C  CD2 . LEU   B 83  ? 1.3212 0.7763 0.6914 0.6043  -0.2276 -0.0911 92  LEU   B CD2 
921  N  N   . SER   B 84  ? 1.2090 0.8034 0.6791 0.5489  -0.1964 -0.0867 93  SER   B N   
922  C  CA  . SER   B 84  ? 1.1998 0.8230 0.6734 0.5595  -0.1932 -0.0903 93  SER   B CA  
923  C  C   . SER   B 84  ? 1.1648 0.8419 0.6585 0.5608  -0.1640 -0.0662 93  SER   B C   
924  O  O   . SER   B 84  ? 1.1559 0.8520 0.6762 0.5370  -0.1467 -0.0481 93  SER   B O   
925  C  CB  . SER   B 84  ? 1.2217 0.8346 0.7214 0.5268  -0.2069 -0.1046 93  SER   B CB  
926  O  OG  . SER   B 84  ? 1.2845 0.8470 0.7725 0.5193  -0.2343 -0.1262 93  SER   B OG  
927  N  N   . GLU   B 85  ? 1.1431 0.8437 0.6243 0.5876  -0.1595 -0.0664 94  GLU   B N   
928  C  CA  . GLU   B 85  ? 1.1065 0.8544 0.6068 0.5889  -0.1330 -0.0443 94  GLU   B CA  
929  C  C   . GLU   B 85  ? 1.0641 0.8209 0.6039 0.5488  -0.1295 -0.0438 94  GLU   B C   
930  O  O   . GLU   B 85  ? 1.0733 0.8057 0.6202 0.5297  -0.1486 -0.0621 94  GLU   B O   
931  C  CB  . GLU   B 85  ? 1.1384 0.9040 0.6089 0.6324  -0.1303 -0.0448 94  GLU   B CB  
932  C  CG  . GLU   B 85  ? 1.1954 0.9589 0.6249 0.6773  -0.1303 -0.0433 94  GLU   B CG  
933  C  CD  . GLU   B 85  ? 1.2121 1.0150 0.6260 0.7146  -0.1100 -0.0258 94  GLU   B CD  
934  O  OE1 . GLU   B 85  ? 1.1783 0.9996 0.6002 0.7147  -0.1038 -0.0223 94  GLU   B OE1 
935  O  OE2 . GLU   B 85  ? 1.2246 1.0411 0.6183 0.7445  -0.0995 -0.0141 94  GLU   B OE2 
936  N  N   . VAL   B 86  ? 1.0164 0.8076 0.5833 0.5350  -0.1052 -0.0228 95  VAL   B N   
937  C  CA  . VAL   B 86  ? 0.9823 0.7840 0.5856 0.4995  -0.0984 -0.0201 95  VAL   B CA  
938  C  C   . VAL   B 86  ? 0.9614 0.7963 0.5730 0.5107  -0.0792 -0.0057 95  VAL   B C   
939  O  O   . VAL   B 86  ? 0.9669 0.8193 0.5601 0.5418  -0.0679 0.0064  95  VAL   B O   
940  C  CB  . VAL   B 86  ? 0.9628 0.7667 0.5943 0.4640  -0.0880 -0.0090 95  VAL   B CB  
941  C  CG1 . VAL   B 86  ? 0.9772 0.7482 0.5967 0.4574  -0.1041 -0.0186 95  VAL   B CG1 
942  C  CG2 . VAL   B 86  ? 0.9483 0.7846 0.5900 0.4684  -0.0638 0.0146  95  VAL   B CG2 
943  N  N   . GLN   B 87  ? 0.9340 0.7774 0.5729 0.4864  -0.0741 -0.0052 96  GLN   B N   
944  C  CA  . GLN   B 87  ? 0.9091 0.7791 0.5567 0.4951  -0.0550 0.0099  96  GLN   B CA  
945  C  C   . GLN   B 87  ? 0.8734 0.7567 0.5563 0.4624  -0.0361 0.0245  96  GLN   B C   
946  O  O   . GLN   B 87  ? 0.8703 0.7436 0.5734 0.4318  -0.0418 0.0162  96  GLN   B O   
947  C  CB  . GLN   B 87  ? 0.9272 0.7966 0.5670 0.5081  -0.0662 -0.0030 96  GLN   B CB  
948  C  CG  . GLN   B 87  ? 0.9828 0.8563 0.5847 0.5534  -0.0706 -0.0045 96  GLN   B CG  
949  C  CD  . GLN   B 87  ? 1.0368 0.9092 0.6263 0.5697  -0.0866 -0.0206 96  GLN   B CD  
950  O  OE1 . GLN   B 87  ? 1.0294 0.9102 0.6410 0.5539  -0.0844 -0.0214 96  GLN   B OE1 
951  N  NE2 . GLN   B 87  ? 1.0637 0.9265 0.6159 0.6040  -0.1039 -0.0347 96  GLN   B NE2 
952  N  N   . LEU   B 88  ? 0.8436 0.7492 0.5341 0.4684  -0.0137 0.0462  97  LEU   B N   
953  C  CA  . LEU   B 88  ? 0.8153 0.7315 0.5382 0.4388  0.0033  0.0587  97  LEU   B CA  
954  C  C   . LEU   B 88  ? 0.8022 0.7247 0.5312 0.4437  0.0115  0.0622  97  LEU   B C   
955  O  O   . LEU   B 88  ? 0.8036 0.7384 0.5201 0.4702  0.0221  0.0747  97  LEU   B O   
956  C  CB  . LEU   B 88  ? 0.8025 0.7389 0.5354 0.4385  0.0223  0.0804  97  LEU   B CB  
957  C  CG  . LEU   B 88  ? 0.8016 0.7491 0.5671 0.4113  0.0406  0.0940  97  LEU   B CG  
958  C  CD1 . LEU   B 88  ? 0.8078 0.7417 0.5920 0.3761  0.0334  0.0815  97  LEU   B CD1 
959  C  CD2 . LEU   B 88  ? 0.7949 0.7649 0.5726 0.4111  0.0568  0.1146  97  LEU   B CD2 
960  N  N   . LEU   B 89  ? 0.7876 0.7024 0.5344 0.4205  0.0070  0.0519  98  LEU   B N   
961  C  CA  . LEU   B 89  ? 0.7722 0.6925 0.5263 0.4245  0.0150  0.0552  98  LEU   B CA  
962  C  C   . LEU   B 89  ? 0.7684 0.6960 0.5455 0.4061  0.0372  0.0735  98  LEU   B C   
963  O  O   . LEU   B 89  ? 0.7646 0.6871 0.5633 0.3770  0.0396  0.0695  98  LEU   B O   
964  C  CB  . LEU   B 89  ? 0.7612 0.6733 0.5267 0.4076  0.0008  0.0363  98  LEU   B CB  
965  C  CG  . LEU   B 89  ? 0.7573 0.6754 0.5336 0.4091  0.0074  0.0371  98  LEU   B CG  
966  C  CD1 . LEU   B 89  ? 0.7567 0.6835 0.5160 0.4417  0.0179  0.0506  98  LEU   B CD1 
967  C  CD2 . LEU   B 89  ? 0.7611 0.6775 0.5421 0.4037  -0.0120 0.0166  98  LEU   B CD2 
968  N  N   . ALA   B 90  ? 0.7618 0.7016 0.5343 0.4224  0.0531  0.0935  99  ALA   B N   
969  C  CA  . ALA   B 90  ? 0.7542 0.7008 0.5505 0.4041  0.0733  0.1116  99  ALA   B CA  
970  C  C   . ALA   B 90  ? 0.7574 0.6988 0.5640 0.4017  0.0848  0.1174  99  ALA   B C   
971  O  O   . ALA   B 90  ? 0.7748 0.7175 0.5650 0.4280  0.0863  0.1209  99  ALA   B O   
972  C  CB  . ALA   B 90  ? 0.7449 0.7094 0.5360 0.4224  0.0869  0.1327  99  ALA   B CB  
973  N  N   . VAL   B 91  ? 0.7429 0.6770 0.5739 0.3724  0.0923  0.1178  100 VAL   B N   
974  C  CA  . VAL   B 91  ? 0.7458 0.6707 0.5862 0.3701  0.1043  0.1238  100 VAL   B CA  
975  C  C   . VAL   B 91  ? 0.7484 0.6737 0.6095 0.3545  0.1235  0.1434  100 VAL   B C   
976  O  O   . VAL   B 91  ? 0.7457 0.6640 0.6265 0.3254  0.1248  0.1386  100 VAL   B O   
977  C  CB  . VAL   B 91  ? 0.7432 0.6566 0.5925 0.3515  0.0950  0.1045  100 VAL   B CB  
978  C  CG1 . VAL   B 91  ? 0.7476 0.6500 0.6042 0.3526  0.1075  0.1102  100 VAL   B CG1 
979  C  CG2 . VAL   B 91  ? 0.7458 0.6619 0.5802 0.3633  0.0751  0.0861  100 VAL   B CG2 
980  N  N   . PRO   B 92  ? 0.7474 0.6825 0.6048 0.3734  0.1382  0.1658  101 PRO   B N   
981  C  CA  . PRO   B 92  ? 0.7436 0.6821 0.6252 0.3561  0.1557  0.1856  101 PRO   B CA  
982  C  C   . PRO   B 92  ? 0.7560 0.6737 0.6525 0.3442  0.1692  0.1933  101 PRO   B C   
983  O  O   . PRO   B 92  ? 0.7701 0.6752 0.6533 0.3611  0.1708  0.1921  101 PRO   B O   
984  C  CB  . PRO   B 92  ? 0.7501 0.7102 0.6214 0.3829  0.1666  0.2079  101 PRO   B CB  
985  C  CG  . PRO   B 92  ? 0.7638 0.7287 0.6012 0.4155  0.1527  0.1964  101 PRO   B CG  
986  C  CD  . PRO   B 92  ? 0.7493 0.6950 0.5803 0.4111  0.1391  0.1744  101 PRO   B CD  
987  N  N   . PRO   B 93  ? 0.7506 0.6633 0.6745 0.3155  0.1778  0.2003  102 PRO   B N   
988  C  CA  . PRO   B 93  ? 0.7575 0.6438 0.6947 0.3033  0.1899  0.2062  102 PRO   B CA  
989  C  C   . PRO   B 93  ? 0.7753 0.6548 0.7029 0.3292  0.2068  0.2292  102 PRO   B C   
990  O  O   . PRO   B 93  ? 0.7690 0.6671 0.6960 0.3439  0.2182  0.2516  102 PRO   B O   
991  C  CB  . PRO   B 93  ? 0.7549 0.6425 0.7232 0.2709  0.1957  0.2130  102 PRO   B CB  
992  C  CG  . PRO   B 93  ? 0.7485 0.6604 0.7185 0.2611  0.1809  0.2006  102 PRO   B CG  
993  C  CD  . PRO   B 93  ? 0.7290 0.6589 0.6725 0.2930  0.1752  0.2012  102 PRO   B CD  
994  N  N   . GLY   B 94  ? 0.7922 0.6473 0.7104 0.3375  0.2086  0.2242  103 GLY   B N   
995  C  CA  . GLY   B 94  ? 0.8073 0.6517 0.7131 0.3641  0.2242  0.2452  103 GLY   B CA  
996  C  C   . GLY   B 94  ? 0.8182 0.6839 0.6949 0.4033  0.2224  0.2525  103 GLY   B C   
997  O  O   . GLY   B 94  ? 0.8213 0.6815 0.6846 0.4287  0.2360  0.2723  103 GLY   B O   
998  N  N   . GLU   B 95  ? 0.8277 0.7163 0.6926 0.4098  0.2060  0.2374  104 GLU   B N   
999  C  CA  . GLU   B 95  ? 0.8461 0.7539 0.6807 0.4473  0.2008  0.2399  104 GLU   B CA  
1000 C  C   . GLU   B 95  ? 0.8641 0.7729 0.6811 0.4558  0.1768  0.2101  104 GLU   B C   
1001 O  O   . GLU   B 95  ? 0.8653 0.7669 0.6957 0.4302  0.1647  0.1894  104 GLU   B O   
1002 C  CB  . GLU   B 95  ? 0.8599 0.7943 0.6943 0.4518  0.2033  0.2509  104 GLU   B CB  
1003 C  CG  . GLU   B 95  ? 0.9127 0.8531 0.7670 0.4459  0.2282  0.2834  104 GLU   B CG  
1004 C  CD  . GLU   B 95  ? 0.9882 0.9578 0.8538 0.4409  0.2317  0.2937  104 GLU   B CD  
1005 O  OE1 . GLU   B 95  ? 0.9846 0.9668 0.8412 0.4413  0.2139  0.2743  104 GLU   B OE1 
1006 O  OE2 . GLU   B 95  ? 1.0078 0.9883 0.8927 0.4366  0.2525  0.3220  104 GLU   B OE2 
1007 N  N   . ARG   B 96  ? 0.8783 0.7971 0.6660 0.4913  0.1695  0.2082  105 ARG   B N   
1008 C  CA  . ARG   B 96  ? 0.9019 0.8241 0.6750 0.5003  0.1456  0.1808  105 ARG   B CA  
1009 C  C   . ARG   B 96  ? 0.9081 0.8405 0.6804 0.4888  0.1269  0.1619  105 ARG   B C   
1010 O  O   . ARG   B 96  ? 0.9041 0.8466 0.6756 0.4888  0.1319  0.1721  105 ARG   B O   
1011 C  CB  . ARG   B 96  ? 0.9502 0.8814 0.6907 0.5437  0.1427  0.1853  105 ARG   B CB  
1012 C  CG  . ARG   B 96  ? 1.0396 0.9713 0.7701 0.5551  0.1229  0.1622  105 ARG   B CG  
1013 C  CD  . ARG   B 96  ? 1.1275 1.0622 0.8330 0.5944  0.1277  0.1733  105 ARG   B CD  
1014 N  NE  . ARG   B 96  ? 1.2132 1.1593 0.8912 0.6271  0.1366  0.1925  105 ARG   B NE  
1015 C  CZ  . ARG   B 96  ? 1.2693 1.2120 0.9386 0.6463  0.1606  0.2227  105 ARG   B CZ  
1016 N  NH1 . ARG   B 96  ? 1.2615 1.1855 0.9469 0.6357  0.1768  0.2362  105 ARG   B NH1 
1017 N  NH2 . ARG   B 96  ? 1.2840 1.2407 0.9274 0.6772  0.1690  0.2402  105 ARG   B NH2 
1018 N  N   . ALA   B 97  ? 0.9072 0.8377 0.6793 0.4806  0.1057  0.1356  106 ALA   B N   
1019 C  CA  . ALA   B 97  ? 0.9103 0.8454 0.6792 0.4714  0.0860  0.1166  106 ALA   B CA  
1020 C  C   . ALA   B 97  ? 0.9277 0.8738 0.6668 0.5043  0.0795  0.1191  106 ALA   B C   
1021 O  O   . ALA   B 97  ? 0.9402 0.8914 0.6567 0.5363  0.0778  0.1216  106 ALA   B O   
1022 C  CB  . ALA   B 97  ? 0.9054 0.8378 0.6782 0.4630  0.0660  0.0916  106 ALA   B CB  
1023 N  N   . LYS   B 98  ? 0.9325 0.8825 0.6692 0.4990  0.0756  0.1182  107 LYS   B N   
1024 C  CA  . LYS   B 98  ? 0.9439 0.9034 0.6504 0.5317  0.0705  0.1205  107 LYS   B CA  
1025 C  C   . LYS   B 98  ? 0.9424 0.8968 0.6415 0.5252  0.0500  0.1010  107 LYS   B C   
1026 O  O   . LYS   B 98  ? 0.9452 0.8976 0.6630 0.4989  0.0524  0.1020  107 LYS   B O   
1027 C  CB  . LYS   B 98  ? 0.9758 0.9489 0.6854 0.5397  0.0950  0.1496  107 LYS   B CB  
1028 C  CG  . LYS   B 98  ? 1.0514 1.0385 0.7267 0.5831  0.0984  0.1603  107 LYS   B CG  
1029 C  CD  . LYS   B 98  ? 1.1029 1.1077 0.7868 0.5898  0.1269  0.1937  107 LYS   B CD  
1030 C  CE  . LYS   B 98  ? 1.1268 1.1380 0.8431 0.5566  0.1350  0.2013  107 LYS   B CE  
1031 N  NZ  . LYS   B 98  ? 1.1388 1.1757 0.8524 0.5740  0.1519  0.2252  107 LYS   B NZ  
1032 N  N   . ASN   B 99  ? 0.9435 0.8943 0.6138 0.5501  0.0294  0.0836  108 ASN   B N   
1033 C  CA  . ASN   B 99  ? 0.9445 0.8846 0.6046 0.5463  0.0092  0.0651  108 ASN   B CA  
1034 C  C   . ASN   B 99  ? 0.9540 0.9029 0.5919 0.5715  0.0159  0.0769  108 ASN   B C   
1035 O  O   . ASN   B 99  ? 0.9643 0.9224 0.5736 0.6087  0.0190  0.0833  108 ASN   B O   
1036 C  CB  . ASN   B 99  ? 0.9525 0.8813 0.5942 0.5584  -0.0187 0.0383  108 ASN   B CB  
1037 C  CG  . ASN   B 99  ? 0.9650 0.8872 0.6327 0.5289  -0.0292 0.0232  108 ASN   B CG  
1038 O  OD1 . ASN   B 99  ? 0.9695 0.8993 0.6553 0.5200  -0.0169 0.0315  108 ASN   B OD1 
1039 N  ND2 . ASN   B 99  ? 0.9583 0.8660 0.6284 0.5141  -0.0520 0.0012  108 ASN   B ND2 
1040 N  N   . ILE   B 100 ? 0.9478 0.8961 0.5981 0.5532  0.0189  0.0807  109 ILE   B N   
1041 C  CA  . ILE   B 100 ? 0.9536 0.9138 0.5864 0.5762  0.0259  0.0924  109 ILE   B CA  
1042 C  C   . ILE   B 100 ? 0.9659 0.9076 0.5831 0.5765  0.0042  0.0725  109 ILE   B C   
1043 O  O   . ILE   B 100 ? 0.9645 0.8987 0.6022 0.5466  0.0013  0.0693  109 ILE   B O   
1044 C  CB  . ILE   B 100 ? 0.9462 0.9269 0.6084 0.5577  0.0502  0.1177  109 ILE   B CB  
1045 C  CG1 . ILE   B 100 ? 0.9517 0.9433 0.6345 0.5499  0.0716  0.1371  109 ILE   B CG1 
1046 C  CG2 . ILE   B 100 ? 0.9524 0.9528 0.5985 0.5848  0.0591  0.1320  109 ILE   B CG2 
1047 C  CD1 . ILE   B 100 ? 0.9745 0.9781 0.6319 0.5892  0.0820  0.1506  109 ILE   B CD1 
1048 N  N   . GLN   B 101 ? 0.9818 0.9147 0.5609 0.6115  -0.0112 0.0594  110 GLN   B N   
1049 C  CA  . GLN   B 101 ? 0.9984 0.9070 0.5588 0.6146  -0.0334 0.0392  110 GLN   B CA  
1050 C  C   . GLN   B 101 ? 0.9968 0.9164 0.5515 0.6252  -0.0232 0.0528  110 GLN   B C   
1051 O  O   . GLN   B 101 ? 0.9904 0.9358 0.5343 0.6528  -0.0056 0.0719  110 GLN   B O   
1052 C  CB  . GLN   B 101 ? 1.0379 0.9291 0.5587 0.6479  -0.0564 0.0170  110 GLN   B CB  
1053 C  CG  . GLN   B 101 ? 1.0900 0.9458 0.5977 0.6411  -0.0843 -0.0091 110 GLN   B CG  
1054 C  CD  . GLN   B 101 ? 1.1388 0.9770 0.6105 0.6710  -0.1089 -0.0332 110 GLN   B CD  
1055 O  OE1 . GLN   B 101 ? 1.1291 0.9735 0.6028 0.6735  -0.1144 -0.0399 110 GLN   B OE1 
1056 N  NE2 . GLN   B 101 ? 1.1640 0.9794 0.6012 0.6954  -0.1253 -0.0476 110 GLN   B NE2 
1057 N  N   . THR   B 102 ? 0.9989 0.9016 0.5631 0.6029  -0.0329 0.0449  111 THR   B N   
1058 C  CA  . THR   B 102 ? 0.9932 0.9066 0.5539 0.6117  -0.0254 0.0564  111 THR   B CA  
1059 C  C   . THR   B 102 ? 1.0052 0.8836 0.5531 0.6044  -0.0478 0.0370  111 THR   B C   
1060 O  O   . THR   B 102 ? 1.0176 0.8671 0.5704 0.5823  -0.0653 0.0184  111 THR   B O   
1061 C  CB  . THR   B 102 ? 0.9922 0.9347 0.5941 0.5823  -0.0026 0.0796  111 THR   B CB  
1062 O  OG1 . THR   B 102 ? 1.0105 0.9740 0.6106 0.5959  0.0070  0.0940  111 THR   B OG1 
1063 C  CG2 . THR   B 102 ? 0.9899 0.9165 0.6219 0.5366  -0.0089 0.0715  111 THR   B CG2 
1064 N  N   . LEU   B 103 ? 1.0018 0.8823 0.5332 0.6240  -0.0471 0.0418  112 LEU   B N   
1065 C  CA  . LEU   B 103 ? 1.0164 0.8617 0.5366 0.6163  -0.0661 0.0269  112 LEU   B CA  
1066 C  C   . LEU   B 103 ? 1.0022 0.8668 0.5538 0.5891  -0.0529 0.0437  112 LEU   B C   
1067 O  O   . LEU   B 103 ? 0.9918 0.8923 0.5500 0.6025  -0.0353 0.0635  112 LEU   B O   
1068 C  CB  . LEU   B 103 ? 1.0356 0.8652 0.5117 0.6598  -0.0769 0.0187  112 LEU   B CB  
1069 C  CG  . LEU   B 103 ? 1.0629 0.8488 0.5264 0.6511  -0.0973 0.0033  112 LEU   B CG  
1070 C  CD1 . LEU   B 103 ? 1.0907 0.8287 0.5334 0.6503  -0.1244 -0.0248 112 LEU   B CD1 
1071 C  CD2 . LEU   B 103 ? 1.0758 0.8632 0.5113 0.6865  -0.0962 0.0084  112 LEU   B CD2 
1072 N  N   . PRO   B 104 ? 0.9986 0.8422 0.5699 0.5516  -0.0613 0.0365  113 PRO   B N   
1073 C  CA  . PRO   B 104 ? 0.9856 0.8482 0.5849 0.5261  -0.0501 0.0511  113 PRO   B CA  
1074 C  C   . PRO   B 104 ? 1.0054 0.8666 0.5891 0.5431  -0.0531 0.0558  113 PRO   B C   
1075 O  O   . PRO   B 104 ? 1.0299 0.8591 0.5798 0.5669  -0.0690 0.0431  113 PRO   B O   
1076 C  CB  . PRO   B 104 ? 0.9931 0.8315 0.6121 0.4852  -0.0589 0.0408  113 PRO   B CB  
1077 C  CG  . PRO   B 104 ? 1.0105 0.8257 0.6195 0.4873  -0.0716 0.0237  113 PRO   B CG  
1078 C  CD  . PRO   B 104 ? 1.0034 0.8095 0.5751 0.5299  -0.0802 0.0160  113 PRO   B CD  
1079 N  N   . GLY   B 105 ? 0.9861 0.8825 0.5956 0.5304  -0.0383 0.0738  114 GLY   B N   
1080 C  CA  . GLY   B 105 ? 0.9875 0.8924 0.5916 0.5406  -0.0388 0.0815  114 GLY   B CA  
1081 C  C   . GLY   B 105 ? 0.9921 0.8735 0.6065 0.5079  -0.0483 0.0763  114 GLY   B C   
1082 O  O   . GLY   B 105 ? 1.0077 0.8544 0.6217 0.4861  -0.0591 0.0626  114 GLY   B O   
1083 N  N   . ILE   B 106 ? 0.9728 0.8751 0.5966 0.5052  -0.0443 0.0878  115 ILE   B N   
1084 C  CA  . ILE   B 106 ? 0.9749 0.8567 0.6037 0.4791  -0.0527 0.0850  115 ILE   B CA  
1085 C  C   . ILE   B 106 ? 0.9428 0.8685 0.6040 0.4587  -0.0410 0.1001  115 ILE   B C   
1086 O  O   . ILE   B 106 ? 0.9245 0.8933 0.5963 0.4746  -0.0307 0.1139  115 ILE   B O   
1087 C  CB  . ILE   B 106 ? 1.0077 0.8555 0.6010 0.5045  -0.0673 0.0798  115 ILE   B CB  
1088 C  CG1 . ILE   B 106 ? 1.0545 0.8498 0.6143 0.5214  -0.0833 0.0612  115 ILE   B CG1 
1089 C  CG2 . ILE   B 106 ? 1.0206 0.8535 0.6170 0.4831  -0.0734 0.0822  115 ILE   B CG2 
1090 C  CD1 . ILE   B 106 ? 1.0841 0.8413 0.6498 0.4896  -0.0933 0.0482  115 ILE   B CD1 
1091 N  N   . PHE   B 107 ? 0.9357 0.8510 0.6122 0.4240  -0.0435 0.0972  116 PHE   B N   
1092 C  CA  . PHE   B 107 ? 0.9149 0.8626 0.6165 0.4028  -0.0376 0.1072  116 PHE   B CA  
1093 C  C   . PHE   B 107 ? 0.9367 0.8557 0.6167 0.4041  -0.0503 0.1046  116 PHE   B C   
1094 O  O   . PHE   B 107 ? 0.9516 0.8289 0.6203 0.3889  -0.0588 0.0948  116 PHE   B O   
1095 C  CB  . PHE   B 107 ? 0.8970 0.8459 0.6243 0.3648  -0.0324 0.1034  116 PHE   B CB  
1096 C  CG  . PHE   B 107 ? 0.8677 0.8555 0.6263 0.3546  -0.0175 0.1112  116 PHE   B CG  
1097 C  CD1 . PHE   B 107 ? 0.8603 0.8772 0.6233 0.3785  -0.0080 0.1213  116 PHE   B CD1 
1098 C  CD2 . PHE   B 107 ? 0.8586 0.8522 0.6413 0.3221  -0.0123 0.1091  116 PHE   B CD2 
1099 C  CE1 . PHE   B 107 ? 0.8458 0.8951 0.6387 0.3678  0.0067  0.1305  116 PHE   B CE1 
1100 C  CE2 . PHE   B 107 ? 0.8461 0.8697 0.6572 0.3123  0.0009  0.1163  116 PHE   B CE2 
1101 C  CZ  . PHE   B 107 ? 0.8338 0.8842 0.6507 0.3341  0.0105  0.1277  116 PHE   B CZ  
1102 N  N   . LYS   B 108 ? 0.9382 0.8784 0.6120 0.4236  -0.0515 0.1140  117 LYS   B N   
1103 C  CA  . LYS   B 108 ? 0.9673 0.8808 0.6190 0.4273  -0.0629 0.1139  117 LYS   B CA  
1104 C  C   . LYS   B 108 ? 0.9540 0.8950 0.6278 0.4006  -0.0603 0.1203  117 LYS   B C   
1105 O  O   . LYS   B 108 ? 0.9294 0.9219 0.6264 0.4015  -0.0535 0.1299  117 LYS   B O   
1106 C  CB  . LYS   B 108 ? 1.0128 0.9362 0.6435 0.4671  -0.0662 0.1208  117 LYS   B CB  
1107 C  CG  . LYS   B 108 ? 1.1045 0.9957 0.7042 0.5004  -0.0714 0.1129  117 LYS   B CG  
1108 C  CD  . LYS   B 108 ? 1.1916 1.0662 0.7592 0.5345  -0.0805 0.1159  117 LYS   B CD  
1109 C  CE  . LYS   B 108 ? 1.2701 1.1147 0.8029 0.5734  -0.0866 0.1075  117 LYS   B CE  
1110 N  NZ  . LYS   B 108 ? 1.3040 1.1545 0.8123 0.6134  -0.0901 0.1145  117 LYS   B NZ  
1111 N  N   . THR   B 109 ? 0.9681 0.8766 0.6349 0.3772  -0.0661 0.1153  118 THR   B N   
1112 C  CA  . THR   B 109 ? 0.9607 0.8902 0.6418 0.3532  -0.0651 0.1196  118 THR   B CA  
1113 C  C   . THR   B 109 ? 0.9838 0.8837 0.6368 0.3593  -0.0751 0.1232  118 THR   B C   
1114 O  O   . THR   B 109 ? 1.0113 0.8660 0.6359 0.3759  -0.0826 0.1208  118 THR   B O   
1115 C  CB  . THR   B 109 ? 0.9736 0.8963 0.6729 0.3182  -0.0597 0.1121  118 THR   B CB  
1116 O  OG1 . THR   B 109 ? 1.0157 0.8871 0.6958 0.3101  -0.0653 0.1052  118 THR   B OG1 
1117 C  CG2 . THR   B 109 ? 0.9585 0.9032 0.6826 0.3126  -0.0498 0.1093  118 THR   B CG2 
1118 N  N   . LYS   B 110 ? 0.9729 0.8952 0.6321 0.3459  -0.0759 0.1285  119 LYS   B N   
1119 C  CA  . LYS   B 110 ? 0.9990 0.8944 0.6307 0.3509  -0.0841 0.1341  119 LYS   B CA  
1120 C  C   . LYS   B 110 ? 1.0292 0.8674 0.6439 0.3334  -0.0860 0.1294  119 LYS   B C   
1121 O  O   . LYS   B 110 ? 1.0522 0.8545 0.6397 0.3407  -0.0924 0.1351  119 LYS   B O   
1122 C  CB  . LYS   B 110 ? 0.9965 0.9332 0.6390 0.3400  -0.0847 0.1398  119 LYS   B CB  
1123 C  CG  . LYS   B 110 ? 1.0292 0.9753 0.6910 0.3049  -0.0792 0.1333  119 LYS   B CG  
1124 C  CD  . LYS   B 110 ? 1.0575 1.0506 0.7325 0.2963  -0.0815 0.1358  119 LYS   B CD  
1125 C  CE  . LYS   B 110 ? 1.1108 1.0922 0.7790 0.2719  -0.0810 0.1324  119 LYS   B CE  
1126 N  NZ  . LYS   B 110 ? 1.1392 1.1152 0.8271 0.2457  -0.0724 0.1220  119 LYS   B NZ  
1127 N  N   . ASP   B 111 ? 1.0218 0.8527 0.6537 0.3108  -0.0802 0.1204  120 ASP   B N   
1128 C  CA  . ASP   B 111 ? 1.0429 0.8289 0.6669 0.2917  -0.0807 0.1161  120 ASP   B CA  
1129 C  C   . ASP   B 111 ? 1.0594 0.8085 0.6779 0.2987  -0.0846 0.1073  120 ASP   B C   
1130 O  O   . ASP   B 111 ? 1.0762 0.7950 0.6963 0.2796  -0.0849 0.1025  120 ASP   B O   
1131 C  CB  . ASP   B 111 ? 1.0481 0.8541 0.6956 0.2605  -0.0719 0.1117  120 ASP   B CB  
1132 C  CG  . ASP   B 111 ? 1.1005 0.9335 0.7482 0.2510  -0.0703 0.1179  120 ASP   B CG  
1133 O  OD1 . ASP   B 111 ? 1.1213 0.9406 0.7455 0.2612  -0.0758 0.1270  120 ASP   B OD1 
1134 O  OD2 . ASP   B 111 ? 1.1122 0.9785 0.7817 0.2343  -0.0641 0.1133  120 ASP   B OD2 
1135 N  N   . GLY   B 112 ? 1.0467 0.8015 0.6597 0.3257  -0.0877 0.1049  121 GLY   B N   
1136 C  CA  . GLY   B 112 ? 1.0491 0.7707 0.6533 0.3364  -0.0933 0.0946  121 GLY   B CA  
1137 C  C   . GLY   B 112 ? 1.0149 0.7682 0.6347 0.3472  -0.0876 0.0894  121 GLY   B C   
1138 O  O   . GLY   B 112 ? 0.9880 0.7888 0.6308 0.3414  -0.0778 0.0942  121 GLY   B O   
1139 N  N   . ASP   B 113 ? 1.0160 0.7421 0.6229 0.3633  -0.0941 0.0795  122 ASP   B N   
1140 C  CA  . ASP   B 113 ? 0.9974 0.7501 0.6138 0.3778  -0.0886 0.0755  122 ASP   B CA  
1141 C  C   . ASP   B 113 ? 0.9829 0.7358 0.6193 0.3556  -0.0847 0.0665  122 ASP   B C   
1142 O  O   . ASP   B 113 ? 0.9915 0.7109 0.6268 0.3372  -0.0912 0.0587  122 ASP   B O   
1143 C  CB  . ASP   B 113 ? 1.0329 0.7621 0.6197 0.4151  -0.0979 0.0697  122 ASP   B CB  
1144 C  CG  . ASP   B 113 ? 1.1025 0.8366 0.6688 0.4439  -0.1005 0.0788  122 ASP   B CG  
1145 O  OD1 . ASP   B 113 ? 1.0787 0.8421 0.6568 0.4356  -0.0948 0.0906  122 ASP   B OD1 
1146 O  OD2 . ASP   B 113 ? 1.1647 0.8740 0.7021 0.4765  -0.1089 0.0733  122 ASP   B OD2 
1147 N  N   . ILE   B 114 ? 0.9559 0.7479 0.6114 0.3580  -0.0736 0.0689  123 ILE   B N   
1148 C  CA  . ILE   B 114 ? 0.9512 0.7484 0.6255 0.3415  -0.0684 0.0620  123 ILE   B CA  
1149 C  C   . ILE   B 114 ? 0.9402 0.7503 0.6087 0.3687  -0.0657 0.0601  123 ILE   B C   
1150 O  O   . ILE   B 114 ? 0.9342 0.7692 0.5977 0.3924  -0.0606 0.0690  123 ILE   B O   
1151 C  CB  . ILE   B 114 ? 0.9417 0.7750 0.6472 0.3146  -0.0547 0.0688  123 ILE   B CB  
1152 C  CG1 . ILE   B 114 ? 0.9616 0.7988 0.6699 0.2972  -0.0548 0.0752  123 ILE   B CG1 
1153 C  CG2 . ILE   B 114 ? 0.9427 0.7712 0.6646 0.2936  -0.0511 0.0608  123 ILE   B CG2 
1154 C  CD1 . ILE   B 114 ? 0.9591 0.8362 0.6947 0.2782  -0.0430 0.0811  123 ILE   B CD1 
1155 N  N   . GLY   B 115 ? 0.9319 0.7299 0.6026 0.3655  -0.0681 0.0498  124 GLY   B N   
1156 C  CA  . GLY   B 115 ? 0.9253 0.7383 0.5904 0.3908  -0.0641 0.0489  124 GLY   B CA  
1157 C  C   . GLY   B 115 ? 0.8944 0.7541 0.5850 0.3864  -0.0451 0.0632  124 GLY   B C   
1158 O  O   . GLY   B 115 ? 0.8823 0.7579 0.5972 0.3590  -0.0373 0.0688  124 GLY   B O   
1159 N  N   . ALA   B 116 ? 0.8795 0.7607 0.5645 0.4135  -0.0376 0.0693  125 ALA   B N   
1160 C  CA  . ALA   B 116 ? 0.8540 0.7784 0.5651 0.4092  -0.0187 0.0851  125 ALA   B CA  
1161 C  C   . ALA   B 116 ? 0.8417 0.7801 0.5471 0.4334  -0.0100 0.0893  125 ALA   B C   
1162 O  O   . ALA   B 116 ? 0.8383 0.7749 0.5182 0.4668  -0.0134 0.0888  125 ALA   B O   
1163 C  CB  . ALA   B 116 ? 0.8407 0.7958 0.5600 0.4146  -0.0125 0.0994  125 ALA   B CB  
1164 N  N   . VAL   B 117 ? 0.8422 0.7933 0.5693 0.4181  0.0014  0.0937  126 VAL   B N   
1165 C  CA  A VAL   B 117 ? 0.8486 0.8126 0.5702 0.4406  0.0111  0.0999  126 VAL   B CA  
1166 C  CA  B VAL   B 117 ? 0.8461 0.8100 0.5684 0.4397  0.0112  0.0998  126 VAL   B CA  
1167 C  C   . VAL   B 117 ? 0.8336 0.8403 0.5775 0.4442  0.0322  0.1231  126 VAL   B C   
1168 O  O   . VAL   B 117 ? 0.8137 0.8368 0.5891 0.4160  0.0414  0.1315  126 VAL   B O   
1169 C  CB  A VAL   B 117 ? 0.8630 0.8100 0.5886 0.4287  0.0091  0.0899  126 VAL   B CB  
1170 C  CB  B VAL   B 117 ? 0.8546 0.8016 0.5840 0.4237  0.0094  0.0899  126 VAL   B CB  
1171 C  CG1 A VAL   B 117 ? 0.8885 0.7994 0.5881 0.4369  -0.0122 0.0685  126 VAL   B CG1 
1172 C  CG1 B VAL   B 117 ? 0.8511 0.8175 0.5859 0.4371  0.0252  0.1021  126 VAL   B CG1 
1173 C  CG2 A VAL   B 117 ? 0.8619 0.8101 0.6186 0.3897  0.0146  0.0903  126 VAL   B CG2 
1174 C  CG2 B VAL   B 117 ? 0.8792 0.7904 0.5832 0.4315  -0.0114 0.0686  126 VAL   B CG2 
1175 N  N   . ALA   B 118 ? 0.8443 0.8700 0.5715 0.4799  0.0393  0.1337  127 ALA   B N   
1176 C  CA  . ALA   B 118 ? 0.8380 0.9081 0.5883 0.4847  0.0602  0.1582  127 ALA   B CA  
1177 C  C   . ALA   B 118 ? 0.8465 0.9290 0.6016 0.4945  0.0765  0.1710  127 ALA   B C   
1178 O  O   . ALA   B 118 ? 0.8593 0.9566 0.5947 0.5296  0.0843  0.1807  127 ALA   B O   
1179 C  CB  . ALA   B 118 ? 0.8393 0.9314 0.5736 0.5166  0.0612  0.1665  127 ALA   B CB  
1180 N  N   . LEU   B 119 ? 0.8400 0.9147 0.6189 0.4651  0.0819  0.1711  128 LEU   B N   
1181 C  CA  . LEU   B 119 ? 0.8326 0.9138 0.6178 0.4705  0.0977  0.1838  128 LEU   B CA  
1182 C  C   . LEU   B 119 ? 0.8122 0.9099 0.6407 0.4364  0.1130  0.1987  128 LEU   B C   
1183 O  O   . LEU   B 119 ? 0.8081 0.8969 0.6556 0.4043  0.1056  0.1890  128 LEU   B O   
1184 C  CB  . LEU   B 119 ? 0.8538 0.9002 0.6199 0.4713  0.0857  0.1648  128 LEU   B CB  
1185 C  CG  . LEU   B 119 ? 0.8911 0.9184 0.6150 0.5041  0.0684  0.1479  128 LEU   B CG  
1186 C  CD1 . LEU   B 119 ? 0.9073 0.9045 0.6203 0.4986  0.0544  0.1280  128 LEU   B CD1 
1187 C  CD2 . LEU   B 119 ? 0.9004 0.9487 0.6010 0.5465  0.0794  0.1625  128 LEU   B CD2 
1188 N  N   . ASP   B 120 ? 0.8003 0.9213 0.6440 0.4436  0.1342  0.2224  129 ASP   B N   
1189 C  CA  . ASP   B 120 ? 0.7859 0.9196 0.6718 0.4111  0.1485  0.2370  129 ASP   B CA  
1190 C  C   . ASP   B 120 ? 0.7866 0.8957 0.6775 0.3998  0.1554  0.2370  129 ASP   B C   
1191 O  O   . ASP   B 120 ? 0.7962 0.9048 0.6716 0.4245  0.1660  0.2482  129 ASP   B O   
1192 C  CB  . ASP   B 120 ? 0.7895 0.9664 0.6968 0.4210  0.1692  0.2666  129 ASP   B CB  
1193 C  CG  . ASP   B 120 ? 0.8528 1.0613 0.7603 0.4332  0.1652  0.2700  129 ASP   B CG  
1194 O  OD1 . ASP   B 120 ? 0.8745 1.0688 0.7686 0.4288  0.1458  0.2495  129 ASP   B OD1 
1195 O  OD2 . ASP   B 120 ? 0.8733 1.1220 0.7948 0.4480  0.1822  0.2945  129 ASP   B OD2 
1196 N  N   . TYR   B 121 ? 0.7797 0.8702 0.6917 0.3643  0.1505  0.2261  130 TYR   B N   
1197 C  CA  . TYR   B 121 ? 0.7883 0.8530 0.7065 0.3513  0.1561  0.2241  130 TYR   B CA  
1198 C  C   . TYR   B 121 ? 0.7646 0.8256 0.7195 0.3115  0.1602  0.2250  130 TYR   B C   
1199 O  O   . TYR   B 121 ? 0.7609 0.8297 0.7283 0.2914  0.1502  0.2157  130 TYR   B O   
1200 C  CB  . TYR   B 121 ? 0.8170 0.8509 0.7092 0.3548  0.1385  0.1983  130 TYR   B CB  
1201 C  CG  . TYR   B 121 ? 0.8511 0.8807 0.7091 0.3923  0.1358  0.1971  130 TYR   B CG  
1202 C  CD1 . TYR   B 121 ? 0.8701 0.8909 0.7211 0.4064  0.1462  0.2056  130 TYR   B CD1 
1203 C  CD2 . TYR   B 121 ? 0.8757 0.9100 0.7068 0.4157  0.1226  0.1877  130 TYR   B CD2 
1204 C  CE1 . TYR   B 121 ? 0.8986 0.9185 0.7164 0.4431  0.1428  0.2044  130 TYR   B CE1 
1205 C  CE2 . TYR   B 121 ? 0.9014 0.9324 0.6994 0.4519  0.1189  0.1855  130 TYR   B CE2 
1206 C  CZ  . TYR   B 121 ? 0.9214 0.9468 0.7127 0.4655  0.1286  0.1934  130 TYR   B CZ  
1207 O  OH  . TYR   B 121 ? 0.9593 0.9824 0.7156 0.5025  0.1229  0.1894  130 TYR   B OH  
1208 N  N   . PRO   B 122 ? 0.7479 0.7935 0.7177 0.3004  0.1731  0.2341  131 PRO   B N   
1209 C  CA  . PRO   B 122 ? 0.7249 0.7614 0.7269 0.2627  0.1745  0.2314  131 PRO   B CA  
1210 C  C   . PRO   B 122 ? 0.7121 0.7305 0.7090 0.2420  0.1556  0.2035  131 PRO   B C   
1211 O  O   . PRO   B 122 ? 0.7295 0.7327 0.6999 0.2544  0.1443  0.1870  131 PRO   B O   
1212 C  CB  . PRO   B 122 ? 0.7416 0.7530 0.7480 0.2618  0.1887  0.2410  131 PRO   B CB  
1213 C  CG  . PRO   B 122 ? 0.7559 0.7757 0.7412 0.2979  0.1999  0.2583  131 PRO   B CG  
1214 C  CD  . PRO   B 122 ? 0.7480 0.7814 0.7037 0.3228  0.1859  0.2465  131 PRO   B CD  
1215 N  N   . ALA   B 123 ? 0.6750 0.6956 0.6976 0.2107  0.1523  0.1986  132 ALA   B N   
1216 C  CA  . ALA   B 123 ? 0.6611 0.6678 0.6789 0.1912  0.1360  0.1743  132 ALA   B CA  
1217 C  C   . ALA   B 123 ? 0.6610 0.6336 0.6599 0.1918  0.1316  0.1570  132 ALA   B C   
1218 O  O   . ALA   B 123 ? 0.6655 0.6312 0.6494 0.1887  0.1181  0.1390  132 ALA   B O   
1219 C  CB  . ALA   B 123 ? 0.6459 0.6589 0.6939 0.1591  0.1346  0.1728  132 ALA   B CB  
1220 N  N   . GLY   B 124 ? 0.6527 0.6065 0.6519 0.1983  0.1434  0.1643  133 GLY   B N   
1221 C  CA  . GLY   B 124 ? 0.6507 0.5768 0.6334 0.2029  0.1407  0.1501  133 GLY   B CA  
1222 C  C   . GLY   B 124 ? 0.6489 0.5765 0.6041 0.2286  0.1324  0.1427  133 GLY   B C   
1223 O  O   . GLY   B 124 ? 0.6482 0.5588 0.5915 0.2340  0.1290  0.1311  133 GLY   B O   
1224 N  N   . THR   B 125 ? 0.6470 0.5955 0.5921 0.2457  0.1285  0.1489  134 THR   B N   
1225 C  CA  . THR   B 125 ? 0.6597 0.6087 0.5783 0.2694  0.1176  0.1401  134 THR   B CA  
1226 C  C   . THR   B 125 ? 0.6527 0.5993 0.5643 0.2569  0.1002  0.1208  134 THR   B C   
1227 O  O   . THR   B 125 ? 0.6619 0.6024 0.5546 0.2701  0.0890  0.1096  134 THR   B O   
1228 C  CB  . THR   B 125 ? 0.6789 0.6480 0.5861 0.2978  0.1226  0.1563  134 THR   B CB  
1229 O  OG1 . THR   B 125 ? 0.6870 0.6598 0.6040 0.3056  0.1413  0.1776  134 THR   B OG1 
1230 C  CG2 . THR   B 125 ? 0.6938 0.6594 0.5708 0.3259  0.1111  0.1466  134 THR   B CG2 
1231 N  N   . SER   B 126 ? 0.6354 0.5862 0.5620 0.2317  0.0974  0.1171  135 SER   B N   
1232 C  CA  . SER   B 126 ? 0.6410 0.5886 0.5595 0.2203  0.0827  0.1016  135 SER   B CA  
1233 C  C   . SER   B 126 ? 0.6392 0.5678 0.5491 0.2162  0.0767  0.0857  135 SER   B C   
1234 O  O   . SER   B 126 ? 0.6359 0.5537 0.5540 0.2079  0.0837  0.0831  135 SER   B O   
1235 C  CB  . SER   B 126 ? 0.6583 0.6133 0.5930 0.1949  0.0812  0.0999  135 SER   B CB  
1236 O  OG  . SER   B 126 ? 0.6946 0.6609 0.6518 0.1854  0.0921  0.1127  135 SER   B OG  
1237 N  N   . GLY   B 127 ? 0.6347 0.5595 0.5289 0.2228  0.0639  0.0758  136 GLY   B N   
1238 C  CA  . GLY   B 127 ? 0.6403 0.5524 0.5287 0.2198  0.0571  0.0619  136 GLY   B CA  
1239 C  C   . GLY   B 127 ? 0.6527 0.5625 0.5269 0.2433  0.0503  0.0590  136 GLY   B C   
1240 O  O   . GLY   B 127 ? 0.6664 0.5693 0.5363 0.2415  0.0405  0.0469  136 GLY   B O   
1241 N  N   . SER   B 128 ? 0.6432 0.5601 0.5102 0.2658  0.0552  0.0701  137 SER   B N   
1242 C  CA  . SER   B 128 ? 0.6468 0.5628 0.4962 0.2925  0.0481  0.0675  137 SER   B CA  
1243 C  C   . SER   B 128 ? 0.6463 0.5549 0.4811 0.2956  0.0296  0.0547  137 SER   B C   
1244 O  O   . SER   B 128 ? 0.6398 0.5491 0.4696 0.2931  0.0255  0.0568  137 SER   B O   
1245 C  CB  . SER   B 128 ? 0.6610 0.5885 0.5027 0.3163  0.0579  0.0839  137 SER   B CB  
1246 O  OG  . SER   B 128 ? 0.6894 0.6189 0.5426 0.3168  0.0742  0.0960  137 SER   B OG  
1247 N  N   . PRO   B 129 ? 0.6543 0.5555 0.4834 0.3007  0.0179  0.0416  138 PRO   B N   
1248 C  CA  . PRO   B 129 ? 0.6733 0.5631 0.4911 0.3006  -0.0006 0.0289  138 PRO   B CA  
1249 C  C   . PRO   B 129 ? 0.7037 0.5900 0.4969 0.3281  -0.0099 0.0289  138 PRO   B C   
1250 O  O   . PRO   B 129 ? 0.7101 0.6050 0.4922 0.3529  -0.0044 0.0358  138 PRO   B O   
1251 C  CB  . PRO   B 129 ? 0.6665 0.5538 0.4909 0.2971  -0.0095 0.0156  138 PRO   B CB  
1252 C  CG  . PRO   B 129 ? 0.6564 0.5540 0.4822 0.3130  0.0011  0.0218  138 PRO   B CG  
1253 C  CD  . PRO   B 129 ? 0.6343 0.5374 0.4692 0.3057  0.0203  0.0374  138 PRO   B CD  
1254 N  N   . ILE   B 130 ? 0.7239 0.5962 0.5069 0.3248  -0.0234 0.0215  139 ILE   B N   
1255 C  CA  . ILE   B 130 ? 0.7487 0.6121 0.5054 0.3508  -0.0349 0.0181  139 ILE   B CA  
1256 C  C   . ILE   B 130 ? 0.7790 0.6219 0.5282 0.3496  -0.0566 -0.0012 139 ILE   B C   
1257 O  O   . ILE   B 130 ? 0.7712 0.6035 0.5342 0.3238  -0.0627 -0.0077 139 ILE   B O   
1258 C  CB  . ILE   B 130 ? 0.7567 0.6179 0.5077 0.3482  -0.0332 0.0258  139 ILE   B CB  
1259 C  CG1 . ILE   B 130 ? 0.7511 0.6369 0.5152 0.3464  -0.0129 0.0445  139 ILE   B CG1 
1260 C  CG2 . ILE   B 130 ? 0.7767 0.6238 0.4978 0.3759  -0.0469 0.0199  139 ILE   B CG2 
1261 C  CD1 . ILE   B 130 ? 0.7552 0.6436 0.5220 0.3351  -0.0118 0.0512  139 ILE   B CD1 
1262 N  N   . LEU   B 131 ? 0.8112 0.6497 0.5398 0.3769  -0.0684 -0.0102 140 LEU   B N   
1263 C  CA  . LEU   B 131 ? 0.8478 0.6694 0.5729 0.3754  -0.0908 -0.0302 140 LEU   B CA  
1264 C  C   . LEU   B 131 ? 0.8960 0.6926 0.5918 0.3952  -0.1110 -0.0428 140 LEU   B C   
1265 O  O   . LEU   B 131 ? 0.9161 0.7134 0.5873 0.4227  -0.1077 -0.0370 140 LEU   B O   
1266 C  CB  . LEU   B 131 ? 0.8492 0.6860 0.5759 0.3897  -0.0925 -0.0356 140 LEU   B CB  
1267 C  CG  . LEU   B 131 ? 0.8538 0.7144 0.5993 0.3846  -0.0709 -0.0215 140 LEU   B CG  
1268 C  CD1 . LEU   B 131 ? 0.8547 0.7273 0.5950 0.4055  -0.0752 -0.0271 140 LEU   B CD1 
1269 C  CD2 . LEU   B 131 ? 0.8535 0.7165 0.6296 0.3480  -0.0631 -0.0194 140 LEU   B CD2 
1270 N  N   . ASP   B 132 ? 0.9174 0.6922 0.6164 0.3825  -0.1323 -0.0605 141 ASP   B N   
1271 C  CA  . ASP   B 132 ? 0.9586 0.7033 0.6300 0.4001  -0.1558 -0.0770 141 ASP   B CA  
1272 C  C   . ASP   B 132 ? 0.9779 0.7256 0.6382 0.4211  -0.1734 -0.0947 141 ASP   B C   
1273 O  O   . ASP   B 132 ? 0.9655 0.7394 0.6416 0.4201  -0.1661 -0.0921 141 ASP   B O   
1274 C  CB  . ASP   B 132 ? 0.9881 0.7018 0.6696 0.3715  -0.1694 -0.0847 141 ASP   B CB  
1275 C  CG  . ASP   B 132 ? 1.0504 0.7653 0.7630 0.3416  -0.1793 -0.0948 141 ASP   B CG  
1276 O  OD1 . ASP   B 132 ? 1.0357 0.7745 0.7601 0.3457  -0.1796 -0.0996 141 ASP   B OD1 
1277 O  OD2 . ASP   B 132 ? 1.0997 0.7928 0.8249 0.3151  -0.1866 -0.0970 141 ASP   B OD2 
1278 N  N   . LYS   B 133 ? 1.0091 0.7287 0.6419 0.4398  -0.1977 -0.1135 142 LYS   B N   
1279 C  CA  . LYS   B 133 ? 1.0325 0.7521 0.6496 0.4625  -0.2186 -0.1335 142 LYS   B CA  
1280 C  C   . LYS   B 133 ? 1.0162 0.7486 0.6672 0.4374  -0.2296 -0.1446 142 LYS   B C   
1281 O  O   . LYS   B 133 ? 1.0149 0.7627 0.6589 0.4568  -0.2400 -0.1555 142 LYS   B O   
1282 C  CB  . LYS   B 133 ? 1.1017 0.7818 0.6829 0.4837  -0.2451 -0.1540 142 LYS   B CB  
1283 C  CG  . LYS   B 133 ? 1.2041 0.8768 0.7499 0.5144  -0.2335 -0.1428 142 LYS   B CG  
1284 C  CD  . LYS   B 133 ? 1.3149 0.9408 0.8269 0.5301  -0.2574 -0.1612 142 LYS   B CD  
1285 C  CE  . LYS   B 133 ? 1.3908 1.0169 0.8658 0.5676  -0.2452 -0.1502 142 LYS   B CE  
1286 N  NZ  . LYS   B 133 ? 1.4655 1.0430 0.9062 0.5839  -0.2671 -0.1674 142 LYS   B NZ  
1287 N  N   . CYS   B 134 ? 1.0028 0.7324 0.6899 0.3965  -0.2266 -0.1410 143 CYS   B N   
1288 C  CA  . CYS   B 134 ? 0.9815 0.7301 0.7059 0.3712  -0.2334 -0.1484 143 CYS   B CA  
1289 C  C   . CYS   B 134 ? 0.9396 0.7275 0.6871 0.3653  -0.2080 -0.1314 143 CYS   B C   
1290 O  O   . CYS   B 134 ? 0.9288 0.7379 0.7059 0.3495  -0.2113 -0.1363 143 CYS   B O   
1291 C  CB  . CYS   B 134 ? 1.0092 0.7376 0.7616 0.3314  -0.2421 -0.1521 143 CYS   B CB  
1292 S  SG  . CYS   B 134 ? 1.1411 0.8146 0.8691 0.3336  -0.2726 -0.1718 143 CYS   B SG  
1293 N  N   . GLY   B 135 ? 0.9154 0.7120 0.6521 0.3756  -0.1832 -0.1116 144 GLY   B N   
1294 C  CA  . GLY   B 135 ? 0.8844 0.7107 0.6416 0.3682  -0.1583 -0.0949 144 GLY   B CA  
1295 C  C   . GLY   B 135 ? 0.8551 0.6816 0.6399 0.3321  -0.1433 -0.0835 144 GLY   B C   
1296 O  O   . GLY   B 135 ? 0.8432 0.6912 0.6477 0.3216  -0.1248 -0.0726 144 GLY   B O   
1297 N  N   . ARG   B 136 ? 0.8395 0.6406 0.6239 0.3141  -0.1511 -0.0859 145 ARG   B N   
1298 C  CA  . ARG   B 136 ? 0.8206 0.6211 0.6269 0.2821  -0.1379 -0.0750 145 ARG   B CA  
1299 C  C   . ARG   B 136 ? 0.7995 0.6036 0.5958 0.2861  -0.1163 -0.0570 145 ARG   B C   
1300 O  O   . ARG   B 136 ? 0.8101 0.6042 0.5803 0.3083  -0.1167 -0.0538 145 ARG   B O   
1301 C  CB  . ARG   B 136 ? 0.8504 0.6214 0.6597 0.2620  -0.1541 -0.0826 145 ARG   B CB  
1302 C  CG  . ARG   B 136 ? 0.8924 0.6603 0.7174 0.2532  -0.1769 -0.1006 145 ARG   B CG  
1303 C  CD  . ARG   B 136 ? 0.9769 0.7109 0.8056 0.2314  -0.1917 -0.1058 145 ARG   B CD  
1304 N  NE  . ARG   B 136 ? 1.0718 0.7693 0.8641 0.2511  -0.2020 -0.1093 145 ARG   B NE  
1305 C  CZ  . ARG   B 136 ? 1.1472 0.8126 0.9322 0.2383  -0.2037 -0.1040 145 ARG   B CZ  
1306 N  NH1 . ARG   B 136 ? 1.1422 0.8079 0.9528 0.2053  -0.1949 -0.0937 145 ARG   B NH1 
1307 N  NH2 . ARG   B 136 ? 1.1765 0.8101 0.9266 0.2607  -0.2130 -0.1079 145 ARG   B NH2 
1308 N  N   . VAL   B 137 ? 0.7637 0.5843 0.5812 0.2657  -0.0976 -0.0457 146 VAL   B N   
1309 C  CA  . VAL   B 137 ? 0.7474 0.5733 0.5597 0.2658  -0.0788 -0.0301 146 VAL   B CA  
1310 C  C   . VAL   B 137 ? 0.7396 0.5448 0.5437 0.2540  -0.0822 -0.0265 146 VAL   B C   
1311 O  O   . VAL   B 137 ? 0.7394 0.5375 0.5572 0.2291  -0.0837 -0.0270 146 VAL   B O   
1312 C  CB  . VAL   B 137 ? 0.7378 0.5849 0.5721 0.2501  -0.0596 -0.0217 146 VAL   B CB  
1313 C  CG1 . VAL   B 137 ? 0.7436 0.5968 0.5730 0.2520  -0.0426 -0.0073 146 VAL   B CG1 
1314 C  CG2 . VAL   B 137 ? 0.7350 0.5998 0.5775 0.2622  -0.0577 -0.0257 146 VAL   B CG2 
1315 N  N   . ILE   B 138 ? 0.7308 0.5271 0.5116 0.2739  -0.0833 -0.0221 147 ILE   B N   
1316 C  CA  . ILE   B 138 ? 0.7289 0.5056 0.4974 0.2694  -0.0870 -0.0179 147 ILE   B CA  
1317 C  C   . ILE   B 138 ? 0.7099 0.5023 0.4829 0.2621  -0.0692 -0.0022 147 ILE   B C   
1318 O  O   . ILE   B 138 ? 0.7129 0.4935 0.4756 0.2600  -0.0710 0.0029  147 ILE   B O   
1319 C  CB  . ILE   B 138 ? 0.7488 0.5046 0.4871 0.2981  -0.1018 -0.0246 147 ILE   B CB  
1320 C  CG1 . ILE   B 138 ? 0.7511 0.5269 0.4755 0.3286  -0.0928 -0.0184 147 ILE   B CG1 
1321 C  CG2 . ILE   B 138 ? 0.7620 0.4956 0.4962 0.2998  -0.1239 -0.0430 147 ILE   B CG2 
1322 C  CD1 . ILE   B 138 ? 0.7820 0.5421 0.4757 0.3573  -0.1022 -0.0209 147 ILE   B CD1 
1323 N  N   . GLY   B 139 ? 0.6813 0.4986 0.4699 0.2575  -0.0534 0.0046  148 GLY   B N   
1324 C  CA  . GLY   B 139 ? 0.6708 0.5039 0.4667 0.2488  -0.0383 0.0172  148 GLY   B CA  
1325 C  C   . GLY   B 139 ? 0.6594 0.5153 0.4666 0.2541  -0.0232 0.0241  148 GLY   B C   
1326 O  O   . GLY   B 139 ? 0.6543 0.5139 0.4613 0.2673  -0.0235 0.0205  148 GLY   B O   
1327 N  N   . LEU   B 140 ? 0.6482 0.5187 0.4655 0.2442  -0.0105 0.0343  149 LEU   B N   
1328 C  CA  . LEU   B 140 ? 0.6317 0.5197 0.4619 0.2461  0.0044  0.0421  149 LEU   B CA  
1329 C  C   . LEU   B 140 ? 0.6342 0.5379 0.4631 0.2571  0.0118  0.0554  149 LEU   B C   
1330 O  O   . LEU   B 140 ? 0.6333 0.5393 0.4586 0.2534  0.0085  0.0587  149 LEU   B O   
1331 C  CB  . LEU   B 140 ? 0.6158 0.5076 0.4642 0.2209  0.0134  0.0410  149 LEU   B CB  
1332 C  CG  . LEU   B 140 ? 0.6154 0.4999 0.4711 0.2083  0.0109  0.0304  149 LEU   B CG  
1333 C  CD1 . LEU   B 140 ? 0.5947 0.4856 0.4658 0.1908  0.0233  0.0308  149 LEU   B CD1 
1334 C  CD2 . LEU   B 140 ? 0.6213 0.5047 0.4746 0.2253  0.0070  0.0252  149 LEU   B CD2 
1335 N  N   . TYR   B 141 ? 0.6356 0.5516 0.4678 0.2719  0.0220  0.0641  150 TYR   B N   
1336 C  CA  . TYR   B 141 ? 0.6345 0.5705 0.4702 0.2832  0.0319  0.0793  150 TYR   B CA  
1337 C  C   . TYR   B 141 ? 0.6185 0.5666 0.4795 0.2608  0.0447  0.0870  150 TYR   B C   
1338 O  O   . TYR   B 141 ? 0.6086 0.5498 0.4795 0.2505  0.0507  0.0839  150 TYR   B O   
1339 C  CB  . TYR   B 141 ? 0.6517 0.5930 0.4766 0.3119  0.0371  0.0858  150 TYR   B CB  
1340 C  CG  . TYR   B 141 ? 0.6619 0.6274 0.4963 0.3227  0.0529  0.1054  150 TYR   B CG  
1341 C  CD1 . TYR   B 141 ? 0.6675 0.6397 0.5205 0.3151  0.0684  0.1159  150 TYR   B CD1 
1342 C  CD2 . TYR   B 141 ? 0.6813 0.6626 0.5064 0.3413  0.0530  0.1144  150 TYR   B CD2 
1343 C  CE1 . TYR   B 141 ? 0.6760 0.6707 0.5414 0.3223  0.0839  0.1362  150 TYR   B CE1 
1344 C  CE2 . TYR   B 141 ? 0.6868 0.6952 0.5242 0.3506  0.0689  0.1345  150 TYR   B CE2 
1345 C  CZ  . TYR   B 141 ? 0.6859 0.7012 0.5445 0.3401  0.0846  0.1460  150 TYR   B CZ  
1346 O  OH  . TYR   B 141 ? 0.6828 0.7256 0.5567 0.3474  0.1011  0.1680  150 TYR   B OH  
1347 N  N   . GLY   B 142 ? 0.6166 0.5820 0.4879 0.2536  0.0479  0.0956  151 GLY   B N   
1348 C  CA  . GLY   B 142 ? 0.6204 0.5966 0.5168 0.2315  0.0578  0.1012  151 GLY   B CA  
1349 C  C   . GLY   B 142 ? 0.6307 0.6188 0.5371 0.2131  0.0534  0.1007  151 GLY   B C   
1350 O  O   . GLY   B 142 ? 0.6300 0.6244 0.5565 0.1927  0.0588  0.1018  151 GLY   B O   
1351 N  N   . ASN   B 143 ? 0.6379 0.6286 0.5297 0.2210  0.0428  0.0988  152 ASN   B N   
1352 C  CA  . ASN   B 143 ? 0.6380 0.6436 0.5372 0.2078  0.0379  0.0997  152 ASN   B CA  
1353 C  C   . ASN   B 143 ? 0.6548 0.6748 0.5422 0.2294  0.0327  0.1073  152 ASN   B C   
1354 O  O   . ASN   B 143 ? 0.6732 0.6749 0.5362 0.2436  0.0233  0.1015  152 ASN   B O   
1355 C  CB  . ASN   B 143 ? 0.6569 0.6447 0.5480 0.1891  0.0292  0.0865  152 ASN   B CB  
1356 C  CG  . ASN   B 143 ? 0.6785 0.6837 0.5771 0.1753  0.0244  0.0873  152 ASN   B CG  
1357 O  OD1 . ASN   B 143 ? 0.6772 0.7075 0.5972 0.1688  0.0289  0.0946  152 ASN   B OD1 
1358 N  ND2 . ASN   B 143 ? 0.6878 0.6812 0.5699 0.1704  0.0149  0.0803  152 ASN   B ND2 
1359 N  N   . GLY   B 144 ? 0.6438 0.6963 0.5495 0.2323  0.0389  0.1203  153 GLY   B N   
1360 C  CA  . GLY   B 144 ? 0.6637 0.7352 0.5599 0.2554  0.0356  0.1288  153 GLY   B CA  
1361 C  C   . GLY   B 144 ? 0.6736 0.7876 0.5968 0.2509  0.0408  0.1421  153 GLY   B C   
1362 O  O   . GLY   B 144 ? 0.6673 0.7928 0.6090 0.2268  0.0375  0.1393  153 GLY   B O   
1363 N  N   . VAL   B 145 ? 0.6878 0.8274 0.6134 0.2750  0.0484  0.1566  154 VAL   B N   
1364 C  CA  . VAL   B 145 ? 0.6956 0.8822 0.6480 0.2751  0.0532  0.1713  154 VAL   B CA  
1365 C  C   . VAL   B 145 ? 0.7196 0.9349 0.6876 0.2919  0.0703  0.1908  154 VAL   B C   
1366 O  O   . VAL   B 145 ? 0.7367 0.9345 0.6861 0.3112  0.0768  0.1924  154 VAL   B O   
1367 C  CB  . VAL   B 145 ? 0.7036 0.8982 0.6359 0.2937  0.0409  0.1696  154 VAL   B CB  
1368 C  CG1 . VAL   B 145 ? 0.7120 0.9071 0.6185 0.3331  0.0434  0.1761  154 VAL   B CG1 
1369 C  CG2 . VAL   B 145 ? 0.6896 0.9291 0.6507 0.2822  0.0386  0.1774  154 VAL   B CG2 
1370 N  N   . VAL   B 146 ? 0.7188 0.9800 0.7226 0.2836  0.0777  0.2060  155 VAL   B N   
1371 C  CA  . VAL   B 146 ? 0.7338 1.0299 0.7573 0.2982  0.0958  0.2283  155 VAL   B CA  
1372 C  C   . VAL   B 146 ? 0.7595 1.0964 0.7808 0.3252  0.0949  0.2392  155 VAL   B C   
1373 O  O   . VAL   B 146 ? 0.7478 1.1102 0.7847 0.3146  0.0855  0.2377  155 VAL   B O   
1374 C  CB  . VAL   B 146 ? 0.7191 1.0377 0.7907 0.2663  0.1070  0.2398  155 VAL   B CB  
1375 C  CG1 . VAL   B 146 ? 0.7104 1.0650 0.8027 0.2820  0.1282  0.2665  155 VAL   B CG1 
1376 C  CG2 . VAL   B 146 ? 0.7399 1.0137 0.8095 0.2419  0.1065  0.2268  155 VAL   B CG2 
1377 N  N   . ILE   B 147 ? 0.7949 1.1362 0.7920 0.3629  0.1029  0.2483  156 ILE   B N   
1378 C  CA  . ILE   B 147 ? 0.8170 1.1956 0.8072 0.3943  0.1028  0.2583  156 ILE   B CA  
1379 C  C   . ILE   B 147 ? 0.8053 1.2489 0.8403 0.3946  0.1215  0.2856  156 ILE   B C   
1380 O  O   . ILE   B 147 ? 0.7941 1.2466 0.8616 0.3716  0.1348  0.2967  156 ILE   B O   
1381 C  CB  . ILE   B 147 ? 0.8594 1.2092 0.7974 0.4373  0.0995  0.2518  156 ILE   B CB  
1382 C  CG1 . ILE   B 147 ? 0.8899 1.2280 0.8172 0.4519  0.1143  0.2593  156 ILE   B CG1 
1383 C  CG2 . ILE   B 147 ? 0.8951 1.1890 0.7968 0.4332  0.0782  0.2262  156 ILE   B CG2 
1384 C  CD1 . ILE   B 147 ? 0.9384 1.2503 0.8131 0.4966  0.1098  0.2516  156 ILE   B CD1 
1385 N  N   . LYS   B 148 ? 0.8041 1.2934 0.8427 0.4197  0.1227  0.2969  157 LYS   B N   
1386 C  CA  . LYS   B 148 ? 0.7857 1.3455 0.8706 0.4206  0.1394  0.3237  157 LYS   B CA  
1387 C  C   . LYS   B 148 ? 0.7803 1.3568 0.8818 0.4264  0.1647  0.3467  157 LYS   B C   
1388 O  O   . LYS   B 148 ? 0.7501 1.3759 0.9032 0.4078  0.1791  0.3683  157 LYS   B O   
1389 C  CB  . LYS   B 148 ? 0.8202 1.4226 0.8952 0.4579  0.1375  0.3317  157 LYS   B CB  
1390 C  CG  . LYS   B 148 ? 0.9358 1.4974 0.9470 0.5010  0.1277  0.3174  157 LYS   B CG  
1391 C  CD  . LYS   B 148 ? 1.0243 1.5783 1.0062 0.5380  0.1437  0.3270  157 LYS   B CD  
1392 C  CE  . LYS   B 148 ? 1.0523 1.6752 1.0677 0.5540  0.1690  0.3586  157 LYS   B CE  
1393 N  NZ  . LYS   B 148 ? 1.0598 1.7421 1.0903 0.5751  0.1691  0.3702  157 LYS   B NZ  
1394 N  N   . ASN   B 149 ? 0.8040 1.3399 0.8638 0.4505  0.1698  0.3425  158 ASN   B N   
1395 C  CA  . ASN   B 149 ? 0.7980 1.3460 0.8669 0.4597  0.1937  0.3646  158 ASN   B CA  
1396 C  C   . ASN   B 149 ? 0.7942 1.3054 0.8792 0.4236  0.1978  0.3615  158 ASN   B C   
1397 O  O   . ASN   B 149 ? 0.8031 1.3105 0.8858 0.4333  0.2160  0.3771  158 ASN   B O   
1398 C  CB  . ASN   B 149 ? 0.8490 1.3817 0.8638 0.5115  0.1989  0.3650  158 ASN   B CB  
1399 C  CG  . ASN   B 149 ? 0.9420 1.4146 0.9010 0.5272  0.1757  0.3339  158 ASN   B CG  
1400 O  OD1 . ASN   B 149 ? 0.9684 1.4350 0.9141 0.5309  0.1582  0.3192  158 ASN   B OD1 
1401 N  ND2 . ASN   B 149 ? 0.9771 1.4044 0.9025 0.5371  0.1751  0.3241  158 ASN   B ND2 
1402 N  N   . GLY   B 150 ? 0.7759 1.2608 0.8749 0.3849  0.1815  0.3423  159 GLY   B N   
1403 C  CA  . GLY   B 150 ? 0.7666 1.2143 0.8794 0.3509  0.1832  0.3364  159 GLY   B CA  
1404 C  C   . GLY   B 150 ? 0.7795 1.1655 0.8457 0.3611  0.1753  0.3163  159 GLY   B C   
1405 O  O   . GLY   B 150 ? 0.7917 1.1435 0.8649 0.3349  0.1745  0.3082  159 GLY   B O   
1406 N  N   . SER   B 151 ? 0.7747 1.1460 0.7934 0.3995  0.1685  0.3074  160 SER   B N   
1407 C  CA  A SER   B 151 ? 0.8000 1.1170 0.7751 0.4115  0.1588  0.2877  160 SER   B CA  
1408 C  CA  B SER   B 151 ? 0.7994 1.1161 0.7762 0.4096  0.1593  0.2880  160 SER   B CA  
1409 C  C   . SER   B 151 ? 0.8021 1.0793 0.7677 0.3859  0.1368  0.2600  160 SER   B C   
1410 O  O   . SER   B 151 ? 0.7922 1.0819 0.7681 0.3734  0.1255  0.2535  160 SER   B O   
1411 C  CB  A SER   B 151 ? 0.8346 1.1488 0.7637 0.4594  0.1563  0.2855  160 SER   B CB  
1412 C  CB  B SER   B 151 ? 0.8344 1.1466 0.7653 0.4580  0.1595  0.2877  160 SER   B CB  
1413 O  OG  A SER   B 151 ? 0.8932 1.1579 0.7831 0.4705  0.1460  0.2664  160 SER   B OG  
1414 O  OG  B SER   B 151 ? 0.8551 1.1976 0.7776 0.4824  0.1558  0.2913  160 SER   B OG  
1415 N  N   . TYR   B 152 ? 0.7891 1.0211 0.7348 0.3800  0.1314  0.2448  161 TYR   B N   
1416 C  CA  . TYR   B 152 ? 0.7745 0.9681 0.7103 0.3575  0.1135  0.2204  161 TYR   B CA  
1417 C  C   . TYR   B 152 ? 0.7732 0.9348 0.6651 0.3796  0.0964  0.2011  161 TYR   B C   
1418 O  O   . TYR   B 152 ? 0.7871 0.9333 0.6511 0.4062  0.0971  0.1990  161 TYR   B O   
1419 C  CB  . TYR   B 152 ? 0.7725 0.9392 0.7187 0.3349  0.1188  0.2163  161 TYR   B CB  
1420 C  CG  . TYR   B 152 ? 0.7831 0.9155 0.7235 0.3099  0.1031  0.1931  161 TYR   B CG  
1421 C  CD1 . TYR   B 152 ? 0.7818 0.9220 0.7424 0.2820  0.0956  0.1871  161 TYR   B CD1 
1422 C  CD2 . TYR   B 152 ? 0.8083 0.9035 0.7225 0.3156  0.0955  0.1774  161 TYR   B CD2 
1423 C  CE1 . TYR   B 152 ? 0.8015 0.9122 0.7535 0.2619  0.0825  0.1671  161 TYR   B CE1 
1424 C  CE2 . TYR   B 152 ? 0.8285 0.8964 0.7385 0.2937  0.0829  0.1581  161 TYR   B CE2 
1425 C  CZ  . TYR   B 152 ? 0.8326 0.9079 0.7601 0.2678  0.0771  0.1536  161 TYR   B CZ  
1426 O  OH  . TYR   B 152 ? 0.8617 0.9119 0.7831 0.2481  0.0664  0.1361  161 TYR   B OH  
1427 N  N   . VAL   B 153 ? 0.7572 0.9064 0.6429 0.3674  0.0802  0.1867  162 VAL   B N   
1428 C  CA  . VAL   B 153 ? 0.7590 0.8725 0.6069 0.3822  0.0629  0.1682  162 VAL   B CA  
1429 C  C   . VAL   B 153 ? 0.7330 0.8154 0.5833 0.3507  0.0515  0.1510  162 VAL   B C   
1430 O  O   . VAL   B 153 ? 0.7131 0.8067 0.5833 0.3266  0.0494  0.1509  162 VAL   B O   
1431 C  CB  . VAL   B 153 ? 0.7692 0.8939 0.5985 0.4066  0.0548  0.1693  162 VAL   B CB  
1432 C  CG1 . VAL   B 153 ? 0.7996 0.8804 0.5882 0.4236  0.0375  0.1507  162 VAL   B CG1 
1433 C  CG2 . VAL   B 153 ? 0.7694 0.9331 0.6004 0.4377  0.0689  0.1888  162 VAL   B CG2 
1434 N  N   . SER   B 154 ? 0.7312 0.7783 0.5632 0.3509  0.0448  0.1370  163 SER   B N   
1435 C  CA  . SER   B 154 ? 0.7269 0.7474 0.5620 0.3225  0.0363  0.1221  163 SER   B CA  
1436 C  C   . SER   B 154 ? 0.7339 0.7241 0.5419 0.3282  0.0191  0.1077  163 SER   B C   
1437 O  O   . SER   B 154 ? 0.7525 0.7283 0.5353 0.3539  0.0124  0.1031  163 SER   B O   
1438 C  CB  . SER   B 154 ? 0.7399 0.7449 0.5795 0.3151  0.0418  0.1174  163 SER   B CB  
1439 O  OG  . SER   B 154 ? 0.7587 0.7363 0.5948 0.2954  0.0325  0.1016  163 SER   B OG  
1440 N  N   . ALA   B 155 ? 0.7187 0.6962 0.5310 0.3039  0.0120  0.0998  164 ALA   B N   
1441 C  CA  . ALA   B 155 ? 0.7281 0.6730 0.5180 0.3039  -0.0030 0.0874  164 ALA   B CA  
1442 C  C   . ALA   B 155 ? 0.7363 0.6550 0.5203 0.3003  -0.0070 0.0752  164 ALA   B C   
1443 O  O   . ALA   B 155 ? 0.7158 0.6418 0.5151 0.2922  0.0022  0.0759  164 ALA   B O   
1444 C  CB  . ALA   B 155 ? 0.7204 0.6631 0.5180 0.2783  -0.0066 0.0853  164 ALA   B CB  
1445 N  N   . ILE   B 156 ? 0.7589 0.6471 0.5218 0.3067  -0.0212 0.0643  165 ILE   B N   
1446 C  CA  . ILE   B 156 ? 0.7764 0.6428 0.5379 0.2997  -0.0274 0.0518  165 ILE   B CA  
1447 C  C   . ILE   B 156 ? 0.7716 0.6278 0.5433 0.2697  -0.0293 0.0483  165 ILE   B C   
1448 O  O   . ILE   B 156 ? 0.7831 0.6180 0.5421 0.2665  -0.0397 0.0450  165 ILE   B O   
1449 C  CB  . ILE   B 156 ? 0.8132 0.6518 0.5490 0.3207  -0.0432 0.0409  165 ILE   B CB  
1450 C  CG1 . ILE   B 156 ? 0.8351 0.6848 0.5537 0.3560  -0.0414 0.0452  165 ILE   B CG1 
1451 C  CG2 . ILE   B 156 ? 0.8247 0.6478 0.5659 0.3099  -0.0499 0.0280  165 ILE   B CG2 
1452 C  CD1 . ILE   B 156 ? 0.8720 0.6926 0.5610 0.3796  -0.0585 0.0326  165 ILE   B CD1 
1453 N  N   . THR   B 157 ? 0.7494 0.6214 0.5427 0.2492  -0.0181 0.0507  166 THR   B N   
1454 C  CA  . THR   B 157 ? 0.7446 0.6127 0.5472 0.2224  -0.0170 0.0484  166 THR   B CA  
1455 C  C   . THR   B 157 ? 0.7468 0.5973 0.5522 0.2101  -0.0216 0.0383  166 THR   B C   
1456 O  O   . THR   B 157 ? 0.7412 0.5980 0.5587 0.2071  -0.0161 0.0345  166 THR   B O   
1457 C  CB  . THR   B 157 ? 0.7372 0.6283 0.5594 0.2077  -0.0042 0.0535  166 THR   B CB  
1458 O  OG1 . THR   B 157 ? 0.7351 0.6466 0.5594 0.2166  -0.0007 0.0635  166 THR   B OG1 
1459 C  CG2 . THR   B 157 ? 0.7425 0.6306 0.5691 0.1841  -0.0034 0.0505  166 THR   B CG2 
1460 N  N   . GLN   B 158 ? 0.7517 0.5814 0.5478 0.2023  -0.0310 0.0353  167 GLN   B N   
1461 C  CA  . GLN   B 158 ? 0.7593 0.5749 0.5618 0.1882  -0.0356 0.0275  167 GLN   B CA  
1462 C  C   . GLN   B 158 ? 0.7893 0.6032 0.5969 0.1644  -0.0313 0.0307  167 GLN   B C   
1463 O  O   . GLN   B 158 ? 0.8021 0.6112 0.5985 0.1624  -0.0325 0.0373  167 GLN   B O   
1464 C  CB  . GLN   B 158 ? 0.7491 0.5378 0.5373 0.1999  -0.0517 0.0207  167 GLN   B CB  
1465 C  CG  . GLN   B 158 ? 0.7293 0.5042 0.5279 0.1850  -0.0592 0.0121  167 GLN   B CG  
1466 C  CD  . GLN   B 158 ? 0.7408 0.5339 0.5573 0.1839  -0.0548 0.0055  167 GLN   B CD  
1467 O  OE1 . GLN   B 158 ? 0.7367 0.5511 0.5661 0.1766  -0.0411 0.0090  167 GLN   B OE1 
1468 N  NE2 . GLN   B 158 ? 0.7370 0.5207 0.5539 0.1913  -0.0673 -0.0050 167 GLN   B NE2 
1469 N  N   . GLY   B 159 ? 0.7988 0.6181 0.6219 0.1486  -0.0262 0.0265  168 GLY   B N   
1470 C  CA  . GLY   B 159 ? 0.8254 0.6445 0.6521 0.1280  -0.0210 0.0298  168 GLY   B CA  
1471 C  C   . GLY   B 159 ? 0.8652 0.6613 0.6887 0.1195  -0.0302 0.0303  168 GLY   B C   
1472 O  O   . GLY   B 159 ? 0.8720 0.6490 0.6888 0.1296  -0.0427 0.0263  168 GLY   B O   
1473 N  N   . LYS   B 160 ? 0.8912 0.6880 0.7186 0.1010  -0.0240 0.0355  169 LYS   B N   
1474 C  CA  . LYS   B 160 ? 0.9283 0.7041 0.7564 0.0886  -0.0300 0.0392  169 LYS   B CA  
1475 C  C   . LYS   B 160 ? 0.9460 0.7363 0.7987 0.0721  -0.0238 0.0363  169 LYS   B C   
1476 O  O   . LYS   B 160 ? 0.9406 0.7545 0.8015 0.0662  -0.0107 0.0367  169 LYS   B O   
1477 C  CB  . LYS   B 160 ? 0.9624 0.7290 0.7739 0.0816  -0.0260 0.0516  169 LYS   B CB  
1478 C  CG  . LYS   B 160 ? 1.0253 0.7658 0.8363 0.0684  -0.0309 0.0588  169 LYS   B CG  
1479 C  CD  . LYS   B 160 ? 1.0876 0.8243 0.8841 0.0600  -0.0228 0.0732  169 LYS   B CD  
1480 C  CE  . LYS   B 160 ? 1.1405 0.8526 0.9408 0.0439  -0.0246 0.0830  169 LYS   B CE  
1481 N  NZ  . LYS   B 160 ? 1.1689 0.8844 0.9573 0.0344  -0.0124 0.0987  169 LYS   B NZ  
1482 N  N   . ARG   B 161 ? 0.9654 0.7427 0.8307 0.0653  -0.0338 0.0327  170 ARG   B N   
1483 C  CA  . ARG   B 161 ? 0.9745 0.7703 0.8673 0.0494  -0.0287 0.0306  170 ARG   B CA  
1484 C  C   . ARG   B 161 ? 0.9992 0.7887 0.8973 0.0282  -0.0225 0.0435  170 ARG   B C   
1485 O  O   . ARG   B 161 ? 1.0192 0.7790 0.9033 0.0251  -0.0296 0.0508  170 ARG   B O   
1486 C  CB  . ARG   B 161 ? 0.9854 0.7768 0.8938 0.0530  -0.0440 0.0185  170 ARG   B CB  
1487 C  CG  . ARG   B 161 ? 0.9903 0.8136 0.9280 0.0460  -0.0383 0.0128  170 ARG   B CG  
1488 C  CD  . ARG   B 161 ? 1.0227 0.8427 0.9788 0.0447  -0.0557 0.0017  170 ARG   B CD  
1489 N  NE  . ARG   B 161 ? 1.0347 0.8850 1.0247 0.0290  -0.0500 0.0015  170 ARG   B NE  
1490 C  CZ  . ARG   B 161 ? 1.0387 0.9165 1.0463 0.0371  -0.0511 -0.0083 170 ARG   B CZ  
1491 N  NH1 . ARG   B 161 ? 1.0284 0.9045 1.0217 0.0605  -0.0578 -0.0182 170 ARG   B NH1 
1492 N  NH2 . ARG   B 161 ? 1.0180 0.9266 1.0575 0.0232  -0.0451 -0.0072 170 ARG   B NH2 
1493 N  N   . GLU   B 162 ? 0.9951 0.8121 0.9121 0.0149  -0.0085 0.0474  171 GLU   B N   
1494 C  CA  . GLU   B 162 ? 1.0108 0.8274 0.9339 -0.0045 0.0009  0.0621  171 GLU   B CA  
1495 C  C   . GLU   B 162 ? 1.0022 0.8247 0.9588 -0.0225 -0.0034 0.0625  171 GLU   B C   
1496 O  O   . GLU   B 162 ? 1.0055 0.8168 0.9691 -0.0401 -0.0008 0.0759  171 GLU   B O   
1497 C  CB  . GLU   B 162 ? 1.0469 0.8918 0.9655 -0.0061 0.0210  0.0679  171 GLU   B CB  
1498 C  CG  . GLU   B 162 ? 1.1434 0.9843 1.0319 0.0085  0.0238  0.0668  171 GLU   B CG  
1499 C  CD  . GLU   B 162 ? 1.2827 1.0971 1.1451 0.0089  0.0200  0.0785  171 GLU   B CD  
1500 O  OE1 . GLU   B 162 ? 1.3104 1.1180 1.1722 -0.0043 0.0260  0.0927  171 GLU   B OE1 
1501 O  OE2 . GLU   B 162 ? 1.3338 1.1354 1.1767 0.0234  0.0118  0.0749  171 GLU   B OE2 
1502 S  S   . DMS   C .   ? 1.2825 1.0899 1.1433 0.0362  0.0635  -0.0857 201 DMS   B S   
1503 O  O   . DMS   C .   ? 1.2788 1.1055 1.1322 0.0470  0.0687  -0.0758 201 DMS   B O   
1504 C  C1  . DMS   C .   ? 1.2942 1.0671 1.1554 0.0450  0.0749  -0.0944 201 DMS   B C1  
1505 C  C2  . DMS   C .   ? 1.2691 1.0791 1.1618 0.0308  0.0628  -0.0679 201 DMS   B C2  
1506 N  N1  . A1B9E D .   ? 0.7275 0.8346 0.7292 0.1656  0.0601  0.1355  202 A1B9E B N1  
1507 N  N3  . A1B9E D .   ? 0.6999 0.7305 0.6541 0.0925  0.0229  0.0650  202 A1B9E B N3  
1508 C  C4  . A1B9E D .   ? 0.7186 0.7860 0.7248 0.1601  0.0777  0.1352  202 A1B9E B C4  
1509 C  C5  . A1B9E D .   ? 0.6995 0.7360 0.6971 0.1242  0.0617  0.1043  202 A1B9E B C5  
1510 C  C6  . A1B9E D .   ? 0.6861 0.7227 0.7059 0.0996  0.0627  0.0999  202 A1B9E B C6  
1511 C  C7  . A1B9E D .   ? 0.6828 0.7170 0.6986 0.0822  0.0513  0.0850  202 A1B9E B C7  
1512 C  C8  . A1B9E D .   ? 0.6897 0.7221 0.6804 0.0892  0.0410  0.0772  202 A1B9E B C8  
1513 C  C10 . A1B9E D .   ? 0.7015 0.7317 0.6749 0.1293  0.0501  0.0945  202 A1B9E B C10 
1514 C  C13 . A1B9E D .   ? 0.7277 0.7930 0.7311 0.1814  0.0912  0.1491  202 A1B9E B C13 
1515 C  C15 . A1B9E D .   ? 0.7338 0.7792 0.7063 0.2234  0.1026  0.1576  202 A1B9E B C15 
1516 C  C17 . A1B9E D .   ? 0.7188 0.8130 0.7444 0.2041  0.1181  0.1852  202 A1B9E B C17 
1517 C  C20 . A1B9E D .   ? 0.6888 0.8465 0.7814 0.1806  0.1331  0.2167  202 A1B9E B C20 
1518 C  C21 . A1B9E D .   ? 0.7162 0.8084 0.7449 0.1830  0.1039  0.1693  202 A1B9E B C21 
1519 O  O1  . A1B9E D .   ? 0.7417 0.8076 0.7026 0.1960  0.0626  0.1300  202 A1B9E B O1  
1520 C  C1  . A1B9E D .   ? 0.7282 0.8091 0.7158 0.1759  0.0666  0.1338  202 A1B9E B C1  
1521 C  C2  . A1B9E D .   ? 0.7193 0.8617 0.7565 0.1553  0.0668  0.1493  202 A1B9E B C2  
1522 C  C3  . A1B9E D .   ? 0.7233 0.8915 0.7668 0.1794  0.0787  0.1698  202 A1B9E B C3  
1523 F  F1  . A1B9E D .   ? 0.7401 0.9014 0.7517 0.2081  0.0746  0.1688  202 A1B9E B F1  
1524 F  F2  . A1B9E D .   ? 0.7085 0.9201 0.7795 0.1754  0.0794  0.1819  202 A1B9E B F2  
1525 N  N2  . A1B9E D .   ? 0.7161 0.7536 0.7132 0.1438  0.0724  0.1174  202 A1B9E B N2  
1526 C  C9  . A1B9E D .   ? 0.6991 0.7278 0.6698 0.1115  0.0407  0.0824  202 A1B9E B C9  
1527 C  C11 . A1B9E D .   ? 0.7081 0.7293 0.6544 0.1127  0.0294  0.0732  202 A1B9E B C11 
1528 C  C12 . A1B9E D .   ? 0.6911 0.7197 0.6687 0.0763  0.0294  0.0625  202 A1B9E B C12 
1529 C  C14 . A1B9E D .   ? 0.7408 0.7829 0.7178 0.2008  0.0910  0.1438  202 A1B9E B C14 
1530 CL CL1 . A1B9E D .   ? 0.7407 0.7606 0.6802 0.2491  0.0995  0.1493  202 A1B9E B CL1 
1531 C  C16 . A1B9E D .   ? 0.7278 0.7984 0.7224 0.2262  0.1167  0.1787  202 A1B9E B C16 
1532 C  C18 . A1B9E D .   ? 0.7080 0.8340 0.7632 0.2046  0.1337  0.2098  202 A1B9E B C18 
1533 C  C19 . A1B9E D .   ? 0.6947 0.8643 0.7596 0.2173  0.1348  0.2237  202 A1B9E B C19 
1534 S  S   . DMS   E .   ? 1.4889 1.2250 1.3562 0.2358  0.1705  -0.0757 203 DMS   B S   
1535 O  O   . DMS   E .   ? 1.4810 1.2273 1.3590 0.2564  0.1734  -0.0634 203 DMS   B O   
1536 C  C1  . DMS   E .   ? 1.5109 1.1884 1.3693 0.2243  0.1701  -0.0786 203 DMS   B C1  
1537 C  C2  . DMS   E .   ? 1.4778 1.2378 1.3559 0.2089  0.1585  -0.0679 203 DMS   B C2  
# 
