data_7IAL
# 
_entry.id   7IAL 
# 
_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   7IAL         pdb_00007ial 10.2210/pdb7ial/pdb 
WWPDB D_1001408524 ?            ?                   
# 
_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                        7IAL 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ni, X.'              1  ? 
'Marples, P.G.'       2  ? 
'Godoy, A.S.'         3  ? 
'Koekemoer, L.'       4  ? 
'Aschenbrenner, J.C.' 5  ? 
'Balcomb, B.H.'       6  ? 
'Fairhead, M.'        7  ? 
'Lithgo, R.M.'        8  ? 
'Lee, A.'             9  ? 
'Kenton, N.'          10 ? 
'Thompson, W.'        11 ? 
'Tomlinson, C.W.E.'   12 ? 
'Wild, C.'            13 ? 
'Winokan, M.'         14 ? 
'Williams, E.P.'      15 ? 
'Chandran, A.V.'      16 ? 
'Walsh, M.A.'         17 ? 
'Fearon, D.'          18 ? 
'von Delft, F.'       19 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B' 5067.486  1  ?                           ?    ? ? 
2 polymer     man 'Serine protease NS3' 18117.629 1  3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE' 78.133    1  ?                           ?    ? ? 
4 non-polymer syn 
'(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-[(4-methylbenzene-1-sulfonyl)methyl]acetamide' 
510.008   1  ?                           ?    ? ? 
5 water       nat water 18.015    87 ?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                                                        DMS 
4 '(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-[(4-methylbenzene-1-sulfonyl)methyl]acetamide' 
A1B80 
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 
A1B80 non-polymer         . 
'(2R)-2-(6-chloro-1H-indazol-4-yl)-2-[(2,3-dihydro-1H-isoindol-5-yl)amino]-N-[(4-methylbenzene-1-sulfonyl)methyl]acetamide' ? 
'C25 H24 Cl N5 O3 S' 510.008 
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 A1B80 1  202 203 A1B80 LIG B . 
E 5 HOH   1  101 136 HOH   HOH A . 
E 5 HOH   2  102 125 HOH   HOH A . 
E 5 HOH   3  103 98  HOH   HOH A . 
E 5 HOH   4  104 34  HOH   HOH A . 
E 5 HOH   5  105 117 HOH   HOH A . 
E 5 HOH   6  106 134 HOH   HOH A . 
E 5 HOH   7  107 20  HOH   HOH A . 
E 5 HOH   8  108 118 HOH   HOH A . 
E 5 HOH   9  109 50  HOH   HOH A . 
E 5 HOH   10 110 49  HOH   HOH A . 
E 5 HOH   11 111 105 HOH   HOH A . 
E 5 HOH   12 112 120 HOH   HOH A . 
E 5 HOH   13 113 29  HOH   HOH A . 
E 5 HOH   14 114 70  HOH   HOH A . 
E 5 HOH   15 115 27  HOH   HOH A . 
E 5 HOH   16 116 119 HOH   HOH A . 
F 5 HOH   1  301 51  HOH   HOH B . 
F 5 HOH   2  302 11  HOH   HOH B . 
F 5 HOH   3  303 132 HOH   HOH B . 
F 5 HOH   4  304 129 HOH   HOH B . 
F 5 HOH   5  305 92  HOH   HOH B . 
F 5 HOH   6  306 14  HOH   HOH B . 
F 5 HOH   7  307 81  HOH   HOH B . 
F 5 HOH   8  308 130 HOH   HOH B . 
F 5 HOH   9  309 1   HOH   HOH B . 
F 5 HOH   10 310 56  HOH   HOH B . 
F 5 HOH   11 311 90  HOH   HOH B . 
F 5 HOH   12 312 89  HOH   HOH B . 
F 5 HOH   13 313 31  HOH   HOH B . 
F 5 HOH   14 314 9   HOH   HOH B . 
F 5 HOH   15 315 63  HOH   HOH B . 
F 5 HOH   16 316 133 HOH   HOH B . 
F 5 HOH   17 317 48  HOH   HOH B . 
F 5 HOH   18 318 32  HOH   HOH B . 
F 5 HOH   19 319 5   HOH   HOH B . 
F 5 HOH   20 320 4   HOH   HOH B . 
F 5 HOH   21 321 2   HOH   HOH B . 
F 5 HOH   22 322 13  HOH   HOH B . 
F 5 HOH   23 323 68  HOH   HOH B . 
F 5 HOH   24 324 69  HOH   HOH B . 
F 5 HOH   25 325 108 HOH   HOH B . 
F 5 HOH   26 326 36  HOH   HOH B . 
F 5 HOH   27 327 10  HOH   HOH B . 
F 5 HOH   28 328 12  HOH   HOH B . 
F 5 HOH   29 329 115 HOH   HOH B . 
F 5 HOH   30 330 61  HOH   HOH B . 
F 5 HOH   31 331 65  HOH   HOH B . 
F 5 HOH   32 332 107 HOH   HOH B . 
F 5 HOH   33 333 73  HOH   HOH B . 
F 5 HOH   34 334 16  HOH   HOH B . 
F 5 HOH   35 335 67  HOH   HOH B . 
F 5 HOH   36 336 28  HOH   HOH B . 
F 5 HOH   37 337 39  HOH   HOH B . 
F 5 HOH   38 338 131 HOH   HOH B . 
F 5 HOH   39 339 58  HOH   HOH B . 
F 5 HOH   40 340 124 HOH   HOH B . 
F 5 HOH   41 341 135 HOH   HOH B . 
F 5 HOH   42 342 106 HOH   HOH B . 
F 5 HOH   43 343 35  HOH   HOH B . 
F 5 HOH   44 344 102 HOH   HOH B . 
F 5 HOH   45 345 62  HOH   HOH B . 
F 5 HOH   46 346 3   HOH   HOH B . 
F 5 HOH   47 347 80  HOH   HOH B . 
F 5 HOH   48 348 24  HOH   HOH B . 
F 5 HOH   49 349 18  HOH   HOH B . 
F 5 HOH   50 350 64  HOH   HOH B . 
F 5 HOH   51 351 23  HOH   HOH B . 
F 5 HOH   52 352 21  HOH   HOH B . 
F 5 HOH   53 353 112 HOH   HOH B . 
F 5 HOH   54 354 100 HOH   HOH B . 
F 5 HOH   55 355 60  HOH   HOH B . 
F 5 HOH   56 356 116 HOH   HOH B . 
F 5 HOH   57 357 126 HOH   HOH B . 
F 5 HOH   58 358 26  HOH   HOH B . 
F 5 HOH   59 359 127 HOH   HOH B . 
F 5 HOH   60 360 94  HOH   HOH B . 
F 5 HOH   61 361 137 HOH   HOH B . 
F 5 HOH   62 362 128 HOH   HOH B . 
F 5 HOH   63 363 87  HOH   HOH B . 
F 5 HOH   64 364 79  HOH   HOH B . 
F 5 HOH   65 365 109 HOH   HOH B . 
F 5 HOH   66 366 54  HOH   HOH B . 
F 5 HOH   67 367 123 HOH   HOH B . 
F 5 HOH   68 368 57  HOH   HOH B . 
F 5 HOH   69 369 75  HOH   HOH B . 
F 5 HOH   70 370 59  HOH   HOH B . 
F 5 HOH   71 371 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           7IAL 
_cell.length_a           42.582 
_cell.length_b           42.582 
_cell.length_c           217.116 
_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                         7IAL 
_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          7IAL 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.130 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.12 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   42.05 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-07-31 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92134 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7IAL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             54.280 
_reflns.d_resolution_high            2.150 
_reflns.number_obs                   11839 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.401 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        6.200 
_reflns.B_iso_Wilson_estimate        44.630 
_reflns.pdbx_redundancy              21.600 
_reflns.pdbx_Rrim_I_all              0.411 
_reflns.pdbx_Rpim_I_all              0.087 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     255310 
_reflns.pdbx_scaling_rejects         421 
_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 2.150 2.270  ? 37235 ? ? 5.678 ? ? ? 22.600 ? 0.700  ? 1649 ? ? ? ? 100.000 5.809 1.212 0.717 ? 
1 2 6.800 54.280 ? 7603  ? ? 0.104 ? ? ? 15.800 ? 18.300 ? 481  ? ? ? ? 99.700  0.108 0.027 0.995 ? 
# 
_refine.entry_id                                 7IAL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.1490 
_refine.ls_d_res_low                             54.2800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7000 
_refine.ls_number_reflns_obs                     11730 
_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                       0.2319 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2955 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8000 
_refine.ls_number_reflns_R_free                  563 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               54.3700 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -6.1662 
_refine.aniso_B[2][2]                            -6.1662 
_refine.aniso_B[3][3]                            12.3323 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9310 
_refine.correlation_coeff_Fo_to_Fc_free          0.8930 
_refine.overall_SU_R_Cruickshank_DPI             0.2790 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2370 
_refine.pdbx_overall_SU_R_Blow_DPI               0.3190 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2470 
_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                                104.020 
_refine.B_iso_min                                33.330 
_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                        7IAL 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.330 
_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                       2.1490 
_refine_hist.d_res_low                        54.2800 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.number_atoms_solvent             87 
_refine_hist.number_atoms_total               1602 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           58.10 
_refine_hist.pdbx_B_iso_mean_solvent          53.06 
_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              272  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1585 ?      ? 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 197  ?      ? 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      1225 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1585 0.007  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2162 0.980  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    3.210  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    20.930 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.1500 
_refine_ls_shell.d_res_low                        2.1800 
_refine_ls_shell.pdbx_total_number_of_bins_used   29 
_refine_ls_shell.percent_reflns_obs               96.2500 
_refine_ls_shell.number_reflns_R_work             399 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3806 
_refine_ls_shell.R_factor_R_free                  0.2843 
_refine_ls_shell.percent_reflns_R_free            4.7700 
_refine_ls_shell.number_reflns_R_free             20 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                419 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7IAL 
_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-0029640-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7IAL 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, XChemExplorer, ASAP Discovery Consortium, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7IAL A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7IAL 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 7IAL SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7IAL MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7IAL MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7IAL 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)' 4300 ? 
1 MORE         -26  ? 
1 'SSA (A^2)'  9750 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
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  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N TYR A 9   ? N TYR A 52  O MET B 17  ? O MET B 26  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N 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 GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7IAL 
_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  ? ? -104.09 -155.87 
2 1 CYS B 80  ? ? 82.19   -14.45  
3 1 ALA B 127 ? ? -100.15 79.09   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 337 ? F HOH . 
2 1 B HOH 371 ? F HOH . 
# 
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 -13.9134 -1.5141 -19.5198 -0.0412 -0.0183 -0.2837 0.1773 0.1293 0.0801 3.3526 4.6723 3.8405 
-1.6812 0.8799 0.9476 0.3776 -0.3215 -0.0562 0.4249 0.1435 -0.4012 -0.5990 -0.1976 0.4376 
'X-RAY DIFFRACTION' 2 ? refined -18.4186 1.0220  -15.6759 0.0784  -0.0060 -0.1107 0.1535 0.0173 0.0316 1.2639 1.7781 2.9696 
-0.9535 0.4582 0.0159 0.3100 -0.2963 -0.0137 0.1117 0.1169 0.0794  -0.1543 0.0639  0.2410 
# 
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 
A1B80 N1   N  N N 1   
A1B80 N3   N  N N 2   
A1B80 C4   C  Y N 3   
A1B80 C5   C  Y N 4   
A1B80 C6   C  N N 5   
A1B80 C7   C  N N 6   
A1B80 C8   C  N R 7   
A1B80 C10  C  Y N 8   
A1B80 C13  C  Y N 9   
A1B80 C15  C  N N 10  
A1B80 C17  C  Y N 11  
A1B80 C20  C  Y N 12  
A1B80 C21  C  Y N 13  
A1B80 C22  C  Y N 14  
A1B80 C24  C  Y N 15  
A1B80 C1   C  N N 16  
A1B80 C2   C  Y N 17  
A1B80 C3   C  Y N 18  
A1B80 S1   S  N N 19  
A1B80 O1   O  N N 20  
A1B80 O2   O  N N 21  
A1B80 O3   O  N N 22  
A1B80 N2   N  N N 23  
A1B80 C9   C  Y N 24  
A1B80 C11  C  Y N 25  
A1B80 C12  C  Y N 26  
A1B80 C14  C  Y N 27  
A1B80 C16  C  N N 28  
A1B80 C18  C  Y N 29  
A1B80 C19  C  Y N 30  
A1B80 CL1  CL N N 31  
A1B80 N4   N  Y N 32  
A1B80 N5   N  Y N 33  
A1B80 C23  C  Y N 34  
A1B80 C25  C  Y N 35  
A1B80 H1   H  N N 36  
A1B80 H2   H  N N 37  
A1B80 H4   H  N N 38  
A1B80 H5   H  N N 39  
A1B80 H6   H  N N 40  
A1B80 H7   H  N N 41  
A1B80 H8   H  N N 42  
A1B80 H9   H  N N 43  
A1B80 H10  H  N N 44  
A1B80 H11  H  N N 45  
A1B80 H12  H  N N 46  
A1B80 H13  H  N N 47  
A1B80 H14  H  N N 48  
A1B80 H15  H  N N 49  
A1B80 H16  H  N N 50  
A1B80 H17  H  N N 51  
A1B80 H18  H  N N 52  
A1B80 H19  H  N N 53  
A1B80 H20  H  N N 54  
A1B80 H21  H  N N 55  
A1B80 H22  H  N N 56  
A1B80 H23  H  N N 57  
A1B80 H24  H  N N 58  
A1B80 H25  H  N N 59  
ALA   N    N  N N 60  
ALA   CA   C  N S 61  
ALA   C    C  N N 62  
ALA   O    O  N N 63  
ALA   CB   C  N N 64  
ALA   OXT  O  N N 65  
ALA   H    H  N N 66  
ALA   H2   H  N N 67  
ALA   HA   H  N N 68  
ALA   HB1  H  N N 69  
ALA   HB2  H  N N 70  
ALA   HB3  H  N N 71  
ALA   HXT  H  N N 72  
ARG   N    N  N N 73  
ARG   CA   C  N S 74  
ARG   C    C  N N 75  
ARG   O    O  N N 76  
ARG   CB   C  N N 77  
ARG   CG   C  N N 78  
ARG   CD   C  N N 79  
ARG   NE   N  N N 80  
ARG   CZ   C  N N 81  
ARG   NH1  N  N N 82  
ARG   NH2  N  N N 83  
ARG   OXT  O  N N 84  
ARG   H    H  N N 85  
ARG   H2   H  N N 86  
ARG   HA   H  N N 87  
ARG   HB2  H  N N 88  
ARG   HB3  H  N N 89  
ARG   HG2  H  N N 90  
ARG   HG3  H  N N 91  
ARG   HD2  H  N N 92  
ARG   HD3  H  N N 93  
ARG   HE   H  N N 94  
ARG   HH11 H  N N 95  
ARG   HH12 H  N N 96  
ARG   HH21 H  N N 97  
ARG   HH22 H  N N 98  
ARG   HXT  H  N N 99  
ASN   N    N  N N 100 
ASN   CA   C  N S 101 
ASN   C    C  N N 102 
ASN   O    O  N N 103 
ASN   CB   C  N N 104 
ASN   CG   C  N N 105 
ASN   OD1  O  N N 106 
ASN   ND2  N  N N 107 
ASN   OXT  O  N N 108 
ASN   H    H  N N 109 
ASN   H2   H  N N 110 
ASN   HA   H  N N 111 
ASN   HB2  H  N N 112 
ASN   HB3  H  N N 113 
ASN   HD21 H  N N 114 
ASN   HD22 H  N N 115 
ASN   HXT  H  N N 116 
ASP   N    N  N N 117 
ASP   CA   C  N S 118 
ASP   C    C  N N 119 
ASP   O    O  N N 120 
ASP   CB   C  N N 121 
ASP   CG   C  N N 122 
ASP   OD1  O  N N 123 
ASP   OD2  O  N N 124 
ASP   OXT  O  N N 125 
ASP   H    H  N N 126 
ASP   H2   H  N N 127 
ASP   HA   H  N N 128 
ASP   HB2  H  N N 129 
ASP   HB3  H  N N 130 
ASP   HD2  H  N N 131 
ASP   HXT  H  N N 132 
CYS   N    N  N N 133 
CYS   CA   C  N R 134 
CYS   C    C  N N 135 
CYS   O    O  N N 136 
CYS   CB   C  N N 137 
CYS   SG   S  N N 138 
CYS   OXT  O  N N 139 
CYS   H    H  N N 140 
CYS   H2   H  N N 141 
CYS   HA   H  N N 142 
CYS   HB2  H  N N 143 
CYS   HB3  H  N N 144 
CYS   HG   H  N N 145 
CYS   HXT  H  N N 146 
DMS   S    S  N N 147 
DMS   O    O  N N 148 
DMS   C1   C  N N 149 
DMS   C2   C  N N 150 
DMS   H11  H  N N 151 
DMS   H12  H  N N 152 
DMS   H13  H  N N 153 
DMS   H21  H  N N 154 
DMS   H22  H  N N 155 
DMS   H23  H  N N 156 
GLN   N    N  N N 157 
GLN   CA   C  N S 158 
GLN   C    C  N N 159 
GLN   O    O  N N 160 
GLN   CB   C  N N 161 
GLN   CG   C  N N 162 
GLN   CD   C  N N 163 
GLN   OE1  O  N N 164 
GLN   NE2  N  N N 165 
GLN   OXT  O  N N 166 
GLN   H    H  N N 167 
GLN   H2   H  N N 168 
GLN   HA   H  N N 169 
GLN   HB2  H  N N 170 
GLN   HB3  H  N N 171 
GLN   HG2  H  N N 172 
GLN   HG3  H  N N 173 
GLN   HE21 H  N N 174 
GLN   HE22 H  N N 175 
GLN   HXT  H  N N 176 
GLU   N    N  N N 177 
GLU   CA   C  N S 178 
GLU   C    C  N N 179 
GLU   O    O  N N 180 
GLU   CB   C  N N 181 
GLU   CG   C  N N 182 
GLU   CD   C  N N 183 
GLU   OE1  O  N N 184 
GLU   OE2  O  N N 185 
GLU   OXT  O  N N 186 
GLU   H    H  N N 187 
GLU   H2   H  N N 188 
GLU   HA   H  N N 189 
GLU   HB2  H  N N 190 
GLU   HB3  H  N N 191 
GLU   HG2  H  N N 192 
GLU   HG3  H  N N 193 
GLU   HE2  H  N N 194 
GLU   HXT  H  N N 195 
GLY   N    N  N N 196 
GLY   CA   C  N N 197 
GLY   C    C  N N 198 
GLY   O    O  N N 199 
GLY   OXT  O  N N 200 
GLY   H    H  N N 201 
GLY   H2   H  N N 202 
GLY   HA2  H  N N 203 
GLY   HA3  H  N N 204 
GLY   HXT  H  N N 205 
HIS   N    N  N N 206 
HIS   CA   C  N S 207 
HIS   C    C  N N 208 
HIS   O    O  N N 209 
HIS   CB   C  N N 210 
HIS   CG   C  Y N 211 
HIS   ND1  N  Y N 212 
HIS   CD2  C  Y N 213 
HIS   CE1  C  Y N 214 
HIS   NE2  N  Y N 215 
HIS   OXT  O  N N 216 
HIS   H    H  N N 217 
HIS   H2   H  N N 218 
HIS   HA   H  N N 219 
HIS   HB2  H  N N 220 
HIS   HB3  H  N N 221 
HIS   HD1  H  N N 222 
HIS   HD2  H  N N 223 
HIS   HE1  H  N N 224 
HIS   HE2  H  N N 225 
HIS   HXT  H  N N 226 
HOH   O    O  N N 227 
HOH   H1   H  N N 228 
HOH   H2   H  N N 229 
ILE   N    N  N N 230 
ILE   CA   C  N S 231 
ILE   C    C  N N 232 
ILE   O    O  N N 233 
ILE   CB   C  N S 234 
ILE   CG1  C  N N 235 
ILE   CG2  C  N N 236 
ILE   CD1  C  N N 237 
ILE   OXT  O  N N 238 
ILE   H    H  N N 239 
ILE   H2   H  N N 240 
ILE   HA   H  N N 241 
ILE   HB   H  N N 242 
ILE   HG12 H  N N 243 
ILE   HG13 H  N N 244 
ILE   HG21 H  N N 245 
ILE   HG22 H  N N 246 
ILE   HG23 H  N N 247 
ILE   HD11 H  N N 248 
ILE   HD12 H  N N 249 
ILE   HD13 H  N N 250 
ILE   HXT  H  N N 251 
LEU   N    N  N N 252 
LEU   CA   C  N S 253 
LEU   C    C  N N 254 
LEU   O    O  N N 255 
LEU   CB   C  N N 256 
LEU   CG   C  N N 257 
LEU   CD1  C  N N 258 
LEU   CD2  C  N N 259 
LEU   OXT  O  N N 260 
LEU   H    H  N N 261 
LEU   H2   H  N N 262 
LEU   HA   H  N N 263 
LEU   HB2  H  N N 264 
LEU   HB3  H  N N 265 
LEU   HG   H  N N 266 
LEU   HD11 H  N N 267 
LEU   HD12 H  N N 268 
LEU   HD13 H  N N 269 
LEU   HD21 H  N N 270 
LEU   HD22 H  N N 271 
LEU   HD23 H  N N 272 
LEU   HXT  H  N N 273 
LYS   N    N  N N 274 
LYS   CA   C  N S 275 
LYS   C    C  N N 276 
LYS   O    O  N N 277 
LYS   CB   C  N N 278 
LYS   CG   C  N N 279 
LYS   CD   C  N N 280 
LYS   CE   C  N N 281 
LYS   NZ   N  N N 282 
LYS   OXT  O  N N 283 
LYS   H    H  N N 284 
LYS   H2   H  N N 285 
LYS   HA   H  N N 286 
LYS   HB2  H  N N 287 
LYS   HB3  H  N N 288 
LYS   HG2  H  N N 289 
LYS   HG3  H  N N 290 
LYS   HD2  H  N N 291 
LYS   HD3  H  N N 292 
LYS   HE2  H  N N 293 
LYS   HE3  H  N N 294 
LYS   HZ1  H  N N 295 
LYS   HZ2  H  N N 296 
LYS   HZ3  H  N N 297 
LYS   HXT  H  N N 298 
MET   N    N  N N 299 
MET   CA   C  N S 300 
MET   C    C  N N 301 
MET   O    O  N N 302 
MET   CB   C  N N 303 
MET   CG   C  N N 304 
MET   SD   S  N N 305 
MET   CE   C  N N 306 
MET   OXT  O  N N 307 
MET   H    H  N N 308 
MET   H2   H  N N 309 
MET   HA   H  N N 310 
MET   HB2  H  N N 311 
MET   HB3  H  N N 312 
MET   HG2  H  N N 313 
MET   HG3  H  N N 314 
MET   HE1  H  N N 315 
MET   HE2  H  N N 316 
MET   HE3  H  N N 317 
MET   HXT  H  N N 318 
PHE   N    N  N N 319 
PHE   CA   C  N S 320 
PHE   C    C  N N 321 
PHE   O    O  N N 322 
PHE   CB   C  N N 323 
PHE   CG   C  Y N 324 
PHE   CD1  C  Y N 325 
PHE   CD2  C  Y N 326 
PHE   CE1  C  Y N 327 
PHE   CE2  C  Y N 328 
PHE   CZ   C  Y N 329 
PHE   OXT  O  N N 330 
PHE   H    H  N N 331 
PHE   H2   H  N N 332 
PHE   HA   H  N N 333 
PHE   HB2  H  N N 334 
PHE   HB3  H  N N 335 
PHE   HD1  H  N N 336 
PHE   HD2  H  N N 337 
PHE   HE1  H  N N 338 
PHE   HE2  H  N N 339 
PHE   HZ   H  N N 340 
PHE   HXT  H  N N 341 
PRO   N    N  N N 342 
PRO   CA   C  N S 343 
PRO   C    C  N N 344 
PRO   O    O  N N 345 
PRO   CB   C  N N 346 
PRO   CG   C  N N 347 
PRO   CD   C  N N 348 
PRO   OXT  O  N N 349 
PRO   H    H  N N 350 
PRO   HA   H  N N 351 
PRO   HB2  H  N N 352 
PRO   HB3  H  N N 353 
PRO   HG2  H  N N 354 
PRO   HG3  H  N N 355 
PRO   HD2  H  N N 356 
PRO   HD3  H  N N 357 
PRO   HXT  H  N N 358 
SER   N    N  N N 359 
SER   CA   C  N S 360 
SER   C    C  N N 361 
SER   O    O  N N 362 
SER   CB   C  N N 363 
SER   OG   O  N N 364 
SER   OXT  O  N N 365 
SER   H    H  N N 366 
SER   H2   H  N N 367 
SER   HA   H  N N 368 
SER   HB2  H  N N 369 
SER   HB3  H  N N 370 
SER   HG   H  N N 371 
SER   HXT  H  N N 372 
THR   N    N  N N 373 
THR   CA   C  N S 374 
THR   C    C  N N 375 
THR   O    O  N N 376 
THR   CB   C  N R 377 
THR   OG1  O  N N 378 
THR   CG2  C  N N 379 
THR   OXT  O  N N 380 
THR   H    H  N N 381 
THR   H2   H  N N 382 
THR   HA   H  N N 383 
THR   HB   H  N N 384 
THR   HG1  H  N N 385 
THR   HG21 H  N N 386 
THR   HG22 H  N N 387 
THR   HG23 H  N N 388 
THR   HXT  H  N N 389 
TRP   N    N  N N 390 
TRP   CA   C  N S 391 
TRP   C    C  N N 392 
TRP   O    O  N N 393 
TRP   CB   C  N N 394 
TRP   CG   C  Y N 395 
TRP   CD1  C  Y N 396 
TRP   CD2  C  Y N 397 
TRP   NE1  N  Y N 398 
TRP   CE2  C  Y N 399 
TRP   CE3  C  Y N 400 
TRP   CZ2  C  Y N 401 
TRP   CZ3  C  Y N 402 
TRP   CH2  C  Y N 403 
TRP   OXT  O  N N 404 
TRP   H    H  N N 405 
TRP   H2   H  N N 406 
TRP   HA   H  N N 407 
TRP   HB2  H  N N 408 
TRP   HB3  H  N N 409 
TRP   HD1  H  N N 410 
TRP   HE1  H  N N 411 
TRP   HE3  H  N N 412 
TRP   HZ2  H  N N 413 
TRP   HZ3  H  N N 414 
TRP   HH2  H  N N 415 
TRP   HXT  H  N N 416 
TYR   N    N  N N 417 
TYR   CA   C  N S 418 
TYR   C    C  N N 419 
TYR   O    O  N N 420 
TYR   CB   C  N N 421 
TYR   CG   C  Y N 422 
TYR   CD1  C  Y N 423 
TYR   CD2  C  Y N 424 
TYR   CE1  C  Y N 425 
TYR   CE2  C  Y N 426 
TYR   CZ   C  Y N 427 
TYR   OH   O  N N 428 
TYR   OXT  O  N N 429 
TYR   H    H  N N 430 
TYR   H2   H  N N 431 
TYR   HA   H  N N 432 
TYR   HB2  H  N N 433 
TYR   HB3  H  N N 434 
TYR   HD1  H  N N 435 
TYR   HD2  H  N N 436 
TYR   HE1  H  N N 437 
TYR   HE2  H  N N 438 
TYR   HH   H  N N 439 
TYR   HXT  H  N N 440 
VAL   N    N  N N 441 
VAL   CA   C  N S 442 
VAL   C    C  N N 443 
VAL   O    O  N N 444 
VAL   CB   C  N N 445 
VAL   CG1  C  N N 446 
VAL   CG2  C  N N 447 
VAL   OXT  O  N N 448 
VAL   H    H  N N 449 
VAL   H2   H  N N 450 
VAL   HA   H  N N 451 
VAL   HB   H  N N 452 
VAL   HG11 H  N N 453 
VAL   HG12 H  N N 454 
VAL   HG13 H  N N 455 
VAL   HG21 H  N N 456 
VAL   HG22 H  N N 457 
VAL   HG23 H  N N 458 
VAL   HXT  H  N N 459 
# 
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 
A1B80 CL1 C19  sing N N 1   
A1B80 C20 C19  doub Y N 2   
A1B80 C20 C21  sing Y N 3   
A1B80 N4  C21  sing Y N 4   
A1B80 N4  N5   sing Y N 5   
A1B80 C19 C18  sing Y N 6   
A1B80 C21 C23  doub Y N 7   
A1B80 N5  C22  doub Y N 8   
A1B80 C18 C17  doub Y N 9   
A1B80 C23 C22  sing Y N 10  
A1B80 C23 C17  sing Y N 11  
A1B80 C17 C8   sing N N 12  
A1B80 O2  S1   doub N N 13  
A1B80 C4  C3   doub Y N 14  
A1B80 C4  C5   sing Y N 15  
A1B80 C6  S1   sing N N 16  
A1B80 C6  N1   sing N N 17  
A1B80 C3  C2   sing Y N 18  
A1B80 S1  C5   sing N N 19  
A1B80 S1  O1   doub N N 20  
A1B80 O3  C7   doub N N 21  
A1B80 C8  C7   sing N N 22  
A1B80 C8  N2   sing N N 23  
A1B80 C5  C24  doub Y N 24  
A1B80 C7  N1   sing N N 25  
A1B80 C2  C1   sing N N 26  
A1B80 C2  C25  doub Y N 27  
A1B80 N2  C9   sing N N 28  
A1B80 C24 C25  sing Y N 29  
A1B80 C9  C14  doub Y N 30  
A1B80 C9  C10  sing Y N 31  
A1B80 C14 C13  sing Y N 32  
A1B80 C10 C11  doub Y N 33  
A1B80 C13 C12  doub Y N 34  
A1B80 C13 C15  sing N N 35  
A1B80 C11 C12  sing Y N 36  
A1B80 C12 C16  sing N N 37  
A1B80 C15 N3   sing N N 38  
A1B80 C16 N3   sing N N 39  
A1B80 N1  H1   sing N N 40  
A1B80 N3  H2   sing N N 41  
A1B80 C4  H4   sing N N 42  
A1B80 C6  H5   sing N N 43  
A1B80 C6  H6   sing N N 44  
A1B80 C8  H7   sing N N 45  
A1B80 C10 H8   sing N N 46  
A1B80 C15 H9   sing N N 47  
A1B80 C15 H10  sing N N 48  
A1B80 C20 H11  sing N N 49  
A1B80 C22 H12  sing N N 50  
A1B80 C24 H13  sing N N 51  
A1B80 C1  H14  sing N N 52  
A1B80 C1  H15  sing N N 53  
A1B80 C1  H16  sing N N 54  
A1B80 C3  H17  sing N N 55  
A1B80 N2  H18  sing N N 56  
A1B80 C11 H19  sing N N 57  
A1B80 C14 H20  sing N N 58  
A1B80 C16 H21  sing N N 59  
A1B80 C16 H22  sing N N 60  
A1B80 C18 H23  sing N N 61  
A1B80 N4  H24  sing N N 62  
A1B80 C25 H25  sing N N 63  
ALA   N   CA   sing N N 64  
ALA   N   H    sing N N 65  
ALA   N   H2   sing N N 66  
ALA   CA  C    sing N N 67  
ALA   CA  CB   sing N N 68  
ALA   CA  HA   sing N N 69  
ALA   C   O    doub N N 70  
ALA   C   OXT  sing N N 71  
ALA   CB  HB1  sing N N 72  
ALA   CB  HB2  sing N N 73  
ALA   CB  HB3  sing N N 74  
ALA   OXT HXT  sing N N 75  
ARG   N   CA   sing N N 76  
ARG   N   H    sing N N 77  
ARG   N   H2   sing N N 78  
ARG   CA  C    sing N N 79  
ARG   CA  CB   sing N N 80  
ARG   CA  HA   sing N N 81  
ARG   C   O    doub N N 82  
ARG   C   OXT  sing N N 83  
ARG   CB  CG   sing N N 84  
ARG   CB  HB2  sing N N 85  
ARG   CB  HB3  sing N N 86  
ARG   CG  CD   sing N N 87  
ARG   CG  HG2  sing N N 88  
ARG   CG  HG3  sing N N 89  
ARG   CD  NE   sing N N 90  
ARG   CD  HD2  sing N N 91  
ARG   CD  HD3  sing N N 92  
ARG   NE  CZ   sing N N 93  
ARG   NE  HE   sing N N 94  
ARG   CZ  NH1  sing N N 95  
ARG   CZ  NH2  doub N N 96  
ARG   NH1 HH11 sing N N 97  
ARG   NH1 HH12 sing N N 98  
ARG   NH2 HH21 sing N N 99  
ARG   NH2 HH22 sing N N 100 
ARG   OXT HXT  sing N N 101 
ASN   N   CA   sing N N 102 
ASN   N   H    sing N N 103 
ASN   N   H2   sing N N 104 
ASN   CA  C    sing N N 105 
ASN   CA  CB   sing N N 106 
ASN   CA  HA   sing N N 107 
ASN   C   O    doub N N 108 
ASN   C   OXT  sing N N 109 
ASN   CB  CG   sing N N 110 
ASN   CB  HB2  sing N N 111 
ASN   CB  HB3  sing N N 112 
ASN   CG  OD1  doub N N 113 
ASN   CG  ND2  sing N N 114 
ASN   ND2 HD21 sing N N 115 
ASN   ND2 HD22 sing N N 116 
ASN   OXT HXT  sing N N 117 
ASP   N   CA   sing N N 118 
ASP   N   H    sing N N 119 
ASP   N   H2   sing N N 120 
ASP   CA  C    sing N N 121 
ASP   CA  CB   sing N N 122 
ASP   CA  HA   sing N N 123 
ASP   C   O    doub N N 124 
ASP   C   OXT  sing N N 125 
ASP   CB  CG   sing N N 126 
ASP   CB  HB2  sing N N 127 
ASP   CB  HB3  sing N N 128 
ASP   CG  OD1  doub N N 129 
ASP   CG  OD2  sing N N 130 
ASP   OD2 HD2  sing N N 131 
ASP   OXT HXT  sing N N 132 
CYS   N   CA   sing N N 133 
CYS   N   H    sing N N 134 
CYS   N   H2   sing N N 135 
CYS   CA  C    sing N N 136 
CYS   CA  CB   sing N N 137 
CYS   CA  HA   sing N N 138 
CYS   C   O    doub N N 139 
CYS   C   OXT  sing N N 140 
CYS   CB  SG   sing N N 141 
CYS   CB  HB2  sing N N 142 
CYS   CB  HB3  sing N N 143 
CYS   SG  HG   sing N N 144 
CYS   OXT HXT  sing N N 145 
DMS   S   O    doub N N 146 
DMS   S   C1   sing N N 147 
DMS   S   C2   sing N N 148 
DMS   C1  H11  sing N N 149 
DMS   C1  H12  sing N N 150 
DMS   C1  H13  sing N N 151 
DMS   C2  H21  sing N N 152 
DMS   C2  H22  sing N N 153 
DMS   C2  H23  sing N N 154 
GLN   N   CA   sing N N 155 
GLN   N   H    sing N N 156 
GLN   N   H2   sing N N 157 
GLN   CA  C    sing N N 158 
GLN   CA  CB   sing N N 159 
GLN   CA  HA   sing N N 160 
GLN   C   O    doub N N 161 
GLN   C   OXT  sing N N 162 
GLN   CB  CG   sing N N 163 
GLN   CB  HB2  sing N N 164 
GLN   CB  HB3  sing N N 165 
GLN   CG  CD   sing N N 166 
GLN   CG  HG2  sing N N 167 
GLN   CG  HG3  sing N N 168 
GLN   CD  OE1  doub N N 169 
GLN   CD  NE2  sing N N 170 
GLN   NE2 HE21 sing N N 171 
GLN   NE2 HE22 sing N N 172 
GLN   OXT HXT  sing N N 173 
GLU   N   CA   sing N N 174 
GLU   N   H    sing N N 175 
GLU   N   H2   sing N N 176 
GLU   CA  C    sing N N 177 
GLU   CA  CB   sing N N 178 
GLU   CA  HA   sing N N 179 
GLU   C   O    doub N N 180 
GLU   C   OXT  sing N N 181 
GLU   CB  CG   sing N N 182 
GLU   CB  HB2  sing N N 183 
GLU   CB  HB3  sing N N 184 
GLU   CG  CD   sing N N 185 
GLU   CG  HG2  sing N N 186 
GLU   CG  HG3  sing N N 187 
GLU   CD  OE1  doub N N 188 
GLU   CD  OE2  sing N N 189 
GLU   OE2 HE2  sing N N 190 
GLU   OXT HXT  sing N N 191 
GLY   N   CA   sing N N 192 
GLY   N   H    sing N N 193 
GLY   N   H2   sing N N 194 
GLY   CA  C    sing N N 195 
GLY   CA  HA2  sing N N 196 
GLY   CA  HA3  sing N N 197 
GLY   C   O    doub N N 198 
GLY   C   OXT  sing N N 199 
GLY   OXT HXT  sing N N 200 
HIS   N   CA   sing N N 201 
HIS   N   H    sing N N 202 
HIS   N   H2   sing N N 203 
HIS   CA  C    sing N N 204 
HIS   CA  CB   sing N N 205 
HIS   CA  HA   sing N N 206 
HIS   C   O    doub N N 207 
HIS   C   OXT  sing N N 208 
HIS   CB  CG   sing N N 209 
HIS   CB  HB2  sing N N 210 
HIS   CB  HB3  sing N N 211 
HIS   CG  ND1  sing Y N 212 
HIS   CG  CD2  doub Y N 213 
HIS   ND1 CE1  doub Y N 214 
HIS   ND1 HD1  sing N N 215 
HIS   CD2 NE2  sing Y N 216 
HIS   CD2 HD2  sing N N 217 
HIS   CE1 NE2  sing Y N 218 
HIS   CE1 HE1  sing N N 219 
HIS   NE2 HE2  sing N N 220 
HIS   OXT HXT  sing N N 221 
HOH   O   H1   sing N N 222 
HOH   O   H2   sing N N 223 
ILE   N   CA   sing N N 224 
ILE   N   H    sing N N 225 
ILE   N   H2   sing N N 226 
ILE   CA  C    sing N N 227 
ILE   CA  CB   sing N N 228 
ILE   CA  HA   sing N N 229 
ILE   C   O    doub N N 230 
ILE   C   OXT  sing N N 231 
ILE   CB  CG1  sing N N 232 
ILE   CB  CG2  sing N N 233 
ILE   CB  HB   sing N N 234 
ILE   CG1 CD1  sing N N 235 
ILE   CG1 HG12 sing N N 236 
ILE   CG1 HG13 sing N N 237 
ILE   CG2 HG21 sing N N 238 
ILE   CG2 HG22 sing N N 239 
ILE   CG2 HG23 sing N N 240 
ILE   CD1 HD11 sing N N 241 
ILE   CD1 HD12 sing N N 242 
ILE   CD1 HD13 sing N N 243 
ILE   OXT HXT  sing N N 244 
LEU   N   CA   sing N N 245 
LEU   N   H    sing N N 246 
LEU   N   H2   sing N N 247 
LEU   CA  C    sing N N 248 
LEU   CA  CB   sing N N 249 
LEU   CA  HA   sing N N 250 
LEU   C   O    doub N N 251 
LEU   C   OXT  sing N N 252 
LEU   CB  CG   sing N N 253 
LEU   CB  HB2  sing N N 254 
LEU   CB  HB3  sing N N 255 
LEU   CG  CD1  sing N N 256 
LEU   CG  CD2  sing N N 257 
LEU   CG  HG   sing N N 258 
LEU   CD1 HD11 sing N N 259 
LEU   CD1 HD12 sing N N 260 
LEU   CD1 HD13 sing N N 261 
LEU   CD2 HD21 sing N N 262 
LEU   CD2 HD22 sing N N 263 
LEU   CD2 HD23 sing N N 264 
LEU   OXT HXT  sing N N 265 
LYS   N   CA   sing N N 266 
LYS   N   H    sing N N 267 
LYS   N   H2   sing N N 268 
LYS   CA  C    sing N N 269 
LYS   CA  CB   sing N N 270 
LYS   CA  HA   sing N N 271 
LYS   C   O    doub N N 272 
LYS   C   OXT  sing N N 273 
LYS   CB  CG   sing N N 274 
LYS   CB  HB2  sing N N 275 
LYS   CB  HB3  sing N N 276 
LYS   CG  CD   sing N N 277 
LYS   CG  HG2  sing N N 278 
LYS   CG  HG3  sing N N 279 
LYS   CD  CE   sing N N 280 
LYS   CD  HD2  sing N N 281 
LYS   CD  HD3  sing N N 282 
LYS   CE  NZ   sing N N 283 
LYS   CE  HE2  sing N N 284 
LYS   CE  HE3  sing N N 285 
LYS   NZ  HZ1  sing N N 286 
LYS   NZ  HZ2  sing N N 287 
LYS   NZ  HZ3  sing N N 288 
LYS   OXT HXT  sing N N 289 
MET   N   CA   sing N N 290 
MET   N   H    sing N N 291 
MET   N   H2   sing N N 292 
MET   CA  C    sing N N 293 
MET   CA  CB   sing N N 294 
MET   CA  HA   sing N N 295 
MET   C   O    doub N N 296 
MET   C   OXT  sing N N 297 
MET   CB  CG   sing N N 298 
MET   CB  HB2  sing N N 299 
MET   CB  HB3  sing N N 300 
MET   CG  SD   sing N N 301 
MET   CG  HG2  sing N N 302 
MET   CG  HG3  sing N N 303 
MET   SD  CE   sing N N 304 
MET   CE  HE1  sing N N 305 
MET   CE  HE2  sing N N 306 
MET   CE  HE3  sing N N 307 
MET   OXT HXT  sing N N 308 
PHE   N   CA   sing N N 309 
PHE   N   H    sing N N 310 
PHE   N   H2   sing N N 311 
PHE   CA  C    sing N N 312 
PHE   CA  CB   sing N N 313 
PHE   CA  HA   sing N N 314 
PHE   C   O    doub N N 315 
PHE   C   OXT  sing N N 316 
PHE   CB  CG   sing N N 317 
PHE   CB  HB2  sing N N 318 
PHE   CB  HB3  sing N N 319 
PHE   CG  CD1  doub Y N 320 
PHE   CG  CD2  sing Y N 321 
PHE   CD1 CE1  sing Y N 322 
PHE   CD1 HD1  sing N N 323 
PHE   CD2 CE2  doub Y N 324 
PHE   CD2 HD2  sing N N 325 
PHE   CE1 CZ   doub Y N 326 
PHE   CE1 HE1  sing N N 327 
PHE   CE2 CZ   sing Y N 328 
PHE   CE2 HE2  sing N N 329 
PHE   CZ  HZ   sing N N 330 
PHE   OXT HXT  sing N N 331 
PRO   N   CA   sing N N 332 
PRO   N   CD   sing N N 333 
PRO   N   H    sing N N 334 
PRO   CA  C    sing N N 335 
PRO   CA  CB   sing N N 336 
PRO   CA  HA   sing N N 337 
PRO   C   O    doub N N 338 
PRO   C   OXT  sing N N 339 
PRO   CB  CG   sing N N 340 
PRO   CB  HB2  sing N N 341 
PRO   CB  HB3  sing N N 342 
PRO   CG  CD   sing N N 343 
PRO   CG  HG2  sing N N 344 
PRO   CG  HG3  sing N N 345 
PRO   CD  HD2  sing N N 346 
PRO   CD  HD3  sing N N 347 
PRO   OXT HXT  sing N N 348 
SER   N   CA   sing N N 349 
SER   N   H    sing N N 350 
SER   N   H2   sing N N 351 
SER   CA  C    sing N N 352 
SER   CA  CB   sing N N 353 
SER   CA  HA   sing N N 354 
SER   C   O    doub N N 355 
SER   C   OXT  sing N N 356 
SER   CB  OG   sing N N 357 
SER   CB  HB2  sing N N 358 
SER   CB  HB3  sing N N 359 
SER   OG  HG   sing N N 360 
SER   OXT HXT  sing N N 361 
THR   N   CA   sing N N 362 
THR   N   H    sing N N 363 
THR   N   H2   sing N N 364 
THR   CA  C    sing N N 365 
THR   CA  CB   sing N N 366 
THR   CA  HA   sing N N 367 
THR   C   O    doub N N 368 
THR   C   OXT  sing N N 369 
THR   CB  OG1  sing N N 370 
THR   CB  CG2  sing N N 371 
THR   CB  HB   sing N N 372 
THR   OG1 HG1  sing N N 373 
THR   CG2 HG21 sing N N 374 
THR   CG2 HG22 sing N N 375 
THR   CG2 HG23 sing N N 376 
THR   OXT HXT  sing N N 377 
TRP   N   CA   sing N N 378 
TRP   N   H    sing N N 379 
TRP   N   H2   sing N N 380 
TRP   CA  C    sing N N 381 
TRP   CA  CB   sing N N 382 
TRP   CA  HA   sing N N 383 
TRP   C   O    doub N N 384 
TRP   C   OXT  sing N N 385 
TRP   CB  CG   sing N N 386 
TRP   CB  HB2  sing N N 387 
TRP   CB  HB3  sing N N 388 
TRP   CG  CD1  doub Y N 389 
TRP   CG  CD2  sing Y N 390 
TRP   CD1 NE1  sing Y N 391 
TRP   CD1 HD1  sing N N 392 
TRP   CD2 CE2  doub Y N 393 
TRP   CD2 CE3  sing Y N 394 
TRP   NE1 CE2  sing Y N 395 
TRP   NE1 HE1  sing N N 396 
TRP   CE2 CZ2  sing Y N 397 
TRP   CE3 CZ3  doub Y N 398 
TRP   CE3 HE3  sing N N 399 
TRP   CZ2 CH2  doub Y N 400 
TRP   CZ2 HZ2  sing N N 401 
TRP   CZ3 CH2  sing Y N 402 
TRP   CZ3 HZ3  sing N N 403 
TRP   CH2 HH2  sing N N 404 
TRP   OXT HXT  sing N N 405 
TYR   N   CA   sing N N 406 
TYR   N   H    sing N N 407 
TYR   N   H2   sing N N 408 
TYR   CA  C    sing N N 409 
TYR   CA  CB   sing N N 410 
TYR   CA  HA   sing N N 411 
TYR   C   O    doub N N 412 
TYR   C   OXT  sing N N 413 
TYR   CB  CG   sing N N 414 
TYR   CB  HB2  sing N N 415 
TYR   CB  HB3  sing N N 416 
TYR   CG  CD1  doub Y N 417 
TYR   CG  CD2  sing Y N 418 
TYR   CD1 CE1  sing Y N 419 
TYR   CD1 HD1  sing N N 420 
TYR   CD2 CE2  doub Y N 421 
TYR   CD2 HD2  sing N N 422 
TYR   CE1 CZ   doub Y N 423 
TYR   CE1 HE1  sing N N 424 
TYR   CE2 CZ   sing Y N 425 
TYR   CE2 HE2  sing N N 426 
TYR   CZ  OH   sing N N 427 
TYR   OH  HH   sing N N 428 
TYR   OXT HXT  sing N N 429 
VAL   N   CA   sing N N 430 
VAL   N   H    sing N N 431 
VAL   N   H2   sing N N 432 
VAL   CA  C    sing N N 433 
VAL   CA  CB   sing N N 434 
VAL   CA  HA   sing N N 435 
VAL   C   O    doub N N 436 
VAL   C   OXT  sing N N 437 
VAL   CB  CG1  sing N N 438 
VAL   CB  CG2  sing N N 439 
VAL   CB  HB   sing N N 440 
VAL   CG1 HG11 sing N N 441 
VAL   CG1 HG12 sing N N 442 
VAL   CG1 HG13 sing N N 443 
VAL   CG2 HG21 sing N N 444 
VAL   CG2 HG22 sing N N 445 
VAL   CG2 HG23 sing N N 446 
VAL   OXT HXT  sing N N 447 
# 
_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                    7IAL 
_atom_sites.fract_transf_matrix[1][1]   0.023484 
_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]   0.023484 
_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]   0.004606 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ASP   A 1 7   ? -20.919 19.471  -7.558  1.00 63.18  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.111 18.624  -7.543  1.00 63.21  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.307 17.912  -8.898  1.00 61.03  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.430 18.563  -9.943  1.00 61.13  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.351 19.435  -7.123  1.00 66.76  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.610 18.600  -7.015  1.00 74.94  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -24.860 18.032  -5.914  1.00 76.11  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -25.352 18.509  -8.028  1.00 78.44  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.318 16.568  -8.869  1.00 58.55  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.433 15.743  -10.065 1.00 56.37  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.857 15.490  -10.562 1.00 54.15  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.802 15.424  -9.775  1.00 53.81  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.708 14.413  -9.869  1.00 56.66  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.260 14.575  -9.568  1.00 57.78  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.460 12.991  -9.280  1.00 59.63  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.773 13.547  -9.111  1.00 57.34  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.989 15.324  -11.890 1.00 52.50  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.261 15.063  -12.557 1.00 51.44  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -25.128 14.080  -13.719 1.00 50.68  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -24.052 13.945  -14.293 1.00 50.29  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.936 16.360  -13.019 1.00 51.22  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -25.165 17.139  -14.066 1.00 52.11  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.206 18.075  -13.697 1.00 52.87  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.475 17.024  -15.419 1.00 52.80  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.514 18.813  -14.649 1.00 53.73  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.792 17.760  -16.381 1.00 53.49  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.810 18.654  -15.990 1.00 54.70  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -23.104 19.378  -16.922 1.00 56.65  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.230 13.403  -14.081 1.00 50.20  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -26.207 12.451  -15.181 1.00 50.13  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.988 12.932  -16.423 1.00 50.74  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.998 13.652  -16.318 1.00 51.50  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.647 11.040  -14.731 1.00 50.31  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -28.096 11.027  -14.206 1.00 50.92  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.663 10.454  -13.721 1.00 50.64  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.645 9.635   -14.003 1.00 51.58  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.499 12.538  -17.605 1.00 50.50  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.108 12.877  -18.898 1.00 51.07  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.185 11.629  -19.731 1.00 51.93  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -26.161 10.979  -19.897 1.00 52.77  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.232 13.866  -19.653 1.00 52.84  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.305 15.282  -19.132 1.00 58.81  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.495 16.262  -19.958 1.00 66.86  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.556 15.826  -20.663 1.00 67.45  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.792 17.477  -19.886 1.00 69.93  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.353 11.300  -20.299 1.00 51.65  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.470 10.092  -21.119 1.00 51.76  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.552 10.139  -22.334 1.00 51.99  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.438 11.190  -22.958 1.00 52.53  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.922 9.855   -21.549 1.00 52.64  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -30.167 8.406   -21.925 1.00 54.71  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.626 8.034   -22.025 1.00 56.50  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.758 6.600   -22.260 1.00 58.28  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.837 6.047   -23.466 1.00 60.61  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.857 6.809   -24.556 1.00 61.78  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.909 4.727   -23.594 1.00 58.99  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.868 9.024   -22.659 1.00 51.36  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -26.005 8.994   -23.855 1.00 51.51  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.372 7.922   -24.882 1.00 51.70  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.731 7.854   -25.924 1.00 52.61  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.537 8.877   -23.480 1.00 51.58  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.389 7.113   -24.612 1.00 51.14  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.812 6.093   -25.561 1.00 51.09  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.359 4.819   -24.958 1.00 51.22  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.425 4.677   -23.731 1.00 50.22  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.804 3.902   -25.843 1.00 51.27  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.339 2.596   -25.467 1.00 51.89  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -28.198 1.621   -25.315 1.00 53.52  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -27.173 1.769   -25.978 1.00 54.00  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.259 2.040   -26.568 1.00 52.35  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.574 2.744   -26.727 1.00 57.05  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.784 3.771   -26.046 1.00 55.62  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.384 2.308   -27.583 1.00 60.83  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.403 0.577   -24.515 1.00 54.02  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.408 -0.462  -24.365 1.00 55.05  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.806 -1.608  -25.276 1.00 56.38  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.665 -2.425  -24.938 1.00 55.78  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -27.251 -0.838  -22.897 1.00 55.51  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.777 0.396   -22.122 1.00 56.58  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.272 -1.977  -22.772 1.00 55.86  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.739 0.242   -20.664 1.00 58.50  ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -27.222 -1.621  -26.480 0.50 57.39  ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -27.224 -1.630  -26.476 0.50 57.33  ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -27.508 -2.615  -27.514 0.50 58.69  ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -27.537 -2.642  -27.478 0.50 58.56  ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -26.239 -3.099  -28.189 0.50 59.88  ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -26.267 -3.090  -28.211 0.50 59.82  ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -25.310 -2.318  -28.374 0.50 59.70  ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -25.338 -2.301  -28.386 0.50 59.62  ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -28.379 -1.994  -28.620 0.50 60.04  ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -28.690 -2.137  -28.401 0.50 59.72  ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -27.730 -0.822  -29.121 0.50 60.99  ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -29.781 -3.061  -28.373 0.50 60.62  ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -29.796 -1.668  -28.154 0.50 60.40  ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -28.259 -1.859  -29.850 0.50 59.90  ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -26.227 -4.362  -28.629 1.00 61.08  ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -25.097 -4.910  -29.386 1.00 64.19  ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -25.218 -4.382  -30.843 1.00 67.54  ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -26.295 -4.439  -31.430 1.00 68.02  ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -25.166 -6.447  -29.376 1.00 64.10  ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -24.131 -7.149  -30.209 1.00 64.91  ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -24.250 -7.525  -31.518 1.00 65.92  ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -22.888 -7.691  -29.749 1.00 65.09  ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -23.123 -8.201  -31.919 1.00 66.29  ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -22.287 -8.351  -30.840 1.00 66.06  ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -22.199 -7.645  -28.531 1.00 65.33  ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -21.043 -8.975  -30.740 1.00 66.59  ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -20.995 -8.305  -28.423 1.00 66.03  ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -20.413 -8.931  -29.524 1.00 66.34  ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -24.136 -3.839  -31.410 1.00 69.84  ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -24.152 -3.316  -32.775 1.00 72.32  ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -23.493 -4.313  -33.723 1.00 75.36  ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -22.291 -4.555  -33.604 1.00 75.59  ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -23.424 -1.951  -32.857 1.00 75.09  ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -23.176 -1.446  -34.281 1.00 82.32  ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -22.410 -0.144  -34.441 1.00 89.82  ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -22.088 0.486   -33.407 1.00 92.46  ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -22.139 0.251   -35.599 1.00 91.23  ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -24.259 -4.879  -34.675 1.00 77.55  ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -23.676 -5.799  -35.647 1.00 80.37  ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -22.835 -4.959  -36.605 1.00 81.98  ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -23.256 -3.864  -36.993 1.00 82.16  ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -24.763 -6.570  -36.415 1.00 84.15  ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -25.522 -7.585  -35.558 1.00 90.12  ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -26.846 -8.022  -36.224 1.00 95.70  ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -28.036 -7.294  -35.619 1.00 100.25 ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -29.332 -7.745  -36.201 1.00 102.67 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -21.628 -5.438  -36.931 1.00 82.80  ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -20.694 -4.716  -37.798 1.00 84.07  ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -20.146 -3.450  -37.131 1.00 84.05  ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -20.201 -2.355  -37.696 1.00 84.38  ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -21.277 -4.416  -39.195 1.00 86.97  ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -21.541 -5.653  -40.026 1.00 93.54  ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -20.731 -6.609  -39.943 1.00 95.44  ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -22.548 -5.661  -40.774 1.00 95.36  ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -19.641 -3.608  -35.914 1.00 83.39  ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -18.984 -2.532  -35.183 1.00 82.98  ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -17.469 -2.662  -35.462 1.00 82.81  ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -17.015 -3.710  -35.949 1.00 82.59  ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -19.263 -2.674  -33.695 1.00 82.81  ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -16.686 -1.609  -35.183 1.00 82.59  ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -15.239 -1.663  -35.413 1.00 82.66  ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -14.573 -2.683  -34.472 1.00 81.25  ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -14.604 -2.510  -33.258 1.00 80.79  ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -14.616 -0.272  -35.231 1.00 86.54  ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -13.111 -0.235  -35.438 1.00 93.33  ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -12.380 0.738   -34.530 1.00 101.60 ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -13.042 1.626   -33.941 1.00 102.53 ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -11.138 0.609   -34.410 1.00 104.02 ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -14.011 -3.763  -35.040 1.00 80.24  ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -13.344 -4.815  -34.273 1.00 79.64  ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -11.870 -4.465  -34.083 1.00 78.36  ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -11.129 -4.428  -35.057 1.00 78.67  ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -13.495 -6.219  -34.916 1.00 80.48  ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -13.049 -7.295  -33.943 1.00 81.06  ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -14.926 -6.477  -35.374 1.00 80.91  ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -11.441 -4.200  -32.840 1.00 76.95  ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -10.046 -3.848  -32.548 1.00 75.98  ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -9.629  -4.332  -31.140 1.00 74.91  ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -10.455 -4.868  -30.416 1.00 74.82  ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -9.816  -2.339  -32.779 1.00 77.21  ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -8.411  -2.100  -32.860 1.00 78.58  ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -10.422 -1.487  -31.683 1.00 76.95  ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -8.355  -4.195  -30.782 1.00 73.98  ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -7.874  -4.611  -29.473 1.00 73.37  ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -7.368  -6.037  -29.402 1.00 72.56  ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -7.970  -6.961  -29.956 1.00 72.42  ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -6.257  -6.225  -28.696 1.00 71.64  ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -5.692  -7.547  -28.489 1.00 71.20  ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -6.235  -8.187  -27.166 1.00 69.12  ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -7.034  -7.565  -26.465 1.00 69.18  ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -4.158  -7.490  -28.565 1.00 73.75  ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -3.532  -6.797  -27.389 1.00 78.59  ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.991  -5.740  -26.944 1.00 80.12  ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -2.463  -7.380  -26.857 1.00 79.69  ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -5.888  -9.447  -26.875 1.00 67.21  ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -6.379  -10.157 -25.686 1.00 66.08  ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -5.243  -10.732 -24.849 1.00 65.05  ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -4.951  -11.918 -24.928 1.00 65.06  ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -7.360  -11.259 -26.076 1.00 67.02  ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -7.100  -11.860 -27.329 1.00 70.27  ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -4.587  -9.903  -24.030 1.00 64.44  ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -3.422  -10.394 -23.275 1.00 64.19  ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -3.725  -11.099 -21.954 1.00 63.86  ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -4.705  -10.764 -21.294 1.00 64.11  ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -2.602  -9.125  -23.058 1.00 64.99  ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -3.658  -8.028  -22.944 1.00 65.66  ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -4.820  -8.457  -23.814 1.00 64.00  ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -2.868  -12.057 -21.560 1.00 63.53  ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -2.983  -12.780 -20.282 1.00 63.88  ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -1.946  -12.207 -19.305 1.00 62.78  ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.741  -12.435 -19.463 1.00 62.76  ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -2.801  -14.300 -20.471 1.00 66.35  ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -4.013  -14.962 -21.136 1.00 71.76  ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -3.843  -16.466 -21.292 1.00 77.24  ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -4.492  -16.974 -22.510 1.00 81.41  ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -5.658  -17.617 -22.526 1.00 83.63  ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -6.310  -17.855 -21.392 1.00 84.20  ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -6.177  -18.034 -23.673 1.00 82.43  ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -2.424  -11.431 -18.321 1.00 61.47  ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -1.592  -10.703 -17.362 1.00 60.31  ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -1.682  -11.206 -15.937 1.00 59.33  ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -2.776  -11.457 -15.463 1.00 59.44  ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -2.019  -9.223  -17.382 1.00 59.78  ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.923  -8.557  -18.745 1.00 60.15  ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -2.603  -7.225  -18.760 1.00 59.72  ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? -0.470  -8.460  -19.195 1.00 60.70  ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? -0.541  -11.279 -15.222 1.00 58.23  ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? -0.537  -11.651 -13.805 1.00 57.64  ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.746  -10.375 -13.011 1.00 55.52  ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? 0.125   -9.510  -13.052 1.00 55.94  ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 0.805   -12.278 -13.397 1.00 60.61  ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 0.896   -13.780 -13.608 1.00 67.38  ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? -0.092  -14.375 -14.100 1.00 68.39  ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 1.957   -14.364 -13.277 1.00 70.32  ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -1.914  -10.214 -12.352 1.00 52.73  ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -2.199  -8.984  -11.616 1.00 50.90  ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -2.551  -9.239  -10.134 1.00 49.42  ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.929  -10.349 -9.754  1.00 49.36  ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -3.279  -8.095  -12.316 1.00 50.72  ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -2.994  -7.914  -13.805 1.00 51.28  ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -4.670  -8.653  -12.104 1.00 50.38  ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -2.387  -8.201  -9.304  1.00 47.91  ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.727  -8.200  -7.876  1.00 47.16  ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.730  -7.060  -7.632  1.00 46.57  ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -3.715  -6.056  -8.348  1.00 46.67  ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -1.487  -7.999  -7.012  1.00 46.52  ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.612  -7.226  -6.654  1.00 45.78  ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.615  -6.198  -6.349  1.00 45.27  ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -5.490  -5.839  -4.877  1.00 45.16  ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.573  -6.723  -4.006  1.00 45.33  ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -7.026  -6.694  -6.676  1.00 44.62  ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -8.153  -5.729  -6.344  1.00 44.77  ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -8.062  -4.465  -7.183  1.00 44.55  ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.494  -6.391  -6.540  1.00 44.79  ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -5.221  -4.560  -4.595  1.00 44.60  ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -5.037  -4.143  -3.220  1.00 44.78  ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -6.367  -3.659  -2.566  1.00 45.94  ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -7.399  -3.570  -3.235  1.00 46.72  ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.880  -3.136  -3.113  1.00 44.94  ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -4.155  -1.725  -3.584  1.00 46.23  ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.327  -1.396  -3.811  1.00 45.05  ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.199  -0.933  -3.659  1.00 47.99  ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -6.326  -3.381  -1.256  1.00 45.91  ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.444  -2.920  -0.446  1.00 46.18  ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -8.036  -1.595  -0.968  1.00 46.40  ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -9.229  -1.356  -0.815  1.00 47.13  ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -6.969  -2.795  1.007   1.00 48.03  ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -8.065  -2.535  2.019   1.00 53.87  ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.642  -2.776  3.450   1.00 60.99  ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.186  -1.813  4.108   1.00 62.36  ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.748  -3.937  3.907   1.00 63.60  ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.224  -0.757  -1.625  1.00 45.23  ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.702  0.492   -2.209  1.00 44.40  ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.383  0.305   -3.596  1.00 43.10  ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.797  1.300   -4.200  1.00 43.02  ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.542  1.462   -2.372  1.00 46.43  ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.278  2.156   -1.170  1.00 49.93  ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.497  -0.935  -4.087  1.00 41.61  ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -9.134  -1.185  -5.376  1.00 41.20  ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.247  -0.888  -6.572  1.00 40.82  ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.732  -0.789  -7.694  1.00 40.47  ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.925  -0.804  -6.351  1.00 40.45  ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -5.974  -0.530  -7.405  1.00 40.87  ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.235  -1.795  -7.838  1.00 42.25  ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.668  -2.522  -7.001  1.00 41.60  ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.979  0.548   -6.952  1.00 41.47  ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.666  1.846   -6.604  1.00 45.02  ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.666  2.172   -7.253  1.00 45.50  ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -5.219  2.517   -5.667  1.00 47.37  ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -5.227  -2.034  -9.166  1.00 43.16  ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.539  -3.158  -9.771  1.00 44.51  ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -3.062  -2.836  -9.971  1.00 48.11  ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.668  -1.680  -10.154 1.00 48.98  ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -5.172  -3.544  -11.122 1.00 43.06  ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.496  -4.270  -11.010 1.00 42.69  ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.546  -5.605  -10.644 1.00 42.80  ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.691  -3.619  -11.279 1.00 42.59  ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -7.772  -6.272  -10.542 1.00 42.81  ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -8.912  -4.293  -11.184 1.00 42.45  ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -8.943  -5.613  -10.819 1.00 41.87  ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -2.248  -3.867  -9.958  1.00 49.79  ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -0.830  -3.742  -10.242 1.00 52.32  ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? -0.381  -4.997  -10.949 1.00 55.43  ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -0.948  -6.074  -10.717 1.00 55.37  ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? -0.013  -3.511  -8.971  1.00 52.71  ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? -0.188  -4.552  -8.024  1.00 54.68  ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 0.606   -4.860  -11.844 1.00 57.86  ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.130   -6.024  -12.537 1.00 61.07  ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.103   -6.738  -11.624 1.00 63.66  ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 2.990   -6.109  -11.060 1.00 64.05  ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 1.821   -5.627  -13.844 1.00 61.68  ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 0.871   -5.139  -14.935 1.00 63.58  ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 1.636   -4.649  -16.137 1.00 64.43  ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? -0.088  -6.237  -15.359 1.00 64.30  ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 1.901   -8.038  -11.439 1.00 65.49  ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 2.759   -8.898  -10.628 1.00 67.73  ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 3.876   -9.408  -11.527 1.00 70.33  ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.612   -9.946  -12.606 1.00 70.58  ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 1.949   -10.085 -10.047 1.00 68.11  ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 2.862   -11.171 -9.480  1.00 68.83  ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 0.961   -9.607  -9.007  1.00 68.25  ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.111   -9.245  -11.092 1.00 72.20  ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.256   -9.737  -11.848 1.00 74.33  ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 7.282   -10.347 -10.889 1.00 75.53  ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 7.685   -11.502 -11.047 1.00 76.25  ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 6.869   -8.615  -12.701 1.00 77.89  ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 6.303   -8.521  -14.111 1.00 84.11  ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 7.346   -8.588  -15.213 1.00 91.86  ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 8.479   -9.057  -14.944 1.00 92.09  ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 7.026   -8.171  -16.350 1.00 95.34  ? 88  GLU   A OE2 1 
ATOM   312  N  N   . GLY   B 2 7   ? -36.351 12.636  -11.634 1.00 68.26  ? 16  GLY   B N   1 
ATOM   313  C  CA  . GLY   B 2 7   ? -35.626 12.850  -12.881 1.00 68.77  ? 16  GLY   B CA  1 
ATOM   314  C  C   . GLY   B 2 7   ? -35.719 11.702  -13.871 1.00 68.98  ? 16  GLY   B C   1 
ATOM   315  O  O   . GLY   B 2 7   ? -36.686 10.932  -13.836 1.00 69.89  ? 16  GLY   B O   1 
ATOM   316  N  N   . GLU   B 2 8   ? -34.720 11.571  -14.775 1.00 67.69  ? 17  GLU   B N   1 
ATOM   317  C  CA  . GLU   B 2 8   ? -34.749 10.498  -15.771 1.00 66.63  ? 17  GLU   B CA  1 
ATOM   318  C  C   . GLU   B 2 8   ? -34.336 9.129   -15.227 1.00 64.55  ? 17  GLU   B C   1 
ATOM   319  O  O   . GLU   B 2 8   ? -33.237 8.960   -14.687 1.00 64.99  ? 17  GLU   B O   1 
ATOM   320  C  CB  . GLU   B 2 8   ? -33.943 10.834  -17.035 1.00 69.46  ? 17  GLU   B CB  1 
ATOM   321  C  CG  . GLU   B 2 8   ? -34.246 9.869   -18.171 1.00 75.16  ? 17  GLU   B CG  1 
ATOM   322  C  CD  . GLU   B 2 8   ? -33.620 10.197  -19.510 1.00 83.18  ? 17  GLU   B CD  1 
ATOM   323  O  OE1 . GLU   B 2 8   ? -32.581 10.894  -19.521 1.00 84.54  ? 17  GLU   B OE1 1 
ATOM   324  O  OE2 . GLU   B 2 8   ? -34.180 9.777   -20.550 1.00 86.23  ? 17  GLU   B OE2 1 
ATOM   325  N  N   A THR   B 2 9   ? -35.223 8.146   -15.376 0.50 63.22  ? 18  THR   B N   1 
ATOM   326  N  N   B THR   B 2 9   ? -35.227 8.149   -15.370 0.50 63.36  ? 18  THR   B N   1 
ATOM   327  C  CA  A THR   B 2 9   ? -34.941 6.791   -14.905 0.50 62.45  ? 18  THR   B CA  1 
ATOM   328  C  CA  B THR   B 2 9   ? -34.973 6.781   -14.925 0.50 62.72  ? 18  THR   B CA  1 
ATOM   329  C  C   A THR   B 2 9   ? -35.017 5.759   -16.057 0.50 61.13  ? 18  THR   B C   1 
ATOM   330  C  C   B THR   B 2 9   ? -34.993 5.759   -16.065 0.50 61.24  ? 18  THR   B C   1 
ATOM   331  O  O   A THR   B 2 9   ? -35.095 4.560   -15.793 0.50 61.25  ? 18  THR   B O   1 
ATOM   332  O  O   B THR   B 2 9   ? -35.031 4.559   -15.793 0.50 61.35  ? 18  THR   B O   1 
ATOM   333  C  CB  A THR   B 2 9   ? -35.816 6.410   -13.676 0.50 63.85  ? 18  THR   B CB  1 
ATOM   334  C  CB  B THR   B 2 9   ? -35.959 6.373   -13.825 0.50 64.50  ? 18  THR   B CB  1 
ATOM   335  O  OG1 A THR   B 2 9   ? -36.278 7.579   -12.977 0.50 65.06  ? 18  THR   B OG1 1 
ATOM   336  O  OG1 B THR   B 2 9   ? -37.289 6.758   -14.201 0.50 65.74  ? 18  THR   B OG1 1 
ATOM   337  C  CG2 A THR   B 2 9   ? -35.082 5.496   -12.693 0.50 63.98  ? 18  THR   B CG2 1 
ATOM   338  C  CG2 B THR   B 2 9   ? -35.589 6.954   -12.463 0.50 64.98  ? 18  THR   B CG2 1 
ATOM   339  N  N   . THR   B 2 10  ? -34.968 6.218   -17.324 1.00 59.72  ? 19  THR   B N   1 
ATOM   340  C  CA  . THR   B 2 10  ? -35.011 5.343   -18.482 1.00 57.67  ? 19  THR   B CA  1 
ATOM   341  C  C   . THR   B 2 10  ? -33.739 4.515   -18.546 1.00 54.55  ? 19  THR   B C   1 
ATOM   342  O  O   . THR   B 2 10  ? -32.656 5.050   -18.336 1.00 54.33  ? 19  THR   B O   1 
ATOM   343  C  CB  . THR   B 2 10  ? -35.148 6.182   -19.772 1.00 59.37  ? 19  THR   B CB  1 
ATOM   344  O  OG1 . THR   B 2 10  ? -36.244 7.096   -19.653 1.00 61.48  ? 19  THR   B OG1 1 
ATOM   345  C  CG2 . THR   B 2 10  ? -35.343 5.322   -21.004 1.00 59.37  ? 19  THR   B CG2 1 
ATOM   346  N  N   . ASP   B 2 11  ? -33.858 3.217   -18.838 1.00 52.10  ? 20  ASP   B N   1 
ATOM   347  C  CA  . ASP   B 2 11  ? -32.712 2.325   -19.006 1.00 50.80  ? 20  ASP   B CA  1 
ATOM   348  C  C   . ASP   B 2 11  ? -31.771 2.878   -20.106 1.00 49.14  ? 20  ASP   B C   1 
ATOM   349  O  O   . ASP   B 2 11  ? -32.233 3.523   -21.049 1.00 49.44  ? 20  ASP   B O   1 
ATOM   350  C  CB  . ASP   B 2 11  ? -33.193 0.923   -19.449 1.00 52.91  ? 20  ASP   B CB  1 
ATOM   351  C  CG  . ASP   B 2 11  ? -33.552 -0.058  -18.343 1.00 58.20  ? 20  ASP   B CG  1 
ATOM   352  O  OD1 . ASP   B 2 11  ? -33.913 0.402   -17.235 1.00 57.63  ? 20  ASP   B OD1 1 
ATOM   353  O  OD2 . ASP   B 2 11  ? -33.480 -1.306  -18.597 1.00 60.92  ? 20  ASP   B OD2 1 
ATOM   354  N  N   . GLY   B 2 12  ? -30.479 2.627   -19.973 1.00 47.08  ? 21  GLY   B N   1 
ATOM   355  C  CA  . GLY   B 2 12  ? -29.507 3.093   -20.946 1.00 45.12  ? 21  GLY   B CA  1 
ATOM   356  C  C   . GLY   B 2 12  ? -28.204 3.540   -20.329 1.00 43.20  ? 21  GLY   B C   1 
ATOM   357  O  O   . GLY   B 2 12  ? -28.013 3.451   -19.116 1.00 43.74  ? 21  GLY   B O   1 
ATOM   358  N  N   . VAL   B 2 13  ? -27.282 3.987   -21.167 1.00 41.14  ? 22  VAL   B N   1 
ATOM   359  C  CA  . VAL   B 2 13  ? -25.980 4.452   -20.721 1.00 39.91  ? 22  VAL   B CA  1 
ATOM   360  C  C   . VAL   B 2 13  ? -26.042 5.975   -20.500 1.00 39.96  ? 22  VAL   B C   1 
ATOM   361  O  O   . VAL   B 2 13  ? -26.824 6.653   -21.166 1.00 40.29  ? 22  VAL   B O   1 
ATOM   362  C  CB  . VAL   B 2 13  ? -24.850 3.965   -21.664 1.00 39.33  ? 22  VAL   B CB  1 
ATOM   363  C  CG1 . VAL   B 2 13  ? -24.983 4.545   -23.082 1.00 39.26  ? 22  VAL   B CG1 1 
ATOM   364  C  CG2 . VAL   B 2 13  ? -23.482 4.237   -21.076 1.00 38.91  ? 22  VAL   B CG2 1 
ATOM   365  N  N   . TYR   B 2 14  ? -25.365 6.486   -19.448 1.00 39.56  ? 23  TYR   B N   1 
ATOM   366  C  CA  . TYR   B 2 14  ? -25.415 7.911   -19.088 1.00 39.48  ? 23  TYR   B CA  1 
ATOM   367  C  C   . TYR   B 2 14  ? -24.021 8.469   -18.853 1.00 40.29  ? 23  TYR   B C   1 
ATOM   368  O  O   . TYR   B 2 14  ? -23.154 7.738   -18.402 1.00 41.28  ? 23  TYR   B O   1 
ATOM   369  C  CB  . TYR   B 2 14  ? -26.194 8.091   -17.757 1.00 38.53  ? 23  TYR   B CB  1 
ATOM   370  C  CG  . TYR   B 2 14  ? -27.694 7.932   -17.862 1.00 37.20  ? 23  TYR   B CG  1 
ATOM   371  C  CD1 . TYR   B 2 14  ? -28.264 6.699   -18.141 1.00 37.05  ? 23  TYR   B CD1 1 
ATOM   372  C  CD2 . TYR   B 2 14  ? -28.544 9.006   -17.637 1.00 37.36  ? 23  TYR   B CD2 1 
ATOM   373  C  CE1 . TYR   B 2 14  ? -29.632 6.551   -18.276 1.00 37.58  ? 23  TYR   B CE1 1 
ATOM   374  C  CE2 . TYR   B 2 14  ? -29.923 8.873   -17.771 1.00 37.85  ? 23  TYR   B CE2 1 
ATOM   375  C  CZ  . TYR   B 2 14  ? -30.462 7.639   -18.089 1.00 38.68  ? 23  TYR   B CZ  1 
ATOM   376  O  OH  . TYR   B 2 14  ? -31.814 7.448   -18.171 1.00 40.55  ? 23  TYR   B OH  1 
ATOM   377  N  N   . ARG   B 2 15  ? -23.827 9.770   -19.054 1.00 39.69  ? 24  ARG   B N   1 
ATOM   378  C  CA  . ARG   B 2 15  ? -22.562 10.428  -18.735 1.00 39.94  ? 24  ARG   B CA  1 
ATOM   379  C  C   . ARG   B 2 15  ? -22.688 11.003  -17.306 1.00 40.35  ? 24  ARG   B C   1 
ATOM   380  O  O   . ARG   B 2 15  ? -23.734 11.506  -16.941 1.00 40.45  ? 24  ARG   B O   1 
ATOM   381  C  CB  . ARG   B 2 15  ? -22.272 11.602  -19.696 1.00 40.97  ? 24  ARG   B CB  1 
ATOM   382  C  CG  . ARG   B 2 15  ? -22.278 11.275  -21.184 1.00 42.80  ? 24  ARG   B CG  1 
ATOM   383  C  CD  . ARG   B 2 15  ? -22.222 12.549  -22.048 1.00 44.66  ? 24  ARG   B CD  1 
ATOM   384  N  NE  . ARG   B 2 15  ? -22.405 12.243  -23.475 1.00 45.29  ? 24  ARG   B NE  1 
ATOM   385  C  CZ  . ARG   B 2 15  ? -21.427 11.851  -24.287 1.00 48.08  ? 24  ARG   B CZ  1 
ATOM   386  N  NH1 . ARG   B 2 15  ? -20.176 11.765  -23.842 1.00 47.71  ? 24  ARG   B NH1 1 
ATOM   387  N  NH2 . ARG   B 2 15  ? -21.692 11.535  -25.551 1.00 47.44  ? 24  ARG   B NH2 1 
ATOM   388  N  N   . VAL   B 2 16  ? -21.626 10.943  -16.527 1.00 40.72  ? 25  VAL   B N   1 
ATOM   389  C  CA  . VAL   B 2 16  ? -21.537 11.477  -15.182 1.00 41.82  ? 25  VAL   B CA  1 
ATOM   390  C  C   . VAL   B 2 16  ? -20.712 12.747  -15.336 1.00 43.52  ? 25  VAL   B C   1 
ATOM   391  O  O   . VAL   B 2 16  ? -19.535 12.695  -15.688 1.00 43.15  ? 25  VAL   B O   1 
ATOM   392  C  CB  . VAL   B 2 16  ? -20.883 10.477  -14.191 1.00 42.57  ? 25  VAL   B CB  1 
ATOM   393  C  CG1 . VAL   B 2 16  ? -20.975 11.003  -12.761 1.00 42.78  ? 25  VAL   B CG1 1 
ATOM   394  C  CG2 . VAL   B 2 16  ? -21.513 9.084   -14.300 1.00 42.89  ? 25  VAL   B CG2 1 
ATOM   395  N  N   . MET   B 2 17  ? -21.358 13.895  -15.156 1.00 45.38  ? 26  MET   B N   1 
ATOM   396  C  CA  . MET   B 2 17  ? -20.767 15.199  -15.376 1.00 47.46  ? 26  MET   B CA  1 
ATOM   397  C  C   . MET   B 2 17  ? -20.571 15.993  -14.091 1.00 50.64  ? 26  MET   B C   1 
ATOM   398  O  O   . MET   B 2 17  ? -21.266 15.762  -13.107 1.00 50.93  ? 26  MET   B O   1 
ATOM   399  C  CB  . MET   B 2 17  ? -21.697 15.999  -16.300 1.00 47.53  ? 26  MET   B CB  1 
ATOM   400  C  CG  . MET   B 2 17  ? -22.114 15.271  -17.563 1.00 48.40  ? 26  MET   B CG  1 
ATOM   401  S  SD  . MET   B 2 17  ? -20.753 15.152  -18.740 1.00 50.21  ? 26  MET   B SD  1 
ATOM   402  C  CE  . MET   B 2 17  ? -20.430 16.876  -19.012 1.00 44.07  ? 26  MET   B CE  1 
ATOM   403  N  N   . THR   B 2 18  ? -19.678 16.992  -14.123 1.00 53.04  ? 27  THR   B N   1 
ATOM   404  C  CA  . THR   B 2 18  ? -19.482 17.874  -12.980 1.00 55.68  ? 27  THR   B CA  1 
ATOM   405  C  C   . THR   B 2 18  ? -19.246 19.329  -13.420 1.00 58.27  ? 27  THR   B C   1 
ATOM   406  O  O   . THR   B 2 18  ? -18.456 19.594  -14.335 1.00 58.36  ? 27  THR   B O   1 
ATOM   407  C  CB  . THR   B 2 18  ? -18.399 17.341  -12.023 1.00 57.46  ? 27  THR   B CB  1 
ATOM   408  O  OG1 . THR   B 2 18  ? -18.395 18.149  -10.846 1.00 59.28  ? 27  THR   B OG1 1 
ATOM   409  C  CG2 . THR   B 2 18  ? -17.016 17.338  -12.633 1.00 57.77  ? 27  THR   B CG2 1 
ATOM   410  N  N   . ARG   B 2 19  ? -19.966 20.270  -12.796 1.00 60.10  ? 28  ARG   B N   1 
ATOM   411  C  CA  . ARG   B 2 19  ? -19.751 21.690  -13.071 1.00 62.65  ? 28  ARG   B CA  1 
ATOM   412  C  C   . ARG   B 2 19  ? -18.838 22.346  -11.989 1.00 63.84  ? 28  ARG   B C   1 
ATOM   413  O  O   . ARG   B 2 19  ? -18.849 23.565  -11.822 1.00 63.76  ? 28  ARG   B O   1 
ATOM   414  C  CB  . ARG   B 2 19  ? -21.087 22.443  -13.231 1.00 65.42  ? 28  ARG   B CB  1 
ATOM   415  C  CG  . ARG   B 2 19  ? -21.806 22.125  -14.540 1.00 71.03  ? 28  ARG   B CG  1 
ATOM   416  C  CD  . ARG   B 2 19  ? -23.001 23.027  -14.784 1.00 76.87  ? 28  ARG   B CD  1 
ATOM   417  N  NE  . ARG   B 2 19  ? -23.951 22.453  -15.745 1.00 82.70  ? 28  ARG   B NE  1 
ATOM   418  C  CZ  . ARG   B 2 19  ? -25.114 21.897  -15.410 1.00 86.76  ? 28  ARG   B CZ  1 
ATOM   419  N  NH1 . ARG   B 2 19  ? -25.481 21.823  -14.133 1.00 87.20  ? 28  ARG   B NH1 1 
ATOM   420  N  NH2 . ARG   B 2 19  ? -25.917 21.405  -16.347 1.00 86.75  ? 28  ARG   B NH2 1 
ATOM   421  N  N   . ARG   B 2 20  ? -18.035 21.527  -11.281 1.00 64.86  ? 29  ARG   B N   1 
ATOM   422  C  CA  . ARG   B 2 20  ? -17.124 21.961  -10.215 1.00 66.50  ? 29  ARG   B CA  1 
ATOM   423  C  C   . ARG   B 2 20  ? -15.775 22.457  -10.759 1.00 67.00  ? 29  ARG   B C   1 
ATOM   424  O  O   . ARG   B 2 20  ? -15.091 23.241  -10.093 1.00 67.64  ? 29  ARG   B O   1 
ATOM   425  C  CB  . ARG   B 2 20  ? -16.930 20.835  -9.182  1.00 68.73  ? 29  ARG   B CB  1 
ATOM   426  C  CG  . ARG   B 2 20  ? -16.097 21.233  -7.970  1.00 73.77  ? 29  ARG   B CG  1 
ATOM   427  C  CD  . ARG   B 2 20  ? -15.754 20.058  -7.070  1.00 78.74  ? 29  ARG   B CD  1 
ATOM   428  N  NE  . ARG   B 2 20  ? -15.164 18.929  -7.798  1.00 83.09  ? 29  ARG   B NE  1 
ATOM   429  C  CZ  . ARG   B 2 20  ? -13.860 18.756  -7.992  1.00 85.86  ? 29  ARG   B CZ  1 
ATOM   430  N  NH1 . ARG   B 2 20  ? -12.987 19.641  -7.519  1.00 85.78  ? 29  ARG   B NH1 1 
ATOM   431  N  NH2 . ARG   B 2 20  ? -13.417 17.696  -8.657  1.00 85.88  ? 29  ARG   B NH2 1 
ATOM   432  N  N   . LEU   B 2 21  ? -15.396 22.023  -11.970 1.00 66.36  ? 30  LEU   B N   1 
ATOM   433  C  CA  . LEU   B 2 21  ? -14.163 22.491  -12.589 1.00 66.24  ? 30  LEU   B CA  1 
ATOM   434  C  C   . LEU   B 2 21  ? -14.517 23.522  -13.697 1.00 65.12  ? 30  LEU   B C   1 
ATOM   435  O  O   . LEU   B 2 21  ? -15.566 24.172  -13.608 1.00 65.58  ? 30  LEU   B O   1 
ATOM   436  C  CB  . LEU   B 2 21  ? -13.317 21.298  -13.112 1.00 66.95  ? 30  LEU   B CB  1 
ATOM   437  C  CG  . LEU   B 2 21  ? -12.791 20.254  -12.112 1.00 69.22  ? 30  LEU   B CG  1 
ATOM   438  C  CD1 . LEU   B 2 21  ? -12.342 20.877  -10.775 1.00 70.00  ? 30  LEU   B CD1 1 
ATOM   439  C  CD2 . LEU   B 2 21  ? -13.787 19.137  -11.906 1.00 70.32  ? 30  LEU   B CD2 1 
ATOM   440  N  N   . LEU   B 2 22  ? -13.643 23.712  -14.699 1.00 63.32  ? 31  LEU   B N   1 
ATOM   441  C  CA  . LEU   B 2 22  ? -13.892 24.618  -15.805 1.00 62.14  ? 31  LEU   B CA  1 
ATOM   442  C  C   . LEU   B 2 22  ? -14.983 24.019  -16.698 1.00 61.99  ? 31  LEU   B C   1 
ATOM   443  O  O   . LEU   B 2 22  ? -14.888 22.842  -17.063 1.00 62.76  ? 31  LEU   B O   1 
ATOM   444  C  CB  . LEU   B 2 22  ? -12.611 24.751  -16.603 1.00 61.47  ? 31  LEU   B CB  1 
ATOM   445  C  CG  . LEU   B 2 22  ? -12.623 25.859  -17.605 1.00 61.73  ? 31  LEU   B CG  1 
ATOM   446  C  CD1 . LEU   B 2 22  ? -12.548 27.206  -16.919 1.00 61.50  ? 31  LEU   B CD1 1 
ATOM   447  C  CD2 . LEU   B 2 22  ? -11.535 25.648  -18.626 1.00 62.02  ? 31  LEU   B CD2 1 
ATOM   448  N  N   . GLY   B 2 23  ? -16.021 24.804  -17.009 1.00 60.50  ? 32  GLY   B N   1 
ATOM   449  C  CA  . GLY   B 2 23  ? -17.154 24.337  -17.804 1.00 59.43  ? 32  GLY   B CA  1 
ATOM   450  C  C   . GLY   B 2 23  ? -17.819 23.089  -17.241 1.00 58.05  ? 32  GLY   B C   1 
ATOM   451  O  O   . GLY   B 2 23  ? -17.841 22.877  -16.026 1.00 57.75  ? 32  GLY   B O   1 
ATOM   452  N  N   . SER   B 2 24  ? -18.354 22.242  -18.123 1.00 56.89  ? 33  SER   B N   1 
ATOM   453  C  CA  . SER   B 2 24  ? -18.949 20.968  -17.709 1.00 55.90  ? 33  SER   B CA  1 
ATOM   454  C  C   . SER   B 2 24  ? -17.933 19.900  -18.065 1.00 53.66  ? 33  SER   B C   1 
ATOM   455  O  O   . SER   B 2 24  ? -17.486 19.858  -19.206 1.00 53.71  ? 33  SER   B O   1 
ATOM   456  C  CB  . SER   B 2 24  ? -20.262 20.714  -18.443 1.00 58.27  ? 33  SER   B CB  1 
ATOM   457  O  OG  . SER   B 2 24  ? -21.186 21.771  -18.216 1.00 61.66  ? 33  SER   B OG  1 
ATOM   458  N  N   . THR   B 2 25  ? -17.535 19.059  -17.094 1.00 51.81  ? 34  THR   B N   1 
ATOM   459  C  CA  . THR   B 2 25  ? -16.508 18.041  -17.304 1.00 50.09  ? 34  THR   B CA  1 
ATOM   460  C  C   . THR   B 2 25  ? -17.028 16.613  -17.087 1.00 48.37  ? 34  THR   B C   1 
ATOM   461  O  O   . THR   B 2 25  ? -17.607 16.326  -16.038 1.00 48.52  ? 34  THR   B O   1 
ATOM   462  C  CB  . THR   B 2 25  ? -15.304 18.335  -16.381 1.00 50.75  ? 34  THR   B CB  1 
ATOM   463  O  OG1 . THR   B 2 25  ? -14.764 19.629  -16.695 1.00 51.79  ? 34  THR   B OG1 1 
ATOM   464  C  CG2 . THR   B 2 25  ? -14.215 17.289  -16.497 1.00 50.45  ? 34  THR   B CG2 1 
ATOM   465  N  N   . GLN   B 2 26  ? -16.807 15.712  -18.067 1.00 46.20  ? 35  GLN   B N   1 
ATOM   466  C  CA  . GLN   B 2 26  ? -17.217 14.325  -17.897 1.00 44.57  ? 35  GLN   B CA  1 
ATOM   467  C  C   . GLN   B 2 26  ? -16.216 13.553  -17.011 1.00 44.71  ? 35  GLN   B C   1 
ATOM   468  O  O   . GLN   B 2 26  ? -15.068 13.315  -17.418 1.00 45.13  ? 35  GLN   B O   1 
ATOM   469  C  CB  . GLN   B 2 26  ? -17.432 13.616  -19.245 1.00 43.04  ? 35  GLN   B CB  1 
ATOM   470  C  CG  . GLN   B 2 26  ? -17.958 12.190  -19.091 1.00 41.50  ? 35  GLN   B CG  1 
ATOM   471  C  CD  . GLN   B 2 26  ? -18.317 11.554  -20.402 1.00 42.22  ? 35  GLN   B CD  1 
ATOM   472  O  OE1 . GLN   B 2 26  ? -18.987 12.157  -21.238 1.00 42.21  ? 35  GLN   B OE1 1 
ATOM   473  N  NE2 . GLN   B 2 26  ? -17.895 10.306  -20.613 1.00 41.87  ? 35  GLN   B NE2 1 
ATOM   474  N  N   . VAL   B 2 27  ? -16.660 13.144  -15.811 1.00 43.65  ? 36  VAL   B N   1 
ATOM   475  C  CA  . VAL   B 2 27  ? -15.823 12.365  -14.892 1.00 43.34  ? 36  VAL   B CA  1 
ATOM   476  C  C   . VAL   B 2 27  ? -16.000 10.826  -15.051 1.00 42.34  ? 36  VAL   B C   1 
ATOM   477  O  O   . VAL   B 2 27  ? -15.184 10.048  -14.540 1.00 42.01  ? 36  VAL   B O   1 
ATOM   478  C  CB  . VAL   B 2 27  ? -16.007 12.802  -13.409 1.00 44.01  ? 36  VAL   B CB  1 
ATOM   479  C  CG1 . VAL   B 2 27  ? -15.488 14.213  -13.188 1.00 44.67  ? 36  VAL   B CG1 1 
ATOM   480  C  CG2 . VAL   B 2 27  ? -17.461 12.686  -12.962 1.00 44.00  ? 36  VAL   B CG2 1 
ATOM   481  N  N   . GLY   B 2 28  ? -17.052 10.411  -15.745 1.00 41.04  ? 37  GLY   B N   1 
ATOM   482  C  CA  . GLY   B 2 28  ? -17.334 8.998   -15.912 1.00 40.39  ? 37  GLY   B CA  1 
ATOM   483  C  C   . GLY   B 2 28  ? -18.643 8.729   -16.618 1.00 39.96  ? 37  GLY   B C   1 
ATOM   484  O  O   . GLY   B 2 28  ? -19.271 9.633   -17.164 1.00 39.83  ? 37  GLY   B O   1 
ATOM   485  N  N   . VAL   B 2 29  ? -19.043 7.462   -16.610 1.00 39.66  ? 38  VAL   B N   1 
ATOM   486  C  CA  . VAL   B 2 29  ? -20.187 6.873   -17.293 1.00 39.77  ? 38  VAL   B CA  1 
ATOM   487  C  C   . VAL   B 2 29  ? -20.873 5.892   -16.346 1.00 39.38  ? 38  VAL   B C   1 
ATOM   488  O  O   . VAL   B 2 29  ? -20.264 5.427   -15.378 1.00 40.66  ? 38  VAL   B O   1 
ATOM   489  C  CB  . VAL   B 2 29  ? -19.693 6.154   -18.601 1.00 41.13  ? 38  VAL   B CB  1 
ATOM   490  C  CG1 . VAL   B 2 29  ? -20.835 5.481   -19.342 1.00 41.92  ? 38  VAL   B CG1 1 
ATOM   491  C  CG2 . VAL   B 2 29  ? -18.967 7.121   -19.544 1.00 41.62  ? 38  VAL   B CG2 1 
ATOM   492  N  N   . GLY   B 2 30  ? -22.127 5.579   -16.619 1.00 38.01  ? 39  GLY   B N   1 
ATOM   493  C  CA  . GLY   B 2 30  ? -22.885 4.636   -15.821 1.00 37.70  ? 39  GLY   B CA  1 
ATOM   494  C  C   . GLY   B 2 30  ? -24.028 3.989   -16.567 1.00 37.86  ? 39  GLY   B C   1 
ATOM   495  O  O   . GLY   B 2 30  ? -24.374 4.399   -17.680 1.00 38.62  ? 39  GLY   B O   1 
ATOM   496  N  N   . VAL   B 2 31  ? -24.593 2.942   -15.984 1.00 37.41  ? 40  VAL   B N   1 
ATOM   497  C  CA  . VAL   B 2 31  ? -25.679 2.186   -16.604 1.00 37.56  ? 40  VAL   B CA  1 
ATOM   498  C  C   . VAL   B 2 31  ? -26.920 2.339   -15.760 1.00 38.32  ? 40  VAL   B C   1 
ATOM   499  O  O   . VAL   B 2 31  ? -26.853 2.121   -14.564 1.00 38.48  ? 40  VAL   B O   1 
ATOM   500  C  CB  . VAL   B 2 31  ? -25.304 0.680   -16.702 1.00 37.35  ? 40  VAL   B CB  1 
ATOM   501  C  CG1 . VAL   B 2 31  ? -26.493 -0.174  -17.128 1.00 36.96  ? 40  VAL   B CG1 1 
ATOM   502  C  CG2 . VAL   B 2 31  ? -24.113 0.471   -17.627 1.00 37.58  ? 40  VAL   B CG2 1 
ATOM   503  N  N   . MET   B 2 32  ? -28.053 2.680   -16.373 1.00 38.68  ? 41  MET   B N   1 
ATOM   504  C  CA  . MET   B 2 32  ? -29.306 2.745   -15.650 1.00 39.26  ? 41  MET   B CA  1 
ATOM   505  C  C   . MET   B 2 32  ? -30.048 1.447   -16.004 1.00 40.95  ? 41  MET   B C   1 
ATOM   506  O  O   . MET   B 2 32  ? -30.219 1.151   -17.186 1.00 41.23  ? 41  MET   B O   1 
ATOM   507  C  CB  . MET   B 2 32  ? -30.089 4.000   -16.048 1.00 38.48  ? 41  MET   B CB  1 
ATOM   508  C  CG  . MET   B 2 32  ? -31.315 4.240   -15.237 1.00 39.63  ? 41  MET   B CG  1 
ATOM   509  S  SD  . MET   B 2 32  ? -30.967 4.742   -13.524 1.00 44.75  ? 41  MET   B SD  1 
ATOM   510  C  CE  . MET   B 2 32  ? -30.435 6.426   -13.783 1.00 43.14  ? 41  MET   B CE  1 
ATOM   511  N  N   . GLN   B 2 33  ? -30.389 0.622   -15.001 1.00 41.58  ? 42  GLN   B N   1 
ATOM   512  C  CA  . GLN   B 2 33  ? -31.106 -0.627  -15.254 1.00 42.43  ? 42  GLN   B CA  1 
ATOM   513  C  C   . GLN   B 2 33  ? -32.002 -0.957  -14.073 1.00 43.32  ? 42  GLN   B C   1 
ATOM   514  O  O   . GLN   B 2 33  ? -31.531 -0.981  -12.938 1.00 43.56  ? 42  GLN   B O   1 
ATOM   515  C  CB  . GLN   B 2 33  ? -30.154 -1.784  -15.537 1.00 44.00  ? 42  GLN   B CB  1 
ATOM   516  C  CG  . GLN   B 2 33  ? -30.934 -3.018  -15.959 1.00 49.19  ? 42  GLN   B CG  1 
ATOM   517  C  CD  . GLN   B 2 33  ? -30.067 -4.166  -16.401 1.00 55.04  ? 42  GLN   B CD  1 
ATOM   518  O  OE1 . GLN   B 2 33  ? -30.105 -5.262  -15.814 1.00 56.59  ? 42  GLN   B OE1 1 
ATOM   519  N  NE2 . GLN   B 2 33  ? -29.271 -3.939  -17.450 1.00 55.51  ? 42  GLN   B NE2 1 
ATOM   520  N  N   . GLU   B 2 34  ? -33.291 -1.198  -14.330 1.00 43.55  ? 43  GLU   B N   1 
ATOM   521  C  CA  . GLU   B 2 34  ? -34.282 -1.493  -13.294 1.00 44.10  ? 43  GLU   B CA  1 
ATOM   522  C  C   . GLU   B 2 34  ? -34.355 -0.420  -12.198 1.00 44.59  ? 43  GLU   B C   1 
ATOM   523  O  O   . GLU   B 2 34  ? -34.500 -0.742  -11.029 1.00 45.93  ? 43  GLU   B O   1 
ATOM   524  C  CB  . GLU   B 2 34  ? -34.085 -2.888  -12.696 1.00 45.94  ? 43  GLU   B CB  1 
ATOM   525  C  CG  . GLU   B 2 34  ? -34.240 -4.019  -13.696 1.00 48.82  ? 43  GLU   B CG  1 
ATOM   526  C  CD  . GLU   B 2 34  ? -33.543 -5.301  -13.279 1.00 54.25  ? 43  GLU   B CD  1 
ATOM   527  O  OE1 . GLU   B 2 34  ? -33.772 -5.764  -12.140 1.00 53.79  ? 43  GLU   B OE1 1 
ATOM   528  O  OE2 . GLU   B 2 34  ? -32.753 -5.836  -14.089 1.00 58.36  ? 43  GLU   B OE2 1 
ATOM   529  N  N   . GLY   B 2 35  ? -34.276 0.846   -12.587 1.00 43.68  ? 44  GLY   B N   1 
ATOM   530  C  CA  . GLY   B 2 35  ? -34.347 1.964   -11.651 1.00 42.84  ? 44  GLY   B CA  1 
ATOM   531  C  C   . GLY   B 2 35  ? -33.103 2.155   -10.808 1.00 41.94  ? 44  GLY   B C   1 
ATOM   532  O  O   . GLY   B 2 35  ? -33.139 2.894   -9.823  1.00 41.92  ? 44  GLY   B O   1 
ATOM   533  N  N   . VAL   B 2 36  ? -31.985 1.492   -11.177 1.00 40.82  ? 45  VAL   B N   1 
ATOM   534  C  CA  . VAL   B 2 36  ? -30.739 1.553   -10.413 1.00 40.31  ? 45  VAL   B CA  1 
ATOM   535  C  C   . VAL   B 2 36  ? -29.596 2.068   -11.284 1.00 38.91  ? 45  VAL   B C   1 
ATOM   536  O  O   . VAL   B 2 36  ? -29.395 1.559   -12.401 1.00 39.25  ? 45  VAL   B O   1 
ATOM   537  C  CB  . VAL   B 2 36  ? -30.406 0.181   -9.749  1.00 41.47  ? 45  VAL   B CB  1 
ATOM   538  C  CG1 . VAL   B 2 36  ? -29.015 0.179   -9.106  1.00 42.17  ? 45  VAL   B CG1 1 
ATOM   539  C  CG2 . VAL   B 2 36  ? -31.466 -0.199  -8.720  1.00 41.90  ? 45  VAL   B CG2 1 
ATOM   540  N  N   . PHE   B 2 37  ? -28.892 3.119   -10.817 1.00 36.89  ? 46  PHE   B N   1 
ATOM   541  C  CA  . PHE   B 2 37  ? -27.753 3.625   -11.567 1.00 36.73  ? 46  PHE   B CA  1 
ATOM   542  C  C   . PHE   B 2 37  ? -26.515 2.911   -11.060 1.00 35.18  ? 46  PHE   B C   1 
ATOM   543  O  O   . PHE   B 2 37  ? -26.304 2.843   -9.869  1.00 34.42  ? 46  PHE   B O   1 
ATOM   544  C  CB  . PHE   B 2 37  ? -27.597 5.148   -11.412 1.00 37.13  ? 46  PHE   B CB  1 
ATOM   545  C  CG  . PHE   B 2 37  ? -26.605 5.746   -12.390 1.00 37.59  ? 46  PHE   B CG  1 
ATOM   546  C  CD1 . PHE   B 2 37  ? -26.874 5.770   -13.745 1.00 38.11  ? 46  PHE   B CD1 1 
ATOM   547  C  CD2 . PHE   B 2 37  ? -25.427 6.316   -11.944 1.00 38.18  ? 46  PHE   B CD2 1 
ATOM   548  C  CE1 . PHE   B 2 37  ? -25.975 6.337   -14.637 1.00 38.63  ? 46  PHE   B CE1 1 
ATOM   549  C  CE2 . PHE   B 2 37  ? -24.521 6.852   -12.839 1.00 38.50  ? 46  PHE   B CE2 1 
ATOM   550  C  CZ  . PHE   B 2 37  ? -24.809 6.877   -14.176 1.00 38.50  ? 46  PHE   B CZ  1 
ATOM   551  N  N   . HIS   B 2 38  ? -25.724 2.342   -11.956 1.00 34.97  ? 47  HIS   B N   1 
ATOM   552  C  CA  . HIS   B 2 38  ? -24.515 1.601   -11.615 1.00 34.40  ? 47  HIS   B CA  1 
ATOM   553  C  C   . HIS   B 2 38  ? -23.327 2.313   -12.222 1.00 35.51  ? 47  HIS   B C   1 
ATOM   554  O  O   . HIS   B 2 38  ? -23.338 2.589   -13.404 1.00 36.39  ? 47  HIS   B O   1 
ATOM   555  C  CB  . HIS   B 2 38  ? -24.554 0.199   -12.231 1.00 33.33  ? 47  HIS   B CB  1 
ATOM   556  C  CG  . HIS   B 2 38  ? -25.813 -0.562  -11.987 1.00 35.01  ? 47  HIS   B CG  1 
ATOM   557  N  ND1 . HIS   B 2 38  ? -27.004 -0.221  -12.619 1.00 36.09  ? 47  HIS   B ND1 1 
ATOM   558  C  CD2 . HIS   B 2 38  ? -26.018 -1.677  -11.248 1.00 36.55  ? 47  HIS   B CD2 1 
ATOM   559  C  CE1 . HIS   B 2 38  ? -27.892 -1.120  -12.222 1.00 36.59  ? 47  HIS   B CE1 1 
ATOM   560  N  NE2 . HIS   B 2 38  ? -27.354 -2.002  -11.379 1.00 37.24  ? 47  HIS   B NE2 1 
ATOM   561  N  N   . THR   B 2 39  ? -22.279 2.555   -11.446 1.00 35.66  ? 48  THR   B N   1 
ATOM   562  C  CA  . THR   B 2 39  ? -21.065 3.176   -11.958 1.00 35.92  ? 48  THR   B CA  1 
ATOM   563  C  C   . THR   B 2 39  ? -19.839 2.653   -11.146 1.00 36.07  ? 48  THR   B C   1 
ATOM   564  O  O   . THR   B 2 39  ? -19.966 1.719   -10.338 1.00 35.72  ? 48  THR   B O   1 
ATOM   565  C  CB  . THR   B 2 39  ? -21.233 4.724   -12.042 1.00 36.89  ? 48  THR   B CB  1 
ATOM   566  O  OG1 . THR   B 2 39  ? -20.096 5.254   -12.726 1.00 37.93  ? 48  THR   B OG1 1 
ATOM   567  C  CG2 . THR   B 2 39  ? -21.396 5.375   -10.675 1.00 36.56  ? 48  THR   B CG2 1 
ATOM   568  N  N   . MET   B 2 40  ? -18.658 3.220   -11.392 1.00 36.27  ? 49  MET   B N   1 
ATOM   569  C  CA  . MET   B 2 40  ? -17.458 2.848   -10.674 1.00 37.06  ? 49  MET   B CA  1 
ATOM   570  C  C   . MET   B 2 40  ? -17.299 3.762   -9.481  1.00 38.09  ? 49  MET   B C   1 
ATOM   571  O  O   . MET   B 2 40  ? -17.626 4.951   -9.563  1.00 38.95  ? 49  MET   B O   1 
ATOM   572  C  CB  . MET   B 2 40  ? -16.251 2.907   -11.621 1.00 37.83  ? 49  MET   B CB  1 
ATOM   573  C  CG  . MET   B 2 40  ? -16.456 2.065   -12.869 1.00 40.48  ? 49  MET   B CG  1 
ATOM   574  S  SD  . MET   B 2 40  ? -15.046 1.034   -13.359 1.00 46.87  ? 49  MET   B SD  1 
ATOM   575  C  CE  . MET   B 2 40  ? -15.248 -0.333  -12.317 1.00 44.31  ? 49  MET   B CE  1 
ATOM   576  N  N   . TRP   B 2 41  ? -16.808 3.228   -8.356  1.00 38.24  ? 50  TRP   B N   1 
ATOM   577  C  CA  A TRP   B 2 41  ? -16.634 4.028   -7.150  0.50 39.21  ? 50  TRP   B CA  1 
ATOM   578  C  CA  B TRP   B 2 41  ? -16.620 4.014   -7.144  0.50 38.49  ? 50  TRP   B CA  1 
ATOM   579  C  C   . TRP   B 2 41  ? -15.739 5.242   -7.365  1.00 39.59  ? 50  TRP   B C   1 
ATOM   580  O  O   . TRP   B 2 41  ? -16.058 6.304   -6.854  1.00 39.84  ? 50  TRP   B O   1 
ATOM   581  C  CB  A TRP   B 2 41  ? -16.130 3.185   -5.957  0.50 39.62  ? 50  TRP   B CB  1 
ATOM   582  C  CB  B TRP   B 2 41  ? -16.060 3.156   -5.983  0.50 37.88  ? 50  TRP   B CB  1 
ATOM   583  C  CG  A TRP   B 2 41  ? -16.162 3.930   -4.651  0.50 40.39  ? 50  TRP   B CG  1 
ATOM   584  C  CG  B TRP   B 2 41  ? -15.879 3.947   -4.723  0.50 37.17  ? 50  TRP   B CG  1 
ATOM   585  C  CD1 A TRP   B 2 41  ? -17.217 4.031   -3.793  0.50 41.19  ? 50  TRP   B CD1 1 
ATOM   586  C  CD1 B TRP   B 2 41  ? -14.839 4.775   -4.415  0.50 37.53  ? 50  TRP   B CD1 1 
ATOM   587  C  CD2 A TRP   B 2 41  ? -15.112 4.737   -4.093  0.50 40.67  ? 50  TRP   B CD2 1 
ATOM   588  C  CD2 B TRP   B 2 41  ? -16.835 4.097   -3.670  0.50 36.66  ? 50  TRP   B CD2 1 
ATOM   589  N  NE1 A TRP   B 2 41  ? -16.888 4.846   -2.734  0.50 41.57  ? 50  TRP   B NE1 1 
ATOM   590  N  NE1 B TRP   B 2 41  ? -15.093 5.436   -3.239  0.50 37.45  ? 50  TRP   B NE1 1 
ATOM   591  C  CE2 A TRP   B 2 41  ? -15.604 5.298   -2.898  0.50 41.44  ? 50  TRP   B CE2 1 
ATOM   592  C  CE2 B TRP   B 2 41  ? -16.307 5.029   -2.753  0.50 37.12  ? 50  TRP   B CE2 1 
ATOM   593  C  CE3 A TRP   B 2 41  ? -13.804 5.043   -4.493  0.50 41.38  ? 50  TRP   B CE3 1 
ATOM   594  C  CE3 B TRP   B 2 41  ? -18.084 3.533   -3.412  0.50 36.99  ? 50  TRP   B CE3 1 
ATOM   595  C  CZ2 A TRP   B 2 41  ? -14.830 6.134   -2.091  0.50 42.43  ? 50  TRP   B CZ2 1 
ATOM   596  C  CZ2 B TRP   B 2 41  ? -16.982 5.396   -1.594  0.50 37.49  ? 50  TRP   B CZ2 1 
ATOM   597  C  CZ3 A TRP   B 2 41  ? -13.043 5.879   -3.697  0.50 42.41  ? 50  TRP   B CZ3 1 
ATOM   598  C  CZ3 B TRP   B 2 41  ? -18.722 3.857   -2.233  0.50 37.84  ? 50  TRP   B CZ3 1 
ATOM   599  C  CH2 A TRP   B 2 41  ? -13.545 6.389   -2.497  0.50 42.58  ? 50  TRP   B CH2 1 
ATOM   600  C  CH2 B TRP   B 2 41  ? -18.183 4.796   -1.351  0.50 37.62  ? 50  TRP   B CH2 1 
ATOM   601  N  N   . HIS   B 2 42  ? -14.605 5.092   -8.076  1.00 40.11  ? 51  HIS   B N   1 
ATOM   602  C  CA  . HIS   B 2 42  ? -13.683 6.231   -8.272  1.00 41.10  ? 51  HIS   B CA  1 
ATOM   603  C  C   . HIS   B 2 42  ? -14.266 7.395   -9.121  1.00 42.20  ? 51  HIS   B C   1 
ATOM   604  O  O   . HIS   B 2 42  ? -13.678 8.473   -9.158  1.00 42.42  ? 51  HIS   B O   1 
ATOM   605  C  CB  . HIS   B 2 42  ? -12.318 5.777   -8.825  1.00 40.95  ? 51  HIS   B CB  1 
ATOM   606  C  CG  . HIS   B 2 42  ? -12.324 5.470   -10.289 1.00 42.74  ? 51  HIS   B CG  1 
ATOM   607  N  ND1 . HIS   B 2 42  ? -12.549 4.182   -10.763 1.00 44.48  ? 51  HIS   B ND1 1 
ATOM   608  C  CD2 . HIS   B 2 42  ? -12.135 6.292   -11.346 1.00 43.09  ? 51  HIS   B CD2 1 
ATOM   609  C  CE1 . HIS   B 2 42  ? -12.479 4.271   -12.079 1.00 44.10  ? 51  HIS   B CE1 1 
ATOM   610  N  NE2 . HIS   B 2 42  ? -12.233 5.520   -12.472 1.00 43.74  ? 51  HIS   B NE2 1 
ATOM   611  N  N   . VAL   B 2 43  ? -15.408 7.179   -9.786  1.00 42.16  ? 52  VAL   B N   1 
ATOM   612  C  CA  . VAL   B 2 43  ? -16.056 8.212   -10.581 1.00 42.40  ? 52  VAL   B CA  1 
ATOM   613  C  C   . VAL   B 2 43  ? -16.772 9.221   -9.653  1.00 42.99  ? 52  VAL   B C   1 
ATOM   614  O  O   . VAL   B 2 43  ? -16.523 10.427  -9.729  1.00 43.39  ? 52  VAL   B O   1 
ATOM   615  C  CB  . VAL   B 2 43  ? -17.031 7.579   -11.619 1.00 42.81  ? 52  VAL   B CB  1 
ATOM   616  C  CG1 . VAL   B 2 43  ? -17.953 8.626   -12.246 1.00 43.21  ? 52  VAL   B CG1 1 
ATOM   617  C  CG2 . VAL   B 2 43  ? -16.275 6.810   -12.689 1.00 42.94  ? 52  VAL   B CG2 1 
ATOM   618  N  N   . THR   B 2 44  ? -17.627 8.721   -8.744  1.00 42.42  ? 53  THR   B N   1 
ATOM   619  C  CA  . THR   B 2 44  ? -18.406 9.594   -7.873  1.00 41.71  ? 53  THR   B CA  1 
ATOM   620  C  C   . THR   B 2 44  ? -17.854 9.766   -6.467  1.00 42.31  ? 53  THR   B C   1 
ATOM   621  O  O   . THR   B 2 44  ? -18.266 10.698  -5.768  1.00 42.12  ? 53  THR   B O   1 
ATOM   622  C  CB  . THR   B 2 44  ? -19.841 9.073   -7.771  1.00 41.01  ? 53  THR   B CB  1 
ATOM   623  O  OG1 . THR   B 2 44  ? -19.847 7.866   -7.024  1.00 40.58  ? 53  THR   B OG1 1 
ATOM   624  C  CG2 . THR   B 2 44  ? -20.481 8.819   -9.125  1.00 41.88  ? 53  THR   B CG2 1 
ATOM   625  N  N   . LYS   B 2 45  ? -16.960 8.845   -6.039  1.00 42.61  ? 54  LYS   B N   1 
ATOM   626  C  CA  . LYS   B 2 45  ? -16.458 8.707   -4.659  1.00 43.57  ? 54  LYS   B CA  1 
ATOM   627  C  C   . LYS   B 2 45  ? -17.624 8.446   -3.679  1.00 43.07  ? 54  LYS   B C   1 
ATOM   628  O  O   . LYS   B 2 45  ? -17.509 8.768   -2.503  1.00 43.39  ? 54  LYS   B O   1 
ATOM   629  C  CB  . LYS   B 2 45  ? -15.625 9.914   -4.178  1.00 46.68  ? 54  LYS   B CB  1 
ATOM   630  C  CG  . LYS   B 2 45  ? -14.601 10.443  -5.165  1.00 52.75  ? 54  LYS   B CG  1 
ATOM   631  C  CD  . LYS   B 2 45  ? -13.484 9.477   -5.482  1.00 58.96  ? 54  LYS   B CD  1 
ATOM   632  C  CE  . LYS   B 2 45  ? -12.516 10.179  -6.421  1.00 64.89  ? 54  LYS   B CE  1 
ATOM   633  N  NZ  . LYS   B 2 45  ? -11.787 9.239   -7.330  1.00 68.39  ? 54  LYS   B NZ  1 
ATOM   634  N  N   . GLY   B 2 46  ? -18.737 7.898   -4.166  1.00 42.46  ? 55  GLY   B N   1 
ATOM   635  C  CA  . GLY   B 2 46  ? -19.908 7.634   -3.348  1.00 42.86  ? 55  GLY   B CA  1 
ATOM   636  C  C   . GLY   B 2 46  ? -20.809 8.829   -3.104  1.00 43.53  ? 55  GLY   B C   1 
ATOM   637  O  O   . GLY   B 2 46  ? -21.771 8.717   -2.352  1.00 43.74  ? 55  GLY   B O   1 
ATOM   638  N  N   . ALA   B 2 47  ? -20.532 9.982   -3.729  1.00 43.79  ? 56  ALA   B N   1 
ATOM   639  C  CA  . ALA   B 2 47  ? -21.348 11.186  -3.540  1.00 44.39  ? 56  ALA   B CA  1 
ATOM   640  C  C   . ALA   B 2 47  ? -22.714 11.100  -4.241  1.00 45.75  ? 56  ALA   B C   1 
ATOM   641  O  O   . ALA   B 2 47  ? -22.884 10.297  -5.150  1.00 46.35  ? 56  ALA   B O   1 
ATOM   642  C  CB  . ALA   B 2 47  ? -20.580 12.411  -4.032  1.00 44.02  ? 56  ALA   B CB  1 
ATOM   643  N  N   . ALA   B 2 48  ? -23.678 11.936  -3.844  1.00 46.19  ? 57  ALA   B N   1 
ATOM   644  C  CA  . ALA   B 2 48  ? -24.998 11.948  -4.456  1.00 46.94  ? 57  ALA   B CA  1 
ATOM   645  C  C   . ALA   B 2 48  ? -24.963 12.507  -5.869  1.00 48.04  ? 57  ALA   B C   1 
ATOM   646  O  O   . ALA   B 2 48  ? -24.140 13.354  -6.195  1.00 48.42  ? 57  ALA   B O   1 
ATOM   647  C  CB  . ALA   B 2 48  ? -25.973 12.741  -3.603  1.00 46.78  ? 57  ALA   B CB  1 
ATOM   648  N  N   . LEU   B 2 49  ? -25.847 12.009  -6.712  1.00 48.44  ? 58  LEU   B N   1 
ATOM   649  C  CA  . LEU   B 2 49  ? -25.932 12.438  -8.095  1.00 49.27  ? 58  LEU   B CA  1 
ATOM   650  C  C   . LEU   B 2 49  ? -27.256 13.153  -8.338  1.00 50.87  ? 58  LEU   B C   1 
ATOM   651  O  O   . LEU   B 2 49  ? -28.210 12.987  -7.587  1.00 51.41  ? 58  LEU   B O   1 
ATOM   652  C  CB  . LEU   B 2 49  ? -25.788 11.235  -9.043  1.00 48.72  ? 58  LEU   B CB  1 
ATOM   653  C  CG  . LEU   B 2 49  ? -24.510 10.425  -8.907  1.00 48.86  ? 58  LEU   B CG  1 
ATOM   654  C  CD1 . LEU   B 2 49  ? -24.557 9.217   -9.793  1.00 48.84  ? 58  LEU   B CD1 1 
ATOM   655  C  CD2 . LEU   B 2 49  ? -23.298 11.258  -9.226  1.00 49.14  ? 58  LEU   B CD2 1 
ATOM   656  N  N   . ARG   B 2 50  ? -27.299 13.969  -9.365  1.00 51.52  ? 59  ARG   B N   1 
ATOM   657  C  CA  . ARG   B 2 50  ? -28.489 14.705  -9.715  1.00 52.90  ? 59  ARG   B CA  1 
ATOM   658  C  C   . ARG   B 2 50  ? -28.953 14.264  -11.107 1.00 53.58  ? 59  ARG   B C   1 
ATOM   659  O  O   . ARG   B 2 50  ? -28.125 13.992  -11.969 1.00 53.14  ? 59  ARG   B O   1 
ATOM   660  C  CB  . ARG   B 2 50  ? -28.165 16.200  -9.656  1.00 55.00  ? 59  ARG   B CB  1 
ATOM   661  C  CG  . ARG   B 2 50  ? -29.275 17.091  -10.132 1.00 59.53  ? 59  ARG   B CG  1 
ATOM   662  C  CD  . ARG   B 2 50  ? -29.019 18.555  -9.810  1.00 64.09  ? 59  ARG   B CD  1 
ATOM   663  N  NE  . ARG   B 2 50  ? -27.714 19.044  -10.269 1.00 67.75  ? 59  ARG   B NE  1 
ATOM   664  C  CZ  . ARG   B 2 50  ? -27.443 19.412  -11.519 1.00 70.56  ? 59  ARG   B CZ  1 
ATOM   665  N  NH1 . ARG   B 2 50  ? -28.369 19.305  -12.468 1.00 69.88  ? 59  ARG   B NH1 1 
ATOM   666  N  NH2 . ARG   B 2 50  ? -26.238 19.871  -11.834 1.00 71.26  ? 59  ARG   B NH2 1 
ATOM   667  N  N   . SER   B 2 51  ? -30.261 14.118  -11.311 1.00 54.60  ? 60  SER   B N   1 
ATOM   668  C  CA  . SER   B 2 51  ? -30.798 13.773  -12.627 1.00 56.70  ? 60  SER   B CA  1 
ATOM   669  C  C   . SER   B 2 51  ? -31.888 14.796  -12.924 1.00 59.26  ? 60  SER   B C   1 
ATOM   670  O  O   . SER   B 2 51  ? -33.049 14.573  -12.607 1.00 59.95  ? 60  SER   B O   1 
ATOM   671  C  CB  . SER   B 2 51  ? -31.354 12.355  -12.635 1.00 57.50  ? 60  SER   B CB  1 
ATOM   672  O  OG  . SER   B 2 51  ? -31.879 12.026  -13.908 1.00 59.37  ? 60  SER   B OG  1 
ATOM   673  N  N   . GLY   B 2 52  ? -31.486 15.956  -13.424 1.00 60.31  ? 61  GLY   B N   1 
ATOM   674  C  CA  . GLY   B 2 52  ? -32.420 17.041  -13.676 1.00 61.34  ? 61  GLY   B CA  1 
ATOM   675  C  C   . GLY   B 2 52  ? -32.854 17.636  -12.358 1.00 62.63  ? 61  GLY   B C   1 
ATOM   676  O  O   . GLY   B 2 52  ? -32.051 18.275  -11.674 1.00 63.65  ? 61  GLY   B O   1 
ATOM   677  N  N   . GLU   B 2 53  ? -34.094 17.364  -11.944 1.00 62.36  ? 62  GLU   B N   1 
ATOM   678  C  CA  . GLU   B 2 53  ? -34.596 17.862  -10.666 1.00 62.54  ? 62  GLU   B CA  1 
ATOM   679  C  C   . GLU   B 2 53  ? -34.395 16.865  -9.522  1.00 62.24  ? 62  GLU   B C   1 
ATOM   680  O  O   . GLU   B 2 53  ? -34.147 17.268  -8.382  1.00 62.62  ? 62  GLU   B O   1 
ATOM   681  C  CB  . GLU   B 2 53  ? -36.077 18.212  -10.781 1.00 65.37  ? 62  GLU   B CB  1 
ATOM   682  C  CG  . GLU   B 2 53  ? -36.346 19.705  -10.784 1.00 71.92  ? 62  GLU   B CG  1 
ATOM   683  C  CD  . GLU   B 2 53  ? -37.805 20.039  -11.029 1.00 79.71  ? 62  GLU   B CD  1 
ATOM   684  O  OE1 . GLU   B 2 53  ? -38.400 19.449  -11.962 1.00 80.69  ? 62  GLU   B OE1 1 
ATOM   685  O  OE2 . GLU   B 2 53  ? -38.356 20.885  -10.286 1.00 81.70  ? 62  GLU   B OE2 1 
ATOM   686  N  N   . GLY   B 2 54  ? -34.533 15.582  -9.833  1.00 61.44  ? 63  GLY   B N   1 
ATOM   687  C  CA  . GLY   B 2 54  ? -34.414 14.511  -8.857  1.00 60.67  ? 63  GLY   B CA  1 
ATOM   688  C  C   . GLY   B 2 54  ? -33.007 14.245  -8.376  1.00 59.47  ? 63  GLY   B C   1 
ATOM   689  O  O   . GLY   B 2 54  ? -32.033 14.536  -9.073  1.00 60.01  ? 63  GLY   B O   1 
ATOM   690  N  N   . ARG   B 2 55  ? -32.901 13.674  -7.175  1.00 57.40  ? 64  ARG   B N   1 
ATOM   691  C  CA  . ARG   B 2 55  ? -31.637 13.320  -6.545  1.00 55.76  ? 64  ARG   B CA  1 
ATOM   692  C  C   . ARG   B 2 55  ? -31.470 11.779  -6.557  1.00 53.66  ? 64  ARG   B C   1 
ATOM   693  O  O   . ARG   B 2 55  ? -32.450 11.040  -6.466  1.00 53.85  ? 64  ARG   B O   1 
ATOM   694  C  CB  . ARG   B 2 55  ? -31.643 13.850  -5.091  1.00 56.61  ? 64  ARG   B CB  1 
ATOM   695  C  CG  . ARG   B 2 55  ? -30.301 13.789  -4.357  1.00 59.49  ? 64  ARG   B CG  1 
ATOM   696  C  CD  . ARG   B 2 55  ? -30.480 14.146  -2.883  1.00 62.91  ? 64  ARG   B CD  1 
ATOM   697  N  NE  . ARG   B 2 55  ? -29.250 13.980  -2.103  1.00 65.79  ? 64  ARG   B NE  1 
ATOM   698  C  CZ  . ARG   B 2 55  ? -28.658 14.957  -1.417  1.00 67.55  ? 64  ARG   B CZ  1 
ATOM   699  N  NH1 . ARG   B 2 55  ? -29.171 16.185  -1.417  1.00 66.86  ? 64  ARG   B NH1 1 
ATOM   700  N  NH2 . ARG   B 2 55  ? -27.546 14.716  -0.733  1.00 66.97  ? 64  ARG   B NH2 1 
ATOM   701  N  N   . LEU   B 2 56  ? -30.241 11.305  -6.692  1.00 51.31  ? 65  LEU   B N   1 
ATOM   702  C  CA  . LEU   B 2 56  ? -29.943 9.880   -6.651  1.00 49.81  ? 65  LEU   B CA  1 
ATOM   703  C  C   . LEU   B 2 56  ? -29.029 9.678   -5.462  1.00 47.37  ? 65  LEU   B C   1 
ATOM   704  O  O   . LEU   B 2 56  ? -27.996 10.340  -5.379  1.00 46.72  ? 65  LEU   B O   1 
ATOM   705  C  CB  . LEU   B 2 56  ? -29.226 9.408   -7.926  1.00 50.22  ? 65  LEU   B CB  1 
ATOM   706  C  CG  . LEU   B 2 56  ? -29.865 9.698   -9.279  1.00 52.73  ? 65  LEU   B CG  1 
ATOM   707  C  CD1 . LEU   B 2 56  ? -29.130 8.956   -10.366 1.00 53.47  ? 65  LEU   B CD1 1 
ATOM   708  C  CD2 . LEU   B 2 56  ? -31.320 9.275   -9.319  1.00 53.81  ? 65  LEU   B CD2 1 
ATOM   709  N  N   . ASP   B 2 57  ? -29.428 8.839   -4.511  1.00 45.98  ? 66  ASP   B N   1 
ATOM   710  C  CA  . ASP   B 2 57  ? -28.601 8.597   -3.330  1.00 45.50  ? 66  ASP   B CA  1 
ATOM   711  C  C   . ASP   B 2 57  ? -27.917 7.234   -3.436  1.00 44.73  ? 66  ASP   B C   1 
ATOM   712  O  O   . ASP   B 2 57  ? -28.509 6.279   -3.955  1.00 45.09  ? 66  ASP   B O   1 
ATOM   713  C  CB  . ASP   B 2 57  ? -29.431 8.703   -2.039  1.00 47.95  ? 66  ASP   B CB  1 
ATOM   714  C  CG  . ASP   B 2 57  ? -30.109 10.053  -1.874  1.00 54.76  ? 66  ASP   B CG  1 
ATOM   715  O  OD1 . ASP   B 2 57  ? -29.407 11.093  -1.988  1.00 55.31  ? 66  ASP   B OD1 1 
ATOM   716  O  OD2 . ASP   B 2 57  ? -31.342 10.073  -1.650  1.00 58.08  ? 66  ASP   B OD2 1 
ATOM   717  N  N   . PRO   B 2 58  ? -26.647 7.134   -2.990  1.00 43.10  ? 67  PRO   B N   1 
ATOM   718  C  CA  . PRO   B 2 58  ? -25.957 5.836   -3.034  1.00 42.09  ? 67  PRO   B CA  1 
ATOM   719  C  C   . PRO   B 2 58  ? -26.660 4.786   -2.172  1.00 41.90  ? 67  PRO   B C   1 
ATOM   720  O  O   . PRO   B 2 58  ? -27.268 5.115   -1.157  1.00 43.09  ? 67  PRO   B O   1 
ATOM   721  C  CB  . PRO   B 2 58  ? -24.560 6.164   -2.500  1.00 42.54  ? 67  PRO   B CB  1 
ATOM   722  C  CG  . PRO   B 2 58  ? -24.761 7.380   -1.665  1.00 43.35  ? 67  PRO   B CG  1 
ATOM   723  C  CD  . PRO   B 2 58  ? -25.825 8.172   -2.341  1.00 41.93  ? 67  PRO   B CD  1 
ATOM   724  N  N   . TYR   B 2 59  ? -26.628 3.532   -2.598  1.00 40.44  ? 68  TYR   B N   1 
ATOM   725  C  CA  . TYR   B 2 59  ? -27.285 2.458   -1.880  1.00 38.87  ? 68  TYR   B CA  1 
ATOM   726  C  C   . TYR   B 2 59  ? -26.265 1.440   -1.432  1.00 38.42  ? 68  TYR   B C   1 
ATOM   727  O  O   . TYR   B 2 59  ? -26.280 1.031   -0.287  1.00 38.63  ? 68  TYR   B O   1 
ATOM   728  C  CB  . TYR   B 2 59  ? -28.379 1.827   -2.753  1.00 37.85  ? 68  TYR   B CB  1 
ATOM   729  C  CG  . TYR   B 2 59  ? -29.153 0.695   -2.111  1.00 37.06  ? 68  TYR   B CG  1 
ATOM   730  C  CD1 . TYR   B 2 59  ? -28.598 -0.573  -1.992  1.00 37.25  ? 68  TYR   B CD1 1 
ATOM   731  C  CD2 . TYR   B 2 59  ? -30.489 0.846   -1.780  1.00 37.10  ? 68  TYR   B CD2 1 
ATOM   732  C  CE1 . TYR   B 2 59  ? -29.313 -1.627  -1.432  1.00 37.63  ? 68  TYR   B CE1 1 
ATOM   733  C  CE2 . TYR   B 2 59  ? -31.234 -0.214  -1.289  1.00 37.76  ? 68  TYR   B CE2 1 
ATOM   734  C  CZ  . TYR   B 2 59  ? -30.642 -1.452  -1.113  1.00 38.46  ? 68  TYR   B CZ  1 
ATOM   735  O  OH  . TYR   B 2 59  ? -31.387 -2.495  -0.622  1.00 39.62  ? 68  TYR   B OH  1 
ATOM   736  N  N   . TRP   B 2 60  ? -25.388 1.031   -2.315  1.00 38.39  ? 69  TRP   B N   1 
ATOM   737  C  CA  . TRP   B 2 60  ? -24.362 0.047   -2.018  1.00 38.46  ? 69  TRP   B CA  1 
ATOM   738  C  C   . TRP   B 2 60  ? -23.069 0.518   -2.671  1.00 39.75  ? 69  TRP   B C   1 
ATOM   739  O  O   . TRP   B 2 60  ? -23.096 1.057   -3.772  1.00 40.00  ? 69  TRP   B O   1 
ATOM   740  C  CB  . TRP   B 2 60  ? -24.773 -1.346  -2.561  1.00 38.08  ? 69  TRP   B CB  1 
ATOM   741  C  CG  . TRP   B 2 60  ? -23.644 -2.345  -2.516  1.00 37.88  ? 69  TRP   B CG  1 
ATOM   742  C  CD1 . TRP   B 2 60  ? -23.184 -3.012  -1.415  1.00 38.45  ? 69  TRP   B CD1 1 
ATOM   743  C  CD2 . TRP   B 2 60  ? -22.727 -2.641  -3.578  1.00 37.57  ? 69  TRP   B CD2 1 
ATOM   744  N  NE1 . TRP   B 2 60  ? -22.052 -3.724  -1.733  1.00 38.53  ? 69  TRP   B NE1 1 
ATOM   745  C  CE2 . TRP   B 2 60  ? -21.741 -3.504  -3.053  1.00 38.09  ? 69  TRP   B CE2 1 
ATOM   746  C  CE3 . TRP   B 2 60  ? -22.617 -2.223  -4.909  1.00 38.14  ? 69  TRP   B CE3 1 
ATOM   747  C  CZ2 . TRP   B 2 60  ? -20.671 -3.964  -3.816  1.00 38.27  ? 69  TRP   B CZ2 1 
ATOM   748  C  CZ3 . TRP   B 2 60  ? -21.565 -2.696  -5.671  1.00 38.71  ? 69  TRP   B CZ3 1 
ATOM   749  C  CH2 . TRP   B 2 60  ? -20.610 -3.560  -5.127  1.00 38.66  ? 69  TRP   B CH2 1 
ATOM   750  N  N   . GLY   B 2 61  ? -21.945 0.278   -2.020  1.00 40.41  ? 70  GLY   B N   1 
ATOM   751  C  CA  . GLY   B 2 61  ? -20.650 0.660   -2.576  1.00 41.08  ? 70  GLY   B CA  1 
ATOM   752  C  C   . GLY   B 2 61  ? -19.512 -0.097  -1.948  1.00 40.66  ? 70  GLY   B C   1 
ATOM   753  O  O   . GLY   B 2 61  ? -19.644 -0.555  -0.826  1.00 41.03  ? 70  GLY   B O   1 
ATOM   754  N  N   . ASP   B 2 62  ? -18.397 -0.238  -2.661  1.00 40.31  ? 71  ASP   B N   1 
ATOM   755  C  CA  . ASP   B 2 62  ? -17.238 -0.978  -2.199  1.00 40.29  ? 71  ASP   B CA  1 
ATOM   756  C  C   . ASP   B 2 62  ? -16.018 -0.502  -2.976  1.00 40.29  ? 71  ASP   B C   1 
ATOM   757  O  O   . ASP   B 2 62  ? -15.966 -0.649  -4.201  1.00 40.17  ? 71  ASP   B O   1 
ATOM   758  C  CB  . ASP   B 2 62  ? -17.449 -2.479  -2.442  1.00 42.67  ? 71  ASP   B CB  1 
ATOM   759  C  CG  . ASP   B 2 62  ? -16.479 -3.372  -1.704  1.00 48.90  ? 71  ASP   B CG  1 
ATOM   760  O  OD1 . ASP   B 2 62  ? -15.343 -3.534  -2.177  1.00 49.48  ? 71  ASP   B OD1 1 
ATOM   761  O  OD2 . ASP   B 2 62  ? -16.860 -3.910  -0.656  1.00 54.32  ? 71  ASP   B OD2 1 
ATOM   762  N  N   . VAL   B 2 63  ? -15.032 0.047   -2.258  1.00 40.32  ? 72  VAL   B N   1 
ATOM   763  C  CA  . VAL   B 2 63  ? -13.800 0.586   -2.816  1.00 40.56  ? 72  VAL   B CA  1 
ATOM   764  C  C   . VAL   B 2 63  ? -12.931 -0.499  -3.455  1.00 40.87  ? 72  VAL   B C   1 
ATOM   765  O  O   . VAL   B 2 63  ? -12.343 -0.248  -4.505  1.00 41.01  ? 72  VAL   B O   1 
ATOM   766  C  CB  . VAL   B 2 63  ? -13.060 1.419   -1.743  1.00 41.08  ? 72  VAL   B CB  1 
ATOM   767  C  CG1 . VAL   B 2 63  ? -11.587 1.610   -2.063  1.00 41.55  ? 72  VAL   B CG1 1 
ATOM   768  C  CG2 . VAL   B 2 63  ? -13.740 2.764   -1.559  1.00 41.79  ? 72  VAL   B CG2 1 
ATOM   769  N  N   . LYS   B 2 64  ? -12.887 -1.709  -2.873  1.00 40.89  ? 73  LYS   B N   1 
ATOM   770  C  CA  . LYS   B 2 64  ? -12.046 -2.772  -3.434  1.00 40.43  ? 73  LYS   B CA  1 
ATOM   771  C  C   . LYS   B 2 64  ? -12.577 -3.263  -4.762  1.00 40.53  ? 73  LYS   B C   1 
ATOM   772  O  O   . LYS   B 2 64  ? -11.820 -3.339  -5.735  1.00 40.36  ? 73  LYS   B O   1 
ATOM   773  C  CB  . LYS   B 2 64  ? -11.809 -3.908  -2.443  1.00 41.55  ? 73  LYS   B CB  1 
ATOM   774  C  CG  . LYS   B 2 64  ? -10.700 -4.841  -2.928  1.00 44.58  ? 73  LYS   B CG  1 
ATOM   775  C  CD  . LYS   B 2 64  ? -10.188 -5.704  -1.800  1.00 48.34  ? 73  LYS   B CD  1 
ATOM   776  C  CE  . LYS   B 2 64  ? -9.482  -6.894  -2.357  1.00 51.76  ? 73  LYS   B CE  1 
ATOM   777  N  NZ  . LYS   B 2 64  ? -9.093  -7.822  -1.284  1.00 54.85  ? 73  LYS   B NZ  1 
ATOM   778  N  N   . GLN   B 2 65  ? -13.896 -3.522  -4.836  1.00 40.18  ? 74  GLN   B N   1 
ATOM   779  C  CA  . GLN   B 2 65  ? -14.535 -3.904  -6.097  1.00 39.58  ? 74  GLN   B CA  1 
ATOM   780  C  C   . GLN   B 2 65  ? -14.546 -2.726  -7.097  1.00 39.15  ? 74  GLN   B C   1 
ATOM   781  O  O   . GLN   B 2 65  ? -14.667 -2.941  -8.303  1.00 39.40  ? 74  GLN   B O   1 
ATOM   782  C  CB  . GLN   B 2 65  ? -15.990 -4.356  -5.843  1.00 41.46  ? 74  GLN   B CB  1 
ATOM   783  C  CG  . GLN   B 2 65  ? -16.121 -5.699  -5.124  1.00 45.86  ? 74  GLN   B CG  1 
ATOM   784  C  CD  . GLN   B 2 65  ? -17.575 -6.135  -4.934  1.00 51.74  ? 74  GLN   B CD  1 
ATOM   785  O  OE1 . GLN   B 2 65  ? -18.392 -6.167  -5.880  1.00 53.23  ? 74  GLN   B OE1 1 
ATOM   786  N  NE2 . GLN   B 2 65  ? -17.921 -6.511  -3.698  1.00 52.24  ? 74  GLN   B NE2 1 
ATOM   787  N  N   . ASP   B 2 66  ? -14.452 -1.484  -6.582  1.00 38.28  ? 75  ASP   B N   1 
ATOM   788  C  CA  . ASP   B 2 66  ? -14.490 -0.217  -7.306  1.00 37.31  ? 75  ASP   B CA  1 
ATOM   789  C  C   . ASP   B 2 66  ? -15.832 -0.051  -7.971  1.00 36.07  ? 75  ASP   B C   1 
ATOM   790  O  O   . ASP   B 2 66  ? -15.896 0.439   -9.085  1.00 35.25  ? 75  ASP   B O   1 
ATOM   791  C  CB  . ASP   B 2 66  ? -13.322 -0.039  -8.292  1.00 38.83  ? 75  ASP   B CB  1 
ATOM   792  C  CG  . ASP   B 2 66  ? -13.209 1.385   -8.811  1.00 42.61  ? 75  ASP   B CG  1 
ATOM   793  O  OD1 . ASP   B 2 66  ? -13.542 2.328   -8.044  1.00 44.55  ? 75  ASP   B OD1 1 
ATOM   794  O  OD2 . ASP   B 2 66  ? -12.794 1.561   -9.974  1.00 42.17  ? 75  ASP   B OD2 1 
ATOM   795  N  N   . LEU   B 2 67  ? -16.927 -0.408  -7.255  1.00 35.65  ? 76  LEU   B N   1 
ATOM   796  C  CA  . LEU   B 2 67  ? -18.290 -0.277  -7.759  1.00 35.16  ? 76  LEU   B CA  1 
ATOM   797  C  C   . LEU   B 2 67  ? -19.213 0.451   -6.770  1.00 35.59  ? 76  LEU   B C   1 
ATOM   798  O  O   . LEU   B 2 67  ? -18.952 0.492   -5.566  1.00 35.50  ? 76  LEU   B O   1 
ATOM   799  C  CB  . LEU   B 2 67  ? -18.876 -1.661  -8.075  1.00 34.59  ? 76  LEU   B CB  1 
ATOM   800  C  CG  . LEU   B 2 67  ? -18.183 -2.461  -9.149  1.00 35.24  ? 76  LEU   B CG  1 
ATOM   801  C  CD1 . LEU   B 2 67  ? -18.716 -3.869  -9.176  1.00 36.09  ? 76  LEU   B CD1 1 
ATOM   802  C  CD2 . LEU   B 2 67  ? -18.296 -1.801  -10.506 1.00 35.11  ? 76  LEU   B CD2 1 
ATOM   803  N  N   . VAL   B 2 68  ? -20.314 1.014   -7.286  1.00 35.70  ? 77  VAL   B N   1 
ATOM   804  C  CA  . VAL   B 2 68  ? -21.324 1.722   -6.478  1.00 35.34  ? 77  VAL   B CA  1 
ATOM   805  C  C   . VAL   B 2 68  ? -22.683 1.716   -7.231  1.00 35.48  ? 77  VAL   B C   1 
ATOM   806  O  O   . VAL   B 2 68  ? -22.704 1.737   -8.446  1.00 35.47  ? 77  VAL   B O   1 
ATOM   807  C  CB  . VAL   B 2 68  ? -20.859 3.155   -6.113  1.00 35.20  ? 77  VAL   B CB  1 
ATOM   808  C  CG1 . VAL   B 2 68  ? -20.538 3.964   -7.360  1.00 35.30  ? 77  VAL   B CG1 1 
ATOM   809  C  CG2 . VAL   B 2 68  ? -21.878 3.880   -5.227  1.00 35.51  ? 77  VAL   B CG2 1 
ATOM   810  N  N   . SER   B 2 69  ? -23.797 1.603   -6.509  1.00 35.89  ? 78  SER   B N   1 
ATOM   811  C  CA  . SER   B 2 69  ? -25.146 1.597   -7.077  1.00 35.61  ? 78  SER   B CA  1 
ATOM   812  C  C   . SER   B 2 69  ? -25.980 2.661   -6.364  1.00 35.38  ? 78  SER   B C   1 
ATOM   813  O  O   . SER   B 2 69  ? -25.731 2.982   -5.206  1.00 35.58  ? 78  SER   B O   1 
ATOM   814  C  CB  . SER   B 2 69  ? -25.797 0.213   -6.971  1.00 36.11  ? 78  SER   B CB  1 
ATOM   815  O  OG  . SER   B 2 69  ? -26.205 -0.104  -5.648  1.00 36.90  ? 78  SER   B OG  1 
ATOM   816  N  N   . TYR   B 2 70  ? -26.935 3.240   -7.084  1.00 35.27  ? 79  TYR   B N   1 
ATOM   817  C  CA  . TYR   B 2 70  ? -27.757 4.357   -6.652  1.00 35.77  ? 79  TYR   B CA  1 
ATOM   818  C  C   . TYR   B 2 70  ? -29.223 3.979   -6.767  1.00 36.24  ? 79  TYR   B C   1 
ATOM   819  O  O   . TYR   B 2 70  ? -29.623 3.413   -7.794  1.00 35.77  ? 79  TYR   B O   1 
ATOM   820  C  CB  . TYR   B 2 70  ? -27.476 5.555   -7.590  1.00 35.71  ? 79  TYR   B CB  1 
ATOM   821  C  CG  . TYR   B 2 70  ? -26.150 6.214   -7.295  1.00 36.75  ? 79  TYR   B CG  1 
ATOM   822  C  CD1 . TYR   B 2 70  ? -24.971 5.753   -7.877  1.00 37.35  ? 79  TYR   B CD1 1 
ATOM   823  C  CD2 . TYR   B 2 70  ? -26.068 7.284   -6.419  1.00 37.87  ? 79  TYR   B CD2 1 
ATOM   824  C  CE1 . TYR   B 2 70  ? -23.744 6.335   -7.575  1.00 38.04  ? 79  TYR   B CE1 1 
ATOM   825  C  CE2 . TYR   B 2 70  ? -24.849 7.854   -6.090  1.00 38.60  ? 79  TYR   B CE2 1 
ATOM   826  C  CZ  . TYR   B 2 70  ? -23.689 7.372   -6.659  1.00 39.53  ? 79  TYR   B CZ  1 
ATOM   827  O  OH  . TYR   B 2 70  ? -22.509 7.993   -6.335  1.00 41.06  ? 79  TYR   B OH  1 
ATOM   828  N  N   . CYS   B 2 71  ? -30.021 4.263   -5.718  1.00 36.30  ? 80  CYS   B N   1 
ATOM   829  C  CA  . CYS   B 2 71  ? -31.473 4.008   -5.725  1.00 37.76  ? 80  CYS   B CA  1 
ATOM   830  C  C   . CYS   B 2 71  ? -31.866 2.558   -5.393  1.00 38.00  ? 80  CYS   B C   1 
ATOM   831  O  O   . CYS   B 2 71  ? -33.034 2.315   -5.056  1.00 39.94  ? 80  CYS   B O   1 
ATOM   832  C  CB  . CYS   B 2 71  ? -32.121 4.467   -7.031  1.00 40.34  ? 80  CYS   B CB  1 
ATOM   833  S  SG  . CYS   B 2 71  ? -31.769 6.198   -7.480  1.00 48.30  ? 80  CYS   B SG  1 
ATOM   834  N  N   . GLY   B 2 72  ? -30.917 1.626   -5.424  1.00 35.50  ? 81  GLY   B N   1 
ATOM   835  C  CA  . GLY   B 2 72  ? -31.229 0.243   -5.095  1.00 34.46  ? 81  GLY   B CA  1 
ATOM   836  C  C   . GLY   B 2 72  ? -30.029 -0.661  -5.199  1.00 34.25  ? 81  GLY   B C   1 
ATOM   837  O  O   . GLY   B 2 72  ? -28.922 -0.224  -5.523  1.00 33.52  ? 81  GLY   B O   1 
ATOM   838  N  N   . PRO   B 2 73  ? -30.234 -1.949  -4.907  1.00 34.55  ? 82  PRO   B N   1 
ATOM   839  C  CA  . PRO   B 2 73  ? -29.114 -2.897  -4.992  1.00 35.23  ? 82  PRO   B CA  1 
ATOM   840  C  C   . PRO   B 2 73  ? -28.599 -3.120  -6.418  1.00 37.17  ? 82  PRO   B C   1 
ATOM   841  O  O   . PRO   B 2 73  ? -29.342 -2.926  -7.387  1.00 37.87  ? 82  PRO   B O   1 
ATOM   842  C  CB  . PRO   B 2 73  ? -29.701 -4.186  -4.426  1.00 35.59  ? 82  PRO   B CB  1 
ATOM   843  C  CG  . PRO   B 2 73  ? -31.188 -4.045  -4.598  1.00 35.62  ? 82  PRO   B CG  1 
ATOM   844  C  CD  . PRO   B 2 73  ? -31.490 -2.592  -4.474  1.00 33.49  ? 82  PRO   B CD  1 
ATOM   845  N  N   . TRP   B 2 74  ? -27.333 -3.586  -6.548  1.00 37.27  ? 83  TRP   B N   1 
ATOM   846  C  CA  . TRP   B 2 74  ? -26.691 -3.909  -7.818  1.00 38.23  ? 83  TRP   B CA  1 
ATOM   847  C  C   . TRP   B 2 74  ? -27.570 -4.898  -8.613  1.00 39.71  ? 83  TRP   B C   1 
ATOM   848  O  O   . TRP   B 2 74  ? -27.960 -5.939  -8.082  1.00 40.19  ? 83  TRP   B O   1 
ATOM   849  C  CB  . TRP   B 2 74  ? -25.279 -4.490  -7.565  1.00 37.56  ? 83  TRP   B CB  1 
ATOM   850  C  CG  . TRP   B 2 74  ? -24.454 -4.642  -8.803  1.00 37.52  ? 83  TRP   B CG  1 
ATOM   851  C  CD1 . TRP   B 2 74  ? -24.346 -5.755  -9.582  1.00 38.36  ? 83  TRP   B CD1 1 
ATOM   852  C  CD2 . TRP   B 2 74  ? -23.636 -3.633  -9.426  1.00 37.53  ? 83  TRP   B CD2 1 
ATOM   853  N  NE1 . TRP   B 2 74  ? -23.513 -5.506  -10.650 1.00 38.77  ? 83  TRP   B NE1 1 
ATOM   854  C  CE2 . TRP   B 2 74  ? -23.095 -4.200  -10.601 1.00 38.37  ? 83  TRP   B CE2 1 
ATOM   855  C  CE3 . TRP   B 2 74  ? -23.309 -2.306  -9.104  1.00 37.41  ? 83  TRP   B CE3 1 
ATOM   856  C  CZ2 . TRP   B 2 74  ? -22.242 -3.487  -11.449 1.00 38.62  ? 83  TRP   B CZ2 1 
ATOM   857  C  CZ3 . TRP   B 2 74  ? -22.462 -1.604  -9.938  1.00 37.81  ? 83  TRP   B CZ3 1 
ATOM   858  C  CH2 . TRP   B 2 74  ? -21.945 -2.189  -11.101 1.00 38.46  ? 83  TRP   B CH2 1 
ATOM   859  N  N   . LYS   B 2 75  ? -27.936 -4.542  -9.852  1.00 40.11  ? 84  LYS   B N   1 
ATOM   860  C  CA  . LYS   B 2 75  ? -28.842 -5.373  -10.643 1.00 40.56  ? 84  LYS   B CA  1 
ATOM   861  C  C   . LYS   B 2 75  ? -28.150 -6.192  -11.720 1.00 41.94  ? 84  LYS   B C   1 
ATOM   862  O  O   . LYS   B 2 75  ? -28.729 -7.165  -12.196 1.00 41.95  ? 84  LYS   B O   1 
ATOM   863  C  CB  . LYS   B 2 75  ? -29.919 -4.495  -11.311 1.00 40.86  ? 84  LYS   B CB  1 
ATOM   864  C  CG  . LYS   B 2 75  ? -30.756 -3.658  -10.357 1.00 42.12  ? 84  LYS   B CG  1 
ATOM   865  C  CD  . LYS   B 2 75  ? -31.737 -4.512  -9.560  1.00 45.12  ? 84  LYS   B CD  1 
ATOM   866  C  CE  . LYS   B 2 75  ? -32.635 -3.675  -8.688  1.00 47.80  ? 84  LYS   B CE  1 
ATOM   867  N  NZ  . LYS   B 2 75  ? -33.724 -4.483  -8.087  1.00 49.57  ? 84  LYS   B NZ  1 
ATOM   868  N  N   . LEU   B 2 76  ? -26.956 -5.768  -12.162 1.00 42.86  ? 85  LEU   B N   1 
ATOM   869  C  CA  . LEU   B 2 76  ? -26.258 -6.393  -13.285 1.00 43.71  ? 85  LEU   B CA  1 
ATOM   870  C  C   . LEU   B 2 76  ? -25.595 -7.698  -12.888 1.00 45.76  ? 85  LEU   B C   1 
ATOM   871  O  O   . LEU   B 2 76  ? -24.682 -7.685  -12.069 1.00 46.33  ? 85  LEU   B O   1 
ATOM   872  C  CB  . LEU   B 2 76  ? -25.238 -5.425  -13.917 1.00 43.08  ? 85  LEU   B CB  1 
ATOM   873  C  CG  . LEU   B 2 76  ? -25.656 -3.953  -14.083 1.00 43.08  ? 85  LEU   B CG  1 
ATOM   874  C  CD1 . LEU   B 2 76  ? -24.509 -3.119  -14.575 1.00 42.91  ? 85  LEU   B CD1 1 
ATOM   875  C  CD2 . LEU   B 2 76  ? -26.812 -3.804  -15.021 1.00 43.51  ? 85  LEU   B CD2 1 
ATOM   876  N  N   . ASP   B 2 77  ? -26.032 -8.828  -13.481 1.00 46.80  ? 86  ASP   B N   1 
ATOM   877  C  CA  . ASP   B 2 77  ? -25.500 -10.140 -13.117 1.00 48.53  ? 86  ASP   B CA  1 
ATOM   878  C  C   . ASP   B 2 77  ? -24.914 -10.974 -14.261 1.00 49.22  ? 86  ASP   B C   1 
ATOM   879  O  O   . ASP   B 2 77  ? -24.364 -12.040 -13.983 1.00 50.28  ? 86  ASP   B O   1 
ATOM   880  C  CB  . ASP   B 2 77  ? -26.552 -10.983 -12.353 1.00 51.35  ? 86  ASP   B CB  1 
ATOM   881  C  CG  . ASP   B 2 77  ? -27.876 -11.185 -13.072 1.00 59.00  ? 86  ASP   B CG  1 
ATOM   882  O  OD1 . ASP   B 2 77  ? -28.113 -10.499 -14.095 1.00 60.36  ? 86  ASP   B OD1 1 
ATOM   883  O  OD2 . ASP   B 2 77  ? -28.688 -12.010 -12.600 1.00 62.79  ? 86  ASP   B OD2 1 
ATOM   884  N  N   . ALA   B 2 78  ? -25.001 -10.524 -15.517 1.00 49.04  ? 87  ALA   B N   1 
ATOM   885  C  CA  . ALA   B 2 78  ? -24.433 -11.292 -16.637 1.00 49.04  ? 87  ALA   B CA  1 
ATOM   886  C  C   . ALA   B 2 78  ? -22.904 -11.437 -16.502 1.00 49.29  ? 87  ALA   B C   1 
ATOM   887  O  O   . ALA   B 2 78  ? -22.259 -10.609 -15.860 1.00 48.54  ? 87  ALA   B O   1 
ATOM   888  C  CB  . ALA   B 2 78  ? -24.792 -10.651 -17.968 1.00 48.35  ? 87  ALA   B CB  1 
ATOM   889  N  N   . ALA   B 2 79  ? -22.328 -12.499 -17.093 1.00 49.93  ? 88  ALA   B N   1 
ATOM   890  C  CA  . ALA   B 2 79  ? -20.890 -12.718 -17.007 1.00 50.82  ? 88  ALA   B CA  1 
ATOM   891  C  C   . ALA   B 2 79  ? -20.287 -13.169 -18.327 1.00 51.68  ? 88  ALA   B C   1 
ATOM   892  O  O   . ALA   B 2 79  ? -20.930 -13.908 -19.061 1.00 51.85  ? 88  ALA   B O   1 
ATOM   893  C  CB  . ALA   B 2 79  ? -20.590 -13.734 -15.924 1.00 51.18  ? 88  ALA   B CB  1 
ATOM   894  N  N   . TRP   B 2 80  ? -19.038 -12.754 -18.619 1.00 52.07  ? 89  TRP   B N   1 
ATOM   895  C  CA  . TRP   B 2 80  ? -18.315 -13.159 -19.827 1.00 53.15  ? 89  TRP   B CA  1 
ATOM   896  C  C   . TRP   B 2 80  ? -18.168 -14.685 -19.843 1.00 54.75  ? 89  TRP   B C   1 
ATOM   897  O  O   . TRP   B 2 80  ? -17.919 -15.282 -18.791 1.00 54.77  ? 89  TRP   B O   1 
ATOM   898  C  CB  . TRP   B 2 80  ? -16.926 -12.509 -19.852 1.00 53.00  ? 89  TRP   B CB  1 
ATOM   899  C  CG  . TRP   B 2 80  ? -16.113 -12.865 -21.062 1.00 53.33  ? 89  TRP   B CG  1 
ATOM   900  C  CD1 . TRP   B 2 80  ? -16.511 -12.805 -22.360 1.00 54.12  ? 89  TRP   B CD1 1 
ATOM   901  C  CD2 . TRP   B 2 80  ? -14.743 -13.286 -21.081 1.00 53.24  ? 89  TRP   B CD2 1 
ATOM   902  N  NE1 . TRP   B 2 80  ? -15.490 -13.211 -23.188 1.00 54.42  ? 89  TRP   B NE1 1 
ATOM   903  C  CE2 . TRP   B 2 80  ? -14.383 -13.482 -22.431 1.00 53.94  ? 89  TRP   B CE2 1 
ATOM   904  C  CE3 . TRP   B 2 80  ? -13.789 -13.534 -20.088 1.00 53.52  ? 89  TRP   B CE3 1 
ATOM   905  C  CZ2 . TRP   B 2 80  ? -13.105 -13.895 -22.814 1.00 54.17  ? 89  TRP   B CZ2 1 
ATOM   906  C  CZ3 . TRP   B 2 80  ? -12.522 -13.947 -20.470 1.00 54.24  ? 89  TRP   B CZ3 1 
ATOM   907  C  CH2 . TRP   B 2 80  ? -12.190 -14.116 -21.818 1.00 54.13  ? 89  TRP   B CH2 1 
ATOM   908  N  N   . ASP   B 2 81  ? -18.371 -15.319 -21.006 1.00 56.09  ? 90  ASP   B N   1 
ATOM   909  C  CA  . ASP   B 2 81  ? -18.300 -16.774 -21.078 1.00 57.59  ? 90  ASP   B CA  1 
ATOM   910  C  C   . ASP   B 2 81  ? -16.872 -17.336 -21.232 1.00 58.78  ? 90  ASP   B C   1 
ATOM   911  O  O   . ASP   B 2 81  ? -16.700 -18.562 -21.280 1.00 59.77  ? 90  ASP   B O   1 
ATOM   912  C  CB  . ASP   B 2 81  ? -19.239 -17.323 -22.159 1.00 59.54  ? 90  ASP   B CB  1 
ATOM   913  C  CG  . ASP   B 2 81  ? -18.921 -16.921 -23.574 1.00 65.91  ? 90  ASP   B CG  1 
ATOM   914  O  OD1 . ASP   B 2 81  ? -17.895 -16.237 -23.784 1.00 67.58  ? 90  ASP   B OD1 1 
ATOM   915  O  OD2 . ASP   B 2 81  ? -19.702 -17.280 -24.481 1.00 68.97  ? 90  ASP   B OD2 1 
ATOM   916  N  N   . GLY   B 2 82  ? -15.870 -16.464 -21.271 1.00 58.50  ? 91  GLY   B N   1 
ATOM   917  C  CA  . GLY   B 2 82  ? -14.486 -16.891 -21.400 1.00 59.31  ? 91  GLY   B CA  1 
ATOM   918  C  C   . GLY   B 2 82  ? -14.075 -17.292 -22.804 1.00 60.03  ? 91  GLY   B C   1 
ATOM   919  O  O   . GLY   B 2 82  ? -12.908 -17.614 -23.035 1.00 60.21  ? 91  GLY   B O   1 
ATOM   920  N  N   . LEU   B 2 83  ? -15.016 -17.257 -23.762 1.00 60.15  ? 92  LEU   B N   1 
ATOM   921  C  CA  . LEU   B 2 83  ? -14.746 -17.674 -25.120 1.00 60.91  ? 92  LEU   B CA  1 
ATOM   922  C  C   . LEU   B 2 83  ? -15.024 -16.639 -26.179 1.00 61.77  ? 92  LEU   B C   1 
ATOM   923  O  O   . LEU   B 2 83  ? -14.239 -16.512 -27.115 1.00 62.66  ? 92  LEU   B O   1 
ATOM   924  C  CB  . LEU   B 2 83  ? -15.608 -18.899 -25.442 1.00 61.36  ? 92  LEU   B CB  1 
ATOM   925  C  CG  . LEU   B 2 83  ? -14.958 -20.251 -25.307 1.00 63.25  ? 92  LEU   B CG  1 
ATOM   926  C  CD1 . LEU   B 2 83  ? -15.100 -20.763 -23.909 1.00 63.51  ? 92  LEU   B CD1 1 
ATOM   927  C  CD2 . LEU   B 2 83  ? -15.628 -21.221 -26.228 1.00 64.40  ? 92  LEU   B CD2 1 
ATOM   928  N  N   . SER   B 2 84  ? -16.189 -15.973 -26.117 1.00 61.29  ? 93  SER   B N   1 
ATOM   929  C  CA  . SER   B 2 84  ? -16.622 -15.109 -27.208 1.00 60.74  ? 93  SER   B CA  1 
ATOM   930  C  C   . SER   B 2 84  ? -16.302 -13.620 -27.051 1.00 60.78  ? 93  SER   B C   1 
ATOM   931  O  O   . SER   B 2 84  ? -16.008 -13.139 -25.955 1.00 61.68  ? 93  SER   B O   1 
ATOM   932  C  CB  . SER   B 2 84  ? -18.113 -15.307 -27.495 1.00 61.41  ? 93  SER   B CB  1 
ATOM   933  O  OG  . SER   B 2 84  ? -18.889 -15.716 -26.381 1.00 63.08  ? 93  SER   B OG  1 
ATOM   934  N  N   . GLU   B 2 85  ? -16.315 -12.917 -28.187 1.00 59.91  ? 94  GLU   B N   1 
ATOM   935  C  CA  . GLU   B 2 85  ? -16.072 -11.494 -28.303 1.00 59.34  ? 94  GLU   B CA  1 
ATOM   936  C  C   . GLU   B 2 85  ? -17.185 -10.715 -27.607 1.00 57.70  ? 94  GLU   B C   1 
ATOM   937  O  O   . GLU   B 2 85  ? -18.288 -11.218 -27.369 1.00 58.11  ? 94  GLU   B O   1 
ATOM   938  C  CB  . GLU   B 2 85  ? -15.939 -11.075 -29.791 1.00 61.45  ? 94  GLU   B CB  1 
ATOM   939  C  CG  . GLU   B 2 85  ? -14.680 -11.614 -30.450 1.00 65.87  ? 94  GLU   B CG  1 
ATOM   940  C  CD  . GLU   B 2 85  ? -14.131 -10.866 -31.653 1.00 70.82  ? 94  GLU   B CD  1 
ATOM   941  O  OE1 . GLU   B 2 85  ? -14.893 -10.103 -32.289 1.00 70.42  ? 94  GLU   B OE1 1 
ATOM   942  O  OE2 . GLU   B 2 85  ? -12.930 -11.046 -31.959 1.00 72.73  ? 94  GLU   B OE2 1 
ATOM   943  N  N   . VAL   B 2 86  ? -16.858 -9.499  -27.217 1.00 55.47  ? 95  VAL   B N   1 
ATOM   944  C  CA  . VAL   B 2 86  ? -17.741 -8.629  -26.455 1.00 53.10  ? 95  VAL   B CA  1 
ATOM   945  C  C   . VAL   B 2 86  ? -17.684 -7.233  -27.057 1.00 52.14  ? 95  VAL   B C   1 
ATOM   946  O  O   . VAL   B 2 86  ? -16.776 -6.932  -27.839 1.00 52.81  ? 95  VAL   B O   1 
ATOM   947  C  CB  . VAL   B 2 86  ? -17.299 -8.588  -24.953 1.00 51.74  ? 95  VAL   B CB  1 
ATOM   948  C  CG1 . VAL   B 2 86  ? -17.137 -9.986  -24.371 1.00 51.94  ? 95  VAL   B CG1 1 
ATOM   949  C  CG2 . VAL   B 2 86  ? -16.022 -7.772  -24.775 1.00 51.35  ? 95  VAL   B CG2 1 
ATOM   950  N  N   . GLN   B 2 87  ? -18.611 -6.357  -26.649 1.00 50.37  ? 96  GLN   B N   1 
ATOM   951  C  CA  . GLN   B 2 87  ? -18.574 -4.985  -27.099 1.00 49.34  ? 96  GLN   B CA  1 
ATOM   952  C  C   . GLN   B 2 87  ? -18.418 -4.033  -25.926 1.00 48.12  ? 96  GLN   B C   1 
ATOM   953  O  O   . GLN   B 2 87  ? -19.054 -4.205  -24.891 1.00 47.52  ? 96  GLN   B O   1 
ATOM   954  C  CB  . GLN   B 2 87  ? -19.791 -4.642  -27.981 1.00 49.99  ? 96  GLN   B CB  1 
ATOM   955  C  CG  . GLN   B 2 87  ? -19.569 -5.128  -29.404 1.00 51.91  ? 96  GLN   B CG  1 
ATOM   956  C  CD  . GLN   B 2 87  ? -20.672 -4.817  -30.369 1.00 54.85  ? 96  GLN   B CD  1 
ATOM   957  O  OE1 . GLN   B 2 87  ? -21.523 -3.941  -30.147 1.00 54.58  ? 96  GLN   B OE1 1 
ATOM   958  N  NE2 . GLN   B 2 87  ? -20.656 -5.526  -31.496 1.00 55.80  ? 96  GLN   B NE2 1 
ATOM   959  N  N   . LEU   B 2 88  ? -17.540 -3.056  -26.083 1.00 47.09  ? 97  LEU   B N   1 
ATOM   960  C  CA  . LEU   B 2 88  ? -17.410 -2.013  -25.106 1.00 46.91  ? 97  LEU   B CA  1 
ATOM   961  C  C   . LEU   B 2 88  ? -18.286 -0.883  -25.667 1.00 46.13  ? 97  LEU   B C   1 
ATOM   962  O  O   . LEU   B 2 88  ? -18.037 -0.438  -26.782 1.00 46.85  ? 97  LEU   B O   1 
ATOM   963  C  CB  . LEU   B 2 88  ? -15.949 -1.558  -24.956 1.00 47.38  ? 97  LEU   B CB  1 
ATOM   964  C  CG  . LEU   B 2 88  ? -15.744 -0.217  -24.223 1.00 49.52  ? 97  LEU   B CG  1 
ATOM   965  C  CD1 . LEU   B 2 88  ? -16.374 -0.227  -22.840 1.00 49.53  ? 97  LEU   B CD1 1 
ATOM   966  C  CD2 . LEU   B 2 88  ? -14.277 0.166   -24.165 1.00 50.62  ? 97  LEU   B CD2 1 
ATOM   967  N  N   . LEU   B 2 89  ? -19.335 -0.476  -24.950 1.00 44.67  ? 98  LEU   B N   1 
ATOM   968  C  CA  . LEU   B 2 89  ? -20.152 0.650   -25.406 1.00 44.15  ? 98  LEU   B CA  1 
ATOM   969  C  C   . LEU   B 2 89  ? -19.466 1.853   -24.779 1.00 44.99  ? 98  LEU   B C   1 
ATOM   970  O  O   . LEU   B 2 89  ? -19.801 2.270   -23.675 1.00 45.24  ? 98  LEU   B O   1 
ATOM   971  C  CB  . LEU   B 2 89  ? -21.642 0.503   -25.030 1.00 43.25  ? 98  LEU   B CB  1 
ATOM   972  C  CG  . LEU   B 2 89  ? -22.611 1.696   -25.280 1.00 44.04  ? 98  LEU   B CG  1 
ATOM   973  C  CD1 . LEU   B 2 89  ? -22.407 2.343   -26.636 1.00 44.74  ? 98  LEU   B CD1 1 
ATOM   974  C  CD2 . LEU   B 2 89  ? -24.034 1.247   -25.171 1.00 44.06  ? 98  LEU   B CD2 1 
ATOM   975  N  N   . ALA   B 2 90  ? -18.406 2.329   -25.445 1.00 45.08  ? 99  ALA   B N   1 
ATOM   976  C  CA  . ALA   B 2 90  ? -17.585 3.430   -24.960 1.00 45.12  ? 99  ALA   B CA  1 
ATOM   977  C  C   . ALA   B 2 90  ? -18.272 4.758   -25.114 1.00 44.75  ? 99  ALA   B C   1 
ATOM   978  O  O   . ALA   B 2 90  ? -18.593 5.143   -26.228 1.00 44.71  ? 99  ALA   B O   1 
ATOM   979  C  CB  . ALA   B 2 90  ? -16.262 3.464   -25.716 1.00 45.30  ? 99  ALA   B CB  1 
ATOM   980  N  N   . VAL   B 2 91  ? -18.417 5.507   -24.020 1.00 44.36  ? 100 VAL   B N   1 
ATOM   981  C  CA  . VAL   B 2 91  ? -18.981 6.845   -24.084 1.00 44.87  ? 100 VAL   B CA  1 
ATOM   982  C  C   . VAL   B 2 91  ? -17.861 7.841   -23.711 1.00 45.41  ? 100 VAL   B C   1 
ATOM   983  O  O   . VAL   B 2 91  ? -17.654 8.134   -22.546 1.00 45.51  ? 100 VAL   B O   1 
ATOM   984  C  CB  . VAL   B 2 91  ? -20.230 6.952   -23.183 1.00 45.22  ? 100 VAL   B CB  1 
ATOM   985  C  CG1 . VAL   B 2 91  ? -20.867 8.337   -23.283 1.00 45.56  ? 100 VAL   B CG1 1 
ATOM   986  C  CG2 . VAL   B 2 91  ? -21.238 5.862   -23.532 1.00 45.15  ? 100 VAL   B CG2 1 
ATOM   987  N  N   . PRO   B 2 92  ? -17.080 8.325   -24.688 1.00 46.09  ? 101 PRO   B N   1 
ATOM   988  C  CA  . PRO   B 2 92  ? -15.950 9.217   -24.352 1.00 46.76  ? 101 PRO   B CA  1 
ATOM   989  C  C   . PRO   B 2 92  ? -16.351 10.672  -24.147 1.00 47.81  ? 101 PRO   B C   1 
ATOM   990  O  O   . PRO   B 2 92  ? -17.379 11.092  -24.674 1.00 48.15  ? 101 PRO   B O   1 
ATOM   991  C  CB  . PRO   B 2 92  ? -14.979 9.028   -25.535 1.00 47.33  ? 101 PRO   B CB  1 
ATOM   992  C  CG  . PRO   B 2 92  ? -15.748 8.265   -26.593 1.00 47.70  ? 101 PRO   B CG  1 
ATOM   993  C  CD  . PRO   B 2 92  ? -17.167 8.076   -26.138 1.00 45.73  ? 101 PRO   B CD  1 
ATOM   994  N  N   . PRO   B 2 93  ? -15.571 11.467  -23.394 1.00 48.35  ? 102 PRO   B N   1 
ATOM   995  C  CA  . PRO   B 2 93  ? -15.964 12.877  -23.175 1.00 49.14  ? 102 PRO   B CA  1 
ATOM   996  C  C   . PRO   B 2 93  ? -16.083 13.682  -24.472 1.00 50.78  ? 102 PRO   B C   1 
ATOM   997  O  O   . PRO   B 2 93  ? -15.208 13.598  -25.341 1.00 51.47  ? 102 PRO   B O   1 
ATOM   998  C  CB  . PRO   B 2 93  ? -14.870 13.418  -22.239 1.00 49.40  ? 102 PRO   B CB  1 
ATOM   999  C  CG  . PRO   B 2 93  ? -14.271 12.186  -21.596 1.00 49.33  ? 102 PRO   B CG  1 
ATOM   1000 C  CD  . PRO   B 2 93  ? -14.343 11.117  -22.651 1.00 47.72  ? 102 PRO   B CD  1 
ATOM   1001 N  N   . GLY   B 2 94  ? -17.204 14.393  -24.622 1.00 51.00  ? 103 GLY   B N   1 
ATOM   1002 C  CA  . GLY   B 2 94  ? -17.518 15.212  -25.792 1.00 51.30  ? 103 GLY   B CA  1 
ATOM   1003 C  C   . GLY   B 2 94  ? -17.784 14.452  -27.083 1.00 51.89  ? 103 GLY   B C   1 
ATOM   1004 O  O   . GLY   B 2 94  ? -17.966 15.052  -28.145 1.00 51.99  ? 103 GLY   B O   1 
ATOM   1005 N  N   . GLU   B 2 95  ? -17.738 13.129  -27.024 1.00 52.26  ? 104 GLU   B N   1 
ATOM   1006 C  CA  . GLU   B 2 95  ? -17.914 12.288  -28.196 1.00 52.86  ? 104 GLU   B CA  1 
ATOM   1007 C  C   . GLU   B 2 95  ? -19.099 11.372  -27.995 1.00 53.23  ? 104 GLU   B C   1 
ATOM   1008 O  O   . GLU   B 2 95  ? -19.439 11.022  -26.865 1.00 53.27  ? 104 GLU   B O   1 
ATOM   1009 C  CB  . GLU   B 2 95  ? -16.635 11.474  -28.468 1.00 55.23  ? 104 GLU   B CB  1 
ATOM   1010 C  CG  . GLU   B 2 95  ? -15.384 12.336  -28.589 1.00 60.27  ? 104 GLU   B CG  1 
ATOM   1011 C  CD  . GLU   B 2 95  ? -14.090 11.586  -28.842 1.00 68.26  ? 104 GLU   B CD  1 
ATOM   1012 O  OE1 . GLU   B 2 95  ? -14.128 10.334  -28.905 1.00 70.57  ? 104 GLU   B OE1 1 
ATOM   1013 O  OE2 . GLU   B 2 95  ? -13.036 12.251  -28.984 1.00 70.10  ? 104 GLU   B OE2 1 
ATOM   1014 N  N   . ARG   B 2 96  ? -19.720 10.988  -29.094 1.00 53.52  ? 105 ARG   B N   1 
ATOM   1015 C  CA  . ARG   B 2 96  ? -20.897 10.145  -29.154 1.00 54.83  ? 105 ARG   B CA  1 
ATOM   1016 C  C   . ARG   B 2 96  ? -20.600 8.733   -28.685 1.00 55.62  ? 105 ARG   B C   1 
ATOM   1017 O  O   . ARG   B 2 96  ? -19.476 8.256   -28.863 1.00 56.16  ? 105 ARG   B O   1 
ATOM   1018 C  CB  . ARG   B 2 96  ? -21.402 10.151  -30.611 1.00 57.58  ? 105 ARG   B CB  1 
ATOM   1019 C  CG  . ARG   B 2 96  ? -22.457 9.113   -30.973 1.00 63.53  ? 105 ARG   B CG  1 
ATOM   1020 C  CD  . ARG   B 2 96  ? -23.574 9.650   -31.863 1.00 69.58  ? 105 ARG   B CD  1 
ATOM   1021 N  NE  . ARG   B 2 96  ? -23.103 10.506  -32.954 1.00 75.29  ? 105 ARG   B NE  1 
ATOM   1022 C  CZ  . ARG   B 2 96  ? -22.563 10.057  -34.085 1.00 79.96  ? 105 ARG   B CZ  1 
ATOM   1023 N  NH1 . ARG   B 2 96  ? -22.172 10.911  -35.024 1.00 80.03  ? 105 ARG   B NH1 1 
ATOM   1024 N  NH2 . ARG   B 2 96  ? -22.402 8.750   -34.282 1.00 80.71  ? 105 ARG   B NH2 1 
ATOM   1025 N  N   . ALA   B 2 97  ? -21.608 8.051   -28.081 1.00 55.49  ? 106 ALA   B N   1 
ATOM   1026 C  CA  . ALA   B 2 97  ? -21.519 6.662   -27.637 1.00 55.84  ? 106 ALA   B CA  1 
ATOM   1027 C  C   . ALA   B 2 97  ? -21.112 5.771   -28.827 1.00 56.63  ? 106 ALA   B C   1 
ATOM   1028 O  O   . ALA   B 2 97  ? -21.614 5.975   -29.932 1.00 57.56  ? 106 ALA   B O   1 
ATOM   1029 C  CB  . ALA   B 2 97  ? -22.861 6.218   -27.088 1.00 55.84  ? 106 ALA   B CB  1 
ATOM   1030 N  N   . LYS   B 2 98  ? -20.175 4.845   -28.631 1.00 56.50  ? 107 LYS   B N   1 
ATOM   1031 C  CA  . LYS   B 2 98  ? -19.656 4.047   -29.738 1.00 57.24  ? 107 LYS   B CA  1 
ATOM   1032 C  C   . LYS   B 2 98  ? -19.296 2.599   -29.342 1.00 56.61  ? 107 LYS   B C   1 
ATOM   1033 O  O   . LYS   B 2 98  ? -18.615 2.374   -28.338 1.00 57.08  ? 107 LYS   B O   1 
ATOM   1034 C  CB  . LYS   B 2 98  ? -18.471 4.826   -30.333 1.00 60.56  ? 107 LYS   B CB  1 
ATOM   1035 C  CG  . LYS   B 2 98  ? -17.478 4.064   -31.195 1.00 65.95  ? 107 LYS   B CG  1 
ATOM   1036 C  CD  . LYS   B 2 98  ? -16.238 4.941   -31.477 1.00 71.06  ? 107 LYS   B CD  1 
ATOM   1037 C  CE  . LYS   B 2 98  ? -15.639 5.574   -30.225 1.00 74.77  ? 107 LYS   B CE  1 
ATOM   1038 N  NZ  . LYS   B 2 98  ? -14.151 5.508   -30.223 1.00 77.22  ? 107 LYS   B NZ  1 
ATOM   1039 N  N   . ASN   B 2 99  ? -19.819 1.620   -30.091 1.00 55.44  ? 108 ASN   B N   1 
ATOM   1040 C  CA  . ASN   B 2 99  ? -19.601 0.202   -29.809 1.00 55.44  ? 108 ASN   B CA  1 
ATOM   1041 C  C   . ASN   B 2 99  ? -18.300 -0.282  -30.412 1.00 55.97  ? 108 ASN   B C   1 
ATOM   1042 O  O   . ASN   B 2 99  ? -18.112 -0.161  -31.617 1.00 57.00  ? 108 ASN   B O   1 
ATOM   1043 C  CB  . ASN   B 2 99  ? -20.745 -0.650  -30.367 1.00 55.86  ? 108 ASN   B CB  1 
ATOM   1044 C  CG  . ASN   B 2 99  ? -22.083 -0.426  -29.709 1.00 59.71  ? 108 ASN   B CG  1 
ATOM   1045 O  OD1 . ASN   B 2 99  ? -22.632 0.689   -29.707 1.00 61.65  ? 108 ASN   B OD1 1 
ATOM   1046 N  ND2 . ASN   B 2 99  ? -22.659 -1.482  -29.158 1.00 59.93  ? 108 ASN   B ND2 1 
ATOM   1047 N  N   . ILE   B 2 100 ? -17.408 -0.837  -29.601 1.00 55.15  ? 109 ILE   B N   1 
ATOM   1048 C  CA  . ILE   B 2 100 ? -16.144 -1.374  -30.096 1.00 55.09  ? 109 ILE   B CA  1 
ATOM   1049 C  C   . ILE   B 2 100 ? -16.065 -2.859  -29.753 1.00 54.75  ? 109 ILE   B C   1 
ATOM   1050 O  O   . ILE   B 2 100 ? -15.986 -3.212  -28.579 1.00 54.83  ? 109 ILE   B O   1 
ATOM   1051 C  CB  . ILE   B 2 100 ? -14.943 -0.626  -29.488 1.00 55.62  ? 109 ILE   B CB  1 
ATOM   1052 C  CG1 . ILE   B 2 100 ? -15.058 0.894   -29.679 1.00 56.43  ? 109 ILE   B CG1 1 
ATOM   1053 C  CG2 . ILE   B 2 100 ? -13.633 -1.195  -30.023 1.00 56.14  ? 109 ILE   B CG2 1 
ATOM   1054 C  CD1 . ILE   B 2 100 ? -14.967 1.363   -31.097 1.00 57.52  ? 109 ILE   B CD1 1 
ATOM   1055 N  N   . GLN   B 2 101 ? -16.065 -3.725  -30.764 1.00 54.08  ? 110 GLN   B N   1 
ATOM   1056 C  CA  . GLN   B 2 101 ? -16.001 -5.166  -30.550 1.00 53.98  ? 110 GLN   B CA  1 
ATOM   1057 C  C   . GLN   B 2 101 ? -14.561 -5.636  -30.342 1.00 54.56  ? 110 GLN   B C   1 
ATOM   1058 O  O   . GLN   B 2 101 ? -13.665 -5.220  -31.068 1.00 54.70  ? 110 GLN   B O   1 
ATOM   1059 C  CB  . GLN   B 2 101 ? -16.657 -5.882  -31.731 1.00 55.13  ? 110 GLN   B CB  1 
ATOM   1060 C  CG  . GLN   B 2 101 ? -16.615 -7.397  -31.626 1.00 58.00  ? 110 GLN   B CG  1 
ATOM   1061 C  CD  . GLN   B 2 101 ? -17.724 -8.053  -32.399 1.00 60.11  ? 110 GLN   B CD  1 
ATOM   1062 O  OE1 . GLN   B 2 101 ? -18.794 -7.470  -32.636 1.00 59.96  ? 110 GLN   B OE1 1 
ATOM   1063 N  NE2 . GLN   B 2 101 ? -17.490 -9.291  -32.793 1.00 59.95  ? 110 GLN   B NE2 1 
ATOM   1064 N  N   . THR   B 2 102 ? -14.325 -6.494  -29.342 1.00 54.90  ? 111 THR   B N   1 
ATOM   1065 C  CA  . THR   B 2 102 ? -12.978 -6.978  -29.041 1.00 55.17  ? 111 THR   B CA  1 
ATOM   1066 C  C   . THR   B 2 102 ? -13.027 -8.345  -28.377 1.00 54.84  ? 111 THR   B C   1 
ATOM   1067 O  O   . THR   B 2 102 ? -14.077 -8.722  -27.859 1.00 55.08  ? 111 THR   B O   1 
ATOM   1068 C  CB  . THR   B 2 102 ? -12.260 -5.961  -28.107 1.00 57.05  ? 111 THR   B CB  1 
ATOM   1069 O  OG1 . THR   B 2 102 ? -10.898 -6.361  -27.904 1.00 58.47  ? 111 THR   B OG1 1 
ATOM   1070 C  CG2 . THR   B 2 102 ? -12.971 -5.769  -26.767 1.00 57.53  ? 111 THR   B CG2 1 
ATOM   1071 N  N   . LEU   B 2 103 ? -11.907 -9.102  -28.397 1.00 54.22  ? 112 LEU   B N   1 
ATOM   1072 C  CA  . LEU   B 2 103 ? -11.867 -10.360 -27.663 1.00 54.42  ? 112 LEU   B CA  1 
ATOM   1073 C  C   . LEU   B 2 103 ? -11.106 -10.062 -26.385 1.00 55.36  ? 112 LEU   B C   1 
ATOM   1074 O  O   . LEU   B 2 103 ? -9.959  -9.587  -26.429 1.00 55.72  ? 112 LEU   B O   1 
ATOM   1075 C  CB  . LEU   B 2 103 ? -11.185 -11.517 -28.395 1.00 54.83  ? 112 LEU   B CB  1 
ATOM   1076 C  CG  . LEU   B 2 103 ? -11.250 -12.818 -27.587 1.00 56.66  ? 112 LEU   B CG  1 
ATOM   1077 C  CD1 . LEU   B 2 103 ? -12.559 -13.540 -27.813 1.00 57.36  ? 112 LEU   B CD1 1 
ATOM   1078 C  CD2 . LEU   B 2 103 ? -10.067 -13.702 -27.845 1.00 57.13  ? 112 LEU   B CD2 1 
ATOM   1079 N  N   . PRO   B 2 104 ? -11.717 -10.337 -25.226 1.00 55.13  ? 113 PRO   B N   1 
ATOM   1080 C  CA  . PRO   B 2 104 ? -11.031 -10.040 -23.978 1.00 55.33  ? 113 PRO   B CA  1 
ATOM   1081 C  C   . PRO   B 2 104 ? -9.904  -11.008 -23.668 1.00 56.38  ? 113 PRO   B C   1 
ATOM   1082 O  O   . PRO   B 2 104 ? -9.922  -12.174 -24.061 1.00 56.42  ? 113 PRO   B O   1 
ATOM   1083 C  CB  . PRO   B 2 104 ? -12.143 -10.125 -22.927 1.00 55.66  ? 113 PRO   B CB  1 
ATOM   1084 C  CG  . PRO   B 2 104 ? -13.422 -10.236 -23.684 1.00 55.94  ? 113 PRO   B CG  1 
ATOM   1085 C  CD  . PRO   B 2 104 ? -13.073 -10.858 -24.990 1.00 54.39  ? 113 PRO   B CD  1 
ATOM   1086 N  N   . GLY   B 2 105 ? -8.922  -10.481 -22.959 1.00 56.56  ? 114 GLY   B N   1 
ATOM   1087 C  CA  . GLY   B 2 105 ? -7.816  -11.226 -22.392 1.00 56.53  ? 114 GLY   B CA  1 
ATOM   1088 C  C   . GLY   B 2 105 ? -8.175  -11.625 -20.972 1.00 56.25  ? 114 GLY   B C   1 
ATOM   1089 O  O   . GLY   B 2 105 ? -9.359  -11.655 -20.614 1.00 56.09  ? 114 GLY   B O   1 
ATOM   1090 N  N   . ILE   B 2 106 ? -7.166  -11.919 -20.139 1.00 55.94  ? 115 ILE   B N   1 
ATOM   1091 C  CA  . ILE   B 2 106 ? -7.368  -12.387 -18.768 1.00 56.39  ? 115 ILE   B CA  1 
ATOM   1092 C  C   . ILE   B 2 106 ? -6.478  -11.653 -17.764 1.00 56.66  ? 115 ILE   B C   1 
ATOM   1093 O  O   . ILE   B 2 106 ? -5.284  -11.507 -18.000 1.00 57.42  ? 115 ILE   B O   1 
ATOM   1094 C  CB  . ILE   B 2 106 ? -6.972  -13.904 -18.665 1.00 57.46  ? 115 ILE   B CB  1 
ATOM   1095 C  CG1 . ILE   B 2 106 ? -7.669  -14.802 -19.681 1.00 59.44  ? 115 ILE   B CG1 1 
ATOM   1096 C  CG2 . ILE   B 2 106 ? -7.160  -14.451 -17.270 1.00 58.34  ? 115 ILE   B CG2 1 
ATOM   1097 C  CD1 . ILE   B 2 106 ? -9.103  -14.836 -19.575 1.00 61.31  ? 115 ILE   B CD1 1 
ATOM   1098 N  N   . PHE   B 2 107 ? -7.029  -11.310 -16.592 1.00 55.74  ? 116 PHE   B N   1 
ATOM   1099 C  CA  . PHE   B 2 107 ? -6.282  -10.840 -15.431 1.00 55.14  ? 116 PHE   B CA  1 
ATOM   1100 C  C   . PHE   B 2 107 ? -6.235  -12.087 -14.559 1.00 55.44  ? 116 PHE   B C   1 
ATOM   1101 O  O   . PHE   B 2 107 ? -7.286  -12.522 -14.095 1.00 55.65  ? 116 PHE   B O   1 
ATOM   1102 C  CB  . PHE   B 2 107 ? -7.063  -9.759  -14.656 1.00 54.26  ? 116 PHE   B CB  1 
ATOM   1103 C  CG  . PHE   B 2 107 ? -6.816  -8.324  -15.057 1.00 54.19  ? 116 PHE   B CG  1 
ATOM   1104 C  CD1 . PHE   B 2 107 ? -6.157  -8.017  -16.240 1.00 54.64  ? 116 PHE   B CD1 1 
ATOM   1105 C  CD2 . PHE   B 2 107 ? -7.265  -7.281  -14.267 1.00 54.49  ? 116 PHE   B CD2 1 
ATOM   1106 C  CE1 . PHE   B 2 107 ? -5.954  -6.696  -16.618 1.00 54.96  ? 116 PHE   B CE1 1 
ATOM   1107 C  CE2 . PHE   B 2 107 ? -7.048  -5.961  -14.642 1.00 55.02  ? 116 PHE   B CE2 1 
ATOM   1108 C  CZ  . PHE   B 2 107 ? -6.407  -5.677  -15.819 1.00 54.76  ? 116 PHE   B CZ  1 
ATOM   1109 N  N   . LYS   B 2 108 ? -5.066  -12.703 -14.375 1.00 55.74  ? 117 LYS   B N   1 
ATOM   1110 C  CA  . LYS   B 2 108 ? -4.950  -13.875 -13.504 1.00 56.63  ? 117 LYS   B CA  1 
ATOM   1111 C  C   . LYS   B 2 108 ? -4.610  -13.342 -12.131 1.00 56.81  ? 117 LYS   B C   1 
ATOM   1112 O  O   . LYS   B 2 108 ? -3.615  -12.641 -12.007 1.00 56.55  ? 117 LYS   B O   1 
ATOM   1113 C  CB  . LYS   B 2 108 ? -3.825  -14.817 -13.977 1.00 59.35  ? 117 LYS   B CB  1 
ATOM   1114 C  CG  . LYS   B 2 108 ? -3.850  -15.146 -15.464 1.00 64.74  ? 117 LYS   B CG  1 
ATOM   1115 C  CD  . LYS   B 2 108 ? -2.598  -15.938 -15.878 1.00 71.18  ? 117 LYS   B CD  1 
ATOM   1116 C  CE  . LYS   B 2 108 ? -1.768  -15.194 -16.915 1.00 76.48  ? 117 LYS   B CE  1 
ATOM   1117 N  NZ  . LYS   B 2 108 ? -0.630  -16.010 -17.447 1.00 79.20  ? 117 LYS   B NZ  1 
ATOM   1118 N  N   . THR   B 2 109 ? -5.436  -13.622 -11.105 1.00 57.57  ? 118 THR   B N   1 
ATOM   1119 C  CA  . THR   B 2 109 ? -5.187  -13.145 -9.733  1.00 58.80  ? 118 THR   B CA  1 
ATOM   1120 C  C   . THR   B 2 109 ? -5.059  -14.327 -8.718  1.00 60.05  ? 118 THR   B C   1 
ATOM   1121 O  O   . THR   B 2 109 ? -5.292  -15.480 -9.082  1.00 60.34  ? 118 THR   B O   1 
ATOM   1122 C  CB  . THR   B 2 109 ? -6.264  -12.096 -9.281  1.00 60.25  ? 118 THR   B CB  1 
ATOM   1123 O  OG1 . THR   B 2 109 ? -7.430  -12.749 -8.777  1.00 61.51  ? 118 THR   B OG1 1 
ATOM   1124 C  CG2 . THR   B 2 109 ? -6.642  -11.096 -10.356 1.00 60.28  ? 118 THR   B CG2 1 
ATOM   1125 N  N   . LYS   B 2 110 ? -4.696  -14.044 -7.451  1.00 60.40  ? 119 LYS   B N   1 
ATOM   1126 C  CA  . LYS   B 2 110 ? -4.607  -15.089 -6.424  1.00 61.55  ? 119 LYS   B CA  1 
ATOM   1127 C  C   . LYS   B 2 110 ? -6.001  -15.654 -6.040  1.00 62.94  ? 119 LYS   B C   1 
ATOM   1128 O  O   . LYS   B 2 110 ? -6.085  -16.735 -5.460  1.00 63.87  ? 119 LYS   B O   1 
ATOM   1129 C  CB  . LYS   B 2 110 ? -3.860  -14.581 -5.176  1.00 62.45  ? 119 LYS   B CB  1 
ATOM   1130 C  CG  . LYS   B 2 110 ? -4.655  -13.592 -4.329  1.00 65.53  ? 119 LYS   B CG  1 
ATOM   1131 C  CD  . LYS   B 2 110 ? -3.793  -12.996 -3.227  1.00 69.39  ? 119 LYS   B CD  1 
ATOM   1132 C  CE  . LYS   B 2 110 ? -4.572  -12.639 -1.980  1.00 72.88  ? 119 LYS   B CE  1 
ATOM   1133 N  NZ  . LYS   B 2 110 ? -5.237  -11.315 -2.087  1.00 75.37  ? 119 LYS   B NZ  1 
ATOM   1134 N  N   . ASP   B 2 111 ? -7.075  -14.926 -6.361  1.00 62.88  ? 120 ASP   B N   1 
ATOM   1135 C  CA  . ASP   B 2 111 ? -8.435  -15.339 -6.079  1.00 63.53  ? 120 ASP   B CA  1 
ATOM   1136 C  C   . ASP   B 2 111 ? -9.223  -15.738 -7.332  1.00 64.55  ? 120 ASP   B C   1 
ATOM   1137 O  O   . ASP   B 2 111 ? -10.440 -15.883 -7.239  1.00 65.55  ? 120 ASP   B O   1 
ATOM   1138 C  CB  . ASP   B 2 111 ? -9.171  -14.214 -5.346  1.00 65.09  ? 120 ASP   B CB  1 
ATOM   1139 C  CG  . ASP   B 2 111 ? -8.604  -13.950 -3.971  1.00 69.11  ? 120 ASP   B CG  1 
ATOM   1140 O  OD1 . ASP   B 2 111 ? -8.336  -14.935 -3.242  1.00 70.42  ? 120 ASP   B OD1 1 
ATOM   1141 O  OD2 . ASP   B 2 111 ? -8.414  -12.762 -3.627  1.00 70.21  ? 120 ASP   B OD2 1 
ATOM   1142 N  N   . GLY   B 2 112 ? -8.557  -15.902 -8.482  1.00 63.79  ? 121 GLY   B N   1 
ATOM   1143 C  CA  . GLY   B 2 112 ? -9.228  -16.303 -9.710  1.00 63.64  ? 121 GLY   B CA  1 
ATOM   1144 C  C   . GLY   B 2 112 ? -8.958  -15.433 -10.921 1.00 63.17  ? 121 GLY   B C   1 
ATOM   1145 O  O   . GLY   B 2 112 ? -8.333  -14.377 -10.810 1.00 63.09  ? 121 GLY   B O   1 
ATOM   1146 N  N   . ASP   B 2 113 ? -9.449  -15.875 -12.091 1.00 62.68  ? 122 ASP   B N   1 
ATOM   1147 C  CA  . ASP   B 2 113 ? -9.295  -15.168 -13.358 1.00 62.43  ? 122 ASP   B CA  1 
ATOM   1148 C  C   . ASP   B 2 113 ? -10.485 -14.234 -13.647 1.00 62.17  ? 122 ASP   B C   1 
ATOM   1149 O  O   . ASP   B 2 113 ? -11.635 -14.572 -13.364 1.00 62.91  ? 122 ASP   B O   1 
ATOM   1150 C  CB  . ASP   B 2 113 ? -9.154  -16.169 -14.514 1.00 64.05  ? 122 ASP   B CB  1 
ATOM   1151 C  CG  . ASP   B 2 113 ? -7.880  -16.995 -14.507 1.00 68.54  ? 122 ASP   B CG  1 
ATOM   1152 O  OD1 . ASP   B 2 113 ? -6.992  -16.710 -13.678 1.00 68.24  ? 122 ASP   B OD1 1 
ATOM   1153 O  OD2 . ASP   B 2 113 ? -7.767  -17.924 -15.347 1.00 71.75  ? 122 ASP   B OD2 1 
ATOM   1154 N  N   . ILE   B 2 114 ? -10.200 -13.064 -14.219 1.00 60.58  ? 123 ILE   B N   1 
ATOM   1155 C  CA  . ILE   B 2 114 ? -11.193 -12.060 -14.588 1.00 59.99  ? 123 ILE   B CA  1 
ATOM   1156 C  C   . ILE   B 2 114 ? -10.933 -11.692 -16.054 1.00 58.67  ? 123 ILE   B C   1 
ATOM   1157 O  O   . ILE   B 2 114 ? -9.778  -11.642 -16.467 1.00 58.45  ? 123 ILE   B O   1 
ATOM   1158 C  CB  . ILE   B 2 114 ? -11.041 -10.790 -13.693 1.00 60.79  ? 123 ILE   B CB  1 
ATOM   1159 C  CG1 . ILE   B 2 114 ? -11.027 -11.127 -12.216 1.00 62.78  ? 123 ILE   B CG1 1 
ATOM   1160 C  CG2 . ILE   B 2 114 ? -12.116 -9.775  -13.966 1.00 61.25  ? 123 ILE   B CG2 1 
ATOM   1161 C  CD1 . ILE   B 2 114 ? -10.449 -10.014 -11.352 1.00 64.74  ? 123 ILE   B CD1 1 
ATOM   1162 N  N   . GLY   B 2 115 ? -11.985 -11.425 -16.822 1.00 57.47  ? 124 GLY   B N   1 
ATOM   1163 C  CA  . GLY   B 2 115 ? -11.818 -10.974 -18.199 1.00 57.07  ? 124 GLY   B CA  1 
ATOM   1164 C  C   . GLY   B 2 115 ? -11.188 -9.593  -18.231 1.00 56.53  ? 124 GLY   B C   1 
ATOM   1165 O  O   . GLY   B 2 115 ? -11.279 -8.850  -17.252 1.00 57.04  ? 124 GLY   B O   1 
ATOM   1166 N  N   . ALA   B 2 116 ? -10.521 -9.238  -19.326 1.00 55.57  ? 125 ALA   B N   1 
ATOM   1167 C  CA  . ALA   B 2 116 ? -9.894  -7.922  -19.441 1.00 55.16  ? 125 ALA   B CA  1 
ATOM   1168 C  C   . ALA   B 2 116 ? -10.001 -7.371  -20.864 1.00 55.24  ? 125 ALA   B C   1 
ATOM   1169 O  O   . ALA   B 2 116 ? -9.829  -8.108  -21.803 1.00 55.35  ? 125 ALA   B O   1 
ATOM   1170 C  CB  . ALA   B 2 116 ? -8.447  -7.986  -18.994 1.00 54.79  ? 125 ALA   B CB  1 
ATOM   1171 N  N   . VAL   B 2 117 ? -10.298 -6.086  -21.018 1.00 55.36  ? 126 VAL   B N   1 
ATOM   1172 C  CA  A VAL   B 2 117 ? -10.411 -5.470  -22.333 0.50 56.13  ? 126 VAL   B CA  1 
ATOM   1173 C  CA  B VAL   B 2 117 ? -10.451 -5.441  -22.310 0.50 55.99  ? 126 VAL   B CA  1 
ATOM   1174 C  C   . VAL   B 2 117 ? -9.246  -4.524  -22.579 1.00 57.06  ? 126 VAL   B C   1 
ATOM   1175 O  O   . VAL   B 2 117 ? -8.935  -3.665  -21.747 1.00 57.37  ? 126 VAL   B O   1 
ATOM   1176 C  CB  A VAL   B 2 117 ? -11.787 -4.833  -22.620 0.50 56.52  ? 126 VAL   B CB  1 
ATOM   1177 C  CB  B VAL   B 2 117 ? -11.827 -4.725  -22.351 0.50 56.11  ? 126 VAL   B CB  1 
ATOM   1178 C  CG1 A VAL   B 2 117 ? -12.835 -5.912  -22.859 0.50 56.84  ? 126 VAL   B CG1 1 
ATOM   1179 C  CG1 B VAL   B 2 117 ? -11.836 -3.513  -23.270 0.50 56.53  ? 126 VAL   B CG1 1 
ATOM   1180 C  CG2 A VAL   B 2 117 ? -12.212 -3.907  -21.494 0.50 57.16  ? 126 VAL   B CG2 1 
ATOM   1181 C  CG2 B VAL   B 2 117 ? -12.930 -5.705  -22.727 0.50 56.36  ? 126 VAL   B CG2 1 
ATOM   1182 N  N   . ALA   B 2 118 ? -8.543  -4.740  -23.703 1.00 57.33  ? 127 ALA   B N   1 
ATOM   1183 C  CA  . ALA   B 2 118 ? -7.381  -3.931  -24.027 1.00 58.84  ? 127 ALA   B CA  1 
ATOM   1184 C  C   . ALA   B 2 118 ? -7.764  -2.873  -25.041 1.00 60.38  ? 127 ALA   B C   1 
ATOM   1185 O  O   . ALA   B 2 118 ? -7.552  -3.032  -26.237 1.00 60.66  ? 127 ALA   B O   1 
ATOM   1186 C  CB  . ALA   B 2 118 ? -6.259  -4.803  -24.562 1.00 59.26  ? 127 ALA   B CB  1 
ATOM   1187 N  N   . LEU   B 2 119 ? -8.393  -1.810  -24.555 1.00 60.72  ? 128 LEU   B N   1 
ATOM   1188 C  CA  . LEU   B 2 119 ? -8.824  -0.684  -25.360 1.00 60.64  ? 128 LEU   B CA  1 
ATOM   1189 C  C   . LEU   B 2 119 ? -8.437  0.571   -24.580 1.00 60.70  ? 128 LEU   B C   1 
ATOM   1190 O  O   . LEU   B 2 119 ? -8.623  0.628   -23.364 1.00 60.59  ? 128 LEU   B O   1 
ATOM   1191 C  CB  . LEU   B 2 119 ? -10.340 -0.741  -25.591 1.00 60.86  ? 128 LEU   B CB  1 
ATOM   1192 C  CG  . LEU   B 2 119 ? -10.864 -1.881  -26.472 1.00 61.85  ? 128 LEU   B CG  1 
ATOM   1193 C  CD1 . LEU   B 2 119 ? -12.382 -1.856  -26.540 1.00 61.92  ? 128 LEU   B CD1 1 
ATOM   1194 C  CD2 . LEU   B 2 119 ? -10.282 -1.814  -27.890 1.00 62.41  ? 128 LEU   B CD2 1 
ATOM   1195 N  N   . ASP   B 2 120 ? -7.853  1.557   -25.263 1.00 60.93  ? 129 ASP   B N   1 
ATOM   1196 C  CA  . ASP   B 2 120 ? -7.402  2.778   -24.601 1.00 61.30  ? 129 ASP   B CA  1 
ATOM   1197 C  C   . ASP   B 2 120 ? -8.393  3.905   -24.752 1.00 59.90  ? 129 ASP   B C   1 
ATOM   1198 O  O   . ASP   B 2 120 ? -8.708  4.258   -25.880 1.00 60.17  ? 129 ASP   B O   1 
ATOM   1199 C  CB  . ASP   B 2 120 ? -6.059  3.212   -25.178 1.00 64.62  ? 129 ASP   B CB  1 
ATOM   1200 C  CG  . ASP   B 2 120 ? -4.958  3.127   -24.152 1.00 73.08  ? 129 ASP   B CG  1 
ATOM   1201 O  OD1 . ASP   B 2 120 ? -4.896  4.022   -23.269 1.00 75.38  ? 129 ASP   B OD1 1 
ATOM   1202 O  OD2 . ASP   B 2 120 ? -4.173  2.147   -24.203 1.00 75.15  ? 129 ASP   B OD2 1 
ATOM   1203 N  N   . TYR   B 2 121 ? -8.830  4.519   -23.640 1.00 58.07  ? 130 TYR   B N   1 
ATOM   1204 C  CA  . TYR   B 2 121 ? -9.793  5.626   -23.662 1.00 57.06  ? 130 TYR   B CA  1 
ATOM   1205 C  C   . TYR   B 2 121 ? -9.503  6.667   -22.558 1.00 55.62  ? 130 TYR   B C   1 
ATOM   1206 O  O   . TYR   B 2 121 ? -8.869  6.331   -21.553 1.00 55.49  ? 130 TYR   B O   1 
ATOM   1207 C  CB  . TYR   B 2 121 ? -11.228 5.078   -23.506 1.00 57.61  ? 130 TYR   B CB  1 
ATOM   1208 C  CG  . TYR   B 2 121 ? -11.826 4.638   -24.818 1.00 59.18  ? 130 TYR   B CG  1 
ATOM   1209 C  CD1 . TYR   B 2 121 ? -12.338 5.564   -25.714 1.00 60.50  ? 130 TYR   B CD1 1 
ATOM   1210 C  CD2 . TYR   B 2 121 ? -11.813 3.304   -25.198 1.00 60.45  ? 130 TYR   B CD2 1 
ATOM   1211 C  CE1 . TYR   B 2 121 ? -12.813 5.175   -26.958 1.00 61.86  ? 130 TYR   B CE1 1 
ATOM   1212 C  CE2 . TYR   B 2 121 ? -12.288 2.902   -26.440 1.00 61.66  ? 130 TYR   B CE2 1 
ATOM   1213 C  CZ  . TYR   B 2 121 ? -12.782 3.843   -27.320 1.00 63.02  ? 130 TYR   B CZ  1 
ATOM   1214 O  OH  . TYR   B 2 121 ? -13.278 3.463   -28.538 1.00 65.62  ? 130 TYR   B OH  1 
ATOM   1215 N  N   . PRO   B 2 122 ? -10.000 7.921   -22.691 1.00 54.18  ? 131 PRO   B N   1 
ATOM   1216 C  CA  . PRO   B 2 122 ? -9.763  8.916   -21.624 1.00 53.09  ? 131 PRO   B CA  1 
ATOM   1217 C  C   . PRO   B 2 122 ? -10.380 8.505   -20.277 1.00 51.74  ? 131 PRO   B C   1 
ATOM   1218 O  O   . PRO   B 2 122 ? -11.349 7.752   -20.260 1.00 51.68  ? 131 PRO   B O   1 
ATOM   1219 C  CB  . PRO   B 2 122 ? -10.400 10.200  -22.180 1.00 53.85  ? 131 PRO   B CB  1 
ATOM   1220 C  CG  . PRO   B 2 122 ? -10.458 9.979   -23.700 1.00 54.47  ? 131 PRO   B CG  1 
ATOM   1221 C  CD  . PRO   B 2 122 ? -10.738 8.510   -23.832 1.00 53.29  ? 131 PRO   B CD  1 
ATOM   1222 N  N   . ALA   B 2 123 ? -9.815  8.981   -19.153 1.00 50.37  ? 132 ALA   B N   1 
ATOM   1223 C  CA  . ALA   B 2 123 ? -10.286 8.635   -17.803 1.00 49.60  ? 132 ALA   B CA  1 
ATOM   1224 C  C   . ALA   B 2 123 ? -11.787 8.863   -17.578 1.00 49.12  ? 132 ALA   B C   1 
ATOM   1225 O  O   . ALA   B 2 123 ? -12.415 8.110   -16.836 1.00 48.81  ? 132 ALA   B O   1 
ATOM   1226 C  CB  . ALA   B 2 123 ? -9.465  9.357   -16.748 1.00 49.30  ? 132 ALA   B CB  1 
ATOM   1227 N  N   . GLY   B 2 124 ? -12.357 9.840   -18.284 1.00 48.49  ? 133 GLY   B N   1 
ATOM   1228 C  CA  . GLY   B 2 124 ? -13.785 10.125  -18.223 1.00 47.61  ? 133 GLY   B CA  1 
ATOM   1229 C  C   . GLY   B 2 124 ? -14.657 9.063   -18.863 1.00 46.49  ? 133 GLY   B C   1 
ATOM   1230 O  O   . GLY   B 2 124 ? -15.876 9.141   -18.769 1.00 46.53  ? 133 GLY   B O   1 
ATOM   1231 N  N   . THR   B 2 125 ? -14.059 8.077   -19.554 1.00 45.90  ? 134 THR   B N   1 
ATOM   1232 C  CA  . THR   B 2 125 ? -14.799 6.964   -20.146 1.00 45.84  ? 134 THR   B CA  1 
ATOM   1233 C  C   . THR   B 2 125 ? -15.112 5.886   -19.060 1.00 44.59  ? 134 THR   B C   1 
ATOM   1234 O  O   . THR   B 2 125 ? -15.919 5.006   -19.326 1.00 44.90  ? 134 THR   B O   1 
ATOM   1235 C  CB  . THR   B 2 125 ? -14.078 6.419   -21.435 1.00 48.13  ? 134 THR   B CB  1 
ATOM   1236 O  OG1 . THR   B 2 125 ? -13.760 7.491   -22.323 1.00 49.30  ? 134 THR   B OG1 1 
ATOM   1237 C  CG2 . THR   B 2 125 ? -14.908 5.425   -22.224 1.00 48.36  ? 134 THR   B CG2 1 
ATOM   1238 N  N   . SER   B 2 126 ? -14.500 5.968   -17.834 1.00 43.42  ? 135 SER   B N   1 
ATOM   1239 C  CA  . SER   B 2 126 ? -14.693 5.045   -16.707 1.00 42.77  ? 135 SER   B CA  1 
ATOM   1240 C  C   . SER   B 2 126 ? -16.167 4.807   -16.379 1.00 40.60  ? 135 SER   B C   1 
ATOM   1241 O  O   . SER   B 2 126 ? -16.878 5.760   -16.084 1.00 40.14  ? 135 SER   B O   1 
ATOM   1242 C  CB  . SER   B 2 126 ? -14.037 5.607   -15.449 1.00 46.02  ? 135 SER   B CB  1 
ATOM   1243 O  OG  . SER   B 2 126 ? -12.635 5.400   -15.406 1.00 50.55  ? 135 SER   B OG  1 
ATOM   1244 N  N   . GLY   B 2 127 ? -16.601 3.552   -16.397 1.00 38.60  ? 136 GLY   B N   1 
ATOM   1245 C  CA  . GLY   B 2 127 ? -17.985 3.199   -16.125 1.00 38.37  ? 136 GLY   B CA  1 
ATOM   1246 C  C   . GLY   B 2 127 ? -18.761 2.755   -17.353 1.00 38.60  ? 136 GLY   B C   1 
ATOM   1247 O  O   . GLY   B 2 127 ? -19.916 2.334   -17.233 1.00 38.90  ? 136 GLY   B O   1 
ATOM   1248 N  N   . SER   B 2 128 ? -18.159 2.884   -18.559 1.00 37.89  ? 137 SER   B N   1 
ATOM   1249 C  CA  . SER   B 2 128 ? -18.785 2.461   -19.801 1.00 37.65  ? 137 SER   B CA  1 
ATOM   1250 C  C   . SER   B 2 128 ? -19.029 0.940   -19.753 1.00 38.42  ? 137 SER   B C   1 
ATOM   1251 O  O   . SER   B 2 128 ? -18.153 0.177   -19.343 1.00 38.08  ? 137 SER   B O   1 
ATOM   1252 C  CB  . SER   B 2 128 ? -17.924 2.856   -21.005 1.00 38.08  ? 137 SER   B CB  1 
ATOM   1253 O  OG  . SER   B 2 128 ? -17.952 4.255   -21.256 1.00 37.69  ? 137 SER   B OG  1 
ATOM   1254 N  N   . PRO   B 2 129 ? -20.242 0.496   -20.110 1.00 39.15  ? 138 PRO   B N   1 
ATOM   1255 C  CA  . PRO   B 2 129 ? -20.546 -0.943  -20.041 1.00 39.46  ? 138 PRO   B CA  1 
ATOM   1256 C  C   . PRO   B 2 129 ? -19.912 -1.833  -21.104 1.00 41.15  ? 138 PRO   B C   1 
ATOM   1257 O  O   . PRO   B 2 129 ? -19.669 -1.428  -22.248 1.00 40.90  ? 138 PRO   B O   1 
ATOM   1258 C  CB  . PRO   B 2 129 ? -22.066 -0.990  -20.189 1.00 39.75  ? 138 PRO   B CB  1 
ATOM   1259 C  CG  . PRO   B 2 129 ? -22.414 0.268   -20.971 1.00 40.40  ? 138 PRO   B CG  1 
ATOM   1260 C  CD  . PRO   B 2 129 ? -21.407 1.294   -20.557 1.00 38.86  ? 138 PRO   B CD  1 
ATOM   1261 N  N   . ILE   B 2 130 ? -19.696 -3.088  -20.715 1.00 41.80  ? 139 ILE   B N   1 
ATOM   1262 C  CA  . ILE   B 2 130 ? -19.197 -4.125  -21.598 1.00 43.09  ? 139 ILE   B CA  1 
ATOM   1263 C  C   . ILE   B 2 130 ? -20.373 -5.092  -21.792 1.00 44.71  ? 139 ILE   B C   1 
ATOM   1264 O  O   . ILE   B 2 130 ? -21.007 -5.488  -20.814 1.00 44.48  ? 139 ILE   B O   1 
ATOM   1265 C  CB  . ILE   B 2 130 ? -17.945 -4.795  -21.013 1.00 43.06  ? 139 ILE   B CB  1 
ATOM   1266 C  CG1 . ILE   B 2 130 ? -16.813 -3.767  -20.877 1.00 43.87  ? 139 ILE   B CG1 1 
ATOM   1267 C  CG2 . ILE   B 2 130 ? -17.517 -6.000  -21.863 1.00 43.39  ? 139 ILE   B CG2 1 
ATOM   1268 C  CD1 . ILE   B 2 130 ? -15.763 -4.173  -19.886 1.00 45.11  ? 139 ILE   B CD1 1 
ATOM   1269 N  N   . LEU   B 2 131 ? -20.707 -5.407  -23.060 1.00 45.70  ? 140 LEU   B N   1 
ATOM   1270 C  CA  . LEU   B 2 131 ? -21.867 -6.208  -23.420 1.00 47.04  ? 140 LEU   B CA  1 
ATOM   1271 C  C   . LEU   B 2 131 ? -21.554 -7.562  -24.036 1.00 48.89  ? 140 LEU   B C   1 
ATOM   1272 O  O   . LEU   B 2 131 ? -20.569 -7.708  -24.753 1.00 48.96  ? 140 LEU   B O   1 
ATOM   1273 C  CB  . LEU   B 2 131 ? -22.682 -5.448  -24.477 1.00 47.30  ? 140 LEU   B CB  1 
ATOM   1274 C  CG  . LEU   B 2 131 ? -22.875 -3.943  -24.346 1.00 48.66  ? 140 LEU   B CG  1 
ATOM   1275 C  CD1 . LEU   B 2 131 ? -23.773 -3.433  -25.450 1.00 49.01  ? 140 LEU   B CD1 1 
ATOM   1276 C  CD2 . LEU   B 2 131 ? -23.432 -3.577  -22.990 1.00 48.99  ? 140 LEU   B CD2 1 
ATOM   1277 N  N   . ASP   B 2 132 ? -22.474 -8.522  -23.867 1.00 50.02  ? 141 ASP   B N   1 
ATOM   1278 C  CA  . ASP   B 2 132 ? -22.383 -9.795  -24.570 1.00 51.54  ? 141 ASP   B CA  1 
ATOM   1279 C  C   . ASP   B 2 132 ? -23.270 -9.710  -25.859 1.00 53.81  ? 141 ASP   B C   1 
ATOM   1280 O  O   . ASP   B 2 132 ? -23.919 -8.677  -26.088 1.00 53.74  ? 141 ASP   B O   1 
ATOM   1281 C  CB  . ASP   B 2 132 ? -22.744 -10.980 -23.662 1.00 51.74  ? 141 ASP   B CB  1 
ATOM   1282 C  CG  . ASP   B 2 132 ? -24.114 -10.944 -23.038 1.00 53.63  ? 141 ASP   B CG  1 
ATOM   1283 O  OD1 . ASP   B 2 132 ? -25.010 -10.313 -23.615 1.00 53.16  ? 141 ASP   B OD1 1 
ATOM   1284 O  OD2 . ASP   B 2 132 ? -24.291 -11.559 -21.973 1.00 56.44  ? 141 ASP   B OD2 1 
ATOM   1285 N  N   . LYS   B 2 133 ? -23.319 -10.774 -26.683 1.00 55.24  ? 142 LYS   B N   1 
ATOM   1286 C  CA  . LYS   B 2 133 ? -24.089 -10.739 -27.933 1.00 56.88  ? 142 LYS   B CA  1 
ATOM   1287 C  C   . LYS   B 2 133 ? -25.595 -10.465 -27.730 1.00 56.89  ? 142 LYS   B C   1 
ATOM   1288 O  O   . LYS   B 2 133 ? -26.269 -10.009 -28.668 1.00 56.81  ? 142 LYS   B O   1 
ATOM   1289 C  CB  . LYS   B 2 133 ? -23.851 -12.003 -28.774 1.00 60.71  ? 142 LYS   B CB  1 
ATOM   1290 C  CG  . LYS   B 2 133 ? -22.418 -12.121 -29.305 1.00 67.79  ? 142 LYS   B CG  1 
ATOM   1291 C  CD  . LYS   B 2 133 ? -21.714 -13.431 -28.854 1.00 74.19  ? 142 LYS   B CD  1 
ATOM   1292 C  CE  . LYS   B 2 133 ? -20.707 -13.926 -29.871 1.00 78.51  ? 142 LYS   B CE  1 
ATOM   1293 N  NZ  . LYS   B 2 133 ? -20.472 -15.394 -29.759 1.00 81.19  ? 142 LYS   B NZ  1 
ATOM   1294 N  N   . CYS   B 2 134 ? -26.109 -10.682 -26.503 1.00 56.47  ? 143 CYS   B N   1 
ATOM   1295 C  CA  . CYS   B 2 134 ? -27.517 -10.380 -26.210 1.00 56.78  ? 143 CYS   B CA  1 
ATOM   1296 C  C   . CYS   B 2 134 ? -27.756 -8.958  -25.705 1.00 55.93  ? 143 CYS   B C   1 
ATOM   1297 O  O   . CYS   B 2 134 ? -28.879 -8.647  -25.332 1.00 56.31  ? 143 CYS   B O   1 
ATOM   1298 C  CB  . CYS   B 2 134 ? -28.102 -11.392 -25.235 1.00 58.75  ? 143 CYS   B CB  1 
ATOM   1299 S  SG  . CYS   B 2 134 ? -28.045 -13.100 -25.819 1.00 65.24  ? 143 CYS   B SG  1 
ATOM   1300 N  N   . GLY   B 2 135 ? -26.721 -8.131  -25.635 1.00 54.72  ? 144 GLY   B N   1 
ATOM   1301 C  CA  . GLY   B 2 135 ? -26.851 -6.782  -25.104 1.00 54.02  ? 144 GLY   B CA  1 
ATOM   1302 C  C   . GLY   B 2 135 ? -26.855 -6.713  -23.586 1.00 52.96  ? 144 GLY   B C   1 
ATOM   1303 O  O   . GLY   B 2 135 ? -27.086 -5.639  -23.021 1.00 53.15  ? 144 GLY   B O   1 
ATOM   1304 N  N   . ARG   B 2 136 ? -26.611 -7.849  -22.903 1.00 51.63  ? 145 ARG   B N   1 
ATOM   1305 C  CA  . ARG   B 2 136 ? -26.562 -7.890  -21.441 1.00 50.78  ? 145 ARG   B CA  1 
ATOM   1306 C  C   . ARG   B 2 136 ? -25.253 -7.299  -20.942 1.00 49.10  ? 145 ARG   B C   1 
ATOM   1307 O  O   . ARG   B 2 136 ? -24.207 -7.546  -21.526 1.00 48.75  ? 145 ARG   B O   1 
ATOM   1308 C  CB  . ARG   B 2 136 ? -26.713 -9.327  -20.926 1.00 52.60  ? 145 ARG   B CB  1 
ATOM   1309 C  CG  . ARG   B 2 136 ? -28.159 -9.816  -20.883 1.00 56.18  ? 145 ARG   B CG  1 
ATOM   1310 C  CD  . ARG   B 2 136 ? -28.224 -11.280 -20.524 1.00 59.61  ? 145 ARG   B CD  1 
ATOM   1311 N  NE  . ARG   B 2 136 ? -27.526 -12.068 -21.530 1.00 64.15  ? 145 ARG   B NE  1 
ATOM   1312 C  CZ  . ARG   B 2 136 ? -26.848 -13.184 -21.290 1.00 66.82  ? 145 ARG   B CZ  1 
ATOM   1313 N  NH1 . ARG   B 2 136 ? -26.782 -13.678 -20.057 1.00 66.43  ? 145 ARG   B NH1 1 
ATOM   1314 N  NH2 . ARG   B 2 136 ? -26.228 -13.814 -22.280 1.00 67.70  ? 145 ARG   B NH2 1 
ATOM   1315 N  N   . VAL   B 2 137 ? -25.307 -6.522  -19.860 1.00 48.11  ? 146 VAL   B N   1 
ATOM   1316 C  CA  . VAL   B 2 137 ? -24.123 -5.881  -19.308 1.00 46.97  ? 146 VAL   B CA  1 
ATOM   1317 C  C   . VAL   B 2 137 ? -23.343 -6.887  -18.470 1.00 46.23  ? 146 VAL   B C   1 
ATOM   1318 O  O   . VAL   B 2 137 ? -23.807 -7.300  -17.412 1.00 46.79  ? 146 VAL   B O   1 
ATOM   1319 C  CB  . VAL   B 2 137 ? -24.514 -4.623  -18.505 1.00 47.21  ? 146 VAL   B CB  1 
ATOM   1320 C  CG1 . VAL   B 2 137 ? -23.280 -3.888  -17.997 1.00 47.84  ? 146 VAL   B CG1 1 
ATOM   1321 C  CG2 . VAL   B 2 137 ? -25.396 -3.693  -19.337 1.00 47.35  ? 146 VAL   B CG2 1 
ATOM   1322 N  N   . ILE   B 2 138 ? -22.186 -7.323  -18.970 1.00 44.71  ? 147 ILE   B N   1 
ATOM   1323 C  CA  . ILE   B 2 138 ? -21.334 -8.303  -18.286 1.00 43.57  ? 147 ILE   B CA  1 
ATOM   1324 C  C   . ILE   B 2 138 ? -20.270 -7.662  -17.365 1.00 42.21  ? 147 ILE   B C   1 
ATOM   1325 O  O   . ILE   B 2 138 ? -19.543 -8.380  -16.672 1.00 42.19  ? 147 ILE   B O   1 
ATOM   1326 C  CB  . ILE   B 2 138 ? -20.694 -9.284  -19.315 1.00 43.82  ? 147 ILE   B CB  1 
ATOM   1327 C  CG1 . ILE   B 2 138 ? -19.807 -8.519  -20.313 1.00 44.82  ? 147 ILE   B CG1 1 
ATOM   1328 C  CG2 . ILE   B 2 138 ? -21.778 -10.073 -20.046 1.00 44.14  ? 147 ILE   B CG2 1 
ATOM   1329 C  CD1 . ILE   B 2 138 ? -19.049 -9.384  -21.299 1.00 45.99  ? 147 ILE   B CD1 1 
ATOM   1330 N  N   . GLY   B 2 139 ? -20.221 -6.336  -17.313 1.00 41.01  ? 148 GLY   B N   1 
ATOM   1331 C  CA  . GLY   B 2 139 ? -19.280 -5.634  -16.445 1.00 40.90  ? 148 GLY   B CA  1 
ATOM   1332 C  C   . GLY   B 2 139 ? -19.029 -4.204  -16.882 1.00 39.86  ? 148 GLY   B C   1 
ATOM   1333 O  O   . GLY   B 2 139 ? -19.542 -3.781  -17.916 1.00 39.26  ? 148 GLY   B O   1 
ATOM   1334 N  N   . LEU   B 2 140 ? -18.253 -3.446  -16.105 1.00 39.16  ? 149 LEU   B N   1 
ATOM   1335 C  CA  . LEU   B 2 140 ? -17.933 -2.064  -16.475 1.00 39.21  ? 149 LEU   B CA  1 
ATOM   1336 C  C   . LEU   B 2 140 ? -16.435 -1.919  -16.708 1.00 39.94  ? 149 LEU   B C   1 
ATOM   1337 O  O   . LEU   B 2 140 ? -15.608 -2.569  -16.058 1.00 39.88  ? 149 LEU   B O   1 
ATOM   1338 C  CB  . LEU   B 2 140 ? -18.371 -1.039  -15.425 1.00 38.76  ? 149 LEU   B CB  1 
ATOM   1339 C  CG  . LEU   B 2 140 ? -19.814 -1.049  -14.945 1.00 39.85  ? 149 LEU   B CG  1 
ATOM   1340 C  CD1 . LEU   B 2 140 ? -20.040 0.063   -13.882 1.00 39.84  ? 149 LEU   B CD1 1 
ATOM   1341 C  CD2 . LEU   B 2 140 ? -20.788 -0.925  -16.085 1.00 40.08  ? 149 LEU   B CD2 1 
ATOM   1342 N  N   . TYR   B 2 141 ? -16.104 -1.033  -17.639 1.00 39.92  ? 150 TYR   B N   1 
ATOM   1343 C  CA  . TYR   B 2 141 ? -14.756 -0.708  -18.068 1.00 39.71  ? 150 TYR   B CA  1 
ATOM   1344 C  C   . TYR   B 2 141 ? -14.264 0.507   -17.282 1.00 39.48  ? 150 TYR   B C   1 
ATOM   1345 O  O   . TYR   B 2 141 ? -15.031 1.451   -17.114 1.00 39.03  ? 150 TYR   B O   1 
ATOM   1346 C  CB  . TYR   B 2 141 ? -14.824 -0.397  -19.584 1.00 39.55  ? 150 TYR   B CB  1 
ATOM   1347 C  CG  . TYR   B 2 141 ? -13.617 0.307   -20.166 1.00 40.49  ? 150 TYR   B CG  1 
ATOM   1348 C  CD1 . TYR   B 2 141 ? -13.563 1.692   -20.239 1.00 41.38  ? 150 TYR   B CD1 1 
ATOM   1349 C  CD2 . TYR   B 2 141 ? -12.535 -0.414  -20.656 1.00 41.98  ? 150 TYR   B CD2 1 
ATOM   1350 C  CE1 . TYR   B 2 141 ? -12.450 2.345   -20.766 1.00 43.02  ? 150 TYR   B CE1 1 
ATOM   1351 C  CE2 . TYR   B 2 141 ? -11.446 0.225   -21.248 1.00 43.19  ? 150 TYR   B CE2 1 
ATOM   1352 C  CZ  . TYR   B 2 141 ? -11.403 1.608   -21.298 1.00 44.05  ? 150 TYR   B CZ  1 
ATOM   1353 O  OH  . TYR   B 2 141 ? -10.314 2.254   -21.851 1.00 45.03  ? 150 TYR   B OH  1 
ATOM   1354 N  N   . GLY   B 2 142 ? -13.003 0.511   -16.859 1.00 39.86  ? 151 GLY   B N   1 
ATOM   1355 C  CA  . GLY   B 2 142 ? -12.468 1.674   -16.155 1.00 41.76  ? 151 GLY   B CA  1 
ATOM   1356 C  C   . GLY   B 2 142 ? -11.590 1.430   -14.947 1.00 43.06  ? 151 GLY   B C   1 
ATOM   1357 O  O   . GLY   B 2 142 ? -11.148 2.393   -14.308 1.00 43.72  ? 151 GLY   B O   1 
ATOM   1358 N  N   . ASN   B 2 143 ? -11.331 0.164   -14.612 1.00 43.12  ? 152 ASN   B N   1 
ATOM   1359 C  CA  . ASN   B 2 143 ? -10.396 -0.154  -13.529 1.00 44.39  ? 152 ASN   B CA  1 
ATOM   1360 C  C   . ASN   B 2 143 ? -9.400  -1.169  -14.055 1.00 46.07  ? 152 ASN   B C   1 
ATOM   1361 O  O   . ASN   B 2 143 ? -9.758  -2.318  -14.310 1.00 46.16  ? 152 ASN   B O   1 
ATOM   1362 C  CB  . ASN   B 2 143 ? -11.074 -0.666  -12.254 1.00 44.90  ? 152 ASN   B CB  1 
ATOM   1363 C  CG  . ASN   B 2 143 ? -10.144 -0.656  -11.052 1.00 46.71  ? 152 ASN   B CG  1 
ATOM   1364 O  OD1 . ASN   B 2 143 ? -9.079  -0.026  -11.062 1.00 48.15  ? 152 ASN   B OD1 1 
ATOM   1365 N  ND2 . ASN   B 2 143 ? -10.520 -1.344  -9.985  1.00 45.38  ? 152 ASN   B ND2 1 
ATOM   1366 N  N   . GLY   B 2 144 ? -8.167  -0.730  -14.239 1.00 47.35  ? 153 GLY   B N   1 
ATOM   1367 C  CA  . GLY   B 2 144 ? -7.152  -1.605  -14.785 1.00 49.98  ? 153 GLY   B CA  1 
ATOM   1368 C  C   . GLY   B 2 144 ? -5.727  -1.214  -14.518 1.00 52.88  ? 153 GLY   B C   1 
ATOM   1369 O  O   . GLY   B 2 144 ? -5.383  -0.734  -13.434 1.00 52.93  ? 153 GLY   B O   1 
ATOM   1370 N  N   . VAL   B 2 145 ? -4.877  -1.475  -15.508 1.00 55.22  ? 154 VAL   B N   1 
ATOM   1371 C  CA  . VAL   B 2 145 ? -3.444  -1.304  -15.348 1.00 57.92  ? 154 VAL   B CA  1 
ATOM   1372 C  C   . VAL   B 2 145 ? -2.743  -0.846  -16.640 1.00 60.55  ? 154 VAL   B C   1 
ATOM   1373 O  O   . VAL   B 2 145 ? -3.343  -0.853  -17.712 1.00 60.42  ? 154 VAL   B O   1 
ATOM   1374 C  CB  . VAL   B 2 145 ? -2.887  -2.652  -14.809 1.00 58.63  ? 154 VAL   B CB  1 
ATOM   1375 C  CG1 . VAL   B 2 145 ? -2.667  -3.659  -15.936 1.00 58.85  ? 154 VAL   B CG1 1 
ATOM   1376 C  CG2 . VAL   B 2 145 ? -1.629  -2.445  -13.979 1.00 59.54  ? 154 VAL   B CG2 1 
ATOM   1377 N  N   . VAL   B 2 146 ? -1.490  -0.387  -16.519 1.00 62.92  ? 155 VAL   B N   1 
ATOM   1378 C  CA  . VAL   B 2 146 ? -0.702  0.033   -17.670 1.00 65.72  ? 155 VAL   B CA  1 
ATOM   1379 C  C   . VAL   B 2 146 ? 0.393   -1.011  -17.896 1.00 68.17  ? 155 VAL   B C   1 
ATOM   1380 O  O   . VAL   B 2 146 ? 1.158   -1.298  -16.979 1.00 68.38  ? 155 VAL   B O   1 
ATOM   1381 C  CB  . VAL   B 2 146 ? -0.160  1.475   -17.533 1.00 66.85  ? 155 VAL   B CB  1 
ATOM   1382 C  CG1 . VAL   B 2 146 ? 0.989   1.730   -18.503 1.00 67.57  ? 155 VAL   B CG1 1 
ATOM   1383 C  CG2 . VAL   B 2 146 ? -1.270  2.483   -17.772 1.00 67.31  ? 155 VAL   B CG2 1 
ATOM   1384 N  N   . ILE   B 2 147 ? 0.425   -1.624  -19.091 1.00 69.80  ? 156 ILE   B N   1 
ATOM   1385 C  CA  . ILE   B 2 147 ? 1.399   -2.671  -19.366 1.00 72.08  ? 156 ILE   B CA  1 
ATOM   1386 C  C   . ILE   B 2 147 ? 2.751   -2.086  -19.812 1.00 74.02  ? 156 ILE   B C   1 
ATOM   1387 O  O   . ILE   B 2 147 ? 2.833   -0.892  -20.072 1.00 74.24  ? 156 ILE   B O   1 
ATOM   1388 C  CB  . ILE   B 2 147 ? 0.823   -3.738  -20.325 1.00 72.95  ? 156 ILE   B CB  1 
ATOM   1389 C  CG1 . ILE   B 2 147 ? 0.246   -3.126  -21.603 1.00 73.67  ? 156 ILE   B CG1 1 
ATOM   1390 C  CG2 . ILE   B 2 147 ? -0.219  -4.577  -19.584 1.00 73.69  ? 156 ILE   B CG2 1 
ATOM   1391 C  CD1 . ILE   B 2 147 ? -0.292  -4.166  -22.583 1.00 74.79  ? 156 ILE   B CD1 1 
ATOM   1392 N  N   . LYS   B 2 148 ? 3.822   -2.908  -19.844 1.00 75.21  ? 157 LYS   B N   1 
ATOM   1393 C  CA  . LYS   B 2 148 ? 5.178   -2.444  -20.166 1.00 76.90  ? 157 LYS   B CA  1 
ATOM   1394 C  C   . LYS   B 2 148 ? 5.314   -1.605  -21.463 1.00 77.80  ? 157 LYS   B C   1 
ATOM   1395 O  O   . LYS   B 2 148 ? 6.287   -0.857  -21.583 1.00 78.40  ? 157 LYS   B O   1 
ATOM   1396 C  CB  . LYS   B 2 148 ? 6.183   -3.603  -20.171 1.00 79.76  ? 157 LYS   B CB  1 
ATOM   1397 C  CG  . LYS   B 2 148 ? 5.838   -4.743  -21.109 1.00 85.49  ? 157 LYS   B CG  1 
ATOM   1398 C  CD  . LYS   B 2 148 ? 6.288   -6.082  -20.521 1.00 91.11  ? 157 LYS   B CD  1 
ATOM   1399 C  CE  . LYS   B 2 148 ? 7.787   -6.222  -20.408 1.00 95.66  ? 157 LYS   B CE  1 
ATOM   1400 N  NZ  . LYS   B 2 148 ? 8.391   -6.773  -21.652 1.00 98.41  ? 157 LYS   B NZ  1 
ATOM   1401 N  N   . ASN   B 2 149 ? 4.355   -1.692  -22.404 1.00 77.51  ? 158 ASN   B N   1 
ATOM   1402 C  CA  . ASN   B 2 149 ? 4.409   -0.863  -23.608 1.00 77.56  ? 158 ASN   B CA  1 
ATOM   1403 C  C   . ASN   B 2 149 ? 3.586   0.455   -23.490 1.00 76.83  ? 158 ASN   B C   1 
ATOM   1404 O  O   . ASN   B 2 149 ? 3.387   1.151   -24.488 1.00 77.15  ? 158 ASN   B O   1 
ATOM   1405 C  CB  . ASN   B 2 149 ? 4.039   -1.663  -24.871 1.00 79.49  ? 158 ASN   B CB  1 
ATOM   1406 C  CG  . ASN   B 2 149 ? 2.565   -1.894  -25.114 1.00 83.02  ? 158 ASN   B CG  1 
ATOM   1407 O  OD1 . ASN   B 2 149 ? 2.003   -2.918  -24.726 1.00 83.81  ? 158 ASN   B OD1 1 
ATOM   1408 N  ND2 . ASN   B 2 149 ? 1.921   -0.968  -25.818 1.00 84.13  ? 158 ASN   B ND2 1 
ATOM   1409 N  N   . GLY   B 2 150 ? 3.138   0.788   -22.283 1.00 75.67  ? 159 GLY   B N   1 
ATOM   1410 C  CA  . GLY   B 2 150 ? 2.389   2.006   -22.006 1.00 74.88  ? 159 GLY   B CA  1 
ATOM   1411 C  C   . GLY   B 2 150 ? 0.891   1.963   -22.235 1.00 73.57  ? 159 GLY   B C   1 
ATOM   1412 O  O   . GLY   B 2 150 ? 0.181   2.871   -21.779 1.00 74.10  ? 159 GLY   B O   1 
ATOM   1413 N  N   . SER   B 2 151 ? 0.381   0.922   -22.934 1.00 71.41  ? 160 SER   B N   1 
ATOM   1414 C  CA  A SER   B 2 151 ? -1.053  0.798   -23.218 0.50 70.71  ? 160 SER   B CA  1 
ATOM   1415 C  CA  B SER   B 2 151 ? -1.058  0.847   -23.207 0.50 70.73  ? 160 SER   B CA  1 
ATOM   1416 C  C   . SER   B 2 151 ? -1.890  0.474   -21.958 1.00 69.40  ? 160 SER   B C   1 
ATOM   1417 O  O   . SER   B 2 151 ? -1.341  0.045   -20.941 1.00 69.65  ? 160 SER   B O   1 
ATOM   1418 C  CB  A SER   B 2 151 ? -1.286  -0.244  -24.309 0.50 72.09  ? 160 SER   B CB  1 
ATOM   1419 C  CB  B SER   B 2 151 ? -1.351  -0.069  -24.396 0.50 72.20  ? 160 SER   B CB  1 
ATOM   1420 O  OG  A SER   B 2 151 ? -2.442  0.051   -25.074 0.50 74.28  ? 160 SER   B OG  1 
ATOM   1421 O  OG  B SER   B 2 151 ? -1.522  -1.429  -24.031 0.50 74.62  ? 160 SER   B OG  1 
ATOM   1422 N  N   . TYR   B 2 152 ? -3.219  0.682   -22.025 1.00 66.34  ? 161 TYR   B N   1 
ATOM   1423 C  CA  . TYR   B 2 152 ? -4.156  0.446   -20.935 1.00 63.61  ? 161 TYR   B CA  1 
ATOM   1424 C  C   . TYR   B 2 152 ? -4.999  -0.828  -21.090 1.00 61.02  ? 161 TYR   B C   1 
ATOM   1425 O  O   . TYR   B 2 152 ? -5.647  -1.025  -22.108 1.00 61.22  ? 161 TYR   B O   1 
ATOM   1426 C  CB  . TYR   B 2 152 ? -5.079  1.676   -20.794 1.00 63.16  ? 161 TYR   B CB  1 
ATOM   1427 C  CG  . TYR   B 2 152 ? -6.103  1.562   -19.689 1.00 62.97  ? 161 TYR   B CG  1 
ATOM   1428 C  CD1 . TYR   B 2 152 ? -5.721  1.582   -18.357 1.00 63.49  ? 161 TYR   B CD1 1 
ATOM   1429 C  CD2 . TYR   B 2 152 ? -7.456  1.464   -19.977 1.00 63.20  ? 161 TYR   B CD2 1 
ATOM   1430 C  CE1 . TYR   B 2 152 ? -6.657  1.471   -17.339 1.00 63.94  ? 161 TYR   B CE1 1 
ATOM   1431 C  CE2 . TYR   B 2 152 ? -8.399  1.350   -18.969 1.00 63.48  ? 161 TYR   B CE2 1 
ATOM   1432 C  CZ  . TYR   B 2 152 ? -7.994  1.353   -17.649 1.00 64.33  ? 161 TYR   B CZ  1 
ATOM   1433 O  OH  . TYR   B 2 152 ? -8.916  1.239   -16.643 1.00 65.15  ? 161 TYR   B OH  1 
ATOM   1434 N  N   . VAL   B 2 153 ? -5.019  -1.675  -20.059 1.00 58.50  ? 162 VAL   B N   1 
ATOM   1435 C  CA  . VAL   B 2 153 ? -5.836  -2.887  -20.065 1.00 56.23  ? 162 VAL   B CA  1 
ATOM   1436 C  C   . VAL   B 2 153 ? -6.780  -2.831  -18.858 1.00 54.01  ? 162 VAL   B C   1 
ATOM   1437 O  O   . VAL   B 2 153 ? -6.324  -2.703  -17.732 1.00 53.78  ? 162 VAL   B O   1 
ATOM   1438 C  CB  . VAL   B 2 153 ? -4.990  -4.189  -20.133 1.00 56.03  ? 162 VAL   B CB  1 
ATOM   1439 C  CG1 . VAL   B 2 153 ? -5.864  -5.423  -19.967 1.00 55.66  ? 162 VAL   B CG1 1 
ATOM   1440 C  CG2 . VAL   B 2 153 ? -4.222  -4.259  -21.456 1.00 56.90  ? 162 VAL   B CG2 1 
ATOM   1441 N  N   . SER   B 2 154 ? -8.095  -2.806  -19.107 1.00 51.92  ? 163 SER   B N   1 
ATOM   1442 C  CA  . SER   B 2 154 ? -9.077  -2.722  -18.038 1.00 49.84  ? 163 SER   B CA  1 
ATOM   1443 C  C   . SER   B 2 154 ? -9.657  -4.070  -17.700 1.00 48.37  ? 163 SER   B C   1 
ATOM   1444 O  O   . SER   B 2 154 ? -9.938  -4.844  -18.594 1.00 47.80  ? 163 SER   B O   1 
ATOM   1445 C  CB  . SER   B 2 154 ? -10.224 -1.800  -18.445 1.00 49.18  ? 163 SER   B CB  1 
ATOM   1446 O  OG  . SER   B 2 154 ? -11.365 -1.898  -17.600 1.00 48.08  ? 163 SER   B OG  1 
ATOM   1447 N  N   . ALA   B 2 155 ? -9.982  -4.284  -16.427 1.00 47.16  ? 164 ALA   B N   1 
ATOM   1448 C  CA  . ALA   B 2 155 ? -10.688 -5.484  -16.017 1.00 46.75  ? 164 ALA   B CA  1 
ATOM   1449 C  C   . ALA   B 2 155 ? -12.152 -5.375  -16.491 1.00 46.31  ? 164 ALA   B C   1 
ATOM   1450 O  O   . ALA   B 2 155 ? -12.663 -4.275  -16.722 1.00 46.09  ? 164 ALA   B O   1 
ATOM   1451 C  CB  . ALA   B 2 155 ? -10.669 -5.589  -14.496 1.00 46.80  ? 164 ALA   B CB  1 
ATOM   1452 N  N   . ILE   B 2 156 ? -12.824 -6.517  -16.628 1.00 46.00  ? 165 ILE   B N   1 
ATOM   1453 C  CA  . ILE   B 2 156 ? -14.255 -6.529  -16.880 1.00 45.77  ? 165 ILE   B CA  1 
ATOM   1454 C  C   . ILE   B 2 156 ? -14.772 -6.635  -15.438 1.00 44.71  ? 165 ILE   B C   1 
ATOM   1455 O  O   . ILE   B 2 156 ? -14.740 -7.732  -14.871 1.00 43.26  ? 165 ILE   B O   1 
ATOM   1456 C  CB  . ILE   B 2 156 ? -14.724 -7.730  -17.733 1.00 46.33  ? 165 ILE   B CB  1 
ATOM   1457 C  CG1 . ILE   B 2 156 ? -14.040 -7.736  -19.107 1.00 47.55  ? 165 ILE   B CG1 1 
ATOM   1458 C  CG2 . ILE   B 2 156 ? -16.256 -7.688  -17.879 1.00 46.89  ? 165 ILE   B CG2 1 
ATOM   1459 C  CD1 . ILE   B 2 156 ? -14.411 -8.941  -19.985 1.00 48.31  ? 165 ILE   B CD1 1 
ATOM   1460 N  N   . THR   B 2 157 ? -15.136 -5.482  -14.814 1.00 44.71  ? 166 THR   B N   1 
ATOM   1461 C  CA  . THR   B 2 157 ? -15.576 -5.433  -13.403 1.00 44.61  ? 166 THR   B CA  1 
ATOM   1462 C  C   . THR   B 2 157 ? -17.073 -5.625  -13.243 1.00 44.60  ? 166 THR   B C   1 
ATOM   1463 O  O   . THR   B 2 157 ? -17.839 -4.732  -13.583 1.00 44.78  ? 166 THR   B O   1 
ATOM   1464 C  CB  . THR   B 2 157 ? -15.183 -4.112  -12.734 1.00 45.51  ? 166 THR   B CB  1 
ATOM   1465 O  OG1 . THR   B 2 157 ? -13.784 -3.894  -12.864 1.00 46.53  ? 166 THR   B OG1 1 
ATOM   1466 C  CG2 . THR   B 2 157 ? -15.533 -4.090  -11.282 1.00 45.88  ? 166 THR   B CG2 1 
ATOM   1467 N  N   . GLN   B 2 158 ? -17.487 -6.754  -12.682 1.00 44.43  ? 167 GLN   B N   1 
ATOM   1468 C  CA  . GLN   B 2 158 ? -18.892 -7.039  -12.462 1.00 45.11  ? 167 GLN   B CA  1 
ATOM   1469 C  C   . GLN   B 2 158 ? -19.201 -7.126  -10.952 1.00 47.45  ? 167 GLN   B C   1 
ATOM   1470 O  O   . GLN   B 2 158 ? -18.378 -7.596  -10.159 1.00 47.07  ? 167 GLN   B O   1 
ATOM   1471 C  CB  . GLN   B 2 158 ? -19.278 -8.342  -13.199 1.00 44.87  ? 167 GLN   B CB  1 
ATOM   1472 C  CG  . GLN   B 2 158 ? -20.763 -8.734  -13.190 1.00 45.02  ? 167 GLN   B CG  1 
ATOM   1473 C  CD  . GLN   B 2 158 ? -21.675 -7.662  -13.745 1.00 46.44  ? 167 GLN   B CD  1 
ATOM   1474 O  OE1 . GLN   B 2 158 ? -21.773 -6.547  -13.212 1.00 46.53  ? 167 GLN   B OE1 1 
ATOM   1475 N  NE2 . GLN   B 2 158 ? -22.398 -7.980  -14.801 1.00 45.48  ? 167 GLN   B NE2 1 
ATOM   1476 N  N   . GLY   B 2 159 ? -20.379 -6.655  -10.572 1.00 49.50  ? 168 GLY   B N   1 
ATOM   1477 C  CA  . GLY   B 2 159 ? -20.829 -6.752  -9.197  1.00 52.35  ? 168 GLY   B CA  1 
ATOM   1478 C  C   . GLY   B 2 159 ? -21.590 -8.041  -8.956  1.00 55.74  ? 168 GLY   B C   1 
ATOM   1479 O  O   . GLY   B 2 159 ? -21.759 -8.864  -9.857  1.00 55.38  ? 168 GLY   B O   1 
ATOM   1480 N  N   . LYS   B 2 160 ? -22.066 -8.221  -7.725  1.00 58.83  ? 169 LYS   B N   1 
ATOM   1481 C  CA  . LYS   B 2 160 ? -22.856 -9.387  -7.348  1.00 61.78  ? 169 LYS   B CA  1 
ATOM   1482 C  C   . LYS   B 2 160 ? -24.323 -8.945  -7.192  1.00 64.13  ? 169 LYS   B C   1 
ATOM   1483 O  O   . LYS   B 2 160 ? -24.587 -7.876  -6.637  1.00 64.10  ? 169 LYS   B O   1 
ATOM   1484 C  CB  . LYS   B 2 160 ? -22.330 -9.965  -6.019  1.00 64.83  ? 169 LYS   B CB  1 
ATOM   1485 C  CG  . LYS   B 2 160 ? -23.011 -11.251 -5.582  1.00 70.90  ? 169 LYS   B CG  1 
ATOM   1486 C  CD  . LYS   B 2 160 ? -23.078 -11.374 -4.062  1.00 76.81  ? 169 LYS   B CD  1 
ATOM   1487 C  CE  . LYS   B 2 160 ? -23.587 -12.735 -3.630  1.00 81.26  ? 169 LYS   B CE  1 
ATOM   1488 N  NZ  . LYS   B 2 160 ? -23.774 -12.826 -2.150  1.00 83.45  ? 169 LYS   B NZ  1 
ATOM   1489 N  N   . ARG   B 2 161 ? -25.270 -9.743  -7.702  1.00 65.93  ? 170 ARG   B N   1 
ATOM   1490 C  CA  . ARG   B 2 161 ? -26.690 -9.432  -7.545  1.00 67.96  ? 170 ARG   B CA  1 
ATOM   1491 C  C   . ARG   B 2 161 ? -27.258 -10.276 -6.385  1.00 69.91  ? 170 ARG   B C   1 
ATOM   1492 O  O   . ARG   B 2 161 ? -27.324 -11.502 -6.487  1.00 70.20  ? 170 ARG   B O   1 
ATOM   1493 C  CB  . ARG   B 2 161 ? -27.473 -9.671  -8.851  1.00 69.06  ? 170 ARG   B CB  1 
ATOM   1494 C  CG  . ARG   B 2 161 ? -28.956 -9.382  -8.692  1.00 71.36  ? 170 ARG   B CG  1 
ATOM   1495 C  CD  . ARG   B 2 161 ? -29.781 -9.659  -9.928  1.00 74.08  ? 170 ARG   B CD  1 
ATOM   1496 N  NE  . ARG   B 2 161 ? -31.135 -9.135  -9.754  1.00 77.29  ? 170 ARG   B NE  1 
ATOM   1497 C  CZ  . ARG   B 2 161 ? -31.819 -8.486  -10.691 1.00 80.37  ? 170 ARG   B CZ  1 
ATOM   1498 N  NH1 . ARG   B 2 161 ? -31.300 -8.310  -11.902 1.00 79.97  ? 170 ARG   B NH1 1 
ATOM   1499 N  NH2 . ARG   B 2 161 ? -33.035 -8.025  -10.432 1.00 80.67  ? 170 ARG   B NH2 1 
ATOM   1500 N  N   . GLU   B 2 162 ? -27.629 -9.624  -5.275  1.00 71.04  ? 171 GLU   B N   1 
ATOM   1501 C  CA  . GLU   B 2 162 ? -28.166 -10.305 -4.092  1.00 72.84  ? 171 GLU   B CA  1 
ATOM   1502 C  C   . GLU   B 2 162 ? -29.545 -10.920 -4.344  1.00 73.66  ? 171 GLU   B C   1 
ATOM   1503 O  O   . GLU   B 2 162 ? -29.860 -11.970 -3.784  1.00 74.12  ? 171 GLU   B O   1 
ATOM   1504 C  CB  . GLU   B 2 162 ? -28.222 -9.342  -2.892  1.00 76.41  ? 171 GLU   B CB  1 
ATOM   1505 C  CG  . GLU   B 2 162 ? -26.879 -9.114  -2.214  1.00 83.61  ? 171 GLU   B CG  1 
ATOM   1506 C  CD  . GLU   B 2 162 ? -26.505 -10.160 -1.176  1.00 92.23  ? 171 GLU   B CD  1 
ATOM   1507 O  OE1 . GLU   B 2 162 ? -27.274 -10.333 -0.201  1.00 93.16  ? 171 GLU   B OE1 1 
ATOM   1508 O  OE2 . GLU   B 2 162 ? -25.441 -10.804 -1.334  1.00 95.05  ? 171 GLU   B OE2 1 
HETATM 1509 S  S   . DMS   C 3 .   ? -18.729 11.913  -0.176  1.00 69.82  ? 201 DMS   B S   1 
HETATM 1510 O  O   . DMS   C 3 .   ? -19.663 10.757  -0.396  1.00 69.69  ? 201 DMS   B O   1 
HETATM 1511 C  C1  . DMS   C 3 .   ? -19.591 13.445  -0.585  1.00 69.74  ? 201 DMS   B C1  1 
HETATM 1512 C  C2  . DMS   C 3 .   ? -17.617 12.066  -1.608  1.00 69.70  ? 201 DMS   B C2  1 
HETATM 1513 N  N1  . A1B80 D 4 .   ? -6.131  3.156   -13.603 1.00 57.59  ? 202 A1B80 B N1  1 
HETATM 1514 N  N3  . A1B80 D 4 .   ? -9.074  2.915   -7.392  1.00 50.82  ? 202 A1B80 B N3  1 
HETATM 1515 C  C4  . A1B80 D 4 .   ? -3.013  5.408   -14.732 1.00 63.58  ? 202 A1B80 B C4  1 
HETATM 1516 C  C5  . A1B80 D 4 .   ? -2.763  4.357   -13.866 1.00 63.12  ? 202 A1B80 B C5  1 
HETATM 1517 C  C6  . A1B80 D 4 .   ? -5.208  3.271   -14.720 1.00 59.83  ? 202 A1B80 B C6  1 
HETATM 1518 C  C7  . A1B80 D 4 .   ? -7.441  3.194   -13.826 1.00 55.60  ? 202 A1B80 B C7  1 
HETATM 1519 C  C8  . A1B80 D 4 .   ? -8.035  4.614   -13.892 1.00 54.51  ? 202 A1B80 B C8  1 
HETATM 1520 C  C10 . A1B80 D 4 .   ? -8.663  5.853   -10.950 1.00 51.68  ? 202 A1B80 B C10 1 
HETATM 1521 C  C13 . A1B80 D 4 .   ? -9.362  3.529   -9.596  1.00 50.93  ? 202 A1B80 B C13 1 
HETATM 1522 C  C15 . A1B80 D 4 .   ? -9.689  2.423   -8.635  1.00 50.50  ? 202 A1B80 B C15 1 
HETATM 1523 C  C17 . A1B80 D 4 .   ? -8.243  5.042   -15.340 1.00 54.94  ? 202 A1B80 B C17 1 
HETATM 1524 C  C20 . A1B80 D 4 .   ? -8.414  5.700   -18.110 1.00 55.39  ? 202 A1B80 B C20 1 
HETATM 1525 C  C21 . A1B80 D 4 .   ? -7.386  6.194   -17.308 1.00 56.27  ? 202 A1B80 B C21 1 
HETATM 1526 C  C22 . A1B80 D 4 .   ? -6.125  6.568   -15.504 1.00 56.64  ? 202 A1B80 B C22 1 
HETATM 1527 C  C24 . A1B80 D 4 .   ? -1.915  4.521   -12.780 1.00 63.58  ? 202 A1B80 B C24 1 
HETATM 1528 C  C1  . A1B80 D 4 .   ? -0.821  8.132   -13.244 1.00 64.41  ? 202 A1B80 B C1  1 
HETATM 1529 C  C2  . A1B80 D 4 .   ? -1.514  6.808   -13.451 1.00 64.21  ? 202 A1B80 B C2  1 
HETATM 1530 C  C3  . A1B80 D 4 .   ? -2.381  6.619   -14.517 1.00 64.03  ? 202 A1B80 B C3  1 
HETATM 1531 S  S1  . A1B80 D 4 .   ? -3.607  2.821   -14.094 1.00 62.21  ? 202 A1B80 B S1  1 
HETATM 1532 O  O1  . A1B80 D 4 .   ? -3.803  2.210   -12.810 1.00 63.38  ? 202 A1B80 B O1  1 
HETATM 1533 O  O2  . A1B80 D 4 .   ? -2.957  2.064   -15.116 1.00 63.16  ? 202 A1B80 B O2  1 
HETATM 1534 O  O3  . A1B80 D 4 .   ? -8.107  2.192   -14.058 1.00 55.06  ? 202 A1B80 B O3  1 
HETATM 1535 N  N2  . A1B80 D 4 .   ? -9.187  4.763   -13.037 1.00 53.38  ? 202 A1B80 B N2  1 
HETATM 1536 C  C9  . A1B80 D 4 .   ? -9.079  4.717   -11.654 1.00 52.15  ? 202 A1B80 B C9  1 
HETATM 1537 C  C11 . A1B80 D 4 .   ? -8.634  5.834   -9.565  1.00 51.34  ? 202 A1B80 B C11 1 
HETATM 1538 C  C12 . A1B80 D 4 .   ? -8.959  4.659   -8.897  1.00 51.03  ? 202 A1B80 B C12 1 
HETATM 1539 C  C14 . A1B80 D 4 .   ? -9.382  3.528   -10.982 1.00 51.51  ? 202 A1B80 B C14 1 
HETATM 1540 C  C16 . A1B80 D 4 .   ? -9.036  4.386   -7.422  1.00 50.96  ? 202 A1B80 B C16 1 
HETATM 1541 C  C18 . A1B80 D 4 .   ? -9.278  4.553   -16.137 1.00 54.29  ? 202 A1B80 B C18 1 
HETATM 1542 C  C19 . A1B80 D 4 .   ? -9.352  4.889   -17.497 1.00 54.28  ? 202 A1B80 B C19 1 
HETATM 1543 CL CL1 . A1B80 D 4 .   ? -10.670 4.286   -18.473 1.00 52.94  ? 202 A1B80 B CL1 1 
HETATM 1544 N  N4  . A1B80 D 4 .   ? -6.347  7.015   -17.597 1.00 56.88  ? 202 A1B80 B N4  1 
HETATM 1545 N  N5  . A1B80 D 4 .   ? -5.563  7.227   -16.502 1.00 56.97  ? 202 A1B80 B N5  1 
HETATM 1546 C  C23 . A1B80 D 4 .   ? -7.277  5.872   -15.945 1.00 56.03  ? 202 A1B80 B C23 1 
HETATM 1547 C  C25 . A1B80 D 4 .   ? -1.296  5.744   -12.589 1.00 63.94  ? 202 A1B80 B C25 1 
HETATM 1548 O  O   . HOH   E 5 .   ? -26.584 19.901  -19.744 1.00 58.12  ? 101 HOH   A O   1 
HETATM 1549 O  O   . HOH   E 5 .   ? -3.363  1.631   -3.984  1.00 51.41  ? 102 HOH   A O   1 
HETATM 1550 O  O   . HOH   E 5 .   ? -23.678 19.087  -19.502 1.00 42.42  ? 103 HOH   A O   1 
HETATM 1551 O  O   . HOH   E 5 .   ? -2.168  -3.901  -6.313  1.00 35.67  ? 104 HOH   A O   1 
HETATM 1552 O  O   . HOH   E 5 .   ? -9.455  -6.757  -25.557 1.00 53.45  ? 105 HOH   A O   1 
HETATM 1553 O  O   . HOH   E 5 .   ? -25.445 12.984  -23.724 1.00 44.36  ? 106 HOH   A O   1 
HETATM 1554 O  O   . HOH   E 5 .   ? -7.056  -8.984  -3.222  1.00 37.82  ? 107 HOH   A O   1 
HETATM 1555 O  O   . HOH   E 5 .   ? -5.168  -14.706 -25.487 1.00 45.82  ? 108 HOH   A O   1 
HETATM 1556 O  O   . HOH   E 5 .   ? -30.857 0.481   -22.955 1.00 53.52  ? 109 HOH   A O   1 
HETATM 1557 O  O   . HOH   E 5 .   ? -7.934  -1.326  6.887   1.00 40.85  ? 110 HOH   A O   1 
HETATM 1558 O  O   . HOH   E 5 .   ? -28.811 -5.824  -27.830 1.00 46.89  ? 111 HOH   A O   1 
HETATM 1559 O  O   . HOH   E 5 .   ? -22.094 -8.884  -34.651 1.00 62.05  ? 112 HOH   A O   1 
HETATM 1560 O  O   . HOH   E 5 .   ? -5.014  -10.110 -5.687  1.00 44.75  ? 113 HOH   A O   1 
HETATM 1561 O  O   . HOH   E 5 .   ? -26.068 -2.633  -35.723 1.00 72.67  ? 114 HOH   A O   1 
HETATM 1562 O  O   . HOH   E 5 .   ? -2.639  -8.225  -3.294  1.00 51.88  ? 115 HOH   A O   1 
HETATM 1563 O  O   . HOH   E 5 .   ? -3.963  -0.521  0.199   1.00 56.78  ? 116 HOH   A O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -31.081 12.804  -19.068 1.00 51.93  ? 301 HOH   B O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -34.063 2.046   -15.383 1.00 37.73  ? 302 HOH   B O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -16.235 26.317  -12.416 1.00 70.89  ? 303 HOH   B O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -17.517 0.901   -33.885 1.00 57.53  ? 304 HOH   B O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -15.741 -10.079 -15.243 1.00 49.67  ? 305 HOH   B O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -6.497  -0.237  -10.990 1.00 39.59  ? 306 HOH   B O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -35.448 -5.694  -10.118 1.00 61.48  ? 307 HOH   B O   1 
HETATM 1571 O  O   . HOH   F 5 .   ? -23.752 -6.388  -4.635  1.00 56.98  ? 308 HOH   B O   1 
HETATM 1572 O  O   . HOH   F 5 .   ? -13.043 -2.188  -14.736 1.00 33.46  ? 309 HOH   B O   1 
HETATM 1573 O  O   . HOH   F 5 .   ? -16.444 -14.813 -16.638 1.00 53.99  ? 310 HOH   B O   1 
HETATM 1574 O  O   . HOH   F 5 .   ? -19.868 -12.281 -25.519 1.00 62.47  ? 311 HOH   B O   1 
HETATM 1575 O  O   . HOH   F 5 .   ? -28.923 -3.998  -22.020 1.00 55.14  ? 312 HOH   B O   1 
HETATM 1576 O  O   . HOH   F 5 .   ? -11.879 2.035   -5.963  1.00 35.35  ? 313 HOH   B O   1 
HETATM 1577 O  O   . HOH   F 5 .   ? -15.319 -4.961  1.308   1.00 45.26  ? 314 HOH   B O   1 
HETATM 1578 O  O   . HOH   F 5 .   ? -27.699 -6.713  -5.490  1.00 64.90  ? 315 HOH   B O   1 
HETATM 1579 O  O   . HOH   F 5 .   ? -4.798  -1.307  -25.003 1.00 54.71  ? 316 HOH   B O   1 
HETATM 1580 O  O   . HOH   F 5 .   ? -34.587 0.746   -3.408  1.00 50.06  ? 317 HOH   B O   1 
HETATM 1581 O  O   . HOH   F 5 .   ? -12.426 -3.363  -10.100 1.00 43.82  ? 318 HOH   B O   1 
HETATM 1582 O  O   . HOH   F 5 .   ? -26.471 -7.769  -16.733 1.00 40.80  ? 319 HOH   B O   1 
HETATM 1583 O  O   . HOH   F 5 .   ? -18.122 -10.795 -16.683 1.00 40.61  ? 320 HOH   B O   1 
HETATM 1584 O  O   . HOH   F 5 .   ? -27.866 -6.117  -18.529 1.00 47.20  ? 321 HOH   B O   1 
HETATM 1585 O  O   . HOH   F 5 .   ? -29.580 -1.807  -19.261 1.00 60.04  ? 322 HOH   B O   1 
HETATM 1586 O  O   . HOH   F 5 .   ? -22.727 -13.804 -21.234 1.00 49.48  ? 323 HOH   B O   1 
HETATM 1587 O  O   . HOH   F 5 .   ? -7.361  -10.711 -5.295  1.00 47.79  ? 324 HOH   B O   1 
HETATM 1588 O  O   . HOH   F 5 .   ? -21.732 -12.219 -12.880 1.00 52.19  ? 325 HOH   B O   1 
HETATM 1589 O  O   . HOH   F 5 .   ? -30.990 13.041  -16.435 1.00 54.63  ? 326 HOH   B O   1 
HETATM 1590 O  O   . HOH   F 5 .   ? -18.870 15.095  -22.389 1.00 37.67  ? 327 HOH   B O   1 
HETATM 1591 O  O   . HOH   F 5 .   ? -7.086  -6.416  0.250   1.00 61.77  ? 328 HOH   B O   1 
HETATM 1592 O  O   . HOH   F 5 .   ? -15.335 9.482   -0.724  1.00 48.98  ? 329 HOH   B O   1 
HETATM 1593 O  O   . HOH   F 5 .   ? -29.876 -4.957  -0.892  1.00 38.36  ? 330 HOH   B O   1 
HETATM 1594 O  O   . HOH   F 5 .   ? -24.094 9.511   -27.705 1.00 44.25  ? 331 HOH   B O   1 
HETATM 1595 O  O   . HOH   F 5 .   ? -8.943  -10.643 -7.442  1.00 55.62  ? 332 HOH   B O   1 
HETATM 1596 O  O   . HOH   F 5 .   ? -11.173 7.718   -14.079 1.00 56.78  ? 333 HOH   B O   1 
HETATM 1597 O  O   . HOH   F 5 .   ? -29.139 16.205  -15.152 1.00 54.56  ? 334 HOH   B O   1 
HETATM 1598 O  O   . HOH   F 5 .   ? -23.997 -14.597 -18.267 1.00 62.57  ? 335 HOH   B O   1 
HETATM 1599 O  O   . HOH   F 5 .   ? -3.256  -11.546 -6.946  1.00 53.34  ? 336 HOH   B O   1 
HETATM 1600 O  O   . HOH   F 5 .   ? -21.291 7.035   -0.000  0.50 42.77  ? 337 HOH   B O   1 
HETATM 1601 O  O   . HOH   F 5 .   ? -19.591 -10.864 -9.774  1.00 56.32  ? 338 HOH   B O   1 
HETATM 1602 O  O   . HOH   F 5 .   ? -16.810 13.264  -5.585  1.00 55.45  ? 339 HOH   B O   1 
HETATM 1603 O  O   . HOH   F 5 .   ? -4.737  2.280   -10.003 1.00 55.55  ? 340 HOH   B O   1 
HETATM 1604 O  O   . HOH   F 5 .   ? -15.370 -8.628  -11.743 1.00 47.71  ? 341 HOH   B O   1 
HETATM 1605 O  O   . HOH   F 5 .   ? -18.486 19.020  -21.955 1.00 57.78  ? 342 HOH   B O   1 
HETATM 1606 O  O   . HOH   F 5 .   ? -17.565 -15.058 -30.952 1.00 54.09  ? 343 HOH   B O   1 
HETATM 1607 O  O   . HOH   F 5 .   ? -30.552 4.601   -2.181  1.00 59.27  ? 344 HOH   B O   1 
HETATM 1608 O  O   . HOH   F 5 .   ? -14.821 -6.629  -1.634  1.00 57.41  ? 345 HOH   B O   1 
HETATM 1609 O  O   . HOH   F 5 .   ? -25.969 -4.863  -3.948  1.00 43.23  ? 346 HOH   B O   1 
HETATM 1610 O  O   . HOH   F 5 .   ? -32.090 -6.979  -6.864  1.00 59.85  ? 347 HOH   B O   1 
HETATM 1611 O  O   . HOH   F 5 .   ? -15.850 -7.165  -8.192  1.00 64.42  ? 348 HOH   B O   1 
HETATM 1612 O  O   . HOH   F 5 .   ? -20.560 -13.718 -22.832 1.00 44.08  ? 349 HOH   B O   1 
HETATM 1613 O  O   . HOH   F 5 .   ? -23.032 -5.869  0.552   1.00 49.53  ? 350 HOH   B O   1 
HETATM 1614 O  O   . HOH   F 5 .   ? -32.294 7.355   -3.852  1.00 60.39  ? 351 HOH   B O   1 
HETATM 1615 O  O   . HOH   F 5 .   ? -14.818 16.732  -20.488 1.00 55.44  ? 352 HOH   B O   1 
HETATM 1616 O  O   . HOH   F 5 .   ? -30.236 -7.588  -5.325  1.00 58.50  ? 353 HOH   B O   1 
HETATM 1617 O  O   . HOH   F 5 .   ? -35.263 1.569   -7.593  1.00 58.44  ? 354 HOH   B O   1 
HETATM 1618 O  O   . HOH   F 5 .   ? -20.112 6.484   -33.218 1.00 62.16  ? 355 HOH   B O   1 
HETATM 1619 O  O   . HOH   F 5 .   ? -15.219 -12.456 -16.533 1.00 43.19  ? 356 HOH   B O   1 
HETATM 1620 O  O   . HOH   F 5 .   ? -22.499 -13.954 -25.633 1.00 51.87  ? 357 HOH   B O   1 
HETATM 1621 O  O   . HOH   F 5 .   ? -16.970 16.503  -21.886 1.00 39.37  ? 358 HOH   B O   1 
HETATM 1622 O  O   . HOH   F 5 .   ? -21.189 13.982  -33.726 1.00 59.11  ? 359 HOH   B O   1 
HETATM 1623 O  O   . HOH   F 5 .   ? -9.952  -20.399 -13.751 1.00 66.83  ? 360 HOH   B O   1 
HETATM 1624 O  O   . HOH   F 5 .   ? 2.985   -6.493  -20.168 1.00 80.50  ? 361 HOH   B O   1 
HETATM 1625 O  O   . HOH   F 5 .   ? -18.765 8.658   -32.995 1.00 62.37  ? 362 HOH   B O   1 
HETATM 1626 O  O   . HOH   F 5 .   ? -1.422  -15.391 -10.414 1.00 64.16  ? 363 HOH   B O   1 
HETATM 1627 O  O   . HOH   F 5 .   ? -23.182 -7.589  -2.266  1.00 60.98  ? 364 HOH   B O   1 
HETATM 1628 O  O   . HOH   F 5 .   ? -11.154 -6.770  2.038   1.00 56.19  ? 365 HOH   B O   1 
HETATM 1629 O  O   . HOH   F 5 .   ? 6.297   -3.663  -16.629 1.00 58.52  ? 366 HOH   B O   1 
HETATM 1630 O  O   . HOH   F 5 .   ? -4.620  5.359   -10.255 1.00 45.54  ? 367 HOH   B O   1 
HETATM 1631 O  O   . HOH   F 5 .   ? -17.372 27.859  -14.270 1.00 61.33  ? 368 HOH   B O   1 
HETATM 1632 O  O   . HOH   F 5 .   ? -11.658 12.567  -14.366 1.00 59.98  ? 369 HOH   B O   1 
HETATM 1633 O  O   . HOH   F 5 .   ? -18.902 -12.131 -13.313 1.00 67.74  ? 370 HOH   B O   1 
HETATM 1634 O  O   . HOH   F 5 .   ? -21.291 4.288   0.000   0.50 69.28  ? 371 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP   A 7   ? 1.0719 0.5895 0.7389 0.1805  -0.0380 -0.0915 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 1.0584 0.6272 0.7162 0.2059  -0.0279 -0.0970 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 1.0233 0.6103 0.6852 0.2047  -0.0127 -0.0697 50  ASP   A C   
4    O  O   . ASP   A 7   ? 1.0432 0.5860 0.6934 0.2094  -0.0143 -0.0548 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.1171 0.6661 0.7534 0.2414  -0.0392 -0.1225 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.2010 0.8092 0.8372 0.2662  -0.0275 -0.1304 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.2013 0.8532 0.8374 0.2711  -0.0219 -0.1470 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.2443 0.8553 0.8808 0.2807  -0.0240 -0.1199 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.9673 0.6152 0.6420 0.1992  0.0010  -0.0631 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.9313 0.6004 0.6102 0.1975  0.0135  -0.0407 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.8988 0.5879 0.5707 0.2262  0.0138  -0.0461 51  MET   A C   
12   O  O   . MET   A 8   ? 0.8845 0.6010 0.5589 0.2443  0.0119  -0.0670 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.9122 0.6306 0.6102 0.1770  0.0254  -0.0312 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.9255 0.6319 0.6379 0.1495  0.0241  -0.0251 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.9227 0.6871 0.6561 0.1318  0.0347  -0.0165 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.8924 0.6367 0.6496 0.1024  0.0294  -0.0116 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.8841 0.5623 0.5482 0.2308  0.0166  -0.0275 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.8659 0.5621 0.5263 0.2578  0.0128  -0.0320 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.8499 0.5653 0.5104 0.2532  0.0202  -0.0129 52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.8533 0.5507 0.5069 0.2340  0.0285  0.0077  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.8890 0.5318 0.5255 0.2845  -0.0025 -0.0372 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.9316 0.5079 0.5404 0.2774  -0.0039 -0.0125 52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.9602 0.4855 0.5632 0.2586  -0.0049 -0.0072 52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.9533 0.5136 0.5393 0.2916  -0.0054 0.0044  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.9996 0.4624 0.5795 0.2492  -0.0025 0.0182  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.9941 0.4902 0.5480 0.2860  -0.0029 0.0302  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 1.0260 0.4737 0.5786 0.2632  0.0004  0.0385  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 1.0815 0.4652 0.6056 0.2534  0.0070  0.0670  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.8280 0.5811 0.4982 0.2716  0.0167  -0.0214 53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.8222 0.5921 0.4906 0.2710  0.0194  -0.0082 53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.8477 0.5894 0.4907 0.2999  0.0048  -0.0057 53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.8611 0.5937 0.5021 0.3255  -0.0092 -0.0212 53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.7920 0.6263 0.4933 0.2638  0.0255  -0.0174 53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.7796 0.6503 0.5048 0.2840  0.0184  -0.0408 53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.7852 0.6384 0.5004 0.2361  0.0390  -0.0137 53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.7569 0.6864 0.5166 0.2763  0.0245  -0.0468 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.8571 0.5843 0.4775 0.2987  0.0074  0.0131  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.8858 0.5829 0.4718 0.3273  -0.0071 0.0182  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.8853 0.6149 0.4728 0.3293  -0.0076 0.0204  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.8945 0.6304 0.4803 0.3077  0.0083  0.0350  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.9473 0.5743 0.4863 0.3252  -0.0013 0.0442  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 1.0436 0.6200 0.5710 0.3311  -0.0081 0.0419  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 1.1861 0.6870 0.6672 0.3273  -0.0016 0.0707  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 1.2002 0.6960 0.6664 0.3103  0.0162  0.0941  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.2505 0.6961 0.7106 0.3413  -0.0132 0.0701  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.8739 0.6234 0.4653 0.3560  -0.0275 0.0048  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.8654 0.6428 0.4584 0.3591  -0.0324 0.0032  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.9013 0.6351 0.4391 0.3620  -0.0256 0.0277  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.9420 0.6209 0.4329 0.3781  -0.0290 0.0418  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.8621 0.6662 0.4718 0.3887  -0.0595 -0.0206 55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.8655 0.7133 0.4998 0.3839  -0.0654 -0.0306 55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.8596 0.7512 0.5359 0.4035  -0.0903 -0.0591 55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.8588 0.7900 0.5656 0.3917  -0.0943 -0.0685 55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.9007 0.8212 0.5810 0.4084  -0.1130 -0.0717 55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.9512 0.8248 0.5712 0.4395  -0.1288 -0.0650 55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.8595 0.8122 0.5696 0.3955  -0.1171 -0.0817 55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.8851 0.6405 0.4257 0.3472  -0.0145 0.0339  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.9168 0.6367 0.4036 0.3527  -0.0049 0.0561  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.9191 0.6553 0.3898 0.3716  -0.0192 0.0467  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.9568 0.6650 0.3769 0.3811  -0.0113 0.0631  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.9164 0.6350 0.4086 0.3212  0.0249  0.0760  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.8835 0.6634 0.3962 0.3773  -0.0395 0.0203  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.8817 0.6755 0.3840 0.3953  -0.0585 0.0068  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.8439 0.6930 0.4092 0.3807  -0.0672 -0.0162 57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.8040 0.6838 0.4206 0.3561  -0.0558 -0.0202 57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.8434 0.7022 0.4025 0.3974  -0.0891 -0.0320 58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.8169 0.7211 0.4336 0.3839  -0.1003 -0.0538 58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.8372 0.7439 0.4525 0.3619  -0.0798 -0.0430 58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.8706 0.7472 0.4340 0.3677  -0.0653 -0.0250 58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.8240 0.7320 0.4331 0.4124  -0.1369 -0.0780 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.8753 0.7924 0.4998 0.4368  -0.1648 -0.0962 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.8544 0.7700 0.4890 0.4349  -0.1550 -0.0893 58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.9214 0.8449 0.5450 0.4611  -0.1990 -0.1191 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.8128 0.7552 0.4845 0.3387  -0.0791 -0.0541 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.8249 0.7690 0.4979 0.3211  -0.0647 -0.0470 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.8415 0.7876 0.5132 0.3348  -0.0899 -0.0672 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.8078 0.7804 0.5313 0.3250  -0.1063 -0.0864 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.8043 0.7756 0.5291 0.2882  -0.0469 -0.0425 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.8236 0.7864 0.5397 0.2796  -0.0256 -0.0250 59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.8086 0.7793 0.5344 0.2740  -0.0368 -0.0368 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.8263 0.8129 0.5837 0.2528  -0.0103 -0.0219 59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.8846 0.8010 0.4951 0.3590  -0.0935 -0.0636 60  THR   A N   
83   N  N   B THR   A 17  ? 0.8836 0.8002 0.4945 0.3588  -0.0935 -0.0636 60  THR   A N   
84   C  CA  A THR   A 17  ? 0.9088 0.8187 0.5026 0.3791  -0.1201 -0.0847 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.9059 0.8170 0.5022 0.3783  -0.1204 -0.0851 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.9481 0.8360 0.4911 0.3878  -0.1046 -0.0740 60  THR   A C   
87   C  C   B THR   A 17  ? 0.9475 0.8352 0.4900 0.3884  -0.1053 -0.0744 60  THR   A C   
88   O  O   A THR   A 17  ? 0.9660 0.8359 0.4663 0.3913  -0.0784 -0.0501 60  THR   A O   
89   O  O   B THR   A 17  ? 0.9651 0.8350 0.4653 0.3917  -0.0788 -0.0503 60  THR   A O   
90   C  CB  A THR   A 17  ? 0.9448 0.8375 0.4991 0.4154  -0.1492 -0.0977 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.9306 0.8331 0.5055 0.4108  -0.1541 -0.1033 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.9900 0.8492 0.4782 0.4317  -0.1306 -0.0731 60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.9148 0.8439 0.5448 0.4084  -0.1864 -0.1340 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.9214 0.8422 0.5315 0.4141  -0.1726 -0.1166 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.9755 0.8380 0.4624 0.4483  -0.1611 -0.0995 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.9617 0.8501 0.5089 0.3932  -0.1216 -0.0931 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 1.0240 0.8935 0.5212 0.4081  -0.1101 -0.0885 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 1.1027 0.9425 0.5211 0.4493  -0.1225 -0.0918 61  TRP   A C   
99   O  O   . TRP   A 18  ? 1.1120 0.9472 0.5255 0.4694  -0.1581 -0.1147 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 1.0114 0.8859 0.5382 0.4036  -0.1297 -0.1118 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 1.0444 0.9006 0.5214 0.4246  -0.1235 -0.1143 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 1.0834 0.9171 0.5041 0.4612  -0.1454 -0.1336 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 1.0430 0.9041 0.5261 0.4123  -0.0968 -0.1015 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 1.1018 0.9266 0.4902 0.4732  -0.1300 -0.1321 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 1.0789 0.9220 0.5092 0.4432  -0.1013 -0.1134 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 1.0259 0.9053 0.5509 0.3811  -0.0704 -0.0818 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 1.0864 0.9328 0.5110 0.4436  -0.0793 -0.1068 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 1.0355 0.9169 0.5563 0.3810  -0.0529 -0.0763 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 1.0603 0.9271 0.5331 0.4120  -0.0559 -0.0881 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 1.1585 0.9791 0.5161 0.4621  -0.0933 -0.0687 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.2293 1.0171 0.5015 0.5018  -0.0993 -0.0665 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.2873 1.0640 0.5120 0.5267  -0.1009 -0.0789 62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.2902 1.0734 0.5083 0.5187  -0.0676 -0.0634 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.2847 1.0539 0.5144 0.5003  -0.0621 -0.0295 62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.4225 1.1526 0.5527 0.5403  -0.0585 -0.0193 62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.5402 1.2469 0.6256 0.5368  -0.0172 0.0205  62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.5523 1.2731 0.6877 0.5020  0.0071  0.0395  62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.5986 1.2705 0.5974 0.5688  -0.0095 0.0328  62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.3312 1.0924 0.5228 0.5592  -0.1406 -0.1087 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.3900 1.1362 0.5274 0.5886  -0.1448 -0.1240 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.4500 1.1709 0.4941 0.6158  -0.1117 -0.0968 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.4735 1.1731 0.4751 0.6288  -0.1116 -0.0811 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.4466 1.1798 0.5709 0.6175  -0.1999 -0.1655 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.4838 1.2402 0.7002 0.5900  -0.2299 -0.1939 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.5555 1.3042 0.7765 0.6121  -0.2881 -0.2341 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.5886 1.3575 0.8631 0.5966  -0.3046 -0.2340 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.6117 1.3822 0.9070 0.6148  -0.3628 -0.2755 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.4688 1.1927 0.4843 0.6228  -0.0810 -0.0890 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.5185 1.2245 0.4513 0.6446  -0.0407 -0.0603 64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.5096 1.2216 0.4622 0.6135  0.0014  -0.0184 64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.5433 1.2263 0.4362 0.6268  0.0149  0.0056  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.6033 1.2683 0.4328 0.6949  -0.0628 -0.0689 64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.7015 1.3571 0.4954 0.7312  -0.0981 -0.1096 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.7147 1.3875 0.5240 0.7294  -0.0831 -0.1188 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.7480 1.3777 0.4976 0.7636  -0.1429 -0.1338 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.4624 1.2080 0.4979 0.5725  0.0194  -0.0105 65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.4449 1.1994 0.5085 0.5402  0.0581  0.0251  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.4426 1.2136 0.4901 0.5395  0.1057  0.0447  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.4415 1.2232 0.4734 0.5597  0.1049  0.0266  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.4010 1.1845 0.5607 0.4992  0.0491  0.0200  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.4369 1.2106 0.4906 0.5173  0.1466  0.0798  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.4310 1.2282 0.4815 0.5131  0.1944  0.0991  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.3710 1.2145 0.5015 0.4921  0.1951  0.0832  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.3352 1.1969 0.5377 0.4572  0.1902  0.0854  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.4822 1.2718 0.5341 0.4880  0.2350  0.1395  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.5571 1.3759 0.6131 0.4808  0.2878  0.1615  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.6322 1.4714 0.7569 0.4353  0.3175  0.1875  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.6456 1.4610 0.7892 0.4141  0.3032  0.1963  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.6369 1.5170 0.7985 0.4220  0.3535  0.1969  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.3591 1.2179 0.4716 0.5172  0.1981  0.0653  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.3169 1.2140 0.4953 0.5049  0.1965  0.0490  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.2777 1.2135 0.4863 0.4891  0.2460  0.0725  67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.2952 1.2374 0.4565 0.5122  0.2784  0.0816  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.3388 1.2309 0.4883 0.5410  0.1710  0.0143  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.3125 1.2337 0.5337 0.5260  0.1604  -0.0030 67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.3694 1.2227 0.4822 0.5603  0.1231  -0.0095 67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.2242 1.1876 0.5118 0.4505  0.2522  0.0816  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.1835 1.1893 0.5141 0.4319  0.2948  0.1012  68  THR   A CA  
159  C  C   . THR   A 25  ? 1.1291 1.1691 0.5480 0.4034  0.2821  0.0916  68  THR   A C   
160  O  O   . THR   A 25  ? 1.1255 1.1518 0.5656 0.3966  0.2446  0.0744  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.2082 1.2017 0.5236 0.4125  0.3285  0.1369  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.2011 1.2372 0.5475 0.4017  0.3746  0.1546  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.1952 1.1743 0.5541 0.3767  0.3111  0.1452  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 1.0857 1.1708 0.5546 0.3889  0.3128  0.1021  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 1.0410 1.1581 0.5884 0.3654  0.2999  0.0935  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 1.0166 1.1579 0.5824 0.3878  0.2873  0.0686  69  GLY   A C   
167  O  O   . GLY   A 26  ? 1.0369 1.1537 0.5609 0.4167  0.2647  0.0479  69  GLY   A O   
168  N  N   . ASN   A 27  ? 0.9679 1.1557 0.5983 0.3752  0.2991  0.0688  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 0.9468 1.1575 0.6009 0.3965  0.2853  0.0456  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 0.9144 1.1083 0.6034 0.3817  0.2430  0.0324  70  ASN   A C   
171  O  O   . ASN   A 27  ? 0.9215 1.0912 0.6157 0.3558  0.2280  0.0408  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 0.9421 1.2155 0.6444 0.3983  0.3207  0.0506  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 0.9673 1.2739 0.7449 0.3606  0.3252  0.0629  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 0.9911 1.2791 0.7739 0.3299  0.3258  0.0800  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 0.9450 1.3005 0.7822 0.3644  0.3258  0.0521  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.8823 1.0835 0.5880 0.4006  0.2235  0.0119  71  SER   A N   
177  C  CA  . SER   A 28  ? 0.8668 1.0466 0.5974 0.3892  0.1857  0.0018  71  SER   A CA  
178  C  C   . SER   A 28  ? 0.8228 1.0400 0.6089 0.3907  0.1822  -0.0044 71  SER   A C   
179  O  O   . SER   A 28  ? 0.8248 1.0382 0.6088 0.4170  0.1664  -0.0228 71  SER   A O   
180  C  CB  . SER   A 28  ? 0.9085 1.0410 0.5970 0.4108  0.1544  -0.0183 71  SER   A CB  
181  O  OG  . SER   A 28  ? 0.9647 1.0948 0.6106 0.4479  0.1625  -0.0327 71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.7867 1.0385 0.6231 0.3641  0.1939  0.0092  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.7512 1.0444 0.6432 0.3684  0.1890  0.0017  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.7504 1.0187 0.6572 0.3614  0.1507  -0.0050 72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.7703 1.0028 0.6628 0.3389  0.1352  0.0028  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.7295 1.0702 0.6696 0.3420  0.2173  0.0180  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.7592 1.0631 0.6725 0.3132  0.2187  0.0348  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.7772 1.0319 0.6225 0.3313  0.2109  0.0302  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.7309 1.0183 0.6648 0.3823  0.1367  -0.0187 73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.7398 1.0027 0.6846 0.3793  0.1013  -0.0229 73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.6901 1.0014 0.6939 0.3650  0.1018  -0.0189 73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.6590 1.0214 0.7040 0.3828  0.1101  -0.0283 73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.7839 1.0242 0.7128 0.4153  0.0792  -0.0417 73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 0.8913 1.0710 0.7641 0.4240  0.0666  -0.0478 73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 0.9759 1.1256 0.8334 0.4584  0.0420  -0.0674 73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.0547 1.1722 0.8664 0.4789  0.0418  -0.0810 73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.1146 1.1703 0.8926 0.4746  0.0173  -0.0856 73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.1320 1.1514 0.9157 0.4500  -0.0047 -0.0751 73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.1208 1.1512 0.8598 0.4950  0.0147  -0.1013 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.6761 0.9740 0.6855 0.3338  0.0927  -0.0069 74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.6305 0.9688 0.6921 0.3162  0.0900  -0.0040 74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.6264 0.9407 0.6873 0.3141  0.0544  -0.0060 74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.6596 0.9208 0.6782 0.3054  0.0398  0.0004  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.6213 0.9630 0.6872 0.2820  0.1099  0.0109  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.6209 0.9820 0.6825 0.2812  0.1476  0.0179  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.6244 0.9691 0.6755 0.2502  0.1616  0.0338  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.5863 1.0156 0.7044 0.2911  0.1697  0.0125  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.5829 0.9381 0.6916 0.3209  0.0412  -0.0143 75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.5848 0.9173 0.6881 0.3206  0.0063  -0.0153 75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.5515 0.8903 0.6677 0.2875  0.0069  -0.0071 75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.5211 0.9128 0.6918 0.2763  0.0174  -0.0111 75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.5935 0.9678 0.7418 0.3467  -0.0129 -0.0305 75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.6966 1.0435 0.8199 0.3838  -0.0302 -0.0397 75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.7454 1.0370 0.8160 0.3872  -0.0289 -0.0344 75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.7111 1.0910 0.8698 0.4103  -0.0472 -0.0537 75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.5493 0.8357 0.6184 0.2713  -0.0023 0.0034  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.5238 0.8112 0.5988 0.2426  -0.0020 0.0091  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.5263 0.7799 0.5716 0.2417  -0.0323 0.0106  76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.5507 0.7662 0.5585 0.2580  -0.0489 0.0132  76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.5368 0.8030 0.5873 0.2207  0.0234  0.0204  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.5301 0.8221 0.5963 0.2250  0.0535  0.0213  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.5710 0.7797 0.5636 0.2206  0.0165  0.0280  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.4981 0.7636 0.5585 0.2230  -0.0392 0.0089  77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.5099 0.7452 0.5370 0.2211  -0.0650 0.0099  77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.5166 0.7312 0.5218 0.1949  -0.0525 0.0166  77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.5016 0.7366 0.5350 0.1776  -0.0318 0.0167  77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.4763 0.7481 0.5431 0.2286  -0.0916 -0.0047 77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.5379 0.7103 0.4913 0.1933  -0.0633 0.0232  78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.5456 0.6985 0.4760 0.1728  -0.0524 0.0276  78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.5547 0.6974 0.4638 0.1734  -0.0763 0.0217  78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.5781 0.6958 0.4484 0.1886  -0.0939 0.0258  78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.5652 0.6790 0.4513 0.1701  -0.0370 0.0409  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.5811 0.6767 0.4434 0.1530  -0.0258 0.0443  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.5603 0.6769 0.4555 0.1382  -0.0094 0.0402  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.6043 0.6673 0.4301 0.1518  -0.0141 0.0557  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.5340 0.6936 0.4670 0.1585  -0.0786 0.0115  79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.5462 0.6969 0.4583 0.1614  -0.1044 0.0016  79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.5926 0.7048 0.4482 0.1540  -0.0961 0.0075  79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.6118 0.7092 0.4543 0.1448  -0.0709 0.0182  79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.5152 0.7051 0.4871 0.1521  -0.1190 -0.0171 79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.5213 0.7158 0.5195 0.1272  -0.1022 -0.0205 79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.5281 0.6929 0.4906 0.1195  -0.0828 -0.0107 79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.5137 0.7401 0.5695 0.1155  -0.1104 -0.0337 79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.6083 0.7062 0.4300 0.1607  -0.1182 -0.0009 80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.6407 0.7068 0.4070 0.1583  -0.1123 0.0015  80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.6362 0.7049 0.4220 0.1391  -0.0942 -0.0040 80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.6649 0.7116 0.4144 0.1361  -0.0773 0.0023  80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.6793 0.7353 0.4101 0.1728  -0.1438 -0.0111 80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.7879 0.8100 0.4487 0.1772  -0.1380 -0.0077 80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.9015 0.9066 0.5094 0.1983  -0.1684 -0.0154 80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.9158 0.9268 0.5270 0.2002  -0.1915 -0.0381 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 0.9576 0.9401 0.5189 0.2137  -0.1708 0.0011  80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.5930 0.6880 0.4376 0.1263  -0.0962 -0.0147 81  SER   A N   
254  C  CA  . SER   A 38  ? 0.5776 0.6689 0.4407 0.1085  -0.0799 -0.0178 81  SER   A CA  
255  C  C   . SER   A 38  ? 0.5576 0.6487 0.4313 0.1013  -0.0486 -0.0014 81  SER   A C   
256  O  O   . SER   A 38  ? 0.5543 0.6392 0.4409 0.0886  -0.0347 -0.0015 81  SER   A O   
257  C  CB  . SER   A 38  ? 0.5751 0.6909 0.4981 0.0950  -0.0929 -0.0331 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.6269 0.7331 0.5370 0.0970  -0.1204 -0.0529 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.5406 0.6343 0.4062 0.1107  -0.0403 0.0114  82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.5340 0.6260 0.4054 0.1071  -0.0153 0.0238  82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.5035 0.6223 0.4252 0.1001  -0.0050 0.0245  82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.4994 0.6150 0.4233 0.0968  0.0155  0.0330  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.4757 0.6233 0.4380 0.0993  -0.0190 0.0154  83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.4524 0.6323 0.4680 0.0917  -0.0063 0.0163  83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.4559 0.6612 0.4883 0.1082  -0.0074 0.0180  83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.4450 0.6585 0.4770 0.1217  -0.0307 0.0105  83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.4371 0.6383 0.5004 0.0762  -0.0189 0.0032  83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.4972 0.6686 0.5448 0.0611  -0.0186 -0.0003 83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.5208 0.6670 0.5410 0.0582  0.0012  0.0105  83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.5220 0.6943 0.5836 0.0546  -0.0408 -0.0157 83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.4598 0.6758 0.5040 0.1096  0.0169  0.0269  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.4633 0.7037 0.5241 0.1272  0.0195  0.0269  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.4691 0.7616 0.5972 0.1231  0.0205  0.0187  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.4630 0.7712 0.6269 0.1022  0.0308  0.0183  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.4559 0.6847 0.4954 0.1336  0.0444  0.0374  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.4837 0.6699 0.4683 0.1418  0.0405  0.0429  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.4956 0.6697 0.4608 0.1596  0.0254  0.0414  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.5015 0.6597 0.4572 0.1316  0.0516  0.0494  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.5232 0.6587 0.4448 0.1629  0.0234  0.0474  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.5238 0.6498 0.4392 0.1373  0.0486  0.0531  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.5249 0.6402 0.4255 0.1509  0.0356  0.0526  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.4748 0.7942 0.6228 0.1430  0.0104  0.0120  85  SER   A N   
283  C  CA  . SER   A 42  ? 0.4636 0.8418 0.6824 0.1430  0.0133  0.0029  85  SER   A CA  
284  C  C   . SER   A 42  ? 0.4954 0.8929 0.7179 0.1704  0.0185  0.0012  85  SER   A C   
285  O  O   . SER   A 42  ? 0.5219 0.8852 0.6966 0.1905  0.0046  0.0025  85  SER   A O   
286  C  CB  . SER   A 42  ? 0.4493 0.8497 0.7036 0.1410  -0.0200 -0.0134 85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.4953 0.8723 0.7099 0.1644  -0.0509 -0.0184 85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.4901 0.9401 0.7681 0.1710  0.0404  -0.0011 86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.5208 0.9940 0.8056 0.2006  0.0458  -0.0061 86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.5319 1.0351 0.8518 0.2203  0.0122  -0.0231 86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.5028 1.0486 0.8824 0.2085  0.0010  -0.0334 86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.4981 1.0195 0.8261 0.1969  0.0853  -0.0022 86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.5492 1.0364 0.8301 0.1872  0.1180  0.0152  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.5310 1.0656 0.8514 0.1829  0.1589  0.0215  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.5972 1.0369 0.8090 0.2121  0.1122  0.0166  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.5769 1.0533 0.8581 0.2503  -0.0070 -0.0266 87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.5918 1.0872 0.8945 0.2766  -0.0417 -0.0417 87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.5853 1.1423 0.9445 0.2990  -0.0273 -0.0533 87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.5984 1.1475 0.9356 0.3128  -0.0037 -0.0491 87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6441 1.0716 0.8723 0.2983  -0.0671 -0.0368 87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6437 1.0848 0.8868 0.3336  -0.1004 -0.0509 87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.6801 1.0556 0.8575 0.2785  -0.0812 -0.0267 87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.5635 1.1836 0.9961 0.3042  -0.0420 -0.0695 88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.5467 1.2354 1.0422 0.3277  -0.0287 -0.0830 88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.5358 1.2594 1.0744 0.3554  -0.0711 -0.1043 88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.5527 1.2690 1.0754 0.3944  -0.0874 -0.1131 88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.5461 1.3005 1.1129 0.2995  0.0131  -0.0802 88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.6406 1.3818 1.1734 0.2959  0.0604  -0.0645 88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.6916 1.5102 1.2883 0.3082  0.0968  -0.0709 88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 0.6519 1.5325 1.3145 0.3301  0.0822  -0.0905 88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.7417 1.5597 1.3209 0.2976  0.1406  -0.0562 88  GLU   A OE2 
312  N  N   . GLY   B 7   ? 0.8928 0.8771 0.8236 0.2413  0.0459  -0.0701 16  GLY   B N   
313  C  CA  . GLY   B 7   ? 0.9144 0.8701 0.8285 0.2462  0.0375  -0.0646 16  GLY   B CA  
314  C  C   . GLY   B 7   ? 0.9061 0.8789 0.8361 0.2413  0.0279  -0.0623 16  GLY   B C   
315  O  O   . GLY   B 7   ? 0.8965 0.9056 0.8535 0.2394  0.0248  -0.0671 16  GLY   B O   
316  N  N   . GLU   B 8   ? 0.9038 0.8510 0.8171 0.2392  0.0229  -0.0549 17  GLU   B N   
317  C  CA  . GLU   B 8   ? 0.8832 0.8420 0.8064 0.2370  0.0127  -0.0534 17  GLU   B CA  
318  C  C   . GLU   B 8   ? 0.8480 0.8201 0.7844 0.2149  0.0137  -0.0506 17  GLU   B C   
319  O  O   . GLU   B 8   ? 0.8632 0.8185 0.7876 0.2016  0.0197  -0.0443 17  GLU   B O   
320  C  CB  . GLU   B 8   ? 0.9368 0.8663 0.8361 0.2467  0.0071  -0.0466 17  GLU   B CB  
321  C  CG  . GLU   B 8   ? 1.0022 0.9443 0.9093 0.2510  -0.0055 -0.0479 17  GLU   B CG  
322  C  CD  . GLU   B 8   ? 1.1206 1.0371 1.0029 0.2646  -0.0110 -0.0416 17  GLU   B CD  
323  O  OE1 . GLU   B 8   ? 1.1546 1.0428 1.0146 0.2628  -0.0033 -0.0328 17  GLU   B OE1 
324  O  OE2 . GLU   B 8   ? 1.1555 1.0806 1.0403 0.2770  -0.0232 -0.0454 17  GLU   B OE2 
325  N  N   A THR   B 9   ? 0.8132 0.8147 0.7742 0.2108  0.0071  -0.0555 18  THR   B N   
326  N  N   B THR   B 9   ? 0.8149 0.8165 0.7759 0.2108  0.0071  -0.0555 18  THR   B N   
327  C  CA  A THR   B 9   ? 0.7966 0.8074 0.7686 0.1901  0.0069  -0.0529 18  THR   B CA  
328  C  CA  B THR   B 9   ? 0.7996 0.8111 0.7722 0.1903  0.0066  -0.0531 18  THR   B CA  
329  C  C   A THR   B 9   ? 0.7779 0.7906 0.7540 0.1905  -0.0076 -0.0537 18  THR   B C   
330  C  C   B THR   B 9   ? 0.7796 0.7918 0.7553 0.1906  -0.0076 -0.0536 18  THR   B C   
331  O  O   A THR   B 9   ? 0.7723 0.7945 0.7604 0.1751  -0.0108 -0.0534 18  THR   B O   
332  O  O   B THR   B 9   ? 0.7743 0.7953 0.7613 0.1749  -0.0106 -0.0531 18  THR   B O   
333  C  CB  A THR   B 9   ? 0.7964 0.8373 0.7925 0.1780  0.0148  -0.0564 18  THR   B CB  
334  C  CB  B THR   B 9   ? 0.8026 0.8467 0.8015 0.1796  0.0129  -0.0574 18  THR   B CB  
335  O  OG1 A THR   B 9   ? 0.8103 0.8565 0.8052 0.1881  0.0243  -0.0600 18  THR   B OG1 
336  O  OG1 B THR   B 9   ? 0.8021 0.8741 0.8215 0.1929  0.0079  -0.0654 18  THR   B OG1 
337  C  CG2 A THR   B 9   ? 0.8008 0.8361 0.7939 0.1566  0.0217  -0.0504 18  THR   B CG2 
338  C  CG2 B THR   B 9   ? 0.8132 0.8520 0.8038 0.1737  0.0278  -0.0553 18  THR   B CG2 
339  N  N   . THR   B 10  ? 0.7685 0.7689 0.7316 0.2087  -0.0167 -0.0545 19  THR   B N   
340  C  CA  . THR   B 10  ? 0.7435 0.7424 0.7054 0.2127  -0.0315 -0.0562 19  THR   B CA  
341  C  C   . THR   B 10  ? 0.7167 0.6944 0.6616 0.2019  -0.0310 -0.0488 19  THR   B C   
342  O  O   . THR   B 10  ? 0.7270 0.6848 0.6526 0.2014  -0.0218 -0.0411 19  THR   B O   
343  C  CB  . THR   B 10  ? 0.7746 0.7613 0.7199 0.2373  -0.0394 -0.0575 19  THR   B CB  
344  O  OG1 . THR   B 10  ? 0.7914 0.7954 0.7489 0.2503  -0.0391 -0.0642 19  THR   B OG1 
345  C  CG2 . THR   B 10  ? 0.7755 0.7620 0.7184 0.2447  -0.0564 -0.0613 19  THR   B CG2 
346  N  N   . ASP   B 11  ? 0.6819 0.6639 0.6338 0.1935  -0.0415 -0.0512 20  ASP   B N   
347  C  CA  . ASP   B 11  ? 0.6782 0.6399 0.6121 0.1870  -0.0433 -0.0453 20  ASP   B CA  
348  C  C   . ASP   B 11  ? 0.6740 0.6135 0.5795 0.2049  -0.0446 -0.0400 20  ASP   B C   
349  O  O   . ASP   B 11  ? 0.6799 0.6186 0.5803 0.2226  -0.0507 -0.0429 20  ASP   B O   
350  C  CB  . ASP   B 11  ? 0.7008 0.6663 0.6434 0.1805  -0.0586 -0.0510 20  ASP   B CB  
351  C  CG  . ASP   B 11  ? 0.7583 0.7339 0.7190 0.1573  -0.0561 -0.0514 20  ASP   B CG  
352  O  OD1 . ASP   B 11  ? 0.7411 0.7321 0.7166 0.1474  -0.0435 -0.0500 20  ASP   B OD1 
353  O  OD2 . ASP   B 11  ? 0.7970 0.7629 0.7548 0.1495  -0.0670 -0.0529 20  ASP   B OD2 
354  N  N   . GLY   B 12  ? 0.6593 0.5826 0.5469 0.2009  -0.0385 -0.0318 21  GLY   B N   
355  C  CA  . GLY   B 12  ? 0.6487 0.5545 0.5110 0.2157  -0.0373 -0.0249 21  GLY   B CA  
356  C  C   . GLY   B 12  ? 0.6310 0.5278 0.4825 0.2083  -0.0235 -0.0149 21  GLY   B C   
357  O  O   . GLY   B 12  ? 0.6328 0.5350 0.4941 0.1925  -0.0158 -0.0141 21  GLY   B O   
358  N  N   . VAL   B 13  ? 0.6159 0.5002 0.4469 0.2196  -0.0204 -0.0071 22  VAL   B N   
359  C  CA  . VAL   B 13  ? 0.6051 0.4837 0.4275 0.2124  -0.0081 0.0029  22  VAL   B CA  
360  C  C   . VAL   B 13  ? 0.6083 0.4801 0.4297 0.2128  0.0015  0.0064  22  VAL   B C   
361  O  O   . VAL   B 13  ? 0.6154 0.4822 0.4333 0.2259  -0.0018 0.0039  22  VAL   B O   
362  C  CB  . VAL   B 13  ? 0.6064 0.4788 0.4090 0.2224  -0.0088 0.0105  22  VAL   B CB  
363  C  CG1 . VAL   B 13  ? 0.6145 0.4774 0.3998 0.2431  -0.0117 0.0134  22  VAL   B CG1 
364  C  CG2 . VAL   B 13  ? 0.6018 0.4754 0.4011 0.2123  0.0031  0.0202  22  VAL   B CG2 
365  N  N   . TYR   B 14  ? 0.6024 0.4732 0.4275 0.1983  0.0117  0.0104  23  TYR   B N   
366  C  CA  . TYR   B 14  ? 0.6059 0.4657 0.4287 0.1965  0.0197  0.0126  23  TYR   B CA  
367  C  C   . TYR   B 14  ? 0.6214 0.4733 0.4360 0.1869  0.0292  0.0229  23  TYR   B C   
368  O  O   . TYR   B 14  ? 0.6298 0.4911 0.4476 0.1772  0.0307  0.0256  23  TYR   B O   
369  C  CB  . TYR   B 14  ? 0.5862 0.4533 0.4245 0.1861  0.0218  0.0043  23  TYR   B CB  
370  C  CG  . TYR   B 14  ? 0.5617 0.4396 0.4120 0.1946  0.0148  -0.0056 23  TYR   B CG  
371  C  CD1 . TYR   B 14  ? 0.5515 0.4440 0.4122 0.1952  0.0057  -0.0108 23  TYR   B CD1 
372  C  CD2 . TYR   B 14  ? 0.5646 0.4386 0.4164 0.2017  0.0170  -0.0103 23  TYR   B CD2 
373  C  CE1 . TYR   B 14  ? 0.5487 0.4552 0.4239 0.2014  -0.0014 -0.0198 23  TYR   B CE1 
374  C  CE2 . TYR   B 14  ? 0.5611 0.4505 0.4266 0.2108  0.0105  -0.0194 23  TYR   B CE2 
375  C  CZ  . TYR   B 14  ? 0.5609 0.4687 0.4400 0.2096  0.0013  -0.0240 23  TYR   B CZ  
376  O  OH  . TYR   B 14  ? 0.5719 0.4998 0.4690 0.2158  -0.0056 -0.0332 23  TYR   B OH  
377  N  N   . ARG   B 15  ? 0.6228 0.4576 0.4279 0.1885  0.0353  0.0281  24  ARG   B N   
378  C  CA  . ARG   B 15  ? 0.6298 0.4573 0.4305 0.1758  0.0440  0.0376  24  ARG   B CA  
379  C  C   . ARG   B 15  ? 0.6336 0.4572 0.4423 0.1611  0.0468  0.0315  24  ARG   B C   
380  O  O   . ARG   B 15  ? 0.6366 0.4535 0.4467 0.1658  0.0450  0.0235  24  ARG   B O   
381  C  CB  . ARG   B 15  ? 0.6557 0.4614 0.4394 0.1831  0.0492  0.0474  24  ARG   B CB  
382  C  CG  . ARG   B 15  ? 0.6837 0.4887 0.4538 0.2013  0.0472  0.0537  24  ARG   B CG  
383  C  CD  . ARG   B 15  ? 0.7225 0.5015 0.4730 0.2095  0.0529  0.0634  24  ARG   B CD  
384  N  NE  . ARG   B 15  ? 0.7365 0.5135 0.4707 0.2304  0.0500  0.0681  24  ARG   B NE  
385  C  CZ  . ARG   B 15  ? 0.7726 0.5566 0.4977 0.2339  0.0550  0.0792  24  ARG   B CZ  
386  N  NH1 . ARG   B 15  ? 0.7612 0.5570 0.4945 0.2170  0.0635  0.0875  24  ARG   B NH1 
387  N  NH2 . ARG   B 15  ? 0.7712 0.5524 0.4788 0.2553  0.0513  0.0818  24  ARG   B NH2 
388  N  N   . VAL   B 16  ? 0.6351 0.4638 0.4482 0.1451  0.0507  0.0349  25  VAL   B N   
389  C  CA  . VAL   B 16  ? 0.6492 0.4730 0.4667 0.1311  0.0527  0.0296  25  VAL   B CA  
390  C  C   . VAL   B 16  ? 0.6804 0.4840 0.4891 0.1229  0.0579  0.0375  25  VAL   B C   
391  O  O   . VAL   B 16  ? 0.6731 0.4833 0.4830 0.1150  0.0613  0.0473  25  VAL   B O   
392  C  CB  . VAL   B 16  ? 0.6487 0.4924 0.4763 0.1189  0.0515  0.0274  25  VAL   B CB  
393  C  CG1 . VAL   B 16  ? 0.6529 0.4905 0.4821 0.1073  0.0525  0.0201  25  VAL   B CG1 
394  C  CG2 . VAL   B 16  ? 0.6452 0.5057 0.4789 0.1262  0.0464  0.0228  25  VAL   B CG2 
395  N  N   . MET   B 17  ? 0.7153 0.4941 0.5149 0.1257  0.0585  0.0338  26  MET   B N   
396  C  CA  . MET   B 17  ? 0.7547 0.5060 0.5424 0.1187  0.0625  0.0410  26  MET   B CA  
397  C  C   . MET   B 17  ? 0.8008 0.5364 0.5869 0.1044  0.0619  0.0344  26  MET   B C   
398  O  O   . MET   B 17  ? 0.8016 0.5423 0.5912 0.1061  0.0590  0.0228  26  MET   B O   
399  C  CB  . MET   B 17  ? 0.7692 0.4958 0.5408 0.1366  0.0624  0.0421  26  MET   B CB  
400  C  CG  . MET   B 17  ? 0.7766 0.5159 0.5465 0.1542  0.0608  0.0461  26  MET   B CG  
401  S  SD  . MET   B 17  ? 0.8001 0.5431 0.5645 0.1503  0.0674  0.0640  26  MET   B SD  
402  C  CE  . MET   B 17  ? 0.7429 0.4439 0.4878 0.1446  0.0734  0.0734  26  MET   B CE  
403  N  N   . THR   B 18  ? 0.8407 0.5547 0.6198 0.0908  0.0645  0.0416  27  THR   B N   
404  C  CA  . THR   B 18  ? 0.8831 0.5756 0.6570 0.0775  0.0621  0.0346  27  THR   B CA  
405  C  C   . THR   B 18  ? 0.9359 0.5862 0.6918 0.0725  0.0639  0.0412  27  THR   B C   
406  O  O   . THR   B 18  ? 0.9385 0.5852 0.6936 0.0654  0.0687  0.0553  27  THR   B O   
407  C  CB  . THR   B 18  ? 0.8932 0.6083 0.6818 0.0581  0.0602  0.0332  27  THR   B CB  
408  O  OG1 . THR   B 18  ? 0.9262 0.6193 0.7071 0.0485  0.0558  0.0234  27  THR   B OG1 
409  C  CG2 . THR   B 18  ? 0.8903 0.6167 0.6879 0.0429  0.0638  0.0470  27  THR   B CG2 
410  N  N   . ARG   B 19  ? 0.9755 0.5928 0.7152 0.0775  0.0604  0.0315  28  ARG   B N   
411  C  CA  . ARG   B 19  ? 1.0306 0.6004 0.7493 0.0720  0.0606  0.0364  28  ARG   B CA  
412  C  C   . ARG   B 19  ? 1.0515 0.6043 0.7698 0.0475  0.0563  0.0325  28  ARG   B C   
413  O  O   . ARG   B 19  ? 1.0725 0.5797 0.7706 0.0428  0.0536  0.0313  28  ARG   B O   
414  C  CB  . ARG   B 19  ? 1.0840 0.6214 0.7801 0.0954  0.0586  0.0289  28  ARG   B CB  
415  C  CG  . ARG   B 19  ? 1.1539 0.6985 0.8463 0.1175  0.0617  0.0355  28  ARG   B CG  
416  C  CD  . ARG   B 19  ? 1.2477 0.7572 0.9157 0.1406  0.0590  0.0296  28  ARG   B CD  
417  N  NE  . ARG   B 19  ? 1.3145 0.8432 0.9845 0.1650  0.0590  0.0300  28  ARG   B NE  
418  C  CZ  . ARG   B 19  ? 1.3548 0.9078 1.0340 0.1827  0.0555  0.0174  28  ARG   B CZ  
419  N  NH1 . ARG   B 19  ? 1.3555 0.9166 1.0411 0.1799  0.0535  0.0042  28  ARG   B NH1 
420  N  NH2 . ARG   B 19  ? 1.3480 0.9183 1.0300 0.2031  0.0539  0.0179  28  ARG   B NH2 
421  N  N   . ARG   B 20  ? 1.0457 0.6338 0.7850 0.0325  0.0546  0.0303  29  ARG   B N   
422  C  CA  . ARG   B 20  ? 1.0679 0.6485 0.8104 0.0094  0.0486  0.0253  29  ARG   B CA  
423  C  C   . ARG   B 20  ? 1.0723 0.6498 0.8235 -0.0149 0.0510  0.0399  29  ARG   B C   
424  O  O   . ARG   B 20  ? 1.0890 0.6440 0.8370 -0.0353 0.0451  0.0373  29  ARG   B O   
425  C  CB  . ARG   B 20  ? 1.0771 0.6979 0.8365 0.0069  0.0451  0.0160  29  ARG   B CB  
426  C  CG  . ARG   B 20  ? 1.1426 0.7569 0.9034 -0.0138 0.0368  0.0082  29  ARG   B CG  
427  C  CD  . ARG   B 20  ? 1.1867 0.8420 0.9630 -0.0160 0.0337  0.0016  29  ARG   B CD  
428  N  NE  . ARG   B 20  ? 1.2202 0.9188 1.0181 -0.0164 0.0389  0.0128  29  ARG   B NE  
429  C  CZ  . ARG   B 20  ? 1.2417 0.9631 1.0573 -0.0341 0.0384  0.0215  29  ARG   B CZ  
430  N  NH1 . ARG   B 20  ? 1.2452 0.9516 1.0623 -0.0558 0.0325  0.0207  29  ARG   B NH1 
431  N  NH2 . ARG   B 20  ? 1.2236 0.9837 1.0556 -0.0301 0.0433  0.0306  29  ARG   B NH2 
432  N  N   . LEU   B 21  ? 1.0531 0.6534 0.8149 -0.0130 0.0593  0.0553  30  LEU   B N   
433  C  CA  . LEU   B 21  ? 1.0483 0.6493 0.8192 -0.0349 0.0642  0.0714  30  LEU   B CA  
434  C  C   . LEU   B 21  ? 1.0564 0.6135 0.8043 -0.0292 0.0704  0.0832  30  LEU   B C   
435  O  O   . LEU   B 21  ? 1.0832 0.6016 0.8068 -0.0129 0.0673  0.0754  30  LEU   B O   
436  C  CB  . LEU   B 21  ? 1.0301 0.6871 0.8267 -0.0368 0.0703  0.0816  30  LEU   B CB  
437  C  CG  . LEU   B 21  ? 1.0370 0.7376 0.8554 -0.0432 0.0645  0.0728  30  LEU   B CG  
438  C  CD1 . LEU   B 21  ? 1.0511 0.7375 0.8710 -0.0634 0.0542  0.0613  30  LEU   B CD1 
439  C  CD2 . LEU   B 21  ? 1.0450 0.7649 0.8619 -0.0198 0.0630  0.0629  30  LEU   B CD2 
440  N  N   . LEU   B 22  ? 1.0300 0.5920 0.7840 -0.0420 0.0793  0.1022  31  LEU   B N   
441  C  CA  . LEU   B 22  ? 1.0364 0.5576 0.7670 -0.0368 0.0864  0.1159  31  LEU   B CA  
442  C  C   . LEU   B 22  ? 1.0367 0.5639 0.7547 -0.0036 0.0903  0.1164  31  LEU   B C   
443  O  O   . LEU   B 22  ? 1.0256 0.5989 0.7600 0.0063  0.0936  0.1182  31  LEU   B O   
444  C  CB  . LEU   B 22  ? 1.0178 0.5552 0.7624 -0.0583 0.0968  0.1371  31  LEU   B CB  
445  C  CG  . LEU   B 22  ? 1.0453 0.5355 0.7648 -0.0600 0.1049  0.1537  31  LEU   B CG  
446  C  CD1 . LEU   B 22  ? 1.0671 0.4995 0.7701 -0.0801 0.0976  0.1498  31  LEU   B CD1 
447  C  CD2 . LEU   B 22  ? 1.0339 0.5544 0.7681 -0.0720 0.1190  0.1765  31  LEU   B CD2 
448  N  N   . GLY   B 23  ? 1.0431 0.5240 0.7316 0.0143  0.0885  0.1135  32  GLY   B N   
449  C  CA  . GLY   B 23  ? 1.0325 0.5171 0.7085 0.0465  0.0897  0.1117  32  GLY   B CA  
450  C  C   . GLY   B 23  ? 0.9950 0.5221 0.6885 0.0614  0.0842  0.0963  32  GLY   B C   
451  O  O   . GLY   B 23  ? 0.9840 0.5214 0.6889 0.0530  0.0777  0.0827  32  GLY   B O   
452  N  N   . SER   B 24  ? 0.9719 0.5231 0.6666 0.0831  0.0864  0.0986  33  SER   B N   
453  C  CA  . SER   B 24  ? 0.9400 0.5318 0.6521 0.0952  0.0815  0.0859  33  SER   B CA  
454  C  C   . SER   B 24  ? 0.8903 0.5256 0.6231 0.0866  0.0861  0.0947  33  SER   B C   
455  O  O   . SER   B 24  ? 0.8917 0.5302 0.6190 0.0904  0.0932  0.1093  33  SER   B O   
456  C  CB  . SER   B 24  ? 0.9748 0.5641 0.6750 0.1250  0.0786  0.0810  33  SER   B CB  
457  O  OG  . SER   B 24  ? 1.0375 0.5879 0.7176 0.1360  0.0745  0.0730  33  SER   B OG  
458  N  N   . THR   B 25  ? 0.8490 0.5166 0.6031 0.0761  0.0824  0.0864  34  THR   B N   
459  C  CA  . THR   B 25  ? 0.8071 0.5160 0.5801 0.0687  0.0859  0.0936  34  THR   B CA  
460  C  C   . THR   B 25  ? 0.7706 0.5126 0.5545 0.0822  0.0808  0.0837  34  THR   B C   
461  O  O   . THR   B 25  ? 0.7697 0.5149 0.5590 0.0817  0.0746  0.0701  34  THR   B O   
462  C  CB  . THR   B 25  ? 0.8075 0.5251 0.5957 0.0412  0.0858  0.0951  34  THR   B CB  
463  O  OG1 . THR   B 25  ? 0.8344 0.5203 0.6131 0.0263  0.0904  0.1058  34  THR   B OG1 
464  C  CG2 . THR   B 25  ? 0.7814 0.5451 0.5902 0.0349  0.0887  0.1016  34  THR   B CG2 
465  N  N   . GLN   B 26  ? 0.7347 0.5001 0.5205 0.0942  0.0836  0.0909  35  GLN   B N   
466  C  CA  . GLN   B 26  ? 0.7019 0.4950 0.4966 0.1053  0.0780  0.0823  35  GLN   B CA  
467  C  C   . GLN   B 26  ? 0.6878 0.5107 0.5004 0.0906  0.0769  0.0807  35  GLN   B C   
468  O  O   . GLN   B 26  ? 0.6842 0.5271 0.5036 0.0844  0.0819  0.0913  35  GLN   B O   
469  C  CB  . GLN   B 26  ? 0.6820 0.4847 0.4684 0.1256  0.0791  0.0883  35  GLN   B CB  
470  C  CG  . GLN   B 26  ? 0.6528 0.4779 0.4462 0.1365  0.0715  0.0785  35  GLN   B CG  
471  C  CD  . GLN   B 26  ? 0.6643 0.4933 0.4464 0.1578  0.0698  0.0817  35  GLN   B CD  
472  O  OE1 . GLN   B 26  ? 0.6756 0.4851 0.4432 0.1709  0.0700  0.0840  35  GLN   B OE1 
473  N  NE2 . GLN   B 26  ? 0.6508 0.5031 0.4369 0.1636  0.0670  0.0813  35  GLN   B NE2 
474  N  N   . VAL   B 27  ? 0.6705 0.4979 0.4900 0.0865  0.0706  0.0679  36  VAL   B N   
475  C  CA  . VAL   B 27  ? 0.6534 0.5066 0.4866 0.0752  0.0680  0.0650  36  VAL   B CA  
476  C  C   . VAL   B 27  ? 0.6319 0.5087 0.4681 0.0880  0.0642  0.0619  36  VAL   B C   
477  O  O   . VAL   B 27  ? 0.6173 0.5168 0.4620 0.0826  0.0624  0.0619  36  VAL   B O   
478  C  CB  . VAL   B 27  ? 0.6644 0.5077 0.5002 0.0623  0.0636  0.0539  36  VAL   B CB  
479  C  CG1 . VAL   B 27  ? 0.6815 0.5017 0.5140 0.0470  0.0656  0.0571  36  VAL   B CG1 
480  C  CG2 . VAL   B 27  ? 0.6705 0.5014 0.4998 0.0735  0.0600  0.0421  36  VAL   B CG2 
481  N  N   . GLY   B 28  ? 0.6203 0.4903 0.4489 0.1047  0.0620  0.0588  37  GLY   B N   
482  C  CA  . GLY   B 28  ? 0.6065 0.4924 0.4360 0.1157  0.0568  0.0550  37  GLY   B CA  
483  C  C   . GLY   B 28  ? 0.6067 0.4824 0.4294 0.1317  0.0526  0.0499  37  GLY   B C   
484  O  O   . GLY   B 28  ? 0.6130 0.4713 0.4289 0.1376  0.0542  0.0506  37  GLY   B O   
485  N  N   . VAL   B 29  ? 0.5989 0.4849 0.4230 0.1387  0.0463  0.0445  38  VAL   B N   
486  C  CA  . VAL   B 29  ? 0.6028 0.4849 0.4233 0.1528  0.0397  0.0389  38  VAL   B CA  
487  C  C   . VAL   B 29  ? 0.5932 0.4815 0.4217 0.1478  0.0340  0.0294  38  VAL   B C   
488  O  O   . VAL   B 29  ? 0.6054 0.5015 0.4379 0.1372  0.0348  0.0289  38  VAL   B O   
489  C  CB  . VAL   B 29  ? 0.6220 0.5092 0.4317 0.1678  0.0374  0.0449  38  VAL   B CB  
490  C  CG1 . VAL   B 29  ? 0.6350 0.5175 0.4403 0.1821  0.0279  0.0378  38  VAL   B CG1 
491  C  CG2 . VAL   B 29  ? 0.6328 0.5150 0.4334 0.1725  0.0453  0.0565  38  VAL   B CG2 
492  N  N   . GLY   B 30  ? 0.5757 0.4615 0.4069 0.1551  0.0282  0.0223  39  GLY   B N   
493  C  CA  . GLY   B 30  ? 0.5669 0.4588 0.4068 0.1494  0.0234  0.0145  39  GLY   B CA  
494  C  C   . GLY   B 30  ? 0.5677 0.4604 0.4104 0.1592  0.0145  0.0086  39  GLY   B C   
495  O  O   . GLY   B 30  ? 0.5807 0.4686 0.4179 0.1724  0.0113  0.0091  39  GLY   B O   
496  N  N   . VAL   B 31  ? 0.5576 0.4558 0.4079 0.1525  0.0097  0.0033  40  VAL   B N   
497  C  CA  . VAL   B 31  ? 0.5570 0.4572 0.4128 0.1581  -0.0005 -0.0030 40  VAL   B CA  
498  C  C   . VAL   B 31  ? 0.5572 0.4677 0.4312 0.1495  0.0011  -0.0097 40  VAL   B C   
499  O  O   . VAL   B 31  ? 0.5561 0.4706 0.4352 0.1366  0.0068  -0.0095 40  VAL   B O   
500  C  CB  . VAL   B 31  ? 0.5581 0.4541 0.4067 0.1564  -0.0085 -0.0030 40  VAL   B CB  
501  C  CG1 . VAL   B 31  ? 0.5502 0.4471 0.4071 0.1570  -0.0202 -0.0106 40  VAL   B CG1 
502  C  CG2 . VAL   B 31  ? 0.5697 0.4587 0.3995 0.1687  -0.0102 0.0031  40  VAL   B CG2 
503  N  N   . MET   B 32  ? 0.5565 0.4733 0.4401 0.1576  -0.0040 -0.0154 41  MET   B N   
504  C  CA  . MET   B 32  ? 0.5518 0.4843 0.4556 0.1508  -0.0025 -0.0219 41  MET   B CA  
505  C  C   . MET   B 32  ? 0.5674 0.5068 0.4817 0.1467  -0.0140 -0.0266 41  MET   B C   
506  O  O   . MET   B 32  ? 0.5738 0.5090 0.4836 0.1578  -0.0253 -0.0293 41  MET   B O   
507  C  CB  . MET   B 32  ? 0.5385 0.4760 0.4474 0.1632  -0.0012 -0.0257 41  MET   B CB  
508  C  CG  . MET   B 32  ? 0.5394 0.4972 0.4693 0.1587  0.0023  -0.0321 41  MET   B CG  
509  S  SD  . MET   B 32  ? 0.6040 0.5628 0.5336 0.1456  0.0176  -0.0300 41  MET   B SD  
510  C  CE  . MET   B 32  ? 0.5960 0.5354 0.5079 0.1582  0.0231  -0.0280 41  MET   B CE  
511  N  N   . GLN   B 33  ? 0.5693 0.5160 0.4946 0.1303  -0.0117 -0.0271 42  GLN   B N   
512  C  CA  . GLN   B 33  ? 0.5753 0.5258 0.5111 0.1227  -0.0226 -0.0310 42  GLN   B CA  
513  C  C   . GLN   B 33  ? 0.5735 0.5420 0.5304 0.1055  -0.0158 -0.0321 42  GLN   B C   
514  O  O   . GLN   B 33  ? 0.5793 0.5449 0.5309 0.0956  -0.0049 -0.0271 42  GLN   B O   
515  C  CB  . GLN   B 33  ? 0.6089 0.5378 0.5251 0.1207  -0.0298 -0.0274 42  GLN   B CB  
516  C  CG  . GLN   B 33  ? 0.6725 0.5996 0.5970 0.1138  -0.0437 -0.0326 42  GLN   B CG  
517  C  CD  . GLN   B 33  ? 0.7630 0.6642 0.6642 0.1159  -0.0534 -0.0306 42  GLN   B CD  
518  O  OE1 . GLN   B 33  ? 0.7867 0.6773 0.6860 0.1020  -0.0562 -0.0293 42  GLN   B OE1 
519  N  NE2 . GLN   B 33  ? 0.7796 0.6690 0.6607 0.1344  -0.0584 -0.0300 42  GLN   B NE2 
520  N  N   . GLU   B 34  ? 0.5618 0.5504 0.5426 0.1022  -0.0221 -0.0383 43  GLU   B N   
521  C  CA  . GLU   B 34  ? 0.5529 0.5647 0.5579 0.0858  -0.0147 -0.0388 43  GLU   B CA  
522  C  C   . GLU   B 34  ? 0.5539 0.5788 0.5618 0.0867  0.0024  -0.0368 43  GLU   B C   
523  O  O   . GLU   B 34  ? 0.5670 0.5987 0.5794 0.0729  0.0131  -0.0330 43  GLU   B O   
524  C  CB  . GLU   B 34  ? 0.5815 0.5810 0.5831 0.0663  -0.0161 -0.0340 43  GLU   B CB  
525  C  CG  . GLU   B 34  ? 0.6233 0.6088 0.6230 0.0641  -0.0345 -0.0375 43  GLU   B CG  
526  C  CD  . GLU   B 34  ? 0.7077 0.6650 0.6885 0.0514  -0.0372 -0.0317 43  GLU   B CD  
527  O  OE1 . GLU   B 34  ? 0.6990 0.6595 0.6851 0.0340  -0.0273 -0.0262 43  GLU   B OE1 
528  O  OE2 . GLU   B 34  ? 0.7760 0.7072 0.7344 0.0603  -0.0490 -0.0324 43  GLU   B OE2 
529  N  N   . GLY   B 35  ? 0.5433 0.5696 0.5465 0.1037  0.0047  -0.0396 44  GLY   B N   
530  C  CA  . GLY   B 35  ? 0.5305 0.5644 0.5328 0.1077  0.0188  -0.0395 44  GLY   B CA  
531  C  C   . GLY   B 35  ? 0.5342 0.5464 0.5129 0.1032  0.0278  -0.0332 44  GLY   B C   
532  O  O   . GLY   B 35  ? 0.5333 0.5498 0.5096 0.1031  0.0393  -0.0333 44  GLY   B O   
533  N  N   . VAL   B 36  ? 0.5337 0.5231 0.4943 0.1005  0.0220  -0.0284 45  VAL   B N   
534  C  CA  . VAL   B 36  ? 0.5400 0.5118 0.4800 0.0960  0.0286  -0.0227 45  VAL   B CA  
535  C  C   . VAL   B 36  ? 0.5344 0.4876 0.4564 0.1068  0.0242  -0.0202 45  VAL   B C   
536  O  O   . VAL   B 36  ? 0.5422 0.4887 0.4604 0.1130  0.0142  -0.0198 45  VAL   B O   
537  C  CB  . VAL   B 36  ? 0.5584 0.5239 0.4935 0.0810  0.0284  -0.0180 45  VAL   B CB  
538  C  CG1 . VAL   B 36  ? 0.5805 0.5286 0.4931 0.0791  0.0325  -0.0126 45  VAL   B CG1 
539  C  CG2 . VAL   B 36  ? 0.5523 0.5363 0.5036 0.0686  0.0365  -0.0183 45  VAL   B CG2 
540  N  N   . PHE   B 37  ? 0.5151 0.4604 0.4262 0.1096  0.0315  -0.0186 46  PHE   B N   
541  C  CA  . PHE   B 37  ? 0.5232 0.4531 0.4191 0.1169  0.0292  -0.0145 46  PHE   B CA  
542  C  C   . PHE   B 37  ? 0.5104 0.4323 0.3938 0.1088  0.0297  -0.0090 46  PHE   B C   
543  O  O   . PHE   B 37  ? 0.5013 0.4242 0.3823 0.0997  0.0356  -0.0087 46  PHE   B O   
544  C  CB  . PHE   B 37  ? 0.5323 0.4554 0.4228 0.1226  0.0354  -0.0154 46  PHE   B CB  
545  C  CG  . PHE   B 37  ? 0.5473 0.4560 0.4250 0.1299  0.0333  -0.0102 46  PHE   B CG  
546  C  CD1 . PHE   B 37  ? 0.5550 0.4614 0.4315 0.1423  0.0269  -0.0095 46  PHE   B CD1 
547  C  CD2 . PHE   B 37  ? 0.5618 0.4603 0.4288 0.1241  0.0379  -0.0057 46  PHE   B CD2 
548  C  CE1 . PHE   B 37  ? 0.5702 0.4639 0.4337 0.1491  0.0270  -0.0032 46  PHE   B CE1 
549  C  CE2 . PHE   B 37  ? 0.5724 0.4607 0.4299 0.1289  0.0374  0.0006  46  PHE   B CE2 
550  C  CZ  . PHE   B 37  ? 0.5741 0.4596 0.4292 0.1415  0.0330  0.0024  46  PHE   B CZ  
551  N  N   . HIS   B 38  ? 0.5131 0.4280 0.3876 0.1138  0.0233  -0.0051 47  HIS   B N   
552  C  CA  . HIS   B 38  ? 0.5118 0.4212 0.3742 0.1095  0.0225  0.0000  47  HIS   B CA  
553  C  C   . HIS   B 38  ? 0.5301 0.4357 0.3835 0.1158  0.0238  0.0051  47  HIS   B C   
554  O  O   . HIS   B 38  ? 0.5428 0.4459 0.3940 0.1263  0.0208  0.0065  47  HIS   B O   
555  C  CB  . HIS   B 38  ? 0.5013 0.4061 0.3592 0.1120  0.0131  0.0004  47  HIS   B CB  
556  C  CG  . HIS   B 38  ? 0.5177 0.4258 0.3868 0.1052  0.0098  -0.0040 47  HIS   B CG  
557  N  ND1 . HIS   B 38  ? 0.5237 0.4401 0.4074 0.1091  0.0066  -0.0092 47  HIS   B ND1 
558  C  CD2 . HIS   B 38  ? 0.5390 0.4432 0.4066 0.0948  0.0085  -0.0032 47  HIS   B CD2 
559  C  CE1 . HIS   B 38  ? 0.5252 0.4458 0.4191 0.0992  0.0039  -0.0116 47  HIS   B CE1 
560  N  NE2 . HIS   B 38  ? 0.5397 0.4516 0.4237 0.0896  0.0056  -0.0076 47  HIS   B NE2 
561  N  N   . THR   B 39  ? 0.5336 0.4397 0.3815 0.1094  0.0281  0.0083  48  THR   B N   
562  C  CA  . THR   B 39  ? 0.5385 0.4450 0.3810 0.1124  0.0299  0.0141  48  THR   B CA  
563  C  C   . THR   B 39  ? 0.5405 0.4526 0.3773 0.1062  0.0300  0.0172  48  THR   B C   
564  O  O   . THR   B 39  ? 0.5374 0.4491 0.3707 0.1021  0.0278  0.0153  48  THR   B O   
565  C  CB  . THR   B 39  ? 0.5515 0.4528 0.3972 0.1115  0.0354  0.0138  48  THR   B CB  
566  O  OG1 . THR   B 39  ? 0.5660 0.4678 0.4076 0.1133  0.0373  0.0212  48  THR   B OG1 
567  C  CG2 . THR   B 39  ? 0.5474 0.4465 0.3951 0.1009  0.0399  0.0093  48  THR   B CG2 
568  N  N   . MET   B 40  ? 0.5414 0.4595 0.3773 0.1058  0.0322  0.0225  49  MET   B N   
569  C  CA  . MET   B 40  ? 0.5491 0.4769 0.3821 0.1009  0.0315  0.0250  49  MET   B CA  
570  C  C   . MET   B 40  ? 0.5613 0.4883 0.3977 0.0885  0.0347  0.0217  49  MET   B C   
571  O  O   . MET   B 40  ? 0.5732 0.4931 0.4138 0.0846  0.0384  0.0205  49  MET   B O   
572  C  CB  . MET   B 40  ? 0.5548 0.4950 0.3877 0.1073  0.0320  0.0328  49  MET   B CB  
573  C  CG  . MET   B 40  ? 0.5913 0.5297 0.4170 0.1225  0.0285  0.0351  49  MET   B CG  
574  S  SD  . MET   B 40  ? 0.6696 0.6244 0.4871 0.1342  0.0255  0.0412  49  MET   B SD  
575  C  CE  . MET   B 40  ? 0.6432 0.5898 0.4506 0.1340  0.0181  0.0357  49  MET   B CE  
576  N  N   . TRP   B 41  ? 0.5632 0.4946 0.3950 0.0832  0.0325  0.0198  50  TRP   B N   
577  C  CA  A TRP   B 41  ? 0.5762 0.5056 0.4081 0.0726  0.0340  0.0153  50  TRP   B CA  
578  C  CA  B TRP   B 41  ? 0.5670 0.4966 0.3988 0.0726  0.0340  0.0154  50  TRP   B CA  
579  C  C   . TRP   B 41  ? 0.5771 0.5108 0.4161 0.0657  0.0352  0.0177  50  TRP   B C   
580  O  O   . TRP   B 41  ? 0.5840 0.5067 0.4232 0.0585  0.0371  0.0133  50  TRP   B O   
581  C  CB  A TRP   B 41  ? 0.5828 0.5167 0.4057 0.0701  0.0304  0.0134  50  TRP   B CB  
582  C  CB  B TRP   B 41  ? 0.5605 0.4952 0.3834 0.0703  0.0302  0.0137  50  TRP   B CB  
583  C  CG  A TRP   B 41  ? 0.5957 0.5245 0.4147 0.0611  0.0312  0.0072  50  TRP   B CG  
584  C  CG  B TRP   B 41  ? 0.5536 0.4852 0.3736 0.0609  0.0304  0.0081  50  TRP   B CG  
585  C  CD1 A TRP   B 41  ? 0.6117 0.5292 0.4243 0.0593  0.0347  0.0018  50  TRP   B CD1 
586  C  CD1 B TRP   B 41  ? 0.5542 0.4932 0.3786 0.0533  0.0278  0.0074  50  TRP   B CD1 
587  C  CD2 A TRP   B 41  ? 0.5963 0.5314 0.4175 0.0531  0.0282  0.0055  50  TRP   B CD2 
588  C  CD2 B TRP   B 41  ? 0.5536 0.4735 0.3657 0.0580  0.0333  0.0018  50  TRP   B CD2 
589  N  NE1 A TRP   B 41  ? 0.6195 0.5334 0.4268 0.0526  0.0339  -0.0038 50  TRP   B NE1 
590  N  NE1 B TRP   B 41  ? 0.5588 0.4878 0.3764 0.0466  0.0275  0.0001  50  TRP   B NE1 
591  C  CE2 A TRP   B 41  ? 0.6128 0.5362 0.4256 0.0478  0.0289  -0.0021 50  TRP   B CE2 
592  C  CE2 B TRP   B 41  ? 0.5612 0.4790 0.3702 0.0505  0.0316  -0.0032 50  TRP   B CE2 
593  C  CE3 A TRP   B 41  ? 0.5970 0.5481 0.4273 0.0495  0.0248  0.0096  50  TRP   B CE3 
594  C  CE3 B TRP   B 41  ? 0.5617 0.4740 0.3698 0.0608  0.0374  0.0002  50  TRP   B CE3 
595  C  CZ2 A TRP   B 41  ? 0.6258 0.5495 0.4369 0.0392  0.0246  -0.0068 50  TRP   B CZ2 
596  C  CZ2 B TRP   B 41  ? 0.5731 0.4799 0.3715 0.0483  0.0340  -0.0102 50  TRP   B CZ2 
597  C  CZ3 A TRP   B 41  ? 0.6082 0.5626 0.4407 0.0388  0.0209  0.0055  50  TRP   B CZ3 
598  C  CZ3 B TRP   B 41  ? 0.5775 0.4828 0.3774 0.0576  0.0412  -0.0054 50  TRP   B CZ3 
599  C  CH2 A TRP   B 41  ? 0.6189 0.5581 0.4408 0.0339  0.0198  -0.0031 50  TRP   B CH2 
600  C  CH2 B TRP   B 41  ? 0.5779 0.4798 0.3717 0.0527  0.0397  -0.0108 50  TRP   B CH2 
601  N  N   . HIS   B 42  ? 0.5767 0.5262 0.4210 0.0674  0.0342  0.0246  51  HIS   B N   
602  C  CA  . HIS   B 42  ? 0.5840 0.5399 0.4376 0.0577  0.0359  0.0283  51  HIS   B CA  
603  C  C   . HIS   B 42  ? 0.6028 0.5423 0.4584 0.0565  0.0412  0.0308  51  HIS   B C   
604  O  O   . HIS   B 42  ? 0.6045 0.5415 0.4657 0.0457  0.0428  0.0333  51  HIS   B O   
605  C  CB  . HIS   B 42  ? 0.5708 0.5531 0.4318 0.0599  0.0350  0.0362  51  HIS   B CB  
606  C  CG  . HIS   B 42  ? 0.5918 0.5790 0.4530 0.0721  0.0389  0.0441  51  HIS   B CG  
607  N  ND1 . HIS   B 42  ? 0.6158 0.6059 0.4681 0.0873  0.0363  0.0447  51  HIS   B ND1 
608  C  CD2 . HIS   B 42  ? 0.5947 0.5816 0.4609 0.0716  0.0449  0.0517  51  HIS   B CD2 
609  C  CE1 . HIS   B 42  ? 0.6102 0.6031 0.4624 0.0965  0.0402  0.0516  51  HIS   B CE1 
610  N  NE2 . HIS   B 42  ? 0.6034 0.5951 0.4635 0.0878  0.0461  0.0566  51  HIS   B NE2 
611  N  N   . VAL   B 43  ? 0.6079 0.5353 0.4586 0.0671  0.0431  0.0299  52  VAL   B N   
612  C  CA  . VAL   B 43  ? 0.6171 0.5274 0.4665 0.0693  0.0471  0.0316  52  VAL   B CA  
613  C  C   . VAL   B 43  ? 0.6325 0.5229 0.4782 0.0624  0.0474  0.0234  52  VAL   B C   
614  O  O   . VAL   B 43  ? 0.6425 0.5189 0.4872 0.0552  0.0492  0.0248  52  VAL   B O   
615  C  CB  . VAL   B 43  ? 0.6247 0.5315 0.4703 0.0848  0.0471  0.0324  52  VAL   B CB  
616  C  CG1 . VAL   B 43  ? 0.6374 0.5248 0.4795 0.0896  0.0498  0.0317  52  VAL   B CG1 
617  C  CG2 . VAL   B 43  ? 0.6216 0.5433 0.4668 0.0937  0.0470  0.0407  52  VAL   B CG2 
618  N  N   . THR   B 44  ? 0.6271 0.5153 0.4693 0.0646  0.0459  0.0151  53  THR   B N   
619  C  CA  . THR   B 44  ? 0.6258 0.4969 0.4623 0.0619  0.0469  0.0067  53  THR   B CA  
620  C  C   . THR   B 44  ? 0.6349 0.5056 0.4671 0.0514  0.0442  0.0008  53  THR   B C   
621  O  O   . THR   B 44  ? 0.6407 0.4943 0.4655 0.0487  0.0444  -0.0062 53  THR   B O   
622  C  CB  . THR   B 44  ? 0.6172 0.4878 0.4530 0.0718  0.0485  0.0013  53  THR   B CB  
623  O  OG1 . THR   B 44  ? 0.6076 0.4911 0.4433 0.0704  0.0471  -0.0003 53  THR   B OG1 
624  C  CG2 . THR   B 44  ? 0.6265 0.4985 0.4663 0.0832  0.0488  0.0053  53  THR   B CG2 
625  N  N   . LYS   B 45  ? 0.6320 0.5205 0.4665 0.0475  0.0408  0.0029  54  LYS   B N   
626  C  CA  . LYS   B 45  ? 0.6451 0.5366 0.4736 0.0404  0.0369  -0.0030 54  LYS   B CA  
627  C  C   . LYS   B 45  ? 0.6451 0.5281 0.4632 0.0452  0.0394  -0.0107 54  LYS   B C   
628  O  O   . LYS   B 45  ? 0.6544 0.5313 0.4629 0.0409  0.0374  -0.0175 54  LYS   B O   
629  C  CB  . LYS   B 45  ? 0.6875 0.5706 0.5157 0.0279  0.0330  -0.0059 54  LYS   B CB  
630  C  CG  . LYS   B 45  ? 0.7583 0.6477 0.5984 0.0206  0.0328  0.0026  54  LYS   B CG  
631  C  CD  . LYS   B 45  ? 0.8236 0.7423 0.6741 0.0198  0.0305  0.0096  54  LYS   B CD  
632  C  CE  . LYS   B 45  ? 0.8920 0.8181 0.7553 0.0113  0.0323  0.0187  54  LYS   B CE  
633  N  NZ  . LYS   B 45  ? 0.9239 0.8780 0.7967 0.0182  0.0344  0.0284  54  LYS   B NZ  
634  N  N   . GLY   B 46  ? 0.6364 0.5202 0.4568 0.0540  0.0437  -0.0098 55  GLY   B N   
635  C  CA  . GLY   B 46  ? 0.6444 0.5251 0.4588 0.0580  0.0479  -0.0154 55  GLY   B CA  
636  C  C   . GLY   B 46  ? 0.6591 0.5254 0.4695 0.0613  0.0516  -0.0223 55  GLY   B C   
637  O  O   . GLY   B 46  ? 0.6632 0.5298 0.4688 0.0654  0.0563  -0.0273 55  GLY   B O   
638  N  N   . ALA   B 47  ? 0.6667 0.5195 0.4778 0.0605  0.0501  -0.0223 56  ALA   B N   
639  C  CA  . ALA   B 47  ? 0.6830 0.5170 0.4866 0.0658  0.0526  -0.0291 56  ALA   B CA  
640  C  C   . ALA   B 47  ? 0.6966 0.5347 0.5069 0.0783  0.0573  -0.0295 56  ALA   B C   
641  O  O   . ALA   B 47  ? 0.6960 0.5474 0.5175 0.0812  0.0572  -0.0236 56  ALA   B O   
642  C  CB  . ALA   B 47  ? 0.6861 0.5003 0.4863 0.0600  0.0489  -0.0278 56  ALA   B CB  
643  N  N   . ALA   B 48  ? 0.7081 0.5355 0.5113 0.0868  0.0605  -0.0370 57  ALA   B N   
644  C  CA  . ALA   B 48  ? 0.7126 0.5472 0.5237 0.0998  0.0643  -0.0384 57  ALA   B CA  
645  C  C   . ALA   B 48  ? 0.7289 0.5532 0.5433 0.1054  0.0615  -0.0337 57  ALA   B C   
646  O  O   . ALA   B 48  ? 0.7434 0.5470 0.5493 0.1008  0.0586  -0.0311 57  ALA   B O   
647  C  CB  . ALA   B 48  ? 0.7163 0.5436 0.5175 0.1097  0.0686  -0.0481 57  ALA   B CB  
648  N  N   . LEU   B 49  ? 0.7252 0.5639 0.5515 0.1148  0.0621  -0.0322 58  LEU   B N   
649  C  CA  . LEU   B 49  ? 0.7382 0.5683 0.5655 0.1230  0.0593  -0.0277 58  LEU   B CA  
650  C  C   . LEU   B 49  ? 0.7595 0.5871 0.5863 0.1398  0.0605  -0.0341 58  LEU   B C   
651  O  O   . LEU   B 49  ? 0.7595 0.6020 0.5919 0.1449  0.0640  -0.0409 58  LEU   B O   
652  C  CB  . LEU   B 49  ? 0.7210 0.5693 0.5607 0.1222  0.0563  -0.0210 58  LEU   B CB  
653  C  CG  . LEU   B 49  ? 0.7209 0.5747 0.5610 0.1093  0.0547  -0.0146 58  LEU   B CG  
654  C  CD1 . LEU   B 49  ? 0.7123 0.5818 0.5615 0.1119  0.0513  -0.0100 58  LEU   B CD1 
655  C  CD2 . LEU   B 49  ? 0.7331 0.5696 0.5643 0.1030  0.0540  -0.0090 58  LEU   B CD2 
656  N  N   . ARG   B 50  ? 0.7763 0.5856 0.5956 0.1491  0.0580  -0.0315 59  ARG   B N   
657  C  CA  . ARG   B 50  ? 0.7961 0.6011 0.6126 0.1678  0.0578  -0.0373 59  ARG   B CA  
658  C  C   . ARG   B 50  ? 0.7981 0.6141 0.6237 0.1782  0.0535  -0.0332 59  ARG   B C   
659  O  O   . ARG   B 50  ? 0.7953 0.6052 0.6185 0.1732  0.0511  -0.0246 59  ARG   B O   
660  C  CB  . ARG   B 50  ? 0.8435 0.6094 0.6368 0.1721  0.0576  -0.0385 59  ARG   B CB  
661  C  CG  . ARG   B 50  ? 0.9075 0.6619 0.6924 0.1942  0.0564  -0.0436 59  ARG   B CG  
662  C  CD  . ARG   B 50  ? 0.9887 0.6996 0.7468 0.1983  0.0559  -0.0463 59  ARG   B CD  
663  N  NE  . ARG   B 50  ? 1.0494 0.7300 0.7948 0.1837  0.0544  -0.0367 59  ARG   B NE  
664  C  CZ  . ARG   B 50  ? 1.0934 0.7566 0.8311 0.1879  0.0528  -0.0275 59  ARG   B CZ  
665  N  NH1 . ARG   B 50  ? 1.0808 0.7532 0.8210 0.2074  0.0510  -0.0274 59  ARG   B NH1 
666  N  NH2 . ARG   B 50  ? 1.1137 0.7522 0.8416 0.1726  0.0531  -0.0179 59  ARG   B NH2 
667  N  N   . SER   B 51  ? 0.8007 0.6363 0.6377 0.1926  0.0522  -0.0394 60  SER   B N   
668  C  CA  . SER   B 51  ? 0.8215 0.6670 0.6658 0.2045  0.0459  -0.0375 60  SER   B CA  
669  C  C   . SER   B 51  ? 0.8579 0.6974 0.6963 0.2265  0.0443  -0.0441 60  SER   B C   
670  O  O   . SER   B 51  ? 0.8521 0.7191 0.7068 0.2354  0.0441  -0.0519 60  SER   B O   
671  C  CB  . SER   B 51  ? 0.8115 0.6931 0.6802 0.1990  0.0433  -0.0392 60  SER   B CB  
672  O  OG  . SER   B 51  ? 0.8301 0.7207 0.7051 0.2110  0.0353  -0.0391 60  SER   B OG  
673  N  N   . GLY   B 52  ? 0.8913 0.6944 0.7057 0.2348  0.0438  -0.0409 61  GLY   B N   
674  C  CA  . GLY   B 52  ? 0.9128 0.7027 0.7154 0.2578  0.0419  -0.0469 61  GLY   B CA  
675  C  C   . GLY   B 52  ? 0.9313 0.7187 0.7297 0.2599  0.0473  -0.0559 61  GLY   B C   
676  O  O   . GLY   B 52  ? 0.9598 0.7179 0.7406 0.2498  0.0506  -0.0546 61  GLY   B O   
677  N  N   . GLU   B 53  ? 0.9111 0.7317 0.7267 0.2722  0.0482  -0.0651 62  GLU   B N   
678  C  CA  . GLU   B 53  ? 0.9139 0.7372 0.7254 0.2771  0.0545  -0.0740 62  GLU   B CA  
679  C  C   . GLU   B 53  ? 0.8949 0.7462 0.7238 0.2574  0.0611  -0.0746 62  GLU   B C   
680  O  O   . GLU   B 53  ? 0.9076 0.7474 0.7241 0.2535  0.0666  -0.0786 62  GLU   B O   
681  C  CB  . GLU   B 53  ? 0.9386 0.7861 0.7591 0.3030  0.0535  -0.0833 62  GLU   B CB  
682  C  CG  . GLU   B 53  ? 1.0445 0.8537 0.8344 0.3257  0.0523  -0.0887 62  GLU   B CG  
683  C  CD  . GLU   B 53  ? 1.1312 0.9670 0.9303 0.3548  0.0500  -0.0977 62  GLU   B CD  
684  O  OE1 . GLU   B 53  ? 1.1261 0.9926 0.9471 0.3605  0.0441  -0.0967 62  GLU   B OE1 
685  O  OE2 . GLU   B 53  ? 1.1645 0.9911 0.9486 0.3730  0.0532  -0.1063 62  GLU   B OE2 
686  N  N   . GLY   B 54  ? 0.8648 0.7500 0.7195 0.2463  0.0600  -0.0709 63  GLY   B N   
687  C  CA  . GLY   B 54  ? 0.8410 0.7525 0.7119 0.2279  0.0659  -0.0700 63  GLY   B CA  
688  C  C   . GLY   B 54  ? 0.8371 0.7269 0.6955 0.2073  0.0672  -0.0636 63  GLY   B C   
689  O  O   . GLY   B 54  ? 0.8571 0.7201 0.7027 0.2025  0.0626  -0.0574 63  GLY   B O   
690  N  N   . ARG   B 55  ? 0.8051 0.7085 0.6674 0.1954  0.0738  -0.0647 64  ARG   B N   
691  C  CA  . ARG   B 55  ? 0.7928 0.6812 0.6446 0.1768  0.0748  -0.0599 64  ARG   B CA  
692  C  C   . ARG   B 55  ? 0.7514 0.6654 0.6220 0.1615  0.0748  -0.0540 64  ARG   B C   
693  O  O   . ARG   B 55  ? 0.7369 0.6816 0.6274 0.1624  0.0774  -0.0554 64  ARG   B O   
694  C  CB  . ARG   B 55  ? 0.8111 0.6920 0.6479 0.1770  0.0815  -0.0663 64  ARG   B CB  
695  C  CG  . ARG   B 55  ? 0.8597 0.7200 0.6808 0.1606  0.0806  -0.0635 64  ARG   B CG  
696  C  CD  . ARG   B 55  ? 0.9090 0.7661 0.7153 0.1629  0.0867  -0.0710 64  ARG   B CD  
697  N  NE  . ARG   B 55  ? 0.9551 0.7968 0.7476 0.1476  0.0846  -0.0694 64  ARG   B NE  
698  C  CZ  . ARG   B 55  ? 0.9954 0.8072 0.7641 0.1478  0.0818  -0.0753 64  ARG   B CZ  
699  N  NH1 . ARG   B 55  ? 0.9989 0.7888 0.7525 0.1628  0.0812  -0.0830 64  ARG   B NH1 
700  N  NH2 . ARG   B 55  ? 0.9943 0.7968 0.7535 0.1335  0.0785  -0.0742 64  ARG   B NH2 
701  N  N   . LEU   B 56  ? 0.7280 0.6294 0.5923 0.1477  0.0715  -0.0473 65  LEU   B N   
702  C  CA  . LEU   B 56  ? 0.6994 0.6177 0.5753 0.1345  0.0706  -0.0418 65  LEU   B CA  
703  C  C   . LEU   B 56  ? 0.6756 0.5855 0.5386 0.1223  0.0740  -0.0406 65  LEU   B C   
704  O  O   . LEU   B 56  ? 0.6798 0.5675 0.5278 0.1190  0.0715  -0.0396 65  LEU   B O   
705  C  CB  . LEU   B 56  ? 0.7063 0.6180 0.5840 0.1322  0.0627  -0.0351 65  LEU   B CB  
706  C  CG  . LEU   B 56  ? 0.7357 0.6483 0.6195 0.1457  0.0571  -0.0356 65  LEU   B CG  
707  C  CD1 . LEU   B 56  ? 0.7466 0.6551 0.6301 0.1429  0.0502  -0.0287 65  LEU   B CD1 
708  C  CD2 . LEU   B 56  ? 0.7333 0.6737 0.6374 0.1523  0.0572  -0.0409 65  LEU   B CD2 
709  N  N   . ASP   B 57  ? 0.6506 0.5778 0.5187 0.1158  0.0797  -0.0407 66  ASP   B N   
710  C  CA  . ASP   B 57  ? 0.6520 0.5714 0.5053 0.1061  0.0824  -0.0398 66  ASP   B CA  
711  C  C   . ASP   B 57  ? 0.6396 0.5639 0.4961 0.0942  0.0791  -0.0323 66  ASP   B C   
712  O  O   . ASP   B 57  ? 0.6342 0.5733 0.5055 0.0920  0.0782  -0.0291 66  ASP   B O   
713  C  CB  . ASP   B 57  ? 0.6803 0.6114 0.5301 0.1089  0.0924  -0.0445 66  ASP   B CB  
714  C  CG  . ASP   B 57  ? 0.7704 0.6960 0.6143 0.1238  0.0956  -0.0530 66  ASP   B CG  
715  O  OD1 . ASP   B 57  ? 0.7915 0.6906 0.6195 0.1275  0.0907  -0.0563 66  ASP   B OD1 
716  O  OD2 . ASP   B 57  ? 0.8012 0.7491 0.6565 0.1320  0.1028  -0.0561 66  ASP   B OD2 
717  N  N   . PRO   B 58  ? 0.6280 0.5391 0.4703 0.0870  0.0759  -0.0298 67  PRO   B N   
718  C  CA  . PRO   B 58  ? 0.6144 0.5287 0.4563 0.0784  0.0723  -0.0231 67  PRO   B CA  
719  C  C   . PRO   B 58  ? 0.6074 0.5338 0.4507 0.0732  0.0785  -0.0211 67  PRO   B C   
720  O  O   . PRO   B 58  ? 0.6226 0.5536 0.4611 0.0745  0.0866  -0.0247 67  PRO   B O   
721  C  CB  . PRO   B 58  ? 0.6296 0.5309 0.4559 0.0737  0.0684  -0.0227 67  PRO   B CB  
722  C  CG  . PRO   B 58  ? 0.6463 0.5383 0.4623 0.0770  0.0720  -0.0301 67  PRO   B CG  
723  C  CD  . PRO   B 58  ? 0.6248 0.5180 0.4502 0.0865  0.0747  -0.0339 67  PRO   B CD  
724  N  N   . TYR   B 59  ? 0.5858 0.5162 0.4346 0.0678  0.0752  -0.0153 68  TYR   B N   
725  C  CA  . TYR   B 59  ? 0.5628 0.5013 0.4128 0.0606  0.0809  -0.0117 68  TYR   B CA  
726  C  C   . TYR   B 59  ? 0.5665 0.4932 0.4000 0.0544  0.0771  -0.0059 68  TYR   B C   
727  O  O   . TYR   B 59  ? 0.5739 0.4990 0.3949 0.0500  0.0831  -0.0036 68  TYR   B O   
728  C  CB  . TYR   B 59  ? 0.5382 0.4902 0.4098 0.0589  0.0796  -0.0105 68  TYR   B CB  
729  C  CG  . TYR   B 59  ? 0.5237 0.4844 0.4000 0.0483  0.0856  -0.0057 68  TYR   B CG  
730  C  CD1 . TYR   B 59  ? 0.5342 0.4818 0.3995 0.0401  0.0814  0.0010  68  TYR   B CD1 
731  C  CD2 . TYR   B 59  ? 0.5112 0.4939 0.4048 0.0467  0.0947  -0.0073 68  TYR   B CD2 
732  C  CE1 . TYR   B 59  ? 0.5367 0.4881 0.4048 0.0286  0.0870  0.0067  68  TYR   B CE1 
733  C  CE2 . TYR   B 59  ? 0.5137 0.5062 0.4149 0.0346  0.1007  -0.0015 68  TYR   B CE2 
734  C  CZ  . TYR   B 59  ? 0.5331 0.5077 0.4207 0.0245  0.0968  0.0059  68  TYR   B CZ  
735  O  OH  . TYR   B 59  ? 0.5439 0.5243 0.4374 0.0107  0.1031  0.0128  68  TYR   B OH  
736  N  N   . TRP   B 60  ? 0.5694 0.4882 0.4011 0.0558  0.0676  -0.0033 69  TRP   B N   
737  C  CA  . TRP   B 60  ? 0.5791 0.4873 0.3947 0.0532  0.0625  0.0019  69  TRP   B CA  
738  C  C   . TRP   B 60  ? 0.5980 0.5025 0.4100 0.0587  0.0546  0.0015  69  TRP   B C   
739  O  O   . TRP   B 60  ? 0.5964 0.5037 0.4197 0.0633  0.0515  0.0002  69  TRP   B O   
740  C  CB  . TRP   B 60  ? 0.5748 0.4787 0.3933 0.0493  0.0585  0.0070  69  TRP   B CB  
741  C  CG  . TRP   B 60  ? 0.5832 0.4731 0.3831 0.0505  0.0511  0.0118  69  TRP   B CG  
742  C  CD1 . TRP   B 60  ? 0.6003 0.4805 0.3800 0.0476  0.0528  0.0156  69  TRP   B CD1 
743  C  CD2 . TRP   B 60  ? 0.5816 0.4667 0.3791 0.0579  0.0411  0.0128  69  TRP   B CD2 
744  N  NE1 . TRP   B 60  ? 0.6094 0.4794 0.3751 0.0533  0.0437  0.0185  69  TRP   B NE1 
745  C  CE2 . TRP   B 60  ? 0.5988 0.4729 0.3756 0.0598  0.0369  0.0169  69  TRP   B CE2 
746  C  CE3 . TRP   B 60  ? 0.5834 0.4732 0.3924 0.0648  0.0359  0.0110  69  TRP   B CE3 
747  C  CZ2 . TRP   B 60  ? 0.6048 0.4751 0.3741 0.0688  0.0278  0.0186  69  TRP   B CZ2 
748  C  CZ3 . TRP   B 60  ? 0.5950 0.4800 0.3956 0.0729  0.0278  0.0135  69  TRP   B CZ3 
749  C  CH2 . TRP   B 60  ? 0.6034 0.4801 0.3853 0.0751  0.0239  0.0170  69  TRP   B CH2 
750  N  N   . GLY   B 61  ? 0.6132 0.5127 0.4096 0.0584  0.0515  0.0031  70  GLY   B N   
751  C  CA  . GLY   B 61  ? 0.6214 0.5226 0.4169 0.0623  0.0446  0.0036  70  GLY   B CA  
752  C  C   . GLY   B 61  ? 0.6222 0.5211 0.4015 0.0632  0.0395  0.0065  70  GLY   B C   
753  O  O   . GLY   B 61  ? 0.6335 0.5268 0.3988 0.0606  0.0421  0.0067  70  GLY   B O   
754  N  N   . ASP   B 62  ? 0.6158 0.5199 0.3959 0.0681  0.0327  0.0089  71  ASP   B N   
755  C  CA  . ASP   B 62  ? 0.6198 0.5253 0.3859 0.0718  0.0265  0.0115  71  ASP   B CA  
756  C  C   . ASP   B 62  ? 0.6118 0.5322 0.3869 0.0758  0.0216  0.0126  71  ASP   B C   
757  O  O   . ASP   B 62  ? 0.6064 0.5302 0.3897 0.0812  0.0204  0.0156  71  ASP   B O   
758  C  CB  . ASP   B 62  ? 0.6576 0.5516 0.4118 0.0769  0.0233  0.0162  71  ASP   B CB  
759  C  CG  . ASP   B 62  ? 0.7447 0.6349 0.4785 0.0824  0.0175  0.0187  71  ASP   B CG  
760  O  OD1 . ASP   B 62  ? 0.7487 0.6493 0.4821 0.0906  0.0110  0.0200  71  ASP   B OD1 
761  O  OD2 . ASP   B 62  ? 0.8229 0.7006 0.5405 0.0795  0.0198  0.0197  71  ASP   B OD2 
762  N  N   . VAL   B 63  ? 0.6094 0.5398 0.3830 0.0731  0.0186  0.0104  72  VAL   B N   
763  C  CA  . VAL   B 63  ? 0.6023 0.5515 0.3874 0.0738  0.0145  0.0118  72  VAL   B CA  
764  C  C   . VAL   B 63  ? 0.6041 0.5635 0.3851 0.0854  0.0092  0.0171  72  VAL   B C   
765  O  O   . VAL   B 63  ? 0.5971 0.5709 0.3902 0.0890  0.0091  0.0208  72  VAL   B O   
766  C  CB  . VAL   B 63  ? 0.6063 0.5632 0.3914 0.0660  0.0113  0.0067  72  VAL   B CB  
767  C  CG1 . VAL   B 63  ? 0.6002 0.5819 0.3964 0.0664  0.0052  0.0090  72  VAL   B CG1 
768  C  CG2 . VAL   B 63  ? 0.6160 0.5635 0.4082 0.0563  0.0160  0.0017  72  VAL   B CG2 
769  N  N   . LYS   B 64  ? 0.6138 0.5641 0.3758 0.0925  0.0052  0.0181  73  LYS   B N   
770  C  CA  . LYS   B 64  ? 0.6083 0.5654 0.3624 0.1064  -0.0009 0.0223  73  LYS   B CA  
771  C  C   . LYS   B 64  ? 0.6118 0.5607 0.3676 0.1137  0.0003  0.0257  73  LYS   B C   
772  O  O   . LYS   B 64  ? 0.6026 0.5669 0.3642 0.1232  -0.0015 0.0288  73  LYS   B O   
773  C  CB  . LYS   B 64  ? 0.6347 0.5799 0.3640 0.1134  -0.0064 0.0226  73  LYS   B CB  
774  C  CG  . LYS   B 64  ? 0.6723 0.6284 0.3930 0.1302  -0.0140 0.0258  73  LYS   B CG  
775  C  CD  . LYS   B 64  ? 0.7307 0.6789 0.4270 0.1378  -0.0207 0.0255  73  LYS   B CD  
776  C  CE  . LYS   B 64  ? 0.7799 0.7264 0.4602 0.1573  -0.0278 0.0289  73  LYS   B CE  
777  N  NZ  . LYS   B 64  ? 0.8339 0.7651 0.4852 0.1665  -0.0345 0.0292  73  LYS   B NZ  
778  N  N   . GLN   B 65  ? 0.6158 0.5429 0.3682 0.1092  0.0036  0.0247  74  GLN   B N   
779  C  CA  . GLN   B 65  ? 0.6103 0.5284 0.3652 0.1149  0.0033  0.0263  74  GLN   B CA  
780  C  C   . GLN   B 65  ? 0.5935 0.5258 0.3684 0.1131  0.0078  0.0266  74  GLN   B C   
781  O  O   . GLN   B 65  ? 0.5964 0.5278 0.3727 0.1217  0.0065  0.0284  74  GLN   B O   
782  C  CB  . GLN   B 65  ? 0.6429 0.5385 0.3938 0.1074  0.0054  0.0246  74  GLN   B CB  
783  C  CG  . GLN   B 65  ? 0.7131 0.5879 0.4415 0.1091  0.0013  0.0264  74  GLN   B CG  
784  C  CD  . GLN   B 65  ? 0.7940 0.6497 0.5221 0.0992  0.0043  0.0260  74  GLN   B CD  
785  O  OE1 . GLN   B 65  ? 0.8108 0.6625 0.5491 0.0984  0.0034  0.0248  74  GLN   B OE1 
786  N  NE2 . GLN   B 65  ? 0.8080 0.6527 0.5242 0.0915  0.0078  0.0275  74  GLN   B NE2 
787  N  N   . ASP   B 66  ? 0.5749 0.5171 0.3624 0.1023  0.0126  0.0246  75  ASP   B N   
788  C  CA  . ASP   B 66  ? 0.5543 0.5051 0.3583 0.0981  0.0175  0.0252  75  ASP   B CA  
789  C  C   . ASP   B 66  ? 0.5421 0.4787 0.3498 0.0981  0.0204  0.0235  75  ASP   B C   
790  O  O   . ASP   B 66  ? 0.5284 0.4678 0.3431 0.1024  0.0221  0.0259  75  ASP   B O   
791  C  CB  . ASP   B 66  ? 0.5648 0.5353 0.3754 0.1054  0.0170  0.0308  75  ASP   B CB  
792  C  CG  . ASP   B 66  ? 0.6052 0.5829 0.4311 0.0977  0.0228  0.0328  75  ASP   B CG  
793  O  OD1 . ASP   B 66  ? 0.6301 0.6016 0.4611 0.0855  0.0252  0.0288  75  ASP   B OD1 
794  O  OD2 . ASP   B 66  ? 0.5948 0.5821 0.4255 0.1044  0.0251  0.0386  75  ASP   B OD2 
795  N  N   . LEU   B 67  ? 0.5427 0.4656 0.3461 0.0930  0.0213  0.0197  76  LEU   B N   
796  C  CA  . LEU   B 67  ? 0.5374 0.4512 0.3473 0.0923  0.0235  0.0172  76  LEU   B CA  
797  C  C   . LEU   B 67  ? 0.5422 0.4529 0.3571 0.0827  0.0296  0.0125  76  LEU   B C   
798  O  O   . LEU   B 67  ? 0.5433 0.4538 0.3516 0.0768  0.0314  0.0110  76  LEU   B O   
799  C  CB  . LEU   B 67  ? 0.5366 0.4391 0.3384 0.0966  0.0183  0.0176  76  LEU   B CB  
800  C  CG  . LEU   B 67  ? 0.5482 0.4494 0.3415 0.1093  0.0114  0.0208  76  LEU   B CG  
801  C  CD1 . LEU   B 67  ? 0.5687 0.4526 0.3500 0.1114  0.0049  0.0203  76  LEU   B CD1 
802  C  CD2 . LEU   B 67  ? 0.5420 0.4484 0.3437 0.1169  0.0117  0.0216  76  LEU   B CD2 
803  N  N   . VAL   B 68  ? 0.5409 0.4497 0.3660 0.0830  0.0325  0.0098  77  VAL   B N   
804  C  CA  . VAL   B 68  ? 0.5349 0.4428 0.3651 0.0772  0.0388  0.0048  77  VAL   B CA  
805  C  C   . VAL   B 68  ? 0.5325 0.4414 0.3744 0.0805  0.0392  0.0024  77  VAL   B C   
806  O  O   . VAL   B 68  ? 0.5311 0.4397 0.3770 0.0877  0.0351  0.0036  77  VAL   B O   
807  C  CB  . VAL   B 68  ? 0.5329 0.4406 0.3640 0.0746  0.0421  0.0024  77  VAL   B CB  
808  C  CG1 . VAL   B 68  ? 0.5322 0.4394 0.3695 0.0798  0.0411  0.0047  77  VAL   B CG1 
809  C  CG2 . VAL   B 68  ? 0.5372 0.4424 0.3695 0.0716  0.0484  -0.0036 77  VAL   B CG2 
810  N  N   . SER   B 69  ? 0.5349 0.4468 0.3819 0.0758  0.0440  -0.0008 78  SER   B N   
811  C  CA  . SER   B 69  ? 0.5243 0.4427 0.3859 0.0780  0.0443  -0.0039 78  SER   B CA  
812  C  C   . SER   B 69  ? 0.5171 0.4422 0.3850 0.0779  0.0524  -0.0089 78  SER   B C   
813  O  O   . SER   B 69  ? 0.5230 0.4464 0.3824 0.0737  0.0582  -0.0099 78  SER   B O   
814  C  CB  . SER   B 69  ? 0.5294 0.4488 0.3940 0.0719  0.0418  -0.0022 78  SER   B CB  
815  O  OG  . SER   B 69  ? 0.5392 0.4614 0.4013 0.0628  0.0494  -0.0015 78  SER   B OG  
816  N  N   . TYR   B 70  ? 0.5092 0.4411 0.3899 0.0846  0.0522  -0.0127 79  TYR   B N   
817  C  CA  . TYR   B 70  ? 0.5118 0.4496 0.3978 0.0892  0.0588  -0.0182 79  TYR   B CA  
818  C  C   . TYR   B 70  ? 0.5050 0.4620 0.4098 0.0899  0.0605  -0.0213 79  TYR   B C   
819  O  O   . TYR   B 70  ? 0.4939 0.4558 0.4093 0.0920  0.0531  -0.0210 79  TYR   B O   
820  C  CB  . TYR   B 70  ? 0.5154 0.4431 0.3983 0.0997  0.0557  -0.0197 79  TYR   B CB  
821  C  CG  . TYR   B 70  ? 0.5389 0.4507 0.4065 0.0968  0.0560  -0.0173 79  TYR   B CG  
822  C  CD1 . TYR   B 70  ? 0.5503 0.4567 0.4122 0.0944  0.0509  -0.0113 79  TYR   B CD1 
823  C  CD2 . TYR   B 70  ? 0.5588 0.4622 0.4179 0.0967  0.0608  -0.0215 79  TYR   B CD2 
824  C  CE1 . TYR   B 70  ? 0.5654 0.4624 0.4173 0.0900  0.0510  -0.0089 79  TYR   B CE1 
825  C  CE2 . TYR   B 70  ? 0.5766 0.4663 0.4235 0.0914  0.0595  -0.0200 79  TYR   B CE2 
826  C  CZ  . TYR   B 70  ? 0.5894 0.4779 0.4346 0.0872  0.0548  -0.0134 79  TYR   B CZ  
827  O  OH  . TYR   B 70  ? 0.6145 0.4940 0.4517 0.0808  0.0535  -0.0120 79  TYR   B OH  
828  N  N   . CYS   B 71  ? 0.5002 0.4695 0.4094 0.0883  0.0698  -0.0244 80  CYS   B N   
829  C  CA  . CYS   B 71  ? 0.5031 0.4974 0.4342 0.0886  0.0731  -0.0272 80  CYS   B CA  
830  C  C   . CYS   B 71  ? 0.4994 0.5041 0.4401 0.0742  0.0739  -0.0223 80  CYS   B C   
831  O  O   . CYS   B 71  ? 0.5098 0.5385 0.4692 0.0704  0.0799  -0.0234 80  CYS   B O   
832  C  CB  . CYS   B 71  ? 0.5288 0.5302 0.4737 0.1002  0.0654  -0.0314 80  CYS   B CB  
833  S  SG  . CYS   B 71  ? 0.6398 0.6244 0.5711 0.1176  0.0649  -0.0359 80  CYS   B SG  
834  N  N   . GLY   B 72  ? 0.4779 0.4652 0.4055 0.0662  0.0688  -0.0167 81  GLY   B N   
835  C  CA  . GLY   B 72  ? 0.4625 0.4523 0.3945 0.0523  0.0689  -0.0115 81  GLY   B CA  
836  C  C   . GLY   B 72  ? 0.4745 0.4402 0.3865 0.0479  0.0618  -0.0061 81  GLY   B C   
837  O  O   . GLY   B 72  ? 0.4750 0.4264 0.3723 0.0554  0.0574  -0.0061 81  GLY   B O   
838  N  N   . PRO   B 73  ? 0.4803 0.4412 0.3914 0.0357  0.0608  -0.0009 82  PRO   B N   
839  C  CA  . PRO   B 73  ? 0.5045 0.4404 0.3938 0.0338  0.0533  0.0041  82  PRO   B CA  
840  C  C   . PRO   B 73  ? 0.5332 0.4583 0.4207 0.0426  0.0394  0.0020  82  PRO   B C   
841  O  O   . PRO   B 73  ? 0.5329 0.4681 0.4376 0.0463  0.0337  -0.0025 82  PRO   B O   
842  C  CB  . PRO   B 73  ? 0.5103 0.4418 0.4001 0.0186  0.0554  0.0099  82  PRO   B CB  
843  C  CG  . PRO   B 73  ? 0.4921 0.4496 0.4117 0.0120  0.0594  0.0071  82  PRO   B CG  
844  C  CD  . PRO   B 73  ? 0.4551 0.4329 0.3845 0.0230  0.0668  0.0011  82  PRO   B CD  
845  N  N   . TRP   B 74  ? 0.5481 0.4539 0.4140 0.0471  0.0335  0.0053  83  TRP   B N   
846  C  CA  . TRP   B 74  ? 0.5662 0.4610 0.4255 0.0572  0.0214  0.0044  83  TRP   B CA  
847  C  C   . TRP   B 74  ? 0.5836 0.4734 0.4518 0.0528  0.0116  0.0026  83  TRP   B C   
848  O  O   . TRP   B 74  ? 0.5939 0.4742 0.4591 0.0408  0.0109  0.0057  83  TRP   B O   
849  C  CB  . TRP   B 74  ? 0.5717 0.4493 0.4061 0.0617  0.0180  0.0089  83  TRP   B CB  
850  C  CG  . TRP   B 74  ? 0.5765 0.4467 0.4023 0.0751  0.0081  0.0084  83  TRP   B CG  
851  C  CD1 . TRP   B 74  ? 0.5961 0.4500 0.4115 0.0795  -0.0031 0.0086  83  TRP   B CD1 
852  C  CD2 . TRP   B 74  ? 0.5739 0.4523 0.3997 0.0864  0.0088  0.0080  83  TRP   B CD2 
853  N  NE1 . TRP   B 74  ? 0.6038 0.4573 0.4120 0.0947  -0.0087 0.0081  83  TRP   B NE1 
854  C  CE2 . TRP   B 74  ? 0.5908 0.4605 0.4067 0.0982  -0.0009 0.0084  83  TRP   B CE2 
855  C  CE3 . TRP   B 74  ? 0.5665 0.4569 0.3982 0.0872  0.0167  0.0075  83  TRP   B CE3 
856  C  CZ2 . TRP   B 74  ? 0.5928 0.4688 0.4060 0.1104  -0.0011 0.0097  83  TRP   B CZ2 
857  C  CZ3 . TRP   B 74  ? 0.5709 0.4649 0.4007 0.0972  0.0155  0.0088  83  TRP   B CZ3 
858  C  CH2 . TRP   B 74  ? 0.5837 0.4723 0.4051 0.1085  0.0076  0.0105  83  TRP   B CH2 
859  N  N   . LYS   B 75  ? 0.5832 0.4789 0.4619 0.0619  0.0037  -0.0025 84  LYS   B N   
860  C  CA  . LYS   B 75  ? 0.5865 0.4793 0.4753 0.0579  -0.0075 -0.0061 84  LYS   B CA  
861  C  C   . LYS   B 75  ? 0.6178 0.4880 0.4877 0.0681  -0.0219 -0.0070 84  LYS   B C   
862  O  O   . LYS   B 75  ? 0.6212 0.4802 0.4924 0.0627  -0.0331 -0.0096 84  LYS   B O   
863  C  CB  . LYS   B 75  ? 0.5744 0.4903 0.4879 0.0623  -0.0085 -0.0127 84  LYS   B CB  
864  C  CG  . LYS   B 75  ? 0.5755 0.5162 0.5086 0.0554  0.0050  -0.0132 84  LYS   B CG  
865  C  CD  . LYS   B 75  ? 0.6055 0.5551 0.5537 0.0364  0.0086  -0.0113 84  LYS   B CD  
866  C  CE  . LYS   B 75  ? 0.6231 0.6016 0.5915 0.0323  0.0226  -0.0121 84  LYS   B CE  
867  N  NZ  . LYS   B 75  ? 0.6340 0.6273 0.6221 0.0136  0.0264  -0.0097 84  LYS   B NZ  
868  N  N   . LEU   B 76  ? 0.6370 0.5015 0.4900 0.0832  -0.0220 -0.0053 85  LEU   B N   
869  C  CA  . LEU   B 76  ? 0.6599 0.5069 0.4939 0.0973  -0.0343 -0.0063 85  LEU   B CA  
870  C  C   . LEU   B 76  ? 0.7018 0.5241 0.5130 0.0950  -0.0395 -0.0028 85  LEU   B C   
871  O  O   . LEU   B 76  ? 0.7136 0.5339 0.5128 0.0950  -0.0324 0.0025  85  LEU   B O   
872  C  CB  . LEU   B 76  ? 0.6523 0.5063 0.4783 0.1140  -0.0307 -0.0044 85  LEU   B CB  
873  C  CG  . LEU   B 76  ? 0.6400 0.5139 0.4831 0.1166  -0.0226 -0.0058 85  LEU   B CG  
874  C  CD1 . LEU   B 76  ? 0.6404 0.5170 0.4731 0.1295  -0.0182 -0.0017 85  LEU   B CD1 
875  C  CD2 . LEU   B 76  ? 0.6390 0.5185 0.4956 0.1205  -0.0306 -0.0124 85  LEU   B CD2 
876  N  N   . ASP   B 77  ? 0.7243 0.5260 0.5278 0.0939  -0.0533 -0.0062 86  ASP   B N   
877  C  CA  . ASP   B 77  ? 0.7644 0.5364 0.5430 0.0920  -0.0599 -0.0032 86  ASP   B CA  
878  C  C   . ASP   B 77  ? 0.7899 0.5369 0.5432 0.1095  -0.0756 -0.0068 86  ASP   B C   
879  O  O   . ASP   B 77  ? 0.8209 0.5401 0.5494 0.1111  -0.0816 -0.0046 86  ASP   B O   
880  C  CB  . ASP   B 77  ? 0.8009 0.5620 0.5882 0.0691  -0.0609 -0.0022 86  ASP   B CB  
881  C  CG  . ASP   B 77  ? 0.8894 0.6543 0.6978 0.0602  -0.0710 -0.0091 86  ASP   B CG  
882  O  OD1 . ASP   B 77  ? 0.8977 0.6785 0.7173 0.0717  -0.0755 -0.0152 86  ASP   B OD1 
883  O  OD2 . ASP   B 77  ? 0.9397 0.6925 0.7536 0.0412  -0.0745 -0.0081 86  ASP   B OD2 
884  N  N   . ALA   B 78  ? 0.7844 0.5388 0.5402 0.1243  -0.0822 -0.0122 87  ALA   B N   
885  C  CA  . ALA   B 78  ? 0.8014 0.5320 0.5299 0.1438  -0.0969 -0.0161 87  ALA   B CA  
886  C  C   . ALA   B 78  ? 0.8147 0.5405 0.5175 0.1608  -0.0926 -0.0105 87  ALA   B C   
887  O  O   . ALA   B 78  ? 0.7952 0.5432 0.5060 0.1601  -0.0786 -0.0045 87  ALA   B O   
888  C  CB  . ALA   B 78  ? 0.7869 0.5288 0.5215 0.1579  -0.1031 -0.0222 87  ALA   B CB  
889  N  N   . ALA   B 79  ? 0.8425 0.5398 0.5146 0.1764  -0.1054 -0.0129 88  ALA   B N   
890  C  CA  . ALA   B 79  ? 0.8624 0.5580 0.5104 0.1949  -0.1022 -0.0080 88  ALA   B CA  
891  C  C   . ALA   B 79  ? 0.8863 0.5693 0.5078 0.2224  -0.1133 -0.0122 88  ALA   B C   
892  O  O   . ALA   B 79  ? 0.9015 0.5578 0.5106 0.2257  -0.1288 -0.0198 88  ALA   B O   
893  C  CB  . ALA   B 79  ? 0.8811 0.5517 0.5116 0.1870  -0.1041 -0.0046 88  ALA   B CB  
894  N  N   . TRP   B 80  ? 0.8880 0.5903 0.5002 0.2422  -0.1056 -0.0073 89  TRP   B N   
895  C  CA  . TRP   B 80  ? 0.9134 0.6080 0.4981 0.2716  -0.1133 -0.0098 89  TRP   B CA  
896  C  C   . TRP   B 80  ? 0.9598 0.6112 0.5093 0.2815  -0.1294 -0.0147 89  TRP   B C   
897  O  O   . TRP   B 80  ? 0.9670 0.6046 0.5096 0.2724  -0.1289 -0.0117 89  TRP   B O   
898  C  CB  . TRP   B 80  ? 0.9006 0.6281 0.4849 0.2874  -0.0997 -0.0017 89  TRP   B CB  
899  C  CG  . TRP   B 80  ? 0.9145 0.6403 0.4713 0.3193  -0.1046 -0.0028 89  TRP   B CG  
900  C  CD1 . TRP   B 80  ? 0.9307 0.6489 0.4768 0.3342  -0.1118 -0.0080 89  TRP   B CD1 
901  C  CD2 . TRP   B 80  ? 0.9170 0.6524 0.4537 0.3417  -0.1016 0.0015  89  TRP   B CD2 
902  N  NE1 . TRP   B 80  ? 0.9433 0.6631 0.4612 0.3651  -0.1134 -0.0071 89  TRP   B NE1 
903  C  CE2 . TRP   B 80  ? 0.9343 0.6674 0.4479 0.3702  -0.1064 -0.0010 89  TRP   B CE2 
904  C  CE3 . TRP   B 80  ? 0.9172 0.6641 0.4524 0.3420  -0.0959 0.0068  89  TRP   B CE3 
905  C  CZ2 . TRP   B 80  ? 0.9410 0.6856 0.4318 0.3988  -0.1043 0.0022  89  TRP   B CZ2 
906  C  CZ3 . TRP   B 80  ? 0.9292 0.6883 0.4434 0.3700  -0.0950 0.0095  89  TRP   B CZ3 
907  C  CH2 . TRP   B 80  ? 0.9348 0.6939 0.4279 0.3980  -0.0984 0.0074  89  TRP   B CH2 
908  N  N   . ASP   B 81  ? 0.9931 0.6198 0.5182 0.2999  -0.1446 -0.0226 90  ASP   B N   
909  C  CA  . ASP   B 81  ? 1.0402 0.6194 0.5286 0.3097  -0.1621 -0.0285 90  ASP   B CA  
910  C  C   . ASP   B 81  ? 1.0676 0.6434 0.5224 0.3403  -0.1619 -0.0258 90  ASP   B C   
911  O  O   . ASP   B 81  ? 1.1062 0.6394 0.5254 0.3521  -0.1765 -0.0306 90  ASP   B O   
912  C  CB  . ASP   B 81  ? 1.0798 0.6275 0.5548 0.3138  -0.1817 -0.0401 90  ASP   B CB  
913  C  CG  . ASP   B 81  ? 1.1605 0.7204 0.6232 0.3417  -0.1842 -0.0441 90  ASP   B CG  
914  O  OD1 . ASP   B 81  ? 1.1709 0.7634 0.6332 0.3597  -0.1699 -0.0368 90  ASP   B OD1 
915  O  OD2 . ASP   B 81  ? 1.2099 0.7474 0.6633 0.3453  -0.2006 -0.0542 90  ASP   B OD2 
916  N  N   . GLY   B 82  ? 1.0456 0.6652 0.5118 0.3523  -0.1457 -0.0182 91  GLY   B N   
917  C  CA  . GLY   B 82  ? 1.0622 0.6889 0.5025 0.3814  -0.1437 -0.0150 91  GLY   B CA  
918  C  C   . GLY   B 82  ? 1.0853 0.7020 0.4937 0.4158  -0.1525 -0.0205 91  GLY   B C   
919  O  O   . GLY   B 82  ? 1.0916 0.7182 0.4779 0.4438  -0.1503 -0.0181 91  GLY   B O   
920  N  N   . LEU   B 83  ? 1.0936 0.6929 0.4989 0.4156  -0.1627 -0.0282 92  LEU   B N   
921  C  CA  . LEU   B 83  ? 1.1194 0.7042 0.4906 0.4488  -0.1728 -0.0348 92  LEU   B CA  
922  C  C   . LEU   B 83  ? 1.1165 0.7289 0.5014 0.4549  -0.1660 -0.0340 92  LEU   B C   
923  O  O   . LEU   B 83  ? 1.1293 0.7569 0.4945 0.4852  -0.1617 -0.0321 92  LEU   B O   
924  C  CB  . LEU   B 83  ? 1.1557 0.6794 0.4963 0.4494  -0.1982 -0.0480 92  LEU   B CB  
925  C  CG  . LEU   B 83  ? 1.2084 0.6906 0.5041 0.4710  -0.2113 -0.0524 92  LEU   B CG  
926  C  CD1 . LEU   B 83  ? 1.2164 0.6780 0.5187 0.4457  -0.2123 -0.0490 92  LEU   B CD1 
927  C  CD2 . LEU   B 83  ? 1.2535 0.6818 0.5115 0.4851  -0.2362 -0.0666 92  LEU   B CD2 
928  N  N   . SER   B 84  ? 1.0994 0.7153 0.5140 0.4288  -0.1663 -0.0359 93  SER   B N   
929  C  CA  . SER   B 84  ? 1.0847 0.7170 0.5060 0.4365  -0.1640 -0.0370 93  SER   B CA  
930  C  C   . SER   B 84  ? 1.0571 0.7394 0.5131 0.4266  -0.1407 -0.0247 93  SER   B C   
931  O  O   . SER   B 84  ? 1.0518 0.7569 0.5347 0.4064  -0.1272 -0.0167 93  SER   B O   
932  C  CB  . SER   B 84  ? 1.1006 0.7047 0.5280 0.4205  -0.1818 -0.0485 93  SER   B CB  
933  O  OG  . SER   B 84  ? 1.1206 0.7083 0.5677 0.3886  -0.1871 -0.0508 93  SER   B OG  
934  N  N   . GLU   B 85  ? 1.0429 0.7394 0.4942 0.4429  -0.1367 -0.0233 94  GLU   B N   
935  C  CA  . GLU   B 85  ? 1.0135 0.7502 0.4909 0.4369  -0.1165 -0.0119 94  GLU   B CA  
936  C  C   . GLU   B 85  ? 0.9786 0.7207 0.4932 0.4041  -0.1142 -0.0125 94  GLU   B C   
937  O  O   . GLU   B 85  ? 0.9904 0.7075 0.5099 0.3895  -0.1292 -0.0226 94  GLU   B O   
938  C  CB  . GLU   B 85  ? 1.0459 0.7876 0.5015 0.4649  -0.1152 -0.0108 94  GLU   B CB  
939  C  CG  . GLU   B 85  ? 1.1106 0.8591 0.5332 0.4987  -0.1111 -0.0069 94  GLU   B CG  
940  C  CD  . GLU   B 85  ? 1.1702 0.9415 0.5792 0.5233  -0.0983 0.0018  94  GLU   B CD  
941  O  OE1 . GLU   B 85  ? 1.1644 0.9337 0.5776 0.5211  -0.0988 0.0013  94  GLU   B OE1 
942  O  OE2 . GLU   B 85  ? 1.1925 0.9849 0.5862 0.5457  -0.0874 0.0096  94  GLU   B OE2 
943  N  N   . VAL   B 86  ? 0.9301 0.7057 0.4717 0.3919  -0.0949 -0.0015 95  VAL   B N   
944  C  CA  . VAL   B 86  ? 0.8853 0.6703 0.4618 0.3629  -0.0894 -0.0006 95  VAL   B CA  
945  C  C   . VAL   B 86  ? 0.8615 0.6701 0.4493 0.3656  -0.0752 0.0079  95  VAL   B C   
946  O  O   . VAL   B 86  ? 0.8706 0.6929 0.4431 0.3857  -0.0661 0.0158  95  VAL   B O   
947  C  CB  . VAL   B 86  ? 0.8566 0.6546 0.4545 0.3406  -0.0798 0.0046  95  VAL   B CB  
948  C  CG1 . VAL   B 86  ? 0.8730 0.6463 0.4540 0.3413  -0.0920 -0.0013 95  VAL   B CG1 
949  C  CG2 . VAL   B 86  ? 0.8376 0.6696 0.4437 0.3440  -0.0607 0.0175  95  VAL   B CG2 
950  N  N   . GLN   B 87  ? 0.8287 0.6423 0.4427 0.3455  -0.0721 0.0072  96  GLN   B N   
951  C  CA  . GLN   B 87  ? 0.8065 0.6378 0.4302 0.3462  -0.0586 0.0158  96  GLN   B CA  
952  C  C   . GLN   B 87  ? 0.7746 0.6249 0.4287 0.3211  -0.0439 0.0228  96  GLN   B C   
953  O  O   . GLN   B 87  ? 0.7623 0.6086 0.4346 0.3008  -0.0475 0.0174  96  GLN   B O   
954  C  CB  . GLN   B 87  ? 0.8203 0.6387 0.4406 0.3528  -0.0690 0.0084  96  GLN   B CB  
955  C  CG  . GLN   B 87  ? 0.8606 0.6659 0.4459 0.3834  -0.0782 0.0055  96  GLN   B CG  
956  C  CD  . GLN   B 87  ? 0.9043 0.6976 0.4821 0.3939  -0.0897 -0.0018 96  GLN   B CD  
957  O  OE1 . GLN   B 87  ? 0.8920 0.6909 0.4908 0.3813  -0.0874 -0.0023 96  GLN   B OE1 
958  N  NE2 . GLN   B 87  ? 0.9330 0.7092 0.4780 0.4200  -0.1029 -0.0082 96  GLN   B NE2 
959  N  N   . LEU   B 88  ? 0.7536 0.6239 0.4118 0.3224  -0.0273 0.0351  97  LEU   B N   
960  C  CA  . LEU   B 88  ? 0.7377 0.6228 0.4219 0.2998  -0.0145 0.0413  97  LEU   B CA  
961  C  C   . LEU   B 88  ? 0.7281 0.6076 0.4169 0.2993  -0.0120 0.0421  97  LEU   B C   
962  O  O   . LEU   B 88  ? 0.7426 0.6222 0.4154 0.3162  -0.0077 0.0484  97  LEU   B O   
963  C  CB  . LEU   B 88  ? 0.7343 0.6440 0.4218 0.2993  0.0012  0.0543  97  LEU   B CB  
964  C  CG  . LEU   B 88  ? 0.7490 0.6721 0.4605 0.2777  0.0149  0.0620  97  LEU   B CG  
965  C  CD1 . LEU   B 88  ? 0.7442 0.6623 0.4753 0.2553  0.0111  0.0544  97  LEU   B CD1 
966  C  CD2 . LEU   B 88  ? 0.7525 0.7021 0.4688 0.2764  0.0288  0.0746  97  LEU   B CD2 
967  N  N   . LEU   B 89  ? 0.7052 0.5792 0.4129 0.2827  -0.0152 0.0356  98  LEU   B N   
968  C  CA  . LEU   B 89  ? 0.6990 0.5680 0.4106 0.2837  -0.0129 0.0362  98  LEU   B CA  
969  C  C   . LEU   B 89  ? 0.7015 0.5815 0.4263 0.2690  0.0037  0.0468  98  LEU   B C   
970  O  O   . LEU   B 89  ? 0.6976 0.5797 0.4416 0.2501  0.0064  0.0441  98  LEU   B O   
971  C  CB  . LEU   B 89  ? 0.6859 0.5465 0.4110 0.2759  -0.0248 0.0235  98  LEU   B CB  
972  C  CG  . LEU   B 89  ? 0.6945 0.5518 0.4268 0.2765  -0.0233 0.0223  98  LEU   B CG  
973  C  CD1 . LEU   B 89  ? 0.7132 0.5634 0.4234 0.2978  -0.0210 0.0290  98  LEU   B CD1 
974  C  CD2 . LEU   B 89  ? 0.6919 0.5462 0.4361 0.2739  -0.0376 0.0089  98  LEU   B CD2 
975  N  N   . ALA   B 90  ? 0.7037 0.5915 0.4176 0.2772  0.0150  0.0593  99  ALA   B N   
976  C  CA  . ALA   B 90  ? 0.6969 0.5951 0.4225 0.2624  0.0304  0.0706  99  ALA   B CA  
977  C  C   . ALA   B 90  ? 0.6959 0.5806 0.4237 0.2581  0.0349  0.0729  99  ALA   B C   
978  O  O   . ALA   B 90  ? 0.7048 0.5787 0.4155 0.2745  0.0347  0.0763  99  ALA   B O   
979  C  CB  . ALA   B 90  ? 0.6980 0.6112 0.4120 0.2727  0.0413  0.0841  99  ALA   B CB  
980  N  N   . VAL   B 91  ? 0.6853 0.5691 0.4312 0.2378  0.0393  0.0718  100 VAL   B N   
981  C  CA  . VAL   B 91  ? 0.6969 0.5650 0.4428 0.2340  0.0440  0.0743  100 VAL   B CA  
982  C  C   . VAL   B 91  ? 0.7005 0.5727 0.4523 0.2181  0.0581  0.0869  100 VAL   B C   
983  O  O   . VAL   B 91  ? 0.6953 0.5710 0.4630 0.1991  0.0601  0.0843  100 VAL   B O   
984  C  CB  . VAL   B 91  ? 0.6995 0.5599 0.4587 0.2260  0.0362  0.0612  100 VAL   B CB  
985  C  CG1 . VAL   B 91  ? 0.7110 0.5531 0.4669 0.2260  0.0400  0.0628  100 VAL   B CG1 
986  C  CG2 . VAL   B 91  ? 0.6991 0.5599 0.4565 0.2382  0.0219  0.0494  100 VAL   B CG2 
987  N  N   . PRO   B 92  ? 0.7130 0.5861 0.4521 0.2251  0.0680  0.1010  101 PRO   B N   
988  C  CA  . PRO   B 92  ? 0.7163 0.5962 0.4640 0.2071  0.0812  0.1138  101 PRO   B CA  
989  C  C   . PRO   B 92  ? 0.7387 0.5929 0.4850 0.1961  0.0860  0.1172  101 PRO   B C   
990  O  O   . PRO   B 92  ? 0.7552 0.5867 0.4875 0.2088  0.0819  0.1138  101 PRO   B O   
991  C  CB  . PRO   B 92  ? 0.7234 0.6170 0.4578 0.2201  0.0907  0.1283  101 PRO   B CB  
992  C  CG  . PRO   B 92  ? 0.7377 0.6237 0.4508 0.2474  0.0818  0.1226  101 PRO   B CG  
993  C  CD  . PRO   B 92  ? 0.7177 0.5863 0.4335 0.2493  0.0677  0.1063  101 PRO   B CD  
994  N  N   . PRO   B 93  ? 0.7405 0.5966 0.4999 0.1734  0.0935  0.1232  102 PRO   B N   
995  C  CA  . PRO   B 93  ? 0.7623 0.5878 0.5168 0.1631  0.0969  0.1257  102 PRO   B CA  
996  C  C   . PRO   B 93  ? 0.7985 0.6016 0.5294 0.1759  0.1042  0.1387  102 PRO   B C   
997  O  O   . PRO   B 93  ? 0.8051 0.6209 0.5297 0.1798  0.1139  0.1530  102 PRO   B O   
998  C  CB  . PRO   B 93  ? 0.7564 0.5915 0.5289 0.1359  0.1029  0.1309  102 PRO   B CB  
999  C  CG  . PRO   B 93  ? 0.7380 0.6085 0.5280 0.1328  0.0987  0.1248  102 PRO   B CG  
1000 C  CD  . PRO   B 93  ? 0.7166 0.6012 0.4953 0.1564  0.0974  0.1265  102 PRO   B CD  
1001 N  N   . GLY   B 94  ? 0.8165 0.5880 0.5332 0.1849  0.0996  0.1334  103 GLY   B N   
1002 C  CA  . GLY   B 94  ? 0.8385 0.5822 0.5285 0.1998  0.1046  0.1441  103 GLY   B CA  
1003 C  C   . GLY   B 94  ? 0.8493 0.6008 0.5215 0.2269  0.1024  0.1464  103 GLY   B C   
1004 O  O   . GLY   B 94  ? 0.8661 0.5963 0.5130 0.2417  0.1070  0.1565  103 GLY   B O   
1005 N  N   . GLU   B 95  ? 0.8411 0.6212 0.5234 0.2340  0.0955  0.1379  104 GLU   B N   
1006 C  CA  . GLU   B 95  ? 0.8520 0.6398 0.5167 0.2596  0.0917  0.1384  104 GLU   B CA  
1007 C  C   . GLU   B 95  ? 0.8540 0.6452 0.5233 0.2720  0.0744  0.1191  104 GLU   B C   
1008 O  O   . GLU   B 95  ? 0.8445 0.6443 0.5353 0.2583  0.0679  0.1071  104 GLU   B O   
1009 C  CB  . GLU   B 95  ? 0.8702 0.6888 0.5393 0.2586  0.0995  0.1475  104 GLU   B CB  
1010 C  CG  . GLU   B 95  ? 0.9321 0.7550 0.6029 0.2429  0.1176  0.1674  104 GLU   B CG  
1011 C  CD  . GLU   B 95  ? 1.0188 0.8780 0.6968 0.2424  0.1265  0.1769  104 GLU   B CD  
1012 O  OE1 . GLU   B 95  ? 1.0412 0.9196 0.7205 0.2556  0.1179  0.1673  104 GLU   B OE1 
1013 O  OE2 . GLU   B 95  ? 1.0374 0.9060 0.7200 0.2289  0.1419  0.1941  104 GLU   B OE2 
1014 N  N   . ARG   B 96  ? 0.8668 0.6513 0.5153 0.2973  0.0669  0.1163  105 ARG   B N   
1015 C  CA  . ARG   B 96  ? 0.8821 0.6687 0.5326 0.3110  0.0493  0.0989  105 ARG   B CA  
1016 C  C   . ARG   B 96  ? 0.8793 0.6897 0.5443 0.3068  0.0422  0.0901  105 ARG   B C   
1017 O  O   . ARG   B 96  ? 0.8821 0.7071 0.5446 0.3056  0.0496  0.0987  105 ARG   B O   
1018 C  CB  . ARG   B 96  ? 0.9316 0.7043 0.5519 0.3402  0.0439  0.1007  105 ARG   B CB  
1019 C  CG  . ARG   B 96  ? 1.0059 0.7833 0.6247 0.3573  0.0242  0.0837  105 ARG   B CG  
1020 C  CD  . ARG   B 96  ? 1.0954 0.8538 0.6944 0.3800  0.0146  0.0792  105 ARG   B CD  
1021 N  NE  . ARG   B 96  ? 1.1849 0.9242 0.7516 0.3956  0.0254  0.0956  105 ARG   B NE  
1022 C  CZ  . ARG   B 96  ? 1.2528 0.9921 0.7931 0.4151  0.0271  0.1029  105 ARG   B CZ  
1023 N  NH1 . ARG   B 96  ? 1.2699 0.9909 0.7801 0.4283  0.0388  0.1192  105 ARG   B NH1 
1024 N  NH2 . ARG   B 96  ? 1.2566 1.0123 0.7979 0.4221  0.0176  0.0944  105 ARG   B NH2 
1025 N  N   . ALA   B 97  ? 0.8712 0.6858 0.5512 0.3047  0.0279  0.0735  106 ALA   B N   
1026 C  CA  . ALA   B 97  ? 0.8666 0.6974 0.5577 0.3013  0.0189  0.0640  106 ALA   B CA  
1027 C  C   . ALA   B 97  ? 0.8837 0.7162 0.5517 0.3231  0.0142  0.0661  106 ALA   B C   
1028 O  O   . ALA   B 97  ? 0.9065 0.7269 0.5534 0.3439  0.0093  0.0663  106 ALA   B O   
1029 C  CB  . ALA   B 97  ? 0.8614 0.6925 0.5679 0.2987  0.0043  0.0475  106 ALA   B CB  
1030 N  N   . LYS   B 98  ? 0.8771 0.7235 0.5461 0.3206  0.0159  0.0679  107 LYS   B N   
1031 C  CA  . LYS   B 98  ? 0.8942 0.7421 0.5384 0.3431  0.0130  0.0706  107 LYS   B CA  
1032 C  C   . LYS   B 98  ? 0.8824 0.7394 0.5291 0.3430  0.0042  0.0627  107 LYS   B C   
1033 O  O   . LYS   B 98  ? 0.8782 0.7487 0.5420 0.3260  0.0101  0.0647  107 LYS   B O   
1034 C  CB  . LYS   B 98  ? 0.9382 0.7927 0.5702 0.3470  0.0320  0.0896  107 LYS   B CB  
1035 C  CG  . LYS   B 98  ? 1.0101 0.8753 0.6202 0.3669  0.0357  0.0965  107 LYS   B CG  
1036 C  CD  . LYS   B 98  ? 1.0710 0.9501 0.6789 0.3629  0.0579  0.1171  107 LYS   B CD  
1037 C  CE  . LYS   B 98  ? 1.1030 0.9960 0.7418 0.3323  0.0686  0.1228  107 LYS   B CE  
1038 N  NZ  . LYS   B 98  ? 1.1228 1.0442 0.7668 0.3284  0.0837  0.1366  107 LYS   B NZ  
1039 N  N   . ASN   B 99  ? 0.8770 0.7239 0.5056 0.3620  -0.0116 0.0525  108 ASN   B N   
1040 C  CA  . ASN   B 99  ? 0.8777 0.7254 0.5035 0.3640  -0.0226 0.0438  108 ASN   B CA  
1041 C  C   . ASN   B 99  ? 0.8883 0.7453 0.4930 0.3808  -0.0150 0.0528  108 ASN   B C   
1042 O  O   . ASN   B 99  ? 0.9116 0.7640 0.4901 0.4042  -0.0138 0.0573  108 ASN   B O   
1043 C  CB  . ASN   B 99  ? 0.8926 0.7224 0.5073 0.3762  -0.0447 0.0280  108 ASN   B CB  
1044 C  CG  . ASN   B 99  ? 0.9347 0.7606 0.5735 0.3597  -0.0542 0.0173  108 ASN   B CG  
1045 O  OD1 . ASN   B 99  ? 0.9558 0.7829 0.6039 0.3561  -0.0488 0.0200  108 ASN   B OD1 
1046 N  ND2 . ASN   B 99  ? 0.9357 0.7566 0.5845 0.3502  -0.0684 0.0052  108 ASN   B ND2 
1047 N  N   . ILE   B 100 ? 0.8698 0.7410 0.4845 0.3711  -0.0098 0.0554  109 ILE   B N   
1048 C  CA  . ILE   B 100 ? 0.8706 0.7554 0.4673 0.3883  -0.0027 0.0633  109 ILE   B CA  
1049 C  C   . ILE   B 100 ? 0.8718 0.7485 0.4598 0.3941  -0.0173 0.0520  109 ILE   B C   
1050 O  O   . ILE   B 100 ? 0.8652 0.7460 0.4722 0.3751  -0.0186 0.0488  109 ILE   B O   
1051 C  CB  . ILE   B 100 ? 0.8615 0.7747 0.4772 0.3736  0.0177  0.0784  109 ILE   B CB  
1052 C  CG1 . ILE   B 100 ? 0.8679 0.7833 0.4930 0.3632  0.0315  0.0896  109 ILE   B CG1 
1053 C  CG2 . ILE   B 100 ? 0.8666 0.8002 0.4662 0.3929  0.0255  0.0866  109 ILE   B CG2 
1054 C  CD1 . ILE   B 100 ? 0.8923 0.8026 0.4907 0.3863  0.0375  0.0983  109 ILE   B CD1 
1055 N  N   . GLN   B 101 ? 0.8786 0.7412 0.4349 0.4211  -0.0284 0.0462  110 GLN   B N   
1056 C  CA  . GLN   B 101 ? 0.8873 0.7349 0.4287 0.4296  -0.0439 0.0350  110 GLN   B CA  
1057 C  C   . GLN   B 101 ? 0.8901 0.7584 0.4244 0.4398  -0.0339 0.0430  110 GLN   B C   
1058 O  O   . GLN   B 101 ? 0.8888 0.7775 0.4119 0.4565  -0.0201 0.0545  110 GLN   B O   
1059 C  CB  . GLN   B 101 ? 0.9222 0.7422 0.4304 0.4549  -0.0624 0.0236  110 GLN   B CB  
1060 C  CG  . GLN   B 101 ? 0.9729 0.7700 0.4608 0.4648  -0.0805 0.0113  110 GLN   B CG  
1061 C  CD  . GLN   B 101 ? 1.0179 0.7819 0.4840 0.4771  -0.1040 -0.0041 110 GLN   B CD  
1062 O  OE1 . GLN   B 101 ? 1.0142 0.7725 0.4915 0.4692  -0.1101 -0.0088 110 GLN   B OE1 
1063 N  NE2 . GLN   B 101 ? 1.0342 0.7753 0.4684 0.4973  -0.1188 -0.0131 110 GLN   B NE2 
1064 N  N   . THR   B 102 ? 0.8935 0.7583 0.4341 0.4302  -0.0404 0.0375  111 THR   B N   
1065 C  CA  . THR   B 102 ? 0.8915 0.7777 0.4269 0.4403  -0.0324 0.0439  111 THR   B CA  
1066 C  C   . THR   B 102 ? 0.8991 0.7624 0.4222 0.4422  -0.0485 0.0328  111 THR   B C   
1067 O  O   . THR   B 102 ? 0.9094 0.7454 0.4379 0.4262  -0.0623 0.0225  111 THR   B O   
1068 C  CB  . THR   B 102 ? 0.8917 0.8134 0.4623 0.4164  -0.0135 0.0564  111 THR   B CB  
1069 O  OG1 . THR   B 102 ? 0.9013 0.8510 0.4694 0.4278  -0.0051 0.0633  111 THR   B OG1 
1070 C  CG2 . THR   B 102 ? 0.8916 0.8047 0.4896 0.3848  -0.0177 0.0509  111 THR   B CG2 
1071 N  N   . LEU   B 103 ? 0.8935 0.7674 0.3993 0.4621  -0.0470 0.0351  112 LEU   B N   
1072 C  CA  . LEU   B 103 ? 0.9083 0.7584 0.4009 0.4634  -0.0614 0.0259  112 LEU   B CA  
1073 C  C   . LEU   B 103 ? 0.9014 0.7804 0.4218 0.4443  -0.0499 0.0334  112 LEU   B C   
1074 O  O   . LEU   B 103 ? 0.8897 0.8084 0.4192 0.4514  -0.0346 0.0443  112 LEU   B O   
1075 C  CB  . LEU   B 103 ? 0.9317 0.7687 0.3830 0.4997  -0.0703 0.0213  112 LEU   B CB  
1076 C  CG  . LEU   B 103 ? 0.9711 0.7754 0.4064 0.4993  -0.0867 0.0117  112 LEU   B CG  
1077 C  CD1 . LEU   B 103 ? 1.0026 0.7553 0.4216 0.4934  -0.1085 -0.0024 112 LEU   B CD1 
1078 C  CD2 . LEU   B 103 ? 0.9859 0.7947 0.3902 0.5325  -0.0881 0.0119  112 LEU   B CD2 
1079 N  N   . PRO   B 104 ? 0.8997 0.7610 0.4339 0.4198  -0.0571 0.0281  113 PRO   B N   
1080 C  CA  . PRO   B 104 ? 0.8856 0.7727 0.4440 0.4024  -0.0475 0.0343  113 PRO   B CA  
1081 C  C   . PRO   B 104 ? 0.9030 0.7967 0.4426 0.4224  -0.0503 0.0347  113 PRO   B C   
1082 O  O   . PRO   B 104 ? 0.9248 0.7884 0.4305 0.4442  -0.0641 0.0271  113 PRO   B O   
1083 C  CB  . PRO   B 104 ? 0.8935 0.7551 0.4662 0.3737  -0.0552 0.0278  113 PRO   B CB  
1084 C  CG  . PRO   B 104 ? 0.9101 0.7410 0.4744 0.3729  -0.0662 0.0197  113 PRO   B CG  
1085 C  CD  . PRO   B 104 ? 0.9053 0.7254 0.4359 0.4056  -0.0734 0.0167  113 PRO   B CD  
1086 N  N   . GLY   B 105 ? 0.8846 0.8178 0.4464 0.4150  -0.0379 0.0431  114 GLY   B N   
1087 C  CA  . GLY   B 105 ? 0.8828 0.8303 0.4350 0.4296  -0.0393 0.0442  114 GLY   B CA  
1088 C  C   . GLY   B 105 ? 0.8837 0.8114 0.4420 0.4086  -0.0468 0.0397  114 GLY   B C   
1089 O  O   . GLY   B 105 ? 0.8918 0.7866 0.4529 0.3887  -0.0535 0.0342  114 GLY   B O   
1090 N  N   . ILE   B 106 ? 0.8716 0.8212 0.4326 0.4130  -0.0452 0.0424  115 ILE   B N   
1091 C  CA  . ILE   B 106 ? 0.8835 0.8142 0.4447 0.3972  -0.0522 0.0390  115 ILE   B CA  
1092 C  C   . ILE   B 106 ? 0.8623 0.8375 0.4529 0.3838  -0.0422 0.0453  115 ILE   B C   
1093 O  O   . ILE   B 106 ? 0.8560 0.8730 0.4529 0.3996  -0.0358 0.0506  115 ILE   B O   
1094 C  CB  . ILE   B 106 ? 0.9207 0.8209 0.4415 0.4236  -0.0665 0.0334  115 ILE   B CB  
1095 C  CG1 . ILE   B 106 ? 0.9732 0.8266 0.4588 0.4415  -0.0794 0.0258  115 ILE   B CG1 
1096 C  CG2 . ILE   B 106 ? 0.9414 0.8180 0.4574 0.4091  -0.0735 0.0311  115 ILE   B CG2 
1097 C  CD1 . ILE   B 106 ? 1.0100 0.8225 0.4971 0.4183  -0.0866 0.0203  115 ILE   B CD1 
1098 N  N   . PHE   B 107 ? 0.8488 0.8143 0.4549 0.3565  -0.0424 0.0441  116 PHE   B N   
1099 C  CA  . PHE   B 107 ? 0.8237 0.8206 0.4507 0.3440  -0.0377 0.0473  116 PHE   B CA  
1100 C  C   . PHE   B 107 ? 0.8477 0.8130 0.4458 0.3531  -0.0502 0.0425  116 PHE   B C   
1101 O  O   . PHE   B 107 ? 0.8687 0.7910 0.4547 0.3402  -0.0566 0.0384  116 PHE   B O   
1102 C  CB  . PHE   B 107 ? 0.8034 0.8001 0.4581 0.3101  -0.0314 0.0477  116 PHE   B CB  
1103 C  CG  . PHE   B 107 ? 0.7792 0.8132 0.4667 0.2965  -0.0182 0.0537  116 PHE   B CG  
1104 C  CD1 . PHE   B 107 ? 0.7743 0.8361 0.4657 0.3121  -0.0111 0.0595  116 PHE   B CD1 
1105 C  CD2 . PHE   B 107 ? 0.7732 0.8118 0.4852 0.2687  -0.0127 0.0540  116 PHE   B CD2 
1106 C  CE1 . PHE   B 107 ? 0.7589 0.8506 0.4785 0.2980  0.0015  0.0664  116 PHE   B CE1 
1107 C  CE2 . PHE   B 107 ? 0.7616 0.8283 0.5006 0.2557  -0.0015 0.0596  116 PHE   B CE2 
1108 C  CZ  . PHE   B 107 ? 0.7487 0.8405 0.4914 0.2694  0.0057  0.0663  116 PHE   B CZ  
1109 N  N   . LYS   B 108 ? 0.8491 0.8340 0.4346 0.3762  -0.0538 0.0434  117 LYS   B N   
1110 C  CA  . LYS   B 108 ? 0.8812 0.8343 0.4361 0.3866  -0.0659 0.0397  117 LYS   B CA  
1111 C  C   . LYS   B 108 ? 0.8695 0.8447 0.4445 0.3679  -0.0631 0.0413  117 LYS   B C   
1112 O  O   . LYS   B 108 ? 0.8404 0.8677 0.4407 0.3687  -0.0566 0.0448  117 LYS   B O   
1113 C  CB  . LYS   B 108 ? 0.9208 0.8846 0.4496 0.4246  -0.0722 0.0391  117 LYS   B CB  
1114 C  CG  . LYS   B 108 ? 0.9976 0.9534 0.5089 0.4480  -0.0730 0.0379  117 LYS   B CG  
1115 C  CD  . LYS   B 108 ? 1.0795 1.0565 0.5685 0.4876  -0.0770 0.0379  117 LYS   B CD  
1116 C  CE  . LYS   B 108 ? 1.1192 1.1553 0.6315 0.5000  -0.0638 0.0439  117 LYS   B CE  
1117 N  NZ  . LYS   B 108 ? 1.1550 1.2113 0.6431 0.5422  -0.0670 0.0434  117 LYS   B NZ  
1118 N  N   . THR   B 109 ? 0.8950 0.8324 0.4599 0.3502  -0.0676 0.0390  118 THR   B N   
1119 C  CA  . THR   B 109 ? 0.9007 0.8538 0.4796 0.3333  -0.0658 0.0397  118 THR   B CA  
1120 C  C   . THR   B 109 ? 0.9400 0.8587 0.4829 0.3444  -0.0769 0.0380  118 THR   B C   
1121 O  O   . THR   B 109 ? 0.9692 0.8466 0.4769 0.3616  -0.0856 0.0364  118 THR   B O   
1122 C  CB  . THR   B 109 ? 0.9127 0.8598 0.5167 0.2992  -0.0577 0.0397  118 THR   B CB  
1123 O  OG1 . THR   B 109 ? 0.9528 0.8485 0.5356 0.2885  -0.0620 0.0377  118 THR   B OG1 
1124 C  CG2 . THR   B 109 ? 0.8985 0.8631 0.5286 0.2897  -0.0485 0.0412  118 THR   B CG2 
1125 N  N   . LYS   B 110 ? 0.9380 0.8702 0.4868 0.3349  -0.0771 0.0383  119 LYS   B N   
1126 C  CA  . LYS   B 110 ? 0.9760 0.8737 0.4888 0.3446  -0.0868 0.0377  119 LYS   B CA  
1127 C  C   . LYS   B 110 ? 1.0214 0.8580 0.5121 0.3278  -0.0879 0.0382  119 LYS   B C   
1128 O  O   . LYS   B 110 ? 1.0593 0.8546 0.5129 0.3372  -0.0960 0.0389  119 LYS   B O   
1129 C  CB  . LYS   B 110 ? 0.9728 0.9027 0.4973 0.3394  -0.0872 0.0375  119 LYS   B CB  
1130 C  CG  . LYS   B 110 ? 1.0049 0.9343 0.5507 0.3070  -0.0795 0.0373  119 LYS   B CG  
1131 C  CD  . LYS   B 110 ? 1.0373 1.0031 0.5961 0.3037  -0.0814 0.0357  119 LYS   B CD  
1132 C  CE  . LYS   B 110 ? 1.0914 1.0334 0.6444 0.2822  -0.0791 0.0350  119 LYS   B CE  
1133 N  NZ  . LYS   B 110 ? 1.1073 1.0623 0.6940 0.2544  -0.0684 0.0339  119 LYS   B NZ  
1134 N  N   . ASP   B 111 ? 1.0146 0.8464 0.5281 0.3033  -0.0797 0.0381  120 ASP   B N   
1135 C  CA  . ASP   B 111 ? 1.0431 0.8267 0.5441 0.2848  -0.0792 0.0387  120 ASP   B CA  
1136 C  C   . ASP   B 111 ? 1.0660 0.8239 0.5628 0.2862  -0.0817 0.0369  120 ASP   B C   
1137 O  O   . ASP   B 111 ? 1.0885 0.8163 0.5859 0.2668  -0.0800 0.0370  120 ASP   B O   
1138 C  CB  . ASP   B 111 ? 1.0481 0.8466 0.5784 0.2554  -0.0684 0.0392  120 ASP   B CB  
1139 C  CG  . ASP   B 111 ? 1.0948 0.9080 0.6230 0.2521  -0.0676 0.0400  120 ASP   B CG  
1140 O  OD1 . ASP   B 111 ? 1.1316 0.9179 0.6262 0.2634  -0.0747 0.0418  120 ASP   B OD1 
1141 O  OD2 . ASP   B 111 ? 1.0869 0.9361 0.6448 0.2390  -0.0608 0.0386  120 ASP   B OD2 
1142 N  N   . GLY   B 112 ? 1.0530 0.8245 0.5462 0.3091  -0.0856 0.0351  121 GLY   B N   
1143 C  CA  . GLY   B 112 ? 1.0621 0.8085 0.5475 0.3137  -0.0898 0.0322  121 GLY   B CA  
1144 C  C   . GLY   B 112 ? 1.0347 0.8198 0.5458 0.3195  -0.0836 0.0314  121 GLY   B C   
1145 O  O   . GLY   B 112 ? 1.0079 0.8411 0.5481 0.3153  -0.0744 0.0339  121 GLY   B O   
1146 N  N   . ASP   B 113 ? 1.0401 0.8023 0.5391 0.3287  -0.0892 0.0281  122 ASP   B N   
1147 C  CA  . ASP   B 113 ? 1.0213 0.8128 0.5379 0.3367  -0.0839 0.0277  122 ASP   B CA  
1148 C  C   . ASP   B 113 ? 1.0080 0.8012 0.5528 0.3110  -0.0772 0.0270  122 ASP   B C   
1149 O  O   . ASP   B 113 ? 1.0302 0.7887 0.5713 0.2939  -0.0814 0.0244  122 ASP   B O   
1150 C  CB  . ASP   B 113 ? 1.0617 0.8269 0.5452 0.3651  -0.0949 0.0235  122 ASP   B CB  
1151 C  CG  . ASP   B 113 ? 1.1264 0.8959 0.5818 0.3972  -0.1010 0.0237  122 ASP   B CG  
1152 O  OD1 . ASP   B 113 ? 1.1082 0.9102 0.5743 0.3983  -0.0960 0.0275  122 ASP   B OD1 
1153 O  OD2 . ASP   B 113 ? 1.1878 0.9286 0.6097 0.4225  -0.1115 0.0194  122 ASP   B OD2 
1154 N  N   . ILE   B 114 ? 0.9650 0.7991 0.5377 0.3087  -0.0666 0.0297  123 ILE   B N   
1155 C  CA  . ILE   B 114 ? 0.9469 0.7868 0.5456 0.2887  -0.0597 0.0294  123 ILE   B CA  
1156 C  C   . ILE   B 114 ? 0.9248 0.7803 0.5240 0.3061  -0.0576 0.0300  123 ILE   B C   
1157 O  O   . ILE   B 114 ? 0.9139 0.7972 0.5097 0.3256  -0.0542 0.0336  123 ILE   B O   
1158 C  CB  . ILE   B 114 ? 0.9345 0.8089 0.5662 0.2673  -0.0473 0.0335  123 ILE   B CB  
1159 C  CG1 . ILE   B 114 ? 0.9634 0.8305 0.5915 0.2559  -0.0485 0.0337  123 ILE   B CG1 
1160 C  CG2 . ILE   B 114 ? 0.9327 0.8070 0.5874 0.2473  -0.0412 0.0325  123 ILE   B CG2 
1161 C  CD1 . ILE   B 114 ? 0.9668 0.8714 0.6217 0.2421  -0.0388 0.0368  123 ILE   B CD1 
1162 N  N   . GLY   B 115 ? 0.9133 0.7534 0.5168 0.2999  -0.0593 0.0268  124 GLY   B N   
1163 C  CA  . GLY   B 115 ? 0.9038 0.7578 0.5068 0.3157  -0.0564 0.0279  124 GLY   B CA  
1164 C  C   . GLY   B 115 ? 0.8724 0.7712 0.5044 0.3083  -0.0407 0.0358  124 GLY   B C   
1165 O  O   . GLY   B 115 ? 0.8665 0.7788 0.5218 0.2862  -0.0337 0.0380  124 GLY   B O   
1166 N  N   . ALA   B 116 ? 0.8533 0.7747 0.4832 0.3264  -0.0347 0.0404  125 ALA   B N   
1167 C  CA  . ALA   B 116 ? 0.8256 0.7879 0.4823 0.3181  -0.0194 0.0493  125 ALA   B CA  
1168 C  C   . ALA   B 116 ? 0.8256 0.7943 0.4788 0.3307  -0.0138 0.0530  125 ALA   B C   
1169 O  O   . ALA   B 116 ? 0.8386 0.7982 0.4664 0.3559  -0.0192 0.0512  125 ALA   B O   
1170 C  CB  . ALA   B 116 ? 0.8067 0.8057 0.4692 0.3260  -0.0138 0.0551  125 ALA   B CB  
1171 N  N   . VAL   B 117 ? 0.8155 0.7969 0.4909 0.3146  -0.0034 0.0581  126 VAL   B N   
1172 C  CA  A VAL   B 117 ? 0.8254 0.8113 0.4960 0.3259  0.0029  0.0631  126 VAL   B CA  
1173 C  CA  B VAL   B 117 ? 0.8236 0.8090 0.4948 0.3250  0.0029  0.0629  126 VAL   B CA  
1174 C  C   . VAL   B 117 ? 0.8175 0.8455 0.5049 0.3252  0.0195  0.0760  126 VAL   B C   
1175 O  O   . VAL   B 117 ? 0.8064 0.8532 0.5201 0.3027  0.0275  0.0806  126 VAL   B O   
1176 C  CB  A VAL   B 117 ? 0.8368 0.7983 0.5124 0.3135  0.0003  0.0588  126 VAL   B CB  
1177 C  CB  B VAL   B 117 ? 0.8297 0.7922 0.5102 0.3083  0.0009  0.0587  126 VAL   B CB  
1178 C  CG1 A VAL   B 117 ? 0.8604 0.7843 0.5150 0.3217  -0.0168 0.0469  126 VAL   B CG1 
1179 C  CG1 B VAL   B 117 ? 0.8292 0.8032 0.5156 0.3094  0.0123  0.0672  126 VAL   B CG1 
1180 C  CG2 A VAL   B 117 ? 0.8345 0.7995 0.5379 0.2840  0.0053  0.0590  126 VAL   B CG2 
1181 C  CG2 B VAL   B 117 ? 0.8522 0.7772 0.5119 0.3168  -0.0155 0.0472  126 VAL   B CG2 
1182 N  N   . ALA   B 118 ? 0.8211 0.8647 0.4925 0.3502  0.0245  0.0820  127 ALA   B N   
1183 C  CA  . ALA   B 118 ? 0.8202 0.9075 0.5078 0.3503  0.0414  0.0958  127 ALA   B CA  
1184 C  C   . ALA   B 118 ? 0.8404 0.9255 0.5284 0.3490  0.0518  0.1040  127 ALA   B C   
1185 O  O   . ALA   B 118 ? 0.8502 0.9376 0.5171 0.3728  0.0556  0.1084  127 ALA   B O   
1186 C  CB  . ALA   B 118 ? 0.8227 0.9351 0.4940 0.3794  0.0430  0.0990  127 ALA   B CB  
1187 N  N   . LEU   B 119 ? 0.8407 0.9172 0.5490 0.3226  0.0556  0.1053  128 LEU   B N   
1188 C  CA  . LEU   B 119 ? 0.8417 0.9116 0.5509 0.3181  0.0650  0.1132  128 LEU   B CA  
1189 C  C   . LEU   B 119 ? 0.8261 0.9138 0.5665 0.2885  0.0763  0.1213  128 LEU   B C   
1190 O  O   . LEU   B 119 ? 0.8201 0.9048 0.5773 0.2686  0.0708  0.1147  128 LEU   B O   
1191 C  CB  . LEU   B 119 ? 0.8628 0.8907 0.5590 0.3184  0.0530  0.1023  128 LEU   B CB  
1192 C  CG  . LEU   B 119 ? 0.8936 0.8984 0.5580 0.3460  0.0398  0.0932  128 LEU   B CG  
1193 C  CD1 . LEU   B 119 ? 0.9082 0.8771 0.5675 0.3411  0.0273  0.0822  128 LEU   B CD1 
1194 C  CD2 . LEU   B 119 ? 0.9044 0.9204 0.5465 0.3725  0.0484  0.1027  128 LEU   B CD2 
1195 N  N   . ASP   B 120 ? 0.8209 0.9265 0.5675 0.2854  0.0919  0.1360  129 ASP   B N   
1196 C  CA  . ASP   B 120 ? 0.8112 0.9318 0.5862 0.2563  0.1021  0.1444  129 ASP   B CA  
1197 C  C   . ASP   B 120 ? 0.8043 0.8929 0.5786 0.2425  0.1041  0.1454  129 ASP   B C   
1198 O  O   . ASP   B 120 ? 0.8177 0.8941 0.5744 0.2553  0.1099  0.1524  129 ASP   B O   
1199 C  CB  . ASP   B 120 ? 0.8355 0.9983 0.6213 0.2574  0.1190  0.1614  129 ASP   B CB  
1200 C  CG  . ASP   B 120 ? 0.9204 1.1213 0.7348 0.2415  0.1202  0.1624  129 ASP   B CG  
1201 O  OD1 . ASP   B 120 ? 0.9420 1.1424 0.7796 0.2126  0.1213  0.1630  129 ASP   B OD1 
1202 O  OD2 . ASP   B 120 ? 0.9378 1.1678 0.7498 0.2591  0.1186  0.1616  129 ASP   B OD2 
1203 N  N   . TYR   B 121 ? 0.7797 0.8553 0.5713 0.2179  0.0998  0.1391  130 TYR   B N   
1204 C  CA  . TYR   B 121 ? 0.7779 0.8217 0.5684 0.2055  0.1008  0.1388  130 TYR   B CA  
1205 C  C   . TYR   B 121 ? 0.7510 0.7968 0.5655 0.1751  0.1040  0.1401  130 TYR   B C   
1206 O  O   . TYR   B 121 ? 0.7367 0.8032 0.5683 0.1637  0.1007  0.1360  130 TYR   B O   
1207 C  CB  . TYR   B 121 ? 0.8001 0.8115 0.5774 0.2141  0.0864  0.1234  130 TYR   B CB  
1208 C  CG  . TYR   B 121 ? 0.8336 0.8301 0.5849 0.2402  0.0834  0.1232  130 TYR   B CG  
1209 C  CD1 . TYR   B 121 ? 0.8607 0.8382 0.5997 0.2450  0.0890  0.1298  130 TYR   B CD1 
1210 C  CD2 . TYR   B 121 ? 0.8536 0.8536 0.5896 0.2614  0.0746  0.1166  130 TYR   B CD2 
1211 C  CE1 . TYR   B 121 ? 0.8907 0.8560 0.6038 0.2707  0.0858  0.1298  130 TYR   B CE1 
1212 C  CE2 . TYR   B 121 ? 0.8821 0.8683 0.5922 0.2864  0.0707  0.1158  130 TYR   B CE2 
1213 C  CZ  . TYR   B 121 ? 0.9084 0.8786 0.6074 0.2912  0.0764  0.1224  130 TYR   B CZ  
1214 O  OH  . TYR   B 121 ? 0.9554 0.9111 0.6269 0.3169  0.0712  0.1208  130 TYR   B OH  
1215 N  N   . PRO   B 122 ? 0.7411 0.7624 0.5549 0.1628  0.1090  0.1445  131 PRO   B N   
1216 C  CA  . PRO   B 122 ? 0.7222 0.7396 0.5553 0.1346  0.1102  0.1440  131 PRO   B CA  
1217 C  C   . PRO   B 122 ? 0.7059 0.7139 0.5461 0.1264  0.0974  0.1274  131 PRO   B C   
1218 O  O   . PRO   B 122 ? 0.7139 0.7072 0.5426 0.1401  0.0885  0.1167  131 PRO   B O   
1219 C  CB  . PRO   B 122 ? 0.7470 0.7303 0.5688 0.1300  0.1159  0.1502  131 PRO   B CB  
1220 C  CG  . PRO   B 122 ? 0.7622 0.7448 0.5628 0.1536  0.1228  0.1605  131 PRO   B CG  
1221 C  CD  . PRO   B 122 ? 0.7459 0.7403 0.5385 0.1754  0.1132  0.1502  131 PRO   B CD  
1222 N  N   . ALA   B 123 ? 0.6794 0.6963 0.5383 0.1039  0.0964  0.1253  132 ALA   B N   
1223 C  CA  . ALA   B 123 ? 0.6703 0.6799 0.5344 0.0960  0.0856  0.1105  132 ALA   B CA  
1224 C  C   . ALA   B 123 ? 0.6804 0.6538 0.5323 0.0998  0.0798  0.1000  132 ALA   B C   
1225 O  O   . ALA   B 123 ? 0.6784 0.6476 0.5285 0.1033  0.0714  0.0885  132 ALA   B O   
1226 C  CB  . ALA   B 123 ? 0.6565 0.6771 0.5396 0.0713  0.0856  0.1105  132 ALA   B CB  
1227 N  N   . GLY   B 124 ? 0.6838 0.6326 0.5263 0.1009  0.0847  0.1049  133 GLY   B N   
1228 C  CA  . GLY   B 124 ? 0.6866 0.6045 0.5178 0.1076  0.0796  0.0958  133 GLY   B CA  
1229 C  C   . GLY   B 124 ? 0.6766 0.5931 0.4966 0.1294  0.0737  0.0900  133 GLY   B C   
1230 O  O   . GLY   B 124 ? 0.6855 0.5827 0.4997 0.1353  0.0684  0.0814  133 GLY   B O   
1231 N  N   . THR   B 125 ? 0.6635 0.6004 0.4801 0.1422  0.0739  0.0944  134 THR   B N   
1232 C  CA  . THR   B 125 ? 0.6677 0.6017 0.4723 0.1623  0.0661  0.0880  134 THR   B CA  
1233 C  C   . THR   B 125 ? 0.6481 0.5872 0.4590 0.1589  0.0567  0.0761  134 THR   B C   
1234 O  O   . THR   B 125 ? 0.6569 0.5889 0.4600 0.1710  0.0485  0.0688  134 THR   B O   
1235 C  CB  . THR   B 125 ? 0.6961 0.6441 0.4885 0.1805  0.0702  0.0977  134 THR   B CB  
1236 O  OG1 . THR   B 125 ? 0.7148 0.6572 0.5011 0.1811  0.0808  0.1103  134 THR   B OG1 
1237 C  CG2 . THR   B 125 ? 0.7077 0.6462 0.4836 0.2024  0.0608  0.0907  134 THR   B CG2 
1238 N  N   . SER   B 126 ? 0.6253 0.5751 0.4492 0.1421  0.0572  0.0741  135 SER   B N   
1239 C  CA  . SER   B 126 ? 0.6148 0.5681 0.4424 0.1379  0.0497  0.0646  135 SER   B CA  
1240 C  C   . SER   B 126 ? 0.5946 0.5286 0.4193 0.1397  0.0434  0.0541  135 SER   B C   
1241 O  O   . SER   B 126 ? 0.5922 0.5128 0.4202 0.1329  0.0455  0.0512  135 SER   B O   
1242 C  CB  . SER   B 126 ? 0.6491 0.6103 0.4891 0.1188  0.0516  0.0636  135 SER   B CB  
1243 O  OG  . SER   B 126 ? 0.6956 0.6824 0.5425 0.1158  0.0545  0.0707  135 SER   B OG  
1244 N  N   . GLY   B 127 ? 0.5716 0.5046 0.3903 0.1483  0.0358  0.0486  136 GLY   B N   
1245 C  CA  . GLY   B 127 ? 0.5731 0.4925 0.3922 0.1487  0.0299  0.0394  136 GLY   B CA  
1246 C  C   . GLY   B 127 ? 0.5817 0.4926 0.3921 0.1646  0.0240  0.0375  136 GLY   B C   
1247 O  O   . GLY   B 127 ? 0.5873 0.4903 0.4002 0.1650  0.0177  0.0297  136 GLY   B O   
1248 N  N   . SER   B 128 ? 0.5752 0.4887 0.3756 0.1777  0.0260  0.0447  137 SER   B N   
1249 C  CA  . SER   B 128 ? 0.5792 0.4839 0.3674 0.1953  0.0193  0.0427  137 SER   B CA  
1250 C  C   . SER   B 128 ? 0.5924 0.4936 0.3737 0.2011  0.0080  0.0358  137 SER   B C   
1251 O  O   . SER   B 128 ? 0.5872 0.4953 0.3646 0.2007  0.0076  0.0377  137 SER   B O   
1252 C  CB  . SER   B 128 ? 0.5872 0.4965 0.3630 0.2088  0.0254  0.0531  137 SER   B CB  
1253 O  OG  . SER   B 128 ? 0.5829 0.4878 0.3614 0.2047  0.0342  0.0594  137 SER   B OG  
1254 N  N   . PRO   B 129 ? 0.6058 0.4957 0.3862 0.2058  -0.0019 0.0274  138 PRO   B N   
1255 C  CA  . PRO   B 129 ? 0.6147 0.4965 0.3882 0.2086  -0.0137 0.0207  138 PRO   B CA  
1256 C  C   . PRO   B 129 ? 0.6452 0.5217 0.3966 0.2282  -0.0204 0.0219  138 PRO   B C   
1257 O  O   . PRO   B 129 ? 0.6458 0.5227 0.3855 0.2441  -0.0190 0.0258  138 PRO   B O   
1258 C  CB  . PRO   B 129 ? 0.6179 0.4922 0.4003 0.2063  -0.0223 0.0115  138 PRO   B CB  
1259 C  CG  . PRO   B 129 ? 0.6250 0.5011 0.4089 0.2142  -0.0178 0.0138  138 PRO   B CG  
1260 C  CD  . PRO   B 129 ? 0.6021 0.4861 0.3882 0.2081  -0.0035 0.0234  138 PRO   B CD  
1261 N  N   . ILE   B 130 ? 0.6589 0.5277 0.4017 0.2283  -0.0282 0.0184  139 ILE   B N   
1262 C  CA  . ILE   B 130 ? 0.6865 0.5453 0.4052 0.2479  -0.0371 0.0173  139 ILE   B CA  
1263 C  C   . ILE   B 130 ? 0.7157 0.5529 0.4300 0.2473  -0.0535 0.0063  139 ILE   B C   
1264 O  O   . ILE   B 130 ? 0.7106 0.5424 0.4371 0.2297  -0.0563 0.0022  139 ILE   B O   
1265 C  CB  . ILE   B 130 ? 0.6872 0.5520 0.3971 0.2501  -0.0341 0.0218  139 ILE   B CB  
1266 C  CG1 . ILE   B 130 ? 0.6860 0.5765 0.4046 0.2489  -0.0186 0.0325  139 ILE   B CG1 
1267 C  CG2 . ILE   B 130 ? 0.7056 0.5558 0.3872 0.2723  -0.0451 0.0189  139 ILE   B CG2 
1268 C  CD1 . ILE   B 130 ? 0.6971 0.5996 0.4173 0.2438  -0.0149 0.0360  139 ILE   B CD1 
1269 N  N   . LEU   B 131 ? 0.7378 0.5634 0.4353 0.2655  -0.0640 0.0017  140 LEU   B N   
1270 C  CA  . LEU   B 131 ? 0.7622 0.5682 0.4569 0.2650  -0.0815 -0.0096 140 LEU   B CA  
1271 C  C   . LEU   B 131 ? 0.8032 0.5855 0.4687 0.2810  -0.0964 -0.0150 140 LEU   B C   
1272 O  O   . LEU   B 131 ? 0.8118 0.5941 0.4543 0.3025  -0.0945 -0.0111 140 LEU   B O   
1273 C  CB  . LEU   B 131 ? 0.7638 0.5724 0.4611 0.2746  -0.0856 -0.0132 140 LEU   B CB  
1274 C  CG  . LEU   B 131 ? 0.7684 0.5958 0.4845 0.2688  -0.0718 -0.0074 140 LEU   B CG  
1275 C  CD1 . LEU   B 131 ? 0.7746 0.5994 0.4880 0.2816  -0.0799 -0.0127 140 LEU   B CD1 
1276 C  CD2 . LEU   B 131 ? 0.7600 0.5973 0.5041 0.2438  -0.0651 -0.0080 140 LEU   B CD2 
1277 N  N   . ASP   B 132 ? 0.8245 0.5858 0.4903 0.2717  -0.1121 -0.0246 141 ASP   B N   
1278 C  CA  . ASP   B 132 ? 0.8635 0.5954 0.4995 0.2869  -0.1299 -0.0322 141 ASP   B CA  
1279 C  C   . ASP   B 132 ? 0.8971 0.6209 0.5264 0.3000  -0.1447 -0.0416 141 ASP   B C   
1280 O  O   . ASP   B 132 ? 0.8835 0.6260 0.5326 0.2964  -0.1398 -0.0413 141 ASP   B O   
1281 C  CB  . ASP   B 132 ? 0.8740 0.5824 0.5096 0.2691  -0.1396 -0.0366 141 ASP   B CB  
1282 C  CG  . ASP   B 132 ? 0.8871 0.5978 0.5527 0.2423  -0.1437 -0.0415 141 ASP   B CG  
1283 O  OD1 . ASP   B 132 ? 0.8716 0.5948 0.5535 0.2416  -0.1470 -0.0462 141 ASP   B OD1 
1284 O  OD2 . ASP   B 132 ? 0.9239 0.6246 0.5960 0.2228  -0.1433 -0.0402 141 ASP   B OD2 
1285 N  N   . LYS   B 133 ? 0.9347 0.6294 0.5346 0.3161  -0.1637 -0.0506 142 LYS   B N   
1286 C  CA  . LYS   B 133 ? 0.9618 0.6477 0.5518 0.3308  -0.1797 -0.0606 142 LYS   B CA  
1287 C  C   . LYS   B 133 ? 0.9486 0.6418 0.5711 0.3093  -0.1885 -0.0686 142 LYS   B C   
1288 O  O   . LYS   B 133 ? 0.9460 0.6436 0.5688 0.3202  -0.1974 -0.0750 142 LYS   B O   
1289 C  CB  . LYS   B 133 ? 1.0356 0.6852 0.5857 0.3516  -0.2002 -0.0703 142 LYS   B CB  
1290 C  CG  . LYS   B 133 ? 1.1374 0.7854 0.6529 0.3807  -0.1917 -0.0633 142 LYS   B CG  
1291 C  CD  . LYS   B 133 ? 1.2361 0.8560 0.7270 0.3839  -0.1986 -0.0649 142 LYS   B CD  
1292 C  CE  . LYS   B 133 ? 1.3119 0.9144 0.7567 0.4209  -0.2052 -0.0674 142 LYS   B CE  
1293 N  NZ  . LYS   B 133 ? 1.3697 0.9306 0.7846 0.4259  -0.2220 -0.0752 142 LYS   B NZ  
1294 N  N   . CYS   B 134 ? 0.9325 0.6303 0.5827 0.2800  -0.1849 -0.0676 143 CYS   B N   
1295 C  CA  . CYS   B 134 ? 0.9200 0.6320 0.6052 0.2590  -0.1905 -0.0739 143 CYS   B CA  
1296 C  C   . CYS   B 134 ? 0.8875 0.6349 0.6027 0.2510  -0.1714 -0.0665 143 CYS   B C   
1297 O  O   . CYS   B 134 ? 0.8767 0.6404 0.6225 0.2344  -0.1735 -0.0709 143 CYS   B O   
1298 C  CB  . CYS   B 134 ? 0.9450 0.6431 0.6440 0.2315  -0.1975 -0.0769 143 CYS   B CB  
1299 S  SG  . CYS   B 134 ? 1.0553 0.7044 0.7193 0.2376  -0.2241 -0.0876 143 CYS   B SG  
1300 N  N   . GLY   B 135 ? 0.8709 0.6301 0.5781 0.2616  -0.1531 -0.0556 144 GLY   B N   
1301 C  CA  . GLY   B 135 ? 0.8446 0.6315 0.5762 0.2538  -0.1352 -0.0485 144 GLY   B CA  
1302 C  C   . GLY   B 135 ? 0.8200 0.6178 0.5746 0.2285  -0.1220 -0.0431 144 GLY   B C   
1303 O  O   . GLY   B 135 ? 0.8084 0.6272 0.5839 0.2202  -0.1084 -0.0387 144 GLY   B O   
1304 N  N   . ARG   B 136 ? 0.8107 0.5921 0.5590 0.2171  -0.1262 -0.0434 145 ARG   B N   
1305 C  CA  . ARG   B 136 ? 0.7919 0.5807 0.5569 0.1946  -0.1140 -0.0377 145 ARG   B CA  
1306 C  C   . ARG   B 136 ? 0.7706 0.5680 0.5271 0.1998  -0.0970 -0.0271 145 ARG   B C   
1307 O  O   . ARG   B 136 ? 0.7771 0.5660 0.5091 0.2175  -0.0976 -0.0240 145 ARG   B O   
1308 C  CB  . ARG   B 136 ? 0.8257 0.5900 0.5827 0.1818  -0.1247 -0.0406 145 ARG   B CB  
1309 C  CG  . ARG   B 136 ? 0.8644 0.6274 0.6426 0.1646  -0.1374 -0.0492 145 ARG   B CG  
1310 C  CD  . ARG   B 136 ? 0.9227 0.6546 0.6878 0.1524  -0.1490 -0.0513 145 ARG   B CD  
1311 N  NE  . ARG   B 136 ? 1.0025 0.7036 0.7312 0.1738  -0.1640 -0.0557 145 ARG   B NE  
1312 C  CZ  . ARG   B 136 ? 1.0566 0.7246 0.7577 0.1751  -0.1705 -0.0546 145 ARG   B CZ  
1313 N  NH1 . ARG   B 136 ? 1.0527 0.7129 0.7582 0.1550  -0.1633 -0.0484 145 ARG   B NH1 
1314 N  NH2 . ARG   B 136 ? 1.0882 0.7295 0.7546 0.1982  -0.1841 -0.0595 145 ARG   B NH2 
1315 N  N   . VAL   B 137 ? 0.7453 0.5607 0.5220 0.1846  -0.0821 -0.0220 146 VAL   B N   
1316 C  CA  . VAL   B 137 ? 0.7290 0.5545 0.5012 0.1866  -0.0670 -0.0129 146 VAL   B CA  
1317 C  C   . VAL   B 137 ? 0.7283 0.5411 0.4869 0.1811  -0.0669 -0.0095 146 VAL   B C   
1318 O  O   . VAL   B 137 ? 0.7333 0.5431 0.5014 0.1634  -0.0653 -0.0098 146 VAL   B O   
1319 C  CB  . VAL   B 137 ? 0.7171 0.5635 0.5131 0.1741  -0.0531 -0.0101 146 VAL   B CB  
1320 C  CG1 . VAL   B 137 ? 0.7233 0.5793 0.5151 0.1753  -0.0394 -0.0015 146 VAL   B CG1 
1321 C  CG2 . VAL   B 137 ? 0.7119 0.5677 0.5194 0.1809  -0.0549 -0.0142 146 VAL   B CG2 
1322 N  N   . ILE   B 138 ? 0.7195 0.5247 0.4544 0.1980  -0.0689 -0.0064 147 ILE   B N   
1323 C  CA  . ILE   B 138 ? 0.7152 0.5076 0.4329 0.1979  -0.0700 -0.0034 147 ILE   B CA  
1324 C  C   . ILE   B 138 ? 0.6897 0.5016 0.4124 0.1942  -0.0555 0.0047  147 ILE   B C   
1325 O  O   . ILE   B 138 ? 0.6963 0.5008 0.4059 0.1944  -0.0558 0.0073  147 ILE   B O   
1326 C  CB  . ILE   B 138 ? 0.7352 0.5077 0.4220 0.2207  -0.0822 -0.0058 147 ILE   B CB  
1327 C  CG1 . ILE   B 138 ? 0.7444 0.5346 0.4241 0.2416  -0.0758 -0.0015 147 ILE   B CG1 
1328 C  CG2 . ILE   B 138 ? 0.7497 0.4976 0.4300 0.2212  -0.0995 -0.0154 147 ILE   B CG2 
1329 C  CD1 . ILE   B 138 ? 0.7747 0.5503 0.4225 0.2674  -0.0850 -0.0030 147 ILE   B CD1 
1330 N  N   . GLY   B 139 ? 0.6611 0.4956 0.4016 0.1904  -0.0440 0.0081  148 GLY   B N   
1331 C  CA  . GLY   B 139 ? 0.6512 0.5040 0.3986 0.1845  -0.0317 0.0146  148 GLY   B CA  
1332 C  C   . GLY   B 139 ? 0.6273 0.4996 0.3875 0.1860  -0.0216 0.0187  148 GLY   B C   
1333 O  O   . GLY   B 139 ? 0.6199 0.4909 0.3808 0.1942  -0.0236 0.0171  148 GLY   B O   
1334 N  N   . LEU   B 140 ? 0.6102 0.4986 0.3793 0.1780  -0.0114 0.0238  149 LEU   B N   
1335 C  CA  . LEU   B 140 ? 0.6023 0.5055 0.3820 0.1774  -0.0018 0.0285  149 LEU   B CA  
1336 C  C   . LEU   B 140 ? 0.6074 0.5278 0.3824 0.1850  0.0036  0.0363  149 LEU   B C   
1337 O  O   . LEU   B 140 ? 0.6063 0.5326 0.3762 0.1852  0.0023  0.0375  149 LEU   B O   
1338 C  CB  . LEU   B 140 ? 0.5893 0.4972 0.3861 0.1596  0.0057  0.0275  149 LEU   B CB  
1339 C  CG  . LEU   B 140 ? 0.6032 0.5016 0.4091 0.1504  0.0033  0.0205  149 LEU   B CG  
1340 C  CD1 . LEU   B 140 ? 0.5968 0.5011 0.4159 0.1361  0.0120  0.0198  149 LEU   B CD1 
1341 C  CD2 . LEU   B 140 ? 0.6080 0.5003 0.4147 0.1596  -0.0017 0.0171  149 LEU   B CD2 
1342 N  N   . TYR   B 141 ? 0.6036 0.5330 0.3804 0.1915  0.0099  0.0421  150 TYR   B N   
1343 C  CA  . TYR   B 141 ? 0.5942 0.5443 0.3701 0.1982  0.0172  0.0512  150 TYR   B CA  
1344 C  C   . TYR   B 141 ? 0.5807 0.5447 0.3748 0.1801  0.0267  0.0556  150 TYR   B C   
1345 O  O   . TYR   B 141 ? 0.5754 0.5297 0.3777 0.1699  0.0297  0.0539  150 TYR   B O   
1346 C  CB  . TYR   B 141 ? 0.5962 0.5446 0.3619 0.2146  0.0193  0.0557  150 TYR   B CB  
1347 C  CG  . TYR   B 141 ? 0.5997 0.5708 0.3680 0.2187  0.0307  0.0675  150 TYR   B CG  
1348 C  CD1 . TYR   B 141 ? 0.6057 0.5807 0.3859 0.2070  0.0407  0.0741  150 TYR   B CD1 
1349 C  CD2 . TYR   B 141 ? 0.6162 0.6045 0.3743 0.2346  0.0317  0.0724  150 TYR   B CD2 
1350 C  CE1 . TYR   B 141 ? 0.6181 0.6142 0.4022 0.2077  0.0521  0.0863  150 TYR   B CE1 
1351 C  CE2 . TYR   B 141 ? 0.6216 0.6352 0.3841 0.2381  0.0436  0.0844  150 TYR   B CE2 
1352 C  CZ  . TYR   B 141 ? 0.6265 0.6442 0.4030 0.2232  0.0541  0.0919  150 TYR   B CZ  
1353 O  OH  . TYR   B 141 ? 0.6283 0.6715 0.4112 0.2234  0.0668  0.1051  150 TYR   B OH  
1354 N  N   . GLY   B 142 ? 0.5762 0.5625 0.3758 0.1773  0.0307  0.0609  151 GLY   B N   
1355 C  CA  . GLY   B 142 ? 0.5902 0.5893 0.4072 0.1591  0.0380  0.0646  151 GLY   B CA  
1356 C  C   . GLY   B 142 ? 0.5984 0.6143 0.4234 0.1495  0.0363  0.0633  151 GLY   B C   
1357 O  O   . GLY   B 142 ? 0.5989 0.6240 0.4381 0.1333  0.0405  0.0649  151 GLY   B O   
1358 N  N   . ASN   B 143 ? 0.6022 0.6198 0.4164 0.1595  0.0291  0.0598  152 ASN   B N   
1359 C  CA  . ASN   B 143 ? 0.6107 0.6461 0.4298 0.1543  0.0265  0.0589  152 ASN   B CA  
1360 C  C   . ASN   B 143 ? 0.6290 0.6828 0.4385 0.1739  0.0238  0.0625  152 ASN   B C   
1361 O  O   . ASN   B 143 ? 0.6422 0.6794 0.4324 0.1888  0.0169  0.0589  152 ASN   B O   
1362 C  CB  . ASN   B 143 ? 0.6256 0.6420 0.4383 0.1463  0.0200  0.0505  152 ASN   B CB  
1363 C  CG  . ASN   B 143 ? 0.6407 0.6749 0.4592 0.1386  0.0177  0.0494  152 ASN   B CG  
1364 O  OD1 . ASN   B 143 ? 0.6449 0.7066 0.4779 0.1339  0.0209  0.0539  152 ASN   B OD1 
1365 N  ND2 . ASN   B 143 ? 0.6325 0.6520 0.4398 0.1367  0.0119  0.0436  152 ASN   B ND2 
1366 N  N   . GLY   B 144 ? 0.6295 0.7174 0.4523 0.1738  0.0293  0.0695  153 GLY   B N   
1367 C  CA  . GLY   B 144 ? 0.6574 0.7689 0.4727 0.1946  0.0282  0.0735  153 GLY   B CA  
1368 C  C   . GLY   B 144 ? 0.6727 0.8287 0.5078 0.1909  0.0325  0.0796  153 GLY   B C   
1369 O  O   . GLY   B 144 ? 0.6647 0.8316 0.5147 0.1738  0.0305  0.0770  153 GLY   B O   
1370 N  N   . VAL   B 145 ? 0.6931 0.8770 0.5279 0.2082  0.0379  0.0872  154 VAL   B N   
1371 C  CA  . VAL   B 145 ? 0.7042 0.9378 0.5589 0.2083  0.0418  0.0933  154 VAL   B CA  
1372 C  C   . VAL   B 145 ? 0.7237 0.9891 0.5879 0.2163  0.0549  0.1059  154 VAL   B C   
1373 O  O   . VAL   B 145 ? 0.7336 0.9796 0.5825 0.2272  0.0597  0.1091  154 VAL   B O   
1374 C  CB  . VAL   B 145 ? 0.7156 0.9573 0.5549 0.2289  0.0313  0.0876  154 VAL   B CB  
1375 C  CG1 . VAL   B 145 ? 0.7254 0.9689 0.5418 0.2607  0.0316  0.0901  154 VAL   B CG1 
1376 C  CG2 . VAL   B 145 ? 0.7041 0.9915 0.5667 0.2218  0.0298  0.0888  154 VAL   B CG2 
1377 N  N   . VAL   B 146 ? 0.7283 1.0437 0.6187 0.2095  0.0610  0.1132  155 VAL   B N   
1378 C  CA  . VAL   B 146 ? 0.7473 1.1002 0.6496 0.2159  0.0752  0.1269  155 VAL   B CA  
1379 C  C   . VAL   B 146 ? 0.7656 1.1601 0.6645 0.2433  0.0741  0.1285  155 VAL   B C   
1380 O  O   . VAL   B 146 ? 0.7547 1.1767 0.6668 0.2414  0.0670  0.1242  155 VAL   B O   
1381 C  CB  . VAL   B 146 ? 0.7413 1.1203 0.6783 0.1849  0.0851  0.1361  155 VAL   B CB  
1382 C  CG1 . VAL   B 146 ? 0.7268 1.1591 0.6815 0.1912  0.0999  0.1513  155 VAL   B CG1 
1383 C  CG2 . VAL   B 146 ? 0.7635 1.0982 0.6957 0.1666  0.0891  0.1371  155 VAL   B CG2 
1384 N  N   . ILE   B 147 ? 0.7924 1.1891 0.6704 0.2714  0.0799  0.1334  156 ILE   B N   
1385 C  CA  . ILE   B 147 ? 0.8123 1.2445 0.6817 0.3023  0.0785  0.1339  156 ILE   B CA  
1386 C  C   . ILE   B 147 ? 0.8034 1.3050 0.7040 0.3013  0.0936  0.1480  156 ILE   B C   
1387 O  O   . ILE   B 147 ? 0.7934 1.3085 0.7188 0.2761  0.1056  0.1581  156 ILE   B O   
1388 C  CB  . ILE   B 147 ? 0.8495 1.2460 0.6763 0.3358  0.0743  0.1297  156 ILE   B CB  
1389 C  CG1 . ILE   B 147 ? 0.8661 1.2488 0.6842 0.3380  0.0866  0.1384  156 ILE   B CG1 
1390 C  CG2 . ILE   B 147 ? 0.8869 1.2249 0.6880 0.3359  0.0571  0.1151  156 ILE   B CG2 
1391 C  CD1 . ILE   B 147 ? 0.9059 1.2544 0.6813 0.3717  0.0810  0.1332  156 ILE   B CD1 
1392 N  N   . LYS   B 148 ? 0.8037 1.3499 0.7040 0.3278  0.0929  0.1488  157 LYS   B N   
1393 C  CA  . LYS   B 148 ? 0.7893 1.4101 0.7226 0.3283  0.1074  0.1621  157 LYS   B CA  
1394 C  C   . LYS   B 148 ? 0.7921 1.4280 0.7360 0.3196  0.1283  0.1788  157 LYS   B C   
1395 O  O   . LYS   B 148 ? 0.7697 1.4567 0.7526 0.2982  0.1404  0.1907  157 LYS   B O   
1396 C  CB  . LYS   B 148 ? 0.8155 1.4776 0.7375 0.3680  0.1055  0.1610  157 LYS   B CB  
1397 C  CG  . LYS   B 148 ? 0.9206 1.5335 0.7944 0.4013  0.0896  0.1473  157 LYS   B CG  
1398 C  CD  . LYS   B 148 ? 0.9899 1.6079 0.8638 0.4062  0.0725  0.1357  157 LYS   B CD  
1399 C  CE  . LYS   B 148 ? 1.0153 1.7093 0.9103 0.4258  0.0761  0.1403  157 LYS   B CE  
1400 N  NZ  . LYS   B 148 ? 1.0471 1.7671 0.9250 0.4620  0.0881  0.1481  157 LYS   B NZ  
1401 N  N   . ASN   B 149 ? 0.8143 1.4066 0.7241 0.3354  0.1322  0.1801  158 ASN   B N   
1402 C  CA  . ASN   B 149 ? 0.8101 1.4123 0.7246 0.3295  0.1520  0.1965  158 ASN   B CA  
1403 C  C   . ASN   B 149 ? 0.8092 1.3742 0.7358 0.2916  0.1552  0.1999  158 ASN   B C   
1404 O  O   . ASN   B 149 ? 0.8174 1.3748 0.7393 0.2877  0.1696  0.2123  158 ASN   B O   
1405 C  CB  . ASN   B 149 ? 0.8560 1.4364 0.7278 0.3676  0.1559  0.1977  158 ASN   B CB  
1406 C  CG  . ASN   B 149 ? 0.9383 1.4429 0.7730 0.3725  0.1431  0.1858  158 ASN   B CG  
1407 O  OD1 . ASN   B 149 ? 0.9674 1.4389 0.7780 0.3879  0.1256  0.1706  158 ASN   B OD1 
1408 N  ND2 . ASN   B 149 ? 0.9639 1.4401 0.7927 0.3602  0.1517  0.1930  158 ASN   B ND2 
1409 N  N   . GLY   B 150 ? 0.7980 1.3397 0.7374 0.2659  0.1419  0.1891  159 GLY   B N   
1410 C  CA  . GLY   B 150 ? 0.7960 1.3025 0.7464 0.2312  0.1429  0.1902  159 GLY   B CA  
1411 C  C   . GLY   B 150 ? 0.8134 1.2505 0.7313 0.2345  0.1358  0.1819  159 GLY   B C   
1412 O  O   . GLY   B 150 ? 0.8285 1.2335 0.7536 0.2078  0.1338  0.1798  159 GLY   B O   
1413 N  N   . SER   B 151 ? 0.8060 1.2193 0.6880 0.2673  0.1310  0.1764  160 SER   B N   
1414 C  CA  A SER   B 151 ? 0.8276 1.1790 0.6799 0.2721  0.1230  0.1678  160 SER   B CA  
1415 C  CA  B SER   B 151 ? 0.8276 1.1789 0.6810 0.2708  0.1233  0.1681  160 SER   B CA  
1416 C  C   . SER   B 151 ? 0.8240 1.1386 0.6741 0.2594  0.1054  0.1513  160 SER   B C   
1417 O  O   . SER   B 151 ? 0.8166 1.1503 0.6794 0.2550  0.0976  0.1452  160 SER   B O   
1418 C  CB  A SER   B 151 ? 0.8617 1.2004 0.6772 0.3101  0.1214  0.1659  160 SER   B CB  
1419 C  CB  B SER   B 151 ? 0.8634 1.2000 0.6799 0.3073  0.1232  0.1675  160 SER   B CB  
1420 O  OG  A SER   B 151 ? 0.9134 1.2038 0.7050 0.3137  0.1193  0.1634  160 SER   B OG  
1421 O  OG  B SER   B 151 ? 0.9057 1.2290 0.7007 0.3300  0.1078  0.1539  160 SER   B OG  
1422 N  N   . TYR   B 152 ? 0.8078 1.0713 0.6414 0.2545  0.0993  0.1444  161 TYR   B N   
1423 C  CA  . TYR   B 152 ? 0.7864 1.0137 0.6167 0.2425  0.0850  0.1301  161 TYR   B CA  
1424 C  C   . TYR   B 152 ? 0.7755 0.9683 0.5746 0.2652  0.0716  0.1183  161 TYR   B C   
1425 O  O   . TYR   B 152 ? 0.7927 0.9633 0.5699 0.2814  0.0716  0.1184  161 TYR   B O   
1426 C  CB  . TYR   B 152 ? 0.7883 0.9856 0.6260 0.2185  0.0879  0.1306  161 TYR   B CB  
1427 C  CG  . TYR   B 152 ? 0.7980 0.9608 0.6339 0.2054  0.0755  0.1170  161 TYR   B CG  
1428 C  CD1 . TYR   B 152 ? 0.7955 0.9693 0.6476 0.1891  0.0698  0.1114  161 TYR   B CD1 
1429 C  CD2 . TYR   B 152 ? 0.8206 0.9419 0.6389 0.2095  0.0696  0.1099  161 TYR   B CD2 
1430 C  CE1 . TYR   B 152 ? 0.8126 0.9558 0.6610 0.1784  0.0600  0.0998  161 TYR   B CE1 
1431 C  CE2 . TYR   B 152 ? 0.8333 0.9273 0.6513 0.1977  0.0599  0.0984  161 TYR   B CE2 
1432 C  CZ  . TYR   B 152 ? 0.8358 0.9403 0.6680 0.1824  0.0559  0.0939  161 TYR   B CZ  
1433 O  OH  . TYR   B 152 ? 0.8554 0.9342 0.6857 0.1718  0.0478  0.0835  161 TYR   B OH  
1434 N  N   . VAL   B 153 ? 0.7471 0.9325 0.5431 0.2652  0.0594  0.1080  162 VAL   B N   
1435 C  CA  . VAL   B 153 ? 0.7403 0.8888 0.5075 0.2822  0.0458  0.0969  162 VAL   B CA  
1436 C  C   . VAL   B 153 ? 0.7207 0.8390 0.4923 0.2612  0.0368  0.0872  162 VAL   B C   
1437 O  O   . VAL   B 153 ? 0.7083 0.8403 0.4948 0.2472  0.0351  0.0855  162 VAL   B O   
1438 C  CB  . VAL   B 153 ? 0.7386 0.9019 0.4883 0.3093  0.0397  0.0948  162 VAL   B CB  
1439 C  CG1 . VAL   B 153 ? 0.7588 0.8774 0.4788 0.3218  0.0240  0.0828  162 VAL   B CG1 
1440 C  CG2 . VAL   B 153 ? 0.7438 0.9336 0.4846 0.3338  0.0493  0.1039  162 VAL   B CG2 
1441 N  N   . SER   B 154 ? 0.7105 0.7908 0.4713 0.2581  0.0320  0.0813  163 SER   B N   
1442 C  CA  . SER   B 154 ? 0.6914 0.7454 0.4569 0.2390  0.0254  0.0729  163 SER   B CA  
1443 C  C   . SER   B 154 ? 0.6895 0.7149 0.4333 0.2490  0.0122  0.0636  163 SER   B C   
1444 O  O   . SER   B 154 ? 0.6949 0.7041 0.4173 0.2682  0.0064  0.0613  163 SER   B O   
1445 C  CB  . SER   B 154 ? 0.6885 0.7214 0.4588 0.2278  0.0285  0.0722  163 SER   B CB  
1446 O  OG  . SER   B 154 ? 0.6832 0.6892 0.4544 0.2144  0.0216  0.0633  163 SER   B OG  
1447 N  N   . ALA   B 155 ? 0.6766 0.6910 0.4244 0.2343  0.0072  0.0581  164 ALA   B N   
1448 C  CA  . ALA   B 155 ? 0.6887 0.6710 0.4166 0.2388  -0.0044 0.0504  164 ALA   B CA  
1449 C  C   . ALA   B 155 ? 0.6938 0.6466 0.4192 0.2330  -0.0076 0.0454  164 ALA   B C   
1450 O  O   . ALA   B 155 ? 0.6844 0.6413 0.4256 0.2218  -0.0009 0.0470  164 ALA   B O   
1451 C  CB  . ALA   B 155 ? 0.6883 0.6682 0.4218 0.2230  -0.0065 0.0475  164 ALA   B CB  
1452 N  N   . ILE   B 156 ? 0.7064 0.6294 0.4118 0.2408  -0.0188 0.0392  165 ILE   B N   
1453 C  CA  . ILE   B 156 ? 0.7117 0.6093 0.4180 0.2326  -0.0237 0.0334  165 ILE   B CA  
1454 C  C   . ILE   B 156 ? 0.6986 0.5871 0.4130 0.2122  -0.0239 0.0307  165 ILE   B C   
1455 O  O   . ILE   B 156 ? 0.6917 0.5621 0.3900 0.2142  -0.0314 0.0284  165 ILE   B O   
1456 C  CB  . ILE   B 156 ? 0.7367 0.6056 0.4180 0.2489  -0.0369 0.0277  165 ILE   B CB  
1457 C  CG1 . ILE   B 156 ? 0.7537 0.6321 0.4209 0.2737  -0.0366 0.0305  165 ILE   B CG1 
1458 C  CG2 . ILE   B 156 ? 0.7485 0.5964 0.4368 0.2367  -0.0426 0.0212  165 ILE   B CG2 
1459 C  CD1 . ILE   B 156 ? 0.7833 0.6309 0.4214 0.2927  -0.0514 0.0235  165 ILE   B CD1 
1460 N  N   . THR   B 157 ? 0.6872 0.5879 0.4238 0.1941  -0.0152 0.0317  166 THR   B N   
1461 C  CA  . THR   B 157 ? 0.6853 0.5808 0.4290 0.1758  -0.0134 0.0296  166 THR   B CA  
1462 C  C   . THR   B 157 ? 0.6904 0.5660 0.4383 0.1648  -0.0164 0.0244  166 THR   B C   
1463 O  O   . THR   B 157 ? 0.6861 0.5663 0.4490 0.1588  -0.0124 0.0228  166 THR   B O   
1464 C  CB  . THR   B 157 ? 0.6829 0.6002 0.4459 0.1630  -0.0034 0.0322  166 THR   B CB  
1465 O  OG1 . THR   B 157 ? 0.6879 0.6284 0.4516 0.1706  -0.0005 0.0374  166 THR   B OG1 
1466 C  CG2 . THR   B 157 ? 0.6883 0.6006 0.4544 0.1476  -0.0017 0.0298  166 THR   B CG2 
1467 N  N   . GLN   B 158 ? 0.6995 0.5539 0.4347 0.1615  -0.0231 0.0221  167 GLN   B N   
1468 C  CA  . GLN   B 158 ? 0.7113 0.5499 0.4527 0.1489  -0.0257 0.0180  167 GLN   B CA  
1469 C  C   . GLN   B 158 ? 0.7410 0.5767 0.4852 0.1323  -0.0203 0.0190  167 GLN   B C   
1470 O  O   . GLN   B 158 ? 0.7419 0.5743 0.4723 0.1340  -0.0203 0.0219  167 GLN   B O   
1471 C  CB  . GLN   B 158 ? 0.7231 0.5352 0.4467 0.1570  -0.0387 0.0147  167 GLN   B CB  
1472 C  CG  . GLN   B 158 ? 0.7269 0.5241 0.4594 0.1433  -0.0435 0.0102  167 GLN   B CG  
1473 C  CD  . GLN   B 158 ? 0.7314 0.5455 0.4878 0.1390  -0.0399 0.0069  167 GLN   B CD  
1474 O  OE1 . GLN   B 158 ? 0.7202 0.5539 0.4937 0.1314  -0.0290 0.0083  167 GLN   B OE1 
1475 N  NE2 . GLN   B 158 ? 0.7221 0.5273 0.4787 0.1444  -0.0499 0.0017  167 GLN   B NE2 
1476 N  N   . GLY   B 159 ? 0.7603 0.5987 0.5216 0.1181  -0.0155 0.0166  168 GLY   B N   
1477 C  CA  . GLY   B 159 ? 0.7967 0.6326 0.5598 0.1032  -0.0093 0.0178  168 GLY   B CA  
1478 C  C   . GLY   B 159 ? 0.8508 0.6630 0.6041 0.0956  -0.0151 0.0182  168 GLY   B C   
1479 O  O   . GLY   B 159 ? 0.8545 0.6503 0.5994 0.1018  -0.0256 0.0163  168 GLY   B O   
1480 N  N   . LYS   B 160 ? 0.8910 0.6999 0.6443 0.0817  -0.0083 0.0207  169 LYS   B N   
1481 C  CA  . LYS   B 160 ? 0.9386 0.7249 0.6840 0.0704  -0.0115 0.0229  169 LYS   B CA  
1482 C  C   . LYS   B 160 ? 0.9549 0.7551 0.7268 0.0548  -0.0050 0.0209  169 LYS   B C   
1483 O  O   . LYS   B 160 ? 0.9421 0.7644 0.7291 0.0510  0.0058  0.0200  169 LYS   B O   
1484 C  CB  . LYS   B 160 ? 0.9890 0.7615 0.7127 0.0665  -0.0072 0.0289  169 LYS   B CB  
1485 C  CG  . LYS   B 160 ? 1.0802 0.8235 0.7901 0.0548  -0.0103 0.0333  169 LYS   B CG  
1486 C  CD  . LYS   B 160 ? 1.1592 0.8993 0.8600 0.0436  0.0009  0.0397  169 LYS   B CD  
1487 C  CE  . LYS   B 160 ? 1.2335 0.9391 0.9148 0.0326  -0.0021 0.0462  169 LYS   B CE  
1488 N  NZ  . LYS   B 160 ? 1.2661 0.9682 0.9364 0.0219  0.0103  0.0538  169 LYS   B NZ  
1489 N  N   . ARG   B 161 ? 0.9795 0.7679 0.7575 0.0465  -0.0122 0.0195  170 ARG   B N   
1490 C  CA  . ARG   B 161 ? 0.9903 0.7960 0.7960 0.0313  -0.0065 0.0177  170 ARG   B CA  
1491 C  C   . ARG   B 161 ? 1.0207 0.8145 0.8212 0.0129  0.0002  0.0248  170 ARG   B C   
1492 O  O   . ARG   B 161 ? 1.0389 0.8040 0.8244 0.0066  -0.0083 0.0277  170 ARG   B O   
1493 C  CB  . ARG   B 161 ? 0.9993 0.8049 0.8198 0.0318  -0.0190 0.0113  170 ARG   B CB  
1494 C  CG  . ARG   B 161 ? 1.0086 0.8405 0.8624 0.0185  -0.0135 0.0085  170 ARG   B CG  
1495 C  CD  . ARG   B 161 ? 1.0384 0.8693 0.9071 0.0157  -0.0277 0.0020  170 ARG   B CD  
1496 N  NE  . ARG   B 161 ? 1.0568 0.9196 0.9604 0.0039  -0.0216 -0.0007 170 ARG   B NE  
1497 C  CZ  . ARG   B 161 ? 1.0815 0.9656 1.0068 0.0109  -0.0275 -0.0086 170 ARG   B CZ  
1498 N  NH1 . ARG   B 161 ? 1.0833 0.9578 0.9976 0.0289  -0.0397 -0.0141 170 ARG   B NH1 
1499 N  NH2 . ARG   B 161 ? 1.0639 0.9801 1.0211 0.0012  -0.0214 -0.0109 170 ARG   B NH2 
1500 N  N   . GLU   B 162 ? 1.0255 0.8385 0.8350 0.0052  0.0155  0.0279  171 GLU   B N   
1501 C  CA  . GLU   B 162 ? 1.0531 0.8580 0.8565 -0.0115 0.0251  0.0360  171 GLU   B CA  
1502 C  C   . GLU   B 162 ? 1.0555 0.8630 0.8804 -0.0305 0.0238  0.0373  171 GLU   B C   
1503 O  O   . GLU   B 162 ? 1.0714 0.8592 0.8855 -0.0456 0.0265  0.0453  171 GLU   B O   
1504 C  CB  . GLU   B 162 ? 1.0893 0.9172 0.8968 -0.0122 0.0420  0.0378  171 GLU   B CB  
1505 C  CG  . GLU   B 162 ? 1.1935 1.0105 0.9729 -0.0002 0.0438  0.0398  171 GLU   B CG  
1506 C  CD  . GLU   B 162 ? 1.3223 1.1110 1.0711 -0.0057 0.0458  0.0490  171 GLU   B CD  
1507 O  OE1 . GLU   B 162 ? 1.3331 1.1244 1.0824 -0.0189 0.0580  0.0554  171 GLU   B OE1 
1508 O  OE2 . GLU   B 162 ? 1.3745 1.1390 1.0979 0.0045  0.0356  0.0502  171 GLU   B OE2 
1509 S  S   . DMS   C .   ? 1.0208 0.8393 0.7928 0.0398  0.0366  -0.0443 201 DMS   B S   
1510 O  O   . DMS   C .   ? 1.0116 0.8471 0.7893 0.0490  0.0440  -0.0401 201 DMS   B O   
1511 C  C1  . DMS   C .   ? 1.0322 0.8209 0.7968 0.0457  0.0389  -0.0496 201 DMS   B C1  
1512 C  C2  . DMS   C .   ? 1.0106 0.8365 0.8013 0.0303  0.0332  -0.0334 201 DMS   B C2  
1513 N  N1  . A1B80 D .   ? 0.7140 0.8660 0.6083 0.1141  0.0500  0.0862  202 A1B80 B N1  
1514 N  N3  . A1B80 D .   ? 0.6722 0.7262 0.5323 0.0747  0.0178  0.0379  202 A1B80 B N3  
1515 C  C4  . A1B80 D .   ? 0.7362 0.9853 0.6943 0.0821  0.0735  0.1166  202 A1B80 B C4  
1516 C  C5  . A1B80 D .   ? 0.7280 0.9886 0.6818 0.0925  0.0625  0.1072  202 A1B80 B C5  
1517 C  C6  . A1B80 D .   ? 0.7294 0.9125 0.6316 0.1228  0.0590  0.0981  202 A1B80 B C6  
1518 C  C7  . A1B80 D .   ? 0.7062 0.8207 0.5855 0.1170  0.0491  0.0816  202 A1B80 B C7  
1519 C  C8  . A1B80 D .   ? 0.6972 0.7909 0.5832 0.0992  0.0545  0.0830  202 A1B80 B C8  
1520 C  C10 . A1B80 D .   ? 0.6683 0.7325 0.5628 0.0615  0.0428  0.0634  202 A1B80 B C10 
1521 C  C13 . A1B80 D .   ? 0.6710 0.7245 0.5397 0.0813  0.0293  0.0496  202 A1B80 B C13 
1522 C  C15 . A1B80 D .   ? 0.6734 0.7180 0.5274 0.0878  0.0221  0.0426  202 A1B80 B C15 
1523 C  C17 . A1B80 D .   ? 0.7058 0.7946 0.5871 0.1076  0.0636  0.0926  202 A1B80 B C17 
1524 C  C20 . A1B80 D .   ? 0.7183 0.8015 0.5846 0.1284  0.0810  0.1125  202 A1B80 B C20 
1525 C  C21 . A1B80 D .   ? 0.7140 0.8221 0.6018 0.1092  0.0828  0.1153  202 A1B80 B C21 
1526 C  C22 . A1B80 D .   ? 0.6979 0.8379 0.6161 0.0806  0.0766  0.1105  202 A1B80 B C22 
1527 C  C24 . A1B80 D .   ? 0.7183 1.0059 0.6915 0.0784  0.0554  0.1030  202 A1B80 B C24 
1528 C  C1  . A1B80 D .   ? 0.7040 1.0082 0.7349 0.0087  0.0738  0.1243  202 A1B80 B C1  
1529 C  C2  . A1B80 D .   ? 0.7150 1.0057 0.7189 0.0395  0.0705  0.1182  202 A1B80 B C2  
1530 C  C3  . A1B80 D .   ? 0.7292 0.9923 0.7114 0.0559  0.0779  0.1226  202 A1B80 B C3  
1531 S  S1  . A1B80 D .   ? 0.7358 0.9710 0.6568 0.1229  0.0558  0.0997  202 A1B80 B S1  
1532 O  O1  . A1B80 D .   ? 0.7567 0.9807 0.6706 0.1217  0.0436  0.0880  202 A1B80 B O1  
1533 O  O2  . A1B80 D .   ? 0.7406 1.0027 0.6565 0.1461  0.0606  0.1070  202 A1B80 B O2  
1534 O  O3  . A1B80 D .   ? 0.7109 0.8090 0.5721 0.1332  0.0443  0.0772  202 A1B80 B O3  
1535 N  N2  . A1B80 D .   ? 0.6960 0.7580 0.5741 0.0927  0.0491  0.0725  202 A1B80 B N2  
1536 C  C9  . A1B80 D .   ? 0.6794 0.7413 0.5608 0.0818  0.0425  0.0643  202 A1B80 B C9  
1537 C  C11 . A1B80 D .   ? 0.6652 0.7262 0.5593 0.0523  0.0354  0.0542  202 A1B80 B C11 
1538 C  C12 . A1B80 D .   ? 0.6670 0.7242 0.5479 0.0630  0.0292  0.0477  202 A1B80 B C12 
1539 C  C14 . A1B80 D .   ? 0.6770 0.7339 0.5460 0.0912  0.0351  0.0573  202 A1B80 B C14 
1540 C  C16 . A1B80 D .   ? 0.6702 0.7217 0.5442 0.0579  0.0216  0.0383  202 A1B80 B C16 
1541 C  C18 . A1B80 D .   ? 0.7117 0.7768 0.5744 0.1243  0.0624  0.0905  202 A1B80 B C18 
1542 C  C19 . A1B80 D .   ? 0.7147 0.7774 0.5703 0.1348  0.0702  0.0996  202 A1B80 B C19 
1543 CL CL1 . A1B80 D .   ? 0.7152 0.7486 0.5475 0.1560  0.0658  0.0949  202 A1B80 B CL1 
1544 N  N4  . A1B80 D .   ? 0.7077 0.8406 0.6128 0.0960  0.0923  0.1273  202 A1B80 B N4  
1545 N  N5  . A1B80 D .   ? 0.6951 0.8490 0.6205 0.0778  0.0881  0.1242  202 A1B80 B N5  
1546 C  C23 . A1B80 D .   ? 0.7072 0.8189 0.6027 0.0994  0.0733  0.1049  202 A1B80 B C23 
1547 C  C25 . A1B80 D .   ? 0.7088 1.0126 0.7079 0.0520  0.0590  0.1080  202 A1B80 B C25 
# 
